data_9J3N
# 
_entry.id   9J3N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9J3N         pdb_00009j3n 10.2210/pdb9j3n/pdb 
WWPDB D_1300049908 ?            ?                   
EMDB  EMD-61120    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1  'Structure model' 1 0 2025-03-19 ? 
2  'EM metadata'     1 0 2025-03-19 ? 
3  FSC               1 0 2025-03-19 ? 
4  'Half map'        1 0 2025-03-19 1 
5  'Half map'        1 0 2025-03-19 2 
6  Image             1 0 2025-03-19 ? 
7  Mask              1 0 2025-03-19 1 
8  'Primary map'     1 0 2025-03-19 ? 
9  'Structure model' 1 1 2025-03-26 ? 
10 'Structure model' 1 2 2025-05-21 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 Mask              repository 'Initial release' ? ? 
8 8 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 9  'Structure model' 'Data collection'     
2 9  'Structure model' 'Database references' 
3 10 'Structure model' 'Data collection'     
4 10 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 9  'Structure model' citation        
2 9  'Structure model' citation_author 
3 9  'Structure model' em_admin        
4 10 'Structure model' citation        
5 10 'Structure model' em_admin        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 9  'Structure model' '_citation.pdbx_database_id_DOI'    
2 9  'Structure model' '_citation.pdbx_database_id_PubMed' 
3 9  'Structure model' '_citation.title'                   
4 9  'Structure model' '_em_admin.last_update'             
5 10 'Structure model' '_citation.journal_volume'          
6 10 'Structure model' '_citation.page_first'              
7 10 'Structure model' '_citation.page_last'               
8 10 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9J3N 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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_database_related.db_name        EMDB 
_pdbx_database_related.details        'ATP bound Chlamydia pneumoniae ATP/ADP translocator NTT1(Inward open state)' 
_pdbx_database_related.db_id          EMD-61120 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 5 
_pdbx_contact_author.email              mrfan@cemps.ac.cn 
_pdbx_contact_author.name_first         Minrui 
_pdbx_contact_author.name_last          Fan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0002-8375-6972 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lin, H.J.'   1 0000-0002-9847-0996 
'Huang, J.'   2 ?                   
'Li, T.M.'    3 0009-0002-1444-1707 
'Li, W.J.'    4 0009-0001-4333-9886 
'Su, N.N.'    5 0000-0002-8737-0412 
'Zhang, J.R.' 6 0009-0004-5131-2992 
'Wu, X.D.'    7 0000-0002-6492-2202 
'Fan, M.R.'   8 0009-0002-8375-6972 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nature 
_citation.journal_id_ASTM           NATUAS 
_citation.journal_id_CSD            0006 
_citation.journal_id_ISSN           1476-4687 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            641 
_citation.language                  ? 
_citation.page_first                797 
_citation.page_last                 804 
_citation.title                     'Structure and mechanism of the plastid/parasite ATP/ADP translocator.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41586-025-08743-3 
_citation.pdbx_database_id_PubMed   40074904 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lin, H.'   1  ?                   
primary 'Huang, J.' 2  ?                   
primary 'Li, T.'    3  ?                   
primary 'Li, W.'    4  ?                   
primary 'Wu, Y.'    5  ?                   
primary 'Yang, T.'  6  ?                   
primary 'Nian, Y.'  7  ?                   
primary 'Lin, X.'   8  ?                   
primary 'Wang, J.'  9  0000-0003-4643-3453 
primary 'Wang, R.'  10 ?                   
primary 'Zhao, X.'  11 ?                   
primary 'Su, N.'    12 0000-0002-8737-0412 
primary 'Zhang, J.' 13 0009-0004-5131-2992 
primary 'Wu, X.'    14 0000-0002-6492-2202 
primary 'Fan, M.'   15 0009-0002-8375-6972 
# 
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 1D10                        13474.846 1 ? ? ? ? 
2 polymer     man 'ADP,ATP carrier protein 1' 65031.344 1 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE" 507.181   1 ? ? ? ? 
# 
_entity_name_com.entity_id   2 
_entity_name_com.name        'ADP/ATP translocase 1' 
# 
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 
;EVQLVESGGGLVQAGGSLRLSCAASGFTFSDTYMGWFRQAPGKEREFVATIDYSGGHTLYADSVKGRFTISRDNSKNTVY
LQMNSLNPEDTAVYYCAARKRYHYYSYWGQGTQVTVSSLEH
;
;EVQLVESGGGLVQAGGSLRLSCAASGFTFSDTYMGWFRQAPGKEREFVATIDYSGGHTLYADSVKGRFTISRDNSKNTVY
LQMNSLNPEDTAVYYCAARKRYHYYSYWGQGTQVTVSSLEH
;
B ? 
2 'polypeptide(L)' no no 
;MTKTEEKPFGKLRSFLWPIHTHELKKVLPMFLMFFCITFNYTVLRDTKDTLIVGAPGSGAEAIPFIKFWLVVPCAIIFML
IYAKLSNILSKQALFYAVGTPFLIFFALFPTVIYPLRDVLHPTEFADRLQAILPPGLLGLVAILRNWTFAAFYVLAELWG
SVMLSLMFWGFANEITKIHEAKRFYALFGIGANISLLASGRAIVWASKLRASVSEGVDPWGISLRLLMAMTIVSGLVLMA
SYWWINKNVLTDPRFYNPEEMQKGKKGAKPKMNMKDSFLYLARSPYILLLALLVIAYGICINLIEVTWKSQLKLQYPNMN
DYSEFMGNFSFWTGVVSVLIMLFVGGNVIRKFGWLTGALVTPVMVLLTGIVFFALVIFRNQASGLVAMFGTTPLMLAVVV
GAIQNILSKSTKYALFDSTKEMAYIPLDQEQKVKGKAAIDVVAARFGKSGGALIQQGLLVICGSIGAMTPYLAVILLFII
AIWLVSATKLNKLFLAQSALKEQEVAQEDSAPASSVDELTSRGRGSGGLNDIFEAQKIEWHEGSGLEVLFQGPDYKDDDD
KWSHPQFEKGGGGSGGSAWSHPQFEK
;
;MTKTEEKPFGKLRSFLWPIHTHELKKVLPMFLMFFCITFNYTVLRDTKDTLIVGAPGSGAEAIPFIKFWLVVPCAIIFML
IYAKLSNILSKQALFYAVGTPFLIFFALFPTVIYPLRDVLHPTEFADRLQAILPPGLLGLVAILRNWTFAAFYVLAELWG
SVMLSLMFWGFANEITKIHEAKRFYALFGIGANISLLASGRAIVWASKLRASVSEGVDPWGISLRLLMAMTIVSGLVLMA
SYWWINKNVLTDPRFYNPEEMQKGKKGAKPKMNMKDSFLYLARSPYILLLALLVIAYGICINLIEVTWKSQLKLQYPNMN
DYSEFMGNFSFWTGVVSVLIMLFVGGNVIRKFGWLTGALVTPVMVLLTGIVFFALVIFRNQASGLVAMFGTTPLMLAVVV
GAIQNILSKSTKYALFDSTKEMAYIPLDQEQKVKGKAAIDVVAARFGKSGGALIQQGLLVICGSIGAMTPYLAVILLFII
AIWLVSATKLNKLFLAQSALKEQEVAQEDSAPASSVDELTSRGRGSGGLNDIFEAQKIEWHEGSGLEVLFQGPDYKDDDD
KWSHPQFEKGGGGSGGSAWSHPQFEK
;
A ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        "ADENOSINE-5'-TRIPHOSPHATE" 
_pdbx_entity_nonpoly.comp_id     ATP 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   VAL n 
1 3   GLN n 
1 4   LEU n 
1 5   VAL n 
1 6   GLU n 
1 7   SER n 
1 8   GLY n 
1 9   GLY n 
1 10  GLY n 
1 11  LEU n 
1 12  VAL n 
1 13  GLN n 
1 14  ALA n 
1 15  GLY n 
1 16  GLY n 
1 17  SER n 
1 18  LEU n 
1 19  ARG n 
1 20  LEU n 
1 21  SER n 
1 22  CYS n 
1 23  ALA n 
1 24  ALA n 
1 25  SER n 
1 26  GLY n 
1 27  PHE n 
1 28  THR n 
1 29  PHE n 
1 30  SER n 
1 31  ASP n 
1 32  THR n 
1 33  TYR n 
1 34  MET n 
1 35  GLY n 
1 36  TRP n 
1 37  PHE n 
1 38  ARG n 
1 39  GLN n 
1 40  ALA n 
1 41  PRO n 
1 42  GLY n 
1 43  LYS n 
1 44  GLU n 
1 45  ARG n 
1 46  GLU n 
1 47  PHE n 
1 48  VAL n 
1 49  ALA n 
1 50  THR n 
1 51  ILE n 
1 52  ASP n 
1 53  TYR n 
1 54  SER n 
1 55  GLY n 
1 56  GLY n 
1 57  HIS n 
1 58  THR n 
1 59  LEU n 
1 60  TYR n 
1 61  ALA n 
1 62  ASP n 
1 63  SER n 
1 64  VAL n 
1 65  LYS n 
1 66  GLY n 
1 67  ARG n 
1 68  PHE n 
1 69  THR n 
1 70  ILE n 
1 71  SER n 
1 72  ARG n 
1 73  ASP n 
1 74  ASN n 
1 75  SER n 
1 76  LYS n 
1 77  ASN n 
1 78  THR n 
1 79  VAL n 
1 80  TYR n 
1 81  LEU n 
1 82  GLN n 
1 83  MET n 
1 84  ASN n 
1 85  SER n 
1 86  LEU n 
1 87  ASN n 
1 88  PRO n 
1 89  GLU n 
1 90  ASP n 
1 91  THR n 
1 92  ALA n 
1 93  VAL n 
1 94  TYR n 
1 95  TYR n 
1 96  CYS n 
1 97  ALA n 
1 98  ALA n 
1 99  ARG n 
1 100 LYS n 
1 101 ARG n 
1 102 TYR n 
1 103 HIS n 
1 104 TYR n 
1 105 TYR n 
1 106 SER n 
1 107 TYR n 
1 108 TRP n 
1 109 GLY n 
1 110 GLN n 
1 111 GLY n 
1 112 THR n 
1 113 GLN n 
1 114 VAL n 
1 115 THR n 
1 116 VAL n 
1 117 SER n 
1 118 SER n 
1 119 LEU n 
1 120 GLU n 
1 121 HIS n 
2 1   MET n 
2 2   THR n 
2 3   LYS n 
2 4   THR n 
2 5   GLU n 
2 6   GLU n 
2 7   LYS n 
2 8   PRO n 
2 9   PHE n 
2 10  GLY n 
2 11  LYS n 
2 12  LEU n 
2 13  ARG n 
2 14  SER n 
2 15  PHE n 
2 16  LEU n 
2 17  TRP n 
2 18  PRO n 
2 19  ILE n 
2 20  HIS n 
2 21  THR n 
2 22  HIS n 
2 23  GLU n 
2 24  LEU n 
2 25  LYS n 
2 26  LYS n 
2 27  VAL n 
2 28  LEU n 
2 29  PRO n 
2 30  MET n 
2 31  PHE n 
2 32  LEU n 
2 33  MET n 
2 34  PHE n 
2 35  PHE n 
2 36  CYS n 
2 37  ILE n 
2 38  THR n 
2 39  PHE n 
2 40  ASN n 
2 41  TYR n 
2 42  THR n 
2 43  VAL n 
2 44  LEU n 
2 45  ARG n 
2 46  ASP n 
2 47  THR n 
2 48  LYS n 
2 49  ASP n 
2 50  THR n 
2 51  LEU n 
2 52  ILE n 
2 53  VAL n 
2 54  GLY n 
2 55  ALA n 
2 56  PRO n 
2 57  GLY n 
2 58  SER n 
2 59  GLY n 
2 60  ALA n 
2 61  GLU n 
2 62  ALA n 
2 63  ILE n 
2 64  PRO n 
2 65  PHE n 
2 66  ILE n 
2 67  LYS n 
2 68  PHE n 
2 69  TRP n 
2 70  LEU n 
2 71  VAL n 
2 72  VAL n 
2 73  PRO n 
2 74  CYS n 
2 75  ALA n 
2 76  ILE n 
2 77  ILE n 
2 78  PHE n 
2 79  MET n 
2 80  LEU n 
2 81  ILE n 
2 82  TYR n 
2 83  ALA n 
2 84  LYS n 
2 85  LEU n 
2 86  SER n 
2 87  ASN n 
2 88  ILE n 
2 89  LEU n 
2 90  SER n 
2 91  LYS n 
2 92  GLN n 
2 93  ALA n 
2 94  LEU n 
2 95  PHE n 
2 96  TYR n 
2 97  ALA n 
2 98  VAL n 
2 99  GLY n 
2 100 THR n 
2 101 PRO n 
2 102 PHE n 
2 103 LEU n 
2 104 ILE n 
2 105 PHE n 
2 106 PHE n 
2 107 ALA n 
2 108 LEU n 
2 109 PHE n 
2 110 PRO n 
2 111 THR n 
2 112 VAL n 
2 113 ILE n 
2 114 TYR n 
2 115 PRO n 
2 116 LEU n 
2 117 ARG n 
2 118 ASP n 
2 119 VAL n 
2 120 LEU n 
2 121 HIS n 
2 122 PRO n 
2 123 THR n 
2 124 GLU n 
2 125 PHE n 
2 126 ALA n 
2 127 ASP n 
2 128 ARG n 
2 129 LEU n 
2 130 GLN n 
2 131 ALA n 
2 132 ILE n 
2 133 LEU n 
2 134 PRO n 
2 135 PRO n 
2 136 GLY n 
2 137 LEU n 
2 138 LEU n 
2 139 GLY n 
2 140 LEU n 
2 141 VAL n 
2 142 ALA n 
2 143 ILE n 
2 144 LEU n 
2 145 ARG n 
2 146 ASN n 
2 147 TRP n 
2 148 THR n 
2 149 PHE n 
2 150 ALA n 
2 151 ALA n 
2 152 PHE n 
2 153 TYR n 
2 154 VAL n 
2 155 LEU n 
2 156 ALA n 
2 157 GLU n 
2 158 LEU n 
2 159 TRP n 
2 160 GLY n 
2 161 SER n 
2 162 VAL n 
2 163 MET n 
2 164 LEU n 
2 165 SER n 
2 166 LEU n 
2 167 MET n 
2 168 PHE n 
2 169 TRP n 
2 170 GLY n 
2 171 PHE n 
2 172 ALA n 
2 173 ASN n 
2 174 GLU n 
2 175 ILE n 
2 176 THR n 
2 177 LYS n 
2 178 ILE n 
2 179 HIS n 
2 180 GLU n 
2 181 ALA n 
2 182 LYS n 
2 183 ARG n 
2 184 PHE n 
2 185 TYR n 
2 186 ALA n 
2 187 LEU n 
2 188 PHE n 
2 189 GLY n 
2 190 ILE n 
2 191 GLY n 
2 192 ALA n 
2 193 ASN n 
2 194 ILE n 
2 195 SER n 
2 196 LEU n 
2 197 LEU n 
2 198 ALA n 
2 199 SER n 
2 200 GLY n 
2 201 ARG n 
2 202 ALA n 
2 203 ILE n 
2 204 VAL n 
2 205 TRP n 
2 206 ALA n 
2 207 SER n 
2 208 LYS n 
2 209 LEU n 
2 210 ARG n 
2 211 ALA n 
2 212 SER n 
2 213 VAL n 
2 214 SER n 
2 215 GLU n 
2 216 GLY n 
2 217 VAL n 
2 218 ASP n 
2 219 PRO n 
2 220 TRP n 
2 221 GLY n 
2 222 ILE n 
2 223 SER n 
2 224 LEU n 
2 225 ARG n 
2 226 LEU n 
2 227 LEU n 
2 228 MET n 
2 229 ALA n 
2 230 MET n 
2 231 THR n 
2 232 ILE n 
2 233 VAL n 
2 234 SER n 
2 235 GLY n 
2 236 LEU n 
2 237 VAL n 
2 238 LEU n 
2 239 MET n 
2 240 ALA n 
2 241 SER n 
2 242 TYR n 
2 243 TRP n 
2 244 TRP n 
2 245 ILE n 
2 246 ASN n 
2 247 LYS n 
2 248 ASN n 
2 249 VAL n 
2 250 LEU n 
2 251 THR n 
2 252 ASP n 
2 253 PRO n 
2 254 ARG n 
2 255 PHE n 
2 256 TYR n 
2 257 ASN n 
2 258 PRO n 
2 259 GLU n 
2 260 GLU n 
2 261 MET n 
2 262 GLN n 
2 263 LYS n 
2 264 GLY n 
2 265 LYS n 
2 266 LYS n 
2 267 GLY n 
2 268 ALA n 
2 269 LYS n 
2 270 PRO n 
2 271 LYS n 
2 272 MET n 
2 273 ASN n 
2 274 MET n 
2 275 LYS n 
2 276 ASP n 
2 277 SER n 
2 278 PHE n 
2 279 LEU n 
2 280 TYR n 
2 281 LEU n 
2 282 ALA n 
2 283 ARG n 
2 284 SER n 
2 285 PRO n 
2 286 TYR n 
2 287 ILE n 
2 288 LEU n 
2 289 LEU n 
2 290 LEU n 
2 291 ALA n 
2 292 LEU n 
2 293 LEU n 
2 294 VAL n 
2 295 ILE n 
2 296 ALA n 
2 297 TYR n 
2 298 GLY n 
2 299 ILE n 
2 300 CYS n 
2 301 ILE n 
2 302 ASN n 
2 303 LEU n 
2 304 ILE n 
2 305 GLU n 
2 306 VAL n 
2 307 THR n 
2 308 TRP n 
2 309 LYS n 
2 310 SER n 
2 311 GLN n 
2 312 LEU n 
2 313 LYS n 
2 314 LEU n 
2 315 GLN n 
2 316 TYR n 
2 317 PRO n 
2 318 ASN n 
2 319 MET n 
2 320 ASN n 
2 321 ASP n 
2 322 TYR n 
2 323 SER n 
2 324 GLU n 
2 325 PHE n 
2 326 MET n 
2 327 GLY n 
2 328 ASN n 
2 329 PHE n 
2 330 SER n 
2 331 PHE n 
2 332 TRP n 
2 333 THR n 
2 334 GLY n 
2 335 VAL n 
2 336 VAL n 
2 337 SER n 
2 338 VAL n 
2 339 LEU n 
2 340 ILE n 
2 341 MET n 
2 342 LEU n 
2 343 PHE n 
2 344 VAL n 
2 345 GLY n 
2 346 GLY n 
2 347 ASN n 
2 348 VAL n 
2 349 ILE n 
2 350 ARG n 
2 351 LYS n 
2 352 PHE n 
2 353 GLY n 
2 354 TRP n 
2 355 LEU n 
2 356 THR n 
2 357 GLY n 
2 358 ALA n 
2 359 LEU n 
2 360 VAL n 
2 361 THR n 
2 362 PRO n 
2 363 VAL n 
2 364 MET n 
2 365 VAL n 
2 366 LEU n 
2 367 LEU n 
2 368 THR n 
2 369 GLY n 
2 370 ILE n 
2 371 VAL n 
2 372 PHE n 
2 373 PHE n 
2 374 ALA n 
2 375 LEU n 
2 376 VAL n 
2 377 ILE n 
2 378 PHE n 
2 379 ARG n 
2 380 ASN n 
2 381 GLN n 
2 382 ALA n 
2 383 SER n 
2 384 GLY n 
2 385 LEU n 
2 386 VAL n 
2 387 ALA n 
2 388 MET n 
2 389 PHE n 
2 390 GLY n 
2 391 THR n 
2 392 THR n 
2 393 PRO n 
2 394 LEU n 
2 395 MET n 
2 396 LEU n 
2 397 ALA n 
2 398 VAL n 
2 399 VAL n 
2 400 VAL n 
2 401 GLY n 
2 402 ALA n 
2 403 ILE n 
2 404 GLN n 
2 405 ASN n 
2 406 ILE n 
2 407 LEU n 
2 408 SER n 
2 409 LYS n 
2 410 SER n 
2 411 THR n 
2 412 LYS n 
2 413 TYR n 
2 414 ALA n 
2 415 LEU n 
2 416 PHE n 
2 417 ASP n 
2 418 SER n 
2 419 THR n 
2 420 LYS n 
2 421 GLU n 
2 422 MET n 
2 423 ALA n 
2 424 TYR n 
2 425 ILE n 
2 426 PRO n 
2 427 LEU n 
2 428 ASP n 
2 429 GLN n 
2 430 GLU n 
2 431 GLN n 
2 432 LYS n 
2 433 VAL n 
2 434 LYS n 
2 435 GLY n 
2 436 LYS n 
2 437 ALA n 
2 438 ALA n 
2 439 ILE n 
2 440 ASP n 
2 441 VAL n 
2 442 VAL n 
2 443 ALA n 
2 444 ALA n 
2 445 ARG n 
2 446 PHE n 
2 447 GLY n 
2 448 LYS n 
2 449 SER n 
2 450 GLY n 
2 451 GLY n 
2 452 ALA n 
2 453 LEU n 
2 454 ILE n 
2 455 GLN n 
2 456 GLN n 
2 457 GLY n 
2 458 LEU n 
2 459 LEU n 
2 460 VAL n 
2 461 ILE n 
2 462 CYS n 
2 463 GLY n 
2 464 SER n 
2 465 ILE n 
2 466 GLY n 
2 467 ALA n 
2 468 MET n 
2 469 THR n 
2 470 PRO n 
2 471 TYR n 
2 472 LEU n 
2 473 ALA n 
2 474 VAL n 
2 475 ILE n 
2 476 LEU n 
2 477 LEU n 
2 478 PHE n 
2 479 ILE n 
2 480 ILE n 
2 481 ALA n 
2 482 ILE n 
2 483 TRP n 
2 484 LEU n 
2 485 VAL n 
2 486 SER n 
2 487 ALA n 
2 488 THR n 
2 489 LYS n 
2 490 LEU n 
2 491 ASN n 
2 492 LYS n 
2 493 LEU n 
2 494 PHE n 
2 495 LEU n 
2 496 ALA n 
2 497 GLN n 
2 498 SER n 
2 499 ALA n 
2 500 LEU n 
2 501 LYS n 
2 502 GLU n 
2 503 GLN n 
2 504 GLU n 
2 505 VAL n 
2 506 ALA n 
2 507 GLN n 
2 508 GLU n 
2 509 ASP n 
2 510 SER n 
2 511 ALA n 
2 512 PRO n 
2 513 ALA n 
2 514 SER n 
2 515 SER n 
2 516 VAL n 
2 517 ASP n 
2 518 GLU n 
2 519 LEU n 
2 520 THR n 
2 521 SER n 
2 522 ARG n 
2 523 GLY n 
2 524 ARG n 
2 525 GLY n 
2 526 SER n 
2 527 GLY n 
2 528 GLY n 
2 529 LEU n 
2 530 ASN n 
2 531 ASP n 
2 532 ILE n 
2 533 PHE n 
2 534 GLU n 
2 535 ALA n 
2 536 GLN n 
2 537 LYS n 
2 538 ILE n 
2 539 GLU n 
2 540 TRP n 
2 541 HIS n 
2 542 GLU n 
2 543 GLY n 
2 544 SER n 
2 545 GLY n 
2 546 LEU n 
2 547 GLU n 
2 548 VAL n 
2 549 LEU n 
2 550 PHE n 
2 551 GLN n 
2 552 GLY n 
2 553 PRO n 
2 554 ASP n 
2 555 TYR n 
2 556 LYS n 
2 557 ASP n 
2 558 ASP n 
2 559 ASP n 
2 560 ASP n 
2 561 LYS n 
2 562 TRP n 
2 563 SER n 
2 564 HIS n 
2 565 PRO n 
2 566 GLN n 
2 567 PHE n 
2 568 GLU n 
2 569 LYS n 
2 570 GLY n 
2 571 GLY n 
2 572 GLY n 
2 573 GLY n 
2 574 SER n 
2 575 GLY n 
2 576 GLY n 
2 577 SER n 
2 578 ALA n 
2 579 TRP n 
2 580 SER n 
2 581 HIS n 
2 582 PRO n 
2 583 GLN n 
2 584 PHE n 
2 585 GLU n 
2 586 LYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 121 ? ? ?                                         ? ? ? ? ? ? 'Vicugna pacos'        30538 ? ? 
? ? ? ? ? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 586 ? ? 'tlcA, adt_1, CPn_0351, CP_0408, CpB0359' ? ? ? ? ? ? 'Chlamydia pneumoniae' 83558 ? ? 
? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
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 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
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   GLU 1   1   1   GLU GLU B . n 
A 1 2   VAL 2   2   2   VAL VAL B . n 
A 1 3   GLN 3   3   3   GLN GLN B . n 
A 1 4   LEU 4   4   4   LEU LEU B . n 
A 1 5   VAL 5   5   5   VAL VAL B . n 
A 1 6   GLU 6   6   6   GLU GLU B . n 
A 1 7   SER 7   7   7   SER SER B . n 
A 1 8   GLY 8   8   8   GLY GLY B . n 
A 1 9   GLY 9   9   9   GLY GLY B . n 
A 1 10  GLY 10  10  10  GLY GLY B . n 
A 1 11  LEU 11  11  11  LEU LEU B . n 
A 1 12  VAL 12  12  12  VAL VAL B . n 
A 1 13  GLN 13  13  13  GLN GLN B . n 
A 1 14  ALA 14  14  14  ALA ALA B . n 
A 1 15  GLY 15  15  15  GLY GLY B . n 
A 1 16  GLY 16  16  16  GLY GLY B . n 
A 1 17  SER 17  17  17  SER SER B . n 
A 1 18  LEU 18  18  18  LEU LEU B . n 
A 1 19  ARG 19  19  19  ARG ARG B . n 
A 1 20  LEU 20  20  20  LEU LEU B . n 
A 1 21  SER 21  21  21  SER SER B . n 
A 1 22  CYS 22  22  22  CYS CYS B . n 
A 1 23  ALA 23  23  23  ALA ALA B . n 
A 1 24  ALA 24  24  24  ALA ALA B . n 
A 1 25  SER 25  25  25  SER SER B . n 
A 1 26  GLY 26  26  26  GLY GLY B . n 
A 1 27  PHE 27  27  27  PHE PHE B . n 
A 1 28  THR 28  28  28  THR THR B . n 
A 1 29  PHE 29  29  29  PHE PHE B . n 
A 1 30  SER 30  30  30  SER SER B . n 
A 1 31  ASP 31  31  31  ASP ASP B . n 
A 1 32  THR 32  32  32  THR THR B . n 
A 1 33  TYR 33  33  33  TYR TYR B . n 
A 1 34  MET 34  34  34  MET MET B . n 
A 1 35  GLY 35  35  35  GLY GLY B . n 
A 1 36  TRP 36  36  36  TRP TRP B . n 
A 1 37  PHE 37  37  37  PHE PHE B . n 
A 1 38  ARG 38  38  38  ARG ARG B . n 
A 1 39  GLN 39  39  39  GLN GLN B . n 
A 1 40  ALA 40  40  40  ALA ALA B . n 
A 1 41  PRO 41  41  41  PRO PRO B . n 
A 1 42  GLY 42  42  42  GLY GLY B . n 
A 1 43  LYS 43  43  43  LYS LYS B . n 
A 1 44  GLU 44  44  44  GLU GLU B . n 
A 1 45  ARG 45  45  45  ARG ARG B . n 
A 1 46  GLU 46  46  46  GLU GLU B . n 
A 1 47  PHE 47  47  47  PHE PHE B . n 
A 1 48  VAL 48  48  48  VAL VAL B . n 
A 1 49  ALA 49  49  49  ALA ALA B . n 
A 1 50  THR 50  50  50  THR THR B . n 
A 1 51  ILE 51  51  51  ILE ILE B . n 
A 1 52  ASP 52  52  52  ASP ASP B . n 
A 1 53  TYR 53  53  53  TYR TYR B . n 
A 1 54  SER 54  54  54  SER SER B . n 
A 1 55  GLY 55  55  55  GLY GLY B . n 
A 1 56  GLY 56  56  56  GLY GLY B . n 
A 1 57  HIS 57  57  57  HIS HIS B . n 
A 1 58  THR 58  58  58  THR THR B . n 
A 1 59  LEU 59  59  59  LEU LEU B . n 
A 1 60  TYR 60  60  60  TYR TYR B . n 
A 1 61  ALA 61  61  61  ALA ALA B . n 
A 1 62  ASP 62  62  62  ASP ASP B . n 
A 1 63  SER 63  63  63  SER SER B . n 
A 1 64  VAL 64  64  64  VAL VAL B . n 
A 1 65  LYS 65  65  65  LYS LYS B . n 
A 1 66  GLY 66  66  66  GLY GLY B . n 
A 1 67  ARG 67  67  67  ARG ARG B . n 
A 1 68  PHE 68  68  68  PHE PHE B . n 
A 1 69  THR 69  69  69  THR THR B . n 
A 1 70  ILE 70  70  70  ILE ILE B . n 
A 1 71  SER 71  71  71  SER SER B . n 
A 1 72  ARG 72  72  72  ARG ARG B . n 
A 1 73  ASP 73  73  73  ASP ASP B . n 
A 1 74  ASN 74  74  74  ASN ASN B . n 
A 1 75  SER 75  75  75  SER SER B . n 
A 1 76  LYS 76  76  76  LYS LYS B . n 
A 1 77  ASN 77  77  77  ASN ASN B . n 
A 1 78  THR 78  78  78  THR THR B . n 
A 1 79  VAL 79  79  79  VAL VAL B . n 
A 1 80  TYR 80  80  80  TYR TYR B . n 
A 1 81  LEU 81  81  81  LEU LEU B . n 
A 1 82  GLN 82  82  82  GLN GLN B . n 
A 1 83  MET 83  83  83  MET MET B . n 
A 1 84  ASN 84  84  84  ASN ASN B . n 
A 1 85  SER 85  85  85  SER SER B . n 
A 1 86  LEU 86  86  86  LEU LEU B . n 
A 1 87  ASN 87  87  87  ASN ASN B . n 
A 1 88  PRO 88  88  88  PRO PRO B . n 
A 1 89  GLU 89  89  89  GLU GLU B . n 
A 1 90  ASP 90  90  90  ASP ASP B . n 
A 1 91  THR 91  91  91  THR THR B . n 
A 1 92  ALA 92  92  92  ALA ALA B . n 
A 1 93  VAL 93  93  93  VAL VAL B . n 
A 1 94  TYR 94  94  94  TYR TYR B . n 
A 1 95  TYR 95  95  95  TYR TYR B . n 
A 1 96  CYS 96  96  96  CYS CYS B . n 
A 1 97  ALA 97  97  97  ALA ALA B . n 
A 1 98  ALA 98  98  98  ALA ALA B . n 
A 1 99  ARG 99  99  99  ARG ARG B . n 
A 1 100 LYS 100 100 100 LYS LYS B . n 
A 1 101 ARG 101 101 101 ARG ARG B . n 
A 1 102 TYR 102 102 102 TYR TYR B . n 
A 1 103 HIS 103 103 103 HIS HIS B . n 
A 1 104 TYR 104 104 104 TYR TYR B . n 
A 1 105 TYR 105 105 105 TYR TYR B . n 
A 1 106 SER 106 106 106 SER SER B . n 
A 1 107 TYR 107 107 107 TYR TYR B . n 
A 1 108 TRP 108 108 108 TRP TRP B . n 
A 1 109 GLY 109 109 109 GLY GLY B . n 
A 1 110 GLN 110 110 110 GLN GLN B . n 
A 1 111 GLY 111 111 111 GLY GLY B . n 
A 1 112 THR 112 112 112 THR THR B . n 
A 1 113 GLN 113 113 113 GLN GLN B . n 
A 1 114 VAL 114 114 114 VAL VAL B . n 
A 1 115 THR 115 115 115 THR THR B . n 
A 1 116 VAL 116 116 116 VAL VAL B . n 
A 1 117 SER 117 117 117 SER SER B . n 
A 1 118 SER 118 118 118 SER SER B . n 
A 1 119 LEU 119 119 119 LEU LEU B . n 
A 1 120 GLU 120 120 120 GLU GLU B . n 
A 1 121 HIS 121 121 121 HIS HIS B . n 
B 2 1   MET 1   1   ?   ?   ?   A . n 
B 2 2   THR 2   2   ?   ?   ?   A . n 
B 2 3   LYS 3   3   ?   ?   ?   A . n 
B 2 4   THR 4   4   ?   ?   ?   A . n 
B 2 5   GLU 5   5   ?   ?   ?   A . n 
B 2 6   GLU 6   6   ?   ?   ?   A . n 
B 2 7   LYS 7   7   ?   ?   ?   A . n 
B 2 8   PRO 8   8   ?   ?   ?   A . n 
B 2 9   PHE 9   9   ?   ?   ?   A . n 
B 2 10  GLY 10  10  ?   ?   ?   A . n 
B 2 11  LYS 11  11  ?   ?   ?   A . n 
B 2 12  LEU 12  12  ?   ?   ?   A . n 
B 2 13  ARG 13  13  ?   ?   ?   A . n 
B 2 14  SER 14  14  ?   ?   ?   A . n 
B 2 15  PHE 15  15  ?   ?   ?   A . n 
B 2 16  LEU 16  16  16  LEU LEU A . n 
B 2 17  TRP 17  17  17  TRP TRP A . n 
B 2 18  PRO 18  18  18  PRO PRO A . n 
B 2 19  ILE 19  19  19  ILE ILE A . n 
B 2 20  HIS 20  20  20  HIS HIS A . n 
B 2 21  THR 21  21  21  THR THR A . n 
B 2 22  HIS 22  22  22  HIS HIS A . n 
B 2 23  GLU 23  23  23  GLU GLU A . n 
B 2 24  LEU 24  24  24  LEU LEU A . n 
B 2 25  LYS 25  25  25  LYS LYS A . n 
B 2 26  LYS 26  26  26  LYS LYS A . n 
B 2 27  VAL 27  27  27  VAL VAL A . n 
B 2 28  LEU 28  28  28  LEU LEU A . n 
B 2 29  PRO 29  29  29  PRO PRO A . n 
B 2 30  MET 30  30  30  MET MET A . n 
B 2 31  PHE 31  31  31  PHE PHE A . n 
B 2 32  LEU 32  32  32  LEU LEU A . n 
B 2 33  MET 33  33  33  MET MET A . n 
B 2 34  PHE 34  34  34  PHE PHE A . n 
B 2 35  PHE 35  35  35  PHE PHE A . n 
B 2 36  CYS 36  36  36  CYS CYS A . n 
B 2 37  ILE 37  37  37  ILE ILE A . n 
B 2 38  THR 38  38  38  THR THR A . n 
B 2 39  PHE 39  39  39  PHE PHE A . n 
B 2 40  ASN 40  40  40  ASN ASN A . n 
B 2 41  TYR 41  41  41  TYR TYR A . n 
B 2 42  THR 42  42  42  THR THR A . n 
B 2 43  VAL 43  43  43  VAL VAL A . n 
B 2 44  LEU 44  44  44  LEU LEU A . n 
B 2 45  ARG 45  45  45  ARG ARG A . n 
B 2 46  ASP 46  46  46  ASP ASP A . n 
B 2 47  THR 47  47  47  THR THR A . n 
B 2 48  LYS 48  48  48  LYS LYS A . n 
B 2 49  ASP 49  49  49  ASP ASP A . n 
B 2 50  THR 50  50  50  THR THR A . n 
B 2 51  LEU 51  51  51  LEU LEU A . n 
B 2 52  ILE 52  52  52  ILE ILE A . n 
B 2 53  VAL 53  53  53  VAL VAL A . n 
B 2 54  GLY 54  54  54  GLY GLY A . n 
B 2 55  ALA 55  55  55  ALA ALA A . n 
B 2 56  PRO 56  56  56  PRO PRO A . n 
B 2 57  GLY 57  57  57  GLY GLY A . n 
B 2 58  SER 58  58  58  SER SER A . n 
B 2 59  GLY 59  59  59  GLY GLY A . n 
B 2 60  ALA 60  60  60  ALA ALA A . n 
B 2 61  GLU 61  61  61  GLU GLU A . n 
B 2 62  ALA 62  62  62  ALA ALA A . n 
B 2 63  ILE 63  63  63  ILE ILE A . n 
B 2 64  PRO 64  64  64  PRO PRO A . n 
B 2 65  PHE 65  65  65  PHE PHE A . n 
B 2 66  ILE 66  66  66  ILE ILE A . n 
B 2 67  LYS 67  67  67  LYS LYS A . n 
B 2 68  PHE 68  68  68  PHE PHE A . n 
B 2 69  TRP 69  69  69  TRP TRP A . n 
B 2 70  LEU 70  70  70  LEU LEU A . n 
B 2 71  VAL 71  71  71  VAL VAL A . n 
B 2 72  VAL 72  72  72  VAL VAL A . n 
B 2 73  PRO 73  73  73  PRO PRO A . n 
B 2 74  CYS 74  74  74  CYS CYS A . n 
B 2 75  ALA 75  75  75  ALA ALA A . n 
B 2 76  ILE 76  76  76  ILE ILE A . n 
B 2 77  ILE 77  77  77  ILE ILE A . n 
B 2 78  PHE 78  78  78  PHE PHE A . n 
B 2 79  MET 79  79  79  MET MET A . n 
B 2 80  LEU 80  80  80  LEU LEU A . n 
B 2 81  ILE 81  81  81  ILE ILE A . n 
B 2 82  TYR 82  82  82  TYR TYR A . n 
B 2 83  ALA 83  83  83  ALA ALA A . n 
B 2 84  LYS 84  84  84  LYS LYS A . n 
B 2 85  LEU 85  85  85  LEU LEU A . n 
B 2 86  SER 86  86  86  SER SER A . n 
B 2 87  ASN 87  87  87  ASN ASN A . n 
B 2 88  ILE 88  88  88  ILE ILE A . n 
B 2 89  LEU 89  89  89  LEU LEU A . n 
B 2 90  SER 90  90  90  SER SER A . n 
B 2 91  LYS 91  91  91  LYS LYS A . n 
B 2 92  GLN 92  92  92  GLN GLN A . n 
B 2 93  ALA 93  93  93  ALA ALA A . n 
B 2 94  LEU 94  94  94  LEU LEU A . n 
B 2 95  PHE 95  95  95  PHE PHE A . n 
B 2 96  TYR 96  96  96  TYR TYR A . n 
B 2 97  ALA 97  97  97  ALA ALA A . n 
B 2 98  VAL 98  98  98  VAL VAL A . n 
B 2 99  GLY 99  99  99  GLY GLY A . n 
B 2 100 THR 100 100 100 THR THR A . n 
B 2 101 PRO 101 101 101 PRO PRO A . n 
B 2 102 PHE 102 102 102 PHE PHE A . n 
B 2 103 LEU 103 103 103 LEU LEU A . n 
B 2 104 ILE 104 104 104 ILE ILE A . n 
B 2 105 PHE 105 105 105 PHE PHE A . n 
B 2 106 PHE 106 106 106 PHE PHE A . n 
B 2 107 ALA 107 107 107 ALA ALA A . n 
B 2 108 LEU 108 108 108 LEU LEU A . n 
B 2 109 PHE 109 109 109 PHE PHE A . n 
B 2 110 PRO 110 110 110 PRO PRO A . n 
B 2 111 THR 111 111 111 THR THR A . n 
B 2 112 VAL 112 112 112 VAL VAL A . n 
B 2 113 ILE 113 113 113 ILE ILE A . n 
B 2 114 TYR 114 114 114 TYR TYR A . n 
B 2 115 PRO 115 115 115 PRO PRO A . n 
B 2 116 LEU 116 116 116 LEU LEU A . n 
B 2 117 ARG 117 117 117 ARG ARG A . n 
B 2 118 ASP 118 118 118 ASP ASP A . n 
B 2 119 VAL 119 119 119 VAL VAL A . n 
B 2 120 LEU 120 120 120 LEU LEU A . n 
B 2 121 HIS 121 121 121 HIS HIS A . n 
B 2 122 PRO 122 122 122 PRO PRO A . n 
B 2 123 THR 123 123 123 THR THR A . n 
B 2 124 GLU 124 124 124 GLU GLU A . n 
B 2 125 PHE 125 125 125 PHE PHE A . n 
B 2 126 ALA 126 126 126 ALA ALA A . n 
B 2 127 ASP 127 127 127 ASP ASP A . n 
B 2 128 ARG 128 128 128 ARG ARG A . n 
B 2 129 LEU 129 129 129 LEU LEU A . n 
B 2 130 GLN 130 130 130 GLN GLN A . n 
B 2 131 ALA 131 131 131 ALA ALA A . n 
B 2 132 ILE 132 132 132 ILE ILE A . n 
B 2 133 LEU 133 133 133 LEU LEU A . n 
B 2 134 PRO 134 134 134 PRO PRO A . n 
B 2 135 PRO 135 135 135 PRO PRO A . n 
B 2 136 GLY 136 136 136 GLY GLY A . n 
B 2 137 LEU 137 137 137 LEU LEU A . n 
B 2 138 LEU 138 138 138 LEU LEU A . n 
B 2 139 GLY 139 139 139 GLY GLY A . n 
B 2 140 LEU 140 140 140 LEU LEU A . n 
B 2 141 VAL 141 141 141 VAL VAL A . n 
B 2 142 ALA 142 142 142 ALA ALA A . n 
B 2 143 ILE 143 143 143 ILE ILE A . n 
B 2 144 LEU 144 144 144 LEU LEU A . n 
B 2 145 ARG 145 145 145 ARG ARG A . n 
B 2 146 ASN 146 146 146 ASN ASN A . n 
B 2 147 TRP 147 147 147 TRP TRP A . n 
B 2 148 THR 148 148 148 THR THR A . n 
B 2 149 PHE 149 149 149 PHE PHE A . n 
B 2 150 ALA 150 150 150 ALA ALA A . n 
B 2 151 ALA 151 151 151 ALA ALA A . n 
B 2 152 PHE 152 152 152 PHE PHE A . n 
B 2 153 TYR 153 153 153 TYR TYR A . n 
B 2 154 VAL 154 154 154 VAL VAL A . n 
B 2 155 LEU 155 155 155 LEU LEU A . n 
B 2 156 ALA 156 156 156 ALA ALA A . n 
B 2 157 GLU 157 157 157 GLU GLU A . n 
B 2 158 LEU 158 158 158 LEU LEU A . n 
B 2 159 TRP 159 159 159 TRP TRP A . n 
B 2 160 GLY 160 160 160 GLY GLY A . n 
B 2 161 SER 161 161 161 SER SER A . n 
B 2 162 VAL 162 162 162 VAL VAL A . n 
B 2 163 MET 163 163 163 MET MET A . n 
B 2 164 LEU 164 164 164 LEU LEU A . n 
B 2 165 SER 165 165 165 SER SER A . n 
B 2 166 LEU 166 166 166 LEU LEU A . n 
B 2 167 MET 167 167 167 MET MET A . n 
B 2 168 PHE 168 168 168 PHE PHE A . n 
B 2 169 TRP 169 169 169 TRP TRP A . n 
B 2 170 GLY 170 170 170 GLY GLY A . n 
B 2 171 PHE 171 171 171 PHE PHE A . n 
B 2 172 ALA 172 172 172 ALA ALA A . n 
B 2 173 ASN 173 173 173 ASN ASN A . n 
B 2 174 GLU 174 174 174 GLU GLU A . n 
B 2 175 ILE 175 175 175 ILE ILE A . n 
B 2 176 THR 176 176 176 THR THR A . n 
B 2 177 LYS 177 177 177 LYS LYS A . n 
B 2 178 ILE 178 178 178 ILE ILE A . n 
B 2 179 HIS 179 179 179 HIS HIS A . n 
B 2 180 GLU 180 180 180 GLU GLU A . n 
B 2 181 ALA 181 181 181 ALA ALA A . n 
B 2 182 LYS 182 182 182 LYS LYS A . n 
B 2 183 ARG 183 183 183 ARG ARG A . n 
B 2 184 PHE 184 184 184 PHE PHE A . n 
B 2 185 TYR 185 185 185 TYR TYR A . n 
B 2 186 ALA 186 186 186 ALA ALA A . n 
B 2 187 LEU 187 187 187 LEU LEU A . n 
B 2 188 PHE 188 188 188 PHE PHE A . n 
B 2 189 GLY 189 189 189 GLY GLY A . n 
B 2 190 ILE 190 190 190 ILE ILE A . n 
B 2 191 GLY 191 191 191 GLY GLY A . n 
B 2 192 ALA 192 192 192 ALA ALA A . n 
B 2 193 ASN 193 193 193 ASN ASN A . n 
B 2 194 ILE 194 194 194 ILE ILE A . n 
B 2 195 SER 195 195 195 SER SER A . n 
B 2 196 LEU 196 196 196 LEU LEU A . n 
B 2 197 LEU 197 197 197 LEU LEU A . n 
B 2 198 ALA 198 198 198 ALA ALA A . n 
B 2 199 SER 199 199 199 SER SER A . n 
B 2 200 GLY 200 200 200 GLY GLY A . n 
B 2 201 ARG 201 201 201 ARG ARG A . n 
B 2 202 ALA 202 202 202 ALA ALA A . n 
B 2 203 ILE 203 203 203 ILE ILE A . n 
B 2 204 VAL 204 204 204 VAL VAL A . n 
B 2 205 TRP 205 205 205 TRP TRP A . n 
B 2 206 ALA 206 206 206 ALA ALA A . n 
B 2 207 SER 207 207 207 SER SER A . n 
B 2 208 LYS 208 208 208 LYS LYS A . n 
B 2 209 LEU 209 209 209 LEU LEU A . n 
B 2 210 ARG 210 210 210 ARG ARG A . n 
B 2 211 ALA 211 211 211 ALA ALA A . n 
B 2 212 SER 212 212 212 SER SER A . n 
B 2 213 VAL 213 213 213 VAL VAL A . n 
B 2 214 SER 214 214 214 SER SER A . n 
B 2 215 GLU 215 215 215 GLU GLU A . n 
B 2 216 GLY 216 216 216 GLY GLY A . n 
B 2 217 VAL 217 217 217 VAL VAL A . n 
B 2 218 ASP 218 218 218 ASP ASP A . n 
B 2 219 PRO 219 219 219 PRO PRO A . n 
B 2 220 TRP 220 220 220 TRP TRP A . n 
B 2 221 GLY 221 221 221 GLY GLY A . n 
B 2 222 ILE 222 222 222 ILE ILE A . n 
B 2 223 SER 223 223 223 SER SER A . n 
B 2 224 LEU 224 224 224 LEU LEU A . n 
B 2 225 ARG 225 225 225 ARG ARG A . n 
B 2 226 LEU 226 226 226 LEU LEU A . n 
B 2 227 LEU 227 227 227 LEU LEU A . n 
B 2 228 MET 228 228 228 MET MET A . n 
B 2 229 ALA 229 229 229 ALA ALA A . n 
B 2 230 MET 230 230 230 MET MET A . n 
B 2 231 THR 231 231 231 THR THR A . n 
B 2 232 ILE 232 232 232 ILE ILE A . n 
B 2 233 VAL 233 233 233 VAL VAL A . n 
B 2 234 SER 234 234 234 SER SER A . n 
B 2 235 GLY 235 235 235 GLY GLY A . n 
B 2 236 LEU 236 236 236 LEU LEU A . n 
B 2 237 VAL 237 237 237 VAL VAL A . n 
B 2 238 LEU 238 238 238 LEU LEU A . n 
B 2 239 MET 239 239 239 MET MET A . n 
B 2 240 ALA 240 240 240 ALA ALA A . n 
B 2 241 SER 241 241 241 SER SER A . n 
B 2 242 TYR 242 242 242 TYR TYR A . n 
B 2 243 TRP 243 243 243 TRP TRP A . n 
B 2 244 TRP 244 244 244 TRP TRP A . n 
B 2 245 ILE 245 245 245 ILE ILE A . n 
B 2 246 ASN 246 246 246 ASN ASN A . n 
B 2 247 LYS 247 247 247 LYS LYS A . n 
B 2 248 ASN 248 248 248 ASN ASN A . n 
B 2 249 VAL 249 249 249 VAL VAL A . n 
B 2 250 LEU 250 250 250 LEU LEU A . n 
B 2 251 THR 251 251 251 THR THR A . n 
B 2 252 ASP 252 252 252 ASP ASP A . n 
B 2 253 PRO 253 253 253 PRO PRO A . n 
B 2 254 ARG 254 254 254 ARG ARG A . n 
B 2 255 PHE 255 255 255 PHE PHE A . n 
B 2 256 TYR 256 256 256 TYR TYR A . n 
B 2 257 ASN 257 257 257 ASN ASN A . n 
B 2 258 PRO 258 258 258 PRO PRO A . n 
B 2 259 GLU 259 259 259 GLU GLU A . n 
B 2 260 GLU 260 260 260 GLU GLU A . n 
B 2 261 MET 261 261 261 MET MET A . n 
B 2 262 GLN 262 262 262 GLN GLN A . n 
B 2 263 LYS 263 263 263 LYS LYS A . n 
B 2 264 GLY 264 264 264 GLY GLY A . n 
B 2 265 LYS 265 265 265 LYS LYS A . n 
B 2 266 LYS 266 266 266 LYS LYS A . n 
B 2 267 GLY 267 267 267 GLY GLY A . n 
B 2 268 ALA 268 268 268 ALA ALA A . n 
B 2 269 LYS 269 269 269 LYS LYS A . n 
B 2 270 PRO 270 270 270 PRO PRO A . n 
B 2 271 LYS 271 271 271 LYS LYS A . n 
B 2 272 MET 272 272 272 MET MET A . n 
B 2 273 ASN 273 273 273 ASN ASN A . n 
B 2 274 MET 274 274 274 MET MET A . n 
B 2 275 LYS 275 275 275 LYS LYS A . n 
B 2 276 ASP 276 276 276 ASP ASP A . n 
B 2 277 SER 277 277 277 SER SER A . n 
B 2 278 PHE 278 278 278 PHE PHE A . n 
B 2 279 LEU 279 279 279 LEU LEU A . n 
B 2 280 TYR 280 280 280 TYR TYR A . n 
B 2 281 LEU 281 281 281 LEU LEU A . n 
B 2 282 ALA 282 282 282 ALA ALA A . n 
B 2 283 ARG 283 283 283 ARG ARG A . n 
B 2 284 SER 284 284 284 SER SER A . n 
B 2 285 PRO 285 285 285 PRO PRO A . n 
B 2 286 TYR 286 286 286 TYR TYR A . n 
B 2 287 ILE 287 287 287 ILE ILE A . n 
B 2 288 LEU 288 288 288 LEU LEU A . n 
B 2 289 LEU 289 289 289 LEU LEU A . n 
B 2 290 LEU 290 290 290 LEU LEU A . n 
B 2 291 ALA 291 291 291 ALA ALA A . n 
B 2 292 LEU 292 292 292 LEU LEU A . n 
B 2 293 LEU 293 293 293 LEU LEU A . n 
B 2 294 VAL 294 294 294 VAL VAL A . n 
B 2 295 ILE 295 295 295 ILE ILE A . n 
B 2 296 ALA 296 296 296 ALA ALA A . n 
B 2 297 TYR 297 297 297 TYR TYR A . n 
B 2 298 GLY 298 298 298 GLY GLY A . n 
B 2 299 ILE 299 299 299 ILE ILE A . n 
B 2 300 CYS 300 300 300 CYS CYS A . n 
B 2 301 ILE 301 301 301 ILE ILE A . n 
B 2 302 ASN 302 302 302 ASN ASN A . n 
B 2 303 LEU 303 303 303 LEU LEU A . n 
B 2 304 ILE 304 304 304 ILE ILE A . n 
B 2 305 GLU 305 305 305 GLU GLU A . n 
B 2 306 VAL 306 306 306 VAL VAL A . n 
B 2 307 THR 307 307 307 THR THR A . n 
B 2 308 TRP 308 308 308 TRP TRP A . n 
B 2 309 LYS 309 309 309 LYS LYS A . n 
B 2 310 SER 310 310 310 SER SER A . n 
B 2 311 GLN 311 311 311 GLN GLN A . n 
B 2 312 LEU 312 312 312 LEU LEU A . n 
B 2 313 LYS 313 313 313 LYS LYS A . n 
B 2 314 LEU 314 314 314 LEU LEU A . n 
B 2 315 GLN 315 315 315 GLN GLN A . n 
B 2 316 TYR 316 316 316 TYR TYR A . n 
B 2 317 PRO 317 317 317 PRO PRO A . n 
B 2 318 ASN 318 318 318 ASN ASN A . n 
B 2 319 MET 319 319 319 MET MET A . n 
B 2 320 ASN 320 320 320 ASN ASN A . n 
B 2 321 ASP 321 321 321 ASP ASP A . n 
B 2 322 TYR 322 322 322 TYR TYR A . n 
B 2 323 SER 323 323 323 SER SER A . n 
B 2 324 GLU 324 324 324 GLU GLU A . n 
B 2 325 PHE 325 325 325 PHE PHE A . n 
B 2 326 MET 326 326 326 MET MET A . n 
B 2 327 GLY 327 327 327 GLY GLY A . n 
B 2 328 ASN 328 328 328 ASN ASN A . n 
B 2 329 PHE 329 329 329 PHE PHE A . n 
B 2 330 SER 330 330 330 SER SER A . n 
B 2 331 PHE 331 331 331 PHE PHE A . n 
B 2 332 TRP 332 332 332 TRP TRP A . n 
B 2 333 THR 333 333 333 THR THR A . n 
B 2 334 GLY 334 334 334 GLY GLY A . n 
B 2 335 VAL 335 335 335 VAL VAL A . n 
B 2 336 VAL 336 336 336 VAL VAL A . n 
B 2 337 SER 337 337 337 SER SER A . n 
B 2 338 VAL 338 338 338 VAL VAL A . n 
B 2 339 LEU 339 339 339 LEU LEU A . n 
B 2 340 ILE 340 340 340 ILE ILE A . n 
B 2 341 MET 341 341 341 MET MET A . n 
B 2 342 LEU 342 342 342 LEU LEU A . n 
B 2 343 PHE 343 343 343 PHE PHE A . n 
B 2 344 VAL 344 344 344 VAL VAL A . n 
B 2 345 GLY 345 345 345 GLY GLY A . n 
B 2 346 GLY 346 346 346 GLY GLY A . n 
B 2 347 ASN 347 347 347 ASN ASN A . n 
B 2 348 VAL 348 348 348 VAL VAL A . n 
B 2 349 ILE 349 349 349 ILE ILE A . n 
B 2 350 ARG 350 350 350 ARG ARG A . n 
B 2 351 LYS 351 351 351 LYS LYS A . n 
B 2 352 PHE 352 352 352 PHE PHE A . n 
B 2 353 GLY 353 353 353 GLY GLY A . n 
B 2 354 TRP 354 354 354 TRP TRP A . n 
B 2 355 LEU 355 355 355 LEU LEU A . n 
B 2 356 THR 356 356 356 THR THR A . n 
B 2 357 GLY 357 357 357 GLY GLY A . n 
B 2 358 ALA 358 358 358 ALA ALA A . n 
B 2 359 LEU 359 359 359 LEU LEU A . n 
B 2 360 VAL 360 360 360 VAL VAL A . n 
B 2 361 THR 361 361 361 THR THR A . n 
B 2 362 PRO 362 362 362 PRO PRO A . n 
B 2 363 VAL 363 363 363 VAL VAL A . n 
B 2 364 MET 364 364 364 MET MET A . n 
B 2 365 VAL 365 365 365 VAL VAL A . n 
B 2 366 LEU 366 366 366 LEU LEU A . n 
B 2 367 LEU 367 367 367 LEU LEU A . n 
B 2 368 THR 368 368 368 THR THR A . n 
B 2 369 GLY 369 369 369 GLY GLY A . n 
B 2 370 ILE 370 370 370 ILE ILE A . n 
B 2 371 VAL 371 371 371 VAL VAL A . n 
B 2 372 PHE 372 372 372 PHE PHE A . n 
B 2 373 PHE 373 373 373 PHE PHE A . n 
B 2 374 ALA 374 374 374 ALA ALA A . n 
B 2 375 LEU 375 375 375 LEU LEU A . n 
B 2 376 VAL 376 376 376 VAL VAL A . n 
B 2 377 ILE 377 377 377 ILE ILE A . n 
B 2 378 PHE 378 378 378 PHE PHE A . n 
B 2 379 ARG 379 379 379 ARG ARG A . n 
B 2 380 ASN 380 380 380 ASN ASN A . n 
B 2 381 GLN 381 381 381 GLN GLN A . n 
B 2 382 ALA 382 382 382 ALA ALA A . n 
B 2 383 SER 383 383 383 SER SER A . n 
B 2 384 GLY 384 384 384 GLY GLY A . n 
B 2 385 LEU 385 385 385 LEU LEU A . n 
B 2 386 VAL 386 386 386 VAL VAL A . n 
B 2 387 ALA 387 387 387 ALA ALA A . n 
B 2 388 MET 388 388 388 MET MET A . n 
B 2 389 PHE 389 389 389 PHE PHE A . n 
B 2 390 GLY 390 390 390 GLY GLY A . n 
B 2 391 THR 391 391 391 THR THR A . n 
B 2 392 THR 392 392 392 THR THR A . n 
B 2 393 PRO 393 393 393 PRO PRO A . n 
B 2 394 LEU 394 394 394 LEU LEU A . n 
B 2 395 MET 395 395 395 MET MET A . n 
B 2 396 LEU 396 396 396 LEU LEU A . n 
B 2 397 ALA 397 397 397 ALA ALA A . n 
B 2 398 VAL 398 398 398 VAL VAL A . n 
B 2 399 VAL 399 399 399 VAL VAL A . n 
B 2 400 VAL 400 400 400 VAL VAL A . n 
B 2 401 GLY 401 401 401 GLY GLY A . n 
B 2 402 ALA 402 402 402 ALA ALA A . n 
B 2 403 ILE 403 403 403 ILE ILE A . n 
B 2 404 GLN 404 404 404 GLN GLN A . n 
B 2 405 ASN 405 405 405 ASN ASN A . n 
B 2 406 ILE 406 406 406 ILE ILE A . n 
B 2 407 LEU 407 407 407 LEU LEU A . n 
B 2 408 SER 408 408 408 SER SER A . n 
B 2 409 LYS 409 409 409 LYS LYS A . n 
B 2 410 SER 410 410 410 SER SER A . n 
B 2 411 THR 411 411 411 THR THR A . n 
B 2 412 LYS 412 412 412 LYS LYS A . n 
B 2 413 TYR 413 413 413 TYR TYR A . n 
B 2 414 ALA 414 414 414 ALA ALA A . n 
B 2 415 LEU 415 415 415 LEU LEU A . n 
B 2 416 PHE 416 416 416 PHE PHE A . n 
B 2 417 ASP 417 417 417 ASP ASP A . n 
B 2 418 SER 418 418 418 SER SER A . n 
B 2 419 THR 419 419 419 THR THR A . n 
B 2 420 LYS 420 420 420 LYS LYS A . n 
B 2 421 GLU 421 421 421 GLU GLU A . n 
B 2 422 MET 422 422 422 MET MET A . n 
B 2 423 ALA 423 423 423 ALA ALA A . n 
B 2 424 TYR 424 424 424 TYR TYR A . n 
B 2 425 ILE 425 425 425 ILE ILE A . n 
B 2 426 PRO 426 426 426 PRO PRO A . n 
B 2 427 LEU 427 427 427 LEU LEU A . n 
B 2 428 ASP 428 428 428 ASP ASP A . n 
B 2 429 GLN 429 429 429 GLN GLN A . n 
B 2 430 GLU 430 430 430 GLU GLU A . n 
B 2 431 GLN 431 431 431 GLN GLN A . n 
B 2 432 LYS 432 432 432 LYS LYS A . n 
B 2 433 VAL 433 433 433 VAL VAL A . n 
B 2 434 LYS 434 434 434 LYS LYS A . n 
B 2 435 GLY 435 435 435 GLY GLY A . n 
B 2 436 LYS 436 436 436 LYS LYS A . n 
B 2 437 ALA 437 437 437 ALA ALA A . n 
B 2 438 ALA 438 438 438 ALA ALA A . n 
B 2 439 ILE 439 439 439 ILE ILE A . n 
B 2 440 ASP 440 440 440 ASP ASP A . n 
B 2 441 VAL 441 441 441 VAL VAL A . n 
B 2 442 VAL 442 442 442 VAL VAL A . n 
B 2 443 ALA 443 443 443 ALA ALA A . n 
B 2 444 ALA 444 444 444 ALA ALA A . n 
B 2 445 ARG 445 445 445 ARG ARG A . n 
B 2 446 PHE 446 446 446 PHE PHE A . n 
B 2 447 GLY 447 447 447 GLY GLY A . n 
B 2 448 LYS 448 448 448 LYS LYS A . n 
B 2 449 SER 449 449 449 SER SER A . n 
B 2 450 GLY 450 450 450 GLY GLY A . n 
B 2 451 GLY 451 451 451 GLY GLY A . n 
B 2 452 ALA 452 452 452 ALA ALA A . n 
B 2 453 LEU 453 453 453 LEU LEU A . n 
B 2 454 ILE 454 454 454 ILE ILE A . n 
B 2 455 GLN 455 455 455 GLN GLN A . n 
B 2 456 GLN 456 456 456 GLN GLN A . n 
B 2 457 GLY 457 457 457 GLY GLY A . n 
B 2 458 LEU 458 458 458 LEU LEU A . n 
B 2 459 LEU 459 459 459 LEU LEU A . n 
B 2 460 VAL 460 460 460 VAL VAL A . n 
B 2 461 ILE 461 461 461 ILE ILE A . n 
B 2 462 CYS 462 462 462 CYS CYS A . n 
B 2 463 GLY 463 463 463 GLY GLY A . n 
B 2 464 SER 464 464 464 SER SER A . n 
B 2 465 ILE 465 465 465 ILE ILE A . n 
B 2 466 GLY 466 466 466 GLY GLY A . n 
B 2 467 ALA 467 467 467 ALA ALA A . n 
B 2 468 MET 468 468 468 MET MET A . n 
B 2 469 THR 469 469 469 THR THR A . n 
B 2 470 PRO 470 470 470 PRO PRO A . n 
B 2 471 TYR 471 471 471 TYR TYR A . n 
B 2 472 LEU 472 472 472 LEU LEU A . n 
B 2 473 ALA 473 473 473 ALA ALA A . n 
B 2 474 VAL 474 474 474 VAL VAL A . n 
B 2 475 ILE 475 475 475 ILE ILE A . n 
B 2 476 LEU 476 476 476 LEU LEU A . n 
B 2 477 LEU 477 477 477 LEU LEU A . n 
B 2 478 PHE 478 478 478 PHE PHE A . n 
B 2 479 ILE 479 479 479 ILE ILE A . n 
B 2 480 ILE 480 480 480 ILE ILE A . n 
B 2 481 ALA 481 481 481 ALA ALA A . n 
B 2 482 ILE 482 482 482 ILE ILE A . n 
B 2 483 TRP 483 483 483 TRP TRP A . n 
B 2 484 LEU 484 484 484 LEU LEU A . n 
B 2 485 VAL 485 485 485 VAL VAL A . n 
B 2 486 SER 486 486 486 SER SER A . n 
B 2 487 ALA 487 487 487 ALA ALA A . n 
B 2 488 THR 488 488 488 THR THR A . n 
B 2 489 LYS 489 489 489 LYS LYS A . n 
B 2 490 LEU 490 490 490 LEU LEU A . n 
B 2 491 ASN 491 491 491 ASN ASN A . n 
B 2 492 LYS 492 492 492 LYS LYS A . n 
B 2 493 LEU 493 493 493 LEU LEU A . n 
B 2 494 PHE 494 494 494 PHE PHE A . n 
B 2 495 LEU 495 495 495 LEU LEU A . n 
B 2 496 ALA 496 496 496 ALA ALA A . n 
B 2 497 GLN 497 497 497 GLN GLN A . n 
B 2 498 SER 498 498 498 SER SER A . n 
B 2 499 ALA 499 499 499 ALA ALA A . n 
B 2 500 LEU 500 500 500 LEU LEU A . n 
B 2 501 LYS 501 501 501 LYS LYS A . n 
B 2 502 GLU 502 502 502 GLU GLU A . n 
B 2 503 GLN 503 503 503 GLN GLN A . n 
B 2 504 GLU 504 504 ?   ?   ?   A . n 
B 2 505 VAL 505 505 ?   ?   ?   A . n 
B 2 506 ALA 506 506 ?   ?   ?   A . n 
B 2 507 GLN 507 507 ?   ?   ?   A . n 
B 2 508 GLU 508 508 ?   ?   ?   A . n 
B 2 509 ASP 509 509 ?   ?   ?   A . n 
B 2 510 SER 510 510 ?   ?   ?   A . n 
B 2 511 ALA 511 511 ?   ?   ?   A . n 
B 2 512 PRO 512 512 ?   ?   ?   A . n 
B 2 513 ALA 513 513 ?   ?   ?   A . n 
B 2 514 SER 514 514 ?   ?   ?   A . n 
B 2 515 SER 515 515 ?   ?   ?   A . n 
B 2 516 VAL 516 516 ?   ?   ?   A . n 
B 2 517 ASP 517 517 ?   ?   ?   A . n 
B 2 518 GLU 518 518 ?   ?   ?   A . n 
B 2 519 LEU 519 519 ?   ?   ?   A . n 
B 2 520 THR 520 520 ?   ?   ?   A . n 
B 2 521 SER 521 521 ?   ?   ?   A . n 
B 2 522 ARG 522 522 ?   ?   ?   A . n 
B 2 523 GLY 523 523 ?   ?   ?   A . n 
B 2 524 ARG 524 524 ?   ?   ?   A . n 
B 2 525 GLY 525 525 ?   ?   ?   A . n 
B 2 526 SER 526 526 ?   ?   ?   A . n 
B 2 527 GLY 527 527 ?   ?   ?   A . n 
B 2 528 GLY 528 528 ?   ?   ?   A . n 
B 2 529 LEU 529 529 ?   ?   ?   A . n 
B 2 530 ASN 530 530 ?   ?   ?   A . n 
B 2 531 ASP 531 531 ?   ?   ?   A . n 
B 2 532 ILE 532 532 ?   ?   ?   A . n 
B 2 533 PHE 533 533 ?   ?   ?   A . n 
B 2 534 GLU 534 534 ?   ?   ?   A . n 
B 2 535 ALA 535 535 ?   ?   ?   A . n 
B 2 536 GLN 536 536 ?   ?   ?   A . n 
B 2 537 LYS 537 537 ?   ?   ?   A . n 
B 2 538 ILE 538 538 ?   ?   ?   A . n 
B 2 539 GLU 539 539 ?   ?   ?   A . n 
B 2 540 TRP 540 540 ?   ?   ?   A . n 
B 2 541 HIS 541 541 ?   ?   ?   A . n 
B 2 542 GLU 542 542 ?   ?   ?   A . n 
B 2 543 GLY 543 543 ?   ?   ?   A . n 
B 2 544 SER 544 544 ?   ?   ?   A . n 
B 2 545 GLY 545 545 ?   ?   ?   A . n 
B 2 546 LEU 546 546 ?   ?   ?   A . n 
B 2 547 GLU 547 547 ?   ?   ?   A . n 
B 2 548 VAL 548 548 ?   ?   ?   A . n 
B 2 549 LEU 549 549 ?   ?   ?   A . n 
B 2 550 PHE 550 550 ?   ?   ?   A . n 
B 2 551 GLN 551 551 ?   ?   ?   A . n 
B 2 552 GLY 552 552 ?   ?   ?   A . n 
B 2 553 PRO 553 553 ?   ?   ?   A . n 
B 2 554 ASP 554 554 ?   ?   ?   A . n 
B 2 555 TYR 555 555 ?   ?   ?   A . n 
B 2 556 LYS 556 556 ?   ?   ?   A . n 
B 2 557 ASP 557 557 ?   ?   ?   A . n 
B 2 558 ASP 558 558 ?   ?   ?   A . n 
B 2 559 ASP 559 559 ?   ?   ?   A . n 
B 2 560 ASP 560 560 ?   ?   ?   A . n 
B 2 561 LYS 561 561 ?   ?   ?   A . n 
B 2 562 TRP 562 562 ?   ?   ?   A . n 
B 2 563 SER 563 563 ?   ?   ?   A . n 
B 2 564 HIS 564 564 ?   ?   ?   A . n 
B 2 565 PRO 565 565 ?   ?   ?   A . n 
B 2 566 GLN 566 566 ?   ?   ?   A . n 
B 2 567 PHE 567 567 ?   ?   ?   A . n 
B 2 568 GLU 568 568 ?   ?   ?   A . n 
B 2 569 LYS 569 569 ?   ?   ?   A . n 
B 2 570 GLY 570 570 ?   ?   ?   A . n 
B 2 571 GLY 571 571 ?   ?   ?   A . n 
B 2 572 GLY 572 572 ?   ?   ?   A . n 
B 2 573 GLY 573 573 ?   ?   ?   A . n 
B 2 574 SER 574 574 ?   ?   ?   A . n 
B 2 575 GLY 575 575 ?   ?   ?   A . n 
B 2 576 GLY 576 576 ?   ?   ?   A . n 
B 2 577 SER 577 577 ?   ?   ?   A . n 
B 2 578 ALA 578 578 ?   ?   ?   A . n 
B 2 579 TRP 579 579 ?   ?   ?   A . n 
B 2 580 SER 580 580 ?   ?   ?   A . n 
B 2 581 HIS 581 581 ?   ?   ?   A . n 
B 2 582 PRO 582 582 ?   ?   ?   A . n 
B 2 583 GLN 583 583 ?   ?   ?   A . n 
B 2 584 PHE 584 584 ?   ?   ?   A . n 
B 2 585 GLU 585 585 ?   ?   ?   A . n 
B 2 586 LYS 586 586 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ATP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ATP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_nonpoly_scheme.asym_id         C 
_pdbx_nonpoly_scheme.entity_id       3 
_pdbx_nonpoly_scheme.mon_id          ATP 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     601 
_pdbx_nonpoly_scheme.auth_seq_num    601 
_pdbx_nonpoly_scheme.pdb_mon_id      ATP 
_pdbx_nonpoly_scheme.auth_mon_id     ATP 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
_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                     9J3N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9J3N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_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                   9J3N 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9J3N 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.004 ? 4934 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.569 ? 6707 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 3.554 ? 2855 ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.040 ? 766  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004 ? 814  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9J3N 
_struct.title                        'ATP bound Chlamydia pneumoniae ATP/ADP translocator NTT1(Inward open state)' 
_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        9J3N 
_struct_keywords.text            'ATP/ADP translocator;non-mitochondrial;antiporter, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
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 PDB 9J3N       9J3N   ? 1 ? 1 
2 UNP TLC1_CHLPN Q9Z8J2 ? 2 
;MTKTEEKPFGKLRSFLWPIHTHELKKVLPMFLMFFCITFNYTVLRDTKDTLIVGAPGSGAEAIPFIKFWLVVPCAIIFML
IYAKLSNILSKQALFYAVGTPFLIFFALFPTVIYPLRDVLHPTEFADRLQAILPPGLLGLVAILRNWTFAAFYVLAELWG
SVMLSLMFWGFANEITKIHEAKRFYALFGIGANISLLASGRAIVWASKLRASVSEGVDPWGISLRLLMAMTIVSGLVLMA
SYWWINKNVLTDPRFYNPEEMQKGKKGAKPKMNMKDSFLYLARSPYILLLALLVIAYGICINLIEVTWKSQLKLQYPNMN
DYSEFMGNFSFWTGVVSVLIMLFVGGNVIRKFGWLTGALVTPVMVLLTGIVFFALVIFRNQASGLVAMFGTTPLMLAVVV
GAIQNILSKSTKYALFDSTKEMAYIPLDQEQKVKGKAAIDVVAARFGKSGGALIQQGLLVICGSIGAMTPYLAVILLFII
AIWLVSATKLNKLFLAQSALKEQEVAQEDSAPASS
;
1 
# 
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 9J3N B 1 ? 121 ? 9J3N   1 ? 121 ? 1 121 
2 2 9J3N A 1 ? 515 ? Q9Z8J2 1 ? 515 ? 1 515 
# 
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 
2 9J3N VAL A 516 ? UNP Q9Z8J2 ? ? 'expression tag' 516 1  
2 9J3N ASP A 517 ? UNP Q9Z8J2 ? ? 'expression tag' 517 2  
2 9J3N GLU A 518 ? UNP Q9Z8J2 ? ? 'expression tag' 518 3  
2 9J3N LEU A 519 ? UNP Q9Z8J2 ? ? 'expression tag' 519 4  
2 9J3N THR A 520 ? UNP Q9Z8J2 ? ? 'expression tag' 520 5  
2 9J3N SER A 521 ? UNP Q9Z8J2 ? ? 'expression tag' 521 6  
2 9J3N ARG A 522 ? UNP Q9Z8J2 ? ? 'expression tag' 522 7  
2 9J3N GLY A 523 ? UNP Q9Z8J2 ? ? 'expression tag' 523 8  
2 9J3N ARG A 524 ? UNP Q9Z8J2 ? ? 'expression tag' 524 9  
2 9J3N GLY A 525 ? UNP Q9Z8J2 ? ? 'expression tag' 525 10 
2 9J3N SER A 526 ? UNP Q9Z8J2 ? ? 'expression tag' 526 11 
2 9J3N GLY A 527 ? UNP Q9Z8J2 ? ? 'expression tag' 527 12 
2 9J3N GLY A 528 ? UNP Q9Z8J2 ? ? 'expression tag' 528 13 
2 9J3N LEU A 529 ? UNP Q9Z8J2 ? ? 'expression tag' 529 14 
2 9J3N ASN A 530 ? UNP Q9Z8J2 ? ? 'expression tag' 530 15 
2 9J3N ASP A 531 ? UNP Q9Z8J2 ? ? 'expression tag' 531 16 
2 9J3N ILE A 532 ? UNP Q9Z8J2 ? ? 'expression tag' 532 17 
2 9J3N PHE A 533 ? UNP Q9Z8J2 ? ? 'expression tag' 533 18 
2 9J3N GLU A 534 ? UNP Q9Z8J2 ? ? 'expression tag' 534 19 
2 9J3N ALA A 535 ? UNP Q9Z8J2 ? ? 'expression tag' 535 20 
2 9J3N GLN A 536 ? UNP Q9Z8J2 ? ? 'expression tag' 536 21 
2 9J3N LYS A 537 ? UNP Q9Z8J2 ? ? 'expression tag' 537 22 
2 9J3N ILE A 538 ? UNP Q9Z8J2 ? ? 'expression tag' 538 23 
2 9J3N GLU A 539 ? UNP Q9Z8J2 ? ? 'expression tag' 539 24 
2 9J3N TRP A 540 ? UNP Q9Z8J2 ? ? 'expression tag' 540 25 
2 9J3N HIS A 541 ? UNP Q9Z8J2 ? ? 'expression tag' 541 26 
2 9J3N GLU A 542 ? UNP Q9Z8J2 ? ? 'expression tag' 542 27 
2 9J3N GLY A 543 ? UNP Q9Z8J2 ? ? 'expression tag' 543 28 
2 9J3N SER A 544 ? UNP Q9Z8J2 ? ? 'expression tag' 544 29 
2 9J3N GLY A 545 ? UNP Q9Z8J2 ? ? 'expression tag' 545 30 
2 9J3N LEU A 546 ? UNP Q9Z8J2 ? ? 'expression tag' 546 31 
2 9J3N GLU A 547 ? UNP Q9Z8J2 ? ? 'expression tag' 547 32 
2 9J3N VAL A 548 ? UNP Q9Z8J2 ? ? 'expression tag' 548 33 
2 9J3N LEU A 549 ? UNP Q9Z8J2 ? ? 'expression tag' 549 34 
2 9J3N PHE A 550 ? UNP Q9Z8J2 ? ? 'expression tag' 550 35 
2 9J3N GLN A 551 ? UNP Q9Z8J2 ? ? 'expression tag' 551 36 
2 9J3N GLY A 552 ? UNP Q9Z8J2 ? ? 'expression tag' 552 37 
2 9J3N PRO A 553 ? UNP Q9Z8J2 ? ? 'expression tag' 553 38 
2 9J3N ASP A 554 ? UNP Q9Z8J2 ? ? 'expression tag' 554 39 
2 9J3N TYR A 555 ? UNP Q9Z8J2 ? ? 'expression tag' 555 40 
2 9J3N LYS A 556 ? UNP Q9Z8J2 ? ? 'expression tag' 556 41 
2 9J3N ASP A 557 ? UNP Q9Z8J2 ? ? 'expression tag' 557 42 
2 9J3N ASP A 558 ? UNP Q9Z8J2 ? ? 'expression tag' 558 43 
2 9J3N ASP A 559 ? UNP Q9Z8J2 ? ? 'expression tag' 559 44 
2 9J3N ASP A 560 ? UNP Q9Z8J2 ? ? 'expression tag' 560 45 
2 9J3N LYS A 561 ? UNP Q9Z8J2 ? ? 'expression tag' 561 46 
2 9J3N TRP A 562 ? UNP Q9Z8J2 ? ? 'expression tag' 562 47 
2 9J3N SER A 563 ? UNP Q9Z8J2 ? ? 'expression tag' 563 48 
2 9J3N HIS A 564 ? UNP Q9Z8J2 ? ? 'expression tag' 564 49 
2 9J3N PRO A 565 ? UNP Q9Z8J2 ? ? 'expression tag' 565 50 
2 9J3N GLN A 566 ? UNP Q9Z8J2 ? ? 'expression tag' 566 51 
2 9J3N PHE A 567 ? UNP Q9Z8J2 ? ? 'expression tag' 567 52 
2 9J3N GLU A 568 ? UNP Q9Z8J2 ? ? 'expression tag' 568 53 
2 9J3N LYS A 569 ? UNP Q9Z8J2 ? ? 'expression tag' 569 54 
2 9J3N GLY A 570 ? UNP Q9Z8J2 ? ? 'expression tag' 570 55 
2 9J3N GLY A 571 ? UNP Q9Z8J2 ? ? 'expression tag' 571 56 
2 9J3N GLY A 572 ? UNP Q9Z8J2 ? ? 'expression tag' 572 57 
2 9J3N GLY A 573 ? UNP Q9Z8J2 ? ? 'expression tag' 573 58 
2 9J3N SER A 574 ? UNP Q9Z8J2 ? ? 'expression tag' 574 59 
2 9J3N GLY A 575 ? UNP Q9Z8J2 ? ? 'expression tag' 575 60 
2 9J3N GLY A 576 ? UNP Q9Z8J2 ? ? 'expression tag' 576 61 
2 9J3N SER A 577 ? UNP Q9Z8J2 ? ? 'expression tag' 577 62 
2 9J3N ALA A 578 ? UNP Q9Z8J2 ? ? 'expression tag' 578 63 
2 9J3N TRP A 579 ? UNP Q9Z8J2 ? ? 'expression tag' 579 64 
2 9J3N SER A 580 ? UNP Q9Z8J2 ? ? 'expression tag' 580 65 
2 9J3N HIS A 581 ? UNP Q9Z8J2 ? ? 'expression tag' 581 66 
2 9J3N PRO A 582 ? UNP Q9Z8J2 ? ? 'expression tag' 582 67 
2 9J3N GLN A 583 ? UNP Q9Z8J2 ? ? 'expression tag' 583 68 
2 9J3N PHE A 584 ? UNP Q9Z8J2 ? ? 'expression tag' 584 69 
2 9J3N GLU A 585 ? UNP Q9Z8J2 ? ? 'expression tag' 585 70 
2 9J3N LYS A 586 ? UNP Q9Z8J2 ? ? 'expression tag' 586 71 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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   ? 
_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 THR A 28  ? SER A 30  ? THR B 28  SER B 30  5 ? 3  
HELX_P HELX_P2  AA2 ASN A 87  ? THR A 91  ? ASN B 87  THR B 91  5 ? 5  
HELX_P HELX_P3  AA3 GLU B 23  ? GLY B 54  ? GLU A 23  GLY A 54  1 ? 32 
HELX_P HELX_P4  AA4 GLU B 61  ? LEU B 70  ? GLU A 61  LEU A 70  1 ? 10 
HELX_P HELX_P5  AA5 LEU B 70  ? SER B 86  ? LEU A 70  SER A 86  1 ? 17 
HELX_P HELX_P6  AA6 SER B 90  ? VAL B 112 ? SER A 90  VAL A 112 1 ? 23 
HELX_P HELX_P7  AA7 LEU B 116 ? HIS B 121 ? LEU A 116 HIS A 121 1 ? 6  
HELX_P HELX_P8  AA8 PRO B 122 ? ALA B 131 ? PRO A 122 ALA A 131 1 ? 10 
HELX_P HELX_P9  AA9 PRO B 134 ? GLY B 136 ? PRO A 134 GLY A 136 5 ? 3  
HELX_P HELX_P10 AB1 LEU B 137 ? ASN B 146 ? LEU A 137 ASN A 146 1 ? 10 
HELX_P HELX_P11 AB2 ASN B 146 ? LEU B 166 ? ASN A 146 LEU A 166 1 ? 21 
HELX_P HELX_P12 AB3 LEU B 166 ? THR B 176 ? LEU A 166 THR A 176 1 ? 11 
HELX_P HELX_P13 AB4 LYS B 177 ? LEU B 209 ? LYS A 177 LEU A 209 1 ? 33 
HELX_P HELX_P14 AB5 ASP B 218 ? VAL B 249 ? ASP A 218 VAL A 249 1 ? 32 
HELX_P HELX_P15 AB6 MET B 261 ? LYS B 266 ? MET A 261 LYS A 266 1 ? 6  
HELX_P HELX_P16 AB7 MET B 274 ? LEU B 279 ? MET A 274 LEU A 279 1 ? 6  
HELX_P HELX_P17 AB8 TYR B 280 ? ARG B 283 ? TYR A 280 ARG A 283 5 ? 4  
HELX_P HELX_P18 AB9 SER B 284 ? TYR B 316 ? SER A 284 TYR A 316 1 ? 33 
HELX_P HELX_P19 AC1 ASN B 318 ? VAL B 344 ? ASN A 318 VAL A 344 1 ? 27 
HELX_P HELX_P20 AC2 GLY B 346 ? PHE B 378 ? GLY A 346 PHE A 378 1 ? 33 
HELX_P HELX_P21 AC3 PHE B 378 ? SER B 383 ? PHE A 378 SER A 383 1 ? 6  
HELX_P HELX_P22 AC4 VAL B 386 ? GLY B 390 ? VAL A 386 GLY A 390 5 ? 5  
HELX_P HELX_P23 AC5 THR B 392 ? THR B 411 ? THR A 392 THR A 411 1 ? 20 
HELX_P HELX_P24 AC6 PHE B 416 ? TYR B 424 ? PHE A 416 TYR A 424 1 ? 9  
HELX_P HELX_P25 AC7 ASP B 428 ? GLY B 463 ? ASP A 428 GLY A 463 1 ? 36 
HELX_P HELX_P26 AC8 SER B 464 ? GLN B 503 ? SER A 464 GLN A 503 1 ? 40 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            22 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           A 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            96 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             22 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             96 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.029 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       22 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      96 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        22 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       96 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY A 10  ? LEU A 11  ? GLY B 10  LEU B 11  
AA1 2 THR A 112 ? THR A 115 ? THR B 112 THR B 115 
AA1 3 ALA A 92  ? LYS A 100 ? ALA B 92  LYS B 100 
AA1 4 THR A 32  ? GLN A 39  ? THR B 32  GLN B 39  
AA1 5 GLU A 46  ? ILE A 51  ? GLU B 46  ILE B 51  
AA1 6 THR A 58  ? TYR A 60  ? THR B 58  TYR B 60  
AA2 1 GLY A 10  ? LEU A 11  ? GLY B 10  LEU B 11  
AA2 2 THR A 112 ? THR A 115 ? THR B 112 THR B 115 
AA2 3 ALA A 92  ? LYS A 100 ? ALA B 92  LYS B 100 
AA2 4 TYR A 107 ? TRP A 108 ? TYR B 107 TRP B 108 
AA3 1 SER A 17  ? LEU A 20  ? SER B 17  LEU B 20  
AA3 2 THR A 78  ? ASN A 84  ? THR B 78  ASN B 84  
AA3 3 THR A 69  ? ASP A 73  ? THR B 69  ASP B 73  
# 
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 GLY A 10  ? N GLY B 10  O THR A 115 ? O THR B 115 
AA1 2 3 O VAL A 114 ? O VAL B 114 N ALA A 92  ? N ALA B 92  
AA1 3 4 O ARG A 99  ? O ARG B 99  N TYR A 33  ? N TYR B 33  
AA1 4 5 N TRP A 36  ? N TRP B 36  O VAL A 48  ? O VAL B 48  
AA1 5 6 N THR A 50  ? N THR B 50  O LEU A 59  ? O LEU B 59  
AA2 1 2 N GLY A 10  ? N GLY B 10  O THR A 115 ? O THR B 115 
AA2 2 3 O VAL A 114 ? O VAL B 114 N ALA A 92  ? N ALA B 92  
AA2 3 4 N ALA A 98  ? N ALA B 98  O TYR A 107 ? O TYR B 107 
AA3 1 2 N LEU A 18  ? N LEU B 18  O MET A 83  ? O MET B 83  
AA3 2 3 O TYR A 80  ? O TYR B 80  N SER A 71  ? N SER B 71  
# 
_pdbx_entry_details.entry_id                   9J3N 
_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   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 VAL B 12  ? ? -123.30 -69.16  
2  1 GLN B 13  ? ? 177.69  174.62  
3  1 ALA B 23  ? ? -69.35  82.23   
4  1 ASP B 52  ? ? -65.39  -77.90  
5  1 TYR B 53  ? ? -145.33 -18.83  
6  1 SER B 54  ? ? -143.44 -0.79   
7  1 THR B 78  ? ? -174.28 135.76  
8  1 SER B 118 ? ? -37.67  126.51  
9  1 GLU B 120 ? ? 56.37   18.94   
10 1 TRP A 17  ? ? -158.98 62.31   
11 1 LEU A 209 ? ? -85.70  33.36   
12 1 ARG A 210 ? ? -68.73  72.44   
13 1 ALA A 211 ? ? -111.11 -169.91 
14 1 SER A 212 ? ? 60.05   65.43   
15 1 PRO A 253 ? ? -68.47  3.64    
16 1 PRO A 258 ? ? -63.98  5.52    
17 1 LYS A 269 ? ? -50.45  108.77  
18 1 ASN A 273 ? ? -64.47  -79.61  
19 1 MET A 274 ? ? -140.17 -41.87  
20 1 PHE A 378 ? ? -93.85  57.89   
21 1 THR A 411 ? ? -91.86  46.67   
22 1 PRO A 426 ? ? -67.95  1.89    
23 1 VAL A 442 ? ? -91.08  -61.43  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9J3N 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9J3N 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.72 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               119152 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.4 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               'MULTIPLE SOURCES' 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Chlamydia pneumoniae ATP/ADP translocator NTT1(Inward open state)' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2' 
# 
_em_imaging.entry_id                        9J3N 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            DIFFRACTION 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1100 
_em_imaging.nominal_defocus_max             2200 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           130000 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9J3N 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          NITROGEN 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9J3N 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? B MET 1   
2  1 Y 1 A THR 2   ? B THR 2   
3  1 Y 1 A LYS 3   ? B LYS 3   
4  1 Y 1 A THR 4   ? B THR 4   
5  1 Y 1 A GLU 5   ? B GLU 5   
6  1 Y 1 A GLU 6   ? B GLU 6   
7  1 Y 1 A LYS 7   ? B LYS 7   
8  1 Y 1 A PRO 8   ? B PRO 8   
9  1 Y 1 A PHE 9   ? B PHE 9   
10 1 Y 1 A GLY 10  ? B GLY 10  
11 1 Y 1 A LYS 11  ? B LYS 11  
12 1 Y 1 A LEU 12  ? B LEU 12  
13 1 Y 1 A ARG 13  ? B ARG 13  
14 1 Y 1 A SER 14  ? B SER 14  
15 1 Y 1 A PHE 15  ? B PHE 15  
16 1 Y 1 A GLU 504 ? B GLU 504 
17 1 Y 1 A VAL 505 ? B VAL 505 
18 1 Y 1 A ALA 506 ? B ALA 506 
19 1 Y 1 A GLN 507 ? B GLN 507 
20 1 Y 1 A GLU 508 ? B GLU 508 
21 1 Y 1 A ASP 509 ? B ASP 509 
22 1 Y 1 A SER 510 ? B SER 510 
23 1 Y 1 A ALA 511 ? B ALA 511 
24 1 Y 1 A PRO 512 ? B PRO 512 
25 1 Y 1 A ALA 513 ? B ALA 513 
26 1 Y 1 A SER 514 ? B SER 514 
27 1 Y 1 A SER 515 ? B SER 515 
28 1 Y 1 A VAL 516 ? B VAL 516 
29 1 Y 1 A ASP 517 ? B ASP 517 
30 1 Y 1 A GLU 518 ? B GLU 518 
31 1 Y 1 A LEU 519 ? B LEU 519 
32 1 Y 1 A THR 520 ? B THR 520 
33 1 Y 1 A SER 521 ? B SER 521 
34 1 Y 1 A ARG 522 ? B ARG 522 
35 1 Y 1 A GLY 523 ? B GLY 523 
36 1 Y 1 A ARG 524 ? B ARG 524 
37 1 Y 1 A GLY 525 ? B GLY 525 
38 1 Y 1 A SER 526 ? B SER 526 
39 1 Y 1 A GLY 527 ? B GLY 527 
40 1 Y 1 A GLY 528 ? B GLY 528 
41 1 Y 1 A LEU 529 ? B LEU 529 
42 1 Y 1 A ASN 530 ? B ASN 530 
43 1 Y 1 A ASP 531 ? B ASP 531 
44 1 Y 1 A ILE 532 ? B ILE 532 
45 1 Y 1 A PHE 533 ? B PHE 533 
46 1 Y 1 A GLU 534 ? B GLU 534 
47 1 Y 1 A ALA 535 ? B ALA 535 
48 1 Y 1 A GLN 536 ? B GLN 536 
49 1 Y 1 A LYS 537 ? B LYS 537 
50 1 Y 1 A ILE 538 ? B ILE 538 
51 1 Y 1 A GLU 539 ? B GLU 539 
52 1 Y 1 A TRP 540 ? B TRP 540 
53 1 Y 1 A HIS 541 ? B HIS 541 
54 1 Y 1 A GLU 542 ? B GLU 542 
55 1 Y 1 A GLY 543 ? B GLY 543 
56 1 Y 1 A SER 544 ? B SER 544 
57 1 Y 1 A GLY 545 ? B GLY 545 
58 1 Y 1 A LEU 546 ? B LEU 546 
59 1 Y 1 A GLU 547 ? B GLU 547 
60 1 Y 1 A VAL 548 ? B VAL 548 
61 1 Y 1 A LEU 549 ? B LEU 549 
62 1 Y 1 A PHE 550 ? B PHE 550 
63 1 Y 1 A GLN 551 ? B GLN 551 
64 1 Y 1 A GLY 552 ? B GLY 552 
65 1 Y 1 A PRO 553 ? B PRO 553 
66 1 Y 1 A ASP 554 ? B ASP 554 
67 1 Y 1 A TYR 555 ? B TYR 555 
68 1 Y 1 A LYS 556 ? B LYS 556 
69 1 Y 1 A ASP 557 ? B ASP 557 
70 1 Y 1 A ASP 558 ? B ASP 558 
71 1 Y 1 A ASP 559 ? B ASP 559 
72 1 Y 1 A ASP 560 ? B ASP 560 
73 1 Y 1 A LYS 561 ? B LYS 561 
74 1 Y 1 A TRP 562 ? B TRP 562 
75 1 Y 1 A SER 563 ? B SER 563 
76 1 Y 1 A HIS 564 ? B HIS 564 
77 1 Y 1 A PRO 565 ? B PRO 565 
78 1 Y 1 A GLN 566 ? B GLN 566 
79 1 Y 1 A PHE 567 ? B PHE 567 
80 1 Y 1 A GLU 568 ? B GLU 568 
81 1 Y 1 A LYS 569 ? B LYS 569 
82 1 Y 1 A GLY 570 ? B GLY 570 
83 1 Y 1 A GLY 571 ? B GLY 571 
84 1 Y 1 A GLY 572 ? B GLY 572 
85 1 Y 1 A GLY 573 ? B GLY 573 
86 1 Y 1 A SER 574 ? B SER 574 
87 1 Y 1 A GLY 575 ? B GLY 575 
88 1 Y 1 A GLY 576 ? B GLY 576 
89 1 Y 1 A SER 577 ? B SER 577 
90 1 Y 1 A ALA 578 ? B ALA 578 
91 1 Y 1 A TRP 579 ? B TRP 579 
92 1 Y 1 A SER 580 ? B SER 580 
93 1 Y 1 A HIS 581 ? B HIS 581 
94 1 Y 1 A PRO 582 ? B PRO 582 
95 1 Y 1 A GLN 583 ? B GLN 583 
96 1 Y 1 A PHE 584 ? B PHE 584 
97 1 Y 1 A GLU 585 ? B GLU 585 
98 1 Y 1 A LYS 586 ? B LYS 586 
# 
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 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
ATP PG     P N N 74  
ATP O1G    O N N 75  
ATP O2G    O N N 76  
ATP O3G    O N N 77  
ATP PB     P N R 78  
ATP O1B    O N N 79  
ATP O2B    O N N 80  
ATP O3B    O N N 81  
ATP PA     P N R 82  
ATP O1A    O N N 83  
ATP O2A    O N N 84  
ATP O3A    O N N 85  
ATP "O5'"  O N N 86  
ATP "C5'"  C N N 87  
ATP "C4'"  C N R 88  
ATP "O4'"  O N N 89  
ATP "C3'"  C N S 90  
ATP "O3'"  O N N 91  
ATP "C2'"  C N R 92  
ATP "O2'"  O N N 93  
ATP "C1'"  C N R 94  
ATP N9     N Y N 95  
ATP C8     C Y N 96  
ATP N7     N Y N 97  
ATP C5     C Y N 98  
ATP C6     C Y N 99  
ATP N6     N N N 100 
ATP N1     N Y N 101 
ATP C2     C Y N 102 
ATP N3     N Y N 103 
ATP C4     C Y N 104 
ATP HOG2   H N N 105 
ATP HOG3   H N N 106 
ATP HOB2   H N N 107 
ATP HOA2   H N N 108 
ATP "H5'1" H N N 109 
ATP "H5'2" H N N 110 
ATP "H4'"  H N N 111 
ATP "H3'"  H N N 112 
ATP "HO3'" H N N 113 
ATP "H2'"  H N N 114 
ATP "HO2'" H N N 115 
ATP "H1'"  H N N 116 
ATP H8     H N N 117 
ATP HN61   H N N 118 
ATP HN62   H N N 119 
ATP H2     H N N 120 
CYS N      N N N 121 
CYS CA     C N R 122 
CYS C      C N N 123 
CYS O      O N N 124 
CYS CB     C N N 125 
CYS SG     S N N 126 
CYS OXT    O N N 127 
CYS H      H N N 128 
CYS H2     H N N 129 
CYS HA     H N N 130 
CYS HB2    H N N 131 
CYS HB3    H N N 132 
CYS HG     H N N 133 
CYS HXT    H N N 134 
GLN N      N N N 135 
GLN CA     C N S 136 
GLN C      C N N 137 
GLN O      O N N 138 
GLN CB     C N N 139 
GLN CG     C N N 140 
GLN CD     C N N 141 
GLN OE1    O N N 142 
GLN NE2    N N N 143 
GLN OXT    O N N 144 
GLN H      H N N 145 
GLN H2     H N N 146 
GLN HA     H N N 147 
GLN HB2    H N N 148 
GLN HB3    H N N 149 
GLN HG2    H N N 150 
GLN HG3    H N N 151 
GLN HE21   H N N 152 
GLN HE22   H N N 153 
GLN HXT    H N N 154 
GLU N      N N N 155 
GLU CA     C N S 156 
GLU C      C N N 157 
GLU O      O N N 158 
GLU CB     C N N 159 
GLU CG     C N N 160 
GLU CD     C N N 161 
GLU OE1    O N N 162 
GLU OE2    O N N 163 
GLU OXT    O N N 164 
GLU H      H N N 165 
GLU H2     H N N 166 
GLU HA     H N N 167 
GLU HB2    H N N 168 
GLU HB3    H N N 169 
GLU HG2    H N N 170 
GLU HG3    H N N 171 
GLU HE2    H N N 172 
GLU HXT    H N N 173 
GLY N      N N N 174 
GLY CA     C N N 175 
GLY C      C N N 176 
GLY O      O N N 177 
GLY OXT    O N N 178 
GLY H      H N N 179 
GLY H2     H N N 180 
GLY HA2    H N N 181 
GLY HA3    H N N 182 
GLY HXT    H N N 183 
HIS N      N N N 184 
HIS CA     C N S 185 
HIS C      C N N 186 
HIS O      O N N 187 
HIS CB     C N N 188 
HIS CG     C Y N 189 
HIS ND1    N Y N 190 
HIS CD2    C Y N 191 
HIS CE1    C Y N 192 
HIS NE2    N Y N 193 
HIS OXT    O N N 194 
HIS H      H N N 195 
HIS H2     H N N 196 
HIS HA     H N N 197 
HIS HB2    H N N 198 
HIS HB3    H N N 199 
HIS HD1    H N N 200 
HIS HD2    H N N 201 
HIS HE1    H N N 202 
HIS HE2    H N N 203 
HIS HXT    H N N 204 
ILE N      N N N 205 
ILE CA     C N S 206 
ILE C      C N N 207 
ILE O      O N N 208 
ILE CB     C N S 209 
ILE CG1    C N N 210 
ILE CG2    C N N 211 
ILE CD1    C N N 212 
ILE OXT    O N N 213 
ILE H      H N N 214 
ILE H2     H N N 215 
ILE HA     H N N 216 
ILE HB     H N N 217 
ILE HG12   H N N 218 
ILE HG13   H N N 219 
ILE HG21   H N N 220 
ILE HG22   H N N 221 
ILE HG23   H N N 222 
ILE HD11   H N N 223 
ILE HD12   H N N 224 
ILE HD13   H N N 225 
ILE HXT    H N N 226 
LEU N      N N N 227 
LEU CA     C N S 228 
LEU C      C N N 229 
LEU O      O N N 230 
LEU CB     C N N 231 
LEU CG     C N N 232 
LEU CD1    C N N 233 
LEU CD2    C N N 234 
LEU OXT    O N N 235 
LEU H      H N N 236 
LEU H2     H N N 237 
LEU HA     H N N 238 
LEU HB2    H N N 239 
LEU HB3    H N N 240 
LEU HG     H N N 241 
LEU HD11   H N N 242 
LEU HD12   H N N 243 
LEU HD13   H N N 244 
LEU HD21   H N N 245 
LEU HD22   H N N 246 
LEU HD23   H N N 247 
LEU HXT    H N N 248 
LYS N      N N N 249 
LYS CA     C N S 250 
LYS C      C N N 251 
LYS O      O N N 252 
LYS CB     C N N 253 
LYS CG     C N N 254 
LYS CD     C N N 255 
LYS CE     C N N 256 
LYS NZ     N N N 257 
LYS OXT    O N N 258 
LYS H      H N N 259 
LYS H2     H N N 260 
LYS HA     H N N 261 
LYS HB2    H N N 262 
LYS HB3    H N N 263 
LYS HG2    H N N 264 
LYS HG3    H N N 265 
LYS HD2    H N N 266 
LYS HD3    H N N 267 
LYS HE2    H N N 268 
LYS HE3    H N N 269 
LYS HZ1    H N N 270 
LYS HZ2    H N N 271 
LYS HZ3    H N N 272 
LYS HXT    H N N 273 
MET N      N N N 274 
MET CA     C N S 275 
MET C      C N N 276 
MET O      O N N 277 
MET CB     C N N 278 
MET CG     C N N 279 
MET SD     S N N 280 
MET CE     C N N 281 
MET OXT    O N N 282 
MET H      H N N 283 
MET H2     H N N 284 
MET HA     H N N 285 
MET HB2    H N N 286 
MET HB3    H N N 287 
MET HG2    H N N 288 
MET HG3    H N N 289 
MET HE1    H N N 290 
MET HE2    H N N 291 
MET HE3    H N N 292 
MET HXT    H N N 293 
PHE N      N N N 294 
PHE CA     C N S 295 
PHE C      C N N 296 
PHE O      O N N 297 
PHE CB     C N N 298 
PHE CG     C Y N 299 
PHE CD1    C Y N 300 
PHE CD2    C Y N 301 
PHE CE1    C Y N 302 
PHE CE2    C Y N 303 
PHE CZ     C Y N 304 
PHE OXT    O N N 305 
PHE H      H N N 306 
PHE H2     H N N 307 
PHE HA     H N N 308 
PHE HB2    H N N 309 
PHE HB3    H N N 310 
PHE HD1    H N N 311 
PHE HD2    H N N 312 
PHE HE1    H N N 313 
PHE HE2    H N N 314 
PHE HZ     H N N 315 
PHE HXT    H N N 316 
PRO N      N N N 317 
PRO CA     C N S 318 
PRO C      C N N 319 
PRO O      O N N 320 
PRO CB     C N N 321 
PRO CG     C N N 322 
PRO CD     C N N 323 
PRO OXT    O N N 324 
PRO H      H N N 325 
PRO HA     H N N 326 
PRO HB2    H N N 327 
PRO HB3    H N N 328 
PRO HG2    H N N 329 
PRO HG3    H N N 330 
PRO HD2    H N N 331 
PRO HD3    H N N 332 
PRO HXT    H N N 333 
SER N      N N N 334 
SER CA     C N S 335 
SER C      C N N 336 
SER O      O N N 337 
SER CB     C N N 338 
SER OG     O N N 339 
SER OXT    O N N 340 
SER H      H N N 341 
SER H2     H N N 342 
SER HA     H N N 343 
SER HB2    H N N 344 
SER HB3    H N N 345 
SER HG     H N N 346 
SER HXT    H N N 347 
THR N      N N N 348 
THR CA     C N S 349 
THR C      C N N 350 
THR O      O N N 351 
THR CB     C N R 352 
THR OG1    O N N 353 
THR CG2    C N N 354 
THR OXT    O N N 355 
THR H      H N N 356 
THR H2     H N N 357 
THR HA     H N N 358 
THR HB     H N N 359 
THR HG1    H N N 360 
THR HG21   H N N 361 
THR HG22   H N N 362 
THR HG23   H N N 363 
THR HXT    H N N 364 
TRP N      N N N 365 
TRP CA     C N S 366 
TRP C      C N N 367 
TRP O      O N N 368 
TRP CB     C N N 369 
TRP CG     C Y N 370 
TRP CD1    C Y N 371 
TRP CD2    C Y N 372 
TRP NE1    N Y N 373 
TRP CE2    C Y N 374 
TRP CE3    C Y N 375 
TRP CZ2    C Y N 376 
TRP CZ3    C Y N 377 
TRP CH2    C Y N 378 
TRP OXT    O N N 379 
TRP H      H N N 380 
TRP H2     H N N 381 
TRP HA     H N N 382 
TRP HB2    H N N 383 
TRP HB3    H N N 384 
TRP HD1    H N N 385 
TRP HE1    H N N 386 
TRP HE3    H N N 387 
TRP HZ2    H N N 388 
TRP HZ3    H N N 389 
TRP HH2    H N N 390 
TRP HXT    H N N 391 
TYR N      N N N 392 
TYR CA     C N S 393 
TYR C      C N N 394 
TYR O      O N N 395 
TYR CB     C N N 396 
TYR CG     C Y N 397 
TYR CD1    C Y N 398 
TYR CD2    C Y N 399 
TYR CE1    C Y N 400 
TYR CE2    C Y N 401 
TYR CZ     C Y N 402 
TYR OH     O N N 403 
TYR OXT    O N N 404 
TYR H      H N N 405 
TYR H2     H N N 406 
TYR HA     H N N 407 
TYR HB2    H N N 408 
TYR HB3    H N N 409 
TYR HD1    H N N 410 
TYR HD2    H N N 411 
TYR HE1    H N N 412 
TYR HE2    H N N 413 
TYR HH     H N N 414 
TYR HXT    H N N 415 
VAL N      N N N 416 
VAL CA     C N S 417 
VAL C      C N N 418 
VAL O      O N N 419 
VAL CB     C N N 420 
VAL CG1    C N N 421 
VAL CG2    C N N 422 
VAL OXT    O N N 423 
VAL H      H N N 424 
VAL H2     H N N 425 
VAL HA     H N N 426 
VAL HB     H N N 427 
VAL HG11   H N N 428 
VAL HG12   H N N 429 
VAL HG13   H N N 430 
VAL HG21   H N N 431 
VAL HG22   H N N 432 
VAL HG23   H N N 433 
VAL HXT    H N N 434 
# 
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 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
ATP PG    O1G    doub N N 70  
ATP PG    O2G    sing N N 71  
ATP PG    O3G    sing N N 72  
ATP PG    O3B    sing N N 73  
ATP O2G   HOG2   sing N N 74  
ATP O3G   HOG3   sing N N 75  
ATP PB    O1B    doub N N 76  
ATP PB    O2B    sing N N 77  
ATP PB    O3B    sing N N 78  
ATP PB    O3A    sing N N 79  
ATP O2B   HOB2   sing N N 80  
ATP PA    O1A    doub N N 81  
ATP PA    O2A    sing N N 82  
ATP PA    O3A    sing N N 83  
ATP PA    "O5'"  sing N N 84  
ATP O2A   HOA2   sing N N 85  
ATP "O5'" "C5'"  sing N N 86  
ATP "C5'" "C4'"  sing N N 87  
ATP "C5'" "H5'1" sing N N 88  
ATP "C5'" "H5'2" sing N N 89  
ATP "C4'" "O4'"  sing N N 90  
ATP "C4'" "C3'"  sing N N 91  
ATP "C4'" "H4'"  sing N N 92  
ATP "O4'" "C1'"  sing N N 93  
ATP "C3'" "O3'"  sing N N 94  
ATP "C3'" "C2'"  sing N N 95  
ATP "C3'" "H3'"  sing N N 96  
ATP "O3'" "HO3'" sing N N 97  
ATP "C2'" "O2'"  sing N N 98  
ATP "C2'" "C1'"  sing N N 99  
ATP "C2'" "H2'"  sing N N 100 
ATP "O2'" "HO2'" sing N N 101 
ATP "C1'" N9     sing N N 102 
ATP "C1'" "H1'"  sing N N 103 
ATP N9    C8     sing Y N 104 
ATP N9    C4     sing Y N 105 
ATP C8    N7     doub Y N 106 
ATP C8    H8     sing N N 107 
ATP N7    C5     sing Y N 108 
ATP C5    C6     sing Y N 109 
ATP C5    C4     doub Y N 110 
ATP C6    N6     sing N N 111 
ATP C6    N1     doub Y N 112 
ATP N6    HN61   sing N N 113 
ATP N6    HN62   sing N N 114 
ATP N1    C2     sing Y N 115 
ATP C2    N3     doub Y N 116 
ATP C2    H2     sing N N 117 
ATP N3    C4     sing Y N 118 
CYS N     CA     sing N N 119 
CYS N     H      sing N N 120 
CYS N     H2     sing N N 121 
CYS CA    C      sing N N 122 
CYS CA    CB     sing N N 123 
CYS CA    HA     sing N N 124 
CYS C     O      doub N N 125 
CYS C     OXT    sing N N 126 
CYS CB    SG     sing N N 127 
CYS CB    HB2    sing N N 128 
CYS CB    HB3    sing N N 129 
CYS SG    HG     sing N N 130 
CYS OXT   HXT    sing N N 131 
GLN N     CA     sing N N 132 
GLN N     H      sing N N 133 
GLN N     H2     sing N N 134 
GLN CA    C      sing N N 135 
GLN CA    CB     sing N N 136 
GLN CA    HA     sing N N 137 
GLN C     O      doub N N 138 
GLN C     OXT    sing N N 139 
GLN CB    CG     sing N N 140 
GLN CB    HB2    sing N N 141 
GLN CB    HB3    sing N N 142 
GLN CG    CD     sing N N 143 
GLN CG    HG2    sing N N 144 
GLN CG    HG3    sing N N 145 
GLN CD    OE1    doub N N 146 
GLN CD    NE2    sing N N 147 
GLN NE2   HE21   sing N N 148 
GLN NE2   HE22   sing N N 149 
GLN OXT   HXT    sing N N 150 
GLU N     CA     sing N N 151 
GLU N     H      sing N N 152 
GLU N     H2     sing N N 153 
GLU CA    C      sing N N 154 
GLU CA    CB     sing N N 155 
GLU CA    HA     sing N N 156 
GLU C     O      doub N N 157 
GLU C     OXT    sing N N 158 
GLU CB    CG     sing N N 159 
GLU CB    HB2    sing N N 160 
GLU CB    HB3    sing N N 161 
GLU CG    CD     sing N N 162 
GLU CG    HG2    sing N N 163 
GLU CG    HG3    sing N N 164 
GLU CD    OE1    doub N N 165 
GLU CD    OE2    sing N N 166 
GLU OE2   HE2    sing N N 167 
GLU OXT   HXT    sing N N 168 
GLY N     CA     sing N N 169 
GLY N     H      sing N N 170 
GLY N     H2     sing N N 171 
GLY CA    C      sing N N 172 
GLY CA    HA2    sing N N 173 
GLY CA    HA3    sing N N 174 
GLY C     O      doub N N 175 
GLY C     OXT    sing N N 176 
GLY OXT   HXT    sing N N 177 
HIS N     CA     sing N N 178 
HIS N     H      sing N N 179 
HIS N     H2     sing N N 180 
HIS CA    C      sing N N 181 
HIS CA    CB     sing N N 182 
HIS CA    HA     sing N N 183 
HIS C     O      doub N N 184 
HIS C     OXT    sing N N 185 
HIS CB    CG     sing N N 186 
HIS CB    HB2    sing N N 187 
HIS CB    HB3    sing N N 188 
HIS CG    ND1    sing Y N 189 
HIS CG    CD2    doub Y N 190 
HIS ND1   CE1    doub Y N 191 
HIS ND1   HD1    sing N N 192 
HIS CD2   NE2    sing Y N 193 
HIS CD2   HD2    sing N N 194 
HIS CE1   NE2    sing Y N 195 
HIS CE1   HE1    sing N N 196 
HIS NE2   HE2    sing N N 197 
HIS OXT   HXT    sing N N 198 
ILE N     CA     sing N N 199 
ILE N     H      sing N N 200 
ILE N     H2     sing N N 201 
ILE CA    C      sing N N 202 
ILE CA    CB     sing N N 203 
ILE CA    HA     sing N N 204 
ILE C     O      doub N N 205 
ILE C     OXT    sing N N 206 
ILE CB    CG1    sing N N 207 
ILE CB    CG2    sing N N 208 
ILE CB    HB     sing N N 209 
ILE CG1   CD1    sing N N 210 
ILE CG1   HG12   sing N N 211 
ILE CG1   HG13   sing N N 212 
ILE CG2   HG21   sing N N 213 
ILE CG2   HG22   sing N N 214 
ILE CG2   HG23   sing N N 215 
ILE CD1   HD11   sing N N 216 
ILE CD1   HD12   sing N N 217 
ILE CD1   HD13   sing N N 218 
ILE OXT   HXT    sing N N 219 
LEU N     CA     sing N N 220 
LEU N     H      sing N N 221 
LEU N     H2     sing N N 222 
LEU CA    C      sing N N 223 
LEU CA    CB     sing N N 224 
LEU CA    HA     sing N N 225 
LEU C     O      doub N N 226 
LEU C     OXT    sing N N 227 
LEU CB    CG     sing N N 228 
LEU CB    HB2    sing N N 229 
LEU CB    HB3    sing N N 230 
LEU CG    CD1    sing N N 231 
LEU CG    CD2    sing N N 232 
LEU CG    HG     sing N N 233 
LEU CD1   HD11   sing N N 234 
LEU CD1   HD12   sing N N 235 
LEU CD1   HD13   sing N N 236 
LEU CD2   HD21   sing N N 237 
LEU CD2   HD22   sing N N 238 
LEU CD2   HD23   sing N N 239 
LEU OXT   HXT    sing N N 240 
LYS N     CA     sing N N 241 
LYS N     H      sing N N 242 
LYS N     H2     sing N N 243 
LYS CA    C      sing N N 244 
LYS CA    CB     sing N N 245 
LYS CA    HA     sing N N 246 
LYS C     O      doub N N 247 
LYS C     OXT    sing N N 248 
LYS CB    CG     sing N N 249 
LYS CB    HB2    sing N N 250 
LYS CB    HB3    sing N N 251 
LYS CG    CD     sing N N 252 
LYS CG    HG2    sing N N 253 
LYS CG    HG3    sing N N 254 
LYS CD    CE     sing N N 255 
LYS CD    HD2    sing N N 256 
LYS CD    HD3    sing N N 257 
LYS CE    NZ     sing N N 258 
LYS CE    HE2    sing N N 259 
LYS CE    HE3    sing N N 260 
LYS NZ    HZ1    sing N N 261 
LYS NZ    HZ2    sing N N 262 
LYS NZ    HZ3    sing N N 263 
LYS OXT   HXT    sing N N 264 
MET N     CA     sing N N 265 
MET N     H      sing N N 266 
MET N     H2     sing N N 267 
MET CA    C      sing N N 268 
MET CA    CB     sing N N 269 
MET CA    HA     sing N N 270 
MET C     O      doub N N 271 
MET C     OXT    sing N N 272 
MET CB    CG     sing N N 273 
MET CB    HB2    sing N N 274 
MET CB    HB3    sing N N 275 
MET CG    SD     sing N N 276 
MET CG    HG2    sing N N 277 
MET CG    HG3    sing N N 278 
MET SD    CE     sing N N 279 
MET CE    HE1    sing N N 280 
MET CE    HE2    sing N N 281 
MET CE    HE3    sing N N 282 
MET OXT   HXT    sing N N 283 
PHE N     CA     sing N N 284 
PHE N     H      sing N N 285 
PHE N     H2     sing N N 286 
PHE CA    C      sing N N 287 
PHE CA    CB     sing N N 288 
PHE CA    HA     sing N N 289 
PHE C     O      doub N N 290 
PHE C     OXT    sing N N 291 
PHE CB    CG     sing N N 292 
PHE CB    HB2    sing N N 293 
PHE CB    HB3    sing N N 294 
PHE CG    CD1    doub Y N 295 
PHE CG    CD2    sing Y N 296 
PHE CD1   CE1    sing Y N 297 
PHE CD1   HD1    sing N N 298 
PHE CD2   CE2    doub Y N 299 
PHE CD2   HD2    sing N N 300 
PHE CE1   CZ     doub Y N 301 
PHE CE1   HE1    sing N N 302 
PHE CE2   CZ     sing Y N 303 
PHE CE2   HE2    sing N N 304 
PHE CZ    HZ     sing N N 305 
PHE OXT   HXT    sing N N 306 
PRO N     CA     sing N N 307 
PRO N     CD     sing N N 308 
PRO N     H      sing N N 309 
PRO CA    C      sing N N 310 
PRO CA    CB     sing N N 311 
PRO CA    HA     sing N N 312 
PRO C     O      doub N N 313 
PRO C     OXT    sing N N 314 
PRO CB    CG     sing N N 315 
PRO CB    HB2    sing N N 316 
PRO CB    HB3    sing N N 317 
PRO CG    CD     sing N N 318 
PRO CG    HG2    sing N N 319 
PRO CG    HG3    sing N N 320 
PRO CD    HD2    sing N N 321 
PRO CD    HD3    sing N N 322 
PRO OXT   HXT    sing N N 323 
SER N     CA     sing N N 324 
SER N     H      sing N N 325 
SER N     H2     sing N N 326 
SER CA    C      sing N N 327 
SER CA    CB     sing N N 328 
SER CA    HA     sing N N 329 
SER C     O      doub N N 330 
SER C     OXT    sing N N 331 
SER CB    OG     sing N N 332 
SER CB    HB2    sing N N 333 
SER CB    HB3    sing N N 334 
SER OG    HG     sing N N 335 
SER OXT   HXT    sing N N 336 
THR N     CA     sing N N 337 
THR N     H      sing N N 338 
THR N     H2     sing N N 339 
THR CA    C      sing N N 340 
THR CA    CB     sing N N 341 
THR CA    HA     sing N N 342 
THR C     O      doub N N 343 
THR C     OXT    sing N N 344 
THR CB    OG1    sing N N 345 
THR CB    CG2    sing N N 346 
THR CB    HB     sing N N 347 
THR OG1   HG1    sing N N 348 
THR CG2   HG21   sing N N 349 
THR CG2   HG22   sing N N 350 
THR CG2   HG23   sing N N 351 
THR OXT   HXT    sing N N 352 
TRP N     CA     sing N N 353 
TRP N     H      sing N N 354 
TRP N     H2     sing N N 355 
TRP CA    C      sing N N 356 
TRP CA    CB     sing N N 357 
TRP CA    HA     sing N N 358 
TRP C     O      doub N N 359 
TRP C     OXT    sing N N 360 
TRP CB    CG     sing N N 361 
TRP CB    HB2    sing N N 362 
TRP CB    HB3    sing N N 363 
TRP CG    CD1    doub Y N 364 
TRP CG    CD2    sing Y N 365 
TRP CD1   NE1    sing Y N 366 
TRP CD1   HD1    sing N N 367 
TRP CD2   CE2    doub Y N 368 
TRP CD2   CE3    sing Y N 369 
TRP NE1   CE2    sing Y N 370 
TRP NE1   HE1    sing N N 371 
TRP CE2   CZ2    sing Y N 372 
TRP CE3   CZ3    doub Y N 373 
TRP CE3   HE3    sing N N 374 
TRP CZ2   CH2    doub Y N 375 
TRP CZ2   HZ2    sing N N 376 
TRP CZ3   CH2    sing Y N 377 
TRP CZ3   HZ3    sing N N 378 
TRP CH2   HH2    sing N N 379 
TRP OXT   HXT    sing N N 380 
TYR N     CA     sing N N 381 
TYR N     H      sing N N 382 
TYR N     H2     sing N N 383 
TYR CA    C      sing N N 384 
TYR CA    CB     sing N N 385 
TYR CA    HA     sing N N 386 
TYR C     O      doub N N 387 
TYR C     OXT    sing N N 388 
TYR CB    CG     sing N N 389 
TYR CB    HB2    sing N N 390 
TYR CB    HB3    sing N N 391 
TYR CG    CD1    doub Y N 392 
TYR CG    CD2    sing Y N 393 
TYR CD1   CE1    sing Y N 394 
TYR CD1   HD1    sing N N 395 
TYR CD2   CE2    doub Y N 396 
TYR CD2   HD2    sing N N 397 
TYR CE1   CZ     doub Y N 398 
TYR CE1   HE1    sing N N 399 
TYR CE2   CZ     sing Y N 400 
TYR CE2   HE2    sing N N 401 
TYR CZ    OH     sing N N 402 
TYR OH    HH     sing N N 403 
TYR OXT   HXT    sing N N 404 
VAL N     CA     sing N N 405 
VAL N     H      sing N N 406 
VAL N     H2     sing N N 407 
VAL CA    C      sing N N 408 
VAL CA    CB     sing N N 409 
VAL CA    HA     sing N N 410 
VAL C     O      doub N N 411 
VAL C     OXT    sing N N 412 
VAL CB    CG1    sing N N 413 
VAL CB    CG2    sing N N 414 
VAL CB    HB     sing N N 415 
VAL CG1   HG11   sing N N 416 
VAL CG1   HG12   sing N N 417 
VAL CG1   HG13   sing N N 418 
VAL CG2   HG21   sing N N 419 
VAL CG2   HG22   sing N N 420 
VAL CG2   HG23   sing N N 421 
VAL OXT   HXT    sing N N 422 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-08-08 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9J3N 
_em_admin.last_update        2025-05-21 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'ATP bound Chlamydia pneumoniae ATP/ADP translocator NTT1(Inward open state)' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          83558 
_em_entity_assembly_naturalsource.organism             'Chlamydia pneumoniae' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 ? ? 
MASKING                    ? 3  ? ? ? ? ? 
'CTF CORRECTION'           ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ? ? 
'MODEL FITTING'            ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'         ? 8  ? ? ? ? ? 
OTHER                      ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ? ? 
CLASSIFICATION             ? 12 1 ? ? ? ? 
RECONSTRUCTION             ? 13 1 ? ? ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Chinese Academy of Sciences' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           XDB0630101 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9J3N 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_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 
C 
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     . GLU A 1 1   ? 124.914 156.488 146.220 1.00 131.82 ? 1   GLU B N     1 
ATOM   2    C CA    . GLU A 1 1   ? 125.469 156.412 144.873 1.00 131.82 ? 1   GLU B CA    1 
ATOM   3    C C     . GLU A 1 1   ? 124.515 155.701 143.919 1.00 131.82 ? 1   GLU B C     1 
ATOM   4    O O     . GLU A 1 1   ? 124.130 156.252 142.890 1.00 131.82 ? 1   GLU B O     1 
ATOM   5    C CB    . GLU A 1 1   ? 126.822 155.696 144.891 1.00 131.82 ? 1   GLU B CB    1 
ATOM   6    C CG    . GLU A 1 1   ? 127.575 155.751 143.569 1.00 131.82 ? 1   GLU B CG    1 
ATOM   7    C CD    . GLU A 1 1   ? 127.641 157.150 142.984 1.00 131.82 ? 1   GLU B CD    1 
ATOM   8    O OE1   . GLU A 1 1   ? 127.422 157.293 141.763 1.00 131.82 ? 1   GLU B OE1   1 
ATOM   9    O OE2   . GLU A 1 1   ? 127.924 158.103 143.740 1.00 131.82 ? 1   GLU B OE2   1 
ATOM   10   N N     . VAL A 1 2   ? 124.148 154.468 144.261 1.00 126.25 ? 2   VAL B N     1 
ATOM   11   C CA    . VAL A 1 2   ? 123.239 153.675 143.440 1.00 126.25 ? 2   VAL B CA    1 
ATOM   12   C C     . VAL A 1 2   ? 122.147 153.116 144.349 1.00 126.25 ? 2   VAL B C     1 
ATOM   13   O O     . VAL A 1 2   ? 121.640 152.008 144.144 1.00 126.25 ? 2   VAL B O     1 
ATOM   14   C CB    . VAL A 1 2   ? 124.010 152.577 142.676 1.00 126.25 ? 2   VAL B CB    1 
ATOM   15   C CG1   . VAL A 1 2   ? 124.614 151.547 143.632 1.00 126.25 ? 2   VAL B CG1   1 
ATOM   16   C CG2   . VAL A 1 2   ? 123.151 151.937 141.581 1.00 126.25 ? 2   VAL B CG2   1 
ATOM   17   N N     . GLN A 1 3   ? 121.769 153.898 145.357 1.00 125.38 ? 3   GLN B N     1 
ATOM   18   C CA    . GLN A 1 3   ? 120.845 153.444 146.390 1.00 125.38 ? 3   GLN B CA    1 
ATOM   19   C C     . GLN A 1 3   ? 119.507 153.005 145.808 1.00 125.38 ? 3   GLN B C     1 
ATOM   20   O O     . GLN A 1 3   ? 118.768 153.814 145.239 1.00 125.38 ? 3   GLN B O     1 
ATOM   21   C CB    . GLN A 1 3   ? 120.631 154.563 147.410 1.00 125.38 ? 3   GLN B CB    1 
ATOM   22   C CG    . GLN A 1 3   ? 119.706 154.192 148.548 1.00 125.38 ? 3   GLN B CG    1 
ATOM   23   C CD    . GLN A 1 3   ? 120.235 153.034 149.365 1.00 125.38 ? 3   GLN B CD    1 
ATOM   24   O OE1   . GLN A 1 3   ? 119.756 151.909 149.245 1.00 125.38 ? 3   GLN B OE1   1 
ATOM   25   N NE2   . GLN A 1 3   ? 121.232 153.303 150.199 1.00 125.38 ? 3   GLN B NE2   1 
ATOM   26   N N     . LEU A 1 4   ? 119.203 151.718 145.956 1.00 119.19 ? 4   LEU B N     1 
ATOM   27   C CA    . LEU A 1 4   ? 117.883 151.171 145.676 1.00 119.19 ? 4   LEU B CA    1 
ATOM   28   C C     . LEU A 1 4   ? 117.209 150.831 146.997 1.00 119.19 ? 4   LEU B C     1 
ATOM   29   O O     . LEU A 1 4   ? 117.876 150.426 147.952 1.00 119.19 ? 4   LEU B O     1 
ATOM   30   C CB    . LEU A 1 4   ? 117.968 149.910 144.812 1.00 119.19 ? 4   LEU B CB    1 
ATOM   31   C CG    . LEU A 1 4   ? 118.869 149.882 143.576 1.00 119.19 ? 4   LEU B CG    1 
ATOM   32   C CD1   . LEU A 1 4   ? 118.987 148.462 143.057 1.00 119.19 ? 4   LEU B CD1   1 
ATOM   33   C CD2   . LEU A 1 4   ? 118.357 150.793 142.481 1.00 119.19 ? 4   LEU B CD2   1 
ATOM   34   N N     . VAL A 1 5   ? 115.891 150.984 147.053 1.00 118.18 ? 5   VAL B N     1 
ATOM   35   C CA    . VAL A 1 5   ? 115.132 150.663 148.256 1.00 118.18 ? 5   VAL B CA    1 
ATOM   36   C C     . VAL A 1 5   ? 113.743 150.194 147.849 1.00 118.18 ? 5   VAL B C     1 
ATOM   37   O O     . VAL A 1 5   ? 113.129 150.751 146.934 1.00 118.18 ? 5   VAL B O     1 
ATOM   38   C CB    . VAL A 1 5   ? 115.064 151.862 149.229 1.00 118.18 ? 5   VAL B CB    1 
ATOM   39   C CG1   . VAL A 1 5   ? 114.319 153.032 148.610 1.00 118.18 ? 5   VAL B CG1   1 
ATOM   40   C CG2   . VAL A 1 5   ? 114.426 151.448 150.547 1.00 118.18 ? 5   VAL B CG2   1 
ATOM   41   N N     . GLU A 1 6   ? 113.261 149.150 148.512 1.00 114.27 ? 6   GLU B N     1 
ATOM   42   C CA    . GLU A 1 6   ? 111.956 148.580 148.223 1.00 114.27 ? 6   GLU B CA    1 
ATOM   43   C C     . GLU A 1 6   ? 110.935 149.005 149.270 1.00 114.27 ? 6   GLU B C     1 
ATOM   44   O O     . GLU A 1 6   ? 111.279 149.448 150.369 1.00 114.27 ? 6   GLU B O     1 
ATOM   45   C CB    . GLU A 1 6   ? 112.029 147.053 148.162 1.00 114.27 ? 6   GLU B CB    1 
ATOM   46   C CG    . GLU A 1 6   ? 112.808 146.503 146.985 1.00 114.27 ? 6   GLU B CG    1 
ATOM   47   C CD    . GLU A 1 6   ? 114.295 146.435 147.249 1.00 114.27 ? 6   GLU B CD    1 
ATOM   48   O OE1   . GLU A 1 6   ? 114.721 146.773 148.372 1.00 114.27 ? 6   GLU B OE1   1 
ATOM   49   O OE2   . GLU A 1 6   ? 115.039 146.033 146.334 1.00 114.27 ? 6   GLU B OE2   1 
ATOM   50   N N     . SER A 1 7   ? 109.664 148.862 148.910 1.00 115.86 ? 7   SER B N     1 
ATOM   51   C CA    . SER A 1 7   ? 108.563 149.155 149.815 1.00 115.86 ? 7   SER B CA    1 
ATOM   52   C C     . SER A 1 7   ? 107.327 148.426 149.317 1.00 115.86 ? 7   SER B C     1 
ATOM   53   O O     . SER A 1 7   ? 107.194 148.135 148.126 1.00 115.86 ? 7   SER B O     1 
ATOM   54   C CB    . SER A 1 7   ? 108.297 150.661 149.918 1.00 115.86 ? 7   SER B CB    1 
ATOM   55   O OG    . SER A 1 7   ? 109.397 151.336 150.501 1.00 115.86 ? 7   SER B OG    1 
ATOM   56   N N     . GLY A 1 8   ? 106.422 148.136 150.246 1.00 119.04 ? 8   GLY B N     1 
ATOM   57   C CA    . GLY A 1 8   ? 105.179 147.474 149.919 1.00 119.04 ? 8   GLY B CA    1 
ATOM   58   C C     . GLY A 1 8   ? 105.102 146.017 150.309 1.00 119.04 ? 8   GLY B C     1 
ATOM   59   O O     . GLY A 1 8   ? 104.112 145.357 149.973 1.00 119.04 ? 8   GLY B O     1 
ATOM   60   N N     . GLY A 1 9   ? 106.111 145.490 150.997 1.00 119.48 ? 9   GLY B N     1 
ATOM   61   C CA    . GLY A 1 9   ? 106.063 144.119 151.450 1.00 119.48 ? 9   GLY B CA    1 
ATOM   62   C C     . GLY A 1 9   ? 105.199 143.945 152.683 1.00 119.48 ? 9   GLY B C     1 
ATOM   63   O O     . GLY A 1 9   ? 104.795 144.903 153.342 1.00 119.48 ? 9   GLY B O     1 
ATOM   64   N N     . GLY A 1 10  ? 104.914 142.697 152.993 1.00 122.68 ? 10  GLY B N     1 
ATOM   65   C CA    . GLY A 1 10  ? 104.096 142.380 154.143 1.00 122.68 ? 10  GLY B CA    1 
ATOM   66   C C     . GLY A 1 10  ? 103.360 141.070 153.918 1.00 122.68 ? 10  GLY B C     1 
ATOM   67   O O     . GLY A 1 10  ? 103.930 140.108 153.407 1.00 122.68 ? 10  GLY B O     1 
ATOM   68   N N     . LEU A 1 11  ? 102.090 141.063 154.313 1.00 127.97 ? 11  LEU B N     1 
ATOM   69   C CA    . LEU A 1 11  ? 101.238 139.893 154.168 1.00 127.97 ? 11  LEU B CA    1 
ATOM   70   C C     . LEU A 1 11  ? 99.807  140.337 153.918 1.00 127.97 ? 11  LEU B C     1 
ATOM   71   O O     . LEU A 1 11  ? 99.355  141.337 154.482 1.00 127.97 ? 11  LEU B O     1 
ATOM   72   C CB    . LEU A 1 11  ? 101.295 138.991 155.412 1.00 127.97 ? 11  LEU B CB    1 
ATOM   73   C CG    . LEU A 1 11  ? 100.557 139.443 156.677 1.00 127.97 ? 11  LEU B CG    1 
ATOM   74   C CD1   . LEU A 1 11  ? 100.375 138.277 157.633 1.00 127.97 ? 11  LEU B CD1   1 
ATOM   75   C CD2   . LEU A 1 11  ? 101.285 140.584 157.370 1.00 127.97 ? 11  LEU B CD2   1 
ATOM   76   N N     . VAL A 1 12  ? 99.102  139.608 153.053 1.00 132.53 ? 12  VAL B N     1 
ATOM   77   C CA    . VAL A 1 12  ? 97.665  139.818 152.922 1.00 132.53 ? 12  VAL B CA    1 
ATOM   78   C C     . VAL A 1 12  ? 96.894  138.523 153.173 1.00 132.53 ? 12  VAL B C     1 
ATOM   79   O O     . VAL A 1 12  ? 96.225  138.391 154.203 1.00 132.53 ? 12  VAL B O     1 
ATOM   80   C CB    . VAL A 1 12  ? 97.331  140.429 151.547 1.00 132.53 ? 12  VAL B CB    1 
ATOM   81   C CG1   . VAL A 1 12  ? 97.721  141.890 151.522 1.00 132.53 ? 12  VAL B CG1   1 
ATOM   82   C CG2   . VAL A 1 12  ? 98.091  139.707 150.438 1.00 132.53 ? 12  VAL B CG2   1 
ATOM   83   N N     . GLN A 1 13  ? 97.008  137.552 152.265 1.00 133.46 ? 13  GLN B N     1 
ATOM   84   C CA    . GLN A 1 13  ? 96.444  136.211 152.405 1.00 133.46 ? 13  GLN B CA    1 
ATOM   85   C C     . GLN A 1 13  ? 96.757  135.444 151.123 1.00 133.46 ? 13  GLN B C     1 
ATOM   86   O O     . GLN A 1 13  ? 97.294  136.000 150.161 1.00 133.46 ? 13  GLN B O     1 
ATOM   87   C CB    . GLN A 1 13  ? 94.935  136.226 152.709 1.00 133.46 ? 13  GLN B CB    1 
ATOM   88   C CG    . GLN A 1 13  ? 93.983  136.596 151.577 1.00 133.46 ? 13  GLN B CG    1 
ATOM   89   C CD    . GLN A 1 13  ? 93.611  135.416 150.703 1.00 133.46 ? 13  GLN B CD    1 
ATOM   90   O OE1   . GLN A 1 13  ? 93.481  134.290 151.184 1.00 133.46 ? 13  GLN B OE1   1 
ATOM   91   N NE2   . GLN A 1 13  ? 93.395  135.675 149.422 1.00 133.46 ? 13  GLN B NE2   1 
ATOM   92   N N     . ALA A 1 14  ? 96.411  134.157 151.120 1.00 132.86 ? 14  ALA B N     1 
ATOM   93   C CA    . ALA A 1 14  ? 96.622  133.307 149.953 1.00 132.86 ? 14  ALA B CA    1 
ATOM   94   C C     . ALA A 1 14  ? 95.629  133.638 148.847 1.00 132.86 ? 14  ALA B C     1 
ATOM   95   O O     . ALA A 1 14  ? 94.514  133.105 148.823 1.00 132.86 ? 14  ALA B O     1 
ATOM   96   C CB    . ALA A 1 14  ? 96.508  131.832 150.341 1.00 132.86 ? 14  ALA B CB    1 
ATOM   97   N N     . GLY A 1 15  ? 96.026  134.510 147.924 1.00 130.74 ? 15  GLY B N     1 
ATOM   98   C CA    . GLY A 1 15  ? 95.147  134.939 146.855 1.00 130.74 ? 15  GLY B CA    1 
ATOM   99   C C     . GLY A 1 15  ? 94.915  136.435 146.877 1.00 130.74 ? 15  GLY B C     1 
ATOM   100  O O     . GLY A 1 15  ? 94.070  136.955 146.144 1.00 130.74 ? 15  GLY B O     1 
ATOM   101  N N     . GLY A 1 16  ? 95.663  137.137 147.724 1.00 129.82 ? 16  GLY B N     1 
ATOM   102  C CA    . GLY A 1 16  ? 95.519  138.572 147.878 1.00 129.82 ? 16  GLY B CA    1 
ATOM   103  C C     . GLY A 1 16  ? 96.202  139.357 146.780 1.00 129.82 ? 16  GLY B C     1 
ATOM   104  O O     . GLY A 1 16  ? 96.274  138.927 145.622 1.00 129.82 ? 16  GLY B O     1 
ATOM   105  N N     . SER A 1 17  ? 96.711  140.531 147.146 1.00 125.53 ? 17  SER B N     1 
ATOM   106  C CA    . SER A 1 17  ? 97.353  141.416 146.185 1.00 125.53 ? 17  SER B CA    1 
ATOM   107  C C     . SER A 1 17  ? 98.291  142.360 146.921 1.00 125.53 ? 17  SER B C     1 
ATOM   108  O O     . SER A 1 17  ? 98.026  142.760 148.058 1.00 125.53 ? 17  SER B O     1 
ATOM   109  C CB    . SER A 1 17  ? 96.320  142.212 145.381 1.00 125.53 ? 17  SER B CB    1 
ATOM   110  O OG    . SER A 1 17  ? 95.513  141.353 144.595 1.00 125.53 ? 17  SER B OG    1 
ATOM   111  N N     . LEU A 1 18  ? 99.392  142.706 146.258 1.00 119.94 ? 18  LEU B N     1 
ATOM   112  C CA    . LEU A 1 18  ? 100.367 143.638 146.803 1.00 119.94 ? 18  LEU B CA    1 
ATOM   113  C C     . LEU A 1 18  ? 101.022 144.386 145.653 1.00 119.94 ? 18  LEU B C     1 
ATOM   114  O O     . LEU A 1 18  ? 101.097 143.889 144.527 1.00 119.94 ? 18  LEU B O     1 
ATOM   115  C CB    . LEU A 1 18  ? 101.424 142.921 147.649 1.00 119.94 ? 18  LEU B CB    1 
ATOM   116  C CG    . LEU A 1 18  ? 101.064 142.638 149.107 1.00 119.94 ? 18  LEU B CG    1 
ATOM   117  C CD1   . LEU A 1 18  ? 101.973 141.569 149.684 1.00 119.94 ? 18  LEU B CD1   1 
ATOM   118  C CD2   . LEU A 1 18  ? 101.137 143.911 149.933 1.00 119.94 ? 18  LEU B CD2   1 
ATOM   119  N N     . ARG A 1 19  ? 101.501 145.592 145.947 1.00 114.49 ? 19  ARG B N     1 
ATOM   120  C CA    . ARG A 1 19  ? 102.164 146.440 144.958 1.00 114.49 ? 19  ARG B CA    1 
ATOM   121  C C     . ARG A 1 19  ? 103.498 146.897 145.535 1.00 114.49 ? 19  ARG B C     1 
ATOM   122  O O     . ARG A 1 19  ? 103.535 147.730 146.445 1.00 114.49 ? 19  ARG B O     1 
ATOM   123  C CB    . ARG A 1 19  ? 101.295 147.631 144.574 1.00 114.49 ? 19  ARG B CB    1 
ATOM   124  C CG    . ARG A 1 19  ? 101.883 148.479 143.461 1.00 114.49 ? 19  ARG B CG    1 
ATOM   125  C CD    . ARG A 1 19  ? 101.044 149.716 143.201 1.00 114.49 ? 19  ARG B CD    1 
ATOM   126  N NE    . ARG A 1 19  ? 101.027 150.066 141.786 1.00 114.49 ? 19  ARG B NE    1 
ATOM   127  C CZ    . ARG A 1 19  ? 100.433 151.147 141.292 1.00 114.49 ? 19  ARG B CZ    1 
ATOM   128  N NH1   . ARG A 1 19  ? 99.803  151.987 142.102 1.00 114.49 ? 19  ARG B NH1   1 
ATOM   129  N NH2   . ARG A 1 19  ? 100.465 151.385 139.988 1.00 114.49 ? 19  ARG B NH2   1 
ATOM   130  N N     . LEU A 1 20  ? 104.588 146.357 145.003 1.00 112.47 ? 20  LEU B N     1 
ATOM   131  C CA    . LEU A 1 20  ? 105.914 146.722 145.469 1.00 112.47 ? 20  LEU B CA    1 
ATOM   132  C C     . LEU A 1 20  ? 106.391 148.000 144.792 1.00 112.47 ? 20  LEU B C     1 
ATOM   133  O O     . LEU A 1 20  ? 105.920 148.373 143.716 1.00 112.47 ? 20  LEU B O     1 
ATOM   134  C CB    . LEU A 1 20  ? 106.905 145.592 145.202 1.00 112.47 ? 20  LEU B CB    1 
ATOM   135  C CG    . LEU A 1 20  ? 106.549 144.245 145.823 1.00 112.47 ? 20  LEU B CG    1 
ATOM   136  C CD1   . LEU A 1 20  ? 107.533 143.184 145.378 1.00 112.47 ? 20  LEU B CD1   1 
ATOM   137  C CD2   . LEU A 1 20  ? 106.510 144.349 147.333 1.00 112.47 ? 20  LEU B CD2   1 
ATOM   138  N N     . SER A 1 21  ? 107.338 148.672 145.440 1.00 113.34 ? 21  SER B N     1 
ATOM   139  C CA    . SER A 1 21  ? 107.916 149.903 144.928 1.00 113.34 ? 21  SER B CA    1 
ATOM   140  C C     . SER A 1 21  ? 109.431 149.777 144.912 1.00 113.34 ? 21  SER B C     1 
ATOM   141  O O     . SER A 1 21  ? 110.012 149.005 145.677 1.00 113.34 ? 21  SER B O     1 
ATOM   142  C CB    . SER A 1 21  ? 107.502 151.111 145.771 1.00 113.34 ? 21  SER B CB    1 
ATOM   143  O OG    . SER A 1 21  ? 106.099 151.301 145.740 1.00 113.34 ? 21  SER B OG    1 
ATOM   144  N N     . CYS A 1 22  ? 110.065 150.539 144.029 1.00 117.67 ? 22  CYS B N     1 
ATOM   145  C CA    . CYS A 1 22  ? 111.513 150.512 143.852 1.00 117.67 ? 22  CYS B CA    1 
ATOM   146  C C     . CYS A 1 22  ? 112.048 151.938 143.759 1.00 117.67 ? 22  CYS B C     1 
ATOM   147  O O     . CYS A 1 22  ? 112.742 152.309 142.812 1.00 117.67 ? 22  CYS B O     1 
ATOM   148  C CB    . CYS A 1 22  ? 111.910 149.686 142.630 1.00 117.67 ? 22  CYS B CB    1 
ATOM   149  S SG    . CYS A 1 22  ? 113.699 149.427 142.488 1.00 117.67 ? 22  CYS B SG    1 
ATOM   150  N N     . ALA A 1 23  ? 111.706 152.768 144.743 1.00 120.99 ? 23  ALA B N     1 
ATOM   151  C CA    . ALA A 1 23  ? 111.988 154.201 144.676 1.00 120.99 ? 23  ALA B CA    1 
ATOM   152  C C     . ALA A 1 23  ? 113.496 154.406 144.788 1.00 120.99 ? 23  ALA B C     1 
ATOM   153  O O     . ALA A 1 23  ? 114.054 154.688 145.851 1.00 120.99 ? 23  ALA B O     1 
ATOM   154  C CB    . ALA A 1 23  ? 111.236 154.945 145.773 1.00 120.99 ? 23  ALA B CB    1 
ATOM   155  N N     . ALA A 1 24  ? 114.162 154.244 143.652 1.00 124.91 ? 24  ALA B N     1 
ATOM   156  C CA    . ALA A 1 24  ? 115.609 154.285 143.544 1.00 124.91 ? 24  ALA B CA    1 
ATOM   157  C C     . ALA A 1 24  ? 116.117 155.718 143.405 1.00 124.91 ? 24  ALA B C     1 
ATOM   158  O O     . ALA A 1 24  ? 115.350 156.680 143.322 1.00 124.91 ? 24  ALA B O     1 
ATOM   159  C CB    . ALA A 1 24  ? 116.061 153.447 142.353 1.00 124.91 ? 24  ALA B CB    1 
ATOM   160  N N     . SER A 1 25  ? 117.442 155.846 143.379 1.00 127.37 ? 25  SER B N     1 
ATOM   161  C CA    . SER A 1 25  ? 118.103 157.131 143.205 1.00 127.37 ? 25  SER B CA    1 
ATOM   162  C C     . SER A 1 25  ? 119.552 156.884 142.817 1.00 127.37 ? 25  SER B C     1 
ATOM   163  O O     . SER A 1 25  ? 120.114 155.822 143.088 1.00 127.37 ? 25  SER B O     1 
ATOM   164  C CB    . SER A 1 25  ? 118.030 157.983 144.476 1.00 127.37 ? 25  SER B CB    1 
ATOM   165  O OG    . SER A 1 25  ? 116.695 158.346 144.778 1.00 127.37 ? 25  SER B OG    1 
ATOM   166  N N     . GLY A 1 26  ? 120.149 157.883 142.179 1.00 127.31 ? 26  GLY B N     1 
ATOM   167  C CA    . GLY A 1 26  ? 121.565 157.870 141.890 1.00 127.31 ? 26  GLY B CA    1 
ATOM   168  C C     . GLY A 1 26  ? 121.978 157.396 140.513 1.00 127.31 ? 26  GLY B C     1 
ATOM   169  O O     . GLY A 1 26  ? 123.109 156.919 140.364 1.00 127.31 ? 26  GLY B O     1 
ATOM   170  N N     . PHE A 1 27  ? 121.115 157.517 139.509 1.00 125.08 ? 27  PHE B N     1 
ATOM   171  C CA    . PHE A 1 27  ? 121.461 157.131 138.147 1.00 125.08 ? 27  PHE B CA    1 
ATOM   172  C C     . PHE A 1 27  ? 120.390 157.651 137.201 1.00 125.08 ? 27  PHE B C     1 
ATOM   173  O O     . PHE A 1 27  ? 119.301 158.047 137.626 1.00 125.08 ? 27  PHE B O     1 
ATOM   174  C CB    . PHE A 1 27  ? 121.615 155.613 138.001 1.00 125.08 ? 27  PHE B CB    1 
ATOM   175  C CG    . PHE A 1 27  ? 120.516 154.824 138.651 1.00 125.08 ? 27  PHE B CG    1 
ATOM   176  C CD1   . PHE A 1 27  ? 120.686 154.291 139.917 1.00 125.08 ? 27  PHE B CD1   1 
ATOM   177  C CD2   . PHE A 1 27  ? 119.315 154.616 137.999 1.00 125.08 ? 27  PHE B CD2   1 
ATOM   178  C CE1   . PHE A 1 27  ? 119.680 153.564 140.518 1.00 125.08 ? 27  PHE B CE1   1 
ATOM   179  C CE2   . PHE A 1 27  ? 118.305 153.892 138.597 1.00 125.08 ? 27  PHE B CE2   1 
ATOM   180  C CZ    . PHE A 1 27  ? 118.489 153.365 139.857 1.00 125.08 ? 27  PHE B CZ    1 
ATOM   181  N N     . THR A 1 28  ? 120.717 157.641 135.912 1.00 123.53 ? 28  THR B N     1 
ATOM   182  C CA    . THR A 1 28  ? 119.790 158.083 134.873 1.00 123.53 ? 28  THR B CA    1 
ATOM   183  C C     . THR A 1 28  ? 118.717 157.018 134.703 1.00 123.53 ? 28  THR B C     1 
ATOM   184  O O     . THR A 1 28  ? 118.884 156.062 133.944 1.00 123.53 ? 28  THR B O     1 
ATOM   185  C CB    . THR A 1 28  ? 120.530 158.335 133.565 1.00 123.53 ? 28  THR B CB    1 
ATOM   186  O OG1   . THR A 1 28  ? 120.825 157.084 132.933 1.00 123.53 ? 28  THR B OG1   1 
ATOM   187  C CG2   . THR A 1 28  ? 121.827 159.080 133.827 1.00 123.53 ? 28  THR B CG2   1 
ATOM   188  N N     . PHE A 1 29  ? 117.607 157.185 135.427 1.00 118.95 ? 29  PHE B N     1 
ATOM   189  C CA    . PHE A 1 29  ? 116.551 156.180 135.435 1.00 118.95 ? 29  PHE B CA    1 
ATOM   190  C C     . PHE A 1 29  ? 116.001 155.922 134.040 1.00 118.95 ? 29  PHE B C     1 
ATOM   191  O O     . PHE A 1 29  ? 115.559 154.807 133.745 1.00 118.95 ? 29  PHE B O     1 
ATOM   192  C CB    . PHE A 1 29  ? 115.430 156.622 136.371 1.00 118.95 ? 29  PHE B CB    1 
ATOM   193  C CG    . PHE A 1 29  ? 114.565 155.501 136.854 1.00 118.95 ? 29  PHE B CG    1 
ATOM   194  C CD1   . PHE A 1 29  ? 113.505 155.047 136.094 1.00 118.95 ? 29  PHE B CD1   1 
ATOM   195  C CD2   . PHE A 1 29  ? 114.807 154.907 138.077 1.00 118.95 ? 29  PHE B CD2   1 
ATOM   196  C CE1   . PHE A 1 29  ? 112.709 154.022 136.543 1.00 118.95 ? 29  PHE B CE1   1 
ATOM   197  C CE2   . PHE A 1 29  ? 114.013 153.882 138.530 1.00 118.95 ? 29  PHE B CE2   1 
ATOM   198  C CZ    . PHE A 1 29  ? 112.963 153.441 137.762 1.00 118.95 ? 29  PHE B CZ    1 
ATOM   199  N N     . SER A 1 30  ? 116.016 156.931 133.170 1.00 120.80 ? 30  SER B N     1 
ATOM   200  C CA    . SER A 1 30  ? 115.533 156.739 131.810 1.00 120.80 ? 30  SER B CA    1 
ATOM   201  C C     . SER A 1 30  ? 116.440 155.837 130.985 1.00 120.80 ? 30  SER B C     1 
ATOM   202  O O     . SER A 1 30  ? 116.060 155.462 129.871 1.00 120.80 ? 30  SER B O     1 
ATOM   203  C CB    . SER A 1 30  ? 115.376 158.092 131.112 1.00 120.80 ? 30  SER B CB    1 
ATOM   204  O OG    . SER A 1 30  ? 116.632 158.723 130.926 1.00 120.80 ? 30  SER B OG    1 
ATOM   205  N N     . ASP A 1 31  ? 117.613 155.476 131.497 1.00 119.07 ? 31  ASP B N     1 
ATOM   206  C CA    . ASP A 1 31  ? 118.581 154.669 130.769 1.00 119.07 ? 31  ASP B CA    1 
ATOM   207  C C     . ASP A 1 31  ? 119.087 153.513 131.622 1.00 119.07 ? 31  ASP B C     1 
ATOM   208  O O     . ASP A 1 31  ? 120.285 153.228 131.665 1.00 119.07 ? 31  ASP B O     1 
ATOM   209  C CB    . ASP A 1 31  ? 119.745 155.528 130.282 1.00 119.07 ? 31  ASP B CB    1 
ATOM   210  C CG    . ASP A 1 31  ? 119.335 156.504 129.198 1.00 119.07 ? 31  ASP B CG    1 
ATOM   211  O OD1   . ASP A 1 31  ? 118.399 156.189 128.434 1.00 119.07 ? 31  ASP B OD1   1 
ATOM   212  O OD2   . ASP A 1 31  ? 119.946 157.591 129.114 1.00 119.07 ? 31  ASP B OD2   1 
ATOM   213  N N     . THR A 1 32  ? 118.179 152.836 132.318 1.00 111.05 ? 32  THR B N     1 
ATOM   214  C CA    . THR A 1 32  ? 118.530 151.679 133.126 1.00 111.05 ? 32  THR B CA    1 
ATOM   215  C C     . THR A 1 32  ? 117.468 150.600 132.973 1.00 111.05 ? 32  THR B C     1 
ATOM   216  O O     . THR A 1 32  ? 116.279 150.888 132.819 1.00 111.05 ? 32  THR B O     1 
ATOM   217  C CB    . THR A 1 32  ? 118.699 152.050 134.606 1.00 111.05 ? 32  THR B CB    1 
ATOM   218  O OG1   . THR A 1 32  ? 119.146 150.906 135.341 1.00 111.05 ? 32  THR B OG1   1 
ATOM   219  C CG2   . THR A 1 32  ? 117.394 152.549 135.194 1.00 111.05 ? 32  THR B CG2   1 
ATOM   220  N N     . TYR A 1 33  ? 117.917 149.350 133.005 1.00 100.99 ? 33  TYR B N     1 
ATOM   221  C CA    . TYR A 1 33  ? 117.045 148.192 132.868 1.00 100.99 ? 33  TYR B CA    1 
ATOM   222  C C     . TYR A 1 33  ? 116.703 147.679 134.260 1.00 100.99 ? 33  TYR B C     1 
ATOM   223  O O     . TYR A 1 33  ? 117.580 147.175 134.968 1.00 100.99 ? 33  TYR B O     1 
ATOM   224  C CB    . TYR A 1 33  ? 117.725 147.096 132.052 1.00 100.99 ? 33  TYR B CB    1 
ATOM   225  C CG    . TYR A 1 33  ? 116.777 146.248 131.246 1.00 100.99 ? 33  TYR B CG    1 
ATOM   226  C CD1   . TYR A 1 33  ? 116.716 146.365 129.868 1.00 100.99 ? 33  TYR B CD1   1 
ATOM   227  C CD2   . TYR A 1 33  ? 115.927 145.349 131.863 1.00 100.99 ? 33  TYR B CD2   1 
ATOM   228  C CE1   . TYR A 1 33  ? 115.853 145.598 129.128 1.00 100.99 ? 33  TYR B CE1   1 
ATOM   229  C CE2   . TYR A 1 33  ? 115.057 144.579 131.130 1.00 100.99 ? 33  TYR B CE2   1 
ATOM   230  C CZ    . TYR A 1 33  ? 115.024 144.708 129.763 1.00 100.99 ? 33  TYR B CZ    1 
ATOM   231  O OH    . TYR A 1 33  ? 114.153 143.943 129.029 1.00 100.99 ? 33  TYR B OH    1 
ATOM   232  N N     . MET A 1 34  ? 115.443 147.808 134.651 1.00 100.77 ? 34  MET B N     1 
ATOM   233  C CA    . MET A 1 34  ? 115.002 147.431 135.984 1.00 100.77 ? 34  MET B CA    1 
ATOM   234  C C     . MET A 1 34  ? 114.307 146.078 135.951 1.00 100.77 ? 34  MET B C     1 
ATOM   235  O O     . MET A 1 34  ? 114.078 145.495 134.891 1.00 100.77 ? 34  MET B O     1 
ATOM   236  C CB    . MET A 1 34  ? 114.068 148.495 136.561 1.00 100.77 ? 34  MET B CB    1 
ATOM   237  C CG    . MET A 1 34  ? 114.566 149.910 136.371 1.00 100.77 ? 34  MET B CG    1 
ATOM   238  S SD    . MET A 1 34  ? 115.831 150.345 137.568 1.00 100.77 ? 34  MET B SD    1 
ATOM   239  C CE    . MET A 1 34  ? 115.033 149.848 139.090 1.00 100.77 ? 34  MET B CE    1 
ATOM   240  N N     . GLY A 1 35  ? 113.974 145.581 137.135 1.00 98.35  ? 35  GLY B N     1 
ATOM   241  C CA    . GLY A 1 35  ? 113.285 144.308 137.240 1.00 98.35  ? 35  GLY B CA    1 
ATOM   242  C C     . GLY A 1 35  ? 113.178 143.880 138.686 1.00 98.35  ? 35  GLY B C     1 
ATOM   243  O O     . GLY A 1 35  ? 113.719 144.522 139.591 1.00 98.35  ? 35  GLY B O     1 
ATOM   244  N N     . TRP A 1 36  ? 112.469 142.771 138.889 1.00 100.57 ? 36  TRP B N     1 
ATOM   245  C CA    . TRP A 1 36  ? 112.205 142.242 140.218 1.00 100.57 ? 36  TRP B CA    1 
ATOM   246  C C     . TRP A 1 36  ? 112.622 140.784 140.300 1.00 100.57 ? 36  TRP B C     1 
ATOM   247  O O     . TRP A 1 36  ? 112.357 140.000 139.385 1.00 100.57 ? 36  TRP B O     1 
ATOM   248  C CB    . TRP A 1 36  ? 110.731 142.363 140.582 1.00 100.57 ? 36  TRP B CB    1 
ATOM   249  C CG    . TRP A 1 36  ? 110.310 143.750 140.873 1.00 100.57 ? 36  TRP B CG    1 
ATOM   250  C CD1   . TRP A 1 36  ? 109.794 144.647 139.993 1.00 100.57 ? 36  TRP B CD1   1 
ATOM   251  C CD2   . TRP A 1 36  ? 110.376 144.415 142.134 1.00 100.57 ? 36  TRP B CD2   1 
ATOM   252  N NE1   . TRP A 1 36  ? 109.527 145.831 140.629 1.00 100.57 ? 36  TRP B NE1   1 
ATOM   253  C CE2   . TRP A 1 36  ? 109.877 145.714 141.947 1.00 100.57 ? 36  TRP B CE2   1 
ATOM   254  C CE3   . TRP A 1 36  ? 110.806 144.036 143.406 1.00 100.57 ? 36  TRP B CE3   1 
ATOM   255  C CZ2   . TRP A 1 36  ? 109.797 146.637 142.981 1.00 100.57 ? 36  TRP B CZ2   1 
ATOM   256  C CZ3   . TRP A 1 36  ? 110.725 144.952 144.431 1.00 100.57 ? 36  TRP B CZ3   1 
ATOM   257  C CH2   . TRP A 1 36  ? 110.226 146.238 144.214 1.00 100.57 ? 36  TRP B CH2   1 
ATOM   258  N N     . PHE A 1 37  ? 113.268 140.427 141.404 1.00 97.65  ? 37  PHE B N     1 
ATOM   259  C CA    . PHE A 1 37  ? 113.690 139.067 141.698 1.00 97.65  ? 37  PHE B CA    1 
ATOM   260  C C     . PHE A 1 37  ? 113.131 138.656 143.052 1.00 97.65  ? 37  PHE B C     1 
ATOM   261  O O     . PHE A 1 37  ? 112.568 139.468 143.787 1.00 97.65  ? 37  PHE B O     1 
ATOM   262  C CB    . PHE A 1 37  ? 115.218 138.942 141.708 1.00 97.65  ? 37  PHE B CB    1 
ATOM   263  C CG    . PHE A 1 37  ? 115.861 139.126 140.364 1.00 97.65  ? 37  PHE B CG    1 
ATOM   264  C CD1   . PHE A 1 37  ? 115.812 140.343 139.716 1.00 97.65  ? 37  PHE B CD1   1 
ATOM   265  C CD2   . PHE A 1 37  ? 116.537 138.086 139.763 1.00 97.65  ? 37  PHE B CD2   1 
ATOM   266  C CE1   . PHE A 1 37  ? 116.405 140.513 138.492 1.00 97.65  ? 37  PHE B CE1   1 
ATOM   267  C CE2   . PHE A 1 37  ? 117.134 138.255 138.540 1.00 97.65  ? 37  PHE B CE2   1 
ATOM   268  C CZ    . PHE A 1 37  ? 117.065 139.470 137.904 1.00 97.65  ? 37  PHE B CZ    1 
ATOM   269  N N     . ARG A 1 38  ? 113.294 137.380 143.385 1.00 102.94 ? 38  ARG B N     1 
ATOM   270  C CA    . ARG A 1 38  ? 112.897 136.896 144.697 1.00 102.94 ? 38  ARG B CA    1 
ATOM   271  C C     . ARG A 1 38  ? 113.773 135.714 145.080 1.00 102.94 ? 38  ARG B C     1 
ATOM   272  O O     . ARG A 1 38  ? 114.268 134.984 144.218 1.00 102.94 ? 38  ARG B O     1 
ATOM   273  C CB    . ARG A 1 38  ? 111.421 136.498 144.735 1.00 102.94 ? 38  ARG B CB    1 
ATOM   274  C CG    . ARG A 1 38  ? 111.040 135.408 143.760 1.00 102.94 ? 38  ARG B CG    1 
ATOM   275  C CD    . ARG A 1 38  ? 109.554 135.123 143.837 1.00 102.94 ? 38  ARG B CD    1 
ATOM   276  N NE    . ARG A 1 38  ? 109.123 134.178 142.816 1.00 102.94 ? 38  ARG B NE    1 
ATOM   277  C CZ    . ARG A 1 38  ? 107.853 133.921 142.532 1.00 102.94 ? 38  ARG B CZ    1 
ATOM   278  N NH1   . ARG A 1 38  ? 106.888 134.542 143.194 1.00 102.94 ? 38  ARG B NH1   1 
ATOM   279  N NH2   . ARG A 1 38  ? 107.547 133.044 141.588 1.00 102.94 ? 38  ARG B NH2   1 
ATOM   280  N N     . GLN A 1 39  ? 113.957 135.533 146.387 1.00 109.18 ? 39  GLN B N     1 
ATOM   281  C CA    . GLN A 1 39  ? 114.826 134.483 146.918 1.00 109.18 ? 39  GLN B CA    1 
ATOM   282  C C     . GLN A 1 39  ? 114.183 133.928 148.183 1.00 109.18 ? 39  GLN B C     1 
ATOM   283  O O     . GLN A 1 39  ? 114.342 134.496 149.266 1.00 109.18 ? 39  GLN B O     1 
ATOM   284  C CB    . GLN A 1 39  ? 116.225 135.016 147.200 1.00 109.18 ? 39  GLN B CB    1 
ATOM   285  C CG    . GLN A 1 39  ? 117.175 133.983 147.775 1.00 109.18 ? 39  GLN B CG    1 
ATOM   286  C CD    . GLN A 1 39  ? 118.621 134.425 147.715 1.00 109.18 ? 39  GLN B CD    1 
ATOM   287  O OE1   . GLN A 1 39  ? 118.915 135.617 147.648 1.00 109.18 ? 39  GLN B OE1   1 
ATOM   288  N NE2   . GLN A 1 39  ? 119.535 133.463 147.735 1.00 109.18 ? 39  GLN B NE2   1 
ATOM   289  N N     . ALA A 1 40  ? 113.460 132.824 148.041 1.00 115.13 ? 40  ALA B N     1 
ATOM   290  C CA    . ALA A 1 40  ? 112.897 132.158 149.200 1.00 115.13 ? 40  ALA B CA    1 
ATOM   291  C C     . ALA A 1 40  ? 114.013 131.523 150.030 1.00 115.13 ? 40  ALA B C     1 
ATOM   292  O O     . ALA A 1 40  ? 115.071 131.178 149.498 1.00 115.13 ? 40  ALA B O     1 
ATOM   293  C CB    . ALA A 1 40  ? 111.893 131.093 148.769 1.00 115.13 ? 40  ALA B CB    1 
ATOM   294  N N     . PRO A 1 41  ? 113.808 131.369 151.337 1.00 117.89 ? 41  PRO B N     1 
ATOM   295  C CA    . PRO A 1 41  ? 114.833 130.721 152.169 1.00 117.89 ? 41  PRO B CA    1 
ATOM   296  C C     . PRO A 1 41  ? 115.040 129.276 151.746 1.00 117.89 ? 41  PRO B C     1 
ATOM   297  O O     . PRO A 1 41  ? 114.103 128.475 151.723 1.00 117.89 ? 41  PRO B O     1 
ATOM   298  C CB    . PRO A 1 41  ? 114.256 130.827 153.586 1.00 117.89 ? 41  PRO B CB    1 
ATOM   299  C CG    . PRO A 1 41  ? 112.787 130.983 153.386 1.00 117.89 ? 41  PRO B CG    1 
ATOM   300  C CD    . PRO A 1 41  ? 112.644 131.792 152.133 1.00 117.89 ? 41  PRO B CD    1 
ATOM   301  N N     . GLY A 1 42  ? 116.285 128.947 151.405 1.00 119.99 ? 42  GLY B N     1 
ATOM   302  C CA    . GLY A 1 42  ? 116.627 127.628 150.923 1.00 119.99 ? 42  GLY B CA    1 
ATOM   303  C C     . GLY A 1 42  ? 116.572 127.462 149.421 1.00 119.99 ? 42  GLY B C     1 
ATOM   304  O O     . GLY A 1 42  ? 116.933 126.390 148.920 1.00 119.99 ? 42  GLY B O     1 
ATOM   305  N N     . LYS A 1 43  ? 116.130 128.478 148.689 1.00 116.16 ? 43  LYS B N     1 
ATOM   306  C CA    . LYS A 1 43  ? 116.067 128.449 147.237 1.00 116.16 ? 43  LYS B CA    1 
ATOM   307  C C     . LYS A 1 43  ? 117.065 129.437 146.649 1.00 116.16 ? 43  LYS B C     1 
ATOM   308  O O     . LYS A 1 43  ? 117.660 130.257 147.353 1.00 116.16 ? 43  LYS B O     1 
ATOM   309  C CB    . LYS A 1 43  ? 114.651 128.769 146.749 1.00 116.16 ? 43  LYS B CB    1 
ATOM   310  C CG    . LYS A 1 43  ? 113.615 127.739 147.149 1.00 116.16 ? 43  LYS B CG    1 
ATOM   311  C CD    . LYS A 1 43  ? 113.825 126.438 146.398 1.00 116.16 ? 43  LYS B CD    1 
ATOM   312  C CE    . LYS A 1 43  ? 113.594 126.623 144.908 1.00 116.16 ? 43  LYS B CE    1 
ATOM   313  N NZ    . LYS A 1 43  ? 112.216 127.108 144.620 1.00 116.16 ? 43  LYS B NZ    1 
ATOM   314  N N     . GLU A 1 44  ? 117.245 129.347 145.337 1.00 115.61 ? 44  GLU B N     1 
ATOM   315  C CA    . GLU A 1 44  ? 118.113 130.262 144.615 1.00 115.61 ? 44  GLU B CA    1 
ATOM   316  C C     . GLU A 1 44  ? 117.311 131.454 144.103 1.00 115.61 ? 44  GLU B C     1 
ATOM   317  O O     . GLU A 1 44  ? 116.104 131.369 143.870 1.00 115.61 ? 44  GLU B O     1 
ATOM   318  C CB    . GLU A 1 44  ? 118.802 129.548 143.453 1.00 115.61 ? 44  GLU B CB    1 
ATOM   319  C CG    . GLU A 1 44  ? 119.789 128.471 143.878 1.00 115.61 ? 44  GLU B CG    1 
ATOM   320  C CD    . GLU A 1 44  ? 121.015 129.038 144.572 1.00 115.61 ? 44  GLU B CD    1 
ATOM   321  O OE1   . GLU A 1 44  ? 121.427 130.166 144.229 1.00 115.61 ? 44  GLU B OE1   1 
ATOM   322  O OE2   . GLU A 1 44  ? 121.568 128.354 145.460 1.00 115.61 ? 44  GLU B OE2   1 
ATOM   323  N N     . ARG A 1 45  ? 118.003 132.576 143.935 1.00 106.29 ? 45  ARG B N     1 
ATOM   324  C CA    . ARG A 1 45  ? 117.352 133.815 143.529 1.00 106.29 ? 45  ARG B CA    1 
ATOM   325  C C     . ARG A 1 45  ? 116.856 133.704 142.092 1.00 106.29 ? 45  ARG B C     1 
ATOM   326  O O     . ARG A 1 45  ? 117.656 133.588 141.158 1.00 106.29 ? 45  ARG B O     1 
ATOM   327  C CB    . ARG A 1 45  ? 118.320 134.984 143.679 1.00 106.29 ? 45  ARG B CB    1 
ATOM   328  C CG    . ARG A 1 45  ? 117.760 136.322 143.248 1.00 106.29 ? 45  ARG B CG    1 
ATOM   329  C CD    . ARG A 1 45  ? 118.709 137.453 143.603 1.00 106.29 ? 45  ARG B CD    1 
ATOM   330  N NE    . ARG A 1 45  ? 118.739 137.713 145.038 1.00 106.29 ? 45  ARG B NE    1 
ATOM   331  C CZ    . ARG A 1 45  ? 119.691 138.409 145.650 1.00 106.29 ? 45  ARG B CZ    1 
ATOM   332  N NH1   . ARG A 1 45  ? 120.696 138.916 144.952 1.00 106.29 ? 45  ARG B NH1   1 
ATOM   333  N NH2   . ARG A 1 45  ? 119.639 138.598 146.960 1.00 106.29 ? 45  ARG B NH2   1 
ATOM   334  N N     . GLU A 1 46  ? 115.539 133.737 141.917 1.00 102.66 ? 46  GLU B N     1 
ATOM   335  C CA    . GLU A 1 46  ? 114.901 133.690 140.611 1.00 102.66 ? 46  GLU B CA    1 
ATOM   336  C C     . GLU A 1 46  ? 114.315 135.053 140.273 1.00 102.66 ? 46  GLU B C     1 
ATOM   337  O O     . GLU A 1 46  ? 114.044 135.869 141.157 1.00 102.66 ? 46  GLU B O     1 
ATOM   338  C CB    . GLU A 1 46  ? 113.801 132.626 140.578 1.00 102.66 ? 46  GLU B CB    1 
ATOM   339  C CG    . GLU A 1 46  ? 112.615 132.947 141.469 1.00 102.66 ? 46  GLU B CG    1 
ATOM   340  C CD    . GLU A 1 46  ? 111.468 131.972 141.293 1.00 102.66 ? 46  GLU B CD    1 
ATOM   341  O OE1   . GLU A 1 46  ? 111.617 131.011 140.510 1.00 102.66 ? 46  GLU B OE1   1 
ATOM   342  O OE2   . GLU A 1 46  ? 110.416 132.168 141.937 1.00 102.66 ? 46  GLU B OE2   1 
ATOM   343  N N     . PHE A 1 47  ? 114.118 135.300 138.982 1.00 97.57  ? 47  PHE B N     1 
ATOM   344  C CA    . PHE A 1 47  ? 113.585 136.580 138.545 1.00 97.57  ? 47  PHE B CA    1 
ATOM   345  C C     . PHE A 1 47  ? 112.072 136.501 138.424 1.00 97.57  ? 47  PHE B C     1 
ATOM   346  O O     . PHE A 1 47  ? 111.506 135.444 138.139 1.00 97.57  ? 47  PHE B O     1 
ATOM   347  C CB    . PHE A 1 47  ? 114.192 137.015 137.211 1.00 97.57  ? 47  PHE B CB    1 
ATOM   348  C CG    . PHE A 1 47  ? 113.664 136.271 136.021 1.00 97.57  ? 47  PHE B CG    1 
ATOM   349  C CD1   . PHE A 1 47  ? 114.192 135.048 135.658 1.00 97.57  ? 47  PHE B CD1   1 
ATOM   350  C CD2   . PHE A 1 47  ? 112.672 136.827 135.233 1.00 97.57  ? 47  PHE B CD2   1 
ATOM   351  C CE1   . PHE A 1 47  ? 113.711 134.375 134.553 1.00 97.57  ? 47  PHE B CE1   1 
ATOM   352  C CE2   . PHE A 1 47  ? 112.191 136.163 134.130 1.00 97.57  ? 47  PHE B CE2   1 
ATOM   353  C CZ    . PHE A 1 47  ? 112.711 134.935 133.787 1.00 97.57  ? 47  PHE B CZ    1 
ATOM   354  N N     . VAL A 1 48  ? 111.419 137.634 138.647 1.00 98.07  ? 48  VAL B N     1 
ATOM   355  C CA    . VAL A 1 48  ? 109.969 137.736 138.588 1.00 98.07  ? 48  VAL B CA    1 
ATOM   356  C C     . VAL A 1 48  ? 109.516 138.477 137.338 1.00 98.07  ? 48  VAL B C     1 
ATOM   357  O O     . VAL A 1 48  ? 108.639 138.007 136.613 1.00 98.07  ? 48  VAL B O     1 
ATOM   358  C CB    . VAL A 1 48  ? 109.414 138.410 139.861 1.00 98.07  ? 48  VAL B CB    1 
ATOM   359  C CG1   . VAL A 1 48  ? 107.990 138.847 139.641 1.00 98.07  ? 48  VAL B CG1   1 
ATOM   360  C CG2   . VAL A 1 48  ? 109.493 137.458 141.029 1.00 98.07  ? 48  VAL B CG2   1 
ATOM   361  N N     . ALA A 1 49  ? 110.120 139.628 137.059 1.00 96.79  ? 49  ALA B N     1 
ATOM   362  C CA    . ALA A 1 49  ? 109.729 140.442 135.919 1.00 96.79  ? 49  ALA B CA    1 
ATOM   363  C C     . ALA A 1 49  ? 110.791 141.503 135.687 1.00 96.79  ? 49  ALA B C     1 
ATOM   364  O O     . ALA A 1 49  ? 111.487 141.906 136.618 1.00 96.79  ? 49  ALA B O     1 
ATOM   365  C CB    . ALA A 1 49  ? 108.363 141.095 136.142 1.00 96.79  ? 49  ALA B CB    1 
ATOM   366  N N     . THR A 1 50  ? 110.916 141.942 134.435 1.00 95.47  ? 50  THR B N     1 
ATOM   367  C CA    . THR A 1 50  ? 111.824 143.023 134.077 1.00 95.47  ? 50  THR B CA    1 
ATOM   368  C C     . THR A 1 50  ? 111.120 143.976 133.124 1.00 95.47  ? 50  THR B C     1 
ATOM   369  O O     . THR A 1 50  ? 110.271 143.565 132.331 1.00 95.47  ? 50  THR B O     1 
ATOM   370  C CB    . THR A 1 50  ? 113.115 142.518 133.417 1.00 95.47  ? 50  THR B CB    1 
ATOM   371  O OG1   . THR A 1 50  ? 112.857 142.197 132.046 1.00 95.47  ? 50  THR B OG1   1 
ATOM   372  C CG2   . THR A 1 50  ? 113.650 141.290 134.129 1.00 95.47  ? 50  THR B CG2   1 
ATOM   373  N N     . ILE A 1 51  ? 111.484 145.252 133.203 1.00 100.16 ? 51  ILE B N     1 
ATOM   374  C CA    . ILE A 1 51  ? 110.886 146.301 132.386 1.00 100.16 ? 51  ILE B CA    1 
ATOM   375  C C     . ILE A 1 51  ? 111.989 146.922 131.535 1.00 100.16 ? 51  ILE B C     1 
ATOM   376  O O     . ILE A 1 51  ? 113.076 147.217 132.042 1.00 100.16 ? 51  ILE B O     1 
ATOM   377  C CB    . ILE A 1 51  ? 110.171 147.352 133.259 1.00 100.16 ? 51  ILE B CB    1 
ATOM   378  C CG1   . ILE A 1 51  ? 109.278 148.250 132.409 1.00 100.16 ? 51  ILE B CG1   1 
ATOM   379  C CG2   . ILE A 1 51  ? 111.150 148.153 134.109 1.00 100.16 ? 51  ILE B CG2   1 
ATOM   380  C CD1   . ILE A 1 51  ? 107.928 147.648 132.134 1.00 100.16 ? 51  ILE B CD1   1 
ATOM   381  N N     . ASP A 1 52  ? 111.730 147.075 130.234 1.00 105.68 ? 52  ASP B N     1 
ATOM   382  C CA    . ASP A 1 52  ? 112.827 147.304 129.298 1.00 105.68 ? 52  ASP B CA    1 
ATOM   383  C C     . ASP A 1 52  ? 113.560 148.625 129.504 1.00 105.68 ? 52  ASP B C     1 
ATOM   384  O O     . ASP A 1 52  ? 114.645 148.641 130.091 1.00 105.68 ? 52  ASP B O     1 
ATOM   385  C CB    . ASP A 1 52  ? 112.295 147.227 127.864 1.00 105.68 ? 52  ASP B CB    1 
ATOM   386  C CG    . ASP A 1 52  ? 113.368 147.482 126.821 1.00 105.68 ? 52  ASP B CG    1 
ATOM   387  O OD1   . ASP A 1 52  ? 113.990 146.508 126.345 1.00 105.68 ? 52  ASP B OD1   1 
ATOM   388  O OD2   . ASP A 1 52  ? 113.569 148.659 126.456 1.00 105.68 ? 52  ASP B OD2   1 
ATOM   389  N N     . TYR A 1 53  ? 112.986 149.738 129.052 1.00 109.82 ? 53  TYR B N     1 
ATOM   390  C CA    . TYR A 1 53  ? 113.534 151.047 129.390 1.00 109.82 ? 53  TYR B CA    1 
ATOM   391  C C     . TYR A 1 53  ? 112.423 152.071 129.552 1.00 109.82 ? 53  TYR B C     1 
ATOM   392  O O     . TYR A 1 53  ? 112.624 153.135 130.145 1.00 109.82 ? 53  TYR B O     1 
ATOM   393  C CB    . TYR A 1 53  ? 114.525 151.516 128.323 1.00 109.82 ? 53  TYR B CB    1 
ATOM   394  C CG    . TYR A 1 53  ? 115.871 150.840 128.395 1.00 109.82 ? 53  TYR B CG    1 
ATOM   395  C CD1   . TYR A 1 53  ? 116.827 151.252 129.307 1.00 109.82 ? 53  TYR B CD1   1 
ATOM   396  C CD2   . TYR A 1 53  ? 116.187 149.793 127.544 1.00 109.82 ? 53  TYR B CD2   1 
ATOM   397  C CE1   . TYR A 1 53  ? 118.058 150.636 129.374 1.00 109.82 ? 53  TYR B CE1   1 
ATOM   398  C CE2   . TYR A 1 53  ? 117.413 149.172 127.603 1.00 109.82 ? 53  TYR B CE2   1 
ATOM   399  C CZ    . TYR A 1 53  ? 118.345 149.596 128.519 1.00 109.82 ? 53  TYR B CZ    1 
ATOM   400  O OH    . TYR A 1 53  ? 119.570 148.973 128.575 1.00 109.82 ? 53  TYR B OH    1 
ATOM   401  N N     . SER A 1 54  ? 111.253 151.755 129.005 1.00 111.46 ? 54  SER B N     1 
ATOM   402  C CA    . SER A 1 54  ? 110.117 152.661 129.037 1.00 111.46 ? 54  SER B CA    1 
ATOM   403  C C     . SER A 1 54  ? 108.791 151.940 129.211 1.00 111.46 ? 54  SER B C     1 
ATOM   404  O O     . SER A 1 54  ? 107.752 152.605 129.264 1.00 111.46 ? 54  SER B O     1 
ATOM   405  C CB    . SER A 1 54  ? 110.072 153.508 127.755 1.00 111.46 ? 54  SER B CB    1 
ATOM   406  O OG    . SER A 1 54  ? 109.837 152.693 126.621 1.00 111.46 ? 54  SER B OG    1 
ATOM   407  N N     . GLY A 1 55  ? 108.788 150.613 129.297 1.00 104.99 ? 55  GLY B N     1 
ATOM   408  C CA    . GLY A 1 55  ? 107.565 149.845 129.390 1.00 104.99 ? 55  GLY B CA    1 
ATOM   409  C C     . GLY A 1 55  ? 107.202 149.078 128.141 1.00 104.99 ? 55  GLY B C     1 
ATOM   410  O O     . GLY A 1 55  ? 106.189 148.369 128.147 1.00 104.99 ? 55  GLY B O     1 
ATOM   411  N N     . GLY A 1 56  ? 107.987 149.193 127.071 1.00 103.16 ? 56  GLY B N     1 
ATOM   412  C CA    . GLY A 1 56  ? 107.657 148.475 125.852 1.00 103.16 ? 56  GLY B CA    1 
ATOM   413  C C     . GLY A 1 56  ? 107.775 146.972 126.016 1.00 103.16 ? 56  GLY B C     1 
ATOM   414  O O     . GLY A 1 56  ? 106.822 146.230 125.764 1.00 103.16 ? 56  GLY B O     1 
ATOM   415  N N     . HIS A 1 57  ? 108.941 146.505 126.446 1.00 98.58  ? 57  HIS B N     1 
ATOM   416  C CA    . HIS A 1 57  ? 109.214 145.084 126.587 1.00 98.58  ? 57  HIS B CA    1 
ATOM   417  C C     . HIS A 1 57  ? 109.174 144.694 128.056 1.00 98.58  ? 57  HIS B C     1 
ATOM   418  O O     . HIS A 1 57  ? 109.898 145.267 128.876 1.00 98.58  ? 57  HIS B O     1 
ATOM   419  C CB    . HIS A 1 57  ? 110.571 144.724 125.987 1.00 98.58  ? 57  HIS B CB    1 
ATOM   420  C CG    . HIS A 1 57  ? 110.833 143.254 125.931 1.00 98.58  ? 57  HIS B CG    1 
ATOM   421  N ND1   . HIS A 1 57  ? 109.824 142.324 125.813 1.00 98.58  ? 57  HIS B ND1   1 
ATOM   422  C CD2   . HIS A 1 57  ? 111.988 142.552 125.980 1.00 98.58  ? 57  HIS B CD2   1 
ATOM   423  C CE1   . HIS A 1 57  ? 110.346 141.112 125.790 1.00 98.58  ? 57  HIS B CE1   1 
ATOM   424  N NE2   . HIS A 1 57  ? 111.658 141.222 125.890 1.00 98.58  ? 57  HIS B NE2   1 
ATOM   425  N N     . THR A 1 58  ? 108.327 143.726 128.382 1.00 96.72  ? 58  THR B N     1 
ATOM   426  C CA    . THR A 1 58  ? 108.257 143.142 129.710 1.00 96.72  ? 58  THR B CA    1 
ATOM   427  C C     . THR A 1 58  ? 108.537 141.653 129.602 1.00 96.72  ? 58  THR B C     1 
ATOM   428  O O     . THR A 1 58  ? 108.078 140.995 128.664 1.00 96.72  ? 58  THR B O     1 
ATOM   429  C CB    . THR A 1 58  ? 106.890 143.364 130.346 1.00 96.72  ? 58  THR B CB    1 
ATOM   430  O OG1   . THR A 1 58  ? 105.890 142.701 129.564 1.00 96.72  ? 58  THR B OG1   1 
ATOM   431  C CG2   . THR A 1 58  ? 106.569 144.837 130.399 1.00 96.72  ? 58  THR B CG2   1 
ATOM   432  N N     . LEU A 1 59  ? 109.291 141.123 130.560 1.00 93.62  ? 59  LEU B N     1 
ATOM   433  C CA    . LEU A 1 59  ? 109.648 139.710 130.580 1.00 93.62  ? 59  LEU B CA    1 
ATOM   434  C C     . LEU A 1 59  ? 109.294 139.148 131.946 1.00 93.62  ? 59  LEU B C     1 
ATOM   435  O O     . LEU A 1 59  ? 109.964 139.452 132.936 1.00 93.62  ? 59  LEU B O     1 
ATOM   436  C CB    . LEU A 1 59  ? 111.132 139.513 130.278 1.00 93.62  ? 59  LEU B CB    1 
ATOM   437  C CG    . LEU A 1 59  ? 111.583 138.071 130.067 1.00 93.62  ? 59  LEU B CG    1 
ATOM   438  C CD1   . LEU A 1 59  ? 110.776 137.421 128.962 1.00 93.62  ? 59  LEU B CD1   1 
ATOM   439  C CD2   . LEU A 1 59  ? 113.059 138.029 129.741 1.00 93.62  ? 59  LEU B CD2   1 
ATOM   440  N N     . TYR A 1 60  ? 108.252 138.329 132.002 1.00 99.06  ? 60  TYR B N     1 
ATOM   441  C CA    . TYR A 1 60  ? 107.804 137.734 133.250 1.00 99.06  ? 60  TYR B CA    1 
ATOM   442  C C     . TYR A 1 60  ? 108.301 136.301 133.362 1.00 99.06  ? 60  TYR B C     1 
ATOM   443  O O     . TYR A 1 60  ? 108.532 135.622 132.359 1.00 99.06  ? 60  TYR B O     1 
ATOM   444  C CB    . TYR A 1 60  ? 106.280 137.752 133.351 1.00 99.06  ? 60  TYR B CB    1 
ATOM   445  C CG    . TYR A 1 60  ? 105.673 139.125 133.241 1.00 99.06  ? 60  TYR B CG    1 
ATOM   446  C CD1   . TYR A 1 60  ? 105.523 139.927 134.356 1.00 99.06  ? 60  TYR B CD1   1 
ATOM   447  C CD2   . TYR A 1 60  ? 105.243 139.616 132.020 1.00 99.06  ? 60  TYR B CD2   1 
ATOM   448  C CE1   . TYR A 1 60  ? 104.971 141.178 134.259 1.00 99.06  ? 60  TYR B CE1   1 
ATOM   449  C CE2   . TYR A 1 60  ? 104.686 140.867 131.913 1.00 99.06  ? 60  TYR B CE2   1 
ATOM   450  C CZ    . TYR A 1 60  ? 104.552 141.645 133.038 1.00 99.06  ? 60  TYR B CZ    1 
ATOM   451  O OH    . TYR A 1 60  ? 103.996 142.898 132.941 1.00 99.06  ? 60  TYR B OH    1 
ATOM   452  N N     . ALA A 1 61  ? 108.472 135.848 134.599 1.00 105.32 ? 61  ALA B N     1 
ATOM   453  C CA    . ALA A 1 61  ? 108.772 134.447 134.837 1.00 105.32 ? 61  ALA B CA    1 
ATOM   454  C C     . ALA A 1 61  ? 107.556 133.594 134.509 1.00 105.32 ? 61  ALA B C     1 
ATOM   455  O O     . ALA A 1 61  ? 106.413 133.984 134.754 1.00 105.32 ? 61  ALA B O     1 
ATOM   456  C CB    . ALA A 1 61  ? 109.193 134.225 136.287 1.00 105.32 ? 61  ALA B CB    1 
ATOM   457  N N     . ASP A 1 62  ? 107.811 132.413 133.942 1.00 109.14 ? 62  ASP B N     1 
ATOM   458  C CA    . ASP A 1 62  ? 106.716 131.535 133.549 1.00 109.14 ? 62  ASP B CA    1 
ATOM   459  C C     . ASP A 1 62  ? 105.842 131.132 134.728 1.00 109.14 ? 62  ASP B C     1 
ATOM   460  O O     . ASP A 1 62  ? 104.715 130.671 134.519 1.00 109.14 ? 62  ASP B O     1 
ATOM   461  C CB    . ASP A 1 62  ? 107.265 130.289 132.854 1.00 109.14 ? 62  ASP B CB    1 
ATOM   462  C CG    . ASP A 1 62  ? 107.669 130.556 131.418 1.00 109.14 ? 62  ASP B CG    1 
ATOM   463  O OD1   . ASP A 1 62  ? 106.923 131.265 130.711 1.00 109.14 ? 62  ASP B OD1   1 
ATOM   464  O OD2   . ASP A 1 62  ? 108.733 130.057 130.996 1.00 109.14 ? 62  ASP B OD2   1 
ATOM   465  N N     . SER A 1 63  ? 106.328 131.298 135.956 1.00 109.77 ? 63  SER B N     1 
ATOM   466  C CA    . SER A 1 63  ? 105.542 130.961 137.133 1.00 109.77 ? 63  SER B CA    1 
ATOM   467  C C     . SER A 1 63  ? 104.652 132.102 137.606 1.00 109.77 ? 63  SER B C     1 
ATOM   468  O O     . SER A 1 63  ? 103.796 131.877 138.467 1.00 109.77 ? 63  SER B O     1 
ATOM   469  C CB    . SER A 1 63  ? 106.466 130.530 138.273 1.00 109.77 ? 63  SER B CB    1 
ATOM   470  O OG    . SER A 1 63  ? 105.777 130.531 139.510 1.00 109.77 ? 63  SER B OG    1 
ATOM   471  N N     . VAL A 1 64  ? 104.828 133.311 137.075 1.00 108.70 ? 64  VAL B N     1 
ATOM   472  C CA    . VAL A 1 64  ? 104.038 134.458 137.509 1.00 108.70 ? 64  VAL B CA    1 
ATOM   473  C C     . VAL A 1 64  ? 103.398 135.137 136.306 1.00 108.70 ? 64  VAL B C     1 
ATOM   474  O O     . VAL A 1 64  ? 102.780 136.198 136.439 1.00 108.70 ? 64  VAL B O     1 
ATOM   475  C CB    . VAL A 1 64  ? 104.893 135.464 138.301 1.00 108.70 ? 64  VAL B CB    1 
ATOM   476  C CG1   . VAL A 1 64  ? 105.614 134.771 139.442 1.00 108.70 ? 64  VAL B CG1   1 
ATOM   477  C CG2   . VAL A 1 64  ? 105.881 136.155 137.383 1.00 108.70 ? 64  VAL B CG2   1 
ATOM   478  N N     . LYS A 1 65  ? 103.545 134.535 135.128 1.00 111.37 ? 65  LYS B N     1 
ATOM   479  C CA    . LYS A 1 65  ? 103.008 135.135 133.915 1.00 111.37 ? 65  LYS B CA    1 
ATOM   480  C C     . LYS A 1 65  ? 101.493 135.256 134.003 1.00 111.37 ? 65  LYS B C     1 
ATOM   481  O O     . LYS A 1 65  ? 100.798 134.312 134.389 1.00 111.37 ? 65  LYS B O     1 
ATOM   482  C CB    . LYS A 1 65  ? 103.403 134.308 132.693 1.00 111.37 ? 65  LYS B CB    1 
ATOM   483  C CG    . LYS A 1 65  ? 103.017 134.942 131.369 1.00 111.37 ? 65  LYS B CG    1 
ATOM   484  C CD    . LYS A 1 65  ? 103.581 134.158 130.197 1.00 111.37 ? 65  LYS B CD    1 
ATOM   485  C CE    . LYS A 1 65  ? 102.915 134.563 128.892 1.00 111.37 ? 65  LYS B CE    1 
ATOM   486  N NZ    . LYS A 1 65  ? 103.017 136.028 128.650 1.00 111.37 ? 65  LYS B NZ    1 
ATOM   487  N N     . GLY A 1 66  ? 100.982 136.433 133.647 1.00 113.65 ? 66  GLY B N     1 
ATOM   488  C CA    . GLY A 1 66  ? 99.572  136.728 133.725 1.00 113.65 ? 66  GLY B CA    1 
ATOM   489  C C     . GLY A 1 66  ? 99.125  137.280 135.063 1.00 113.65 ? 66  GLY B C     1 
ATOM   490  O O     . GLY A 1 66  ? 98.233  138.133 135.105 1.00 113.65 ? 66  GLY B O     1 
ATOM   491  N N     . ARG A 1 67  ? 99.726  136.815 136.158 1.00 115.40 ? 67  ARG B N     1 
ATOM   492  C CA    . ARG A 1 67  ? 99.371  137.317 137.481 1.00 115.40 ? 67  ARG B CA    1 
ATOM   493  C C     . ARG A 1 67  ? 100.051 138.651 137.762 1.00 115.40 ? 67  ARG B C     1 
ATOM   494  O O     . ARG A 1 67  ? 99.386  139.658 138.028 1.00 115.40 ? 67  ARG B O     1 
ATOM   495  C CB    . ARG A 1 67  ? 99.750  136.293 138.552 1.00 115.40 ? 67  ARG B CB    1 
ATOM   496  C CG    . ARG A 1 67  ? 98.747  135.175 138.744 1.00 115.40 ? 67  ARG B CG    1 
ATOM   497  C CD    . ARG A 1 67  ? 99.172  134.278 139.889 1.00 115.40 ? 67  ARG B CD    1 
ATOM   498  N NE    . ARG A 1 67  ? 100.441 133.613 139.611 1.00 115.40 ? 67  ARG B NE    1 
ATOM   499  C CZ    . ARG A 1 67  ? 101.303 133.232 140.547 1.00 115.40 ? 67  ARG B CZ    1 
ATOM   500  N NH1   . ARG A 1 67  ? 101.034 133.454 141.826 1.00 115.40 ? 67  ARG B NH1   1 
ATOM   501  N NH2   . ARG A 1 67  ? 102.434 132.633 140.205 1.00 115.40 ? 67  ARG B NH2   1 
ATOM   502  N N     . PHE A 1 68  ? 101.376 138.673 137.711 1.00 112.04 ? 68  PHE B N     1 
ATOM   503  C CA    . PHE A 1 68  ? 102.141 139.862 138.044 1.00 112.04 ? 68  PHE B CA    1 
ATOM   504  C C     . PHE A 1 68  ? 102.283 140.766 136.829 1.00 112.04 ? 68  PHE B C     1 
ATOM   505  O O     . PHE A 1 68  ? 102.290 140.306 135.685 1.00 112.04 ? 68  PHE B O     1 
ATOM   506  C CB    . PHE A 1 68  ? 103.529 139.490 138.565 1.00 112.04 ? 68  PHE B CB    1 
ATOM   507  C CG    . PHE A 1 68  ? 103.521 138.798 139.899 1.00 112.04 ? 68  PHE B CG    1 
ATOM   508  C CD1   . PHE A 1 68  ? 102.336 138.498 140.541 1.00 112.04 ? 68  PHE B CD1   1 
ATOM   509  C CD2   . PHE A 1 68  ? 104.709 138.456 140.513 1.00 112.04 ? 68  PHE B CD2   1 
ATOM   510  C CE1   . PHE A 1 68  ? 102.339 137.864 141.761 1.00 112.04 ? 68  PHE B CE1   1 
ATOM   511  C CE2   . PHE A 1 68  ? 104.718 137.826 141.733 1.00 112.04 ? 68  PHE B CE2   1 
ATOM   512  C CZ    . PHE A 1 68  ? 103.533 137.529 142.359 1.00 112.04 ? 68  PHE B CZ    1 
ATOM   513  N N     . THR A 1 69  ? 102.406 142.064 137.089 1.00 106.91 ? 69  THR B N     1 
ATOM   514  C CA    . THR A 1 69  ? 102.686 143.034 136.041 1.00 106.91 ? 69  THR B CA    1 
ATOM   515  C C     . THR A 1 69  ? 103.656 144.078 136.570 1.00 106.91 ? 69  THR B C     1 
ATOM   516  O O     . THR A 1 69  ? 103.481 144.604 137.672 1.00 106.91 ? 69  THR B O     1 
ATOM   517  C CB    . THR A 1 69  ? 101.400 143.693 135.510 1.00 106.91 ? 69  THR B CB    1 
ATOM   518  O OG1   . THR A 1 69  ? 101.727 144.615 134.463 1.00 106.91 ? 69  THR B OG1   1 
ATOM   519  C CG2   . THR A 1 69  ? 100.635 144.409 136.606 1.00 106.91 ? 69  THR B CG2   1 
ATOM   520  N N     . ILE A 1 70  ? 104.696 144.348 135.788 1.00 102.90 ? 70  ILE B N     1 
ATOM   521  C CA    . ILE A 1 70  ? 105.754 145.278 136.162 1.00 102.90 ? 70  ILE B CA    1 
ATOM   522  C C     . ILE A 1 70  ? 105.580 146.547 135.345 1.00 102.90 ? 70  ILE B C     1 
ATOM   523  O O     . ILE A 1 70  ? 105.318 146.486 134.138 1.00 102.90 ? 70  ILE B O     1 
ATOM   524  C CB    . ILE A 1 70  ? 107.146 144.660 135.949 1.00 102.90 ? 70  ILE B CB    1 
ATOM   525  C CG1   . ILE A 1 70  ? 108.241 145.670 136.281 1.00 102.90 ? 70  ILE B CG1   1 
ATOM   526  C CG2   . ILE A 1 70  ? 107.298 144.149 134.525 1.00 102.90 ? 70  ILE B CG2   1 
ATOM   527  C CD1   . ILE A 1 70  ? 109.632 145.103 136.181 1.00 102.90 ? 70  ILE B CD1   1 
ATOM   528  N N     . SER A 1 71  ? 105.706 147.693 136.002 1.00 106.22 ? 71  SER B N     1 
ATOM   529  C CA    . SER A 1 71  ? 105.538 148.977 135.343 1.00 106.22 ? 71  SER B CA    1 
ATOM   530  C C     . SER A 1 71  ? 106.439 149.998 136.013 1.00 106.22 ? 71  SER B C     1 
ATOM   531  O O     . SER A 1 71  ? 106.615 149.974 137.233 1.00 106.22 ? 71  SER B O     1 
ATOM   532  C CB    . SER A 1 71  ? 104.082 149.443 135.398 1.00 106.22 ? 71  SER B CB    1 
ATOM   533  O OG    . SER A 1 71  ? 103.683 149.714 136.731 1.00 106.22 ? 71  SER B OG    1 
ATOM   534  N N     . ARG A 1 72  ? 107.006 150.890 135.214 1.00 111.39 ? 72  ARG B N     1 
ATOM   535  C CA    . ARG A 1 72  ? 107.918 151.909 135.706 1.00 111.39 ? 72  ARG B CA    1 
ATOM   536  C C     . ARG A 1 72  ? 107.330 153.292 135.453 1.00 111.39 ? 72  ARG B C     1 
ATOM   537  O O     . ARG A 1 72  ? 106.271 153.444 134.844 1.00 111.39 ? 72  ARG B O     1 
ATOM   538  C CB    . ARG A 1 72  ? 109.292 151.782 135.043 1.00 111.39 ? 72  ARG B CB    1 
ATOM   539  C CG    . ARG A 1 72  ? 109.278 152.001 133.545 1.00 111.39 ? 72  ARG B CG    1 
ATOM   540  C CD    . ARG A 1 72  ? 110.577 151.546 132.919 1.00 111.39 ? 72  ARG B CD    1 
ATOM   541  N NE    . ARG A 1 72  ? 111.726 152.215 133.514 1.00 111.39 ? 72  ARG B NE    1 
ATOM   542  C CZ    . ARG A 1 72  ? 112.977 151.788 133.400 1.00 111.39 ? 72  ARG B CZ    1 
ATOM   543  N NH1   . ARG A 1 72  ? 113.241 150.686 132.713 1.00 111.39 ? 72  ARG B NH1   1 
ATOM   544  N NH2   . ARG A 1 72  ? 113.964 152.458 133.976 1.00 111.39 ? 72  ARG B NH2   1 
ATOM   545  N N     . ASP A 1 73  ? 108.043 154.309 135.933 1.00 120.24 ? 73  ASP B N     1 
ATOM   546  C CA    . ASP A 1 73  ? 107.659 155.700 135.708 1.00 120.24 ? 73  ASP B CA    1 
ATOM   547  C C     . ASP A 1 73  ? 108.965 156.487 135.637 1.00 120.24 ? 73  ASP B C     1 
ATOM   548  O O     . ASP A 1 73  ? 109.527 156.851 136.672 1.00 120.24 ? 73  ASP B O     1 
ATOM   549  C CB    . ASP A 1 73  ? 106.744 156.199 136.821 1.00 120.24 ? 73  ASP B CB    1 
ATOM   550  C CG    . ASP A 1 73  ? 106.298 157.645 136.633 1.00 120.24 ? 73  ASP B CG    1 
ATOM   551  O OD1   . ASP A 1 73  ? 105.166 157.960 137.052 1.00 120.24 ? 73  ASP B OD1   1 
ATOM   552  O OD2   . ASP A 1 73  ? 107.057 158.472 136.085 1.00 120.24 ? 73  ASP B OD2   1 
ATOM   553  N N     . ASN A 1 74  ? 109.444 156.735 134.418 1.00 120.52 ? 74  ASN B N     1 
ATOM   554  C CA    . ASN A 1 74  ? 110.726 157.414 134.263 1.00 120.52 ? 74  ASN B CA    1 
ATOM   555  C C     . ASN A 1 74  ? 110.713 158.799 134.900 1.00 120.52 ? 74  ASN B C     1 
ATOM   556  O O     . ASN A 1 74  ? 111.761 159.285 135.341 1.00 120.52 ? 74  ASN B O     1 
ATOM   557  C CB    . ASN A 1 74  ? 111.096 157.505 132.781 1.00 120.52 ? 74  ASN B CB    1 
ATOM   558  C CG    . ASN A 1 74  ? 111.333 156.141 132.152 1.00 120.52 ? 74  ASN B CG    1 
ATOM   559  O OD1   . ASN A 1 74  ? 110.596 155.714 131.261 1.00 120.52 ? 74  ASN B OD1   1 
ATOM   560  N ND2   . ASN A 1 74  ? 112.371 155.452 132.612 1.00 120.52 ? 74  ASN B ND2   1 
ATOM   561  N N     . SER A 1 75  ? 109.546 159.444 134.965 1.00 122.11 ? 75  SER B N     1 
ATOM   562  C CA    . SER A 1 75  ? 109.442 160.749 135.610 1.00 122.11 ? 75  SER B CA    1 
ATOM   563  C C     . SER A 1 75  ? 109.497 160.622 137.127 1.00 122.11 ? 75  SER B C     1 
ATOM   564  O O     . SER A 1 75  ? 110.395 161.172 137.772 1.00 122.11 ? 75  SER B O     1 
ATOM   565  C CB    . SER A 1 75  ? 108.146 161.440 135.179 1.00 122.11 ? 75  SER B CB    1 
ATOM   566  O OG    . SER A 1 75  ? 107.015 160.656 135.529 1.00 122.11 ? 75  SER B OG    1 
ATOM   567  N N     . LYS A 1 76  ? 108.545 159.895 137.706 1.00 123.75 ? 76  LYS B N     1 
ATOM   568  C CA    . LYS A 1 76  ? 108.523 159.613 139.138 1.00 123.75 ? 76  LYS B CA    1 
ATOM   569  C C     . LYS A 1 76  ? 109.380 158.376 139.367 1.00 123.75 ? 76  LYS B C     1 
ATOM   570  O O     . LYS A 1 76  ? 108.907 157.248 139.211 1.00 123.75 ? 76  LYS B O     1 
ATOM   571  C CB    . LYS A 1 76  ? 107.094 159.392 139.619 1.00 123.75 ? 76  LYS B CB    1 
ATOM   572  C CG    . LYS A 1 76  ? 106.964 159.192 141.118 1.00 123.75 ? 76  LYS B CG    1 
ATOM   573  C CD    . LYS A 1 76  ? 105.549 158.797 141.497 1.00 123.75 ? 76  LYS B CD    1 
ATOM   574  C CE    . LYS A 1 76  ? 104.586 159.967 141.362 1.00 123.75 ? 76  LYS B CE    1 
ATOM   575  N NZ    . LYS A 1 76  ? 103.213 159.630 141.847 1.00 123.75 ? 76  LYS B NZ    1 
ATOM   576  N N     . ASN A 1 77  ? 110.634 158.581 139.780 1.00 121.65 ? 77  ASN B N     1 
ATOM   577  C CA    . ASN A 1 77  ? 111.597 157.487 139.774 1.00 121.65 ? 77  ASN B CA    1 
ATOM   578  C C     . ASN A 1 77  ? 111.173 156.396 140.745 1.00 121.65 ? 77  ASN B C     1 
ATOM   579  O O     . ASN A 1 77  ? 111.366 156.517 141.958 1.00 121.65 ? 77  ASN B O     1 
ATOM   580  C CB    . ASN A 1 77  ? 112.991 158.004 140.125 1.00 121.65 ? 77  ASN B CB    1 
ATOM   581  C CG    . ASN A 1 77  ? 113.784 158.405 138.904 1.00 121.65 ? 77  ASN B CG    1 
ATOM   582  O OD1   . ASN A 1 77  ? 113.231 158.564 137.815 1.00 121.65 ? 77  ASN B OD1   1 
ATOM   583  N ND2   . ASN A 1 77  ? 115.088 158.578 139.077 1.00 121.65 ? 77  ASN B ND2   1 
ATOM   584  N N     . THR A 1 78  ? 110.609 155.320 140.203 1.00 117.18 ? 78  THR B N     1 
ATOM   585  C CA    . THR A 1 78  ? 110.076 154.214 140.983 1.00 117.18 ? 78  THR B CA    1 
ATOM   586  C C     . THR A 1 78  ? 109.649 153.119 140.021 1.00 117.18 ? 78  THR B C     1 
ATOM   587  O O     . THR A 1 78  ? 109.026 153.407 138.998 1.00 117.18 ? 78  THR B O     1 
ATOM   588  C CB    . THR A 1 78  ? 108.883 154.658 141.842 1.00 117.18 ? 78  THR B CB    1 
ATOM   589  O OG1   . THR A 1 78  ? 109.349 155.453 142.940 1.00 117.18 ? 78  THR B OG1   1 
ATOM   590  C CG2   . THR A 1 78  ? 108.124 153.459 142.382 1.00 117.18 ? 78  THR B CG2   1 
ATOM   591  N N     . VAL A 1 79  ? 109.988 151.876 140.343 1.00 110.87 ? 79  VAL B N     1 
ATOM   592  C CA    . VAL A 1 79  ? 109.533 150.716 139.587 1.00 110.87 ? 79  VAL B CA    1 
ATOM   593  C C     . VAL A 1 79  ? 108.474 150.002 140.408 1.00 110.87 ? 79  VAL B C     1 
ATOM   594  O O     . VAL A 1 79  ? 108.669 149.748 141.602 1.00 110.87 ? 79  VAL B O     1 
ATOM   595  C CB    . VAL A 1 79  ? 110.693 149.772 139.238 1.00 110.87 ? 79  VAL B CB    1 
ATOM   596  C CG1   . VAL A 1 79  ? 110.161 148.445 138.747 1.00 110.87 ? 79  VAL B CG1   1 
ATOM   597  C CG2   . VAL A 1 79  ? 111.549 150.397 138.182 1.00 110.87 ? 79  VAL B CG2   1 
ATOM   598  N N     . TYR A 1 80  ? 107.356 149.686 139.772 1.00 110.08 ? 80  TYR B N     1 
ATOM   599  C CA    . TYR A 1 80  ? 106.249 149.020 140.433 1.00 110.08 ? 80  TYR B CA    1 
ATOM   600  C C     . TYR A 1 80  ? 106.194 147.556 140.022 1.00 110.08 ? 80  TYR B C     1 
ATOM   601  O O     . TYR A 1 80  ? 106.714 147.164 138.975 1.00 110.08 ? 80  TYR B O     1 
ATOM   602  C CB    . TYR A 1 80  ? 104.923 149.701 140.088 1.00 110.08 ? 80  TYR B CB    1 
ATOM   603  C CG    . TYR A 1 80  ? 104.696 151.019 140.791 1.00 110.08 ? 80  TYR B CG    1 
ATOM   604  C CD1   . TYR A 1 80  ? 104.063 151.069 142.024 1.00 110.08 ? 80  TYR B CD1   1 
ATOM   605  C CD2   . TYR A 1 80  ? 105.106 152.213 140.217 1.00 110.08 ? 80  TYR B CD2   1 
ATOM   606  C CE1   . TYR A 1 80  ? 103.851 152.270 142.669 1.00 110.08 ? 80  TYR B CE1   1 
ATOM   607  C CE2   . TYR A 1 80  ? 104.898 153.419 140.854 1.00 110.08 ? 80  TYR B CE2   1 
ATOM   608  C CZ    . TYR A 1 80  ? 104.270 153.441 142.080 1.00 110.08 ? 80  TYR B CZ    1 
ATOM   609  O OH    . TYR A 1 80  ? 104.061 154.640 142.719 1.00 110.08 ? 80  TYR B OH    1 
ATOM   610  N N     . LEU A 1 81  ? 105.560 146.747 140.867 1.00 109.46 ? 81  LEU B N     1 
ATOM   611  C CA    . LEU A 1 81  ? 105.265 145.352 140.548 1.00 109.46 ? 81  LEU B CA    1 
ATOM   612  C C     . LEU A 1 81  ? 103.909 145.040 141.169 1.00 109.46 ? 81  LEU B C     1 
ATOM   613  O O     . LEU A 1 81  ? 103.817 144.775 142.370 1.00 109.46 ? 81  LEU B O     1 
ATOM   614  C CB    . LEU A 1 81  ? 106.342 144.407 141.062 1.00 109.46 ? 81  LEU B CB    1 
ATOM   615  C CG    . LEU A 1 81  ? 106.154 142.934 140.691 1.00 109.46 ? 81  LEU B CG    1 
ATOM   616  C CD1   . LEU A 1 81  ? 106.803 142.623 139.354 1.00 109.46 ? 81  LEU B CD1   1 
ATOM   617  C CD2   . LEU A 1 81  ? 106.710 142.033 141.778 1.00 109.46 ? 81  LEU B CD2   1 
ATOM   618  N N     . GLN A 1 82  ? 102.864 145.078 140.349 1.00 114.73 ? 82  GLN B N     1 
ATOM   619  C CA    . GLN A 1 82  ? 101.512 144.811 140.823 1.00 114.73 ? 82  GLN B CA    1 
ATOM   620  C C     . GLN A 1 82  ? 101.310 143.303 140.884 1.00 114.73 ? 82  GLN B C     1 
ATOM   621  O O     . GLN A 1 82  ? 101.205 142.639 139.848 1.00 114.73 ? 82  GLN B O     1 
ATOM   622  C CB    . GLN A 1 82  ? 100.485 145.472 139.911 1.00 114.73 ? 82  GLN B CB    1 
ATOM   623  C CG    . GLN A 1 82  ? 99.066  145.420 140.436 1.00 114.73 ? 82  GLN B CG    1 
ATOM   624  C CD    . GLN A 1 82  ? 98.885  146.249 141.684 1.00 114.73 ? 82  GLN B CD    1 
ATOM   625  O OE1   . GLN A 1 82  ? 99.339  147.388 141.755 1.00 114.73 ? 82  GLN B OE1   1 
ATOM   626  N NE2   . GLN A 1 82  ? 98.219  145.681 142.678 1.00 114.73 ? 82  GLN B NE2   1 
ATOM   627  N N     . MET A 1 83  ? 101.262 142.763 142.095 1.00 118.23 ? 83  MET B N     1 
ATOM   628  C CA    . MET A 1 83  ? 101.106 141.335 142.313 1.00 118.23 ? 83  MET B CA    1 
ATOM   629  C C     . MET A 1 83  ? 99.642  141.020 142.583 1.00 118.23 ? 83  MET B C     1 
ATOM   630  O O     . MET A 1 83  ? 99.029  141.614 143.474 1.00 118.23 ? 83  MET B O     1 
ATOM   631  C CB    . MET A 1 83  ? 101.980 140.869 143.476 1.00 118.23 ? 83  MET B CB    1 
ATOM   632  C CG    . MET A 1 83  ? 103.467 141.023 143.214 1.00 118.23 ? 83  MET B CG    1 
ATOM   633  S SD    . MET A 1 83  ? 104.506 140.251 144.466 1.00 118.23 ? 83  MET B SD    1 
ATOM   634  C CE    . MET A 1 83  ? 104.202 141.318 145.867 1.00 118.23 ? 83  MET B CE    1 
ATOM   635  N N     . ASN A 1 84  ? 99.087  140.089 141.810 1.00 122.15 ? 84  ASN B N     1 
ATOM   636  C CA    . ASN A 1 84  ? 97.694  139.692 141.942 1.00 122.15 ? 84  ASN B CA    1 
ATOM   637  C C     . ASN A 1 84  ? 97.599  138.175 141.970 1.00 122.15 ? 84  ASN B C     1 
ATOM   638  O O     . ASN A 1 84  ? 98.416  137.478 141.365 1.00 122.15 ? 84  ASN B O     1 
ATOM   639  C CB    . ASN A 1 84  ? 96.843  140.248 140.798 1.00 122.15 ? 84  ASN B CB    1 
ATOM   640  C CG    . ASN A 1 84  ? 96.683  141.752 140.873 1.00 122.15 ? 84  ASN B CG    1 
ATOM   641  O OD1   . ASN A 1 84  ? 96.603  142.324 141.959 1.00 122.15 ? 84  ASN B OD1   1 
ATOM   642  N ND2   . ASN A 1 84  ? 96.635  142.401 139.717 1.00 122.15 ? 84  ASN B ND2   1 
ATOM   643  N N     . SER A 1 85  ? 96.585  137.674 142.675 1.00 124.86 ? 85  SER B N     1 
ATOM   644  C CA    . SER A 1 85  ? 96.370  136.238 142.834 1.00 124.86 ? 85  SER B CA    1 
ATOM   645  C C     . SER A 1 85  ? 97.598  135.567 143.444 1.00 124.86 ? 85  SER B C     1 
ATOM   646  O O     . SER A 1 85  ? 98.116  134.575 142.929 1.00 124.86 ? 85  SER B O     1 
ATOM   647  C CB    . SER A 1 85  ? 95.989  135.582 141.504 1.00 124.86 ? 85  SER B CB    1 
ATOM   648  O OG    . SER A 1 85  ? 94.739  136.057 141.030 1.00 124.86 ? 85  SER B OG    1 
ATOM   649  N N     . LEU A 1 86  ? 98.070  136.131 144.554 1.00 126.58 ? 86  LEU B N     1 
ATOM   650  C CA    . LEU A 1 86  ? 99.256  135.606 145.216 1.00 126.58 ? 86  LEU B CA    1 
ATOM   651  C C     . LEU A 1 86  ? 99.009  134.193 145.725 1.00 126.58 ? 86  LEU B C     1 
ATOM   652  O O     . LEU A 1 86  ? 98.051  133.934 146.457 1.00 126.58 ? 86  LEU B O     1 
ATOM   653  C CB    . LEU A 1 86  ? 99.661  136.515 146.377 1.00 126.58 ? 86  LEU B CB    1 
ATOM   654  C CG    . LEU A 1 86  ? 100.191 137.905 146.038 1.00 126.58 ? 86  LEU B CG    1 
ATOM   655  C CD1   . LEU A 1 86  ? 100.365 138.726 147.301 1.00 126.58 ? 86  LEU B CD1   1 
ATOM   656  C CD2   . LEU A 1 86  ? 101.508 137.784 145.299 1.00 126.58 ? 86  LEU B CD2   1 
ATOM   657  N N     . ASN A 1 87  ? 99.885  133.279 145.342 1.00 125.53 ? 87  ASN B N     1 
ATOM   658  C CA    . ASN A 1 87  ? 99.838  131.908 145.816 1.00 125.53 ? 87  ASN B CA    1 
ATOM   659  C C     . ASN A 1 87  ? 100.783 131.732 146.994 1.00 125.53 ? 87  ASN B C     1 
ATOM   660  O O     . ASN A 1 87  ? 101.731 132.505 147.160 1.00 125.53 ? 87  ASN B O     1 
ATOM   661  C CB    . ASN A 1 87  ? 100.223 130.930 144.697 1.00 125.53 ? 87  ASN B CB    1 
ATOM   662  C CG    . ASN A 1 87  ? 99.186  130.871 143.593 1.00 125.53 ? 87  ASN B CG    1 
ATOM   663  O OD1   . ASN A 1 87  ? 97.984  130.886 143.856 1.00 125.53 ? 87  ASN B OD1   1 
ATOM   664  N ND2   . ASN A 1 87  ? 99.647  130.798 142.351 1.00 125.53 ? 87  ASN B ND2   1 
ATOM   665  N N     . PRO A 1 88  ? 100.548 130.735 147.849 1.00 126.69 ? 88  PRO B N     1 
ATOM   666  C CA    . PRO A 1 88  ? 101.511 130.459 148.926 1.00 126.69 ? 88  PRO B CA    1 
ATOM   667  C C     . PRO A 1 88  ? 102.914 130.183 148.419 1.00 126.69 ? 88  PRO B C     1 
ATOM   668  O O     . PRO A 1 88  ? 103.876 130.376 149.170 1.00 126.69 ? 88  PRO B O     1 
ATOM   669  C CB    . PRO A 1 88  ? 100.913 129.231 149.623 1.00 126.69 ? 88  PRO B CB    1 
ATOM   670  C CG    . PRO A 1 88  ? 99.454  129.325 149.346 1.00 126.69 ? 88  PRO B CG    1 
ATOM   671  C CD    . PRO A 1 88  ? 99.339  129.904 147.964 1.00 126.69 ? 88  PRO B CD    1 
ATOM   672  N N     . GLU A 1 89  ? 103.061 129.744 147.168 1.00 123.74 ? 89  GLU B N     1 
ATOM   673  C CA    . GLU A 1 89  ? 104.378 129.552 146.578 1.00 123.74 ? 89  GLU B CA    1 
ATOM   674  C C     . GLU A 1 89  ? 105.092 130.867 146.298 1.00 123.74 ? 89  GLU B C     1 
ATOM   675  O O     . GLU A 1 89  ? 106.294 130.849 146.012 1.00 123.74 ? 89  GLU B O     1 
ATOM   676  C CB    . GLU A 1 89  ? 104.254 128.749 145.282 1.00 123.74 ? 89  GLU B CB    1 
ATOM   677  C CG    . GLU A 1 89  ? 103.802 127.311 145.479 1.00 123.74 ? 89  GLU B CG    1 
ATOM   678  C CD    . GLU A 1 89  ? 104.253 126.394 144.358 1.00 123.74 ? 89  GLU B CD    1 
ATOM   679  O OE1   . GLU A 1 89  ? 104.815 125.319 144.657 1.00 123.74 ? 89  GLU B OE1   1 
ATOM   680  O OE2   . GLU A 1 89  ? 104.043 126.746 143.178 1.00 123.74 ? 89  GLU B OE2   1 
ATOM   681  N N     . ASP A 1 90  ? 104.391 131.998 146.375 1.00 119.65 ? 90  ASP B N     1 
ATOM   682  C CA    . ASP A 1 90  ? 104.983 133.292 146.063 1.00 119.65 ? 90  ASP B CA    1 
ATOM   683  C C     . ASP A 1 90  ? 105.763 133.891 147.222 1.00 119.65 ? 90  ASP B C     1 
ATOM   684  O O     . ASP A 1 90  ? 106.494 134.863 147.009 1.00 119.65 ? 90  ASP B O     1 
ATOM   685  C CB    . ASP A 1 90  ? 103.898 134.281 145.629 1.00 119.65 ? 90  ASP B CB    1 
ATOM   686  C CG    . ASP A 1 90  ? 103.472 134.085 144.191 1.00 119.65 ? 90  ASP B CG    1 
ATOM   687  O OD1   . ASP A 1 90  ? 104.268 133.534 143.404 1.00 119.65 ? 90  ASP B OD1   1 
ATOM   688  O OD2   . ASP A 1 90  ? 102.341 134.486 143.845 1.00 119.65 ? 90  ASP B OD2   1 
ATOM   689  N N     . THR A 1 91  ? 105.621 133.353 148.431 1.00 118.05 ? 91  THR B N     1 
ATOM   690  C CA    . THR A 1 91  ? 106.283 133.941 149.587 1.00 118.05 ? 91  THR B CA    1 
ATOM   691  C C     . THR A 1 91  ? 107.797 133.917 149.418 1.00 118.05 ? 91  THR B C     1 
ATOM   692  O O     . THR A 1 91  ? 108.389 132.882 149.098 1.00 118.05 ? 91  THR B O     1 
ATOM   693  C CB    . THR A 1 91  ? 105.860 133.216 150.871 1.00 118.05 ? 91  THR B CB    1 
ATOM   694  O OG1   . THR A 1 91  ? 106.399 133.898 152.008 1.00 118.05 ? 91  THR B OG1   1 
ATOM   695  C CG2   . THR A 1 91  ? 106.305 131.755 150.882 1.00 118.05 ? 91  THR B CG2   1 
ATOM   696  N N     . ALA A 1 92  ? 108.414 135.084 149.597 1.00 111.72 ? 92  ALA B N     1 
ATOM   697  C CA    . ALA A 1 92  ? 109.857 135.256 149.487 1.00 111.72 ? 92  ALA B CA    1 
ATOM   698  C C     . ALA A 1 92  ? 110.231 136.683 149.852 1.00 111.72 ? 92  ALA B C     1 
ATOM   699  O O     . ALA A 1 92  ? 109.355 137.505 150.138 1.00 111.72 ? 92  ALA B O     1 
ATOM   700  C CB    . ALA A 1 92  ? 110.348 134.935 148.074 1.00 111.72 ? 92  ALA B CB    1 
ATOM   701  N N     . VAL A 1 93  ? 111.522 136.990 149.842 1.00 108.72 ? 93  VAL B N     1 
ATOM   702  C CA    . VAL A 1 93  ? 112.000 138.362 149.941 1.00 108.72 ? 93  VAL B CA    1 
ATOM   703  C C     . VAL A 1 93  ? 112.277 138.865 148.528 1.00 108.72 ? 93  VAL B C     1 
ATOM   704  O O     . VAL A 1 93  ? 113.123 138.317 147.811 1.00 108.72 ? 93  VAL B O     1 
ATOM   705  C CB    . VAL A 1 93  ? 113.229 138.472 150.860 1.00 108.72 ? 93  VAL B CB    1 
ATOM   706  C CG1   . VAL A 1 93  ? 114.381 137.611 150.374 1.00 108.72 ? 93  VAL B CG1   1 
ATOM   707  C CG2   . VAL A 1 93  ? 113.669 139.920 150.970 1.00 108.72 ? 93  VAL B CG2   1 
ATOM   708  N N     . TYR A 1 94  ? 111.530 139.881 148.110 1.00 106.50 ? 94  TYR B N     1 
ATOM   709  C CA    . TYR A 1 94  ? 111.580 140.369 146.739 1.00 106.50 ? 94  TYR B CA    1 
ATOM   710  C C     . TYR A 1 94  ? 112.607 141.486 146.632 1.00 106.50 ? 94  TYR B C     1 
ATOM   711  O O     . TYR A 1 94  ? 112.518 142.488 147.349 1.00 106.50 ? 94  TYR B O     1 
ATOM   712  C CB    . TYR A 1 94  ? 110.205 140.860 146.295 1.00 106.50 ? 94  TYR B CB    1 
ATOM   713  C CG    . TYR A 1 94  ? 109.250 139.752 145.931 1.00 106.50 ? 94  TYR B CG    1 
ATOM   714  C CD1   . TYR A 1 94  ? 109.082 139.362 144.614 1.00 106.50 ? 94  TYR B CD1   1 
ATOM   715  C CD2   . TYR A 1 94  ? 108.518 139.094 146.906 1.00 106.50 ? 94  TYR B CD2   1 
ATOM   716  C CE1   . TYR A 1 94  ? 108.212 138.352 144.280 1.00 106.50 ? 94  TYR B CE1   1 
ATOM   717  C CE2   . TYR A 1 94  ? 107.646 138.081 146.580 1.00 106.50 ? 94  TYR B CE2   1 
ATOM   718  C CZ    . TYR A 1 94  ? 107.498 137.715 145.266 1.00 106.50 ? 94  TYR B CZ    1 
ATOM   719  O OH    . TYR A 1 94  ? 106.629 136.705 144.936 1.00 106.50 ? 94  TYR B OH    1 
ATOM   720  N N     . TYR A 1 95  ? 113.572 141.316 145.738 1.00 105.22 ? 95  TYR B N     1 
ATOM   721  C CA    . TYR A 1 95  ? 114.608 142.308 145.508 1.00 105.22 ? 95  TYR B CA    1 
ATOM   722  C C     . TYR A 1 95  ? 114.328 143.056 144.216 1.00 105.22 ? 95  TYR B C     1 
ATOM   723  O O     . TYR A 1 95  ? 113.876 142.467 143.232 1.00 105.22 ? 95  TYR B O     1 
ATOM   724  C CB    . TYR A 1 95  ? 115.989 141.659 145.423 1.00 105.22 ? 95  TYR B CB    1 
ATOM   725  C CG    . TYR A 1 95  ? 116.388 140.868 146.641 1.00 105.22 ? 95  TYR B CG    1 
ATOM   726  C CD1   . TYR A 1 95  ? 117.078 141.466 147.684 1.00 105.22 ? 95  TYR B CD1   1 
ATOM   727  C CD2   . TYR A 1 95  ? 116.086 139.521 146.743 1.00 105.22 ? 95  TYR B CD2   1 
ATOM   728  C CE1   . TYR A 1 95  ? 117.447 140.745 148.798 1.00 105.22 ? 95  TYR B CE1   1 
ATOM   729  C CE2   . TYR A 1 95  ? 116.452 138.793 147.848 1.00 105.22 ? 95  TYR B CE2   1 
ATOM   730  C CZ    . TYR A 1 95  ? 117.131 139.409 148.875 1.00 105.22 ? 95  TYR B CZ    1 
ATOM   731  O OH    . TYR A 1 95  ? 117.498 138.683 149.983 1.00 105.22 ? 95  TYR B OH    1 
ATOM   732  N N     . CYS A 1 96  ? 114.601 144.351 144.223 1.00 107.79 ? 96  CYS B N     1 
ATOM   733  C CA    . CYS A 1 96  ? 114.564 145.123 142.996 1.00 107.79 ? 96  CYS B CA    1 
ATOM   734  C C     . CYS A 1 96  ? 115.967 145.232 142.415 1.00 107.79 ? 96  CYS B C     1 
ATOM   735  O O     . CYS A 1 96  ? 116.929 145.561 143.109 1.00 107.79 ? 96  CYS B O     1 
ATOM   736  C CB    . CYS A 1 96  ? 113.986 146.513 143.248 1.00 107.79 ? 96  CYS B CB    1 
ATOM   737  S SG    . CYS A 1 96  ? 113.892 147.539 141.771 1.00 107.79 ? 96  CYS B SG    1 
ATOM   738  N N     . ALA A 1 97  ? 116.075 144.954 141.121 1.00 102.42 ? 97  ALA B N     1 
ATOM   739  C CA    . ALA A 1 97  ? 117.373 144.960 140.470 1.00 102.42 ? 97  ALA B CA    1 
ATOM   740  C C     . ALA A 1 97  ? 117.380 146.039 139.403 1.00 102.42 ? 97  ALA B C     1 
ATOM   741  O O     . ALA A 1 97  ? 116.326 146.478 138.938 1.00 102.42 ? 97  ALA B O     1 
ATOM   742  C CB    . ALA A 1 97  ? 117.708 143.596 139.863 1.00 102.42 ? 97  ALA B CB    1 
ATOM   743  N N     . ALA A 1 98  ? 118.580 146.464 139.021 1.00 104.32 ? 98  ALA B N     1 
ATOM   744  C CA    . ALA A 1 98  ? 118.748 147.583 138.100 1.00 104.32 ? 98  ALA B CA    1 
ATOM   745  C C     . ALA A 1 98  ? 120.059 147.405 137.355 1.00 104.32 ? 98  ALA B C     1 
ATOM   746  O O     . ALA A 1 98  ? 121.125 147.364 137.974 1.00 104.32 ? 98  ALA B O     1 
ATOM   747  C CB    . ALA A 1 98  ? 118.730 148.914 138.848 1.00 104.32 ? 98  ALA B CB    1 
ATOM   748  N N     . ARG A 1 99  ? 119.984 147.309 136.034 1.00 102.76 ? 99  ARG B N     1 
ATOM   749  C CA    . ARG A 1 99  ? 121.160 147.237 135.181 1.00 102.76 ? 99  ARG B CA    1 
ATOM   750  C C     . ARG A 1 99  ? 121.225 148.493 134.326 1.00 102.76 ? 99  ARG B C     1 
ATOM   751  O O     . ARG A 1 99  ? 120.220 148.893 133.732 1.00 102.76 ? 99  ARG B O     1 
ATOM   752  C CB    . ARG A 1 99  ? 121.122 145.995 134.292 1.00 102.76 ? 99  ARG B CB    1 
ATOM   753  C CG    . ARG A 1 99  ? 122.228 145.951 133.262 1.00 102.76 ? 99  ARG B CG    1 
ATOM   754  C CD    . ARG A 1 99  ? 122.112 144.728 132.385 1.00 102.76 ? 99  ARG B CD    1 
ATOM   755  N NE    . ARG A 1 99  ? 120.928 144.780 131.538 1.00 102.76 ? 99  ARG B NE    1 
ATOM   756  C CZ    . ARG A 1 99  ? 120.876 145.414 130.374 1.00 102.76 ? 99  ARG B CZ    1 
ATOM   757  N NH1   . ARG A 1 99  ? 121.942 146.053 129.918 1.00 102.76 ? 99  ARG B NH1   1 
ATOM   758  N NH2   . ARG A 1 99  ? 119.759 145.410 129.664 1.00 102.76 ? 99  ARG B NH2   1 
ATOM   759  N N     . LYS A 1 100 ? 122.400 149.113 134.272 1.00 111.64 ? 100 LYS B N     1 
ATOM   760  C CA    . LYS A 1 100 ? 122.567 150.302 133.454 1.00 111.64 ? 100 LYS B CA    1 
ATOM   761  C C     . LYS A 1 100 ? 122.463 149.942 131.973 1.00 111.64 ? 100 LYS B C     1 
ATOM   762  O O     . LYS A 1 100 ? 122.487 148.772 131.585 1.00 111.64 ? 100 LYS B O     1 
ATOM   763  C CB    . LYS A 1 100 ? 123.898 150.981 133.764 1.00 111.64 ? 100 LYS B CB    1 
ATOM   764  C CG    . LYS A 1 100 ? 124.070 151.329 135.233 1.00 111.64 ? 100 LYS B CG    1 
ATOM   765  C CD    . LYS A 1 100 ? 125.169 152.354 135.440 1.00 111.64 ? 100 LYS B CD    1 
ATOM   766  C CE    . LYS A 1 100 ? 124.764 153.708 134.885 1.00 111.64 ? 100 LYS B CE    1 
ATOM   767  N NZ    . LYS A 1 100 ? 123.534 154.228 135.540 1.00 111.64 ? 100 LYS B NZ    1 
ATOM   768  N N     . ARG A 1 101 ? 122.343 150.977 131.138 1.00 115.20 ? 101 ARG B N     1 
ATOM   769  C CA    . ARG A 1 101 ? 121.996 150.761 129.736 1.00 115.20 ? 101 ARG B CA    1 
ATOM   770  C C     . ARG A 1 101 ? 123.041 149.931 129.004 1.00 115.20 ? 101 ARG B C     1 
ATOM   771  O O     . ARG A 1 101 ? 122.710 149.237 128.036 1.00 115.20 ? 101 ARG B O     1 
ATOM   772  C CB    . ARG A 1 101 ? 121.797 152.102 129.029 1.00 115.20 ? 101 ARG B CB    1 
ATOM   773  C CG    . ARG A 1 101 ? 121.200 151.975 127.636 1.00 115.20 ? 101 ARG B CG    1 
ATOM   774  C CD    . ARG A 1 101 ? 120.947 153.330 127.006 1.00 115.20 ? 101 ARG B CD    1 
ATOM   775  N NE    . ARG A 1 101 ? 119.527 153.668 126.997 1.00 115.20 ? 101 ARG B NE    1 
ATOM   776  C CZ    . ARG A 1 101 ? 118.681 153.311 126.037 1.00 115.20 ? 101 ARG B CZ    1 
ATOM   777  N NH1   . ARG A 1 101 ? 119.111 152.599 125.004 1.00 115.20 ? 101 ARG B NH1   1 
ATOM   778  N NH2   . ARG A 1 101 ? 117.405 153.662 126.108 1.00 115.20 ? 101 ARG B NH2   1 
ATOM   779  N N     . TYR A 1 102 ? 124.297 149.975 129.442 1.00 118.70 ? 102 TYR B N     1 
ATOM   780  C CA    . TYR A 1 102 ? 125.350 149.242 128.761 1.00 118.70 ? 102 TYR B CA    1 
ATOM   781  C C     . TYR A 1 102 ? 126.187 148.368 129.684 1.00 118.70 ? 102 TYR B C     1 
ATOM   782  O O     . TYR A 1 102 ? 127.054 147.639 129.193 1.00 118.70 ? 102 TYR B O     1 
ATOM   783  C CB    . TYR A 1 102 ? 126.267 150.210 128.000 1.00 118.70 ? 102 TYR B CB    1 
ATOM   784  C CG    . TYR A 1 102 ? 125.655 150.729 126.718 1.00 118.70 ? 102 TYR B CG    1 
ATOM   785  C CD1   . TYR A 1 102 ? 124.654 151.691 126.744 1.00 118.70 ? 102 TYR B CD1   1 
ATOM   786  C CD2   . TYR A 1 102 ? 126.071 150.251 125.484 1.00 118.70 ? 102 TYR B CD2   1 
ATOM   787  C CE1   . TYR A 1 102 ? 124.088 152.164 125.577 1.00 118.70 ? 102 TYR B CE1   1 
ATOM   788  C CE2   . TYR A 1 102 ? 125.511 150.719 124.311 1.00 118.70 ? 102 TYR B CE2   1 
ATOM   789  C CZ    . TYR A 1 102 ? 124.519 151.676 124.364 1.00 118.70 ? 102 TYR B CZ    1 
ATOM   790  O OH    . TYR A 1 102 ? 123.957 152.147 123.200 1.00 118.70 ? 102 TYR B OH    1 
ATOM   791  N N     . HIS A 1 103 ? 125.956 148.414 130.992 1.00 118.46 ? 103 HIS B N     1 
ATOM   792  C CA    . HIS A 1 103 ? 126.667 147.532 131.901 1.00 118.46 ? 103 HIS B CA    1 
ATOM   793  C C     . HIS A 1 103 ? 126.128 146.108 131.781 1.00 118.46 ? 103 HIS B C     1 
ATOM   794  O O     . HIS A 1 103 ? 125.173 145.831 131.051 1.00 118.46 ? 103 HIS B O     1 
ATOM   795  C CB    . HIS A 1 103 ? 126.544 148.030 133.340 1.00 118.46 ? 103 HIS B CB    1 
ATOM   796  C CG    . HIS A 1 103 ? 127.232 149.335 133.589 1.00 118.46 ? 103 HIS B CG    1 
ATOM   797  N ND1   . HIS A 1 103 ? 127.046 150.441 132.788 1.00 118.46 ? 103 HIS B ND1   1 
ATOM   798  C CD2   . HIS A 1 103 ? 128.106 149.711 134.553 1.00 118.46 ? 103 HIS B CD2   1 
ATOM   799  C CE1   . HIS A 1 103 ? 127.776 151.442 133.247 1.00 118.46 ? 103 HIS B CE1   1 
ATOM   800  N NE2   . HIS A 1 103 ? 128.428 151.025 134.317 1.00 118.46 ? 103 HIS B NE2   1 
ATOM   801  N N     . TYR A 1 104 ? 126.756 145.192 132.516 1.00 118.35 ? 104 TYR B N     1 
ATOM   802  C CA    . TYR A 1 104 ? 126.373 143.790 132.483 1.00 118.35 ? 104 TYR B CA    1 
ATOM   803  C C     . TYR A 1 104 ? 126.052 143.221 133.856 1.00 118.35 ? 104 TYR B C     1 
ATOM   804  O O     . TYR A 1 104 ? 125.686 142.045 133.950 1.00 118.35 ? 104 TYR B O     1 
ATOM   805  C CB    . TYR A 1 104 ? 127.478 142.949 131.829 1.00 118.35 ? 104 TYR B CB    1 
ATOM   806  C CG    . TYR A 1 104 ? 128.662 142.680 132.728 1.00 118.35 ? 104 TYR B CG    1 
ATOM   807  C CD1   . TYR A 1 104 ? 129.587 143.677 133.010 1.00 118.35 ? 104 TYR B CD1   1 
ATOM   808  C CD2   . TYR A 1 104 ? 128.860 141.425 133.289 1.00 118.35 ? 104 TYR B CD2   1 
ATOM   809  C CE1   . TYR A 1 104 ? 130.671 143.433 133.831 1.00 118.35 ? 104 TYR B CE1   1 
ATOM   810  C CE2   . TYR A 1 104 ? 129.942 141.172 134.111 1.00 118.35 ? 104 TYR B CE2   1 
ATOM   811  C CZ    . TYR A 1 104 ? 130.845 142.179 134.378 1.00 118.35 ? 104 TYR B CZ    1 
ATOM   812  O OH    . TYR A 1 104 ? 131.924 141.931 135.195 1.00 118.35 ? 104 TYR B OH    1 
ATOM   813  N N     . TYR A 1 105 ? 126.179 144.009 134.918 1.00 118.12 ? 105 TYR B N     1 
ATOM   814  C CA    . TYR A 1 105 ? 125.860 143.564 136.266 1.00 118.12 ? 105 TYR B CA    1 
ATOM   815  C C     . TYR A 1 105 ? 124.791 144.469 136.856 1.00 118.12 ? 105 TYR B C     1 
ATOM   816  O O     . TYR A 1 105 ? 124.782 145.679 136.609 1.00 118.12 ? 105 TYR B O     1 
ATOM   817  C CB    . TYR A 1 105 ? 127.105 143.551 137.159 1.00 118.12 ? 105 TYR B CB    1 
ATOM   818  C CG    . TYR A 1 105 ? 127.528 144.910 137.666 1.00 118.12 ? 105 TYR B CG    1 
ATOM   819  C CD1   . TYR A 1 105 ? 128.030 145.870 136.799 1.00 118.12 ? 105 TYR B CD1   1 
ATOM   820  C CD2   . TYR A 1 105 ? 127.435 145.228 139.014 1.00 118.12 ? 105 TYR B CD2   1 
ATOM   821  C CE1   . TYR A 1 105 ? 128.422 147.111 137.258 1.00 118.12 ? 105 TYR B CE1   1 
ATOM   822  C CE2   . TYR A 1 105 ? 127.825 146.468 139.483 1.00 118.12 ? 105 TYR B CE2   1 
ATOM   823  C CZ    . TYR A 1 105 ? 128.318 147.405 138.601 1.00 118.12 ? 105 TYR B CZ    1 
ATOM   824  O OH    . TYR A 1 105 ? 128.709 148.641 139.061 1.00 118.12 ? 105 TYR B OH    1 
ATOM   825  N N     . SER A 1 106 ? 123.894 143.879 137.636 1.00 111.69 ? 106 SER B N     1 
ATOM   826  C CA    . SER A 1 106 ? 122.718 144.566 138.144 1.00 111.69 ? 106 SER B CA    1 
ATOM   827  C C     . SER A 1 106 ? 122.887 144.868 139.624 1.00 111.69 ? 106 SER B C     1 
ATOM   828  O O     . SER A 1 106 ? 123.271 143.989 140.400 1.00 111.69 ? 106 SER B O     1 
ATOM   829  C CB    . SER A 1 106 ? 121.463 143.722 137.920 1.00 111.69 ? 106 SER B CB    1 
ATOM   830  O OG    . SER A 1 106 ? 121.268 142.810 138.986 1.00 111.69 ? 106 SER B OG    1 
ATOM   831  N N     . TYR A 1 107 ? 122.596 146.106 140.009 1.00 113.52 ? 107 TYR B N     1 
ATOM   832  C CA    . TYR A 1 107 ? 122.597 146.485 141.413 1.00 113.52 ? 107 TYR B CA    1 
ATOM   833  C C     . TYR A 1 107 ? 121.337 145.969 142.092 1.00 113.52 ? 107 TYR B C     1 
ATOM   834  O O     . TYR A 1 107 ? 120.271 145.882 141.482 1.00 113.52 ? 107 TYR B O     1 
ATOM   835  C CB    . TYR A 1 107 ? 122.683 148.003 141.563 1.00 113.52 ? 107 TYR B CB    1 
ATOM   836  C CG    . TYR A 1 107 ? 123.802 148.637 140.773 1.00 113.52 ? 107 TYR B CG    1 
ATOM   837  C CD1   . TYR A 1 107 ? 125.069 148.780 141.320 1.00 113.52 ? 107 TYR B CD1   1 
ATOM   838  C CD2   . TYR A 1 107 ? 123.593 149.092 139.480 1.00 113.52 ? 107 TYR B CD2   1 
ATOM   839  C CE1   . TYR A 1 107 ? 126.094 149.360 140.602 1.00 113.52 ? 107 TYR B CE1   1 
ATOM   840  C CE2   . TYR A 1 107 ? 124.612 149.673 138.754 1.00 113.52 ? 107 TYR B CE2   1 
ATOM   841  C CZ    . TYR A 1 107 ? 125.860 149.804 139.319 1.00 113.52 ? 107 TYR B CZ    1 
ATOM   842  O OH    . TYR A 1 107 ? 126.878 150.383 138.597 1.00 113.52 ? 107 TYR B OH    1 
ATOM   843  N N     . TRP A 1 108 ? 121.466 145.628 143.368 1.00 107.31 ? 108 TRP B N     1 
ATOM   844  C CA    . TRP A 1 108 ? 120.375 145.030 144.116 1.00 107.31 ? 108 TRP B CA    1 
ATOM   845  C C     . TRP A 1 108 ? 120.012 145.892 145.314 1.00 107.31 ? 108 TRP B C     1 
ATOM   846  O O     . TRP A 1 108 ? 120.874 146.520 145.935 1.00 107.31 ? 108 TRP B O     1 
ATOM   847  C CB    . TRP A 1 108 ? 120.742 143.626 144.588 1.00 107.31 ? 108 TRP B CB    1 
ATOM   848  C CG    . TRP A 1 108 ? 121.132 142.732 143.471 1.00 107.31 ? 108 TRP B CG    1 
ATOM   849  C CD1   . TRP A 1 108 ? 122.366 142.610 142.914 1.00 107.31 ? 108 TRP B CD1   1 
ATOM   850  C CD2   . TRP A 1 108 ? 120.277 141.841 142.756 1.00 107.31 ? 108 TRP B CD2   1 
ATOM   851  N NE1   . TRP A 1 108 ? 122.337 141.691 141.897 1.00 107.31 ? 108 TRP B NE1   1 
ATOM   852  C CE2   . TRP A 1 108 ? 121.063 141.204 141.780 1.00 107.31 ? 108 TRP B CE2   1 
ATOM   853  C CE3   . TRP A 1 108 ? 118.923 141.517 142.848 1.00 107.31 ? 108 TRP B CE3   1 
ATOM   854  C CZ2   . TRP A 1 108 ? 120.541 140.263 140.904 1.00 107.31 ? 108 TRP B CZ2   1 
ATOM   855  C CZ3   . TRP A 1 108 ? 118.408 140.585 141.980 1.00 107.31 ? 108 TRP B CZ3   1 
ATOM   856  C CH2   . TRP A 1 108 ? 119.213 139.967 141.019 1.00 107.31 ? 108 TRP B CH2   1 
ATOM   857  N N     . GLY A 1 109 ? 118.720 145.912 145.635 1.00 110.58 ? 109 GLY B N     1 
ATOM   858  C CA    . GLY A 1 109 ? 118.240 146.589 146.818 1.00 110.58 ? 109 GLY B CA    1 
ATOM   859  C C     . GLY A 1 109 ? 118.258 145.681 148.031 1.00 110.58 ? 109 GLY B C     1 
ATOM   860  O O     . GLY A 1 109 ? 118.528 144.484 147.949 1.00 110.58 ? 109 GLY B O     1 
ATOM   861  N N     . GLN A 1 110 ? 117.963 146.278 149.186 1.00 114.56 ? 110 GLN B N     1 
ATOM   862  C CA    . GLN A 1 110 ? 117.951 145.513 150.426 1.00 114.56 ? 110 GLN B CA    1 
ATOM   863  C C     . GLN A 1 110 ? 116.861 144.452 150.436 1.00 114.56 ? 110 GLN B C     1 
ATOM   864  O O     . GLN A 1 110 ? 116.923 143.525 151.250 1.00 114.56 ? 110 GLN B O     1 
ATOM   865  C CB    . GLN A 1 110 ? 117.779 146.449 151.621 1.00 114.56 ? 110 GLN B CB    1 
ATOM   866  C CG    . GLN A 1 110 ? 118.920 147.439 151.791 1.00 114.56 ? 110 GLN B CG    1 
ATOM   867  C CD    . GLN A 1 110 ? 120.256 146.757 152.005 1.00 114.56 ? 110 GLN B CD    1 
ATOM   868  O OE1   . GLN A 1 110 ? 121.119 146.772 151.128 1.00 114.56 ? 110 GLN B OE1   1 
ATOM   869  N NE2   . GLN A 1 110 ? 120.433 146.153 153.174 1.00 114.56 ? 110 GLN B NE2   1 
ATOM   870  N N     . GLY A 1 111 ? 115.869 144.568 149.558 1.00 113.92 ? 111 GLY B N     1 
ATOM   871  C CA    . GLY A 1 111 ? 114.840 143.557 149.440 1.00 113.92 ? 111 GLY B CA    1 
ATOM   872  C C     . GLY A 1 111 ? 113.766 143.684 150.495 1.00 113.92 ? 111 GLY B C     1 
ATOM   873  O O     . GLY A 1 111 ? 114.066 143.903 151.671 1.00 113.92 ? 111 GLY B O     1 
ATOM   874  N N     . THR A 1 112 ? 112.509 143.550 150.091 1.00 114.32 ? 112 THR B N     1 
ATOM   875  C CA    . THR A 1 112 ? 111.387 143.556 151.015 1.00 114.32 ? 112 THR B CA    1 
ATOM   876  C C     . THR A 1 112 ? 110.788 142.159 151.078 1.00 114.32 ? 112 THR B C     1 
ATOM   877  O O     . THR A 1 112 ? 110.724 141.455 150.067 1.00 114.32 ? 112 THR B O     1 
ATOM   878  C CB    . THR A 1 112 ? 110.325 144.577 150.599 1.00 114.32 ? 112 THR B CB    1 
ATOM   879  O OG1   . THR A 1 112 ? 109.226 144.525 151.515 1.00 114.32 ? 112 THR B OG1   1 
ATOM   880  C CG2   . THR A 1 112 ? 109.825 144.299 149.189 1.00 114.32 ? 112 THR B CG2   1 
ATOM   881  N N     . GLN A 1 113 ? 110.370 141.753 152.272 1.00 116.25 ? 113 GLN B N     1 
ATOM   882  C CA    . GLN A 1 113 ? 109.890 140.398 152.492 1.00 116.25 ? 113 GLN B CA    1 
ATOM   883  C C     . GLN A 1 113 ? 108.386 140.340 152.263 1.00 116.25 ? 113 GLN B C     1 
ATOM   884  O O     . GLN A 1 113 ? 107.640 141.179 152.775 1.00 116.25 ? 113 GLN B O     1 
ATOM   885  C CB    . GLN A 1 113 ? 110.230 139.928 153.905 1.00 116.25 ? 113 GLN B CB    1 
ATOM   886  C CG    . GLN A 1 113 ? 110.061 138.435 154.119 1.00 116.25 ? 113 GLN B CG    1 
ATOM   887  C CD    . GLN A 1 113 ? 108.638 138.046 154.455 1.00 116.25 ? 113 GLN B CD    1 
ATOM   888  O OE1   . GLN A 1 113 ? 107.884 138.834 155.026 1.00 116.25 ? 113 GLN B OE1   1 
ATOM   889  N NE2   . GLN A 1 113 ? 108.264 136.822 154.106 1.00 116.25 ? 113 GLN B NE2   1 
ATOM   890  N N     . VAL A 1 114 ? 107.949 139.346 151.496 1.00 116.66 ? 114 VAL B N     1 
ATOM   891  C CA    . VAL A 1 114 ? 106.541 139.136 151.188 1.00 116.66 ? 114 VAL B CA    1 
ATOM   892  C C     . VAL A 1 114 ? 106.159 137.734 151.637 1.00 116.66 ? 114 VAL B C     1 
ATOM   893  O O     . VAL A 1 114 ? 106.811 136.756 151.255 1.00 116.66 ? 114 VAL B O     1 
ATOM   894  C CB    . VAL A 1 114 ? 106.253 139.327 149.688 1.00 116.66 ? 114 VAL B CB    1 
ATOM   895  C CG1   . VAL A 1 114 ? 104.846 138.868 149.359 1.00 116.66 ? 114 VAL B CG1   1 
ATOM   896  C CG2   . VAL A 1 114 ? 106.450 140.778 149.296 1.00 116.66 ? 114 VAL B CG2   1 
ATOM   897  N N     . THR A 1 115 ? 105.109 137.640 152.445 1.00 122.53 ? 115 THR B N     1 
ATOM   898  C CA    . THR A 1 115 ? 104.608 136.364 152.928 1.00 122.53 ? 115 THR B CA    1 
ATOM   899  C C     . THR A 1 115 ? 103.093 136.343 152.796 1.00 122.53 ? 115 THR B C     1 
ATOM   900  O O     . THR A 1 115 ? 102.433 137.372 152.933 1.00 122.53 ? 115 THR B O     1 
ATOM   901  C CB    . THR A 1 115 ? 105.037 136.111 154.384 1.00 122.53 ? 115 THR B CB    1 
ATOM   902  O OG1   . THR A 1 115 ? 104.622 134.804 154.792 1.00 122.53 ? 115 THR B OG1   1 
ATOM   903  C CG2   . THR A 1 115 ? 104.447 137.152 155.321 1.00 122.53 ? 115 THR B CG2   1 
ATOM   904  N N     . VAL A 1 116 ? 102.545 135.167 152.495 1.00 127.64 ? 116 VAL B N     1 
ATOM   905  C CA    . VAL A 1 116 ? 101.116 135.049 152.219 1.00 127.64 ? 116 VAL B CA    1 
ATOM   906  C C     . VAL A 1 116 ? 100.512 133.819 152.889 1.00 127.64 ? 116 VAL B C     1 
ATOM   907  O O     . VAL A 1 116 ? 100.645 132.699 152.385 1.00 127.64 ? 116 VAL B O     1 
ATOM   908  C CB    . VAL A 1 116 ? 100.860 135.033 150.699 1.00 127.64 ? 116 VAL B CB    1 
ATOM   909  C CG1   . VAL A 1 116 ? 101.005 136.426 150.127 1.00 127.64 ? 116 VAL B CG1   1 
ATOM   910  C CG2   . VAL A 1 116 ? 101.843 134.106 150.003 1.00 127.64 ? 116 VAL B CG2   1 
ATOM   911  N N     . SER A 1 117 ? 99.832  134.024 154.021 1.00 131.20 ? 117 SER B N     1 
ATOM   912  C CA    . SER A 1 117 ? 99.053  132.978 154.689 1.00 131.20 ? 117 SER B CA    1 
ATOM   913  C C     . SER A 1 117 ? 99.888  131.708 154.882 1.00 131.20 ? 117 SER B C     1 
ATOM   914  O O     . SER A 1 117 ? 99.638  130.667 154.277 1.00 131.20 ? 117 SER B O     1 
ATOM   915  C CB    . SER A 1 117 ? 97.768  132.682 153.911 1.00 131.20 ? 117 SER B CB    1 
ATOM   916  O OG    . SER A 1 117 ? 97.044  131.626 154.510 1.00 131.20 ? 117 SER B OG    1 
ATOM   917  N N     . SER A 1 118 ? 100.889 131.841 155.756 1.00 134.28 ? 118 SER B N     1 
ATOM   918  C CA    . SER A 1 118 ? 101.964 130.865 155.923 1.00 134.28 ? 118 SER B CA    1 
ATOM   919  C C     . SER A 1 118 ? 101.465 129.433 155.790 1.00 134.28 ? 118 SER B C     1 
ATOM   920  O O     . SER A 1 118 ? 100.537 129.016 156.486 1.00 134.28 ? 118 SER B O     1 
ATOM   921  C CB    . SER A 1 118 ? 102.617 131.059 157.292 1.00 134.28 ? 118 SER B CB    1 
ATOM   922  O OG    . SER A 1 118 ? 101.693 130.772 158.332 1.00 134.28 ? 118 SER B OG    1 
ATOM   923  N N     . LEU A 1 119 ? 102.110 128.676 154.905 1.00 134.95 ? 119 LEU B N     1 
ATOM   924  C CA    . LEU A 1 119 ? 101.574 127.404 154.423 1.00 134.95 ? 119 LEU B CA    1 
ATOM   925  C C     . LEU A 1 119 ? 102.163 126.255 155.235 1.00 134.95 ? 119 LEU B C     1 
ATOM   926  O O     . LEU A 1 119 ? 103.333 125.898 155.083 1.00 134.95 ? 119 LEU B O     1 
ATOM   927  C CB    . LEU A 1 119 ? 101.830 127.251 152.925 1.00 134.95 ? 119 LEU B CB    1 
ATOM   928  C CG    . LEU A 1 119 ? 103.236 127.085 152.338 1.00 134.95 ? 119 LEU B CG    1 
ATOM   929  C CD1   . LEU A 1 119 ? 103.154 126.541 150.924 1.00 134.95 ? 119 LEU B CD1   1 
ATOM   930  C CD2   . LEU A 1 119 ? 104.009 128.398 152.355 1.00 134.95 ? 119 LEU B CD2   1 
ATOM   931  N N     . GLU A 1 120 ? 101.345 125.686 156.120 1.00 136.18 ? 120 GLU B N     1 
ATOM   932  C CA    . GLU A 1 120 ? 101.685 124.498 156.900 1.00 136.18 ? 120 GLU B CA    1 
ATOM   933  C C     . GLU A 1 120 ? 102.962 124.675 157.716 1.00 136.18 ? 120 GLU B C     1 
ATOM   934  O O     . GLU A 1 120 ? 103.564 123.685 158.143 1.00 136.18 ? 120 GLU B O     1 
ATOM   935  C CB    . GLU A 1 120 ? 101.802 123.262 156.000 1.00 136.18 ? 120 GLU B CB    1 
ATOM   936  C CG    . GLU A 1 120 ? 100.727 123.161 154.923 1.00 136.18 ? 120 GLU B CG    1 
ATOM   937  C CD    . GLU A 1 120 ? 99.330  123.435 155.451 1.00 136.18 ? 120 GLU B CD    1 
ATOM   938  O OE1   . GLU A 1 120 ? 98.964  122.880 156.509 1.00 136.18 ? 120 GLU B OE1   1 
ATOM   939  O OE2   . GLU A 1 120 ? 98.598  124.214 154.808 1.00 136.18 ? 120 GLU B OE2   1 
ATOM   940  N N     . HIS A 1 121 ? 103.376 125.920 157.940 1.00 137.00 ? 121 HIS B N     1 
ATOM   941  C CA    . HIS A 1 121 ? 104.562 126.250 158.730 1.00 137.00 ? 121 HIS B CA    1 
ATOM   942  C C     . HIS A 1 121 ? 105.795 125.457 158.301 1.00 137.00 ? 121 HIS B C     1 
ATOM   943  O O     . HIS A 1 121 ? 105.937 125.094 157.133 1.00 137.00 ? 121 HIS B O     1 
ATOM   944  C CB    . HIS A 1 121 ? 104.282 126.024 160.218 1.00 137.00 ? 121 HIS B CB    1 
ATOM   945  C CG    . HIS A 1 121 ? 103.088 126.771 160.728 1.00 137.00 ? 121 HIS B CG    1 
ATOM   946  N ND1   . HIS A 1 121 ? 101.794 126.399 160.430 1.00 137.00 ? 121 HIS B ND1   1 
ATOM   947  C CD2   . HIS A 1 121 ? 102.990 127.870 161.514 1.00 137.00 ? 121 HIS B CD2   1 
ATOM   948  C CE1   . HIS A 1 121 ? 100.952 127.235 161.010 1.00 137.00 ? 121 HIS B CE1   1 
ATOM   949  N NE2   . HIS A 1 121 ? 101.652 128.137 161.674 1.00 137.00 ? 121 HIS B NE2   1 
ATOM   950  N N     . LEU B 2 16  ? 126.610 137.174 90.788  1.00 123.21 ? 16  LEU A N     1 
ATOM   951  C CA    . LEU B 2 16  ? 127.373 137.094 89.547  1.00 123.21 ? 16  LEU A CA    1 
ATOM   952  C C     . LEU B 2 16  ? 126.564 136.448 88.428  1.00 123.21 ? 16  LEU A C     1 
ATOM   953  O O     . LEU B 2 16  ? 125.455 135.958 88.646  1.00 123.21 ? 16  LEU A O     1 
ATOM   954  C CB    . LEU B 2 16  ? 128.676 136.316 89.759  1.00 123.21 ? 16  LEU A CB    1 
ATOM   955  C CG    . LEU B 2 16  ? 129.903 137.096 90.240  1.00 123.21 ? 16  LEU A CG    1 
ATOM   956  C CD1   . LEU B 2 16  ? 130.307 138.142 89.209  1.00 123.21 ? 16  LEU A CD1   1 
ATOM   957  C CD2   . LEU B 2 16  ? 129.668 137.735 91.601  1.00 123.21 ? 16  LEU A CD2   1 
ATOM   958  N N     . TRP B 2 17  ? 127.136 136.456 87.229  1.00 124.36 ? 17  TRP A N     1 
ATOM   959  C CA    . TRP B 2 17  ? 126.511 135.892 86.041  1.00 124.36 ? 17  TRP A CA    1 
ATOM   960  C C     . TRP B 2 17  ? 127.599 135.600 85.016  1.00 124.36 ? 17  TRP A C     1 
ATOM   961  O O     . TRP B 2 17  ? 127.597 136.186 83.926  1.00 124.36 ? 17  TRP A O     1 
ATOM   962  C CB    . TRP B 2 17  ? 125.475 136.869 85.484  1.00 124.36 ? 17  TRP A CB    1 
ATOM   963  C CG    . TRP B 2 17  ? 124.546 136.315 84.453  1.00 124.36 ? 17  TRP A CG    1 
ATOM   964  C CD1   . TRP B 2 17  ? 124.487 136.659 83.136  1.00 124.36 ? 17  TRP A CD1   1 
ATOM   965  C CD2   . TRP B 2 17  ? 123.511 135.349 84.662  1.00 124.36 ? 17  TRP A CD2   1 
ATOM   966  N NE1   . TRP B 2 17  ? 123.490 135.955 82.507  1.00 124.36 ? 17  TRP A NE1   1 
ATOM   967  C CE2   . TRP B 2 17  ? 122.874 135.145 83.423  1.00 124.36 ? 17  TRP A CE2   1 
ATOM   968  C CE3   . TRP B 2 17  ? 123.064 134.632 85.775  1.00 124.36 ? 17  TRP A CE3   1 
ATOM   969  C CZ2   . TRP B 2 17  ? 121.816 134.255 83.266  1.00 124.36 ? 17  TRP A CZ2   1 
ATOM   970  C CZ3   . TRP B 2 17  ? 122.016 133.746 85.616  1.00 124.36 ? 17  TRP A CZ3   1 
ATOM   971  C CH2   . TRP B 2 17  ? 121.405 133.564 84.371  1.00 124.36 ? 17  TRP A CH2   1 
ATOM   972  N N     . PRO B 2 18  ? 128.556 134.703 85.326  1.00 123.45 ? 18  PRO A N     1 
ATOM   973  C CA    . PRO B 2 18  ? 129.735 134.498 84.475  1.00 123.45 ? 18  PRO A CA    1 
ATOM   974  C C     . PRO B 2 18  ? 129.520 133.474 83.362  1.00 123.45 ? 18  PRO A C     1 
ATOM   975  O O     . PRO B 2 18  ? 130.312 132.548 83.184  1.00 123.45 ? 18  PRO A O     1 
ATOM   976  C CB    . PRO B 2 18  ? 130.795 134.025 85.473  1.00 123.45 ? 18  PRO A CB    1 
ATOM   977  C CG    . PRO B 2 18  ? 130.038 133.650 86.754  1.00 123.45 ? 18  PRO A CG    1 
ATOM   978  C CD    . PRO B 2 18  ? 128.574 133.795 86.482  1.00 123.45 ? 18  PRO A CD    1 
ATOM   979  N N     . ILE B 2 19  ? 128.441 133.642 82.609  1.00 120.82 ? 19  ILE A N     1 
ATOM   980  C CA    . ILE B 2 19  ? 128.079 132.727 81.537  1.00 120.82 ? 19  ILE A CA    1 
ATOM   981  C C     . ILE B 2 19  ? 127.922 133.513 80.245  1.00 120.82 ? 19  ILE A C     1 
ATOM   982  O O     . ILE B 2 19  ? 127.359 134.614 80.237  1.00 120.82 ? 19  ILE A O     1 
ATOM   983  C CB    . ILE B 2 19  ? 126.797 131.942 81.877  1.00 120.82 ? 19  ILE A CB    1 
ATOM   984  C CG1   . ILE B 2 19  ? 125.647 132.904 82.162  1.00 120.82 ? 19  ILE A CG1   1 
ATOM   985  C CG2   . ILE B 2 19  ? 127.039 131.018 83.061  1.00 120.82 ? 19  ILE A CG2   1 
ATOM   986  C CD1   . ILE B 2 19  ? 124.336 132.218 82.349  1.00 120.82 ? 19  ILE A CD1   1 
ATOM   987  N N     . HIS B 2 20  ? 128.435 132.950 79.154  1.00 120.13 ? 20  HIS A N     1 
ATOM   988  C CA    . HIS B 2 20  ? 128.400 133.616 77.863  1.00 120.13 ? 20  HIS A CA    1 
ATOM   989  C C     . HIS B 2 20  ? 126.963 133.732 77.356  1.00 120.13 ? 20  HIS A C     1 
ATOM   990  O O     . HIS B 2 20  ? 126.012 133.237 77.969  1.00 120.13 ? 20  HIS A O     1 
ATOM   991  C CB    . HIS B 2 20  ? 129.259 132.861 76.850  1.00 120.13 ? 20  HIS A CB    1 
ATOM   992  C CG    . HIS B 2 20  ? 130.720 132.863 77.175  1.00 120.13 ? 20  HIS A CG    1 
ATOM   993  N ND1   . HIS B 2 20  ? 131.240 133.539 78.257  1.00 120.13 ? 20  HIS A ND1   1 
ATOM   994  C CD2   . HIS B 2 20  ? 131.770 132.271 76.560  1.00 120.13 ? 20  HIS A CD2   1 
ATOM   995  C CE1   . HIS B 2 20  ? 132.549 133.362 78.296  1.00 120.13 ? 20  HIS A CE1   1 
ATOM   996  N NE2   . HIS B 2 20  ? 132.896 132.596 77.277  1.00 120.13 ? 20  HIS A NE2   1 
ATOM   997  N N     . THR B 2 21  ? 126.813 134.406 76.214  1.00 121.86 ? 21  THR A N     1 
ATOM   998  C CA    . THR B 2 21  ? 125.487 134.637 75.655  1.00 121.86 ? 21  THR A CA    1 
ATOM   999  C C     . THR B 2 21  ? 124.972 133.431 74.881  1.00 121.86 ? 21  THR A C     1 
ATOM   1000 O O     . THR B 2 21  ? 123.758 133.207 74.827  1.00 121.86 ? 21  THR A O     1 
ATOM   1001 C CB    . THR B 2 21  ? 125.516 135.871 74.747  1.00 121.86 ? 21  THR A CB    1 
ATOM   1002 O OG1   . THR B 2 21  ? 126.018 136.994 75.483  1.00 121.86 ? 21  THR A OG1   1 
ATOM   1003 C CG2   . THR B 2 21  ? 124.122 136.205 74.236  1.00 121.86 ? 21  THR A CG2   1 
ATOM   1004 N N     . HIS B 2 22  ? 125.868 132.628 74.303  1.00 119.80 ? 22  HIS A N     1 
ATOM   1005 C CA    . HIS B 2 22  ? 125.425 131.491 73.504  1.00 119.80 ? 22  HIS A CA    1 
ATOM   1006 C C     . HIS B 2 22  ? 125.061 130.289 74.364  1.00 119.80 ? 22  HIS A C     1 
ATOM   1007 O O     . HIS B 2 22  ? 124.205 129.492 73.970  1.00 119.80 ? 22  HIS A O     1 
ATOM   1008 C CB    . HIS B 2 22  ? 126.503 131.107 72.488  1.00 119.80 ? 22  HIS A CB    1 
ATOM   1009 C CG    . HIS B 2 22  ? 127.791 130.664 73.107  1.00 119.80 ? 22  HIS A CG    1 
ATOM   1010 N ND1   . HIS B 2 22  ? 128.709 131.550 73.628  1.00 119.80 ? 22  HIS A ND1   1 
ATOM   1011 C CD2   . HIS B 2 22  ? 128.321 129.430 73.278  1.00 119.80 ? 22  HIS A CD2   1 
ATOM   1012 C CE1   . HIS B 2 22  ? 129.747 130.880 74.098  1.00 119.80 ? 22  HIS A CE1   1 
ATOM   1013 N NE2   . HIS B 2 22  ? 129.536 129.592 73.897  1.00 119.80 ? 22  HIS A NE2   1 
ATOM   1014 N N     . GLU B 2 23  ? 125.681 130.148 75.534  1.00 115.82 ? 23  GLU A N     1 
ATOM   1015 C CA    . GLU B 2 23  ? 125.383 129.055 76.449  1.00 115.82 ? 23  GLU A CA    1 
ATOM   1016 C C     . GLU B 2 23  ? 124.115 129.293 77.256  1.00 115.82 ? 23  GLU A C     1 
ATOM   1017 O O     . GLU B 2 23  ? 123.757 128.451 78.085  1.00 115.82 ? 23  GLU A O     1 
ATOM   1018 C CB    . GLU B 2 23  ? 126.562 128.831 77.398  1.00 115.82 ? 23  GLU A CB    1 
ATOM   1019 C CG    . GLU B 2 23  ? 127.917 128.985 76.734  1.00 115.82 ? 23  GLU A CG    1 
ATOM   1020 C CD    . GLU B 2 23  ? 129.067 128.835 77.707  1.00 115.82 ? 23  GLU A CD    1 
ATOM   1021 O OE1   . GLU B 2 23  ? 129.111 129.587 78.703  1.00 115.82 ? 23  GLU A OE1   1 
ATOM   1022 O OE2   . GLU B 2 23  ? 129.934 127.970 77.470  1.00 115.82 ? 23  GLU A OE2   1 
ATOM   1023 N N     . LEU B 2 24  ? 123.441 130.421 77.024  1.00 111.55 ? 24  LEU A N     1 
ATOM   1024 C CA    . LEU B 2 24  ? 122.245 130.762 77.786  1.00 111.55 ? 24  LEU A CA    1 
ATOM   1025 C C     . LEU B 2 24  ? 121.139 129.733 77.585  1.00 111.55 ? 24  LEU A C     1 
ATOM   1026 O O     . LEU B 2 24  ? 120.506 129.291 78.554  1.00 111.55 ? 24  LEU A O     1 
ATOM   1027 C CB    . LEU B 2 24  ? 121.777 132.161 77.383  1.00 111.55 ? 24  LEU A CB    1 
ATOM   1028 C CG    . LEU B 2 24  ? 120.512 132.760 77.987  1.00 111.55 ? 24  LEU A CG    1 
ATOM   1029 C CD1   . LEU B 2 24  ? 120.718 134.233 78.279  1.00 111.55 ? 24  LEU A CD1   1 
ATOM   1030 C CD2   . LEU B 2 24  ? 119.354 132.577 77.022  1.00 111.55 ? 24  LEU A CD2   1 
ATOM   1031 N N     . LYS B 2 25  ? 120.895 129.337 76.332  1.00 109.43 ? 25  LYS A N     1 
ATOM   1032 C CA    . LYS B 2 25  ? 119.833 128.379 76.039  1.00 109.43 ? 25  LYS A CA    1 
ATOM   1033 C C     . LYS B 2 25  ? 120.072 127.046 76.729  1.00 109.43 ? 25  LYS A C     1 
ATOM   1034 O O     . LYS B 2 25  ? 119.123 126.295 76.974  1.00 109.43 ? 25  LYS A O     1 
ATOM   1035 C CB    . LYS B 2 25  ? 119.716 128.179 74.528  1.00 109.43 ? 25  LYS A CB    1 
ATOM   1036 C CG    . LYS B 2 25  ? 118.502 127.381 74.094  1.00 109.43 ? 25  LYS A CG    1 
ATOM   1037 C CD    . LYS B 2 25  ? 118.355 127.376 72.583  1.00 109.43 ? 25  LYS A CD    1 
ATOM   1038 C CE    . LYS B 2 25  ? 117.162 126.540 72.151  1.00 109.43 ? 25  LYS A CE    1 
ATOM   1039 N NZ    . LYS B 2 25  ? 116.953 126.580 70.678  1.00 109.43 ? 25  LYS A NZ    1 
ATOM   1040 N N     . LYS B 2 26  ? 121.323 126.737 77.057  1.00 108.81 ? 26  LYS A N     1 
ATOM   1041 C CA    . LYS B 2 26  ? 121.639 125.491 77.738  1.00 108.81 ? 26  LYS A CA    1 
ATOM   1042 C C     . LYS B 2 26  ? 121.645 125.637 79.251  1.00 108.81 ? 26  LYS A C     1 
ATOM   1043 O O     . LYS B 2 26  ? 121.271 124.695 79.958  1.00 108.81 ? 26  LYS A O     1 
ATOM   1044 C CB    . LYS B 2 26  ? 123.000 124.968 77.272  1.00 108.81 ? 26  LYS A CB    1 
ATOM   1045 C CG    . LYS B 2 26  ? 123.442 123.681 77.944  1.00 108.81 ? 26  LYS A CG    1 
ATOM   1046 C CD    . LYS B 2 26  ? 124.899 123.384 77.650  1.00 108.81 ? 26  LYS A CD    1 
ATOM   1047 C CE    . LYS B 2 26  ? 125.394 122.202 78.460  1.00 108.81 ? 26  LYS A CE    1 
ATOM   1048 N NZ    . LYS B 2 26  ? 126.852 121.981 78.272  1.00 108.81 ? 26  LYS A NZ    1 
ATOM   1049 N N     . VAL B 2 27  ? 122.048 126.795 79.765  1.00 104.13 ? 27  VAL A N     1 
ATOM   1050 C CA    . VAL B 2 27  ? 122.205 126.934 81.206  1.00 104.13 ? 27  VAL A CA    1 
ATOM   1051 C C     . VAL B 2 27  ? 120.906 127.347 81.893  1.00 104.13 ? 27  VAL A C     1 
ATOM   1052 O O     . VAL B 2 27  ? 120.677 126.970 83.046  1.00 104.13 ? 27  VAL A O     1 
ATOM   1053 C CB    . VAL B 2 27  ? 123.336 127.922 81.531  1.00 104.13 ? 27  VAL A CB    1 
ATOM   1054 C CG1   . VAL B 2 27  ? 123.016 129.290 80.979  1.00 104.13 ? 27  VAL A CG1   1 
ATOM   1055 C CG2   . VAL B 2 27  ? 123.590 127.979 83.027  1.00 104.13 ? 27  VAL A CG2   1 
ATOM   1056 N N     . LEU B 2 28  ? 120.035 128.105 81.221  1.00 101.56 ? 28  LEU A N     1 
ATOM   1057 C CA    . LEU B 2 28  ? 118.798 128.520 81.881  1.00 101.56 ? 28  LEU A CA    1 
ATOM   1058 C C     . LEU B 2 28  ? 117.909 127.344 82.265  1.00 101.56 ? 28  LEU A C     1 
ATOM   1059 O O     . LEU B 2 28  ? 117.373 127.352 83.386  1.00 101.56 ? 28  LEU A O     1 
ATOM   1060 C CB    . LEU B 2 28  ? 118.038 129.529 81.017  1.00 101.56 ? 28  LEU A CB    1 
ATOM   1061 C CG    . LEU B 2 28  ? 118.672 130.910 80.891  1.00 101.56 ? 28  LEU A CG    1 
ATOM   1062 C CD1   . LEU B 2 28  ? 117.773 131.804 80.066  1.00 101.56 ? 28  LEU A CD1   1 
ATOM   1063 C CD2   . LEU B 2 28  ? 118.923 131.511 82.260  1.00 101.56 ? 28  LEU A CD2   1 
ATOM   1064 N N     . PRO B 2 29  ? 117.693 126.328 81.423  1.00 98.84  ? 29  PRO A N     1 
ATOM   1065 C CA    . PRO B 2 29  ? 116.977 125.146 81.924  1.00 98.84  ? 29  PRO A CA    1 
ATOM   1066 C C     . PRO B 2 29  ? 117.714 124.447 83.050  1.00 98.84  ? 29  PRO A C     1 
ATOM   1067 O O     . PRO B 2 29  ? 117.076 123.964 83.990  1.00 98.84  ? 29  PRO A O     1 
ATOM   1068 C CB    . PRO B 2 29  ? 116.846 124.258 80.678  1.00 98.84  ? 29  PRO A CB    1 
ATOM   1069 C CG    . PRO B 2 29  ? 117.838 124.792 79.709  1.00 98.84  ? 29  PRO A CG    1 
ATOM   1070 C CD    . PRO B 2 29  ? 117.903 126.251 79.969  1.00 98.84  ? 29  PRO A CD    1 
ATOM   1071 N N     . MET B 2 30  ? 119.046 124.399 82.995  1.00 97.99  ? 30  MET A N     1 
ATOM   1072 C CA    . MET B 2 30  ? 119.804 123.804 84.091  1.00 97.99  ? 30  MET A CA    1 
ATOM   1073 C C     . MET B 2 30  ? 119.647 124.612 85.370  1.00 97.99  ? 30  MET A C     1 
ATOM   1074 O O     . MET B 2 30  ? 119.461 124.043 86.453  1.00 97.99  ? 30  MET A O     1 
ATOM   1075 C CB    . MET B 2 30  ? 121.280 123.694 83.716  1.00 97.99  ? 30  MET A CB    1 
ATOM   1076 C CG    . MET B 2 30  ? 121.577 122.702 82.615  1.00 97.99  ? 30  MET A CG    1 
ATOM   1077 S SD    . MET B 2 30  ? 123.339 122.402 82.420  1.00 97.99  ? 30  MET A SD    1 
ATOM   1078 C CE    . MET B 2 30  ? 123.704 121.588 83.969  1.00 97.99  ? 30  MET A CE    1 
ATOM   1079 N N     . PHE B 2 31  ? 119.729 125.939 85.268  1.00 93.70  ? 31  PHE A N     1 
ATOM   1080 C CA    . PHE B 2 31  ? 119.574 126.776 86.451  1.00 93.70  ? 31  PHE A CA    1 
ATOM   1081 C C     . PHE B 2 31  ? 118.168 126.663 87.015  1.00 93.70  ? 31  PHE A C     1 
ATOM   1082 O O     . PHE B 2 31  ? 117.980 126.682 88.233  1.00 93.70  ? 31  PHE A O     1 
ATOM   1083 C CB    . PHE B 2 31  ? 119.904 128.230 86.118  1.00 93.70  ? 31  PHE A CB    1 
ATOM   1084 C CG    . PHE B 2 31  ? 119.831 129.152 87.298  1.00 93.70  ? 31  PHE A CG    1 
ATOM   1085 C CD1   . PHE B 2 31  ? 120.918 129.306 88.138  1.00 93.70  ? 31  PHE A CD1   1 
ATOM   1086 C CD2   . PHE B 2 31  ? 118.680 129.870 87.564  1.00 93.70  ? 31  PHE A CD2   1 
ATOM   1087 C CE1   . PHE B 2 31  ? 120.856 130.153 89.220  1.00 93.70  ? 31  PHE A CE1   1 
ATOM   1088 C CE2   . PHE B 2 31  ? 118.613 130.717 88.647  1.00 93.70  ? 31  PHE A CE2   1 
ATOM   1089 C CZ    . PHE B 2 31  ? 119.703 130.860 89.476  1.00 93.70  ? 31  PHE A CZ    1 
ATOM   1090 N N     . LEU B 2 32  ? 117.168 126.527 86.143  1.00 90.21  ? 32  LEU A N     1 
ATOM   1091 C CA    . LEU B 2 32  ? 115.799 126.355 86.614  1.00 90.21  ? 32  LEU A CA    1 
ATOM   1092 C C     . LEU B 2 32  ? 115.628 125.015 87.314  1.00 90.21  ? 32  LEU A C     1 
ATOM   1093 O O     . LEU B 2 32  ? 114.984 124.935 88.365  1.00 90.21  ? 32  LEU A O     1 
ATOM   1094 C CB    . LEU B 2 32  ? 114.826 126.480 85.444  1.00 90.21  ? 32  LEU A CB    1 
ATOM   1095 C CG    . LEU B 2 32  ? 113.395 126.884 85.789  1.00 90.21  ? 32  LEU A CG    1 
ATOM   1096 C CD1   . LEU B 2 32  ? 113.383 128.210 86.524  1.00 90.21  ? 32  LEU A CD1   1 
ATOM   1097 C CD2   . LEU B 2 32  ? 112.549 126.958 84.533  1.00 90.21  ? 32  LEU A CD2   1 
ATOM   1098 N N     . MET B 2 33  ? 116.201 123.951 86.747  1.00 88.46  ? 33  MET A N     1 
ATOM   1099 C CA    . MET B 2 33  ? 116.158 122.646 87.395  1.00 88.46  ? 33  MET A CA    1 
ATOM   1100 C C     . MET B 2 33  ? 116.801 122.701 88.771  1.00 88.46  ? 33  MET A C     1 
ATOM   1101 O O     . MET B 2 33  ? 116.248 122.186 89.749  1.00 88.46  ? 33  MET A O     1 
ATOM   1102 C CB    . MET B 2 33  ? 116.861 121.606 86.525  1.00 88.46  ? 33  MET A CB    1 
ATOM   1103 C CG    . MET B 2 33  ? 116.092 121.186 85.296  1.00 88.46  ? 33  MET A CG    1 
ATOM   1104 S SD    . MET B 2 33  ? 116.906 119.836 84.434  1.00 88.46  ? 33  MET A SD    1 
ATOM   1105 C CE    . MET B 2 33  ? 117.169 118.698 85.788  1.00 88.46  ? 33  MET A CE    1 
ATOM   1106 N N     . PHE B 2 34  ? 117.973 123.330 88.868  1.00 84.98  ? 34  PHE A N     1 
ATOM   1107 C CA    . PHE B 2 34  ? 118.657 123.400 90.153  1.00 84.98  ? 34  PHE A CA    1 
ATOM   1108 C C     . PHE B 2 34  ? 117.885 124.254 91.145  1.00 84.98  ? 34  PHE A C     1 
ATOM   1109 O O     . PHE B 2 34  ? 117.806 123.915 92.330  1.00 84.98  ? 34  PHE A O     1 
ATOM   1110 C CB    . PHE B 2 34  ? 120.069 123.945 89.982  1.00 84.98  ? 34  PHE A CB    1 
ATOM   1111 C CG    . PHE B 2 34  ? 120.928 123.759 91.191  1.00 84.98  ? 34  PHE A CG    1 
ATOM   1112 C CD1   . PHE B 2 34  ? 121.061 122.514 91.768  1.00 84.98  ? 34  PHE A CD1   1 
ATOM   1113 C CD2   . PHE B 2 34  ? 121.589 124.823 91.762  1.00 84.98  ? 34  PHE A CD2   1 
ATOM   1114 C CE1   . PHE B 2 34  ? 121.847 122.333 92.876  1.00 84.98  ? 34  PHE A CE1   1 
ATOM   1115 C CE2   . PHE B 2 34  ? 122.371 124.640 92.877  1.00 84.98  ? 34  PHE A CE2   1 
ATOM   1116 C CZ    . PHE B 2 34  ? 122.501 123.397 93.432  1.00 84.98  ? 34  PHE A CZ    1 
ATOM   1117 N N     . PHE B 2 35  ? 117.322 125.373 90.687  1.00 81.42  ? 35  PHE A N     1 
ATOM   1118 C CA    . PHE B 2 35  ? 116.527 126.214 91.569  1.00 81.42  ? 35  PHE A CA    1 
ATOM   1119 C C     . PHE B 2 35  ? 115.338 125.446 92.116  1.00 81.42  ? 35  PHE A C     1 
ATOM   1120 O O     . PHE B 2 35  ? 115.055 125.496 93.315  1.00 81.42  ? 35  PHE A O     1 
ATOM   1121 C CB    . PHE B 2 35  ? 116.064 127.466 90.828  1.00 81.42  ? 35  PHE A CB    1 
ATOM   1122 C CG    . PHE B 2 35  ? 115.407 128.484 91.712  1.00 81.42  ? 35  PHE A CG    1 
ATOM   1123 C CD1   . PHE B 2 35  ? 114.056 128.407 91.997  1.00 81.42  ? 35  PHE A CD1   1 
ATOM   1124 C CD2   . PHE B 2 35  ? 116.140 129.518 92.258  1.00 81.42  ? 35  PHE A CD2   1 
ATOM   1125 C CE1   . PHE B 2 35  ? 113.454 129.338 92.810  1.00 81.42  ? 35  PHE A CE1   1 
ATOM   1126 C CE2   . PHE B 2 35  ? 115.541 130.452 93.069  1.00 81.42  ? 35  PHE A CE2   1 
ATOM   1127 C CZ    . PHE B 2 35  ? 114.196 130.362 93.346  1.00 81.42  ? 35  PHE A CZ    1 
ATOM   1128 N N     . CYS B 2 36  ? 114.632 124.716 91.252  1.00 80.94  ? 36  CYS A N     1 
ATOM   1129 C CA    . CYS B 2 36  ? 113.483 123.949 91.717  1.00 80.94  ? 36  CYS A CA    1 
ATOM   1130 C C     . CYS B 2 36  ? 113.901 122.852 92.685  1.00 80.94  ? 36  CYS A C     1 
ATOM   1131 O O     . CYS B 2 36  ? 113.249 122.642 93.715  1.00 80.94  ? 36  CYS A O     1 
ATOM   1132 C CB    . CYS B 2 36  ? 112.725 123.359 90.531  1.00 80.94  ? 36  CYS A CB    1 
ATOM   1133 S SG    . CYS B 2 36  ? 112.131 124.581 89.349  1.00 80.94  ? 36  CYS A SG    1 
ATOM   1134 N N     . ILE B 2 37  ? 114.997 122.153 92.386  1.00 79.05  ? 37  ILE A N     1 
ATOM   1135 C CA    . ILE B 2 37  ? 115.413 121.050 93.244  1.00 79.05  ? 37  ILE A CA    1 
ATOM   1136 C C     . ILE B 2 37  ? 115.852 121.565 94.606  1.00 79.05  ? 37  ILE A C     1 
ATOM   1137 O O     . ILE B 2 37  ? 115.493 120.995 95.640  1.00 79.05  ? 37  ILE A O     1 
ATOM   1138 C CB    . ILE B 2 37  ? 116.518 120.227 92.562  1.00 79.05  ? 37  ILE A CB    1 
ATOM   1139 C CG1   . ILE B 2 37  ? 115.940 119.469 91.372  1.00 79.05  ? 37  ILE A CG1   1 
ATOM   1140 C CG2   . ILE B 2 37  ? 117.115 119.244 93.534  1.00 79.05  ? 37  ILE A CG2   1 
ATOM   1141 C CD1   . ILE B 2 37  ? 116.954 118.678 90.607  1.00 79.05  ? 37  ILE A CD1   1 
ATOM   1142 N N     . THR B 2 38  ? 116.606 122.663 94.640  1.00 78.92  ? 38  THR A N     1 
ATOM   1143 C CA    . THR B 2 38  ? 117.054 123.201 95.918  1.00 78.92  ? 38  THR A CA    1 
ATOM   1144 C C     . THR B 2 38  ? 115.916 123.862 96.686  1.00 78.92  ? 38  THR A C     1 
ATOM   1145 O O     . THR B 2 38  ? 115.893 123.805 97.920  1.00 78.92  ? 38  THR A O     1 
ATOM   1146 C CB    . THR B 2 38  ? 118.193 124.190 95.698  1.00 78.92  ? 38  THR A CB    1 
ATOM   1147 O OG1   . THR B 2 38  ? 117.853 125.077 94.628  1.00 78.92  ? 38  THR A OG1   1 
ATOM   1148 C CG2   . THR B 2 38  ? 119.466 123.453 95.346  1.00 78.92  ? 38  THR A CG2   1 
ATOM   1149 N N     . PHE B 2 39  ? 114.966 124.484 95.986  1.00 74.80  ? 39  PHE A N     1 
ATOM   1150 C CA    . PHE B 2 39  ? 113.786 125.028 96.643  1.00 74.80  ? 39  PHE A CA    1 
ATOM   1151 C C     . PHE B 2 39  ? 113.000 123.920 97.328  1.00 74.80  ? 39  PHE A C     1 
ATOM   1152 O O     . PHE B 2 39  ? 112.633 124.037 98.504  1.00 74.80  ? 39  PHE A O     1 
ATOM   1153 C CB    . PHE B 2 39  ? 112.927 125.761 95.610  1.00 74.80  ? 39  PHE A CB    1 
ATOM   1154 C CG    . PHE B 2 39  ? 111.674 126.374 96.168  1.00 74.80  ? 39  PHE A CG    1 
ATOM   1155 C CD1   . PHE B 2 39  ? 110.513 125.634 96.280  1.00 74.80  ? 39  PHE A CD1   1 
ATOM   1156 C CD2   . PHE B 2 39  ? 111.650 127.699 96.549  1.00 74.80  ? 39  PHE A CD2   1 
ATOM   1157 C CE1   . PHE B 2 39  ? 109.366 126.196 96.782  1.00 74.80  ? 39  PHE A CE1   1 
ATOM   1158 C CE2   . PHE B 2 39  ? 110.499 128.264 97.048  1.00 74.80  ? 39  PHE A CE2   1 
ATOM   1159 C CZ    . PHE B 2 39  ? 109.359 127.512 97.166  1.00 74.80  ? 39  PHE A CZ    1 
ATOM   1160 N N     . ASN B 2 40  ? 112.739 122.829 96.604  1.00 77.30  ? 40  ASN A N     1 
ATOM   1161 C CA    . ASN B 2 40  ? 112.073 121.684 97.211  1.00 77.30  ? 40  ASN A CA    1 
ATOM   1162 C C     . ASN B 2 40  ? 112.892 121.114 98.356  1.00 77.30  ? 40  ASN A C     1 
ATOM   1163 O O     . ASN B 2 40  ? 112.335 120.715 99.381  1.00 77.30  ? 40  ASN A O     1 
ATOM   1164 C CB    . ASN B 2 40  ? 111.816 120.607 96.164  1.00 77.30  ? 40  ASN A CB    1 
ATOM   1165 C CG    . ASN B 2 40  ? 110.595 120.888 95.344  1.00 77.30  ? 40  ASN A CG    1 
ATOM   1166 O OD1   . ASN B 2 40  ? 110.085 122.001 95.348  1.00 77.30  ? 40  ASN A OD1   1 
ATOM   1167 N ND2   . ASN B 2 40  ? 110.113 119.881 94.631  1.00 77.30  ? 40  ASN A ND2   1 
ATOM   1168 N N     . TYR B 2 41  ? 114.214 121.060 98.201  1.00 82.56  ? 41  TYR A N     1 
ATOM   1169 C CA    . TYR B 2 41  ? 115.050 120.490 99.248  1.00 82.56  ? 41  TYR A CA    1 
ATOM   1170 C C     . TYR B 2 41  ? 114.941 121.298 100.528 1.00 82.56  ? 41  TYR A C     1 
ATOM   1171 O O     . TYR B 2 41  ? 114.786 120.735 101.612 1.00 82.56  ? 41  TYR A O     1 
ATOM   1172 C CB    . TYR B 2 41  ? 116.502 120.411 98.790  1.00 82.56  ? 41  TYR A CB    1 
ATOM   1173 C CG    . TYR B 2 41  ? 117.449 120.055 99.907  1.00 82.56  ? 41  TYR A CG    1 
ATOM   1174 C CD1   . TYR B 2 41  ? 117.293 118.879 100.620 1.00 82.56  ? 41  TYR A CD1   1 
ATOM   1175 C CD2   . TYR B 2 41  ? 118.492 120.896 100.254 1.00 82.56  ? 41  TYR A CD2   1 
ATOM   1176 C CE1   . TYR B 2 41  ? 118.151 118.548 101.643 1.00 82.56  ? 41  TYR A CE1   1 
ATOM   1177 C CE2   . TYR B 2 41  ? 119.356 120.573 101.276 1.00 82.56  ? 41  TYR A CE2   1 
ATOM   1178 C CZ    . TYR B 2 41  ? 119.180 119.398 101.966 1.00 82.56  ? 41  TYR A CZ    1 
ATOM   1179 O OH    . TYR B 2 41  ? 120.040 119.071 102.987 1.00 82.56  ? 41  TYR A OH    1 
ATOM   1180 N N     . THR B 2 42  ? 115.003 122.624 100.422 1.00 77.55  ? 42  THR A N     1 
ATOM   1181 C CA    . THR B 2 42  ? 114.888 123.457 101.614 1.00 77.55  ? 42  THR A CA    1 
ATOM   1182 C C     . THR B 2 42  ? 113.491 123.370 102.214 1.00 77.55  ? 42  THR A C     1 
ATOM   1183 O O     . THR B 2 42  ? 113.340 123.260 103.439 1.00 77.55  ? 42  THR A O     1 
ATOM   1184 C CB    . THR B 2 42  ? 115.239 124.904 101.282 1.00 77.55  ? 42  THR A CB    1 
ATOM   1185 O OG1   . THR B 2 42  ? 116.556 124.960 100.724 1.00 77.55  ? 42  THR A OG1   1 
ATOM   1186 C CG2   . THR B 2 42  ? 115.199 125.754 102.533 1.00 77.55  ? 42  THR A CG2   1 
ATOM   1187 N N     . VAL B 2 43  ? 112.458 123.403 101.369 1.00 75.41  ? 43  VAL A N     1 
ATOM   1188 C CA    . VAL B 2 43  ? 111.088 123.343 101.869 1.00 75.41  ? 43  VAL A CA    1 
ATOM   1189 C C     . VAL B 2 43  ? 110.859 122.045 102.629 1.00 75.41  ? 43  VAL A C     1 
ATOM   1190 O O     . VAL B 2 43  ? 110.313 122.040 103.737 1.00 75.41  ? 43  VAL A O     1 
ATOM   1191 C CB    . VAL B 2 43  ? 110.088 123.505 100.712 1.00 75.41  ? 43  VAL A CB    1 
ATOM   1192 C CG1   . VAL B 2 43  ? 108.714 123.026 101.131 1.00 75.41  ? 43  VAL A CG1   1 
ATOM   1193 C CG2   . VAL B 2 43  ? 110.032 124.951 100.265 1.00 75.41  ? 43  VAL A CG2   1 
ATOM   1194 N N     . LEU B 2 44  ? 111.303 120.925 102.058 1.00 77.20  ? 44  LEU A N     1 
ATOM   1195 C CA    . LEU B 2 44  ? 111.106 119.636 102.705 1.00 77.20  ? 44  LEU A CA    1 
ATOM   1196 C C     . LEU B 2 44  ? 112.020 119.463 103.906 1.00 77.20  ? 44  LEU A C     1 
ATOM   1197 O O     . LEU B 2 44  ? 111.625 118.833 104.887 1.00 77.20  ? 44  LEU A O     1 
ATOM   1198 C CB    . LEU B 2 44  ? 111.333 118.511 101.703 1.00 77.20  ? 44  LEU A CB    1 
ATOM   1199 C CG    . LEU B 2 44  ? 110.414 118.519 100.487 1.00 77.20  ? 44  LEU A CG    1 
ATOM   1200 C CD1   . LEU B 2 44  ? 111.055 117.743 99.361  1.00 77.20  ? 44  LEU A CD1   1 
ATOM   1201 C CD2   . LEU B 2 44  ? 109.067 117.940 100.848 1.00 77.20  ? 44  LEU A CD2   1 
ATOM   1202 N N     . ARG B 2 45  ? 113.229 120.021 103.859 1.00 82.26  ? 45  ARG A N     1 
ATOM   1203 C CA    . ARG B 2 45  ? 114.137 119.933 104.994 1.00 82.26  ? 45  ARG A CA    1 
ATOM   1204 C C     . ARG B 2 45  ? 113.574 120.663 106.201 1.00 82.26  ? 45  ARG A C     1 
ATOM   1205 O O     . ARG B 2 45  ? 113.767 120.232 107.342 1.00 82.26  ? 45  ARG A O     1 
ATOM   1206 C CB    . ARG B 2 45  ? 115.496 120.508 104.602 1.00 82.26  ? 45  ARG A CB    1 
ATOM   1207 C CG    . ARG B 2 45  ? 116.528 120.521 105.702 1.00 82.26  ? 45  ARG A CG    1 
ATOM   1208 C CD    . ARG B 2 45  ? 117.647 121.480 105.354 1.00 82.26  ? 45  ARG A CD    1 
ATOM   1209 N NE    . ARG B 2 45  ? 118.961 120.947 105.687 1.00 82.26  ? 45  ARG A NE    1 
ATOM   1210 C CZ    . ARG B 2 45  ? 119.467 120.925 106.914 1.00 82.26  ? 45  ARG A CZ    1 
ATOM   1211 N NH1   . ARG B 2 45  ? 118.768 121.407 107.932 1.00 82.26  ? 45  ARG A NH1   1 
ATOM   1212 N NH2   . ARG B 2 45  ? 120.675 120.424 107.125 1.00 82.26  ? 45  ARG A NH2   1 
ATOM   1213 N N     . ASP B 2 46  ? 112.872 121.769 105.971 1.00 78.91  ? 46  ASP A N     1 
ATOM   1214 C CA    . ASP B 2 46  ? 112.258 122.469 107.092 1.00 78.91  ? 46  ASP A CA    1 
ATOM   1215 C C     . ASP B 2 46  ? 110.947 121.814 107.512 1.00 78.91  ? 46  ASP A C     1 
ATOM   1216 O O     . ASP B 2 46  ? 110.652 121.719 108.710 1.00 78.91  ? 46  ASP A O     1 
ATOM   1217 C CB    . ASP B 2 46  ? 112.049 123.937 106.733 1.00 78.91  ? 46  ASP A CB    1 
ATOM   1218 C CG    . ASP B 2 46  ? 113.355 124.653 106.454 1.00 78.91  ? 46  ASP A CG    1 
ATOM   1219 O OD1   . ASP B 2 46  ? 114.403 124.198 106.955 1.00 78.91  ? 46  ASP A OD1   1 
ATOM   1220 O OD2   . ASP B 2 46  ? 113.341 125.671 105.735 1.00 78.91  ? 46  ASP A OD2   1 
ATOM   1221 N N     . THR B 2 47  ? 110.164 121.329 106.546 1.00 78.46  ? 47  THR A N     1 
ATOM   1222 C CA    . THR B 2 47  ? 108.871 120.740 106.870 1.00 78.46  ? 47  THR A CA    1 
ATOM   1223 C C     . THR B 2 47  ? 109.025 119.405 107.586 1.00 78.46  ? 47  THR A C     1 
ATOM   1224 O O     . THR B 2 47  ? 108.201 119.060 108.438 1.00 78.46  ? 47  THR A O     1 
ATOM   1225 C CB    . THR B 2 47  ? 108.045 120.573 105.598 1.00 78.46  ? 47  THR A CB    1 
ATOM   1226 O OG1   . THR B 2 47  ? 108.099 121.785 104.837 1.00 78.46  ? 47  THR A OG1   1 
ATOM   1227 C CG2   . THR B 2 47  ? 106.602 120.269 105.940 1.00 78.46  ? 47  THR A CG2   1 
ATOM   1228 N N     . LYS B 2 48  ? 110.073 118.643 107.270 1.00 77.16  ? 48  LYS A N     1 
ATOM   1229 C CA    . LYS B 2 48  ? 110.273 117.363 107.938 1.00 77.16  ? 48  LYS A CA    1 
ATOM   1230 C C     . LYS B 2 48  ? 110.630 117.567 109.402 1.00 77.16  ? 48  LYS A C     1 
ATOM   1231 O O     . LYS B 2 48  ? 110.139 116.842 110.275 1.00 77.16  ? 48  LYS A O     1 
ATOM   1232 C CB    . LYS B 2 48  ? 111.352 116.553 107.219 1.00 77.16  ? 48  LYS A CB    1 
ATOM   1233 C CG    . LYS B 2 48  ? 112.760 117.098 107.368 1.00 77.16  ? 48  LYS A CG    1 
ATOM   1234 C CD    . LYS B 2 48  ? 113.793 116.209 106.718 1.00 77.16  ? 48  LYS A CD    1 
ATOM   1235 C CE    . LYS B 2 48  ? 115.184 116.743 106.983 1.00 77.16  ? 48  LYS A CE    1 
ATOM   1236 N NZ    . LYS B 2 48  ? 116.214 116.015 106.205 1.00 77.16  ? 48  LYS A NZ    1 
ATOM   1237 N N     . ASP B 2 49  ? 111.465 118.566 109.694 1.00 79.99  ? 49  ASP A N     1 
ATOM   1238 C CA    . ASP B 2 49  ? 111.754 118.891 111.083 1.00 79.99  ? 49  ASP A CA    1 
ATOM   1239 C C     . ASP B 2 49  ? 110.507 119.397 111.783 1.00 79.99  ? 49  ASP A C     1 
ATOM   1240 O O     . ASP B 2 49  ? 110.220 118.998 112.912 1.00 79.99  ? 49  ASP A O     1 
ATOM   1241 C CB    . ASP B 2 49  ? 112.874 119.924 111.169 1.00 79.99  ? 49  ASP A CB    1 
ATOM   1242 C CG    . ASP B 2 49  ? 114.211 119.368 110.731 1.00 79.99  ? 49  ASP A CG    1 
ATOM   1243 O OD1   . ASP B 2 49  ? 114.604 118.295 111.233 1.00 79.99  ? 49  ASP A OD1   1 
ATOM   1244 O OD2   . ASP B 2 49  ? 114.872 120.008 109.887 1.00 79.99  ? 49  ASP A OD2   1 
ATOM   1245 N N     . THR B 2 50  ? 109.744 120.270 111.123 1.00 77.38  ? 50  THR A N     1 
ATOM   1246 C CA    . THR B 2 50  ? 108.488 120.733 111.703 1.00 77.38  ? 50  THR A CA    1 
ATOM   1247 C C     . THR B 2 50  ? 107.596 119.560 112.085 1.00 77.38  ? 50  THR A C     1 
ATOM   1248 O O     . THR B 2 50  ? 107.108 119.478 113.217 1.00 77.38  ? 50  THR A O     1 
ATOM   1249 C CB    . THR B 2 50  ? 107.768 121.653 110.720 1.00 77.38  ? 50  THR A CB    1 
ATOM   1250 O OG1   . THR B 2 50  ? 108.643 122.720 110.340 1.00 77.38  ? 50  THR A OG1   1 
ATOM   1251 C CG2   . THR B 2 50  ? 106.523 122.232 111.355 1.00 77.38  ? 50  THR A CG2   1 
ATOM   1252 N N     . LEU B 2 51  ? 107.409 118.619 111.160 1.00 75.25  ? 51  LEU A N     1 
ATOM   1253 C CA    . LEU B 2 51  ? 106.490 117.509 111.384 1.00 75.25  ? 51  LEU A CA    1 
ATOM   1254 C C     . LEU B 2 51  ? 106.995 116.575 112.475 1.00 75.25  ? 51  LEU A C     1 
ATOM   1255 O O     . LEU B 2 51  ? 106.224 116.146 113.339 1.00 75.25  ? 51  LEU A O     1 
ATOM   1256 C CB    . LEU B 2 51  ? 106.278 116.741 110.082 1.00 75.25  ? 51  LEU A CB    1 
ATOM   1257 C CG    . LEU B 2 51  ? 105.402 117.399 109.022 1.00 75.25  ? 51  LEU A CG    1 
ATOM   1258 C CD1   . LEU B 2 51  ? 105.500 116.623 107.732 1.00 75.25  ? 51  LEU A CD1   1 
ATOM   1259 C CD2   . LEU B 2 51  ? 103.967 117.468 109.490 1.00 75.25  ? 51  LEU A CD2   1 
ATOM   1260 N N     . ILE B 2 52  ? 108.284 116.235 112.450 1.00 77.19  ? 52  ILE A N     1 
ATOM   1261 C CA    . ILE B 2 52  ? 108.807 115.272 113.414 1.00 77.19  ? 52  ILE A CA    1 
ATOM   1262 C C     . ILE B 2 52  ? 108.889 115.886 114.804 1.00 77.19  ? 52  ILE A C     1 
ATOM   1263 O O     . ILE B 2 52  ? 108.484 115.269 115.795 1.00 77.19  ? 52  ILE A O     1 
ATOM   1264 C CB    . ILE B 2 52  ? 110.170 114.731 112.952 1.00 77.19  ? 52  ILE A CB    1 
ATOM   1265 C CG1   . ILE B 2 52  ? 109.990 113.889 111.695 1.00 77.19  ? 52  ILE A CG1   1 
ATOM   1266 C CG2   . ILE B 2 52  ? 110.820 113.912 114.047 1.00 77.19  ? 52  ILE A CG2   1 
ATOM   1267 C CD1   . ILE B 2 52  ? 109.095 112.694 111.911 1.00 77.19  ? 52  ILE A CD1   1 
ATOM   1268 N N     . VAL B 2 53  ? 109.411 117.107 114.904 1.00 76.39  ? 53  VAL A N     1 
ATOM   1269 C CA    . VAL B 2 53  ? 109.612 117.716 116.210 1.00 76.39  ? 53  VAL A CA    1 
ATOM   1270 C C     . VAL B 2 53  ? 108.283 118.147 116.817 1.00 76.39  ? 53  VAL A C     1 
ATOM   1271 O O     . VAL B 2 53  ? 108.067 118.007 118.025 1.00 76.39  ? 53  VAL A O     1 
ATOM   1272 C CB    . VAL B 2 53  ? 110.599 118.888 116.091 1.00 76.39  ? 53  VAL A CB    1 
ATOM   1273 C CG1   . VAL B 2 53  ? 110.853 119.490 117.436 1.00 76.39  ? 53  VAL A CG1   1 
ATOM   1274 C CG2   . VAL B 2 53  ? 111.905 118.413 115.487 1.00 76.39  ? 53  VAL A CG2   1 
ATOM   1275 N N     . GLY B 2 54  ? 107.369 118.664 116.002 1.00 77.52  ? 54  GLY A N     1 
ATOM   1276 C CA    . GLY B 2 54  ? 106.098 119.111 116.525 1.00 77.52  ? 54  GLY A CA    1 
ATOM   1277 C C     . GLY B 2 54  ? 105.015 118.065 116.615 1.00 77.52  ? 54  GLY A C     1 
ATOM   1278 O O     . GLY B 2 54  ? 103.878 118.397 116.961 1.00 77.52  ? 54  GLY A O     1 
ATOM   1279 N N     . ALA B 2 55  ? 105.322 116.807 116.317 1.00 80.40  ? 55  ALA A N     1 
ATOM   1280 C CA    . ALA B 2 55  ? 104.300 115.776 116.320 1.00 80.40  ? 55  ALA A CA    1 
ATOM   1281 C C     . ALA B 2 55  ? 103.858 115.463 117.748 1.00 80.40  ? 55  ALA A C     1 
ATOM   1282 O O     . ALA B 2 55  ? 104.599 115.704 118.703 1.00 80.40  ? 55  ALA A O     1 
ATOM   1283 C CB    . ALA B 2 55  ? 104.821 114.509 115.651 1.00 80.40  ? 55  ALA A CB    1 
ATOM   1284 N N     . PRO B 2 56  ? 102.648 114.935 117.920 1.00 84.61  ? 56  PRO A N     1 
ATOM   1285 C CA    . PRO B 2 56  ? 102.216 114.512 119.257 1.00 84.61  ? 56  PRO A CA    1 
ATOM   1286 C C     . PRO B 2 56  ? 103.054 113.345 119.754 1.00 84.61  ? 56  PRO A C     1 
ATOM   1287 O O     . PRO B 2 56  ? 103.241 112.350 119.052 1.00 84.61  ? 56  PRO A O     1 
ATOM   1288 C CB    . PRO B 2 56  ? 100.753 114.109 119.046 1.00 84.61  ? 56  PRO A CB    1 
ATOM   1289 C CG    . PRO B 2 56  ? 100.338 114.821 117.807 1.00 84.61  ? 56  PRO A CG    1 
ATOM   1290 C CD    . PRO B 2 56  ? 101.553 114.853 116.941 1.00 84.61  ? 56  PRO A CD    1 
ATOM   1291 N N     . GLY B 2 57  ? 103.562 113.475 120.976 1.00 85.21  ? 57  GLY A N     1 
ATOM   1292 C CA    . GLY B 2 57  ? 104.373 112.426 121.556 1.00 85.21  ? 57  GLY A CA    1 
ATOM   1293 C C     . GLY B 2 57  ? 105.742 112.262 120.944 1.00 85.21  ? 57  GLY A C     1 
ATOM   1294 O O     . GLY B 2 57  ? 106.413 111.265 121.221 1.00 85.21  ? 57  GLY A O     1 
ATOM   1295 N N     . SER B 2 58  ? 106.178 113.206 120.122 1.00 81.41  ? 58  SER A N     1 
ATOM   1296 C CA    . SER B 2 58  ? 107.479 113.163 119.475 1.00 81.41  ? 58  SER A CA    1 
ATOM   1297 C C     . SER B 2 58  ? 108.304 114.367 119.916 1.00 81.41  ? 58  SER A C     1 
ATOM   1298 O O     . SER B 2 58  ? 107.905 115.136 120.793 1.00 81.41  ? 58  SER A O     1 
ATOM   1299 C CB    . SER B 2 58  ? 107.320 113.119 117.955 1.00 81.41  ? 58  SER A CB    1 
ATOM   1300 O OG    . SER B 2 58  ? 108.580 113.171 117.314 1.00 81.41  ? 58  SER A OG    1 
ATOM   1301 N N     . GLY B 2 59  ? 109.465 114.526 119.297 1.00 79.44  ? 59  GLY A N     1 
ATOM   1302 C CA    . GLY B 2 59  ? 110.329 115.640 119.627 1.00 79.44  ? 59  GLY A CA    1 
ATOM   1303 C C     . GLY B 2 59  ? 111.614 115.555 118.841 1.00 79.44  ? 59  GLY A C     1 
ATOM   1304 O O     . GLY B 2 59  ? 111.726 114.792 117.880 1.00 79.44  ? 59  GLY A O     1 
ATOM   1305 N N     . ALA B 2 60  ? 112.593 116.352 119.265 1.00 80.47  ? 60  ALA A N     1 
ATOM   1306 C CA    . ALA B 2 60  ? 113.889 116.326 118.604 1.00 80.47  ? 60  ALA A CA    1 
ATOM   1307 C C     . ALA B 2 60  ? 114.634 115.025 118.849 1.00 80.47  ? 60  ALA A C     1 
ATOM   1308 O O     . ALA B 2 60  ? 115.584 114.724 118.120 1.00 80.47  ? 60  ALA A O     1 
ATOM   1309 C CB    . ALA B 2 60  ? 114.741 117.506 119.063 1.00 80.47  ? 60  ALA A CB    1 
ATOM   1310 N N     . GLU B 2 61  ? 114.230 114.248 119.855 1.00 83.47  ? 61  GLU A N     1 
ATOM   1311 C CA    . GLU B 2 61  ? 114.891 112.978 120.123 1.00 83.47  ? 61  GLU A CA    1 
ATOM   1312 C C     . GLU B 2 61  ? 114.635 111.953 119.032 1.00 83.47  ? 61  GLU A C     1 
ATOM   1313 O O     . GLU B 2 61  ? 115.416 111.007 118.895 1.00 83.47  ? 61  GLU A O     1 
ATOM   1314 C CB    . GLU B 2 61  ? 114.435 112.420 121.468 1.00 83.47  ? 61  GLU A CB    1 
ATOM   1315 C CG    . GLU B 2 61  ? 112.935 112.324 121.610 1.00 83.47  ? 61  GLU A CG    1 
ATOM   1316 C CD    . GLU B 2 61  ? 112.368 113.443 122.452 1.00 83.47  ? 61  GLU A CD    1 
ATOM   1317 O OE1   . GLU B 2 61  ? 113.138 114.347 122.834 1.00 83.47  ? 61  GLU A OE1   1 
ATOM   1318 O OE2   . GLU B 2 61  ? 111.151 113.424 122.730 1.00 83.47  ? 61  GLU A OE2   1 
ATOM   1319 N N     . ALA B 2 62  ? 113.563 112.111 118.259 1.00 78.75  ? 62  ALA A N     1 
ATOM   1320 C CA    . ALA B 2 62  ? 113.285 111.188 117.170 1.00 78.75  ? 62  ALA A CA    1 
ATOM   1321 C C     . ALA B 2 62  ? 114.199 111.403 115.977 1.00 78.75  ? 62  ALA A C     1 
ATOM   1322 O O     . ALA B 2 62  ? 114.268 110.536 115.103 1.00 78.75  ? 62  ALA A O     1 
ATOM   1323 C CB    . ALA B 2 62  ? 111.827 111.317 116.730 1.00 78.75  ? 62  ALA A CB    1 
ATOM   1324 N N     . ILE B 2 63  ? 114.909 112.527 115.928 1.00 78.10  ? 63  ILE A N     1 
ATOM   1325 C CA    . ILE B 2 63  ? 115.724 112.840 114.754 1.00 78.10  ? 63  ILE A CA    1 
ATOM   1326 C C     . ILE B 2 63  ? 116.932 111.919 114.626 1.00 78.10  ? 63  ILE A C     1 
ATOM   1327 O O     . ILE B 2 63  ? 117.158 111.383 113.527 1.00 78.10  ? 63  ILE A O     1 
ATOM   1328 C CB    . ILE B 2 63  ? 116.107 114.328 114.761 1.00 78.10  ? 63  ILE A CB    1 
ATOM   1329 C CG1   . ILE B 2 63  ? 114.857 115.187 114.578 1.00 78.10  ? 63  ILE A CG1   1 
ATOM   1330 C CG2   . ILE B 2 63  ? 117.126 114.622 113.679 1.00 78.10  ? 63  ILE A CG2   1 
ATOM   1331 C CD1   . ILE B 2 63  ? 115.101 116.660 114.741 1.00 78.10  ? 63  ILE A CD1   1 
ATOM   1332 N N     . PRO B 2 64  ? 117.745 111.691 115.667 1.00 80.71  ? 64  PRO A N     1 
ATOM   1333 C CA    . PRO B 2 64  ? 118.870 110.764 115.495 1.00 80.71  ? 64  PRO A CA    1 
ATOM   1334 C C     . PRO B 2 64  ? 118.429 109.333 115.280 1.00 80.71  ? 64  PRO A C     1 
ATOM   1335 O O     . PRO B 2 64  ? 119.171 108.553 114.671 1.00 80.71  ? 64  PRO A O     1 
ATOM   1336 C CB    . PRO B 2 64  ? 119.658 110.921 116.801 1.00 80.71  ? 64  PRO A CB    1 
ATOM   1337 C CG    . PRO B 2 64  ? 118.652 111.341 117.781 1.00 80.71  ? 64  PRO A CG    1 
ATOM   1338 C CD    . PRO B 2 64  ? 117.731 112.252 117.031 1.00 80.71  ? 64  PRO A CD    1 
ATOM   1339 N N     . PHE B 2 65  ? 117.243 108.960 115.758 1.00 76.65  ? 65  PHE A N     1 
ATOM   1340 C CA    . PHE B 2 65  ? 116.753 107.610 115.515 1.00 76.65  ? 65  PHE A CA    1 
ATOM   1341 C C     . PHE B 2 65  ? 116.288 107.447 114.077 1.00 76.65  ? 65  PHE A C     1 
ATOM   1342 O O     . PHE B 2 65  ? 116.565 106.423 113.445 1.00 76.65  ? 65  PHE A O     1 
ATOM   1343 C CB    . PHE B 2 65  ? 115.627 107.276 116.485 1.00 76.65  ? 65  PHE A CB    1 
ATOM   1344 C CG    . PHE B 2 65  ? 116.104 106.904 117.851 1.00 76.65  ? 65  PHE A CG    1 
ATOM   1345 C CD1   . PHE B 2 65  ? 116.459 105.603 118.141 1.00 76.65  ? 65  PHE A CD1   1 
ATOM   1346 C CD2   . PHE B 2 65  ? 116.202 107.856 118.844 1.00 76.65  ? 65  PHE A CD2   1 
ATOM   1347 C CE1   . PHE B 2 65  ? 116.899 105.258 119.395 1.00 76.65  ? 65  PHE A CE1   1 
ATOM   1348 C CE2   . PHE B 2 65  ? 116.643 107.516 120.100 1.00 76.65  ? 65  PHE A CE2   1 
ATOM   1349 C CZ    . PHE B 2 65  ? 116.991 106.216 120.376 1.00 76.65  ? 65  PHE A CZ    1 
ATOM   1350 N N     . ILE B 2 66  ? 115.578 108.439 113.541 1.00 77.24  ? 66  ILE A N     1 
ATOM   1351 C CA    . ILE B 2 66  ? 115.180 108.382 112.138 1.00 77.24  ? 66  ILE A CA    1 
ATOM   1352 C C     . ILE B 2 66  ? 116.414 108.364 111.250 1.00 77.24  ? 66  ILE A C     1 
ATOM   1353 O O     . ILE B 2 66  ? 116.636 107.414 110.493 1.00 77.24  ? 66  ILE A O     1 
ATOM   1354 C CB    . ILE B 2 66  ? 114.254 109.555 111.779 1.00 77.24  ? 66  ILE A CB    1 
ATOM   1355 C CG1   . ILE B 2 66  ? 112.935 109.450 112.533 1.00 77.24  ? 66  ILE A CG1   1 
ATOM   1356 C CG2   . ILE B 2 66  ? 113.986 109.560 110.294 1.00 77.24  ? 66  ILE A CG2   1 
ATOM   1357 C CD1   . ILE B 2 66  ? 111.962 110.537 112.201 1.00 77.24  ? 66  ILE A CD1   1 
ATOM   1358 N N     . LYS B 2 67  ? 117.264 109.387 111.385 1.00 80.33  ? 67  LYS A N     1 
ATOM   1359 C CA    . LYS B 2 67  ? 118.406 109.579 110.496 1.00 80.33  ? 67  LYS A CA    1 
ATOM   1360 C C     . LYS B 2 67  ? 119.268 108.335 110.341 1.00 80.33  ? 67  LYS A C     1 
ATOM   1361 O O     . LYS B 2 67  ? 120.029 108.239 109.373 1.00 80.33  ? 67  LYS A O     1 
ATOM   1362 C CB    . LYS B 2 67  ? 119.274 110.728 111.008 1.00 80.33  ? 67  LYS A CB    1 
ATOM   1363 C CG    . LYS B 2 67  ? 118.877 112.088 110.481 1.00 80.33  ? 67  LYS A CG    1 
ATOM   1364 C CD    . LYS B 2 67  ? 119.911 113.131 110.848 1.00 80.33  ? 67  LYS A CD    1 
ATOM   1365 C CE    . LYS B 2 67  ? 119.606 114.457 110.182 1.00 80.33  ? 67  LYS A CE    1 
ATOM   1366 N NZ    . LYS B 2 67  ? 119.569 114.326 108.703 1.00 80.33  ? 67  LYS A NZ    1 
ATOM   1367 N N     . PHE B 2 68  ? 119.174 107.383 111.264 1.00 80.49  ? 68  PHE A N     1 
ATOM   1368 C CA    . PHE B 2 68  ? 119.950 106.156 111.189 1.00 80.49  ? 68  PHE A CA    1 
ATOM   1369 C C     . PHE B 2 68  ? 119.101 104.931 110.891 1.00 80.49  ? 68  PHE A C     1 
ATOM   1370 O O     . PHE B 2 68  ? 119.394 104.199 109.946 1.00 80.49  ? 68  PHE A O     1 
ATOM   1371 C CB    . PHE B 2 68  ? 120.725 105.946 112.494 1.00 80.49  ? 68  PHE A CB    1 
ATOM   1372 C CG    . PHE B 2 68  ? 121.636 104.758 112.472 1.00 80.49  ? 68  PHE A CG    1 
ATOM   1373 C CD1   . PHE B 2 68  ? 122.830 104.800 111.778 1.00 80.49  ? 68  PHE A CD1   1 
ATOM   1374 C CD2   . PHE B 2 68  ? 121.301 103.600 113.146 1.00 80.49  ? 68  PHE A CD2   1 
ATOM   1375 C CE1   . PHE B 2 68  ? 123.669 103.710 111.754 1.00 80.49  ? 68  PHE A CE1   1 
ATOM   1376 C CE2   . PHE B 2 68  ? 122.137 102.507 113.125 1.00 80.49  ? 68  PHE A CE2   1 
ATOM   1377 C CZ    . PHE B 2 68  ? 123.322 102.562 112.428 1.00 80.49  ? 68  PHE A CZ    1 
ATOM   1378 N N     . TRP B 2 69  ? 118.048 104.677 111.664 1.00 78.02  ? 69  TRP A N     1 
ATOM   1379 C CA    . TRP B 2 69  ? 117.299 103.444 111.485 1.00 78.02  ? 69  TRP A CA    1 
ATOM   1380 C C     . TRP B 2 69  ? 116.291 103.504 110.347 1.00 78.02  ? 69  TRP A C     1 
ATOM   1381 O O     . TRP B 2 69  ? 115.695 102.471 110.028 1.00 78.02  ? 69  TRP A O     1 
ATOM   1382 C CB    . TRP B 2 69  ? 116.580 103.080 112.783 1.00 78.02  ? 69  TRP A CB    1 
ATOM   1383 C CG    . TRP B 2 69  ? 117.510 102.677 113.872 1.00 78.02  ? 69  TRP A CG    1 
ATOM   1384 C CD1   . TRP B 2 69  ? 117.693 103.305 115.063 1.00 78.02  ? 69  TRP A CD1   1 
ATOM   1385 C CD2   . TRP B 2 69  ? 118.392 101.552 113.871 1.00 78.02  ? 69  TRP A CD2   1 
ATOM   1386 N NE1   . TRP B 2 69  ? 118.634 102.643 115.807 1.00 78.02  ? 69  TRP A NE1   1 
ATOM   1387 C CE2   . TRP B 2 69  ? 119.079 101.561 115.096 1.00 78.02  ? 69  TRP A CE2   1 
ATOM   1388 C CE3   . TRP B 2 69  ? 118.667 100.537 112.952 1.00 78.02  ? 69  TRP A CE3   1 
ATOM   1389 C CZ2   . TRP B 2 69  ? 120.022 100.596 115.428 1.00 78.02  ? 69  TRP A CZ2   1 
ATOM   1390 C CZ3   . TRP B 2 69  ? 119.602 99.582  113.282 1.00 78.02  ? 69  TRP A CZ3   1 
ATOM   1391 C CH2   . TRP B 2 69  ? 120.269 99.617  114.509 1.00 78.02  ? 69  TRP A CH2   1 
ATOM   1392 N N     . LEU B 2 70  ? 116.079 104.660 109.730 1.00 77.61  ? 70  LEU A N     1 
ATOM   1393 C CA    . LEU B 2 70  ? 115.158 104.742 108.607 1.00 77.61  ? 70  LEU A CA    1 
ATOM   1394 C C     . LEU B 2 70  ? 115.787 105.367 107.377 1.00 77.61  ? 70  LEU A C     1 
ATOM   1395 O O     . LEU B 2 70  ? 115.484 104.945 106.262 1.00 77.61  ? 70  LEU A O     1 
ATOM   1396 C CB    . LEU B 2 70  ? 113.916 105.544 108.996 1.00 77.61  ? 70  LEU A CB    1 
ATOM   1397 C CG    . LEU B 2 70  ? 112.871 104.842 109.853 1.00 77.61  ? 70  LEU A CG    1 
ATOM   1398 C CD1   . LEU B 2 70  ? 111.587 105.638 109.823 1.00 77.61  ? 70  LEU A CD1   1 
ATOM   1399 C CD2   . LEU B 2 70  ? 112.639 103.434 109.354 1.00 77.61  ? 70  LEU A CD2   1 
ATOM   1400 N N     . VAL B 2 71  ? 116.656 106.360 107.548 1.00 80.31  ? 71  VAL A N     1 
ATOM   1401 C CA    . VAL B 2 71  ? 117.157 107.097 106.395 1.00 80.31  ? 71  VAL A CA    1 
ATOM   1402 C C     . VAL B 2 71  ? 118.168 106.263 105.621 1.00 80.31  ? 71  VAL A C     1 
ATOM   1403 O O     . VAL B 2 71  ? 118.053 106.107 104.401 1.00 80.31  ? 71  VAL A O     1 
ATOM   1404 C CB    . VAL B 2 71  ? 117.749 108.447 106.831 1.00 80.31  ? 71  VAL A CB    1 
ATOM   1405 C CG1   . VAL B 2 71  ? 118.541 109.059 105.696 1.00 80.31  ? 71  VAL A CG1   1 
ATOM   1406 C CG2   . VAL B 2 71  ? 116.640 109.388 107.258 1.00 80.31  ? 71  VAL A CG2   1 
ATOM   1407 N N     . VAL B 2 72  ? 119.162 105.705 106.306 1.00 82.81  ? 72  VAL A N     1 
ATOM   1408 C CA    . VAL B 2 72  ? 120.218 104.991 105.588 1.00 82.81  ? 72  VAL A CA    1 
ATOM   1409 C C     . VAL B 2 72  ? 119.755 103.624 105.083 1.00 82.81  ? 72  VAL A C     1 
ATOM   1410 O O     . VAL B 2 72  ? 120.189 103.227 103.994 1.00 82.81  ? 72  VAL A O     1 
ATOM   1411 C CB    . VAL B 2 72  ? 121.512 104.880 106.419 1.00 82.81  ? 72  VAL A CB    1 
ATOM   1412 C CG1   . VAL B 2 72  ? 122.000 106.259 106.830 1.00 82.81  ? 72  VAL A CG1   1 
ATOM   1413 C CG2   . VAL B 2 72  ? 121.375 103.978 107.614 1.00 82.81  ? 72  VAL A CG2   1 
ATOM   1414 N N     . PRO B 2 73  ? 118.884 102.865 105.768 1.00 83.09  ? 73  PRO A N     1 
ATOM   1415 C CA    . PRO B 2 73  ? 118.411 101.632 105.120 1.00 83.09  ? 73  PRO A CA    1 
ATOM   1416 C C     . PRO B 2 73  ? 117.514 101.913 103.932 1.00 83.09  ? 73  PRO A C     1 
ATOM   1417 O O     . PRO B 2 73  ? 117.619 101.229 102.907 1.00 83.09  ? 73  PRO A O     1 
ATOM   1418 C CB    . PRO B 2 73  ? 117.673 100.902 106.247 1.00 83.09  ? 73  PRO A CB    1 
ATOM   1419 C CG    . PRO B 2 73  ? 117.203 101.962 107.113 1.00 83.09  ? 73  PRO A CG    1 
ATOM   1420 C CD    . PRO B 2 73  ? 118.260 103.017 107.096 1.00 83.09  ? 73  PRO A CD    1 
ATOM   1421 N N     . CYS B 2 74  ? 116.641 102.917 104.028 1.00 85.68  ? 74  CYS A N     1 
ATOM   1422 C CA    . CYS B 2 74  ? 115.886 103.335 102.854 1.00 85.68  ? 74  CYS A CA    1 
ATOM   1423 C C     . CYS B 2 74  ? 116.804 103.914 101.790 1.00 85.68  ? 74  CYS A C     1 
ATOM   1424 O O     . CYS B 2 74  ? 116.523 103.786 100.596 1.00 85.68  ? 74  CYS A O     1 
ATOM   1425 C CB    . CYS B 2 74  ? 114.813 104.347 103.242 1.00 85.68  ? 74  CYS A CB    1 
ATOM   1426 S SG    . CYS B 2 74  ? 113.486 103.661 104.242 1.00 85.68  ? 74  CYS A SG    1 
ATOM   1427 N N     . ALA B 2 75  ? 117.919 104.523 102.195 1.00 85.54  ? 75  ALA A N     1 
ATOM   1428 C CA    . ALA B 2 75  ? 118.888 105.003 101.218 1.00 85.54  ? 75  ALA A CA    1 
ATOM   1429 C C     . ALA B 2 75  ? 119.484 103.845 100.430 1.00 85.54  ? 75  ALA A C     1 
ATOM   1430 O O     . ALA B 2 75  ? 119.583 103.905 99.201  1.00 85.54  ? 75  ALA A O     1 
ATOM   1431 C CB    . ALA B 2 75  ? 119.987 105.807 101.912 1.00 85.54  ? 75  ALA A CB    1 
ATOM   1432 N N     . ILE B 2 76  ? 119.880 102.773 101.122 1.00 87.47  ? 76  ILE A N     1 
ATOM   1433 C CA    . ILE B 2 76  ? 120.446 101.617 100.431 1.00 87.47  ? 76  ILE A CA    1 
ATOM   1434 C C     . ILE B 2 76  ? 119.392 100.939 99.568  1.00 87.47  ? 76  ILE A C     1 
ATOM   1435 O O     . ILE B 2 76  ? 119.675 100.497 98.448  1.00 87.47  ? 76  ILE A O     1 
ATOM   1436 C CB    . ILE B 2 76  ? 121.063 100.630 101.439 1.00 87.47  ? 76  ILE A CB    1 
ATOM   1437 C CG1   . ILE B 2 76  ? 121.976 101.359 102.422 1.00 87.47  ? 76  ILE A CG1   1 
ATOM   1438 C CG2   . ILE B 2 76  ? 121.820 99.533  100.717 1.00 87.47  ? 76  ILE A CG2   1 
ATOM   1439 C CD1   . ILE B 2 76  ? 123.198 101.965 101.778 1.00 87.47  ? 76  ILE A CD1   1 
ATOM   1440 N N     . ILE B 2 77  ? 118.160 100.849 100.069 1.00 87.70  ? 77  ILE A N     1 
ATOM   1441 C CA    . ILE B 2 77  ? 117.085 100.247 99.286  1.00 87.70  ? 77  ILE A CA    1 
ATOM   1442 C C     . ILE B 2 77  ? 116.861 101.039 98.004  1.00 87.70  ? 77  ILE A C     1 
ATOM   1443 O O     . ILE B 2 77  ? 116.751 100.470 96.911  1.00 87.70  ? 77  ILE A O     1 
ATOM   1444 C CB    . ILE B 2 77  ? 115.799 100.151 100.125 1.00 87.70  ? 77  ILE A CB    1 
ATOM   1445 C CG1   . ILE B 2 77  ? 115.959 99.102  101.224 1.00 87.70  ? 77  ILE A CG1   1 
ATOM   1446 C CG2   . ILE B 2 77  ? 114.611 99.817  99.243  1.00 87.70  ? 77  ILE A CG2   1 
ATOM   1447 C CD1   . ILE B 2 77  ? 114.832 99.100  102.231 1.00 87.70  ? 77  ILE A CD1   1 
ATOM   1448 N N     . PHE B 2 78  ? 116.810 102.367 98.116  1.00 91.13  ? 78  PHE A N     1 
ATOM   1449 C CA    . PHE B 2 78  ? 116.573 103.193 96.941  1.00 91.13  ? 78  PHE A CA    1 
ATOM   1450 C C     . PHE B 2 78  ? 117.750 103.134 95.984  1.00 91.13  ? 78  PHE A C     1 
ATOM   1451 O O     . PHE B 2 78  ? 117.558 103.145 94.767  1.00 91.13  ? 78  PHE A O     1 
ATOM   1452 C CB    . PHE B 2 78  ? 116.289 104.638 97.347  1.00 91.13  ? 78  PHE A CB    1 
ATOM   1453 C CG    . PHE B 2 78  ? 115.685 105.465 96.246  1.00 91.13  ? 78  PHE A CG    1 
ATOM   1454 C CD1   . PHE B 2 78  ? 116.479 106.019 95.258  1.00 91.13  ? 78  PHE A CD1   1 
ATOM   1455 C CD2   . PHE B 2 78  ? 114.318 105.677 96.196  1.00 91.13  ? 78  PHE A CD2   1 
ATOM   1456 C CE1   . PHE B 2 78  ? 115.923 106.768 94.245  1.00 91.13  ? 78  PHE A CE1   1 
ATOM   1457 C CE2   . PHE B 2 78  ? 113.756 106.428 95.186  1.00 91.13  ? 78  PHE A CE2   1 
ATOM   1458 C CZ    . PHE B 2 78  ? 114.561 106.974 94.210  1.00 91.13  ? 78  PHE A CZ    1 
ATOM   1459 N N     . MET B 2 79  ? 118.976 103.078 96.507  1.00 93.68  ? 79  MET A N     1 
ATOM   1460 C CA    . MET B 2 79  ? 120.136 102.988 95.628  1.00 93.68  ? 79  MET A CA    1 
ATOM   1461 C C     . MET B 2 79  ? 120.143 101.670 94.867  1.00 93.68  ? 79  MET A C     1 
ATOM   1462 O O     . MET B 2 79  ? 120.492 101.634 93.684  1.00 93.68  ? 79  MET A O     1 
ATOM   1463 C CB    . MET B 2 79  ? 121.424 103.156 96.430  1.00 93.68  ? 79  MET A CB    1 
ATOM   1464 C CG    . MET B 2 79  ? 121.662 104.572 96.917  1.00 93.68  ? 79  MET A CG    1 
ATOM   1465 S SD    . MET B 2 79  ? 121.449 105.801 95.619  1.00 93.68  ? 79  MET A SD    1 
ATOM   1466 C CE    . MET B 2 79  ? 122.752 105.321 94.489  1.00 93.68  ? 79  MET A CE    1 
ATOM   1467 N N     . LEU B 2 80  ? 119.733 100.581 95.518  1.00 92.99  ? 80  LEU A N     1 
ATOM   1468 C CA    . LEU B 2 80  ? 119.641 99.307  94.813  1.00 92.99  ? 80  LEU A CA    1 
ATOM   1469 C C     . LEU B 2 80  ? 118.550 99.341  93.751  1.00 92.99  ? 80  LEU A C     1 
ATOM   1470 O O     . LEU B 2 80  ? 118.760 98.883  92.618  1.00 92.99  ? 80  LEU A O     1 
ATOM   1471 C CB    . LEU B 2 80  ? 119.388 98.172  95.803  1.00 92.99  ? 80  LEU A CB    1 
ATOM   1472 C CG    . LEU B 2 80  ? 120.548 97.829  96.737  1.00 92.99  ? 80  LEU A CG    1 
ATOM   1473 C CD1   . LEU B 2 80  ? 120.111 96.805  97.768  1.00 92.99  ? 80  LEU A CD1   1 
ATOM   1474 C CD2   . LEU B 2 80  ? 121.744 97.325  95.946  1.00 92.99  ? 80  LEU A CD2   1 
ATOM   1475 N N     . ILE B 2 81  ? 117.378 99.878  94.098  1.00 92.92  ? 81  ILE A N     1 
ATOM   1476 C CA    . ILE B 2 81  ? 116.293 99.971  93.124  1.00 92.92  ? 81  ILE A CA    1 
ATOM   1477 C C     . ILE B 2 81  ? 116.714 100.834 91.943  1.00 92.92  ? 81  ILE A C     1 
ATOM   1478 O O     . ILE B 2 81  ? 116.433 100.508 90.787  1.00 92.92  ? 81  ILE A O     1 
ATOM   1479 C CB    . ILE B 2 81  ? 115.016 100.510 93.793  1.00 92.92  ? 81  ILE A CB    1 
ATOM   1480 C CG1   . ILE B 2 81  ? 114.478 99.503  94.808  1.00 92.92  ? 81  ILE A CG1   1 
ATOM   1481 C CG2   . ILE B 2 81  ? 113.957 100.809 92.751  1.00 92.92  ? 81  ILE A CG2   1 
ATOM   1482 C CD1   . ILE B 2 81  ? 113.228 99.966  95.518  1.00 92.92  ? 81  ILE A CD1   1 
ATOM   1483 N N     . TYR B 2 82  ? 117.425 101.927 92.212  1.00 94.12  ? 82  TYR A N     1 
ATOM   1484 C CA    . TYR B 2 82  ? 117.873 102.818 91.150  1.00 94.12  ? 82  TYR A CA    1 
ATOM   1485 C C     . TYR B 2 82  ? 118.923 102.151 90.274  1.00 94.12  ? 82  TYR A C     1 
ATOM   1486 O O     . TYR B 2 82  ? 118.906 102.305 89.048  1.00 94.12  ? 82  TYR A O     1 
ATOM   1487 C CB    . TYR B 2 82  ? 118.423 104.102 91.764  1.00 94.12  ? 82  TYR A CB    1 
ATOM   1488 C CG    . TYR B 2 82  ? 119.000 105.078 90.774  1.00 94.12  ? 82  TYR A CG    1 
ATOM   1489 C CD1   . TYR B 2 82  ? 118.182 105.950 90.079  1.00 94.12  ? 82  TYR A CD1   1 
ATOM   1490 C CD2   . TYR B 2 82  ? 120.366 105.138 90.547  1.00 94.12  ? 82  TYR A CD2   1 
ATOM   1491 C CE1   . TYR B 2 82  ? 118.703 106.847 89.181  1.00 94.12  ? 82  TYR A CE1   1 
ATOM   1492 C CE2   . TYR B 2 82  ? 120.897 106.033 89.648  1.00 94.12  ? 82  TYR A CE2   1 
ATOM   1493 C CZ    . TYR B 2 82  ? 120.060 106.886 88.967  1.00 94.12  ? 82  TYR A CZ    1 
ATOM   1494 O OH    . TYR B 2 82  ? 120.584 107.783 88.068  1.00 94.12  ? 82  TYR A OH    1 
ATOM   1495 N N     . ALA B 2 83  ? 119.850 101.411 90.885  1.00 97.18  ? 83  ALA A N     1 
ATOM   1496 C CA    . ALA B 2 83  ? 120.883 100.737 90.110  1.00 97.18  ? 83  ALA A CA    1 
ATOM   1497 C C     . ALA B 2 83  ? 120.283 99.667  89.212  1.00 97.18  ? 83  ALA A C     1 
ATOM   1498 O O     . ALA B 2 83  ? 120.735 99.477  88.077  1.00 97.18  ? 83  ALA A O     1 
ATOM   1499 C CB    . ALA B 2 83  ? 121.933 100.134 91.042  1.00 97.18  ? 83  ALA A CB    1 
ATOM   1500 N N     . LYS B 2 84  ? 119.265 98.957  89.693  1.00 100.08 ? 84  LYS A N     1 
ATOM   1501 C CA    . LYS B 2 84  ? 118.651 97.957  88.831  1.00 100.08 ? 84  LYS A CA    1 
ATOM   1502 C C     . LYS B 2 84  ? 117.638 98.558  87.866  1.00 100.08 ? 84  LYS A C     1 
ATOM   1503 O O     . LYS B 2 84  ? 117.274 97.897  86.888  1.00 100.08 ? 84  LYS A O     1 
ATOM   1504 C CB    . LYS B 2 84  ? 117.979 96.858  89.657  1.00 100.08 ? 84  LYS A CB    1 
ATOM   1505 C CG    . LYS B 2 84  ? 116.671 97.252  90.298  1.00 100.08 ? 84  LYS A CG    1 
ATOM   1506 C CD    . LYS B 2 84  ? 116.106 96.090  91.096  1.00 100.08 ? 84  LYS A CD    1 
ATOM   1507 C CE    . LYS B 2 84  ? 115.759 94.918  90.184  1.00 100.08 ? 84  LYS A CE    1 
ATOM   1508 N NZ    . LYS B 2 84  ? 114.669 95.236  89.221  1.00 100.08 ? 84  LYS A NZ    1 
ATOM   1509 N N     . LEU B 2 85  ? 117.168 99.780  88.120  1.00 99.05  ? 85  LEU A N     1 
ATOM   1510 C CA    . LEU B 2 85  ? 116.239 100.457 87.224  1.00 99.05  ? 85  LEU A CA    1 
ATOM   1511 C C     . LEU B 2 85  ? 116.940 101.176 86.084  1.00 99.05  ? 85  LEU A C     1 
ATOM   1512 O O     . LEU B 2 85  ? 116.376 101.284 84.990  1.00 99.05  ? 85  LEU A O     1 
ATOM   1513 C CB    . LEU B 2 85  ? 115.397 101.469 88.007  1.00 99.05  ? 85  LEU A CB    1 
ATOM   1514 C CG    . LEU B 2 85  ? 113.989 101.061 88.436  1.00 99.05  ? 85  LEU A CG    1 
ATOM   1515 C CD1   . LEU B 2 85  ? 113.280 102.235 89.084  1.00 99.05  ? 85  LEU A CD1   1 
ATOM   1516 C CD2   . LEU B 2 85  ? 113.198 100.549 87.251  1.00 99.05  ? 85  LEU A CD2   1 
ATOM   1517 N N     . SER B 2 86  ? 118.151 101.681 86.319  1.00 99.70  ? 86  SER A N     1 
ATOM   1518 C CA    . SER B 2 86  ? 118.878 102.383 85.270  1.00 99.70  ? 86  SER A CA    1 
ATOM   1519 C C     . SER B 2 86  ? 119.208 101.478 84.092  1.00 99.70  ? 86  SER A C     1 
ATOM   1520 O O     . SER B 2 86  ? 119.424 101.977 82.983  1.00 99.70  ? 86  SER A O     1 
ATOM   1521 C CB    . SER B 2 86  ? 120.162 102.988 85.835  1.00 99.70  ? 86  SER A CB    1 
ATOM   1522 O OG    . SER B 2 86  ? 120.836 102.062 86.666  1.00 99.70  ? 86  SER A OG    1 
ATOM   1523 N N     . ASN B 2 87  ? 119.243 100.166 84.302  1.00 102.28 ? 87  ASN A N     1 
ATOM   1524 C CA    . ASN B 2 87  ? 119.551 99.227  83.236  1.00 102.28 ? 87  ASN A CA    1 
ATOM   1525 C C     . ASN B 2 87  ? 118.328 98.815  82.430  1.00 102.28 ? 87  ASN A C     1 
ATOM   1526 O O     . ASN B 2 87  ? 118.487 98.252  81.342  1.00 102.28 ? 87  ASN A O     1 
ATOM   1527 C CB    . ASN B 2 87  ? 120.222 97.980  83.814  1.00 102.28 ? 87  ASN A CB    1 
ATOM   1528 C CG    . ASN B 2 87  ? 121.326 98.317  84.790  1.00 102.28 ? 87  ASN A CG    1 
ATOM   1529 O OD1   . ASN B 2 87  ? 121.895 99.407  84.747  1.00 102.28 ? 87  ASN A OD1   1 
ATOM   1530 N ND2   . ASN B 2 87  ? 121.637 97.382  85.678  1.00 102.28 ? 87  ASN A ND2   1 
ATOM   1531 N N     . ILE B 2 88  ? 117.124 99.080  82.927  1.00 101.30 ? 88  ILE A N     1 
ATOM   1532 C CA    . ILE B 2 88  ? 115.907 98.745  82.203  1.00 101.30 ? 88  ILE A CA    1 
ATOM   1533 C C     . ILE B 2 88  ? 115.226 99.970  81.603  1.00 101.30 ? 88  ILE A C     1 
ATOM   1534 O O     . ILE B 2 88  ? 114.512 99.830  80.597  1.00 101.30 ? 88  ILE A O     1 
ATOM   1535 C CB    . ILE B 2 88  ? 114.922 97.967  83.101  1.00 101.30 ? 88  ILE A CB    1 
ATOM   1536 C CG1   . ILE B 2 88  ? 113.779 97.374  82.274  1.00 101.30 ? 88  ILE A CG1   1 
ATOM   1537 C CG2   . ILE B 2 88  ? 114.379 98.855  84.202  1.00 101.30 ? 88  ILE A CG2   1 
ATOM   1538 C CD1   . ILE B 2 88  ? 114.243 96.538  81.102  1.00 101.30 ? 88  ILE A CD1   1 
ATOM   1539 N N     . LEU B 2 89  ? 115.434 101.157 82.161  1.00 100.10 ? 89  LEU A N     1 
ATOM   1540 C CA    . LEU B 2 89  ? 114.867 102.391 81.644  1.00 100.10 ? 89  LEU A CA    1 
ATOM   1541 C C     . LEU B 2 89  ? 115.956 103.243 81.009  1.00 100.10 ? 89  LEU A C     1 
ATOM   1542 O O     . LEU B 2 89  ? 117.141 103.118 81.329  1.00 100.10 ? 89  LEU A O     1 
ATOM   1543 C CB    . LEU B 2 89  ? 114.172 103.180 82.758  1.00 100.10 ? 89  LEU A CB    1 
ATOM   1544 C CG    . LEU B 2 89  ? 112.944 102.528 83.391  1.00 100.10 ? 89  LEU A CG    1 
ATOM   1545 C CD1   . LEU B 2 89  ? 112.494 103.315 84.606  1.00 100.10 ? 89  LEU A CD1   1 
ATOM   1546 C CD2   . LEU B 2 89  ? 111.821 102.421 82.378  1.00 100.10 ? 89  LEU A CD2   1 
ATOM   1547 N N     . SER B 2 90  ? 115.542 104.117 80.095  1.00 99.39  ? 90  SER A N     1 
ATOM   1548 C CA    . SER B 2 90  ? 116.466 105.071 79.505  1.00 99.39  ? 90  SER A CA    1 
ATOM   1549 C C     . SER B 2 90  ? 116.800 106.158 80.524  1.00 99.39  ? 90  SER A C     1 
ATOM   1550 O O     . SER B 2 90  ? 116.266 106.192 81.633  1.00 99.39  ? 90  SER A O     1 
ATOM   1551 C CB    . SER B 2 90  ? 115.875 105.668 78.231  1.00 99.39  ? 90  SER A CB    1 
ATOM   1552 O OG    . SER B 2 90  ? 114.641 106.309 78.490  1.00 99.39  ? 90  SER A OG    1 
ATOM   1553 N N     . LYS B 2 91  ? 117.697 107.066 80.139  1.00 99.83  ? 91  LYS A N     1 
ATOM   1554 C CA    . LYS B 2 91  ? 118.142 108.100 81.069  1.00 99.83  ? 91  LYS A CA    1 
ATOM   1555 C C     . LYS B 2 91  ? 116.995 109.024 81.460  1.00 99.83  ? 91  LYS A C     1 
ATOM   1556 O O     . LYS B 2 91  ? 116.733 109.241 82.650  1.00 99.83  ? 91  LYS A O     1 
ATOM   1557 C CB    . LYS B 2 91  ? 119.295 108.895 80.458  1.00 99.83  ? 91  LYS A CB    1 
ATOM   1558 C CG    . LYS B 2 91  ? 120.661 108.507 80.996  1.00 99.83  ? 91  LYS A CG    1 
ATOM   1559 C CD    . LYS B 2 91  ? 121.756 109.387 80.420  1.00 99.83  ? 91  LYS A CD    1 
ATOM   1560 C CE    . LYS B 2 91  ? 121.960 109.110 78.941  1.00 99.83  ? 91  LYS A CE    1 
ATOM   1561 N NZ    . LYS B 2 91  ? 123.016 109.977 78.353  1.00 99.83  ? 91  LYS A NZ    1 
ATOM   1562 N N     . GLN B 2 92  ? 116.293 109.578 80.470  1.00 98.28  ? 92  GLN A N     1 
ATOM   1563 C CA    . GLN B 2 92  ? 115.191 110.483 80.774  1.00 98.28  ? 92  GLN A CA    1 
ATOM   1564 C C     . GLN B 2 92  ? 114.031 109.742 81.425  1.00 98.28  ? 92  GLN A C     1 
ATOM   1565 O O     . GLN B 2 92  ? 113.391 110.264 82.347  1.00 98.28  ? 92  GLN A O     1 
ATOM   1566 C CB    . GLN B 2 92  ? 114.736 111.198 79.505  1.00 98.28  ? 92  GLN A CB    1 
ATOM   1567 C CG    . GLN B 2 92  ? 114.592 110.292 78.301  1.00 98.28  ? 92  GLN A CG    1 
ATOM   1568 C CD    . GLN B 2 92  ? 114.173 111.045 77.059  1.00 98.28  ? 92  GLN A CD    1 
ATOM   1569 O OE1   . GLN B 2 92  ? 114.089 112.273 77.063  1.00 98.28  ? 92  GLN A OE1   1 
ATOM   1570 N NE2   . GLN B 2 92  ? 113.907 110.313 75.984  1.00 98.28  ? 92  GLN A NE2   1 
ATOM   1571 N N     . ALA B 2 93  ? 113.743 108.526 80.960  1.00 96.28  ? 93  ALA A N     1 
ATOM   1572 C CA    . ALA B 2 93  ? 112.705 107.731 81.604  1.00 96.28  ? 93  ALA A CA    1 
ATOM   1573 C C     . ALA B 2 93  ? 113.084 107.410 83.040  1.00 96.28  ? 93  ALA A C     1 
ATOM   1574 O O     . ALA B 2 93  ? 112.221 107.366 83.921  1.00 96.28  ? 93  ALA A O     1 
ATOM   1575 C CB    . ALA B 2 93  ? 112.451 106.449 80.814  1.00 96.28  ? 93  ALA A CB    1 
ATOM   1576 N N     . LEU B 2 94  ? 114.375 107.203 83.300  1.00 94.56  ? 94  LEU A N     1 
ATOM   1577 C CA    . LEU B 2 94  ? 114.823 106.980 84.669  1.00 94.56  ? 94  LEU A CA    1 
ATOM   1578 C C     . LEU B 2 94  ? 114.620 108.224 85.518  1.00 94.56  ? 94  LEU A C     1 
ATOM   1579 O O     . LEU B 2 94  ? 114.149 108.138 86.659  1.00 94.56  ? 94  LEU A O     1 
ATOM   1580 C CB    . LEU B 2 94  ? 116.291 106.564 84.677  1.00 94.56  ? 94  LEU A CB    1 
ATOM   1581 C CG    . LEU B 2 94  ? 116.984 106.449 86.029  1.00 94.56  ? 94  LEU A CG    1 
ATOM   1582 C CD1   . LEU B 2 94  ? 116.334 105.370 86.868  1.00 94.56  ? 94  LEU A CD1   1 
ATOM   1583 C CD2   . LEU B 2 94  ? 118.456 106.162 85.820  1.00 94.56  ? 94  LEU A CD2   1 
ATOM   1584 N N     . PHE B 2 95  ? 114.972 109.392 84.977  1.00 91.18  ? 95  PHE A N     1 
ATOM   1585 C CA    . PHE B 2 95  ? 114.753 110.643 85.695  1.00 91.18  ? 95  PHE A CA    1 
ATOM   1586 C C     . PHE B 2 95  ? 113.286 110.811 86.060  1.00 91.18  ? 95  PHE A C     1 
ATOM   1587 O O     . PHE B 2 95  ? 112.952 111.164 87.195  1.00 91.18  ? 95  PHE A O     1 
ATOM   1588 C CB    . PHE B 2 95  ? 115.236 111.821 84.852  1.00 91.18  ? 95  PHE A CB    1 
ATOM   1589 C CG    . PHE B 2 95  ? 115.310 113.120 85.603  1.00 91.18  ? 95  PHE A CG    1 
ATOM   1590 C CD1   . PHE B 2 95  ? 114.192 113.921 85.741  1.00 91.18  ? 95  PHE A CD1   1 
ATOM   1591 C CD2   . PHE B 2 95  ? 116.502 113.544 86.161  1.00 91.18  ? 95  PHE A CD2   1 
ATOM   1592 C CE1   . PHE B 2 95  ? 114.260 115.113 86.427  1.00 91.18  ? 95  PHE A CE1   1 
ATOM   1593 C CE2   . PHE B 2 95  ? 116.574 114.735 86.847  1.00 91.18  ? 95  PHE A CE2   1 
ATOM   1594 C CZ    . PHE B 2 95  ? 115.453 115.520 86.981  1.00 91.18  ? 95  PHE A CZ    1 
ATOM   1595 N N     . TYR B 2 96  ? 112.392 110.558 85.105  1.00 92.20  ? 96  TYR A N     1 
ATOM   1596 C CA    . TYR B 2 96  ? 110.965 110.698 85.382  1.00 92.20  ? 96  TYR A CA    1 
ATOM   1597 C C     . TYR B 2 96  ? 110.499 109.679 86.413  1.00 92.20  ? 96  TYR A C     1 
ATOM   1598 O O     . TYR B 2 96  ? 109.798 110.026 87.369  1.00 92.20  ? 96  TYR A O     1 
ATOM   1599 C CB    . TYR B 2 96  ? 110.160 110.564 84.092  1.00 92.20  ? 96  TYR A CB    1 
ATOM   1600 C CG    . TYR B 2 96  ? 110.378 111.697 83.124  1.00 92.20  ? 96  TYR A CG    1 
ATOM   1601 C CD1   . TYR B 2 96  ? 110.381 113.012 83.557  1.00 92.20  ? 96  TYR A CD1   1 
ATOM   1602 C CD2   . TYR B 2 96  ? 110.581 111.451 81.777  1.00 92.20  ? 96  TYR A CD2   1 
ATOM   1603 C CE1   . TYR B 2 96  ? 110.582 114.048 82.678  1.00 92.20  ? 96  TYR A CE1   1 
ATOM   1604 C CE2   . TYR B 2 96  ? 110.784 112.481 80.890  1.00 92.20  ? 96  TYR A CE2   1 
ATOM   1605 C CZ    . TYR B 2 96  ? 110.783 113.776 81.345  1.00 92.20  ? 96  TYR A CZ    1 
ATOM   1606 O OH    . TYR B 2 96  ? 110.985 114.804 80.458  1.00 92.20  ? 96  TYR A OH    1 
ATOM   1607 N N     . ALA B 2 97  ? 110.875 108.411 86.238  1.00 90.23  ? 97  ALA A N     1 
ATOM   1608 C CA    . ALA B 2 97  ? 110.419 107.366 87.142  1.00 90.23  ? 97  ALA A CA    1 
ATOM   1609 C C     . ALA B 2 97  ? 110.985 107.521 88.545  1.00 90.23  ? 97  ALA A C     1 
ATOM   1610 O O     . ALA B 2 97  ? 110.440 106.935 89.484  1.00 90.23  ? 97  ALA A O     1 
ATOM   1611 C CB    . ALA B 2 97  ? 110.787 105.993 86.583  1.00 90.23  ? 97  ALA A CB    1 
ATOM   1612 N N     . VAL B 2 98  ? 112.066 108.275 88.709  1.00 88.43  ? 98  VAL A N     1 
ATOM   1613 C CA    . VAL B 2 98  ? 112.588 108.541 90.044  1.00 88.43  ? 98  VAL A CA    1 
ATOM   1614 C C     . VAL B 2 98  ? 111.995 109.815 90.632  1.00 88.43  ? 98  VAL A C     1 
ATOM   1615 O O     . VAL B 2 98  ? 111.742 109.889 91.836  1.00 88.43  ? 98  VAL A O     1 
ATOM   1616 C CB    . VAL B 2 98  ? 114.127 108.597 90.002  1.00 88.43  ? 98  VAL A CB    1 
ATOM   1617 C CG1   . VAL B 2 98  ? 114.681 109.066 91.328  1.00 88.43  ? 98  VAL A CG1   1 
ATOM   1618 C CG2   . VAL B 2 98  ? 114.685 107.229 89.664  1.00 88.43  ? 98  VAL A CG2   1 
ATOM   1619 N N     . GLY B 2 99  ? 111.734 110.827 89.802  1.00 86.59  ? 99  GLY A N     1 
ATOM   1620 C CA    . GLY B 2 99  ? 111.256 112.093 90.324  1.00 86.59  ? 99  GLY A CA    1 
ATOM   1621 C C     . GLY B 2 99  ? 109.764 112.162 90.560  1.00 86.59  ? 99  GLY A C     1 
ATOM   1622 O O     . GLY B 2 99  ? 109.318 112.852 91.479  1.00 86.59  ? 99  GLY A O     1 
ATOM   1623 N N     . THR B 2 100 ? 108.973 111.466 89.750  1.00 84.92  ? 100 THR A N     1 
ATOM   1624 C CA    . THR B 2 100 ? 107.523 111.564 89.868  1.00 84.92  ? 100 THR A CA    1 
ATOM   1625 C C     . THR B 2 100 ? 106.952 110.885 91.113  1.00 84.92  ? 100 THR A C     1 
ATOM   1626 O O     . THR B 2 100 ? 105.925 111.349 91.618  1.00 84.92  ? 100 THR A O     1 
ATOM   1627 C CB    . THR B 2 100 ? 106.839 111.017 88.612  1.00 84.92  ? 100 THR A CB    1 
ATOM   1628 O OG1   . THR B 2 100 ? 107.190 109.644 88.413  1.00 84.92  ? 100 THR A OG1   1 
ATOM   1629 C CG2   . THR B 2 100 ? 107.235 111.833 87.393  1.00 84.92  ? 100 THR A CG2   1 
ATOM   1630 N N     . PRO B 2 101 ? 107.529 109.791 91.632  1.00 83.12  ? 101 PRO A N     1 
ATOM   1631 C CA    . PRO B 2 101 ? 107.029 109.291 92.924  1.00 83.12  ? 101 PRO A CA    1 
ATOM   1632 C C     . PRO B 2 101 ? 107.149 110.311 94.038  1.00 83.12  ? 101 PRO A C     1 
ATOM   1633 O O     . PRO B 2 101 ? 106.281 110.372 94.918  1.00 83.12  ? 101 PRO A O     1 
ATOM   1634 C CB    . PRO B 2 101 ? 107.903 108.059 93.181  1.00 83.12  ? 101 PRO A CB    1 
ATOM   1635 C CG    . PRO B 2 101 ? 108.261 107.590 91.841  1.00 83.12  ? 101 PRO A CG    1 
ATOM   1636 C CD    . PRO B 2 101 ? 108.481 108.836 91.039  1.00 83.12  ? 101 PRO A CD    1 
ATOM   1637 N N     . PHE B 2 102 ? 108.207 111.123 94.021  1.00 80.02  ? 102 PHE A N     1 
ATOM   1638 C CA    . PHE B 2 102 ? 108.338 112.191 95.004  1.00 80.02  ? 102 PHE A CA    1 
ATOM   1639 C C     . PHE B 2 102 ? 107.164 113.155 94.921  1.00 80.02  ? 102 PHE A C     1 
ATOM   1640 O O     . PHE B 2 102 ? 106.551 113.496 95.938  1.00 80.02  ? 102 PHE A O     1 
ATOM   1641 C CB    . PHE B 2 102 ? 109.655 112.935 94.795  1.00 80.02  ? 102 PHE A CB    1 
ATOM   1642 C CG    . PHE B 2 102 ? 110.843 112.241 95.384  1.00 80.02  ? 102 PHE A CG    1 
ATOM   1643 C CD1   . PHE B 2 102 ? 111.013 112.175 96.752  1.00 80.02  ? 102 PHE A CD1   1 
ATOM   1644 C CD2   . PHE B 2 102 ? 111.794 111.663 94.567  1.00 80.02  ? 102 PHE A CD2   1 
ATOM   1645 C CE1   . PHE B 2 102 ? 112.106 111.539 97.293  1.00 80.02  ? 102 PHE A CE1   1 
ATOM   1646 C CE2   . PHE B 2 102 ? 112.889 111.028 95.104  1.00 80.02  ? 102 PHE A CE2   1 
ATOM   1647 C CZ    . PHE B 2 102 ? 113.045 110.966 96.468  1.00 80.02  ? 102 PHE A CZ    1 
ATOM   1648 N N     . LEU B 2 103 ? 106.835 113.605 93.709  1.00 79.93  ? 103 LEU A N     1 
ATOM   1649 C CA    . LEU B 2 103 ? 105.729 114.541 93.546  1.00 79.93  ? 103 LEU A CA    1 
ATOM   1650 C C     . LEU B 2 103 ? 104.401 113.890 93.900  1.00 79.93  ? 103 LEU A C     1 
ATOM   1651 O O     . LEU B 2 103 ? 103.513 114.545 94.454  1.00 79.93  ? 103 LEU A O     1 
ATOM   1652 C CB    . LEU B 2 103 ? 105.698 115.075 92.117  1.00 79.93  ? 103 LEU A CB    1 
ATOM   1653 C CG    . LEU B 2 103 ? 106.979 115.739 91.616  1.00 79.93  ? 103 LEU A CG    1 
ATOM   1654 C CD1   . LEU B 2 103 ? 106.728 116.426 90.290  1.00 79.93  ? 103 LEU A CD1   1 
ATOM   1655 C CD2   . LEU B 2 103 ? 107.508 116.723 92.640  1.00 79.93  ? 103 LEU A CD2   1 
ATOM   1656 N N     . ILE B 2 104 ? 104.250 112.600 93.607  1.00 79.88  ? 104 ILE A N     1 
ATOM   1657 C CA    . ILE B 2 104 ? 103.018 111.904 93.966  1.00 79.88  ? 104 ILE A CA    1 
ATOM   1658 C C     . ILE B 2 104 ? 102.862 111.864 95.479  1.00 79.88  ? 104 ILE A C     1 
ATOM   1659 O O     . ILE B 2 104 ? 101.777 112.115 96.016  1.00 79.88  ? 104 ILE A O     1 
ATOM   1660 C CB    . ILE B 2 104 ? 102.996 110.493 93.355  1.00 79.88  ? 104 ILE A CB    1 
ATOM   1661 C CG1   . ILE B 2 104 ? 102.858 110.574 91.835  1.00 79.88  ? 104 ILE A CG1   1 
ATOM   1662 C CG2   . ILE B 2 104 ? 101.857 109.682 93.934  1.00 79.88  ? 104 ILE A CG2   1 
ATOM   1663 C CD1   . ILE B 2 104 ? 102.729 109.230 91.163  1.00 79.88  ? 104 ILE A CD1   1 
ATOM   1664 N N     . PHE B 2 105 ? 103.951 111.576 96.194  1.00 78.40  ? 105 PHE A N     1 
ATOM   1665 C CA    . PHE B 2 105 ? 103.867 111.545 97.650  1.00 78.40  ? 105 PHE A CA    1 
ATOM   1666 C C     . PHE B 2 105 ? 103.608 112.930 98.219  1.00 78.40  ? 105 PHE A C     1 
ATOM   1667 O O     . PHE B 2 105 ? 102.837 113.080 99.170  1.00 78.40  ? 105 PHE A O     1 
ATOM   1668 C CB    . PHE B 2 105 ? 105.139 110.968 98.263  1.00 78.40  ? 105 PHE A CB    1 
ATOM   1669 C CG    . PHE B 2 105 ? 105.135 110.992 99.764  1.00 78.40  ? 105 PHE A CG    1 
ATOM   1670 C CD1   . PHE B 2 105 ? 104.426 110.046 100.481 1.00 78.40  ? 105 PHE A CD1   1 
ATOM   1671 C CD2   . PHE B 2 105 ? 105.815 111.976 100.459 1.00 78.40  ? 105 PHE A CD2   1 
ATOM   1672 C CE1   . PHE B 2 105 ? 104.409 110.069 101.858 1.00 78.40  ? 105 PHE A CE1   1 
ATOM   1673 C CE2   . PHE B 2 105 ? 105.800 112.003 101.836 1.00 78.40  ? 105 PHE A CE2   1 
ATOM   1674 C CZ    . PHE B 2 105 ? 105.096 111.049 102.535 1.00 78.40  ? 105 PHE A CZ    1 
ATOM   1675 N N     . PHE B 2 106 ? 104.254 113.955 97.666  1.00 79.43  ? 106 PHE A N     1 
ATOM   1676 C CA    . PHE B 2 106 ? 104.074 115.298 98.200  1.00 79.43  ? 106 PHE A CA    1 
ATOM   1677 C C     . PHE B 2 106 ? 102.726 115.896 97.828  1.00 79.43  ? 106 PHE A C     1 
ATOM   1678 O O     . PHE B 2 106 ? 102.294 116.858 98.467  1.00 79.43  ? 106 PHE A O     1 
ATOM   1679 C CB    . PHE B 2 106 ? 105.203 116.211 97.728  1.00 79.43  ? 106 PHE A CB    1 
ATOM   1680 C CG    . PHE B 2 106 ? 106.560 115.758 98.167  1.00 79.43  ? 106 PHE A CG    1 
ATOM   1681 C CD1   . PHE B 2 106 ? 106.733 115.154 99.400  1.00 79.43  ? 106 PHE A CD1   1 
ATOM   1682 C CD2   . PHE B 2 106 ? 107.662 115.930 97.352  1.00 79.43  ? 106 PHE A CD2   1 
ATOM   1683 C CE1   . PHE B 2 106 ? 107.977 114.728 99.810  1.00 79.43  ? 106 PHE A CE1   1 
ATOM   1684 C CE2   . PHE B 2 106 ? 108.908 115.504 97.756  1.00 79.43  ? 106 PHE A CE2   1 
ATOM   1685 C CZ    . PHE B 2 106 ? 109.065 114.902 98.988  1.00 79.43  ? 106 PHE A CZ    1 
ATOM   1686 N N     . ALA B 2 107 ? 102.057 115.352 96.813  1.00 77.87  ? 107 ALA A N     1 
ATOM   1687 C CA    . ALA B 2 107 ? 100.681 115.742 96.546  1.00 77.87  ? 107 ALA A CA    1 
ATOM   1688 C C     . ALA B 2 107 ? 99.700  114.956 97.400  1.00 77.87  ? 107 ALA A C     1 
ATOM   1689 O O     . ALA B 2 107 ? 98.650  115.485 97.776  1.00 77.87  ? 107 ALA A O     1 
ATOM   1690 C CB    . ALA B 2 107 ? 100.353 115.549 95.066  1.00 77.87  ? 107 ALA A CB    1 
ATOM   1691 N N     . LEU B 2 108 ? 100.022 113.702 97.717  1.00 78.67  ? 108 LEU A N     1 
ATOM   1692 C CA    . LEU B 2 108 ? 99.133  112.879 98.523  1.00 78.67  ? 108 LEU A CA    1 
ATOM   1693 C C     . LEU B 2 108 ? 99.252  113.157 100.012 1.00 78.67  ? 108 LEU A C     1 
ATOM   1694 O O     . LEU B 2 108 ? 98.324  112.834 100.760 1.00 78.67  ? 108 LEU A O     1 
ATOM   1695 C CB    . LEU B 2 108 ? 99.410  111.398 98.267  1.00 78.67  ? 108 LEU A CB    1 
ATOM   1696 C CG    . LEU B 2 108 ? 98.675  110.755 97.095  1.00 78.67  ? 108 LEU A CG    1 
ATOM   1697 C CD1   . LEU B 2 108 ? 99.375  109.480 96.674  1.00 78.67  ? 108 LEU A CD1   1 
ATOM   1698 C CD2   . LEU B 2 108 ? 97.238  110.470 97.475  1.00 78.67  ? 108 LEU A CD2   1 
ATOM   1699 N N     . PHE B 2 109 ? 100.359 113.735 100.462 1.00 77.46  ? 109 PHE A N     1 
ATOM   1700 C CA    . PHE B 2 109 ? 100.561 113.905 101.893 1.00 77.46  ? 109 PHE A CA    1 
ATOM   1701 C C     . PHE B 2 109 ? 99.543  114.881 102.477 1.00 77.46  ? 109 PHE A C     1 
ATOM   1702 O O     . PHE B 2 109 ? 98.676  114.447 103.243 1.00 77.46  ? 109 PHE A O     1 
ATOM   1703 C CB    . PHE B 2 109 ? 101.996 114.348 102.190 1.00 77.46  ? 109 PHE A CB    1 
ATOM   1704 C CG    . PHE B 2 109 ? 102.357 114.289 103.641 1.00 77.46  ? 109 PHE A CG    1 
ATOM   1705 C CD1   . PHE B 2 109 ? 102.459 113.077 104.294 1.00 77.46  ? 109 PHE A CD1   1 
ATOM   1706 C CD2   . PHE B 2 109 ? 102.590 115.448 104.355 1.00 77.46  ? 109 PHE A CD2   1 
ATOM   1707 C CE1   . PHE B 2 109 ? 102.789 113.022 105.628 1.00 77.46  ? 109 PHE A CE1   1 
ATOM   1708 C CE2   . PHE B 2 109 ? 102.918 115.397 105.689 1.00 77.46  ? 109 PHE A CE2   1 
ATOM   1709 C CZ    . PHE B 2 109 ? 103.019 114.183 106.326 1.00 77.46  ? 109 PHE A CZ    1 
ATOM   1710 N N     . PRO B 2 110 ? 99.560  116.173 102.119 1.00 78.84  ? 110 PRO A N     1 
ATOM   1711 C CA    . PRO B 2 110 ? 98.665  117.113 102.804 1.00 78.84  ? 110 PRO A CA    1 
ATOM   1712 C C     . PRO B 2 110 ? 97.205  116.911 102.466 1.00 78.84  ? 110 PRO A C     1 
ATOM   1713 O O     . PRO B 2 110 ? 96.344  117.449 103.171 1.00 78.84  ? 110 PRO A O     1 
ATOM   1714 C CB    . PRO B 2 110 ? 99.159  118.473 102.313 1.00 78.84  ? 110 PRO A CB    1 
ATOM   1715 C CG    . PRO B 2 110 ? 99.575  118.192 100.933 1.00 78.84  ? 110 PRO A CG    1 
ATOM   1716 C CD    . PRO B 2 110 ? 100.207 116.824 100.964 1.00 78.84  ? 110 PRO A CD    1 
ATOM   1717 N N     . THR B 2 111 ? 96.897  116.160 101.413 1.00 80.50  ? 111 THR A N     1 
ATOM   1718 C CA    . THR B 2 111 ? 95.523  115.967 100.978 1.00 80.50  ? 111 THR A CA    1 
ATOM   1719 C C     . THR B 2 111 ? 94.917  114.659 101.457 1.00 80.50  ? 111 THR A C     1 
ATOM   1720 O O     . THR B 2 111 ? 93.704  114.599 101.677 1.00 80.50  ? 111 THR A O     1 
ATOM   1721 C CB    . THR B 2 111 ? 95.445  116.020 99.450  1.00 80.50  ? 111 THR A CB    1 
ATOM   1722 O OG1   . THR B 2 111 ? 96.508  115.241 98.892  1.00 80.50  ? 111 THR A OG1   1 
ATOM   1723 C CG2   . THR B 2 111 ? 95.575  117.449 98.965  1.00 80.50  ? 111 THR A CG2   1 
ATOM   1724 N N     . VAL B 2 112 ? 95.725  113.613 101.625 1.00 79.71  ? 112 VAL A N     1 
ATOM   1725 C CA    . VAL B 2 112 ? 95.242  112.287 101.988 1.00 79.71  ? 112 VAL A CA    1 
ATOM   1726 C C     . VAL B 2 112 ? 95.904  111.778 103.263 1.00 79.71  ? 112 VAL A C     1 
ATOM   1727 O O     . VAL B 2 112 ? 95.231  111.268 104.163 1.00 79.71  ? 112 VAL A O     1 
ATOM   1728 C CB    . VAL B 2 112 ? 95.442  111.282 100.832 1.00 79.71  ? 112 VAL A CB    1 
ATOM   1729 C CG1   . VAL B 2 112 ? 95.226  109.863 101.318 1.00 79.71  ? 112 VAL A CG1   1 
ATOM   1730 C CG2   . VAL B 2 112 ? 94.501  111.603 99.688  1.00 79.71  ? 112 VAL A CG2   1 
ATOM   1731 N N     . ILE B 2 113 ? 97.225  111.915 103.362 1.00 78.07  ? 113 ILE A N     1 
ATOM   1732 C CA    . ILE B 2 113 ? 97.944  111.233 104.432 1.00 78.07  ? 113 ILE A CA    1 
ATOM   1733 C C     . ILE B 2 113 ? 97.892  112.033 105.726 1.00 78.07  ? 113 ILE A C     1 
ATOM   1734 O O     . ILE B 2 113 ? 97.714  111.466 106.808 1.00 78.07  ? 113 ILE A O     1 
ATOM   1735 C CB    . ILE B 2 113 ? 99.390  110.947 103.995 1.00 78.07  ? 113 ILE A CB    1 
ATOM   1736 C CG1   . ILE B 2 113 ? 99.410  109.894 102.889 1.00 78.07  ? 113 ILE A CG1   1 
ATOM   1737 C CG2   . ILE B 2 113 ? 100.215 110.475 105.168 1.00 78.07  ? 113 ILE A CG2   1 
ATOM   1738 C CD1   . ILE B 2 113 ? 100.797 109.526 102.429 1.00 78.07  ? 113 ILE A CD1   1 
ATOM   1739 N N     . TYR B 2 114 ? 98.034  113.351 105.647 1.00 78.45  ? 114 TYR A N     1 
ATOM   1740 C CA    . TYR B 2 114 ? 98.014  114.162 106.858 1.00 78.45  ? 114 TYR A CA    1 
ATOM   1741 C C     . TYR B 2 114 ? 96.616  114.260 107.465 1.00 78.45  ? 114 TYR A C     1 
ATOM   1742 O O     . TYR B 2 114 ? 96.491  114.216 108.694 1.00 78.45  ? 114 TYR A O     1 
ATOM   1743 C CB    . TYR B 2 114 ? 98.569  115.561 106.592 1.00 78.45  ? 114 TYR A CB    1 
ATOM   1744 C CG    . TYR B 2 114 ? 98.690  116.395 107.844 1.00 78.45  ? 114 TYR A CG    1 
ATOM   1745 C CD1   . TYR B 2 114 ? 99.812  116.309 108.649 1.00 78.45  ? 114 TYR A CD1   1 
ATOM   1746 C CD2   . TYR B 2 114 ? 97.680  117.262 108.224 1.00 78.45  ? 114 TYR A CD2   1 
ATOM   1747 C CE1   . TYR B 2 114 ? 99.926  117.064 109.793 1.00 78.45  ? 114 TYR A CE1   1 
ATOM   1748 C CE2   . TYR B 2 114 ? 97.785  118.019 109.365 1.00 78.45  ? 114 TYR A CE2   1 
ATOM   1749 C CZ    . TYR B 2 114 ? 98.909  117.916 110.146 1.00 78.45  ? 114 TYR A CZ    1 
ATOM   1750 O OH    . TYR B 2 114 ? 99.013  118.673 111.287 1.00 78.45  ? 114 TYR A OH    1 
ATOM   1751 N N     . PRO B 2 115 ? 95.548  114.421 106.676 1.00 79.63  ? 115 PRO A N     1 
ATOM   1752 C CA    . PRO B 2 115 ? 94.210  114.378 107.284 1.00 79.63  ? 115 PRO A CA    1 
ATOM   1753 C C     . PRO B 2 115 ? 93.903  113.062 107.968 1.00 79.63  ? 115 PRO A C     1 
ATOM   1754 O O     . PRO B 2 115 ? 93.139  113.042 108.940 1.00 79.63  ? 115 PRO A O     1 
ATOM   1755 C CB    . PRO B 2 115 ? 93.281  114.625 106.091 1.00 79.63  ? 115 PRO A CB    1 
ATOM   1756 C CG    . PRO B 2 115 ? 94.088  115.442 105.176 1.00 79.63  ? 115 PRO A CG    1 
ATOM   1757 C CD    . PRO B 2 115 ? 95.473  114.886 105.279 1.00 79.63  ? 115 PRO A CD    1 
ATOM   1758 N N     . LEU B 2 116 ? 94.474  111.959 107.492 1.00 80.05  ? 116 LEU A N     1 
ATOM   1759 C CA    . LEU B 2 116 ? 94.275  110.651 108.096 1.00 80.05  ? 116 LEU A CA    1 
ATOM   1760 C C     . LEU B 2 116 ? 95.330  110.325 109.143 1.00 80.05  ? 116 LEU A C     1 
ATOM   1761 O O     . LEU B 2 116 ? 95.446  109.165 109.550 1.00 80.05  ? 116 LEU A O     1 
ATOM   1762 C CB    . LEU B 2 116 ? 94.259  109.569 107.016 1.00 80.05  ? 116 LEU A CB    1 
ATOM   1763 C CG    . LEU B 2 116 ? 92.912  109.238 106.371 1.00 80.05  ? 116 LEU A CG    1 
ATOM   1764 C CD1   . LEU B 2 116 ? 92.385  110.408 105.563 1.00 80.05  ? 116 LEU A CD1   1 
ATOM   1765 C CD2   . LEU B 2 116 ? 93.033  108.003 105.499 1.00 80.05  ? 116 LEU A CD2   1 
ATOM   1766 N N     . ARG B 2 117 ? 96.101  111.320 109.588 1.00 82.01  ? 117 ARG A N     1 
ATOM   1767 C CA    . ARG B 2 117 ? 97.158  111.062 110.558 1.00 82.01  ? 117 ARG A CA    1 
ATOM   1768 C C     . ARG B 2 117 ? 96.618  110.575 111.893 1.00 82.01  ? 117 ARG A C     1 
ATOM   1769 O O     . ARG B 2 117 ? 97.364  109.953 112.654 1.00 82.01  ? 117 ARG A O     1 
ATOM   1770 C CB    . ARG B 2 117 ? 98.002  112.316 110.770 1.00 82.01  ? 117 ARG A CB    1 
ATOM   1771 C CG    . ARG B 2 117 ? 97.435  113.280 111.790 1.00 82.01  ? 117 ARG A CG    1 
ATOM   1772 C CD    . ARG B 2 117 ? 98.037  114.660 111.640 1.00 82.01  ? 117 ARG A CD    1 
ATOM   1773 N NE    . ARG B 2 117 ? 97.400  115.628 112.525 1.00 82.01  ? 117 ARG A NE    1 
ATOM   1774 C CZ    . ARG B 2 117 ? 96.233  116.212 112.277 1.00 82.01  ? 117 ARG A CZ    1 
ATOM   1775 N NH1   . ARG B 2 117 ? 95.571  115.928 111.165 1.00 82.01  ? 117 ARG A NH1   1 
ATOM   1776 N NH2   . ARG B 2 117 ? 95.728  117.082 113.139 1.00 82.01  ? 117 ARG A NH2   1 
ATOM   1777 N N     . ASP B 2 118 ? 95.355  110.840 112.202 1.00 86.70  ? 118 ASP A N     1 
ATOM   1778 C CA    . ASP B 2 118 ? 94.747  110.320 113.417 1.00 86.70  ? 118 ASP A CA    1 
ATOM   1779 C C     . ASP B 2 118 ? 94.124  108.949 113.213 1.00 86.70  ? 118 ASP A C     1 
ATOM   1780 O O     . ASP B 2 118 ? 93.477  108.434 114.129 1.00 86.70  ? 118 ASP A O     1 
ATOM   1781 C CB    . ASP B 2 118 ? 93.695  111.299 113.944 1.00 86.70  ? 118 ASP A CB    1 
ATOM   1782 C CG    . ASP B 2 118 ? 94.311  112.470 114.683 1.00 86.70  ? 118 ASP A CG    1 
ATOM   1783 O OD1   . ASP B 2 118 ? 93.648  113.522 114.792 1.00 86.70  ? 118 ASP A OD1   1 
ATOM   1784 O OD2   . ASP B 2 118 ? 95.460  112.337 115.154 1.00 86.70  ? 118 ASP A OD2   1 
ATOM   1785 N N     . VAL B 2 119 ? 94.302  108.355 112.037 1.00 82.94  ? 119 VAL A N     1 
ATOM   1786 C CA    . VAL B 2 119 ? 93.842  107.006 111.757 1.00 82.94  ? 119 VAL A CA    1 
ATOM   1787 C C     . VAL B 2 119 ? 95.006  106.072 111.461 1.00 82.94  ? 119 VAL A C     1 
ATOM   1788 O O     . VAL B 2 119 ? 95.017  104.925 111.911 1.00 82.94  ? 119 VAL A O     1 
ATOM   1789 C CB    . VAL B 2 119 ? 92.828  107.008 110.594 1.00 82.94  ? 119 VAL A CB    1 
ATOM   1790 C CG1   . VAL B 2 119 ? 92.511  105.591 110.157 1.00 82.94  ? 119 VAL A CG1   1 
ATOM   1791 C CG2   . VAL B 2 119 ? 91.563  107.743 110.998 1.00 82.94  ? 119 VAL A CG2   1 
ATOM   1792 N N     . LEU B 2 120 ? 96.003  106.553 110.718 1.00 79.10  ? 120 LEU A N     1 
ATOM   1793 C CA    . LEU B 2 120 ? 97.148  105.716 110.384 1.00 79.10  ? 120 LEU A CA    1 
ATOM   1794 C C     . LEU B 2 120 ? 98.077  105.543 111.578 1.00 79.10  ? 120 LEU A C     1 
ATOM   1795 O O     . LEU B 2 120 ? 98.619  104.454 111.796 1.00 79.10  ? 120 LEU A O     1 
ATOM   1796 C CB    . LEU B 2 120 ? 97.902  106.315 109.200 1.00 79.10  ? 120 LEU A CB    1 
ATOM   1797 C CG    . LEU B 2 120 ? 97.073  106.511 107.934 1.00 79.10  ? 120 LEU A CG    1 
ATOM   1798 C CD1   . LEU B 2 120 ? 97.904  107.162 106.848 1.00 79.10  ? 120 LEU A CD1   1 
ATOM   1799 C CD2   . LEU B 2 120 ? 96.516  105.182 107.461 1.00 79.10  ? 120 LEU A CD2   1 
ATOM   1800 N N     . HIS B 2 121 ? 98.269  106.593 112.358 1.00 78.96  ? 121 HIS A N     1 
ATOM   1801 C CA    . HIS B 2 121 ? 99.187  106.536 113.487 1.00 78.96  ? 121 HIS A CA    1 
ATOM   1802 C C     . HIS B 2 121 ? 98.604  105.694 114.611 1.00 78.96  ? 121 HIS A C     1 
ATOM   1803 O O     . HIS B 2 121 ? 97.506  105.998 115.095 1.00 78.96  ? 121 HIS A O     1 
ATOM   1804 C CB    . HIS B 2 121 ? 99.481  107.937 113.992 1.00 78.96  ? 121 HIS A CB    1 
ATOM   1805 C CG    . HIS B 2 121 ? 100.254 108.772 113.025 1.00 78.96  ? 121 HIS A CG    1 
ATOM   1806 N ND1   . HIS B 2 121 ? 100.648 110.062 113.304 1.00 78.96  ? 121 HIS A ND1   1 
ATOM   1807 C CD2   . HIS B 2 121 ? 100.708 108.500 111.781 1.00 78.96  ? 121 HIS A CD2   1 
ATOM   1808 C CE1   . HIS B 2 121 ? 101.310 110.550 112.272 1.00 78.96  ? 121 HIS A CE1   1 
ATOM   1809 N NE2   . HIS B 2 121 ? 101.361 109.622 111.335 1.00 78.96  ? 121 HIS A NE2   1 
ATOM   1810 N N     . PRO B 2 122 ? 99.289  104.650 115.061 1.00 87.34  ? 122 PRO A N     1 
ATOM   1811 C CA    . PRO B 2 122 ? 98.807  103.841 116.194 1.00 87.34  ? 122 PRO A CA    1 
ATOM   1812 C C     . PRO B 2 122 ? 99.216  104.427 117.545 1.00 87.34  ? 122 PRO A C     1 
ATOM   1813 O O     . PRO B 2 122 ? 100.159 103.988 118.198 1.00 87.34  ? 122 PRO A O     1 
ATOM   1814 C CB    . PRO B 2 122 ? 99.470  102.488 115.939 1.00 87.34  ? 122 PRO A CB    1 
ATOM   1815 C CG    . PRO B 2 122 ? 100.770 102.850 115.297 1.00 87.34  ? 122 PRO A CG    1 
ATOM   1816 C CD    . PRO B 2 122 ? 100.541 104.114 114.500 1.00 87.34  ? 122 PRO A CD    1 
ATOM   1817 N N     . THR B 2 123 ? 98.482  105.452 117.984 1.00 94.13  ? 123 THR A N     1 
ATOM   1818 C CA    . THR B 2 123 ? 98.832  106.125 119.231 1.00 94.13  ? 123 THR A CA    1 
ATOM   1819 C C     . THR B 2 123 ? 98.710  105.182 120.422 1.00 94.13  ? 123 THR A C     1 
ATOM   1820 O O     . THR B 2 123 ? 99.557  105.195 121.323 1.00 94.13  ? 123 THR A O     1 
ATOM   1821 C CB    . THR B 2 123 ? 97.950  107.358 119.435 1.00 94.13  ? 123 THR A CB    1 
ATOM   1822 O OG1   . THR B 2 123 ? 96.577  106.956 119.533 1.00 94.13  ? 123 THR A OG1   1 
ATOM   1823 C CG2   . THR B 2 123 ? 98.108  108.320 118.267 1.00 94.13  ? 123 THR A CG2   1 
ATOM   1824 N N     . GLU B 2 124 ? 97.670  104.347 120.437 1.00 98.47  ? 124 GLU A N     1 
ATOM   1825 C CA    . GLU B 2 124 ? 97.470  103.427 121.552 1.00 98.47  ? 124 GLU A CA    1 
ATOM   1826 C C     . GLU B 2 124 ? 98.605  102.416 121.642 1.00 98.47  ? 124 GLU A C     1 
ATOM   1827 O O     . GLU B 2 124 ? 99.209  102.238 122.706 1.00 98.47  ? 124 GLU A O     1 
ATOM   1828 C CB    . GLU B 2 124 ? 96.126  102.716 121.399 1.00 98.47  ? 124 GLU A CB    1 
ATOM   1829 C CG    . GLU B 2 124 ? 95.796  101.766 122.531 1.00 98.47  ? 124 GLU A CG    1 
ATOM   1830 C CD    . GLU B 2 124 ? 94.450  101.098 122.346 1.00 98.47  ? 124 GLU A CD    1 
ATOM   1831 O OE1   . GLU B 2 124 ? 93.792  101.364 121.318 1.00 98.47  ? 124 GLU A OE1   1 
ATOM   1832 O OE2   . GLU B 2 124 ? 94.049  100.307 123.224 1.00 98.47  ? 124 GLU A OE2   1 
ATOM   1833 N N     . PHE B 2 125 ? 98.909  101.740 120.535 1.00 94.65  ? 125 PHE A N     1 
ATOM   1834 C CA    . PHE B 2 125 ? 100.021 100.800 120.547 1.00 94.65  ? 125 PHE A CA    1 
ATOM   1835 C C     . PHE B 2 125 ? 101.333 101.510 120.830 1.00 94.65  ? 125 PHE A C     1 
ATOM   1836 O O     . PHE B 2 125 ? 102.205 100.957 121.507 1.00 94.65  ? 125 PHE A O     1 
ATOM   1837 C CB    . PHE B 2 125 ? 100.097 100.052 119.219 1.00 94.65  ? 125 PHE A CB    1 
ATOM   1838 C CG    . PHE B 2 125 ? 101.202 99.042  119.156 1.00 94.65  ? 125 PHE A CG    1 
ATOM   1839 C CD1   . PHE B 2 125 ? 101.021 97.773  119.672 1.00 94.65  ? 125 PHE A CD1   1 
ATOM   1840 C CD2   . PHE B 2 125 ? 102.417 99.357  118.576 1.00 94.65  ? 125 PHE A CD2   1 
ATOM   1841 C CE1   . PHE B 2 125 ? 102.031 96.839  119.616 1.00 94.65  ? 125 PHE A CE1   1 
ATOM   1842 C CE2   . PHE B 2 125 ? 103.431 98.425  118.517 1.00 94.65  ? 125 PHE A CE2   1 
ATOM   1843 C CZ    . PHE B 2 125 ? 103.238 97.165  119.037 1.00 94.65  ? 125 PHE A CZ    1 
ATOM   1844 N N     . ALA B 2 126 ? 101.481 102.744 120.348 1.00 92.95  ? 126 ALA A N     1 
ATOM   1845 C CA    . ALA B 2 126 ? 102.725 103.474 120.552 1.00 92.95  ? 126 ALA A CA    1 
ATOM   1846 C C     . ALA B 2 126 ? 102.960 103.761 122.026 1.00 92.95  ? 126 ALA A C     1 
ATOM   1847 O O     . ALA B 2 126 ? 104.072 103.581 122.530 1.00 92.95  ? 126 ALA A O     1 
ATOM   1848 C CB    . ALA B 2 126 ? 102.715 104.771 119.751 1.00 92.95  ? 126 ALA A CB    1 
ATOM   1849 N N     . ASP B 2 127 ? 101.926 104.203 122.745 1.00 95.18  ? 127 ASP A N     1 
ATOM   1850 C CA    . ASP B 2 127 ? 102.163 104.497 124.154 1.00 95.18  ? 127 ASP A CA    1 
ATOM   1851 C C     . ASP B 2 127 ? 102.217 103.225 124.992 1.00 95.18  ? 127 ASP A C     1 
ATOM   1852 O O     . ASP B 2 127 ? 102.956 103.176 125.983 1.00 95.18  ? 127 ASP A O     1 
ATOM   1853 C CB    . ASP B 2 127 ? 101.130 105.507 124.685 1.00 95.18  ? 127 ASP A CB    1 
ATOM   1854 C CG    . ASP B 2 127 ? 99.747  104.912 124.936 1.00 95.18  ? 127 ASP A CG    1 
ATOM   1855 O OD1   . ASP B 2 127 ? 99.539  103.693 124.807 1.00 95.18  ? 127 ASP A OD1   1 
ATOM   1856 O OD2   . ASP B 2 127 ? 98.840  105.700 125.278 1.00 95.18  ? 127 ASP A OD2   1 
ATOM   1857 N N     . ARG B 2 128 ? 101.488 102.176 124.595 1.00 94.22  ? 128 ARG A N     1 
ATOM   1858 C CA    . ARG B 2 128 ? 101.641 100.893 125.272 1.00 94.22  ? 128 ARG A CA    1 
ATOM   1859 C C     . ARG B 2 128 ? 103.048 100.340 125.097 1.00 94.22  ? 128 ARG A C     1 
ATOM   1860 O O     . ARG B 2 128 ? 103.544 99.620  125.970 1.00 94.22  ? 128 ARG A O     1 
ATOM   1861 C CB    . ARG B 2 128 ? 100.612 99.891  124.752 1.00 94.22  ? 128 ARG A CB    1 
ATOM   1862 C CG    . ARG B 2 128 ? 99.317  99.856  125.544 1.00 94.22  ? 128 ARG A CG    1 
ATOM   1863 C CD    . ARG B 2 128 ? 98.494  98.628  125.193 1.00 94.22  ? 128 ARG A CD    1 
ATOM   1864 N NE    . ARG B 2 128 ? 98.214  98.548  123.762 1.00 94.22  ? 128 ARG A NE    1 
ATOM   1865 C CZ    . ARG B 2 128 ? 97.609  97.521  123.174 1.00 94.22  ? 128 ARG A CZ    1 
ATOM   1866 N NH1   . ARG B 2 128 ? 97.215  96.479  123.894 1.00 94.22  ? 128 ARG A NH1   1 
ATOM   1867 N NH2   . ARG B 2 128 ? 97.397  97.534  121.865 1.00 94.22  ? 128 ARG A NH2   1 
ATOM   1868 N N     . LEU B 2 129 ? 103.701 100.657 123.979 1.00 90.42  ? 129 LEU A N     1 
ATOM   1869 C CA    . LEU B 2 129 ? 105.089 100.256 123.785 1.00 90.42  ? 129 LEU A CA    1 
ATOM   1870 C C     . LEU B 2 129 ? 106.041 101.150 124.568 1.00 90.42  ? 129 LEU A C     1 
ATOM   1871 O O     . LEU B 2 129 ? 106.983 100.658 125.195 1.00 90.42  ? 129 LEU A O     1 
ATOM   1872 C CB    . LEU B 2 129 ? 105.440 100.285 122.300 1.00 90.42  ? 129 LEU A CB    1 
ATOM   1873 C CG    . LEU B 2 129 ? 106.890 99.974  121.939 1.00 90.42  ? 129 LEU A CG    1 
ATOM   1874 C CD1   . LEU B 2 129 ? 107.220 98.534  122.280 1.00 90.42  ? 129 LEU A CD1   1 
ATOM   1875 C CD2   . LEU B 2 129 ? 107.147 100.252 120.470 1.00 90.42  ? 129 LEU A CD2   1 
ATOM   1876 N N     . GLN B 2 130 ? 105.808 102.463 124.538 1.00 89.85  ? 130 GLN A N     1 
ATOM   1877 C CA    . GLN B 2 130 ? 106.657 103.394 125.271 1.00 89.85  ? 130 GLN A CA    1 
ATOM   1878 C C     . GLN B 2 130 ? 106.644 103.105 126.764 1.00 89.85  ? 130 GLN A C     1 
ATOM   1879 O O     . GLN B 2 130 ? 107.646 103.335 127.449 1.00 89.85  ? 130 GLN A O     1 
ATOM   1880 C CB    . GLN B 2 130 ? 106.207 104.829 125.000 1.00 89.85  ? 130 GLN A CB    1 
ATOM   1881 C CG    . GLN B 2 130 ? 107.049 105.895 125.669 1.00 89.85  ? 130 GLN A CG    1 
ATOM   1882 C CD    . GLN B 2 130 ? 106.614 107.294 125.287 1.00 89.85  ? 130 GLN A CD    1 
ATOM   1883 O OE1   . GLN B 2 130 ? 106.280 107.558 124.132 1.00 89.85  ? 130 GLN A OE1   1 
ATOM   1884 N NE2   . GLN B 2 130 ? 106.609 108.199 126.258 1.00 89.85  ? 130 GLN A NE2   1 
ATOM   1885 N N     . ALA B 2 131 ? 105.527 102.596 127.285 1.00 90.29  ? 131 ALA A N     1 
ATOM   1886 C CA    . ALA B 2 131 ? 105.479 102.195 128.686 1.00 90.29  ? 131 ALA A CA    1 
ATOM   1887 C C     . ALA B 2 131 ? 106.364 100.994 128.989 1.00 90.29  ? 131 ALA A C     1 
ATOM   1888 O O     . ALA B 2 131 ? 106.533 100.656 130.164 1.00 90.29  ? 131 ALA A O     1 
ATOM   1889 C CB    . ALA B 2 131 ? 104.039 101.888 129.095 1.00 90.29  ? 131 ALA A CB    1 
ATOM   1890 N N     . ILE B 2 132 ? 106.922 100.347 127.972 1.00 91.29  ? 132 ILE A N     1 
ATOM   1891 C CA    . ILE B 2 132 ? 107.783 99.184  128.152 1.00 91.29  ? 132 ILE A CA    1 
ATOM   1892 C C     . ILE B 2 132 ? 109.244 99.528  127.899 1.00 91.29  ? 132 ILE A C     1 
ATOM   1893 O O     . ILE B 2 132 ? 110.126 99.127  128.657 1.00 91.29  ? 132 ILE A O     1 
ATOM   1894 C CB    . ILE B 2 132 ? 107.313 98.031  127.237 1.00 91.29  ? 132 ILE A CB    1 
ATOM   1895 C CG1   . ILE B 2 132 ? 105.965 97.492  127.712 1.00 91.29  ? 132 ILE A CG1   1 
ATOM   1896 C CG2   . ILE B 2 132 ? 108.349 96.925  127.195 1.00 91.29  ? 132 ILE A CG2   1 
ATOM   1897 C CD1   . ILE B 2 132 ? 105.956 97.057  129.158 1.00 91.29  ? 132 ILE A CD1   1 
ATOM   1898 N N     . LEU B 2 133 ? 109.514 100.277 126.835 1.00 87.02  ? 133 LEU A N     1 
ATOM   1899 C CA    . LEU B 2 133 ? 110.876 100.633 126.487 1.00 87.02  ? 133 LEU A CA    1 
ATOM   1900 C C     . LEU B 2 133 ? 111.440 101.637 127.489 1.00 87.02  ? 133 LEU A C     1 
ATOM   1901 O O     . LEU B 2 133 ? 110.689 102.327 128.181 1.00 87.02  ? 133 LEU A O     1 
ATOM   1902 C CB    . LEU B 2 133 ? 110.921 101.212 125.076 1.00 87.02  ? 133 LEU A CB    1 
ATOM   1903 C CG    . LEU B 2 133 ? 110.471 100.275 123.957 1.00 87.02  ? 133 LEU A CG    1 
ATOM   1904 C CD1   . LEU B 2 133 ? 110.922 100.803 122.610 1.00 87.02  ? 133 LEU A CD1   1 
ATOM   1905 C CD2   . LEU B 2 133 ? 111.009 98.875  124.187 1.00 87.02  ? 133 LEU A CD2   1 
ATOM   1906 N N     . PRO B 2 134 ? 112.763 101.726 127.594 1.00 85.24  ? 134 PRO A N     1 
ATOM   1907 C CA    . PRO B 2 134 ? 113.375 102.726 128.470 1.00 85.24  ? 134 PRO A CA    1 
ATOM   1908 C C     . PRO B 2 134 ? 113.058 104.130 127.993 1.00 85.24  ? 134 PRO A C     1 
ATOM   1909 O O     . PRO B 2 134 ? 112.797 104.343 126.800 1.00 85.24  ? 134 PRO A O     1 
ATOM   1910 C CB    . PRO B 2 134 ? 114.876 102.426 128.356 1.00 85.24  ? 134 PRO A CB    1 
ATOM   1911 C CG    . PRO B 2 134 ? 114.945 101.017 127.903 1.00 85.24  ? 134 PRO A CG    1 
ATOM   1912 C CD    . PRO B 2 134 ? 113.770 100.829 127.006 1.00 85.24  ? 134 PRO A CD    1 
ATOM   1913 N N     . PRO B 2 135 ? 113.070 105.115 128.892 1.00 82.91  ? 135 PRO A N     1 
ATOM   1914 C CA    . PRO B 2 135 ? 112.698 106.481 128.491 1.00 82.91  ? 135 PRO A CA    1 
ATOM   1915 C C     . PRO B 2 135 ? 113.584 107.067 127.410 1.00 82.91  ? 135 PRO A C     1 
ATOM   1916 O O     . PRO B 2 135 ? 113.219 108.090 126.822 1.00 82.91  ? 135 PRO A O     1 
ATOM   1917 C CB    . PRO B 2 135 ? 112.818 107.272 129.799 1.00 82.91  ? 135 PRO A CB    1 
ATOM   1918 C CG    . PRO B 2 135 ? 112.657 106.248 130.871 1.00 82.91  ? 135 PRO A CG    1 
ATOM   1919 C CD    . PRO B 2 135 ? 113.313 105.014 130.339 1.00 82.91  ? 135 PRO A CD    1 
ATOM   1920 N N     . GLY B 2 136 ? 114.734 106.458 127.126 1.00 80.94  ? 136 GLY A N     1 
ATOM   1921 C CA    . GLY B 2 136 ? 115.571 106.953 126.050 1.00 80.94  ? 136 GLY A CA    1 
ATOM   1922 C C     . GLY B 2 136 ? 115.046 106.589 124.679 1.00 80.94  ? 136 GLY A C     1 
ATOM   1923 O O     . GLY B 2 136 ? 115.318 107.290 123.701 1.00 80.94  ? 136 GLY A O     1 
ATOM   1924 N N     . LEU B 2 137 ? 114.291 105.497 124.585 1.00 81.21  ? 137 LEU A N     1 
ATOM   1925 C CA    . LEU B 2 137 ? 113.680 105.075 123.335 1.00 81.21  ? 137 LEU A CA    1 
ATOM   1926 C C     . LEU B 2 137 ? 112.365 105.795 123.060 1.00 81.21  ? 137 LEU A C     1 
ATOM   1927 O O     . LEU B 2 137 ? 111.554 105.310 122.262 1.00 81.21  ? 137 LEU A O     1 
ATOM   1928 C CB    . LEU B 2 137 ? 113.473 103.561 123.338 1.00 81.21  ? 137 LEU A CB    1 
ATOM   1929 C CG    . LEU B 2 137 ? 114.758 102.753 123.517 1.00 81.21  ? 137 LEU A CG    1 
ATOM   1930 C CD1   . LEU B 2 137 ? 114.483 101.267 123.416 1.00 81.21  ? 137 LEU A CD1   1 
ATOM   1931 C CD2   . LEU B 2 137 ? 115.786 103.173 122.489 1.00 81.21  ? 137 LEU A CD2   1 
ATOM   1932 N N     . LEU B 2 138 ? 112.129 106.930 123.720 1.00 82.40  ? 138 LEU A N     1 
ATOM   1933 C CA    . LEU B 2 138 ? 110.993 107.767 123.357 1.00 82.40  ? 138 LEU A CA    1 
ATOM   1934 C C     . LEU B 2 138 ? 111.115 108.236 121.917 1.00 82.40  ? 138 LEU A C     1 
ATOM   1935 O O     . LEU B 2 138 ? 110.122 108.279 121.184 1.00 82.40  ? 138 LEU A O     1 
ATOM   1936 C CB    . LEU B 2 138 ? 110.893 108.959 124.307 1.00 82.40  ? 138 LEU A CB    1 
ATOM   1937 C CG    . LEU B 2 138 ? 109.544 109.674 124.394 1.00 82.40  ? 138 LEU A CG    1 
ATOM   1938 C CD1   . LEU B 2 138 ? 109.327 110.213 125.797 1.00 82.40  ? 138 LEU A CD1   1 
ATOM   1939 C CD2   . LEU B 2 138 ? 109.450 110.795 123.377 1.00 82.40  ? 138 LEU A CD2   1 
ATOM   1940 N N     . GLY B 2 139 ? 112.330 108.575 121.487 1.00 79.27  ? 139 GLY A N     1 
ATOM   1941 C CA    . GLY B 2 139 ? 112.546 108.942 120.102 1.00 79.27  ? 139 GLY A CA    1 
ATOM   1942 C C     . GLY B 2 139 ? 112.397 107.791 119.134 1.00 79.27  ? 139 GLY A C     1 
ATOM   1943 O O     . GLY B 2 139 ? 112.208 108.023 117.937 1.00 79.27  ? 139 GLY A O     1 
ATOM   1944 N N     . LEU B 2 140 ? 112.484 106.555 119.622 1.00 77.84  ? 140 LEU A N     1 
ATOM   1945 C CA    . LEU B 2 140 ? 112.278 105.403 118.754 1.00 77.84  ? 140 LEU A CA    1 
ATOM   1946 C C     . LEU B 2 140 ? 110.803 105.049 118.655 1.00 77.84  ? 140 LEU A C     1 
ATOM   1947 O O     . LEU B 2 140 ? 110.330 104.641 117.590 1.00 77.84  ? 140 LEU A O     1 
ATOM   1948 C CB    . LEU B 2 140 ? 113.081 104.208 119.264 1.00 77.84  ? 140 LEU A CB    1 
ATOM   1949 C CG    . LEU B 2 140 ? 113.095 102.978 118.359 1.00 77.84  ? 140 LEU A CG    1 
ATOM   1950 C CD1   . LEU B 2 140 ? 113.874 103.258 117.089 1.00 77.84  ? 140 LEU A CD1   1 
ATOM   1951 C CD2   . LEU B 2 140 ? 113.676 101.786 119.093 1.00 77.84  ? 140 LEU A CD2   1 
ATOM   1952 N N     . VAL B 2 141 ? 110.061 105.194 119.752 1.00 79.91  ? 141 VAL A N     1 
ATOM   1953 C CA    . VAL B 2 141 ? 108.624 104.962 119.687 1.00 79.91  ? 141 VAL A CA    1 
ATOM   1954 C C     . VAL B 2 141 ? 107.893 106.139 119.061 1.00 79.91  ? 141 VAL A C     1 
ATOM   1955 O O     . VAL B 2 141 ? 106.743 105.987 118.639 1.00 79.91  ? 141 VAL A O     1 
ATOM   1956 C CB    . VAL B 2 141 ? 108.030 104.666 121.072 1.00 79.91  ? 141 VAL A CB    1 
ATOM   1957 C CG1   . VAL B 2 141 ? 108.724 103.477 121.693 1.00 79.91  ? 141 VAL A CG1   1 
ATOM   1958 C CG2   . VAL B 2 141 ? 108.131 105.880 121.967 1.00 79.91  ? 141 VAL A CG2   1 
ATOM   1959 N N     . ALA B 2 142 ? 108.528 107.310 118.979 1.00 79.12  ? 142 ALA A N     1 
ATOM   1960 C CA    . ALA B 2 142 ? 107.936 108.419 118.246 1.00 79.12  ? 142 ALA A CA    1 
ATOM   1961 C C     . ALA B 2 142 ? 107.969 108.190 116.745 1.00 79.12  ? 142 ALA A C     1 
ATOM   1962 O O     . ALA B 2 142 ? 107.205 108.828 116.016 1.00 79.12  ? 142 ALA A O     1 
ATOM   1963 C CB    . ALA B 2 142 ? 108.654 109.722 118.590 1.00 79.12  ? 142 ALA A CB    1 
ATOM   1964 N N     . ILE B 2 143 ? 108.842 107.305 116.268 1.00 76.29  ? 143 ILE A N     1 
ATOM   1965 C CA    . ILE B 2 143 ? 108.824 106.930 114.861 1.00 76.29  ? 143 ILE A CA    1 
ATOM   1966 C C     . ILE B 2 143 ? 107.608 106.067 114.565 1.00 76.29  ? 143 ILE A C     1 
ATOM   1967 O O     . ILE B 2 143 ? 106.917 106.261 113.562 1.00 76.29  ? 143 ILE A O     1 
ATOM   1968 C CB    . ILE B 2 143 ? 110.124 106.203 114.482 1.00 76.29  ? 143 ILE A CB    1 
ATOM   1969 C CG1   . ILE B 2 143 ? 111.329 107.118 114.665 1.00 76.29  ? 143 ILE A CG1   1 
ATOM   1970 C CG2   . ILE B 2 143 ? 110.052 105.708 113.057 1.00 76.29  ? 143 ILE A CG2   1 
ATOM   1971 C CD1   . ILE B 2 143 ? 112.645 106.422 114.425 1.00 76.29  ? 143 ILE A CD1   1 
ATOM   1972 N N     . LEU B 2 144 ? 107.332 105.098 115.436 1.00 78.82  ? 144 LEU A N     1 
ATOM   1973 C CA    . LEU B 2 144 ? 106.170 104.242 115.239 1.00 78.82  ? 144 LEU A CA    1 
ATOM   1974 C C     . LEU B 2 144 ? 104.875 104.982 115.538 1.00 78.82  ? 144 LEU A C     1 
ATOM   1975 O O     . LEU B 2 144 ? 103.822 104.632 114.995 1.00 78.82  ? 144 LEU A O     1 
ATOM   1976 C CB    . LEU B 2 144 ? 106.290 102.997 116.113 1.00 78.82  ? 144 LEU A CB    1 
ATOM   1977 C CG    . LEU B 2 144 ? 105.276 101.886 115.863 1.00 78.82  ? 144 LEU A CG    1 
ATOM   1978 C CD1   . LEU B 2 144 ? 105.505 101.262 114.499 1.00 78.82  ? 144 LEU A CD1   1 
ATOM   1979 C CD2   . LEU B 2 144 ? 105.375 100.842 116.954 1.00 78.82  ? 144 LEU A CD2   1 
ATOM   1980 N N     . ARG B 2 145 ? 104.929 106.003 116.392 1.00 81.71  ? 145 ARG A N     1 
ATOM   1981 C CA    . ARG B 2 145 ? 103.740 106.788 116.691 1.00 81.71  ? 145 ARG A CA    1 
ATOM   1982 C C     . ARG B 2 145 ? 103.395 107.755 115.571 1.00 81.71  ? 145 ARG A C     1 
ATOM   1983 O O     . ARG B 2 145 ? 102.233 108.150 115.447 1.00 81.71  ? 145 ARG A O     1 
ATOM   1984 C CB    . ARG B 2 145 ? 103.936 107.560 117.995 1.00 81.71  ? 145 ARG A CB    1 
ATOM   1985 C CG    . ARG B 2 145 ? 102.671 108.190 118.544 1.00 81.71  ? 145 ARG A CG    1 
ATOM   1986 C CD    . ARG B 2 145 ? 102.987 109.192 119.632 1.00 81.71  ? 145 ARG A CD    1 
ATOM   1987 N NE    . ARG B 2 145 ? 103.919 108.652 120.612 1.00 81.71  ? 145 ARG A NE    1 
ATOM   1988 C CZ    . ARG B 2 145 ? 103.552 107.965 121.686 1.00 81.71  ? 145 ARG A CZ    1 
ATOM   1989 N NH1   . ARG B 2 145 ? 102.269 107.731 121.917 1.00 81.71  ? 145 ARG A NH1   1 
ATOM   1990 N NH2   . ARG B 2 145 ? 104.467 107.511 122.529 1.00 81.71  ? 145 ARG A NH2   1 
ATOM   1991 N N     . ASN B 2 146 ? 104.371 108.143 114.760 1.00 77.23  ? 146 ASN A N     1 
ATOM   1992 C CA    . ASN B 2 146 ? 104.201 109.116 113.688 1.00 77.23  ? 146 ASN A CA    1 
ATOM   1993 C C     . ASN B 2 146 ? 104.843 108.601 112.411 1.00 77.23  ? 146 ASN A C     1 
ATOM   1994 O O     . ASN B 2 146 ? 105.638 109.282 111.762 1.00 77.23  ? 146 ASN A O     1 
ATOM   1995 C CB    . ASN B 2 146 ? 104.784 110.464 114.088 1.00 77.23  ? 146 ASN A CB    1 
ATOM   1996 C CG    . ASN B 2 146 ? 104.222 110.972 115.397 1.00 77.23  ? 146 ASN A CG    1 
ATOM   1997 O OD1   . ASN B 2 146 ? 103.096 111.460 115.453 1.00 77.23  ? 146 ASN A OD1   1 
ATOM   1998 N ND2   . ASN B 2 146 ? 105.006 110.858 116.459 1.00 77.23  ? 146 ASN A ND2   1 
ATOM   1999 N N     . TRP B 2 147 ? 104.507 107.365 112.040 1.00 72.93  ? 147 TRP A N     1 
ATOM   2000 C CA    . TRP B 2 147 ? 105.221 106.699 110.958 1.00 72.93  ? 147 TRP A CA    1 
ATOM   2001 C C     . TRP B 2 147 ? 104.984 107.366 109.611 1.00 72.93  ? 147 TRP A C     1 
ATOM   2002 O O     . TRP B 2 147 ? 105.822 107.241 108.715 1.00 72.93  ? 147 TRP A O     1 
ATOM   2003 C CB    . TRP B 2 147 ? 104.832 105.225 110.904 1.00 72.93  ? 147 TRP A CB    1 
ATOM   2004 C CG    . TRP B 2 147 ? 103.449 104.973 110.429 1.00 72.93  ? 147 TRP A CG    1 
ATOM   2005 C CD1   . TRP B 2 147 ? 102.330 104.873 111.191 1.00 72.93  ? 147 TRP A CD1   1 
ATOM   2006 C CD2   . TRP B 2 147 ? 103.036 104.769 109.077 1.00 72.93  ? 147 TRP A CD2   1 
ATOM   2007 N NE1   . TRP B 2 147 ? 101.239 104.626 110.399 1.00 72.93  ? 147 TRP A NE1   1 
ATOM   2008 C CE2   . TRP B 2 147 ? 101.648 104.557 109.094 1.00 72.93  ? 147 TRP A CE2   1 
ATOM   2009 C CE3   . TRP B 2 147 ? 103.706 104.748 107.853 1.00 72.93  ? 147 TRP A CE3   1 
ATOM   2010 C CZ2   . TRP B 2 147 ? 100.917 104.327 107.937 1.00 72.93  ? 147 TRP A CZ2   1 
ATOM   2011 C CZ3   . TRP B 2 147 ? 102.980 104.520 106.707 1.00 72.93  ? 147 TRP A CZ3   1 
ATOM   2012 C CH2   . TRP B 2 147 ? 101.600 104.313 106.755 1.00 72.93  ? 147 TRP A CH2   1 
ATOM   2013 N N     . THR B 2 148 ? 103.871 108.078 109.436 1.00 74.25  ? 148 THR A N     1 
ATOM   2014 C CA    . THR B 2 148 ? 103.708 108.838 108.201 1.00 74.25  ? 148 THR A CA    1 
ATOM   2015 C C     . THR B 2 148 ? 104.601 110.070 108.205 1.00 74.25  ? 148 THR A C     1 
ATOM   2016 O O     . THR B 2 148 ? 105.163 110.441 107.170 1.00 74.25  ? 148 THR A O     1 
ATOM   2017 C CB    . THR B 2 148 ? 102.248 109.234 107.997 1.00 74.25  ? 148 THR A CB    1 
ATOM   2018 O OG1   . THR B 2 148 ? 101.805 110.021 109.104 1.00 74.25  ? 148 THR A OG1   1 
ATOM   2019 C CG2   . THR B 2 148 ? 101.380 108.000 107.890 1.00 74.25  ? 148 THR A CG2   1 
ATOM   2020 N N     . PHE B 2 149 ? 104.767 110.702 109.366 1.00 73.13  ? 149 PHE A N     1 
ATOM   2021 C CA    . PHE B 2 149 ? 105.733 111.788 109.469 1.00 73.13  ? 149 PHE A CA    1 
ATOM   2022 C C     . PHE B 2 149 ? 107.149 111.261 109.300 1.00 73.13  ? 149 PHE A C     1 
ATOM   2023 O O     . PHE B 2 149 ? 108.019 111.949 108.757 1.00 73.13  ? 149 PHE A O     1 
ATOM   2024 C CB    . PHE B 2 149 ? 105.584 112.508 110.807 1.00 73.13  ? 149 PHE A CB    1 
ATOM   2025 C CG    . PHE B 2 149 ? 104.273 113.221 110.975 1.00 73.13  ? 149 PHE A CG    1 
ATOM   2026 C CD1   . PHE B 2 149 ? 103.368 113.302 109.937 1.00 73.13  ? 149 PHE A CD1   1 
ATOM   2027 C CD2   . PHE B 2 149 ? 103.951 113.813 112.178 1.00 73.13  ? 149 PHE A CD2   1 
ATOM   2028 C CE1   . PHE B 2 149 ? 102.170 113.953 110.096 1.00 73.13  ? 149 PHE A CE1   1 
ATOM   2029 C CE2   . PHE B 2 149 ? 102.754 114.466 112.341 1.00 73.13  ? 149 PHE A CE2   1 
ATOM   2030 C CZ    . PHE B 2 149 ? 101.863 114.536 111.298 1.00 73.13  ? 149 PHE A CZ    1 
ATOM   2031 N N     . ALA B 2 150 ? 107.391 110.023 109.734 1.00 72.17  ? 150 ALA A N     1 
ATOM   2032 C CA    . ALA B 2 150 ? 108.697 109.414 109.518 1.00 72.17  ? 150 ALA A CA    1 
ATOM   2033 C C     . ALA B 2 150 ? 108.924 109.123 108.043 1.00 72.17  ? 150 ALA A C     1 
ATOM   2034 O O     . ALA B 2 150 ? 110.039 109.280 107.538 1.00 72.17  ? 150 ALA A O     1 
ATOM   2035 C CB    . ALA B 2 150 ? 108.826 108.137 110.344 1.00 72.17  ? 150 ALA A CB    1 
ATOM   2036 N N     . ALA B 2 151 ? 107.878 108.699 107.334 1.00 71.47  ? 151 ALA A N     1 
ATOM   2037 C CA    . ALA B 2 151 ? 107.992 108.513 105.893 1.00 71.47  ? 151 ALA A CA    1 
ATOM   2038 C C     . ALA B 2 151 ? 108.244 109.838 105.193 1.00 71.47  ? 151 ALA A C     1 
ATOM   2039 O O     . ALA B 2 151 ? 109.007 109.902 104.226 1.00 71.47  ? 151 ALA A O     1 
ATOM   2040 C CB    . ALA B 2 151 ? 106.731 107.846 105.347 1.00 71.47  ? 151 ALA A CB    1 
ATOM   2041 N N     . PHE B 2 152 ? 107.607 110.909 105.667 1.00 74.55  ? 152 PHE A N     1 
ATOM   2042 C CA    . PHE B 2 152 ? 107.891 112.234 105.129 1.00 74.55  ? 152 PHE A CA    1 
ATOM   2043 C C     . PHE B 2 152 ? 109.347 112.616 105.358 1.00 74.55  ? 152 PHE A C     1 
ATOM   2044 O O     . PHE B 2 152 ? 109.998 113.161 104.463 1.00 74.55  ? 152 PHE A O     1 
ATOM   2045 C CB    . PHE B 2 152 ? 106.959 113.269 105.758 1.00 74.55  ? 152 PHE A CB    1 
ATOM   2046 C CG    . PHE B 2 152 ? 107.031 114.624 105.112 1.00 74.55  ? 152 PHE A CG    1 
ATOM   2047 C CD1   . PHE B 2 152 ? 108.044 115.508 105.429 1.00 74.55  ? 152 PHE A CD1   1 
ATOM   2048 C CD2   . PHE B 2 152 ? 106.085 115.011 104.186 1.00 74.55  ? 152 PHE A CD2   1 
ATOM   2049 C CE1   . PHE B 2 152 ? 108.112 116.744 104.836 1.00 74.55  ? 152 PHE A CE1   1 
ATOM   2050 C CE2   . PHE B 2 152 ? 106.150 116.249 103.592 1.00 74.55  ? 152 PHE A CE2   1 
ATOM   2051 C CZ    . PHE B 2 152 ? 107.165 117.115 103.918 1.00 74.55  ? 152 PHE A CZ    1 
ATOM   2052 N N     . TYR B 2 153 ? 109.870 112.350 106.555 1.00 75.73  ? 153 TYR A N     1 
ATOM   2053 C CA    . TYR B 2 153 ? 111.272 112.647 106.833 1.00 75.73  ? 153 TYR A CA    1 
ATOM   2054 C C     . TYR B 2 153 ? 112.190 111.849 105.919 1.00 75.73  ? 153 TYR A C     1 
ATOM   2055 O O     . TYR B 2 153 ? 113.150 112.391 105.356 1.00 75.73  ? 153 TYR A O     1 
ATOM   2056 C CB    . TYR B 2 153 ? 111.584 112.351 108.299 1.00 75.73  ? 153 TYR A CB    1 
ATOM   2057 C CG    . TYR B 2 153 ? 112.847 112.997 108.824 1.00 75.73  ? 153 TYR A CG    1 
ATOM   2058 C CD1   . TYR B 2 153 ? 114.096 112.523 108.461 1.00 75.73  ? 153 TYR A CD1   1 
ATOM   2059 C CD2   . TYR B 2 153 ? 112.787 114.069 109.697 1.00 75.73  ? 153 TYR A CD2   1 
ATOM   2060 C CE1   . TYR B 2 153 ? 115.245 113.104 108.944 1.00 75.73  ? 153 TYR A CE1   1 
ATOM   2061 C CE2   . TYR B 2 153 ? 113.931 114.654 110.186 1.00 75.73  ? 153 TYR A CE2   1 
ATOM   2062 C CZ    . TYR B 2 153 ? 115.156 114.169 109.806 1.00 75.73  ? 153 TYR A CZ    1 
ATOM   2063 O OH    . TYR B 2 153 ? 116.300 114.754 110.292 1.00 75.73  ? 153 TYR A OH    1 
ATOM   2064 N N     . VAL B 2 154 ? 111.907 110.556 105.761 1.00 73.65  ? 154 VAL A N     1 
ATOM   2065 C CA    . VAL B 2 154 ? 112.725 109.701 104.908 1.00 73.65  ? 154 VAL A CA    1 
ATOM   2066 C C     . VAL B 2 154 ? 112.690 110.193 103.471 1.00 73.65  ? 154 VAL A C     1 
ATOM   2067 O O     . VAL B 2 154 ? 113.722 110.254 102.801 1.00 73.65  ? 154 VAL A O     1 
ATOM   2068 C CB    . VAL B 2 154 ? 112.260 108.239 105.014 1.00 73.65  ? 154 VAL A CB    1 
ATOM   2069 C CG1   . VAL B 2 154 ? 112.931 107.397 103.954 1.00 73.65  ? 154 VAL A CG1   1 
ATOM   2070 C CG2   . VAL B 2 154 ? 112.561 107.693 106.389 1.00 73.65  ? 154 VAL A CG2   1 
ATOM   2071 N N     . LEU B 2 155 ? 111.510 110.567 102.978 1.00 75.17  ? 155 LEU A N     1 
ATOM   2072 C CA    . LEU B 2 155 ? 111.399 110.974 101.584 1.00 75.17  ? 155 LEU A CA    1 
ATOM   2073 C C     . LEU B 2 155 ? 111.964 112.367 101.353 1.00 75.17  ? 155 LEU A C     1 
ATOM   2074 O O     . LEU B 2 155 ? 112.425 112.663 100.252 1.00 75.17  ? 155 LEU A O     1 
ATOM   2075 C CB    . LEU B 2 155 ? 109.947 110.893 101.128 1.00 75.17  ? 155 LEU A CB    1 
ATOM   2076 C CG    . LEU B 2 155 ? 109.517 109.460 100.824 1.00 75.17  ? 155 LEU A CG    1 
ATOM   2077 C CD1   . LEU B 2 155 ? 108.123 109.417 100.250 1.00 75.17  ? 155 LEU A CD1   1 
ATOM   2078 C CD2   . LEU B 2 155 ? 110.501 108.813 99.870  1.00 75.17  ? 155 LEU A CD2   1 
ATOM   2079 N N     . ALA B 2 156 ? 111.974 113.224 102.373 1.00 75.83  ? 156 ALA A N     1 
ATOM   2080 C CA    . ALA B 2 156 ? 112.665 114.501 102.239 1.00 75.83  ? 156 ALA A CA    1 
ATOM   2081 C C     . ALA B 2 156 ? 114.174 114.301 102.198 1.00 75.83  ? 156 ALA A C     1 
ATOM   2082 O O     . ALA B 2 156 ? 114.869 114.914 101.376 1.00 75.83  ? 156 ALA A O     1 
ATOM   2083 C CB    . ALA B 2 156 ? 112.276 115.428 103.386 1.00 75.83  ? 156 ALA A CB    1 
ATOM   2084 N N     . GLU B 2 157 ? 114.698 113.450 103.085 1.00 80.53  ? 157 GLU A N     1 
ATOM   2085 C CA    . GLU B 2 157 ? 116.111 113.094 103.024 1.00 80.53  ? 157 GLU A CA    1 
ATOM   2086 C C     . GLU B 2 157 ? 116.458 112.463 101.683 1.00 80.53  ? 157 GLU A C     1 
ATOM   2087 O O     . GLU B 2 157 ? 117.528 112.723 101.123 1.00 80.53  ? 157 GLU A O     1 
ATOM   2088 C CB    . GLU B 2 157 ? 116.460 112.143 104.167 1.00 80.53  ? 157 GLU A CB    1 
ATOM   2089 C CG    . GLU B 2 157 ? 116.558 112.799 105.531 1.00 80.53  ? 157 GLU A CG    1 
ATOM   2090 C CD    . GLU B 2 157 ? 117.950 113.309 105.837 1.00 80.53  ? 157 GLU A CD    1 
ATOM   2091 O OE1   . GLU B 2 157 ? 118.929 112.693 105.368 1.00 80.53  ? 157 GLU A OE1   1 
ATOM   2092 O OE2   . GLU B 2 157 ? 118.068 114.325 106.552 1.00 80.53  ? 157 GLU A OE2   1 
ATOM   2093 N N     . LEU B 2 158 ? 115.559 111.639 101.145 1.00 79.80  ? 158 LEU A N     1 
ATOM   2094 C CA    . LEU B 2 158 ? 115.821 110.996 99.866  1.00 79.80  ? 158 LEU A CA    1 
ATOM   2095 C C     . LEU B 2 158 ? 115.710 111.975 98.712  1.00 79.80  ? 158 LEU A C     1 
ATOM   2096 O O     . LEU B 2 158 ? 116.415 111.820 97.718  1.00 79.80  ? 158 LEU A O     1 
ATOM   2097 C CB    . LEU B 2 158 ? 114.871 109.822 99.646  1.00 79.80  ? 158 LEU A CB    1 
ATOM   2098 C CG    . LEU B 2 158 ? 115.120 108.566 100.476 1.00 79.80  ? 158 LEU A CG    1 
ATOM   2099 C CD1   . LEU B 2 158 ? 114.287 107.417 99.945  1.00 79.80  ? 158 LEU A CD1   1 
ATOM   2100 C CD2   . LEU B 2 158 ? 116.591 108.211 100.480 1.00 79.80  ? 158 LEU A CD2   1 
ATOM   2101 N N     . TRP B 2 159 ? 114.838 112.976 98.806  1.00 76.98  ? 159 TRP A N     1 
ATOM   2102 C CA    . TRP B 2 159 ? 114.882 114.057 97.832  1.00 76.98  ? 159 TRP A CA    1 
ATOM   2103 C C     . TRP B 2 159 ? 116.251 114.709 97.849  1.00 76.98  ? 159 TRP A C     1 
ATOM   2104 O O     . TRP B 2 159 ? 116.951 114.738 96.833  1.00 76.98  ? 159 TRP A O     1 
ATOM   2105 C CB    . TRP B 2 159 ? 113.792 115.091 98.113  1.00 76.98  ? 159 TRP A CB    1 
ATOM   2106 C CG    . TRP B 2 159 ? 113.805 116.221 97.123  1.00 76.98  ? 159 TRP A CG    1 
ATOM   2107 C CD1   . TRP B 2 159 ? 114.559 117.351 97.185  1.00 76.98  ? 159 TRP A CD1   1 
ATOM   2108 C CD2   . TRP B 2 159 ? 113.040 116.318 95.917  1.00 76.98  ? 159 TRP A CD2   1 
ATOM   2109 N NE1   . TRP B 2 159 ? 114.311 118.148 96.099  1.00 76.98  ? 159 TRP A NE1   1 
ATOM   2110 C CE2   . TRP B 2 159 ? 113.380 117.535 95.304  1.00 76.98  ? 159 TRP A CE2   1 
ATOM   2111 C CE3   . TRP B 2 159 ? 112.099 115.494 95.299  1.00 76.98  ? 159 TRP A CE3   1 
ATOM   2112 C CZ2   . TRP B 2 159 ? 112.814 117.948 94.106  1.00 76.98  ? 159 TRP A CZ2   1 
ATOM   2113 C CZ3   . TRP B 2 159 ? 111.539 115.907 94.111  1.00 76.98  ? 159 TRP A CZ3   1 
ATOM   2114 C CH2   . TRP B 2 159 ? 111.897 117.122 93.527  1.00 76.98  ? 159 TRP A CH2   1 
ATOM   2115 N N     . GLY B 2 160 ? 116.671 115.178 99.024  1.00 83.26  ? 160 GLY A N     1 
ATOM   2116 C CA    . GLY B 2 160 ? 117.966 115.823 99.144  1.00 83.26  ? 160 GLY A CA    1 
ATOM   2117 C C     . GLY B 2 160 ? 119.116 114.982 98.630  1.00 83.26  ? 160 GLY A C     1 
ATOM   2118 O O     . GLY B 2 160 ? 120.049 115.508 98.020  1.00 83.26  ? 160 GLY A O     1 
ATOM   2119 N N     . SER B 2 161 ? 119.072 113.670 98.862  1.00 84.07  ? 161 SER A N     1 
ATOM   2120 C CA    . SER B 2 161 ? 120.141 112.802 98.369  1.00 84.07  ? 161 SER A CA    1 
ATOM   2121 C C     . SER B 2 161 ? 119.987 112.543 96.875  1.00 84.07  ? 161 SER A C     1 
ATOM   2122 O O     . SER B 2 161 ? 120.782 113.026 96.067  1.00 84.07  ? 161 SER A O     1 
ATOM   2123 C CB    . SER B 2 161 ? 120.156 111.484 99.150  1.00 84.07  ? 161 SER A CB    1 
ATOM   2124 O OG    . SER B 2 161 ? 120.501 111.698 100.506 1.00 84.07  ? 161 SER A OG    1 
ATOM   2125 N N     . VAL B 2 162 ? 118.925 111.845 96.485  1.00 84.88  ? 162 VAL A N     1 
ATOM   2126 C CA    . VAL B 2 162 ? 118.741 111.424 95.106  1.00 84.88  ? 162 VAL A CA    1 
ATOM   2127 C C     . VAL B 2 162 ? 118.607 112.629 94.189  1.00 84.88  ? 162 VAL A C     1 
ATOM   2128 O O     . VAL B 2 162 ? 119.544 112.947 93.453  1.00 84.88  ? 162 VAL A O     1 
ATOM   2129 C CB    . VAL B 2 162 ? 117.506 110.518 94.988  1.00 84.88  ? 162 VAL A CB    1 
ATOM   2130 C CG1   . VAL B 2 162 ? 117.347 110.029 93.571  1.00 84.88  ? 162 VAL A CG1   1 
ATOM   2131 C CG2   . VAL B 2 162 ? 117.621 109.353 95.948  1.00 84.88  ? 162 VAL A CG2   1 
ATOM   2132 N N     . MET B 2 163 ? 117.514 113.384 94.327  1.00 84.36  ? 163 MET A N     1 
ATOM   2133 C CA    . MET B 2 163 ? 117.162 114.348 93.295  1.00 84.36  ? 163 MET A CA    1 
ATOM   2134 C C     . MET B 2 163 ? 118.172 115.474 93.193  1.00 84.36  ? 163 MET A C     1 
ATOM   2135 O O     . MET B 2 163 ? 118.251 116.127 92.149  1.00 84.36  ? 163 MET A O     1 
ATOM   2136 C CB    . MET B 2 163 ? 115.775 114.927 93.561  1.00 84.36  ? 163 MET A CB    1 
ATOM   2137 C CG    . MET B 2 163 ? 114.629 114.015 93.164  1.00 84.36  ? 163 MET A CG    1 
ATOM   2138 S SD    . MET B 2 163 ? 114.640 113.549 91.424  1.00 84.36  ? 163 MET A SD    1 
ATOM   2139 C CE    . MET B 2 163 ? 114.782 115.148 90.641  1.00 84.36  ? 163 MET A CE    1 
ATOM   2140 N N     . LEU B 2 164 ? 118.949 115.714 94.245  1.00 86.12  ? 164 LEU A N     1 
ATOM   2141 C CA    . LEU B 2 164 ? 119.934 116.784 94.232  1.00 86.12  ? 164 LEU A CA    1 
ATOM   2142 C C     . LEU B 2 164 ? 121.335 116.269 93.924  1.00 86.12  ? 164 LEU A C     1 
ATOM   2143 O O     . LEU B 2 164 ? 121.946 116.699 92.943  1.00 86.12  ? 164 LEU A O     1 
ATOM   2144 C CB    . LEU B 2 164 ? 119.902 117.532 95.570  1.00 86.12  ? 164 LEU A CB    1 
ATOM   2145 C CG    . LEU B 2 164 ? 120.828 118.738 95.681  1.00 86.12  ? 164 LEU A CG    1 
ATOM   2146 C CD1   . LEU B 2 164 ? 120.514 119.715 94.582  1.00 86.12  ? 164 LEU A CD1   1 
ATOM   2147 C CD2   . LEU B 2 164 ? 120.649 119.404 97.027  1.00 86.12  ? 164 LEU A CD2   1 
ATOM   2148 N N     . SER B 2 165 ? 121.857 115.343 94.733  1.00 87.74  ? 165 SER A N     1 
ATOM   2149 C CA    . SER B 2 165 ? 123.235 114.912 94.550  1.00 87.74  ? 165 SER A CA    1 
ATOM   2150 C C     . SER B 2 165 ? 123.369 113.872 93.445  1.00 87.74  ? 165 SER A C     1 
ATOM   2151 O O     . SER B 2 165 ? 124.337 113.909 92.680  1.00 87.74  ? 165 SER A O     1 
ATOM   2152 C CB    . SER B 2 165 ? 123.786 114.358 95.863  1.00 87.74  ? 165 SER A CB    1 
ATOM   2153 O OG    . SER B 2 165 ? 123.570 115.264 96.928  1.00 87.74  ? 165 SER A OG    1 
ATOM   2154 N N     . LEU B 2 166 ? 122.442 112.919 93.352  1.00 89.58  ? 166 LEU A N     1 
ATOM   2155 C CA    . LEU B 2 166 ? 122.598 111.864 92.362  1.00 89.58  ? 166 LEU A CA    1 
ATOM   2156 C C     . LEU B 2 166 ? 122.012 112.282 91.018  1.00 89.58  ? 166 LEU A C     1 
ATOM   2157 O O     . LEU B 2 166 ? 122.748 112.439 90.041  1.00 89.58  ? 166 LEU A O     1 
ATOM   2158 C CB    . LEU B 2 166 ? 121.934 110.578 92.864  1.00 89.58  ? 166 LEU A CB    1 
ATOM   2159 C CG    . LEU B 2 166 ? 121.731 109.458 91.845  1.00 89.58  ? 166 LEU A CG    1 
ATOM   2160 C CD1   . LEU B 2 166 ? 123.028 108.711 91.598  1.00 89.58  ? 166 LEU A CD1   1 
ATOM   2161 C CD2   . LEU B 2 166 ? 120.645 108.510 92.315  1.00 89.58  ? 166 LEU A CD2   1 
ATOM   2162 N N     . MET B 2 167 ? 120.704 112.530 90.973  1.00 91.25  ? 167 MET A N     1 
ATOM   2163 C CA    . MET B 2 167 ? 120.013 112.788 89.715  1.00 91.25  ? 167 MET A CA    1 
ATOM   2164 C C     . MET B 2 167 ? 120.527 114.039 89.017  1.00 91.25  ? 167 MET A C     1 
ATOM   2165 O O     . MET B 2 167 ? 121.062 113.959 87.904  1.00 91.25  ? 167 MET A O     1 
ATOM   2166 C CB    . MET B 2 167 ? 118.509 112.915 89.946  1.00 91.25  ? 167 MET A CB    1 
ATOM   2167 C CG    . MET B 2 167 ? 117.839 111.634 90.382  1.00 91.25  ? 167 MET A CG    1 
ATOM   2168 S SD    . MET B 2 167 ? 118.375 110.210 89.424  1.00 91.25  ? 167 MET A SD    1 
ATOM   2169 C CE    . MET B 2 167 ? 117.767 110.635 87.798  1.00 91.25  ? 167 MET A CE    1 
ATOM   2170 N N     . PHE B 2 168 ? 120.362 115.198 89.659  1.00 88.87  ? 168 PHE A N     1 
ATOM   2171 C CA    . PHE B 2 168 ? 120.710 116.446 88.994  1.00 88.87  ? 168 PHE A CA    1 
ATOM   2172 C C     . PHE B 2 168 ? 122.198 116.527 88.708  1.00 88.87  ? 168 PHE A C     1 
ATOM   2173 O O     . PHE B 2 168 ? 122.604 117.025 87.656  1.00 88.87  ? 168 PHE A O     1 
ATOM   2174 C CB    . PHE B 2 168 ? 120.290 117.653 89.825  1.00 88.87  ? 168 PHE A CB    1 
ATOM   2175 C CG    . PHE B 2 168 ? 120.749 118.958 89.241  1.00 88.87  ? 168 PHE A CG    1 
ATOM   2176 C CD1   . PHE B 2 168 ? 120.124 119.486 88.128  1.00 88.87  ? 168 PHE A CD1   1 
ATOM   2177 C CD2   . PHE B 2 168 ? 121.826 119.633 89.776  1.00 88.87  ? 168 PHE A CD2   1 
ATOM   2178 C CE1   . PHE B 2 168 ? 120.551 120.673 87.577  1.00 88.87  ? 168 PHE A CE1   1 
ATOM   2179 C CE2   . PHE B 2 168 ? 122.258 120.817 89.223  1.00 88.87  ? 168 PHE A CE2   1 
ATOM   2180 C CZ    . PHE B 2 168 ? 121.618 121.339 88.126  1.00 88.87  ? 168 PHE A CZ    1 
ATOM   2181 N N     . TRP B 2 169 ? 123.033 116.059 89.632  1.00 92.50  ? 169 TRP A N     1 
ATOM   2182 C CA    . TRP B 2 169 ? 124.462 116.221 89.410  1.00 92.50  ? 169 TRP A CA    1 
ATOM   2183 C C     . TRP B 2 169 ? 125.000 115.224 88.398  1.00 92.50  ? 169 TRP A C     1 
ATOM   2184 O O     . TRP B 2 169 ? 125.931 115.556 87.660  1.00 92.50  ? 169 TRP A O     1 
ATOM   2185 C CB    . TRP B 2 169 ? 125.225 116.127 90.727  1.00 92.50  ? 169 TRP A CB    1 
ATOM   2186 C CG    . TRP B 2 169 ? 125.193 117.409 91.503  1.00 92.50  ? 169 TRP A CG    1 
ATOM   2187 C CD1   . TRP B 2 169 ? 124.769 117.576 92.785  1.00 92.50  ? 169 TRP A CD1   1 
ATOM   2188 C CD2   . TRP B 2 169 ? 125.590 118.706 91.041  1.00 92.50  ? 169 TRP A CD2   1 
ATOM   2189 N NE1   . TRP B 2 169 ? 124.879 118.892 93.154  1.00 92.50  ? 169 TRP A NE1   1 
ATOM   2190 C CE2   . TRP B 2 169 ? 125.381 119.607 92.101  1.00 92.50  ? 169 TRP A CE2   1 
ATOM   2191 C CE3   . TRP B 2 169 ? 126.105 119.192 89.837  1.00 92.50  ? 169 TRP A CE3   1 
ATOM   2192 C CZ2   . TRP B 2 169 ? 125.669 120.962 91.994  1.00 92.50  ? 169 TRP A CZ2   1 
ATOM   2193 C CZ3   . TRP B 2 169 ? 126.388 120.537 89.733  1.00 92.50  ? 169 TRP A CZ3   1 
ATOM   2194 C CH2   . TRP B 2 169 ? 126.170 121.407 90.804  1.00 92.50  ? 169 TRP A CH2   1 
ATOM   2195 N N     . GLY B 2 170 ? 124.426 114.023 88.309  1.00 97.90  ? 170 GLY A N     1 
ATOM   2196 C CA    . GLY B 2 170 ? 124.762 113.153 87.200  1.00 97.90  ? 170 GLY A CA    1 
ATOM   2197 C C     . GLY B 2 170 ? 124.341 113.750 85.875  1.00 97.90  ? 170 GLY A C     1 
ATOM   2198 O O     . GLY B 2 170 ? 125.101 113.726 84.905  1.00 97.90  ? 170 GLY A O     1 
ATOM   2199 N N     . PHE B 2 171 ? 123.137 114.324 85.827  1.00 100.04 ? 171 PHE A N     1 
ATOM   2200 C CA    . PHE B 2 171 ? 122.682 115.007 84.620  1.00 100.04 ? 171 PHE A CA    1 
ATOM   2201 C C     . PHE B 2 171 ? 123.642 116.122 84.226  1.00 100.04 ? 171 PHE A C     1 
ATOM   2202 O O     . PHE B 2 171 ? 124.038 116.239 83.060  1.00 100.04 ? 171 PHE A O     1 
ATOM   2203 C CB    . PHE B 2 171 ? 121.276 115.557 84.845  1.00 100.04 ? 171 PHE A CB    1 
ATOM   2204 C CG    . PHE B 2 171 ? 120.699 116.257 83.655  1.00 100.04 ? 171 PHE A CG    1 
ATOM   2205 C CD1   . PHE B 2 171 ? 120.562 115.599 82.449  1.00 100.04 ? 171 PHE A CD1   1 
ATOM   2206 C CD2   . PHE B 2 171 ? 120.282 117.570 83.747  1.00 100.04 ? 171 PHE A CD2   1 
ATOM   2207 C CE1   . PHE B 2 171 ? 120.027 116.241 81.356  1.00 100.04 ? 171 PHE A CE1   1 
ATOM   2208 C CE2   . PHE B 2 171 ? 119.745 118.215 82.657  1.00 100.04 ? 171 PHE A CE2   1 
ATOM   2209 C CZ    . PHE B 2 171 ? 119.617 117.549 81.460  1.00 100.04 ? 171 PHE A CZ    1 
ATOM   2210 N N     . ALA B 2 172 ? 124.039 116.945 85.196  1.00 101.59 ? 172 ALA A N     1 
ATOM   2211 C CA    . ALA B 2 172 ? 124.931 118.061 84.912  1.00 101.59 ? 172 ALA A CA    1 
ATOM   2212 C C     . ALA B 2 172 ? 126.286 117.567 84.429  1.00 101.59 ? 172 ALA A C     1 
ATOM   2213 O O     . ALA B 2 172 ? 126.734 117.929 83.336  1.00 101.59 ? 172 ALA A O     1 
ATOM   2214 C CB    . ALA B 2 172 ? 125.086 118.936 86.154  1.00 101.59 ? 172 ALA A CB    1 
ATOM   2215 N N     . ASN B 2 173 ? 126.944 116.716 85.222  1.00 103.81 ? 173 ASN A N     1 
ATOM   2216 C CA    . ASN B 2 173 ? 128.261 116.215 84.850  1.00 103.81 ? 173 ASN A CA    1 
ATOM   2217 C C     . ASN B 2 173 ? 128.228 115.465 83.526  1.00 103.81 ? 173 ASN A C     1 
ATOM   2218 O O     . ASN B 2 173 ? 129.251 115.378 82.839  1.00 103.81 ? 173 ASN A O     1 
ATOM   2219 C CB    . ASN B 2 173 ? 128.807 115.314 85.956  1.00 103.81 ? 173 ASN A CB    1 
ATOM   2220 C CG    . ASN B 2 173 ? 128.987 116.049 87.266  1.00 103.81 ? 173 ASN A CG    1 
ATOM   2221 O OD1   . ASN B 2 173 ? 129.191 117.261 87.286  1.00 103.81 ? 173 ASN A OD1   1 
ATOM   2222 N ND2   . ASN B 2 173 ? 128.911 115.318 88.371  1.00 103.81 ? 173 ASN A ND2   1 
ATOM   2223 N N     . GLU B 2 174 ? 127.071 114.922 83.146  1.00 110.73 ? 174 GLU A N     1 
ATOM   2224 C CA    . GLU B 2 174 ? 126.970 114.267 81.851  1.00 110.73 ? 174 GLU A CA    1 
ATOM   2225 C C     . GLU B 2 174 ? 126.847 115.278 80.719  1.00 110.73 ? 174 GLU A C     1 
ATOM   2226 O O     . GLU B 2 174 ? 127.495 115.126 79.678  1.00 110.73 ? 174 GLU A O     1 
ATOM   2227 C CB    . GLU B 2 174 ? 125.780 113.309 81.841  1.00 110.73 ? 174 GLU A CB    1 
ATOM   2228 C CG    . GLU B 2 174 ? 125.504 112.670 80.491  1.00 110.73 ? 174 GLU A CG    1 
ATOM   2229 C CD    . GLU B 2 174 ? 126.587 111.695 80.068  1.00 110.73 ? 174 GLU A CD    1 
ATOM   2230 O OE1   . GLU B 2 174 ? 127.310 111.181 80.947  1.00 110.73 ? 174 GLU A OE1   1 
ATOM   2231 O OE2   . GLU B 2 174 ? 126.715 111.442 78.852  1.00 110.73 ? 174 GLU A OE2   1 
ATOM   2232 N N     . ILE B 2 175 ? 126.033 116.321 80.901  1.00 108.42 ? 175 ILE A N     1 
ATOM   2233 C CA    . ILE B 2 175 ? 125.737 117.237 79.802  1.00 108.42 ? 175 ILE A CA    1 
ATOM   2234 C C     . ILE B 2 175 ? 126.599 118.490 79.804  1.00 108.42 ? 175 ILE A C     1 
ATOM   2235 O O     . ILE B 2 175 ? 126.635 119.197 78.784  1.00 108.42 ? 175 ILE A O     1 
ATOM   2236 C CB    . ILE B 2 175 ? 124.249 117.640 79.795  1.00 108.42 ? 175 ILE A CB    1 
ATOM   2237 C CG1   . ILE B 2 175 ? 123.976 118.688 80.871  1.00 108.42 ? 175 ILE A CG1   1 
ATOM   2238 C CG2   . ILE B 2 175 ? 123.372 116.418 79.986  1.00 108.42 ? 175 ILE A CG2   1 
ATOM   2239 C CD1   . ILE B 2 175 ? 122.615 119.318 80.764  1.00 108.42 ? 175 ILE A CD1   1 
ATOM   2240 N N     . THR B 2 176 ? 127.290 118.796 80.896  1.00 109.05 ? 176 THR A N     1 
ATOM   2241 C CA    . THR B 2 176 ? 128.125 119.986 80.914  1.00 109.05 ? 176 THR A CA    1 
ATOM   2242 C C     . THR B 2 176 ? 129.474 119.695 80.267  1.00 109.05 ? 176 THR A C     1 
ATOM   2243 O O     . THR B 2 176 ? 129.956 118.559 80.263  1.00 109.05 ? 176 THR A O     1 
ATOM   2244 C CB    . THR B 2 176 ? 128.326 120.501 82.341  1.00 109.05 ? 176 THR A CB    1 
ATOM   2245 O OG1   . THR B 2 176 ? 128.825 121.842 82.297  1.00 109.05 ? 176 THR A OG1   1 
ATOM   2246 C CG2   . THR B 2 176 ? 129.325 119.637 83.093  1.00 109.05 ? 176 THR A CG2   1 
ATOM   2247 N N     . LYS B 2 177 ? 130.065 120.731 79.687  1.00 114.27 ? 177 LYS A N     1 
ATOM   2248 C CA    . LYS B 2 177 ? 131.400 120.634 79.121  1.00 114.27 ? 177 LYS A CA    1 
ATOM   2249 C C     . LYS B 2 177 ? 132.430 121.085 80.147  1.00 114.27 ? 177 LYS A C     1 
ATOM   2250 O O     . LYS B 2 177 ? 132.145 121.908 81.019  1.00 114.27 ? 177 LYS A O     1 
ATOM   2251 C CB    . LYS B 2 177 ? 131.515 121.481 77.854  1.00 114.27 ? 177 LYS A CB    1 
ATOM   2252 C CG    . LYS B 2 177 ? 130.706 120.953 76.684  1.00 114.27 ? 177 LYS A CG    1 
ATOM   2253 C CD    . LYS B 2 177 ? 130.817 121.870 75.479  1.00 114.27 ? 177 LYS A CD    1 
ATOM   2254 C CE    . LYS B 2 177 ? 130.147 121.260 74.262  1.00 114.27 ? 177 LYS A CE    1 
ATOM   2255 N NZ    . LYS B 2 177 ? 130.762 119.955 73.898  1.00 114.27 ? 177 LYS A NZ    1 
ATOM   2256 N N     . ILE B 2 178 ? 133.637 120.528 80.038  1.00 115.38 ? 178 ILE A N     1 
ATOM   2257 C CA    . ILE B 2 178 ? 134.685 120.839 81.007  1.00 115.38 ? 178 ILE A CA    1 
ATOM   2258 C C     . ILE B 2 178 ? 135.045 122.318 80.950  1.00 115.38 ? 178 ILE A C     1 
ATOM   2259 O O     . ILE B 2 178 ? 135.322 122.944 81.980  1.00 115.38 ? 178 ILE A O     1 
ATOM   2260 C CB    . ILE B 2 178 ? 135.914 119.939 80.779  1.00 115.38 ? 178 ILE A CB    1 
ATOM   2261 C CG1   . ILE B 2 178 ? 135.571 118.474 81.059  1.00 115.38 ? 178 ILE A CG1   1 
ATOM   2262 C CG2   . ILE B 2 178 ? 137.077 120.374 81.657  1.00 115.38 ? 178 ILE A CG2   1 
ATOM   2263 C CD1   . ILE B 2 178 ? 135.099 117.697 79.849  1.00 115.38 ? 178 ILE A CD1   1 
ATOM   2264 N N     . HIS B 2 179 ? 135.015 122.910 79.755  1.00 114.16 ? 179 HIS A N     1 
ATOM   2265 C CA    . HIS B 2 179 ? 135.291 124.335 79.638  1.00 114.16 ? 179 HIS A CA    1 
ATOM   2266 C C     . HIS B 2 179 ? 134.139 125.194 80.140  1.00 114.16 ? 179 HIS A C     1 
ATOM   2267 O O     . HIS B 2 179 ? 134.316 126.407 80.295  1.00 114.16 ? 179 HIS A O     1 
ATOM   2268 C CB    . HIS B 2 179 ? 135.614 124.697 78.187  1.00 114.16 ? 179 HIS A CB    1 
ATOM   2269 C CG    . HIS B 2 179 ? 134.409 124.851 77.314  1.00 114.16 ? 179 HIS A CG    1 
ATOM   2270 N ND1   . HIS B 2 179 ? 133.759 126.055 77.149  1.00 114.16 ? 179 HIS A ND1   1 
ATOM   2271 C CD2   . HIS B 2 179 ? 133.737 123.954 76.554  1.00 114.16 ? 179 HIS A CD2   1 
ATOM   2272 C CE1   . HIS B 2 179 ? 132.739 125.894 76.326  1.00 114.16 ? 179 HIS A CE1   1 
ATOM   2273 N NE2   . HIS B 2 179 ? 132.703 124.628 75.952  1.00 114.16 ? 179 HIS A NE2   1 
ATOM   2274 N N     . GLU B 2 180 ? 132.971 124.601 80.394  1.00 112.65 ? 180 GLU A N     1 
ATOM   2275 C CA    . GLU B 2 180 ? 131.852 125.305 81.006  1.00 112.65 ? 180 GLU A CA    1 
ATOM   2276 C C     . GLU B 2 180 ? 131.698 125.000 82.487  1.00 112.65 ? 180 GLU A C     1 
ATOM   2277 O O     . GLU B 2 180 ? 131.153 125.836 83.217  1.00 112.65 ? 180 GLU A O     1 
ATOM   2278 C CB    . GLU B 2 180 ? 130.540 124.940 80.302  1.00 112.65 ? 180 GLU A CB    1 
ATOM   2279 C CG    . GLU B 2 180 ? 130.530 125.171 78.807  1.00 112.65 ? 180 GLU A CG    1 
ATOM   2280 C CD    . GLU B 2 180 ? 129.261 124.663 78.151  1.00 112.65 ? 180 GLU A CD    1 
ATOM   2281 O OE1   . GLU B 2 180 ? 128.657 123.709 78.684  1.00 112.65 ? 180 GLU A OE1   1 
ATOM   2282 O OE2   . GLU B 2 180 ? 128.867 125.219 77.106  1.00 112.65 ? 180 GLU A OE2   1 
ATOM   2283 N N     . ALA B 2 181 ? 132.213 123.851 82.934  1.00 109.89 ? 181 ALA A N     1 
ATOM   2284 C CA    . ALA B 2 181 ? 131.837 123.287 84.227  1.00 109.89 ? 181 ALA A CA    1 
ATOM   2285 C C     . ALA B 2 181 ? 132.067 124.262 85.373  1.00 109.89 ? 181 ALA A C     1 
ATOM   2286 O O     . ALA B 2 181 ? 131.217 124.389 86.257  1.00 109.89 ? 181 ALA A O     1 
ATOM   2287 C CB    . ALA B 2 181 ? 132.609 121.992 84.473  1.00 109.89 ? 181 ALA A CB    1 
ATOM   2288 N N     . LYS B 2 182 ? 133.205 124.956 85.383  1.00 108.84 ? 182 LYS A N     1 
ATOM   2289 C CA    . LYS B 2 182 ? 133.518 125.825 86.514  1.00 108.84 ? 182 LYS A CA    1 
ATOM   2290 C C     . LYS B 2 182 ? 132.513 126.965 86.626  1.00 108.84 ? 182 LYS A C     1 
ATOM   2291 O O     . LYS B 2 182 ? 131.956 127.216 87.702  1.00 108.84 ? 182 LYS A O     1 
ATOM   2292 C CB    . LYS B 2 182 ? 134.939 126.370 86.381  1.00 108.84 ? 182 LYS A CB    1 
ATOM   2293 C CG    . LYS B 2 182 ? 135.375 127.231 87.551  1.00 108.84 ? 182 LYS A CG    1 
ATOM   2294 C CD    . LYS B 2 182 ? 136.871 127.484 87.529  1.00 108.84 ? 182 LYS A CD    1 
ATOM   2295 C CE    . LYS B 2 182 ? 137.288 128.398 88.668  1.00 108.84 ? 182 LYS A CE    1 
ATOM   2296 N NZ    . LYS B 2 182 ? 136.792 127.905 89.981  1.00 108.84 ? 182 LYS A NZ    1 
ATOM   2297 N N     . ARG B 2 183 ? 132.264 127.663 85.518  1.00 111.29 ? 183 ARG A N     1 
ATOM   2298 C CA    . ARG B 2 183 ? 131.324 128.777 85.541  1.00 111.29 ? 183 ARG A CA    1 
ATOM   2299 C C     . ARG B 2 183 ? 129.907 128.299 85.826  1.00 111.29 ? 183 ARG A C     1 
ATOM   2300 O O     . ARG B 2 183 ? 129.170 128.941 86.585  1.00 111.29 ? 183 ARG A O     1 
ATOM   2301 C CB    . ARG B 2 183 ? 131.387 129.534 84.216  1.00 111.29 ? 183 ARG A CB    1 
ATOM   2302 C CG    . ARG B 2 183 ? 132.780 130.042 83.879  1.00 111.29 ? 183 ARG A CG    1 
ATOM   2303 C CD    . ARG B 2 183 ? 132.826 130.692 82.510  1.00 111.29 ? 183 ARG A CD    1 
ATOM   2304 N NE    . ARG B 2 183 ? 132.638 129.719 81.440  1.00 111.29 ? 183 ARG A NE    1 
ATOM   2305 C CZ    . ARG B 2 183 ? 131.605 129.717 80.606  1.00 111.29 ? 183 ARG A CZ    1 
ATOM   2306 N NH1   . ARG B 2 183 ? 130.662 130.642 80.713  1.00 111.29 ? 183 ARG A NH1   1 
ATOM   2307 N NH2   . ARG B 2 183 ? 131.516 128.793 79.661  1.00 111.29 ? 183 ARG A NH2   1 
ATOM   2308 N N     . PHE B 2 184 ? 129.511 127.167 85.240  1.00 106.43 ? 184 PHE A N     1 
ATOM   2309 C CA    . PHE B 2 184 ? 128.168 126.650 85.479  1.00 106.43 ? 184 PHE A CA    1 
ATOM   2310 C C     . PHE B 2 184 ? 127.985 126.259 86.938  1.00 106.43 ? 184 PHE A C     1 
ATOM   2311 O O     . PHE B 2 184 ? 126.931 126.513 87.529  1.00 106.43 ? 184 PHE A O     1 
ATOM   2312 C CB    . PHE B 2 184 ? 127.888 125.459 84.564  1.00 106.43 ? 184 PHE A CB    1 
ATOM   2313 C CG    . PHE B 2 184 ? 127.454 125.844 83.181  1.00 106.43 ? 184 PHE A CG    1 
ATOM   2314 C CD1   . PHE B 2 184 ? 127.876 127.030 82.609  1.00 106.43 ? 184 PHE A CD1   1 
ATOM   2315 C CD2   . PHE B 2 184 ? 126.621 125.017 82.452  1.00 106.43 ? 184 PHE A CD2   1 
ATOM   2316 C CE1   . PHE B 2 184 ? 127.477 127.380 81.339  1.00 106.43 ? 184 PHE A CE1   1 
ATOM   2317 C CE2   . PHE B 2 184 ? 126.219 125.363 81.182  1.00 106.43 ? 184 PHE A CE2   1 
ATOM   2318 C CZ    . PHE B 2 184 ? 126.648 126.546 80.626  1.00 106.43 ? 184 PHE A CZ    1 
ATOM   2319 N N     . TYR B 2 185 ? 129.011 125.665 87.548  1.00 105.18 ? 185 TYR A N     1 
ATOM   2320 C CA    . TYR B 2 185 ? 128.903 125.254 88.940  1.00 105.18 ? 185 TYR A CA    1 
ATOM   2321 C C     . TYR B 2 185 ? 128.943 126.449 89.879  1.00 105.18 ? 185 TYR A C     1 
ATOM   2322 O O     . TYR B 2 185 ? 128.298 126.424 90.929  1.00 105.18 ? 185 TYR A O     1 
ATOM   2323 C CB    . TYR B 2 185 ? 130.013 124.263 89.287  1.00 105.18 ? 185 TYR A CB    1 
ATOM   2324 C CG    . TYR B 2 185 ? 129.924 122.942 88.552  1.00 105.18 ? 185 TYR A CG    1 
ATOM   2325 C CD1   . TYR B 2 185 ? 128.803 122.612 87.802  1.00 105.18 ? 185 TYR A CD1   1 
ATOM   2326 C CD2   . TYR B 2 185 ? 130.967 122.028 88.604  1.00 105.18 ? 185 TYR A CD2   1 
ATOM   2327 C CE1   . TYR B 2 185 ? 128.723 121.410 87.129  1.00 105.18 ? 185 TYR A CE1   1 
ATOM   2328 C CE2   . TYR B 2 185 ? 130.895 120.824 87.935  1.00 105.18 ? 185 TYR A CE2   1 
ATOM   2329 C CZ    . TYR B 2 185 ? 129.771 120.521 87.199  1.00 105.18 ? 185 TYR A CZ    1 
ATOM   2330 O OH    . TYR B 2 185 ? 129.698 119.321 86.531  1.00 105.18 ? 185 TYR A OH    1 
ATOM   2331 N N     . ALA B 2 186 ? 129.677 127.505 89.524  1.00 102.47 ? 186 ALA A N     1 
ATOM   2332 C CA    . ALA B 2 186 ? 129.617 128.725 90.325  1.00 102.47 ? 186 ALA A CA    1 
ATOM   2333 C C     . ALA B 2 186 ? 128.234 129.362 90.249  1.00 102.47 ? 186 ALA A C     1 
ATOM   2334 O O     . ALA B 2 186 ? 127.694 129.827 91.264  1.00 102.47 ? 186 ALA A O     1 
ATOM   2335 C CB    . ALA B 2 186 ? 130.689 129.709 89.863  1.00 102.47 ? 186 ALA A CB    1 
ATOM   2336 N N     . LEU B 2 187 ? 127.645 129.387 89.052  1.00 101.61 ? 187 LEU A N     1 
ATOM   2337 C CA    . LEU B 2 187 ? 126.291 129.910 88.909  1.00 101.61 ? 187 LEU A CA    1 
ATOM   2338 C C     . LEU B 2 187 ? 125.298 129.071 89.698  1.00 101.61 ? 187 LEU A C     1 
ATOM   2339 O O     . LEU B 2 187 ? 124.371 129.607 90.311  1.00 101.61 ? 187 LEU A O     1 
ATOM   2340 C CB    . LEU B 2 187 ? 125.902 129.963 87.434  1.00 101.61 ? 187 LEU A CB    1 
ATOM   2341 C CG    . LEU B 2 187 ? 124.483 130.438 87.143  1.00 101.61 ? 187 LEU A CG    1 
ATOM   2342 C CD1   . LEU B 2 187 ? 124.275 131.835 87.694  1.00 101.61 ? 187 LEU A CD1   1 
ATOM   2343 C CD2   . LEU B 2 187 ? 124.216 130.410 85.654  1.00 101.61 ? 187 LEU A CD2   1 
ATOM   2344 N N     . PHE B 2 188 ? 125.483 127.751 89.707  1.00 97.00  ? 188 PHE A N     1 
ATOM   2345 C CA    . PHE B 2 188 ? 124.620 126.898 90.515  1.00 97.00  ? 188 PHE A CA    1 
ATOM   2346 C C     . PHE B 2 188 ? 124.839 127.146 92.002  1.00 97.00  ? 188 PHE A C     1 
ATOM   2347 O O     . PHE B 2 188 ? 123.891 127.102 92.789  1.00 97.00  ? 188 PHE A O     1 
ATOM   2348 C CB    . PHE B 2 188 ? 124.860 125.429 90.174  1.00 97.00  ? 188 PHE A CB    1 
ATOM   2349 C CG    . PHE B 2 188 ? 124.509 125.070 88.761  1.00 97.00  ? 188 PHE A CG    1 
ATOM   2350 C CD1   . PHE B 2 188 ? 123.592 125.818 88.049  1.00 97.00  ? 188 PHE A CD1   1 
ATOM   2351 C CD2   . PHE B 2 188 ? 125.097 123.983 88.146  1.00 97.00  ? 188 PHE A CD2   1 
ATOM   2352 C CE1   . PHE B 2 188 ? 123.273 125.489 86.752  1.00 97.00  ? 188 PHE A CE1   1 
ATOM   2353 C CE2   . PHE B 2 188 ? 124.779 123.650 86.849  1.00 97.00  ? 188 PHE A CE2   1 
ATOM   2354 C CZ    . PHE B 2 188 ? 123.866 124.405 86.153  1.00 97.00  ? 188 PHE A CZ    1 
ATOM   2355 N N     . GLY B 2 189 ? 126.077 127.417 92.405  1.00 94.51  ? 189 GLY A N     1 
ATOM   2356 C CA    . GLY B 2 189 ? 126.333 127.722 93.801  1.00 94.51  ? 189 GLY A CA    1 
ATOM   2357 C C     . GLY B 2 189 ? 125.632 128.987 94.253  1.00 94.51  ? 189 GLY A C     1 
ATOM   2358 O O     . GLY B 2 189 ? 125.120 129.057 95.372  1.00 94.51  ? 189 GLY A O     1 
ATOM   2359 N N     . ILE B 2 190 ? 125.598 130.004 93.391  1.00 93.29  ? 190 ILE A N     1 
ATOM   2360 C CA    . ILE B 2 190 ? 124.888 131.224 93.771  1.00 93.29  ? 190 ILE A CA    1 
ATOM   2361 C C     . ILE B 2 190 ? 123.379 131.025 93.660  1.00 93.29  ? 190 ILE A C     1 
ATOM   2362 O O     . ILE B 2 190 ? 122.604 131.627 94.418  1.00 93.29  ? 190 ILE A O     1 
ATOM   2363 C CB    . ILE B 2 190 ? 125.378 132.426 92.940  1.00 93.29  ? 190 ILE A CB    1 
ATOM   2364 C CG1   . ILE B 2 190 ? 125.146 133.726 93.709  1.00 93.29  ? 190 ILE A CG1   1 
ATOM   2365 C CG2   . ILE B 2 190 ? 124.680 132.499 91.597  1.00 93.29  ? 190 ILE A CG2   1 
ATOM   2366 C CD1   . ILE B 2 190 ? 125.861 134.915 93.119  1.00 93.29  ? 190 ILE A CD1   1 
ATOM   2367 N N     . GLY B 2 191 ? 122.934 130.161 92.746  1.00 89.03  ? 191 GLY A N     1 
ATOM   2368 C CA    . GLY B 2 191 ? 121.517 129.874 92.645  1.00 89.03  ? 191 GLY A CA    1 
ATOM   2369 C C     . GLY B 2 191 ? 120.998 129.072 93.816  1.00 89.03  ? 191 GLY A C     1 
ATOM   2370 O O     . GLY B 2 191 ? 119.824 129.175 94.166  1.00 89.03  ? 191 GLY A O     1 
ATOM   2371 N N     . ALA B 2 192 ? 121.862 128.276 94.443  1.00 86.00  ? 192 ALA A N     1 
ATOM   2372 C CA    . ALA B 2 192 ? 121.462 127.567 95.652  1.00 86.00  ? 192 ALA A CA    1 
ATOM   2373 C C     . ALA B 2 192 ? 121.171 128.542 96.782  1.00 86.00  ? 192 ALA A C     1 
ATOM   2374 O O     . ALA B 2 192 ? 120.224 128.351 97.549  1.00 86.00  ? 192 ALA A O     1 
ATOM   2375 C CB    . ALA B 2 192 ? 122.545 126.572 96.063  1.00 86.00  ? 192 ALA A CB    1 
ATOM   2376 N N     . ASN B 2 193 ? 121.954 129.616 96.881  1.00 87.38  ? 193 ASN A N     1 
ATOM   2377 C CA    . ASN B 2 193 ? 121.686 130.624 97.900  1.00 87.38  ? 193 ASN A CA    1 
ATOM   2378 C C     . ASN B 2 193 ? 120.455 131.449 97.548  1.00 87.38  ? 193 ASN A C     1 
ATOM   2379 O O     . ASN B 2 193 ? 119.662 131.801 98.431  1.00 87.38  ? 193 ASN A O     1 
ATOM   2380 C CB    . ASN B 2 193 ? 122.907 131.521 98.077  1.00 87.38  ? 193 ASN A CB    1 
ATOM   2381 C CG    . ASN B 2 193 ? 124.171 130.733 98.332  1.00 87.38  ? 193 ASN A CG    1 
ATOM   2382 O OD1   . ASN B 2 193 ? 124.158 129.734 99.048  1.00 87.38  ? 193 ASN A OD1   1 
ATOM   2383 N ND2   . ASN B 2 193 ? 125.273 131.175 97.741  1.00 87.38  ? 193 ASN A ND2   1 
ATOM   2384 N N     . ILE B 2 194 ? 120.274 131.769 96.266  1.00 82.16  ? 194 ILE A N     1 
ATOM   2385 C CA    . ILE B 2 194 ? 119.056 132.464 95.860  1.00 82.16  ? 194 ILE A CA    1 
ATOM   2386 C C     . ILE B 2 194 ? 117.830 131.610 96.168  1.00 82.16  ? 194 ILE A C     1 
ATOM   2387 O O     . ILE B 2 194 ? 116.789 132.119 96.600  1.00 82.16  ? 194 ILE A O     1 
ATOM   2388 C CB    . ILE B 2 194 ? 119.127 132.847 94.372  1.00 82.16  ? 194 ILE A CB    1 
ATOM   2389 C CG1   . ILE B 2 194 ? 120.181 133.932 94.156  1.00 82.16  ? 194 ILE A CG1   1 
ATOM   2390 C CG2   . ILE B 2 194 ? 117.780 133.331 93.879  1.00 82.16  ? 194 ILE A CG2   1 
ATOM   2391 C CD1   . ILE B 2 194 ? 120.292 134.394 92.722  1.00 82.16  ? 194 ILE A CD1   1 
ATOM   2392 N N     . SER B 2 195 ? 117.943 130.295 95.984  1.00 79.32  ? 195 SER A N     1 
ATOM   2393 C CA    . SER B 2 195 ? 116.825 129.413 96.289  1.00 79.32  ? 195 SER A CA    1 
ATOM   2394 C C     . SER B 2 195 ? 116.647 129.240 97.786  1.00 79.32  ? 195 SER A C     1 
ATOM   2395 O O     . SER B 2 195 ? 115.530 129.001 98.243  1.00 79.32  ? 195 SER A O     1 
ATOM   2396 C CB    . SER B 2 195 ? 117.021 128.054 95.627  1.00 79.32  ? 195 SER A CB    1 
ATOM   2397 O OG    . SER B 2 195 ? 118.117 127.372 96.203  1.00 79.32  ? 195 SER A OG    1 
ATOM   2398 N N     . LEU B 2 196 ? 117.722 129.359 98.564  1.00 79.19  ? 196 LEU A N     1 
ATOM   2399 C CA    . LEU B 2 196 ? 117.562 129.435 100.011 1.00 79.19  ? 196 LEU A CA    1 
ATOM   2400 C C     . LEU B 2 196 ? 116.742 130.656 100.396 1.00 79.19  ? 196 LEU A C     1 
ATOM   2401 O O     . LEU B 2 196 ? 115.818 130.560 101.208 1.00 79.19  ? 196 LEU A O     1 
ATOM   2402 C CB    . LEU B 2 196 ? 118.925 129.465 100.698 1.00 79.19  ? 196 LEU A CB    1 
ATOM   2403 C CG    . LEU B 2 196 ? 119.443 128.124 101.210 1.00 79.19  ? 196 LEU A CG    1 
ATOM   2404 C CD1   . LEU B 2 196 ? 120.905 128.229 101.590 1.00 79.19  ? 196 LEU A CD1   1 
ATOM   2405 C CD2   . LEU B 2 196 ? 118.618 127.668 102.393 1.00 79.19  ? 196 LEU A CD2   1 
ATOM   2406 N N     . LEU B 2 197 ? 117.055 131.808 99.803  1.00 74.70  ? 197 LEU A N     1 
ATOM   2407 C CA    . LEU B 2 197 ? 116.263 133.013 100.040 1.00 74.70  ? 197 LEU A CA    1 
ATOM   2408 C C     . LEU B 2 197 ? 114.799 132.790 99.678  1.00 74.70  ? 197 LEU A C     1 
ATOM   2409 O O     . LEU B 2 197 ? 113.893 133.098 100.464 1.00 74.70  ? 197 LEU A O     1 
ATOM   2410 C CB    . LEU B 2 197 ? 116.828 134.178 99.231  1.00 74.70  ? 197 LEU A CB    1 
ATOM   2411 C CG    . LEU B 2 197 ? 118.211 134.692 99.600  1.00 74.70  ? 197 LEU A CG    1 
ATOM   2412 C CD1   . LEU B 2 197 ? 118.571 135.889 98.749  1.00 74.70  ? 197 LEU A CD1   1 
ATOM   2413 C CD2   . LEU B 2 197 ? 118.233 135.053 101.055 1.00 74.70  ? 197 LEU A CD2   1 
ATOM   2414 N N     . ALA B 2 198 ? 114.553 132.262 98.478  1.00 73.59  ? 198 ALA A N     1 
ATOM   2415 C CA    . ALA B 2 198 ? 113.186 132.103 97.996  1.00 73.59  ? 198 ALA A CA    1 
ATOM   2416 C C     . ALA B 2 198 ? 112.412 131.095 98.832  1.00 73.59  ? 198 ALA A C     1 
ATOM   2417 O O     . ALA B 2 198 ? 111.257 131.338 99.192  1.00 73.59  ? 198 ALA A O     1 
ATOM   2418 C CB    . ALA B 2 198 ? 113.192 131.686 96.528  1.00 73.59  ? 198 ALA A CB    1 
ATOM   2419 N N     . SER B 2 199 ? 113.025 129.955 99.150  1.00 75.20  ? 199 SER A N     1 
ATOM   2420 C CA    . SER B 2 199 ? 112.349 128.950 99.957  1.00 75.20  ? 199 SER A CA    1 
ATOM   2421 C C     . SER B 2 199 ? 112.120 129.445 101.374 1.00 75.20  ? 199 SER A C     1 
ATOM   2422 O O     . SER B 2 199 ? 111.098 129.125 101.984 1.00 75.20  ? 199 SER A O     1 
ATOM   2423 C CB    . SER B 2 199 ? 113.156 127.655 99.966  1.00 75.20  ? 199 SER A CB    1 
ATOM   2424 O OG    . SER B 2 199 ? 114.530 127.919 100.171 1.00 75.20  ? 199 SER A OG    1 
ATOM   2425 N N     . GLY B 2 200 ? 113.042 130.242 101.911 1.00 76.45  ? 200 GLY A N     1 
ATOM   2426 C CA    . GLY B 2 200 ? 112.817 130.813 103.225 1.00 76.45  ? 200 GLY A CA    1 
ATOM   2427 C C     . GLY B 2 200 ? 111.636 131.758 103.239 1.00 76.45  ? 200 GLY A C     1 
ATOM   2428 O O     . GLY B 2 200 ? 110.768 131.673 104.110 1.00 76.45  ? 200 GLY A O     1 
ATOM   2429 N N     . ARG B 2 201 ? 111.587 132.674 102.270 1.00 78.20  ? 201 ARG A N     1 
ATOM   2430 C CA    . ARG B 2 201 ? 110.448 133.580 102.181 1.00 78.20  ? 201 ARG A CA    1 
ATOM   2431 C C     . ARG B 2 201 ? 109.150 132.815 101.961 1.00 78.20  ? 201 ARG A C     1 
ATOM   2432 O O     . ARG B 2 201 ? 108.111 133.164 102.530 1.00 78.20  ? 201 ARG A O     1 
ATOM   2433 C CB    . ARG B 2 201 ? 110.665 134.593 101.061 1.00 78.20  ? 201 ARG A CB    1 
ATOM   2434 C CG    . ARG B 2 201 ? 111.341 135.870 101.507 1.00 78.20  ? 201 ARG A CG    1 
ATOM   2435 C CD    . ARG B 2 201 ? 110.492 136.608 102.522 1.00 78.20  ? 201 ARG A CD    1 
ATOM   2436 N NE    . ARG B 2 201 ? 110.976 136.396 103.881 1.00 78.20  ? 201 ARG A NE    1 
ATOM   2437 C CZ    . ARG B 2 201 ? 110.391 136.886 104.966 1.00 78.20  ? 201 ARG A CZ    1 
ATOM   2438 N NH1   . ARG B 2 201 ? 109.292 137.617 104.854 1.00 78.20  ? 201 ARG A NH1   1 
ATOM   2439 N NH2   . ARG B 2 201 ? 110.903 136.642 106.164 1.00 78.20  ? 201 ARG A NH2   1 
ATOM   2440 N N     . ALA B 2 202 ? 109.194 131.754 101.155 1.00 75.43  ? 202 ALA A N     1 
ATOM   2441 C CA    . ALA B 2 202 ? 107.983 131.001 100.861 1.00 75.43  ? 202 ALA A CA    1 
ATOM   2442 C C     . ALA B 2 202 ? 107.496 130.241 102.084 1.00 75.43  ? 202 ALA A C     1 
ATOM   2443 O O     . ALA B 2 202 ? 106.291 130.177 102.341 1.00 75.43  ? 202 ALA A O     1 
ATOM   2444 C CB    . ALA B 2 202 ? 108.232 130.044 99.699  1.00 75.43  ? 202 ALA A CB    1 
ATOM   2445 N N     . ILE B 2 203 ? 108.415 129.657 102.852 1.00 74.90  ? 203 ILE A N     1 
ATOM   2446 C CA    . ILE B 2 203 ? 108.020 128.960 104.068 1.00 74.90  ? 203 ILE A CA    1 
ATOM   2447 C C     . ILE B 2 203 ? 107.491 129.949 105.095 1.00 74.90  ? 203 ILE A C     1 
ATOM   2448 O O     . ILE B 2 203 ? 106.499 129.679 105.782 1.00 74.90  ? 203 ILE A O     1 
ATOM   2449 C CB    . ILE B 2 203 ? 109.197 128.139 104.617 1.00 74.90  ? 203 ILE A CB    1 
ATOM   2450 C CG1   . ILE B 2 203 ? 109.547 127.012 103.653 1.00 74.90  ? 203 ILE A CG1   1 
ATOM   2451 C CG2   . ILE B 2 203 ? 108.851 127.554 105.964 1.00 74.90  ? 203 ILE A CG2   1 
ATOM   2452 C CD1   . ILE B 2 203 ? 110.894 126.416 103.903 1.00 74.90  ? 203 ILE A CD1   1 
ATOM   2453 N N     . VAL B 2 204 ? 108.124 131.120 105.200 1.00 77.48  ? 204 VAL A N     1 
ATOM   2454 C CA    . VAL B 2 204 ? 107.641 132.146 106.117 1.00 77.48  ? 204 VAL A CA    1 
ATOM   2455 C C     . VAL B 2 204 ? 106.230 132.573 105.742 1.00 77.48  ? 204 VAL A C     1 
ATOM   2456 O O     . VAL B 2 204 ? 105.368 132.739 106.609 1.00 77.48  ? 204 VAL A O     1 
ATOM   2457 C CB    . VAL B 2 204 ? 108.610 133.340 106.139 1.00 77.48  ? 204 VAL A CB    1 
ATOM   2458 C CG1   . VAL B 2 204 ? 107.930 134.569 106.708 1.00 77.48  ? 204 VAL A CG1   1 
ATOM   2459 C CG2   . VAL B 2 204 ? 109.838 132.998 106.946 1.00 77.48  ? 204 VAL A CG2   1 
ATOM   2460 N N     . TRP B 2 205 ? 105.968 132.746 104.446 1.00 78.11  ? 205 TRP A N     1 
ATOM   2461 C CA    . TRP B 2 205 ? 104.637 133.149 104.004 1.00 78.11  ? 205 TRP A CA    1 
ATOM   2462 C C     . TRP B 2 205 ? 103.613 132.050 104.263 1.00 78.11  ? 205 TRP A C     1 
ATOM   2463 O O     . TRP B 2 205 ? 102.540 132.304 104.824 1.00 78.11  ? 205 TRP A O     1 
ATOM   2464 C CB    . TRP B 2 205 ? 104.677 133.518 102.522 1.00 78.11  ? 205 TRP A CB    1 
ATOM   2465 C CG    . TRP B 2 205 ? 103.336 133.625 101.879 1.00 78.11  ? 205 TRP A CG    1 
ATOM   2466 C CD1   . TRP B 2 205 ? 102.474 134.675 101.955 1.00 78.11  ? 205 TRP A CD1   1 
ATOM   2467 C CD2   . TRP B 2 205 ? 102.706 132.650 101.044 1.00 78.11  ? 205 TRP A CD2   1 
ATOM   2468 N NE1   . TRP B 2 205 ? 101.342 134.413 101.226 1.00 78.11  ? 205 TRP A NE1   1 
ATOM   2469 C CE2   . TRP B 2 205 ? 101.461 133.174 100.656 1.00 78.11  ? 205 TRP A CE2   1 
ATOM   2470 C CE3   . TRP B 2 205 ? 103.074 131.382 100.589 1.00 78.11  ? 205 TRP A CE3   1 
ATOM   2471 C CZ2   . TRP B 2 205 ? 100.584 132.477 99.835  1.00 78.11  ? 205 TRP A CZ2   1 
ATOM   2472 C CZ3   . TRP B 2 205 ? 102.202 130.692 99.778  1.00 78.11  ? 205 TRP A CZ3   1 
ATOM   2473 C CH2   . TRP B 2 205 ? 100.971 131.239 99.409  1.00 78.11  ? 205 TRP A CH2   1 
ATOM   2474 N N     . ALA B 2 206 ? 103.929 130.819 103.859 1.00 79.78  ? 206 ALA A N     1 
ATOM   2475 C CA    . ALA B 2 206 ? 103.002 129.711 104.054 1.00 79.78  ? 206 ALA A CA    1 
ATOM   2476 C C     . ALA B 2 206 ? 102.739 129.449 105.528 1.00 79.78  ? 206 ALA A C     1 
ATOM   2477 O O     . ALA B 2 206 ? 101.700 128.882 105.879 1.00 79.78  ? 206 ALA A O     1 
ATOM   2478 C CB    . ALA B 2 206 ? 103.541 128.453 103.379 1.00 79.78  ? 206 ALA A CB    1 
ATOM   2479 N N     . SER B 2 207 ? 103.657 129.852 106.406 1.00 79.98  ? 207 SER A N     1 
ATOM   2480 C CA    . SER B 2 207 ? 103.436 129.646 107.830 1.00 79.98  ? 207 SER A CA    1 
ATOM   2481 C C     . SER B 2 207 ? 102.669 130.807 108.452 1.00 79.98  ? 207 SER A C     1 
ATOM   2482 O O     . SER B 2 207 ? 101.728 130.588 109.222 1.00 79.98  ? 207 SER A O     1 
ATOM   2483 C CB    . SER B 2 207 ? 104.775 129.446 108.529 1.00 79.98  ? 207 SER A CB    1 
ATOM   2484 O OG    . SER B 2 207 ? 105.427 128.300 108.015 1.00 79.98  ? 207 SER A OG    1 
ATOM   2485 N N     . LYS B 2 208 ? 103.044 132.044 108.127 1.00 87.15  ? 208 LYS A N     1 
ATOM   2486 C CA    . LYS B 2 208 ? 102.324 133.227 108.578 1.00 87.15  ? 208 LYS A CA    1 
ATOM   2487 C C     . LYS B 2 208 ? 100.972 133.389 107.905 1.00 87.15  ? 208 LYS A C     1 
ATOM   2488 O O     . LYS B 2 208 ? 100.268 134.361 108.195 1.00 87.15  ? 208 LYS A O     1 
ATOM   2489 C CB    . LYS B 2 208 ? 103.162 134.481 108.332 1.00 87.15  ? 208 LYS A CB    1 
ATOM   2490 C CG    . LYS B 2 208 ? 104.344 134.624 109.259 1.00 87.15  ? 208 LYS A CG    1 
ATOM   2491 C CD    . LYS B 2 208 ? 105.150 135.863 108.927 1.00 87.15  ? 208 LYS A CD    1 
ATOM   2492 C CE    . LYS B 2 208 ? 104.425 137.124 109.358 1.00 87.15  ? 208 LYS A CE    1 
ATOM   2493 N NZ    . LYS B 2 208 ? 104.377 137.249 110.840 1.00 87.15  ? 208 LYS A NZ    1 
ATOM   2494 N N     . LEU B 2 209 ? 100.591 132.468 107.024 1.00 95.25  ? 209 LEU A N     1 
ATOM   2495 C CA    . LEU B 2 209 ? 99.249  132.484 106.446 1.00 95.25  ? 209 LEU A CA    1 
ATOM   2496 C C     . LEU B 2 209 ? 98.266  131.754 107.354 1.00 95.25  ? 209 LEU A C     1 
ATOM   2497 O O     . LEU B 2 209 ? 97.303  131.115 106.925 1.00 95.25  ? 209 LEU A O     1 
ATOM   2498 C CB    . LEU B 2 209 ? 99.278  131.902 105.033 1.00 95.25  ? 209 LEU A CB    1 
ATOM   2499 C CG    . LEU B 2 209 ? 98.117  132.203 104.071 1.00 95.25  ? 209 LEU A CG    1 
ATOM   2500 C CD1   . LEU B 2 209 ? 98.663  132.444 102.687 1.00 95.25  ? 209 LEU A CD1   1 
ATOM   2501 C CD2   . LEU B 2 209 ? 97.097  131.081 103.995 1.00 95.25  ? 209 LEU A CD2   1 
ATOM   2502 N N     . ARG B 2 210 ? 98.514  131.857 108.660 1.00 106.77 ? 210 ARG A N     1 
ATOM   2503 C CA    . ARG B 2 210 ? 97.641  131.300 109.683 1.00 106.77 ? 210 ARG A CA    1 
ATOM   2504 C C     . ARG B 2 210 ? 96.345  132.100 109.678 1.00 106.77 ? 210 ARG A C     1 
ATOM   2505 O O     . ARG B 2 210 ? 96.081  132.897 110.584 1.00 106.77 ? 210 ARG A O     1 
ATOM   2506 C CB    . ARG B 2 210 ? 98.338  131.367 111.047 1.00 106.77 ? 210 ARG A CB    1 
ATOM   2507 C CG    . ARG B 2 210 ? 97.591  130.769 112.223 1.00 106.77 ? 210 ARG A CG    1 
ATOM   2508 C CD    . ARG B 2 210 ? 98.394  130.992 113.498 1.00 106.77 ? 210 ARG A CD    1 
ATOM   2509 N NE    . ARG B 2 210 ? 97.673  130.597 114.704 1.00 106.77 ? 210 ARG A NE    1 
ATOM   2510 C CZ    . ARG B 2 210 ? 97.743  129.394 115.263 1.00 106.77 ? 210 ARG A CZ    1 
ATOM   2511 N NH1   . ARG B 2 210 ? 98.515  128.457 114.731 1.00 106.77 ? 210 ARG A NH1   1 
ATOM   2512 N NH2   . ARG B 2 210 ? 97.049  129.129 116.361 1.00 106.77 ? 210 ARG A NH2   1 
ATOM   2513 N N     . ALA B 2 211 ? 95.543  131.889 108.641 1.00 117.43 ? 211 ALA A N     1 
ATOM   2514 C CA    . ALA B 2 211 ? 94.335  132.635 108.338 1.00 117.43 ? 211 ALA A CA    1 
ATOM   2515 C C     . ALA B 2 211 ? 93.117  131.740 108.542 1.00 117.43 ? 211 ALA A C     1 
ATOM   2516 O O     . ALA B 2 211 ? 93.218  130.635 109.090 1.00 117.43 ? 211 ALA A O     1 
ATOM   2517 C CB    . ALA B 2 211 ? 94.402  133.191 106.914 1.00 117.43 ? 211 ALA A CB    1 
ATOM   2518 N N     . SER B 2 212 ? 91.956  132.230 108.100 1.00 128.26 ? 212 SER A N     1 
ATOM   2519 C CA    . SER B 2 212 ? 90.673  131.555 108.291 1.00 128.26 ? 212 SER A CA    1 
ATOM   2520 C C     . SER B 2 212 ? 90.387  131.381 109.786 1.00 128.26 ? 212 SER A C     1 
ATOM   2521 O O     . SER B 2 212 ? 90.338  130.276 110.329 1.00 128.26 ? 212 SER A O     1 
ATOM   2522 C CB    . SER B 2 212 ? 90.638  130.214 107.547 1.00 128.26 ? 212 SER A CB    1 
ATOM   2523 O OG    . SER B 2 212 ? 90.751  130.409 106.147 1.00 128.26 ? 212 SER A OG    1 
ATOM   2524 N N     . VAL B 2 213 ? 90.212  132.535 110.433 1.00 133.36 ? 213 VAL A N     1 
ATOM   2525 C CA    . VAL B 2 213 ? 90.048  132.649 111.880 1.00 133.36 ? 213 VAL A CA    1 
ATOM   2526 C C     . VAL B 2 213 ? 88.949  131.722 112.390 1.00 133.36 ? 213 VAL A C     1 
ATOM   2527 O O     . VAL B 2 213 ? 88.930  131.362 113.572 1.00 133.36 ? 213 VAL A O     1 
ATOM   2528 C CB    . VAL B 2 213 ? 89.766  134.113 112.274 1.00 133.36 ? 213 VAL A CB    1 
ATOM   2529 C CG1   . VAL B 2 213 ? 88.398  134.550 111.771 1.00 133.36 ? 213 VAL A CG1   1 
ATOM   2530 C CG2   . VAL B 2 213 ? 89.895  134.307 113.781 1.00 133.36 ? 213 VAL A CG2   1 
ATOM   2531 N N     . SER B 2 214 ? 88.034  131.323 111.507 1.00 135.36 ? 214 SER A N     1 
ATOM   2532 C CA    . SER B 2 214 ? 87.034  130.331 111.875 1.00 135.36 ? 214 SER A CA    1 
ATOM   2533 C C     . SER B 2 214 ? 87.713  129.042 112.320 1.00 135.36 ? 214 SER A C     1 
ATOM   2534 O O     . SER B 2 214 ? 88.415  128.387 111.545 1.00 135.36 ? 214 SER A O     1 
ATOM   2535 C CB    . SER B 2 214 ? 86.095  130.058 110.699 1.00 135.36 ? 214 SER A CB    1 
ATOM   2536 O OG    . SER B 2 214 ? 85.328  131.205 110.382 1.00 135.36 ? 214 SER A OG    1 
ATOM   2537 N N     . GLU B 2 215 ? 87.494  128.677 113.579 1.00 135.20 ? 215 GLU A N     1 
ATOM   2538 C CA    . GLU B 2 215 ? 88.176  127.540 114.171 1.00 135.20 ? 215 GLU A CA    1 
ATOM   2539 C C     . GLU B 2 215 ? 87.572  126.227 113.676 1.00 135.20 ? 215 GLU A C     1 
ATOM   2540 O O     . GLU B 2 215 ? 86.659  126.198 112.846 1.00 135.20 ? 215 GLU A O     1 
ATOM   2541 C CB    . GLU B 2 215 ? 88.127  127.613 115.698 1.00 135.20 ? 215 GLU A CB    1 
ATOM   2542 C CG    . GLU B 2 215 ? 88.670  128.909 116.303 1.00 135.20 ? 215 GLU A CG    1 
ATOM   2543 C CD    . GLU B 2 215 ? 87.699  130.073 116.218 1.00 135.20 ? 215 GLU A CD    1 
ATOM   2544 O OE1   . GLU B 2 215 ? 86.593  129.894 115.667 1.00 135.20 ? 215 GLU A OE1   1 
ATOM   2545 O OE2   . GLU B 2 215 ? 88.045  131.169 116.707 1.00 135.20 ? 215 GLU A OE2   1 
ATOM   2546 N N     . GLY B 2 216 ? 88.102  125.125 114.202 1.00 127.12 ? 216 GLY A N     1 
ATOM   2547 C CA    . GLY B 2 216 ? 87.741  123.804 113.746 1.00 127.12 ? 216 GLY A CA    1 
ATOM   2548 C C     . GLY B 2 216 ? 88.598  123.270 112.621 1.00 127.12 ? 216 GLY A C     1 
ATOM   2549 O O     . GLY B 2 216 ? 88.553  122.064 112.348 1.00 127.12 ? 216 GLY A O     1 
ATOM   2550 N N     . VAL B 2 217 ? 89.372  124.124 111.960 1.00 115.98 ? 217 VAL A N     1 
ATOM   2551 C CA    . VAL B 2 217 ? 90.291  123.707 110.910 1.00 115.98 ? 217 VAL A CA    1 
ATOM   2552 C C     . VAL B 2 217 ? 91.698  123.671 111.483 1.00 115.98 ? 217 VAL A C     1 
ATOM   2553 O O     . VAL B 2 217 ? 92.018  124.364 112.456 1.00 115.98 ? 217 VAL A O     1 
ATOM   2554 C CB    . VAL B 2 217 ? 90.215  124.639 109.683 1.00 115.98 ? 217 VAL A CB    1 
ATOM   2555 C CG1   . VAL B 2 217 ? 88.830  124.584 109.060 1.00 115.98 ? 217 VAL A CG1   1 
ATOM   2556 C CG2   . VAL B 2 217 ? 90.577  126.063 110.073 1.00 115.98 ? 217 VAL A CG2   1 
ATOM   2557 N N     . ASP B 2 218 ? 92.544  122.848 110.880 1.00 98.41  ? 218 ASP A N     1 
ATOM   2558 C CA    . ASP B 2 218 ? 93.927  122.733 111.317 1.00 98.41  ? 218 ASP A CA    1 
ATOM   2559 C C     . ASP B 2 218 ? 94.727  123.922 110.802 1.00 98.41  ? 218 ASP A C     1 
ATOM   2560 O O     . ASP B 2 218 ? 94.863  124.080 109.585 1.00 98.41  ? 218 ASP A O     1 
ATOM   2561 C CB    . ASP B 2 218 ? 94.537  121.433 110.811 1.00 98.41  ? 218 ASP A CB    1 
ATOM   2562 C CG    . ASP B 2 218 ? 95.763  121.020 111.595 1.00 98.41  ? 218 ASP A CG    1 
ATOM   2563 O OD1   . ASP B 2 218 ? 96.236  119.882 111.400 1.00 98.41  ? 218 ASP A OD1   1 
ATOM   2564 O OD2   . ASP B 2 218 ? 96.253  121.830 112.408 1.00 98.41  ? 218 ASP A OD2   1 
ATOM   2565 N N     . PRO B 2 219 ? 95.257  124.779 111.676 1.00 90.60  ? 219 PRO A N     1 
ATOM   2566 C CA    . PRO B 2 219 ? 96.081  125.893 111.185 1.00 90.60  ? 219 PRO A CA    1 
ATOM   2567 C C     . PRO B 2 219 ? 97.324  125.430 110.456 1.00 90.60  ? 219 PRO A C     1 
ATOM   2568 O O     . PRO B 2 219 ? 97.768  126.098 109.516 1.00 90.60  ? 219 PRO A O     1 
ATOM   2569 C CB    . PRO B 2 219 ? 96.427  126.666 112.465 1.00 90.60  ? 219 PRO A CB    1 
ATOM   2570 C CG    . PRO B 2 219 ? 96.276  125.671 113.562 1.00 90.60  ? 219 PRO A CG    1 
ATOM   2571 C CD    . PRO B 2 219 ? 95.158  124.766 113.144 1.00 90.60  ? 219 PRO A CD    1 
ATOM   2572 N N     . TRP B 2 220 ? 97.899  124.297 110.859 1.00 81.21  ? 220 TRP A N     1 
ATOM   2573 C CA    . TRP B 2 220 ? 99.045  123.745 110.153 1.00 81.21  ? 220 TRP A CA    1 
ATOM   2574 C C     . TRP B 2 220 ? 98.639  122.968 108.913 1.00 81.21  ? 220 TRP A C     1 
ATOM   2575 O O     . TRP B 2 220 ? 99.467  122.785 108.019 1.00 81.21  ? 220 TRP A O     1 
ATOM   2576 C CB    . TRP B 2 220 ? 99.857  122.847 111.087 1.00 81.21  ? 220 TRP A CB    1 
ATOM   2577 C CG    . TRP B 2 220 ? 100.929 122.058 110.402 1.00 81.21  ? 220 TRP A CG    1 
ATOM   2578 C CD1   . TRP B 2 220 ? 100.993 120.706 110.280 1.00 81.21  ? 220 TRP A CD1   1 
ATOM   2579 C CD2   . TRP B 2 220 ? 102.089 122.574 109.744 1.00 81.21  ? 220 TRP A CD2   1 
ATOM   2580 N NE1   . TRP B 2 220 ? 102.120 120.344 109.589 1.00 81.21  ? 220 TRP A NE1   1 
ATOM   2581 C CE2   . TRP B 2 220 ? 102.811 121.475 109.249 1.00 81.21  ? 220 TRP A CE2   1 
ATOM   2582 C CE3   . TRP B 2 220 ? 102.589 123.860 109.526 1.00 81.21  ? 220 TRP A CE3   1 
ATOM   2583 C CZ2   . TRP B 2 220 ? 104.002 121.620 108.551 1.00 81.21  ? 220 TRP A CZ2   1 
ATOM   2584 C CZ3   . TRP B 2 220 ? 103.769 124.002 108.833 1.00 81.21  ? 220 TRP A CZ3   1 
ATOM   2585 C CH2   . TRP B 2 220 ? 104.464 122.889 108.354 1.00 81.21  ? 220 TRP A CH2   1 
ATOM   2586 N N     . GLY B 2 221 ? 97.390  122.514 108.829 1.00 84.27  ? 221 GLY A N     1 
ATOM   2587 C CA    . GLY B 2 221 ? 96.942  121.850 107.617 1.00 84.27  ? 221 GLY A CA    1 
ATOM   2588 C C     . GLY B 2 221 ? 97.006  122.755 106.403 1.00 84.27  ? 221 GLY A C     1 
ATOM   2589 O O     . GLY B 2 221 ? 97.453  122.343 105.332 1.00 84.27  ? 221 GLY A O     1 
ATOM   2590 N N     . ILE B 2 222 ? 96.579  124.009 106.560 1.00 83.29  ? 222 ILE A N     1 
ATOM   2591 C CA    . ILE B 2 222 ? 96.614  124.957 105.450 1.00 83.29  ? 222 ILE A CA    1 
ATOM   2592 C C     . ILE B 2 222 ? 98.052  125.280 105.069 1.00 83.29  ? 222 ILE A C     1 
ATOM   2593 O O     . ILE B 2 222 ? 98.397  125.358 103.883 1.00 83.29  ? 222 ILE A O     1 
ATOM   2594 C CB    . ILE B 2 222 ? 95.829  126.228 105.814 1.00 83.29  ? 222 ILE A CB    1 
ATOM   2595 C CG1   . ILE B 2 222 ? 94.389  125.878 106.186 1.00 83.29  ? 222 ILE A CG1   1 
ATOM   2596 C CG2   . ILE B 2 222 ? 95.852  127.213 104.662 1.00 83.29  ? 222 ILE A CG2   1 
ATOM   2597 C CD1   . ILE B 2 222 ? 93.619  125.218 105.070 1.00 83.29  ? 222 ILE A CD1   1 
ATOM   2598 N N     . SER B 2 223 ? 98.912  125.483 106.068 1.00 80.05  ? 223 SER A N     1 
ATOM   2599 C CA    . SER B 2 223 ? 100.316 125.761 105.791 1.00 80.05  ? 223 SER A CA    1 
ATOM   2600 C C     . SER B 2 223 ? 100.978 124.589 105.083 1.00 80.05  ? 223 SER A C     1 
ATOM   2601 O O     . SER B 2 223 ? 101.786 124.782 104.170 1.00 80.05  ? 223 SER A O     1 
ATOM   2602 C CB    . SER B 2 223 ? 101.052 126.082 107.089 1.00 80.05  ? 223 SER A CB    1 
ATOM   2603 O OG    . SER B 2 223 ? 100.342 127.040 107.853 1.00 80.05  ? 223 SER A OG    1 
ATOM   2604 N N     . LEU B 2 224 ? 100.640 123.363 105.482 1.00 79.90  ? 224 LEU A N     1 
ATOM   2605 C CA    . LEU B 2 224 ? 101.209 122.189 104.835 1.00 79.90  ? 224 LEU A CA    1 
ATOM   2606 C C     . LEU B 2 224 ? 100.699 122.051 103.411 1.00 79.90  ? 224 LEU A C     1 
ATOM   2607 O O     . LEU B 2 224 ? 101.460 121.687 102.509 1.00 79.90  ? 224 LEU A O     1 
ATOM   2608 C CB    . LEU B 2 224 ? 100.883 120.935 105.644 1.00 79.90  ? 224 LEU A CB    1 
ATOM   2609 C CG    . LEU B 2 224 ? 101.553 119.643 105.186 1.00 79.90  ? 224 LEU A CG    1 
ATOM   2610 C CD1   . LEU B 2 224 ? 103.049 119.728 105.382 1.00 79.90  ? 224 LEU A CD1   1 
ATOM   2611 C CD2   . LEU B 2 224 ? 100.982 118.461 105.938 1.00 79.90  ? 224 LEU A CD2   1 
ATOM   2612 N N     . ARG B 2 225 ? 99.415  122.334 103.189 1.00 81.97  ? 225 ARG A N     1 
ATOM   2613 C CA    . ARG B 2 225 ? 98.887  122.314 101.832 1.00 81.97  ? 225 ARG A CA    1 
ATOM   2614 C C     . ARG B 2 225 ? 99.609  123.322 100.953 1.00 81.97  ? 225 ARG A C     1 
ATOM   2615 O O     . ARG B 2 225 ? 99.973  123.011 99.817  1.00 81.97  ? 225 ARG A O     1 
ATOM   2616 C CB    . ARG B 2 225 ? 97.386  122.591 101.841 1.00 81.97  ? 225 ARG A CB    1 
ATOM   2617 C CG    . ARG B 2 225 ? 96.539  121.382 102.171 1.00 81.97  ? 225 ARG A CG    1 
ATOM   2618 C CD    . ARG B 2 225 ? 95.084  121.765 102.350 1.00 81.97  ? 225 ARG A CD    1 
ATOM   2619 N NE    . ARG B 2 225 ? 94.323  120.708 103.008 1.00 81.97  ? 225 ARG A NE    1 
ATOM   2620 C CZ    . ARG B 2 225 ? 93.676  119.744 102.363 1.00 81.97  ? 225 ARG A CZ    1 
ATOM   2621 N NH1   . ARG B 2 225 ? 93.694  119.704 101.039 1.00 81.97  ? 225 ARG A NH1   1 
ATOM   2622 N NH2   . ARG B 2 225 ? 93.008  118.822 103.041 1.00 81.97  ? 225 ARG A NH2   1 
ATOM   2623 N N     . LEU B 2 226 ? 99.854  124.526 101.472 1.00 79.55  ? 226 LEU A N     1 
ATOM   2624 C CA    . LEU B 2 226 ? 100.555 125.537 100.685 1.00 79.55  ? 226 LEU A CA    1 
ATOM   2625 C C     . LEU B 2 226 ? 101.997 125.132 100.410 1.00 79.55  ? 226 LEU A C     1 
ATOM   2626 O O     . LEU B 2 226 ? 102.486 125.281 99.283  1.00 79.55  ? 226 LEU A O     1 
ATOM   2627 C CB    . LEU B 2 226 ? 100.511 126.882 101.402 1.00 79.55  ? 226 LEU A CB    1 
ATOM   2628 C CG    . LEU B 2 226 ? 99.244  127.696 101.175 1.00 79.55  ? 226 LEU A CG    1 
ATOM   2629 C CD1   . LEU B 2 226 ? 99.290  128.957 102.001 1.00 79.55  ? 226 LEU A CD1   1 
ATOM   2630 C CD2   . LEU B 2 226 ? 99.094  128.022 99.702  1.00 79.55  ? 226 LEU A CD2   1 
ATOM   2631 N N     . LEU B 2 227 ? 102.698 124.631 101.429 1.00 78.65  ? 227 LEU A N     1 
ATOM   2632 C CA    . LEU B 2 227 ? 104.084 124.219 101.242 1.00 78.65  ? 227 LEU A CA    1 
ATOM   2633 C C     . LEU B 2 227 ? 104.190 123.097 100.221 1.00 78.65  ? 227 LEU A C     1 
ATOM   2634 O O     . LEU B 2 227 ? 105.021 123.154 99.309  1.00 78.65  ? 227 LEU A O     1 
ATOM   2635 C CB    . LEU B 2 227 ? 104.688 123.784 102.577 1.00 78.65  ? 227 LEU A CB    1 
ATOM   2636 C CG    . LEU B 2 227 ? 104.953 124.874 103.615 1.00 78.65  ? 227 LEU A CG    1 
ATOM   2637 C CD1   . LEU B 2 227 ? 105.218 124.257 104.972 1.00 78.65  ? 227 LEU A CD1   1 
ATOM   2638 C CD2   . LEU B 2 227 ? 106.116 125.739 103.186 1.00 78.65  ? 227 LEU A CD2   1 
ATOM   2639 N N     . MET B 2 228 ? 103.346 122.072 100.347 1.00 80.53  ? 228 MET A N     1 
ATOM   2640 C CA    . MET B 2 228 ? 103.408 120.963 99.407  1.00 80.53  ? 228 MET A CA    1 
ATOM   2641 C C     . MET B 2 228 ? 102.903 121.364 98.029  1.00 80.53  ? 228 MET A C     1 
ATOM   2642 O O     . MET B 2 228 ? 103.328 120.783 97.030  1.00 80.53  ? 228 MET A O     1 
ATOM   2643 C CB    . MET B 2 228 ? 102.621 119.773 99.945  1.00 80.53  ? 228 MET A CB    1 
ATOM   2644 C CG    . MET B 2 228 ? 103.126 119.258 101.280 1.00 80.53  ? 228 MET A CG    1 
ATOM   2645 S SD    . MET B 2 228 ? 104.668 118.340 101.148 1.00 80.53  ? 228 MET A SD    1 
ATOM   2646 C CE    . MET B 2 228 ? 105.853 119.589 101.635 1.00 80.53  ? 228 MET A CE    1 
ATOM   2647 N N     . ALA B 2 229 ? 102.035 122.372 97.942  1.00 79.21  ? 229 ALA A N     1 
ATOM   2648 C CA    . ALA B 2 229 ? 101.622 122.857 96.632  1.00 79.21  ? 229 ALA A CA    1 
ATOM   2649 C C     . ALA B 2 229 ? 102.763 123.580 95.938  1.00 79.21  ? 229 ALA A C     1 
ATOM   2650 O O     . ALA B 2 229 ? 102.976 123.402 94.734  1.00 79.21  ? 229 ALA A O     1 
ATOM   2651 C CB    . ALA B 2 229 ? 100.408 123.772 96.768  1.00 79.21  ? 229 ALA A CB    1 
ATOM   2652 N N     . MET B 2 230 ? 103.506 124.401 96.680  1.00 79.10  ? 230 MET A N     1 
ATOM   2653 C CA    . MET B 2 230 ? 104.703 125.012 96.114  1.00 79.10  ? 230 MET A CA    1 
ATOM   2654 C C     . MET B 2 230 ? 105.715 123.949 95.714  1.00 79.10  ? 230 MET A C     1 
ATOM   2655 O O     . MET B 2 230 ? 106.363 124.062 94.670  1.00 79.10  ? 230 MET A O     1 
ATOM   2656 C CB    . MET B 2 230 ? 105.318 125.995 97.108  1.00 79.10  ? 230 MET A CB    1 
ATOM   2657 C CG    . MET B 2 230 ? 104.425 127.173 97.432  1.00 79.10  ? 230 MET A CG    1 
ATOM   2658 S SD    . MET B 2 230 ? 105.188 128.323 98.582  1.00 79.10  ? 230 MET A SD    1 
ATOM   2659 C CE    . MET B 2 230 ? 105.811 127.189 99.812  1.00 79.10  ? 230 MET A CE    1 
ATOM   2660 N N     . THR B 2 231 ? 105.846 122.898 96.523  1.00 79.04  ? 231 THR A N     1 
ATOM   2661 C CA    . THR B 2 231 ? 106.736 121.796 96.173  1.00 79.04  ? 231 THR A CA    1 
ATOM   2662 C C     . THR B 2 231 ? 106.298 121.114 94.882  1.00 79.04  ? 231 THR A C     1 
ATOM   2663 O O     . THR B 2 231 ? 107.134 120.776 94.039  1.00 79.04  ? 231 THR A O     1 
ATOM   2664 C CB    . THR B 2 231 ? 106.799 120.788 97.320  1.00 79.04  ? 231 THR A CB    1 
ATOM   2665 O OG1   . THR B 2 231 ? 107.345 121.421 98.482  1.00 79.04  ? 231 THR A OG1   1 
ATOM   2666 C CG2   . THR B 2 231 ? 107.667 119.606 96.947  1.00 79.04  ? 231 THR A CG2   1 
ATOM   2667 N N     . ILE B 2 232 ? 104.993 120.908 94.705  1.00 79.17  ? 232 ILE A N     1 
ATOM   2668 C CA    . ILE B 2 232 ? 104.505 120.242 93.501  1.00 79.17  ? 232 ILE A CA    1 
ATOM   2669 C C     . ILE B 2 232 ? 104.703 121.126 92.279  1.00 79.17  ? 232 ILE A C     1 
ATOM   2670 O O     . ILE B 2 232 ? 105.098 120.646 91.212  1.00 79.17  ? 232 ILE A O     1 
ATOM   2671 C CB    . ILE B 2 232 ? 103.032 119.831 93.664  1.00 79.17  ? 232 ILE A CB    1 
ATOM   2672 C CG1   . ILE B 2 232 ? 102.895 118.755 94.737  1.00 79.17  ? 232 ILE A CG1   1 
ATOM   2673 C CG2   . ILE B 2 232 ? 102.476 119.320 92.351  1.00 79.17  ? 232 ILE A CG2   1 
ATOM   2674 C CD1   . ILE B 2 232 ? 103.935 117.677 94.641  1.00 79.17  ? 232 ILE A CD1   1 
ATOM   2675 N N     . VAL B 2 233 ? 104.431 122.426 92.404  1.00 79.17  ? 233 VAL A N     1 
ATOM   2676 C CA    . VAL B 2 233 ? 104.652 123.326 91.275  1.00 79.17  ? 233 VAL A CA    1 
ATOM   2677 C C     . VAL B 2 233 ? 106.132 123.384 90.926  1.00 79.17  ? 233 VAL A C     1 
ATOM   2678 O O     . VAL B 2 233 ? 106.506 123.412 89.748  1.00 79.17  ? 233 VAL A O     1 
ATOM   2679 C CB    . VAL B 2 233 ? 104.088 124.726 91.576  1.00 79.17  ? 233 VAL A CB    1 
ATOM   2680 C CG1   . VAL B 2 233 ? 104.271 125.630 90.376  1.00 79.17  ? 233 VAL A CG1   1 
ATOM   2681 C CG2   . VAL B 2 233 ? 102.619 124.636 91.921  1.00 79.17  ? 233 VAL A CG2   1 
ATOM   2682 N N     . SER B 2 234 ? 106.997 123.361 91.937  1.00 78.61  ? 234 SER A N     1 
ATOM   2683 C CA    . SER B 2 234 ? 108.429 123.394 91.678  1.00 78.61  ? 234 SER A CA    1 
ATOM   2684 C C     . SER B 2 234 ? 108.902 122.105 91.021  1.00 78.61  ? 234 SER A C     1 
ATOM   2685 O O     . SER B 2 234 ? 109.729 122.138 90.106  1.00 78.61  ? 234 SER A O     1 
ATOM   2686 C CB    . SER B 2 234 ? 109.172 123.651 92.983  1.00 78.61  ? 234 SER A CB    1 
ATOM   2687 O OG    . SER B 2 234 ? 110.569 123.607 92.797  1.00 78.61  ? 234 SER A OG    1 
ATOM   2688 N N     . GLY B 2 235 ? 108.377 120.961 91.457  1.00 80.66  ? 235 GLY A N     1 
ATOM   2689 C CA    . GLY B 2 235 ? 108.738 119.707 90.821  1.00 80.66  ? 235 GLY A CA    1 
ATOM   2690 C C     . GLY B 2 235 ? 108.218 119.606 89.401  1.00 80.66  ? 235 GLY A C     1 
ATOM   2691 O O     . GLY B 2 235 ? 108.871 119.027 88.530  1.00 80.66  ? 235 GLY A O     1 
ATOM   2692 N N     . LEU B 2 236 ? 107.044 120.179 89.142  1.00 81.66  ? 236 LEU A N     1 
ATOM   2693 C CA    . LEU B 2 236 ? 106.520 120.190 87.783  1.00 81.66  ? 236 LEU A CA    1 
ATOM   2694 C C     . LEU B 2 236 ? 107.355 121.089 86.885  1.00 81.66  ? 236 LEU A C     1 
ATOM   2695 O O     . LEU B 2 236 ? 107.608 120.750 85.726  1.00 81.66  ? 236 LEU A O     1 
ATOM   2696 C CB    . LEU B 2 236 ? 105.059 120.633 87.785  1.00 81.66  ? 236 LEU A CB    1 
ATOM   2697 C CG    . LEU B 2 236 ? 104.061 119.602 88.306  1.00 81.66  ? 236 LEU A CG    1 
ATOM   2698 C CD1   . LEU B 2 236 ? 102.662 120.181 88.319  1.00 81.66  ? 236 LEU A CD1   1 
ATOM   2699 C CD2   . LEU B 2 236 ? 104.113 118.343 87.464  1.00 81.66  ? 236 LEU A CD2   1 
ATOM   2700 N N     . VAL B 2 237 ? 107.803 122.234 87.403  1.00 84.25  ? 237 VAL A N     1 
ATOM   2701 C CA    . VAL B 2 237 ? 108.696 123.090 86.627  1.00 84.25  ? 237 VAL A CA    1 
ATOM   2702 C C     . VAL B 2 237 ? 110.029 122.389 86.397  1.00 84.25  ? 237 VAL A C     1 
ATOM   2703 O O     . VAL B 2 237 ? 110.641 122.522 85.332  1.00 84.25  ? 237 VAL A O     1 
ATOM   2704 C CB    . VAL B 2 237 ? 108.878 124.450 87.324  1.00 84.25  ? 237 VAL A CB    1 
ATOM   2705 C CG1   . VAL B 2 237 ? 109.934 125.273 86.614  1.00 84.25  ? 237 VAL A CG1   1 
ATOM   2706 C CG2   . VAL B 2 237 ? 107.562 125.201 87.355  1.00 84.25  ? 237 VAL A CG2   1 
ATOM   2707 N N     . LEU B 2 238 ? 110.487 121.616 87.381  1.00 85.17  ? 238 LEU A N     1 
ATOM   2708 C CA    . LEU B 2 238 ? 111.700 120.821 87.215  1.00 85.17  ? 238 LEU A CA    1 
ATOM   2709 C C     . LEU B 2 238 ? 111.549 119.814 86.083  1.00 85.17  ? 238 LEU A C     1 
ATOM   2710 O O     . LEU B 2 238 ? 112.411 119.715 85.203  1.00 85.17  ? 238 LEU A O     1 
ATOM   2711 C CB    . LEU B 2 238 ? 112.026 120.108 88.524  1.00 85.17  ? 238 LEU A CB    1 
ATOM   2712 C CG    . LEU B 2 238 ? 112.982 118.923 88.457  1.00 85.17  ? 238 LEU A CG    1 
ATOM   2713 C CD1   . LEU B 2 238 ? 114.366 119.377 88.058  1.00 85.17  ? 238 LEU A CD1   1 
ATOM   2714 C CD2   . LEU B 2 238 ? 113.004 118.210 89.790  1.00 85.17  ? 238 LEU A CD2   1 
ATOM   2715 N N     . MET B 2 239 ? 110.459 119.046 86.099  1.00 88.19  ? 239 MET A N     1 
ATOM   2716 C CA    . MET B 2 239 ? 110.228 118.060 85.049  1.00 88.19  ? 239 MET A CA    1 
ATOM   2717 C C     . MET B 2 239 ? 110.069 118.727 83.690  1.00 88.19  ? 239 MET A C     1 
ATOM   2718 O O     . MET B 2 239 ? 110.556 118.214 82.677  1.00 88.19  ? 239 MET A O     1 
ATOM   2719 C CB    . MET B 2 239 ? 108.996 117.221 85.381  1.00 88.19  ? 239 MET A CB    1 
ATOM   2720 C CG    . MET B 2 239 ? 109.139 116.381 86.634  1.00 88.19  ? 239 MET A CG    1 
ATOM   2721 S SD    . MET B 2 239 ? 110.483 115.191 86.514  1.00 88.19  ? 239 MET A SD    1 
ATOM   2722 C CE    . MET B 2 239 ? 110.968 115.064 88.230  1.00 88.19  ? 239 MET A CE    1 
ATOM   2723 N N     . ALA B 2 240 ? 109.400 119.880 83.648  1.00 88.73  ? 240 ALA A N     1 
ATOM   2724 C CA    . ALA B 2 240 ? 109.206 120.573 82.382  1.00 88.73  ? 240 ALA A CA    1 
ATOM   2725 C C     . ALA B 2 240 ? 110.524 121.099 81.836  1.00 88.73  ? 240 ALA A C     1 
ATOM   2726 O O     . ALA B 2 240 ? 110.778 121.022 80.631  1.00 88.73  ? 240 ALA A O     1 
ATOM   2727 C CB    . ALA B 2 240 ? 108.204 121.712 82.555  1.00 88.73  ? 240 ALA A CB    1 
ATOM   2728 N N     . SER B 2 241 ? 111.383 121.625 82.708  1.00 90.91  ? 241 SER A N     1 
ATOM   2729 C CA    . SER B 2 241 ? 112.677 122.116 82.254  1.00 90.91  ? 241 SER A CA    1 
ATOM   2730 C C     . SER B 2 241 ? 113.577 120.970 81.821  1.00 90.91  ? 241 SER A C     1 
ATOM   2731 O O     . SER B 2 241 ? 114.358 121.112 80.876  1.00 90.91  ? 241 SER A O     1 
ATOM   2732 C CB    . SER B 2 241 ? 113.336 122.940 83.354  1.00 90.91  ? 241 SER A CB    1 
ATOM   2733 O OG    . SER B 2 241 ? 113.225 122.283 84.600  1.00 90.91  ? 241 SER A OG    1 
ATOM   2734 N N     . TYR B 2 242 ? 113.472 119.819 82.487  1.00 93.35  ? 242 TYR A N     1 
ATOM   2735 C CA    . TYR B 2 242 ? 114.221 118.647 82.048  1.00 93.35  ? 242 TYR A CA    1 
ATOM   2736 C C     . TYR B 2 242 ? 113.760 118.188 80.671  1.00 93.35  ? 242 TYR A C     1 
ATOM   2737 O O     . TYR B 2 242 ? 114.584 117.904 79.793  1.00 93.35  ? 242 TYR A O     1 
ATOM   2738 C CB    . TYR B 2 242 ? 114.072 117.526 83.074  1.00 93.35  ? 242 TYR A CB    1 
ATOM   2739 C CG    . TYR B 2 242 ? 114.892 116.297 82.780  1.00 93.35  ? 242 TYR A CG    1 
ATOM   2740 C CD1   . TYR B 2 242 ? 114.282 115.104 82.427  1.00 93.35  ? 242 TYR A CD1   1 
ATOM   2741 C CD2   . TYR B 2 242 ? 116.274 116.327 82.853  1.00 93.35  ? 242 TYR A CD2   1 
ATOM   2742 C CE1   . TYR B 2 242 ? 115.025 113.978 82.161  1.00 93.35  ? 242 TYR A CE1   1 
ATOM   2743 C CE2   . TYR B 2 242 ? 117.024 115.206 82.586  1.00 93.35  ? 242 TYR A CE2   1 
ATOM   2744 C CZ    . TYR B 2 242 ? 116.396 114.036 82.238  1.00 93.35  ? 242 TYR A CZ    1 
ATOM   2745 O OH    . TYR B 2 242 ? 117.145 112.916 81.972  1.00 93.35  ? 242 TYR A OH    1 
ATOM   2746 N N     . TRP B 2 243 ? 112.445 118.127 80.458  1.00 95.15  ? 243 TRP A N     1 
ATOM   2747 C CA    . TRP B 2 243 ? 111.926 117.773 79.142  1.00 95.15  ? 243 TRP A CA    1 
ATOM   2748 C C     . TRP B 2 243 ? 112.374 118.773 78.085  1.00 95.15  ? 243 TRP A C     1 
ATOM   2749 O O     . TRP B 2 243 ? 112.732 118.389 76.966  1.00 95.15  ? 243 TRP A O     1 
ATOM   2750 C CB    . TRP B 2 243 ? 110.403 117.691 79.186  1.00 95.15  ? 243 TRP A CB    1 
ATOM   2751 C CG    . TRP B 2 243 ? 109.777 117.563 77.841  1.00 95.15  ? 243 TRP A CG    1 
ATOM   2752 C CD1   . TRP B 2 243 ? 109.539 116.411 77.158  1.00 95.15  ? 243 TRP A CD1   1 
ATOM   2753 C CD2   . TRP B 2 243 ? 109.306 118.628 77.012  1.00 95.15  ? 243 TRP A CD2   1 
ATOM   2754 N NE1   . TRP B 2 243 ? 108.949 116.691 75.951  1.00 95.15  ? 243 TRP A NE1   1 
ATOM   2755 C CE2   . TRP B 2 243 ? 108.795 118.047 75.838  1.00 95.15  ? 243 TRP A CE2   1 
ATOM   2756 C CE3   . TRP B 2 243 ? 109.267 120.018 77.147  1.00 95.15  ? 243 TRP A CE3   1 
ATOM   2757 C CZ2   . TRP B 2 243 ? 108.251 118.804 74.807  1.00 95.15  ? 243 TRP A CZ2   1 
ATOM   2758 C CZ3   . TRP B 2 243 ? 108.727 120.769 76.122  1.00 95.15  ? 243 TRP A CZ3   1 
ATOM   2759 C CH2   . TRP B 2 243 ? 108.227 120.161 74.967  1.00 95.15  ? 243 TRP A CH2   1 
ATOM   2760 N N     . TRP B 2 244 ? 112.368 120.062 78.425  1.00 97.47  ? 244 TRP A N     1 
ATOM   2761 C CA    . TRP B 2 244 ? 112.747 121.082 77.455  1.00 97.47  ? 244 TRP A CA    1 
ATOM   2762 C C     . TRP B 2 244 ? 114.226 120.997 77.113  1.00 97.47  ? 244 TRP A C     1 
ATOM   2763 O O     . TRP B 2 244 ? 114.608 121.146 75.948  1.00 97.47  ? 244 TRP A O     1 
ATOM   2764 C CB    . TRP B 2 244 ? 112.400 122.468 77.990  1.00 97.47  ? 244 TRP A CB    1 
ATOM   2765 C CG    . TRP B 2 244 ? 112.473 123.538 76.955  1.00 97.47  ? 244 TRP A CG    1 
ATOM   2766 C CD1   . TRP B 2 244 ? 111.449 124.007 76.192  1.00 97.47  ? 244 TRP A CD1   1 
ATOM   2767 C CD2   . TRP B 2 244 ? 113.634 124.277 76.569  1.00 97.47  ? 244 TRP A CD2   1 
ATOM   2768 N NE1   . TRP B 2 244 ? 111.899 124.993 75.352  1.00 97.47  ? 244 TRP A NE1   1 
ATOM   2769 C CE2   . TRP B 2 244 ? 113.239 125.177 75.564  1.00 97.47  ? 244 TRP A CE2   1 
ATOM   2770 C CE3   . TRP B 2 244 ? 114.969 124.265 76.975  1.00 97.47  ? 244 TRP A CE3   1 
ATOM   2771 C CZ2   . TRP B 2 244 ? 114.130 126.056 74.960  1.00 97.47  ? 244 TRP A CZ2   1 
ATOM   2772 C CZ3   . TRP B 2 244 ? 115.852 125.137 76.374  1.00 97.47  ? 244 TRP A CZ3   1 
ATOM   2773 C CH2   . TRP B 2 244 ? 115.429 126.021 75.378  1.00 97.47  ? 244 TRP A CH2   1 
ATOM   2774 N N     . ILE B 2 245 ? 115.077 120.757 78.111  1.00 99.30  ? 245 ILE A N     1 
ATOM   2775 C CA    . ILE B 2 245 ? 116.506 120.682 77.842  1.00 99.30  ? 245 ILE A CA    1 
ATOM   2776 C C     . ILE B 2 245 ? 116.854 119.374 77.146  1.00 99.30  ? 245 ILE A C     1 
ATOM   2777 O O     . ILE B 2 245 ? 117.899 119.271 76.494  1.00 99.30  ? 245 ILE A O     1 
ATOM   2778 C CB    . ILE B 2 245 ? 117.306 120.874 79.143  1.00 99.30  ? 245 ILE A CB    1 
ATOM   2779 C CG1   . ILE B 2 245 ? 118.772 121.153 78.828  1.00 99.30  ? 245 ILE A CG1   1 
ATOM   2780 C CG2   . ILE B 2 245 ? 117.189 119.659 80.028  1.00 99.30  ? 245 ILE A CG2   1 
ATOM   2781 C CD1   . ILE B 2 245 ? 119.632 121.272 80.045  1.00 99.30  ? 245 ILE A CD1   1 
ATOM   2782 N N     . ASN B 2 246 ? 115.993 118.361 77.253  1.00 99.13  ? 246 ASN A N     1 
ATOM   2783 C CA    . ASN B 2 246 ? 116.228 117.140 76.490  1.00 99.13  ? 246 ASN A CA    1 
ATOM   2784 C C     . ASN B 2 246 ? 115.777 117.281 75.044  1.00 99.13  ? 246 ASN A C     1 
ATOM   2785 O O     . ASN B 2 246 ? 116.443 116.778 74.134  1.00 99.13  ? 246 ASN A O     1 
ATOM   2786 C CB    . ASN B 2 246 ? 115.516 115.960 77.142  1.00 99.13  ? 246 ASN A CB    1 
ATOM   2787 C CG    . ASN B 2 246 ? 116.199 115.497 78.398  1.00 99.13  ? 246 ASN A CG    1 
ATOM   2788 O OD1   . ASN B 2 246 ? 117.420 115.389 78.452  1.00 99.13  ? 246 ASN A OD1   1 
ATOM   2789 N ND2   . ASN B 2 246 ? 115.413 115.219 79.422  1.00 99.13  ? 246 ASN A ND2   1 
ATOM   2790 N N     . LYS B 2 247 ? 114.655 117.959 74.809  1.00 102.01 ? 247 LYS A N     1 
ATOM   2791 C CA    . LYS B 2 247 ? 114.115 118.031 73.459  1.00 102.01 ? 247 LYS A CA    1 
ATOM   2792 C C     . LYS B 2 247 ? 114.698 119.174 72.640  1.00 102.01 ? 247 LYS A C     1 
ATOM   2793 O O     . LYS B 2 247 ? 114.670 119.106 71.407  1.00 102.01 ? 247 LYS A O     1 
ATOM   2794 C CB    . LYS B 2 247 ? 112.592 118.164 73.505  1.00 102.01 ? 247 LYS A CB    1 
ATOM   2795 C CG    . LYS B 2 247 ? 111.906 117.818 72.194  1.00 102.01 ? 247 LYS A CG    1 
ATOM   2796 C CD    . LYS B 2 247 ? 110.513 118.414 72.119  1.00 102.01 ? 247 LYS A CD    1 
ATOM   2797 C CE    . LYS B 2 247 ? 109.782 117.940 70.875  1.00 102.01 ? 247 LYS A CE    1 
ATOM   2798 N NZ    . LYS B 2 247 ? 109.560 116.469 70.894  1.00 102.01 ? 247 LYS A NZ    1 
ATOM   2799 N N     . ASN B 2 248 ? 115.224 120.218 73.280  1.00 105.07 ? 248 ASN A N     1 
ATOM   2800 C CA    . ASN B 2 248 ? 115.703 121.387 72.560  1.00 105.07 ? 248 ASN A CA    1 
ATOM   2801 C C     . ASN B 2 248 ? 117.189 121.664 72.718  1.00 105.07 ? 248 ASN A C     1 
ATOM   2802 O O     . ASN B 2 248 ? 117.735 122.436 71.924  1.00 105.07 ? 248 ASN A O     1 
ATOM   2803 C CB    . ASN B 2 248 ? 114.932 122.641 72.999  1.00 105.07 ? 248 ASN A CB    1 
ATOM   2804 C CG    . ASN B 2 248 ? 113.474 122.597 72.601  1.00 105.07 ? 248 ASN A CG    1 
ATOM   2805 O OD1   . ASN B 2 248 ? 112.874 121.528 72.519  1.00 105.07 ? 248 ASN A OD1   1 
ATOM   2806 N ND2   . ASN B 2 248 ? 112.895 123.764 72.348  1.00 105.07 ? 248 ASN A ND2   1 
ATOM   2807 N N     . VAL B 2 249 ? 117.855 121.076 73.704  1.00 109.10 ? 249 VAL A N     1 
ATOM   2808 C CA    . VAL B 2 249 ? 119.264 121.332 73.966  1.00 109.10 ? 249 VAL A CA    1 
ATOM   2809 C C     . VAL B 2 249 ? 120.106 120.078 73.769  1.00 109.10 ? 249 VAL A C     1 
ATOM   2810 O O     . VAL B 2 249 ? 121.052 120.075 72.981  1.00 109.10 ? 249 VAL A O     1 
ATOM   2811 C CB    . VAL B 2 249 ? 119.466 121.916 75.381  1.00 109.10 ? 249 VAL A CB    1 
ATOM   2812 C CG1   . VAL B 2 249 ? 120.944 122.024 75.701  1.00 109.10 ? 249 VAL A CG1   1 
ATOM   2813 C CG2   . VAL B 2 249 ? 118.795 123.269 75.490  1.00 109.10 ? 249 VAL A CG2   1 
ATOM   2814 N N     . LEU B 2 250 ? 119.775 118.999 74.478  1.00 111.26 ? 250 LEU A N     1 
ATOM   2815 C CA    . LEU B 2 250 ? 120.576 117.785 74.400  1.00 111.26 ? 250 LEU A CA    1 
ATOM   2816 C C     . LEU B 2 250 ? 120.481 117.092 73.049  1.00 111.26 ? 250 LEU A C     1 
ATOM   2817 O O     . LEU B 2 250 ? 121.216 116.126 72.818  1.00 111.26 ? 250 LEU A O     1 
ATOM   2818 C CB    . LEU B 2 250 ? 120.170 116.812 75.504  1.00 111.26 ? 250 LEU A CB    1 
ATOM   2819 C CG    . LEU B 2 250 ? 120.475 117.253 76.934  1.00 111.26 ? 250 LEU A CG    1 
ATOM   2820 C CD1   . LEU B 2 250 ? 120.480 116.049 77.850  1.00 111.26 ? 250 LEU A CD1   1 
ATOM   2821 C CD2   . LEU B 2 250 ? 121.799 117.989 77.006  1.00 111.26 ? 250 LEU A CD2   1 
ATOM   2822 N N     . THR B 2 251 ? 119.604 117.548 72.159  1.00 114.27 ? 251 THR A N     1 
ATOM   2823 C CA    . THR B 2 251 ? 119.562 117.036 70.799  1.00 114.27 ? 251 THR A CA    1 
ATOM   2824 C C     . THR B 2 251 ? 120.196 117.989 69.798  1.00 114.27 ? 251 THR A C     1 
ATOM   2825 O O     . THR B 2 251 ? 120.338 117.629 68.625  1.00 114.27 ? 251 THR A O     1 
ATOM   2826 C CB    . THR B 2 251 ? 118.117 116.747 70.378  1.00 114.27 ? 251 THR A CB    1 
ATOM   2827 O OG1   . THR B 2 251 ? 118.118 115.886 69.232  1.00 114.27 ? 251 THR A OG1   1 
ATOM   2828 C CG2   . THR B 2 251 ? 117.398 118.039 70.030  1.00 114.27 ? 251 THR A CG2   1 
ATOM   2829 N N     . ASP B 2 252 ? 120.574 119.183 70.232  1.00 121.75 ? 252 ASP A N     1 
ATOM   2830 C CA    . ASP B 2 252 ? 121.240 120.136 69.358  1.00 121.75 ? 252 ASP A CA    1 
ATOM   2831 C C     . ASP B 2 252 ? 122.727 119.803 69.306  1.00 121.75 ? 252 ASP A C     1 
ATOM   2832 O O     . ASP B 2 252 ? 123.369 119.727 70.360  1.00 121.75 ? 252 ASP A O     1 
ATOM   2833 C CB    . ASP B 2 252 ? 121.019 121.557 69.871  1.00 121.75 ? 252 ASP A CB    1 
ATOM   2834 C CG    . ASP B 2 252 ? 121.482 122.627 68.892  1.00 121.75 ? 252 ASP A CG    1 
ATOM   2835 O OD1   . ASP B 2 252 ? 122.460 122.404 68.151  1.00 121.75 ? 252 ASP A OD1   1 
ATOM   2836 O OD2   . ASP B 2 252 ? 120.857 123.709 68.868  1.00 121.75 ? 252 ASP A OD2   1 
ATOM   2837 N N     . PRO B 2 253 ? 123.310 119.595 68.121  1.00 124.93 ? 253 PRO A N     1 
ATOM   2838 C CA    . PRO B 2 253 ? 124.745 119.283 68.043  1.00 124.93 ? 253 PRO A CA    1 
ATOM   2839 C C     . PRO B 2 253 ? 125.657 120.437 68.428  1.00 124.93 ? 253 PRO A C     1 
ATOM   2840 O O     . PRO B 2 253 ? 126.880 120.293 68.326  1.00 124.93 ? 253 PRO A O     1 
ATOM   2841 C CB    . PRO B 2 253 ? 124.942 118.905 66.564  1.00 124.93 ? 253 PRO A CB    1 
ATOM   2842 C CG    . PRO B 2 253 ? 123.571 118.587 66.052  1.00 124.93 ? 253 PRO A CG    1 
ATOM   2843 C CD    . PRO B 2 253 ? 122.647 119.482 66.812  1.00 124.93 ? 253 PRO A CD    1 
ATOM   2844 N N     . ARG B 2 254 ? 125.110 121.572 68.862  1.00 125.28 ? 254 ARG A N     1 
ATOM   2845 C CA    . ARG B 2 254 ? 125.920 122.719 69.249  1.00 125.28 ? 254 ARG A CA    1 
ATOM   2846 C C     . ARG B 2 254 ? 126.182 122.757 70.751  1.00 125.28 ? 254 ARG A C     1 
ATOM   2847 O O     . ARG B 2 254 ? 127.270 123.157 71.177  1.00 125.28 ? 254 ARG A O     1 
ATOM   2848 C CB    . ARG B 2 254 ? 125.241 124.012 68.780  1.00 125.28 ? 254 ARG A CB    1 
ATOM   2849 C CG    . ARG B 2 254 ? 126.058 125.290 68.954  1.00 125.28 ? 254 ARG A CG    1 
ATOM   2850 C CD    . ARG B 2 254 ? 125.740 125.991 70.269  1.00 125.28 ? 254 ARG A CD    1 
ATOM   2851 N NE    . ARG B 2 254 ? 124.318 126.311 70.381  1.00 125.28 ? 254 ARG A NE    1 
ATOM   2852 C CZ    . ARG B 2 254 ? 123.750 127.396 69.862  1.00 125.28 ? 254 ARG A CZ    1 
ATOM   2853 N NH1   . ARG B 2 254 ? 124.484 128.278 69.199  1.00 125.28 ? 254 ARG A NH1   1 
ATOM   2854 N NH2   . ARG B 2 254 ? 122.447 127.601 70.012  1.00 125.28 ? 254 ARG A NH2   1 
ATOM   2855 N N     . PHE B 2 255 ? 125.211 122.345 71.565  1.00 121.79 ? 255 PHE A N     1 
ATOM   2856 C CA    . PHE B 2 255 ? 125.362 122.379 73.015  1.00 121.79 ? 255 PHE A CA    1 
ATOM   2857 C C     . PHE B 2 255 ? 125.914 121.074 73.578  1.00 121.79 ? 255 PHE A C     1 
ATOM   2858 O O     . PHE B 2 255 ? 126.814 121.090 74.423  1.00 121.79 ? 255 PHE A O     1 
ATOM   2859 C CB    . PHE B 2 255 ? 124.018 122.700 73.673  1.00 121.79 ? 255 PHE A CB    1 
ATOM   2860 C CG    . PHE B 2 255 ? 123.566 124.110 73.464  1.00 121.79 ? 255 PHE A CG    1 
ATOM   2861 C CD1   . PHE B 2 255 ? 122.383 124.382 72.804  1.00 121.79 ? 255 PHE A CD1   1 
ATOM   2862 C CD2   . PHE B 2 255 ? 124.325 125.165 73.931  1.00 121.79 ? 255 PHE A CD2   1 
ATOM   2863 C CE1   . PHE B 2 255 ? 121.966 125.680 72.613  1.00 121.79 ? 255 PHE A CE1   1 
ATOM   2864 C CE2   . PHE B 2 255 ? 123.914 126.464 73.742  1.00 121.79 ? 255 PHE A CE2   1 
ATOM   2865 C CZ    . PHE B 2 255 ? 122.731 126.723 73.086  1.00 121.79 ? 255 PHE A CZ    1 
ATOM   2866 N N     . TYR B 2 256 ? 125.387 119.940 73.125  1.00 127.52 ? 256 TYR A N     1 
ATOM   2867 C CA    . TYR B 2 256 ? 125.721 118.644 73.694  1.00 127.52 ? 256 TYR A CA    1 
ATOM   2868 C C     . TYR B 2 256 ? 125.873 117.612 72.590  1.00 127.52 ? 256 TYR A C     1 
ATOM   2869 O O     . TYR B 2 256 ? 125.145 117.637 71.593  1.00 127.52 ? 256 TYR A O     1 
ATOM   2870 C CB    . TYR B 2 256 ? 124.650 118.189 74.693  1.00 127.52 ? 256 TYR A CB    1 
ATOM   2871 C CG    . TYR B 2 256 ? 124.794 116.759 75.161  1.00 127.52 ? 256 TYR A CG    1 
ATOM   2872 C CD1   . TYR B 2 256 ? 125.858 116.373 75.963  1.00 127.52 ? 256 TYR A CD1   1 
ATOM   2873 C CD2   . TYR B 2 256 ? 123.857 115.798 74.810  1.00 127.52 ? 256 TYR A CD2   1 
ATOM   2874 C CE1   . TYR B 2 256 ? 125.989 115.070 76.395  1.00 127.52 ? 256 TYR A CE1   1 
ATOM   2875 C CE2   . TYR B 2 256 ? 123.979 114.493 75.238  1.00 127.52 ? 256 TYR A CE2   1 
ATOM   2876 C CZ    . TYR B 2 256 ? 125.046 114.134 76.030  1.00 127.52 ? 256 TYR A CZ    1 
ATOM   2877 O OH    . TYR B 2 256 ? 125.173 112.834 76.458  1.00 127.52 ? 256 TYR A OH    1 
ATOM   2878 N N     . ASN B 2 257 ? 126.828 116.710 72.779  1.00 142.10 ? 257 ASN A N     1 
ATOM   2879 C CA    . ASN B 2 257 ? 127.092 115.608 71.867  1.00 142.10 ? 257 ASN A CA    1 
ATOM   2880 C C     . ASN B 2 257 ? 127.695 114.467 72.676  1.00 142.10 ? 257 ASN A C     1 
ATOM   2881 O O     . ASN B 2 257 ? 128.736 114.651 73.319  1.00 142.10 ? 257 ASN A O     1 
ATOM   2882 C CB    . ASN B 2 257 ? 128.032 116.047 70.741  1.00 142.10 ? 257 ASN A CB    1 
ATOM   2883 C CG    . ASN B 2 257 ? 128.123 115.028 69.615  1.00 142.10 ? 257 ASN A CG    1 
ATOM   2884 O OD1   . ASN B 2 257 ? 127.501 113.969 69.661  1.00 142.10 ? 257 ASN A OD1   1 
ATOM   2885 N ND2   . ASN B 2 257 ? 128.904 115.353 68.591  1.00 142.10 ? 257 ASN A ND2   1 
ATOM   2886 N N     . PRO B 2 258 ? 127.078 113.281 72.680  1.00 147.77 ? 258 PRO A N     1 
ATOM   2887 C CA    . PRO B 2 258 ? 127.591 112.179 73.510  1.00 147.77 ? 258 PRO A CA    1 
ATOM   2888 C C     . PRO B 2 258 ? 128.978 111.687 73.121  1.00 147.77 ? 258 PRO A C     1 
ATOM   2889 O O     . PRO B 2 258 ? 129.446 110.698 73.697  1.00 147.77 ? 258 PRO A O     1 
ATOM   2890 C CB    . PRO B 2 258 ? 126.539 111.075 73.314  1.00 147.77 ? 258 PRO A CB    1 
ATOM   2891 C CG    . PRO B 2 258 ? 125.825 111.437 72.049  1.00 147.77 ? 258 PRO A CG    1 
ATOM   2892 C CD    . PRO B 2 258 ? 125.811 112.930 72.018  1.00 147.77 ? 258 PRO A CD    1 
ATOM   2893 N N     . GLU B 2 259 ? 129.652 112.335 72.172  1.00 155.27 ? 259 GLU A N     1 
ATOM   2894 C CA    . GLU B 2 259 ? 131.009 111.980 71.785  1.00 155.27 ? 259 GLU A CA    1 
ATOM   2895 C C     . GLU B 2 259 ? 132.060 112.597 72.701  1.00 155.27 ? 259 GLU A C     1 
ATOM   2896 O O     . GLU B 2 259 ? 133.258 112.496 72.409  1.00 155.27 ? 259 GLU A O     1 
ATOM   2897 C CB    . GLU B 2 259 ? 131.271 112.417 70.342  1.00 155.27 ? 259 GLU A CB    1 
ATOM   2898 C CG    . GLU B 2 259 ? 130.373 111.761 69.310  1.00 155.27 ? 259 GLU A CG    1 
ATOM   2899 C CD    . GLU B 2 259 ? 130.617 110.274 69.178  1.00 155.27 ? 259 GLU A CD    1 
ATOM   2900 O OE1   . GLU B 2 259 ? 131.770 109.835 69.370  1.00 155.27 ? 259 GLU A OE1   1 
ATOM   2901 O OE2   . GLU B 2 259 ? 129.651 109.542 68.880  1.00 155.27 ? 259 GLU A OE2   1 
ATOM   2902 N N     . GLU B 2 260 ? 131.645 113.234 73.795  1.00 156.65 ? 260 GLU A N     1 
ATOM   2903 C CA    . GLU B 2 260 ? 132.564 113.990 74.638  1.00 156.65 ? 260 GLU A CA    1 
ATOM   2904 C C     . GLU B 2 260 ? 132.878 113.299 75.959  1.00 156.65 ? 260 GLU A C     1 
ATOM   2905 O O     . GLU B 2 260 ? 134.050 113.070 76.270  1.00 156.65 ? 260 GLU A O     1 
ATOM   2906 C CB    . GLU B 2 260 ? 131.993 115.389 74.903  1.00 156.65 ? 260 GLU A CB    1 
ATOM   2907 C CG    . GLU B 2 260 ? 131.981 116.290 73.675  1.00 156.65 ? 260 GLU A CG    1 
ATOM   2908 C CD    . GLU B 2 260 ? 133.334 116.375 72.993  1.00 156.65 ? 260 GLU A CD    1 
ATOM   2909 O OE1   . GLU B 2 260 ? 134.359 116.438 73.704  1.00 156.65 ? 260 GLU A OE1   1 
ATOM   2910 O OE2   . GLU B 2 260 ? 133.373 116.376 71.744  1.00 156.65 ? 260 GLU A OE2   1 
ATOM   2911 N N     . MET B 2 261 ? 131.859 112.957 76.745  1.00 158.36 ? 261 MET A N     1 
ATOM   2912 C CA    . MET B 2 261 ? 132.092 112.346 78.047  1.00 158.36 ? 261 MET A CA    1 
ATOM   2913 C C     . MET B 2 261 ? 132.430 110.863 77.945  1.00 158.36 ? 261 MET A C     1 
ATOM   2914 O O     . MET B 2 261 ? 132.789 110.249 78.957  1.00 158.36 ? 261 MET A O     1 
ATOM   2915 C CB    . MET B 2 261 ? 130.869 112.558 78.949  1.00 158.36 ? 261 MET A CB    1 
ATOM   2916 C CG    . MET B 2 261 ? 131.107 112.262 80.424  1.00 158.36 ? 261 MET A CG    1 
ATOM   2917 S SD    . MET B 2 261 ? 132.311 113.394 81.150  1.00 158.36 ? 261 MET A SD    1 
ATOM   2918 C CE    . MET B 2 261 ? 132.940 112.409 82.507  1.00 158.36 ? 261 MET A CE    1 
ATOM   2919 N N     . GLN B 2 262 ? 132.341 110.278 76.747  1.00 162.95 ? 262 GLN A N     1 
ATOM   2920 C CA    . GLN B 2 262 ? 132.780 108.899 76.563  1.00 162.95 ? 262 GLN A CA    1 
ATOM   2921 C C     . GLN B 2 262 ? 134.265 108.756 76.871  1.00 162.95 ? 262 GLN A C     1 
ATOM   2922 O O     . GLN B 2 262 ? 134.705 107.717 77.378  1.00 162.95 ? 262 GLN A O     1 
ATOM   2923 C CB    . GLN B 2 262 ? 132.475 108.440 75.136  1.00 162.95 ? 262 GLN A CB    1 
ATOM   2924 C CG    . GLN B 2 262 ? 132.793 106.978 74.858  1.00 162.95 ? 262 GLN A CG    1 
ATOM   2925 C CD    . GLN B 2 262 ? 132.440 106.567 73.440  1.00 162.95 ? 262 GLN A CD    1 
ATOM   2926 O OE1   . GLN B 2 262 ? 131.991 107.386 72.638  1.00 162.95 ? 262 GLN A OE1   1 
ATOM   2927 N NE2   . GLN B 2 262 ? 132.642 105.293 73.124  1.00 162.95 ? 262 GLN A NE2   1 
ATOM   2928 N N     . LYS B 2 263 ? 135.049 109.800 76.584  1.00 163.77 ? 263 LYS A N     1 
ATOM   2929 C CA    . LYS B 2 263 ? 136.475 109.783 76.895  1.00 163.77 ? 263 LYS A CA    1 
ATOM   2930 C C     . LYS B 2 263 ? 136.714 109.526 78.377  1.00 163.77 ? 263 LYS A C     1 
ATOM   2931 O O     . LYS B 2 263 ? 137.550 108.691 78.746  1.00 163.77 ? 263 LYS A O     1 
ATOM   2932 C CB    . LYS B 2 263 ? 137.112 111.110 76.482  1.00 163.77 ? 263 LYS A CB    1 
ATOM   2933 C CG    . LYS B 2 263 ? 136.685 111.614 75.117  1.00 163.77 ? 263 LYS A CG    1 
ATOM   2934 C CD    . LYS B 2 263 ? 137.493 112.835 74.707  1.00 163.77 ? 263 LYS A CD    1 
ATOM   2935 C CE    . LYS B 2 263 ? 137.320 113.965 75.714  1.00 163.77 ? 263 LYS A CE    1 
ATOM   2936 N NZ    . LYS B 2 263 ? 137.384 115.310 75.077  1.00 163.77 ? 263 LYS A NZ    1 
ATOM   2937 N N     . GLY B 2 264 ? 135.988 110.236 79.242  1.00 165.10 ? 264 GLY A N     1 
ATOM   2938 C CA    . GLY B 2 264 ? 136.161 110.046 80.670  1.00 165.10 ? 264 GLY A CA    1 
ATOM   2939 C C     . GLY B 2 264 ? 135.440 108.826 81.201  1.00 165.10 ? 264 GLY A C     1 
ATOM   2940 O O     . GLY B 2 264 ? 135.827 108.275 82.236  1.00 165.10 ? 264 GLY A O     1 
ATOM   2941 N N     . LYS B 2 265 ? 134.385 108.387 80.513  1.00 166.33 ? 265 LYS A N     1 
ATOM   2942 C CA    . LYS B 2 265 ? 133.640 107.220 80.966  1.00 166.33 ? 265 LYS A CA    1 
ATOM   2943 C C     . LYS B 2 265 ? 134.276 105.909 80.513  1.00 166.33 ? 265 LYS A C     1 
ATOM   2944 O O     . LYS B 2 265 ? 133.840 104.842 80.961  1.00 166.33 ? 265 LYS A O     1 
ATOM   2945 C CB    . LYS B 2 265 ? 132.186 107.309 80.485  1.00 166.33 ? 265 LYS A CB    1 
ATOM   2946 C CG    . LYS B 2 265 ? 131.234 106.328 81.162  1.00 166.33 ? 265 LYS A CG    1 
ATOM   2947 C CD    . LYS B 2 265 ? 129.786 106.571 80.771  1.00 166.33 ? 265 LYS A CD    1 
ATOM   2948 C CE    . LYS B 2 265 ? 129.495 106.049 79.377  1.00 166.33 ? 265 LYS A CE    1 
ATOM   2949 N NZ    . LYS B 2 265 ? 129.529 104.561 79.347  1.00 166.33 ? 265 LYS A NZ    1 
ATOM   2950 N N     . LYS B 2 266 ? 135.286 105.959 79.635  1.00 165.84 ? 266 LYS A N     1 
ATOM   2951 C CA    . LYS B 2 266 ? 136.084 104.766 79.357  1.00 165.84 ? 266 LYS A CA    1 
ATOM   2952 C C     . LYS B 2 266 ? 136.551 104.117 80.654  1.00 165.84 ? 266 LYS A C     1 
ATOM   2953 O O     . LYS B 2 266 ? 136.386 102.910 80.858  1.00 165.84 ? 266 LYS A O     1 
ATOM   2954 C CB    . LYS B 2 266 ? 137.284 105.117 78.475  1.00 165.84 ? 266 LYS A CB    1 
ATOM   2955 C CG    . LYS B 2 266 ? 136.934 105.643 77.095  1.00 165.84 ? 266 LYS A CG    1 
ATOM   2956 C CD    . LYS B 2 266 ? 135.921 104.751 76.394  1.00 165.84 ? 266 LYS A CD    1 
ATOM   2957 C CE    . LYS B 2 266 ? 136.610 103.663 75.588  1.00 165.84 ? 266 LYS A CE    1 
ATOM   2958 N NZ    . LYS B 2 266 ? 135.677 102.558 75.236  1.00 165.84 ? 266 LYS A NZ    1 
ATOM   2959 N N     . GLY B 2 267 ? 137.138 104.912 81.544  1.00 169.62 ? 267 GLY A N     1 
ATOM   2960 C CA    . GLY B 2 267 ? 137.425 104.469 82.891  1.00 169.62 ? 267 GLY A CA    1 
ATOM   2961 C C     . GLY B 2 267 ? 136.245 104.714 83.808  1.00 169.62 ? 267 GLY A C     1 
ATOM   2962 O O     . GLY B 2 267 ? 136.256 105.657 84.605  1.00 169.62 ? 267 GLY A O     1 
ATOM   2963 N N     . ALA B 2 268 ? 135.211 103.881 83.682  1.00 171.28 ? 268 ALA A N     1 
ATOM   2964 C CA    . ALA B 2 268 ? 133.996 104.058 84.467  1.00 171.28 ? 268 ALA A CA    1 
ATOM   2965 C C     . ALA B 2 268 ? 134.306 104.042 85.959  1.00 171.28 ? 268 ALA A C     1 
ATOM   2966 O O     . ALA B 2 268 ? 135.176 103.300 86.422  1.00 171.28 ? 268 ALA A O     1 
ATOM   2967 C CB    . ALA B 2 268 ? 132.982 102.966 84.127  1.00 171.28 ? 268 ALA A CB    1 
ATOM   2968 N N     . LYS B 2 269 ? 133.574 104.873 86.708  1.00 171.92 ? 269 LYS A N     1 
ATOM   2969 C CA    . LYS B 2 269 ? 133.782 105.144 88.127  1.00 171.92 ? 269 LYS A CA    1 
ATOM   2970 C C     . LYS B 2 269 ? 133.893 103.872 88.959  1.00 171.92 ? 269 LYS A C     1 
ATOM   2971 O O     . LYS B 2 269 ? 132.894 103.169 89.163  1.00 171.92 ? 269 LYS A O     1 
ATOM   2972 C CB    . LYS B 2 269 ? 132.643 106.015 88.660  1.00 171.92 ? 269 LYS A CB    1 
ATOM   2973 C CG    . LYS B 2 269 ? 132.730 106.322 90.145  1.00 171.92 ? 269 LYS A CG    1 
ATOM   2974 C CD    . LYS B 2 269 ? 133.920 107.209 90.463  1.00 171.92 ? 269 LYS A CD    1 
ATOM   2975 C CE    . LYS B 2 269 ? 133.910 107.629 91.922  1.00 171.92 ? 269 LYS A CE    1 
ATOM   2976 N NZ    . LYS B 2 269 ? 134.109 106.468 92.833  1.00 171.92 ? 269 LYS A NZ    1 
ATOM   2977 N N     . PRO B 2 270 ? 135.089 103.544 89.457  1.00 173.25 ? 270 PRO A N     1 
ATOM   2978 C CA    . PRO B 2 270 ? 135.271 102.385 90.358  1.00 173.25 ? 270 PRO A CA    1 
ATOM   2979 C C     . PRO B 2 270 ? 135.055 102.732 91.832  1.00 173.25 ? 270 PRO A C     1 
ATOM   2980 O O     . PRO B 2 270 ? 135.987 102.953 92.610  1.00 173.25 ? 270 PRO A O     1 
ATOM   2981 C CB    . PRO B 2 270 ? 136.716 101.973 90.078  1.00 173.25 ? 270 PRO A CB    1 
ATOM   2982 C CG    . PRO B 2 270 ? 137.403 103.273 89.765  1.00 173.25 ? 270 PRO A CG    1 
ATOM   2983 C CD    . PRO B 2 270 ? 136.372 104.204 89.153  1.00 173.25 ? 270 PRO A CD    1 
ATOM   2984 N N     . LYS B 2 271 ? 133.789 102.789 92.239  1.00 169.54 ? 271 LYS A N     1 
ATOM   2985 C CA    . LYS B 2 271 ? 133.465 103.135 93.619  1.00 169.54 ? 271 LYS A CA    1 
ATOM   2986 C C     . LYS B 2 271 ? 133.872 102.000 94.555  1.00 169.54 ? 271 LYS A C     1 
ATOM   2987 O O     . LYS B 2 271 ? 133.398 100.866 94.421  1.00 169.54 ? 271 LYS A O     1 
ATOM   2988 C CB    . LYS B 2 271 ? 131.978 103.467 93.756  1.00 169.54 ? 271 LYS A CB    1 
ATOM   2989 C CG    . LYS B 2 271 ? 131.009 102.351 93.392  1.00 169.54 ? 271 LYS A CG    1 
ATOM   2990 C CD    . LYS B 2 271 ? 129.568 102.790 93.605  1.00 169.54 ? 271 LYS A CD    1 
ATOM   2991 C CE    . LYS B 2 271 ? 129.128 103.777 92.536  1.00 169.54 ? 271 LYS A CE    1 
ATOM   2992 N NZ    . LYS B 2 271 ? 127.679 104.103 92.637  1.00 169.54 ? 271 LYS A NZ    1 
ATOM   2993 N N     . MET B 2 272 ? 134.775 102.303 95.483  1.00 163.75 ? 272 MET A N     1 
ATOM   2994 C CA    . MET B 2 272 ? 135.214 101.326 96.468  1.00 163.75 ? 272 MET A CA    1 
ATOM   2995 C C     . MET B 2 272 ? 134.105 101.103 97.494  1.00 163.75 ? 272 MET A C     1 
ATOM   2996 O O     . MET B 2 272 ? 133.399 102.038 97.881  1.00 163.75 ? 272 MET A O     1 
ATOM   2997 C CB    . MET B 2 272 ? 136.482 101.821 97.157  1.00 163.75 ? 272 MET A CB    1 
ATOM   2998 C CG    . MET B 2 272 ? 137.601 102.204 96.200  1.00 163.75 ? 272 MET A CG    1 
ATOM   2999 S SD    . MET B 2 272 ? 139.259 102.159 96.901  1.00 163.75 ? 272 MET A SD    1 
ATOM   3000 C CE    . MET B 2 272 ? 139.682 100.440 96.664  1.00 163.75 ? 272 MET A CE    1 
ATOM   3001 N N     . ASN B 2 273 ? 133.934 99.849  97.924  1.00 162.87 ? 273 ASN A N     1 
ATOM   3002 C CA    . ASN B 2 273 ? 132.744 99.512  98.700  1.00 162.87 ? 273 ASN A CA    1 
ATOM   3003 C C     . ASN B 2 273 ? 132.675 100.225 100.048 1.00 162.87 ? 273 ASN A C     1 
ATOM   3004 O O     . ASN B 2 273 ? 131.966 101.230 100.173 1.00 162.87 ? 273 ASN A O     1 
ATOM   3005 C CB    . ASN B 2 273 ? 132.679 97.999  98.908  1.00 162.87 ? 273 ASN A CB    1 
ATOM   3006 C CG    . ASN B 2 273 ? 134.033 97.397  99.237  1.00 162.87 ? 273 ASN A CG    1 
ATOM   3007 O OD1   . ASN B 2 273 ? 134.775 97.936  100.057 1.00 162.87 ? 273 ASN A OD1   1 
ATOM   3008 N ND2   . ASN B 2 273 ? 134.362 96.281  98.598  1.00 162.87 ? 273 ASN A ND2   1 
ATOM   3009 N N     . MET B 2 274 ? 133.403 99.736  101.057 1.00 161.48 ? 274 MET A N     1 
ATOM   3010 C CA    . MET B 2 274 ? 133.650 100.507 102.273 1.00 161.48 ? 274 MET A CA    1 
ATOM   3011 C C     . MET B 2 274 ? 135.075 100.345 102.796 1.00 161.48 ? 274 MET A C     1 
ATOM   3012 O O     . MET B 2 274 ? 135.722 101.320 103.201 1.00 161.48 ? 274 MET A O     1 
ATOM   3013 C CB    . MET B 2 274 ? 132.654 100.119 103.372 1.00 161.48 ? 274 MET A CB    1 
ATOM   3014 C CG    . MET B 2 274 ? 131.197 100.446 103.063 1.00 161.48 ? 274 MET A CG    1 
ATOM   3015 S SD    . MET B 2 274 ? 130.897 102.222 102.935 1.00 161.48 ? 274 MET A SD    1 
ATOM   3016 C CE    . MET B 2 274 ? 130.726 102.656 104.662 1.00 161.48 ? 274 MET A CE    1 
ATOM   3017 N N     . LYS B 2 275 ? 135.587 99.113  102.768 1.00 159.61 ? 275 LYS A N     1 
ATOM   3018 C CA    . LYS B 2 275 ? 136.746 98.772  103.585 1.00 159.61 ? 275 LYS A CA    1 
ATOM   3019 C C     . LYS B 2 275 ? 138.037 98.650  102.795 1.00 159.61 ? 275 LYS A C     1 
ATOM   3020 O O     . LYS B 2 275 ? 139.116 98.857  103.365 1.00 159.61 ? 275 LYS A O     1 
ATOM   3021 C CB    . LYS B 2 275 ? 136.485 97.474  104.361 1.00 159.61 ? 275 LYS A CB    1 
ATOM   3022 C CG    . LYS B 2 275 ? 135.237 97.543  105.233 1.00 159.61 ? 275 LYS A CG    1 
ATOM   3023 C CD    . LYS B 2 275 ? 135.550 97.234  106.689 1.00 159.61 ? 275 LYS A CD    1 
ATOM   3024 C CE    . LYS B 2 275 ? 134.276 97.086  107.510 1.00 159.61 ? 275 LYS A CE    1 
ATOM   3025 N NZ    . LYS B 2 275 ? 134.492 97.370  108.958 1.00 159.61 ? 275 LYS A NZ    1 
ATOM   3026 N N     . ASP B 2 276 ? 137.957 98.363  101.497 1.00 160.11 ? 276 ASP A N     1 
ATOM   3027 C CA    . ASP B 2 276 ? 139.106 98.611  100.638 1.00 160.11 ? 276 ASP A CA    1 
ATOM   3028 C C     . ASP B 2 276 ? 139.540 100.071 100.708 1.00 160.11 ? 276 ASP A C     1 
ATOM   3029 O O     . ASP B 2 276 ? 140.682 100.389 100.361 1.00 160.11 ? 276 ASP A O     1 
ATOM   3030 C CB    . ASP B 2 276 ? 138.788 98.199  99.201  1.00 160.11 ? 276 ASP A CB    1 
ATOM   3031 C CG    . ASP B 2 276 ? 137.464 98.756  98.714  1.00 160.11 ? 276 ASP A CG    1 
ATOM   3032 O OD1   . ASP B 2 276 ? 136.832 99.542  99.451  1.00 160.11 ? 276 ASP A OD1   1 
ATOM   3033 O OD2   . ASP B 2 276 ? 137.054 98.402  97.589  1.00 160.11 ? 276 ASP A OD2   1 
ATOM   3034 N N     . SER B 2 277 ? 138.652 100.958 101.163 1.00 157.28 ? 277 SER A N     1 
ATOM   3035 C CA    . SER B 2 277 ? 139.007 102.326 101.504 1.00 157.28 ? 277 SER A CA    1 
ATOM   3036 C C     . SER B 2 277 ? 139.217 102.536 102.997 1.00 157.28 ? 277 SER A C     1 
ATOM   3037 O O     . SER B 2 277 ? 139.963 103.443 103.374 1.00 157.28 ? 277 SER A O     1 
ATOM   3038 C CB    . SER B 2 277 ? 137.928 103.300 101.023 1.00 157.28 ? 277 SER A CB    1 
ATOM   3039 O OG    . SER B 2 277 ? 137.585 103.049 99.678  1.00 157.28 ? 277 SER A OG    1 
ATOM   3040 N N     . PHE B 2 278 ? 138.566 101.745 103.856 1.00 156.70 ? 278 PHE A N     1 
ATOM   3041 C CA    . PHE B 2 278 ? 138.867 101.835 105.282 1.00 156.70 ? 278 PHE A CA    1 
ATOM   3042 C C     . PHE B 2 278 ? 140.331 101.515 105.561 1.00 156.70 ? 278 PHE A C     1 
ATOM   3043 O O     . PHE B 2 278 ? 140.900 102.009 106.540 1.00 156.70 ? 278 PHE A O     1 
ATOM   3044 C CB    . PHE B 2 278 ? 137.953 100.904 106.078 1.00 156.70 ? 278 PHE A CB    1 
ATOM   3045 C CG    . PHE B 2 278 ? 137.947 101.175 107.557 1.00 156.70 ? 278 PHE A CG    1 
ATOM   3046 C CD1   . PHE B 2 278 ? 137.065 102.092 108.103 1.00 156.70 ? 278 PHE A CD1   1 
ATOM   3047 C CD2   . PHE B 2 278 ? 138.818 100.506 108.402 1.00 156.70 ? 278 PHE A CD2   1 
ATOM   3048 C CE1   . PHE B 2 278 ? 137.056 102.342 109.461 1.00 156.70 ? 278 PHE A CE1   1 
ATOM   3049 C CE2   . PHE B 2 278 ? 138.814 100.752 109.761 1.00 156.70 ? 278 PHE A CE2   1 
ATOM   3050 C CZ    . PHE B 2 278 ? 137.931 101.671 110.291 1.00 156.70 ? 278 PHE A CZ    1 
ATOM   3051 N N     . LEU B 2 279 ? 140.951 100.687 104.719 1.00 154.53 ? 279 LEU A N     1 
ATOM   3052 C CA    . LEU B 2 279 ? 142.384 100.432 104.844 1.00 154.53 ? 279 LEU A CA    1 
ATOM   3053 C C     . LEU B 2 279 ? 143.215 101.528 104.189 1.00 154.53 ? 279 LEU A C     1 
ATOM   3054 O O     . LEU B 2 279 ? 144.331 101.818 104.643 1.00 154.53 ? 279 LEU A O     1 
ATOM   3055 C CB    . LEU B 2 279 ? 142.739 99.073  104.238 1.00 154.53 ? 279 LEU A CB    1 
ATOM   3056 C CG    . LEU B 2 279 ? 142.587 97.811  105.094 1.00 154.53 ? 279 LEU A CG    1 
ATOM   3057 C CD1   . LEU B 2 279 ? 143.593 97.822  106.234 1.00 154.53 ? 279 LEU A CD1   1 
ATOM   3058 C CD2   . LEU B 2 279 ? 141.171 97.639  105.625 1.00 154.53 ? 279 LEU A CD2   1 
ATOM   3059 N N     . TYR B 2 280 ? 142.694 102.150 103.130 1.00 153.30 ? 280 TYR A N     1 
ATOM   3060 C CA    . TYR B 2 280 ? 143.385 103.289 102.538 1.00 153.30 ? 280 TYR A CA    1 
ATOM   3061 C C     . TYR B 2 280 ? 143.406 104.472 103.495 1.00 153.30 ? 280 TYR A C     1 
ATOM   3062 O O     . TYR B 2 280 ? 144.319 105.301 103.443 1.00 153.30 ? 280 TYR A O     1 
ATOM   3063 C CB    . TYR B 2 280 ? 142.728 103.665 101.210 1.00 153.30 ? 280 TYR A CB    1 
ATOM   3064 C CG    . TYR B 2 280 ? 143.030 102.687 100.094 1.00 153.30 ? 280 TYR A CG    1 
ATOM   3065 C CD1   . TYR B 2 280 ? 142.386 102.777 98.867  1.00 153.30 ? 280 TYR A CD1   1 
ATOM   3066 C CD2   . TYR B 2 280 ? 143.963 101.671 100.270 1.00 153.30 ? 280 TYR A CD2   1 
ATOM   3067 C CE1   . TYR B 2 280 ? 142.667 101.887 97.846  1.00 153.30 ? 280 TYR A CE1   1 
ATOM   3068 C CE2   . TYR B 2 280 ? 144.246 100.774 99.258  1.00 153.30 ? 280 TYR A CE2   1 
ATOM   3069 C CZ    . TYR B 2 280 ? 143.595 100.886 98.048  1.00 153.30 ? 280 TYR A CZ    1 
ATOM   3070 O OH    . TYR B 2 280 ? 143.874 99.996  97.036  1.00 153.30 ? 280 TYR A OH    1 
ATOM   3071 N N     . LEU B 2 281 ? 142.407 104.568 104.370 1.00 146.35 ? 281 LEU A N     1 
ATOM   3072 C CA    . LEU B 2 281 ? 142.467 105.529 105.464 1.00 146.35 ? 281 LEU A CA    1 
ATOM   3073 C C     . LEU B 2 281 ? 143.536 105.165 106.484 1.00 146.35 ? 281 LEU A C     1 
ATOM   3074 O O     . LEU B 2 281 ? 143.822 105.968 107.376 1.00 146.35 ? 281 LEU A O     1 
ATOM   3075 C CB    . LEU B 2 281 ? 141.111 105.645 106.163 1.00 146.35 ? 281 LEU A CB    1 
ATOM   3076 C CG    . LEU B 2 281 ? 140.071 106.634 105.626 1.00 146.35 ? 281 LEU A CG    1 
ATOM   3077 C CD1   . LEU B 2 281 ? 139.806 106.456 104.142 1.00 146.35 ? 281 LEU A CD1   1 
ATOM   3078 C CD2   . LEU B 2 281 ? 138.780 106.503 106.418 1.00 146.35 ? 281 LEU A CD2   1 
ATOM   3079 N N     . ALA B 2 282 ? 144.123 103.975 106.380 1.00 148.42 ? 282 ALA A N     1 
ATOM   3080 C CA    . ALA B 2 282 ? 145.216 103.565 107.247 1.00 148.42 ? 282 ALA A CA    1 
ATOM   3081 C C     . ALA B 2 282 ? 146.543 103.441 106.512 1.00 148.42 ? 282 ALA A C     1 
ATOM   3082 O O     . ALA B 2 282 ? 147.553 103.112 107.142 1.00 148.42 ? 282 ALA A O     1 
ATOM   3083 C CB    . ALA B 2 282 ? 144.878 102.235 107.926 1.00 148.42 ? 282 ALA A CB    1 
ATOM   3084 N N     . ARG B 2 283 ? 146.563 103.675 105.197 1.00 145.31 ? 283 ARG A N     1 
ATOM   3085 C CA    . ARG B 2 283 ? 147.814 103.625 104.444 1.00 145.31 ? 283 ARG A CA    1 
ATOM   3086 C C     . ARG B 2 283 ? 148.845 104.601 105.014 1.00 145.31 ? 283 ARG A C     1 
ATOM   3087 O O     . ARG B 2 283 ? 149.960 104.197 105.361 1.00 145.31 ? 283 ARG A O     1 
ATOM   3088 C CB    . ARG B 2 283 ? 147.592 103.899 102.944 1.00 145.31 ? 283 ARG A CB    1 
ATOM   3089 C CG    . ARG B 2 283 ? 147.204 105.332 102.587 1.00 145.31 ? 283 ARG A CG    1 
ATOM   3090 C CD    . ARG B 2 283 ? 147.174 105.626 101.101 1.00 145.31 ? 283 ARG A CD    1 
ATOM   3091 N NE    . ARG B 2 283 ? 146.049 105.033 100.392 1.00 145.31 ? 283 ARG A NE    1 
ATOM   3092 C CZ    . ARG B 2 283 ? 145.891 105.123 99.077  1.00 145.31 ? 283 ARG A CZ    1 
ATOM   3093 N NH1   . ARG B 2 283 ? 146.783 105.783 98.351  1.00 145.31 ? 283 ARG A NH1   1 
ATOM   3094 N NH2   . ARG B 2 283 ? 144.845 104.570 98.486  1.00 145.31 ? 283 ARG A NH2   1 
ATOM   3095 N N     . SER B 2 284 ? 148.487 105.881 105.115 1.00 134.97 ? 284 SER A N     1 
ATOM   3096 C CA    . SER B 2 284 ? 149.421 106.960 105.392 1.00 134.97 ? 284 SER A CA    1 
ATOM   3097 C C     . SER B 2 284 ? 148.708 108.022 106.208 1.00 134.97 ? 284 SER A C     1 
ATOM   3098 O O     . SER B 2 284 ? 147.502 108.229 106.031 1.00 134.97 ? 284 SER A O     1 
ATOM   3099 C CB    . SER B 2 284 ? 149.969 107.571 104.095 1.00 134.97 ? 284 SER A CB    1 
ATOM   3100 O OG    . SER B 2 284 ? 150.730 108.735 104.360 1.00 134.97 ? 284 SER A OG    1 
ATOM   3101 N N     . PRO B 2 285 ? 149.421 108.714 107.100 1.00 128.73 ? 285 PRO A N     1 
ATOM   3102 C CA    . PRO B 2 285 ? 148.749 109.674 107.990 1.00 128.73 ? 285 PRO A CA    1 
ATOM   3103 C C     . PRO B 2 285 ? 148.068 110.830 107.275 1.00 128.73 ? 285 PRO A C     1 
ATOM   3104 O O     . PRO B 2 285 ? 147.196 111.464 107.875 1.00 128.73 ? 285 PRO A O     1 
ATOM   3105 C CB    . PRO B 2 285 ? 149.887 110.171 108.896 1.00 128.73 ? 285 PRO A CB    1 
ATOM   3106 C CG    . PRO B 2 285 ? 151.154 109.783 108.190 1.00 128.73 ? 285 PRO A CG    1 
ATOM   3107 C CD    . PRO B 2 285 ? 150.835 108.523 107.459 1.00 128.73 ? 285 PRO A CD    1 
ATOM   3108 N N     . TYR B 2 286 ? 148.422 111.131 106.025 1.00 124.01 ? 286 TYR A N     1 
ATOM   3109 C CA    . TYR B 2 286 ? 147.807 112.259 105.330 1.00 124.01 ? 286 TYR A CA    1 
ATOM   3110 C C     . TYR B 2 286 ? 146.309 112.039 105.139 1.00 124.01 ? 286 TYR A C     1 
ATOM   3111 O O     . TYR B 2 286 ? 145.476 112.814 105.635 1.00 124.01 ? 286 TYR A O     1 
ATOM   3112 C CB    . TYR B 2 286 ? 148.497 112.471 103.982 1.00 124.01 ? 286 TYR A CB    1 
ATOM   3113 C CG    . TYR B 2 286 ? 148.376 113.873 103.433 1.00 124.01 ? 286 TYR A CG    1 
ATOM   3114 C CD1   . TYR B 2 286 ? 147.254 114.264 102.719 1.00 124.01 ? 286 TYR A CD1   1 
ATOM   3115 C CD2   . TYR B 2 286 ? 149.389 114.800 103.620 1.00 124.01 ? 286 TYR A CD2   1 
ATOM   3116 C CE1   . TYR B 2 286 ? 147.141 115.539 102.214 1.00 124.01 ? 286 TYR A CE1   1 
ATOM   3117 C CE2   . TYR B 2 286 ? 149.285 116.078 103.117 1.00 124.01 ? 286 TYR A CE2   1 
ATOM   3118 C CZ    . TYR B 2 286 ? 148.160 116.441 102.416 1.00 124.01 ? 286 TYR A CZ    1 
ATOM   3119 O OH    . TYR B 2 286 ? 148.054 117.715 101.915 1.00 124.01 ? 286 TYR A OH    1 
ATOM   3120 N N     . ILE B 2 287 ? 145.952 110.980 104.412 1.00 123.14 ? 287 ILE A N     1 
ATOM   3121 C CA    . ILE B 2 287 ? 144.547 110.685 104.160 1.00 123.14 ? 287 ILE A CA    1 
ATOM   3122 C C     . ILE B 2 287 ? 143.838 110.351 105.464 1.00 123.14 ? 287 ILE A C     1 
ATOM   3123 O O     . ILE B 2 287 ? 142.646 110.632 105.630 1.00 123.14 ? 287 ILE A O     1 
ATOM   3124 C CB    . ILE B 2 287 ? 144.425 109.548 103.130 1.00 123.14 ? 287 ILE A CB    1 
ATOM   3125 C CG1   . ILE B 2 287 ? 145.150 109.930 101.840 1.00 123.14 ? 287 ILE A CG1   1 
ATOM   3126 C CG2   . ILE B 2 287 ? 142.970 109.243 102.830 1.00 123.14 ? 287 ILE A CG2   1 
ATOM   3127 C CD1   . ILE B 2 287 ? 144.588 111.161 101.172 1.00 123.14 ? 287 ILE A CD1   1 
ATOM   3128 N N     . LEU B 2 288 ? 144.567 109.774 106.422 1.00 120.81 ? 288 LEU A N     1 
ATOM   3129 C CA    . LEU B 2 288 ? 143.983 109.487 107.728 1.00 120.81 ? 288 LEU A CA    1 
ATOM   3130 C C     . LEU B 2 288 ? 143.534 110.766 108.422 1.00 120.81 ? 288 LEU A C     1 
ATOM   3131 O O     . LEU B 2 288 ? 142.395 110.864 108.889 1.00 120.81 ? 288 LEU A O     1 
ATOM   3132 C CB    . LEU B 2 288 ? 144.986 108.728 108.596 1.00 120.81 ? 288 LEU A CB    1 
ATOM   3133 C CG    . LEU B 2 288 ? 144.610 108.581 110.072 1.00 120.81 ? 288 LEU A CG    1 
ATOM   3134 C CD1   . LEU B 2 288 ? 143.398 107.681 110.226 1.00 120.81 ? 288 LEU A CD1   1 
ATOM   3135 C CD2   . LEU B 2 288 ? 145.783 108.049 110.877 1.00 120.81 ? 288 LEU A CD2   1 
ATOM   3136 N N     . LEU B 2 289 ? 144.422 111.758 108.507 1.00 111.70 ? 289 LEU A N     1 
ATOM   3137 C CA    . LEU B 2 289 ? 144.064 113.013 109.158 1.00 111.70 ? 289 LEU A CA    1 
ATOM   3138 C C     . LEU B 2 289 ? 142.972 113.744 108.393 1.00 111.70 ? 289 LEU A C     1 
ATOM   3139 O O     . LEU B 2 289 ? 142.115 114.395 109.000 1.00 111.70 ? 289 LEU A O     1 
ATOM   3140 C CB    . LEU B 2 289 ? 145.294 113.902 109.319 1.00 111.70 ? 289 LEU A CB    1 
ATOM   3141 C CG    . LEU B 2 289 ? 146.417 113.372 110.209 1.00 111.70 ? 289 LEU A CG    1 
ATOM   3142 C CD1   . LEU B 2 289 ? 147.622 114.291 110.149 1.00 111.70 ? 289 LEU A CD1   1 
ATOM   3143 C CD2   . LEU B 2 289 ? 145.937 113.204 111.641 1.00 111.70 ? 289 LEU A CD2   1 
ATOM   3144 N N     . LEU B 2 290 ? 142.980 113.657 107.062 1.00 113.53 ? 290 LEU A N     1 
ATOM   3145 C CA    . LEU B 2 290 ? 141.920 114.325 106.311 1.00 113.53 ? 290 LEU A CA    1 
ATOM   3146 C C     . LEU B 2 290 ? 140.569 113.667 106.572 1.00 113.53 ? 290 LEU A C     1 
ATOM   3147 O O     . LEU B 2 290 ? 139.548 114.355 106.721 1.00 113.53 ? 290 LEU A O     1 
ATOM   3148 C CB    . LEU B 2 290 ? 142.255 114.330 104.823 1.00 113.53 ? 290 LEU A CB    1 
ATOM   3149 C CG    . LEU B 2 290 ? 141.529 115.383 103.989 1.00 113.53 ? 290 LEU A CG    1 
ATOM   3150 C CD1   . LEU B 2 290 ? 142.444 115.889 102.891 1.00 113.53 ? 290 LEU A CD1   1 
ATOM   3151 C CD2   . LEU B 2 290 ? 140.246 114.826 103.402 1.00 113.53 ? 290 LEU A CD2   1 
ATOM   3152 N N     . ALA B 2 291 ? 140.546 112.334 106.646 1.00 112.07 ? 291 ALA A N     1 
ATOM   3153 C CA    . ALA B 2 291 ? 139.330 111.637 107.043 1.00 112.07 ? 291 ALA A CA    1 
ATOM   3154 C C     . ALA B 2 291 ? 138.915 112.030 108.449 1.00 112.07 ? 291 ALA A C     1 
ATOM   3155 O O     . ALA B 2 291 ? 137.722 112.142 108.742 1.00 112.07 ? 291 ALA A O     1 
ATOM   3156 C CB    . ALA B 2 291 ? 139.535 110.126 106.956 1.00 112.07 ? 291 ALA A CB    1 
ATOM   3157 N N     . LEU B 2 292 ? 139.889 112.222 109.339 1.00 106.89 ? 292 LEU A N     1 
ATOM   3158 C CA    . LEU B 2 292 ? 139.572 112.656 110.695 1.00 106.89 ? 292 LEU A CA    1 
ATOM   3159 C C     . LEU B 2 292 ? 138.897 114.018 110.682 1.00 106.89 ? 292 LEU A C     1 
ATOM   3160 O O     . LEU B 2 292 ? 137.921 114.239 111.404 1.00 106.89 ? 292 LEU A O     1 
ATOM   3161 C CB    . LEU B 2 292 ? 140.839 112.692 111.546 1.00 106.89 ? 292 LEU A CB    1 
ATOM   3162 C CG    . LEU B 2 292 ? 141.331 111.343 112.068 1.00 106.89 ? 292 LEU A CG    1 
ATOM   3163 C CD1   . LEU B 2 292 ? 142.515 111.531 112.999 1.00 106.89 ? 292 LEU A CD1   1 
ATOM   3164 C CD2   . LEU B 2 292 ? 140.206 110.603 112.769 1.00 106.89 ? 292 LEU A CD2   1 
ATOM   3165 N N     . LEU B 2 293 ? 139.399 114.937 109.858 1.00 101.20 ? 293 LEU A N     1 
ATOM   3166 C CA    . LEU B 2 293 ? 138.767 116.247 109.721 1.00 101.20 ? 293 LEU A CA    1 
ATOM   3167 C C     . LEU B 2 293 ? 137.329 116.116 109.236 1.00 101.20 ? 293 LEU A C     1 
ATOM   3168 O O     . LEU B 2 293 ? 136.410 116.718 109.805 1.00 101.20 ? 293 LEU A O     1 
ATOM   3169 C CB    . LEU B 2 293 ? 139.571 117.123 108.761 1.00 101.20 ? 293 LEU A CB    1 
ATOM   3170 C CG    . LEU B 2 293 ? 140.523 118.140 109.381 1.00 101.20 ? 293 LEU A CG    1 
ATOM   3171 C CD1   . LEU B 2 293 ? 141.634 117.433 110.116 1.00 101.20 ? 293 LEU A CD1   1 
ATOM   3172 C CD2   . LEU B 2 293 ? 141.088 119.051 108.311 1.00 101.20 ? 293 LEU A CD2   1 
ATOM   3173 N N     . VAL B 2 294 ? 137.117 115.331 108.177 1.00 104.30 ? 294 VAL A N     1 
ATOM   3174 C CA    . VAL B 2 294 ? 135.774 115.223 107.611 1.00 104.30 ? 294 VAL A CA    1 
ATOM   3175 C C     . VAL B 2 294 ? 134.819 114.569 108.603 1.00 104.30 ? 294 VAL A C     1 
ATOM   3176 O O     . VAL B 2 294 ? 133.680 115.022 108.780 1.00 104.30 ? 294 VAL A O     1 
ATOM   3177 C CB    . VAL B 2 294 ? 135.812 114.459 106.277 1.00 104.30 ? 294 VAL A CB    1 
ATOM   3178 C CG1   . VAL B 2 294 ? 134.422 114.398 105.672 1.00 104.30 ? 294 VAL A CG1   1 
ATOM   3179 C CG2   . VAL B 2 294 ? 136.776 115.126 105.320 1.00 104.30 ? 294 VAL A CG2   1 
ATOM   3180 N N     . ILE B 2 295 ? 135.264 113.501 109.265 1.00 102.86 ? 295 ILE A N     1 
ATOM   3181 C CA    . ILE B 2 295 ? 134.428 112.807 110.237 1.00 102.86 ? 295 ILE A CA    1 
ATOM   3182 C C     . ILE B 2 295 ? 134.113 113.714 111.417 1.00 102.86 ? 295 ILE A C     1 
ATOM   3183 O O     . ILE B 2 295 ? 132.977 113.749 111.904 1.00 102.86 ? 295 ILE A O     1 
ATOM   3184 C CB    . ILE B 2 295 ? 135.120 111.509 110.690 1.00 102.86 ? 295 ILE A CB    1 
ATOM   3185 C CG1   . ILE B 2 295 ? 135.109 110.474 109.566 1.00 102.86 ? 295 ILE A CG1   1 
ATOM   3186 C CG2   . ILE B 2 295 ? 134.454 110.948 111.930 1.00 102.86 ? 295 ILE A CG2   1 
ATOM   3187 C CD1   . ILE B 2 295 ? 135.920 109.240 109.874 1.00 102.86 ? 295 ILE A CD1   1 
ATOM   3188 N N     . ALA B 2 296 ? 135.109 114.462 111.895 1.00 96.22  ? 296 ALA A N     1 
ATOM   3189 C CA    . ALA B 2 296 ? 134.886 115.359 113.017 1.00 96.22  ? 296 ALA A CA    1 
ATOM   3190 C C     . ALA B 2 296 ? 133.887 116.444 112.657 1.00 96.22  ? 296 ALA A C     1 
ATOM   3191 O O     . ALA B 2 296 ? 133.023 116.789 113.467 1.00 96.22  ? 296 ALA A O     1 
ATOM   3192 C CB    . ALA B 2 296 ? 136.209 115.970 113.468 1.00 96.22  ? 296 ALA A CB    1 
ATOM   3193 N N     . TYR B 2 297 ? 133.976 116.987 111.442 1.00 97.12  ? 297 TYR A N     1 
ATOM   3194 C CA    . TYR B 2 297 ? 132.983 117.963 111.009 1.00 97.12  ? 297 TYR A CA    1 
ATOM   3195 C C     . TYR B 2 297 ? 131.594 117.341 110.977 1.00 97.12  ? 297 TYR A C     1 
ATOM   3196 O O     . TYR B 2 297 ? 130.623 117.918 111.483 1.00 97.12  ? 297 TYR A O     1 
ATOM   3197 C CB    . TYR B 2 297 ? 133.350 118.527 109.635 1.00 97.12  ? 297 TYR A CB    1 
ATOM   3198 C CG    . TYR B 2 297 ? 132.314 119.481 109.084 1.00 97.12  ? 297 TYR A CG    1 
ATOM   3199 C CD1   . TYR B 2 297 ? 132.370 120.836 109.373 1.00 97.12  ? 297 TYR A CD1   1 
ATOM   3200 C CD2   . TYR B 2 297 ? 131.278 119.028 108.278 1.00 97.12  ? 297 TYR A CD2   1 
ATOM   3201 C CE1   . TYR B 2 297 ? 131.426 121.712 108.880 1.00 97.12  ? 297 TYR A CE1   1 
ATOM   3202 C CE2   . TYR B 2 297 ? 130.328 119.897 107.781 1.00 97.12  ? 297 TYR A CE2   1 
ATOM   3203 C CZ    . TYR B 2 297 ? 130.409 121.238 108.084 1.00 97.12  ? 297 TYR A CZ    1 
ATOM   3204 O OH    . TYR B 2 297 ? 129.466 122.108 107.590 1.00 97.12  ? 297 TYR A OH    1 
ATOM   3205 N N     . GLY B 2 298 ? 131.481 116.161 110.367 1.00 97.18  ? 298 GLY A N     1 
ATOM   3206 C CA    . GLY B 2 298 ? 130.184 115.517 110.256 1.00 97.18  ? 298 GLY A CA    1 
ATOM   3207 C C     . GLY B 2 298 ? 129.551 115.227 111.601 1.00 97.18  ? 298 GLY A C     1 
ATOM   3208 O O     . GLY B 2 298 ? 128.331 115.307 111.754 1.00 97.18  ? 298 GLY A O     1 
ATOM   3209 N N     . ILE B 2 299 ? 130.369 114.887 112.595 1.00 93.27  ? 299 ILE A N     1 
ATOM   3210 C CA    . ILE B 2 299 ? 129.818 114.584 113.911 1.00 93.27  ? 299 ILE A CA    1 
ATOM   3211 C C     . ILE B 2 299 ? 129.511 115.861 114.681 1.00 93.27  ? 299 ILE A C     1 
ATOM   3212 O O     . ILE B 2 299 ? 128.498 115.942 115.384 1.00 93.27  ? 299 ILE A O     1 
ATOM   3213 C CB    . ILE B 2 299 ? 130.767 113.666 114.698 1.00 93.27  ? 299 ILE A CB    1 
ATOM   3214 C CG1   . ILE B 2 299 ? 131.049 112.391 113.910 1.00 93.27  ? 299 ILE A CG1   1 
ATOM   3215 C CG2   . ILE B 2 299 ? 130.151 113.302 116.026 1.00 93.27  ? 299 ILE A CG2   1 
ATOM   3216 C CD1   . ILE B 2 299 ? 131.934 111.413 114.641 1.00 93.27  ? 299 ILE A CD1   1 
ATOM   3217 N N     . CYS B 2 300 ? 130.370 116.877 114.569 1.00 93.61  ? 300 CYS A N     1 
ATOM   3218 C CA    . CYS B 2 300 ? 130.159 118.105 115.324 1.00 93.61  ? 300 CYS A CA    1 
ATOM   3219 C C     . CYS B 2 300 ? 128.934 118.860 114.832 1.00 93.61  ? 300 CYS A C     1 
ATOM   3220 O O     . CYS B 2 300 ? 128.214 119.466 115.632 1.00 93.61  ? 300 CYS A O     1 
ATOM   3221 C CB    . CYS B 2 300 ? 131.396 118.995 115.245 1.00 93.61  ? 300 CYS A CB    1 
ATOM   3222 S SG    . CYS B 2 300 ? 132.832 118.365 116.119 1.00 93.61  ? 300 CYS A SG    1 
ATOM   3223 N N     . ILE B 2 301 ? 128.674 118.840 113.524 1.00 93.80  ? 301 ILE A N     1 
ATOM   3224 C CA    . ILE B 2 301 ? 127.493 119.533 113.020 1.00 93.80  ? 301 ILE A CA    1 
ATOM   3225 C C     . ILE B 2 301 ? 126.220 118.850 113.501 1.00 93.80  ? 301 ILE A C     1 
ATOM   3226 O O     . ILE B 2 301 ? 125.208 119.512 113.759 1.00 93.80  ? 301 ILE A O     1 
ATOM   3227 C CB    . ILE B 2 301 ? 127.543 119.632 111.483 1.00 93.80  ? 301 ILE A CB    1 
ATOM   3228 C CG1   . ILE B 2 301 ? 128.790 120.401 111.048 1.00 93.80  ? 301 ILE A CG1   1 
ATOM   3229 C CG2   . ILE B 2 301 ? 126.299 120.312 110.944 1.00 93.80  ? 301 ILE A CG2   1 
ATOM   3230 C CD1   . ILE B 2 301 ? 128.869 121.801 111.607 1.00 93.80  ? 301 ILE A CD1   1 
ATOM   3231 N N     . ASN B 2 302 ? 126.250 117.527 113.657 1.00 93.30  ? 302 ASN A N     1 
ATOM   3232 C CA    . ASN B 2 302 ? 125.053 116.801 114.064 1.00 93.30  ? 302 ASN A CA    1 
ATOM   3233 C C     . ASN B 2 302 ? 124.847 116.822 115.572 1.00 93.30  ? 302 ASN A C     1 
ATOM   3234 O O     . ASN B 2 302 ? 123.703 116.757 116.033 1.00 93.30  ? 302 ASN A O     1 
ATOM   3235 C CB    . ASN B 2 302 ? 125.125 115.355 113.567 1.00 93.30  ? 302 ASN A CB    1 
ATOM   3236 C CG    . ASN B 2 302 ? 123.755 114.733 113.373 1.00 93.30  ? 302 ASN A CG    1 
ATOM   3237 O OD1   . ASN B 2 302 ? 122.810 115.034 114.102 1.00 93.30  ? 302 ASN A OD1   1 
ATOM   3238 N ND2   . ASN B 2 302 ? 123.642 113.855 112.385 1.00 93.30  ? 302 ASN A ND2   1 
ATOM   3239 N N     . LEU B 2 303 ? 125.927 116.901 116.354 1.00 88.55  ? 303 LEU A N     1 
ATOM   3240 C CA    . LEU B 2 303 ? 125.790 116.827 117.807 1.00 88.55  ? 303 LEU A CA    1 
ATOM   3241 C C     . LEU B 2 303 ? 124.946 117.971 118.350 1.00 88.55  ? 303 LEU A C     1 
ATOM   3242 O O     . LEU B 2 303 ? 124.172 117.787 119.296 1.00 88.55  ? 303 LEU A O     1 
ATOM   3243 C CB    . LEU B 2 303 ? 127.167 116.826 118.469 1.00 88.55  ? 303 LEU A CB    1 
ATOM   3244 C CG    . LEU B 2 303 ? 127.942 115.509 118.479 1.00 88.55  ? 303 LEU A CG    1 
ATOM   3245 C CD1   . LEU B 2 303 ? 129.014 115.544 119.547 1.00 88.55  ? 303 LEU A CD1   1 
ATOM   3246 C CD2   . LEU B 2 303 ? 127.015 114.324 118.683 1.00 88.55  ? 303 LEU A CD2   1 
ATOM   3247 N N     . ILE B 2 304 ? 125.078 119.160 117.764 1.00 87.55  ? 304 ILE A N     1 
ATOM   3248 C CA    . ILE B 2 304 ? 124.386 120.331 118.286 1.00 87.55  ? 304 ILE A CA    1 
ATOM   3249 C C     . ILE B 2 304 ? 122.973 120.463 117.741 1.00 87.55  ? 304 ILE A C     1 
ATOM   3250 O O     . ILE B 2 304 ? 122.133 121.112 118.376 1.00 87.55  ? 304 ILE A O     1 
ATOM   3251 C CB    . ILE B 2 304 ? 125.204 121.591 117.966 1.00 87.55  ? 304 ILE A CB    1 
ATOM   3252 C CG1   . ILE B 2 304 ? 126.692 121.293 118.145 1.00 87.55  ? 304 ILE A CG1   1 
ATOM   3253 C CG2   . ILE B 2 304 ? 124.789 122.743 118.855 1.00 87.55  ? 304 ILE A CG2   1 
ATOM   3254 C CD1   . ILE B 2 304 ? 127.611 122.322 117.548 1.00 87.55  ? 304 ILE A CD1   1 
ATOM   3255 N N     . GLU B 2 305 ? 122.684 119.855 116.589 1.00 90.73  ? 305 GLU A N     1 
ATOM   3256 C CA    . GLU B 2 305 ? 121.415 120.107 115.915 1.00 90.73  ? 305 GLU A CA    1 
ATOM   3257 C C     . GLU B 2 305 ? 120.237 119.531 116.687 1.00 90.73  ? 305 GLU A C     1 
ATOM   3258 O O     . GLU B 2 305 ? 119.169 120.144 116.732 1.00 90.73  ? 305 GLU A O     1 
ATOM   3259 C CB    . GLU B 2 305 ? 121.448 119.541 114.497 1.00 90.73  ? 305 GLU A CB    1 
ATOM   3260 C CG    . GLU B 2 305 ? 122.148 120.436 113.491 1.00 90.73  ? 305 GLU A CG    1 
ATOM   3261 C CD    . GLU B 2 305 ? 122.038 119.909 112.076 1.00 90.73  ? 305 GLU A CD    1 
ATOM   3262 O OE1   . GLU B 2 305 ? 121.429 118.836 111.889 1.00 90.73  ? 305 GLU A OE1   1 
ATOM   3263 O OE2   . GLU B 2 305 ? 122.558 120.569 111.151 1.00 90.73  ? 305 GLU A OE2   1 
ATOM   3264 N N     . VAL B 2 306 ? 120.401 118.360 117.299 1.00 83.70  ? 306 VAL A N     1 
ATOM   3265 C CA    . VAL B 2 306 ? 119.276 117.753 118.002 1.00 83.70  ? 306 VAL A CA    1 
ATOM   3266 C C     . VAL B 2 306 ? 118.925 118.557 119.246 1.00 83.70  ? 306 VAL A C     1 
ATOM   3267 O O     . VAL B 2 306 ? 117.746 118.793 119.539 1.00 83.70  ? 306 VAL A O     1 
ATOM   3268 C CB    . VAL B 2 306 ? 119.590 116.285 118.336 1.00 83.70  ? 306 VAL A CB    1 
ATOM   3269 C CG1   . VAL B 2 306 ? 118.678 115.779 119.438 1.00 83.70  ? 306 VAL A CG1   1 
ATOM   3270 C CG2   . VAL B 2 306 ? 119.441 115.432 117.093 1.00 83.70  ? 306 VAL A CG2   1 
ATOM   3271 N N     . THR B 2 307 ? 119.935 119.017 119.984 1.00 83.15  ? 307 THR A N     1 
ATOM   3272 C CA    . THR B 2 307 ? 119.668 119.854 121.148 1.00 83.15  ? 307 THR A CA    1 
ATOM   3273 C C     . THR B 2 307 ? 119.086 121.198 120.733 1.00 83.15  ? 307 THR A C     1 
ATOM   3274 O O     . THR B 2 307 ? 118.180 121.726 121.392 1.00 83.15  ? 307 THR A O     1 
ATOM   3275 C CB    . THR B 2 307 ? 120.947 120.046 121.958 1.00 83.15  ? 307 THR A CB    1 
ATOM   3276 O OG1   . THR B 2 307 ? 121.548 118.771 122.208 1.00 83.15  ? 307 THR A OG1   1 
ATOM   3277 C CG2   . THR B 2 307 ? 120.638 120.719 123.281 1.00 83.15  ? 307 THR A CG2   1 
ATOM   3278 N N     . TRP B 2 308 ? 119.579 121.759 119.627 1.00 79.58  ? 308 TRP A N     1 
ATOM   3279 C CA    . TRP B 2 308 ? 119.037 123.019 119.136 1.00 79.58  ? 308 TRP A CA    1 
ATOM   3280 C C     . TRP B 2 308 ? 117.581 122.864 118.726 1.00 79.58  ? 308 TRP A C     1 
ATOM   3281 O O     . TRP B 2 308 ? 116.756 123.744 118.987 1.00 79.58  ? 308 TRP A O     1 
ATOM   3282 C CB    . TRP B 2 308 ? 119.879 123.517 117.966 1.00 79.58  ? 308 TRP A CB    1 
ATOM   3283 C CG    . TRP B 2 308 ? 119.362 124.749 117.321 1.00 79.58  ? 308 TRP A CG    1 
ATOM   3284 C CD1   . TRP B 2 308 ? 119.135 125.950 117.916 1.00 79.58  ? 308 TRP A CD1   1 
ATOM   3285 C CD2   . TRP B 2 308 ? 119.021 124.912 115.944 1.00 79.58  ? 308 TRP A CD2   1 
ATOM   3286 N NE1   . TRP B 2 308 ? 118.671 126.853 116.995 1.00 79.58  ? 308 TRP A NE1   1 
ATOM   3287 C CE2   . TRP B 2 308 ? 118.590 126.238 115.774 1.00 79.58  ? 308 TRP A CE2   1 
ATOM   3288 C CE3   . TRP B 2 308 ? 119.036 124.062 114.836 1.00 79.58  ? 308 TRP A CE3   1 
ATOM   3289 C CZ2   . TRP B 2 308 ? 118.173 126.733 114.545 1.00 79.58  ? 308 TRP A CZ2   1 
ATOM   3290 C CZ3   . TRP B 2 308 ? 118.626 124.555 113.619 1.00 79.58  ? 308 TRP A CZ3   1 
ATOM   3291 C CH2   . TRP B 2 308 ? 118.200 125.877 113.482 1.00 79.58  ? 308 TRP A CH2   1 
ATOM   3292 N N     . LYS B 2 309 ? 117.235 121.741 118.106 1.00 78.84  ? 309 LYS A N     1 
ATOM   3293 C CA    . LYS B 2 309 ? 115.852 121.539 117.699 1.00 78.84  ? 309 LYS A CA    1 
ATOM   3294 C C     . LYS B 2 309 ? 114.960 121.233 118.893 1.00 78.84  ? 309 LYS A C     1 
ATOM   3295 O O     . LYS B 2 309 ? 113.767 121.551 118.870 1.00 78.84  ? 309 LYS A O     1 
ATOM   3296 C CB    . LYS B 2 309 ? 115.776 120.433 116.652 1.00 78.84  ? 309 LYS A CB    1 
ATOM   3297 C CG    . LYS B 2 309 ? 116.084 120.936 115.253 1.00 78.84  ? 309 LYS A CG    1 
ATOM   3298 C CD    . LYS B 2 309 ? 116.673 119.858 114.372 1.00 78.84  ? 309 LYS A CD    1 
ATOM   3299 C CE    . LYS B 2 309 ? 117.026 120.411 113.007 1.00 78.84  ? 309 LYS A CE    1 
ATOM   3300 N NZ    . LYS B 2 309 ? 117.838 119.445 112.225 1.00 78.84  ? 309 LYS A NZ    1 
ATOM   3301 N N     . SER B 2 310 ? 115.517 120.648 119.953 1.00 79.52  ? 310 SER A N     1 
ATOM   3302 C CA    . SER B 2 310 ? 114.765 120.552 121.200 1.00 79.52  ? 310 SER A CA    1 
ATOM   3303 C C     . SER B 2 310 ? 114.474 121.939 121.759 1.00 79.52  ? 310 SER A C     1 
ATOM   3304 O O     . SER B 2 310 ? 113.357 122.217 122.217 1.00 79.52  ? 310 SER A O     1 
ATOM   3305 C CB    . SER B 2 310 ? 115.534 119.712 122.215 1.00 79.52  ? 310 SER A CB    1 
ATOM   3306 O OG    . SER B 2 310 ? 116.682 120.402 122.669 1.00 79.52  ? 310 SER A OG    1 
ATOM   3307 N N     . GLN B 2 311 ? 115.467 122.829 121.719 1.00 79.37  ? 311 GLN A N     1 
ATOM   3308 C CA    . GLN B 2 311 ? 115.242 124.201 122.164 1.00 79.37  ? 311 GLN A CA    1 
ATOM   3309 C C     . GLN B 2 311 ? 114.211 124.904 121.288 1.00 79.37  ? 311 GLN A C     1 
ATOM   3310 O O     . GLN B 2 311 ? 113.435 125.734 121.773 1.00 79.37  ? 311 GLN A O     1 
ATOM   3311 C CB    . GLN B 2 311 ? 116.559 124.973 122.174 1.00 79.37  ? 311 GLN A CB    1 
ATOM   3312 C CG    . GLN B 2 311 ? 117.613 124.385 123.092 1.00 79.37  ? 311 GLN A CG    1 
ATOM   3313 C CD    . GLN B 2 311 ? 117.112 124.199 124.509 1.00 79.37  ? 311 GLN A CD    1 
ATOM   3314 O OE1   . GLN B 2 311 ? 116.961 125.163 125.256 1.00 79.37  ? 311 GLN A OE1   1 
ATOM   3315 N NE2   . GLN B 2 311 ? 116.851 122.955 124.886 1.00 79.37  ? 311 GLN A NE2   1 
ATOM   3316 N N     . LEU B 2 312 ? 114.189 124.583 119.995 1.00 75.70  ? 312 LEU A N     1 
ATOM   3317 C CA    . LEU B 2 312 ? 113.168 125.137 119.109 1.00 75.70  ? 312 LEU A CA    1 
ATOM   3318 C C     . LEU B 2 312 ? 111.778 124.634 119.468 1.00 75.70  ? 312 LEU A C     1 
ATOM   3319 O O     . LEU B 2 312 ? 110.820 125.412 119.498 1.00 75.70  ? 312 LEU A O     1 
ATOM   3320 C CB    . LEU B 2 312 ? 113.488 124.807 117.655 1.00 75.70  ? 312 LEU A CB    1 
ATOM   3321 C CG    . LEU B 2 312 ? 114.267 125.846 116.858 1.00 75.70  ? 312 LEU A CG    1 
ATOM   3322 C CD1   . LEU B 2 312 ? 115.621 126.083 117.441 1.00 75.70  ? 312 LEU A CD1   1 
ATOM   3323 C CD2   . LEU B 2 312 ? 114.396 125.357 115.433 1.00 75.70  ? 312 LEU A CD2   1 
ATOM   3324 N N     . LYS B 2 313 ? 111.642 123.332 119.719 1.00 75.56  ? 313 LYS A N     1 
ATOM   3325 C CA    . LYS B 2 313 ? 110.351 122.806 120.147 1.00 75.56  ? 313 LYS A CA    1 
ATOM   3326 C C     . LYS B 2 313 ? 109.910 123.447 121.451 1.00 75.56  ? 313 LYS A C     1 
ATOM   3327 O O     . LYS B 2 313 ? 108.711 123.629 121.691 1.00 75.56  ? 313 LYS A O     1 
ATOM   3328 C CB    . LYS B 2 313 ? 110.419 121.292 120.308 1.00 75.56  ? 313 LYS A CB    1 
ATOM   3329 C CG    . LYS B 2 313 ? 109.080 120.655 120.616 1.00 75.56  ? 313 LYS A CG    1 
ATOM   3330 C CD    . LYS B 2 313 ? 109.212 119.158 120.789 1.00 75.56  ? 313 LYS A CD    1 
ATOM   3331 C CE    . LYS B 2 313 ? 107.907 118.551 121.252 1.00 75.56  ? 313 LYS A CE    1 
ATOM   3332 N NZ    . LYS B 2 313 ? 106.781 119.001 120.398 1.00 75.56  ? 313 LYS A NZ    1 
ATOM   3333 N N     . LEU B 2 314 ? 110.866 123.789 122.313 1.00 78.16  ? 314 LEU A N     1 
ATOM   3334 C CA    . LEU B 2 314 ? 110.518 124.468 123.555 1.00 78.16  ? 314 LEU A CA    1 
ATOM   3335 C C     . LEU B 2 314 ? 110.049 125.892 123.290 1.00 78.16  ? 314 LEU A C     1 
ATOM   3336 O O     . LEU B 2 314 ? 109.055 126.344 123.868 1.00 78.16  ? 314 LEU A O     1 
ATOM   3337 C CB    . LEU B 2 314 ? 111.713 124.464 124.505 1.00 78.16  ? 314 LEU A CB    1 
ATOM   3338 C CG    . LEU B 2 314 ? 111.981 123.145 125.222 1.00 78.16  ? 314 LEU A CG    1 
ATOM   3339 C CD1   . LEU B 2 314 ? 113.164 123.282 126.160 1.00 78.16  ? 314 LEU A CD1   1 
ATOM   3340 C CD2   . LEU B 2 314 ? 110.744 122.700 125.975 1.00 78.16  ? 314 LEU A CD2   1 
ATOM   3341 N N     . GLN B 2 315 ? 110.752 126.612 122.417 1.00 76.86  ? 315 GLN A N     1 
ATOM   3342 C CA    . GLN B 2 315 ? 110.424 128.008 122.155 1.00 76.86  ? 315 GLN A CA    1 
ATOM   3343 C C     . GLN B 2 315 ? 109.212 128.143 121.244 1.00 76.86  ? 315 GLN A C     1 
ATOM   3344 O O     . GLN B 2 315 ? 108.372 129.025 121.452 1.00 76.86  ? 315 GLN A O     1 
ATOM   3345 C CB    . GLN B 2 315 ? 111.632 128.715 121.545 1.00 76.86  ? 315 GLN A CB    1 
ATOM   3346 C CG    . GLN B 2 315 ? 111.383 130.157 121.168 1.00 76.86  ? 315 GLN A CG    1 
ATOM   3347 C CD    . GLN B 2 315 ? 111.155 131.040 122.372 1.00 76.86  ? 315 GLN A CD    1 
ATOM   3348 O OE1   . GLN B 2 315 ? 111.673 130.779 123.455 1.00 76.86  ? 315 GLN A OE1   1 
ATOM   3349 N NE2   . GLN B 2 315 ? 110.373 132.094 122.190 1.00 76.86  ? 315 GLN A NE2   1 
ATOM   3350 N N     . TYR B 2 316 ? 109.102 127.283 120.233 1.00 75.45  ? 316 TYR A N     1 
ATOM   3351 C CA    . TYR B 2 316 ? 108.011 127.321 119.264 1.00 75.45  ? 316 TYR A CA    1 
ATOM   3352 C C     . TYR B 2 316 ? 107.208 126.032 119.368 1.00 75.45  ? 316 TYR A C     1 
ATOM   3353 O O     . TYR B 2 316 ? 107.484 125.062 118.649 1.00 75.45  ? 316 TYR A O     1 
ATOM   3354 C CB    . TYR B 2 316 ? 108.559 127.510 117.850 1.00 75.45  ? 316 TYR A CB    1 
ATOM   3355 C CG    . TYR B 2 316 ? 109.481 128.696 117.721 1.00 75.45  ? 316 TYR A CG    1 
ATOM   3356 C CD1   . TYR B 2 316 ? 108.986 129.989 117.765 1.00 75.45  ? 316 TYR A CD1   1 
ATOM   3357 C CD2   . TYR B 2 316 ? 110.845 128.524 117.559 1.00 75.45  ? 316 TYR A CD2   1 
ATOM   3358 C CE1   . TYR B 2 316 ? 109.822 131.074 117.651 1.00 75.45  ? 316 TYR A CE1   1 
ATOM   3359 C CE2   . TYR B 2 316 ? 111.688 129.605 117.443 1.00 75.45  ? 316 TYR A CE2   1 
ATOM   3360 C CZ    . TYR B 2 316 ? 111.170 130.877 117.490 1.00 75.45  ? 316 TYR A CZ    1 
ATOM   3361 O OH    . TYR B 2 316 ? 112.005 131.960 117.374 1.00 75.45  ? 316 TYR A OH    1 
ATOM   3362 N N     . PRO B 2 317 ? 106.208 125.968 120.243 1.00 76.85  ? 317 PRO A N     1 
ATOM   3363 C CA    . PRO B 2 317 ? 105.499 124.703 120.474 1.00 76.85  ? 317 PRO A CA    1 
ATOM   3364 C C     . PRO B 2 317 ? 104.713 124.206 119.272 1.00 76.85  ? 317 PRO A C     1 
ATOM   3365 O O     . PRO B 2 317 ? 104.832 123.037 118.893 1.00 76.85  ? 317 PRO A O     1 
ATOM   3366 C CB    . PRO B 2 317 ? 104.562 125.038 121.641 1.00 76.85  ? 317 PRO A CB    1 
ATOM   3367 C CG    . PRO B 2 317 ? 105.152 126.250 122.274 1.00 76.85  ? 317 PRO A CG    1 
ATOM   3368 C CD    . PRO B 2 317 ? 105.757 127.026 121.157 1.00 76.85  ? 317 PRO A CD    1 
ATOM   3369 N N     . ASN B 2 318 ? 103.906 125.072 118.668 1.00 79.13  ? 318 ASN A N     1 
ATOM   3370 C CA    . ASN B 2 318 ? 103.043 124.649 117.578 1.00 79.13  ? 318 ASN A CA    1 
ATOM   3371 C C     . ASN B 2 318 ? 103.819 124.583 116.268 1.00 79.13  ? 318 ASN A C     1 
ATOM   3372 O O     . ASN B 2 318 ? 104.896 125.164 116.120 1.00 79.13  ? 318 ASN A O     1 
ATOM   3373 C CB    . ASN B 2 318 ? 101.856 125.595 117.435 1.00 79.13  ? 318 ASN A CB    1 
ATOM   3374 C CG    . ASN B 2 318 ? 102.282 127.028 117.298 1.00 79.13  ? 318 ASN A CG    1 
ATOM   3375 O OD1   . ASN B 2 318 ? 103.365 127.401 117.740 1.00 79.13  ? 318 ASN A OD1   1 
ATOM   3376 N ND2   . ASN B 2 318 ? 101.437 127.846 116.685 1.00 79.13  ? 318 ASN A ND2   1 
ATOM   3377 N N     . MET B 2 319 ? 103.247 123.858 115.304 1.00 80.34  ? 319 MET A N     1 
ATOM   3378 C CA    . MET B 2 319 ? 103.954 123.599 114.056 1.00 80.34  ? 319 MET A CA    1 
ATOM   3379 C C     . MET B 2 319 ? 104.074 124.847 113.196 1.00 80.34  ? 319 MET A C     1 
ATOM   3380 O O     . MET B 2 319 ? 105.028 124.970 112.422 1.00 80.34  ? 319 MET A O     1 
ATOM   3381 C CB    . MET B 2 319 ? 103.250 122.494 113.272 1.00 80.34  ? 319 MET A CB    1 
ATOM   3382 C CG    . MET B 2 319 ? 103.215 121.153 113.976 1.00 80.34  ? 319 MET A CG    1 
ATOM   3383 S SD    . MET B 2 319 ? 103.299 119.782 112.818 1.00 80.34  ? 319 MET A SD    1 
ATOM   3384 C CE    . MET B 2 319 ? 102.687 118.445 113.832 1.00 80.34  ? 319 MET A CE    1 
ATOM   3385 N N     . ASN B 2 320 ? 103.133 125.784 113.316 1.00 81.39  ? 320 ASN A N     1 
ATOM   3386 C CA    . ASN B 2 320 ? 103.166 126.965 112.460 1.00 81.39  ? 320 ASN A CA    1 
ATOM   3387 C C     . ASN B 2 320 ? 104.326 127.880 112.824 1.00 81.39  ? 320 ASN A C     1 
ATOM   3388 O O     . ASN B 2 320 ? 105.063 128.338 111.947 1.00 81.39  ? 320 ASN A O     1 
ATOM   3389 C CB    . ASN B 2 320 ? 101.841 127.713 112.546 1.00 81.39  ? 320 ASN A CB    1 
ATOM   3390 C CG    . ASN B 2 320 ? 100.800 127.145 111.618 1.00 81.39  ? 320 ASN A CG    1 
ATOM   3391 O OD1   . ASN B 2 320 ? 100.065 126.232 111.982 1.00 81.39  ? 320 ASN A OD1   1 
ATOM   3392 N ND2   . ASN B 2 320 ? 100.734 127.678 110.406 1.00 81.39  ? 320 ASN A ND2   1 
ATOM   3393 N N     . ASP B 2 321 ? 104.516 128.149 114.116 1.00 79.58  ? 321 ASP A N     1 
ATOM   3394 C CA    . ASP B 2 321 ? 105.639 128.987 114.520 1.00 79.58  ? 321 ASP A CA    1 
ATOM   3395 C C     . ASP B 2 321 ? 106.971 128.277 114.324 1.00 79.58  ? 321 ASP A C     1 
ATOM   3396 O O     . ASP B 2 321 ? 107.966 128.923 113.985 1.00 79.58  ? 321 ASP A O     1 
ATOM   3397 C CB    . ASP B 2 321 ? 105.472 129.438 115.969 1.00 79.58  ? 321 ASP A CB    1 
ATOM   3398 C CG    . ASP B 2 321 ? 104.264 130.335 116.162 1.00 79.58  ? 321 ASP A CG    1 
ATOM   3399 O OD1   . ASP B 2 321 ? 103.259 129.882 116.744 1.00 79.58  ? 321 ASP A OD1   1 
ATOM   3400 O OD2   . ASP B 2 321 ? 104.320 131.505 115.732 1.00 79.58  ? 321 ASP A OD2   1 
ATOM   3401 N N     . TYR B 2 322 ? 107.011 126.957 114.511 1.00 75.17  ? 322 TYR A N     1 
ATOM   3402 C CA    . TYR B 2 322 ? 108.231 126.211 114.218 1.00 75.17  ? 322 TYR A CA    1 
ATOM   3403 C C     . TYR B 2 322 ? 108.595 126.329 112.745 1.00 75.17  ? 322 TYR A C     1 
ATOM   3404 O O     . TYR B 2 322 ? 109.750 126.595 112.397 1.00 75.17  ? 322 TYR A O     1 
ATOM   3405 C CB    . TYR B 2 322 ? 108.060 124.746 114.621 1.00 75.17  ? 322 TYR A CB    1 
ATOM   3406 C CG    . TYR B 2 322 ? 109.351 123.957 114.719 1.00 75.17  ? 322 TYR A CG    1 
ATOM   3407 C CD1   . TYR B 2 322 ? 110.152 123.750 113.609 1.00 75.17  ? 322 TYR A CD1   1 
ATOM   3408 C CD2   . TYR B 2 322 ? 109.759 123.412 115.921 1.00 75.17  ? 322 TYR A CD2   1 
ATOM   3409 C CE1   . TYR B 2 322 ? 111.319 123.035 113.696 1.00 75.17  ? 322 TYR A CE1   1 
ATOM   3410 C CE2   . TYR B 2 322 ? 110.927 122.695 116.015 1.00 75.17  ? 322 TYR A CE2   1 
ATOM   3411 C CZ    . TYR B 2 322 ? 111.701 122.510 114.899 1.00 75.17  ? 322 TYR A CZ    1 
ATOM   3412 O OH    . TYR B 2 322 ? 112.869 121.794 114.981 1.00 75.17  ? 322 TYR A OH    1 
ATOM   3413 N N     . SER B 2 323 ? 107.617 126.134 111.861 1.00 76.67  ? 323 SER A N     1 
ATOM   3414 C CA    . SER B 2 323 ? 107.891 126.223 110.433 1.00 76.67  ? 323 SER A CA    1 
ATOM   3415 C C     . SER B 2 323 ? 108.237 127.646 110.027 1.00 76.67  ? 323 SER A C     1 
ATOM   3416 O O     . SER B 2 323 ? 109.060 127.855 109.133 1.00 76.67  ? 323 SER A O     1 
ATOM   3417 C CB    . SER B 2 323 ? 106.696 125.715 109.633 1.00 76.67  ? 323 SER A CB    1 
ATOM   3418 O OG    . SER B 2 323 ? 107.011 125.647 108.255 1.00 76.67  ? 323 SER A OG    1 
ATOM   3419 N N     . GLU B 2 324 ? 107.630 128.641 110.674 1.00 79.36  ? 324 GLU A N     1 
ATOM   3420 C CA    . GLU B 2 324 ? 107.970 130.023 110.364 1.00 79.36  ? 324 GLU A CA    1 
ATOM   3421 C C     . GLU B 2 324 ? 109.395 130.343 110.790 1.00 79.36  ? 324 GLU A C     1 
ATOM   3422 O O     . GLU B 2 324 ? 110.124 131.042 110.075 1.00 79.36  ? 324 GLU A O     1 
ATOM   3423 C CB    . GLU B 2 324 ? 106.982 130.971 111.037 1.00 79.36  ? 324 GLU A CB    1 
ATOM   3424 C CG    . GLU B 2 324 ? 107.253 132.434 110.766 1.00 79.36  ? 324 GLU A CG    1 
ATOM   3425 C CD    . GLU B 2 324 ? 106.433 133.351 111.646 1.00 79.36  ? 324 GLU A CD    1 
ATOM   3426 O OE1   . GLU B 2 324 ? 105.514 132.858 112.330 1.00 79.36  ? 324 GLU A OE1   1 
ATOM   3427 O OE2   . GLU B 2 324 ? 106.705 134.569 111.651 1.00 79.36  ? 324 GLU A OE2   1 
ATOM   3428 N N     . PHE B 2 325 ? 109.819 129.832 111.947 1.00 77.53  ? 325 PHE A N     1 
ATOM   3429 C CA    . PHE B 2 325 ? 111.205 130.027 112.348 1.00 77.53  ? 325 PHE A CA    1 
ATOM   3430 C C     . PHE B 2 325 ? 112.151 129.306 111.406 1.00 77.53  ? 325 PHE A C     1 
ATOM   3431 O O     . PHE B 2 325 ? 113.228 129.818 111.101 1.00 77.53  ? 325 PHE A O     1 
ATOM   3432 C CB    . PHE B 2 325 ? 111.447 129.553 113.777 1.00 77.53  ? 325 PHE A CB    1 
ATOM   3433 C CG    . PHE B 2 325 ? 112.890 129.642 114.192 1.00 77.53  ? 325 PHE A CG    1 
ATOM   3434 C CD1   . PHE B 2 325 ? 113.413 130.828 114.670 1.00 77.53  ? 325 PHE A CD1   1 
ATOM   3435 C CD2   . PHE B 2 325 ? 113.728 128.548 114.081 1.00 77.53  ? 325 PHE A CD2   1 
ATOM   3436 C CE1   . PHE B 2 325 ? 114.738 130.916 115.041 1.00 77.53  ? 325 PHE A CE1   1 
ATOM   3437 C CE2   . PHE B 2 325 ? 115.053 128.636 114.446 1.00 77.53  ? 325 PHE A CE2   1 
ATOM   3438 C CZ    . PHE B 2 325 ? 115.556 129.819 114.929 1.00 77.53  ? 325 PHE A CZ    1 
ATOM   3439 N N     . MET B 2 326 ? 111.781 128.109 110.950 1.00 79.43  ? 326 MET A N     1 
ATOM   3440 C CA    . MET B 2 326 ? 112.640 127.397 110.010 1.00 79.43  ? 326 MET A CA    1 
ATOM   3441 C C     . MET B 2 326 ? 112.716 128.131 108.680 1.00 79.43  ? 326 MET A C     1 
ATOM   3442 O O     . MET B 2 326 ? 113.762 128.138 108.025 1.00 79.43  ? 326 MET A O     1 
ATOM   3443 C CB    . MET B 2 326 ? 112.144 125.967 109.814 1.00 79.43  ? 326 MET A CB    1 
ATOM   3444 C CG    . MET B 2 326 ? 112.357 125.074 111.020 1.00 79.43  ? 326 MET A CG    1 
ATOM   3445 S SD    . MET B 2 326 ? 114.045 125.126 111.649 1.00 79.43  ? 326 MET A SD    1 
ATOM   3446 C CE    . MET B 2 326 ? 114.924 124.272 110.347 1.00 79.43  ? 326 MET A CE    1 
ATOM   3447 N N     . GLY B 2 327 ? 111.627 128.783 108.280 1.00 77.34  ? 327 GLY A N     1 
ATOM   3448 C CA    . GLY B 2 327 ? 111.665 129.593 107.076 1.00 77.34  ? 327 GLY A CA    1 
ATOM   3449 C C     . GLY B 2 327 ? 112.561 130.805 107.221 1.00 77.34  ? 327 GLY A C     1 
ATOM   3450 O O     . GLY B 2 327 ? 113.352 131.114 106.329 1.00 77.34  ? 327 GLY A O     1 
ATOM   3451 N N     . ASN B 2 328 ? 112.447 131.512 108.346 1.00 78.32  ? 328 ASN A N     1 
ATOM   3452 C CA    . ASN B 2 328 ? 113.335 132.646 108.590 1.00 78.32  ? 328 ASN A CA    1 
ATOM   3453 C C     . ASN B 2 328 ? 114.784 132.192 108.690 1.00 78.32  ? 328 ASN A C     1 
ATOM   3454 O O     . ASN B 2 328 ? 115.697 132.884 108.225 1.00 78.32  ? 328 ASN A O     1 
ATOM   3455 C CB    . ASN B 2 328 ? 112.912 133.378 109.860 1.00 78.32  ? 328 ASN A CB    1 
ATOM   3456 C CG    . ASN B 2 328 ? 111.785 134.353 109.618 1.00 78.32  ? 328 ASN A CG    1 
ATOM   3457 O OD1   . ASN B 2 328 ? 111.811 135.120 108.658 1.00 78.32  ? 328 ASN A OD1   1 
ATOM   3458 N ND2   . ASN B 2 328 ? 110.784 134.329 110.487 1.00 78.32  ? 328 ASN A ND2   1 
ATOM   3459 N N     . PHE B 2 329 ? 115.011 131.024 109.287 1.00 77.38  ? 329 PHE A N     1 
ATOM   3460 C CA    . PHE B 2 329 ? 116.355 130.478 109.408 1.00 77.38  ? 329 PHE A CA    1 
ATOM   3461 C C     . PHE B 2 329 ? 116.927 130.133 108.043 1.00 77.38  ? 329 PHE A C     1 
ATOM   3462 O O     . PHE B 2 329 ? 118.106 130.378 107.778 1.00 77.38  ? 329 PHE A O     1 
ATOM   3463 C CB    . PHE B 2 329 ? 116.315 129.252 110.320 1.00 77.38  ? 329 PHE A CB    1 
ATOM   3464 C CG    . PHE B 2 329 ? 117.580 128.451 110.334 1.00 77.38  ? 329 PHE A CG    1 
ATOM   3465 C CD1   . PHE B 2 329 ? 118.671 128.869 111.067 1.00 77.38  ? 329 PHE A CD1   1 
ATOM   3466 C CD2   . PHE B 2 329 ? 117.668 127.265 109.632 1.00 77.38  ? 329 PHE A CD2   1 
ATOM   3467 C CE1   . PHE B 2 329 ? 119.825 128.128 111.087 1.00 77.38  ? 329 PHE A CE1   1 
ATOM   3468 C CE2   . PHE B 2 329 ? 118.823 126.524 109.648 1.00 77.38  ? 329 PHE A CE2   1 
ATOM   3469 C CZ    . PHE B 2 329 ? 119.901 126.956 110.375 1.00 77.38  ? 329 PHE A CZ    1 
ATOM   3470 N N     . SER B 2 330 ? 116.099 129.585 107.153 1.00 76.93  ? 330 SER A N     1 
ATOM   3471 C CA    . SER B 2 330 ? 116.552 129.322 105.793 1.00 76.93  ? 330 SER A CA    1 
ATOM   3472 C C     . SER B 2 330 ? 116.844 130.619 105.054 1.00 76.93  ? 330 SER A C     1 
ATOM   3473 O O     . SER B 2 330 ? 117.852 130.728 104.344 1.00 76.93  ? 330 SER A O     1 
ATOM   3474 C CB    . SER B 2 330 ? 115.503 128.504 105.047 1.00 76.93  ? 330 SER A CB    1 
ATOM   3475 O OG    . SER B 2 330 ? 115.302 127.250 105.669 1.00 76.93  ? 330 SER A OG    1 
ATOM   3476 N N     . PHE B 2 331 ? 115.976 131.617 105.215 1.00 76.77  ? 331 PHE A N     1 
ATOM   3477 C CA    . PHE B 2 331 ? 116.198 132.906 104.572 1.00 76.77  ? 331 PHE A CA    1 
ATOM   3478 C C     . PHE B 2 331 ? 117.517 133.522 105.013 1.00 76.77  ? 331 PHE A C     1 
ATOM   3479 O O     . PHE B 2 331 ? 118.287 134.023 104.187 1.00 76.77  ? 331 PHE A O     1 
ATOM   3480 C CB    . PHE B 2 331 ? 115.038 133.852 104.879 1.00 76.77  ? 331 PHE A CB    1 
ATOM   3481 C CG    . PHE B 2 331 ? 115.151 135.186 104.207 1.00 76.77  ? 331 PHE A CG    1 
ATOM   3482 C CD1   . PHE B 2 331 ? 114.687 135.366 102.919 1.00 76.77  ? 331 PHE A CD1   1 
ATOM   3483 C CD2   . PHE B 2 331 ? 115.718 136.261 104.862 1.00 76.77  ? 331 PHE A CD2   1 
ATOM   3484 C CE1   . PHE B 2 331 ? 114.792 136.589 102.299 1.00 76.77  ? 331 PHE A CE1   1 
ATOM   3485 C CE2   . PHE B 2 331 ? 115.825 137.484 104.244 1.00 76.77  ? 331 PHE A CE2   1 
ATOM   3486 C CZ    . PHE B 2 331 ? 115.362 137.649 102.963 1.00 76.77  ? 331 PHE A CZ    1 
ATOM   3487 N N     . TRP B 2 332 ? 117.805 133.482 106.311 1.00 77.80  ? 332 TRP A N     1 
ATOM   3488 C CA    . TRP B 2 332 ? 119.020 134.123 106.793 1.00 77.80  ? 332 TRP A CA    1 
ATOM   3489 C C     . TRP B 2 332 ? 120.254 133.276 106.526 1.00 77.80  ? 332 TRP A C     1 
ATOM   3490 O O     . TRP B 2 332 ? 121.346 133.825 106.355 1.00 77.80  ? 332 TRP A O     1 
ATOM   3491 C CB    . TRP B 2 332 ? 118.883 134.455 108.275 1.00 77.80  ? 332 TRP A CB    1 
ATOM   3492 C CG    . TRP B 2 332 ? 118.007 135.639 108.477 1.00 77.80  ? 332 TRP A CG    1 
ATOM   3493 C CD1   . TRP B 2 332 ? 116.760 135.653 109.019 1.00 77.80  ? 332 TRP A CD1   1 
ATOM   3494 C CD2   . TRP B 2 332 ? 118.294 136.986 108.094 1.00 77.80  ? 332 TRP A CD2   1 
ATOM   3495 N NE1   . TRP B 2 332 ? 116.258 136.930 109.018 1.00 77.80  ? 332 TRP A NE1   1 
ATOM   3496 C CE2   . TRP B 2 332 ? 117.183 137.767 108.454 1.00 77.80  ? 332 TRP A CE2   1 
ATOM   3497 C CE3   . TRP B 2 332 ? 119.389 137.610 107.494 1.00 77.80  ? 332 TRP A CE3   1 
ATOM   3498 C CZ2   . TRP B 2 332 ? 117.135 139.138 108.232 1.00 77.80  ? 332 TRP A CZ2   1 
ATOM   3499 C CZ3   . TRP B 2 332 ? 119.339 138.968 107.274 1.00 77.80  ? 332 TRP A CZ3   1 
ATOM   3500 C CH2   . TRP B 2 332 ? 118.221 139.718 107.642 1.00 77.80  ? 332 TRP A CH2   1 
ATOM   3501 N N     . THR B 2 333 ? 120.104 131.953 106.455 1.00 79.48  ? 333 THR A N     1 
ATOM   3502 C CA    . THR B 2 333 ? 121.177 131.125 105.926 1.00 79.48  ? 333 THR A CA    1 
ATOM   3503 C C     . THR B 2 333 ? 121.514 131.534 104.503 1.00 79.48  ? 333 THR A C     1 
ATOM   3504 O O     . THR B 2 333 ? 122.688 131.635 104.140 1.00 79.48  ? 333 THR A O     1 
ATOM   3505 C CB    . THR B 2 333 ? 120.781 129.652 105.977 1.00 79.48  ? 333 THR A CB    1 
ATOM   3506 O OG1   . THR B 2 333 ? 120.318 129.327 107.291 1.00 79.48  ? 333 THR A OG1   1 
ATOM   3507 C CG2   . THR B 2 333 ? 121.969 128.777 105.639 1.00 79.48  ? 333 THR A CG2   1 
ATOM   3508 N N     . GLY B 2 334 ? 120.492 131.798 103.689 1.00 80.86  ? 334 GLY A N     1 
ATOM   3509 C CA    . GLY B 2 334 ? 120.739 132.265 102.336 1.00 80.86  ? 334 GLY A CA    1 
ATOM   3510 C C     . GLY B 2 334 ? 121.407 133.626 102.300 1.00 80.86  ? 334 GLY A C     1 
ATOM   3511 O O     . GLY B 2 334 ? 122.307 133.865 101.492 1.00 80.86  ? 334 GLY A O     1 
ATOM   3512 N N     . VAL B 2 335 ? 120.972 134.538 103.170 1.00 81.04  ? 335 VAL A N     1 
ATOM   3513 C CA    . VAL B 2 335 ? 121.573 135.871 103.214 1.00 81.04  ? 335 VAL A CA    1 
ATOM   3514 C C     . VAL B 2 335 ? 123.050 135.778 103.574 1.00 81.04  ? 335 VAL A C     1 
ATOM   3515 O O     . VAL B 2 335 ? 123.910 136.377 102.917 1.00 81.04  ? 335 VAL A O     1 
ATOM   3516 C CB    . VAL B 2 335 ? 120.817 136.777 104.201 1.00 81.04  ? 335 VAL A CB    1 
ATOM   3517 C CG1   . VAL B 2 335 ? 121.522 138.111 104.330 1.00 81.04  ? 335 VAL A CG1   1 
ATOM   3518 C CG2   . VAL B 2 335 ? 119.393 136.989 103.749 1.00 81.04  ? 335 VAL A CG2   1 
ATOM   3519 N N     . VAL B 2 336 ? 123.366 135.025 104.628 1.00 84.75  ? 336 VAL A N     1 
ATOM   3520 C CA    . VAL B 2 336 ? 124.753 134.903 105.057 1.00 84.75  ? 336 VAL A CA    1 
ATOM   3521 C C     . VAL B 2 336 ? 125.571 134.150 104.017 1.00 84.75  ? 336 VAL A C     1 
ATOM   3522 O O     . VAL B 2 336 ? 126.754 134.441 103.813 1.00 84.75  ? 336 VAL A O     1 
ATOM   3523 C CB    . VAL B 2 336 ? 124.825 134.235 106.441 1.00 84.75  ? 336 VAL A CB    1 
ATOM   3524 C CG1   . VAL B 2 336 ? 126.266 134.056 106.874 1.00 84.75  ? 336 VAL A CG1   1 
ATOM   3525 C CG2   . VAL B 2 336 ? 124.073 135.068 107.458 1.00 84.75  ? 336 VAL A CG2   1 
ATOM   3526 N N     . SER B 2 337 ? 124.956 133.195 103.317 1.00 87.90  ? 337 SER A N     1 
ATOM   3527 C CA    . SER B 2 337 ? 125.671 132.480 102.269 1.00 87.90  ? 337 SER A CA    1 
ATOM   3528 C C     . SER B 2 337 ? 126.008 133.402 101.107 1.00 87.90  ? 337 SER A C     1 
ATOM   3529 O O     . SER B 2 337 ? 127.106 133.327 100.548 1.00 87.90  ? 337 SER A O     1 
ATOM   3530 C CB    . SER B 2 337 ? 124.840 131.294 101.786 1.00 87.90  ? 337 SER A CB    1 
ATOM   3531 O OG    . SER B 2 337 ? 124.635 130.359 102.827 1.00 87.90  ? 337 SER A OG    1 
ATOM   3532 N N     . VAL B 2 338 ? 125.074 134.272 100.722 1.00 90.07  ? 338 VAL A N     1 
ATOM   3533 C CA    . VAL B 2 338 ? 125.359 135.243 99.670  1.00 90.07  ? 338 VAL A CA    1 
ATOM   3534 C C     . VAL B 2 338 ? 126.469 136.184 100.111 1.00 90.07  ? 338 VAL A C     1 
ATOM   3535 O O     . VAL B 2 338 ? 127.401 136.471 99.348  1.00 90.07  ? 338 VAL A O     1 
ATOM   3536 C CB    . VAL B 2 338 ? 124.084 136.017 99.289  1.00 90.07  ? 338 VAL A CB    1 
ATOM   3537 C CG1   . VAL B 2 338 ? 124.421 137.136 98.319  1.00 90.07  ? 338 VAL A CG1   1 
ATOM   3538 C CG2   . VAL B 2 338 ? 123.062 135.087 98.674  1.00 90.07  ? 338 VAL A CG2   1 
ATOM   3539 N N     . LEU B 2 339 ? 126.388 136.677 101.348 1.00 95.16  ? 339 LEU A N     1 
ATOM   3540 C CA    . LEU B 2 339 ? 127.428 137.568 101.853 1.00 95.16  ? 339 LEU A CA    1 
ATOM   3541 C C     . LEU B 2 339 ? 128.790 136.890 101.830 1.00 95.16  ? 339 LEU A C     1 
ATOM   3542 O O     . LEU B 2 339 ? 129.794 137.508 101.458 1.00 95.16  ? 339 LEU A O     1 
ATOM   3543 C CB    . LEU B 2 339 ? 127.082 138.030 103.267 1.00 95.16  ? 339 LEU A CB    1 
ATOM   3544 C CG    . LEU B 2 339 ? 125.918 139.010 103.381 1.00 95.16  ? 339 LEU A CG    1 
ATOM   3545 C CD1   . LEU B 2 339 ? 125.708 139.412 104.828 1.00 95.16  ? 339 LEU A CD1   1 
ATOM   3546 C CD2   . LEU B 2 339 ? 126.164 140.230 102.513 1.00 95.16  ? 339 LEU A CD2   1 
ATOM   3547 N N     . ILE B 2 340 ? 128.842 135.613 102.206 1.00 97.63  ? 340 ILE A N     1 
ATOM   3548 C CA    . ILE B 2 340 ? 130.109 134.891 102.209 1.00 97.63  ? 340 ILE A CA    1 
ATOM   3549 C C     . ILE B 2 340 ? 130.620 134.707 100.787 1.00 97.63  ? 340 ILE A C     1 
ATOM   3550 O O     . ILE B 2 340 ? 131.755 135.075 100.473 1.00 97.63  ? 340 ILE A O     1 
ATOM   3551 C CB    . ILE B 2 340 ? 129.958 133.548 102.940 1.00 97.63  ? 340 ILE A CB    1 
ATOM   3552 C CG1   . ILE B 2 340 ? 129.820 133.796 104.439 1.00 97.63  ? 340 ILE A CG1   1 
ATOM   3553 C CG2   . ILE B 2 340 ? 131.141 132.649 102.649 1.00 97.63  ? 340 ILE A CG2   1 
ATOM   3554 C CD1   . ILE B 2 340 ? 130.931 134.638 105.014 1.00 97.63  ? 340 ILE A CD1   1 
ATOM   3555 N N     . MET B 2 341 ? 129.778 134.168 99.901  1.00 104.06 ? 341 MET A N     1 
ATOM   3556 C CA    . MET B 2 341 ? 130.181 133.962 98.514  1.00 104.06 ? 341 MET A CA    1 
ATOM   3557 C C     . MET B 2 341 ? 130.626 135.259 97.855  1.00 104.06 ? 341 MET A C     1 
ATOM   3558 O O     . MET B 2 341 ? 131.393 135.227 96.886  1.00 104.06 ? 341 MET A O     1 
ATOM   3559 C CB    . MET B 2 341 ? 129.032 133.347 97.712  1.00 104.06 ? 341 MET A CB    1 
ATOM   3560 C CG    . MET B 2 341 ? 128.628 131.940 98.122  1.00 104.06 ? 341 MET A CG    1 
ATOM   3561 S SD    . MET B 2 341 ? 129.928 130.710 97.910  1.00 104.06 ? 341 MET A SD    1 
ATOM   3562 C CE    . MET B 2 341 ? 130.434 130.460 99.608  1.00 104.06 ? 341 MET A CE    1 
ATOM   3563 N N     . LEU B 2 342 ? 130.163 136.404 98.353  1.00 105.22 ? 342 LEU A N     1 
ATOM   3564 C CA    . LEU B 2 342 ? 130.520 137.669 97.729  1.00 105.22 ? 342 LEU A CA    1 
ATOM   3565 C C     . LEU B 2 342 ? 131.732 138.337 98.366  1.00 105.22 ? 342 LEU A C     1 
ATOM   3566 O O     . LEU B 2 342 ? 132.444 139.074 97.675  1.00 105.22 ? 342 LEU A O     1 
ATOM   3567 C CB    . LEU B 2 342 ? 129.320 138.625 97.766  1.00 105.22 ? 342 LEU A CB    1 
ATOM   3568 C CG    . LEU B 2 342 ? 129.332 139.877 96.880  1.00 105.22 ? 342 LEU A CG    1 
ATOM   3569 C CD1   . LEU B 2 342 ? 127.910 140.236 96.489  1.00 105.22 ? 342 LEU A CD1   1 
ATOM   3570 C CD2   . LEU B 2 342 ? 129.997 141.065 97.557  1.00 105.22 ? 342 LEU A CD2   1 
ATOM   3571 N N     . PHE B 2 343 ? 132.000 138.098 99.648  1.00 108.95 ? 343 PHE A N     1 
ATOM   3572 C CA    . PHE B 2 343 ? 133.082 138.799 100.332 1.00 108.95 ? 343 PHE A CA    1 
ATOM   3573 C C     . PHE B 2 343 ? 134.244 137.909 100.745 1.00 108.95 ? 343 PHE A C     1 
ATOM   3574 O O     . PHE B 2 343 ? 135.399 138.316 100.605 1.00 108.95 ? 343 PHE A O     1 
ATOM   3575 C CB    . PHE B 2 343 ? 132.541 139.517 101.572 1.00 108.95 ? 343 PHE A CB    1 
ATOM   3576 C CG    . PHE B 2 343 ? 131.730 140.741 101.259 1.00 108.95 ? 343 PHE A CG    1 
ATOM   3577 C CD1   . PHE B 2 343 ? 132.351 141.949 100.992 1.00 108.95 ? 343 PHE A CD1   1 
ATOM   3578 C CD2   . PHE B 2 343 ? 130.347 140.685 101.237 1.00 108.95 ? 343 PHE A CD2   1 
ATOM   3579 C CE1   . PHE B 2 343 ? 131.608 143.076 100.704 1.00 108.95 ? 343 PHE A CE1   1 
ATOM   3580 C CE2   . PHE B 2 343 ? 129.599 141.809 100.951 1.00 108.95 ? 343 PHE A CE2   1 
ATOM   3581 C CZ    . PHE B 2 343 ? 130.230 143.006 100.683 1.00 108.95 ? 343 PHE A CZ    1 
ATOM   3582 N N     . VAL B 2 344 ? 133.983 136.708 101.256 1.00 113.15 ? 344 VAL A N     1 
ATOM   3583 C CA    . VAL B 2 344 ? 135.032 135.863 101.812 1.00 113.15 ? 344 VAL A CA    1 
ATOM   3584 C C     . VAL B 2 344 ? 135.099 134.604 100.951 1.00 113.15 ? 344 VAL A C     1 
ATOM   3585 O O     . VAL B 2 344 ? 135.367 133.502 101.441 1.00 113.15 ? 344 VAL A O     1 
ATOM   3586 C CB    . VAL B 2 344 ? 134.752 135.556 103.299 1.00 113.15 ? 344 VAL A CB    1 
ATOM   3587 C CG1   . VAL B 2 344 ? 135.907 134.800 103.961 1.00 113.15 ? 344 VAL A CG1   1 
ATOM   3588 C CG2   . VAL B 2 344 ? 134.453 136.841 104.055 1.00 113.15 ? 344 VAL A CG2   1 
ATOM   3589 N N     . GLY B 2 345 ? 134.832 134.761 99.656  1.00 118.93 ? 345 GLY A N     1 
ATOM   3590 C CA    . GLY B 2 345 ? 134.824 133.640 98.736  1.00 118.93 ? 345 GLY A CA    1 
ATOM   3591 C C     . GLY B 2 345 ? 136.123 132.862 98.710  1.00 118.93 ? 345 GLY A C     1 
ATOM   3592 O O     . GLY B 2 345 ? 136.160 131.692 99.101  1.00 118.93 ? 345 GLY A O     1 
ATOM   3593 N N     . GLY B 2 346 ? 137.197 133.498 98.251  1.00 125.73 ? 346 GLY A N     1 
ATOM   3594 C CA    . GLY B 2 346 ? 138.502 132.868 98.253  1.00 125.73 ? 346 GLY A CA    1 
ATOM   3595 C C     . GLY B 2 346 ? 139.539 133.697 98.981  1.00 125.73 ? 346 GLY A C     1 
ATOM   3596 O O     . GLY B 2 346 ? 140.741 133.433 98.883  1.00 125.73 ? 346 GLY A O     1 
ATOM   3597 N N     . ASN B 2 347 ? 139.077 134.710 99.712  1.00 127.38 ? 347 ASN A N     1 
ATOM   3598 C CA    . ASN B 2 347 ? 139.961 135.641 100.399 1.00 127.38 ? 347 ASN A CA    1 
ATOM   3599 C C     . ASN B 2 347 ? 140.790 134.964 101.482 1.00 127.38 ? 347 ASN A C     1 
ATOM   3600 O O     . ASN B 2 347 ? 142.019 134.886 101.367 1.00 127.38 ? 347 ASN A O     1 
ATOM   3601 C CB    . ASN B 2 347 ? 139.147 136.782 101.014 1.00 127.38 ? 347 ASN A CB    1 
ATOM   3602 C CG    . ASN B 2 347 ? 139.790 138.138 100.804 1.00 127.38 ? 347 ASN A CG    1 
ATOM   3603 O OD1   . ASN B 2 347 ? 140.526 138.347 99.839  1.00 127.38 ? 347 ASN A OD1   1 
ATOM   3604 N ND2   . ASN B 2 347 ? 139.513 139.070 101.708 1.00 127.38 ? 347 ASN A ND2   1 
ATOM   3605 N N     . VAL B 2 348 ? 140.114 134.443 102.511 1.00 126.11 ? 348 VAL A N     1 
ATOM   3606 C CA    . VAL B 2 348 ? 140.777 134.101 103.766 1.00 126.11 ? 348 VAL A CA    1 
ATOM   3607 C C     . VAL B 2 348 ? 141.807 132.995 103.581 1.00 126.11 ? 348 VAL A C     1 
ATOM   3608 O O     . VAL B 2 348 ? 142.886 133.044 104.185 1.00 126.11 ? 348 VAL A O     1 
ATOM   3609 C CB    . VAL B 2 348 ? 139.725 133.728 104.829 1.00 126.11 ? 348 VAL A CB    1 
ATOM   3610 C CG1   . VAL B 2 348 ? 138.834 132.607 104.331 1.00 126.11 ? 348 VAL A CG1   1 
ATOM   3611 C CG2   . VAL B 2 348 ? 140.400 133.337 106.134 1.00 126.11 ? 348 VAL A CG2   1 
ATOM   3612 N N     . ILE B 2 349 ? 141.515 131.997 102.743 1.00 124.14 ? 349 ILE A N     1 
ATOM   3613 C CA    . ILE B 2 349 ? 142.428 130.866 102.595 1.00 124.14 ? 349 ILE A CA    1 
ATOM   3614 C C     . ILE B 2 349 ? 143.786 131.341 102.092 1.00 124.14 ? 349 ILE A C     1 
ATOM   3615 O O     . ILE B 2 349 ? 144.821 131.095 102.720 1.00 124.14 ? 349 ILE A O     1 
ATOM   3616 C CB    . ILE B 2 349 ? 141.816 129.786 101.683 1.00 124.14 ? 349 ILE A CB    1 
ATOM   3617 C CG1   . ILE B 2 349 ? 141.402 130.363 100.328 1.00 124.14 ? 349 ILE A CG1   1 
ATOM   3618 C CG2   . ILE B 2 349 ? 140.627 129.128 102.365 1.00 124.14 ? 349 ILE A CG2   1 
ATOM   3619 C CD1   . ILE B 2 349 ? 141.035 129.315 99.301  1.00 124.14 ? 349 ILE A CD1   1 
ATOM   3620 N N     . ARG B 2 350 ? 143.800 132.074 100.979 1.00 126.42 ? 350 ARG A N     1 
ATOM   3621 C CA    . ARG B 2 350 ? 145.073 132.503 100.413 1.00 126.42 ? 350 ARG A CA    1 
ATOM   3622 C C     . ARG B 2 350 ? 145.663 133.671 101.193 1.00 126.42 ? 350 ARG A C     1 
ATOM   3623 O O     . ARG B 2 350 ? 146.878 133.895 101.145 1.00 126.42 ? 350 ARG A O     1 
ATOM   3624 C CB    . ARG B 2 350 ? 144.892 132.856 98.935  1.00 126.42 ? 350 ARG A CB    1 
ATOM   3625 C CG    . ARG B 2 350 ? 146.162 133.296 98.219  1.00 126.42 ? 350 ARG A CG    1 
ATOM   3626 C CD    . ARG B 2 350 ? 145.862 134.286 97.107  1.00 126.42 ? 350 ARG A CD    1 
ATOM   3627 N NE    . ARG B 2 350 ? 145.058 133.684 96.047  1.00 126.42 ? 350 ARG A NE    1 
ATOM   3628 C CZ    . ARG B 2 350 ? 143.886 134.157 95.637  1.00 126.42 ? 350 ARG A CZ    1 
ATOM   3629 N NH1   . ARG B 2 350 ? 143.377 135.247 96.194  1.00 126.42 ? 350 ARG A NH1   1 
ATOM   3630 N NH2   . ARG B 2 350 ? 143.223 133.543 94.667  1.00 126.42 ? 350 ARG A NH2   1 
ATOM   3631 N N     . LYS B 2 351 ? 144.836 134.406 101.938 1.00 126.12 ? 351 LYS A N     1 
ATOM   3632 C CA    . LYS B 2 351 ? 145.359 135.526 102.707 1.00 126.12 ? 351 LYS A CA    1 
ATOM   3633 C C     . LYS B 2 351 ? 146.057 135.070 103.980 1.00 126.12 ? 351 LYS A C     1 
ATOM   3634 O O     . LYS B 2 351 ? 147.005 135.726 104.427 1.00 126.12 ? 351 LYS A O     1 
ATOM   3635 C CB    . LYS B 2 351 ? 144.229 136.501 103.045 1.00 126.12 ? 351 LYS A CB    1 
ATOM   3636 C CG    . LYS B 2 351 ? 144.687 137.790 103.707 1.00 126.12 ? 351 LYS A CG    1 
ATOM   3637 C CD    . LYS B 2 351 ? 143.514 138.715 103.993 1.00 126.12 ? 351 LYS A CD    1 
ATOM   3638 C CE    . LYS B 2 351 ? 143.407 139.814 102.948 1.00 126.12 ? 351 LYS A CE    1 
ATOM   3639 N NZ    . LYS B 2 351 ? 142.316 140.776 103.265 1.00 126.12 ? 351 LYS A NZ    1 
ATOM   3640 N N     . PHE B 2 352 ? 145.625 133.955 104.571 1.00 122.58 ? 352 PHE A N     1 
ATOM   3641 C CA    . PHE B 2 352 ? 146.137 133.544 105.871 1.00 122.58 ? 352 PHE A CA    1 
ATOM   3642 C C     . PHE B 2 352 ? 146.676 132.118 105.898 1.00 122.58 ? 352 PHE A C     1 
ATOM   3643 O O     . PHE B 2 352 ? 146.924 131.590 106.987 1.00 122.58 ? 352 PHE A O     1 
ATOM   3644 C CB    . PHE B 2 352 ? 145.045 133.704 106.930 1.00 122.58 ? 352 PHE A CB    1 
ATOM   3645 C CG    . PHE B 2 352 ? 144.668 135.129 107.204 1.00 122.58 ? 352 PHE A CG    1 
ATOM   3646 C CD1   . PHE B 2 352 ? 145.640 136.089 107.415 1.00 122.58 ? 352 PHE A CD1   1 
ATOM   3647 C CD2   . PHE B 2 352 ? 143.338 135.508 107.245 1.00 122.58 ? 352 PHE A CD2   1 
ATOM   3648 C CE1   . PHE B 2 352 ? 145.293 137.402 107.666 1.00 122.58 ? 352 PHE A CE1   1 
ATOM   3649 C CE2   . PHE B 2 352 ? 142.984 136.819 107.494 1.00 122.58 ? 352 PHE A CE2   1 
ATOM   3650 C CZ    . PHE B 2 352 ? 143.963 137.767 107.705 1.00 122.58 ? 352 PHE A CZ    1 
ATOM   3651 N N     . GLY B 2 353 ? 146.880 131.477 104.747 1.00 116.54 ? 353 GLY A N     1 
ATOM   3652 C CA    . GLY B 2 353 ? 147.434 130.139 104.754 1.00 116.54 ? 353 GLY A CA    1 
ATOM   3653 C C     . GLY B 2 353 ? 146.356 129.088 104.909 1.00 116.54 ? 353 GLY A C     1 
ATOM   3654 O O     . GLY B 2 353 ? 145.173 129.375 105.106 1.00 116.54 ? 353 GLY A O     1 
ATOM   3655 N N     . TRP B 2 354 ? 146.779 127.828 104.816 1.00 108.28 ? 354 TRP A N     1 
ATOM   3656 C CA    . TRP B 2 354 ? 145.819 126.734 104.887 1.00 108.28 ? 354 TRP A CA    1 
ATOM   3657 C C     . TRP B 2 354 ? 145.413 126.413 106.317 1.00 108.28 ? 354 TRP A C     1 
ATOM   3658 O O     . TRP B 2 354 ? 144.263 126.028 106.556 1.00 108.28 ? 354 TRP A O     1 
ATOM   3659 C CB    . TRP B 2 354 ? 146.388 125.483 104.219 1.00 108.28 ? 354 TRP A CB    1 
ATOM   3660 C CG    . TRP B 2 354 ? 145.438 124.328 104.218 1.00 108.28 ? 354 TRP A CG    1 
ATOM   3661 C CD1   . TRP B 2 354 ? 144.556 123.996 103.236 1.00 108.28 ? 354 TRP A CD1   1 
ATOM   3662 C CD2   . TRP B 2 354 ? 145.271 123.353 105.252 1.00 108.28 ? 354 TRP A CD2   1 
ATOM   3663 N NE1   . TRP B 2 354 ? 143.851 122.874 103.591 1.00 108.28 ? 354 TRP A NE1   1 
ATOM   3664 C CE2   . TRP B 2 354 ? 144.271 122.461 104.826 1.00 108.28 ? 354 TRP A CE2   1 
ATOM   3665 C CE3   . TRP B 2 354 ? 145.869 123.149 106.497 1.00 108.28 ? 354 TRP A CE3   1 
ATOM   3666 C CZ2   . TRP B 2 354 ? 143.856 121.383 105.599 1.00 108.28 ? 354 TRP A CZ2   1 
ATOM   3667 C CZ3   . TRP B 2 354 ? 145.456 122.080 107.262 1.00 108.28 ? 354 TRP A CZ3   1 
ATOM   3668 C CH2   . TRP B 2 354 ? 144.460 121.210 106.811 1.00 108.28 ? 354 TRP A CH2   1 
ATOM   3669 N N     . LEU B 2 355 ? 146.338 126.542 107.271 1.00 105.01 ? 355 LEU A N     1 
ATOM   3670 C CA    . LEU B 2 355 ? 146.041 126.159 108.647 1.00 105.01 ? 355 LEU A CA    1 
ATOM   3671 C C     . LEU B 2 355 ? 144.908 126.997 109.220 1.00 105.01 ? 355 LEU A C     1 
ATOM   3672 O O     . LEU B 2 355 ? 143.992 126.468 109.855 1.00 105.01 ? 355 LEU A O     1 
ATOM   3673 C CB    . LEU B 2 355 ? 147.294 126.290 109.511 1.00 105.01 ? 355 LEU A CB    1 
ATOM   3674 C CG    . LEU B 2 355 ? 147.121 125.992 111.001 1.00 105.01 ? 355 LEU A CG    1 
ATOM   3675 C CD1   . LEU B 2 355 ? 146.510 124.620 111.209 1.00 105.01 ? 355 LEU A CD1   1 
ATOM   3676 C CD2   . LEU B 2 355 ? 148.453 126.094 111.721 1.00 105.01 ? 355 LEU A CD2   1 
ATOM   3677 N N     . THR B 2 356 ? 144.942 128.309 108.991 1.00 106.30 ? 356 THR A N     1 
ATOM   3678 C CA    . THR B 2 356 ? 143.904 129.168 109.549 1.00 106.30 ? 356 THR A CA    1 
ATOM   3679 C C     . THR B 2 356 ? 142.556 128.893 108.902 1.00 106.30 ? 356 THR A C     1 
ATOM   3680 O O     . THR B 2 356 ? 141.525 128.870 109.585 1.00 106.30 ? 356 THR A O     1 
ATOM   3681 C CB    . THR B 2 356 ? 144.284 130.632 109.379 1.00 106.30 ? 356 THR A CB    1 
ATOM   3682 O OG1   . THR B 2 356 ? 144.135 130.994 108.004 1.00 106.30 ? 356 THR A OG1   1 
ATOM   3683 C CG2   . THR B 2 356 ? 145.723 130.854 109.810 1.00 106.30 ? 356 THR A CG2   1 
ATOM   3684 N N     . GLY B 2 357 ? 142.538 128.701 107.583 1.00 102.74 ? 357 GLY A N     1 
ATOM   3685 C CA    . GLY B 2 357 ? 141.290 128.367 106.918 1.00 102.74 ? 357 GLY A CA    1 
ATOM   3686 C C     . GLY B 2 357 ? 140.710 127.056 107.409 1.00 102.74 ? 357 GLY A C     1 
ATOM   3687 O O     . GLY B 2 357 ? 139.494 126.922 107.560 1.00 102.74 ? 357 GLY A O     1 
ATOM   3688 N N     . ALA B 2 358 ? 141.571 126.076 107.675 1.00 101.28 ? 358 ALA A N     1 
ATOM   3689 C CA    . ALA B 2 358 ? 141.105 124.800 108.195 1.00 101.28 ? 358 ALA A CA    1 
ATOM   3690 C C     . ALA B 2 358 ? 140.740 124.869 109.668 1.00 101.28 ? 358 ALA A C     1 
ATOM   3691 O O     . ALA B 2 358 ? 140.025 123.988 110.153 1.00 101.28 ? 358 ALA A O     1 
ATOM   3692 C CB    . ALA B 2 358 ? 142.168 123.722 107.982 1.00 101.28 ? 358 ALA A CB    1 
ATOM   3693 N N     . LEU B 2 359 ? 141.221 125.880 110.388 1.00 96.29  ? 359 LEU A N     1 
ATOM   3694 C CA    . LEU B 2 359 ? 140.932 126.010 111.808 1.00 96.29  ? 359 LEU A CA    1 
ATOM   3695 C C     . LEU B 2 359 ? 139.757 126.926 112.116 1.00 96.29  ? 359 LEU A C     1 
ATOM   3696 O O     . LEU B 2 359 ? 139.229 126.863 113.229 1.00 96.29  ? 359 LEU A O     1 
ATOM   3697 C CB    . LEU B 2 359 ? 142.165 126.524 112.561 1.00 96.29  ? 359 LEU A CB    1 
ATOM   3698 C CG    . LEU B 2 359 ? 143.297 125.527 112.802 1.00 96.29  ? 359 LEU A CG    1 
ATOM   3699 C CD1   . LEU B 2 359 ? 144.248 126.045 113.863 1.00 96.29  ? 359 LEU A CD1   1 
ATOM   3700 C CD2   . LEU B 2 359 ? 142.745 124.174 113.192 1.00 96.29  ? 359 LEU A CD2   1 
ATOM   3701 N N     . VAL B 2 360 ? 139.346 127.781 111.178 1.00 94.62  ? 360 VAL A N     1 
ATOM   3702 C CA    . VAL B 2 360 ? 138.220 128.677 111.442 1.00 94.62  ? 360 VAL A CA    1 
ATOM   3703 C C     . VAL B 2 360 ? 136.965 127.881 111.774 1.00 94.62  ? 360 VAL A C     1 
ATOM   3704 O O     . VAL B 2 360 ? 136.249 128.192 112.732 1.00 94.62  ? 360 VAL A O     1 
ATOM   3705 C CB    . VAL B 2 360 ? 137.980 129.625 110.253 1.00 94.62  ? 360 VAL A CB    1 
ATOM   3706 C CG1   . VAL B 2 360 ? 136.664 130.353 110.428 1.00 94.62  ? 360 VAL A CG1   1 
ATOM   3707 C CG2   . VAL B 2 360 ? 139.095 130.641 110.157 1.00 94.62  ? 360 VAL A CG2   1 
ATOM   3708 N N     . THR B 2 361 ? 136.681 126.840 110.997 1.00 92.61  ? 361 THR A N     1 
ATOM   3709 C CA    . THR B 2 361 ? 135.452 126.081 111.217 1.00 92.61  ? 361 THR A CA    1 
ATOM   3710 C C     . THR B 2 361 ? 135.450 125.334 112.545 1.00 92.61  ? 361 THR A C     1 
ATOM   3711 O O     . THR B 2 361 ? 134.444 125.422 113.272 1.00 92.61  ? 361 THR A O     1 
ATOM   3712 C CB    . THR B 2 361 ? 135.208 125.132 110.040 1.00 92.61  ? 361 THR A CB    1 
ATOM   3713 O OG1   . THR B 2 361 ? 135.120 125.889 108.828 1.00 92.61  ? 361 THR A OG1   1 
ATOM   3714 C CG2   . THR B 2 361 ? 133.916 124.368 110.241 1.00 92.61  ? 361 THR A CG2   1 
ATOM   3715 N N     . PRO B 2 362 ? 136.501 124.599 112.932 1.00 89.99  ? 362 PRO A N     1 
ATOM   3716 C CA    . PRO B 2 362 ? 136.464 123.961 114.256 1.00 89.99  ? 362 PRO A CA    1 
ATOM   3717 C C     . PRO B 2 362 ? 136.387 124.950 115.402 1.00 89.99  ? 362 PRO A C     1 
ATOM   3718 O O     . PRO B 2 362 ? 135.639 124.708 116.351 1.00 89.99  ? 362 PRO A O     1 
ATOM   3719 C CB    . PRO B 2 362 ? 137.763 123.144 114.293 1.00 89.99  ? 362 PRO A CB    1 
ATOM   3720 C CG    . PRO B 2 362 ? 138.618 123.728 113.259 1.00 89.99  ? 362 PRO A CG    1 
ATOM   3721 C CD    . PRO B 2 362 ? 137.697 124.185 112.183 1.00 89.99  ? 362 PRO A CD    1 
ATOM   3722 N N     . VAL B 2 363 ? 137.126 126.061 115.350 1.00 89.71  ? 363 VAL A N     1 
ATOM   3723 C CA    . VAL B 2 363 ? 137.081 126.987 116.477 1.00 89.71  ? 363 VAL A CA    1 
ATOM   3724 C C     . VAL B 2 363 ? 135.752 127.729 116.509 1.00 89.71  ? 363 VAL A C     1 
ATOM   3725 O O     . VAL B 2 363 ? 135.255 128.072 117.586 1.00 89.71  ? 363 VAL A O     1 
ATOM   3726 C CB    . VAL B 2 363 ? 138.270 127.966 116.443 1.00 89.71  ? 363 VAL A CB    1 
ATOM   3727 C CG1   . VAL B 2 363 ? 139.586 127.204 116.424 1.00 89.71  ? 363 VAL A CG1   1 
ATOM   3728 C CG2   . VAL B 2 363 ? 138.164 128.928 115.275 1.00 89.71  ? 363 VAL A CG2   1 
ATOM   3729 N N     . MET B 2 364 ? 135.137 127.963 115.349 1.00 91.28  ? 364 MET A N     1 
ATOM   3730 C CA    . MET B 2 364 ? 133.821 128.592 115.333 1.00 91.28  ? 364 MET A CA    1 
ATOM   3731 C C     . MET B 2 364 ? 132.773 127.657 115.913 1.00 91.28  ? 364 MET A C     1 
ATOM   3732 O O     . MET B 2 364 ? 131.925 128.071 116.714 1.00 91.28  ? 364 MET A O     1 
ATOM   3733 C CB    . MET B 2 364 ? 133.447 129.004 113.911 1.00 91.28  ? 364 MET A CB    1 
ATOM   3734 C CG    . MET B 2 364 ? 132.066 129.618 113.784 1.00 91.28  ? 364 MET A CG    1 
ATOM   3735 S SD    . MET B 2 364 ? 130.829 128.422 113.251 1.00 91.28  ? 364 MET A SD    1 
ATOM   3736 C CE    . MET B 2 364 ? 131.543 127.872 111.705 1.00 91.28  ? 364 MET A CE    1 
ATOM   3737 N N     . VAL B 2 365 ? 132.811 126.384 115.510 1.00 88.65  ? 365 VAL A N     1 
ATOM   3738 C CA    . VAL B 2 365 ? 131.911 125.400 116.099 1.00 88.65  ? 365 VAL A CA    1 
ATOM   3739 C C     . VAL B 2 365 ? 132.156 125.295 117.596 1.00 88.65  ? 365 VAL A C     1 
ATOM   3740 O O     . VAL B 2 365 ? 131.213 125.232 118.387 1.00 88.65  ? 365 VAL A O     1 
ATOM   3741 C CB    . VAL B 2 365 ? 132.069 124.039 115.398 1.00 88.65  ? 365 VAL A CB    1 
ATOM   3742 C CG1   . VAL B 2 365 ? 131.316 122.966 116.155 1.00 88.65  ? 365 VAL A CG1   1 
ATOM   3743 C CG2   . VAL B 2 365 ? 131.567 124.122 113.971 1.00 88.65  ? 365 VAL A CG2   1 
ATOM   3744 N N     . LEU B 2 366 ? 133.422 125.336 118.011 1.00 87.87  ? 366 LEU A N     1 
ATOM   3745 C CA    . LEU B 2 366 ? 133.755 125.235 119.427 1.00 87.87  ? 366 LEU A CA    1 
ATOM   3746 C C     . LEU B 2 366 ? 133.165 126.394 120.214 1.00 87.87  ? 366 LEU A C     1 
ATOM   3747 O O     . LEU B 2 366 ? 132.509 126.189 121.237 1.00 87.87  ? 366 LEU A O     1 
ATOM   3748 C CB    . LEU B 2 366 ? 135.271 125.182 119.599 1.00 87.87  ? 366 LEU A CB    1 
ATOM   3749 C CG    . LEU B 2 366 ? 135.800 125.120 121.030 1.00 87.87  ? 366 LEU A CG    1 
ATOM   3750 C CD1   . LEU B 2 366 ? 135.241 123.910 121.750 1.00 87.87  ? 366 LEU A CD1   1 
ATOM   3751 C CD2   . LEU B 2 366 ? 137.315 125.091 121.027 1.00 87.87  ? 366 LEU A CD2   1 
ATOM   3752 N N     . LEU B 2 367 ? 133.384 127.623 119.748 1.00 88.66  ? 367 LEU A N     1 
ATOM   3753 C CA    . LEU B 2 367 ? 132.877 128.788 120.465 1.00 88.66  ? 367 LEU A CA    1 
ATOM   3754 C C     . LEU B 2 367 ? 131.354 128.800 120.493 1.00 88.66  ? 367 LEU A C     1 
ATOM   3755 O O     . LEU B 2 367 ? 130.741 128.851 121.569 1.00 88.66  ? 367 LEU A O     1 
ATOM   3756 C CB    . LEU B 2 367 ? 133.411 130.066 119.824 1.00 88.66  ? 367 LEU A CB    1 
ATOM   3757 C CG    . LEU B 2 367 ? 134.588 130.732 120.533 1.00 88.66  ? 367 LEU A CG    1 
ATOM   3758 C CD1   . LEU B 2 367 ? 135.761 129.775 120.640 1.00 88.66  ? 367 LEU A CD1   1 
ATOM   3759 C CD2   . LEU B 2 367 ? 134.994 132.000 119.806 1.00 88.66  ? 367 LEU A CD2   1 
ATOM   3760 N N     . THR B 2 368 ? 130.724 128.769 119.317 1.00 88.29  ? 368 THR A N     1 
ATOM   3761 C CA    . THR B 2 368 ? 129.272 128.827 119.251 1.00 88.29  ? 368 THR A CA    1 
ATOM   3762 C C     . THR B 2 368 ? 128.604 127.557 119.754 1.00 88.29  ? 368 THR A C     1 
ATOM   3763 O O     . THR B 2 368 ? 127.372 127.509 119.807 1.00 88.29  ? 368 THR A O     1 
ATOM   3764 C CB    . THR B 2 368 ? 128.825 129.111 117.819 1.00 88.29  ? 368 THR A CB    1 
ATOM   3765 O OG1   . THR B 2 368 ? 129.626 128.349 116.911 1.00 88.29  ? 368 THR A OG1   1 
ATOM   3766 C CG2   . THR B 2 368 ? 128.975 130.586 117.500 1.00 88.29  ? 368 THR A CG2   1 
ATOM   3767 N N     . GLY B 2 369 ? 129.373 126.536 120.121 1.00 86.10  ? 369 GLY A N     1 
ATOM   3768 C CA    . GLY B 2 369 ? 128.801 125.353 120.715 1.00 86.10  ? 369 GLY A CA    1 
ATOM   3769 C C     . GLY B 2 369 ? 128.956 125.349 122.216 1.00 86.10  ? 369 GLY A C     1 
ATOM   3770 O O     . GLY B 2 369 ? 128.049 124.910 122.919 1.00 86.10  ? 369 GLY A O     1 
ATOM   3771 N N     . ILE B 2 370 ? 130.083 125.843 122.731 1.00 86.88  ? 370 ILE A N     1 
ATOM   3772 C CA    . ILE B 2 370 ? 130.213 125.943 124.178 1.00 86.88  ? 370 ILE A CA    1 
ATOM   3773 C C     . ILE B 2 370 ? 129.289 127.023 124.713 1.00 86.88  ? 370 ILE A C     1 
ATOM   3774 O O     . ILE B 2 370 ? 128.708 126.871 125.790 1.00 86.88  ? 370 ILE A O     1 
ATOM   3775 C CB    . ILE B 2 370 ? 131.676 126.179 124.601 1.00 86.88  ? 370 ILE A CB    1 
ATOM   3776 C CG1   . ILE B 2 370 ? 132.203 127.512 124.072 1.00 86.88  ? 370 ILE A CG1   1 
ATOM   3777 C CG2   . ILE B 2 370 ? 132.554 125.017 124.170 1.00 86.88  ? 370 ILE A CG2   1 
ATOM   3778 C CD1   . ILE B 2 370 ? 133.644 127.781 124.433 1.00 86.88  ? 370 ILE A CD1   1 
ATOM   3779 N N     . VAL B 2 371 ? 129.087 128.104 123.955 1.00 82.20  ? 371 VAL A N     1 
ATOM   3780 C CA    . VAL B 2 371 ? 128.117 129.108 124.387 1.00 82.20  ? 371 VAL A CA    1 
ATOM   3781 C C     . VAL B 2 371 ? 126.711 128.524 124.381 1.00 82.20  ? 371 VAL A C     1 
ATOM   3782 O O     . VAL B 2 371 ? 125.935 128.713 125.328 1.00 82.20  ? 371 VAL A O     1 
ATOM   3783 C CB    . VAL B 2 371 ? 128.212 130.366 123.508 1.00 82.20  ? 371 VAL A CB    1 
ATOM   3784 C CG1   . VAL B 2 371 ? 127.191 131.388 123.952 1.00 82.20  ? 371 VAL A CG1   1 
ATOM   3785 C CG2   . VAL B 2 371 ? 129.603 130.955 123.590 1.00 82.20  ? 371 VAL A CG2   1 
ATOM   3786 N N     . PHE B 2 372 ? 126.367 127.790 123.322 1.00 80.81  ? 372 PHE A N     1 
ATOM   3787 C CA    . PHE B 2 372 ? 125.044 127.185 123.230 1.00 80.81  ? 372 PHE A CA    1 
ATOM   3788 C C     . PHE B 2 372 ? 124.815 126.179 124.350 1.00 80.81  ? 372 PHE A C     1 
ATOM   3789 O O     . PHE B 2 372 ? 123.760 126.182 124.992 1.00 80.81  ? 372 PHE A O     1 
ATOM   3790 C CB    . PHE B 2 372 ? 124.878 126.520 121.865 1.00 80.81  ? 372 PHE A CB    1 
ATOM   3791 C CG    . PHE B 2 372 ? 123.654 125.667 121.751 1.00 80.81  ? 372 PHE A CG    1 
ATOM   3792 C CD1   . PHE B 2 372 ? 122.416 126.237 121.546 1.00 80.81  ? 372 PHE A CD1   1 
ATOM   3793 C CD2   . PHE B 2 372 ? 123.744 124.293 121.841 1.00 80.81  ? 372 PHE A CD2   1 
ATOM   3794 C CE1   . PHE B 2 372 ? 121.293 125.455 121.442 1.00 80.81  ? 372 PHE A CE1   1 
ATOM   3795 C CE2   . PHE B 2 372 ? 122.624 123.508 121.736 1.00 80.81  ? 372 PHE A CE2   1 
ATOM   3796 C CZ    . PHE B 2 372 ? 121.399 124.089 121.536 1.00 80.81  ? 372 PHE A CZ    1 
ATOM   3797 N N     . PHE B 2 373 ? 125.796 125.314 124.607 1.00 82.01  ? 373 PHE A N     1 
ATOM   3798 C CA    . PHE B 2 373 ? 125.638 124.303 125.642 1.00 82.01  ? 373 PHE A CA    1 
ATOM   3799 C C     . PHE B 2 373 ? 125.690 124.912 127.035 1.00 82.01  ? 373 PHE A C     1 
ATOM   3800 O O     . PHE B 2 373 ? 125.119 124.348 127.970 1.00 82.01  ? 373 PHE A O     1 
ATOM   3801 C CB    . PHE B 2 373 ? 126.704 123.223 125.483 1.00 82.01  ? 373 PHE A CB    1 
ATOM   3802 C CG    . PHE B 2 373 ? 126.401 122.236 124.397 1.00 82.01  ? 373 PHE A CG    1 
ATOM   3803 C CD1   . PHE B 2 373 ? 125.179 121.595 124.349 1.00 82.01  ? 373 PHE A CD1   1 
ATOM   3804 C CD2   . PHE B 2 373 ? 127.336 121.952 123.421 1.00 82.01  ? 373 PHE A CD2   1 
ATOM   3805 C CE1   . PHE B 2 373 ? 124.897 120.690 123.350 1.00 82.01  ? 373 PHE A CE1   1 
ATOM   3806 C CE2   . PHE B 2 373 ? 127.058 121.048 122.420 1.00 82.01  ? 373 PHE A CE2   1 
ATOM   3807 C CZ    . PHE B 2 373 ? 125.839 120.417 122.384 1.00 82.01  ? 373 PHE A CZ    1 
ATOM   3808 N N     . ALA B 2 374 ? 126.349 126.059 127.199 1.00 80.90  ? 374 ALA A N     1 
ATOM   3809 C CA    . ALA B 2 374 ? 126.289 126.750 128.478 1.00 80.90  ? 374 ALA A CA    1 
ATOM   3810 C C     . ALA B 2 374 ? 124.911 127.351 128.702 1.00 80.90  ? 374 ALA A C     1 
ATOM   3811 O O     . ALA B 2 374 ? 124.392 127.330 129.823 1.00 80.90  ? 374 ALA A O     1 
ATOM   3812 C CB    . ALA B 2 374 ? 127.365 127.830 128.544 1.00 80.90  ? 374 ALA A CB    1 
ATOM   3813 N N     . LEU B 2 375 ? 124.303 127.889 127.645 1.00 80.35  ? 375 LEU A N     1 
ATOM   3814 C CA    . LEU B 2 375 ? 122.947 128.410 127.770 1.00 80.35  ? 375 LEU A CA    1 
ATOM   3815 C C     . LEU B 2 375 ? 121.936 127.296 128.002 1.00 80.35  ? 375 LEU A C     1 
ATOM   3816 O O     . LEU B 2 375 ? 120.939 127.503 128.699 1.00 80.35  ? 375 LEU A O     1 
ATOM   3817 C CB    . LEU B 2 375 ? 122.576 129.209 126.526 1.00 80.35  ? 375 LEU A CB    1 
ATOM   3818 C CG    . LEU B 2 375 ? 123.280 130.556 126.398 1.00 80.35  ? 375 LEU A CG    1 
ATOM   3819 C CD1   . LEU B 2 375 ? 123.281 131.020 124.958 1.00 80.35  ? 375 LEU A CD1   1 
ATOM   3820 C CD2   . LEU B 2 375 ? 122.614 131.579 127.295 1.00 80.35  ? 375 LEU A CD2   1 
ATOM   3821 N N     . VAL B 2 376 ? 122.171 126.117 127.430 1.00 80.07  ? 376 VAL A N     1 
ATOM   3822 C CA    . VAL B 2 376 ? 121.221 125.019 127.581 1.00 80.07  ? 376 VAL A CA    1 
ATOM   3823 C C     . VAL B 2 376 ? 121.385 124.334 128.931 1.00 80.07  ? 376 VAL A C     1 
ATOM   3824 O O     . VAL B 2 376 ? 120.398 123.976 129.580 1.00 80.07  ? 376 VAL A O     1 
ATOM   3825 C CB    . VAL B 2 376 ? 121.371 124.023 126.419 1.00 80.07  ? 376 VAL A CB    1 
ATOM   3826 C CG1   . VAL B 2 376 ? 120.531 122.789 126.672 1.00 80.07  ? 376 VAL A CG1   1 
ATOM   3827 C CG2   . VAL B 2 376 ? 120.961 124.673 125.117 1.00 80.07  ? 376 VAL A CG2   1 
ATOM   3828 N N     . ILE B 2 377 ? 122.623 124.136 129.377 1.00 81.64  ? 377 ILE A N     1 
ATOM   3829 C CA    . ILE B 2 377 ? 122.858 123.459 130.646 1.00 81.64  ? 377 ILE A CA    1 
ATOM   3830 C C     . ILE B 2 377 ? 122.583 124.394 131.812 1.00 81.64  ? 377 ILE A C     1 
ATOM   3831 O O     . ILE B 2 377 ? 121.854 124.049 132.748 1.00 81.64  ? 377 ILE A O     1 
ATOM   3832 C CB    . ILE B 2 377 ? 124.293 122.908 130.697 1.00 81.64  ? 377 ILE A CB    1 
ATOM   3833 C CG1   . ILE B 2 377 ? 124.481 121.810 129.656 1.00 81.64  ? 377 ILE A CG1   1 
ATOM   3834 C CG2   . ILE B 2 377 ? 124.605 122.375 132.079 1.00 81.64  ? 377 ILE A CG2   1 
ATOM   3835 C CD1   . ILE B 2 377 ? 125.923 121.442 129.432 1.00 81.64  ? 377 ILE A CD1   1 
ATOM   3836 N N     . PHE B 2 378 ? 123.159 125.591 131.775 1.00 85.55  ? 378 PHE A N     1 
ATOM   3837 C CA    . PHE B 2 378 ? 122.992 126.561 132.854 1.00 85.55  ? 378 PHE A CA    1 
ATOM   3838 C C     . PHE B 2 378 ? 121.835 127.513 132.544 1.00 85.55  ? 378 PHE A C     1 
ATOM   3839 O O     . PHE B 2 378 ? 121.988 128.730 132.481 1.00 85.55  ? 378 PHE A O     1 
ATOM   3840 C CB    . PHE B 2 378 ? 124.292 127.322 133.082 1.00 85.55  ? 378 PHE A CB    1 
ATOM   3841 C CG    . PHE B 2 378 ? 125.490 126.435 133.240 1.00 85.55  ? 378 PHE A CG    1 
ATOM   3842 C CD1   . PHE B 2 378 ? 125.497 125.419 134.176 1.00 85.55  ? 378 PHE A CD1   1 
ATOM   3843 C CD2   . PHE B 2 378 ? 126.608 126.614 132.447 1.00 85.55  ? 378 PHE A CD2   1 
ATOM   3844 C CE1   . PHE B 2 378 ? 126.595 124.602 134.320 1.00 85.55  ? 378 PHE A CE1   1 
ATOM   3845 C CE2   . PHE B 2 378 ? 127.709 125.799 132.587 1.00 85.55  ? 378 PHE A CE2   1 
ATOM   3846 C CZ    . PHE B 2 378 ? 127.702 124.792 133.524 1.00 85.55  ? 378 PHE A CZ    1 
ATOM   3847 N N     . ARG B 2 379 ? 120.655 126.925 132.345 1.00 87.45  ? 379 ARG A N     1 
ATOM   3848 C CA    . ARG B 2 379 ? 119.460 127.733 132.127 1.00 87.45  ? 379 ARG A CA    1 
ATOM   3849 C C     . ARG B 2 379 ? 119.102 128.522 133.377 1.00 87.45  ? 379 ARG A C     1 
ATOM   3850 O O     . ARG B 2 379 ? 119.006 129.754 133.339 1.00 87.45  ? 379 ARG A O     1 
ATOM   3851 C CB    . ARG B 2 379 ? 118.289 126.847 131.707 1.00 87.45  ? 379 ARG A CB    1 
ATOM   3852 C CG    . ARG B 2 379 ? 118.390 126.305 130.302 1.00 87.45  ? 379 ARG A CG    1 
ATOM   3853 C CD    . ARG B 2 379 ? 117.578 127.142 129.333 1.00 87.45  ? 379 ARG A CD    1 
ATOM   3854 N NE    . ARG B 2 379 ? 116.143 126.936 129.499 1.00 87.45  ? 379 ARG A NE    1 
ATOM   3855 C CZ    . ARG B 2 379 ? 115.434 126.048 128.812 1.00 87.45  ? 379 ARG A CZ    1 
ATOM   3856 N NH1   . ARG B 2 379 ? 116.029 125.280 127.910 1.00 87.45  ? 379 ARG A NH1   1 
ATOM   3857 N NH2   . ARG B 2 379 ? 114.131 125.928 129.026 1.00 87.45  ? 379 ARG A NH2   1 
ATOM   3858 N N     . ASN B 2 380 ? 118.899 127.826 134.497 1.00 87.58  ? 380 ASN A N     1 
ATOM   3859 C CA    . ASN B 2 380 ? 118.491 128.498 135.725 1.00 87.58  ? 380 ASN A CA    1 
ATOM   3860 C C     . ASN B 2 380 ? 119.544 129.484 136.206 1.00 87.58  ? 380 ASN A C     1 
ATOM   3861 O O     . ASN B 2 380 ? 119.204 130.504 136.813 1.00 87.58  ? 380 ASN A O     1 
ATOM   3862 C CB    . ASN B 2 380 ? 118.195 127.466 136.808 1.00 87.58  ? 380 ASN A CB    1 
ATOM   3863 C CG    . ASN B 2 380 ? 117.308 126.346 136.314 1.00 87.58  ? 380 ASN A CG    1 
ATOM   3864 O OD1   . ASN B 2 380 ? 116.487 126.540 135.419 1.00 87.58  ? 380 ASN A OD1   1 
ATOM   3865 N ND2   . ASN B 2 380 ? 117.470 125.163 136.892 1.00 87.58  ? 380 ASN A ND2   1 
ATOM   3866 N N     . GLN B 2 381 ? 120.821 129.203 135.950 1.00 86.77  ? 381 GLN A N     1 
ATOM   3867 C CA    . GLN B 2 381 ? 121.863 130.149 136.325 1.00 86.77  ? 381 GLN A CA    1 
ATOM   3868 C C     . GLN B 2 381 ? 121.839 131.377 135.424 1.00 86.77  ? 381 GLN A C     1 
ATOM   3869 O O     . GLN B 2 381 ? 122.132 132.490 135.875 1.00 86.77  ? 381 GLN A O     1 
ATOM   3870 C CB    . GLN B 2 381 ? 123.230 129.470 136.276 1.00 86.77  ? 381 GLN A CB    1 
ATOM   3871 C CG    . GLN B 2 381 ? 123.591 128.709 137.540 1.00 86.77  ? 381 GLN A CG    1 
ATOM   3872 C CD    . GLN B 2 381 ? 122.783 127.441 137.714 1.00 86.77  ? 381 GLN A CD    1 
ATOM   3873 O OE1   . GLN B 2 381 ? 122.086 127.268 138.712 1.00 86.77  ? 381 GLN A OE1   1 
ATOM   3874 N NE2   . GLN B 2 381 ? 122.876 126.543 136.743 1.00 86.77  ? 381 GLN A NE2   1 
ATOM   3875 N N     . ALA B 2 382 ? 121.486 131.197 134.151 1.00 87.65  ? 382 ALA A N     1 
ATOM   3876 C CA    . ALA B 2 382 ? 121.453 132.321 133.224 1.00 87.65  ? 382 ALA A CA    1 
ATOM   3877 C C     . ALA B 2 382 ? 120.140 133.085 133.318 1.00 87.65  ? 382 ALA A C     1 
ATOM   3878 O O     . ALA B 2 382 ? 120.128 134.316 133.222 1.00 87.65  ? 382 ALA A O     1 
ATOM   3879 C CB    . ALA B 2 382 ? 121.684 131.835 131.794 1.00 87.65  ? 382 ALA A CB    1 
ATOM   3880 N N     . SER B 2 383 ? 119.032 132.383 133.529 1.00 89.15  ? 383 SER A N     1 
ATOM   3881 C CA    . SER B 2 383 ? 117.734 133.039 133.643 1.00 89.15  ? 383 SER A CA    1 
ATOM   3882 C C     . SER B 2 383 ? 117.748 133.901 134.894 1.00 89.15  ? 383 SER A C     1 
ATOM   3883 O O     . SER B 2 383 ? 117.660 133.400 136.016 1.00 89.15  ? 383 SER A O     1 
ATOM   3884 C CB    . SER B 2 383 ? 116.614 132.008 133.696 1.00 89.15  ? 383 SER A CB    1 
ATOM   3885 O OG    . SER B 2 383 ? 116.511 131.442 134.989 1.00 89.15  ? 383 SER A OG    1 
ATOM   3886 N N     . GLY B 2 384 ? 117.859 135.208 134.699 1.00 90.45  ? 384 GLY A N     1 
ATOM   3887 C CA    . GLY B 2 384 ? 118.003 136.147 135.790 1.00 90.45  ? 384 GLY A CA    1 
ATOM   3888 C C     . GLY B 2 384 ? 119.078 137.159 135.466 1.00 90.45  ? 384 GLY A C     1 
ATOM   3889 O O     . GLY B 2 384 ? 118.974 138.331 135.831 1.00 90.45  ? 384 GLY A O     1 
ATOM   3890 N N     . LEU B 2 385 ? 120.117 136.714 134.766 1.00 90.84  ? 385 LEU A N     1 
ATOM   3891 C CA    . LEU B 2 385 ? 121.079 137.634 134.178 1.00 90.84  ? 385 LEU A CA    1 
ATOM   3892 C C     . LEU B 2 385 ? 120.713 137.948 132.737 1.00 90.84  ? 385 LEU A C     1 
ATOM   3893 O O     . LEU B 2 385 ? 120.923 139.071 132.269 1.00 90.84  ? 385 LEU A O     1 
ATOM   3894 C CB    . LEU B 2 385 ? 122.491 137.046 134.259 1.00 90.84  ? 385 LEU A CB    1 
ATOM   3895 C CG    . LEU B 2 385 ? 123.680 137.933 133.883 1.00 90.84  ? 385 LEU A CG    1 
ATOM   3896 C CD1   . LEU B 2 385 ? 124.896 137.533 134.698 1.00 90.84  ? 385 LEU A CD1   1 
ATOM   3897 C CD2   . LEU B 2 385 ? 123.998 137.841 132.399 1.00 90.84  ? 385 LEU A CD2   1 
ATOM   3898 N N     . VAL B 2 386 ? 120.167 136.959 132.029 1.00 88.73  ? 386 VAL A N     1 
ATOM   3899 C CA    . VAL B 2 386 ? 119.662 137.187 130.683 1.00 88.73  ? 386 VAL A CA    1 
ATOM   3900 C C     . VAL B 2 386 ? 118.304 137.869 130.733 1.00 88.73  ? 386 VAL A C     1 
ATOM   3901 O O     . VAL B 2 386 ? 117.961 138.651 129.839 1.00 88.73  ? 386 VAL A O     1 
ATOM   3902 C CB    . VAL B 2 386 ? 119.602 135.860 129.910 1.00 88.73  ? 386 VAL A CB    1 
ATOM   3903 C CG1   . VAL B 2 386 ? 119.352 136.117 128.446 1.00 88.73  ? 386 VAL A CG1   1 
ATOM   3904 C CG2   . VAL B 2 386 ? 120.889 135.089 130.096 1.00 88.73  ? 386 VAL A CG2   1 
ATOM   3905 N N     . ALA B 2 387 ? 117.512 137.591 131.772 1.00 91.60  ? 387 ALA A N     1 
ATOM   3906 C CA    . ALA B 2 387 ? 116.215 138.242 131.919 1.00 91.60  ? 387 ALA A CA    1 
ATOM   3907 C C     . ALA B 2 387 ? 116.354 139.753 131.994 1.00 91.60  ? 387 ALA A C     1 
ATOM   3908 O O     . ALA B 2 387 ? 115.441 140.481 131.592 1.00 91.60  ? 387 ALA A O     1 
ATOM   3909 C CB    . ALA B 2 387 ? 115.499 137.718 133.161 1.00 91.60  ? 387 ALA A CB    1 
ATOM   3910 N N     . MET B 2 388 ? 117.482 140.242 132.498 1.00 93.95  ? 388 MET A N     1 
ATOM   3911 C CA    . MET B 2 388 ? 117.773 141.666 132.527 1.00 93.95  ? 388 MET A CA    1 
ATOM   3912 C C     . MET B 2 388 ? 118.169 142.208 131.169 1.00 93.95  ? 388 MET A C     1 
ATOM   3913 O O     . MET B 2 388 ? 118.594 143.364 131.074 1.00 93.95  ? 388 MET A O     1 
ATOM   3914 C CB    . MET B 2 388 ? 118.876 141.954 133.543 1.00 93.95  ? 388 MET A CB    1 
ATOM   3915 C CG    . MET B 2 388 ? 118.367 142.097 134.948 1.00 93.95  ? 388 MET A CG    1 
ATOM   3916 S SD    . MET B 2 388 ? 117.804 143.771 135.244 1.00 93.95  ? 388 MET A SD    1 
ATOM   3917 C CE    . MET B 2 388 ? 116.583 143.458 136.497 1.00 93.95  ? 388 MET A CE    1 
ATOM   3918 N N     . PHE B 2 389 ? 118.047 141.397 130.120 1.00 93.85  ? 389 PHE A N     1 
ATOM   3919 C CA    . PHE B 2 389 ? 118.322 141.838 128.762 1.00 93.85  ? 389 PHE A CA    1 
ATOM   3920 C C     . PHE B 2 389 ? 117.125 141.637 127.844 1.00 93.85  ? 389 PHE A C     1 
ATOM   3921 O O     . PHE B 2 389 ? 117.262 141.787 126.626 1.00 93.85  ? 389 PHE A O     1 
ATOM   3922 C CB    . PHE B 2 389 ? 119.546 141.114 128.195 1.00 93.85  ? 389 PHE A CB    1 
ATOM   3923 C CG    . PHE B 2 389 ? 120.851 141.644 128.708 1.00 93.85  ? 389 PHE A CG    1 
ATOM   3924 C CD1   . PHE B 2 389 ? 121.409 141.141 129.866 1.00 93.85  ? 389 PHE A CD1   1 
ATOM   3925 C CD2   . PHE B 2 389 ? 121.517 142.646 128.032 1.00 93.85  ? 389 PHE A CD2   1 
ATOM   3926 C CE1   . PHE B 2 389 ? 122.605 141.627 130.340 1.00 93.85  ? 389 PHE A CE1   1 
ATOM   3927 C CE2   . PHE B 2 389 ? 122.714 143.136 128.502 1.00 93.85  ? 389 PHE A CE2   1 
ATOM   3928 C CZ    . PHE B 2 389 ? 123.259 142.625 129.657 1.00 93.85  ? 389 PHE A CZ    1 
ATOM   3929 N N     . GLY B 2 390 ? 115.960 141.298 128.394 1.00 93.06  ? 390 GLY A N     1 
ATOM   3930 C CA    . GLY B 2 390 ? 114.732 141.223 127.650 1.00 93.06  ? 390 GLY A CA    1 
ATOM   3931 C C     . GLY B 2 390 ? 114.417 139.854 127.088 1.00 93.06  ? 390 GLY A C     1 
ATOM   3932 O O     . GLY B 2 390 ? 113.331 139.659 126.535 1.00 93.06  ? 390 GLY A O     1 
ATOM   3933 N N     . THR B 2 391 ? 115.336 138.907 127.208 1.00 87.13  ? 391 THR A N     1 
ATOM   3934 C CA    . THR B 2 391 ? 115.142 137.581 126.651 1.00 87.13  ? 391 THR A CA    1 
ATOM   3935 C C     . THR B 2 391 ? 115.441 136.513 127.692 1.00 87.13  ? 391 THR A C     1 
ATOM   3936 O O     . THR B 2 391 ? 116.132 136.752 128.685 1.00 87.13  ? 391 THR A O     1 
ATOM   3937 C CB    . THR B 2 391 ? 116.026 137.372 125.418 1.00 87.13  ? 391 THR A CB    1 
ATOM   3938 O OG1   . THR B 2 391 ? 115.881 136.028 124.946 1.00 87.13  ? 391 THR A OG1   1 
ATOM   3939 C CG2   . THR B 2 391 ? 117.480 137.633 125.757 1.00 87.13  ? 391 THR A CG2   1 
ATOM   3940 N N     . THR B 2 392 ? 114.902 135.339 127.453 1.00 83.33  ? 392 THR A N     1 
ATOM   3941 C CA    . THR B 2 392 ? 115.117 134.162 128.273 1.00 83.33  ? 392 THR A CA    1 
ATOM   3942 C C     . THR B 2 392 ? 116.288 133.358 127.731 1.00 83.33  ? 392 THR A C     1 
ATOM   3943 O O     . THR B 2 392 ? 116.633 133.470 126.553 1.00 83.33  ? 392 THR A O     1 
ATOM   3944 C CB    . THR B 2 392 ? 113.856 133.303 128.289 1.00 83.33  ? 392 THR A CB    1 
ATOM   3945 O OG1   . THR B 2 392 ? 113.548 132.888 126.954 1.00 83.33  ? 392 THR A OG1   1 
ATOM   3946 C CG2   . THR B 2 392 ? 112.686 134.088 128.849 1.00 83.33  ? 392 THR A CG2   1 
ATOM   3947 N N     . PRO B 2 393 ? 116.935 132.538 128.562 1.00 82.62  ? 393 PRO A N     1 
ATOM   3948 C CA    . PRO B 2 393 ? 118.029 131.707 128.042 1.00 82.62  ? 393 PRO A CA    1 
ATOM   3949 C C     . PRO B 2 393 ? 117.567 130.679 127.032 1.00 82.62  ? 393 PRO A C     1 
ATOM   3950 O O     . PRO B 2 393 ? 118.398 130.153 126.286 1.00 82.62  ? 393 PRO A O     1 
ATOM   3951 C CB    . PRO B 2 393 ? 118.599 131.047 129.302 1.00 82.62  ? 393 PRO A CB    1 
ATOM   3952 C CG    . PRO B 2 393 ? 117.477 131.055 130.263 1.00 82.62  ? 393 PRO A CG    1 
ATOM   3953 C CD    . PRO B 2 393 ? 116.740 132.333 130.006 1.00 82.62  ? 393 PRO A CD    1 
ATOM   3954 N N     . LEU B 2 394 ? 116.267 130.393 126.960 1.00 79.69  ? 394 LEU A N     1 
ATOM   3955 C CA    . LEU B 2 394 ? 115.762 129.514 125.913 1.00 79.69  ? 394 LEU A CA    1 
ATOM   3956 C C     . LEU B 2 394 ? 115.829 130.197 124.555 1.00 79.69  ? 394 LEU A C     1 
ATOM   3957 O O     . LEU B 2 394 ? 116.353 129.631 123.590 1.00 79.69  ? 394 LEU A O     1 
ATOM   3958 C CB    . LEU B 2 394 ? 114.331 129.085 126.230 1.00 79.69  ? 394 LEU A CB    1 
ATOM   3959 C CG    . LEU B 2 394 ? 113.569 128.362 125.122 1.00 79.69  ? 394 LEU A CG    1 
ATOM   3960 C CD1   . LEU B 2 394 ? 114.316 127.123 124.683 1.00 79.69  ? 394 LEU A CD1   1 
ATOM   3961 C CD2   . LEU B 2 394 ? 112.175 128.003 125.593 1.00 79.69  ? 394 LEU A CD2   1 
ATOM   3962 N N     . MET B 2 395 ? 115.299 131.418 124.460 1.00 80.85  ? 395 MET A N     1 
ATOM   3963 C CA    . MET B 2 395 ? 115.388 132.166 123.210 1.00 80.85  ? 395 MET A CA    1 
ATOM   3964 C C     . MET B 2 395 ? 116.835 132.480 122.862 1.00 80.85  ? 395 MET A C     1 
ATOM   3965 O O     . MET B 2 395 ? 117.223 132.450 121.691 1.00 80.85  ? 395 MET A O     1 
ATOM   3966 C CB    . MET B 2 395 ? 114.568 133.452 123.309 1.00 80.85  ? 395 MET A CB    1 
ATOM   3967 C CG    . MET B 2 395 ? 114.812 134.444 122.184 1.00 80.85  ? 395 MET A CG    1 
ATOM   3968 S SD    . MET B 2 395 ? 114.595 133.728 120.545 1.00 80.85  ? 395 MET A SD    1 
ATOM   3969 C CE    . MET B 2 395 ? 112.821 133.528 120.503 1.00 80.85  ? 395 MET A CE    1 
ATOM   3970 N N     . LEU B 2 396 ? 117.656 132.761 123.871 1.00 78.81  ? 396 LEU A N     1 
ATOM   3971 C CA    . LEU B 2 396 ? 119.056 133.064 123.605 1.00 78.81  ? 396 LEU A CA    1 
ATOM   3972 C C     . LEU B 2 396 ? 119.796 131.829 123.111 1.00 78.81  ? 396 LEU A C     1 
ATOM   3973 O O     . LEU B 2 396 ? 120.650 131.922 122.224 1.00 78.81  ? 396 LEU A O     1 
ATOM   3974 C CB    . LEU B 2 396 ? 119.714 133.630 124.860 1.00 78.81  ? 396 LEU A CB    1 
ATOM   3975 C CG    . LEU B 2 396 ? 121.002 134.407 124.620 1.00 78.81  ? 396 LEU A CG    1 
ATOM   3976 C CD1   . LEU B 2 396 ? 120.712 135.626 123.770 1.00 78.81  ? 396 LEU A CD1   1 
ATOM   3977 C CD2   . LEU B 2 396 ? 121.630 134.813 125.935 1.00 78.81  ? 396 LEU A CD2   1 
ATOM   3978 N N     . ALA B 2 397 ? 119.464 130.657 123.655 1.00 78.49  ? 397 ALA A N     1 
ATOM   3979 C CA    . ALA B 2 397 ? 120.066 129.422 123.166 1.00 78.49  ? 397 ALA A CA    1 
ATOM   3980 C C     . ALA B 2 397 ? 119.593 129.105 121.757 1.00 78.49  ? 397 ALA A C     1 
ATOM   3981 O O     . ALA B 2 397 ? 120.376 128.634 120.927 1.00 78.49  ? 397 ALA A O     1 
ATOM   3982 C CB    . ALA B 2 397 ? 119.743 128.268 124.111 1.00 78.49  ? 397 ALA A CB    1 
ATOM   3983 N N     . VAL B 2 398 ? 118.314 129.358 121.470 1.00 78.75  ? 398 VAL A N     1 
ATOM   3984 C CA    . VAL B 2 398 ? 117.803 129.191 120.112 1.00 78.75  ? 398 VAL A CA    1 
ATOM   3985 C C     . VAL B 2 398 ? 118.572 130.080 119.147 1.00 78.75  ? 398 VAL A C     1 
ATOM   3986 O O     . VAL B 2 398 ? 118.977 129.649 118.062 1.00 78.75  ? 398 VAL A O     1 
ATOM   3987 C CB    . VAL B 2 398 ? 116.295 129.492 120.067 1.00 78.75  ? 398 VAL A CB    1 
ATOM   3988 C CG1   . VAL B 2 398 ? 115.842 129.704 118.638 1.00 78.75  ? 398 VAL A CG1   1 
ATOM   3989 C CG2   . VAL B 2 398 ? 115.514 128.368 120.710 1.00 78.75  ? 398 VAL A CG2   1 
ATOM   3990 N N     . VAL B 2 399 ? 118.798 131.334 119.538 1.00 77.82  ? 399 VAL A N     1 
ATOM   3991 C CA    . VAL B 2 399 ? 119.486 132.281 118.666 1.00 77.82  ? 399 VAL A CA    1 
ATOM   3992 C C     . VAL B 2 399 ? 120.934 131.859 118.458 1.00 77.82  ? 399 VAL A C     1 
ATOM   3993 O O     . VAL B 2 399 ? 121.457 131.915 117.341 1.00 77.82  ? 399 VAL A O     1 
ATOM   3994 C CB    . VAL B 2 399 ? 119.388 133.704 119.240 1.00 77.82  ? 399 VAL A CB    1 
ATOM   3995 C CG1   . VAL B 2 399 ? 120.470 134.588 118.657 1.00 77.82  ? 399 VAL A CG1   1 
ATOM   3996 C CG2   . VAL B 2 399 ? 118.019 134.287 118.958 1.00 77.82  ? 399 VAL A CG2   1 
ATOM   3997 N N     . VAL B 2 400 ? 121.602 131.419 119.525 1.00 79.99  ? 400 VAL A N     1 
ATOM   3998 C CA    . VAL B 2 400 ? 123.005 131.031 119.400 1.00 79.99  ? 400 VAL A CA    1 
ATOM   3999 C C     . VAL B 2 400 ? 123.140 129.776 118.547 1.00 79.99  ? 400 VAL A C     1 
ATOM   4000 O O     . VAL B 2 400 ? 124.053 129.667 117.719 1.00 79.99  ? 400 VAL A O     1 
ATOM   4001 C CB    . VAL B 2 400 ? 123.636 130.846 120.791 1.00 79.99  ? 400 VAL A CB    1 
ATOM   4002 C CG1   . VAL B 2 400 ? 124.987 130.171 120.673 1.00 79.99  ? 400 VAL A CG1   1 
ATOM   4003 C CG2   . VAL B 2 400 ? 123.780 132.187 121.481 1.00 79.99  ? 400 VAL A CG2   1 
ATOM   4004 N N     . GLY B 2 401 ? 122.230 128.817 118.718 1.00 80.66  ? 401 GLY A N     1 
ATOM   4005 C CA    . GLY B 2 401 ? 122.268 127.628 117.886 1.00 80.66  ? 401 GLY A CA    1 
ATOM   4006 C C     . GLY B 2 401 ? 121.969 127.930 116.431 1.00 80.66  ? 401 GLY A C     1 
ATOM   4007 O O     . GLY B 2 401 ? 122.583 127.358 115.528 1.00 80.66  ? 401 GLY A O     1 
ATOM   4008 N N     . ALA B 2 402 ? 121.021 128.837 116.184 1.00 78.92  ? 402 ALA A N     1 
ATOM   4009 C CA    . ALA B 2 402 ? 120.745 129.256 114.817 1.00 78.92  ? 402 ALA A CA    1 
ATOM   4010 C C     . ALA B 2 402 ? 121.953 129.948 114.208 1.00 78.92  ? 402 ALA A C     1 
ATOM   4011 O O     . ALA B 2 402 ? 122.263 129.743 113.032 1.00 78.92  ? 402 ALA A O     1 
ATOM   4012 C CB    . ALA B 2 402 ? 119.528 130.177 114.784 1.00 78.92  ? 402 ALA A CB    1 
ATOM   4013 N N     . ILE B 2 403 ? 122.653 130.763 114.996 1.00 80.08  ? 403 ILE A N     1 
ATOM   4014 C CA    . ILE B 2 403 ? 123.848 131.439 114.502 1.00 80.08  ? 403 ILE A CA    1 
ATOM   4015 C C     . ILE B 2 403 ? 124.927 130.423 114.164 1.00 80.08  ? 403 ILE A C     1 
ATOM   4016 O O     . ILE B 2 403 ? 125.604 130.531 113.136 1.00 80.08  ? 403 ILE A O     1 
ATOM   4017 C CB    . ILE B 2 403 ? 124.341 132.467 115.535 1.00 80.08  ? 403 ILE A CB    1 
ATOM   4018 C CG1   . ILE B 2 403 ? 123.449 133.706 115.521 1.00 80.08  ? 403 ILE A CG1   1 
ATOM   4019 C CG2   . ILE B 2 403 ? 125.783 132.846 115.270 1.00 80.08  ? 403 ILE A CG2   1 
ATOM   4020 C CD1   . ILE B 2 403 ? 123.859 134.759 116.522 1.00 80.08  ? 403 ILE A CD1   1 
ATOM   4021 N N     . GLN B 2 404 ? 125.092 129.411 115.014 1.00 85.22  ? 404 GLN A N     1 
ATOM   4022 C CA    . GLN B 2 404 ? 126.088 128.378 114.751 1.00 85.22  ? 404 GLN A CA    1 
ATOM   4023 C C     . GLN B 2 404 ? 125.759 127.611 113.479 1.00 85.22  ? 404 GLN A C     1 
ATOM   4024 O O     . GLN B 2 404 ? 126.631 127.386 112.631 1.00 85.22  ? 404 GLN A O     1 
ATOM   4025 C CB    . GLN B 2 404 ? 126.177 127.429 115.943 1.00 85.22  ? 404 GLN A CB    1 
ATOM   4026 C CG    . GLN B 2 404 ? 127.286 126.412 115.830 1.00 85.22  ? 404 GLN A CG    1 
ATOM   4027 C CD    . GLN B 2 404 ? 126.756 125.014 115.655 1.00 85.22  ? 404 GLN A CD    1 
ATOM   4028 O OE1   . GLN B 2 404 ? 125.775 124.628 116.287 1.00 85.22  ? 404 GLN A OE1   1 
ATOM   4029 N NE2   . GLN B 2 404 ? 127.397 124.243 114.787 1.00 85.22  ? 404 GLN A NE2   1 
ATOM   4030 N N     . ASN B 2 405 ? 124.498 127.202 113.329 1.00 83.68  ? 405 ASN A N     1 
ATOM   4031 C CA    . ASN B 2 405 ? 124.093 126.469 112.135 1.00 83.68  ? 405 ASN A CA    1 
ATOM   4032 C C     . ASN B 2 405 ? 124.244 127.321 110.884 1.00 83.68  ? 405 ASN A C     1 
ATOM   4033 O O     . ASN B 2 405 ? 124.694 126.828 109.844 1.00 83.68  ? 405 ASN A O     1 
ATOM   4034 C CB    . ASN B 2 405 ? 122.653 125.987 112.281 1.00 83.68  ? 405 ASN A CB    1 
ATOM   4035 C CG    . ASN B 2 405 ? 122.564 124.585 112.830 1.00 83.68  ? 405 ASN A CG    1 
ATOM   4036 O OD1   . ASN B 2 405 ? 122.635 123.611 112.084 1.00 83.68  ? 405 ASN A OD1   1 
ATOM   4037 N ND2   . ASN B 2 405 ? 122.410 124.472 114.143 1.00 83.68  ? 405 ASN A ND2   1 
ATOM   4038 N N     . ILE B 2 406 ? 123.871 128.598 110.962 1.00 81.15  ? 406 ILE A N     1 
ATOM   4039 C CA    . ILE B 2 406 ? 123.993 129.487 109.813 1.00 81.15  ? 406 ILE A CA    1 
ATOM   4040 C C     . ILE B 2 406 ? 125.453 129.646 109.424 1.00 81.15  ? 406 ILE A C     1 
ATOM   4041 O O     . ILE B 2 406 ? 125.810 129.552 108.246 1.00 81.15  ? 406 ILE A O     1 
ATOM   4042 C CB    . ILE B 2 406 ? 123.339 130.845 110.118 1.00 81.15  ? 406 ILE A CB    1 
ATOM   4043 C CG1   . ILE B 2 406 ? 121.821 130.739 110.010 1.00 81.15  ? 406 ILE A CG1   1 
ATOM   4044 C CG2   . ILE B 2 406 ? 123.861 131.908 109.180 1.00 81.15  ? 406 ILE A CG2   1 
ATOM   4045 C CD1   . ILE B 2 406 ? 121.096 131.996 110.401 1.00 81.15  ? 406 ILE A CD1   1 
ATOM   4046 N N     . LEU B 2 407 ? 126.324 129.861 110.411 1.00 85.35  ? 407 LEU A N     1 
ATOM   4047 C CA    . LEU B 2 407 ? 127.737 130.052 110.115 1.00 85.35  ? 407 LEU A CA    1 
ATOM   4048 C C     . LEU B 2 407 ? 128.349 128.795 109.515 1.00 85.35  ? 407 LEU A C     1 
ATOM   4049 O O     . LEU B 2 407 ? 129.144 128.874 108.573 1.00 85.35  ? 407 LEU A O     1 
ATOM   4050 C CB    . LEU B 2 407 ? 128.483 130.463 111.380 1.00 85.35  ? 407 LEU A CB    1 
ATOM   4051 C CG    . LEU B 2 407 ? 128.356 131.935 111.763 1.00 85.35  ? 407 LEU A CG    1 
ATOM   4052 C CD1   . LEU B 2 407 ? 129.159 132.231 113.016 1.00 85.35  ? 407 LEU A CD1   1 
ATOM   4053 C CD2   . LEU B 2 407 ? 128.801 132.821 110.614 1.00 85.35  ? 407 LEU A CD2   1 
ATOM   4054 N N     . SER B 2 408 ? 127.970 127.622 110.026 1.00 89.08  ? 408 SER A N     1 
ATOM   4055 C CA    . SER B 2 408 ? 128.515 126.382 109.483 1.00 89.08  ? 408 SER A CA    1 
ATOM   4056 C C     . SER B 2 408 ? 128.025 126.142 108.060 1.00 89.08  ? 408 SER A C     1 
ATOM   4057 O O     . SER B 2 408 ? 128.829 125.960 107.137 1.00 89.08  ? 408 SER A O     1 
ATOM   4058 C CB    . SER B 2 408 ? 128.143 125.208 110.386 1.00 89.08  ? 408 SER A CB    1 
ATOM   4059 O OG    . SER B 2 408 ? 126.768 124.891 110.272 1.00 89.08  ? 408 SER A OG    1 
ATOM   4060 N N     . LYS B 2 409 ? 126.706 126.143 107.856 1.00 88.26  ? 409 LYS A N     1 
ATOM   4061 C CA    . LYS B 2 409 ? 126.164 125.903 106.526 1.00 88.26  ? 409 LYS A CA    1 
ATOM   4062 C C     . LYS B 2 409 ? 126.535 127.001 105.540 1.00 88.26  ? 409 LYS A C     1 
ATOM   4063 O O     . LYS B 2 409 ? 126.425 126.786 104.330 1.00 88.26  ? 409 LYS A O     1 
ATOM   4064 C CB    . LYS B 2 409 ? 124.644 125.756 106.593 1.00 88.26  ? 409 LYS A CB    1 
ATOM   4065 C CG    . LYS B 2 409 ? 124.170 124.667 107.537 1.00 88.26  ? 409 LYS A CG    1 
ATOM   4066 C CD    . LYS B 2 409 ? 122.796 124.153 107.147 1.00 88.26  ? 409 LYS A CD    1 
ATOM   4067 C CE    . LYS B 2 409 ? 122.839 123.431 105.810 1.00 88.26  ? 409 LYS A CE    1 
ATOM   4068 N NZ    . LYS B 2 409 ? 121.522 122.835 105.456 1.00 88.26  ? 409 LYS A NZ    1 
ATOM   4069 N N     . SER B 2 410 ? 126.976 128.162 106.022 1.00 90.71  ? 410 SER A N     1 
ATOM   4070 C CA    . SER B 2 410 ? 127.393 129.246 105.143 1.00 90.71  ? 410 SER A CA    1 
ATOM   4071 C C     . SER B 2 410 ? 128.867 129.127 104.775 1.00 90.71  ? 410 SER A C     1 
ATOM   4072 O O     . SER B 2 410 ? 129.207 128.974 103.599 1.00 90.71  ? 410 SER A O     1 
ATOM   4073 C CB    . SER B 2 410 ? 127.114 130.593 105.814 1.00 90.71  ? 410 SER A CB    1 
ATOM   4074 O OG    . SER B 2 410 ? 127.564 131.659 105.003 1.00 90.71  ? 410 SER A OG    1 
ATOM   4075 N N     . THR B 2 411 ? 129.751 129.194 105.766 1.00 97.84  ? 411 THR A N     1 
ATOM   4076 C CA    . THR B 2 411 ? 131.174 129.012 105.499 1.00 97.84  ? 411 THR A CA    1 
ATOM   4077 C C     . THR B 2 411 ? 131.586 127.556 105.659 1.00 97.84  ? 411 THR A C     1 
ATOM   4078 O O     . THR B 2 411 ? 132.585 127.243 106.301 1.00 97.84  ? 411 THR A O     1 
ATOM   4079 C CB    . THR B 2 411 ? 131.997 129.903 106.418 1.00 97.84  ? 411 THR A CB    1 
ATOM   4080 O OG1   . THR B 2 411 ? 131.883 129.428 107.764 1.00 97.84  ? 411 THR A OG1   1 
ATOM   4081 C CG2   . THR B 2 411 ? 131.512 131.334 106.356 1.00 97.84  ? 411 THR A CG2   1 
ATOM   4082 N N     . LYS B 2 412 ? 130.804 126.649 105.080 1.00 101.68 ? 412 LYS A N     1 
ATOM   4083 C CA    . LYS B 2 412 ? 131.339 125.337 104.745 1.00 101.68 ? 412 LYS A CA    1 
ATOM   4084 C C     . LYS B 2 412 ? 131.976 125.363 103.362 1.00 101.68 ? 412 LYS A C     1 
ATOM   4085 O O     . LYS B 2 412 ? 133.185 125.161 103.233 1.00 101.68 ? 412 LYS A O     1 
ATOM   4086 C CB    . LYS B 2 412 ? 130.239 124.274 104.808 1.00 101.68 ? 412 LYS A CB    1 
ATOM   4087 C CG    . LYS B 2 412 ? 130.731 122.878 104.460 1.00 101.68 ? 412 LYS A CG    1 
ATOM   4088 C CD    . LYS B 2 412 ? 129.593 121.877 104.378 1.00 101.68 ? 412 LYS A CD    1 
ATOM   4089 C CE    . LYS B 2 412 ? 130.101 120.507 103.963 1.00 101.68 ? 412 LYS A CE    1 
ATOM   4090 N NZ    . LYS B 2 412 ? 128.991 119.531 103.787 1.00 101.68 ? 412 LYS A NZ    1 
ATOM   4091 N N     . TYR B 2 413 ? 131.182 125.674 102.336 1.00 110.76 ? 413 TYR A N     1 
ATOM   4092 C CA    . TYR B 2 413 ? 131.652 125.620 100.956 1.00 110.76 ? 413 TYR A CA    1 
ATOM   4093 C C     . TYR B 2 413 ? 132.844 126.531 100.700 1.00 110.76 ? 413 TYR A C     1 
ATOM   4094 O O     . TYR B 2 413 ? 133.613 126.277 99.767  1.00 110.76 ? 413 TYR A O     1 
ATOM   4095 C CB    . TYR B 2 413 ? 130.505 125.985 100.012 1.00 110.76 ? 413 TYR A CB    1 
ATOM   4096 C CG    . TYR B 2 413 ? 130.853 125.900 98.544  1.00 110.76 ? 413 TYR A CG    1 
ATOM   4097 C CD1   . TYR B 2 413 ? 130.953 124.672 97.903  1.00 110.76 ? 413 TYR A CD1   1 
ATOM   4098 C CD2   . TYR B 2 413 ? 131.075 127.049 97.795  1.00 110.76 ? 413 TYR A CD2   1 
ATOM   4099 C CE1   . TYR B 2 413 ? 131.267 124.590 96.560  1.00 110.76 ? 413 TYR A CE1   1 
ATOM   4100 C CE2   . TYR B 2 413 ? 131.389 126.977 96.451  1.00 110.76 ? 413 TYR A CE2   1 
ATOM   4101 C CZ    . TYR B 2 413 ? 131.484 125.744 95.839  1.00 110.76 ? 413 TYR A CZ    1 
ATOM   4102 O OH    . TYR B 2 413 ? 131.797 125.665 94.501  1.00 110.76 ? 413 TYR A OH    1 
ATOM   4103 N N     . ALA B 2 414 ? 133.024 127.580 101.503 1.00 108.01 ? 414 ALA A N     1 
ATOM   4104 C CA    . ALA B 2 414 ? 134.095 128.537 101.279 1.00 108.01 ? 414 ALA A CA    1 
ATOM   4105 C C     . ALA B 2 414 ? 135.264 128.396 102.238 1.00 108.01 ? 414 ALA A C     1 
ATOM   4106 O O     . ALA B 2 414 ? 136.326 128.966 101.971 1.00 108.01 ? 414 ALA A O     1 
ATOM   4107 C CB    . ALA B 2 414 ? 133.559 129.972 101.375 1.00 108.01 ? 414 ALA A CB    1 
ATOM   4108 N N     . LEU B 2 415 ? 135.105 127.670 103.336 1.00 104.23 ? 415 LEU A N     1 
ATOM   4109 C CA    . LEU B 2 415 ? 136.166 127.558 104.326 1.00 104.23 ? 415 LEU A CA    1 
ATOM   4110 C C     . LEU B 2 415 ? 136.603 126.131 104.602 1.00 104.23 ? 415 LEU A C     1 
ATOM   4111 O O     . LEU B 2 415 ? 137.798 125.884 104.757 1.00 104.23 ? 415 LEU A O     1 
ATOM   4112 C CB    . LEU B 2 415 ? 135.728 128.215 105.637 1.00 104.23 ? 415 LEU A CB    1 
ATOM   4113 C CG    . LEU B 2 415 ? 136.223 129.646 105.813 1.00 104.23 ? 415 LEU A CG    1 
ATOM   4114 C CD1   . LEU B 2 415 ? 135.556 130.297 107.001 1.00 104.23 ? 415 LEU A CD1   1 
ATOM   4115 C CD2   . LEU B 2 415 ? 137.726 129.644 105.983 1.00 104.23 ? 415 LEU A CD2   1 
ATOM   4116 N N     . PHE B 2 416 ? 135.676 125.180 104.672 1.00 104.28 ? 416 PHE A N     1 
ATOM   4117 C CA    . PHE B 2 416 ? 136.038 123.810 105.001 1.00 104.28 ? 416 PHE A CA    1 
ATOM   4118 C C     . PHE B 2 416 ? 136.283 122.974 103.751 1.00 104.28 ? 416 PHE A C     1 
ATOM   4119 O O     . PHE B 2 416 ? 137.316 122.307 103.641 1.00 104.28 ? 416 PHE A O     1 
ATOM   4120 C CB    . PHE B 2 416 ? 134.945 123.176 105.861 1.00 104.28 ? 416 PHE A CB    1 
ATOM   4121 C CG    . PHE B 2 416 ? 135.185 121.733 106.170 1.00 104.28 ? 416 PHE A CG    1 
ATOM   4122 C CD1   . PHE B 2 416 ? 136.319 121.341 106.854 1.00 104.28 ? 416 PHE A CD1   1 
ATOM   4123 C CD2   . PHE B 2 416 ? 134.278 120.770 105.777 1.00 104.28 ? 416 PHE A CD2   1 
ATOM   4124 C CE1   . PHE B 2 416 ? 136.543 120.014 107.140 1.00 104.28 ? 416 PHE A CE1   1 
ATOM   4125 C CE2   . PHE B 2 416 ? 134.497 119.442 106.060 1.00 104.28 ? 416 PHE A CE2   1 
ATOM   4126 C CZ    . PHE B 2 416 ? 135.632 119.063 106.743 1.00 104.28 ? 416 PHE A CZ    1 
ATOM   4127 N N     . ASP B 2 417 ? 135.338 122.992 102.808 1.00 108.88 ? 417 ASP A N     1 
ATOM   4128 C CA    . ASP B 2 417 ? 135.534 122.279 101.552 1.00 108.88 ? 417 ASP A CA    1 
ATOM   4129 C C     . ASP B 2 417 ? 136.705 122.856 100.770 1.00 108.88 ? 417 ASP A C     1 
ATOM   4130 O O     . ASP B 2 417 ? 137.449 122.116 100.111 1.00 108.88 ? 417 ASP A O     1 
ATOM   4131 C CB    . ASP B 2 417 ? 134.256 122.329 100.717 1.00 108.88 ? 417 ASP A CB    1 
ATOM   4132 C CG    . ASP B 2 417 ? 133.183 121.397 101.238 1.00 108.88 ? 417 ASP A CG    1 
ATOM   4133 O OD1   . ASP B 2 417 ? 133.419 120.736 102.269 1.00 108.88 ? 417 ASP A OD1   1 
ATOM   4134 O OD2   . ASP B 2 417 ? 132.102 121.325 100.617 1.00 108.88 ? 417 ASP A OD2   1 
ATOM   4135 N N     . SER B 2 418 ? 136.886 124.175 100.831 1.00 109.84 ? 418 SER A N     1 
ATOM   4136 C CA    . SER B 2 418 ? 137.976 124.819 100.116 1.00 109.84 ? 418 SER A CA    1 
ATOM   4137 C C     . SER B 2 418 ? 139.341 124.425 100.654 1.00 109.84 ? 418 SER A C     1 
ATOM   4138 O O     . SER B 2 418 ? 140.306 124.401 99.884  1.00 109.84 ? 418 SER A O     1 
ATOM   4139 C CB    . SER B 2 418 ? 137.817 126.335 100.175 1.00 109.84 ? 418 SER A CB    1 
ATOM   4140 O OG    . SER B 2 418 ? 138.882 126.975 99.499  1.00 109.84 ? 418 SER A OG    1 
ATOM   4141 N N     . THR B 2 419 ? 139.448 124.117 101.944 1.00 108.97 ? 419 THR A N     1 
ATOM   4142 C CA    . THR B 2 419 ? 140.691 123.618 102.518 1.00 108.97 ? 419 THR A CA    1 
ATOM   4143 C C     . THR B 2 419 ? 140.855 122.118 102.340 1.00 108.97 ? 419 THR A C     1 
ATOM   4144 O O     . THR B 2 419 ? 141.978 121.645 102.160 1.00 108.97 ? 419 THR A O     1 
ATOM   4145 C CB    . THR B 2 419 ? 140.774 123.969 104.005 1.00 108.97 ? 419 THR A CB    1 
ATOM   4146 O OG1   . THR B 2 419 ? 139.633 123.439 104.689 1.00 108.97 ? 419 THR A OG1   1 
ATOM   4147 C CG2   . THR B 2 419 ? 140.835 125.472 104.191 1.00 108.97 ? 419 THR A CG2   1 
ATOM   4148 N N     . LYS B 2 420 ? 139.757 121.361 102.367 1.00 113.34 ? 420 LYS A N     1 
ATOM   4149 C CA    . LYS B 2 420 ? 139.808 119.949 102.006 1.00 113.34 ? 420 LYS A CA    1 
ATOM   4150 C C     . LYS B 2 420 ? 140.403 119.764 100.615 1.00 113.34 ? 420 LYS A C     1 
ATOM   4151 O O     . LYS B 2 420 ? 141.432 119.099 100.436 1.00 113.34 ? 420 LYS A O     1 
ATOM   4152 C CB    . LYS B 2 420 ? 138.402 119.353 102.057 1.00 113.34 ? 420 LYS A CB    1 
ATOM   4153 C CG    . LYS B 2 420 ? 138.061 118.614 103.330 1.00 113.34 ? 420 LYS A CG    1 
ATOM   4154 C CD    . LYS B 2 420 ? 136.620 118.130 103.286 1.00 113.34 ? 420 LYS A CD    1 
ATOM   4155 C CE    . LYS B 2 420 ? 136.271 117.559 101.919 1.00 113.34 ? 420 LYS A CE    1 
ATOM   4156 N NZ    . LYS B 2 420 ? 134.803 117.528 101.681 1.00 113.34 ? 420 LYS A NZ    1 
ATOM   4157 N N     . GLU B 2 421 ? 139.754 120.356 99.612  1.00 118.32 ? 421 GLU A N     1 
ATOM   4158 C CA    . GLU B 2 421 ? 140.221 120.193 98.242  1.00 118.32 ? 421 GLU A CA    1 
ATOM   4159 C C     . GLU B 2 421 ? 141.608 120.789 98.045  1.00 118.32 ? 421 GLU A C     1 
ATOM   4160 O O     . GLU B 2 421 ? 142.382 120.288 97.221  1.00 118.32 ? 421 GLU A O     1 
ATOM   4161 C CB    . GLU B 2 421 ? 139.217 120.806 97.269  1.00 118.32 ? 421 GLU A CB    1 
ATOM   4162 C CG    . GLU B 2 421 ? 137.902 120.043 97.205  1.00 118.32 ? 421 GLU A CG    1 
ATOM   4163 C CD    . GLU B 2 421 ? 136.917 120.651 96.230  1.00 118.32 ? 421 GLU A CD    1 
ATOM   4164 O OE1   . GLU B 2 421 ? 137.204 121.743 95.699  1.00 118.32 ? 421 GLU A OE1   1 
ATOM   4165 O OE2   . GLU B 2 421 ? 135.858 120.034 95.989  1.00 118.32 ? 421 GLU A OE2   1 
ATOM   4166 N N     . MET B 2 422 ? 141.944 121.847 98.786  1.00 117.86 ? 422 MET A N     1 
ATOM   4167 C CA    . MET B 2 422 ? 143.298 122.383 98.714  1.00 117.86 ? 422 MET A CA    1 
ATOM   4168 C C     . MET B 2 422 ? 144.316 121.402 99.281  1.00 117.86 ? 422 MET A C     1 
ATOM   4169 O O     . MET B 2 422 ? 145.444 121.323 98.783  1.00 117.86 ? 422 MET A O     1 
ATOM   4170 C CB    . MET B 2 422 ? 143.375 123.720 99.449  1.00 117.86 ? 422 MET A CB    1 
ATOM   4171 C CG    . MET B 2 422 ? 144.743 124.376 99.420  1.00 117.86 ? 422 MET A CG    1 
ATOM   4172 S SD    . MET B 2 422 ? 144.663 126.137 99.788  1.00 117.86 ? 422 MET A SD    1 
ATOM   4173 C CE    . MET B 2 422 ? 143.546 126.694 98.507  1.00 117.86 ? 422 MET A CE    1 
ATOM   4174 N N     . ALA B 2 423 ? 143.938 120.645 100.312 1.00 121.20 ? 423 ALA A N     1 
ATOM   4175 C CA    . ALA B 2 423 ? 144.824 119.611 100.831 1.00 121.20 ? 423 ALA A CA    1 
ATOM   4176 C C     . ALA B 2 423 ? 144.940 118.445 99.863  1.00 121.20 ? 423 ALA A C     1 
ATOM   4177 O O     . ALA B 2 423 ? 145.962 117.752 99.848  1.00 121.20 ? 423 ALA A O     1 
ATOM   4178 C CB    . ALA B 2 423 ? 144.329 119.123 102.192 1.00 121.20 ? 423 ALA A CB    1 
ATOM   4179 N N     . TYR B 2 424 ? 143.905 118.208 99.057  1.00 125.92 ? 424 TYR A N     1 
ATOM   4180 C CA    . TYR B 2 424 ? 143.985 117.165 98.039  1.00 125.92 ? 424 TYR A CA    1 
ATOM   4181 C C     . TYR B 2 424 ? 144.998 117.473 96.942  1.00 125.92 ? 424 TYR A C     1 
ATOM   4182 O O     . TYR B 2 424 ? 145.292 116.585 96.136  1.00 125.92 ? 424 TYR A O     1 
ATOM   4183 C CB    . TYR B 2 424 ? 142.616 116.944 97.396  1.00 125.92 ? 424 TYR A CB    1 
ATOM   4184 C CG    . TYR B 2 424 ? 141.639 116.172 98.247  1.00 125.92 ? 424 TYR A CG    1 
ATOM   4185 C CD1   . TYR B 2 424 ? 142.074 115.192 99.125  1.00 125.92 ? 424 TYR A CD1   1 
ATOM   4186 C CD2   . TYR B 2 424 ? 140.278 116.426 98.171  1.00 125.92 ? 424 TYR A CD2   1 
ATOM   4187 C CE1   . TYR B 2 424 ? 141.178 114.485 99.902  1.00 125.92 ? 424 TYR A CE1   1 
ATOM   4188 C CE2   . TYR B 2 424 ? 139.377 115.727 98.945  1.00 125.92 ? 424 TYR A CE2   1 
ATOM   4189 C CZ    . TYR B 2 424 ? 139.832 114.759 99.808  1.00 125.92 ? 424 TYR A CZ    1 
ATOM   4190 O OH    . TYR B 2 424 ? 138.931 114.063 100.578 1.00 125.92 ? 424 TYR A OH    1 
ATOM   4191 N N     . ILE B 2 425 ? 145.537 118.687 96.889  1.00 124.97 ? 425 ILE A N     1 
ATOM   4192 C CA    . ILE B 2 425 ? 146.350 119.129 95.756  1.00 124.97 ? 425 ILE A CA    1 
ATOM   4193 C C     . ILE B 2 425 ? 147.747 118.512 95.755  1.00 124.97 ? 425 ILE A C     1 
ATOM   4194 O O     . ILE B 2 425 ? 148.108 117.850 94.772  1.00 124.97 ? 425 ILE A O     1 
ATOM   4195 C CB    . ILE B 2 425 ? 146.434 120.663 95.703  1.00 124.97 ? 425 ILE A CB    1 
ATOM   4196 C CG1   . ILE B 2 425 ? 145.040 121.271 95.544  1.00 124.97 ? 425 ILE A CG1   1 
ATOM   4197 C CG2   . ILE B 2 425 ? 147.346 121.108 94.573  1.00 124.97 ? 425 ILE A CG2   1 
ATOM   4198 C CD1   . ILE B 2 425 ? 144.203 120.617 94.466  1.00 124.97 ? 425 ILE A CD1   1 
ATOM   4199 N N     . PRO B 2 426 ? 148.572 118.684 96.796  1.00 128.35 ? 426 PRO A N     1 
ATOM   4200 C CA    . PRO B 2 426 ? 149.986 118.290 96.676  1.00 128.35 ? 426 PRO A CA    1 
ATOM   4201 C C     . PRO B 2 426 ? 150.218 116.792 96.561  1.00 128.35 ? 426 PRO A C     1 
ATOM   4202 O O     . PRO B 2 426 ? 151.377 116.370 96.493  1.00 128.35 ? 426 PRO A O     1 
ATOM   4203 C CB    . PRO B 2 426 ? 150.619 118.841 97.967  1.00 128.35 ? 426 PRO A CB    1 
ATOM   4204 C CG    . PRO B 2 426 ? 149.580 119.719 98.590  1.00 128.35 ? 426 PRO A CG    1 
ATOM   4205 C CD    . PRO B 2 426 ? 148.275 119.158 98.157  1.00 128.35 ? 426 PRO A CD    1 
ATOM   4206 N N     . LEU B 2 427 ? 149.169 115.978 96.538  1.00 134.07 ? 427 LEU A N     1 
ATOM   4207 C CA    . LEU B 2 427 ? 149.328 114.538 96.423  1.00 134.07 ? 427 LEU A CA    1 
ATOM   4208 C C     . LEU B 2 427 ? 149.538 114.132 94.969  1.00 134.07 ? 427 LEU A C     1 
ATOM   4209 O O     . LEU B 2 427 ? 149.138 114.838 94.039  1.00 134.07 ? 427 LEU A O     1 
ATOM   4210 C CB    . LEU B 2 427 ? 148.100 113.822 96.985  1.00 134.07 ? 427 LEU A CB    1 
ATOM   4211 C CG    . LEU B 2 427 ? 147.735 114.124 98.438  1.00 134.07 ? 427 LEU A CG    1 
ATOM   4212 C CD1   . LEU B 2 427 ? 146.691 113.144 98.934  1.00 134.07 ? 427 LEU A CD1   1 
ATOM   4213 C CD2   . LEU B 2 427 ? 148.967 114.083 99.321  1.00 134.07 ? 427 LEU A CD2   1 
ATOM   4214 N N     . ASP B 2 428 ? 150.178 112.980 94.780  1.00 140.94 ? 428 ASP A N     1 
ATOM   4215 C CA    . ASP B 2 428 ? 150.294 112.405 93.450  1.00 140.94 ? 428 ASP A CA    1 
ATOM   4216 C C     . ASP B 2 428 ? 148.930 111.917 92.970  1.00 140.94 ? 428 ASP A C     1 
ATOM   4217 O O     . ASP B 2 428 ? 148.064 111.545 93.764  1.00 140.94 ? 428 ASP A O     1 
ATOM   4218 C CB    . ASP B 2 428 ? 151.302 111.257 93.444  1.00 140.94 ? 428 ASP A CB    1 
ATOM   4219 C CG    . ASP B 2 428 ? 152.607 111.624 94.120  1.00 140.94 ? 428 ASP A CG    1 
ATOM   4220 O OD1   . ASP B 2 428 ? 153.279 112.563 93.644  1.00 140.94 ? 428 ASP A OD1   1 
ATOM   4221 O OD2   . ASP B 2 428 ? 152.961 110.975 95.125  1.00 140.94 ? 428 ASP A OD2   1 
ATOM   4222 N N     . GLN B 2 429 ? 148.756 111.909 91.644  1.00 142.92 ? 429 GLN A N     1 
ATOM   4223 C CA    . GLN B 2 429 ? 147.433 111.697 91.059  1.00 142.92 ? 429 GLN A CA    1 
ATOM   4224 C C     . GLN B 2 429 ? 146.791 110.406 91.550  1.00 142.92 ? 429 GLN A C     1 
ATOM   4225 O O     . GLN B 2 429 ? 145.599 110.387 91.881  1.00 142.92 ? 429 GLN A O     1 
ATOM   4226 C CB    . GLN B 2 429 ? 147.527 111.695 89.532  1.00 142.92 ? 429 GLN A CB    1 
ATOM   4227 C CG    . GLN B 2 429 ? 146.239 111.293 88.806  1.00 142.92 ? 429 GLN A CG    1 
ATOM   4228 C CD    . GLN B 2 429 ? 145.053 112.212 89.084  1.00 142.92 ? 429 GLN A CD    1 
ATOM   4229 O OE1   . GLN B 2 429 ? 145.171 113.223 89.777  1.00 142.92 ? 429 GLN A OE1   1 
ATOM   4230 N NE2   . GLN B 2 429 ? 143.897 111.855 88.537  1.00 142.92 ? 429 GLN A NE2   1 
ATOM   4231 N N     . GLU B 2 430 ? 147.562 109.319 91.605  1.00 144.35 ? 430 GLU A N     1 
ATOM   4232 C CA    . GLU B 2 430 ? 147.027 108.039 92.059  1.00 144.35 ? 430 GLU A CA    1 
ATOM   4233 C C     . GLU B 2 430 ? 146.452 108.152 93.465  1.00 144.35 ? 430 GLU A C     1 
ATOM   4234 O O     . GLU B 2 430 ? 145.248 107.958 93.681  1.00 144.35 ? 430 GLU A O     1 
ATOM   4235 C CB    . GLU B 2 430 ? 148.121 106.970 92.003  1.00 144.35 ? 430 GLU A CB    1 
ATOM   4236 C CG    . GLU B 2 430 ? 147.677 105.593 92.474  1.00 144.35 ? 430 GLU A CG    1 
ATOM   4237 C CD    . GLU B 2 430 ? 148.009 105.339 93.933  1.00 144.35 ? 430 GLU A CD    1 
ATOM   4238 O OE1   . GLU B 2 430 ? 147.278 104.564 94.585  1.00 144.35 ? 430 GLU A OE1   1 
ATOM   4239 O OE2   . GLU B 2 430 ? 149.001 105.914 94.427  1.00 144.35 ? 430 GLU A OE2   1 
ATOM   4240 N N     . GLN B 2 431 ? 147.312 108.469 94.438  1.00 140.54 ? 431 GLN A N     1 
ATOM   4241 C CA    . GLN B 2 431 ? 146.852 108.594 95.814  1.00 140.54 ? 431 GLN A CA    1 
ATOM   4242 C C     . GLN B 2 431 ? 145.835 109.715 95.947  1.00 140.54 ? 431 GLN A C     1 
ATOM   4243 O O     . GLN B 2 431 ? 144.905 109.620 96.749  1.00 140.54 ? 431 GLN A O     1 
ATOM   4244 C CB    . GLN B 2 431 ? 148.035 108.820 96.758  1.00 140.54 ? 431 GLN A CB    1 
ATOM   4245 C CG    . GLN B 2 431 ? 148.786 110.123 96.547  1.00 140.54 ? 431 GLN A CG    1 
ATOM   4246 C CD    . GLN B 2 431 ? 149.847 110.360 97.603  1.00 140.54 ? 431 GLN A CD    1 
ATOM   4247 O OE1   . GLN B 2 431 ? 149.966 109.598 98.562  1.00 140.54 ? 431 GLN A OE1   1 
ATOM   4248 N NE2   . GLN B 2 431 ? 150.624 111.422 97.433  1.00 140.54 ? 431 GLN A NE2   1 
ATOM   4249 N N     . LYS B 2 432 ? 145.967 110.766 95.135  1.00 138.89 ? 432 LYS A N     1 
ATOM   4250 C CA    . LYS B 2 432 ? 144.998 111.856 95.168  1.00 138.89 ? 432 LYS A CA    1 
ATOM   4251 C C     . LYS B 2 432 ? 143.590 111.341 94.904  1.00 138.89 ? 432 LYS A C     1 
ATOM   4252 O O     . LYS B 2 432 ? 142.701 111.463 95.755  1.00 138.89 ? 432 LYS A O     1 
ATOM   4253 C CB    . LYS B 2 432 ? 145.379 112.929 94.147  1.00 138.89 ? 432 LYS A CB    1 
ATOM   4254 C CG    . LYS B 2 432 ? 144.448 114.125 94.114  1.00 138.89 ? 432 LYS A CG    1 
ATOM   4255 C CD    . LYS B 2 432 ? 144.916 115.145 93.090  1.00 138.89 ? 432 LYS A CD    1 
ATOM   4256 C CE    . LYS B 2 432 ? 143.953 116.314 92.983  1.00 138.89 ? 432 LYS A CE    1 
ATOM   4257 N NZ    . LYS B 2 432 ? 144.360 117.267 91.914  1.00 138.89 ? 432 LYS A NZ    1 
ATOM   4258 N N     . VAL B 2 433 ? 143.374 110.745 93.729  1.00 140.76 ? 433 VAL A N     1 
ATOM   4259 C CA    . VAL B 2 433 ? 142.028 110.318 93.357  1.00 140.76 ? 433 VAL A CA    1 
ATOM   4260 C C     . VAL B 2 433 ? 141.555 109.182 94.256  1.00 140.76 ? 433 VAL A C     1 
ATOM   4261 O O     . VAL B 2 433 ? 140.382 109.137 94.651  1.00 140.76 ? 433 VAL A O     1 
ATOM   4262 C CB    . VAL B 2 433 ? 141.971 109.935 91.864  1.00 140.76 ? 433 VAL A CB    1 
ATOM   4263 C CG1   . VAL B 2 433 ? 142.894 108.764 91.556  1.00 140.76 ? 433 VAL A CG1   1 
ATOM   4264 C CG2   . VAL B 2 433 ? 140.541 109.621 91.449  1.00 140.76 ? 433 VAL A CG2   1 
ATOM   4265 N N     . LYS B 2 434 ? 142.456 108.269 94.631  1.00 141.57 ? 434 LYS A N     1 
ATOM   4266 C CA    . LYS B 2 434 ? 142.029 107.125 95.430  1.00 141.57 ? 434 LYS A CA    1 
ATOM   4267 C C     . LYS B 2 434 ? 141.635 107.554 96.838  1.00 141.57 ? 434 LYS A C     1 
ATOM   4268 O O     . LYS B 2 434 ? 140.591 107.142 97.354  1.00 141.57 ? 434 LYS A O     1 
ATOM   4269 C CB    . LYS B 2 434 ? 143.122 106.055 95.455  1.00 141.57 ? 434 LYS A CB    1 
ATOM   4270 C CG    . LYS B 2 434 ? 143.387 105.435 94.084  1.00 141.57 ? 434 LYS A CG    1 
ATOM   4271 C CD    . LYS B 2 434 ? 142.186 104.622 93.598  1.00 141.57 ? 434 LYS A CD    1 
ATOM   4272 C CE    . LYS B 2 434 ? 142.418 104.048 92.203  1.00 141.57 ? 434 LYS A CE    1 
ATOM   4273 N NZ    . LYS B 2 434 ? 143.477 103.001 92.188  1.00 141.57 ? 434 LYS A NZ    1 
ATOM   4274 N N     . GLY B 2 435 ? 142.447 108.400 97.474  1.00 138.24 ? 435 GLY A N     1 
ATOM   4275 C CA    . GLY B 2 435 ? 142.089 108.910 98.781  1.00 138.24 ? 435 GLY A CA    1 
ATOM   4276 C C     . GLY B 2 435 ? 140.880 109.819 98.754  1.00 138.24 ? 435 GLY A C     1 
ATOM   4277 O O     . GLY B 2 435 ? 140.094 109.829 99.700  1.00 138.24 ? 435 GLY A O     1 
ATOM   4278 N N     . LYS B 2 436 ? 140.706 110.595 97.680  1.00 134.89 ? 436 LYS A N     1 
ATOM   4279 C CA    . LYS B 2 436 ? 139.505 111.415 97.571  1.00 134.89 ? 436 LYS A CA    1 
ATOM   4280 C C     . LYS B 2 436 ? 138.262 110.544 97.503  1.00 134.89 ? 436 LYS A C     1 
ATOM   4281 O O     . LYS B 2 436 ? 137.266 110.812 98.188  1.00 134.89 ? 436 LYS A O     1 
ATOM   4282 C CB    . LYS B 2 436 ? 139.589 112.324 96.346  1.00 134.89 ? 436 LYS A CB    1 
ATOM   4283 C CG    . LYS B 2 436 ? 138.511 113.395 96.307  1.00 134.89 ? 436 LYS A CG    1 
ATOM   4284 C CD    . LYS B 2 436 ? 138.735 114.373 95.171  1.00 134.89 ? 436 LYS A CD    1 
ATOM   4285 C CE    . LYS B 2 436 ? 137.831 115.585 95.312  1.00 134.89 ? 436 LYS A CE    1 
ATOM   4286 N NZ    . LYS B 2 436 ? 136.395 115.198 95.392  1.00 134.89 ? 436 LYS A NZ    1 
ATOM   4287 N N     . ALA B 2 437 ? 138.304 109.492 96.681  1.00 138.51 ? 437 ALA A N     1 
ATOM   4288 C CA    . ALA B 2 437 ? 137.197 108.546 96.638  1.00 138.51 ? 437 ALA A CA    1 
ATOM   4289 C C     . ALA B 2 437 ? 136.979 107.899 97.998  1.00 138.51 ? 437 ALA A C     1 
ATOM   4290 O O     . ALA B 2 437 ? 135.838 107.742 98.439  1.00 138.51 ? 437 ALA A O     1 
ATOM   4291 C CB    . ALA B 2 437 ? 137.455 107.483 95.571  1.00 138.51 ? 437 ALA A CB    1 
ATOM   4292 N N     . ALA B 2 438 ? 138.066 107.536 98.683  1.00 139.98 ? 438 ALA A N     1 
ATOM   4293 C CA    . ALA B 2 438 ? 137.952 106.894 99.989  1.00 139.98 ? 438 ALA A CA    1 
ATOM   4294 C C     . ALA B 2 438 ? 137.248 107.800 100.991 1.00 139.98 ? 438 ALA A C     1 
ATOM   4295 O O     . ALA B 2 438 ? 136.294 107.385 101.661 1.00 139.98 ? 438 ALA A O     1 
ATOM   4296 C CB    . ALA B 2 438 ? 139.340 106.506 100.497 1.00 139.98 ? 438 ALA A CB    1 
ATOM   4297 N N     . ILE B 2 439 ? 137.720 109.042 101.120 1.00 134.65 ? 439 ILE A N     1 
ATOM   4298 C CA    . ILE B 2 439 ? 137.070 109.989 102.018 1.00 134.65 ? 439 ILE A CA    1 
ATOM   4299 C C     . ILE B 2 439 ? 135.610 110.169 101.637 1.00 134.65 ? 439 ILE A C     1 
ATOM   4300 O O     . ILE B 2 439 ? 134.718 109.973 102.469 1.00 134.65 ? 439 ILE A O     1 
ATOM   4301 C CB    . ILE B 2 439 ? 137.804 111.343 102.031 1.00 134.65 ? 439 ILE A CB    1 
ATOM   4302 C CG1   . ILE B 2 439 ? 139.298 111.156 102.282 1.00 134.65 ? 439 ILE A CG1   1 
ATOM   4303 C CG2   . ILE B 2 439 ? 137.213 112.250 103.087 1.00 134.65 ? 439 ILE A CG2   1 
ATOM   4304 C CD1   . ILE B 2 439 ? 139.615 110.301 103.469 1.00 134.65 ? 439 ILE A CD1   1 
ATOM   4305 N N     . ASP B 2 440 ? 135.331 110.519 100.382 1.00 139.20 ? 440 ASP A N     1 
ATOM   4306 C CA    . ASP B 2 440 ? 133.962 110.834 100.007 1.00 139.20 ? 440 ASP A CA    1 
ATOM   4307 C C     . ASP B 2 440 ? 133.073 109.599 99.903  1.00 139.20 ? 440 ASP A C     1 
ATOM   4308 O O     . ASP B 2 440 ? 131.881 109.742 99.614  1.00 139.20 ? 440 ASP A O     1 
ATOM   4309 C CB    . ASP B 2 440 ? 133.952 111.607 98.685  1.00 139.20 ? 440 ASP A CB    1 
ATOM   4310 C CG    . ASP B 2 440 ? 132.686 112.427 98.493  1.00 139.20 ? 440 ASP A CG    1 
ATOM   4311 O OD1   . ASP B 2 440 ? 132.563 113.097 97.446  1.00 139.20 ? 440 ASP A OD1   1 
ATOM   4312 O OD2   . ASP B 2 440 ? 131.823 112.426 99.396  1.00 139.20 ? 440 ASP A OD2   1 
ATOM   4313 N N     . VAL B 2 441 ? 133.600 108.392 100.123 1.00 140.55 ? 441 VAL A N     1 
ATOM   4314 C CA    . VAL B 2 441 ? 132.778 107.184 100.167 1.00 140.55 ? 441 VAL A CA    1 
ATOM   4315 C C     . VAL B 2 441 ? 132.504 106.746 101.605 1.00 140.55 ? 441 VAL A C     1 
ATOM   4316 O O     . VAL B 2 441 ? 131.401 106.301 101.923 1.00 140.55 ? 441 VAL A O     1 
ATOM   4317 C CB    . VAL B 2 441 ? 133.395 106.037 99.332  1.00 140.55 ? 441 VAL A CB    1 
ATOM   4318 C CG1   . VAL B 2 441 ? 134.601 105.403 100.018 1.00 140.55 ? 441 VAL A CG1   1 
ATOM   4319 C CG2   . VAL B 2 441 ? 132.340 104.984 99.020  1.00 140.55 ? 441 VAL A CG2   1 
ATOM   4320 N N     . VAL B 2 442 ? 133.492 106.873 102.495 1.00 135.43 ? 442 VAL A N     1 
ATOM   4321 C CA    . VAL B 2 442 ? 133.235 106.484 103.880 1.00 135.43 ? 442 VAL A CA    1 
ATOM   4322 C C     . VAL B 2 442 ? 132.731 107.677 104.689 1.00 135.43 ? 442 VAL A C     1 
ATOM   4323 O O     . VAL B 2 442 ? 131.589 107.679 105.160 1.00 135.43 ? 442 VAL A O     1 
ATOM   4324 C CB    . VAL B 2 442 ? 134.468 105.807 104.520 1.00 135.43 ? 442 VAL A CB    1 
ATOM   4325 C CG1   . VAL B 2 442 ? 134.772 104.500 103.807 1.00 135.43 ? 442 VAL A CG1   1 
ATOM   4326 C CG2   . VAL B 2 442 ? 135.697 106.702 104.526 1.00 135.43 ? 442 VAL A CG2   1 
ATOM   4327 N N     . ALA B 2 443 ? 133.537 108.732 104.809 1.00 125.62 ? 443 ALA A N     1 
ATOM   4328 C CA    . ALA B 2 443 ? 133.213 109.820 105.720 1.00 125.62 ? 443 ALA A CA    1 
ATOM   4329 C C     . ALA B 2 443 ? 132.048 110.672 105.241 1.00 125.62 ? 443 ALA A C     1 
ATOM   4330 O O     . ALA B 2 443 ? 131.622 111.574 105.970 1.00 125.62 ? 443 ALA A O     1 
ATOM   4331 C CB    . ALA B 2 443 ? 134.440 110.705 105.934 1.00 125.62 ? 443 ALA A CB    1 
ATOM   4332 N N     . ALA B 2 444 ? 131.530 110.415 104.039 1.00 129.36 ? 444 ALA A N     1 
ATOM   4333 C CA    . ALA B 2 444 ? 130.366 111.151 103.562 1.00 129.36 ? 444 ALA A CA    1 
ATOM   4334 C C     . ALA B 2 444 ? 129.164 110.898 104.461 1.00 129.36 ? 444 ALA A C     1 
ATOM   4335 O O     . ALA B 2 444 ? 128.457 111.833 104.853 1.00 129.36 ? 444 ALA A O     1 
ATOM   4336 C CB    . ALA B 2 444 ? 130.056 110.766 102.116 1.00 129.36 ? 444 ALA A CB    1 
ATOM   4337 N N     . ARG B 2 445 ? 129.047 109.691 104.983 1.00 122.65 ? 445 ARG A N     1 
ATOM   4338 C CA    . ARG B 2 445 ? 127.953 109.487 105.929 1.00 122.65 ? 445 ARG A CA    1 
ATOM   4339 C C     . ARG B 2 445 ? 128.542 109.076 107.225 1.00 122.65 ? 445 ARG A C     1 
ATOM   4340 O O     . ARG B 2 445 ? 128.045 109.418 108.281 1.00 122.65 ? 445 ARG A O     1 
ATOM   4341 C CB    . ARG B 2 445 ? 126.955 108.442 105.452 1.00 122.65 ? 445 ARG A CB    1 
ATOM   4342 C CG    . ARG B 2 445 ? 125.628 108.487 106.179 1.00 122.65 ? 445 ARG A CG    1 
ATOM   4343 C CD    . ARG B 2 445 ? 124.605 109.291 105.403 1.00 122.65 ? 445 ARG A CD    1 
ATOM   4344 N NE    . ARG B 2 445 ? 123.892 108.471 104.435 1.00 122.65 ? 445 ARG A NE    1 
ATOM   4345 C CZ    . ARG B 2 445 ? 122.610 108.624 104.133 1.00 122.65 ? 445 ARG A CZ    1 
ATOM   4346 N NH1   . ARG B 2 445 ? 121.906 109.568 104.732 1.00 122.65 ? 445 ARG A NH1   1 
ATOM   4347 N NH2   . ARG B 2 445 ? 122.034 107.837 103.238 1.00 122.65 ? 445 ARG A NH2   1 
ATOM   4348 N N     . PHE B 2 446 ? 129.628 108.368 107.145 1.00 115.28 ? 446 PHE A N     1 
ATOM   4349 C CA    . PHE B 2 446 ? 130.153 107.886 108.416 1.00 115.28 ? 446 PHE A CA    1 
ATOM   4350 C C     . PHE B 2 446 ? 129.996 108.939 109.499 1.00 115.28 ? 446 PHE A C     1 
ATOM   4351 O O     . PHE B 2 446 ? 129.576 108.628 110.616 1.00 115.28 ? 446 PHE A O     1 
ATOM   4352 C CB    . PHE B 2 446 ? 131.622 107.493 108.263 1.00 115.28 ? 446 PHE A CB    1 
ATOM   4353 C CG    . PHE B 2 446 ? 132.209 106.838 109.483 1.00 115.28 ? 446 PHE A CG    1 
ATOM   4354 C CD1   . PHE B 2 446 ? 132.185 105.462 109.623 1.00 115.28 ? 446 PHE A CD1   1 
ATOM   4355 C CD2   . PHE B 2 446 ? 132.793 107.598 110.483 1.00 115.28 ? 446 PHE A CD2   1 
ATOM   4356 C CE1   . PHE B 2 446 ? 132.727 104.856 110.739 1.00 115.28 ? 446 PHE A CE1   1 
ATOM   4357 C CE2   . PHE B 2 446 ? 133.336 106.996 111.601 1.00 115.28 ? 446 PHE A CE2   1 
ATOM   4358 C CZ    . PHE B 2 446 ? 133.302 105.624 111.729 1.00 115.28 ? 446 PHE A CZ    1 
ATOM   4359 N N     . GLY B 2 447 ? 130.317 110.189 109.185 1.00 108.77 ? 447 GLY A N     1 
ATOM   4360 C CA    . GLY B 2 447 ? 130.165 111.270 110.136 1.00 108.77 ? 447 GLY A CA    1 
ATOM   4361 C C     . GLY B 2 447 ? 128.736 111.460 110.596 1.00 108.77 ? 447 GLY A C     1 
ATOM   4362 O O     . GLY B 2 447 ? 128.474 111.561 111.797 1.00 108.77 ? 447 GLY A O     1 
ATOM   4363 N N     . LYS B 2 448 ? 127.799 111.506 109.647 1.00 106.19 ? 448 LYS A N     1 
ATOM   4364 C CA    . LYS B 2 448 ? 126.397 111.689 110.006 1.00 106.19 ? 448 LYS A CA    1 
ATOM   4365 C C     . LYS B 2 448 ? 125.871 110.510 110.813 1.00 106.19 ? 448 LYS A C     1 
ATOM   4366 O O     . LYS B 2 448 ? 125.220 110.701 111.846 1.00 106.19 ? 448 LYS A O     1 
ATOM   4367 C CB    . LYS B 2 448 ? 125.547 111.902 108.756 1.00 106.19 ? 448 LYS A CB    1 
ATOM   4368 C CG    . LYS B 2 448 ? 125.827 113.211 108.036 1.00 106.19 ? 448 LYS A CG    1 
ATOM   4369 C CD    . LYS B 2 448 ? 124.769 113.488 106.981 1.00 106.19 ? 448 LYS A CD    1 
ATOM   4370 C CE    . LYS B 2 448 ? 124.930 112.570 105.785 1.00 106.19 ? 448 LYS A CE    1 
ATOM   4371 N NZ    . LYS B 2 448 ? 123.960 112.896 104.705 1.00 106.19 ? 448 LYS A NZ    1 
ATOM   4372 N N     . SER B 2 449 ? 126.135 109.283 110.359 1.00 102.31 ? 449 SER A N     1 
ATOM   4373 C CA    . SER B 2 449 ? 125.645 108.112 111.074 1.00 102.31 ? 449 SER A CA    1 
ATOM   4374 C C     . SER B 2 449 ? 126.274 108.010 112.457 1.00 102.31 ? 449 SER A C     1 
ATOM   4375 O O     . SER B 2 449 ? 125.628 107.569 113.411 1.00 102.31 ? 449 SER A O     1 
ATOM   4376 C CB    . SER B 2 449 ? 125.929 106.854 110.257 1.00 102.31 ? 449 SER A CB    1 
ATOM   4377 O OG    . SER B 2 449 ? 125.247 106.895 109.016 1.00 102.31 ? 449 SER A OG    1 
ATOM   4378 N N     . GLY B 2 450 ? 127.525 108.449 112.600 1.00 96.75  ? 450 GLY A N     1 
ATOM   4379 C CA    . GLY B 2 450 ? 128.161 108.410 113.905 1.00 96.75  ? 450 GLY A CA    1 
ATOM   4380 C C     . GLY B 2 450 ? 127.629 109.475 114.839 1.00 96.75  ? 450 GLY A C     1 
ATOM   4381 O O     . GLY B 2 450 ? 127.453 109.231 116.034 1.00 96.75  ? 450 GLY A O     1 
ATOM   4382 N N     . GLY B 2 451 ? 127.372 110.672 114.314 1.00 93.11  ? 451 GLY A N     1 
ATOM   4383 C CA    . GLY B 2 451 ? 126.742 111.697 115.125 1.00 93.11  ? 451 GLY A CA    1 
ATOM   4384 C C     . GLY B 2 451 ? 125.334 111.314 115.531 1.00 93.11  ? 451 GLY A C     1 
ATOM   4385 O O     . GLY B 2 451 ? 124.831 111.762 116.562 1.00 93.11  ? 451 GLY A O     1 
ATOM   4386 N N     . ALA B 2 452 ? 124.678 110.482 114.723 1.00 89.17  ? 452 ALA A N     1 
ATOM   4387 C CA    . ALA B 2 452 ? 123.361 109.985 115.103 1.00 89.17  ? 452 ALA A CA    1 
ATOM   4388 C C     . ALA B 2 452 ? 123.468 108.872 116.138 1.00 89.17  ? 452 ALA A C     1 
ATOM   4389 O O     . ALA B 2 452 ? 122.670 108.814 117.078 1.00 89.17  ? 452 ALA A O     1 
ATOM   4390 C CB    . ALA B 2 452 ? 122.608 109.499 113.867 1.00 89.17  ? 452 ALA A CB    1 
ATOM   4391 N N     . LEU B 2 453 ? 124.455 107.988 115.990 1.00 87.19  ? 453 LEU A N     1 
ATOM   4392 C CA    . LEU B 2 453 ? 124.597 106.870 116.916 1.00 87.19  ? 453 LEU A CA    1 
ATOM   4393 C C     . LEU B 2 453 ? 125.064 107.338 118.286 1.00 87.19  ? 453 LEU A C     1 
ATOM   4394 O O     . LEU B 2 453 ? 124.641 106.791 119.310 1.00 87.19  ? 453 LEU A O     1 
ATOM   4395 C CB    . LEU B 2 453 ? 125.568 105.839 116.347 1.00 87.19  ? 453 LEU A CB    1 
ATOM   4396 C CG    . LEU B 2 453 ? 124.975 104.801 115.401 1.00 87.19  ? 453 LEU A CG    1 
ATOM   4397 C CD1   . LEU B 2 453 ? 126.080 103.993 114.747 1.00 87.19  ? 453 LEU A CD1   1 
ATOM   4398 C CD2   . LEU B 2 453 ? 124.019 103.894 116.149 1.00 87.19  ? 453 LEU A CD2   1 
ATOM   4399 N N     . ILE B 2 454 ? 125.947 108.336 118.327 1.00 86.71  ? 454 ILE A N     1 
ATOM   4400 C CA    . ILE B 2 454 ? 126.356 108.913 119.603 1.00 86.71  ? 454 ILE A CA    1 
ATOM   4401 C C     . ILE B 2 454 ? 125.146 109.458 120.345 1.00 86.71  ? 454 ILE A C     1 
ATOM   4402 O O     . ILE B 2 454 ? 124.978 109.227 121.548 1.00 86.71  ? 454 ILE A O     1 
ATOM   4403 C CB    . ILE B 2 454 ? 127.418 110.003 119.380 1.00 86.71  ? 454 ILE A CB    1 
ATOM   4404 C CG1   . ILE B 2 454 ? 128.751 109.381 118.972 1.00 86.71  ? 454 ILE A CG1   1 
ATOM   4405 C CG2   . ILE B 2 454 ? 127.589 110.837 120.628 1.00 86.71  ? 454 ILE A CG2   1 
ATOM   4406 C CD1   . ILE B 2 454 ? 129.824 110.400 118.682 1.00 86.71  ? 454 ILE A CD1   1 
ATOM   4407 N N     . GLN B 2 455 ? 124.276 110.176 119.637 1.00 86.01  ? 455 GLN A N     1 
ATOM   4408 C CA    . GLN B 2 455 ? 123.106 110.755 120.284 1.00 86.01  ? 455 GLN A CA    1 
ATOM   4409 C C     . GLN B 2 455 ? 122.101 109.683 120.674 1.00 86.01  ? 455 GLN A C     1 
ATOM   4410 O O     . GLN B 2 455 ? 121.432 109.806 121.702 1.00 86.01  ? 455 GLN A O     1 
ATOM   4411 C CB    . GLN B 2 455 ? 122.470 111.798 119.374 1.00 86.01  ? 455 GLN A CB    1 
ATOM   4412 C CG    . GLN B 2 455 ? 123.393 112.955 119.078 1.00 86.01  ? 455 GLN A CG    1 
ATOM   4413 C CD    . GLN B 2 455 ? 122.651 114.218 118.735 1.00 86.01  ? 455 GLN A CD    1 
ATOM   4414 O OE1   . GLN B 2 455 ? 122.204 114.947 119.617 1.00 86.01  ? 455 GLN A OE1   1 
ATOM   4415 N NE2   . GLN B 2 455 ? 122.524 114.496 117.445 1.00 86.01  ? 455 GLN A NE2   1 
ATOM   4416 N N     . GLN B 2 456 ? 121.989 108.615 119.883 1.00 82.27  ? 456 GLN A N     1 
ATOM   4417 C CA    . GLN B 2 456 ? 121.133 107.500 120.276 1.00 82.27  ? 456 GLN A CA    1 
ATOM   4418 C C     . GLN B 2 456 ? 121.628 106.863 121.565 1.00 82.27  ? 456 GLN A C     1 
ATOM   4419 O O     . GLN B 2 456 ? 120.846 106.604 122.488 1.00 82.27  ? 456 GLN A O     1 
ATOM   4420 C CB    . GLN B 2 456 ? 121.078 106.455 119.166 1.00 82.27  ? 456 GLN A CB    1 
ATOM   4421 C CG    . GLN B 2 456 ? 120.351 106.892 117.928 1.00 82.27  ? 456 GLN A CG    1 
ATOM   4422 C CD    . GLN B 2 456 ? 120.370 105.831 116.860 1.00 82.27  ? 456 GLN A CD    1 
ATOM   4423 O OE1   . GLN B 2 456 ? 120.345 104.638 117.154 1.00 82.27  ? 456 GLN A OE1   1 
ATOM   4424 N NE2   . GLN B 2 456 ? 120.419 106.256 115.610 1.00 82.27  ? 456 GLN A NE2   1 
ATOM   4425 N N     . GLY B 2 457 ? 122.930 106.592 121.640 1.00 83.51  ? 457 GLY A N     1 
ATOM   4426 C CA    . GLY B 2 457 ? 123.483 106.010 122.848 1.00 83.51  ? 457 GLY A CA    1 
ATOM   4427 C C     . GLY B 2 457 ? 123.329 106.919 124.049 1.00 83.51  ? 457 GLY A C     1 
ATOM   4428 O O     . GLY B 2 457 ? 123.006 106.464 125.147 1.00 83.51  ? 457 GLY A O     1 
ATOM   4429 N N     . LEU B 2 458 ? 123.549 108.220 123.855 1.00 83.96  ? 458 LEU A N     1 
ATOM   4430 C CA    . LEU B 2 458 ? 123.398 109.159 124.957 1.00 83.96  ? 458 LEU A CA    1 
ATOM   4431 C C     . LEU B 2 458 ? 121.946 109.287 125.391 1.00 83.96  ? 458 LEU A C     1 
ATOM   4432 O O     . LEU B 2 458 ? 121.676 109.468 126.580 1.00 83.96  ? 458 LEU A O     1 
ATOM   4433 C CB    . LEU B 2 458 ? 123.960 110.520 124.564 1.00 83.96  ? 458 LEU A CB    1 
ATOM   4434 C CG    . LEU B 2 458 ? 125.483 110.584 124.501 1.00 83.96  ? 458 LEU A CG    1 
ATOM   4435 C CD1   . LEU B 2 458 ? 125.928 111.902 123.909 1.00 83.96  ? 458 LEU A CD1   1 
ATOM   4436 C CD2   . LEU B 2 458 ? 126.076 110.387 125.881 1.00 83.96  ? 458 LEU A CD2   1 
ATOM   4437 N N     . LEU B 2 459 ? 121.001 109.186 124.457 1.00 81.62  ? 459 LEU A N     1 
ATOM   4438 C CA    . LEU B 2 459 ? 119.595 109.220 124.832 1.00 81.62  ? 459 LEU A CA    1 
ATOM   4439 C C     . LEU B 2 459 ? 119.207 107.969 125.603 1.00 81.62  ? 459 LEU A C     1 
ATOM   4440 O O     . LEU B 2 459 ? 118.454 108.043 126.579 1.00 81.62  ? 459 LEU A O     1 
ATOM   4441 C CB    . LEU B 2 459 ? 118.723 109.372 123.589 1.00 81.62  ? 459 LEU A CB    1 
ATOM   4442 C CG    . LEU B 2 459 ? 118.594 110.778 123.010 1.00 81.62  ? 459 LEU A CG    1 
ATOM   4443 C CD1   . LEU B 2 459 ? 118.316 110.721 121.523 1.00 81.62  ? 459 LEU A CD1   1 
ATOM   4444 C CD2   . LEU B 2 459 ? 117.499 111.538 123.726 1.00 81.62  ? 459 LEU A CD2   1 
ATOM   4445 N N     . VAL B 2 460 ? 119.719 106.811 125.188 1.00 80.71  ? 460 VAL A N     1 
ATOM   4446 C CA    . VAL B 2 460 ? 119.368 105.570 125.871 1.00 80.71  ? 460 VAL A CA    1 
ATOM   4447 C C     . VAL B 2 460 ? 119.981 105.532 127.263 1.00 80.71  ? 460 VAL A C     1 
ATOM   4448 O O     . VAL B 2 460 ? 119.334 105.114 128.229 1.00 80.71  ? 460 VAL A O     1 
ATOM   4449 C CB    . VAL B 2 460 ? 119.795 104.357 125.028 1.00 80.71  ? 460 VAL A CB    1 
ATOM   4450 C CG1   . VAL B 2 460 ? 119.594 103.075 125.811 1.00 80.71  ? 460 VAL A CG1   1 
ATOM   4451 C CG2   . VAL B 2 460 ? 119.009 104.315 123.737 1.00 80.71  ? 460 VAL A CG2   1 
ATOM   4452 N N     . ILE B 2 461 ? 121.230 105.974 127.395 1.00 82.49  ? 461 ILE A N     1 
ATOM   4453 C CA    . ILE B 2 461 ? 121.911 105.912 128.683 1.00 82.49  ? 461 ILE A CA    1 
ATOM   4454 C C     . ILE B 2 461 ? 121.403 107.000 129.620 1.00 82.49  ? 461 ILE A C     1 
ATOM   4455 O O     . ILE B 2 461 ? 120.983 106.721 130.749 1.00 82.49  ? 461 ILE A O     1 
ATOM   4456 C CB    . ILE B 2 461 ? 123.433 106.012 128.479 1.00 82.49  ? 461 ILE A CB    1 
ATOM   4457 C CG1   . ILE B 2 461 ? 123.938 104.829 127.655 1.00 82.49  ? 461 ILE A CG1   1 
ATOM   4458 C CG2   . ILE B 2 461 ? 124.143 106.065 129.816 1.00 82.49  ? 461 ILE A CG2   1 
ATOM   4459 C CD1   . ILE B 2 461 ? 125.352 104.999 127.155 1.00 82.49  ? 461 ILE A CD1   1 
ATOM   4460 N N     . CYS B 2 462 ? 121.433 108.254 129.170 1.00 84.35  ? 462 CYS A N     1 
ATOM   4461 C CA    . CYS B 2 462 ? 121.057 109.371 130.029 1.00 84.35  ? 462 CYS A CA    1 
ATOM   4462 C C     . CYS B 2 462 ? 119.559 109.384 130.296 1.00 84.35  ? 462 CYS A C     1 
ATOM   4463 O O     . CYS B 2 462 ? 119.125 109.509 131.446 1.00 84.35  ? 462 CYS A O     1 
ATOM   4464 C CB    . CYS B 2 462 ? 121.504 110.684 129.392 1.00 84.35  ? 462 CYS A CB    1 
ATOM   4465 S SG    . CYS B 2 462 ? 123.293 110.892 129.334 1.00 84.35  ? 462 CYS A SG    1 
ATOM   4466 N N     . GLY B 2 463 ? 118.752 109.263 129.248 1.00 83.86  ? 463 GLY A N     1 
ATOM   4467 C CA    . GLY B 2 463 ? 117.316 109.143 129.388 1.00 83.86  ? 463 GLY A CA    1 
ATOM   4468 C C     . GLY B 2 463 ? 116.512 110.269 128.781 1.00 83.86  ? 463 GLY A C     1 
ATOM   4469 O O     . GLY B 2 463 ? 115.284 110.146 128.695 1.00 83.86  ? 463 GLY A O     1 
ATOM   4470 N N     . SER B 2 464 ? 117.146 111.361 128.364 1.00 86.74  ? 464 SER A N     1 
ATOM   4471 C CA    . SER B 2 464 ? 116.432 112.477 127.760 1.00 86.74  ? 464 SER A CA    1 
ATOM   4472 C C     . SER B 2 464 ? 117.429 113.339 127.002 1.00 86.74  ? 464 SER A C     1 
ATOM   4473 O O     . SER B 2 464 ? 118.630 113.065 126.984 1.00 86.74  ? 464 SER A O     1 
ATOM   4474 C CB    . SER B 2 464 ? 115.687 113.312 128.808 1.00 86.74  ? 464 SER A CB    1 
ATOM   4475 O OG    . SER B 2 464 ? 114.900 112.504 129.664 1.00 86.74  ? 464 SER A OG    1 
ATOM   4476 N N     . ILE B 2 465 ? 116.909 114.389 126.368 1.00 86.64  ? 465 ILE A N     1 
ATOM   4477 C CA    . ILE B 2 465 ? 117.784 115.355 125.715 1.00 86.64  ? 465 ILE A CA    1 
ATOM   4478 C C     . ILE B 2 465 ? 118.349 116.333 126.733 1.00 86.64  ? 465 ILE A C     1 
ATOM   4479 O O     . ILE B 2 465 ? 119.511 116.743 126.640 1.00 86.64  ? 465 ILE A O     1 
ATOM   4480 C CB    . ILE B 2 465 ? 117.032 116.081 124.587 1.00 86.64  ? 465 ILE A CB    1 
ATOM   4481 C CG1   . ILE B 2 465 ? 116.730 115.119 123.442 1.00 86.64  ? 465 ILE A CG1   1 
ATOM   4482 C CG2   . ILE B 2 465 ? 117.838 117.259 124.075 1.00 86.64  ? 465 ILE A CG2   1 
ATOM   4483 C CD1   . ILE B 2 465 ? 115.973 115.761 122.312 1.00 86.64  ? 465 ILE A CD1   1 
ATOM   4484 N N     . GLY B 2 466 ? 117.545 116.715 127.724 1.00 88.41  ? 466 GLY A N     1 
ATOM   4485 C CA    . GLY B 2 466 ? 118.032 117.613 128.754 1.00 88.41  ? 466 GLY A CA    1 
ATOM   4486 C C     . GLY B 2 466 ? 119.072 116.979 129.651 1.00 88.41  ? 466 GLY A C     1 
ATOM   4487 O O     . GLY B 2 466 ? 119.909 117.679 130.225 1.00 88.41  ? 466 GLY A O     1 
ATOM   4488 N N     . ALA B 2 467 ? 119.037 115.656 129.788 1.00 86.48  ? 467 ALA A N     1 
ATOM   4489 C CA    . ALA B 2 467 ? 119.985 114.957 130.640 1.00 86.48  ? 467 ALA A CA    1 
ATOM   4490 C C     . ALA B 2 467 ? 121.263 114.565 129.917 1.00 86.48  ? 467 ALA A C     1 
ATOM   4491 O O     . ALA B 2 467 ? 122.264 114.268 130.577 1.00 86.48  ? 467 ALA A O     1 
ATOM   4492 C CB    . ALA B 2 467 ? 119.338 113.703 131.233 1.00 86.48  ? 467 ALA A CB    1 
ATOM   4493 N N     . MET B 2 468 ? 121.256 114.556 128.587 1.00 87.98  ? 468 MET A N     1 
ATOM   4494 C CA    . MET B 2 468 ? 122.427 114.180 127.811 1.00 87.98  ? 468 MET A CA    1 
ATOM   4495 C C     . MET B 2 468 ? 123.259 115.372 127.369 1.00 87.98  ? 468 MET A C     1 
ATOM   4496 O O     . MET B 2 468 ? 124.368 115.175 126.865 1.00 87.98  ? 468 MET A O     1 
ATOM   4497 C CB    . MET B 2 468 ? 122.011 113.380 126.574 1.00 87.98  ? 468 MET A CB    1 
ATOM   4498 C CG    . MET B 2 468 ? 121.422 114.236 125.472 1.00 87.98  ? 468 MET A CG    1 
ATOM   4499 S SD    . MET B 2 468 ? 120.878 113.289 124.041 1.00 87.98  ? 468 MET A SD    1 
ATOM   4500 C CE    . MET B 2 468 ? 122.338 113.353 123.015 1.00 87.98  ? 468 MET A CE    1 
ATOM   4501 N N     . THR B 2 469 ? 122.759 116.591 127.536 1.00 84.62  ? 469 THR A N     1 
ATOM   4502 C CA    . THR B 2 469 ? 123.480 117.770 127.072 1.00 84.62  ? 469 THR A CA    1 
ATOM   4503 C C     . THR B 2 469 ? 124.787 118.050 127.819 1.00 84.62  ? 469 THR A C     1 
ATOM   4504 O O     . THR B 2 469 ? 125.673 118.682 127.233 1.00 84.62  ? 469 THR A O     1 
ATOM   4505 C CB    . THR B 2 469 ? 122.570 119.006 127.093 1.00 84.62  ? 469 THR A CB    1 
ATOM   4506 O OG1   . THR B 2 469 ? 123.280 120.130 126.560 1.00 84.62  ? 469 THR A OG1   1 
ATOM   4507 C CG2   . THR B 2 469 ? 122.069 119.334 128.484 1.00 84.62  ? 469 THR A CG2   1 
ATOM   4508 N N     . PRO B 2 470 ? 124.980 117.636 129.082 1.00 84.00  ? 470 PRO A N     1 
ATOM   4509 C CA    . PRO B 2 470 ? 126.329 117.769 129.648 1.00 84.00  ? 470 PRO A CA    1 
ATOM   4510 C C     . PRO B 2 470 ? 127.320 116.814 129.018 1.00 84.00  ? 470 PRO A C     1 
ATOM   4511 O O     . PRO B 2 470 ? 128.519 117.114 128.983 1.00 84.00  ? 470 PRO A O     1 
ATOM   4512 C CB    . PRO B 2 470 ? 126.125 117.465 131.138 1.00 84.00  ? 470 PRO A CB    1 
ATOM   4513 C CG    . PRO B 2 470 ? 124.681 117.638 131.370 1.00 84.00  ? 470 PRO A CG    1 
ATOM   4514 C CD    . PRO B 2 470 ? 124.046 117.160 130.117 1.00 84.00  ? 470 PRO A CD    1 
ATOM   4515 N N     . TYR B 2 471 ? 126.855 115.669 128.517 1.00 84.87  ? 471 TYR A N     1 
ATOM   4516 C CA    . TYR B 2 471 ? 127.744 114.710 127.876 1.00 84.87  ? 471 TYR A CA    1 
ATOM   4517 C C     . TYR B 2 471 ? 127.980 115.046 126.413 1.00 84.87  ? 471 TYR A C     1 
ATOM   4518 O O     . TYR B 2 471 ? 129.019 114.678 125.859 1.00 84.87  ? 471 TYR A O     1 
ATOM   4519 C CB    . TYR B 2 471 ? 127.173 113.303 128.013 1.00 84.87  ? 471 TYR A CB    1 
ATOM   4520 C CG    . TYR B 2 471 ? 127.024 112.859 129.445 1.00 84.87  ? 471 TYR A CG    1 
ATOM   4521 C CD1   . TYR B 2 471 ? 128.060 112.216 130.101 1.00 84.87  ? 471 TYR A CD1   1 
ATOM   4522 C CD2   . TYR B 2 471 ? 125.854 113.095 130.145 1.00 84.87  ? 471 TYR A CD2   1 
ATOM   4523 C CE1   . TYR B 2 471 ? 127.931 111.813 131.411 1.00 84.87  ? 471 TYR A CE1   1 
ATOM   4524 C CE2   . TYR B 2 471 ? 125.715 112.696 131.456 1.00 84.87  ? 471 TYR A CE2   1 
ATOM   4525 C CZ    . TYR B 2 471 ? 126.757 112.056 132.083 1.00 84.87  ? 471 TYR A CZ    1 
ATOM   4526 O OH    . TYR B 2 471 ? 126.625 111.655 133.391 1.00 84.87  ? 471 TYR A OH    1 
ATOM   4527 N N     . LEU B 2 472 ? 127.035 115.734 125.771 1.00 84.73  ? 472 LEU A N     1 
ATOM   4528 C CA    . LEU B 2 472 ? 127.273 116.209 124.414 1.00 84.73  ? 472 LEU A CA    1 
ATOM   4529 C C     . LEU B 2 472 ? 128.366 117.265 124.393 1.00 84.73  ? 472 LEU A C     1 
ATOM   4530 O O     . LEU B 2 472 ? 129.156 117.332 123.446 1.00 84.73  ? 472 LEU A O     1 
ATOM   4531 C CB    . LEU B 2 472 ? 125.988 116.771 123.816 1.00 84.73  ? 472 LEU A CB    1 
ATOM   4532 C CG    . LEU B 2 472 ? 125.103 115.792 123.056 1.00 84.73  ? 472 LEU A CG    1 
ATOM   4533 C CD1   . LEU B 2 472 ? 123.991 116.544 122.356 1.00 84.73  ? 472 LEU A CD1   1 
ATOM   4534 C CD2   . LEU B 2 472 ? 125.929 115.013 122.060 1.00 84.73  ? 472 LEU A CD2   1 
ATOM   4535 N N     . ALA B 2 473 ? 128.425 118.102 125.428 1.00 84.84  ? 473 ALA A N     1 
ATOM   4536 C CA    . ALA B 2 473 ? 129.454 119.132 125.481 1.00 84.84  ? 473 ALA A CA    1 
ATOM   4537 C C     . ALA B 2 473 ? 130.831 118.520 125.691 1.00 84.84  ? 473 ALA A C     1 
ATOM   4538 O O     . ALA B 2 473 ? 131.824 119.003 125.139 1.00 84.84  ? 473 ALA A O     1 
ATOM   4539 C CB    . ALA B 2 473 ? 129.134 120.136 126.587 1.00 84.84  ? 473 ALA A CB    1 
ATOM   4540 N N     . VAL B 2 474 ? 130.912 117.454 126.487 1.00 84.43  ? 474 VAL A N     1 
ATOM   4541 C CA    . VAL B 2 474 ? 132.191 116.784 126.693 1.00 84.43  ? 474 VAL A CA    1 
ATOM   4542 C C     . VAL B 2 474 ? 132.605 116.034 125.437 1.00 84.43  ? 474 VAL A C     1 
ATOM   4543 O O     . VAL B 2 474 ? 133.782 116.030 125.060 1.00 84.43  ? 474 VAL A O     1 
ATOM   4544 C CB    . VAL B 2 474 ? 132.112 115.849 127.912 1.00 84.43  ? 474 VAL A CB    1 
ATOM   4545 C CG1   . VAL B 2 474 ? 133.403 115.069 128.065 1.00 84.43  ? 474 VAL A CG1   1 
ATOM   4546 C CG2   . VAL B 2 474 ? 131.820 116.647 129.169 1.00 84.43  ? 474 VAL A CG2   1 
ATOM   4547 N N     . ILE B 2 475 ? 131.649 115.392 124.765 1.00 83.84  ? 475 ILE A N     1 
ATOM   4548 C CA    . ILE B 2 475 ? 131.962 114.690 123.526 1.00 83.84  ? 475 ILE A CA    1 
ATOM   4549 C C     . ILE B 2 475 ? 132.340 115.681 122.435 1.00 83.84  ? 475 ILE A C     1 
ATOM   4550 O O     . ILE B 2 475 ? 133.272 115.445 121.658 1.00 83.84  ? 475 ILE A O     1 
ATOM   4551 C CB    . ILE B 2 475 ? 130.778 113.801 123.110 1.00 83.84  ? 475 ILE A CB    1 
ATOM   4552 C CG1   . ILE B 2 475 ? 130.665 112.606 124.052 1.00 83.84  ? 475 ILE A CG1   1 
ATOM   4553 C CG2   . ILE B 2 475 ? 130.946 113.314 121.690 1.00 83.84  ? 475 ILE A CG2   1 
ATOM   4554 C CD1   . ILE B 2 475 ? 129.578 111.639 123.679 1.00 83.84  ? 475 ILE A CD1   1 
ATOM   4555 N N     . LEU B 2 476 ? 131.636 116.812 122.366 1.00 84.73  ? 476 LEU A N     1 
ATOM   4556 C CA    . LEU B 2 476 ? 131.971 117.838 121.384 1.00 84.73  ? 476 LEU A CA    1 
ATOM   4557 C C     . LEU B 2 476 ? 133.365 118.399 121.623 1.00 84.73  ? 476 LEU A C     1 
ATOM   4558 O O     . LEU B 2 476 ? 134.074 118.744 120.672 1.00 84.73  ? 476 LEU A O     1 
ATOM   4559 C CB    . LEU B 2 476 ? 130.922 118.948 121.417 1.00 84.73  ? 476 LEU A CB    1 
ATOM   4560 C CG    . LEU B 2 476 ? 131.016 120.101 120.423 1.00 84.73  ? 476 LEU A CG    1 
ATOM   4561 C CD1   . LEU B 2 476 ? 129.629 120.538 120.042 1.00 84.73  ? 476 LEU A CD1   1 
ATOM   4562 C CD2   . LEU B 2 476 ? 131.752 121.269 121.046 1.00 84.73  ? 476 LEU A CD2   1 
ATOM   4563 N N     . LEU B 2 477 ? 133.775 118.508 122.886 1.00 85.56  ? 477 LEU A N     1 
ATOM   4564 C CA    . LEU B 2 477 ? 135.129 118.962 123.178 1.00 85.56  ? 477 LEU A CA    1 
ATOM   4565 C C     . LEU B 2 477 ? 136.152 117.893 122.827 1.00 85.56  ? 477 LEU A C     1 
ATOM   4566 O O     . LEU B 2 477 ? 137.275 118.208 122.419 1.00 85.56  ? 477 LEU A O     1 
ATOM   4567 C CB    . LEU B 2 477 ? 135.247 119.353 124.649 1.00 85.56  ? 477 LEU A CB    1 
ATOM   4568 C CG    . LEU B 2 477 ? 135.014 120.823 124.986 1.00 85.56  ? 477 LEU A CG    1 
ATOM   4569 C CD1   . LEU B 2 477 ? 134.819 121.001 126.481 1.00 85.56  ? 477 LEU A CD1   1 
ATOM   4570 C CD2   . LEU B 2 477 ? 136.181 121.655 124.497 1.00 85.56  ? 477 LEU A CD2   1 
ATOM   4571 N N     . PHE B 2 478 ? 135.785 116.621 122.981 1.00 88.92  ? 478 PHE A N     1 
ATOM   4572 C CA    . PHE B 2 478 ? 136.719 115.546 122.671 1.00 88.92  ? 478 PHE A CA    1 
ATOM   4573 C C     . PHE B 2 478 ? 136.886 115.363 121.171 1.00 88.92  ? 478 PHE A C     1 
ATOM   4574 O O     . PHE B 2 478 ? 137.924 114.867 120.722 1.00 88.92  ? 478 PHE A O     1 
ATOM   4575 C CB    . PHE B 2 478 ? 136.250 114.243 123.315 1.00 88.92  ? 478 PHE A CB    1 
ATOM   4576 C CG    . PHE B 2 478 ? 137.115 113.062 122.991 1.00 88.92  ? 478 PHE A CG    1 
ATOM   4577 C CD1   . PHE B 2 478 ? 138.352 112.909 123.590 1.00 88.92  ? 478 PHE A CD1   1 
ATOM   4578 C CD2   . PHE B 2 478 ? 136.690 112.102 122.088 1.00 88.92  ? 478 PHE A CD2   1 
ATOM   4579 C CE1   . PHE B 2 478 ? 139.151 111.823 123.293 1.00 88.92  ? 478 PHE A CE1   1 
ATOM   4580 C CE2   . PHE B 2 478 ? 137.483 111.014 121.787 1.00 88.92  ? 478 PHE A CE2   1 
ATOM   4581 C CZ    . PHE B 2 478 ? 138.715 110.874 122.390 1.00 88.92  ? 478 PHE A CZ    1 
ATOM   4582 N N     . ILE B 2 479 ? 135.890 115.758 120.386 1.00 85.38  ? 479 ILE A N     1 
ATOM   4583 C CA    . ILE B 2 479 ? 135.959 115.604 118.938 1.00 85.38  ? 479 ILE A CA    1 
ATOM   4584 C C     . ILE B 2 479 ? 136.598 116.818 118.282 1.00 85.38  ? 479 ILE A C     1 
ATOM   4585 O O     . ILE B 2 479 ? 137.396 116.681 117.353 1.00 85.38  ? 479 ILE A O     1 
ATOM   4586 C CB    . ILE B 2 479 ? 134.552 115.330 118.382 1.00 85.38  ? 479 ILE A CB    1 
ATOM   4587 C CG1   . ILE B 2 479 ? 134.061 113.973 118.875 1.00 85.38  ? 479 ILE A CG1   1 
ATOM   4588 C CG2   . ILE B 2 479 ? 134.559 115.364 116.873 1.00 85.38  ? 479 ILE A CG2   1 
ATOM   4589 C CD1   . ILE B 2 479 ? 132.656 113.662 118.480 1.00 85.38  ? 479 ILE A CD1   1 
ATOM   4590 N N     . ILE B 2 480 ? 136.263 118.018 118.755 1.00 85.86  ? 480 ILE A N     1 
ATOM   4591 C CA    . ILE B 2 480 ? 136.916 119.219 118.251 1.00 85.86  ? 480 ILE A CA    1 
ATOM   4592 C C     . ILE B 2 480 ? 138.389 119.221 118.624 1.00 85.86  ? 480 ILE A C     1 
ATOM   4593 O O     . ILE B 2 480 ? 139.226 119.744 117.879 1.00 85.86  ? 480 ILE A O     1 
ATOM   4594 C CB    . ILE B 2 480 ? 136.179 120.469 118.766 1.00 85.86  ? 480 ILE A CB    1 
ATOM   4595 C CG1   . ILE B 2 480 ? 134.872 120.640 117.998 1.00 85.86  ? 480 ILE A CG1   1 
ATOM   4596 C CG2   . ILE B 2 480 ? 137.033 121.708 118.631 1.00 85.86  ? 480 ILE A CG2   1 
ATOM   4597 C CD1   . ILE B 2 480 ? 134.073 121.820 118.425 1.00 85.86  ? 480 ILE A CD1   1 
ATOM   4598 N N     . ALA B 2 481 ? 138.740 118.615 119.759 1.00 87.24  ? 481 ALA A N     1 
ATOM   4599 C CA    . ALA B 2 481 ? 140.151 118.436 120.080 1.00 87.24  ? 481 ALA A CA    1 
ATOM   4600 C C     . ALA B 2 481 ? 140.832 117.551 119.047 1.00 87.24  ? 481 ALA A C     1 
ATOM   4601 O O     . ALA B 2 481 ? 141.942 117.851 118.596 1.00 87.24  ? 481 ALA A O     1 
ATOM   4602 C CB    . ALA B 2 481 ? 140.305 117.846 121.480 1.00 87.24  ? 481 ALA A CB    1 
ATOM   4603 N N     . ILE B 2 482 ? 140.179 116.455 118.658 1.00 88.67  ? 482 ILE A N     1 
ATOM   4604 C CA    . ILE B 2 482 ? 140.684 115.635 117.561 1.00 88.67  ? 482 ILE A CA    1 
ATOM   4605 C C     . ILE B 2 482 ? 140.691 116.435 116.267 1.00 88.67  ? 482 ILE A C     1 
ATOM   4606 O O     . ILE B 2 482 ? 141.637 116.362 115.476 1.00 88.67  ? 482 ILE A O     1 
ATOM   4607 C CB    . ILE B 2 482 ? 139.844 114.353 117.427 1.00 88.67  ? 482 ILE A CB    1 
ATOM   4608 C CG1   . ILE B 2 482 ? 140.014 113.471 118.662 1.00 88.67  ? 482 ILE A CG1   1 
ATOM   4609 C CG2   . ILE B 2 482 ? 140.223 113.590 116.174 1.00 88.67  ? 482 ILE A CG2   1 
ATOM   4610 C CD1   . ILE B 2 482 ? 139.030 112.330 118.724 1.00 88.67  ? 482 ILE A CD1   1 
ATOM   4611 N N     . TRP B 2 483 ? 139.633 117.213 116.036 1.00 89.06  ? 483 TRP A N     1 
ATOM   4612 C CA    . TRP B 2 483 ? 139.544 118.032 114.833 1.00 89.06  ? 483 TRP A CA    1 
ATOM   4613 C C     . TRP B 2 483 ? 140.668 119.058 114.776 1.00 89.06  ? 483 TRP A C     1 
ATOM   4614 O O     . TRP B 2 483 ? 141.249 119.297 113.712 1.00 89.06  ? 483 TRP A O     1 
ATOM   4615 C CB    . TRP B 2 483 ? 138.181 118.720 114.798 1.00 89.06  ? 483 TRP A CB    1 
ATOM   4616 C CG    . TRP B 2 483 ? 137.816 119.367 113.512 1.00 89.06  ? 483 TRP A CG    1 
ATOM   4617 C CD1   . TRP B 2 483 ? 138.598 119.512 112.410 1.00 89.06  ? 483 TRP A CD1   1 
ATOM   4618 C CD2   . TRP B 2 483 ? 136.561 119.968 113.196 1.00 89.06  ? 483 TRP A CD2   1 
ATOM   4619 N NE1   . TRP B 2 483 ? 137.907 120.166 111.423 1.00 89.06  ? 483 TRP A NE1   1 
ATOM   4620 C CE2   . TRP B 2 483 ? 136.651 120.457 111.883 1.00 89.06  ? 483 TRP A CE2   1 
ATOM   4621 C CE3   . TRP B 2 483 ? 135.368 120.140 113.899 1.00 89.06  ? 483 TRP A CE3   1 
ATOM   4622 C CZ2   . TRP B 2 483 ? 135.595 121.103 111.258 1.00 89.06  ? 483 TRP A CZ2   1 
ATOM   4623 C CZ3   . TRP B 2 483 ? 134.323 120.780 113.278 1.00 89.06  ? 483 TRP A CZ3   1 
ATOM   4624 C CH2   . TRP B 2 483 ? 134.441 121.256 111.972 1.00 89.06  ? 483 TRP A CH2   1 
ATOM   4625 N N     . LEU B 2 484 ? 140.996 119.672 115.913 1.00 90.21  ? 484 LEU A N     1 
ATOM   4626 C CA    . LEU B 2 484 ? 142.022 120.707 115.914 1.00 90.21  ? 484 LEU A CA    1 
ATOM   4627 C C     . LEU B 2 484 ? 143.418 120.105 115.833 1.00 90.21  ? 484 LEU A C     1 
ATOM   4628 O O     . LEU B 2 484 ? 144.295 120.650 115.154 1.00 90.21  ? 484 LEU A O     1 
ATOM   4629 C CB    . LEU B 2 484 ? 141.886 121.584 117.157 1.00 90.21  ? 484 LEU A CB    1 
ATOM   4630 C CG    . LEU B 2 484 ? 140.679 122.521 117.210 1.00 90.21  ? 484 LEU A CG    1 
ATOM   4631 C CD1   . LEU B 2 484 ? 140.461 123.017 118.625 1.00 90.21  ? 484 LEU A CD1   1 
ATOM   4632 C CD2   . LEU B 2 484 ? 140.858 123.685 116.261 1.00 90.21  ? 484 LEU A CD2   1 
ATOM   4633 N N     . VAL B 2 485 ? 143.649 118.984 116.519 1.00 94.30  ? 485 VAL A N     1 
ATOM   4634 C CA    . VAL B 2 485 ? 144.974 118.374 116.503 1.00 94.30  ? 485 VAL A CA    1 
ATOM   4635 C C     . VAL B 2 485 ? 145.247 117.718 115.156 1.00 94.30  ? 485 VAL A C     1 
ATOM   4636 O O     . VAL B 2 485 ? 146.379 117.734 114.661 1.00 94.30  ? 485 VAL A O     1 
ATOM   4637 C CB    . VAL B 2 485 ? 145.118 117.375 117.665 1.00 94.30  ? 485 VAL A CB    1 
ATOM   4638 C CG1   . VAL B 2 485 ? 146.425 116.613 117.554 1.00 94.30  ? 485 VAL A CG1   1 
ATOM   4639 C CG2   . VAL B 2 485 ? 145.058 118.105 118.993 1.00 94.30  ? 485 VAL A CG2   1 
ATOM   4640 N N     . SER B 2 486 ? 144.218 117.143 114.533 1.00 98.20  ? 486 SER A N     1 
ATOM   4641 C CA    . SER B 2 486 ? 144.410 116.549 113.216 1.00 98.20  ? 486 SER A CA    1 
ATOM   4642 C C     . SER B 2 486 ? 144.624 117.612 112.150 1.00 98.20  ? 486 SER A C     1 
ATOM   4643 O O     . SER B 2 486 ? 145.447 117.424 111.249 1.00 98.20  ? 486 SER A O     1 
ATOM   4644 C CB    . SER B 2 486 ? 143.220 115.666 112.854 1.00 98.20  ? 486 SER A CB    1 
ATOM   4645 O OG    . SER B 2 486 ? 142.001 116.319 113.149 1.00 98.20  ? 486 SER A OG    1 
ATOM   4646 N N     . ALA B 2 487 ? 143.903 118.731 112.234 1.00 99.04  ? 487 ALA A N     1 
ATOM   4647 C CA    . ALA B 2 487 ? 144.129 119.815 111.285 1.00 99.04  ? 487 ALA A CA    1 
ATOM   4648 C C     . ALA B 2 487 ? 145.486 120.468 111.499 1.00 99.04  ? 487 ALA A C     1 
ATOM   4649 O O     . ALA B 2 487 ? 146.110 120.925 110.537 1.00 99.04  ? 487 ALA A O     1 
ATOM   4650 C CB    . ALA B 2 487 ? 143.015 120.854 111.395 1.00 99.04  ? 487 ALA A CB    1 
ATOM   4651 N N     . THR B 2 488 ? 145.958 120.521 112.745 1.00 101.19 ? 488 THR A N     1 
ATOM   4652 C CA    . THR B 2 488 ? 147.278 121.081 113.008 1.00 101.19 ? 488 THR A CA    1 
ATOM   4653 C C     . THR B 2 488 ? 148.376 120.149 112.515 1.00 101.19 ? 488 THR A C     1 
ATOM   4654 O O     . THR B 2 488 ? 149.413 120.606 112.023 1.00 101.19 ? 488 THR A O     1 
ATOM   4655 C CB    . THR B 2 488 ? 147.443 121.360 114.500 1.00 101.19 ? 488 THR A CB    1 
ATOM   4656 O OG1   . THR B 2 488 ? 146.408 122.248 114.937 1.00 101.19 ? 488 THR A OG1   1 
ATOM   4657 C CG2   . THR B 2 488 ? 148.791 121.999 114.777 1.00 101.19 ? 488 THR A CG2   1 
ATOM   4658 N N     . LYS B 2 489 ? 148.163 118.838 112.631 1.00 105.84 ? 489 LYS A N     1 
ATOM   4659 C CA    . LYS B 2 489 ? 149.150 117.889 112.128 1.00 105.84 ? 489 LYS A CA    1 
ATOM   4660 C C     . LYS B 2 489 ? 149.088 117.789 110.611 1.00 105.84 ? 489 LYS A C     1 
ATOM   4661 O O     . LYS B 2 489 ? 150.127 117.707 109.947 1.00 105.84 ? 489 LYS A O     1 
ATOM   4662 C CB    . LYS B 2 489 ? 148.939 116.520 112.771 1.00 105.84 ? 489 LYS A CB    1 
ATOM   4663 C CG    . LYS B 2 489 ? 149.381 116.442 114.221 1.00 105.84 ? 489 LYS A CG    1 
ATOM   4664 C CD    . LYS B 2 489 ? 150.803 115.925 114.337 1.00 105.84 ? 489 LYS A CD    1 
ATOM   4665 C CE    . LYS B 2 489 ? 150.898 114.472 113.906 1.00 105.84 ? 489 LYS A CE    1 
ATOM   4666 N NZ    . LYS B 2 489 ? 152.267 113.922 114.099 1.00 105.84 ? 489 LYS A NZ    1 
ATOM   4667 N N     . LEU B 2 490 ? 147.878 117.793 110.044 1.00 107.33 ? 490 LEU A N     1 
ATOM   4668 C CA    . LEU B 2 490 ? 147.740 117.779 108.591 1.00 107.33 ? 490 LEU A CA    1 
ATOM   4669 C C     . LEU B 2 490 ? 148.401 118.995 107.959 1.00 107.33 ? 490 LEU A C     1 
ATOM   4670 O O     . LEU B 2 490 ? 148.910 118.911 106.836 1.00 107.33 ? 490 LEU A O     1 
ATOM   4671 C CB    . LEU B 2 490 ? 146.263 117.716 108.206 1.00 107.33 ? 490 LEU A CB    1 
ATOM   4672 C CG    . LEU B 2 490 ? 145.917 117.750 106.720 1.00 107.33 ? 490 LEU A CG    1 
ATOM   4673 C CD1   . LEU B 2 490 ? 146.612 116.620 105.991 1.00 107.33 ? 490 LEU A CD1   1 
ATOM   4674 C CD2   . LEU B 2 490 ? 144.417 117.664 106.523 1.00 107.33 ? 490 LEU A CD2   1 
ATOM   4675 N N     . ASN B 2 491 ? 148.415 120.126 108.666 1.00 110.80 ? 491 ASN A N     1 
ATOM   4676 C CA    . ASN B 2 491 ? 149.068 121.321 108.145 1.00 110.80 ? 491 ASN A CA    1 
ATOM   4677 C C     . ASN B 2 491 ? 150.576 121.139 108.054 1.00 110.80 ? 491 ASN A C     1 
ATOM   4678 O O     . ASN B 2 491 ? 151.230 121.791 107.233 1.00 110.80 ? 491 ASN A O     1 
ATOM   4679 C CB    . ASN B 2 491 ? 148.726 122.525 109.021 1.00 110.80 ? 491 ASN A CB    1 
ATOM   4680 C CG    . ASN B 2 491 ? 149.487 123.771 108.623 1.00 110.80 ? 491 ASN A CG    1 
ATOM   4681 O OD1   . ASN B 2 491 ? 149.164 124.418 107.629 1.00 110.80 ? 491 ASN A OD1   1 
ATOM   4682 N ND2   . ASN B 2 491 ? 150.506 124.115 109.401 1.00 110.80 ? 491 ASN A ND2   1 
ATOM   4683 N N     . LYS B 2 492 ? 151.147 120.257 108.877 1.00 112.83 ? 492 LYS A N     1 
ATOM   4684 C CA    . LYS B 2 492 ? 152.581 120.009 108.795 1.00 112.83 ? 492 LYS A CA    1 
ATOM   4685 C C     . LYS B 2 492 ? 152.918 119.121 107.605 1.00 112.83 ? 492 LYS A C     1 
ATOM   4686 O O     . LYS B 2 492 ? 153.936 119.330 106.937 1.00 112.83 ? 492 LYS A O     1 
ATOM   4687 C CB    . LYS B 2 492 ? 153.084 119.382 110.094 1.00 112.83 ? 492 LYS A CB    1 
ATOM   4688 C CG    . LYS B 2 492 ? 153.206 120.366 111.243 1.00 112.83 ? 492 LYS A CG    1 
ATOM   4689 C CD    . LYS B 2 492 ? 153.954 119.754 112.413 1.00 112.83 ? 492 LYS A CD    1 
ATOM   4690 C CE    . LYS B 2 492 ? 154.147 120.765 113.531 1.00 112.83 ? 492 LYS A CE    1 
ATOM   4691 N NZ    . LYS B 2 492 ? 152.853 121.335 113.997 1.00 112.83 ? 492 LYS A NZ    1 
ATOM   4692 N N     . LEU B 2 493 ? 152.078 118.125 107.325 1.00 117.47 ? 493 LEU A N     1 
ATOM   4693 C CA    . LEU B 2 493 ? 152.279 117.299 106.143 1.00 117.47 ? 493 LEU A CA    1 
ATOM   4694 C C     . LEU B 2 493 ? 151.805 117.985 104.871 1.00 117.47 ? 493 LEU A C     1 
ATOM   4695 O O     . LEU B 2 493 ? 152.181 117.558 103.774 1.00 117.47 ? 493 LEU A O     1 
ATOM   4696 C CB    . LEU B 2 493 ? 151.564 115.954 106.305 1.00 117.47 ? 493 LEU A CB    1 
ATOM   4697 C CG    . LEU B 2 493 ? 152.171 114.956 107.296 1.00 117.47 ? 493 LEU A CG    1 
ATOM   4698 C CD1   . LEU B 2 493 ? 151.540 115.091 108.672 1.00 117.47 ? 493 LEU A CD1   1 
ATOM   4699 C CD2   . LEU B 2 493 ? 152.015 113.536 106.776 1.00 117.47 ? 493 LEU A CD2   1 
ATOM   4700 N N     . PHE B 2 494 ? 150.986 119.031 104.989 1.00 118.38 ? 494 PHE A N     1 
ATOM   4701 C CA    . PHE B 2 494 ? 150.566 119.783 103.813 1.00 118.38 ? 494 PHE A CA    1 
ATOM   4702 C C     . PHE B 2 494 ? 151.614 120.811 103.410 1.00 118.38 ? 494 PHE A C     1 
ATOM   4703 O O     . PHE B 2 494 ? 151.849 121.026 102.216 1.00 118.38 ? 494 PHE A O     1 
ATOM   4704 C CB    . PHE B 2 494 ? 149.222 120.461 104.081 1.00 118.38 ? 494 PHE A CB    1 
ATOM   4705 C CG    . PHE B 2 494 ? 148.793 121.411 103.002 1.00 118.38 ? 494 PHE A CG    1 
ATOM   4706 C CD1   . PHE B 2 494 ? 148.133 120.948 101.881 1.00 118.38 ? 494 PHE A CD1   1 
ATOM   4707 C CD2   . PHE B 2 494 ? 149.035 122.767 103.117 1.00 118.38 ? 494 PHE A CD2   1 
ATOM   4708 C CE1   . PHE B 2 494 ? 147.733 121.816 100.889 1.00 118.38 ? 494 PHE A CE1   1 
ATOM   4709 C CE2   . PHE B 2 494 ? 148.637 123.641 102.129 1.00 118.38 ? 494 PHE A CE2   1 
ATOM   4710 C CZ    . PHE B 2 494 ? 147.984 123.164 101.014 1.00 118.38 ? 494 PHE A CZ    1 
ATOM   4711 N N     . LEU B 2 495 ? 152.248 121.458 104.389 1.00 121.58 ? 495 LEU A N     1 
ATOM   4712 C CA    . LEU B 2 495 ? 153.271 122.449 104.078 1.00 121.58 ? 495 LEU A CA    1 
ATOM   4713 C C     . LEU B 2 495 ? 154.541 121.790 103.557 1.00 121.58 ? 495 LEU A C     1 
ATOM   4714 O O     . LEU B 2 495 ? 155.191 122.315 102.645 1.00 121.58 ? 495 LEU A O     1 
ATOM   4715 C CB    . LEU B 2 495 ? 153.575 123.293 105.314 1.00 121.58 ? 495 LEU A CB    1 
ATOM   4716 C CG    . LEU B 2 495 ? 152.548 124.371 105.659 1.00 121.58 ? 495 LEU A CG    1 
ATOM   4717 C CD1   . LEU B 2 495 ? 152.989 125.155 106.883 1.00 121.58 ? 495 LEU A CD1   1 
ATOM   4718 C CD2   . LEU B 2 495 ? 152.331 125.296 104.474 1.00 121.58 ? 495 LEU A CD2   1 
ATOM   4719 N N     . ALA B 2 496 ? 154.912 120.642 104.124 1.00 126.52 ? 496 ALA A N     1 
ATOM   4720 C CA    . ALA B 2 496 ? 156.139 119.974 103.708 1.00 126.52 ? 496 ALA A CA    1 
ATOM   4721 C C     . ALA B 2 496 ? 156.021 119.440 102.287 1.00 126.52 ? 496 ALA A C     1 
ATOM   4722 O O     . ALA B 2 496 ? 156.900 119.675 101.450 1.00 126.52 ? 496 ALA A O     1 
ATOM   4723 C CB    . ALA B 2 496 ? 156.477 118.846 104.683 1.00 126.52 ? 496 ALA A CB    1 
ATOM   4724 N N     . GLN B 2 497 ? 154.938 118.718 101.995 1.00 129.54 ? 497 GLN A N     1 
ATOM   4725 C CA    . GLN B 2 497 ? 154.778 118.127 100.672 1.00 129.54 ? 497 GLN A CA    1 
ATOM   4726 C C     . GLN B 2 497 ? 154.606 119.192 99.597  1.00 129.54 ? 497 GLN A C     1 
ATOM   4727 O O     . GLN B 2 497 ? 154.987 118.972 98.442  1.00 129.54 ? 497 GLN A O     1 
ATOM   4728 C CB    . GLN B 2 497 ? 153.591 117.165 100.673 1.00 129.54 ? 497 GLN A CB    1 
ATOM   4729 C CG    . GLN B 2 497 ? 153.421 116.382 99.386  1.00 129.54 ? 497 GLN A CG    1 
ATOM   4730 C CD    . GLN B 2 497 ? 152.650 115.094 99.589  1.00 129.54 ? 497 GLN A CD    1 
ATOM   4731 O OE1   . GLN B 2 497 ? 151.826 114.987 100.496 1.00 129.54 ? 497 GLN A OE1   1 
ATOM   4732 N NE2   . GLN B 2 497 ? 152.917 114.106 98.744  1.00 129.54 ? 497 GLN A NE2   1 
ATOM   4733 N N     . SER B 2 498 ? 154.049 120.350 99.955  1.00 132.21 ? 498 SER A N     1 
ATOM   4734 C CA    . SER B 2 498 ? 153.886 121.425 98.982  1.00 132.21 ? 498 SER A CA    1 
ATOM   4735 C C     . SER B 2 498 ? 155.223 122.032 98.579  1.00 132.21 ? 498 SER A C     1 
ATOM   4736 O O     . SER B 2 498 ? 155.363 122.530 97.457  1.00 132.21 ? 498 SER A O     1 
ATOM   4737 C CB    . SER B 2 498 ? 152.963 122.506 99.544  1.00 132.21 ? 498 SER A CB    1 
ATOM   4738 O OG    . SER B 2 498 ? 151.659 121.997 99.765  1.00 132.21 ? 498 SER A OG    1 
ATOM   4739 N N     . ALA B 2 499 ? 156.213 122.004 99.475  1.00 136.84 ? 499 ALA A N     1 
ATOM   4740 C CA    . ALA B 2 499 ? 157.504 122.607 99.162  1.00 136.84 ? 499 ALA A CA    1 
ATOM   4741 C C     . ALA B 2 499 ? 158.293 121.754 98.175  1.00 136.84 ? 499 ALA A C     1 
ATOM   4742 O O     . ALA B 2 499 ? 158.857 122.278 97.207  1.00 136.84 ? 499 ALA A O     1 
ATOM   4743 C CB    . ALA B 2 499 ? 158.305 122.827 100.444 1.00 136.84 ? 499 ALA A CB    1 
ATOM   4744 N N     . LEU B 2 500 ? 158.345 120.439 98.402  1.00 138.39 ? 500 LEU A N     1 
ATOM   4745 C CA    . LEU B 2 500 ? 159.068 119.566 97.483  1.00 138.39 ? 500 LEU A CA    1 
ATOM   4746 C C     . LEU B 2 500 ? 158.366 119.468 96.134  1.00 138.39 ? 500 LEU A C     1 
ATOM   4747 O O     . LEU B 2 500 ? 159.016 119.208 95.115  1.00 138.39 ? 500 LEU A O     1 
ATOM   4748 C CB    . LEU B 2 500 ? 159.251 118.180 98.107  1.00 138.39 ? 500 LEU A CB    1 
ATOM   4749 C CG    . LEU B 2 500 ? 158.023 117.379 98.556  1.00 138.39 ? 500 LEU A CG    1 
ATOM   4750 C CD1   . LEU B 2 500 ? 157.459 116.520 97.431  1.00 138.39 ? 500 LEU A CD1   1 
ATOM   4751 C CD2   . LEU B 2 500 ? 158.364 116.520 99.764  1.00 138.39 ? 500 LEU A CD2   1 
ATOM   4752 N N     . LYS B 2 501 ? 157.046 119.667 96.107  1.00 140.37 ? 501 LYS A N     1 
ATOM   4753 C CA    . LYS B 2 501 ? 156.315 119.682 94.847  1.00 140.37 ? 501 LYS A CA    1 
ATOM   4754 C C     . LYS B 2 501 ? 156.679 120.886 93.987  1.00 140.37 ? 501 LYS A C     1 
ATOM   4755 O O     . LYS B 2 501 ? 156.537 120.825 92.761  1.00 140.37 ? 501 LYS A O     1 
ATOM   4756 C CB    . LYS B 2 501 ? 154.808 119.664 95.122  1.00 140.37 ? 501 LYS A CB    1 
ATOM   4757 C CG    . LYS B 2 501 ? 153.934 119.579 93.881  1.00 140.37 ? 501 LYS A CG    1 
ATOM   4758 C CD    . LYS B 2 501 ? 154.081 118.231 93.196  1.00 140.37 ? 501 LYS A CD    1 
ATOM   4759 C CE    . LYS B 2 501 ? 153.241 118.160 91.932  1.00 140.37 ? 501 LYS A CE    1 
ATOM   4760 N NZ    . LYS B 2 501 ? 151.784 118.210 92.228  1.00 140.37 ? 501 LYS A NZ    1 
ATOM   4761 N N     . GLU B 2 502 ? 157.157 121.970 94.603  1.00 144.65 ? 502 GLU A N     1 
ATOM   4762 C CA    . GLU B 2 502 ? 157.530 123.158 93.840  1.00 144.65 ? 502 GLU A CA    1 
ATOM   4763 C C     . GLU B 2 502 ? 158.722 122.881 92.933  1.00 144.65 ? 502 GLU A C     1 
ATOM   4764 O O     . GLU B 2 502 ? 158.702 123.225 91.745  1.00 144.65 ? 502 GLU A O     1 
ATOM   4765 C CB    . GLU B 2 502 ? 157.836 124.312 94.795  1.00 144.65 ? 502 GLU A CB    1 
ATOM   4766 C CG    . GLU B 2 502 ? 158.192 125.615 94.105  1.00 144.65 ? 502 GLU A CG    1 
ATOM   4767 C CD    . GLU B 2 502 ? 157.030 126.199 93.329  1.00 144.65 ? 502 GLU A CD    1 
ATOM   4768 O OE1   . GLU B 2 502 ? 155.869 125.921 93.696  1.00 144.65 ? 502 GLU A OE1   1 
ATOM   4769 O OE2   . GLU B 2 502 ? 157.276 126.935 92.351  1.00 144.65 ? 502 GLU A OE2   1 
ATOM   4770 N N     . GLN B 2 503 ? 159.770 122.269 93.475  1.00 143.37 ? 503 GLN A N     1 
ATOM   4771 C CA    . GLN B 2 503 ? 160.942 121.911 92.688  1.00 143.37 ? 503 GLN A CA    1 
ATOM   4772 C C     . GLN B 2 503 ? 160.654 120.707 91.797  1.00 143.37 ? 503 GLN A C     1 
ATOM   4773 O O     . GLN B 2 503 ? 160.575 120.832 90.576  1.00 143.37 ? 503 GLN A O     1 
ATOM   4774 C CB    . GLN B 2 503 ? 162.137 121.626 93.605  1.00 143.37 ? 503 GLN A CB    1 
ATOM   4775 C CG    . GLN B 2 503 ? 161.923 120.493 94.605  1.00 143.37 ? 503 GLN A CG    1 
ATOM   4776 C CD    . GLN B 2 503 ? 162.215 119.121 94.024  1.00 143.37 ? 503 GLN A CD    1 
ATOM   4777 O OE1   . GLN B 2 503 ? 163.045 118.977 93.126  1.00 143.37 ? 503 GLN A OE1   1 
ATOM   4778 N NE2   . GLN B 2 503 ? 161.530 118.104 94.535  1.00 143.37 ? 503 GLN A NE2   1 
HETATM 4779 P PG    . ATP C 3 .   ? 120.176 116.876 106.439 1.00 107.03 ? 601 ATP A PG    1 
HETATM 4780 O O1G   . ATP C 3 .   ? 119.380 117.355 107.629 1.00 107.03 ? 601 ATP A O1G   1 
HETATM 4781 O O2G   . ATP C 3 .   ? 119.486 116.993 105.108 1.00 107.03 ? 601 ATP A O2G   1 
HETATM 4782 O O3G   . ATP C 3 .   ? 120.867 115.556 106.610 1.00 107.03 ? 601 ATP A O3G   1 
HETATM 4783 P PB    . ATP C 3 .   ? 122.740 117.706 107.199 1.00 107.03 ? 601 ATP A PB    1 
HETATM 4784 O O1B   . ATP C 3 .   ? 122.501 116.722 108.312 1.00 107.03 ? 601 ATP A O1B   1 
HETATM 4785 O O2B   . ATP C 3 .   ? 123.367 119.039 107.487 1.00 107.03 ? 601 ATP A O2B   1 
HETATM 4786 O O3B   . ATP C 3 .   ? 121.371 117.943 106.391 1.00 107.03 ? 601 ATP A O3B   1 
HETATM 4787 P PA    . ATP C 3 .   ? 123.211 117.411 104.593 1.00 107.03 ? 601 ATP A PA    1 
HETATM 4788 O O1A   . ATP C 3 .   ? 123.139 118.907 104.562 1.00 107.03 ? 601 ATP A O1A   1 
HETATM 4789 O O2A   . ATP C 3 .   ? 122.024 116.584 104.204 1.00 107.03 ? 601 ATP A O2A   1 
HETATM 4790 O O3A   . ATP C 3 .   ? 123.603 116.988 106.074 1.00 107.03 ? 601 ATP A O3A   1 
HETATM 4791 O "O5'" . ATP C 3 .   ? 124.491 116.995 103.735 1.00 107.03 ? 601 ATP A "O5'" 1 
HETATM 4792 C "C5'" . ATP C 3 .   ? 124.635 117.613 102.471 1.00 107.03 ? 601 ATP A "C5'" 1 
HETATM 4793 C "C4'" . ATP C 3 .   ? 123.275 117.481 101.813 1.00 107.03 ? 601 ATP A "C4'" 1 
HETATM 4794 O "O4'" . ATP C 3 .   ? 122.658 118.759 101.675 1.00 107.03 ? 601 ATP A "O4'" 1 
HETATM 4795 C "C3'" . ATP C 3 .   ? 123.417 116.882 100.440 1.00 107.03 ? 601 ATP A "C3'" 1 
HETATM 4796 O "O3'" . ATP C 3 .   ? 122.662 115.679 100.397 1.00 107.03 ? 601 ATP A "O3'" 1 
HETATM 4797 C "C2'" . ATP C 3 .   ? 122.861 117.907 99.497  1.00 107.03 ? 601 ATP A "C2'" 1 
HETATM 4798 O "O2'" . ATP C 3 .   ? 121.634 117.414 99.005  1.00 107.03 ? 601 ATP A "O2'" 1 
HETATM 4799 C "C1'" . ATP C 3 .   ? 122.596 119.146 100.310 1.00 107.03 ? 601 ATP A "C1'" 1 
HETATM 4800 N N9    . ATP C 3 .   ? 123.647 120.155 100.098 1.00 107.03 ? 601 ATP A N9    1 
HETATM 4801 C C8    . ATP C 3 .   ? 124.971 119.952 100.228 1.00 107.03 ? 601 ATP A C8    1 
HETATM 4802 N N7    . ATP C 3 .   ? 125.670 121.085 99.976  1.00 107.03 ? 601 ATP A N7    1 
HETATM 4803 C C5    . ATP C 3 .   ? 124.772 122.040 99.683  1.00 107.03 ? 601 ATP A C5    1 
HETATM 4804 C C6    . ATP C 3 .   ? 124.825 123.467 99.320  1.00 107.03 ? 601 ATP A C6    1 
HETATM 4805 N N6    . ATP C 3 .   ? 126.004 124.112 99.222  1.00 107.03 ? 601 ATP A N6    1 
HETATM 4806 N N1    . ATP C 3 .   ? 123.657 124.098 99.092  1.00 107.03 ? 601 ATP A N1    1 
HETATM 4807 C C2    . ATP C 3 .   ? 122.472 123.468 99.185  1.00 107.03 ? 601 ATP A C2    1 
HETATM 4808 N N3    . ATP C 3 .   ? 122.349 122.174 99.509  1.00 107.03 ? 601 ATP A N3    1 
HETATM 4809 C C4    . ATP C 3 .   ? 123.441 121.424 99.768  1.00 107.03 ? 601 ATP A C4    1 
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