data_8Z03
# 
_entry.id   8Z03 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8Z03         pdb_00008z03 10.2210/pdb8z03/pdb 
WWPDB D_1300046752 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-12-11 
2 'Structure model' 1 1 2024-12-18 
3 'Structure model' 1 2 2025-02-19 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 '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 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
# 
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  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.pdbx_database_id_DOI'    
6  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
7  2 'Structure model' '_citation.title'                   
8  2 'Structure model' '_citation.year'                    
9  3 'Structure model' '_citation.journal_volume'          
10 3 'Structure model' '_citation.page_first'              
11 3 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Z03 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 yzhao4@uchicago.edu Yingming Zhao  ? 'principal investigator/group leader' 0000-0003-1928-2151 
4 hhuang@simm.ac.cn   He       Huang ? 'principal investigator/group leader' 0000-0001-6998-8131 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Liu, R.L.'  1 0000-0002-8744-5656 
'Ren, X.L.'  2 0000-0002-6429-9609 
'Li, L.T.'   3 0000-0001-5536-1581 
'Zhang, Y.'  4 0000-0002-1778-8389 
'Huang, H.'  5 0000-0001-6998-8131 
'Zhao, Y.M.' 6 0000-0003-1928-2151 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Cell Metab.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1932-7420 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            37 
_citation.language                  ? 
_citation.page_first                377 
_citation.page_last                 ? 
_citation.title                     
'Nuclear GTPSCS functions as a lactyl-CoA synthetase to promote histone lactylation and gliomagenesis.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.cmet.2024.11.005 
_citation.pdbx_database_id_PubMed   39642882 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Liu, R.'            1  ? 
primary 'Ren, X.'            2  ? 
primary 'Park, Y.E.'         3  ? 
primary 'Feng, H.'           4  ? 
primary 'Sheng, X.'          5  ? 
primary 'Song, X.'           6  ? 
primary 'AminiTabrizi, R.'   7  ? 
primary 'Shah, H.'           8  ? 
primary 'Li, L.'             9  ? 
primary 'Zhang, Y.'          10 ? 
primary 'Abdullah, K.G.'     11 ? 
primary 'Dubois-Coyne, S.'   12 ? 
primary 'Lin, H.'            13 ? 
primary 'Cole, P.A.'         14 ? 
primary 'DeBerardinis, R.J.' 15 ? 
primary 'McBrayer, S.K.'     16 ? 
primary 'Huang, H.'          17 ? 
primary 'Zhao, Y.'           18 ? 
# 
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 'Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial' 34250.133 1   6.2.1.4,6.2.1.5 ? ? ? 
2 polymer     man 'Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial'      42627.781 1   6.2.1.4         ? ? ? 
3 non-polymer syn 'COENZYME A'                                                           767.534   1   ?               ? ? ? 
4 non-polymer syn 'PHOSPHATE ION'                                                        94.971    1   ?               ? ? ? 
5 non-polymer syn '(2S)-2-HYDROXYPROPANOIC ACID'                                         90.078    1   ?               ? ? ? 
6 non-polymer syn 'MAGNESIUM ION'                                                        24.305    1   ?               ? ? ? 
7 water       nat water                                                                  18.015    214 ?               ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Succinyl-CoA synthetase subunit alpha,SCS-alpha'                                                               
2 'GTP-specific succinyl-CoA synthetase subunit beta,G-SCS,GTPSCS,Succinyl-CoA synthetase beta-G chain,SCS-betaG' 
# 
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 
;MSYTASRQHLYVDKNTKIICQGFTGKQGTFHSQQALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYV
PPPFAAAAINEAIEAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGECKIGIMPGHIHKKGRIGIVS
RSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCLEIFLNDSATEGIILIGEIGGNAEENAAEFLKQHNSGPNSK
PVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKEKISALQSAGVVVSMSPAQLGTTIYKEFEKRKMLENLYFQGHHHHHHH
H
;
;MSYTASRQHLYVDKNTKIICQGFTGKQGTFHSQQALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYV
PPPFAAAAINEAIEAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGECKIGIMPGHIHKKGRIGIVS
RSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCLEIFLNDSATEGIILIGEIGGNAEENAAEFLKQHNSGPNSK
PVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKEKISALQSAGVVVSMSPAQLGTTIYKEFEKRKMLENLYFQGHHHHHHH
H
;
A ? 
2 'polypeptide(L)' no no 
;MNLQEYQSKKLMSDNGVRVQRFFVADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLA
KQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIFE
GIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMD
DKSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEA
ILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLEDAAKKAVASVAKK
;
;MNLQEYQSKKLMSDNGVRVQRFFVADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLA
KQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIFE
GIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMD
DKSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEA
ILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLEDAAKKAVASVAKK
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'COENZYME A'                   COA 
4 'PHOSPHATE ION'                PO4 
5 '(2S)-2-HYDROXYPROPANOIC ACID' 2OP 
6 'MAGNESIUM ION'                MG  
7 water                          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   TYR n 
1 4   THR n 
1 5   ALA n 
1 6   SER n 
1 7   ARG n 
1 8   GLN n 
1 9   HIS n 
1 10  LEU n 
1 11  TYR n 
1 12  VAL n 
1 13  ASP n 
1 14  LYS n 
1 15  ASN n 
1 16  THR n 
1 17  LYS n 
1 18  ILE n 
1 19  ILE n 
1 20  CYS n 
1 21  GLN n 
1 22  GLY n 
1 23  PHE n 
1 24  THR n 
1 25  GLY n 
1 26  LYS n 
1 27  GLN n 
1 28  GLY n 
1 29  THR n 
1 30  PHE n 
1 31  HIS n 
1 32  SER n 
1 33  GLN n 
1 34  GLN n 
1 35  ALA n 
1 36  LEU n 
1 37  GLU n 
1 38  TYR n 
1 39  GLY n 
1 40  THR n 
1 41  LYS n 
1 42  LEU n 
1 43  VAL n 
1 44  GLY n 
1 45  GLY n 
1 46  THR n 
1 47  THR n 
1 48  PRO n 
1 49  GLY n 
1 50  LYS n 
1 51  GLY n 
1 52  GLY n 
1 53  GLN n 
1 54  THR n 
1 55  HIS n 
1 56  LEU n 
1 57  GLY n 
1 58  LEU n 
1 59  PRO n 
1 60  VAL n 
1 61  PHE n 
1 62  ASN n 
1 63  THR n 
1 64  VAL n 
1 65  LYS n 
1 66  GLU n 
1 67  ALA n 
1 68  LYS n 
1 69  GLU n 
1 70  GLN n 
1 71  THR n 
1 72  GLY n 
1 73  ALA n 
1 74  THR n 
1 75  ALA n 
1 76  SER n 
1 77  VAL n 
1 78  ILE n 
1 79  TYR n 
1 80  VAL n 
1 81  PRO n 
1 82  PRO n 
1 83  PRO n 
1 84  PHE n 
1 85  ALA n 
1 86  ALA n 
1 87  ALA n 
1 88  ALA n 
1 89  ILE n 
1 90  ASN n 
1 91  GLU n 
1 92  ALA n 
1 93  ILE n 
1 94  GLU n 
1 95  ALA n 
1 96  GLU n 
1 97  ILE n 
1 98  PRO n 
1 99  LEU n 
1 100 VAL n 
1 101 VAL n 
1 102 CYS n 
1 103 ILE n 
1 104 THR n 
1 105 GLU n 
1 106 GLY n 
1 107 ILE n 
1 108 PRO n 
1 109 GLN n 
1 110 GLN n 
1 111 ASP n 
1 112 MET n 
1 113 VAL n 
1 114 ARG n 
1 115 VAL n 
1 116 LYS n 
1 117 HIS n 
1 118 LYS n 
1 119 LEU n 
1 120 LEU n 
1 121 ARG n 
1 122 GLN n 
1 123 GLU n 
1 124 LYS n 
1 125 THR n 
1 126 ARG n 
1 127 LEU n 
1 128 ILE n 
1 129 GLY n 
1 130 PRO n 
1 131 ASN n 
1 132 CYS n 
1 133 PRO n 
1 134 GLY n 
1 135 VAL n 
1 136 ILE n 
1 137 ASN n 
1 138 PRO n 
1 139 GLY n 
1 140 GLU n 
1 141 CYS n 
1 142 LYS n 
1 143 ILE n 
1 144 GLY n 
1 145 ILE n 
1 146 MET n 
1 147 PRO n 
1 148 GLY n 
1 149 HIS n 
1 150 ILE n 
1 151 HIS n 
1 152 LYS n 
1 153 LYS n 
1 154 GLY n 
1 155 ARG n 
1 156 ILE n 
1 157 GLY n 
1 158 ILE n 
1 159 VAL n 
1 160 SER n 
1 161 ARG n 
1 162 SER n 
1 163 GLY n 
1 164 THR n 
1 165 LEU n 
1 166 THR n 
1 167 TYR n 
1 168 GLU n 
1 169 ALA n 
1 170 VAL n 
1 171 HIS n 
1 172 GLN n 
1 173 THR n 
1 174 THR n 
1 175 GLN n 
1 176 VAL n 
1 177 GLY n 
1 178 LEU n 
1 179 GLY n 
1 180 GLN n 
1 181 SER n 
1 182 LEU n 
1 183 CYS n 
1 184 VAL n 
1 185 GLY n 
1 186 ILE n 
1 187 GLY n 
1 188 GLY n 
1 189 ASP n 
1 190 PRO n 
1 191 PHE n 
1 192 ASN n 
1 193 GLY n 
1 194 THR n 
1 195 ASP n 
1 196 PHE n 
1 197 ILE n 
1 198 ASP n 
1 199 CYS n 
1 200 LEU n 
1 201 GLU n 
1 202 ILE n 
1 203 PHE n 
1 204 LEU n 
1 205 ASN n 
1 206 ASP n 
1 207 SER n 
1 208 ALA n 
1 209 THR n 
1 210 GLU n 
1 211 GLY n 
1 212 ILE n 
1 213 ILE n 
1 214 LEU n 
1 215 ILE n 
1 216 GLY n 
1 217 GLU n 
1 218 ILE n 
1 219 GLY n 
1 220 GLY n 
1 221 ASN n 
1 222 ALA n 
1 223 GLU n 
1 224 GLU n 
1 225 ASN n 
1 226 ALA n 
1 227 ALA n 
1 228 GLU n 
1 229 PHE n 
1 230 LEU n 
1 231 LYS n 
1 232 GLN n 
1 233 HIS n 
1 234 ASN n 
1 235 SER n 
1 236 GLY n 
1 237 PRO n 
1 238 ASN n 
1 239 SER n 
1 240 LYS n 
1 241 PRO n 
1 242 VAL n 
1 243 VAL n 
1 244 SER n 
1 245 PHE n 
1 246 ILE n 
1 247 ALA n 
1 248 GLY n 
1 249 LEU n 
1 250 THR n 
1 251 ALA n 
1 252 PRO n 
1 253 PRO n 
1 254 GLY n 
1 255 ARG n 
1 256 ARG n 
1 257 MET n 
1 258 GLY n 
1 259 HIS n 
1 260 ALA n 
1 261 GLY n 
1 262 ALA n 
1 263 ILE n 
1 264 ILE n 
1 265 ALA n 
1 266 GLY n 
1 267 GLY n 
1 268 LYS n 
1 269 GLY n 
1 270 GLY n 
1 271 ALA n 
1 272 LYS n 
1 273 GLU n 
1 274 LYS n 
1 275 ILE n 
1 276 SER n 
1 277 ALA n 
1 278 LEU n 
1 279 GLN n 
1 280 SER n 
1 281 ALA n 
1 282 GLY n 
1 283 VAL n 
1 284 VAL n 
1 285 VAL n 
1 286 SER n 
1 287 MET n 
1 288 SER n 
1 289 PRO n 
1 290 ALA n 
1 291 GLN n 
1 292 LEU n 
1 293 GLY n 
1 294 THR n 
1 295 THR n 
1 296 ILE n 
1 297 TYR n 
1 298 LYS n 
1 299 GLU n 
1 300 PHE n 
1 301 GLU n 
1 302 LYS n 
1 303 ARG n 
1 304 LYS n 
1 305 MET n 
1 306 LEU n 
1 307 GLU n 
1 308 ASN n 
1 309 LEU n 
1 310 TYR n 
1 311 PHE n 
1 312 GLN n 
1 313 GLY n 
1 314 HIS n 
1 315 HIS n 
1 316 HIS n 
1 317 HIS n 
1 318 HIS n 
1 319 HIS n 
1 320 HIS n 
1 321 HIS n 
2 1   MET n 
2 2   ASN n 
2 3   LEU n 
2 4   GLN n 
2 5   GLU n 
2 6   TYR n 
2 7   GLN n 
2 8   SER n 
2 9   LYS n 
2 10  LYS n 
2 11  LEU n 
2 12  MET n 
2 13  SER n 
2 14  ASP n 
2 15  ASN n 
2 16  GLY n 
2 17  VAL n 
2 18  ARG n 
2 19  VAL n 
2 20  GLN n 
2 21  ARG n 
2 22  PHE n 
2 23  PHE n 
2 24  VAL n 
2 25  ALA n 
2 26  ASP n 
2 27  THR n 
2 28  ALA n 
2 29  ASN n 
2 30  GLU n 
2 31  ALA n 
2 32  LEU n 
2 33  GLU n 
2 34  ALA n 
2 35  ALA n 
2 36  LYS n 
2 37  ARG n 
2 38  LEU n 
2 39  ASN n 
2 40  ALA n 
2 41  LYS n 
2 42  GLU n 
2 43  ILE n 
2 44  VAL n 
2 45  LEU n 
2 46  LYS n 
2 47  ALA n 
2 48  GLN n 
2 49  ILE n 
2 50  LEU n 
2 51  ALA n 
2 52  GLY n 
2 53  GLY n 
2 54  ARG n 
2 55  GLY n 
2 56  LYS n 
2 57  GLY n 
2 58  VAL n 
2 59  PHE n 
2 60  ASN n 
2 61  SER n 
2 62  GLY n 
2 63  LEU n 
2 64  LYS n 
2 65  GLY n 
2 66  GLY n 
2 67  VAL n 
2 68  HIS n 
2 69  LEU n 
2 70  THR n 
2 71  LYS n 
2 72  ASP n 
2 73  PRO n 
2 74  ASN n 
2 75  VAL n 
2 76  VAL n 
2 77  GLY n 
2 78  GLN n 
2 79  LEU n 
2 80  ALA n 
2 81  LYS n 
2 82  GLN n 
2 83  MET n 
2 84  ILE n 
2 85  GLY n 
2 86  TYR n 
2 87  ASN n 
2 88  LEU n 
2 89  ALA n 
2 90  THR n 
2 91  LYS n 
2 92  GLN n 
2 93  THR n 
2 94  PRO n 
2 95  LYS n 
2 96  GLU n 
2 97  GLY n 
2 98  VAL n 
2 99  LYS n 
2 100 VAL n 
2 101 ASN n 
2 102 LYS n 
2 103 VAL n 
2 104 MET n 
2 105 VAL n 
2 106 ALA n 
2 107 GLU n 
2 108 ALA n 
2 109 LEU n 
2 110 ASP n 
2 111 ILE n 
2 112 SER n 
2 113 ARG n 
2 114 GLU n 
2 115 THR n 
2 116 TYR n 
2 117 LEU n 
2 118 ALA n 
2 119 ILE n 
2 120 LEU n 
2 121 MET n 
2 122 ASP n 
2 123 ARG n 
2 124 SER n 
2 125 CYS n 
2 126 ASN n 
2 127 GLY n 
2 128 PRO n 
2 129 VAL n 
2 130 LEU n 
2 131 VAL n 
2 132 GLY n 
2 133 SER n 
2 134 PRO n 
2 135 GLN n 
2 136 GLY n 
2 137 GLY n 
2 138 VAL n 
2 139 ASP n 
2 140 ILE n 
2 141 GLU n 
2 142 GLU n 
2 143 VAL n 
2 144 ALA n 
2 145 ALA n 
2 146 SER n 
2 147 ASN n 
2 148 PRO n 
2 149 GLU n 
2 150 LEU n 
2 151 ILE n 
2 152 PHE n 
2 153 LYS n 
2 154 GLU n 
2 155 GLN n 
2 156 ILE n 
2 157 ASP n 
2 158 ILE n 
2 159 PHE n 
2 160 GLU n 
2 161 GLY n 
2 162 ILE n 
2 163 LYS n 
2 164 ASP n 
2 165 SER n 
2 166 GLN n 
2 167 ALA n 
2 168 GLN n 
2 169 ARG n 
2 170 MET n 
2 171 ALA n 
2 172 GLU n 
2 173 ASN n 
2 174 LEU n 
2 175 GLY n 
2 176 PHE n 
2 177 VAL n 
2 178 GLY n 
2 179 PRO n 
2 180 LEU n 
2 181 LYS n 
2 182 SER n 
2 183 GLN n 
2 184 ALA n 
2 185 ALA n 
2 186 ASP n 
2 187 GLN n 
2 188 ILE n 
2 189 THR n 
2 190 LYS n 
2 191 LEU n 
2 192 TYR n 
2 193 ASN n 
2 194 LEU n 
2 195 PHE n 
2 196 LEU n 
2 197 LYS n 
2 198 ILE n 
2 199 ASP n 
2 200 ALA n 
2 201 THR n 
2 202 GLN n 
2 203 VAL n 
2 204 GLU n 
2 205 VAL n 
2 206 ASN n 
2 207 PRO n 
2 208 PHE n 
2 209 GLY n 
2 210 GLU n 
2 211 THR n 
2 212 PRO n 
2 213 GLU n 
2 214 GLY n 
2 215 GLN n 
2 216 VAL n 
2 217 VAL n 
2 218 CYS n 
2 219 PHE n 
2 220 ASP n 
2 221 ALA n 
2 222 LYS n 
2 223 ILE n 
2 224 ASN n 
2 225 PHE n 
2 226 ASP n 
2 227 ASP n 
2 228 ASN n 
2 229 ALA n 
2 230 GLU n 
2 231 PHE n 
2 232 ARG n 
2 233 GLN n 
2 234 LYS n 
2 235 ASP n 
2 236 ILE n 
2 237 PHE n 
2 238 ALA n 
2 239 MET n 
2 240 ASP n 
2 241 ASP n 
2 242 LYS n 
2 243 SER n 
2 244 GLU n 
2 245 ASN n 
2 246 GLU n 
2 247 PRO n 
2 248 ILE n 
2 249 GLU n 
2 250 ASN n 
2 251 GLU n 
2 252 ALA n 
2 253 ALA n 
2 254 LYS n 
2 255 TYR n 
2 256 ASP n 
2 257 LEU n 
2 258 LYS n 
2 259 TYR n 
2 260 ILE n 
2 261 GLY n 
2 262 LEU n 
2 263 ASP n 
2 264 GLY n 
2 265 ASN n 
2 266 ILE n 
2 267 ALA n 
2 268 CYS n 
2 269 PHE n 
2 270 VAL n 
2 271 ASN n 
2 272 GLY n 
2 273 ALA n 
2 274 GLY n 
2 275 LEU n 
2 276 ALA n 
2 277 MET n 
2 278 ALA n 
2 279 THR n 
2 280 CYS n 
2 281 ASP n 
2 282 ILE n 
2 283 ILE n 
2 284 PHE n 
2 285 LEU n 
2 286 ASN n 
2 287 GLY n 
2 288 GLY n 
2 289 LYS n 
2 290 PRO n 
2 291 ALA n 
2 292 ASN n 
2 293 PHE n 
2 294 LEU n 
2 295 ASP n 
2 296 LEU n 
2 297 GLY n 
2 298 GLY n 
2 299 GLY n 
2 300 VAL n 
2 301 LYS n 
2 302 GLU n 
2 303 ALA n 
2 304 GLN n 
2 305 VAL n 
2 306 TYR n 
2 307 GLN n 
2 308 ALA n 
2 309 PHE n 
2 310 LYS n 
2 311 LEU n 
2 312 LEU n 
2 313 THR n 
2 314 ALA n 
2 315 ASP n 
2 316 PRO n 
2 317 LYS n 
2 318 VAL n 
2 319 GLU n 
2 320 ALA n 
2 321 ILE n 
2 322 LEU n 
2 323 VAL n 
2 324 ASN n 
2 325 ILE n 
2 326 PHE n 
2 327 GLY n 
2 328 GLY n 
2 329 ILE n 
2 330 VAL n 
2 331 ASN n 
2 332 CYS n 
2 333 ALA n 
2 334 ILE n 
2 335 ILE n 
2 336 ALA n 
2 337 ASN n 
2 338 GLY n 
2 339 ILE n 
2 340 THR n 
2 341 LYS n 
2 342 ALA n 
2 343 CYS n 
2 344 ARG n 
2 345 GLU n 
2 346 LEU n 
2 347 GLU n 
2 348 LEU n 
2 349 LYS n 
2 350 VAL n 
2 351 PRO n 
2 352 LEU n 
2 353 VAL n 
2 354 VAL n 
2 355 ARG n 
2 356 LEU n 
2 357 GLU n 
2 358 GLY n 
2 359 THR n 
2 360 ASN n 
2 361 VAL n 
2 362 GLN n 
2 363 GLU n 
2 364 ALA n 
2 365 GLN n 
2 366 LYS n 
2 367 ILE n 
2 368 LEU n 
2 369 ASN n 
2 370 ASN n 
2 371 SER n 
2 372 GLY n 
2 373 LEU n 
2 374 PRO n 
2 375 ILE n 
2 376 THR n 
2 377 SER n 
2 378 ALA n 
2 379 ILE n 
2 380 ASP n 
2 381 LEU n 
2 382 GLU n 
2 383 ASP n 
2 384 ALA n 
2 385 ALA n 
2 386 LYS n 
2 387 LYS n 
2 388 ALA n 
2 389 VAL n 
2 390 ALA n 
2 391 SER n 
2 392 VAL n 
2 393 ALA n 
2 394 LYS n 
2 395 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' 1 321 human ? SUCLG1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 
469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 395 human ? SUCLG2 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 
469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
2OP non-polymer         . '(2S)-2-HYDROXYPROPANOIC ACID' ? 'C3 H6 O3'            90.078  
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 
COA non-polymer         . 'COENZYME A'                   ? 'C21 H36 N7 O16 P3 S' 767.534 
CYS 'L-peptide linking' y CYSTEINE                       ? 'C3 H7 N O2 S'        121.158 
GLN 'L-peptide linking' y GLUTAMINE                      ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                        ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                      ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                          ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                     ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                        ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                         ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                     ? 'C5 H11 N O2 S'       149.211 
MG  non-polymer         . 'MAGNESIUM ION'                ? 'Mg 2'                24.305  
PHE 'L-peptide linking' y PHENYLALANINE                  ? 'C9 H11 N O2'         165.189 
PO4 non-polymer         . 'PHOSPHATE ION'                ? 'O4 P -3'             94.971  
PRO 'L-peptide linking' y PROLINE                        ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                         ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                      ? 'C4 H9 N O3'          119.119 
TYR 'L-peptide linking' y TYROSINE                       ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                         ? 'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   2   SER SER A . n 
A 1 3   TYR 3   3   3   TYR TYR A . n 
A 1 4   THR 4   4   4   THR THR A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   ARG 7   7   7   ARG ARG A . n 
A 1 8   GLN 8   8   8   GLN GLN A . n 
A 1 9   HIS 9   9   9   HIS HIS A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  TYR 11  11  11  TYR TYR A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  LYS 14  14  14  LYS LYS A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  THR 16  16  16  THR THR A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  CYS 20  20  20  CYS CYS A . n 
A 1 21  GLN 21  21  21  GLN GLN A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  PHE 23  23  23  PHE PHE A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  LYS 26  26  26  LYS LYS A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  THR 29  29  29  THR THR A . n 
A 1 30  PHE 30  30  30  PHE PHE A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  GLN 33  33  33  GLN GLN A . n 
A 1 34  GLN 34  34  34  GLN GLN A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  THR 46  46  46  THR THR A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  HIS 55  55  55  HIS HIS A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  PRO 59  59  59  PRO PRO A . n 
A 1 60  VAL 60  60  60  VAL VAL A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  GLN 70  70  70  GLN GLN A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  PRO 81  81  81  PRO PRO A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  PHE 84  84  84  PHE PHE A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  GLU 96  96  96  GLU GLU A . n 
A 1 97  ILE 97  97  97  ILE ILE A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 CYS 102 102 102 CYS CYS A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 THR 104 104 104 THR THR A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLN 109 109 109 GLN GLN A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 ASP 111 111 111 ASP ASP A . n 
A 1 112 MET 112 112 112 MET MET A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 GLN 122 122 122 GLN GLN A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 ARG 126 126 126 ARG ARG A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 ILE 128 128 128 ILE ILE A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 CYS 132 132 132 CYS CYS A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 ASN 137 137 137 ASN ASN A . n 
A 1 138 PRO 138 138 138 PRO PRO A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 CYS 141 141 141 CYS CYS A . n 
A 1 142 LYS 142 142 142 LYS LYS A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 MET 146 146 146 MET MET A . n 
A 1 147 PRO 147 147 147 PRO PRO A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 HIS 149 149 149 HIS HIS A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 HIS 151 151 151 HIS HIS A . n 
A 1 152 LYS 152 152 152 LYS LYS A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 VAL 170 170 170 VAL VAL A . n 
A 1 171 HIS 171 171 171 HIS HIS A . n 
A 1 172 GLN 172 172 172 GLN GLN A . n 
A 1 173 THR 173 173 173 THR THR A . n 
A 1 174 THR 174 174 174 THR THR A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 VAL 176 176 176 VAL VAL A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 CYS 183 183 183 CYS CYS A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 PHE 191 191 191 PHE PHE A . n 
A 1 192 ASN 192 192 192 ASN ASN A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 PHE 196 196 196 PHE PHE A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 ASP 198 198 198 ASP ASP A . n 
A 1 199 CYS 199 199 199 CYS CYS A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 GLU 201 201 201 GLU GLU A . n 
A 1 202 ILE 202 202 202 ILE ILE A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 ASP 206 206 206 ASP ASP A . n 
A 1 207 SER 207 207 207 SER SER A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 GLY 216 216 216 GLY GLY A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 GLY 219 219 219 GLY GLY A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 ASN 225 225 225 ASN ASN A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 PHE 229 229 229 PHE PHE A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 LYS 231 231 231 LYS LYS A . n 
A 1 232 GLN 232 232 232 GLN GLN A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 ASN 234 234 234 ASN ASN A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 VAL 242 242 242 VAL VAL A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 GLY 248 248 248 GLY GLY A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 THR 250 250 250 THR THR A . n 
A 1 251 ALA 251 251 251 ALA ALA A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 PRO 253 253 253 PRO PRO A . n 
A 1 254 GLY 254 254 254 GLY GLY A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 MET 257 257 257 MET MET A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 HIS 259 259 259 HIS HIS A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 GLY 261 261 261 GLY GLY A . n 
A 1 262 ALA 262 262 262 ALA ALA A . n 
A 1 263 ILE 263 263 263 ILE ILE A . n 
A 1 264 ILE 264 264 264 ILE ILE A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 LYS 268 268 268 LYS LYS A . n 
A 1 269 GLY 269 269 269 GLY GLY A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 LYS 272 272 272 LYS LYS A . n 
A 1 273 GLU 273 273 273 GLU GLU A . n 
A 1 274 LYS 274 274 274 LYS LYS A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 SER 276 276 276 SER SER A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 GLN 279 279 279 GLN GLN A . n 
A 1 280 SER 280 280 280 SER SER A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 GLY 282 282 282 GLY GLY A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 VAL 285 285 285 VAL VAL A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 MET 287 287 287 MET MET A . n 
A 1 288 SER 288 288 288 SER SER A . n 
A 1 289 PRO 289 289 289 PRO PRO A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 GLN 291 291 291 GLN GLN A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 THR 294 294 294 THR THR A . n 
A 1 295 THR 295 295 295 THR THR A . n 
A 1 296 ILE 296 296 296 ILE ILE A . n 
A 1 297 TYR 297 297 297 TYR TYR A . n 
A 1 298 LYS 298 298 298 LYS LYS A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 GLU 301 301 301 GLU GLU A . n 
A 1 302 LYS 302 302 302 LYS LYS A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 MET 305 305 305 MET MET A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 ASN 308 308 308 ASN ASN A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 TYR 310 310 310 TYR TYR A . n 
A 1 311 PHE 311 311 311 PHE PHE A . n 
A 1 312 GLN 312 312 312 GLN GLN A . n 
A 1 313 GLY 313 313 ?   ?   ?   A . n 
A 1 314 HIS 314 314 ?   ?   ?   A . n 
A 1 315 HIS 315 315 ?   ?   ?   A . n 
A 1 316 HIS 316 316 ?   ?   ?   A . n 
A 1 317 HIS 317 317 ?   ?   ?   A . n 
A 1 318 HIS 318 318 ?   ?   ?   A . n 
A 1 319 HIS 319 319 ?   ?   ?   A . n 
A 1 320 HIS 320 320 ?   ?   ?   A . n 
A 1 321 HIS 321 321 ?   ?   ?   A . n 
B 2 1   MET 1   1   1   MET MET B . n 
B 2 2   ASN 2   2   2   ASN ASN B . n 
B 2 3   LEU 3   3   3   LEU LEU B . n 
B 2 4   GLN 4   4   4   GLN GLN B . n 
B 2 5   GLU 5   5   5   GLU GLU B . n 
B 2 6   TYR 6   6   6   TYR TYR B . n 
B 2 7   GLN 7   7   7   GLN GLN B . n 
B 2 8   SER 8   8   8   SER SER B . n 
B 2 9   LYS 9   9   9   LYS LYS B . n 
B 2 10  LYS 10  10  10  LYS LYS B . n 
B 2 11  LEU 11  11  11  LEU LEU B . n 
B 2 12  MET 12  12  12  MET MET B . n 
B 2 13  SER 13  13  13  SER SER B . n 
B 2 14  ASP 14  14  14  ASP ASP B . n 
B 2 15  ASN 15  15  15  ASN ASN B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  VAL 17  17  17  VAL VAL B . n 
B 2 18  ARG 18  18  18  ARG ARG B . n 
B 2 19  VAL 19  19  19  VAL VAL B . n 
B 2 20  GLN 20  20  20  GLN GLN B . n 
B 2 21  ARG 21  21  21  ARG ARG B . n 
B 2 22  PHE 22  22  22  PHE PHE B . n 
B 2 23  PHE 23  23  23  PHE PHE B . n 
B 2 24  VAL 24  24  24  VAL VAL B . n 
B 2 25  ALA 25  25  25  ALA ALA B . n 
B 2 26  ASP 26  26  26  ASP ASP B . n 
B 2 27  THR 27  27  27  THR THR B . n 
B 2 28  ALA 28  28  28  ALA ALA B . n 
B 2 29  ASN 29  29  29  ASN ASN B . n 
B 2 30  GLU 30  30  30  GLU GLU B . n 
B 2 31  ALA 31  31  31  ALA ALA B . n 
B 2 32  LEU 32  32  32  LEU LEU B . n 
B 2 33  GLU 33  33  33  GLU GLU B . n 
B 2 34  ALA 34  34  34  ALA ALA B . n 
B 2 35  ALA 35  35  35  ALA ALA B . n 
B 2 36  LYS 36  36  36  LYS LYS B . n 
B 2 37  ARG 37  37  37  ARG ARG B . n 
B 2 38  LEU 38  38  38  LEU LEU B . n 
B 2 39  ASN 39  39  39  ASN ASN B . n 
B 2 40  ALA 40  40  40  ALA ALA B . n 
B 2 41  LYS 41  41  41  LYS LYS B . n 
B 2 42  GLU 42  42  42  GLU GLU B . n 
B 2 43  ILE 43  43  43  ILE ILE B . n 
B 2 44  VAL 44  44  44  VAL VAL B . n 
B 2 45  LEU 45  45  45  LEU LEU B . n 
B 2 46  LYS 46  46  46  LYS LYS B . n 
B 2 47  ALA 47  47  47  ALA ALA B . n 
B 2 48  GLN 48  48  48  GLN GLN B . n 
B 2 49  ILE 49  49  49  ILE ILE B . n 
B 2 50  LEU 50  50  50  LEU LEU B . n 
B 2 51  ALA 51  51  51  ALA ALA B . n 
B 2 52  GLY 52  52  52  GLY GLY B . n 
B 2 53  GLY 53  53  53  GLY GLY B . n 
B 2 54  ARG 54  54  54  ARG ARG B . n 
B 2 55  GLY 55  55  55  GLY GLY B . n 
B 2 56  LYS 56  56  56  LYS LYS B . n 
B 2 57  GLY 57  57  57  GLY GLY B . n 
B 2 58  VAL 58  58  58  VAL VAL B . n 
B 2 59  PHE 59  59  59  PHE PHE B . n 
B 2 60  ASN 60  60  60  ASN ASN B . n 
B 2 61  SER 61  61  61  SER SER B . n 
B 2 62  GLY 62  62  62  GLY GLY B . n 
B 2 63  LEU 63  63  63  LEU LEU B . n 
B 2 64  LYS 64  64  64  LYS LYS B . n 
B 2 65  GLY 65  65  65  GLY GLY B . n 
B 2 66  GLY 66  66  66  GLY GLY B . n 
B 2 67  VAL 67  67  67  VAL VAL B . n 
B 2 68  HIS 68  68  68  HIS HIS B . n 
B 2 69  LEU 69  69  69  LEU LEU B . n 
B 2 70  THR 70  70  70  THR THR B . n 
B 2 71  LYS 71  71  71  LYS LYS B . n 
B 2 72  ASP 72  72  72  ASP ASP B . n 
B 2 73  PRO 73  73  73  PRO PRO B . n 
B 2 74  ASN 74  74  74  ASN ASN B . n 
B 2 75  VAL 75  75  75  VAL VAL B . n 
B 2 76  VAL 76  76  76  VAL VAL B . n 
B 2 77  GLY 77  77  77  GLY GLY B . n 
B 2 78  GLN 78  78  78  GLN GLN B . n 
B 2 79  LEU 79  79  79  LEU LEU B . n 
B 2 80  ALA 80  80  80  ALA ALA B . n 
B 2 81  LYS 81  81  81  LYS LYS B . n 
B 2 82  GLN 82  82  82  GLN GLN B . n 
B 2 83  MET 83  83  83  MET MET B . n 
B 2 84  ILE 84  84  84  ILE ILE B . n 
B 2 85  GLY 85  85  85  GLY GLY B . n 
B 2 86  TYR 86  86  86  TYR TYR B . n 
B 2 87  ASN 87  87  87  ASN ASN B . n 
B 2 88  LEU 88  88  88  LEU LEU B . n 
B 2 89  ALA 89  89  89  ALA ALA B . n 
B 2 90  THR 90  90  90  THR THR B . n 
B 2 91  LYS 91  91  91  LYS LYS B . n 
B 2 92  GLN 92  92  92  GLN GLN B . n 
B 2 93  THR 93  93  93  THR THR B . n 
B 2 94  PRO 94  94  94  PRO PRO B . n 
B 2 95  LYS 95  95  95  LYS LYS B . n 
B 2 96  GLU 96  96  96  GLU GLU B . n 
B 2 97  GLY 97  97  97  GLY GLY B . n 
B 2 98  VAL 98  98  98  VAL VAL B . n 
B 2 99  LYS 99  99  99  LYS LYS B . n 
B 2 100 VAL 100 100 100 VAL VAL B . n 
B 2 101 ASN 101 101 101 ASN ASN B . n 
B 2 102 LYS 102 102 102 LYS LYS B . n 
B 2 103 VAL 103 103 103 VAL VAL B . n 
B 2 104 MET 104 104 104 MET MET B . n 
B 2 105 VAL 105 105 105 VAL VAL B . n 
B 2 106 ALA 106 106 106 ALA ALA B . n 
B 2 107 GLU 107 107 107 GLU GLU B . n 
B 2 108 ALA 108 108 108 ALA ALA B . n 
B 2 109 LEU 109 109 109 LEU LEU B . n 
B 2 110 ASP 110 110 110 ASP ASP B . n 
B 2 111 ILE 111 111 111 ILE ILE B . n 
B 2 112 SER 112 112 112 SER SER B . n 
B 2 113 ARG 113 113 113 ARG ARG B . n 
B 2 114 GLU 114 114 114 GLU GLU B . n 
B 2 115 THR 115 115 115 THR THR B . n 
B 2 116 TYR 116 116 116 TYR TYR B . n 
B 2 117 LEU 117 117 117 LEU LEU B . n 
B 2 118 ALA 118 118 118 ALA ALA B . n 
B 2 119 ILE 119 119 119 ILE ILE B . n 
B 2 120 LEU 120 120 120 LEU LEU B . n 
B 2 121 MET 121 121 121 MET MET B . n 
B 2 122 ASP 122 122 122 ASP ASP B . n 
B 2 123 ARG 123 123 123 ARG ARG B . n 
B 2 124 SER 124 124 124 SER SER B . n 
B 2 125 CYS 125 125 125 CYS CYS B . n 
B 2 126 ASN 126 126 126 ASN ASN B . n 
B 2 127 GLY 127 127 127 GLY GLY B . n 
B 2 128 PRO 128 128 128 PRO PRO B . n 
B 2 129 VAL 129 129 129 VAL VAL B . n 
B 2 130 LEU 130 130 130 LEU LEU B . n 
B 2 131 VAL 131 131 131 VAL VAL B . n 
B 2 132 GLY 132 132 132 GLY GLY B . n 
B 2 133 SER 133 133 133 SER SER B . n 
B 2 134 PRO 134 134 134 PRO PRO B . n 
B 2 135 GLN 135 135 135 GLN GLN B . n 
B 2 136 GLY 136 136 136 GLY GLY B . n 
B 2 137 GLY 137 137 137 GLY GLY B . n 
B 2 138 VAL 138 138 138 VAL VAL B . n 
B 2 139 ASP 139 139 139 ASP ASP B . n 
B 2 140 ILE 140 140 140 ILE ILE B . n 
B 2 141 GLU 141 141 141 GLU GLU B . n 
B 2 142 GLU 142 142 142 GLU GLU B . n 
B 2 143 VAL 143 143 143 VAL VAL B . n 
B 2 144 ALA 144 144 144 ALA ALA B . n 
B 2 145 ALA 145 145 145 ALA ALA B . n 
B 2 146 SER 146 146 146 SER SER B . n 
B 2 147 ASN 147 147 147 ASN ASN B . n 
B 2 148 PRO 148 148 148 PRO PRO B . n 
B 2 149 GLU 149 149 149 GLU GLU B . n 
B 2 150 LEU 150 150 150 LEU LEU B . n 
B 2 151 ILE 151 151 151 ILE ILE B . n 
B 2 152 PHE 152 152 152 PHE PHE B . n 
B 2 153 LYS 153 153 153 LYS LYS B . n 
B 2 154 GLU 154 154 154 GLU GLU B . n 
B 2 155 GLN 155 155 155 GLN GLN B . n 
B 2 156 ILE 156 156 156 ILE ILE B . n 
B 2 157 ASP 157 157 157 ASP ASP B . n 
B 2 158 ILE 158 158 158 ILE ILE B . n 
B 2 159 PHE 159 159 159 PHE PHE B . n 
B 2 160 GLU 160 160 160 GLU GLU B . n 
B 2 161 GLY 161 161 161 GLY GLY B . n 
B 2 162 ILE 162 162 162 ILE ILE B . n 
B 2 163 LYS 163 163 163 LYS LYS B . n 
B 2 164 ASP 164 164 164 ASP ASP B . n 
B 2 165 SER 165 165 165 SER SER B . n 
B 2 166 GLN 166 166 166 GLN GLN B . n 
B 2 167 ALA 167 167 167 ALA ALA B . n 
B 2 168 GLN 168 168 168 GLN GLN B . n 
B 2 169 ARG 169 169 169 ARG ARG B . n 
B 2 170 MET 170 170 170 MET MET B . n 
B 2 171 ALA 171 171 171 ALA ALA B . n 
B 2 172 GLU 172 172 172 GLU GLU B . n 
B 2 173 ASN 173 173 173 ASN ASN B . n 
B 2 174 LEU 174 174 174 LEU LEU B . n 
B 2 175 GLY 175 175 175 GLY GLY B . n 
B 2 176 PHE 176 176 176 PHE PHE B . n 
B 2 177 VAL 177 177 177 VAL VAL B . n 
B 2 178 GLY 178 178 178 GLY GLY B . n 
B 2 179 PRO 179 179 179 PRO PRO B . n 
B 2 180 LEU 180 180 180 LEU LEU B . n 
B 2 181 LYS 181 181 181 LYS LYS B . n 
B 2 182 SER 182 182 182 SER SER B . n 
B 2 183 GLN 183 183 183 GLN GLN B . n 
B 2 184 ALA 184 184 184 ALA ALA B . n 
B 2 185 ALA 185 185 185 ALA ALA B . n 
B 2 186 ASP 186 186 186 ASP ASP B . n 
B 2 187 GLN 187 187 187 GLN GLN B . n 
B 2 188 ILE 188 188 188 ILE ILE B . n 
B 2 189 THR 189 189 189 THR THR B . n 
B 2 190 LYS 190 190 190 LYS LYS B . n 
B 2 191 LEU 191 191 191 LEU LEU B . n 
B 2 192 TYR 192 192 192 TYR TYR B . n 
B 2 193 ASN 193 193 193 ASN ASN B . n 
B 2 194 LEU 194 194 194 LEU LEU B . n 
B 2 195 PHE 195 195 195 PHE PHE B . n 
B 2 196 LEU 196 196 196 LEU LEU B . n 
B 2 197 LYS 197 197 197 LYS LYS B . n 
B 2 198 ILE 198 198 198 ILE ILE B . n 
B 2 199 ASP 199 199 199 ASP ASP B . n 
B 2 200 ALA 200 200 200 ALA ALA B . n 
B 2 201 THR 201 201 201 THR THR B . n 
B 2 202 GLN 202 202 202 GLN GLN B . n 
B 2 203 VAL 203 203 203 VAL VAL B . n 
B 2 204 GLU 204 204 204 GLU GLU B . n 
B 2 205 VAL 205 205 205 VAL VAL B . n 
B 2 206 ASN 206 206 206 ASN ASN B . n 
B 2 207 PRO 207 207 207 PRO PRO B . n 
B 2 208 PHE 208 208 208 PHE PHE B . n 
B 2 209 GLY 209 209 209 GLY GLY B . n 
B 2 210 GLU 210 210 210 GLU GLU B . n 
B 2 211 THR 211 211 211 THR THR B . n 
B 2 212 PRO 212 212 212 PRO PRO B . n 
B 2 213 GLU 213 213 213 GLU GLU B . n 
B 2 214 GLY 214 214 214 GLY GLY B . n 
B 2 215 GLN 215 215 215 GLN GLN B . n 
B 2 216 VAL 216 216 216 VAL VAL B . n 
B 2 217 VAL 217 217 217 VAL VAL B . n 
B 2 218 CYS 218 218 218 CYS CYS B . n 
B 2 219 PHE 219 219 219 PHE PHE B . n 
B 2 220 ASP 220 220 220 ASP ASP B . n 
B 2 221 ALA 221 221 221 ALA ALA B . n 
B 2 222 LYS 222 222 222 LYS LYS B . n 
B 2 223 ILE 223 223 223 ILE ILE B . n 
B 2 224 ASN 224 224 224 ASN ASN B . n 
B 2 225 PHE 225 225 225 PHE PHE B . n 
B 2 226 ASP 226 226 226 ASP ASP B . n 
B 2 227 ASP 227 227 227 ASP ASP B . n 
B 2 228 ASN 228 228 228 ASN ASN B . n 
B 2 229 ALA 229 229 229 ALA ALA B . n 
B 2 230 GLU 230 230 230 GLU GLU B . n 
B 2 231 PHE 231 231 231 PHE PHE B . n 
B 2 232 ARG 232 232 232 ARG ARG B . n 
B 2 233 GLN 233 233 233 GLN GLN B . n 
B 2 234 LYS 234 234 234 LYS LYS B . n 
B 2 235 ASP 235 235 235 ASP ASP B . n 
B 2 236 ILE 236 236 236 ILE ILE B . n 
B 2 237 PHE 237 237 237 PHE PHE B . n 
B 2 238 ALA 238 238 238 ALA ALA B . n 
B 2 239 MET 239 239 239 MET MET B . n 
B 2 240 ASP 240 240 240 ASP ASP B . n 
B 2 241 ASP 241 241 241 ASP ASP B . n 
B 2 242 LYS 242 242 242 LYS LYS B . n 
B 2 243 SER 243 243 243 SER SER B . n 
B 2 244 GLU 244 244 244 GLU GLU B . n 
B 2 245 ASN 245 245 245 ASN ASN B . n 
B 2 246 GLU 246 246 246 GLU GLU B . n 
B 2 247 PRO 247 247 247 PRO PRO B . n 
B 2 248 ILE 248 248 248 ILE ILE B . n 
B 2 249 GLU 249 249 249 GLU GLU B . n 
B 2 250 ASN 250 250 250 ASN ASN B . n 
B 2 251 GLU 251 251 251 GLU GLU B . n 
B 2 252 ALA 252 252 252 ALA ALA B . n 
B 2 253 ALA 253 253 253 ALA ALA B . n 
B 2 254 LYS 254 254 254 LYS LYS B . n 
B 2 255 TYR 255 255 255 TYR TYR B . n 
B 2 256 ASP 256 256 256 ASP ASP B . n 
B 2 257 LEU 257 257 257 LEU LEU B . n 
B 2 258 LYS 258 258 258 LYS LYS B . n 
B 2 259 TYR 259 259 259 TYR TYR B . n 
B 2 260 ILE 260 260 260 ILE ILE B . n 
B 2 261 GLY 261 261 261 GLY GLY B . n 
B 2 262 LEU 262 262 262 LEU LEU B . n 
B 2 263 ASP 263 263 263 ASP ASP B . n 
B 2 264 GLY 264 264 264 GLY GLY B . n 
B 2 265 ASN 265 265 265 ASN ASN B . n 
B 2 266 ILE 266 266 266 ILE ILE B . n 
B 2 267 ALA 267 267 267 ALA ALA B . n 
B 2 268 CYS 268 268 268 CYS CYS B . n 
B 2 269 PHE 269 269 269 PHE PHE B . n 
B 2 270 VAL 270 270 270 VAL VAL B . n 
B 2 271 ASN 271 271 271 ASN ASN B . n 
B 2 272 GLY 272 272 272 GLY GLY B . n 
B 2 273 ALA 273 273 273 ALA ALA B . n 
B 2 274 GLY 274 274 274 GLY GLY B . n 
B 2 275 LEU 275 275 275 LEU LEU B . n 
B 2 276 ALA 276 276 276 ALA ALA B . n 
B 2 277 MET 277 277 277 MET MET B . n 
B 2 278 ALA 278 278 278 ALA ALA B . n 
B 2 279 THR 279 279 279 THR THR B . n 
B 2 280 CYS 280 280 280 CYS CYS B . n 
B 2 281 ASP 281 281 281 ASP ASP B . n 
B 2 282 ILE 282 282 282 ILE ILE B . n 
B 2 283 ILE 283 283 283 ILE ILE B . n 
B 2 284 PHE 284 284 284 PHE PHE B . n 
B 2 285 LEU 285 285 285 LEU LEU B . n 
B 2 286 ASN 286 286 286 ASN ASN B . n 
B 2 287 GLY 287 287 287 GLY GLY B . n 
B 2 288 GLY 288 288 288 GLY GLY B . n 
B 2 289 LYS 289 289 289 LYS LYS B . n 
B 2 290 PRO 290 290 290 PRO PRO B . n 
B 2 291 ALA 291 291 291 ALA ALA B . n 
B 2 292 ASN 292 292 292 ASN ASN B . n 
B 2 293 PHE 293 293 293 PHE PHE B . n 
B 2 294 LEU 294 294 294 LEU LEU B . n 
B 2 295 ASP 295 295 295 ASP ASP B . n 
B 2 296 LEU 296 296 296 LEU LEU B . n 
B 2 297 GLY 297 297 297 GLY GLY B . n 
B 2 298 GLY 298 298 298 GLY GLY B . n 
B 2 299 GLY 299 299 299 GLY GLY B . n 
B 2 300 VAL 300 300 300 VAL VAL B . n 
B 2 301 LYS 301 301 301 LYS LYS B . n 
B 2 302 GLU 302 302 302 GLU GLU B . n 
B 2 303 ALA 303 303 303 ALA ALA B . n 
B 2 304 GLN 304 304 304 GLN GLN B . n 
B 2 305 VAL 305 305 305 VAL VAL B . n 
B 2 306 TYR 306 306 306 TYR TYR B . n 
B 2 307 GLN 307 307 307 GLN GLN B . n 
B 2 308 ALA 308 308 308 ALA ALA B . n 
B 2 309 PHE 309 309 309 PHE PHE B . n 
B 2 310 LYS 310 310 310 LYS LYS B . n 
B 2 311 LEU 311 311 311 LEU LEU B . n 
B 2 312 LEU 312 312 312 LEU LEU B . n 
B 2 313 THR 313 313 313 THR THR B . n 
B 2 314 ALA 314 314 314 ALA ALA B . n 
B 2 315 ASP 315 315 315 ASP ASP B . n 
B 2 316 PRO 316 316 316 PRO PRO B . n 
B 2 317 LYS 317 317 317 LYS LYS B . n 
B 2 318 VAL 318 318 318 VAL VAL B . n 
B 2 319 GLU 319 319 319 GLU GLU B . n 
B 2 320 ALA 320 320 320 ALA ALA B . n 
B 2 321 ILE 321 321 321 ILE ILE B . n 
B 2 322 LEU 322 322 322 LEU LEU B . n 
B 2 323 VAL 323 323 323 VAL VAL B . n 
B 2 324 ASN 324 324 324 ASN ASN B . n 
B 2 325 ILE 325 325 325 ILE ILE B . n 
B 2 326 PHE 326 326 326 PHE PHE B . n 
B 2 327 GLY 327 327 327 GLY GLY B . n 
B 2 328 GLY 328 328 328 GLY GLY B . n 
B 2 329 ILE 329 329 329 ILE ILE B . n 
B 2 330 VAL 330 330 330 VAL VAL B . n 
B 2 331 ASN 331 331 331 ASN ASN B . n 
B 2 332 CYS 332 332 332 CYS CYS B . n 
B 2 333 ALA 333 333 333 ALA ALA B . n 
B 2 334 ILE 334 334 334 ILE ILE B . n 
B 2 335 ILE 335 335 335 ILE ILE B . n 
B 2 336 ALA 336 336 336 ALA ALA B . n 
B 2 337 ASN 337 337 337 ASN ASN B . n 
B 2 338 GLY 338 338 338 GLY GLY B . n 
B 2 339 ILE 339 339 339 ILE ILE B . n 
B 2 340 THR 340 340 340 THR THR B . n 
B 2 341 LYS 341 341 341 LYS LYS B . n 
B 2 342 ALA 342 342 342 ALA ALA B . n 
B 2 343 CYS 343 343 343 CYS CYS B . n 
B 2 344 ARG 344 344 344 ARG ARG B . n 
B 2 345 GLU 345 345 345 GLU GLU B . n 
B 2 346 LEU 346 346 346 LEU LEU B . n 
B 2 347 GLU 347 347 347 GLU GLU B . n 
B 2 348 LEU 348 348 348 LEU LEU B . n 
B 2 349 LYS 349 349 349 LYS LYS B . n 
B 2 350 VAL 350 350 350 VAL VAL B . n 
B 2 351 PRO 351 351 351 PRO PRO B . n 
B 2 352 LEU 352 352 352 LEU LEU B . n 
B 2 353 VAL 353 353 353 VAL VAL B . n 
B 2 354 VAL 354 354 354 VAL VAL B . n 
B 2 355 ARG 355 355 355 ARG ARG B . n 
B 2 356 LEU 356 356 356 LEU LEU B . n 
B 2 357 GLU 357 357 357 GLU GLU B . n 
B 2 358 GLY 358 358 358 GLY GLY B . n 
B 2 359 THR 359 359 359 THR THR B . n 
B 2 360 ASN 360 360 360 ASN ASN B . n 
B 2 361 VAL 361 361 361 VAL VAL B . n 
B 2 362 GLN 362 362 362 GLN GLN B . n 
B 2 363 GLU 363 363 363 GLU GLU B . n 
B 2 364 ALA 364 364 364 ALA ALA B . n 
B 2 365 GLN 365 365 365 GLN GLN B . n 
B 2 366 LYS 366 366 366 LYS LYS B . n 
B 2 367 ILE 367 367 367 ILE ILE B . n 
B 2 368 LEU 368 368 368 LEU LEU B . n 
B 2 369 ASN 369 369 369 ASN ASN B . n 
B 2 370 ASN 370 370 370 ASN ASN B . n 
B 2 371 SER 371 371 371 SER SER B . n 
B 2 372 GLY 372 372 372 GLY GLY B . n 
B 2 373 LEU 373 373 373 LEU LEU B . n 
B 2 374 PRO 374 374 374 PRO PRO B . n 
B 2 375 ILE 375 375 375 ILE ILE B . n 
B 2 376 THR 376 376 376 THR THR B . n 
B 2 377 SER 377 377 377 SER SER B . n 
B 2 378 ALA 378 378 378 ALA ALA B . n 
B 2 379 ILE 379 379 379 ILE ILE B . n 
B 2 380 ASP 380 380 380 ASP ASP B . n 
B 2 381 LEU 381 381 381 LEU LEU B . n 
B 2 382 GLU 382 382 382 GLU GLU B . n 
B 2 383 ASP 383 383 383 ASP ASP B . n 
B 2 384 ALA 384 384 384 ALA ALA B . n 
B 2 385 ALA 385 385 385 ALA ALA B . n 
B 2 386 LYS 386 386 386 LYS LYS B . n 
B 2 387 LYS 387 387 387 LYS LYS B . n 
B 2 388 ALA 388 388 388 ALA ALA B . n 
B 2 389 VAL 389 389 389 VAL VAL B . n 
B 2 390 ALA 390 390 390 ALA ALA B . n 
B 2 391 SER 391 391 391 SER SER B . n 
B 2 392 VAL 392 392 392 VAL VAL B . n 
B 2 393 ALA 393 393 393 ALA ALA B . n 
B 2 394 LYS 394 394 ?   ?   ?   B . n 
B 2 395 LYS 395 395 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 COA ? ? COA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 2OP ? ? 2OP ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
4 PO4 ? ? PO4 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 COA 1   2001 2001 COA COA A . 
D 4 PO4 1   2002 2002 PO4 PO4 A . 
E 5 2OP 1   401  401  2OP 2OP B . 
F 6 MG  1   402  402  MG  MG  B . 
G 7 HOH 1   2101 2101 HOH HOH A . 
G 7 HOH 2   2102 2102 HOH HOH A . 
G 7 HOH 3   2103 2103 HOH HOH A . 
G 7 HOH 4   2104 2104 HOH HOH A . 
G 7 HOH 5   2105 2105 HOH HOH A . 
G 7 HOH 6   2106 2106 HOH HOH A . 
G 7 HOH 7   2107 2107 HOH HOH A . 
G 7 HOH 8   2108 2108 HOH HOH A . 
G 7 HOH 9   2109 2109 HOH HOH A . 
G 7 HOH 10  2110 2110 HOH HOH A . 
G 7 HOH 11  2111 2111 HOH HOH A . 
G 7 HOH 12  2112 2112 HOH HOH A . 
G 7 HOH 13  2113 2113 HOH HOH A . 
G 7 HOH 14  2114 2114 HOH HOH A . 
G 7 HOH 15  2115 2115 HOH HOH A . 
G 7 HOH 16  2116 2116 HOH HOH A . 
G 7 HOH 17  2117 2117 HOH HOH A . 
G 7 HOH 18  2118 2118 HOH HOH A . 
G 7 HOH 19  2119 2119 HOH HOH A . 
G 7 HOH 20  2120 2120 HOH HOH A . 
G 7 HOH 21  2121 2121 HOH HOH A . 
G 7 HOH 22  2122 2122 HOH HOH A . 
G 7 HOH 23  2123 2123 HOH HOH A . 
G 7 HOH 24  2124 2124 HOH HOH A . 
G 7 HOH 25  2125 2125 HOH HOH A . 
G 7 HOH 26  2126 2126 HOH HOH A . 
G 7 HOH 27  2127 2127 HOH HOH A . 
G 7 HOH 28  2128 2128 HOH HOH A . 
G 7 HOH 29  2129 2129 HOH HOH A . 
G 7 HOH 30  2130 2130 HOH HOH A . 
G 7 HOH 31  2131 2131 HOH HOH A . 
G 7 HOH 32  2132 2132 HOH HOH A . 
G 7 HOH 33  2133 2133 HOH HOH A . 
G 7 HOH 34  2134 2134 HOH HOH A . 
G 7 HOH 35  2135 2135 HOH HOH A . 
G 7 HOH 36  2136 2136 HOH HOH A . 
G 7 HOH 37  2137 2137 HOH HOH A . 
G 7 HOH 38  2138 2138 HOH HOH A . 
G 7 HOH 39  2139 2139 HOH HOH A . 
G 7 HOH 40  2140 2140 HOH HOH A . 
G 7 HOH 41  2141 2141 HOH HOH A . 
G 7 HOH 42  2142 2142 HOH HOH A . 
G 7 HOH 43  2143 2143 HOH HOH A . 
G 7 HOH 44  2144 2144 HOH HOH A . 
G 7 HOH 45  2145 2145 HOH HOH A . 
G 7 HOH 46  2146 2146 HOH HOH A . 
G 7 HOH 47  2147 2147 HOH HOH A . 
G 7 HOH 48  2148 2148 HOH HOH A . 
G 7 HOH 49  2149 2149 HOH HOH A . 
G 7 HOH 50  2150 2150 HOH HOH A . 
G 7 HOH 51  2151 2151 HOH HOH A . 
G 7 HOH 52  2152 2152 HOH HOH A . 
G 7 HOH 53  2153 2153 HOH HOH A . 
G 7 HOH 54  2154 2154 HOH HOH A . 
G 7 HOH 55  2155 2155 HOH HOH A . 
G 7 HOH 56  2156 2156 HOH HOH A . 
G 7 HOH 57  2157 2157 HOH HOH A . 
G 7 HOH 58  2158 2158 HOH HOH A . 
G 7 HOH 59  2159 2159 HOH HOH A . 
G 7 HOH 60  2160 2160 HOH HOH A . 
G 7 HOH 61  2161 2161 HOH HOH A . 
G 7 HOH 62  2162 2162 HOH HOH A . 
G 7 HOH 63  2163 2163 HOH HOH A . 
G 7 HOH 64  2164 2164 HOH HOH A . 
G 7 HOH 65  2165 2165 HOH HOH A . 
G 7 HOH 66  2166 2166 HOH HOH A . 
G 7 HOH 67  2167 2167 HOH HOH A . 
G 7 HOH 68  2168 2168 HOH HOH A . 
G 7 HOH 69  2169 2169 HOH HOH A . 
G 7 HOH 70  2170 2170 HOH HOH A . 
G 7 HOH 71  2171 2171 HOH HOH A . 
G 7 HOH 72  2172 2172 HOH HOH A . 
G 7 HOH 73  2173 2173 HOH HOH A . 
G 7 HOH 74  2174 2174 HOH HOH A . 
G 7 HOH 75  2175 2175 HOH HOH A . 
G 7 HOH 76  2176 2176 HOH HOH A . 
G 7 HOH 77  2177 2177 HOH HOH A . 
G 7 HOH 78  2178 2178 HOH HOH A . 
G 7 HOH 79  2179 2179 HOH HOH A . 
G 7 HOH 80  2180 2180 HOH HOH A . 
G 7 HOH 81  2181 2181 HOH HOH A . 
G 7 HOH 82  2182 2182 HOH HOH A . 
G 7 HOH 83  2183 2183 HOH HOH A . 
G 7 HOH 84  2184 2184 HOH HOH A . 
G 7 HOH 85  2185 2185 HOH HOH A . 
G 7 HOH 86  2186 2186 HOH HOH A . 
G 7 HOH 87  2187 2187 HOH HOH A . 
G 7 HOH 88  2188 2188 HOH HOH A . 
G 7 HOH 89  2189 2189 HOH HOH A . 
G 7 HOH 90  2190 2190 HOH HOH A . 
G 7 HOH 91  2191 2191 HOH HOH A . 
G 7 HOH 92  2192 2192 HOH HOH A . 
G 7 HOH 93  2193 2193 HOH HOH A . 
G 7 HOH 94  2194 2194 HOH HOH A . 
G 7 HOH 95  2195 2195 HOH HOH A . 
G 7 HOH 96  2196 2196 HOH HOH A . 
G 7 HOH 97  2197 2197 HOH HOH A . 
G 7 HOH 98  2198 2198 HOH HOH A . 
G 7 HOH 99  2199 2199 HOH HOH A . 
G 7 HOH 100 2200 2200 HOH HOH A . 
G 7 HOH 101 2201 2201 HOH HOH A . 
G 7 HOH 102 2202 2202 HOH HOH A . 
G 7 HOH 103 2203 2203 HOH HOH A . 
G 7 HOH 104 2204 2204 HOH HOH A . 
G 7 HOH 105 2205 2205 HOH HOH A . 
G 7 HOH 106 2206 2206 HOH HOH A . 
G 7 HOH 107 2207 2207 HOH HOH A . 
G 7 HOH 108 2208 2208 HOH HOH A . 
G 7 HOH 109 2209 2209 HOH HOH A . 
G 7 HOH 110 2210 2210 HOH HOH A . 
G 7 HOH 111 2211 2211 HOH HOH A . 
G 7 HOH 112 2212 2212 HOH HOH A . 
G 7 HOH 113 2213 2213 HOH HOH A . 
G 7 HOH 114 2214 2214 HOH HOH A . 
G 7 HOH 115 2215 2215 HOH HOH A . 
G 7 HOH 116 2216 2216 HOH HOH A . 
G 7 HOH 117 2217 2217 HOH HOH A . 
H 7 HOH 1   501  501  HOH HOH B . 
H 7 HOH 2   502  502  HOH HOH B . 
H 7 HOH 3   503  503  HOH HOH B . 
H 7 HOH 4   504  504  HOH HOH B . 
H 7 HOH 5   505  505  HOH HOH B . 
H 7 HOH 6   506  506  HOH HOH B . 
H 7 HOH 7   507  507  HOH HOH B . 
H 7 HOH 8   508  508  HOH HOH B . 
H 7 HOH 9   509  509  HOH HOH B . 
H 7 HOH 10  510  510  HOH HOH B . 
H 7 HOH 11  511  511  HOH HOH B . 
H 7 HOH 12  512  512  HOH HOH B . 
H 7 HOH 13  513  513  HOH HOH B . 
H 7 HOH 14  514  514  HOH HOH B . 
H 7 HOH 15  515  515  HOH HOH B . 
H 7 HOH 16  516  516  HOH HOH B . 
H 7 HOH 17  517  517  HOH HOH B . 
H 7 HOH 18  518  518  HOH HOH B . 
H 7 HOH 19  519  519  HOH HOH B . 
H 7 HOH 20  520  520  HOH HOH B . 
H 7 HOH 21  521  521  HOH HOH B . 
H 7 HOH 22  522  522  HOH HOH B . 
H 7 HOH 23  523  523  HOH HOH B . 
H 7 HOH 24  524  524  HOH HOH B . 
H 7 HOH 25  525  525  HOH HOH B . 
H 7 HOH 26  526  526  HOH HOH B . 
H 7 HOH 27  527  527  HOH HOH B . 
H 7 HOH 28  528  528  HOH HOH B . 
H 7 HOH 29  529  529  HOH HOH B . 
H 7 HOH 30  530  530  HOH HOH B . 
H 7 HOH 31  531  531  HOH HOH B . 
H 7 HOH 32  532  532  HOH HOH B . 
H 7 HOH 33  533  533  HOH HOH B . 
H 7 HOH 34  534  534  HOH HOH B . 
H 7 HOH 35  535  535  HOH HOH B . 
H 7 HOH 36  536  536  HOH HOH B . 
H 7 HOH 37  537  537  HOH HOH B . 
H 7 HOH 38  538  538  HOH HOH B . 
H 7 HOH 39  539  539  HOH HOH B . 
H 7 HOH 40  540  540  HOH HOH B . 
H 7 HOH 41  541  541  HOH HOH B . 
H 7 HOH 42  542  542  HOH HOH B . 
H 7 HOH 43  543  543  HOH HOH B . 
H 7 HOH 44  544  544  HOH HOH B . 
H 7 HOH 45  545  545  HOH HOH B . 
H 7 HOH 46  546  546  HOH HOH B . 
H 7 HOH 47  547  547  HOH HOH B . 
H 7 HOH 48  548  548  HOH HOH B . 
H 7 HOH 49  549  549  HOH HOH B . 
H 7 HOH 50  550  550  HOH HOH B . 
H 7 HOH 51  551  551  HOH HOH B . 
H 7 HOH 52  552  552  HOH HOH B . 
H 7 HOH 53  553  553  HOH HOH B . 
H 7 HOH 54  554  554  HOH HOH B . 
H 7 HOH 55  555  555  HOH HOH B . 
H 7 HOH 56  556  556  HOH HOH B . 
H 7 HOH 57  557  557  HOH HOH B . 
H 7 HOH 58  558  558  HOH HOH B . 
H 7 HOH 59  559  559  HOH HOH B . 
H 7 HOH 60  560  560  HOH HOH B . 
H 7 HOH 61  561  561  HOH HOH B . 
H 7 HOH 62  562  562  HOH HOH B . 
H 7 HOH 63  563  563  HOH HOH B . 
H 7 HOH 64  564  564  HOH HOH B . 
H 7 HOH 65  565  565  HOH HOH B . 
H 7 HOH 66  566  566  HOH HOH B . 
H 7 HOH 67  567  567  HOH HOH B . 
H 7 HOH 68  568  568  HOH HOH B . 
H 7 HOH 69  569  569  HOH HOH B . 
H 7 HOH 70  570  570  HOH HOH B . 
H 7 HOH 71  571  571  HOH HOH B . 
H 7 HOH 72  572  572  HOH HOH B . 
H 7 HOH 73  573  573  HOH HOH B . 
H 7 HOH 74  574  574  HOH HOH B . 
H 7 HOH 75  575  575  HOH HOH B . 
H 7 HOH 76  576  576  HOH HOH B . 
H 7 HOH 77  577  577  HOH HOH B . 
H 7 HOH 78  578  578  HOH HOH B . 
H 7 HOH 79  579  579  HOH HOH B . 
H 7 HOH 80  580  580  HOH HOH B . 
H 7 HOH 81  581  581  HOH HOH B . 
H 7 HOH 82  582  582  HOH HOH B . 
H 7 HOH 83  583  583  HOH HOH B . 
H 7 HOH 84  584  584  HOH HOH B . 
H 7 HOH 85  585  585  HOH HOH B . 
H 7 HOH 86  586  586  HOH HOH B . 
H 7 HOH 87  587  587  HOH HOH B . 
H 7 HOH 88  588  588  HOH HOH B . 
H 7 HOH 89  589  589  HOH HOH B . 
H 7 HOH 90  590  590  HOH HOH B . 
H 7 HOH 91  591  591  HOH HOH B . 
H 7 HOH 92  592  592  HOH HOH B . 
H 7 HOH 93  593  593  HOH HOH B . 
H 7 HOH 94  594  594  HOH HOH B . 
H 7 HOH 95  595  595  HOH HOH B . 
H 7 HOH 96  596  596  HOH HOH B . 
H 7 HOH 97  597  597  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 8   ? CD  ? A GLN 8   CD  
2  1 Y 1 A GLN 8   ? OE1 ? A GLN 8   OE1 
3  1 Y 1 A GLN 8   ? NE2 ? A GLN 8   NE2 
4  1 Y 1 A LYS 14  ? CD  ? A LYS 14  CD  
5  1 Y 1 A LYS 14  ? CE  ? A LYS 14  CE  
6  1 Y 1 A LYS 14  ? NZ  ? A LYS 14  NZ  
7  1 Y 1 A LYS 26  ? CE  ? A LYS 26  CE  
8  1 Y 1 A LYS 26  ? NZ  ? A LYS 26  NZ  
9  1 Y 1 A HIS 149 ? CG  ? A HIS 149 CG  
10 1 Y 1 A HIS 149 ? ND1 ? A HIS 149 ND1 
11 1 Y 1 A HIS 149 ? CD2 ? A HIS 149 CD2 
12 1 Y 1 A HIS 149 ? CE1 ? A HIS 149 CE1 
13 1 Y 1 A HIS 149 ? NE2 ? A HIS 149 NE2 
14 1 Y 1 A LYS 231 ? NZ  ? A LYS 231 NZ  
15 1 Y 1 A LYS 268 ? CG  ? A LYS 268 CG  
16 1 Y 1 A LYS 268 ? CD  ? A LYS 268 CD  
17 1 Y 1 A LYS 268 ? CE  ? A LYS 268 CE  
18 1 Y 1 A LYS 268 ? NZ  ? A LYS 268 NZ  
19 1 Y 1 A LYS 302 ? CE  ? A LYS 302 CE  
20 1 Y 1 A LYS 302 ? NZ  ? A LYS 302 NZ  
21 1 Y 1 B ARG 18  ? NE  ? B ARG 18  NE  
22 1 Y 1 B ARG 18  ? CZ  ? B ARG 18  CZ  
23 1 Y 1 B ARG 18  ? NH1 ? B ARG 18  NH1 
24 1 Y 1 B ARG 18  ? NH2 ? B ARG 18  NH2 
25 1 Y 1 B LYS 64  ? CE  ? B LYS 64  CE  
26 1 Y 1 B LYS 64  ? NZ  ? B LYS 64  NZ  
27 1 Y 1 B LYS 81  ? CG  ? B LYS 81  CG  
28 1 Y 1 B LYS 81  ? CD  ? B LYS 81  CD  
29 1 Y 1 B LYS 81  ? CE  ? B LYS 81  CE  
30 1 Y 1 B LYS 81  ? NZ  ? B LYS 81  NZ  
31 1 Y 1 B LYS 91  ? CD  ? B LYS 91  CD  
32 1 Y 1 B LYS 91  ? CE  ? B LYS 91  CE  
33 1 Y 1 B LYS 91  ? NZ  ? B LYS 91  NZ  
34 1 Y 1 B LYS 95  ? CG  ? B LYS 95  CG  
35 1 Y 1 B LYS 95  ? CD  ? B LYS 95  CD  
36 1 Y 1 B LYS 95  ? CE  ? B LYS 95  CE  
37 1 Y 1 B LYS 95  ? NZ  ? B LYS 95  NZ  
38 1 Y 1 B LYS 99  ? NZ  ? B LYS 99  NZ  
39 1 Y 1 B GLU 141 ? CD  ? B GLU 141 CD  
40 1 Y 1 B GLU 141 ? OE1 ? B GLU 141 OE1 
41 1 Y 1 B GLU 141 ? OE2 ? B GLU 141 OE2 
42 1 Y 1 B LYS 163 ? CD  ? B LYS 163 CD  
43 1 Y 1 B LYS 163 ? CE  ? B LYS 163 CE  
44 1 Y 1 B LYS 163 ? NZ  ? B LYS 163 NZ  
45 1 Y 1 B LYS 222 ? CE  ? B LYS 222 CE  
46 1 Y 1 B LYS 222 ? NZ  ? B LYS 222 NZ  
47 1 Y 1 B LYS 234 ? CD  ? B LYS 234 CD  
48 1 Y 1 B LYS 234 ? CE  ? B LYS 234 CE  
49 1 Y 1 B LYS 234 ? NZ  ? B LYS 234 NZ  
50 1 Y 1 B LYS 289 ? NZ  ? B LYS 289 NZ  
51 1 Y 1 B LYS 301 ? CE  ? B LYS 301 CE  
52 1 Y 1 B LYS 301 ? NZ  ? B LYS 301 NZ  
53 1 Y 1 B LYS 317 ? CD  ? B LYS 317 CD  
54 1 Y 1 B LYS 317 ? CE  ? B LYS 317 CE  
55 1 Y 1 B LYS 317 ? NZ  ? B LYS 317 NZ  
56 1 Y 1 B LEU 346 ? CG  ? B LEU 346 CG  
57 1 Y 1 B LEU 346 ? CD1 ? B LEU 346 CD1 
58 1 Y 1 B LEU 346 ? CD2 ? B LEU 346 CD2 
59 1 Y 1 B GLN 362 ? CD  ? B GLN 362 CD  
60 1 Y 1 B GLN 362 ? OE1 ? B GLN 362 OE1 
61 1 Y 1 B GLN 362 ? NE2 ? B GLN 362 NE2 
62 1 Y 1 B LYS 366 ? CE  ? B LYS 366 CE  
63 1 Y 1 B LYS 366 ? NZ  ? B LYS 366 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.7.2     1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.14_3260 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27      3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? autoPROC    ? ? ? .         4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .         5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   92.130 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z03 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     54.120 
_cell.length_a_esd                 ? 
_cell.length_b                     134.370 
_cell.length_b_esd                 ? 
_cell.length_c                     57.830 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8Z03 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   8Z03 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.73 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.00 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Ammonium sulfate, 0.1 M TRIS pH=7.5, 20% w/v PEG MME 5000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-12-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97915 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97915 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Z03 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.990 
_reflns.d_resolution_low                               43.810 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     55815 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.000 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.100 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.600 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           432 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.201 
_reflns.pdbx_Rpim_I_all                                0.087 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       286049 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.986 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.180 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.990 2.040  ? ? 21847 ? ? ? 4109 ? ? ? ? ? ? ? ? ? ? ? 5.300 ? ? 2.200  0.965 0.410 ? 1 1 0.701 ? ? 98.700 ? 0.872 ? ? ? ? ? ? ? 
? ? 
8.900 43.810 ? ? 3276  ? ? ? 630  ? ? ? ? ? ? ? ? ? ? ? 5.200 ? ? 14.600 0.101 0.044 ? 2 1 0.984 ? ? 97.100 ? 0.091 ? ? ? ? ? ? ? 
? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                60.550 
_refine.B_iso_mean                               23.8282 
_refine.B_iso_min                                10.460 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8Z03 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.9900 
_refine.ls_d_res_low                             42.1290 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     55773 
_refine.ls_number_reflns_R_free                  2806 
_refine.ls_number_reflns_R_work                  52967 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.7900 
_refine.ls_percent_reflns_R_free                 5.0300 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2090 
_refine.ls_R_factor_R_free                       0.2437 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2072 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.390 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5cae 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.0500 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2600 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.9900 
_refine_hist.d_res_low                        42.1290 
_refine_hist.number_atoms_solvent             214 
_refine_hist.number_atoms_total               5493 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       704 
_refine_hist.pdbx_B_iso_mean_ligand           20.25 
_refine_hist.pdbx_B_iso_mean_solvent          24.89 
_refine_hist.pdbx_number_atoms_protein        5219 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         60 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.9900 2.0243  . . 138 2601 98.0000  . . . 0.0000 0.2680 . . . . . . . . . . . 0.3381 
'X-RAY DIFFRACTION' 2.0243 2.0611  . . 149 2665 99.0000  . . . 0.0000 0.2530 . . . . . . . . . . . 0.2713 
'X-RAY DIFFRACTION' 2.0611 2.1008  . . 171 2588 98.0000  . . . 0.0000 0.2367 . . . . . . . . . . . 0.2916 
'X-RAY DIFFRACTION' 2.1008 2.1437  . . 144 2642 99.0000  . . . 0.0000 0.2315 . . . . . . . . . . . 0.3308 
'X-RAY DIFFRACTION' 2.1437 2.1903  . . 144 2610 98.0000  . . . 0.0000 0.2185 . . . . . . . . . . . 0.3019 
'X-RAY DIFFRACTION' 2.1903 2.2412  . . 164 2661 99.0000  . . . 0.0000 0.2154 . . . . . . . . . . . 0.2495 
'X-RAY DIFFRACTION' 2.2412 2.2973  . . 141 2621 99.0000  . . . 0.0000 0.2132 . . . . . . . . . . . 0.2636 
'X-RAY DIFFRACTION' 2.2973 2.3594  . . 162 2641 98.0000  . . . 0.0000 0.2164 . . . . . . . . . . . 0.2730 
'X-RAY DIFFRACTION' 2.3594 2.4288  . . 143 2638 100.0000 . . . 0.0000 0.2129 . . . . . . . . . . . 0.2499 
'X-RAY DIFFRACTION' 2.4288 2.5072  . . 104 2685 99.0000  . . . 0.0000 0.2132 . . . . . . . . . . . 0.2857 
'X-RAY DIFFRACTION' 2.5072 2.5968  . . 112 2673 99.0000  . . . 0.0000 0.2146 . . . . . . . . . . . 0.2662 
'X-RAY DIFFRACTION' 2.5968 2.7007  . . 131 2686 99.0000  . . . 0.0000 0.2176 . . . . . . . . . . . 0.2801 
'X-RAY DIFFRACTION' 2.7007 2.8236  . . 126 2660 99.0000  . . . 0.0000 0.2175 . . . . . . . . . . . 0.2416 
'X-RAY DIFFRACTION' 2.8236 2.9724  . . 180 2613 99.0000  . . . 0.0000 0.2202 . . . . . . . . . . . 0.2501 
'X-RAY DIFFRACTION' 2.9724 3.1586  . . 142 2648 99.0000  . . . 0.0000 0.2239 . . . . . . . . . . . 0.2290 
'X-RAY DIFFRACTION' 3.1586 3.4024  . . 113 2702 99.0000  . . . 0.0000 0.2032 . . . . . . . . . . . 0.2552 
'X-RAY DIFFRACTION' 3.4024 3.7446  . . 129 2632 99.0000  . . . 0.0000 0.1956 . . . . . . . . . . . 0.2500 
'X-RAY DIFFRACTION' 3.7446 4.2860  . . 101 2696 99.0000  . . . 0.0000 0.1771 . . . . . . . . . . . 0.2108 
'X-RAY DIFFRACTION' 4.2860 5.3981  . . 170 2643 98.0000  . . . 0.0000 0.1806 . . . . . . . . . . . 0.1809 
'X-RAY DIFFRACTION' 5.3981 42.1290 . . 142 2662 98.0000  . . . 0.0000 0.2004 . . . . . . . . . . . 0.2078 
# 
_struct.entry_id                     8Z03 
_struct.title                        'Lactate bound to human GTP-specific succinyl-CoA synthetase' 
_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        8Z03 
_struct_keywords.text            'GTP-specific succinyl-CoA synthetase, GTPSCS, lactyl-CoA ligase, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
H N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SUCA_HUMAN  P53597 ? 1 
;SYTASRQHLYVDKNTKIICQGFTGKQGTFHSQQALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYVP
PPFAAAAINEAIEAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGECKIGIMPGHIHKKGRIGIVSR
SGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCLEIFLNDSATEGIILIGEIGGNAEENAAEFLKQHNSGPNSKP
VVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKEKISALQSAGVVVSMSPAQLGTTIYKEFEKRKML
;
42 
2 UNP SUCB2_HUMAN Q96I99 ? 2 
;NLQEYQSKKLMSDNGVRVQRFFVADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAK
QMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIFEG
IKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDD
KSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAI
LVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLEDAAKKAVASVAKK
;
39 
# 
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 8Z03 A 2 ? 306 ? P53597 42 ? 346 ? 2 306 
2 2 8Z03 B 2 ? 395 ? Q96I99 39 ? 432 ? 2 395 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8Z03 MET A 1   ? UNP P53597 ? ? 'initiating methionine' 1   1  
1 8Z03 GLU A 307 ? UNP P53597 ? ? 'expression tag'        307 2  
1 8Z03 ASN A 308 ? UNP P53597 ? ? 'expression tag'        308 3  
1 8Z03 LEU A 309 ? UNP P53597 ? ? 'expression tag'        309 4  
1 8Z03 TYR A 310 ? UNP P53597 ? ? 'expression tag'        310 5  
1 8Z03 PHE A 311 ? UNP P53597 ? ? 'expression tag'        311 6  
1 8Z03 GLN A 312 ? UNP P53597 ? ? 'expression tag'        312 7  
1 8Z03 GLY A 313 ? UNP P53597 ? ? 'expression tag'        313 8  
1 8Z03 HIS A 314 ? UNP P53597 ? ? 'expression tag'        314 9  
1 8Z03 HIS A 315 ? UNP P53597 ? ? 'expression tag'        315 10 
1 8Z03 HIS A 316 ? UNP P53597 ? ? 'expression tag'        316 11 
1 8Z03 HIS A 317 ? UNP P53597 ? ? 'expression tag'        317 12 
1 8Z03 HIS A 318 ? UNP P53597 ? ? 'expression tag'        318 13 
1 8Z03 HIS A 319 ? UNP P53597 ? ? 'expression tag'        319 14 
1 8Z03 HIS A 320 ? UNP P53597 ? ? 'expression tag'        320 15 
1 8Z03 HIS A 321 ? UNP P53597 ? ? 'expression tag'        321 16 
2 8Z03 MET B 1   ? UNP Q96I99 ? ? 'initiating methionine' 1   17 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6040  ? 
1 MORE         -43   ? 
1 'SSA (A^2)'  27400 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 2   ? TYR A 11  ? SER A 2   TYR A 11  5 ? 10 
HELX_P HELX_P2  AA2 GLY A 25  ? TYR A 38  ? GLY A 25  TYR A 38  1 ? 14 
HELX_P HELX_P3  AA3 THR A 63  ? GLY A 72  ? THR A 63  GLY A 72  1 ? 10 
HELX_P HELX_P4  AA4 PRO A 81  ? ALA A 95  ? PRO A 81  ALA A 95  1 ? 15 
HELX_P HELX_P5  AA5 PRO A 108 ? ARG A 121 ? PRO A 108 ARG A 121 1 ? 14 
HELX_P HELX_P6  AA6 SER A 162 ? VAL A 176 ? SER A 162 VAL A 176 1 ? 15 
HELX_P HELX_P7  AA7 ASP A 195 ? ASN A 205 ? ASP A 195 ASN A 205 1 ? 11 
HELX_P HELX_P8  AA8 ASN A 221 ? ASN A 234 ? ASN A 221 ASN A 234 1 ? 14 
HELX_P HELX_P9  AA9 GLY A 270 ? ALA A 281 ? GLY A 270 ALA A 281 1 ? 12 
HELX_P HELX_P10 AB1 SER A 288 ? ALA A 290 ? SER A 288 ALA A 290 5 ? 3  
HELX_P HELX_P11 AB2 GLN A 291 ? PHE A 311 ? GLN A 291 PHE A 311 1 ? 21 
HELX_P HELX_P12 AB3 GLN B 4   ? ASP B 14  ? GLN B 4   ASP B 14  1 ? 11 
HELX_P HELX_P13 AB4 THR B 27  ? ASN B 39  ? THR B 27  ASN B 39  1 ? 13 
HELX_P HELX_P14 AB5 ASP B 72  ? GLN B 82  ? ASP B 72  GLN B 82  1 ? 11 
HELX_P HELX_P15 AB6 ARG B 123 ? ASN B 126 ? ARG B 123 ASN B 126 5 ? 4  
HELX_P HELX_P16 AB7 ASP B 139 ? ASN B 147 ? ASP B 139 ASN B 147 1 ? 9  
HELX_P HELX_P17 AB8 PRO B 148 ? ILE B 151 ? PRO B 148 ILE B 151 5 ? 4  
HELX_P HELX_P18 AB9 LYS B 163 ? LEU B 174 ? LYS B 163 LEU B 174 1 ? 12 
HELX_P HELX_P19 AC1 GLY B 178 ? ILE B 198 ? GLY B 178 ILE B 198 1 ? 21 
HELX_P HELX_P20 AC2 ASP B 227 ? ARG B 232 ? ASP B 227 ARG B 232 5 ? 6  
HELX_P HELX_P21 AC3 GLN B 233 ? MET B 239 ? GLN B 233 MET B 239 1 ? 7  
HELX_P HELX_P22 AC4 GLU B 246 ? LYS B 254 ? GLU B 246 LYS B 254 1 ? 9  
HELX_P HELX_P23 AC5 GLY B 272 ? ASN B 286 ? GLY B 272 ASN B 286 1 ? 15 
HELX_P HELX_P24 AC6 LYS B 301 ? ALA B 314 ? LYS B 301 ALA B 314 1 ? 14 
HELX_P HELX_P25 AC7 ASN B 331 ? ARG B 344 ? ASN B 331 ARG B 344 1 ? 14 
HELX_P HELX_P26 AC8 ASN B 360 ? GLY B 372 ? ASN B 360 GLY B 372 1 ? 13 
HELX_P HELX_P27 AC9 ASP B 380 ? VAL B 392 ? ASP B 380 VAL B 392 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? E 2OP . O   ? ? ? 1_555 F MG . MG ? ? B 2OP 401 B MG 402 1_555 ? ? ? ? ? ? ? 1.973 ? ? 
metalc2 metalc ? ? E 2OP . OXT ? ? ? 1_555 F MG . MG ? ? B 2OP 401 B MG 402 1_555 ? ? ? ? ? ? ? 2.974 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   E 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   2OP 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    2OP 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     401 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   F 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    MG 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     402 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   OXT 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   E 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   2OP 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    2OP 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     401 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 47.7 
_pdbx_struct_conn_angle.value_esd             ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 129 A . ? GLY 129 A PRO 130 A ? PRO 130 A 1 7.42 
2 ASN 206 B . ? ASN 206 B PRO 207 B ? PRO 207 B 1 4.04 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
AA5 ? 5 ? 
AA6 ? 5 ? 
AA7 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? 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 THR A 54  ? HIS A 55  ? THR A 54  HIS A 55  
AA1 2 LEU A 58  ? PHE A 61  ? LEU A 58  PHE A 61  
AA1 3 LEU A 42  ? THR A 46  ? LEU A 42  THR A 46  
AA1 4 ILE A 18  ? GLN A 21  ? ILE A 18  GLN A 21  
AA1 5 ALA A 75  ? ILE A 78  ? ALA A 75  ILE A 78  
AA1 6 LEU A 99  ? CYS A 102 ? LEU A 99  CYS A 102 
AA1 7 ARG A 126 ? ILE A 128 ? ARG A 126 ILE A 128 
AA2 1 CYS A 141 ? GLY A 144 ? CYS A 141 GLY A 144 
AA2 2 GLY A 134 ? ASN A 137 ? GLY A 134 ASN A 137 
AA2 3 GLN A 180 ? GLY A 185 ? GLN A 180 GLY A 185 
AA2 4 LYS A 153 ? SER A 160 ? LYS A 153 SER A 160 
AA2 5 GLY A 211 ? GLU A 217 ? GLY A 211 GLU A 217 
AA2 6 VAL A 242 ? ALA A 247 ? VAL A 242 ALA A 247 
AA2 7 VAL A 284 ? VAL A 285 ? VAL A 284 VAL A 285 
AA3 1 PHE B 22  ? ALA B 25  ? PHE B 22  ALA B 25  
AA3 2 VAL B 103 ? GLU B 107 ? VAL B 103 GLU B 107 
AA3 3 ILE B 43  ? ALA B 47  ? ILE B 43  ALA B 47  
AA3 4 VAL B 67  ? THR B 70  ? VAL B 67  THR B 70  
AA4 1 VAL B 58  ? PHE B 59  ? VAL B 58  PHE B 59  
AA4 2 ASN B 87  ? ALA B 89  ? ASN B 87  ALA B 89  
AA4 3 VAL B 98  ? LYS B 99  ? VAL B 98  LYS B 99  
AA5 1 PHE B 152 ? GLN B 155 ? PHE B 152 GLN B 155 
AA5 2 GLY B 127 ? SER B 133 ? GLY B 127 SER B 133 
AA5 3 ARG B 113 ? ASP B 122 ? ARG B 113 ASP B 122 
AA5 4 ALA B 200 ? GLU B 210 ? ALA B 200 GLU B 210 
AA5 5 VAL B 216 ? CYS B 218 ? VAL B 216 CYS B 218 
AA6 1 PHE B 152 ? GLN B 155 ? PHE B 152 GLN B 155 
AA6 2 GLY B 127 ? SER B 133 ? GLY B 127 SER B 133 
AA6 3 ARG B 113 ? ASP B 122 ? ARG B 113 ASP B 122 
AA6 4 ALA B 200 ? GLU B 210 ? ALA B 200 GLU B 210 
AA6 5 ALA B 221 ? PHE B 225 ? ALA B 221 PHE B 225 
AA7 1 LYS B 258 ? GLY B 261 ? LYS B 258 GLY B 261 
AA7 2 ASN B 292 ? LEU B 296 ? ASN B 292 LEU B 296 
AA7 3 ILE B 266 ? ASN B 271 ? ILE B 266 ASN B 271 
AA7 4 ALA B 320 ? GLY B 327 ? ALA B 320 GLY B 327 
AA7 5 LEU B 352 ? GLY B 358 ? LEU B 352 GLY B 358 
AA7 6 ILE B 375 ? SER B 377 ? ILE B 375 SER B 377 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N HIS A 55  ? N HIS A 55  O LEU A 58  ? O LEU A 58  
AA1 2 3 O PHE A 61  ? O PHE A 61  N GLY A 45  ? N GLY A 45  
AA1 3 4 O VAL A 43  ? O VAL A 43  N ILE A 18  ? N ILE A 18  
AA1 4 5 N GLN A 21  ? N GLN A 21  O VAL A 77  ? O VAL A 77  
AA1 5 6 N SER A 76  ? N SER A 76  O VAL A 101 ? O VAL A 101 
AA1 6 7 N VAL A 100 ? N VAL A 100 O ARG A 126 ? O ARG A 126 
AA2 1 2 O CYS A 141 ? O CYS A 141 N ASN A 137 ? N ASN A 137 
AA2 2 3 N GLY A 134 ? N GLY A 134 O GLY A 185 ? O GLY A 185 
AA2 3 4 O VAL A 184 ? O VAL A 184 N ILE A 158 ? N ILE A 158 
AA2 4 5 N VAL A 159 ? N VAL A 159 O ILE A 215 ? O ILE A 215 
AA2 5 6 N ILE A 212 ? N ILE A 212 O VAL A 243 ? O VAL A 243 
AA2 6 7 N VAL A 242 ? N VAL A 242 O VAL A 284 ? O VAL A 284 
AA3 1 2 N PHE B 23  ? N PHE B 23  O VAL B 105 ? O VAL B 105 
AA3 2 3 O MET B 104 ? O MET B 104 N LYS B 46  ? N LYS B 46  
AA3 3 4 N LEU B 45  ? N LEU B 45  O HIS B 68  ? O HIS B 68  
AA4 1 2 N VAL B 58  ? N VAL B 58  O ALA B 89  ? O ALA B 89  
AA4 2 3 N LEU B 88  ? N LEU B 88  O VAL B 98  ? O VAL B 98  
AA5 1 2 O PHE B 152 ? O PHE B 152 N GLY B 132 ? N GLY B 132 
AA5 2 3 O VAL B 131 ? O VAL B 131 N ALA B 118 ? N ALA B 118 
AA5 3 4 N LEU B 117 ? N LEU B 117 O VAL B 205 ? O VAL B 205 
AA5 4 5 N GLY B 209 ? N GLY B 209 O VAL B 217 ? O VAL B 217 
AA6 1 2 O PHE B 152 ? O PHE B 152 N GLY B 132 ? N GLY B 132 
AA6 2 3 O VAL B 131 ? O VAL B 131 N ALA B 118 ? N ALA B 118 
AA6 3 4 N LEU B 117 ? N LEU B 117 O VAL B 205 ? O VAL B 205 
AA6 4 5 N GLU B 204 ? N GLU B 204 O LYS B 222 ? O LYS B 222 
AA7 1 2 N ILE B 260 ? N ILE B 260 O PHE B 293 ? O PHE B 293 
AA7 2 3 O LEU B 296 ? O LEU B 296 N VAL B 270 ? N VAL B 270 
AA7 3 4 N ALA B 267 ? N ALA B 267 O ALA B 320 ? O ALA B 320 
AA7 4 5 N VAL B 323 ? N VAL B 323 O VAL B 353 ? O VAL B 353 
AA7 5 6 N LEU B 352 ? N LEU B 352 O THR B 376 ? O THR B 376 
# 
_pdbx_entry_details.entry_id                   8Z03 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 123 ? ? -144.45 11.45 
2 1 ASP B 263 ? ? -103.35 65.52 
# 
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   ? A MET 1   
2  1 Y 1 A GLY 313 ? A GLY 313 
3  1 Y 1 A HIS 314 ? A HIS 314 
4  1 Y 1 A HIS 315 ? A HIS 315 
5  1 Y 1 A HIS 316 ? A HIS 316 
6  1 Y 1 A HIS 317 ? A HIS 317 
7  1 Y 1 A HIS 318 ? A HIS 318 
8  1 Y 1 A HIS 319 ? A HIS 319 
9  1 Y 1 A HIS 320 ? A HIS 320 
10 1 Y 1 A HIS 321 ? A HIS 321 
11 1 Y 1 B LYS 394 ? B LYS 394 
12 1 Y 1 B LYS 395 ? B LYS 395 
# 
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 
2OP C    C  N N 1   
2OP O    O  N N 2   
2OP CB   C  N N 3   
2OP OHN  O  N N 4   
2OP CA   C  N S 5   
2OP OXT  O  N N 6   
2OP HB1  H  N N 7   
2OP HB2  H  N N 8   
2OP HB3  H  N N 9   
2OP H    H  N N 10  
2OP HA   H  N N 11  
2OP HXT  H  N N 12  
ALA N    N  N N 13  
ALA CA   C  N S 14  
ALA C    C  N N 15  
ALA O    O  N N 16  
ALA CB   C  N N 17  
ALA OXT  O  N N 18  
ALA H    H  N N 19  
ALA H2   H  N N 20  
ALA HA   H  N N 21  
ALA HB1  H  N N 22  
ALA HB2  H  N N 23  
ALA HB3  H  N N 24  
ALA HXT  H  N N 25  
ARG N    N  N N 26  
ARG CA   C  N S 27  
ARG C    C  N N 28  
ARG O    O  N N 29  
ARG CB   C  N N 30  
ARG CG   C  N N 31  
ARG CD   C  N N 32  
ARG NE   N  N N 33  
ARG CZ   C  N N 34  
ARG NH1  N  N N 35  
ARG NH2  N  N N 36  
ARG OXT  O  N N 37  
ARG H    H  N N 38  
ARG H2   H  N N 39  
ARG HA   H  N N 40  
ARG HB2  H  N N 41  
ARG HB3  H  N N 42  
ARG HG2  H  N N 43  
ARG HG3  H  N N 44  
ARG HD2  H  N N 45  
ARG HD3  H  N N 46  
ARG HE   H  N N 47  
ARG HH11 H  N N 48  
ARG HH12 H  N N 49  
ARG HH21 H  N N 50  
ARG HH22 H  N N 51  
ARG HXT  H  N N 52  
ASN N    N  N N 53  
ASN CA   C  N S 54  
ASN C    C  N N 55  
ASN O    O  N N 56  
ASN CB   C  N N 57  
ASN CG   C  N N 58  
ASN OD1  O  N N 59  
ASN ND2  N  N N 60  
ASN OXT  O  N N 61  
ASN H    H  N N 62  
ASN H2   H  N N 63  
ASN HA   H  N N 64  
ASN HB2  H  N N 65  
ASN HB3  H  N N 66  
ASN HD21 H  N N 67  
ASN HD22 H  N N 68  
ASN HXT  H  N N 69  
ASP N    N  N N 70  
ASP CA   C  N S 71  
ASP C    C  N N 72  
ASP O    O  N N 73  
ASP CB   C  N N 74  
ASP CG   C  N N 75  
ASP OD1  O  N N 76  
ASP OD2  O  N N 77  
ASP OXT  O  N N 78  
ASP H    H  N N 79  
ASP H2   H  N N 80  
ASP HA   H  N N 81  
ASP HB2  H  N N 82  
ASP HB3  H  N N 83  
ASP HD2  H  N N 84  
ASP HXT  H  N N 85  
COA N1A  N  Y N 86  
COA C2A  C  Y N 87  
COA N3A  N  Y N 88  
COA C4A  C  Y N 89  
COA C5A  C  Y N 90  
COA C6A  C  Y N 91  
COA N6A  N  N N 92  
COA N7A  N  Y N 93  
COA C8A  C  Y N 94  
COA N9A  N  Y N 95  
COA C1B  C  N R 96  
COA C2B  C  N R 97  
COA O2B  O  N N 98  
COA C3B  C  N S 99  
COA O3B  O  N N 100 
COA P3B  P  N N 101 
COA O7A  O  N N 102 
COA O8A  O  N N 103 
COA O9A  O  N N 104 
COA C4B  C  N R 105 
COA O4B  O  N N 106 
COA C5B  C  N N 107 
COA O5B  O  N N 108 
COA P1A  P  N S 109 
COA O1A  O  N N 110 
COA O2A  O  N N 111 
COA O3A  O  N N 112 
COA P2A  P  N S 113 
COA O4A  O  N N 114 
COA O5A  O  N N 115 
COA O6A  O  N N 116 
COA CBP  C  N N 117 
COA CCP  C  N N 118 
COA CDP  C  N N 119 
COA CEP  C  N N 120 
COA CAP  C  N R 121 
COA OAP  O  N N 122 
COA C9P  C  N N 123 
COA O9P  O  N N 124 
COA N8P  N  N N 125 
COA C7P  C  N N 126 
COA C6P  C  N N 127 
COA C5P  C  N N 128 
COA O5P  O  N N 129 
COA N4P  N  N N 130 
COA C3P  C  N N 131 
COA C2P  C  N N 132 
COA S1P  S  N N 133 
COA H2A  H  N N 134 
COA H61A H  N N 135 
COA H62A H  N N 136 
COA H8A  H  N N 137 
COA H1B  H  N N 138 
COA H2B  H  N N 139 
COA HO2A H  N N 140 
COA H3B  H  N N 141 
COA HOA8 H  N N 142 
COA HOA9 H  N N 143 
COA H4B  H  N N 144 
COA H51A H  N N 145 
COA H52A H  N N 146 
COA HOA2 H  N N 147 
COA HOA5 H  N N 148 
COA H121 H  N N 149 
COA H122 H  N N 150 
COA H131 H  N N 151 
COA H132 H  N N 152 
COA H133 H  N N 153 
COA H141 H  N N 154 
COA H142 H  N N 155 
COA H143 H  N N 156 
COA H10  H  N N 157 
COA HO1  H  N N 158 
COA HN8  H  N N 159 
COA H71  H  N N 160 
COA H72  H  N N 161 
COA H61  H  N N 162 
COA H62  H  N N 163 
COA HN4  H  N N 164 
COA H31  H  N N 165 
COA H32  H  N N 166 
COA H21  H  N N 167 
COA H22  H  N N 168 
COA HS1  H  N N 169 
CYS N    N  N N 170 
CYS CA   C  N R 171 
CYS C    C  N N 172 
CYS O    O  N N 173 
CYS CB   C  N N 174 
CYS SG   S  N N 175 
CYS OXT  O  N N 176 
CYS H    H  N N 177 
CYS H2   H  N N 178 
CYS HA   H  N N 179 
CYS HB2  H  N N 180 
CYS HB3  H  N N 181 
CYS HG   H  N N 182 
CYS HXT  H  N N 183 
GLN N    N  N N 184 
GLN CA   C  N S 185 
GLN C    C  N N 186 
GLN O    O  N N 187 
GLN CB   C  N N 188 
GLN CG   C  N N 189 
GLN CD   C  N N 190 
GLN OE1  O  N N 191 
GLN NE2  N  N N 192 
GLN OXT  O  N N 193 
GLN H    H  N N 194 
GLN H2   H  N N 195 
GLN HA   H  N N 196 
GLN HB2  H  N N 197 
GLN HB3  H  N N 198 
GLN HG2  H  N N 199 
GLN HG3  H  N N 200 
GLN HE21 H  N N 201 
GLN HE22 H  N N 202 
GLN HXT  H  N N 203 
GLU N    N  N N 204 
GLU CA   C  N S 205 
GLU C    C  N N 206 
GLU O    O  N N 207 
GLU CB   C  N N 208 
GLU CG   C  N N 209 
GLU CD   C  N N 210 
GLU OE1  O  N N 211 
GLU OE2  O  N N 212 
GLU OXT  O  N N 213 
GLU H    H  N N 214 
GLU H2   H  N N 215 
GLU HA   H  N N 216 
GLU HB2  H  N N 217 
GLU HB3  H  N N 218 
GLU HG2  H  N N 219 
GLU HG3  H  N N 220 
GLU HE2  H  N N 221 
GLU HXT  H  N N 222 
GLY N    N  N N 223 
GLY CA   C  N N 224 
GLY C    C  N N 225 
GLY O    O  N N 226 
GLY OXT  O  N N 227 
GLY H    H  N N 228 
GLY H2   H  N N 229 
GLY HA2  H  N N 230 
GLY HA3  H  N N 231 
GLY HXT  H  N N 232 
HIS N    N  N N 233 
HIS CA   C  N S 234 
HIS C    C  N N 235 
HIS O    O  N N 236 
HIS CB   C  N N 237 
HIS CG   C  Y N 238 
HIS ND1  N  Y N 239 
HIS CD2  C  Y N 240 
HIS CE1  C  Y N 241 
HIS NE2  N  Y N 242 
HIS OXT  O  N N 243 
HIS H    H  N N 244 
HIS H2   H  N N 245 
HIS HA   H  N N 246 
HIS HB2  H  N N 247 
HIS HB3  H  N N 248 
HIS HD1  H  N N 249 
HIS HD2  H  N N 250 
HIS HE1  H  N N 251 
HIS HE2  H  N N 252 
HIS HXT  H  N N 253 
HOH O    O  N N 254 
HOH H1   H  N N 255 
HOH H2   H  N N 256 
ILE N    N  N N 257 
ILE CA   C  N S 258 
ILE C    C  N N 259 
ILE O    O  N N 260 
ILE CB   C  N S 261 
ILE CG1  C  N N 262 
ILE CG2  C  N N 263 
ILE CD1  C  N N 264 
ILE OXT  O  N N 265 
ILE H    H  N N 266 
ILE H2   H  N N 267 
ILE HA   H  N N 268 
ILE HB   H  N N 269 
ILE HG12 H  N N 270 
ILE HG13 H  N N 271 
ILE HG21 H  N N 272 
ILE HG22 H  N N 273 
ILE HG23 H  N N 274 
ILE HD11 H  N N 275 
ILE HD12 H  N N 276 
ILE HD13 H  N N 277 
ILE HXT  H  N N 278 
LEU N    N  N N 279 
LEU CA   C  N S 280 
LEU C    C  N N 281 
LEU O    O  N N 282 
LEU CB   C  N N 283 
LEU CG   C  N N 284 
LEU CD1  C  N N 285 
LEU CD2  C  N N 286 
LEU OXT  O  N N 287 
LEU H    H  N N 288 
LEU H2   H  N N 289 
LEU HA   H  N N 290 
LEU HB2  H  N N 291 
LEU HB3  H  N N 292 
LEU HG   H  N N 293 
LEU HD11 H  N N 294 
LEU HD12 H  N N 295 
LEU HD13 H  N N 296 
LEU HD21 H  N N 297 
LEU HD22 H  N N 298 
LEU HD23 H  N N 299 
LEU HXT  H  N N 300 
LYS N    N  N N 301 
LYS CA   C  N S 302 
LYS C    C  N N 303 
LYS O    O  N N 304 
LYS CB   C  N N 305 
LYS CG   C  N N 306 
LYS CD   C  N N 307 
LYS CE   C  N N 308 
LYS NZ   N  N N 309 
LYS OXT  O  N N 310 
LYS H    H  N N 311 
LYS H2   H  N N 312 
LYS HA   H  N N 313 
LYS HB2  H  N N 314 
LYS HB3  H  N N 315 
LYS HG2  H  N N 316 
LYS HG3  H  N N 317 
LYS HD2  H  N N 318 
LYS HD3  H  N N 319 
LYS HE2  H  N N 320 
LYS HE3  H  N N 321 
LYS HZ1  H  N N 322 
LYS HZ2  H  N N 323 
LYS HZ3  H  N N 324 
LYS HXT  H  N N 325 
MET N    N  N N 326 
MET CA   C  N S 327 
MET C    C  N N 328 
MET O    O  N N 329 
MET CB   C  N N 330 
MET CG   C  N N 331 
MET SD   S  N N 332 
MET CE   C  N N 333 
MET OXT  O  N N 334 
MET H    H  N N 335 
MET H2   H  N N 336 
MET HA   H  N N 337 
MET HB2  H  N N 338 
MET HB3  H  N N 339 
MET HG2  H  N N 340 
MET HG3  H  N N 341 
MET HE1  H  N N 342 
MET HE2  H  N N 343 
MET HE3  H  N N 344 
MET HXT  H  N N 345 
MG  MG   MG N N 346 
PHE N    N  N N 347 
PHE CA   C  N S 348 
PHE C    C  N N 349 
PHE O    O  N N 350 
PHE CB   C  N N 351 
PHE CG   C  Y N 352 
PHE CD1  C  Y N 353 
PHE CD2  C  Y N 354 
PHE CE1  C  Y N 355 
PHE CE2  C  Y N 356 
PHE CZ   C  Y N 357 
PHE OXT  O  N N 358 
PHE H    H  N N 359 
PHE H2   H  N N 360 
PHE HA   H  N N 361 
PHE HB2  H  N N 362 
PHE HB3  H  N N 363 
PHE HD1  H  N N 364 
PHE HD2  H  N N 365 
PHE HE1  H  N N 366 
PHE HE2  H  N N 367 
PHE HZ   H  N N 368 
PHE HXT  H  N N 369 
PO4 P    P  N N 370 
PO4 O1   O  N N 371 
PO4 O2   O  N N 372 
PO4 O3   O  N N 373 
PO4 O4   O  N N 374 
PRO N    N  N N 375 
PRO CA   C  N S 376 
PRO C    C  N N 377 
PRO O    O  N N 378 
PRO CB   C  N N 379 
PRO CG   C  N N 380 
PRO CD   C  N N 381 
PRO OXT  O  N N 382 
PRO H    H  N N 383 
PRO HA   H  N N 384 
PRO HB2  H  N N 385 
PRO HB3  H  N N 386 
PRO HG2  H  N N 387 
PRO HG3  H  N N 388 
PRO HD2  H  N N 389 
PRO HD3  H  N N 390 
PRO HXT  H  N N 391 
SER N    N  N N 392 
SER CA   C  N S 393 
SER C    C  N N 394 
SER O    O  N N 395 
SER CB   C  N N 396 
SER OG   O  N N 397 
SER OXT  O  N N 398 
SER H    H  N N 399 
SER H2   H  N N 400 
SER HA   H  N N 401 
SER HB2  H  N N 402 
SER HB3  H  N N 403 
SER HG   H  N N 404 
SER HXT  H  N N 405 
THR N    N  N N 406 
THR CA   C  N S 407 
THR C    C  N N 408 
THR O    O  N N 409 
THR CB   C  N R 410 
THR OG1  O  N N 411 
THR CG2  C  N N 412 
THR OXT  O  N N 413 
THR H    H  N N 414 
THR H2   H  N N 415 
THR HA   H  N N 416 
THR HB   H  N N 417 
THR HG1  H  N N 418 
THR HG21 H  N N 419 
THR HG22 H  N N 420 
THR HG23 H  N N 421 
THR HXT  H  N N 422 
TYR N    N  N N 423 
TYR CA   C  N S 424 
TYR C    C  N N 425 
TYR O    O  N N 426 
TYR CB   C  N N 427 
TYR CG   C  Y N 428 
TYR CD1  C  Y N 429 
TYR CD2  C  Y N 430 
TYR CE1  C  Y N 431 
TYR CE2  C  Y N 432 
TYR CZ   C  Y N 433 
TYR OH   O  N N 434 
TYR OXT  O  N N 435 
TYR H    H  N N 436 
TYR H2   H  N N 437 
TYR HA   H  N N 438 
TYR HB2  H  N N 439 
TYR HB3  H  N N 440 
TYR HD1  H  N N 441 
TYR HD2  H  N N 442 
TYR HE1  H  N N 443 
TYR HE2  H  N N 444 
TYR HH   H  N N 445 
TYR HXT  H  N N 446 
VAL N    N  N N 447 
VAL CA   C  N S 448 
VAL C    C  N N 449 
VAL O    O  N N 450 
VAL CB   C  N N 451 
VAL CG1  C  N N 452 
VAL CG2  C  N N 453 
VAL OXT  O  N N 454 
VAL H    H  N N 455 
VAL H2   H  N N 456 
VAL HA   H  N N 457 
VAL HB   H  N N 458 
VAL HG11 H  N N 459 
VAL HG12 H  N N 460 
VAL HG13 H  N N 461 
VAL HG21 H  N N 462 
VAL HG22 H  N N 463 
VAL HG23 H  N N 464 
VAL HXT  H  N N 465 
# 
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 
2OP C   O    doub N N 1   
2OP C   CA   sing N N 2   
2OP CB  CA   sing N N 3   
2OP CB  HB1  sing N N 4   
2OP CB  HB2  sing N N 5   
2OP CB  HB3  sing N N 6   
2OP OHN CA   sing N N 7   
2OP C   OXT  sing N N 8   
2OP OHN H    sing N N 9   
2OP CA  HA   sing N N 10  
2OP OXT HXT  sing N N 11  
ALA N   CA   sing N N 12  
ALA N   H    sing N N 13  
ALA N   H2   sing N N 14  
ALA CA  C    sing N N 15  
ALA CA  CB   sing N N 16  
ALA CA  HA   sing N N 17  
ALA C   O    doub N N 18  
ALA C   OXT  sing N N 19  
ALA CB  HB1  sing N N 20  
ALA CB  HB2  sing N N 21  
ALA CB  HB3  sing N N 22  
ALA OXT HXT  sing N N 23  
ARG N   CA   sing N N 24  
ARG N   H    sing N N 25  
ARG N   H2   sing N N 26  
ARG CA  C    sing N N 27  
ARG CA  CB   sing N N 28  
ARG CA  HA   sing N N 29  
ARG C   O    doub N N 30  
ARG C   OXT  sing N N 31  
ARG CB  CG   sing N N 32  
ARG CB  HB2  sing N N 33  
ARG CB  HB3  sing N N 34  
ARG CG  CD   sing N N 35  
ARG CG  HG2  sing N N 36  
ARG CG  HG3  sing N N 37  
ARG CD  NE   sing N N 38  
ARG CD  HD2  sing N N 39  
ARG CD  HD3  sing N N 40  
ARG NE  CZ   sing N N 41  
ARG NE  HE   sing N N 42  
ARG CZ  NH1  sing N N 43  
ARG CZ  NH2  doub N N 44  
ARG NH1 HH11 sing N N 45  
ARG NH1 HH12 sing N N 46  
ARG NH2 HH21 sing N N 47  
ARG NH2 HH22 sing N N 48  
ARG OXT HXT  sing N N 49  
ASN N   CA   sing N N 50  
ASN N   H    sing N N 51  
ASN N   H2   sing N N 52  
ASN CA  C    sing N N 53  
ASN CA  CB   sing N N 54  
ASN CA  HA   sing N N 55  
ASN C   O    doub N N 56  
ASN C   OXT  sing N N 57  
ASN CB  CG   sing N N 58  
ASN CB  HB2  sing N N 59  
ASN CB  HB3  sing N N 60  
ASN CG  OD1  doub N N 61  
ASN CG  ND2  sing N N 62  
ASN ND2 HD21 sing N N 63  
ASN ND2 HD22 sing N N 64  
ASN OXT HXT  sing N N 65  
ASP N   CA   sing N N 66  
ASP N   H    sing N N 67  
ASP N   H2   sing N N 68  
ASP CA  C    sing N N 69  
ASP CA  CB   sing N N 70  
ASP CA  HA   sing N N 71  
ASP C   O    doub N N 72  
ASP C   OXT  sing N N 73  
ASP CB  CG   sing N N 74  
ASP CB  HB2  sing N N 75  
ASP CB  HB3  sing N N 76  
ASP CG  OD1  doub N N 77  
ASP CG  OD2  sing N N 78  
ASP OD2 HD2  sing N N 79  
ASP OXT HXT  sing N N 80  
COA N1A C2A  sing Y N 81  
COA N1A C6A  doub Y N 82  
COA C2A N3A  doub Y N 83  
COA C2A H2A  sing N N 84  
COA N3A C4A  sing Y N 85  
COA C4A C5A  doub Y N 86  
COA C4A N9A  sing Y N 87  
COA C5A C6A  sing Y N 88  
COA C5A N7A  sing Y N 89  
COA C6A N6A  sing N N 90  
COA N6A H61A sing N N 91  
COA N6A H62A sing N N 92  
COA N7A C8A  doub Y N 93  
COA C8A N9A  sing Y N 94  
COA C8A H8A  sing N N 95  
COA N9A C1B  sing N N 96  
COA C1B C2B  sing N N 97  
COA C1B O4B  sing N N 98  
COA C1B H1B  sing N N 99  
COA C2B O2B  sing N N 100 
COA C2B C3B  sing N N 101 
COA C2B H2B  sing N N 102 
COA O2B HO2A sing N N 103 
COA C3B O3B  sing N N 104 
COA C3B C4B  sing N N 105 
COA C3B H3B  sing N N 106 
COA O3B P3B  sing N N 107 
COA P3B O7A  doub N N 108 
COA P3B O8A  sing N N 109 
COA P3B O9A  sing N N 110 
COA O8A HOA8 sing N N 111 
COA O9A HOA9 sing N N 112 
COA C4B O4B  sing N N 113 
COA C4B C5B  sing N N 114 
COA C4B H4B  sing N N 115 
COA C5B O5B  sing N N 116 
COA C5B H51A sing N N 117 
COA C5B H52A sing N N 118 
COA O5B P1A  sing N N 119 
COA P1A O1A  doub N N 120 
COA P1A O2A  sing N N 121 
COA P1A O3A  sing N N 122 
COA O2A HOA2 sing N N 123 
COA O3A P2A  sing N N 124 
COA P2A O4A  doub N N 125 
COA P2A O5A  sing N N 126 
COA P2A O6A  sing N N 127 
COA O5A HOA5 sing N N 128 
COA O6A CCP  sing N N 129 
COA CBP CCP  sing N N 130 
COA CBP CDP  sing N N 131 
COA CBP CEP  sing N N 132 
COA CBP CAP  sing N N 133 
COA CCP H121 sing N N 134 
COA CCP H122 sing N N 135 
COA CDP H131 sing N N 136 
COA CDP H132 sing N N 137 
COA CDP H133 sing N N 138 
COA CEP H141 sing N N 139 
COA CEP H142 sing N N 140 
COA CEP H143 sing N N 141 
COA CAP OAP  sing N N 142 
COA CAP C9P  sing N N 143 
COA CAP H10  sing N N 144 
COA OAP HO1  sing N N 145 
COA C9P O9P  doub N N 146 
COA C9P N8P  sing N N 147 
COA N8P C7P  sing N N 148 
COA N8P HN8  sing N N 149 
COA C7P C6P  sing N N 150 
COA C7P H71  sing N N 151 
COA C7P H72  sing N N 152 
COA C6P C5P  sing N N 153 
COA C6P H61  sing N N 154 
COA C6P H62  sing N N 155 
COA C5P O5P  doub N N 156 
COA C5P N4P  sing N N 157 
COA N4P C3P  sing N N 158 
COA N4P HN4  sing N N 159 
COA C3P C2P  sing N N 160 
COA C3P H31  sing N N 161 
COA C3P H32  sing N N 162 
COA C2P S1P  sing N N 163 
COA C2P H21  sing N N 164 
COA C2P H22  sing N N 165 
COA S1P HS1  sing N N 166 
CYS N   CA   sing N N 167 
CYS N   H    sing N N 168 
CYS N   H2   sing N N 169 
CYS CA  C    sing N N 170 
CYS CA  CB   sing N N 171 
CYS CA  HA   sing N N 172 
CYS C   O    doub N N 173 
CYS C   OXT  sing N N 174 
CYS CB  SG   sing N N 175 
CYS CB  HB2  sing N N 176 
CYS CB  HB3  sing N N 177 
CYS SG  HG   sing N N 178 
CYS OXT HXT  sing N N 179 
GLN N   CA   sing N N 180 
GLN N   H    sing N N 181 
GLN N   H2   sing N N 182 
GLN CA  C    sing N N 183 
GLN CA  CB   sing N N 184 
GLN CA  HA   sing N N 185 
GLN C   O    doub N N 186 
GLN C   OXT  sing N N 187 
GLN CB  CG   sing N N 188 
GLN CB  HB2  sing N N 189 
GLN CB  HB3  sing N N 190 
GLN CG  CD   sing N N 191 
GLN CG  HG2  sing N N 192 
GLN CG  HG3  sing N N 193 
GLN CD  OE1  doub N N 194 
GLN CD  NE2  sing N N 195 
GLN NE2 HE21 sing N N 196 
GLN NE2 HE22 sing N N 197 
GLN OXT HXT  sing N N 198 
GLU N   CA   sing N N 199 
GLU N   H    sing N N 200 
GLU N   H2   sing N N 201 
GLU CA  C    sing N N 202 
GLU CA  CB   sing N N 203 
GLU CA  HA   sing N N 204 
GLU C   O    doub N N 205 
GLU C   OXT  sing N N 206 
GLU CB  CG   sing N N 207 
GLU CB  HB2  sing N N 208 
GLU CB  HB3  sing N N 209 
GLU CG  CD   sing N N 210 
GLU CG  HG2  sing N N 211 
GLU CG  HG3  sing N N 212 
GLU CD  OE1  doub N N 213 
GLU CD  OE2  sing N N 214 
GLU OE2 HE2  sing N N 215 
GLU OXT HXT  sing N N 216 
GLY N   CA   sing N N 217 
GLY N   H    sing N N 218 
GLY N   H2   sing N N 219 
GLY CA  C    sing N N 220 
GLY CA  HA2  sing N N 221 
GLY CA  HA3  sing N N 222 
GLY C   O    doub N N 223 
GLY C   OXT  sing N N 224 
GLY OXT HXT  sing N N 225 
HIS N   CA   sing N N 226 
HIS N   H    sing N N 227 
HIS N   H2   sing N N 228 
HIS CA  C    sing N N 229 
HIS CA  CB   sing N N 230 
HIS CA  HA   sing N N 231 
HIS C   O    doub N N 232 
HIS C   OXT  sing N N 233 
HIS CB  CG   sing N N 234 
HIS CB  HB2  sing N N 235 
HIS CB  HB3  sing N N 236 
HIS CG  ND1  sing Y N 237 
HIS CG  CD2  doub Y N 238 
HIS ND1 CE1  doub Y N 239 
HIS ND1 HD1  sing N N 240 
HIS CD2 NE2  sing Y N 241 
HIS CD2 HD2  sing N N 242 
HIS CE1 NE2  sing Y N 243 
HIS CE1 HE1  sing N N 244 
HIS NE2 HE2  sing N N 245 
HIS OXT HXT  sing N N 246 
HOH O   H1   sing N N 247 
HOH O   H2   sing N N 248 
ILE N   CA   sing N N 249 
ILE N   H    sing N N 250 
ILE N   H2   sing N N 251 
ILE CA  C    sing N N 252 
ILE CA  CB   sing N N 253 
ILE CA  HA   sing N N 254 
ILE C   O    doub N N 255 
ILE C   OXT  sing N N 256 
ILE CB  CG1  sing N N 257 
ILE CB  CG2  sing N N 258 
ILE CB  HB   sing N N 259 
ILE CG1 CD1  sing N N 260 
ILE CG1 HG12 sing N N 261 
ILE CG1 HG13 sing N N 262 
ILE CG2 HG21 sing N N 263 
ILE CG2 HG22 sing N N 264 
ILE CG2 HG23 sing N N 265 
ILE CD1 HD11 sing N N 266 
ILE CD1 HD12 sing N N 267 
ILE CD1 HD13 sing N N 268 
ILE OXT HXT  sing N N 269 
LEU N   CA   sing N N 270 
LEU N   H    sing N N 271 
LEU N   H2   sing N N 272 
LEU CA  C    sing N N 273 
LEU CA  CB   sing N N 274 
LEU CA  HA   sing N N 275 
LEU C   O    doub N N 276 
LEU C   OXT  sing N N 277 
LEU CB  CG   sing N N 278 
LEU CB  HB2  sing N N 279 
LEU CB  HB3  sing N N 280 
LEU CG  CD1  sing N N 281 
LEU CG  CD2  sing N N 282 
LEU CG  HG   sing N N 283 
LEU CD1 HD11 sing N N 284 
LEU CD1 HD12 sing N N 285 
LEU CD1 HD13 sing N N 286 
LEU CD2 HD21 sing N N 287 
LEU CD2 HD22 sing N N 288 
LEU CD2 HD23 sing N N 289 
LEU OXT HXT  sing N N 290 
LYS N   CA   sing N N 291 
LYS N   H    sing N N 292 
LYS N   H2   sing N N 293 
LYS CA  C    sing N N 294 
LYS CA  CB   sing N N 295 
LYS CA  HA   sing N N 296 
LYS C   O    doub N N 297 
LYS C   OXT  sing N N 298 
LYS CB  CG   sing N N 299 
LYS CB  HB2  sing N N 300 
LYS CB  HB3  sing N N 301 
LYS CG  CD   sing N N 302 
LYS CG  HG2  sing N N 303 
LYS CG  HG3  sing N N 304 
LYS CD  CE   sing N N 305 
LYS CD  HD2  sing N N 306 
LYS CD  HD3  sing N N 307 
LYS CE  NZ   sing N N 308 
LYS CE  HE2  sing N N 309 
LYS CE  HE3  sing N N 310 
LYS NZ  HZ1  sing N N 311 
LYS NZ  HZ2  sing N N 312 
LYS NZ  HZ3  sing N N 313 
LYS OXT HXT  sing N N 314 
MET N   CA   sing N N 315 
MET N   H    sing N N 316 
MET N   H2   sing N N 317 
MET CA  C    sing N N 318 
MET CA  CB   sing N N 319 
MET CA  HA   sing N N 320 
MET C   O    doub N N 321 
MET C   OXT  sing N N 322 
MET CB  CG   sing N N 323 
MET CB  HB2  sing N N 324 
MET CB  HB3  sing N N 325 
MET CG  SD   sing N N 326 
MET CG  HG2  sing N N 327 
MET CG  HG3  sing N N 328 
MET SD  CE   sing N N 329 
MET CE  HE1  sing N N 330 
MET CE  HE2  sing N N 331 
MET CE  HE3  sing N N 332 
MET OXT HXT  sing N N 333 
PHE N   CA   sing N N 334 
PHE N   H    sing N N 335 
PHE N   H2   sing N N 336 
PHE CA  C    sing N N 337 
PHE CA  CB   sing N N 338 
PHE CA  HA   sing N N 339 
PHE C   O    doub N N 340 
PHE C   OXT  sing N N 341 
PHE CB  CG   sing N N 342 
PHE CB  HB2  sing N N 343 
PHE CB  HB3  sing N N 344 
PHE CG  CD1  doub Y N 345 
PHE CG  CD2  sing Y N 346 
PHE CD1 CE1  sing Y N 347 
PHE CD1 HD1  sing N N 348 
PHE CD2 CE2  doub Y N 349 
PHE CD2 HD2  sing N N 350 
PHE CE1 CZ   doub Y N 351 
PHE CE1 HE1  sing N N 352 
PHE CE2 CZ   sing Y N 353 
PHE CE2 HE2  sing N N 354 
PHE CZ  HZ   sing N N 355 
PHE OXT HXT  sing N N 356 
PO4 P   O1   doub N N 357 
PO4 P   O2   sing N N 358 
PO4 P   O3   sing N N 359 
PO4 P   O4   sing N N 360 
PRO N   CA   sing N N 361 
PRO N   CD   sing N N 362 
PRO N   H    sing N N 363 
PRO CA  C    sing N N 364 
PRO CA  CB   sing N N 365 
PRO CA  HA   sing N N 366 
PRO C   O    doub N N 367 
PRO C   OXT  sing N N 368 
PRO CB  CG   sing N N 369 
PRO CB  HB2  sing N N 370 
PRO CB  HB3  sing N N 371 
PRO CG  CD   sing N N 372 
PRO CG  HG2  sing N N 373 
PRO CG  HG3  sing N N 374 
PRO CD  HD2  sing N N 375 
PRO CD  HD3  sing N N 376 
PRO OXT HXT  sing N N 377 
SER N   CA   sing N N 378 
SER N   H    sing N N 379 
SER N   H2   sing N N 380 
SER CA  C    sing N N 381 
SER CA  CB   sing N N 382 
SER CA  HA   sing N N 383 
SER C   O    doub N N 384 
SER C   OXT  sing N N 385 
SER CB  OG   sing N N 386 
SER CB  HB2  sing N N 387 
SER CB  HB3  sing N N 388 
SER OG  HG   sing N N 389 
SER OXT HXT  sing N N 390 
THR N   CA   sing N N 391 
THR N   H    sing N N 392 
THR N   H2   sing N N 393 
THR CA  C    sing N N 394 
THR CA  CB   sing N N 395 
THR CA  HA   sing N N 396 
THR C   O    doub N N 397 
THR C   OXT  sing N N 398 
THR CB  OG1  sing N N 399 
THR CB  CG2  sing N N 400 
THR CB  HB   sing N N 401 
THR OG1 HG1  sing N N 402 
THR CG2 HG21 sing N N 403 
THR CG2 HG22 sing N N 404 
THR CG2 HG23 sing N N 405 
THR OXT HXT  sing N N 406 
TYR N   CA   sing N N 407 
TYR N   H    sing N N 408 
TYR N   H2   sing N N 409 
TYR CA  C    sing N N 410 
TYR CA  CB   sing N N 411 
TYR CA  HA   sing N N 412 
TYR C   O    doub N N 413 
TYR C   OXT  sing N N 414 
TYR CB  CG   sing N N 415 
TYR CB  HB2  sing N N 416 
TYR CB  HB3  sing N N 417 
TYR CG  CD1  doub Y N 418 
TYR CG  CD2  sing Y N 419 
TYR CD1 CE1  sing Y N 420 
TYR CD1 HD1  sing N N 421 
TYR CD2 CE2  doub Y N 422 
TYR CD2 HD2  sing N N 423 
TYR CE1 CZ   doub Y N 424 
TYR CE1 HE1  sing N N 425 
TYR CE2 CZ   sing Y N 426 
TYR CE2 HE2  sing N N 427 
TYR CZ  OH   sing N N 428 
TYR OH  HH   sing N N 429 
TYR OXT HXT  sing N N 430 
VAL N   CA   sing N N 431 
VAL N   H    sing N N 432 
VAL N   H2   sing N N 433 
VAL CA  C    sing N N 434 
VAL CA  CB   sing N N 435 
VAL CA  HA   sing N N 436 
VAL C   O    doub N N 437 
VAL C   OXT  sing N N 438 
VAL CB  CG1  sing N N 439 
VAL CB  CG2  sing N N 440 
VAL CB  HB   sing N N 441 
VAL CG1 HG11 sing N N 442 
VAL CG1 HG12 sing N N 443 
VAL CG1 HG13 sing N N 444 
VAL CG2 HG21 sing N N 445 
VAL CG2 HG22 sing N N 446 
VAL CG2 HG23 sing N N 447 
VAL OXT HXT  sing N N 448 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM135504 1 
'National Institutes of Health/National Cancer Institute (NIH/NCI)'                        'United States' CA251677 2 
'National Natural Science Foundation of China (NSFC)'                                      China           81973164 3 
# 
_pdbx_initial_refinement_model.accession_code   5CAE 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    8Z03 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.018477 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000688 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007442 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.017304 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
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   . SER A 1 2   ? -12.120 -37.210 0.122   1.00 19.58 ? 2    SER A N   1 
ATOM   2    C  CA  . SER A 1 2   ? -11.310 -36.118 0.630   1.00 24.61 ? 2    SER A CA  1 
ATOM   3    C  C   . SER A 1 2   ? -9.830  -36.489 0.564   1.00 25.40 ? 2    SER A C   1 
ATOM   4    O  O   . SER A 1 2   ? -9.470  -37.621 0.219   1.00 21.92 ? 2    SER A O   1 
ATOM   5    C  CB  . SER A 1 2   ? -11.681 -35.780 2.069   1.00 24.44 ? 2    SER A CB  1 
ATOM   6    O  OG  . SER A 1 2   ? -10.989 -36.650 2.962   1.00 25.33 ? 2    SER A OG  1 
ATOM   7    N  N   . TYR A 1 3   ? -8.980  -35.532 0.944   1.00 19.98 ? 3    TYR A N   1 
ATOM   8    C  CA  . TYR A 1 3   ? -7.539  -35.743 0.855   1.00 20.69 ? 3    TYR A CA  1 
ATOM   9    C  C   . TYR A 1 3   ? -7.084  -36.942 1.682   1.00 19.11 ? 3    TYR A C   1 
ATOM   10   O  O   . TYR A 1 3   ? -6.075  -37.574 1.347   1.00 18.89 ? 3    TYR A O   1 
ATOM   11   C  CB  . TYR A 1 3   ? -6.811  -34.476 1.304   1.00 19.01 ? 3    TYR A CB  1 
ATOM   12   C  CG  . TYR A 1 3   ? -5.293  -34.596 1.344   1.00 18.28 ? 3    TYR A CG  1 
ATOM   13   C  CD1 . TYR A 1 3   ? -4.559  -34.880 0.180   1.00 18.35 ? 3    TYR A CD1 1 
ATOM   14   C  CD2 . TYR A 1 3   ? -4.594  -34.390 2.529   1.00 16.76 ? 3    TYR A CD2 1 
ATOM   15   C  CE1 . TYR A 1 3   ? -3.170  -34.962 0.206   1.00 14.85 ? 3    TYR A CE1 1 
ATOM   16   C  CE2 . TYR A 1 3   ? -3.211  -34.476 2.566   1.00 16.89 ? 3    TYR A CE2 1 
ATOM   17   C  CZ  . TYR A 1 3   ? -2.506  -34.763 1.401   1.00 15.08 ? 3    TYR A CZ  1 
ATOM   18   O  OH  . TYR A 1 3   ? -1.135  -34.851 1.447   1.00 16.50 ? 3    TYR A OH  1 
ATOM   19   N  N   . THR A 1 4   ? -7.804  -37.266 2.764   1.00 18.56 ? 4    THR A N   1 
ATOM   20   C  CA  . THR A 1 4   ? -7.428  -38.399 3.609   1.00 20.20 ? 4    THR A CA  1 
ATOM   21   C  C   . THR A 1 4   ? -7.400  -39.705 2.832   1.00 19.22 ? 4    THR A C   1 
ATOM   22   O  O   . THR A 1 4   ? -6.718  -40.648 3.251   1.00 22.99 ? 4    THR A O   1 
ATOM   23   C  CB  . THR A 1 4   ? -8.397  -38.550 4.797   1.00 24.04 ? 4    THR A CB  1 
ATOM   24   O  OG1 . THR A 1 4   ? -9.681  -38.934 4.315   1.00 25.29 ? 4    THR A OG1 1 
ATOM   25   C  CG2 . THR A 1 4   ? -8.547  -37.243 5.565   1.00 19.31 ? 4    THR A CG2 1 
ATOM   26   N  N   . ALA A 1 5   ? -8.133  -39.780 1.720   1.00 16.59 ? 5    ALA A N   1 
ATOM   27   C  CA  . ALA A 1 5   ? -8.177  -40.979 0.894   1.00 25.73 ? 5    ALA A CA  1 
ATOM   28   C  C   . ALA A 1 5   ? -6.838  -41.308 0.246   1.00 27.04 ? 5    ALA A C   1 
ATOM   29   O  O   . ALA A 1 5   ? -6.684  -42.418 -0.283  1.00 26.66 ? 5    ALA A O   1 
ATOM   30   C  CB  . ALA A 1 5   ? -9.250  -40.824 -0.191  1.00 24.23 ? 5    ALA A CB  1 
ATOM   31   N  N   . SER A 1 6   ? -5.876  -40.386 0.258   1.00 20.00 ? 6    SER A N   1 
ATOM   32   C  CA  . SER A 1 6   ? -4.568  -40.642 -0.326  1.00 19.22 ? 6    SER A CA  1 
ATOM   33   C  C   . SER A 1 6   ? -3.544  -41.112 0.698   1.00 18.60 ? 6    SER A C   1 
ATOM   34   O  O   . SER A 1 6   ? -2.367  -41.266 0.342   1.00 16.80 ? 6    SER A O   1 
ATOM   35   C  CB  . SER A 1 6   ? -4.049  -39.383 -1.031  1.00 16.88 ? 6    SER A CB  1 
ATOM   36   O  OG  . SER A 1 6   ? -3.699  -38.385 -0.080  1.00 16.40 ? 6    SER A OG  1 
ATOM   37   N  N   . ARG A 1 7   ? -3.954  -41.326 1.959   1.00 20.15 ? 7    ARG A N   1 
ATOM   38   C  CA  . ARG A 1 7   ? -2.998  -41.695 3.003   1.00 19.41 ? 7    ARG A CA  1 
ATOM   39   C  C   . ARG A 1 7   ? -2.267  -42.975 2.657   1.00 18.74 ? 7    ARG A C   1 
ATOM   40   O  O   . ARG A 1 7   ? -1.081  -43.123 2.975   1.00 16.43 ? 7    ARG A O   1 
ATOM   41   C  CB  . ARG A 1 7   ? -3.687  -41.891 4.348   1.00 19.84 ? 7    ARG A CB  1 
ATOM   42   C  CG  . ARG A 1 7   ? -3.888  -40.679 5.176   1.00 22.16 ? 7    ARG A CG  1 
ATOM   43   C  CD  . ARG A 1 7   ? -4.813  -41.063 6.326   1.00 19.66 ? 7    ARG A CD  1 
ATOM   44   N  NE  . ARG A 1 7   ? -5.120  -39.922 7.176   1.00 22.67 ? 7    ARG A NE  1 
ATOM   45   C  CZ  . ARG A 1 7   ? -6.173  -39.877 7.978   1.00 25.59 ? 7    ARG A CZ  1 
ATOM   46   N  NH1 . ARG A 1 7   ? -7.010  -40.904 8.006   1.00 32.65 ? 7    ARG A NH1 1 
ATOM   47   N  NH2 . ARG A 1 7   ? -6.393  -38.811 8.738   1.00 25.52 ? 7    ARG A NH2 1 
ATOM   48   N  N   . GLN A 1 8   ? -2.966  -43.927 2.035   1.00 17.54 ? 8    GLN A N   1 
ATOM   49   C  CA  . GLN A 1 8   ? -2.328  -45.212 1.771   1.00 19.49 ? 8    GLN A CA  1 
ATOM   50   C  C   . GLN A 1 8   ? -1.096  -45.060 0.894   1.00 16.23 ? 8    GLN A C   1 
ATOM   51   O  O   . GLN A 1 8   ? -0.196  -45.895 0.981   1.00 16.03 ? 8    GLN A O   1 
ATOM   52   C  CB  . GLN A 1 8   ? -3.323  -46.199 1.137   1.00 21.74 ? 8    GLN A CB  1 
ATOM   53   C  CG  . GLN A 1 8   ? -3.977  -45.696 -0.144  1.00 27.28 ? 8    GLN A CG  1 
ATOM   54   N  N   . HIS A 1 9   ? -1.012  -43.986 0.089   1.00 16.33 ? 9    HIS A N   1 
ATOM   55   C  CA  . HIS A 1 9   ? 0.133   -43.806 -0.802  1.00 15.40 ? 9    HIS A CA  1 
ATOM   56   C  C   . HIS A 1 9   ? 1.435   -43.607 -0.035  1.00 18.18 ? 9    HIS A C   1 
ATOM   57   O  O   . HIS A 1 9   ? 2.509   -43.708 -0.637  1.00 17.63 ? 9    HIS A O   1 
ATOM   58   C  CB  . HIS A 1 9   ? -0.096  -42.617 -1.747  1.00 15.33 ? 9    HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 9   ? -1.362  -42.711 -2.553  1.00 22.89 ? 9    HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 9   ? -2.102  -43.873 -2.653  1.00 23.04 ? 9    HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 9   ? -2.022  -41.781 -3.289  1.00 18.06 ? 9    HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 9   ? -3.159  -43.656 -3.420  1.00 24.72 ? 9    HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 9   ? -3.137  -42.393 -3.815  1.00 23.71 ? 9    HIS A NE2 1 
ATOM   64   N  N   . LEU A 1 10  ? 1.359   -43.313 1.271   1.00 19.89 ? 10   LEU A N   1 
ATOM   65   C  CA  . LEU A 1 10  ? 2.560   -43.172 2.098   1.00 16.50 ? 10   LEU A CA  1 
ATOM   66   C  C   . LEU A 1 10  ? 3.357   -44.465 2.159   1.00 21.20 ? 10   LEU A C   1 
ATOM   67   O  O   . LEU A 1 10  ? 4.578   -44.431 2.392   1.00 17.32 ? 10   LEU A O   1 
ATOM   68   C  CB  . LEU A 1 10  ? 2.181   -42.749 3.526   1.00 15.90 ? 10   LEU A CB  1 
ATOM   69   C  CG  . LEU A 1 10  ? 1.502   -41.391 3.752   1.00 16.50 ? 10   LEU A CG  1 
ATOM   70   C  CD1 . LEU A 1 10  ? 0.967   -41.236 5.177   1.00 17.69 ? 10   LEU A CD1 1 
ATOM   71   C  CD2 . LEU A 1 10  ? 2.473   -40.242 3.447   1.00 15.17 ? 10   LEU A CD2 1 
ATOM   72   N  N   . TYR A 1 11  ? 2.690   -45.612 1.986   1.00 17.80 ? 11   TYR A N   1 
ATOM   73   C  CA  . TYR A 1 11  ? 3.323   -46.901 2.267   1.00 20.38 ? 11   TYR A CA  1 
ATOM   74   C  C   . TYR A 1 11  ? 4.020   -47.388 1.001   1.00 20.24 ? 11   TYR A C   1 
ATOM   75   O  O   . TYR A 1 11  ? 3.571   -48.306 0.311   1.00 13.29 ? 11   TYR A O   1 
ATOM   76   C  CB  . TYR A 1 11  ? 2.309   -47.910 2.802   1.00 21.63 ? 11   TYR A CB  1 
ATOM   77   C  CG  . TYR A 1 11  ? 2.912   -48.881 3.803   1.00 20.50 ? 11   TYR A CG  1 
ATOM   78   C  CD1 . TYR A 1 11  ? 4.098   -49.554 3.521   1.00 24.09 ? 11   TYR A CD1 1 
ATOM   79   C  CD2 . TYR A 1 11  ? 2.308   -49.108 5.038   1.00 21.30 ? 11   TYR A CD2 1 
ATOM   80   C  CE1 . TYR A 1 11  ? 4.665   -50.443 4.432   1.00 24.45 ? 11   TYR A CE1 1 
ATOM   81   C  CE2 . TYR A 1 11  ? 2.875   -49.980 5.960   1.00 21.77 ? 11   TYR A CE2 1 
ATOM   82   C  CZ  . TYR A 1 11  ? 4.052   -50.649 5.646   1.00 22.66 ? 11   TYR A CZ  1 
ATOM   83   O  OH  . TYR A 1 11  ? 4.612   -51.511 6.556   1.00 21.55 ? 11   TYR A OH  1 
ATOM   84   N  N   . VAL A 1 12  ? 5.164   -46.758 0.717   1.00 16.76 ? 12   VAL A N   1 
ATOM   85   C  CA  . VAL A 1 12  ? 5.976   -47.148 -0.430  1.00 18.09 ? 12   VAL A CA  1 
ATOM   86   C  C   . VAL A 1 12  ? 6.440   -48.591 -0.267  1.00 20.01 ? 12   VAL A C   1 
ATOM   87   O  O   . VAL A 1 12  ? 6.561   -49.102 0.856   1.00 19.94 ? 12   VAL A O   1 
ATOM   88   C  CB  . VAL A 1 12  ? 7.172   -46.194 -0.552  1.00 16.21 ? 12   VAL A CB  1 
ATOM   89   C  CG1 . VAL A 1 12  ? 6.673   -44.783 -0.806  1.00 17.10 ? 12   VAL A CG1 1 
ATOM   90   C  CG2 . VAL A 1 12  ? 7.970   -46.216 0.750   1.00 14.94 ? 12   VAL A CG2 1 
ATOM   91   N  N   . ASP A 1 13  ? 6.681   -49.265 -1.389  1.00 18.24 ? 13   ASP A N   1 
ATOM   92   C  CA  . ASP A 1 13  ? 7.099   -50.668 -1.323  1.00 19.82 ? 13   ASP A CA  1 
ATOM   93   C  C   . ASP A 1 13  ? 7.992   -50.999 -2.517  1.00 22.32 ? 13   ASP A C   1 
ATOM   94   O  O   . ASP A 1 13  ? 8.373   -50.123 -3.303  1.00 16.79 ? 13   ASP A O   1 
ATOM   95   C  CB  . ASP A 1 13  ? 5.880   -51.601 -1.212  1.00 24.49 ? 13   ASP A CB  1 
ATOM   96   C  CG  . ASP A 1 13  ? 4.913   -51.496 -2.393  1.00 25.07 ? 13   ASP A CG  1 
ATOM   97   O  OD1 . ASP A 1 13  ? 5.332   -51.247 -3.550  1.00 21.17 ? 13   ASP A OD1 1 
ATOM   98   O  OD2 . ASP A 1 13  ? 3.708   -51.677 -2.144  1.00 25.16 ? 13   ASP A OD2 1 
ATOM   99   N  N   . LYS A 1 14  ? 8.328   -52.285 -2.647  1.00 21.83 ? 14   LYS A N   1 
ATOM   100  C  CA  . LYS A 1 14  ? 9.168   -52.741 -3.751  1.00 22.74 ? 14   LYS A CA  1 
ATOM   101  C  C   . LYS A 1 14  ? 8.598   -52.391 -5.127  1.00 19.56 ? 14   LYS A C   1 
ATOM   102  O  O   . LYS A 1 14  ? 9.358   -52.328 -6.096  1.00 21.41 ? 14   LYS A O   1 
ATOM   103  C  CB  . LYS A 1 14  ? 9.370   -54.256 -3.649  1.00 21.62 ? 14   LYS A CB  1 
ATOM   104  C  CG  . LYS A 1 14  ? 8.067   -55.047 -3.652  1.00 28.13 ? 14   LYS A CG  1 
ATOM   105  N  N   . ASN A 1 15  ? 7.291   -52.178 -5.247  1.00 22.11 ? 15   ASN A N   1 
ATOM   106  C  CA  . ASN A 1 15  ? 6.684   -51.858 -6.536  1.00 22.08 ? 15   ASN A CA  1 
ATOM   107  C  C   . ASN A 1 15  ? 6.645   -50.364 -6.848  1.00 24.22 ? 15   ASN A C   1 
ATOM   108  O  O   . ASN A 1 15  ? 6.290   -49.994 -7.970  1.00 22.98 ? 15   ASN A O   1 
ATOM   109  C  CB  . ASN A 1 15  ? 5.254   -52.418 -6.602  1.00 27.67 ? 15   ASN A CB  1 
ATOM   110  C  CG  . ASN A 1 15  ? 5.218   -53.942 -6.505  1.00 31.94 ? 15   ASN A CG  1 
ATOM   111  O  OD1 . ASN A 1 15  ? 6.122   -54.623 -6.997  1.00 28.78 ? 15   ASN A OD1 1 
ATOM   112  N  ND2 . ASN A 1 15  ? 4.183   -54.476 -5.853  1.00 28.59 ? 15   ASN A ND2 1 
ATOM   113  N  N   . THR A 1 16  ? 6.988   -49.500 -5.897  1.00 19.71 ? 16   THR A N   1 
ATOM   114  C  CA  . THR A 1 16  ? 6.960   -48.062 -6.142  1.00 19.10 ? 16   THR A CA  1 
ATOM   115  C  C   . THR A 1 16  ? 8.026   -47.649 -7.157  1.00 23.40 ? 16   THR A C   1 
ATOM   116  O  O   . THR A 1 16  ? 9.210   -47.967 -6.997  1.00 20.74 ? 16   THR A O   1 
ATOM   117  C  CB  . THR A 1 16  ? 7.182   -47.306 -4.834  1.00 18.26 ? 16   THR A CB  1 
ATOM   118  O  OG1 . THR A 1 16  ? 6.237   -47.763 -3.859  1.00 19.15 ? 16   THR A OG1 1 
ATOM   119  C  CG2 . THR A 1 16  ? 7.021   -45.783 -5.053  1.00 16.63 ? 16   THR A CG2 1 
ATOM   120  N  N   . LYS A 1 17  ? 7.612   -46.910 -8.187  1.00 21.35 ? 17   LYS A N   1 
ATOM   121  C  CA  . LYS A 1 17  ? 8.520   -46.357 -9.187  1.00 18.71 ? 17   LYS A CA  1 
ATOM   122  C  C   . LYS A 1 17  ? 8.629   -44.846 -8.997  1.00 17.80 ? 17   LYS A C   1 
ATOM   123  O  O   . LYS A 1 17  ? 7.609   -44.161 -8.895  1.00 16.31 ? 17   LYS A O   1 
ATOM   124  C  CB  . LYS A 1 17  ? 8.024   -46.666 -10.605 1.00 24.78 ? 17   LYS A CB  1 
ATOM   125  C  CG  . LYS A 1 17  ? 7.920   -48.141 -10.932 1.00 23.52 ? 17   LYS A CG  1 
ATOM   126  C  CD  . LYS A 1 17  ? 7.650   -48.344 -12.419 1.00 29.45 ? 17   LYS A CD  1 
ATOM   127  C  CE  . LYS A 1 17  ? 7.326   -49.799 -12.715 1.00 38.42 ? 17   LYS A CE  1 
ATOM   128  N  NZ  . LYS A 1 17  ? 6.056   -50.204 -12.047 1.00 41.51 ? 17   LYS A NZ  1 
ATOM   129  N  N   . ILE A 1 18  ? 9.860   -44.326 -8.990  1.00 18.94 ? 18   ILE A N   1 
ATOM   130  C  CA  . ILE A 1 18  ? 10.142  -42.963 -8.549  1.00 18.13 ? 18   ILE A CA  1 
ATOM   131  C  C   . ILE A 1 18  ? 10.743  -42.164 -9.697  1.00 17.77 ? 18   ILE A C   1 
ATOM   132  O  O   . ILE A 1 18  ? 11.548  -42.693 -10.468 1.00 18.07 ? 18   ILE A O   1 
ATOM   133  C  CB  . ILE A 1 18  ? 11.101  -42.964 -7.333  1.00 18.18 ? 18   ILE A CB  1 
ATOM   134  C  CG1 . ILE A 1 18  ? 10.462  -43.689 -6.148  1.00 16.82 ? 18   ILE A CG1 1 
ATOM   135  C  CG2 . ILE A 1 18  ? 11.493  -41.549 -6.948  1.00 19.67 ? 18   ILE A CG2 1 
ATOM   136  C  CD1 . ILE A 1 18  ? 11.034  -45.031 -5.893  1.00 23.56 ? 18   ILE A CD1 1 
ATOM   137  N  N   . ILE A 1 19  ? 10.345  -40.887 -9.808  1.00 17.65 ? 19   ILE A N   1 
ATOM   138  C  CA  . ILE A 1 19  ? 11.053  -39.899 -10.620 1.00 19.06 ? 19   ILE A CA  1 
ATOM   139  C  C   . ILE A 1 19  ? 11.586  -38.799 -9.707  1.00 19.39 ? 19   ILE A C   1 
ATOM   140  O  O   . ILE A 1 19  ? 11.015  -38.500 -8.652  1.00 17.54 ? 19   ILE A O   1 
ATOM   141  C  CB  . ILE A 1 19  ? 10.173  -39.283 -11.736 1.00 18.88 ? 19   ILE A CB  1 
ATOM   142  C  CG1 . ILE A 1 19  ? 8.949   -38.583 -11.131 1.00 18.16 ? 19   ILE A CG1 1 
ATOM   143  C  CG2 . ILE A 1 19  ? 9.783   -40.341 -12.751 1.00 15.22 ? 19   ILE A CG2 1 
ATOM   144  C  CD1 . ILE A 1 19  ? 8.226   -37.628 -12.093 1.00 19.78 ? 19   ILE A CD1 1 
ATOM   145  N  N   . CYS A 1 20  ? 12.672  -38.168 -10.132 1.00 18.30 ? 20   CYS A N   1 
ATOM   146  C  CA  . CYS A 1 20  ? 13.292  -37.096 -9.360  1.00 15.41 ? 20   CYS A CA  1 
ATOM   147  C  C   . CYS A 1 20  ? 12.997  -35.750 -10.018 1.00 17.70 ? 20   CYS A C   1 
ATOM   148  O  O   . CYS A 1 20  ? 13.318  -35.548 -11.193 1.00 15.91 ? 20   CYS A O   1 
ATOM   149  C  CB  . CYS A 1 20  ? 14.795  -37.344 -9.245  1.00 17.66 ? 20   CYS A CB  1 
ATOM   150  S  SG  . CYS A 1 20  ? 15.706  -36.136 -8.289  1.00 19.08 ? 20   CYS A SG  1 
ATOM   151  N  N   . GLN A 1 21  ? 12.373  -34.837 -9.269  1.00 16.12 ? 21   GLN A N   1 
ATOM   152  C  CA  . GLN A 1 21  ? 12.178  -33.462 -9.720  1.00 14.61 ? 21   GLN A CA  1 
ATOM   153  C  C   . GLN A 1 21  ? 13.399  -32.656 -9.283  1.00 15.63 ? 21   GLN A C   1 
ATOM   154  O  O   . GLN A 1 21  ? 13.750  -32.637 -8.097  1.00 16.48 ? 21   GLN A O   1 
ATOM   155  C  CB  . GLN A 1 21  ? 10.868  -32.880 -9.172  1.00 13.49 ? 21   GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 21  ? 9.631   -33.521 -9.826  1.00 15.45 ? 21   GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 21  ? 8.288   -32.986 -9.310  1.00 14.31 ? 21   GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 21  ? 7.582   -33.667 -8.580  1.00 12.24 ? 21   GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 21  ? 7.928   -31.776 -9.720  1.00 13.98 ? 21   GLN A NE2 1 
ATOM   160  N  N   . GLY A 1 22  ? 14.062  -32.023 -10.242 1.00 16.51 ? 22   GLY A N   1 
ATOM   161  C  CA  . GLY A 1 22  ? 15.387  -31.493 -9.998  1.00 16.18 ? 22   GLY A CA  1 
ATOM   162  C  C   . GLY A 1 22  ? 16.480  -32.496 -10.263 1.00 18.62 ? 22   GLY A C   1 
ATOM   163  O  O   . GLY A 1 22  ? 17.538  -32.419 -9.626  1.00 19.48 ? 22   GLY A O   1 
ATOM   164  N  N   . PHE A 1 23  ? 16.248  -33.419 -11.212 1.00 17.98 ? 23   PHE A N   1 
ATOM   165  C  CA  . PHE A 1 23  ? 17.104  -34.572 -11.496 1.00 20.61 ? 23   PHE A CA  1 
ATOM   166  C  C   . PHE A 1 23  ? 18.572  -34.195 -11.702 1.00 21.71 ? 23   PHE A C   1 
ATOM   167  O  O   . PHE A 1 23  ? 19.473  -34.861 -11.181 1.00 18.93 ? 23   PHE A O   1 
ATOM   168  C  CB  . PHE A 1 23  ? 16.561  -35.272 -12.750 1.00 19.60 ? 23   PHE A CB  1 
ATOM   169  C  CG  . PHE A 1 23  ? 17.044  -36.680 -12.960 1.00 18.94 ? 23   PHE A CG  1 
ATOM   170  C  CD1 . PHE A 1 23  ? 17.586  -37.430 -11.929 1.00 21.23 ? 23   PHE A CD1 1 
ATOM   171  C  CD2 . PHE A 1 23  ? 16.934  -37.264 -14.220 1.00 21.19 ? 23   PHE A CD2 1 
ATOM   172  C  CE1 . PHE A 1 23  ? 18.013  -38.751 -12.153 1.00 22.55 ? 23   PHE A CE1 1 
ATOM   173  C  CE2 . PHE A 1 23  ? 17.349  -38.585 -14.454 1.00 19.68 ? 23   PHE A CE2 1 
ATOM   174  C  CZ  . PHE A 1 23  ? 17.887  -39.327 -13.423 1.00 20.73 ? 23   PHE A CZ  1 
ATOM   175  N  N   . THR A 1 24  ? 18.834  -33.152 -12.487 1.00 20.52 ? 24   THR A N   1 
ATOM   176  C  CA  . THR A 1 24  ? 20.197  -32.812 -12.885 1.00 18.93 ? 24   THR A CA  1 
ATOM   177  C  C   . THR A 1 24  ? 20.890  -31.846 -11.931 1.00 24.90 ? 24   THR A C   1 
ATOM   178  O  O   . THR A 1 24  ? 22.047  -31.492 -12.169 1.00 21.54 ? 24   THR A O   1 
ATOM   179  C  CB  . THR A 1 24  ? 20.206  -32.207 -14.297 1.00 22.56 ? 24   THR A CB  1 
ATOM   180  O  OG1 . THR A 1 24  ? 19.320  -31.085 -14.341 1.00 19.85 ? 24   THR A OG1 1 
ATOM   181  C  CG2 . THR A 1 24  ? 19.755  -33.230 -15.325 1.00 22.37 ? 24   THR A CG2 1 
ATOM   182  N  N   . GLY A 1 25  ? 20.227  -31.412 -10.864 1.00 22.19 ? 25   GLY A N   1 
ATOM   183  C  CA  . GLY A 1 25  ? 20.859  -30.539 -9.895  1.00 21.24 ? 25   GLY A CA  1 
ATOM   184  C  C   . GLY A 1 25  ? 21.860  -31.290 -9.040  1.00 19.62 ? 25   GLY A C   1 
ATOM   185  O  O   . GLY A 1 25  ? 22.086  -32.489 -9.190  1.00 21.90 ? 25   GLY A O   1 
ATOM   186  N  N   . LYS A 1 26  ? 22.464  -30.556 -8.104  1.00 16.89 ? 26   LYS A N   1 
ATOM   187  C  CA  . LYS A 1 26  ? 23.528  -31.114 -7.273  1.00 21.28 ? 26   LYS A CA  1 
ATOM   188  C  C   . LYS A 1 26  ? 23.016  -32.243 -6.385  1.00 25.87 ? 26   LYS A C   1 
ATOM   189  O  O   . LYS A 1 26  ? 23.511  -33.375 -6.446  1.00 23.84 ? 26   LYS A O   1 
ATOM   190  C  CB  . LYS A 1 26  ? 24.150  -30.007 -6.422  1.00 23.41 ? 26   LYS A CB  1 
ATOM   191  C  CG  . LYS A 1 26  ? 25.644  -30.078 -6.321  1.00 30.51 ? 26   LYS A CG  1 
ATOM   192  C  CD  . LYS A 1 26  ? 26.095  -30.106 -4.865  1.00 35.70 ? 26   LYS A CD  1 
ATOM   193  N  N   . GLN A 1 27  ? 22.030  -31.949 -5.528  1.00 21.07 ? 27   GLN A N   1 
ATOM   194  C  CA  . GLN A 1 27  ? 21.517  -32.978 -4.631  1.00 21.78 ? 27   GLN A CA  1 
ATOM   195  C  C   . GLN A 1 27  ? 20.646  -33.988 -5.367  1.00 19.88 ? 27   GLN A C   1 
ATOM   196  O  O   . GLN A 1 27  ? 20.638  -35.177 -5.011  1.00 22.55 ? 27   GLN A O   1 
ATOM   197  C  CB  . GLN A 1 27  ? 20.735  -32.340 -3.476  1.00 22.76 ? 27   GLN A CB  1 
ATOM   198  C  CG  . GLN A 1 27  ? 21.549  -31.404 -2.577  1.00 18.71 ? 27   GLN A CG  1 
ATOM   199  C  CD  . GLN A 1 27  ? 22.821  -32.026 -2.035  1.00 28.74 ? 27   GLN A CD  1 
ATOM   200  O  OE1 . GLN A 1 27  ? 22.894  -33.233 -1.801  1.00 32.80 ? 27   GLN A OE1 1 
ATOM   201  N  NE2 . GLN A 1 27  ? 23.834  -31.194 -1.822  1.00 33.07 ? 27   GLN A NE2 1 
ATOM   202  N  N   . GLY A 1 28  ? 19.894  -33.536 -6.369  1.00 17.82 ? 28   GLY A N   1 
ATOM   203  C  CA  . GLY A 1 28  ? 19.160  -34.474 -7.203  1.00 17.49 ? 28   GLY A CA  1 
ATOM   204  C  C   . GLY A 1 28  ? 20.063  -35.528 -7.811  1.00 19.59 ? 28   GLY A C   1 
ATOM   205  O  O   . GLY A 1 28  ? 19.767  -36.723 -7.756  1.00 22.26 ? 28   GLY A O   1 
ATOM   206  N  N   . THR A 1 29  ? 21.200  -35.102 -8.363  1.00 21.98 ? 29   THR A N   1 
ATOM   207  C  CA  . THR A 1 29  ? 22.122  -36.062 -8.958  1.00 21.71 ? 29   THR A CA  1 
ATOM   208  C  C   . THR A 1 29  ? 22.692  -36.999 -7.900  1.00 24.93 ? 29   THR A C   1 
ATOM   209  O  O   . THR A 1 29  ? 22.612  -38.219 -8.048  1.00 23.02 ? 29   THR A O   1 
ATOM   210  C  CB  . THR A 1 29  ? 23.242  -35.346 -9.705  1.00 24.25 ? 29   THR A CB  1 
ATOM   211  O  OG1 . THR A 1 29  ? 22.698  -34.670 -10.848 1.00 23.32 ? 29   THR A OG1 1 
ATOM   212  C  CG2 . THR A 1 29  ? 24.286  -36.346 -10.171 1.00 26.25 ? 29   THR A CG2 1 
ATOM   213  N  N   . PHE A 1 30  ? 23.259  -36.448 -6.815  1.00 28.61 ? 30   PHE A N   1 
ATOM   214  C  CA  . PHE A 1 30  ? 23.904  -37.300 -5.812  1.00 25.97 ? 30   PHE A CA  1 
ATOM   215  C  C   . PHE A 1 30  ? 22.919  -38.300 -5.216  1.00 30.46 ? 30   PHE A C   1 
ATOM   216  O  O   . PHE A 1 30  ? 23.216  -39.498 -5.116  1.00 30.36 ? 30   PHE A O   1 
ATOM   217  C  CB  . PHE A 1 30  ? 24.548  -36.458 -4.704  1.00 29.23 ? 30   PHE A CB  1 
ATOM   218  C  CG  . PHE A 1 30  ? 25.152  -37.283 -3.587  1.00 31.84 ? 30   PHE A CG  1 
ATOM   219  C  CD1 . PHE A 1 30  ? 24.398  -37.646 -2.483  1.00 35.12 ? 30   PHE A CD1 1 
ATOM   220  C  CD2 . PHE A 1 30  ? 26.468  -37.705 -3.650  1.00 39.31 ? 30   PHE A CD2 1 
ATOM   221  C  CE1 . PHE A 1 30  ? 24.941  -38.403 -1.466  1.00 33.17 ? 30   PHE A CE1 1 
ATOM   222  C  CE2 . PHE A 1 30  ? 27.019  -38.459 -2.631  1.00 37.21 ? 30   PHE A CE2 1 
ATOM   223  C  CZ  . PHE A 1 30  ? 26.251  -38.810 -1.541  1.00 36.58 ? 30   PHE A CZ  1 
ATOM   224  N  N   . HIS A 1 31  ? 21.731  -37.835 -4.824  1.00 23.31 ? 31   HIS A N   1 
ATOM   225  C  CA  . HIS A 1 31  ? 20.824  -38.749 -4.145  1.00 21.41 ? 31   HIS A CA  1 
ATOM   226  C  C   . HIS A 1 31  ? 20.153  -39.701 -5.121  1.00 28.98 ? 31   HIS A C   1 
ATOM   227  O  O   . HIS A 1 31  ? 19.811  -40.827 -4.738  1.00 28.38 ? 31   HIS A O   1 
ATOM   228  C  CB  . HIS A 1 31  ? 19.819  -37.956 -3.306  1.00 23.35 ? 31   HIS A CB  1 
ATOM   229  C  CG  . HIS A 1 31  ? 20.467  -37.215 -2.178  1.00 23.75 ? 31   HIS A CG  1 
ATOM   230  N  ND1 . HIS A 1 31  ? 20.829  -37.830 -0.999  1.00 25.43 ? 31   HIS A ND1 1 
ATOM   231  C  CD2 . HIS A 1 31  ? 20.882  -35.932 -2.074  1.00 23.73 ? 31   HIS A CD2 1 
ATOM   232  C  CE1 . HIS A 1 31  ? 21.418  -36.951 -0.208  1.00 26.68 ? 31   HIS A CE1 1 
ATOM   233  N  NE2 . HIS A 1 31  ? 21.460  -35.791 -0.836  1.00 26.72 ? 31   HIS A NE2 1 
ATOM   234  N  N   . SER A 1 32  ? 20.014  -39.297 -6.387  1.00 24.48 ? 32   SER A N   1 
ATOM   235  C  CA  . SER A 1 32  ? 19.599  -40.238 -7.421  1.00 25.03 ? 32   SER A CA  1 
ATOM   236  C  C   . SER A 1 32  ? 20.657  -41.312 -7.648  1.00 28.14 ? 32   SER A C   1 
ATOM   237  O  O   . SER A 1 32  ? 20.317  -42.490 -7.813  1.00 29.47 ? 32   SER A O   1 
ATOM   238  C  CB  . SER A 1 32  ? 19.299  -39.500 -8.732  1.00 25.83 ? 32   SER A CB  1 
ATOM   239  O  OG  . SER A 1 32  ? 18.018  -38.868 -8.700  1.00 22.47 ? 32   SER A OG  1 
ATOM   240  N  N   . GLN A 1 33  ? 21.939  -40.927 -7.686  1.00 26.54 ? 33   GLN A N   1 
ATOM   241  C  CA  . GLN A 1 33  ? 23.005  -41.926 -7.777  1.00 29.13 ? 33   GLN A CA  1 
ATOM   242  C  C   . GLN A 1 33  ? 22.904  -42.924 -6.632  1.00 37.34 ? 33   GLN A C   1 
ATOM   243  O  O   . GLN A 1 33  ? 22.932  -44.146 -6.844  1.00 38.25 ? 33   GLN A O   1 
ATOM   244  C  CB  . GLN A 1 33  ? 24.378  -41.245 -7.776  1.00 36.93 ? 33   GLN A CB  1 
ATOM   245  C  CG  . GLN A 1 33  ? 24.648  -40.344 -8.986  1.00 38.64 ? 33   GLN A CG  1 
ATOM   246  C  CD  . GLN A 1 33  ? 25.908  -39.484 -8.851  1.00 36.97 ? 33   GLN A CD  1 
ATOM   247  O  OE1 . GLN A 1 33  ? 26.079  -38.724 -7.882  1.00 35.00 ? 33   GLN A OE1 1 
ATOM   248  N  NE2 . GLN A 1 33  ? 26.789  -39.591 -9.839  1.00 39.11 ? 33   GLN A NE2 1 
ATOM   249  N  N   . GLN A 1 34  ? 22.751  -42.414 -5.406  1.00 34.37 ? 34   GLN A N   1 
ATOM   250  C  CA  . GLN A 1 34  ? 22.683  -43.281 -4.235  1.00 32.50 ? 34   GLN A CA  1 
ATOM   251  C  C   . GLN A 1 34  ? 21.471  -44.193 -4.287  1.00 36.70 ? 34   GLN A C   1 
ATOM   252  O  O   . GLN A 1 34  ? 21.551  -45.357 -3.880  1.00 42.91 ? 34   GLN A O   1 
ATOM   253  C  CB  . GLN A 1 34  ? 22.666  -42.441 -2.958  1.00 39.21 ? 34   GLN A CB  1 
ATOM   254  C  CG  . GLN A 1 34  ? 23.971  -41.700 -2.682  1.00 40.54 ? 34   GLN A CG  1 
ATOM   255  C  CD  . GLN A 1 34  ? 25.066  -42.603 -2.138  1.00 43.43 ? 34   GLN A CD  1 
ATOM   256  O  OE1 . GLN A 1 34  ? 25.205  -43.756 -2.548  1.00 46.62 ? 34   GLN A OE1 1 
ATOM   257  N  NE2 . GLN A 1 34  ? 25.853  -42.076 -1.205  1.00 46.16 ? 34   GLN A NE2 1 
ATOM   258  N  N   . ALA A 1 35  ? 20.335  -43.684 -4.776  1.00 32.98 ? 35   ALA A N   1 
ATOM   259  C  CA  . ALA A 1 35  ? 19.147  -44.523 -4.892  1.00 31.87 ? 35   ALA A CA  1 
ATOM   260  C  C   . ALA A 1 35  ? 19.369  -45.655 -5.890  1.00 34.75 ? 35   ALA A C   1 
ATOM   261  O  O   . ALA A 1 35  ? 18.959  -46.795 -5.646  1.00 36.12 ? 35   ALA A O   1 
ATOM   262  C  CB  . ALA A 1 35  ? 17.938  -43.677 -5.289  1.00 29.24 ? 35   ALA A CB  1 
ATOM   263  N  N   . LEU A 1 36  ? 20.031  -45.364 -7.013  1.00 39.99 ? 36   LEU A N   1 
ATOM   264  C  CA  . LEU A 1 36  ? 20.339  -46.411 -7.985  1.00 39.69 ? 36   LEU A CA  1 
ATOM   265  C  C   . LEU A 1 36  ? 21.288  -47.449 -7.391  1.00 38.90 ? 36   LEU A C   1 
ATOM   266  O  O   . LEU A 1 36  ? 21.055  -48.657 -7.507  1.00 39.32 ? 36   LEU A O   1 
ATOM   267  C  CB  . LEU A 1 36  ? 20.927  -45.788 -9.253  1.00 34.65 ? 36   LEU A CB  1 
ATOM   268  C  CG  . LEU A 1 36  ? 19.941  -44.987 -10.110 1.00 32.76 ? 36   LEU A CG  1 
ATOM   269  C  CD1 . LEU A 1 36  ? 20.671  -44.192 -11.177 1.00 32.16 ? 36   LEU A CD1 1 
ATOM   270  C  CD2 . LEU A 1 36  ? 18.875  -45.907 -10.738 1.00 25.15 ? 36   LEU A CD2 1 
ATOM   271  N  N   . GLU A 1 37  ? 22.355  -46.990 -6.727  1.00 43.05 ? 37   GLU A N   1 
ATOM   272  C  CA  . GLU A 1 37  ? 23.288  -47.898 -6.059  1.00 45.28 ? 37   GLU A CA  1 
ATOM   273  C  C   . GLU A 1 37  ? 22.631  -48.700 -4.947  1.00 37.11 ? 37   GLU A C   1 
ATOM   274  O  O   . GLU A 1 37  ? 23.142  -49.758 -4.582  1.00 48.83 ? 37   GLU A O   1 
ATOM   275  C  CB  . GLU A 1 37  ? 24.475  -47.115 -5.492  1.00 45.85 ? 37   GLU A CB  1 
ATOM   276  C  CG  . GLU A 1 37  ? 25.647  -46.986 -6.450  1.00 46.96 ? 37   GLU A CG  1 
ATOM   277  C  CD  . GLU A 1 37  ? 26.662  -45.957 -5.998  1.00 55.17 ? 37   GLU A CD  1 
ATOM   278  O  OE1 . GLU A 1 37  ? 27.097  -45.143 -6.845  1.00 50.09 ? 37   GLU A OE1 1 
ATOM   279  O  OE2 . GLU A 1 37  ? 27.016  -45.957 -4.796  1.00 60.55 ? 37   GLU A OE2 1 
ATOM   280  N  N   . TYR A 1 38  ? 21.514  -48.224 -4.411  1.00 40.81 ? 38   TYR A N   1 
ATOM   281  C  CA  . TYR A 1 38  ? 20.741  -48.891 -3.370  1.00 37.45 ? 38   TYR A CA  1 
ATOM   282  C  C   . TYR A 1 38  ? 19.659  -49.804 -3.942  1.00 44.83 ? 38   TYR A C   1 
ATOM   283  O  O   . TYR A 1 38  ? 18.954  -50.474 -3.174  1.00 39.31 ? 38   TYR A O   1 
ATOM   284  C  CB  . TYR A 1 38  ? 20.114  -47.818 -2.469  1.00 40.66 ? 38   TYR A CB  1 
ATOM   285  C  CG  . TYR A 1 38  ? 19.429  -48.264 -1.191  1.00 43.45 ? 38   TYR A CG  1 
ATOM   286  C  CD1 . TYR A 1 38  ? 18.080  -48.609 -1.184  1.00 35.70 ? 38   TYR A CD1 1 
ATOM   287  C  CD2 . TYR A 1 38  ? 20.111  -48.265 0.023   1.00 37.46 ? 38   TYR A CD2 1 
ATOM   288  C  CE1 . TYR A 1 38  ? 17.443  -48.985 -0.025  1.00 34.54 ? 38   TYR A CE1 1 
ATOM   289  C  CE2 . TYR A 1 38  ? 19.474  -48.639 1.198   1.00 35.42 ? 38   TYR A CE2 1 
ATOM   290  C  CZ  . TYR A 1 38  ? 18.141  -48.991 1.168   1.00 31.69 ? 38   TYR A CZ  1 
ATOM   291  O  OH  . TYR A 1 38  ? 17.490  -49.364 2.320   1.00 28.32 ? 38   TYR A OH  1 
ATOM   292  N  N   . GLY A 1 39  ? 19.507  -49.837 -5.268  1.00 41.52 ? 39   GLY A N   1 
ATOM   293  C  CA  . GLY A 1 39  ? 18.522  -50.684 -5.909  1.00 38.00 ? 39   GLY A CA  1 
ATOM   294  C  C   . GLY A 1 39  ? 17.108  -50.151 -5.943  1.00 37.94 ? 39   GLY A C   1 
ATOM   295  O  O   . GLY A 1 39  ? 16.185  -50.913 -6.242  1.00 33.71 ? 39   GLY A O   1 
ATOM   296  N  N   . THR A 1 40  ? 16.894  -48.868 -5.652  1.00 36.98 ? 40   THR A N   1 
ATOM   297  C  CA  . THR A 1 40  ? 15.540  -48.325 -5.636  1.00 27.05 ? 40   THR A CA  1 
ATOM   298  C  C   . THR A 1 40  ? 15.116  -47.974 -7.065  1.00 21.44 ? 40   THR A C   1 
ATOM   299  O  O   . THR A 1 40  ? 15.941  -47.591 -7.897  1.00 25.20 ? 40   THR A O   1 
ATOM   300  C  CB  . THR A 1 40  ? 15.471  -47.122 -4.675  1.00 31.40 ? 40   THR A CB  1 
ATOM   301  O  OG1 . THR A 1 40  ? 15.121  -47.588 -3.350  1.00 39.52 ? 40   THR A OG1 1 
ATOM   302  C  CG2 . THR A 1 40  ? 14.459  -46.073 -5.110  1.00 26.42 ? 40   THR A CG2 1 
ATOM   303  N  N   . LYS A 1 41  ? 13.831  -48.164 -7.366  1.00 23.17 ? 41   LYS A N   1 
ATOM   304  C  CA  . LYS A 1 41  ? 13.338  -48.111 -8.745  1.00 19.26 ? 41   LYS A CA  1 
ATOM   305  C  C   . LYS A 1 41  ? 13.125  -46.660 -9.187  1.00 23.34 ? 41   LYS A C   1 
ATOM   306  O  O   . LYS A 1 41  ? 12.010  -46.190 -9.439  1.00 18.49 ? 41   LYS A O   1 
ATOM   307  C  CB  . LYS A 1 41  ? 12.068  -48.942 -8.882  1.00 21.35 ? 41   LYS A CB  1 
ATOM   308  C  CG  . LYS A 1 41  ? 12.275  -50.444 -8.591  1.00 18.57 ? 41   LYS A CG  1 
ATOM   309  C  CD  . LYS A 1 41  ? 11.000  -51.248 -8.879  1.00 23.30 ? 41   LYS A CD  1 
ATOM   310  C  CE  . LYS A 1 41  ? 11.200  -52.739 -8.595  1.00 26.52 ? 41   LYS A CE  1 
ATOM   311  N  NZ  . LYS A 1 41  ? 11.432  -53.004 -7.149  1.00 26.86 ? 41   LYS A NZ  1 
ATOM   312  N  N   . LEU A 1 42  ? 14.241  -45.945 -9.281  1.00 20.13 ? 42   LEU A N   1 
ATOM   313  C  CA  . LEU A 1 42  ? 14.257  -44.615 -9.873  1.00 19.45 ? 42   LEU A CA  1 
ATOM   314  C  C   . LEU A 1 42  ? 14.294  -44.754 -11.391 1.00 18.97 ? 42   LEU A C   1 
ATOM   315  O  O   . LEU A 1 42  ? 15.184  -45.415 -11.933 1.00 18.57 ? 42   LEU A O   1 
ATOM   316  C  CB  . LEU A 1 42  ? 15.467  -43.845 -9.361  1.00 19.27 ? 42   LEU A CB  1 
ATOM   317  C  CG  . LEU A 1 42  ? 15.730  -42.518 -10.062 1.00 18.08 ? 42   LEU A CG  1 
ATOM   318  C  CD1 . LEU A 1 42  ? 14.633  -41.554 -9.679  1.00 19.59 ? 42   LEU A CD1 1 
ATOM   319  C  CD2 . LEU A 1 42  ? 17.081  -42.020 -9.643  1.00 21.05 ? 42   LEU A CD2 1 
ATOM   320  N  N   . VAL A 1 43  ? 13.342  -44.137 -12.086 1.00 17.97 ? 43   VAL A N   1 
ATOM   321  C  CA  . VAL A 1 43  ? 13.124  -44.424 -13.501 1.00 18.96 ? 43   VAL A CA  1 
ATOM   322  C  C   . VAL A 1 43  ? 13.288  -43.205 -14.408 1.00 21.43 ? 43   VAL A C   1 
ATOM   323  O  O   . VAL A 1 43  ? 13.122  -43.332 -15.627 1.00 18.20 ? 43   VAL A O   1 
ATOM   324  C  CB  . VAL A 1 43  ? 11.744  -45.074 -13.723 1.00 19.29 ? 43   VAL A CB  1 
ATOM   325  C  CG1 . VAL A 1 43  ? 11.645  -46.393 -12.936 1.00 18.53 ? 43   VAL A CG1 1 
ATOM   326  C  CG2 . VAL A 1 43  ? 10.634  -44.123 -13.318 1.00 18.76 ? 43   VAL A CG2 1 
ATOM   327  N  N   . GLY A 1 44  ? 13.641  -42.050 -13.872 1.00 16.73 ? 44   GLY A N   1 
ATOM   328  C  CA  . GLY A 1 44  ? 13.783  -40.852 -14.669 1.00 16.05 ? 44   GLY A CA  1 
ATOM   329  C  C   . GLY A 1 44  ? 13.557  -39.650 -13.780 1.00 17.37 ? 44   GLY A C   1 
ATOM   330  O  O   . GLY A 1 44  ? 13.440  -39.784 -12.574 1.00 19.51 ? 44   GLY A O   1 
ATOM   331  N  N   . GLY A 1 45  ? 13.494  -38.474 -14.397 1.00 15.88 ? 45   GLY A N   1 
ATOM   332  C  CA  . GLY A 1 45  ? 13.393  -37.260 -13.599 1.00 17.74 ? 45   GLY A CA  1 
ATOM   333  C  C   . GLY A 1 45  ? 13.086  -36.056 -14.460 1.00 16.14 ? 45   GLY A C   1 
ATOM   334  O  O   . GLY A 1 45  ? 13.040  -36.138 -15.693 1.00 16.07 ? 45   GLY A O   1 
ATOM   335  N  N   . THR A 1 46  ? 12.855  -34.924 -13.797 1.00 15.92 ? 46   THR A N   1 
ATOM   336  C  CA  . THR A 1 46  ? 12.499  -33.712 -14.523 1.00 14.62 ? 46   THR A CA  1 
ATOM   337  C  C   . THR A 1 46  ? 13.519  -32.612 -14.277 1.00 16.27 ? 46   THR A C   1 
ATOM   338  O  O   . THR A 1 46  ? 14.028  -32.441 -13.164 1.00 18.53 ? 46   THR A O   1 
ATOM   339  C  CB  . THR A 1 46  ? 11.071  -33.191 -14.194 1.00 15.54 ? 46   THR A CB  1 
ATOM   340  O  OG1 . THR A 1 46  ? 10.980  -32.763 -12.836 1.00 16.59 ? 46   THR A OG1 1 
ATOM   341  C  CG2 . THR A 1 46  ? 9.998   -34.252 -14.481 1.00 17.22 ? 46   THR A CG2 1 
ATOM   342  N  N   . THR A 1 47  ? 13.842  -31.915 -15.347 1.00 18.40 ? 47   THR A N   1 
ATOM   343  C  CA  . THR A 1 47  ? 14.443  -30.592 -15.317 1.00 15.80 ? 47   THR A CA  1 
ATOM   344  C  C   . THR A 1 47  ? 13.907  -29.814 -16.516 1.00 20.74 ? 47   THR A C   1 
ATOM   345  O  O   . THR A 1 47  ? 14.222  -30.148 -17.674 1.00 19.65 ? 47   THR A O   1 
ATOM   346  C  CB  . THR A 1 47  ? 15.965  -30.638 -15.373 1.00 18.47 ? 47   THR A CB  1 
ATOM   347  O  OG1 . THR A 1 47  ? 16.485  -31.536 -14.383 1.00 20.76 ? 47   THR A OG1 1 
ATOM   348  C  CG2 . THR A 1 47  ? 16.529  -29.230 -15.152 1.00 24.91 ? 47   THR A CG2 1 
ATOM   349  N  N   . PRO A 1 48  ? 13.101  -28.782 -16.279 1.00 20.40 ? 48   PRO A N   1 
ATOM   350  C  CA  . PRO A 1 48  ? 12.583  -27.966 -17.385 1.00 24.33 ? 48   PRO A CA  1 
ATOM   351  C  C   . PRO A 1 48  ? 13.713  -27.456 -18.266 1.00 26.12 ? 48   PRO A C   1 
ATOM   352  O  O   . PRO A 1 48  ? 14.696  -26.903 -17.779 1.00 22.40 ? 48   PRO A O   1 
ATOM   353  C  CB  . PRO A 1 48  ? 11.864  -26.818 -16.664 1.00 27.42 ? 48   PRO A CB  1 
ATOM   354  C  CG  . PRO A 1 48  ? 11.473  -27.407 -15.318 1.00 22.51 ? 48   PRO A CG  1 
ATOM   355  C  CD  . PRO A 1 48  ? 12.645  -28.293 -14.963 1.00 23.53 ? 48   PRO A CD  1 
ATOM   356  N  N   . GLY A 1 49  ? 13.562  -27.642 -19.577 1.00 28.08 ? 49   GLY A N   1 
ATOM   357  C  CA  . GLY A 1 49  ? 14.589  -27.237 -20.520 1.00 27.14 ? 49   GLY A CA  1 
ATOM   358  C  C   . GLY A 1 49  ? 15.667  -28.271 -20.765 1.00 29.94 ? 49   GLY A C   1 
ATOM   359  O  O   . GLY A 1 49  ? 16.674  -27.957 -21.417 1.00 29.48 ? 49   GLY A O   1 
ATOM   360  N  N   . LYS A 1 50  ? 15.489  -29.499 -20.268 1.00 24.44 ? 50   LYS A N   1 
ATOM   361  C  CA  . LYS A 1 50  ? 16.469  -30.547 -20.493 1.00 21.61 ? 50   LYS A CA  1 
ATOM   362  C  C   . LYS A 1 50  ? 15.803  -31.850 -20.909 1.00 20.24 ? 50   LYS A C   1 
ATOM   363  O  O   . LYS A 1 50  ? 16.470  -32.895 -20.915 1.00 22.86 ? 50   LYS A O   1 
ATOM   364  C  CB  . LYS A 1 50  ? 17.345  -30.751 -19.248 1.00 25.21 ? 50   LYS A CB  1 
ATOM   365  C  CG  . LYS A 1 50  ? 18.315  -29.611 -18.977 1.00 25.44 ? 50   LYS A CG  1 
ATOM   366  C  CD  . LYS A 1 50  ? 19.327  -29.963 -17.879 1.00 25.43 ? 50   LYS A CD  1 
ATOM   367  C  CE  . LYS A 1 50  ? 20.434  -28.912 -17.820 1.00 25.54 ? 50   LYS A CE  1 
ATOM   368  N  NZ  . LYS A 1 50  ? 21.415  -29.156 -16.735 1.00 28.26 ? 50   LYS A NZ  1 
ATOM   369  N  N   . GLY A 1 51  ? 14.514  -31.822 -21.244 1.00 18.35 ? 51   GLY A N   1 
ATOM   370  C  CA  . GLY A 1 51  ? 13.842  -33.002 -21.744 1.00 22.15 ? 51   GLY A CA  1 
ATOM   371  C  C   . GLY A 1 51  ? 14.538  -33.586 -22.962 1.00 24.60 ? 51   GLY A C   1 
ATOM   372  O  O   . GLY A 1 51  ? 14.848  -32.860 -23.913 1.00 21.45 ? 51   GLY A O   1 
ATOM   373  N  N   . GLY A 1 52  ? 14.795  -34.896 -22.936 1.00 20.39 ? 52   GLY A N   1 
ATOM   374  C  CA  . GLY A 1 52  ? 15.454  -35.600 -24.017 1.00 19.65 ? 52   GLY A CA  1 
ATOM   375  C  C   . GLY A 1 52  ? 16.859  -36.043 -23.692 1.00 19.81 ? 52   GLY A C   1 
ATOM   376  O  O   . GLY A 1 52  ? 17.382  -36.937 -24.363 1.00 23.00 ? 52   GLY A O   1 
ATOM   377  N  N   . GLN A 1 53  ? 17.489  -35.439 -22.688 1.00 16.29 ? 53   GLN A N   1 
ATOM   378  C  CA  . GLN A 1 53  ? 18.800  -35.878 -22.256 1.00 19.40 ? 53   GLN A CA  1 
ATOM   379  C  C   . GLN A 1 53  ? 18.687  -37.166 -21.453 1.00 21.79 ? 53   GLN A C   1 
ATOM   380  O  O   . GLN A 1 53  ? 17.597  -37.626 -21.104 1.00 23.30 ? 53   GLN A O   1 
ATOM   381  C  CB  . GLN A 1 53  ? 19.486  -34.800 -21.419 1.00 17.40 ? 53   GLN A CB  1 
ATOM   382  C  CG  . GLN A 1 53  ? 19.725  -33.517 -22.183 1.00 18.84 ? 53   GLN A CG  1 
ATOM   383  C  CD  . GLN A 1 53  ? 20.315  -32.424 -21.324 1.00 21.29 ? 53   GLN A CD  1 
ATOM   384  O  OE1 . GLN A 1 53  ? 20.490  -32.587 -20.118 1.00 20.68 ? 53   GLN A OE1 1 
ATOM   385  N  NE2 . GLN A 1 53  ? 20.639  -31.301 -21.948 1.00 23.55 ? 53   GLN A NE2 1 
ATOM   386  N  N   . THR A 1 54  ? 19.842  -37.742 -21.153 1.00 19.22 ? 54   THR A N   1 
ATOM   387  C  CA  . THR A 1 54  ? 19.940  -38.914 -20.302 1.00 22.32 ? 54   THR A CA  1 
ATOM   388  C  C   . THR A 1 54  ? 20.877  -38.581 -19.154 1.00 25.68 ? 54   THR A C   1 
ATOM   389  O  O   . THR A 1 54  ? 21.939  -37.985 -19.360 1.00 23.37 ? 54   THR A O   1 
ATOM   390  C  CB  . THR A 1 54  ? 20.445  -40.139 -21.089 1.00 25.56 ? 54   THR A CB  1 
ATOM   391  O  OG1 . THR A 1 54  ? 19.724  -40.233 -22.321 1.00 22.19 ? 54   THR A OG1 1 
ATOM   392  C  CG2 . THR A 1 54  ? 20.214  -41.423 -20.300 1.00 23.27 ? 54   THR A CG2 1 
ATOM   393  N  N   . HIS A 1 55  ? 20.471  -38.965 -17.945 1.00 23.10 ? 55   HIS A N   1 
ATOM   394  C  CA  . HIS A 1 55  ? 21.195  -38.640 -16.724 1.00 24.43 ? 55   HIS A CA  1 
ATOM   395  C  C   . HIS A 1 55  ? 21.197  -39.898 -15.870 1.00 26.04 ? 55   HIS A C   1 
ATOM   396  O  O   . HIS A 1 55  ? 20.127  -40.456 -15.590 1.00 21.32 ? 55   HIS A O   1 
ATOM   397  C  CB  . HIS A 1 55  ? 20.522  -37.466 -15.996 1.00 23.88 ? 55   HIS A CB  1 
ATOM   398  C  CG  . HIS A 1 55  ? 21.297  -36.925 -14.831 1.00 26.07 ? 55   HIS A CG  1 
ATOM   399  N  ND1 . HIS A 1 55  ? 22.646  -36.640 -14.893 1.00 22.46 ? 55   HIS A ND1 1 
ATOM   400  C  CD2 . HIS A 1 55  ? 20.894  -36.569 -13.586 1.00 20.47 ? 55   HIS A CD2 1 
ATOM   401  C  CE1 . HIS A 1 55  ? 23.045  -36.149 -13.730 1.00 25.22 ? 55   HIS A CE1 1 
ATOM   402  N  NE2 . HIS A 1 55  ? 22.001  -36.096 -12.919 1.00 25.15 ? 55   HIS A NE2 1 
ATOM   403  N  N   . LEU A 1 56  ? 22.395  -40.364 -15.499 1.00 20.97 ? 56   LEU A N   1 
ATOM   404  C  CA  . LEU A 1 56  ? 22.568  -41.605 -14.741 1.00 25.53 ? 56   LEU A CA  1 
ATOM   405  C  C   . LEU A 1 56  ? 21.962  -42.798 -15.470 1.00 24.84 ? 56   LEU A C   1 
ATOM   406  O  O   . LEU A 1 56  ? 21.488  -43.742 -14.839 1.00 24.88 ? 56   LEU A O   1 
ATOM   407  C  CB  . LEU A 1 56  ? 21.966  -41.486 -13.337 1.00 27.95 ? 56   LEU A CB  1 
ATOM   408  C  CG  . LEU A 1 56  ? 22.303  -40.196 -12.598 1.00 22.58 ? 56   LEU A CG  1 
ATOM   409  C  CD1 . LEU A 1 56  ? 21.640  -40.205 -11.233 1.00 23.76 ? 56   LEU A CD1 1 
ATOM   410  C  CD2 . LEU A 1 56  ? 23.812  -40.046 -12.473 1.00 24.42 ? 56   LEU A CD2 1 
ATOM   411  N  N   . GLY A 1 57  ? 21.958  -42.748 -16.802 1.00 25.77 ? 57   GLY A N   1 
ATOM   412  C  CA  . GLY A 1 57  ? 21.370  -43.791 -17.616 1.00 27.10 ? 57   GLY A CA  1 
ATOM   413  C  C   . GLY A 1 57  ? 19.867  -43.735 -17.730 1.00 25.35 ? 57   GLY A C   1 
ATOM   414  O  O   . GLY A 1 57  ? 19.273  -44.650 -18.306 1.00 23.86 ? 57   GLY A O   1 
ATOM   415  N  N   . LEU A 1 58  ? 19.232  -42.695 -17.194 1.00 20.74 ? 58   LEU A N   1 
ATOM   416  C  CA  . LEU A 1 58  ? 17.790  -42.561 -17.132 1.00 19.44 ? 58   LEU A CA  1 
ATOM   417  C  C   . LEU A 1 58  ? 17.314  -41.361 -17.940 1.00 19.89 ? 58   LEU A C   1 
ATOM   418  O  O   . LEU A 1 58  ? 18.051  -40.382 -18.103 1.00 22.44 ? 58   LEU A O   1 
ATOM   419  C  CB  . LEU A 1 58  ? 17.330  -42.392 -15.680 1.00 20.33 ? 58   LEU A CB  1 
ATOM   420  C  CG  . LEU A 1 58  ? 17.752  -43.498 -14.726 1.00 20.44 ? 58   LEU A CG  1 
ATOM   421  C  CD1 . LEU A 1 58  ? 17.276  -43.160 -13.324 1.00 18.99 ? 58   LEU A CD1 1 
ATOM   422  C  CD2 . LEU A 1 58  ? 17.143  -44.793 -15.200 1.00 21.48 ? 58   LEU A CD2 1 
ATOM   423  N  N   . PRO A 1 59  ? 16.077  -41.394 -18.435 1.00 20.52 ? 59   PRO A N   1 
ATOM   424  C  CA  . PRO A 1 59  ? 15.581  -40.279 -19.247 1.00 20.70 ? 59   PRO A CA  1 
ATOM   425  C  C   . PRO A 1 59  ? 15.279  -39.042 -18.415 1.00 22.79 ? 59   PRO A C   1 
ATOM   426  O  O   . PRO A 1 59  ? 14.806  -39.134 -17.280 1.00 18.34 ? 59   PRO A O   1 
ATOM   427  C  CB  . PRO A 1 59  ? 14.299  -40.844 -19.863 1.00 17.82 ? 59   PRO A CB  1 
ATOM   428  C  CG  . PRO A 1 59  ? 13.827  -41.832 -18.862 1.00 17.57 ? 59   PRO A CG  1 
ATOM   429  C  CD  . PRO A 1 59  ? 15.085  -42.479 -18.346 1.00 20.50 ? 59   PRO A CD  1 
ATOM   430  N  N   . VAL A 1 60  ? 15.539  -37.877 -19.006 1.00 17.28 ? 60   VAL A N   1 
ATOM   431  C  CA  . VAL A 1 60  ? 15.180  -36.585 -18.434 1.00 18.62 ? 60   VAL A CA  1 
ATOM   432  C  C   . VAL A 1 60  ? 14.004  -36.041 -19.230 1.00 19.93 ? 60   VAL A C   1 
ATOM   433  O  O   . VAL A 1 60  ? 13.995  -36.104 -20.465 1.00 20.55 ? 60   VAL A O   1 
ATOM   434  C  CB  . VAL A 1 60  ? 16.362  -35.590 -18.465 1.00 18.74 ? 60   VAL A CB  1 
ATOM   435  C  CG1 . VAL A 1 60  ? 15.964  -34.236 -17.839 1.00 18.48 ? 60   VAL A CG1 1 
ATOM   436  C  CG2 . VAL A 1 60  ? 17.550  -36.171 -17.767 1.00 21.28 ? 60   VAL A CG2 1 
ATOM   437  N  N   . PHE A 1 61  ? 13.027  -35.488 -18.524 1.00 17.05 ? 61   PHE A N   1 
ATOM   438  C  CA  . PHE A 1 61  ? 11.821  -34.945 -19.116 1.00 16.06 ? 61   PHE A CA  1 
ATOM   439  C  C   . PHE A 1 61  ? 11.666  -33.481 -18.727 1.00 18.48 ? 61   PHE A C   1 
ATOM   440  O  O   . PHE A 1 61  ? 12.200  -33.030 -17.706 1.00 19.15 ? 61   PHE A O   1 
ATOM   441  C  CB  . PHE A 1 61  ? 10.575  -35.724 -18.656 1.00 21.16 ? 61   PHE A CB  1 
ATOM   442  C  CG  . PHE A 1 61  ? 10.679  -37.218 -18.834 1.00 17.93 ? 61   PHE A CG  1 
ATOM   443  C  CD1 . PHE A 1 61  ? 11.242  -38.014 -17.852 1.00 18.51 ? 61   PHE A CD1 1 
ATOM   444  C  CD2 . PHE A 1 61  ? 10.192  -37.824 -19.980 1.00 20.98 ? 61   PHE A CD2 1 
ATOM   445  C  CE1 . PHE A 1 61  ? 11.323  -39.400 -18.017 1.00 19.03 ? 61   PHE A CE1 1 
ATOM   446  C  CE2 . PHE A 1 61  ? 10.272  -39.205 -20.155 1.00 17.30 ? 61   PHE A CE2 1 
ATOM   447  C  CZ  . PHE A 1 61  ? 10.825  -39.997 -19.169 1.00 15.80 ? 61   PHE A CZ  1 
ATOM   448  N  N   . ASN A 1 62  ? 10.907  -32.747 -19.547 1.00 15.35 ? 62   ASN A N   1 
ATOM   449  C  CA  . ASN A 1 62  ? 10.567  -31.365 -19.219 1.00 19.90 ? 62   ASN A CA  1 
ATOM   450  C  C   . ASN A 1 62  ? 9.459   -31.260 -18.173 1.00 19.78 ? 62   ASN A C   1 
ATOM   451  O  O   . ASN A 1 62  ? 9.472   -30.328 -17.363 1.00 21.22 ? 62   ASN A O   1 
ATOM   452  C  CB  . ASN A 1 62  ? 10.149  -30.604 -20.477 1.00 21.78 ? 62   ASN A CB  1 
ATOM   453  C  CG  . ASN A 1 62  ? 11.301  -30.409 -21.437 1.00 22.03 ? 62   ASN A CG  1 
ATOM   454  O  OD1 . ASN A 1 62  ? 12.383  -29.973 -21.042 1.00 21.98 ? 62   ASN A OD1 1 
ATOM   455  N  ND2 . ASN A 1 62  ? 11.090  -30.774 -22.694 1.00 23.62 ? 62   ASN A ND2 1 
ATOM   456  N  N   . THR A 1 63  ? 8.498   -32.179 -18.165 1.00 18.83 ? 63   THR A N   1 
ATOM   457  C  CA  . THR A 1 63  ? 7.340   -32.049 -17.289 1.00 18.73 ? 63   THR A CA  1 
ATOM   458  C  C   . THR A 1 63  ? 7.077   -33.358 -16.548 1.00 17.82 ? 63   THR A C   1 
ATOM   459  O  O   . THR A 1 63  ? 7.461   -34.450 -16.982 1.00 14.84 ? 63   THR A O   1 
ATOM   460  C  CB  . THR A 1 63  ? 6.063   -31.624 -18.059 1.00 17.17 ? 63   THR A CB  1 
ATOM   461  O  OG1 . THR A 1 63  ? 5.566   -32.720 -18.837 1.00 20.91 ? 63   THR A OG1 1 
ATOM   462  C  CG2 . THR A 1 63  ? 6.330   -30.434 -18.996 1.00 20.30 ? 63   THR A CG2 1 
ATOM   463  N  N   . VAL A 1 64  ? 6.393   -33.232 -15.408 1.00 19.54 ? 64   VAL A N   1 
ATOM   464  C  CA  . VAL A 1 64  ? 6.019   -34.420 -14.644 1.00 14.72 ? 64   VAL A CA  1 
ATOM   465  C  C   . VAL A 1 64  ? 5.028   -35.257 -15.440 1.00 17.32 ? 64   VAL A C   1 
ATOM   466  O  O   . VAL A 1 64  ? 5.111   -36.491 -15.461 1.00 17.43 ? 64   VAL A O   1 
ATOM   467  C  CB  . VAL A 1 64  ? 5.456   -34.018 -13.267 1.00 14.18 ? 64   VAL A CB  1 
ATOM   468  C  CG1 . VAL A 1 64  ? 4.878   -35.244 -12.541 1.00 15.77 ? 64   VAL A CG1 1 
ATOM   469  C  CG2 . VAL A 1 64  ? 6.550   -33.340 -12.425 1.00 14.35 ? 64   VAL A CG2 1 
ATOM   470  N  N   . LYS A 1 65  ? 4.092   -34.596 -16.128 1.00 18.26 ? 65   LYS A N   1 
ATOM   471  C  CA  . LYS A 1 65  ? 3.084   -35.322 -16.897 1.00 18.94 ? 65   LYS A CA  1 
ATOM   472  C  C   . LYS A 1 65  ? 3.740   -36.245 -17.924 1.00 18.70 ? 65   LYS A C   1 
ATOM   473  O  O   . LYS A 1 65  ? 3.372   -37.418 -18.043 1.00 19.62 ? 65   LYS A O   1 
ATOM   474  C  CB  . LYS A 1 65  ? 2.128   -34.325 -17.563 1.00 16.54 ? 65   LYS A CB  1 
ATOM   475  C  CG  . LYS A 1 65  ? 1.079   -34.932 -18.515 1.00 23.15 ? 65   LYS A CG  1 
ATOM   476  C  CD  . LYS A 1 65  ? 0.212   -33.822 -19.140 1.00 25.65 ? 65   LYS A CD  1 
ATOM   477  C  CE  . LYS A 1 65  ? -0.422  -34.233 -20.491 1.00 31.49 ? 65   LYS A CE  1 
ATOM   478  N  NZ  . LYS A 1 65  ? -1.152  -35.525 -20.434 1.00 31.68 ? 65   LYS A NZ  1 
ATOM   479  N  N   . GLU A 1 66  ? 4.737   -35.736 -18.654 1.00 16.27 ? 66   GLU A N   1 
ATOM   480  C  CA  . GLU A 1 66  ? 5.458   -36.567 -19.614 1.00 16.90 ? 66   GLU A CA  1 
ATOM   481  C  C   . GLU A 1 66  ? 6.203   -37.690 -18.913 1.00 20.17 ? 66   GLU A C   1 
ATOM   482  O  O   . GLU A 1 66  ? 6.143   -38.846 -19.347 1.00 20.50 ? 66   GLU A O   1 
ATOM   483  C  CB  . GLU A 1 66  ? 6.435   -35.720 -20.435 1.00 20.16 ? 66   GLU A CB  1 
ATOM   484  C  CG  . GLU A 1 66  ? 5.771   -34.835 -21.474 1.00 22.48 ? 66   GLU A CG  1 
ATOM   485  C  CD  . GLU A 1 66  ? 6.744   -33.835 -22.074 1.00 30.46 ? 66   GLU A CD  1 
ATOM   486  O  OE1 . GLU A 1 66  ? 6.516   -33.387 -23.224 1.00 40.27 ? 66   GLU A OE1 1 
ATOM   487  O  OE2 . GLU A 1 66  ? 7.740   -33.500 -21.389 1.00 33.71 ? 66   GLU A OE2 1 
ATOM   488  N  N   . ALA A 1 67  ? 6.933   -37.356 -17.838 1.00 17.82 ? 67   ALA A N   1 
ATOM   489  C  CA  . ALA A 1 67  ? 7.667   -38.348 -17.060 1.00 14.62 ? 67   ALA A CA  1 
ATOM   490  C  C   . ALA A 1 67  ? 6.760   -39.481 -16.616 1.00 16.96 ? 67   ALA A C   1 
ATOM   491  O  O   . ALA A 1 67  ? 7.100   -40.661 -16.763 1.00 19.56 ? 67   ALA A O   1 
ATOM   492  C  CB  . ALA A 1 67  ? 8.321   -37.681 -15.840 1.00 16.55 ? 67   ALA A CB  1 
ATOM   493  N  N   . LYS A 1 68  ? 5.580   -39.134 -16.093 1.00 16.16 ? 68   LYS A N   1 
ATOM   494  C  CA  . LYS A 1 68  ? 4.663   -40.149 -15.582 1.00 20.63 ? 68   LYS A CA  1 
ATOM   495  C  C   . LYS A 1 68  ? 4.114   -41.020 -16.707 1.00 19.29 ? 68   LYS A C   1 
ATOM   496  O  O   . LYS A 1 68  ? 4.056   -42.251 -16.574 1.00 18.83 ? 68   LYS A O   1 
ATOM   497  C  CB  . LYS A 1 68  ? 3.516   -39.482 -14.830 1.00 18.16 ? 68   LYS A CB  1 
ATOM   498  C  CG  . LYS A 1 68  ? 2.553   -40.467 -14.170 1.00 17.09 ? 68   LYS A CG  1 
ATOM   499  C  CD  . LYS A 1 68  ? 1.341   -39.733 -13.629 1.00 19.65 ? 68   LYS A CD  1 
ATOM   500  C  CE  . LYS A 1 68  ? 0.500   -40.620 -12.740 1.00 21.10 ? 68   LYS A CE  1 
ATOM   501  N  NZ  . LYS A 1 68  ? -0.094  -41.756 -13.501 1.00 20.89 ? 68   LYS A NZ  1 
ATOM   502  N  N   . GLU A 1 69  ? 3.702   -40.390 -17.817 1.00 19.62 ? 69   GLU A N   1 
ATOM   503  C  CA  . GLU A 1 69  ? 3.139   -41.136 -18.942 1.00 18.96 ? 69   GLU A CA  1 
ATOM   504  C  C   . GLU A 1 69  ? 4.143   -42.114 -19.531 1.00 16.85 ? 69   GLU A C   1 
ATOM   505  O  O   . GLU A 1 69  ? 3.770   -43.201 -19.977 1.00 22.57 ? 69   GLU A O   1 
ATOM   506  C  CB  . GLU A 1 69  ? 2.662   -40.176 -20.030 1.00 18.22 ? 69   GLU A CB  1 
ATOM   507  C  CG  . GLU A 1 69  ? 1.456   -39.319 -19.652 1.00 22.29 ? 69   GLU A CG  1 
ATOM   508  C  CD  . GLU A 1 69  ? 1.217   -38.184 -20.647 1.00 30.50 ? 69   GLU A CD  1 
ATOM   509  O  OE1 . GLU A 1 69  ? 0.065   -37.714 -20.741 1.00 31.57 ? 69   GLU A OE1 1 
ATOM   510  O  OE2 . GLU A 1 69  ? 2.183   -37.757 -21.333 1.00 30.77 ? 69   GLU A OE2 1 
ATOM   511  N  N   . GLN A 1 70  ? 5.416   -41.741 -19.569 1.00 18.81 ? 70   GLN A N   1 
ATOM   512  C  CA  . GLN A 1 70  ? 6.429   -42.539 -20.250 1.00 19.02 ? 70   GLN A CA  1 
ATOM   513  C  C   . GLN A 1 70  ? 7.136   -43.545 -19.345 1.00 22.49 ? 70   GLN A C   1 
ATOM   514  O  O   . GLN A 1 70  ? 7.772   -44.474 -19.865 1.00 18.85 ? 70   GLN A O   1 
ATOM   515  C  CB  . GLN A 1 70  ? 7.449   -41.610 -20.922 1.00 22.24 ? 70   GLN A CB  1 
ATOM   516  C  CG  . GLN A 1 70  ? 6.771   -40.745 -22.001 1.00 23.18 ? 70   GLN A CG  1 
ATOM   517  C  CD  . GLN A 1 70  ? 7.710   -39.849 -22.780 1.00 26.85 ? 70   GLN A CD  1 
ATOM   518  O  OE1 . GLN A 1 70  ? 8.829   -40.232 -23.118 1.00 28.62 ? 70   GLN A OE1 1 
ATOM   519  N  NE2 . GLN A 1 70  ? 7.241   -38.641 -23.089 1.00 28.50 ? 70   GLN A NE2 1 
ATOM   520  N  N   . THR A 1 71  ? 7.002   -43.424 -18.014 1.00 22.69 ? 71   THR A N   1 
ATOM   521  C  CA  . THR A 1 71  ? 7.640   -44.351 -17.083 1.00 21.17 ? 71   THR A CA  1 
ATOM   522  C  C   . THR A 1 71  ? 6.674   -45.098 -16.177 1.00 20.76 ? 71   THR A C   1 
ATOM   523  O  O   . THR A 1 71  ? 7.077   -46.100 -15.582 1.00 20.59 ? 71   THR A O   1 
ATOM   524  C  CB  . THR A 1 71  ? 8.645   -43.628 -16.171 1.00 18.99 ? 71   THR A CB  1 
ATOM   525  O  OG1 . THR A 1 71  ? 7.938   -42.753 -15.284 1.00 18.08 ? 71   THR A OG1 1 
ATOM   526  C  CG2 . THR A 1 71  ? 9.662   -42.820 -16.982 1.00 19.01 ? 71   THR A CG2 1 
ATOM   527  N  N   . GLY A 1 72  ? 5.431   -44.638 -16.029 1.00 21.60 ? 72   GLY A N   1 
ATOM   528  C  CA  . GLY A 1 72  ? 4.562   -45.284 -15.064 1.00 22.46 ? 72   GLY A CA  1 
ATOM   529  C  C   . GLY A 1 72  ? 4.924   -45.001 -13.623 1.00 21.15 ? 72   GLY A C   1 
ATOM   530  O  O   . GLY A 1 72  ? 4.487   -45.726 -12.721 1.00 20.02 ? 72   GLY A O   1 
ATOM   531  N  N   . ALA A 1 73  ? 5.709   -43.958 -13.380 1.00 19.46 ? 73   ALA A N   1 
ATOM   532  C  CA  . ALA A 1 73  ? 6.100   -43.611 -12.016 1.00 18.28 ? 73   ALA A CA  1 
ATOM   533  C  C   . ALA A 1 73  ? 4.878   -43.356 -11.145 1.00 19.59 ? 73   ALA A C   1 
ATOM   534  O  O   . ALA A 1 73  ? 3.878   -42.793 -11.592 1.00 19.93 ? 73   ALA A O   1 
ATOM   535  C  CB  . ALA A 1 73  ? 6.996   -42.376 -12.023 1.00 20.27 ? 73   ALA A CB  1 
ATOM   536  N  N   . THR A 1 74  ? 4.956   -43.793 -9.895  1.00 14.70 ? 74   THR A N   1 
ATOM   537  C  CA  . THR A 1 74  ? 3.907   -43.537 -8.923  1.00 18.47 ? 74   THR A CA  1 
ATOM   538  C  C   . THR A 1 74  ? 4.368   -42.646 -7.771  1.00 19.60 ? 74   THR A C   1 
ATOM   539  O  O   . THR A 1 74  ? 3.593   -42.413 -6.836  1.00 19.49 ? 74   THR A O   1 
ATOM   540  C  CB  . THR A 1 74  ? 3.386   -44.866 -8.376  1.00 15.99 ? 74   THR A CB  1 
ATOM   541  O  OG1 . THR A 1 74  ? 4.491   -45.601 -7.845  1.00 21.39 ? 74   THR A OG1 1 
ATOM   542  C  CG2 . THR A 1 74  ? 2.715   -45.674 -9.506  1.00 18.55 ? 74   THR A CG2 1 
ATOM   543  N  N   . ALA A 1 75  ? 5.609   -42.164 -7.799  1.00 18.84 ? 75   ALA A N   1 
ATOM   544  C  CA  . ALA A 1 75  ? 6.117   -41.285 -6.756  1.00 13.10 ? 75   ALA A CA  1 
ATOM   545  C  C   . ALA A 1 75  ? 7.139   -40.336 -7.354  1.00 17.52 ? 75   ALA A C   1 
ATOM   546  O  O   . ALA A 1 75  ? 7.809   -40.656 -8.342  1.00 15.52 ? 75   ALA A O   1 
ATOM   547  C  CB  . ALA A 1 75  ? 6.761   -42.065 -5.608  1.00 13.98 ? 75   ALA A CB  1 
ATOM   548  N  N   . SER A 1 76  ? 7.251   -39.159 -6.749  1.00 11.33 ? 76   SER A N   1 
ATOM   549  C  CA  . SER A 1 76  ? 8.251   -38.188 -7.153  1.00 12.51 ? 76   SER A CA  1 
ATOM   550  C  C   . SER A 1 76  ? 8.946   -37.645 -5.912  1.00 13.94 ? 76   SER A C   1 
ATOM   551  O  O   . SER A 1 76  ? 8.340   -37.538 -4.838  1.00 16.15 ? 76   SER A O   1 
ATOM   552  C  CB  . SER A 1 76  ? 7.610   -37.054 -7.957  1.00 16.27 ? 76   SER A CB  1 
ATOM   553  O  OG  . SER A 1 76  ? 8.581   -36.087 -8.301  1.00 22.79 ? 76   SER A OG  1 
ATOM   554  N  N   . VAL A 1 77  ? 10.239  -37.364 -6.043  1.00 13.90 ? 77   VAL A N   1 
ATOM   555  C  CA  . VAL A 1 77  ? 11.019  -36.746 -4.975  1.00 14.11 ? 77   VAL A CA  1 
ATOM   556  C  C   . VAL A 1 77  ? 11.571  -35.426 -5.510  1.00 16.85 ? 77   VAL A C   1 
ATOM   557  O  O   . VAL A 1 77  ? 12.032  -35.344 -6.657  1.00 15.49 ? 77   VAL A O   1 
ATOM   558  C  CB  . VAL A 1 77  ? 12.130  -37.688 -4.445  1.00 16.87 ? 77   VAL A CB  1 
ATOM   559  C  CG1 . VAL A 1 77  ? 13.288  -37.876 -5.461  1.00 17.44 ? 77   VAL A CG1 1 
ATOM   560  C  CG2 . VAL A 1 77  ? 12.648  -37.232 -3.072  1.00 15.68 ? 77   VAL A CG2 1 
ATOM   561  N  N   . ILE A 1 78  ? 11.486  -34.379 -4.693  1.00 14.57 ? 78   ILE A N   1 
ATOM   562  C  CA  . ILE A 1 78  ? 11.715  -33.012 -5.150  1.00 15.54 ? 78   ILE A CA  1 
ATOM   563  C  C   . ILE A 1 78  ? 13.004  -32.485 -4.540  1.00 15.45 ? 78   ILE A C   1 
ATOM   564  O  O   . ILE A 1 78  ? 13.136  -32.404 -3.312  1.00 14.45 ? 78   ILE A O   1 
ATOM   565  C  CB  . ILE A 1 78  ? 10.528  -32.103 -4.814  1.00 16.34 ? 78   ILE A CB  1 
ATOM   566  C  CG1 . ILE A 1 78  ? 9.308   -32.589 -5.583  1.00 16.40 ? 78   ILE A CG1 1 
ATOM   567  C  CG2 . ILE A 1 78  ? 10.860  -30.626 -5.158  1.00 14.81 ? 78   ILE A CG2 1 
ATOM   568  C  CD1 . ILE A 1 78  ? 8.052   -31.741 -5.384  1.00 16.40 ? 78   ILE A CD1 1 
ATOM   569  N  N   . TYR A 1 79  ? 13.963  -32.143 -5.409  1.00 13.53 ? 79   TYR A N   1 
ATOM   570  C  CA  . TYR A 1 79  ? 15.217  -31.537 -4.988  1.00 16.45 ? 79   TYR A CA  1 
ATOM   571  C  C   . TYR A 1 79  ? 15.358  -30.188 -5.694  1.00 18.64 ? 79   TYR A C   1 
ATOM   572  O  O   . TYR A 1 79  ? 16.417  -29.860 -6.246  1.00 17.93 ? 79   TYR A O   1 
ATOM   573  C  CB  . TYR A 1 79  ? 16.392  -32.471 -5.285  1.00 15.75 ? 79   TYR A CB  1 
ATOM   574  C  CG  . TYR A 1 79  ? 16.461  -33.726 -4.419  1.00 15.41 ? 79   TYR A CG  1 
ATOM   575  C  CD1 . TYR A 1 79  ? 17.055  -33.699 -3.164  1.00 18.94 ? 79   TYR A CD1 1 
ATOM   576  C  CD2 . TYR A 1 79  ? 15.961  -34.937 -4.867  1.00 17.52 ? 79   TYR A CD2 1 
ATOM   577  C  CE1 . TYR A 1 79  ? 17.140  -34.851 -2.370  1.00 18.11 ? 79   TYR A CE1 1 
ATOM   578  C  CE2 . TYR A 1 79  ? 16.043  -36.099 -4.070  1.00 14.78 ? 79   TYR A CE2 1 
ATOM   579  C  CZ  . TYR A 1 79  ? 16.629  -36.037 -2.830  1.00 16.73 ? 79   TYR A CZ  1 
ATOM   580  O  OH  . TYR A 1 79  ? 16.715  -37.156 -2.033  1.00 20.42 ? 79   TYR A OH  1 
ATOM   581  N  N   . VAL A 1 80  ? 14.273  -29.416 -5.683  1.00 13.46 ? 80   VAL A N   1 
ATOM   582  C  CA  . VAL A 1 80  ? 14.138  -28.168 -6.421  1.00 14.35 ? 80   VAL A CA  1 
ATOM   583  C  C   . VAL A 1 80  ? 14.316  -27.017 -5.434  1.00 14.54 ? 80   VAL A C   1 
ATOM   584  O  O   . VAL A 1 80  ? 13.767  -27.092 -4.328  1.00 13.20 ? 80   VAL A O   1 
ATOM   585  C  CB  . VAL A 1 80  ? 12.769  -28.105 -7.119  1.00 11.99 ? 80   VAL A CB  1 
ATOM   586  C  CG1 . VAL A 1 80  ? 12.493  -26.681 -7.655  1.00 14.02 ? 80   VAL A CG1 1 
ATOM   587  C  CG2 . VAL A 1 80  ? 12.698  -29.136 -8.230  1.00 14.92 ? 80   VAL A CG2 1 
ATOM   588  N  N   . PRO A 1 81  ? 15.027  -25.940 -5.783  1.00 16.83 ? 81   PRO A N   1 
ATOM   589  C  CA  . PRO A 1 81  ? 15.369  -24.904 -4.782  1.00 14.68 ? 81   PRO A CA  1 
ATOM   590  C  C   . PRO A 1 81  ? 14.136  -24.151 -4.318  1.00 16.01 ? 81   PRO A C   1 
ATOM   591  O  O   . PRO A 1 81  ? 13.106  -24.154 -5.010  1.00 16.19 ? 81   PRO A O   1 
ATOM   592  C  CB  . PRO A 1 81  ? 16.336  -23.971 -5.536  1.00 20.25 ? 81   PRO A CB  1 
ATOM   593  C  CG  . PRO A 1 81  ? 16.852  -24.791 -6.690  1.00 23.45 ? 81   PRO A CG  1 
ATOM   594  C  CD  . PRO A 1 81  ? 15.681  -25.678 -7.075  1.00 18.76 ? 81   PRO A CD  1 
ATOM   595  N  N   . PRO A 1 82  ? 14.237  -23.450 -3.185  1.00 16.96 ? 82   PRO A N   1 
ATOM   596  C  CA  . PRO A 1 82  ? 13.052  -22.849 -2.528  1.00 16.18 ? 82   PRO A CA  1 
ATOM   597  C  C   . PRO A 1 82  ? 12.217  -21.952 -3.433  1.00 14.89 ? 82   PRO A C   1 
ATOM   598  O  O   . PRO A 1 82  ? 10.985  -21.977 -3.326  1.00 16.23 ? 82   PRO A O   1 
ATOM   599  C  CB  . PRO A 1 82  ? 13.670  -22.052 -1.359  1.00 17.84 ? 82   PRO A CB  1 
ATOM   600  C  CG  . PRO A 1 82  ? 14.916  -22.837 -0.993  1.00 15.90 ? 82   PRO A CG  1 
ATOM   601  C  CD  . PRO A 1 82  ? 15.424  -23.449 -2.298  1.00 15.94 ? 82   PRO A CD  1 
ATOM   602  N  N   . PRO A 1 83  ? 12.809  -21.120 -4.310  1.00 15.18 ? 83   PRO A N   1 
ATOM   603  C  CA  . PRO A 1 83  ? 11.954  -20.236 -5.120  1.00 17.22 ? 83   PRO A CA  1 
ATOM   604  C  C   . PRO A 1 83  ? 10.985  -20.962 -6.049  1.00 18.16 ? 83   PRO A C   1 
ATOM   605  O  O   . PRO A 1 83  ? 9.933   -20.407 -6.381  1.00 14.79 ? 83   PRO A O   1 
ATOM   606  C  CB  . PRO A 1 83  ? 12.967  -19.406 -5.923  1.00 19.78 ? 83   PRO A CB  1 
ATOM   607  C  CG  . PRO A 1 83  ? 14.177  -19.426 -5.134  1.00 17.57 ? 83   PRO A CG  1 
ATOM   608  C  CD  . PRO A 1 83  ? 14.225  -20.826 -4.569  1.00 17.96 ? 83   PRO A CD  1 
ATOM   609  N  N   . PHE A 1 84  ? 11.297  -22.177 -6.487  1.00 16.56 ? 84   PHE A N   1 
ATOM   610  C  CA  . PHE A 1 84  ? 10.448  -22.864 -7.445  1.00 13.76 ? 84   PHE A CA  1 
ATOM   611  C  C   . PHE A 1 84  ? 9.895   -24.190 -6.946  1.00 12.61 ? 84   PHE A C   1 
ATOM   612  O  O   . PHE A 1 84  ? 9.170   -24.858 -7.697  1.00 13.22 ? 84   PHE A O   1 
ATOM   613  C  CB  . PHE A 1 84  ? 11.215  -23.100 -8.758  1.00 17.96 ? 84   PHE A CB  1 
ATOM   614  C  CG  . PHE A 1 84  ? 11.924  -21.876 -9.287  1.00 17.45 ? 84   PHE A CG  1 
ATOM   615  C  CD1 . PHE A 1 84  ? 11.212  -20.823 -9.828  1.00 21.31 ? 84   PHE A CD1 1 
ATOM   616  C  CD2 . PHE A 1 84  ? 13.308  -21.796 -9.251  1.00 22.06 ? 84   PHE A CD2 1 
ATOM   617  C  CE1 . PHE A 1 84  ? 11.875  -19.697 -10.326 1.00 29.39 ? 84   PHE A CE1 1 
ATOM   618  C  CE2 . PHE A 1 84  ? 13.987  -20.675 -9.750  1.00 26.12 ? 84   PHE A CE2 1 
ATOM   619  C  CZ  . PHE A 1 84  ? 13.270  -19.626 -10.288 1.00 26.09 ? 84   PHE A CZ  1 
ATOM   620  N  N   . ALA A 1 85  ? 10.201  -24.595 -5.711  1.00 15.16 ? 85   ALA A N   1 
ATOM   621  C  CA  . ALA A 1 85  ? 9.800   -25.927 -5.263  1.00 12.21 ? 85   ALA A CA  1 
ATOM   622  C  C   . ALA A 1 85  ? 8.290   -26.055 -5.077  1.00 14.85 ? 85   ALA A C   1 
ATOM   623  O  O   . ALA A 1 85  ? 7.744   -27.151 -5.260  1.00 13.56 ? 85   ALA A O   1 
ATOM   624  C  CB  . ALA A 1 85  ? 10.522  -26.293 -3.968  1.00 12.43 ? 85   ALA A CB  1 
ATOM   625  N  N   . ALA A 1 86  ? 7.594   -24.965 -4.721  1.00 14.92 ? 86   ALA A N   1 
ATOM   626  C  CA  . ALA A 1 86  ? 6.144   -25.058 -4.563  1.00 15.95 ? 86   ALA A CA  1 
ATOM   627  C  C   . ALA A 1 86  ? 5.457   -25.267 -5.910  1.00 14.60 ? 86   ALA A C   1 
ATOM   628  O  O   . ALA A 1 86  ? 4.522   -26.072 -6.020  1.00 11.72 ? 86   ALA A O   1 
ATOM   629  C  CB  . ALA A 1 86  ? 5.591   -23.809 -3.867  1.00 11.19 ? 86   ALA A CB  1 
ATOM   630  N  N   . ALA A 1 87  ? 5.900   -24.548 -6.947  1.00 14.81 ? 87   ALA A N   1 
ATOM   631  C  CA  . ALA A 1 87  ? 5.404   -24.849 -8.285  1.00 14.23 ? 87   ALA A CA  1 
ATOM   632  C  C   . ALA A 1 87  ? 5.729   -26.289 -8.681  1.00 14.47 ? 87   ALA A C   1 
ATOM   633  O  O   . ALA A 1 87  ? 4.942   -26.920 -9.394  1.00 16.29 ? 87   ALA A O   1 
ATOM   634  C  CB  . ALA A 1 87  ? 5.970   -23.852 -9.307  1.00 16.75 ? 87   ALA A CB  1 
ATOM   635  N  N   . ALA A 1 88  ? 6.867   -26.837 -8.203  1.00 17.14 ? 88   ALA A N   1 
ATOM   636  C  CA  . ALA A 1 88  ? 7.198   -28.234 -8.484  1.00 16.54 ? 88   ALA A CA  1 
ATOM   637  C  C   . ALA A 1 88  ? 6.222   -29.193 -7.801  1.00 17.28 ? 88   ALA A C   1 
ATOM   638  O  O   . ALA A 1 88  ? 5.761   -30.164 -8.422  1.00 14.75 ? 88   ALA A O   1 
ATOM   639  C  CB  . ALA A 1 88  ? 8.638   -28.541 -8.057  1.00 12.68 ? 88   ALA A CB  1 
ATOM   640  N  N   . ILE A 1 89  ? 5.901   -28.949 -6.521  1.00 13.26 ? 89   ILE A N   1 
ATOM   641  C  CA  . ILE A 1 89  ? 4.848   -29.735 -5.872  1.00 15.01 ? 89   ILE A CA  1 
ATOM   642  C  C   . ILE A 1 89  ? 3.534   -29.596 -6.633  1.00 12.80 ? 89   ILE A C   1 
ATOM   643  O  O   . ILE A 1 89  ? 2.843   -30.587 -6.893  1.00 14.99 ? 89   ILE A O   1 
ATOM   644  C  CB  . ILE A 1 89  ? 4.665   -29.325 -4.399  1.00 14.61 ? 89   ILE A CB  1 
ATOM   645  C  CG1 . ILE A 1 89  ? 5.995   -29.394 -3.623  1.00 15.71 ? 89   ILE A CG1 1 
ATOM   646  C  CG2 . ILE A 1 89  ? 3.569   -30.198 -3.766  1.00 13.86 ? 89   ILE A CG2 1 
ATOM   647  C  CD1 . ILE A 1 89  ? 5.950   -28.669 -2.255  1.00 13.65 ? 89   ILE A CD1 1 
ATOM   648  N  N   . ASN A 1 90  ? 3.159   -28.355 -6.981  1.00 13.29 ? 90   ASN A N   1 
ATOM   649  C  CA  . ASN A 1 90  ? 1.904   -28.120 -7.700  1.00 15.48 ? 90   ASN A CA  1 
ATOM   650  C  C   . ASN A 1 90  ? 1.853   -28.896 -9.010  1.00 17.59 ? 90   ASN A C   1 
ATOM   651  O  O   . ASN A 1 90  ? 0.798   -29.427 -9.378  1.00 13.09 ? 90   ASN A O   1 
ATOM   652  C  CB  . ASN A 1 90  ? 1.709   -26.626 -7.972  1.00 17.00 ? 90   ASN A CB  1 
ATOM   653  C  CG  . ASN A 1 90  ? 1.204   -25.874 -6.758  1.00 22.65 ? 90   ASN A CG  1 
ATOM   654  O  OD1 . ASN A 1 90  ? 0.635   -26.466 -5.827  1.00 21.52 ? 90   ASN A OD1 1 
ATOM   655  N  ND2 . ASN A 1 90  ? 1.392   -24.562 -6.767  1.00 20.56 ? 90   ASN A ND2 1 
ATOM   656  N  N   . GLU A 1 91  ? 2.985   -28.971 -9.729  1.00 16.57 ? 91   GLU A N   1 
ATOM   657  C  CA  . GLU A 1 91  ? 3.021   -29.716 -10.985 1.00 15.18 ? 91   GLU A CA  1 
ATOM   658  C  C   . GLU A 1 91  ? 2.758   -31.204 -10.752 1.00 15.25 ? 91   GLU A C   1 
ATOM   659  O  O   . GLU A 1 91  ? 2.000   -31.842 -11.495 1.00 14.44 ? 91   GLU A O   1 
ATOM   660  C  CB  . GLU A 1 91  ? 4.365   -29.519 -11.694 1.00 15.64 ? 91   GLU A CB  1 
ATOM   661  C  CG  . GLU A 1 91  ? 4.311   -30.005 -13.155 1.00 17.04 ? 91   GLU A CG  1 
ATOM   662  C  CD  . GLU A 1 91  ? 5.668   -30.015 -13.858 1.00 16.29 ? 91   GLU A CD  1 
ATOM   663  O  OE1 . GLU A 1 91  ? 6.618   -29.407 -13.345 1.00 18.23 ? 91   GLU A OE1 1 
ATOM   664  O  OE2 . GLU A 1 91  ? 5.773   -30.649 -14.929 1.00 19.12 ? 91   GLU A OE2 1 
ATOM   665  N  N   . ALA A 1 92  ? 3.371   -31.767 -9.717  1.00 16.19 ? 92   ALA A N   1 
ATOM   666  C  CA  . ALA A 1 92  ? 3.168   -33.174 -9.406  1.00 15.54 ? 92   ALA A CA  1 
ATOM   667  C  C   . ALA A 1 92  ? 1.732   -33.442 -8.956  1.00 17.40 ? 92   ALA A C   1 
ATOM   668  O  O   . ALA A 1 92  ? 1.154   -34.479 -9.296  1.00 15.16 ? 92   ALA A O   1 
ATOM   669  C  CB  . ALA A 1 92  ? 4.184   -33.608 -8.346  1.00 14.41 ? 92   ALA A CB  1 
ATOM   670  N  N   . ILE A 1 93  ? 1.130   -32.515 -8.207  1.00 14.47 ? 93   ILE A N   1 
ATOM   671  C  CA  . ILE A 1 93  ? -0.291  -32.656 -7.886  1.00 15.81 ? 93   ILE A CA  1 
ATOM   672  C  C   . ILE A 1 93  ? -1.137  -32.601 -9.155  1.00 16.38 ? 93   ILE A C   1 
ATOM   673  O  O   . ILE A 1 93  ? -2.073  -33.395 -9.333  1.00 17.34 ? 93   ILE A O   1 
ATOM   674  C  CB  . ILE A 1 93  ? -0.736  -31.575 -6.888  1.00 11.84 ? 93   ILE A CB  1 
ATOM   675  C  CG1 . ILE A 1 93  ? 0.021   -31.701 -5.566  1.00 17.05 ? 93   ILE A CG1 1 
ATOM   676  C  CG2 . ILE A 1 93  ? -2.247  -31.671 -6.639  1.00 17.06 ? 93   ILE A CG2 1 
ATOM   677  C  CD1 . ILE A 1 93  ? -0.262  -30.531 -4.617  1.00 15.61 ? 93   ILE A CD1 1 
ATOM   678  N  N   . GLU A 1 94  ? -0.851  -31.635 -10.036 1.00 17.18 ? 94   GLU A N   1 
ATOM   679  C  CA  . GLU A 1 94  ? -1.631  -31.511 -11.263 1.00 19.79 ? 94   GLU A CA  1 
ATOM   680  C  C   . GLU A 1 94  ? -1.515  -32.763 -12.108 1.00 17.69 ? 94   GLU A C   1 
ATOM   681  O  O   . GLU A 1 94  ? -2.477  -33.151 -12.783 1.00 19.74 ? 94   GLU A O   1 
ATOM   682  C  CB  . GLU A 1 94  ? -1.180  -30.289 -12.067 1.00 20.47 ? 94   GLU A CB  1 
ATOM   683  C  CG  . GLU A 1 94  ? -2.130  -29.119 -12.004 1.00 30.14 ? 94   GLU A CG  1 
ATOM   684  C  CD  . GLU A 1 94  ? -3.538  -29.508 -12.423 1.00 31.45 ? 94   GLU A CD  1 
ATOM   685  O  OE1 . GLU A 1 94  ? -4.398  -29.677 -11.538 1.00 30.47 ? 94   GLU A OE1 1 
ATOM   686  O  OE2 . GLU A 1 94  ? -3.779  -29.660 -13.636 1.00 38.49 ? 94   GLU A OE2 1 
ATOM   687  N  N   . ALA A 1 95  ? -0.357  -33.413 -12.071 1.00 17.49 ? 95   ALA A N   1 
ATOM   688  C  CA  . ALA A 1 95  ? -0.119  -34.630 -12.841 1.00 19.57 ? 95   ALA A CA  1 
ATOM   689  C  C   . ALA A 1 95  ? -0.652  -35.882 -12.150 1.00 20.15 ? 95   ALA A C   1 
ATOM   690  O  O   . ALA A 1 95  ? -0.555  -36.979 -12.718 1.00 18.18 ? 95   ALA A O   1 
ATOM   691  C  CB  . ALA A 1 95  ? 1.381   -34.776 -13.120 1.00 14.36 ? 95   ALA A CB  1 
ATOM   692  N  N   . GLU A 1 96  ? -1.196  -35.741 -10.944 1.00 16.69 ? 96   GLU A N   1 
ATOM   693  C  CA  . GLU A 1 96  ? -1.858  -36.831 -10.226 1.00 17.38 ? 96   GLU A CA  1 
ATOM   694  C  C   . GLU A 1 96  ? -0.885  -37.955 -9.862  1.00 16.70 ? 96   GLU A C   1 
ATOM   695  O  O   . GLU A 1 96  ? -1.268  -39.119 -9.789  1.00 18.03 ? 96   GLU A O   1 
ATOM   696  C  CB  . GLU A 1 96  ? -3.064  -37.361 -11.021 1.00 21.37 ? 96   GLU A CB  1 
ATOM   697  C  CG  . GLU A 1 96  ? -4.108  -36.253 -11.309 1.00 19.95 ? 96   GLU A CG  1 
ATOM   698  C  CD  . GLU A 1 96  ? -5.351  -36.761 -12.037 1.00 26.06 ? 96   GLU A CD  1 
ATOM   699  O  OE1 . GLU A 1 96  ? -5.279  -37.833 -12.659 1.00 27.76 ? 96   GLU A OE1 1 
ATOM   700  O  OE2 . GLU A 1 96  ? -6.395  -36.085 -11.983 1.00 28.07 ? 96   GLU A OE2 1 
ATOM   701  N  N   . ILE A 1 97  ? 0.372   -37.599 -9.610  1.00 17.69 ? 97   ILE A N   1 
ATOM   702  C  CA  . ILE A 1 97  ? 1.388   -38.479 -9.025  1.00 20.22 ? 97   ILE A CA  1 
ATOM   703  C  C   . ILE A 1 97  ? 0.896   -38.964 -7.662  1.00 15.65 ? 97   ILE A C   1 
ATOM   704  O  O   . ILE A 1 97  ? 0.602   -38.124 -6.806  1.00 15.08 ? 97   ILE A O   1 
ATOM   705  C  CB  . ILE A 1 97  ? 2.733   -37.733 -8.888  1.00 17.10 ? 97   ILE A CB  1 
ATOM   706  C  CG1 . ILE A 1 97  ? 3.319   -37.401 -10.264 1.00 22.88 ? 97   ILE A CG1 1 
ATOM   707  C  CG2 . ILE A 1 97  ? 3.718   -38.520 -8.050  1.00 18.94 ? 97   ILE A CG2 1 
ATOM   708  C  CD1 . ILE A 1 97  ? 3.985   -38.596 -10.977 1.00 22.59 ? 97   ILE A CD1 1 
ATOM   709  N  N   . PRO A 1 98  ? 0.787   -40.279 -7.406  1.00 15.22 ? 98   PRO A N   1 
ATOM   710  C  CA  . PRO A 1 98  ? 0.203   -40.716 -6.115  1.00 15.78 ? 98   PRO A CA  1 
ATOM   711  C  C   . PRO A 1 98  ? 0.954   -40.212 -4.890  1.00 16.86 ? 98   PRO A C   1 
ATOM   712  O  O   . PRO A 1 98  ? 0.314   -39.789 -3.919  1.00 15.78 ? 98   PRO A O   1 
ATOM   713  C  CB  . PRO A 1 98  ? 0.218   -42.253 -6.223  1.00 16.74 ? 98   PRO A CB  1 
ATOM   714  C  CG  . PRO A 1 98  ? -0.002  -42.484 -7.763  1.00 18.90 ? 98   PRO A CG  1 
ATOM   715  C  CD  . PRO A 1 98  ? 0.836   -41.375 -8.400  1.00 17.96 ? 98   PRO A CD  1 
ATOM   716  N  N   . LEU A 1 99  ? 2.288   -40.211 -4.911  1.00 16.16 ? 99   LEU A N   1 
ATOM   717  C  CA  . LEU A 1 99  ? 3.073   -39.747 -3.773  1.00 15.37 ? 99   LEU A CA  1 
ATOM   718  C  C   . LEU A 1 99  ? 4.106   -38.715 -4.211  1.00 16.63 ? 99   LEU A C   1 
ATOM   719  O  O   . LEU A 1 99  ? 4.883   -38.969 -5.139  1.00 16.43 ? 99   LEU A O   1 
ATOM   720  C  CB  . LEU A 1 99  ? 3.773   -40.917 -3.095  1.00 13.91 ? 99   LEU A CB  1 
ATOM   721  C  CG  . LEU A 1 99  ? 4.567   -40.534 -1.847  1.00 15.56 ? 99   LEU A CG  1 
ATOM   722  C  CD1 . LEU A 1 99  ? 3.630   -40.190 -0.688  1.00 14.69 ? 99   LEU A CD1 1 
ATOM   723  C  CD2 . LEU A 1 99  ? 5.484   -41.674 -1.476  1.00 14.25 ? 99   LEU A CD2 1 
ATOM   724  N  N   . VAL A 1 100 ? 4.140   -37.572 -3.527  1.00 16.68 ? 100  VAL A N   1 
ATOM   725  C  CA  . VAL A 1 100 ? 5.176   -36.555 -3.740  1.00 16.02 ? 100  VAL A CA  1 
ATOM   726  C  C   . VAL A 1 100 ? 5.931   -36.330 -2.434  1.00 18.07 ? 100  VAL A C   1 
ATOM   727  O  O   . VAL A 1 100 ? 5.324   -35.988 -1.407  1.00 13.08 ? 100  VAL A O   1 
ATOM   728  C  CB  . VAL A 1 100 ? 4.594   -35.236 -4.255  1.00 17.70 ? 100  VAL A CB  1 
ATOM   729  C  CG1 . VAL A 1 100 ? 5.723   -34.210 -4.486  1.00 18.70 ? 100  VAL A CG1 1 
ATOM   730  C  CG2 . VAL A 1 100 ? 3.826   -35.485 -5.529  1.00 19.68 ? 100  VAL A CG2 1 
ATOM   731  N  N   . VAL A 1 101 ? 7.253   -36.501 -2.481  1.00 12.83 ? 101  VAL A N   1 
ATOM   732  C  CA  . VAL A 1 101 ? 8.137   -36.270 -1.346  1.00 17.00 ? 101  VAL A CA  1 
ATOM   733  C  C   . VAL A 1 101 ? 9.001   -35.044 -1.638  1.00 18.32 ? 101  VAL A C   1 
ATOM   734  O  O   . VAL A 1 101 ? 9.824   -35.059 -2.567  1.00 14.39 ? 101  VAL A O   1 
ATOM   735  C  CB  . VAL A 1 101 ? 9.017   -37.489 -1.060  1.00 13.62 ? 101  VAL A CB  1 
ATOM   736  C  CG1 . VAL A 1 101 ? 9.887   -37.229 0.181   1.00 16.03 ? 101  VAL A CG1 1 
ATOM   737  C  CG2 . VAL A 1 101 ? 8.154   -38.762 -0.888  1.00 16.99 ? 101  VAL A CG2 1 
ATOM   738  N  N   . CYS A 1 102 ? 8.852   -33.996 -0.819  1.00 15.58 ? 102  CYS A N   1 
ATOM   739  C  CA  . CYS A 1 102 ? 9.585   -32.748 -1.025  1.00 12.60 ? 102  CYS A CA  1 
ATOM   740  C  C   . CYS A 1 102 ? 10.646  -32.594 0.056   1.00 12.72 ? 102  CYS A C   1 
ATOM   741  O  O   . CYS A 1 102 ? 10.325  -32.409 1.236   1.00 14.57 ? 102  CYS A O   1 
ATOM   742  C  CB  . CYS A 1 102 ? 8.643   -31.556 -1.048  1.00 12.07 ? 102  CYS A CB  1 
ATOM   743  S  SG  . CYS A 1 102 ? 9.496   -30.044 -1.522  1.00 14.46 ? 102  CYS A SG  1 
ATOM   744  N  N   . ILE A 1 103 ? 11.906  -32.691 -0.360  1.00 13.86 ? 103  ILE A N   1 
ATOM   745  C  CA  . ILE A 1 103 ? 13.058  -32.557 0.526   1.00 12.47 ? 103  ILE A CA  1 
ATOM   746  C  C   . ILE A 1 103 ? 13.346  -31.092 0.847   1.00 14.87 ? 103  ILE A C   1 
ATOM   747  O  O   . ILE A 1 103 ? 13.765  -30.773 1.967   1.00 14.19 ? 103  ILE A O   1 
ATOM   748  C  CB  . ILE A 1 103 ? 14.274  -33.233 -0.129  1.00 14.83 ? 103  ILE A CB  1 
ATOM   749  C  CG1 . ILE A 1 103 ? 13.928  -34.680 -0.521  1.00 14.45 ? 103  ILE A CG1 1 
ATOM   750  C  CG2 . ILE A 1 103 ? 15.464  -33.216 0.822   1.00 15.84 ? 103  ILE A CG2 1 
ATOM   751  C  CD1 . ILE A 1 103 ? 13.497  -35.541 0.672   1.00 14.51 ? 103  ILE A CD1 1 
ATOM   752  N  N   . THR A 1 104 ? 13.081  -30.198 -0.113  1.00 15.18 ? 104  THR A N   1 
ATOM   753  C  CA  . THR A 1 104 ? 13.497  -28.801 -0.077  1.00 12.57 ? 104  THR A CA  1 
ATOM   754  C  C   . THR A 1 104 ? 13.237  -28.133 1.269   1.00 12.60 ? 104  THR A C   1 
ATOM   755  O  O   . THR A 1 104 ? 12.136  -28.205 1.818   1.00 14.41 ? 104  THR A O   1 
ATOM   756  C  CB  . THR A 1 104 ? 12.763  -28.042 -1.187  1.00 12.14 ? 104  THR A CB  1 
ATOM   757  O  OG1 . THR A 1 104 ? 12.986  -28.711 -2.439  1.00 13.32 ? 104  THR A OG1 1 
ATOM   758  C  CG2 . THR A 1 104 ? 13.266  -26.602 -1.287  1.00 13.02 ? 104  THR A CG2 1 
ATOM   759  N  N   . GLU A 1 105 ? 14.250  -27.459 1.785   1.00 16.87 ? 105  GLU A N   1 
ATOM   760  C  CA  . GLU A 1 105 ? 14.087  -26.568 2.928   1.00 17.20 ? 105  GLU A CA  1 
ATOM   761  C  C   . GLU A 1 105 ? 14.038  -25.119 2.440   1.00 19.36 ? 105  GLU A C   1 
ATOM   762  O  O   . GLU A 1 105 ? 14.705  -24.762 1.470   1.00 18.80 ? 105  GLU A O   1 
ATOM   763  C  CB  . GLU A 1 105 ? 15.228  -26.764 3.941   1.00 16.96 ? 105  GLU A CB  1 
ATOM   764  C  CG  . GLU A 1 105 ? 15.333  -25.691 5.018   1.00 23.49 ? 105  GLU A CG  1 
ATOM   765  C  CD  . GLU A 1 105 ? 16.662  -25.745 5.801   1.00 37.25 ? 105  GLU A CD  1 
ATOM   766  O  OE1 . GLU A 1 105 ? 16.630  -25.562 7.037   1.00 43.37 ? 105  GLU A OE1 1 
ATOM   767  O  OE2 . GLU A 1 105 ? 17.736  -25.961 5.190   1.00 35.06 ? 105  GLU A OE2 1 
ATOM   768  N  N   . GLY A 1 106 ? 13.212  -24.297 3.083   1.00 15.69 ? 106  GLY A N   1 
ATOM   769  C  CA  . GLY A 1 106 ? 13.170  -22.873 2.793   1.00 17.02 ? 106  GLY A CA  1 
ATOM   770  C  C   . GLY A 1 106 ? 12.057  -22.386 1.883   1.00 15.26 ? 106  GLY A C   1 
ATOM   771  O  O   . GLY A 1 106 ? 12.107  -21.230 1.442   1.00 15.68 ? 106  GLY A O   1 
ATOM   772  N  N   . ILE A 1 107 ? 11.066  -23.219 1.576   1.00 15.76 ? 107  ILE A N   1 
ATOM   773  C  CA  . ILE A 1 107 ? 9.914   -22.771 0.792   1.00 14.59 ? 107  ILE A CA  1 
ATOM   774  C  C   . ILE A 1 107 ? 9.139   -21.742 1.611   1.00 14.40 ? 107  ILE A C   1 
ATOM   775  O  O   . ILE A 1 107 ? 8.758   -22.035 2.746   1.00 14.95 ? 107  ILE A O   1 
ATOM   776  C  CB  . ILE A 1 107 ? 8.992   -23.946 0.404   1.00 11.28 ? 107  ILE A CB  1 
ATOM   777  C  CG1 . ILE A 1 107 ? 9.745   -25.018 -0.401  1.00 12.47 ? 107  ILE A CG1 1 
ATOM   778  C  CG2 . ILE A 1 107 ? 7.804   -23.434 -0.389  1.00 12.91 ? 107  ILE A CG2 1 
ATOM   779  C  CD1 . ILE A 1 107 ? 8.897   -26.221 -0.764  1.00 14.73 ? 107  ILE A CD1 1 
ATOM   780  N  N   . PRO A 1 108 ? 8.902   -20.540 1.089   1.00 14.77 ? 108  PRO A N   1 
ATOM   781  C  CA  . PRO A 1 108 ? 8.027   -19.578 1.778   1.00 15.18 ? 108  PRO A CA  1 
ATOM   782  C  C   . PRO A 1 108 ? 6.728   -20.203 2.269   1.00 13.76 ? 108  PRO A C   1 
ATOM   783  O  O   . PRO A 1 108 ? 6.090   -20.990 1.565   1.00 16.74 ? 108  PRO A O   1 
ATOM   784  C  CB  . PRO A 1 108 ? 7.736   -18.530 0.694   1.00 15.14 ? 108  PRO A CB  1 
ATOM   785  C  CG  . PRO A 1 108 ? 8.907   -18.603 -0.239  1.00 15.73 ? 108  PRO A CG  1 
ATOM   786  C  CD  . PRO A 1 108 ? 9.380   -20.037 -0.216  1.00 14.22 ? 108  PRO A CD  1 
ATOM   787  N  N   . GLN A 1 109 ? 6.334   -19.836 3.491   1.00 12.24 ? 109  GLN A N   1 
ATOM   788  C  CA  . GLN A 1 109 ? 5.069   -20.314 4.046   1.00 15.87 ? 109  GLN A CA  1 
ATOM   789  C  C   . GLN A 1 109 ? 3.883   -19.923 3.167   1.00 14.14 ? 109  GLN A C   1 
ATOM   790  O  O   . GLN A 1 109 ? 2.951   -20.714 2.987   1.00 14.52 ? 109  GLN A O   1 
ATOM   791  C  CB  . GLN A 1 109 ? 4.888   -19.781 5.471   1.00 14.80 ? 109  GLN A CB  1 
ATOM   792  C  CG  . GLN A 1 109 ? 6.000   -20.216 6.440   1.00 14.82 ? 109  GLN A CG  1 
ATOM   793  C  CD  . GLN A 1 109 ? 5.743   -19.789 7.877   1.00 15.79 ? 109  GLN A CD  1 
ATOM   794  O  OE1 . GLN A 1 109 ? 4.603   -19.602 8.285   1.00 18.64 ? 109  GLN A OE1 1 
ATOM   795  N  NE2 . GLN A 1 109 ? 6.805   -19.601 8.629   1.00 15.98 ? 109  GLN A NE2 1 
ATOM   796  N  N   . GLN A 1 110 ? 3.897   -18.713 2.601   1.00 14.32 ? 110  GLN A N   1 
ATOM   797  C  CA  . GLN A 1 110 ? 2.774   -18.301 1.759   1.00 14.14 ? 110  GLN A CA  1 
ATOM   798  C  C   . GLN A 1 110 ? 2.660   -19.198 0.532   1.00 15.31 ? 110  GLN A C   1 
ATOM   799  O  O   . GLN A 1 110 ? 1.551   -19.544 0.109   1.00 14.02 ? 110  GLN A O   1 
ATOM   800  C  CB  . GLN A 1 110 ? 2.913   -16.833 1.334   1.00 17.85 ? 110  GLN A CB  1 
ATOM   801  C  CG  . GLN A 1 110 ? 1.623   -16.257 0.768   1.00 16.83 ? 110  GLN A CG  1 
ATOM   802  C  CD  . GLN A 1 110 ? 1.784   -14.871 0.168   1.00 20.92 ? 110  GLN A CD  1 
ATOM   803  O  OE1 . GLN A 1 110 ? 1.441   -14.650 -0.994  1.00 22.72 ? 110  GLN A OE1 1 
ATOM   804  N  NE2 . GLN A 1 110 ? 2.289   -13.926 0.959   1.00 19.13 ? 110  GLN A NE2 1 
ATOM   805  N  N   . ASP A 1 111 ? 3.803   -19.596 -0.041  1.00 12.86 ? 111  ASP A N   1 
ATOM   806  C  CA  . ASP A 1 111 ? 3.802   -20.580 -1.123  1.00 17.09 ? 111  ASP A CA  1 
ATOM   807  C  C   . ASP A 1 111 ? 3.146   -21.880 -0.678  1.00 15.53 ? 111  ASP A C   1 
ATOM   808  O  O   . ASP A 1 111 ? 2.339   -22.464 -1.404  1.00 13.23 ? 111  ASP A O   1 
ATOM   809  C  CB  . ASP A 1 111 ? 5.232   -20.867 -1.590  1.00 14.14 ? 111  ASP A CB  1 
ATOM   810  C  CG  . ASP A 1 111 ? 5.818   -19.758 -2.422  1.00 20.16 ? 111  ASP A CG  1 
ATOM   811  O  OD1 . ASP A 1 111 ? 5.212   -18.659 -2.505  1.00 20.13 ? 111  ASP A OD1 1 
ATOM   812  O  OD2 . ASP A 1 111 ? 6.892   -20.008 -3.011  1.00 18.68 ? 111  ASP A OD2 1 
ATOM   813  N  N   . MET A 1 112 ? 3.511   -22.370 0.508   1.00 15.76 ? 112  MET A N   1 
ATOM   814  C  CA  . MET A 1 112 ? 2.960   -23.650 0.946   1.00 17.00 ? 112  MET A CA  1 
ATOM   815  C  C   . MET A 1 112 ? 1.483   -23.542 1.298   1.00 15.95 ? 112  MET A C   1 
ATOM   816  O  O   . MET A 1 112 ? 0.744   -24.523 1.140   1.00 16.98 ? 112  MET A O   1 
ATOM   817  C  CB  . MET A 1 112 ? 3.752   -24.206 2.131   1.00 15.88 ? 112  MET A CB  1 
ATOM   818  C  CG  . MET A 1 112 ? 5.069   -24.849 1.710   1.00 15.35 ? 112  MET A CG  1 
ATOM   819  S  SD  . MET A 1 112 ? 4.840   -26.080 0.399   1.00 17.01 ? 112  MET A SD  1 
ATOM   820  C  CE  . MET A 1 112 ? 3.615   -27.153 1.146   1.00 13.82 ? 112  MET A CE  1 
ATOM   821  N  N   . VAL A 1 113 ? 1.038   -22.383 1.794   1.00 16.14 ? 113  VAL A N   1 
ATOM   822  C  CA  . VAL A 1 113 ? -0.398  -22.197 2.011   1.00 15.10 ? 113  VAL A CA  1 
ATOM   823  C  C   . VAL A 1 113 ? -1.141  -22.368 0.693   1.00 13.31 ? 113  VAL A C   1 
ATOM   824  O  O   . VAL A 1 113 ? -2.196  -23.018 0.627   1.00 15.66 ? 113  VAL A O   1 
ATOM   825  C  CB  . VAL A 1 113 ? -0.672  -20.823 2.652   1.00 15.94 ? 113  VAL A CB  1 
ATOM   826  C  CG1 . VAL A 1 113 ? -2.176  -20.470 2.599   1.00 18.67 ? 113  VAL A CG1 1 
ATOM   827  C  CG2 . VAL A 1 113 ? -0.155  -20.786 4.093   1.00 14.13 ? 113  VAL A CG2 1 
ATOM   828  N  N   . ARG A 1 114 ? -0.572  -21.835 -0.386  1.00 15.31 ? 114  ARG A N   1 
ATOM   829  C  CA  . ARG A 1 114 ? -1.186  -21.984 -1.698  1.00 16.57 ? 114  ARG A CA  1 
ATOM   830  C  C   . ARG A 1 114 ? -1.161  -23.434 -2.149  1.00 16.16 ? 114  ARG A C   1 
ATOM   831  O  O   . ARG A 1 114 ? -2.156  -23.947 -2.671  1.00 16.51 ? 114  ARG A O   1 
ATOM   832  C  CB  . ARG A 1 114 ? -0.477  -21.094 -2.722  1.00 18.03 ? 114  ARG A CB  1 
ATOM   833  C  CG  . ARG A 1 114 ? -0.768  -19.589 -2.535  1.00 16.53 ? 114  ARG A CG  1 
ATOM   834  C  CD  . ARG A 1 114 ? 0.130   -18.713 -3.439  1.00 25.93 ? 114  ARG A CD  1 
ATOM   835  N  NE  . ARG A 1 114 ? 0.163   -17.324 -2.970  1.00 27.96 ? 114  ARG A NE  1 
ATOM   836  C  CZ  . ARG A 1 114 ? -0.810  -16.449 -3.201  1.00 31.05 ? 114  ARG A CZ  1 
ATOM   837  N  NH1 . ARG A 1 114 ? -1.888  -16.805 -3.900  1.00 23.71 ? 114  ARG A NH1 1 
ATOM   838  N  NH2 . ARG A 1 114 ? -0.712  -15.215 -2.730  1.00 30.38 ? 114  ARG A NH2 1 
ATOM   839  N  N   . VAL A 1 115 ? -0.020  -24.099 -1.977  1.00 13.26 ? 115  VAL A N   1 
ATOM   840  C  CA  . VAL A 1 115 ? 0.082   -25.519 -2.301  1.00 16.54 ? 115  VAL A CA  1 
ATOM   841  C  C   . VAL A 1 115 ? -0.946  -26.314 -1.504  1.00 14.98 ? 115  VAL A C   1 
ATOM   842  O  O   . VAL A 1 115 ? -1.604  -27.218 -2.032  1.00 16.26 ? 115  VAL A O   1 
ATOM   843  C  CB  . VAL A 1 115 ? 1.521   -26.011 -2.036  1.00 17.10 ? 115  VAL A CB  1 
ATOM   844  C  CG1 . VAL A 1 115 ? 1.616   -27.557 -2.128  1.00 17.77 ? 115  VAL A CG1 1 
ATOM   845  C  CG2 . VAL A 1 115 ? 2.495   -25.352 -2.998  1.00 11.73 ? 115  VAL A CG2 1 
ATOM   846  N  N   . LYS A 1 116 ? -1.098  -25.993 -0.216  1.00 15.67 ? 116  LYS A N   1 
ATOM   847  C  CA  . LYS A 1 116 ? -2.017  -26.760 0.626   1.00 16.15 ? 116  LYS A CA  1 
ATOM   848  C  C   . LYS A 1 116 ? -3.460  -26.606 0.171   1.00 16.31 ? 116  LYS A C   1 
ATOM   849  O  O   . LYS A 1 116 ? -4.252  -27.550 0.283   1.00 19.22 ? 116  LYS A O   1 
ATOM   850  C  CB  . LYS A 1 116 ? -1.883  -26.334 2.089   1.00 14.43 ? 116  LYS A CB  1 
ATOM   851  C  CG  . LYS A 1 116 ? -0.797  -27.061 2.819   1.00 22.29 ? 116  LYS A CG  1 
ATOM   852  C  CD  . LYS A 1 116 ? -1.224  -27.374 4.258   1.00 26.99 ? 116  LYS A CD  1 
ATOM   853  C  CE  . LYS A 1 116 ? -1.980  -28.699 4.368   1.00 23.95 ? 116  LYS A CE  1 
ATOM   854  N  NZ  . LYS A 1 116 ? -1.893  -29.186 5.771   1.00 23.05 ? 116  LYS A NZ  1 
ATOM   855  N  N   . HIS A 1 117 ? -3.813  -25.422 -0.321  1.00 15.56 ? 117  HIS A N   1 
ATOM   856  C  CA  . HIS A 1 117 ? -5.158  -25.160 -0.818  1.00 18.24 ? 117  HIS A CA  1 
ATOM   857  C  C   . HIS A 1 117 ? -5.505  -26.102 -1.968  1.00 19.53 ? 117  HIS A C   1 
ATOM   858  O  O   . HIS A 1 117 ? -6.598  -26.684 -2.015  1.00 18.12 ? 117  HIS A O   1 
ATOM   859  C  CB  . HIS A 1 117 ? -5.219  -23.695 -1.264  1.00 19.34 ? 117  HIS A CB  1 
ATOM   860  C  CG  . HIS A 1 117 ? -6.579  -23.226 -1.663  1.00 22.65 ? 117  HIS A CG  1 
ATOM   861  N  ND1 . HIS A 1 117 ? -7.186  -23.611 -2.839  1.00 23.23 ? 117  HIS A ND1 1 
ATOM   862  C  CD2 . HIS A 1 117 ? -7.429  -22.358 -1.065  1.00 21.91 ? 117  HIS A CD2 1 
ATOM   863  C  CE1 . HIS A 1 117 ? -8.364  -23.018 -2.935  1.00 25.07 ? 117  HIS A CE1 1 
ATOM   864  N  NE2 . HIS A 1 117 ? -8.537  -22.255 -1.870  1.00 23.05 ? 117  HIS A NE2 1 
ATOM   865  N  N   . LYS A 1 118 ? -4.577  -26.256 -2.913  1.00 16.81 ? 118  LYS A N   1 
ATOM   866  C  CA  . LYS A 1 118 ? -4.758  -27.212 -4.001  1.00 18.37 ? 118  LYS A CA  1 
ATOM   867  C  C   . LYS A 1 118 ? -4.776  -28.647 -3.480  1.00 16.84 ? 118  LYS A C   1 
ATOM   868  O  O   . LYS A 1 118 ? -5.598  -29.460 -3.919  1.00 18.59 ? 118  LYS A O   1 
ATOM   869  C  CB  . LYS A 1 118 ? -3.650  -27.028 -5.038  1.00 16.58 ? 118  LYS A CB  1 
ATOM   870  C  CG  . LYS A 1 118 ? -3.786  -27.908 -6.295  1.00 18.51 ? 118  LYS A CG  1 
ATOM   871  C  CD  . LYS A 1 118 ? -2.564  -27.750 -7.234  1.00 23.41 ? 118  LYS A CD  1 
ATOM   872  C  CE  . LYS A 1 118 ? -2.939  -27.042 -8.544  1.00 28.75 ? 118  LYS A CE  1 
ATOM   873  N  NZ  . LYS A 1 118 ? -3.843  -27.896 -9.405  1.00 31.48 ? 118  LYS A NZ  1 
ATOM   874  N  N   . LEU A 1 119 ? -3.881  -28.964 -2.537  1.00 15.74 ? 119  LEU A N   1 
ATOM   875  C  CA  . LEU A 1 119 ? -3.691  -30.338 -2.069  1.00 16.94 ? 119  LEU A CA  1 
ATOM   876  C  C   . LEU A 1 119 ? -4.933  -30.866 -1.364  1.00 17.21 ? 119  LEU A C   1 
ATOM   877  O  O   . LEU A 1 119 ? -5.308  -32.035 -1.533  1.00 13.69 ? 119  LEU A O   1 
ATOM   878  C  CB  . LEU A 1 119 ? -2.490  -30.399 -1.119  1.00 14.02 ? 119  LEU A CB  1 
ATOM   879  C  CG  . LEU A 1 119 ? -1.992  -31.753 -0.572  1.00 19.13 ? 119  LEU A CG  1 
ATOM   880  C  CD1 . LEU A 1 119 ? -1.350  -32.643 -1.677  1.00 12.27 ? 119  LEU A CD1 1 
ATOM   881  C  CD2 . LEU A 1 119 ? -1.015  -31.564 0.599   1.00 13.93 ? 119  LEU A CD2 1 
ATOM   882  N  N   . LEU A 1 120 ? -5.560  -30.021 -0.549  1.00 14.95 ? 120  LEU A N   1 
ATOM   883  C  CA  . LEU A 1 120 ? -6.693  -30.438 0.264   1.00 17.55 ? 120  LEU A CA  1 
ATOM   884  C  C   . LEU A 1 120 ? -7.950  -30.621 -0.560  1.00 16.59 ? 120  LEU A C   1 
ATOM   885  O  O   . LEU A 1 120 ? -8.895  -31.260 -0.084  1.00 19.43 ? 120  LEU A O   1 
ATOM   886  C  CB  . LEU A 1 120 ? -6.947  -29.410 1.374   1.00 17.69 ? 120  LEU A CB  1 
ATOM   887  C  CG  . LEU A 1 120 ? -5.869  -29.378 2.459   1.00 21.82 ? 120  LEU A CG  1 
ATOM   888  C  CD1 . LEU A 1 120 ? -6.029  -28.175 3.429   1.00 23.82 ? 120  LEU A CD1 1 
ATOM   889  C  CD2 . LEU A 1 120 ? -5.885  -30.695 3.214   1.00 22.04 ? 120  LEU A CD2 1 
ATOM   890  N  N   . ARG A 1 121 ? -7.983  -30.061 -1.770  1.00 15.82 ? 121  ARG A N   1 
ATOM   891  C  CA  . ARG A 1 121 ? -9.133  -30.146 -2.654  1.00 18.86 ? 121  ARG A CA  1 
ATOM   892  C  C   . ARG A 1 121 ? -8.984  -31.243 -3.700  1.00 17.73 ? 121  ARG A C   1 
ATOM   893  O  O   . ARG A 1 121 ? -9.745  -31.268 -4.670  1.00 17.61 ? 121  ARG A O   1 
ATOM   894  C  CB  . ARG A 1 121 ? -9.366  -28.790 -3.322  1.00 18.13 ? 121  ARG A CB  1 
ATOM   895  C  CG  . ARG A 1 121 ? -9.756  -27.744 -2.300  1.00 19.73 ? 121  ARG A CG  1 
ATOM   896  C  CD  . ARG A 1 121 ? -9.769  -26.330 -2.821  1.00 18.71 ? 121  ARG A CD  1 
ATOM   897  N  NE  . ARG A 1 121 ? -10.427 -25.471 -1.839  1.00 23.72 ? 121  ARG A NE  1 
ATOM   898  C  CZ  . ARG A 1 121 ? -9.891  -25.115 -0.676  1.00 26.54 ? 121  ARG A CZ  1 
ATOM   899  N  NH1 . ARG A 1 121 ? -8.668  -25.528 -0.339  1.00 21.29 ? 121  ARG A NH1 1 
ATOM   900  N  NH2 . ARG A 1 121 ? -10.578 -24.340 0.155   1.00 28.75 ? 121  ARG A NH2 1 
ATOM   901  N  N   . GLN A 1 122 ? -8.027  -32.147 -3.525  1.00 14.28 ? 122  GLN A N   1 
ATOM   902  C  CA  . GLN A 1 122 ? -7.895  -33.306 -4.393  1.00 18.85 ? 122  GLN A CA  1 
ATOM   903  C  C   . GLN A 1 122 ? -7.548  -34.516 -3.533  1.00 17.87 ? 122  GLN A C   1 
ATOM   904  O  O   . GLN A 1 122 ? -7.344  -34.403 -2.323  1.00 17.65 ? 122  GLN A O   1 
ATOM   905  C  CB  . GLN A 1 122 ? -6.850  -33.052 -5.484  1.00 21.43 ? 122  GLN A CB  1 
ATOM   906  C  CG  . GLN A 1 122 ? -5.475  -32.716 -4.944  1.00 16.05 ? 122  GLN A CG  1 
ATOM   907  C  CD  . GLN A 1 122 ? -4.673  -33.967 -4.609  1.00 16.91 ? 122  GLN A CD  1 
ATOM   908  O  OE1 . GLN A 1 122 ? -4.468  -34.838 -5.465  1.00 15.32 ? 122  GLN A OE1 1 
ATOM   909  N  NE2 . GLN A 1 122 ? -4.214  -34.064 -3.362  1.00 12.68 ? 122  GLN A NE2 1 
ATOM   910  N  N   . GLU A 1 123 ? -7.501  -35.694 -4.151  1.00 16.76 ? 123  GLU A N   1 
ATOM   911  C  CA  . GLU A 1 123 ? -7.124  -36.869 -3.383  1.00 17.29 ? 123  GLU A CA  1 
ATOM   912  C  C   . GLU A 1 123 ? -6.301  -37.887 -4.161  1.00 18.49 ? 123  GLU A C   1 
ATOM   913  O  O   . GLU A 1 123 ? -6.116  -39.003 -3.662  1.00 18.98 ? 123  GLU A O   1 
ATOM   914  C  CB  . GLU A 1 123 ? -8.362  -37.552 -2.792  1.00 26.82 ? 123  GLU A CB  1 
ATOM   915  C  CG  . GLU A 1 123 ? -9.411  -37.964 -3.807  1.00 23.06 ? 123  GLU A CG  1 
ATOM   916  C  CD  . GLU A 1 123 ? -10.656 -38.407 -3.113  1.00 29.40 ? 123  GLU A CD  1 
ATOM   917  O  OE1 . GLU A 1 123 ? -10.853 -39.635 -2.957  1.00 28.43 ? 123  GLU A OE1 1 
ATOM   918  O  OE2 . GLU A 1 123 ? -11.410 -37.516 -2.675  1.00 33.34 ? 123  GLU A OE2 1 
ATOM   919  N  N   . LYS A 1 124 ? -5.798  -37.557 -5.351  1.00 17.17 ? 124  LYS A N   1 
ATOM   920  C  CA  . LYS A 1 124 ? -4.906  -38.503 -6.021  1.00 18.42 ? 124  LYS A CA  1 
ATOM   921  C  C   . LYS A 1 124 ? -3.514  -38.476 -5.409  1.00 20.01 ? 124  LYS A C   1 
ATOM   922  O  O   . LYS A 1 124 ? -2.863  -39.514 -5.298  1.00 21.45 ? 124  LYS A O   1 
ATOM   923  C  CB  . LYS A 1 124 ? -4.804  -38.189 -7.517  1.00 20.63 ? 124  LYS A CB  1 
ATOM   924  C  CG  . LYS A 1 124 ? -6.102  -37.743 -8.173  1.00 27.25 ? 124  LYS A CG  1 
ATOM   925  C  CD  . LYS A 1 124 ? -7.065  -38.900 -8.370  1.00 35.25 ? 124  LYS A CD  1 
ATOM   926  C  CE  . LYS A 1 124 ? -8.094  -38.568 -9.465  1.00 39.69 ? 124  LYS A CE  1 
ATOM   927  N  NZ  . LYS A 1 124 ? -9.255  -39.517 -9.471  1.00 41.54 ? 124  LYS A NZ  1 
ATOM   928  N  N   . THR A 1 125 ? -3.050  -37.298 -5.005  1.00 17.31 ? 125  THR A N   1 
ATOM   929  C  CA  . THR A 1 125 ? -1.657  -37.057 -4.655  1.00 16.27 ? 125  THR A CA  1 
ATOM   930  C  C   . THR A 1 125 ? -1.513  -36.895 -3.145  1.00 15.92 ? 125  THR A C   1 
ATOM   931  O  O   . THR A 1 125 ? -2.178  -36.042 -2.539  1.00 14.77 ? 125  THR A O   1 
ATOM   932  C  CB  . THR A 1 125 ? -1.137  -35.789 -5.352  1.00 14.47 ? 125  THR A CB  1 
ATOM   933  O  OG1 . THR A 1 125 ? -1.173  -35.960 -6.774  1.00 16.90 ? 125  THR A OG1 1 
ATOM   934  C  CG2 . THR A 1 125 ? 0.296   -35.463 -4.915  1.00 13.95 ? 125  THR A CG2 1 
ATOM   935  N  N   . ARG A 1 126 ? -0.611  -37.669 -2.558  1.00 15.38 ? 126  ARG A N   1 
ATOM   936  C  CA  . ARG A 1 126 ? -0.220  -37.524 -1.158  1.00 14.48 ? 126  ARG A CA  1 
ATOM   937  C  C   . ARG A 1 126 ? 1.122   -36.802 -1.107  1.00 15.23 ? 126  ARG A C   1 
ATOM   938  O  O   . ARG A 1 126 ? 2.090   -37.248 -1.731  1.00 15.16 ? 126  ARG A O   1 
ATOM   939  C  CB  . ARG A 1 126 ? -0.143  -38.900 -0.490  1.00 14.83 ? 126  ARG A CB  1 
ATOM   940  C  CG  . ARG A 1 126 ? 0.551   -38.993 0.852   1.00 13.74 ? 126  ARG A CG  1 
ATOM   941  C  CD  . ARG A 1 126 ? -0.056  -38.078 1.920   1.00 14.73 ? 126  ARG A CD  1 
ATOM   942  N  NE  . ARG A 1 126 ? -1.511  -38.182 2.065   1.00 14.45 ? 126  ARG A NE  1 
ATOM   943  C  CZ  . ARG A 1 126 ? -2.189  -37.697 3.109   1.00 16.97 ? 126  ARG A CZ  1 
ATOM   944  N  NH1 . ARG A 1 126 ? -1.530  -37.101 4.097   1.00 14.26 ? 126  ARG A NH1 1 
ATOM   945  N  NH2 . ARG A 1 126 ? -3.518  -37.812 3.180   1.00 14.07 ? 126  ARG A NH2 1 
ATOM   946  N  N   . LEU A 1 127 ? 1.174   -35.679 -0.382  1.00 15.44 ? 127  LEU A N   1 
ATOM   947  C  CA  . LEU A 1 127 ? 2.414   -34.939 -0.188  1.00 13.71 ? 127  LEU A CA  1 
ATOM   948  C  C   . LEU A 1 127 ? 3.010   -35.257 1.179   1.00 13.64 ? 127  LEU A C   1 
ATOM   949  O  O   . LEU A 1 127 ? 2.314   -35.192 2.201   1.00 15.11 ? 127  LEU A O   1 
ATOM   950  C  CB  . LEU A 1 127 ? 2.189   -33.428 -0.322  1.00 14.57 ? 127  LEU A CB  1 
ATOM   951  C  CG  . LEU A 1 127 ? 3.376   -32.552 0.115   1.00 14.34 ? 127  LEU A CG  1 
ATOM   952  C  CD1 . LEU A 1 127 ? 4.613   -32.799 -0.778  1.00 15.73 ? 127  LEU A CD1 1 
ATOM   953  C  CD2 . LEU A 1 127 ? 2.989   -31.064 0.158   1.00 12.07 ? 127  LEU A CD2 1 
ATOM   954  N  N   . ILE A 1 128 ? 4.293   -35.615 1.184   1.00 15.13 ? 128  ILE A N   1 
ATOM   955  C  CA  . ILE A 1 128 ? 5.128   -35.661 2.382   1.00 12.98 ? 128  ILE A CA  1 
ATOM   956  C  C   . ILE A 1 128 ? 6.088   -34.487 2.297   1.00 14.30 ? 128  ILE A C   1 
ATOM   957  O  O   . ILE A 1 128 ? 6.832   -34.361 1.316   1.00 13.26 ? 128  ILE A O   1 
ATOM   958  C  CB  . ILE A 1 128 ? 5.918   -36.972 2.488   1.00 15.18 ? 128  ILE A CB  1 
ATOM   959  C  CG1 . ILE A 1 128 ? 4.998   -38.197 2.418   1.00 16.71 ? 128  ILE A CG1 1 
ATOM   960  C  CG2 . ILE A 1 128 ? 6.728   -36.987 3.786   1.00 20.12 ? 128  ILE A CG2 1 
ATOM   961  C  CD1 . ILE A 1 128 ? 5.762   -39.541 2.398   1.00 18.13 ? 128  ILE A CD1 1 
ATOM   962  N  N   . GLY A 1 129 ? 6.089   -33.635 3.319   1.00 13.35 ? 129  GLY A N   1 
ATOM   963  C  CA  . GLY A 1 129 ? 6.937   -32.467 3.308   1.00 14.76 ? 129  GLY A CA  1 
ATOM   964  C  C   . GLY A 1 129 ? 6.181   -31.163 3.131   1.00 13.58 ? 129  GLY A C   1 
ATOM   965  O  O   . GLY A 1 129 ? 4.948   -31.116 3.200   1.00 14.39 ? 129  GLY A O   1 
ATOM   966  N  N   . PRO A 1 130 ? 6.914   -30.073 2.857   1.00 10.92 ? 130  PRO A N   1 
ATOM   967  C  CA  . PRO A 1 130 ? 8.364   -30.077 2.564   1.00 12.93 ? 130  PRO A CA  1 
ATOM   968  C  C   . PRO A 1 130 ? 9.310   -30.148 3.777   1.00 15.11 ? 130  PRO A C   1 
ATOM   969  O  O   . PRO A 1 130 ? 8.918   -30.456 4.913   1.00 13.70 ? 130  PRO A O   1 
ATOM   970  C  CB  . PRO A 1 130 ? 8.562   -28.739 1.841   1.00 12.58 ? 130  PRO A CB  1 
ATOM   971  C  CG  . PRO A 1 130 ? 7.540   -27.829 2.480   1.00 13.23 ? 130  PRO A CG  1 
ATOM   972  C  CD  . PRO A 1 130 ? 6.326   -28.727 2.728   1.00 12.57 ? 130  PRO A CD  1 
ATOM   973  N  N   . ASN A 1 131 ? 10.580  -29.844 3.518   1.00 14.37 ? 131  ASN A N   1 
ATOM   974  C  CA  . ASN A 1 131 ? 11.609  -29.785 4.563   1.00 12.66 ? 131  ASN A CA  1 
ATOM   975  C  C   . ASN A 1 131 ? 11.646  -31.068 5.390   1.00 16.90 ? 131  ASN A C   1 
ATOM   976  O  O   . ASN A 1 131 ? 11.648  -31.045 6.631   1.00 17.50 ? 131  ASN A O   1 
ATOM   977  C  CB  . ASN A 1 131 ? 11.403  -28.560 5.464   1.00 15.79 ? 131  ASN A CB  1 
ATOM   978  C  CG  . ASN A 1 131 ? 12.609  -28.291 6.368   1.00 16.80 ? 131  ASN A CG  1 
ATOM   979  O  OD1 . ASN A 1 131 ? 13.712  -28.731 6.074   1.00 13.68 ? 131  ASN A OD1 1 
ATOM   980  N  ND2 . ASN A 1 131 ? 12.396  -27.567 7.458   1.00 17.02 ? 131  ASN A ND2 1 
ATOM   981  N  N   . CYS A 1 132 ? 11.688  -32.203 4.699   1.00 13.33 ? 132  CYS A N   1 
ATOM   982  C  CA  . CYS A 1 132 ? 11.616  -33.500 5.352   1.00 14.08 ? 132  CYS A CA  1 
ATOM   983  C  C   . CYS A 1 132 ? 12.661  -34.455 4.802   1.00 15.74 ? 132  CYS A C   1 
ATOM   984  O  O   . CYS A 1 132 ? 13.153  -34.279 3.682   1.00 14.42 ? 132  CYS A O   1 
ATOM   985  C  CB  . CYS A 1 132 ? 10.220  -34.118 5.181   1.00 15.36 ? 132  CYS A CB  1 
ATOM   986  S  SG  . CYS A 1 132 ? 9.898   -34.877 3.587   1.00 18.46 ? 132  CYS A SG  1 
ATOM   987  N  N   . PRO A 1 133 ? 13.047  -35.474 5.586   1.00 14.70 ? 133  PRO A N   1 
ATOM   988  C  CA  . PRO A 1 133 ? 14.046  -36.432 5.110   1.00 17.16 ? 133  PRO A CA  1 
ATOM   989  C  C   . PRO A 1 133 ? 13.494  -37.445 4.120   1.00 15.65 ? 133  PRO A C   1 
ATOM   990  O  O   . PRO A 1 133 ? 14.288  -38.121 3.464   1.00 13.52 ? 133  PRO A O   1 
ATOM   991  C  CB  . PRO A 1 133 ? 14.489  -37.141 6.398   1.00 15.04 ? 133  PRO A CB  1 
ATOM   992  C  CG  . PRO A 1 133 ? 13.183  -37.155 7.223   1.00 16.31 ? 133  PRO A CG  1 
ATOM   993  C  CD  . PRO A 1 133 ? 12.640  -35.756 6.977   1.00 13.25 ? 133  PRO A CD  1 
ATOM   994  N  N   . GLY A 1 134 ? 12.186  -37.607 4.031   1.00 12.21 ? 134  GLY A N   1 
ATOM   995  C  CA  . GLY A 1 134 ? 11.580  -38.582 3.144   1.00 16.90 ? 134  GLY A CA  1 
ATOM   996  C  C   . GLY A 1 134 ? 10.950  -39.752 3.884   1.00 14.49 ? 134  GLY A C   1 
ATOM   997  O  O   . GLY A 1 134 ? 10.596  -39.674 5.062   1.00 15.62 ? 134  GLY A O   1 
ATOM   998  N  N   . VAL A 1 135 ? 10.822  -40.864 3.168   1.00 13.84 ? 135  VAL A N   1 
ATOM   999  C  CA  . VAL A 1 135 ? 10.118  -42.049 3.650   1.00 13.13 ? 135  VAL A CA  1 
ATOM   1000 C  C   . VAL A 1 135 ? 10.942  -43.266 3.253   1.00 15.65 ? 135  VAL A C   1 
ATOM   1001 O  O   . VAL A 1 135 ? 11.583  -43.269 2.192   1.00 14.33 ? 135  VAL A O   1 
ATOM   1002 C  CB  . VAL A 1 135 ? 8.674   -42.114 3.090   1.00 12.98 ? 135  VAL A CB  1 
ATOM   1003 C  CG1 . VAL A 1 135 ? 8.687   -42.001 1.550   1.00 14.61 ? 135  VAL A CG1 1 
ATOM   1004 C  CG2 . VAL A 1 135 ? 7.955   -43.392 3.520   1.00 13.26 ? 135  VAL A CG2 1 
ATOM   1005 N  N   . ILE A 1 136 ? 10.976  -44.276 4.131   1.00 12.33 ? 136  ILE A N   1 
ATOM   1006 C  CA  . ILE A 1 136 ? 11.703  -45.510 3.848   1.00 16.20 ? 136  ILE A CA  1 
ATOM   1007 C  C   . ILE A 1 136 ? 10.909  -46.716 4.348   1.00 16.38 ? 136  ILE A C   1 
ATOM   1008 O  O   . ILE A 1 136 ? 10.395  -46.724 5.470   1.00 13.97 ? 136  ILE A O   1 
ATOM   1009 C  CB  . ILE A 1 136 ? 13.136  -45.509 4.430   1.00 17.75 ? 136  ILE A CB  1 
ATOM   1010 C  CG1 . ILE A 1 136 ? 13.852  -46.820 4.062   1.00 19.75 ? 136  ILE A CG1 1 
ATOM   1011 C  CG2 . ILE A 1 136 ? 13.152  -45.293 5.956   1.00 20.37 ? 136  ILE A CG2 1 
ATOM   1012 C  CD1 . ILE A 1 136 ? 15.379  -46.746 4.168   1.00 18.13 ? 136  ILE A CD1 1 
ATOM   1013 N  N   . ASN A 1 137 ? 10.797  -47.725 3.492   1.00 18.55 ? 137  ASN A N   1 
ATOM   1014 C  CA  . ASN A 1 137 ? 10.355  -49.070 3.845   1.00 16.61 ? 137  ASN A CA  1 
ATOM   1015 C  C   . ASN A 1 137 ? 11.584  -49.957 3.709   1.00 18.65 ? 137  ASN A C   1 
ATOM   1016 O  O   . ASN A 1 137 ? 11.926  -50.372 2.587   1.00 19.88 ? 137  ASN A O   1 
ATOM   1017 C  CB  . ASN A 1 137 ? 9.234   -49.524 2.902   1.00 18.52 ? 137  ASN A CB  1 
ATOM   1018 C  CG  . ASN A 1 137 ? 8.787   -50.960 3.133   1.00 22.28 ? 137  ASN A CG  1 
ATOM   1019 O  OD1 . ASN A 1 137 ? 9.426   -51.737 3.837   1.00 20.21 ? 137  ASN A OD1 1 
ATOM   1020 N  ND2 . ASN A 1 137 ? 7.681   -51.315 2.513   1.00 18.13 ? 137  ASN A ND2 1 
ATOM   1021 N  N   . PRO A 1 138 ? 12.288  -50.260 4.805   1.00 18.77 ? 138  PRO A N   1 
ATOM   1022 C  CA  . PRO A 1 138 ? 13.649  -50.805 4.688   1.00 21.32 ? 138  PRO A CA  1 
ATOM   1023 C  C   . PRO A 1 138 ? 13.688  -52.085 3.865   1.00 21.76 ? 138  PRO A C   1 
ATOM   1024 O  O   . PRO A 1 138 ? 12.841  -52.964 4.017   1.00 22.52 ? 138  PRO A O   1 
ATOM   1025 C  CB  . PRO A 1 138 ? 14.046  -51.057 6.147   1.00 23.35 ? 138  PRO A CB  1 
ATOM   1026 C  CG  . PRO A 1 138 ? 13.255  -49.977 6.908   1.00 19.14 ? 138  PRO A CG  1 
ATOM   1027 C  CD  . PRO A 1 138 ? 11.923  -49.985 6.208   1.00 18.77 ? 138  PRO A CD  1 
ATOM   1028 N  N   . GLY A 1 139 ? 14.671  -52.166 2.973   1.00 26.68 ? 139  GLY A N   1 
ATOM   1029 C  CA  . GLY A 1 139 ? 14.806  -53.276 2.047   1.00 23.31 ? 139  GLY A CA  1 
ATOM   1030 C  C   . GLY A 1 139 ? 13.801  -53.323 0.917   1.00 28.12 ? 139  GLY A C   1 
ATOM   1031 O  O   . GLY A 1 139 ? 13.882  -54.234 0.086   1.00 26.55 ? 139  GLY A O   1 
ATOM   1032 N  N   . GLU A 1 140 ? 12.843  -52.398 0.854   1.00 23.60 ? 140  GLU A N   1 
ATOM   1033 C  CA  . GLU A 1 140 ? 11.870  -52.390 -0.236  1.00 22.57 ? 140  GLU A CA  1 
ATOM   1034 C  C   . GLU A 1 140 ? 11.858  -51.090 -1.023  1.00 23.68 ? 140  GLU A C   1 
ATOM   1035 O  O   . GLU A 1 140 ? 11.751  -51.122 -2.247  1.00 20.90 ? 140  GLU A O   1 
ATOM   1036 C  CB  . GLU A 1 140 ? 10.458  -52.667 0.290   1.00 21.28 ? 140  GLU A CB  1 
ATOM   1037 C  CG  . GLU A 1 140 ? 10.159  -54.135 0.581   1.00 25.70 ? 140  GLU A CG  1 
ATOM   1038 C  CD  . GLU A 1 140 ? 8.660   -54.432 0.603   1.00 33.07 ? 140  GLU A CD  1 
ATOM   1039 O  OE1 . GLU A 1 140 ? 7.952   -54.106 -0.384  1.00 31.31 ? 140  GLU A OE1 1 
ATOM   1040 O  OE2 . GLU A 1 140 ? 8.180   -54.996 1.615   1.00 40.14 ? 140  GLU A OE2 1 
ATOM   1041 N  N   . CYS A 1 141 ? 11.965  -49.941 -0.359  1.00 18.87 ? 141  CYS A N   1 
ATOM   1042 C  CA  . CYS A 1 141 ? 11.905  -48.679 -1.084  1.00 17.70 ? 141  CYS A CA  1 
ATOM   1043 C  C   . CYS A 1 141 ? 12.367  -47.517 -0.213  1.00 17.01 ? 141  CYS A C   1 
ATOM   1044 O  O   . CYS A 1 141 ? 11.790  -47.286 0.854   1.00 18.44 ? 141  CYS A O   1 
ATOM   1045 C  CB  . CYS A 1 141 ? 10.482  -48.410 -1.581  1.00 15.24 ? 141  CYS A CB  1 
ATOM   1046 S  SG  . CYS A 1 141 ? 10.336  -46.865 -2.540  1.00 17.33 ? 141  CYS A SG  1 
ATOM   1047 N  N   . LYS A 1 142 ? 13.353  -46.756 -0.683  1.00 18.36 ? 142  LYS A N   1 
ATOM   1048 C  CA  . LYS A 1 142 ? 13.857  -45.575 0.008   1.00 17.49 ? 142  LYS A CA  1 
ATOM   1049 C  C   . LYS A 1 142 ? 13.739  -44.344 -0.879  1.00 20.65 ? 142  LYS A C   1 
ATOM   1050 O  O   . LYS A 1 142 ? 14.234  -44.335 -2.011  1.00 18.45 ? 142  LYS A O   1 
ATOM   1051 C  CB  . LYS A 1 142 ? 15.318  -45.759 0.435   1.00 20.13 ? 142  LYS A CB  1 
ATOM   1052 C  CG  . LYS A 1 142 ? 15.986  -44.464 0.881   1.00 22.96 ? 142  LYS A CG  1 
ATOM   1053 C  CD  . LYS A 1 142 ? 17.215  -44.737 1.731   1.00 29.04 ? 142  LYS A CD  1 
ATOM   1054 C  CE  . LYS A 1 142 ? 18.504  -44.611 0.966   1.00 31.88 ? 142  LYS A CE  1 
ATOM   1055 N  NZ  . LYS A 1 142 ? 19.562  -43.982 1.826   1.00 27.84 ? 142  LYS A NZ  1 
ATOM   1056 N  N   . ILE A 1 143 ? 13.094  -43.307 -0.349  1.00 16.83 ? 143  ILE A N   1 
ATOM   1057 C  CA  . ILE A 1 143 ? 12.895  -42.030 -1.034  1.00 17.93 ? 143  ILE A CA  1 
ATOM   1058 C  C   . ILE A 1 143 ? 13.329  -40.953 -0.046  1.00 16.81 ? 143  ILE A C   1 
ATOM   1059 O  O   . ILE A 1 143 ? 12.571  -40.603 0.867   1.00 18.39 ? 143  ILE A O   1 
ATOM   1060 C  CB  . ILE A 1 143 ? 11.440  -41.812 -1.469  1.00 18.51 ? 143  ILE A CB  1 
ATOM   1061 C  CG1 . ILE A 1 143 ? 10.925  -42.982 -2.330  1.00 20.30 ? 143  ILE A CG1 1 
ATOM   1062 C  CG2 . ILE A 1 143 ? 11.293  -40.484 -2.215  1.00 19.37 ? 143  ILE A CG2 1 
ATOM   1063 C  CD1 . ILE A 1 143 ? 9.438   -42.897 -2.628  1.00 16.71 ? 143  ILE A CD1 1 
ATOM   1064 N  N   . GLY A 1 144 ? 14.536  -40.439 -0.202  1.00 16.63 ? 144  GLY A N   1 
ATOM   1065 C  CA  . GLY A 1 144 ? 14.965  -39.333 0.633   1.00 18.62 ? 144  GLY A CA  1 
ATOM   1066 C  C   . GLY A 1 144 ? 16.448  -39.396 0.953   1.00 19.58 ? 144  GLY A C   1 
ATOM   1067 O  O   . GLY A 1 144 ? 17.234  -39.999 0.226   1.00 15.96 ? 144  GLY A O   1 
ATOM   1068 N  N   . ILE A 1 145 ? 16.801  -38.744 2.061   1.00 16.04 ? 145  ILE A N   1 
ATOM   1069 C  CA  . ILE A 1 145 ? 18.190  -38.436 2.371   1.00 20.82 ? 145  ILE A CA  1 
ATOM   1070 C  C   . ILE A 1 145 ? 18.710  -39.172 3.588   1.00 19.81 ? 145  ILE A C   1 
ATOM   1071 O  O   . ILE A 1 145 ? 19.848  -38.915 3.994   1.00 21.55 ? 145  ILE A O   1 
ATOM   1072 C  CB  . ILE A 1 145 ? 18.386  -36.923 2.561   1.00 21.80 ? 145  ILE A CB  1 
ATOM   1073 C  CG1 . ILE A 1 145 ? 17.504  -36.453 3.718   1.00 19.40 ? 145  ILE A CG1 1 
ATOM   1074 C  CG2 . ILE A 1 145 ? 18.079  -36.196 1.255   1.00 18.78 ? 145  ILE A CG2 1 
ATOM   1075 C  CD1 . ILE A 1 145 ? 17.952  -35.196 4.338   1.00 21.18 ? 145  ILE A CD1 1 
ATOM   1076 N  N   . MET A 1 146 ? 17.919  -40.058 4.199   1.00 18.83 ? 146  MET A N   1 
ATOM   1077 C  CA  . MET A 1 146 ? 18.344  -40.690 5.437   1.00 19.73 ? 146  MET A CA  1 
ATOM   1078 C  C   . MET A 1 146 ? 19.621  -41.504 5.202   1.00 19.67 ? 146  MET A C   1 
ATOM   1079 O  O   . MET A 1 146 ? 19.852  -41.999 4.098   1.00 22.58 ? 146  MET A O   1 
ATOM   1080 C  CB  . MET A 1 146 ? 17.227  -41.576 6.000   1.00 17.76 ? 146  MET A CB  1 
ATOM   1081 C  CG  . MET A 1 146 ? 16.704  -42.682 5.068   1.00 20.97 ? 146  MET A CG  1 
ATOM   1082 S  SD  . MET A 1 146 ? 15.657  -42.150 3.671   1.00 25.29 ? 146  MET A SD  1 
ATOM   1083 C  CE  . MET A 1 146 ? 14.192  -41.537 4.536   1.00 18.82 ? 146  MET A CE  1 
ATOM   1084 N  N   . PRO A 1 147 ? 20.488  -41.620 6.205   1.00 21.06 ? 147  PRO A N   1 
ATOM   1085 C  CA  . PRO A 1 147 ? 21.772  -42.308 5.992   1.00 21.91 ? 147  PRO A CA  1 
ATOM   1086 C  C   . PRO A 1 147 ? 21.579  -43.804 5.808   1.00 27.68 ? 147  PRO A C   1 
ATOM   1087 O  O   . PRO A 1 147 ? 20.555  -44.378 6.183   1.00 24.95 ? 147  PRO A O   1 
ATOM   1088 C  CB  . PRO A 1 147 ? 22.568  -42.004 7.269   1.00 23.58 ? 147  PRO A CB  1 
ATOM   1089 C  CG  . PRO A 1 147 ? 21.547  -41.613 8.284   1.00 20.40 ? 147  PRO A CG  1 
ATOM   1090 C  CD  . PRO A 1 147 ? 20.400  -41.000 7.537   1.00 19.84 ? 147  PRO A CD  1 
ATOM   1091 N  N   . GLY A 1 148 ? 22.602  -44.439 5.208   1.00 25.97 ? 148  GLY A N   1 
ATOM   1092 C  CA  . GLY A 1 148 ? 22.570  -45.868 4.977   1.00 27.66 ? 148  GLY A CA  1 
ATOM   1093 C  C   . GLY A 1 148 ? 23.207  -46.655 6.115   1.00 29.68 ? 148  GLY A C   1 
ATOM   1094 O  O   . GLY A 1 148 ? 23.824  -46.094 7.023   1.00 27.38 ? 148  GLY A O   1 
ATOM   1095 N  N   . HIS A 1 149 ? 23.035  -47.977 6.044   1.00 24.19 ? 149  HIS A N   1 
ATOM   1096 C  CA  . HIS A 1 149 ? 23.610  -48.920 7.000   1.00 26.02 ? 149  HIS A CA  1 
ATOM   1097 C  C   . HIS A 1 149 ? 23.106  -48.693 8.420   1.00 28.62 ? 149  HIS A C   1 
ATOM   1098 O  O   . HIS A 1 149 ? 23.799  -49.005 9.387   1.00 28.50 ? 149  HIS A O   1 
ATOM   1099 C  CB  . HIS A 1 149 ? 25.144  -48.884 6.975   1.00 35.09 ? 149  HIS A CB  1 
ATOM   1100 N  N   . ILE A 1 150 ? 21.893  -48.170 8.581   1.00 24.93 ? 150  ILE A N   1 
ATOM   1101 C  CA  . ILE A 1 150 ? 21.310  -48.094 9.917   1.00 20.90 ? 150  ILE A CA  1 
ATOM   1102 C  C   . ILE A 1 150 ? 19.934  -48.725 10.011  1.00 21.00 ? 150  ILE A C   1 
ATOM   1103 O  O   . ILE A 1 150 ? 19.480  -49.014 11.131  1.00 17.87 ? 150  ILE A O   1 
ATOM   1104 C  CB  . ILE A 1 150 ? 21.264  -46.633 10.430  1.00 24.25 ? 150  ILE A CB  1 
ATOM   1105 C  CG1 . ILE A 1 150 ? 20.348  -45.765 9.563   1.00 27.17 ? 150  ILE A CG1 1 
ATOM   1106 C  CG2 . ILE A 1 150 ? 22.676  -46.034 10.517  1.00 21.25 ? 150  ILE A CG2 1 
ATOM   1107 C  CD1 . ILE A 1 150 ? 20.069  -44.370 10.177  1.00 21.97 ? 150  ILE A CD1 1 
ATOM   1108 N  N   . HIS A 1 151 ? 19.236  -48.987 8.906   1.00 21.68 ? 151  HIS A N   1 
ATOM   1109 C  CA  . HIS A 1 151 ? 17.870  -49.490 8.977   1.00 22.06 ? 151  HIS A CA  1 
ATOM   1110 C  C   . HIS A 1 151 ? 17.836  -51.015 9.014   1.00 24.51 ? 151  HIS A C   1 
ATOM   1111 O  O   . HIS A 1 151 ? 18.776  -51.699 8.597   1.00 23.94 ? 151  HIS A O   1 
ATOM   1112 C  CB  . HIS A 1 151 ? 17.048  -48.990 7.791   1.00 21.94 ? 151  HIS A CB  1 
ATOM   1113 C  CG  . HIS A 1 151 ? 17.002  -47.496 7.669   1.00 19.32 ? 151  HIS A CG  1 
ATOM   1114 N  ND1 . HIS A 1 151 ? 17.996  -46.767 7.052   1.00 19.55 ? 151  HIS A ND1 1 
ATOM   1115 C  CD2 . HIS A 1 151 ? 16.070  -46.597 8.069   1.00 16.83 ? 151  HIS A CD2 1 
ATOM   1116 C  CE1 . HIS A 1 151 ? 17.682  -45.483 7.077   1.00 18.20 ? 151  HIS A CE1 1 
ATOM   1117 N  NE2 . HIS A 1 151 ? 16.521  -45.351 7.694   1.00 17.40 ? 151  HIS A NE2 1 
ATOM   1118 N  N   . LYS A 1 152 ? 16.726  -51.546 9.520   1.00 19.57 ? 152  LYS A N   1 
ATOM   1119 C  CA  . LYS A 1 152 ? 16.502  -52.987 9.494   1.00 25.49 ? 152  LYS A CA  1 
ATOM   1120 C  C   . LYS A 1 152 ? 15.006  -53.212 9.374   1.00 24.48 ? 152  LYS A C   1 
ATOM   1121 O  O   . LYS A 1 152 ? 14.243  -52.683 10.186  1.00 20.35 ? 152  LYS A O   1 
ATOM   1122 C  CB  . LYS A 1 152 ? 17.064  -53.657 10.753  1.00 26.32 ? 152  LYS A CB  1 
ATOM   1123 C  CG  . LYS A 1 152 ? 17.426  -55.132 10.579  1.00 36.13 ? 152  LYS A CG  1 
ATOM   1124 C  CD  . LYS A 1 152 ? 16.203  -56.025 10.499  1.00 38.34 ? 152  LYS A CD  1 
ATOM   1125 C  CE  . LYS A 1 152 ? 16.385  -57.169 9.500   1.00 40.70 ? 152  LYS A CE  1 
ATOM   1126 N  NZ  . LYS A 1 152 ? 15.083  -57.864 9.235   1.00 28.59 ? 152  LYS A NZ  1 
ATOM   1127 N  N   . LYS A 1 153 ? 14.582  -53.975 8.363   1.00 19.86 ? 153  LYS A N   1 
ATOM   1128 C  CA  . LYS A 1 153 ? 13.157  -54.234 8.204   1.00 21.80 ? 153  LYS A CA  1 
ATOM   1129 C  C   . LYS A 1 153 ? 12.623  -54.919 9.456   1.00 22.02 ? 153  LYS A C   1 
ATOM   1130 O  O   . LYS A 1 153 ? 13.212  -55.882 9.949   1.00 23.68 ? 153  LYS A O   1 
ATOM   1131 C  CB  . LYS A 1 153 ? 12.894  -55.096 6.968   1.00 23.07 ? 153  LYS A CB  1 
ATOM   1132 C  CG  . LYS A 1 153 ? 11.428  -55.354 6.730   1.00 23.97 ? 153  LYS A CG  1 
ATOM   1133 C  CD  . LYS A 1 153 ? 10.685  -54.113 6.208   1.00 24.45 ? 153  LYS A CD  1 
ATOM   1134 C  CE  . LYS A 1 153 ? 9.162   -54.296 6.343   1.00 22.76 ? 153  LYS A CE  1 
ATOM   1135 N  NZ  . LYS A 1 153 ? 8.388   -53.130 5.817   1.00 27.00 ? 153  LYS A NZ  1 
ATOM   1136 N  N   . GLY A 1 154 ? 11.546  -54.379 10.008  1.00 19.15 ? 154  GLY A N   1 
ATOM   1137 C  CA  . GLY A 1 154 ? 11.081  -54.849 11.290  1.00 19.31 ? 154  GLY A CA  1 
ATOM   1138 C  C   . GLY A 1 154 ? 9.687   -54.375 11.643  1.00 20.88 ? 154  GLY A C   1 
ATOM   1139 O  O   . GLY A 1 154 ? 8.837   -54.190 10.768  1.00 20.31 ? 154  GLY A O   1 
ATOM   1140 N  N   . ARG A 1 155 ? 9.474   -54.122 12.932  1.00 18.51 ? 155  ARG A N   1 
ATOM   1141 C  CA  . ARG A 1 155 ? 8.148   -54.088 13.525  1.00 20.90 ? 155  ARG A CA  1 
ATOM   1142 C  C   . ARG A 1 155 ? 7.671   -52.707 13.947  1.00 20.90 ? 155  ARG A C   1 
ATOM   1143 O  O   . ARG A 1 155 ? 6.513   -52.589 14.361  1.00 19.70 ? 155  ARG A O   1 
ATOM   1144 C  CB  . ARG A 1 155 ? 8.115   -55.004 14.765  1.00 22.78 ? 155  ARG A CB  1 
ATOM   1145 C  CG  . ARG A 1 155 ? 8.896   -56.308 14.585  1.00 34.16 ? 155  ARG A CG  1 
ATOM   1146 C  CD  . ARG A 1 155 ? 9.398   -56.883 15.920  1.00 31.55 ? 155  ARG A CD  1 
ATOM   1147 N  NE  . ARG A 1 155 ? 8.328   -57.496 16.689  1.00 31.78 ? 155  ARG A NE  1 
ATOM   1148 C  CZ  . ARG A 1 155 ? 8.499   -58.140 17.846  1.00 40.67 ? 155  ARG A CZ  1 
ATOM   1149 N  NH1 . ARG A 1 155 ? 9.710   -58.251 18.391  1.00 34.11 ? 155  ARG A NH1 1 
ATOM   1150 N  NH2 . ARG A 1 155 ? 7.449   -58.668 18.463  1.00 33.50 ? 155  ARG A NH2 1 
ATOM   1151 N  N   . ILE A 1 156 ? 8.518   -51.675 13.893  1.00 17.48 ? 156  ILE A N   1 
ATOM   1152 C  CA  . ILE A 1 156 ? 8.224   -50.373 14.481  1.00 13.37 ? 156  ILE A CA  1 
ATOM   1153 C  C   . ILE A 1 156 ? 7.971   -49.354 13.372  1.00 16.52 ? 156  ILE A C   1 
ATOM   1154 O  O   . ILE A 1 156 ? 8.791   -49.194 12.460  1.00 16.61 ? 156  ILE A O   1 
ATOM   1155 C  CB  . ILE A 1 156 ? 9.370   -49.918 15.396  1.00 16.84 ? 156  ILE A CB  1 
ATOM   1156 C  CG1 . ILE A 1 156 ? 9.503   -50.891 16.570  1.00 19.99 ? 156  ILE A CG1 1 
ATOM   1157 C  CG2 . ILE A 1 156 ? 9.135   -48.529 15.922  1.00 13.35 ? 156  ILE A CG2 1 
ATOM   1158 C  CD1 . ILE A 1 156 ? 10.676  -50.586 17.397  1.00 25.29 ? 156  ILE A CD1 1 
ATOM   1159 N  N   . GLY A 1 157 ? 6.838   -48.665 13.448  1.00 14.35 ? 157  GLY A N   1 
ATOM   1160 C  CA  . GLY A 1 157 ? 6.588   -47.529 12.576  1.00 16.89 ? 157  GLY A CA  1 
ATOM   1161 C  C   . GLY A 1 157 ? 7.029   -46.239 13.249  1.00 15.84 ? 157  GLY A C   1 
ATOM   1162 O  O   . GLY A 1 157 ? 6.766   -46.013 14.428  1.00 18.56 ? 157  GLY A O   1 
ATOM   1163 N  N   . ILE A 1 158 ? 7.721   -45.400 12.494  1.00 13.75 ? 158  ILE A N   1 
ATOM   1164 C  CA  . ILE A 1 158 ? 8.274   -44.169 13.038  1.00 14.92 ? 158  ILE A CA  1 
ATOM   1165 C  C   . ILE A 1 158 ? 7.686   -42.996 12.264  1.00 13.23 ? 158  ILE A C   1 
ATOM   1166 O  O   . ILE A 1 158 ? 7.664   -43.003 11.027  1.00 14.89 ? 158  ILE A O   1 
ATOM   1167 C  CB  . ILE A 1 158 ? 9.816   -44.171 12.991  1.00 13.80 ? 158  ILE A CB  1 
ATOM   1168 C  CG1 . ILE A 1 158 ? 10.347  -45.381 13.784  1.00 16.20 ? 158  ILE A CG1 1 
ATOM   1169 C  CG2 . ILE A 1 158 ? 10.388  -42.825 13.512  1.00 14.20 ? 158  ILE A CG2 1 
ATOM   1170 C  CD1 . ILE A 1 158 ? 11.841  -45.600 13.673  1.00 17.66 ? 158  ILE A CD1 1 
ATOM   1171 N  N   . VAL A 1 159 ? 7.170   -42.010 12.989  1.00 15.90 ? 159  VAL A N   1 
ATOM   1172 C  CA  . VAL A 1 159 ? 6.763   -40.750 12.372  1.00 14.81 ? 159  VAL A CA  1 
ATOM   1173 C  C   . VAL A 1 159 ? 7.414   -39.620 13.155  1.00 15.58 ? 159  VAL A C   1 
ATOM   1174 O  O   . VAL A 1 159 ? 7.444   -39.643 14.392  1.00 13.22 ? 159  VAL A O   1 
ATOM   1175 C  CB  . VAL A 1 159 ? 5.224   -40.599 12.290  1.00 15.87 ? 159  VAL A CB  1 
ATOM   1176 C  CG1 . VAL A 1 159 ? 4.554   -40.787 13.648  1.00 13.63 ? 159  VAL A CG1 1 
ATOM   1177 C  CG2 . VAL A 1 159 ? 4.835   -39.263 11.635  1.00 12.91 ? 159  VAL A CG2 1 
ATOM   1178 N  N   . SER A 1 160 ? 7.979   -38.651 12.434  1.00 11.32 ? 160  SER A N   1 
ATOM   1179 C  CA  . SER A 1 160 ? 8.852   -37.681 13.076  1.00 14.05 ? 160  SER A CA  1 
ATOM   1180 C  C   . SER A 1 160 ? 8.780   -36.345 12.351  1.00 13.63 ? 160  SER A C   1 
ATOM   1181 O  O   . SER A 1 160 ? 8.771   -36.301 11.115  1.00 12.70 ? 160  SER A O   1 
ATOM   1182 C  CB  . SER A 1 160 ? 10.301  -38.197 13.085  1.00 13.01 ? 160  SER A CB  1 
ATOM   1183 O  OG  . SER A 1 160 ? 11.210  -37.205 13.540  1.00 14.86 ? 160  SER A OG  1 
ATOM   1184 N  N   . ARG A 1 161 ? 8.745   -35.261 13.128  1.00 14.09 ? 161  ARG A N   1 
ATOM   1185 C  CA  . ARG A 1 161 ? 8.901   -33.925 12.563  1.00 13.61 ? 161  ARG A CA  1 
ATOM   1186 C  C   . ARG A 1 161 ? 10.364  -33.558 12.371  1.00 16.20 ? 161  ARG A C   1 
ATOM   1187 O  O   . ARG A 1 161 ? 10.653  -32.472 11.864  1.00 21.88 ? 161  ARG A O   1 
ATOM   1188 C  CB  . ARG A 1 161 ? 8.221   -32.878 13.456  1.00 15.66 ? 161  ARG A CB  1 
ATOM   1189 C  CG  . ARG A 1 161 ? 6.711   -32.816 13.344  1.00 15.91 ? 161  ARG A CG  1 
ATOM   1190 C  CD  . ARG A 1 161 ? 6.115   -31.908 14.418  1.00 19.66 ? 161  ARG A CD  1 
ATOM   1191 N  NE  . ARG A 1 161 ? 6.477   -30.500 14.273  1.00 15.28 ? 161  ARG A NE  1 
ATOM   1192 C  CZ  . ARG A 1 161 ? 6.440   -29.610 15.261  1.00 16.23 ? 161  ARG A CZ  1 
ATOM   1193 N  NH1 . ARG A 1 161 ? 6.072   -29.965 16.490  1.00 15.64 ? 161  ARG A NH1 1 
ATOM   1194 N  NH2 . ARG A 1 161 ? 6.756   -28.352 15.019  1.00 18.94 ? 161  ARG A NH2 1 
ATOM   1195 N  N   . SER A 1 162 ? 11.289  -34.434 12.756  1.00 16.36 ? 162  SER A N   1 
ATOM   1196 C  CA  . SER A 1 162 ? 12.721  -34.170 12.640  1.00 20.66 ? 162  SER A CA  1 
ATOM   1197 C  C   . SER A 1 162 ? 13.409  -35.290 11.867  1.00 17.30 ? 162  SER A C   1 
ATOM   1198 O  O   . SER A 1 162 ? 13.287  -36.468 12.220  1.00 22.90 ? 162  SER A O   1 
ATOM   1199 C  CB  . SER A 1 162 ? 13.352  -34.015 14.038  1.00 16.83 ? 162  SER A CB  1 
ATOM   1200 O  OG  . SER A 1 162 ? 14.772  -33.992 13.978  1.00 21.70 ? 162  SER A OG  1 
ATOM   1201 N  N   . GLY A 1 163 ? 14.178  -34.926 10.846  1.00 21.46 ? 163  GLY A N   1 
ATOM   1202 C  CA  . GLY A 1 163 ? 14.957  -35.932 10.141  1.00 16.94 ? 163  GLY A CA  1 
ATOM   1203 C  C   . GLY A 1 163 ? 16.087  -36.510 10.977  1.00 18.25 ? 163  GLY A C   1 
ATOM   1204 O  O   . GLY A 1 163 ? 16.249  -37.732 11.062  1.00 18.53 ? 163  GLY A O   1 
ATOM   1205 N  N   . THR A 1 164 ? 16.903  -35.648 11.595  1.00 17.17 ? 164  THR A N   1 
ATOM   1206 C  CA  . THR A 1 164 ? 18.026  -36.180 12.371  1.00 16.59 ? 164  THR A CA  1 
ATOM   1207 C  C   . THR A 1 164 ? 17.552  -37.053 13.526  1.00 18.56 ? 164  THR A C   1 
ATOM   1208 O  O   . THR A 1 164 ? 18.222  -38.026 13.885  1.00 16.04 ? 164  THR A O   1 
ATOM   1209 C  CB  . THR A 1 164 ? 18.927  -35.055 12.895  1.00 20.31 ? 164  THR A CB  1 
ATOM   1210 O  OG1 . THR A 1 164 ? 18.139  -34.032 13.512  1.00 22.13 ? 164  THR A OG1 1 
ATOM   1211 C  CG2 . THR A 1 164 ? 19.798  -34.479 11.764  1.00 19.77 ? 164  THR A CG2 1 
ATOM   1212 N  N   . LEU A 1 165 ? 16.406  -36.721 14.136  1.00 18.41 ? 165  LEU A N   1 
ATOM   1213 C  CA  . LEU A 1 165 ? 15.898  -37.580 15.204  1.00 14.24 ? 165  LEU A CA  1 
ATOM   1214 C  C   . LEU A 1 165 ? 15.371  -38.890 14.659  1.00 17.74 ? 165  LEU A C   1 
ATOM   1215 O  O   . LEU A 1 165 ? 15.391  -39.910 15.366  1.00 18.11 ? 165  LEU A O   1 
ATOM   1216 C  CB  . LEU A 1 165 ? 14.807  -36.869 16.004  1.00 19.27 ? 165  LEU A CB  1 
ATOM   1217 C  CG  . LEU A 1 165 ? 15.369  -35.848 16.991  1.00 17.79 ? 165  LEU A CG  1 
ATOM   1218 C  CD1 . LEU A 1 165 ? 14.261  -35.167 17.797  1.00 12.42 ? 165  LEU A CD1 1 
ATOM   1219 C  CD2 . LEU A 1 165 ? 16.377  -36.528 17.905  1.00 15.06 ? 165  LEU A CD2 1 
ATOM   1220 N  N   . THR A 1 166 ? 14.888  -38.888 13.419  1.00 13.56 ? 166  THR A N   1 
ATOM   1221 C  CA  . THR A 1 166 ? 14.534  -40.155 12.796  1.00 17.50 ? 166  THR A CA  1 
ATOM   1222 C  C   . THR A 1 166 ? 15.745  -41.074 12.729  1.00 19.72 ? 166  THR A C   1 
ATOM   1223 O  O   . THR A 1 166 ? 15.647  -42.262 13.064  1.00 18.12 ? 166  THR A O   1 
ATOM   1224 C  CB  . THR A 1 166 ? 13.956  -39.920 11.403  1.00 20.60 ? 166  THR A CB  1 
ATOM   1225 O  OG1 . THR A 1 166 ? 12.622  -39.421 11.527  1.00 25.35 ? 166  THR A OG1 1 
ATOM   1226 C  CG2 . THR A 1 166 ? 13.912  -41.194 10.659  1.00 23.98 ? 166  THR A CG2 1 
ATOM   1227 N  N   . TYR A 1 167 ? 16.911  -40.531 12.341  1.00 15.80 ? 167  TYR A N   1 
ATOM   1228 C  CA  . TYR A 1 167 ? 18.095  -41.384 12.214  1.00 18.37 ? 167  TYR A CA  1 
ATOM   1229 C  C   . TYR A 1 167 ? 18.448  -42.008 13.557  1.00 17.57 ? 167  TYR A C   1 
ATOM   1230 O  O   . TYR A 1 167 ? 18.760  -43.200 13.632  1.00 16.61 ? 167  TYR A O   1 
ATOM   1231 C  CB  . TYR A 1 167 ? 19.290  -40.597 11.671  1.00 17.13 ? 167  TYR A CB  1 
ATOM   1232 C  CG  . TYR A 1 167 ? 18.993  -39.688 10.495  1.00 17.15 ? 167  TYR A CG  1 
ATOM   1233 C  CD1 . TYR A 1 167 ? 17.918  -39.932 9.637   1.00 16.69 ? 167  TYR A CD1 1 
ATOM   1234 C  CD2 . TYR A 1 167 ? 19.813  -38.593 10.229  1.00 16.85 ? 167  TYR A CD2 1 
ATOM   1235 C  CE1 . TYR A 1 167 ? 17.645  -39.091 8.572   1.00 16.51 ? 167  TYR A CE1 1 
ATOM   1236 C  CE2 . TYR A 1 167 ? 19.562  -37.758 9.162   1.00 18.71 ? 167  TYR A CE2 1 
ATOM   1237 C  CZ  . TYR A 1 167 ? 18.472  -38.011 8.337   1.00 19.40 ? 167  TYR A CZ  1 
ATOM   1238 O  OH  . TYR A 1 167 ? 18.209  -37.171 7.285   1.00 17.54 ? 167  TYR A OH  1 
ATOM   1239 N  N   . GLU A 1 168 ? 18.385  -41.207 14.628  1.00 17.53 ? 168  GLU A N   1 
ATOM   1240 C  CA  . GLU A 1 168 ? 18.610  -41.707 15.982  1.00 17.59 ? 168  GLU A CA  1 
ATOM   1241 C  C   . GLU A 1 168 ? 17.654  -42.843 16.323  1.00 17.84 ? 168  GLU A C   1 
ATOM   1242 O  O   . GLU A 1 168 ? 18.077  -43.890 16.822  1.00 21.15 ? 168  GLU A O   1 
ATOM   1243 C  CB  . GLU A 1 168 ? 18.445  -40.573 16.996  1.00 19.96 ? 168  GLU A CB  1 
ATOM   1244 C  CG  . GLU A 1 168 ? 19.688  -39.777 17.272  1.00 17.45 ? 168  GLU A CG  1 
ATOM   1245 C  CD  . GLU A 1 168 ? 20.763  -40.595 17.976  1.00 19.94 ? 168  GLU A CD  1 
ATOM   1246 O  OE1 . GLU A 1 168 ? 20.466  -41.662 18.559  1.00 21.04 ? 168  GLU A OE1 1 
ATOM   1247 O  OE2 . GLU A 1 168 ? 21.919  -40.157 17.955  1.00 27.85 ? 168  GLU A OE2 1 
ATOM   1248 N  N   . ALA A 1 169 ? 16.349  -42.636 16.097  1.00 18.51 ? 169  ALA A N   1 
ATOM   1249 C  CA  . ALA A 1 169 ? 15.376  -43.668 16.436  1.00 21.70 ? 169  ALA A CA  1 
ATOM   1250 C  C   . ALA A 1 169 ? 15.539  -44.900 15.557  1.00 19.24 ? 169  ALA A C   1 
ATOM   1251 O  O   . ALA A 1 169 ? 15.314  -46.027 16.018  1.00 16.50 ? 169  ALA A O   1 
ATOM   1252 C  CB  . ALA A 1 169 ? 13.955  -43.119 16.320  1.00 22.41 ? 169  ALA A CB  1 
ATOM   1253 N  N   . VAL A 1 170 ? 15.927  -44.717 14.297  1.00 15.26 ? 170  VAL A N   1 
ATOM   1254 C  CA  . VAL A 1 170 ? 16.191  -45.882 13.451  1.00 19.77 ? 170  VAL A CA  1 
ATOM   1255 C  C   . VAL A 1 170 ? 17.360  -46.676 14.022  1.00 18.41 ? 170  VAL A C   1 
ATOM   1256 O  O   . VAL A 1 170 ? 17.258  -47.882 14.276  1.00 18.43 ? 170  VAL A O   1 
ATOM   1257 C  CB  . VAL A 1 170 ? 16.448  -45.447 11.995  1.00 19.91 ? 170  VAL A CB  1 
ATOM   1258 C  CG1 . VAL A 1 170 ? 17.158  -46.564 11.208  1.00 17.59 ? 170  VAL A CG1 1 
ATOM   1259 C  CG2 . VAL A 1 170 ? 15.143  -45.029 11.323  1.00 15.96 ? 170  VAL A CG2 1 
ATOM   1260 N  N   . HIS A 1 171 ? 18.476  -45.986 14.262  1.00 20.61 ? 171  HIS A N   1 
ATOM   1261 C  CA  . HIS A 1 171 ? 19.677  -46.598 14.824  1.00 19.83 ? 171  HIS A CA  1 
ATOM   1262 C  C   . HIS A 1 171 ? 19.370  -47.321 16.132  1.00 21.02 ? 171  HIS A C   1 
ATOM   1263 O  O   . HIS A 1 171 ? 19.802  -48.460 16.349  1.00 17.73 ? 171  HIS A O   1 
ATOM   1264 C  CB  . HIS A 1 171 ? 20.724  -45.501 15.035  1.00 19.66 ? 171  HIS A CB  1 
ATOM   1265 C  CG  . HIS A 1 171 ? 22.123  -45.995 15.206  1.00 22.37 ? 171  HIS A CG  1 
ATOM   1266 N  ND1 . HIS A 1 171 ? 22.694  -46.938 14.376  1.00 30.34 ? 171  HIS A ND1 1 
ATOM   1267 C  CD2 . HIS A 1 171 ? 23.090  -45.625 16.076  1.00 21.14 ? 171  HIS A CD2 1 
ATOM   1268 C  CE1 . HIS A 1 171 ? 23.941  -47.155 14.755  1.00 22.98 ? 171  HIS A CE1 1 
ATOM   1269 N  NE2 . HIS A 1 171 ? 24.208  -46.364 15.778  1.00 25.98 ? 171  HIS A NE2 1 
ATOM   1270 N  N   . GLN A 1 172 ? 18.601  -46.678 17.010  1.00 18.69 ? 172  GLN A N   1 
ATOM   1271 C  CA  . GLN A 1 172 ? 18.301  -47.297 18.295  1.00 21.11 ? 172  GLN A CA  1 
ATOM   1272 C  C   . GLN A 1 172 ? 17.419  -48.536 18.142  1.00 21.17 ? 172  GLN A C   1 
ATOM   1273 O  O   . GLN A 1 172 ? 17.661  -49.549 18.805  1.00 21.79 ? 172  GLN A O   1 
ATOM   1274 C  CB  . GLN A 1 172 ? 17.663  -46.271 19.225  1.00 15.47 ? 172  GLN A CB  1 
ATOM   1275 C  CG  . GLN A 1 172 ? 18.627  -45.192 19.656  1.00 18.27 ? 172  GLN A CG  1 
ATOM   1276 C  CD  . GLN A 1 172 ? 17.929  -44.087 20.403  1.00 19.69 ? 172  GLN A CD  1 
ATOM   1277 O  OE1 . GLN A 1 172 ? 16.925  -44.317 21.102  1.00 17.56 ? 172  GLN A OE1 1 
ATOM   1278 N  NE2 . GLN A 1 172 ? 18.427  -42.870 20.242  1.00 15.61 ? 172  GLN A NE2 1 
ATOM   1279 N  N   . THR A 1 173 ? 16.400  -48.486 17.275  1.00 17.75 ? 173  THR A N   1 
ATOM   1280 C  CA  . THR A 1 173 ? 15.535  -49.651 17.121  1.00 19.62 ? 173  THR A CA  1 
ATOM   1281 C  C   . THR A 1 173 ? 16.214  -50.772 16.344  1.00 22.41 ? 173  THR A C   1 
ATOM   1282 O  O   . THR A 1 173 ? 15.886  -51.944 16.552  1.00 21.93 ? 173  THR A O   1 
ATOM   1283 C  CB  . THR A 1 173 ? 14.220  -49.283 16.441  1.00 17.71 ? 173  THR A CB  1 
ATOM   1284 O  OG1 . THR A 1 173 ? 14.488  -48.599 15.215  1.00 18.92 ? 173  THR A OG1 1 
ATOM   1285 C  CG2 . THR A 1 173 ? 13.393  -48.404 17.358  1.00 17.34 ? 173  THR A CG2 1 
ATOM   1286 N  N   . THR A 1 174 ? 17.143  -50.447 15.444  1.00 20.41 ? 174  THR A N   1 
ATOM   1287 C  CA  . THR A 1 174 ? 17.966  -51.503 14.855  1.00 19.43 ? 174  THR A CA  1 
ATOM   1288 C  C   . THR A 1 174 ? 18.869  -52.130 15.911  1.00 24.28 ? 174  THR A C   1 
ATOM   1289 O  O   . THR A 1 174 ? 18.998  -53.357 15.987  1.00 25.33 ? 174  THR A O   1 
ATOM   1290 C  CB  . THR A 1 174 ? 18.799  -50.935 13.697  1.00 19.45 ? 174  THR A CB  1 
ATOM   1291 O  OG1 . THR A 1 174 ? 17.927  -50.553 12.630  1.00 19.01 ? 174  THR A OG1 1 
ATOM   1292 C  CG2 . THR A 1 174 ? 19.835  -51.955 13.172  1.00 20.00 ? 174  THR A CG2 1 
ATOM   1293 N  N   . GLN A 1 175 ? 19.470  -51.301 16.763  1.00 21.85 ? 175  GLN A N   1 
ATOM   1294 C  CA  . GLN A 1 175 ? 20.437  -51.810 17.725  1.00 23.63 ? 175  GLN A CA  1 
ATOM   1295 C  C   . GLN A 1 175 ? 19.784  -52.673 18.801  1.00 25.77 ? 175  GLN A C   1 
ATOM   1296 O  O   . GLN A 1 175 ? 20.436  -53.584 19.323  1.00 24.50 ? 175  GLN A O   1 
ATOM   1297 C  CB  . GLN A 1 175 ? 21.209  -50.643 18.337  1.00 21.88 ? 175  GLN A CB  1 
ATOM   1298 C  CG  . GLN A 1 175 ? 22.188  -50.027 17.335  1.00 31.73 ? 175  GLN A CG  1 
ATOM   1299 C  CD  . GLN A 1 175 ? 23.372  -49.330 17.977  1.00 34.51 ? 175  GLN A CD  1 
ATOM   1300 O  OE1 . GLN A 1 175 ? 23.215  -48.560 18.920  1.00 36.66 ? 175  GLN A OE1 1 
ATOM   1301 N  NE2 . GLN A 1 175 ? 24.571  -49.601 17.458  1.00 38.53 ? 175  GLN A NE2 1 
ATOM   1302 N  N   . VAL A 1 176 ? 18.509  -52.428 19.141  1.00 20.87 ? 176  VAL A N   1 
ATOM   1303 C  CA  . VAL A 1 176 ? 17.818  -53.317 20.071  1.00 24.49 ? 176  VAL A CA  1 
ATOM   1304 C  C   . VAL A 1 176 ? 17.126  -54.484 19.367  1.00 28.36 ? 176  VAL A C   1 
ATOM   1305 O  O   . VAL A 1 176 ? 16.454  -55.284 20.032  1.00 24.85 ? 176  VAL A O   1 
ATOM   1306 C  CB  . VAL A 1 176 ? 16.787  -52.582 20.964  1.00 23.67 ? 176  VAL A CB  1 
ATOM   1307 C  CG1 . VAL A 1 176 ? 17.478  -51.551 21.877  1.00 20.38 ? 176  VAL A CG1 1 
ATOM   1308 C  CG2 . VAL A 1 176 ? 15.669  -51.946 20.140  1.00 21.45 ? 176  VAL A CG2 1 
ATOM   1309 N  N   . GLY A 1 177 ? 17.263  -54.607 18.049  1.00 30.39 ? 177  GLY A N   1 
ATOM   1310 C  CA  . GLY A 1 177 ? 16.793  -55.786 17.336  1.00 26.85 ? 177  GLY A CA  1 
ATOM   1311 C  C   . GLY A 1 177 ? 15.345  -55.776 16.893  1.00 27.18 ? 177  GLY A C   1 
ATOM   1312 O  O   . GLY A 1 177 ? 14.841  -56.827 16.492  1.00 27.27 ? 177  GLY A O   1 
ATOM   1313 N  N   . LEU A 1 178 ? 14.664  -54.627 16.931  1.00 25.03 ? 178  LEU A N   1 
ATOM   1314 C  CA  . LEU A 1 178 ? 13.251  -54.561 16.560  1.00 25.08 ? 178  LEU A CA  1 
ATOM   1315 C  C   . LEU A 1 178 ? 13.016  -54.129 15.110  1.00 27.50 ? 178  LEU A C   1 
ATOM   1316 O  O   . LEU A 1 178 ? 12.018  -54.540 14.496  1.00 22.83 ? 178  LEU A O   1 
ATOM   1317 C  CB  . LEU A 1 178 ? 12.521  -53.580 17.481  1.00 27.09 ? 178  LEU A CB  1 
ATOM   1318 C  CG  . LEU A 1 178 ? 12.389  -53.986 18.946  1.00 28.61 ? 178  LEU A CG  1 
ATOM   1319 C  CD1 . LEU A 1 178 ? 12.092  -52.774 19.809  1.00 21.55 ? 178  LEU A CD1 1 
ATOM   1320 C  CD2 . LEU A 1 178 ? 11.293  -55.042 19.058  1.00 21.97 ? 178  LEU A CD2 1 
ATOM   1321 N  N   . GLY A 1 179 ? 13.883  -53.280 14.568  1.00 19.77 ? 179  GLY A N   1 
ATOM   1322 C  CA  . GLY A 1 179 ? 13.752  -52.836 13.196  1.00 17.65 ? 179  GLY A CA  1 
ATOM   1323 C  C   . GLY A 1 179 ? 12.525  -51.972 12.979  1.00 20.24 ? 179  GLY A C   1 
ATOM   1324 O  O   . GLY A 1 179 ? 11.722  -51.723 13.877  1.00 18.55 ? 179  GLY A O   1 
ATOM   1325 N  N   . GLN A 1 180 ? 12.379  -51.522 11.733  1.00 18.22 ? 180  GLN A N   1 
ATOM   1326 C  CA  . GLN A 1 180 ? 11.359  -50.557 11.347  1.00 17.40 ? 180  GLN A CA  1 
ATOM   1327 C  C   . GLN A 1 180 ? 10.481  -51.153 10.255  1.00 18.17 ? 180  GLN A C   1 
ATOM   1328 O  O   . GLN A 1 180 ? 10.989  -51.779 9.322   1.00 16.16 ? 180  GLN A O   1 
ATOM   1329 C  CB  . GLN A 1 180 ? 11.983  -49.257 10.833  1.00 18.34 ? 180  GLN A CB  1 
ATOM   1330 C  CG  . GLN A 1 180 ? 13.051  -48.660 11.737  1.00 17.54 ? 180  GLN A CG  1 
ATOM   1331 C  CD  . GLN A 1 180 ? 14.401  -49.314 11.539  1.00 21.58 ? 180  GLN A CD  1 
ATOM   1332 O  OE1 . GLN A 1 180 ? 14.763  -49.676 10.423  1.00 16.64 ? 180  GLN A OE1 1 
ATOM   1333 N  NE2 . GLN A 1 180 ? 15.153  -49.475 12.628  1.00 20.41 ? 180  GLN A NE2 1 
ATOM   1334 N  N   . SER A 1 181 ? 9.160   -50.957 10.366  1.00 15.83 ? 181  SER A N   1 
ATOM   1335 C  CA  . SER A 1 181 ? 8.283   -51.346 9.259   1.00 18.57 ? 181  SER A CA  1 
ATOM   1336 C  C   . SER A 1 181 ? 8.231   -50.259 8.183   1.00 18.50 ? 181  SER A C   1 
ATOM   1337 O  O   . SER A 1 181 ? 8.417   -50.533 6.994   1.00 16.71 ? 181  SER A O   1 
ATOM   1338 C  CB  . SER A 1 181 ? 6.879   -51.638 9.779   1.00 18.57 ? 181  SER A CB  1 
ATOM   1339 O  OG  . SER A 1 181 ? 6.406   -50.531 10.541  1.00 16.47 ? 181  SER A OG  1 
ATOM   1340 N  N   . LEU A 1 182 ? 7.967   -49.025 8.593   1.00 16.44 ? 182  LEU A N   1 
ATOM   1341 C  CA  . LEU A 1 182 ? 7.846   -47.885 7.698   1.00 19.06 ? 182  LEU A CA  1 
ATOM   1342 C  C   . LEU A 1 182 ? 8.195   -46.637 8.495   1.00 19.87 ? 182  LEU A C   1 
ATOM   1343 O  O   . LEU A 1 182 ? 7.740   -46.481 9.632   1.00 19.49 ? 182  LEU A O   1 
ATOM   1344 C  CB  . LEU A 1 182 ? 6.428   -47.764 7.123   1.00 17.37 ? 182  LEU A CB  1 
ATOM   1345 C  CG  . LEU A 1 182 ? 6.164   -46.564 6.212   1.00 20.31 ? 182  LEU A CG  1 
ATOM   1346 C  CD1 . LEU A 1 182 ? 6.963   -46.682 4.937   1.00 14.28 ? 182  LEU A CD1 1 
ATOM   1347 C  CD2 . LEU A 1 182 ? 4.666   -46.467 5.932   1.00 17.55 ? 182  LEU A CD2 1 
ATOM   1348 N  N   . CYS A 1 183 ? 8.992   -45.751 7.898   1.00 14.32 ? 183  CYS A N   1 
ATOM   1349 C  CA  . CYS A 1 183 ? 9.455   -44.549 8.579   1.00 16.16 ? 183  CYS A CA  1 
ATOM   1350 C  C   . CYS A 1 183 ? 9.146   -43.320 7.730   1.00 17.27 ? 183  CYS A C   1 
ATOM   1351 O  O   . CYS A 1 183 ? 9.553   -43.240 6.562   1.00 16.88 ? 183  CYS A O   1 
ATOM   1352 C  CB  . CYS A 1 183 ? 10.951  -44.648 8.887   1.00 21.34 ? 183  CYS A CB  1 
ATOM   1353 S  SG  . CYS A 1 183 ? 11.608  -43.166 9.660   1.00 33.45 ? 183  CYS A SG  1 
ATOM   1354 N  N   . VAL A 1 184 ? 8.417   -42.374 8.315   1.00 14.89 ? 184  VAL A N   1 
ATOM   1355 C  CA  . VAL A 1 184 ? 7.917   -41.202 7.607   1.00 16.78 ? 184  VAL A CA  1 
ATOM   1356 C  C   . VAL A 1 184 ? 8.412   -39.956 8.325   1.00 15.76 ? 184  VAL A C   1 
ATOM   1357 O  O   . VAL A 1 184 ? 8.070   -39.726 9.493   1.00 14.02 ? 184  VAL A O   1 
ATOM   1358 C  CB  . VAL A 1 184 ? 6.382   -41.210 7.512   1.00 13.63 ? 184  VAL A CB  1 
ATOM   1359 C  CG1 . VAL A 1 184 ? 5.893   -40.037 6.667   1.00 13.90 ? 184  VAL A CG1 1 
ATOM   1360 C  CG2 . VAL A 1 184 ? 5.918   -42.513 6.896   1.00 14.77 ? 184  VAL A CG2 1 
ATOM   1361 N  N   . GLY A 1 185 ? 9.209   -39.152 7.634   1.00 15.10 ? 185  GLY A N   1 
ATOM   1362 C  CA  . GLY A 1 185 ? 9.589   -37.870 8.196   1.00 13.36 ? 185  GLY A CA  1 
ATOM   1363 C  C   . GLY A 1 185 ? 8.663   -36.808 7.644   1.00 14.47 ? 185  GLY A C   1 
ATOM   1364 O  O   . GLY A 1 185 ? 8.715   -36.520 6.447   1.00 13.03 ? 185  GLY A O   1 
ATOM   1365 N  N   . ILE A 1 186 ? 7.778   -36.258 8.481   1.00 12.97 ? 186  ILE A N   1 
ATOM   1366 C  CA  . ILE A 1 186 ? 6.825   -35.258 7.995   1.00 14.03 ? 186  ILE A CA  1 
ATOM   1367 C  C   . ILE A 1 186 ? 7.422   -33.861 7.932   1.00 16.28 ? 186  ILE A C   1 
ATOM   1368 O  O   . ILE A 1 186 ? 6.762   -32.943 7.427   1.00 16.18 ? 186  ILE A O   1 
ATOM   1369 C  CB  . ILE A 1 186 ? 5.533   -35.244 8.838   1.00 18.50 ? 186  ILE A CB  1 
ATOM   1370 C  CG1 . ILE A 1 186 ? 5.788   -34.841 10.290  1.00 17.96 ? 186  ILE A CG1 1 
ATOM   1371 C  CG2 . ILE A 1 186 ? 4.853   -36.623 8.805   1.00 16.15 ? 186  ILE A CG2 1 
ATOM   1372 C  CD1 . ILE A 1 186 ? 4.477   -34.524 11.067  1.00 17.70 ? 186  ILE A CD1 1 
ATOM   1373 N  N   . GLY A 1 187 ? 8.651   -33.678 8.415   1.00 15.38 ? 187  GLY A N   1 
ATOM   1374 C  CA  . GLY A 1 187 ? 9.389   -32.446 8.222   1.00 16.70 ? 187  GLY A CA  1 
ATOM   1375 C  C   . GLY A 1 187 ? 9.095   -31.380 9.266   1.00 17.58 ? 187  GLY A C   1 
ATOM   1376 O  O   . GLY A 1 187 ? 8.197   -31.500 10.101  1.00 15.88 ? 187  GLY A O   1 
ATOM   1377 N  N   . GLY A 1 188 ? 9.865   -30.292 9.186   1.00 17.53 ? 188  GLY A N   1 
ATOM   1378 C  CA  . GLY A 1 188 ? 9.806   -29.251 10.198  1.00 20.17 ? 188  GLY A CA  1 
ATOM   1379 C  C   . GLY A 1 188 ? 9.123   -27.956 9.789   1.00 18.84 ? 188  GLY A C   1 
ATOM   1380 O  O   . GLY A 1 188 ? 9.333   -26.914 10.422  1.00 21.27 ? 188  GLY A O   1 
ATOM   1381 N  N   . ASP A 1 189 ? 8.322   -28.001 8.757   1.00 15.87 ? 189  ASP A N   1 
ATOM   1382 C  CA  . ASP A 1 189 ? 7.682   -26.771 8.319   1.00 16.02 ? 189  ASP A CA  1 
ATOM   1383 C  C   . ASP A 1 189 ? 6.262   -26.688 8.868   1.00 20.09 ? 189  ASP A C   1 
ATOM   1384 O  O   . ASP A 1 189 ? 5.632   -27.720 9.127   1.00 15.04 ? 189  ASP A O   1 
ATOM   1385 C  CB  . ASP A 1 189 ? 7.652   -26.687 6.793   1.00 16.03 ? 189  ASP A CB  1 
ATOM   1386 C  CG  . ASP A 1 189 ? 8.980   -26.218 6.217   1.00 20.19 ? 189  ASP A CG  1 
ATOM   1387 O  OD1 . ASP A 1 189 ? 9.923   -25.978 7.011   1.00 15.75 ? 189  ASP A OD1 1 
ATOM   1388 O  OD2 . ASP A 1 189 ? 9.077   -26.086 4.975   1.00 20.07 ? 189  ASP A OD2 1 
ATOM   1389 N  N   . PRO A 1 190 ? 5.753   -25.468 9.084   1.00 16.93 ? 190  PRO A N   1 
ATOM   1390 C  CA  . PRO A 1 190 ? 4.427   -25.332 9.693   1.00 18.31 ? 190  PRO A CA  1 
ATOM   1391 C  C   . PRO A 1 190 ? 3.298   -25.720 8.767   1.00 21.93 ? 190  PRO A C   1 
ATOM   1392 O  O   . PRO A 1 190 ? 2.218   -26.083 9.259   1.00 19.04 ? 190  PRO A O   1 
ATOM   1393 C  CB  . PRO A 1 190 ? 4.360   -23.849 10.052  1.00 19.52 ? 190  PRO A CB  1 
ATOM   1394 C  CG  . PRO A 1 190 ? 5.262   -23.191 9.044   1.00 17.18 ? 190  PRO A CG  1 
ATOM   1395 C  CD  . PRO A 1 190 ? 6.368   -24.155 8.792   1.00 19.38 ? 190  PRO A CD  1 
ATOM   1396 N  N   . PHE A 1 191 ? 3.500   -25.644 7.449   1.00 17.66 ? 191  PHE A N   1 
ATOM   1397 C  CA  . PHE A 1 191 ? 2.489   -26.032 6.469   1.00 16.68 ? 191  PHE A CA  1 
ATOM   1398 C  C   . PHE A 1 191 ? 3.063   -27.160 5.629   1.00 15.48 ? 191  PHE A C   1 
ATOM   1399 O  O   . PHE A 1 191 ? 3.994   -26.941 4.846   1.00 14.90 ? 191  PHE A O   1 
ATOM   1400 C  CB  . PHE A 1 191 ? 2.082   -24.852 5.591   1.00 16.28 ? 191  PHE A CB  1 
ATOM   1401 C  CG  . PHE A 1 191 ? 1.441   -23.736 6.360   1.00 18.25 ? 191  PHE A CG  1 
ATOM   1402 C  CD1 . PHE A 1 191 ? 0.118   -23.833 6.769   1.00 16.34 ? 191  PHE A CD1 1 
ATOM   1403 C  CD2 . PHE A 1 191 ? 2.167   -22.608 6.701   1.00 16.59 ? 191  PHE A CD2 1 
ATOM   1404 C  CE1 . PHE A 1 191 ? -0.492  -22.796 7.491   1.00 18.58 ? 191  PHE A CE1 1 
ATOM   1405 C  CE2 . PHE A 1 191 ? 1.570   -21.571 7.423   1.00 22.42 ? 191  PHE A CE2 1 
ATOM   1406 C  CZ  . PHE A 1 191 ? 0.234   -21.673 7.818   1.00 19.48 ? 191  PHE A CZ  1 
ATOM   1407 N  N   . ASN A 1 192 ? 2.494   -28.351 5.766   1.00 13.61 ? 192  ASN A N   1 
ATOM   1408 C  CA  . ASN A 1 192 ? 3.049   -29.541 5.122   1.00 13.49 ? 192  ASN A CA  1 
ATOM   1409 C  C   . ASN A 1 192 ? 1.906   -30.456 4.690   1.00 14.21 ? 192  ASN A C   1 
ATOM   1410 O  O   . ASN A 1 192 ? 0.736   -30.199 4.985   1.00 16.46 ? 192  ASN A O   1 
ATOM   1411 C  CB  . ASN A 1 192 ? 4.026   -30.228 6.076   1.00 12.87 ? 192  ASN A CB  1 
ATOM   1412 C  CG  . ASN A 1 192 ? 3.376   -30.653 7.373   1.00 16.19 ? 192  ASN A CG  1 
ATOM   1413 O  OD1 . ASN A 1 192 ? 2.309   -31.252 7.374   1.00 16.16 ? 192  ASN A OD1 1 
ATOM   1414 N  ND2 . ASN A 1 192 ? 4.019   -30.326 8.504   1.00 20.01 ? 192  ASN A ND2 1 
ATOM   1415 N  N   . GLY A 1 193 ? 2.241   -31.555 4.017   1.00 13.94 ? 193  GLY A N   1 
ATOM   1416 C  CA  . GLY A 1 193 ? 1.205   -32.386 3.416   1.00 15.08 ? 193  GLY A CA  1 
ATOM   1417 C  C   . GLY A 1 193 ? 0.688   -33.581 4.211   1.00 17.68 ? 193  GLY A C   1 
ATOM   1418 O  O   . GLY A 1 193 ? -0.298  -34.213 3.799   1.00 15.59 ? 193  GLY A O   1 
ATOM   1419 N  N   . THR A 1 194 ? 1.340   -33.914 5.335   1.00 14.15 ? 194  THR A N   1 
ATOM   1420 C  CA  . THR A 1 194 ? 1.054   -35.133 6.095   1.00 10.86 ? 194  THR A CA  1 
ATOM   1421 C  C   . THR A 1 194 ? 1.360   -34.862 7.565   1.00 17.74 ? 194  THR A C   1 
ATOM   1422 O  O   . THR A 1 194 ? 2.458   -34.397 7.879   1.00 12.93 ? 194  THR A O   1 
ATOM   1423 C  CB  . THR A 1 194 ? 1.911   -36.313 5.600   1.00 15.78 ? 194  THR A CB  1 
ATOM   1424 O  OG1 . THR A 1 194 ? 1.502   -36.721 4.291   1.00 13.84 ? 194  THR A OG1 1 
ATOM   1425 C  CG2 . THR A 1 194 ? 1.815   -37.498 6.536   1.00 12.67 ? 194  THR A CG2 1 
ATOM   1426 N  N   . ASP A 1 195 ? 0.408   -35.155 8.468   1.00 16.13 ? 195  ASP A N   1 
ATOM   1427 C  CA  . ASP A 1 195 ? 0.618   -34.905 9.893   1.00 13.86 ? 195  ASP A CA  1 
ATOM   1428 C  C   . ASP A 1 195 ? 0.836   -36.229 10.641  1.00 13.29 ? 195  ASP A C   1 
ATOM   1429 O  O   . ASP A 1 195 ? 0.928   -37.300 10.035  1.00 13.06 ? 195  ASP A O   1 
ATOM   1430 C  CB  . ASP A 1 195 ? -0.554  -34.084 10.462  1.00 12.70 ? 195  ASP A CB  1 
ATOM   1431 C  CG  . ASP A 1 195 ? -1.891  -34.851 10.458  1.00 15.41 ? 195  ASP A CG  1 
ATOM   1432 O  OD1 . ASP A 1 195 ? -1.947  -35.989 9.960   1.00 15.50 ? 195  ASP A OD1 1 
ATOM   1433 O  OD2 . ASP A 1 195 ? -2.895  -34.314 10.970  1.00 17.22 ? 195  ASP A OD2 1 
ATOM   1434 N  N   . PHE A 1 196 ? 0.929   -36.153 11.973  1.00 11.34 ? 196  PHE A N   1 
ATOM   1435 C  CA  . PHE A 1 196 ? 1.127   -37.360 12.771  1.00 13.96 ? 196  PHE A CA  1 
ATOM   1436 C  C   . PHE A 1 196 ? -0.025  -38.346 12.576  1.00 13.55 ? 196  PHE A C   1 
ATOM   1437 O  O   . PHE A 1 196 ? 0.190   -39.531 12.292  1.00 11.15 ? 196  PHE A O   1 
ATOM   1438 C  CB  . PHE A 1 196 ? 1.257   -37.000 14.253  1.00 12.03 ? 196  PHE A CB  1 
ATOM   1439 C  CG  . PHE A 1 196 ? 2.532   -36.270 14.610  1.00 13.82 ? 196  PHE A CG  1 
ATOM   1440 C  CD1 . PHE A 1 196 ? 3.766   -36.902 14.496  1.00 11.12 ? 196  PHE A CD1 1 
ATOM   1441 C  CD2 . PHE A 1 196 ? 2.488   -34.970 15.092  1.00 14.54 ? 196  PHE A CD2 1 
ATOM   1442 C  CE1 . PHE A 1 196 ? 4.932   -36.253 14.852  1.00 14.02 ? 196  PHE A CE1 1 
ATOM   1443 C  CE2 . PHE A 1 196 ? 3.651   -34.298 15.436  1.00 16.94 ? 196  PHE A CE2 1 
ATOM   1444 C  CZ  . PHE A 1 196 ? 4.879   -34.952 15.332  1.00 16.83 ? 196  PHE A CZ  1 
ATOM   1445 N  N   . ILE A 1 197 ? -1.257  -37.858 12.721  1.00 10.54 ? 197  ILE A N   1 
ATOM   1446 C  CA  . ILE A 1 197 ? -2.446  -38.713 12.687  1.00 15.43 ? 197  ILE A CA  1 
ATOM   1447 C  C   . ILE A 1 197 ? -2.531  -39.488 11.373  1.00 15.43 ? 197  ILE A C   1 
ATOM   1448 O  O   . ILE A 1 197 ? -2.886  -40.680 11.355  1.00 15.02 ? 197  ILE A O   1 
ATOM   1449 C  CB  . ILE A 1 197 ? -3.696  -37.850 12.953  1.00 15.63 ? 197  ILE A CB  1 
ATOM   1450 C  CG1 . ILE A 1 197 ? -3.752  -37.497 14.453  1.00 17.10 ? 197  ILE A CG1 1 
ATOM   1451 C  CG2 . ILE A 1 197 ? -4.974  -38.544 12.487  1.00 19.67 ? 197  ILE A CG2 1 
ATOM   1452 C  CD1 . ILE A 1 197 ? -4.870  -36.532 14.822  1.00 16.52 ? 197  ILE A CD1 1 
ATOM   1453 N  N   . ASP A 1 198 ? -2.195  -38.830 10.257  1.00 18.20 ? 198  ASP A N   1 
ATOM   1454 C  CA  . ASP A 1 198 ? -2.084  -39.518 8.971   1.00 15.14 ? 198  ASP A CA  1 
ATOM   1455 C  C   . ASP A 1 198 ? -1.243  -40.776 9.103   1.00 17.21 ? 198  ASP A C   1 
ATOM   1456 O  O   . ASP A 1 198 ? -1.672  -41.873 8.730   1.00 15.69 ? 198  ASP A O   1 
ATOM   1457 C  CB  . ASP A 1 198 ? -1.450  -38.590 7.922   1.00 14.40 ? 198  ASP A CB  1 
ATOM   1458 C  CG  . ASP A 1 198 ? -2.405  -37.544 7.393   1.00 17.83 ? 198  ASP A CG  1 
ATOM   1459 O  OD1 . ASP A 1 198 ? -3.637  -37.802 7.347   1.00 13.71 ? 198  ASP A OD1 1 
ATOM   1460 O  OD2 . ASP A 1 198 ? -1.909  -36.462 7.003   1.00 16.61 ? 198  ASP A OD2 1 
ATOM   1461 N  N   . CYS A 1 199 ? -0.036  -40.635 9.660   1.00 16.34 ? 199  CYS A N   1 
ATOM   1462 C  CA  . CYS A 1 199 ? 0.858   -41.786 9.772   1.00 16.94 ? 199  CYS A CA  1 
ATOM   1463 C  C   . CYS A 1 199 ? 0.368   -42.788 10.816  1.00 16.56 ? 199  CYS A C   1 
ATOM   1464 O  O   . CYS A 1 199 ? 0.517   -43.999 10.630  1.00 16.65 ? 199  CYS A O   1 
ATOM   1465 C  CB  . CYS A 1 199 ? 2.269   -41.313 10.102  1.00 17.18 ? 199  CYS A CB  1 
ATOM   1466 S  SG  . CYS A 1 199 ? 2.982   -40.254 8.826   1.00 14.75 ? 199  CYS A SG  1 
ATOM   1467 N  N   . LEU A 1 200 ? -0.211  -42.307 11.921  1.00 16.51 ? 200  LEU A N   1 
ATOM   1468 C  CA  . LEU A 1 200 ? -0.705  -43.225 12.946  1.00 15.29 ? 200  LEU A CA  1 
ATOM   1469 C  C   . LEU A 1 200 ? -1.804  -44.131 12.400  1.00 18.42 ? 200  LEU A C   1 
ATOM   1470 O  O   . LEU A 1 200 ? -1.870  -45.322 12.742  1.00 16.97 ? 200  LEU A O   1 
ATOM   1471 C  CB  . LEU A 1 200 ? -1.207  -42.443 14.151  1.00 15.06 ? 200  LEU A CB  1 
ATOM   1472 C  CG  . LEU A 1 200 ? -0.105  -41.640 14.860  1.00 18.09 ? 200  LEU A CG  1 
ATOM   1473 C  CD1 . LEU A 1 200 ? -0.690  -40.744 15.950  1.00 19.61 ? 200  LEU A CD1 1 
ATOM   1474 C  CD2 . LEU A 1 200 ? 0.928   -42.594 15.456  1.00 13.53 ? 200  LEU A CD2 1 
ATOM   1475 N  N   . GLU A 1 201 ? -2.678  -43.583 11.553  1.00 19.50 ? 201  GLU A N   1 
ATOM   1476 C  CA  . GLU A 1 201 ? -3.734  -44.386 10.950  1.00 19.40 ? 201  GLU A CA  1 
ATOM   1477 C  C   . GLU A 1 201 ? -3.146  -45.515 10.109  1.00 21.64 ? 201  GLU A C   1 
ATOM   1478 O  O   . GLU A 1 201 ? -3.592  -46.669 10.196  1.00 21.24 ? 201  GLU A O   1 
ATOM   1479 C  CB  . GLU A 1 201 ? -4.653  -43.483 10.112  1.00 24.49 ? 201  GLU A CB  1 
ATOM   1480 C  CG  . GLU A 1 201 ? -5.772  -44.217 9.370   1.00 33.14 ? 201  GLU A CG  1 
ATOM   1481 C  CD  . GLU A 1 201 ? -6.968  -44.525 10.258  1.00 34.27 ? 201  GLU A CD  1 
ATOM   1482 O  OE1 . GLU A 1 201 ? -7.953  -45.113 9.755   1.00 44.82 ? 201  GLU A OE1 1 
ATOM   1483 O  OE2 . GLU A 1 201 ? -6.930  -44.166 11.452  1.00 44.49 ? 201  GLU A OE2 1 
ATOM   1484 N  N   . ILE A 1 202 ? -2.133  -45.203 9.296   1.00 17.40 ? 202  ILE A N   1 
ATOM   1485 C  CA  . ILE A 1 202 ? -1.464  -46.232 8.513   1.00 16.39 ? 202  ILE A CA  1 
ATOM   1486 C  C   . ILE A 1 202 ? -0.787  -47.247 9.433   1.00 19.84 ? 202  ILE A C   1 
ATOM   1487 O  O   . ILE A 1 202 ? -0.898  -48.460 9.221   1.00 19.86 ? 202  ILE A O   1 
ATOM   1488 C  CB  . ILE A 1 202 ? -0.460  -45.599 7.535   1.00 18.96 ? 202  ILE A CB  1 
ATOM   1489 C  CG1 . ILE A 1 202 ? -1.189  -44.735 6.502   1.00 21.57 ? 202  ILE A CG1 1 
ATOM   1490 C  CG2 . ILE A 1 202 ? 0.351   -46.689 6.824   1.00 18.10 ? 202  ILE A CG2 1 
ATOM   1491 C  CD1 . ILE A 1 202 ? -2.117  -45.529 5.620   1.00 18.17 ? 202  ILE A CD1 1 
ATOM   1492 N  N   . PHE A 1 203 ? -0.092  -46.769 10.477  1.00 14.38 ? 203  PHE A N   1 
ATOM   1493 C  CA  . PHE A 1 203 ? 0.602   -47.676 11.394  1.00 17.85 ? 203  PHE A CA  1 
ATOM   1494 C  C   . PHE A 1 203 ? -0.377  -48.597 12.125  1.00 19.15 ? 203  PHE A C   1 
ATOM   1495 O  O   . PHE A 1 203 ? -0.160  -49.813 12.215  1.00 22.26 ? 203  PHE A O   1 
ATOM   1496 C  CB  . PHE A 1 203 ? 1.424   -46.878 12.415  1.00 16.81 ? 203  PHE A CB  1 
ATOM   1497 C  CG  . PHE A 1 203 ? 2.593   -46.129 11.828  1.00 13.13 ? 203  PHE A CG  1 
ATOM   1498 C  CD1 . PHE A 1 203 ? 3.143   -46.501 10.621  1.00 17.58 ? 203  PHE A CD1 1 
ATOM   1499 C  CD2 . PHE A 1 203 ? 3.148   -45.057 12.510  1.00 15.22 ? 203  PHE A CD2 1 
ATOM   1500 C  CE1 . PHE A 1 203 ? 4.230   -45.816 10.086  1.00 19.22 ? 203  PHE A CE1 1 
ATOM   1501 C  CE2 . PHE A 1 203 ? 4.240   -44.361 11.979  1.00 16.10 ? 203  PHE A CE2 1 
ATOM   1502 C  CZ  . PHE A 1 203 ? 4.769   -44.733 10.772  1.00 14.44 ? 203  PHE A CZ  1 
ATOM   1503 N  N   . LEU A 1 204 ? -1.446  -48.022 12.687  1.00 15.80 ? 204  LEU A N   1 
ATOM   1504 C  CA  . LEU A 1 204 ? -2.393  -48.808 13.471  1.00 22.01 ? 204  LEU A CA  1 
ATOM   1505 C  C   . LEU A 1 204 ? -3.098  -49.861 12.627  1.00 24.95 ? 204  LEU A C   1 
ATOM   1506 O  O   . LEU A 1 204 ? -3.526  -50.892 13.155  1.00 21.35 ? 204  LEU A O   1 
ATOM   1507 C  CB  . LEU A 1 204 ? -3.430  -47.901 14.132  1.00 18.08 ? 204  LEU A CB  1 
ATOM   1508 C  CG  . LEU A 1 204 ? -2.982  -47.043 15.306  1.00 19.33 ? 204  LEU A CG  1 
ATOM   1509 C  CD1 . LEU A 1 204 ? -4.136  -46.213 15.814  1.00 19.94 ? 204  LEU A CD1 1 
ATOM   1510 C  CD2 . LEU A 1 204 ? -2.394  -47.908 16.442  1.00 16.79 ? 204  LEU A CD2 1 
ATOM   1511 N  N   . ASN A 1 205 ? -3.248  -49.623 11.329  1.00 21.75 ? 205  ASN A N   1 
ATOM   1512 C  CA  . ASN A 1 205 ? -3.917  -50.586 10.470  1.00 22.32 ? 205  ASN A CA  1 
ATOM   1513 C  C   . ASN A 1 205 ? -2.949  -51.495 9.721   1.00 23.52 ? 205  ASN A C   1 
ATOM   1514 O  O   . ASN A 1 205 ? -3.389  -52.308 8.904   1.00 25.98 ? 205  ASN A O   1 
ATOM   1515 C  CB  . ASN A 1 205 ? -4.852  -49.852 9.505   1.00 28.14 ? 205  ASN A CB  1 
ATOM   1516 C  CG  . ASN A 1 205 ? -6.112  -49.338 10.205  1.00 30.50 ? 205  ASN A CG  1 
ATOM   1517 O  OD1 . ASN A 1 205 ? -6.946  -50.125 10.651  1.00 37.22 ? 205  ASN A OD1 1 
ATOM   1518 N  ND2 . ASN A 1 205 ? -6.243  -48.020 10.316  1.00 34.23 ? 205  ASN A ND2 1 
ATOM   1519 N  N   . ASP A 1 206 ? -1.652  -51.403 9.999   1.00 23.13 ? 206  ASP A N   1 
ATOM   1520 C  CA  . ASP A 1 206 ? -0.642  -52.186 9.299   1.00 22.97 ? 206  ASP A CA  1 
ATOM   1521 C  C   . ASP A 1 206 ? -0.236  -53.390 10.148  1.00 23.06 ? 206  ASP A C   1 
ATOM   1522 O  O   . ASP A 1 206 ? 0.320   -53.225 11.237  1.00 20.51 ? 206  ASP A O   1 
ATOM   1523 C  CB  . ASP A 1 206 ? 0.579   -51.325 8.993   1.00 25.04 ? 206  ASP A CB  1 
ATOM   1524 C  CG  . ASP A 1 206 ? 1.691   -52.122 8.358   1.00 25.14 ? 206  ASP A CG  1 
ATOM   1525 O  OD1 . ASP A 1 206 ? 1.370   -53.113 7.664   1.00 24.08 ? 206  ASP A OD1 1 
ATOM   1526 O  OD2 . ASP A 1 206 ? 2.879   -51.793 8.595   1.00 26.27 ? 206  ASP A OD2 1 
ATOM   1527 N  N   . SER A 1 207 ? -0.464  -54.602 9.631   1.00 22.03 ? 207  SER A N   1 
ATOM   1528 C  CA  . SER A 1 207 ? -0.155  -55.778 10.438  1.00 24.16 ? 207  SER A CA  1 
ATOM   1529 C  C   . SER A 1 207 ? 1.347   -55.932 10.670  1.00 26.00 ? 207  SER A C   1 
ATOM   1530 O  O   . SER A 1 207 ? 1.756   -56.491 11.692  1.00 25.97 ? 207  SER A O   1 
ATOM   1531 C  CB  . SER A 1 207 ? -0.736  -57.042 9.797   1.00 22.78 ? 207  SER A CB  1 
ATOM   1532 O  OG  . SER A 1 207 ? -0.282  -57.196 8.472   1.00 32.03 ? 207  SER A OG  1 
ATOM   1533 N  N   . ALA A 1 208 ? 2.185   -55.442 9.756   1.00 23.81 ? 208  ALA A N   1 
ATOM   1534 C  CA  . ALA A 1 208 ? 3.623   -55.558 9.982   1.00 24.58 ? 208  ALA A CA  1 
ATOM   1535 C  C   . ALA A 1 208 ? 4.130   -54.588 11.043  1.00 23.18 ? 208  ALA A C   1 
ATOM   1536 O  O   . ALA A 1 208 ? 5.229   -54.791 11.573  1.00 26.02 ? 208  ALA A O   1 
ATOM   1537 C  CB  . ALA A 1 208 ? 4.391   -55.342 8.675   1.00 25.19 ? 208  ALA A CB  1 
ATOM   1538 N  N   . THR A 1 209 ? 3.371   -53.541 11.367  1.00 21.93 ? 209  THR A N   1 
ATOM   1539 C  CA  . THR A 1 209 ? 3.758   -52.598 12.414  1.00 19.66 ? 209  THR A CA  1 
ATOM   1540 C  C   . THR A 1 209 ? 3.198   -53.068 13.752  1.00 18.56 ? 209  THR A C   1 
ATOM   1541 O  O   . THR A 1 209 ? 1.981   -53.177 13.914  1.00 21.41 ? 209  THR A O   1 
ATOM   1542 C  CB  . THR A 1 209 ? 3.263   -51.187 12.091  1.00 20.47 ? 209  THR A CB  1 
ATOM   1543 O  OG1 . THR A 1 209 ? 3.868   -50.727 10.868  1.00 17.80 ? 209  THR A OG1 1 
ATOM   1544 C  CG2 . THR A 1 209 ? 3.633   -50.223 13.225  1.00 17.48 ? 209  THR A CG2 1 
ATOM   1545 N  N   . GLU A 1 210 ? 4.078   -53.339 14.717  1.00 18.50 ? 210  GLU A N   1 
ATOM   1546 C  CA  . GLU A 1 210 ? 3.635   -53.796 16.031  1.00 20.20 ? 210  GLU A CA  1 
ATOM   1547 C  C   . GLU A 1 210 ? 3.811   -52.770 17.133  1.00 21.60 ? 210  GLU A C   1 
ATOM   1548 O  O   . GLU A 1 210 ? 3.227   -52.942 18.209  1.00 19.41 ? 210  GLU A O   1 
ATOM   1549 C  CB  . GLU A 1 210 ? 4.376   -55.077 16.429  1.00 23.12 ? 210  GLU A CB  1 
ATOM   1550 C  CG  . GLU A 1 210 ? 4.166   -56.196 15.432  1.00 24.64 ? 210  GLU A CG  1 
ATOM   1551 C  CD  . GLU A 1 210 ? 4.872   -57.471 15.837  1.00 30.69 ? 210  GLU A CD  1 
ATOM   1552 O  OE1 . GLU A 1 210 ? 5.182   -57.637 17.039  1.00 32.92 ? 210  GLU A OE1 1 
ATOM   1553 O  OE2 . GLU A 1 210 ? 5.120   -58.301 14.943  1.00 33.61 ? 210  GLU A OE2 1 
ATOM   1554 N  N   . GLY A 1 211 ? 4.609   -51.728 16.902  1.00 18.36 ? 211  GLY A N   1 
ATOM   1555 C  CA  . GLY A 1 211 ? 4.758   -50.643 17.849  1.00 16.51 ? 211  GLY A CA  1 
ATOM   1556 C  C   . GLY A 1 211 ? 5.059   -49.378 17.074  1.00 14.93 ? 211  GLY A C   1 
ATOM   1557 O  O   . GLY A 1 211 ? 5.331   -49.423 15.877  1.00 17.31 ? 211  GLY A O   1 
ATOM   1558 N  N   . ILE A 1 212 ? 5.003   -48.237 17.763  1.00 15.66 ? 212  ILE A N   1 
ATOM   1559 C  CA  . ILE A 1 212 ? 5.115   -46.943 17.094  1.00 15.10 ? 212  ILE A CA  1 
ATOM   1560 C  C   . ILE A 1 212 ? 6.039   -46.032 17.886  1.00 16.50 ? 212  ILE A C   1 
ATOM   1561 O  O   . ILE A 1 212 ? 5.965   -45.963 19.118  1.00 15.14 ? 212  ILE A O   1 
ATOM   1562 C  CB  . ILE A 1 212 ? 3.738   -46.271 16.917  1.00 17.01 ? 212  ILE A CB  1 
ATOM   1563 C  CG1 . ILE A 1 212 ? 2.844   -47.125 16.027  1.00 13.77 ? 212  ILE A CG1 1 
ATOM   1564 C  CG2 . ILE A 1 212 ? 3.888   -44.835 16.343  1.00 14.56 ? 212  ILE A CG2 1 
ATOM   1565 C  CD1 . ILE A 1 212 ? 1.412   -46.722 16.092  1.00 14.45 ? 212  ILE A CD1 1 
ATOM   1566 N  N   . ILE A 1 213 ? 6.903   -45.322 17.173  1.00 11.59 ? 213  ILE A N   1 
ATOM   1567 C  CA  . ILE A 1 213 ? 7.655   -44.214 17.748  1.00 16.89 ? 213  ILE A CA  1 
ATOM   1568 C  C   . ILE A 1 213 ? 7.141   -42.930 17.113  1.00 13.77 ? 213  ILE A C   1 
ATOM   1569 O  O   . ILE A 1 213 ? 7.113   -42.801 15.883  1.00 11.72 ? 213  ILE A O   1 
ATOM   1570 C  CB  . ILE A 1 213 ? 9.168   -44.387 17.550  1.00 15.26 ? 213  ILE A CB  1 
ATOM   1571 C  CG1 . ILE A 1 213 ? 9.660   -45.517 18.446  1.00 14.81 ? 213  ILE A CG1 1 
ATOM   1572 C  CG2 . ILE A 1 213 ? 9.903   -43.077 17.872  1.00 16.93 ? 213  ILE A CG2 1 
ATOM   1573 C  CD1 . ILE A 1 213 ? 11.078  -45.958 18.166  1.00 14.68 ? 213  ILE A CD1 1 
ATOM   1574 N  N   . LEU A 1 214 ? 6.713   -41.991 17.948  1.00 15.75 ? 214  LEU A N   1 
ATOM   1575 C  CA  . LEU A 1 214 ? 6.286   -40.671 17.492  1.00 12.56 ? 214  LEU A CA  1 
ATOM   1576 C  C   . LEU A 1 214 ? 7.286   -39.650 18.009  1.00 12.64 ? 214  LEU A C   1 
ATOM   1577 O  O   . LEU A 1 214 ? 7.445   -39.491 19.223  1.00 14.94 ? 214  LEU A O   1 
ATOM   1578 C  CB  . LEU A 1 214 ? 4.862   -40.347 17.968  1.00 14.80 ? 214  LEU A CB  1 
ATOM   1579 C  CG  . LEU A 1 214 ? 4.199   -39.030 17.521  1.00 15.61 ? 214  LEU A CG  1 
ATOM   1580 C  CD1 . LEU A 1 214 ? 2.675   -39.156 17.534  1.00 14.14 ? 214  LEU A CD1 1 
ATOM   1581 C  CD2 . LEU A 1 214 ? 4.629   -37.831 18.378  1.00 16.30 ? 214  LEU A CD2 1 
ATOM   1582 N  N   . ILE A 1 215 ? 7.953   -38.955 17.096  1.00 11.93 ? 215  ILE A N   1 
ATOM   1583 C  CA  . ILE A 1 215 ? 8.973   -37.977 17.457  1.00 12.24 ? 215  ILE A CA  1 
ATOM   1584 C  C   . ILE A 1 215 ? 8.418   -36.601 17.142  1.00 11.71 ? 215  ILE A C   1 
ATOM   1585 O  O   . ILE A 1 215 ? 8.123   -36.302 15.979  1.00 10.46 ? 215  ILE A O   1 
ATOM   1586 C  CB  . ILE A 1 215 ? 10.293  -38.218 16.707  1.00 15.10 ? 215  ILE A CB  1 
ATOM   1587 C  CG1 . ILE A 1 215 ? 10.839  -39.622 16.986  1.00 14.62 ? 215  ILE A CG1 1 
ATOM   1588 C  CG2 . ILE A 1 215 ? 11.342  -37.158 17.092  1.00 14.17 ? 215  ILE A CG2 1 
ATOM   1589 C  CD1 . ILE A 1 215 ? 12.086  -39.923 16.192  1.00 17.11 ? 215  ILE A CD1 1 
ATOM   1590 N  N   . GLY A 1 216 ? 8.273   -35.769 18.174  1.00 12.92 ? 216  GLY A N   1 
ATOM   1591 C  CA  . GLY A 1 216 ? 7.793   -34.413 17.983  1.00 13.99 ? 216  GLY A CA  1 
ATOM   1592 C  C   . GLY A 1 216 ? 8.711   -33.349 18.561  1.00 16.79 ? 216  GLY A C   1 
ATOM   1593 O  O   . GLY A 1 216 ? 9.853   -33.631 18.957  1.00 12.37 ? 216  GLY A O   1 
ATOM   1594 N  N   . GLU A 1 217 ? 8.224   -32.115 18.617  1.00 13.55 ? 217  GLU A N   1 
ATOM   1595 C  CA  . GLU A 1 217 ? 9.029   -30.998 19.103  1.00 15.69 ? 217  GLU A CA  1 
ATOM   1596 C  C   . GLU A 1 217 ? 8.091   -29.840 19.420  1.00 17.85 ? 217  GLU A C   1 
ATOM   1597 O  O   . GLU A 1 217 ? 6.870   -29.942 19.249  1.00 14.91 ? 217  GLU A O   1 
ATOM   1598 C  CB  . GLU A 1 217 ? 10.100  -30.595 18.081  1.00 13.03 ? 217  GLU A CB  1 
ATOM   1599 C  CG  . GLU A 1 217 ? 9.555   -30.155 16.709  1.00 16.90 ? 217  GLU A CG  1 
ATOM   1600 C  CD  . GLU A 1 217 ? 10.633  -30.087 15.618  1.00 19.40 ? 217  GLU A CD  1 
ATOM   1601 O  OE1 . GLU A 1 217 ? 11.417  -31.048 15.456  1.00 21.81 ? 217  GLU A OE1 1 
ATOM   1602 O  OE2 . GLU A 1 217 ? 10.696  -29.063 14.913  1.00 23.81 ? 217  GLU A OE2 1 
ATOM   1603 N  N   . ILE A 1 218 ? 8.674   -28.727 19.879  1.00 16.19 ? 218  ILE A N   1 
ATOM   1604 C  CA  . ILE A 1 218 ? 7.850   -27.570 20.247  1.00 17.26 ? 218  ILE A CA  1 
ATOM   1605 C  C   . ILE A 1 218 ? 7.149   -27.000 19.013  1.00 17.73 ? 218  ILE A C   1 
ATOM   1606 O  O   . ILE A 1 218 ? 7.578   -27.187 17.869  1.00 17.81 ? 218  ILE A O   1 
ATOM   1607 C  CB  . ILE A 1 218 ? 8.695   -26.484 20.927  1.00 18.58 ? 218  ILE A CB  1 
ATOM   1608 C  CG1 . ILE A 1 218 ? 9.776   -25.988 19.947  1.00 17.95 ? 218  ILE A CG1 1 
ATOM   1609 C  CG2 . ILE A 1 218 ? 9.230   -26.961 22.276  1.00 16.57 ? 218  ILE A CG2 1 
ATOM   1610 C  CD1 . ILE A 1 218 ? 10.551  -24.809 20.440  1.00 19.39 ? 218  ILE A CD1 1 
ATOM   1611 N  N   . GLY A 1 219 ? 6.061   -26.262 19.263  1.00 21.33 ? 219  GLY A N   1 
ATOM   1612 C  CA  . GLY A 1 219 ? 5.353   -25.563 18.203  1.00 22.46 ? 219  GLY A CA  1 
ATOM   1613 C  C   . GLY A 1 219 ? 4.094   -26.243 17.698  1.00 22.59 ? 219  GLY A C   1 
ATOM   1614 O  O   . GLY A 1 219 ? 4.057   -27.463 17.513  1.00 19.75 ? 219  GLY A O   1 
ATOM   1615 N  N   . GLY A 1 220 ? 3.045   -25.457 17.462  1.00 20.12 ? 220  GLY A N   1 
ATOM   1616 C  CA  . GLY A 1 220 ? 1.821   -26.037 16.947  1.00 19.07 ? 220  GLY A CA  1 
ATOM   1617 C  C   . GLY A 1 220 ? 1.145   -26.946 17.963  1.00 20.10 ? 220  GLY A C   1 
ATOM   1618 O  O   . GLY A 1 220 ? 1.468   -26.961 19.158  1.00 22.20 ? 220  GLY A O   1 
ATOM   1619 N  N   . ASN A 1 221 ? 0.194   -27.741 17.465  1.00 20.35 ? 221  ASN A N   1 
ATOM   1620 C  CA  . ASN A 1 221 ? -0.524  -28.626 18.375  1.00 22.46 ? 221  ASN A CA  1 
ATOM   1621 C  C   . ASN A 1 221 ? -0.751  -29.995 17.763  1.00 18.38 ? 221  ASN A C   1 
ATOM   1622 O  O   . ASN A 1 221 ? -1.703  -30.691 18.131  1.00 19.93 ? 221  ASN A O   1 
ATOM   1623 C  CB  . ASN A 1 221 ? -1.853  -28.004 18.823  1.00 25.67 ? 221  ASN A CB  1 
ATOM   1624 C  CG  . ASN A 1 221 ? -2.840  -27.833 17.688  1.00 27.70 ? 221  ASN A CG  1 
ATOM   1625 O  OD1 . ASN A 1 221 ? -2.559  -28.174 16.538  1.00 31.53 ? 221  ASN A OD1 1 
ATOM   1626 N  ND2 . ASN A 1 221 ? -4.024  -27.322 18.012  1.00 37.62 ? 221  ASN A ND2 1 
ATOM   1627 N  N   . ALA A 1 222 ? 0.125   -30.415 16.846  1.00 15.82 ? 222  ALA A N   1 
ATOM   1628 C  CA  . ALA A 1 222 ? -0.101  -31.695 16.192  1.00 17.66 ? 222  ALA A CA  1 
ATOM   1629 C  C   . ALA A 1 222 ? 0.153   -32.867 17.141  1.00 16.85 ? 222  ALA A C   1 
ATOM   1630 O  O   . ALA A 1 222 ? -0.474  -33.926 16.992  1.00 16.88 ? 222  ALA A O   1 
ATOM   1631 C  CB  . ALA A 1 222 ? 0.763   -31.806 14.935  1.00 17.89 ? 222  ALA A CB  1 
ATOM   1632 N  N   . GLU A 1 223 ? 1.074   -32.711 18.105  1.00 15.06 ? 223  GLU A N   1 
ATOM   1633 C  CA  . GLU A 1 223 ? 1.299   -33.795 19.064  1.00 18.32 ? 223  GLU A CA  1 
ATOM   1634 C  C   . GLU A 1 223 ? 0.098   -33.943 19.993  1.00 17.80 ? 223  GLU A C   1 
ATOM   1635 O  O   . GLU A 1 223 ? -0.328  -35.068 20.291  1.00 17.41 ? 223  GLU A O   1 
ATOM   1636 C  CB  . GLU A 1 223 ? 2.587   -33.553 19.856  1.00 15.29 ? 223  GLU A CB  1 
ATOM   1637 C  CG  . GLU A 1 223 ? 3.858   -33.661 18.996  1.00 13.17 ? 223  GLU A CG  1 
ATOM   1638 C  CD  . GLU A 1 223 ? 4.185   -32.385 18.229  1.00 22.61 ? 223  GLU A CD  1 
ATOM   1639 O  OE1 . GLU A 1 223 ? 3.355   -31.437 18.215  1.00 19.86 ? 223  GLU A OE1 1 
ATOM   1640 O  OE2 . GLU A 1 223 ? 5.283   -32.332 17.626  1.00 18.93 ? 223  GLU A OE2 1 
ATOM   1641 N  N   . GLU A 1 224 ? -0.471  -32.812 20.431  1.00 17.14 ? 224  GLU A N   1 
ATOM   1642 C  CA  . GLU A 1 224 ? -1.682  -32.839 21.252  1.00 21.24 ? 224  GLU A CA  1 
ATOM   1643 C  C   . GLU A 1 224 ? -2.830  -33.524 20.520  1.00 21.06 ? 224  GLU A C   1 
ATOM   1644 O  O   . GLU A 1 224 ? -3.523  -34.376 21.092  1.00 17.65 ? 224  GLU A O   1 
ATOM   1645 C  CB  . GLU A 1 224 ? -2.076  -31.413 21.660  1.00 19.48 ? 224  GLU A CB  1 
ATOM   1646 C  CG  . GLU A 1 224 ? -1.189  -30.784 22.731  1.00 17.44 ? 224  GLU A CG  1 
ATOM   1647 C  CD  . GLU A 1 224 ? 0.007   -29.997 22.166  1.00 18.92 ? 224  GLU A CD  1 
ATOM   1648 O  OE1 . GLU A 1 224 ? 0.453   -30.263 21.038  1.00 17.88 ? 224  GLU A OE1 1 
ATOM   1649 O  OE2 . GLU A 1 224 ? 0.512   -29.112 22.877  1.00 24.28 ? 224  GLU A OE2 1 
ATOM   1650 N  N   . ASN A 1 225 ? -3.044  -33.163 19.248  1.00 19.41 ? 225  ASN A N   1 
ATOM   1651 C  CA  . ASN A 1 225 ? -4.099  -33.787 18.457  1.00 18.76 ? 225  ASN A CA  1 
ATOM   1652 C  C   . ASN A 1 225 ? -3.862  -35.280 18.304  1.00 21.14 ? 225  ASN A C   1 
ATOM   1653 O  O   . ASN A 1 225 ? -4.795  -36.086 18.421  1.00 20.66 ? 225  ASN A O   1 
ATOM   1654 C  CB  . ASN A 1 225 ? -4.189  -33.136 17.075  1.00 21.68 ? 225  ASN A CB  1 
ATOM   1655 C  CG  . ASN A 1 225 ? -4.653  -31.702 17.135  1.00 25.33 ? 225  ASN A CG  1 
ATOM   1656 O  OD1 . ASN A 1 225 ? -5.159  -31.242 18.160  1.00 23.85 ? 225  ASN A OD1 1 
ATOM   1657 N  ND2 . ASN A 1 225 ? -4.481  -30.982 16.029  1.00 24.61 ? 225  ASN A ND2 1 
ATOM   1658 N  N   . ALA A 1 226 ? -2.623  -35.668 17.998  1.00 16.66 ? 226  ALA A N   1 
ATOM   1659 C  CA  . ALA A 1 226 ? -2.344  -37.090 17.842  1.00 17.63 ? 226  ALA A CA  1 
ATOM   1660 C  C   . ALA A 1 226 ? -2.557  -37.835 19.159  1.00 19.12 ? 226  ALA A C   1 
ATOM   1661 O  O   . ALA A 1 226 ? -3.020  -38.981 19.162  1.00 19.75 ? 226  ALA A O   1 
ATOM   1662 C  CB  . ALA A 1 226 ? -0.925  -37.293 17.321  1.00 18.75 ? 226  ALA A CB  1 
ATOM   1663 N  N   . ALA A 1 227 ? -2.219  -37.198 20.283  1.00 14.65 ? 227  ALA A N   1 
ATOM   1664 C  CA  . ALA A 1 227 ? -2.431  -37.832 21.583  1.00 19.27 ? 227  ALA A CA  1 
ATOM   1665 C  C   . ALA A 1 227 ? -3.899  -38.139 21.799  1.00 20.80 ? 227  ALA A C   1 
ATOM   1666 O  O   . ALA A 1 227 ? -4.258  -39.266 22.154  1.00 20.88 ? 227  ALA A O   1 
ATOM   1667 C  CB  . ALA A 1 227 ? -1.924  -36.942 22.716  1.00 17.35 ? 227  ALA A CB  1 
ATOM   1668 N  N   . GLU A 1 228 ? -4.767  -37.139 21.596  1.00 20.44 ? 228  GLU A N   1 
ATOM   1669 C  CA  . GLU A 1 228 ? -6.204  -37.378 21.726  1.00 25.56 ? 228  GLU A CA  1 
ATOM   1670 C  C   . GLU A 1 228 ? -6.665  -38.474 20.774  1.00 22.41 ? 228  GLU A C   1 
ATOM   1671 O  O   . GLU A 1 228 ? -7.473  -39.333 21.148  1.00 26.00 ? 228  GLU A O   1 
ATOM   1672 C  CB  . GLU A 1 228 ? -6.987  -36.084 21.482  1.00 27.89 ? 228  GLU A CB  1 
ATOM   1673 C  CG  . GLU A 1 228 ? -8.507  -36.252 21.573  1.00 25.02 ? 228  GLU A CG  1 
ATOM   1674 C  CD  . GLU A 1 228 ? -8.970  -36.599 22.983  1.00 26.71 ? 228  GLU A CD  1 
ATOM   1675 O  OE1 . GLU A 1 228 ? -9.970  -37.331 23.125  1.00 28.10 ? 228  GLU A OE1 1 
ATOM   1676 O  OE2 . GLU A 1 228 ? -8.334  -36.130 23.950  1.00 30.35 ? 228  GLU A OE2 1 
ATOM   1677 N  N   . PHE A 1 229 ? -6.138  -38.474 19.545  1.00 23.42 ? 229  PHE A N   1 
ATOM   1678 C  CA  . PHE A 1 229 ? -6.430  -39.539 18.588  1.00 20.56 ? 229  PHE A CA  1 
ATOM   1679 C  C   . PHE A 1 229 ? -6.024  -40.909 19.132  1.00 25.26 ? 229  PHE A C   1 
ATOM   1680 O  O   . PHE A 1 229 ? -6.770  -41.884 18.997  1.00 21.34 ? 229  PHE A O   1 
ATOM   1681 C  CB  . PHE A 1 229 ? -5.709  -39.263 17.266  1.00 19.84 ? 229  PHE A CB  1 
ATOM   1682 C  CG  . PHE A 1 229 ? -5.807  -40.391 16.265  1.00 23.61 ? 229  PHE A CG  1 
ATOM   1683 C  CD1 . PHE A 1 229 ? -6.919  -40.511 15.442  1.00 26.50 ? 229  PHE A CD1 1 
ATOM   1684 C  CD2 . PHE A 1 229 ? -4.775  -41.308 16.124  1.00 21.20 ? 229  PHE A CD2 1 
ATOM   1685 C  CE1 . PHE A 1 229 ? -7.017  -41.546 14.518  1.00 26.86 ? 229  PHE A CE1 1 
ATOM   1686 C  CE2 . PHE A 1 229 ? -4.863  -42.339 15.211  1.00 24.46 ? 229  PHE A CE2 1 
ATOM   1687 C  CZ  . PHE A 1 229 ? -5.992  -42.462 14.402  1.00 27.26 ? 229  PHE A CZ  1 
ATOM   1688 N  N   . LEU A 1 230 ? -4.831  -41.006 19.721  1.00 20.61 ? 230  LEU A N   1 
ATOM   1689 C  CA  . LEU A 1 230 ? -4.388  -42.284 20.265  1.00 23.03 ? 230  LEU A CA  1 
ATOM   1690 C  C   . LEU A 1 230 ? -5.200  -42.666 21.496  1.00 19.80 ? 230  LEU A C   1 
ATOM   1691 O  O   . LEU A 1 230 ? -5.527  -43.841 21.688  1.00 22.18 ? 230  LEU A O   1 
ATOM   1692 C  CB  . LEU A 1 230 ? -2.899  -42.222 20.604  1.00 19.83 ? 230  LEU A CB  1 
ATOM   1693 C  CG  . LEU A 1 230 ? -1.971  -42.123 19.398  1.00 16.19 ? 230  LEU A CG  1 
ATOM   1694 C  CD1 . LEU A 1 230 ? -0.522  -41.974 19.862  1.00 22.03 ? 230  LEU A CD1 1 
ATOM   1695 C  CD2 . LEU A 1 230 ? -2.135  -43.358 18.531  1.00 15.08 ? 230  LEU A CD2 1 
ATOM   1696 N  N   . LYS A 1 231 ? -5.519  -41.686 22.349  1.00 21.10 ? 231  LYS A N   1 
ATOM   1697 C  CA  . LYS A 1 231 ? -6.356  -41.971 23.514  1.00 25.27 ? 231  LYS A CA  1 
ATOM   1698 C  C   . LYS A 1 231 ? -7.674  -42.608 23.099  1.00 27.45 ? 231  LYS A C   1 
ATOM   1699 O  O   . LYS A 1 231 ? -8.105  -43.604 23.695  1.00 29.03 ? 231  LYS A O   1 
ATOM   1700 C  CB  . LYS A 1 231 ? -6.613  -40.696 24.307  1.00 22.48 ? 231  LYS A CB  1 
ATOM   1701 C  CG  . LYS A 1 231 ? -7.537  -40.877 25.491  1.00 27.01 ? 231  LYS A CG  1 
ATOM   1702 C  CD  . LYS A 1 231 ? -7.767  -39.551 26.198  1.00 28.52 ? 231  LYS A CD  1 
ATOM   1703 C  CE  . LYS A 1 231 ? -6.444  -38.930 26.650  1.00 34.08 ? 231  LYS A CE  1 
ATOM   1704 N  N   . GLN A 1 232 ? -8.301  -42.076 22.044  1.00 22.04 ? 232  GLN A N   1 
ATOM   1705 C  CA  . GLN A 1 232 ? -9.607  -42.566 21.619  1.00 29.38 ? 232  GLN A CA  1 
ATOM   1706 C  C   . GLN A 1 232 ? -9.529  -43.875 20.867  1.00 28.19 ? 232  GLN A C   1 
ATOM   1707 O  O   . GLN A 1 232 ? -10.457 -44.677 20.957  1.00 31.77 ? 232  GLN A O   1 
ATOM   1708 C  CB  . GLN A 1 232 ? -10.315 -41.554 20.709  1.00 27.83 ? 232  GLN A CB  1 
ATOM   1709 C  CG  . GLN A 1 232 ? -10.929 -40.388 21.419  1.00 38.29 ? 232  GLN A CG  1 
ATOM   1710 C  CD  . GLN A 1 232 ? -12.038 -39.729 20.614  1.00 41.99 ? 232  GLN A CD  1 
ATOM   1711 O  OE1 . GLN A 1 232 ? -11.990 -39.667 19.382  1.00 47.97 ? 232  GLN A OE1 1 
ATOM   1712 N  NE2 . GLN A 1 232 ? -13.066 -39.265 21.316  1.00 47.17 ? 232  GLN A NE2 1 
ATOM   1713 N  N   . HIS A 1 233 ? -8.474  -44.097 20.083  1.00 28.21 ? 233  HIS A N   1 
ATOM   1714 C  CA  . HIS A 1 233 ? -8.500  -45.175 19.100  1.00 22.61 ? 233  HIS A CA  1 
ATOM   1715 C  C   . HIS A 1 233 ? -7.347  -46.169 19.189  1.00 26.17 ? 233  HIS A C   1 
ATOM   1716 O  O   . HIS A 1 233 ? -7.255  -47.057 18.330  1.00 22.13 ? 233  HIS A O   1 
ATOM   1717 C  CB  . HIS A 1 233 ? -8.549  -44.581 17.690  1.00 30.44 ? 233  HIS A CB  1 
ATOM   1718 C  CG  . HIS A 1 233 ? -9.610  -43.543 17.533  1.00 33.09 ? 233  HIS A CG  1 
ATOM   1719 N  ND1 . HIS A 1 233 ? -9.336  -42.252 17.136  1.00 31.68 ? 233  HIS A ND1 1 
ATOM   1720 C  CD2 . HIS A 1 233 ? -10.948 -43.600 17.747  1.00 31.47 ? 233  HIS A CD2 1 
ATOM   1721 C  CE1 . HIS A 1 233 ? -10.461 -41.558 17.106  1.00 29.88 ? 233  HIS A CE1 1 
ATOM   1722 N  NE2 . HIS A 1 233 ? -11.454 -42.353 17.470  1.00 36.99 ? 233  HIS A NE2 1 
ATOM   1723 N  N   . ASN A 1 234 ? -6.480  -46.058 20.192  1.00 21.74 ? 234  ASN A N   1 
ATOM   1724 C  CA  . ASN A 1 234 ? -5.403  -47.012 20.440  1.00 25.56 ? 234  ASN A CA  1 
ATOM   1725 C  C   . ASN A 1 234 ? -5.355  -47.342 21.920  1.00 23.36 ? 234  ASN A C   1 
ATOM   1726 O  O   . ASN A 1 234 ? -4.300  -47.342 22.561  1.00 24.03 ? 234  ASN A O   1 
ATOM   1727 C  CB  . ASN A 1 234 ? -4.058  -46.460 19.961  1.00 19.63 ? 234  ASN A CB  1 
ATOM   1728 C  CG  . ASN A 1 234 ? -2.989  -47.512 19.897  1.00 19.79 ? 234  ASN A CG  1 
ATOM   1729 O  OD1 . ASN A 1 234 ? -3.196  -48.595 19.350  1.00 21.25 ? 234  ASN A OD1 1 
ATOM   1730 N  ND2 . ASN A 1 234 ? -1.824  -47.207 20.461  1.00 21.39 ? 234  ASN A ND2 1 
ATOM   1731 N  N   . SER A 1 235 ? -6.526  -47.598 22.501  1.00 25.92 ? 235  SER A N   1 
ATOM   1732 C  CA  . SER A 1 235 ? -6.600  -47.849 23.928  1.00 27.69 ? 235  SER A CA  1 
ATOM   1733 C  C   . SER A 1 235 ? -7.356  -49.112 24.310  1.00 27.06 ? 235  SER A C   1 
ATOM   1734 O  O   . SER A 1 235 ? -7.459  -49.404 25.506  1.00 32.14 ? 235  SER A O   1 
ATOM   1735 C  CB  . SER A 1 235 ? -7.227  -46.651 24.640  1.00 22.89 ? 235  SER A CB  1 
ATOM   1736 O  OG  . SER A 1 235 ? -6.348  -45.545 24.584  1.00 30.55 ? 235  SER A OG  1 
ATOM   1737 N  N   . GLY A 1 236 ? -7.867  -49.874 23.352  1.00 29.22 ? 236  GLY A N   1 
ATOM   1738 C  CA  . GLY A 1 236 ? -8.519  -51.124 23.669  1.00 33.95 ? 236  GLY A CA  1 
ATOM   1739 C  C   . GLY A 1 236 ? -7.538  -52.274 23.771  1.00 36.92 ? 236  GLY A C   1 
ATOM   1740 O  O   . GLY A 1 236 ? -6.317  -52.073 23.814  1.00 30.73 ? 236  GLY A O   1 
ATOM   1741 N  N   . PRO A 1 237 ? -8.048  -53.510 23.817  1.00 38.00 ? 237  PRO A N   1 
ATOM   1742 C  CA  . PRO A 1 237 ? -7.170  -54.657 23.589  1.00 37.99 ? 237  PRO A CA  1 
ATOM   1743 C  C   . PRO A 1 237 ? -6.666  -54.596 22.160  1.00 35.90 ? 237  PRO A C   1 
ATOM   1744 O  O   . PRO A 1 237 ? -7.235  -53.917 21.302  1.00 47.47 ? 237  PRO A O   1 
ATOM   1745 C  CB  . PRO A 1 237 ? -8.081  -55.869 23.829  1.00 37.36 ? 237  PRO A CB  1 
ATOM   1746 C  CG  . PRO A 1 237 ? -9.438  -55.375 23.507  1.00 39.58 ? 237  PRO A CG  1 
ATOM   1747 C  CD  . PRO A 1 237 ? -9.463  -53.918 23.923  1.00 39.72 ? 237  PRO A CD  1 
ATOM   1748 N  N   . ASN A 1 238 ? -5.557  -55.277 21.915  1.00 33.23 ? 238  ASN A N   1 
ATOM   1749 C  CA  . ASN A 1 238 ? -4.850  -55.241 20.643  1.00 34.68 ? 238  ASN A CA  1 
ATOM   1750 C  C   . ASN A 1 238 ? -4.239  -53.877 20.333  1.00 29.16 ? 238  ASN A C   1 
ATOM   1751 O  O   . ASN A 1 238 ? -3.673  -53.724 19.253  1.00 28.50 ? 238  ASN A O   1 
ATOM   1752 C  CB  . ASN A 1 238 ? -5.736  -55.645 19.454  1.00 33.04 ? 238  ASN A CB  1 
ATOM   1753 C  CG  . ASN A 1 238 ? -6.684  -56.774 19.792  1.00 40.17 ? 238  ASN A CG  1 
ATOM   1754 O  OD1 . ASN A 1 238 ? -7.900  -56.573 19.884  1.00 38.89 ? 238  ASN A OD1 1 
ATOM   1755 N  ND2 . ASN A 1 238 ? -6.135  -57.971 19.979  1.00 36.99 ? 238  ASN A ND2 1 
ATOM   1756 N  N   . SER A 1 239 ? -4.334  -52.885 21.224  1.00 25.76 ? 239  SER A N   1 
ATOM   1757 C  CA  . SER A 1 239 ? -3.648  -51.619 20.983  1.00 23.62 ? 239  SER A CA  1 
ATOM   1758 C  C   . SER A 1 239 ? -2.146  -51.854 20.824  1.00 23.43 ? 239  SER A C   1 
ATOM   1759 O  O   . SER A 1 239 ? -1.593  -52.846 21.302  1.00 19.73 ? 239  SER A O   1 
ATOM   1760 C  CB  . SER A 1 239 ? -3.899  -50.634 22.121  1.00 27.35 ? 239  SER A CB  1 
ATOM   1761 O  OG  . SER A 1 239 ? -3.194  -50.989 23.304  1.00 24.44 ? 239  SER A OG  1 
ATOM   1762 N  N   . LYS A 1 240 ? -1.479  -50.919 20.133  1.00 18.89 ? 240  LYS A N   1 
ATOM   1763 C  CA  . LYS A 1 240 ? -0.056  -51.074 19.859  1.00 19.21 ? 240  LYS A CA  1 
ATOM   1764 C  C   . LYS A 1 240 ? 0.743   -50.129 20.744  1.00 19.03 ? 240  LYS A C   1 
ATOM   1765 O  O   . LYS A 1 240 ? 0.318   -48.989 20.962  1.00 20.29 ? 240  LYS A O   1 
ATOM   1766 C  CB  . LYS A 1 240 ? 0.265   -50.794 18.378  1.00 19.65 ? 240  LYS A CB  1 
ATOM   1767 C  CG  . LYS A 1 240 ? -0.666  -51.523 17.393  1.00 17.22 ? 240  LYS A CG  1 
ATOM   1768 C  CD  . LYS A 1 240 ? -0.249  -51.337 15.919  1.00 21.27 ? 240  LYS A CD  1 
ATOM   1769 C  CE  . LYS A 1 240 ? -0.948  -52.365 15.003  1.00 23.32 ? 240  LYS A CE  1 
ATOM   1770 N  NZ  . LYS A 1 240 ? -0.599  -52.207 13.537  1.00 19.14 ? 240  LYS A NZ  1 
ATOM   1771 N  N   . PRO A 1 241 ? 1.880   -50.562 21.290  1.00 19.72 ? 241  PRO A N   1 
ATOM   1772 C  CA  . PRO A 1 241 ? 2.660   -49.655 22.135  1.00 20.22 ? 241  PRO A CA  1 
ATOM   1773 C  C   . PRO A 1 241 ? 3.149   -48.471 21.320  1.00 16.65 ? 241  PRO A C   1 
ATOM   1774 O  O   . PRO A 1 241 ? 3.567   -48.619 20.167  1.00 18.57 ? 241  PRO A O   1 
ATOM   1775 C  CB  . PRO A 1 241 ? 3.817   -50.530 22.636  1.00 19.72 ? 241  PRO A CB  1 
ATOM   1776 C  CG  . PRO A 1 241 ? 3.835   -51.713 21.727  1.00 25.98 ? 241  PRO A CG  1 
ATOM   1777 C  CD  . PRO A 1 241 ? 2.458   -51.919 21.250  1.00 20.03 ? 241  PRO A CD  1 
ATOM   1778 N  N   . VAL A 1 242 ? 3.023   -47.284 21.902  1.00 13.67 ? 242  VAL A N   1 
ATOM   1779 C  CA  . VAL A 1 242 ? 3.521   -46.053 21.301  1.00 16.30 ? 242  VAL A CA  1 
ATOM   1780 C  C   . VAL A 1 242 ? 4.506   -45.423 22.275  1.00 15.47 ? 242  VAL A C   1 
ATOM   1781 O  O   . VAL A 1 242 ? 4.197   -45.264 23.461  1.00 18.19 ? 242  VAL A O   1 
ATOM   1782 C  CB  . VAL A 1 242 ? 2.388   -45.072 20.961  1.00 17.16 ? 242  VAL A CB  1 
ATOM   1783 C  CG1 . VAL A 1 242 ? 2.959   -43.823 20.297  1.00 17.34 ? 242  VAL A CG1 1 
ATOM   1784 C  CG2 . VAL A 1 242 ? 1.346   -45.741 20.060  1.00 17.52 ? 242  VAL A CG2 1 
ATOM   1785 N  N   . VAL A 1 243 ? 5.697   -45.101 21.778  1.00 17.53 ? 243  VAL A N   1 
ATOM   1786 C  CA  . VAL A 1 243 ? 6.736   -44.415 22.536  1.00 14.07 ? 243  VAL A CA  1 
ATOM   1787 C  C   . VAL A 1 243 ? 6.996   -43.087 21.842  1.00 14.99 ? 243  VAL A C   1 
ATOM   1788 O  O   . VAL A 1 243 ? 6.960   -43.005 20.608  1.00 15.09 ? 243  VAL A O   1 
ATOM   1789 C  CB  . VAL A 1 243 ? 8.016   -45.272 22.634  1.00 15.37 ? 243  VAL A CB  1 
ATOM   1790 C  CG1 . VAL A 1 243 ? 9.227   -44.456 23.190  1.00 15.60 ? 243  VAL A CG1 1 
ATOM   1791 C  CG2 . VAL A 1 243 ? 7.754   -46.453 23.528  1.00 13.78 ? 243  VAL A CG2 1 
ATOM   1792 N  N   . SER A 1 244 ? 7.219   -42.039 22.624  1.00 15.40 ? 244  SER A N   1 
ATOM   1793 C  CA  . SER A 1 244 ? 7.428   -40.720 22.046  1.00 15.62 ? 244  SER A CA  1 
ATOM   1794 C  C   . SER A 1 244 ? 8.618   -40.031 22.686  1.00 15.46 ? 244  SER A C   1 
ATOM   1795 O  O   . SER A 1 244 ? 8.999   -40.342 23.814  1.00 14.41 ? 244  SER A O   1 
ATOM   1796 C  CB  . SER A 1 244 ? 6.170   -39.846 22.200  1.00 15.02 ? 244  SER A CB  1 
ATOM   1797 O  OG  . SER A 1 244 ? 6.355   -38.599 21.566  1.00 19.35 ? 244  SER A OG  1 
ATOM   1798 N  N   . PHE A 1 245 ? 9.226   -39.109 21.926  1.00 12.96 ? 245  PHE A N   1 
ATOM   1799 C  CA  . PHE A 1 245 ? 10.165  -38.135 22.455  1.00 15.88 ? 245  PHE A CA  1 
ATOM   1800 C  C   . PHE A 1 245 ? 9.795   -36.785 21.864  1.00 16.99 ? 245  PHE A C   1 
ATOM   1801 O  O   . PHE A 1 245 ? 9.490   -36.690 20.669  1.00 14.48 ? 245  PHE A O   1 
ATOM   1802 C  CB  . PHE A 1 245 ? 11.638  -38.463 22.119  1.00 11.84 ? 245  PHE A CB  1 
ATOM   1803 C  CG  . PHE A 1 245 ? 12.582  -37.332 22.424  1.00 16.06 ? 245  PHE A CG  1 
ATOM   1804 C  CD1 . PHE A 1 245 ? 13.065  -37.150 23.707  1.00 16.35 ? 245  PHE A CD1 1 
ATOM   1805 C  CD2 . PHE A 1 245 ? 12.965  -36.435 21.434  1.00 14.69 ? 245  PHE A CD2 1 
ATOM   1806 C  CE1 . PHE A 1 245 ? 13.917  -36.102 23.999  1.00 15.85 ? 245  PHE A CE1 1 
ATOM   1807 C  CE2 . PHE A 1 245 ? 13.804  -35.384 21.719  1.00 16.20 ? 245  PHE A CE2 1 
ATOM   1808 C  CZ  . PHE A 1 245 ? 14.288  -35.215 23.004  1.00 18.07 ? 245  PHE A CZ  1 
ATOM   1809 N  N   . ILE A 1 246 ? 9.795   -35.753 22.706  1.00 17.37 ? 246  ILE A N   1 
ATOM   1810 C  CA  . ILE A 1 246 ? 9.431   -34.397 22.294  1.00 14.33 ? 246  ILE A CA  1 
ATOM   1811 C  C   . ILE A 1 246 ? 10.638  -33.505 22.507  1.00 14.82 ? 246  ILE A C   1 
ATOM   1812 O  O   . ILE A 1 246 ? 11.003  -33.211 23.653  1.00 13.80 ? 246  ILE A O   1 
ATOM   1813 C  CB  . ILE A 1 246 ? 8.225   -33.848 23.059  1.00 13.46 ? 246  ILE A CB  1 
ATOM   1814 C  CG1 . ILE A 1 246 ? 6.981   -34.737 22.879  1.00 14.32 ? 246  ILE A CG1 1 
ATOM   1815 C  CG2 . ILE A 1 246 ? 7.951   -32.391 22.600  1.00 12.49 ? 246  ILE A CG2 1 
ATOM   1816 C  CD1 . ILE A 1 246 ? 6.401   -34.763 21.449  1.00 14.70 ? 246  ILE A CD1 1 
ATOM   1817 N  N   . ALA A 1 247 ? 11.229  -33.041 21.407  1.00 14.62 ? 247  ALA A N   1 
ATOM   1818 C  CA  . ALA A 1 247 ? 12.392  -32.170 21.469  1.00 15.17 ? 247  ALA A CA  1 
ATOM   1819 C  C   . ALA A 1 247 ? 12.011  -30.754 21.898  1.00 16.61 ? 247  ALA A C   1 
ATOM   1820 O  O   . ALA A 1 247 ? 10.944  -30.249 21.550  1.00 15.82 ? 247  ALA A O   1 
ATOM   1821 C  CB  . ALA A 1 247 ? 13.087  -32.140 20.104  1.00 13.53 ? 247  ALA A CB  1 
ATOM   1822 N  N   . GLY A 1 248 ? 12.891  -30.111 22.663  1.00 17.18 ? 248  GLY A N   1 
ATOM   1823 C  CA  . GLY A 1 248 ? 12.752  -28.704 22.980  1.00 13.53 ? 248  GLY A CA  1 
ATOM   1824 C  C   . GLY A 1 248 ? 12.368  -28.389 24.406  1.00 18.28 ? 248  GLY A C   1 
ATOM   1825 O  O   . GLY A 1 248 ? 11.928  -27.266 24.669  1.00 15.92 ? 248  GLY A O   1 
ATOM   1826 N  N   . LEU A 1 249 ? 12.511  -29.346 25.323  1.00 17.11 ? 249  LEU A N   1 
ATOM   1827 C  CA  . LEU A 1 249 ? 12.270  -29.104 26.742  1.00 21.49 ? 249  LEU A CA  1 
ATOM   1828 C  C   . LEU A 1 249 ? 13.044  -27.902 27.258  1.00 19.30 ? 249  LEU A C   1 
ATOM   1829 O  O   . LEU A 1 249 ? 12.546  -27.181 28.125  1.00 20.96 ? 249  LEU A O   1 
ATOM   1830 C  CB  . LEU A 1 249 ? 12.638  -30.357 27.553  1.00 19.53 ? 249  LEU A CB  1 
ATOM   1831 C  CG  . LEU A 1 249 ? 12.255  -30.420 29.037  1.00 27.32 ? 249  LEU A CG  1 
ATOM   1832 C  CD1 . LEU A 1 249 ? 10.756  -30.607 29.217  1.00 20.82 ? 249  LEU A CD1 1 
ATOM   1833 C  CD2 . LEU A 1 249 ? 13.014  -31.540 29.741  1.00 23.67 ? 249  LEU A CD2 1 
ATOM   1834 N  N   . THR A 1 250 ? 14.251  -27.657 26.740  1.00 18.35 ? 250  THR A N   1 
ATOM   1835 C  CA  . THR A 1 250 ? 15.078  -26.538 27.189  1.00 17.33 ? 250  THR A CA  1 
ATOM   1836 C  C   . THR A 1 250 ? 15.051  -25.351 26.238  1.00 22.10 ? 250  THR A C   1 
ATOM   1837 O  O   . THR A 1 250 ? 15.898  -24.460 26.356  1.00 21.40 ? 250  THR A O   1 
ATOM   1838 C  CB  . THR A 1 250 ? 16.536  -26.976 27.368  1.00 23.36 ? 250  THR A CB  1 
ATOM   1839 O  OG1 . THR A 1 250 ? 17.079  -27.372 26.100  1.00 20.14 ? 250  THR A OG1 1 
ATOM   1840 C  CG2 . THR A 1 250 ? 16.637  -28.131 28.336  1.00 25.46 ? 250  THR A CG2 1 
ATOM   1841 N  N   . ALA A 1 251 ? 14.133  -25.328 25.278  1.00 18.16 ? 251  ALA A N   1 
ATOM   1842 C  CA  . ALA A 1 251 ? 14.157  -24.259 24.299  1.00 20.23 ? 251  ALA A CA  1 
ATOM   1843 C  C   . ALA A 1 251 ? 13.660  -22.963 24.940  1.00 25.56 ? 251  ALA A C   1 
ATOM   1844 O  O   . ALA A 1 251 ? 12.729  -22.994 25.746  1.00 23.89 ? 251  ALA A O   1 
ATOM   1845 C  CB  . ALA A 1 251 ? 13.292  -24.616 23.100  1.00 20.03 ? 251  ALA A CB  1 
ATOM   1846 N  N   . PRO A 1 252 ? 14.271  -21.820 24.618  1.00 20.38 ? 252  PRO A N   1 
ATOM   1847 C  CA  . PRO A 1 252 ? 13.749  -20.550 25.123  1.00 28.48 ? 252  PRO A CA  1 
ATOM   1848 C  C   . PRO A 1 252 ? 12.435  -20.204 24.450  1.00 26.85 ? 252  PRO A C   1 
ATOM   1849 O  O   . PRO A 1 252 ? 12.171  -20.625 23.311  1.00 27.33 ? 252  PRO A O   1 
ATOM   1850 C  CB  . PRO A 1 252 ? 14.852  -19.542 24.745  1.00 23.73 ? 252  PRO A CB  1 
ATOM   1851 C  CG  . PRO A 1 252 ? 15.452  -20.133 23.508  1.00 26.39 ? 252  PRO A CG  1 
ATOM   1852 C  CD  . PRO A 1 252 ? 15.453  -21.625 23.761  1.00 21.03 ? 252  PRO A CD  1 
ATOM   1853 N  N   . PRO A 1 253 ? 11.568  -19.447 25.123  1.00 27.71 ? 253  PRO A N   1 
ATOM   1854 C  CA  . PRO A 1 253 ? 10.290  -19.082 24.505  1.00 26.21 ? 253  PRO A CA  1 
ATOM   1855 C  C   . PRO A 1 253 ? 10.474  -18.044 23.413  1.00 28.04 ? 253  PRO A C   1 
ATOM   1856 O  O   . PRO A 1 253 ? 11.363  -17.191 23.471  1.00 32.43 ? 253  PRO A O   1 
ATOM   1857 C  CB  . PRO A 1 253 ? 9.477   -18.519 25.679  1.00 33.32 ? 253  PRO A CB  1 
ATOM   1858 C  CG  . PRO A 1 253 ? 10.520  -18.001 26.638  1.00 29.60 ? 253  PRO A CG  1 
ATOM   1859 C  CD  . PRO A 1 253 ? 11.640  -19.022 26.534  1.00 29.51 ? 253  PRO A CD  1 
ATOM   1860 N  N   . GLY A 1 254 ? 9.625   -18.138 22.394  1.00 26.07 ? 254  GLY A N   1 
ATOM   1861 C  CA  . GLY A 1 254 ? 9.556   -17.101 21.383  1.00 31.48 ? 254  GLY A CA  1 
ATOM   1862 C  C   . GLY A 1 254 ? 10.726  -17.067 20.431  1.00 31.60 ? 254  GLY A C   1 
ATOM   1863 O  O   . GLY A 1 254 ? 11.051  -16.000 19.898  1.00 26.06 ? 254  GLY A O   1 
ATOM   1864 N  N   . ARG A 1 255 ? 11.380  -18.207 20.220  1.00 30.38 ? 255  ARG A N   1 
ATOM   1865 C  CA  . ARG A 1 255 ? 12.488  -18.337 19.286  1.00 24.10 ? 255  ARG A CA  1 
ATOM   1866 C  C   . ARG A 1 255 ? 12.205  -19.510 18.364  1.00 26.06 ? 255  ARG A C   1 
ATOM   1867 O  O   . ARG A 1 255 ? 11.710  -20.550 18.809  1.00 22.32 ? 255  ARG A O   1 
ATOM   1868 C  CB  . ARG A 1 255 ? 13.825  -18.568 20.008  1.00 25.25 ? 255  ARG A CB  1 
ATOM   1869 C  CG  . ARG A 1 255 ? 14.249  -17.470 20.983  1.00 28.56 ? 255  ARG A CG  1 
ATOM   1870 C  CD  . ARG A 1 255 ? 14.294  -16.088 20.323  1.00 30.28 ? 255  ARG A CD  1 
ATOM   1871 N  NE  . ARG A 1 255 ? 15.275  -15.998 19.234  1.00 26.00 ? 255  ARG A NE  1 
ATOM   1872 C  CZ  . ARG A 1 255 ? 16.585  -15.856 19.416  1.00 26.41 ? 255  ARG A CZ  1 
ATOM   1873 N  NH1 . ARG A 1 255 ? 17.098  -15.806 20.651  1.00 26.22 ? 255  ARG A NH1 1 
ATOM   1874 N  NH2 . ARG A 1 255 ? 17.384  -15.771 18.362  1.00 27.04 ? 255  ARG A NH2 1 
ATOM   1875 N  N   . ARG A 1 256 ? 12.502  -19.336 17.080  1.00 23.68 ? 256  ARG A N   1 
ATOM   1876 C  CA  . ARG A 1 256 ? 12.399  -20.427 16.123  1.00 25.54 ? 256  ARG A CA  1 
ATOM   1877 C  C   . ARG A 1 256 ? 13.660  -21.274 16.249  1.00 26.53 ? 256  ARG A C   1 
ATOM   1878 O  O   . ARG A 1 256 ? 14.769  -20.797 15.985  1.00 22.25 ? 256  ARG A O   1 
ATOM   1879 C  CB  . ARG A 1 256 ? 12.207  -19.878 14.711  1.00 28.32 ? 256  ARG A CB  1 
ATOM   1880 C  CG  . ARG A 1 256 ? 10.816  -19.259 14.495  1.00 34.16 ? 256  ARG A CG  1 
ATOM   1881 C  CD  . ARG A 1 256 ? 10.782  -18.254 13.342  1.00 36.86 ? 256  ARG A CD  1 
ATOM   1882 N  NE  . ARG A 1 256 ? 11.748  -17.187 13.557  1.00 36.12 ? 256  ARG A NE  1 
ATOM   1883 C  CZ  . ARG A 1 256 ? 11.960  -16.186 12.716  1.00 37.83 ? 256  ARG A CZ  1 
ATOM   1884 N  NH1 . ARG A 1 256 ? 11.262  -16.105 11.594  1.00 36.94 ? 256  ARG A NH1 1 
ATOM   1885 N  NH2 . ARG A 1 256 ? 12.871  -15.266 13.003  1.00 41.78 ? 256  ARG A NH2 1 
ATOM   1886 N  N   . MET A 1 257 ? 13.497  -22.516 16.696  1.00 19.82 ? 257  MET A N   1 
ATOM   1887 C  CA  . MET A 1 257 ? 14.636  -23.387 16.984  1.00 20.95 ? 257  MET A CA  1 
ATOM   1888 C  C   . MET A 1 257 ? 15.014  -24.164 15.725  1.00 20.35 ? 257  MET A C   1 
ATOM   1889 O  O   . MET A 1 257 ? 14.809  -25.373 15.606  1.00 20.45 ? 257  MET A O   1 
ATOM   1890 C  CB  . MET A 1 257 ? 14.319  -24.299 18.160  1.00 16.49 ? 257  MET A CB  1 
ATOM   1891 C  CG  . MET A 1 257 ? 13.817  -23.520 19.378  1.00 20.69 ? 257  MET A CG  1 
ATOM   1892 S  SD  . MET A 1 257 ? 15.061  -22.402 20.106  1.00 22.35 ? 257  MET A SD  1 
ATOM   1893 C  CE  . MET A 1 257 ? 16.235  -23.634 20.717  1.00 18.39 ? 257  MET A CE  1 
ATOM   1894 N  N   . GLY A 1 258 ? 15.579  -23.427 14.771  1.00 19.34 ? 258  GLY A N   1 
ATOM   1895 C  CA  . GLY A 1 258 ? 16.018  -24.001 13.508  1.00 20.54 ? 258  GLY A CA  1 
ATOM   1896 C  C   . GLY A 1 258 ? 14.879  -24.249 12.536  1.00 31.00 ? 258  GLY A C   1 
ATOM   1897 O  O   . GLY A 1 258 ? 14.879  -23.760 11.399  1.00 31.14 ? 258  GLY A O   1 
ATOM   1898 N  N   . HIS A 1 259 ? 13.902  -25.031 12.976  1.00 28.52 ? 259  HIS A N   1 
ATOM   1899 C  CA  . HIS A 1 259 ? 12.719  -25.287 12.176  1.00 28.21 ? 259  HIS A CA  1 
ATOM   1900 C  C   . HIS A 1 259 ? 11.798  -24.086 12.202  1.00 23.98 ? 259  HIS A C   1 
ATOM   1901 O  O   . HIS A 1 259 ? 11.542  -23.509 13.261  1.00 25.80 ? 259  HIS A O   1 
ATOM   1902 C  CB  . HIS A 1 259 ? 11.962  -26.504 12.705  1.00 25.89 ? 259  HIS A CB  1 
ATOM   1903 C  CG  . HIS A 1 259 ? 12.538  -27.805 12.271  1.00 17.52 ? 259  HIS A CG  1 
ATOM   1904 N  ND1 . HIS A 1 259 ? 12.228  -28.992 12.898  1.00 21.41 ? 259  HIS A ND1 1 
ATOM   1905 C  CD2 . HIS A 1 259 ? 13.380  -28.118 11.256  1.00 18.54 ? 259  HIS A CD2 1 
ATOM   1906 C  CE1 . HIS A 1 259 ? 12.859  -29.982 12.291  1.00 17.78 ? 259  HIS A CE1 1 
ATOM   1907 N  NE2 . HIS A 1 259 ? 13.566  -29.479 11.293  1.00 21.22 ? 259  HIS A NE2 1 
ATOM   1908 N  N   . ALA A 1 260 ? 11.288  -23.718 11.023  1.00 31.14 ? 260  ALA A N   1 
ATOM   1909 C  CA  . ALA A 1 260 ? 10.256  -22.687 10.957  1.00 32.05 ? 260  ALA A CA  1 
ATOM   1910 C  C   . ALA A 1 260 ? 9.115   -23.004 11.913  1.00 30.25 ? 260  ALA A C   1 
ATOM   1911 O  O   . ALA A 1 260 ? 8.594   -22.111 12.592  1.00 31.59 ? 260  ALA A O   1 
ATOM   1912 C  CB  . ALA A 1 260 ? 9.744   -22.555 9.517   1.00 30.51 ? 260  ALA A CB  1 
ATOM   1913 N  N   . GLY A 1 261 ? 8.736   -24.285 12.008  1.00 27.67 ? 261  GLY A N   1 
ATOM   1914 C  CA  . GLY A 1 261 ? 7.643   -24.673 12.885  1.00 26.30 ? 261  GLY A CA  1 
ATOM   1915 C  C   . GLY A 1 261 ? 7.977   -24.748 14.368  1.00 30.66 ? 261  GLY A C   1 
ATOM   1916 O  O   . GLY A 1 261 ? 7.056   -24.778 15.192  1.00 26.26 ? 261  GLY A O   1 
ATOM   1917 N  N   . ALA A 1 262 ? 9.264   -24.768 14.734  1.00 26.71 ? 262  ALA A N   1 
ATOM   1918 C  CA  . ALA A 1 262 ? 9.674   -25.062 16.112  1.00 20.26 ? 262  ALA A CA  1 
ATOM   1919 C  C   . ALA A 1 262 ? 9.747   -23.774 16.930  1.00 25.82 ? 262  ALA A C   1 
ATOM   1920 O  O   . ALA A 1 262 ? 10.808  -23.175 17.118  1.00 26.48 ? 262  ALA A O   1 
ATOM   1921 C  CB  . ALA A 1 262 ? 11.006  -25.792 16.114  1.00 17.73 ? 262  ALA A CB  1 
ATOM   1922 N  N   . ILE A 1 263 ? 8.600   -23.346 17.448  1.00 26.48 ? 263  ILE A N   1 
ATOM   1923 C  CA  . ILE A 1 263 ? 8.554   -22.088 18.188  1.00 25.16 ? 263  ILE A CA  1 
ATOM   1924 C  C   . ILE A 1 263 ? 7.456   -22.154 19.235  1.00 26.77 ? 263  ILE A C   1 
ATOM   1925 O  O   . ILE A 1 263 ? 6.338   -22.603 18.964  1.00 31.90 ? 263  ILE A O   1 
ATOM   1926 C  CB  . ILE A 1 263 ? 8.368   -20.865 17.251  1.00 23.51 ? 263  ILE A CB  1 
ATOM   1927 C  CG1 . ILE A 1 263 ? 8.228   -19.580 18.082  1.00 28.16 ? 263  ILE A CG1 1 
ATOM   1928 C  CG2 . ILE A 1 263 ? 7.189   -21.069 16.289  1.00 27.88 ? 263  ILE A CG2 1 
ATOM   1929 C  CD1 . ILE A 1 263 ? 8.938   -18.357 17.480  1.00 25.73 ? 263  ILE A CD1 1 
ATOM   1930 N  N   . ILE A 1 264 ? 7.794   -21.694 20.436  1.00 23.77 ? 264  ILE A N   1 
ATOM   1931 C  CA  . ILE A 1 264 ? 6.850   -21.527 21.531  1.00 28.45 ? 264  ILE A CA  1 
ATOM   1932 C  C   . ILE A 1 264 ? 6.334   -20.092 21.457  1.00 32.22 ? 264  ILE A C   1 
ATOM   1933 O  O   . ILE A 1 264 ? 6.989   -19.165 21.929  1.00 32.74 ? 264  ILE A O   1 
ATOM   1934 C  CB  . ILE A 1 264 ? 7.510   -21.811 22.881  1.00 27.63 ? 264  ILE A CB  1 
ATOM   1935 C  CG1 . ILE A 1 264 ? 8.046   -23.246 22.930  1.00 26.92 ? 264  ILE A CG1 1 
ATOM   1936 C  CG2 . ILE A 1 264 ? 6.535   -21.527 24.026  1.00 31.43 ? 264  ILE A CG2 1 
ATOM   1937 C  CD1 . ILE A 1 264 ? 9.044   -23.476 24.048  1.00 24.69 ? 264  ILE A CD1 1 
ATOM   1938 N  N   . ALA A 1 265 ? 5.156   -19.907 20.870  1.00 30.34 ? 265  ALA A N   1 
ATOM   1939 C  CA  . ALA A 1 265 ? 4.584   -18.584 20.678  1.00 35.47 ? 265  ALA A CA  1 
ATOM   1940 C  C   . ALA A 1 265 ? 3.315   -18.423 21.507  1.00 39.55 ? 265  ALA A C   1 
ATOM   1941 O  O   . ALA A 1 265 ? 2.566   -19.380 21.719  1.00 40.48 ? 265  ALA A O   1 
ATOM   1942 C  CB  . ALA A 1 265 ? 4.284   -18.331 19.198  1.00 35.34 ? 265  ALA A CB  1 
ATOM   1943 N  N   . GLY A 1 266 ? 3.090   -17.199 21.988  1.00 42.34 ? 266  GLY A N   1 
ATOM   1944 C  CA  . GLY A 1 266 ? 1.910   -16.873 22.770  1.00 39.59 ? 266  GLY A CA  1 
ATOM   1945 C  C   . GLY A 1 266 ? 1.667   -17.801 23.942  1.00 37.00 ? 266  GLY A C   1 
ATOM   1946 O  O   . GLY A 1 266 ? 0.516   -18.087 24.286  1.00 37.78 ? 266  GLY A O   1 
ATOM   1947 N  N   . GLY A 1 267 ? 2.743   -18.294 24.554  1.00 39.70 ? 267  GLY A N   1 
ATOM   1948 C  CA  . GLY A 1 267 ? 2.637   -19.265 25.621  1.00 35.46 ? 267  GLY A CA  1 
ATOM   1949 C  C   . GLY A 1 267 ? 2.204   -20.651 25.192  1.00 35.24 ? 267  GLY A C   1 
ATOM   1950 O  O   . GLY A 1 267 ? 2.018   -21.516 26.053  1.00 39.14 ? 267  GLY A O   1 
ATOM   1951 N  N   . LYS A 1 268 ? 2.032   -20.892 23.899  1.00 32.85 ? 268  LYS A N   1 
ATOM   1952 C  CA  . LYS A 1 268 ? 1.591   -22.178 23.388  1.00 36.19 ? 268  LYS A CA  1 
ATOM   1953 C  C   . LYS A 1 268 ? 2.714   -22.831 22.592  1.00 33.73 ? 268  LYS A C   1 
ATOM   1954 O  O   . LYS A 1 268 ? 3.535   -22.152 21.972  1.00 29.58 ? 268  LYS A O   1 
ATOM   1955 C  CB  . LYS A 1 268 ? 0.345   -22.018 22.510  1.00 38.48 ? 268  LYS A CB  1 
ATOM   1956 N  N   . GLY A 1 269 ? 2.751   -24.162 22.623  1.00 29.29 ? 269  GLY A N   1 
ATOM   1957 C  CA  . GLY A 1 269 ? 3.772   -24.916 21.919  1.00 27.67 ? 269  GLY A CA  1 
ATOM   1958 C  C   . GLY A 1 269 ? 4.851   -25.526 22.788  1.00 20.52 ? 269  GLY A C   1 
ATOM   1959 O  O   . GLY A 1 269 ? 5.764   -26.155 22.242  1.00 25.39 ? 269  GLY A O   1 
ATOM   1960 N  N   . GLY A 1 270 ? 4.776   -25.394 24.109  1.00 26.24 ? 270  GLY A N   1 
ATOM   1961 C  CA  . GLY A 1 270 ? 5.824   -25.934 24.966  1.00 21.35 ? 270  GLY A CA  1 
ATOM   1962 C  C   . GLY A 1 270 ? 5.895   -27.451 24.912  1.00 27.53 ? 270  GLY A C   1 
ATOM   1963 O  O   . GLY A 1 270 ? 4.915   -28.136 24.603  1.00 22.77 ? 270  GLY A O   1 
ATOM   1964 N  N   . ALA A 1 271 ? 7.090   -27.985 25.217  1.00 22.51 ? 271  ALA A N   1 
ATOM   1965 C  CA  . ALA A 1 271 ? 7.294   -29.434 25.159  1.00 20.05 ? 271  ALA A CA  1 
ATOM   1966 C  C   . ALA A 1 271 ? 6.635   -30.140 26.340  1.00 18.55 ? 271  ALA A C   1 
ATOM   1967 O  O   . ALA A 1 271 ? 6.100   -31.244 26.188  1.00 22.38 ? 271  ALA A O   1 
ATOM   1968 C  CB  . ALA A 1 271 ? 8.793   -29.758 25.106  1.00 18.01 ? 271  ALA A CB  1 
ATOM   1969 N  N   . LYS A 1 272 ? 6.684   -29.535 27.531  1.00 18.98 ? 272  LYS A N   1 
ATOM   1970 C  CA  . LYS A 1 272 ? 6.040   -30.124 28.706  1.00 24.45 ? 272  LYS A CA  1 
ATOM   1971 C  C   . LYS A 1 272 ? 4.567   -30.429 28.454  1.00 20.96 ? 272  LYS A C   1 
ATOM   1972 O  O   . LYS A 1 272 ? 4.085   -31.520 28.774  1.00 20.82 ? 272  LYS A O   1 
ATOM   1973 C  CB  . LYS A 1 272 ? 6.166   -29.195 29.915  1.00 26.26 ? 272  LYS A CB  1 
ATOM   1974 C  CG  . LYS A 1 272 ? 7.544   -29.139 30.548  1.00 27.64 ? 272  LYS A CG  1 
ATOM   1975 C  CD  . LYS A 1 272 ? 7.619   -27.981 31.533  1.00 28.14 ? 272  LYS A CD  1 
ATOM   1976 C  CE  . LYS A 1 272 ? 9.009   -27.388 31.547  1.00 36.37 ? 272  LYS A CE  1 
ATOM   1977 N  NZ  . LYS A 1 272 ? 9.479   -27.079 30.161  1.00 40.45 ? 272  LYS A NZ  1 
ATOM   1978 N  N   . GLU A 1 273 ? 3.828   -29.464 27.899  1.00 24.60 ? 273  GLU A N   1 
ATOM   1979 C  CA  . GLU A 1 273 ? 2.406   -29.690 27.659  1.00 22.29 ? 273  GLU A CA  1 
ATOM   1980 C  C   . GLU A 1 273 ? 2.181   -30.842 26.680  1.00 23.58 ? 273  GLU A C   1 
ATOM   1981 O  O   . GLU A 1 273 ? 1.211   -31.603 26.820  1.00 19.36 ? 273  GLU A O   1 
ATOM   1982 C  CB  . GLU A 1 273 ? 1.743   -28.400 27.158  1.00 24.41 ? 273  GLU A CB  1 
ATOM   1983 C  CG  . GLU A 1 273 ? 1.823   -27.180 28.123  1.00 25.85 ? 273  GLU A CG  1 
ATOM   1984 C  CD  . GLU A 1 273 ? 3.219   -26.561 28.224  1.00 34.96 ? 273  GLU A CD  1 
ATOM   1985 O  OE1 . GLU A 1 273 ? 4.026   -26.730 27.295  1.00 32.36 ? 273  GLU A OE1 1 
ATOM   1986 O  OE2 . GLU A 1 273 ? 3.530   -25.918 29.252  1.00 47.80 ? 273  GLU A OE2 1 
ATOM   1987 N  N   . LYS A 1 274 ? 3.084   -31.013 25.707  1.00 20.18 ? 274  LYS A N   1 
ATOM   1988 C  CA  . LYS A 1 274 ? 2.956   -32.125 24.770  1.00 15.17 ? 274  LYS A CA  1 
ATOM   1989 C  C   . LYS A 1 274 ? 3.259   -33.464 25.438  1.00 17.52 ? 274  LYS A C   1 
ATOM   1990 O  O   . LYS A 1 274 ? 2.554   -34.451 25.202  1.00 14.63 ? 274  LYS A O   1 
ATOM   1991 C  CB  . LYS A 1 274 ? 3.881   -31.904 23.565  1.00 17.58 ? 274  LYS A CB  1 
ATOM   1992 C  CG  . LYS A 1 274 ? 3.434   -30.788 22.637  1.00 17.13 ? 274  LYS A CG  1 
ATOM   1993 C  CD  . LYS A 1 274 ? 4.510   -30.401 21.629  1.00 16.89 ? 274  LYS A CD  1 
ATOM   1994 C  CE  . LYS A 1 274 ? 4.101   -29.125 20.884  1.00 17.48 ? 274  LYS A CE  1 
ATOM   1995 N  NZ  . LYS A 1 274 ? 2.953   -29.436 19.984  1.00 18.07 ? 274  LYS A NZ  1 
ATOM   1996 N  N   . ILE A 1 275 ? 4.323   -33.521 26.250  1.00 18.15 ? 275  ILE A N   1 
ATOM   1997 C  CA  . ILE A 1 275 ? 4.652   -34.739 26.995  1.00 14.96 ? 275  ILE A CA  1 
ATOM   1998 C  C   . ILE A 1 275 ? 3.478   -35.150 27.886  1.00 17.26 ? 275  ILE A C   1 
ATOM   1999 O  O   . ILE A 1 275 ? 3.082   -36.324 27.924  1.00 15.60 ? 275  ILE A O   1 
ATOM   2000 C  CB  . ILE A 1 275 ? 5.948   -34.507 27.802  1.00 17.46 ? 275  ILE A CB  1 
ATOM   2001 C  CG1 . ILE A 1 275 ? 7.148   -34.356 26.848  1.00 17.51 ? 275  ILE A CG1 1 
ATOM   2002 C  CG2 . ILE A 1 275 ? 6.186   -35.603 28.860  1.00 15.98 ? 275  ILE A CG2 1 
ATOM   2003 C  CD1 . ILE A 1 275 ? 8.413   -33.828 27.513  1.00 18.37 ? 275  ILE A CD1 1 
ATOM   2004 N  N   . SER A 1 276 ? 2.868   -34.175 28.572  1.00 18.08 ? 276  SER A N   1 
ATOM   2005 C  CA  . SER A 1 276 ? 1.769   -34.468 29.488  1.00 18.84 ? 276  SER A CA  1 
ATOM   2006 C  C   . SER A 1 276 ? 0.524   -34.947 28.750  1.00 19.03 ? 276  SER A C   1 
ATOM   2007 O  O   . SER A 1 276 ? -0.164  -35.863 29.220  1.00 20.81 ? 276  SER A O   1 
ATOM   2008 C  CB  . SER A 1 276 ? 1.459   -33.238 30.330  1.00 23.37 ? 276  SER A CB  1 
ATOM   2009 O  OG  . SER A 1 276 ? 2.623   -32.832 31.034  1.00 26.06 ? 276  SER A OG  1 
ATOM   2010 N  N   . ALA A 1 277 ? 0.225   -34.364 27.584  1.00 20.15 ? 277  ALA A N   1 
ATOM   2011 C  CA  . ALA A 1 277 ? -0.903  -34.849 26.793  1.00 17.14 ? 277  ALA A CA  1 
ATOM   2012 C  C   . ALA A 1 277 ? -0.664  -36.271 26.312  1.00 21.42 ? 277  ALA A C   1 
ATOM   2013 O  O   . ALA A 1 277 ? -1.568  -37.118 26.349  1.00 18.28 ? 277  ALA A O   1 
ATOM   2014 C  CB  . ALA A 1 277 ? -1.149  -33.936 25.590  1.00 20.53 ? 277  ALA A CB  1 
ATOM   2015 N  N   . LEU A 1 278 ? 0.541   -36.542 25.804  1.00 19.88 ? 278  LEU A N   1 
ATOM   2016 C  CA  . LEU A 1 278 ? 0.831   -37.880 25.304  1.00 17.86 ? 278  LEU A CA  1 
ATOM   2017 C  C   . LEU A 1 278 ? 0.748   -38.896 26.438  1.00 18.69 ? 278  LEU A C   1 
ATOM   2018 O  O   . LEU A 1 278 ? 0.082   -39.932 26.311  1.00 20.51 ? 278  LEU A O   1 
ATOM   2019 C  CB  . LEU A 1 278 ? 2.206   -37.896 24.619  1.00 16.79 ? 278  LEU A CB  1 
ATOM   2020 C  CG  . LEU A 1 278 ? 2.245   -37.052 23.320  1.00 19.09 ? 278  LEU A CG  1 
ATOM   2021 C  CD1 . LEU A 1 278 ? 3.663   -36.671 22.880  1.00 16.53 ? 278  LEU A CD1 1 
ATOM   2022 C  CD2 . LEU A 1 278 ? 1.532   -37.778 22.181  1.00 15.33 ? 278  LEU A CD2 1 
ATOM   2023 N  N   . GLN A 1 279 ? 1.383   -38.585 27.573  1.00 17.47 ? 279  GLN A N   1 
ATOM   2024 C  CA  . GLN A 1 279 ? 1.318   -39.461 28.740  1.00 19.87 ? 279  GLN A CA  1 
ATOM   2025 C  C   . GLN A 1 279 ? -0.127  -39.723 29.151  1.00 20.09 ? 279  GLN A C   1 
ATOM   2026 O  O   . GLN A 1 279 ? -0.526  -40.873 29.369  1.00 19.05 ? 279  GLN A O   1 
ATOM   2027 C  CB  . GLN A 1 279 ? 2.110   -38.847 29.898  1.00 21.11 ? 279  GLN A CB  1 
ATOM   2028 C  CG  . GLN A 1 279 ? 3.626   -39.010 29.758  1.00 18.06 ? 279  GLN A CG  1 
ATOM   2029 C  CD  . GLN A 1 279 ? 4.412   -38.255 30.802  1.00 24.03 ? 279  GLN A CD  1 
ATOM   2030 O  OE1 . GLN A 1 279 ? 3.976   -37.211 31.304  1.00 24.93 ? 279  GLN A OE1 1 
ATOM   2031 N  NE2 . GLN A 1 279 ? 5.589   -38.772 31.133  1.00 25.26 ? 279  GLN A NE2 1 
ATOM   2032 N  N   . SER A 1 280 ? -0.936  -38.669 29.258  1.00 19.49 ? 280  SER A N   1 
ATOM   2033 C  CA  . SER A 1 280 ? -2.307  -38.899 29.697  1.00 24.12 ? 280  SER A CA  1 
ATOM   2034 C  C   . SER A 1 280 ? -3.100  -39.688 28.657  1.00 21.33 ? 280  SER A C   1 
ATOM   2035 O  O   . SER A 1 280 ? -4.100  -40.318 29.007  1.00 23.72 ? 280  SER A O   1 
ATOM   2036 C  CB  . SER A 1 280 ? -2.980  -37.569 30.053  1.00 21.62 ? 280  SER A CB  1 
ATOM   2037 O  OG  . SER A 1 280 ? -3.129  -36.743 28.915  1.00 38.52 ? 280  SER A OG  1 
ATOM   2038 N  N   . ALA A 1 281 ? -2.622  -39.754 27.413  1.00 22.14 ? 281  ALA A N   1 
ATOM   2039 C  CA  . ALA A 1 281 ? -3.234  -40.596 26.393  1.00 19.07 ? 281  ALA A CA  1 
ATOM   2040 C  C   . ALA A 1 281 ? -2.743  -42.039 26.424  1.00 19.15 ? 281  ALA A C   1 
ATOM   2041 O  O   . ALA A 1 281 ? -3.240  -42.862 25.655  1.00 23.20 ? 281  ALA A O   1 
ATOM   2042 C  CB  . ALA A 1 281 ? -2.984  -40.002 25.002  1.00 22.32 ? 281  ALA A CB  1 
ATOM   2043 N  N   . GLY A 1 282 ? -1.782  -42.367 27.279  1.00 19.77 ? 282  GLY A N   1 
ATOM   2044 C  CA  . GLY A 1 282 ? -1.252  -43.711 27.321  1.00 21.12 ? 282  GLY A CA  1 
ATOM   2045 C  C   . GLY A 1 282 ? -0.022  -43.918 26.473  1.00 20.86 ? 282  GLY A C   1 
ATOM   2046 O  O   . GLY A 1 282 ? 0.400   -45.064 26.288  1.00 16.32 ? 282  GLY A O   1 
ATOM   2047 N  N   . VAL A 1 283 ? 0.548   -42.851 25.923  1.00 21.30 ? 283  VAL A N   1 
ATOM   2048 C  CA  . VAL A 1 283 ? 1.827   -42.960 25.230  1.00 19.35 ? 283  VAL A CA  1 
ATOM   2049 C  C   . VAL A 1 283 ? 2.931   -42.990 26.275  1.00 18.34 ? 283  VAL A C   1 
ATOM   2050 O  O   . VAL A 1 283 ? 2.887   -42.242 27.259  1.00 17.37 ? 283  VAL A O   1 
ATOM   2051 C  CB  . VAL A 1 283 ? 2.014   -41.791 24.247  1.00 18.25 ? 283  VAL A CB  1 
ATOM   2052 C  CG1 . VAL A 1 283 ? 3.406   -41.839 23.620  1.00 15.99 ? 283  VAL A CG1 1 
ATOM   2053 C  CG2 . VAL A 1 283 ? 0.954   -41.847 23.167  1.00 16.21 ? 283  VAL A CG2 1 
ATOM   2054 N  N   . VAL A 1 284 ? 3.929   -43.850 26.081  1.00 17.94 ? 284  VAL A N   1 
ATOM   2055 C  CA  . VAL A 1 284 ? 5.093   -43.862 26.964  1.00 18.27 ? 284  VAL A CA  1 
ATOM   2056 C  C   . VAL A 1 284 ? 6.141   -42.905 26.396  1.00 16.59 ? 284  VAL A C   1 
ATOM   2057 O  O   . VAL A 1 284 ? 6.603   -43.061 25.263  1.00 14.08 ? 284  VAL A O   1 
ATOM   2058 C  CB  . VAL A 1 284 ? 5.639   -45.284 27.135  1.00 18.60 ? 284  VAL A CB  1 
ATOM   2059 C  CG1 . VAL A 1 284 ? 6.909   -45.287 27.990  1.00 19.79 ? 284  VAL A CG1 1 
ATOM   2060 C  CG2 . VAL A 1 284 ? 4.555   -46.140 27.777  1.00 21.07 ? 284  VAL A CG2 1 
ATOM   2061 N  N   . VAL A 1 285 ? 6.488   -41.886 27.163  1.00 15.50 ? 285  VAL A N   1 
ATOM   2062 C  CA  . VAL A 1 285 ? 7.384   -40.842 26.687  1.00 18.49 ? 285  VAL A CA  1 
ATOM   2063 C  C   . VAL A 1 285 ? 8.776   -41.135 27.217  1.00 18.59 ? 285  VAL A C   1 
ATOM   2064 O  O   . VAL A 1 285 ? 8.973   -41.260 28.427  1.00 21.20 ? 285  VAL A O   1 
ATOM   2065 C  CB  . VAL A 1 285 ? 6.923   -39.446 27.128  1.00 16.41 ? 285  VAL A CB  1 
ATOM   2066 C  CG1 . VAL A 1 285 ? 7.987   -38.430 26.751  1.00 15.91 ? 285  VAL A CG1 1 
ATOM   2067 C  CG2 . VAL A 1 285 ? 5.555   -39.087 26.502  1.00 19.29 ? 285  VAL A CG2 1 
ATOM   2068 N  N   . SER A 1 286 ? 9.734   -41.264 26.314  1.00 17.80 ? 286  SER A N   1 
ATOM   2069 C  CA  . SER A 1 286 ? 11.136  -41.309 26.699  1.00 17.22 ? 286  SER A CA  1 
ATOM   2070 C  C   . SER A 1 286 ? 11.599  -39.881 26.979  1.00 17.62 ? 286  SER A C   1 
ATOM   2071 O  O   . SER A 1 286 ? 11.558  -39.017 26.092  1.00 20.08 ? 286  SER A O   1 
ATOM   2072 C  CB  . SER A 1 286 ? 11.956  -41.961 25.585  1.00 17.67 ? 286  SER A CB  1 
ATOM   2073 O  OG  . SER A 1 286 ? 13.325  -42.070 25.944  1.00 21.79 ? 286  SER A OG  1 
ATOM   2074 N  N   . MET A 1 287 ? 11.992  -39.604 28.220  1.00 17.89 ? 287  MET A N   1 
ATOM   2075 C  CA  . MET A 1 287 ? 12.539  -38.286 28.506  1.00 18.58 ? 287  MET A CA  1 
ATOM   2076 C  C   . MET A 1 287 ? 13.805  -38.048 27.690  1.00 17.22 ? 287  MET A C   1 
ATOM   2077 O  O   . MET A 1 287 ? 14.029  -36.942 27.180  1.00 17.72 ? 287  MET A O   1 
ATOM   2078 C  CB  . MET A 1 287 ? 12.817  -38.137 30.000  1.00 19.74 ? 287  MET A CB  1 
ATOM   2079 C  CG  . MET A 1 287 ? 11.571  -38.119 30.901  1.00 23.87 ? 287  MET A CG  1 
ATOM   2080 S  SD  . MET A 1 287 ? 10.279  -37.033 30.276  1.00 32.20 ? 287  MET A SD  1 
ATOM   2081 C  CE  . MET A 1 287 ? 11.011  -35.394 30.426  1.00 27.89 ? 287  MET A CE  1 
ATOM   2082 N  N   . SER A 1 288 ? 14.626  -39.095 27.519  1.00 18.32 ? 288  SER A N   1 
ATOM   2083 C  CA  . SER A 1 288 ? 15.889  -38.954 26.805  1.00 15.00 ? 288  SER A CA  1 
ATOM   2084 C  C   . SER A 1 288 ? 15.753  -39.330 25.331  1.00 15.61 ? 288  SER A C   1 
ATOM   2085 O  O   . SER A 1 288 ? 15.129  -40.338 24.997  1.00 14.70 ? 288  SER A O   1 
ATOM   2086 C  CB  . SER A 1 288 ? 16.974  -39.823 27.446  1.00 18.28 ? 288  SER A CB  1 
ATOM   2087 O  OG  . SER A 1 288 ? 18.145  -39.787 26.655  1.00 15.63 ? 288  SER A OG  1 
ATOM   2088 N  N   . PRO A 1 289 ? 16.364  -38.549 24.433  1.00 15.73 ? 289  PRO A N   1 
ATOM   2089 C  CA  . PRO A 1 289 ? 16.381  -38.943 23.018  1.00 17.04 ? 289  PRO A CA  1 
ATOM   2090 C  C   . PRO A 1 289 ? 17.234  -40.168 22.754  1.00 14.97 ? 289  PRO A C   1 
ATOM   2091 O  O   . PRO A 1 289 ? 17.058  -40.815 21.714  1.00 17.98 ? 289  PRO A O   1 
ATOM   2092 C  CB  . PRO A 1 289 ? 16.950  -37.703 22.313  1.00 15.82 ? 289  PRO A CB  1 
ATOM   2093 C  CG  . PRO A 1 289 ? 17.820  -37.054 23.351  1.00 15.39 ? 289  PRO A CG  1 
ATOM   2094 C  CD  . PRO A 1 289 ? 17.117  -37.303 24.678  1.00 17.10 ? 289  PRO A CD  1 
ATOM   2095 N  N   . ALA A 1 290 ? 18.143  -40.509 23.662  1.00 15.29 ? 290  ALA A N   1 
ATOM   2096 C  CA  . ALA A 1 290 ? 18.984  -41.681 23.480  1.00 17.95 ? 290  ALA A CA  1 
ATOM   2097 C  C   . ALA A 1 290 ? 18.279  -42.979 23.845  1.00 15.98 ? 290  ALA A C   1 
ATOM   2098 O  O   . ALA A 1 290 ? 18.793  -44.059 23.517  1.00 16.71 ? 290  ALA A O   1 
ATOM   2099 C  CB  . ALA A 1 290 ? 20.268  -41.534 24.310  1.00 18.15 ? 290  ALA A CB  1 
ATOM   2100 N  N   . GLN A 1 291 ? 17.113  -42.913 24.498  1.00 16.62 ? 291  GLN A N   1 
ATOM   2101 C  CA  . GLN A 1 291 ? 16.488  -44.108 25.064  1.00 16.06 ? 291  GLN A CA  1 
ATOM   2102 C  C   . GLN A 1 291 ? 15.205  -44.508 24.346  1.00 18.19 ? 291  GLN A C   1 
ATOM   2103 O  O   . GLN A 1 291 ? 14.351  -45.171 24.944  1.00 17.95 ? 291  GLN A O   1 
ATOM   2104 C  CB  . GLN A 1 291 ? 16.200  -43.918 26.556  1.00 15.12 ? 291  GLN A CB  1 
ATOM   2105 C  CG  . GLN A 1 291 ? 17.434  -43.577 27.389  1.00 15.69 ? 291  GLN A CG  1 
ATOM   2106 C  CD  . GLN A 1 291 ? 18.602  -44.531 27.133  1.00 21.75 ? 291  GLN A CD  1 
ATOM   2107 O  OE1 . GLN A 1 291 ? 18.408  -45.718 26.866  1.00 19.47 ? 291  GLN A OE1 1 
ATOM   2108 N  NE2 . GLN A 1 291 ? 19.828  -44.002 27.201  1.00 20.77 ? 291  GLN A NE2 1 
ATOM   2109 N  N   . LEU A 1 292 ? 15.050  -44.133 23.077  1.00 18.27 ? 292  LEU A N   1 
ATOM   2110 C  CA  . LEU A 1 292 ? 13.841  -44.515 22.358  1.00 15.80 ? 292  LEU A CA  1 
ATOM   2111 C  C   . LEU A 1 292 ? 13.848  -45.999 22.036  1.00 19.10 ? 292  LEU A C   1 
ATOM   2112 O  O   . LEU A 1 292 ? 12.817  -46.674 22.176  1.00 16.60 ? 292  LEU A O   1 
ATOM   2113 C  CB  . LEU A 1 292 ? 13.691  -43.679 21.091  1.00 14.87 ? 292  LEU A CB  1 
ATOM   2114 C  CG  . LEU A 1 292 ? 13.256  -42.221 21.261  1.00 14.90 ? 292  LEU A CG  1 
ATOM   2115 C  CD1 . LEU A 1 292 ? 13.632  -41.451 20.032  1.00 20.31 ? 292  LEU A CD1 1 
ATOM   2116 C  CD2 . LEU A 1 292 ? 11.737  -42.166 21.471  1.00 14.62 ? 292  LEU A CD2 1 
ATOM   2117 N  N   . GLY A 1 293 ? 15.001  -46.530 21.611  1.00 15.75 ? 293  GLY A N   1 
ATOM   2118 C  CA  . GLY A 1 293 ? 15.084  -47.956 21.339  1.00 15.84 ? 293  GLY A CA  1 
ATOM   2119 C  C   . GLY A 1 293 ? 14.859  -48.792 22.583  1.00 18.08 ? 293  GLY A C   1 
ATOM   2120 O  O   . GLY A 1 293 ? 14.088  -49.758 22.570  1.00 18.16 ? 293  GLY A O   1 
ATOM   2121 N  N   . THR A 1 294 ? 15.502  -48.409 23.692  1.00 20.05 ? 294  THR A N   1 
ATOM   2122 C  CA  . THR A 1 294 ? 15.389  -49.208 24.910  1.00 20.04 ? 294  THR A CA  1 
ATOM   2123 C  C   . THR A 1 294 ? 14.008  -49.078 25.541  1.00 20.47 ? 294  THR A C   1 
ATOM   2124 O  O   . THR A 1 294 ? 13.500  -50.055 26.112  1.00 18.72 ? 294  THR A O   1 
ATOM   2125 C  CB  . THR A 1 294 ? 16.484  -48.831 25.917  1.00 17.00 ? 294  THR A CB  1 
ATOM   2126 O  OG1 . THR A 1 294 ? 16.395  -47.446 26.269  1.00 20.25 ? 294  THR A OG1 1 
ATOM   2127 C  CG2 . THR A 1 294 ? 17.872  -49.111 25.333  1.00 18.85 ? 294  THR A CG2 1 
ATOM   2128 N  N   . THR A 1 295 ? 13.370  -47.907 25.419  1.00 17.68 ? 295  THR A N   1 
ATOM   2129 C  CA  . THR A 1 295 ? 12.033  -47.739 25.980  1.00 17.63 ? 295  THR A CA  1 
ATOM   2130 C  C   . THR A 1 295 ? 11.022  -48.619 25.246  1.00 17.58 ? 295  THR A C   1 
ATOM   2131 O  O   . THR A 1 295 ? 10.268  -49.362 25.883  1.00 16.83 ? 295  THR A O   1 
ATOM   2132 C  CB  . THR A 1 295 ? 11.610  -46.262 25.961  1.00 16.93 ? 295  THR A CB  1 
ATOM   2133 O  OG1 . THR A 1 295 ? 12.549  -45.494 26.714  1.00 13.98 ? 295  THR A OG1 1 
ATOM   2134 C  CG2 . THR A 1 295 ? 10.212  -46.052 26.605  1.00 14.54 ? 295  THR A CG2 1 
ATOM   2135 N  N   . ILE A 1 296 ? 11.017  -48.594 23.908  1.00 17.45 ? 296  ILE A N   1 
ATOM   2136 C  CA  . ILE A 1 296 ? 9.995   -49.378 23.210  1.00 16.64 ? 296  ILE A CA  1 
ATOM   2137 C  C   . ILE A 1 296 ? 10.289  -50.867 23.315  1.00 19.05 ? 296  ILE A C   1 
ATOM   2138 O  O   . ILE A 1 296 ? 9.357   -51.682 23.353  1.00 19.87 ? 296  ILE A O   1 
ATOM   2139 C  CB  . ILE A 1 296 ? 9.818   -48.939 21.741  1.00 14.95 ? 296  ILE A CB  1 
ATOM   2140 C  CG1 . ILE A 1 296 ? 8.534   -49.577 21.171  1.00 19.37 ? 296  ILE A CG1 1 
ATOM   2141 C  CG2 . ILE A 1 296 ? 11.056  -49.287 20.901  1.00 13.02 ? 296  ILE A CG2 1 
ATOM   2142 C  CD1 . ILE A 1 296 ? 7.951   -48.845 19.973  1.00 18.30 ? 296  ILE A CD1 1 
ATOM   2143 N  N   . TYR A 1 297 ? 11.569  -51.253 23.379  1.00 18.75 ? 297  TYR A N   1 
ATOM   2144 C  CA  . TYR A 1 297 ? 11.894  -52.646 23.658  1.00 18.69 ? 297  TYR A CA  1 
ATOM   2145 C  C   . TYR A 1 297 ? 11.318  -53.080 25.001  1.00 20.07 ? 297  TYR A C   1 
ATOM   2146 O  O   . TYR A 1 297 ? 10.741  -54.166 25.116  1.00 18.24 ? 297  TYR A O   1 
ATOM   2147 C  CB  . TYR A 1 297 ? 13.407  -52.866 23.623  1.00 22.68 ? 297  TYR A CB  1 
ATOM   2148 C  CG  . TYR A 1 297 ? 13.799  -54.327 23.776  1.00 24.07 ? 297  TYR A CG  1 
ATOM   2149 C  CD1 . TYR A 1 297 ? 13.832  -54.930 25.029  1.00 31.21 ? 297  TYR A CD1 1 
ATOM   2150 C  CD2 . TYR A 1 297 ? 14.142  -55.096 22.671  1.00 24.98 ? 297  TYR A CD2 1 
ATOM   2151 C  CE1 . TYR A 1 297 ? 14.188  -56.261 25.180  1.00 34.06 ? 297  TYR A CE1 1 
ATOM   2152 C  CE2 . TYR A 1 297 ? 14.501  -56.435 22.809  1.00 35.72 ? 297  TYR A CE2 1 
ATOM   2153 C  CZ  . TYR A 1 297 ? 14.519  -57.011 24.071  1.00 33.11 ? 297  TYR A CZ  1 
ATOM   2154 O  OH  . TYR A 1 297 ? 14.869  -58.335 24.236  1.00 38.10 ? 297  TYR A OH  1 
ATOM   2155 N  N   . LYS A 1 298 ? 11.449  -52.244 26.033  1.00 19.02 ? 298  LYS A N   1 
ATOM   2156 C  CA  . LYS A 1 298 ? 10.862  -52.611 27.314  1.00 20.98 ? 298  LYS A CA  1 
ATOM   2157 C  C   . LYS A 1 298 ? 9.339   -52.685 27.217  1.00 23.15 ? 298  LYS A C   1 
ATOM   2158 O  O   . LYS A 1 298 ? 8.721   -53.587 27.793  1.00 18.53 ? 298  LYS A O   1 
ATOM   2159 C  CB  . LYS A 1 298 ? 11.301  -51.633 28.404  1.00 21.76 ? 298  LYS A CB  1 
ATOM   2160 C  CG  . LYS A 1 298 ? 12.771  -51.763 28.795  1.00 27.30 ? 298  LYS A CG  1 
ATOM   2161 C  CD  . LYS A 1 298 ? 13.237  -50.553 29.628  1.00 27.27 ? 298  LYS A CD  1 
ATOM   2162 C  CE  . LYS A 1 298 ? 14.744  -50.582 29.891  1.00 37.36 ? 298  LYS A CE  1 
ATOM   2163 N  NZ  . LYS A 1 298 ? 15.211  -49.302 30.508  1.00 46.83 ? 298  LYS A NZ  1 
ATOM   2164 N  N   . GLU A 1 299 ? 8.718   -51.774 26.455  1.00 19.05 ? 299  GLU A N   1 
ATOM   2165 C  CA  . GLU A 1 299 ? 7.266   -51.830 26.287  1.00 24.26 ? 299  GLU A CA  1 
ATOM   2166 C  C   . GLU A 1 299 ? 6.830   -53.126 25.609  1.00 21.24 ? 299  GLU A C   1 
ATOM   2167 O  O   . GLU A 1 299 ? 5.831   -53.728 26.013  1.00 22.87 ? 299  GLU A O   1 
ATOM   2168 C  CB  . GLU A 1 299 ? 6.756   -50.612 25.509  1.00 23.02 ? 299  GLU A CB  1 
ATOM   2169 C  CG  . GLU A 1 299 ? 6.765   -49.321 26.316  1.00 23.13 ? 299  GLU A CG  1 
ATOM   2170 C  CD  . GLU A 1 299 ? 6.033   -49.468 27.647  1.00 30.94 ? 299  GLU A CD  1 
ATOM   2171 O  OE1 . GLU A 1 299 ? 4.898   -49.990 27.656  1.00 28.54 ? 299  GLU A OE1 1 
ATOM   2172 O  OE2 . GLU A 1 299 ? 6.601   -49.068 28.687  1.00 32.63 ? 299  GLU A OE2 1 
ATOM   2173 N  N   . PHE A 1 300 ? 7.569   -53.586 24.588  1.00 19.11 ? 300  PHE A N   1 
ATOM   2174 C  CA  . PHE A 1 300 ? 7.240   -54.876 23.976  1.00 19.84 ? 300  PHE A CA  1 
ATOM   2175 C  C   . PHE A 1 300 ? 7.303   -56.003 24.996  1.00 24.16 ? 300  PHE A C   1 
ATOM   2176 O  O   . PHE A 1 300 ? 6.394   -56.837 25.064  1.00 28.99 ? 300  PHE A O   1 
ATOM   2177 C  CB  . PHE A 1 300 ? 8.175   -55.182 22.803  1.00 24.97 ? 300  PHE A CB  1 
ATOM   2178 C  CG  . PHE A 1 300 ? 7.694   -54.616 21.494  1.00 22.89 ? 300  PHE A CG  1 
ATOM   2179 C  CD1 . PHE A 1 300 ? 7.441   -53.260 21.371  1.00 23.82 ? 300  PHE A CD1 1 
ATOM   2180 C  CD2 . PHE A 1 300 ? 7.475   -55.440 20.399  1.00 30.35 ? 300  PHE A CD2 1 
ATOM   2181 C  CE1 . PHE A 1 300 ? 6.981   -52.719 20.161  1.00 23.32 ? 300  PHE A CE1 1 
ATOM   2182 C  CE2 . PHE A 1 300 ? 7.026   -54.913 19.188  1.00 30.38 ? 300  PHE A CE2 1 
ATOM   2183 C  CZ  . PHE A 1 300 ? 6.784   -53.537 19.077  1.00 22.41 ? 300  PHE A CZ  1 
ATOM   2184 N  N   . GLU A 1 301 ? 8.362   -56.037 25.806  1.00 22.56 ? 301  GLU A N   1 
ATOM   2185 C  CA  . GLU A 1 301 ? 8.504   -57.101 26.795  1.00 26.88 ? 301  GLU A CA  1 
ATOM   2186 C  C   . GLU A 1 301 ? 7.396   -57.047 27.845  1.00 26.20 ? 301  GLU A C   1 
ATOM   2187 O  O   . GLU A 1 301 ? 6.930   -58.097 28.304  1.00 23.69 ? 301  GLU A O   1 
ATOM   2188 C  CB  . GLU A 1 301 ? 9.885   -57.023 27.441  1.00 22.06 ? 301  GLU A CB  1 
ATOM   2189 C  CG  . GLU A 1 301 ? 11.023  -57.412 26.506  1.00 27.14 ? 301  GLU A CG  1 
ATOM   2190 C  CD  . GLU A 1 301 ? 10.928  -58.870 26.039  1.00 37.58 ? 301  GLU A CD  1 
ATOM   2191 O  OE1 . GLU A 1 301 ? 10.312  -59.127 24.976  1.00 39.04 ? 301  GLU A OE1 1 
ATOM   2192 O  OE2 . GLU A 1 301 ? 11.463  -59.758 26.744  1.00 40.34 ? 301  GLU A OE2 1 
ATOM   2193 N  N   . LYS A 1 302 ? 6.941   -55.839 28.224  1.00 21.48 ? 302  LYS A N   1 
ATOM   2194 C  CA  . LYS A 1 302 ? 5.816   -55.745 29.164  1.00 25.44 ? 302  LYS A CA  1 
ATOM   2195 C  C   . LYS A 1 302 ? 4.512   -56.240 28.538  1.00 26.92 ? 302  LYS A C   1 
ATOM   2196 O  O   . LYS A 1 302 ? 3.709   -56.905 29.211  1.00 23.05 ? 302  LYS A O   1 
ATOM   2197 C  CB  . LYS A 1 302 ? 5.642   -54.312 29.674  1.00 28.14 ? 302  LYS A CB  1 
ATOM   2198 C  CG  . LYS A 1 302 ? 6.754   -53.824 30.598  1.00 31.63 ? 302  LYS A CG  1 
ATOM   2199 C  CD  . LYS A 1 302 ? 6.466   -52.420 31.134  1.00 35.92 ? 302  LYS A CD  1 
ATOM   2200 N  N   . ARG A 1 303 ? 4.269   -55.900 27.266  1.00 24.72 ? 303  ARG A N   1 
ATOM   2201 C  CA  . ARG A 1 303 ? 3.108   -56.434 26.553  1.00 26.58 ? 303  ARG A CA  1 
ATOM   2202 C  C   . ARG A 1 303 ? 3.153   -57.952 26.476  1.00 26.78 ? 303  ARG A C   1 
ATOM   2203 O  O   . ARG A 1 303 ? 2.123   -58.619 26.634  1.00 28.44 ? 303  ARG A O   1 
ATOM   2204 C  CB  . ARG A 1 303 ? 3.023   -55.852 25.139  1.00 24.60 ? 303  ARG A CB  1 
ATOM   2205 C  CG  . ARG A 1 303 ? 2.804   -54.343 25.082  1.00 33.58 ? 303  ARG A CG  1 
ATOM   2206 C  CD  . ARG A 1 303 ? 1.533   -53.930 25.805  1.00 35.56 ? 303  ARG A CD  1 
ATOM   2207 N  NE  . ARG A 1 303 ? 1.230   -52.512 25.605  1.00 39.94 ? 303  ARG A NE  1 
ATOM   2208 C  CZ  . ARG A 1 303 ? 0.360   -52.058 24.707  1.00 34.32 ? 303  ARG A CZ  1 
ATOM   2209 N  NH1 . ARG A 1 303 ? 0.142   -50.753 24.593  1.00 28.25 ? 303  ARG A NH1 1 
ATOM   2210 N  NH2 . ARG A 1 303 ? -0.293  -52.919 23.928  1.00 26.34 ? 303  ARG A NH2 1 
ATOM   2211 N  N   . LYS A 1 304 ? 4.327   -58.514 26.177  1.00 24.62 ? 304  LYS A N   1 
ATOM   2212 C  CA  . LYS A 1 304 ? 4.491   -59.964 26.229  1.00 30.47 ? 304  LYS A CA  1 
ATOM   2213 C  C   . LYS A 1 304 ? 4.049   -60.511 27.578  1.00 28.00 ? 304  LYS A C   1 
ATOM   2214 O  O   . LYS A 1 304 ? 3.279   -61.475 27.649  1.00 27.63 ? 304  LYS A O   1 
ATOM   2215 C  CB  . LYS A 1 304 ? 5.948   -60.353 25.970  1.00 30.38 ? 304  LYS A CB  1 
ATOM   2216 C  CG  . LYS A 1 304 ? 6.256   -60.816 24.565  1.00 34.34 ? 304  LYS A CG  1 
ATOM   2217 C  CD  . LYS A 1 304 ? 6.518   -59.638 23.648  1.00 36.60 ? 304  LYS A CD  1 
ATOM   2218 C  CE  . LYS A 1 304 ? 7.426   -60.023 22.491  1.00 36.98 ? 304  LYS A CE  1 
ATOM   2219 N  NZ  . LYS A 1 304 ? 7.405   -58.988 21.420  1.00 34.86 ? 304  LYS A NZ  1 
ATOM   2220 N  N   . MET A 1 305 ? 4.537   -59.915 28.668  1.00 26.20 ? 305  MET A N   1 
ATOM   2221 C  CA  . MET A 1 305 ? 4.255   -60.499 29.978  1.00 26.16 ? 305  MET A CA  1 
ATOM   2222 C  C   . MET A 1 305 ? 2.778   -60.356 30.321  1.00 28.91 ? 305  MET A C   1 
ATOM   2223 O  O   . MET A 1 305 ? 2.154   -61.307 30.816  1.00 26.69 ? 305  MET A O   1 
ATOM   2224 C  CB  . MET A 1 305 ? 5.132   -59.856 31.052  1.00 27.70 ? 305  MET A CB  1 
ATOM   2225 C  CG  . MET A 1 305 ? 6.622   -60.203 30.957  1.00 35.11 ? 305  MET A CG  1 
ATOM   2226 S  SD  . MET A 1 305 ? 7.034   -61.975 30.867  1.00 51.73 ? 305  MET A SD  1 
ATOM   2227 C  CE  . MET A 1 305 ? 6.338   -62.611 32.387  1.00 37.97 ? 305  MET A CE  1 
ATOM   2228 N  N   . LEU A 1 306 ? 2.196   -59.187 30.021  1.00 24.75 ? 306  LEU A N   1 
ATOM   2229 C  CA  . LEU A 1 306 ? 0.779   -58.954 30.287  1.00 28.64 ? 306  LEU A CA  1 
ATOM   2230 C  C   . LEU A 1 306 ? -0.095  -59.912 29.493  1.00 27.00 ? 306  LEU A C   1 
ATOM   2231 O  O   . LEU A 1 306 ? -1.068  -60.461 30.022  1.00 25.19 ? 306  LEU A O   1 
ATOM   2232 C  CB  . LEU A 1 306 ? 0.401   -57.509 29.947  1.00 30.41 ? 306  LEU A CB  1 
ATOM   2233 C  CG  . LEU A 1 306 ? 0.899   -56.319 30.776  1.00 35.63 ? 306  LEU A CG  1 
ATOM   2234 C  CD1 . LEU A 1 306 ? 0.363   -55.020 30.175  1.00 35.80 ? 306  LEU A CD1 1 
ATOM   2235 C  CD2 . LEU A 1 306 ? 0.475   -56.433 32.240  1.00 32.19 ? 306  LEU A CD2 1 
ATOM   2236 N  N   . GLU A 1 307 ? 0.229   -60.114 28.214  1.00 25.75 ? 307  GLU A N   1 
ATOM   2237 C  CA  . GLU A 1 307 ? -0.589  -60.994 27.384  1.00 31.46 ? 307  GLU A CA  1 
ATOM   2238 C  C   . GLU A 1 307 ? -0.565  -62.427 27.918  1.00 32.84 ? 307  GLU A C   1 
ATOM   2239 O  O   . GLU A 1 307 ? -1.587  -63.126 27.907  1.00 29.59 ? 307  GLU A O   1 
ATOM   2240 C  CB  . GLU A 1 307 ? -0.095  -60.941 25.937  1.00 36.19 ? 307  GLU A CB  1 
ATOM   2241 C  CG  . GLU A 1 307 ? -1.143  -60.566 24.878  1.00 37.98 ? 307  GLU A CG  1 
ATOM   2242 C  CD  . GLU A 1 307 ? -1.708  -59.170 25.043  1.00 39.52 ? 307  GLU A CD  1 
ATOM   2243 O  OE1 . GLU A 1 307 ? -2.947  -59.035 25.071  1.00 42.57 ? 307  GLU A OE1 1 
ATOM   2244 O  OE2 . GLU A 1 307 ? -0.918  -58.204 25.143  1.00 47.74 ? 307  GLU A OE2 1 
ATOM   2245 N  N   . ASN A 1 308 ? 0.590   -62.874 28.407  1.00 28.91 ? 308  ASN A N   1 
ATOM   2246 C  CA  . ASN A 1 308 ? 0.702   -64.221 28.951  1.00 31.41 ? 308  ASN A CA  1 
ATOM   2247 C  C   . ASN A 1 308 ? 0.104   -64.318 30.350  1.00 31.60 ? 308  ASN A C   1 
ATOM   2248 O  O   . ASN A 1 308 ? -0.321  -65.400 30.773  1.00 31.24 ? 308  ASN A O   1 
ATOM   2249 C  CB  . ASN A 1 308 ? 2.169   -64.644 28.971  1.00 33.19 ? 308  ASN A CB  1 
ATOM   2250 C  CG  . ASN A 1 308 ? 2.353   -66.059 29.457  1.00 41.33 ? 308  ASN A CG  1 
ATOM   2251 O  OD1 . ASN A 1 308 ? 2.546   -66.292 30.646  1.00 47.81 ? 308  ASN A OD1 1 
ATOM   2252 N  ND2 . ASN A 1 308 ? 2.280   -67.019 28.540  1.00 48.84 ? 308  ASN A ND2 1 
ATOM   2253 N  N   . LEU A 1 309 ? 0.048   -63.197 31.067  1.00 30.48 ? 309  LEU A N   1 
ATOM   2254 C  CA  . LEU A 1 309 ? -0.461  -63.207 32.426  1.00 27.99 ? 309  LEU A CA  1 
ATOM   2255 C  C   . LEU A 1 309 ? -1.983  -63.277 32.451  1.00 28.97 ? 309  LEU A C   1 
ATOM   2256 O  O   . LEU A 1 309 ? -2.551  -64.085 33.193  1.00 27.38 ? 309  LEU A O   1 
ATOM   2257 C  CB  . LEU A 1 309 ? 0.044   -61.969 33.163  1.00 26.86 ? 309  LEU A CB  1 
ATOM   2258 C  CG  . LEU A 1 309 ? -0.248  -61.806 34.650  1.00 31.49 ? 309  LEU A CG  1 
ATOM   2259 C  CD1 . LEU A 1 309 ? 0.308   -62.982 35.456  1.00 26.58 ? 309  LEU A CD1 1 
ATOM   2260 C  CD2 . LEU A 1 309 ? 0.317   -60.478 35.147  1.00 26.92 ? 309  LEU A CD2 1 
ATOM   2261 N  N   . TYR A 1 310 ? -2.653  -62.470 31.613  1.00 30.93 ? 310  TYR A N   1 
ATOM   2262 C  CA  . TYR A 1 310 ? -4.099  -62.280 31.658  1.00 28.81 ? 310  TYR A CA  1 
ATOM   2263 C  C   . TYR A 1 310 ? -4.837  -62.682 30.383  1.00 29.67 ? 310  TYR A C   1 
ATOM   2264 O  O   . TYR A 1 310 ? -6.067  -62.782 30.417  1.00 30.49 ? 310  TYR A O   1 
ATOM   2265 C  CB  . TYR A 1 310 ? -4.451  -60.804 31.950  1.00 27.31 ? 310  TYR A CB  1 
ATOM   2266 C  CG  . TYR A 1 310 ? -3.922  -60.203 33.249  1.00 29.53 ? 310  TYR A CG  1 
ATOM   2267 C  CD1 . TYR A 1 310 ? -4.351  -60.667 34.480  1.00 36.61 ? 310  TYR A CD1 1 
ATOM   2268 C  CD2 . TYR A 1 310 ? -3.031  -59.138 33.233  1.00 31.87 ? 310  TYR A CD2 1 
ATOM   2269 C  CE1 . TYR A 1 310 ? -3.879  -60.110 35.665  1.00 35.44 ? 310  TYR A CE1 1 
ATOM   2270 C  CE2 . TYR A 1 310 ? -2.557  -58.574 34.408  1.00 31.05 ? 310  TYR A CE2 1 
ATOM   2271 C  CZ  . TYR A 1 310 ? -2.990  -59.066 35.622  1.00 35.14 ? 310  TYR A CZ  1 
ATOM   2272 O  OH  . TYR A 1 310 ? -2.536  -58.515 36.801  1.00 36.69 ? 310  TYR A OH  1 
ATOM   2273 N  N   . PHE A 1 311 ? -4.155  -62.885 29.258  1.00 30.19 ? 311  PHE A N   1 
ATOM   2274 C  CA  . PHE A 1 311 ? -4.858  -63.022 27.983  1.00 33.11 ? 311  PHE A CA  1 
ATOM   2275 C  C   . PHE A 1 311 ? -4.385  -64.241 27.215  1.00 33.12 ? 311  PHE A C   1 
ATOM   2276 O  O   . PHE A 1 311 ? -4.200  -64.197 25.995  1.00 41.19 ? 311  PHE A O   1 
ATOM   2277 C  CB  . PHE A 1 311 ? -4.709  -61.759 27.136  1.00 29.64 ? 311  PHE A CB  1 
ATOM   2278 C  CG  . PHE A 1 311 ? -5.167  -60.532 27.837  1.00 27.22 ? 311  PHE A CG  1 
ATOM   2279 C  CD1 . PHE A 1 311 ? -6.522  -60.283 28.000  1.00 25.60 ? 311  PHE A CD1 1 
ATOM   2280 C  CD2 . PHE A 1 311 ? -4.250  -59.646 28.375  1.00 27.03 ? 311  PHE A CD2 1 
ATOM   2281 C  CE1 . PHE A 1 311 ? -6.957  -59.154 28.685  1.00 27.60 ? 311  PHE A CE1 1 
ATOM   2282 C  CE2 . PHE A 1 311 ? -4.678  -58.509 29.060  1.00 26.02 ? 311  PHE A CE2 1 
ATOM   2283 C  CZ  . PHE A 1 311 ? -6.025  -58.268 29.216  1.00 23.16 ? 311  PHE A CZ  1 
ATOM   2284 N  N   . GLN A 1 312 ? -4.176  -65.345 27.913  1.00 32.76 ? 312  GLN A N   1 
ATOM   2285 C  CA  . GLN A 1 312 ? -3.883  -66.595 27.233  1.00 40.07 ? 312  GLN A CA  1 
ATOM   2286 C  C   . GLN A 1 312 ? -5.145  -67.102 26.533  1.00 39.41 ? 312  GLN A C   1 
ATOM   2287 O  O   . GLN A 1 312 ? -5.122  -67.414 25.343  1.00 44.66 ? 312  GLN A O   1 
ATOM   2288 C  CB  . GLN A 1 312 ? -3.365  -67.642 28.211  1.00 39.18 ? 312  GLN A CB  1 
ATOM   2289 C  CG  . GLN A 1 312 ? -1.993  -67.364 28.787  1.00 38.70 ? 312  GLN A CG  1 
ATOM   2290 C  CD  . GLN A 1 312 ? -1.406  -68.612 29.419  1.00 40.76 ? 312  GLN A CD  1 
ATOM   2291 O  OE1 . GLN A 1 312 ? -1.695  -69.724 28.976  1.00 48.06 ? 312  GLN A OE1 1 
ATOM   2292 N  NE2 . GLN A 1 312 ? -0.591  -68.440 30.462  1.00 34.69 ? 312  GLN A NE2 1 
ATOM   2293 N  N   . MET B 2 1   ? 13.909  -11.422 11.985  1.00 24.17 ? 1    MET B N   1 
ATOM   2294 C  CA  . MET B 2 1   ? 14.387  -10.048 11.846  1.00 27.05 ? 1    MET B CA  1 
ATOM   2295 C  C   . MET B 2 1   ? 13.473  -9.084  12.596  1.00 25.31 ? 1    MET B C   1 
ATOM   2296 O  O   . MET B 2 1   ? 12.442  -9.492  13.129  1.00 26.91 ? 1    MET B O   1 
ATOM   2297 C  CB  . MET B 2 1   ? 14.475  -9.654  10.378  1.00 27.85 ? 1    MET B CB  1 
ATOM   2298 C  CG  . MET B 2 1   ? 13.130  -9.499  9.708   1.00 24.42 ? 1    MET B CG  1 
ATOM   2299 S  SD  . MET B 2 1   ? 13.268  -8.548  8.192   1.00 26.48 ? 1    MET B SD  1 
ATOM   2300 C  CE  . MET B 2 1   ? 13.376  -6.866  8.775   1.00 25.05 ? 1    MET B CE  1 
ATOM   2301 N  N   . ASN B 2 2   ? 13.863  -7.811  12.643  1.00 23.92 ? 2    ASN B N   1 
ATOM   2302 C  CA  . ASN B 2 2   ? 13.189  -6.799  13.451  1.00 23.57 ? 2    ASN B CA  1 
ATOM   2303 C  C   . ASN B 2 2   ? 13.184  -5.472  12.707  1.00 23.31 ? 2    ASN B C   1 
ATOM   2304 O  O   . ASN B 2 2   ? 14.157  -5.140  12.021  1.00 22.75 ? 2    ASN B O   1 
ATOM   2305 C  CB  . ASN B 2 2   ? 13.885  -6.595  14.812  1.00 23.61 ? 2    ASN B CB  1 
ATOM   2306 C  CG  . ASN B 2 2   ? 13.933  -7.853  15.644  1.00 26.52 ? 2    ASN B CG  1 
ATOM   2307 O  OD1 . ASN B 2 2   ? 14.914  -8.590  15.615  1.00 30.11 ? 2    ASN B OD1 1 
ATOM   2308 N  ND2 . ASN B 2 2   ? 12.879  -8.098  16.405  1.00 23.75 ? 2    ASN B ND2 1 
ATOM   2309 N  N   . LEU B 2 3   ? 12.099  -4.707  12.862  1.00 20.67 ? 3    LEU B N   1 
ATOM   2310 C  CA  . LEU B 2 3   ? 12.004  -3.341  12.352  1.00 21.29 ? 3    LEU B CA  1 
ATOM   2311 C  C   . LEU B 2 3   ? 11.773  -2.363  13.494  1.00 24.83 ? 3    LEU B C   1 
ATOM   2312 O  O   . LEU B 2 3   ? 11.028  -2.659  14.435  1.00 20.84 ? 3    LEU B O   1 
ATOM   2313 C  CB  . LEU B 2 3   ? 10.871  -3.183  11.340  1.00 22.10 ? 3    LEU B CB  1 
ATOM   2314 C  CG  . LEU B 2 3   ? 10.975  -3.943  10.019  1.00 20.13 ? 3    LEU B CG  1 
ATOM   2315 C  CD1 . LEU B 2 3   ? 9.676   -3.809  9.246   1.00 18.15 ? 3    LEU B CD1 1 
ATOM   2316 C  CD2 . LEU B 2 3   ? 12.128  -3.443  9.188   1.00 21.08 ? 3    LEU B CD2 1 
ATOM   2317 N  N   . GLN B 2 4   ? 12.424  -1.199  13.413  1.00 23.22 ? 4    GLN B N   1 
ATOM   2318 C  CA  . GLN B 2 4   ? 12.114  -0.112  14.328  1.00 21.08 ? 4    GLN B CA  1 
ATOM   2319 C  C   . GLN B 2 4   ? 10.703  0.409   14.044  1.00 22.32 ? 4    GLN B C   1 
ATOM   2320 O  O   . GLN B 2 4   ? 10.135  0.190   12.970  1.00 18.16 ? 4    GLN B O   1 
ATOM   2321 C  CB  . GLN B 2 4   ? 13.144  1.022   14.200  1.00 22.62 ? 4    GLN B CB  1 
ATOM   2322 C  CG  . GLN B 2 4   ? 14.581  0.727   14.749  1.00 21.21 ? 4    GLN B CG  1 
ATOM   2323 C  CD  . GLN B 2 4   ? 14.732  0.944   16.275  1.00 25.12 ? 4    GLN B CD  1 
ATOM   2324 O  OE1 . GLN B 2 4   ? 13.766  0.857   17.038  1.00 23.13 ? 4    GLN B OE1 1 
ATOM   2325 N  NE2 . GLN B 2 4   ? 15.955  1.237   16.709  1.00 26.29 ? 4    GLN B NE2 1 
ATOM   2326 N  N   . GLU B 2 5   ? 10.144  1.127   15.023  1.00 26.74 ? 5    GLU B N   1 
ATOM   2327 C  CA  . GLU B 2 5   ? 8.789   1.660   14.874  1.00 21.30 ? 5    GLU B CA  1 
ATOM   2328 C  C   . GLU B 2 5   ? 8.644   2.515   13.617  1.00 19.01 ? 5    GLU B C   1 
ATOM   2329 O  O   . GLU B 2 5   ? 7.647   2.396   12.891  1.00 22.06 ? 5    GLU B O   1 
ATOM   2330 C  CB  . GLU B 2 5   ? 8.403   2.477   16.110  1.00 22.34 ? 5    GLU B CB  1 
ATOM   2331 C  CG  . GLU B 2 5   ? 6.935   2.912   16.109  1.00 22.88 ? 5    GLU B CG  1 
ATOM   2332 C  CD  . GLU B 2 5   ? 6.612   3.859   17.255  1.00 22.50 ? 5    GLU B CD  1 
ATOM   2333 O  OE1 . GLU B 2 5   ? 7.546   4.257   17.976  1.00 24.93 ? 5    GLU B OE1 1 
ATOM   2334 O  OE2 . GLU B 2 5   ? 5.432   4.216   17.415  1.00 24.64 ? 5    GLU B OE2 1 
ATOM   2335 N  N   . TYR B 2 6   ? 9.621   3.378   13.330  1.00 20.39 ? 6    TYR B N   1 
ATOM   2336 C  CA  . TYR B 2 6   ? 9.465   4.245   12.161  1.00 23.28 ? 6    TYR B CA  1 
ATOM   2337 C  C   . TYR B 2 6   ? 9.512   3.452   10.863  1.00 24.67 ? 6    TYR B C   1 
ATOM   2338 O  O   . TYR B 2 6   ? 8.897   3.865   9.869   1.00 22.74 ? 6    TYR B O   1 
ATOM   2339 C  CB  . TYR B 2 6   ? 10.509  5.361   12.163  1.00 21.93 ? 6    TYR B CB  1 
ATOM   2340 C  CG  . TYR B 2 6   ? 11.923  4.936   11.886  1.00 22.31 ? 6    TYR B CG  1 
ATOM   2341 C  CD1 . TYR B 2 6   ? 12.412  4.872   10.583  1.00 26.54 ? 6    TYR B CD1 1 
ATOM   2342 C  CD2 . TYR B 2 6   ? 12.788  4.636   12.922  1.00 20.11 ? 6    TYR B CD2 1 
ATOM   2343 C  CE1 . TYR B 2 6   ? 13.716  4.492   10.323  1.00 20.77 ? 6    TYR B CE1 1 
ATOM   2344 C  CE2 . TYR B 2 6   ? 14.091  4.255   12.667  1.00 24.30 ? 6    TYR B CE2 1 
ATOM   2345 C  CZ  . TYR B 2 6   ? 14.542  4.186   11.367  1.00 22.51 ? 6    TYR B CZ  1 
ATOM   2346 O  OH  . TYR B 2 6   ? 15.838  3.794   11.123  1.00 30.83 ? 6    TYR B OH  1 
ATOM   2347 N  N   . GLN B 2 7   ? 10.201  2.303   10.865  1.00 21.67 ? 7    GLN B N   1 
ATOM   2348 C  CA  . GLN B 2 7   ? 10.300  1.466   9.670   1.00 19.31 ? 7    GLN B CA  1 
ATOM   2349 C  C   . GLN B 2 7   ? 9.016   0.686   9.407   1.00 19.03 ? 7    GLN B C   1 
ATOM   2350 O  O   . GLN B 2 7   ? 8.580   0.580   8.256   1.00 19.19 ? 7    GLN B O   1 
ATOM   2351 C  CB  . GLN B 2 7   ? 11.498  0.519   9.797   1.00 25.76 ? 7    GLN B CB  1 
ATOM   2352 C  CG  . GLN B 2 7   ? 12.844  1.188   9.444   1.00 25.21 ? 7    GLN B CG  1 
ATOM   2353 C  CD  . GLN B 2 7   ? 14.044  0.486   10.055  1.00 30.03 ? 7    GLN B CD  1 
ATOM   2354 O  OE1 . GLN B 2 7   ? 13.944  -0.138  11.122  1.00 30.11 ? 7    GLN B OE1 1 
ATOM   2355 N  NE2 . GLN B 2 7   ? 15.191  0.571   9.373   1.00 27.78 ? 7    GLN B NE2 1 
ATOM   2356 N  N   . SER B 2 8   ? 8.393   0.124   10.443  1.00 18.67 ? 8    SER B N   1 
ATOM   2357 C  CA  . SER B 2 8   ? 7.149   -0.602  10.196  1.00 23.78 ? 8    SER B CA  1 
ATOM   2358 C  C   . SER B 2 8   ? 6.020   0.354   9.839   1.00 19.57 ? 8    SER B C   1 
ATOM   2359 O  O   . SER B 2 8   ? 5.205   0.054   8.959   1.00 18.55 ? 8    SER B O   1 
ATOM   2360 C  CB  . SER B 2 8   ? 6.771   -1.467  11.402  1.00 19.06 ? 8    SER B CB  1 
ATOM   2361 O  OG  . SER B 2 8   ? 6.799   -0.730  12.617  1.00 21.73 ? 8    SER B OG  1 
ATOM   2362 N  N   . LYS B 2 9   ? 5.964   1.518   10.496  1.00 14.77 ? 9    LYS B N   1 
ATOM   2363 C  CA  . LYS B 2 9   ? 4.886   2.469   10.238  1.00 16.05 ? 9    LYS B CA  1 
ATOM   2364 C  C   . LYS B 2 9   ? 4.979   3.098   8.847   1.00 16.68 ? 9    LYS B C   1 
ATOM   2365 O  O   . LYS B 2 9   ? 3.947   3.354   8.221   1.00 17.94 ? 9    LYS B O   1 
ATOM   2366 C  CB  . LYS B 2 9   ? 4.870   3.549   11.319  1.00 19.11 ? 9    LYS B CB  1 
ATOM   2367 C  CG  . LYS B 2 9   ? 4.373   3.014   12.648  1.00 20.91 ? 9    LYS B CG  1 
ATOM   2368 C  CD  . LYS B 2 9   ? 3.866   4.086   13.585  1.00 29.54 ? 9    LYS B CD  1 
ATOM   2369 C  CE  . LYS B 2 9   ? 3.192   3.432   14.775  1.00 25.72 ? 9    LYS B CE  1 
ATOM   2370 N  NZ  . LYS B 2 9   ? 2.875   4.401   15.840  1.00 25.39 ? 9    LYS B NZ  1 
ATOM   2371 N  N   . LYS B 2 10  ? 6.192   3.368   8.347   1.00 17.68 ? 10   LYS B N   1 
ATOM   2372 C  CA  . LYS B 2 10  ? 6.333   3.816   6.960   1.00 13.92 ? 10   LYS B CA  1 
ATOM   2373 C  C   . LYS B 2 10  ? 5.855   2.739   5.995   1.00 21.70 ? 10   LYS B C   1 
ATOM   2374 O  O   . LYS B 2 10  ? 5.126   3.020   5.033   1.00 20.76 ? 10   LYS B O   1 
ATOM   2375 C  CB  . LYS B 2 10  ? 7.789   4.179   6.659   1.00 18.71 ? 10   LYS B CB  1 
ATOM   2376 C  CG  . LYS B 2 10  ? 8.084   4.393   5.142   1.00 26.13 ? 10   LYS B CG  1 
ATOM   2377 C  CD  . LYS B 2 10  ? 9.528   4.806   4.890   1.00 26.05 ? 10   LYS B CD  1 
ATOM   2378 C  CE  . LYS B 2 10  ? 9.840   4.897   3.394   1.00 27.82 ? 10   LYS B CE  1 
ATOM   2379 N  NZ  . LYS B 2 10  ? 8.899   5.828   2.682   1.00 31.31 ? 10   LYS B NZ  1 
ATOM   2380 N  N   . LEU B 2 11  ? 6.264   1.491   6.247   1.00 19.82 ? 11   LEU B N   1 
ATOM   2381 C  CA  . LEU B 2 11  ? 5.854   0.370   5.411   1.00 17.93 ? 11   LEU B CA  1 
ATOM   2382 C  C   . LEU B 2 11  ? 4.340   0.257   5.367   1.00 19.32 ? 11   LEU B C   1 
ATOM   2383 O  O   . LEU B 2 11  ? 3.751   0.106   4.292   1.00 21.83 ? 11   LEU B O   1 
ATOM   2384 C  CB  . LEU B 2 11  ? 6.479   -0.909  5.951   1.00 23.15 ? 11   LEU B CB  1 
ATOM   2385 C  CG  . LEU B 2 11  ? 6.324   -2.189  5.146   1.00 20.15 ? 11   LEU B CG  1 
ATOM   2386 C  CD1 . LEU B 2 11  ? 7.125   -2.068  3.851   1.00 22.33 ? 11   LEU B CD1 1 
ATOM   2387 C  CD2 . LEU B 2 11  ? 6.791   -3.356  5.993   1.00 17.62 ? 11   LEU B CD2 1 
ATOM   2388 N  N   . MET B 2 12  ? 3.688   0.362   6.527   1.00 17.45 ? 12   MET B N   1 
ATOM   2389 C  CA  . MET B 2 12  ? 2.230   0.364   6.555   1.00 16.87 ? 12   MET B CA  1 
ATOM   2390 C  C   . MET B 2 12  ? 1.675   1.595   5.845   1.00 19.58 ? 12   MET B C   1 
ATOM   2391 O  O   . MET B 2 12  ? 0.812   1.477   4.967   1.00 16.60 ? 12   MET B O   1 
ATOM   2392 C  CB  . MET B 2 12  ? 1.730   0.303   8.000   1.00 23.37 ? 12   MET B CB  1 
ATOM   2393 C  CG  . MET B 2 12  ? 2.177   -0.924  8.768   1.00 20.42 ? 12   MET B CG  1 
ATOM   2394 S  SD  . MET B 2 12  ? 1.988   -0.699  10.548  1.00 26.15 ? 12   MET B SD  1 
ATOM   2395 C  CE  . MET B 2 12  ? 0.213   -0.522  10.690  1.00 18.67 ? 12   MET B CE  1 
ATOM   2396 N  N   . SER B 2 13  ? 2.191   2.783   6.183   1.00 18.95 ? 13   SER B N   1 
ATOM   2397 C  CA  . SER B 2 13  ? 1.671   4.012   5.590   1.00 19.14 ? 13   SER B CA  1 
ATOM   2398 C  C   . SER B 2 13  ? 1.851   4.020   4.073   1.00 20.46 ? 13   SER B C   1 
ATOM   2399 O  O   . SER B 2 13  ? 0.984   4.517   3.344   1.00 23.10 ? 13   SER B O   1 
ATOM   2400 C  CB  . SER B 2 13  ? 2.351   5.228   6.221   1.00 19.17 ? 13   SER B CB  1 
ATOM   2401 O  OG  . SER B 2 13  ? 2.054   6.405   5.495   1.00 26.72 ? 13   SER B OG  1 
ATOM   2402 N  N   . ASP B 2 14  ? 2.963   3.466   3.575   1.00 18.65 ? 14   ASP B N   1 
ATOM   2403 C  CA  . ASP B 2 14  ? 3.178   3.391   2.132   1.00 22.40 ? 14   ASP B CA  1 
ATOM   2404 C  C   . ASP B 2 14  ? 2.240   2.407   1.444   1.00 26.29 ? 14   ASP B C   1 
ATOM   2405 O  O   . ASP B 2 14  ? 2.149   2.408   0.206   1.00 22.31 ? 14   ASP B O   1 
ATOM   2406 C  CB  . ASP B 2 14  ? 4.627   3.018   1.829   1.00 20.67 ? 14   ASP B CB  1 
ATOM   2407 C  CG  . ASP B 2 14  ? 5.571   4.182   2.043   1.00 23.04 ? 14   ASP B CG  1 
ATOM   2408 O  OD1 . ASP B 2 14  ? 5.082   5.318   2.217   1.00 24.26 ? 14   ASP B OD1 1 
ATOM   2409 O  OD2 . ASP B 2 14  ? 6.795   3.970   2.040   1.00 25.07 ? 14   ASP B OD2 1 
ATOM   2410 N  N   . ASN B 2 15  ? 1.539   1.577   2.206   1.00 19.28 ? 15   ASN B N   1 
ATOM   2411 C  CA  . ASN B 2 15  ? 0.600   0.630   1.639   1.00 18.67 ? 15   ASN B CA  1 
ATOM   2412 C  C   . ASN B 2 15  ? -0.835  0.965   2.025   1.00 21.08 ? 15   ASN B C   1 
ATOM   2413 O  O   . ASN B 2 15  ? -1.697  0.087   2.086   1.00 19.66 ? 15   ASN B O   1 
ATOM   2414 C  CB  . ASN B 2 15  ? 1.006   -0.787  2.040   1.00 19.25 ? 15   ASN B CB  1 
ATOM   2415 C  CG  . ASN B 2 15  ? 2.162   -1.300  1.190   1.00 20.40 ? 15   ASN B CG  1 
ATOM   2416 O  OD1 . ASN B 2 15  ? 1.947   -1.945  0.163   1.00 24.42 ? 15   ASN B OD1 1 
ATOM   2417 N  ND2 . ASN B 2 15  ? 3.396   -0.983  1.594   1.00 21.27 ? 15   ASN B ND2 1 
ATOM   2418 N  N   . GLY B 2 16  ? -1.105  2.250   2.264   1.00 23.26 ? 16   GLY B N   1 
ATOM   2419 C  CA  . GLY B 2 16  ? -2.451  2.734   2.469   1.00 21.13 ? 16   GLY B CA  1 
ATOM   2420 C  C   . GLY B 2 16  ? -3.006  2.518   3.854   1.00 22.90 ? 16   GLY B C   1 
ATOM   2421 O  O   . GLY B 2 16  ? -4.182  2.843   4.089   1.00 20.33 ? 16   GLY B O   1 
ATOM   2422 N  N   . VAL B 2 17  ? -2.217  1.956   4.775   1.00 19.96 ? 17   VAL B N   1 
ATOM   2423 C  CA  . VAL B 2 17  ? -2.658  1.800   6.156   1.00 20.02 ? 17   VAL B CA  1 
ATOM   2424 C  C   . VAL B 2 17  ? -2.504  3.130   6.877   1.00 25.32 ? 17   VAL B C   1 
ATOM   2425 O  O   . VAL B 2 17  ? -1.505  3.832   6.698   1.00 27.50 ? 17   VAL B O   1 
ATOM   2426 C  CB  . VAL B 2 17  ? -1.862  0.693   6.870   1.00 21.70 ? 17   VAL B CB  1 
ATOM   2427 C  CG1 . VAL B 2 17  ? -2.340  0.581   8.315   1.00 18.58 ? 17   VAL B CG1 1 
ATOM   2428 C  CG2 . VAL B 2 17  ? -2.013  -0.634  6.141   1.00 20.12 ? 17   VAL B CG2 1 
ATOM   2429 N  N   . ARG B 2 18  ? -3.488  3.481   7.707   1.00 25.02 ? 18   ARG B N   1 
ATOM   2430 C  CA  . ARG B 2 18  ? -3.513  4.785   8.367   1.00 22.28 ? 18   ARG B CA  1 
ATOM   2431 C  C   . ARG B 2 18  ? -2.747  4.712   9.683   1.00 21.56 ? 18   ARG B C   1 
ATOM   2432 O  O   . ARG B 2 18  ? -3.153  4.001   10.614  1.00 23.86 ? 18   ARG B O   1 
ATOM   2433 C  CB  . ARG B 2 18  ? -4.949  5.251   8.598   1.00 23.67 ? 18   ARG B CB  1 
ATOM   2434 C  CG  . ARG B 2 18  ? -5.040  6.617   9.243   1.00 28.17 ? 18   ARG B CG  1 
ATOM   2435 C  CD  . ARG B 2 18  ? -6.354  7.309   8.889   1.00 37.32 ? 18   ARG B CD  1 
ATOM   2436 N  N   . VAL B 2 19  ? -1.640  5.450   9.755   1.00 18.84 ? 19   VAL B N   1 
ATOM   2437 C  CA  . VAL B 2 19  ? -0.856  5.620   10.969  1.00 15.98 ? 19   VAL B CA  1 
ATOM   2438 C  C   . VAL B 2 19  ? -0.816  7.110   11.309  1.00 19.81 ? 19   VAL B C   1 
ATOM   2439 O  O   . VAL B 2 19  ? -1.137  7.966   10.489  1.00 20.53 ? 19   VAL B O   1 
ATOM   2440 C  CB  . VAL B 2 19  ? 0.574   5.069   10.813  1.00 23.32 ? 19   VAL B CB  1 
ATOM   2441 C  CG1 . VAL B 2 19  ? 0.548   3.603   10.454  1.00 19.08 ? 19   VAL B CG1 1 
ATOM   2442 C  CG2 . VAL B 2 19  ? 1.318   5.869   9.737   1.00 18.67 ? 19   VAL B CG2 1 
ATOM   2443 N  N   . GLN B 2 20  ? -0.387  7.420   12.526  1.00 25.77 ? 20   GLN B N   1 
ATOM   2444 C  CA  . GLN B 2 20  ? -0.196  8.822   12.853  1.00 24.90 ? 20   GLN B CA  1 
ATOM   2445 C  C   . GLN B 2 20  ? 0.968   9.395   12.046  1.00 28.17 ? 20   GLN B C   1 
ATOM   2446 O  O   . GLN B 2 20  ? 2.012   8.758   11.880  1.00 25.46 ? 20   GLN B O   1 
ATOM   2447 C  CB  . GLN B 2 20  ? 0.017   9.017   14.356  1.00 23.80 ? 20   GLN B CB  1 
ATOM   2448 C  CG  . GLN B 2 20  ? 1.038   8.168   15.045  1.00 33.71 ? 20   GLN B CG  1 
ATOM   2449 C  CD  . GLN B 2 20  ? 0.551   7.771   16.442  1.00 34.70 ? 20   GLN B CD  1 
ATOM   2450 O  OE1 . GLN B 2 20  ? 0.260   6.596   16.707  1.00 29.73 ? 20   GLN B OE1 1 
ATOM   2451 N  NE2 . GLN B 2 20  ? 0.429   8.757   17.330  1.00 30.69 ? 20   GLN B NE2 1 
ATOM   2452 N  N   . ARG B 2 21  ? 0.757   10.591  11.501  1.00 22.95 ? 21   ARG B N   1 
ATOM   2453 C  CA  . ARG B 2 21  ? 1.779   11.257  10.698  1.00 26.33 ? 21   ARG B CA  1 
ATOM   2454 C  C   . ARG B 2 21  ? 3.028   11.506  11.544  1.00 23.64 ? 21   ARG B C   1 
ATOM   2455 O  O   . ARG B 2 21  ? 2.932   11.848  12.726  1.00 22.19 ? 21   ARG B O   1 
ATOM   2456 C  CB  . ARG B 2 21  ? 1.205   12.570  10.143  1.00 26.91 ? 21   ARG B CB  1 
ATOM   2457 C  CG  . ARG B 2 21  ? 2.129   13.359  9.226   1.00 33.36 ? 21   ARG B CG  1 
ATOM   2458 C  CD  . ARG B 2 21  ? 1.357   14.448  8.468   1.00 38.81 ? 21   ARG B CD  1 
ATOM   2459 N  NE  . ARG B 2 21  ? 2.229   15.530  7.999   1.00 36.64 ? 21   ARG B NE  1 
ATOM   2460 C  CZ  . ARG B 2 21  ? 2.408   16.678  8.651   1.00 38.18 ? 21   ARG B CZ  1 
ATOM   2461 N  NH1 . ARG B 2 21  ? 1.778   16.892  9.802   1.00 30.86 ? 21   ARG B NH1 1 
ATOM   2462 N  NH2 . ARG B 2 21  ? 3.217   17.611  8.159   1.00 35.39 ? 21   ARG B NH2 1 
ATOM   2463 N  N   . PHE B 2 22  ? 4.209   11.295  10.961  1.00 22.54 ? 22   PHE B N   1 
ATOM   2464 C  CA  . PHE B 2 22  ? 5.422   11.384  11.771  1.00 22.41 ? 22   PHE B CA  1 
ATOM   2465 C  C   . PHE B 2 22  ? 6.629   11.745  10.919  1.00 23.38 ? 22   PHE B C   1 
ATOM   2466 O  O   . PHE B 2 22  ? 6.623   11.605  9.694   1.00 23.68 ? 22   PHE B O   1 
ATOM   2467 C  CB  . PHE B 2 22  ? 5.713   10.069  12.531  1.00 23.49 ? 22   PHE B CB  1 
ATOM   2468 C  CG  . PHE B 2 22  ? 6.201   8.941   11.653  1.00 22.81 ? 22   PHE B CG  1 
ATOM   2469 C  CD1 . PHE B 2 22  ? 7.558   8.802   11.356  1.00 23.53 ? 22   PHE B CD1 1 
ATOM   2470 C  CD2 . PHE B 2 22  ? 5.310   8.015   11.133  1.00 25.57 ? 22   PHE B CD2 1 
ATOM   2471 C  CE1 . PHE B 2 22  ? 8.012   7.771   10.540  1.00 21.07 ? 22   PHE B CE1 1 
ATOM   2472 C  CE2 . PHE B 2 22  ? 5.763   6.976   10.325  1.00 21.51 ? 22   PHE B CE2 1 
ATOM   2473 C  CZ  . PHE B 2 22  ? 7.111   6.865   10.024  1.00 19.94 ? 22   PHE B CZ  1 
ATOM   2474 N  N   . PHE B 2 23  ? 7.679   12.188  11.606  1.00 25.36 ? 23   PHE B N   1 
ATOM   2475 C  CA  . PHE B 2 23  ? 9.009   12.329  11.037  1.00 22.70 ? 23   PHE B CA  1 
ATOM   2476 C  C   . PHE B 2 23  ? 10.020  11.677  11.970  1.00 22.61 ? 23   PHE B C   1 
ATOM   2477 O  O   . PHE B 2 23  ? 9.758   11.451  13.154  1.00 22.31 ? 23   PHE B O   1 
ATOM   2478 C  CB  . PHE B 2 23  ? 9.384   13.805  10.807  1.00 27.31 ? 23   PHE B CB  1 
ATOM   2479 C  CG  . PHE B 2 23  ? 8.422   14.540  9.925   1.00 27.65 ? 23   PHE B CG  1 
ATOM   2480 C  CD1 . PHE B 2 23  ? 8.423   14.331  8.552   1.00 30.97 ? 23   PHE B CD1 1 
ATOM   2481 C  CD2 . PHE B 2 23  ? 7.516   15.435  10.467  1.00 24.74 ? 23   PHE B CD2 1 
ATOM   2482 C  CE1 . PHE B 2 23  ? 7.531   14.995  7.739   1.00 35.82 ? 23   PHE B CE1 1 
ATOM   2483 C  CE2 . PHE B 2 23  ? 6.628   16.107  9.666   1.00 29.59 ? 23   PHE B CE2 1 
ATOM   2484 C  CZ  . PHE B 2 23  ? 6.627   15.890  8.297   1.00 34.80 ? 23   PHE B CZ  1 
ATOM   2485 N  N   . VAL B 2 24  ? 11.188  11.374  11.419  1.00 24.83 ? 24   VAL B N   1 
ATOM   2486 C  CA  . VAL B 2 24  ? 12.260  10.705  12.142  1.00 22.70 ? 24   VAL B CA  1 
ATOM   2487 C  C   . VAL B 2 24  ? 13.413  11.686  12.273  1.00 25.53 ? 24   VAL B C   1 
ATOM   2488 O  O   . VAL B 2 24  ? 13.768  12.359  11.301  1.00 22.85 ? 24   VAL B O   1 
ATOM   2489 C  CB  . VAL B 2 24  ? 12.706  9.426   11.413  1.00 26.95 ? 24   VAL B CB  1 
ATOM   2490 C  CG1 . VAL B 2 24  ? 13.648  8.617   12.282  1.00 27.41 ? 24   VAL B CG1 1 
ATOM   2491 C  CG2 . VAL B 2 24  ? 11.489  8.609   10.990  1.00 25.93 ? 24   VAL B CG2 1 
ATOM   2492 N  N   . ALA B 2 25  ? 13.999  11.767  13.465  1.00 25.27 ? 25   ALA B N   1 
ATOM   2493 C  CA  . ALA B 2 25  ? 15.045  12.744  13.748  1.00 27.32 ? 25   ALA B CA  1 
ATOM   2494 C  C   . ALA B 2 25  ? 16.300  12.049  14.249  1.00 29.46 ? 25   ALA B C   1 
ATOM   2495 O  O   . ALA B 2 25  ? 16.225  11.137  15.081  1.00 27.48 ? 25   ALA B O   1 
ATOM   2496 C  CB  . ALA B 2 25  ? 14.582  13.762  14.785  1.00 24.43 ? 25   ALA B CB  1 
ATOM   2497 N  N   . ASP B 2 26  ? 17.448  12.489  13.725  1.00 31.88 ? 26   ASP B N   1 
ATOM   2498 C  CA  . ASP B 2 26  ? 18.766  12.073  14.190  1.00 32.43 ? 26   ASP B CA  1 
ATOM   2499 C  C   . ASP B 2 26  ? 19.381  13.027  15.206  1.00 33.31 ? 26   ASP B C   1 
ATOM   2500 O  O   . ASP B 2 26  ? 20.305  12.630  15.925  1.00 31.70 ? 26   ASP B O   1 
ATOM   2501 C  CB  . ASP B 2 26  ? 19.736  11.950  13.008  1.00 36.48 ? 26   ASP B CB  1 
ATOM   2502 C  CG  . ASP B 2 26  ? 19.388  10.809  12.089  1.00 44.29 ? 26   ASP B CG  1 
ATOM   2503 O  OD1 . ASP B 2 26  ? 18.740  9.846   12.555  1.00 47.04 ? 26   ASP B OD1 1 
ATOM   2504 O  OD2 . ASP B 2 26  ? 19.767  10.870  10.902  1.00 44.21 ? 26   ASP B OD2 1 
ATOM   2505 N  N   . THR B 2 27  ? 18.934  14.276  15.257  1.00 32.13 ? 27   THR B N   1 
ATOM   2506 C  CA  . THR B 2 27  ? 19.481  15.253  16.188  1.00 37.33 ? 27   THR B CA  1 
ATOM   2507 C  C   . THR B 2 27  ? 18.344  16.002  16.870  1.00 34.47 ? 27   THR B C   1 
ATOM   2508 O  O   . THR B 2 27  ? 17.210  16.029  16.384  1.00 33.18 ? 27   THR B O   1 
ATOM   2509 C  CB  . THR B 2 27  ? 20.415  16.261  15.490  1.00 31.95 ? 27   THR B CB  1 
ATOM   2510 O  OG1 . THR B 2 27  ? 19.634  17.270  14.851  1.00 34.17 ? 27   THR B OG1 1 
ATOM   2511 C  CG2 . THR B 2 27  ? 21.267  15.579  14.445  1.00 31.90 ? 27   THR B CG2 1 
ATOM   2512 N  N   . ALA B 2 28  ? 18.664  16.614  18.011  1.00 32.82 ? 28   ALA B N   1 
ATOM   2513 C  CA  . ALA B 2 28  ? 17.681  17.431  18.712  1.00 34.03 ? 28   ALA B CA  1 
ATOM   2514 C  C   . ALA B 2 28  ? 17.149  18.545  17.820  1.00 31.80 ? 28   ALA B C   1 
ATOM   2515 O  O   . ALA B 2 28  ? 15.963  18.893  17.887  1.00 34.76 ? 28   ALA B O   1 
ATOM   2516 C  CB  . ALA B 2 28  ? 18.303  18.012  19.981  1.00 35.56 ? 28   ALA B CB  1 
ATOM   2517 N  N   . ASN B 2 29  ? 18.012  19.109  16.971  1.00 30.12 ? 29   ASN B N   1 
ATOM   2518 C  CA  . ASN B 2 29  ? 17.595  20.177  16.069  1.00 35.56 ? 29   ASN B CA  1 
ATOM   2519 C  C   . ASN B 2 29  ? 16.619  19.661  15.016  1.00 31.59 ? 29   ASN B C   1 
ATOM   2520 O  O   . ASN B 2 29  ? 15.642  20.340  14.684  1.00 31.24 ? 29   ASN B O   1 
ATOM   2521 C  CB  . ASN B 2 29  ? 18.829  20.807  15.415  1.00 36.75 ? 29   ASN B CB  1 
ATOM   2522 C  CG  . ASN B 2 29  ? 18.693  22.302  15.220  1.00 42.20 ? 29   ASN B CG  1 
ATOM   2523 O  OD1 . ASN B 2 29  ? 17.618  22.806  14.885  1.00 46.11 ? 29   ASN B OD1 1 
ATOM   2524 N  ND2 . ASN B 2 29  ? 19.788  23.026  15.432  1.00 46.27 ? 29   ASN B ND2 1 
ATOM   2525 N  N   . GLU B 2 30  ? 16.870  18.466  14.473  1.00 35.43 ? 30   GLU B N   1 
ATOM   2526 C  CA  . GLU B 2 30  ? 15.921  17.856  13.544  1.00 33.77 ? 30   GLU B CA  1 
ATOM   2527 C  C   . GLU B 2 30  ? 14.586  17.580  14.223  1.00 32.28 ? 30   GLU B C   1 
ATOM   2528 O  O   . GLU B 2 30  ? 13.518  17.818  13.639  1.00 32.73 ? 30   GLU B O   1 
ATOM   2529 C  CB  . GLU B 2 30  ? 16.503  16.563  12.958  1.00 29.58 ? 30   GLU B CB  1 
ATOM   2530 C  CG  . GLU B 2 30  ? 17.387  16.791  11.739  1.00 32.82 ? 30   GLU B CG  1 
ATOM   2531 C  CD  . GLU B 2 30  ? 17.862  15.498  11.075  1.00 42.51 ? 30   GLU B CD  1 
ATOM   2532 O  OE1 . GLU B 2 30  ? 17.894  14.429  11.734  1.00 37.05 ? 30   GLU B OE1 1 
ATOM   2533 O  OE2 . GLU B 2 30  ? 18.208  15.558  9.876   1.00 49.98 ? 30   GLU B OE2 1 
ATOM   2534 N  N   . ALA B 2 31  ? 14.625  17.072  15.457  1.00 30.52 ? 31   ALA B N   1 
ATOM   2535 C  CA  . ALA B 2 31  ? 13.391  16.846  16.207  1.00 27.98 ? 31   ALA B CA  1 
ATOM   2536 C  C   . ALA B 2 31  ? 12.626  18.151  16.399  1.00 29.76 ? 31   ALA B C   1 
ATOM   2537 O  O   . ALA B 2 31  ? 11.404  18.204  16.206  1.00 24.56 ? 31   ALA B O   1 
ATOM   2538 C  CB  . ALA B 2 31  ? 13.720  16.204  17.555  1.00 23.94 ? 31   ALA B CB  1 
ATOM   2539 N  N   . LEU B 2 32  ? 13.340  19.218  16.762  1.00 31.92 ? 32   LEU B N   1 
ATOM   2540 C  CA  . LEU B 2 32  ? 12.744  20.547  16.805  1.00 30.47 ? 32   LEU B CA  1 
ATOM   2541 C  C   . LEU B 2 32  ? 12.035  20.863  15.493  1.00 30.68 ? 32   LEU B C   1 
ATOM   2542 O  O   . LEU B 2 32  ? 10.837  21.165  15.478  1.00 30.29 ? 32   LEU B O   1 
ATOM   2543 C  CB  . LEU B 2 32  ? 13.825  21.592  17.110  1.00 33.85 ? 32   LEU B CB  1 
ATOM   2544 C  CG  . LEU B 2 32  ? 13.432  23.077  17.088  1.00 33.04 ? 32   LEU B CG  1 
ATOM   2545 C  CD1 . LEU B 2 32  ? 12.319  23.351  18.080  1.00 30.09 ? 32   LEU B CD1 1 
ATOM   2546 C  CD2 . LEU B 2 32  ? 14.640  23.953  17.393  1.00 32.78 ? 32   LEU B CD2 1 
ATOM   2547 N  N   . GLU B 2 33  ? 12.759  20.754  14.374  1.00 31.14 ? 33   GLU B N   1 
ATOM   2548 C  CA  . GLU B 2 33  ? 12.194  21.107  13.071  1.00 29.59 ? 33   GLU B CA  1 
ATOM   2549 C  C   . GLU B 2 33  ? 11.019  20.209  12.703  1.00 34.02 ? 33   GLU B C   1 
ATOM   2550 O  O   . GLU B 2 33  ? 9.971   20.694  12.260  1.00 30.37 ? 33   GLU B O   1 
ATOM   2551 C  CB  . GLU B 2 33  ? 13.275  21.042  11.986  1.00 34.37 ? 33   GLU B CB  1 
ATOM   2552 C  CG  . GLU B 2 33  ? 14.003  22.358  11.749  1.00 37.24 ? 33   GLU B CG  1 
ATOM   2553 C  CD  . GLU B 2 33  ? 13.164  23.369  10.980  1.00 51.11 ? 33   GLU B CD  1 
ATOM   2554 O  OE1 . GLU B 2 33  ? 12.713  23.047  9.859   1.00 56.13 ? 33   GLU B OE1 1 
ATOM   2555 O  OE2 . GLU B 2 33  ? 12.953  24.487  11.496  1.00 53.09 ? 33   GLU B OE2 1 
ATOM   2556 N  N   . ALA B 2 34  ? 11.183  18.888  12.855  1.00 27.47 ? 34   ALA B N   1 
ATOM   2557 C  CA  . ALA B 2 34  ? 10.078  17.978  12.586  1.00 26.11 ? 34   ALA B CA  1 
ATOM   2558 C  C   . ALA B 2 34  ? 8.834   18.386  13.363  1.00 25.35 ? 34   ALA B C   1 
ATOM   2559 O  O   . ALA B 2 34  ? 7.723   18.390  12.817  1.00 26.98 ? 34   ALA B O   1 
ATOM   2560 C  CB  . ALA B 2 34  ? 10.483  16.543  12.933  1.00 24.38 ? 34   ALA B CB  1 
ATOM   2561 N  N   . ALA B 2 35  ? 9.006   18.750  14.636  1.00 23.84 ? 35   ALA B N   1 
ATOM   2562 C  CA  . ALA B 2 35  ? 7.863   19.112  15.471  1.00 23.22 ? 35   ALA B CA  1 
ATOM   2563 C  C   . ALA B 2 35  ? 7.137   20.328  14.912  1.00 29.33 ? 35   ALA B C   1 
ATOM   2564 O  O   . ALA B 2 35  ? 5.900   20.353  14.857  1.00 26.48 ? 35   ALA B O   1 
ATOM   2565 C  CB  . ALA B 2 35  ? 8.320   19.372  16.905  1.00 25.04 ? 35   ALA B CB  1 
ATOM   2566 N  N   . LYS B 2 36  ? 7.891   21.347  14.492  1.00 30.85 ? 36   LYS B N   1 
ATOM   2567 C  CA  . LYS B 2 36  ? 7.276   22.497  13.834  1.00 34.95 ? 36   LYS B CA  1 
ATOM   2568 C  C   . LYS B 2 36  ? 6.596   22.083  12.538  1.00 29.16 ? 36   LYS B C   1 
ATOM   2569 O  O   . LYS B 2 36  ? 5.493   22.549  12.232  1.00 29.04 ? 36   LYS B O   1 
ATOM   2570 C  CB  . LYS B 2 36  ? 8.324   23.581  13.567  1.00 32.72 ? 36   LYS B CB  1 
ATOM   2571 C  CG  . LYS B 2 36  ? 8.744   24.352  14.810  1.00 36.88 ? 36   LYS B CG  1 
ATOM   2572 C  CD  . LYS B 2 36  ? 9.718   25.471  14.461  1.00 46.19 ? 36   LYS B CD  1 
ATOM   2573 C  CE  . LYS B 2 36  ? 11.022  24.912  13.921  1.00 41.41 ? 36   LYS B CE  1 
ATOM   2574 N  NZ  . LYS B 2 36  ? 12.062  25.971  13.694  1.00 46.44 ? 36   LYS B NZ  1 
ATOM   2575 N  N   . ARG B 2 37  ? 7.225   21.175  11.784  1.00 29.74 ? 37   ARG B N   1 
ATOM   2576 C  CA  . ARG B 2 37  ? 6.690   20.762  10.488  1.00 30.06 ? 37   ARG B CA  1 
ATOM   2577 C  C   . ARG B 2 37  ? 5.341   20.060  10.615  1.00 26.90 ? 37   ARG B C   1 
ATOM   2578 O  O   . ARG B 2 37  ? 4.512   20.149  9.704   1.00 31.56 ? 37   ARG B O   1 
ATOM   2579 C  CB  . ARG B 2 37  ? 7.706   19.856  9.778   1.00 32.59 ? 37   ARG B CB  1 
ATOM   2580 C  CG  . ARG B 2 37  ? 7.271   19.357  8.391   1.00 36.31 ? 37   ARG B CG  1 
ATOM   2581 C  CD  . ARG B 2 37  ? 8.432   19.237  7.407   1.00 32.01 ? 37   ARG B CD  1 
ATOM   2582 N  NE  . ARG B 2 37  ? 9.548   18.451  7.923   1.00 42.83 ? 37   ARG B NE  1 
ATOM   2583 C  CZ  . ARG B 2 37  ? 10.692  18.963  8.379   1.00 46.37 ? 37   ARG B CZ  1 
ATOM   2584 N  NH1 . ARG B 2 37  ? 10.886  20.280  8.384   1.00 44.15 ? 37   ARG B NH1 1 
ATOM   2585 N  NH2 . ARG B 2 37  ? 11.647  18.154  8.828   1.00 37.26 ? 37   ARG B NH2 1 
ATOM   2586 N  N   . LEU B 2 38  ? 5.098   19.368  11.732  1.00 29.13 ? 38   LEU B N   1 
ATOM   2587 C  CA  . LEU B 2 38  ? 3.865   18.598  11.888  1.00 23.81 ? 38   LEU B CA  1 
ATOM   2588 C  C   . LEU B 2 38  ? 2.632   19.492  11.899  1.00 25.85 ? 38   LEU B C   1 
ATOM   2589 O  O   . LEU B 2 38  ? 1.573   19.097  11.391  1.00 22.73 ? 38   LEU B O   1 
ATOM   2590 C  CB  . LEU B 2 38  ? 3.902   17.785  13.177  1.00 25.05 ? 38   LEU B CB  1 
ATOM   2591 C  CG  . LEU B 2 38  ? 4.660   16.465  13.154  1.00 26.28 ? 38   LEU B CG  1 
ATOM   2592 C  CD1 . LEU B 2 38  ? 4.735   15.924  14.576  1.00 22.67 ? 38   LEU B CD1 1 
ATOM   2593 C  CD2 . LEU B 2 38  ? 3.942   15.502  12.233  1.00 25.50 ? 38   LEU B CD2 1 
ATOM   2594 N  N   . ASN B 2 39  ? 2.740   20.683  12.499  1.00 22.41 ? 39   ASN B N   1 
ATOM   2595 C  CA  . ASN B 2 39  ? 1.582   21.553  12.705  1.00 23.98 ? 39   ASN B CA  1 
ATOM   2596 C  C   . ASN B 2 39  ? 0.455   20.782  13.387  1.00 25.24 ? 39   ASN B C   1 
ATOM   2597 O  O   . ASN B 2 39  ? -0.713  20.863  12.997  1.00 27.45 ? 39   ASN B O   1 
ATOM   2598 C  CB  . ASN B 2 39  ? 1.105   22.157  11.379  1.00 23.08 ? 39   ASN B CB  1 
ATOM   2599 C  CG  . ASN B 2 39  ? 1.937   23.344  10.949  1.00 23.39 ? 39   ASN B CG  1 
ATOM   2600 O  OD1 . ASN B 2 39  ? 2.461   23.381  9.842   1.00 28.43 ? 39   ASN B OD1 1 
ATOM   2601 N  ND2 . ASN B 2 39  ? 2.071   24.319  11.833  1.00 19.50 ? 39   ASN B ND2 1 
ATOM   2602 N  N   . ALA B 2 40  ? 0.822   19.977  14.378  1.00 23.90 ? 40   ALA B N   1 
ATOM   2603 C  CA  . ALA B 2 40  ? -0.142  19.176  15.116  1.00 29.30 ? 40   ALA B CA  1 
ATOM   2604 C  C   . ALA B 2 40  ? -0.598  19.925  16.359  1.00 24.81 ? 40   ALA B C   1 
ATOM   2605 O  O   . ALA B 2 40  ? 0.134   20.745  16.908  1.00 23.73 ? 40   ALA B O   1 
ATOM   2606 C  CB  . ALA B 2 40  ? 0.467   17.831  15.511  1.00 23.10 ? 40   ALA B CB  1 
ATOM   2607 N  N   . LYS B 2 41  ? -1.821  19.642  16.803  1.00 24.55 ? 41   LYS B N   1 
ATOM   2608 C  CA  . LYS B 2 41  ? -2.248  20.192  18.085  1.00 27.99 ? 41   LYS B CA  1 
ATOM   2609 C  C   . LYS B 2 41  ? -1.353  19.679  19.211  1.00 27.91 ? 41   LYS B C   1 
ATOM   2610 O  O   . LYS B 2 41  ? -0.832  20.461  20.009  1.00 21.61 ? 41   LYS B O   1 
ATOM   2611 C  CB  . LYS B 2 41  ? -3.711  19.855  18.358  1.00 27.09 ? 41   LYS B CB  1 
ATOM   2612 C  CG  . LYS B 2 41  ? -4.180  20.421  19.691  1.00 25.01 ? 41   LYS B CG  1 
ATOM   2613 C  CD  . LYS B 2 41  ? -5.576  19.958  20.058  1.00 30.40 ? 41   LYS B CD  1 
ATOM   2614 C  CE  . LYS B 2 41  ? -5.989  20.535  21.408  1.00 31.08 ? 41   LYS B CE  1 
ATOM   2615 N  NZ  . LYS B 2 41  ? -7.453  20.405  21.610  1.00 34.75 ? 41   LYS B NZ  1 
ATOM   2616 N  N   . GLU B 2 42  ? -1.123  18.364  19.259  1.00 24.80 ? 42   GLU B N   1 
ATOM   2617 C  CA  . GLU B 2 42  ? -0.213  17.766  20.227  1.00 23.20 ? 42   GLU B CA  1 
ATOM   2618 C  C   . GLU B 2 42  ? 0.781   16.850  19.523  1.00 26.11 ? 42   GLU B C   1 
ATOM   2619 O  O   . GLU B 2 42  ? 0.473   16.229  18.502  1.00 21.89 ? 42   GLU B O   1 
ATOM   2620 C  CB  . GLU B 2 42  ? -0.979  16.977  21.314  1.00 30.75 ? 42   GLU B CB  1 
ATOM   2621 C  CG  . GLU B 2 42  ? -0.077  16.455  22.437  1.00 30.67 ? 42   GLU B CG  1 
ATOM   2622 C  CD  . GLU B 2 42  ? -0.816  16.209  23.726  1.00 38.74 ? 42   GLU B CD  1 
ATOM   2623 O  OE1 . GLU B 2 42  ? -1.964  15.697  23.676  1.00 44.28 ? 42   GLU B OE1 1 
ATOM   2624 O  OE2 . GLU B 2 42  ? -0.244  16.535  24.794  1.00 43.47 ? 42   GLU B OE2 1 
ATOM   2625 N  N   . ILE B 2 43  ? 1.977   16.764  20.097  1.00 26.42 ? 43   ILE B N   1 
ATOM   2626 C  CA  . ILE B 2 43  ? 3.094   16.023  19.535  1.00 23.33 ? 43   ILE B CA  1 
ATOM   2627 C  C   . ILE B 2 43  ? 3.488   14.924  20.509  1.00 25.03 ? 43   ILE B C   1 
ATOM   2628 O  O   . ILE B 2 43  ? 3.534   15.151  21.722  1.00 24.32 ? 43   ILE B O   1 
ATOM   2629 C  CB  . ILE B 2 43  ? 4.290   16.954  19.274  1.00 25.43 ? 43   ILE B CB  1 
ATOM   2630 C  CG1 . ILE B 2 43  ? 3.862   18.133  18.402  1.00 20.89 ? 43   ILE B CG1 1 
ATOM   2631 C  CG2 . ILE B 2 43  ? 5.456   16.187  18.663  1.00 24.77 ? 43   ILE B CG2 1 
ATOM   2632 C  CD1 . ILE B 2 43  ? 4.904   19.230  18.343  1.00 25.18 ? 43   ILE B CD1 1 
ATOM   2633 N  N   . VAL B 2 44  ? 3.773   13.733  19.987  1.00 29.98 ? 44   VAL B N   1 
ATOM   2634 C  CA  . VAL B 2 44  ? 4.321   12.651  20.797  1.00 24.70 ? 44   VAL B CA  1 
ATOM   2635 C  C   . VAL B 2 44  ? 5.711   12.325  20.271  1.00 21.66 ? 44   VAL B C   1 
ATOM   2636 O  O   . VAL B 2 44  ? 5.891   12.076  19.070  1.00 23.60 ? 44   VAL B O   1 
ATOM   2637 C  CB  . VAL B 2 44  ? 3.400   11.416  20.822  1.00 26.43 ? 44   VAL B CB  1 
ATOM   2638 C  CG1 . VAL B 2 44  ? 3.074   10.918  19.416  1.00 30.06 ? 44   VAL B CG1 1 
ATOM   2639 C  CG2 . VAL B 2 44  ? 4.014   10.305  21.687  1.00 25.84 ? 44   VAL B CG2 1 
ATOM   2640 N  N   . LEU B 2 45  ? 6.694   12.367  21.168  1.00 22.10 ? 45   LEU B N   1 
ATOM   2641 C  CA  . LEU B 2 45  ? 8.091   12.088  20.856  1.00 23.37 ? 45   LEU B CA  1 
ATOM   2642 C  C   . LEU B 2 45  ? 8.415   10.691  21.371  1.00 27.05 ? 45   LEU B C   1 
ATOM   2643 O  O   . LEU B 2 45  ? 8.080   10.360  22.509  1.00 22.04 ? 45   LEU B O   1 
ATOM   2644 C  CB  . LEU B 2 45  ? 9.006   13.130  21.505  1.00 25.41 ? 45   LEU B CB  1 
ATOM   2645 C  CG  . LEU B 2 45  ? 10.507  12.875  21.683  1.00 27.78 ? 45   LEU B CG  1 
ATOM   2646 C  CD1 . LEU B 2 45  ? 11.254  13.022  20.361  1.00 20.98 ? 45   LEU B CD1 1 
ATOM   2647 C  CD2 . LEU B 2 45  ? 11.084  13.818  22.744  1.00 24.77 ? 45   LEU B CD2 1 
ATOM   2648 N  N   . LYS B 2 46  ? 9.025   9.859   20.525  1.00 22.58 ? 46   LYS B N   1 
ATOM   2649 C  CA  . LYS B 2 46  ? 9.173   8.444   20.850  1.00 23.61 ? 46   LYS B CA  1 
ATOM   2650 C  C   . LYS B 2 46  ? 10.579  7.991   20.497  1.00 20.36 ? 46   LYS B C   1 
ATOM   2651 O  O   . LYS B 2 46  ? 10.966  8.026   19.324  1.00 20.44 ? 46   LYS B O   1 
ATOM   2652 C  CB  . LYS B 2 46  ? 8.130   7.588   20.111  1.00 25.26 ? 46   LYS B CB  1 
ATOM   2653 C  CG  . LYS B 2 46  ? 6.691   8.072   20.291  1.00 22.40 ? 46   LYS B CG  1 
ATOM   2654 C  CD  . LYS B 2 46  ? 5.684   7.145   19.627  1.00 20.89 ? 46   LYS B CD  1 
ATOM   2655 C  CE  . LYS B 2 46  ? 5.553   5.839   20.389  1.00 25.60 ? 46   LYS B CE  1 
ATOM   2656 N  NZ  . LYS B 2 46  ? 4.548   4.947   19.734  1.00 26.42 ? 46   LYS B NZ  1 
ATOM   2657 N  N   . ALA B 2 47  ? 11.332  7.574   21.514  1.00 22.12 ? 47   ALA B N   1 
ATOM   2658 C  CA  . ALA B 2 47  ? 12.648  6.984   21.296  1.00 23.39 ? 47   ALA B CA  1 
ATOM   2659 C  C   . ALA B 2 47  ? 12.506  5.703   20.496  1.00 18.29 ? 47   ALA B C   1 
ATOM   2660 O  O   . ALA B 2 47  ? 11.587  4.915   20.722  1.00 19.71 ? 47   ALA B O   1 
ATOM   2661 C  CB  . ALA B 2 47  ? 13.338  6.683   22.631  1.00 24.59 ? 47   ALA B CB  1 
ATOM   2662 N  N   . GLN B 2 48  ? 13.432  5.487   19.568  1.00 21.51 ? 48   GLN B N   1 
ATOM   2663 C  CA  . GLN B 2 48  ? 13.349  4.345   18.660  1.00 20.28 ? 48   GLN B CA  1 
ATOM   2664 C  C   . GLN B 2 48  ? 14.273  3.246   19.161  1.00 24.18 ? 48   GLN B C   1 
ATOM   2665 O  O   . GLN B 2 48  ? 15.470  3.216   18.859  1.00 21.77 ? 48   GLN B O   1 
ATOM   2666 C  CB  . GLN B 2 48  ? 13.672  4.766   17.232  1.00 22.19 ? 48   GLN B CB  1 
ATOM   2667 C  CG  . GLN B 2 48  ? 12.652  5.759   16.682  1.00 19.01 ? 48   GLN B CG  1 
ATOM   2668 C  CD  . GLN B 2 48  ? 11.240  5.181   16.602  1.00 22.69 ? 48   GLN B CD  1 
ATOM   2669 O  OE1 . GLN B 2 48  ? 10.890  4.532   15.623  1.00 19.37 ? 48   GLN B OE1 1 
ATOM   2670 N  NE2 . GLN B 2 48  ? 10.417  5.447   17.615  1.00 18.35 ? 48   GLN B NE2 1 
ATOM   2671 N  N   . ILE B 2 49  ? 13.701  2.340   19.958  1.00 20.62 ? 49   ILE B N   1 
ATOM   2672 C  CA  . ILE B 2 49  ? 14.306  1.055   20.281  1.00 22.09 ? 49   ILE B CA  1 
ATOM   2673 C  C   . ILE B 2 49  ? 13.228  -0.009  20.111  1.00 25.48 ? 49   ILE B C   1 
ATOM   2674 O  O   . ILE B 2 49  ? 12.039  0.292   20.014  1.00 21.15 ? 49   ILE B O   1 
ATOM   2675 C  CB  . ILE B 2 49  ? 14.913  1.007   21.703  1.00 22.29 ? 49   ILE B CB  1 
ATOM   2676 C  CG1 . ILE B 2 49  ? 13.817  1.044   22.759  1.00 23.56 ? 49   ILE B CG1 1 
ATOM   2677 C  CG2 . ILE B 2 49  ? 15.898  2.164   21.914  1.00 22.46 ? 49   ILE B CG2 1 
ATOM   2678 C  CD1 . ILE B 2 49  ? 14.326  0.727   24.162  1.00 27.24 ? 49   ILE B CD1 1 
ATOM   2679 N  N   . LEU B 2 50  ? 13.658  -1.269  20.074  1.00 25.37 ? 50   LEU B N   1 
ATOM   2680 C  CA  . LEU B 2 50  ? 12.736  -2.363  19.796  1.00 25.89 ? 50   LEU B CA  1 
ATOM   2681 C  C   . LEU B 2 50  ? 12.033  -2.875  21.046  1.00 28.08 ? 50   LEU B C   1 
ATOM   2682 O  O   . LEU B 2 50  ? 10.885  -3.346  20.961  1.00 22.55 ? 50   LEU B O   1 
ATOM   2683 C  CB  . LEU B 2 50  ? 13.482  -3.522  19.122  1.00 24.53 ? 50   LEU B CB  1 
ATOM   2684 C  CG  . LEU B 2 50  ? 14.354  -3.134  17.928  1.00 24.06 ? 50   LEU B CG  1 
ATOM   2685 C  CD1 . LEU B 2 50  ? 15.351  -4.245  17.607  1.00 27.94 ? 50   LEU B CD1 1 
ATOM   2686 C  CD2 . LEU B 2 50  ? 13.465  -2.831  16.730  1.00 25.46 ? 50   LEU B CD2 1 
ATOM   2687 N  N   . ALA B 2 51  ? 12.697  -2.795  22.195  1.00 25.13 ? 51   ALA B N   1 
ATOM   2688 C  CA  . ALA B 2 51  ? 12.138  -3.318  23.428  1.00 23.17 ? 51   ALA B CA  1 
ATOM   2689 C  C   . ALA B 2 51  ? 10.918  -2.511  23.846  1.00 25.55 ? 51   ALA B C   1 
ATOM   2690 O  O   . ALA B 2 51  ? 10.813  -1.313  23.565  1.00 23.83 ? 51   ALA B O   1 
ATOM   2691 C  CB  . ALA B 2 51  ? 13.189  -3.299  24.534  1.00 22.87 ? 51   ALA B CB  1 
ATOM   2692 N  N   . GLY B 2 52  ? 9.979   -3.190  24.511  1.00 26.52 ? 52   GLY B N   1 
ATOM   2693 C  CA  . GLY B 2 52  ? 8.780   -2.545  25.001  1.00 28.69 ? 52   GLY B CA  1 
ATOM   2694 C  C   . GLY B 2 52  ? 9.032   -1.718  26.252  1.00 28.98 ? 52   GLY B C   1 
ATOM   2695 O  O   . GLY B 2 52  ? 10.155  -1.577  26.735  1.00 24.53 ? 52   GLY B O   1 
ATOM   2696 N  N   . GLY B 2 53  ? 7.950   -1.136  26.765  1.00 24.70 ? 53   GLY B N   1 
ATOM   2697 C  CA  . GLY B 2 53  ? 8.026   -0.348  27.981  1.00 26.45 ? 53   GLY B CA  1 
ATOM   2698 C  C   . GLY B 2 53  ? 8.738   0.978   27.846  1.00 25.37 ? 53   GLY B C   1 
ATOM   2699 O  O   . GLY B 2 53  ? 9.253   1.493   28.839  1.00 25.79 ? 53   GLY B O   1 
ATOM   2700 N  N   . ARG B 2 54  ? 8.766   1.561   26.641  1.00 22.36 ? 54   ARG B N   1 
ATOM   2701 C  CA  . ARG B 2 54  ? 9.528   2.787   26.437  1.00 21.40 ? 54   ARG B CA  1 
ATOM   2702 C  C   . ARG B 2 54  ? 9.011   3.931   27.293  1.00 22.97 ? 54   ARG B C   1 
ATOM   2703 O  O   . ARG B 2 54  ? 9.804   4.752   27.767  1.00 22.33 ? 54   ARG B O   1 
ATOM   2704 C  CB  . ARG B 2 54  ? 9.505   3.182   24.965  1.00 22.65 ? 54   ARG B CB  1 
ATOM   2705 C  CG  . ARG B 2 54  ? 10.400  2.303   24.087  1.00 21.97 ? 54   ARG B CG  1 
ATOM   2706 C  CD  . ARG B 2 54  ? 10.218  2.663   22.639  1.00 18.42 ? 54   ARG B CD  1 
ATOM   2707 N  NE  . ARG B 2 54  ? 8.885   2.325   22.153  1.00 19.88 ? 54   ARG B NE  1 
ATOM   2708 C  CZ  . ARG B 2 54  ? 8.371   2.808   21.026  1.00 22.66 ? 54   ARG B CZ  1 
ATOM   2709 N  NH1 . ARG B 2 54  ? 9.067   3.669   20.292  1.00 22.86 ? 54   ARG B NH1 1 
ATOM   2710 N  NH2 . ARG B 2 54  ? 7.165   2.434   20.634  1.00 23.98 ? 54   ARG B NH2 1 
ATOM   2711 N  N   . GLY B 2 55  ? 7.701   3.986   27.523  1.00 23.31 ? 55   GLY B N   1 
ATOM   2712 C  CA  . GLY B 2 55  ? 7.128   5.135   28.206  1.00 25.28 ? 55   GLY B CA  1 
ATOM   2713 C  C   . GLY B 2 55  ? 7.616   5.285   29.635  1.00 26.26 ? 55   GLY B C   1 
ATOM   2714 O  O   . GLY B 2 55  ? 7.909   6.396   30.087  1.00 26.47 ? 55   GLY B O   1 
ATOM   2715 N  N   . LYS B 2 56  ? 7.711   4.174   30.363  1.00 28.38 ? 56   LYS B N   1 
ATOM   2716 C  CA  . LYS B 2 56  ? 8.170   4.175   31.747  1.00 28.85 ? 56   LYS B CA  1 
ATOM   2717 C  C   . LYS B 2 56  ? 9.681   4.024   31.880  1.00 29.04 ? 56   LYS B C   1 
ATOM   2718 O  O   . LYS B 2 56  ? 10.180  3.968   33.006  1.00 30.93 ? 56   LYS B O   1 
ATOM   2719 C  CB  . LYS B 2 56  ? 7.482   3.055   32.530  1.00 33.82 ? 56   LYS B CB  1 
ATOM   2720 C  CG  . LYS B 2 56  ? 5.970   3.152   32.572  1.00 33.27 ? 56   LYS B CG  1 
ATOM   2721 C  CD  . LYS B 2 56  ? 5.517   4.268   33.477  1.00 36.40 ? 56   LYS B CD  1 
ATOM   2722 C  CE  . LYS B 2 56  ? 5.740   3.938   34.936  1.00 45.97 ? 56   LYS B CE  1 
ATOM   2723 N  NZ  . LYS B 2 56  ? 5.509   5.162   35.761  1.00 46.88 ? 56   LYS B NZ  1 
ATOM   2724 N  N   . GLY B 2 57  ? 10.418  3.960   30.773  1.00 29.63 ? 57   GLY B N   1 
ATOM   2725 C  CA  . GLY B 2 57  ? 11.855  3.786   30.821  1.00 25.14 ? 57   GLY B CA  1 
ATOM   2726 C  C   . GLY B 2 57  ? 12.597  5.048   31.232  1.00 32.26 ? 57   GLY B C   1 
ATOM   2727 O  O   . GLY B 2 57  ? 12.027  6.127   31.406  1.00 29.88 ? 57   GLY B O   1 
ATOM   2728 N  N   . VAL B 2 58  ? 13.912  4.891   31.393  1.00 28.79 ? 58   VAL B N   1 
ATOM   2729 C  CA  . VAL B 2 58  ? 14.784  5.937   31.920  1.00 30.47 ? 58   VAL B CA  1 
ATOM   2730 C  C   . VAL B 2 58  ? 16.056  5.982   31.086  1.00 31.71 ? 58   VAL B C   1 
ATOM   2731 O  O   . VAL B 2 58  ? 16.605  4.940   30.717  1.00 32.47 ? 58   VAL B O   1 
ATOM   2732 C  CB  . VAL B 2 58  ? 15.133  5.696   33.408  1.00 30.06 ? 58   VAL B CB  1 
ATOM   2733 C  CG1 . VAL B 2 58  ? 15.852  6.907   33.998  1.00 34.51 ? 58   VAL B CG1 1 
ATOM   2734 C  CG2 . VAL B 2 58  ? 13.890  5.356   34.216  1.00 30.29 ? 58   VAL B CG2 1 
ATOM   2735 N  N   . PHE B 2 59  ? 16.537  7.187   30.804  1.00 28.97 ? 59   PHE B N   1 
ATOM   2736 C  CA  . PHE B 2 59  ? 17.786  7.375   30.081  1.00 31.41 ? 59   PHE B CA  1 
ATOM   2737 C  C   . PHE B 2 59  ? 18.934  7.558   31.063  1.00 37.45 ? 59   PHE B C   1 
ATOM   2738 O  O   . PHE B 2 59  ? 18.744  8.027   32.188  1.00 36.65 ? 59   PHE B O   1 
ATOM   2739 C  CB  . PHE B 2 59  ? 17.719  8.591   29.152  1.00 29.58 ? 59   PHE B CB  1 
ATOM   2740 C  CG  . PHE B 2 59  ? 16.784  8.415   27.975  1.00 33.04 ? 59   PHE B CG  1 
ATOM   2741 C  CD1 . PHE B 2 59  ? 15.440  8.738   28.080  1.00 31.34 ? 59   PHE B CD1 1 
ATOM   2742 C  CD2 . PHE B 2 59  ? 17.258  7.946   26.761  1.00 27.78 ? 59   PHE B CD2 1 
ATOM   2743 C  CE1 . PHE B 2 59  ? 14.588  8.591   26.999  1.00 27.88 ? 59   PHE B CE1 1 
ATOM   2744 C  CE2 . PHE B 2 59  ? 16.406  7.789   25.685  1.00 30.59 ? 59   PHE B CE2 1 
ATOM   2745 C  CZ  . PHE B 2 59  ? 15.072  8.106   25.807  1.00 25.02 ? 59   PHE B CZ  1 
ATOM   2746 N  N   . ASN B 2 60  ? 20.137  7.191   30.625  1.00 37.72 ? 60   ASN B N   1 
ATOM   2747 C  CA  . ASN B 2 60  ? 21.311  7.438   31.447  1.00 39.30 ? 60   ASN B CA  1 
ATOM   2748 C  C   . ASN B 2 60  ? 21.736  8.904   31.412  1.00 41.06 ? 60   ASN B C   1 
ATOM   2749 O  O   . ASN B 2 60  ? 22.652  9.289   32.147  1.00 34.57 ? 60   ASN B O   1 
ATOM   2750 C  CB  . ASN B 2 60  ? 22.458  6.502   31.028  1.00 37.72 ? 60   ASN B CB  1 
ATOM   2751 C  CG  . ASN B 2 60  ? 22.983  6.785   29.633  1.00 38.17 ? 60   ASN B CG  1 
ATOM   2752 O  OD1 . ASN B 2 60  ? 22.323  7.437   28.828  1.00 40.25 ? 60   ASN B OD1 1 
ATOM   2753 N  ND2 . ASN B 2 60  ? 24.183  6.284   29.339  1.00 39.25 ? 60   ASN B ND2 1 
ATOM   2754 N  N   . SER B 2 61  ? 21.080  9.728   30.590  1.00 39.45 ? 61   SER B N   1 
ATOM   2755 C  CA  . SER B 2 61  ? 21.180  11.177  30.714  1.00 35.34 ? 61   SER B CA  1 
ATOM   2756 C  C   . SER B 2 61  ? 20.480  11.712  31.955  1.00 33.45 ? 61   SER B C   1 
ATOM   2757 O  O   . SER B 2 61  ? 20.660  12.886  32.283  1.00 38.01 ? 61   SER B O   1 
ATOM   2758 C  CB  . SER B 2 61  ? 20.579  11.857  29.479  1.00 38.91 ? 61   SER B CB  1 
ATOM   2759 O  OG  . SER B 2 61  ? 19.171  11.670  29.422  1.00 35.71 ? 61   SER B OG  1 
ATOM   2760 N  N   . GLY B 2 62  ? 19.672  10.898  32.634  1.00 35.64 ? 62   GLY B N   1 
ATOM   2761 C  CA  . GLY B 2 62  ? 18.818  11.344  33.709  1.00 35.49 ? 62   GLY B CA  1 
ATOM   2762 C  C   . GLY B 2 62  ? 17.357  11.484  33.314  1.00 36.03 ? 62   GLY B C   1 
ATOM   2763 O  O   . GLY B 2 62  ? 16.472  11.364  34.173  1.00 32.34 ? 62   GLY B O   1 
ATOM   2764 N  N   . LEU B 2 63  ? 17.088  11.709  32.030  1.00 35.77 ? 63   LEU B N   1 
ATOM   2765 C  CA  . LEU B 2 63  ? 15.721  11.868  31.556  1.00 29.77 ? 63   LEU B CA  1 
ATOM   2766 C  C   . LEU B 2 63  ? 14.871  10.656  31.902  1.00 31.35 ? 63   LEU B C   1 
ATOM   2767 O  O   . LEU B 2 63  ? 15.262  9.509   31.656  1.00 34.79 ? 63   LEU B O   1 
ATOM   2768 C  CB  . LEU B 2 63  ? 15.713  12.095  30.045  1.00 32.49 ? 63   LEU B CB  1 
ATOM   2769 C  CG  . LEU B 2 63  ? 14.331  12.398  29.456  1.00 31.59 ? 63   LEU B CG  1 
ATOM   2770 C  CD1 . LEU B 2 63  ? 13.728  13.628  30.141  1.00 33.00 ? 63   LEU B CD1 1 
ATOM   2771 C  CD2 . LEU B 2 63  ? 14.413  12.603  27.953  1.00 31.66 ? 63   LEU B CD2 1 
ATOM   2772 N  N   . LYS B 2 64  ? 13.704  10.914  32.482  1.00 26.46 ? 64   LYS B N   1 
ATOM   2773 C  CA  . LYS B 2 64  ? 12.695  9.886   32.691  1.00 29.19 ? 64   LYS B CA  1 
ATOM   2774 C  C   . LYS B 2 64  ? 11.723  9.900   31.516  1.00 30.23 ? 64   LYS B C   1 
ATOM   2775 O  O   . LYS B 2 64  ? 11.287  10.974  31.080  1.00 25.75 ? 64   LYS B O   1 
ATOM   2776 C  CB  . LYS B 2 64  ? 11.954  10.115  34.008  1.00 30.59 ? 64   LYS B CB  1 
ATOM   2777 C  CG  . LYS B 2 64  ? 12.770  9.769   35.256  1.00 33.67 ? 64   LYS B CG  1 
ATOM   2778 C  CD  . LYS B 2 64  ? 12.031  10.148  36.532  1.00 34.56 ? 64   LYS B CD  1 
ATOM   2779 N  N   . GLY B 2 65  ? 11.411  8.710   30.993  1.00 28.00 ? 65   GLY B N   1 
ATOM   2780 C  CA  . GLY B 2 65  ? 10.432  8.553   29.934  1.00 28.39 ? 65   GLY B CA  1 
ATOM   2781 C  C   . GLY B 2 65  ? 10.994  8.538   28.523  1.00 26.42 ? 65   GLY B C   1 
ATOM   2782 O  O   . GLY B 2 65  ? 11.622  9.505   28.084  1.00 24.09 ? 65   GLY B O   1 
ATOM   2783 N  N   . GLY B 2 66  ? 10.787  7.435   27.801  1.00 26.54 ? 66   GLY B N   1 
ATOM   2784 C  CA  . GLY B 2 66  ? 11.163  7.368   26.400  1.00 22.49 ? 66   GLY B CA  1 
ATOM   2785 C  C   . GLY B 2 66  ? 10.069  7.778   25.445  1.00 22.33 ? 66   GLY B C   1 
ATOM   2786 O  O   . GLY B 2 66  ? 10.293  7.834   24.230  1.00 23.23 ? 66   GLY B O   1 
ATOM   2787 N  N   . VAL B 2 67  ? 8.878   8.034   25.983  1.00 20.71 ? 67   VAL B N   1 
ATOM   2788 C  CA  . VAL B 2 67  ? 7.742   8.590   25.256  1.00 24.74 ? 67   VAL B CA  1 
ATOM   2789 C  C   . VAL B 2 67  ? 7.306   9.832   26.021  1.00 25.51 ? 67   VAL B C   1 
ATOM   2790 O  O   . VAL B 2 67  ? 7.041   9.754   27.224  1.00 22.90 ? 67   VAL B O   1 
ATOM   2791 C  CB  . VAL B 2 67  ? 6.571   7.594   25.134  1.00 22.63 ? 67   VAL B CB  1 
ATOM   2792 C  CG1 . VAL B 2 67  ? 5.385   8.250   24.428  1.00 24.12 ? 67   VAL B CG1 1 
ATOM   2793 C  CG2 . VAL B 2 67  ? 7.005   6.310   24.390  1.00 19.35 ? 67   VAL B CG2 1 
ATOM   2794 N  N   . HIS B 2 68  ? 7.266   10.973  25.337  1.00 25.56 ? 68   HIS B N   1 
ATOM   2795 C  CA  . HIS B 2 68  ? 6.798   12.228  25.910  1.00 24.27 ? 68   HIS B CA  1 
ATOM   2796 C  C   . HIS B 2 68  ? 5.794   12.860  24.963  1.00 26.32 ? 68   HIS B C   1 
ATOM   2797 O  O   . HIS B 2 68  ? 5.952   12.779  23.737  1.00 21.99 ? 68   HIS B O   1 
ATOM   2798 C  CB  . HIS B 2 68  ? 7.949   13.220  26.148  1.00 20.39 ? 68   HIS B CB  1 
ATOM   2799 C  CG  . HIS B 2 68  ? 8.759   12.921  27.369  1.00 30.68 ? 68   HIS B CG  1 
ATOM   2800 N  ND1 . HIS B 2 68  ? 8.584   13.593  28.559  1.00 29.58 ? 68   HIS B ND1 1 
ATOM   2801 C  CD2 . HIS B 2 68  ? 9.730   12.003  27.594  1.00 31.15 ? 68   HIS B CD2 1 
ATOM   2802 C  CE1 . HIS B 2 68  ? 9.414   13.106  29.465  1.00 29.01 ? 68   HIS B CE1 1 
ATOM   2803 N  NE2 . HIS B 2 68  ? 10.122  12.141  28.903  1.00 32.67 ? 68   HIS B NE2 1 
ATOM   2804 N  N   . LEU B 2 69  ? 4.771   13.492  25.540  1.00 24.32 ? 69   LEU B N   1 
ATOM   2805 C  CA  . LEU B 2 69  ? 3.813   14.313  24.812  1.00 25.12 ? 69   LEU B CA  1 
ATOM   2806 C  C   . LEU B 2 69  ? 3.991   15.779  25.175  1.00 25.77 ? 69   LEU B C   1 
ATOM   2807 O  O   . LEU B 2 69  ? 4.256   16.112  26.334  1.00 25.53 ? 69   LEU B O   1 
ATOM   2808 C  CB  . LEU B 2 69  ? 2.375   13.896  25.117  1.00 26.18 ? 69   LEU B CB  1 
ATOM   2809 C  CG  . LEU B 2 69  ? 1.976   12.559  24.503  1.00 26.45 ? 69   LEU B CG  1 
ATOM   2810 C  CD1 . LEU B 2 69  ? 2.217   11.455  25.517  1.00 27.63 ? 69   LEU B CD1 1 
ATOM   2811 C  CD2 . LEU B 2 69  ? 0.539   12.587  24.038  1.00 21.63 ? 69   LEU B CD2 1 
ATOM   2812 N  N   . THR B 2 70  ? 3.829   16.648  24.180  1.00 25.92 ? 70   THR B N   1 
ATOM   2813 C  CA  . THR B 2 70  ? 3.833   18.084  24.407  1.00 27.43 ? 70   THR B CA  1 
ATOM   2814 C  C   . THR B 2 70  ? 3.170   18.768  23.220  1.00 29.22 ? 70   THR B C   1 
ATOM   2815 O  O   . THR B 2 70  ? 3.000   18.172  22.151  1.00 25.69 ? 70   THR B O   1 
ATOM   2816 C  CB  . THR B 2 70  ? 5.253   18.625  24.601  1.00 26.44 ? 70   THR B CB  1 
ATOM   2817 O  OG1 . THR B 2 70  ? 5.214   20.059  24.621  1.00 25.74 ? 70   THR B OG1 1 
ATOM   2818 C  CG2 . THR B 2 70  ? 6.166   18.169  23.454  1.00 22.62 ? 70   THR B CG2 1 
ATOM   2819 N  N   . LYS B 2 71  ? 2.811   20.039  23.418  1.00 28.29 ? 71   LYS B N   1 
ATOM   2820 C  CA  . LYS B 2 71  ? 2.335   20.896  22.335  1.00 25.87 ? 71   LYS B CA  1 
ATOM   2821 C  C   . LYS B 2 71  ? 3.421   21.800  21.780  1.00 28.17 ? 71   LYS B C   1 
ATOM   2822 O  O   . LYS B 2 71  ? 3.180   22.497  20.788  1.00 33.26 ? 71   LYS B O   1 
ATOM   2823 C  CB  . LYS B 2 71  ? 1.163   21.756  22.813  1.00 22.54 ? 71   LYS B CB  1 
ATOM   2824 C  CG  . LYS B 2 71  ? -0.101  20.974  23.049  1.00 22.13 ? 71   LYS B CG  1 
ATOM   2825 C  CD  . LYS B 2 71  ? -1.052  21.753  23.920  1.00 28.20 ? 71   LYS B CD  1 
ATOM   2826 C  CE  . LYS B 2 71  ? -2.489  21.320  23.690  1.00 27.28 ? 71   LYS B CE  1 
ATOM   2827 N  NZ  . LYS B 2 71  ? -2.734  19.885  23.991  1.00 37.89 ? 71   LYS B NZ  1 
ATOM   2828 N  N   . ASP B 2 72  ? 4.606   21.797  22.385  1.00 30.58 ? 72   ASP B N   1 
ATOM   2829 C  CA  . ASP B 2 72  ? 5.611   22.828  22.148  1.00 29.85 ? 72   ASP B CA  1 
ATOM   2830 C  C   . ASP B 2 72  ? 6.835   22.230  21.478  1.00 24.56 ? 72   ASP B C   1 
ATOM   2831 O  O   . ASP B 2 72  ? 7.557   21.450  22.117  1.00 28.26 ? 72   ASP B O   1 
ATOM   2832 C  CB  . ASP B 2 72  ? 5.997   23.482  23.478  1.00 32.62 ? 72   ASP B CB  1 
ATOM   2833 C  CG  . ASP B 2 72  ? 6.960   24.658  23.321  1.00 32.00 ? 72   ASP B CG  1 
ATOM   2834 O  OD1 . ASP B 2 72  ? 7.654   24.787  22.289  1.00 27.59 ? 72   ASP B OD1 1 
ATOM   2835 O  OD2 . ASP B 2 72  ? 7.030   25.453  24.276  1.00 29.77 ? 72   ASP B OD2 1 
ATOM   2836 N  N   . PRO B 2 73  ? 7.128   22.584  20.222  1.00 29.73 ? 73   PRO B N   1 
ATOM   2837 C  CA  . PRO B 2 73  ? 8.307   22.008  19.548  1.00 27.09 ? 73   PRO B CA  1 
ATOM   2838 C  C   . PRO B 2 73  ? 9.625   22.227  20.282  1.00 30.04 ? 73   PRO B C   1 
ATOM   2839 O  O   . PRO B 2 73  ? 10.508  21.360  20.208  1.00 28.34 ? 73   PRO B O   1 
ATOM   2840 C  CB  . PRO B 2 73  ? 8.300   22.708  18.183  1.00 30.35 ? 73   PRO B CB  1 
ATOM   2841 C  CG  . PRO B 2 73  ? 6.863   23.032  17.933  1.00 31.58 ? 73   PRO B CG  1 
ATOM   2842 C  CD  . PRO B 2 73  ? 6.278   23.360  19.295  1.00 32.23 ? 73   PRO B CD  1 
ATOM   2843 N  N   . ASN B 2 74  ? 9.797   23.358  20.981  1.00 34.31 ? 74   ASN B N   1 
ATOM   2844 C  CA  . ASN B 2 74  ? 11.016  23.561  21.768  1.00 28.69 ? 74   ASN B CA  1 
ATOM   2845 C  C   . ASN B 2 74  ? 11.177  22.459  22.808  1.00 29.93 ? 74   ASN B C   1 
ATOM   2846 O  O   . ASN B 2 74  ? 12.285  21.957  23.032  1.00 31.79 ? 74   ASN B O   1 
ATOM   2847 C  CB  . ASN B 2 74  ? 10.993  24.936  22.453  1.00 30.79 ? 74   ASN B CB  1 
ATOM   2848 C  CG  . ASN B 2 74  ? 10.991  26.089  21.469  1.00 36.07 ? 74   ASN B CG  1 
ATOM   2849 O  OD1 . ASN B 2 74  ? 11.717  26.078  20.474  1.00 35.54 ? 74   ASN B OD1 1 
ATOM   2850 N  ND2 . ASN B 2 74  ? 10.174  27.105  21.750  1.00 38.89 ? 74   ASN B ND2 1 
ATOM   2851 N  N   . VAL B 2 75  ? 10.072  22.062  23.443  1.00 28.96 ? 75   VAL B N   1 
ATOM   2852 C  CA  . VAL B 2 75  ? 10.106  20.970  24.409  1.00 29.77 ? 75   VAL B CA  1 
ATOM   2853 C  C   . VAL B 2 75  ? 10.515  19.664  23.725  1.00 30.58 ? 75   VAL B C   1 
ATOM   2854 O  O   . VAL B 2 75  ? 11.263  18.859  24.295  1.00 29.36 ? 75   VAL B O   1 
ATOM   2855 C  CB  . VAL B 2 75  ? 8.741   20.864  25.123  1.00 32.34 ? 75   VAL B CB  1 
ATOM   2856 C  CG1 . VAL B 2 75  ? 8.627   19.575  25.943  1.00 24.33 ? 75   VAL B CG1 1 
ATOM   2857 C  CG2 . VAL B 2 75  ? 8.506   22.099  26.020  1.00 25.81 ? 75   VAL B CG2 1 
ATOM   2858 N  N   . VAL B 2 76  ? 10.052  19.450  22.485  1.00 31.66 ? 76   VAL B N   1 
ATOM   2859 C  CA  . VAL B 2 76  ? 10.504  18.306  21.683  1.00 28.03 ? 76   VAL B CA  1 
ATOM   2860 C  C   . VAL B 2 76  ? 12.011  18.353  21.479  1.00 29.06 ? 76   VAL B C   1 
ATOM   2861 O  O   . VAL B 2 76  ? 12.697  17.323  21.550  1.00 28.12 ? 76   VAL B O   1 
ATOM   2862 C  CB  . VAL B 2 76  ? 9.776   18.266  20.323  1.00 29.57 ? 76   VAL B CB  1 
ATOM   2863 C  CG1 . VAL B 2 76  ? 10.199  17.024  19.524  1.00 23.37 ? 76   VAL B CG1 1 
ATOM   2864 C  CG2 . VAL B 2 76  ? 8.260   18.309  20.506  1.00 28.91 ? 76   VAL B CG2 1 
ATOM   2865 N  N   . GLY B 2 77  ? 12.549  19.541  21.191  1.00 30.77 ? 77   GLY B N   1 
ATOM   2866 C  CA  . GLY B 2 77  ? 13.987  19.662  21.007  1.00 29.51 ? 77   GLY B CA  1 
ATOM   2867 C  C   . GLY B 2 77  ? 14.757  19.383  22.283  1.00 35.25 ? 77   GLY B C   1 
ATOM   2868 O  O   . GLY B 2 77  ? 15.732  18.621  22.283  1.00 33.26 ? 77   GLY B O   1 
ATOM   2869 N  N   . GLN B 2 78  ? 14.317  19.989  23.395  1.00 32.97 ? 78   GLN B N   1 
ATOM   2870 C  CA  . GLN B 2 78  ? 15.022  19.835  24.664  1.00 34.35 ? 78   GLN B CA  1 
ATOM   2871 C  C   . GLN B 2 78  ? 15.030  18.384  25.116  1.00 34.85 ? 78   GLN B C   1 
ATOM   2872 O  O   . GLN B 2 78  ? 16.052  17.877  25.594  1.00 29.18 ? 78   GLN B O   1 
ATOM   2873 C  CB  . GLN B 2 78  ? 14.372  20.719  25.733  1.00 37.10 ? 78   GLN B CB  1 
ATOM   2874 C  CG  . GLN B 2 78  ? 14.379  22.204  25.402  1.00 34.76 ? 78   GLN B CG  1 
ATOM   2875 C  CD  . GLN B 2 78  ? 13.451  23.011  26.295  1.00 36.81 ? 78   GLN B CD  1 
ATOM   2876 O  OE1 . GLN B 2 78  ? 12.900  22.500  27.270  1.00 42.52 ? 78   GLN B OE1 1 
ATOM   2877 N  NE2 . GLN B 2 78  ? 13.274  24.278  25.963  1.00 35.91 ? 78   GLN B NE2 1 
ATOM   2878 N  N   . LEU B 2 79  ? 13.887  17.705  24.985  1.00 36.06 ? 79   LEU B N   1 
ATOM   2879 C  CA  . LEU B 2 79  ? 13.799  16.311  25.392  1.00 33.60 ? 79   LEU B CA  1 
ATOM   2880 C  C   . LEU B 2 79  ? 14.594  15.414  24.454  1.00 32.39 ? 79   LEU B C   1 
ATOM   2881 O  O   . LEU B 2 79  ? 15.209  14.439  24.897  1.00 28.98 ? 79   LEU B O   1 
ATOM   2882 C  CB  . LEU B 2 79  ? 12.337  15.874  25.441  1.00 32.26 ? 79   LEU B CB  1 
ATOM   2883 C  CG  . LEU B 2 79  ? 11.537  16.462  26.590  1.00 31.10 ? 79   LEU B CG  1 
ATOM   2884 C  CD1 . LEU B 2 79  ? 10.081  16.076  26.449  1.00 34.48 ? 79   LEU B CD1 1 
ATOM   2885 C  CD2 . LEU B 2 79  ? 12.109  15.975  27.915  1.00 33.67 ? 79   LEU B CD2 1 
ATOM   2886 N  N   . ALA B 2 80  ? 14.595  15.724  23.157  1.00 31.65 ? 80   ALA B N   1 
ATOM   2887 C  CA  . ALA B 2 80  ? 15.324  14.879  22.215  1.00 32.98 ? 80   ALA B CA  1 
ATOM   2888 C  C   . ALA B 2 80  ? 16.820  14.894  22.506  1.00 33.88 ? 80   ALA B C   1 
ATOM   2889 O  O   . ALA B 2 80  ? 17.478  13.847  22.453  1.00 29.89 ? 80   ALA B O   1 
ATOM   2890 C  CB  . ALA B 2 80  ? 15.052  15.317  20.777  1.00 27.07 ? 80   ALA B CB  1 
ATOM   2891 N  N   . LYS B 2 81  ? 17.374  16.071  22.819  1.00 36.64 ? 81   LYS B N   1 
ATOM   2892 C  CA  . LYS B 2 81  ? 18.795  16.157  23.157  1.00 35.63 ? 81   LYS B CA  1 
ATOM   2893 C  C   . LYS B 2 81  ? 19.132  15.339  24.397  1.00 32.72 ? 81   LYS B C   1 
ATOM   2894 O  O   . LYS B 2 81  ? 20.285  14.926  24.574  1.00 34.99 ? 81   LYS B O   1 
ATOM   2895 C  CB  . LYS B 2 81  ? 19.208  17.619  23.362  1.00 39.25 ? 81   LYS B CB  1 
ATOM   2896 N  N   . GLN B 2 82  ? 18.159  15.113  25.276  1.00 29.23 ? 82   GLN B N   1 
ATOM   2897 C  CA  . GLN B 2 82  ? 18.363  14.204  26.399  1.00 31.54 ? 82   GLN B CA  1 
ATOM   2898 C  C   . GLN B 2 82  ? 18.178  12.741  26.006  1.00 35.96 ? 82   GLN B C   1 
ATOM   2899 O  O   . GLN B 2 82  ? 18.412  11.853  26.836  1.00 36.01 ? 82   GLN B O   1 
ATOM   2900 C  CB  . GLN B 2 82  ? 17.414  14.557  27.555  1.00 36.70 ? 82   GLN B CB  1 
ATOM   2901 C  CG  . GLN B 2 82  ? 17.660  15.924  28.229  1.00 33.71 ? 82   GLN B CG  1 
ATOM   2902 C  CD  . GLN B 2 82  ? 16.637  16.238  29.331  1.00 38.99 ? 82   GLN B CD  1 
ATOM   2903 O  OE1 . GLN B 2 82  ? 16.773  15.781  30.469  1.00 43.65 ? 82   GLN B OE1 1 
ATOM   2904 N  NE2 . GLN B 2 82  ? 15.609  17.019  28.992  1.00 39.40 ? 82   GLN B NE2 1 
ATOM   2905 N  N   . MET B 2 83  ? 17.775  12.469  24.766  1.00 32.91 ? 83   MET B N   1 
ATOM   2906 C  CA  . MET B 2 83  ? 17.514  11.115  24.296  1.00 30.03 ? 83   MET B CA  1 
ATOM   2907 C  C   . MET B 2 83  ? 18.600  10.589  23.372  1.00 30.66 ? 83   MET B C   1 
ATOM   2908 O  O   . MET B 2 83  ? 19.114  9.485   23.582  1.00 33.15 ? 83   MET B O   1 
ATOM   2909 C  CB  . MET B 2 83  ? 16.162  11.065  23.568  1.00 24.95 ? 83   MET B CB  1 
ATOM   2910 C  CG  . MET B 2 83  ? 14.961  11.195  24.480  1.00 29.83 ? 83   MET B CG  1 
ATOM   2911 S  SD  . MET B 2 83  ? 13.451  10.700  23.637  1.00 28.94 ? 83   MET B SD  1 
ATOM   2912 C  CE  . MET B 2 83  ? 12.285  10.643  24.984  1.00 30.81 ? 83   MET B CE  1 
ATOM   2913 N  N   . ILE B 2 84  ? 18.960  11.355  22.353  1.00 31.66 ? 84   ILE B N   1 
ATOM   2914 C  CA  . ILE B 2 84  ? 19.789  10.854  21.266  1.00 30.75 ? 84   ILE B CA  1 
ATOM   2915 C  C   . ILE B 2 84  ? 21.234  10.735  21.735  1.00 36.26 ? 84   ILE B C   1 
ATOM   2916 O  O   . ILE B 2 84  ? 21.769  11.626  22.405  1.00 36.30 ? 84   ILE B O   1 
ATOM   2917 C  CB  . ILE B 2 84  ? 19.646  11.769  20.037  1.00 33.48 ? 84   ILE B CB  1 
ATOM   2918 C  CG1 . ILE B 2 84  ? 18.167  11.869  19.641  1.00 31.91 ? 84   ILE B CG1 1 
ATOM   2919 C  CG2 . ILE B 2 84  ? 20.474  11.252  18.872  1.00 31.87 ? 84   ILE B CG2 1 
ATOM   2920 C  CD1 . ILE B 2 84  ? 17.888  12.847  18.523  1.00 30.07 ? 84   ILE B CD1 1 
ATOM   2921 N  N   . GLY B 2 85  ? 21.869  9.619   21.391  1.00 36.80 ? 85   GLY B N   1 
ATOM   2922 C  CA  . GLY B 2 85  ? 23.188  9.315   21.888  1.00 30.08 ? 85   GLY B CA  1 
ATOM   2923 C  C   . GLY B 2 85  ? 23.225  8.771   23.301  1.00 36.66 ? 85   GLY B C   1 
ATOM   2924 O  O   . GLY B 2 85  ? 24.321  8.517   23.818  1.00 40.71 ? 85   GLY B O   1 
ATOM   2925 N  N   . TYR B 2 86  ? 22.076  8.583   23.945  1.00 32.01 ? 86   TYR B N   1 
ATOM   2926 C  CA  . TYR B 2 86  ? 22.012  8.017   25.285  1.00 32.73 ? 86   TYR B CA  1 
ATOM   2927 C  C   . TYR B 2 86  ? 21.372  6.638   25.229  1.00 35.57 ? 86   TYR B C   1 
ATOM   2928 O  O   . TYR B 2 86  ? 20.864  6.212   24.189  1.00 34.83 ? 86   TYR B O   1 
ATOM   2929 C  CB  . TYR B 2 86  ? 21.243  8.943   26.237  1.00 33.28 ? 86   TYR B CB  1 
ATOM   2930 C  CG  . TYR B 2 86  ? 21.989  10.225  26.544  1.00 33.89 ? 86   TYR B CG  1 
ATOM   2931 C  CD1 . TYR B 2 86  ? 22.955  10.267  27.549  1.00 36.41 ? 86   TYR B CD1 1 
ATOM   2932 C  CD2 . TYR B 2 86  ? 21.735  11.390  25.830  1.00 35.32 ? 86   TYR B CD2 1 
ATOM   2933 C  CE1 . TYR B 2 86  ? 23.644  11.433  27.833  1.00 34.40 ? 86   TYR B CE1 1 
ATOM   2934 C  CE2 . TYR B 2 86  ? 22.422  12.562  26.109  1.00 35.87 ? 86   TYR B CE2 1 
ATOM   2935 C  CZ  . TYR B 2 86  ? 23.374  12.573  27.109  1.00 38.39 ? 86   TYR B CZ  1 
ATOM   2936 O  OH  . TYR B 2 86  ? 24.061  13.732  27.393  1.00 42.88 ? 86   TYR B OH  1 
ATOM   2937 N  N   . ASN B 2 87  ? 21.419  5.937   26.362  1.00 28.72 ? 87   ASN B N   1 
ATOM   2938 C  CA  . ASN B 2 87  ? 20.882  4.586   26.484  1.00 33.38 ? 87   ASN B CA  1 
ATOM   2939 C  C   . ASN B 2 87  ? 19.569  4.612   27.255  1.00 33.56 ? 87   ASN B C   1 
ATOM   2940 O  O   . ASN B 2 87  ? 19.507  5.126   28.381  1.00 29.82 ? 87   ASN B O   1 
ATOM   2941 C  CB  . ASN B 2 87  ? 21.869  3.650   27.187  1.00 32.11 ? 87   ASN B CB  1 
ATOM   2942 C  CG  . ASN B 2 87  ? 22.949  3.127   26.255  1.00 33.71 ? 87   ASN B CG  1 
ATOM   2943 O  OD1 . ASN B 2 87  ? 23.314  3.775   25.282  1.00 32.86 ? 87   ASN B OD1 1 
ATOM   2944 N  ND2 . ASN B 2 87  ? 23.461  1.940   26.554  1.00 38.38 ? 87   ASN B ND2 1 
ATOM   2945 N  N   . LEU B 2 88  ? 18.533  4.046   26.652  1.00 31.92 ? 88   LEU B N   1 
ATOM   2946 C  CA  . LEU B 2 88  ? 17.208  3.969   27.248  1.00 30.40 ? 88   LEU B CA  1 
ATOM   2947 C  C   . LEU B 2 88  ? 17.013  2.572   27.819  1.00 27.41 ? 88   LEU B C   1 
ATOM   2948 O  O   . LEU B 2 88  ? 17.025  1.587   27.073  1.00 29.60 ? 88   LEU B O   1 
ATOM   2949 C  CB  . LEU B 2 88  ? 16.130  4.279   26.212  1.00 27.64 ? 88   LEU B CB  1 
ATOM   2950 C  CG  . LEU B 2 88  ? 14.696  4.025   26.676  1.00 32.34 ? 88   LEU B CG  1 
ATOM   2951 C  CD1 . LEU B 2 88  ? 14.354  4.894   27.894  1.00 24.97 ? 88   LEU B CD1 1 
ATOM   2952 C  CD2 . LEU B 2 88  ? 13.721  4.262   25.531  1.00 22.23 ? 88   LEU B CD2 1 
ATOM   2953 N  N   . ALA B 2 89  ? 16.863  2.488   29.135  1.00 27.74 ? 89   ALA B N   1 
ATOM   2954 C  CA  . ALA B 2 89  ? 16.594  1.232   29.810  1.00 30.78 ? 89   ALA B CA  1 
ATOM   2955 C  C   . ALA B 2 89  ? 15.116  1.168   30.155  1.00 29.77 ? 89   ALA B C   1 
ATOM   2956 O  O   . ALA B 2 89  ? 14.524  2.171   30.567  1.00 26.67 ? 89   ALA B O   1 
ATOM   2957 C  CB  . ALA B 2 89  ? 17.444  1.093   31.076  1.00 33.71 ? 89   ALA B CB  1 
ATOM   2958 N  N   . THR B 2 90  ? 14.522  -0.005  29.953  1.00 26.41 ? 90   THR B N   1 
ATOM   2959 C  CA  . THR B 2 90  ? 13.114  -0.250  30.233  1.00 29.54 ? 90   THR B CA  1 
ATOM   2960 C  C   . THR B 2 90  ? 12.990  -1.591  30.937  1.00 29.13 ? 90   THR B C   1 
ATOM   2961 O  O   . THR B 2 90  ? 13.960  -2.346  31.050  1.00 31.07 ? 90   THR B O   1 
ATOM   2962 C  CB  . THR B 2 90  ? 12.258  -0.281  28.960  1.00 26.69 ? 90   THR B CB  1 
ATOM   2963 O  OG1 . THR B 2 90  ? 12.479  -1.524  28.278  1.00 30.17 ? 90   THR B OG1 1 
ATOM   2964 C  CG2 . THR B 2 90  ? 12.598  0.876   28.029  1.00 23.96 ? 90   THR B CG2 1 
ATOM   2965 N  N   . LYS B 2 91  ? 11.770  -1.909  31.372  1.00 27.01 ? 91   LYS B N   1 
ATOM   2966 C  CA  . LYS B 2 91  ? 11.537  -3.204  32.008  1.00 33.02 ? 91   LYS B CA  1 
ATOM   2967 C  C   . LYS B 2 91  ? 11.886  -4.385  31.102  1.00 37.04 ? 91   LYS B C   1 
ATOM   2968 O  O   . LYS B 2 91  ? 12.011  -5.511  31.598  1.00 29.30 ? 91   LYS B O   1 
ATOM   2969 C  CB  . LYS B 2 91  ? 10.082  -3.328  32.447  1.00 28.11 ? 91   LYS B CB  1 
ATOM   2970 C  CG  . LYS B 2 91  ? 9.726   -2.496  33.664  1.00 34.28 ? 91   LYS B CG  1 
ATOM   2971 N  N   . GLN B 2 92  ? 12.035  -4.169  29.793  1.00 28.83 ? 92   GLN B N   1 
ATOM   2972 C  CA  . GLN B 2 92  ? 12.307  -5.261  28.862  1.00 32.99 ? 92   GLN B CA  1 
ATOM   2973 C  C   . GLN B 2 92  ? 13.705  -5.198  28.260  1.00 32.03 ? 92   GLN B C   1 
ATOM   2974 O  O   . GLN B 2 92  ? 14.012  -5.993  27.368  1.00 36.33 ? 92   GLN B O   1 
ATOM   2975 C  CB  . GLN B 2 92  ? 11.259  -5.289  27.745  1.00 30.18 ? 92   GLN B CB  1 
ATOM   2976 C  CG  . GLN B 2 92  ? 9.849   -5.599  28.228  1.00 33.39 ? 92   GLN B CG  1 
ATOM   2977 C  CD  . GLN B 2 92  ? 8.807   -5.467  27.126  1.00 39.55 ? 92   GLN B CD  1 
ATOM   2978 O  OE1 . GLN B 2 92  ? 7.932   -4.601  27.186  1.00 45.50 ? 92   GLN B OE1 1 
ATOM   2979 N  NE2 . GLN B 2 92  ? 8.890   -6.334  26.119  1.00 46.51 ? 92   GLN B NE2 1 
ATOM   2980 N  N   . THR B 2 93  ? 14.555  -4.282  28.714  1.00 29.31 ? 93   THR B N   1 
ATOM   2981 C  CA  . THR B 2 93  ? 15.944  -4.196  28.284  1.00 31.50 ? 93   THR B CA  1 
ATOM   2982 C  C   . THR B 2 93  ? 16.866  -4.695  29.385  1.00 33.59 ? 93   THR B C   1 
ATOM   2983 O  O   . THR B 2 93  ? 16.477  -4.749  30.556  1.00 31.02 ? 93   THR B O   1 
ATOM   2984 C  CB  . THR B 2 93  ? 16.366  -2.756  27.955  1.00 33.45 ? 93   THR B CB  1 
ATOM   2985 O  OG1 . THR B 2 93  ? 16.194  -1.937  29.118  1.00 30.30 ? 93   THR B OG1 1 
ATOM   2986 C  CG2 . THR B 2 93  ? 15.592  -2.183  26.790  1.00 29.95 ? 93   THR B CG2 1 
ATOM   2987 N  N   . PRO B 2 94  ? 18.107  -5.051  29.049  1.00 36.45 ? 94   PRO B N   1 
ATOM   2988 C  CA  . PRO B 2 94  ? 19.127  -5.212  30.089  1.00 37.25 ? 94   PRO B CA  1 
ATOM   2989 C  C   . PRO B 2 94  ? 19.316  -3.912  30.857  1.00 41.51 ? 94   PRO B C   1 
ATOM   2990 O  O   . PRO B 2 94  ? 18.956  -2.827  30.394  1.00 35.79 ? 94   PRO B O   1 
ATOM   2991 C  CB  . PRO B 2 94  ? 20.387  -5.587  29.300  1.00 34.52 ? 94   PRO B CB  1 
ATOM   2992 C  CG  . PRO B 2 94  ? 19.866  -6.212  28.043  1.00 34.53 ? 94   PRO B CG  1 
ATOM   2993 C  CD  . PRO B 2 94  ? 18.621  -5.421  27.717  1.00 32.43 ? 94   PRO B CD  1 
ATOM   2994 N  N   . LYS B 2 95  ? 19.899  -4.036  32.055  1.00 42.07 ? 95   LYS B N   1 
ATOM   2995 C  CA  . LYS B 2 95  ? 20.011  -2.897  32.963  1.00 36.35 ? 95   LYS B CA  1 
ATOM   2996 C  C   . LYS B 2 95  ? 20.688  -1.698  32.313  1.00 36.64 ? 95   LYS B C   1 
ATOM   2997 O  O   . LYS B 2 95  ? 20.382  -0.552  32.658  1.00 37.87 ? 95   LYS B O   1 
ATOM   2998 C  CB  . LYS B 2 95  ? 20.772  -3.305  34.226  1.00 43.70 ? 95   LYS B CB  1 
ATOM   2999 N  N   . GLU B 2 96  ? 21.588  -1.938  31.362  1.00 34.65 ? 96   GLU B N   1 
ATOM   3000 C  CA  . GLU B 2 96  ? 22.359  -0.880  30.719  1.00 36.64 ? 96   GLU B CA  1 
ATOM   3001 C  C   . GLU B 2 96  ? 21.631  -0.239  29.536  1.00 38.44 ? 96   GLU B C   1 
ATOM   3002 O  O   . GLU B 2 96  ? 22.163  0.708   28.935  1.00 33.15 ? 96   GLU B O   1 
ATOM   3003 C  CB  . GLU B 2 96  ? 23.710  -1.441  30.270  1.00 38.14 ? 96   GLU B CB  1 
ATOM   3004 C  CG  . GLU B 2 96  ? 24.353  -2.360  31.303  1.00 44.32 ? 96   GLU B CG  1 
ATOM   3005 C  CD  . GLU B 2 96  ? 24.067  -3.840  31.052  1.00 52.38 ? 96   GLU B CD  1 
ATOM   3006 O  OE1 . GLU B 2 96  ? 23.807  -4.214  29.885  1.00 50.50 ? 96   GLU B OE1 1 
ATOM   3007 O  OE2 . GLU B 2 96  ? 24.110  -4.632  32.021  1.00 49.99 ? 96   GLU B OE2 1 
ATOM   3008 N  N   . GLY B 2 97  ? 20.445  -0.737  29.181  1.00 37.09 ? 97   GLY B N   1 
ATOM   3009 C  CA  . GLY B 2 97  ? 19.615  -0.093  28.180  1.00 34.78 ? 97   GLY B CA  1 
ATOM   3010 C  C   . GLY B 2 97  ? 20.116  -0.259  26.754  1.00 33.40 ? 97   GLY B C   1 
ATOM   3011 O  O   . GLY B 2 97  ? 21.013  -1.041  26.449  1.00 34.99 ? 97   GLY B O   1 
ATOM   3012 N  N   . VAL B 2 98  ? 19.501  0.518   25.866  1.00 32.75 ? 98   VAL B N   1 
ATOM   3013 C  CA  . VAL B 2 98  ? 19.736  0.421   24.431  1.00 30.90 ? 98   VAL B CA  1 
ATOM   3014 C  C   . VAL B 2 98  ? 20.022  1.816   23.902  1.00 31.54 ? 98   VAL B C   1 
ATOM   3015 O  O   . VAL B 2 98  ? 19.259  2.748   24.171  1.00 31.58 ? 98   VAL B O   1 
ATOM   3016 C  CB  . VAL B 2 98  ? 18.528  -0.199  23.703  1.00 29.42 ? 98   VAL B CB  1 
ATOM   3017 C  CG1 . VAL B 2 98  ? 18.739  -0.188  22.192  1.00 27.45 ? 98   VAL B CG1 1 
ATOM   3018 C  CG2 . VAL B 2 98  ? 18.260  -1.616  24.213  1.00 30.26 ? 98   VAL B CG2 1 
ATOM   3019 N  N   . LYS B 2 99  ? 21.106  1.959   23.145  1.00 28.80 ? 99   LYS B N   1 
ATOM   3020 C  CA  . LYS B 2 99  ? 21.450  3.263   22.597  1.00 32.54 ? 99   LYS B CA  1 
ATOM   3021 C  C   . LYS B 2 99  ? 20.364  3.751   21.642  1.00 36.87 ? 99   LYS B C   1 
ATOM   3022 O  O   . LYS B 2 99  ? 19.886  3.002   20.780  1.00 34.77 ? 99   LYS B O   1 
ATOM   3023 C  CB  . LYS B 2 99  ? 22.800  3.205   21.880  1.00 32.58 ? 99   LYS B CB  1 
ATOM   3024 C  CG  . LYS B 2 99  ? 23.343  4.587   21.525  1.00 38.27 ? 99   LYS B CG  1 
ATOM   3025 C  CD  . LYS B 2 99  ? 24.834  4.537   21.218  1.00 45.38 ? 99   LYS B CD  1 
ATOM   3026 C  CE  . LYS B 2 99  ? 25.295  5.804   20.530  1.00 41.02 ? 99   LYS B CE  1 
ATOM   3027 N  N   . VAL B 2 100 ? 19.983  5.016   21.805  1.00 33.08 ? 100  VAL B N   1 
ATOM   3028 C  CA  . VAL B 2 100 ? 18.956  5.669   21.000  1.00 33.82 ? 100  VAL B CA  1 
ATOM   3029 C  C   . VAL B 2 100 ? 19.658  6.519   19.949  1.00 32.15 ? 100  VAL B C   1 
ATOM   3030 O  O   . VAL B 2 100 ? 20.301  7.521   20.278  1.00 32.09 ? 100  VAL B O   1 
ATOM   3031 C  CB  . VAL B 2 100 ? 18.030  6.528   21.874  1.00 29.00 ? 100  VAL B CB  1 
ATOM   3032 C  CG1 . VAL B 2 100 ? 17.021  7.310   21.015  1.00 26.91 ? 100  VAL B CG1 1 
ATOM   3033 C  CG2 . VAL B 2 100 ? 17.324  5.655   22.888  1.00 28.70 ? 100  VAL B CG2 1 
ATOM   3034 N  N   . ASN B 2 101 ? 19.544  6.128   18.681  1.00 27.98 ? 101  ASN B N   1 
ATOM   3035 C  CA  . ASN B 2 101 ? 20.118  6.917   17.595  1.00 32.86 ? 101  ASN B CA  1 
ATOM   3036 C  C   . ASN B 2 101 ? 19.089  7.766   16.869  1.00 29.62 ? 101  ASN B C   1 
ATOM   3037 O  O   . ASN B 2 101 ? 19.465  8.721   16.188  1.00 32.07 ? 101  ASN B O   1 
ATOM   3038 C  CB  . ASN B 2 101 ? 20.813  6.015   16.563  1.00 32.27 ? 101  ASN B CB  1 
ATOM   3039 C  CG  . ASN B 2 101 ? 21.951  5.224   17.157  1.00 36.72 ? 101  ASN B CG  1 
ATOM   3040 O  OD1 . ASN B 2 101 ? 22.840  5.786   17.797  1.00 37.59 ? 101  ASN B OD1 1 
ATOM   3041 N  ND2 . ASN B 2 101 ? 21.916  3.903   16.975  1.00 37.34 ? 101  ASN B ND2 1 
ATOM   3042 N  N   . LYS B 2 102 ? 17.810  7.432   16.980  1.00 25.95 ? 102  LYS B N   1 
ATOM   3043 C  CA  . LYS B 2 102 ? 16.774  8.156   16.268  1.00 25.52 ? 102  LYS B CA  1 
ATOM   3044 C  C   . LYS B 2 102 ? 15.583  8.334   17.194  1.00 25.58 ? 102  LYS B C   1 
ATOM   3045 O  O   . LYS B 2 102 ? 15.368  7.537   18.111  1.00 23.87 ? 102  LYS B O   1 
ATOM   3046 C  CB  . LYS B 2 102 ? 16.373  7.421   14.971  1.00 23.90 ? 102  LYS B CB  1 
ATOM   3047 C  CG  . LYS B 2 102 ? 17.514  7.337   13.951  1.00 27.26 ? 102  LYS B CG  1 
ATOM   3048 C  CD  . LYS B 2 102 ? 17.149  6.601   12.674  1.00 30.49 ? 102  LYS B CD  1 
ATOM   3049 C  CE  . LYS B 2 102 ? 18.309  6.652   11.675  1.00 34.26 ? 102  LYS B CE  1 
ATOM   3050 N  NZ  . LYS B 2 102 ? 17.973  5.975   10.389  1.00 43.62 ? 102  LYS B NZ  1 
ATOM   3051 N  N   . VAL B 2 103 ? 14.828  9.404   16.967  1.00 27.65 ? 103  VAL B N   1 
ATOM   3052 C  CA  . VAL B 2 103 ? 13.556  9.590   17.647  1.00 24.43 ? 103  VAL B CA  1 
ATOM   3053 C  C   . VAL B 2 103 ? 12.475  9.791   16.595  1.00 21.28 ? 103  VAL B C   1 
ATOM   3054 O  O   . VAL B 2 103 ? 12.715  10.349  15.520  1.00 21.81 ? 103  VAL B O   1 
ATOM   3055 C  CB  . VAL B 2 103 ? 13.583  10.769  18.645  1.00 22.93 ? 103  VAL B CB  1 
ATOM   3056 C  CG1 . VAL B 2 103 ? 14.644  10.542  19.713  1.00 24.14 ? 103  VAL B CG1 1 
ATOM   3057 C  CG2 . VAL B 2 103 ? 13.825  12.084  17.916  1.00 26.82 ? 103  VAL B CG2 1 
ATOM   3058 N  N   . MET B 2 104 ? 11.280  9.309   16.901  1.00 19.96 ? 104  MET B N   1 
ATOM   3059 C  CA  . MET B 2 104 ? 10.117  9.611   16.088  1.00 18.44 ? 104  MET B CA  1 
ATOM   3060 C  C   . MET B 2 104 ? 9.420   10.835  16.675  1.00 20.19 ? 104  MET B C   1 
ATOM   3061 O  O   . MET B 2 104 ? 9.220   10.918  17.885  1.00 20.12 ? 104  MET B O   1 
ATOM   3062 C  CB  . MET B 2 104 ? 9.160   8.423   16.030  1.00 20.20 ? 104  MET B CB  1 
ATOM   3063 C  CG  . MET B 2 104 ? 7.839   8.736   15.345  1.00 20.71 ? 104  MET B CG  1 
ATOM   3064 S  SD  . MET B 2 104 ? 6.692   7.334   15.269  1.00 25.86 ? 104  MET B SD  1 
ATOM   3065 C  CE  . MET B 2 104 ? 7.652   6.195   14.301  1.00 21.00 ? 104  MET B CE  1 
ATOM   3066 N  N   . VAL B 2 105 ? 9.077   11.784  15.815  1.00 19.33 ? 105  VAL B N   1 
ATOM   3067 C  CA  . VAL B 2 105 ? 8.268   12.946  16.168  1.00 20.98 ? 105  VAL B CA  1 
ATOM   3068 C  C   . VAL B 2 105 ? 6.956   12.789  15.417  1.00 17.30 ? 105  VAL B C   1 
ATOM   3069 O  O   . VAL B 2 105 ? 6.935   12.872  14.182  1.00 23.93 ? 105  VAL B O   1 
ATOM   3070 C  CB  . VAL B 2 105 ? 8.985   14.255  15.795  1.00 21.79 ? 105  VAL B CB  1 
ATOM   3071 C  CG1 . VAL B 2 105 ? 8.170   15.471  16.182  1.00 17.91 ? 105  VAL B CG1 1 
ATOM   3072 C  CG2 . VAL B 2 105 ? 10.377  14.295  16.424  1.00 23.17 ? 105  VAL B CG2 1 
ATOM   3073 N  N   . ALA B 2 106 ? 5.863   12.546  16.134  1.00 18.78 ? 106  ALA B N   1 
ATOM   3074 C  CA  . ALA B 2 106 ? 4.599   12.187  15.504  1.00 19.43 ? 106  ALA B CA  1 
ATOM   3075 C  C   . ALA B 2 106 ? 3.452   13.036  16.043  1.00 25.07 ? 106  ALA B C   1 
ATOM   3076 O  O   . ALA B 2 106 ? 3.490   13.542  17.170  1.00 23.78 ? 106  ALA B O   1 
ATOM   3077 C  CB  . ALA B 2 106 ? 4.260   10.698  15.722  1.00 20.82 ? 106  ALA B CB  1 
ATOM   3078 N  N   . GLU B 2 107 ? 2.406   13.166  15.230  1.00 21.49 ? 107  GLU B N   1 
ATOM   3079 C  CA  . GLU B 2 107 ? 1.178   13.763  15.732  1.00 20.45 ? 107  GLU B CA  1 
ATOM   3080 C  C   . GLU B 2 107 ? 0.602   12.870  16.814  1.00 26.48 ? 107  GLU B C   1 
ATOM   3081 O  O   . GLU B 2 107 ? 0.448   11.657  16.629  1.00 25.53 ? 107  GLU B O   1 
ATOM   3082 C  CB  . GLU B 2 107 ? 0.149   13.977  14.611  1.00 27.85 ? 107  GLU B CB  1 
ATOM   3083 C  CG  . GLU B 2 107 ? -0.274  12.726  13.860  1.00 30.08 ? 107  GLU B CG  1 
ATOM   3084 C  CD  . GLU B 2 107 ? -1.447  12.966  12.921  1.00 40.38 ? 107  GLU B CD  1 
ATOM   3085 O  OE1 . GLU B 2 107 ? -1.806  12.005  12.199  1.00 24.99 ? 107  GLU B OE1 1 
ATOM   3086 O  OE2 . GLU B 2 107 ? -2.001  14.108  12.909  1.00 36.78 ? 107  GLU B OE2 1 
ATOM   3087 N  N   . ALA B 2 108 ? 0.329   13.463  17.968  1.00 21.73 ? 108  ALA B N   1 
ATOM   3088 C  CA  . ALA B 2 108 ? -0.327  12.731  19.039  1.00 26.26 ? 108  ALA B CA  1 
ATOM   3089 C  C   . ALA B 2 108 ? -1.824  12.767  18.781  1.00 29.69 ? 108  ALA B C   1 
ATOM   3090 O  O   . ALA B 2 108 ? -2.406  13.848  18.622  1.00 28.64 ? 108  ALA B O   1 
ATOM   3091 C  CB  . ALA B 2 108 ? 0.017   13.331  20.399  1.00 21.02 ? 108  ALA B CB  1 
ATOM   3092 N  N   . LEU B 2 109 ? -2.431  11.592  18.693  1.00 26.80 ? 109  LEU B N   1 
ATOM   3093 C  CA  . LEU B 2 109 ? -3.857  11.444  18.452  1.00 31.21 ? 109  LEU B CA  1 
ATOM   3094 C  C   . LEU B 2 109 ? -4.489  10.812  19.684  1.00 29.65 ? 109  LEU B C   1 
ATOM   3095 O  O   . LEU B 2 109 ? -3.964  9.829   20.212  1.00 31.00 ? 109  LEU B O   1 
ATOM   3096 C  CB  . LEU B 2 109 ? -4.119  10.571  17.213  1.00 29.38 ? 109  LEU B CB  1 
ATOM   3097 C  CG  . LEU B 2 109 ? -3.565  10.986  15.847  1.00 30.05 ? 109  LEU B CG  1 
ATOM   3098 C  CD1 . LEU B 2 109 ? -3.617  9.819   14.864  1.00 27.78 ? 109  LEU B CD1 1 
ATOM   3099 C  CD2 . LEU B 2 109 ? -4.320  12.175  15.279  1.00 29.42 ? 109  LEU B CD2 1 
ATOM   3100 N  N   . ASP B 2 110 ? -5.593  11.383  20.152  1.00 31.87 ? 110  ASP B N   1 
ATOM   3101 C  CA  . ASP B 2 110 ? -6.360  10.737  21.206  1.00 35.88 ? 110  ASP B CA  1 
ATOM   3102 C  C   . ASP B 2 110 ? -6.993  9.464   20.669  1.00 35.81 ? 110  ASP B C   1 
ATOM   3103 O  O   . ASP B 2 110 ? -7.310  9.354   19.484  1.00 36.14 ? 110  ASP B O   1 
ATOM   3104 C  CB  . ASP B 2 110 ? -7.458  11.658  21.735  1.00 36.42 ? 110  ASP B CB  1 
ATOM   3105 C  CG  . ASP B 2 110 ? -6.912  12.909  22.380  1.00 44.74 ? 110  ASP B CG  1 
ATOM   3106 O  OD1 . ASP B 2 110 ? -5.847  12.831  23.023  1.00 41.92 ? 110  ASP B OD1 1 
ATOM   3107 O  OD2 . ASP B 2 110 ? -7.557  13.970  22.249  1.00 46.77 ? 110  ASP B OD2 1 
ATOM   3108 N  N   . ILE B 2 111 ? -7.192  8.496   21.550  1.00 37.33 ? 111  ILE B N   1 
ATOM   3109 C  CA  . ILE B 2 111 ? -7.870  7.266   21.183  1.00 36.31 ? 111  ILE B CA  1 
ATOM   3110 C  C   . ILE B 2 111 ? -9.149  7.165   21.996  1.00 34.02 ? 111  ILE B C   1 
ATOM   3111 O  O   . ILE B 2 111 ? -9.121  7.282   23.225  1.00 35.73 ? 111  ILE B O   1 
ATOM   3112 C  CB  . ILE B 2 111 ? -6.965  6.039   21.388  1.00 37.25 ? 111  ILE B CB  1 
ATOM   3113 C  CG1 . ILE B 2 111 ? -7.692  4.765   20.969  1.00 35.75 ? 111  ILE B CG1 1 
ATOM   3114 C  CG2 . ILE B 2 111 ? -6.431  5.971   22.825  1.00 36.17 ? 111  ILE B CG2 1 
ATOM   3115 C  CD1 . ILE B 2 111 ? -6.733  3.685   20.514  1.00 34.76 ? 111  ILE B CD1 1 
ATOM   3116 N  N   . SER B 2 112 ? -10.270 6.974   21.303  1.00 38.75 ? 112  SER B N   1 
ATOM   3117 C  CA  . SER B 2 112 ? -11.551 6.805   21.980  1.00 38.53 ? 112  SER B CA  1 
ATOM   3118 C  C   . SER B 2 112 ? -11.736 5.375   22.463  1.00 46.30 ? 112  SER B C   1 
ATOM   3119 O  O   . SER B 2 112 ? -12.176 5.150   23.597  1.00 46.76 ? 112  SER B O   1 
ATOM   3120 C  CB  . SER B 2 112 ? -12.694 7.185   21.044  1.00 42.02 ? 112  SER B CB  1 
ATOM   3121 O  OG  . SER B 2 112 ? -12.411 8.398   20.387  1.00 44.53 ? 112  SER B OG  1 
ATOM   3122 N  N   . ARG B 2 113 ? -11.404 4.400   21.622  1.00 39.50 ? 113  ARG B N   1 
ATOM   3123 C  CA  . ARG B 2 113 ? -11.526 3.004   21.999  1.00 39.08 ? 113  ARG B CA  1 
ATOM   3124 C  C   . ARG B 2 113 ? -10.374 2.206   21.409  1.00 36.36 ? 113  ARG B C   1 
ATOM   3125 O  O   . ARG B 2 113 ? -9.919  2.482   20.297  1.00 37.02 ? 113  ARG B O   1 
ATOM   3126 C  CB  . ARG B 2 113 ? -12.854 2.430   21.529  1.00 38.72 ? 113  ARG B CB  1 
ATOM   3127 C  CG  . ARG B 2 113 ? -13.362 1.265   22.355  1.00 38.28 ? 113  ARG B CG  1 
ATOM   3128 C  CD  . ARG B 2 113 ? -14.784 0.960   21.921  1.00 42.12 ? 113  ARG B CD  1 
ATOM   3129 N  NE  . ARG B 2 113 ? -14.918 1.182   20.483  1.00 47.03 ? 113  ARG B NE  1 
ATOM   3130 C  CZ  . ARG B 2 113 ? -14.771 0.230   19.570  1.00 43.64 ? 113  ARG B CZ  1 
ATOM   3131 N  NH1 . ARG B 2 113 ? -14.512 -1.014  19.955  1.00 38.86 ? 113  ARG B NH1 1 
ATOM   3132 N  NH2 . ARG B 2 113 ? -14.901 0.517   18.282  1.00 42.95 ? 113  ARG B NH2 1 
ATOM   3133 N  N   . GLU B 2 114 ? -9.919  1.213   22.164  1.00 33.99 ? 114  GLU B N   1 
ATOM   3134 C  CA  . GLU B 2 114 ? -8.794  0.369   21.799  1.00 30.26 ? 114  GLU B CA  1 
ATOM   3135 C  C   . GLU B 2 114 ? -9.289  -1.024  21.449  1.00 31.33 ? 114  GLU B C   1 
ATOM   3136 O  O   . GLU B 2 114 ? -9.987  -1.659  22.248  1.00 32.82 ? 114  GLU B O   1 
ATOM   3137 C  CB  . GLU B 2 114 ? -7.782  0.280   22.944  1.00 30.27 ? 114  GLU B CB  1 
ATOM   3138 C  CG  . GLU B 2 114 ? -6.933  1.515   23.126  1.00 32.82 ? 114  GLU B CG  1 
ATOM   3139 C  CD  . GLU B 2 114 ? -6.045  1.421   24.335  1.00 37.97 ? 114  GLU B CD  1 
ATOM   3140 O  OE1 . GLU B 2 114 ? -6.529  1.729   25.443  1.00 50.60 ? 114  GLU B OE1 1 
ATOM   3141 O  OE2 . GLU B 2 114 ? -4.877  1.014   24.189  1.00 42.16 ? 114  GLU B OE2 1 
ATOM   3142 N  N   . THR B 2 115 ? -8.919  -1.498  20.269  1.00 25.88 ? 115  THR B N   1 
ATOM   3143 C  CA  . THR B 2 115 ? -9.200  -2.860  19.849  1.00 24.52 ? 115  THR B CA  1 
ATOM   3144 C  C   . THR B 2 115 ? -7.897  -3.532  19.440  1.00 26.91 ? 115  THR B C   1 
ATOM   3145 O  O   . THR B 2 115 ? -6.849  -2.890  19.287  1.00 22.76 ? 115  THR B O   1 
ATOM   3146 C  CB  . THR B 2 115 ? -10.213 -2.906  18.691  1.00 28.48 ? 115  THR B CB  1 
ATOM   3147 O  OG1 . THR B 2 115 ? -9.636  -2.330  17.507  1.00 28.30 ? 115  THR B OG1 1 
ATOM   3148 C  CG2 . THR B 2 115 ? -11.499 -2.151  19.054  1.00 30.59 ? 115  THR B CG2 1 
ATOM   3149 N  N   . TYR B 2 116 ? -7.980  -4.842  19.263  1.00 25.06 ? 116  TYR B N   1 
ATOM   3150 C  CA  . TYR B 2 116 ? -6.877  -5.653  18.769  1.00 24.72 ? 116  TYR B CA  1 
ATOM   3151 C  C   . TYR B 2 116 ? -7.210  -6.145  17.366  1.00 22.99 ? 116  TYR B C   1 
ATOM   3152 O  O   . TYR B 2 116 ? -8.343  -6.548  17.093  1.00 23.37 ? 116  TYR B O   1 
ATOM   3153 C  CB  . TYR B 2 116 ? -6.621  -6.838  19.710  1.00 23.03 ? 116  TYR B CB  1 
ATOM   3154 C  CG  . TYR B 2 116 ? -5.524  -7.788  19.271  1.00 24.48 ? 116  TYR B CG  1 
ATOM   3155 C  CD1 . TYR B 2 116 ? -5.793  -8.840  18.398  1.00 24.48 ? 116  TYR B CD1 1 
ATOM   3156 C  CD2 . TYR B 2 116 ? -4.225  -7.642  19.741  1.00 23.36 ? 116  TYR B CD2 1 
ATOM   3157 C  CE1 . TYR B 2 116 ? -4.797  -9.715  17.997  1.00 23.54 ? 116  TYR B CE1 1 
ATOM   3158 C  CE2 . TYR B 2 116 ? -3.225  -8.514  19.350  1.00 24.57 ? 116  TYR B CE2 1 
ATOM   3159 C  CZ  . TYR B 2 116 ? -3.525  -9.555  18.476  1.00 22.57 ? 116  TYR B CZ  1 
ATOM   3160 O  OH  . TYR B 2 116 ? -2.532  -10.420 18.078  1.00 25.23 ? 116  TYR B OH  1 
ATOM   3161 N  N   . LEU B 2 117 ? -6.226  -6.105  16.468  1.00 23.04 ? 117  LEU B N   1 
ATOM   3162 C  CA  . LEU B 2 117 ? -6.449  -6.642  15.130  1.00 19.97 ? 117  LEU B CA  1 
ATOM   3163 C  C   . LEU B 2 117 ? -5.143  -7.176  14.558  1.00 22.15 ? 117  LEU B C   1 
ATOM   3164 O  O   . LEU B 2 117 ? -4.161  -6.434  14.434  1.00 18.54 ? 117  LEU B O   1 
ATOM   3165 C  CB  . LEU B 2 117 ? -7.038  -5.600  14.189  1.00 18.10 ? 117  LEU B CB  1 
ATOM   3166 C  CG  . LEU B 2 117 ? -7.198  -6.359  12.880  1.00 21.56 ? 117  LEU B CG  1 
ATOM   3167 C  CD1 . LEU B 2 117 ? -8.445  -7.211  12.944  1.00 19.72 ? 117  LEU B CD1 1 
ATOM   3168 C  CD2 . LEU B 2 117 ? -7.165  -5.476  11.683  1.00 26.32 ? 117  LEU B CD2 1 
ATOM   3169 N  N   . ALA B 2 118 ? -5.139  -8.458  14.199  1.00 18.81 ? 118  ALA B N   1 
ATOM   3170 C  CA  . ALA B 2 118 ? -3.970  -9.070  13.592  1.00 17.76 ? 118  ALA B CA  1 
ATOM   3171 C  C   . ALA B 2 118 ? -4.393  -9.939  12.411  1.00 22.17 ? 118  ALA B C   1 
ATOM   3172 O  O   . ALA B 2 118 ? -5.549  -10.352 12.288  1.00 18.11 ? 118  ALA B O   1 
ATOM   3173 C  CB  . ALA B 2 118 ? -3.171  -9.889  14.615  1.00 16.07 ? 118  ALA B CB  1 
ATOM   3174 N  N   . ILE B 2 119 ? -3.434  -10.179 11.520  1.00 18.53 ? 119  ILE B N   1 
ATOM   3175 C  CA  . ILE B 2 119 ? -3.531  -11.185 10.472  1.00 16.84 ? 119  ILE B CA  1 
ATOM   3176 C  C   . ILE B 2 119 ? -2.322  -12.088 10.650  1.00 19.71 ? 119  ILE B C   1 
ATOM   3177 O  O   . ILE B 2 119 ? -1.208  -11.594 10.857  1.00 18.23 ? 119  ILE B O   1 
ATOM   3178 C  CB  . ILE B 2 119 ? -3.556  -10.543 9.066   1.00 20.40 ? 119  ILE B CB  1 
ATOM   3179 C  CG1 . ILE B 2 119 ? -4.695  -9.530  8.975   1.00 21.75 ? 119  ILE B CG1 1 
ATOM   3180 C  CG2 . ILE B 2 119 ? -3.703  -11.604 7.960   1.00 20.48 ? 119  ILE B CG2 1 
ATOM   3181 C  CD1 . ILE B 2 119 ? -4.287  -8.226  8.408   1.00 27.32 ? 119  ILE B CD1 1 
ATOM   3182 N  N   . LEU B 2 120 ? -2.538  -13.400 10.627  1.00 17.51 ? 120  LEU B N   1 
ATOM   3183 C  CA  . LEU B 2 120 ? -1.427  -14.321 10.810  1.00 17.84 ? 120  LEU B CA  1 
ATOM   3184 C  C   . LEU B 2 120 ? -1.612  -15.529 9.914   1.00 17.59 ? 120  LEU B C   1 
ATOM   3185 O  O   . LEU B 2 120 ? -2.731  -15.870 9.535   1.00 18.38 ? 120  LEU B O   1 
ATOM   3186 C  CB  . LEU B 2 120 ? -1.280  -14.779 12.267  1.00 21.50 ? 120  LEU B CB  1 
ATOM   3187 C  CG  . LEU B 2 120 ? -2.108  -15.972 12.733  1.00 20.09 ? 120  LEU B CG  1 
ATOM   3188 C  CD1 . LEU B 2 120 ? -1.544  -16.539 14.006  1.00 26.48 ? 120  LEU B CD1 1 
ATOM   3189 C  CD2 . LEU B 2 120 ? -3.527  -15.550 12.953  1.00 27.56 ? 120  LEU B CD2 1 
ATOM   3190 N  N   . MET B 2 121 ? -0.487  -16.139 9.542   1.00 20.20 ? 121  MET B N   1 
ATOM   3191 C  CA  . MET B 2 121 ? -0.487  -17.457 8.927   1.00 21.27 ? 121  MET B CA  1 
ATOM   3192 C  C   . MET B 2 121 ? -0.712  -18.452 10.048  1.00 22.06 ? 121  MET B C   1 
ATOM   3193 O  O   . MET B 2 121 ? 0.178   -18.674 10.874  1.00 23.21 ? 121  MET B O   1 
ATOM   3194 C  CB  . MET B 2 121 ? 0.834   -17.748 8.218   1.00 24.15 ? 121  MET B CB  1 
ATOM   3195 C  CG  . MET B 2 121 ? 1.040   -16.970 6.956   1.00 23.95 ? 121  MET B CG  1 
ATOM   3196 S  SD  . MET B 2 121 ? -0.221  -17.287 5.706   1.00 21.28 ? 121  MET B SD  1 
ATOM   3197 C  CE  . MET B 2 121 ? 0.498   -16.323 4.374   1.00 20.84 ? 121  MET B CE  1 
ATOM   3198 N  N   . ASP B 2 122 ? -1.898  -19.018 10.109  1.00 16.66 ? 122  ASP B N   1 
ATOM   3199 C  CA  . ASP B 2 122 ? -2.274  -19.873 11.223  1.00 20.49 ? 122  ASP B CA  1 
ATOM   3200 C  C   . ASP B 2 122 ? -2.109  -21.325 10.790  1.00 19.52 ? 122  ASP B C   1 
ATOM   3201 O  O   . ASP B 2 122 ? -2.818  -21.793 9.891   1.00 20.60 ? 122  ASP B O   1 
ATOM   3202 C  CB  . ASP B 2 122 ? -3.701  -19.554 11.654  1.00 20.09 ? 122  ASP B CB  1 
ATOM   3203 C  CG  . ASP B 2 122 ? -4.098  -20.270 12.917  1.00 26.52 ? 122  ASP B CG  1 
ATOM   3204 O  OD1 . ASP B 2 122 ? -3.305  -21.099 13.426  1.00 36.15 ? 122  ASP B OD1 1 
ATOM   3205 O  OD2 . ASP B 2 122 ? -5.206  -20.006 13.405  1.00 23.42 ? 122  ASP B OD2 1 
ATOM   3206 N  N   . ARG B 2 123 ? -1.156  -22.028 11.418  1.00 18.43 ? 123  ARG B N   1 
ATOM   3207 C  CA  . ARG B 2 123 ? -0.897  -23.426 11.073  1.00 18.14 ? 123  ARG B CA  1 
ATOM   3208 C  C   . ARG B 2 123 ? -2.145  -24.270 11.246  1.00 21.31 ? 123  ARG B C   1 
ATOM   3209 O  O   . ARG B 2 123 ? -2.385  -25.194 10.465  1.00 19.66 ? 123  ARG B O   1 
ATOM   3210 C  CB  . ARG B 2 123 ? 0.227   -24.019 11.940  1.00 25.01 ? 123  ARG B CB  1 
ATOM   3211 C  CG  . ARG B 2 123 ? 1.182   -23.023 12.564  1.00 30.54 ? 123  ARG B CG  1 
ATOM   3212 C  CD  . ARG B 2 123 ? 1.943   -23.627 13.758  1.00 27.20 ? 123  ARG B CD  1 
ATOM   3213 N  NE  . ARG B 2 123 ? 2.658   -24.854 13.398  1.00 24.19 ? 123  ARG B NE  1 
ATOM   3214 C  CZ  . ARG B 2 123 ? 3.813   -25.226 13.944  1.00 29.22 ? 123  ARG B CZ  1 
ATOM   3215 N  NH1 . ARG B 2 123 ? 4.386   -24.447 14.855  1.00 28.68 ? 123  ARG B NH1 1 
ATOM   3216 N  NH2 . ARG B 2 123 ? 4.403   -26.362 13.567  1.00 22.43 ? 123  ARG B NH2 1 
ATOM   3217 N  N   . SER B 2 124 ? -2.948  -23.966 12.273  1.00 20.10 ? 124  SER B N   1 
ATOM   3218 C  CA  . SER B 2 124 ? -4.126  -24.773 12.568  1.00 22.82 ? 124  SER B CA  1 
ATOM   3219 C  C   . SER B 2 124 ? -5.119  -24.722 11.426  1.00 23.24 ? 124  SER B C   1 
ATOM   3220 O  O   . SER B 2 124 ? -5.774  -25.724 11.127  1.00 26.73 ? 124  SER B O   1 
ATOM   3221 C  CB  . SER B 2 124 ? -4.794  -24.296 13.856  1.00 22.57 ? 124  SER B CB  1 
ATOM   3222 O  OG  . SER B 2 124 ? -3.971  -24.545 14.973  1.00 34.51 ? 124  SER B OG  1 
ATOM   3223 N  N   . CYS B 2 125 ? -5.223  -23.570 10.761  1.00 20.45 ? 125  CYS B N   1 
ATOM   3224 C  CA  . CYS B 2 125 ? -6.256  -23.311 9.767   1.00 21.29 ? 125  CYS B CA  1 
ATOM   3225 C  C   . CYS B 2 125 ? -5.779  -23.444 8.328   1.00 22.60 ? 125  CYS B C   1 
ATOM   3226 O  O   . CYS B 2 125 ? -6.551  -23.139 7.415   1.00 27.97 ? 125  CYS B O   1 
ATOM   3227 C  CB  . CYS B 2 125 ? -6.836  -21.909 9.974   1.00 22.29 ? 125  CYS B CB  1 
ATOM   3228 S  SG  . CYS B 2 125 ? -7.782  -21.717 11.507  1.00 22.36 ? 125  CYS B SG  1 
ATOM   3229 N  N   . ASN B 2 126 ? -4.538  -23.875 8.097   1.00 22.65 ? 126  ASN B N   1 
ATOM   3230 C  CA  . ASN B 2 126 ? -3.966  -24.039 6.754   1.00 17.60 ? 126  ASN B CA  1 
ATOM   3231 C  C   . ASN B 2 126 ? -3.856  -22.722 5.967   1.00 22.17 ? 126  ASN B C   1 
ATOM   3232 O  O   . ASN B 2 126 ? -3.730  -22.752 4.735   1.00 19.36 ? 126  ASN B O   1 
ATOM   3233 C  CB  . ASN B 2 126 ? -4.767  -25.035 5.899   1.00 25.75 ? 126  ASN B CB  1 
ATOM   3234 C  CG  . ASN B 2 126 ? -5.173  -26.269 6.643   1.00 25.55 ? 126  ASN B CG  1 
ATOM   3235 O  OD1 . ASN B 2 126 ? -4.378  -26.878 7.341   1.00 25.41 ? 126  ASN B OD1 1 
ATOM   3236 N  ND2 . ASN B 2 126 ? -6.427  -26.668 6.472   1.00 31.45 ? 126  ASN B ND2 1 
ATOM   3237 N  N   . GLY B 2 127 ? -3.908  -21.547 6.604   1.00 19.41 ? 127  GLY B N   1 
ATOM   3238 C  CA  . GLY B 2 127 ? -3.819  -20.313 5.851   1.00 16.83 ? 127  GLY B CA  1 
ATOM   3239 C  C   . GLY B 2 127 ? -3.971  -19.056 6.686   1.00 18.62 ? 127  GLY B C   1 
ATOM   3240 O  O   . GLY B 2 127 ? -3.908  -19.096 7.920   1.00 19.99 ? 127  GLY B O   1 
ATOM   3241 N  N   . PRO B 2 128 ? -4.164  -17.908 6.029   1.00 20.53 ? 128  PRO B N   1 
ATOM   3242 C  CA  . PRO B 2 128 ? -4.283  -16.649 6.779   1.00 16.44 ? 128  PRO B CA  1 
ATOM   3243 C  C   . PRO B 2 128 ? -5.603  -16.583 7.524   1.00 19.38 ? 128  PRO B C   1 
ATOM   3244 O  O   . PRO B 2 128 ? -6.643  -17.041 7.039   1.00 15.84 ? 128  PRO B O   1 
ATOM   3245 C  CB  . PRO B 2 128 ? -4.205  -15.567 5.698   1.00 17.09 ? 128  PRO B CB  1 
ATOM   3246 C  CG  . PRO B 2 128 ? -3.830  -16.266 4.430   1.00 20.88 ? 128  PRO B CG  1 
ATOM   3247 C  CD  . PRO B 2 128 ? -4.268  -17.691 4.580   1.00 18.39 ? 128  PRO B CD  1 
ATOM   3248 N  N   . VAL B 2 129 ? -5.555  -16.028 8.730   1.00 22.53 ? 129  VAL B N   1 
ATOM   3249 C  CA  . VAL B 2 129 ? -6.776  -15.772 9.482   1.00 18.05 ? 129  VAL B CA  1 
ATOM   3250 C  C   . VAL B 2 129 ? -6.683  -14.393 10.120  1.00 19.63 ? 129  VAL B C   1 
ATOM   3251 O  O   . VAL B 2 129 ? -5.605  -13.961 10.550  1.00 19.71 ? 129  VAL B O   1 
ATOM   3252 C  CB  . VAL B 2 129 ? -7.077  -16.885 10.525  1.00 21.24 ? 129  VAL B CB  1 
ATOM   3253 C  CG1 . VAL B 2 129 ? -6.452  -18.225 10.138  1.00 19.07 ? 129  VAL B CG1 1 
ATOM   3254 C  CG2 . VAL B 2 129 ? -6.737  -16.483 11.949  1.00 26.47 ? 129  VAL B CG2 1 
ATOM   3255 N  N   . LEU B 2 130 ? -7.806  -13.677 10.124  1.00 20.99 ? 130  LEU B N   1 
ATOM   3256 C  CA  . LEU B 2 130 ? -7.909  -12.433 10.879  1.00 17.34 ? 130  LEU B CA  1 
ATOM   3257 C  C   . LEU B 2 130 ? -8.234  -12.749 12.325  1.00 21.18 ? 130  LEU B C   1 
ATOM   3258 O  O   . LEU B 2 130 ? -9.089  -13.591 12.606  1.00 23.58 ? 130  LEU B O   1 
ATOM   3259 C  CB  . LEU B 2 130 ? -9.005  -11.521 10.331  1.00 20.62 ? 130  LEU B CB  1 
ATOM   3260 C  CG  . LEU B 2 130 ? -9.177  -11.226 8.858   1.00 22.59 ? 130  LEU B CG  1 
ATOM   3261 C  CD1 . LEU B 2 130 ? -10.312 -10.212 8.700   1.00 23.94 ? 130  LEU B CD1 1 
ATOM   3262 C  CD2 . LEU B 2 130 ? -7.878  -10.686 8.293   1.00 25.45 ? 130  LEU B CD2 1 
ATOM   3263 N  N   . VAL B 2 131 ? -7.555  -12.065 13.241  1.00 21.40 ? 131  VAL B N   1 
ATOM   3264 C  CA  . VAL B 2 131 ? -7.741  -12.244 14.672  1.00 23.42 ? 131  VAL B CA  1 
ATOM   3265 C  C   . VAL B 2 131 ? -8.009  -10.869 15.259  1.00 25.34 ? 131  VAL B C   1 
ATOM   3266 O  O   . VAL B 2 131 ? -7.207  -9.947  15.063  1.00 20.43 ? 131  VAL B O   1 
ATOM   3267 C  CB  . VAL B 2 131 ? -6.520  -12.887 15.347  1.00 25.34 ? 131  VAL B CB  1 
ATOM   3268 C  CG1 . VAL B 2 131 ? -6.700  -12.877 16.869  1.00 29.95 ? 131  VAL B CG1 1 
ATOM   3269 C  CG2 . VAL B 2 131 ? -6.322  -14.299 14.837  1.00 23.87 ? 131  VAL B CG2 1 
ATOM   3270 N  N   . GLY B 2 132 ? -9.131  -10.730 15.959  1.00 21.12 ? 132  GLY B N   1 
ATOM   3271 C  CA  . GLY B 2 132 ? -9.566  -9.425  16.431  1.00 24.14 ? 132  GLY B CA  1 
ATOM   3272 C  C   . GLY B 2 132 ? -10.266 -9.523  17.767  1.00 29.85 ? 132  GLY B C   1 
ATOM   3273 O  O   . GLY B 2 132 ? -10.861 -10.553 18.111  1.00 28.79 ? 132  GLY B O   1 
ATOM   3274 N  N   . SER B 2 133 ? -10.197 -8.430  18.528  1.00 23.85 ? 133  SER B N   1 
ATOM   3275 C  CA  . SER B 2 133 ? -10.855 -8.382  19.818  1.00 27.38 ? 133  SER B CA  1 
ATOM   3276 C  C   . SER B 2 133 ? -11.228 -6.946  20.149  1.00 28.75 ? 133  SER B C   1 
ATOM   3277 O  O   . SER B 2 133 ? -10.418 -6.035  19.917  1.00 28.14 ? 133  SER B O   1 
ATOM   3278 C  CB  . SER B 2 133 ? -9.970  -8.948  20.930  1.00 26.86 ? 133  SER B CB  1 
ATOM   3279 O  OG  . SER B 2 133 ? -10.582 -8.759  22.196  1.00 30.13 ? 133  SER B OG  1 
ATOM   3280 N  N   . PRO B 2 134 ? -12.429 -6.708  20.688  1.00 31.72 ? 134  PRO B N   1 
ATOM   3281 C  CA  . PRO B 2 134 ? -12.732 -5.378  21.237  1.00 29.88 ? 134  PRO B CA  1 
ATOM   3282 C  C   . PRO B 2 134 ? -11.894 -5.028  22.452  1.00 25.42 ? 134  PRO B C   1 
ATOM   3283 O  O   . PRO B 2 134 ? -11.872 -3.859  22.849  1.00 26.60 ? 134  PRO B O   1 
ATOM   3284 C  CB  . PRO B 2 134 ? -14.223 -5.471  21.589  1.00 29.76 ? 134  PRO B CB  1 
ATOM   3285 C  CG  . PRO B 2 134 ? -14.465 -6.932  21.812  1.00 30.70 ? 134  PRO B CG  1 
ATOM   3286 C  CD  . PRO B 2 134 ? -13.562 -7.642  20.829  1.00 30.27 ? 134  PRO B CD  1 
ATOM   3287 N  N   . GLN B 2 135 ? -11.207 -5.990  23.060  1.00 26.26 ? 135  GLN B N   1 
ATOM   3288 C  CA  . GLN B 2 135 ? -10.371 -5.709  24.226  1.00 28.45 ? 135  GLN B CA  1 
ATOM   3289 C  C   . GLN B 2 135 ? -8.960  -5.394  23.743  1.00 29.11 ? 135  GLN B C   1 
ATOM   3290 O  O   . GLN B 2 135 ? -8.103  -6.275  23.628  1.00 28.76 ? 135  GLN B O   1 
ATOM   3291 C  CB  . GLN B 2 135 ? -10.389 -6.876  25.202  1.00 29.42 ? 135  GLN B CB  1 
ATOM   3292 C  CG  . GLN B 2 135 ? -9.567  -6.612  26.451  1.00 38.97 ? 135  GLN B CG  1 
ATOM   3293 C  CD  . GLN B 2 135 ? -10.156 -7.260  27.681  1.00 45.15 ? 135  GLN B CD  1 
ATOM   3294 O  OE1 . GLN B 2 135 ? -9.521  -8.106  28.314  1.00 54.59 ? 135  GLN B OE1 1 
ATOM   3295 N  NE2 . GLN B 2 135 ? -11.378 -6.867  28.031  1.00 47.23 ? 135  GLN B NE2 1 
ATOM   3296 N  N   . GLY B 2 136 ? -8.716  -4.097  23.440  1.00 30.49 ? 136  GLY B N   1 
ATOM   3297 C  CA  . GLY B 2 136 ? -7.420  -3.667  22.965  1.00 27.07 ? 136  GLY B CA  1 
ATOM   3298 C  C   . GLY B 2 136 ? -6.493  -3.227  24.076  1.00 31.40 ? 136  GLY B C   1 
ATOM   3299 O  O   . GLY B 2 136 ? -6.937  -2.908  25.175  1.00 33.86 ? 136  GLY B O   1 
ATOM   3300 N  N   . GLY B 2 137 ? -5.193  -3.227  23.774  1.00 23.91 ? 137  GLY B N   1 
ATOM   3301 C  CA  . GLY B 2 137 ? -4.191  -2.719  24.693  1.00 31.62 ? 137  GLY B CA  1 
ATOM   3302 C  C   . GLY B 2 137 ? -3.598  -3.741  25.635  1.00 33.45 ? 137  GLY B C   1 
ATOM   3303 O  O   . GLY B 2 137 ? -2.827  -3.371  26.531  1.00 35.37 ? 137  GLY B O   1 
ATOM   3304 N  N   . VAL B 2 138 ? -3.928  -5.010  25.459  1.00 31.36 ? 138  VAL B N   1 
ATOM   3305 C  CA  . VAL B 2 138 ? -3.482  -6.081  26.334  1.00 31.92 ? 138  VAL B CA  1 
ATOM   3306 C  C   . VAL B 2 138 ? -2.976  -7.200  25.438  1.00 32.90 ? 138  VAL B C   1 
ATOM   3307 O  O   . VAL B 2 138 ? -3.442  -7.364  24.306  1.00 26.60 ? 138  VAL B O   1 
ATOM   3308 C  CB  . VAL B 2 138 ? -4.621  -6.549  27.282  1.00 37.64 ? 138  VAL B CB  1 
ATOM   3309 C  CG1 . VAL B 2 138 ? -5.942  -5.838  26.955  1.00 35.94 ? 138  VAL B CG1 1 
ATOM   3310 C  CG2 . VAL B 2 138 ? -4.821  -8.038  27.231  1.00 38.10 ? 138  VAL B CG2 1 
ATOM   3311 N  N   . ASP B 2 139 ? -1.970  -7.929  25.915  1.00 35.32 ? 139  ASP B N   1 
ATOM   3312 C  CA  . ASP B 2 139 ? -1.438  -9.032  25.126  1.00 34.94 ? 139  ASP B CA  1 
ATOM   3313 C  C   . ASP B 2 139 ? -2.568  -9.978  24.749  1.00 32.31 ? 139  ASP B C   1 
ATOM   3314 O  O   . ASP B 2 139 ? -3.477  -10.232 25.541  1.00 32.43 ? 139  ASP B O   1 
ATOM   3315 C  CB  . ASP B 2 139 ? -0.349  -9.776  25.902  1.00 41.35 ? 139  ASP B CB  1 
ATOM   3316 C  CG  . ASP B 2 139 ? 0.919   -8.959  26.048  1.00 46.66 ? 139  ASP B CG  1 
ATOM   3317 O  OD1 . ASP B 2 139 ? 0.985   -7.849  25.469  1.00 42.94 ? 139  ASP B OD1 1 
ATOM   3318 O  OD2 . ASP B 2 139 ? 1.845   -9.428  26.743  1.00 48.63 ? 139  ASP B OD2 1 
ATOM   3319 N  N   . ILE B 2 140 ? -2.536  -10.458 23.508  1.00 30.11 ? 140  ILE B N   1 
ATOM   3320 C  CA  . ILE B 2 140 ? -3.655  -11.256 23.028  1.00 35.99 ? 140  ILE B CA  1 
ATOM   3321 C  C   . ILE B 2 140 ? -3.784  -12.540 23.849  1.00 31.81 ? 140  ILE B C   1 
ATOM   3322 O  O   . ILE B 2 140 ? -4.897  -12.990 24.139  1.00 35.62 ? 140  ILE B O   1 
ATOM   3323 C  CB  . ILE B 2 140 ? -3.513  -11.532 21.517  1.00 26.55 ? 140  ILE B CB  1 
ATOM   3324 C  CG1 . ILE B 2 140 ? -4.825  -12.084 20.955  1.00 24.98 ? 140  ILE B CG1 1 
ATOM   3325 C  CG2 . ILE B 2 140 ? -2.388  -12.492 21.242  1.00 28.69 ? 140  ILE B CG2 1 
ATOM   3326 C  CD1 . ILE B 2 140 ? -6.002  -11.169 21.168  1.00 30.39 ? 140  ILE B CD1 1 
ATOM   3327 N  N   . GLU B 2 141 ? -2.653  -13.123 24.272  1.00 36.86 ? 141  GLU B N   1 
ATOM   3328 C  CA  . GLU B 2 141 ? -2.690  -14.334 25.089  1.00 32.94 ? 141  GLU B CA  1 
ATOM   3329 C  C   . GLU B 2 141 ? -3.468  -14.105 26.378  1.00 36.65 ? 141  GLU B C   1 
ATOM   3330 O  O   . GLU B 2 141 ? -4.176  -15.006 26.847  1.00 42.03 ? 141  GLU B O   1 
ATOM   3331 C  CB  . GLU B 2 141 ? -1.265  -14.791 25.398  1.00 37.66 ? 141  GLU B CB  1 
ATOM   3332 C  CG  . GLU B 2 141 ? -0.262  -14.450 24.307  1.00 41.86 ? 141  GLU B CG  1 
ATOM   3333 N  N   . GLU B 2 142 ? -3.370  -12.897 26.942  1.00 36.72 ? 142  GLU B N   1 
ATOM   3334 C  CA  . GLU B 2 142 ? -4.109  -12.545 28.153  1.00 39.39 ? 142  GLU B CA  1 
ATOM   3335 C  C   . GLU B 2 142 ? -5.619  -12.565 27.918  1.00 37.59 ? 142  GLU B C   1 
ATOM   3336 O  O   . GLU B 2 142 ? -6.375  -13.123 28.721  1.00 36.67 ? 142  GLU B O   1 
ATOM   3337 C  CB  . GLU B 2 142 ? -3.660  -11.168 28.643  1.00 42.98 ? 142  GLU B CB  1 
ATOM   3338 C  CG  . GLU B 2 142 ? -3.693  -10.984 30.150  1.00 50.00 ? 142  GLU B CG  1 
ATOM   3339 C  CD  . GLU B 2 142 ? -3.595  -9.519  30.558  1.00 54.12 ? 142  GLU B CD  1 
ATOM   3340 O  OE1 . GLU B 2 142 ? -4.654  -8.894  30.798  1.00 51.90 ? 142  GLU B OE1 1 
ATOM   3341 O  OE2 . GLU B 2 142 ? -2.461  -8.992  30.623  1.00 55.72 ? 142  GLU B OE2 1 
ATOM   3342 N  N   . VAL B 2 143 ? -6.082  -11.935 26.832  1.00 40.32 ? 143  VAL B N   1 
ATOM   3343 C  CA  . VAL B 2 143 ? -7.506  -11.987 26.494  1.00 36.19 ? 143  VAL B CA  1 
ATOM   3344 C  C   . VAL B 2 143 ? -7.961  -13.432 26.321  1.00 37.65 ? 143  VAL B C   1 
ATOM   3345 O  O   . VAL B 2 143 ? -9.009  -13.839 26.838  1.00 39.33 ? 143  VAL B O   1 
ATOM   3346 C  CB  . VAL B 2 143 ? -7.793  -11.161 25.229  1.00 37.16 ? 143  VAL B CB  1 
ATOM   3347 C  CG1 . VAL B 2 143 ? -9.289  -11.095 24.976  1.00 39.44 ? 143  VAL B CG1 1 
ATOM   3348 C  CG2 . VAL B 2 143 ? -7.202  -9.777  25.345  1.00 33.32 ? 143  VAL B CG2 1 
ATOM   3349 N  N   . ALA B 2 144 ? -7.178  -14.228 25.584  1.00 32.57 ? 144  ALA B N   1 
ATOM   3350 C  CA  . ALA B 2 144 ? -7.541  -15.623 25.355  1.00 37.10 ? 144  ALA B CA  1 
ATOM   3351 C  C   . ALA B 2 144 ? -7.712  -16.376 26.672  1.00 41.29 ? 144  ALA B C   1 
ATOM   3352 O  O   . ALA B 2 144 ? -8.627  -17.194 26.813  1.00 40.56 ? 144  ALA B O   1 
ATOM   3353 C  CB  . ALA B 2 144 ? -6.487  -16.298 24.480  1.00 40.91 ? 144  ALA B CB  1 
ATOM   3354 N  N   . ALA B 2 145 ? -6.853  -16.098 27.653  1.00 39.56 ? 145  ALA B N   1 
ATOM   3355 C  CA  . ALA B 2 145 ? -6.986  -16.726 28.964  1.00 45.30 ? 145  ALA B CA  1 
ATOM   3356 C  C   . ALA B 2 145 ? -8.191  -16.178 29.727  1.00 47.29 ? 145  ALA B C   1 
ATOM   3357 O  O   . ALA B 2 145 ? -9.015  -16.945 30.243  1.00 47.06 ? 145  ALA B O   1 
ATOM   3358 C  CB  . ALA B 2 145 ? -5.701  -16.520 29.765  1.00 38.00 ? 145  ALA B CB  1 
ATOM   3359 N  N   . SER B 2 146 ? -8.304  -14.850 29.815  1.00 45.07 ? 146  SER B N   1 
ATOM   3360 C  CA  . SER B 2 146 ? -9.396  -14.232 30.563  1.00 39.65 ? 146  SER B CA  1 
ATOM   3361 C  C   . SER B 2 146 ? -10.729 -14.411 29.851  1.00 46.07 ? 146  SER B C   1 
ATOM   3362 O  O   . SER B 2 146 ? -11.689 -14.934 30.428  1.00 48.86 ? 146  SER B O   1 
ATOM   3363 C  CB  . SER B 2 146 ? -9.110  -12.742 30.777  1.00 42.24 ? 146  SER B CB  1 
ATOM   3364 O  OG  . SER B 2 146 ? -8.176  -12.531 31.823  1.00 50.72 ? 146  SER B OG  1 
ATOM   3365 N  N   . ASN B 2 147 ? -10.814 -13.962 28.596  1.00 43.61 ? 147  ASN B N   1 
ATOM   3366 C  CA  . ASN B 2 147 ? -12.096 -13.785 27.911  1.00 40.61 ? 147  ASN B CA  1 
ATOM   3367 C  C   . ASN B 2 147 ? -11.996 -14.257 26.470  1.00 39.01 ? 147  ASN B C   1 
ATOM   3368 O  O   . ASN B 2 147 ? -12.124 -13.464 25.529  1.00 40.97 ? 147  ASN B O   1 
ATOM   3369 C  CB  . ASN B 2 147 ? -12.527 -12.320 27.971  1.00 40.79 ? 147  ASN B CB  1 
ATOM   3370 C  CG  . ASN B 2 147 ? -12.681 -11.824 29.391  1.00 46.41 ? 147  ASN B CG  1 
ATOM   3371 O  OD1 . ASN B 2 147 ? -13.117 -12.564 30.269  1.00 44.51 ? 147  ASN B OD1 1 
ATOM   3372 N  ND2 . ASN B 2 147 ? -12.317 -10.573 29.627  1.00 46.56 ? 147  ASN B ND2 1 
ATOM   3373 N  N   . PRO B 2 148 ? -11.786 -15.558 26.256  1.00 42.16 ? 148  PRO B N   1 
ATOM   3374 C  CA  . PRO B 2 148 ? -11.603 -16.049 24.878  1.00 40.19 ? 148  PRO B CA  1 
ATOM   3375 C  C   . PRO B 2 148 ? -12.809 -15.811 23.989  1.00 39.63 ? 148  PRO B C   1 
ATOM   3376 O  O   . PRO B 2 148 ? -12.661 -15.787 22.760  1.00 38.29 ? 148  PRO B O   1 
ATOM   3377 C  CB  . PRO B 2 148 ? -11.324 -17.547 25.069  1.00 42.41 ? 148  PRO B CB  1 
ATOM   3378 C  CG  . PRO B 2 148 ? -11.945 -17.884 26.397  1.00 45.83 ? 148  PRO B CG  1 
ATOM   3379 C  CD  . PRO B 2 148 ? -11.770 -16.652 27.245  1.00 45.32 ? 148  PRO B CD  1 
ATOM   3380 N  N   . GLU B 2 149 ? -13.995 -15.616 24.570  1.00 35.83 ? 149  GLU B N   1 
ATOM   3381 C  CA  . GLU B 2 149 ? -15.182 -15.323 23.773  1.00 34.99 ? 149  GLU B CA  1 
ATOM   3382 C  C   . GLU B 2 149 ? -15.083 -13.980 23.064  1.00 35.77 ? 149  GLU B C   1 
ATOM   3383 O  O   . GLU B 2 149 ? -15.806 -13.750 22.088  1.00 35.24 ? 149  GLU B O   1 
ATOM   3384 C  CB  . GLU B 2 149 ? -16.426 -15.342 24.658  1.00 33.51 ? 149  GLU B CB  1 
ATOM   3385 C  CG  . GLU B 2 149 ? -16.488 -14.211 25.664  1.00 35.98 ? 149  GLU B CG  1 
ATOM   3386 C  CD  . GLU B 2 149 ? -15.653 -14.474 26.915  1.00 37.33 ? 149  GLU B CD  1 
ATOM   3387 O  OE1 . GLU B 2 149 ? -14.924 -15.488 26.972  1.00 39.26 ? 149  GLU B OE1 1 
ATOM   3388 O  OE2 . GLU B 2 149 ? -15.726 -13.655 27.843  1.00 37.42 ? 149  GLU B OE2 1 
ATOM   3389 N  N   . LEU B 2 150 ? -14.209 -13.091 23.534  1.00 34.81 ? 150  LEU B N   1 
ATOM   3390 C  CA  . LEU B 2 150 ? -13.966 -11.810 22.888  1.00 37.40 ? 150  LEU B CA  1 
ATOM   3391 C  C   . LEU B 2 150 ? -12.890 -11.891 21.810  1.00 31.47 ? 150  LEU B C   1 
ATOM   3392 O  O   . LEU B 2 150 ? -12.446 -10.849 21.319  1.00 30.49 ? 150  LEU B O   1 
ATOM   3393 C  CB  . LEU B 2 150 ? -13.579 -10.758 23.929  1.00 33.91 ? 150  LEU B CB  1 
ATOM   3394 C  CG  . LEU B 2 150 ? -14.603 -10.489 25.037  1.00 39.18 ? 150  LEU B CG  1 
ATOM   3395 C  CD1 . LEU B 2 150 ? -14.106 -9.374  25.950  1.00 36.04 ? 150  LEU B CD1 1 
ATOM   3396 C  CD2 . LEU B 2 150 ? -15.953 -10.140 24.454  1.00 36.44 ? 150  LEU B CD2 1 
ATOM   3397 N  N   . ILE B 2 151 ? -12.453 -13.095 21.448  1.00 32.76 ? 151  ILE B N   1 
ATOM   3398 C  CA  . ILE B 2 151 ? -11.534 -13.306 20.335  1.00 28.85 ? 151  ILE B CA  1 
ATOM   3399 C  C   . ILE B 2 151 ? -12.354 -13.773 19.138  1.00 29.42 ? 151  ILE B C   1 
ATOM   3400 O  O   . ILE B 2 151 ? -12.944 -14.864 19.161  1.00 25.73 ? 151  ILE B O   1 
ATOM   3401 C  CB  . ILE B 2 151 ? -10.445 -14.326 20.680  1.00 33.87 ? 151  ILE B CB  1 
ATOM   3402 C  CG1 . ILE B 2 151 ? -9.913  -14.080 22.098  1.00 37.07 ? 151  ILE B CG1 1 
ATOM   3403 C  CG2 . ILE B 2 151 ? -9.343  -14.325 19.589  1.00 27.13 ? 151  ILE B CG2 1 
ATOM   3404 C  CD1 . ILE B 2 151 ? -8.603  -13.379 22.174  1.00 31.92 ? 151  ILE B CD1 1 
ATOM   3405 N  N   . PHE B 2 152 ? -12.387 -12.952 18.089  1.00 25.49 ? 152  PHE B N   1 
ATOM   3406 C  CA  . PHE B 2 152 ? -13.071 -13.273 16.841  1.00 25.31 ? 152  PHE B CA  1 
ATOM   3407 C  C   . PHE B 2 152 ? -12.057 -13.606 15.759  1.00 24.23 ? 152  PHE B C   1 
ATOM   3408 O  O   . PHE B 2 152 ? -10.984 -12.998 15.694  1.00 26.48 ? 152  PHE B O   1 
ATOM   3409 C  CB  . PHE B 2 152 ? -13.938 -12.113 16.374  1.00 21.36 ? 152  PHE B CB  1 
ATOM   3410 C  CG  . PHE B 2 152 ? -15.034 -11.751 17.336  1.00 30.97 ? 152  PHE B CG  1 
ATOM   3411 C  CD1 . PHE B 2 152 ? -16.210 -12.483 17.367  1.00 27.83 ? 152  PHE B CD1 1 
ATOM   3412 C  CD2 . PHE B 2 152 ? -14.889 -10.674 18.207  1.00 31.22 ? 152  PHE B CD2 1 
ATOM   3413 C  CE1 . PHE B 2 152 ? -17.234 -12.147 18.243  1.00 34.42 ? 152  PHE B CE1 1 
ATOM   3414 C  CE2 . PHE B 2 152 ? -15.909 -10.332 19.090  1.00 36.64 ? 152  PHE B CE2 1 
ATOM   3415 C  CZ  . PHE B 2 152 ? -17.083 -11.071 19.104  1.00 31.82 ? 152  PHE B CZ  1 
ATOM   3416 N  N   . LYS B 2 153 ? -12.392 -14.578 14.915  1.00 19.04 ? 153  LYS B N   1 
ATOM   3417 C  CA  . LYS B 2 153 ? -11.496 -14.988 13.846  1.00 24.16 ? 153  LYS B CA  1 
ATOM   3418 C  C   . LYS B 2 153 ? -12.277 -15.181 12.552  1.00 25.23 ? 153  LYS B C   1 
ATOM   3419 O  O   . LYS B 2 153 ? -13.453 -15.552 12.566  1.00 17.90 ? 153  LYS B O   1 
ATOM   3420 C  CB  . LYS B 2 153 ? -10.734 -16.272 14.208  1.00 22.76 ? 153  LYS B CB  1 
ATOM   3421 C  CG  . LYS B 2 153 ? -9.906  -16.150 15.504  1.00 23.37 ? 153  LYS B CG  1 
ATOM   3422 C  CD  . LYS B 2 153 ? -9.017  -17.362 15.723  1.00 22.00 ? 153  LYS B CD  1 
ATOM   3423 C  CE  . LYS B 2 153 ? -8.145  -17.201 16.962  1.00 26.35 ? 153  LYS B CE  1 
ATOM   3424 N  NZ  . LYS B 2 153 ? -7.237  -18.376 17.164  1.00 19.58 ? 153  LYS B NZ  1 
ATOM   3425 N  N   . GLU B 2 154 ? -11.608 -14.896 11.433  1.00 16.90 ? 154  GLU B N   1 
ATOM   3426 C  CA  . GLU B 2 154 ? -12.110 -15.159 10.093  1.00 21.66 ? 154  GLU B CA  1 
ATOM   3427 C  C   . GLU B 2 154 ? -11.016 -15.889 9.330   1.00 21.30 ? 154  GLU B C   1 
ATOM   3428 O  O   . GLU B 2 154 ? -9.863  -15.444 9.330   1.00 20.14 ? 154  GLU B O   1 
ATOM   3429 C  CB  . GLU B 2 154 ? -12.483 -13.866 9.349   1.00 22.30 ? 154  GLU B CB  1 
ATOM   3430 C  CG  . GLU B 2 154 ? -13.436 -12.938 10.106  1.00 30.01 ? 154  GLU B CG  1 
ATOM   3431 C  CD  . GLU B 2 154 ? -14.878 -13.410 10.045  1.00 30.16 ? 154  GLU B CD  1 
ATOM   3432 O  OE1 . GLU B 2 154 ? -15.165 -14.323 9.246   1.00 25.98 ? 154  GLU B OE1 1 
ATOM   3433 O  OE2 . GLU B 2 154 ? -15.721 -12.860 10.786  1.00 37.17 ? 154  GLU B OE2 1 
ATOM   3434 N  N   . GLN B 2 155 ? -11.361 -17.001 8.685   1.00 20.04 ? 155  GLN B N   1 
ATOM   3435 C  CA  . GLN B 2 155 ? -10.400 -17.704 7.840   1.00 20.13 ? 155  GLN B CA  1 
ATOM   3436 C  C   . GLN B 2 155 ? -10.465 -17.117 6.437   1.00 22.16 ? 155  GLN B C   1 
ATOM   3437 O  O   . GLN B 2 155 ? -11.546 -17.008 5.854   1.00 19.63 ? 155  GLN B O   1 
ATOM   3438 C  CB  . GLN B 2 155 ? -10.670 -19.211 7.829   1.00 22.26 ? 155  GLN B CB  1 
ATOM   3439 C  CG  . GLN B 2 155 ? -10.332 -19.871 9.165   1.00 22.36 ? 155  GLN B CG  1 
ATOM   3440 C  CD  . GLN B 2 155 ? -10.655 -21.350 9.213   1.00 25.19 ? 155  GLN B CD  1 
ATOM   3441 O  OE1 . GLN B 2 155 ? -10.289 -22.110 8.318   1.00 28.16 ? 155  GLN B OE1 1 
ATOM   3442 N  NE2 . GLN B 2 155 ? -11.346 -21.771 10.276  1.00 22.15 ? 155  GLN B NE2 1 
ATOM   3443 N  N   . ILE B 2 156 ? -9.312  -16.696 5.915   1.00 23.23 ? 156  ILE B N   1 
ATOM   3444 C  CA  . ILE B 2 156 ? -9.236  -16.006 4.629   1.00 17.00 ? 156  ILE B CA  1 
ATOM   3445 C  C   . ILE B 2 156 ? -8.705  -16.974 3.586   1.00 18.01 ? 156  ILE B C   1 
ATOM   3446 O  O   . ILE B 2 156 ? -7.594  -17.500 3.726   1.00 17.43 ? 156  ILE B O   1 
ATOM   3447 C  CB  . ILE B 2 156 ? -8.344  -14.755 4.697   1.00 19.54 ? 156  ILE B CB  1 
ATOM   3448 C  CG1 . ILE B 2 156 ? -8.788  -13.793 5.811   1.00 18.48 ? 156  ILE B CG1 1 
ATOM   3449 C  CG2 . ILE B 2 156 ? -8.360  -14.035 3.358   1.00 21.10 ? 156  ILE B CG2 1 
ATOM   3450 C  CD1 . ILE B 2 156 ? -10.229 -13.335 5.709   1.00 19.97 ? 156  ILE B CD1 1 
ATOM   3451 N  N   . ASP B 2 157 ? -9.477  -17.193 2.526   1.00 19.10 ? 157  ASP B N   1 
ATOM   3452 C  CA  . ASP B 2 157 ? -9.048  -18.109 1.470   1.00 22.79 ? 157  ASP B CA  1 
ATOM   3453 C  C   . ASP B 2 157 ? -7.926  -17.457 0.659   1.00 21.16 ? 157  ASP B C   1 
ATOM   3454 O  O   . ASP B 2 157 ? -8.093  -16.351 0.136   1.00 19.80 ? 157  ASP B O   1 
ATOM   3455 C  CB  . ASP B 2 157 ? -10.242 -18.481 0.591   1.00 23.36 ? 157  ASP B CB  1 
ATOM   3456 C  CG  . ASP B 2 157 ? -9.860  -19.352 -0.585  1.00 20.91 ? 157  ASP B CG  1 
ATOM   3457 O  OD1 . ASP B 2 157 ? -9.274  -18.829 -1.553  1.00 22.71 ? 157  ASP B OD1 1 
ATOM   3458 O  OD2 . ASP B 2 157 ? -10.151 -20.565 -0.539  1.00 23.77 ? 157  ASP B OD2 1 
ATOM   3459 N  N   . ILE B 2 158 ? -6.785  -18.150 0.548   1.00 22.05 ? 158  ILE B N   1 
ATOM   3460 C  CA  . ILE B 2 158 ? -5.570  -17.541 -0.002  1.00 20.86 ? 158  ILE B CA  1 
ATOM   3461 C  C   . ILE B 2 158 ? -5.762  -17.085 -1.444  1.00 24.56 ? 158  ILE B C   1 
ATOM   3462 O  O   . ILE B 2 158 ? -5.151  -16.098 -1.872  1.00 22.45 ? 158  ILE B O   1 
ATOM   3463 C  CB  . ILE B 2 158 ? -4.376  -18.519 0.131   1.00 21.41 ? 158  ILE B CB  1 
ATOM   3464 C  CG1 . ILE B 2 158 ? -3.072  -17.836 -0.275  1.00 26.74 ? 158  ILE B CG1 1 
ATOM   3465 C  CG2 . ILE B 2 158 ? -4.600  -19.779 -0.696  1.00 20.12 ? 158  ILE B CG2 1 
ATOM   3466 C  CD1 . ILE B 2 158 ? -2.749  -16.587 0.558   1.00 28.07 ? 158  ILE B CD1 1 
ATOM   3467 N  N   . PHE B 2 159 ? -6.602  -17.774 -2.221  1.00 23.96 ? 159  PHE B N   1 
ATOM   3468 C  CA  . PHE B 2 159 ? -6.783  -17.383 -3.620  1.00 22.14 ? 159  PHE B CA  1 
ATOM   3469 C  C   . PHE B 2 159 ? -7.950  -16.429 -3.828  1.00 22.27 ? 159  PHE B C   1 
ATOM   3470 O  O   . PHE B 2 159 ? -7.884  -15.577 -4.718  1.00 26.95 ? 159  PHE B O   1 
ATOM   3471 C  CB  . PHE B 2 159 ? -6.974  -18.616 -4.509  1.00 26.81 ? 159  PHE B CB  1 
ATOM   3472 C  CG  . PHE B 2 159 ? -5.713  -19.401 -4.726  1.00 23.48 ? 159  PHE B CG  1 
ATOM   3473 C  CD1 . PHE B 2 159 ? -4.669  -18.868 -5.471  1.00 20.29 ? 159  PHE B CD1 1 
ATOM   3474 C  CD2 . PHE B 2 159 ? -5.568  -20.667 -4.190  1.00 23.56 ? 159  PHE B CD2 1 
ATOM   3475 C  CE1 . PHE B 2 159 ? -3.501  -19.589 -5.663  1.00 24.41 ? 159  PHE B CE1 1 
ATOM   3476 C  CE2 . PHE B 2 159 ? -4.402  -21.394 -4.387  1.00 20.00 ? 159  PHE B CE2 1 
ATOM   3477 C  CZ  . PHE B 2 159 ? -3.368  -20.852 -5.128  1.00 21.47 ? 159  PHE B CZ  1 
ATOM   3478 N  N   . GLU B 2 160 ? -9.014  -16.543 -3.024  1.00 23.43 ? 160  GLU B N   1 
ATOM   3479 C  CA  . GLU B 2 160 ? -10.105 -15.573 -3.091  1.00 26.74 ? 160  GLU B CA  1 
ATOM   3480 C  C   . GLU B 2 160 ? -9.691  -14.199 -2.555  1.00 30.05 ? 160  GLU B C   1 
ATOM   3481 O  O   . GLU B 2 160 ? -10.213 -13.173 -3.008  1.00 30.94 ? 160  GLU B O   1 
ATOM   3482 C  CB  . GLU B 2 160 ? -11.297 -16.109 -2.307  1.00 28.97 ? 160  GLU B CB  1 
ATOM   3483 C  CG  . GLU B 2 160 ? -12.584 -15.332 -2.480  1.00 34.47 ? 160  GLU B CG  1 
ATOM   3484 C  CD  . GLU B 2 160 ? -13.677 -15.870 -1.575  1.00 45.84 ? 160  GLU B CD  1 
ATOM   3485 O  OE1 . GLU B 2 160 ? -14.867 -15.801 -1.959  1.00 48.50 ? 160  GLU B OE1 1 
ATOM   3486 O  OE2 . GLU B 2 160 ? -13.337 -16.378 -0.477  1.00 45.31 ? 160  GLU B OE2 1 
ATOM   3487 N  N   . GLY B 2 161 ? -8.760  -14.154 -1.604  1.00 20.80 ? 161  GLY B N   1 
ATOM   3488 C  CA  . GLY B 2 161 ? -8.445  -12.925 -0.901  1.00 23.20 ? 161  GLY B CA  1 
ATOM   3489 C  C   . GLY B 2 161 ? -9.515  -12.537 0.100   1.00 23.74 ? 161  GLY B C   1 
ATOM   3490 O  O   . GLY B 2 161 ? -10.586 -13.157 0.131   1.00 25.22 ? 161  GLY B O   1 
ATOM   3491 N  N   . ILE B 2 162 ? -9.248  -11.517 0.927   1.00 24.19 ? 162  ILE B N   1 
ATOM   3492 C  CA  . ILE B 2 162 ? -10.219 -11.131 1.945   1.00 21.23 ? 162  ILE B CA  1 
ATOM   3493 C  C   . ILE B 2 162 ? -11.479 -10.622 1.264   1.00 29.65 ? 162  ILE B C   1 
ATOM   3494 O  O   . ILE B 2 162 ? -11.421 -9.919  0.246   1.00 23.22 ? 162  ILE B O   1 
ATOM   3495 C  CB  . ILE B 2 162 ? -9.632  -10.087 2.913   1.00 23.92 ? 162  ILE B CB  1 
ATOM   3496 C  CG1 . ILE B 2 162 ? -10.565 -9.885  4.112   1.00 22.04 ? 162  ILE B CG1 1 
ATOM   3497 C  CG2 . ILE B 2 162 ? -9.348  -8.774  2.198   1.00 23.83 ? 162  ILE B CG2 1 
ATOM   3498 C  CD1 . ILE B 2 162 ? -9.937  -9.117  5.249   1.00 22.21 ? 162  ILE B CD1 1 
ATOM   3499 N  N   . LYS B 2 163 ? -12.627 -11.045 1.784   1.00 30.09 ? 163  LYS B N   1 
ATOM   3500 C  CA  . LYS B 2 163 ? -13.915 -10.634 1.253   1.00 33.99 ? 163  LYS B CA  1 
ATOM   3501 C  C   . LYS B 2 163 ? -14.433 -9.417  2.008   1.00 29.05 ? 163  LYS B C   1 
ATOM   3502 O  O   . LYS B 2 163 ? -14.189 -9.254  3.205   1.00 28.86 ? 163  LYS B O   1 
ATOM   3503 C  CB  . LYS B 2 163 ? -14.930 -11.775 1.352   1.00 28.79 ? 163  LYS B CB  1 
ATOM   3504 C  CG  . LYS B 2 163 ? -14.641 -12.946 0.439   1.00 31.99 ? 163  LYS B CG  1 
ATOM   3505 N  N   . ASP B 2 164 ? -15.157 -8.557  1.288   1.00 35.79 ? 164  ASP B N   1 
ATOM   3506 C  CA  . ASP B 2 164 ? -15.788 -7.410  1.930   1.00 32.40 ? 164  ASP B CA  1 
ATOM   3507 C  C   . ASP B 2 164 ? -16.620 -7.842  3.127   1.00 33.48 ? 164  ASP B C   1 
ATOM   3508 O  O   . ASP B 2 164 ? -16.556 -7.222  4.194   1.00 30.80 ? 164  ASP B O   1 
ATOM   3509 C  CB  . ASP B 2 164 ? -16.651 -6.651  0.922   1.00 34.45 ? 164  ASP B CB  1 
ATOM   3510 C  CG  . ASP B 2 164 ? -17.408 -5.498  1.556   1.00 40.60 ? 164  ASP B CG  1 
ATOM   3511 O  OD1 . ASP B 2 164 ? -16.756 -4.541  2.031   1.00 43.78 ? 164  ASP B OD1 1 
ATOM   3512 O  OD2 . ASP B 2 164 ? -18.655 -5.545  1.587   1.00 45.14 ? 164  ASP B OD2 1 
ATOM   3513 N  N   . SER B 2 165 ? -17.381 -8.933  2.980   1.00 33.00 ? 165  SER B N   1 
ATOM   3514 C  CA  . SER B 2 165 ? -18.216 -9.407  4.077   1.00 33.69 ? 165  SER B CA  1 
ATOM   3515 C  C   . SER B 2 165 ? -17.373 -9.782  5.289   1.00 32.46 ? 165  SER B C   1 
ATOM   3516 O  O   . SER B 2 165 ? -17.778 -9.545  6.435   1.00 28.91 ? 165  SER B O   1 
ATOM   3517 C  CB  . SER B 2 165 ? -19.064 -10.596 3.614   1.00 32.36 ? 165  SER B CB  1 
ATOM   3518 O  OG  . SER B 2 165 ? -18.240 -11.663 3.170   1.00 32.77 ? 165  SER B OG  1 
ATOM   3519 N  N   . GLN B 2 166 ? -16.190 -10.363 5.057   1.00 31.60 ? 166  GLN B N   1 
ATOM   3520 C  CA  . GLN B 2 166 ? -15.314 -10.741 6.167   1.00 30.71 ? 166  GLN B CA  1 
ATOM   3521 C  C   . GLN B 2 166 ? -14.729 -9.514  6.863   1.00 24.46 ? 166  GLN B C   1 
ATOM   3522 O  O   . GLN B 2 166 ? -14.668 -9.465  8.096   1.00 25.88 ? 166  GLN B O   1 
ATOM   3523 C  CB  . GLN B 2 166 ? -14.194 -11.659 5.665   1.00 26.06 ? 166  GLN B CB  1 
ATOM   3524 C  CG  . GLN B 2 166 ? -14.648 -13.075 5.350   1.00 27.11 ? 166  GLN B CG  1 
ATOM   3525 C  CD  . GLN B 2 166 ? -13.557 -13.923 4.698   1.00 29.59 ? 166  GLN B CD  1 
ATOM   3526 O  OE1 . GLN B 2 166 ? -12.901 -13.490 3.747   1.00 31.03 ? 166  GLN B OE1 1 
ATOM   3527 N  NE2 . GLN B 2 166 ? -13.355 -15.132 5.216   1.00 27.60 ? 166  GLN B NE2 1 
ATOM   3528 N  N   . ALA B 2 167 ? -14.279 -8.521  6.096   1.00 26.01 ? 167  ALA B N   1 
ATOM   3529 C  CA  . ALA B 2 167 ? -13.763 -7.304  6.721   1.00 26.42 ? 167  ALA B CA  1 
ATOM   3530 C  C   . ALA B 2 167 ? -14.867 -6.552  7.455   1.00 28.50 ? 167  ALA B C   1 
ATOM   3531 O  O   . ALA B 2 167 ? -14.630 -5.999  8.538   1.00 24.51 ? 167  ALA B O   1 
ATOM   3532 C  CB  . ALA B 2 167 ? -13.104 -6.407  5.675   1.00 23.16 ? 167  ALA B CB  1 
ATOM   3533 N  N   . GLN B 2 168 ? -16.085 -6.545  6.893   1.00 29.49 ? 168  GLN B N   1 
ATOM   3534 C  CA  . GLN B 2 168 ? -17.209 -5.872  7.544   1.00 31.30 ? 168  GLN B CA  1 
ATOM   3535 C  C   . GLN B 2 168 ? -17.573 -6.546  8.854   1.00 30.16 ? 168  GLN B C   1 
ATOM   3536 O  O   . GLN B 2 168 ? -17.817 -5.866  9.860   1.00 30.19 ? 168  GLN B O   1 
ATOM   3537 C  CB  . GLN B 2 168 ? -18.430 -5.841  6.624   1.00 31.47 ? 168  GLN B CB  1 
ATOM   3538 C  CG  . GLN B 2 168 ? -18.278 -4.999  5.373   1.00 29.79 ? 168  GLN B CG  1 
ATOM   3539 C  CD  . GLN B 2 168 ? -18.155 -3.524  5.666   1.00 39.92 ? 168  GLN B CD  1 
ATOM   3540 O  OE1 . GLN B 2 168 ? -18.587 -3.048  6.719   1.00 40.88 ? 168  GLN B OE1 1 
ATOM   3541 N  NE2 . GLN B 2 168 ? -17.561 -2.784  4.734   1.00 38.79 ? 168  GLN B NE2 1 
ATOM   3542 N  N   . ARG B 2 169 ? -17.629 -7.885  8.859   1.00 27.88 ? 169  ARG B N   1 
ATOM   3543 C  CA  . ARG B 2 169 ? -18.045 -8.605  10.060  1.00 32.97 ? 169  ARG B CA  1 
ATOM   3544 C  C   . ARG B 2 169 ? -17.004 -8.488  11.166  1.00 31.04 ? 169  ARG B C   1 
ATOM   3545 O  O   . ARG B 2 169 ? -17.358 -8.388  12.348  1.00 32.19 ? 169  ARG B O   1 
ATOM   3546 C  CB  . ARG B 2 169 ? -18.328 -10.078 9.733   1.00 30.19 ? 169  ARG B CB  1 
ATOM   3547 C  CG  . ARG B 2 169 ? -18.454 -10.991 10.961  1.00 38.48 ? 169  ARG B CG  1 
ATOM   3548 C  CD  . ARG B 2 169 ? -19.038 -12.370 10.622  1.00 35.31 ? 169  ARG B CD  1 
ATOM   3549 N  NE  . ARG B 2 169 ? -18.176 -13.150 9.742   1.00 38.00 ? 169  ARG B NE  1 
ATOM   3550 C  CZ  . ARG B 2 169 ? -18.397 -13.348 8.443   1.00 37.59 ? 169  ARG B CZ  1 
ATOM   3551 N  NH1 . ARG B 2 169 ? -19.471 -12.832 7.851   1.00 34.49 ? 169  ARG B NH1 1 
ATOM   3552 N  NH2 . ARG B 2 169 ? -17.542 -14.078 7.735   1.00 36.46 ? 169  ARG B NH2 1 
ATOM   3553 N  N   . MET B 2 170 ? -15.715 -8.496  10.813  1.00 28.34 ? 170  MET B N   1 
ATOM   3554 C  CA  . MET B 2 170 ? -14.700 -8.286  11.844  1.00 26.06 ? 170  MET B CA  1 
ATOM   3555 C  C   . MET B 2 170 ? -14.798 -6.881  12.429  1.00 28.43 ? 170  MET B C   1 
ATOM   3556 O  O   . MET B 2 170 ? -14.688 -6.701  13.649  1.00 26.69 ? 170  MET B O   1 
ATOM   3557 C  CB  . MET B 2 170 ? -13.299 -8.532  11.291  1.00 23.80 ? 170  MET B CB  1 
ATOM   3558 C  CG  . MET B 2 170 ? -12.207 -8.325  12.340  1.00 18.69 ? 170  MET B CG  1 
ATOM   3559 S  SD  . MET B 2 170 ? -12.318 -9.479  13.725  1.00 25.38 ? 170  MET B SD  1 
ATOM   3560 C  CE  . MET B 2 170 ? -12.239 -11.038 12.861  1.00 29.18 ? 170  MET B CE  1 
ATOM   3561 N  N   . ALA B 2 171 ? -14.998 -5.875  11.574  1.00 25.32 ? 171  ALA B N   1 
ATOM   3562 C  CA  . ALA B 2 171 ? -15.158 -4.510  12.065  1.00 29.91 ? 171  ALA B CA  1 
ATOM   3563 C  C   . ALA B 2 171 ? -16.329 -4.419  13.041  1.00 29.39 ? 171  ALA B C   1 
ATOM   3564 O  O   . ALA B 2 171 ? -16.195 -3.875  14.145  1.00 26.92 ? 171  ALA B O   1 
ATOM   3565 C  CB  . ALA B 2 171 ? -15.335 -3.555  10.885  1.00 24.67 ? 171  ALA B CB  1 
ATOM   3566 N  N   . GLU B 2 172 ? -17.478 -4.984  12.662  1.00 32.99 ? 172  GLU B N   1 
ATOM   3567 C  CA  . GLU B 2 172 ? -18.597 -5.096  13.592  1.00 29.75 ? 172  GLU B CA  1 
ATOM   3568 C  C   . GLU B 2 172 ? -18.184 -5.819  14.868  1.00 37.76 ? 172  GLU B C   1 
ATOM   3569 O  O   . GLU B 2 172 ? -18.477 -5.363  15.982  1.00 30.04 ? 172  GLU B O   1 
ATOM   3570 C  CB  . GLU B 2 172 ? -19.757 -5.819  12.916  1.00 36.76 ? 172  GLU B CB  1 
ATOM   3571 C  CG  . GLU B 2 172 ? -20.968 -5.996  13.812  1.00 43.74 ? 172  GLU B CG  1 
ATOM   3572 C  CD  . GLU B 2 172 ? -22.239 -6.134  13.007  1.00 51.06 ? 172  GLU B CD  1 
ATOM   3573 O  OE1 . GLU B 2 172 ? -23.334 -5.924  13.575  1.00 58.53 ? 172  GLU B OE1 1 
ATOM   3574 O  OE2 . GLU B 2 172 ? -22.132 -6.443  11.799  1.00 51.22 ? 172  GLU B OE2 1 
ATOM   3575 N  N   . ASN B 2 173 ? -17.483 -6.945  14.728  1.00 31.03 ? 173  ASN B N   1 
ATOM   3576 C  CA  . ASN B 2 173 ? -17.068 -7.696  15.906  1.00 31.16 ? 173  ASN B CA  1 
ATOM   3577 C  C   . ASN B 2 173 ? -16.179 -6.866  16.833  1.00 35.33 ? 173  ASN B C   1 
ATOM   3578 O  O   . ASN B 2 173 ? -16.128 -7.126  18.041  1.00 28.85 ? 173  ASN B O   1 
ATOM   3579 C  CB  . ASN B 2 173 ? -16.361 -8.981  15.470  1.00 32.21 ? 173  ASN B CB  1 
ATOM   3580 C  CG  . ASN B 2 173 ? -17.338 -10.049 14.999  1.00 36.69 ? 173  ASN B CG  1 
ATOM   3581 O  OD1 . ASN B 2 173 ? -18.508 -10.050 15.389  1.00 33.72 ? 173  ASN B OD1 1 
ATOM   3582 N  ND2 . ASN B 2 173 ? -16.859 -10.968 14.163  1.00 38.88 ? 173  ASN B ND2 1 
ATOM   3583 N  N   . LEU B 2 174 ? -15.482 -5.863  16.303  1.00 30.97 ? 174  LEU B N   1 
ATOM   3584 C  CA  . LEU B 2 174 ? -14.619 -5.033  17.132  1.00 31.47 ? 174  LEU B CA  1 
ATOM   3585 C  C   . LEU B 2 174 ? -15.306 -3.766  17.628  1.00 31.68 ? 174  LEU B C   1 
ATOM   3586 O  O   . LEU B 2 174 ? -14.659 -2.957  18.298  1.00 30.31 ? 174  LEU B O   1 
ATOM   3587 C  CB  . LEU B 2 174 ? -13.337 -4.652  16.374  1.00 30.08 ? 174  LEU B CB  1 
ATOM   3588 C  CG  . LEU B 2 174 ? -12.511 -5.807  15.793  1.00 32.54 ? 174  LEU B CG  1 
ATOM   3589 C  CD1 . LEU B 2 174 ? -11.119 -5.359  15.384  1.00 27.30 ? 174  LEU B CD1 1 
ATOM   3590 C  CD2 . LEU B 2 174 ? -12.456 -6.979  16.761  1.00 29.70 ? 174  LEU B CD2 1 
ATOM   3591 N  N   . GLY B 2 175 ? -16.581 -3.563  17.300  1.00 34.97 ? 175  GLY B N   1 
ATOM   3592 C  CA  . GLY B 2 175 ? -17.339 -2.451  17.847  1.00 37.59 ? 175  GLY B CA  1 
ATOM   3593 C  C   . GLY B 2 175 ? -17.331 -1.161  17.055  1.00 39.95 ? 175  GLY B C   1 
ATOM   3594 O  O   . GLY B 2 175 ? -17.716 -0.119  17.600  1.00 40.08 ? 175  GLY B O   1 
ATOM   3595 N  N   . PHE B 2 176 ? -16.914 -1.183  15.792  1.00 38.30 ? 176  PHE B N   1 
ATOM   3596 C  CA  . PHE B 2 176 ? -16.998 -0.002  14.937  1.00 40.27 ? 176  PHE B CA  1 
ATOM   3597 C  C   . PHE B 2 176 ? -18.390 0.048   14.317  1.00 44.85 ? 176  PHE B C   1 
ATOM   3598 O  O   . PHE B 2 176 ? -18.818 -0.918  13.673  1.00 43.94 ? 176  PHE B O   1 
ATOM   3599 C  CB  . PHE B 2 176 ? -15.918 -0.029  13.853  1.00 37.67 ? 176  PHE B CB  1 
ATOM   3600 C  CG  . PHE B 2 176 ? -14.513 0.077   14.389  1.00 34.10 ? 176  PHE B CG  1 
ATOM   3601 C  CD1 . PHE B 2 176 ? -13.826 -1.059  14.794  1.00 32.18 ? 176  PHE B CD1 1 
ATOM   3602 C  CD2 . PHE B 2 176 ? -13.882 1.308   14.480  1.00 32.30 ? 176  PHE B CD2 1 
ATOM   3603 C  CE1 . PHE B 2 176 ? -12.540 -0.968  15.287  1.00 33.03 ? 176  PHE B CE1 1 
ATOM   3604 C  CE2 . PHE B 2 176 ? -12.587 1.414   14.975  1.00 37.30 ? 176  PHE B CE2 1 
ATOM   3605 C  CZ  . PHE B 2 176 ? -11.914 0.273   15.379  1.00 37.23 ? 176  PHE B CZ  1 
ATOM   3606 N  N   . VAL B 2 177 ? -19.104 1.158   14.523  1.00 42.25 ? 177  VAL B N   1 
ATOM   3607 C  CA  . VAL B 2 177 ? -20.479 1.282   14.057  1.00 47.10 ? 177  VAL B CA  1 
ATOM   3608 C  C   . VAL B 2 177 ? -20.568 2.405   13.033  1.00 47.11 ? 177  VAL B C   1 
ATOM   3609 O  O   . VAL B 2 177 ? -19.754 3.331   13.011  1.00 46.72 ? 177  VAL B O   1 
ATOM   3610 C  CB  . VAL B 2 177 ? -21.482 1.525   15.208  1.00 47.56 ? 177  VAL B CB  1 
ATOM   3611 C  CG1 . VAL B 2 177 ? -20.964 0.932   16.519  1.00 42.89 ? 177  VAL B CG1 1 
ATOM   3612 C  CG2 . VAL B 2 177 ? -21.791 3.007   15.356  1.00 43.93 ? 177  VAL B CG2 1 
ATOM   3613 N  N   . GLY B 2 178 ? -21.581 2.305   12.175  1.00 44.37 ? 178  GLY B N   1 
ATOM   3614 C  CA  . GLY B 2 178 ? -21.871 3.327   11.201  1.00 42.36 ? 178  GLY B CA  1 
ATOM   3615 C  C   . GLY B 2 178 ? -20.701 3.651   10.300  1.00 46.98 ? 178  GLY B C   1 
ATOM   3616 O  O   . GLY B 2 178 ? -20.196 2.796   9.566   1.00 50.08 ? 178  GLY B O   1 
ATOM   3617 N  N   . PRO B 2 179 ? -20.246 4.909   10.342  1.00 48.64 ? 179  PRO B N   1 
ATOM   3618 C  CA  . PRO B 2 179 ? -19.209 5.350   9.390   1.00 49.40 ? 179  PRO B CA  1 
ATOM   3619 C  C   . PRO B 2 179 ? -17.835 4.778   9.680   1.00 46.92 ? 179  PRO B C   1 
ATOM   3620 O  O   . PRO B 2 179 ? -17.022 4.643   8.756   1.00 44.61 ? 179  PRO B O   1 
ATOM   3621 C  CB  . PRO B 2 179 ? -19.210 6.881   9.544   1.00 48.97 ? 179  PRO B CB  1 
ATOM   3622 C  CG  . PRO B 2 179 ? -20.440 7.213   10.375  1.00 46.98 ? 179  PRO B CG  1 
ATOM   3623 C  CD  . PRO B 2 179 ? -20.697 6.005   11.216  1.00 47.63 ? 179  PRO B CD  1 
ATOM   3624 N  N   . LEU B 2 180 ? -17.550 4.431   10.927  1.00 43.41 ? 180  LEU B N   1 
ATOM   3625 C  CA  . LEU B 2 180 ? -16.252 3.874   11.250  1.00 41.49 ? 180  LEU B CA  1 
ATOM   3626 C  C   . LEU B 2 180 ? -16.182 2.372   10.989  1.00 41.18 ? 180  LEU B C   1 
ATOM   3627 O  O   . LEU B 2 180 ? -15.077 1.819   10.942  1.00 34.24 ? 180  LEU B O   1 
ATOM   3628 C  CB  . LEU B 2 180 ? -15.898 4.199   12.705  1.00 37.26 ? 180  LEU B CB  1 
ATOM   3629 C  CG  . LEU B 2 180 ? -16.047 5.689   13.036  1.00 42.02 ? 180  LEU B CG  1 
ATOM   3630 C  CD1 . LEU B 2 180 ? -15.288 6.040   14.275  1.00 40.81 ? 180  LEU B CD1 1 
ATOM   3631 C  CD2 . LEU B 2 180 ? -15.575 6.572   11.890  1.00 47.22 ? 180  LEU B CD2 1 
ATOM   3632 N  N   . LYS B 2 181 ? -17.324 1.706   10.787  1.00 38.71 ? 181  LYS B N   1 
ATOM   3633 C  CA  . LYS B 2 181 ? -17.284 0.312   10.359  1.00 37.77 ? 181  LYS B CA  1 
ATOM   3634 C  C   . LYS B 2 181 ? -16.662 0.193   8.975   1.00 39.46 ? 181  LYS B C   1 
ATOM   3635 O  O   . LYS B 2 181 ? -15.708 -0.571  8.776   1.00 34.19 ? 181  LYS B O   1 
ATOM   3636 C  CB  . LYS B 2 181 ? -18.686 -0.305  10.374  1.00 44.07 ? 181  LYS B CB  1 
ATOM   3637 C  CG  . LYS B 2 181 ? -18.753 -1.720  9.761   1.00 36.03 ? 181  LYS B CG  1 
ATOM   3638 C  CD  . LYS B 2 181 ? -19.935 -2.519  10.312  1.00 39.10 ? 181  LYS B CD  1 
ATOM   3639 C  CE  . LYS B 2 181 ? -20.606 -3.367  9.246   1.00 42.83 ? 181  LYS B CE  1 
ATOM   3640 N  NZ  . LYS B 2 181 ? -21.762 -4.113  9.804   1.00 38.72 ? 181  LYS B NZ  1 
ATOM   3641 N  N   . SER B 2 182 ? -17.193 0.946   8.003   1.00 33.62 ? 182  SER B N   1 
ATOM   3642 C  CA  . SER B 2 182 ? -16.652 0.900   6.649   1.00 35.09 ? 182  SER B CA  1 
ATOM   3643 C  C   . SER B 2 182 ? -15.197 1.349   6.615   1.00 33.19 ? 182  SER B C   1 
ATOM   3644 O  O   . SER B 2 182 ? -14.401 0.841   5.816   1.00 28.66 ? 182  SER B O   1 
ATOM   3645 C  CB  . SER B 2 182 ? -17.499 1.773   5.722   1.00 41.56 ? 182  SER B CB  1 
ATOM   3646 O  OG  . SER B 2 182 ? -18.873 1.700   6.074   1.00 48.26 ? 182  SER B OG  1 
ATOM   3647 N  N   . GLN B 2 183 ? -14.841 2.308   7.467   1.00 32.80 ? 183  GLN B N   1 
ATOM   3648 C  CA  . GLN B 2 183 ? -13.463 2.766   7.551   1.00 32.59 ? 183  GLN B CA  1 
ATOM   3649 C  C   . GLN B 2 183 ? -12.562 1.679   8.127   1.00 25.81 ? 183  GLN B C   1 
ATOM   3650 O  O   . GLN B 2 183 ? -11.494 1.392   7.579   1.00 27.24 ? 183  GLN B O   1 
ATOM   3651 C  CB  . GLN B 2 183 ? -13.404 4.038   8.399   1.00 34.10 ? 183  GLN B CB  1 
ATOM   3652 C  CG  . GLN B 2 183 ? -12.166 4.870   8.193   1.00 37.33 ? 183  GLN B CG  1 
ATOM   3653 C  CD  . GLN B 2 183 ? -12.102 6.053   9.144   1.00 38.22 ? 183  GLN B CD  1 
ATOM   3654 O  OE1 . GLN B 2 183 ? -11.018 6.507   9.519   1.00 38.08 ? 183  GLN B OE1 1 
ATOM   3655 N  NE2 . GLN B 2 183 ? -13.268 6.557   9.543   1.00 41.20 ? 183  GLN B NE2 1 
ATOM   3656 N  N   . ALA B 2 184 ? -12.971 1.069   9.243   1.00 27.84 ? 184  ALA B N   1 
ATOM   3657 C  CA  . ALA B 2 184 ? -12.187 -0.023  9.814   1.00 29.84 ? 184  ALA B CA  1 
ATOM   3658 C  C   . ALA B 2 184 ? -12.149 -1.222  8.875   1.00 30.06 ? 184  ALA B C   1 
ATOM   3659 O  O   . ALA B 2 184 ? -11.120 -1.909  8.769   1.00 25.47 ? 184  ALA B O   1 
ATOM   3660 C  CB  . ALA B 2 184 ? -12.756 -0.434  11.172  1.00 29.72 ? 184  ALA B CB  1 
ATOM   3661 N  N   . ALA B 2 185 ? -13.268 -1.502  8.199   1.00 23.92 ? 185  ALA B N   1 
ATOM   3662 C  CA  . ALA B 2 185 ? -13.282 -2.592  7.236   1.00 26.18 ? 185  ALA B CA  1 
ATOM   3663 C  C   . ALA B 2 185 ? -12.281 -2.338  6.119   1.00 25.30 ? 185  ALA B C   1 
ATOM   3664 O  O   . ALA B 2 185 ? -11.572 -3.254  5.689   1.00 22.97 ? 185  ALA B O   1 
ATOM   3665 C  CB  . ALA B 2 185 ? -14.690 -2.785  6.667   1.00 28.10 ? 185  ALA B CB  1 
ATOM   3666 N  N   . ASP B 2 186 ? -12.190 -1.094  5.652   1.00 25.81 ? 186  ASP B N   1 
ATOM   3667 C  CA  . ASP B 2 186 ? -11.235 -0.784  4.597   1.00 25.53 ? 186  ASP B CA  1 
ATOM   3668 C  C   . ASP B 2 186 ? -9.802  -0.912  5.106   1.00 23.96 ? 186  ASP B C   1 
ATOM   3669 O  O   . ASP B 2 186 ? -8.924  -1.407  4.391   1.00 23.44 ? 186  ASP B O   1 
ATOM   3670 C  CB  . ASP B 2 186 ? -11.513 0.616   4.051   1.00 27.84 ? 186  ASP B CB  1 
ATOM   3671 C  CG  . ASP B 2 186 ? -10.681 0.945   2.850   1.00 31.24 ? 186  ASP B CG  1 
ATOM   3672 O  OD1 . ASP B 2 186 ? -10.661 0.141   1.899   1.00 39.46 ? 186  ASP B OD1 1 
ATOM   3673 O  OD2 . ASP B 2 186 ? -10.057 2.019   2.845   1.00 36.96 ? 186  ASP B OD2 1 
ATOM   3674 N  N   . GLN B 2 187 ? -9.555  -0.493  6.347   1.00 26.07 ? 187  GLN B N   1 
ATOM   3675 C  CA  . GLN B 2 187 ? -8.224  -0.622  6.932   1.00 24.03 ? 187  GLN B CA  1 
ATOM   3676 C  C   . GLN B 2 187 ? -7.834  -2.088  7.116   1.00 23.81 ? 187  GLN B C   1 
ATOM   3677 O  O   . GLN B 2 187 ? -6.679  -2.462  6.888   1.00 20.85 ? 187  GLN B O   1 
ATOM   3678 C  CB  . GLN B 2 187 ? -8.181  0.129   8.260   1.00 24.42 ? 187  GLN B CB  1 
ATOM   3679 C  CG  . GLN B 2 187 ? -8.052  1.648   8.063   1.00 26.45 ? 187  GLN B CG  1 
ATOM   3680 C  CD  . GLN B 2 187 ? -6.726  2.007   7.412   1.00 27.00 ? 187  GLN B CD  1 
ATOM   3681 O  OE1 . GLN B 2 187 ? -5.675  1.840   8.014   1.00 26.17 ? 187  GLN B OE1 1 
ATOM   3682 N  NE2 . GLN B 2 187 ? -6.775  2.494   6.174   1.00 27.49 ? 187  GLN B NE2 1 
ATOM   3683 N  N   . ILE B 2 188 ? -8.787  -2.930  7.522   1.00 23.53 ? 188  ILE B N   1 
ATOM   3684 C  CA  . ILE B 2 188 ? -8.537  -4.368  7.648   1.00 20.50 ? 188  ILE B CA  1 
ATOM   3685 C  C   . ILE B 2 188 ? -8.147  -4.966  6.297   1.00 19.62 ? 188  ILE B C   1 
ATOM   3686 O  O   . ILE B 2 188 ? -7.197  -5.757  6.192   1.00 18.43 ? 188  ILE B O   1 
ATOM   3687 C  CB  . ILE B 2 188 ? -9.777  -5.054  8.242   1.00 21.09 ? 188  ILE B CB  1 
ATOM   3688 C  CG1 . ILE B 2 188 ? -9.895  -4.717  9.734   1.00 19.68 ? 188  ILE B CG1 1 
ATOM   3689 C  CG2 . ILE B 2 188 ? -9.758  -6.554  7.972   1.00 21.02 ? 188  ILE B CG2 1 
ATOM   3690 C  CD1 . ILE B 2 188 ? -11.144 -5.273  10.399  1.00 23.18 ? 188  ILE B CD1 1 
ATOM   3691 N  N   . THR B 2 189 ? -8.867  -4.583  5.239   1.00 19.90 ? 189  THR B N   1 
ATOM   3692 C  CA  . THR B 2 189 ? -8.523  -5.036  3.891   1.00 20.85 ? 189  THR B CA  1 
ATOM   3693 C  C   . THR B 2 189 ? -7.101  -4.631  3.511   1.00 20.04 ? 189  THR B C   1 
ATOM   3694 O  O   . THR B 2 189 ? -6.341  -5.440  2.966   1.00 19.18 ? 189  THR B O   1 
ATOM   3695 C  CB  . THR B 2 189 ? -9.534  -4.480  2.887   1.00 21.84 ? 189  THR B CB  1 
ATOM   3696 O  OG1 . THR B 2 189 ? -10.823 -5.007  3.187   1.00 21.86 ? 189  THR B OG1 1 
ATOM   3697 C  CG2 . THR B 2 189 ? -9.165  -4.828  1.442   1.00 18.78 ? 189  THR B CG2 1 
ATOM   3698 N  N   . LYS B 2 190 ? -6.731  -3.364  3.765   1.00 20.36 ? 190  LYS B N   1 
ATOM   3699 C  CA  . LYS B 2 190 ? -5.392  -2.896  3.408   1.00 19.85 ? 190  LYS B CA  1 
ATOM   3700 C  C   . LYS B 2 190 ? -4.319  -3.591  4.238   1.00 18.70 ? 190  LYS B C   1 
ATOM   3701 O  O   . LYS B 2 190 ? -3.231  -3.885  3.730   1.00 16.78 ? 190  LYS B O   1 
ATOM   3702 C  CB  . LYS B 2 190 ? -5.301  -1.373  3.570   1.00 22.39 ? 190  LYS B CB  1 
ATOM   3703 C  CG  . LYS B 2 190 ? -6.026  -0.581  2.449   1.00 24.97 ? 190  LYS B CG  1 
ATOM   3704 C  CD  . LYS B 2 190 ? -6.332  0.857   2.853   1.00 28.16 ? 190  LYS B CD  1 
ATOM   3705 C  CE  . LYS B 2 190 ? -7.042  1.597   1.727   1.00 31.95 ? 190  LYS B CE  1 
ATOM   3706 N  NZ  . LYS B 2 190 ? -6.371  1.344   0.424   1.00 29.38 ? 190  LYS B NZ  1 
ATOM   3707 N  N   . LEU B 2 191 ? -4.603  -3.850  5.516   1.00 18.91 ? 191  LEU B N   1 
ATOM   3708 C  CA  . LEU B 2 191 ? -3.665  -4.590  6.358   1.00 19.82 ? 191  LEU B CA  1 
ATOM   3709 C  C   . LEU B 2 191 ? -3.495  -6.026  5.869   1.00 15.91 ? 191  LEU B C   1 
ATOM   3710 O  O   . LEU B 2 191 ? -2.378  -6.542  5.842   1.00 16.73 ? 191  LEU B O   1 
ATOM   3711 C  CB  . LEU B 2 191 ? -4.140  -4.591  7.809   1.00 19.09 ? 191  LEU B CB  1 
ATOM   3712 C  CG  . LEU B 2 191 ? -3.835  -3.403  8.716   1.00 20.57 ? 191  LEU B CG  1 
ATOM   3713 C  CD1 . LEU B 2 191 ? -4.692  -3.501  9.962   1.00 18.97 ? 191  LEU B CD1 1 
ATOM   3714 C  CD2 . LEU B 2 191 ? -2.374  -3.396  9.092   1.00 17.90 ? 191  LEU B CD2 1 
ATOM   3715 N  N   . TYR B 2 192 ? -4.585  -6.676  5.463   1.00 18.11 ? 192  TYR B N   1 
ATOM   3716 C  CA  . TYR B 2 192 ? -4.470  -8.030  4.928   1.00 18.05 ? 192  TYR B CA  1 
ATOM   3717 C  C   . TYR B 2 192 ? -3.598  -8.054  3.683   1.00 18.29 ? 192  TYR B C   1 
ATOM   3718 O  O   . TYR B 2 192 ? -2.728  -8.918  3.539   1.00 16.69 ? 192  TYR B O   1 
ATOM   3719 C  CB  . TYR B 2 192 ? -5.843  -8.617  4.617   1.00 17.54 ? 192  TYR B CB  1 
ATOM   3720 C  CG  . TYR B 2 192 ? -5.724  -9.969  3.939   1.00 18.74 ? 192  TYR B CG  1 
ATOM   3721 C  CD1 . TYR B 2 192 ? -5.398  -11.104 4.671   1.00 20.14 ? 192  TYR B CD1 1 
ATOM   3722 C  CD2 . TYR B 2 192 ? -5.893  -10.101 2.572   1.00 18.75 ? 192  TYR B CD2 1 
ATOM   3723 C  CE1 . TYR B 2 192 ? -5.270  -12.344 4.061   1.00 17.55 ? 192  TYR B CE1 1 
ATOM   3724 C  CE2 . TYR B 2 192 ? -5.762  -11.341 1.949   1.00 20.88 ? 192  TYR B CE2 1 
ATOM   3725 C  CZ  . TYR B 2 192 ? -5.449  -12.456 2.706   1.00 18.50 ? 192  TYR B CZ  1 
ATOM   3726 O  OH  . TYR B 2 192 ? -5.319  -13.695 2.101   1.00 19.08 ? 192  TYR B OH  1 
ATOM   3727 N  N   . ASN B 2 193 ? -3.818  -7.104  2.769   1.00 20.28 ? 193  ASN B N   1 
ATOM   3728 C  CA  . ASN B 2 193 ? -3.041  -7.069  1.533   1.00 18.80 ? 193  ASN B CA  1 
ATOM   3729 C  C   . ASN B 2 193 ? -1.581  -6.721  1.805   1.00 17.68 ? 193  ASN B C   1 
ATOM   3730 O  O   . ASN B 2 193 ? -0.671  -7.273  1.171   1.00 18.12 ? 193  ASN B O   1 
ATOM   3731 C  CB  . ASN B 2 193 ? -3.703  -6.098  0.556   1.00 18.28 ? 193  ASN B CB  1 
ATOM   3732 C  CG  . ASN B 2 193 ? -5.017  -6.652  0.028   1.00 26.32 ? 193  ASN B CG  1 
ATOM   3733 O  OD1 . ASN B 2 193 ? -5.187  -7.876  -0.040  1.00 25.82 ? 193  ASN B OD1 1 
ATOM   3734 N  ND2 . ASN B 2 193 ? -5.958  -5.771  -0.324  1.00 22.48 ? 193  ASN B ND2 1 
ATOM   3735 N  N   . LEU B 2 194 ? -1.335  -5.834  2.770   1.00 19.43 ? 194  LEU B N   1 
ATOM   3736 C  CA  . LEU B 2 194 ? 0.029   -5.605  3.236   1.00 18.91 ? 194  LEU B CA  1 
ATOM   3737 C  C   . LEU B 2 194 ? 0.658   -6.914  3.713   1.00 16.30 ? 194  LEU B C   1 
ATOM   3738 O  O   . LEU B 2 194 ? 1.727   -7.313  3.246   1.00 17.82 ? 194  LEU B O   1 
ATOM   3739 C  CB  . LEU B 2 194 ? 0.015   -4.554  4.356   1.00 16.22 ? 194  LEU B CB  1 
ATOM   3740 C  CG  . LEU B 2 194 ? 1.361   -4.323  5.046   1.00 19.88 ? 194  LEU B CG  1 
ATOM   3741 C  CD1 . LEU B 2 194 ? 2.409   -3.844  4.034   1.00 20.84 ? 194  LEU B CD1 1 
ATOM   3742 C  CD2 . LEU B 2 194 ? 1.221   -3.340  6.196   1.00 20.52 ? 194  LEU B CD2 1 
ATOM   3743 N  N   . PHE B 2 195 ? -0.013  -7.595  4.646   1.00 15.29 ? 195  PHE B N   1 
ATOM   3744 C  CA  . PHE B 2 195 ? 0.409   -8.900  5.149   1.00 15.97 ? 195  PHE B CA  1 
ATOM   3745 C  C   . PHE B 2 195 ? 0.865   -9.842  4.036   1.00 16.87 ? 195  PHE B C   1 
ATOM   3746 O  O   . PHE B 2 195 ? 1.919   -10.485 4.142   1.00 14.90 ? 195  PHE B O   1 
ATOM   3747 C  CB  . PHE B 2 195 ? -0.767  -9.474  5.949   1.00 14.68 ? 195  PHE B CB  1 
ATOM   3748 C  CG  . PHE B 2 195 ? -0.687  -10.944 6.243   1.00 17.70 ? 195  PHE B CG  1 
ATOM   3749 C  CD1 . PHE B 2 195 ? -0.092  -11.401 7.411   1.00 15.89 ? 195  PHE B CD1 1 
ATOM   3750 C  CD2 . PHE B 2 195 ? -1.274  -11.870 5.380   1.00 14.88 ? 195  PHE B CD2 1 
ATOM   3751 C  CE1 . PHE B 2 195 ? -0.042  -12.761 7.702   1.00 17.77 ? 195  PHE B CE1 1 
ATOM   3752 C  CE2 . PHE B 2 195 ? -1.231  -13.224 5.663   1.00 14.50 ? 195  PHE B CE2 1 
ATOM   3753 C  CZ  . PHE B 2 195 ? -0.627  -13.676 6.829   1.00 15.66 ? 195  PHE B CZ  1 
ATOM   3754 N  N   . LEU B 2 196 ? 0.096   -9.912  2.946   1.00 14.85 ? 196  LEU B N   1 
ATOM   3755 C  CA  . LEU B 2 196 ? 0.471   -10.796 1.842   1.00 20.33 ? 196  LEU B CA  1 
ATOM   3756 C  C   . LEU B 2 196 ? 1.672   -10.263 1.075   1.00 18.07 ? 196  LEU B C   1 
ATOM   3757 O  O   . LEU B 2 196 ? 2.568   -11.029 0.705   1.00 16.19 ? 196  LEU B O   1 
ATOM   3758 C  CB  . LEU B 2 196 ? -0.703  -10.988 0.880   1.00 16.70 ? 196  LEU B CB  1 
ATOM   3759 C  CG  . LEU B 2 196 ? -1.845  -11.891 1.316   1.00 19.80 ? 196  LEU B CG  1 
ATOM   3760 C  CD1 . LEU B 2 196 ? -2.861  -11.983 0.183   1.00 18.73 ? 196  LEU B CD1 1 
ATOM   3761 C  CD2 . LEU B 2 196 ? -1.317  -13.281 1.680   1.00 20.34 ? 196  LEU B CD2 1 
ATOM   3762 N  N   . LYS B 2 197 ? 1.678   -8.965  0.774   1.00 17.69 ? 197  LYS B N   1 
ATOM   3763 C  CA  . LYS B 2 197 ? 2.726   -8.406  -0.080  1.00 18.34 ? 197  LYS B CA  1 
ATOM   3764 C  C   . LYS B 2 197 ? 4.109   -8.580  0.529   1.00 16.15 ? 197  LYS B C   1 
ATOM   3765 O  O   . LYS B 2 197 ? 5.091   -8.764  -0.196  1.00 17.49 ? 197  LYS B O   1 
ATOM   3766 C  CB  . LYS B 2 197 ? 2.448   -6.924  -0.331  1.00 17.60 ? 197  LYS B CB  1 
ATOM   3767 C  CG  . LYS B 2 197 ? 3.552   -6.180  -1.076  1.00 20.88 ? 197  LYS B CG  1 
ATOM   3768 C  CD  . LYS B 2 197 ? 3.220   -4.695  -1.123  1.00 16.28 ? 197  LYS B CD  1 
ATOM   3769 C  CE  . LYS B 2 197 ? 4.179   -3.939  -2.021  1.00 21.50 ? 197  LYS B CE  1 
ATOM   3770 N  NZ  . LYS B 2 197 ? 3.781   -2.503  -2.098  1.00 16.75 ? 197  LYS B NZ  1 
ATOM   3771 N  N   . ILE B 2 198 ? 4.216   -8.545  1.854   1.00 15.05 ? 198  ILE B N   1 
ATOM   3772 C  CA  . ILE B 2 198 ? 5.522   -8.509  2.495   1.00 13.14 ? 198  ILE B CA  1 
ATOM   3773 C  C   . ILE B 2 198 ? 5.934   -9.870  3.047   1.00 16.30 ? 198  ILE B C   1 
ATOM   3774 O  O   . ILE B 2 198 ? 6.958   -9.966  3.715   1.00 14.83 ? 198  ILE B O   1 
ATOM   3775 C  CB  . ILE B 2 198 ? 5.557   -7.440  3.595   1.00 15.26 ? 198  ILE B CB  1 
ATOM   3776 C  CG1 . ILE B 2 198 ? 4.587   -7.801  4.720   1.00 15.57 ? 198  ILE B CG1 1 
ATOM   3777 C  CG2 . ILE B 2 198 ? 5.224   -6.081  2.995   1.00 14.87 ? 198  ILE B CG2 1 
ATOM   3778 C  CD1 . ILE B 2 198 ? 4.535   -6.728  5.855   1.00 18.27 ? 198  ILE B CD1 1 
ATOM   3779 N  N   . ASP B 2 199 ? 5.164   -10.928 2.768   1.00 17.95 ? 199  ASP B N   1 
ATOM   3780 C  CA  . ASP B 2 199 ? 5.461   -12.265 3.301   1.00 16.27 ? 199  ASP B CA  1 
ATOM   3781 C  C   . ASP B 2 199 ? 5.607   -12.222 4.817   1.00 16.93 ? 199  ASP B C   1 
ATOM   3782 O  O   . ASP B 2 199 ? 6.546   -12.773 5.399   1.00 16.50 ? 199  ASP B O   1 
ATOM   3783 C  CB  . ASP B 2 199 ? 6.705   -12.869 2.642   1.00 13.72 ? 199  ASP B CB  1 
ATOM   3784 C  CG  . ASP B 2 199 ? 6.405   -13.460 1.269   1.00 14.77 ? 199  ASP B CG  1 
ATOM   3785 O  OD1 . ASP B 2 199 ? 5.784   -14.549 1.205   1.00 13.69 ? 199  ASP B OD1 1 
ATOM   3786 O  OD2 . ASP B 2 199 ? 6.769   -12.823 0.253   1.00 15.12 ? 199  ASP B OD2 1 
ATOM   3787 N  N   . ALA B 2 200 ? 4.693   -11.506 5.457   1.00 13.57 ? 200  ALA B N   1 
ATOM   3788 C  CA  . ALA B 2 200 ? 4.586   -11.566 6.903   1.00 15.71 ? 200  ALA B CA  1 
ATOM   3789 C  C   . ALA B 2 200 ? 4.062   -12.933 7.320   1.00 17.09 ? 200  ALA B C   1 
ATOM   3790 O  O   . ALA B 2 200 ? 3.278   -13.570 6.605   1.00 14.01 ? 200  ALA B O   1 
ATOM   3791 C  CB  . ALA B 2 200 ? 3.652   -10.462 7.414   1.00 15.72 ? 200  ALA B CB  1 
ATOM   3792 N  N   . THR B 2 201 ? 4.534   -13.401 8.472   1.00 16.13 ? 201  THR B N   1 
ATOM   3793 C  CA  . THR B 2 201 ? 3.822   -14.443 9.190   1.00 18.47 ? 201  THR B CA  1 
ATOM   3794 C  C   . THR B 2 201 ? 2.792   -13.860 10.149  1.00 15.91 ? 201  THR B C   1 
ATOM   3795 O  O   . THR B 2 201 ? 1.827   -14.554 10.498  1.00 15.99 ? 201  THR B O   1 
ATOM   3796 C  CB  . THR B 2 201 ? 4.807   -15.356 9.954   1.00 17.25 ? 201  THR B CB  1 
ATOM   3797 O  OG1 . THR B 2 201 ? 5.464   -14.607 10.979  1.00 16.11 ? 201  THR B OG1 1 
ATOM   3798 C  CG2 . THR B 2 201 ? 5.868   -15.887 9.011   1.00 17.27 ? 201  THR B CG2 1 
ATOM   3799 N  N   . GLN B 2 202 ? 2.963   -12.601 10.564  1.00 16.03 ? 202  GLN B N   1 
ATOM   3800 C  CA  . GLN B 2 202 ? 1.947   -11.920 11.359  1.00 17.52 ? 202  GLN B CA  1 
ATOM   3801 C  C   . GLN B 2 202 ? 2.080   -10.404 11.204  1.00 16.99 ? 202  GLN B C   1 
ATOM   3802 O  O   . GLN B 2 202 ? 3.190   -9.858  11.208  1.00 18.20 ? 202  GLN B O   1 
ATOM   3803 C  CB  . GLN B 2 202 ? 2.047   -12.298 12.844  1.00 15.89 ? 202  GLN B CB  1 
ATOM   3804 C  CG  . GLN B 2 202 ? 0.935   -11.672 13.679  1.00 17.85 ? 202  GLN B CG  1 
ATOM   3805 C  CD  . GLN B 2 202 ? 0.951   -12.117 15.138  1.00 22.25 ? 202  GLN B CD  1 
ATOM   3806 O  OE1 . GLN B 2 202 ? 0.195   -13.003 15.520  1.00 24.90 ? 202  GLN B OE1 1 
ATOM   3807 N  NE2 . GLN B 2 202 ? 1.795   -11.491 15.955  1.00 20.45 ? 202  GLN B NE2 1 
ATOM   3808 N  N   . VAL B 2 203 ? 0.947   -9.733  11.058  1.00 16.97 ? 203  VAL B N   1 
ATOM   3809 C  CA  . VAL B 2 203 ? 0.871   -8.276  11.201  1.00 15.10 ? 203  VAL B CA  1 
ATOM   3810 C  C   . VAL B 2 203 ? -0.080  -8.046  12.355  1.00 19.00 ? 203  VAL B C   1 
ATOM   3811 O  O   . VAL B 2 203 ? -1.265  -8.393  12.259  1.00 17.28 ? 203  VAL B O   1 
ATOM   3812 C  CB  . VAL B 2 203 ? 0.379   -7.573  9.930   1.00 14.63 ? 203  VAL B CB  1 
ATOM   3813 C  CG1 . VAL B 2 203 ? 0.200   -6.052  10.183  1.00 18.93 ? 203  VAL B CG1 1 
ATOM   3814 C  CG2 . VAL B 2 203 ? 1.342   -7.812  8.788   1.00 15.09 ? 203  VAL B CG2 1 
ATOM   3815 N  N   . GLU B 2 204 ? 0.441   -7.525  13.462  1.00 15.93 ? 204  GLU B N   1 
ATOM   3816 C  CA  . GLU B 2 204 ? -0.318  -7.357  14.695  1.00 17.57 ? 204  GLU B CA  1 
ATOM   3817 C  C   . GLU B 2 204 ? -0.480  -5.869  14.974  1.00 16.78 ? 204  GLU B C   1 
ATOM   3818 O  O   . GLU B 2 204 ? 0.519   -5.173  15.172  1.00 19.24 ? 204  GLU B O   1 
ATOM   3819 C  CB  . GLU B 2 204 ? 0.391   -8.036  15.868  1.00 16.08 ? 204  GLU B CB  1 
ATOM   3820 C  CG  . GLU B 2 204 ? -0.300  -7.831  17.209  1.00 19.59 ? 204  GLU B CG  1 
ATOM   3821 C  CD  . GLU B 2 204 ? 0.312   -8.680  18.292  1.00 24.52 ? 204  GLU B CD  1 
ATOM   3822 O  OE1 . GLU B 2 204 ? 1.460   -8.396  18.666  1.00 24.46 ? 204  GLU B OE1 1 
ATOM   3823 O  OE2 . GLU B 2 204 ? -0.330  -9.658  18.735  1.00 25.74 ? 204  GLU B OE2 1 
ATOM   3824 N  N   . VAL B 2 205 ? -1.722  -5.391  15.002  1.00 16.34 ? 205  VAL B N   1 
ATOM   3825 C  CA  . VAL B 2 205 ? -2.020  -3.990  15.290  1.00 19.45 ? 205  VAL B CA  1 
ATOM   3826 C  C   . VAL B 2 205 ? -2.674  -3.915  16.666  1.00 19.83 ? 205  VAL B C   1 
ATOM   3827 O  O   . VAL B 2 205 ? -3.783  -4.430  16.856  1.00 20.76 ? 205  VAL B O   1 
ATOM   3828 C  CB  . VAL B 2 205 ? -2.921  -3.364  14.215  1.00 18.25 ? 205  VAL B CB  1 
ATOM   3829 C  CG1 . VAL B 2 205 ? -3.172  -1.870  14.529  1.00 17.56 ? 205  VAL B CG1 1 
ATOM   3830 C  CG2 . VAL B 2 205 ? -2.310  -3.533  12.833  1.00 15.40 ? 205  VAL B CG2 1 
ATOM   3831 N  N   . ASN B 2 206 ? -1.983  -3.256  17.630  1.00 18.92 ? 206  ASN B N   1 
ATOM   3832 C  CA  . ASN B 2 206 ? -2.473  -3.056  18.996  1.00 21.38 ? 206  ASN B CA  1 
ATOM   3833 C  C   . ASN B 2 206 ? -1.898  -1.790  19.625  1.00 21.41 ? 206  ASN B C   1 
ATOM   3834 O  O   . ASN B 2 206 ? -0.729  -1.776  20.027  1.00 24.55 ? 206  ASN B O   1 
ATOM   3835 C  CB  . ASN B 2 206 ? -2.128  -4.244  19.896  1.00 18.16 ? 206  ASN B CB  1 
ATOM   3836 C  CG  . ASN B 2 206 ? -3.020  -4.316  21.127  1.00 23.69 ? 206  ASN B CG  1 
ATOM   3837 O  OD1 . ASN B 2 206 ? -4.031  -3.630  21.202  1.00 21.63 ? 206  ASN B OD1 1 
ATOM   3838 N  ND2 . ASN B 2 206 ? -2.673  -5.189  22.073  1.00 23.01 ? 206  ASN B ND2 1 
ATOM   3839 N  N   . PRO B 2 207 ? -2.708  -0.739  19.810  1.00 22.81 ? 207  PRO B N   1 
ATOM   3840 C  CA  . PRO B 2 207 ? -4.140  -0.816  19.503  1.00 24.07 ? 207  PRO B CA  1 
ATOM   3841 C  C   . PRO B 2 207 ? -4.531  -0.378  18.094  1.00 21.23 ? 207  PRO B C   1 
ATOM   3842 O  O   . PRO B 2 207 ? -3.930  0.534   17.501  1.00 23.04 ? 207  PRO B O   1 
ATOM   3843 C  CB  . PRO B 2 207 ? -4.757  0.124   20.539  1.00 28.75 ? 207  PRO B CB  1 
ATOM   3844 C  CG  . PRO B 2 207 ? -3.699  1.164   20.746  1.00 23.09 ? 207  PRO B CG  1 
ATOM   3845 C  CD  . PRO B 2 207 ? -2.370  0.473   20.578  1.00 22.72 ? 207  PRO B CD  1 
ATOM   3846 N  N   . PHE B 2 208 ? -5.550  -1.060  17.578  1.00 20.21 ? 208  PHE B N   1 
ATOM   3847 C  CA  . PHE B 2 208 ? -6.265  -0.672  16.367  1.00 20.29 ? 208  PHE B CA  1 
ATOM   3848 C  C   . PHE B 2 208 ? -7.371  0.261   16.846  1.00 28.24 ? 208  PHE B C   1 
ATOM   3849 O  O   . PHE B 2 208 ? -8.305  -0.177  17.526  1.00 22.05 ? 208  PHE B O   1 
ATOM   3850 C  CB  . PHE B 2 208 ? -6.799  -1.918  15.652  1.00 23.37 ? 208  PHE B CB  1 
ATOM   3851 C  CG  . PHE B 2 208 ? -7.506  -1.648  14.334  1.00 24.19 ? 208  PHE B CG  1 
ATOM   3852 C  CD1 . PHE B 2 208 ? -6.872  -0.964  13.296  1.00 21.09 ? 208  PHE B CD1 1 
ATOM   3853 C  CD2 . PHE B 2 208 ? -8.789  -2.137  14.118  1.00 23.74 ? 208  PHE B CD2 1 
ATOM   3854 C  CE1 . PHE B 2 208 ? -7.527  -0.734  12.090  1.00 21.88 ? 208  PHE B CE1 1 
ATOM   3855 C  CE2 . PHE B 2 208 ? -9.456  -1.922  12.914  1.00 19.97 ? 208  PHE B CE2 1 
ATOM   3856 C  CZ  . PHE B 2 208 ? -8.828  -1.224  11.892  1.00 21.32 ? 208  PHE B CZ  1 
ATOM   3857 N  N   . GLY B 2 209 ? -7.231  1.554   16.558  1.00 29.20 ? 209  GLY B N   1 
ATOM   3858 C  CA  . GLY B 2 209 ? -7.855  2.590   17.358  1.00 28.64 ? 209  GLY B CA  1 
ATOM   3859 C  C   . GLY B 2 209 ? -8.783  3.523   16.602  1.00 32.95 ? 209  GLY B C   1 
ATOM   3860 O  O   . GLY B 2 209 ? -8.595  3.799   15.417  1.00 30.89 ? 209  GLY B O   1 
ATOM   3861 N  N   . GLU B 2 210 ? -9.769  4.033   17.322  1.00 34.13 ? 210  GLU B N   1 
ATOM   3862 C  CA  . GLU B 2 210 ? -10.706 5.025   16.826  1.00 38.43 ? 210  GLU B CA  1 
ATOM   3863 C  C   . GLU B 2 210 ? -10.469 6.322   17.590  1.00 35.40 ? 210  GLU B C   1 
ATOM   3864 O  O   . GLU B 2 210 ? -10.436 6.319   18.825  1.00 35.14 ? 210  GLU B O   1 
ATOM   3865 C  CB  . GLU B 2 210 ? -12.137 4.511   16.999  1.00 42.48 ? 210  GLU B CB  1 
ATOM   3866 C  CG  . GLU B 2 210 ? -13.217 5.547   17.116  1.00 39.42 ? 210  GLU B CG  1 
ATOM   3867 C  CD  . GLU B 2 210 ? -14.589 4.897   17.177  1.00 50.08 ? 210  GLU B CD  1 
ATOM   3868 O  OE1 . GLU B 2 210 ? -14.677 3.677   16.904  1.00 45.93 ? 210  GLU B OE1 1 
ATOM   3869 O  OE2 . GLU B 2 210 ? -15.576 5.601   17.479  1.00 49.22 ? 210  GLU B OE2 1 
ATOM   3870 N  N   . THR B 2 211 ? -10.249 7.416   16.858  1.00 34.30 ? 211  THR B N   1 
ATOM   3871 C  CA  . THR B 2 211 ? -10.000 8.710   17.484  1.00 37.45 ? 211  THR B CA  1 
ATOM   3872 C  C   . THR B 2 211 ? -11.311 9.448   17.748  1.00 37.82 ? 211  THR B C   1 
ATOM   3873 O  O   . THR B 2 211 ? -12.331 9.174   17.107  1.00 32.38 ? 211  THR B O   1 
ATOM   3874 C  CB  . THR B 2 211 ? -9.102  9.561   16.593  1.00 34.82 ? 211  THR B CB  1 
ATOM   3875 O  OG1 . THR B 2 211 ? -9.881  10.093  15.522  1.00 35.64 ? 211  THR B OG1 1 
ATOM   3876 C  CG2 . THR B 2 211 ? -7.972  8.732   16.018  1.00 32.17 ? 211  THR B CG2 1 
ATOM   3877 N  N   . PRO B 2 212 ? -11.323 10.394  18.698  1.00 37.85 ? 212  PRO B N   1 
ATOM   3878 C  CA  . PRO B 2 212 ? -12.552 11.177  18.933  1.00 41.89 ? 212  PRO B CA  1 
ATOM   3879 C  C   . PRO B 2 212 ? -13.104 11.834  17.677  1.00 40.66 ? 212  PRO B C   1 
ATOM   3880 O  O   . PRO B 2 212 ? -14.323 11.984  17.549  1.00 41.02 ? 212  PRO B O   1 
ATOM   3881 C  CB  . PRO B 2 212 ? -12.109 12.226  19.965  1.00 41.16 ? 212  PRO B CB  1 
ATOM   3882 C  CG  . PRO B 2 212 ? -10.944 11.625  20.650  1.00 39.92 ? 212  PRO B CG  1 
ATOM   3883 C  CD  . PRO B 2 212 ? -10.243 10.768  19.630  1.00 38.81 ? 212  PRO B CD  1 
ATOM   3884 N  N   . GLU B 2 213 ? -12.242 12.214  16.737  1.00 38.13 ? 213  GLU B N   1 
ATOM   3885 C  CA  . GLU B 2 213 ? -12.658 12.865  15.507  1.00 38.58 ? 213  GLU B CA  1 
ATOM   3886 C  C   . GLU B 2 213 ? -13.211 11.887  14.472  1.00 37.60 ? 213  GLU B C   1 
ATOM   3887 O  O   . GLU B 2 213 ? -13.516 12.309  13.354  1.00 40.23 ? 213  GLU B O   1 
ATOM   3888 C  CB  . GLU B 2 213 ? -11.482 13.648  14.911  1.00 41.47 ? 213  GLU B CB  1 
ATOM   3889 C  CG  . GLU B 2 213 ? -10.794 14.610  15.882  1.00 39.75 ? 213  GLU B CG  1 
ATOM   3890 C  CD  . GLU B 2 213 ? -9.762  13.928  16.781  1.00 50.49 ? 213  GLU B CD  1 
ATOM   3891 O  OE1 . GLU B 2 213 ? -10.082 13.635  17.952  1.00 44.55 ? 213  GLU B OE1 1 
ATOM   3892 O  OE2 . GLU B 2 213 ? -8.627  13.680  16.312  1.00 57.49 ? 213  GLU B OE2 1 
ATOM   3893 N  N   . GLY B 2 214 ? -13.339 10.606  14.806  1.00 33.91 ? 214  GLY B N   1 
ATOM   3894 C  CA  . GLY B 2 214 ? -13.927 9.645   13.891  1.00 33.99 ? 214  GLY B CA  1 
ATOM   3895 C  C   . GLY B 2 214 ? -12.973 9.041   12.882  1.00 36.52 ? 214  GLY B C   1 
ATOM   3896 O  O   . GLY B 2 214 ? -13.370 8.772   11.742  1.00 37.10 ? 214  GLY B O   1 
ATOM   3897 N  N   . GLN B 2 215 ? -11.724 8.806   13.274  1.00 37.49 ? 215  GLN B N   1 
ATOM   3898 C  CA  . GLN B 2 215 ? -10.713 8.206   12.414  1.00 35.39 ? 215  GLN B CA  1 
ATOM   3899 C  C   . GLN B 2 215 ? -10.301 6.844   12.957  1.00 30.68 ? 215  GLN B C   1 
ATOM   3900 O  O   . GLN B 2 215 ? -10.118 6.678   14.164  1.00 30.16 ? 215  GLN B O   1 
ATOM   3901 C  CB  . GLN B 2 215 ? -9.479  9.103   12.316  1.00 40.26 ? 215  GLN B CB  1 
ATOM   3902 C  CG  . GLN B 2 215 ? -9.698  10.356  11.511  1.00 39.71 ? 215  GLN B CG  1 
ATOM   3903 C  CD  . GLN B 2 215 ? -9.304  10.168  10.073  1.00 42.67 ? 215  GLN B CD  1 
ATOM   3904 O  OE1 . GLN B 2 215 ? -8.242  10.624  9.647   1.00 48.96 ? 215  GLN B OE1 1 
ATOM   3905 N  NE2 . GLN B 2 215 ? -10.152 9.482   9.310   1.00 50.99 ? 215  GLN B NE2 1 
ATOM   3906 N  N   . VAL B 2 216 ? -10.164 5.873   12.066  1.00 30.30 ? 216  VAL B N   1 
ATOM   3907 C  CA  . VAL B 2 216 ? -9.620  4.564   12.420  1.00 29.41 ? 216  VAL B CA  1 
ATOM   3908 C  C   . VAL B 2 216 ? -8.130  4.594   12.109  1.00 25.27 ? 216  VAL B C   1 
ATOM   3909 O  O   . VAL B 2 216 ? -7.734  4.863   10.970  1.00 26.12 ? 216  VAL B O   1 
ATOM   3910 C  CB  . VAL B 2 216 ? -10.327 3.435   11.655  1.00 31.80 ? 216  VAL B CB  1 
ATOM   3911 C  CG1 . VAL B 2 216 ? -9.804  2.078   12.114  1.00 29.44 ? 216  VAL B CG1 1 
ATOM   3912 C  CG2 . VAL B 2 216 ? -11.827 3.521   11.857  1.00 29.95 ? 216  VAL B CG2 1 
ATOM   3913 N  N   . VAL B 2 217 ? -7.306  4.326   13.119  1.00 23.84 ? 217  VAL B N   1 
ATOM   3914 C  CA  . VAL B 2 217 ? -5.862  4.499   13.041  1.00 24.93 ? 217  VAL B CA  1 
ATOM   3915 C  C   . VAL B 2 217 ? -5.175  3.277   13.641  1.00 25.16 ? 217  VAL B C   1 
ATOM   3916 O  O   . VAL B 2 217 ? -5.618  2.751   14.670  1.00 25.20 ? 217  VAL B O   1 
ATOM   3917 C  CB  . VAL B 2 217 ? -5.424  5.781   13.787  1.00 25.21 ? 217  VAL B CB  1 
ATOM   3918 C  CG1 . VAL B 2 217 ? -3.906  5.932   13.767  1.00 24.11 ? 217  VAL B CG1 1 
ATOM   3919 C  CG2 . VAL B 2 217 ? -6.109  7.001   13.184  1.00 24.28 ? 217  VAL B CG2 1 
ATOM   3920 N  N   . CYS B 2 218 ? -4.080  2.835   13.006  1.00 18.35 ? 218  CYS B N   1 
ATOM   3921 C  CA  . CYS B 2 218 ? -3.168  1.861   13.612  1.00 22.41 ? 218  CYS B CA  1 
ATOM   3922 C  C   . CYS B 2 218 ? -2.161  2.626   14.463  1.00 21.48 ? 218  CYS B C   1 
ATOM   3923 O  O   . CYS B 2 218 ? -1.221  3.230   13.941  1.00 24.26 ? 218  CYS B O   1 
ATOM   3924 C  CB  . CYS B 2 218 ? -2.474  1.016   12.544  1.00 19.73 ? 218  CYS B CB  1 
ATOM   3925 S  SG  . CYS B 2 218 ? -3.633  0.147   11.466  1.00 20.95 ? 218  CYS B SG  1 
ATOM   3926 N  N   . PHE B 2 219 ? -2.353  2.601   15.785  1.00 19.45 ? 219  PHE B N   1 
ATOM   3927 C  CA  . PHE B 2 219 ? -1.507  3.398   16.667  1.00 27.69 ? 219  PHE B CA  1 
ATOM   3928 C  C   . PHE B 2 219 ? -0.144  2.755   16.880  1.00 26.40 ? 219  PHE B C   1 
ATOM   3929 O  O   . PHE B 2 219 ? 0.865   3.459   16.977  1.00 23.46 ? 219  PHE B O   1 
ATOM   3930 C  CB  . PHE B 2 219 ? -2.196  3.614   18.016  1.00 27.17 ? 219  PHE B CB  1 
ATOM   3931 C  CG  . PHE B 2 219 ? -3.240  4.696   18.000  1.00 28.10 ? 219  PHE B CG  1 
ATOM   3932 C  CD1 . PHE B 2 219 ? -4.519  4.438   17.523  1.00 29.03 ? 219  PHE B CD1 1 
ATOM   3933 C  CD2 . PHE B 2 219 ? -2.952  5.960   18.481  1.00 28.39 ? 219  PHE B CD2 1 
ATOM   3934 C  CE1 . PHE B 2 219 ? -5.492  5.435   17.509  1.00 31.73 ? 219  PHE B CE1 1 
ATOM   3935 C  CE2 . PHE B 2 219 ? -3.922  6.961   18.475  1.00 32.80 ? 219  PHE B CE2 1 
ATOM   3936 C  CZ  . PHE B 2 219 ? -5.191  6.695   17.983  1.00 32.86 ? 219  PHE B CZ  1 
ATOM   3937 N  N   . ASP B 2 220 ? -0.101  1.424   16.971  1.00 24.30 ? 220  ASP B N   1 
ATOM   3938 C  CA  . ASP B 2 220 ? 1.137   0.687   17.178  1.00 20.74 ? 220  ASP B CA  1 
ATOM   3939 C  C   . ASP B 2 220 ? 0.969   -0.668  16.517  1.00 22.88 ? 220  ASP B C   1 
ATOM   3940 O  O   . ASP B 2 220 ? -0.132  -1.228  16.506  1.00 19.26 ? 220  ASP B O   1 
ATOM   3941 C  CB  . ASP B 2 220 ? 1.482   0.512   18.669  1.00 20.91 ? 220  ASP B CB  1 
ATOM   3942 C  CG  . ASP B 2 220 ? 1.832   1.841   19.354  1.00 31.65 ? 220  ASP B CG  1 
ATOM   3943 O  OD1 . ASP B 2 220 ? 2.833   2.477   18.965  1.00 33.95 ? 220  ASP B OD1 1 
ATOM   3944 O  OD2 . ASP B 2 220 ? 1.084   2.264   20.259  1.00 38.05 ? 220  ASP B OD2 1 
ATOM   3945 N  N   . ALA B 2 221 ? 2.061   -1.185  15.961  1.00 20.32 ? 221  ALA B N   1 
ATOM   3946 C  CA  . ALA B 2 221 ? 1.987   -2.440  15.233  1.00 18.04 ? 221  ALA B CA  1 
ATOM   3947 C  C   . ALA B 2 221 ? 3.298   -3.193  15.395  1.00 20.76 ? 221  ALA B C   1 
ATOM   3948 O  O   . ALA B 2 221 ? 4.341   -2.612  15.707  1.00 17.91 ? 221  ALA B O   1 
ATOM   3949 C  CB  . ALA B 2 221 ? 1.667   -2.211  13.751  1.00 20.86 ? 221  ALA B CB  1 
ATOM   3950 N  N   . LYS B 2 222 ? 3.221   -4.507  15.192  1.00 17.62 ? 222  LYS B N   1 
ATOM   3951 C  CA  . LYS B 2 222 ? 4.380   -5.384  15.233  1.00 20.06 ? 222  LYS B CA  1 
ATOM   3952 C  C   . LYS B 2 222 ? 4.236   -6.374  14.088  1.00 21.91 ? 222  LYS B C   1 
ATOM   3953 O  O   . LYS B 2 222 ? 3.178   -6.996  13.946  1.00 19.93 ? 222  LYS B O   1 
ATOM   3954 C  CB  . LYS B 2 222 ? 4.474   -6.118  16.579  1.00 25.23 ? 222  LYS B CB  1 
ATOM   3955 C  CG  . LYS B 2 222 ? 5.672   -7.035  16.692  1.00 26.03 ? 222  LYS B CG  1 
ATOM   3956 C  CD  . LYS B 2 222 ? 6.630   -6.553  17.751  1.00 37.99 ? 222  LYS B CD  1 
ATOM   3957 N  N   . ILE B 2 223 ? 5.276   -6.495  13.264  1.00 16.70 ? 223  ILE B N   1 
ATOM   3958 C  CA  . ILE B 2 223 ? 5.269   -7.363  12.090  1.00 18.71 ? 223  ILE B CA  1 
ATOM   3959 C  C   . ILE B 2 223 ? 6.363   -8.412  12.248  1.00 20.71 ? 223  ILE B C   1 
ATOM   3960 O  O   . ILE B 2 223 ? 7.519   -8.070  12.527  1.00 19.76 ? 223  ILE B O   1 
ATOM   3961 C  CB  . ILE B 2 223 ? 5.471   -6.566  10.787  1.00 17.12 ? 223  ILE B CB  1 
ATOM   3962 C  CG1 . ILE B 2 223 ? 4.499   -5.391  10.709  1.00 18.64 ? 223  ILE B CG1 1 
ATOM   3963 C  CG2 . ILE B 2 223 ? 5.293   -7.473  9.558   1.00 16.83 ? 223  ILE B CG2 1 
ATOM   3964 C  CD1 . ILE B 2 223 ? 4.683   -4.529  9.469   1.00 22.59 ? 223  ILE B CD1 1 
ATOM   3965 N  N   . ASN B 2 224 ? 5.987   -9.682  12.071  1.00 18.28 ? 224  ASN B N   1 
ATOM   3966 C  CA  . ASN B 2 224 ? 6.907   -10.811 11.967  1.00 17.96 ? 224  ASN B CA  1 
ATOM   3967 C  C   . ASN B 2 224 ? 6.986   -11.224 10.508  1.00 17.00 ? 224  ASN B C   1 
ATOM   3968 O  O   . ASN B 2 224 ? 5.950   -11.362 9.849   1.00 15.90 ? 224  ASN B O   1 
ATOM   3969 C  CB  . ASN B 2 224 ? 6.439   -12.022 12.785  1.00 14.38 ? 224  ASN B CB  1 
ATOM   3970 C  CG  . ASN B 2 224 ? 6.176   -11.680 14.225  1.00 22.38 ? 224  ASN B CG  1 
ATOM   3971 O  OD1 . ASN B 2 224 ? 6.742   -10.723 14.755  1.00 26.73 ? 224  ASN B OD1 1 
ATOM   3972 N  ND2 . ASN B 2 224 ? 5.310   -12.451 14.871  1.00 21.68 ? 224  ASN B ND2 1 
ATOM   3973 N  N   . PHE B 2 225 ? 8.204   -11.442 10.017  1.00 16.59 ? 225  PHE B N   1 
ATOM   3974 C  CA  . PHE B 2 225 ? 8.429   -11.766 8.618   1.00 16.06 ? 225  PHE B CA  1 
ATOM   3975 C  C   . PHE B 2 225 ? 8.839   -13.227 8.481   1.00 14.34 ? 225  PHE B C   1 
ATOM   3976 O  O   . PHE B 2 225 ? 9.441   -13.807 9.385   1.00 18.50 ? 225  PHE B O   1 
ATOM   3977 C  CB  . PHE B 2 225 ? 9.501   -10.849 8.007   1.00 16.98 ? 225  PHE B CB  1 
ATOM   3978 C  CG  . PHE B 2 225 ? 9.110   -9.391  7.984   1.00 17.35 ? 225  PHE B CG  1 
ATOM   3979 C  CD1 . PHE B 2 225 ? 9.406   -8.563  9.053   1.00 16.90 ? 225  PHE B CD1 1 
ATOM   3980 C  CD2 . PHE B 2 225 ? 8.416   -8.866  6.907   1.00 18.00 ? 225  PHE B CD2 1 
ATOM   3981 C  CE1 . PHE B 2 225 ? 9.037   -7.232  9.040   1.00 16.53 ? 225  PHE B CE1 1 
ATOM   3982 C  CE2 . PHE B 2 225 ? 8.040   -7.540  6.887   1.00 18.77 ? 225  PHE B CE2 1 
ATOM   3983 C  CZ  . PHE B 2 225 ? 8.355   -6.719  7.950   1.00 16.49 ? 225  PHE B CZ  1 
ATOM   3984 N  N   . ASP B 2 226 ? 8.458   -13.823 7.354   1.00 14.08 ? 226  ASP B N   1 
ATOM   3985 C  CA  . ASP B 2 226 ? 8.844   -15.187 7.007   1.00 14.73 ? 226  ASP B CA  1 
ATOM   3986 C  C   . ASP B 2 226 ? 10.281  -15.178 6.514   1.00 16.78 ? 226  ASP B C   1 
ATOM   3987 O  O   . ASP B 2 226 ? 10.554  -14.678 5.417   1.00 16.62 ? 226  ASP B O   1 
ATOM   3988 C  CB  . ASP B 2 226 ? 7.894   -15.733 5.942   1.00 13.51 ? 226  ASP B CB  1 
ATOM   3989 C  CG  . ASP B 2 226 ? 8.291   -17.103 5.438   1.00 15.24 ? 226  ASP B CG  1 
ATOM   3990 O  OD1 . ASP B 2 226 ? 9.192   -17.742 6.039   1.00 14.82 ? 226  ASP B OD1 1 
ATOM   3991 O  OD2 . ASP B 2 226 ? 7.691   -17.534 4.420   1.00 14.90 ? 226  ASP B OD2 1 
ATOM   3992 N  N   . ASP B 2 227 ? 11.199  -15.749 7.311   1.00 15.62 ? 227  ASP B N   1 
ATOM   3993 C  CA  . ASP B 2 227 ? 12.600  -15.826 6.896   1.00 20.50 ? 227  ASP B CA  1 
ATOM   3994 C  C   . ASP B 2 227 ? 12.759  -16.545 5.559   1.00 17.43 ? 227  ASP B C   1 
ATOM   3995 O  O   . ASP B 2 227 ? 13.721  -16.279 4.831   1.00 15.86 ? 227  ASP B O   1 
ATOM   3996 C  CB  . ASP B 2 227 ? 13.458  -16.524 7.966   1.00 19.45 ? 227  ASP B CB  1 
ATOM   3997 C  CG  . ASP B 2 227 ? 13.824  -15.606 9.121   1.00 26.64 ? 227  ASP B CG  1 
ATOM   3998 O  OD1 . ASP B 2 227 ? 13.856  -14.374 8.928   1.00 29.85 ? 227  ASP B OD1 1 
ATOM   3999 O  OD2 . ASP B 2 227 ? 14.090  -16.120 10.226  1.00 33.86 ? 227  ASP B OD2 1 
ATOM   4000 N  N   . ASN B 2 228 ? 11.822  -17.428 5.204   1.00 15.62 ? 228  ASN B N   1 
ATOM   4001 C  CA  . ASN B 2 228 ? 11.987  -18.182 3.965   1.00 16.47 ? 228  ASN B CA  1 
ATOM   4002 C  C   . ASN B 2 228 ? 11.760  -17.326 2.721   1.00 17.23 ? 228  ASN B C   1 
ATOM   4003 O  O   . ASN B 2 228 ? 12.115  -17.764 1.626   1.00 19.05 ? 228  ASN B O   1 
ATOM   4004 C  CB  . ASN B 2 228 ? 11.050  -19.409 3.930   1.00 13.61 ? 228  ASN B CB  1 
ATOM   4005 C  CG  . ASN B 2 228 ? 11.540  -20.562 4.824   1.00 17.63 ? 228  ASN B CG  1 
ATOM   4006 O  OD1 . ASN B 2 228 ? 12.592  -20.470 5.451   1.00 14.39 ? 228  ASN B OD1 1 
ATOM   4007 N  ND2 . ASN B 2 228 ? 10.771  -21.652 4.874   1.00 15.24 ? 228  ASN B ND2 1 
ATOM   4008 N  N   . ALA B 2 229 ? 11.195  -16.126 2.853   1.00 15.45 ? 229  ALA B N   1 
ATOM   4009 C  CA  . ALA B 2 229 ? 10.946  -15.257 1.710   1.00 15.77 ? 229  ALA B CA  1 
ATOM   4010 C  C   . ALA B 2 229 ? 11.935  -14.095 1.596   1.00 18.25 ? 229  ALA B C   1 
ATOM   4011 O  O   . ALA B 2 229 ? 11.695  -13.176 0.804   1.00 16.43 ? 229  ALA B O   1 
ATOM   4012 C  CB  . ALA B 2 229 ? 9.521   -14.706 1.773   1.00 15.34 ? 229  ALA B CB  1 
ATOM   4013 N  N   . GLU B 2 230 ? 13.022  -14.101 2.377   1.00 18.46 ? 230  GLU B N   1 
ATOM   4014 C  CA  . GLU B 2 230 ? 14.029  -13.053 2.256   1.00 17.96 ? 230  GLU B CA  1 
ATOM   4015 C  C   . GLU B 2 230 ? 14.469  -12.865 0.810   1.00 18.00 ? 230  GLU B C   1 
ATOM   4016 O  O   . GLU B 2 230 ? 14.662  -11.734 0.359   1.00 19.16 ? 230  GLU B O   1 
ATOM   4017 C  CB  . GLU B 2 230 ? 15.244  -13.374 3.119   1.00 20.91 ? 230  GLU B CB  1 
ATOM   4018 C  CG  . GLU B 2 230 ? 16.334  -12.312 2.976   1.00 22.39 ? 230  GLU B CG  1 
ATOM   4019 C  CD  . GLU B 2 230 ? 17.520  -12.564 3.869   1.00 29.84 ? 230  GLU B CD  1 
ATOM   4020 O  OE1 . GLU B 2 230 ? 17.456  -13.492 4.707   1.00 24.93 ? 230  GLU B OE1 1 
ATOM   4021 O  OE2 . GLU B 2 230 ? 18.521  -11.824 3.729   1.00 39.10 ? 230  GLU B OE2 1 
ATOM   4022 N  N   . PHE B 2 231 ? 14.584  -13.961 0.054   1.00 17.41 ? 231  PHE B N   1 
ATOM   4023 C  CA  . PHE B 2 231 ? 15.027  -13.857 -1.332  1.00 18.68 ? 231  PHE B CA  1 
ATOM   4024 C  C   . PHE B 2 231 ? 14.102  -12.982 -2.166  1.00 19.31 ? 231  PHE B C   1 
ATOM   4025 O  O   . PHE B 2 231 ? 14.528  -12.452 -3.194  1.00 21.83 ? 231  PHE B O   1 
ATOM   4026 C  CB  . PHE B 2 231 ? 15.168  -15.262 -1.957  1.00 25.09 ? 231  PHE B CB  1 
ATOM   4027 C  CG  . PHE B 2 231 ? 13.858  -15.909 -2.353  1.00 20.72 ? 231  PHE B CG  1 
ATOM   4028 C  CD1 . PHE B 2 231 ? 13.288  -15.664 -3.593  1.00 21.20 ? 231  PHE B CD1 1 
ATOM   4029 C  CD2 . PHE B 2 231 ? 13.223  -16.787 -1.499  1.00 19.48 ? 231  PHE B CD2 1 
ATOM   4030 C  CE1 . PHE B 2 231 ? 12.087  -16.252 -3.957  1.00 20.61 ? 231  PHE B CE1 1 
ATOM   4031 C  CE2 . PHE B 2 231 ? 12.029  -17.392 -1.867  1.00 18.44 ? 231  PHE B CE2 1 
ATOM   4032 C  CZ  . PHE B 2 231 ? 11.457  -17.117 -3.091  1.00 17.13 ? 231  PHE B CZ  1 
ATOM   4033 N  N   . ARG B 2 232 ? 12.845  -12.806 -1.760  1.00 17.39 ? 232  ARG B N   1 
ATOM   4034 C  CA  . ARG B 2 232 ? 11.962  -11.904 -2.482  1.00 18.42 ? 232  ARG B CA  1 
ATOM   4035 C  C   . ARG B 2 232 ? 11.535  -10.726 -1.622  1.00 17.72 ? 232  ARG B C   1 
ATOM   4036 O  O   . ARG B 2 232 ? 10.593  -10.012 -1.987  1.00 17.72 ? 232  ARG B O   1 
ATOM   4037 C  CB  . ARG B 2 232 ? 10.736  -12.642 -3.044  1.00 20.63 ? 232  ARG B CB  1 
ATOM   4038 C  CG  . ARG B 2 232 ? 9.800   -13.280 -2.034  1.00 17.38 ? 232  ARG B CG  1 
ATOM   4039 C  CD  . ARG B 2 232 ? 8.883   -14.291 -2.687  1.00 16.85 ? 232  ARG B CD  1 
ATOM   4040 N  NE  . ARG B 2 232 ? 7.800   -14.725 -1.798  1.00 16.97 ? 232  ARG B NE  1 
ATOM   4041 C  CZ  . ARG B 2 232 ? 7.011   -15.770 -2.027  1.00 18.09 ? 232  ARG B CZ  1 
ATOM   4042 N  NH1 . ARG B 2 232 ? 7.172   -16.502 -3.127  1.00 21.87 ? 232  ARG B NH1 1 
ATOM   4043 N  NH2 . ARG B 2 232 ? 6.047   -16.085 -1.161  1.00 15.77 ? 232  ARG B NH2 1 
ATOM   4044 N  N   . GLN B 2 233 ? 12.202  -10.505 -0.496  1.00 14.32 ? 233  GLN B N   1 
ATOM   4045 C  CA  . GLN B 2 233 ? 11.938  -9.351  0.359   1.00 19.27 ? 233  GLN B CA  1 
ATOM   4046 C  C   . GLN B 2 233 ? 13.253  -8.673  0.745   1.00 19.59 ? 233  GLN B C   1 
ATOM   4047 O  O   . GLN B 2 233 ? 13.457  -8.254  1.886   1.00 17.20 ? 233  GLN B O   1 
ATOM   4048 C  CB  . GLN B 2 233 ? 11.136  -9.760  1.593   1.00 16.06 ? 233  GLN B CB  1 
ATOM   4049 C  CG  . GLN B 2 233 ? 9.793   -10.427 1.296   1.00 16.59 ? 233  GLN B CG  1 
ATOM   4050 C  CD  . GLN B 2 233 ? 8.760   -9.467  0.688   1.00 15.68 ? 233  GLN B CD  1 
ATOM   4051 O  OE1 . GLN B 2 233 ? 8.945   -8.246  0.695   1.00 18.15 ? 233  GLN B OE1 1 
ATOM   4052 N  NE2 . GLN B 2 233 ? 7.672   -10.024 0.154   1.00 15.08 ? 233  GLN B NE2 1 
ATOM   4053 N  N   . LYS B 2 234 ? 14.173  -8.567  -0.216  1.00 20.23 ? 234  LYS B N   1 
ATOM   4054 C  CA  . LYS B 2 234 ? 15.507  -8.064  0.093   1.00 20.88 ? 234  LYS B CA  1 
ATOM   4055 C  C   . LYS B 2 234 ? 15.454  -6.656  0.692   1.00 19.87 ? 234  LYS B C   1 
ATOM   4056 O  O   . LYS B 2 234 ? 16.207  -6.344  1.623   1.00 22.26 ? 234  LYS B O   1 
ATOM   4057 C  CB  . LYS B 2 234 ? 16.368  -8.087  -1.170  1.00 21.72 ? 234  LYS B CB  1 
ATOM   4058 C  CG  . LYS B 2 234 ? 17.816  -7.719  -0.925  1.00 29.73 ? 234  LYS B CG  1 
ATOM   4059 N  N   . ASP B 2 235 ? 14.554  -5.802  0.195   1.00 20.74 ? 235  ASP B N   1 
ATOM   4060 C  CA  . ASP B 2 235 ? 14.487  -4.428  0.700   1.00 25.02 ? 235  ASP B CA  1 
ATOM   4061 C  C   . ASP B 2 235 ? 14.088  -4.391  2.166   1.00 22.95 ? 235  ASP B C   1 
ATOM   4062 O  O   . ASP B 2 235 ? 14.649  -3.619  2.955   1.00 19.84 ? 235  ASP B O   1 
ATOM   4063 C  CB  . ASP B 2 235 ? 13.488  -3.610  -0.106  1.00 24.89 ? 235  ASP B CB  1 
ATOM   4064 C  CG  . ASP B 2 235 ? 13.989  -3.283  -1.479  1.00 30.36 ? 235  ASP B CG  1 
ATOM   4065 O  OD1 . ASP B 2 235 ? 15.199  -3.483  -1.717  1.00 25.10 ? 235  ASP B OD1 1 
ATOM   4066 O  OD2 . ASP B 2 235 ? 13.168  -2.834  -2.301  1.00 29.90 ? 235  ASP B OD2 1 
ATOM   4067 N  N   . ILE B 2 236 ? 13.082  -5.184  2.536   1.00 21.45 ? 236  ILE B N   1 
ATOM   4068 C  CA  . ILE B 2 236 ? 12.654  -5.243  3.931   1.00 20.79 ? 236  ILE B CA  1 
ATOM   4069 C  C   . ILE B 2 236 ? 13.766  -5.814  4.805   1.00 21.26 ? 236  ILE B C   1 
ATOM   4070 O  O   . ILE B 2 236 ? 14.082  -5.274  5.872   1.00 21.55 ? 236  ILE B O   1 
ATOM   4071 C  CB  . ILE B 2 236 ? 11.355  -6.061  4.051   1.00 16.64 ? 236  ILE B CB  1 
ATOM   4072 C  CG1 . ILE B 2 236 ? 10.173  -5.261  3.490   1.00 24.72 ? 236  ILE B CG1 1 
ATOM   4073 C  CG2 . ILE B 2 236 ? 11.115  -6.485  5.481   1.00 15.67 ? 236  ILE B CG2 1 
ATOM   4074 C  CD1 . ILE B 2 236 ? 8.877   -6.073  3.370   1.00 18.92 ? 236  ILE B CD1 1 
ATOM   4075 N  N   . PHE B 2 237 ? 14.373  -6.923  4.377   1.00 20.59 ? 237  PHE B N   1 
ATOM   4076 C  CA  . PHE B 2 237 ? 15.403  -7.530  5.216   1.00 17.11 ? 237  PHE B CA  1 
ATOM   4077 C  C   . PHE B 2 237 ? 16.665  -6.680  5.286   1.00 20.72 ? 237  PHE B C   1 
ATOM   4078 O  O   . PHE B 2 237 ? 17.424  -6.806  6.251   1.00 20.82 ? 237  PHE B O   1 
ATOM   4079 C  CB  . PHE B 2 237 ? 15.731  -8.948  4.731   1.00 19.80 ? 237  PHE B CB  1 
ATOM   4080 C  CG  . PHE B 2 237 ? 14.739  -9.989  5.197   1.00 18.69 ? 237  PHE B CG  1 
ATOM   4081 C  CD1 . PHE B 2 237 ? 13.470  -10.065 4.625   1.00 23.41 ? 237  PHE B CD1 1 
ATOM   4082 C  CD2 . PHE B 2 237 ? 15.060  -10.867 6.217   1.00 22.13 ? 237  PHE B CD2 1 
ATOM   4083 C  CE1 . PHE B 2 237 ? 12.542  -11.017 5.054   1.00 19.23 ? 237  PHE B CE1 1 
ATOM   4084 C  CE2 . PHE B 2 237 ? 14.137  -11.819 6.664   1.00 24.70 ? 237  PHE B CE2 1 
ATOM   4085 C  CZ  . PHE B 2 237 ? 12.869  -11.890 6.070   1.00 21.17 ? 237  PHE B CZ  1 
ATOM   4086 N  N   . ALA B 2 238 ? 16.899  -5.799  4.311   1.00 20.33 ? 238  ALA B N   1 
ATOM   4087 C  CA  . ALA B 2 238 ? 18.006  -4.857  4.441   1.00 21.60 ? 238  ALA B CA  1 
ATOM   4088 C  C   . ALA B 2 238 ? 17.789  -3.874  5.586   1.00 25.73 ? 238  ALA B C   1 
ATOM   4089 O  O   . ALA B 2 238 ? 18.763  -3.311  6.093   1.00 21.88 ? 238  ALA B O   1 
ATOM   4090 C  CB  . ALA B 2 238 ? 18.218  -4.101  3.127   1.00 21.57 ? 238  ALA B CB  1 
ATOM   4091 N  N   . MET B 2 239 ? 16.537  -3.661  6.005   1.00 21.77 ? 239  MET B N   1 
ATOM   4092 C  CA  . MET B 2 239 ? 16.211  -2.783  7.124   1.00 23.58 ? 239  MET B CA  1 
ATOM   4093 C  C   . MET B 2 239 ? 16.342  -3.454  8.483   1.00 25.79 ? 239  MET B C   1 
ATOM   4094 O  O   . MET B 2 239 ? 16.084  -2.799  9.507   1.00 27.88 ? 239  MET B O   1 
ATOM   4095 C  CB  . MET B 2 239 ? 14.783  -2.257  6.980   1.00 27.74 ? 239  MET B CB  1 
ATOM   4096 C  CG  . MET B 2 239 ? 14.574  -1.335  5.800   1.00 24.98 ? 239  MET B CG  1 
ATOM   4097 S  SD  . MET B 2 239 ? 12.954  -0.537  5.840   1.00 27.08 ? 239  MET B SD  1 
ATOM   4098 C  CE  . MET B 2 239 ? 11.830  -1.926  5.638   1.00 24.23 ? 239  MET B CE  1 
ATOM   4099 N  N   . ASP B 2 240 ? 16.698  -4.734  8.519   1.00 18.08 ? 240  ASP B N   1 
ATOM   4100 C  CA  . ASP B 2 240 ? 16.792  -5.469  9.776   1.00 25.04 ? 240  ASP B CA  1 
ATOM   4101 C  C   . ASP B 2 240 ? 17.599  -4.692  10.812  1.00 22.76 ? 240  ASP B C   1 
ATOM   4102 O  O   . ASP B 2 240 ? 18.721  -4.267  10.548  1.00 23.65 ? 240  ASP B O   1 
ATOM   4103 C  CB  . ASP B 2 240 ? 17.440  -6.834  9.528   1.00 23.01 ? 240  ASP B CB  1 
ATOM   4104 C  CG  . ASP B 2 240 ? 17.375  -7.737  10.740  1.00 24.92 ? 240  ASP B CG  1 
ATOM   4105 O  OD1 . ASP B 2 240 ? 16.665  -7.400  11.706  1.00 23.87 ? 240  ASP B OD1 1 
ATOM   4106 O  OD2 . ASP B 2 240 ? 18.029  -8.795  10.725  1.00 25.74 ? 240  ASP B OD2 1 
ATOM   4107 N  N   . ASP B 2 241 ? 17.013  -4.506  11.991  1.00 20.41 ? 241  ASP B N   1 
ATOM   4108 C  CA  . ASP B 2 241 ? 17.680  -3.865  13.118  1.00 24.48 ? 241  ASP B CA  1 
ATOM   4109 C  C   . ASP B 2 241 ? 18.190  -4.960  14.046  1.00 25.44 ? 241  ASP B C   1 
ATOM   4110 O  O   . ASP B 2 241 ? 17.406  -5.586  14.771  1.00 23.38 ? 241  ASP B O   1 
ATOM   4111 C  CB  . ASP B 2 241 ? 16.730  -2.924  13.854  1.00 26.86 ? 241  ASP B CB  1 
ATOM   4112 C  CG  . ASP B 2 241 ? 17.344  -2.327  15.111  1.00 29.40 ? 241  ASP B CG  1 
ATOM   4113 O  OD1 . ASP B 2 241 ? 18.533  -2.580  15.401  1.00 27.04 ? 241  ASP B OD1 1 
ATOM   4114 O  OD2 . ASP B 2 241 ? 16.622  -1.605  15.833  1.00 36.21 ? 241  ASP B OD2 1 
ATOM   4115 N  N   . LYS B 2 242 ? 19.503  -5.155  14.051  1.00 20.34 ? 242  LYS B N   1 
ATOM   4116 C  CA  . LYS B 2 242 ? 20.148  -6.220  14.801  1.00 28.58 ? 242  LYS B CA  1 
ATOM   4117 C  C   . LYS B 2 242 ? 20.711  -5.767  16.148  1.00 27.16 ? 242  LYS B C   1 
ATOM   4118 O  O   . LYS B 2 242 ? 21.235  -6.598  16.900  1.00 25.75 ? 242  LYS B O   1 
ATOM   4119 C  CB  . LYS B 2 242 ? 21.272  -6.820  13.946  1.00 29.09 ? 242  LYS B CB  1 
ATOM   4120 C  CG  . LYS B 2 242 ? 20.792  -7.389  12.618  1.00 25.29 ? 242  LYS B CG  1 
ATOM   4121 C  CD  . LYS B 2 242 ? 21.935  -8.081  11.886  1.00 32.19 ? 242  LYS B CD  1 
ATOM   4122 C  CE  . LYS B 2 242 ? 21.460  -8.769  10.614  1.00 30.56 ? 242  LYS B CE  1 
ATOM   4123 N  NZ  . LYS B 2 242 ? 20.726  -10.028 10.938  1.00 34.42 ? 242  LYS B NZ  1 
ATOM   4124 N  N   . SER B 2 243 ? 20.600  -4.480  16.481  1.00 21.89 ? 243  SER B N   1 
ATOM   4125 C  CA  . SER B 2 243 ? 21.375  -3.909  17.580  1.00 24.65 ? 243  SER B CA  1 
ATOM   4126 C  C   . SER B 2 243 ? 20.917  -4.351  18.967  1.00 24.79 ? 243  SER B C   1 
ATOM   4127 O  O   . SER B 2 243 ? 21.621  -4.067  19.941  1.00 25.20 ? 243  SER B O   1 
ATOM   4128 C  CB  . SER B 2 243 ? 21.347  -2.382  17.495  1.00 26.27 ? 243  SER B CB  1 
ATOM   4129 O  OG  . SER B 2 243 ? 20.048  -1.913  17.773  1.00 32.11 ? 243  SER B OG  1 
ATOM   4130 N  N   . GLU B 2 244 ? 19.783  -5.033  19.106  1.00 22.43 ? 244  GLU B N   1 
ATOM   4131 C  CA  . GLU B 2 244 ? 19.399  -5.559  20.412  1.00 25.83 ? 244  GLU B CA  1 
ATOM   4132 C  C   . GLU B 2 244 ? 19.455  -7.078  20.460  1.00 25.65 ? 244  GLU B C   1 
ATOM   4133 O  O   . GLU B 2 244 ? 18.964  -7.675  21.426  1.00 25.50 ? 244  GLU B O   1 
ATOM   4134 C  CB  . GLU B 2 244 ? 18.008  -5.055  20.827  1.00 23.84 ? 244  GLU B CB  1 
ATOM   4135 C  CG  . GLU B 2 244 ? 17.943  -3.543  20.970  1.00 25.15 ? 244  GLU B CG  1 
ATOM   4136 C  CD  . GLU B 2 244 ? 16.536  -3.005  21.244  1.00 24.15 ? 244  GLU B CD  1 
ATOM   4137 O  OE1 . GLU B 2 244 ? 15.843  -3.512  22.146  1.00 22.01 ? 244  GLU B OE1 1 
ATOM   4138 O  OE2 . GLU B 2 244 ? 16.127  -2.063  20.543  1.00 26.26 ? 244  GLU B OE2 1 
ATOM   4139 N  N   . ASN B 2 245 ? 20.041  -7.717  19.446  1.00 22.68 ? 245  ASN B N   1 
ATOM   4140 C  CA  . ASN B 2 245 ? 20.218  -9.163  19.461  1.00 23.60 ? 245  ASN B CA  1 
ATOM   4141 C  C   . ASN B 2 245 ? 21.439  -9.555  20.291  1.00 24.07 ? 245  ASN B C   1 
ATOM   4142 O  O   . ASN B 2 245 ? 22.367  -8.772  20.503  1.00 24.66 ? 245  ASN B O   1 
ATOM   4143 C  CB  . ASN B 2 245 ? 20.403  -9.722  18.049  1.00 24.25 ? 245  ASN B CB  1 
ATOM   4144 C  CG  . ASN B 2 245 ? 19.209  -9.490  17.152  1.00 30.33 ? 245  ASN B CG  1 
ATOM   4145 O  OD1 . ASN B 2 245 ? 18.066  -9.393  17.611  1.00 27.54 ? 245  ASN B OD1 1 
ATOM   4146 N  ND2 . ASN B 2 245 ? 19.468  -9.415  15.852  1.00 21.60 ? 245  ASN B ND2 1 
ATOM   4147 N  N   . GLU B 2 246 ? 21.429  -10.797 20.747  1.00 24.54 ? 246  GLU B N   1 
ATOM   4148 C  CA  . GLU B 2 246 ? 22.580  -11.345 21.439  1.00 24.24 ? 246  GLU B CA  1 
ATOM   4149 C  C   . GLU B 2 246 ? 23.792  -11.331 20.501  1.00 24.36 ? 246  GLU B C   1 
ATOM   4150 O  O   . GLU B 2 246 ? 23.659  -11.697 19.328  1.00 23.22 ? 246  GLU B O   1 
ATOM   4151 C  CB  . GLU B 2 246 ? 22.242  -12.756 21.911  1.00 27.62 ? 246  GLU B CB  1 
ATOM   4152 C  CG  . GLU B 2 246 ? 23.202  -13.335 22.911  1.00 30.65 ? 246  GLU B CG  1 
ATOM   4153 C  CD  . GLU B 2 246 ? 24.277  -14.132 22.220  1.00 30.52 ? 246  GLU B CD  1 
ATOM   4154 O  OE1 . GLU B 2 246 ? 24.000  -14.624 21.105  1.00 33.66 ? 246  GLU B OE1 1 
ATOM   4155 O  OE2 . GLU B 2 246 ? 25.398  -14.243 22.761  1.00 37.38 ? 246  GLU B OE2 1 
ATOM   4156 N  N   . PRO B 2 247 ? 24.966  -10.870 20.958  1.00 23.09 ? 247  PRO B N   1 
ATOM   4157 C  CA  . PRO B 2 247 ? 26.099  -10.690 20.024  1.00 29.08 ? 247  PRO B CA  1 
ATOM   4158 C  C   . PRO B 2 247 ? 26.493  -11.940 19.238  1.00 21.14 ? 247  PRO B C   1 
ATOM   4159 O  O   . PRO B 2 247 ? 26.710  -11.861 18.025  1.00 22.77 ? 247  PRO B O   1 
ATOM   4160 C  CB  . PRO B 2 247 ? 27.230  -10.218 20.952  1.00 25.32 ? 247  PRO B CB  1 
ATOM   4161 C  CG  . PRO B 2 247 ? 26.527  -9.538  22.084  1.00 28.65 ? 247  PRO B CG  1 
ATOM   4162 C  CD  . PRO B 2 247 ? 25.226  -10.266 22.279  1.00 23.44 ? 247  PRO B CD  1 
ATOM   4163 N  N   . ILE B 2 248 ? 26.589  -13.094 19.897  1.00 21.10 ? 248  ILE B N   1 
ATOM   4164 C  CA  . ILE B 2 248 ? 27.041  -14.295 19.199  1.00 24.93 ? 248  ILE B CA  1 
ATOM   4165 C  C   . ILE B 2 248 ? 26.027  -14.717 18.149  1.00 22.69 ? 248  ILE B C   1 
ATOM   4166 O  O   . ILE B 2 248 ? 26.404  -15.231 17.094  1.00 21.11 ? 248  ILE B O   1 
ATOM   4167 C  CB  . ILE B 2 248 ? 27.341  -15.427 20.201  1.00 21.33 ? 248  ILE B CB  1 
ATOM   4168 C  CG1 . ILE B 2 248 ? 28.291  -14.925 21.294  1.00 25.63 ? 248  ILE B CG1 1 
ATOM   4169 C  CG2 . ILE B 2 248 ? 28.010  -16.603 19.481  1.00 21.91 ? 248  ILE B CG2 1 
ATOM   4170 C  CD1 . ILE B 2 248 ? 28.604  -15.971 22.358  1.00 25.44 ? 248  ILE B CD1 1 
ATOM   4171 N  N   . GLU B 2 249 ? 24.733  -14.460 18.390  1.00 19.96 ? 249  GLU B N   1 
ATOM   4172 C  CA  . GLU B 2 249 ? 23.723  -14.708 17.365  1.00 19.93 ? 249  GLU B CA  1 
ATOM   4173 C  C   . GLU B 2 249 ? 23.931  -13.810 16.156  1.00 20.29 ? 249  GLU B C   1 
ATOM   4174 O  O   . GLU B 2 249 ? 23.828  -14.270 15.014  1.00 18.58 ? 249  GLU B O   1 
ATOM   4175 C  CB  . GLU B 2 249 ? 22.325  -14.523 17.957  1.00 21.25 ? 249  GLU B CB  1 
ATOM   4176 C  CG  . GLU B 2 249 ? 22.036  -15.557 19.027  1.00 27.08 ? 249  GLU B CG  1 
ATOM   4177 C  CD  . GLU B 2 249 ? 20.682  -15.393 19.685  1.00 28.22 ? 249  GLU B CD  1 
ATOM   4178 O  OE1 . GLU B 2 249 ? 20.530  -15.900 20.813  1.00 24.10 ? 249  GLU B OE1 1 
ATOM   4179 O  OE2 . GLU B 2 249 ? 19.786  -14.780 19.070  1.00 24.46 ? 249  GLU B OE2 1 
ATOM   4180 N  N   . ASN B 2 250 ? 24.239  -12.525 16.388  1.00 21.85 ? 250  ASN B N   1 
ATOM   4181 C  CA  . ASN B 2 250 ? 24.550  -11.616 15.288  1.00 23.91 ? 250  ASN B CA  1 
ATOM   4182 C  C   . ASN B 2 250 ? 25.780  -12.076 14.516  1.00 24.90 ? 250  ASN B C   1 
ATOM   4183 O  O   . ASN B 2 250 ? 25.827  -11.953 13.287  1.00 30.69 ? 250  ASN B O   1 
ATOM   4184 C  CB  . ASN B 2 250 ? 24.756  -10.197 15.820  1.00 25.58 ? 250  ASN B CB  1 
ATOM   4185 C  CG  . ASN B 2 250 ? 23.443  -9.520  16.175  1.00 24.13 ? 250  ASN B CG  1 
ATOM   4186 O  OD1 . ASN B 2 250 ? 22.381  -9.942  15.716  1.00 24.70 ? 250  ASN B OD1 1 
ATOM   4187 N  ND2 . ASN B 2 250 ? 23.507  -8.477  16.987  1.00 20.64 ? 250  ASN B ND2 1 
ATOM   4188 N  N   . GLU B 2 251 ? 26.792  -12.595 15.217  1.00 19.66 ? 251  GLU B N   1 
ATOM   4189 C  CA  . GLU B 2 251 ? 27.952  -13.142 14.523  1.00 23.26 ? 251  GLU B CA  1 
ATOM   4190 C  C   . GLU B 2 251 ? 27.569  -14.358 13.686  1.00 23.53 ? 251  GLU B C   1 
ATOM   4191 O  O   . GLU B 2 251 ? 27.985  -14.481 12.530  1.00 24.96 ? 251  GLU B O   1 
ATOM   4192 C  CB  . GLU B 2 251 ? 29.044  -13.488 15.535  1.00 26.33 ? 251  GLU B CB  1 
ATOM   4193 C  CG  . GLU B 2 251 ? 30.356  -13.945 14.918  1.00 34.94 ? 251  GLU B CG  1 
ATOM   4194 C  CD  . GLU B 2 251 ? 31.172  -12.803 14.343  1.00 43.47 ? 251  GLU B CD  1 
ATOM   4195 O  OE1 . GLU B 2 251 ? 30.816  -11.625 14.596  1.00 43.61 ? 251  GLU B OE1 1 
ATOM   4196 O  OE2 . GLU B 2 251 ? 32.171  -13.095 13.640  1.00 40.14 ? 251  GLU B OE2 1 
ATOM   4197 N  N   . ALA B 2 252 ? 26.732  -15.242 14.230  1.00 21.99 ? 252  ALA B N   1 
ATOM   4198 C  CA  . ALA B 2 252 ? 26.354  -16.445 13.494  1.00 20.28 ? 252  ALA B CA  1 
ATOM   4199 C  C   . ALA B 2 252 ? 25.541  -16.109 12.244  1.00 21.85 ? 252  ALA B C   1 
ATOM   4200 O  O   . ALA B 2 252 ? 25.673  -16.780 11.214  1.00 20.09 ? 252  ALA B O   1 
ATOM   4201 C  CB  . ALA B 2 252 ? 25.569  -17.391 14.408  1.00 17.20 ? 252  ALA B CB  1 
ATOM   4202 N  N   . ALA B 2 253 ? 24.690  -15.080 12.315  1.00 24.96 ? 253  ALA B N   1 
ATOM   4203 C  CA  . ALA B 2 253 ? 23.837  -14.750 11.176  1.00 26.87 ? 253  ALA B CA  1 
ATOM   4204 C  C   . ALA B 2 253 ? 24.661  -14.306 9.970   1.00 24.23 ? 253  ALA B C   1 
ATOM   4205 O  O   . ALA B 2 253 ? 24.232  -14.486 8.824   1.00 23.79 ? 253  ALA B O   1 
ATOM   4206 C  CB  . ALA B 2 253 ? 22.825  -13.668 11.572  1.00 19.96 ? 253  ALA B CB  1 
ATOM   4207 N  N   . LYS B 2 254 ? 25.846  -13.738 10.209  1.00 29.13 ? 254  LYS B N   1 
ATOM   4208 C  CA  . LYS B 2 254 ? 26.719  -13.340 9.110   1.00 27.65 ? 254  LYS B CA  1 
ATOM   4209 C  C   . LYS B 2 254 ? 27.064  -14.524 8.224   1.00 27.21 ? 254  LYS B C   1 
ATOM   4210 O  O   . LYS B 2 254 ? 27.343  -14.346 7.036   1.00 29.05 ? 254  LYS B O   1 
ATOM   4211 C  CB  . LYS B 2 254 ? 27.998  -12.713 9.660   1.00 29.40 ? 254  LYS B CB  1 
ATOM   4212 C  CG  . LYS B 2 254 ? 27.773  -11.410 10.409  1.00 31.86 ? 254  LYS B CG  1 
ATOM   4213 C  CD  . LYS B 2 254 ? 28.990  -11.034 11.228  1.00 28.91 ? 254  LYS B CD  1 
ATOM   4214 C  CE  . LYS B 2 254 ? 28.832  -9.639  11.837  1.00 37.47 ? 254  LYS B CE  1 
ATOM   4215 N  NZ  . LYS B 2 254 ? 29.943  -9.302  12.785  1.00 45.80 ? 254  LYS B NZ  1 
ATOM   4216 N  N   . TYR B 2 255 ? 27.047  -15.738 8.778   1.00 24.35 ? 255  TYR B N   1 
ATOM   4217 C  CA  . TYR B 2 255 ? 27.390  -16.934 8.016   1.00 26.99 ? 255  TYR B CA  1 
ATOM   4218 C  C   . TYR B 2 255 ? 26.191  -17.843 7.793   1.00 22.06 ? 255  TYR B C   1 
ATOM   4219 O  O   . TYR B 2 255 ? 26.363  -19.039 7.546   1.00 26.90 ? 255  TYR B O   1 
ATOM   4220 C  CB  . TYR B 2 255 ? 28.518  -17.689 8.716   1.00 25.53 ? 255  TYR B CB  1 
ATOM   4221 C  CG  . TYR B 2 255 ? 29.610  -16.763 9.213   1.00 23.32 ? 255  TYR B CG  1 
ATOM   4222 C  CD1 . TYR B 2 255 ? 30.523  -16.198 8.332   1.00 25.68 ? 255  TYR B CD1 1 
ATOM   4223 C  CD2 . TYR B 2 255 ? 29.731  -16.467 10.565  1.00 24.49 ? 255  TYR B CD2 1 
ATOM   4224 C  CE1 . TYR B 2 255 ? 31.525  -15.348 8.785   1.00 28.48 ? 255  TYR B CE1 1 
ATOM   4225 C  CE2 . TYR B 2 255 ? 30.722  -15.623 11.029  1.00 27.30 ? 255  TYR B CE2 1 
ATOM   4226 C  CZ  . TYR B 2 255 ? 31.617  -15.065 10.135  1.00 33.18 ? 255  TYR B CZ  1 
ATOM   4227 O  OH  . TYR B 2 255 ? 32.604  -14.231 10.599  1.00 36.32 ? 255  TYR B OH  1 
ATOM   4228 N  N   . ASP B 2 256 ? 24.978  -17.296 7.871   1.00 21.82 ? 256  ASP B N   1 
ATOM   4229 C  CA  . ASP B 2 256 ? 23.747  -18.058 7.661   1.00 22.11 ? 256  ASP B CA  1 
ATOM   4230 C  C   . ASP B 2 256 ? 23.617  -19.222 8.644   1.00 22.93 ? 256  ASP B C   1 
ATOM   4231 O  O   . ASP B 2 256 ? 23.055  -20.263 8.298   1.00 22.30 ? 256  ASP B O   1 
ATOM   4232 C  CB  . ASP B 2 256 ? 23.644  -18.584 6.222   1.00 28.82 ? 256  ASP B CB  1 
ATOM   4233 C  CG  . ASP B 2 256 ? 23.216  -17.518 5.226   1.00 41.41 ? 256  ASP B CG  1 
ATOM   4234 O  OD1 . ASP B 2 256 ? 23.169  -16.315 5.592   1.00 36.60 ? 256  ASP B OD1 1 
ATOM   4235 O  OD2 . ASP B 2 256 ? 22.922  -17.898 4.067   1.00 47.15 ? 256  ASP B OD2 1 
ATOM   4236 N  N   . LEU B 2 257 ? 24.115  -19.046 9.871   1.00 21.67 ? 257  LEU B N   1 
ATOM   4237 C  CA  . LEU B 2 257 ? 24.085  -20.079 10.904  1.00 23.34 ? 257  LEU B CA  1 
ATOM   4238 C  C   . LEU B 2 257 ? 22.927  -19.841 11.869  1.00 19.61 ? 257  LEU B C   1 
ATOM   4239 O  O   . LEU B 2 257 ? 22.657  -18.704 12.253  1.00 20.82 ? 257  LEU B O   1 
ATOM   4240 C  CB  . LEU B 2 257 ? 25.396  -20.101 11.693  1.00 18.21 ? 257  LEU B CB  1 
ATOM   4241 C  CG  . LEU B 2 257 ? 26.681  -20.470 10.957  1.00 18.27 ? 257  LEU B CG  1 
ATOM   4242 C  CD1 . LEU B 2 257 ? 27.852  -20.166 11.862  1.00 21.65 ? 257  LEU B CD1 1 
ATOM   4243 C  CD2 . LEU B 2 257 ? 26.674  -21.950 10.602  1.00 18.43 ? 257  LEU B CD2 1 
ATOM   4244 N  N   . LYS B 2 258 ? 22.268  -20.923 12.276  1.00 21.25 ? 258  LYS B N   1 
ATOM   4245 C  CA  . LYS B 2 258 ? 21.175  -20.878 13.254  1.00 22.44 ? 258  LYS B CA  1 
ATOM   4246 C  C   . LYS B 2 258 ? 21.751  -21.177 14.643  1.00 20.61 ? 258  LYS B C   1 
ATOM   4247 O  O   . LYS B 2 258 ? 21.942  -22.336 15.023  1.00 21.49 ? 258  LYS B O   1 
ATOM   4248 C  CB  . LYS B 2 258 ? 20.066  -21.856 12.873  1.00 23.86 ? 258  LYS B CB  1 
ATOM   4249 C  CG  . LYS B 2 258 ? 19.494  -21.654 11.462  1.00 30.68 ? 258  LYS B CG  1 
ATOM   4250 C  CD  . LYS B 2 258 ? 18.468  -22.759 11.091  1.00 35.14 ? 258  LYS B CD  1 
ATOM   4251 C  CE  . LYS B 2 258 ? 18.270  -22.897 9.578   1.00 38.06 ? 258  LYS B CE  1 
ATOM   4252 N  NZ  . LYS B 2 258 ? 18.247  -24.339 9.140   1.00 41.92 ? 258  LYS B NZ  1 
ATOM   4253 N  N   . TYR B 2 259 ? 22.042  -20.117 15.386  1.00 19.63 ? 259  TYR B N   1 
ATOM   4254 C  CA  . TYR B 2 259 ? 22.632  -20.182 16.711  1.00 19.51 ? 259  TYR B CA  1 
ATOM   4255 C  C   . TYR B 2 259 ? 21.724  -19.431 17.667  1.00 23.02 ? 259  TYR B C   1 
ATOM   4256 O  O   . TYR B 2 259 ? 21.276  -18.324 17.353  1.00 19.19 ? 259  TYR B O   1 
ATOM   4257 C  CB  . TYR B 2 259 ? 24.030  -19.555 16.717  1.00 16.80 ? 259  TYR B CB  1 
ATOM   4258 C  CG  . TYR B 2 259 ? 24.684  -19.421 18.083  1.00 19.28 ? 259  TYR B CG  1 
ATOM   4259 C  CD1 . TYR B 2 259 ? 24.312  -18.413 18.965  1.00 21.52 ? 259  TYR B CD1 1 
ATOM   4260 C  CD2 . TYR B 2 259 ? 25.700  -20.284 18.475  1.00 18.38 ? 259  TYR B CD2 1 
ATOM   4261 C  CE1 . TYR B 2 259 ? 24.913  -18.284 20.211  1.00 20.44 ? 259  TYR B CE1 1 
ATOM   4262 C  CE2 . TYR B 2 259 ? 26.306  -20.160 19.710  1.00 18.23 ? 259  TYR B CE2 1 
ATOM   4263 C  CZ  . TYR B 2 259 ? 25.910  -19.155 20.570  1.00 21.18 ? 259  TYR B CZ  1 
ATOM   4264 O  OH  . TYR B 2 259 ? 26.515  -19.028 21.791  1.00 20.45 ? 259  TYR B OH  1 
ATOM   4265 N  N   . ILE B 2 260 ? 21.463  -20.022 18.832  1.00 19.60 ? 260  ILE B N   1 
ATOM   4266 C  CA  . ILE B 2 260 ? 20.657  -19.379 19.863  1.00 20.85 ? 260  ILE B CA  1 
ATOM   4267 C  C   . ILE B 2 260 ? 21.399  -19.495 21.190  1.00 25.76 ? 260  ILE B C   1 
ATOM   4268 O  O   . ILE B 2 260 ? 21.709  -20.607 21.641  1.00 21.75 ? 260  ILE B O   1 
ATOM   4269 C  CB  . ILE B 2 260 ? 19.247  -19.994 19.950  1.00 22.09 ? 260  ILE B CB  1 
ATOM   4270 C  CG1 . ILE B 2 260 ? 18.475  -19.690 18.655  1.00 24.59 ? 260  ILE B CG1 1 
ATOM   4271 C  CG2 . ILE B 2 260 ? 18.518  -19.467 21.155  1.00 20.75 ? 260  ILE B CG2 1 
ATOM   4272 C  CD1 . ILE B 2 260 ? 16.982  -19.857 18.747  1.00 26.38 ? 260  ILE B CD1 1 
ATOM   4273 N  N   . GLY B 2 261 ? 21.700  -18.353 21.802  1.00 21.42 ? 261  GLY B N   1 
ATOM   4274 C  CA  . GLY B 2 261 ? 22.466  -18.356 23.033  1.00 20.93 ? 261  GLY B CA  1 
ATOM   4275 C  C   . GLY B 2 261 ? 21.593  -18.747 24.211  1.00 24.94 ? 261  GLY B C   1 
ATOM   4276 O  O   . GLY B 2 261 ? 20.464  -18.283 24.355  1.00 25.25 ? 261  GLY B O   1 
ATOM   4277 N  N   . LEU B 2 262 ? 22.127  -19.630 25.050  1.00 23.34 ? 262  LEU B N   1 
ATOM   4278 C  CA  . LEU B 2 262 ? 21.445  -20.114 26.244  1.00 23.73 ? 262  LEU B CA  1 
ATOM   4279 C  C   . LEU B 2 262 ? 22.270  -19.763 27.483  1.00 26.96 ? 262  LEU B C   1 
ATOM   4280 O  O   . LEU B 2 262 ? 23.304  -19.095 27.404  1.00 27.65 ? 262  LEU B O   1 
ATOM   4281 C  CB  . LEU B 2 262 ? 21.191  -21.622 26.152  1.00 23.61 ? 262  LEU B CB  1 
ATOM   4282 C  CG  . LEU B 2 262 ? 20.397  -22.063 24.916  1.00 24.13 ? 262  LEU B CG  1 
ATOM   4283 C  CD1 . LEU B 2 262 ? 20.400  -23.573 24.772  1.00 17.65 ? 262  LEU B CD1 1 
ATOM   4284 C  CD2 . LEU B 2 262 ? 18.971  -21.528 24.955  1.00 23.29 ? 262  LEU B CD2 1 
ATOM   4285 N  N   . ASP B 2 263 ? 21.774  -20.200 28.635  1.00 26.01 ? 263  ASP B N   1 
ATOM   4286 C  CA  . ASP B 2 263 ? 22.336  -19.869 29.947  1.00 32.12 ? 263  ASP B CA  1 
ATOM   4287 C  C   . ASP B 2 263 ? 23.134  -21.046 30.511  1.00 37.86 ? 263  ASP B C   1 
ATOM   4288 O  O   . ASP B 2 263 ? 22.757  -21.654 31.522  1.00 39.19 ? 263  ASP B O   1 
ATOM   4289 C  CB  . ASP B 2 263 ? 21.206  -19.466 30.895  1.00 32.42 ? 263  ASP B CB  1 
ATOM   4290 C  CG  . ASP B 2 263 ? 21.696  -18.804 32.159  1.00 50.47 ? 263  ASP B CG  1 
ATOM   4291 O  OD1 . ASP B 2 263 ? 22.319  -17.724 32.058  1.00 54.98 ? 263  ASP B OD1 1 
ATOM   4292 O  OD2 . ASP B 2 263 ? 21.421  -19.341 33.260  1.00 52.77 ? 263  ASP B OD2 1 
ATOM   4293 N  N   . GLY B 2 264 ? 24.237  -21.395 29.852  1.00 27.11 ? 264  GLY B N   1 
ATOM   4294 C  CA  . GLY B 2 264 ? 24.969  -22.573 30.266  1.00 20.00 ? 264  GLY B CA  1 
ATOM   4295 C  C   . GLY B 2 264 ? 26.445  -22.485 29.954  1.00 19.63 ? 264  GLY B C   1 
ATOM   4296 O  O   . GLY B 2 264 ? 26.946  -21.468 29.465  1.00 18.24 ? 264  GLY B O   1 
ATOM   4297 N  N   . ASN B 2 265 ? 27.145  -23.586 30.237  1.00 18.29 ? 265  ASN B N   1 
ATOM   4298 C  CA  . ASN B 2 265 ? 28.581  -23.655 30.023  1.00 21.07 ? 265  ASN B CA  1 
ATOM   4299 C  C   . ASN B 2 265 ? 29.025  -24.837 29.170  1.00 17.92 ? 265  ASN B C   1 
ATOM   4300 O  O   . ASN B 2 265 ? 30.230  -24.995 28.950  1.00 22.66 ? 265  ASN B O   1 
ATOM   4301 C  CB  . ASN B 2 265 ? 29.321  -23.696 31.368  1.00 19.45 ? 265  ASN B CB  1 
ATOM   4302 C  CG  . ASN B 2 265 ? 28.991  -24.945 32.185  1.00 22.79 ? 265  ASN B CG  1 
ATOM   4303 O  OD1 . ASN B 2 265 ? 28.103  -25.726 31.835  1.00 18.92 ? 265  ASN B OD1 1 
ATOM   4304 N  ND2 . ASN B 2 265 ? 29.693  -25.115 33.294  1.00 20.25 ? 265  ASN B ND2 1 
ATOM   4305 N  N   . ILE B 2 266 ? 28.106  -25.665 28.691  1.00 16.02 ? 266  ILE B N   1 
ATOM   4306 C  CA  . ILE B 2 266 ? 28.418  -26.770 27.789  1.00 17.53 ? 266  ILE B CA  1 
ATOM   4307 C  C   . ILE B 2 266 ? 27.898  -26.396 26.403  1.00 20.85 ? 266  ILE B C   1 
ATOM   4308 O  O   . ILE B 2 266 ? 26.682  -26.372 26.167  1.00 18.02 ? 266  ILE B O   1 
ATOM   4309 C  CB  . ILE B 2 266 ? 27.816  -28.090 28.286  1.00 14.79 ? 266  ILE B CB  1 
ATOM   4310 C  CG1 . ILE B 2 266 ? 28.250  -28.322 29.737  1.00 23.25 ? 266  ILE B CG1 1 
ATOM   4311 C  CG2 . ILE B 2 266 ? 28.242  -29.253 27.394  1.00 16.24 ? 266  ILE B CG2 1 
ATOM   4312 C  CD1 . ILE B 2 266 ? 28.052  -29.736 30.242  1.00 21.38 ? 266  ILE B CD1 1 
ATOM   4313 N  N   . ALA B 2 267 ? 28.821  -26.102 25.488  1.00 19.86 ? 267  ALA B N   1 
ATOM   4314 C  CA  . ALA B 2 267 ? 28.471  -25.737 24.125  1.00 18.59 ? 267  ALA B CA  1 
ATOM   4315 C  C   . ALA B 2 267 ? 27.997  -26.955 23.339  1.00 19.18 ? 267  ALA B C   1 
ATOM   4316 O  O   . ALA B 2 267 ? 28.432  -28.083 23.577  1.00 16.20 ? 267  ALA B O   1 
ATOM   4317 C  CB  . ALA B 2 267 ? 29.670  -25.102 23.416  1.00 18.58 ? 267  ALA B CB  1 
ATOM   4318 N  N   . CYS B 2 268 ? 27.094  -26.712 22.384  1.00 17.20 ? 268  CYS B N   1 
ATOM   4319 C  CA  . CYS B 2 268 ? 26.552  -27.756 21.526  1.00 16.00 ? 268  CYS B CA  1 
ATOM   4320 C  C   . CYS B 2 268 ? 26.834  -27.438 20.064  1.00 18.05 ? 268  CYS B C   1 
ATOM   4321 O  O   . CYS B 2 268 ? 26.658  -26.299 19.614  1.00 17.43 ? 268  CYS B O   1 
ATOM   4322 C  CB  . CYS B 2 268 ? 25.035  -27.928 21.731  1.00 17.63 ? 268  CYS B CB  1 
ATOM   4323 S  SG  . CYS B 2 268 ? 24.625  -28.520 23.396  1.00 18.87 ? 268  CYS B SG  1 
ATOM   4324 N  N   . PHE B 2 269 ? 27.250  -28.466 19.332  1.00 17.04 ? 269  PHE B N   1 
ATOM   4325 C  CA  . PHE B 2 269 ? 27.621  -28.359 17.922  1.00 12.94 ? 269  PHE B CA  1 
ATOM   4326 C  C   . PHE B 2 269 ? 26.953  -29.543 17.234  1.00 14.25 ? 269  PHE B C   1 
ATOM   4327 O  O   . PHE B 2 269 ? 27.471  -30.658 17.286  1.00 16.90 ? 269  PHE B O   1 
ATOM   4328 C  CB  . PHE B 2 269 ? 29.137  -28.393 17.799  1.00 18.69 ? 269  PHE B CB  1 
ATOM   4329 C  CG  . PHE B 2 269 ? 29.671  -27.930 16.480  1.00 16.81 ? 269  PHE B CG  1 
ATOM   4330 C  CD1 . PHE B 2 269 ? 29.893  -26.586 16.245  1.00 18.97 ? 269  PHE B CD1 1 
ATOM   4331 C  CD2 . PHE B 2 269 ? 30.004  -28.848 15.495  1.00 20.42 ? 269  PHE B CD2 1 
ATOM   4332 C  CE1 . PHE B 2 269 ? 30.418  -26.151 15.025  1.00 21.74 ? 269  PHE B CE1 1 
ATOM   4333 C  CE2 . PHE B 2 269 ? 30.525  -28.421 14.275  1.00 24.88 ? 269  PHE B CE2 1 
ATOM   4334 C  CZ  . PHE B 2 269 ? 30.740  -27.070 14.050  1.00 17.70 ? 269  PHE B CZ  1 
ATOM   4335 N  N   . VAL B 2 270 ? 25.802  -29.306 16.595  1.00 14.98 ? 270  VAL B N   1 
ATOM   4336 C  CA  . VAL B 2 270 ? 24.926  -30.375 16.125  1.00 14.17 ? 270  VAL B CA  1 
ATOM   4337 C  C   . VAL B 2 270 ? 24.395  -30.019 14.741  1.00 14.86 ? 270  VAL B C   1 
ATOM   4338 O  O   . VAL B 2 270 ? 24.264  -28.844 14.386  1.00 15.17 ? 270  VAL B O   1 
ATOM   4339 C  CB  . VAL B 2 270 ? 23.747  -30.619 17.104  1.00 11.27 ? 270  VAL B CB  1 
ATOM   4340 C  CG1 . VAL B 2 270 ? 22.940  -31.836 16.705  1.00 13.56 ? 270  VAL B CG1 1 
ATOM   4341 C  CG2 . VAL B 2 270 ? 24.243  -30.770 18.571  1.00 13.17 ? 270  VAL B CG2 1 
ATOM   4342 N  N   . ASN B 2 271 ? 24.084  -31.042 13.958  1.00 12.69 ? 271  ASN B N   1 
ATOM   4343 C  CA  . ASN B 2 271 ? 23.349  -30.864 12.715  1.00 17.15 ? 271  ASN B CA  1 
ATOM   4344 C  C   . ASN B 2 271 ? 21.892  -31.250 12.935  1.00 16.62 ? 271  ASN B C   1 
ATOM   4345 O  O   . ASN B 2 271 ? 21.605  -32.261 13.585  1.00 20.93 ? 271  ASN B O   1 
ATOM   4346 C  CB  . ASN B 2 271 ? 23.934  -31.693 11.574  1.00 13.46 ? 271  ASN B CB  1 
ATOM   4347 C  CG  . ASN B 2 271 ? 23.755  -33.191 11.776  1.00 21.80 ? 271  ASN B CG  1 
ATOM   4348 O  OD1 . ASN B 2 271 ? 24.176  -33.750 12.789  1.00 15.06 ? 271  ASN B OD1 1 
ATOM   4349 N  ND2 . ASN B 2 271 ? 23.122  -33.852 10.798  1.00 19.53 ? 271  ASN B ND2 1 
ATOM   4350 N  N   . GLY B 2 272 ? 20.978  -30.434 12.387  1.00 17.40 ? 272  GLY B N   1 
ATOM   4351 C  CA  . GLY B 2 272 ? 19.550  -30.693 12.440  1.00 17.12 ? 272  GLY B CA  1 
ATOM   4352 C  C   . GLY B 2 272 ? 18.854  -30.015 13.599  1.00 18.53 ? 272  GLY B C   1 
ATOM   4353 O  O   . GLY B 2 272 ? 19.406  -29.955 14.703  1.00 13.58 ? 272  GLY B O   1 
ATOM   4354 N  N   . ALA B 2 273 ? 17.648  -29.477 13.356  1.00 15.85 ? 273  ALA B N   1 
ATOM   4355 C  CA  . ALA B 2 273 ? 16.950  -28.756 14.415  1.00 22.16 ? 273  ALA B CA  1 
ATOM   4356 C  C   . ALA B 2 273 ? 16.519  -29.702 15.523  1.00 15.31 ? 273  ALA B C   1 
ATOM   4357 O  O   . ALA B 2 273 ? 16.689  -29.404 16.710  1.00 13.64 ? 273  ALA B O   1 
ATOM   4358 C  CB  . ALA B 2 273 ? 15.739  -28.006 13.853  1.00 19.48 ? 273  ALA B CB  1 
ATOM   4359 N  N   . GLY B 2 274 ? 15.949  -30.846 15.152  1.00 15.23 ? 274  GLY B N   1 
ATOM   4360 C  CA  . GLY B 2 274 ? 15.501  -31.788 16.162  1.00 15.42 ? 274  GLY B CA  1 
ATOM   4361 C  C   . GLY B 2 274 ? 16.643  -32.312 17.012  1.00 14.42 ? 274  GLY B C   1 
ATOM   4362 O  O   . GLY B 2 274 ? 16.567  -32.317 18.244  1.00 13.90 ? 274  GLY B O   1 
ATOM   4363 N  N   . LEU B 2 275 ? 17.727  -32.756 16.361  1.00 16.56 ? 275  LEU B N   1 
ATOM   4364 C  CA  . LEU B 2 275 ? 18.867  -33.300 17.098  1.00 12.56 ? 275  LEU B CA  1 
ATOM   4365 C  C   . LEU B 2 275 ? 19.538  -32.229 17.947  1.00 14.60 ? 275  LEU B C   1 
ATOM   4366 O  O   . LEU B 2 275 ? 19.981  -32.508 19.069  1.00 15.31 ? 275  LEU B O   1 
ATOM   4367 C  CB  . LEU B 2 275 ? 19.872  -33.923 16.129  1.00 14.12 ? 275  LEU B CB  1 
ATOM   4368 C  CG  . LEU B 2 275 ? 20.975  -34.806 16.714  1.00 15.16 ? 275  LEU B CG  1 
ATOM   4369 C  CD1 . LEU B 2 275 ? 20.426  -36.025 17.475  1.00 14.43 ? 275  LEU B CD1 1 
ATOM   4370 C  CD2 . LEU B 2 275 ? 21.910  -35.250 15.594  1.00 14.90 ? 275  LEU B CD2 1 
ATOM   4371 N  N   . ALA B 2 276 ? 19.604  -30.988 17.444  1.00 14.96 ? 276  ALA B N   1 
ATOM   4372 C  CA  . ALA B 2 276 ? 20.218  -29.914 18.229  1.00 13.58 ? 276  ALA B CA  1 
ATOM   4373 C  C   . ALA B 2 276 ? 19.396  -29.597 19.474  1.00 16.22 ? 276  ALA B C   1 
ATOM   4374 O  O   . ALA B 2 276 ? 19.950  -29.457 20.573  1.00 15.76 ? 276  ALA B O   1 
ATOM   4375 C  CB  . ALA B 2 276 ? 20.396  -28.668 17.369  1.00 15.10 ? 276  ALA B CB  1 
ATOM   4376 N  N   . MET B 2 277 ? 18.073  -29.447 19.322  1.00 13.38 ? 277  MET B N   1 
ATOM   4377 C  CA  . MET B 2 277 ? 17.211  -29.275 20.497  1.00 14.76 ? 277  MET B CA  1 
ATOM   4378 C  C   . MET B 2 277 ? 17.409  -30.415 21.485  1.00 15.24 ? 277  MET B C   1 
ATOM   4379 O  O   . MET B 2 277 ? 17.555  -30.189 22.689  1.00 16.20 ? 277  MET B O   1 
ATOM   4380 C  CB  . MET B 2 277 ? 15.740  -29.205 20.088  1.00 14.18 ? 277  MET B CB  1 
ATOM   4381 C  CG  . MET B 2 277 ? 15.244  -27.785 19.696  1.00 17.90 ? 277  MET B CG  1 
ATOM   4382 S  SD  . MET B 2 277 ? 13.446  -27.747 19.388  1.00 18.91 ? 277  MET B SD  1 
ATOM   4383 C  CE  . MET B 2 277 ? 13.366  -28.289 17.679  1.00 16.37 ? 277  MET B CE  1 
ATOM   4384 N  N   . ALA B 2 278 ? 17.421  -31.656 20.988  1.00 14.53 ? 278  ALA B N   1 
ATOM   4385 C  CA  . ALA B 2 278 ? 17.514  -32.804 21.878  1.00 12.51 ? 278  ALA B CA  1 
ATOM   4386 C  C   . ALA B 2 278 ? 18.872  -32.882 22.566  1.00 15.45 ? 278  ALA B C   1 
ATOM   4387 O  O   . ALA B 2 278 ? 18.966  -33.390 23.683  1.00 13.71 ? 278  ALA B O   1 
ATOM   4388 C  CB  . ALA B 2 278 ? 17.254  -34.095 21.107  1.00 14.11 ? 278  ALA B CB  1 
ATOM   4389 N  N   . THR B 2 279 ? 19.931  -32.417 21.907  1.00 14.89 ? 279  THR B N   1 
ATOM   4390 C  CA  . THR B 2 279 ? 21.250  -32.391 22.535  1.00 12.65 ? 279  THR B CA  1 
ATOM   4391 C  C   . THR B 2 279 ? 21.275  -31.419 23.709  1.00 15.29 ? 279  THR B C   1 
ATOM   4392 O  O   . THR B 2 279 ? 21.777  -31.752 24.794  1.00 15.80 ? 279  THR B O   1 
ATOM   4393 C  CB  . THR B 2 279 ? 22.305  -32.019 21.494  1.00 14.76 ? 279  THR B CB  1 
ATOM   4394 O  OG1 . THR B 2 279 ? 22.306  -33.018 20.471  1.00 12.58 ? 279  THR B OG1 1 
ATOM   4395 C  CG2 . THR B 2 279 ? 23.689  -31.924 22.149  1.00 16.95 ? 279  THR B CG2 1 
ATOM   4396 N  N   . CYS B 2 280 ? 20.724  -30.215 23.518  1.00 12.42 ? 280  CYS B N   1 
ATOM   4397 C  CA  . CYS B 2 280 ? 20.554  -29.308 24.654  1.00 14.31 ? 280  CYS B CA  1 
ATOM   4398 C  C   . CYS B 2 280 ? 19.747  -29.980 25.763  1.00 17.63 ? 280  CYS B C   1 
ATOM   4399 O  O   . CYS B 2 280 ? 20.096  -29.881 26.948  1.00 15.34 ? 280  CYS B O   1 
ATOM   4400 C  CB  . CYS B 2 280 ? 19.860  -28.014 24.219  1.00 18.87 ? 280  CYS B CB  1 
ATOM   4401 S  SG  . CYS B 2 280 ? 20.667  -27.031 22.903  1.00 18.79 ? 280  CYS B SG  1 
ATOM   4402 N  N   . ASP B 2 281 ? 18.669  -30.676 25.391  1.00 14.86 ? 281  ASP B N   1 
ATOM   4403 C  CA  . ASP B 2 281 ? 17.799  -31.298 26.381  1.00 17.86 ? 281  ASP B CA  1 
ATOM   4404 C  C   . ASP B 2 281 ? 18.515  -32.401 27.144  1.00 17.53 ? 281  ASP B C   1 
ATOM   4405 O  O   . ASP B 2 281 ? 18.345  -32.526 28.359  1.00 17.98 ? 281  ASP B O   1 
ATOM   4406 C  CB  . ASP B 2 281 ? 16.549  -31.884 25.723  1.00 14.31 ? 281  ASP B CB  1 
ATOM   4407 C  CG  . ASP B 2 281 ? 15.727  -30.840 24.981  1.00 19.54 ? 281  ASP B CG  1 
ATOM   4408 O  OD1 . ASP B 2 281 ? 15.867  -29.617 25.260  1.00 15.69 ? 281  ASP B OD1 1 
ATOM   4409 O  OD2 . ASP B 2 281 ? 14.947  -31.265 24.098  1.00 22.13 ? 281  ASP B OD2 1 
ATOM   4410 N  N   . ILE B 2 282 ? 19.275  -33.247 26.449  1.00 15.92 ? 282  ILE B N   1 
ATOM   4411 C  CA  . ILE B 2 282 ? 19.862  -34.381 27.155  1.00 15.39 ? 282  ILE B CA  1 
ATOM   4412 C  C   . ILE B 2 282 ? 21.006  -33.911 28.057  1.00 16.56 ? 282  ILE B C   1 
ATOM   4413 O  O   . ILE B 2 282 ? 21.291  -34.532 29.094  1.00 14.90 ? 282  ILE B O   1 
ATOM   4414 C  CB  . ILE B 2 282 ? 20.276  -35.486 26.150  1.00 15.08 ? 282  ILE B CB  1 
ATOM   4415 C  CG1 . ILE B 2 282 ? 20.590  -36.782 26.901  1.00 17.29 ? 282  ILE B CG1 1 
ATOM   4416 C  CG2 . ILE B 2 282 ? 21.459  -35.036 25.244  1.00 14.97 ? 282  ILE B CG2 1 
ATOM   4417 C  CD1 . ILE B 2 282 ? 20.787  -38.003 26.007  1.00 19.32 ? 282  ILE B CD1 1 
ATOM   4418 N  N   . ILE B 2 283 ? 21.637  -32.779 27.728  1.00 15.11 ? 283  ILE B N   1 
ATOM   4419 C  CA  . ILE B 2 283 ? 22.574  -32.177 28.675  1.00 14.90 ? 283  ILE B CA  1 
ATOM   4420 C  C   . ILE B 2 283 ? 21.849  -31.800 29.959  1.00 21.19 ? 283  ILE B C   1 
ATOM   4421 O  O   . ILE B 2 283 ? 22.286  -32.144 31.069  1.00 17.93 ? 283  ILE B O   1 
ATOM   4422 C  CB  . ILE B 2 283 ? 23.268  -30.962 28.045  1.00 14.72 ? 283  ILE B CB  1 
ATOM   4423 C  CG1 . ILE B 2 283 ? 24.177  -31.421 26.903  1.00 11.94 ? 283  ILE B CG1 1 
ATOM   4424 C  CG2 . ILE B 2 283 ? 24.033  -30.174 29.109  1.00 14.69 ? 283  ILE B CG2 1 
ATOM   4425 C  CD1 . ILE B 2 283 ? 24.811  -30.291 26.171  1.00 15.04 ? 283  ILE B CD1 1 
ATOM   4426 N  N   . PHE B 2 284 ? 20.728  -31.077 29.824  1.00 17.03 ? 284  PHE B N   1 
ATOM   4427 C  CA  . PHE B 2 284 ? 19.938  -30.716 30.995  1.00 18.66 ? 284  PHE B CA  1 
ATOM   4428 C  C   . PHE B 2 284 ? 19.514  -31.958 31.766  1.00 19.14 ? 284  PHE B C   1 
ATOM   4429 O  O   . PHE B 2 284 ? 19.620  -32.006 32.993  1.00 19.59 ? 284  PHE B O   1 
ATOM   4430 C  CB  . PHE B 2 284 ? 18.709  -29.905 30.586  1.00 19.14 ? 284  PHE B CB  1 
ATOM   4431 C  CG  . PHE B 2 284 ? 17.627  -29.880 31.649  1.00 21.77 ? 284  PHE B CG  1 
ATOM   4432 C  CD1 . PHE B 2 284 ? 17.640  -28.913 32.645  1.00 26.20 ? 284  PHE B CD1 1 
ATOM   4433 C  CD2 . PHE B 2 284 ? 16.610  -30.822 31.651  1.00 22.54 ? 284  PHE B CD2 1 
ATOM   4434 C  CE1 . PHE B 2 284 ? 16.656  -28.885 33.633  1.00 25.33 ? 284  PHE B CE1 1 
ATOM   4435 C  CE2 . PHE B 2 284 ? 15.625  -30.812 32.640  1.00 28.30 ? 284  PHE B CE2 1 
ATOM   4436 C  CZ  . PHE B 2 284 ? 15.649  -29.829 33.624  1.00 22.87 ? 284  PHE B CZ  1 
ATOM   4437 N  N   . LEU B 2 285 ? 19.030  -32.981 31.059  1.00 16.96 ? 285  LEU B N   1 
ATOM   4438 C  CA  . LEU B 2 285 ? 18.537  -34.171 31.749  1.00 15.87 ? 285  LEU B CA  1 
ATOM   4439 C  C   . LEU B 2 285 ? 19.622  -34.874 32.559  1.00 17.71 ? 285  LEU B C   1 
ATOM   4440 O  O   . LEU B 2 285 ? 19.314  -35.534 33.560  1.00 17.40 ? 285  LEU B O   1 
ATOM   4441 C  CB  . LEU B 2 285 ? 17.937  -35.148 30.744  1.00 20.32 ? 285  LEU B CB  1 
ATOM   4442 C  CG  . LEU B 2 285 ? 16.661  -34.789 29.993  1.00 19.13 ? 285  LEU B CG  1 
ATOM   4443 C  CD1 . LEU B 2 285 ? 16.378  -35.944 29.022  1.00 21.68 ? 285  LEU B CD1 1 
ATOM   4444 C  CD2 . LEU B 2 285 ? 15.487  -34.592 30.949  1.00 18.87 ? 285  LEU B CD2 1 
ATOM   4445 N  N   . ASN B 2 286 ? 20.885  -34.793 32.128  1.00 21.41 ? 286  ASN B N   1 
ATOM   4446 C  CA  . ASN B 2 286 ? 21.986  -35.399 32.866  1.00 17.63 ? 286  ASN B CA  1 
ATOM   4447 C  C   . ASN B 2 286 ? 22.633  -34.435 33.844  1.00 21.10 ? 286  ASN B C   1 
ATOM   4448 O  O   . ASN B 2 286 ? 23.766  -34.677 34.274  1.00 20.97 ? 286  ASN B O   1 
ATOM   4449 C  CB  . ASN B 2 286 ? 23.039  -35.956 31.906  1.00 18.07 ? 286  ASN B CB  1 
ATOM   4450 C  CG  . ASN B 2 286 ? 22.662  -37.312 31.361  1.00 22.65 ? 286  ASN B CG  1 
ATOM   4451 O  OD1 . ASN B 2 286 ? 22.907  -38.325 32.002  1.00 26.15 ? 286  ASN B OD1 1 
ATOM   4452 N  ND2 . ASN B 2 286 ? 22.046  -37.342 30.178  1.00 21.24 ? 286  ASN B ND2 1 
ATOM   4453 N  N   . GLY B 2 287 ? 21.959  -33.332 34.175  1.00 19.52 ? 287  GLY B N   1 
ATOM   4454 C  CA  . GLY B 2 287 ? 22.417  -32.455 35.225  1.00 20.24 ? 287  GLY B CA  1 
ATOM   4455 C  C   . GLY B 2 287 ? 23.363  -31.353 34.810  1.00 24.84 ? 287  GLY B C   1 
ATOM   4456 O  O   . GLY B 2 287 ? 23.998  -30.756 35.684  1.00 24.22 ? 287  GLY B O   1 
ATOM   4457 N  N   . GLY B 2 288 ? 23.462  -31.044 33.514  1.00 23.60 ? 288  GLY B N   1 
ATOM   4458 C  CA  . GLY B 2 288 ? 24.286  -29.965 33.021  1.00 19.41 ? 288  GLY B CA  1 
ATOM   4459 C  C   . GLY B 2 288 ? 23.457  -28.807 32.479  1.00 22.86 ? 288  GLY B C   1 
ATOM   4460 O  O   . GLY B 2 288 ? 22.232  -28.823 32.469  1.00 18.83 ? 288  GLY B O   1 
ATOM   4461 N  N   . LYS B 2 289 ? 24.166  -27.781 32.025  1.00 20.54 ? 289  LYS B N   1 
ATOM   4462 C  CA  . LYS B 2 289 ? 23.533  -26.567 31.512  1.00 19.15 ? 289  LYS B CA  1 
ATOM   4463 C  C   . LYS B 2 289 ? 24.086  -26.267 30.127  1.00 21.06 ? 289  LYS B C   1 
ATOM   4464 O  O   . LYS B 2 289 ? 25.271  -25.886 30.007  1.00 19.46 ? 289  LYS B O   1 
ATOM   4465 C  CB  . LYS B 2 289 ? 23.753  -25.388 32.453  1.00 21.86 ? 289  LYS B CB  1 
ATOM   4466 C  CG  . LYS B 2 289 ? 23.158  -25.604 33.858  1.00 34.18 ? 289  LYS B CG  1 
ATOM   4467 C  CD  . LYS B 2 289 ? 23.395  -24.397 34.765  1.00 32.63 ? 289  LYS B CD  1 
ATOM   4468 C  CE  . LYS B 2 289 ? 24.851  -23.942 34.718  1.00 36.36 ? 289  LYS B CE  1 
ATOM   4469 N  N   . PRO B 2 290 ? 23.289  -26.433 29.069  1.00 16.93 ? 290  PRO B N   1 
ATOM   4470 C  CA  . PRO B 2 290 ? 23.802  -26.183 27.714  1.00 15.86 ? 290  PRO B CA  1 
ATOM   4471 C  C   . PRO B 2 290 ? 24.065  -24.700 27.508  1.00 17.50 ? 290  PRO B C   1 
ATOM   4472 O  O   . PRO B 2 290 ? 23.311  -23.848 27.981  1.00 17.34 ? 290  PRO B O   1 
ATOM   4473 C  CB  . PRO B 2 290 ? 22.677  -26.696 26.807  1.00 18.56 ? 290  PRO B CB  1 
ATOM   4474 C  CG  . PRO B 2 290 ? 21.427  -26.586 27.644  1.00 15.78 ? 290  PRO B CG  1 
ATOM   4475 C  CD  . PRO B 2 290 ? 21.868  -26.829 29.075  1.00 18.63 ? 290  PRO B CD  1 
ATOM   4476 N  N   . ALA B 2 291 ? 25.166  -24.389 26.818  1.00 18.85 ? 291  ALA B N   1 
ATOM   4477 C  CA  . ALA B 2 291 ? 25.523  -22.991 26.587  1.00 15.42 ? 291  ALA B CA  1 
ATOM   4478 C  C   . ALA B 2 291 ? 24.836  -22.387 25.372  1.00 18.92 ? 291  ALA B C   1 
ATOM   4479 O  O   . ALA B 2 291 ? 24.770  -21.155 25.265  1.00 22.87 ? 291  ALA B O   1 
ATOM   4480 C  CB  . ALA B 2 291 ? 27.041  -22.845 26.415  1.00 19.51 ? 291  ALA B CB  1 
ATOM   4481 N  N   . ASN B 2 292 ? 24.346  -23.209 24.447  1.00 19.53 ? 292  ASN B N   1 
ATOM   4482 C  CA  . ASN B 2 292 ? 23.773  -22.693 23.211  1.00 18.26 ? 292  ASN B CA  1 
ATOM   4483 C  C   . ASN B 2 292 ? 23.029  -23.807 22.498  1.00 18.51 ? 292  ASN B C   1 
ATOM   4484 O  O   . ASN B 2 292 ? 23.233  -24.992 22.764  1.00 17.44 ? 292  ASN B O   1 
ATOM   4485 C  CB  . ASN B 2 292 ? 24.842  -22.139 22.271  1.00 20.08 ? 292  ASN B CB  1 
ATOM   4486 C  CG  . ASN B 2 292 ? 25.691  -23.242 21.672  1.00 18.10 ? 292  ASN B CG  1 
ATOM   4487 O  OD1 . ASN B 2 292 ? 26.544  -23.806 22.349  1.00 20.89 ? 292  ASN B OD1 1 
ATOM   4488 N  ND2 . ASN B 2 292 ? 25.439  -23.576 20.413  1.00 18.60 ? 292  ASN B ND2 1 
ATOM   4489 N  N   . PHE B 2 293 ? 22.163  -23.391 21.578  1.00 18.59 ? 293  PHE B N   1 
ATOM   4490 C  CA  . PHE B 2 293 ? 21.600  -24.224 20.531  1.00 17.73 ? 293  PHE B CA  1 
ATOM   4491 C  C   . PHE B 2 293 ? 22.332  -23.865 19.248  1.00 15.02 ? 293  PHE B C   1 
ATOM   4492 O  O   . PHE B 2 293 ? 22.578  -22.689 18.984  1.00 17.88 ? 293  PHE B O   1 
ATOM   4493 C  CB  . PHE B 2 293 ? 20.087  -23.945 20.426  1.00 18.86 ? 293  PHE B CB  1 
ATOM   4494 C  CG  . PHE B 2 293 ? 19.422  -24.447 19.177  1.00 17.25 ? 293  PHE B CG  1 
ATOM   4495 C  CD1 . PHE B 2 293 ? 19.278  -23.614 18.073  1.00 19.04 ? 293  PHE B CD1 1 
ATOM   4496 C  CD2 . PHE B 2 293 ? 18.848  -25.711 19.138  1.00 14.24 ? 293  PHE B CD2 1 
ATOM   4497 C  CE1 . PHE B 2 293 ? 18.638  -24.053 16.924  1.00 17.95 ? 293  PHE B CE1 1 
ATOM   4498 C  CE2 . PHE B 2 293 ? 18.199  -26.156 18.003  1.00 16.12 ? 293  PHE B CE2 1 
ATOM   4499 C  CZ  . PHE B 2 293 ? 18.093  -25.326 16.889  1.00 19.69 ? 293  PHE B CZ  1 
ATOM   4500 N  N   . LEU B 2 294 ? 22.726  -24.867 18.474  1.00 15.13 ? 294  LEU B N   1 
ATOM   4501 C  CA  . LEU B 2 294 ? 23.302  -24.606 17.160  1.00 16.49 ? 294  LEU B CA  1 
ATOM   4502 C  C   . LEU B 2 294 ? 22.834  -25.695 16.219  1.00 17.07 ? 294  LEU B C   1 
ATOM   4503 O  O   . LEU B 2 294 ? 23.047  -26.879 16.484  1.00 16.28 ? 294  LEU B O   1 
ATOM   4504 C  CB  . LEU B 2 294 ? 24.830  -24.559 17.184  1.00 16.17 ? 294  LEU B CB  1 
ATOM   4505 C  CG  . LEU B 2 294 ? 25.408  -24.609 15.758  1.00 21.17 ? 294  LEU B CG  1 
ATOM   4506 C  CD1 . LEU B 2 294 ? 25.361  -23.240 15.047  1.00 16.96 ? 294  LEU B CD1 1 
ATOM   4507 C  CD2 . LEU B 2 294 ? 26.807  -25.165 15.730  1.00 22.82 ? 294  LEU B CD2 1 
ATOM   4508 N  N   . ASP B 2 295 ? 22.220  -25.290 15.120  1.00 17.43 ? 295  ASP B N   1 
ATOM   4509 C  CA  . ASP B 2 295 ? 21.645  -26.219 14.151  1.00 19.04 ? 295  ASP B CA  1 
ATOM   4510 C  C   . ASP B 2 295 ? 22.401  -26.036 12.838  1.00 19.33 ? 295  ASP B C   1 
ATOM   4511 O  O   . ASP B 2 295 ? 22.175  -25.058 12.121  1.00 20.62 ? 295  ASP B O   1 
ATOM   4512 C  CB  . ASP B 2 295 ? 20.151  -25.955 13.999  1.00 19.01 ? 295  ASP B CB  1 
ATOM   4513 C  CG  . ASP B 2 295 ? 19.555  -26.622 12.795  1.00 21.24 ? 295  ASP B CG  1 
ATOM   4514 O  OD1 . ASP B 2 295 ? 20.159  -27.583 12.256  1.00 22.29 ? 295  ASP B OD1 1 
ATOM   4515 O  OD2 . ASP B 2 295 ? 18.451  -26.188 12.408  1.00 22.20 ? 295  ASP B OD2 1 
ATOM   4516 N  N   . LEU B 2 296 ? 23.298  -26.973 12.529  1.00 15.42 ? 296  LEU B N   1 
ATOM   4517 C  CA  . LEU B 2 296 ? 23.937  -26.994 11.221  1.00 19.53 ? 296  LEU B CA  1 
ATOM   4518 C  C   . LEU B 2 296 ? 22.963  -27.602 10.218  1.00 23.00 ? 296  LEU B C   1 
ATOM   4519 O  O   . LEU B 2 296 ? 22.529  -28.746 10.387  1.00 21.25 ? 296  LEU B O   1 
ATOM   4520 C  CB  . LEU B 2 296 ? 25.239  -27.786 11.265  1.00 14.70 ? 296  LEU B CB  1 
ATOM   4521 C  CG  . LEU B 2 296 ? 26.312  -27.229 12.212  1.00 20.07 ? 296  LEU B CG  1 
ATOM   4522 C  CD1 . LEU B 2 296 ? 27.564  -28.130 12.165  1.00 17.38 ? 296  LEU B CD1 1 
ATOM   4523 C  CD2 . LEU B 2 296 ? 26.661  -25.769 11.891  1.00 15.29 ? 296  LEU B CD2 1 
ATOM   4524 N  N   . GLY B 2 297 ? 22.618  -26.835 9.187   1.00 19.17 ? 297  GLY B N   1 
ATOM   4525 C  CA  . GLY B 2 297 ? 21.587  -27.248 8.255   1.00 25.53 ? 297  GLY B CA  1 
ATOM   4526 C  C   . GLY B 2 297 ? 22.107  -28.158 7.160   1.00 23.21 ? 297  GLY B C   1 
ATOM   4527 O  O   . GLY B 2 297 ? 23.307  -28.373 7.019   1.00 22.29 ? 297  GLY B O   1 
ATOM   4528 N  N   . GLY B 2 298 ? 21.162  -28.678 6.370   1.00 24.25 ? 298  GLY B N   1 
ATOM   4529 C  CA  . GLY B 2 298 ? 21.510  -29.632 5.326   1.00 25.79 ? 298  GLY B CA  1 
ATOM   4530 C  C   . GLY B 2 298 ? 22.612  -29.156 4.397   1.00 26.50 ? 298  GLY B C   1 
ATOM   4531 O  O   . GLY B 2 298 ? 23.532  -29.913 4.070   1.00 23.90 ? 298  GLY B O   1 
ATOM   4532 N  N   . GLY B 2 299 ? 22.541  -27.900 3.962   1.00 23.97 ? 299  GLY B N   1 
ATOM   4533 C  CA  . GLY B 2 299 ? 23.508  -27.403 3.000   1.00 26.04 ? 299  GLY B CA  1 
ATOM   4534 C  C   . GLY B 2 299 ? 24.727  -26.736 3.612   1.00 29.78 ? 299  GLY B C   1 
ATOM   4535 O  O   . GLY B 2 299 ? 25.387  -25.921 2.957   1.00 26.54 ? 299  GLY B O   1 
ATOM   4536 N  N   . VAL B 2 300 ? 25.064  -27.084 4.856   1.00 23.39 ? 300  VAL B N   1 
ATOM   4537 C  CA  . VAL B 2 300 ? 26.208  -26.441 5.502   1.00 22.42 ? 300  VAL B CA  1 
ATOM   4538 C  C   . VAL B 2 300 ? 27.493  -26.762 4.744   1.00 21.16 ? 300  VAL B C   1 
ATOM   4539 O  O   . VAL B 2 300 ? 27.722  -27.900 4.313   1.00 22.25 ? 300  VAL B O   1 
ATOM   4540 C  CB  . VAL B 2 300 ? 26.305  -26.858 6.983   1.00 20.65 ? 300  VAL B CB  1 
ATOM   4541 C  CG1 . VAL B 2 300 ? 26.733  -28.325 7.131   1.00 23.97 ? 300  VAL B CG1 1 
ATOM   4542 C  CG2 . VAL B 2 300 ? 27.252  -25.922 7.756   1.00 19.55 ? 300  VAL B CG2 1 
ATOM   4543 N  N   . LYS B 2 301 ? 28.338  -25.745 4.568   1.00 20.44 ? 301  LYS B N   1 
ATOM   4544 C  CA  . LYS B 2 301 ? 29.626  -25.874 3.898   1.00 21.90 ? 301  LYS B CA  1 
ATOM   4545 C  C   . LYS B 2 301 ? 30.762  -25.774 4.908   1.00 21.19 ? 301  LYS B C   1 
ATOM   4546 O  O   . LYS B 2 301 ? 30.579  -25.283 6.022   1.00 19.86 ? 301  LYS B O   1 
ATOM   4547 C  CB  . LYS B 2 301 ? 29.792  -24.792 2.822   1.00 24.74 ? 301  LYS B CB  1 
ATOM   4548 C  CG  . LYS B 2 301 ? 28.626  -24.721 1.842   1.00 28.02 ? 301  LYS B CG  1 
ATOM   4549 C  CD  . LYS B 2 301 ? 28.850  -23.653 0.777   1.00 33.60 ? 301  LYS B CD  1 
ATOM   4550 N  N   . GLU B 2 302 ? 31.959  -26.210 4.488   1.00 22.79 ? 302  GLU B N   1 
ATOM   4551 C  CA  . GLU B 2 302 ? 33.079  -26.324 5.425   1.00 19.31 ? 302  GLU B CA  1 
ATOM   4552 C  C   . GLU B 2 302 ? 33.435  -24.977 6.043   1.00 22.31 ? 302  GLU B C   1 
ATOM   4553 O  O   . GLU B 2 302 ? 33.754  -24.896 7.235   1.00 21.52 ? 302  GLU B O   1 
ATOM   4554 C  CB  . GLU B 2 302 ? 34.310  -26.936 4.737   1.00 25.13 ? 302  GLU B CB  1 
ATOM   4555 C  CG  . GLU B 2 302 ? 35.540  -26.964 5.661   1.00 20.11 ? 302  GLU B CG  1 
ATOM   4556 C  CD  . GLU B 2 302 ? 36.870  -27.306 4.985   1.00 31.48 ? 302  GLU B CD  1 
ATOM   4557 O  OE1 . GLU B 2 302 ? 36.920  -28.183 4.091   1.00 25.20 ? 302  GLU B OE1 1 
ATOM   4558 O  OE2 . GLU B 2 302 ? 37.890  -26.700 5.381   1.00 27.24 ? 302  GLU B OE2 1 
ATOM   4559 N  N   . ALA B 2 303 ? 33.399  -23.903 5.255   1.00 22.25 ? 303  ALA B N   1 
ATOM   4560 C  CA  . ALA B 2 303 ? 33.710  -22.595 5.825   1.00 19.55 ? 303  ALA B CA  1 
ATOM   4561 C  C   . ALA B 2 303 ? 32.694  -22.195 6.893   1.00 20.61 ? 303  ALA B C   1 
ATOM   4562 O  O   . ALA B 2 303 ? 33.052  -21.532 7.873   1.00 21.43 ? 303  ALA B O   1 
ATOM   4563 C  CB  . ALA B 2 303 ? 33.787  -21.543 4.719   1.00 26.84 ? 303  ALA B CB  1 
ATOM   4564 N  N   . GLN B 2 304 ? 31.429  -22.580 6.725   1.00 16.05 ? 304  GLN B N   1 
ATOM   4565 C  CA  . GLN B 2 304 ? 30.427  -22.292 7.749   1.00 19.12 ? 304  GLN B CA  1 
ATOM   4566 C  C   . GLN B 2 304 ? 30.651  -23.115 9.012   1.00 20.37 ? 304  GLN B C   1 
ATOM   4567 O  O   . GLN B 2 304 ? 30.482  -22.597 10.125  1.00 17.04 ? 304  GLN B O   1 
ATOM   4568 C  CB  . GLN B 2 304 ? 29.018  -22.551 7.216   1.00 16.81 ? 304  GLN B CB  1 
ATOM   4569 C  CG  . GLN B 2 304 ? 28.525  -21.526 6.220   1.00 21.31 ? 304  GLN B CG  1 
ATOM   4570 C  CD  . GLN B 2 304 ? 27.226  -21.964 5.600   1.00 23.59 ? 304  GLN B CD  1 
ATOM   4571 O  OE1 . GLN B 2 304 ? 27.138  -23.066 5.057   1.00 23.24 ? 304  GLN B OE1 1 
ATOM   4572 N  NE2 . GLN B 2 304 ? 26.203  -21.125 5.696   1.00 25.15 ? 304  GLN B NE2 1 
ATOM   4573 N  N   . VAL B 2 305 ? 30.970  -24.412 8.858   1.00 16.23 ? 305  VAL B N   1 
ATOM   4574 C  CA  . VAL B 2 305 ? 31.342  -25.240 10.011  1.00 17.80 ? 305  VAL B CA  1 
ATOM   4575 C  C   . VAL B 2 305 ? 32.464  -24.572 10.791  1.00 20.03 ? 305  VAL B C   1 
ATOM   4576 O  O   . VAL B 2 305 ? 32.449  -24.505 12.029  1.00 16.92 ? 305  VAL B O   1 
ATOM   4577 C  CB  . VAL B 2 305 ? 31.773  -26.649 9.550   1.00 18.07 ? 305  VAL B CB  1 
ATOM   4578 C  CG1 . VAL B 2 305 ? 32.301  -27.436 10.732  1.00 18.79 ? 305  VAL B CG1 1 
ATOM   4579 C  CG2 . VAL B 2 305 ? 30.631  -27.392 8.865   1.00 20.93 ? 305  VAL B CG2 1 
ATOM   4580 N  N   . TYR B 2 306 ? 33.462  -24.076 10.063  1.00 21.67 ? 306  TYR B N   1 
ATOM   4581 C  CA  . TYR B 2 306 ? 34.623  -23.455 10.682  1.00 20.04 ? 306  TYR B CA  1 
ATOM   4582 C  C   . TYR B 2 306 ? 34.209  -22.225 11.478  1.00 16.01 ? 306  TYR B C   1 
ATOM   4583 O  O   . TYR B 2 306 ? 34.505  -22.117 12.673  1.00 16.50 ? 306  TYR B O   1 
ATOM   4584 C  CB  . TYR B 2 306 ? 35.644  -23.132 9.580   1.00 21.43 ? 306  TYR B CB  1 
ATOM   4585 C  CG  . TYR B 2 306 ? 36.656  -22.070 9.897   1.00 20.19 ? 306  TYR B CG  1 
ATOM   4586 C  CD1 . TYR B 2 306 ? 37.833  -22.371 10.568  1.00 15.42 ? 306  TYR B CD1 1 
ATOM   4587 C  CD2 . TYR B 2 306 ? 36.446  -20.756 9.493   1.00 23.52 ? 306  TYR B CD2 1 
ATOM   4588 C  CE1 . TYR B 2 306 ? 38.766  -21.376 10.853  1.00 16.72 ? 306  TYR B CE1 1 
ATOM   4589 C  CE2 . TYR B 2 306 ? 37.375  -19.757 9.772   1.00 23.30 ? 306  TYR B CE2 1 
ATOM   4590 C  CZ  . TYR B 2 306 ? 38.529  -20.078 10.446  1.00 16.78 ? 306  TYR B CZ  1 
ATOM   4591 O  OH  . TYR B 2 306 ? 39.433  -19.072 10.713  1.00 21.30 ? 306  TYR B OH  1 
ATOM   4592 N  N   . GLN B 2 307 ? 33.472  -21.313 10.846  1.00 18.55 ? 307  GLN B N   1 
ATOM   4593 C  CA  . GLN B 2 307 ? 32.998  -20.132 11.563  1.00 19.49 ? 307  GLN B CA  1 
ATOM   4594 C  C   . GLN B 2 307 ? 32.114  -20.529 12.735  1.00 20.31 ? 307  GLN B C   1 
ATOM   4595 O  O   . GLN B 2 307 ? 32.142  -19.878 13.786  1.00 19.09 ? 307  GLN B O   1 
ATOM   4596 C  CB  . GLN B 2 307 ? 32.233  -19.185 10.629  1.00 23.14 ? 307  GLN B CB  1 
ATOM   4597 C  CG  . GLN B 2 307 ? 33.053  -18.556 9.474   1.00 22.06 ? 307  GLN B CG  1 
ATOM   4598 C  CD  . GLN B 2 307 ? 34.194  -17.649 9.938   1.00 28.20 ? 307  GLN B CD  1 
ATOM   4599 O  OE1 . GLN B 2 307 ? 34.196  -17.148 11.063  1.00 30.45 ? 307  GLN B OE1 1 
ATOM   4600 N  NE2 . GLN B 2 307 ? 35.171  -17.435 9.060   1.00 31.16 ? 307  GLN B NE2 1 
ATOM   4601 N  N   . ALA B 2 308 ? 31.309  -21.586 12.571  1.00 17.04 ? 308  ALA B N   1 
ATOM   4602 C  CA  . ALA B 2 308 ? 30.420  -21.995 13.658  1.00 16.01 ? 308  ALA B CA  1 
ATOM   4603 C  C   . ALA B 2 308 ? 31.220  -22.492 14.853  1.00 16.59 ? 308  ALA B C   1 
ATOM   4604 O  O   . ALA B 2 308 ? 30.914  -22.151 16.007  1.00 16.65 ? 308  ALA B O   1 
ATOM   4605 C  CB  . ALA B 2 308 ? 29.452  -23.074 13.174  1.00 14.96 ? 308  ALA B CB  1 
ATOM   4606 N  N   . PHE B 2 309 ? 32.252  -23.300 14.606  1.00 16.24 ? 309  PHE B N   1 
ATOM   4607 C  CA  . PHE B 2 309 ? 33.025  -23.797 15.733  1.00 14.37 ? 309  PHE B CA  1 
ATOM   4608 C  C   . PHE B 2 309 ? 33.678  -22.648 16.490  1.00 16.52 ? 309  PHE B C   1 
ATOM   4609 O  O   . PHE B 2 309 ? 33.807  -22.707 17.717  1.00 17.17 ? 309  PHE B O   1 
ATOM   4610 C  CB  . PHE B 2 309 ? 34.070  -24.806 15.272  1.00 15.51 ? 309  PHE B CB  1 
ATOM   4611 C  CG  . PHE B 2 309 ? 34.493  -25.741 16.355  1.00 19.28 ? 309  PHE B CG  1 
ATOM   4612 C  CD1 . PHE B 2 309 ? 33.677  -26.800 16.715  1.00 17.36 ? 309  PHE B CD1 1 
ATOM   4613 C  CD2 . PHE B 2 309 ? 35.678  -25.541 17.046  1.00 21.07 ? 309  PHE B CD2 1 
ATOM   4614 C  CE1 . PHE B 2 309 ? 34.038  -27.665 17.740  1.00 20.41 ? 309  PHE B CE1 1 
ATOM   4615 C  CE2 . PHE B 2 309 ? 36.053  -26.404 18.075  1.00 18.29 ? 309  PHE B CE2 1 
ATOM   4616 C  CZ  . PHE B 2 309 ? 35.231  -27.469 18.417  1.00 16.45 ? 309  PHE B CZ  1 
ATOM   4617 N  N   . LYS B 2 310 ? 34.065  -21.585 15.782  1.00 15.05 ? 310  LYS B N   1 
ATOM   4618 C  CA  . LYS B 2 310 ? 34.679  -20.432 16.433  1.00 18.74 ? 310  LYS B CA  1 
ATOM   4619 C  C   . LYS B 2 310 ? 33.688  -19.624 17.274  1.00 20.44 ? 310  LYS B C   1 
ATOM   4620 O  O   . LYS B 2 310 ? 34.116  -18.878 18.161  1.00 24.51 ? 310  LYS B O   1 
ATOM   4621 C  CB  . LYS B 2 310 ? 35.343  -19.543 15.379  1.00 17.93 ? 310  LYS B CB  1 
ATOM   4622 C  CG  . LYS B 2 310 ? 36.511  -20.224 14.679  1.00 19.18 ? 310  LYS B CG  1 
ATOM   4623 C  CD  . LYS B 2 310 ? 37.234  -19.315 13.685  1.00 20.48 ? 310  LYS B CD  1 
ATOM   4624 C  CE  . LYS B 2 310 ? 37.638  -17.987 14.305  1.00 20.45 ? 310  LYS B CE  1 
ATOM   4625 N  NZ  . LYS B 2 310 ? 38.505  -17.242 13.350  1.00 23.38 ? 310  LYS B NZ  1 
ATOM   4626 N  N   . LEU B 2 311 ? 32.379  -19.745 17.026  1.00 19.84 ? 311  LEU B N   1 
ATOM   4627 C  CA  . LEU B 2 311 ? 31.422  -19.098 17.924  1.00 20.45 ? 311  LEU B CA  1 
ATOM   4628 C  C   . LEU B 2 311 ? 31.496  -19.708 19.307  1.00 21.50 ? 311  LEU B C   1 
ATOM   4629 O  O   . LEU B 2 311 ? 31.146  -19.054 20.297  1.00 25.68 ? 311  LEU B O   1 
ATOM   4630 C  CB  . LEU B 2 311 ? 29.989  -19.230 17.408  1.00 24.65 ? 311  LEU B CB  1 
ATOM   4631 C  CG  . LEU B 2 311 ? 29.631  -18.811 15.984  1.00 23.53 ? 311  LEU B CG  1 
ATOM   4632 C  CD1 . LEU B 2 311 ? 28.237  -19.316 15.628  1.00 21.49 ? 311  LEU B CD1 1 
ATOM   4633 C  CD2 . LEU B 2 311 ? 29.731  -17.310 15.830  1.00 24.46 ? 311  LEU B CD2 1 
ATOM   4634 N  N   . LEU B 2 312 ? 31.910  -20.967 19.385  1.00 18.73 ? 312  LEU B N   1 
ATOM   4635 C  CA  . LEU B 2 312 ? 32.013  -21.666 20.655  1.00 21.86 ? 312  LEU B CA  1 
ATOM   4636 C  C   . LEU B 2 312 ? 33.365  -21.421 21.312  1.00 21.85 ? 312  LEU B C   1 
ATOM   4637 O  O   . LEU B 2 312 ? 33.423  -21.047 22.486  1.00 22.70 ? 312  LEU B O   1 
ATOM   4638 C  CB  . LEU B 2 312 ? 31.791  -23.166 20.434  1.00 19.08 ? 312  LEU B CB  1 
ATOM   4639 C  CG  . LEU B 2 312 ? 30.578  -23.457 19.540  1.00 19.37 ? 312  LEU B CG  1 
ATOM   4640 C  CD1 . LEU B 2 312 ? 30.366  -24.946 19.406  1.00 15.14 ? 312  LEU B CD1 1 
ATOM   4641 C  CD2 . LEU B 2 312 ? 29.337  -22.786 20.104  1.00 18.44 ? 312  LEU B CD2 1 
ATOM   4642 N  N   . THR B 2 313 ? 34.456  -21.611 20.557  1.00 22.49 ? 313  THR B N   1 
ATOM   4643 C  CA  . THR B 2 313 ? 35.792  -21.529 21.142  1.00 24.19 ? 313  THR B CA  1 
ATOM   4644 C  C   . THR B 2 313 ? 36.113  -20.127 21.647  1.00 25.45 ? 313  THR B C   1 
ATOM   4645 O  O   . THR B 2 313 ? 36.909  -19.975 22.583  1.00 30.25 ? 313  THR B O   1 
ATOM   4646 C  CB  . THR B 2 313 ? 36.843  -21.988 20.131  1.00 21.67 ? 313  THR B CB  1 
ATOM   4647 O  OG1 . THR B 2 313 ? 36.687  -21.264 18.905  1.00 23.01 ? 313  THR B OG1 1 
ATOM   4648 C  CG2 . THR B 2 313 ? 36.688  -23.473 19.842  1.00 20.23 ? 313  THR B CG2 1 
ATOM   4649 N  N   . ALA B 2 314 ? 35.494  -19.101 21.078  1.00 24.07 ? 314  ALA B N   1 
ATOM   4650 C  CA  . ALA B 2 314 ? 35.721  -17.731 21.511  1.00 22.70 ? 314  ALA B CA  1 
ATOM   4651 C  C   . ALA B 2 314 ? 34.687  -17.258 22.534  1.00 28.54 ? 314  ALA B C   1 
ATOM   4652 O  O   . ALA B 2 314 ? 34.613  -16.060 22.828  1.00 24.84 ? 314  ALA B O   1 
ATOM   4653 C  CB  . ALA B 2 314 ? 35.729  -16.798 20.299  1.00 24.44 ? 314  ALA B CB  1 
ATOM   4654 N  N   . ASP B 2 315 ? 33.882  -18.165 23.078  1.00 25.00 ? 315  ASP B N   1 
ATOM   4655 C  CA  . ASP B 2 315 ? 32.892  -17.779 24.071  1.00 21.21 ? 315  ASP B CA  1 
ATOM   4656 C  C   . ASP B 2 315 ? 33.460  -18.057 25.456  1.00 23.09 ? 315  ASP B C   1 
ATOM   4657 O  O   . ASP B 2 315 ? 33.689  -19.228 25.795  1.00 24.28 ? 315  ASP B O   1 
ATOM   4658 C  CB  . ASP B 2 315 ? 31.595  -18.551 23.847  1.00 20.65 ? 315  ASP B CB  1 
ATOM   4659 C  CG  . ASP B 2 315 ? 30.483  -18.126 24.786  1.00 22.81 ? 315  ASP B CG  1 
ATOM   4660 O  OD1 . ASP B 2 315 ? 30.720  -17.294 25.678  1.00 28.76 ? 315  ASP B OD1 1 
ATOM   4661 O  OD2 . ASP B 2 315 ? 29.364  -18.630 24.630  1.00 21.64 ? 315  ASP B OD2 1 
ATOM   4662 N  N   . PRO B 2 316 ? 33.711  -17.033 26.284  1.00 26.03 ? 316  PRO B N   1 
ATOM   4663 C  CA  . PRO B 2 316 ? 34.385  -17.277 27.575  1.00 29.66 ? 316  PRO B CA  1 
ATOM   4664 C  C   . PRO B 2 316 ? 33.547  -18.057 28.561  1.00 25.96 ? 316  PRO B C   1 
ATOM   4665 O  O   . PRO B 2 316 ? 34.090  -18.550 29.556  1.00 21.89 ? 316  PRO B O   1 
ATOM   4666 C  CB  . PRO B 2 316 ? 34.666  -15.862 28.101  1.00 32.37 ? 316  PRO B CB  1 
ATOM   4667 C  CG  . PRO B 2 316 ? 33.593  -15.012 27.453  1.00 25.14 ? 316  PRO B CG  1 
ATOM   4668 C  CD  . PRO B 2 316 ? 33.365  -15.612 26.093  1.00 24.99 ? 316  PRO B CD  1 
ATOM   4669 N  N   . LYS B 2 317 ? 32.238  -18.148 28.341  1.00 25.82 ? 317  LYS B N   1 
ATOM   4670 C  CA  . LYS B 2 317 ? 31.374  -18.930 29.211  1.00 22.75 ? 317  LYS B CA  1 
ATOM   4671 C  C   . LYS B 2 317 ? 31.485  -20.420 28.932  1.00 23.68 ? 317  LYS B C   1 
ATOM   4672 O  O   . LYS B 2 317 ? 31.134  -21.235 29.793  1.00 18.74 ? 317  LYS B O   1 
ATOM   4673 C  CB  . LYS B 2 317 ? 29.924  -18.473 29.028  1.00 28.26 ? 317  LYS B CB  1 
ATOM   4674 C  CG  . LYS B 2 317 ? 29.055  -18.652 30.257  1.00 39.68 ? 317  LYS B CG  1 
ATOM   4675 N  N   . VAL B 2 318 ? 31.970  -20.789 27.751  1.00 19.88 ? 318  VAL B N   1 
ATOM   4676 C  CA  . VAL B 2 318 ? 31.985  -22.184 27.328  1.00 20.65 ? 318  VAL B CA  1 
ATOM   4677 C  C   . VAL B 2 318 ? 33.087  -22.910 28.093  1.00 24.35 ? 318  VAL B C   1 
ATOM   4678 O  O   . VAL B 2 318 ? 34.260  -22.527 28.024  1.00 24.06 ? 318  VAL B O   1 
ATOM   4679 C  CB  . VAL B 2 318 ? 32.177  -22.290 25.806  1.00 21.16 ? 318  VAL B CB  1 
ATOM   4680 C  CG1 . VAL B 2 318 ? 32.556  -23.698 25.394  1.00 18.30 ? 318  VAL B CG1 1 
ATOM   4681 C  CG2 . VAL B 2 318 ? 30.885  -21.870 25.100  1.00 22.33 ? 318  VAL B CG2 1 
ATOM   4682 N  N   . GLU B 2 319 ? 32.711  -23.952 28.840  1.00 19.19 ? 319  GLU B N   1 
ATOM   4683 C  CA  . GLU B 2 319 ? 33.691  -24.758 29.556  1.00 20.81 ? 319  GLU B CA  1 
ATOM   4684 C  C   . GLU B 2 319 ? 33.904  -26.131 28.945  1.00 21.67 ? 319  GLU B C   1 
ATOM   4685 O  O   . GLU B 2 319 ? 34.863  -26.811 29.319  1.00 22.93 ? 319  GLU B O   1 
ATOM   4686 C  CB  . GLU B 2 319 ? 33.291  -24.906 31.034  1.00 19.60 ? 319  GLU B CB  1 
ATOM   4687 C  CG  . GLU B 2 319 ? 33.457  -23.605 31.833  1.00 24.88 ? 319  GLU B CG  1 
ATOM   4688 C  CD  . GLU B 2 319 ? 32.761  -23.638 33.188  1.00 28.43 ? 319  GLU B CD  1 
ATOM   4689 O  OE1 . GLU B 2 319 ? 32.042  -22.670 33.502  1.00 29.67 ? 319  GLU B OE1 1 
ATOM   4690 O  OE2 . GLU B 2 319 ? 32.926  -24.629 33.927  1.00 28.68 ? 319  GLU B OE2 1 
ATOM   4691 N  N   . ALA B 2 320 ? 33.052  -26.551 28.013  1.00 17.23 ? 320  ALA B N   1 
ATOM   4692 C  CA  . ALA B 2 320 ? 33.232  -27.817 27.317  1.00 19.00 ? 320  ALA B CA  1 
ATOM   4693 C  C   . ALA B 2 320 ? 32.397  -27.779 26.051  1.00 17.59 ? 320  ALA B C   1 
ATOM   4694 O  O   . ALA B 2 320 ? 31.424  -27.022 25.951  1.00 16.59 ? 320  ALA B O   1 
ATOM   4695 C  CB  . ALA B 2 320 ? 32.843  -29.024 28.181  1.00 16.47 ? 320  ALA B CB  1 
ATOM   4696 N  N   . ILE B 2 321 ? 32.781  -28.612 25.084  1.00 16.67 ? 321  ILE B N   1 
ATOM   4697 C  CA  . ILE B 2 321 ? 32.136  -28.621 23.778  1.00 17.24 ? 321  ILE B CA  1 
ATOM   4698 C  C   . ILE B 2 321 ? 31.662  -30.032 23.478  1.00 17.76 ? 321  ILE B C   1 
ATOM   4699 O  O   . ILE B 2 321 ? 32.435  -30.995 23.571  1.00 16.17 ? 321  ILE B O   1 
ATOM   4700 C  CB  . ILE B 2 321 ? 33.073  -28.102 22.670  1.00 20.18 ? 321  ILE B CB  1 
ATOM   4701 C  CG1 . ILE B 2 321 ? 33.473  -26.649 22.951  1.00 18.24 ? 321  ILE B CG1 1 
ATOM   4702 C  CG2 . ILE B 2 321 ? 32.403  -28.204 21.312  1.00 14.48 ? 321  ILE B CG2 1 
ATOM   4703 C  CD1 . ILE B 2 321 ? 34.488  -26.083 21.947  1.00 17.17 ? 321  ILE B CD1 1 
ATOM   4704 N  N   . LEU B 2 322 ? 30.382  -30.160 23.149  1.00 13.79 ? 322  LEU B N   1 
ATOM   4705 C  CA  . LEU B 2 322 ? 29.790  -31.447 22.804  1.00 15.62 ? 322  LEU B CA  1 
ATOM   4706 C  C   . LEU B 2 322 ? 29.465  -31.385 21.317  1.00 16.23 ? 322  LEU B C   1 
ATOM   4707 O  O   . LEU B 2 322 ? 28.568  -30.640 20.893  1.00 11.31 ? 322  LEU B O   1 
ATOM   4708 C  CB  . LEU B 2 322 ? 28.545  -31.742 23.650  1.00 13.91 ? 322  LEU B CB  1 
ATOM   4709 C  CG  . LEU B 2 322 ? 27.979  -33.172 23.693  1.00 18.22 ? 322  LEU B CG  1 
ATOM   4710 C  CD1 . LEU B 2 322 ? 26.762  -33.264 24.640  1.00 14.15 ? 322  LEU B CD1 1 
ATOM   4711 C  CD2 . LEU B 2 322 ? 27.606  -33.712 22.334  1.00 21.20 ? 322  LEU B CD2 1 
ATOM   4712 N  N   . VAL B 2 323 ? 30.196  -32.155 20.529  1.00 15.50 ? 323  VAL B N   1 
ATOM   4713 C  CA  . VAL B 2 323 ? 29.921  -32.279 19.108  1.00 15.12 ? 323  VAL B CA  1 
ATOM   4714 C  C   . VAL B 2 323 ? 29.088  -33.529 18.901  1.00 17.17 ? 323  VAL B C   1 
ATOM   4715 O  O   . VAL B 2 323 ? 29.512  -34.638 19.249  1.00 17.23 ? 323  VAL B O   1 
ATOM   4716 C  CB  . VAL B 2 323 ? 31.209  -32.345 18.281  1.00 16.83 ? 323  VAL B CB  1 
ATOM   4717 C  CG1 . VAL B 2 323 ? 30.854  -32.700 16.873  1.00 17.42 ? 323  VAL B CG1 1 
ATOM   4718 C  CG2 . VAL B 2 323 ? 31.930  -31.007 18.309  1.00 15.62 ? 323  VAL B CG2 1 
ATOM   4719 N  N   . ASN B 2 324 ? 27.905  -33.374 18.328  1.00 15.80 ? 324  ASN B N   1 
ATOM   4720 C  CA  . ASN B 2 324 ? 27.072  -34.543 18.087  1.00 14.05 ? 324  ASN B CA  1 
ATOM   4721 C  C   . ASN B 2 324 ? 26.469  -34.438 16.699  1.00 18.25 ? 324  ASN B C   1 
ATOM   4722 O  O   . ASN B 2 324 ? 25.640  -33.559 16.445  1.00 15.81 ? 324  ASN B O   1 
ATOM   4723 C  CB  . ASN B 2 324 ? 25.990  -34.686 19.150  1.00 17.18 ? 324  ASN B CB  1 
ATOM   4724 C  CG  . ASN B 2 324 ? 25.017  -35.775 18.814  1.00 17.04 ? 324  ASN B CG  1 
ATOM   4725 O  OD1 . ASN B 2 324 ? 25.411  -36.871 18.464  1.00 18.33 ? 324  ASN B OD1 1 
ATOM   4726 N  ND2 . ASN B 2 324 ? 23.737  -35.461 18.874  1.00 18.82 ? 324  ASN B ND2 1 
ATOM   4727 N  N   . ILE B 2 325 ? 26.862  -35.353 15.816  1.00 15.69 ? 325  ILE B N   1 
ATOM   4728 C  CA  . ILE B 2 325 ? 26.502  -35.294 14.409  1.00 15.90 ? 325  ILE B CA  1 
ATOM   4729 C  C   . ILE B 2 325 ? 25.921  -36.632 13.993  1.00 16.42 ? 325  ILE B C   1 
ATOM   4730 O  O   . ILE B 2 325 ? 26.564  -37.678 14.161  1.00 13.87 ? 325  ILE B O   1 
ATOM   4731 C  CB  . ILE B 2 325 ? 27.713  -34.953 13.518  1.00 18.25 ? 325  ILE B CB  1 
ATOM   4732 C  CG1 . ILE B 2 325 ? 28.385  -33.661 13.984  1.00 15.02 ? 325  ILE B CG1 1 
ATOM   4733 C  CG2 . ILE B 2 325 ? 27.279  -34.857 12.071  1.00 15.07 ? 325  ILE B CG2 1 
ATOM   4734 C  CD1 . ILE B 2 325 ? 27.590  -32.445 13.733  1.00 16.20 ? 325  ILE B CD1 1 
ATOM   4735 N  N   . PHE B 2 326 ? 24.718  -36.606 13.431  1.00 14.45 ? 326  PHE B N   1 
ATOM   4736 C  CA  . PHE B 2 326 ? 24.160  -37.796 12.789  1.00 16.60 ? 326  PHE B CA  1 
ATOM   4737 C  C   . PHE B 2 326 ? 23.870  -37.396 11.352  1.00 15.53 ? 326  PHE B C   1 
ATOM   4738 O  O   . PHE B 2 326 ? 22.808  -36.854 11.056  1.00 12.28 ? 326  PHE B O   1 
ATOM   4739 C  CB  . PHE B 2 326 ? 22.924  -38.334 13.495  1.00 16.64 ? 326  PHE B CB  1 
ATOM   4740 C  CG  . PHE B 2 326 ? 22.758  -39.826 13.335  1.00 17.59 ? 326  PHE B CG  1 
ATOM   4741 C  CD1 . PHE B 2 326 ? 23.112  -40.448 12.144  1.00 16.36 ? 326  PHE B CD1 1 
ATOM   4742 C  CD2 . PHE B 2 326 ? 22.297  -40.611 14.381  1.00 17.97 ? 326  PHE B CD2 1 
ATOM   4743 C  CE1 . PHE B 2 326 ? 22.983  -41.823 11.987  1.00 16.47 ? 326  PHE B CE1 1 
ATOM   4744 C  CE2 . PHE B 2 326 ? 22.158  -41.996 14.227  1.00 18.69 ? 326  PHE B CE2 1 
ATOM   4745 C  CZ  . PHE B 2 326 ? 22.493  -42.600 13.037  1.00 14.47 ? 326  PHE B CZ  1 
ATOM   4746 N  N   . GLY B 2 327 ? 24.838  -37.660 10.474  1.00 19.62 ? 327  GLY B N   1 
ATOM   4747 C  CA  . GLY B 2 327 ? 24.831  -37.078 9.151   1.00 17.68 ? 327  GLY B CA  1 
ATOM   4748 C  C   . GLY B 2 327 ? 23.924  -37.835 8.204   1.00 20.53 ? 327  GLY B C   1 
ATOM   4749 O  O   . GLY B 2 327 ? 24.018  -39.060 8.068   1.00 17.57 ? 327  GLY B O   1 
ATOM   4750 N  N   . GLY B 2 328 ? 23.049  -37.098 7.545   1.00 16.64 ? 328  GLY B N   1 
ATOM   4751 C  CA  . GLY B 2 328 ? 22.202  -37.601 6.492   1.00 15.78 ? 328  GLY B CA  1 
ATOM   4752 C  C   . GLY B 2 328 ? 22.653  -36.966 5.199   1.00 20.98 ? 328  GLY B C   1 
ATOM   4753 O  O   . GLY B 2 328 ? 23.556  -37.474 4.523   1.00 21.28 ? 328  GLY B O   1 
ATOM   4754 N  N   . ILE B 2 329 ? 22.005  -35.860 4.828   1.00 16.12 ? 329  ILE B N   1 
ATOM   4755 C  CA  . ILE B 2 329 ? 22.520  -35.050 3.725   1.00 22.45 ? 329  ILE B CA  1 
ATOM   4756 C  C   . ILE B 2 329 ? 23.835  -34.354 4.102   1.00 22.83 ? 329  ILE B C   1 
ATOM   4757 O  O   . ILE B 2 329 ? 24.607  -33.980 3.214   1.00 20.54 ? 329  ILE B O   1 
ATOM   4758 C  CB  . ILE B 2 329 ? 21.450  -34.041 3.257   1.00 23.60 ? 329  ILE B CB  1 
ATOM   4759 C  CG1 . ILE B 2 329 ? 21.863  -33.347 1.952   1.00 25.03 ? 329  ILE B CG1 1 
ATOM   4760 C  CG2 . ILE B 2 329 ? 21.238  -32.965 4.292   1.00 24.39 ? 329  ILE B CG2 1 
ATOM   4761 C  CD1 . ILE B 2 329 ? 20.869  -32.266 1.515   1.00 25.75 ? 329  ILE B CD1 1 
ATOM   4762 N  N   . VAL B 2 330 ? 24.133  -34.216 5.393   1.00 20.76 ? 330  VAL B N   1 
ATOM   4763 C  CA  . VAL B 2 330 ? 25.407  -33.655 5.852   1.00 21.01 ? 330  VAL B CA  1 
ATOM   4764 C  C   . VAL B 2 330 ? 26.489  -34.732 5.832   1.00 20.95 ? 330  VAL B C   1 
ATOM   4765 O  O   . VAL B 2 330 ? 26.327  -35.809 6.422   1.00 21.96 ? 330  VAL B O   1 
ATOM   4766 C  CB  . VAL B 2 330 ? 25.259  -33.062 7.264   1.00 22.88 ? 330  VAL B CB  1 
ATOM   4767 C  CG1 . VAL B 2 330 ? 26.628  -32.835 7.889   1.00 24.79 ? 330  VAL B CG1 1 
ATOM   4768 C  CG2 . VAL B 2 330 ? 24.464  -31.759 7.224   1.00 18.07 ? 330  VAL B CG2 1 
ATOM   4769 N  N   . ASN B 2 331 ? 27.605  -34.438 5.168   1.00 23.98 ? 331  ASN B N   1 
ATOM   4770 C  CA  . ASN B 2 331 ? 28.753  -35.339 5.126   1.00 23.23 ? 331  ASN B CA  1 
ATOM   4771 C  C   . ASN B 2 331 ? 29.629  -35.090 6.358   1.00 21.02 ? 331  ASN B C   1 
ATOM   4772 O  O   . ASN B 2 331 ? 30.072  -33.963 6.585   1.00 22.19 ? 331  ASN B O   1 
ATOM   4773 C  CB  . ASN B 2 331 ? 29.531  -35.136 3.816   1.00 20.83 ? 331  ASN B CB  1 
ATOM   4774 C  CG  . ASN B 2 331 ? 30.664  -36.136 3.644   1.00 25.82 ? 331  ASN B CG  1 
ATOM   4775 O  OD1 . ASN B 2 331 ? 31.450  -36.364 4.563   1.00 25.59 ? 331  ASN B OD1 1 
ATOM   4776 N  ND2 . ASN B 2 331 ? 30.744  -36.751 2.467   1.00 31.53 ? 331  ASN B ND2 1 
ATOM   4777 N  N   . CYS B 2 332 ? 29.863  -36.138 7.164   1.00 23.03 ? 332  CYS B N   1 
ATOM   4778 C  CA  . CYS B 2 332 ? 30.592  -35.973 8.427   1.00 20.13 ? 332  CYS B CA  1 
ATOM   4779 C  C   . CYS B 2 332 ? 32.009  -35.430 8.223   1.00 18.84 ? 332  CYS B C   1 
ATOM   4780 O  O   . CYS B 2 332 ? 32.545  -34.749 9.106   1.00 20.42 ? 332  CYS B O   1 
ATOM   4781 C  CB  . CYS B 2 332 ? 30.656  -37.304 9.192   1.00 18.57 ? 332  CYS B CB  1 
ATOM   4782 S  SG  . CYS B 2 332 ? 29.093  -37.852 9.994   1.00 18.55 ? 332  CYS B SG  1 
ATOM   4783 N  N   . ALA B 2 333 ? 32.637  -35.719 7.087   1.00 19.05 ? 333  ALA B N   1 
ATOM   4784 C  CA  . ALA B 2 333 ? 33.987  -35.214 6.856   1.00 19.67 ? 333  ALA B CA  1 
ATOM   4785 C  C   . ALA B 2 333 ? 34.016  -33.692 6.768   1.00 21.19 ? 333  ALA B C   1 
ATOM   4786 O  O   . ALA B 2 333 ? 35.008  -33.070 7.165   1.00 17.49 ? 333  ALA B O   1 
ATOM   4787 C  CB  . ALA B 2 333 ? 34.567  -35.825 5.583   1.00 20.74 ? 333  ALA B CB  1 
ATOM   4788 N  N   . ILE B 2 334 ? 32.949  -33.072 6.239   1.00 18.03 ? 334  ILE B N   1 
ATOM   4789 C  CA  . ILE B 2 334 ? 32.892  -31.613 6.202   1.00 20.90 ? 334  ILE B CA  1 
ATOM   4790 C  C   . ILE B 2 334 ? 32.922  -31.044 7.616   1.00 17.38 ? 334  ILE B C   1 
ATOM   4791 O  O   . ILE B 2 334 ? 33.593  -30.038 7.882   1.00 19.71 ? 334  ILE B O   1 
ATOM   4792 C  CB  . ILE B 2 334 ? 31.651  -31.144 5.422   1.00 23.62 ? 334  ILE B CB  1 
ATOM   4793 C  CG1 . ILE B 2 334 ? 31.730  -31.611 3.958   1.00 23.64 ? 334  ILE B CG1 1 
ATOM   4794 C  CG2 . ILE B 2 334 ? 31.519  -29.628 5.495   1.00 23.92 ? 334  ILE B CG2 1 
ATOM   4795 C  CD1 . ILE B 2 334 ? 30.535  -31.201 3.112   1.00 27.18 ? 334  ILE B CD1 1 
ATOM   4796 N  N   . ILE B 2 335 ? 32.194  -31.677 8.543   1.00 17.14 ? 335  ILE B N   1 
ATOM   4797 C  CA  . ILE B 2 335 ? 32.244  -31.269 9.945   1.00 16.07 ? 335  ILE B CA  1 
ATOM   4798 C  C   . ILE B 2 335 ? 33.660  -31.422 10.488  1.00 16.50 ? 335  ILE B C   1 
ATOM   4799 O  O   . ILE B 2 335 ? 34.212  -30.500 11.101  1.00 19.17 ? 335  ILE B O   1 
ATOM   4800 C  CB  . ILE B 2 335 ? 31.239  -32.079 10.794  1.00 16.16 ? 335  ILE B CB  1 
ATOM   4801 C  CG1 . ILE B 2 335 ? 29.838  -32.129 10.164  1.00 16.87 ? 335  ILE B CG1 1 
ATOM   4802 C  CG2 . ILE B 2 335 ? 31.215  -31.548 12.250  1.00 18.83 ? 335  ILE B CG2 1 
ATOM   4803 C  CD1 . ILE B 2 335 ? 29.139  -30.780 9.997   1.00 16.59 ? 335  ILE B CD1 1 
ATOM   4804 N  N   . ALA B 2 336 ? 34.261  -32.607 10.303  1.00 16.36 ? 336  ALA B N   1 
ATOM   4805 C  CA  . ALA B 2 336 ? 35.590  -32.853 10.864  1.00 19.14 ? 336  ALA B CA  1 
ATOM   4806 C  C   . ALA B 2 336 ? 36.611  -31.866 10.314  1.00 14.35 ? 336  ALA B C   1 
ATOM   4807 O  O   . ALA B 2 336 ? 37.456  -31.362 11.057  1.00 17.86 ? 336  ALA B O   1 
ATOM   4808 C  CB  . ALA B 2 336 ? 36.034  -34.289 10.581  1.00 16.30 ? 336  ALA B CB  1 
ATOM   4809 N  N   . ASN B 2 337 ? 36.527  -31.565 9.016   1.00 16.27 ? 337  ASN B N   1 
ATOM   4810 C  CA  . ASN B 2 337 ? 37.462  -30.634 8.389   1.00 16.19 ? 337  ASN B CA  1 
ATOM   4811 C  C   . ASN B 2 337 ? 37.311  -29.224 8.947   1.00 19.85 ? 337  ASN B C   1 
ATOM   4812 O  O   . ASN B 2 337 ? 38.307  -28.533 9.185   1.00 19.34 ? 337  ASN B O   1 
ATOM   4813 C  CB  . ASN B 2 337 ? 37.255  -30.642 6.871   1.00 16.31 ? 337  ASN B CB  1 
ATOM   4814 C  CG  . ASN B 2 337 ? 37.874  -31.854 6.221   1.00 22.26 ? 337  ASN B CG  1 
ATOM   4815 O  OD1 . ASN B 2 337 ? 38.799  -32.444 6.775   1.00 21.62 ? 337  ASN B OD1 1 
ATOM   4816 N  ND2 . ASN B 2 337 ? 37.383  -32.227 5.049   1.00 19.63 ? 337  ASN B ND2 1 
ATOM   4817 N  N   . GLY B 2 338 ? 36.076  -28.767 9.149   1.00 17.26 ? 338  GLY B N   1 
ATOM   4818 C  CA  . GLY B 2 338 ? 35.887  -27.425 9.672   1.00 16.75 ? 338  GLY B CA  1 
ATOM   4819 C  C   . GLY B 2 338 ? 36.329  -27.298 11.119  1.00 17.37 ? 338  GLY B C   1 
ATOM   4820 O  O   . GLY B 2 338 ? 36.849  -26.259 11.527  1.00 16.65 ? 338  GLY B O   1 
ATOM   4821 N  N   . ILE B 2 339 ? 36.105  -28.344 11.917  1.00 14.37 ? 339  ILE B N   1 
ATOM   4822 C  CA  . ILE B 2 339 ? 36.521  -28.342 13.315  1.00 16.25 ? 339  ILE B CA  1 
ATOM   4823 C  C   . ILE B 2 339 ? 38.039  -28.311 13.419  1.00 17.84 ? 339  ILE B C   1 
ATOM   4824 O  O   . ILE B 2 339 ? 38.619  -27.484 14.135  1.00 17.97 ? 339  ILE B O   1 
ATOM   4825 C  CB  . ILE B 2 339 ? 35.935  -29.564 14.046  1.00 20.67 ? 339  ILE B CB  1 
ATOM   4826 C  CG1 . ILE B 2 339 ? 34.419  -29.410 14.209  1.00 20.45 ? 339  ILE B CG1 1 
ATOM   4827 C  CG2 . ILE B 2 339 ? 36.606  -29.746 15.400  1.00 20.82 ? 339  ILE B CG2 1 
ATOM   4828 C  CD1 . ILE B 2 339 ? 33.765  -30.643 14.749  1.00 20.42 ? 339  ILE B CD1 1 
ATOM   4829 N  N   . THR B 2 340 ? 38.711  -29.203 12.692  1.00 19.45 ? 340  THR B N   1 
ATOM   4830 C  CA  . THR B 2 340 ? 40.165  -29.249 12.799  1.00 19.33 ? 340  THR B CA  1 
ATOM   4831 C  C   . THR B 2 340 ? 40.787  -27.945 12.308  1.00 17.64 ? 340  THR B C   1 
ATOM   4832 O  O   . THR B 2 340 ? 41.740  -27.448 12.912  1.00 18.93 ? 340  THR B O   1 
ATOM   4833 C  CB  . THR B 2 340 ? 40.729  -30.454 12.038  1.00 20.07 ? 340  THR B CB  1 
ATOM   4834 O  OG1 . THR B 2 340 ? 40.285  -30.423 10.685  1.00 20.84 ? 340  THR B OG1 1 
ATOM   4835 C  CG2 . THR B 2 340 ? 40.262  -31.774 12.678  1.00 18.85 ? 340  THR B CG2 1 
ATOM   4836 N  N   . LYS B 2 341 ? 40.235  -27.358 11.237  1.00 15.61 ? 341  LYS B N   1 
ATOM   4837 C  CA  . LYS B 2 341 ? 40.750  -26.079 10.752  1.00 19.50 ? 341  LYS B CA  1 
ATOM   4838 C  C   . LYS B 2 341 ? 40.585  -24.976 11.793  1.00 19.58 ? 341  LYS B C   1 
ATOM   4839 O  O   . LYS B 2 341 ? 41.471  -24.128 11.950  1.00 19.90 ? 341  LYS B O   1 
ATOM   4840 C  CB  . LYS B 2 341 ? 40.055  -25.679 9.447   1.00 19.96 ? 341  LYS B CB  1 
ATOM   4841 C  CG  . LYS B 2 341 ? 40.541  -24.340 8.861   1.00 23.21 ? 341  LYS B CG  1 
ATOM   4842 C  CD  . LYS B 2 341 ? 39.655  -23.866 7.688   1.00 26.65 ? 341  LYS B CD  1 
ATOM   4843 C  CE  . LYS B 2 341 ? 40.237  -22.604 7.042   1.00 31.37 ? 341  LYS B CE  1 
ATOM   4844 N  NZ  . LYS B 2 341 ? 39.404  -22.068 5.917   1.00 28.73 ? 341  LYS B NZ  1 
ATOM   4845 N  N   . ALA B 2 342 ? 39.452  -24.959 12.512  1.00 19.30 ? 342  ALA B N   1 
ATOM   4846 C  CA  . ALA B 2 342 ? 39.262  -23.954 13.557  1.00 17.85 ? 342  ALA B CA  1 
ATOM   4847 C  C   . ALA B 2 342 ? 40.217  -24.180 14.730  1.00 20.75 ? 342  ALA B C   1 
ATOM   4848 O  O   . ALA B 2 342 ? 40.738  -23.218 15.309  1.00 22.31 ? 342  ALA B O   1 
ATOM   4849 C  CB  . ALA B 2 342 ? 37.809  -23.959 14.046  1.00 17.09 ? 342  ALA B CB  1 
ATOM   4850 N  N   . CYS B 2 343 ? 40.443  -25.440 15.108  1.00 19.49 ? 343  CYS B N   1 
ATOM   4851 C  CA  . CYS B 2 343 ? 41.299  -25.735 16.253  1.00 18.71 ? 343  CYS B CA  1 
ATOM   4852 C  C   . CYS B 2 343 ? 42.777  -25.549 15.930  1.00 22.24 ? 343  CYS B C   1 
ATOM   4853 O  O   . CYS B 2 343 ? 43.590  -25.439 16.851  1.00 26.89 ? 343  CYS B O   1 
ATOM   4854 C  CB  . CYS B 2 343 ? 41.034  -27.163 16.755  1.00 15.42 ? 343  CYS B CB  1 
ATOM   4855 S  SG  . CYS B 2 343 ? 39.380  -27.410 17.509  1.00 20.27 ? 343  CYS B SG  1 
ATOM   4856 N  N   . ARG B 2 344 ? 43.147  -25.509 14.650  1.00 22.82 ? 344  ARG B N   1 
ATOM   4857 C  CA  . ARG B 2 344 ? 44.531  -25.204 14.309  1.00 26.44 ? 344  ARG B CA  1 
ATOM   4858 C  C   . ARG B 2 344 ? 44.940  -23.804 14.759  1.00 27.40 ? 344  ARG B C   1 
ATOM   4859 O  O   . ARG B 2 344 ? 46.139  -23.553 14.910  1.00 24.96 ? 344  ARG B O   1 
ATOM   4860 C  CB  . ARG B 2 344 ? 44.756  -25.381 12.801  1.00 26.35 ? 344  ARG B CB  1 
ATOM   4861 C  CG  . ARG B 2 344 ? 44.896  -26.846 12.396  1.00 23.70 ? 344  ARG B CG  1 
ATOM   4862 C  CD  . ARG B 2 344 ? 45.584  -27.043 11.056  1.00 25.03 ? 344  ARG B CD  1 
ATOM   4863 N  NE  . ARG B 2 344 ? 44.706  -26.793 9.914   1.00 28.18 ? 344  ARG B NE  1 
ATOM   4864 C  CZ  . ARG B 2 344 ? 43.827  -27.674 9.438   1.00 29.34 ? 344  ARG B CZ  1 
ATOM   4865 N  NH1 . ARG B 2 344 ? 43.701  -28.867 10.015  1.00 27.08 ? 344  ARG B NH1 1 
ATOM   4866 N  NH2 . ARG B 2 344 ? 43.065  -27.363 8.387   1.00 27.99 ? 344  ARG B NH2 1 
ATOM   4867 N  N   . GLU B 2 345 ? 43.968  -22.919 15.049  1.00 27.79 ? 345  GLU B N   1 
ATOM   4868 C  CA  . GLU B 2 345 ? 44.195  -21.519 15.402  1.00 23.17 ? 345  GLU B CA  1 
ATOM   4869 C  C   . GLU B 2 345 ? 44.361  -21.265 16.887  1.00 23.88 ? 345  GLU B C   1 
ATOM   4870 O  O   . GLU B 2 345 ? 44.748  -20.154 17.257  1.00 28.01 ? 345  GLU B O   1 
ATOM   4871 C  CB  . GLU B 2 345 ? 43.026  -20.647 14.929  1.00 23.40 ? 345  GLU B CB  1 
ATOM   4872 C  CG  . GLU B 2 345 ? 42.703  -20.805 13.476  1.00 22.92 ? 345  GLU B CG  1 
ATOM   4873 C  CD  . GLU B 2 345 ? 41.624  -19.853 13.027  1.00 20.85 ? 345  GLU B CD  1 
ATOM   4874 O  OE1 . GLU B 2 345 ? 40.953  -19.248 13.892  1.00 23.83 ? 345  GLU B OE1 1 
ATOM   4875 O  OE2 . GLU B 2 345 ? 41.453  -19.706 11.811  1.00 23.06 ? 345  GLU B OE2 1 
ATOM   4876 N  N   . LEU B 2 346 ? 44.039  -22.227 17.748  1.00 25.96 ? 346  LEU B N   1 
ATOM   4877 C  CA  . LEU B 2 346 ? 44.004  -21.981 19.177  1.00 24.12 ? 346  LEU B CA  1 
ATOM   4878 C  C   . LEU B 2 346 ? 44.564  -23.177 19.931  1.00 24.72 ? 346  LEU B C   1 
ATOM   4879 O  O   . LEU B 2 346 ? 44.560  -24.303 19.436  1.00 27.02 ? 346  LEU B O   1 
ATOM   4880 C  CB  . LEU B 2 346 ? 42.578  -21.695 19.658  1.00 32.72 ? 346  LEU B CB  1 
ATOM   4881 N  N   . GLU B 2 347 ? 45.066  -22.920 21.128  1.00 31.14 ? 347  GLU B N   1 
ATOM   4882 C  CA  . GLU B 2 347 ? 45.395  -23.994 22.061  1.00 31.99 ? 347  GLU B CA  1 
ATOM   4883 C  C   . GLU B 2 347 ? 44.094  -24.391 22.749  1.00 31.48 ? 347  GLU B C   1 
ATOM   4884 O  O   . GLU B 2 347 ? 43.623  -23.698 23.652  1.00 32.17 ? 347  GLU B O   1 
ATOM   4885 C  CB  . GLU B 2 347 ? 46.447  -23.534 23.061  1.00 36.87 ? 347  GLU B CB  1 
ATOM   4886 C  CG  . GLU B 2 347 ? 47.310  -24.651 23.621  1.00 44.60 ? 347  GLU B CG  1 
ATOM   4887 C  CD  . GLU B 2 347 ? 48.459  -24.120 24.459  1.00 49.74 ? 347  GLU B CD  1 
ATOM   4888 O  OE1 . GLU B 2 347 ? 48.337  -24.103 25.705  1.00 53.23 ? 347  GLU B OE1 1 
ATOM   4889 O  OE2 . GLU B 2 347 ? 49.476  -23.704 23.867  1.00 54.90 ? 347  GLU B OE2 1 
ATOM   4890 N  N   . LEU B 2 348 ? 43.487  -25.484 22.292  1.00 29.20 ? 348  LEU B N   1 
ATOM   4891 C  CA  . LEU B 2 348 ? 42.225  -25.957 22.856  1.00 29.32 ? 348  LEU B CA  1 
ATOM   4892 C  C   . LEU B 2 348 ? 42.366  -26.183 24.354  1.00 32.34 ? 348  LEU B C   1 
ATOM   4893 O  O   . LEU B 2 348 ? 43.134  -27.043 24.791  1.00 36.22 ? 348  LEU B O   1 
ATOM   4894 C  CB  . LEU B 2 348 ? 41.805  -27.254 22.166  1.00 31.95 ? 348  LEU B CB  1 
ATOM   4895 C  CG  . LEU B 2 348 ? 40.342  -27.506 21.796  1.00 33.75 ? 348  LEU B CG  1 
ATOM   4896 C  CD1 . LEU B 2 348 ? 39.910  -28.861 22.314  1.00 35.03 ? 348  LEU B CD1 1 
ATOM   4897 C  CD2 . LEU B 2 348 ? 39.414  -26.414 22.299  1.00 31.48 ? 348  LEU B CD2 1 
ATOM   4898 N  N   . LYS B 2 349 ? 41.619  -25.420 25.146  1.00 31.48 ? 349  LYS B N   1 
ATOM   4899 C  CA  . LYS B 2 349 ? 41.717  -25.527 26.595  1.00 30.16 ? 349  LYS B CA  1 
ATOM   4900 C  C   . LYS B 2 349 ? 40.422  -25.986 27.265  1.00 37.14 ? 349  LYS B C   1 
ATOM   4901 O  O   . LYS B 2 349 ? 40.321  -25.910 28.497  1.00 32.37 ? 349  LYS B O   1 
ATOM   4902 C  CB  . LYS B 2 349 ? 42.193  -24.190 27.173  1.00 37.58 ? 349  LYS B CB  1 
ATOM   4903 C  CG  . LYS B 2 349 ? 43.659  -23.874 26.798  1.00 37.07 ? 349  LYS B CG  1 
ATOM   4904 C  CD  . LYS B 2 349 ? 43.991  -22.394 26.933  1.00 41.79 ? 349  LYS B CD  1 
ATOM   4905 C  CE  . LYS B 2 349 ? 43.065  -21.517 26.078  1.00 44.64 ? 349  LYS B CE  1 
ATOM   4906 N  NZ  . LYS B 2 349 ? 43.364  -21.536 24.613  1.00 36.61 ? 349  LYS B NZ  1 
ATOM   4907 N  N   . VAL B 2 350 ? 39.446  -26.489 26.506  1.00 26.20 ? 350  VAL B N   1 
ATOM   4908 C  CA  . VAL B 2 350 ? 38.215  -27.029 27.092  1.00 24.31 ? 350  VAL B CA  1 
ATOM   4909 C  C   . VAL B 2 350 ? 38.020  -28.468 26.622  1.00 22.73 ? 350  VAL B C   1 
ATOM   4910 O  O   . VAL B 2 350 ? 38.467  -28.823 25.518  1.00 23.97 ? 350  VAL B O   1 
ATOM   4911 C  CB  . VAL B 2 350 ? 36.985  -26.166 26.742  1.00 20.89 ? 350  VAL B CB  1 
ATOM   4912 C  CG1 . VAL B 2 350 ? 37.128  -24.750 27.312  1.00 23.83 ? 350  VAL B CG1 1 
ATOM   4913 C  CG2 . VAL B 2 350 ? 36.735  -26.140 25.225  1.00 24.46 ? 350  VAL B CG2 1 
ATOM   4914 N  N   . PRO B 2 351 ? 37.395  -29.333 27.423  1.00 19.75 ? 351  PRO B N   1 
ATOM   4915 C  CA  . PRO B 2 351 ? 37.100  -30.687 26.944  1.00 20.51 ? 351  PRO B CA  1 
ATOM   4916 C  C   . PRO B 2 351 ? 36.258  -30.641 25.676  1.00 22.58 ? 351  PRO B C   1 
ATOM   4917 O  O   . PRO B 2 351 ? 35.399  -29.769 25.511  1.00 20.73 ? 351  PRO B O   1 
ATOM   4918 C  CB  . PRO B 2 351 ? 36.336  -31.317 28.112  1.00 18.02 ? 351  PRO B CB  1 
ATOM   4919 C  CG  . PRO B 2 351 ? 36.855  -30.605 29.313  1.00 20.13 ? 351  PRO B CG  1 
ATOM   4920 C  CD  . PRO B 2 351 ? 37.095  -29.183 28.859  1.00 22.99 ? 351  PRO B CD  1 
ATOM   4921 N  N   . LEU B 2 352 ? 36.530  -31.580 24.767  1.00 20.55 ? 352  LEU B N   1 
ATOM   4922 C  CA  . LEU B 2 352 ? 35.823  -31.682 23.487  1.00 19.24 ? 352  LEU B CA  1 
ATOM   4923 C  C   . LEU B 2 352 ? 35.289  -33.110 23.347  1.00 18.93 ? 352  LEU B C   1 
ATOM   4924 O  O   . LEU B 2 352 ? 36.037  -34.038 23.030  1.00 20.44 ? 352  LEU B O   1 
ATOM   4925 C  CB  . LEU B 2 352 ? 36.740  -31.304 22.323  1.00 22.10 ? 352  LEU B CB  1 
ATOM   4926 C  CG  . LEU B 2 352 ? 36.280  -31.510 20.872  1.00 19.34 ? 352  LEU B CG  1 
ATOM   4927 C  CD1 . LEU B 2 352 ? 35.029  -30.677 20.544  1.00 17.15 ? 352  LEU B CD1 1 
ATOM   4928 C  CD2 . LEU B 2 352 ? 37.412  -31.169 19.912  1.00 18.25 ? 352  LEU B CD2 1 
ATOM   4929 N  N   . VAL B 2 353 ? 33.998  -33.292 23.606  1.00 13.64 ? 353  VAL B N   1 
ATOM   4930 C  CA  . VAL B 2 353 ? 33.345  -34.594 23.481  1.00 15.61 ? 353  VAL B CA  1 
ATOM   4931 C  C   . VAL B 2 353 ? 32.737  -34.676 22.094  1.00 15.79 ? 353  VAL B C   1 
ATOM   4932 O  O   . VAL B 2 353 ? 32.040  -33.749 21.661  1.00 15.26 ? 353  VAL B O   1 
ATOM   4933 C  CB  . VAL B 2 353 ? 32.266  -34.773 24.557  1.00 20.57 ? 353  VAL B CB  1 
ATOM   4934 C  CG1 . VAL B 2 353 ? 31.643  -36.167 24.467  1.00 18.12 ? 353  VAL B CG1 1 
ATOM   4935 C  CG2 . VAL B 2 353 ? 32.847  -34.498 25.937  1.00 17.64 ? 353  VAL B CG2 1 
ATOM   4936 N  N   . VAL B 2 354 ? 33.002  -35.767 21.385  1.00 13.80 ? 354  VAL B N   1 
ATOM   4937 C  CA  . VAL B 2 354 ? 32.648  -35.852 19.974  1.00 19.95 ? 354  VAL B CA  1 
ATOM   4938 C  C   . VAL B 2 354 ? 31.940  -37.166 19.718  1.00 21.73 ? 354  VAL B C   1 
ATOM   4939 O  O   . VAL B 2 354 ? 32.468  -38.237 20.042  1.00 22.88 ? 354  VAL B O   1 
ATOM   4940 C  CB  . VAL B 2 354 ? 33.875  -35.721 19.055  1.00 19.51 ? 354  VAL B CB  1 
ATOM   4941 C  CG1 . VAL B 2 354 ? 33.459  -35.930 17.612  1.00 22.35 ? 354  VAL B CG1 1 
ATOM   4942 C  CG2 . VAL B 2 354 ? 34.521  -34.334 19.233  1.00 22.65 ? 354  VAL B CG2 1 
ATOM   4943 N  N   . ARG B 2 355 ? 30.750  -37.077 19.130  1.00 19.00 ? 355  ARG B N   1 
ATOM   4944 C  CA  . ARG B 2 355 ? 29.975  -38.242 18.721  1.00 20.88 ? 355  ARG B CA  1 
ATOM   4945 C  C   . ARG B 2 355 ? 29.596  -38.034 17.266  1.00 20.32 ? 355  ARG B C   1 
ATOM   4946 O  O   . ARG B 2 355 ? 28.968  -37.029 16.931  1.00 19.75 ? 355  ARG B O   1 
ATOM   4947 C  CB  . ARG B 2 355 ? 28.731  -38.415 19.605  1.00 26.20 ? 355  ARG B CB  1 
ATOM   4948 C  CG  . ARG B 2 355 ? 27.975  -39.756 19.478  1.00 21.54 ? 355  ARG B CG  1 
ATOM   4949 C  CD  . ARG B 2 355 ? 27.094  -39.793 18.249  1.00 26.56 ? 355  ARG B CD  1 
ATOM   4950 N  NE  . ARG B 2 355 ? 26.098  -40.869 18.267  1.00 28.59 ? 355  ARG B NE  1 
ATOM   4951 C  CZ  . ARG B 2 355 ? 24.780  -40.678 18.329  1.00 24.04 ? 355  ARG B CZ  1 
ATOM   4952 N  NH1 . ARG B 2 355 ? 24.275  -39.453 18.391  1.00 21.56 ? 355  ARG B NH1 1 
ATOM   4953 N  NH2 . ARG B 2 355 ? 23.957  -41.723 18.315  1.00 27.17 ? 355  ARG B NH2 1 
ATOM   4954 N  N   . LEU B 2 356 ? 29.984  -38.973 16.406  1.00 19.49 ? 356  LEU B N   1 
ATOM   4955 C  CA  . LEU B 2 356 ? 29.729  -38.875 14.978  1.00 22.82 ? 356  LEU B CA  1 
ATOM   4956 C  C   . LEU B 2 356 ? 29.038  -40.139 14.503  1.00 20.92 ? 356  LEU B C   1 
ATOM   4957 O  O   . LEU B 2 356 ? 29.462  -41.246 14.846  1.00 19.83 ? 356  LEU B O   1 
ATOM   4958 C  CB  . LEU B 2 356 ? 31.032  -38.687 14.179  1.00 22.83 ? 356  LEU B CB  1 
ATOM   4959 C  CG  . LEU B 2 356 ? 31.934  -37.507 14.531  1.00 26.10 ? 356  LEU B CG  1 
ATOM   4960 C  CD1 . LEU B 2 356 ? 33.103  -37.482 13.552  1.00 29.24 ? 356  LEU B CD1 1 
ATOM   4961 C  CD2 . LEU B 2 356 ? 31.164  -36.209 14.438  1.00 21.87 ? 356  LEU B CD2 1 
ATOM   4962 N  N   . GLU B 2 357 ? 27.997  -39.969 13.686  1.00 21.06 ? 357  GLU B N   1 
ATOM   4963 C  CA  . GLU B 2 357 ? 27.314  -41.085 13.050  1.00 21.38 ? 357  GLU B CA  1 
ATOM   4964 C  C   . GLU B 2 357 ? 26.872  -40.668 11.656  1.00 19.11 ? 357  GLU B C   1 
ATOM   4965 O  O   . GLU B 2 357 ? 26.813  -39.482 11.333  1.00 16.46 ? 357  GLU B O   1 
ATOM   4966 C  CB  . GLU B 2 357 ? 26.087  -41.552 13.853  1.00 19.29 ? 357  GLU B CB  1 
ATOM   4967 C  CG  . GLU B 2 357 ? 26.373  -41.986 15.267  1.00 24.72 ? 357  GLU B CG  1 
ATOM   4968 C  CD  . GLU B 2 357 ? 26.915  -43.401 15.375  1.00 31.20 ? 357  GLU B CD  1 
ATOM   4969 O  OE1 . GLU B 2 357 ? 27.038  -44.085 14.333  1.00 27.17 ? 357  GLU B OE1 1 
ATOM   4970 O  OE2 . GLU B 2 357 ? 27.216  -43.819 16.518  1.00 30.36 ? 357  GLU B OE2 1 
ATOM   4971 N  N   . GLY B 2 358 ? 26.558  -41.667 10.829  1.00 18.24 ? 358  GLY B N   1 
ATOM   4972 C  CA  . GLY B 2 358 ? 25.950  -41.411 9.536   1.00 18.91 ? 358  GLY B CA  1 
ATOM   4973 C  C   . GLY B 2 358 ? 26.910  -41.304 8.364   1.00 22.22 ? 358  GLY B C   1 
ATOM   4974 O  O   . GLY B 2 358 ? 27.962  -41.948 8.338   1.00 19.97 ? 358  GLY B O   1 
ATOM   4975 N  N   . THR B 2 359 ? 26.547  -40.462 7.400   1.00 21.98 ? 359  THR B N   1 
ATOM   4976 C  CA  . THR B 2 359 ? 27.233  -40.369 6.113   1.00 22.89 ? 359  THR B CA  1 
ATOM   4977 C  C   . THR B 2 359 ? 28.732  -40.088 6.276   1.00 22.28 ? 359  THR B C   1 
ATOM   4978 O  O   . THR B 2 359 ? 29.130  -39.103 6.908   1.00 21.07 ? 359  THR B O   1 
ATOM   4979 C  CB  . THR B 2 359 ? 26.561  -39.271 5.279   1.00 24.61 ? 359  THR B CB  1 
ATOM   4980 O  OG1 . THR B 2 359 ? 25.174  -39.596 5.081   1.00 21.91 ? 359  THR B OG1 1 
ATOM   4981 C  CG2 . THR B 2 359 ? 27.257  -39.083 3.926   1.00 24.17 ? 359  THR B CG2 1 
ATOM   4982 N  N   . ASN B 2 360 ? 29.555  -40.976 5.706   1.00 17.47 ? 360  ASN B N   1 
ATOM   4983 C  CA  . ASN B 2 360 ? 31.011  -40.808 5.630   1.00 24.68 ? 360  ASN B CA  1 
ATOM   4984 C  C   . ASN B 2 360 ? 31.657  -40.718 7.018   1.00 23.84 ? 360  ASN B C   1 
ATOM   4985 O  O   . ASN B 2 360 ? 32.688  -40.064 7.199   1.00 24.02 ? 360  ASN B O   1 
ATOM   4986 C  CB  . ASN B 2 360 ? 31.370  -39.581 4.771   1.00 24.83 ? 360  ASN B CB  1 
ATOM   4987 C  CG  . ASN B 2 360 ? 32.763  -39.687 4.122   1.00 31.89 ? 360  ASN B CG  1 
ATOM   4988 O  OD1 . ASN B 2 360 ? 33.252  -40.789 3.840   1.00 27.84 ? 360  ASN B OD1 1 
ATOM   4989 N  ND2 . ASN B 2 360 ? 33.400  -38.532 3.876   1.00 23.80 ? 360  ASN B ND2 1 
ATOM   4990 N  N   . VAL B 2 361 ? 31.083  -41.398 8.012   1.00 23.86 ? 361  VAL B N   1 
ATOM   4991 C  CA  . VAL B 2 361 ? 31.599  -41.280 9.374   1.00 22.50 ? 361  VAL B CA  1 
ATOM   4992 C  C   . VAL B 2 361 ? 33.029  -41.818 9.469   1.00 19.00 ? 361  VAL B C   1 
ATOM   4993 O  O   . VAL B 2 361 ? 33.865  -41.267 10.193  1.00 16.92 ? 361  VAL B O   1 
ATOM   4994 C  CB  . VAL B 2 361 ? 30.653  -41.980 10.372  1.00 21.37 ? 361  VAL B CB  1 
ATOM   4995 C  CG1 . VAL B 2 361 ? 30.535  -43.462 10.061  1.00 20.92 ? 361  VAL B CG1 1 
ATOM   4996 C  CG2 . VAL B 2 361 ? 31.138  -41.776 11.798  1.00 24.69 ? 361  VAL B CG2 1 
ATOM   4997 N  N   . GLN B 2 362 ? 33.342  -42.883 8.729   1.00 21.21 ? 362  GLN B N   1 
ATOM   4998 C  CA  . GLN B 2 362 ? 34.680  -43.472 8.823   1.00 20.69 ? 362  GLN B CA  1 
ATOM   4999 C  C   . GLN B 2 362 ? 35.762  -42.471 8.425   1.00 22.94 ? 362  GLN B C   1 
ATOM   5000 O  O   . GLN B 2 362 ? 36.776  -42.330 9.118   1.00 24.73 ? 362  GLN B O   1 
ATOM   5001 C  CB  . GLN B 2 362 ? 34.777  -44.730 7.958   1.00 22.23 ? 362  GLN B CB  1 
ATOM   5002 C  CG  . GLN B 2 362 ? 36.195  -45.276 7.864   1.00 27.66 ? 362  GLN B CG  1 
ATOM   5003 N  N   . GLU B 2 363 ? 35.557  -41.754 7.319   1.00 21.18 ? 363  GLU B N   1 
ATOM   5004 C  CA  . GLU B 2 363 ? 36.549  -40.773 6.887   1.00 24.30 ? 363  GLU B CA  1 
ATOM   5005 C  C   . GLU B 2 363 ? 36.659  -39.623 7.884   1.00 21.62 ? 363  GLU B C   1 
ATOM   5006 O  O   . GLU B 2 363 ? 37.766  -39.178 8.212   1.00 21.99 ? 363  GLU B O   1 
ATOM   5007 C  CB  . GLU B 2 363 ? 36.184  -40.249 5.498   1.00 21.97 ? 363  GLU B CB  1 
ATOM   5008 C  CG  . GLU B 2 363 ? 37.173  -39.248 4.948   1.00 32.37 ? 363  GLU B CG  1 
ATOM   5009 C  CD  . GLU B 2 363 ? 36.694  -38.602 3.655   1.00 34.70 ? 363  GLU B CD  1 
ATOM   5010 O  OE1 . GLU B 2 363 ? 37.342  -37.631 3.209   1.00 49.02 ? 363  GLU B OE1 1 
ATOM   5011 O  OE2 . GLU B 2 363 ? 35.677  -39.060 3.092   1.00 35.63 ? 363  GLU B OE2 1 
ATOM   5012 N  N   . ALA B 2 364 ? 35.518  -39.134 8.373   1.00 20.18 ? 364  ALA B N   1 
ATOM   5013 C  CA  . ALA B 2 364 ? 35.519  -38.070 9.372   1.00 19.81 ? 364  ALA B CA  1 
ATOM   5014 C  C   . ALA B 2 364 ? 36.296  -38.476 10.613  1.00 17.77 ? 364  ALA B C   1 
ATOM   5015 O  O   . ALA B 2 364 ? 37.073  -37.681 11.151  1.00 19.82 ? 364  ALA B O   1 
ATOM   5016 C  CB  . ALA B 2 364 ? 34.084  -37.710 9.756   1.00 18.70 ? 364  ALA B CB  1 
ATOM   5017 N  N   . GLN B 2 365 ? 36.085  -39.708 11.092  1.00 17.69 ? 365  GLN B N   1 
ATOM   5018 C  CA  . GLN B 2 365 ? 36.816  -40.183 12.260  1.00 23.99 ? 365  GLN B CA  1 
ATOM   5019 C  C   . GLN B 2 365 ? 38.322  -40.163 12.021  1.00 20.54 ? 365  GLN B C   1 
ATOM   5020 O  O   . GLN B 2 365 ? 39.092  -39.813 12.919  1.00 22.96 ? 365  GLN B O   1 
ATOM   5021 C  CB  . GLN B 2 365 ? 36.381  -41.600 12.620  1.00 26.43 ? 365  GLN B CB  1 
ATOM   5022 C  CG  . GLN B 2 365 ? 36.640  -41.919 14.058  1.00 29.35 ? 365  GLN B CG  1 
ATOM   5023 C  CD  . GLN B 2 365 ? 35.688  -41.153 14.944  1.00 37.87 ? 365  GLN B CD  1 
ATOM   5024 O  OE1 . GLN B 2 365 ? 34.471  -41.356 14.876  1.00 44.89 ? 365  GLN B OE1 1 
ATOM   5025 N  NE2 . GLN B 2 365 ? 36.224  -40.237 15.751  1.00 38.89 ? 365  GLN B NE2 1 
ATOM   5026 N  N   . LYS B 2 366 ? 38.760  -40.562 10.826  1.00 21.94 ? 366  LYS B N   1 
ATOM   5027 C  CA  . LYS B 2 366 ? 40.191  -40.558 10.526  1.00 22.13 ? 366  LYS B CA  1 
ATOM   5028 C  C   . LYS B 2 366 ? 40.738  -39.140 10.538  1.00 24.16 ? 366  LYS B C   1 
ATOM   5029 O  O   . LYS B 2 366 ? 41.839  -38.894 11.043  1.00 24.77 ? 366  LYS B O   1 
ATOM   5030 C  CB  . LYS B 2 366 ? 40.451  -41.228 9.174   1.00 20.62 ? 366  LYS B CB  1 
ATOM   5031 C  CG  . LYS B 2 366 ? 40.032  -42.690 9.121   1.00 23.19 ? 366  LYS B CG  1 
ATOM   5032 C  CD  . LYS B 2 366 ? 40.314  -43.314 7.753   1.00 29.90 ? 366  LYS B CD  1 
ATOM   5033 N  N   . ILE B 2 367 ? 39.964  -38.189 10.005  1.00 21.19 ? 367  ILE B N   1 
ATOM   5034 C  CA  . ILE B 2 367 ? 40.362  -36.789 10.034  1.00 21.41 ? 367  ILE B CA  1 
ATOM   5035 C  C   . ILE B 2 367 ? 40.552  -36.313 11.470  1.00 25.30 ? 367  ILE B C   1 
ATOM   5036 O  O   . ILE B 2 367 ? 41.545  -35.647 11.791  1.00 25.29 ? 367  ILE B O   1 
ATOM   5037 C  CB  . ILE B 2 367 ? 39.331  -35.935 9.277   1.00 21.66 ? 367  ILE B CB  1 
ATOM   5038 C  CG1 . ILE B 2 367 ? 39.323  -36.319 7.793   1.00 21.12 ? 367  ILE B CG1 1 
ATOM   5039 C  CG2 . ILE B 2 367 ? 39.623  -34.457 9.493   1.00 17.90 ? 367  ILE B CG2 1 
ATOM   5040 C  CD1 . ILE B 2 367 ? 38.124  -35.779 6.996   1.00 17.88 ? 367  ILE B CD1 1 
ATOM   5041 N  N   . LEU B 2 368 ? 39.611  -36.643 12.360  1.00 20.90 ? 368  LEU B N   1 
ATOM   5042 C  CA  . LEU B 2 368 ? 39.785  -36.267 13.764  1.00 18.09 ? 368  LEU B CA  1 
ATOM   5043 C  C   . LEU B 2 368 ? 40.994  -36.963 14.383  1.00 24.14 ? 368  LEU B C   1 
ATOM   5044 O  O   . LEU B 2 368 ? 41.735  -36.354 15.169  1.00 22.62 ? 368  LEU B O   1 
ATOM   5045 C  CB  . LEU B 2 368 ? 38.523  -36.592 14.561  1.00 18.40 ? 368  LEU B CB  1 
ATOM   5046 C  CG  . LEU B 2 368 ? 37.299  -35.837 14.051  1.00 22.30 ? 368  LEU B CG  1 
ATOM   5047 C  CD1 . LEU B 2 368 ? 36.089  -36.180 14.880  1.00 20.95 ? 368  LEU B CD1 1 
ATOM   5048 C  CD2 . LEU B 2 368 ? 37.580  -34.348 14.068  1.00 20.22 ? 368  LEU B CD2 1 
ATOM   5049 N  N   . ASN B 2 369 ? 41.213  -38.233 14.042  1.00 25.34 ? 369  ASN B N   1 
ATOM   5050 C  CA  . ASN B 2 369 ? 42.378  -38.954 14.557  1.00 28.23 ? 369  ASN B CA  1 
ATOM   5051 C  C   . ASN B 2 369 ? 43.688  -38.297 14.124  1.00 26.85 ? 369  ASN B C   1 
ATOM   5052 O  O   . ASN B 2 369 ? 44.593  -38.091 14.939  1.00 30.12 ? 369  ASN B O   1 
ATOM   5053 C  CB  . ASN B 2 369 ? 42.333  -40.404 14.088  1.00 28.33 ? 369  ASN B CB  1 
ATOM   5054 C  CG  . ASN B 2 369 ? 41.254  -41.185 14.771  1.00 26.13 ? 369  ASN B CG  1 
ATOM   5055 O  OD1 . ASN B 2 369 ? 40.769  -40.782 15.821  1.00 28.53 ? 369  ASN B OD1 1 
ATOM   5056 N  ND2 . ASN B 2 369 ? 40.870  -42.307 14.190  1.00 26.37 ? 369  ASN B ND2 1 
ATOM   5057 N  N   . ASN B 2 370 ? 43.814  -37.975 12.837  1.00 28.99 ? 370  ASN B N   1 
ATOM   5058 C  CA  . ASN B 2 370 ? 45.039  -37.358 12.343  1.00 30.80 ? 370  ASN B CA  1 
ATOM   5059 C  C   . ASN B 2 370 ? 45.321  -36.006 12.978  1.00 30.55 ? 370  ASN B C   1 
ATOM   5060 O  O   . ASN B 2 370 ? 46.474  -35.565 12.980  1.00 30.61 ? 370  ASN B O   1 
ATOM   5061 C  CB  . ASN B 2 370 ? 44.968  -37.197 10.831  1.00 32.49 ? 370  ASN B CB  1 
ATOM   5062 C  CG  . ASN B 2 370 ? 44.932  -38.516 10.121  1.00 31.43 ? 370  ASN B CG  1 
ATOM   5063 O  OD1 . ASN B 2 370 ? 45.244  -39.552 10.712  1.00 28.38 ? 370  ASN B OD1 1 
ATOM   5064 N  ND2 . ASN B 2 370 ? 44.552  -38.496 8.843   1.00 32.25 ? 370  ASN B ND2 1 
ATOM   5065 N  N   . SER B 2 371 ? 44.304  -35.330 13.511  1.00 26.71 ? 371  SER B N   1 
ATOM   5066 C  CA  . SER B 2 371 ? 44.523  -33.976 14.005  1.00 20.20 ? 371  SER B CA  1 
ATOM   5067 C  C   . SER B 2 371 ? 45.371  -33.961 15.269  1.00 24.41 ? 371  SER B C   1 
ATOM   5068 O  O   . SER B 2 371 ? 46.015  -32.952 15.568  1.00 24.18 ? 371  SER B O   1 
ATOM   5069 C  CB  . SER B 2 371 ? 43.181  -33.288 14.272  1.00 21.96 ? 371  SER B CB  1 
ATOM   5070 O  OG  . SER B 2 371 ? 42.572  -33.832 15.430  1.00 23.91 ? 371  SER B OG  1 
ATOM   5071 N  N   . GLY B 2 372 ? 45.369  -35.047 16.038  1.00 28.23 ? 372  GLY B N   1 
ATOM   5072 C  CA  . GLY B 2 372 ? 46.009  -34.991 17.330  1.00 21.86 ? 372  GLY B CA  1 
ATOM   5073 C  C   . GLY B 2 372 ? 45.288  -34.119 18.334  1.00 24.33 ? 372  GLY B C   1 
ATOM   5074 O  O   . GLY B 2 372 ? 45.886  -33.719 19.336  1.00 27.06 ? 372  GLY B O   1 
ATOM   5075 N  N   . LEU B 2 373 ? 44.014  -33.814 18.092  1.00 20.53 ? 373  LEU B N   1 
ATOM   5076 C  CA  . LEU B 2 373 ? 43.235  -33.032 19.036  1.00 21.84 ? 373  LEU B CA  1 
ATOM   5077 C  C   . LEU B 2 373 ? 42.894  -33.861 20.271  1.00 20.65 ? 373  LEU B C   1 
ATOM   5078 O  O   . LEU B 2 373 ? 42.646  -35.064 20.173  1.00 21.41 ? 373  LEU B O   1 
ATOM   5079 C  CB  . LEU B 2 373 ? 41.942  -32.540 18.392  1.00 21.58 ? 373  LEU B CB  1 
ATOM   5080 C  CG  . LEU B 2 373 ? 42.066  -31.437 17.352  1.00 25.57 ? 373  LEU B CG  1 
ATOM   5081 C  CD1 . LEU B 2 373 ? 40.700  -31.166 16.707  1.00 23.49 ? 373  LEU B CD1 1 
ATOM   5082 C  CD2 . LEU B 2 373 ? 42.626  -30.189 18.003  1.00 21.53 ? 373  LEU B CD2 1 
ATOM   5083 N  N   . PRO B 2 374 ? 42.858  -33.235 21.449  1.00 20.01 ? 374  PRO B N   1 
ATOM   5084 C  CA  . PRO B 2 374 ? 42.416  -33.954 22.654  1.00 22.05 ? 374  PRO B CA  1 
ATOM   5085 C  C   . PRO B 2 374 ? 40.900  -34.162 22.674  1.00 25.16 ? 374  PRO B C   1 
ATOM   5086 O  O   . PRO B 2 374 ? 40.142  -33.374 23.258  1.00 28.95 ? 374  PRO B O   1 
ATOM   5087 C  CB  . PRO B 2 374 ? 42.887  -33.048 23.798  1.00 20.81 ? 374  PRO B CB  1 
ATOM   5088 C  CG  . PRO B 2 374 ? 42.964  -31.684 23.188  1.00 29.60 ? 374  PRO B CG  1 
ATOM   5089 C  CD  . PRO B 2 374 ? 43.380  -31.893 21.755  1.00 27.95 ? 374  PRO B CD  1 
ATOM   5090 N  N   . ILE B 2 375 ? 40.455  -35.232 22.027  1.00 27.38 ? 375  ILE B N   1 
ATOM   5091 C  CA  . ILE B 2 375 ? 39.038  -35.556 21.868  1.00 27.34 ? 375  ILE B CA  1 
ATOM   5092 C  C   . ILE B 2 375 ? 38.708  -36.763 22.739  1.00 26.48 ? 375  ILE B C   1 
ATOM   5093 O  O   . ILE B 2 375 ? 39.407  -37.781 22.679  1.00 25.56 ? 375  ILE B O   1 
ATOM   5094 C  CB  . ILE B 2 375 ? 38.713  -35.855 20.391  1.00 26.58 ? 375  ILE B CB  1 
ATOM   5095 C  CG1 . ILE B 2 375 ? 38.896  -34.592 19.528  1.00 22.49 ? 375  ILE B CG1 1 
ATOM   5096 C  CG2 . ILE B 2 375 ? 37.314  -36.492 20.260  1.00 21.17 ? 375  ILE B CG2 1 
ATOM   5097 C  CD1 . ILE B 2 375 ? 38.928  -34.868 18.026  1.00 25.54 ? 375  ILE B CD1 1 
ATOM   5098 N  N   . THR B 2 376 ? 37.638  -36.671 23.531  1.00 22.26 ? 376  THR B N   1 
ATOM   5099 C  CA  . THR B 2 376 ? 37.099  -37.853 24.200  1.00 20.84 ? 376  THR B CA  1 
ATOM   5100 C  C   . THR B 2 376 ? 35.865  -38.318 23.433  1.00 23.42 ? 376  THR B C   1 
ATOM   5101 O  O   . THR B 2 376 ? 34.901  -37.562 23.258  1.00 20.34 ? 376  THR B O   1 
ATOM   5102 C  CB  . THR B 2 376 ? 36.810  -37.607 25.690  1.00 28.89 ? 376  THR B CB  1 
ATOM   5103 O  OG1 . THR B 2 376 ? 35.539  -38.152 26.079  1.00 30.68 ? 376  THR B OG1 1 
ATOM   5104 C  CG2 . THR B 2 376 ? 36.859  -36.185 26.024  1.00 19.70 ? 376  THR B CG2 1 
ATOM   5105 N  N   . SER B 2 377 ? 35.935  -39.543 22.926  1.00 23.07 ? 377  SER B N   1 
ATOM   5106 C  CA  . SER B 2 377 ? 34.904  -40.160 22.115  1.00 22.61 ? 377  SER B CA  1 
ATOM   5107 C  C   . SER B 2 377 ? 33.727  -40.620 22.970  1.00 25.80 ? 377  SER B C   1 
ATOM   5108 O  O   . SER B 2 377 ? 33.852  -40.884 24.165  1.00 29.87 ? 377  SER B O   1 
ATOM   5109 C  CB  . SER B 2 377 ? 35.479  -41.353 21.358  1.00 24.25 ? 377  SER B CB  1 
ATOM   5110 O  OG  . SER B 2 377 ? 36.543  -40.930 20.539  1.00 35.85 ? 377  SER B OG  1 
ATOM   5111 N  N   . ALA B 2 378 ? 32.575  -40.735 22.324  1.00 27.97 ? 378  ALA B N   1 
ATOM   5112 C  CA  . ALA B 2 378 ? 31.351  -41.191 22.962  1.00 28.31 ? 378  ALA B CA  1 
ATOM   5113 C  C   . ALA B 2 378 ? 30.675  -42.224 22.069  1.00 23.32 ? 378  ALA B C   1 
ATOM   5114 O  O   . ALA B 2 378 ? 30.686  -42.086 20.845  1.00 26.26 ? 378  ALA B O   1 
ATOM   5115 C  CB  . ALA B 2 378 ? 30.411  -40.019 23.217  1.00 25.69 ? 378  ALA B CB  1 
ATOM   5116 N  N   . ILE B 2 379 ? 30.077  -43.249 22.683  1.00 25.82 ? 379  ILE B N   1 
ATOM   5117 C  CA  . ILE B 2 379 ? 29.447  -44.304 21.892  1.00 29.65 ? 379  ILE B CA  1 
ATOM   5118 C  C   . ILE B 2 379 ? 28.027  -43.925 21.459  1.00 31.76 ? 379  ILE B C   1 
ATOM   5119 O  O   . ILE B 2 379 ? 27.552  -44.379 20.411  1.00 26.61 ? 379  ILE B O   1 
ATOM   5120 C  CB  . ILE B 2 379 ? 29.454  -45.629 22.671  1.00 31.03 ? 379  ILE B CB  1 
ATOM   5121 C  CG1 . ILE B 2 379 ? 28.617  -45.517 23.944  1.00 33.77 ? 379  ILE B CG1 1 
ATOM   5122 C  CG2 . ILE B 2 379 ? 30.891  -46.045 23.006  1.00 35.45 ? 379  ILE B CG2 1 
ATOM   5123 C  CD1 . ILE B 2 379 ? 28.509  -46.825 24.716  1.00 35.78 ? 379  ILE B CD1 1 
ATOM   5124 N  N   . ASP B 2 380 ? 27.326  -43.106 22.238  1.00 27.76 ? 380  ASP B N   1 
ATOM   5125 C  CA  . ASP B 2 380 ? 25.969  -42.712 21.887  1.00 29.74 ? 380  ASP B CA  1 
ATOM   5126 C  C   . ASP B 2 380 ? 25.689  -41.352 22.504  1.00 22.59 ? 380  ASP B C   1 
ATOM   5127 O  O   . ASP B 2 380 ? 26.528  -40.775 23.195  1.00 21.31 ? 380  ASP B O   1 
ATOM   5128 C  CB  . ASP B 2 380 ? 24.932  -43.750 22.344  1.00 28.39 ? 380  ASP B CB  1 
ATOM   5129 C  CG  . ASP B 2 380 ? 24.989  -44.032 23.847  1.00 31.06 ? 380  ASP B CG  1 
ATOM   5130 O  OD1 . ASP B 2 380 ? 24.856  -43.099 24.668  1.00 24.53 ? 380  ASP B OD1 1 
ATOM   5131 O  OD2 . ASP B 2 380 ? 25.148  -45.217 24.209  1.00 37.87 ? 380  ASP B OD2 1 
ATOM   5132 N  N   . LEU B 2 381 ? 24.487  -40.841 22.258  1.00 22.72 ? 381  LEU B N   1 
ATOM   5133 C  CA  . LEU B 2 381 ? 24.196  -39.500 22.737  1.00 20.51 ? 381  LEU B CA  1 
ATOM   5134 C  C   . LEU B 2 381 ? 24.095  -39.451 24.257  1.00 18.62 ? 381  LEU B C   1 
ATOM   5135 O  O   . LEU B 2 381 ? 24.459  -38.439 24.857  1.00 17.88 ? 381  LEU B O   1 
ATOM   5136 C  CB  . LEU B 2 381 ? 22.925  -38.974 22.082  1.00 20.74 ? 381  LEU B CB  1 
ATOM   5137 C  CG  . LEU B 2 381 ? 22.466  -37.580 22.470  1.00 19.16 ? 381  LEU B CG  1 
ATOM   5138 C  CD1 . LEU B 2 381 ? 23.581  -36.563 22.249  1.00 17.21 ? 381  LEU B CD1 1 
ATOM   5139 C  CD2 . LEU B 2 381 ? 21.226  -37.245 21.632  1.00 22.51 ? 381  LEU B CD2 1 
ATOM   5140 N  N   . GLU B 2 382 ? 23.614  -40.515 24.901  1.00 19.68 ? 382  GLU B N   1 
ATOM   5141 C  CA  . GLU B 2 382 ? 23.611  -40.505 26.361  1.00 19.55 ? 382  GLU B CA  1 
ATOM   5142 C  C   . GLU B 2 382 ? 25.034  -40.493 26.902  1.00 17.17 ? 382  GLU B C   1 
ATOM   5143 O  O   . GLU B 2 382 ? 25.356  -39.707 27.793  1.00 17.92 ? 382  GLU B O   1 
ATOM   5144 C  CB  . GLU B 2 382 ? 22.846  -41.705 26.916  1.00 17.51 ? 382  GLU B CB  1 
ATOM   5145 C  CG  . GLU B 2 382 ? 22.447  -41.523 28.390  1.00 22.28 ? 382  GLU B CG  1 
ATOM   5146 C  CD  . GLU B 2 382 ? 21.123  -40.770 28.546  1.00 26.77 ? 382  GLU B CD  1 
ATOM   5147 O  OE1 . GLU B 2 382 ? 20.105  -41.186 27.932  1.00 25.40 ? 382  GLU B OE1 1 
ATOM   5148 O  OE2 . GLU B 2 382 ? 21.097  -39.753 29.270  1.00 25.28 ? 382  GLU B OE2 1 
ATOM   5149 N  N   . ASP B 2 383 ? 25.904  -41.322 26.331  1.00 17.03 ? 383  ASP B N   1 
ATOM   5150 C  CA  . ASP B 2 383 ? 27.308  -41.346 26.732  1.00 20.55 ? 383  ASP B CA  1 
ATOM   5151 C  C   . ASP B 2 383 ? 27.967  -39.982 26.520  1.00 21.55 ? 383  ASP B C   1 
ATOM   5152 O  O   . ASP B 2 383 ? 28.683  -39.485 27.398  1.00 19.96 ? 383  ASP B O   1 
ATOM   5153 C  CB  . ASP B 2 383 ? 28.022  -42.454 25.952  1.00 20.56 ? 383  ASP B CB  1 
ATOM   5154 C  CG  . ASP B 2 383 ? 29.449  -42.693 26.427  1.00 25.46 ? 383  ASP B CG  1 
ATOM   5155 O  OD1 . ASP B 2 383 ? 29.681  -42.754 27.658  1.00 21.48 ? 383  ASP B OD1 1 
ATOM   5156 O  OD2 . ASP B 2 383 ? 30.332  -42.828 25.554  1.00 22.44 ? 383  ASP B OD2 1 
ATOM   5157 N  N   . ALA B 2 384 ? 27.689  -39.330 25.390  1.00 20.37 ? 384  ALA B N   1 
ATOM   5158 C  CA  . ALA B 2 384 ? 28.277  -38.012 25.152  1.00 23.47 ? 384  ALA B CA  1 
ATOM   5159 C  C   . ALA B 2 384 ? 27.846  -37.014 26.219  1.00 20.19 ? 384  ALA B C   1 
ATOM   5160 O  O   . ALA B 2 384 ? 28.681  -36.305 26.790  1.00 17.66 ? 384  ALA B O   1 
ATOM   5161 C  CB  . ALA B 2 384 ? 27.904  -37.508 23.762  1.00 20.33 ? 384  ALA B CB  1 
ATOM   5162 N  N   . ALA B 2 385 ? 26.542  -36.956 26.516  1.00 18.51 ? 385  ALA B N   1 
ATOM   5163 C  CA  . ALA B 2 385 ? 26.044  -35.976 27.483  1.00 18.88 ? 385  ALA B CA  1 
ATOM   5164 C  C   . ALA B 2 385 ? 26.620  -36.216 28.870  1.00 16.40 ? 385  ALA B C   1 
ATOM   5165 O  O   . ALA B 2 385 ? 26.969  -35.267 29.572  1.00 17.18 ? 385  ALA B O   1 
ATOM   5166 C  CB  . ALA B 2 385 ? 24.512  -36.012 27.552  1.00 17.94 ? 385  ALA B CB  1 
ATOM   5167 N  N   . LYS B 2 386 ? 26.684  -37.478 29.296  1.00 18.64 ? 386  LYS B N   1 
ATOM   5168 C  CA  . LYS B 2 386 ? 27.237  -37.783 30.609  1.00 21.04 ? 386  LYS B CA  1 
ATOM   5169 C  C   . LYS B 2 386 ? 28.696  -37.356 30.701  1.00 21.89 ? 386  LYS B C   1 
ATOM   5170 O  O   . LYS B 2 386 ? 29.116  -36.789 31.713  1.00 21.40 ? 386  LYS B O   1 
ATOM   5171 C  CB  . LYS B 2 386 ? 27.083  -39.280 30.908  1.00 24.77 ? 386  LYS B CB  1 
ATOM   5172 C  CG  . LYS B 2 386 ? 25.635  -39.681 31.230  1.00 30.95 ? 386  LYS B CG  1 
ATOM   5173 C  CD  . LYS B 2 386 ? 25.465  -41.163 31.564  1.00 31.65 ? 386  LYS B CD  1 
ATOM   5174 C  CE  . LYS B 2 386 ? 24.028  -41.436 32.020  1.00 33.55 ? 386  LYS B CE  1 
ATOM   5175 N  NZ  . LYS B 2 386 ? 23.749  -42.888 32.181  1.00 34.36 ? 386  LYS B NZ  1 
ATOM   5176 N  N   . LYS B 2 387 ? 29.478  -37.596 29.638  1.00 19.49 ? 387  LYS B N   1 
ATOM   5177 C  CA  . LYS B 2 387 ? 30.892  -37.218 29.659  1.00 22.19 ? 387  LYS B CA  1 
ATOM   5178 C  C   . LYS B 2 387 ? 31.070  -35.708 29.602  1.00 22.18 ? 387  LYS B C   1 
ATOM   5179 O  O   . LYS B 2 387 ? 31.945  -35.156 30.284  1.00 22.22 ? 387  LYS B O   1 
ATOM   5180 C  CB  . LYS B 2 387 ? 31.634  -37.896 28.504  1.00 20.65 ? 387  LYS B CB  1 
ATOM   5181 C  CG  . LYS B 2 387 ? 31.731  -39.421 28.668  1.00 23.42 ? 387  LYS B CG  1 
ATOM   5182 C  CD  . LYS B 2 387 ? 32.273  -40.144 27.421  1.00 20.70 ? 387  LYS B CD  1 
ATOM   5183 C  CE  . LYS B 2 387 ? 32.637  -41.585 27.778  1.00 24.10 ? 387  LYS B CE  1 
ATOM   5184 N  NZ  . LYS B 2 387 ? 32.990  -42.424 26.591  1.00 32.71 ? 387  LYS B NZ  1 
ATOM   5185 N  N   . ALA B 2 388 ? 30.235  -35.013 28.820  1.00 18.23 ? 388  ALA B N   1 
ATOM   5186 C  CA  . ALA B 2 388 ? 30.351  -33.561 28.748  1.00 16.14 ? 388  ALA B CA  1 
ATOM   5187 C  C   . ALA B 2 388 ? 30.026  -32.919 30.085  1.00 19.16 ? 388  ALA B C   1 
ATOM   5188 O  O   . ALA B 2 388 ? 30.691  -31.958 30.499  1.00 19.92 ? 388  ALA B O   1 
ATOM   5189 C  CB  . ALA B 2 388 ? 29.440  -33.008 27.648  1.00 19.05 ? 388  ALA B CB  1 
ATOM   5190 N  N   . VAL B 2 389 ? 29.001  -33.434 30.771  1.00 20.72 ? 389  VAL B N   1 
ATOM   5191 C  CA  . VAL B 2 389 ? 28.636  -32.920 32.085  1.00 19.79 ? 389  VAL B CA  1 
ATOM   5192 C  C   . VAL B 2 389 ? 29.753  -33.192 33.085  1.00 20.98 ? 389  VAL B C   1 
ATOM   5193 O  O   . VAL B 2 389 ? 30.175  -32.301 33.831  1.00 25.91 ? 389  VAL B O   1 
ATOM   5194 C  CB  . VAL B 2 389 ? 27.302  -33.540 32.545  1.00 20.20 ? 389  VAL B CB  1 
ATOM   5195 C  CG1 . VAL B 2 389 ? 27.103  -33.335 34.036  1.00 19.47 ? 389  VAL B CG1 1 
ATOM   5196 C  CG2 . VAL B 2 389 ? 26.139  -32.968 31.759  1.00 15.97 ? 389  VAL B CG2 1 
ATOM   5197 N  N   . ALA B 2 390 ? 30.262  -34.423 33.098  1.00 21.10 ? 390  ALA B N   1 
ATOM   5198 C  CA  . ALA B 2 390 ? 31.301  -34.787 34.052  1.00 22.42 ? 390  ALA B CA  1 
ATOM   5199 C  C   . ALA B 2 390 ? 32.572  -33.985 33.803  1.00 29.35 ? 390  ALA B C   1 
ATOM   5200 O  O   . ALA B 2 390 ? 33.236  -33.547 34.751  1.00 26.97 ? 390  ALA B O   1 
ATOM   5201 C  CB  . ALA B 2 390 ? 31.568  -36.293 33.981  1.00 19.84 ? 390  ALA B CB  1 
ATOM   5202 N  N   . SER B 2 391 ? 32.889  -33.722 32.533  1.00 22.79 ? 391  SER B N   1 
ATOM   5203 C  CA  . SER B 2 391 ? 34.096  -32.974 32.193  1.00 23.32 ? 391  SER B CA  1 
ATOM   5204 C  C   . SER B 2 391 ? 34.138  -31.579 32.820  1.00 27.35 ? 391  SER B C   1 
ATOM   5205 O  O   . SER B 2 391 ? 35.230  -31.010 32.948  1.00 29.12 ? 391  SER B O   1 
ATOM   5206 C  CB  . SER B 2 391 ? 34.216  -32.847 30.678  1.00 21.25 ? 391  SER B CB  1 
ATOM   5207 O  OG  . SER B 2 391 ? 33.474  -31.725 30.238  1.00 22.89 ? 391  SER B OG  1 
ATOM   5208 N  N   . VAL B 2 392 ? 32.993  -31.001 33.195  1.00 23.61 ? 392  VAL B N   1 
ATOM   5209 C  CA  . VAL B 2 392 ? 32.962  -29.715 33.883  1.00 24.96 ? 392  VAL B CA  1 
ATOM   5210 C  C   . VAL B 2 392 ? 32.387  -29.825 35.289  1.00 31.22 ? 392  VAL B C   1 
ATOM   5211 O  O   . VAL B 2 392 ? 32.063  -28.805 35.898  1.00 33.64 ? 392  VAL B O   1 
ATOM   5212 C  CB  . VAL B 2 392 ? 32.191  -28.643 33.081  1.00 27.26 ? 392  VAL B CB  1 
ATOM   5213 C  CG1 . VAL B 2 392 ? 32.784  -28.471 31.702  1.00 27.96 ? 392  VAL B CG1 1 
ATOM   5214 C  CG2 . VAL B 2 392 ? 30.708  -28.977 32.998  1.00 27.24 ? 392  VAL B CG2 1 
ATOM   5215 N  N   . ALA B 2 393 ? 32.240  -31.040 35.813  1.00 31.50 ? 393  ALA B N   1 
ATOM   5216 C  CA  . ALA B 2 393 ? 31.793  -31.227 37.192  1.00 38.79 ? 393  ALA B CA  1 
ATOM   5217 C  C   . ALA B 2 393 ? 32.813  -30.635 38.166  1.00 38.03 ? 393  ALA B C   1 
ATOM   5218 O  O   . ALA B 2 393 ? 32.612  -29.546 38.708  1.00 45.31 ? 393  ALA B O   1 
ATOM   5219 C  CB  . ALA B 2 393 ? 31.561  -32.710 37.492  1.00 35.45 ? 393  ALA B CB  1 
HETATM 5220 N  N1A . COA C 3 .   ? 11.179  -28.660 -11.668 1.00 17.66 ? 2001 COA A N1A 1 
HETATM 5221 C  C2A . COA C 3 .   ? 12.287  -29.403 -11.777 1.00 15.43 ? 2001 COA A C2A 1 
HETATM 5222 N  N3A . COA C 3 .   ? 13.559  -29.035 -11.663 1.00 15.10 ? 2001 COA A N3A 1 
HETATM 5223 C  C4A . COA C 3 .   ? 13.646  -27.718 -11.407 1.00 17.39 ? 2001 COA A C4A 1 
HETATM 5224 C  C5A . COA C 3 .   ? 12.607  -26.823 -11.263 1.00 15.85 ? 2001 COA A C5A 1 
HETATM 5225 C  C6A . COA C 3 .   ? 11.302  -27.335 -11.407 1.00 15.10 ? 2001 COA A C6A 1 
HETATM 5226 N  N6A . COA C 3 .   ? 10.193  -26.611 -11.291 1.00 17.45 ? 2001 COA A N6A 1 
HETATM 5227 N  N7A . COA C 3 .   ? 13.103  -25.549 -10.992 1.00 17.95 ? 2001 COA A N7A 1 
HETATM 5228 C  C8A . COA C 3 .   ? 14.409  -25.693 -10.976 1.00 16.65 ? 2001 COA A C8A 1 
HETATM 5229 N  N9A . COA C 3 .   ? 14.795  -27.000 -11.232 1.00 16.53 ? 2001 COA A N9A 1 
HETATM 5230 C  C1B . COA C 3 .   ? 16.144  -27.554 -11.256 1.00 18.25 ? 2001 COA A C1B 1 
HETATM 5231 C  C2B . COA C 3 .   ? 17.255  -26.608 -11.699 1.00 18.31 ? 2001 COA A C2B 1 
HETATM 5232 O  O2B . COA C 3 .   ? 17.310  -26.393 -13.093 1.00 22.03 ? 2001 COA A O2B 1 
HETATM 5233 C  C3B . COA C 3 .   ? 18.489  -27.305 -11.113 1.00 22.41 ? 2001 COA A C3B 1 
HETATM 5234 O  O3B . COA C 3 .   ? 19.021  -28.261 -12.028 1.00 21.90 ? 2001 COA A O3B 1 
HETATM 5235 P  P3B . COA C 3 .   ? 20.172  -27.676 -13.026 1.00 27.67 ? 2001 COA A P3B 1 
HETATM 5236 O  O7A . COA C 3 .   ? 21.338  -27.187 -12.195 1.00 23.75 ? 2001 COA A O7A 1 
HETATM 5237 O  O8A . COA C 3 .   ? 20.550  -28.869 -13.883 1.00 25.61 ? 2001 COA A O8A 1 
HETATM 5238 O  O9A . COA C 3 .   ? 19.548  -26.567 -13.841 1.00 20.96 ? 2001 COA A O9A 1 
HETATM 5239 C  C4B . COA C 3 .   ? 17.935  -28.031 -9.878  1.00 19.71 ? 2001 COA A C4B 1 
HETATM 5240 O  O4B . COA C 3 .   ? 16.496  -27.867 -9.930  1.00 17.98 ? 2001 COA A O4B 1 
HETATM 5241 C  C5B . COA C 3 .   ? 18.449  -27.524 -8.552  1.00 20.27 ? 2001 COA A C5B 1 
HETATM 5242 O  O5B . COA C 3 .   ? 19.861  -27.810 -8.471  1.00 22.26 ? 2001 COA A O5B 1 
HETATM 5243 P  P1A . COA C 3 .   ? 20.899  -26.879 -7.664  1.00 22.84 ? 2001 COA A P1A 1 
HETATM 5244 O  O1A . COA C 3 .   ? 20.686  -25.444 -8.017  1.00 24.45 ? 2001 COA A O1A 1 
HETATM 5245 O  O2A . COA C 3 .   ? 22.248  -27.489 -7.832  1.00 21.60 ? 2001 COA A O2A 1 
HETATM 5246 O  O3A . COA C 3 .   ? 20.417  -27.063 -6.146  1.00 17.38 ? 2001 COA A O3A 1 
HETATM 5247 P  P2A . COA C 3 .   ? 20.949  -28.078 -5.030  1.00 22.76 ? 2001 COA A P2A 1 
HETATM 5248 O  O4A . COA C 3 .   ? 22.325  -27.692 -4.609  1.00 21.12 ? 2001 COA A O4A 1 
HETATM 5249 O  O5A . COA C 3 .   ? 20.736  -29.468 -5.547  1.00 19.05 ? 2001 COA A O5A 1 
HETATM 5250 O  O6A . COA C 3 .   ? 19.946  -27.746 -3.819  1.00 22.00 ? 2001 COA A O6A 1 
HETATM 5251 C  CBP . COA C 3 .   ? 17.906  -28.353 -2.677  1.00 17.15 ? 2001 COA A CBP 1 
HETATM 5252 C  CCP . COA C 3 .   ? 18.514  -27.920 -4.009  1.00 19.93 ? 2001 COA A CCP 1 
HETATM 5253 C  CDP . COA C 3 .   ? 18.442  -29.737 -2.307  1.00 17.76 ? 2001 COA A CDP 1 
HETATM 5254 C  CEP . COA C 3 .   ? 16.384  -28.439 -2.831  1.00 16.64 ? 2001 COA A CEP 1 
HETATM 5255 C  CAP . COA C 3 .   ? 18.290  -27.346 -1.584  1.00 18.41 ? 2001 COA A CAP 1 
HETATM 5256 O  OAP . COA C 3 .   ? 17.748  -26.072 -1.912  1.00 14.89 ? 2001 COA A OAP 1 
HETATM 5257 C  C9P . COA C 3 .   ? 17.841  -27.742 -0.188  1.00 18.98 ? 2001 COA A C9P 1 
HETATM 5258 O  O9P . COA C 3 .   ? 16.676  -27.561 0.144   1.00 18.28 ? 2001 COA A O9P 1 
HETATM 5259 N  N8P . COA C 3 .   ? 18.751  -28.251 0.629   1.00 16.15 ? 2001 COA A N8P 1 
HETATM 5260 C  C7P . COA C 3 .   ? 18.429  -28.690 1.983   1.00 18.96 ? 2001 COA A C7P 1 
HETATM 5261 C  C6P . COA C 3 .   ? 17.514  -29.890 2.000   1.00 13.77 ? 2001 COA A C6P 1 
HETATM 5262 C  C5P . COA C 3 .   ? 17.264  -30.345 3.424   1.00 19.16 ? 2001 COA A C5P 1 
HETATM 5263 O  O5P . COA C 3 .   ? 18.174  -30.344 4.252   1.00 21.22 ? 2001 COA A O5P 1 
HETATM 5264 N  N4P . COA C 3 .   ? 16.023  -30.737 3.728   1.00 16.84 ? 2001 COA A N4P 1 
HETATM 5265 C  C3P . COA C 3 .   ? 15.573  -31.109 5.062   1.00 17.95 ? 2001 COA A C3P 1 
HETATM 5266 C  C2P . COA C 3 .   ? 16.014  -32.493 5.451   1.00 23.26 ? 2001 COA A C2P 1 
HETATM 5267 S  S1P . COA C 3 .   ? 15.179  -33.120 6.934   1.00 27.27 ? 2001 COA A S1P 1 
HETATM 5268 P  P   . PO4 D 4 .   ? 16.014  -31.746 11.238  1.00 20.07 ? 2002 PO4 A P   1 
HETATM 5269 O  O1  . PO4 D 4 .   ? 14.720  -31.923 10.476  1.00 26.05 ? 2002 PO4 A O1  1 
HETATM 5270 O  O2  . PO4 D 4 .   ? 16.537  -30.367 10.944  1.00 15.80 ? 2002 PO4 A O2  1 
HETATM 5271 O  O3  . PO4 D 4 .   ? 16.950  -32.836 10.863  1.00 21.35 ? 2002 PO4 A O3  1 
HETATM 5272 O  O4  . PO4 D 4 .   ? 15.707  -31.820 12.721  1.00 22.80 ? 2002 PO4 A O4  1 
HETATM 5273 C  C   . 2OP E 5 .   ? 20.663  -32.642 8.368   0.82 30.74 ? 401  2OP B C   1 
HETATM 5274 O  O   . 2OP E 5 .   ? 19.416  -32.441 8.497   0.82 33.49 ? 401  2OP B O   1 
HETATM 5275 C  CB  . 2OP E 5 .   ? 20.054  -34.802 7.160   0.82 17.42 ? 401  2OP B CB  1 
HETATM 5276 O  OHN . 2OP E 5 .   ? 22.251  -34.453 7.988   0.82 17.13 ? 401  2OP B OHN 1 
HETATM 5277 C  CA  . 2OP E 5 .   ? 21.154  -33.788 7.471   0.82 27.04 ? 401  2OP B CA  1 
HETATM 5278 O  OXT . 2OP E 5 .   ? 21.497  -31.884 8.947   0.82 25.77 ? 401  2OP B OXT 1 
HETATM 5279 MG MG  . MG  F 6 .   ? 18.805  -30.619 8.943   0.76 33.61 ? 402  MG  B MG  1 
HETATM 5280 O  O   . HOH G 7 .   ? 13.733  -30.932 -24.307 1.00 30.39 ? 2101 HOH A O   1 
HETATM 5281 O  O   . HOH G 7 .   ? 2.344   -36.389 32.720  1.00 27.50 ? 2102 HOH A O   1 
HETATM 5282 O  O   . HOH G 7 .   ? -3.358  -44.596 24.125  1.00 28.45 ? 2103 HOH A O   1 
HETATM 5283 O  O   . HOH G 7 .   ? 6.277   -51.625 -10.180 1.00 31.21 ? 2104 HOH A O   1 
HETATM 5284 O  O   . HOH G 7 .   ? 18.388  -28.740 6.039   1.00 32.01 ? 2105 HOH A O   1 
HETATM 5285 O  O   . HOH G 7 .   ? 10.786  -39.294 -24.304 1.00 30.97 ? 2106 HOH A O   1 
HETATM 5286 O  O   . HOH G 7 .   ? 10.457  -17.371 9.595   1.00 26.59 ? 2107 HOH A O   1 
HETATM 5287 O  O   . HOH G 7 .   ? 12.791  -32.821 25.430  1.00 16.81 ? 2108 HOH A O   1 
HETATM 5288 O  O   . HOH G 7 .   ? 10.481  -25.943 2.845   1.00 11.86 ? 2109 HOH A O   1 
HETATM 5289 O  O   . HOH G 7 .   ? 14.768  -25.907 8.763   1.00 26.77 ? 2110 HOH A O   1 
HETATM 5290 O  O   . HOH G 7 .   ? 10.851  -48.945 -5.282  1.00 25.91 ? 2111 HOH A O   1 
HETATM 5291 O  O   . HOH G 7 .   ? 2.548   -52.963 -4.080  1.00 33.14 ? 2112 HOH A O   1 
HETATM 5292 O  O   . HOH G 7 .   ? -0.890  -30.820 28.141  1.00 22.28 ? 2113 HOH A O   1 
HETATM 5293 O  O   . HOH G 7 .   ? 10.621  -20.901 21.153  1.00 24.00 ? 2114 HOH A O   1 
HETATM 5294 O  O   . HOH G 7 .   ? -7.109  -29.554 -6.044  1.00 17.40 ? 2115 HOH A O   1 
HETATM 5295 O  O   . HOH G 7 .   ? 7.312   -34.916 -25.194 1.00 23.57 ? 2116 HOH A O   1 
HETATM 5296 O  O   . HOH G 7 .   ? 9.215   -48.868 28.615  1.00 27.64 ? 2117 HOH A O   1 
HETATM 5297 O  O   . HOH G 7 .   ? 3.496   -45.094 -2.646  1.00 26.80 ? 2118 HOH A O   1 
HETATM 5298 O  O   . HOH G 7 .   ? 3.782   -22.519 18.330  1.00 30.97 ? 2119 HOH A O   1 
HETATM 5299 O  O   . HOH G 7 .   ? 1.698   -43.674 -13.252 1.00 20.29 ? 2120 HOH A O   1 
HETATM 5300 O  O   . HOH G 7 .   ? 9.477   -30.646 -12.019 1.00 17.76 ? 2121 HOH A O   1 
HETATM 5301 O  O   . HOH G 7 .   ? 8.450   -21.920 -4.108  1.00 15.34 ? 2122 HOH A O   1 
HETATM 5302 O  O   . HOH G 7 .   ? 6.507   -29.807 11.263  1.00 19.35 ? 2123 HOH A O   1 
HETATM 5303 O  O   . HOH G 7 .   ? 7.701   -23.845 4.384   1.00 16.75 ? 2124 HOH A O   1 
HETATM 5304 O  O   . HOH G 7 .   ? -9.770  -32.989 1.748   1.00 18.19 ? 2125 HOH A O   1 
HETATM 5305 O  O   . HOH G 7 .   ? 19.348  -24.053 -9.860  1.00 25.47 ? 2126 HOH A O   1 
HETATM 5306 O  O   . HOH G 7 .   ? 8.268   -18.782 -4.955  1.00 18.05 ? 2127 HOH A O   1 
HETATM 5307 O  O   . HOH G 7 .   ? 17.465  -24.690 0.367   1.00 20.55 ? 2128 HOH A O   1 
HETATM 5308 O  O   . HOH G 7 .   ? -4.257  -34.479 -8.211  1.00 17.00 ? 2129 HOH A O   1 
HETATM 5309 O  O   . HOH G 7 .   ? -3.752  -41.584 -6.761  1.00 23.35 ? 2130 HOH A O   1 
HETATM 5310 O  O   . HOH G 7 .   ? 3.362   -48.099 -12.140 1.00 27.78 ? 2131 HOH A O   1 
HETATM 5311 O  O   . HOH G 7 .   ? 9.247   -42.849 -23.589 1.00 33.62 ? 2132 HOH A O   1 
HETATM 5312 O  O   . HOH G 7 .   ? 21.276  -44.389 22.523  1.00 26.01 ? 2133 HOH A O   1 
HETATM 5313 O  O   . HOH G 7 .   ? 13.150  -45.566 -17.138 1.00 23.51 ? 2134 HOH A O   1 
HETATM 5314 O  O   . HOH G 7 .   ? 23.334  -27.514 -10.408 1.00 31.77 ? 2135 HOH A O   1 
HETATM 5315 O  O   . HOH G 7 .   ? 4.132   -38.270 -23.132 1.00 27.13 ? 2136 HOH A O   1 
HETATM 5316 O  O   . HOH G 7 .   ? 2.848   -29.480 16.173  1.00 21.14 ? 2137 HOH A O   1 
HETATM 5317 O  O   . HOH G 7 .   ? 8.622   -27.706 13.163  1.00 22.00 ? 2138 HOH A O   1 
HETATM 5318 O  O   . HOH G 7 .   ? -3.275  -34.122 6.877   1.00 24.78 ? 2139 HOH A O   1 
HETATM 5319 O  O   . HOH G 7 .   ? -4.948  -36.704 5.206   1.00 19.76 ? 2140 HOH A O   1 
HETATM 5320 O  O   . HOH G 7 .   ? 3.120   -25.850 -11.114 1.00 17.16 ? 2141 HOH A O   1 
HETATM 5321 O  O   . HOH G 7 .   ? -8.791  -35.819 -6.559  1.00 21.21 ? 2142 HOH A O   1 
HETATM 5322 O  O   . HOH G 7 .   ? 16.357  -39.498 -3.410  1.00 22.28 ? 2143 HOH A O   1 
HETATM 5323 O  O   . HOH G 7 .   ? 1.289   -31.336 -14.104 1.00 18.51 ? 2144 HOH A O   1 
HETATM 5324 O  O   . HOH G 7 .   ? 3.370   -31.672 -15.803 1.00 18.56 ? 2145 HOH A O   1 
HETATM 5325 O  O   . HOH G 7 .   ? 4.587   -33.683 5.906   1.00 12.99 ? 2146 HOH A O   1 
HETATM 5326 O  O   . HOH G 7 .   ? 19.102  -30.995 -7.182  1.00 22.70 ? 2147 HOH A O   1 
HETATM 5327 O  O   . HOH G 7 .   ? 7.447   -27.232 -11.841 1.00 15.93 ? 2148 HOH A O   1 
HETATM 5328 O  O   . HOH G 7 .   ? -2.326  -13.138 -3.619  1.00 35.39 ? 2149 HOH A O   1 
HETATM 5329 O  O   . HOH G 7 .   ? -7.217  -48.427 15.912  1.00 34.36 ? 2150 HOH A O   1 
HETATM 5330 O  O   . HOH G 7 .   ? 2.418   -27.211 23.577  1.00 25.74 ? 2151 HOH A O   1 
HETATM 5331 O  O   . HOH G 7 .   ? 10.331  -36.429 25.352  1.00 14.71 ? 2152 HOH A O   1 
HETATM 5332 O  O   . HOH G 7 .   ? 19.423  -24.384 -3.360  1.00 24.67 ? 2153 HOH A O   1 
HETATM 5333 O  O   . HOH G 7 .   ? 10.874  -35.111 9.299   1.00 16.76 ? 2154 HOH A O   1 
HETATM 5334 O  O   . HOH G 7 .   ? 7.137   -30.191 7.054   1.00 11.46 ? 2155 HOH A O   1 
HETATM 5335 O  O   . HOH G 7 .   ? 20.238  -23.750 -5.831  1.00 23.51 ? 2156 HOH A O   1 
HETATM 5336 O  O   . HOH G 7 .   ? 5.182   -24.481 5.497   1.00 14.23 ? 2157 HOH A O   1 
HETATM 5337 O  O   . HOH G 7 .   ? 12.306  -32.842 9.346   1.00 20.03 ? 2158 HOH A O   1 
HETATM 5338 O  O   . HOH G 7 .   ? 15.171  -42.943 8.271   1.00 26.64 ? 2159 HOH A O   1 
HETATM 5339 O  O   . HOH G 7 .   ? 14.433  -41.510 28.965  1.00 22.05 ? 2160 HOH A O   1 
HETATM 5340 O  O   . HOH G 7 .   ? -1.418  -45.229 22.438  1.00 19.69 ? 2161 HOH A O   1 
HETATM 5341 O  O   . HOH G 7 .   ? 11.838  -41.644 30.174  1.00 25.14 ? 2162 HOH A O   1 
HETATM 5342 O  O   . HOH G 7 .   ? 12.209  -34.777 27.116  1.00 22.97 ? 2163 HOH A O   1 
HETATM 5343 O  O   . HOH G 7 .   ? 16.308  -39.330 -6.493  1.00 23.28 ? 2164 HOH A O   1 
HETATM 5344 O  O   . HOH G 7 .   ? -10.878 -34.750 -2.956  1.00 31.50 ? 2165 HOH A O   1 
HETATM 5345 O  O   . HOH G 7 .   ? 17.902  -46.673 22.880  1.00 17.29 ? 2166 HOH A O   1 
HETATM 5346 O  O   . HOH G 7 .   ? 10.694  -33.780 15.850  1.00 14.08 ? 2167 HOH A O   1 
HETATM 5347 O  O   . HOH G 7 .   ? 11.831  -24.394 5.595   1.00 17.81 ? 2168 HOH A O   1 
HETATM 5348 O  O   . HOH G 7 .   ? -6.741  -25.006 -5.310  1.00 22.80 ? 2169 HOH A O   1 
HETATM 5349 O  O   . HOH G 7 .   ? 21.261  -34.599 -18.218 1.00 25.34 ? 2170 HOH A O   1 
HETATM 5350 O  O   . HOH G 7 .   ? -2.406  -54.916 7.535   1.00 29.61 ? 2171 HOH A O   1 
HETATM 5351 O  O   . HOH G 7 .   ? 0.278   -28.545 7.611   1.00 18.57 ? 2172 HOH A O   1 
HETATM 5352 O  O   . HOH G 7 .   ? -4.293  -36.335 25.773  1.00 27.83 ? 2173 HOH A O   1 
HETATM 5353 O  O   . HOH G 7 .   ? 7.254   -22.004 -6.635  1.00 13.28 ? 2174 HOH A O   1 
HETATM 5354 O  O   . HOH G 7 .   ? 5.891   -41.670 29.996  1.00 23.18 ? 2175 HOH A O   1 
HETATM 5355 O  O   . HOH G 7 .   ? 9.515   -26.291 25.982  1.00 21.80 ? 2176 HOH A O   1 
HETATM 5356 O  O   . HOH G 7 .   ? 16.355  -54.756 6.183   1.00 29.18 ? 2177 HOH A O   1 
HETATM 5357 O  O   . HOH G 7 .   ? -9.246  -47.464 21.444  1.00 27.39 ? 2178 HOH A O   1 
HETATM 5358 O  O   . HOH G 7 .   ? 10.295  -17.673 -7.358  1.00 27.33 ? 2179 HOH A O   1 
HETATM 5359 O  O   . HOH G 7 .   ? -10.620 -33.381 -1.165  1.00 24.65 ? 2180 HOH A O   1 
HETATM 5360 O  O   . HOH G 7 .   ? -1.680  -24.241 -5.587  1.00 22.84 ? 2181 HOH A O   1 
HETATM 5361 O  O   . HOH G 7 .   ? -6.046  -44.033 2.128   1.00 32.30 ? 2182 HOH A O   1 
HETATM 5362 O  O   . HOH G 7 .   ? -0.192  -36.780 -15.663 1.00 27.03 ? 2183 HOH A O   1 
HETATM 5363 O  O   . HOH G 7 .   ? 18.963  -45.828 4.122   1.00 28.30 ? 2184 HOH A O   1 
HETATM 5364 O  O   . HOH G 7 .   ? -10.341 -37.922 -7.176  1.00 33.11 ? 2185 HOH A O   1 
HETATM 5365 O  O   . HOH G 7 .   ? 11.508  -23.325 -12.225 1.00 35.83 ? 2186 HOH A O   1 
HETATM 5366 O  O   . HOH G 7 .   ? 3.137   -32.061 -20.494 1.00 25.90 ? 2187 HOH A O   1 
HETATM 5367 O  O   . HOH G 7 .   ? 21.703  -28.607 0.120   1.00 18.86 ? 2188 HOH A O   1 
HETATM 5368 O  O   . HOH G 7 .   ? 15.950  -41.899 -2.577  1.00 23.56 ? 2189 HOH A O   1 
HETATM 5369 O  O   . HOH G 7 .   ? -5.460  -33.197 -12.134 1.00 27.40 ? 2190 HOH A O   1 
HETATM 5370 O  O   . HOH G 7 .   ? 3.879   -30.821 11.532  1.00 23.18 ? 2191 HOH A O   1 
HETATM 5371 O  O   . HOH G 7 .   ? -2.787  -54.242 12.707  1.00 22.28 ? 2192 HOH A O   1 
HETATM 5372 O  O   . HOH G 7 .   ? 0.235   -40.990 -16.492 1.00 27.66 ? 2193 HOH A O   1 
HETATM 5373 O  O   . HOH G 7 .   ? -7.243  -24.355 2.245   1.00 31.07 ? 2194 HOH A O   1 
HETATM 5374 O  O   . HOH G 7 .   ? -1.603  -31.883 7.444   1.00 28.11 ? 2195 HOH A O   1 
HETATM 5375 O  O   . HOH G 7 .   ? -1.286  -34.800 14.019  1.00 14.99 ? 2196 HOH A O   1 
HETATM 5376 O  O   . HOH G 7 .   ? 2.564   -44.434 -4.551  1.00 27.69 ? 2197 HOH A O   1 
HETATM 5377 O  O   . HOH G 7 .   ? -5.592  -30.442 -8.410  1.00 20.27 ? 2198 HOH A O   1 
HETATM 5378 O  O   . HOH G 7 .   ? 10.423  -27.002 -20.100 1.00 31.68 ? 2199 HOH A O   1 
HETATM 5379 O  O   . HOH G 7 .   ? 2.141   -21.715 -5.380  1.00 27.74 ? 2200 HOH A O   1 
HETATM 5380 O  O   . HOH G 7 .   ? 19.427  -25.383 2.060   1.00 26.32 ? 2201 HOH A O   1 
HETATM 5381 O  O   . HOH G 7 .   ? 10.913  -34.054 -23.118 1.00 32.19 ? 2202 HOH A O   1 
HETATM 5382 O  O   . HOH G 7 .   ? 14.015  -15.918 16.068  1.00 29.78 ? 2203 HOH A O   1 
HETATM 5383 O  O   . HOH G 7 .   ? 13.250  -24.274 8.090   1.00 27.67 ? 2204 HOH A O   1 
HETATM 5384 O  O   . HOH G 7 .   ? 25.144  -38.550 -16.572 1.00 32.31 ? 2205 HOH A O   1 
HETATM 5385 O  O   . HOH G 7 .   ? -0.778  -32.226 -15.785 1.00 23.71 ? 2206 HOH A O   1 
HETATM 5386 O  O   . HOH G 7 .   ? 19.665  -48.466 21.620  1.00 23.33 ? 2207 HOH A O   1 
HETATM 5387 O  O   . HOH G 7 .   ? 17.538  -52.058 5.184   1.00 30.45 ? 2208 HOH A O   1 
HETATM 5388 O  O   . HOH G 7 .   ? 0.848   -27.025 -12.106 1.00 24.47 ? 2209 HOH A O   1 
HETATM 5389 O  O   . HOH G 7 .   ? 2.415   -30.883 -18.205 1.00 21.01 ? 2210 HOH A O   1 
HETATM 5390 O  O   . HOH G 7 .   ? 4.458   -21.191 -6.194  1.00 25.40 ? 2211 HOH A O   1 
HETATM 5391 O  O   . HOH G 7 .   ? 8.544   -18.058 -9.010  1.00 24.75 ? 2212 HOH A O   1 
HETATM 5392 O  O   . HOH G 7 .   ? 9.174   -14.660 14.718  1.00 32.32 ? 2213 HOH A O   1 
HETATM 5393 O  O   . HOH G 7 .   ? -5.949  -32.787 -9.288  1.00 25.53 ? 2214 HOH A O   1 
HETATM 5394 O  O   . HOH G 7 .   ? -1.128  -27.942 -16.015 1.00 31.92 ? 2215 HOH A O   1 
HETATM 5395 O  O   . HOH G 7 .   ? -7.791  -26.785 -6.397  1.00 23.59 ? 2216 HOH A O   1 
HETATM 5396 O  O   . HOH G 7 .   ? 0.990   -28.576 -14.152 1.00 22.57 ? 2217 HOH A O   1 
HETATM 5397 O  O   . HOH H 7 .   ? 23.682  -4.911  27.800  1.00 35.71 ? 501  HOH B O   1 
HETATM 5398 O  O   . HOH H 7 .   ? 33.758  -42.601 5.104   1.00 26.80 ? 502  HOH B O   1 
HETATM 5399 O  O   . HOH H 7 .   ? -15.492 -15.112 20.178  1.00 30.90 ? 503  HOH B O   1 
HETATM 5400 O  O   . HOH H 7 .   ? 22.886  -23.233 10.788  1.00 24.57 ? 504  HOH B O   1 
HETATM 5401 O  O   . HOH H 7 .   ? -9.531  -24.362 8.232   1.00 28.86 ? 505  HOH B O   1 
HETATM 5402 O  O   . HOH H 7 .   ? 12.334  -13.031 10.201  1.00 28.33 ? 506  HOH B O   1 
HETATM 5403 O  O   . HOH H 7 .   ? 9.160   -19.669 7.488   1.00 17.85 ? 507  HOH B O   1 
HETATM 5404 O  O   . HOH H 7 .   ? 44.722  -38.136 17.357  1.00 30.89 ? 508  HOH B O   1 
HETATM 5405 O  O   . HOH H 7 .   ? 8.150   -14.904 11.157  1.00 24.33 ? 509  HOH B O   1 
HETATM 5406 O  O   . HOH H 7 .   ? 24.914  -10.082 11.954  1.00 25.99 ? 510  HOH B O   1 
HETATM 5407 O  O   . HOH H 7 .   ? 28.814  -19.924 21.971  1.00 23.58 ? 511  HOH B O   1 
HETATM 5408 O  O   . HOH H 7 .   ? 35.761  -38.880 17.790  1.00 30.70 ? 512  HOH B O   1 
HETATM 5409 O  O   . HOH H 7 .   ? -2.832  16.226  17.980  1.00 24.20 ? 513  HOH B O   1 
HETATM 5410 O  O   . HOH H 7 .   ? 28.091  -37.162 33.963  1.00 20.56 ? 514  HOH B O   1 
HETATM 5411 O  O   . HOH H 7 .   ? 0.334   5.280   14.571  1.00 23.88 ? 515  HOH B O   1 
HETATM 5412 O  O   . HOH H 7 .   ? -5.468  -6.297  23.258  1.00 28.54 ? 516  HOH B O   1 
HETATM 5413 O  O   . HOH H 7 .   ? 15.274  -13.122 10.724  1.00 32.10 ? 517  HOH B O   1 
HETATM 5414 O  O   . HOH H 7 .   ? 26.961  -27.759 32.878  1.00 21.02 ? 518  HOH B O   1 
HETATM 5415 O  O   . HOH H 7 .   ? 37.398  -16.331 11.223  1.00 24.42 ? 519  HOH B O   1 
HETATM 5416 O  O   . HOH H 7 .   ? 21.684  -17.084 14.045  1.00 27.55 ? 520  HOH B O   1 
HETATM 5417 O  O   . HOH H 7 .   ? 5.722   -16.328 3.215   1.00 15.04 ? 521  HOH B O   1 
HETATM 5418 O  O   . HOH H 7 .   ? 40.035  -17.575 8.663   1.00 20.74 ? 522  HOH B O   1 
HETATM 5419 O  O   . HOH H 7 .   ? 26.977  -44.257 11.724  1.00 30.89 ? 523  HOH B O   1 
HETATM 5420 O  O   . HOH H 7 .   ? 32.845  -17.351 13.846  1.00 28.90 ? 524  HOH B O   1 
HETATM 5421 O  O   . HOH H 7 .   ? 26.499  -30.209 4.005   1.00 25.92 ? 525  HOH B O   1 
HETATM 5422 O  O   . HOH H 7 .   ? -4.644  -23.079 2.270   1.00 20.36 ? 526  HOH B O   1 
HETATM 5423 O  O   . HOH H 7 .   ? 11.201  1.392   17.448  1.00 21.18 ? 527  HOH B O   1 
HETATM 5424 O  O   . HOH H 7 .   ? 31.771  -44.143 6.978   1.00 28.75 ? 528  HOH B O   1 
HETATM 5425 O  O   . HOH H 7 .   ? -5.415  -13.783 -0.568  1.00 20.75 ? 529  HOH B O   1 
HETATM 5426 O  O   . HOH H 7 .   ? 3.441   -9.434  15.003  1.00 25.39 ? 530  HOH B O   1 
HETATM 5427 O  O   . HOH H 7 .   ? 6.424   7.297   3.418   1.00 31.23 ? 531  HOH B O   1 
HETATM 5428 O  O   . HOH H 7 .   ? 40.377  -30.662 25.053  1.00 24.86 ? 532  HOH B O   1 
HETATM 5429 O  O   . HOH H 7 .   ? 10.071  1.361   6.145   1.00 21.35 ? 533  HOH B O   1 
HETATM 5430 O  O   . HOH H 7 .   ? 22.298  -41.859 21.044  1.00 25.06 ? 534  HOH B O   1 
HETATM 5431 O  O   . HOH H 7 .   ? 43.074  -29.248 14.434  1.00 18.25 ? 535  HOH B O   1 
HETATM 5432 O  O   . HOH H 7 .   ? 14.288  -19.340 1.220   1.00 19.93 ? 536  HOH B O   1 
HETATM 5433 O  O   . HOH H 7 .   ? 15.491  -1.100  2.254   1.00 25.02 ? 537  HOH B O   1 
HETATM 5434 O  O   . HOH H 7 .   ? -0.963  23.216  19.966  1.00 21.43 ? 538  HOH B O   1 
HETATM 5435 O  O   . HOH H 7 .   ? -0.132  -3.765  -0.000  1.00 23.39 ? 539  HOH B O   1 
HETATM 5436 O  O   . HOH H 7 .   ? 7.259   -2.427  14.760  1.00 26.73 ? 540  HOH B O   1 
HETATM 5437 O  O   . HOH H 7 .   ? -2.260  -2.567  1.491   1.00 19.46 ? 541  HOH B O   1 
HETATM 5438 O  O   . HOH H 7 .   ? 11.182  11.469  8.644   1.00 24.51 ? 542  HOH B O   1 
HETATM 5439 O  O   . HOH H 7 .   ? 44.805  -30.044 12.290  1.00 28.19 ? 543  HOH B O   1 
HETATM 5440 O  O   . HOH H 7 .   ? 2.344   -13.241 3.985   1.00 17.75 ? 544  HOH B O   1 
HETATM 5441 O  O   . HOH H 7 .   ? 31.858  -16.372 20.628  1.00 25.67 ? 545  HOH B O   1 
HETATM 5442 O  O   . HOH H 7 .   ? 39.344  -18.907 23.444  1.00 34.37 ? 546  HOH B O   1 
HETATM 5443 O  O   . HOH H 7 .   ? 17.909  -6.292  17.454  1.00 25.73 ? 547  HOH B O   1 
HETATM 5444 O  O   . HOH H 7 .   ? 15.087  -16.451 1.233   1.00 24.24 ? 548  HOH B O   1 
HETATM 5445 O  O   . HOH H 7 .   ? 7.461   -6.422  -0.866  1.00 26.19 ? 549  HOH B O   1 
HETATM 5446 O  O   . HOH H 7 .   ? 33.417  -23.754 2.435   1.00 22.88 ? 550  HOH B O   1 
HETATM 5447 O  O   . HOH H 7 .   ? 10.947  -6.267  0.461   1.00 22.21 ? 551  HOH B O   1 
HETATM 5448 O  O   . HOH H 7 .   ? -7.249  -9.718  -0.636  1.00 19.37 ? 552  HOH B O   1 
HETATM 5449 O  O   . HOH H 7 .   ? 40.668  -29.035 7.700   1.00 22.99 ? 553  HOH B O   1 
HETATM 5450 O  O   . HOH H 7 .   ? 34.210  -36.816 30.707  1.00 26.22 ? 554  HOH B O   1 
HETATM 5451 O  O   . HOH H 7 .   ? 44.004  -40.660 7.056   1.00 25.39 ? 555  HOH B O   1 
HETATM 5452 O  O   . HOH H 7 .   ? -6.922  -19.826 6.400   1.00 27.21 ? 556  HOH B O   1 
HETATM 5453 O  O   . HOH H 7 .   ? 27.312  -32.354 3.215   1.00 27.09 ? 557  HOH B O   1 
HETATM 5454 O  O   . HOH H 7 .   ? -11.697 -15.357 1.928   1.00 24.24 ? 558  HOH B O   1 
HETATM 5455 O  O   . HOH H 7 .   ? 4.181   -16.156 5.732   1.00 19.84 ? 559  HOH B O   1 
HETATM 5456 O  O   . HOH H 7 .   ? 9.495   -12.130 4.589   1.00 22.77 ? 560  HOH B O   1 
HETATM 5457 O  O   . HOH H 7 .   ? 38.423  -29.648 2.100   1.00 39.49 ? 561  HOH B O   1 
HETATM 5458 O  O   . HOH H 7 .   ? 3.769   3.158   21.871  1.00 26.38 ? 562  HOH B O   1 
HETATM 5459 O  O   . HOH H 7 .   ? 8.594   -15.793 -5.549  1.00 18.56 ? 563  HOH B O   1 
HETATM 5460 O  O   . HOH H 7 .   ? 39.741  -23.326 24.449  1.00 30.64 ? 564  HOH B O   1 
HETATM 5461 O  O   . HOH H 7 .   ? 10.433  -11.246 11.993  1.00 21.42 ? 565  HOH B O   1 
HETATM 5462 O  O   . HOH H 7 .   ? 37.516  -22.338 24.173  1.00 29.98 ? 566  HOH B O   1 
HETATM 5463 O  O   . HOH H 7 .   ? 7.546   -4.657  13.339  1.00 16.55 ? 567  HOH B O   1 
HETATM 5464 O  O   . HOH H 7 .   ? 5.816   -1.777  0.138   1.00 23.97 ? 568  HOH B O   1 
HETATM 5465 O  O   . HOH H 7 .   ? -1.056  -8.157  -1.618  1.00 24.59 ? 569  HOH B O   1 
HETATM 5466 O  O   . HOH H 7 .   ? 38.412  -33.763 25.621  1.00 27.83 ? 570  HOH B O   1 
HETATM 5467 O  O   . HOH H 7 .   ? 6.979   11.103  29.853  1.00 22.01 ? 571  HOH B O   1 
HETATM 5468 O  O   . HOH H 7 .   ? 12.568  -6.068  -1.992  1.00 26.22 ? 572  HOH B O   1 
HETATM 5469 O  O   . HOH H 7 .   ? 2.538   21.190  26.145  1.00 30.30 ? 573  HOH B O   1 
HETATM 5470 O  O   . HOH H 7 .   ? 41.756  -31.548 8.338   1.00 33.65 ? 574  HOH B O   1 
HETATM 5471 O  O   . HOH H 7 .   ? -6.241  -20.694 2.055   1.00 24.22 ? 575  HOH B O   1 
HETATM 5472 O  O   . HOH H 7 .   ? 25.470  -16.984 24.056  1.00 31.92 ? 576  HOH B O   1 
HETATM 5473 O  O   . HOH H 7 .   ? 13.448  -8.688  -3.180  1.00 24.59 ? 577  HOH B O   1 
HETATM 5474 O  O   . HOH H 7 .   ? -0.157  -6.959  21.793  1.00 28.91 ? 578  HOH B O   1 
HETATM 5475 O  O   . HOH H 7 .   ? 22.426  -27.679 19.753  1.00 19.35 ? 579  HOH B O   1 
HETATM 5476 O  O   . HOH H 7 .   ? 18.454  -1.108  10.619  1.00 31.37 ? 580  HOH B O   1 
HETATM 5477 O  O   . HOH H 7 .   ? 1.735   -11.991 19.037  1.00 27.85 ? 581  HOH B O   1 
HETATM 5478 O  O   . HOH H 7 .   ? -0.929  7.143   7.224   1.00 28.61 ? 582  HOH B O   1 
HETATM 5479 O  O   . HOH H 7 .   ? 16.061  -27.408 22.980  1.00 18.30 ? 583  HOH B O   1 
HETATM 5480 O  O   . HOH H 7 .   ? 25.601  -36.562 1.631   1.00 29.66 ? 584  HOH B O   1 
HETATM 5481 O  O   . HOH H 7 .   ? 4.424   18.238  5.266   1.00 37.41 ? 585  HOH B O   1 
HETATM 5482 O  O   . HOH H 7 .   ? 3.178   -29.501 13.184  1.00 26.81 ? 586  HOH B O   1 
HETATM 5483 O  O   . HOH H 7 .   ? -4.277  -2.806  -0.375  1.00 21.52 ? 587  HOH B O   1 
HETATM 5484 O  O   . HOH H 7 .   ? -1.318  0.508   -1.315  1.00 32.09 ? 588  HOH B O   1 
HETATM 5485 O  O   . HOH H 7 .   ? 4.268   9.578   7.948   1.00 35.89 ? 589  HOH B O   1 
HETATM 5486 O  O   . HOH H 7 .   ? 0.525   -9.713  -2.538  1.00 23.82 ? 590  HOH B O   1 
HETATM 5487 O  O   . HOH H 7 .   ? -0.817  -5.127  -2.092  1.00 24.98 ? 591  HOH B O   1 
HETATM 5488 O  O   . HOH H 7 .   ? 6.012   7.451   6.401   1.00 25.41 ? 592  HOH B O   1 
HETATM 5489 O  O   . HOH H 7 .   ? 10.960  -1.484  2.058   1.00 30.05 ? 593  HOH B O   1 
HETATM 5490 O  O   . HOH H 7 .   ? 9.707   -3.533  0.391   1.00 26.30 ? 594  HOH B O   1 
HETATM 5491 O  O   . HOH H 7 .   ? 7.438   -4.028  0.333   1.00 27.33 ? 595  HOH B O   1 
HETATM 5492 O  O   . HOH H 7 .   ? 8.448   7.973   7.121   1.00 23.07 ? 596  HOH B O   1 
HETATM 5493 O  O   . HOH H 7 .   ? 38.039  -33.953 30.123  1.00 31.38 ? 597  HOH B O   1 
# 
