data_9GWO
# 
_entry.id   9GWO 
# 
_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   9GWO         pdb_00009gwo 10.2210/pdb9gwo/pdb 
WWPDB D_1292141423 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GWO 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'contains the same protein complex with Tubercidin'              8BSD unspecified 
PDB 'contains the same protein complex with Adenosine'               8BZV unspecified 
PDB 'contains the same protein complex with MTA'                     8C5M unspecified 
PDB 'contains the same protein complex with MTA+GLY'                 8OT0 unspecified 
PDB 'contains the same protein complex with ATP'                     8OSX unspecified 
PDB 'contains the same protein complex with ADP'                     8OV1 unspecified 
PDB 'contains the same protein complex with SAM analog BDH 33959089' 8OTR unspecified 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              dominik.oberthuer@desy.de 
_pdbx_contact_author.name_first         Dominik 
_pdbx_contact_author.name_last          Oberthuer 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0894-9590 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kremling, V.'  1 0000-0002-4877-2902 
'Sprenger, J.'  2 0000-0001-7977-3484 
'Oberthuer, D.' 3 0000-0002-0894-9590 
'Kiene, A.'     4 0000-0001-7480-8027 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structures of SARS-CoV-2 methyltransferase nsp10-16 with Cap0-site binders' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kremling, V.'   1 0000-0002-4877-2902 
primary 'Sprenger, J.'   2 0000-0001-7977-3484 
primary 'Oberthuer, D.'  3 0000-0002-0894-9590 
primary 'Middendorf, P.' 4 0000-0002-5243-8384 
primary 'Falke, S.'      5 0000-0003-3409-1791 
primary 'Kiene, A.'      6 0000-0001-7480-8027 
primary 'Klopprogge, B.' 7 0000-0002-0718-1786 
primary 'Scheer, T.E.S.' 8 0009-0000-2377-3127 
primary 'Creon, A.'      9 0009-0005-0266-6759 
# 
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 
;2'-O-methyltransferase nsp16
;
34150.090 1   2.1.1.57 ? ? ? 
2  polymer     man 'Non-structural protein 10' 14859.983 1   ?        ? ? ? 
3  non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237   1   ?        ? ? ? 
4  non-polymer syn 1,2-ETHANEDIOL 62.068    14  ?        ? ? ? 
5  non-polymer syn 'SODIUM ION' 22.990    2   ?        ? ? ? 
6  non-polymer syn 
;7-[(3~{S},4~{S},6~{R})-1-[(2~{S})-2-azanyl-3-(1~{H}-indol-3-yl)propanoyl]-4-methyl-4,6-bis(oxidanyl)azepan-3-yl]-1,3-dimethyl-purine-2,6-dione
;
509.558   1   ?        ? ? ? 
7  non-polymer nat 'DIMETHYL SULFOXIDE' 78.133    1   ?        ? ? ? 
8  non-polymer syn S-ADENOSYLMETHIONINE 398.437   1   ?        ? ? ? 
9  non-polymer syn 'ZINC ION' 65.409    2   ?        ? ? ? 
10 non-polymer syn IMIDAZOLE 69.085    1   ?        ? ? ? 
11 water       nat water 18.015    110 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Non-structural protein 16,nsp16'      
2 'nsp10,Growth factor-like peptide,GFL' 
# 
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 
;SSQAWQPGVAMPNLYKMQRMLLEKCDLQNYGDSATLPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAP
GTAVLRQWLPTGTLLVDSDLNDFVSDADSTLIGDCATVHTANKWDLIISDMYDPKTKNVTKENDSKEGFFTYICGFIQQK
LALGGSVAIKITEHSWNADLYKLMGHFAWWTAFVTNVNASSSEAFLIGCNYLGKPREQIDGYVMHANYIFWRNTNPIQLS
SYSLFDMSKFPLKLRGTAVMSLKEGQINDMILSLLSKGRLIIRENNRVVISSDVLVNNENLYFQ
;
;SSQAWQPGVAMPNLYKMQRMLLEKCDLQNYGDSATLPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAP
GTAVLRQWLPTGTLLVDSDLNDFVSDADSTLIGDCATVHTANKWDLIISDMYDPKTKNVTKENDSKEGFFTYICGFIQQK
LALGGSVAIKITEHSWNADLYKLMGHFAWWTAFVTNVNASSSEAFLIGCNYLGKPREQIDGYVMHANYIFWRNTNPIQLS
SYSLFDMSKFPLKLRGTAVMSLKEGQINDMILSLLSKGRLIIRENNRVVISSDVLVNNENLYFQ
;
A ? 
2 'polypeptide(L)' no no 
;GAGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRC
HIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQ
;
;GAGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRC
HIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQ
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3  '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES   
4  1,2-ETHANEDIOL EDO   
5  'SODIUM ION' NA    
6  
;7-[(3~{S},4~{S},6~{R})-1-[(2~{S})-2-azanyl-3-(1~{H}-indol-3-yl)propanoyl]-4-methyl-4,6-bis(oxidanyl)azepan-3-yl]-1,3-dimethyl-purine-2,6-dione
;
A1IQS 
7  'DIMETHYL SULFOXIDE' DMS   
8  S-ADENOSYLMETHIONINE SAM   
9  'ZINC ION' ZN    
10 IMIDAZOLE IMD   
11 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   SER n 
1 3   GLN n 
1 4   ALA n 
1 5   TRP n 
1 6   GLN n 
1 7   PRO n 
1 8   GLY n 
1 9   VAL n 
1 10  ALA n 
1 11  MET n 
1 12  PRO n 
1 13  ASN n 
1 14  LEU n 
1 15  TYR n 
1 16  LYS n 
1 17  MET n 
1 18  GLN n 
1 19  ARG n 
1 20  MET n 
1 21  LEU n 
1 22  LEU n 
1 23  GLU n 
1 24  LYS n 
1 25  CYS n 
1 26  ASP n 
1 27  LEU n 
1 28  GLN n 
1 29  ASN n 
1 30  TYR n 
1 31  GLY n 
1 32  ASP n 
1 33  SER n 
1 34  ALA n 
1 35  THR n 
1 36  LEU n 
1 37  PRO n 
1 38  LYS n 
1 39  GLY n 
1 40  ILE n 
1 41  MET n 
1 42  MET n 
1 43  ASN n 
1 44  VAL n 
1 45  ALA n 
1 46  LYS n 
1 47  TYR n 
1 48  THR n 
1 49  GLN n 
1 50  LEU n 
1 51  CYS n 
1 52  GLN n 
1 53  TYR n 
1 54  LEU n 
1 55  ASN n 
1 56  THR n 
1 57  LEU n 
1 58  THR n 
1 59  LEU n 
1 60  ALA n 
1 61  VAL n 
1 62  PRO n 
1 63  TYR n 
1 64  ASN n 
1 65  MET n 
1 66  ARG n 
1 67  VAL n 
1 68  ILE n 
1 69  HIS n 
1 70  PHE n 
1 71  GLY n 
1 72  ALA n 
1 73  GLY n 
1 74  SER n 
1 75  ASP n 
1 76  LYS n 
1 77  GLY n 
1 78  VAL n 
1 79  ALA n 
1 80  PRO n 
1 81  GLY n 
1 82  THR n 
1 83  ALA n 
1 84  VAL n 
1 85  LEU n 
1 86  ARG n 
1 87  GLN n 
1 88  TRP n 
1 89  LEU n 
1 90  PRO n 
1 91  THR n 
1 92  GLY n 
1 93  THR n 
1 94  LEU n 
1 95  LEU n 
1 96  VAL n 
1 97  ASP n 
1 98  SER n 
1 99  ASP n 
1 100 LEU n 
1 101 ASN n 
1 102 ASP n 
1 103 PHE n 
1 104 VAL n 
1 105 SER n 
1 106 ASP n 
1 107 ALA n 
1 108 ASP n 
1 109 SER n 
1 110 THR n 
1 111 LEU n 
1 112 ILE n 
1 113 GLY n 
1 114 ASP n 
1 115 CYS n 
1 116 ALA n 
1 117 THR n 
1 118 VAL n 
1 119 HIS n 
1 120 THR n 
1 121 ALA n 
1 122 ASN n 
1 123 LYS n 
1 124 TRP n 
1 125 ASP n 
1 126 LEU n 
1 127 ILE n 
1 128 ILE n 
1 129 SER n 
1 130 ASP n 
1 131 MET n 
1 132 TYR n 
1 133 ASP n 
1 134 PRO n 
1 135 LYS n 
1 136 THR n 
1 137 LYS n 
1 138 ASN n 
1 139 VAL n 
1 140 THR n 
1 141 LYS n 
1 142 GLU n 
1 143 ASN n 
1 144 ASP n 
1 145 SER n 
1 146 LYS n 
1 147 GLU n 
1 148 GLY n 
1 149 PHE n 
1 150 PHE n 
1 151 THR n 
1 152 TYR n 
1 153 ILE n 
1 154 CYS n 
1 155 GLY n 
1 156 PHE n 
1 157 ILE n 
1 158 GLN n 
1 159 GLN n 
1 160 LYS n 
1 161 LEU n 
1 162 ALA n 
1 163 LEU n 
1 164 GLY n 
1 165 GLY n 
1 166 SER n 
1 167 VAL n 
1 168 ALA n 
1 169 ILE n 
1 170 LYS n 
1 171 ILE n 
1 172 THR n 
1 173 GLU n 
1 174 HIS n 
1 175 SER n 
1 176 TRP n 
1 177 ASN n 
1 178 ALA n 
1 179 ASP n 
1 180 LEU n 
1 181 TYR n 
1 182 LYS n 
1 183 LEU n 
1 184 MET n 
1 185 GLY n 
1 186 HIS n 
1 187 PHE n 
1 188 ALA n 
1 189 TRP n 
1 190 TRP n 
1 191 THR n 
1 192 ALA n 
1 193 PHE n 
1 194 VAL n 
1 195 THR n 
1 196 ASN n 
1 197 VAL n 
1 198 ASN n 
1 199 ALA n 
1 200 SER n 
1 201 SER n 
1 202 SER n 
1 203 GLU n 
1 204 ALA n 
1 205 PHE n 
1 206 LEU n 
1 207 ILE n 
1 208 GLY n 
1 209 CYS n 
1 210 ASN n 
1 211 TYR n 
1 212 LEU n 
1 213 GLY n 
1 214 LYS n 
1 215 PRO n 
1 216 ARG n 
1 217 GLU n 
1 218 GLN n 
1 219 ILE n 
1 220 ASP n 
1 221 GLY n 
1 222 TYR n 
1 223 VAL n 
1 224 MET n 
1 225 HIS n 
1 226 ALA n 
1 227 ASN n 
1 228 TYR n 
1 229 ILE n 
1 230 PHE n 
1 231 TRP n 
1 232 ARG n 
1 233 ASN n 
1 234 THR n 
1 235 ASN n 
1 236 PRO n 
1 237 ILE n 
1 238 GLN n 
1 239 LEU n 
1 240 SER n 
1 241 SER n 
1 242 TYR n 
1 243 SER n 
1 244 LEU n 
1 245 PHE n 
1 246 ASP n 
1 247 MET n 
1 248 SER n 
1 249 LYS n 
1 250 PHE n 
1 251 PRO n 
1 252 LEU n 
1 253 LYS n 
1 254 LEU n 
1 255 ARG n 
1 256 GLY n 
1 257 THR n 
1 258 ALA n 
1 259 VAL n 
1 260 MET n 
1 261 SER n 
1 262 LEU n 
1 263 LYS n 
1 264 GLU n 
1 265 GLY n 
1 266 GLN n 
1 267 ILE n 
1 268 ASN n 
1 269 ASP n 
1 270 MET n 
1 271 ILE n 
1 272 LEU n 
1 273 SER n 
1 274 LEU n 
1 275 LEU n 
1 276 SER n 
1 277 LYS n 
1 278 GLY n 
1 279 ARG n 
1 280 LEU n 
1 281 ILE n 
1 282 ILE n 
1 283 ARG n 
1 284 GLU n 
1 285 ASN n 
1 286 ASN n 
1 287 ARG n 
1 288 VAL n 
1 289 VAL n 
1 290 ILE n 
1 291 SER n 
1 292 SER n 
1 293 ASP n 
1 294 VAL n 
1 295 LEU n 
1 296 VAL n 
1 297 ASN n 
1 298 ASN n 
1 299 GLU n 
1 300 ASN n 
1 301 LEU n 
1 302 TYR n 
1 303 PHE n 
1 304 GLN n 
2 1   GLY n 
2 2   ALA n 
2 3   GLY n 
2 4   ASN n 
2 5   ALA n 
2 6   THR n 
2 7   GLU n 
2 8   VAL n 
2 9   PRO n 
2 10  ALA n 
2 11  ASN n 
2 12  SER n 
2 13  THR n 
2 14  VAL n 
2 15  LEU n 
2 16  SER n 
2 17  PHE n 
2 18  CYS n 
2 19  ALA n 
2 20  PHE n 
2 21  ALA n 
2 22  VAL n 
2 23  ASP n 
2 24  ALA n 
2 25  ALA n 
2 26  LYS n 
2 27  ALA n 
2 28  TYR n 
2 29  LYS n 
2 30  ASP n 
2 31  TYR n 
2 32  LEU n 
2 33  ALA n 
2 34  SER n 
2 35  GLY n 
2 36  GLY n 
2 37  GLN n 
2 38  PRO n 
2 39  ILE n 
2 40  THR n 
2 41  ASN n 
2 42  CYS n 
2 43  VAL n 
2 44  LYS n 
2 45  MET n 
2 46  LEU n 
2 47  CYS n 
2 48  THR n 
2 49  HIS n 
2 50  THR n 
2 51  GLY n 
2 52  THR n 
2 53  GLY n 
2 54  GLN n 
2 55  ALA n 
2 56  ILE n 
2 57  THR n 
2 58  VAL n 
2 59  THR n 
2 60  PRO n 
2 61  GLU n 
2 62  ALA n 
2 63  ASN n 
2 64  MET n 
2 65  ASP n 
2 66  GLN n 
2 67  GLU n 
2 68  SER n 
2 69  PHE n 
2 70  GLY n 
2 71  GLY n 
2 72  ALA n 
2 73  SER n 
2 74  CYS n 
2 75  CYS n 
2 76  LEU n 
2 77  TYR n 
2 78  CYS n 
2 79  ARG n 
2 80  CYS n 
2 81  HIS n 
2 82  ILE n 
2 83  ASP n 
2 84  HIS n 
2 85  PRO n 
2 86  ASN n 
2 87  PRO n 
2 88  LYS n 
2 89  GLY n 
2 90  PHE n 
2 91  CYS n 
2 92  ASP n 
2 93  LEU n 
2 94  LYS n 
2 95  GLY n 
2 96  LYS n 
2 97  TYR n 
2 98  VAL n 
2 99  GLN n 
2 100 ILE n 
2 101 PRO n 
2 102 THR n 
2 103 THR n 
2 104 CYS n 
2 105 ALA n 
2 106 ASN n 
2 107 ASP n 
2 108 PRO n 
2 109 VAL n 
2 110 GLY n 
2 111 PHE n 
2 112 THR n 
2 113 LEU n 
2 114 LYS n 
2 115 ASN n 
2 116 THR n 
2 117 VAL n 
2 118 CYS n 
2 119 THR n 
2 120 VAL n 
2 121 CYS n 
2 122 GLY n 
2 123 MET n 
2 124 TRP n 
2 125 LYS n 
2 126 GLY n 
2 127 TYR n 
2 128 GLY n 
2 129 CYS n 
2 130 SER n 
2 131 CYS n 
2 132 ASP n 
2 133 GLN n 
2 134 LEU n 
2 135 ARG n 
2 136 GLU n 
2 137 PRO n 
2 138 MET n 
2 139 LEU n 
2 140 GLN 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' 1 304 ? ? 'rep, 1a-1b' ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? 
? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 140 ? ? 'rep, 1a-1b' ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? 
? ? ? ? ? ? '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 
A1IQS non-polymer         . 
;7-[(3~{S},4~{S},6~{R})-1-[(2~{S})-2-azanyl-3-(1~{H}-indol-3-yl)propanoyl]-4-methyl-4,6-bis(oxidanyl)azepan-3-yl]-1,3-dimethyl-purine-2,6-dione
;
?                 'C25 H31 N7 O5'   509.558 
ALA   'L-peptide linking' y ALANINE ?                 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ?                 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE ?                 'C3 H7 N O2 S'    121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ?                 'C2 H6 O S'       78.133  
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'        62.068  
GLN   'L-peptide linking' y GLUTAMINE ?                 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE ?                 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE ?                 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER ?                 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                 'C6 H13 N O2'     131.173 
IMD   non-polymer         . IMIDAZOLE ?                 'C3 H5 N2 1'      69.085  
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 
MES   non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' ?                 'C6 H13 N O4 S'   195.237 
MET   'L-peptide linking' y METHIONINE ?                 'C5 H11 N O2 S'   149.211 
NA    non-polymer         . 'SODIUM ION' ?                 'Na 1'            22.990  
PHE   'L-peptide linking' y PHENYLALANINE ?                 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ?                 'C5 H9 N O2'      115.130 
SAM   non-polymer         . S-ADENOSYLMETHIONINE ?                 'C15 H22 N6 O5 S' 398.437 
SER   'L-peptide linking' y SERINE ?                 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE ?                 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE ?                 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE ?                 'C5 H11 N O2'     117.146 
ZN    non-polymer         . 'ZINC ION' ?                 'Zn 2'            65.409  
# 
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   SER 1   6799 6799 SER SER A . n 
A 1 2   SER 2   6800 6800 SER SER A . n 
A 1 3   GLN 3   6801 6801 GLN GLN A . n 
A 1 4   ALA 4   6802 6802 ALA ALA A . n 
A 1 5   TRP 5   6803 6803 TRP TRP A . n 
A 1 6   GLN 6   6804 6804 GLN GLN A . n 
A 1 7   PRO 7   6805 6805 PRO PRO A . n 
A 1 8   GLY 8   6806 6806 GLY GLY A . n 
A 1 9   VAL 9   6807 6807 VAL VAL A . n 
A 1 10  ALA 10  6808 6808 ALA ALA A . n 
A 1 11  MET 11  6809 6809 MET MET A . n 
A 1 12  PRO 12  6810 6810 PRO PRO A . n 
A 1 13  ASN 13  6811 6811 ASN ASN A . n 
A 1 14  LEU 14  6812 6812 LEU LEU A . n 
A 1 15  TYR 15  6813 6813 TYR TYR A . n 
A 1 16  LYS 16  6814 6814 LYS LYS A . n 
A 1 17  MET 17  6815 6815 MET MET A . n 
A 1 18  GLN 18  6816 6816 GLN GLN A . n 
A 1 19  ARG 19  6817 6817 ARG ARG A . n 
A 1 20  MET 20  6818 6818 MET MET A . n 
A 1 21  LEU 21  6819 6819 LEU LEU A . n 
A 1 22  LEU 22  6820 6820 LEU LEU A . n 
A 1 23  GLU 23  6821 6821 GLU GLU A . n 
A 1 24  LYS 24  6822 6822 LYS LYS A . n 
A 1 25  CYS 25  6823 6823 CYS CYS A . n 
A 1 26  ASP 26  6824 6824 ASP ASP A . n 
A 1 27  LEU 27  6825 6825 LEU LEU A . n 
A 1 28  GLN 28  6826 6826 GLN GLN A . n 
A 1 29  ASN 29  6827 6827 ASN ASN A . n 
A 1 30  TYR 30  6828 6828 TYR TYR A . n 
A 1 31  GLY 31  6829 6829 GLY GLY A . n 
A 1 32  ASP 32  6830 6830 ASP ASP A . n 
A 1 33  SER 33  6831 6831 SER SER A . n 
A 1 34  ALA 34  6832 6832 ALA ALA A . n 
A 1 35  THR 35  6833 6833 THR THR A . n 
A 1 36  LEU 36  6834 6834 LEU LEU A . n 
A 1 37  PRO 37  6835 6835 PRO PRO A . n 
A 1 38  LYS 38  6836 6836 LYS LYS A . n 
A 1 39  GLY 39  6837 6837 GLY GLY A . n 
A 1 40  ILE 40  6838 6838 ILE ILE A . n 
A 1 41  MET 41  6839 6839 MET MET A . n 
A 1 42  MET 42  6840 6840 MET MET A . n 
A 1 43  ASN 43  6841 6841 ASN ASN A . n 
A 1 44  VAL 44  6842 6842 VAL VAL A . n 
A 1 45  ALA 45  6843 6843 ALA ALA A . n 
A 1 46  LYS 46  6844 6844 LYS LYS A . n 
A 1 47  TYR 47  6845 6845 TYR TYR A . n 
A 1 48  THR 48  6846 6846 THR THR A . n 
A 1 49  GLN 49  6847 6847 GLN GLN A . n 
A 1 50  LEU 50  6848 6848 LEU LEU A . n 
A 1 51  CYS 51  6849 6849 CYS CYS A . n 
A 1 52  GLN 52  6850 6850 GLN GLN A . n 
A 1 53  TYR 53  6851 6851 TYR TYR A . n 
A 1 54  LEU 54  6852 6852 LEU LEU A . n 
A 1 55  ASN 55  6853 6853 ASN ASN A . n 
A 1 56  THR 56  6854 6854 THR THR A . n 
A 1 57  LEU 57  6855 6855 LEU LEU A . n 
A 1 58  THR 58  6856 6856 THR THR A . n 
A 1 59  LEU 59  6857 6857 LEU LEU A . n 
A 1 60  ALA 60  6858 6858 ALA ALA A . n 
A 1 61  VAL 61  6859 6859 VAL VAL A . n 
A 1 62  PRO 62  6860 6860 PRO PRO A . n 
A 1 63  TYR 63  6861 6861 TYR TYR A . n 
A 1 64  ASN 64  6862 6862 ASN ASN A . n 
A 1 65  MET 65  6863 6863 MET MET A . n 
A 1 66  ARG 66  6864 6864 ARG ARG A . n 
A 1 67  VAL 67  6865 6865 VAL VAL A . n 
A 1 68  ILE 68  6866 6866 ILE ILE A . n 
A 1 69  HIS 69  6867 6867 HIS HIS A . n 
A 1 70  PHE 70  6868 6868 PHE PHE A . n 
A 1 71  GLY 71  6869 6869 GLY GLY A . n 
A 1 72  ALA 72  6870 6870 ALA ALA A . n 
A 1 73  GLY 73  6871 6871 GLY GLY A . n 
A 1 74  SER 74  6872 6872 SER SER A . n 
A 1 75  ASP 75  6873 6873 ASP ASP A . n 
A 1 76  LYS 76  6874 6874 LYS LYS A . n 
A 1 77  GLY 77  6875 6875 GLY GLY A . n 
A 1 78  VAL 78  6876 6876 VAL VAL A . n 
A 1 79  ALA 79  6877 6877 ALA ALA A . n 
A 1 80  PRO 80  6878 6878 PRO PRO A . n 
A 1 81  GLY 81  6879 6879 GLY GLY A . n 
A 1 82  THR 82  6880 6880 THR THR A . n 
A 1 83  ALA 83  6881 6881 ALA ALA A . n 
A 1 84  VAL 84  6882 6882 VAL VAL A . n 
A 1 85  LEU 85  6883 6883 LEU LEU A . n 
A 1 86  ARG 86  6884 6884 ARG ARG A . n 
A 1 87  GLN 87  6885 6885 GLN GLN A . n 
A 1 88  TRP 88  6886 6886 TRP TRP A . n 
A 1 89  LEU 89  6887 6887 LEU LEU A . n 
A 1 90  PRO 90  6888 6888 PRO PRO A . n 
A 1 91  THR 91  6889 6889 THR THR A . n 
A 1 92  GLY 92  6890 6890 GLY GLY A . n 
A 1 93  THR 93  6891 6891 THR THR A . n 
A 1 94  LEU 94  6892 6892 LEU LEU A . n 
A 1 95  LEU 95  6893 6893 LEU LEU A . n 
A 1 96  VAL 96  6894 6894 VAL VAL A . n 
A 1 97  ASP 97  6895 6895 ASP ASP A . n 
A 1 98  SER 98  6896 6896 SER SER A . n 
A 1 99  ASP 99  6897 6897 ASP ASP A . n 
A 1 100 LEU 100 6898 6898 LEU LEU A . n 
A 1 101 ASN 101 6899 6899 ASN ASN A . n 
A 1 102 ASP 102 6900 6900 ASP ASP A . n 
A 1 103 PHE 103 6901 6901 PHE PHE A . n 
A 1 104 VAL 104 6902 6902 VAL VAL A . n 
A 1 105 SER 105 6903 6903 SER SER A . n 
A 1 106 ASP 106 6904 6904 ASP ASP A . n 
A 1 107 ALA 107 6905 6905 ALA ALA A . n 
A 1 108 ASP 108 6906 6906 ASP ASP A . n 
A 1 109 SER 109 6907 6907 SER SER A . n 
A 1 110 THR 110 6908 6908 THR THR A . n 
A 1 111 LEU 111 6909 6909 LEU LEU A . n 
A 1 112 ILE 112 6910 6910 ILE ILE A . n 
A 1 113 GLY 113 6911 6911 GLY GLY A . n 
A 1 114 ASP 114 6912 6912 ASP ASP A . n 
A 1 115 CYS 115 6913 6913 CYS CYS A . n 
A 1 116 ALA 116 6914 6914 ALA ALA A . n 
A 1 117 THR 117 6915 6915 THR THR A . n 
A 1 118 VAL 118 6916 6916 VAL VAL A . n 
A 1 119 HIS 119 6917 6917 HIS HIS A . n 
A 1 120 THR 120 6918 6918 THR THR A . n 
A 1 121 ALA 121 6919 6919 ALA ALA A . n 
A 1 122 ASN 122 6920 6920 ASN ASN A . n 
A 1 123 LYS 123 6921 6921 LYS LYS A . n 
A 1 124 TRP 124 6922 6922 TRP TRP A . n 
A 1 125 ASP 125 6923 6923 ASP ASP A . n 
A 1 126 LEU 126 6924 6924 LEU LEU A . n 
A 1 127 ILE 127 6925 6925 ILE ILE A . n 
A 1 128 ILE 128 6926 6926 ILE ILE A . n 
A 1 129 SER 129 6927 6927 SER SER A . n 
A 1 130 ASP 130 6928 6928 ASP ASP A . n 
A 1 131 MET 131 6929 6929 MET MET A . n 
A 1 132 TYR 132 6930 6930 TYR TYR A . n 
A 1 133 ASP 133 6931 6931 ASP ASP A . n 
A 1 134 PRO 134 6932 6932 PRO PRO A . n 
A 1 135 LYS 135 6933 6933 LYS LYS A . n 
A 1 136 THR 136 6934 6934 THR THR A . n 
A 1 137 LYS 137 6935 6935 LYS LYS A . n 
A 1 138 ASN 138 6936 6936 ASN ASN A . n 
A 1 139 VAL 139 6937 6937 VAL VAL A . n 
A 1 140 THR 140 6938 6938 THR THR A . n 
A 1 141 LYS 141 6939 6939 LYS LYS A . n 
A 1 142 GLU 142 6940 6940 GLU GLU A . n 
A 1 143 ASN 143 6941 6941 ASN ASN A . n 
A 1 144 ASP 144 6942 6942 ASP ASP A . n 
A 1 145 SER 145 6943 6943 SER SER A . n 
A 1 146 LYS 146 6944 6944 LYS LYS A . n 
A 1 147 GLU 147 6945 6945 GLU GLU A . n 
A 1 148 GLY 148 6946 6946 GLY GLY A . n 
A 1 149 PHE 149 6947 6947 PHE PHE A . n 
A 1 150 PHE 150 6948 6948 PHE PHE A . n 
A 1 151 THR 151 6949 6949 THR THR A . n 
A 1 152 TYR 152 6950 6950 TYR TYR A . n 
A 1 153 ILE 153 6951 6951 ILE ILE A . n 
A 1 154 CYS 154 6952 6952 CYS CYS A . n 
A 1 155 GLY 155 6953 6953 GLY GLY A . n 
A 1 156 PHE 156 6954 6954 PHE PHE A . n 
A 1 157 ILE 157 6955 6955 ILE ILE A . n 
A 1 158 GLN 158 6956 6956 GLN GLN A . n 
A 1 159 GLN 159 6957 6957 GLN GLN A . n 
A 1 160 LYS 160 6958 6958 LYS LYS A . n 
A 1 161 LEU 161 6959 6959 LEU LEU A . n 
A 1 162 ALA 162 6960 6960 ALA ALA A . n 
A 1 163 LEU 163 6961 6961 LEU LEU A . n 
A 1 164 GLY 164 6962 6962 GLY GLY A . n 
A 1 165 GLY 165 6963 6963 GLY GLY A . n 
A 1 166 SER 166 6964 6964 SER SER A . n 
A 1 167 VAL 167 6965 6965 VAL VAL A . n 
A 1 168 ALA 168 6966 6966 ALA ALA A . n 
A 1 169 ILE 169 6967 6967 ILE ILE A . n 
A 1 170 LYS 170 6968 6968 LYS LYS A . n 
A 1 171 ILE 171 6969 6969 ILE ILE A . n 
A 1 172 THR 172 6970 6970 THR THR A . n 
A 1 173 GLU 173 6971 6971 GLU GLU A . n 
A 1 174 HIS 174 6972 6972 HIS HIS A . n 
A 1 175 SER 175 6973 6973 SER SER A . n 
A 1 176 TRP 176 6974 6974 TRP TRP A . n 
A 1 177 ASN 177 6975 6975 ASN ASN A . n 
A 1 178 ALA 178 6976 6976 ALA ALA A . n 
A 1 179 ASP 179 6977 6977 ASP ASP A . n 
A 1 180 LEU 180 6978 6978 LEU LEU A . n 
A 1 181 TYR 181 6979 6979 TYR TYR A . n 
A 1 182 LYS 182 6980 6980 LYS LYS A . n 
A 1 183 LEU 183 6981 6981 LEU LEU A . n 
A 1 184 MET 184 6982 6982 MET MET A . n 
A 1 185 GLY 185 6983 6983 GLY GLY A . n 
A 1 186 HIS 186 6984 6984 HIS HIS A . n 
A 1 187 PHE 187 6985 6985 PHE PHE A . n 
A 1 188 ALA 188 6986 6986 ALA ALA A . n 
A 1 189 TRP 189 6987 6987 TRP TRP A . n 
A 1 190 TRP 190 6988 6988 TRP TRP A . n 
A 1 191 THR 191 6989 6989 THR THR A . n 
A 1 192 ALA 192 6990 6990 ALA ALA A . n 
A 1 193 PHE 193 6991 6991 PHE PHE A . n 
A 1 194 VAL 194 6992 6992 VAL VAL A . n 
A 1 195 THR 195 6993 6993 THR THR A . n 
A 1 196 ASN 196 6994 6994 ASN ASN A . n 
A 1 197 VAL 197 6995 6995 VAL VAL A . n 
A 1 198 ASN 198 6996 6996 ASN ASN A . n 
A 1 199 ALA 199 6997 6997 ALA ALA A . n 
A 1 200 SER 200 6998 6998 SER SER A . n 
A 1 201 SER 201 6999 6999 SER SER A . n 
A 1 202 SER 202 7000 7000 SER SER A . n 
A 1 203 GLU 203 7001 7001 GLU GLU A . n 
A 1 204 ALA 204 7002 7002 ALA ALA A . n 
A 1 205 PHE 205 7003 7003 PHE PHE A . n 
A 1 206 LEU 206 7004 7004 LEU LEU A . n 
A 1 207 ILE 207 7005 7005 ILE ILE A . n 
A 1 208 GLY 208 7006 7006 GLY GLY A . n 
A 1 209 CYS 209 7007 7007 CYS CYS A . n 
A 1 210 ASN 210 7008 7008 ASN ASN A . n 
A 1 211 TYR 211 7009 7009 TYR TYR A . n 
A 1 212 LEU 212 7010 7010 LEU LEU A . n 
A 1 213 GLY 213 7011 7011 GLY GLY A . n 
A 1 214 LYS 214 7012 7012 LYS LYS A . n 
A 1 215 PRO 215 7013 7013 PRO PRO A . n 
A 1 216 ARG 216 7014 7014 ARG ARG A . n 
A 1 217 GLU 217 7015 7015 GLU GLU A . n 
A 1 218 GLN 218 7016 7016 GLN GLN A . n 
A 1 219 ILE 219 7017 7017 ILE ILE A . n 
A 1 220 ASP 220 7018 7018 ASP ASP A . n 
A 1 221 GLY 221 7019 7019 GLY GLY A . n 
A 1 222 TYR 222 7020 7020 TYR TYR A . n 
A 1 223 VAL 223 7021 7021 VAL VAL A . n 
A 1 224 MET 224 7022 7022 MET MET A . n 
A 1 225 HIS 225 7023 7023 HIS HIS A . n 
A 1 226 ALA 226 7024 7024 ALA ALA A . n 
A 1 227 ASN 227 7025 7025 ASN ASN A . n 
A 1 228 TYR 228 7026 7026 TYR TYR A . n 
A 1 229 ILE 229 7027 7027 ILE ILE A . n 
A 1 230 PHE 230 7028 7028 PHE PHE A . n 
A 1 231 TRP 231 7029 7029 TRP TRP A . n 
A 1 232 ARG 232 7030 7030 ARG ARG A . n 
A 1 233 ASN 233 7031 7031 ASN ASN A . n 
A 1 234 THR 234 7032 7032 THR THR A . n 
A 1 235 ASN 235 7033 7033 ASN ASN A . n 
A 1 236 PRO 236 7034 7034 PRO PRO A . n 
A 1 237 ILE 237 7035 7035 ILE ILE A . n 
A 1 238 GLN 238 7036 7036 GLN GLN A . n 
A 1 239 LEU 239 7037 7037 LEU LEU A . n 
A 1 240 SER 240 7038 7038 SER SER A . n 
A 1 241 SER 241 7039 7039 SER SER A . n 
A 1 242 TYR 242 7040 7040 TYR TYR A . n 
A 1 243 SER 243 7041 7041 SER SER A . n 
A 1 244 LEU 244 7042 7042 LEU LEU A . n 
A 1 245 PHE 245 7043 7043 PHE PHE A . n 
A 1 246 ASP 246 7044 7044 ASP ASP A . n 
A 1 247 MET 247 7045 7045 MET MET A . n 
A 1 248 SER 248 7046 7046 SER SER A . n 
A 1 249 LYS 249 7047 7047 LYS LYS A . n 
A 1 250 PHE 250 7048 7048 PHE PHE A . n 
A 1 251 PRO 251 7049 7049 PRO PRO A . n 
A 1 252 LEU 252 7050 7050 LEU LEU A . n 
A 1 253 LYS 253 7051 7051 LYS LYS A . n 
A 1 254 LEU 254 7052 7052 LEU LEU A . n 
A 1 255 ARG 255 7053 7053 ARG ARG A . n 
A 1 256 GLY 256 7054 7054 GLY GLY A . n 
A 1 257 THR 257 7055 7055 THR THR A . n 
A 1 258 ALA 258 7056 7056 ALA ALA A . n 
A 1 259 VAL 259 7057 7057 VAL VAL A . n 
A 1 260 MET 260 7058 7058 MET MET A . n 
A 1 261 SER 261 7059 7059 SER SER A . n 
A 1 262 LEU 262 7060 7060 LEU LEU A . n 
A 1 263 LYS 263 7061 7061 LYS LYS A . n 
A 1 264 GLU 264 7062 7062 GLU GLU A . n 
A 1 265 GLY 265 7063 7063 GLY GLY A . n 
A 1 266 GLN 266 7064 7064 GLN GLN A . n 
A 1 267 ILE 267 7065 7065 ILE ILE A . n 
A 1 268 ASN 268 7066 7066 ASN ASN A . n 
A 1 269 ASP 269 7067 7067 ASP ASP A . n 
A 1 270 MET 270 7068 7068 MET MET A . n 
A 1 271 ILE 271 7069 7069 ILE ILE A . n 
A 1 272 LEU 272 7070 7070 LEU LEU A . n 
A 1 273 SER 273 7071 7071 SER SER A . n 
A 1 274 LEU 274 7072 7072 LEU LEU A . n 
A 1 275 LEU 275 7073 7073 LEU LEU A . n 
A 1 276 SER 276 7074 7074 SER SER A . n 
A 1 277 LYS 277 7075 7075 LYS LYS A . n 
A 1 278 GLY 278 7076 7076 GLY GLY A . n 
A 1 279 ARG 279 7077 7077 ARG ARG A . n 
A 1 280 LEU 280 7078 7078 LEU LEU A . n 
A 1 281 ILE 281 7079 7079 ILE ILE A . n 
A 1 282 ILE 282 7080 7080 ILE ILE A . n 
A 1 283 ARG 283 7081 7081 ARG ARG A . n 
A 1 284 GLU 284 7082 7082 GLU GLU A . n 
A 1 285 ASN 285 7083 7083 ASN ASN A . n 
A 1 286 ASN 286 7084 7084 ASN ASN A . n 
A 1 287 ARG 287 7085 7085 ARG ARG A . n 
A 1 288 VAL 288 7086 7086 VAL VAL A . n 
A 1 289 VAL 289 7087 7087 VAL VAL A . n 
A 1 290 ILE 290 7088 7088 ILE ILE A . n 
A 1 291 SER 291 7089 7089 SER SER A . n 
A 1 292 SER 292 7090 7090 SER SER A . n 
A 1 293 ASP 293 7091 7091 ASP ASP A . n 
A 1 294 VAL 294 7092 7092 VAL VAL A . n 
A 1 295 LEU 295 7093 7093 LEU LEU A . n 
A 1 296 VAL 296 7094 7094 VAL VAL A . n 
A 1 297 ASN 297 7095 7095 ASN ASN A . n 
A 1 298 ASN 298 7096 7096 ASN ASN A . n 
A 1 299 GLU 299 7097 7097 GLU GLU A . n 
A 1 300 ASN 300 7098 7098 ASN ASN A . n 
A 1 301 LEU 301 7099 ?    ?   ?   A . n 
A 1 302 TYR 302 7100 ?    ?   ?   A . n 
A 1 303 PHE 303 7101 ?    ?   ?   A . n 
A 1 304 GLN 304 7102 ?    ?   ?   A . n 
B 2 1   GLY 1   4252 ?    ?   ?   B . n 
B 2 2   ALA 2   4253 ?    ?   ?   B . n 
B 2 3   GLY 3   4254 ?    ?   ?   B . n 
B 2 4   ASN 4   4255 ?    ?   ?   B . n 
B 2 5   ALA 5   4256 ?    ?   ?   B . n 
B 2 6   THR 6   4257 ?    ?   ?   B . n 
B 2 7   GLU 7   4258 ?    ?   ?   B . n 
B 2 8   VAL 8   4259 ?    ?   ?   B . n 
B 2 9   PRO 9   4260 ?    ?   ?   B . n 
B 2 10  ALA 10  4261 ?    ?   ?   B . n 
B 2 11  ASN 11  4262 ?    ?   ?   B . n 
B 2 12  SER 12  4263 ?    ?   ?   B . n 
B 2 13  THR 13  4264 ?    ?   ?   B . n 
B 2 14  VAL 14  4265 ?    ?   ?   B . n 
B 2 15  LEU 15  4266 ?    ?   ?   B . n 
B 2 16  SER 16  4267 ?    ?   ?   B . n 
B 2 17  PHE 17  4268 ?    ?   ?   B . n 
B 2 18  CYS 18  4269 ?    ?   ?   B . n 
B 2 19  ALA 19  4270 4270 ALA ALA B . n 
B 2 20  PHE 20  4271 4271 PHE PHE B . n 
B 2 21  ALA 21  4272 4272 ALA ALA B . n 
B 2 22  VAL 22  4273 4273 VAL VAL B . n 
B 2 23  ASP 23  4274 4274 ASP ASP B . n 
B 2 24  ALA 24  4275 4275 ALA ALA B . n 
B 2 25  ALA 25  4276 4276 ALA ALA B . n 
B 2 26  LYS 26  4277 4277 LYS LYS B . n 
B 2 27  ALA 27  4278 4278 ALA ALA B . n 
B 2 28  TYR 28  4279 4279 TYR TYR B . n 
B 2 29  LYS 29  4280 4280 LYS LYS B . n 
B 2 30  ASP 30  4281 4281 ASP ASP B . n 
B 2 31  TYR 31  4282 4282 TYR TYR B . n 
B 2 32  LEU 32  4283 4283 LEU LEU B . n 
B 2 33  ALA 33  4284 4284 ALA ALA B . n 
B 2 34  SER 34  4285 4285 SER SER B . n 
B 2 35  GLY 35  4286 4286 GLY GLY B . n 
B 2 36  GLY 36  4287 4287 GLY GLY B . n 
B 2 37  GLN 37  4288 4288 GLN GLN B . n 
B 2 38  PRO 38  4289 4289 PRO PRO B . n 
B 2 39  ILE 39  4290 4290 ILE ILE B . n 
B 2 40  THR 40  4291 4291 THR THR B . n 
B 2 41  ASN 41  4292 4292 ASN ASN B . n 
B 2 42  CYS 42  4293 4293 CYS CYS B . n 
B 2 43  VAL 43  4294 4294 VAL VAL B . n 
B 2 44  LYS 44  4295 4295 LYS LYS B . n 
B 2 45  MET 45  4296 4296 MET MET B . n 
B 2 46  LEU 46  4297 4297 LEU LEU B . n 
B 2 47  CYS 47  4298 4298 CYS CYS B . n 
B 2 48  THR 48  4299 4299 THR THR B . n 
B 2 49  HIS 49  4300 4300 HIS HIS B . n 
B 2 50  THR 50  4301 4301 THR THR B . n 
B 2 51  GLY 51  4302 4302 GLY GLY B . n 
B 2 52  THR 52  4303 4303 THR THR B . n 
B 2 53  GLY 53  4304 4304 GLY GLY B . n 
B 2 54  GLN 54  4305 4305 GLN GLN B . n 
B 2 55  ALA 55  4306 4306 ALA ALA B . n 
B 2 56  ILE 56  4307 4307 ILE ILE B . n 
B 2 57  THR 57  4308 4308 THR THR B . n 
B 2 58  VAL 58  4309 4309 VAL VAL B . n 
B 2 59  THR 59  4310 4310 THR THR B . n 
B 2 60  PRO 60  4311 4311 PRO PRO B . n 
B 2 61  GLU 61  4312 4312 GLU GLU B . n 
B 2 62  ALA 62  4313 4313 ALA ALA B . n 
B 2 63  ASN 63  4314 4314 ASN ASN B . n 
B 2 64  MET 64  4315 4315 MET MET B . n 
B 2 65  ASP 65  4316 4316 ASP ASP B . n 
B 2 66  GLN 66  4317 4317 GLN GLN B . n 
B 2 67  GLU 67  4318 4318 GLU GLU B . n 
B 2 68  SER 68  4319 4319 SER SER B . n 
B 2 69  PHE 69  4320 4320 PHE PHE B . n 
B 2 70  GLY 70  4321 4321 GLY GLY B . n 
B 2 71  GLY 71  4322 4322 GLY GLY B . n 
B 2 72  ALA 72  4323 4323 ALA ALA B . n 
B 2 73  SER 73  4324 4324 SER SER B . n 
B 2 74  CYS 74  4325 4325 CYS CYS B . n 
B 2 75  CYS 75  4326 4326 CYS CYS B . n 
B 2 76  LEU 76  4327 4327 LEU LEU B . n 
B 2 77  TYR 77  4328 4328 TYR TYR B . n 
B 2 78  CYS 78  4329 4329 CYS CYS B . n 
B 2 79  ARG 79  4330 4330 ARG ARG B . n 
B 2 80  CYS 80  4331 4331 CYS CYS B . n 
B 2 81  HIS 81  4332 4332 HIS HIS B . n 
B 2 82  ILE 82  4333 4333 ILE ILE B . n 
B 2 83  ASP 83  4334 4334 ASP ASP B . n 
B 2 84  HIS 84  4335 4335 HIS HIS B . n 
B 2 85  PRO 85  4336 4336 PRO PRO B . n 
B 2 86  ASN 86  4337 4337 ASN ASN B . n 
B 2 87  PRO 87  4338 4338 PRO PRO B . n 
B 2 88  LYS 88  4339 4339 LYS LYS B . n 
B 2 89  GLY 89  4340 4340 GLY GLY B . n 
B 2 90  PHE 90  4341 4341 PHE PHE B . n 
B 2 91  CYS 91  4342 4342 CYS CYS B . n 
B 2 92  ASP 92  4343 4343 ASP ASP B . n 
B 2 93  LEU 93  4344 4344 LEU LEU B . n 
B 2 94  LYS 94  4345 4345 LYS LYS B . n 
B 2 95  GLY 95  4346 4346 GLY GLY B . n 
B 2 96  LYS 96  4347 4347 LYS LYS B . n 
B 2 97  TYR 97  4348 4348 TYR TYR B . n 
B 2 98  VAL 98  4349 4349 VAL VAL B . n 
B 2 99  GLN 99  4350 4350 GLN GLN B . n 
B 2 100 ILE 100 4351 4351 ILE ILE B . n 
B 2 101 PRO 101 4352 4352 PRO PRO B . n 
B 2 102 THR 102 4353 4353 THR THR B . n 
B 2 103 THR 103 4354 4354 THR THR B . n 
B 2 104 CYS 104 4355 4355 CYS CYS B . n 
B 2 105 ALA 105 4356 4356 ALA ALA B . n 
B 2 106 ASN 106 4357 4357 ASN ASN B . n 
B 2 107 ASP 107 4358 4358 ASP ASP B . n 
B 2 108 PRO 108 4359 4359 PRO PRO B . n 
B 2 109 VAL 109 4360 4360 VAL VAL B . n 
B 2 110 GLY 110 4361 4361 GLY GLY B . n 
B 2 111 PHE 111 4362 4362 PHE PHE B . n 
B 2 112 THR 112 4363 4363 THR THR B . n 
B 2 113 LEU 113 4364 4364 LEU LEU B . n 
B 2 114 LYS 114 4365 4365 LYS LYS B . n 
B 2 115 ASN 115 4366 4366 ASN ASN B . n 
B 2 116 THR 116 4367 4367 THR THR B . n 
B 2 117 VAL 117 4368 4368 VAL VAL B . n 
B 2 118 CYS 118 4369 4369 CYS CYS B . n 
B 2 119 THR 119 4370 4370 THR THR B . n 
B 2 120 VAL 120 4371 4371 VAL VAL B . n 
B 2 121 CYS 121 4372 4372 CYS CYS B . n 
B 2 122 GLY 122 4373 4373 GLY GLY B . n 
B 2 123 MET 123 4374 4374 MET MET B . n 
B 2 124 TRP 124 4375 4375 TRP TRP B . n 
B 2 125 LYS 125 4376 4376 LYS LYS B . n 
B 2 126 GLY 126 4377 4377 GLY GLY B . n 
B 2 127 TYR 127 4378 4378 TYR TYR B . n 
B 2 128 GLY 128 4379 4379 GLY GLY B . n 
B 2 129 CYS 129 4380 4380 CYS CYS B . n 
B 2 130 SER 130 4381 4381 SER SER B . n 
B 2 131 CYS 131 4382 4382 CYS CYS B . n 
B 2 132 ASP 132 4383 4383 ASP ASP B . n 
B 2 133 GLN 133 4384 4384 GLN GLN B . n 
B 2 134 LEU 134 4385 ?    ?   ?   B . n 
B 2 135 ARG 135 4386 ?    ?   ?   B . n 
B 2 136 GLU 136 4387 ?    ?   ?   B . n 
B 2 137 PRO 137 4388 ?    ?   ?   B . n 
B 2 138 MET 138 4389 ?    ?   ?   B . n 
B 2 139 LEU 139 4390 ?    ?   ?   B . n 
B 2 140 GLN 140 4391 ?    ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IQS 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IQS 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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  MES   1  7201 7906 MES   MES A . 
D  4  EDO   1  7202 7907 EDO   EDO A . 
E  4  EDO   1  7203 7909 EDO   EDO A . 
F  4  EDO   1  7204 7910 EDO   EDO A . 
G  5  NA    1  7205 7914 NA    NA  A . 
H  4  EDO   1  7206 7920 EDO   EDO A . 
I  4  EDO   1  7207 7922 EDO   EDO A . 
J  4  EDO   1  7208 7924 EDO   EDO A . 
K  6  A1IQS 1  7209 8001 A1IQS LIG A . 
L  4  EDO   1  7210 8101 EDO   EDO A . 
M  4  EDO   1  7211 8301 EDO   EDO A . 
N  4  EDO   1  7212 8401 EDO   EDO A . 
O  4  EDO   1  7213 8501 EDO   EDO A . 
P  7  DMS   1  7214 8601 DMS   DMS A . 
Q  4  EDO   1  7215 8701 EDO   EDO A . 
R  8  SAM   1  7216 8801 SAM   SAM A . 
S  5  NA    1  7217 1    NA    NA  A . 
T  4  EDO   1  8201 8201 EDO   EDO B . 
U  9  ZN    1  8202 8653 ZN    ZN  B . 
V  9  ZN    1  8203 8654 ZN    ZN  B . 
W  4  EDO   1  8204 8657 EDO   EDO B . 
X  10 IMD   1  8205 8660 IMD   IMD B . 
Y  4  EDO   1  8206 8701 EDO   EDO B . 
Z  11 HOH   1  7301 93   HOH   HOH A . 
Z  11 HOH   2  7302 43   HOH   HOH A . 
Z  11 HOH   3  7303 86   HOH   HOH A . 
Z  11 HOH   4  7304 55   HOH   HOH A . 
Z  11 HOH   5  7305 63   HOH   HOH A . 
Z  11 HOH   6  7306 66   HOH   HOH A . 
Z  11 HOH   7  7307 88   HOH   HOH A . 
Z  11 HOH   8  7308 13   HOH   HOH A . 
Z  11 HOH   9  7309 50   HOH   HOH A . 
Z  11 HOH   10 7310 25   HOH   HOH A . 
Z  11 HOH   11 7311 53   HOH   HOH A . 
Z  11 HOH   12 7312 36   HOH   HOH A . 
Z  11 HOH   13 7313 32   HOH   HOH A . 
Z  11 HOH   14 7314 3    HOH   HOH A . 
Z  11 HOH   15 7315 59   HOH   HOH A . 
Z  11 HOH   16 7316 61   HOH   HOH A . 
Z  11 HOH   17 7317 12   HOH   HOH A . 
Z  11 HOH   18 7318 60   HOH   HOH A . 
Z  11 HOH   19 7319 56   HOH   HOH A . 
Z  11 HOH   20 7320 14   HOH   HOH A . 
Z  11 HOH   21 7321 94   HOH   HOH A . 
Z  11 HOH   22 7322 107  HOH   HOH A . 
Z  11 HOH   23 7323 40   HOH   HOH A . 
Z  11 HOH   24 7324 115  HOH   HOH A . 
Z  11 HOH   25 7325 16   HOH   HOH A . 
Z  11 HOH   26 7326 21   HOH   HOH A . 
Z  11 HOH   27 7327 2    HOH   HOH A . 
Z  11 HOH   28 7328 54   HOH   HOH A . 
Z  11 HOH   29 7329 11   HOH   HOH A . 
Z  11 HOH   30 7330 47   HOH   HOH A . 
Z  11 HOH   31 7331 42   HOH   HOH A . 
Z  11 HOH   32 7332 1    HOH   HOH A . 
Z  11 HOH   33 7333 39   HOH   HOH A . 
Z  11 HOH   34 7334 87   HOH   HOH A . 
Z  11 HOH   35 7335 49   HOH   HOH A . 
Z  11 HOH   36 7336 22   HOH   HOH A . 
Z  11 HOH   37 7337 5    HOH   HOH A . 
Z  11 HOH   38 7338 44   HOH   HOH A . 
Z  11 HOH   39 7339 58   HOH   HOH A . 
Z  11 HOH   40 7340 79   HOH   HOH A . 
Z  11 HOH   41 7341 8    HOH   HOH A . 
Z  11 HOH   42 7342 34   HOH   HOH A . 
Z  11 HOH   43 7343 45   HOH   HOH A . 
Z  11 HOH   44 7344 35   HOH   HOH A . 
Z  11 HOH   45 7345 82   HOH   HOH A . 
Z  11 HOH   46 7346 64   HOH   HOH A . 
Z  11 HOH   47 7347 18   HOH   HOH A . 
Z  11 HOH   48 7348 7    HOH   HOH A . 
Z  11 HOH   49 7349 28   HOH   HOH A . 
Z  11 HOH   50 7350 6    HOH   HOH A . 
Z  11 HOH   51 7351 17   HOH   HOH A . 
Z  11 HOH   52 7352 83   HOH   HOH A . 
Z  11 HOH   53 7353 72   HOH   HOH A . 
Z  11 HOH   54 7354 70   HOH   HOH A . 
Z  11 HOH   55 7355 98   HOH   HOH A . 
Z  11 HOH   56 7356 19   HOH   HOH A . 
Z  11 HOH   57 7357 92   HOH   HOH A . 
Z  11 HOH   58 7358 62   HOH   HOH A . 
Z  11 HOH   59 7359 81   HOH   HOH A . 
Z  11 HOH   60 7360 15   HOH   HOH A . 
Z  11 HOH   61 7361 68   HOH   HOH A . 
Z  11 HOH   62 7362 78   HOH   HOH A . 
Z  11 HOH   63 7363 90   HOH   HOH A . 
Z  11 HOH   64 7364 74   HOH   HOH A . 
Z  11 HOH   65 7365 69   HOH   HOH A . 
Z  11 HOH   66 7366 65   HOH   HOH A . 
Z  11 HOH   67 7367 114  HOH   HOH A . 
Z  11 HOH   68 7368 30   HOH   HOH A . 
Z  11 HOH   69 7369 4    HOH   HOH A . 
Z  11 HOH   70 7370 31   HOH   HOH A . 
Z  11 HOH   71 7371 52   HOH   HOH A . 
Z  11 HOH   72 7372 80   HOH   HOH A . 
Z  11 HOH   73 7373 108  HOH   HOH A . 
Z  11 HOH   74 7374 85   HOH   HOH A . 
Z  11 HOH   75 7375 96   HOH   HOH A . 
Z  11 HOH   76 7376 37   HOH   HOH A . 
Z  11 HOH   77 7377 27   HOH   HOH A . 
Z  11 HOH   78 7378 46   HOH   HOH A . 
Z  11 HOH   79 7379 71   HOH   HOH A . 
Z  11 HOH   80 7380 97   HOH   HOH A . 
Z  11 HOH   81 7381 110  HOH   HOH A . 
Z  11 HOH   82 7382 51   HOH   HOH A . 
Z  11 HOH   83 7383 95   HOH   HOH A . 
Z  11 HOH   84 7384 112  HOH   HOH A . 
Z  11 HOH   85 7385 91   HOH   HOH A . 
Z  11 HOH   86 7386 113  HOH   HOH A . 
Z  11 HOH   87 7387 99   HOH   HOH A . 
Z  11 HOH   88 7388 106  HOH   HOH A . 
Z  11 HOH   89 7389 104  HOH   HOH A . 
AA 11 HOH   1  8301 48   HOH   HOH B . 
AA 11 HOH   2  8302 10   HOH   HOH B . 
AA 11 HOH   3  8303 111  HOH   HOH B . 
AA 11 HOH   4  8304 38   HOH   HOH B . 
AA 11 HOH   5  8305 75   HOH   HOH B . 
AA 11 HOH   6  8306 100  HOH   HOH B . 
AA 11 HOH   7  8307 41   HOH   HOH B . 
AA 11 HOH   8  8308 77   HOH   HOH B . 
AA 11 HOH   9  8309 73   HOH   HOH B . 
AA 11 HOH   10 8310 57   HOH   HOH B . 
AA 11 HOH   11 8311 89   HOH   HOH B . 
AA 11 HOH   12 8312 24   HOH   HOH B . 
AA 11 HOH   13 8313 26   HOH   HOH B . 
AA 11 HOH   14 8314 105  HOH   HOH B . 
AA 11 HOH   15 8315 67   HOH   HOH B . 
AA 11 HOH   16 8316 20   HOH   HOH B . 
AA 11 HOH   17 8317 101  HOH   HOH B . 
AA 11 HOH   18 8318 109  HOH   HOH B . 
AA 11 HOH   19 8319 9    HOH   HOH B . 
AA 11 HOH   20 8320 103  HOH   HOH B . 
AA 11 HOH   21 8321 102  HOH   HOH B . 
# 
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 reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? BUILT=20210205 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? BUILT=20210205 2 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21.1-5286    3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? 0.8.9.1        4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21.1-5286    5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GWO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     168.080 
_cell.length_a_esd                 ? 
_cell.length_b                     168.080 
_cell.length_b_esd                 ? 
_cell.length_c                     51.720 
_cell.length_c_esd                 ? 
_cell.volume                       1265380.760 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9GWO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            
;P 31 2"
;
_symmetry.space_group_name_H-M             'P 31 2 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                   9GWO 
_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             4.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          71.42 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    '400 mM sodium fluoride, 100 mM 2-(N-morpholino)ethanesulfonic acid' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_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 EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-08-21 
_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   1.033220 
_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                        'PETRA III, DESY BEAMLINE P11' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.033220 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   P11 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, DESY' 
# 
_reflns.B_iso_Wilson_estimate                          36.66 
_reflns.entry_id                                       9GWO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.0 
_reflns.d_resolution_low                               48.74 
_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                                     56567 
_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                           99.76 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.85 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.1653 
_reflns.pdbx_Rpim_I_all                                0.04894 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1578 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.0 
_reflns_shell.d_res_low                                     2.072 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.89 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5625 
_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                               11.7 
_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                               1.967 
_reflns_shell.pdbx_Rpim_I_all                               0.5755 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.574 
_reflns_shell.pdbx_CC_star                                  0.854 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.00 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.88 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               42.70 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GWO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.00 
_refine.ls_d_res_low                             48.74 
_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                     56561 
_refine.ls_number_reflns_R_free                  1997 
_refine.ls_number_reflns_R_work                  54564 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.76 
_refine.ls_percent_reflns_R_free                 3.53 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1886 
_refine.ls_R_factor_R_free                       0.2030 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1889 
_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                          1.56 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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                 20.5305 
_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                            0.2395 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        48.74 
_refine_hist.number_atoms_solvent             110 
_refine_hist.number_atoms_total               3459 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3204 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         145 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0078  ? 3420 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8957  ? 4619 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0595  ? 508  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0064  ? 612  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.7793 ? 1263 ? f_dihedral_angle_d ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.00 
_refine_ls_shell.d_res_low                        2.05 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             143 
_refine_ls_shell.number_reflns_R_work             5625 
_refine_ls_shell.percent_reflns_obs               100.00 
_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                  0.3050 
_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                  0.3218 
# 
_struct.entry_id                     9GWO 
_struct.title                        
'SARS-CoV-2 methyltransferase nsp10-16 in complex with SAM and theophylline derivative LAS 54571126' 
_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        9GWO 
_struct_keywords.text            'methyltransferase, complex, inhibitor, viral protein' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1  ? 
B  N N 2  ? 
C  N N 3  ? 
D  N N 4  ? 
E  N N 4  ? 
F  N N 4  ? 
G  N N 5  ? 
H  N N 4  ? 
I  N N 4  ? 
J  N N 4  ? 
K  N N 6  ? 
L  N N 4  ? 
M  N N 4  ? 
N  N N 4  ? 
O  N N 4  ? 
P  N N 7  ? 
Q  N N 4  ? 
R  N N 8  ? 
S  N N 5  ? 
T  N N 4  ? 
U  N N 9  ? 
V  N N 9  ? 
W  N N 4  ? 
X  N N 10 ? 
Y  N N 4  ? 
Z  N N 11 ? 
AA N N 11 ? 
# 
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 R1AB_SARS2 P0DTD1 ? 1 
;SSQAWQPGVAMPNLYKMQRMLLEKCDLQNYGDSATLPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAP
GTAVLRQWLPTGTLLVDSDLNDFVSDADSTLIGDCATVHTANKWDLIISDMYDPKTKNVTKENDSKEGFFTYICGFIQQK
LALGGSVAIKITEHSWNADLYKLMGHFAWWTAFVTNVNASSSEAFLIGCNYLGKPREQIDGYVMHANYIFWRNTNPIQLS
SYSLFDMSKFPLKLRGTAVMSLKEGQINDMILSLLSKGRLIIRENNRVVISSDVLVNN
;
6799 
2 UNP R1AB_SARS2 P0DTD1 ? 2 
;AGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCH
IDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQ
;
4254 
# 
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 9GWO A 1 ? 298 ? P0DTD1 6799 ? 7096 ? 6799 7096 
2 2 9GWO B 2 ? 140 ? P0DTD1 4254 ? 4392 ? 4253 4391 
# 
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 9GWO GLU A 299 ? UNP P0DTD1 ? ? 'expression tag' 7097 1 
1 9GWO ASN A 300 ? UNP P0DTD1 ? ? 'expression tag' 7098 2 
1 9GWO LEU A 301 ? UNP P0DTD1 ? ? 'expression tag' 7099 3 
1 9GWO TYR A 302 ? UNP P0DTD1 ? ? 'expression tag' 7100 4 
1 9GWO PHE A 303 ? UNP P0DTD1 ? ? 'expression tag' 7101 5 
1 9GWO GLN A 304 ? UNP P0DTD1 ? ? 'expression tag' 7102 6 
2 9GWO GLY B 1   ? UNP P0DTD1 ? ? 'expression tag' 4252 7 
# 
_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)' 4480  ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  21080 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 1   ? GLN A 6   ? SER A 6799 GLN A 6804 5 ? 6  
HELX_P HELX_P2  AA2 PRO A 12  ? MET A 17  ? PRO A 6810 MET A 6815 1 ? 6  
HELX_P HELX_P3  AA3 MET A 41  ? ASN A 55  ? MET A 6839 ASN A 6853 1 ? 15 
HELX_P HELX_P4  AA4 ALA A 79  ? LEU A 89  ? ALA A 6877 LEU A 6887 1 ? 11 
HELX_P HELX_P5  AA5 ASP A 114 ? ALA A 116 ? ASP A 6912 ALA A 6914 5 ? 3  
HELX_P HELX_P6  AA6 ASP A 133 ? LYS A 137 ? ASP A 6931 LYS A 6935 5 ? 5  
HELX_P HELX_P7  AA7 GLY A 148 ? LYS A 160 ? GLY A 6946 LYS A 6958 1 ? 13 
HELX_P HELX_P8  AA8 ASN A 177 ? GLY A 185 ? ASN A 6975 GLY A 6983 1 ? 9  
HELX_P HELX_P9  AA9 VAL A 197 ? ALA A 199 ? VAL A 6995 ALA A 6997 5 ? 3  
HELX_P HELX_P10 AB1 ASP A 220 ? ASN A 235 ? ASP A 7018 ASN A 7033 1 ? 16 
HELX_P HELX_P11 AB2 SER A 241 ? ASP A 246 ? SER A 7039 ASP A 7044 5 ? 6  
HELX_P HELX_P12 AB3 LYS A 263 ? ILE A 267 ? LYS A 7061 ILE A 7065 5 ? 5  
HELX_P HELX_P13 AB4 ASN A 268 ? LYS A 277 ? ASN A 7066 LYS A 7075 1 ? 10 
HELX_P HELX_P14 AB5 ASP B 23  ? SER B 34  ? ASP B 4274 SER B 4285 1 ? 12 
HELX_P HELX_P15 AB6 ALA B 72  ? CYS B 74  ? ALA B 4323 CYS B 4325 5 ? 3  
HELX_P HELX_P16 AB7 CYS B 75  ? HIS B 81  ? CYS B 4326 HIS B 4332 1 ? 7  
HELX_P HELX_P17 AB8 THR B 103 ? ALA B 105 ? THR B 4354 ALA B 4356 5 ? 3  
HELX_P HELX_P18 AB9 ASP B 107 ? ASN B 115 ? ASP B 4358 ASN B 4366 1 ? 9  
# 
_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 ? ? A ALA 60  O   ? ? ? 1_555 G NA  . NA ? ? A ALA 6858 A NA  7205 1_555 ? ? ? ? ? ? ? 2.931 ? ? 
metalc2  metalc ? ? A ASP 125 O   ? ? ? 1_555 G NA  . NA ? ? A ASP 6923 A NA  7205 1_555 ? ? ? ? ? ? ? 2.825 ? ? 
metalc3  metalc ? ? A TYR 132 OH  ? ? ? 1_555 S NA  . NA ? ? A TYR 6930 A NA  7217 1_555 ? ? ? ? ? ? ? 2.783 ? ? 
metalc4  metalc ? ? A THR 172 OG1 ? ? ? 1_555 S NA  . NA ? ? A THR 6970 A NA  7217 1_555 ? ? ? ? ? ? ? 2.757 ? ? 
metalc5  metalc ? ? G NA  .   NA  ? ? ? 1_555 Z HOH . O  ? ? A NA  7205 A HOH 7325 1_555 ? ? ? ? ? ? ? 2.607 ? ? 
metalc6  metalc ? ? S NA  .   NA  ? ? ? 1_555 Z HOH . O  ? ? A NA  7217 A HOH 7371 1_555 ? ? ? ? ? ? ? 2.193 ? ? 
metalc7  metalc ? ? B CYS 75  SG  ? ? ? 1_555 U ZN  . ZN ? ? B CYS 4326 B ZN  8202 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc8  metalc ? ? B CYS 78  SG  ? ? ? 1_555 U ZN  . ZN ? ? B CYS 4329 B ZN  8202 1_555 ? ? ? ? ? ? ? 2.279 ? ? 
metalc9  metalc ? ? B HIS 84  NE2 ? ? ? 1_555 U ZN  . ZN ? ? B HIS 4335 B ZN  8202 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
metalc10 metalc ? ? B CYS 91  SG  ? ? ? 1_555 U ZN  . ZN ? ? B CYS 4342 B ZN  8202 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
metalc11 metalc ? ? B CYS 118 SG  ? ? ? 1_555 V ZN  . ZN ? ? B CYS 4369 B ZN  8203 1_555 ? ? ? ? ? ? ? 2.299 ? ? 
metalc12 metalc ? ? B CYS 121 SG  ? ? ? 1_555 V ZN  . ZN ? ? B CYS 4372 B ZN  8203 1_555 ? ? ? ? ? ? ? 2.497 ? ? 
metalc13 metalc ? ? B CYS 129 SG  ? ? ? 1_555 V ZN  . ZN ? ? B CYS 4380 B ZN  8203 1_555 ? ? ? ? ? ? ? 2.203 ? ? 
metalc14 metalc ? ? B CYS 131 SG  ? ? ? 1_555 V ZN  . ZN ? ? B CYS 4382 B ZN  8203 1_555 ? ? ? ? ? ? ? 2.616 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A ALA 60  ? A ALA 6858 ? 1_555 NA ? G NA . ? A NA 7205 ? 1_555 O   ? A ASP 125 ? A ASP 6923 ? 1_555 133.4 ? 
2  O   ? A ALA 60  ? A ALA 6858 ? 1_555 NA ? G NA . ? A NA 7205 ? 1_555 O   ? Z HOH .   ? A HOH 7325 ? 1_555 95.8  ? 
3  O   ? A ASP 125 ? A ASP 6923 ? 1_555 NA ? G NA . ? A NA 7205 ? 1_555 O   ? Z HOH .   ? A HOH 7325 ? 1_555 107.3 ? 
4  OH  ? A TYR 132 ? A TYR 6930 ? 1_555 NA ? S NA . ? A NA 7217 ? 1_555 OG1 ? A THR 172 ? A THR 6970 ? 1_555 110.2 ? 
5  OH  ? A TYR 132 ? A TYR 6930 ? 1_555 NA ? S NA . ? A NA 7217 ? 1_555 O   ? Z HOH .   ? A HOH 7371 ? 1_555 137.7 ? 
6  OG1 ? A THR 172 ? A THR 6970 ? 1_555 NA ? S NA . ? A NA 7217 ? 1_555 O   ? Z HOH .   ? A HOH 7371 ? 1_555 77.6  ? 
7  SG  ? B CYS 75  ? B CYS 4326 ? 1_555 ZN ? U ZN . ? B ZN 8202 ? 1_555 SG  ? B CYS 78  ? B CYS 4329 ? 1_555 116.0 ? 
8  SG  ? B CYS 75  ? B CYS 4326 ? 1_555 ZN ? U ZN . ? B ZN 8202 ? 1_555 NE2 ? B HIS 84  ? B HIS 4335 ? 1_555 104.6 ? 
9  SG  ? B CYS 78  ? B CYS 4329 ? 1_555 ZN ? U ZN . ? B ZN 8202 ? 1_555 NE2 ? B HIS 84  ? B HIS 4335 ? 1_555 109.1 ? 
10 SG  ? B CYS 75  ? B CYS 4326 ? 1_555 ZN ? U ZN . ? B ZN 8202 ? 1_555 SG  ? B CYS 91  ? B CYS 4342 ? 1_555 111.2 ? 
11 SG  ? B CYS 78  ? B CYS 4329 ? 1_555 ZN ? U ZN . ? B ZN 8202 ? 1_555 SG  ? B CYS 91  ? B CYS 4342 ? 1_555 115.7 ? 
12 NE2 ? B HIS 84  ? B HIS 4335 ? 1_555 ZN ? U ZN . ? B ZN 8202 ? 1_555 SG  ? B CYS 91  ? B CYS 4342 ? 1_555 98.1  ? 
13 SG  ? B CYS 118 ? B CYS 4369 ? 1_555 ZN ? V ZN . ? B ZN 8203 ? 1_555 SG  ? B CYS 121 ? B CYS 4372 ? 1_555 101.8 ? 
14 SG  ? B CYS 118 ? B CYS 4369 ? 1_555 ZN ? V ZN . ? B ZN 8203 ? 1_555 SG  ? B CYS 129 ? B CYS 4380 ? 1_555 113.6 ? 
15 SG  ? B CYS 121 ? B CYS 4372 ? 1_555 ZN ? V ZN . ? B ZN 8203 ? 1_555 SG  ? B CYS 129 ? B CYS 4380 ? 1_555 113.0 ? 
16 SG  ? B CYS 118 ? B CYS 4369 ? 1_555 ZN ? V ZN . ? B ZN 8203 ? 1_555 SG  ? B CYS 131 ? B CYS 4382 ? 1_555 111.7 ? 
17 SG  ? B CYS 121 ? B CYS 4372 ? 1_555 ZN ? V ZN . ? B ZN 8203 ? 1_555 SG  ? B CYS 131 ? B CYS 4382 ? 1_555 102.3 ? 
18 SG  ? B CYS 129 ? B CYS 4380 ? 1_555 ZN ? V ZN . ? B ZN 8203 ? 1_555 SG  ? B CYS 131 ? B CYS 4382 ? 1_555 113.4 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY A 8   ? ALA A 10  ? GLY A 6806 ALA A 6808 
AA1 2 PHE A 187 ? THR A 195 ? PHE A 6985 THR A 6993 
AA1 3 ALA A 204 ? TYR A 211 ? ALA A 7002 TYR A 7009 
AA1 4 LEU A 161 ? ILE A 171 ? LEU A 6959 ILE A 6969 
AA1 5 TRP A 124 ? SER A 129 ? TRP A 6922 SER A 6927 
AA1 6 ARG A 66  ? PHE A 70  ? ARG A 6864 PHE A 6868 
AA1 7 LEU A 94  ? ASP A 99  ? LEU A 6892 ASP A 6897 
AA1 8 SER A 109 ? ILE A 112 ? SER A 6907 ILE A 6910 
AA2 1 VAL A 118 ? THR A 120 ? VAL A 6916 THR A 6918 
AA2 2 ILE A 290 ? SER A 292 ? ILE A 7088 SER A 7090 
AA3 1 ALA A 258 ? MET A 260 ? ALA A 7056 MET A 7058 
AA3 2 LEU A 280 ? ILE A 282 ? LEU A 7078 ILE A 7080 
AA4 1 ILE B 56  ? THR B 57  ? ILE B 4307 THR B 4308 
AA4 2 TYR B 97  ? PRO B 101 ? TYR B 4348 PRO B 4352 
AA4 3 GLN B 66  ? GLY B 70  ? GLN B 4317 GLY B 4321 
# 
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 VAL A 9   ? N VAL A 6807 O VAL A 194 ? O VAL A 6992 
AA1 2 3 N TRP A 189 ? N TRP A 6987 O CYS A 209 ? O CYS A 7007 
AA1 3 4 O LEU A 206 ? O LEU A 7004 N ILE A 169 ? N ILE A 6967 
AA1 4 5 O ALA A 162 ? O ALA A 6960 N TRP A 124 ? N TRP A 6922 
AA1 5 6 O ILE A 128 ? O ILE A 6926 N PHE A 70  ? N PHE A 6868 
AA1 6 7 N VAL A 67  ? N VAL A 6865 O LEU A 94  ? O LEU A 6892 
AA1 7 8 N ASP A 97  ? N ASP A 6895 O LEU A 111 ? O LEU A 6909 
AA2 1 2 N HIS A 119 ? N HIS A 6917 O SER A 291 ? O SER A 7089 
AA3 1 2 N ALA A 258 ? N ALA A 7056 O ILE A 281 ? O ILE A 7079 
AA4 1 2 N THR B 57  ? N THR B 4308 O TYR B 97  ? O TYR B 4348 
AA4 2 3 O ILE B 100 ? O ILE B 4351 N GLU B 67  ? N GLU B 4318 
# 
_pdbx_entry_details.entry_id                   9GWO 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    7355 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    7389 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.85 
# 
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 LYS A 6935 ? ? -76.63  36.51   
2 1 GLU A 6945 ? ? -101.33 -112.14 
3 1 ASN A 7008 ? ? 69.59   92.42   
4 1 ASN A 7084 ? ? -68.72  -168.47 
5 1 ASP B 4358 ? ? -151.76 71.06   
6 1 TYR B 4378 ? ? -142.57 47.70   
7 1 CYS B 4382 ? ? -67.51  4.13    
# 
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 LEU 7099 ? A LEU 301 
2  1 Y 1 A TYR 7100 ? A TYR 302 
3  1 Y 1 A PHE 7101 ? A PHE 303 
4  1 Y 1 A GLN 7102 ? A GLN 304 
5  1 Y 1 B GLY 4252 ? B GLY 1   
6  1 Y 1 B ALA 4253 ? B ALA 2   
7  1 Y 1 B GLY 4254 ? B GLY 3   
8  1 Y 1 B ASN 4255 ? B ASN 4   
9  1 Y 1 B ALA 4256 ? B ALA 5   
10 1 Y 1 B THR 4257 ? B THR 6   
11 1 Y 1 B GLU 4258 ? B GLU 7   
12 1 Y 1 B VAL 4259 ? B VAL 8   
13 1 Y 1 B PRO 4260 ? B PRO 9   
14 1 Y 1 B ALA 4261 ? B ALA 10  
15 1 Y 1 B ASN 4262 ? B ASN 11  
16 1 Y 1 B SER 4263 ? B SER 12  
17 1 Y 1 B THR 4264 ? B THR 13  
18 1 Y 1 B VAL 4265 ? B VAL 14  
19 1 Y 1 B LEU 4266 ? B LEU 15  
20 1 Y 1 B SER 4267 ? B SER 16  
21 1 Y 1 B PHE 4268 ? B PHE 17  
22 1 Y 1 B CYS 4269 ? B CYS 18  
23 1 Y 1 B LEU 4385 ? B LEU 134 
24 1 Y 1 B ARG 4386 ? B ARG 135 
25 1 Y 1 B GLU 4387 ? B GLU 136 
26 1 Y 1 B PRO 4388 ? B PRO 137 
27 1 Y 1 B MET 4389 ? B MET 138 
28 1 Y 1 B LEU 4390 ? B LEU 139 
29 1 Y 1 B GLN 4391 ? B GLN 140 
# 
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 
A1IQS N1     N  Y N 1   
A1IQS N3     N  N N 2   
A1IQS C4     C  Y N 3   
A1IQS C5     C  N N 4   
A1IQS C6     C  N S 5   
A1IQS C7     C  N S 6   
A1IQS C8     C  N N 7   
A1IQS C10    C  N N 8   
A1IQS C13    C  N N 9   
A1IQS C15    C  Y N 10  
A1IQS C17    C  Y N 11  
A1IQS C20    C  Y N 12  
A1IQS C21    C  Y N 13  
A1IQS C22    C  N N 14  
A1IQS C24    C  N N 15  
A1IQS N      N  N N 16  
A1IQS C      C  N N 17  
A1IQS O      O  N N 18  
A1IQS C1     C  N N 19  
A1IQS C11    C  N N 20  
A1IQS C12    C  N S 21  
A1IQS C14    C  Y N 22  
A1IQS C16    C  Y N 23  
A1IQS C18    C  Y N 24  
A1IQS C19    C  Y N 25  
A1IQS C2     C  Y N 26  
A1IQS C23    C  N N 27  
A1IQS C3     C  Y N 28  
A1IQS C9     C  N R 29  
A1IQS N2     N  Y N 30  
A1IQS N4     N  N N 31  
A1IQS N5     N  N N 32  
A1IQS N6     N  Y N 33  
A1IQS O1     O  N N 34  
A1IQS O2     O  N N 35  
A1IQS O3     O  N N 36  
A1IQS O4     O  N N 37  
A1IQS H6     H  N N 38  
A1IQS H5     H  N N 39  
A1IQS H4     H  N N 40  
A1IQS H      H  N N 41  
A1IQS H8     H  N N 42  
A1IQS H9     H  N N 43  
A1IQS H12    H  N N 44  
A1IQS H11    H  N N 45  
A1IQS H15    H  N N 46  
A1IQS H16    H  N N 47  
A1IQS H18    H  N N 48  
A1IQS H21    H  N N 49  
A1IQS H22    H  N N 50  
A1IQS H23    H  N N 51  
A1IQS H24    H  N N 52  
A1IQS H28    H  N N 53  
A1IQS H30    H  N N 54  
A1IQS H29    H  N N 55  
A1IQS H2     H  N N 56  
A1IQS H19    H  N N 57  
A1IQS H20    H  N N 58  
A1IQS H25    H  N N 59  
A1IQS H27    H  N N 60  
A1IQS H26    H  N N 61  
A1IQS H3     H  N N 62  
A1IQS H1     H  N N 63  
A1IQS H13    H  N N 64  
A1IQS H14    H  N N 65  
A1IQS H17    H  N N 66  
A1IQS H7     H  N N 67  
A1IQS H10    H  N N 68  
ALA   N      N  N N 69  
ALA   CA     C  N S 70  
ALA   C      C  N N 71  
ALA   O      O  N N 72  
ALA   CB     C  N N 73  
ALA   OXT    O  N N 74  
ALA   H      H  N N 75  
ALA   H2     H  N N 76  
ALA   HA     H  N N 77  
ALA   HB1    H  N N 78  
ALA   HB2    H  N N 79  
ALA   HB3    H  N N 80  
ALA   HXT    H  N N 81  
ARG   N      N  N N 82  
ARG   CA     C  N S 83  
ARG   C      C  N N 84  
ARG   O      O  N N 85  
ARG   CB     C  N N 86  
ARG   CG     C  N N 87  
ARG   CD     C  N N 88  
ARG   NE     N  N N 89  
ARG   CZ     C  N N 90  
ARG   NH1    N  N N 91  
ARG   NH2    N  N N 92  
ARG   OXT    O  N N 93  
ARG   H      H  N N 94  
ARG   H2     H  N N 95  
ARG   HA     H  N N 96  
ARG   HB2    H  N N 97  
ARG   HB3    H  N N 98  
ARG   HG2    H  N N 99  
ARG   HG3    H  N N 100 
ARG   HD2    H  N N 101 
ARG   HD3    H  N N 102 
ARG   HE     H  N N 103 
ARG   HH11   H  N N 104 
ARG   HH12   H  N N 105 
ARG   HH21   H  N N 106 
ARG   HH22   H  N N 107 
ARG   HXT    H  N N 108 
ASN   N      N  N N 109 
ASN   CA     C  N S 110 
ASN   C      C  N N 111 
ASN   O      O  N N 112 
ASN   CB     C  N N 113 
ASN   CG     C  N N 114 
ASN   OD1    O  N N 115 
ASN   ND2    N  N N 116 
ASN   OXT    O  N N 117 
ASN   H      H  N N 118 
ASN   H2     H  N N 119 
ASN   HA     H  N N 120 
ASN   HB2    H  N N 121 
ASN   HB3    H  N N 122 
ASN   HD21   H  N N 123 
ASN   HD22   H  N N 124 
ASN   HXT    H  N N 125 
ASP   N      N  N N 126 
ASP   CA     C  N S 127 
ASP   C      C  N N 128 
ASP   O      O  N N 129 
ASP   CB     C  N N 130 
ASP   CG     C  N N 131 
ASP   OD1    O  N N 132 
ASP   OD2    O  N N 133 
ASP   OXT    O  N N 134 
ASP   H      H  N N 135 
ASP   H2     H  N N 136 
ASP   HA     H  N N 137 
ASP   HB2    H  N N 138 
ASP   HB3    H  N N 139 
ASP   HD2    H  N N 140 
ASP   HXT    H  N N 141 
CYS   N      N  N N 142 
CYS   CA     C  N R 143 
CYS   C      C  N N 144 
CYS   O      O  N N 145 
CYS   CB     C  N N 146 
CYS   SG     S  N N 147 
CYS   OXT    O  N N 148 
CYS   H      H  N N 149 
CYS   H2     H  N N 150 
CYS   HA     H  N N 151 
CYS   HB2    H  N N 152 
CYS   HB3    H  N N 153 
CYS   HG     H  N N 154 
CYS   HXT    H  N N 155 
DMS   S      S  N N 156 
DMS   O      O  N N 157 
DMS   C1     C  N N 158 
DMS   C2     C  N N 159 
DMS   H11    H  N N 160 
DMS   H12    H  N N 161 
DMS   H13    H  N N 162 
DMS   H21    H  N N 163 
DMS   H22    H  N N 164 
DMS   H23    H  N N 165 
EDO   C1     C  N N 166 
EDO   O1     O  N N 167 
EDO   C2     C  N N 168 
EDO   O2     O  N N 169 
EDO   H11    H  N N 170 
EDO   H12    H  N N 171 
EDO   HO1    H  N N 172 
EDO   H21    H  N N 173 
EDO   H22    H  N N 174 
EDO   HO2    H  N N 175 
GLN   N      N  N N 176 
GLN   CA     C  N S 177 
GLN   C      C  N N 178 
GLN   O      O  N N 179 
GLN   CB     C  N N 180 
GLN   CG     C  N N 181 
GLN   CD     C  N N 182 
GLN   OE1    O  N N 183 
GLN   NE2    N  N N 184 
GLN   OXT    O  N N 185 
GLN   H      H  N N 186 
GLN   H2     H  N N 187 
GLN   HA     H  N N 188 
GLN   HB2    H  N N 189 
GLN   HB3    H  N N 190 
GLN   HG2    H  N N 191 
GLN   HG3    H  N N 192 
GLN   HE21   H  N N 193 
GLN   HE22   H  N N 194 
GLN   HXT    H  N N 195 
GLU   N      N  N N 196 
GLU   CA     C  N S 197 
GLU   C      C  N N 198 
GLU   O      O  N N 199 
GLU   CB     C  N N 200 
GLU   CG     C  N N 201 
GLU   CD     C  N N 202 
GLU   OE1    O  N N 203 
GLU   OE2    O  N N 204 
GLU   OXT    O  N N 205 
GLU   H      H  N N 206 
GLU   H2     H  N N 207 
GLU   HA     H  N N 208 
GLU   HB2    H  N N 209 
GLU   HB3    H  N N 210 
GLU   HG2    H  N N 211 
GLU   HG3    H  N N 212 
GLU   HE2    H  N N 213 
GLU   HXT    H  N N 214 
GLY   N      N  N N 215 
GLY   CA     C  N N 216 
GLY   C      C  N N 217 
GLY   O      O  N N 218 
GLY   OXT    O  N N 219 
GLY   H      H  N N 220 
GLY   H2     H  N N 221 
GLY   HA2    H  N N 222 
GLY   HA3    H  N N 223 
GLY   HXT    H  N N 224 
HIS   N      N  N N 225 
HIS   CA     C  N S 226 
HIS   C      C  N N 227 
HIS   O      O  N N 228 
HIS   CB     C  N N 229 
HIS   CG     C  Y N 230 
HIS   ND1    N  Y N 231 
HIS   CD2    C  Y N 232 
HIS   CE1    C  Y N 233 
HIS   NE2    N  Y N 234 
HIS   OXT    O  N N 235 
HIS   H      H  N N 236 
HIS   H2     H  N N 237 
HIS   HA     H  N N 238 
HIS   HB2    H  N N 239 
HIS   HB3    H  N N 240 
HIS   HD1    H  N N 241 
HIS   HD2    H  N N 242 
HIS   HE1    H  N N 243 
HIS   HE2    H  N N 244 
HIS   HXT    H  N N 245 
HOH   O      O  N N 246 
HOH   H1     H  N N 247 
HOH   H2     H  N N 248 
ILE   N      N  N N 249 
ILE   CA     C  N S 250 
ILE   C      C  N N 251 
ILE   O      O  N N 252 
ILE   CB     C  N S 253 
ILE   CG1    C  N N 254 
ILE   CG2    C  N N 255 
ILE   CD1    C  N N 256 
ILE   OXT    O  N N 257 
ILE   H      H  N N 258 
ILE   H2     H  N N 259 
ILE   HA     H  N N 260 
ILE   HB     H  N N 261 
ILE   HG12   H  N N 262 
ILE   HG13   H  N N 263 
ILE   HG21   H  N N 264 
ILE   HG22   H  N N 265 
ILE   HG23   H  N N 266 
ILE   HD11   H  N N 267 
ILE   HD12   H  N N 268 
ILE   HD13   H  N N 269 
ILE   HXT    H  N N 270 
IMD   N1     N  Y N 271 
IMD   C2     C  Y N 272 
IMD   N3     N  Y N 273 
IMD   C4     C  Y N 274 
IMD   C5     C  Y N 275 
IMD   HN1    H  N N 276 
IMD   H2     H  N N 277 
IMD   HN3    H  N N 278 
IMD   H4     H  N N 279 
IMD   H5     H  N N 280 
LEU   N      N  N N 281 
LEU   CA     C  N S 282 
LEU   C      C  N N 283 
LEU   O      O  N N 284 
LEU   CB     C  N N 285 
LEU   CG     C  N N 286 
LEU   CD1    C  N N 287 
LEU   CD2    C  N N 288 
LEU   OXT    O  N N 289 
LEU   H      H  N N 290 
LEU   H2     H  N N 291 
LEU   HA     H  N N 292 
LEU   HB2    H  N N 293 
LEU   HB3    H  N N 294 
LEU   HG     H  N N 295 
LEU   HD11   H  N N 296 
LEU   HD12   H  N N 297 
LEU   HD13   H  N N 298 
LEU   HD21   H  N N 299 
LEU   HD22   H  N N 300 
LEU   HD23   H  N N 301 
LEU   HXT    H  N N 302 
LYS   N      N  N N 303 
LYS   CA     C  N S 304 
LYS   C      C  N N 305 
LYS   O      O  N N 306 
LYS   CB     C  N N 307 
LYS   CG     C  N N 308 
LYS   CD     C  N N 309 
LYS   CE     C  N N 310 
LYS   NZ     N  N N 311 
LYS   OXT    O  N N 312 
LYS   H      H  N N 313 
LYS   H2     H  N N 314 
LYS   HA     H  N N 315 
LYS   HB2    H  N N 316 
LYS   HB3    H  N N 317 
LYS   HG2    H  N N 318 
LYS   HG3    H  N N 319 
LYS   HD2    H  N N 320 
LYS   HD3    H  N N 321 
LYS   HE2    H  N N 322 
LYS   HE3    H  N N 323 
LYS   HZ1    H  N N 324 
LYS   HZ2    H  N N 325 
LYS   HZ3    H  N N 326 
LYS   HXT    H  N N 327 
MES   O1     O  N N 328 
MES   C2     C  N N 329 
MES   C3     C  N N 330 
MES   N4     N  N N 331 
MES   C5     C  N N 332 
MES   C6     C  N N 333 
MES   C7     C  N N 334 
MES   C8     C  N N 335 
MES   S      S  N N 336 
MES   O1S    O  N N 337 
MES   O2S    O  N N 338 
MES   O3S    O  N N 339 
MES   H21    H  N N 340 
MES   H22    H  N N 341 
MES   H31    H  N N 342 
MES   H32    H  N N 343 
MES   HN4    H  N N 344 
MES   H51    H  N N 345 
MES   H52    H  N N 346 
MES   H61    H  N N 347 
MES   H62    H  N N 348 
MES   H71    H  N N 349 
MES   H72    H  N N 350 
MES   H81    H  N N 351 
MES   H82    H  N N 352 
MET   N      N  N N 353 
MET   CA     C  N S 354 
MET   C      C  N N 355 
MET   O      O  N N 356 
MET   CB     C  N N 357 
MET   CG     C  N N 358 
MET   SD     S  N N 359 
MET   CE     C  N N 360 
MET   OXT    O  N N 361 
MET   H      H  N N 362 
MET   H2     H  N N 363 
MET   HA     H  N N 364 
MET   HB2    H  N N 365 
MET   HB3    H  N N 366 
MET   HG2    H  N N 367 
MET   HG3    H  N N 368 
MET   HE1    H  N N 369 
MET   HE2    H  N N 370 
MET   HE3    H  N N 371 
MET   HXT    H  N N 372 
NA    NA     NA N N 373 
PHE   N      N  N N 374 
PHE   CA     C  N S 375 
PHE   C      C  N N 376 
PHE   O      O  N N 377 
PHE   CB     C  N N 378 
PHE   CG     C  Y N 379 
PHE   CD1    C  Y N 380 
PHE   CD2    C  Y N 381 
PHE   CE1    C  Y N 382 
PHE   CE2    C  Y N 383 
PHE   CZ     C  Y N 384 
PHE   OXT    O  N N 385 
PHE   H      H  N N 386 
PHE   H2     H  N N 387 
PHE   HA     H  N N 388 
PHE   HB2    H  N N 389 
PHE   HB3    H  N N 390 
PHE   HD1    H  N N 391 
PHE   HD2    H  N N 392 
PHE   HE1    H  N N 393 
PHE   HE2    H  N N 394 
PHE   HZ     H  N N 395 
PHE   HXT    H  N N 396 
PRO   N      N  N N 397 
PRO   CA     C  N S 398 
PRO   C      C  N N 399 
PRO   O      O  N N 400 
PRO   CB     C  N N 401 
PRO   CG     C  N N 402 
PRO   CD     C  N N 403 
PRO   OXT    O  N N 404 
PRO   H      H  N N 405 
PRO   HA     H  N N 406 
PRO   HB2    H  N N 407 
PRO   HB3    H  N N 408 
PRO   HG2    H  N N 409 
PRO   HG3    H  N N 410 
PRO   HD2    H  N N 411 
PRO   HD3    H  N N 412 
PRO   HXT    H  N N 413 
SAM   N      N  N N 414 
SAM   CA     C  N S 415 
SAM   C      C  N N 416 
SAM   O      O  N N 417 
SAM   OXT    O  N N 418 
SAM   CB     C  N N 419 
SAM   CG     C  N N 420 
SAM   SD     S  N S 421 
SAM   CE     C  N N 422 
SAM   "C5'"  C  N N 423 
SAM   "C4'"  C  N S 424 
SAM   "O4'"  O  N N 425 
SAM   "C3'"  C  N S 426 
SAM   "O3'"  O  N N 427 
SAM   "C2'"  C  N R 428 
SAM   "O2'"  O  N N 429 
SAM   "C1'"  C  N R 430 
SAM   N9     N  Y N 431 
SAM   C8     C  Y N 432 
SAM   N7     N  Y N 433 
SAM   C5     C  Y N 434 
SAM   C6     C  Y N 435 
SAM   N6     N  N N 436 
SAM   N1     N  Y N 437 
SAM   C2     C  Y N 438 
SAM   N3     N  Y N 439 
SAM   C4     C  Y N 440 
SAM   HN1    H  N N 441 
SAM   HN2    H  N N 442 
SAM   HA     H  N N 443 
SAM   HB1    H  N N 444 
SAM   HB2    H  N N 445 
SAM   HG1    H  N N 446 
SAM   HG2    H  N N 447 
SAM   HE1    H  N N 448 
SAM   HE2    H  N N 449 
SAM   HE3    H  N N 450 
SAM   "H5'1" H  N N 451 
SAM   "H5'2" H  N N 452 
SAM   "H4'"  H  N N 453 
SAM   "H3'"  H  N N 454 
SAM   "HO3'" H  N N 455 
SAM   "H2'"  H  N N 456 
SAM   "HO2'" H  N N 457 
SAM   "H1'"  H  N N 458 
SAM   H8     H  N N 459 
SAM   HN61   H  N N 460 
SAM   HN62   H  N N 461 
SAM   H2     H  N N 462 
SER   N      N  N N 463 
SER   CA     C  N S 464 
SER   C      C  N N 465 
SER   O      O  N N 466 
SER   CB     C  N N 467 
SER   OG     O  N N 468 
SER   OXT    O  N N 469 
SER   H      H  N N 470 
SER   H2     H  N N 471 
SER   HA     H  N N 472 
SER   HB2    H  N N 473 
SER   HB3    H  N N 474 
SER   HG     H  N N 475 
SER   HXT    H  N N 476 
THR   N      N  N N 477 
THR   CA     C  N S 478 
THR   C      C  N N 479 
THR   O      O  N N 480 
THR   CB     C  N R 481 
THR   OG1    O  N N 482 
THR   CG2    C  N N 483 
THR   OXT    O  N N 484 
THR   H      H  N N 485 
THR   H2     H  N N 486 
THR   HA     H  N N 487 
THR   HB     H  N N 488 
THR   HG1    H  N N 489 
THR   HG21   H  N N 490 
THR   HG22   H  N N 491 
THR   HG23   H  N N 492 
THR   HXT    H  N N 493 
TRP   N      N  N N 494 
TRP   CA     C  N S 495 
TRP   C      C  N N 496 
TRP   O      O  N N 497 
TRP   CB     C  N N 498 
TRP   CG     C  Y N 499 
TRP   CD1    C  Y N 500 
TRP   CD2    C  Y N 501 
TRP   NE1    N  Y N 502 
TRP   CE2    C  Y N 503 
TRP   CE3    C  Y N 504 
TRP   CZ2    C  Y N 505 
TRP   CZ3    C  Y N 506 
TRP   CH2    C  Y N 507 
TRP   OXT    O  N N 508 
TRP   H      H  N N 509 
TRP   H2     H  N N 510 
TRP   HA     H  N N 511 
TRP   HB2    H  N N 512 
TRP   HB3    H  N N 513 
TRP   HD1    H  N N 514 
TRP   HE1    H  N N 515 
TRP   HE3    H  N N 516 
TRP   HZ2    H  N N 517 
TRP   HZ3    H  N N 518 
TRP   HH2    H  N N 519 
TRP   HXT    H  N N 520 
TYR   N      N  N N 521 
TYR   CA     C  N S 522 
TYR   C      C  N N 523 
TYR   O      O  N N 524 
TYR   CB     C  N N 525 
TYR   CG     C  Y N 526 
TYR   CD1    C  Y N 527 
TYR   CD2    C  Y N 528 
TYR   CE1    C  Y N 529 
TYR   CE2    C  Y N 530 
TYR   CZ     C  Y N 531 
TYR   OH     O  N N 532 
TYR   OXT    O  N N 533 
TYR   H      H  N N 534 
TYR   H2     H  N N 535 
TYR   HA     H  N N 536 
TYR   HB2    H  N N 537 
TYR   HB3    H  N N 538 
TYR   HD1    H  N N 539 
TYR   HD2    H  N N 540 
TYR   HE1    H  N N 541 
TYR   HE2    H  N N 542 
TYR   HH     H  N N 543 
TYR   HXT    H  N N 544 
VAL   N      N  N N 545 
VAL   CA     C  N S 546 
VAL   C      C  N N 547 
VAL   O      O  N N 548 
VAL   CB     C  N N 549 
VAL   CG1    C  N N 550 
VAL   CG2    C  N N 551 
VAL   OXT    O  N N 552 
VAL   H      H  N N 553 
VAL   H2     H  N N 554 
VAL   HA     H  N N 555 
VAL   HB     H  N N 556 
VAL   HG11   H  N N 557 
VAL   HG12   H  N N 558 
VAL   HG13   H  N N 559 
VAL   HG21   H  N N 560 
VAL   HG22   H  N N 561 
VAL   HG23   H  N N 562 
VAL   HXT    H  N N 563 
ZN    ZN     ZN N N 564 
# 
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 
A1IQS O     C      doub N N 1   
A1IQS C     N      sing N N 2   
A1IQS N     C1     sing N N 3   
A1IQS O1    C1     doub N N 4   
A1IQS C1    C2     sing N N 5   
A1IQS C2    N1     sing Y N 6   
A1IQS C3    N1     sing Y N 7   
A1IQS N2    C3     doub Y N 8   
A1IQS C4    N2     sing Y N 9   
A1IQS C2    C4     doub Y N 10  
A1IQS N3    C4     sing N N 11  
A1IQS C     N3     sing N N 12  
A1IQS C5    N3     sing N N 13  
A1IQS N1    C6     sing N N 14  
A1IQS C6    C7     sing N N 15  
A1IQS O2    C7     sing N N 16  
A1IQS C7    C8     sing N N 17  
A1IQS C8    C9     sing N N 18  
A1IQS O3    C9     sing N N 19  
A1IQS C9    C10    sing N N 20  
A1IQS C10   N4     sing N N 21  
A1IQS N4    C11    sing N N 22  
A1IQS C11   O4     doub N N 23  
A1IQS C12   C11    sing N N 24  
A1IQS N5    C12    sing N N 25  
A1IQS C13   C12    sing N N 26  
A1IQS C14   C13    sing N N 27  
A1IQS C14   C15    sing Y N 28  
A1IQS C15   C16    doub Y N 29  
A1IQS C16   N6     sing Y N 30  
A1IQS N6    C17    sing Y N 31  
A1IQS C17   C14    doub Y N 32  
A1IQS C18   C16    sing Y N 33  
A1IQS C19   C18    doub Y N 34  
A1IQS C20   C19    sing Y N 35  
A1IQS C21   C20    doub Y N 36  
A1IQS C15   C21    sing Y N 37  
A1IQS C22   N4     sing N N 38  
A1IQS C6    C22    sing N N 39  
A1IQS C23   C7     sing N N 40  
A1IQS C24   N      sing N N 41  
A1IQS C5    H6     sing N N 42  
A1IQS C5    H5     sing N N 43  
A1IQS C5    H4     sing N N 44  
A1IQS C6    H      sing N N 45  
A1IQS C8    H8     sing N N 46  
A1IQS C8    H9     sing N N 47  
A1IQS C10   H12    sing N N 48  
A1IQS C10   H11    sing N N 49  
A1IQS C13   H15    sing N N 50  
A1IQS C13   H16    sing N N 51  
A1IQS C17   H18    sing N N 52  
A1IQS C20   H21    sing N N 53  
A1IQS C21   H22    sing N N 54  
A1IQS C22   H23    sing N N 55  
A1IQS C22   H24    sing N N 56  
A1IQS C24   H28    sing N N 57  
A1IQS C24   H30    sing N N 58  
A1IQS C24   H29    sing N N 59  
A1IQS C12   H2     sing N N 60  
A1IQS C18   H19    sing N N 61  
A1IQS C19   H20    sing N N 62  
A1IQS C23   H25    sing N N 63  
A1IQS C23   H27    sing N N 64  
A1IQS C23   H26    sing N N 65  
A1IQS C3    H3     sing N N 66  
A1IQS C9    H1     sing N N 67  
A1IQS N5    H13    sing N N 68  
A1IQS N5    H14    sing N N 69  
A1IQS N6    H17    sing N N 70  
A1IQS O2    H7     sing N N 71  
A1IQS O3    H10    sing N N 72  
ALA   N     CA     sing N N 73  
ALA   N     H      sing N N 74  
ALA   N     H2     sing N N 75  
ALA   CA    C      sing N N 76  
ALA   CA    CB     sing N N 77  
ALA   CA    HA     sing N N 78  
ALA   C     O      doub N N 79  
ALA   C     OXT    sing N N 80  
ALA   CB    HB1    sing N N 81  
ALA   CB    HB2    sing N N 82  
ALA   CB    HB3    sing N N 83  
ALA   OXT   HXT    sing N N 84  
ARG   N     CA     sing N N 85  
ARG   N     H      sing N N 86  
ARG   N     H2     sing N N 87  
ARG   CA    C      sing N N 88  
ARG   CA    CB     sing N N 89  
ARG   CA    HA     sing N N 90  
ARG   C     O      doub N N 91  
ARG   C     OXT    sing N N 92  
ARG   CB    CG     sing N N 93  
ARG   CB    HB2    sing N N 94  
ARG   CB    HB3    sing N N 95  
ARG   CG    CD     sing N N 96  
ARG   CG    HG2    sing N N 97  
ARG   CG    HG3    sing N N 98  
ARG   CD    NE     sing N N 99  
ARG   CD    HD2    sing N N 100 
ARG   CD    HD3    sing N N 101 
ARG   NE    CZ     sing N N 102 
ARG   NE    HE     sing N N 103 
ARG   CZ    NH1    sing N N 104 
ARG   CZ    NH2    doub N N 105 
ARG   NH1   HH11   sing N N 106 
ARG   NH1   HH12   sing N N 107 
ARG   NH2   HH21   sing N N 108 
ARG   NH2   HH22   sing N N 109 
ARG   OXT   HXT    sing N N 110 
ASN   N     CA     sing N N 111 
ASN   N     H      sing N N 112 
ASN   N     H2     sing N N 113 
ASN   CA    C      sing N N 114 
ASN   CA    CB     sing N N 115 
ASN   CA    HA     sing N N 116 
ASN   C     O      doub N N 117 
ASN   C     OXT    sing N N 118 
ASN   CB    CG     sing N N 119 
ASN   CB    HB2    sing N N 120 
ASN   CB    HB3    sing N N 121 
ASN   CG    OD1    doub N N 122 
ASN   CG    ND2    sing N N 123 
ASN   ND2   HD21   sing N N 124 
ASN   ND2   HD22   sing N N 125 
ASN   OXT   HXT    sing N N 126 
ASP   N     CA     sing N N 127 
ASP   N     H      sing N N 128 
ASP   N     H2     sing N N 129 
ASP   CA    C      sing N N 130 
ASP   CA    CB     sing N N 131 
ASP   CA    HA     sing N N 132 
ASP   C     O      doub N N 133 
ASP   C     OXT    sing N N 134 
ASP   CB    CG     sing N N 135 
ASP   CB    HB2    sing N N 136 
ASP   CB    HB3    sing N N 137 
ASP   CG    OD1    doub N N 138 
ASP   CG    OD2    sing N N 139 
ASP   OD2   HD2    sing N N 140 
ASP   OXT   HXT    sing N N 141 
CYS   N     CA     sing N N 142 
CYS   N     H      sing N N 143 
CYS   N     H2     sing N N 144 
CYS   CA    C      sing N N 145 
CYS   CA    CB     sing N N 146 
CYS   CA    HA     sing N N 147 
CYS   C     O      doub N N 148 
CYS   C     OXT    sing N N 149 
CYS   CB    SG     sing N N 150 
CYS   CB    HB2    sing N N 151 
CYS   CB    HB3    sing N N 152 
CYS   SG    HG     sing N N 153 
CYS   OXT   HXT    sing N N 154 
DMS   S     O      doub N N 155 
DMS   S     C1     sing N N 156 
DMS   S     C2     sing N N 157 
DMS   C1    H11    sing N N 158 
DMS   C1    H12    sing N N 159 
DMS   C1    H13    sing N N 160 
DMS   C2    H21    sing N N 161 
DMS   C2    H22    sing N N 162 
DMS   C2    H23    sing N N 163 
EDO   C1    O1     sing N N 164 
EDO   C1    C2     sing N N 165 
EDO   C1    H11    sing N N 166 
EDO   C1    H12    sing N N 167 
EDO   O1    HO1    sing N N 168 
EDO   C2    O2     sing N N 169 
EDO   C2    H21    sing N N 170 
EDO   C2    H22    sing N N 171 
EDO   O2    HO2    sing N N 172 
GLN   N     CA     sing N N 173 
GLN   N     H      sing N N 174 
GLN   N     H2     sing N N 175 
GLN   CA    C      sing N N 176 
GLN   CA    CB     sing N N 177 
GLN   CA    HA     sing N N 178 
GLN   C     O      doub N N 179 
GLN   C     OXT    sing N N 180 
GLN   CB    CG     sing N N 181 
GLN   CB    HB2    sing N N 182 
GLN   CB    HB3    sing N N 183 
GLN   CG    CD     sing N N 184 
GLN   CG    HG2    sing N N 185 
GLN   CG    HG3    sing N N 186 
GLN   CD    OE1    doub N N 187 
GLN   CD    NE2    sing N N 188 
GLN   NE2   HE21   sing N N 189 
GLN   NE2   HE22   sing N N 190 
GLN   OXT   HXT    sing N N 191 
GLU   N     CA     sing N N 192 
GLU   N     H      sing N N 193 
GLU   N     H2     sing N N 194 
GLU   CA    C      sing N N 195 
GLU   CA    CB     sing N N 196 
GLU   CA    HA     sing N N 197 
GLU   C     O      doub N N 198 
GLU   C     OXT    sing N N 199 
GLU   CB    CG     sing N N 200 
GLU   CB    HB2    sing N N 201 
GLU   CB    HB3    sing N N 202 
GLU   CG    CD     sing N N 203 
GLU   CG    HG2    sing N N 204 
GLU   CG    HG3    sing N N 205 
GLU   CD    OE1    doub N N 206 
GLU   CD    OE2    sing N N 207 
GLU   OE2   HE2    sing N N 208 
GLU   OXT   HXT    sing N N 209 
GLY   N     CA     sing N N 210 
GLY   N     H      sing N N 211 
GLY   N     H2     sing N N 212 
GLY   CA    C      sing N N 213 
GLY   CA    HA2    sing N N 214 
GLY   CA    HA3    sing N N 215 
GLY   C     O      doub N N 216 
GLY   C     OXT    sing N N 217 
GLY   OXT   HXT    sing N N 218 
HIS   N     CA     sing N N 219 
HIS   N     H      sing N N 220 
HIS   N     H2     sing N N 221 
HIS   CA    C      sing N N 222 
HIS   CA    CB     sing N N 223 
HIS   CA    HA     sing N N 224 
HIS   C     O      doub N N 225 
HIS   C     OXT    sing N N 226 
HIS   CB    CG     sing N N 227 
HIS   CB    HB2    sing N N 228 
HIS   CB    HB3    sing N N 229 
HIS   CG    ND1    sing Y N 230 
HIS   CG    CD2    doub Y N 231 
HIS   ND1   CE1    doub Y N 232 
HIS   ND1   HD1    sing N N 233 
HIS   CD2   NE2    sing Y N 234 
HIS   CD2   HD2    sing N N 235 
HIS   CE1   NE2    sing Y N 236 
HIS   CE1   HE1    sing N N 237 
HIS   NE2   HE2    sing N N 238 
HIS   OXT   HXT    sing N N 239 
HOH   O     H1     sing N N 240 
HOH   O     H2     sing N N 241 
ILE   N     CA     sing N N 242 
ILE   N     H      sing N N 243 
ILE   N     H2     sing N N 244 
ILE   CA    C      sing N N 245 
ILE   CA    CB     sing N N 246 
ILE   CA    HA     sing N N 247 
ILE   C     O      doub N N 248 
ILE   C     OXT    sing N N 249 
ILE   CB    CG1    sing N N 250 
ILE   CB    CG2    sing N N 251 
ILE   CB    HB     sing N N 252 
ILE   CG1   CD1    sing N N 253 
ILE   CG1   HG12   sing N N 254 
ILE   CG1   HG13   sing N N 255 
ILE   CG2   HG21   sing N N 256 
ILE   CG2   HG22   sing N N 257 
ILE   CG2   HG23   sing N N 258 
ILE   CD1   HD11   sing N N 259 
ILE   CD1   HD12   sing N N 260 
ILE   CD1   HD13   sing N N 261 
ILE   OXT   HXT    sing N N 262 
IMD   N1    C2     sing Y N 263 
IMD   N1    C5     sing Y N 264 
IMD   N1    HN1    sing N N 265 
IMD   C2    N3     doub Y N 266 
IMD   C2    H2     sing N N 267 
IMD   N3    C4     sing Y N 268 
IMD   N3    HN3    sing N N 269 
IMD   C4    C5     doub Y N 270 
IMD   C4    H4     sing N N 271 
IMD   C5    H5     sing N N 272 
LEU   N     CA     sing N N 273 
LEU   N     H      sing N N 274 
LEU   N     H2     sing N N 275 
LEU   CA    C      sing N N 276 
LEU   CA    CB     sing N N 277 
LEU   CA    HA     sing N N 278 
LEU   C     O      doub N N 279 
LEU   C     OXT    sing N N 280 
LEU   CB    CG     sing N N 281 
LEU   CB    HB2    sing N N 282 
LEU   CB    HB3    sing N N 283 
LEU   CG    CD1    sing N N 284 
LEU   CG    CD2    sing N N 285 
LEU   CG    HG     sing N N 286 
LEU   CD1   HD11   sing N N 287 
LEU   CD1   HD12   sing N N 288 
LEU   CD1   HD13   sing N N 289 
LEU   CD2   HD21   sing N N 290 
LEU   CD2   HD22   sing N N 291 
LEU   CD2   HD23   sing N N 292 
LEU   OXT   HXT    sing N N 293 
LYS   N     CA     sing N N 294 
LYS   N     H      sing N N 295 
LYS   N     H2     sing N N 296 
LYS   CA    C      sing N N 297 
LYS   CA    CB     sing N N 298 
LYS   CA    HA     sing N N 299 
LYS   C     O      doub N N 300 
LYS   C     OXT    sing N N 301 
LYS   CB    CG     sing N N 302 
LYS   CB    HB2    sing N N 303 
LYS   CB    HB3    sing N N 304 
LYS   CG    CD     sing N N 305 
LYS   CG    HG2    sing N N 306 
LYS   CG    HG3    sing N N 307 
LYS   CD    CE     sing N N 308 
LYS   CD    HD2    sing N N 309 
LYS   CD    HD3    sing N N 310 
LYS   CE    NZ     sing N N 311 
LYS   CE    HE2    sing N N 312 
LYS   CE    HE3    sing N N 313 
LYS   NZ    HZ1    sing N N 314 
LYS   NZ    HZ2    sing N N 315 
LYS   NZ    HZ3    sing N N 316 
LYS   OXT   HXT    sing N N 317 
MES   O1    C2     sing N N 318 
MES   O1    C6     sing N N 319 
MES   C2    C3     sing N N 320 
MES   C2    H21    sing N N 321 
MES   C2    H22    sing N N 322 
MES   C3    N4     sing N N 323 
MES   C3    H31    sing N N 324 
MES   C3    H32    sing N N 325 
MES   N4    C5     sing N N 326 
MES   N4    C7     sing N N 327 
MES   N4    HN4    sing N N 328 
MES   C5    C6     sing N N 329 
MES   C5    H51    sing N N 330 
MES   C5    H52    sing N N 331 
MES   C6    H61    sing N N 332 
MES   C6    H62    sing N N 333 
MES   C7    C8     sing N N 334 
MES   C7    H71    sing N N 335 
MES   C7    H72    sing N N 336 
MES   C8    S      sing N N 337 
MES   C8    H81    sing N N 338 
MES   C8    H82    sing N N 339 
MES   S     O1S    doub N N 340 
MES   S     O2S    doub N N 341 
MES   S     O3S    sing N N 342 
MET   N     CA     sing N N 343 
MET   N     H      sing N N 344 
MET   N     H2     sing N N 345 
MET   CA    C      sing N N 346 
MET   CA    CB     sing N N 347 
MET   CA    HA     sing N N 348 
MET   C     O      doub N N 349 
MET   C     OXT    sing N N 350 
MET   CB    CG     sing N N 351 
MET   CB    HB2    sing N N 352 
MET   CB    HB3    sing N N 353 
MET   CG    SD     sing N N 354 
MET   CG    HG2    sing N N 355 
MET   CG    HG3    sing N N 356 
MET   SD    CE     sing N N 357 
MET   CE    HE1    sing N N 358 
MET   CE    HE2    sing N N 359 
MET   CE    HE3    sing N N 360 
MET   OXT   HXT    sing N N 361 
PHE   N     CA     sing N N 362 
PHE   N     H      sing N N 363 
PHE   N     H2     sing N N 364 
PHE   CA    C      sing N N 365 
PHE   CA    CB     sing N N 366 
PHE   CA    HA     sing N N 367 
PHE   C     O      doub N N 368 
PHE   C     OXT    sing N N 369 
PHE   CB    CG     sing N N 370 
PHE   CB    HB2    sing N N 371 
PHE   CB    HB3    sing N N 372 
PHE   CG    CD1    doub Y N 373 
PHE   CG    CD2    sing Y N 374 
PHE   CD1   CE1    sing Y N 375 
PHE   CD1   HD1    sing N N 376 
PHE   CD2   CE2    doub Y N 377 
PHE   CD2   HD2    sing N N 378 
PHE   CE1   CZ     doub Y N 379 
PHE   CE1   HE1    sing N N 380 
PHE   CE2   CZ     sing Y N 381 
PHE   CE2   HE2    sing N N 382 
PHE   CZ    HZ     sing N N 383 
PHE   OXT   HXT    sing N N 384 
PRO   N     CA     sing N N 385 
PRO   N     CD     sing N N 386 
PRO   N     H      sing N N 387 
PRO   CA    C      sing N N 388 
PRO   CA    CB     sing N N 389 
PRO   CA    HA     sing N N 390 
PRO   C     O      doub N N 391 
PRO   C     OXT    sing N N 392 
PRO   CB    CG     sing N N 393 
PRO   CB    HB2    sing N N 394 
PRO   CB    HB3    sing N N 395 
PRO   CG    CD     sing N N 396 
PRO   CG    HG2    sing N N 397 
PRO   CG    HG3    sing N N 398 
PRO   CD    HD2    sing N N 399 
PRO   CD    HD3    sing N N 400 
PRO   OXT   HXT    sing N N 401 
SAM   N     CA     sing N N 402 
SAM   N     HN1    sing N N 403 
SAM   N     HN2    sing N N 404 
SAM   CA    C      sing N N 405 
SAM   CA    CB     sing N N 406 
SAM   CA    HA     sing N N 407 
SAM   C     O      doub N N 408 
SAM   C     OXT    sing N N 409 
SAM   CB    CG     sing N N 410 
SAM   CB    HB1    sing N N 411 
SAM   CB    HB2    sing N N 412 
SAM   CG    SD     sing N N 413 
SAM   CG    HG1    sing N N 414 
SAM   CG    HG2    sing N N 415 
SAM   SD    CE     sing N N 416 
SAM   SD    "C5'"  sing N N 417 
SAM   CE    HE1    sing N N 418 
SAM   CE    HE2    sing N N 419 
SAM   CE    HE3    sing N N 420 
SAM   "C5'" "C4'"  sing N N 421 
SAM   "C5'" "H5'1" sing N N 422 
SAM   "C5'" "H5'2" sing N N 423 
SAM   "C4'" "O4'"  sing N N 424 
SAM   "C4'" "C3'"  sing N N 425 
SAM   "C4'" "H4'"  sing N N 426 
SAM   "O4'" "C1'"  sing N N 427 
SAM   "C3'" "O3'"  sing N N 428 
SAM   "C3'" "C2'"  sing N N 429 
SAM   "C3'" "H3'"  sing N N 430 
SAM   "O3'" "HO3'" sing N N 431 
SAM   "C2'" "O2'"  sing N N 432 
SAM   "C2'" "C1'"  sing N N 433 
SAM   "C2'" "H2'"  sing N N 434 
SAM   "O2'" "HO2'" sing N N 435 
SAM   "C1'" N9     sing N N 436 
SAM   "C1'" "H1'"  sing N N 437 
SAM   N9    C8     sing Y N 438 
SAM   N9    C4     sing Y N 439 
SAM   C8    N7     doub Y N 440 
SAM   C8    H8     sing N N 441 
SAM   N7    C5     sing Y N 442 
SAM   C5    C6     sing Y N 443 
SAM   C5    C4     doub Y N 444 
SAM   C6    N6     sing N N 445 
SAM   C6    N1     doub Y N 446 
SAM   N6    HN61   sing N N 447 
SAM   N6    HN62   sing N N 448 
SAM   N1    C2     sing Y N 449 
SAM   C2    N3     doub Y N 450 
SAM   C2    H2     sing N N 451 
SAM   N3    C4     sing Y N 452 
SER   N     CA     sing N N 453 
SER   N     H      sing N N 454 
SER   N     H2     sing N N 455 
SER   CA    C      sing N N 456 
SER   CA    CB     sing N N 457 
SER   CA    HA     sing N N 458 
SER   C     O      doub N N 459 
SER   C     OXT    sing N N 460 
SER   CB    OG     sing N N 461 
SER   CB    HB2    sing N N 462 
SER   CB    HB3    sing N N 463 
SER   OG    HG     sing N N 464 
SER   OXT   HXT    sing N N 465 
THR   N     CA     sing N N 466 
THR   N     H      sing N N 467 
THR   N     H2     sing N N 468 
THR   CA    C      sing N N 469 
THR   CA    CB     sing N N 470 
THR   CA    HA     sing N N 471 
THR   C     O      doub N N 472 
THR   C     OXT    sing N N 473 
THR   CB    OG1    sing N N 474 
THR   CB    CG2    sing N N 475 
THR   CB    HB     sing N N 476 
THR   OG1   HG1    sing N N 477 
THR   CG2   HG21   sing N N 478 
THR   CG2   HG22   sing N N 479 
THR   CG2   HG23   sing N N 480 
THR   OXT   HXT    sing N N 481 
TRP   N     CA     sing N N 482 
TRP   N     H      sing N N 483 
TRP   N     H2     sing N N 484 
TRP   CA    C      sing N N 485 
TRP   CA    CB     sing N N 486 
TRP   CA    HA     sing N N 487 
TRP   C     O      doub N N 488 
TRP   C     OXT    sing N N 489 
TRP   CB    CG     sing N N 490 
TRP   CB    HB2    sing N N 491 
TRP   CB    HB3    sing N N 492 
TRP   CG    CD1    doub Y N 493 
TRP   CG    CD2    sing Y N 494 
TRP   CD1   NE1    sing Y N 495 
TRP   CD1   HD1    sing N N 496 
TRP   CD2   CE2    doub Y N 497 
TRP   CD2   CE3    sing Y N 498 
TRP   NE1   CE2    sing Y N 499 
TRP   NE1   HE1    sing N N 500 
TRP   CE2   CZ2    sing Y N 501 
TRP   CE3   CZ3    doub Y N 502 
TRP   CE3   HE3    sing N N 503 
TRP   CZ2   CH2    doub Y N 504 
TRP   CZ2   HZ2    sing N N 505 
TRP   CZ3   CH2    sing Y N 506 
TRP   CZ3   HZ3    sing N N 507 
TRP   CH2   HH2    sing N N 508 
TRP   OXT   HXT    sing N N 509 
TYR   N     CA     sing N N 510 
TYR   N     H      sing N N 511 
TYR   N     H2     sing N N 512 
TYR   CA    C      sing N N 513 
TYR   CA    CB     sing N N 514 
TYR   CA    HA     sing N N 515 
TYR   C     O      doub N N 516 
TYR   C     OXT    sing N N 517 
TYR   CB    CG     sing N N 518 
TYR   CB    HB2    sing N N 519 
TYR   CB    HB3    sing N N 520 
TYR   CG    CD1    doub Y N 521 
TYR   CG    CD2    sing Y N 522 
TYR   CD1   CE1    sing Y N 523 
TYR   CD1   HD1    sing N N 524 
TYR   CD2   CE2    doub Y N 525 
TYR   CD2   HD2    sing N N 526 
TYR   CE1   CZ     doub Y N 527 
TYR   CE1   HE1    sing N N 528 
TYR   CE2   CZ     sing Y N 529 
TYR   CE2   HE2    sing N N 530 
TYR   CZ    OH     sing N N 531 
TYR   OH    HH     sing N N 532 
TYR   OXT   HXT    sing N N 533 
VAL   N     CA     sing N N 534 
VAL   N     H      sing N N 535 
VAL   N     H2     sing N N 536 
VAL   CA    C      sing N N 537 
VAL   CA    CB     sing N N 538 
VAL   CA    HA     sing N N 539 
VAL   C     O      doub N N 540 
VAL   C     OXT    sing N N 541 
VAL   CB    CG1    sing N N 542 
VAL   CB    CG2    sing N N 543 
VAL   CB    HB     sing N N 544 
VAL   CG1   HG11   sing N N 545 
VAL   CG1   HG12   sing N N 546 
VAL   CG1   HG13   sing N N 547 
VAL   CG2   HG21   sing N N 548 
VAL   CG2   HG22   sing N N 549 
VAL   CG2   HG23   sing N N 550 
VAL   OXT   HXT    sing N N 551 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           'DESY Strategy Fund MUXCOSDYN' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7JIB 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GWO 
_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]   0.005950 
_atom_sites.fract_transf_matrix[1][2]   0.003435 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006870 
_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]   0.019335 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
H  
N  
NA 
O  
S  
ZN 
# 
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  1   ? -82.71496  46.77814  29.18425  1.000 72.23779  ?  6799 SER   A N      1 
ATOM   2    C  CA     . SER   A  1  1   ? -83.58796  47.75347  28.53090  1.000 76.32939  ?  6799 SER   A CA     1 
ATOM   3    C  C      . SER   A  1  1   ? -84.00332  47.23994  27.16280  1.000 68.64882  ?  6799 SER   A C      1 
ATOM   4    O  O      . SER   A  1  1   ? -85.05116  46.57508  27.01079  1.000 59.03014  ?  6799 SER   A O      1 
ATOM   5    C  CB     . SER   A  1  1   ? -82.88907  49.11205  28.38967  1.000 76.87707  ?  6799 SER   A CB     1 
ATOM   6    O  OG     . SER   A  1  1   ? -81.93038  49.08957  27.33703  1.000 73.43829  ?  6799 SER   A OG     1 
ATOM   7    N  N      . SER   A  1  2   ? -83.14810  47.56488  26.18343  1.000 67.33690  ?  6800 SER   A N      1 
ATOM   8    C  CA     . SER   A  1  2   ? -83.25619  47.11737  24.79878  1.000 62.80838  ?  6800 SER   A CA     1 
ATOM   9    C  C      . SER   A  1  2   ? -83.21150  45.59526  24.71927  1.000 58.45010  ?  6800 SER   A C      1 
ATOM   10   O  O      . SER   A  1  2   ? -83.54208  45.00585  23.67469  1.000 48.90811  ?  6800 SER   A O      1 
ATOM   11   C  CB     . SER   A  1  2   ? -82.12792  47.74240  23.97061  1.000 63.15480  ?  6800 SER   A CB     1 
ATOM   12   O  OG     . SER   A  1  2   ? -82.06772  47.19463  22.66734  1.000 67.77623  ?  6800 SER   A OG     1 
ATOM   13   N  N      . GLN   A  1  3   ? -82.83028  44.96114  25.82885  1.000 53.02702  ?  6801 GLN   A N      1 
ATOM   14   C  CA     . GLN   A  1  3   ? -82.68294  43.51642  25.83126  1.000 43.80740  ?  6801 GLN   A CA     1 
ATOM   15   C  C      . GLN   A  1  3   ? -84.01762  42.81009  25.63919  1.000 39.02061  ?  6801 GLN   A C      1 
ATOM   16   O  O      . GLN   A  1  3   ? -84.04619  41.68303  25.12430  1.000 36.75388  ?  6801 GLN   A O      1 
ATOM   17   C  CB     . GLN   A  1  3   ? -82.00251  43.06696  27.12247  1.000 44.99150  ?  6801 GLN   A CB     1 
ATOM   18   C  CG     . GLN   A  1  3   ? -80.49971  43.32690  27.11609  1.000 52.60552  ?  6801 GLN   A CG     1 
ATOM   19   C  CD     . GLN   A  1  3   ? -79.80802  42.91261  28.41990  1.000 59.18013  ?  6801 GLN   A CD     1 
ATOM   20   O  OE1    . GLN   A  1  3   ? -80.45745  42.62942  29.44057  1.000 57.74035  ?  6801 GLN   A OE1    1 
ATOM   21   N  NE2    . GLN   A  1  3   ? -78.47891  42.87779  28.38660  1.000 60.15438  ?  6801 GLN   A NE2    1 
ATOM   22   N  N      . ALA   A  1  4   ? -85.12974  43.44555  26.01880  1.000 36.55455  ?  6802 ALA   A N      1 
ATOM   23   C  CA     . ALA   A  1  4   ? -86.42498  42.77380  25.91715  1.000 37.44456  ?  6802 ALA   A CA     1 
ATOM   24   C  C      . ALA   A  1  4   ? -86.82590  42.48245  24.47305  1.000 36.61693  ?  6802 ALA   A C      1 
ATOM   25   O  O      . ALA   A  1  4   ? -87.69419  41.63207  24.24018  1.000 34.29985  ?  6802 ALA   A O      1 
ATOM   26   C  CB     . ALA   A  1  4   ? -87.52899  43.59667  26.60306  1.000 35.04631  ?  6802 ALA   A CB     1 
ATOM   27   N  N      . TRP   A  1  5   ? -86.22825  43.16150  23.50124  1.000 35.52828  ?  6803 TRP   A N      1 
ATOM   28   C  CA     . TRP   A  1  5   ? -86.52036  42.89249  22.10343  1.000 35.81341  ?  6803 TRP   A CA     1 
ATOM   29   C  C      . TRP   A  1  5   ? -85.52492  41.92797  21.48279  1.000 36.86543  ?  6803 TRP   A C      1 
ATOM   30   O  O      . TRP   A  1  5   ? -85.70463  41.53536  20.32702  1.000 38.27361  ?  6803 TRP   A O      1 
ATOM   31   C  CB     . TRP   A  1  5   ? -86.57661  44.20713  21.31005  1.000 41.76195  ?  6803 TRP   A CB     1 
ATOM   32   C  CG     . TRP   A  1  5   ? -87.82451  44.99389  21.64983  1.000 35.79674  ?  6803 TRP   A CG     1 
ATOM   33   C  CD1    . TRP   A  1  5   ? -89.04447  44.87544  21.05676  1.000 40.58646  ?  6803 TRP   A CD1    1 
ATOM   34   C  CD2    . TRP   A  1  5   ? -87.97584  45.97655  22.67952  1.000 39.41299  ?  6803 TRP   A CD2    1 
ATOM   35   N  NE1    . TRP   A  1  5   ? -89.95153  45.71587  21.64809  1.000 42.27045  ?  6803 TRP   A NE1    1 
ATOM   36   C  CE2    . TRP   A  1  5   ? -89.31949  46.41132  22.64592  1.000 40.95426  ?  6803 TRP   A CE2    1 
ATOM   37   C  CE3    . TRP   A  1  5   ? -87.11157  46.53536  23.62101  1.000 41.23785  ?  6803 TRP   A CE3    1 
ATOM   38   C  CZ2    . TRP   A  1  5   ? -89.81461  47.37889  23.51576  1.000 41.11017  ?  6803 TRP   A CZ2    1 
ATOM   39   C  CZ3    . TRP   A  1  5   ? -87.60712  47.49708  24.48788  1.000 44.41960  ?  6803 TRP   A CZ3    1 
ATOM   40   C  CH2    . TRP   A  1  5   ? -88.94775  47.90915  24.42559  1.000 46.06906  ?  6803 TRP   A CH2    1 
ATOM   41   N  N      . GLN   A  1  6   ? -84.50810  41.51036  22.23198  1.000 29.58481  ?  6804 GLN   A N      1 
ATOM   42   C  CA     . GLN   A  1  6   ? -83.61008  40.47295  21.75852  1.000 31.96809  ?  6804 GLN   A CA     1 
ATOM   43   C  C      . GLN   A  1  6   ? -84.20612  39.09165  22.04156  1.000 31.52292  ?  6804 GLN   A C      1 
ATOM   44   O  O      . GLN   A  1  6   ? -85.13696  38.95887  22.84383  1.000 27.97420  ?  6804 GLN   A O      1 
ATOM   45   C  CB     . GLN   A  1  6   ? -82.25243  40.61935  22.43983  1.000 33.27736  ?  6804 GLN   A CB     1 
ATOM   46   C  CG     . GLN   A  1  6   ? -81.54583  41.94586  22.11312  1.000 40.92677  ?  6804 GLN   A CG     1 
ATOM   47   C  CD     . GLN   A  1  6   ? -81.38369  42.13752  20.61148  1.000 47.73361  ?  6804 GLN   A CD     1 
ATOM   48   O  OE1    . GLN   A  1  6   ? -80.91789  41.23961  19.90192  1.000 53.20661  ?  6804 GLN   A OE1    1 
ATOM   49   N  NE2    . GLN   A  1  6   ? -81.78332  43.30196  20.11634  1.000 54.18329  ?  6804 GLN   A NE2    1 
ATOM   50   N  N      . PRO   A  1  7   ? -83.69462  38.04406  21.38946  1.000 28.21929  ?  6805 PRO   A N      1 
ATOM   51   C  CA     . PRO   A  1  7   ? -84.13788  36.68365  21.74965  1.000 26.49567  ?  6805 PRO   A CA     1 
ATOM   52   C  C      . PRO   A  1  7   ? -83.73728  36.29138  23.16175  1.000 28.54297  ?  6805 PRO   A C      1 
ATOM   53   O  O      . PRO   A  1  7   ? -84.39453  35.43084  23.76620  1.000 28.88248  ?  6805 PRO   A O      1 
ATOM   54   C  CB     . PRO   A  1  7   ? -83.45698  35.79623  20.70508  1.000 27.67689  ?  6805 PRO   A CB     1 
ATOM   55   C  CG     . PRO   A  1  7   ? -82.25687  36.59131  20.23068  1.000 30.31714  ?  6805 PRO   A CG     1 
ATOM   56   C  CD     . PRO   A  1  7   ? -82.68752  38.05371  20.31475  1.000 26.09699  ?  6805 PRO   A CD     1 
ATOM   57   N  N      . GLY   A  1  8   ? -82.70075  36.91234  23.71364  1.000 25.75253  ?  6806 GLY   A N      1 
ATOM   58   C  CA     . GLY   A  1  8   ? -82.23024  36.55542  25.03891  1.000 26.41869  ?  6806 GLY   A CA     1 
ATOM   59   C  C      . GLY   A  1  8   ? -80.98908  37.36019  25.35396  1.000 27.89272  ?  6806 GLY   A C      1 
ATOM   60   O  O      . GLY   A  1  8   ? -80.68297  38.33447  24.67074  1.000 27.52159  ?  6806 GLY   A O      1 
ATOM   61   N  N      . VAL   A  1  9   ? -80.26536  36.95525  26.39184  1.000 26.92764  ?  6807 VAL   A N      1 
ATOM   62   C  CA     . VAL   A  1  9   ? -79.08488  37.70073  26.81293  1.000 27.20980  ?  6807 VAL   A CA     1 
ATOM   63   C  C      . VAL   A  1  9   ? -77.92385  36.73625  26.94781  1.000 29.70368  ?  6807 VAL   A C      1 
ATOM   64   O  O      . VAL   A  1  9   ? -78.05947  35.69015  27.59494  1.000 27.52777  ?  6807 VAL   A O      1 
ATOM   65   C  CB     . VAL   A  1  9   ? -79.31341  38.45061  28.14089  1.000 27.23835  ?  6807 VAL   A CB     1 
ATOM   66   C  CG1    . VAL   A  1  9   ? -78.06705  39.28917  28.50910  1.000 31.07390  ?  6807 VAL   A CG1    1 
ATOM   67   C  CG2    . VAL   A  1  9   ? -80.52301  39.36659  28.01558  1.000 33.86880  ?  6807 VAL   A CG2    1 
ATOM   68   N  N      . ALA   A  1  10  ? -76.78565  37.09761  26.35847  1.000 25.23170  ?  6808 ALA   A N      1 
ATOM   69   C  CA     . ALA   A  1  10  ? -75.55067  36.33848  26.49192  1.000 26.68039  ?  6808 ALA   A CA     1 
ATOM   70   C  C      . ALA   A  1  10  ? -74.68918  36.90250  27.61522  1.000 30.64148  ?  6808 ALA   A C      1 
ATOM   71   O  O      . ALA   A  1  10  ? -74.67542  38.11113  27.87108  1.000 28.08247  ?  6808 ALA   A O      1 
ATOM   72   C  CB     . ALA   A  1  10  ? -74.74858  36.36291  25.18798  1.000 26.42389  ?  6808 ALA   A CB     1 
ATOM   73   N  N      . MET   A  1  11  ? -73.93846  36.02381  28.25860  1.000 27.55706  ?  6809 MET   A N      1 
ATOM   74   C  CA     . MET   A  1  11  ? -73.07628  36.42668  29.36792  1.000 28.21508  ?  6809 MET   A CA     1 
ATOM   75   C  C      . MET   A  1  11  ? -72.03830  37.43695  28.87638  1.000 28.75910  ?  6809 MET   A C      1 
ATOM   76   O  O      . MET   A  1  11  ? -71.26260  37.11432  27.96932  1.000 28.59934  ?  6809 MET   A O      1 
ATOM   77   C  CB     . MET   A  1  11  ? -72.40200  35.18598  29.94745  1.000 30.02423  ?  6809 MET   A CB     1 
ATOM   78   C  CG     . MET   A  1  11  ? -71.50538  35.39073  31.14754  1.000 28.26163  ?  6809 MET   A CG     1 
ATOM   79   S  SD     . MET   A  1  11  ? -70.90660  33.78458  31.74321  1.000 28.60047  ?  6809 MET   A SD     1 
ATOM   80   C  CE     . MET   A  1  11  ? -69.82257  34.32995  33.09731  1.000 26.28792  ?  6809 MET   A CE     1 
ATOM   81   N  N      . PRO   A  1  12  ? -72.00114  38.65426  29.41608  1.000 30.31386  ?  6810 PRO   A N      1 
ATOM   82   C  CA     . PRO   A  1  12  ? -71.02279  39.64562  28.93784  1.000 32.40582  ?  6810 PRO   A CA     1 
ATOM   83   C  C      . PRO   A  1  12  ? -69.58191  39.23442  29.22040  1.000 29.87054  ?  6810 PRO   A C      1 
ATOM   84   O  O      . PRO   A  1  12  ? -69.27355  38.61518  30.23906  1.000 29.52628  ?  6810 PRO   A O      1 
ATOM   85   C  CB     . PRO   A  1  12  ? -71.39240  40.91685  29.70956  1.000 32.74498  ?  6810 PRO   A CB     1 
ATOM   86   C  CG     . PRO   A  1  12  ? -72.85989  40.72084  30.09704  1.000 34.76063  ?  6810 PRO   A CG     1 
ATOM   87   C  CD     . PRO   A  1  12  ? -72.95519  39.22603  30.38060  1.000 30.13729  ?  6810 PRO   A CD     1 
ATOM   88   N  N      . ASN   A  1  13  ? -68.68835  39.61599  28.30033  1.000 33.76701  ?  6811 ASN   A N      1 
ATOM   89   C  CA     . ASN   A  1  13  ? -67.31102  39.12576  28.35622  1.000 35.50338  ?  6811 ASN   A CA     1 
ATOM   90   C  C      . ASN   A  1  13  ? -66.64859  39.44294  29.69210  1.000 32.83361  ?  6811 ASN   A C      1 
ATOM   91   O  O      . ASN   A  1  13  ? -65.85829  38.63986  30.19552  1.000 34.69546  ?  6811 ASN   A O      1 
ATOM   92   C  CB     . ASN   A  1  13  ? -66.48781  39.70360  27.20412  1.000 35.82086  ?  6811 ASN   A CB     1 
ATOM   93   C  CG     . ASN   A  1  13  ? -66.78755  39.02608  25.87962  1.000 42.71770  ?  6811 ASN   A CG     1 
ATOM   94   O  OD1    . ASN   A  1  13  ? -67.41760  37.96686  25.84953  1.000 42.16688  ?  6811 ASN   A OD1    1 
ATOM   95   N  ND2    . ASN   A  1  13  ? -66.32529  39.61980  24.77846  1.000 37.54224  ?  6811 ASN   A ND2    1 
ATOM   96   N  N      . LEU   A  1  14  ? -66.96590  40.59487  30.29843  1.000 31.29546  ?  6812 LEU   A N      1 
ATOM   97   C  CA     . LEU   A  1  14  ? -66.28889  40.95676  31.54623  1.000 32.19564  ?  6812 LEU   A CA     1 
ATOM   98   C  C      . LEU   A  1  14  ? -66.61462  39.97075  32.65720  1.000 35.66784  ?  6812 LEU   A C      1 
ATOM   99   O  O      . LEU   A  1  14  ? -65.76422  39.67635  33.50149  1.000 33.35743  ?  6812 LEU   A O      1 
ATOM   100  C  CB     . LEU   A  1  14  ? -66.66050  42.37520  31.98382  1.000 33.58449  ?  6812 LEU   A CB     1 
ATOM   101  C  CG     . LEU   A  1  14  ? -65.80110  42.92141  33.14579  1.000 38.23410  ?  6812 LEU   A CG     1 
ATOM   102  C  CD1    . LEU   A  1  14  ? -64.28761  42.80844  32.86114  1.000 35.76438  ?  6812 LEU   A CD1    1 
ATOM   103  C  CD2    . LEU   A  1  14  ? -66.14020  44.37859  33.41607  1.000 38.44056  ?  6812 LEU   A CD2    1 
ATOM   104  N  N      . TYR   A  1  15  ? -67.83841  39.43399  32.67325  1.000 30.24894  ?  6813 TYR   A N      1 
ATOM   105  C  CA     . TYR   A  1  15  ? -68.15939  38.44727  33.69460  1.000 31.25600  ?  6813 TYR   A CA     1 
ATOM   106  C  C      . TYR   A  1  15  ? -67.36776  37.16440  33.48439  1.000 28.28893  ?  6813 TYR   A C      1 
ATOM   107  O  O      . TYR   A  1  15  ? -67.01143  36.49354  34.45351  1.000 31.42646  ?  6813 TYR   A O      1 
ATOM   108  C  CB     . TYR   A  1  15  ? -69.66364  38.15783  33.69947  1.000 29.46597  ?  6813 TYR   A CB     1 
ATOM   109  C  CG     . TYR   A  1  15  ? -70.47992  39.29757  34.26420  1.000 32.34551  ?  6813 TYR   A CG     1 
ATOM   110  C  CD1    . TYR   A  1  15  ? -70.65580  39.43089  35.63618  1.000 34.05583  ?  6813 TYR   A CD1    1 
ATOM   111  C  CD2    . TYR   A  1  15  ? -71.05657  40.24396  33.43423  1.000 33.15656  ?  6813 TYR   A CD2    1 
ATOM   112  C  CE1    . TYR   A  1  15  ? -71.40647  40.47219  36.16664  1.000 35.44707  ?  6813 TYR   A CE1    1 
ATOM   113  C  CE2    . TYR   A  1  15  ? -71.81710  41.29602  33.96196  1.000 33.64692  ?  6813 TYR   A CE2    1 
ATOM   114  C  CZ     . TYR   A  1  15  ? -71.98426  41.38953  35.32810  1.000 34.99903  ?  6813 TYR   A CZ     1 
ATOM   115  O  OH     . TYR   A  1  15  ? -72.71811  42.42478  35.88167  1.000 36.71594  ?  6813 TYR   A OH     1 
ATOM   116  N  N      . LYS   A  1  16  ? -67.07688  36.81460  32.23305  1.000 29.86486  ?  6814 LYS   A N      1 
ATOM   117  C  CA     . LYS   A  1  16  ? -66.26810  35.62189  31.97600  1.000 34.27535  ?  6814 LYS   A CA     1 
ATOM   118  C  C      . LYS   A  1  16  ? -64.87218  35.74216  32.58023  1.000 37.73592  ?  6814 LYS   A C      1 
ATOM   119  O  O      . LYS   A  1  16  ? -64.24561  34.72393  32.90063  1.000 37.90943  ?  6814 LYS   A O      1 
ATOM   120  C  CB     . LYS   A  1  16  ? -66.15998  35.37907  30.46991  1.000 30.18368  ?  6814 LYS   A CB     1 
ATOM   121  C  CG     . LYS   A  1  16  ? -67.50810  35.18000  29.77465  1.000 31.73697  ?  6814 LYS   A CG     1 
ATOM   122  C  CD     . LYS   A  1  16  ? -67.32587  35.06991  28.25657  1.000 31.50094  ?  6814 LYS   A CD     1 
ATOM   123  C  CE     . LYS   A  1  16  ? -68.67010  35.00995  27.54624  1.000 32.13111  ?  6814 LYS   A CE     1 
ATOM   124  N  NZ     . LYS   A  1  16  ? -68.56042  35.33428  26.09476  1.000 33.48397  ?  6814 LYS   A NZ     1 
ATOM   125  N  N      . MET   A  1  17  ? -64.35978  36.96508  32.72225  1.000 35.21394  ?  6815 MET   A N      1 
ATOM   126  C  CA     . MET   A  1  17  ? -62.98463  37.20156  33.16383  1.000 35.81584  ?  6815 MET   A CA     1 
ATOM   127  C  C      . MET   A  1  17  ? -62.83313  37.29788  34.67390  1.000 35.69818  ?  6815 MET   A C      1 
ATOM   128  O  O      . MET   A  1  17  ? -61.72144  37.53618  35.15384  1.000 39.20429  ?  6815 MET   A O      1 
ATOM   129  C  CB     . MET   A  1  17  ? -62.44644  38.49195  32.53797  1.000 33.93322  ?  6815 MET   A CB     1 
ATOM   130  C  CG     . MET   A  1  17  ? -62.64981  38.54126  31.04516  1.000 38.74506  ?  6815 MET   A CG     1 
ATOM   131  S  SD     . MET   A  1  17  ? -62.09587  40.11243  30.41496  1.000 42.44289  ?  6815 MET   A SD     1 
ATOM   132  C  CE     . MET   A  1  17  ? -60.41851  40.10395  30.97674  1.000 41.75537  ?  6815 MET   A CE     1 
ATOM   133  N  N      . GLN   A  1  18  ? -63.90927  37.15421  35.43749  1.000 31.88907  ?  6816 GLN   A N      1 
ATOM   134  C  CA     . GLN   A  1  18  ? -63.80670  37.28650  36.88054  1.000 33.09843  ?  6816 GLN   A CA     1 
ATOM   135  C  C      . GLN   A  1  18  ? -63.26775  35.98621  37.46904  1.000 37.77556  ?  6816 GLN   A C      1 
ATOM   136  O  O      . GLN   A  1  18  ? -63.04817  34.99978  36.76177  1.000 37.65126  ?  6816 GLN   A O      1 
ATOM   137  C  CB     . GLN   A  1  18  ? -65.16559  37.66569  37.47764  1.000 33.85317  ?  6816 GLN   A CB     1 
ATOM   138  C  CG     . GLN   A  1  18  ? -65.69532  38.96190  36.90822  1.000 30.77872  ?  6816 GLN   A CG     1 
ATOM   139  C  CD     . GLN   A  1  18  ? -64.68579  40.09011  37.09657  1.000 33.42433  ?  6816 GLN   A CD     1 
ATOM   140  O  OE1    . GLN   A  1  18  ? -64.23546  40.34701  38.21383  1.000 33.92908  ?  6816 GLN   A OE1    1 
ATOM   141  N  NE2    . GLN   A  1  18  ? -64.31288  40.74732  36.00613  1.000 31.84196  ?  6816 GLN   A NE2    1 
ATOM   142  N  N      . ARG   A  1  19  ? -63.03073  35.98049  38.78100  1.000 34.24786  ?  6817 ARG   A N      1 
ATOM   143  C  CA     . ARG   A  1  19  ? -62.68926  34.75842  39.51031  1.000 40.29636  ?  6817 ARG   A CA     1 
ATOM   144  C  C      . ARG   A  1  19  ? -63.57749  34.68036  40.75022  1.000 39.23642  ?  6817 ARG   A C      1 
ATOM   145  O  O      . ARG   A  1  19  ? -63.11914  34.78204  41.88645  1.000 41.52487  ?  6817 ARG   A O      1 
ATOM   146  C  CB     . ARG   A  1  19  ? -61.19120  34.70268  39.86662  1.000 45.98481  ?  6817 ARG   A CB     1 
ATOM   147  C  CG     . ARG   A  1  19  ? -60.29566  34.51596  38.64242  1.000 52.50052  ?  6817 ARG   A CG     1 
ATOM   148  C  CD     . ARG   A  1  19  ? -58.99007  33.78507  38.94849  1.000 66.55318  ?  6817 ARG   A CD     1 
ATOM   149  N  NE     . ARG   A  1  19  ? -59.20249  32.46804  39.54415  1.000 70.71970  ?  6817 ARG   A NE     1 
ATOM   150  C  CZ     . ARG   A  1  19  ? -59.10613  32.20995  40.84349  1.000 71.43036  ?  6817 ARG   A CZ     1 
ATOM   151  N  NH1    . ARG   A  1  19  ? -58.79414  33.15998  41.71504  1.000 63.85071  ?  6817 ARG   A NH1    1 
ATOM   152  N  NH2    . ARG   A  1  19  ? -59.32420  30.96748  41.27926  1.000 60.53662  ?  6817 ARG   A NH2    1 
ATOM   153  N  N      . MET   A  1  20  ? -64.87065  34.47710  40.52173  1.000 38.39806  ?  6818 MET   A N      1 
ATOM   154  C  CA     . MET   A  1  20  ? -65.84114  34.47978  41.60580  1.000 33.78364  ?  6818 MET   A CA     1 
ATOM   155  C  C      . MET   A  1  20  ? -65.84929  33.13168  42.31416  1.000 37.68041  ?  6818 MET   A C      1 
ATOM   156  O  O      . MET   A  1  20  ? -65.34722  32.12757  41.79782  1.000 39.65736  ?  6818 MET   A O      1 
ATOM   157  C  CB     . MET   A  1  20  ? -67.24043  34.80426  41.07486  1.000 36.71663  ?  6818 MET   A CB     1 
ATOM   158  C  CG     . MET   A  1  20  ? -67.32524  36.08936  40.28530  1.000 38.23019  ?  6818 MET   A CG     1 
ATOM   159  S  SD     . MET   A  1  20  ? -66.78242  37.46028  41.32637  1.000 46.38582  ?  6818 MET   A SD     1 
ATOM   160  C  CE     . MET   A  1  20  ? -67.88149  37.21343  42.69717  1.000 46.25024  ?  6818 MET   A CE     1 
ATOM   161  N  N      . LEU   A  1  21  ? -66.40741  33.12301  43.52400  1.000 38.18340  ?  6819 LEU   A N      1 
ATOM   162  C  CA     . LEU   A  1  21  ? -66.70705  31.89532  44.24719  1.000 41.20274  ?  6819 LEU   A CA     1 
ATOM   163  C  C      . LEU   A  1  21  ? -68.16821  31.53824  44.03538  1.000 37.78330  ?  6819 LEU   A C      1 
ATOM   164  O  O      . LEU   A  1  21  ? -69.00876  32.40767  43.79957  1.000 36.85322  ?  6819 LEU   A O      1 
ATOM   165  C  CB     . LEU   A  1  21  ? -66.43227  32.03335  45.75137  1.000 44.53644  ?  6819 LEU   A CB     1 
ATOM   166  C  CG     . LEU   A  1  21  ? -64.98828  32.32200  46.17674  1.000 45.58773  ?  6819 LEU   A CG     1 
ATOM   167  C  CD1    . LEU   A  1  21  ? -64.88382  32.37063  47.69246  1.000 54.13469  ?  6819 LEU   A CD1    1 
ATOM   168  C  CD2    . LEU   A  1  21  ? -64.01260  31.29440  45.57372  1.000 49.49225  ?  6819 LEU   A CD2    1 
ATOM   169  N  N      . LEU   A  1  22  ? -68.46545  30.24963  44.13582  1.000 37.71019  ?  6820 LEU   A N      1 
ATOM   170  C  CA     . LEU   A  1  22  ? -69.79802  29.76384  43.82171  1.000 38.87567  ?  6820 LEU   A CA     1 
ATOM   171  C  C      . LEU   A  1  22  ? -70.76399  30.09689  44.94813  1.000 44.24559  ?  6820 LEU   A C      1 
ATOM   172  O  O      . LEU   A  1  22  ? -70.52931  29.75063  46.10813  1.000 49.80687  ?  6820 LEU   A O      1 
ATOM   173  C  CB     . LEU   A  1  22  ? -69.77920  28.25883  43.56426  1.000 38.01836  ?  6820 LEU   A CB     1 
ATOM   174  C  CG     . LEU   A  1  22  ? -71.12939  27.66008  43.15492  1.000 42.24980  ?  6820 LEU   A CG     1 
ATOM   175  C  CD1    . LEU   A  1  22  ? -71.71298  28.37757  41.93923  1.000 41.23024  ?  6820 LEU   A CD1    1 
ATOM   176  C  CD2    . LEU   A  1  22  ? -70.99676  26.17120  42.86953  1.000 43.46544  ?  6820 LEU   A CD2    1 
ATOM   177  N  N      . GLU   A  1  23  ? -71.85897  30.75381  44.59460  1.000 44.81096  ?  6821 GLU   A N      1 
ATOM   178  C  CA     . GLU   A  1  23  ? -72.92643  31.09954  45.50964  1.000 43.25155  ?  6821 GLU   A CA     1 
ATOM   179  C  C      . GLU   A  1  23  ? -74.21847  30.44522  45.05533  1.000 44.12451  ?  6821 GLU   A C      1 
ATOM   180  O  O      . GLU   A  1  23  ? -74.33222  29.95825  43.92983  1.000 40.80597  ?  6821 GLU   A O      1 
ATOM   181  C  CB     . GLU   A  1  23  ? -73.12344  32.61261  45.56635  1.000 46.63021  ?  6821 GLU   A CB     1 
ATOM   182  C  CG     . GLU   A  1  23  ? -71.99973  33.37075  46.22256  1.000 47.35867  ?  6821 GLU   A CG     1 
ATOM   183  C  CD     . GLU   A  1  23  ? -72.36909  34.82436  46.44764  1.000 59.78173  ?  6821 GLU   A CD     1 
ATOM   184  O  OE1    . GLU   A  1  23  ? -72.31433  35.60493  45.46670  1.000 56.84038  ?  6821 GLU   A OE1    1 
ATOM   185  O  OE2    . GLU   A  1  23  ? -72.73869  35.17256  47.59700  1.000 67.99529  ?  6821 GLU   A OE2    1 
ATOM   186  N  N      . LYS   A  1  24  ? -75.19812  30.45821  45.95026  1.000 41.69925  ?  6822 LYS   A N      1 
ATOM   187  C  CA     . LYS   A  1  24  ? -76.55610  30.07807  45.59061  1.000 44.01350  ?  6822 LYS   A CA     1 
ATOM   188  C  C      . LYS   A  1  24  ? -77.10917  31.03534  44.53543  1.000 42.40897  ?  6822 LYS   A C      1 
ATOM   189  O  O      . LYS   A  1  24  ? -76.83016  32.23855  44.54820  1.000 42.63995  ?  6822 LYS   A O      1 
ATOM   190  C  CB     . LYS   A  1  24  ? -77.43050  30.08001  46.84620  1.000 45.74607  ?  6822 LYS   A CB     1 
ATOM   191  C  CG     . LYS   A  1  24  ? -78.86772  29.65034  46.64271  1.000 54.90256  ?  6822 LYS   A CG     1 
ATOM   192  C  CD     . LYS   A  1  24  ? -79.63851  29.70925  47.96583  1.000 60.53154  ?  6822 LYS   A CD     1 
ATOM   193  C  CE     . LYS   A  1  24  ? -81.15220  29.79760  47.74641  1.000 66.34802  ?  6822 LYS   A CE     1 
ATOM   194  N  NZ     . LYS   A  1  24  ? -81.77044  28.47578  47.49231  1.000 69.32557  ?  6822 LYS   A NZ     1 
ATOM   195  N  N      . CYS   A  1  25  ? -77.88556  30.49931  43.59944  1.000 41.19805  ?  6823 CYS   A N      1 
ATOM   196  C  CA     . CYS   A  1  25  ? -78.51352  31.32133  42.57683  1.000 36.82508  ?  6823 CYS   A CA     1 
ATOM   197  C  C      . CYS   A  1  25  ? -79.84101  31.83002  43.11515  1.000 43.64051  ?  6823 CYS   A C      1 
ATOM   198  O  O      . CYS   A  1  25  ? -80.70952  31.03813  43.48795  1.000 46.83206  ?  6823 CYS   A O      1 
ATOM   199  C  CB     . CYS   A  1  25  ? -78.72723  30.54625  41.27591  1.000 41.49184  ?  6823 CYS   A CB     1 
ATOM   200  S  SG     . CYS   A  1  25  ? -79.24393  31.61390  39.89866  1.000 42.43036  ?  6823 CYS   A SG     1 
ATOM   201  N  N      . ASP   A  1  26  ? -79.99604  33.14711  43.14950  1.000 43.82324  ?  6824 ASP   A N      1 
ATOM   202  C  CA     . ASP   A  1  26  ? -81.19229  33.78495  43.68924  1.000 48.26584  ?  6824 ASP   A CA     1 
ATOM   203  C  C      . ASP   A  1  26  ? -81.68104  34.78402  42.64713  1.000 46.45015  ?  6824 ASP   A C      1 
ATOM   204  O  O      . ASP   A  1  26  ? -81.11552  35.87179  42.49775  1.000 43.05847  ?  6824 ASP   A O      1 
ATOM   205  C  CB     . ASP   A  1  26  ? -80.87830  34.44417  45.02124  1.000 52.44015  ?  6824 ASP   A CB     1 
ATOM   206  C  CG     . ASP   A  1  26  ? -82.08324  35.09743  45.67087  1.000 64.91098  ?  6824 ASP   A CG     1 
ATOM   207  O  OD1    . ASP   A  1  26  ? -83.17096  35.15839  45.05169  1.000 70.20106  ?  6824 ASP   A OD1    1 
ATOM   208  O  OD2    . ASP   A  1  26  ? -81.92322  35.57009  46.82131  1.000 69.73533  ?  6824 ASP   A OD2    1 
ATOM   209  N  N      . LEU   A  1  27  ? -82.72221  34.41377  41.91930  1.000 43.54220  ?  6825 LEU   A N      1 
ATOM   210  C  CA     . LEU   A  1  27  ? -83.20971  35.21010  40.80320  1.000 46.12744  ?  6825 LEU   A CA     1 
ATOM   211  C  C      . LEU   A  1  27  ? -84.36889  36.08372  41.27250  1.000 48.43510  ?  6825 LEU   A C      1 
ATOM   212  O  O      . LEU   A  1  27  ? -85.36943  35.57890  41.79387  1.000 47.98547  ?  6825 LEU   A O      1 
ATOM   213  C  CB     . LEU   A  1  27  ? -83.62913  34.31548  39.63498  1.000 41.86306  ?  6825 LEU   A CB     1 
ATOM   214  C  CG     . LEU   A  1  27  ? -82.48903  33.52663  38.98986  1.000 39.96702  ?  6825 LEU   A CG     1 
ATOM   215  C  CD1    . LEU   A  1  27  ? -82.96602  32.75074  37.77325  1.000 35.26232  ?  6825 LEU   A CD1    1 
ATOM   216  C  CD2    . LEU   A  1  27  ? -81.34017  34.46328  38.61898  1.000 36.76802  ?  6825 LEU   A CD2    1 
ATOM   217  N  N      . GLN   A  1  28  ? -84.21096  37.39354  41.10016  1.000 46.71111  ?  6826 GLN   A N      1 
ATOM   218  C  CA     . GLN   A  1  28  ? -85.25213  38.34310  41.48102  1.000 52.73282  ?  6826 GLN   A CA     1 
ATOM   219  C  C      . GLN   A  1  28  ? -86.56167  38.05316  40.75147  1.000 51.81974  ?  6826 GLN   A C      1 
ATOM   220  O  O      . GLN   A  1  28  ? -87.64374  38.12645  41.34617  1.000 54.06043  ?  6826 GLN   A O      1 
ATOM   221  C  CB     . GLN   A  1  28  ? -84.75142  39.76723  41.19650  1.000 48.38960  ?  6826 GLN   A CB     1 
ATOM   222  C  CG     . GLN   A  1  28  ? -85.81794  40.82110  40.97791  1.000 56.25589  ?  6826 GLN   A CG     1 
ATOM   223  C  CD     . GLN   A  1  28  ? -85.24246  42.11298  40.38287  1.000 59.34383  ?  6826 GLN   A CD     1 
ATOM   224  O  OE1    . GLN   A  1  28  ? -85.70239  42.59477  39.33915  1.000 57.77143  ?  6826 GLN   A OE1    1 
ATOM   225  N  NE2    . GLN   A  1  28  ? -84.22683  42.67069  41.04445  1.000 54.00682  ?  6826 GLN   A NE2    1 
ATOM   226  N  N      . ASN   A  1  29  ? -86.48226  37.70971  39.46343  1.000 53.57972  ?  6827 ASN   A N      1 
ATOM   227  C  CA     . ASN   A  1  29  ? -87.64811  37.43869  38.63042  1.000 50.72422  ?  6827 ASN   A CA     1 
ATOM   228  C  C      . ASN   A  1  29  ? -88.09443  35.98046  38.70310  1.000 54.35123  ?  6827 ASN   A C      1 
ATOM   229  O  O      . ASN   A  1  29  ? -88.87692  35.53596  37.85682  1.000 57.17422  ?  6827 ASN   A O      1 
ATOM   230  C  CB     . ASN   A  1  29  ? -87.35643  37.84952  37.17914  1.000 50.60358  ?  6827 ASN   A CB     1 
ATOM   231  C  CG     . ASN   A  1  29  ? -86.96415  39.34863  37.05499  1.000 62.45324  ?  6827 ASN   A CG     1 
ATOM   232  O  OD1    . ASN   A  1  29  ? -87.10731  40.13206  38.00980  1.000 55.10031  ?  6827 ASN   A OD1    1 
ATOM   233  N  ND2    . ASN   A  1  29  ? -86.47007  39.74176  35.87658  1.000 54.35770  ?  6827 ASN   A ND2    1 
ATOM   234  N  N      . TYR   A  1  30  ? -87.62377  35.23453  39.70182  1.000 52.31963  ?  6828 TYR   A N      1 
ATOM   235  C  CA     . TYR   A  1  30  ? -88.00472  33.83477  39.84384  1.000 58.32219  ?  6828 TYR   A CA     1 
ATOM   236  C  C      . TYR   A  1  30  ? -89.51239  33.70718  40.02795  1.000 66.67571  ?  6828 TYR   A C      1 
ATOM   237  O  O      . TYR   A  1  30  ? -90.10508  34.36336  40.88818  1.000 76.08239  ?  6828 TYR   A O      1 
ATOM   238  C  CB     . TYR   A  1  30  ? -87.27478  33.21209  41.03414  1.000 66.42699  ?  6828 TYR   A CB     1 
ATOM   239  C  CG     . TYR   A  1  30  ? -87.42693  31.70704  41.14093  1.000 80.04668  ?  6828 TYR   A CG     1 
ATOM   240  C  CD1    . TYR   A  1  30  ? -86.68330  30.85379  40.32622  1.000 75.90780  ?  6828 TYR   A CD1    1 
ATOM   241  C  CD2    . TYR   A  1  30  ? -88.29963  31.13628  42.06420  1.000 88.49854  ?  6828 TYR   A CD2    1 
ATOM   242  C  CE1    . TYR   A  1  30  ? -86.81157  29.47668  40.42307  1.000 84.48780  ?  6828 TYR   A CE1    1 
ATOM   243  C  CE2    . TYR   A  1  30  ? -88.43249  29.75727  42.16989  1.000 90.81223  ?  6828 TYR   A CE2    1 
ATOM   244  C  CZ     . TYR   A  1  30  ? -87.68720  28.93401  41.34685  1.000 89.60465  ?  6828 TYR   A CZ     1 
ATOM   245  O  OH     . TYR   A  1  30  ? -87.81211  27.56582  41.44322  1.000 93.14500  ?  6828 TYR   A OH     1 
ATOM   246  N  N      . GLY   A  1  31  ? -90.13616  32.85143  39.22782  1.000 64.66994  ?  6829 GLY   A N      1 
ATOM   247  C  CA     . GLY   A  1  31  ? -91.56475  32.65117  39.30988  1.000 72.95815  ?  6829 GLY   A CA     1 
ATOM   248  C  C      . GLY   A  1  31  ? -92.39104  33.49392  38.36005  1.000 70.28736  ?  6829 GLY   A C      1 
ATOM   249  O  O      . GLY   A  1  31  ? -93.53069  33.11792  38.05950  1.000 73.52542  ?  6829 GLY   A O      1 
ATOM   250  N  N      . ASP   A  1  32  ? -91.86737  34.63594  37.90033  1.000 67.09769  ?  6830 ASP   A N      1 
ATOM   251  C  CA     . ASP   A  1  32  ? -92.44427  35.32208  36.74623  1.000 64.35577  ?  6830 ASP   A CA     1 
ATOM   252  C  C      . ASP   A  1  32  ? -92.57667  34.36081  35.56785  1.000 65.22292  ?  6830 ASP   A C      1 
ATOM   253  O  O      . ASP   A  1  32  ? -91.87285  33.34897  35.49926  1.000 61.44393  ?  6830 ASP   A O      1 
ATOM   254  C  CB     . ASP   A  1  32  ? -91.58420  36.51324  36.31101  1.000 65.63199  ?  6830 ASP   A CB     1 
ATOM   255  C  CG     . ASP   A  1  32  ? -91.71617  37.71124  37.22621  1.000 73.35731  ?  6830 ASP   A CG     1 
ATOM   256  O  OD1    . ASP   A  1  32  ? -92.13303  37.52915  38.39427  1.000 72.07061  ?  6830 ASP   A OD1    1 
ATOM   257  O  OD2    . ASP   A  1  32  ? -91.39669  38.83724  36.75786  1.000 65.97990  ?  6830 ASP   A OD2    1 
ATOM   258  N  N      . SER   A  1  33  ? -93.46704  34.68538  34.62896  1.000 65.13497  ?  6831 SER   A N      1 
ATOM   259  C  CA     . SER   A  1  33  ? -93.55713  33.98375  33.35730  1.000 57.78730  ?  6831 SER   A CA     1 
ATOM   260  C  C      . SER   A  1  33  ? -93.76740  35.00501  32.25251  1.000 59.14436  ?  6831 SER   A C      1 
ATOM   261  O  O      . SER   A  1  33  ? -94.40320  36.04523  32.45791  1.000 59.81297  ?  6831 SER   A O      1 
ATOM   262  C  CB     . SER   A  1  33  ? -94.68959  32.95478  33.33674  1.000 61.63922  ?  6831 SER   A CB     1 
ATOM   263  O  OG     . SER   A  1  33  ? -94.26209  31.71055  33.86697  1.000 65.24574  ?  6831 SER   A OG     1 
ATOM   264  N  N      . ALA   A  1  34  ? -93.18749  34.72373  31.09001  1.000 51.52372  ?  6832 ALA   A N      1 
ATOM   265  C  CA     . ALA   A  1  34  ? -93.49333  35.53203  29.92618  1.000 48.62877  ?  6832 ALA   A CA     1 
ATOM   266  C  C      . ALA   A  1  34  ? -94.86112  35.14183  29.38562  1.000 47.71476  ?  6832 ALA   A C      1 
ATOM   267  O  O      . ALA   A  1  34  ? -95.38033  34.05503  29.66017  1.000 46.54347  ?  6832 ALA   A O      1 
ATOM   268  C  CB     . ALA   A  1  34  ? -92.44070  35.35881  28.83207  1.000 44.63308  ?  6832 ALA   A CB     1 
ATOM   269  N  N      . THR   A  1  35  ? -95.43878  36.03968  28.59670  1.000 48.82140  ?  6833 THR   A N      1 
ATOM   270  C  CA     . THR   A  1  35  ? -96.72130  35.77749  27.95360  1.000 49.14716  ?  6833 THR   A CA     1 
ATOM   271  C  C      . THR   A  1  35  ? -96.43586  35.17944  26.58163  1.000 41.17125  ?  6833 THR   A C      1 
ATOM   272  O  O      . THR   A  1  35  ? -96.02034  35.87864  25.65800  1.000 44.40173  ?  6833 THR   A O      1 
ATOM   273  C  CB     . THR   A  1  35  ? -97.54527  37.05638  27.86774  1.000 52.31728  ?  6833 THR   A CB     1 
ATOM   274  O  OG1    . THR   A  1  35  ? -97.84149  37.49683  29.19828  1.000 53.57600  ?  6833 THR   A OG1    1 
ATOM   275  C  CG2    . THR   A  1  35  ? -98.84842  36.80193  27.12528  1.000 51.79548  ?  6833 THR   A CG2    1 
ATOM   276  N  N      . LEU   A  1  36  ? -96.63308  33.89228  26.45118  1.000 38.40759  ?  6834 LEU   A N      1 
ATOM   277  C  CA     . LEU   A  1  36  ? -96.38361  33.25722  25.16728  1.000 39.16754  ?  6834 LEU   A CA     1 
ATOM   278  C  C      . LEU   A  1  36  ? -97.52713  33.54229  24.19679  1.000 36.65190  ?  6834 LEU   A C      1 
ATOM   279  O  O      . LEU   A  1  36  ? -98.67635  33.66105  24.61675  1.000 39.37729  ?  6834 LEU   A O      1 
ATOM   280  C  CB     . LEU   A  1  36  ? -96.23463  31.75227  25.35417  1.000 37.85561  ?  6834 LEU   A CB     1 
ATOM   281  C  CG     . LEU   A  1  36  ? -95.12830  31.36578  26.33341  1.000 37.71876  ?  6834 LEU   A CG     1 
ATOM   282  C  CD1    . LEU   A  1  36  ? -95.08534  29.85918  26.55178  1.000 35.41185  ?  6834 LEU   A CD1    1 
ATOM   283  C  CD2    . LEU   A  1  36  ? -93.80807  31.86979  25.79412  1.000 36.21712  ?  6834 LEU   A CD2    1 
ATOM   284  N  N      . PRO   A  1  37  ? -97.23928  33.64675  22.88608  1.000 36.31452  ?  6835 PRO   A N      1 
ATOM   285  C  CA     . PRO   A  1  37  ? -98.32617  33.76475  21.90490  1.000 33.02267  ?  6835 PRO   A CA     1 
ATOM   286  C  C      . PRO   A  1  37  ? -99.33322  32.64836  22.08916  1.000 38.12554  ?  6835 PRO   A C      1 
ATOM   287  O  O      . PRO   A  1  37  ? -98.99274  31.57433  22.58630  1.000 33.20188  ?  6835 PRO   A O      1 
ATOM   288  C  CB     . PRO   A  1  37  ? -97.61151  33.65690  20.55072  1.000 30.45767  ?  6835 PRO   A CB     1 
ATOM   289  C  CG     . PRO   A  1  37  ? -96.19146  34.10915  20.84452  1.000 34.21603  ?  6835 PRO   A CG     1 
ATOM   290  C  CD     . PRO   A  1  37  ? -95.91466  33.60198  22.24047  1.000 36.88805  ?  6835 PRO   A CD     1 
ATOM   291  N  N      . LYS   A  1  38  ? -100.56372 32.88532  21.65150  1.000 36.14484  ?  6836 LYS   A N      1 
ATOM   292  C  CA     . LYS   A  1  38  ? -101.63682 31.93766  21.91197  1.000 38.25420  ?  6836 LYS   A CA     1 
ATOM   293  C  C      . LYS   A  1  38  ? -101.28834 30.54519  21.38349  1.000 31.53132  ?  6836 LYS   A C      1 
ATOM   294  O  O      . LYS   A  1  38  ? -100.91271 30.37998  20.21566  1.000 33.16862  ?  6836 LYS   A O      1 
ATOM   295  C  CB     . LYS   A  1  38  ? -102.92739 32.44684  21.27059  1.000 37.54271  ?  6836 LYS   A CB     1 
ATOM   296  C  CG     . LYS   A  1  38  ? -104.12882 31.56980  21.52937  1.000 43.56374  ?  6836 LYS   A CG     1 
ATOM   297  C  CD     . LYS   A  1  38  ? -105.40361 32.26363  21.10835  1.000 43.81500  ?  6836 LYS   A CD     1 
ATOM   298  C  CE     . LYS   A  1  38  ? -106.52883 31.25395  20.96063  1.000 51.87311  ?  6836 LYS   A CE     1 
ATOM   299  N  NZ     . LYS   A  1  38  ? -106.27164 30.34280  19.80487  1.000 58.68848  ?  6836 LYS   A NZ     1 
ATOM   300  N  N      . GLY   A  1  39  ? -101.40518 29.54299  22.25307  1.000 34.89936  ?  6837 GLY   A N      1 
ATOM   301  C  CA     . GLY   A  1  39  ? -101.20473 28.15690  21.86011  1.000 33.99011  ?  6837 GLY   A CA     1 
ATOM   302  C  C      . GLY   A  1  39  ? -99.76813  27.70793  21.67156  1.000 35.55529  ?  6837 GLY   A C      1 
ATOM   303  O  O      . GLY   A  1  39  ? -99.55693  26.57692  21.21494  1.000 35.33349  ?  6837 GLY   A O      1 
ATOM   304  N  N      . ILE   A  1  40  ? -98.76919  28.55394  21.97912  1.000 31.48472  ?  6838 ILE   A N      1 
ATOM   305  C  CA     . ILE   A  1  40  ? -97.35903  28.19267  21.79742  1.000 33.19096  ?  6838 ILE   A CA     1 
ATOM   306  C  C      . ILE   A  1  40  ? -96.80127  27.63694  23.11136  1.000 31.41956  ?  6838 ILE   A C      1 
ATOM   307  O  O      . ILE   A  1  40  ? -96.98516  28.24158  24.17387  1.000 36.21964  ?  6838 ILE   A O      1 
ATOM   308  C  CB     . ILE   A  1  40  ? -96.53315  29.40186  21.31135  1.000 32.86284  ?  6838 ILE   A CB     1 
ATOM   309  C  CG1    . ILE   A  1  40  ? -97.00105  29.88357  19.93459  1.000 28.13474  ?  6838 ILE   A CG1    1 
ATOM   310  C  CG2    . ILE   A  1  40  ? -95.05503  29.01095  21.16323  1.000 24.78148  ?  6838 ILE   A CG2    1 
ATOM   311  C  CD1    . ILE   A  1  40  ? -96.70058  28.89827  18.79256  1.000 29.39854  ?  6838 ILE   A CD1    1 
ATOM   312  N  N      . MET   A  1  41  ? -96.12517  26.47863  23.03557  1.000 32.97131  ?  6839 MET   A N      1 
ATOM   313  C  CA     . MET   A  1  41  ? -95.48528  25.81094  24.17928  1.000 31.17489  ?  6839 MET   A CA     1 
ATOM   314  C  C      . MET   A  1  41  ? -94.18233  26.50318  24.58123  1.000 28.99454  ?  6839 MET   A C      1 
ATOM   315  O  O      . MET   A  1  41  ? -93.41833  26.95625  23.72855  1.000 30.15848  ?  6839 MET   A O      1 
ATOM   316  C  CB     . MET   A  1  41  ? -95.10557  24.35954  23.84149  1.000 33.11222  ?  6839 MET   A CB     1 
ATOM   317  C  CG     . MET   A  1  41  ? -96.18472  23.39015  23.30596  1.000 45.10538  ?  6839 MET   A CG     1 
ATOM   318  S  SD     . MET   A  1  41  ? -95.35238  21.93366  22.53094  1.000 43.85471  ?  6839 MET   A SD     1 
ATOM   319  C  CE     . MET   A  1  41  ? -96.69747  20.71531  22.47970  1.000 49.21438  ?  6839 MET   A CE     1 
ATOM   320  N  N      . MET   A  1  42  ? -93.88566  26.49006  25.88586  1.000 29.39156  ?  6840 MET   A N      1 
ATOM   321  C  CA     . MET   A  1  42  ? -92.60639  27.01185  26.37275  1.000 30.65154  ?  6840 MET   A CA     1 
ATOM   322  C  C      . MET   A  1  42  ? -91.42611  26.47171  25.57049  1.000 31.66478  ?  6840 MET   A C      1 
ATOM   323  O  O      . MET   A  1  42  ? -90.51365  27.22303  25.20225  1.000 32.42024  ?  6840 MET   A O      1 
ATOM   324  C  CB     . MET   A  1  42  ? -92.43831  26.68952  27.86453  1.000 31.22377  ?  6840 MET   A CB     1 
ATOM   325  C  CG     . MET   A  1  42  ? -91.07283  27.04255  28.41392  1.000 35.75608  ?  6840 MET   A CG     1 
ATOM   326  S  SD     . MET   A  1  42  ? -90.65433  28.79772  28.15607  1.000 40.46787  ?  6840 MET   A SD     1 
ATOM   327  C  CE     . MET   A  1  42  ? -91.66450  29.57386  29.39019  1.000 35.52812  ?  6840 MET   A CE     1 
ATOM   328  N  N      . ASN   A  1  43  ? -91.43066  25.18007  25.24569  1.000 28.43754  ?  6841 ASN   A N      1 
ATOM   329  C  CA     . ASN   A  1  43  ? -90.23141  24.64478  24.61274  1.000 28.34498  ?  6841 ASN   A CA     1 
ATOM   330  C  C      . ASN   A  1  43  ? -90.11352  25.03887  23.14995  1.000 28.64422  ?  6841 ASN   A C      1 
ATOM   331  O  O      . ASN   A  1  43  ? -88.99661  25.17290  22.63935  1.000 29.45643  ?  6841 ASN   A O      1 
ATOM   332  C  CB     . ASN   A  1  43  ? -90.16991  23.13152  24.81187  1.000 38.72369  ?  6841 ASN   A CB     1 
ATOM   333  C  CG     . ASN   A  1  43  ? -89.67665  22.78121  26.21375  1.000 50.67132  ?  6841 ASN   A CG     1 
ATOM   334  O  OD1    . ASN   A  1  43  ? -88.84921  23.50401  26.78448  1.000 51.33579  ?  6841 ASN   A OD1    1 
ATOM   335  N  ND2    . ASN   A  1  43  ? -90.24340  21.74860  26.80583  1.000 56.15444  ?  6841 ASN   A ND2    1 
ATOM   336  N  N      . VAL   A  1  44  ? -91.22413  25.28332  22.46464  1.000 27.36834  ?  6842 VAL   A N      1 
ATOM   337  C  CA     . VAL   A  1  44  ? -91.11735  25.85147  21.12314  1.000 27.40668  ?  6842 VAL   A CA     1 
ATOM   338  C  C      . VAL   A  1  44  ? -90.52193  27.25677  21.19247  1.000 25.50442  ?  6842 VAL   A C      1 
ATOM   339  O  O      . VAL   A  1  44  ? -89.63989  27.62542  20.40532  1.000 25.63829  ?  6842 VAL   A O      1 
ATOM   340  C  CB     . VAL   A  1  44  ? -92.49170  25.86651  20.43785  1.000 26.58088  ?  6842 VAL   A CB     1 
ATOM   341  C  CG1    . VAL   A  1  44  ? -92.43927  26.80269  19.26909  1.000 23.37368  ?  6842 VAL   A CG1    1 
ATOM   342  C  CG2    . VAL   A  1  44  ? -92.89584  24.42358  19.97966  1.000 25.56992  ?  6842 VAL   A CG2    1 
ATOM   343  N  N      . ALA   A  1  45  ? -91.01257  28.06191  22.13159  1.000 25.19174  ?  6843 ALA   A N      1 
ATOM   344  C  CA     . ALA   A  1  45  ? -90.52973  29.43032  22.29206  1.000 23.83614  ?  6843 ALA   A CA     1 
ATOM   345  C  C      . ALA   A  1  45  ? -89.06420  29.45446  22.68712  1.000 28.57174  ?  6843 ALA   A C      1 
ATOM   346  O  O      . ALA   A  1  45  ? -88.27476  30.24311  22.14836  1.000 26.47628  ?  6843 ALA   A O      1 
ATOM   347  C  CB     . ALA   A  1  45  ? -91.38144  30.14234  23.34396  1.000 26.30100  ?  6843 ALA   A CB     1 
ATOM   348  N  N      . LYS   A  1  46  ? -88.67966  28.58962  23.62405  1.000 26.52891  ?  6844 LYS   A N      1 
ATOM   349  C  CA     . LYS   A  1  46  ? -87.29518  28.54535  24.07423  1.000 27.09943  ?  6844 LYS   A CA     1 
ATOM   350  C  C      . LYS   A  1  46  ? -86.35646  28.19028  22.92455  1.000 26.38250  ?  6844 LYS   A C      1 
ATOM   351  O  O      . LYS   A  1  46  ? -85.35205  28.87446  22.69067  1.000 26.02863  ?  6844 LYS   A O      1 
ATOM   352  C  CB     . LYS   A  1  46  ? -87.17163  27.54381  25.21691  1.000 27.03929  ?  6844 LYS   A CB     1 
ATOM   353  C  CG     . LYS   A  1  46  ? -85.79245  27.45434  25.81737  1.000 32.58087  ?  6844 LYS   A CG     1 
ATOM   354  C  CD     . LYS   A  1  46  ? -85.70380  26.21237  26.71433  1.000 34.31172  ?  6844 LYS   A CD     1 
ATOM   355  C  CE     . LYS   A  1  46  ? -86.67608  26.26476  27.89232  1.000 33.54478  ?  6844 LYS   A CE     1 
ATOM   356  N  NZ     . LYS   A  1  46  ? -86.37825  25.15453  28.87011  1.000 34.88325  ?  6844 LYS   A NZ     1 
ATOM   357  N  N      . TYR   A  1  47  ? -86.66720  27.11906  22.18334  1.000 24.96260  ?  6845 TYR   A N      1 
ATOM   358  C  CA     . TYR   A  1  47  ? -85.81859  26.75721  21.04512  1.000 24.57433  ?  6845 TYR   A CA     1 
ATOM   359  C  C      . TYR   A  1  47  ? -85.82668  27.82891  19.96770  1.000 25.27301  ?  6845 TYR   A C      1 
ATOM   360  O  O      . TYR   A  1  47  ? -84.79999  28.08123  19.33453  1.000 25.83146  ?  6845 TYR   A O      1 
ATOM   361  C  CB     . TYR   A  1  47  ? -86.25103  25.42240  20.44918  1.000 23.85869  ?  6845 TYR   A CB     1 
ATOM   362  C  CG     . TYR   A  1  47  ? -85.62399  24.23398  21.14357  1.000 29.01204  ?  6845 TYR   A CG     1 
ATOM   363  C  CD1    . TYR   A  1  47  ? -86.00988  23.87868  22.43541  1.000 32.61356  ?  6845 TYR   A CD1    1 
ATOM   364  C  CD2    . TYR   A  1  47  ? -84.64763  23.45536  20.50212  1.000 31.26222  ?  6845 TYR   A CD2    1 
ATOM   365  C  CE1    . TYR   A  1  47  ? -85.44873  22.76087  23.07926  1.000 35.98318  ?  6845 TYR   A CE1    1 
ATOM   366  C  CE2    . TYR   A  1  47  ? -84.07610  22.34551  21.13559  1.000 30.08636  ?  6845 TYR   A CE2    1 
ATOM   367  C  CZ     . TYR   A  1  47  ? -84.48417  22.00723  22.42232  1.000 34.60714  ?  6845 TYR   A CZ     1 
ATOM   368  O  OH     . TYR   A  1  47  ? -83.94566  20.91538  23.06045  1.000 36.64044  ?  6845 TYR   A OH     1 
ATOM   369  N  N      . THR   A  1  48  ? -86.98272  28.44026  19.70528  1.000 22.87041  ?  6846 THR   A N      1 
ATOM   370  C  CA     . THR   A  1  48  ? -86.99973  29.51818  18.72024  1.000 23.44271  ?  6846 THR   A CA     1 
ATOM   371  C  C      . THR   A  1  48  ? -86.00732  30.61871  19.09087  1.000 23.76673  ?  6846 THR   A C      1 
ATOM   372  O  O      . THR   A  1  48  ? -85.22558  31.06014  18.24259  1.000 27.06285  ?  6846 THR   A O      1 
ATOM   373  C  CB     . THR   A  1  48  ? -88.41426  30.06917  18.57617  1.000 27.51894  ?  6846 THR   A CB     1 
ATOM   374  O  OG1    . THR   A  1  48  ? -89.27530  29.01154  18.14004  1.000 28.16340  ?  6846 THR   A OG1    1 
ATOM   375  C  CG2    . THR   A  1  48  ? -88.46210  31.18627  17.51380  1.000 29.58750  ?  6846 THR   A CG2    1 
ATOM   376  N  N      . GLN   A  1  49  ? -85.97753  31.03170  20.36657  1.000 26.50407  ?  6847 GLN   A N      1 
ATOM   377  C  CA     . GLN   A  1  49  ? -85.06484  32.10687  20.76930  1.000 23.79452  ?  6847 GLN   A CA     1 
ATOM   378  C  C      . GLN   A  1  49  ? -83.61337  31.64484  20.73974  1.000 25.01949  ?  6847 GLN   A C      1 
ATOM   379  O  O      . GLN   A  1  49  ? -82.71529  32.41531  20.37409  1.000 26.11535  ?  6847 GLN   A O      1 
ATOM   380  C  CB     . GLN   A  1  49  ? -85.44248  32.63673  22.14856  1.000 24.90465  ?  6847 GLN   A CB     1 
ATOM   381  C  CG     . GLN   A  1  49  ? -86.61526  33.66897  22.06029  1.000 24.23197  ?  6847 GLN   A CG     1 
ATOM   382  C  CD     . GLN   A  1  49  ? -87.04978  34.20992  23.40097  1.000 28.00436  ?  6847 GLN   A CD     1 
ATOM   383  O  OE1    . GLN   A  1  49  ? -86.79696  33.61463  24.46289  1.000 26.52548  ?  6847 GLN   A OE1    1 
ATOM   384  N  NE2    . GLN   A  1  49  ? -87.72090  35.36533  23.36486  1.000 27.11338  ?  6847 GLN   A NE2    1 
ATOM   385  N  N      . LEU   A  1  50  ? -83.35751  30.38191  21.09153  1.000 23.28166  ?  6848 LEU   A N      1 
ATOM   386  C  CA     . LEU   A  1  50  ? -81.99661  29.86410  20.95842  1.000 24.29762  ?  6848 LEU   A CA     1 
ATOM   387  C  C      . LEU   A  1  50  ? -81.52957  29.94901  19.51057  1.000 26.14403  ?  6848 LEU   A C      1 
ATOM   388  O  O      . LEU   A  1  50  ? -80.41112  30.39200  19.23378  1.000 28.68244  ?  6848 LEU   A O      1 
ATOM   389  C  CB     . LEU   A  1  50  ? -81.92790  28.42607  21.47016  1.000 24.26372  ?  6848 LEU   A CB     1 
ATOM   390  C  CG     . LEU   A  1  50  ? -80.63707  27.68159  21.13954  1.000 27.14385  ?  6848 LEU   A CG     1 
ATOM   391  C  CD1    . LEU   A  1  50  ? -79.48635  28.40762  21.82012  1.000 25.28770  ?  6848 LEU   A CD1    1 
ATOM   392  C  CD2    . LEU   A  1  50  ? -80.69922  26.18551  21.61069  1.000 25.22457  ?  6848 LEU   A CD2    1 
ATOM   393  N  N      . CYS   A  1  51  ? -82.38565  29.53883  18.56440  1.000 24.21530  ?  6849 CYS   A N      1 
ATOM   394  C  CA     . CYS   A  1  51  ? -82.02194  29.60616  17.14915  1.000 23.13559  ?  6849 CYS   A CA     1 
ATOM   395  C  C      . CYS   A  1  51  ? -81.87496  31.04994  16.67052  1.000 26.26987  ?  6849 CYS   A C      1 
ATOM   396  O  O      . CYS   A  1  51  ? -81.00139  31.34449  15.84422  1.000 25.72521  ?  6849 CYS   A O      1 
ATOM   397  C  CB     . CYS   A  1  51  ? -83.06189  28.86569  16.30076  1.000 25.85119  ?  6849 CYS   A CB     1 
ATOM   398  S  SG     . CYS   A  1  51  ? -82.96445  27.01741  16.53173  1.000 28.11640  ?  6849 CYS   A SG     1 
ATOM   399  N  N      . GLN   A  1  52  ? -82.74899  31.94937  17.12811  1.000 25.88380  ?  6850 GLN   A N      1 
ATOM   400  C  CA     . GLN   A  1  52  ? -82.60207  33.35845  16.74697  1.000 25.77648  ?  6850 GLN   A CA     1 
ATOM   401  C  C      . GLN   A  1  52  ? -81.25358  33.90473  17.19855  1.000 30.78788  ?  6850 GLN   A C      1 
ATOM   402  O  O      . GLN   A  1  52  ? -80.60448  34.67312  16.46664  1.000 30.48942  ?  6850 GLN   A O      1 
ATOM   403  C  CB     . GLN   A  1  52  ? -83.73381  34.19849  17.33321  1.000 25.62243  ?  6850 GLN   A CB     1 
ATOM   404  C  CG     . GLN   A  1  52  ? -85.09107  33.91602  16.73193  1.000 24.35452  ?  6850 GLN   A CG     1 
ATOM   405  C  CD     . GLN   A  1  52  ? -86.18719  34.70990  17.39925  1.000 29.52836  ?  6850 GLN   A CD     1 
ATOM   406  O  OE1    . GLN   A  1  52  ? -86.19418  34.89057  18.62274  1.000 27.46290  ?  6850 GLN   A OE1    1 
ATOM   407  N  NE2    . GLN   A  1  52  ? -87.13814  35.17895  16.60316  1.000 32.21308  ?  6850 GLN   A NE2    1 
ATOM   408  N  N      . TYR   A  1  53  ? -80.79749  33.49772  18.38781  1.000 28.42987  ?  6851 TYR   A N      1 
ATOM   409  C  CA     . TYR   A  1  53  ? -79.48258  33.94265  18.84170  1.000 28.77895  ?  6851 TYR   A CA     1 
ATOM   410  C  C      . TYR   A  1  53  ? -78.35806  33.26120  18.05793  1.000 33.70446  ?  6851 TYR   A C      1 
ATOM   411  O  O      . TYR   A  1  53  ? -77.34644  33.89780  17.71156  1.000 29.15444  ?  6851 TYR   A O      1 
ATOM   412  C  CB     . TYR   A  1  53  ? -79.32855  33.69237  20.34186  1.000 26.76721  ?  6851 TYR   A CB     1 
ATOM   413  C  CG     . TYR   A  1  53  ? -77.96452  34.10641  20.82839  1.000 28.09182  ?  6851 TYR   A CG     1 
ATOM   414  C  CD1    . TYR   A  1  53  ? -77.61544  35.45051  20.89997  1.000 26.84894  ?  6851 TYR   A CD1    1 
ATOM   415  C  CD2    . TYR   A  1  53  ? -77.00868  33.15358  21.14833  1.000 28.12124  ?  6851 TYR   A CD2    1 
ATOM   416  C  CE1    . TYR   A  1  53  ? -76.32838  35.83784  21.31261  1.000 31.92110  ?  6851 TYR   A CE1    1 
ATOM   417  C  CE2    . TYR   A  1  53  ? -75.73876  33.52471  21.56715  1.000 29.51233  ?  6851 TYR   A CE2    1 
ATOM   418  C  CZ     . TYR   A  1  53  ? -75.40765  34.86454  21.64359  1.000 30.66323  ?  6851 TYR   A CZ     1 
ATOM   419  O  OH     . TYR   A  1  53  ? -74.14404  35.22784  22.06172  1.000 35.13094  ?  6851 TYR   A OH     1 
ATOM   420  N  N      . LEU   A  1  54  ? -78.49865  31.96402  17.76974  1.000 27.29387  ?  6852 LEU   A N      1 
ATOM   421  C  CA     . LEU   A  1  54  ? -77.47484  31.31084  16.96332  1.000 27.16558  ?  6852 LEU   A CA     1 
ATOM   422  C  C      . LEU   A  1  54  ? -77.37944  31.93104  15.57224  1.000 30.06126  ?  6852 LEU   A C      1 
ATOM   423  O  O      . LEU   A  1  54  ? -76.31182  31.90327  14.96520  1.000 29.73601  ?  6852 LEU   A O      1 
ATOM   424  C  CB     . LEU   A  1  54  ? -77.73969  29.79735  16.87341  1.000 28.57984  ?  6852 LEU   A CB     1 
ATOM   425  C  CG     . LEU   A  1  54  ? -77.65746  29.00632  18.18183  1.000 27.28968  ?  6852 LEU   A CG     1 
ATOM   426  C  CD1    . LEU   A  1  54  ? -78.06857  27.54398  17.95227  1.000 26.50947  ?  6852 LEU   A CD1    1 
ATOM   427  C  CD2    . LEU   A  1  54  ? -76.24487  29.07694  18.79038  1.000 27.82689  ?  6852 LEU   A CD2    1 
ATOM   428  N  N      . ASN   A  1  55  ? -78.46318  32.53368  15.06958  1.000 29.32724  ?  6853 ASN   A N      1 
ATOM   429  C  CA     . ASN   A  1  55  ? -78.38596  33.24242  13.79380  1.000 31.36911  ?  6853 ASN   A CA     1 
ATOM   430  C  C      . ASN   A  1  55  ? -77.40271  34.40761  13.82744  1.000 32.70259  ?  6853 ASN   A C      1 
ATOM   431  O  O      . ASN   A  1  55  ? -77.00158  34.88958  12.76745  1.000 32.71457  ?  6853 ASN   A O      1 
ATOM   432  C  CB     . ASN   A  1  55  ? -79.76666  33.76487  13.39077  1.000 28.08536  ?  6853 ASN   A CB     1 
ATOM   433  C  CG     . ASN   A  1  55  ? -80.63883  32.68644  12.77189  1.000 30.77266  ?  6853 ASN   A CG     1 
ATOM   434  O  OD1    . ASN   A  1  55  ? -80.13668  31.69277  12.25477  1.000 29.67850  ?  6853 ASN   A OD1    1 
ATOM   435  N  ND2    . ASN   A  1  55  ? -81.94400  32.88895  12.80005  1.000 33.62007  ?  6853 ASN   A ND2    1 
ATOM   436  N  N      . THR   A  1  56  ? -77.02655  34.89867  15.00435  1.000 32.14242  ?  6854 THR   A N      1 
ATOM   437  C  CA     . THR   A  1  56  ? -76.11610  36.03461  15.06623  1.000 31.09163  ?  6854 THR   A CA     1 
ATOM   438  C  C      . THR   A  1  56  ? -74.66374  35.61278  15.16990  1.000 34.60481  ?  6854 THR   A C      1 
ATOM   439  O  O      . THR   A  1  56  ? -73.79456  36.48039  15.23981  1.000 34.16125  ?  6854 THR   A O      1 
ATOM   440  C  CB     . THR   A  1  56  ? -76.45890  36.94803  16.25072  1.000 34.49372  ?  6854 THR   A CB     1 
ATOM   441  O  OG1    . THR   A  1  56  ? -76.13041  36.28239  17.48414  1.000 32.28367  ?  6854 THR   A OG1    1 
ATOM   442  C  CG2    . THR   A  1  56  ? -77.95447  37.29717  16.24627  1.000 31.82552  ?  6854 THR   A CG2    1 
ATOM   443  N  N      . LEU   A  1  57  ? -74.37256  34.31682  15.20709  1.000 29.82950  ?  6855 LEU   A N      1 
ATOM   444  C  CA     . LEU   A  1  57  ? -73.00098  33.85826  15.36719  1.000 30.35140  ?  6855 LEU   A CA     1 
ATOM   445  C  C      . LEU   A  1  57  ? -72.46221  33.37396  14.02875  1.000 33.20155  ?  6855 LEU   A C      1 
ATOM   446  O  O      . LEU   A  1  57  ? -73.17798  33.29920  13.03638  1.000 34.73460  ?  6855 LEU   A O      1 
ATOM   447  C  CB     . LEU   A  1  57  ? -72.92380  32.74136  16.41559  1.000 34.89825  ?  6855 LEU   A CB     1 
ATOM   448  C  CG     . LEU   A  1  57  ? -73.61818  33.02934  17.75134  1.000 34.46429  ?  6855 LEU   A CG     1 
ATOM   449  C  CD1    . LEU   A  1  57  ? -73.53390  31.79656  18.60627  1.000 30.47684  ?  6855 LEU   A CD1    1 
ATOM   450  C  CD2    . LEU   A  1  57  ? -72.95582  34.22566  18.45509  1.000 32.62447  ?  6855 LEU   A CD2    1 
ATOM   451  N  N      . THR   A  1  58  ? -71.18209  33.02967  14.00818  1.000 32.60389  ?  6856 THR   A N      1 
ATOM   452  C  CA     . THR   A  1  58  ? -70.54212  32.58148  12.77133  1.000 33.22020  ?  6856 THR   A CA     1 
ATOM   453  C  C      . THR   A  1  58  ? -70.57215  31.05090  12.65716  1.000 36.26905  ?  6856 THR   A C      1 
ATOM   454  O  O      . THR   A  1  58  ? -69.54227  30.37269  12.58069  1.000 34.89039  ?  6856 THR   A O      1 
ATOM   455  C  CB     . THR   A  1  58  ? -69.12217  33.12649  12.70101  1.000 34.82325  ?  6856 THR   A CB     1 
ATOM   456  O  OG1    . THR   A  1  58  ? -68.37704  32.67569  13.84004  1.000 34.13233  ?  6856 THR   A OG1    1 
ATOM   457  C  CG2    . THR   A  1  58  ? -69.15328  34.65743  12.69416  1.000 38.26103  ?  6856 THR   A CG2    1 
ATOM   458  N  N      . LEU   A  1  59  ? -71.79171  30.50942  12.64217  1.000 31.30338  ?  6857 LEU   A N      1 
ATOM   459  C  CA     . LEU   A  1  59  ? -71.96813  29.07090  12.47087  1.000 35.83508  ?  6857 LEU   A CA     1 
ATOM   460  C  C      . LEU   A  1  59  ? -71.56903  28.62595  11.06716  1.000 36.01772  ?  6857 LEU   A C      1 
ATOM   461  O  O      . LEU   A  1  59  ? -71.91841  29.26491  10.06617  1.000 35.26634  ?  6857 LEU   A O      1 
ATOM   462  C  CB     . LEU   A  1  59  ? -73.42258  28.66719  12.70674  1.000 33.20930  ?  6857 LEU   A CB     1 
ATOM   463  C  CG     . LEU   A  1  59  ? -74.06073  28.86170  14.06884  1.000 41.41256  ?  6857 LEU   A CG     1 
ATOM   464  C  CD1    . LEU   A  1  59  ? -75.31427  27.99088  14.15687  1.000 37.83639  ?  6857 LEU   A CD1    1 
ATOM   465  C  CD2    . LEU   A  1  59  ? -73.08460  28.55292  15.19376  1.000 40.05361  ?  6857 LEU   A CD2    1 
ATOM   466  N  N      . ALA   A  1  60  ? -70.83780  27.51670  10.99513  1.000 33.22242  ?  6858 ALA   A N      1 
ATOM   467  C  CA     . ALA   A  1  60  ? -70.59411  26.87258  9.71170   1.000 33.27484  ?  6858 ALA   A CA     1 
ATOM   468  C  C      . ALA   A  1  60  ? -71.86543  26.16876  9.24934   1.000 35.94889  ?  6858 ALA   A C      1 
ATOM   469  O  O      . ALA   A  1  60  ? -72.49087  25.43002  10.02110  1.000 34.84752  ?  6858 ALA   A O      1 
ATOM   470  C  CB     . ALA   A  1  60  ? -69.44541  25.87399  9.83112   1.000 31.06536  ?  6858 ALA   A CB     1 
ATOM   471  N  N      . VAL   A  1  61  ? -72.25700  26.39672  7.99792   1.000 30.03025  ?  6859 VAL   A N      1 
ATOM   472  C  CA     . VAL   A  1  61  ? -73.47747  25.78056  7.48031   1.000 34.11145  ?  6859 VAL   A CA     1 
ATOM   473  C  C      . VAL   A  1  61  ? -73.17588  25.10623  6.14484   1.000 38.75699  ?  6859 VAL   A C      1 
ATOM   474  O  O      . VAL   A  1  61  ? -73.45116  25.67071  5.07683   1.000 32.93680  ?  6859 VAL   A O      1 
ATOM   475  C  CB     . VAL   A  1  61  ? -74.61495  26.80854  7.36030   1.000 34.79633  ?  6859 VAL   A CB     1 
ATOM   476  C  CG1    . VAL   A  1  61  ? -75.93112  26.11230  6.99085   1.000 34.42969  ?  6859 VAL   A CG1    1 
ATOM   477  C  CG2    . VAL   A  1  61  ? -74.76560  27.60110  8.66578   1.000 36.21703  ?  6859 VAL   A CG2    1 
ATOM   478  N  N      . PRO   A  1  62  ? -72.62151  23.90224  6.15823   1.000 35.35842  ?  6860 PRO   A N      1 
ATOM   479  C  CA     . PRO   A  1  62  ? -72.29449  23.21904  4.90720   1.000 38.25435  ?  6860 PRO   A CA     1 
ATOM   480  C  C      . PRO   A  1  62  ? -73.52985  22.64841  4.22856   1.000 43.62147  ?  6860 PRO   A C      1 
ATOM   481  O  O      . PRO   A  1  62  ? -74.60512  22.52508  4.82208   1.000 37.64939  ?  6860 PRO   A O      1 
ATOM   482  C  CB     . PRO   A  1  62  ? -71.36089  22.09296  5.35662   1.000 38.18455  ?  6860 PRO   A CB     1 
ATOM   483  C  CG     . PRO   A  1  62  ? -71.76378  21.82350  6.75829   1.000 38.35482  ?  6860 PRO   A CG     1 
ATOM   484  C  CD     . PRO   A  1  62  ? -72.17204  23.15009  7.33771   1.000 35.26227  ?  6860 PRO   A CD     1 
ATOM   485  N  N      . TYR   A  1  63  ? -73.35468  22.30197  2.95029   1.000 42.99283  ?  6861 TYR   A N      1 
ATOM   486  C  CA     . TYR   A  1  63  ? -74.29735  21.39479  2.31153   1.000 44.97101  ?  6861 TYR   A CA     1 
ATOM   487  C  C      . TYR   A  1  63  ? -74.24892  20.06638  3.04721   1.000 38.29364  ?  6861 TYR   A C      1 
ATOM   488  O  O      . TYR   A  1  63  ? -73.21090  19.67322  3.57692   1.000 41.03400  ?  6861 TYR   A O      1 
ATOM   489  C  CB     . TYR   A  1  63  ? -73.95822  21.20099  0.82501   1.000 45.76408  ?  6861 TYR   A CB     1 
ATOM   490  C  CG     . TYR   A  1  63  ? -74.19042  22.43280  -0.00905  1.000 45.88259  ?  6861 TYR   A CG     1 
ATOM   491  C  CD1    . TYR   A  1  63  ? -75.47741  22.82243  -0.35067  1.000 52.26077  ?  6861 TYR   A CD1    1 
ATOM   492  C  CD2    . TYR   A  1  63  ? -73.12576  23.21572  -0.45061  1.000 46.86826  ?  6861 TYR   A CD2    1 
ATOM   493  C  CE1    . TYR   A  1  63  ? -75.70410  23.95487  -1.09496  1.000 51.60946  ?  6861 TYR   A CE1    1 
ATOM   494  C  CE2    . TYR   A  1  63  ? -73.34475  24.35313  -1.20342  1.000 45.58064  ?  6861 TYR   A CE2    1 
ATOM   495  C  CZ     . TYR   A  1  63  ? -74.63358  24.71628  -1.51915  1.000 50.68032  ?  6861 TYR   A CZ     1 
ATOM   496  O  OH     . TYR   A  1  63  ? -74.87424  25.83978  -2.26608  1.000 59.81318  ?  6861 TYR   A OH     1 
ATOM   497  N  N      . ASN   A  1  64  ? -75.38258  19.37859  3.10504   1.000 46.26593  ?  6862 ASN   A N      1 
ATOM   498  C  CA     . ASN   A  1  64  ? -75.45573  18.09633  3.80493   1.000 46.19849  ?  6862 ASN   A CA     1 
ATOM   499  C  C      . ASN   A  1  64  ? -74.94630  18.24237  5.23759   1.000 41.70344  ?  6862 ASN   A C      1 
ATOM   500  O  O      . ASN   A  1  64  ? -74.08632  17.49820  5.71007   1.000 40.30311  ?  6862 ASN   A O      1 
ATOM   501  C  CB     . ASN   A  1  64  ? -74.68654  17.01960  3.04659   1.000 43.52266  ?  6862 ASN   A CB     1 
ATOM   502  C  CG     . ASN   A  1  64  ? -75.29472  16.73634  1.68944   1.000 61.23824  ?  6862 ASN   A CG     1 
ATOM   503  O  OD1    . ASN   A  1  64  ? -76.52462  16.65874  1.54249   1.000 63.91699  ?  6862 ASN   A OD1    1 
ATOM   504  N  ND2    . ASN   A  1  64  ? -74.43975  16.60744  0.67849   1.000 63.80497  ?  6862 ASN   A ND2    1 
ATOM   505  N  N      . MET   A  1  65  ? -75.47754  19.25026  5.91202   1.000 40.12096  ?  6863 MET   A N      1 
ATOM   506  C  CA     . MET   A  1  65  ? -75.16370  19.50408  7.30192   1.000 36.66687  ?  6863 MET   A CA     1 
ATOM   507  C  C      . MET   A  1  65  ? -75.69866  18.37079  8.17335   1.000 34.02024  ?  6863 MET   A C      1 
ATOM   508  O  O      . MET   A  1  65  ? -76.72639  17.76113  7.87117   1.000 36.51170  ?  6863 MET   A O      1 
ATOM   509  C  CB     . MET   A  1  65  ? -75.77809  20.84409  7.70616   1.000 33.40813  ?  6863 MET   A CB     1 
ATOM   510  C  CG     . MET   A  1  65  ? -75.43552  21.30917  9.09260   1.000 33.98800  ?  6863 MET   A CG     1 
ATOM   511  S  SD     . MET   A  1  65  ? -76.16693  22.91124  9.39750   1.000 38.88704  ?  6863 MET   A SD     1 
ATOM   512  C  CE     . MET   A  1  65  ? -75.40066  23.30743  10.97724  1.000 30.50813  ?  6863 MET   A CE     1 
ATOM   513  N  N      . ARG   A  1  66  ? -74.98774  18.08461  9.26217   1.000 32.34262  ?  6864 ARG   A N      1 
ATOM   514  C  CA     . ARG   A  1  66  ? -75.35276  17.01892  10.19141  1.000 34.33866  ?  6864 ARG   A CA     1 
ATOM   515  C  C      . ARG   A  1  66  ? -75.53269  17.60361  11.58577  1.000 32.89334  ?  6864 ARG   A C      1 
ATOM   516  O  O      . ARG   A  1  66  ? -74.58949  18.17496  12.14744  1.000 30.82364  ?  6864 ARG   A O      1 
ATOM   517  C  CB     . ARG   A  1  66  ? -74.27536  15.93440  10.20972  1.000 35.77275  ?  6864 ARG   A CB     1 
ATOM   518  C  CG     . ARG   A  1  66  ? -73.88360  15.46051  8.83580   1.000 36.22454  ?  6864 ARG   A CG     1 
ATOM   519  C  CD     . ARG   A  1  66  ? -72.43978  15.01868  8.85005   1.000 41.77472  ?  6864 ARG   A CD     1 
ATOM   520  N  NE     . ARG   A  1  66  ? -72.10219  14.18862  7.70216   1.000 41.00552  ?  6864 ARG   A NE     1 
ATOM   521  C  CZ     . ARG   A  1  66  ? -71.05499  13.38012  7.67505   1.000 43.38499  ?  6864 ARG   A CZ     1 
ATOM   522  N  NH1    . ARG   A  1  66  ? -70.22911  13.29110  8.70440   1.000 40.74080  ?  6864 ARG   A NH1    1 
ATOM   523  N  NH2    . ARG   A  1  66  ? -70.83006  12.64179  6.59142   1.000 45.98791  ?  6864 ARG   A NH2    1 
ATOM   524  N  N      . VAL   A  1  67  ? -76.72675  17.44325  12.15145  1.000 26.73122  ?  6865 VAL   A N      1 
ATOM   525  C  CA     . VAL   A  1  67  ? -77.04803  17.96606  13.47421  1.000 28.91189  ?  6865 VAL   A CA     1 
ATOM   526  C  C      . VAL   A  1  67  ? -77.58576  16.82775  14.32909  1.000 30.49715  ?  6865 VAL   A C      1 
ATOM   527  O  O      . VAL   A  1  67  ? -78.45755  16.07226  13.88175  1.000 31.38786  ?  6865 VAL   A O      1 
ATOM   528  C  CB     . VAL   A  1  67  ? -78.09192  19.09333  13.38482  1.000 26.57865  ?  6865 VAL   A CB     1 
ATOM   529  C  CG1    . VAL   A  1  67  ? -78.38340  19.67592  14.77141  1.000 29.18001  ?  6865 VAL   A CG1    1 
ATOM   530  C  CG2    . VAL   A  1  67  ? -77.63823  20.15423  12.39495  1.000 27.10154  ?  6865 VAL   A CG2    1 
ATOM   531  N  N      . ILE   A  1  68  ? -77.11421  16.73257  15.57065  1.000 28.52110  ?  6866 ILE   A N      1 
ATOM   532  C  CA     . ILE   A  1  68  ? -77.64097  15.74973  16.51176  1.000 27.97103  ?  6866 ILE   A CA     1 
ATOM   533  C  C      . ILE   A  1  68  ? -78.15496  16.46880  17.75157  1.000 32.19136  ?  6866 ILE   A C      1 
ATOM   534  O  O      . ILE   A  1  68  ? -77.52564  17.40431  18.26116  1.000 27.48150  ?  6866 ILE   A O      1 
ATOM   535  C  CB     . ILE   A  1  68  ? -76.59421  14.68207  16.87584  1.000 28.87226  ?  6866 ILE   A CB     1 
ATOM   536  C  CG1    . ILE   A  1  68  ? -77.22169  13.60607  17.75984  1.000 30.54804  ?  6866 ILE   A CG1    1 
ATOM   537  C  CG2    . ILE   A  1  68  ? -75.38145  15.31316  17.53343  1.000 27.41488  ?  6866 ILE   A CG2    1 
ATOM   538  C  CD1    . ILE   A  1  68  ? -76.42649  12.30767  17.74917  1.000 30.40354  ?  6866 ILE   A CD1    1 
ATOM   539  N  N      . HIS   A  1  69  ? -79.31141  16.02733  18.22716  1.000 26.49365  ?  6867 HIS   A N      1 
ATOM   540  C  CA     . HIS   A  1  69  ? -80.05908  16.69649  19.28634  1.000 28.31014  ?  6867 HIS   A CA     1 
ATOM   541  C  C      . HIS   A  1  69  ? -80.32304  15.70078  20.41434  1.000 29.39707  ?  6867 HIS   A C      1 
ATOM   542  O  O      . HIS   A  1  69  ? -81.15933  14.80726  20.26225  1.000 26.89637  ?  6867 HIS   A O      1 
ATOM   543  C  CB     . HIS   A  1  69  ? -81.37304  17.23853  18.70777  1.000 24.94164  ?  6867 HIS   A CB     1 
ATOM   544  C  CG     . HIS   A  1  69  ? -82.25125  17.94629  19.69242  1.000 25.54214  ?  6867 HIS   A CG     1 
ATOM   545  N  ND1    . HIS   A  1  69  ? -83.60885  18.10296  19.48688  1.000 22.44269  ?  6867 HIS   A ND1    1 
ATOM   546  C  CD2    . HIS   A  1  69  ? -81.97262  18.57432  20.85987  1.000 25.83642  ?  6867 HIS   A CD2    1 
ATOM   547  C  CE1    . HIS   A  1  69  ? -84.13075  18.77835  20.49720  1.000 24.90700  ?  6867 HIS   A CE1    1 
ATOM   548  N  NE2    . HIS   A  1  69  ? -83.15906  19.08611  21.33873  1.000 24.67814  ?  6867 HIS   A NE2    1 
ATOM   549  N  N      . PHE   A  1  70  ? -79.62170  15.84762  21.54064  1.000 26.42601  ?  6868 PHE   A N      1 
ATOM   550  C  CA     . PHE   A  1  70  ? -79.83544  14.99998  22.71080  1.000 24.37087  ?  6868 PHE   A CA     1 
ATOM   551  C  C      . PHE   A  1  70  ? -80.85707  15.61406  23.65519  1.000 30.67799  ?  6868 PHE   A C      1 
ATOM   552  O  O      . PHE   A  1  70  ? -80.98375  16.83535  23.75301  1.000 27.27538  ?  6868 PHE   A O      1 
ATOM   553  C  CB     . PHE   A  1  70  ? -78.52806  14.77482  23.46648  1.000 24.08557  ?  6868 PHE   A CB     1 
ATOM   554  C  CG     . PHE   A  1  70  ? -77.48642  14.06646  22.65823  1.000 29.34350  ?  6868 PHE   A CG     1 
ATOM   555  C  CD1    . PHE   A  1  70  ? -77.49953  12.68294  22.54951  1.000 30.15270  ?  6868 PHE   A CD1    1 
ATOM   556  C  CD2    . PHE   A  1  70  ? -76.51352  14.77556  21.99493  1.000 31.10510  ?  6868 PHE   A CD2    1 
ATOM   557  C  CE1    . PHE   A  1  70  ? -76.54541  12.02269  21.80113  1.000 31.86121  ?  6868 PHE   A CE1    1 
ATOM   558  C  CE2    . PHE   A  1  70  ? -75.53895  14.11716  21.24482  1.000 30.52340  ?  6868 PHE   A CE2    1 
ATOM   559  C  CZ     . PHE   A  1  70  ? -75.56576  12.73797  21.15305  1.000 31.30030  ?  6868 PHE   A CZ     1 
ATOM   560  N  N      . GLY   A  1  71  ? -81.55310  14.75400  24.39187  1.000 28.44664  ?  6869 GLY   A N      1 
ATOM   561  C  CA     . GLY   A  1  71  ? -82.59742  15.21832  25.29160  1.000 28.30238  ?  6869 GLY   A CA     1 
ATOM   562  C  C      . GLY   A  1  71  ? -83.80336  15.78491  24.57789  1.000 28.68897  ?  6869 GLY   A C      1 
ATOM   563  O  O      . GLY   A  1  71  ? -84.37917  16.77735  25.03508  1.000 28.19634  ?  6869 GLY   A O      1 
ATOM   564  N  N      . ALA   A  1  72  ? -84.21387  15.16278  23.47105  1.000 27.14376  ?  6870 ALA   A N      1 
ATOM   565  C  CA     . ALA   A  1  72  ? -85.21637  15.71747  22.57547  1.000 25.47261  ?  6870 ALA   A CA     1 
ATOM   566  C  C      . ALA   A  1  72  ? -86.65192  15.37393  22.95288  1.000 29.98548  ?  6870 ALA   A C      1 
ATOM   567  O  O      . ALA   A  1  72  ? -87.57514  16.00515  22.43425  1.000 33.29713  ?  6870 ALA   A O      1 
ATOM   568  C  CB     . ALA   A  1  72  ? -84.94214  15.23486  21.14384  1.000 25.27078  ?  6870 ALA   A CB     1 
ATOM   569  N  N      . GLY   A  1  73  ? -86.87797  14.37761  23.80367  1.000 32.37807  ?  6871 GLY   A N      1 
ATOM   570  C  CA     . GLY   A  1  73  ? -88.24708  14.00621  24.15754  1.000 31.95863  ?  6871 GLY   A CA     1 
ATOM   571  C  C      . GLY   A  1  73  ? -88.83376  14.87610  25.25765  1.000 37.87251  ?  6871 GLY   A C      1 
ATOM   572  O  O      . GLY   A  1  73  ? -88.13909  15.34102  26.15077  1.000 44.92396  ?  6871 GLY   A O      1 
ATOM   573  N  N      . SER   A  1  74  ? -90.14292  15.09369  25.19018  1.000 40.87311  ?  6872 SER   A N      1 
ATOM   574  C  CA     . SER   A  1  74  ? -90.87774  15.77396  26.24623  1.000 43.83233  ?  6872 SER   A CA     1 
ATOM   575  C  C      . SER   A  1  74  ? -91.71980  14.76160  27.01034  1.000 47.65916  ?  6872 SER   A C      1 
ATOM   576  O  O      . SER   A  1  74  ? -91.97480  13.65195  26.53403  1.000 41.57897  ?  6872 SER   A O      1 
ATOM   577  C  CB     . SER   A  1  74  ? -91.77332  16.87939  25.67681  1.000 42.61812  ?  6872 SER   A CB     1 
ATOM   578  O  OG     . SER   A  1  74  ? -92.85874  16.34454  24.93265  1.000 42.56142  ?  6872 SER   A OG     1 
ATOM   579  N  N      . ASP   A  1  75  ? -92.15937  15.15405  28.20705  1.000 46.39940  ?  6873 ASP   A N      1 
ATOM   580  C  CA     . ASP   A  1  75  ? -93.10725  14.31245  28.92997  1.000 49.22926  ?  6873 ASP   A CA     1 
ATOM   581  C  C      . ASP   A  1  75  ? -94.43369  14.18654  28.19211  1.000 49.90811  ?  6873 ASP   A C      1 
ATOM   582  O  O      . ASP   A  1  75  ? -95.25879  13.35163  28.57090  1.000 50.34900  ?  6873 ASP   A O      1 
ATOM   583  C  CB     . ASP   A  1  75  ? -93.34146  14.84928  30.34698  1.000 49.96383  ?  6873 ASP   A CB     1 
ATOM   584  C  CG     . ASP   A  1  75  ? -93.93020  16.25200  30.36696  1.000 58.13994  ?  6873 ASP   A CG     1 
ATOM   585  O  OD1    . ASP   A  1  75  ? -94.17949  16.82665  29.28319  1.000 60.12124  ?  6873 ASP   A OD1    1 
ATOM   586  O  OD2    . ASP   A  1  75  ? -94.12832  16.79320  31.48345  1.000 61.14714  ?  6873 ASP   A OD2    1 
ATOM   587  N  N      . LYS   A  1  76  ? -94.65229  14.98545  27.14710  1.000 46.28647  ?  6874 LYS   A N      1 
ATOM   588  C  CA     . LYS   A  1  76  ? -95.83396  14.86353  26.30619  1.000 46.41081  ?  6874 LYS   A CA     1 
ATOM   589  C  C      . LYS   A  1  76  ? -95.68819  13.78919  25.23665  1.000 40.16874  ?  6874 LYS   A C      1 
ATOM   590  O  O      . LYS   A  1  76  ? -96.64090  13.55765  24.48692  1.000 43.25630  ?  6874 LYS   A O      1 
ATOM   591  C  CB     . LYS   A  1  76  ? -96.13320  16.20851  25.63328  1.000 48.33842  ?  6874 LYS   A CB     1 
ATOM   592  C  CG     . LYS   A  1  76  ? -95.69068  17.45054  26.42085  1.000 53.68222  ?  6874 LYS   A CG     1 
ATOM   593  C  CD     . LYS   A  1  76  ? -95.28690  18.60851  25.47223  1.000 54.40261  ?  6874 LYS   A CD     1 
ATOM   594  C  CE     . LYS   A  1  76  ? -95.21221  19.97199  26.20170  1.000 60.71356  ?  6874 LYS   A CE     1 
ATOM   595  N  NZ     . LYS   A  1  76  ? -96.54808  20.59268  26.52895  1.000 57.57572  ?  6874 LYS   A NZ     1 
ATOM   596  N  N      . GLY   A  1  77  ? -94.52255  13.15196  25.11679  1.000 33.23208  ?  6875 GLY   A N      1 
ATOM   597  C  CA     . GLY   A  1  77  ? -94.30779  12.15690  24.07885  1.000 33.40544  ?  6875 GLY   A CA     1 
ATOM   598  C  C      . GLY   A  1  77  ? -93.98694  12.69833  22.69902  1.000 37.56230  ?  6875 GLY   A C      1 
ATOM   599  O  O      . GLY   A  1  77  ? -93.95363  11.91522  21.73930  1.000 34.12801  ?  6875 GLY   A O      1 
ATOM   600  N  N      . VAL   A  1  78  ? -93.74545  14.00741  22.55969  1.000 32.01790  ?  6876 VAL   A N      1 
ATOM   601  C  CA     . VAL   A  1  78  ? -93.39136  14.60074  21.27234  1.000 29.38173  ?  6876 VAL   A CA     1 
ATOM   602  C  C      . VAL   A  1  78  ? -92.04592  15.31657  21.41534  1.000 33.99112  ?  6876 VAL   A C      1 
ATOM   603  O  O      . VAL   A  1  78  ? -91.41123  15.25085  22.47050  1.000 34.53932  ?  6876 VAL   A O      1 
ATOM   604  C  CB     . VAL   A  1  78  ? -94.49535  15.55596  20.79084  1.000 30.61698  ?  6876 VAL   A CB     1 
ATOM   605  C  CG1    . VAL   A  1  78  ? -95.76896  14.76390  20.49319  1.000 30.76944  ?  6876 VAL   A CG1    1 
ATOM   606  C  CG2    . VAL   A  1  78  ? -94.75570  16.62014  21.84558  1.000 29.76199  ?  6876 VAL   A CG2    1 
ATOM   607  N  N      . ALA   A  1  79  ? -91.59276  15.99367  20.36149  1.000 29.14004  ?  6877 ALA   A N      1 
ATOM   608  C  CA     . ALA   A  1  79  ? -90.26108  16.60104  20.31940  1.000 27.21741  ?  6877 ALA   A CA     1 
ATOM   609  C  C      . ALA   A  1  79  ? -90.38359  18.02952  19.80598  1.000 30.99070  ?  6877 ALA   A C      1 
ATOM   610  O  O      . ALA   A  1  79  ? -90.06794  18.31224  18.64268  1.000 29.14410  ?  6877 ALA   A O      1 
ATOM   611  C  CB     . ALA   A  1  79  ? -89.30913  15.77282  19.45428  1.000 27.73359  ?  6877 ALA   A CB     1 
ATOM   612  N  N      . PRO   A  1  80  ? -90.85452  18.96014  20.64959  1.000 28.36173  ?  6878 PRO   A N      1 
ATOM   613  C  CA     . PRO   A  1  80  ? -91.01548  20.34777  20.18645  1.000 28.91980  ?  6878 PRO   A CA     1 
ATOM   614  C  C      . PRO   A  1  80  ? -89.70787  20.97812  19.73326  1.000 28.36670  ?  6878 PRO   A C      1 
ATOM   615  O  O      . PRO   A  1  80  ? -89.67851  21.64883  18.69597  1.000 28.15882  ?  6878 PRO   A O      1 
ATOM   616  C  CB     . PRO   A  1  80  ? -91.58356  21.06813  21.41732  1.000 29.87357  ?  6878 PRO   A CB     1 
ATOM   617  C  CG     . PRO   A  1  80  ? -92.09911  19.99600  22.32810  1.000 35.38698  ?  6878 PRO   A CG     1 
ATOM   618  C  CD     . PRO   A  1  80  ? -91.22659  18.79284  22.06411  1.000 30.55900  ?  6878 PRO   A CD     1 
ATOM   619  N  N      . GLY   A  1  81  ? -88.62764  20.80824  20.50069  1.000 28.05182  ?  6879 GLY   A N      1 
ATOM   620  C  CA     . GLY   A  1  81  ? -87.35406  21.39013  20.10174  1.000 27.54797  ?  6879 GLY   A CA     1 
ATOM   621  C  C      . GLY   A  1  81  ? -86.87335  20.87559  18.75927  1.000 33.06717  ?  6879 GLY   A C      1 
ATOM   622  O  O      . GLY   A  1  81  ? -86.33036  21.62935  17.94545  1.000 28.95748  ?  6879 GLY   A O      1 
ATOM   623  N  N      . THR   A  1  82  ? -87.04184  19.57668  18.51255  1.000 26.52083  ?  6880 THR   A N      1 
ATOM   624  C  CA     . THR   A  1  82  ? -86.63781  19.03401  17.22975  1.000 23.00654  ?  6880 THR   A CA     1 
ATOM   625  C  C      . THR   A  1  82  ? -87.41356  19.69031  16.09393  1.000 26.11966  ?  6880 THR   A C      1 
ATOM   626  O  O      . THR   A  1  82  ? -86.84688  19.97912  15.03914  1.000 28.68851  ?  6880 THR   A O      1 
ATOM   627  C  CB     . THR   A  1  82  ? -86.83834  17.51448  17.21932  1.000 29.33484  ?  6880 THR   A CB     1 
ATOM   628  O  OG1    . THR   A  1  82  ? -85.93163  16.91501  18.16159  1.000 26.67143  ?  6880 THR   A OG1    1 
ATOM   629  C  CG2    . THR   A  1  82  ? -86.55362  16.95006  15.85407  1.000 27.54451  ?  6880 THR   A CG2    1 
ATOM   630  N  N      . ALA   A  1  83  ? -88.70699  19.94867  16.29745  1.000 22.79131  ?  6881 ALA   A N      1 
ATOM   631  C  CA     . ALA   A  1  83  ? -89.49870  20.57666  15.24594  1.000 26.42685  ?  6881 ALA   A CA     1 
ATOM   632  C  C      . ALA   A  1  83  ? -88.97842  21.97107  14.93205  1.000 27.88946  ?  6881 ALA   A C      1 
ATOM   633  O  O      . ALA   A  1  83  ? -88.97591  22.38377  13.76860  1.000 27.02561  ?  6881 ALA   A O      1 
ATOM   634  C  CB     . ALA   A  1  83  ? -90.97336  20.64326  15.64622  1.000 26.29642  ?  6881 ALA   A CB     1 
ATOM   635  N  N      . VAL   A  1  84  ? -88.57238  22.72265  15.96355  1.000 26.04874  ?  6882 VAL   A N      1 
ATOM   636  C  CA     . VAL   A  1  84  ? -88.00885  24.05386  15.73599  1.000 27.98993  ?  6882 VAL   A CA     1 
ATOM   637  C  C      . VAL   A  1  84  ? -86.66076  23.95085  15.03759  1.000 24.86189  ?  6882 VAL   A C      1 
ATOM   638  O  O      . VAL   A  1  84  ? -86.35982  24.72546  14.12271  1.000 26.71221  ?  6882 VAL   A O      1 
ATOM   639  C  CB     . VAL   A  1  84  ? -87.88486  24.82857  17.06139  1.000 27.76409  ?  6882 VAL   A CB     1 
ATOM   640  C  CG1    . VAL   A  1  84  ? -87.16707  26.19017  16.82545  1.000 24.61013  ?  6882 VAL   A CG1    1 
ATOM   641  C  CG2    . VAL   A  1  84  ? -89.26056  25.07648  17.66905  1.000 23.05287  ?  6882 VAL   A CG2    1 
ATOM   642  N  N      . LEU   A  1  85  ? -85.81309  23.01567  15.46617  1.000 25.57017  ?  6883 LEU   A N      1 
ATOM   643  C  CA     . LEU   A  1  85  ? -84.52565  22.85841  14.79636  1.000 25.14396  ?  6883 LEU   A CA     1 
ATOM   644  C  C      . LEU   A  1  85  ? -84.71329  22.55242  13.32261  1.000 27.67525  ?  6883 LEU   A C      1 
ATOM   645  O  O      . LEU   A  1  85  ? -83.98317  23.07349  12.47711  1.000 28.21535  ?  6883 LEU   A O      1 
ATOM   646  C  CB     . LEU   A  1  85  ? -83.70013  21.75056  15.44793  1.000 25.17485  ?  6883 LEU   A CB     1 
ATOM   647  C  CG     . LEU   A  1  85  ? -83.18209  22.03223  16.85373  1.000 27.97012  ?  6883 LEU   A CG     1 
ATOM   648  C  CD1    . LEU   A  1  85  ? -82.45542  20.77753  17.38225  1.000 25.84873  ?  6883 LEU   A CD1    1 
ATOM   649  C  CD2    . LEU   A  1  85  ? -82.27907  23.26026  16.80252  1.000 30.92594  ?  6883 LEU   A CD2    1 
ATOM   650  N  N      . ARG   A  1  86  ? -85.64736  21.65977  13.00030  1.000 28.23057  ?  6884 ARG   A N      1 
ATOM   651  C  CA     . ARG   A  1  86  ? -85.86761  21.30831  11.60427  1.000 31.49234  ?  6884 ARG   A CA     1 
ATOM   652  C  C      . ARG   A  1  86  ? -86.39696  22.50182  10.81690  1.000 27.41922  ?  6884 ARG   A C      1 
ATOM   653  O  O      . ARG   A  1  86  ? -86.01311  22.70584  9.66624   1.000 30.09032  ?  6884 ARG   A O      1 
ATOM   654  C  CB     . ARG   A  1  86  ? -86.83791  20.13451  11.50712  1.000 27.31642  ?  6884 ARG   A CB     1 
ATOM   655  C  CG     . ARG   A  1  86  ? -86.72513  19.35229  10.19591  1.000 34.53585  ?  6884 ARG   A CG     1 
ATOM   656  C  CD     . ARG   A  1  86  ? -87.52620  18.06830  10.29709  1.000 35.30686  ?  6884 ARG   A CD     1 
ATOM   657  N  NE     . ARG   A  1  86  ? -87.50227  17.25402  9.08668   1.000 34.23465  ?  6884 ARG   A NE     1 
ATOM   658  C  CZ     . ARG   A  1  86  ? -86.51419  16.43969  8.74351   1.000 40.61596  ?  6884 ARG   A CZ     1 
ATOM   659  N  NH1    . ARG   A  1  86  ? -85.34153  16.46676  9.36419   1.000 35.51154  ?  6884 ARG   A NH1    1 
ATOM   660  N  NH2    . ARG   A  1  86  ? -86.70856  15.56881  7.75508   1.000 41.43554  ?  6884 ARG   A NH2    1 
ATOM   661  N  N      . GLN   A  1  87  ? -87.28349  23.29530  11.42394  1.000 26.26080  ?  6885 GLN   A N      1 
ATOM   662  C  CA     . GLN   A  1  87  ? -87.72612  24.53437  10.79472  1.000 27.68144  ?  6885 GLN   A CA     1 
ATOM   663  C  C      . GLN   A  1  87  ? -86.54492  25.46809  10.54125  1.000 29.99566  ?  6885 GLN   A C      1 
ATOM   664  O  O      . GLN   A  1  87  ? -86.39483  26.03167  9.45042   1.000 32.21439  ?  6885 GLN   A O      1 
ATOM   665  C  CB     . GLN   A  1  87  ? -88.76116  25.20958  11.69511  1.000 26.78609  ?  6885 GLN   A CB     1 
ATOM   666  C  CG     . GLN   A  1  87  ? -89.11899  26.62997  11.27494  1.000 29.45114  ?  6885 GLN   A CG     1 
ATOM   667  C  CD     . GLN   A  1  87  ? -90.00700  27.31317  12.29696  1.000 33.01233  ?  6885 GLN   A CD     1 
ATOM   668  O  OE1    . GLN   A  1  87  ? -90.15360  26.84231  13.44278  1.000 27.32774  ?  6885 GLN   A OE1    1 
ATOM   669  N  NE2    . GLN   A  1  87  ? -90.60098  28.42526  11.89995  1.000 30.41272  ?  6885 GLN   A NE2    1 
ATOM   670  N  N      . TRP   A  1  88  ? -85.67603  25.60666  11.53803  1.000 29.30405  ?  6886 TRP   A N      1 
ATOM   671  C  CA     . TRP   A  1  88  ? -84.55078  26.52972  11.47352  1.000 28.49979  ?  6886 TRP   A CA     1 
ATOM   672  C  C      . TRP   A  1  88  ? -83.51255  26.09620  10.44731  1.000 31.65216  ?  6886 TRP   A C      1 
ATOM   673  O  O      . TRP   A  1  88  ? -83.01076  26.92244  9.66709   1.000 26.11589  ?  6886 TRP   A O      1 
ATOM   674  C  CB     . TRP   A  1  88  ? -83.92052  26.61548  12.85818  1.000 25.44967  ?  6886 TRP   A CB     1 
ATOM   675  C  CG     . TRP   A  1  88  ? -82.72807  27.48892  12.96672  1.000 26.03842  ?  6886 TRP   A CG     1 
ATOM   676  C  CD1    . TRP   A  1  88  ? -82.64305  28.81828  12.65350  1.000 27.87747  ?  6886 TRP   A CD1    1 
ATOM   677  C  CD2    . TRP   A  1  88  ? -81.45317  27.10769  13.48035  1.000 27.39019  ?  6886 TRP   A CD2    1 
ATOM   678  N  NE1    . TRP   A  1  88  ? -81.36264  29.28764  12.92723  1.000 25.18898  ?  6886 TRP   A NE1    1 
ATOM   679  C  CE2    . TRP   A  1  88  ? -80.62159  28.25024  13.44173  1.000 27.59339  ?  6886 TRP   A CE2    1 
ATOM   680  C  CE3    . TRP   A  1  88  ? -80.93010  25.90518  13.96952  1.000 27.80732  ?  6886 TRP   A CE3    1 
ATOM   681  C  CZ2    . TRP   A  1  88  ? -79.29673  28.21636  13.86044  1.000 27.60829  ?  6886 TRP   A CZ2    1 
ATOM   682  C  CZ3    . TRP   A  1  88  ? -79.61635  25.87235  14.37938  1.000 29.68231  ?  6886 TRP   A CZ3    1 
ATOM   683  C  CH2    . TRP   A  1  88  ? -78.81095  27.03188  14.33409  1.000 28.08632  ?  6886 TRP   A CH2    1 
ATOM   684  N  N      . LEU   A  1  89  ? -83.16364  24.81259  10.44730  1.000 29.66211  ?  6887 LEU   A N      1 
ATOM   685  C  CA     . LEU   A  1  89  ? -82.06767  24.33222  9.62958   1.000 29.36307  ?  6887 LEU   A CA     1 
ATOM   686  C  C      . LEU   A  1  89  ? -82.46266  24.26050  8.15110   1.000 29.51079  ?  6887 LEU   A C      1 
ATOM   687  O  O      . LEU   A  1  89  ? -83.62545  24.01831  7.81923   1.000 31.14664  ?  6887 LEU   A O      1 
ATOM   688  C  CB     . LEU   A  1  89  ? -81.63779  22.95088  10.10839  1.000 26.83595  ?  6887 LEU   A CB     1 
ATOM   689  C  CG     . LEU   A  1  89  ? -81.09976  22.91195  11.54038  1.000 30.66065  ?  6887 LEU   A CG     1 
ATOM   690  C  CD1    . LEU   A  1  89  ? -81.15660  21.48237  12.05716  1.000 24.05419  ?  6887 LEU   A CD1    1 
ATOM   691  C  CD2    . LEU   A  1  89  ? -79.66982  23.45839  11.60888  1.000 24.03736  ?  6887 LEU   A CD2    1 
ATOM   692  N  N      . PRO   A  1  90  ? -81.49929  24.41558  7.24363   1.000 28.93259  ?  6888 PRO   A N      1 
ATOM   693  C  CA     . PRO   A  1  90  ? -81.82188  24.33056  5.80971   1.000 33.71093  ?  6888 PRO   A CA     1 
ATOM   694  C  C      . PRO   A  1  90  ? -82.50988  23.00702  5.49362   1.000 34.59392  ?  6888 PRO   A C      1 
ATOM   695  O  O      . PRO   A  1  90  ? -82.21948  21.96936  6.10168   1.000 30.95986  ?  6888 PRO   A O      1 
ATOM   696  C  CB     . PRO   A  1  90  ? -80.45076  24.43552  5.12253   1.000 34.12511  ?  6888 PRO   A CB     1 
ATOM   697  C  CG     . PRO   A  1  90  ? -79.50777  25.02696  6.16928   1.000 32.96630  ?  6888 PRO   A CG     1 
ATOM   698  C  CD     . PRO   A  1  90  ? -80.05261  24.53554  7.49414   1.000 31.55812  ?  6888 PRO   A CD     1 
ATOM   699  N  N      . THR   A  1  91  ? -83.45094  23.05787  4.55435   1.000 34.28282  ?  6889 THR   A N      1 
ATOM   700  C  CA     . THR   A  1  91  ? -84.13113  21.84440  4.12568   1.000 35.10329  ?  6889 THR   A CA     1 
ATOM   701  C  C      . THR   A  1  91  ? -83.11650  20.82476  3.62766   1.000 35.11753  ?  6889 THR   A C      1 
ATOM   702  O  O      . THR   A  1  91  ? -82.18633  21.15753  2.89150   1.000 36.25320  ?  6889 THR   A O      1 
ATOM   703  C  CB     . THR   A  1  91  ? -85.14348  22.16484  3.02652   1.000 39.95184  ?  6889 THR   A CB     1 
ATOM   704  O  OG1    . THR   A  1  91  ? -86.11729  23.07473  3.54489   1.000 36.74238  ?  6889 THR   A OG1    1 
ATOM   705  C  CG2    . THR   A  1  91  ? -85.85232  20.88589  2.54410   1.000 38.53314  ?  6889 THR   A CG2    1 
ATOM   706  N  N      . GLY   A  1  92  ? -83.28782  19.57402  4.04561   1.000 35.60385  ?  6890 GLY   A N      1 
ATOM   707  C  CA     . GLY   A  1  92  ? -82.34034  18.53188  3.71528   1.000 34.30649  ?  6890 GLY   A CA     1 
ATOM   708  C  C      . GLY   A  1  92  ? -81.31342  18.24633  4.79571   1.000 38.50483  ?  6890 GLY   A C      1 
ATOM   709  O  O      . GLY   A  1  92  ? -80.64312  17.20942  4.72221   1.000 35.56595  ?  6890 GLY   A O      1 
ATOM   710  N  N      . THR   A  1  93  ? -81.16838  19.12796  5.79256   1.000 33.27639  ?  6891 THR   A N      1 
ATOM   711  C  CA     . THR   A  1  93  ? -80.21429  18.89152  6.87250   1.000 34.54981  ?  6891 THR   A CA     1 
ATOM   712  C  C      . THR   A  1  93  ? -80.51348  17.55853  7.54747   1.000 32.08058  ?  6891 THR   A C      1 
ATOM   713  O  O      . THR   A  1  93  ? -81.66386  17.25938  7.88951   1.000 32.67957  ?  6891 THR   A O      1 
ATOM   714  C  CB     . THR   A  1  93  ? -80.26731  20.03576  7.89894   1.000 32.30227  ?  6891 THR   A CB     1 
ATOM   715  O  OG1    . THR   A  1  93  ? -79.88612  21.25773  7.26482   1.000 31.53070  ?  6891 THR   A OG1    1 
ATOM   716  C  CG2    . THR   A  1  93  ? -79.31454  19.78317  9.08428   1.000 27.92484  ?  6891 THR   A CG2    1 
ATOM   717  N  N      . LEU   A  1  94  ? -79.47738  16.74762  7.71422   1.000 31.67603  ?  6892 LEU   A N      1 
ATOM   718  C  CA     . LEU   A  1  94  ? -79.62365  15.49630  8.44677   1.000 31.90410  ?  6892 LEU   A CA     1 
ATOM   719  C  C      . LEU   A  1  94  ? -79.74498  15.80178  9.92721   1.000 33.79450  ?  6892 LEU   A C      1 
ATOM   720  O  O      . LEU   A  1  94  ? -78.81599  16.34486  10.53010  1.000 34.48221  ?  6892 LEU   A O      1 
ATOM   721  C  CB     . LEU   A  1  94  ? -78.43031  14.57588  8.20738   1.000 34.64900  ?  6892 LEU   A CB     1 
ATOM   722  C  CG     . LEU   A  1  94  ? -78.27364  13.89324  6.85239   1.000 44.46068  ?  6892 LEU   A CG     1 
ATOM   723  C  CD1    . LEU   A  1  94  ? -77.29742  12.72874  6.99317   1.000 47.75262  ?  6892 LEU   A CD1    1 
ATOM   724  C  CD2    . LEU   A  1  94  ? -79.60332  13.40264  6.33009   1.000 43.31753  ?  6892 LEU   A CD2    1 
ATOM   725  N  N      . LEU   A  1  95  ? -80.88375  15.46079  10.51382  1.000 23.56734  ?  6893 LEU   A N      1 
ATOM   726  C  CA     . LEU   A  1  95  ? -81.14606  15.74931  11.91654  1.000 31.07562  ?  6893 LEU   A CA     1 
ATOM   727  C  C      . LEU   A  1  95  ? -81.44986  14.43938  12.62586  1.000 32.28894  ?  6893 LEU   A C      1 
ATOM   728  O  O      . LEU   A  1  95  ? -82.38224  13.72343  12.23333  1.000 32.58984  ?  6893 LEU   A O      1 
ATOM   729  C  CB     . LEU   A  1  95  ? -82.31674  16.71571  12.05615  1.000 26.76808  ?  6893 LEU   A CB     1 
ATOM   730  C  CG     . LEU   A  1  95  ? -82.77736  17.09914  13.45733  1.000 31.64170  ?  6893 LEU   A CG     1 
ATOM   731  C  CD1    . LEU   A  1  95  ? -81.65417  17.73433  14.23441  1.000 27.77457  ?  6893 LEU   A CD1    1 
ATOM   732  C  CD2    . LEU   A  1  95  ? -83.92717  18.05900  13.32540  1.000 29.11652  ?  6893 LEU   A CD2    1 
ATOM   733  N  N      . VAL   A  1  96  ? -80.65166  14.12246  13.64462  1.000 27.15884  ?  6894 VAL   A N      1 
ATOM   734  C  CA     . VAL   A  1  96  ? -80.84551  12.94733  14.49782  1.000 29.40066  ?  6894 VAL   A CA     1 
ATOM   735  C  C      . VAL   A  1  96  ? -81.16965  13.43908  15.89583  1.000 30.95569  ?  6894 VAL   A C      1 
ATOM   736  O  O      . VAL   A  1  96  ? -80.52117  14.36895  16.39097  1.000 27.43245  ?  6894 VAL   A O      1 
ATOM   737  C  CB     . VAL   A  1  96  ? -79.57901  12.07064  14.52547  1.000 32.26388  ?  6894 VAL   A CB     1 
ATOM   738  C  CG1    . VAL   A  1  96  ? -79.67617  10.98051  15.63649  1.000 30.59152  ?  6894 VAL   A CG1    1 
ATOM   739  C  CG2    . VAL   A  1  96  ? -79.33061  11.47073  13.16145  1.000 30.55775  ?  6894 VAL   A CG2    1 
ATOM   740  N  N      . ASP   A  1  97  ? -82.16756  12.83992  16.54045  1.000 26.19644  ?  6895 ASP   A N      1 
ATOM   741  C  CA     . ASP   A  1  97  ? -82.38796  13.18739  17.93943  1.000 28.07116  ?  6895 ASP   A CA     1 
ATOM   742  C  C      . ASP   A  1  97  ? -82.48340  11.92277  18.78562  1.000 34.59056  ?  6895 ASP   A C      1 
ATOM   743  O  O      . ASP   A  1  97  ? -82.48471  10.79448  18.27565  1.000 32.59135  ?  6895 ASP   A O      1 
ATOM   744  C  CB     . ASP   A  1  97  ? -83.61164  14.10780  18.12096  1.000 25.88493  ?  6895 ASP   A CB     1 
ATOM   745  C  CG     . ASP   A  1  97  ? -84.91631  13.46649  17.69735  1.000 33.78059  ?  6895 ASP   A CG     1 
ATOM   746  O  OD1    . ASP   A  1  97  ? -84.90493  12.26319  17.35837  1.000 35.42543  ?  6895 ASP   A OD1    1 
ATOM   747  O  OD2    . ASP   A  1  97  ? -85.96207  14.17135  17.71606  1.000 30.54833  ?  6895 ASP   A OD2    1 
ATOM   748  N  N      . SER   A  1  98  ? -82.51949  12.12833  20.09936  1.000 31.33325  ?  6896 SER   A N      1 
ATOM   749  C  CA     . SER   A  1  98  ? -82.34089  11.04272  21.04761  1.000 32.63867  ?  6896 SER   A CA     1 
ATOM   750  C  C      . SER   A  1  98  ? -82.91475  11.44140  22.39708  1.000 32.92172  ?  6896 SER   A C      1 
ATOM   751  O  O      . SER   A  1  98  ? -82.90664  12.62182  22.77624  1.000 30.53267  ?  6896 SER   A O      1 
ATOM   752  C  CB     . SER   A  1  98  ? -80.85452  10.68224  21.20803  1.000 34.09467  ?  6896 SER   A CB     1 
ATOM   753  O  OG     . SER   A  1  98  ? -80.69155  9.61105   22.12439  1.000 43.38151  ?  6896 SER   A OG     1 
ATOM   754  N  N      . ASP   A  1  99  ? -83.38301  10.43900  23.13125  1.000 27.85300  ?  6897 ASP   A N      1 
ATOM   755  C  CA     . ASP   A  1  99  ? -83.79525  10.65806  24.50627  1.000 30.70010  ?  6897 ASP   A CA     1 
ATOM   756  C  C      . ASP   A  1  99  ? -83.89773  9.31292   25.21456  1.000 38.37355  ?  6897 ASP   A C      1 
ATOM   757  O  O      . ASP   A  1  99  ? -83.88113  8.24437   24.59096  1.000 33.34648  ?  6897 ASP   A O      1 
ATOM   758  C  CB     . ASP   A  1  99  ? -85.11146  11.44402  24.59134  1.000 30.16894  ?  6897 ASP   A CB     1 
ATOM   759  C  CG     . ASP   A  1  99  ? -85.24104  12.19426  25.91093  1.000 41.78333  ?  6897 ASP   A CG     1 
ATOM   760  O  OD1    . ASP   A  1  99  ? -85.07994  11.54942  26.96819  1.000 52.83433  ?  6897 ASP   A OD1    1 
ATOM   761  O  OD2    . ASP   A  1  99  ? -85.45190  13.42673  25.91466  1.000 35.41847  ?  6897 ASP   A OD2    1 
ATOM   762  N  N      . LEU   A  1  100 ? -83.98085  9.39322   26.54379  1.000 34.28811  ?  6898 LEU   A N      1 
ATOM   763  C  CA     . LEU   A  1  100 ? -84.10379  8.20356   27.37562  1.000 40.78187  ?  6898 LEU   A CA     1 
ATOM   764  C  C      . LEU   A  1  100 ? -85.42188  7.48844   27.11125  1.000 39.45707  ?  6898 LEU   A C      1 
ATOM   765  O  O      . LEU   A  1  100 ? -85.45909  6.26058   26.99483  1.000 40.68229  ?  6898 LEU   A O      1 
ATOM   766  C  CB     . LEU   A  1  100 ? -83.98489  8.60652   28.85253  1.000 43.19118  ?  6898 LEU   A CB     1 
ATOM   767  C  CG     . LEU   A  1  100 ? -83.87307  7.52505   29.92536  1.000 48.03599  ?  6898 LEU   A CG     1 
ATOM   768  C  CD1    . LEU   A  1  100 ? -82.72358  6.58349   29.59183  1.000 46.91853  ?  6898 LEU   A CD1    1 
ATOM   769  C  CD2    . LEU   A  1  100 ? -83.66393  8.17270   31.28458  1.000 47.93793  ?  6898 LEU   A CD2    1 
ATOM   770  N  N      . ASN   A  1  101 ? -86.50767  8.24339   26.98467  1.000 38.30776  ?  6899 ASN   A N      1 
ATOM   771  C  CA     . ASN   A  1  101 ? -87.85431  7.70354   26.87959  1.000 42.57776  ?  6899 ASN   A CA     1 
ATOM   772  C  C      . ASN   A  1  101 ? -88.42073  7.89285   25.47433  1.000 40.61262  ?  6899 ASN   A C      1 
ATOM   773  O  O      . ASN   A  1  101 ? -88.03633  8.80734   24.73305  1.000 37.33212  ?  6899 ASN   A O      1 
ATOM   774  C  CB     . ASN   A  1  101 ? -88.77967  8.37101   27.90906  1.000 47.70052  ?  6899 ASN   A CB     1 
ATOM   775  C  CG     . ASN   A  1  101 ? -88.17574  8.39193   29.31366  1.000 52.03939  ?  6899 ASN   A CG     1 
ATOM   776  O  OD1    . ASN   A  1  101 ? -88.07590  9.44990   29.94828  1.000 55.20667  ?  6899 ASN   A OD1    1 
ATOM   777  N  ND2    . ASN   A  1  101 ? -87.75930  7.22984   29.79418  1.000 40.90589  ?  6899 ASN   A ND2    1 
ATOM   778  N  N      . ASP   A  1  102 ? -89.37318  7.02547   25.13773  1.000 36.43781  ?  6900 ASP   A N      1 
ATOM   779  C  CA     . ASP   A  1  102 ? -89.96679  6.99523   23.80712  1.000 38.26441  ?  6900 ASP   A CA     1 
ATOM   780  C  C      . ASP   A  1  102 ? -90.68099  8.29928   23.47685  1.000 38.57646  ?  6900 ASP   A C      1 
ATOM   781  O  O      . ASP   A  1  102 ? -91.36468  8.87965   24.32190  1.000 39.95942  ?  6900 ASP   A O      1 
ATOM   782  C  CB     . ASP   A  1  102 ? -90.97962  5.86142   23.71244  1.000 45.35866  ?  6900 ASP   A CB     1 
ATOM   783  C  CG     . ASP   A  1  102 ? -90.81744  5.05974   22.46261  1.000 58.55362  ?  6900 ASP   A CG     1 
ATOM   784  O  OD1    . ASP   A  1  102 ? -90.89406  3.81711   22.56802  1.000 65.35899  ?  6900 ASP   A OD1    1 
ATOM   785  O  OD2    . ASP   A  1  102 ? -90.61353  5.66617   21.38007  1.000 64.39188  ?  6900 ASP   A OD2    1 
ATOM   786  N  N      . PHE   A  1  103 ? -90.56018  8.74009   22.22635  1.000 36.68613  ?  6901 PHE   A N      1 
ATOM   787  C  CA     . PHE   A  1  103 ? -91.27850  9.93608   21.79366  1.000 36.52297  ?  6901 PHE   A CA     1 
ATOM   788  C  C      . PHE   A  1  103 ? -91.37182  9.91289   20.27283  1.000 34.78452  ?  6901 PHE   A C      1 
ATOM   789  O  O      . PHE   A  1  103 ? -90.56959  9.26147   19.60058  1.000 34.45551  ?  6901 PHE   A O      1 
ATOM   790  C  CB     . PHE   A  1  103 ? -90.57448  11.21591  22.28637  1.000 28.78123  ?  6901 PHE   A CB     1 
ATOM   791  C  CG     . PHE   A  1  103 ? -89.18377  11.42448  21.68617  1.000 33.27851  ?  6901 PHE   A CG     1 
ATOM   792  C  CD1    . PHE   A  1  103 ? -88.09156  10.69411  22.13954  1.000 31.86107  ?  6901 PHE   A CD1    1 
ATOM   793  C  CD2    . PHE   A  1  103 ? -88.97350  12.35849  20.68480  1.000 34.00787  ?  6901 PHE   A CD2    1 
ATOM   794  C  CE1    . PHE   A  1  103 ? -86.81220  10.87221  21.58963  1.000 26.92857  ?  6901 PHE   A CE1    1 
ATOM   795  C  CE2    . PHE   A  1  103 ? -87.68918  12.56152  20.12881  1.000 30.96268  ?  6901 PHE   A CE2    1 
ATOM   796  C  CZ     . PHE   A  1  103 ? -86.61136  11.81596  20.58310  1.000 30.55539  ?  6901 PHE   A CZ     1 
ATOM   797  N  N      . VAL   A  1  104 ? -92.34518  10.63335  19.72504  1.000 33.33419  ?  6902 VAL   A N      1 
ATOM   798  C  CA     . VAL   A  1  104 ? -92.46408  10.72446  18.27148  1.000 40.56102  ?  6902 VAL   A CA     1 
ATOM   799  C  C      . VAL   A  1  104 ? -91.87454  12.04740  17.81618  1.000 37.04283  ?  6902 VAL   A C      1 
ATOM   800  O  O      . VAL   A  1  104 ? -92.09281  13.09138  18.44127  1.000 36.99103  ?  6902 VAL   A O      1 
ATOM   801  C  CB     . VAL   A  1  104 ? -93.91949  10.55857  17.79281  1.000 41.57315  ?  6902 VAL   A CB     1 
ATOM   802  C  CG1    . VAL   A  1  104 ? -94.59845  9.41554   18.55037  1.000 49.02926  ?  6902 VAL   A CG1    1 
ATOM   803  C  CG2    . VAL   A  1  104 ? -94.67957  11.83134  17.91729  1.000 40.92616  ?  6902 VAL   A CG2    1 
ATOM   804  N  N      . SER   A  1  105 ? -91.12155  12.00654  16.72731  1.000 34.21245  ?  6903 SER   A N      1 
ATOM   805  C  CA     . SER   A  1  105 ? -90.23727  13.10327  16.37749  1.000 34.35932  ?  6903 SER   A CA     1 
ATOM   806  C  C      . SER   A  1  105 ? -90.24471  13.31398  14.87609  1.000 34.53132  ?  6903 SER   A C      1 
ATOM   807  O  O      . SER   A  1  105 ? -90.47938  12.37917  14.11098  1.000 35.74192  ?  6903 SER   A O      1 
ATOM   808  C  CB     . SER   A  1  105 ? -88.80526  12.81128  16.83933  1.000 35.90901  ?  6903 SER   A CB     1 
ATOM   809  O  OG     . SER   A  1  105 ? -87.87392  13.53049  16.05672  1.000 38.05287  ?  6903 SER   A OG     1 
ATOM   810  N  N      . ASP   A  1  106 ? -89.95006  14.54443  14.46572  1.000 31.54145  ?  6904 ASP   A N      1 
ATOM   811  C  CA     . ASP   A  1  106 ? -89.74391  14.87929  13.06487  1.000 32.27752  ?  6904 ASP   A CA     1 
ATOM   812  C  C      . ASP   A  1  106 ? -88.31518  14.66394  12.59612  1.000 29.40564  ?  6904 ASP   A C      1 
ATOM   813  O  O      . ASP   A  1  106 ? -88.02484  14.91938  11.42826  1.000 32.34886  ?  6904 ASP   A O      1 
ATOM   814  C  CB     . ASP   A  1  106 ? -90.14756  16.33041  12.82098  1.000 29.39626  ?  6904 ASP   A CB     1 
ATOM   815  C  CG     . ASP   A  1  106 ? -91.64715  16.53532  12.95912  1.000 36.71139  ?  6904 ASP   A CG     1 
ATOM   816  O  OD1    . ASP   A  1  106 ? -92.39496  15.98571  12.10781  1.000 38.99478  ?  6904 ASP   A OD1    1 
ATOM   817  O  OD2    . ASP   A  1  106 ? -92.07870  17.22286  13.91981  1.000 34.14273  ?  6904 ASP   A OD2    1 
ATOM   818  N  N      . ALA   A  1  107 ? -87.41594  14.21090  13.46424  1.000 28.68736  ?  6905 ALA   A N      1 
ATOM   819  C  CA     . ALA   A  1  107 ? -86.04189  14.00031  13.04334  1.000 31.93049  ?  6905 ALA   A CA     1 
ATOM   820  C  C      . ALA   A  1  107 ? -85.96564  12.91722  11.96794  1.000 33.00245  ?  6905 ALA   A C      1 
ATOM   821  O  O      . ALA   A  1  107 ? -86.87271  12.10457  11.80893  1.000 30.72509  ?  6905 ALA   A O      1 
ATOM   822  C  CB     . ALA   A  1  107 ? -85.17884  13.61545  14.23926  1.000 28.56354  ?  6905 ALA   A CB     1 
ATOM   823  N  N      . ASP   A  1  108 ? -84.83746  12.88640  11.24979  1.000 30.87801  ?  6906 ASP   A N      1 
ATOM   824  C  CA     . ASP   A  1  108 ? -84.64129  11.84275  10.24389  1.000 35.89341  ?  6906 ASP   A CA     1 
ATOM   825  C  C      . ASP   A  1  108 ? -84.41404  10.47672  10.88286  1.000 35.66890  ?  6906 ASP   A C      1 
ATOM   826  O  O      . ASP   A  1  108 ? -84.83410  9.45795   10.33173  1.000 37.19740  ?  6906 ASP   A O      1 
ATOM   827  C  CB     . ASP   A  1  108 ? -83.48845  12.22617  9.32547   1.000 30.59431  ?  6906 ASP   A CB     1 
ATOM   828  C  CG     . ASP   A  1  108 ? -83.77381  13.54262  8.59571   1.000 39.45475  ?  6906 ASP   A CG     1 
ATOM   829  O  OD1    . ASP   A  1  108 ? -84.77562  13.58179  7.83320   1.000 39.14106  ?  6906 ASP   A OD1    1 
ATOM   830  O  OD2    . ASP   A  1  108 ? -83.05462  14.54351  8.83079   1.000 36.79967  ?  6906 ASP   A OD2    1 
ATOM   831  N  N      . SER   A  1  109 ? -83.74857  10.42947  12.03186  1.000 34.67447  ?  6907 SER   A N      1 
ATOM   832  C  CA     . SER   A  1  109 ? -83.65143  9.21460   12.82960  1.000 33.82332  ?  6907 SER   A CA     1 
ATOM   833  C  C      . SER   A  1  109 ? -83.70498  9.59985   14.29030  1.000 32.62137  ?  6907 SER   A C      1 
ATOM   834  O  O      . SER   A  1  109 ? -83.22901  10.66552  14.67783  1.000 30.50457  ?  6907 SER   A O      1 
ATOM   835  C  CB     . SER   A  1  109 ? -82.35419  8.43943   12.57777  1.000 35.78090  ?  6907 SER   A CB     1 
ATOM   836  O  OG     . SER   A  1  109 ? -82.41718  7.70866   11.37472  1.000 54.67077  ?  6907 SER   A OG     1 
ATOM   837  N  N      . THR   A  1  110 ? -84.26077  8.70643   15.09517  1.000 27.95775  ?  6908 THR   A N      1 
ATOM   838  C  CA     . THR   A  1  110 ? -84.40672  8.89276   16.52789  1.000 36.51440  ?  6908 THR   A CA     1 
ATOM   839  C  C      . THR   A  1  110 ? -83.86458  7.66344   17.23515  1.000 38.40795  ?  6908 THR   A C      1 
ATOM   840  O  O      . THR   A  1  110 ? -84.20931  6.54041   16.86597  1.000 33.91028  ?  6908 THR   A O      1 
ATOM   841  C  CB     . THR   A  1  110 ? -85.87878  9.10980   16.89653  1.000 38.11956  ?  6908 THR   A CB     1 
ATOM   842  O  OG1    . THR   A  1  110 ? -86.37065  10.27395  16.22653  1.000 34.18468  ?  6908 THR   A OG1    1 
ATOM   843  C  CG2    . THR   A  1  110 ? -86.05623  9.28978   18.39209  1.000 31.39244  ?  6908 THR   A CG2    1 
ATOM   844  N  N      . LEU   A  1  111 ? -83.01815  7.86837   18.24145  1.000 34.60488  ?  6909 LEU   A N      1 
ATOM   845  C  CA     . LEU   A  1  111 ? -82.49038  6.77622   19.05459  1.000 36.23880  ?  6909 LEU   A CA     1 
ATOM   846  C  C      . LEU   A  1  111 ? -83.03250  6.91719   20.46565  1.000 37.62134  ?  6909 LEU   A C      1 
ATOM   847  O  O      . LEU   A  1  111 ? -82.98811  8.01013   21.03830  1.000 34.94401  ?  6909 LEU   A O      1 
ATOM   848  C  CB     . LEU   A  1  111 ? -80.96361  6.78170   19.06730  1.000 33.02698  ?  6909 LEU   A CB     1 
ATOM   849  C  CG     . LEU   A  1  111 ? -80.28303  6.56882   17.72077  1.000 35.36564  ?  6909 LEU   A CG     1 
ATOM   850  C  CD1    . LEU   A  1  111 ? -78.80493  6.71509   17.88236  1.000 36.79908  ?  6909 LEU   A CD1    1 
ATOM   851  C  CD2    . LEU   A  1  111 ? -80.60948  5.19297   17.16251  1.000 40.15445  ?  6909 LEU   A CD2    1 
ATOM   852  N  N      . ILE   A  1  112 ? -83.57720  5.82871   21.01143  1.000 36.37230  ?  6910 ILE   A N      1 
ATOM   853  C  CA     . ILE   A  1  112 ? -84.15970  5.82513   22.34822  1.000 36.51396  ?  6910 ILE   A CA     1 
ATOM   854  C  C      . ILE   A  1  112 ? -83.23436  5.05408   23.27323  1.000 39.82424  ?  6910 ILE   A C      1 
ATOM   855  O  O      . ILE   A  1  112 ? -82.86560  3.91501   22.97543  1.000 40.84772  ?  6910 ILE   A O      1 
ATOM   856  C  CB     . ILE   A  1  112 ? -85.56665  5.20394   22.36872  1.000 40.58722  ?  6910 ILE   A CB     1 
ATOM   857  C  CG1    . ILE   A  1  112 ? -86.49187  5.90701   21.37466  1.000 40.07380  ?  6910 ILE   A CG1    1 
ATOM   858  C  CG2    . ILE   A  1  112 ? -86.13154  5.27240   23.78340  1.000 37.29393  ?  6910 ILE   A CG2    1 
ATOM   859  C  CD1    . ILE   A  1  112 ? -86.63844  7.40490   21.63103  1.000 36.50839  ?  6910 ILE   A CD1    1 
ATOM   860  N  N      . GLY   A  1  113 ? -82.89160  5.66012   24.40499  1.000 36.30684  ?  6911 GLY   A N      1 
ATOM   861  C  CA     . GLY   A  1  113 ? -82.02112  5.05050   25.38534  1.000 35.79462  ?  6911 GLY   A CA     1 
ATOM   862  C  C      . GLY   A  1  113 ? -81.14696  6.08112   26.06994  1.000 41.35935  ?  6911 GLY   A C      1 
ATOM   863  O  O      . GLY   A  1  113 ? -81.19591  7.27172   25.72869  1.000 37.20657  ?  6911 GLY   A O      1 
ATOM   864  N  N      . ASP   A  1  114 ? -80.36091  5.65348   27.05244  1.000 36.35273  ?  6912 ASP   A N      1 
ATOM   865  C  CA     . ASP   A  1  114 ? -79.41429  6.56302   27.68437  1.000 39.42335  ?  6912 ASP   A CA     1 
ATOM   866  C  C      . ASP   A  1  114 ? -78.41456  7.06104   26.64069  1.000 37.54395  ?  6912 ASP   A C      1 
ATOM   867  O  O      . ASP   A  1  114 ? -77.98899  6.31115   25.75715  1.000 33.93619  ?  6912 ASP   A O      1 
ATOM   868  C  CB     . ASP   A  1  114 ? -78.70426  5.85263   28.84712  1.000 38.83894  ?  6912 ASP   A CB     1 
ATOM   869  C  CG     . ASP   A  1  114 ? -77.77108  6.77115   29.60883  1.000 40.55978  ?  6912 ASP   A CG     1 
ATOM   870  O  OD1    . ASP   A  1  114 ? -78.24863  7.52331   30.47797  1.000 47.65298  ?  6912 ASP   A OD1    1 
ATOM   871  O  OD2    . ASP   A  1  114 ? -76.55787  6.75474   29.33492  1.000 43.00713  ?  6912 ASP   A OD2    1 
ATOM   872  N  N      . CYS   A  1  115 ? -78.04131  8.34129   26.72203  1.000 31.28228  ?  6913 CYS   A N      1 
ATOM   873  C  CA     . CYS   A  1  115 ? -77.18863  8.88325   25.66579  1.000 31.84099  ?  6913 CYS   A CA     1 
ATOM   874  C  C      . CYS   A  1  115 ? -75.89192  8.09942   25.54428  1.000 32.20213  ?  6913 CYS   A C      1 
ATOM   875  O  O      . CYS   A  1  115 ? -75.28991  8.06021   24.46723  1.000 34.27270  ?  6913 CYS   A O      1 
ATOM   876  C  CB     . CYS   A  1  115 ? -76.88085  10.36359  25.91288  1.000 37.95618  ?  6913 CYS   A CB     1 
ATOM   877  S  SG     . CYS   A  1  115 ? -76.00909  10.66288  27.47173  1.000 36.38817  ?  6913 CYS   A SG     1 
ATOM   878  N  N      . ALA   A  1  116 ? -75.43723  7.48678   26.63587  1.000 32.57190  ?  6914 ALA   A N      1 
ATOM   879  C  CA     . ALA   A  1  116 ? -74.20622  6.70478   26.59495  1.000 36.82100  ?  6914 ALA   A CA     1 
ATOM   880  C  C      . ALA   A  1  116 ? -74.32306  5.49552   25.67813  1.000 37.03584  ?  6914 ALA   A C      1 
ATOM   881  O  O      . ALA   A  1  116 ? -73.29845  4.92857   25.29942  1.000 37.31039  ?  6914 ALA   A O      1 
ATOM   882  C  CB     . ALA   A  1  116 ? -73.82363  6.24146   28.00245  1.000 35.89194  ?  6914 ALA   A CB     1 
ATOM   883  N  N      . THR   A  1  117 ? -75.53894  5.08052   25.31682  1.000 33.49223  ?  6915 THR   A N      1 
ATOM   884  C  CA     . THR   A  1  117 ? -75.68412  3.97850   24.37198  1.000 37.64118  ?  6915 THR   A CA     1 
ATOM   885  C  C      . THR   A  1  117 ? -75.60133  4.42361   22.91658  1.000 43.69138  ?  6915 THR   A C      1 
ATOM   886  O  O      . THR   A  1  117 ? -75.66595  3.56746   22.02762  1.000 39.53422  ?  6915 THR   A O      1 
ATOM   887  C  CB     . THR   A  1  117 ? -77.00952  3.24643   24.58167  1.000 34.74935  ?  6915 THR   A CB     1 
ATOM   888  O  OG1    . THR   A  1  117 ? -78.10198  4.10808   24.24405  1.000 35.88987  ?  6915 THR   A OG1    1 
ATOM   889  C  CG2    . THR   A  1  117 ? -77.15203  2.76842   26.02660  1.000 37.49292  ?  6915 THR   A CG2    1 
ATOM   890  N  N      . VAL   A  1  118 ? -75.44901  5.72221   22.64610  1.000 33.81996  ?  6916 VAL   A N      1 
ATOM   891  C  CA     . VAL   A  1  118 ? -75.47966  6.23779   21.28307  1.000 33.78865  ?  6916 VAL   A CA     1 
ATOM   892  C  C      . VAL   A  1  118 ? -74.07365  6.24476   20.70619  1.000 37.88726  ?  6916 VAL   A C      1 
ATOM   893  O  O      . VAL   A  1  118 ? -73.14829  6.79356   21.31739  1.000 37.36448  ?  6916 VAL   A O      1 
ATOM   894  C  CB     . VAL   A  1  118 ? -76.09030  7.64724   21.24311  1.000 34.09525  ?  6916 VAL   A CB     1 
ATOM   895  C  CG1    . VAL   A  1  118 ? -75.89274  8.24981   19.86819  1.000 32.32112  ?  6916 VAL   A CG1    1 
ATOM   896  C  CG2    . VAL   A  1  118 ? -77.54872  7.57939   21.60715  1.000 30.45876  ?  6916 VAL   A CG2    1 
ATOM   897  N  N      . HIS   A  1  119 ? -73.91518  5.64907   19.51396  1.000 35.64403  ?  6917 HIS   A N      1 
ATOM   898  C  CA     . HIS   A  1  119 ? -72.66673  5.69230   18.77080  1.000 36.15301  ?  6917 HIS   A CA     1 
ATOM   899  C  C      . HIS   A  1  119 ? -72.92763  6.19723   17.36439  1.000 37.16423  ?  6917 HIS   A C      1 
ATOM   900  O  O      . HIS   A  1  119 ? -73.99759  5.97618   16.79967  1.000 37.06990  ?  6917 HIS   A O      1 
ATOM   901  C  CB     . HIS   A  1  119 ? -71.99584  4.32716   18.73812  1.000 36.21441  ?  6917 HIS   A CB     1 
ATOM   902  C  CG     . HIS   A  1  119 ? -71.67676  3.81188   20.10173  1.000 44.22495  ?  6917 HIS   A CG     1 
ATOM   903  N  ND1    . HIS   A  1  119 ? -72.62275  3.21012   20.90176  1.000 50.10265  ?  6917 HIS   A ND1    1 
ATOM   904  C  CD2    . HIS   A  1  119 ? -70.53752  3.86416   20.83582  1.000 49.15034  ?  6917 HIS   A CD2    1 
ATOM   905  C  CE1    . HIS   A  1  119 ? -72.07387  2.89025   22.06245  1.000 46.82280  ?  6917 HIS   A CE1    1 
ATOM   906  N  NE2    . HIS   A  1  119 ? -70.80945  3.27467   22.04805  1.000 49.67765  ?  6917 HIS   A NE2    1 
ATOM   907  N  N      . THR   A  1  120 ? -71.95930  6.92226   16.81572  1.000 37.87359  ?  6918 THR   A N      1 
ATOM   908  C  CA     . THR   A  1  120 ? -72.07325  7.36362   15.43793  1.000 38.88778  ?  6918 THR   A CA     1 
ATOM   909  C  C      . THR   A  1  120 ? -70.73298  7.14716   14.76703  1.000 45.20002  ?  6918 THR   A C      1 
ATOM   910  O  O      . THR   A  1  120 ? -69.68173  7.31328   15.39354  1.000 41.84823  ?  6918 THR   A O      1 
ATOM   911  C  CB     . THR   A  1  120 ? -72.52404  8.83530   15.32308  1.000 39.22098  ?  6918 THR   A CB     1 
ATOM   912  O  OG1    . THR   A  1  120 ? -71.52938  9.72091   15.85475  1.000 41.83309  ?  6918 THR   A OG1    1 
ATOM   913  C  CG2    . THR   A  1  120 ? -73.81212  9.05347   16.10388  1.000 41.14877  ?  6918 THR   A CG2    1 
ATOM   914  N  N      . ALA   A  1  121 ? -70.78113  6.71605   13.50465  1.000 49.79459  ?  6919 ALA   A N      1 
ATOM   915  C  CA     . ALA   A  1  121 ? -69.54918  6.55376   12.74570  1.000 52.20255  ?  6919 ALA   A CA     1 
ATOM   916  C  C      . ALA   A  1  121 ? -68.96014  7.91476   12.40120  1.000 49.86217  ?  6919 ALA   A C      1 
ATOM   917  O  O      . ALA   A  1  121 ? -67.74348  8.12184   12.47571  1.000 52.37990  ?  6919 ALA   A O      1 
ATOM   918  C  CB     . ALA   A  1  121 ? -69.82713  5.72959   11.48158  1.000 47.00958  ?  6919 ALA   A CB     1 
ATOM   919  N  N      . ASN   A  1  122 ? -69.82168  8.86860   12.10380  1.000 45.87121  ?  6920 ASN   A N      1 
ATOM   920  C  CA     . ASN   A  1  122 ? -69.43625  10.11528  11.47485  1.000 47.38874  ?  6920 ASN   A CA     1 
ATOM   921  C  C      . ASN   A  1  122 ? -69.31259  11.24603  12.49676  1.000 44.27296  ?  6920 ASN   A C      1 
ATOM   922  O  O      . ASN   A  1  122 ? -69.61353  11.09698  13.68437  1.000 40.02993  ?  6920 ASN   A O      1 
ATOM   923  C  CB     . ASN   A  1  122 ? -70.45867  10.45661  10.39381  1.000 46.31569  ?  6920 ASN   A CB     1 
ATOM   924  C  CG     . ASN   A  1  122 ? -71.87785  10.44886  10.92306  1.000 50.39363  ?  6920 ASN   A CG     1 
ATOM   925  O  OD1    . ASN   A  1  122 ? -72.45581  11.50503  11.19616  1.000 50.59126  ?  6920 ASN   A OD1    1 
ATOM   926  N  ND2    . ASN   A  1  122 ? -72.45041  9.25567   11.07747  1.000 50.12551  ?  6920 ASN   A ND2    1 
ATOM   927  N  N      . LYS   A  1  123 ? -68.83642  12.38710  12.01455  1.000 43.08911  ?  6921 LYS   A N      1 
ATOM   928  C  CA     . LYS   A  1  123 ? -68.72719  13.59296  12.81825  1.000 36.50252  ?  6921 LYS   A CA     1 
ATOM   929  C  C      . LYS   A  1  123 ? -69.87540  14.53620  12.49009  1.000 36.26398  ?  6921 LYS   A C      1 
ATOM   930  O  O      . LYS   A  1  123 ? -70.58104  14.37000  11.49118  1.000 36.29821  ?  6921 LYS   A O      1 
ATOM   931  C  CB     . LYS   A  1  123 ? -67.37408  14.26839  12.59174  1.000 37.36836  ?  6921 LYS   A CB     1 
ATOM   932  C  CG     . LYS   A  1  123 ? -66.24567  13.46797  13.22267  1.000 35.95826  ?  6921 LYS   A CG     1 
ATOM   933  C  CD     . LYS   A  1  123 ? -64.92925  14.22116  13.21514  1.000 39.73848  ?  6921 LYS   A CD     1 
ATOM   934  C  CE     . LYS   A  1  123 ? -63.85796  13.39372  13.92764  1.000 40.89382  ?  6921 LYS   A CE     1 
ATOM   935  N  NZ     . LYS   A  1  123 ? -62.75262  14.26330  14.44184  1.000 54.01784  ?  6921 LYS   A NZ     1 
ATOM   936  N  N      . TRP   A  1  124 ? -70.08639  15.51508  13.36829  1.000 31.40340  ?  6922 TRP   A N      1 
ATOM   937  C  CA     . TRP   A  1  124 ? -71.28643  16.33028  13.30859  1.000 29.14614  ?  6922 TRP   A CA     1 
ATOM   938  C  C      . TRP   A  1  124 ? -70.90696  17.79917  13.20810  1.000 29.67567  ?  6922 TRP   A C      1 
ATOM   939  O  O      . TRP   A  1  124 ? -69.83352  18.21314  13.65710  1.000 30.39012  ?  6922 TRP   A O      1 
ATOM   940  C  CB     . TRP   A  1  124 ? -72.17870  16.06164  14.53822  1.000 28.40003  ?  6922 TRP   A CB     1 
ATOM   941  C  CG     . TRP   A  1  124 ? -72.60643  14.61904  14.56824  1.000 32.95497  ?  6922 TRP   A CG     1 
ATOM   942  C  CD1    . TRP   A  1  124 ? -71.88372  13.55880  15.04631  1.000 30.72657  ?  6922 TRP   A CD1    1 
ATOM   943  C  CD2    . TRP   A  1  124 ? -73.81770  14.07360  14.03245  1.000 29.15953  ?  6922 TRP   A CD2    1 
ATOM   944  N  NE1    . TRP   A  1  124 ? -72.58449  12.38701  14.85364  1.000 34.55654  ?  6922 TRP   A NE1    1 
ATOM   945  C  CE2    . TRP   A  1  124 ? -73.77327  12.67716  14.23461  1.000 33.88257  ?  6922 TRP   A CE2    1 
ATOM   946  C  CE3    . TRP   A  1  124 ? -74.93564  14.62816  13.40331  1.000 33.63126  ?  6922 TRP   A CE3    1 
ATOM   947  C  CZ2    . TRP   A  1  124 ? -74.79689  11.83138  13.82280  1.000 32.76881  ?  6922 TRP   A CZ2    1 
ATOM   948  C  CZ3    . TRP   A  1  124 ? -75.97577  13.77479  13.01189  1.000 33.14589  ?  6922 TRP   A CZ3    1 
ATOM   949  C  CH2    . TRP   A  1  124 ? -75.88836  12.39905  13.22050  1.000 32.58144  ?  6922 TRP   A CH2    1 
ATOM   950  N  N      . ASP   A  1  125 ? -71.79609  18.58229  12.61483  1.000 30.67183  ?  6923 ASP   A N      1 
ATOM   951  C  CA     . ASP   A  1  125 ? -71.55321  20.01403  12.47280  1.000 31.97648  ?  6923 ASP   A CA     1 
ATOM   952  C  C      . ASP   A  1  125 ? -72.15256  20.83636  13.61065  1.000 35.29974  ?  6923 ASP   A C      1 
ATOM   953  O  O      . ASP   A  1  125 ? -71.65867  21.93441  13.89908  1.000 30.81872  ?  6923 ASP   A O      1 
ATOM   954  C  CB     . ASP   A  1  125 ? -72.10857  20.50568  11.12849  1.000 28.89590  ?  6923 ASP   A CB     1 
ATOM   955  C  CG     . ASP   A  1  125 ? -71.58960  19.67576  9.94190   1.000 38.51093  ?  6923 ASP   A CG     1 
ATOM   956  O  OD1    . ASP   A  1  125 ? -70.39159  19.31065  9.94891   1.000 34.18247  ?  6923 ASP   A OD1    1 
ATOM   957  O  OD2    . ASP   A  1  125 ? -72.38420  19.37154  9.01490   1.000 37.27385  ?  6923 ASP   A OD2    1 
ATOM   958  N  N      . LEU   A  1  126 ? -73.18267  20.32704  14.27314  1.000 27.58320  ?  6924 LEU   A N      1 
ATOM   959  C  CA     . LEU   A  1  126 ? -73.86137  21.04957  15.33719  1.000 26.88630  ?  6924 LEU   A CA     1 
ATOM   960  C  C      . LEU   A  1  126 ? -74.40781  20.00691  16.29084  1.000 31.51302  ?  6924 LEU   A C      1 
ATOM   961  O  O      . LEU   A  1  126 ? -75.06470  19.06233  15.84348  1.000 26.73616  ?  6924 LEU   A O      1 
ATOM   962  C  CB     . LEU   A  1  126 ? -75.00130  21.90270  14.76813  1.000 26.87614  ?  6924 LEU   A CB     1 
ATOM   963  C  CG     . LEU   A  1  126 ? -75.77794  22.79311  15.73046  1.000 36.27675  ?  6924 LEU   A CG     1 
ATOM   964  C  CD1    . LEU   A  1  126 ? -74.80331  23.84675  16.29968  1.000 32.16717  ?  6924 LEU   A CD1    1 
ATOM   965  C  CD2    . LEU   A  1  126 ? -76.96249  23.44956  14.99427  1.000 23.64275  ?  6924 LEU   A CD2    1 
ATOM   966  N  N      . ILE   A  1  127 ? -74.13323  20.17041  17.58111  1.000 25.51527  ?  6925 ILE   A N      1 
ATOM   967  C  CA     . ILE   A  1  127 ? -74.66295  19.30754  18.63447  1.000 28.92489  ?  6925 ILE   A CA     1 
ATOM   968  C  C      . ILE   A  1  127 ? -75.51833  20.17107  19.55313  1.000 29.05039  ?  6925 ILE   A C      1 
ATOM   969  O  O      . ILE   A  1  127 ? -75.03405  21.17444  20.08272  1.000 26.69560  ?  6925 ILE   A O      1 
ATOM   970  C  CB     . ILE   A  1  127 ? -73.53539  18.63290  19.42781  1.000 29.47628  ?  6925 ILE   A CB     1 
ATOM   971  C  CG1    . ILE   A  1  127 ? -72.65177  17.78488  18.49937  1.000 26.79472  ?  6925 ILE   A CG1    1 
ATOM   972  C  CG2    . ILE   A  1  127 ? -74.12162  17.79721  20.56200  1.000 28.92282  ?  6925 ILE   A CG2    1 
ATOM   973  C  CD1    . ILE   A  1  127 ? -71.34753  17.34405  19.16873  1.000 29.98736  ?  6925 ILE   A CD1    1 
ATOM   974  N  N      . ILE   A  1  128 ? -76.77915  19.78924  19.73934  1.000 27.11693  ?  6926 ILE   A N      1 
ATOM   975  C  CA     . ILE   A  1  128 ? -77.69682  20.47417  20.64824  1.000 24.84496  ?  6926 ILE   A CA     1 
ATOM   976  C  C      . ILE   A  1  128 ? -78.06163  19.48804  21.74459  1.000 30.74735  ?  6926 ILE   A C      1 
ATOM   977  O  O      . ILE   A  1  128 ? -78.42502  18.34398  21.45402  1.000 29.16151  ?  6926 ILE   A O      1 
ATOM   978  C  CB     . ILE   A  1  128 ? -78.98507  20.94726  19.94687  1.000 28.21191  ?  6926 ILE   A CB     1 
ATOM   979  C  CG1    . ILE   A  1  128 ? -78.69778  21.68687  18.62492  1.000 28.93773  ?  6926 ILE   A CG1    1 
ATOM   980  C  CG2    . ILE   A  1  128 ? -79.82469  21.78741  20.89078  1.000 28.48725  ?  6926 ILE   A CG2    1 
ATOM   981  C  CD1    . ILE   A  1  128 ? -78.01412  23.01683  18.81300  1.000 31.51520  ?  6926 ILE   A CD1    1 
ATOM   982  N  N      . SER   A  1  129 ? -78.00274  19.92563  22.99488  1.000 25.19111  ?  6927 SER   A N      1 
ATOM   983  C  CA     . SER   A  1  129 ? -78.41321  19.06926  24.09889  1.000 26.50067  ?  6927 SER   A CA     1 
ATOM   984  C  C      . SER   A  1  129 ? -79.34474  19.83028  25.01460  1.000 29.77357  ?  6927 SER   A C      1 
ATOM   985  O  O      . SER   A  1  129 ? -78.98675  20.89123  25.53433  1.000 27.86219  ?  6927 SER   A O      1 
ATOM   986  C  CB     . SER   A  1  129 ? -77.22606  18.55995  24.90077  1.000 25.00034  ?  6927 SER   A CB     1 
ATOM   987  O  OG     . SER   A  1  129 ? -77.71429  17.93781  26.07382  1.000 29.98824  ?  6927 SER   A OG     1 
ATOM   988  N  N      . ASP   A  1  130 ? -80.53079  19.27203  25.22152  1.000 26.78279  ?  6928 ASP   A N      1 
ATOM   989  C  CA     . ASP   A  1  130 ? -81.44077  19.73553  26.25379  1.000 28.62742  ?  6928 ASP   A CA     1 
ATOM   990  C  C      . ASP   A  1  130 ? -81.49457  18.75544  27.42549  1.000 30.02795  ?  6928 ASP   A C      1 
ATOM   991  O  O      . ASP   A  1  130 ? -82.44262  18.76580  28.21069  1.000 25.31398  ?  6928 ASP   A O      1 
ATOM   992  C  CB     . ASP   A  1  130 ? -82.82978  19.96898  25.65174  1.000 28.28185  ?  6928 ASP   A CB     1 
ATOM   993  C  CG     . ASP   A  1  130 ? -83.62858  21.00629  26.43312  1.000 44.25206  ?  6928 ASP   A CG     1 
ATOM   994  O  OD1    . ASP   A  1  130 ? -84.87808  20.86693  26.52905  1.000 44.68867  ?  6928 ASP   A OD1    1 
ATOM   995  O  OD2    . ASP   A  1  130 ? -82.97813  21.92147  27.00837  1.000 48.64716  ?  6928 ASP   A OD2    1 
ATOM   996  N  N      . MET   A  1  131 ? -80.50586  17.87995  27.53742  1.000 26.47732  ?  6929 MET   A N      1 
ATOM   997  C  CA     . MET   A  1  131 ? -80.55746  16.87375  28.58970  1.000 30.43873  ?  6929 MET   A CA     1 
ATOM   998  C  C      . MET   A  1  131 ? -80.53941  17.52782  29.96312  1.000 30.49877  ?  6929 MET   A C      1 
ATOM   999  O  O      . MET   A  1  131 ? -79.79596  18.48500  30.21148  1.000 27.91907  ?  6929 MET   A O      1 
ATOM   1000 C  CB     . MET   A  1  131 ? -79.39365  15.88755  28.44786  1.000 29.73658  ?  6929 MET   A CB     1 
ATOM   1001 C  CG     . MET   A  1  131 ? -79.57963  14.99341  27.22828  1.000 30.03039  ?  6929 MET   A CG     1 
ATOM   1002 S  SD     . MET   A  1  131 ? -78.44994  13.58806  27.20552  1.000 31.78567  ?  6929 MET   A SD     1 
ATOM   1003 C  CE     . MET   A  1  131 ? -76.91980  14.43186  26.86371  1.000 31.03451  ?  6929 MET   A CE     1 
ATOM   1004 N  N      . TYR   A  1  132 ? -81.38757  17.01562  30.84711  1.000 27.31234  ?  6930 TYR   A N      1 
ATOM   1005 C  CA     . TYR   A  1  132 ? -81.59525  17.61998  32.15292  1.000 31.15546  ?  6930 TYR   A CA     1 
ATOM   1006 C  C      . TYR   A  1  132 ? -82.28295  16.61092  33.05741  1.000 34.93447  ?  6930 TYR   A C      1 
ATOM   1007 O  O      . TYR   A  1  132 ? -83.25650  15.97986  32.64417  1.000 32.23006  ?  6930 TYR   A O      1 
ATOM   1008 C  CB     . TYR   A  1  132 ? -82.45212  18.87741  32.03055  1.000 31.14055  ?  6930 TYR   A CB     1 
ATOM   1009 C  CG     . TYR   A  1  132 ? -82.74574  19.52873  33.35078  1.000 35.08080  ?  6930 TYR   A CG     1 
ATOM   1010 C  CD1    . TYR   A  1  132 ? -81.72259  20.08020  34.11249  1.000 33.40425  ?  6930 TYR   A CD1    1 
ATOM   1011 C  CD2    . TYR   A  1  132 ? -84.04841  19.59518  33.83997  1.000 40.14483  ?  6930 TYR   A CD2    1 
ATOM   1012 C  CE1    . TYR   A  1  132 ? -81.97996  20.67659  35.34014  1.000 35.38781  ?  6930 TYR   A CE1    1 
ATOM   1013 C  CE2    . TYR   A  1  132 ? -84.32241  20.19980  35.05741  1.000 41.76250  ?  6930 TYR   A CE2    1 
ATOM   1014 C  CZ     . TYR   A  1  132 ? -83.28653  20.73551  35.80102  1.000 40.49620  ?  6930 TYR   A CZ     1 
ATOM   1015 O  OH     . TYR   A  1  132 ? -83.56226  21.32621  37.00545  1.000 47.81076  ?  6930 TYR   A OH     1 
ATOM   1016 N  N      . ASP   A  1  133 ? -81.79480  16.47687  34.28412  1.000 34.24993  ?  6931 ASP   A N      1 
ATOM   1017 C  CA     . ASP   A  1  133 ? -82.46343  15.65119  35.28770  1.000 42.49564  ?  6931 ASP   A CA     1 
ATOM   1018 C  C      . ASP   A  1  133 ? -82.98614  16.51867  36.42636  1.000 40.18668  ?  6931 ASP   A C      1 
ATOM   1019 O  O      . ASP   A  1  133 ? -82.18169  17.06795  37.19241  1.000 43.18222  ?  6931 ASP   A O      1 
ATOM   1020 C  CB     . ASP   A  1  133 ? -81.49582  14.59762  35.82353  1.000 40.80908  ?  6931 ASP   A CB     1 
ATOM   1021 C  CG     . ASP   A  1  133 ? -82.14961  13.66634  36.82932  1.000 57.21378  ?  6931 ASP   A CG     1 
ATOM   1022 O  OD1    . ASP   A  1  133 ? -83.24886  13.99424  37.35210  1.000 55.97562  ?  6931 ASP   A OD1    1 
ATOM   1023 O  OD2    . ASP   A  1  133 ? -81.55281  12.60348  37.09327  1.000 59.76383  ?  6931 ASP   A OD2    1 
ATOM   1024 N  N      . PRO   A  1  134 ? -84.30374  16.66841  36.59804  1.000 47.56162  ?  6932 PRO   A N      1 
ATOM   1025 C  CA     . PRO   A  1  134 ? -84.81333  17.60967  37.61518  1.000 52.28405  ?  6932 PRO   A CA     1 
ATOM   1026 C  C      . PRO   A  1  134 ? -84.44457  17.23386  39.04488  1.000 52.56823  ?  6932 PRO   A C      1 
ATOM   1027 O  O      . PRO   A  1  134 ? -84.56374  18.07855  39.94027  1.000 60.60020  ?  6932 PRO   A O      1 
ATOM   1028 C  CB     . PRO   A  1  134 ? -86.33529  17.57309  37.40429  1.000 50.73675  ?  6932 PRO   A CB     1 
ATOM   1029 C  CG     . PRO   A  1  134 ? -86.53207  16.95953  36.05889  1.000 52.23737  ?  6932 PRO   A CG     1 
ATOM   1030 C  CD     . PRO   A  1  134 ? -85.39816  15.99806  35.88405  1.000 47.14631  ?  6932 PRO   A CD     1 
ATOM   1031 N  N      . LYS   A  1  135 ? -83.98669  16.00494  39.28530  1.000 52.20221  ?  6933 LYS   A N      1 
ATOM   1032 C  CA     . LYS   A  1  135 ? -83.47549  15.62807  40.59519  1.000 56.43302  ?  6933 LYS   A CA     1 
ATOM   1033 C  C      . LYS   A  1  135 ? -82.12893  16.27221  40.93026  1.000 63.39173  ?  6933 LYS   A C      1 
ATOM   1034 O  O      . LYS   A  1  135 ? -81.56424  15.96044  41.98984  1.000 64.62738  ?  6933 LYS   A O      1 
ATOM   1035 C  CB     . LYS   A  1  135 ? -83.37422  14.10440  40.68439  1.000 59.39473  ?  6933 LYS   A CB     1 
ATOM   1036 C  CG     . LYS   A  1  135 ? -84.73503  13.41804  40.75136  1.000 56.28017  ?  6933 LYS   A CG     1 
ATOM   1037 C  CD     . LYS   A  1  135 ? -84.60702  11.98531  41.24625  1.000 67.70019  ?  6933 LYS   A CD     1 
ATOM   1038 C  CE     . LYS   A  1  135 ? -84.15282  11.02355  40.15468  1.000 69.07184  ?  6933 LYS   A CE     1 
ATOM   1039 N  NZ     . LYS   A  1  135 ? -85.29288  10.16455  39.71959  1.000 70.20913  ?  6933 LYS   A NZ     1 
ATOM   1040 N  N      . THR   A  1  136 ? -81.59030  17.15063  40.07537  1.000 56.80329  ?  6934 THR   A N      1 
ATOM   1041 C  CA     . THR   A  1  136 ? -80.41111  17.92296  40.45711  1.000 55.09798  ?  6934 THR   A CA     1 
ATOM   1042 C  C      . THR   A  1  136 ? -80.76002  19.20220  41.21064  1.000 52.83257  ?  6934 THR   A C      1 
ATOM   1043 O  O      . THR   A  1  136 ? -79.87888  19.78136  41.85394  1.000 59.95058  ?  6934 THR   A O      1 
ATOM   1044 C  CB     . THR   A  1  136 ? -79.56064  18.29840  39.22907  1.000 49.91457  ?  6934 THR   A CB     1 
ATOM   1045 O  OG1    . THR   A  1  136 ? -80.36266  19.03951  38.29718  1.000 46.56970  ?  6934 THR   A OG1    1 
ATOM   1046 C  CG2    . THR   A  1  136 ? -78.97182  17.05970  38.55431  1.000 43.24859  ?  6934 THR   A CG2    1 
ATOM   1047 N  N      . LYS   A  1  137 ? -82.01004  19.66245  41.14106  1.000 54.74518  ?  6935 LYS   A N      1 
ATOM   1048 C  CA     . LYS   A  1  137 ? -82.42000  20.90724  41.79351  1.000 60.61138  ?  6935 LYS   A CA     1 
ATOM   1049 C  C      . LYS   A  1  137 ? -82.60269  20.75030  43.30095  1.000 69.18629  ?  6935 LYS   A C      1 
ATOM   1050 O  O      . LYS   A  1  137 ? -83.49881  21.35903  43.89161  1.000 73.68813  ?  6935 LYS   A O      1 
ATOM   1051 C  CB     . LYS   A  1  137 ? -83.69942  21.42720  41.14226  1.000 60.74164  ?  6935 LYS   A CB     1 
ATOM   1052 C  CG     . LYS   A  1  137 ? -83.90423  22.93148  41.28550  1.000 68.00000  ?  6935 LYS   A CG     1 
ATOM   1053 C  CD     . LYS   A  1  137 ? -85.03959  23.41797  40.38130  1.000 78.59958  ?  6935 LYS   A CD     1 
ATOM   1054 C  CE     . LYS   A  1  137 ? -85.18521  24.94250  40.41146  1.000 84.85879  ?  6935 LYS   A CE     1 
ATOM   1055 N  NZ     . LYS   A  1  137 ? -86.42572  25.41594  39.71645  1.000 86.81470  ?  6935 LYS   A NZ     1 
ATOM   1056 N  N      . ASN   A  1  138 ? -81.75482  19.93763  43.93423  1.000 70.93564  ?  6936 ASN   A N      1 
ATOM   1057 C  CA     . ASN   A  1  138 ? -81.77211  19.70575  45.37982  1.000 70.63275  ?  6936 ASN   A CA     1 
ATOM   1058 C  C      . ASN   A  1  138 ? -80.95220  20.80096  46.06075  1.000 69.63832  ?  6936 ASN   A C      1 
ATOM   1059 O  O      . ASN   A  1  138 ? -79.71827  20.73540  46.10556  1.000 64.30883  ?  6936 ASN   A O      1 
ATOM   1060 C  CB     . ASN   A  1  138 ? -81.22553  18.31554  45.68849  1.000 67.55191  ?  6936 ASN   A CB     1 
ATOM   1061 C  CG     . ASN   A  1  138 ? -81.29157  17.97394  47.16007  1.000 78.32492  ?  6936 ASN   A CG     1 
ATOM   1062 O  OD1    . ASN   A  1  138 ? -81.15036  18.84375  48.02253  1.000 71.80493  ?  6936 ASN   A OD1    1 
ATOM   1063 N  ND2    . ASN   A  1  138 ? -81.50163  16.69373  47.45849  1.000 80.93449  ?  6936 ASN   A ND2    1 
ATOM   1064 N  N      . VAL   A  1  139 ? -81.64700  21.81185  46.60180  1.000 67.33252  ?  6937 VAL   A N      1 
ATOM   1065 C  CA     . VAL   A  1  139 ? -80.99437  22.97223  47.21364  1.000 69.07766  ?  6937 VAL   A CA     1 
ATOM   1066 C  C      . VAL   A  1  139 ? -80.39329  22.68569  48.58361  1.000 72.34760  ?  6937 VAL   A C      1 
ATOM   1067 O  O      . VAL   A  1  139 ? -79.71004  23.55707  49.14123  1.000 68.67303  ?  6937 VAL   A O      1 
ATOM   1068 C  CB     . VAL   A  1  139 ? -81.98724  24.14897  47.33788  1.000 71.88345  ?  6937 VAL   A CB     1 
ATOM   1069 C  CG1    . VAL   A  1  139 ? -82.51363  24.56424  45.96127  1.000 69.59708  ?  6937 VAL   A CG1    1 
ATOM   1070 C  CG2    . VAL   A  1  139 ? -83.14309  23.79437  48.27876  1.000 68.86208  ?  6937 VAL   A CG2    1 
ATOM   1071 N  N      . THR   A  1  140 ? -80.59919  21.48674  49.13728  1.000 69.29789  ?  6938 THR   A N      1 
ATOM   1072 C  CA     . THR   A  1  140 ? -80.13157  21.17144  50.48354  1.000 71.55980  ?  6938 THR   A CA     1 
ATOM   1073 C  C      . THR   A  1  140 ? -78.69936  20.63761  50.53220  1.000 68.09797  ?  6938 THR   A C      1 
ATOM   1074 O  O      . THR   A  1  140 ? -78.08055  20.68245  51.60297  1.000 68.60209  ?  6938 THR   A O      1 
ATOM   1075 C  CB     . THR   A  1  140 ? -81.07356  20.15367  51.15530  1.000 65.84133  ?  6938 THR   A CB     1 
ATOM   1076 O  OG1    . THR   A  1  140 ? -81.01107  18.90127  50.46224  1.000 64.82251  ?  6938 THR   A OG1    1 
ATOM   1077 C  CG2    . THR   A  1  140 ? -82.52406  20.66069  51.15934  1.000 59.15925  ?  6938 THR   A CG2    1 
ATOM   1078 N  N      . LYS   A  1  141 ? -78.15394  20.14396  49.41954  1.000 67.92252  ?  6939 LYS   A N      1 
ATOM   1079 C  CA     . LYS   A  1  141 ? -76.80729  19.58435  49.39006  1.000 63.71682  ?  6939 LYS   A CA     1 
ATOM   1080 C  C      . LYS   A  1  141 ? -75.87745  20.45685  48.54743  1.000 56.98384  ?  6939 LYS   A C      1 
ATOM   1081 O  O      . LYS   A  1  141 ? -76.31487  21.27910  47.73526  1.000 58.29975  ?  6939 LYS   A O      1 
ATOM   1082 C  CB     . LYS   A  1  141 ? -76.82113  18.14780  48.84770  1.000 68.98939  ?  6939 LYS   A CB     1 
ATOM   1083 C  CG     . LYS   A  1  141 ? -78.18068  17.44387  48.96245  1.000 73.08486  ?  6939 LYS   A CG     1 
ATOM   1084 C  CD     . LYS   A  1  141 ? -78.07164  15.92232  48.79363  1.000 78.34530  ?  6939 LYS   A CD     1 
ATOM   1085 C  CE     . LYS   A  1  141 ? -77.93283  15.50709  47.32684  1.000 81.22289  ?  6939 LYS   A CE     1 
ATOM   1086 N  NZ     . LYS   A  1  141 ? -77.45750  14.09509  47.17748  1.000 78.17293  ?  6939 LYS   A NZ     1 
ATOM   1087 N  N      . GLU   A  1  142 ? -74.57737  20.26936  48.75763  1.000 49.71730  ?  6940 GLU   A N      1 
ATOM   1088 C  CA     . GLU   A  1  142 ? -73.57715  21.06123  48.05851  1.000 48.85321  ?  6940 GLU   A CA     1 
ATOM   1089 C  C      . GLU   A  1  142 ? -73.74636  20.94007  46.54485  1.000 50.90767  ?  6940 GLU   A C      1 
ATOM   1090 O  O      . GLU   A  1  142 ? -74.25476  19.93993  46.03392  1.000 48.88751  ?  6940 GLU   A O      1 
ATOM   1091 C  CB     . GLU   A  1  142 ? -72.19073  20.60750  48.47406  1.000 47.08763  ?  6940 GLU   A CB     1 
ATOM   1092 C  CG     . GLU   A  1  142 ? -71.06905  21.45801  47.93752  1.000 58.11924  ?  6940 GLU   A CG     1 
ATOM   1093 C  CD     . GLU   A  1  142 ? -69.73512  21.03598  48.51665  1.000 73.05641  ?  6940 GLU   A CD     1 
ATOM   1094 O  OE1    . GLU   A  1  142 ? -68.69794  21.20525  47.83466  1.000 80.68689  ?  6940 GLU   A OE1    1 
ATOM   1095 O  OE2    . GLU   A  1  142 ? -69.73558  20.52304  49.66203  1.000 73.35211  ?  6940 GLU   A OE2    1 
ATOM   1096 N  N      . ASN   A  1  143 ? -73.32253  21.97495  45.82204  1.000 44.55147  ?  6941 ASN   A N      1 
ATOM   1097 C  CA     . ASN   A  1  143 ? -73.51462  22.05008  44.36880  1.000 45.79343  ?  6941 ASN   A CA     1 
ATOM   1098 C  C      . ASN   A  1  143 ? -72.18094  21.77576  43.67244  1.000 41.24673  ?  6941 ASN   A C      1 
ATOM   1099 O  O      . ASN   A  1  143 ? -71.42223  22.69171  43.35876  1.000 39.21727  ?  6941 ASN   A O      1 
ATOM   1100 C  CB     . ASN   A  1  143 ? -74.08801  23.41055  43.95459  1.000 40.86396  ?  6941 ASN   A CB     1 
ATOM   1101 C  CG     . ASN   A  1  143 ? -74.31624  23.51106  42.44619  1.000 40.05954  ?  6941 ASN   A CG     1 
ATOM   1102 O  OD1    . ASN   A  1  143 ? -74.28882  22.50458  41.73903  1.000 35.92366  ?  6941 ASN   A OD1    1 
ATOM   1103 N  ND2    . ASN   A  1  143 ? -74.54562  24.72200  41.95544  1.000 35.08832  ?  6941 ASN   A ND2    1 
ATOM   1104 N  N      . ASP   A  1  144 ? -71.90669  20.50954  43.40290  1.000 38.47790  ?  6942 ASP   A N      1 
ATOM   1105 C  CA     . ASP   A  1  144 ? -70.64676  20.13375  42.77778  1.000 39.63545  ?  6942 ASP   A CA     1 
ATOM   1106 C  C      . ASP   A  1  144 ? -70.82626  19.85662  41.28029  1.000 35.87905  ?  6942 ASP   A C      1 
ATOM   1107 O  O      . ASP   A  1  144 ? -71.94214  19.67257  40.78239  1.000 36.57457  ?  6942 ASP   A O      1 
ATOM   1108 C  CB     . ASP   A  1  144 ? -70.05644  18.90478  43.47821  1.000 48.12121  ?  6942 ASP   A CB     1 
ATOM   1109 C  CG     . ASP   A  1  144 ? -68.56217  18.71418  43.18218  1.000 62.42350  ?  6942 ASP   A CG     1 
ATOM   1110 O  OD1    . ASP   A  1  144 ? -67.94326  19.61899  42.55239  1.000 57.38914  ?  6942 ASP   A OD1    1 
ATOM   1111 O  OD2    . ASP   A  1  144 ? -68.00954  17.65269  43.58013  1.000 69.80754  ?  6942 ASP   A OD2    1 
ATOM   1112 N  N      . SER   A  1  145 ? -69.70529  19.86035  40.56130  1.000 32.56442  ?  6943 SER   A N      1 
ATOM   1113 C  CA     . SER   A  1  145 ? -69.71796  19.50929  39.15189  1.000 35.26914  ?  6943 SER   A CA     1 
ATOM   1114 C  C      . SER   A  1  145 ? -70.36163  18.13953  38.98252  1.000 36.24586  ?  6943 SER   A C      1 
ATOM   1115 O  O      . SER   A  1  145 ? -70.09075  17.21914  39.75373  1.000 33.37696  ?  6943 SER   A O      1 
ATOM   1116 C  CB     . SER   A  1  145 ? -68.29367  19.51493  38.60960  1.000 33.87452  ?  6943 SER   A CB     1 
ATOM   1117 O  OG     . SER   A  1  145 ? -68.23927  19.14101  37.24131  1.000 34.32459  ?  6943 SER   A OG     1 
ATOM   1118 N  N      . LYS   A  1  146 ? -71.25876  18.01482  38.01064  1.000 30.01600  ?  6944 LYS   A N      1 
ATOM   1119 C  CA     . LYS   A  1  146 ? -71.99538  16.77472  37.81423  1.000 33.90880  ?  6944 LYS   A CA     1 
ATOM   1120 C  C      . LYS   A  1  146 ? -71.37662  15.94568  36.68948  1.000 36.46396  ?  6944 LYS   A C      1 
ATOM   1121 O  O      . LYS   A  1  146 ? -70.80193  16.47770  35.73688  1.000 36.51875  ?  6944 LYS   A O      1 
ATOM   1122 C  CB     . LYS   A  1  146 ? -73.46517  17.06313  37.49967  1.000 34.84811  ?  6944 LYS   A CB     1 
ATOM   1123 C  CG     . LYS   A  1  146 ? -74.14625  18.00319  38.50672  1.000 34.80262  ?  6944 LYS   A CG     1 
ATOM   1124 C  CD     . LYS   A  1  146 ? -74.31043  17.32737  39.87782  1.000 37.89364  ?  6944 LYS   A CD     1 
ATOM   1125 C  CE     . LYS   A  1  146 ? -75.18167  18.17881  40.79440  1.000 36.93061  ?  6944 LYS   A CE     1 
ATOM   1126 N  NZ     . LYS   A  1  146 ? -74.61957  19.56912  40.97299  1.000 34.85295  ?  6944 LYS   A NZ     1 
ATOM   1127 N  N      . GLU   A  1  147 ? -71.52154  14.62821  36.79440  1.000 35.66875  ?  6945 GLU   A N      1 
ATOM   1128 C  CA     . GLU   A  1  147 ? -71.00394  13.73456  35.76386  1.000 38.14671  ?  6945 GLU   A CA     1 
ATOM   1129 C  C      . GLU   A  1  147 ? -72.13462  13.27224  34.85511  1.000 41.03382  ?  6945 GLU   A C      1 
ATOM   1130 O  O      . GLU   A  1  147 ? -72.71301  14.07857  34.11925  1.000 38.01551  ?  6945 GLU   A O      1 
ATOM   1131 C  CB     . GLU   A  1  147 ? -70.30964  12.52978  36.39763  1.000 41.90628  ?  6945 GLU   A CB     1 
ATOM   1132 C  CG     . GLU   A  1  147 ? -69.47120  12.90851  37.57963  1.000 47.40752  ?  6945 GLU   A CG     1 
ATOM   1133 C  CD     . GLU   A  1  147 ? -68.04687  13.18355  37.19785  1.000 62.23835  ?  6945 GLU   A CD     1 
ATOM   1134 O  OE1    . GLU   A  1  147 ? -67.15306  12.46905  37.71439  1.000 69.82633  ?  6945 GLU   A OE1    1 
ATOM   1135 O  OE2    . GLU   A  1  147 ? -67.82268  14.10110  36.37557  1.000 63.03679  ?  6945 GLU   A OE2    1 
ATOM   1136 N  N      . GLY   A  1  148 ? -72.46506  11.98288  34.91926  1.000 33.76476  ?  6946 GLY   A N      1 
ATOM   1137 C  CA     . GLY   A  1  148 ? -73.59720  11.45424  34.16875  1.000 34.27493  ?  6946 GLY   A CA     1 
ATOM   1138 C  C      . GLY   A  1  148 ? -73.50429  11.80130  32.70258  1.000 29.52212  ?  6946 GLY   A C      1 
ATOM   1139 O  O      . GLY   A  1  148 ? -72.45667  11.65631  32.06847  1.000 33.29330  ?  6946 GLY   A O      1 
ATOM   1140 N  N      . PHE   A  1  149 ? -74.59514  12.31915  32.13546  1.000 31.34310  ?  6947 PHE   A N      1 
ATOM   1141 C  CA     . PHE   A  1  149 ? -74.59273  12.57924  30.70085  1.000 30.20237  ?  6947 PHE   A CA     1 
ATOM   1142 C  C      . PHE   A  1  149 ? -73.60078  13.66429  30.30505  1.000 32.67875  ?  6947 PHE   A C      1 
ATOM   1143 O  O      . PHE   A  1  149 ? -73.25613  13.76333  29.12222  1.000 30.95123  ?  6947 PHE   A O      1 
ATOM   1144 C  CB     . PHE   A  1  149 ? -76.00933  12.92830  30.21040  1.000 35.42792  ?  6947 PHE   A CB     1 
ATOM   1145 C  CG     . PHE   A  1  149 ? -76.59092  14.20144  30.79931  1.000 32.02736  ?  6947 PHE   A CG     1 
ATOM   1146 C  CD1    . PHE   A  1  149 ? -76.11034  15.45636  30.40391  1.000 30.67445  ?  6947 PHE   A CD1    1 
ATOM   1147 C  CD2    . PHE   A  1  149 ? -77.65153  14.14521  31.69903  1.000 33.69589  ?  6947 PHE   A CD2    1 
ATOM   1148 C  CE1    . PHE   A  1  149 ? -76.66450  16.63765  30.93186  1.000 30.48798  ?  6947 PHE   A CE1    1 
ATOM   1149 C  CE2    . PHE   A  1  149 ? -78.21901  15.32361  32.23284  1.000 33.65314  ?  6947 PHE   A CE2    1 
ATOM   1150 C  CZ     . PHE   A  1  149 ? -77.72145  16.56555  31.84788  1.000 30.10456  ?  6947 PHE   A CZ     1 
ATOM   1151 N  N      . PHE   A  1  150 ? -73.13511  14.48607  31.25113  1.000 31.31597  ?  6948 PHE   A N      1 
ATOM   1152 C  CA     . PHE   A  1  150 ? -72.13295  15.48836  30.90146  1.000 30.10624  ?  6948 PHE   A CA     1 
ATOM   1153 C  C      . PHE   A  1  150 ? -70.80697  14.84794  30.54379  1.000 32.93260  ?  6948 PHE   A C      1 
ATOM   1154 O  O      . PHE   A  1  150 ? -70.07109  15.37646  29.70300  1.000 32.38869  ?  6948 PHE   A O      1 
ATOM   1155 C  CB     . PHE   A  1  150 ? -71.90744  16.48270  32.04796  1.000 29.58762  ?  6948 PHE   A CB     1 
ATOM   1156 C  CG     . PHE   A  1  150 ? -72.98620  17.52184  32.18509  1.000 30.39772  ?  6948 PHE   A CG     1 
ATOM   1157 C  CD1    . PHE   A  1  150 ? -73.11003  18.53832  31.26086  1.000 31.74630  ?  6948 PHE   A CD1    1 
ATOM   1158 C  CD2    . PHE   A  1  150 ? -73.85193  17.49849  33.26564  1.000 29.56901  ?  6948 PHE   A CD2    1 
ATOM   1159 C  CE1    . PHE   A  1  150 ? -74.09404  19.51035  31.40397  1.000 32.87218  ?  6948 PHE   A CE1    1 
ATOM   1160 C  CE2    . PHE   A  1  150 ? -74.83124  18.46073  33.40946  1.000 32.43104  ?  6948 PHE   A CE2    1 
ATOM   1161 C  CZ     . PHE   A  1  150 ? -74.95508  19.47012  32.46994  1.000 28.72881  ?  6948 PHE   A CZ     1 
ATOM   1162 N  N      . THR   A  1  151 ? -70.46328  13.73411  31.19047  1.000 31.71581  ?  6949 THR   A N      1 
ATOM   1163 C  CA     . THR   A  1  151 ? -69.24876  13.02603  30.80634  1.000 35.48195  ?  6949 THR   A CA     1 
ATOM   1164 C  C      . THR   A  1  151 ? -69.35979  12.53547  29.37673  1.000 31.37555  ?  6949 THR   A C      1 
ATOM   1165 O  O      . THR   A  1  151 ? -68.42542  12.69023  28.58070  1.000 33.96444  ?  6949 THR   A O      1 
ATOM   1166 C  CB     . THR   A  1  151 ? -68.99130  11.86383  31.76092  1.000 37.02064  ?  6949 THR   A CB     1 
ATOM   1167 O  OG1    . THR   A  1  151 ? -68.97111  12.36373  33.09969  1.000 40.85747  ?  6949 THR   A OG1    1 
ATOM   1168 C  CG2    . THR   A  1  151 ? -67.64240  11.21498  31.45886  1.000 37.46393  ?  6949 THR   A CG2    1 
ATOM   1169 N  N      . TYR   A  1  152 ? -70.52145  11.98632  29.01337  1.000 30.44817  ?  6950 TYR   A N      1 
ATOM   1170 C  CA     . TYR   A  1  152 ? -70.71860  11.55326  27.63461  1.000 30.11289  ?  6950 TYR   A CA     1 
ATOM   1171 C  C      . TYR   A  1  152 ? -70.59504  12.72717  26.67262  1.000 29.68960  ?  6950 TYR   A C      1 
ATOM   1172 O  O      . TYR   A  1  152 ? -69.89157  12.64625  25.66070  1.000 33.12920  ?  6950 TYR   A O      1 
ATOM   1173 C  CB     . TYR   A  1  152 ? -72.08354  10.88355  27.49118  1.000 31.90158  ?  6950 TYR   A CB     1 
ATOM   1174 C  CG     . TYR   A  1  152 ? -72.41452  10.52935  26.07043  1.000 35.63998  ?  6950 TYR   A CG     1 
ATOM   1175 C  CD1    . TYR   A  1  152 ? -71.90704  9.36846   25.48735  1.000 35.23262  ?  6950 TYR   A CD1    1 
ATOM   1176 C  CD2    . TYR   A  1  152 ? -73.22387  11.36242  25.29609  1.000 33.18425  ?  6950 TYR   A CD2    1 
ATOM   1177 C  CE1    . TYR   A  1  152 ? -72.21550  9.03813   24.16729  1.000 35.12735  ?  6950 TYR   A CE1    1 
ATOM   1178 C  CE2    . TYR   A  1  152 ? -73.53299  11.04958  23.98194  1.000 35.02258  ?  6950 TYR   A CE2    1 
ATOM   1179 C  CZ     . TYR   A  1  152 ? -73.02350  9.88503   23.42007  1.000 38.43442  ?  6950 TYR   A CZ     1 
ATOM   1180 O  OH     . TYR   A  1  152 ? -73.32723  9.56496   22.11613  1.000 37.72249  ?  6950 TYR   A OH     1 
ATOM   1181 N  N      . ILE   A  1  153 ? -71.26519  13.84386  26.98429  1.000 34.28545  ?  6951 ILE   A N      1 
ATOM   1182 C  CA     . ILE   A  1  153 ? -71.26981  14.99565  26.08077  1.000 28.70781  ?  6951 ILE   A CA     1 
ATOM   1183 C  C      . ILE   A  1  153 ? -69.84825  15.49530  25.81708  1.000 31.70500  ?  6951 ILE   A C      1 
ATOM   1184 O  O      . ILE   A  1  153 ? -69.49568  15.83095  24.67766  1.000 34.64014  ?  6951 ILE   A O      1 
ATOM   1185 C  CB     . ILE   A  1  153 ? -72.16366  16.11332  26.64984  1.000 34.71049  ?  6951 ILE   A CB     1 
ATOM   1186 C  CG1    . ILE   A  1  153 ? -73.63235  15.78683  26.41094  1.000 34.21912  ?  6951 ILE   A CG1    1 
ATOM   1187 C  CG2    . ILE   A  1  153 ? -71.84557  17.43148  25.97673  1.000 35.40895  ?  6951 ILE   A CG2    1 
ATOM   1188 C  CD1    . ILE   A  1  153 ? -73.91909  15.44771  24.93832  1.000 44.79879  ?  6951 ILE   A CD1    1 
ATOM   1189 N  N      . CYS   A  1  154 ? -69.02521  15.61208  26.86228  1.000 30.15016  ?  6952 CYS   A N      1 
ATOM   1190 C  CA     . CYS   A  1  154 ? -67.65354  16.07642  26.64878  1.000 33.08392  ?  6952 CYS   A CA     1 
ATOM   1191 C  C      . CYS   A  1  154 ? -66.89990  15.13309  25.71969  1.000 35.53377  ?  6952 CYS   A C      1 
ATOM   1192 O  O      . CYS   A  1  154 ? -66.19429  15.57337  24.80396  1.000 32.48689  ?  6952 CYS   A O      1 
ATOM   1193 C  CB     . CYS   A  1  154 ? -66.90633  16.19308  27.97666  1.000 33.11351  ?  6952 CYS   A CB     1 
ATOM   1194 S  SG     . CYS   A  1  154 ? -67.48543  17.54402  29.04126  1.000 38.38851  ?  6952 CYS   A SG     1 
ATOM   1195 N  N      . GLY   A  1  155 ? -67.01719  13.82229  25.96127  1.000 35.15078  ?  6953 GLY   A N      1 
ATOM   1196 C  CA     . GLY   A  1  155 ? -66.34887  12.86864  25.09400  1.000 30.58287  ?  6953 GLY   A CA     1 
ATOM   1197 C  C      . GLY   A  1  155 ? -66.90180  12.91499  23.68609  1.000 33.63281  ?  6953 GLY   A C      1 
ATOM   1198 O  O      . GLY   A  1  155 ? -66.15142  12.89010  22.70831  1.000 34.53833  ?  6953 GLY   A O      1 
ATOM   1199 N  N      . PHE   A  1  156 ? -68.22685  13.01301  23.56276  1.000 34.14989  ?  6954 PHE   A N      1 
ATOM   1200 C  CA     . PHE   A  1  156 ? -68.82541  13.08486  22.23838  1.000 30.65732  ?  6954 PHE   A CA     1 
ATOM   1201 C  C      . PHE   A  1  156 ? -68.31523  14.30263  21.48544  1.000 33.31361  ?  6954 PHE   A C      1 
ATOM   1202 O  O      . PHE   A  1  156 ? -68.04418  14.23126  20.28314  1.000 33.74042  ?  6954 PHE   A O      1 
ATOM   1203 C  CB     . PHE   A  1  156 ? -70.35286  13.10840  22.34832  1.000 34.99242  ?  6954 PHE   A CB     1 
ATOM   1204 C  CG     . PHE   A  1  156 ? -71.05880  12.88933  21.03680  1.000 36.02286  ?  6954 PHE   A CG     1 
ATOM   1205 C  CD1    . PHE   A  1  156 ? -71.33548  13.95480  20.19673  1.000 32.99386  ?  6954 PHE   A CD1    1 
ATOM   1206 C  CD2    . PHE   A  1  156 ? -71.43105  11.60813  20.63730  1.000 35.46323  ?  6954 PHE   A CD2    1 
ATOM   1207 C  CE1    . PHE   A  1  156 ? -71.97090  13.75096  18.98150  1.000 36.09892  ?  6954 PHE   A CE1    1 
ATOM   1208 C  CE2    . PHE   A  1  156 ? -72.07105  11.40383  19.42307  1.000 37.06409  ?  6954 PHE   A CE2    1 
ATOM   1209 C  CZ     . PHE   A  1  156 ? -72.34297  12.48025  18.59805  1.000 34.32217  ?  6954 PHE   A CZ     1 
ATOM   1210 N  N      . ILE   A  1  157 ? -68.14723  15.42976  22.17606  1.000 32.76697  ?  6955 ILE   A N      1 
ATOM   1211 C  CA     . ILE   A  1  157 ? -67.68035  16.62449  21.48403  1.000 32.13135  ?  6955 ILE   A CA     1 
ATOM   1212 C  C      . ILE   A  1  157 ? -66.25814  16.42424  20.98181  1.000 35.69987  ?  6955 ILE   A C      1 
ATOM   1213 O  O      . ILE   A  1  157 ? -65.94248  16.71561  19.82152  1.000 36.59399  ?  6955 ILE   A O      1 
ATOM   1214 C  CB     . ILE   A  1  157 ? -67.78506  17.85492  22.39964  1.000 34.24168  ?  6955 ILE   A CB     1 
ATOM   1215 C  CG1    . ILE   A  1  157 ? -69.25323  18.25676  22.57137  1.000 32.55944  ?  6955 ILE   A CG1    1 
ATOM   1216 C  CG2    . ILE   A  1  157 ? -66.97191  19.00265  21.81850  1.000 36.73709  ?  6955 ILE   A CG2    1 
ATOM   1217 C  CD1    . ILE   A  1  157 ? -69.47433  19.31808  23.67805  1.000 29.95839  ?  6955 ILE   A CD1    1 
ATOM   1218 N  N      . GLN   A  1  158 ? -65.37992  15.91170  21.84436  1.000 33.62063  ?  6956 GLN   A N      1 
ATOM   1219 C  CA     . GLN   A  1  158 ? -63.97754  15.78448  21.46837  1.000 36.19579  ?  6956 GLN   A CA     1 
ATOM   1220 C  C      . GLN   A  1  158 ? -63.76181  14.73939  20.37918  1.000 39.33307  ?  6956 GLN   A C      1 
ATOM   1221 O  O      . GLN   A  1  158 ? -62.83803  14.87651  19.57549  1.000 43.13759  ?  6956 GLN   A O      1 
ATOM   1222 C  CB     . GLN   A  1  158 ? -63.14541  15.44038  22.69295  1.000 38.38657  ?  6956 GLN   A CB     1 
ATOM   1223 C  CG     . GLN   A  1  158 ? -63.14837  16.54195  23.71580  1.000 41.99582  ?  6956 GLN   A CG     1 
ATOM   1224 C  CD     . GLN   A  1  158 ? -62.38447  16.17687  24.95567  1.000 42.84210  ?  6956 GLN   A CD     1 
ATOM   1225 O  OE1    . GLN   A  1  158 ? -61.19971  16.47323  25.06948  1.000 52.76321  ?  6956 GLN   A OE1    1 
ATOM   1226 N  NE2    . GLN   A  1  158 ? -63.05913  15.53630  25.90177  1.000 42.23495  ?  6956 GLN   A NE2    1 
ATOM   1227 N  N      . GLN   A  1  159 ? -64.58597  13.69595  20.33178  1.000 35.83914  ?  6957 GLN   A N      1 
ATOM   1228 C  CA     . GLN   A  1  159 ? -64.40094  12.63667  19.34453  1.000 38.80692  ?  6957 GLN   A CA     1 
ATOM   1229 C  C      . GLN   A  1  159 ? -65.24312  12.81493  18.08723  1.000 38.03163  ?  6957 GLN   A C      1 
ATOM   1230 O  O      . GLN   A  1  159 ? -64.82700  12.36524  17.01887  1.000 36.37063  ?  6957 GLN   A O      1 
ATOM   1231 C  CB     . GLN   A  1  159 ? -64.71445  11.26817  19.97071  1.000 41.08817  ?  6957 GLN   A CB     1 
ATOM   1232 C  CG     . GLN   A  1  159 ? -63.88625  10.95307  21.21010  1.000 45.57451  ?  6957 GLN   A CG     1 
ATOM   1233 C  CD     . GLN   A  1  159 ? -64.57697  9.96437   22.14763  1.000 56.40092  ?  6957 GLN   A CD     1 
ATOM   1234 O  OE1    . GLN   A  1  159 ? -65.40122  9.15018   21.71978  1.000 59.94769  ?  6957 GLN   A OE1    1 
ATOM   1235 N  NE2    . GLN   A  1  159 ? -64.24655  10.03917  23.43593  1.000 60.52932  ?  6957 GLN   A NE2    1 
ATOM   1236 N  N      . LYS   A  1  160 ? -66.40636  13.46890  18.16655  1.000 32.06568  ?  6958 LYS   A N      1 
ATOM   1237 C  CA     . LYS   A  1  160 ? -67.35969  13.43719  17.06803  1.000 32.96001  ?  6958 LYS   A CA     1 
ATOM   1238 C  C      . LYS   A  1  160 ? -67.82363  14.80698  16.58639  1.000 36.77107  ?  6958 LYS   A C      1 
ATOM   1239 O  O      . LYS   A  1  160 ? -68.69632  14.86951  15.71256  1.000 33.10880  ?  6958 LYS   A O      1 
ATOM   1240 C  CB     . LYS   A  1  160 ? -68.59361  12.60406  17.46102  1.000 33.99000  ?  6958 LYS   A CB     1 
ATOM   1241 C  CG     . LYS   A  1  160 ? -68.25137  11.18103  17.92606  1.000 38.61670  ?  6958 LYS   A CG     1 
ATOM   1242 C  CD     . LYS   A  1  160 ? -67.79100  10.34927  16.75647  1.000 40.48884  ?  6958 LYS   A CD     1 
ATOM   1243 C  CE     . LYS   A  1  160 ? -67.26559  8.97902   17.20591  1.000 48.49969  ?  6958 LYS   A CE     1 
ATOM   1244 N  NZ     . LYS   A  1  160 ? -66.84885  8.21894   15.99976  1.000 51.58328  ?  6958 LYS   A NZ     1 
ATOM   1245 N  N      . LEU   A  1  161 ? -67.27651  15.90081  17.10389  1.000 30.15170  ?  6959 LEU   A N      1 
ATOM   1246 C  CA     . LEU   A  1  161 ? -67.63644  17.20802  16.57364  1.000 31.74961  ?  6959 LEU   A CA     1 
ATOM   1247 C  C      . LEU   A  1  161 ? -66.62706  17.60095  15.50064  1.000 30.79491  ?  6959 LEU   A C      1 
ATOM   1248 O  O      . LEU   A  1  161 ? -65.41627  17.56771  15.73024  1.000 30.72856  ?  6959 LEU   A O      1 
ATOM   1249 C  CB     . LEU   A  1  161 ? -67.70036  18.26471  17.68548  1.000 27.33892  ?  6959 LEU   A CB     1 
ATOM   1250 C  CG     . LEU   A  1  161 ? -68.13244  19.65498  17.22167  1.000 31.15790  ?  6959 LEU   A CG     1 
ATOM   1251 C  CD1    . LEU   A  1  161 ? -69.58645  19.65098  16.70540  1.000 27.73457  ?  6959 LEU   A CD1    1 
ATOM   1252 C  CD2    . LEU   A  1  161 ? -67.96557  20.63774  18.36802  1.000 31.50586  ?  6959 LEU   A CD2    1 
ATOM   1253 N  N      . ALA   A  1  162 ? -67.12493  17.95133  14.32497  1.000 31.63988  ?  6960 ALA   A N      1 
ATOM   1254 C  CA     . ALA   A  1  162 ? -66.23146  18.38799  13.26214  1.000 33.99482  ?  6960 ALA   A CA     1 
ATOM   1255 C  C      . ALA   A  1  162 ? -65.48968  19.64799  13.68274  1.000 38.25885  ?  6960 ALA   A C      1 
ATOM   1256 O  O      . ALA   A  1  162 ? -66.03636  20.50728  14.37796  1.000 33.43798  ?  6960 ALA   A O      1 
ATOM   1257 C  CB     . ALA   A  1  162 ? -67.02230  18.67594  11.99334  1.000 31.90312  ?  6960 ALA   A CB     1 
ATOM   1258 N  N      . LEU   A  1  163 ? -64.24935  19.78803  13.21878  1.000 35.33891  ?  6961 LEU   A N      1 
ATOM   1259 C  CA     . LEU   A  1  163 ? -63.58824  21.07419  13.38510  1.000 36.13813  ?  6961 LEU   A CA     1 
ATOM   1260 C  C      . LEU   A  1  163 ? -64.39926  22.13642  12.66574  1.000 32.22867  ?  6961 LEU   A C      1 
ATOM   1261 O  O      . LEU   A  1  163 ? -64.85583  21.92889  11.54202  1.000 32.97100  ?  6961 LEU   A O      1 
ATOM   1262 C  CB     . LEU   A  1  163 ? -62.16219  21.03316  12.83732  1.000 38.50294  ?  6961 LEU   A CB     1 
ATOM   1263 C  CG     . LEU   A  1  163 ? -61.21250  20.05520  13.52383  1.000 34.70849  ?  6961 LEU   A CG     1 
ATOM   1264 C  CD1    . LEU   A  1  163 ? -59.78011  20.31194  13.07568  1.000 40.39436  ?  6961 LEU   A CD1    1 
ATOM   1265 C  CD2    . LEU   A  1  163 ? -61.33890  20.15274  15.01079  1.000 34.15257  ?  6961 LEU   A CD2    1 
ATOM   1266 N  N      . GLY   A  1  164 ? -64.59639  23.27857  13.31541  1.000 31.90876  ?  6962 GLY   A N      1 
ATOM   1267 C  CA     . GLY   A  1  164 ? -65.47439  24.28434  12.78244  1.000 28.30001  ?  6962 GLY   A CA     1 
ATOM   1268 C  C      . GLY   A  1  164 ? -66.91481  24.17891  13.24523  1.000 32.95202  ?  6962 GLY   A C      1 
ATOM   1269 O  O      . GLY   A  1  164 ? -67.67274  25.15309  13.09652  1.000 30.31271  ?  6962 GLY   A O      1 
ATOM   1270 N  N      . GLY   A  1  165 ? -67.30945  23.03649  13.81098  1.000 30.82075  ?  6963 GLY   A N      1 
ATOM   1271 C  CA     . GLY   A  1  165 ? -68.66259  22.85449  14.30088  1.000 29.73513  ?  6963 GLY   A CA     1 
ATOM   1272 C  C      . GLY   A  1  165 ? -68.93502  23.65037  15.57150  1.000 31.56973  ?  6963 GLY   A C      1 
ATOM   1273 O  O      . GLY   A  1  165 ? -68.04827  24.24085  16.18720  1.000 28.71607  ?  6963 GLY   A O      1 
ATOM   1274 N  N      . SER   A  1  166 ? -70.20103  23.64351  15.97765  1.000 27.18572  ?  6964 SER   A N      1 
ATOM   1275 C  CA     . SER   A  1  166 ? -70.66218  24.38718  17.14187  1.000 30.69429  ?  6964 SER   A CA     1 
ATOM   1276 C  C      . SER   A  1  166 ? -71.54926  23.51876  18.01889  1.000 27.43777  ?  6964 SER   A C      1 
ATOM   1277 O  O      . SER   A  1  166 ? -72.08042  22.49962  17.57272  1.000 26.75432  ?  6964 SER   A O      1 
ATOM   1278 C  CB     . SER   A  1  166 ? -71.41321  25.65143  16.71142  1.000 27.18025  ?  6964 SER   A CB     1 
ATOM   1279 O  OG     . SER   A  1  166 ? -70.48032  26.50656  16.06167  1.000 33.52800  ?  6964 SER   A OG     1 
ATOM   1280 N  N      . VAL   A  1  167 ? -71.71066  23.93666  19.28453  1.000 28.38518  ?  6965 VAL   A N      1 
ATOM   1281 C  CA     . VAL   A  1  167 ? -72.55467  23.21120  20.23397  1.000 28.33134  ?  6965 VAL   A CA     1 
ATOM   1282 C  C      . VAL   A  1  167 ? -73.39597  24.19552  21.03835  1.000 31.68951  ?  6965 VAL   A C      1 
ATOM   1283 O  O      . VAL   A  1  167 ? -73.01007  25.35233  21.24630  1.000 26.39978  ?  6965 VAL   A O      1 
ATOM   1284 C  CB     . VAL   A  1  167 ? -71.73502  22.31181  21.19824  1.000 27.66093  ?  6965 VAL   A CB     1 
ATOM   1285 C  CG1    . VAL   A  1  167 ? -70.73579  21.40730  20.41742  1.000 25.36714  ?  6965 VAL   A CG1    1 
ATOM   1286 C  CG2    . VAL   A  1  167 ? -71.04560  23.14200  22.28396  1.000 27.91962  ?  6965 VAL   A CG2    1 
ATOM   1287 N  N      . ALA   A  1  168 ? -74.54427  23.71125  21.51522  1.000 25.01797  ?  6966 ALA   A N      1 
ATOM   1288 C  CA     . ALA   A  1  168 ? -75.36886  24.42351  22.49173  1.000 27.84671  ?  6966 ALA   A CA     1 
ATOM   1289 C  C      . ALA   A  1  168 ? -75.88630  23.40363  23.50218  1.000 29.01285  ?  6966 ALA   A C      1 
ATOM   1290 O  O      . ALA   A  1  168 ? -76.69324  22.53494  23.14685  1.000 29.81316  ?  6966 ALA   A O      1 
ATOM   1291 C  CB     . ALA   A  1  168 ? -76.52619  25.15255  21.80332  1.000 24.28674  ?  6966 ALA   A CB     1 
ATOM   1292 N  N      . ILE   A  1  169 ? -75.44016  23.51185  24.75524  1.000 25.57626  ?  6967 ILE   A N      1 
ATOM   1293 C  CA     . ILE   A  1  169 ? -75.66452  22.49514  25.78837  1.000 26.68616  ?  6967 ILE   A CA     1 
ATOM   1294 C  C      . ILE   A  1  169 ? -76.40101  23.14961  26.95359  1.000 28.27498  ?  6967 ILE   A C      1 
ATOM   1295 O  O      . ILE   A  1  169 ? -75.88250  24.09721  27.55717  1.000 25.88202  ?  6967 ILE   A O      1 
ATOM   1296 C  CB     . ILE   A  1  169 ? -74.33684  21.88731  26.27978  1.000 24.78062  ?  6967 ILE   A CB     1 
ATOM   1297 C  CG1    . ILE   A  1  169 ? -73.44839  21.46774  25.08996  1.000 28.90554  ?  6967 ILE   A CG1    1 
ATOM   1298 C  CG2    . ILE   A  1  169 ? -74.58265  20.74354  27.30606  1.000 26.27063  ?  6967 ILE   A CG2    1 
ATOM   1299 C  CD1    . ILE   A  1  169 ? -73.99980  20.29184  24.26514  1.000 29.28496  ?  6967 ILE   A CD1    1 
ATOM   1300 N  N      . LYS   A  1  170 ? -77.59204  22.64047  27.28153  1.000 24.39054  ?  6968 LYS   A N      1 
ATOM   1301 C  CA     . LYS   A  1  170 ? -78.35907  23.20988  28.38277  1.000 28.50767  ?  6968 LYS   A CA     1 
ATOM   1302 C  C      . LYS   A  1  170 ? -77.68816  22.91192  29.71880  1.000 32.58423  ?  6968 LYS   A C      1 
ATOM   1303 O  O      . LYS   A  1  170 ? -77.34729  21.75783  30.01253  1.000 31.21082  ?  6968 LYS   A O      1 
ATOM   1304 C  CB     . LYS   A  1  170 ? -79.79362  22.67261  28.39669  1.000 30.36684  ?  6968 LYS   A CB     1 
ATOM   1305 C  CG     . LYS   A  1  170 ? -80.66735  23.35887  29.47542  1.000 29.15672  ?  6968 LYS   A CG     1 
ATOM   1306 C  CD     . LYS   A  1  170 ? -81.45238  22.37824  30.34710  1.000 32.04048  ?  6968 LYS   A CD     1 
ATOM   1307 C  CE     . LYS   A  1  170 ? -82.83596  22.09463  29.68630  1.000 42.24542  ?  6968 LYS   A CE     1 
ATOM   1308 N  NZ     . LYS   A  1  170 ? -84.05786  22.63391  30.46987  1.000 52.73169  ?  6968 LYS   A NZ     1 
ATOM   1309 N  N      . ILE   A  1  171 ? -77.48592  23.96635  30.51668  1.000 26.09563  ?  6969 ILE   A N      1 
ATOM   1310 C  CA     . ILE   A  1  171 ? -77.05934  23.87346  31.90820  1.000 24.78981  ?  6969 ILE   A CA     1 
ATOM   1311 C  C      . ILE   A  1  171 ? -78.06234  24.63127  32.76772  1.000 28.34587  ?  6969 ILE   A C      1 
ATOM   1312 O  O      . ILE   A  1  171 ? -78.92824  25.34374  32.26337  1.000 26.92974  ?  6969 ILE   A O      1 
ATOM   1313 C  CB     . ILE   A  1  171 ? -75.64117  24.43540  32.12970  1.000 27.65727  ?  6969 ILE   A CB     1 
ATOM   1314 C  CG1    . ILE   A  1  171 ? -75.60600  25.93623  31.78369  1.000 28.67258  ?  6969 ILE   A CG1    1 
ATOM   1315 C  CG2    . ILE   A  1  171 ? -74.63234  23.66314  31.29813  1.000 29.05721  ?  6969 ILE   A CG2    1 
ATOM   1316 C  CD1    . ILE   A  1  171 ? -74.33391  26.66257  32.24054  1.000 28.65246  ?  6969 ILE   A CD1    1 
ATOM   1317 N  N      . THR   A  1  172 ? -77.95168  24.43917  34.08420  1.000 27.39428  ?  6970 THR   A N      1 
ATOM   1318 C  CA     . THR   A  1  172 ? -78.70671  25.19578  35.08198  1.000 30.87802  ?  6970 THR   A CA     1 
ATOM   1319 C  C      . THR   A  1  172 ? -77.76734  25.46910  36.24989  1.000 30.59037  ?  6970 THR   A C      1 
ATOM   1320 O  O      . THR   A  1  172 ? -76.57662  25.12789  36.20747  1.000 26.16989  ?  6970 THR   A O      1 
ATOM   1321 C  CB     . THR   A  1  172 ? -79.94737  24.44338  35.59057  1.000 32.67403  ?  6970 THR   A CB     1 
ATOM   1322 O  OG1    . THR   A  1  172 ? -79.53290  23.34048  36.40984  1.000 31.17967  ?  6970 THR   A OG1    1 
ATOM   1323 C  CG2    . THR   A  1  172 ? -80.79887  23.92503  34.45492  1.000 29.75993  ?  6970 THR   A CG2    1 
ATOM   1324 N  N      . GLU   A  1  173 ? -78.30440  26.05820  37.32024  1.000 28.34004  ?  6971 GLU   A N      1 
ATOM   1325 C  CA     . GLU   A  1  173 ? -77.47999  26.27776  38.50927  1.000 32.17064  ?  6971 GLU   A CA     1 
ATOM   1326 C  C      . GLU   A  1  173 ? -76.83620  24.97483  38.97762  1.000 31.58260  ?  6971 GLU   A C      1 
ATOM   1327 O  O      . GLU   A  1  173 ? -75.62263  24.91430  39.21119  1.000 30.71094  ?  6971 GLU   A O      1 
ATOM   1328 C  CB     . GLU   A  1  173 ? -78.31050  26.89135  39.64165  1.000 34.53304  ?  6971 GLU   A CB     1 
ATOM   1329 C  CG     . GLU   A  1  173 ? -77.50044  27.05450  40.94944  1.000 34.59669  ?  6971 GLU   A CG     1 
ATOM   1330 C  CD     . GLU   A  1  173 ? -78.35078  27.43695  42.15526  1.000 41.26160  ?  6971 GLU   A CD     1 
ATOM   1331 O  OE1    . GLU   A  1  173 ? -79.59289  27.48951  42.01825  1.000 43.73845  ?  6971 GLU   A OE1    1 
ATOM   1332 O  OE2    . GLU   A  1  173 ? -77.77636  27.67041  43.25316  1.000 40.75514  ?  6971 GLU   A OE2    1 
ATOM   1333 N  N      . HIS   A  1  174 ? -77.63113  23.90592  39.07896  1.000 27.93208  ?  6972 HIS   A N      1 
ATOM   1334 C  CA     . HIS   A  1  174 ? -77.13983  22.63363  39.60172  1.000 32.05777  ?  6972 HIS   A CA     1 
ATOM   1335 C  C      . HIS   A  1  174 ? -76.77240  21.60372  38.53228  1.000 37.10851  ?  6972 HIS   A C      1 
ATOM   1336 O  O      . HIS   A  1  174 ? -76.03978  20.65107  38.84145  1.000 32.40709  ?  6972 HIS   A O      1 
ATOM   1337 C  CB     . HIS   A  1  174 ? -78.18325  22.01044  40.53537  1.000 34.87662  ?  6972 HIS   A CB     1 
ATOM   1338 C  CG     . HIS   A  1  174 ? -78.48177  22.84071  41.74314  1.000 41.28196  ?  6972 HIS   A CG     1 
ATOM   1339 N  ND1    . HIS   A  1  174 ? -77.72212  22.78311  42.89387  1.000 43.99110  ?  6972 HIS   A ND1    1 
ATOM   1340 C  CD2    . HIS   A  1  174 ? -79.45699  23.75156  41.97908  1.000 39.33031  ?  6972 HIS   A CD2    1 
ATOM   1341 C  CE1    . HIS   A  1  174 ? -78.21396  23.62966  43.78259  1.000 45.34540  ?  6972 HIS   A CE1    1 
ATOM   1342 N  NE2    . HIS   A  1  174 ? -79.26624  24.22828  43.25259  1.000 41.94933  ?  6972 HIS   A NE2    1 
ATOM   1343 N  N      . SER   A  1  175 ? -77.25944  21.75849  37.29817  1.000 29.19336  ?  6973 SER   A N      1 
ATOM   1344 C  CA     . SER   A  1  175 ? -76.95078  20.84067  36.19666  1.000 30.53190  ?  6973 SER   A CA     1 
ATOM   1345 C  C      . SER   A  1  175 ? -75.85208  21.46669  35.34527  1.000 30.34881  ?  6973 SER   A C      1 
ATOM   1346 O  O      . SER   A  1  175 ? -76.11815  22.23407  34.41789  1.000 26.41213  ?  6973 SER   A O      1 
ATOM   1347 C  CB     . SER   A  1  175 ? -78.19662  20.54220  35.36952  1.000 31.77349  ?  6973 SER   A CB     1 
ATOM   1348 O  OG     . SER   A  1  175 ? -77.89827  19.56605  34.37016  1.000 31.22606  ?  6973 SER   A OG     1 
ATOM   1349 N  N      . TRP   A  1  176 ? -74.60534  21.13603  35.67089  1.000 26.42067  ?  6974 TRP   A N      1 
ATOM   1350 C  CA     . TRP   A  1  176 ? -73.44755  21.72858  35.01771  1.000 28.14451  ?  6974 TRP   A CA     1 
ATOM   1351 C  C      . TRP   A  1  176 ? -72.25673  20.81018  35.23183  1.000 29.37665  ?  6974 TRP   A C      1 
ATOM   1352 O  O      . TRP   A  1  176 ? -72.28983  19.89082  36.05916  1.000 32.22808  ?  6974 TRP   A O      1 
ATOM   1353 C  CB     . TRP   A  1  176 ? -73.13906  23.12340  35.56573  1.000 28.17429  ?  6974 TRP   A CB     1 
ATOM   1354 C  CG     . TRP   A  1  176 ? -72.71755  23.08433  37.00227  1.000 33.15229  ?  6974 TRP   A CG     1 
ATOM   1355 C  CD1    . TRP   A  1  176 ? -73.53096  22.94858  38.09812  1.000 32.05369  ?  6974 TRP   A CD1    1 
ATOM   1356 C  CD2    . TRP   A  1  176 ? -71.38139  23.16248  37.50003  1.000 29.47858  ?  6974 TRP   A CD2    1 
ATOM   1357 N  NE1    . TRP   A  1  176 ? -72.77682  22.94849  39.24092  1.000 35.49340  ?  6974 TRP   A NE1    1 
ATOM   1358 C  CE2    . TRP   A  1  176 ? -71.45355  23.08878  38.90068  1.000 33.85829  ?  6974 TRP   A CE2    1 
ATOM   1359 C  CE3    . TRP   A  1  176 ? -70.12643  23.30211  36.89310  1.000 31.19587  ?  6974 TRP   A CE3    1 
ATOM   1360 C  CZ2    . TRP   A  1  176 ? -70.31818  23.13289  39.70737  1.000 30.68660  ?  6974 TRP   A CZ2    1 
ATOM   1361 C  CZ3    . TRP   A  1  176 ? -69.00337  23.35633  37.69656  1.000 31.08744  ?  6974 TRP   A CZ3    1 
ATOM   1362 C  CH2    . TRP   A  1  176 ? -69.10686  23.26483  39.08589  1.000 34.41380  ?  6974 TRP   A CH2    1 
ATOM   1363 N  N      . ASN   A  1  177 ? -71.19129  21.07937  34.48755  1.000 24.99936  ?  6975 ASN   A N      1 
ATOM   1364 C  CA     . ASN   A  1  177 ? -70.01450  20.22223  34.55117  1.000 28.97005  ?  6975 ASN   A CA     1 
ATOM   1365 C  C      . ASN   A  1  177 ? -68.79734  21.08418  34.26132  1.000 31.38589  ?  6975 ASN   A C      1 
ATOM   1366 O  O      . ASN   A  1  177 ? -68.81795  21.88312  33.31885  1.000 29.10026  ?  6975 ASN   A O      1 
ATOM   1367 C  CB     . ASN   A  1  177 ? -70.12042  19.06392  33.53883  1.000 26.28832  ?  6975 ASN   A CB     1 
ATOM   1368 C  CG     . ASN   A  1  177 ? -68.82325  18.29221  33.39317  1.000 32.67588  ?  6975 ASN   A CG     1 
ATOM   1369 O  OD1    . ASN   A  1  177 ? -67.93959  18.66799  32.62289  1.000 30.58826  ?  6975 ASN   A OD1    1 
ATOM   1370 N  ND2    . ASN   A  1  177 ? -68.70787  17.19799  34.13002  1.000 31.36486  ?  6975 ASN   A ND2    1 
ATOM   1371 N  N      . ALA   A  1  178 ? -67.74143  20.91739  35.06487  1.000 32.24492  ?  6976 ALA   A N      1 
ATOM   1372 C  CA     . ALA   A  1  178 ? -66.57255  21.78931  34.94832  1.000 32.03247  ?  6976 ALA   A CA     1 
ATOM   1373 C  C      . ALA   A  1  178 ? -65.78171  21.51945  33.67580  1.000 32.69161  ?  6976 ALA   A C      1 
ATOM   1374 O  O      . ALA   A  1  178 ? -65.21563  22.44838  33.08798  1.000 34.14224  ?  6976 ALA   A O      1 
ATOM   1375 C  CB     . ALA   A  1  178 ? -65.66070  21.61858  36.16362  1.000 28.35352  ?  6976 ALA   A CB     1 
ATOM   1376 N  N      . ASP   A  1  179 ? -65.66515  20.24836  33.26857  1.000 29.74331  ?  6977 ASP   A N      1 
ATOM   1377 C  CA     . ASP   A  1  179 ? -64.94239  19.93564  32.03377  1.000 33.35682  ?  6977 ASP   A CA     1 
ATOM   1378 C  C      . ASP   A  1  179 ? -65.63891  20.49358  30.80061  1.000 32.32637  ?  6977 ASP   A C      1 
ATOM   1379 O  O      . ASP   A  1  179 ? -64.97433  20.87362  29.82785  1.000 32.12808  ?  6977 ASP   A O      1 
ATOM   1380 C  CB     . ASP   A  1  179 ? -64.76321  18.42800  31.89285  1.000 37.01174  ?  6977 ASP   A CB     1 
ATOM   1381 C  CG     . ASP   A  1  179 ? -63.57662  17.93229  32.66318  1.000 54.22729  ?  6977 ASP   A CG     1 
ATOM   1382 O  OD1    . ASP   A  1  179 ? -62.52454  18.61719  32.59517  1.000 56.92601  ?  6977 ASP   A OD1    1 
ATOM   1383 O  OD2    . ASP   A  1  179 ? -63.70094  16.89681  33.35770  1.000 60.37840  ?  6977 ASP   A OD2    1 
ATOM   1384 N  N      . LEU   A  1  180 ? -66.96867  20.57106  30.81797  1.000 30.25467  ?  6978 LEU   A N      1 
ATOM   1385 C  CA     . LEU   A  1  180 ? -67.66436  21.19418  29.69571  1.000 31.69449  ?  6978 LEU   A CA     1 
ATOM   1386 C  C      . LEU   A  1  180 ? -67.29771  22.67461  29.56663  1.000 28.90040  ?  6978 LEU   A C      1 
ATOM   1387 O  O      . LEU   A  1  180 ? -67.05316  23.16930  28.45574  1.000 30.58805  ?  6978 LEU   A O      1 
ATOM   1388 C  CB     . LEU   A  1  180 ? -69.17555  21.01596  29.85514  1.000 29.94282  ?  6978 LEU   A CB     1 
ATOM   1389 C  CG     . LEU   A  1  180 ? -69.99916  21.66464  28.75088  1.000 30.61429  ?  6978 LEU   A CG     1 
ATOM   1390 C  CD1    . LEU   A  1  180 ? -69.68851  20.98721  27.43388  1.000 29.06704  ?  6978 LEU   A CD1    1 
ATOM   1391 C  CD2    . LEU   A  1  180 ? -71.48666  21.54924  29.08660  1.000 31.06764  ?  6978 LEU   A CD2    1 
ATOM   1392 N  N      . TYR   A  1  181 ? -67.26871  23.40871  30.68413  1.000 28.88196  ?  6979 TYR   A N      1 
ATOM   1393 C  CA     . TYR   A  1  181 ? -66.78193  24.78883  30.62909  1.000 29.26882  ?  6979 TYR   A CA     1 
ATOM   1394 C  C      . TYR   A  1  181 ? -65.34424  24.83279  30.12654  1.000 29.99462  ?  6979 TYR   A C      1 
ATOM   1395 O  O      . TYR   A  1  181 ? -64.98522  25.66432  29.28600  1.000 30.47720  ?  6979 TYR   A O      1 
ATOM   1396 C  CB     . TYR   A  1  181 ? -66.86396  25.43282  32.01082  1.000 28.57956  ?  6979 TYR   A CB     1 
ATOM   1397 C  CG     . TYR   A  1  181 ? -68.20277  26.00336  32.44370  1.000 30.34792  ?  6979 TYR   A CG     1 
ATOM   1398 C  CD1    . TYR   A  1  181 ? -68.63227  27.22683  31.96046  1.000 32.47191  ?  6979 TYR   A CD1    1 
ATOM   1399 C  CD2    . TYR   A  1  181 ? -68.98617  25.36656  33.40225  1.000 28.65758  ?  6979 TYR   A CD2    1 
ATOM   1400 C  CE1    . TYR   A  1  181 ? -69.82706  27.79488  32.37976  1.000 30.20314  ?  6979 TYR   A CE1    1 
ATOM   1401 C  CE2    . TYR   A  1  181 ? -70.19643  25.92877  33.82655  1.000 27.29835  ?  6979 TYR   A CE2    1 
ATOM   1402 C  CZ     . TYR   A  1  181 ? -70.59911  27.15212  33.29842  1.000 31.16504  ?  6979 TYR   A CZ     1 
ATOM   1403 O  OH     . TYR   A  1  181 ? -71.76618  27.76719  33.71168  1.000 32.05369  ?  6979 TYR   A OH     1 
ATOM   1404 N  N      . LYS   A  1  182 ? -64.48932  23.95561  30.65852  1.000 31.87948  ?  6980 LYS   A N      1 
ATOM   1405 C  CA     . LYS   A  1  182 ? -63.12051  23.88857  30.15385  1.000 30.95476  ?  6980 LYS   A CA     1 
ATOM   1406 C  C      . LYS   A  1  182 ? -63.10385  23.67409  28.64239  1.000 32.62210  ?  6980 LYS   A C      1 
ATOM   1407 O  O      . LYS   A  1  182 ? -62.30805  24.28970  27.92543  1.000 30.39257  ?  6980 LYS   A O      1 
ATOM   1408 C  CB     . LYS   A  1  182 ? -62.36570  22.77452  30.87309  1.000 33.83434  ?  6980 LYS   A CB     1 
ATOM   1409 C  CG     . LYS   A  1  182 ? -60.88507  22.69965  30.55543  1.000 40.43608  ?  6980 LYS   A CG     1 
ATOM   1410 C  CD     . LYS   A  1  182 ? -60.27195  21.47613  31.24361  1.000 47.01633  ?  6980 LYS   A CD     1 
ATOM   1411 C  CE     . LYS   A  1  182 ? -58.91036  21.80048  31.81847  1.000 56.65902  ?  6980 LYS   A CE     1 
ATOM   1412 N  NZ     . LYS   A  1  182 ? -57.88985  20.76968  31.44001  1.000 65.04043  ?  6980 LYS   A NZ     1 
ATOM   1413 N  N      . LEU   A  1  183 ? -63.98176  22.80678  28.13601  1.000 30.95144  ?  6981 LEU   A N      1 
ATOM   1414 C  CA     . LEU   A  1  183 ? -64.00588  22.52793  26.70492  1.000 32.32114  ?  6981 LEU   A CA     1 
ATOM   1415 C  C      . LEU   A  1  183 ? -64.46737  23.73561  25.89156  1.000 32.48469  ?  6981 LEU   A C      1 
ATOM   1416 O  O      . LEU   A  1  183 ? -64.13700  23.84975  24.70656  1.000 29.94580  ?  6981 LEU   A O      1 
ATOM   1417 C  CB     . LEU   A  1  183 ? -64.90947  21.32559  26.45897  1.000 33.14328  ?  6981 LEU   A CB     1 
ATOM   1418 C  CG     . LEU   A  1  183 ? -64.81064  20.53314  25.17227  1.000 44.46614  ?  6981 LEU   A CG     1 
ATOM   1419 C  CD1    . LEU   A  1  183 ? -63.35279  20.26966  24.85606  1.000 41.40383  ?  6981 LEU   A CD1    1 
ATOM   1420 C  CD2    . LEU   A  1  183 ? -65.58777  19.22072  25.36693  1.000 36.92581  ?  6981 LEU   A CD2    1 
ATOM   1421 N  N      . MET   A  1  184 ? -65.20298  24.66383  26.50654  1.000 29.19790  ?  6982 MET   A N      1 
ATOM   1422 C  CA     . MET   A  1  184 ? -65.55873  25.89180  25.79931  1.000 28.87119  ?  6982 MET   A CA     1 
ATOM   1423 C  C      . MET   A  1  184 ? -64.31995  26.63449  25.31110  1.000 28.99882  ?  6982 MET   A C      1 
ATOM   1424 O  O      . MET   A  1  184 ? -64.37386  27.34012  24.29555  1.000 28.54534  ?  6982 MET   A O      1 
ATOM   1425 C  CB     . MET   A  1  184 ? -66.40180  26.79731  26.70743  1.000 25.57970  ?  6982 MET   A CB     1 
ATOM   1426 C  CG     . MET   A  1  184 ? -67.83931  26.27014  27.03911  1.000 27.90777  ?  6982 MET   A CG     1 
ATOM   1427 S  SD     . MET   A  1  184 ? -68.81048  26.13952  25.50546  1.000 32.56805  ?  6982 MET   A SD     1 
ATOM   1428 C  CE     . MET   A  1  184 ? -68.78886  24.41226  25.25722  1.000 31.97400  ?  6982 MET   A CE     1 
ATOM   1429 N  N      . GLY   A  1  185 ? -63.20320  26.50979  26.01743  1.000 32.43439  ?  6983 GLY   A N      1 
ATOM   1430 C  CA     . GLY   A  1  185 ? -62.00934  27.17537  25.54383  1.000 31.93892  ?  6983 GLY   A CA     1 
ATOM   1431 C  C      . GLY   A  1  185 ? -61.33978  26.52086  24.35680  1.000 40.16332  ?  6983 GLY   A C      1 
ATOM   1432 O  O      . GLY   A  1  185 ? -60.27560  26.98369  23.93257  1.000 33.85512  ?  6983 GLY   A O      1 
ATOM   1433 N  N      . HIS   A  1  186 ? -61.92610  25.44834  23.81643  1.000 33.79270  ?  6984 HIS   A N      1 
ATOM   1434 C  CA     . HIS   A  1  186 ? -61.45230  24.79188  22.60215  1.000 32.49785  ?  6984 HIS   A CA     1 
ATOM   1435 C  C      . HIS   A  1  186 ? -62.23371  25.23378  21.37823  1.000 34.57142  ?  6984 HIS   A C      1 
ATOM   1436 O  O      . HIS   A  1  186 ? -62.14386  24.59469  20.32477  1.000 35.62773  ?  6984 HIS   A O      1 
ATOM   1437 C  CB     . HIS   A  1  186 ? -61.55100  23.27095  22.72817  1.000 33.66424  ?  6984 HIS   A CB     1 
ATOM   1438 C  CG     . HIS   A  1  186 ? -60.69637  22.68595  23.80932  1.000 41.61739  ?  6984 HIS   A CG     1 
ATOM   1439 N  ND1    . HIS   A  1  186 ? -60.08476  21.45596  23.68184  1.000 44.00537  ?  6984 HIS   A ND1    1 
ATOM   1440 C  CD2    . HIS   A  1  186 ? -60.37941  23.13631  25.04697  1.000 39.51154  ?  6984 HIS   A CD2    1 
ATOM   1441 C  CE1    . HIS   A  1  186 ? -59.41944  21.17727  24.78843  1.000 40.36830  ?  6984 HIS   A CE1    1 
ATOM   1442 N  NE2    . HIS   A  1  186 ? -59.57729  22.18238  25.63141  1.000 43.87432  ?  6984 HIS   A NE2    1 
ATOM   1443 N  N      . PHE   A  1  187 ? -63.03772  26.27594  21.51689  1.000 31.97429  ?  6985 PHE   A N      1 
ATOM   1444 C  CA     . PHE   A  1  187 ? -63.77063  26.88957  20.43303  1.000 31.46890  ?  6985 PHE   A CA     1 
ATOM   1445 C  C      . PHE   A  1  187 ? -63.20166  28.28003  20.19393  1.000 31.79414  ?  6985 PHE   A C      1 
ATOM   1446 O  O      . PHE   A  1  187 ? -62.53797  28.85649  21.05882  1.000 34.85312  ?  6985 PHE   A O      1 
ATOM   1447 C  CB     . PHE   A  1  187 ? -65.26448  26.97334  20.76863  1.000 30.39607  ?  6985 PHE   A CB     1 
ATOM   1448 C  CG     . PHE   A  1  187 ? -65.94216  25.63839  20.85502  1.000 30.35354  ?  6985 PHE   A CG     1 
ATOM   1449 C  CD1    . PHE   A  1  187 ? -65.78404  24.83360  21.97203  1.000 29.26247  ?  6985 PHE   A CD1    1 
ATOM   1450 C  CD2    . PHE   A  1  187 ? -66.74921  25.18884  19.81465  1.000 28.99497  ?  6985 PHE   A CD2    1 
ATOM   1451 C  CE1    . PHE   A  1  187 ? -66.41642  23.60350  22.05761  1.000 28.55203  ?  6985 PHE   A CE1    1 
ATOM   1452 C  CE2    . PHE   A  1  187 ? -67.39347  23.94094  19.89604  1.000 28.94646  ?  6985 PHE   A CE2    1 
ATOM   1453 C  CZ     . PHE   A  1  187 ? -67.21852  23.15944  21.01425  1.000 27.66227  ?  6985 PHE   A CZ     1 
ATOM   1454 N  N      . ALA   A  1  188 ? -63.44440  28.80592  18.99564  1.000 29.54646  ?  6986 ALA   A N      1 
ATOM   1455 C  CA     . ALA   A  1  188 ? -62.99602  30.15969  18.69722  1.000 34.02941  ?  6986 ALA   A CA     1 
ATOM   1456 C  C      . ALA   A  1  188 ? -63.68135  31.18226  19.59179  1.000 36.97238  ?  6986 ALA   A C      1 
ATOM   1457 O  O      . ALA   A  1  188 ? -63.10731  32.23767  19.87550  1.000 32.01607  ?  6986 ALA   A O      1 
ATOM   1458 C  CB     . ALA   A  1  188 ? -63.24837  30.49316  17.23094  1.000 33.41909  ?  6986 ALA   A CB     1 
ATOM   1459 N  N      . TRP   A  1  189 ? -64.88787  30.87916  20.06046  1.000 29.55132  ?  6987 TRP   A N      1 
ATOM   1460 C  CA     . TRP   A  1  189 ? -65.62948  31.77821  20.93439  1.000 31.96592  ?  6987 TRP   A CA     1 
ATOM   1461 C  C      . TRP   A  1  189 ? -66.65227  30.94563  21.69498  1.000 35.56565  ?  6987 TRP   A C      1 
ATOM   1462 O  O      . TRP   A  1  189 ? -66.99040  29.82960  21.28493  1.000 34.05250  ?  6987 TRP   A O      1 
ATOM   1463 C  CB     . TRP   A  1  189 ? -66.30083  32.87970  20.11831  1.000 29.35061  ?  6987 TRP   A CB     1 
ATOM   1464 C  CG     . TRP   A  1  189 ? -66.92605  33.97167  20.91200  1.000 34.80048  ?  6987 TRP   A CG     1 
ATOM   1465 C  CD1    . TRP   A  1  189 ? -66.29734  35.05844  21.45834  1.000 36.18710  ?  6987 TRP   A CD1    1 
ATOM   1466 C  CD2    . TRP   A  1  189 ? -68.31368  34.11219  21.21868  1.000 32.41848  ?  6987 TRP   A CD2    1 
ATOM   1467 N  NE1    . TRP   A  1  189 ? -67.21773  35.86381  22.09789  1.000 39.82516  ?  6987 TRP   A NE1    1 
ATOM   1468 C  CE2    . TRP   A  1  189 ? -68.46119  35.30122  21.96603  1.000 36.62593  ?  6987 TRP   A CE2    1 
ATOM   1469 C  CE3    . TRP   A  1  189 ? -69.44819  33.34505  20.93927  1.000 32.83394  ?  6987 TRP   A CE3    1 
ATOM   1470 C  CZ2    . TRP   A  1  189 ? -69.68788  35.73378  22.43486  1.000 35.37057  ?  6987 TRP   A CZ2    1 
ATOM   1471 C  CZ3    . TRP   A  1  189 ? -70.67284  33.78275  21.40918  1.000 34.19951  ?  6987 TRP   A CZ3    1 
ATOM   1472 C  CH2    . TRP   A  1  189 ? -70.78355  34.96657  22.13913  1.000 36.15247  ?  6987 TRP   A CH2    1 
ATOM   1473 N  N      . TRP   A  1  190 ? -67.13801  31.49008  22.80958  1.000 31.70319  ?  6988 TRP   A N      1 
ATOM   1474 C  CA     . TRP   A  1  190 ? -68.10486  30.76070  23.62834  1.000 31.36763  ?  6988 TRP   A CA     1 
ATOM   1475 C  C      . TRP   A  1  190 ? -68.90907  31.76950  24.43512  1.000 34.01849  ?  6988 TRP   A C      1 
ATOM   1476 O  O      . TRP   A  1  190 ? -68.48118  32.91258  24.62354  1.000 28.39940  ?  6988 TRP   A O      1 
ATOM   1477 C  CB     . TRP   A  1  190 ? -67.40759  29.75947  24.56003  1.000 29.76358  ?  6988 TRP   A CB     1 
ATOM   1478 C  CG     . TRP   A  1  190 ? -66.85347  30.43482  25.80954  1.000 29.96407  ?  6988 TRP   A CG     1 
ATOM   1479 C  CD1    . TRP   A  1  190 ? -65.63625  31.05231  25.94669  1.000 29.81890  ?  6988 TRP   A CD1    1 
ATOM   1480 C  CD2    . TRP   A  1  190 ? -67.51632  30.56290  27.07897  1.000 29.00680  ?  6988 TRP   A CD2    1 
ATOM   1481 N  NE1    . TRP   A  1  190 ? -65.50925  31.56604  27.23588  1.000 35.05884  ?  6988 TRP   A NE1    1 
ATOM   1482 C  CE2    . TRP   A  1  190 ? -66.65212  31.28659  27.93918  1.000 33.40606  ?  6988 TRP   A CE2    1 
ATOM   1483 C  CE3    . TRP   A  1  190 ? -68.76461  30.14558  27.56892  1.000 28.98605  ?  6988 TRP   A CE3    1 
ATOM   1484 C  CZ2    . TRP   A  1  190 ? -66.99093  31.58435  29.25587  1.000 30.58682  ?  6988 TRP   A CZ2    1 
ATOM   1485 C  CZ3    . TRP   A  1  190 ? -69.10002  30.44177  28.87993  1.000 27.27977  ?  6988 TRP   A CZ3    1 
ATOM   1486 C  CH2    . TRP   A  1  190 ? -68.20875  31.15067  29.71277  1.000 30.90431  ?  6988 TRP   A CH2    1 
ATOM   1487 N  N      . THR   A  1  191 ? -70.08610  31.33891  24.89990  1.000 26.53062  ?  6989 THR   A N      1 
ATOM   1488 C  CA     . THR   A  1  191 ? -70.89162  32.15237  25.80617  1.000 29.75999  ?  6989 THR   A CA     1 
ATOM   1489 C  C      . THR   A  1  191 ? -71.88772  31.25117  26.53252  1.000 30.86373  ?  6989 THR   A C      1 
ATOM   1490 O  O      . THR   A  1  191 ? -71.97101  30.04487  26.27547  1.000 27.13949  ?  6989 THR   A O      1 
ATOM   1491 C  CB     . THR   A  1  191 ? -71.60628  33.29963  25.06648  1.000 30.12743  ?  6989 THR   A CB     1 
ATOM   1492 O  OG1    . THR   A  1  191 ? -72.11966  34.22495  26.03613  1.000 29.84931  ?  6989 THR   A OG1    1 
ATOM   1493 C  CG2    . THR   A  1  191 ? -72.79753  32.78022  24.22273  1.000 26.69549  ?  6989 THR   A CG2    1 
ATOM   1494 N  N      . ALA   A  1  192 ? -72.57007  31.83316  27.51932  1.000 28.72613  ?  6990 ALA   A N      1 
ATOM   1495 C  CA     . ALA   A  1  192 ? -73.74022  31.22730  28.14594  1.000 27.29135  ?  6990 ALA   A CA     1 
ATOM   1496 C  C      . ALA   A  1  192 ? -74.90918  32.13441  27.81678  1.000 28.40244  ?  6990 ALA   A C      1 
ATOM   1497 O  O      . ALA   A  1  192 ? -74.86222  33.33692  28.09773  1.000 28.32823  ?  6990 ALA   A O      1 
ATOM   1498 C  CB     . ALA   A  1  192 ? -73.58995  31.06565  29.66038  1.000 25.77332  ?  6990 ALA   A CB     1 
ATOM   1499 N  N      . PHE   A  1  193 ? -75.91377  31.57240  27.15948  1.000 24.89185  ?  6991 PHE   A N      1 
ATOM   1500 C  CA     . PHE   A  1  193 ? -77.01664  32.32851  26.59080  1.000 25.91550  ?  6991 PHE   A CA     1 
ATOM   1501 C  C      . PHE   A  1  193 ? -78.29930  31.98785  27.33037  1.000 27.50106  ?  6991 PHE   A C      1 
ATOM   1502 O  O      . PHE   A  1  193 ? -78.65252  30.80449  27.46395  1.000 24.75754  ?  6991 PHE   A O      1 
ATOM   1503 C  CB     . PHE   A  1  193 ? -77.17182  32.02549  25.09586  1.000 26.48217  ?  6991 PHE   A CB     1 
ATOM   1504 C  CG     . PHE   A  1  193 ? -78.38471  32.64917  24.49938  1.000 29.53264  ?  6991 PHE   A CG     1 
ATOM   1505 C  CD1    . PHE   A  1  193 ? -78.39895  34.01010  24.20318  1.000 26.44243  ?  6991 PHE   A CD1    1 
ATOM   1506 C  CD2    . PHE   A  1  193 ? -79.53430  31.90634  24.30390  1.000 27.30531  ?  6991 PHE   A CD2    1 
ATOM   1507 C  CE1    . PHE   A  1  193 ? -79.53268  34.61019  23.69324  1.000 29.18019  ?  6991 PHE   A CE1    1 
ATOM   1508 C  CE2    . PHE   A  1  193 ? -80.68807  32.50883  23.78145  1.000 28.90857  ?  6991 PHE   A CE2    1 
ATOM   1509 C  CZ     . PHE   A  1  193 ? -80.67678  33.86254  23.46969  1.000 27.40201  ?  6991 PHE   A CZ     1 
ATOM   1510 N  N      . VAL   A  1  194 ? -78.99688  33.01799  27.79342  1.000 24.22391  ?  6992 VAL   A N      1 
ATOM   1511 C  CA     . VAL   A  1  194 ? -80.25878  32.87279  28.51489  1.000 25.41424  ?  6992 VAL   A CA     1 
ATOM   1512 C  C      . VAL   A  1  194 ? -81.38305  33.33728  27.59730  1.000 29.65431  ?  6992 VAL   A C      1 
ATOM   1513 O  O      . VAL   A  1  194 ? -81.36480  34.47741  27.12519  1.000 27.76132  ?  6992 VAL   A O      1 
ATOM   1514 C  CB     . VAL   A  1  194 ? -80.25499  33.68773  29.81800  1.000 26.53317  ?  6992 VAL   A CB     1 
ATOM   1515 C  CG1    . VAL   A  1  194 ? -81.62760  33.61597  30.50365  1.000 24.48147  ?  6992 VAL   A CG1    1 
ATOM   1516 C  CG2    . VAL   A  1  194 ? -79.12788  33.21638  30.74654  1.000 25.21212  ?  6992 VAL   A CG2    1 
ATOM   1517 N  N      . THR   A  1  195 ? -82.38726  32.48569  27.37275  1.000 27.99681  ?  6993 THR   A N      1 
ATOM   1518 C  CA     . THR   A  1  195 ? -83.51224  32.91008  26.54933  1.000 23.49546  ?  6993 THR   A CA     1 
ATOM   1519 C  C      . THR   A  1  195 ? -84.40708  33.87035  27.32424  1.000 24.83373  ?  6993 THR   A C      1 
ATOM   1520 O  O      . THR   A  1  195 ? -84.65075  33.69322  28.51880  1.000 27.14020  ?  6993 THR   A O      1 
ATOM   1521 C  CB     . THR   A  1  195 ? -84.33964  31.71019  26.08258  1.000 30.62630  ?  6993 THR   A CB     1 
ATOM   1522 O  OG1    . THR   A  1  195 ? -84.98985  31.11241  27.20945  1.000 29.58654  ?  6993 THR   A OG1    1 
ATOM   1523 C  CG2    . THR   A  1  195 ? -83.46652  30.65545  25.38210  1.000 24.08355  ?  6993 THR   A CG2    1 
ATOM   1524 N  N      . ASN   A  1  196 ? -84.93042  34.88197  26.62881  1.000 26.00983  ?  6994 ASN   A N      1 
ATOM   1525 C  CA     . ASN   A  1  196 ? -85.79872  35.84239  27.30675  1.000 26.55427  ?  6994 ASN   A CA     1 
ATOM   1526 C  C      . ASN   A  1  196 ? -87.11165  35.21569  27.78195  1.000 29.59256  ?  6994 ASN   A C      1 
ATOM   1527 O  O      . ASN   A  1  196 ? -87.70482  35.71019  28.74177  1.000 30.80832  ?  6994 ASN   A O      1 
ATOM   1528 C  CB     . ASN   A  1  196 ? -86.09666  37.02669  26.39679  1.000 27.23417  ?  6994 ASN   A CB     1 
ATOM   1529 C  CG     . ASN   A  1  196 ? -85.07398  38.13229  26.52707  1.000 31.50796  ?  6994 ASN   A CG     1 
ATOM   1530 O  OD1    . ASN   A  1  196 ? -84.36805  38.22757  27.53018  1.000 31.29207  ?  6994 ASN   A OD1    1 
ATOM   1531 N  ND2    . ASN   A  1  196 ? -85.02494  39.00676  25.53617  1.000 34.54137  ?  6994 ASN   A ND2    1 
ATOM   1532 N  N      . VAL   A  1  197 ? -87.60686  34.15443  27.13543  1.000 30.78527  ?  6995 VAL   A N      1 
ATOM   1533 C  CA     . VAL   A  1  197 ? -88.83996  33.55364  27.65412  1.000 29.57374  ?  6995 VAL   A CA     1 
ATOM   1534 C  C      . VAL   A  1  197 ? -88.60079  32.78209  28.93546  1.000 34.32487  ?  6995 VAL   A C      1 
ATOM   1535 O  O      . VAL   A  1  197 ? -89.54587  32.56971  29.69920  1.000 32.83073  ?  6995 VAL   A O      1 
ATOM   1536 C  CB     . VAL   A  1  197 ? -89.56000  32.59744  26.67522  1.000 32.72385  ?  6995 VAL   A CB     1 
ATOM   1537 C  CG1    . VAL   A  1  197 ? -90.23654  33.36733  25.57156  1.000 33.13339  ?  6995 VAL   A CG1    1 
ATOM   1538 C  CG2    . VAL   A  1  197 ? -88.61219  31.50046  26.12811  1.000 26.46276  ?  6995 VAL   A CG2    1 
ATOM   1539 N  N      . ASN   A  1  198 ? -87.38310  32.32291  29.19532  1.000 29.05586  ?  6996 ASN   A N      1 
ATOM   1540 C  CA     . ASN   A  1  198 ? -87.15027  31.50758  30.38148  1.000 27.57269  ?  6996 ASN   A CA     1 
ATOM   1541 C  C      . ASN   A  1  198 ? -86.16267  32.17560  31.33298  1.000 31.93188  ?  6996 ASN   A C      1 
ATOM   1542 O  O      . ASN   A  1  198 ? -85.51076  31.50767  32.13801  1.000 32.42428  ?  6996 ASN   A O      1 
ATOM   1543 C  CB     . ASN   A  1  198 ? -86.67426  30.10914  29.99386  1.000 29.95209  ?  6996 ASN   A CB     1 
ATOM   1544 C  CG     . ASN   A  1  198 ? -86.90745  29.09102  31.09753  1.000 34.58410  ?  6996 ASN   A CG     1 
ATOM   1545 O  OD1    . ASN   A  1  198 ? -87.80186  29.26445  31.93051  1.000 31.64201  ?  6996 ASN   A OD1    1 
ATOM   1546 N  ND2    . ASN   A  1  198 ? -86.09768  28.02629  31.11722  1.000 31.97813  ?  6996 ASN   A ND2    1 
ATOM   1547 N  N      . ALA   A  1  199 ? -86.07313  33.50857  31.27222  1.000 30.94794  ?  6997 ALA   A N      1 
ATOM   1548 C  CA     . ALA   A  1  199 ? -85.09487  34.26113  32.04851  1.000 30.22695  ?  6997 ALA   A CA     1 
ATOM   1549 C  C      . ALA   A  1  199 ? -85.33243  34.20560  33.55038  1.000 34.11219  ?  6997 ALA   A C      1 
ATOM   1550 O  O      . ALA   A  1  199 ? -84.46330  34.64336  34.31294  1.000 31.03222  ?  6997 ALA   A O      1 
ATOM   1551 C  CB     . ALA   A  1  199 ? -85.10230  35.71674  31.59403  1.000 32.36669  ?  6997 ALA   A CB     1 
ATOM   1552 N  N      . SER   A  1  200 ? -86.48243  33.71411  33.99969  1.000 29.92129  ?  6998 SER   A N      1 
ATOM   1553 C  CA     . SER   A  1  200 ? -86.69975  33.54009  35.42630  1.000 28.70147  ?  6998 SER   A CA     1 
ATOM   1554 C  C      . SER   A  1  200 ? -86.06436  32.26491  35.94643  1.000 34.05843  ?  6998 SER   A C      1 
ATOM   1555 O  O      . SER   A  1  200 ? -86.16452  31.97959  37.14124  1.000 38.94063  ?  6998 SER   A O      1 
ATOM   1556 C  CB     . SER   A  1  200 ? -88.19854  33.51793  35.73378  1.000 39.34761  ?  6998 SER   A CB     1 
ATOM   1557 O  OG     . SER   A  1  200 ? -88.80412  32.48906  34.97632  1.000 40.16267  ?  6998 SER   A OG     1 
ATOM   1558 N  N      . SER   A  1  201 ? -85.40366  31.50592  35.08607  1.000 33.65676  ?  6999 SER   A N      1 
ATOM   1559 C  CA     . SER   A  1  201 ? -84.79077  30.24456  35.45530  1.000 31.87635  ?  6999 SER   A CA     1 
ATOM   1560 C  C      . SER   A  1  201 ? -83.27500  30.37547  35.36934  1.000 31.22832  ?  6999 SER   A C      1 
ATOM   1561 O  O      . SER   A  1  201 ? -82.74957  31.18693  34.59628  1.000 31.85338  ?  6999 SER   A O      1 
ATOM   1562 C  CB     . SER   A  1  201 ? -85.29947  29.13223  34.53148  1.000 31.95392  ?  6999 SER   A CB     1 
ATOM   1563 O  OG     . SER   A  1  201 ? -84.43656  28.01824  34.52208  1.000 32.17587  ?  6999 SER   A OG     1 
ATOM   1564 N  N      . SER   A  1  202 ? -82.56447  29.58963  36.18749  1.000 27.99824  ?  7000 SER   A N      1 
ATOM   1565 C  CA     . SER   A  1  202 ? -81.10967  29.60274  36.09481  1.000 30.22040  ?  7000 SER   A CA     1 
ATOM   1566 C  C      . SER   A  1  202 ? -80.60390  28.85063  34.86462  1.000 31.85826  ?  7000 SER   A C      1 
ATOM   1567 O  O      . SER   A  1  202 ? -79.38933  28.80503  34.61962  1.000 25.81713  ?  7000 SER   A O      1 
ATOM   1568 C  CB     . SER   A  1  202 ? -80.49943  29.02030  37.36788  1.000 34.25317  ?  7000 SER   A CB     1 
ATOM   1569 O  OG     . SER   A  1  202 ? -80.72168  27.62907  37.43198  1.000 30.31587  ?  7000 SER   A OG     1 
ATOM   1570 N  N      . GLU   A  1  203 ? -81.50534  28.27814  34.07387  1.000 27.49719  ?  7001 GLU   A N      1 
ATOM   1571 C  CA     . GLU   A  1  203 ? -81.10645  27.65083  32.82517  1.000 30.13849  ?  7001 GLU   A CA     1 
ATOM   1572 C  C      . GLU   A  1  203 ? -80.29429  28.61062  31.95816  1.000 29.38559  ?  7001 GLU   A C      1 
ATOM   1573 O  O      . GLU   A  1  203 ? -80.50036  29.82407  31.97260  1.000 25.63110  ?  7001 GLU   A O      1 
ATOM   1574 C  CB     . GLU   A  1  203 ? -82.35481  27.20569  32.07863  1.000 29.67149  ?  7001 GLU   A CB     1 
ATOM   1575 C  CG     . GLU   A  1  203 ? -82.12771  26.93615  30.62682  1.000 33.13526  ?  7001 GLU   A CG     1 
ATOM   1576 C  CD     . GLU   A  1  203 ? -83.43821  26.58618  29.94205  1.000 41.31101  ?  7001 GLU   A CD     1 
ATOM   1577 O  OE1    . GLU   A  1  203 ? -83.89521  25.42936  30.11852  1.000 34.95291  ?  7001 GLU   A OE1    1 
ATOM   1578 O  OE2    . GLU   A  1  203 ? -84.01906  27.47292  29.26800  1.000 39.29170  ?  7001 GLU   A OE2    1 
ATOM   1579 N  N      . ALA   A  1  204 ? -79.33141  28.05664  31.23023  1.000 25.11177  ?  7002 ALA   A N      1 
ATOM   1580 C  CA     . ALA   A  1  204 ? -78.65020  28.74688  30.14229  1.000 26.91661  ?  7002 ALA   A CA     1 
ATOM   1581 C  C      . ALA   A  1  204 ? -78.21934  27.68389  29.14359  1.000 26.96532  ?  7002 ALA   A C      1 
ATOM   1582 O  O      . ALA   A  1  204 ? -78.16206  26.49430  29.46862  1.000 26.88902  ?  7002 ALA   A O      1 
ATOM   1583 C  CB     . ALA   A  1  204 ? -77.42715  29.54302  30.63118  1.000 25.01042  ?  7002 ALA   A CB     1 
ATOM   1584 N  N      . PHE   A  1  205 ? -77.93397  28.10934  27.92283  1.000 24.27759  ?  7003 PHE   A N      1 
ATOM   1585 C  CA     . PHE   A  1  205 ? -77.28532  27.24836  26.94588  1.000 26.19406  ?  7003 PHE   A CA     1 
ATOM   1586 C  C      . PHE   A  1  205 ? -75.82890  27.64681  26.86073  1.000 25.39744  ?  7003 PHE   A C      1 
ATOM   1587 O  O      . PHE   A  1  205 ? -75.52042  28.79749  26.53360  1.000 29.37787  ?  7003 PHE   A O      1 
ATOM   1588 C  CB     . PHE   A  1  205 ? -77.96199  27.34961  25.58290  1.000 25.56872  ?  7003 PHE   A CB     1 
ATOM   1589 C  CG     . PHE   A  1  205 ? -79.31195  26.70175  25.55800  1.000 28.85964  ?  7003 PHE   A CG     1 
ATOM   1590 C  CD1    . PHE   A  1  205 ? -80.44573  27.42492  25.90379  1.000 27.24224  ?  7003 PHE   A CD1    1 
ATOM   1591 C  CD2    . PHE   A  1  205 ? -79.43819  25.35550  25.23502  1.000 28.79393  ?  7003 PHE   A CD2    1 
ATOM   1592 C  CE1    . PHE   A  1  205 ? -81.69474  26.82321  25.90175  1.000 35.76809  ?  7003 PHE   A CE1    1 
ATOM   1593 C  CE2    . PHE   A  1  205 ? -80.67851  24.73941  25.22660  1.000 29.72913  ?  7003 PHE   A CE2    1 
ATOM   1594 C  CZ     . PHE   A  1  205 ? -81.80978  25.46192  25.55262  1.000 33.78097  ?  7003 PHE   A CZ     1 
ATOM   1595 N  N      . LEU   A  1  206 ? -74.94118  26.70137  27.16545  1.000 25.79965  ?  7004 LEU   A N      1 
ATOM   1596 C  CA     . LEU   A  1  206 ? -73.50968  26.88047  26.94657  1.000 22.36403  ?  7004 LEU   A CA     1 
ATOM   1597 C  C      . LEU   A  1  206 ? -73.20360  26.66279  25.47379  1.000 27.80081  ?  7004 LEU   A C      1 
ATOM   1598 O  O      . LEU   A  1  206 ? -73.32977  25.54409  24.96773  1.000 28.44257  ?  7004 LEU   A O      1 
ATOM   1599 C  CB     . LEU   A  1  206 ? -72.71964  25.89282  27.79467  1.000 29.10385  ?  7004 LEU   A CB     1 
ATOM   1600 C  CG     . LEU   A  1  206 ? -72.10630  26.31080  29.10872  1.000 41.00441  ?  7004 LEU   A CG     1 
ATOM   1601 C  CD1    . LEU   A  1  206 ? -71.03051  25.27221  29.41911  1.000 32.33695  ?  7004 LEU   A CD1    1 
ATOM   1602 C  CD2    . LEU   A  1  206 ? -71.53291  27.73676  28.99991  1.000 32.54948  ?  7004 LEU   A CD2    1 
ATOM   1603 N  N      . ILE   A  1  207 ? -72.78942  27.72377  24.79017  1.000 27.16922  ?  7005 ILE   A N      1 
ATOM   1604 C  CA     . ILE   A  1  207 ? -72.60763  27.72537  23.34909  1.000 25.79348  ?  7005 ILE   A CA     1 
ATOM   1605 C  C      . ILE   A  1  207 ? -71.11794  27.81609  23.04007  1.000 33.48691  ?  7005 ILE   A C      1 
ATOM   1606 O  O      . ILE   A  1  207 ? -70.42819  28.76194  23.46057  1.000 27.11072  ?  7005 ILE   A O      1 
ATOM   1607 C  CB     . ILE   A  1  207 ? -73.39143  28.86597  22.68827  1.000 30.21788  ?  7005 ILE   A CB     1 
ATOM   1608 C  CG1    . ILE   A  1  207 ? -74.90394  28.64589  22.87890  1.000 26.07070  ?  7005 ILE   A CG1    1 
ATOM   1609 C  CG2    . ILE   A  1  207 ? -73.03669  28.99780  21.22746  1.000 27.43328  ?  7005 ILE   A CG2    1 
ATOM   1610 C  CD1    . ILE   A  1  207 ? -75.71682  29.88069  22.55735  1.000 25.54517  ?  7005 ILE   A CD1    1 
ATOM   1611 N  N      . GLY   A  1  208 ? -70.60954  26.81684  22.33108  1.000 28.57495  ?  7006 GLY   A N      1 
ATOM   1612 C  CA     . GLY   A  1  208 ? -69.25884  26.85590  21.80175  1.000 31.85621  ?  7006 GLY   A CA     1 
ATOM   1613 C  C      . GLY   A  1  208 ? -69.34092  27.04679  20.29919  1.000 31.42437  ?  7006 GLY   A C      1 
ATOM   1614 O  O      . GLY   A  1  208 ? -70.03977  26.29486  19.60966  1.000 32.87084  ?  7006 GLY   A O      1 
ATOM   1615 N  N      . CYS   A  1  209 ? -68.63278  28.06255  19.80456  1.000 31.47356  ?  7007 CYS   A N      1 
ATOM   1616 C  CA     . CYS   A  1  209 ? -68.79609  28.54384  18.43456  1.000 31.00594  ?  7007 CYS   A CA     1 
ATOM   1617 C  C      . CYS   A  1  209 ? -67.50813  28.28825  17.65930  1.000 34.58128  ?  7007 CYS   A C      1 
ATOM   1618 O  O      . CYS   A  1  209 ? -66.47737  28.91598  17.95029  1.000 31.58990  ?  7007 CYS   A O      1 
ATOM   1619 C  CB     . CYS   A  1  209 ? -69.14320  30.03304  18.41596  1.000 30.87702  ?  7007 CYS   A CB     1 
ATOM   1620 S  SG     . CYS   A  1  209 ? -69.60146  30.61790  16.77945  1.000 40.81799  ?  7007 CYS   A SG     1 
ATOM   1621 N  N      . ASN   A  1  210 ? -67.57389  27.36078  16.68139  1.000 33.10021  ?  7008 ASN   A N      1 
ATOM   1622 C  CA     . ASN   A  1  210 ? -66.46711  26.99376  15.79052  1.000 28.71290  ?  7008 ASN   A CA     1 
ATOM   1623 C  C      . ASN   A  1  210 ? -65.36124  26.24413  16.52983  1.000 35.41752  ?  7008 ASN   A C      1 
ATOM   1624 O  O      . ASN   A  1  210 ? -64.41654  26.85508  17.04820  1.000 31.14539  ?  7008 ASN   A O      1 
ATOM   1625 C  CB     . ASN   A  1  210 ? -65.88569  28.23261  15.08972  1.000 31.89633  ?  7008 ASN   A CB     1 
ATOM   1626 C  CG     . ASN   A  1  210 ? -66.94220  29.02494  14.33781  1.000 36.10191  ?  7008 ASN   A CG     1 
ATOM   1627 O  OD1    . ASN   A  1  210 ? -67.09052  30.22775  14.54377  1.000 37.40763  ?  7008 ASN   A OD1    1 
ATOM   1628 N  ND2    . ASN   A  1  210 ? -67.68866  28.34989  13.46104  1.000 34.58081  ?  7008 ASN   A ND2    1 
ATOM   1629 N  N      . TYR   A  1  211 ? -65.45518  24.91352  16.52403  1.000 27.94213  ?  7009 TYR   A N      1 
ATOM   1630 C  CA     . TYR   A  1  211 ? -64.57034  24.04558  17.28770  1.000 30.53655  ?  7009 TYR   A CA     1 
ATOM   1631 C  C      . TYR   A  1  211 ? -63.18046  23.99631  16.66044  1.000 33.98595  ?  7009 TYR   A C      1 
ATOM   1632 O  O      . TYR   A  1  211 ? -63.04857  23.85079  15.44265  1.000 31.95429  ?  7009 TYR   A O      1 
ATOM   1633 C  CB     . TYR   A  1  211 ? -65.19331  22.64805  17.33040  1.000 30.56838  ?  7009 TYR   A CB     1 
ATOM   1634 C  CG     . TYR   A  1  211 ? -64.45140  21.59811  18.11959  1.000 33.71217  ?  7009 TYR   A CG     1 
ATOM   1635 C  CD1    . TYR   A  1  211 ? -64.04974  21.83759  19.42848  1.000 32.01838  ?  7009 TYR   A CD1    1 
ATOM   1636 C  CD2    . TYR   A  1  211 ? -64.19822  20.33982  17.56920  1.000 31.57841  ?  7009 TYR   A CD2    1 
ATOM   1637 C  CE1    . TYR   A  1  211 ? -63.38716  20.86826  20.16713  1.000 34.82240  ?  7009 TYR   A CE1    1 
ATOM   1638 C  CE2    . TYR   A  1  211 ? -63.53700  19.35761  18.30437  1.000 34.56708  ?  7009 TYR   A CE2    1 
ATOM   1639 C  CZ     . TYR   A  1  211 ? -63.13460  19.63526  19.59839  1.000 31.52487  ?  7009 TYR   A CZ     1 
ATOM   1640 O  OH     . TYR   A  1  211 ? -62.48692  18.68467  20.33912  1.000 38.03992  ?  7009 TYR   A OH     1 
ATOM   1641 N  N      . LEU   A  1  212 ? -62.14119  24.10236  17.49419  1.000 32.43371  ?  7010 LEU   A N      1 
ATOM   1642 C  CA     . LEU   A  1  212 ? -60.76010  24.10432  17.02901  1.000 30.25239  ?  7010 LEU   A CA     1 
ATOM   1643 C  C      . LEU   A  1  212 ? -60.01226  22.83445  17.38243  1.000 34.31697  ?  7010 LEU   A C      1 
ATOM   1644 O  O      . LEU   A  1  212 ? -58.91285  22.62554  16.86371  1.000 39.21943  ?  7010 LEU   A O      1 
ATOM   1645 C  CB     . LEU   A  1  212 ? -59.97616  25.30010  17.60389  1.000 32.83335  ?  7010 LEU   A CB     1 
ATOM   1646 C  CG     . LEU   A  1  212 ? -60.57866  26.69400  17.38708  1.000 36.86521  ?  7010 LEU   A CG     1 
ATOM   1647 C  CD1    . LEU   A  1  212 ? -59.71541  27.77038  18.04235  1.000 35.56734  ?  7010 LEU   A CD1    1 
ATOM   1648 C  CD2    . LEU   A  1  212 ? -60.76534  26.99787  15.91281  1.000 35.39294  ?  7010 LEU   A CD2    1 
ATOM   1649 N  N      . GLY   A  1  213 ? -60.55826  21.99746  18.25773  1.000 35.68394  ?  7011 GLY   A N      1 
ATOM   1650 C  CA     . GLY   A  1  213 ? -59.93982  20.72074  18.55976  1.000 40.54065  ?  7011 GLY   A CA     1 
ATOM   1651 C  C      . GLY   A  1  213 ? -58.76226  20.77832  19.50472  1.000 45.53880  ?  7011 GLY   A C      1 
ATOM   1652 O  O      . GLY   A  1  213 ? -58.14788  19.73474  19.76809  1.000 47.99455  ?  7011 GLY   A O      1 
ATOM   1653 N  N      . LYS   A  1  214 ? -58.41347  21.95312  20.00926  1.000 38.76378  ?  7012 LYS   A N      1 
ATOM   1654 C  CA     . LYS   A  1  214 ? -57.35529  22.09750  20.99589  1.000 44.76176  ?  7012 LYS   A CA     1 
ATOM   1655 C  C      . LYS   A  1  214 ? -57.59914  23.38728  21.75694  1.000 43.29167  ?  7012 LYS   A C      1 
ATOM   1656 O  O      . LYS   A  1  214 ? -58.34726  24.25676  21.29024  1.000 40.92821  ?  7012 LYS   A O      1 
ATOM   1657 C  CB     . LYS   A  1  214 ? -55.96500  22.10502  20.34831  1.000 38.90187  ?  7012 LYS   A CB     1 
ATOM   1658 C  CG     . LYS   A  1  214 ? -55.78887  23.10856  19.21957  1.000 47.55590  ?  7012 LYS   A CG     1 
ATOM   1659 C  CD     . LYS   A  1  214 ? -54.37954  23.00766  18.60893  1.000 57.43321  ?  7012 LYS   A CD     1 
ATOM   1660 C  CE     . LYS   A  1  214 ? -54.11133  24.18534  17.68052  1.000 65.87778  ?  7012 LYS   A CE     1 
ATOM   1661 N  NZ     . LYS   A  1  214 ? -54.77962  25.41960  18.19735  1.000 64.94012  ?  7012 LYS   A NZ     1 
ATOM   1662 N  N      . PRO   A  1  215 ? -57.00255  23.53810  22.93853  1.000 47.35980  ?  7013 PRO   A N      1 
ATOM   1663 C  CA     . PRO   A  1  215 ? -57.30034  24.71639  23.76649  1.000 43.44923  ?  7013 PRO   A CA     1 
ATOM   1664 C  C      . PRO   A  1  215 ? -56.78170  25.98221  23.10500  1.000 44.28571  ?  7013 PRO   A C      1 
ATOM   1665 O  O      . PRO   A  1  215 ? -55.59392  26.10576  22.80981  1.000 50.74444  ?  7013 PRO   A O      1 
ATOM   1666 C  CB     . PRO   A  1  215 ? -56.57788  24.42221  25.08661  1.000 44.43545  ?  7013 PRO   A CB     1 
ATOM   1667 C  CG     . PRO   A  1  215 ? -55.53789  23.41225  24.73944  1.000 50.93131  ?  7013 PRO   A CG     1 
ATOM   1668 C  CD     . PRO   A  1  215 ? -56.09065  22.59547  23.61036  1.000 43.18098  ?  7013 PRO   A CD     1 
ATOM   1669 N  N      . ARG   A  1  216 ? -57.69486  26.90072  22.82642  1.000 37.14397  ?  7014 ARG   A N      1 
ATOM   1670 C  CA     . ARG   A  1  216 ? -57.31440  28.27149  22.53042  1.000 39.66567  ?  7014 ARG   A CA     1 
ATOM   1671 C  C      . ARG   A  1  216 ? -57.08867  29.06148  23.80436  1.000 45.40594  ?  7014 ARG   A C      1 
ATOM   1672 O  O      . ARG   A  1  216 ? -56.33887  30.04391  23.79715  1.000 46.33085  ?  7014 ARG   A O      1 
ATOM   1673 C  CB     . ARG   A  1  216 ? -58.40929  28.93992  21.69792  1.000 41.60278  ?  7014 ARG   A CB     1 
ATOM   1674 C  CG     . ARG   A  1  216 ? -58.08344  30.33070  21.23652  1.000 45.91210  ?  7014 ARG   A CG     1 
ATOM   1675 C  CD     . ARG   A  1  216 ? -59.32034  30.99474  20.67224  1.000 44.33201  ?  7014 ARG   A CD     1 
ATOM   1676 N  NE     . ARG   A  1  216 ? -60.37644  31.01883  21.67348  1.000 47.68300  ?  7014 ARG   A NE     1 
ATOM   1677 C  CZ     . ARG   A  1  216 ? -60.54135  31.99458  22.55641  1.000 53.87590  ?  7014 ARG   A CZ     1 
ATOM   1678 N  NH1    . ARG   A  1  216 ? -59.75505  33.06071  22.55689  1.000 44.21133  ?  7014 ARG   A NH1    1 
ATOM   1679 N  NH2    . ARG   A  1  216 ? -61.51127  31.89101  23.46854  1.000 43.23036  ?  7014 ARG   A NH2    1 
ATOM   1680 N  N      . GLU   A  1  217 ? -57.71781  28.63725  24.89753  1.000 46.07252  ?  7015 GLU   A N      1 
ATOM   1681 C  CA     . GLU   A  1  217 ? -57.66969  29.35073  26.15999  1.000 40.87605  ?  7015 GLU   A CA     1 
ATOM   1682 C  C      . GLU   A  1  217 ? -57.91437  28.35596  27.28323  1.000 43.89249  ?  7015 GLU   A C      1 
ATOM   1683 O  O      . GLU   A  1  217 ? -58.68626  27.40249  27.12561  1.000 41.63875  ?  7015 GLU   A O      1 
ATOM   1684 C  CB     . GLU   A  1  217 ? -58.70616  30.47742  26.15909  1.000 43.68989  ?  7015 GLU   A CB     1 
ATOM   1685 C  CG     . GLU   A  1  217 ? -59.43954  30.64618  27.43924  1.000 54.90348  ?  7015 GLU   A CG     1 
ATOM   1686 C  CD     . GLU   A  1  217 ? -60.47909  31.75946  27.34700  1.000 62.08973  ?  7015 GLU   A CD     1 
ATOM   1687 O  OE1    . GLU   A  1  217 ? -61.00467  32.01478  26.22820  1.000 62.35806  ?  7015 GLU   A OE1    1 
ATOM   1688 O  OE2    . GLU   A  1  217 ? -60.74466  32.38784  28.39659  1.000 58.64895  ?  7015 GLU   A OE2    1 
ATOM   1689 N  N      . GLN   A  1  218 ? -57.22352  28.55436  28.39705  1.000 39.11503  ?  7016 GLN   A N      1 
ATOM   1690 C  CA     . GLN   A  1  218 ? -57.37017  27.69177  29.55829  1.000 40.55948  ?  7016 GLN   A CA     1 
ATOM   1691 C  C      . GLN   A  1  218 ? -58.48634  28.23844  30.43248  1.000 44.06953  ?  7016 GLN   A C      1 
ATOM   1692 O  O      . GLN   A  1  218 ? -58.44114  29.40188  30.83798  1.000 47.09834  ?  7016 GLN   A O      1 
ATOM   1693 C  CB     . GLN   A  1  218 ? -56.06036  27.60500  30.33891  1.000 47.12215  ?  7016 GLN   A CB     1 
ATOM   1694 C  CG     . GLN   A  1  218 ? -54.95692  26.86508  29.58567  1.000 52.90245  ?  7016 GLN   A CG     1 
ATOM   1695 C  CD     . GLN   A  1  218 ? -55.30277  25.40441  29.37744  1.000 57.77463  ?  7016 GLN   A CD     1 
ATOM   1696 O  OE1    . GLN   A  1  218 ? -55.90948  24.77355  30.24936  1.000 64.07086  ?  7016 GLN   A OE1    1 
ATOM   1697 N  NE2    . GLN   A  1  218 ? -54.93402  24.85926  28.21893  1.000 60.10031  ?  7016 GLN   A NE2    1 
ATOM   1698 N  N      . ILE   A  1  219 ? -59.49542  27.41280  30.69587  1.000 38.40946  ?  7017 ILE   A N      1 
ATOM   1699 C  CA     . ILE   A  1  219 ? -60.65893  27.80626  31.47856  1.000 36.23659  ?  7017 ILE   A CA     1 
ATOM   1700 C  C      . ILE   A  1  219 ? -60.77634  26.85031  32.65122  1.000 34.72111  ?  7017 ILE   A C      1 
ATOM   1701 O  O      . ILE   A  1  219 ? -60.78985  25.63021  32.45832  1.000 39.90193  ?  7017 ILE   A O      1 
ATOM   1702 C  CB     . ILE   A  1  219 ? -61.95070  27.79183  30.63125  1.000 38.85684  ?  7017 ILE   A CB     1 
ATOM   1703 C  CG1    . ILE   A  1  219 ? -61.93923  28.93857  29.62439  1.000 37.88980  ?  7017 ILE   A CG1    1 
ATOM   1704 C  CG2    . ILE   A  1  219 ? -63.19891  27.86742  31.52775  1.000 35.37326  ?  7017 ILE   A CG2    1 
ATOM   1705 C  CD1    . ILE   A  1  219 ? -63.16902  29.00127  28.74050  1.000 37.50638  ?  7017 ILE   A CD1    1 
ATOM   1706 N  N      . ASP   A  1  220 ? -60.85172  27.40305  33.86141  1.000 31.30854  ?  7018 ASP   A N      1 
ATOM   1707 C  CA     . ASP   A  1  220 ? -61.20096  26.64224  35.05855  1.000 37.15631  ?  7018 ASP   A CA     1 
ATOM   1708 C  C      . ASP   A  1  220 ? -62.72251  26.60329  35.14829  1.000 37.43904  ?  7018 ASP   A C      1 
ATOM   1709 O  O      . ASP   A  1  220 ? -63.36511  27.64108  35.33877  1.000 37.46935  ?  7018 ASP   A O      1 
ATOM   1710 C  CB     . ASP   A  1  220 ? -60.56777  27.28050  36.29753  1.000 33.42460  ?  7018 ASP   A CB     1 
ATOM   1711 C  CG     . ASP   A  1  220 ? -60.93983  26.57393  37.60843  1.000 43.75000  ?  7018 ASP   A CG     1 
ATOM   1712 O  OD1    . ASP   A  1  220 ? -62.09431  26.11976  37.77565  1.000 39.70903  ?  7018 ASP   A OD1    1 
ATOM   1713 O  OD2    . ASP   A  1  220 ? -60.06229  26.49654  38.49917  1.000 47.27688  ?  7018 ASP   A OD2    1 
ATOM   1714 N  N      . GLY   A  1  221 ? -63.30042  25.40623  35.02128  1.000 33.44674  ?  7019 GLY   A N      1 
ATOM   1715 C  CA     . GLY   A  1  221 ? -64.74658  25.30182  34.91408  1.000 36.68557  ?  7019 GLY   A CA     1 
ATOM   1716 C  C      . GLY   A  1  221 ? -65.48683  25.53159  36.21573  1.000 36.13774  ?  7019 GLY   A C      1 
ATOM   1717 O  O      . GLY   A  1  221 ? -66.64112  25.97583  36.20177  1.000 34.87894  ?  7019 GLY   A O      1 
ATOM   1718 N  N      . TYR   A  1  222 ? -64.86502  25.20597  37.35726  1.000 34.52619  ?  7020 TYR   A N      1 
ATOM   1719 C  CA     . TYR   A  1  222 ? -65.50403  25.51788  38.63867  1.000 36.21780  ?  7020 TYR   A CA     1 
ATOM   1720 C  C      . TYR   A  1  222 ? -65.61640  27.02665  38.81964  1.000 34.94973  ?  7020 TYR   A C      1 
ATOM   1721 O  O      . TYR   A  1  222 ? -66.65712  27.53899  39.24332  1.000 35.52235  ?  7020 TYR   A O      1 
ATOM   1722 C  CB     . TYR   A  1  222 ? -64.72202  24.89478  39.79764  1.000 36.28131  ?  7020 TYR   A CB     1 
ATOM   1723 C  CG     . TYR   A  1  222 ? -64.55668  23.40009  39.68122  1.000 37.92280  ?  7020 TYR   A CG     1 
ATOM   1724 C  CD1    . TYR   A  1  222 ? -63.49805  22.85776  38.95165  1.000 38.92337  ?  7020 TYR   A CD1    1 
ATOM   1725 C  CD2    . TYR   A  1  222 ? -65.45467  22.53058  40.29167  1.000 41.67965  ?  7020 TYR   A CD2    1 
ATOM   1726 C  CE1    . TYR   A  1  222 ? -63.33950  21.47802  38.82651  1.000 42.97345  ?  7020 TYR   A CE1    1 
ATOM   1727 C  CE2    . TYR   A  1  222 ? -65.30507  21.13883  40.17144  1.000 38.52750  ?  7020 TYR   A CE2    1 
ATOM   1728 C  CZ     . TYR   A  1  222 ? -64.24211  20.63144  39.43635  1.000 41.77524  ?  7020 TYR   A CZ     1 
ATOM   1729 O  OH     . TYR   A  1  222 ? -64.06606  19.27561  39.29539  1.000 54.09129  ?  7020 TYR   A OH     1 
ATOM   1730 N  N      . VAL   A  1  223 ? -64.55910  27.75423  38.47577  1.000 30.94484  ?  7021 VAL   A N      1 
ATOM   1731 C  CA     . VAL   A  1  223 ? -64.60804  29.20891  38.54774  1.000 36.45904  ?  7021 VAL   A CA     1 
ATOM   1732 C  C      . VAL   A  1  223 ? -65.59443  29.76877  37.52997  1.000 35.34936  ?  7021 VAL   A C      1 
ATOM   1733 O  O      . VAL   A  1  223 ? -66.34848  30.70294  37.83008  1.000 32.24979  ?  7021 VAL   A O      1 
ATOM   1734 C  CB     . VAL   A  1  223 ? -63.20855  29.80969  38.34919  1.000 36.62666  ?  7021 VAL   A CB     1 
ATOM   1735 C  CG1    . VAL   A  1  223 ? -63.30740  31.32120  38.31342  1.000 34.58646  ?  7021 VAL   A CG1    1 
ATOM   1736 C  CG2    . VAL   A  1  223 ? -62.26405  29.35178  39.48134  1.000 35.51083  ?  7021 VAL   A CG2    1 
ATOM   1737 N  N      . MET   A  1  224 ? -65.60518  29.22751  36.30768  1.000 31.72121  ?  7022 MET   A N      1 
ATOM   1738 C  CA     . MET   A  1  224 ? -66.45969  29.84859  35.30534  1.000 32.03969  ?  7022 MET   A CA     1 
ATOM   1739 C  C      . MET   A  1  224 ? -67.93843  29.66750  35.64342  1.000 30.25194  ?  7022 MET   A C      1 
ATOM   1740 O  O      . MET   A  1  224 ? -68.75522  30.55730  35.36929  1.000 30.54157  ?  7022 MET   A O      1 
ATOM   1741 C  CB     . MET   A  1  224 ? -66.13794  29.30892  33.91147  1.000 32.35641  ?  7022 MET   A CB     1 
ATOM   1742 C  CG     . MET   A  1  224 ? -66.75735  30.14814  32.80135  1.000 28.77386  ?  7022 MET   A CG     1 
ATOM   1743 S  SD     . MET   A  1  224 ? -66.13674  31.85619  32.67599  1.000 32.07351  ?  7022 MET   A SD     1 
ATOM   1744 C  CE     . MET   A  1  224 ? -64.53524  31.58000  31.86532  1.000 31.55159  ?  7022 MET   A CE     1 
ATOM   1745 N  N      . HIS   A  1  225 ? -68.31717  28.54416  36.24658  1.000 28.08922  ?  7023 HIS   A N      1 
ATOM   1746 C  CA     . HIS   A  1  225 ? -69.71917  28.40158  36.63805  1.000 29.84909  ?  7023 HIS   A CA     1 
ATOM   1747 C  C      . HIS   A  1  225 ? -70.05954  29.36608  37.76660  1.000 34.08358  ?  7023 HIS   A C      1 
ATOM   1748 O  O      . HIS   A  1  225 ? -71.17503  29.89979  37.82249  1.000 31.30342  ?  7023 HIS   A O      1 
ATOM   1749 C  CB     . HIS   A  1  225 ? -70.03418  26.96879  37.06450  1.000 27.95115  ?  7023 HIS   A CB     1 
ATOM   1750 C  CG     . HIS   A  1  225 ? -71.50253  26.69861  37.23310  1.000 28.98496  ?  7023 HIS   A CG     1 
ATOM   1751 N  ND1    . HIS   A  1  225 ? -72.40695  26.82839  36.20074  1.000 29.77175  ?  7023 HIS   A ND1    1 
ATOM   1752 C  CD2    . HIS   A  1  225 ? -72.22060  26.29396  38.31104  1.000 30.26137  ?  7023 HIS   A CD2    1 
ATOM   1753 C  CE1    . HIS   A  1  225 ? -73.61950  26.51335  36.63252  1.000 29.38984  ?  7023 HIS   A CE1    1 
ATOM   1754 N  NE2    . HIS   A  1  225 ? -73.53447  26.19342  37.91210  1.000 32.92812  ?  7023 HIS   A NE2    1 
ATOM   1755 N  N      . ALA   A  1  226 ? -69.11043  29.59145  38.68451  1.000 28.70259  ?  7024 ALA   A N      1 
ATOM   1756 C  CA     . ALA   A  1  226 ? -69.29980  30.61859  39.70019  1.000 30.50698  ?  7024 ALA   A CA     1 
ATOM   1757 C  C      . ALA   A  1  226 ? -69.47101  31.98047  39.04939  1.000 30.53204  ?  7024 ALA   A C      1 
ATOM   1758 O  O      . ALA   A  1  226 ? -70.30516  32.78907  39.48608  1.000 31.47249  ?  7024 ALA   A O      1 
ATOM   1759 C  CB     . ALA   A  1  226 ? -68.11317  30.62359  40.67281  1.000 32.30738  ?  7024 ALA   A CB     1 
ATOM   1760 N  N      . ASN   A  1  227 ? -68.68597  32.25300  38.00054  1.000 26.76766  ?  7025 ASN   A N      1 
ATOM   1761 C  CA     . ASN   A  1  227 ? -68.83549  33.50890  37.26985  1.000 27.53112  ?  7025 ASN   A CA     1 
ATOM   1762 C  C      . ASN   A  1  227 ? -70.21230  33.60816  36.63146  1.000 31.70394  ?  7025 ASN   A C      1 
ATOM   1763 O  O      . ASN   A  1  227 ? -70.82318  34.68551  36.61344  1.000 27.16821  ?  7025 ASN   A O      1 
ATOM   1764 C  CB     . ASN   A  1  227 ? -67.77355  33.62725  36.18048  1.000 27.80730  ?  7025 ASN   A CB     1 
ATOM   1765 C  CG     . ASN   A  1  227 ? -66.38182  33.85409  36.72998  1.000 34.82535  ?  7025 ASN   A CG     1 
ATOM   1766 O  OD1    . ASN   A  1  227 ? -66.19518  34.20177  37.90160  1.000 32.91025  ?  7025 ASN   A OD1    1 
ATOM   1767 N  ND2    . ASN   A  1  227 ? -65.39074  33.66029  35.87451  1.000 28.93426  ?  7025 ASN   A ND2    1 
ATOM   1768 N  N      . TYR   A  1  228 ? -70.69742  32.49861  36.06131  1.000 29.16291  ?  7026 TYR   A N      1 
ATOM   1769 C  CA     . TYR   A  1  228 ? -72.01133  32.49449  35.42943  1.000 26.79628  ?  7026 TYR   A CA     1 
ATOM   1770 C  C      . TYR   A  1  228 ? -73.09592  32.81025  36.45426  1.000 26.98188  ?  7026 TYR   A C      1 
ATOM   1771 O  O      . TYR   A  1  228 ? -73.97911  33.64528  36.21569  1.000 28.92853  ?  7026 TYR   A O      1 
ATOM   1772 C  CB     . TYR   A  1  228 ? -72.27238  31.13159  34.74394  1.000 25.94287  ?  7026 TYR   A CB     1 
ATOM   1773 C  CG     . TYR   A  1  228 ? -73.73779  30.94482  34.39593  1.000 22.22306  ?  7026 TYR   A CG     1 
ATOM   1774 C  CD1    . TYR   A  1  228 ? -74.31995  31.67021  33.36523  1.000 24.83367  ?  7026 TYR   A CD1    1 
ATOM   1775 C  CD2    . TYR   A  1  228 ? -74.54179  30.08835  35.12574  1.000 28.17038  ?  7026 TYR   A CD2    1 
ATOM   1776 C  CE1    . TYR   A  1  228 ? -75.68708  31.52422  33.05115  1.000 25.75003  ?  7026 TYR   A CE1    1 
ATOM   1777 C  CE2    . TYR   A  1  228 ? -75.90736  29.93939  34.82060  1.000 26.71939  ?  7026 TYR   A CE2    1 
ATOM   1778 C  CZ     . TYR   A  1  228 ? -76.46370  30.67166  33.78823  1.000 25.86148  ?  7026 TYR   A CZ     1 
ATOM   1779 O  OH     . TYR   A  1  228 ? -77.81159  30.54034  33.50349  1.000 28.42918  ?  7026 TYR   A OH     1 
ATOM   1780 N  N      . ILE   A  1  229 ? -73.04852  32.14105  37.60348  1.000 26.87545  ?  7027 ILE   A N      1 
ATOM   1781 C  CA     . ILE   A  1  229 ? -74.04163  32.37364  38.65004  1.000 30.06444  ?  7027 ILE   A CA     1 
ATOM   1782 C  C      . ILE   A  1  229 ? -73.94528  33.80296  39.17989  1.000 30.62219  ?  7027 ILE   A C      1 
ATOM   1783 O  O      . ILE   A  1  229 ? -74.96308  34.45749  39.43715  1.000 28.87919  ?  7027 ILE   A O      1 
ATOM   1784 C  CB     . ILE   A  1  229 ? -73.88138  31.35001  39.78670  1.000 32.67864  ?  7027 ILE   A CB     1 
ATOM   1785 C  CG1    . ILE   A  1  229 ? -74.22825  29.92769  39.29723  1.000 29.61986  ?  7027 ILE   A CG1    1 
ATOM   1786 C  CG2    . ILE   A  1  229 ? -74.76531  31.74242  40.97185  1.000 30.52802  ?  7027 ILE   A CG2    1 
ATOM   1787 C  CD1    . ILE   A  1  229 ? -75.60958  29.79896  38.65397  1.000 31.41720  ?  7027 ILE   A CD1    1 
ATOM   1788 N  N      . PHE   A  1  230 ? -72.72867  34.30940  39.35469  1.000 29.62402  ?  7028 PHE   A N      1 
ATOM   1789 C  CA     . PHE   A  1  230 ? -72.57184  35.71169  39.73071  1.000 30.48406  ?  7028 PHE   A CA     1 
ATOM   1790 C  C      . PHE   A  1  230 ? -73.28178  36.63554  38.74698  1.000 30.04750  ?  7028 PHE   A C      1 
ATOM   1791 O  O      . PHE   A  1  230 ? -74.04077  37.52607  39.15252  1.000 31.57919  ?  7028 PHE   A O      1 
ATOM   1792 C  CB     . PHE   A  1  230 ? -71.09333  36.08012  39.80777  1.000 28.93423  ?  7028 PHE   A CB     1 
ATOM   1793 C  CG     . PHE   A  1  230 ? -70.85902  37.52422  40.20112  1.000 37.53389  ?  7028 PHE   A CG     1 
ATOM   1794 C  CD1    . PHE   A  1  230 ? -70.31894  38.41386  39.30033  1.000 37.23395  ?  7028 PHE   A CD1    1 
ATOM   1795 C  CD2    . PHE   A  1  230 ? -71.20134  37.98092  41.47118  1.000 36.45842  ?  7028 PHE   A CD2    1 
ATOM   1796 C  CE1    . PHE   A  1  230 ? -70.09529  39.75430  39.66357  1.000 45.19951  ?  7028 PHE   A CE1    1 
ATOM   1797 C  CE2    . PHE   A  1  230 ? -70.99116  39.30092  41.83737  1.000 36.29386  ?  7028 PHE   A CE2    1 
ATOM   1798 C  CZ     . PHE   A  1  230 ? -70.44400  40.18739  40.93563  1.000 33.36162  ?  7028 PHE   A CZ     1 
ATOM   1799 N  N      . TRP   A  1  231 ? -73.01928  36.46133  37.44543  1.000 30.13486  ?  7029 TRP   A N      1 
ATOM   1800 C  CA     . TRP   A  1  231 ? -73.71595  37.24919  36.43167  1.000 30.45504  ?  7029 TRP   A CA     1 
ATOM   1801 C  C      . TRP   A  1  231 ? -75.22609  37.15335  36.61633  1.000 28.67687  ?  7029 TRP   A C      1 
ATOM   1802 O  O      . TRP   A  1  231 ? -75.91674  38.17205  36.70720  1.000 28.10264  ?  7029 TRP   A O      1 
ATOM   1803 C  CB     . TRP   A  1  231 ? -73.31564  36.78720  35.02329  1.000 28.78593  ?  7029 TRP   A CB     1 
ATOM   1804 C  CG     . TRP   A  1  231 ? -74.20249  37.36603  33.94283  1.000 28.88294  ?  7029 TRP   A CG     1 
ATOM   1805 C  CD1    . TRP   A  1  231 ? -74.49843  38.69168  33.74009  1.000 30.18244  ?  7029 TRP   A CD1    1 
ATOM   1806 C  CD2    . TRP   A  1  231 ? -74.90403  36.64230  32.92114  1.000 28.12923  ?  7029 TRP   A CD2    1 
ATOM   1807 N  NE1    . TRP   A  1  231 ? -75.33163  38.82955  32.65950  1.000 29.79657  ?  7029 TRP   A NE1    1 
ATOM   1808 C  CE2    . TRP   A  1  231 ? -75.61348  37.58738  32.15093  1.000 29.33038  ?  7029 TRP   A CE2    1 
ATOM   1809 C  CE3    . TRP   A  1  231 ? -75.00920  35.28527  32.59121  1.000 28.12799  ?  7029 TRP   A CE3    1 
ATOM   1810 C  CZ2    . TRP   A  1  231 ? -76.40249  37.22114  31.06247  1.000 26.51686  ?  7029 TRP   A CZ2    1 
ATOM   1811 C  CZ3    . TRP   A  1  231 ? -75.79451  34.92212  31.51065  1.000 25.74059  ?  7029 TRP   A CZ3    1 
ATOM   1812 C  CH2    . TRP   A  1  231 ? -76.49096  35.88318  30.76705  1.000 27.58453  ?  7029 TRP   A CH2    1 
ATOM   1813 N  N      . ARG   A  1  232 ? -75.75692  35.92828  36.68455  1.000 29.40678  ?  7030 ARG   A N      1 
ATOM   1814 C  CA     . ARG   A  1  232 ? -77.20004  35.76012  36.84131  1.000 30.74407  ?  7030 ARG   A CA     1 
ATOM   1815 C  C      . ARG   A  1  232 ? -77.70412  36.42169  38.12227  1.000 32.11464  ?  7030 ARG   A C      1 
ATOM   1816 O  O      . ARG   A  1  232 ? -78.78086  37.02588  38.12888  1.000 33.39814  ?  7030 ARG   A O      1 
ATOM   1817 C  CB     . ARG   A  1  232 ? -77.56397  34.26900  36.82578  1.000 29.57468  ?  7030 ARG   A CB     1 
ATOM   1818 C  CG     . ARG   A  1  232 ? -77.25930  33.53193  35.47103  1.000 23.52245  ?  7030 ARG   A CG     1 
ATOM   1819 C  CD     . ARG   A  1  232 ? -77.89627  34.20014  34.25944  1.000 28.49495  ?  7030 ARG   A CD     1 
ATOM   1820 N  NE     . ARG   A  1  232 ? -79.31080  34.50898  34.44015  1.000 26.08594  ?  7030 ARG   A NE     1 
ATOM   1821 C  CZ     . ARG   A  1  232 ? -80.29861  33.62675  34.34644  1.000 30.91780  ?  7030 ARG   A CZ     1 
ATOM   1822 N  NH1    . ARG   A  1  232 ? -80.07059  32.35558  34.06385  1.000 25.74951  ?  7030 ARG   A NH1    1 
ATOM   1823 N  NH2    . ARG   A  1  232 ? -81.54848  34.03059  34.53805  1.000 29.43867  ?  7030 ARG   A NH2    1 
ATOM   1824 N  N      . ASN   A  1  233 ? -76.94187  36.31058  39.22067  1.000 31.55589  ?  7031 ASN   A N      1 
ATOM   1825 C  CA     . ASN   A  1  233 ? -77.38690  36.84769  40.50734  1.000 30.67731  ?  7031 ASN   A CA     1 
ATOM   1826 C  C      . ASN   A  1  233 ? -77.48296  38.36684  40.49501  1.000 35.21451  ?  7031 ASN   A C      1 
ATOM   1827 O  O      . ASN   A  1  233 ? -78.31664  38.93034  41.21099  1.000 36.33613  ?  7031 ASN   A O      1 
ATOM   1828 C  CB     . ASN   A  1  233 ? -76.44838  36.40627  41.63173  1.000 30.88091  ?  7031 ASN   A CB     1 
ATOM   1829 C  CG     . ASN   A  1  233 ? -76.85730  35.10222  42.24068  1.000 38.15583  ?  7031 ASN   A CG     1 
ATOM   1830 O  OD1    . ASN   A  1  233 ? -78.00822  34.67555  42.10123  1.000 37.50131  ?  7031 ASN   A OD1    1 
ATOM   1831 N  ND2    . ASN   A  1  233 ? -75.92756  34.45257  42.93072  1.000 33.68946  ?  7031 ASN   A ND2    1 
ATOM   1832 N  N      . THR   A  1  234 ? -76.66192  39.04739  39.69078  1.000 31.06490  ?  7032 THR   A N      1 
ATOM   1833 C  CA     . THR   A  1  234 ? -76.58324  40.50126  39.72790  1.000 31.53460  ?  7032 THR   A CA     1 
ATOM   1834 C  C      . THR   A  1  234 ? -77.20341  41.18661  38.52122  1.000 35.41669  ?  7032 THR   A C      1 
ATOM   1835 O  O      . THR   A  1  234 ? -77.16136  42.41872  38.44379  1.000 38.53594  ?  7032 THR   A O      1 
ATOM   1836 C  CB     . THR   A  1  234 ? -75.11908  40.94978  39.86609  1.000 31.36921  ?  7032 THR   A CB     1 
ATOM   1837 O  OG1    . THR   A  1  234 ? -74.35385  40.46651  38.75004  1.000 31.76389  ?  7032 THR   A OG1    1 
ATOM   1838 C  CG2    . THR   A  1  234 ? -74.53812  40.39645  41.13191  1.000 26.98464  ?  7032 THR   A CG2    1 
ATOM   1839 N  N      . ASN   A  1  235 ? -77.76510  40.44203  37.57068  1.000 33.68491  ?  7033 ASN   A N      1 
ATOM   1840 C  CA     . ASN   A  1  235 ? -78.33166  41.01698  36.35099  1.000 32.16984  ?  7033 ASN   A CA     1 
ATOM   1841 C  C      . ASN   A  1  235 ? -79.69451  40.40471  36.09310  1.000 34.57264  ?  7033 ASN   A C      1 
ATOM   1842 O  O      . ASN   A  1  235 ? -79.82227  39.46774  35.29466  1.000 31.69593  ?  7033 ASN   A O      1 
ATOM   1843 C  CB     . ASN   A  1  235 ? -77.43259  40.79009  35.14269  1.000 32.38826  ?  7033 ASN   A CB     1 
ATOM   1844 C  CG     . ASN   A  1  235 ? -76.19790  41.60352  35.20073  1.000 38.82236  ?  7033 ASN   A CG     1 
ATOM   1845 O  OD1    . ASN   A  1  235 ? -76.12735  42.68079  34.61930  1.000 40.21636  ?  7033 ASN   A OD1    1 
ATOM   1846 N  ND2    . ASN   A  1  235 ? -75.20264  41.10629  35.92604  1.000 34.89482  ?  7033 ASN   A ND2    1 
ATOM   1847 N  N      . PRO   A  1  236 ? -80.73506  40.91705  36.73788  1.000 37.37445  ?  7034 PRO   A N      1 
ATOM   1848 C  CA     . PRO   A  1  236 ? -82.08959  40.44714  36.42744  1.000 36.50553  ?  7034 PRO   A CA     1 
ATOM   1849 C  C      . PRO   A  1  236 ? -82.36894  40.62363  34.94662  1.000 36.82459  ?  7034 PRO   A C      1 
ATOM   1850 O  O      . PRO   A  1  236 ? -82.02236  41.63779  34.34495  1.000 33.10211  ?  7034 PRO   A O      1 
ATOM   1851 C  CB     . PRO   A  1  236 ? -82.99015  41.35215  37.27818  1.000 41.32564  ?  7034 PRO   A CB     1 
ATOM   1852 C  CG     . PRO   A  1  236 ? -82.08988  41.94621  38.31980  1.000 41.96364  ?  7034 PRO   A CG     1 
ATOM   1853 C  CD     . PRO   A  1  236 ? -80.73209  42.04915  37.67965  1.000 38.05931  ?  7034 PRO   A CD     1 
ATOM   1854 N  N      . ILE   A  1  237 ? -82.98114  39.61671  34.34614  1.000 35.18261  ?  7035 ILE   A N      1 
ATOM   1855 C  CA     . ILE   A  1  237 ? -83.33771  39.66384  32.93981  1.000 33.62689  ?  7035 ILE   A CA     1 
ATOM   1856 C  C      . ILE   A  1  237 ? -84.85251  39.72530  32.87938  1.000 38.16987  ?  7035 ILE   A C      1 
ATOM   1857 O  O      . ILE   A  1  237 ? -85.53612  38.89141  33.48573  1.000 34.79763  ?  7035 ILE   A O      1 
ATOM   1858 C  CB     . ILE   A  1  237 ? -82.77782  38.45774  32.17586  1.000 32.81369  ?  7035 ILE   A CB     1 
ATOM   1859 C  CG1    . ILE   A  1  237 ? -81.25090  38.51517  32.18300  1.000 31.63622  ?  7035 ILE   A CG1    1 
ATOM   1860 C  CG2    . ILE   A  1  237 ? -83.30208  38.44377  30.75260  1.000 30.29866  ?  7035 ILE   A CG2    1 
ATOM   1861 C  CD1    . ILE   A  1  237 ? -80.60395  37.18670  31.89417  1.000 28.24817  ?  7035 ILE   A CD1    1 
ATOM   1862 N  N      . GLN   A  1  238 ? -85.37503  40.74227  32.20328  1.000 32.53932  ?  7036 GLN   A N      1 
ATOM   1863 C  CA     . GLN   A  1  238 ? -86.81651  40.92135  32.09524  1.000 36.25557  ?  7036 GLN   A CA     1 
ATOM   1864 C  C      . GLN   A  1  238 ? -87.38991  39.83801  31.19394  1.000 32.46198  ?  7036 GLN   A C      1 
ATOM   1865 O  O      . GLN   A  1  238 ? -86.94742  39.68819  30.05078  1.000 34.20345  ?  7036 GLN   A O      1 
ATOM   1866 C  CB     . GLN   A  1  238 ? -87.11891  42.30801  31.52836  1.000 40.62731  ?  7036 GLN   A CB     1 
ATOM   1867 C  CG     . GLN   A  1  238 ? -88.57706  42.55050  31.15719  1.000 44.71528  ?  7036 GLN   A CG     1 
ATOM   1868 C  CD     . GLN   A  1  238 ? -88.78771  43.90978  30.49033  1.000 55.84116  ?  7036 GLN   A CD     1 
ATOM   1869 O  OE1    . GLN   A  1  238 ? -87.96266  44.81820  30.63334  1.000 59.53577  ?  7036 GLN   A OE1    1 
ATOM   1870 N  NE2    . GLN   A  1  238 ? -89.88362  44.04468  29.73854  1.000 58.18060  ?  7036 GLN   A NE2    1 
ATOM   1871 N  N      . LEU   A  1  239 ? -88.35385  39.07394  31.70478  1.000 33.85373  ?  7037 LEU   A N      1 
ATOM   1872 C  CA     . LEU   A  1  239 ? -89.02119  38.07847  30.88149  1.000 33.01726  ?  7037 LEU   A CA     1 
ATOM   1873 C  C      . LEU   A  1  239 ? -89.58005  38.73622  29.63420  1.000 36.98121  ?  7037 LEU   A C      1 
ATOM   1874 O  O      . LEU   A  1  239 ? -90.17589  39.81426  29.69715  1.000 34.32853  ?  7037 LEU   A O      1 
ATOM   1875 C  CB     . LEU   A  1  239 ? -90.15678  37.40825  31.65540  1.000 39.45703  ?  7037 LEU   A CB     1 
ATOM   1876 C  CG     . LEU   A  1  239 ? -89.80030  36.31296  32.64791  1.000 40.56296  ?  7037 LEU   A CG     1 
ATOM   1877 C  CD1    . LEU   A  1  239 ? -89.44041  35.02882  31.92753  1.000 36.98840  ?  7037 LEU   A CD1    1 
ATOM   1878 C  CD2    . LEU   A  1  239 ? -88.65958  36.78038  33.49964  1.000 44.80607  ?  7037 LEU   A CD2    1 
ATOM   1879 N  N      . SER   A  1  240 ? -89.41462  38.07726  28.49458  1.000 34.71978  ?  7038 SER   A N      1 
ATOM   1880 C  CA     . SER   A  1  240 ? -89.91952  38.68727  27.27837  1.000 32.82630  ?  7038 SER   A CA     1 
ATOM   1881 C  C      . SER   A  1  240 ? -90.15898  37.63611  26.20556  1.000 32.87145  ?  7038 SER   A C      1 
ATOM   1882 O  O      . SER   A  1  240 ? -89.33184  36.73925  25.99866  1.000 35.86930  ?  7038 SER   A O      1 
ATOM   1883 C  CB     . SER   A  1  240 ? -88.95214  39.75139  26.75674  1.000 30.14360  ?  7038 SER   A CB     1 
ATOM   1884 O  OG     . SER   A  1  240 ? -89.48176  40.28092  25.55171  1.000 35.27752  ?  7038 SER   A OG     1 
ATOM   1885 N  N      . SER   A  1  241 ? -91.28510  37.77049  25.50874  1.000 30.29303  ?  7039 SER   A N      1 
ATOM   1886 C  CA     . SER   A  1  241 ? -91.58909  36.95495  24.34371  1.000 31.92030  ?  7039 SER   A CA     1 
ATOM   1887 C  C      . SER   A  1  241 ? -91.59162  37.76931  23.05715  1.000 33.57524  ?  7039 SER   A C      1 
ATOM   1888 O  O      . SER   A  1  241 ? -92.00707  37.25028  22.01263  1.000 30.93491  ?  7039 SER   A O      1 
ATOM   1889 C  CB     . SER   A  1  241 ? -92.93976  36.25689  24.53433  1.000 34.17482  ?  7039 SER   A CB     1 
ATOM   1890 O  OG     . SER   A  1  241 ? -93.95521  37.23972  24.62099  1.000 45.77150  ?  7039 SER   A OG     1 
ATOM   1891 N  N      A TYR   A  1  242 ? -91.09688  39.01483  23.10795  0.628 29.81512  ?  7040 TYR   A N      1 
ATOM   1892 N  N      B TYR   A  1  242 ? -91.12787  39.02596  23.09510  0.372 30.00556  ?  7040 TYR   A N      1 
ATOM   1893 C  CA     A TYR   A  1  242 ? -91.18540  39.93126  21.97352  0.628 31.51156  ?  7040 TYR   A CA     1 
ATOM   1894 C  CA     B TYR   A  1  242 ? -91.22325  39.88664  21.91717  0.372 31.97578  ?  7040 TYR   A CA     1 
ATOM   1895 C  C      A TYR   A  1  242 ? -90.58433  39.34676  20.69325  0.628 30.08413  ?  7040 TYR   A C      1 
ATOM   1896 C  C      B TYR   A  1  242 ? -90.63421  39.22699  20.67844  0.372 30.25714  ?  7040 TYR   A C      1 
ATOM   1897 O  O      A TYR   A  1  242 ? -91.16548  39.48485  19.61410  0.628 29.96608  ?  7040 TYR   A O      1 
ATOM   1898 O  O      B TYR   A  1  242 ? -91.26239  39.20525  19.61646  0.372 30.31760  ?  7040 TYR   A O      1 
ATOM   1899 C  CB     A TYR   A  1  242 ? -90.50013  41.25878  22.32107  0.628 32.92567  ?  7040 TYR   A CB     1 
ATOM   1900 C  CB     B TYR   A  1  242 ? -90.52213  41.22608  22.14938  0.372 32.88338  ?  7040 TYR   A CB     1 
ATOM   1901 C  CG     A TYR   A  1  242 ? -91.19496  42.09731  23.38853  0.628 34.38264  ?  7040 TYR   A CG     1 
ATOM   1902 C  CG     B TYR   A  1  242 ? -90.21035  41.92832  20.84276  0.372 33.04358  ?  7040 TYR   A CG     1 
ATOM   1903 C  CD1    A TYR   A  1  242 ? -92.42115  41.71305  23.93424  0.628 32.97825  ?  7040 TYR   A CD1    1 
ATOM   1904 C  CD1    B TYR   A  1  242 ? -91.17126  42.70098  20.19995  0.372 36.11314  ?  7040 TYR   A CD1    1 
ATOM   1905 C  CD2    A TYR   A  1  242 ? -90.62167  43.29162  23.83776  0.628 35.34690  ?  7040 TYR   A CD2    1 
ATOM   1906 C  CD2    B TYR   A  1  242 ? -88.96237  41.79822  20.23668  0.372 33.59634  ?  7040 TYR   A CD2    1 
ATOM   1907 C  CE1    A TYR   A  1  242 ? -93.04661  42.49489  24.90952  0.628 33.13049  ?  7040 TYR   A CE1    1 
ATOM   1908 C  CE1    B TYR   A  1  242 ? -90.88732  43.34435  18.99575  0.372 35.75179  ?  7040 TYR   A CE1    1 
ATOM   1909 C  CE2    A TYR   A  1  242 ? -91.23692  44.06947  24.80023  0.628 32.62621  ?  7040 TYR   A CE2    1 
ATOM   1910 C  CE2    B TYR   A  1  242 ? -88.67392  42.42257  19.03877  0.372 31.76881  ?  7040 TYR   A CE2    1 
ATOM   1911 C  CZ     A TYR   A  1  242 ? -92.44731  43.66726  25.33096  0.628 31.69386  ?  7040 TYR   A CZ     1 
ATOM   1912 C  CZ     B TYR   A  1  242 ? -89.64011  43.19728  18.42415  0.372 35.67288  ?  7040 TYR   A CZ     1 
ATOM   1913 O  OH     A TYR   A  1  242 ? -93.05679  44.43948  26.28638  0.628 35.69188  ?  7040 TYR   A OH     1 
ATOM   1914 O  OH     B TYR   A  1  242 ? -89.35721  43.82239  17.23707  0.372 32.49035  ?  7040 TYR   A OH     1 
ATOM   1915 N  N      . SER   A  1  243 ? -89.40700  38.71971  20.77587  1.000 29.50636  ?  7041 SER   A N      1 
ATOM   1916 C  CA     . SER   A  1  243 ? -88.75965  38.25367  19.55478  1.000 26.23354  ?  7041 SER   A CA     1 
ATOM   1917 C  C      . SER   A  1  243 ? -89.53420  37.13249  18.86879  1.000 29.63960  ?  7041 SER   A C      1 
ATOM   1918 O  O      . SER   A  1  243 ? -89.25206  36.82639  17.70593  1.000 28.39766  ?  7041 SER   A O      1 
ATOM   1919 C  CB     . SER   A  1  243 ? -87.32926  37.77668  19.82608  1.000 27.99093  ?  7041 SER   A CB     1 
ATOM   1920 O  OG     . SER   A  1  243 ? -87.33567  36.49495  20.44116  1.000 31.14879  ?  7041 SER   A OG     1 
ATOM   1921 N  N      . LEU   A  1  244 ? -90.47568  36.49366  19.56113  1.000 29.21688  ?  7042 LEU   A N      1 
ATOM   1922 C  CA     . LEU   A  1  244 ? -91.22089  35.39853  18.94814  1.000 32.99477  ?  7042 LEU   A CA     1 
ATOM   1923 C  C      . LEU   A  1  244 ? -92.18300  35.88043  17.86928  1.000 36.76433  ?  7042 LEU   A C      1 
ATOM   1924 O  O      . LEU   A  1  244 ? -92.62330  35.07256  17.04062  1.000 33.49709  ?  7042 LEU   A O      1 
ATOM   1925 C  CB     . LEU   A  1  244 ? -92.00329  34.63061  20.01050  1.000 27.22386  ?  7042 LEU   A CB     1 
ATOM   1926 C  CG     . LEU   A  1  244 ? -91.23049  34.07938  21.20963  1.000 29.27748  ?  7042 LEU   A CG     1 
ATOM   1927 C  CD1    . LEU   A  1  244 ? -92.22123  33.44009  22.18362  1.000 31.51564  ?  7042 LEU   A CD1    1 
ATOM   1928 C  CD2    . LEU   A  1  244 ? -90.17921  33.04784  20.74635  1.000 28.56993  ?  7042 LEU   A CD2    1 
ATOM   1929 N  N      . PHE   A  1  245 ? -92.52301  37.16413  17.85951  1.000 31.65057  ?  7043 PHE   A N      1 
ATOM   1930 C  CA     . PHE   A  1  245 ? -93.47991  37.67695  16.89626  1.000 32.87022  ?  7043 PHE   A CA     1 
ATOM   1931 C  C      . PHE   A  1  245 ? -92.84131  38.16226  15.60775  1.000 37.19519  ?  7043 PHE   A C      1 
ATOM   1932 O  O      . PHE   A  1  245 ? -93.55018  38.71638  14.76708  1.000 47.98631  ?  7043 PHE   A O      1 
ATOM   1933 C  CB     . PHE   A  1  245 ? -94.27406  38.82006  17.50524  1.000 31.85673  ?  7043 PHE   A CB     1 
ATOM   1934 C  CG     . PHE   A  1  245 ? -95.20499  38.39258  18.59684  1.000 34.54778  ?  7043 PHE   A CG     1 
ATOM   1935 C  CD1    . PHE   A  1  245 ? -94.75393  38.26057  19.89045  1.000 29.08413  ?  7043 PHE   A CD1    1 
ATOM   1936 C  CD2    . PHE   A  1  245 ? -96.54510  38.14927  18.32183  1.000 35.00169  ?  7043 PHE   A CD2    1 
ATOM   1937 C  CE1    . PHE   A  1  245 ? -95.60714  37.88660  20.89919  1.000 34.87415  ?  7043 PHE   A CE1    1 
ATOM   1938 C  CE2    . PHE   A  1  245 ? -97.41036  37.77661  19.32027  1.000 35.11038  ?  7043 PHE   A CE2    1 
ATOM   1939 C  CZ     . PHE   A  1  245 ? -96.94642  37.63884  20.61431  1.000 36.00500  ?  7043 PHE   A CZ     1 
ATOM   1940 N  N      . ASP   A  1  246 ? -91.53196  37.99712  15.42875  1.000 37.36293  ?  7044 ASP   A N      1 
ATOM   1941 C  CA     . ASP   A  1  246 ? -90.88162  38.40140  14.18462  1.000 36.51264  ?  7044 ASP   A CA     1 
ATOM   1942 C  C      . ASP   A  1  246 ? -89.99574  37.27460  13.68114  1.000 36.34957  ?  7044 ASP   A C      1 
ATOM   1943 O  O      . ASP   A  1  246 ? -88.82906  37.16083  14.07302  1.000 35.45652  ?  7044 ASP   A O      1 
ATOM   1944 C  CB     . ASP   A  1  246 ? -90.07143  39.67624  14.33647  1.000 40.86690  ?  7044 ASP   A CB     1 
ATOM   1945 C  CG     . ASP   A  1  246 ? -89.43132  40.09791  13.00878  1.000 48.12143  ?  7044 ASP   A CG     1 
ATOM   1946 O  OD1    . ASP   A  1  246 ? -89.83470  39.54629  11.93655  1.000 40.77599  ?  7044 ASP   A OD1    1 
ATOM   1947 O  OD2    . ASP   A  1  246 ? -88.52657  40.95996  13.04900  1.000 59.60658  ?  7044 ASP   A OD2    1 
ATOM   1948 N  N      . MET   A  1  247 ? -90.54389  36.49956  12.75379  1.000 35.95575  ?  7045 MET   A N      1 
ATOM   1949 C  CA     . MET   A  1  247 ? -89.92064  35.28821  12.25574  1.000 36.09347  ?  7045 MET   A CA     1 
ATOM   1950 C  C      . MET   A  1  247 ? -89.42154  35.43235  10.82699  1.000 32.58896  ?  7045 MET   A C      1 
ATOM   1951 O  O      . MET   A  1  247 ? -88.99939  34.43938  10.22411  1.000 30.97693  ?  7045 MET   A O      1 
ATOM   1952 C  CB     . MET   A  1  247 ? -90.91854  34.13546  12.38383  1.000 32.85404  ?  7045 MET   A CB     1 
ATOM   1953 C  CG     . MET   A  1  247 ? -91.20800  33.78031  13.85679  1.000 35.07567  ?  7045 MET   A CG     1 
ATOM   1954 S  SD     . MET   A  1  247 ? -89.81887  32.97752  14.67982  1.000 36.18250  ?  7045 MET   A SD     1 
ATOM   1955 C  CE     . MET   A  1  247 ? -89.77276  31.40299  13.78285  1.000 29.27931  ?  7045 MET   A CE     1 
ATOM   1956 N  N      . SER   A  1  248 ? -89.42301  36.65325  10.27558  1.000 35.16363  ?  7046 SER   A N      1 
ATOM   1957 C  CA     . SER   A  1  248 ? -89.10911  36.80433  8.85652   1.000 34.25376  ?  7046 SER   A CA     1 
ATOM   1958 C  C      . SER   A  1  248 ? -87.66365  36.44964  8.55253   1.000 32.12028  ?  7046 SER   A C      1 
ATOM   1959 O  O      . SER   A  1  248 ? -87.36559  35.97573  7.44948   1.000 37.39166  ?  7046 SER   A O      1 
ATOM   1960 C  CB     . SER   A  1  248 ? -89.41907  38.22889  8.37594   1.000 35.97758  ?  7046 SER   A CB     1 
ATOM   1961 O  OG     . SER   A  1  248 ? -88.73258  39.18193  9.15925   1.000 41.69892  ?  7046 SER   A OG     1 
ATOM   1962 N  N      . LYS   A  1  249 ? -86.75275  36.66179  9.49650   1.000 32.08160  ?  7047 LYS   A N      1 
ATOM   1963 C  CA     . LYS   A  1  249 ? -85.34743  36.33035  9.28806   1.000 35.93783  ?  7047 LYS   A CA     1 
ATOM   1964 C  C      . LYS   A  1  249 ? -84.93707  35.05976  10.02509  1.000 32.68262  ?  7047 LYS   A C      1 
ATOM   1965 O  O      . LYS   A  1  249 ? -83.74469  34.83390  10.24219  1.000 35.11791  ?  7047 LYS   A O      1 
ATOM   1966 C  CB     . LYS   A  1  249 ? -84.45174  37.48893  9.72560   1.000 38.39238  ?  7047 LYS   A CB     1 
ATOM   1967 C  CG     . LYS   A  1  249 ? -84.91049  38.83691  9.22230   1.000 45.29352  ?  7047 LYS   A CG     1 
ATOM   1968 C  CD     . LYS   A  1  249 ? -84.36937  39.13724  7.83830   1.000 52.19738  ?  7047 LYS   A CD     1 
ATOM   1969 C  CE     . LYS   A  1  249 ? -84.63683  40.60654  7.46440   1.000 59.66463  ?  7047 LYS   A CE     1 
ATOM   1970 N  NZ     . LYS   A  1  249 ? -86.10549  40.92038  7.43405   1.000 63.15685  ?  7047 LYS   A NZ     1 
ATOM   1971 N  N      . PHE   A  1  250 ? -85.89916  34.20807  10.38657  1.000 34.45548  ?  7048 PHE   A N      1 
ATOM   1972 C  CA     . PHE   A  1  250 ? -85.57647  33.05764  11.23309  1.000 31.07810  ?  7048 PHE   A CA     1 
ATOM   1973 C  C      . PHE   A  1  250 ? -84.69255  32.01856  10.55678  1.000 29.41081  ?  7048 PHE   A C      1 
ATOM   1974 O  O      . PHE   A  1  250 ? -83.74551  31.53887  11.20293  1.000 32.99209  ?  7048 PHE   A O      1 
ATOM   1975 C  CB     . PHE   A  1  250 ? -86.86273  32.40446  11.74384  1.000 32.30504  ?  7048 PHE   A CB     1 
ATOM   1976 C  CG     . PHE   A  1  250 ? -86.60993  31.27102  12.70163  1.000 27.00854  ?  7048 PHE   A CG     1 
ATOM   1977 C  CD1    . PHE   A  1  250 ? -86.06759  31.51853  13.95424  1.000 29.08471  ?  7048 PHE   A CD1    1 
ATOM   1978 C  CD2    . PHE   A  1  250 ? -86.91318  29.97316  12.34688  1.000 29.40800  ?  7048 PHE   A CD2    1 
ATOM   1979 C  CE1    . PHE   A  1  250 ? -85.82785  30.47490  14.85540  1.000 28.30924  ?  7048 PHE   A CE1    1 
ATOM   1980 C  CE2    . PHE   A  1  250 ? -86.68947  28.91994  13.22682  1.000 28.06440  ?  7048 PHE   A CE2    1 
ATOM   1981 C  CZ     . PHE   A  1  250 ? -86.14159  29.16591  14.48272  1.000 27.52133  ?  7048 PHE   A CZ     1 
ATOM   1982 N  N      . PRO   A  1  251 ? -84.94143  31.59808  9.31248   1.000 32.16499  ?  7049 PRO   A N      1 
ATOM   1983 C  CA     . PRO   A  1  251 ? -84.20991  30.44159  8.76814   1.000 34.66522  ?  7049 PRO   A CA     1 
ATOM   1984 C  C      . PRO   A  1  251 ? -82.70084  30.61751  8.83321   1.000 37.88807  ?  7049 PRO   A C      1 
ATOM   1985 O  O      . PRO   A  1  251 ? -82.16369  31.68955  8.55506   1.000 36.19529  ?  7049 PRO   A O      1 
ATOM   1986 C  CB     . PRO   A  1  251 ? -84.69461  30.36432  7.31546   1.000 34.14898  ?  7049 PRO   A CB     1 
ATOM   1987 C  CG     . PRO   A  1  251 ? -86.04024  31.02274  7.34599   1.000 34.93604  ?  7049 PRO   A CG     1 
ATOM   1988 C  CD     . PRO   A  1  251 ? -85.94413  32.10873  8.36055   1.000 33.08049  ?  7049 PRO   A CD     1 
ATOM   1989 N  N      . LEU   A  1  252 ? -82.01446  29.54568  9.20951   1.000 33.02789  ?  7050 LEU   A N      1 
ATOM   1990 C  CA     . LEU   A  1  252 ? -80.56165  29.56245  9.18695   1.000 35.24327  ?  7050 LEU   A CA     1 
ATOM   1991 C  C      . LEU   A  1  252 ? -80.07516  29.72503  7.74876   1.000 39.46388  ?  7050 LEU   A C      1 
ATOM   1992 O  O      . LEU   A  1  252 ? -80.47942  28.98157  6.84970   1.000 37.15807  ?  7050 LEU   A O      1 
ATOM   1993 C  CB     . LEU   A  1  252 ? -80.00992  28.27177  9.79458   1.000 28.56227  ?  7050 LEU   A CB     1 
ATOM   1994 C  CG     . LEU   A  1  252 ? -78.48066  28.17898  9.76237   1.000 30.43710  ?  7050 LEU   A CG     1 
ATOM   1995 C  CD1    . LEU   A  1  252 ? -77.81591  29.33556  10.49513  1.000 33.50218  ?  7050 LEU   A CD1    1 
ATOM   1996 C  CD2    . LEU   A  1  252 ? -78.00309  26.84980  10.35461  1.000 28.75765  ?  7050 LEU   A CD2    1 
ATOM   1997 N  N      . LYS   A  1  253 ? -79.19621  30.69219  7.53974   1.000 40.36175  ?  7051 LYS   A N      1 
ATOM   1998 C  CA     . LYS   A  1  253 ? -78.70519  31.00800  6.20691   1.000 45.80974  ?  7051 LYS   A CA     1 
ATOM   1999 C  C      . LYS   A  1  253 ? -77.84689  29.86036  5.69318   1.000 42.96847  ?  7051 LYS   A C      1 
ATOM   2000 O  O      . LYS   A  1  253 ? -76.92583  29.41361  6.38351   1.000 41.24887  ?  7051 LYS   A O      1 
ATOM   2001 C  CB     . LYS   A  1  253 ? -77.89699  32.30699  6.26494   1.000 52.43080  ?  7051 LYS   A CB     1 
ATOM   2002 C  CG     . LYS   A  1  253 ? -78.55352  33.43180  7.11979   1.000 55.50387  ?  7051 LYS   A CG     1 
ATOM   2003 C  CD     . LYS   A  1  253 ? -78.36868  33.24652  8.66903   1.000 54.46507  ?  7051 LYS   A CD     1 
ATOM   2004 C  CE     . LYS   A  1  253 ? -79.22835  34.22356  9.48911   1.000 56.20144  ?  7051 LYS   A CE     1 
ATOM   2005 N  NZ     . LYS   A  1  253 ? -80.73441  34.05698  9.30741   1.000 50.75329  ?  7051 LYS   A NZ     1 
ATOM   2006 N  N      . LEU   A  1  254 ? -78.14508  29.36230  4.49316   1.000 48.05520  ?  7052 LEU   A N      1 
ATOM   2007 C  CA     . LEU   A  1  254 ? -77.34441  28.27064  3.93437   1.000 46.94869  ?  7052 LEU   A CA     1 
ATOM   2008 C  C      . LEU   A  1  254 ? -76.10503  28.89350  3.30914   1.000 51.05774  ?  7052 LEU   A C      1 
ATOM   2009 O  O      . LEU   A  1  254 ? -76.15300  29.43941  2.20499   1.000 54.06163  ?  7052 LEU   A O      1 
ATOM   2010 C  CB     . LEU   A  1  254 ? -78.14600  27.44052  2.93461   1.000 51.04655  ?  7052 LEU   A CB     1 
ATOM   2011 C  CG     . LEU   A  1  254 ? -77.44635  26.26000  2.21331   1.000 51.85938  ?  7052 LEU   A CG     1 
ATOM   2012 C  CD1    . LEU   A  1  254 ? -76.59307  25.34469  3.12562   1.000 48.79731  ?  7052 LEU   A CD1    1 
ATOM   2013 C  CD2    . LEU   A  1  254 ? -78.46270  25.41136  1.44065   1.000 52.53699  ?  7052 LEU   A CD2    1 
ATOM   2014 N  N      . ARG   A  1  255 ? -74.98944  28.81888  4.03031   1.000 47.28699  ?  7053 ARG   A N      1 
ATOM   2015 C  CA     . ARG   A  1  255 ? -73.74257  29.45449  3.62702   1.000 47.31178  ?  7053 ARG   A CA     1 
ATOM   2016 C  C      . ARG   A  1  255 ? -72.91608  28.59391  2.67834   1.000 48.03190  ?  7053 ARG   A C      1 
ATOM   2017 O  O      . ARG   A  1  255 ? -71.92193  29.08273  2.13419   1.000 51.05219  ?  7053 ARG   A O      1 
ATOM   2018 C  CB     . ARG   A  1  255 ? -72.91417  29.81414  4.87798   1.000 41.89597  ?  7053 ARG   A CB     1 
ATOM   2019 C  CG     . ARG   A  1  255 ? -73.64771  30.74318  5.86585   1.000 44.13595  ?  7053 ARG   A CG     1 
ATOM   2020 C  CD     . ARG   A  1  255 ? -72.79098  31.14193  7.09835   1.000 46.18920  ?  7053 ARG   A CD     1 
ATOM   2021 N  NE     . ARG   A  1  255 ? -73.31177  32.33251  7.77989   1.000 58.18499  ?  7053 ARG   A NE     1 
ATOM   2022 C  CZ     . ARG   A  1  255 ? -73.88908  32.35749  8.98160   1.000 59.06791  ?  7053 ARG   A CZ     1 
ATOM   2023 N  NH1    . ARG   A  1  255 ? -74.02928  31.25857  9.71701   1.000 41.87663  ?  7053 ARG   A NH1    1 
ATOM   2024 N  NH2    . ARG   A  1  255 ? -74.33344  33.51915  9.46338   1.000 57.33725  ?  7053 ARG   A NH2    1 
ATOM   2025 N  N      . GLY   A  1  256 ? -73.29639  27.33353  2.47662   1.000 45.54829  ?  7054 GLY   A N      1 
ATOM   2026 C  CA     . GLY   A  1  256 ? -72.52427  26.40350  1.67590   1.000 44.41792  ?  7054 GLY   A CA     1 
ATOM   2027 C  C      . GLY   A  1  256 ? -71.08684  26.27476  2.11898   1.000 49.87672  ?  7054 GLY   A C      1 
ATOM   2028 O  O      . GLY   A  1  256 ? -70.19223  26.08672  1.28744   1.000 53.01672  ?  7054 GLY   A O      1 
ATOM   2029 N  N      . THR   A  1  257 ? -70.85276  26.38001  3.43131   1.000 42.71066  ?  7055 THR   A N      1 
ATOM   2030 C  CA     . THR   A  1  257 ? -69.50333  26.32264  3.98338   1.000 42.39151  ?  7055 THR   A CA     1 
ATOM   2031 C  C      . THR   A  1  257 ? -68.74801  25.12677  3.42978   1.000 39.63901  ?  7055 THR   A C      1 
ATOM   2032 O  O      . THR   A  1  257 ? -69.30716  24.03516  3.27863   1.000 46.92694  ?  7055 THR   A O      1 
ATOM   2033 C  CB     . THR   A  1  257 ? -69.55960  26.22692  5.51872   1.000 35.71174  ?  7055 THR   A CB     1 
ATOM   2034 O  OG1    . THR   A  1  257 ? -70.40722  27.25330  6.03895   1.000 38.30761  ?  7055 THR   A OG1    1 
ATOM   2035 C  CG2    . THR   A  1  257 ? -68.17279  26.36326  6.10370   1.000 39.56137  ?  7055 THR   A CG2    1 
ATOM   2036 N  N      . ALA   A  1  258 ? -67.45852  25.32847  3.16268   1.000 42.39573  ?  7056 ALA   A N      1 
ATOM   2037 C  CA     . ALA   A  1  258 ? -66.63449  24.26526  2.60766   1.000 41.75796  ?  7056 ALA   A CA     1 
ATOM   2038 C  C      . ALA   A  1  258 ? -66.36157  23.18147  3.64376   1.000 43.94074  ?  7056 ALA   A C      1 
ATOM   2039 O  O      . ALA   A  1  258 ? -66.12646  23.46434  4.82489   1.000 40.32765  ?  7056 ALA   A O      1 
ATOM   2040 C  CB     . ALA   A  1  258 ? -65.30484  24.82327  2.09098   1.000 41.56619  ?  7056 ALA   A CB     1 
ATOM   2041 N  N      . VAL   A  1  259 ? -66.38215  21.93021  3.18176   1.000 42.95070  ?  7057 VAL   A N      1 
ATOM   2042 C  CA     . VAL   A  1  259 ? -66.04310  20.75965  3.98089   1.000 40.41808  ?  7057 VAL   A CA     1 
ATOM   2043 C  C      . VAL   A  1  259 ? -64.81659  20.12250  3.35274   1.000 44.55594  ?  7057 VAL   A C      1 
ATOM   2044 O  O      . VAL   A  1  259 ? -64.80985  19.84654  2.14809   1.000 47.42198  ?  7057 VAL   A O      1 
ATOM   2045 C  CB     . VAL   A  1  259 ? -67.19737  19.74232  4.03664   1.000 41.31324  ?  7057 VAL   A CB     1 
ATOM   2046 C  CG1    . VAL   A  1  259 ? -66.76771  18.48511  4.78172   1.000 38.55974  ?  7057 VAL   A CG1    1 
ATOM   2047 C  CG2    . VAL   A  1  259 ? -68.44243  20.36056  4.66000   1.000 38.66806  ?  7057 VAL   A CG2    1 
ATOM   2048 N  N      . MET   A  1  260 ? -63.78715  19.89187  4.16030   1.000 40.48466  ?  7058 MET   A N      1 
ATOM   2049 C  CA     . MET   A  1  260 ? -62.56456  19.24647  3.70963   1.000 48.01262  ?  7058 MET   A CA     1 
ATOM   2050 C  C      . MET   A  1  260 ? -62.16871  18.16809  4.69304   1.000 41.63374  ?  7058 MET   A C      1 
ATOM   2051 O  O      . MET   A  1  260 ? -62.38873  18.29007  5.89861   1.000 44.98293  ?  7058 MET   A O      1 
ATOM   2052 C  CB     . MET   A  1  260 ? -61.39920  20.22414  3.58843   1.000 48.74018  ?  7058 MET   A CB     1 
ATOM   2053 C  CG     . MET   A  1  260 ? -61.49761  21.17408  2.42345   1.000 55.31961  ?  7058 MET   A CG     1 
ATOM   2054 S  SD     . MET   A  1  260 ? -60.26701  22.47572  2.64060   1.000 71.90342  ?  7058 MET   A SD     1 
ATOM   2055 C  CE     . MET   A  1  260 ? -59.18262  21.69934  3.82951   1.000 56.37120  ?  7058 MET   A CE     1 
ATOM   2056 N  N      . SER   A  1  261 ? -61.55613  17.12192  4.17471   1.000 45.18570  ?  7059 SER   A N      1 
ATOM   2057 C  CA     . SER   A  1  261 ? -60.93379  16.12355  5.02042   1.000 51.83629  ?  7059 SER   A CA     1 
ATOM   2058 C  C      . SER   A  1  261 ? -59.45518  16.46302  5.14161   1.000 60.90311  ?  7059 SER   A C      1 
ATOM   2059 O  O      . SER   A  1  261 ? -58.77210  16.65944  4.13101   1.000 68.10202  ?  7059 SER   A O      1 
ATOM   2060 C  CB     . SER   A  1  261 ? -61.13439  14.72636  4.44080   1.000 57.33910  ?  7059 SER   A CB     1 
ATOM   2061 O  OG     . SER   A  1  261 ? -60.32202  13.78953  5.11843   1.000 68.61787  ?  7059 SER   A OG     1 
ATOM   2062 N  N      . LEU   A  1  262 ? -58.97140  16.56764  6.37275   1.000 55.51427  ?  7060 LEU   A N      1 
ATOM   2063 C  CA     . LEU   A  1  262 ? -57.57918  16.90870  6.60303   1.000 64.43992  ?  7060 LEU   A CA     1 
ATOM   2064 C  C      . LEU   A  1  262 ? -57.05830  16.07946  7.76023   1.000 69.85647  ?  7060 LEU   A C      1 
ATOM   2065 O  O      . LEU   A  1  262 ? -57.82254  15.56943  8.58357   1.000 73.00948  ?  7060 LEU   A O      1 
ATOM   2066 C  CB     . LEU   A  1  262 ? -57.37924  18.40504  6.89566   1.000 64.06422  ?  7060 LEU   A CB     1 
ATOM   2067 C  CG     . LEU   A  1  262 ? -57.60196  19.40027  5.75619   1.000 59.17385  ?  7060 LEU   A CG     1 
ATOM   2068 C  CD1    . LEU   A  1  262 ? -57.50967  20.82558  6.28339   1.000 59.68852  ?  7060 LEU   A CD1    1 
ATOM   2069 C  CD2    . LEU   A  1  262 ? -56.59124  19.17901  4.64317   1.000 66.43370  ?  7060 LEU   A CD2    1 
ATOM   2070 N  N      . LYS   A  1  263 ? -55.73862  15.95015  7.80841   1.000 76.82323  ?  7061 LYS   A N      1 
ATOM   2071 C  CA     . LYS   A  1  263 ? -55.06344  15.16323  8.82605   1.000 77.79309  ?  7061 LYS   A CA     1 
ATOM   2072 C  C      . LYS   A  1  263 ? -54.35661  16.10614  9.79377   1.000 77.58127  ?  7061 LYS   A C      1 
ATOM   2073 O  O      . LYS   A  1  263 ? -53.85974  17.16644  9.39895   1.000 77.83627  ?  7061 LYS   A O      1 
ATOM   2074 C  CB     . LYS   A  1  263 ? -54.07708  14.17403  8.18561   1.000 74.62153  ?  7061 LYS   A CB     1 
ATOM   2075 C  CG     . LYS   A  1  263 ? -54.61660  13.46676  6.91881   1.000 75.49783  ?  7061 LYS   A CG     1 
ATOM   2076 C  CD     . LYS   A  1  263 ? -56.13639  13.20743  7.00589   1.000 79.73015  ?  7061 LYS   A CD     1 
ATOM   2077 C  CE     . LYS   A  1  263 ? -56.72606  12.55477  5.73570   1.000 76.37791  ?  7061 LYS   A CE     1 
ATOM   2078 N  NZ     . LYS   A  1  263 ? -56.73852  13.43533  4.51734   1.000 78.68797  ?  7061 LYS   A NZ     1 
ATOM   2079 N  N      . GLU   A  1  264 ? -54.32908  15.71467  11.07181  1.000 79.13581  ?  7062 GLU   A N      1 
ATOM   2080 C  CA     . GLU   A  1  264 ? -53.90416  16.63224  12.12676  1.000 86.03326  ?  7062 GLU   A CA     1 
ATOM   2081 C  C      . GLU   A  1  264 ? -52.61937  17.37484  11.77670  1.000 84.67384  ?  7062 GLU   A C      1 
ATOM   2082 O  O      . GLU   A  1  264 ? -52.42080  18.51379  12.21662  1.000 82.99626  ?  7062 GLU   A O      1 
ATOM   2083 C  CB     . GLU   A  1  264 ? -53.72234  15.87995  13.44545  1.000 86.31442  ?  7062 GLU   A CB     1 
ATOM   2084 C  CG     . GLU   A  1  264 ? -53.22698  16.77069  14.58316  1.000 95.84457  ?  7062 GLU   A CG     1 
ATOM   2085 C  CD     . GLU   A  1  264 ? -52.48095  15.99257  15.64981  1.000 102.06599 ?  7062 GLU   A CD     1 
ATOM   2086 O  OE1    . GLU   A  1  264 ? -52.30793  14.76886  15.46502  1.000 102.89909 ?  7062 GLU   A OE1    1 
ATOM   2087 O  OE2    . GLU   A  1  264 ? -52.07223  16.59738  16.66801  1.000 101.59796 ?  7062 GLU   A OE2    1 
ATOM   2088 N  N      . GLY   A  1  265 ? -51.73449  16.75613  10.99417  1.000 81.84974  ?  7063 GLY   A N      1 
ATOM   2089 C  CA     . GLY   A  1  265 ? -50.51189  17.43613  10.61324  1.000 80.87177  ?  7063 GLY   A CA     1 
ATOM   2090 C  C      . GLY   A  1  265 ? -50.72220  18.64294  9.72127   1.000 79.80218  ?  7063 GLY   A C      1 
ATOM   2091 O  O      . GLY   A  1  265 ? -49.82514  19.48674  9.61953   1.000 83.24357  ?  7063 GLY   A O      1 
ATOM   2092 N  N      . GLN   A  1  266 ? -51.88463  18.75242  9.08010   1.000 76.77633  ?  7064 GLN   A N      1 
ATOM   2093 C  CA     . GLN   A  1  266 ? -52.12429  19.79813  8.09399   1.000 74.71883  ?  7064 GLN   A CA     1 
ATOM   2094 C  C      . GLN   A  1  266 ? -52.91943  20.97800  8.63627   1.000 74.62387  ?  7064 GLN   A C      1 
ATOM   2095 O  O      . GLN   A  1  266 ? -53.22536  21.89668  7.86939   1.000 71.36878  ?  7064 GLN   A O      1 
ATOM   2096 C  CB     . GLN   A  1  266 ? -52.86045  19.22814  6.88089   1.000 76.70003  ?  7064 GLN   A CB     1 
ATOM   2097 C  CG     . GLN   A  1  266 ? -52.37919  17.86900  6.40889   1.000 76.44250  ?  7064 GLN   A CG     1 
ATOM   2098 C  CD     . GLN   A  1  266 ? -53.27601  17.31763  5.32203   1.000 75.71480  ?  7064 GLN   A CD     1 
ATOM   2099 O  OE1    . GLN   A  1  266 ? -54.07274  16.40942  5.55894   1.000 74.95088  ?  7064 GLN   A OE1    1 
ATOM   2100 N  NE2    . GLN   A  1  266 ? -53.16983  17.88512  4.12476   1.000 73.10748  ?  7064 GLN   A NE2    1 
ATOM   2101 N  N      . ILE   A  1  267 ? -53.27849  20.97580  9.92073   1.000 75.11680  ?  7065 ILE   A N      1 
ATOM   2102 C  CA     . ILE   A  1  267 ? -54.04098  22.08576  10.48188  1.000 71.14231  ?  7065 ILE   A CA     1 
ATOM   2103 C  C      . ILE   A  1  267 ? -53.07918  23.21039  10.84058  1.000 69.24573  ?  7065 ILE   A C      1 
ATOM   2104 O  O      . ILE   A  1  267 ? -52.60694  23.30380  11.98038  1.000 72.85956  ?  7065 ILE   A O      1 
ATOM   2105 C  CB     . ILE   A  1  267 ? -54.87110  21.65858  11.70769  1.000 70.20064  ?  7065 ILE   A CB     1 
ATOM   2106 C  CG1    . ILE   A  1  267 ? -55.49914  20.27987  11.49088  1.000 70.45062  ?  7065 ILE   A CG1    1 
ATOM   2107 C  CG2    . ILE   A  1  267 ? -55.96820  22.67711  11.97297  1.000 61.30556  ?  7065 ILE   A CG2    1 
ATOM   2108 C  CD1    . ILE   A  1  267 ? -56.64823  20.27308  10.51065  1.000 63.59214  ?  7065 ILE   A CD1    1 
ATOM   2109 N  N      . ASN   A  1  268 ? -52.77876  24.06226  9.86395   1.000 67.85411  ?  7066 ASN   A N      1 
ATOM   2110 C  CA     . ASN   A  1  268 ? -51.91466  25.21405  10.05215  1.000 66.11490  ?  7066 ASN   A CA     1 
ATOM   2111 C  C      . ASN   A  1  268 ? -52.74638  26.43210  10.46030  1.000 68.89614  ?  7066 ASN   A C      1 
ATOM   2112 O  O      . ASN   A  1  268 ? -53.97587  26.37238  10.57644  1.000 65.62072  ?  7066 ASN   A O      1 
ATOM   2113 C  CB     . ASN   A  1  268 ? -51.12116  25.48573  8.77609   1.000 62.65717  ?  7066 ASN   A CB     1 
ATOM   2114 C  CG     . ASN   A  1  268 ? -52.01102  25.83898  7.60217   1.000 65.06693  ?  7066 ASN   A CG     1 
ATOM   2115 O  OD1    . ASN   A  1  268 ? -52.85956  26.72785  7.68973   1.000 63.36236  ?  7066 ASN   A OD1    1 
ATOM   2116 N  ND2    . ASN   A  1  268 ? -51.82912  25.13419  6.49585   1.000 66.40600  ?  7066 ASN   A ND2    1 
ATOM   2117 N  N      . ASP   A  1  269 ? -52.06894  27.56745  10.65815  1.000 64.39654  ?  7067 ASP   A N      1 
ATOM   2118 C  CA     . ASP   A  1  269 ? -52.76195  28.74920  11.16127  1.000 64.20111  ?  7067 ASP   A CA     1 
ATOM   2119 C  C      . ASP   A  1  269 ? -53.72808  29.32499  10.13573  1.000 63.64302  ?  7067 ASP   A C      1 
ATOM   2120 O  O      . ASP   A  1  269 ? -54.76004  29.89253  10.51457  1.000 61.83693  ?  7067 ASP   A O      1 
ATOM   2121 C  CB     . ASP   A  1  269 ? -51.76075  29.81395  11.60221  1.000 65.34244  ?  7067 ASP   A CB     1 
ATOM   2122 C  CG     . ASP   A  1  269 ? -50.95628  29.38357  12.80954  1.000 75.40924  ?  7067 ASP   A CG     1 
ATOM   2123 O  OD1    . ASP   A  1  269 ? -49.84778  29.92861  13.00758  1.000 78.18026  ?  7067 ASP   A OD1    1 
ATOM   2124 O  OD2    . ASP   A  1  269 ? -51.42498  28.48297  13.54685  1.000 77.22606  ?  7067 ASP   A OD2    1 
ATOM   2125 N  N      . MET   A  1  270 ? -53.42422  29.20315  8.84417   1.000 59.73704  ?  7068 MET   A N      1 
ATOM   2126 C  CA     . MET   A  1  270 ? -54.40386  29.60190  7.84068   1.000 61.63086  ?  7068 MET   A CA     1 
ATOM   2127 C  C      . MET   A  1  270 ? -55.70334  28.82228  8.02144   1.000 56.43166  ?  7068 MET   A C      1 
ATOM   2128 O  O      . MET   A  1  270 ? -56.79690  29.39935  8.01807   1.000 49.61658  ?  7068 MET   A O      1 
ATOM   2129 C  CB     . MET   A  1  270 ? -53.82835  29.39312  6.44042   1.000 61.51944  ?  7068 MET   A CB     1 
ATOM   2130 C  CG     . MET   A  1  270 ? -54.41269  30.31269  5.38200   1.000 69.29545  ?  7068 MET   A CG     1 
ATOM   2131 S  SD     . MET   A  1  270 ? -55.69973  29.51655  4.40760   1.000 88.85536  ?  7068 MET   A SD     1 
ATOM   2132 C  CE     . MET   A  1  270 ? -54.82646  28.06172  3.80385   1.000 66.16714  ?  7068 MET   A CE     1 
ATOM   2133 N  N      . ILE   A  1  271 ? -55.59557  27.50474  8.20980   1.000 53.71425  ?  7069 ILE   A N      1 
ATOM   2134 C  CA     . ILE   A  1  271 ? -56.78304  26.67463  8.41078   1.000 54.68333  ?  7069 ILE   A CA     1 
ATOM   2135 C  C      . ILE   A  1  271 ? -57.48906  27.06551  9.70496   1.000 49.38645  ?  7069 ILE   A C      1 
ATOM   2136 O  O      . ILE   A  1  271 ? -58.70038  27.31371  9.72585   1.000 44.82303  ?  7069 ILE   A O      1 
ATOM   2137 C  CB     . ILE   A  1  271 ? -56.39893  25.18403  8.41456   1.000 55.82636  ?  7069 ILE   A CB     1 
ATOM   2138 C  CG1    . ILE   A  1  271 ? -55.81603  24.76071  7.05710   1.000 57.21997  ?  7069 ILE   A CG1    1 
ATOM   2139 C  CG2    . ILE   A  1  271 ? -57.58557  24.33266  8.81773   1.000 48.79690  ?  7069 ILE   A CG2    1 
ATOM   2140 C  CD1    . ILE   A  1  271 ? -56.77546  24.86274  5.88554   1.000 49.16247  ?  7069 ILE   A CD1    1 
ATOM   2141 N  N      . LEU   A  1  272 ? -56.73555  27.12375  10.80542  1.000 52.68609  ?  7070 LEU   A N      1 
ATOM   2142 C  CA     . LEU   A  1  272 ? -57.29933  27.53822  12.08434  1.000 50.16219  ?  7070 LEU   A CA     1 
ATOM   2143 C  C      . LEU   A  1  272 ? -57.99615  28.88304  11.98072  1.000 49.75223  ?  7070 LEU   A C      1 
ATOM   2144 O  O      . LEU   A  1  272 ? -58.99587  29.11954  12.66794  1.000 49.43161  ?  7070 LEU   A O      1 
ATOM   2145 C  CB     . LEU   A  1  272 ? -56.20416  27.59495  13.14712  1.000 52.81971  ?  7070 LEU   A CB     1 
ATOM   2146 C  CG     . LEU   A  1  272 ? -55.64512  26.25524  13.63194  1.000 59.66415  ?  7070 LEU   A CG     1 
ATOM   2147 C  CD1    . LEU   A  1  272 ? -54.43258  26.45920  14.53618  1.000 63.08084  ?  7070 LEU   A CD1    1 
ATOM   2148 C  CD2    . LEU   A  1  272 ? -56.72364  25.46858  14.36030  1.000 57.65820  ?  7070 LEU   A CD2    1 
ATOM   2149 N  N      . SER   A  1  273 ? -57.49300  29.77058  11.12422  1.000 46.75365  ?  7071 SER   A N      1 
ATOM   2150 C  CA     . SER   A  1  273 ? -58.12902  31.06723  10.93893  1.000 43.94141  ?  7071 SER   A CA     1 
ATOM   2151 C  C      . SER   A  1  273 ? -59.47424  30.92292  10.23629  1.000 48.36384  ?  7071 SER   A C      1 
ATOM   2152 O  O      . SER   A  1  273 ? -60.46155  31.55630  10.63096  1.000 45.61288  ?  7071 SER   A O      1 
ATOM   2153 C  CB     . SER   A  1  273 ? -57.18077  31.98947  10.16103  1.000 56.79290  ?  7071 SER   A CB     1 
ATOM   2154 O  OG     . SER   A  1  273 ? -57.83933  33.11672  9.61665   1.000 58.20751  ?  7071 SER   A OG     1 
ATOM   2155 N  N      . LEU   A  1  274 ? -59.53919  30.08224  9.20278   1.000 45.36790  ?  7072 LEU   A N      1 
ATOM   2156 C  CA     . LEU   A  1  274 ? -60.80794  29.85051  8.52181   1.000 43.86158  ?  7072 LEU   A CA     1 
ATOM   2157 C  C      . LEU   A  1  274 ? -61.80954  29.15531  9.44103   1.000 43.38920  ?  7072 LEU   A C      1 
ATOM   2158 O  O      . LEU   A  1  274 ? -63.00506  29.48043  9.42640   1.000 39.33733  ?  7072 LEU   A O      1 
ATOM   2159 C  CB     . LEU   A  1  274 ? -60.56860  29.03455  7.25434   1.000 46.47532  ?  7072 LEU   A CB     1 
ATOM   2160 C  CG     . LEU   A  1  274 ? -59.75276  29.75040  6.16906   1.000 53.91964  ?  7072 LEU   A CG     1 
ATOM   2161 C  CD1    . LEU   A  1  274 ? -59.30705  28.75076  5.09854   1.000 50.98454  ?  7072 LEU   A CD1    1 
ATOM   2162 C  CD2    . LEU   A  1  274 ? -60.56685  30.88090  5.53902   1.000 41.52278  ?  7072 LEU   A CD2    1 
ATOM   2163 N  N      . LEU   A  1  275 ? -61.33655  28.21273  10.26155  1.000 37.97030  ?  7073 LEU   A N      1 
ATOM   2164 C  CA     . LEU   A  1  275 ? -62.21523  27.56812  11.23276  1.000 40.50211  ?  7073 LEU   A CA     1 
ATOM   2165 C  C      . LEU   A  1  275 ? -62.83061  28.59842  12.16477  1.000 42.12435  ?  7073 LEU   A C      1 
ATOM   2166 O  O      . LEU   A  1  275 ? -64.04602  28.59684  12.40232  1.000 39.34264  ?  7073 LEU   A O      1 
ATOM   2167 C  CB     . LEU   A  1  275 ? -61.43944  26.52155  12.03152  1.000 38.30423  ?  7073 LEU   A CB     1 
ATOM   2168 C  CG     . LEU   A  1  275 ? -60.95837  25.28690  11.25986  1.000 39.95807  ?  7073 LEU   A CG     1 
ATOM   2169 C  CD1    . LEU   A  1  275 ? -60.17941  24.36997  12.19230  1.000 35.72676  ?  7073 LEU   A CD1    1 
ATOM   2170 C  CD2    . LEU   A  1  275 ? -62.12450  24.53643  10.59185  1.000 37.65580  ?  7073 LEU   A CD2    1 
ATOM   2171 N  N      . SER   A  1  276 ? -61.99789  29.51216  12.67635  1.000 41.76640  ?  7074 SER   A N      1 
ATOM   2172 C  CA     . SER   A  1  276 ? -62.43329  30.50360  13.65083  1.000 40.01096  ?  7074 SER   A CA     1 
ATOM   2173 C  C      . SER   A  1  276 ? -63.45686  31.47016  13.09301  1.000 42.39250  ?  7074 SER   A C      1 
ATOM   2174 O  O      . SER   A  1  276 ? -64.16733  32.11237  13.87646  1.000 41.12371  ?  7074 SER   A O      1 
ATOM   2175 C  CB     . SER   A  1  276 ? -61.23101  31.29841  14.15233  1.000 39.22845  ?  7074 SER   A CB     1 
ATOM   2176 O  OG     . SER   A  1  276 ? -60.40323  30.46602  14.92611  1.000 45.86904  ?  7074 SER   A OG     1 
ATOM   2177 N  N      . LYS   A  1  277 ? -63.52210  31.61869  11.77021  1.000 38.97961  ?  7075 LYS   A N      1 
ATOM   2178 C  CA     . LYS   A  1  277 ? -64.41503  32.56896  11.11963  1.000 39.40135  ?  7075 LYS   A CA     1 
ATOM   2179 C  C      . LYS   A  1  277 ? -65.67556  31.91671  10.57623  1.000 38.27146  ?  7075 LYS   A C      1 
ATOM   2180 O  O      . LYS   A  1  277 ? -66.48222  32.59224  9.93272   1.000 42.36631  ?  7075 LYS   A O      1 
ATOM   2181 C  CB     . LYS   A  1  277 ? -63.68949  33.29457  9.98049   1.000 42.93042  ?  7075 LYS   A CB     1 
ATOM   2182 C  CG     . LYS   A  1  277 ? -62.49233  34.14431  10.42908  1.000 51.69156  ?  7075 LYS   A CG     1 
ATOM   2183 C  CD     . LYS   A  1  277 ? -61.78543  34.79615  9.22631   1.000 56.59789  ?  7075 LYS   A CD     1 
ATOM   2184 C  CE     . LYS   A  1  277 ? -60.44693  35.43013  9.62293   1.000 61.37270  ?  7075 LYS   A CE     1 
ATOM   2185 N  NZ     . LYS   A  1  277 ? -60.56900  36.39291  10.76596  1.000 65.74318  ?  7075 LYS   A NZ     1 
ATOM   2186 N  N      . GLY   A  1  278 ? -65.87675  30.62841  10.82610  1.000 39.76695  ?  7076 GLY   A N      1 
ATOM   2187 C  CA     . GLY   A  1  278 ? -67.07910  29.98514  10.33208  1.000 40.39117  ?  7076 GLY   A CA     1 
ATOM   2188 C  C      . GLY   A  1  278 ? -67.05120  29.69073  8.85212   1.000 40.58161  ?  7076 GLY   A C      1 
ATOM   2189 O  O      . GLY   A  1  278 ? -68.11211  29.53991  8.23778   1.000 43.78491  ?  7076 GLY   A O      1 
ATOM   2190 N  N      . ARG   A  1  279 ? -65.86112  29.59875  8.25852   1.000 40.30682  ?  7077 ARG   A N      1 
ATOM   2191 C  CA     . ARG   A  1  279 ? -65.71406  29.45128  6.81902   1.000 44.83302  ?  7077 ARG   A CA     1 
ATOM   2192 C  C      . ARG   A  1  279 ? -65.24996  28.06301  6.40684   1.000 39.37320  ?  7077 ARG   A C      1 
ATOM   2193 O  O      . ARG   A  1  279 ? -65.00082  27.83655  5.21666   1.000 41.16249  ?  7077 ARG   A O      1 
ATOM   2194 C  CB     . ARG   A  1  279 ? -64.73640  30.50854  6.28209   1.000 42.12085  ?  7077 ARG   A CB     1 
ATOM   2195 C  CG     . ARG   A  1  279 ? -65.20360  31.93384  6.53902   1.000 46.66213  ?  7077 ARG   A CG     1 
ATOM   2196 C  CD     . ARG   A  1  279 ? -64.37273  32.93458  5.74478   1.000 53.84808  ?  7077 ARG   A CD     1 
ATOM   2197 N  NE     . ARG   A  1  279 ? -64.59042  34.29888  6.20832   1.000 65.85859  ?  7077 ARG   A NE     1 
ATOM   2198 C  CZ     . ARG   A  1  279 ? -63.65741  35.24285  6.20974   1.000 69.32302  ?  7077 ARG   A CZ     1 
ATOM   2199 N  NH1    . ARG   A  1  279 ? -62.43028  35.00352  5.76519   1.000 65.73504  ?  7077 ARG   A NH1    1 
ATOM   2200 N  NH2    . ARG   A  1  279 ? -63.95946  36.45349  6.67458   1.000 62.96433  ?  7077 ARG   A NH2    1 
ATOM   2201 N  N      . LEU   A  1  280 ? -65.12796  27.13049  7.34627   1.000 39.69908  ?  7078 LEU   A N      1 
ATOM   2202 C  CA     . LEU   A  1  280 ? -64.57747  25.82930  7.00925   1.000 39.36201  ?  7078 LEU   A CA     1 
ATOM   2203 C  C      . LEU   A  1  280 ? -65.04835  24.79325  8.01675   1.000 38.25729  ?  7078 LEU   A C      1 
ATOM   2204 O  O      . LEU   A  1  280 ? -65.10450  25.07055  9.21903   1.000 38.96346  ?  7078 LEU   A O      1 
ATOM   2205 C  CB     . LEU   A  1  280 ? -63.04756  25.89060  6.98060   1.000 37.82854  ?  7078 LEU   A CB     1 
ATOM   2206 C  CG     . LEU   A  1  280 ? -62.31986  24.57009  6.72386   1.000 44.80528  ?  7078 LEU   A CG     1 
ATOM   2207 C  CD1    . LEU   A  1  280 ? -62.70473  24.03201  5.36049   1.000 40.86541  ?  7078 LEU   A CD1    1 
ATOM   2208 C  CD2    . LEU   A  1  280 ? -60.80628  24.74133  6.84005   1.000 41.84265  ?  7078 LEU   A CD2    1 
ATOM   2209 N  N      . ILE   A  1  281 ? -65.36687  23.59929  7.51643   1.000 37.81316  ?  7079 ILE   A N      1 
ATOM   2210 C  CA     . ILE   A  1  281 ? -65.65126  22.42353  8.33435   1.000 35.57614  ?  7079 ILE   A CA     1 
ATOM   2211 C  C      . ILE   A  1  281 ? -64.66236  21.32929  7.94900   1.000 37.03058  ?  7079 ILE   A C      1 
ATOM   2212 O  O      . ILE   A  1  281 ? -64.40130  21.11320  6.76287   1.000 40.82448  ?  7079 ILE   A O      1 
ATOM   2213 C  CB     . ILE   A  1  281 ? -67.10128  21.94313  8.12789   1.000 39.78440  ?  7079 ILE   A CB     1 
ATOM   2214 C  CG1    . ILE   A  1  281 ? -68.09181  22.87288  8.82866   1.000 37.48127  ?  7079 ILE   A CG1    1 
ATOM   2215 C  CG2    . ILE   A  1  281 ? -67.26618  20.50188  8.58437   1.000 36.02585  ?  7079 ILE   A CG2    1 
ATOM   2216 C  CD1    . ILE   A  1  281 ? -68.26887  22.53056  10.29813  1.000 39.53770  ?  7079 ILE   A CD1    1 
ATOM   2217 N  N      . ILE   A  1  282 ? -64.09809  20.64628  8.93256   1.000 34.94977  ?  7080 ILE   A N      1 
ATOM   2218 C  CA     . ILE   A  1  282 ? -63.14127  19.58229  8.65567   1.000 37.63349  ?  7080 ILE   A CA     1 
ATOM   2219 C  C      . ILE   A  1  282 ? -63.70855  18.29067  9.20937   1.000 41.68140  ?  7080 ILE   A C      1 
ATOM   2220 O  O      . ILE   A  1  282 ? -63.83759  18.13103  10.43281  1.000 39.68200  ?  7080 ILE   A O      1 
ATOM   2221 C  CB     . ILE   A  1  282 ? -61.75572  19.86608  9.24290   1.000 39.21047  ?  7080 ILE   A CB     1 
ATOM   2222 C  CG1    . ILE   A  1  282 ? -61.12666  21.06896  8.53830   1.000 39.81541  ?  7080 ILE   A CG1    1 
ATOM   2223 C  CG2    . ILE   A  1  282 ? -60.86955  18.62787  9.13154   1.000 41.60203  ?  7080 ILE   A CG2    1 
ATOM   2224 C  CD1    . ILE   A  1  282 ? -59.77559  21.44018  9.10923   1.000 50.05291  ?  7080 ILE   A CD1    1 
ATOM   2225 N  N      . ARG   A  1  283 ? -64.03721  17.36871  8.30720   1.000 38.94747  ?  7081 ARG   A N      1 
ATOM   2226 C  CA     . ARG   A  1  283 ? -64.53381  16.03779  8.63001   1.000 40.79668  ?  7081 ARG   A CA     1 
ATOM   2227 C  C      . ARG   A  1  283 ? -64.65572  15.27658  7.31891   1.000 43.26052  ?  7081 ARG   A C      1 
ATOM   2228 O  O      . ARG   A  1  283 ? -64.68099  15.87702  6.24025   1.000 41.27506  ?  7081 ARG   A O      1 
ATOM   2229 C  CB     . ARG   A  1  283 ? -65.89381  16.08645  9.34403   1.000 34.51954  ?  7081 ARG   A CB     1 
ATOM   2230 C  CG     . ARG   A  1  283 ? -66.99534  16.77966  8.52231   1.000 33.95570  ?  7081 ARG   A CG     1 
ATOM   2231 C  CD     . ARG   A  1  283 ? -68.39451  16.40669  9.04396   1.000 34.76256  ?  7081 ARG   A CD     1 
ATOM   2232 N  NE     . ARG   A  1  283 ? -69.45695  17.24799  8.50102   1.000 32.76473  ?  7081 ARG   A NE     1 
ATOM   2233 C  CZ     . ARG   A  1  283 ? -69.99561  17.09449  7.30092   1.000 38.65069  ?  7081 ARG   A CZ     1 
ATOM   2234 N  NH1    . ARG   A  1  283 ? -69.58687  16.13904  6.47595   1.000 39.05059  ?  7081 ARG   A NH1    1 
ATOM   2235 N  NH2    . ARG   A  1  283 ? -70.95778  17.92716  6.91146   1.000 33.58647  ?  7081 ARG   A NH2    1 
ATOM   2236 N  N      . GLU   A  1  284 ? -64.76805  13.95575  7.42644   1.000 44.50171  ?  7082 GLU   A N      1 
ATOM   2237 C  CA     . GLU   A  1  284 ? -65.15343  13.16314  6.26923   1.000 49.61013  ?  7082 GLU   A CA     1 
ATOM   2238 C  C      . GLU   A  1  284 ? -66.57912  13.50604  5.85730   1.000 47.82341  ?  7082 GLU   A C      1 
ATOM   2239 O  O      . GLU   A  1  284 ? -67.37458  14.03097  6.64266   1.000 47.34454  ?  7082 GLU   A O      1 
ATOM   2240 C  CB     . GLU   A  1  284 ? -65.05034  11.66868  6.56411   1.000 53.52219  ?  7082 GLU   A CB     1 
ATOM   2241 C  CG     . GLU   A  1  284 ? -63.66184  11.17530  7.00091   1.000 63.31563  ?  7082 GLU   A CG     1 
ATOM   2242 C  CD     . GLU   A  1  284 ? -62.57692  11.35349  5.93516   1.000 69.07329  ?  7082 GLU   A CD     1 
ATOM   2243 O  OE1    . GLU   A  1  284 ? -61.50006  11.89869  6.27745   1.000 73.28365  ?  7082 GLU   A OE1    1 
ATOM   2244 O  OE2    . GLU   A  1  284 ? -62.79565  10.95208  4.76480   1.000 70.51210  ?  7082 GLU   A OE2    1 
ATOM   2245 N  N      . ASN   A  1  285 ? -66.90139  13.21510  4.60149   1.000 47.34298  ?  7083 ASN   A N      1 
ATOM   2246 C  CA     . ASN   A  1  285 ? -68.23316  13.48357  4.07692   1.000 48.84149  ?  7083 ASN   A CA     1 
ATOM   2247 C  C      . ASN   A  1  285 ? -68.93729  12.19077  3.67676   1.000 52.35576  ?  7083 ASN   A C      1 
ATOM   2248 O  O      . ASN   A  1  285 ? -69.76741  12.17991  2.76720   1.000 52.94618  ?  7083 ASN   A O      1 
ATOM   2249 C  CB     . ASN   A  1  285 ? -68.16549  14.45571  2.90381   1.000 48.77446  ?  7083 ASN   A CB     1 
ATOM   2250 C  CG     . ASN   A  1  285 ? -69.38809  15.35207  2.81720   1.000 58.17163  ?  7083 ASN   A CG     1 
ATOM   2251 O  OD1    . ASN   A  1  285 ? -70.22493  15.37699  3.72551   1.000 53.47334  ?  7083 ASN   A OD1    1 
ATOM   2252 N  ND2    . ASN   A  1  285 ? -69.49192  16.10702  1.72462   1.000 58.43632  ?  7083 ASN   A ND2    1 
ATOM   2253 N  N      . ASN   A  1  286 ? -68.61289  11.09688  4.35824   1.000 51.92124  ?  7084 ASN   A N      1 
ATOM   2254 C  CA     . ASN   A  1  286 ? -69.20755  9.79769   4.06883   1.000 54.55459  ?  7084 ASN   A CA     1 
ATOM   2255 C  C      . ASN   A  1  286 ? -70.68522  9.80250   4.45944   1.000 56.29261  ?  7084 ASN   A C      1 
ATOM   2256 O  O      . ASN   A  1  286 ? -71.29227  10.84211  4.73655   1.000 54.35515  ?  7084 ASN   A O      1 
ATOM   2257 C  CB     . ASN   A  1  286 ? -68.45208  8.69217   4.79998   1.000 52.92752  ?  7084 ASN   A CB     1 
ATOM   2258 C  CG     . ASN   A  1  286 ? -66.99949  8.61267   4.39615   1.000 59.78986  ?  7084 ASN   A CG     1 
ATOM   2259 O  OD1    . ASN   A  1  286 ? -66.65488  8.82316   3.22648   1.000 62.66438  ?  7084 ASN   A OD1    1 
ATOM   2260 N  ND2    . ASN   A  1  286 ? -66.13032  8.31294   5.36354   1.000 56.79495  ?  7084 ASN   A ND2    1 
ATOM   2261 N  N      . ARG   A  1  287 ? -71.28367  8.61842   4.47059   1.000 49.07575  ?  7085 ARG   A N      1 
ATOM   2262 C  CA     . ARG   A  1  287 ? -72.67150  8.49271   4.87341   1.000 48.15676  ?  7085 ARG   A CA     1 
ATOM   2263 C  C      . ARG   A  1  287 ? -72.78043  8.50913   6.39442   1.000 44.38985  ?  7085 ARG   A C      1 
ATOM   2264 O  O      . ARG   A  1  287 ? -71.84556  8.15957   7.11959   1.000 43.32717  ?  7085 ARG   A O      1 
ATOM   2265 C  CB     . ARG   A  1  287 ? -73.27063  7.21013   4.30422   1.000 50.18252  ?  7085 ARG   A CB     1 
ATOM   2266 C  CG     . ARG   A  1  287 ? -72.34047  6.02985   4.42506   1.000 50.72493  ?  7085 ARG   A CG     1 
ATOM   2267 C  CD     . ARG   A  1  287 ? -72.84120  4.88945   3.57744   1.000 58.79781  ?  7085 ARG   A CD     1 
ATOM   2268 N  NE     . ARG   A  1  287 ? -72.62050  3.61027   4.23629   1.000 62.24644  ?  7085 ARG   A NE     1 
ATOM   2269 C  CZ     . ARG   A  1  287 ? -73.49096  2.61184   4.21087   1.000 67.70458  ?  7085 ARG   A CZ     1 
ATOM   2270 N  NH1    . ARG   A  1  287 ? -74.65206  2.72537   3.58120   1.000 63.55161  ?  7085 ARG   A NH1    1 
ATOM   2271 N  NH2    . ARG   A  1  287 ? -73.19571  1.47795   4.84123   1.000 68.89097  ?  7085 ARG   A NH2    1 
ATOM   2272 N  N      . VAL   A  1  288 ? -73.94165  8.92681   6.87472   1.000 43.46928  ?  7086 VAL   A N      1 
ATOM   2273 C  CA     . VAL   A  1  288 ? -74.18975  9.04777   8.30497   1.000 38.92574  ?  7086 VAL   A CA     1 
ATOM   2274 C  C      . VAL   A  1  288 ? -74.81256  7.75346   8.81224   1.000 36.97157  ?  7086 VAL   A C      1 
ATOM   2275 O  O      . VAL   A  1  288 ? -75.89987  7.36887   8.37438   1.000 34.59650  ?  7086 VAL   A O      1 
ATOM   2276 C  CB     . VAL   A  1  288 ? -75.10107  10.24299  8.59417   1.000 41.00178  ?  7086 VAL   A CB     1 
ATOM   2277 C  CG1    . VAL   A  1  288 ? -75.48262  10.25493  10.04951  1.000 41.10030  ?  7086 VAL   A CG1    1 
ATOM   2278 C  CG2    . VAL   A  1  288 ? -74.39284  11.54020  8.17177   1.000 43.48697  ?  7086 VAL   A CG2    1 
ATOM   2279 N  N      . VAL   A  1  289 ? -74.13232  7.09775   9.74811   1.000 32.38526  ?  7087 VAL   A N      1 
ATOM   2280 C  CA     . VAL   A  1  289 ? -74.57767  5.84394   10.34357  1.000 35.37530  ?  7087 VAL   A CA     1 
ATOM   2281 C  C      . VAL   A  1  289 ? -74.51471  5.98550   11.85754  1.000 37.36932  ?  7087 VAL   A C      1 
ATOM   2282 O  O      . VAL   A  1  289 ? -73.50632  6.45167   12.40525  1.000 35.54541  ?  7087 VAL   A O      1 
ATOM   2283 C  CB     . VAL   A  1  289 ? -73.71694  4.64993   9.87818   1.000 37.28483  ?  7087 VAL   A CB     1 
ATOM   2284 C  CG1    . VAL   A  1  289 ? -74.25048  3.34942   10.48773  1.000 36.64353  ?  7087 VAL   A CG1    1 
ATOM   2285 C  CG2    . VAL   A  1  289 ? -73.70649  4.57228   8.35111   1.000 35.94641  ?  7087 VAL   A CG2    1 
ATOM   2286 N  N      . ILE   A  1  290 ? -75.59210  5.58843   12.52817  1.000 27.85072  ?  7088 ILE   A N      1 
ATOM   2287 C  CA     . ILE   A  1  290 ? -75.71736  5.71527   13.97015  1.000 32.76076  ?  7088 ILE   A CA     1 
ATOM   2288 C  C      . ILE   A  1  290 ? -76.22318  4.38851   14.50646  1.000 35.31711  ?  7088 ILE   A C      1 
ATOM   2289 O  O      . ILE   A  1  290 ? -76.74963  3.55999   13.76637  1.000 33.57685  ?  7088 ILE   A O      1 
ATOM   2290 C  CB     . ILE   A  1  290 ? -76.67968  6.85774   14.37195  1.000 30.97519  ?  7088 ILE   A CB     1 
ATOM   2291 C  CG1    . ILE   A  1  290 ? -78.10256  6.47931   13.95472  1.000 32.75442  ?  7088 ILE   A CG1    1 
ATOM   2292 C  CG2    . ILE   A  1  290 ? -76.25650  8.16345   13.69971  1.000 34.77468  ?  7088 ILE   A CG2    1 
ATOM   2293 C  CD1    . ILE   A  1  290 ? -79.14916  7.54797   14.16644  1.000 30.00170  ?  7088 ILE   A CD1    1 
ATOM   2294 N  N      . SER   A  1  291 ? -76.08358  4.20053   15.81297  1.000 32.45342  ?  7089 SER   A N      1 
ATOM   2295 C  CA     . SER   A  1  291 ? -76.66245  3.02054   16.43577  1.000 33.05311  ?  7089 SER   A CA     1 
ATOM   2296 C  C      . SER   A  1  291 ? -76.76318  3.26203   17.93352  1.000 36.01718  ?  7089 SER   A C      1 
ATOM   2297 O  O      . SER   A  1  291 ? -76.10711  4.14990   18.48446  1.000 32.47503  ?  7089 SER   A O      1 
ATOM   2298 C  CB     . SER   A  1  291 ? -75.81369  1.77961   16.14391  1.000 34.06609  ?  7089 SER   A CB     1 
ATOM   2299 O  OG     . SER   A  1  291 ? -74.54691  1.92019   16.74822  1.000 35.28831  ?  7089 SER   A OG     1 
ATOM   2300 N  N      . SER   A  1  292 ? -77.58619  2.45945   18.59126  1.000 33.66367  ?  7090 SER   A N      1 
ATOM   2301 C  CA     . SER   A  1  292 ? -77.68127  2.48558   20.04309  1.000 37.43508  ?  7090 SER   A CA     1 
ATOM   2302 C  C      . SER   A  1  292 ? -77.44924  1.08023   20.56688  1.000 35.37531  ?  7090 SER   A C      1 
ATOM   2303 O  O      . SER   A  1  292 ? -78.03692  0.11790   20.05432  1.000 37.09997  ?  7090 SER   A O      1 
ATOM   2304 C  CB     . SER   A  1  292 ? -79.04127  3.01123   20.52231  1.000 42.10143  ?  7090 SER   A CB     1 
ATOM   2305 O  OG     . SER   A  1  292 ? -80.07562  2.16499   20.07889  1.000 51.20885  ?  7090 SER   A OG     1 
ATOM   2306 N  N      . ASP   A  1  293 ? -76.58461  0.96727   21.57031  1.000 33.18278  ?  7091 ASP   A N      1 
ATOM   2307 C  CA     . ASP   A  1  293 ? -76.30948  -0.32725  22.17049  1.000 37.65146  ?  7091 ASP   A CA     1 
ATOM   2308 C  C      . ASP   A  1  293 ? -77.54004  -0.81584  22.91059  1.000 39.46085  ?  7091 ASP   A C      1 
ATOM   2309 O  O      . ASP   A  1  293 ? -78.23803  -0.03370  23.56071  1.000 39.09118  ?  7091 ASP   A O      1 
ATOM   2310 C  CB     . ASP   A  1  293 ? -75.13607  -0.23303  23.13732  1.000 40.49160  ?  7091 ASP   A CB     1 
ATOM   2311 C  CG     . ASP   A  1  293 ? -73.82793  0.04990   22.44303  1.000 45.84446  ?  7091 ASP   A CG     1 
ATOM   2312 O  OD1    . ASP   A  1  293 ? -73.73384  -0.13614  21.21429  1.000 45.85306  ?  7091 ASP   A OD1    1 
ATOM   2313 O  OD2    . ASP   A  1  293 ? -72.87598  0.44491   23.14454  1.000 55.22246  ?  7091 ASP   A OD2    1 
ATOM   2314 N  N      . VAL   A  1  294 ? -77.81587  -2.11208  22.80266  1.000 35.64169  ?  7092 VAL   A N      1 
ATOM   2315 C  CA     . VAL   A  1  294 ? -78.91618  -2.74007  23.52226  1.000 37.28490  ?  7092 VAL   A CA     1 
ATOM   2316 C  C      . VAL   A  1  294 ? -78.34696  -3.82967  24.41812  1.000 39.95982  ?  7092 VAL   A C      1 
ATOM   2317 O  O      . VAL   A  1  294 ? -77.62257  -4.71493  23.94686  1.000 37.61771  ?  7092 VAL   A O      1 
ATOM   2318 C  CB     . VAL   A  1  294 ? -79.97282  -3.31698  22.56687  1.000 38.71983  ?  7092 VAL   A CB     1 
ATOM   2319 C  CG1    . VAL   A  1  294 ? -81.06404  -4.02195  23.37159  1.000 35.77968  ?  7092 VAL   A CG1    1 
ATOM   2320 C  CG2    . VAL   A  1  294 ? -80.55890  -2.21053  21.71150  1.000 40.58242  ?  7092 VAL   A CG2    1 
ATOM   2321 N  N      . LEU   A  1  295 ? -78.66249  -3.74787  25.70635  1.000 37.19729  ?  7093 LEU   A N      1 
ATOM   2322 C  CA     . LEU   A  1  295 ? -78.27323  -4.76452  26.66681  1.000 42.13889  ?  7093 LEU   A CA     1 
ATOM   2323 C  C      . LEU   A  1  295 ? -79.24852  -5.93045  26.58187  1.000 40.02429  ?  7093 LEU   A C      1 
ATOM   2324 O  O      . LEU   A  1  295 ? -80.46243  -5.72941  26.61510  1.000 37.84290  ?  7093 LEU   A O      1 
ATOM   2325 C  CB     . LEU   A  1  295 ? -78.27063  -4.18164  28.07702  1.000 44.25480  ?  7093 LEU   A CB     1 
ATOM   2326 C  CG     . LEU   A  1  295 ? -77.91853  -5.16911  29.18637  1.000 45.02854  ?  7093 LEU   A CG     1 
ATOM   2327 C  CD1    . LEU   A  1  295 ? -76.44443  -5.52587  29.09867  1.000 44.45152  ?  7093 LEU   A CD1    1 
ATOM   2328 C  CD2    . LEU   A  1  295 ? -78.28315  -4.61437  30.56340  1.000 48.10701  ?  7093 LEU   A CD2    1 
ATOM   2329 N  N      . VAL   A  1  296 ? -78.72944  -7.14539  26.44943  1.000 34.12295  ?  7094 VAL   A N      1 
ATOM   2330 C  CA     . VAL   A  1  296 ? -79.57792  -8.32402  26.29197  1.000 39.82910  ?  7094 VAL   A CA     1 
ATOM   2331 C  C      . VAL   A  1  296 ? -79.65239  -9.06547  27.61737  1.000 42.54288  ?  7094 VAL   A C      1 
ATOM   2332 O  O      . VAL   A  1  296 ? -78.62157  -9.30785  28.25960  1.000 42.28591  ?  7094 VAL   A O      1 
ATOM   2333 C  CB     . VAL   A  1  296 ? -79.05553  -9.24965  25.18317  1.000 43.19086  ?  7094 VAL   A CB     1 
ATOM   2334 C  CG1    . VAL   A  1  296 ? -80.04188  -10.40731 24.95465  1.000 38.24515  ?  7094 VAL   A CG1    1 
ATOM   2335 C  CG2    . VAL   A  1  296 ? -78.81443  -8.45653  23.91917  1.000 40.32374  ?  7094 VAL   A CG2    1 
ATOM   2336 N  N      . ASN   A  1  297 ? -80.87171  -9.44843  28.00709  1.000 47.39035  ?  7095 ASN   A N      1 
ATOM   2337 C  CA     . ASN   A  1  297 ? -81.16384  -10.11569 29.26868  1.000 48.94566  ?  7095 ASN   A CA     1 
ATOM   2338 C  C      . ASN   A  1  297 ? -82.27548  -11.13352 29.07215  1.000 46.82392  ?  7095 ASN   A C      1 
ATOM   2339 O  O      . ASN   A  1  297 ? -83.28441  -10.83677 28.42583  1.000 41.36675  ?  7095 ASN   A O      1 
ATOM   2340 C  CB     . ASN   A  1  297 ? -81.61023  -9.10848  30.33804  1.000 51.75389  ?  7095 ASN   A CB     1 
ATOM   2341 C  CG     . ASN   A  1  297 ? -80.45374  -8.54512  31.11076  1.000 64.44300  ?  7095 ASN   A CG     1 
ATOM   2342 O  OD1    . ASN   A  1  297 ? -79.54275  -9.28465  31.50238  1.000 70.79882  ?  7095 ASN   A OD1    1 
ATOM   2343 N  ND2    . ASN   A  1  297 ? -80.46801  -7.22761  31.33549  1.000 66.14937  ?  7095 ASN   A ND2    1 
ATOM   2344 N  N      . ASN   A  1  298 ? -82.11765  -12.31772 29.66496  1.000 47.28310  ?  7096 ASN   A N      1 
ATOM   2345 C  CA     . ASN   A  1  298 ? -83.20233  -13.29766 29.74138  1.000 47.14220  ?  7096 ASN   A CA     1 
ATOM   2346 C  C      . ASN   A  1  298 ? -83.53183  -13.51150 31.21829  1.000 48.96208  ?  7096 ASN   A C      1 
ATOM   2347 O  O      . ASN   A  1  298 ? -82.74197  -14.10786 31.95575  1.000 48.28374  ?  7096 ASN   A O      1 
ATOM   2348 C  CB     . ASN   A  1  298 ? -82.82614  -14.61489 29.04649  1.000 44.87734  ?  7096 ASN   A CB     1 
ATOM   2349 C  CG     . ASN   A  1  298 ? -83.99229  -15.59859 28.98808  1.000 41.00878  ?  7096 ASN   A CG     1 
ATOM   2350 O  OD1    . ASN   A  1  298 ? -85.00179  -15.41816 29.67367  1.000 42.81370  ?  7096 ASN   A OD1    1 
ATOM   2351 N  ND2    . ASN   A  1  298 ? -83.85861  -16.63901 28.17505  1.000 37.68225  ?  7096 ASN   A ND2    1 
ATOM   2352 N  N      . GLU   A  1  299 ? -84.69826  -13.03238 31.63935  1.000 53.82824  ?  7097 GLU   A N      1 
ATOM   2353 C  CA     . GLU   A  1  299 ? -85.12748  -13.01227 33.03562  1.000 60.31221  ?  7097 GLU   A CA     1 
ATOM   2354 C  C      . GLU   A  1  299 ? -85.96425  -14.22803 33.43675  1.000 60.61824  ?  7097 GLU   A C      1 
ATOM   2355 O  O      . GLU   A  1  299 ? -86.56345  -14.21821 34.51830  1.000 60.94396  ?  7097 GLU   A O      1 
ATOM   2356 C  CB     . GLU   A  1  299 ? -85.93155  -11.73611 33.30736  1.000 61.20884  ?  7097 GLU   A CB     1 
ATOM   2357 C  CG     . GLU   A  1  299 ? -87.28965  -11.67670 32.57813  1.000 61.70480  ?  7097 GLU   A CG     1 
ATOM   2358 C  CD     . GLU   A  1  299 ? -87.17659  -11.65493 31.04230  1.000 70.23958  ?  7097 GLU   A CD     1 
ATOM   2359 O  OE1    . GLU   A  1  299 ? -86.10731  -12.01823 30.49784  1.000 68.28542  ?  7097 GLU   A OE1    1 
ATOM   2360 O  OE2    . GLU   A  1  299 ? -88.16412  -11.27112 30.37431  1.000 75.83614  ?  7097 GLU   A OE2    1 
ATOM   2361 N  N      . ASN   A  1  300 ? -86.03530  -15.25548 32.59074  1.000 55.23018  ?  7098 ASN   A N      1 
ATOM   2362 C  CA     . ASN   A  1  300 ? -86.83171  -16.45121 32.87137  1.000 52.50961  ?  7098 ASN   A CA     1 
ATOM   2363 C  C      . ASN   A  1  300 ? -86.08489  -17.39769 33.80553  1.000 49.70636  ?  7098 ASN   A C      1 
ATOM   2364 O  O      . ASN   A  1  300 ? -84.86620  -17.54791 33.68927  1.000 53.39537  ?  7098 ASN   A O      1 
ATOM   2365 C  CB     . ASN   A  1  300 ? -87.20068  -17.17807 31.56739  1.000 46.31249  ?  7098 ASN   A CB     1 
ATOM   2366 C  CG     . ASN   A  1  300 ? -88.14077  -16.36344 30.68346  1.000 53.01191  ?  7098 ASN   A CG     1 
ATOM   2367 O  OD1    . ASN   A  1  300 ? -89.34123  -16.27458 30.94072  1.000 54.95487  ?  7098 ASN   A OD1    1 
ATOM   2368 N  ND2    . ASN   A  1  300 ? -87.59376  -15.77146 29.63125  1.000 50.13773  ?  7098 ASN   A ND2    1 
ATOM   2369 N  N      . ALA   B  2  19  ? -106.67773 -10.91423 7.86912   1.000 67.41551  ?  4270 ALA   B N      1 
ATOM   2370 C  CA     . ALA   B  2  19  ? -108.05077 -10.42528 7.76646   1.000 71.71368  ?  4270 ALA   B CA     1 
ATOM   2371 C  C      . ALA   B  2  19  ? -108.32924 -9.33643  8.80465   1.000 70.15777  ?  4270 ALA   B C      1 
ATOM   2372 O  O      . ALA   B  2  19  ? -108.87911 -8.28662  8.46972   1.000 75.57601  ?  4270 ALA   B O      1 
ATOM   2373 C  CB     . ALA   B  2  19  ? -109.04396 -11.57610 7.91733   1.000 67.40254  ?  4270 ALA   B CB     1 
ATOM   2374 N  N      . PHE   B  2  20  ? -107.94466 -9.58024  10.05901  1.000 68.61112  ?  4271 PHE   B N      1 
ATOM   2375 C  CA     . PHE   B  2  20  ? -108.13088 -8.58670  11.10931  1.000 66.95771  ?  4271 PHE   B CA     1 
ATOM   2376 C  C      . PHE   B  2  20  ? -107.00003 -7.56564  11.11705  1.000 69.51739  ?  4271 PHE   B C      1 
ATOM   2377 O  O      . PHE   B  2  20  ? -105.82426 -7.90696  10.94396  1.000 67.63768  ?  4271 PHE   B O      1 
ATOM   2378 C  CB     . PHE   B  2  20  ? -108.21726 -9.23732  12.48982  1.000 59.07741  ?  4271 PHE   B CB     1 
ATOM   2379 C  CG     . PHE   B  2  20  ? -108.20277 -8.23920  13.62807  1.000 57.85952  ?  4271 PHE   B CG     1 
ATOM   2380 C  CD1    . PHE   B  2  20  ? -109.35482 -7.56244  13.99405  1.000 55.69155  ?  4271 PHE   B CD1    1 
ATOM   2381 C  CD2    . PHE   B  2  20  ? -107.03484 -7.96836  14.32134  1.000 54.25885  ?  4271 PHE   B CD2    1 
ATOM   2382 C  CE1    . PHE   B  2  20  ? -109.34071 -6.64090  15.04165  1.000 54.32053  ?  4271 PHE   B CE1    1 
ATOM   2383 C  CE2    . PHE   B  2  20  ? -107.01882 -7.04935  15.37049  1.000 55.18651  ?  4271 PHE   B CE2    1 
ATOM   2384 C  CZ     . PHE   B  2  20  ? -108.17621 -6.38720  15.72714  1.000 51.23867  ?  4271 PHE   B CZ     1 
ATOM   2385 N  N      . ALA   B  2  21  ? -107.37580 -6.30781  11.34689  1.000 67.32669  ?  4272 ALA   B N      1 
ATOM   2386 C  CA     . ALA   B  2  21  ? -106.44655 -5.19445  11.48108  1.000 61.98222  ?  4272 ALA   B CA     1 
ATOM   2387 C  C      . ALA   B  2  21  ? -107.17418 -4.09048  12.22936  1.000 63.61310  ?  4272 ALA   B C      1 
ATOM   2388 O  O      . ALA   B  2  21  ? -108.31919 -3.77409  11.89187  1.000 63.08467  ?  4272 ALA   B O      1 
ATOM   2389 C  CB     . ALA   B  2  21  ? -105.97345 -4.69819  10.11227  1.000 62.27480  ?  4272 ALA   B CB     1 
ATOM   2390 N  N      . VAL   B  2  22  ? -106.53204 -3.52785  13.25727  1.000 61.03253  ?  4273 VAL   B N      1 
ATOM   2391 C  CA     . VAL   B  2  22  ? -107.16578 -2.44271  13.99332  1.000 66.69220  ?  4273 VAL   B CA     1 
ATOM   2392 C  C      . VAL   B  2  22  ? -107.40187 -1.28232  13.03827  1.000 66.80479  ?  4273 VAL   B C      1 
ATOM   2393 O  O      . VAL   B  2  22  ? -106.55025 -0.96338  12.19726  1.000 66.69269  ?  4273 VAL   B O      1 
ATOM   2394 C  CB     . VAL   B  2  22  ? -106.30716 -2.01126  15.19383  1.000 62.27089  ?  4273 VAL   B CB     1 
ATOM   2395 C  CG1    . VAL   B  2  22  ? -105.91002 -3.21980  16.02115  1.000 60.02887  ?  4273 VAL   B CG1    1 
ATOM   2396 C  CG2    . VAL   B  2  22  ? -105.07804 -1.23821  14.72021  1.000 63.27940  ?  4273 VAL   B CG2    1 
ATOM   2397 N  N      . ASP   B  2  23  ? -108.57665 -0.66184  13.13783  1.000 61.29716  ?  4274 ASP   B N      1 
ATOM   2398 C  CA     . ASP   B  2  23  ? -108.89638 0.51066   12.32087  1.000 63.02937  ?  4274 ASP   B CA     1 
ATOM   2399 C  C      . ASP   B  2  23  ? -108.80773 1.73782   13.22521  1.000 59.64568  ?  4274 ASP   B C      1 
ATOM   2400 O  O      . ASP   B  2  23  ? -109.79208 2.16292   13.83210  1.000 57.95437  ?  4274 ASP   B O      1 
ATOM   2401 C  CB     . ASP   B  2  23  ? -110.26693 0.38087   11.66597  1.000 59.90293  ?  4274 ASP   B CB     1 
ATOM   2402 C  CG     . ASP   B  2  23  ? -110.48367 1.41329   10.56048  1.000 65.97442  ?  4274 ASP   B CG     1 
ATOM   2403 O  OD1    . ASP   B  2  23  ? -109.76322 2.43839   10.54552  1.000 59.89682  ?  4274 ASP   B OD1    1 
ATOM   2404 O  OD2    . ASP   B  2  23  ? -111.36966 1.20142   9.70463   1.000 73.23198  ?  4274 ASP   B OD2    1 
ATOM   2405 N  N      . ALA   B  2  24  ? -107.60501 2.31202   13.31500  1.000 57.03170  ?  4275 ALA   B N      1 
ATOM   2406 C  CA     . ALA   B  2  24  ? -107.40262 3.46513   14.18775  1.000 57.45041  ?  4275 ALA   B CA     1 
ATOM   2407 C  C      . ALA   B  2  24  ? -108.15435 4.68860   13.67370  1.000 52.85413  ?  4275 ALA   B C      1 
ATOM   2408 O  O      . ALA   B  2  24  ? -108.80505 5.39791   14.45164  1.000 50.39197  ?  4275 ALA   B O      1 
ATOM   2409 C  CB     . ALA   B  2  24  ? -105.91093 3.76843   14.32123  1.000 50.31830  ?  4275 ALA   B CB     1 
ATOM   2410 N  N      . ALA   B  2  25  ? -108.07012 4.95331   12.36434  1.000 52.09581  ?  4276 ALA   B N      1 
ATOM   2411 C  CA     . ALA   B  2  25  ? -108.79624 6.07535   11.77930  1.000 52.51544  ?  4276 ALA   B CA     1 
ATOM   2412 C  C      . ALA   B  2  25  ? -110.26136 6.05172   12.19766  1.000 54.52437  ?  4276 ALA   B C      1 
ATOM   2413 O  O      . ALA   B  2  25  ? -110.79688 7.04278   12.71060  1.000 47.26306  ?  4276 ALA   B O      1 
ATOM   2414 C  CB     . ALA   B  2  25  ? -108.66127 6.04223   10.25538  1.000 55.07728  ?  4276 ALA   B CB     1 
ATOM   2415 N  N      . LYS   B  2  26  ? -110.91621 4.90375   12.02723  1.000 56.05158  ?  4277 LYS   B N      1 
ATOM   2416 C  CA     . LYS   B  2  26  ? -112.33239 4.81574   12.35928  1.000 51.99404  ?  4277 LYS   B CA     1 
ATOM   2417 C  C      . LYS   B  2  26  ? -112.56102 4.98593   13.85718  1.000 50.94022  ?  4277 LYS   B C      1 
ATOM   2418 O  O      . LYS   B  2  26  ? -113.52649 5.63718   14.27520  1.000 50.02807  ?  4277 LYS   B O      1 
ATOM   2419 C  CB     . LYS   B  2  26  ? -112.89281 3.48398   11.85433  1.000 54.55504  ?  4277 LYS   B CB     1 
ATOM   2420 C  CG     . LYS   B  2  26  ? -114.39270 3.33877   12.00099  1.000 62.47197  ?  4277 LYS   B CG     1 
ATOM   2421 C  CD     . LYS   B  2  26  ? -114.93605 2.29636   11.02234  1.000 67.74053  ?  4277 LYS   B CD     1 
ATOM   2422 C  CE     . LYS   B  2  26  ? -116.20406 1.64705   11.55263  1.000 69.15964  ?  4277 LYS   B CE     1 
ATOM   2423 N  NZ     . LYS   B  2  26  ? -115.92532 0.84063   12.78167  1.000 76.95399  ?  4277 LYS   B NZ     1 
ATOM   2424 N  N      . ALA   B  2  27  ? -111.67111 4.42964   14.68393  1.000 51.64832  ?  4278 ALA   B N      1 
ATOM   2425 C  CA     . ALA   B  2  27  ? -111.84484 4.53657   16.13002  1.000 49.44777  ?  4278 ALA   B CA     1 
ATOM   2426 C  C      . ALA   B  2  27  ? -111.77210 5.98580   16.59013  1.000 52.23679  ?  4278 ALA   B C      1 
ATOM   2427 O  O      . ALA   B  2  27  ? -112.52706 6.40407   17.48022  1.000 50.90874  ?  4278 ALA   B O      1 
ATOM   2428 C  CB     . ALA   B  2  27  ? -110.79130 3.69805   16.85302  1.000 48.38698  ?  4278 ALA   B CB     1 
ATOM   2429 N  N      . TYR   B  2  28  ? -110.86251 6.77111   16.00598  1.000 49.75795  ?  4279 TYR   B N      1 
ATOM   2430 C  CA     . TYR   B  2  28  ? -110.73052 8.15422   16.45661  1.000 50.50415  ?  4279 TYR   B CA     1 
ATOM   2431 C  C      . TYR   B  2  28  ? -111.95502 8.96424   16.05287  1.000 48.07656  ?  4279 TYR   B C      1 
ATOM   2432 O  O      . TYR   B  2  28  ? -112.50390 9.71485   16.87031  1.000 46.37821  ?  4279 TYR   B O      1 
ATOM   2433 C  CB     . TYR   B  2  28  ? -109.43772 8.77881   15.91685  1.000 46.68991  ?  4279 TYR   B CB     1 
ATOM   2434 C  CG     . TYR   B  2  28  ? -109.12830 10.16157  16.49634  1.000 48.68782  ?  4279 TYR   B CG     1 
ATOM   2435 C  CD1    . TYR   B  2  28  ? -108.98291 10.35326  17.86624  1.000 46.30165  ?  4279 TYR   B CD1    1 
ATOM   2436 C  CD2    . TYR   B  2  28  ? -108.97441 11.26945  15.66742  1.000 48.62004  ?  4279 TYR   B CD2    1 
ATOM   2437 C  CE1    . TYR   B  2  28  ? -108.69541 11.62298  18.39900  1.000 48.56496  ?  4279 TYR   B CE1    1 
ATOM   2438 C  CE2    . TYR   B  2  28  ? -108.69039 12.53829  16.19043  1.000 46.94627  ?  4279 TYR   B CE2    1 
ATOM   2439 C  CZ     . TYR   B  2  28  ? -108.55144 12.70833  17.55314  1.000 45.51411  ?  4279 TYR   B CZ     1 
ATOM   2440 O  OH     . TYR   B  2  28  ? -108.27356 13.96873  18.06316  1.000 45.02859  ?  4279 TYR   B OH     1 
ATOM   2441 N  N      . LYS   B  2  29  ? -112.43597 8.77707   14.81638  1.000 50.98164  ?  4280 LYS   B N      1 
ATOM   2442 C  CA     . LYS   B  2  29  ? -113.65132 9.46986   14.38214  1.000 53.21976  ?  4280 LYS   B CA     1 
ATOM   2443 C  C      . LYS   B  2  29  ? -114.83154 9.16046   15.29847  1.000 52.89766  ?  4280 LYS   B C      1 
ATOM   2444 O  O      . LYS   B  2  29  ? -115.58504 10.06619  15.67371  1.000 54.60835  ?  4280 LYS   B O      1 
ATOM   2445 C  CB     . LYS   B  2  29  ? -113.97352 9.11512   12.92966  1.000 50.59585  ?  4280 LYS   B CB     1 
ATOM   2446 C  CG     . LYS   B  2  29  ? -112.91114 9.60910   11.95043  1.000 53.11437  ?  4280 LYS   B CG     1 
ATOM   2447 C  CD     . LYS   B  2  29  ? -113.16633 9.17742   10.50958  1.000 53.38245  ?  4280 LYS   B CD     1 
ATOM   2448 C  CE     . LYS   B  2  29  ? -111.84694 9.10904   9.73498   1.000 56.26628  ?  4280 LYS   B CE     1 
ATOM   2449 N  NZ     . LYS   B  2  29  ? -112.02076 9.03331   8.25017   1.000 55.43707  ?  4280 LYS   B NZ     1 
ATOM   2450 N  N      . ASP   B  2  30  ? -114.99910 7.89546   15.69753  1.000 56.39674  ?  4281 ASP   B N      1 
ATOM   2451 C  CA     . ASP   B  2  30  ? -116.12771 7.56098   16.56876  1.000 56.17322  ?  4281 ASP   B CA     1 
ATOM   2452 C  C      . ASP   B  2  30  ? -115.93493 8.14179   17.96272  1.000 55.00530  ?  4281 ASP   B C      1 
ATOM   2453 O  O      . ASP   B  2  30  ? -116.88380 8.66127   18.56436  1.000 56.48087  ?  4281 ASP   B O      1 
ATOM   2454 C  CB     . ASP   B  2  30  ? -116.32510 6.04370   16.64292  1.000 58.81770  ?  4281 ASP   B CB     1 
ATOM   2455 C  CG     . ASP   B  2  30  ? -116.69666 5.43426   15.29895  1.000 62.77936  ?  4281 ASP   B CG     1 
ATOM   2456 O  OD1    . ASP   B  2  30  ? -117.13049 6.18725   14.39578  1.000 63.36119  ?  4281 ASP   B OD1    1 
ATOM   2457 O  OD2    . ASP   B  2  30  ? -116.55154 4.20026   15.14370  1.000 68.82393  ?  4281 ASP   B OD2    1 
ATOM   2458 N  N      . TYR   B  2  31  ? -114.71273 8.06105   18.49287  1.000 54.36573  ?  4282 TYR   B N      1 
ATOM   2459 C  CA     . TYR   B  2  31  ? -114.41609 8.70599   19.76572  1.000 53.32032  ?  4282 TYR   B CA     1 
ATOM   2460 C  C      . TYR   B  2  31  ? -114.74899 10.19497  19.70979  1.000 55.48228  ?  4282 TYR   B C      1 
ATOM   2461 O  O      . TYR   B  2  31  ? -115.33584 10.74387  20.64815  1.000 57.83351  ?  4282 TYR   B O      1 
ATOM   2462 C  CB     . TYR   B  2  31  ? -112.94436 8.46220   20.12205  1.000 54.79019  ?  4282 TYR   B CB     1 
ATOM   2463 C  CG     . TYR   B  2  31  ? -112.35328 9.36413   21.18547  1.000 54.13682  ?  4282 TYR   B CG     1 
ATOM   2464 C  CD1    . TYR   B  2  31  ? -111.65933 10.51715  20.83140  1.000 57.04235  ?  4282 TYR   B CD1    1 
ATOM   2465 C  CD2    . TYR   B  2  31  ? -112.46089 9.05482   22.53530  1.000 53.24395  ?  4282 TYR   B CD2    1 
ATOM   2466 C  CE1    . TYR   B  2  31  ? -111.10280 11.34969  21.78900  1.000 56.41377  ?  4282 TYR   B CE1    1 
ATOM   2467 C  CE2    . TYR   B  2  31  ? -111.90462 9.88033   23.50435  1.000 57.42820  ?  4282 TYR   B CE2    1 
ATOM   2468 C  CZ     . TYR   B  2  31  ? -111.22320 11.03098  23.12001  1.000 60.66961  ?  4282 TYR   B CZ     1 
ATOM   2469 O  OH     . TYR   B  2  31  ? -110.65637 11.87091  24.05666  1.000 56.72982  ?  4282 TYR   B OH     1 
ATOM   2470 N  N      . LEU   B  2  32  ? -114.39448 10.86373  18.60957  1.000 55.26024  ?  4283 LEU   B N      1 
ATOM   2471 C  CA     . LEU   B  2  32  ? -114.71361 12.28213  18.47306  1.000 55.03070  ?  4283 LEU   B CA     1 
ATOM   2472 C  C      . LEU   B  2  32  ? -116.22023 12.50031  18.41317  1.000 59.47852  ?  4283 LEU   B C      1 
ATOM   2473 O  O      . LEU   B  2  32  ? -116.76169 13.36671  19.11156  1.000 52.56156  ?  4283 LEU   B O      1 
ATOM   2474 C  CB     . LEU   B  2  32  ? -114.04633 12.85277  17.22259  1.000 48.86983  ?  4283 LEU   B CB     1 
ATOM   2475 C  CG     . LEU   B  2  32  ? -112.53681 13.08896  17.28149  1.000 51.26855  ?  4283 LEU   B CG     1 
ATOM   2476 C  CD1    . LEU   B  2  32  ? -112.03342 13.54295  15.91764  1.000 46.15400  ?  4283 LEU   B CD1    1 
ATOM   2477 C  CD2    . LEU   B  2  32  ? -112.21024 14.11145  18.35884  1.000 48.26013  ?  4283 LEU   B CD2    1 
ATOM   2478 N  N      . ALA   B  2  33  ? -116.91266 11.71658  17.57731  1.000 57.01449  ?  4284 ALA   B N      1 
ATOM   2479 C  CA     . ALA   B  2  33  ? -118.35336 11.89159  17.39790  1.000 59.20831  ?  4284 ALA   B CA     1 
ATOM   2480 C  C      . ALA   B  2  33  ? -119.11167 11.74644  18.70989  1.000 60.64987  ?  4284 ALA   B C      1 
ATOM   2481 O  O      . ALA   B  2  33  ? -120.12009 12.42673  18.92135  1.000 64.31196  ?  4284 ALA   B O      1 
ATOM   2482 C  CB     . ALA   B  2  33  ? -118.87973 10.89329  16.36865  1.000 53.84580  ?  4284 ALA   B CB     1 
ATOM   2483 N  N      . SER   B  2  34  ? -118.64799 10.87636  19.60238  1.000 61.53936  ?  4285 SER   B N      1 
ATOM   2484 C  CA     . SER   B  2  34  ? -119.28912 10.68221  20.89340  1.000 61.27409  ?  4285 SER   B CA     1 
ATOM   2485 C  C      . SER   B  2  34  ? -118.80341 11.67159  21.95161  1.000 60.56694  ?  4285 SER   B C      1 
ATOM   2486 O  O      . SER   B  2  34  ? -118.99252 11.42434  23.14809  1.000 63.21022  ?  4285 SER   B O      1 
ATOM   2487 C  CB     . SER   B  2  34  ? -119.06877 9.24684   21.37737  1.000 62.26111  ?  4285 SER   B CB     1 
ATOM   2488 O  OG     . SER   B  2  34  ? -117.90121 9.15811   22.17713  1.000 69.00831  ?  4285 SER   B OG     1 
ATOM   2489 N  N      . GLY   B  2  35  ? -118.16694 12.76838  21.54431  1.000 64.88036  ?  4286 GLY   B N      1 
ATOM   2490 C  CA     . GLY   B  2  35  ? -117.77804 13.80686  22.48036  1.000 62.11417  ?  4286 GLY   B CA     1 
ATOM   2491 C  C      . GLY   B  2  35  ? -116.43190 13.64263  23.15358  1.000 62.66837  ?  4286 GLY   B C      1 
ATOM   2492 O  O      . GLY   B  2  35  ? -116.24397 14.15339  24.26502  1.000 65.68944  ?  4286 GLY   B O      1 
ATOM   2493 N  N      . GLY   B  2  36  ? -115.48171 12.95818  22.52060  1.000 57.92209  ?  4287 GLY   B N      1 
ATOM   2494 C  CA     . GLY   B  2  36  ? -114.16583 12.80128  23.11959  1.000 59.49596  ?  4287 GLY   B CA     1 
ATOM   2495 C  C      . GLY   B  2  36  ? -113.28245 14.02289  22.91623  1.000 57.83528  ?  4287 GLY   B C      1 
ATOM   2496 O  O      . GLY   B  2  36  ? -113.40439 14.75796  21.93599  1.000 53.09728  ?  4287 GLY   B O      1 
ATOM   2497 N  N      . GLN   B  2  37  ? -112.38266 14.24049  23.87184  1.000 58.61711  ?  4288 GLN   B N      1 
ATOM   2498 C  CA     . GLN   B  2  37  ? -111.43011 15.34657  23.77137  1.000 56.49486  ?  4288 GLN   B CA     1 
ATOM   2499 C  C      . GLN   B  2  37  ? -110.41701 15.06556  22.66556  1.000 53.09792  ?  4288 GLN   B C      1 
ATOM   2500 O  O      . GLN   B  2  37  ? -109.80393 13.99403  22.65238  1.000 48.79717  ?  4288 GLN   B O      1 
ATOM   2501 C  CB     . GLN   B  2  37  ? -110.71093 15.54664  25.10453  1.000 62.66824  ?  4288 GLN   B CB     1 
ATOM   2502 C  CG     . GLN   B  2  37  ? -111.38629 16.53949  26.04933  1.000 73.61323  ?  4288 GLN   B CG     1 
ATOM   2503 C  CD     . GLN   B  2  37  ? -110.91318 17.97860  25.83490  1.000 85.80894  ?  4288 GLN   B CD     1 
ATOM   2504 O  OE1    . GLN   B  2  37  ? -109.85882 18.22183  25.23069  1.000 81.78438  ?  4288 GLN   B OE1    1 
ATOM   2505 N  NE2    . GLN   B  2  37  ? -111.69633 18.93860  26.32941  1.000 85.82050  ?  4288 GLN   B NE2    1 
ATOM   2506 N  N      . PRO   B  2  38  ? -110.20953 15.98525  21.72600  1.000 49.26857  ?  4289 PRO   B N      1 
ATOM   2507 C  CA     . PRO   B  2  38  ? -109.23227 15.72549  20.65984  1.000 46.11785  ?  4289 PRO   B CA     1 
ATOM   2508 C  C      . PRO   B  2  38  ? -107.82474 15.53817  21.22264  1.000 43.48068  ?  4289 PRO   B C      1 
ATOM   2509 O  O      . PRO   B  2  38  ? -107.48696 16.00313  22.31225  1.000 41.77738  ?  4289 PRO   B O      1 
ATOM   2510 C  CB     . PRO   B  2  38  ? -109.32579 16.97542  19.77418  1.000 44.05754  ?  4289 PRO   B CB     1 
ATOM   2511 C  CG     . PRO   B  2  38  ? -110.68019 17.57551  20.09703  1.000 45.46731  ?  4289 PRO   B CG     1 
ATOM   2512 C  CD     . PRO   B  2  38  ? -110.90931 17.26991  21.54905  1.000 48.29635  ?  4289 PRO   B CD     1 
ATOM   2513 N  N      . ILE   B  2  39  ? -107.00101 14.81934  20.46419  1.000 38.06227  ?  4290 ILE   B N      1 
ATOM   2514 C  CA     . ILE   B  2  39  ? -105.60899 14.61864  20.84874  1.000 39.55117  ?  4290 ILE   B CA     1 
ATOM   2515 C  C      . ILE   B  2  39  ? -104.91955 15.96909  20.99548  1.000 43.04370  ?  4290 ILE   B C      1 
ATOM   2516 O  O      . ILE   B  2  39  ? -105.04183 16.84607  20.13110  1.000 38.39524  ?  4290 ILE   B O      1 
ATOM   2517 C  CB     . ILE   B  2  39  ? -104.90517 13.73742  19.80756  1.000 41.66883  ?  4290 ILE   B CB     1 
ATOM   2518 C  CG1    . ILE   B  2  39  ? -105.41891 12.30111  19.90658  1.000 44.57791  ?  4290 ILE   B CG1    1 
ATOM   2519 C  CG2    . ILE   B  2  39  ? -103.37565 13.78380  19.97514  1.000 42.07281  ?  4290 ILE   B CG2    1 
ATOM   2520 C  CD1    . ILE   B  2  39  ? -105.06534 11.48777  18.70642  1.000 41.55835  ?  4290 ILE   B CD1    1 
ATOM   2521 N  N      . THR   B  2  40  ? -104.17894 16.13610  22.08175  1.000 41.10606  ?  4291 THR   B N      1 
ATOM   2522 C  CA     . THR   B  2  40  ? -103.52396 17.39313  22.41428  1.000 39.97163  ?  4291 THR   B CA     1 
ATOM   2523 C  C      . THR   B  2  40  ? -102.01066 17.29211  22.19854  1.000 38.43209  ?  4291 THR   B C      1 
ATOM   2524 O  O      . THR   B  2  40  ? -101.46918 16.26168  21.77604  1.000 36.31999  ?  4291 THR   B O      1 
ATOM   2525 C  CB     . THR   B  2  40  ? -103.83806 17.77911  23.86074  1.000 44.44093  ?  4291 THR   B CB     1 
ATOM   2526 O  OG1    . THR   B  2  40  ? -103.46747 16.69842  24.73186  1.000 48.85133  ?  4291 THR   B OG1    1 
ATOM   2527 C  CG2    . THR   B  2  40  ? -105.31729 18.05552  24.03204  1.000 48.04073  ?  4291 THR   B CG2    1 
ATOM   2528 N  N      . ASN   B  2  41  ? -101.32973 18.39461  22.49881  1.000 33.69770  ?  4292 ASN   B N      1 
ATOM   2529 C  CA     . ASN   B  2  41  ? -99.87649  18.50419  22.44897  1.000 36.15654  ?  4292 ASN   B CA     1 
ATOM   2530 C  C      . ASN   B  2  41  ? -99.33203  18.36345  21.03946  1.000 33.84465  ?  4292 ASN   B C      1 
ATOM   2531 O  O      . ASN   B  2  41  ? -98.15841  18.03004  20.84926  1.000 35.20579  ?  4292 ASN   B O      1 
ATOM   2532 C  CB     . ASN   B  2  41  ? -99.22491  17.49864  23.40391  1.000 38.82991  ?  4292 ASN   B CB     1 
ATOM   2533 C  CG     . ASN   B  2  41  ? -99.48531  17.85627  24.86486  1.000 42.45124  ?  4292 ASN   B CG     1 
ATOM   2534 O  OD1    . ASN   B  2  41  ? -99.32549  19.00573  25.25489  1.000 47.06370  ?  4292 ASN   B OD1    1 
ATOM   2535 N  ND2    . ASN   B  2  41  ? -99.93440  16.89395  25.65636  1.000 43.33159  ?  4292 ASN   B ND2    1 
ATOM   2536 N  N      . CYS   B  2  42  ? -100.15014 18.63536  20.02941  1.000 32.34313  ?  4293 CYS   B N      1 
ATOM   2537 C  CA     . CYS   B  2  42  ? -99.58510  18.85783  18.70718  1.000 30.96036  ?  4293 CYS   B CA     1 
ATOM   2538 C  C      . CYS   B  2  42  ? -98.69343  20.09225  18.76499  1.000 29.10907  ?  4293 CYS   B C      1 
ATOM   2539 O  O      . CYS   B  2  42  ? -99.04158  21.08978  19.40131  1.000 30.69863  ?  4293 CYS   B O      1 
ATOM   2540 C  CB     . CYS   B  2  42  ? -100.69367 19.04198  17.68176  1.000 33.67021  ?  4293 CYS   B CB     1 
ATOM   2541 S  SG     . CYS   B  2  42  ? -101.81102 17.58057  17.61964  1.000 37.95544  ?  4293 CYS   B SG     1 
ATOM   2542 N  N      . VAL   B  2  43  ? -97.53316  20.01499  18.12386  1.000 28.20405  ?  4294 VAL   B N      1 
ATOM   2543 C  CA     . VAL   B  2  43  ? -96.47589  21.01347  18.29930  1.000 23.40688  ?  4294 VAL   B CA     1 
ATOM   2544 C  C      . VAL   B  2  43  ? -96.74546  22.16487  17.33307  1.000 27.84625  ?  4294 VAL   B C      1 
ATOM   2545 O  O      . VAL   B  2  43  ? -96.48659  22.05420  16.13623  1.000 30.22946  ?  4294 VAL   B O      1 
ATOM   2546 C  CB     . VAL   B  2  43  ? -95.09295  20.41455  18.06296  1.000 26.58926  ?  4294 VAL   B CB     1 
ATOM   2547 C  CG1    . VAL   B  2  43  ? -94.02167  21.52802  18.19917  1.000 29.12150  ?  4294 VAL   B CG1    1 
ATOM   2548 C  CG2    . VAL   B  2  43  ? -94.83479  19.24727  19.03123  1.000 29.75283  ?  4294 VAL   B CG2    1 
ATOM   2549 N  N      . LYS   B  2  44  ? -97.25273  23.28169  17.84978  1.000 28.37828  ?  4295 LYS   B N      1 
ATOM   2550 C  CA     . LYS   B  2  44  ? -97.53118  24.44738  17.01315  1.000 29.60997  ?  4295 LYS   B CA     1 
ATOM   2551 C  C      . LYS   B  2  44  ? -96.27274  25.30073  16.85296  1.000 30.19028  ?  4295 LYS   B C      1 
ATOM   2552 O  O      . LYS   B  2  44  ? -95.57945  25.58103  17.83683  1.000 31.73925  ?  4295 LYS   B O      1 
ATOM   2553 C  CB     . LYS   B  2  44  ? -98.66150  25.28145  17.61475  1.000 28.46819  ?  4295 LYS   B CB     1 
ATOM   2554 C  CG     . LYS   B  2  44  ? -99.14395  26.38545  16.66902  1.000 33.74385  ?  4295 LYS   B CG     1 
ATOM   2555 C  CD     . LYS   B  2  44  ? -100.56235 26.85783  17.03209  1.000 36.97291  ?  4295 LYS   B CD     1 
ATOM   2556 C  CE     . LYS   B  2  44  ? -100.52857 28.06547  17.92573  1.000 38.05504  ?  4295 LYS   B CE     1 
ATOM   2557 N  NZ     . LYS   B  2  44  ? -101.89255 28.68621  18.07815  1.000 37.58746  ?  4295 LYS   B NZ     1 
ATOM   2558 N  N      . MET   B  2  45  ? -95.97534  25.69577  15.61245  1.000 29.00179  ?  4296 MET   B N      1 
ATOM   2559 C  CA     . MET   B  2  45  ? -94.75679  26.41099  15.27146  1.000 25.93102  ?  4296 MET   B CA     1 
ATOM   2560 C  C      . MET   B  2  45  ? -94.98946  27.91590  15.26870  1.000 31.06095  ?  4296 MET   B C      1 
ATOM   2561 O  O      . MET   B  2  45  ? -96.09341  28.39068  14.99395  1.000 25.88977  ?  4296 MET   B O      1 
ATOM   2562 C  CB     . MET   B  2  45  ? -94.25466  25.98905  13.89535  1.000 26.11180  ?  4296 MET   B CB     1 
ATOM   2563 C  CG     . MET   B  2  45  ? -94.05056  24.47425  13.76118  1.000 31.33527  ?  4296 MET   B CG     1 
ATOM   2564 S  SD     . MET   B  2  45  ? -93.20242  23.56236  15.03158  1.000 30.97369  ?  4296 MET   B SD     1 
ATOM   2565 C  CE     . MET   B  2  45  ? -91.58198  24.42924  15.01252  1.000 24.85354  ?  4296 MET   B CE     1 
ATOM   2566 N  N      . LEU   B  2  46  ? -93.93539  28.66923  15.56759  1.000 30.93290  ?  4297 LEU   B N      1 
ATOM   2567 C  CA     . LEU   B  2  46  ? -93.96819  30.09946  15.30063  1.000 29.16801  ?  4297 LEU   B CA     1 
ATOM   2568 C  C      . LEU   B  2  46  ? -93.59684  30.33837  13.84392  1.000 34.13679  ?  4297 LEU   B C      1 
ATOM   2569 O  O      . LEU   B  2  46  ? -92.66041  29.72765  13.32135  1.000 33.37390  ?  4297 LEU   B O      1 
ATOM   2570 C  CB     . LEU   B  2  46  ? -93.00509  30.84294  16.22888  1.000 30.79164  ?  4297 LEU   B CB     1 
ATOM   2571 C  CG     . LEU   B  2  46  ? -93.43407  30.85776  17.69395  1.000 29.11725  ?  4297 LEU   B CG     1 
ATOM   2572 C  CD1    . LEU   B  2  46  ? -92.25427  31.04655  18.60821  1.000 28.23656  ?  4297 LEU   B CD1    1 
ATOM   2573 C  CD2    . LEU   B  2  46  ? -94.47002  31.96457  17.90525  1.000 30.09958  ?  4297 LEU   B CD2    1 
ATOM   2574 N  N      . CYS   B  2  47  ? -94.32991  31.22861  13.18016  1.000 29.94129  ?  4298 CYS   B N      1 
ATOM   2575 C  CA     . CYS   B  2  47  ? -94.02805  31.54807  11.78657  1.000 32.08848  ?  4298 CYS   B CA     1 
ATOM   2576 C  C      . CYS   B  2  47  ? -94.63747  32.91002  11.48372  1.000 33.01972  ?  4298 CYS   B C      1 
ATOM   2577 O  O      . CYS   B  2  47  ? -95.33603  33.49037  12.31835  1.000 32.18575  ?  4298 CYS   B O      1 
ATOM   2578 C  CB     . CYS   B  2  47  ? -94.55816  30.46728  10.83218  1.000 33.20677  ?  4298 CYS   B CB     1 
ATOM   2579 S  SG     . CYS   B  2  47  ? -96.33848  30.08354  11.10056  1.000 37.31771  ?  4298 CYS   B SG     1 
ATOM   2580 N  N      . THR   B  2  48  ? -94.39367  33.39705  10.26355  1.000 33.26434  ?  4299 THR   B N      1 
ATOM   2581 C  CA     . THR   B  2  48  ? -94.86551  34.72629  9.87721   1.000 39.03056  ?  4299 THR   B CA     1 
ATOM   2582 C  C      . THR   B  2  48  ? -96.35461  34.74258  9.57712   1.000 33.93510  ?  4299 THR   B C      1 
ATOM   2583 O  O      . THR   B  2  48  ? -96.99183  35.78960  9.69938   1.000 38.92102  ?  4299 THR   B O      1 
ATOM   2584 C  CB     . THR   B  2  48  ? -94.11152  35.20819  8.64805   1.000 34.79071  ?  4299 THR   B CB     1 
ATOM   2585 O  OG1    . THR   B  2  48  ? -94.28103  34.24842  7.59814   1.000 39.75804  ?  4299 THR   B OG1    1 
ATOM   2586 C  CG2    . THR   B  2  48  ? -92.61931  35.31214  8.95578   1.000 39.49692  ?  4299 THR   B CG2    1 
ATOM   2587 N  N      . HIS   B  2  49  ? -96.92371  33.59396  9.20061   1.000 36.90711  ?  4300 HIS   B N      1 
ATOM   2588 C  CA     . HIS   B  2  49  ? -98.29968  33.51782  8.72745   1.000 36.43277  ?  4300 HIS   B CA     1 
ATOM   2589 C  C      . HIS   B  2  49  ? -98.50136  34.30865  7.43680   1.000 41.55847  ?  4300 HIS   B C      1 
ATOM   2590 O  O      . HIS   B  2  49  ? -99.58180  34.85494  7.19710   1.000 39.90596  ?  4300 HIS   B O      1 
ATOM   2591 C  CB     . HIS   B  2  49  ? -99.25874  33.97943  9.81856   1.000 31.12340  ?  4300 HIS   B CB     1 
ATOM   2592 C  CG     . HIS   B  2  49  ? -99.28232  33.06013  10.99247  1.000 40.70580  ?  4300 HIS   B CG     1 
ATOM   2593 N  ND1    . HIS   B  2  49  ? -100.19635 32.03427  11.11120  1.000 37.14040  ?  4300 HIS   B ND1    1 
ATOM   2594 C  CD2    . HIS   B  2  49  ? -98.46359  32.96822  12.07125  1.000 39.55340  ?  4300 HIS   B CD2    1 
ATOM   2595 C  CE1    . HIS   B  2  49  ? -99.96184  31.37481  12.23340  1.000 40.16414  ?  4300 HIS   B CE1    1 
ATOM   2596 N  NE2    . HIS   B  2  49  ? -98.91569  31.92002  12.83311  1.000 37.18282  ?  4300 HIS   B NE2    1 
ATOM   2597 N  N      . THR   B  2  50  ? -97.45610  34.37121  6.60057   1.000 34.45190  ?  4301 THR   B N      1 
ATOM   2598 C  CA     . THR   B  2  50  ? -97.53074  34.95639  5.26997   1.000 40.86618  ?  4301 THR   B CA     1 
ATOM   2599 C  C      . THR   B  2  50  ? -97.04714  33.94954  4.23062   1.000 40.86640  ?  4301 THR   B C      1 
ATOM   2600 O  O      . THR   B  2  50  ? -96.48246  34.33376  3.20444   1.000 37.78714  ?  4301 THR   B O      1 
ATOM   2601 C  CB     . THR   B  2  50  ? -96.71941  36.25916  5.17366   1.000 40.24623  ?  4301 THR   B CB     1 
ATOM   2602 O  OG1    . THR   B  2  50  ? -95.34319  36.00018  5.47066   1.000 40.00188  ?  4301 THR   B OG1    1 
ATOM   2603 C  CG2    . THR   B  2  50  ? -97.24374  37.34011  6.14887   1.000 34.09945  ?  4301 THR   B CG2    1 
ATOM   2604 N  N      . GLY   B  2  51  ? -97.24483  32.64911  4.48981   1.000 39.11133  ?  4302 GLY   B N      1 
ATOM   2605 C  CA     . GLY   B  2  51  ? -96.73476  31.61562  3.61534   1.000 37.54459  ?  4302 GLY   B CA     1 
ATOM   2606 C  C      . GLY   B  2  51  ? -97.74738  31.18342  2.56562   1.000 43.24302  ?  4302 GLY   B C      1 
ATOM   2607 O  O      . GLY   B  2  51  ? -98.84897  31.71104  2.46784   1.000 43.14430  ?  4302 GLY   B O      1 
ATOM   2608 N  N      . THR   B  2  52  ? -97.35926  30.16832  1.78768   1.000 43.66126  ?  4303 THR   B N      1 
ATOM   2609 C  CA     . THR   B  2  52  ? -98.15512  29.74971  0.63512   1.000 41.17068  ?  4303 THR   B CA     1 
ATOM   2610 C  C      . THR   B  2  52  ? -99.51977  29.18937  1.01329   1.000 44.06004  ?  4303 THR   B C      1 
ATOM   2611 O  O      . THR   B  2  52  ? -100.42714 29.20340  0.17775   1.000 42.96680  ?  4303 THR   B O      1 
ATOM   2612 C  CB     . THR   B  2  52  ? -97.40188  28.70733  -0.18198  1.000 43.42136  ?  4303 THR   B CB     1 
ATOM   2613 O  OG1    . THR   B  2  52  ? -97.26853  27.50630  0.58731   1.000 48.17196  ?  4303 THR   B OG1    1 
ATOM   2614 C  CG2    . THR   B  2  52  ? -96.01721  29.22047  -0.56907  1.000 40.73030  ?  4303 THR   B CG2    1 
ATOM   2615 N  N      . GLY   B  2  53  ? -99.69309  28.69860  2.23809   1.000 41.46236  ?  4304 GLY   B N      1 
ATOM   2616 C  CA     . GLY   B  2  53  ? -100.94696 28.08204  2.63662   1.000 38.15808  ?  4304 GLY   B CA     1 
ATOM   2617 C  C      . GLY   B  2  53  ? -101.15525 26.65416  2.16512   1.000 38.44089  ?  4304 GLY   B C      1 
ATOM   2618 O  O      . GLY   B  2  53  ? -102.22248 26.08844  2.42303   1.000 39.77178  ?  4304 GLY   B O      1 
ATOM   2619 N  N      . GLN   B  2  54  ? -100.18130 26.04980  1.48844   1.000 38.18271  ?  4305 GLN   B N      1 
ATOM   2620 C  CA     . GLN   B  2  54  ? -100.30042 24.65200  1.09405   1.000 41.73566  ?  4305 GLN   B CA     1 
ATOM   2621 C  C      . GLN   B  2  54  ? -100.39509 23.73965  2.32061   1.000 43.86824  ?  4305 GLN   B C      1 
ATOM   2622 O  O      . GLN   B  2  54  ? -100.00443 24.10286  3.43120   1.000 37.16984  ?  4305 GLN   B O      1 
ATOM   2623 C  CB     . GLN   B  2  54  ? -99.10884  24.23560  0.24593   1.000 43.27151  ?  4305 GLN   B CB     1 
ATOM   2624 C  CG     . GLN   B  2  54  ? -98.85337  25.12042  -0.93095  1.000 49.82489  ?  4305 GLN   B CG     1 
ATOM   2625 C  CD     . GLN   B  2  54  ? -98.00274  24.42608  -1.95628  1.000 54.79321  ?  4305 GLN   B CD     1 
ATOM   2626 O  OE1    . GLN   B  2  54  ? -98.51737  23.69985  -2.80761  1.000 59.25091  ?  4305 GLN   B OE1    1 
ATOM   2627 N  NE2    . GLN   B  2  54  ? -96.68908  24.60656  -1.86171  1.000 56.82069  ?  4305 GLN   B NE2    1 
ATOM   2628 N  N      . ALA   B  2  55  ? -100.89595 22.52366  2.09804   1.000 37.93666  ?  4306 ALA   B N      1 
ATOM   2629 C  CA     . ALA   B  2  55  ? -101.29254 21.66613  3.21277   1.000 39.68740  ?  4306 ALA   B CA     1 
ATOM   2630 C  C      . ALA   B  2  55  ? -100.09129 21.12607  3.97968   1.000 36.03783  ?  4306 ALA   B C      1 
ATOM   2631 O  O      . ALA   B  2  55  ? -100.05089 21.20665  5.20956   1.000 38.03449  ?  4306 ALA   B O      1 
ATOM   2632 C  CB     . ALA   B  2  55  ? -102.14619 20.50841  2.70527   1.000 40.62353  ?  4306 ALA   B CB     1 
ATOM   2633 N  N      . ILE   B  2  56  ? -99.11414  20.55849  3.27647   1.000 38.35086  ?  4307 ILE   B N      1 
ATOM   2634 C  CA     . ILE   B  2  56  ? -98.02625  19.79958  3.88733   1.000 38.99749  ?  4307 ILE   B CA     1 
ATOM   2635 C  C      . ILE   B  2  56  ? -96.73762  20.23402  3.21780   1.000 40.69172  ?  4307 ILE   B C      1 
ATOM   2636 O  O      . ILE   B  2  56  ? -96.58089  20.05267  2.00445   1.000 40.29104  ?  4307 ILE   B O      1 
ATOM   2637 C  CB     . ILE   B  2  56  ? -98.22180  18.28104  3.72243   1.000 38.45338  ?  4307 ILE   B CB     1 
ATOM   2638 C  CG1    . ILE   B  2  56  ? -99.53821  17.84621  4.37253   1.000 39.64240  ?  4307 ILE   B CG1    1 
ATOM   2639 C  CG2    . ILE   B  2  56  ? -97.03084  17.51903  4.29303   1.000 35.88970  ?  4307 ILE   B CG2    1 
ATOM   2640 C  CD1    . ILE   B  2  56  ? -99.89134  16.37578  4.11147   1.000 40.26786  ?  4307 ILE   B CD1    1 
ATOM   2641 N  N      . THR   B  2  57  ? -95.81071  20.79753  3.99422   1.000 35.07666  ?  4308 THR   B N      1 
ATOM   2642 C  CA     . THR   B  2  57  ? -94.66243  21.46124  3.39694   1.000 35.31753  ?  4308 THR   B CA     1 
ATOM   2643 C  C      . THR   B  2  57  ? -93.39785  21.14689  4.18119   1.000 33.57703  ?  4308 THR   B C      1 
ATOM   2644 O  O      . THR   B  2  57  ? -93.44685  20.69170  5.32251   1.000 36.92600  ?  4308 THR   B O      1 
ATOM   2645 C  CB     . THR   B  2  57  ? -94.88440  22.97596  3.33248   1.000 38.89043  ?  4308 THR   B CB     1 
ATOM   2646 O  OG1    . THR   B  2  57  ? -95.22971  23.45745  4.63820   1.000 31.45767  ?  4308 THR   B OG1    1 
ATOM   2647 C  CG2    . THR   B  2  57  ? -96.03555  23.30805  2.35247   1.000 39.83877  ?  4308 THR   B CG2    1 
ATOM   2648 N  N      . VAL   B  2  58  ? -92.24747  21.41636  3.55596   1.000 35.24880  ?  4309 VAL   B N      1 
ATOM   2649 C  CA     . VAL   B  2  58  ? -90.97148  21.12483  4.20757   1.000 36.89220  ?  4309 VAL   B CA     1 
ATOM   2650 C  C      . VAL   B  2  58  ? -90.60335  22.14032  5.27640   1.000 37.86615  ?  4309 VAL   B C      1 
ATOM   2651 O  O      . VAL   B  2  58  ? -89.67597  21.89458  6.05492   1.000 30.78627  ?  4309 VAL   B O      1 
ATOM   2652 C  CB     . VAL   B  2  58  ? -89.81232  21.04518  3.19527   1.000 38.29413  ?  4309 VAL   B CB     1 
ATOM   2653 C  CG1    . VAL   B  2  58  ? -90.04176  19.89771  2.21871   1.000 42.71817  ?  4309 VAL   B CG1    1 
ATOM   2654 C  CG2    . VAL   B  2  58  ? -89.63806  22.36638  2.46165   1.000 37.78469  ?  4309 VAL   B CG2    1 
ATOM   2655 N  N      . THR   B  2  59  ? -91.30292  23.26720  5.33687   1.000 36.28307  ?  4310 THR   B N      1 
ATOM   2656 C  CA     . THR   B  2  59  ? -91.09234  24.30914  6.32669   1.000 35.43391  ?  4310 THR   B CA     1 
ATOM   2657 C  C      . THR   B  2  59  ? -92.46158  24.93144  6.56592   1.000 37.43887  ?  4310 THR   B C      1 
ATOM   2658 O  O      . THR   B  2  59  ? -93.34023  24.81153  5.70194   1.000 38.13877  ?  4310 THR   B O      1 
ATOM   2659 C  CB     . THR   B  2  59  ? -90.05846  25.33846  5.82726   1.000 41.45661  ?  4310 THR   B CB     1 
ATOM   2660 O  OG1    . THR   B  2  59  ? -89.58793  26.14431  6.91972   1.000 40.46158  ?  4310 THR   B OG1    1 
ATOM   2661 C  CG2    . THR   B  2  59  ? -90.66181  26.23549  4.75476   1.000 42.04610  ?  4310 THR   B CG2    1 
ATOM   2662 N  N      . PRO   B  2  60  ? -92.70190  25.53310  7.73020   1.000 34.79839  ?  4311 PRO   B N      1 
ATOM   2663 C  CA     . PRO   B  2  60  ? -94.03140  26.10514  8.00462   1.000 33.78696  ?  4311 PRO   B CA     1 
ATOM   2664 C  C      . PRO   B  2  60  ? -94.46600  27.08998  6.93332   1.000 38.36175  ?  4311 PRO   B C      1 
ATOM   2665 O  O      . PRO   B  2  60  ? -93.69842  27.95663  6.52316   1.000 39.96992  ?  4311 PRO   B O      1 
ATOM   2666 C  CB     . PRO   B  2  60  ? -93.84332  26.80141  9.35186   1.000 31.84043  ?  4311 PRO   B CB     1 
ATOM   2667 C  CG     . PRO   B  2  60  ? -92.75783  26.03358  10.01487  1.000 29.46565  ?  4311 PRO   B CG     1 
ATOM   2668 C  CD     . PRO   B  2  60  ? -91.81921  25.62346  8.90512   1.000 33.83173  ?  4311 PRO   B CD     1 
ATOM   2669 N  N      . GLU   B  2  61  ? -95.72563  26.96981  6.49878   1.000 35.65019  ?  4312 GLU   B N      1 
ATOM   2670 C  CA     . GLU   B  2  61  ? -96.23174  27.80991  5.42004   1.000 39.37521  ?  4312 GLU   B CA     1 
ATOM   2671 C  C      . GLU   B  2  61  ? -97.61728  28.37626  5.71513   1.000 38.12509  ?  4312 GLU   B C      1 
ATOM   2672 O  O      . GLU   B  2  61  ? -98.33827  28.73890  4.77622   1.000 40.44192  ?  4312 GLU   B O      1 
ATOM   2673 C  CB     . GLU   B  2  61  ? -96.28258  27.02494  4.10191   1.000 35.36853  ?  4312 GLU   B CB     1 
ATOM   2674 C  CG     . GLU   B  2  61  ? -94.92673  26.77497  3.46251   1.000 35.80658  ?  4312 GLU   B CG     1 
ATOM   2675 C  CD     . GLU   B  2  61  ? -94.32083  28.04898  2.88640   1.000 41.50492  ?  4312 GLU   B CD     1 
ATOM   2676 O  OE1    . GLU   B  2  61  ? -95.02525  29.07702  2.85400   1.000 46.28256  ?  4312 GLU   B OE1    1 
ATOM   2677 O  OE2    . GLU   B  2  61  ? -93.14708  28.02909  2.46617   1.000 45.16829  ?  4312 GLU   B OE2    1 
ATOM   2678 N  N      . ALA   B  2  62  ? -98.01493  28.45430  6.98223   1.000 29.32430  ?  4313 ALA   B N      1 
ATOM   2679 C  CA     . ALA   B  2  62  ? -99.32288  28.99487  7.31234   1.000 37.48950  ?  4313 ALA   B CA     1 
ATOM   2680 C  C      . ALA   B  2  62  ? -99.50992  30.35680  6.65561   1.000 42.02765  ?  4313 ALA   B C      1 
ATOM   2681 O  O      . ALA   B  2  62  ? -98.58594  31.17813  6.61974   1.000 33.86806  ?  4313 ALA   B O      1 
ATOM   2682 C  CB     . ALA   B  2  62  ? -99.47334  29.13199  8.82730   1.000 38.04293  ?  4313 ALA   B CB     1 
ATOM   2683 N  N      . ASN   B  2  63  ? -100.70938 30.58850  6.12906   1.000 38.29574  ?  4314 ASN   B N      1 
ATOM   2684 C  CA     . ASN   B  2  63  ? -101.10340 31.93125  5.73779   1.000 38.25302  ?  4314 ASN   B CA     1 
ATOM   2685 C  C      . ASN   B  2  63  ? -101.87274 32.53713  6.89752   1.000 39.58020  ?  4314 ASN   B C      1 
ATOM   2686 O  O      . ASN   B  2  63  ? -101.86949 32.00758  8.01441   1.000 37.17023  ?  4314 ASN   B O      1 
ATOM   2687 C  CB     . ASN   B  2  63  ? -101.90365 31.92671  4.42907   1.000 38.68754  ?  4314 ASN   B CB     1 
ATOM   2688 C  CG     . ASN   B  2  63  ? -103.19054 31.14439  4.52570   1.000 38.02549  ?  4314 ASN   B CG     1 
ATOM   2689 O  OD1    . ASN   B  2  63  ? -103.77134 30.98383  5.60233   1.000 38.27004  ?  4314 ASN   B OD1    1 
ATOM   2690 N  ND2    . ASN   B  2  63  ? -103.65003 30.65051  3.38856   1.000 41.44809  ?  4314 ASN   B ND2    1 
ATOM   2691 N  N      . MET   B  2  64  ? -102.54864 33.65604  6.64755   1.000 34.80250  ?  4315 MET   B N      1 
ATOM   2692 C  CA     . MET   B  2  64  ? -103.17766 34.38061  7.74060   1.000 37.35539  ?  4315 MET   B CA     1 
ATOM   2693 C  C      . MET   B  2  64  ? -104.28255 33.58128  8.40515   1.000 35.71853  ?  4315 MET   B C      1 
ATOM   2694 O  O      . MET   B  2  64  ? -104.64743 33.88918  9.54584   1.000 39.76004  ?  4315 MET   B O      1 
ATOM   2695 C  CB     . MET   B  2  64  ? -103.75216 35.71675  7.24272   1.000 38.90300  ?  4315 MET   B CB     1 
ATOM   2696 C  CG     . MET   B  2  64  ? -104.31899 36.58604  8.36893   1.000 50.68571  ?  4315 MET   B CG     1 
ATOM   2697 S  SD     . MET   B  2  64  ? -104.77137 38.28890  7.87602   1.000 59.94527  ?  4315 MET   B SD     1 
ATOM   2698 C  CE     . MET   B  2  64  ? -106.37772 38.01665  7.10682   1.000 55.13389  ?  4315 MET   B CE     1 
ATOM   2699 N  N      . ASP   B  2  65  ? -104.82114 32.56671  7.72689   1.000 38.34696  ?  4316 ASP   B N      1 
ATOM   2700 C  CA     . ASP   B  2  65  ? -105.95233 31.80071  8.23305   1.000 40.05411  ?  4316 ASP   B CA     1 
ATOM   2701 C  C      . ASP   B  2  65  ? -105.56993 30.41503  8.75125   1.000 45.07897  ?  4316 ASP   B C      1 
ATOM   2702 O  O      . ASP   B  2  65  ? -106.46465 29.58884  8.98464   1.000 37.15150  ?  4316 ASP   B O      1 
ATOM   2703 C  CB     . ASP   B  2  65  ? -107.00988 31.63907  7.14428   1.000 45.41210  ?  4316 ASP   B CB     1 
ATOM   2704 C  CG     . ASP   B  2  65  ? -107.45926 32.96556  6.56110   1.000 45.92679  ?  4316 ASP   B CG     1 
ATOM   2705 O  OD1    . ASP   B  2  65  ? -107.38040 33.10644  5.32792   1.000 49.41991  ?  4316 ASP   B OD1    1 
ATOM   2706 O  OD2    . ASP   B  2  65  ? -107.87736 33.84564  7.34442   1.000 46.97197  ?  4316 ASP   B OD2    1 
ATOM   2707 N  N      . GLN   B  2  66  ? -104.28097 30.13538  8.93461   1.000 38.17472  ?  4317 GLN   B N      1 
ATOM   2708 C  CA     . GLN   B  2  66  ? -103.82488 28.80160  9.30724   1.000 36.57076  ?  4317 GLN   B CA     1 
ATOM   2709 C  C      . GLN   B  2  66  ? -102.83002 28.87404  10.46021  1.000 40.76339  ?  4317 GLN   B C      1 
ATOM   2710 O  O      . GLN   B  2  66  ? -102.25170 29.92154  10.75353  1.000 33.99658  ?  4317 GLN   B O      1 
ATOM   2711 C  CB     . GLN   B  2  66  ? -103.15801 28.08319  8.12360   1.000 35.68233  ?  4317 GLN   B CB     1 
ATOM   2712 C  CG     . GLN   B  2  66  ? -104.01477 27.92842  6.85416   1.000 33.94854  ?  4317 GLN   B CG     1 
ATOM   2713 C  CD     . GLN   B  2  66  ? -103.15302 27.59943  5.66408   1.000 37.93674  ?  4317 GLN   B CD     1 
ATOM   2714 O  OE1    . GLN   B  2  66  ? -102.02283 28.07049  5.56894   1.000 41.17126  ?  4317 GLN   B OE1    1 
ATOM   2715 N  NE2    . GLN   B  2  66  ? -103.66055 26.78018  4.76037   1.000 37.12043  ?  4317 GLN   B NE2    1 
ATOM   2716 N  N      . GLU   B  2  67  ? -102.64755 27.73613  11.12028  1.000 38.59534  ?  4318 GLU   B N      1 
ATOM   2717 C  CA     . GLU   B  2  67  ? -101.54233 27.49446  12.03021  1.000 34.38934  ?  4318 GLU   B CA     1 
ATOM   2718 C  C      . GLU   B  2  67  ? -100.67987 26.40082  11.42325  1.000 35.86361  ?  4318 GLU   B C      1 
ATOM   2719 O  O      . GLU   B  2  67  ? -101.18696 25.52800  10.71589  1.000 35.80673  ?  4318 GLU   B O      1 
ATOM   2720 C  CB     . GLU   B  2  67  ? -102.05131 27.05722  13.40887  1.000 37.37007  ?  4318 GLU   B CB     1 
ATOM   2721 C  CG     . GLU   B  2  67  ? -102.96096 28.05026  14.11754  1.000 37.57136  ?  4318 GLU   B CG     1 
ATOM   2722 C  CD     . GLU   B  2  67  ? -102.17408 29.13569  14.82989  1.000 46.49273  ?  4318 GLU   B CD     1 
ATOM   2723 O  OE1    . GLU   B  2  67  ? -101.07317 29.48567  14.33903  1.000 48.34631  ?  4318 GLU   B OE1    1 
ATOM   2724 O  OE2    . GLU   B  2  67  ? -102.63056 29.61680  15.89576  1.000 45.87076  ?  4318 GLU   B OE2    1 
ATOM   2725 N  N      . SER   B  2  68  ? -99.37492  26.45273  11.66283  1.000 34.45615  ?  4319 SER   B N      1 
ATOM   2726 C  CA     . SER   B  2  68  ? -98.48415  25.38926  11.21138  1.000 32.90314  ?  4319 SER   B CA     1 
ATOM   2727 C  C      . SER   B  2  68  ? -98.10373  24.51428  12.39647  1.000 33.31669  ?  4319 SER   B C      1 
ATOM   2728 O  O      . SER   B  2  68  ? -97.83172  25.02585  13.48431  1.000 30.60781  ?  4319 SER   B O      1 
ATOM   2729 C  CB     . SER   B  2  68  ? -97.20964  25.94148  10.57088  1.000 33.31516  ?  4319 SER   B CB     1 
ATOM   2730 O  OG     . SER   B  2  68  ? -97.50086  26.62552  9.37783   1.000 33.79120  ?  4319 SER   B OG     1 
ATOM   2731 N  N      . PHE   B  2  69  ? -98.05817  23.19933  12.17496  1.000 30.87920  ?  4320 PHE   B N      1 
ATOM   2732 C  CA     . PHE   B  2  69  ? -97.70113  22.24615  13.21386  1.000 28.97558  ?  4320 PHE   B CA     1 
ATOM   2733 C  C      . PHE   B  2  69  ? -96.61330  21.30746  12.71140  1.000 27.82964  ?  4320 PHE   B C      1 
ATOM   2734 O  O      . PHE   B  2  69  ? -96.54281  20.98953  11.52070  1.000 29.96051  ?  4320 PHE   B O      1 
ATOM   2735 C  CB     . PHE   B  2  69  ? -98.91014  21.38114  13.65484  1.000 29.54344  ?  4320 PHE   B CB     1 
ATOM   2736 C  CG     . PHE   B  2  69  ? -99.99649  22.13707  14.34737  1.000 32.07185  ?  4320 PHE   B CG     1 
ATOM   2737 C  CD1    . PHE   B  2  69  ? -101.00456 22.75336  13.61637  1.000 34.53208  ?  4320 PHE   B CD1    1 
ATOM   2738 C  CD2    . PHE   B  2  69  ? -100.04408 22.19118  15.72889  1.000 27.26624  ?  4320 PHE   B CD2    1 
ATOM   2739 C  CE1    . PHE   B  2  69  ? -102.03193 23.42084  14.25829  1.000 30.87448  ?  4320 PHE   B CE1    1 
ATOM   2740 C  CE2    . PHE   B  2  69  ? -101.07684 22.85371  16.37663  1.000 33.50468  ?  4320 PHE   B CE2    1 
ATOM   2741 C  CZ     . PHE   B  2  69  ? -102.06652 23.47083  15.64335  1.000 34.17784  ?  4320 PHE   B CZ     1 
ATOM   2742 N  N      . GLY   B  2  70  ? -95.78811  20.82605  13.63693  1.000 30.02419  ?  4321 GLY   B N      1 
ATOM   2743 C  CA     . GLY   B  2  70  ? -94.85195  19.76745  13.28282  1.000 30.33884  ?  4321 GLY   B CA     1 
ATOM   2744 C  C      . GLY   B  2  70  ? -95.62703  18.53277  12.84019  1.000 31.39374  ?  4321 GLY   B C      1 
ATOM   2745 O  O      . GLY   B  2  70  ? -96.57146  18.12332  13.52376  1.000 34.08710  ?  4321 GLY   B O      1 
ATOM   2746 N  N      . GLY   B  2  71  ? -95.25616  17.94427  11.70184  1.000 31.78655  ?  4322 GLY   B N      1 
ATOM   2747 C  CA     . GLY   B  2  71  ? -96.10555  16.92703  11.09215  1.000 34.57802  ?  4322 GLY   B CA     1 
ATOM   2748 C  C      . GLY   B  2  71  ? -96.29273  15.70171  11.96751  1.000 36.15262  ?  4322 GLY   B C      1 
ATOM   2749 O  O      . GLY   B  2  71  ? -97.41493  15.23216  12.16505  1.000 35.75567  ?  4322 GLY   B O      1 
ATOM   2750 N  N      . ALA   B  2  72  ? -95.19342  15.15787  12.50097  1.000 37.29678  ?  4323 ALA   B N      1 
ATOM   2751 C  CA     . ALA   B  2  72  ? -95.29482  13.91324  13.26502  1.000 34.73135  ?  4323 ALA   B CA     1 
ATOM   2752 C  C      . ALA   B  2  72  ? -96.28688  14.03964  14.40837  1.000 37.74616  ?  4323 ALA   B C      1 
ATOM   2753 O  O      . ALA   B  2  72  ? -97.00960  13.08770  14.72146  1.000 33.36366  ?  4323 ALA   B O      1 
ATOM   2754 C  CB     . ALA   B  2  72  ? -93.92770  13.50080  13.81939  1.000 32.62867  ?  4323 ALA   B CB     1 
ATOM   2755 N  N      . SER   B  2  73  ? -96.31638  15.19379  15.07565  1.000 30.16791  ?  4324 SER   B N      1 
ATOM   2756 C  CA     . SER   B  2  73  ? -97.22414  15.34887  16.20818  1.000 32.68737  ?  4324 SER   B CA     1 
ATOM   2757 C  C      . SER   B  2  73  ? -98.68543  15.44274  15.78411  1.000 33.38546  ?  4324 SER   B C      1 
ATOM   2758 O  O      . SER   B  2  73  ? -99.56842  15.39940  16.64988  1.000 32.53420  ?  4324 SER   B O      1 
ATOM   2759 C  CB     . SER   B  2  73  ? -96.85364  16.58641  17.01751  1.000 34.14427  ?  4324 SER   B CB     1 
ATOM   2760 O  OG     . SER   B  2  73  ? -97.15072  17.75611  16.27115  1.000 35.62209  ?  4324 SER   B OG     1 
ATOM   2761 N  N      . CYS   B  2  74  ? -98.96279  15.56899  14.48782  1.000 32.49821  ?  4325 CYS   B N      1 
ATOM   2762 C  CA     . CYS   B  2  74  ? -100.33463 15.63740  13.98570  1.000 32.23904  ?  4325 CYS   B CA     1 
ATOM   2763 C  C      . CYS   B  2  74  ? -100.76381 14.35163  13.28731  1.000 36.04903  ?  4325 CYS   B C      1 
ATOM   2764 O  O      . CYS   B  2  74  ? -101.84123 14.31101  12.68195  1.000 37.77513  ?  4325 CYS   B O      1 
ATOM   2765 C  CB     . CYS   B  2  74  ? -100.49002 16.81078  13.02087  1.000 37.78902  ?  4325 CYS   B CB     1 
ATOM   2766 S  SG     . CYS   B  2  74  ? -100.23320 18.43013  13.80555  1.000 38.07071  ?  4325 CYS   B SG     1 
ATOM   2767 N  N      . CYS   B  2  75  ? -99.94436  13.31290  13.33797  1.000 36.84548  ?  4326 CYS   B N      1 
ATOM   2768 C  CA     . CYS   B  2  75  ? -100.20938 12.06960  12.62634  1.000 37.83431  ?  4326 CYS   B CA     1 
ATOM   2769 C  C      . CYS   B  2  75  ? -100.78726 11.07422  13.61426  1.000 37.81001  ?  4326 CYS   B C      1 
ATOM   2770 O  O      . CYS   B  2  75  ? -100.11640 10.69734  14.57745  1.000 33.77410  ?  4326 CYS   B O      1 
ATOM   2771 C  CB     . CYS   B  2  75  ? -98.93031  11.52867  11.99647  1.000 39.23127  ?  4326 CYS   B CB     1 
ATOM   2772 S  SG     . CYS   B  2  75  ? -99.08345  9.88599   11.23723  1.000 38.94427  ?  4326 CYS   B SG     1 
ATOM   2773 N  N      . LEU   B  2  76  ? -102.03803 10.67299  13.38782  1.000 39.24054  ?  4327 LEU   B N      1 
ATOM   2774 C  CA     . LEU   B  2  76  ? -102.67623 9.69453   14.26161  1.000 41.54410  ?  4327 LEU   B CA     1 
ATOM   2775 C  C      . LEU   B  2  76  ? -101.78578 8.47696   14.48338  1.000 37.08408  ?  4327 LEU   B C      1 
ATOM   2776 O  O      . LEU   B  2  76  ? -101.62831 8.00548   15.61550  1.000 37.67994  ?  4327 LEU   B O      1 
ATOM   2777 C  CB     . LEU   B  2  76  ? -104.02152 9.26299   13.66818  1.000 41.63898  ?  4327 LEU   B CB     1 
ATOM   2778 C  CG     . LEU   B  2  76  ? -104.78754 8.26554   14.53865  1.000 44.02917  ?  4327 LEU   B CG     1 
ATOM   2779 C  CD1    . LEU   B  2  76  ? -105.25510 8.91506   15.83343  1.000 41.29928  ?  4327 LEU   B CD1    1 
ATOM   2780 C  CD2    . LEU   B  2  76  ? -105.96927 7.66887   13.76894  1.000 46.83287  ?  4327 LEU   B CD2    1 
ATOM   2781 N  N      . TYR   B  2  77  ? -101.19270 7.95455   13.41579  1.000 36.74928  ?  4328 TYR   B N      1 
ATOM   2782 C  CA     . TYR   B  2  77  ? -100.43306 6.71428   13.54127  1.000 42.93157  ?  4328 TYR   B CA     1 
ATOM   2783 C  C      . TYR   B  2  77  ? -99.13983  6.93345   14.30963  1.000 42.82594  ?  4328 TYR   B C      1 
ATOM   2784 O  O      . TYR   B  2  77  ? -98.78844  6.12913   15.18053  1.000 39.69634  ?  4328 TYR   B O      1 
ATOM   2785 C  CB     . TYR   B  2  77  ? -100.17116 6.13226   12.15588  1.000 45.39225  ?  4328 TYR   B CB     1 
ATOM   2786 C  CG     . TYR   B  2  77  ? -101.46006 6.02873   11.38486  1.000 49.21493  ?  4328 TYR   B CG     1 
ATOM   2787 C  CD1    . TYR   B  2  77  ? -102.42752 5.09914   11.74790  1.000 49.36985  ?  4328 TYR   B CD1    1 
ATOM   2788 C  CD2    . TYR   B  2  77  ? -101.74084 6.89745   10.33442  1.000 46.89171  ?  4328 TYR   B CD2    1 
ATOM   2789 C  CE1    . TYR   B  2  77  ? -103.63346 5.01638   11.06697  1.000 53.12667  ?  4328 TYR   B CE1    1 
ATOM   2790 C  CE2    . TYR   B  2  77  ? -102.93657 6.82259   9.64582   1.000 48.89625  ?  4328 TYR   B CE2    1 
ATOM   2791 C  CZ     . TYR   B  2  77  ? -103.88165 5.88239   10.01037  1.000 53.82513  ?  4328 TYR   B CZ     1 
ATOM   2792 O  OH     . TYR   B  2  77  ? -105.07429 5.80098   9.31933   1.000 54.43237  ?  4328 TYR   B OH     1 
ATOM   2793 N  N      . CYS   B  2  78  ? -98.41202  8.01116   14.00231  1.000 41.81111  ?  4329 CYS   B N      1 
ATOM   2794 C  CA     . CYS   B  2  78  ? -97.25440  8.36130   14.81873  1.000 37.35429  ?  4329 CYS   B CA     1 
ATOM   2795 C  C      . CYS   B  2  78  ? -97.65054  8.46715   16.28779  1.000 38.44584  ?  4329 CYS   B C      1 
ATOM   2796 O  O      . CYS   B  2  78  ? -97.03702  7.84110   17.15498  1.000 39.63509  ?  4329 CYS   B O      1 
ATOM   2797 C  CB     . CYS   B  2  78  ? -96.63486  9.67884   14.33414  1.000 40.97282  ?  4329 CYS   B CB     1 
ATOM   2798 S  SG     . CYS   B  2  78  ? -95.71933  9.60456   12.75482  1.000 40.81878  ?  4329 CYS   B SG     1 
ATOM   2799 N  N      . ARG   B  2  79  ? -98.69849  9.24667   16.58365  1.000 34.86764  ?  4330 ARG   B N      1 
ATOM   2800 C  CA     . ARG   B  2  79  ? -99.03229  9.53921   17.97140  1.000 34.19582  ?  4330 ARG   B CA     1 
ATOM   2801 C  C      . ARG   B  2  79  ? -99.52215  8.30311   18.71395  1.000 43.45869  ?  4330 ARG   B C      1 
ATOM   2802 O  O      . ARG   B  2  79  ? -99.33023  8.20132   19.93240  1.000 37.71601  ?  4330 ARG   B O      1 
ATOM   2803 C  CB     . ARG   B  2  79  ? -100.09317 10.64371  18.04681  1.000 36.04920  ?  4330 ARG   B CB     1 
ATOM   2804 C  CG     . ARG   B  2  79  ? -99.58506  12.06595  17.68724  1.000 35.55909  ?  4330 ARG   B CG     1 
ATOM   2805 C  CD     . ARG   B  2  79  ? -98.50148  12.57585  18.64178  1.000 31.66616  ?  4330 ARG   B CD     1 
ATOM   2806 N  NE     . ARG   B  2  79  ? -99.00277  12.75762  19.99718  1.000 34.60901  ?  4330 ARG   B NE     1 
ATOM   2807 C  CZ     . ARG   B  2  79  ? -99.69740  13.80573  20.41701  1.000 36.90376  ?  4330 ARG   B CZ     1 
ATOM   2808 N  NH1    . ARG   B  2  79  ? -99.96368  14.83505  19.61776  1.000 32.31757  ?  4330 ARG   B NH1    1 
ATOM   2809 N  NH2    . ARG   B  2  79  ? -100.12511 13.83024  21.67393  1.000 34.35070  ?  4330 ARG   B NH2    1 
ATOM   2810 N  N      . CYS   B  2  80  ? -100.16870 7.36801   18.01680  1.000 38.79863  ?  4331 CYS   B N      1 
ATOM   2811 C  CA     . CYS   B  2  80  ? -100.70252 6.18323   18.67318  1.000 44.07196  ?  4331 CYS   B CA     1 
ATOM   2812 C  C      . CYS   B  2  80  ? -99.72364  5.01946   18.67607  1.000 46.49283  ?  4331 CYS   B C      1 
ATOM   2813 O  O      . CYS   B  2  80  ? -100.02030 3.98375   19.27983  1.000 49.30916  ?  4331 CYS   B O      1 
ATOM   2814 C  CB     . CYS   B  2  80  ? -102.01891 5.76358   18.01391  1.000 43.57465  ?  4331 CYS   B CB     1 
ATOM   2815 S  SG     . CYS   B  2  80  ? -103.37353 6.91001   18.39738  1.000 49.75896  ?  4331 CYS   B SG     1 
ATOM   2816 N  N      . HIS   B  2  81  ? -98.56115  5.16407   18.04117  1.000 43.55489  ?  4332 HIS   B N      1 
ATOM   2817 C  CA     . HIS   B  2  81  ? -97.56097  4.10042   18.03009  1.000 45.75998  ?  4332 HIS   B CA     1 
ATOM   2818 C  C      . HIS   B  2  81  ? -98.12307  2.86641   17.33144  1.000 47.50948  ?  4332 HIS   B C      1 
ATOM   2819 O  O      . HIS   B  2  81  ? -98.09783  1.75374   17.86102  1.000 52.80638  ?  4332 HIS   B O      1 
ATOM   2820 C  CB     . HIS   B  2  81  ? -97.09551  3.75712   19.45116  1.000 45.80215  ?  4332 HIS   B CB     1 
ATOM   2821 C  CG     . HIS   B  2  81  ? -96.55603  4.92706   20.21958  1.000 52.96928  ?  4332 HIS   B CG     1 
ATOM   2822 N  ND1    . HIS   B  2  81  ? -96.37102  4.89710   21.58626  1.000 57.67343  ?  4332 HIS   B ND1    1 
ATOM   2823 C  CD2    . HIS   B  2  81  ? -96.15538  6.15742   19.81367  1.000 52.85016  ?  4332 HIS   B CD2    1 
ATOM   2824 C  CE1    . HIS   B  2  81  ? -95.87981  6.05653   21.98890  1.000 59.69895  ?  4332 HIS   B CE1    1 
ATOM   2825 N  NE2    . HIS   B  2  81  ? -95.74239  6.84053   20.93284  1.000 57.82606  ?  4332 HIS   B NE2    1 
ATOM   2826 N  N      . ILE   B  2  82  ? -98.65908  3.07533   16.13307  1.000 45.59157  ?  4333 ILE   B N      1 
ATOM   2827 C  CA     . ILE   B  2  82  ? -99.19573  1.98041   15.34039  1.000 48.19306  ?  4333 ILE   B CA     1 
ATOM   2828 C  C      . ILE   B  2  82  ? -98.72232  2.13480   13.90355  1.000 49.68959  ?  4333 ILE   B C      1 
ATOM   2829 O  O      . ILE   B  2  82  ? -98.23699  3.19024   13.49091  1.000 45.22489  ?  4333 ILE   B O      1 
ATOM   2830 C  CB     . ILE   B  2  82  ? -100.73433 1.91167   15.41035  1.000 46.49013  ?  4333 ILE   B CB     1 
ATOM   2831 C  CG1    . ILE   B  2  82  ? -101.36796 3.12342   14.73728  1.000 48.08096  ?  4333 ILE   B CG1    1 
ATOM   2832 C  CG2    . ILE   B  2  82  ? -101.19085 1.89333   16.84549  1.000 50.18392  ?  4333 ILE   B CG2    1 
ATOM   2833 C  CD1    . ILE   B  2  82  ? -102.84305 3.22319   15.02469  1.000 44.63181  ?  4333 ILE   B CD1    1 
ATOM   2834 N  N      . ASP   B  2  83  ? -98.85122  1.05174   13.14340  1.000 52.45066  ?  4334 ASP   B N      1 
ATOM   2835 C  CA     . ASP   B  2  83  ? -98.33964  1.03532   11.78206  1.000 47.52581  ?  4334 ASP   B CA     1 
ATOM   2836 C  C      . ASP   B  2  83  ? -99.11218  2.01839   10.91214  1.000 49.19433  ?  4334 ASP   B C      1 
ATOM   2837 O  O      . ASP   B  2  83  ? -100.29861 2.28214   11.13091  1.000 46.74479  ?  4334 ASP   B O      1 
ATOM   2838 C  CB     . ASP   B  2  83  ? -98.42806  -0.37430  11.19303  1.000 53.16817  ?  4334 ASP   B CB     1 
ATOM   2839 C  CG     . ASP   B  2  83  ? -97.43204  -1.34749  11.83171  1.000 61.05310  ?  4334 ASP   B CG     1 
ATOM   2840 O  OD1    . ASP   B  2  83  ? -96.56886  -0.91385  12.63284  1.000 60.65861  ?  4334 ASP   B OD1    1 
ATOM   2841 O  OD2    . ASP   B  2  83  ? -97.51754  -2.55741  11.52978  1.000 65.57356  ?  4334 ASP   B OD2    1 
ATOM   2842 N  N      . HIS   B  2  84  ? -98.41954  2.57262   9.92053   1.000 51.62109  ?  4335 HIS   B N      1 
ATOM   2843 C  CA     . HIS   B  2  84  ? -99.08938  3.47967   8.99892   1.000 57.74508  ?  4335 HIS   B CA     1 
ATOM   2844 C  C      . HIS   B  2  84  ? -99.83344  2.68271   7.92775   1.000 61.21875  ?  4335 HIS   B C      1 
ATOM   2845 O  O      . HIS   B  2  84  ? -99.33587  1.65296   7.46838   1.000 58.65841  ?  4335 HIS   B O      1 
ATOM   2846 C  CB     . HIS   B  2  84  ? -98.08214  4.43088   8.34971   1.000 56.20453  ?  4335 HIS   B CB     1 
ATOM   2847 C  CG     . HIS   B  2  84  ? -97.58216  5.50279   9.27261   1.000 57.19434  ?  4335 HIS   B CG     1 
ATOM   2848 N  ND1    . HIS   B  2  84  ? -96.68177  5.25467   10.28789  1.000 50.68730  ?  4335 HIS   B ND1    1 
ATOM   2849 C  CD2    . HIS   B  2  84  ? -97.86606  6.82625   9.33868   1.000 51.38990  ?  4335 HIS   B CD2    1 
ATOM   2850 C  CE1    . HIS   B  2  84  ? -96.43319  6.37816   10.93833  1.000 50.87270  ?  4335 HIS   B CE1    1 
ATOM   2851 N  NE2    . HIS   B  2  84  ? -97.13674  7.34675   10.38108  1.000 50.23877  ?  4335 HIS   B NE2    1 
ATOM   2852 N  N      . PRO   B  2  85  ? -101.02491 3.13350   7.52416   1.000 64.80141  ?  4336 PRO   B N      1 
ATOM   2853 C  CA     . PRO   B  2  85  ? -101.80194 2.37990   6.51728   1.000 72.11798  ?  4336 PRO   B CA     1 
ATOM   2854 C  C      . PRO   B  2  85  ? -101.08921 2.20321   5.18511   1.000 75.78799  ?  4336 PRO   B C      1 
ATOM   2855 O  O      . PRO   B  2  85  ? -101.34921 1.22322   4.47871   1.000 82.44363  ?  4336 PRO   B O      1 
ATOM   2856 C  CB     . PRO   B  2  85  ? -103.08128 3.21814   6.36314   1.000 71.27771  ?  4336 PRO   B CB     1 
ATOM   2857 C  CG     . PRO   B  2  85  ? -102.72180 4.58019   6.87926   1.000 69.84858  ?  4336 PRO   B CG     1 
ATOM   2858 C  CD     . PRO   B  2  85  ? -101.72747 4.34149   7.98108   1.000 64.12407  ?  4336 PRO   B CD     1 
ATOM   2859 N  N      . ASN   B  2  86  ? -100.20839 3.12024   4.80988   1.000 83.17015  ?  4337 ASN   B N      1 
ATOM   2860 C  CA     . ASN   B  2  86  ? -99.39434  2.91577   3.62338   1.000 83.76055  ?  4337 ASN   B CA     1 
ATOM   2861 C  C      . ASN   B  2  86  ? -98.68279  1.56328   3.71479   1.000 85.74200  ?  4337 ASN   B C      1 
ATOM   2862 O  O      . ASN   B  2  86  ? -98.10493  1.24416   4.76388   1.000 84.28320  ?  4337 ASN   B O      1 
ATOM   2863 C  CB     . ASN   B  2  86  ? -98.37145  4.04551   3.48776   1.000 79.48934  ?  4337 ASN   B CB     1 
ATOM   2864 C  CG     . ASN   B  2  86  ? -97.84271  4.18658   2.07218   1.000 89.88622  ?  4337 ASN   B CG     1 
ATOM   2865 O  OD1    . ASN   B  2  86  ? -97.01875  3.38465   1.62006   1.000 91.04915  ?  4337 ASN   B OD1    1 
ATOM   2866 N  ND2    . ASN   B  2  86  ? -98.31305  5.21460   1.36268   1.000 91.10382  ?  4337 ASN   B ND2    1 
ATOM   2867 N  N      . PRO   B  2  87  ? -98.71427  0.74023   2.65908   1.000 91.41560  ?  4338 PRO   B N      1 
ATOM   2868 C  CA     . PRO   B  2  87  ? -98.01734  -0.55929  2.73555   1.000 90.45640  ?  4338 PRO   B CA     1 
ATOM   2869 C  C      . PRO   B  2  87  ? -96.54132  -0.44286  3.07709   1.000 88.46993  ?  4338 PRO   B C      1 
ATOM   2870 O  O      . PRO   B  2  87  ? -95.99744  -1.32606  3.75094   1.000 87.54450  ?  4338 PRO   B O      1 
ATOM   2871 C  CB     . PRO   B  2  87  ? -98.23469  -1.15385  1.33623   1.000 89.05613  ?  4338 PRO   B CB     1 
ATOM   2872 C  CG     . PRO   B  2  87  ? -99.50051  -0.51840  0.85657   1.000 87.51267  ?  4338 PRO   B CG     1 
ATOM   2873 C  CD     . PRO   B  2  87  ? -99.48138  0.88436   1.40799   1.000 88.81603  ?  4338 PRO   B CD     1 
ATOM   2874 N  N      . LYS   B  2  88  ? -95.87082  0.61907   2.62511   1.000 86.99086  ?  4339 LYS   B N      1 
ATOM   2875 C  CA     . LYS   B  2  88  ? -94.46555  0.82807   2.95297   1.000 86.58609  ?  4339 LYS   B CA     1 
ATOM   2876 C  C      . LYS   B  2  88  ? -94.25520  1.36480   4.36475   1.000 85.23513  ?  4339 LYS   B C      1 
ATOM   2877 O  O      . LYS   B  2  88  ? -93.10041  1.52603   4.78220   1.000 82.69559  ?  4339 LYS   B O      1 
ATOM   2878 C  CB     . LYS   B  2  88  ? -93.82340  1.78719   1.94474   1.000 85.70951  ?  4339 LYS   B CB     1 
ATOM   2879 C  CG     . LYS   B  2  88  ? -93.65713  1.22124   0.54442   1.000 86.83539  ?  4339 LYS   B CG     1 
ATOM   2880 C  CD     . LYS   B  2  88  ? -94.43065  2.05264   -0.46973  1.000 89.47998  ?  4339 LYS   B CD     1 
ATOM   2881 C  CE     . LYS   B  2  88  ? -93.91095  1.83217   -1.88335  1.000 87.00142  ?  4339 LYS   B CE     1 
ATOM   2882 N  NZ     . LYS   B  2  88  ? -94.58586  2.71775   -2.86981  1.000 81.96856  ?  4339 LYS   B NZ     1 
ATOM   2883 N  N      . GLY   B  2  89  ? -95.32644  1.63909   5.10681   1.000 80.98086  ?  4340 GLY   B N      1 
ATOM   2884 C  CA     . GLY   B  2  89  ? -95.17706  2.28102   6.40060   1.000 78.12743  ?  4340 GLY   B CA     1 
ATOM   2885 C  C      . GLY   B  2  89  ? -94.61144  3.68183   6.32779   1.000 76.38419  ?  4340 GLY   B C      1 
ATOM   2886 O  O      . GLY   B  2  89  ? -94.04589  4.16559   7.31054   1.000 76.18796  ?  4340 GLY   B O      1 
ATOM   2887 N  N      . PHE   B  2  90  ? -94.73817  4.34222   5.17950   1.000 75.67768  ?  4341 PHE   B N      1 
ATOM   2888 C  CA     . PHE   B  2  90  ? -94.27999  5.71406   5.01808   1.000 69.85413  ?  4341 PHE   B CA     1 
ATOM   2889 C  C      . PHE   B  2  90  ? -95.30237  6.67722   5.61858   1.000 69.09019  ?  4341 PHE   B C      1 
ATOM   2890 O  O      . PHE   B  2  90  ? -96.51530  6.43952   5.55657   1.000 66.24543  ?  4341 PHE   B O      1 
ATOM   2891 C  CB     . PHE   B  2  90  ? -94.04315  6.00980   3.53296   1.000 69.16674  ?  4341 PHE   B CB     1 
ATOM   2892 C  CG     . PHE   B  2  90  ? -93.98982  7.47735   3.18569   1.000 73.84271  ?  4341 PHE   B CG     1 
ATOM   2893 C  CD1    . PHE   B  2  90  ? -92.78724  8.17436   3.21441   1.000 69.90787  ?  4341 PHE   B CD1    1 
ATOM   2894 C  CD2    . PHE   B  2  90  ? -95.14267  8.15169   2.79227   1.000 72.93439  ?  4341 PHE   B CD2    1 
ATOM   2895 C  CE1    . PHE   B  2  90  ? -92.73703  9.52471   2.87516   1.000 69.60583  ?  4341 PHE   B CE1    1 
ATOM   2896 C  CE2    . PHE   B  2  90  ? -95.10169  9.50115   2.45338   1.000 69.87507  ?  4341 PHE   B CE2    1 
ATOM   2897 C  CZ     . PHE   B  2  90  ? -93.89587  10.19000  2.49676   1.000 69.18180  ?  4341 PHE   B CZ     1 
ATOM   2898 N  N      . CYS   B  2  91  ? -94.80359  7.75072   6.23391   1.000 62.93664  ?  4342 CYS   B N      1 
ATOM   2899 C  CA     . CYS   B  2  91  ? -95.64217  8.76533   6.85878   1.000 56.84094  ?  4342 CYS   B CA     1 
ATOM   2900 C  C      . CYS   B  2  91  ? -95.61845  10.02699  6.00941   1.000 54.75605  ?  4342 CYS   B C      1 
ATOM   2901 O  O      . CYS   B  2  91  ? -94.54551  10.56650  5.72128   1.000 56.36349  ?  4342 CYS   B O      1 
ATOM   2902 C  CB     . CYS   B  2  91  ? -95.18056  9.07917   8.28103   1.000 51.12652  ?  4342 CYS   B CB     1 
ATOM   2903 S  SG     . CYS   B  2  91  ? -96.34495  10.16890  9.12689   1.000 42.75353  ?  4342 CYS   B SG     1 
ATOM   2904 N  N      . ASP   B  2  92  ? -96.80395  10.49173  5.61363   1.000 53.58369  ?  4343 ASP   B N      1 
ATOM   2905 C  CA     . ASP   B  2  92  ? -96.92133  11.72132  4.83907   1.000 58.09915  ?  4343 ASP   B CA     1 
ATOM   2906 C  C      . ASP   B  2  92  ? -96.51719  12.96156  5.62714   1.000 53.20602  ?  4343 ASP   B C      1 
ATOM   2907 O  O      . ASP   B  2  92  ? -96.19834  13.98925  5.01680   1.000 47.42891  ?  4343 ASP   B O      1 
ATOM   2908 C  CB     . ASP   B  2  92  ? -98.36285  11.89788  4.35862   1.000 58.87880  ?  4343 ASP   B CB     1 
ATOM   2909 C  CG     . ASP   B  2  92  ? -98.61699  11.25380  3.01346   1.000 69.31928  ?  4343 ASP   B CG     1 
ATOM   2910 O  OD1    . ASP   B  2  92  ? -97.66377  10.70442  2.41521   1.000 70.12747  ?  4343 ASP   B OD1    1 
ATOM   2911 O  OD2    . ASP   B  2  92  ? -99.78046  11.30528  2.55649   1.000 70.88472  ?  4343 ASP   B OD2    1 
ATOM   2912 N  N      . LEU   B  2  93  ? -96.55563  12.90079  6.95749   1.000 45.21014  ?  4344 LEU   B N      1 
ATOM   2913 C  CA     . LEU   B  2  93  ? -96.44681  14.08362  7.80372   1.000 40.65800  ?  4344 LEU   B CA     1 
ATOM   2914 C  C      . LEU   B  2  93  ? -95.12369  14.19571  8.53328   1.000 40.22620  ?  4344 LEU   B C      1 
ATOM   2915 O  O      . LEU   B  2  93  ? -94.61858  15.30660  8.72059   1.000 39.58061  ?  4344 LEU   B O      1 
ATOM   2916 C  CB     . LEU   B  2  93  ? -97.57458  14.08890  8.83168   1.000 37.55002  ?  4344 LEU   B CB     1 
ATOM   2917 C  CG     . LEU   B  2  93  ? -98.98340  14.18768  8.26485   1.000 41.44062  ?  4344 LEU   B CG     1 
ATOM   2918 C  CD1    . LEU   B  2  93  ? -99.98369  13.87609  9.35811   1.000 38.42897  ?  4344 LEU   B CD1    1 
ATOM   2919 C  CD2    . LEU   B  2  93  ? -99.21013  15.58829  7.73330   1.000 38.02200  ?  4344 LEU   B CD2    1 
ATOM   2920 N  N      . LYS   B  2  94  ? -94.55617  13.07118  8.95450   1.000 38.21266  ?  4345 LYS   B N      1 
ATOM   2921 C  CA     . LYS   B  2  94  ? -93.33861  13.10647  9.74491   1.000 35.98376  ?  4345 LYS   B CA     1 
ATOM   2922 C  C      . LYS   B  2  94  ? -92.23384  13.82318  8.98912   1.000 32.28668  ?  4345 LYS   B C      1 
ATOM   2923 O  O      . LYS   B  2  94  ? -91.99879  13.56246  7.80952   1.000 38.71697  ?  4345 LYS   B O      1 
ATOM   2924 C  CB     . LYS   B  2  94  ? -92.90393  11.68224  10.10143  1.000 38.60873  ?  4345 LYS   B CB     1 
ATOM   2925 C  CG     . LYS   B  2  94  ? -91.51591  11.56733  10.68611  1.000 36.94187  ?  4345 LYS   B CG     1 
ATOM   2926 C  CD     . LYS   B  2  94  ? -91.22482  10.09556  10.99904  1.000 44.46935  ?  4345 LYS   B CD     1 
ATOM   2927 C  CE     . LYS   B  2  94  ? -89.87844  9.93861   11.67349  1.000 43.31425  ?  4345 LYS   B CE     1 
ATOM   2928 N  NZ     . LYS   B  2  94  ? -90.06581  9.69679   13.14296  1.000 51.39245  ?  4345 LYS   B NZ     1 
ATOM   2929 N  N      . GLY   B  2  95  ? -91.52808  14.70643  9.68780   1.000 37.18204  ?  4346 GLY   B N      1 
ATOM   2930 C  CA     . GLY   B  2  95  ? -90.43885  15.44339  9.08897   1.000 31.97751  ?  4346 GLY   B CA     1 
ATOM   2931 C  C      . GLY   B  2  95  ? -90.86710  16.65154  8.29274   1.000 33.83037  ?  4346 GLY   B C      1 
ATOM   2932 O  O      . GLY   B  2  95  ? -90.00187  17.34595  7.73554   1.000 34.34040  ?  4346 GLY   B O      1 
ATOM   2933 N  N      . LYS   B  2  96  ? -92.16751  16.92478  8.22544   1.000 30.29359  ?  4347 LYS   B N      1 
ATOM   2934 C  CA     . LYS   B  2  96  ? -92.71862  18.04930  7.48875   1.000 29.86448  ?  4347 LYS   B CA     1 
ATOM   2935 C  C      . LYS   B  2  96  ? -93.60298  18.87020  8.42607   1.000 31.10815  ?  4347 LYS   B C      1 
ATOM   2936 O  O      . LYS   B  2  96  ? -93.72348  18.57562  9.62094   1.000 31.10813  ?  4347 LYS   B O      1 
ATOM   2937 C  CB     . LYS   B  2  96  ? -93.49298  17.55301  6.26441   1.000 35.40420  ?  4347 LYS   B CB     1 
ATOM   2938 C  CG     . LYS   B  2  96  ? -92.58656  16.85478  5.23772   1.000 36.17109  ?  4347 LYS   B CG     1 
ATOM   2939 C  CD     . LYS   B  2  96  ? -93.38981  16.24069  4.09502   1.000 40.26796  ?  4347 LYS   B CD     1 
ATOM   2940 C  CE     . LYS   B  2  96  ? -92.46942  15.48116  3.13874   1.000 52.81327  ?  4347 LYS   B CE     1 
ATOM   2941 N  NZ     . LYS   B  2  96  ? -92.56505  14.00204  3.37051   1.000 56.82336  ?  4347 LYS   B NZ     1 
ATOM   2942 N  N      . TYR   B  2  97  ? -94.23994  19.90028  7.87620   1.000 29.65379  ?  4348 TYR   B N      1 
ATOM   2943 C  CA     . TYR   B  2  97  ? -95.13895  20.76563  8.62675   1.000 27.56926  ?  4348 TYR   B CA     1 
ATOM   2944 C  C      . TYR   B  2  97  ? -96.50484  20.73659  7.96632   1.000 30.61439  ?  4348 TYR   B C      1 
ATOM   2945 O  O      . TYR   B  2  97  ? -96.60951  20.72240  6.73977   1.000 34.09806  ?  4348 TYR   B O      1 
ATOM   2946 C  CB     . TYR   B  2  97  ? -94.57786  22.20539  8.70753   1.000 31.93341  ?  4348 TYR   B CB     1 
ATOM   2947 C  CG     . TYR   B  2  97  ? -93.25193  22.13858  9.42396   1.000 29.89414  ?  4348 TYR   B CG     1 
ATOM   2948 C  CD1    . TYR   B  2  97  ? -92.08777  21.85416  8.71962   1.000 30.90177  ?  4348 TYR   B CD1    1 
ATOM   2949 C  CD2    . TYR   B  2  97  ? -93.18208  22.23485  10.81643  1.000 29.13591  ?  4348 TYR   B CD2    1 
ATOM   2950 C  CE1    . TYR   B  2  97  ? -90.85736  21.71602  9.37142   1.000 27.09543  ?  4348 TYR   B CE1    1 
ATOM   2951 C  CE2    . TYR   B  2  97  ? -91.95389  22.09978  11.48291  1.000 25.15002  ?  4348 TYR   B CE2    1 
ATOM   2952 C  CZ     . TYR   B  2  97  ? -90.81543  21.82665  10.75679  1.000 25.12142  ?  4348 TYR   B CZ     1 
ATOM   2953 O  OH     . TYR   B  2  97  ? -89.61351  21.68439  11.41020  1.000 30.06839  ?  4348 TYR   B OH     1 
ATOM   2954 N  N      . VAL   B  2  98  ? -97.55243  20.72293  8.77477   1.000 30.45115  ?  4349 VAL   B N      1 
ATOM   2955 C  CA     . VAL   B  2  98  ? -98.90593  20.66307  8.25426   1.000 33.05119  ?  4349 VAL   B CA     1 
ATOM   2956 C  C      . VAL   B  2  98  ? -99.60989  21.96021  8.61857   1.000 35.50035  ?  4349 VAL   B C      1 
ATOM   2957 O  O      . VAL   B  2  98  ? -99.57064  22.39902  9.77794   1.000 34.44916  ?  4349 VAL   B O      1 
ATOM   2958 C  CB     . VAL   B  2  98  ? -99.66800  19.43567  8.77935   1.000 37.47487  ?  4349 VAL   B CB     1 
ATOM   2959 C  CG1    . VAL   B  2  98  ? -99.72632  19.44610  10.29720  1.000 36.18608  ?  4349 VAL   B CG1    1 
ATOM   2960 C  CG2    . VAL   B  2  98  ? -101.09235 19.42182  8.21154   1.000 38.57155  ?  4349 VAL   B CG2    1 
ATOM   2961 N  N      . GLN   B  2  99  ? -100.22856 22.58547  7.62225   1.000 34.95837  ?  4350 GLN   B N      1 
ATOM   2962 C  CA     . GLN   B  2  99  ? -101.00605 23.79823  7.82553   1.000 33.94398  ?  4350 GLN   B CA     1 
ATOM   2963 C  C      . GLN   B  2  99  ? -102.45820 23.42439  8.12377   1.000 39.76582  ?  4350 GLN   B C      1 
ATOM   2964 O  O      . GLN   B  2  99  ? -103.10503 22.72756  7.32999   1.000 38.84395  ?  4350 GLN   B O      1 
ATOM   2965 C  CB     . GLN   B  2  99  ? -100.89219 24.68954  6.59063   1.000 36.08392  ?  4350 GLN   B CB     1 
ATOM   2966 C  CG     . GLN   B  2  99  ? -99.61070  25.52607  6.52606   1.000 34.87660  ?  4350 GLN   B CG     1 
ATOM   2967 C  CD     . GLN   B  2  99  ? -98.34316  24.69912  6.57053   1.000 40.56304  ?  4350 GLN   B CD     1 
ATOM   2968 O  OE1    . GLN   B  2  99  ? -97.49118  24.89646  7.44863   1.000 36.66356  ?  4350 GLN   B OE1    1 
ATOM   2969 N  NE2    . GLN   B  2  99  ? -98.20208  23.76842  5.62146   1.000 32.73746  ?  4350 GLN   B NE2    1 
ATOM   2970 N  N      . ILE   B  2  100 ? -102.96200 23.86720  9.27012   1.000 35.75618  ?  4351 ILE   B N      1 
ATOM   2971 C  CA     . ILE   B  2  100 ? -104.31994 23.57715  9.71320   1.000 35.66723  ?  4351 ILE   B CA     1 
ATOM   2972 C  C      . ILE   B  2  100 ? -105.08650 24.89094  9.75553   1.000 39.37299  ?  4351 ILE   B C      1 
ATOM   2973 O  O      . ILE   B  2  100 ? -104.59393 25.86342  10.33827  1.000 34.24258  ?  4351 ILE   B O      1 
ATOM   2974 C  CB     . ILE   B  2  100 ? -104.36246 22.90328  11.09753  1.000 34.75662  ?  4351 ILE   B CB     1 
ATOM   2975 C  CG1    . ILE   B  2  100 ? -103.52844 21.60504  11.10887  1.000 34.94291  ?  4351 ILE   B CG1    1 
ATOM   2976 C  CG2    . ILE   B  2  100 ? -105.81118 22.69009  11.55409  1.000 34.47440  ?  4351 ILE   B CG2    1 
ATOM   2977 C  CD1    . ILE   B  2  100 ? -104.00432 20.53999  10.10266  1.000 37.14939  ?  4351 ILE   B CD1    1 
ATOM   2978 N  N      . PRO   B  2  101 ? -106.29028 24.95758  9.17885   1.000 37.42795  ?  4352 PRO   B N      1 
ATOM   2979 C  CA     . PRO   B  2  101 ? -107.12431 26.15653  9.33132   1.000 36.45312  ?  4352 PRO   B CA     1 
ATOM   2980 C  C      . PRO   B  2  101 ? -107.26318 26.52248  10.79418  1.000 38.64193  ?  4352 PRO   B C      1 
ATOM   2981 O  O      . PRO   B  2  101 ? -107.46698 25.65718  11.64841  1.000 37.80144  ?  4352 PRO   B O      1 
ATOM   2982 C  CB     . PRO   B  2  101 ? -108.47145 25.72948  8.73310   1.000 39.40373  ?  4352 PRO   B CB     1 
ATOM   2983 C  CG     . PRO   B  2  101 ? -108.12088 24.65729  7.75430   1.000 37.20566  ?  4352 PRO   B CG     1 
ATOM   2984 C  CD     . PRO   B  2  101 ? -106.94648 23.92605  8.35260   1.000 39.68029  ?  4352 PRO   B CD     1 
ATOM   2985 N  N      . THR   B  2  102 ? -107.16926 27.82238  11.08354  1.000 37.34056  ?  4353 THR   B N      1 
ATOM   2986 C  CA     . THR   B  2  102 ? -107.22078 28.26158  12.47430  1.000 35.28603  ?  4353 THR   B CA     1 
ATOM   2987 C  C      . THR   B  2  102 ? -108.49293 27.77803  13.15587  1.000 41.00492  ?  4353 THR   B C      1 
ATOM   2988 O  O      . THR   B  2  102 ? -108.47504 27.41767  14.33726  1.000 41.26799  ?  4353 THR   B O      1 
ATOM   2989 C  CB     . THR   B  2  102 ? -107.11491 29.79133  12.56416  1.000 40.69096  ?  4353 THR   B CB     1 
ATOM   2990 O  OG1    . THR   B  2  102 ? -105.87563 30.22132  11.98825  1.000 42.60130  ?  4353 THR   B OG1    1 
ATOM   2991 C  CG2    . THR   B  2  102 ? -107.14797 30.23936  14.01130  1.000 38.27131  ?  4353 THR   B CG2    1 
ATOM   2992 N  N      . THR   B  2  103 ? -109.60710 27.74880  12.42511  1.000 44.44587  ?  4354 THR   B N      1 
ATOM   2993 C  CA     . THR   B  2  103 ? -110.86800 27.33756  13.03071  1.000 44.92218  ?  4354 THR   B CA     1 
ATOM   2994 C  C      . THR   B  2  103 ? -110.88307 25.85800  13.40093  1.000 44.64604  ?  4354 THR   B C      1 
ATOM   2995 O  O      . THR   B  2  103 ? -111.71869 25.44897  14.21459  1.000 49.85786  ?  4354 THR   B O      1 
ATOM   2996 C  CB     . THR   B  2  103 ? -112.02910 27.64680  12.08167  1.000 43.15268  ?  4354 THR   B CB     1 
ATOM   2997 O  OG1    . THR   B  2  103 ? -111.76065 27.05163  10.80660  1.000 44.89892  ?  4354 THR   B OG1    1 
ATOM   2998 C  CG2    . THR   B  2  103 ? -112.17653 29.13976  11.89815  1.000 47.56385  ?  4354 THR   B CG2    1 
ATOM   2999 N  N      . CYS   B  2  104 ? -109.98690 25.05291  12.82891  1.000 43.57959  ?  4355 CYS   B N      1 
ATOM   3000 C  CA     . CYS   B  2  104 ? -109.92234 23.62042  13.10340  1.000 44.29921  ?  4355 CYS   B CA     1 
ATOM   3001 C  C      . CYS   B  2  104 ? -108.70842 23.24107  13.93545  1.000 46.28549  ?  4355 CYS   B C      1 
ATOM   3002 O  O      . CYS   B  2  104 ? -108.46386 22.04946  14.15068  1.000 42.49919  ?  4355 CYS   B O      1 
ATOM   3003 C  CB     . CYS   B  2  104 ? -109.90148 22.83248  11.79480  1.000 43.47881  ?  4355 CYS   B CB     1 
ATOM   3004 S  SG     . CYS   B  2  104 ? -111.32144 23.12630  10.69056  1.000 50.19285  ?  4355 CYS   B SG     1 
ATOM   3005 N  N      . ALA   B  2  105 ? -107.94406 24.22347  14.41360  1.000 45.05546  ?  4356 ALA   B N      1 
ATOM   3006 C  CA     . ALA   B  2  105 ? -106.67266 23.93890  15.06644  1.000 41.38460  ?  4356 ALA   B CA     1 
ATOM   3007 C  C      . ALA   B  2  105 ? -106.83775 23.36070  16.45955  1.000 41.99293  ?  4356 ALA   B C      1 
ATOM   3008 O  O      . ALA   B  2  105 ? -105.83200 23.00529  17.07927  1.000 43.95655  ?  4356 ALA   B O      1 
ATOM   3009 C  CB     . ALA   B  2  105 ? -105.81199 25.20259  15.13091  1.000 37.91992  ?  4356 ALA   B CB     1 
ATOM   3010 N  N      . ASN   B  2  106 ? -108.06267 23.26534  16.97742  1.000 42.35839  ?  4357 ASN   B N      1 
ATOM   3011 C  CA     . ASN   B  2  106 ? -108.26353 22.56065  18.24111  1.000 44.37214  ?  4357 ASN   B CA     1 
ATOM   3012 C  C      . ASN   B  2  106 ? -108.09047 21.05084  18.10167  1.000 44.13084  ?  4357 ASN   B C      1 
ATOM   3013 O  O      . ASN   B  2  106 ? -108.02865 20.35648  19.12178  1.000 43.13920  ?  4357 ASN   B O      1 
ATOM   3014 C  CB     . ASN   B  2  106 ? -109.65594 22.86228  18.79578  1.000 44.14920  ?  4357 ASN   B CB     1 
ATOM   3015 C  CG     . ASN   B  2  106 ? -110.76195 22.42177  17.84460  1.000 52.76381  ?  4357 ASN   B CG     1 
ATOM   3016 O  OD1    . ASN   B  2  106 ? -110.88358 22.94871  16.73053  1.000 56.69598  ?  4357 ASN   B OD1    1 
ATOM   3017 N  ND2    . ASN   B  2  106 ? -111.56902 21.45116  18.27190  1.000 54.09142  ?  4357 ASN   B ND2    1 
ATOM   3018 N  N      . ASP   B  2  107 ? -108.00784 20.52736  16.87559  1.000 41.43895  ?  4358 ASP   B N      1 
ATOM   3019 C  CA     . ASP   B  2  107 ? -107.93220 19.08086  16.64495  1.000 38.88514  ?  4358 ASP   B CA     1 
ATOM   3020 C  C      . ASP   B  2  107 ? -107.17711 18.81947  15.35114  1.000 36.84033  ?  4358 ASP   B C      1 
ATOM   3021 O  O      . ASP   B  2  107 ? -107.75576 18.40710  14.34648  1.000 38.16868  ?  4358 ASP   B O      1 
ATOM   3022 C  CB     . ASP   B  2  107 ? -109.33414 18.46608  16.59042  1.000 41.74179  ?  4358 ASP   B CB     1 
ATOM   3023 C  CG     . ASP   B  2  107 ? -109.31114 16.94934  16.35188  1.000 51.71920  ?  4358 ASP   B CG     1 
ATOM   3024 O  OD1    . ASP   B  2  107 ? -108.24719 16.30554  16.57301  1.000 41.16427  ?  4358 ASP   B OD1    1 
ATOM   3025 O  OD2    . ASP   B  2  107 ? -110.36913 16.40003  15.94329  1.000 49.71058  ?  4358 ASP   B OD2    1 
ATOM   3026 N  N      . PRO   B  2  108 ? -105.86254 19.04991  15.34222  1.000 37.76828  ?  4359 PRO   B N      1 
ATOM   3027 C  CA     . PRO   B  2  108 ? -105.10417 18.82141  14.10301  1.000 34.65896  ?  4359 PRO   B CA     1 
ATOM   3028 C  C      . PRO   B  2  108 ? -105.06380 17.36362  13.67018  1.000 35.75447  ?  4359 PRO   B C      1 
ATOM   3029 O  O      . PRO   B  2  108 ? -104.99267 17.09421  12.46567  1.000 34.18177  ?  4359 PRO   B O      1 
ATOM   3030 C  CB     . PRO   B  2  108 ? -103.70087 19.33825  14.44844  1.000 32.87910  ?  4359 PRO   B CB     1 
ATOM   3031 C  CG     . PRO   B  2  108 ? -103.92195 20.28412  15.60611  1.000 39.60113  ?  4359 PRO   B CG     1 
ATOM   3032 C  CD     . PRO   B  2  108 ? -105.04468 19.68686  16.38957  1.000 39.04596  ?  4359 PRO   B CD     1 
ATOM   3033 N  N      . VAL   B  2  109 ? -105.05280 16.40895  14.60338  1.000 36.04869  ?  4360 VAL   B N      1 
ATOM   3034 C  CA     . VAL   B  2  109 ? -105.04809 15.00927  14.18781  1.000 37.54426  ?  4360 VAL   B CA     1 
ATOM   3035 C  C      . VAL   B  2  109 ? -106.34515 14.68679  13.45617  1.000 37.16629  ?  4360 VAL   B C      1 
ATOM   3036 O  O      . VAL   B  2  109 ? -106.33603 14.11503  12.35790  1.000 40.50800  ?  4360 VAL   B O      1 
ATOM   3037 C  CB     . VAL   B  2  109 ? -104.82640 14.07781  15.39346  1.000 40.72181  ?  4360 VAL   B CB     1 
ATOM   3038 C  CG1    . VAL   B  2  109 ? -104.86268 12.63848  14.91932  1.000 37.02088  ?  4360 VAL   B CG1    1 
ATOM   3039 C  CG2    . VAL   B  2  109 ? -103.47317 14.36113  16.06573  1.000 34.39733  ?  4360 VAL   B CG2    1 
ATOM   3040 N  N      . GLY   B  2  110 ? -107.47914 15.07821  14.04401  1.000 38.67466  ?  4361 GLY   B N      1 
ATOM   3041 C  CA     . GLY   B  2  110 ? -108.75215 14.89269  13.36282  1.000 37.86442  ?  4361 GLY   B CA     1 
ATOM   3042 C  C      . GLY   B  2  110 ? -108.76921 15.54018  11.99387  1.000 41.73148  ?  4361 GLY   B C      1 
ATOM   3043 O  O      . GLY   B  2  110 ? -109.22849 14.94143  11.01680  1.000 40.34521  ?  4361 GLY   B O      1 
ATOM   3044 N  N      . PHE   B  2  111 ? -108.24417 16.76494  11.89170  1.000 40.73205  ?  4362 PHE   B N      1 
ATOM   3045 C  CA     . PHE   B  2  111 ? -108.29232 17.45504  10.60909  1.000 38.94992  ?  4362 PHE   B CA     1 
ATOM   3046 C  C      . PHE   B  2  111 ? -107.49313 16.71427  9.54371   1.000 39.37423  ?  4362 PHE   B C      1 
ATOM   3047 O  O      . PHE   B  2  111 ? -107.98823 16.48922  8.43423   1.000 44.09387  ?  4362 PHE   B O      1 
ATOM   3048 C  CB     . PHE   B  2  111 ? -107.79231 18.89137  10.73593  1.000 39.68964  ?  4362 PHE   B CB     1 
ATOM   3049 C  CG     . PHE   B  2  111 ? -107.99089 19.69038  9.48495   1.000 35.83924  ?  4362 PHE   B CG     1 
ATOM   3050 C  CD1    . PHE   B  2  111 ? -107.07887 19.61448  8.44995   1.000 40.80813  ?  4362 PHE   B CD1    1 
ATOM   3051 C  CD2    . PHE   B  2  111 ? -109.11465 20.48486  9.32990   1.000 38.39726  ?  4362 PHE   B CD2    1 
ATOM   3052 C  CE1    . PHE   B  2  111 ? -107.26027 20.34053  7.28002   1.000 41.62368  ?  4362 PHE   B CE1    1 
ATOM   3053 C  CE2    . PHE   B  2  111 ? -109.30632 21.20836  8.17333   1.000 44.38342  ?  4362 PHE   B CE2    1 
ATOM   3054 C  CZ     . PHE   B  2  111 ? -108.37269 21.13767  7.14337   1.000 41.71510  ?  4362 PHE   B CZ     1 
ATOM   3055 N  N      . THR   B  2  112 ? -106.23488 16.36431  9.83463   1.000 36.83321  ?  4363 THR   B N      1 
ATOM   3056 C  CA     . THR   B  2  112 ? -105.43431 15.69656  8.80859   1.000 37.58552  ?  4363 THR   B CA     1 
ATOM   3057 C  C      . THR   B  2  112 ? -106.04615 14.35768  8.42021   1.000 45.01698  ?  4363 THR   B C      1 
ATOM   3058 O  O      . THR   B  2  112 ? -105.94478 13.93749  7.26037   1.000 44.66284  ?  4363 THR   B O      1 
ATOM   3059 C  CB     . THR   B  2  112 ? -103.99011 15.49419  9.27679   1.000 42.85375  ?  4363 THR   B CB     1 
ATOM   3060 O  OG1    . THR   B  2  112 ? -103.96601 14.64040  10.43194  1.000 45.69964  ?  4363 THR   B OG1    1 
ATOM   3061 C  CG2    . THR   B  2  112 ? -103.35101 16.83857  9.63416   1.000 41.49967  ?  4363 THR   B CG2    1 
ATOM   3062 N  N      . LEU   B  2  113 ? -106.69116 13.68527  9.37355   1.000 43.99427  ?  4364 LEU   B N      1 
ATOM   3063 C  CA     . LEU   B  2  113 ? -107.29176 12.38092  9.10464   1.000 46.05119  ?  4364 LEU   B CA     1 
ATOM   3064 C  C      . LEU   B  2  113 ? -108.47004 12.50579  8.14764   1.000 52.07437  ?  4364 LEU   B C      1 
ATOM   3065 O  O      . LEU   B  2  113 ? -108.54123 11.79018  7.13989   1.000 54.58153  ?  4364 LEU   B O      1 
ATOM   3066 C  CB     . LEU   B  2  113 ? -107.73756 11.75124  10.42053  1.000 47.45209  ?  4364 LEU   B CB     1 
ATOM   3067 C  CG     . LEU   B  2  113 ? -107.70380 10.24168  10.58299  1.000 54.65844  ?  4364 LEU   B CG     1 
ATOM   3068 C  CD1    . LEU   B  2  113 ? -106.33142 9.71113   10.21958  1.000 52.69537  ?  4364 LEU   B CD1    1 
ATOM   3069 C  CD2    . LEU   B  2  113 ? -108.02285 9.93455   12.02613  1.000 52.33674  ?  4364 LEU   B CD2    1 
ATOM   3070 N  N      . LYS   B  2  114 ? -109.39310 13.43495  8.43931   1.000 45.84367  ?  4365 LYS   B N      1 
ATOM   3071 C  CA     . LYS   B  2  114 ? -110.64688 13.56306  7.71037   1.000 46.51185  ?  4365 LYS   B CA     1 
ATOM   3072 C  C      . LYS   B  2  114 ? -110.49841 14.22937  6.35336   1.000 52.76643  ?  4365 LYS   B C      1 
ATOM   3073 O  O      . LYS   B  2  114 ? -111.36070 14.03255  5.49266   1.000 57.97240  ?  4365 LYS   B O      1 
ATOM   3074 C  CB     . LYS   B  2  114 ? -111.65987 14.35819  8.53420   1.000 45.23665  ?  4365 LYS   B CB     1 
ATOM   3075 C  CG     . LYS   B  2  114 ? -112.11550 13.65371  9.80373   1.000 52.79008  ?  4365 LYS   B CG     1 
ATOM   3076 C  CD     . LYS   B  2  114 ? -112.98195 14.56747  10.66707  1.000 50.73621  ?  4365 LYS   B CD     1 
ATOM   3077 C  CE     . LYS   B  2  114 ? -113.45240 13.85672  11.93667  1.000 49.44051  ?  4365 LYS   B CE     1 
ATOM   3078 N  NZ     . LYS   B  2  114 ? -114.12128 14.78621  12.89369  1.000 53.34318  ?  4365 LYS   B NZ     1 
ATOM   3079 N  N      . ASN   B  2  115 ? -109.45432 15.01770  6.13302   1.000 51.14040  ?  4366 ASN   B N      1 
ATOM   3080 C  CA     . ASN   B  2  115 ? -109.35621 15.79700  4.90653   1.000 49.03579  ?  4366 ASN   B CA     1 
ATOM   3081 C  C      . ASN   B  2  115 ? -108.29494 15.21917  3.98370   1.000 47.38460  ?  4366 ASN   B C      1 
ATOM   3082 O  O      . ASN   B  2  115 ? -107.51336 14.33886  4.35467   1.000 51.45145  ?  4366 ASN   B O      1 
ATOM   3083 C  CB     . ASN   B  2  115 ? -109.05932 17.26697  5.21980   1.000 47.21918  ?  4366 ASN   B CB     1 
ATOM   3084 C  CG     . ASN   B  2  115 ? -110.23022 17.96307  5.87883   1.000 46.71810  ?  4366 ASN   B CG     1 
ATOM   3085 O  OD1    . ASN   B  2  115 ? -111.13525 18.44247  5.19794   1.000 47.72228  ?  4366 ASN   B OD1    1 
ATOM   3086 N  ND2    . ASN   B  2  115 ? -110.22306 18.02169  7.20785   1.000 45.55912  ?  4366 ASN   B ND2    1 
ATOM   3087 N  N      . THR   B  2  116 ? -108.26512 15.74032  2.76371   1.000 49.09523  ?  4367 THR   B N      1 
ATOM   3088 C  CA     . THR   B  2  116 ? -107.34971 15.23166  1.75892   1.000 50.58122  ?  4367 THR   B CA     1 
ATOM   3089 C  C      . THR   B  2  116 ? -106.73666 16.39880  0.99829   1.000 48.69756  ?  4367 THR   B C      1 
ATOM   3090 O  O      . THR   B  2  116 ? -107.34802 17.46338  0.85506   1.000 49.16704  ?  4367 THR   B O      1 
ATOM   3091 C  CB     . THR   B  2  116 ? -108.07126 14.23890  0.81704   1.000 56.91045  ?  4367 THR   B CB     1 
ATOM   3092 O  OG1    . THR   B  2  116 ? -107.34105 14.10314  -0.40820  1.000 61.97057  ?  4367 THR   B OG1    1 
ATOM   3093 C  CG2    . THR   B  2  116 ? -109.48995 14.69974  0.52310   1.000 52.71600  ?  4367 THR   B CG2    1 
ATOM   3094 N  N      . VAL   B  2  117 ? -105.50990 16.18350  0.52665   1.000 49.27008  ?  4368 VAL   B N      1 
ATOM   3095 C  CA     . VAL   B  2  117 ? -104.69374 17.20725  -0.11902  1.000 50.54035  ?  4368 VAL   B CA     1 
ATOM   3096 C  C      . VAL   B  2  117 ? -104.86473 17.11164  -1.63070  1.000 58.23405  ?  4368 VAL   B C      1 
ATOM   3097 O  O      . VAL   B  2  117 ? -104.69646 16.03276  -2.21780  1.000 55.40203  ?  4368 VAL   B O      1 
ATOM   3098 C  CB     . VAL   B  2  117 ? -103.20941 17.05041  0.25955   1.000 47.82158  ?  4368 VAL   B CB     1 
ATOM   3099 C  CG1    . VAL   B  2  117 ? -102.38260 18.17088  -0.36589  1.000 49.52030  ?  4368 VAL   B CG1    1 
ATOM   3100 C  CG2    . VAL   B  2  117 ? -103.02924 17.00656  1.76092   1.000 42.70231  ?  4368 VAL   B CG2    1 
ATOM   3101 N  N      . CYS   B  2  118 ? -105.15959 18.24226  -2.26944  1.000 57.52778  ?  4369 CYS   B N      1 
ATOM   3102 C  CA     . CYS   B  2  118 ? -105.24629 18.26225  -3.72454  1.000 60.09048  ?  4369 CYS   B CA     1 
ATOM   3103 C  C      . CYS   B  2  118 ? -103.89195 17.95315  -4.34357  1.000 61.48476  ?  4369 CYS   B C      1 
ATOM   3104 O  O      . CYS   B  2  118 ? -102.90021 18.64553  -4.08885  1.000 57.49023  ?  4369 CYS   B O      1 
ATOM   3105 C  CB     . CYS   B  2  118 ? -105.75003 19.61146  -4.23131  1.000 62.06571  ?  4369 CYS   B CB     1 
ATOM   3106 S  SG     . CYS   B  2  118 ? -105.53996 19.77504  -6.04201  1.000 67.69426  ?  4369 CYS   B SG     1 
ATOM   3107 N  N      . THR   B  2  119 ? -103.86150 16.92424  -5.18404  1.000 65.92538  ?  4370 THR   B N      1 
ATOM   3108 C  CA     . THR   B  2  119 ? -102.61686 16.48673  -5.79426  1.000 63.28519  ?  4370 THR   B CA     1 
ATOM   3109 C  C      . THR   B  2  119 ? -102.08967 17.45241  -6.85470  1.000 64.53929  ?  4370 THR   B C      1 
ATOM   3110 O  O      . THR   B  2  119 ? -100.95612 17.27282  -7.31724  1.000 64.65574  ?  4370 THR   B O      1 
ATOM   3111 C  CB     . THR   B  2  119 ? -102.82179 15.09821  -6.39346  1.000 64.00673  ?  4370 THR   B CB     1 
ATOM   3112 O  OG1    . THR   B  2  119 ? -101.73665 14.80131  -7.27836  1.000 72.20843  ?  4370 THR   B OG1    1 
ATOM   3113 C  CG2    . THR   B  2  119 ? -104.15322 15.03340  -7.15023  1.000 61.29449  ?  4370 THR   B CG2    1 
ATOM   3114 N  N      . VAL   B  2  120 ? -102.86122 18.47141  -7.23859  1.000 64.89172  ?  4371 VAL   B N      1 
ATOM   3115 C  CA     . VAL   B  2  120 ? -102.43564 19.40469  -8.27894  1.000 66.23413  ?  4371 VAL   B CA     1 
ATOM   3116 C  C      . VAL   B  2  120 ? -101.77206 20.62979  -7.66027  1.000 61.74399  ?  4371 VAL   B C      1 
ATOM   3117 O  O      . VAL   B  2  120 ? -100.63013 20.96368  -7.99312  1.000 64.10120  ?  4371 VAL   B O      1 
ATOM   3118 C  CB     . VAL   B  2  120 ? -103.62185 19.82893  -9.17007  1.000 65.79140  ?  4371 VAL   B CB     1 
ATOM   3119 C  CG1    . VAL   B  2  120 ? -103.20201 20.94770  -10.12496 1.000 58.31164  ?  4371 VAL   B CG1    1 
ATOM   3120 C  CG2    . VAL   B  2  120 ? -104.17911 18.63587  -9.93473  1.000 62.74446  ?  4371 VAL   B CG2    1 
ATOM   3121 N  N      . CYS   B  2  121 ? -102.48633 21.31364  -6.76571  1.000 58.97453  ?  4372 CYS   B N      1 
ATOM   3122 C  CA     . CYS   B  2  121 ? -102.03612 22.58183  -6.20647  1.000 62.27914  ?  4372 CYS   B CA     1 
ATOM   3123 C  C      . CYS   B  2  121 ? -101.52794 22.47974  -4.77217  1.000 61.49697  ?  4372 CYS   B C      1 
ATOM   3124 O  O      . CYS   B  2  121 ? -101.07883 23.49061  -4.22059  1.000 59.11917  ?  4372 CYS   B O      1 
ATOM   3125 C  CB     . CYS   B  2  121 ? -103.17064 23.60797  -6.25949  1.000 57.85339  ?  4372 CYS   B CB     1 
ATOM   3126 S  SG     . CYS   B  2  121 ? -104.52673 23.23909  -5.12246  1.000 60.41170  ?  4372 CYS   B SG     1 
ATOM   3127 N  N      . GLY   B  2  122 ? -101.61239 21.30775  -4.14270  1.000 56.75526  ?  4373 GLY   B N      1 
ATOM   3128 C  CA     . GLY   B  2  122 ? -101.09687 21.12091  -2.80199  1.000 52.53245  ?  4373 GLY   B CA     1 
ATOM   3129 C  C      . GLY   B  2  122 ? -101.91504 21.73027  -1.67843  1.000 56.62408  ?  4373 GLY   B C      1 
ATOM   3130 O  O      . GLY   B  2  122 ? -101.49345 21.63799  -0.51829  1.000 49.24343  ?  4373 GLY   B O      1 
ATOM   3131 N  N      . MET   B  2  123 ? -103.05594 22.35749  -1.97119  1.000 52.02430  ?  4374 MET   B N      1 
ATOM   3132 C  CA     . MET   B  2  123 ? -103.91734 22.90296  -0.93325  1.000 46.06420  ?  4374 MET   B CA     1 
ATOM   3133 C  C      . MET   B  2  123 ? -104.84983 21.81995  -0.39770  1.000 49.96519  ?  4374 MET   B C      1 
ATOM   3134 O  O      . MET   B  2  123 ? -105.01913 20.75872  -0.99831  1.000 53.61959  ?  4374 MET   B O      1 
ATOM   3135 C  CB     . MET   B  2  123 ? -104.73618 24.07880  -1.46703  1.000 48.56359  ?  4374 MET   B CB     1 
ATOM   3136 C  CG     . MET   B  2  123 ? -103.92947 25.13350  -2.19920  1.000 54.80924  ?  4374 MET   B CG     1 
ATOM   3137 S  SD     . MET   B  2  123 ? -102.87895 26.15451  -1.12670  1.000 58.37137  ?  4374 MET   B SD     1 
ATOM   3138 C  CE     . MET   B  2  123 ? -104.11364 26.93808  -0.06448  1.000 52.12692  ?  4374 MET   B CE     1 
ATOM   3139 N  N      . TRP   B  2  124 ? -105.45708 22.09312  0.75489   1.000 50.65648  ?  4375 TRP   B N      1 
ATOM   3140 C  CA     . TRP   B  2  124 ? -106.48388 21.20230  1.27283   1.000 49.48120  ?  4375 TRP   B CA     1 
ATOM   3141 C  C      . TRP   B  2  124 ? -107.73739 21.33082  0.42463   1.000 53.77860  ?  4375 TRP   B C      1 
ATOM   3142 O  O      . TRP   B  2  124 ? -108.18194 22.44513  0.13321   1.000 50.92389  ?  4375 TRP   B O      1 
ATOM   3143 C  CB     . TRP   B  2  124 ? -106.82202 21.53474  2.72495   1.000 49.81286  ?  4375 TRP   B CB     1 
ATOM   3144 C  CG     . TRP   B  2  124 ? -105.79380 21.10597  3.72960   1.000 49.98762  ?  4375 TRP   B CG     1 
ATOM   3145 C  CD1    . TRP   B  2  124 ? -104.95405 21.92082  4.43248   1.000 43.73886  ?  4375 TRP   B CD1    1 
ATOM   3146 C  CD2    . TRP   B  2  124 ? -105.49837 19.76270  4.15212   1.000 50.16702  ?  4375 TRP   B CD2    1 
ATOM   3147 N  NE1    . TRP   B  2  124 ? -104.15754 21.17404  5.26353   1.000 46.39609  ?  4375 TRP   B NE1    1 
ATOM   3148 C  CE2    . TRP   B  2  124 ? -104.46817 19.84698  5.11482   1.000 47.44901  ?  4375 TRP   B CE2    1 
ATOM   3149 C  CE3    . TRP   B  2  124 ? -106.00550 18.50035  3.81267   1.000 48.64770  ?  4375 TRP   B CE3    1 
ATOM   3150 C  CZ2    . TRP   B  2  124 ? -103.92853 18.71740  5.74122   1.000 45.09597  ?  4375 TRP   B CZ2    1 
ATOM   3151 C  CZ3    . TRP   B  2  124 ? -105.47112 17.37465  4.43892   1.000 47.45341  ?  4375 TRP   B CZ3    1 
ATOM   3152 C  CH2    . TRP   B  2  124 ? -104.44257 17.49300  5.39077   1.000 46.23070  ?  4375 TRP   B CH2    1 
ATOM   3153 N  N      . LYS   B  2  125 ? -108.32183 20.19509  0.04576   1.000 56.72212  ?  4376 LYS   B N      1 
ATOM   3154 C  CA     . LYS   B  2  125 ? -109.60914 20.22778  -0.63814  1.000 53.47810  ?  4376 LYS   B CA     1 
ATOM   3155 C  C      . LYS   B  2  125 ? -110.63616 20.91322  0.24713   1.000 53.22695  ?  4376 LYS   B C      1 
ATOM   3156 O  O      . LYS   B  2  125 ? -110.80998 20.54792  1.41351   1.000 58.94575  ?  4376 LYS   B O      1 
ATOM   3157 C  CB     . LYS   B  2  125 ? -110.07204 18.81488  -0.98410  1.000 51.40300  ?  4376 LYS   B CB     1 
ATOM   3158 C  CG     . LYS   B  2  125 ? -109.04732 18.00560  -1.75409  1.000 58.90183  ?  4376 LYS   B CG     1 
ATOM   3159 C  CD     . LYS   B  2  125 ? -109.64221 17.41622  -3.03070  1.000 65.71020  ?  4376 LYS   B CD     1 
ATOM   3160 C  CE     . LYS   B  2  125 ? -109.09914 16.00651  -3.33950  1.000 72.74885  ?  4376 LYS   B CE     1 
ATOM   3161 N  NZ     . LYS   B  2  125 ? -107.85764 15.90044  -4.20066  1.000 74.12817  ?  4376 LYS   B NZ     1 
ATOM   3162 N  N      . GLY   B  2  126 ? -111.31606 21.91238  -0.30466  1.000 52.20555  ?  4377 GLY   B N      1 
ATOM   3163 C  CA     . GLY   B  2  126 ? -112.30605 22.64244  0.45773   1.000 54.61810  ?  4377 GLY   B CA     1 
ATOM   3164 C  C      . GLY   B  2  126 ? -111.74597 23.61455  1.47022   1.000 58.00976  ?  4377 GLY   B C      1 
ATOM   3165 O  O      . GLY   B  2  126 ? -112.51945 24.20312  2.23189   1.000 52.64356  ?  4377 GLY   B O      1 
ATOM   3166 N  N      . TYR   B  2  127 ? -110.42921 23.80195  1.50911   1.000 58.04948  ?  4378 TYR   B N      1 
ATOM   3167 C  CA     . TYR   B  2  127 ? -109.79549 24.75963  2.41277   1.000 59.01465  ?  4378 TYR   B CA     1 
ATOM   3168 C  C      . TYR   B  2  127 ? -108.62090 25.42674  1.70580   1.000 60.12519  ?  4378 TYR   B C      1 
ATOM   3169 O  O      . TYR   B  2  127 ? -107.51069 25.51402  2.23506   1.000 58.01026  ?  4378 TYR   B O      1 
ATOM   3170 C  CB     . TYR   B  2  127 ? -109.32976 24.08579  3.70268   1.000 49.33964  ?  4378 TYR   B CB     1 
ATOM   3171 C  CG     . TYR   B  2  127 ? -110.43162 23.56182  4.59829   1.000 49.09534  ?  4378 TYR   B CG     1 
ATOM   3172 C  CD1    . TYR   B  2  127 ? -111.05712 24.39751  5.51477   1.000 47.94149  ?  4378 TYR   B CD1    1 
ATOM   3173 C  CD2    . TYR   B  2  127 ? -110.82037 22.22575  4.55466   1.000 49.94515  ?  4378 TYR   B CD2    1 
ATOM   3174 C  CE1    . TYR   B  2  127 ? -112.05171 23.93062  6.35048   1.000 49.54662  ?  4378 TYR   B CE1    1 
ATOM   3175 C  CE2    . TYR   B  2  127 ? -111.82371 21.74007  5.39644   1.000 50.64732  ?  4378 TYR   B CE2    1 
ATOM   3176 C  CZ     . TYR   B  2  127 ? -112.43555 22.60428  6.29133   1.000 52.50544  ?  4378 TYR   B CZ     1 
ATOM   3177 O  OH     . TYR   B  2  127 ? -113.43044 22.15805  7.13713   1.000 55.44583  ?  4378 TYR   B OH     1 
ATOM   3178 N  N      . GLY   B  2  128 ? -108.85293 25.88562  0.47884   1.000 56.19773  ?  4379 GLY   B N      1 
ATOM   3179 C  CA     . GLY   B  2  128 ? -107.79810 26.52770  -0.27560  1.000 53.53786  ?  4379 GLY   B CA     1 
ATOM   3180 C  C      . GLY   B  2  128 ? -107.74560 26.10296  -1.72564  1.000 55.26009  ?  4379 GLY   B C      1 
ATOM   3181 O  O      . GLY   B  2  128 ? -107.43587 26.91926  -2.59684  1.000 65.22257  ?  4379 GLY   B O      1 
ATOM   3182 N  N      . CYS   B  2  129 ? -108.04194 24.83458  -2.00424  1.000 62.20540  ?  4380 CYS   B N      1 
ATOM   3183 C  CA     . CYS   B  2  129 ? -108.00164 24.34068  -3.37686  1.000 65.99194  ?  4380 CYS   B CA     1 
ATOM   3184 C  C      . CYS   B  2  129 ? -109.15739 24.90940  -4.19185  1.000 69.16882  ?  4380 CYS   B C      1 
ATOM   3185 O  O      . CYS   B  2  129 ? -110.32027 24.84065  -3.77840  1.000 65.87276  ?  4380 CYS   B O      1 
ATOM   3186 C  CB     . CYS   B  2  129 ? -108.05934 22.81743  -3.40670  1.000 65.49026  ?  4380 CYS   B CB     1 
ATOM   3187 S  SG     . CYS   B  2  129 ? -108.29865 22.15761  -5.08959  1.000 70.59143  ?  4380 CYS   B SG     1 
ATOM   3188 N  N      . SER   B  2  130 ? -108.83348 25.45438  -5.36671  1.000 70.28633  ?  4381 SER   B N      1 
ATOM   3189 C  CA     . SER   B  2  130 ? -109.82775 26.07497  -6.23462  1.000 74.30821  ?  4381 SER   B CA     1 
ATOM   3190 C  C      . SER   B  2  130 ? -109.80643 25.48691  -7.64142  1.000 80.98059  ?  4381 SER   B C      1 
ATOM   3191 O  O      . SER   B  2  130 ? -110.31704 26.11403  -8.57717  1.000 81.45555  ?  4381 SER   B O      1 
ATOM   3192 C  CB     . SER   B  2  130 ? -109.61159 27.58762  -6.29053  1.000 71.95637  ?  4381 SER   B CB     1 
ATOM   3193 O  OG     . SER   B  2  130 ? -108.24869 27.88886  -6.54702  1.000 70.72958  ?  4381 SER   B OG     1 
ATOM   3194 N  N      . CYS   B  2  131 ? -109.22885 24.29280  -7.80882  1.000 80.89468  ?  4382 CYS   B N      1 
ATOM   3195 C  CA     . CYS   B  2  131 ? -109.10023 23.65658  -9.11742  1.000 84.12280  ?  4382 CYS   B CA     1 
ATOM   3196 C  C      . CYS   B  2  131 ? -110.44396 23.23765  -9.71018  1.000 85.90971  ?  4382 CYS   B C      1 
ATOM   3197 O  O      . CYS   B  2  131 ? -110.46203 22.63532  -10.79204 1.000 81.80062  ?  4382 CYS   B O      1 
ATOM   3198 C  CB     . CYS   B  2  131 ? -108.16678 22.44094  -9.01413  1.000 79.67665  ?  4382 CYS   B CB     1 
ATOM   3199 S  SG     . CYS   B  2  131 ? -106.42202 22.81766  -8.59895  1.000 81.22302  ?  4382 CYS   B SG     1 
ATOM   3200 N  N      . ASP   B  2  132 ? -111.55720 23.55888  -9.04375  1.000 86.36072  ?  4383 ASP   B N      1 
ATOM   3201 C  CA     . ASP   B  2  132 ? -112.89219 23.13784  -9.45183  1.000 85.72558  ?  4383 ASP   B CA     1 
ATOM   3202 C  C      . ASP   B  2  132 ? -113.75705 24.30193  -9.93462  1.000 87.70354  ?  4383 ASP   B C      1 
ATOM   3203 O  O      . ASP   B  2  132 ? -114.98590 24.17555  -9.98606  1.000 90.61215  ?  4383 ASP   B O      1 
ATOM   3204 C  CB     . ASP   B  2  132 ? -113.58076 22.41639  -8.29242  1.000 86.64596  ?  4383 ASP   B CB     1 
ATOM   3205 C  CG     . ASP   B  2  132 ? -112.71998 21.31130  -7.70101  1.000 92.15044  ?  4383 ASP   B CG     1 
ATOM   3206 O  OD1    . ASP   B  2  132 ? -112.59531 20.24438  -8.34394  1.000 88.27522  ?  4383 ASP   B OD1    1 
ATOM   3207 O  OD2    . ASP   B  2  132 ? -112.14960 21.52081  -6.60336  1.000 90.03127  ?  4383 ASP   B OD2    1 
ATOM   3208 N  N      . GLN   B  2  133 ? -113.14642 25.42898  -10.29109 1.000 85.59052  ?  4384 GLN   B N      1 
ATOM   3209 C  CA     . GLN   B  2  133 ? -113.89593 26.59701  -10.74406 1.000 83.78347  ?  4384 GLN   B CA     1 
ATOM   3210 C  C      . GLN   B  2  133 ? -113.37794 27.10931  -12.08940 1.000 84.89018  ?  4384 GLN   B C      1 
ATOM   3211 O  O      . GLN   B  2  133 ? -113.98459 27.98707  -12.71201 1.000 87.14137  ?  4384 GLN   B O      1 
ATOM   3212 C  CB     . GLN   B  2  133 ? -113.82674 27.70674  -9.69291  1.000 83.24182  ?  4384 GLN   B CB     1 
ATOM   3213 C  CG     . GLN   B  2  133 ? -112.41550 28.20466  -9.42009  1.000 80.36313  ?  4384 GLN   B CG     1 
ATOM   3214 C  CD     . GLN   B  2  133 ? -112.36548 29.29759  -8.36515  1.000 78.11234  ?  4384 GLN   B CD     1 
ATOM   3215 O  OE1    . GLN   B  2  133 ? -113.05004 29.22660  -7.33674  1.000 77.49818  ?  4384 GLN   B OE1    1 
ATOM   3216 N  NE2    . GLN   B  2  133 ? -111.54934 30.31967  -8.61687  1.000 73.60756  ?  4384 GLN   B NE2    1 
HETATM 3217 O  O1     . MES   C  3  .   ? -69.80045  34.87629  16.24044  1.000 41.17068  ?  7201 MES   A O1     1 
HETATM 3218 C  C2     . MES   C  3  .   ? -68.61529  34.79173  16.99814  1.000 41.73670  ?  7201 MES   A C2     1 
HETATM 3219 C  C3     . MES   C  3  .   ? -68.65768  35.69784  18.21179  1.000 40.10078  ?  7201 MES   A C3     1 
HETATM 3220 N  N4     . MES   C  3  .   ? -69.01019  37.09563  17.80473  1.000 44.01532  ?  7201 MES   A N4     1 
HETATM 3221 C  C5     . MES   C  3  .   ? -70.28922  37.09816  17.02361  1.000 44.84912  ?  7201 MES   A C5     1 
HETATM 3222 C  C6     . MES   C  3  .   ? -70.09637  36.19482  15.82696  1.000 41.80187  ?  7201 MES   A C6     1 
HETATM 3223 C  C7     . MES   C  3  .   ? -69.00442  38.03828  18.96948  1.000 50.64372  ?  7201 MES   A C7     1 
HETATM 3224 C  C8     . MES   C  3  .   ? -67.62937  38.12476  19.60578  1.000 53.49566  ?  7201 MES   A C8     1 
HETATM 3225 S  S      . MES   C  3  .   ? -67.53840  39.45124  20.85781  1.000 67.67697  ?  7201 MES   A S      1 
HETATM 3226 O  O1S    . MES   C  3  .   ? -68.93877  39.62345  21.32834  1.000 67.81263  ?  7201 MES   A O1S    1 
HETATM 3227 O  O2S    . MES   C  3  .   ? -67.00232  40.61518  20.11902  1.000 59.93480  ?  7201 MES   A O2S    1 
HETATM 3228 O  O3S    . MES   C  3  .   ? -66.63107  38.90678  21.89338  1.000 47.26953  ?  7201 MES   A O3S    1 
HETATM 3229 C  C1     . EDO   D  4  .   ? -71.66987  2.92610   13.57014  1.000 52.76708  ?  7202 EDO   A C1     1 
HETATM 3230 O  O1     . EDO   D  4  .   ? -72.72484  3.02147   14.50084  1.000 51.68741  ?  7202 EDO   A O1     1 
HETATM 3231 C  C2     . EDO   D  4  .   ? -70.36626  3.03817   14.32829  1.000 63.78131  ?  7202 EDO   A C2     1 
HETATM 3232 O  O2     . EDO   D  4  .   ? -70.64435  3.27302   15.69606  1.000 58.28960  ?  7202 EDO   A O2     1 
HETATM 3233 C  C1     . EDO   E  4  .   ? -77.66737  26.09011  46.01174  1.000 59.38409  ?  7203 EDO   A C1     1 
HETATM 3234 O  O1     . EDO   E  4  .   ? -79.01689  26.12328  45.56530  1.000 53.05717  ?  7203 EDO   A O1     1 
HETATM 3235 C  C2     . EDO   E  4  .   ? -77.45185  25.13004  47.16537  1.000 62.20207  ?  7203 EDO   A C2     1 
HETATM 3236 O  O2     . EDO   E  4  .   ? -76.74050  23.97848  46.75173  1.000 60.18629  ?  7203 EDO   A O2     1 
HETATM 3237 C  C1     . EDO   F  4  .   ? -72.22417  27.20475  47.19971  1.000 64.85670  ?  7204 EDO   A C1     1 
HETATM 3238 O  O1     . EDO   F  4  .   ? -72.69541  27.75334  48.42407  1.000 68.24775  ?  7204 EDO   A O1     1 
HETATM 3239 C  C2     . EDO   F  4  .   ? -72.99395  25.96511  46.77852  1.000 61.78696  ?  7204 EDO   A C2     1 
HETATM 3240 O  O2     . EDO   F  4  .   ? -72.19108  24.80149  46.90236  1.000 50.64253  ?  7204 EDO   A O2     1 
HETATM 3241 NA NA     . NA    G  5  .   ? -72.21041  24.46654  12.77523  1.000 41.58117  1  7205 NA    A NA     1 
HETATM 3242 C  C1     . EDO   H  4  .   ? -62.29631  18.89202  28.68683  1.000 55.94008  ?  7206 EDO   A C1     1 
HETATM 3243 O  O1     . EDO   H  4  .   ? -62.70674  17.53478  28.77048  1.000 66.73286  ?  7206 EDO   A O1     1 
HETATM 3244 C  C2     . EDO   H  4  .   ? -60.83557  19.01714  29.06707  1.000 62.55645  ?  7206 EDO   A C2     1 
HETATM 3245 O  O2     . EDO   H  4  .   ? -60.05290  19.36870  27.94680  1.000 58.61413  ?  7206 EDO   A O2     1 
HETATM 3246 C  C1     . EDO   I  4  .   ? -73.16621  37.77020  19.56616  1.000 53.92137  ?  7207 EDO   A C1     1 
HETATM 3247 O  O1     . EDO   I  4  .   ? -74.46086  38.00626  19.04435  1.000 49.15939  ?  7207 EDO   A O1     1 
HETATM 3248 C  C2     . EDO   I  4  .   ? -72.99969  38.43618  20.91723  1.000 54.99015  ?  7207 EDO   A C2     1 
HETATM 3249 O  O2     . EDO   I  4  .   ? -73.91887  37.94076  21.87133  1.000 47.92011  ?  7207 EDO   A O2     1 
HETATM 3250 C  C1     . EDO   J  4  .   ? -66.96165  11.31248  9.01538   1.000 56.83858  ?  7208 EDO   A C1     1 
HETATM 3251 O  O1     . EDO   J  4  .   ? -67.96068  12.27502  9.30992   1.000 45.51292  ?  7208 EDO   A O1     1 
HETATM 3252 C  C2     . EDO   J  4  .   ? -67.54324  10.24920  8.10914   1.000 57.05436  ?  7208 EDO   A C2     1 
HETATM 3253 O  O2     . EDO   J  4  .   ? -68.42455  10.85180  7.17971   1.000 56.78597  ?  7208 EDO   A O2     1 
HETATM 3254 N  N1     . A1IQS K  6  .   ? -85.10645  31.49015  44.52972  0.792 88.67719  ?  7209 A1IQS A N1     1 
HETATM 3255 N  N3     . A1IQS K  6  .   ? -83.64484  29.67165  41.89686  0.792 82.61772  ?  7209 A1IQS A N3     1 
HETATM 3256 C  C4     . A1IQS K  6  .   ? -84.11506  30.62271  42.76580  0.792 82.24131  ?  7209 A1IQS A C4     1 
HETATM 3257 C  C5     . A1IQS K  6  .   ? -82.91601  30.04276  40.68077  0.792 63.77306  ?  7209 A1IQS A C5     1 
HETATM 3258 C  C6     . A1IQS K  6  .   ? -85.86510  31.71334  45.77838  0.792 100.77700 ?  7209 A1IQS A C6     1 
HETATM 3259 C  C7     . A1IQS K  6  .   ? -85.20803  31.27974  47.11295  0.792 101.87449 ?  7209 A1IQS A C7     1 
HETATM 3260 C  C8     . A1IQS K  6  .   ? -86.29425  31.23839  48.21130  0.792 109.37650 ?  7209 A1IQS A C8     1 
HETATM 3261 C  C10    . A1IQS K  6  .   ? -88.50821  32.35827  47.54966  0.792 114.95505 ?  7209 A1IQS A C10    1 
HETATM 3262 C  C13    . A1IQS K  6  .   ? -90.79445  32.22002  44.29960  0.792 114.05465 ?  7209 A1IQS A C13    1 
HETATM 3263 C  C15    . A1IQS K  6  .   ? -91.18883  29.97178  45.60217  0.792 127.28516 ?  7209 A1IQS A C15    1 
HETATM 3264 C  C17    . A1IQS K  6  .   ? -92.84021  31.48236  45.65281  0.792 125.28543 ?  7209 A1IQS A C17    1 
HETATM 3265 C  C20    . A1IQS K  6  .   ? -89.97118  27.94041  46.02504  0.792 125.29159 ?  7209 A1IQS A C20    1 
HETATM 3266 C  C21    . A1IQS K  6  .   ? -90.04408  29.19218  45.43152  0.792 122.65392 ?  7209 A1IQS A C21    1 
HETATM 3267 C  C22    . A1IQS K  6  .   ? -87.31832  31.28098  45.66524  0.792 105.95849 ?  7209 A1IQS A C22    1 
HETATM 3268 C  C24    . A1IQS K  6  .   ? -84.81074  26.58237  43.56918  0.792 88.13148  ?  7209 A1IQS A C24    1 
HETATM 3269 N  N      . A1IQS K  6  .   ? -84.59215  28.00736  43.30604  0.792 88.16124  ?  7209 A1IQS A N      1 
HETATM 3270 C  C      . A1IQS K  6  .   ? -83.87040  28.32544  42.15834  0.792 88.35456  ?  7209 A1IQS A C      1 
HETATM 3271 O  O      . A1IQS K  6  .   ? -83.45081  27.45690  41.41384  0.792 113.80220 ?  7209 A1IQS A O      1 
HETATM 3272 C  C1     . A1IQS K  6  .   ? -85.11920  28.92127  44.23398  0.792 90.59473  ?  7209 A1IQS A C1     1 
HETATM 3273 C  C11    . A1IQS K  6  .   ? -88.69868  33.24348  45.24192  0.792 109.63810 ?  7209 A1IQS A C11    1 
HETATM 3274 C  C12    . A1IQS K  6  .   ? -90.20385  33.39571  45.09493  0.792 111.62062 ?  7209 A1IQS A C12    1 
HETATM 3275 C  C14    . A1IQS K  6  .   ? -91.58790  31.27800  45.14409  0.792 123.59262 ?  7209 A1IQS A C14    1 
HETATM 3276 C  C16    . A1IQS K  6  .   ? -92.24106  29.45982  46.37452  0.792 134.03447 ?  7209 A1IQS A C16    1 
HETATM 3277 C  C18    . A1IQS K  6  .   ? -92.17356  28.20597  46.97241  0.792 134.98573 ?  7209 A1IQS A C18    1 
HETATM 3278 C  C19    . A1IQS K  6  .   ? -91.02427  27.45267  46.78766  0.792 130.77809 ?  7209 A1IQS A C19    1 
HETATM 3279 C  C2     . A1IQS K  6  .   ? -84.81717  30.28304  43.89458  0.792 89.84884  ?  7209 A1IQS A C2     1 
HETATM 3280 C  C23    . A1IQS K  6  .   ? -84.46865  29.94897  47.07073  0.792 97.90619  ?  7209 A1IQS A C23    1 
HETATM 3281 C  C3     . A1IQS K  6  .   ? -84.55663  32.44751  43.71708  0.792 76.76407  ?  7209 A1IQS A C3     1 
HETATM 3282 C  C9     . A1IQS K  6  .   ? -87.24740  32.41611  48.40507  0.792 113.35331 ?  7209 A1IQS A C9     1 
HETATM 3283 N  N2     . A1IQS K  6  .   ? -83.95622  31.96606  42.65105  0.792 69.75961  ?  7209 A1IQS A N2     1 
HETATM 3284 N  N4     . A1IQS K  6  .   ? -88.22263  32.33393  46.11750  0.792 111.82262 ?  7209 A1IQS A N4     1 
HETATM 3285 N  N5     . A1IQS K  6  .   ? -90.51977  34.64859  44.38686  0.792 103.76624 ?  7209 A1IQS A N5     1 
HETATM 3286 N  N6     . A1IQS K  6  .   ? -93.24106  30.40350  46.39027  0.792 132.84242 ?  7209 A1IQS A N6     1 
HETATM 3287 O  O1     . A1IQS K  6  .   ? -85.78099  28.52632  45.18582  0.792 93.44791  ?  7209 A1IQS A O1     1 
HETATM 3288 O  O2     . A1IQS K  6  .   ? -84.21925  32.29099  47.38725  0.792 96.10518  ?  7209 A1IQS A O2     1 
HETATM 3289 O  O3     . A1IQS K  6  .   ? -86.54904  33.63509  48.13161  0.792 108.87287 ?  7209 A1IQS A O3     1 
HETATM 3290 O  O4     . A1IQS K  6  .   ? -87.95354  33.93874  44.57345  0.792 102.12430 ?  7209 A1IQS A O4     1 
HETATM 3291 C  C1     . EDO   L  4  .   ? -78.53712  20.37693  4.48830   1.000 52.20368  ?  7210 EDO   A C1     1 
HETATM 3292 O  O1     . EDO   L  4  .   ? -77.56522  21.38070  4.72224   1.000 47.70220  ?  7210 EDO   A O1     1 
HETATM 3293 C  C2     . EDO   L  4  .   ? -79.16974  20.46180  3.10679   1.000 48.18699  ?  7210 EDO   A C2     1 
HETATM 3294 O  O2     . EDO   L  4  .   ? -78.16655  20.34132  2.11967   1.000 60.24301  ?  7210 EDO   A O2     1 
HETATM 3295 C  C1     . EDO   M  4  .   ? -104.56378 26.39222  19.71291  1.000 59.04884  ?  7211 EDO   A C1     1 
HETATM 3296 O  O1     . EDO   M  4  .   ? -103.76271 26.01964  18.61323  1.000 59.33082  ?  7211 EDO   A O1     1 
HETATM 3297 C  C2     . EDO   M  4  .   ? -104.46005 27.88042  19.95150  1.000 54.80573  ?  7211 EDO   A C2     1 
HETATM 3298 O  O2     . EDO   M  4  .   ? -104.70548 28.15426  21.31904  1.000 61.75053  ?  7211 EDO   A O2     1 
HETATM 3299 C  C1     . EDO   N  4  .   ? -94.25614  38.77283  28.90573  1.000 54.75019  ?  7212 EDO   A C1     1 
HETATM 3300 O  O1     . EDO   N  4  .   ? -94.31893  39.31311  30.21444  1.000 66.67961  ?  7212 EDO   A O1     1 
HETATM 3301 C  C2     . EDO   N  4  .   ? -94.03681  39.88340  27.91103  1.000 47.31005  ?  7212 EDO   A C2     1 
HETATM 3302 O  O2     . EDO   N  4  .   ? -93.56901  39.32715  26.70256  1.000 45.15302  ?  7212 EDO   A O2     1 
HETATM 3303 C  C1     . EDO   O  4  .   ? -76.23696  15.44458  35.39901  1.000 39.69360  ?  7213 EDO   A C1     1 
HETATM 3304 O  O1     . EDO   O  4  .   ? -77.58633  15.27797  35.80317  1.000 48.71119  ?  7213 EDO   A O1     1 
HETATM 3305 C  C2     . EDO   O  4  .   ? -75.57566  14.09380  35.41396  1.000 45.90588  ?  7213 EDO   A C2     1 
HETATM 3306 O  O2     . EDO   O  4  .   ? -76.30383  13.20051  34.59165  1.000 55.56141  ?  7213 EDO   A O2     1 
HETATM 3307 S  S      . DMS   P  7  .   ? -58.56854  15.43440  12.44908  1.000 103.78621 ?  7214 DMS   A S      1 
HETATM 3308 O  O      . DMS   P  7  .   ? -58.47395  16.39181  11.28489  1.000 80.53931  ?  7214 DMS   A O      1 
HETATM 3309 C  C1     . DMS   P  7  .   ? -59.91245  16.00605  13.51780  1.000 76.77727  ?  7214 DMS   A C1     1 
HETATM 3310 C  C2     . DMS   P  7  .   ? -59.35765  13.92738  11.84030  1.000 91.14003  ?  7214 DMS   A C2     1 
HETATM 3311 C  C1     . EDO   Q  4  .   ? -75.87777  -0.25520  26.69213  1.000 50.87084  ?  7215 EDO   A C1     1 
HETATM 3312 O  O1     . EDO   Q  4  .   ? -74.71485  -0.70910  27.35017  1.000 61.12401  ?  7215 EDO   A O1     1 
HETATM 3313 C  C2     . EDO   Q  4  .   ? -77.12716  -0.86238  27.28283  1.000 55.88876  ?  7215 EDO   A C2     1 
HETATM 3314 O  O2     . EDO   Q  4  .   ? -77.28385  -0.47211  28.63466  1.000 65.60215  ?  7215 EDO   A O2     1 
HETATM 3315 N  N      . SAM   R  8  .   ? -90.04924  19.36382  25.56036  0.702 52.93838  ?  7216 SAM   A N      1 
HETATM 3316 C  CA     . SAM   R  8  .   ? -88.55421  19.45614  25.66958  0.702 50.59371  ?  7216 SAM   A CA     1 
HETATM 3317 C  C      . SAM   R  8  .   ? -87.85437  19.58781  24.31356  0.702 46.70259  ?  7216 SAM   A C      1 
HETATM 3318 O  O      . SAM   R  8  .   ? -86.62582  19.32879  24.33651  0.702 44.94974  ?  7216 SAM   A O      1 
HETATM 3319 O  OXT    . SAM   R  8  .   ? -88.52637  19.87421  23.29722  0.702 43.59272  -1 7216 SAM   A OXT    1 
HETATM 3320 C  CB     . SAM   R  8  .   ? -87.95959  18.22424  26.37001  0.702 47.77718  ?  7216 SAM   A CB     1 
HETATM 3321 C  CG     . SAM   R  8  .   ? -86.55052  18.27685  26.94796  0.702 48.02849  ?  7216 SAM   A CG     1 
HETATM 3322 S  SD     . SAM   R  8  .   ? -86.51984  17.60415  28.67485  0.702 68.31220  ?  7216 SAM   A SD     1 
HETATM 3323 C  CE     . SAM   R  8  .   ? -86.03643  19.13609  29.45693  0.702 54.68388  ?  7216 SAM   A CE     1 
HETATM 3324 C  "C5'"  . SAM   R  8  .   ? -84.86215  16.87551  29.13689  0.702 46.21131  ?  7216 SAM   A "C5'"  1 
HETATM 3325 C  "C4'"  . SAM   R  8  .   ? -84.68190  15.41594  28.74038  0.702 41.91447  ?  7216 SAM   A "C4'"  1 
HETATM 3326 O  "O4'"  . SAM   R  8  .   ? -83.36672  14.92168  29.06193  0.702 42.94277  ?  7216 SAM   A "O4'"  1 
HETATM 3327 C  "C3'"  . SAM   R  8  .   ? -85.65299  14.44661  29.42467  0.702 47.86191  ?  7216 SAM   A "C3'"  1 
HETATM 3328 O  "O3'"  . SAM   R  8  .   ? -86.75589  14.22929  28.55440  0.702 45.17069  ?  7216 SAM   A "O3'"  1 
HETATM 3329 C  "C2'"  . SAM   R  8  .   ? -84.80587  13.17978  29.67720  0.702 44.99938  ?  7216 SAM   A "C2'"  1 
HETATM 3330 O  "O2'"  . SAM   R  8  .   ? -85.44935  11.99816  29.21287  0.702 45.71016  ?  7216 SAM   A "O2'"  1 
HETATM 3331 C  "C1'"  . SAM   R  8  .   ? -83.47985  13.51400  28.99135  0.702 43.83672  ?  7216 SAM   A "C1'"  1 
HETATM 3332 N  N9     . SAM   R  8  .   ? -82.31920  12.90990  29.63897  0.702 42.18928  ?  7216 SAM   A N9     1 
HETATM 3333 C  C8     . SAM   R  8  .   ? -81.86637  13.11932  30.91286  0.702 39.61753  ?  7216 SAM   A C8     1 
HETATM 3334 N  N7     . SAM   R  8  .   ? -80.81520  12.40103  31.23949  0.702 39.94708  ?  7216 SAM   A N7     1 
HETATM 3335 C  C5     . SAM   R  8  .   ? -80.56066  11.66368  30.08806  0.702 38.60060  ?  7216 SAM   A C5     1 
HETATM 3336 C  C6     . SAM   R  8  .   ? -79.58016  10.69454  29.78014  0.702 42.13463  ?  7216 SAM   A C6     1 
HETATM 3337 N  N6     . SAM   R  8  .   ? -78.66070  10.25194  30.64736  0.702 40.48805  ?  7216 SAM   A N6     1 
HETATM 3338 N  N1     . SAM   R  8  .   ? -79.60921  10.14908  28.54227  0.702 32.97192  ?  7216 SAM   A N1     1 
HETATM 3339 C  C2     . SAM   R  8  .   ? -80.55612  10.54522  27.68619  0.702 40.26622  ?  7216 SAM   A C2     1 
HETATM 3340 N  N3     . SAM   R  8  .   ? -81.52899  11.44449  27.86863  0.702 40.47837  ?  7216 SAM   A N3     1 
HETATM 3341 C  C4     . SAM   R  8  .   ? -81.47691  11.96794  29.09644  0.702 40.20354  ?  7216 SAM   A C4     1 
HETATM 3342 H  HN1    . SAM   R  8  .   ? -90.49653  20.07300  25.83727  0.702 63.55126  ?  7216 SAM   A HN1    1 
HETATM 3343 H  HN2    . SAM   R  8  .   ? -90.36536  19.24095  24.74510  0.702 63.55126  ?  7216 SAM   A HN2    1 
HETATM 3344 H  HA     . SAM   R  8  .   ? -88.45102  20.29975  26.15549  0.702 60.73765  ?  7216 SAM   A HA     1 
HETATM 3345 H  HB1    . SAM   R  8  .   ? -88.56360  17.97440  27.09885  0.702 57.35782  ?  7216 SAM   A HB1    1 
HETATM 3346 H  HB2    . SAM   R  8  .   ? -87.98625  17.47841  25.73640  0.702 57.35782  ?  7216 SAM   A HB2    1 
HETATM 3347 H  HG1    . SAM   R  8  .   ? -85.93394  17.74902  26.40054  0.702 57.65939  ?  7216 SAM   A HG1    1 
HETATM 3348 H  HG2    . SAM   R  8  .   ? -86.22179  19.19873  26.97038  0.702 57.65939  ?  7216 SAM   A HG2    1 
HETATM 3349 H  HE1    . SAM   R  8  .   ? -85.65267  18.93985  30.33594  0.702 65.64586  ?  7216 SAM   A HE1    1 
HETATM 3350 H  HE2    . SAM   R  8  .   ? -85.37120  19.58573  28.89682  0.702 65.64586  ?  7216 SAM   A HE2    1 
HETATM 3351 H  HE3    . SAM   R  8  .   ? -86.82541  19.70670  29.55872  0.702 65.64586  ?  7216 SAM   A HE3    1 
HETATM 3352 H  "H5'1" . SAM   R  8  .   ? -84.19203  17.44141  28.70199  0.702 55.47878  ?  7216 SAM   A "H5'1" 1 
HETATM 3353 H  "H5'2" . SAM   R  8  .   ? -84.78324  16.98689  30.10633  0.702 55.47878  ?  7216 SAM   A "H5'2" 1 
HETATM 3354 H  "H4'"  . SAM   R  8  .   ? -84.73583  15.34267  27.76562  0.702 50.32256  ?  7216 SAM   A "H4'"  1 
HETATM 3355 H  "H3'"  . SAM   R  8  .   ? -86.01161  14.76821  30.27697  0.702 57.45950  ?  7216 SAM   A "H3'"  1 
HETATM 3356 H  "HO3'" . SAM   R  8  .   ? -86.63913  14.76628  27.90594  0.702 54.23003  ?  7216 SAM   A "HO3'" 1 
HETATM 3357 H  "H2'"  . SAM   R  8  .   ? -84.63690  13.04833  30.63251  0.702 54.02446  ?  7216 SAM   A "H2'"  1 
HETATM 3358 H  "HO2'" . SAM   R  8  .   ? -86.26270  12.20393  29.07638  0.702 54.87739  ?  7216 SAM   A "HO2'" 1 
HETATM 3359 H  "H1'"  . SAM   R  8  .   ? -83.44501  13.24136  28.05172  0.702 52.62927  ?  7216 SAM   A "H1'"  1 
HETATM 3360 H  H8     . SAM   R  8  .   ? -82.30346  13.75580  31.51477  0.702 47.56624  ?  7216 SAM   A H8     1 
HETATM 3361 H  HN61   . SAM   R  8  .   ? -78.65333  10.57672  31.46843  0.702 48.61087  ?  7216 SAM   A HN61   1 
HETATM 3362 H  HN62   . SAM   R  8  .   ? -78.07839  9.64331   30.38248  0.702 48.61087  ?  7216 SAM   A HN62   1 
HETATM 3363 H  H2     . SAM   R  8  .   ? -80.53117  10.11650  26.80640  0.702 48.34467  ?  7216 SAM   A H2     1 
HETATM 3364 H  HN3    . SAM   R  8  .   ? -90.42521  18.70715  26.01547  0.702 63.55126  ?  7216 SAM   A HN3    1 
HETATM 3365 NA NA     . NA    S  5  .   ? -81.25891  22.25291  38.26365  1.000 56.37106  1  7217 NA    A NA     1 
HETATM 3366 C  C1     . EDO   T  4  .   ? -87.79592  18.90400  5.74031   1.000 43.17642  ?  8201 EDO   B C1     1 
HETATM 3367 O  O1     . EDO   T  4  .   ? -88.99568  19.45573  6.21680   1.000 41.08764  ?  8201 EDO   B O1     1 
HETATM 3368 C  C2     . EDO   T  4  .   ? -86.62997  19.77080  6.16401   1.000 43.03209  ?  8201 EDO   B C2     1 
HETATM 3369 O  O2     . EDO   T  4  .   ? -85.42380  19.04988  6.12385   1.000 38.87257  ?  8201 EDO   B O2     1 
HETATM 3370 ZN ZN     . ZN    U  9  .   ? -97.08457  9.37075   10.94543  0.836 37.92099  2  8202 ZN    B ZN     1 
HETATM 3371 ZN ZN     . ZN    V  9  .   ? -106.37973 21.91322  -6.14469  1.000 69.29133  2  8203 ZN    B ZN     1 
HETATM 3372 C  C1     . EDO   W  4  .   ? -99.69236  7.19629   24.61828  1.000 71.45263  ?  8204 EDO   B C1     1 
HETATM 3373 O  O1     . EDO   W  4  .   ? -98.95899  7.41830   25.79926  1.000 82.85897  ?  8204 EDO   B O1     1 
HETATM 3374 C  C2     . EDO   W  4  .   ? -98.75294  6.79782   23.51114  1.000 67.53941  ?  8204 EDO   B C2     1 
HETATM 3375 O  O2     . EDO   W  4  .   ? -99.50758  6.50725   22.35362  1.000 64.21265  ?  8204 EDO   B O2     1 
HETATM 3376 N  N1     . IMD   X  10 .   ? -102.16971 9.10908   21.73774  1.000 63.57944  ?  8205 IMD   B N1     1 
HETATM 3377 C  C2     . IMD   X  10 .   ? -101.75930 10.30631  22.12064  1.000 59.76785  ?  8205 IMD   B C2     1 
HETATM 3378 N  N3     . IMD   X  10 .   ? -102.67467 10.79901  22.94091  1.000 66.79729  ?  8205 IMD   B N3     1 
HETATM 3379 C  C4     . IMD   X  10 .   ? -103.69657 9.89960   23.09272  1.000 68.79594  ?  8205 IMD   B C4     1 
HETATM 3380 C  C5     . IMD   X  10 .   ? -103.37430 8.82629   22.32527  1.000 70.11099  ?  8205 IMD   B C5     1 
HETATM 3381 C  C1     . EDO   Y  4  .   ? -107.08460 36.40825  12.31709  1.000 48.99265  ?  8206 EDO   B C1     1 
HETATM 3382 O  O1     . EDO   Y  4  .   ? -105.89400 36.32162  11.56567  1.000 59.40566  ?  8206 EDO   B O1     1 
HETATM 3383 C  C2     . EDO   Y  4  .   ? -107.61227 37.81558  12.17162  1.000 48.04368  ?  8206 EDO   B C2     1 
HETATM 3384 O  O2     . EDO   Y  4  .   ? -107.66797 38.14159  10.80574  1.000 44.29835  ?  8206 EDO   B O2     1 
HETATM 3385 O  O      . HOH   Z  11 .   ? -81.63835  27.04849  40.16395  1.000 50.90894  ?  7301 HOH   A O      1 
HETATM 3386 O  O      . HOH   Z  11 .   ? -70.91670  36.57943  25.61970  1.000 31.44335  ?  7302 HOH   A O      1 
HETATM 3387 O  O      . HOH   Z  11 .   ? -80.27965  9.71881   24.54422  1.000 34.71047  ?  7303 HOH   A O      1 
HETATM 3388 O  O      . HOH   Z  11 .   ? -60.80299  19.37419  22.02282  1.000 42.68102  ?  7304 HOH   A O      1 
HETATM 3389 O  O      . HOH   Z  11 .   ? -69.26350  29.52039  5.98647   1.000 40.09738  ?  7305 HOH   A O      1 
HETATM 3390 O  O      . HOH   Z  11 .   ? -79.40594  40.48181  24.27214  1.000 43.73202  ?  7306 HOH   A O      1 
HETATM 3391 O  O      . HOH   Z  11 .   ? -65.98718  33.83952  14.25207  1.000 41.31066  ?  7307 HOH   A O      1 
HETATM 3392 O  O      . HOH   Z  11 .   ? -89.84067  32.39123  8.95928   1.000 33.26487  ?  7308 HOH   A O      1 
HETATM 3393 O  O      . HOH   Z  11 .   ? -86.22613  22.53177  27.92232  1.000 39.96738  ?  7309 HOH   A O      1 
HETATM 3394 O  O      . HOH   Z  11 .   ? -87.35882  18.29215  21.27583  1.000 30.78653  ?  7310 HOH   A O      1 
HETATM 3395 O  O      . HOH   Z  11 .   ? -70.56752  22.24048  1.91242   1.000 41.99528  ?  7311 HOH   A O      1 
HETATM 3396 O  O      . HOH   Z  11 .   ? -94.30767  17.01790  15.22647  1.000 36.86434  ?  7312 HOH   A O      1 
HETATM 3397 O  O      . HOH   Z  11 .   ? -82.55040  27.38474  6.86216   1.000 38.54035  ?  7313 HOH   A O      1 
HETATM 3398 O  O      . HOH   Z  11 .   ? -83.13181  29.89341  28.76075  1.000 29.14444  ?  7314 HOH   A O      1 
HETATM 3399 O  O      . HOH   Z  11 .   ? -87.43456  9.95435   13.82578  1.000 37.40465  ?  7315 HOH   A O      1 
HETATM 3400 O  O      . HOH   Z  11 .   ? -62.00034  23.10084  34.95945  1.000 38.96407  ?  7316 HOH   A O      1 
HETATM 3401 O  O      . HOH   Z  11 .   ? -78.65622  20.32249  31.94096  1.000 25.68457  ?  7317 HOH   A O      1 
HETATM 3402 O  O      . HOH   Z  11 .   ? -76.13274  -9.34299  29.20233  1.000 45.25153  ?  7318 HOH   A O      1 
HETATM 3403 O  O      . HOH   Z  11 .   ? -88.46032  25.11081  30.53615  1.000 40.76882  ?  7319 HOH   A O      1 
HETATM 3404 O  O      . HOH   Z  11 .   ? -59.79164  25.30889  28.39928  1.000 35.84794  ?  7320 HOH   A O      1 
HETATM 3405 O  O      . HOH   Z  11 .   ? -73.44841  18.30585  43.53002  1.000 47.04538  ?  7321 HOH   A O      1 
HETATM 3406 O  O      . HOH   Z  11 .   ? -64.00635  15.83420  17.23551  1.000 44.32234  ?  7322 HOH   A O      1 
HETATM 3407 O  O      . HOH   Z  11 .   ? -71.10297  22.99501  32.40427  1.000 31.38955  ?  7323 HOH   A O      1 
HETATM 3408 O  O      . HOH   Z  11 .   ? -73.997    -0.671    3.415     1.000 64.74749  ?  7324 HOH   A O      1 
HETATM 3409 O  O      . HOH   Z  11 .   ? -70.23287  26.04326  13.40724  1.000 31.45843  ?  7325 HOH   A O      1 
HETATM 3410 O  O      . HOH   Z  11 .   ? -87.79315  38.54561  23.17973  1.000 26.93046  ?  7326 HOH   A O      1 
HETATM 3411 O  O      . HOH   Z  11 .   ? -84.88629  40.72100  28.47337  1.000 34.79827  ?  7327 HOH   A O      1 
HETATM 3412 O  O      . HOH   Z  11 .   ? -72.92829  34.84412  42.92523  1.000 39.76599  ?  7328 HOH   A O      1 
HETATM 3413 O  O      . HOH   Z  11 .   ? -92.73649  15.60063  17.59706  1.000 33.28474  ?  7329 HOH   A O      1 
HETATM 3414 O  O      . HOH   Z  11 .   ? -75.16347  8.69072   30.65306  1.000 47.11655  ?  7330 HOH   A O      1 
HETATM 3415 O  O      . HOH   Z  11 .   ? -79.30707  17.29211  35.13207  1.000 35.23920  ?  7331 HOH   A O      1 
HETATM 3416 O  O      . HOH   Z  11 .   ? -77.80281  19.38895  28.56052  1.000 28.12689  ?  7332 HOH   A O      1 
HETATM 3417 O  O      . HOH   Z  11 .   ? -72.49946  42.71128  38.60147  1.000 37.85566  ?  7333 HOH   A O      1 
HETATM 3418 O  O      . HOH   Z  11 .   ? -79.25320  37.57729  43.60868  1.000 44.39453  ?  7334 HOH   A O      1 
HETATM 3419 O  O      . HOH   Z  11 .   ? -61.01458  33.26047  18.39614  1.000 42.44362  ?  7335 HOH   A O      1 
HETATM 3420 O  O      . HOH   Z  11 .   ? -75.06149  27.24895  43.63205  1.000 39.38454  ?  7336 HOH   A O      1 
HETATM 3421 O  O      . HOH   Z  11 .   ? -90.57631  16.79622  16.22046  1.000 30.06375  ?  7337 HOH   A O      1 
HETATM 3422 O  O      . HOH   Z  11 .   ? -83.74754  37.06300  35.50340  1.000 37.65877  ?  7338 HOH   A O      1 
HETATM 3423 O  O      . HOH   Z  11 .   ? -83.72566  3.45839   19.53859  1.000 50.80295  ?  7339 HOH   A O      1 
HETATM 3424 O  O      . HOH   Z  11 .   ? -65.86864  27.32269  10.69468  1.000 39.67263  ?  7340 HOH   A O      1 
HETATM 3425 O  O      . HOH   Z  11 .   ? -80.62723  36.83160  35.79909  1.000 30.83601  ?  7341 HOH   A O      1 
HETATM 3426 O  O      . HOH   Z  11 .   ? -83.44551  18.78465  9.42352   1.000 35.48072  ?  7342 HOH   A O      1 
HETATM 3427 O  O      . HOH   Z  11 .   ? -69.73466  40.82067  25.99534  1.000 36.95169  ?  7343 HOH   A O      1 
HETATM 3428 O  O      . HOH   Z  11 .   ? -80.50957  2.88961   27.54871  1.000 42.57423  ?  7344 HOH   A O      1 
HETATM 3429 O  O      . HOH   Z  11 .   ? -68.46188  42.62223  29.04295  1.000 37.54758  ?  7345 HOH   A O      1 
HETATM 3430 O  O      . HOH   Z  11 .   ? -95.57649  9.62466   21.97676  1.000 43.70790  ?  7346 HOH   A O      1 
HETATM 3431 O  O      . HOH   Z  11 .   ? -89.64440  29.58692  9.51294   1.000 34.86920  ?  7347 HOH   A O      1 
HETATM 3432 O  O      . HOH   Z  11 .   ? -61.99842  42.33187  35.68333  1.000 36.84927  ?  7348 HOH   A O      1 
HETATM 3433 O  O      . HOH   Z  11 .   ? -76.39442  41.18289  31.50477  1.000 39.75551  ?  7349 HOH   A O      1 
HETATM 3434 O  O      . HOH   Z  11 .   ? -91.11249  27.87230  15.90025  1.000 25.75863  ?  7350 HOH   A O      1 
HETATM 3435 O  O      . HOH   Z  11 .   ? -71.30323  32.68922  42.14177  1.000 32.97845  ?  7351 HOH   A O      1 
HETATM 3436 O  O      . HOH   Z  11 .   ? -77.03546  34.46926  46.29477  1.000 51.86716  ?  7352 HOH   A O      1 
HETATM 3437 O  O      . HOH   Z  11 .   ? -65.51924  17.82001  35.34783  1.000 48.04656  ?  7353 HOH   A O      1 
HETATM 3438 O  O      . HOH   Z  11 .   ? -65.60553  12.77423  28.98974  1.000 48.84306  ?  7354 HOH   A O      1 
HETATM 3439 O  O      . HOH   Z  11 .   ? -63.26997  38.31606  40.40134  1.000 42.75600  ?  7355 HOH   A O      1 
HETATM 3440 O  O      . HOH   Z  11 .   ? -84.36517  21.02601  8.04978   1.000 31.36573  ?  7356 HOH   A O      1 
HETATM 3441 O  O      . HOH   Z  11 .   ? -83.86321  28.01376  38.18483  1.000 46.37640  ?  7357 HOH   A O      1 
HETATM 3442 O  O      . HOH   Z  11 .   ? -83.19629  -8.35170  26.73916  1.000 45.24973  ?  7358 HOH   A O      1 
HETATM 3443 O  O      . HOH   Z  11 .   ? -66.77245  14.94335  33.84537  1.000 54.34205  ?  7359 HOH   A O      1 
HETATM 3444 O  O      . HOH   Z  11 .   ? -84.03077  25.51975  3.17673   1.000 38.42965  ?  7360 HOH   A O      1 
HETATM 3445 O  O      . HOH   Z  11 .   ? -93.03808  23.08818  26.41663  1.000 41.79324  ?  7361 HOH   A O      1 
HETATM 3446 O  O      . HOH   Z  11 .   ? -81.17142  38.19170  39.25763  1.000 39.84462  ?  7362 HOH   A O      1 
HETATM 3447 O  O      . HOH   Z  11 .   ? -64.85795  29.34081  42.41229  1.000 45.42041  ?  7363 HOH   A O      1 
HETATM 3448 O  O      . HOH   Z  11 .   ? -83.90520  37.84648  38.13718  1.000 46.70390  ?  7364 HOH   A O      1 
HETATM 3449 O  O      . HOH   Z  11 .   ? -58.40704  22.50699  28.27069  1.000 53.07432  ?  7365 HOH   A O      1 
HETATM 3450 O  O      . HOH   Z  11 .   ? -80.44884  12.13888  25.04978  1.000 34.09420  ?  7366 HOH   A O      1 
HETATM 3451 O  O      . HOH   Z  11 .   ? -78.52320  2.05352   29.44184  1.000 49.66241  ?  7367 HOH   A O      1 
HETATM 3452 O  O      . HOH   Z  11 .   ? -89.42871  39.69481  34.35690  1.000 42.35402  ?  7368 HOH   A O      1 
HETATM 3453 O  O      . HOH   Z  11 .   ? -79.531    -1.031    17.803    1.000 33.25609  ?  7369 HOH   A O      1 
HETATM 3454 O  O      . HOH   Z  11 .   ? -76.69120  39.56121  24.72315  1.000 36.01811  ?  7370 HOH   A O      1 
HETATM 3455 O  O      . HOH   Z  11 .   ? -80.58343  24.08384  39.26501  1.000 42.08719  ?  7371 HOH   A O      1 
HETATM 3456 O  O      . HOH   Z  11 .   ? -80.32703  -1.39428  26.51604  1.000 52.83348  ?  7372 HOH   A O      1 
HETATM 3457 O  O      . HOH   Z  11 .   ? -64.45197  7.88458   19.15406  1.000 57.24835  ?  7373 HOH   A O      1 
HETATM 3458 O  O      . HOH   Z  11 .   ? -76.41766  19.86390  43.38397  1.000 47.87118  ?  7374 HOH   A O      1 
HETATM 3459 O  O      . HOH   Z  11 .   ? -67.54127  35.54062  44.97230  1.000 52.51915  ?  7375 HOH   A O      1 
HETATM 3460 O  O      . HOH   Z  11 .   ? -71.81104  38.54342  24.02589  1.000 41.07256  ?  7376 HOH   A O      1 
HETATM 3461 O  O      . HOH   Z  11 .   ? -83.21779  35.55660  13.75967  1.000 39.60250  ?  7377 HOH   A O      1 
HETATM 3462 O  O      . HOH   Z  11 .   ? -86.08393  42.78876  35.37428  1.000 48.47017  ?  7378 HOH   A O      1 
HETATM 3463 O  O      . HOH   Z  11 .   ? -67.37719  21.41844  0.25798   1.000 51.00056  ?  7379 HOH   A O      1 
HETATM 3464 O  O      . HOH   Z  11 .   ? -74.31392  30.91557  48.93142  1.000 51.30472  ?  7380 HOH   A O      1 
HETATM 3465 O  O      . HOH   Z  11 .   ? -55.689    33.057    24.561    1.000 55.33138  ?  7381 HOH   A O      1 
HETATM 3466 O  O      . HOH   Z  11 .   ? -85.97257  35.39420  13.57505  1.000 40.00979  ?  7382 HOH   A O      1 
HETATM 3467 O  O      . HOH   Z  11 .   ? -61.40168  30.60809  34.06774  1.000 40.13413  ?  7383 HOH   A O      1 
HETATM 3468 O  O      . HOH   Z  11 .   ? -69.74513  7.34249   19.20419  1.000 50.15600  ?  7384 HOH   A O      1 
HETATM 3469 O  O      . HOH   Z  11 .   ? -83.77433  24.95449  37.68703  1.000 62.90504  ?  7385 HOH   A O      1 
HETATM 3470 O  O      . HOH   Z  11 .   ? -76.05625  3.43233   29.60811  1.000 52.65240  ?  7386 HOH   A O      1 
HETATM 3471 O  O      . HOH   Z  11 .   ? -74.23021  38.29935  44.67717  1.000 54.11717  ?  7387 HOH   A O      1 
HETATM 3472 O  O      . HOH   Z  11 .   ? -98.60881  24.85114  25.37317  1.000 47.26353  ?  7388 HOH   A O      1 
HETATM 3473 O  O      . HOH   Z  11 .   ? -63.679    38.534    42.195    1.000 62.36360  ?  7389 HOH   A O      1 
HETATM 3474 O  O      . HOH   AA 11 .   ? -105.69914 16.75314  17.50701  1.000 41.24160  ?  8301 HOH   B O      1 
HETATM 3475 O  O      . HOH   AA 11 .   ? -98.46878  28.43135  13.67760  1.000 33.33307  ?  8302 HOH   B O      1 
HETATM 3476 O  O      . HOH   AA 11 .   ? -112.64291 17.68923  16.76420  1.000 52.68771  ?  8303 HOH   B O      1 
HETATM 3477 O  O      . HOH   AA 11 .   ? -96.16671  25.28910  20.51100  1.000 36.37324  ?  8304 HOH   B O      1 
HETATM 3478 O  O      . HOH   AA 11 .   ? -90.69359  9.29880   15.81081  1.000 47.95955  ?  8305 HOH   B O      1 
HETATM 3479 O  O      . HOH   AA 11 .   ? -99.15356  20.21169  0.09283   1.000 47.29177  ?  8306 HOH   B O      1 
HETATM 3480 O  O      . HOH   AA 11 .   ? -96.06910  31.15063  7.97698   1.000 35.75661  ?  8307 HOH   B O      1 
HETATM 3481 O  O      . HOH   AA 11 .   ? -92.70025  31.69815  8.70578   1.000 42.60484  ?  8308 HOH   B O      1 
HETATM 3482 O  O      . HOH   AA 11 .   ? -110.16136 17.86536  2.44411   1.000 51.04726  ?  8309 HOH   B O      1 
HETATM 3483 O  O      . HOH   AA 11 .   ? -99.62617  30.80882  16.44885  1.000 42.73206  ?  8310 HOH   B O      1 
HETATM 3484 O  O      . HOH   AA 11 .   ? -95.54291  2.46145   10.01311  1.000 57.44569  ?  8311 HOH   B O      1 
HETATM 3485 O  O      . HOH   AA 11 .   ? -98.20878  10.34753  21.51299  1.000 43.74952  ?  8312 HOH   B O      1 
HETATM 3486 O  O      . HOH   AA 11 .   ? -93.90569  30.84754  6.31307   1.000 39.88648  ?  8313 HOH   B O      1 
HETATM 3487 O  O      . HOH   AA 11 .   ? -109.33077 29.57266  9.53203   1.000 46.55271  ?  8314 HOH   B O      1 
HETATM 3488 O  O      . HOH   AA 11 .   ? -98.58063  23.72642  20.66596  1.000 40.24582  ?  8315 HOH   B O      1 
HETATM 3489 O  O      . HOH   AA 11 .   ? -92.77199  22.43648  0.72126   1.000 42.53283  ?  8316 HOH   B O      1 
HETATM 3490 O  O      . HOH   AA 11 .   ? -96.78116  21.29117  -0.84752  1.000 49.79386  ?  8317 HOH   B O      1 
HETATM 3491 O  O      . HOH   AA 11 .   ? -103.77363 13.56712  23.96046  1.000 51.74989  ?  8318 HOH   B O      1 
HETATM 3492 O  O      . HOH   AA 11 .   ? -102.98293 20.10270  19.95635  1.000 45.63612  ?  8319 HOH   B O      1 
HETATM 3493 O  O      . HOH   AA 11 .   ? -92.66527  6.33145   9.94691   1.000 62.13285  ?  8320 HOH   B O      1 
HETATM 3494 O  O      . HOH   AA 11 .   ? -98.60209  17.75928  -0.27881  1.000 53.31520  ?  8321 HOH   B O      1 
# 
