data_8YKJ
# 
_entry.id   8YKJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8YKJ         pdb_00008ykj 10.2210/pdb8ykj/pdb 
WWPDB D_1300043861 ?            ?                   
# 
_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       2024-11-27 
# 
_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                        8YKJ 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rmsl_2040@163.com 
_pdbx_contact_author.name_first         Jian 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9511-4219 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhou, X.L.' 1 ? 
'Lin, C.'    2 ? 
'Li, W.W.'   3 ? 
'Zhang, J.'  4 ? 
'Li, J.'     5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            276 
_citation.language                  ? 
_citation.page_first                133706 
_citation.page_last                 133706 
_citation.title                     
'Crystal structures of coronaviral main proteases in complex with the non-covalent inhibitor X77.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2024.133706 
_citation.pdbx_database_id_PubMed   38981557 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Jiang, H.' 1 ? 
primary 'Li, W.'    2 ? 
primary 'Zhou, X.'  3 ? 
primary 'Zhang, J.' 4 ? 
primary 'Li, J.'    5 ? 
# 
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 'Non-structural protein 11'                                                                                  
33305.016 2   ? N142A ? ? 
2 non-polymer syn 'N-(4-tert-butylphenyl)-N-[(1R)-2-(cyclohexylamino)-2-oxo-1-(pyridin-3-yl)ethyl]-1H-imidazole-4-carboxamide' 
459.583   2   ? ?     ? ? 
3 water       nat water                                                                                                        
18.015    106 ? ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        nsp11 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;FRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSM
QNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYM
HHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPL
TQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;FRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSM
QNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYM
HHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPL
TQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGV
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'N-(4-tert-butylphenyl)-N-[(1R)-2-(cyclohexylamino)-2-oxo-1-(pyridin-3-yl)ethyl]-1H-imidazole-4-carboxamide' X77 
3 water                                                                                                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PHE n 
1 2   ARG n 
1 3   LYS n 
1 4   MET n 
1 5   ALA n 
1 6   PHE n 
1 7   PRO n 
1 8   SER n 
1 9   GLY n 
1 10  LYS n 
1 11  VAL n 
1 12  GLU n 
1 13  GLY n 
1 14  CYS n 
1 15  MET n 
1 16  VAL n 
1 17  GLN n 
1 18  VAL n 
1 19  THR n 
1 20  CYS n 
1 21  GLY n 
1 22  THR n 
1 23  THR n 
1 24  THR n 
1 25  LEU n 
1 26  ASN n 
1 27  GLY n 
1 28  LEU n 
1 29  TRP n 
1 30  LEU n 
1 31  ASP n 
1 32  ASP n 
1 33  VAL n 
1 34  VAL n 
1 35  TYR n 
1 36  CYS n 
1 37  PRO n 
1 38  ARG n 
1 39  HIS n 
1 40  VAL n 
1 41  ILE n 
1 42  CYS n 
1 43  THR n 
1 44  SER n 
1 45  GLU n 
1 46  ASP n 
1 47  MET n 
1 48  LEU n 
1 49  ASN n 
1 50  PRO n 
1 51  ASN n 
1 52  TYR n 
1 53  GLU n 
1 54  ASP n 
1 55  LEU n 
1 56  LEU n 
1 57  ILE n 
1 58  ARG n 
1 59  LYS n 
1 60  SER n 
1 61  ASN n 
1 62  HIS n 
1 63  ASN n 
1 64  PHE n 
1 65  LEU n 
1 66  VAL n 
1 67  GLN n 
1 68  ALA n 
1 69  GLY n 
1 70  ASN n 
1 71  VAL n 
1 72  GLN n 
1 73  LEU n 
1 74  ARG n 
1 75  VAL n 
1 76  ILE n 
1 77  GLY n 
1 78  HIS n 
1 79  SER n 
1 80  MET n 
1 81  GLN n 
1 82  ASN n 
1 83  CYS n 
1 84  VAL n 
1 85  LEU n 
1 86  LYS n 
1 87  LEU n 
1 88  LYS n 
1 89  VAL n 
1 90  ASP n 
1 91  THR n 
1 92  ALA n 
1 93  ASN n 
1 94  PRO n 
1 95  LYS n 
1 96  THR n 
1 97  PRO n 
1 98  LYS n 
1 99  TYR n 
1 100 LYS n 
1 101 PHE n 
1 102 VAL n 
1 103 ARG n 
1 104 ILE n 
1 105 GLN n 
1 106 PRO n 
1 107 GLY n 
1 108 GLN n 
1 109 THR n 
1 110 PHE n 
1 111 SER n 
1 112 VAL n 
1 113 LEU n 
1 114 ALA n 
1 115 CYS n 
1 116 TYR n 
1 117 ASN n 
1 118 GLY n 
1 119 SER n 
1 120 PRO n 
1 121 SER n 
1 122 GLY n 
1 123 VAL n 
1 124 TYR n 
1 125 GLN n 
1 126 CYS n 
1 127 ALA n 
1 128 MET n 
1 129 ARG n 
1 130 PRO n 
1 131 ASN n 
1 132 PHE n 
1 133 THR n 
1 134 ILE n 
1 135 LYS n 
1 136 GLY n 
1 137 SER n 
1 138 PHE n 
1 139 LEU n 
1 140 ASN n 
1 141 GLY n 
1 142 SER n 
1 143 CYS n 
1 144 GLY n 
1 145 SER n 
1 146 VAL n 
1 147 GLY n 
1 148 PHE n 
1 149 ASN n 
1 150 ILE n 
1 151 ASP n 
1 152 TYR n 
1 153 ASP n 
1 154 CYS n 
1 155 VAL n 
1 156 SER n 
1 157 PHE n 
1 158 CYS n 
1 159 TYR n 
1 160 MET n 
1 161 HIS n 
1 162 HIS n 
1 163 MET n 
1 164 GLU n 
1 165 LEU n 
1 166 PRO n 
1 167 THR n 
1 168 GLY n 
1 169 VAL n 
1 170 HIS n 
1 171 ALA n 
1 172 GLY n 
1 173 THR n 
1 174 ASP n 
1 175 LEU n 
1 176 GLU n 
1 177 GLY n 
1 178 ASN n 
1 179 PHE n 
1 180 TYR n 
1 181 GLY n 
1 182 PRO n 
1 183 PHE n 
1 184 VAL n 
1 185 ASP n 
1 186 ARG n 
1 187 GLN n 
1 188 THR n 
1 189 ALA n 
1 190 GLN n 
1 191 ALA n 
1 192 ALA n 
1 193 GLY n 
1 194 THR n 
1 195 ASP n 
1 196 THR n 
1 197 THR n 
1 198 ILE n 
1 199 THR n 
1 200 VAL n 
1 201 ASN n 
1 202 VAL n 
1 203 LEU n 
1 204 ALA n 
1 205 TRP n 
1 206 LEU n 
1 207 TYR n 
1 208 ALA n 
1 209 ALA n 
1 210 VAL n 
1 211 ILE n 
1 212 ASN n 
1 213 GLY n 
1 214 ASP n 
1 215 ARG n 
1 216 TRP n 
1 217 PHE n 
1 218 LEU n 
1 219 ASN n 
1 220 ARG n 
1 221 PHE n 
1 222 THR n 
1 223 THR n 
1 224 THR n 
1 225 LEU n 
1 226 ASN n 
1 227 ASP n 
1 228 PHE n 
1 229 ASN n 
1 230 LEU n 
1 231 VAL n 
1 232 ALA n 
1 233 MET n 
1 234 LYS n 
1 235 TYR n 
1 236 ASN n 
1 237 TYR n 
1 238 GLU n 
1 239 PRO n 
1 240 LEU n 
1 241 THR n 
1 242 GLN n 
1 243 ASP n 
1 244 HIS n 
1 245 VAL n 
1 246 ASP n 
1 247 ILE n 
1 248 LEU n 
1 249 GLY n 
1 250 PRO n 
1 251 LEU n 
1 252 SER n 
1 253 ALA n 
1 254 GLN n 
1 255 THR n 
1 256 GLY n 
1 257 ILE n 
1 258 ALA n 
1 259 VAL n 
1 260 LEU n 
1 261 ASP n 
1 262 MET n 
1 263 CYS n 
1 264 ALA n 
1 265 SER n 
1 266 LEU n 
1 267 LYS n 
1 268 GLU n 
1 269 LEU n 
1 270 LEU n 
1 271 GLN n 
1 272 ASN n 
1 273 GLY n 
1 274 MET n 
1 275 ASN n 
1 276 GLY n 
1 277 ARG n 
1 278 THR n 
1 279 ILE n 
1 280 LEU n 
1 281 GLY n 
1 282 SER n 
1 283 ALA n 
1 284 LEU n 
1 285 LEU n 
1 286 GLU n 
1 287 ASP n 
1 288 GLU n 
1 289 PHE n 
1 290 THR n 
1 291 PRO n 
1 292 PHE n 
1 293 ASP n 
1 294 VAL n 
1 295 VAL n 
1 296 ARG n 
1 297 GLN n 
1 298 CYS n 
1 299 SER n 
1 300 GLY n 
1 301 VAL n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   301 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_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      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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               'BL21(DE3)' 
_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                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
X77 non-polymer         . 
'N-(4-tert-butylphenyl)-N-[(1R)-2-(cyclohexylamino)-2-oxo-1-(pyridin-3-yl)ethyl]-1H-imidazole-4-carboxamide' ? 'C27 H33 N5 O2'  
459.583 
# 
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   PHE 1   3   3   PHE PHE A . n 
A 1 2   ARG 2   4   4   ARG ARG A . n 
A 1 3   LYS 3   5   5   LYS LYS A . n 
A 1 4   MET 4   6   6   MET MET A . n 
A 1 5   ALA 5   7   7   ALA ALA A . n 
A 1 6   PHE 6   8   8   PHE PHE A . n 
A 1 7   PRO 7   9   9   PRO PRO A . n 
A 1 8   SER 8   10  10  SER SER A . n 
A 1 9   GLY 9   11  11  GLY GLY A . n 
A 1 10  LYS 10  12  12  LYS LYS A . n 
A 1 11  VAL 11  13  13  VAL VAL A . n 
A 1 12  GLU 12  14  14  GLU GLU A . n 
A 1 13  GLY 13  15  15  GLY GLY A . n 
A 1 14  CYS 14  16  16  CYS CYS A . n 
A 1 15  MET 15  17  17  MET MET A . n 
A 1 16  VAL 16  18  18  VAL VAL A . n 
A 1 17  GLN 17  19  19  GLN GLN A . n 
A 1 18  VAL 18  20  20  VAL VAL A . n 
A 1 19  THR 19  21  21  THR THR A . n 
A 1 20  CYS 20  22  22  CYS CYS A . n 
A 1 21  GLY 21  23  23  GLY GLY A . n 
A 1 22  THR 22  24  24  THR THR A . n 
A 1 23  THR 23  25  25  THR THR A . n 
A 1 24  THR 24  26  26  THR THR A . n 
A 1 25  LEU 25  27  27  LEU LEU A . n 
A 1 26  ASN 26  28  28  ASN ASN A . n 
A 1 27  GLY 27  29  29  GLY GLY A . n 
A 1 28  LEU 28  30  30  LEU LEU A . n 
A 1 29  TRP 29  31  31  TRP TRP A . n 
A 1 30  LEU 30  32  32  LEU LEU A . n 
A 1 31  ASP 31  33  33  ASP ASP A . n 
A 1 32  ASP 32  34  34  ASP ASP A . n 
A 1 33  VAL 33  35  35  VAL VAL A . n 
A 1 34  VAL 34  36  36  VAL VAL A . n 
A 1 35  TYR 35  37  37  TYR TYR A . n 
A 1 36  CYS 36  38  38  CYS CYS A . n 
A 1 37  PRO 37  39  39  PRO PRO A . n 
A 1 38  ARG 38  40  40  ARG ARG A . n 
A 1 39  HIS 39  41  41  HIS HIS A . n 
A 1 40  VAL 40  42  42  VAL VAL A . n 
A 1 41  ILE 41  43  43  ILE ILE A . n 
A 1 42  CYS 42  44  44  CYS CYS A . n 
A 1 43  THR 43  45  45  THR THR A . n 
A 1 44  SER 44  46  46  SER SER A . n 
A 1 45  GLU 45  47  47  GLU GLU A . n 
A 1 46  ASP 46  48  48  ASP ASP A . n 
A 1 47  MET 47  49  49  MET MET A . n 
A 1 48  LEU 48  50  50  LEU LEU A . n 
A 1 49  ASN 49  51  51  ASN ASN A . n 
A 1 50  PRO 50  52  52  PRO PRO A . n 
A 1 51  ASN 51  53  53  ASN ASN A . n 
A 1 52  TYR 52  54  54  TYR TYR A . n 
A 1 53  GLU 53  55  55  GLU GLU A . n 
A 1 54  ASP 54  56  56  ASP ASP A . n 
A 1 55  LEU 55  57  57  LEU LEU A . n 
A 1 56  LEU 56  58  58  LEU LEU A . n 
A 1 57  ILE 57  59  59  ILE ILE A . n 
A 1 58  ARG 58  60  60  ARG ARG A . n 
A 1 59  LYS 59  61  61  LYS LYS A . n 
A 1 60  SER 60  62  62  SER SER A . n 
A 1 61  ASN 61  63  63  ASN ASN A . n 
A 1 62  HIS 62  64  64  HIS HIS A . n 
A 1 63  ASN 63  65  65  ASN ASN A . n 
A 1 64  PHE 64  66  66  PHE PHE A . n 
A 1 65  LEU 65  67  67  LEU LEU A . n 
A 1 66  VAL 66  68  68  VAL VAL A . n 
A 1 67  GLN 67  69  69  GLN GLN A . n 
A 1 68  ALA 68  70  70  ALA ALA A . n 
A 1 69  GLY 69  71  71  GLY GLY A . n 
A 1 70  ASN 70  72  72  ASN ASN A . n 
A 1 71  VAL 71  73  73  VAL VAL A . n 
A 1 72  GLN 72  74  74  GLN GLN A . n 
A 1 73  LEU 73  75  75  LEU LEU A . n 
A 1 74  ARG 74  76  76  ARG ARG A . n 
A 1 75  VAL 75  77  77  VAL VAL A . n 
A 1 76  ILE 76  78  78  ILE ILE A . n 
A 1 77  GLY 77  79  79  GLY GLY A . n 
A 1 78  HIS 78  80  80  HIS HIS A . n 
A 1 79  SER 79  81  81  SER SER A . n 
A 1 80  MET 80  82  82  MET MET A . n 
A 1 81  GLN 81  83  83  GLN GLN A . n 
A 1 82  ASN 82  84  84  ASN ASN A . n 
A 1 83  CYS 83  85  85  CYS CYS A . n 
A 1 84  VAL 84  86  86  VAL VAL A . n 
A 1 85  LEU 85  87  87  LEU LEU A . n 
A 1 86  LYS 86  88  88  LYS LYS A . n 
A 1 87  LEU 87  89  89  LEU LEU A . n 
A 1 88  LYS 88  90  90  LYS LYS A . n 
A 1 89  VAL 89  91  91  VAL VAL A . n 
A 1 90  ASP 90  92  92  ASP ASP A . n 
A 1 91  THR 91  93  93  THR THR A . n 
A 1 92  ALA 92  94  94  ALA ALA A . n 
A 1 93  ASN 93  95  95  ASN ASN A . n 
A 1 94  PRO 94  96  96  PRO PRO A . n 
A 1 95  LYS 95  97  97  LYS LYS A . n 
A 1 96  THR 96  98  98  THR THR A . n 
A 1 97  PRO 97  99  99  PRO PRO A . n 
A 1 98  LYS 98  100 100 LYS LYS A . n 
A 1 99  TYR 99  101 101 TYR TYR A . n 
A 1 100 LYS 100 102 102 LYS LYS A . n 
A 1 101 PHE 101 103 103 PHE PHE A . n 
A 1 102 VAL 102 104 104 VAL VAL A . n 
A 1 103 ARG 103 105 105 ARG ARG A . n 
A 1 104 ILE 104 106 106 ILE ILE A . n 
A 1 105 GLN 105 107 107 GLN GLN A . n 
A 1 106 PRO 106 108 108 PRO PRO A . n 
A 1 107 GLY 107 109 109 GLY GLY A . n 
A 1 108 GLN 108 110 110 GLN GLN A . n 
A 1 109 THR 109 111 111 THR THR A . n 
A 1 110 PHE 110 112 112 PHE PHE A . n 
A 1 111 SER 111 113 113 SER SER A . n 
A 1 112 VAL 112 114 114 VAL VAL A . n 
A 1 113 LEU 113 115 115 LEU LEU A . n 
A 1 114 ALA 114 116 116 ALA ALA A . n 
A 1 115 CYS 115 117 117 CYS CYS A . n 
A 1 116 TYR 116 118 118 TYR TYR A . n 
A 1 117 ASN 117 119 119 ASN ASN A . n 
A 1 118 GLY 118 120 120 GLY GLY A . n 
A 1 119 SER 119 121 121 SER SER A . n 
A 1 120 PRO 120 122 122 PRO PRO A . n 
A 1 121 SER 121 123 123 SER SER A . n 
A 1 122 GLY 122 124 124 GLY GLY A . n 
A 1 123 VAL 123 125 125 VAL VAL A . n 
A 1 124 TYR 124 126 126 TYR TYR A . n 
A 1 125 GLN 125 127 127 GLN GLN A . n 
A 1 126 CYS 126 128 128 CYS CYS A . n 
A 1 127 ALA 127 129 129 ALA ALA A . n 
A 1 128 MET 128 130 130 MET MET A . n 
A 1 129 ARG 129 131 131 ARG ARG A . n 
A 1 130 PRO 130 132 132 PRO PRO A . n 
A 1 131 ASN 131 133 133 ASN ASN A . n 
A 1 132 PHE 132 134 134 PHE PHE A . n 
A 1 133 THR 133 135 135 THR THR A . n 
A 1 134 ILE 134 136 136 ILE ILE A . n 
A 1 135 LYS 135 137 137 LYS LYS A . n 
A 1 136 GLY 136 138 138 GLY GLY A . n 
A 1 137 SER 137 139 139 SER SER A . n 
A 1 138 PHE 138 140 140 PHE PHE A . n 
A 1 139 LEU 139 141 141 LEU LEU A . n 
A 1 140 ASN 140 142 142 ASN ASN A . n 
A 1 141 GLY 141 143 143 GLY GLY A . n 
A 1 142 SER 142 144 144 SER SER A . n 
A 1 143 CYS 143 145 145 CYS CYS A . n 
A 1 144 GLY 144 146 146 GLY GLY A . n 
A 1 145 SER 145 147 147 SER SER A . n 
A 1 146 VAL 146 148 148 VAL VAL A . n 
A 1 147 GLY 147 149 149 GLY GLY A . n 
A 1 148 PHE 148 150 150 PHE PHE A . n 
A 1 149 ASN 149 151 151 ASN ASN A . n 
A 1 150 ILE 150 152 152 ILE ILE A . n 
A 1 151 ASP 151 153 153 ASP ASP A . n 
A 1 152 TYR 152 154 154 TYR TYR A . n 
A 1 153 ASP 153 155 155 ASP ASP A . n 
A 1 154 CYS 154 156 156 CYS CYS A . n 
A 1 155 VAL 155 157 157 VAL VAL A . n 
A 1 156 SER 156 158 158 SER SER A . n 
A 1 157 PHE 157 159 159 PHE PHE A . n 
A 1 158 CYS 158 160 160 CYS CYS A . n 
A 1 159 TYR 159 161 161 TYR TYR A . n 
A 1 160 MET 160 162 162 MET MET A . n 
A 1 161 HIS 161 163 163 HIS HIS A . n 
A 1 162 HIS 162 164 164 HIS HIS A . n 
A 1 163 MET 163 165 165 MET MET A . n 
A 1 164 GLU 164 166 166 GLU GLU A . n 
A 1 165 LEU 165 167 167 LEU LEU A . n 
A 1 166 PRO 166 168 168 PRO PRO A . n 
A 1 167 THR 167 169 169 THR THR A . n 
A 1 168 GLY 168 170 170 GLY GLY A . n 
A 1 169 VAL 169 171 171 VAL VAL A . n 
A 1 170 HIS 170 172 172 HIS HIS A . n 
A 1 171 ALA 171 173 173 ALA ALA A . n 
A 1 172 GLY 172 174 174 GLY GLY A . n 
A 1 173 THR 173 175 175 THR THR A . n 
A 1 174 ASP 174 176 176 ASP ASP A . n 
A 1 175 LEU 175 177 177 LEU LEU A . n 
A 1 176 GLU 176 178 178 GLU GLU A . n 
A 1 177 GLY 177 179 179 GLY GLY A . n 
A 1 178 ASN 178 180 180 ASN ASN A . n 
A 1 179 PHE 179 181 181 PHE PHE A . n 
A 1 180 TYR 180 182 182 TYR TYR A . n 
A 1 181 GLY 181 183 183 GLY GLY A . n 
A 1 182 PRO 182 184 184 PRO PRO A . n 
A 1 183 PHE 183 185 185 PHE PHE A . n 
A 1 184 VAL 184 186 186 VAL VAL A . n 
A 1 185 ASP 185 187 187 ASP ASP A . n 
A 1 186 ARG 186 188 188 ARG ARG A . n 
A 1 187 GLN 187 189 189 GLN GLN A . n 
A 1 188 THR 188 190 190 THR THR A . n 
A 1 189 ALA 189 191 191 ALA ALA A . n 
A 1 190 GLN 190 192 192 GLN GLN A . n 
A 1 191 ALA 191 193 193 ALA ALA A . n 
A 1 192 ALA 192 194 194 ALA ALA A . n 
A 1 193 GLY 193 195 195 GLY GLY A . n 
A 1 194 THR 194 196 196 THR THR A . n 
A 1 195 ASP 195 197 197 ASP ASP A . n 
A 1 196 THR 196 198 198 THR THR A . n 
A 1 197 THR 197 199 199 THR THR A . n 
A 1 198 ILE 198 200 200 ILE ILE A . n 
A 1 199 THR 199 201 201 THR THR A . n 
A 1 200 VAL 200 202 202 VAL VAL A . n 
A 1 201 ASN 201 203 203 ASN ASN A . n 
A 1 202 VAL 202 204 204 VAL VAL A . n 
A 1 203 LEU 203 205 205 LEU LEU A . n 
A 1 204 ALA 204 206 206 ALA ALA A . n 
A 1 205 TRP 205 207 207 TRP TRP A . n 
A 1 206 LEU 206 208 208 LEU LEU A . n 
A 1 207 TYR 207 209 209 TYR TYR A . n 
A 1 208 ALA 208 210 210 ALA ALA A . n 
A 1 209 ALA 209 211 211 ALA ALA A . n 
A 1 210 VAL 210 212 212 VAL VAL A . n 
A 1 211 ILE 211 213 213 ILE ILE A . n 
A 1 212 ASN 212 214 214 ASN ASN A . n 
A 1 213 GLY 213 215 215 GLY GLY A . n 
A 1 214 ASP 214 216 216 ASP ASP A . n 
A 1 215 ARG 215 217 217 ARG ARG A . n 
A 1 216 TRP 216 218 218 TRP TRP A . n 
A 1 217 PHE 217 219 219 PHE PHE A . n 
A 1 218 LEU 218 220 220 LEU LEU A . n 
A 1 219 ASN 219 221 221 ASN ASN A . n 
A 1 220 ARG 220 222 222 ARG ARG A . n 
A 1 221 PHE 221 223 223 PHE PHE A . n 
A 1 222 THR 222 224 224 THR THR A . n 
A 1 223 THR 223 225 225 THR THR A . n 
A 1 224 THR 224 226 226 THR THR A . n 
A 1 225 LEU 225 227 227 LEU LEU A . n 
A 1 226 ASN 226 228 228 ASN ASN A . n 
A 1 227 ASP 227 229 229 ASP ASP A . n 
A 1 228 PHE 228 230 230 PHE PHE A . n 
A 1 229 ASN 229 231 231 ASN ASN A . n 
A 1 230 LEU 230 232 232 LEU LEU A . n 
A 1 231 VAL 231 233 233 VAL VAL A . n 
A 1 232 ALA 232 234 234 ALA ALA A . n 
A 1 233 MET 233 235 235 MET MET A . n 
A 1 234 LYS 234 236 236 LYS LYS A . n 
A 1 235 TYR 235 237 237 TYR TYR A . n 
A 1 236 ASN 236 238 238 ASN ASN A . n 
A 1 237 TYR 237 239 239 TYR TYR A . n 
A 1 238 GLU 238 240 240 GLU GLU A . n 
A 1 239 PRO 239 241 241 PRO PRO A . n 
A 1 240 LEU 240 242 242 LEU LEU A . n 
A 1 241 THR 241 243 243 THR THR A . n 
A 1 242 GLN 242 244 244 GLN GLN A . n 
A 1 243 ASP 243 245 245 ASP ASP A . n 
A 1 244 HIS 244 246 246 HIS HIS A . n 
A 1 245 VAL 245 247 247 VAL VAL A . n 
A 1 246 ASP 246 248 248 ASP ASP A . n 
A 1 247 ILE 247 249 249 ILE ILE A . n 
A 1 248 LEU 248 250 250 LEU LEU A . n 
A 1 249 GLY 249 251 251 GLY GLY A . n 
A 1 250 PRO 250 252 252 PRO PRO A . n 
A 1 251 LEU 251 253 253 LEU LEU A . n 
A 1 252 SER 252 254 254 SER SER A . n 
A 1 253 ALA 253 255 255 ALA ALA A . n 
A 1 254 GLN 254 256 256 GLN GLN A . n 
A 1 255 THR 255 257 257 THR THR A . n 
A 1 256 GLY 256 258 258 GLY GLY A . n 
A 1 257 ILE 257 259 259 ILE ILE A . n 
A 1 258 ALA 258 260 260 ALA ALA A . n 
A 1 259 VAL 259 261 261 VAL VAL A . n 
A 1 260 LEU 260 262 262 LEU LEU A . n 
A 1 261 ASP 261 263 263 ASP ASP A . n 
A 1 262 MET 262 264 264 MET MET A . n 
A 1 263 CYS 263 265 265 CYS CYS A . n 
A 1 264 ALA 264 266 266 ALA ALA A . n 
A 1 265 SER 265 267 267 SER SER A . n 
A 1 266 LEU 266 268 268 LEU LEU A . n 
A 1 267 LYS 267 269 269 LYS LYS A . n 
A 1 268 GLU 268 270 270 GLU GLU A . n 
A 1 269 LEU 269 271 271 LEU LEU A . n 
A 1 270 LEU 270 272 272 LEU LEU A . n 
A 1 271 GLN 271 273 273 GLN GLN A . n 
A 1 272 ASN 272 274 274 ASN ASN A . n 
A 1 273 GLY 273 275 275 GLY GLY A . n 
A 1 274 MET 274 276 276 MET MET A . n 
A 1 275 ASN 275 277 277 ASN ASN A . n 
A 1 276 GLY 276 278 278 GLY GLY A . n 
A 1 277 ARG 277 279 279 ARG ARG A . n 
A 1 278 THR 278 280 280 THR THR A . n 
A 1 279 ILE 279 281 281 ILE ILE A . n 
A 1 280 LEU 280 282 282 LEU LEU A . n 
A 1 281 GLY 281 283 283 GLY GLY A . n 
A 1 282 SER 282 284 284 SER SER A . n 
A 1 283 ALA 283 285 285 ALA ALA A . n 
A 1 284 LEU 284 286 286 LEU LEU A . n 
A 1 285 LEU 285 287 287 LEU LEU A . n 
A 1 286 GLU 286 288 288 GLU GLU A . n 
A 1 287 ASP 287 289 289 ASP ASP A . n 
A 1 288 GLU 288 290 290 GLU GLU A . n 
A 1 289 PHE 289 291 291 PHE PHE A . n 
A 1 290 THR 290 292 292 THR THR A . n 
A 1 291 PRO 291 293 293 PRO PRO A . n 
A 1 292 PHE 292 294 294 PHE PHE A . n 
A 1 293 ASP 293 295 295 ASP ASP A . n 
A 1 294 VAL 294 296 296 VAL VAL A . n 
A 1 295 VAL 295 297 297 VAL VAL A . n 
A 1 296 ARG 296 298 298 ARG ARG A . n 
A 1 297 GLN 297 299 299 GLN GLN A . n 
A 1 298 CYS 298 300 ?   ?   ?   A . n 
A 1 299 SER 299 301 ?   ?   ?   A . n 
A 1 300 GLY 300 302 ?   ?   ?   A . n 
A 1 301 VAL 301 303 ?   ?   ?   A . n 
B 1 1   PHE 1   3   3   PHE PHE B . n 
B 1 2   ARG 2   4   4   ARG ARG B . n 
B 1 3   LYS 3   5   5   LYS LYS B . n 
B 1 4   MET 4   6   6   MET MET B . n 
B 1 5   ALA 5   7   7   ALA ALA B . n 
B 1 6   PHE 6   8   8   PHE PHE B . n 
B 1 7   PRO 7   9   9   PRO PRO B . n 
B 1 8   SER 8   10  10  SER SER B . n 
B 1 9   GLY 9   11  11  GLY GLY B . n 
B 1 10  LYS 10  12  12  LYS LYS B . n 
B 1 11  VAL 11  13  13  VAL VAL B . n 
B 1 12  GLU 12  14  14  GLU GLU B . n 
B 1 13  GLY 13  15  15  GLY GLY B . n 
B 1 14  CYS 14  16  16  CYS CYS B . n 
B 1 15  MET 15  17  17  MET MET B . n 
B 1 16  VAL 16  18  18  VAL VAL B . n 
B 1 17  GLN 17  19  19  GLN GLN B . n 
B 1 18  VAL 18  20  20  VAL VAL B . n 
B 1 19  THR 19  21  21  THR THR B . n 
B 1 20  CYS 20  22  22  CYS CYS B . n 
B 1 21  GLY 21  23  23  GLY GLY B . n 
B 1 22  THR 22  24  24  THR THR B . n 
B 1 23  THR 23  25  25  THR THR B . n 
B 1 24  THR 24  26  26  THR THR B . n 
B 1 25  LEU 25  27  27  LEU LEU B . n 
B 1 26  ASN 26  28  28  ASN ASN B . n 
B 1 27  GLY 27  29  29  GLY GLY B . n 
B 1 28  LEU 28  30  30  LEU LEU B . n 
B 1 29  TRP 29  31  31  TRP TRP B . n 
B 1 30  LEU 30  32  32  LEU LEU B . n 
B 1 31  ASP 31  33  33  ASP ASP B . n 
B 1 32  ASP 32  34  34  ASP ASP B . n 
B 1 33  VAL 33  35  35  VAL VAL B . n 
B 1 34  VAL 34  36  36  VAL VAL B . n 
B 1 35  TYR 35  37  37  TYR TYR B . n 
B 1 36  CYS 36  38  38  CYS CYS B . n 
B 1 37  PRO 37  39  39  PRO PRO B . n 
B 1 38  ARG 38  40  40  ARG ARG B . n 
B 1 39  HIS 39  41  41  HIS HIS B . n 
B 1 40  VAL 40  42  42  VAL VAL B . n 
B 1 41  ILE 41  43  43  ILE ILE B . n 
B 1 42  CYS 42  44  44  CYS CYS B . n 
B 1 43  THR 43  45  45  THR THR B . n 
B 1 44  SER 44  46  46  SER SER B . n 
B 1 45  GLU 45  47  47  GLU GLU B . n 
B 1 46  ASP 46  48  48  ASP ASP B . n 
B 1 47  MET 47  49  49  MET MET B . n 
B 1 48  LEU 48  50  50  LEU LEU B . n 
B 1 49  ASN 49  51  51  ASN ASN B . n 
B 1 50  PRO 50  52  52  PRO PRO B . n 
B 1 51  ASN 51  53  53  ASN ASN B . n 
B 1 52  TYR 52  54  54  TYR TYR B . n 
B 1 53  GLU 53  55  55  GLU GLU B . n 
B 1 54  ASP 54  56  56  ASP ASP B . n 
B 1 55  LEU 55  57  57  LEU LEU B . n 
B 1 56  LEU 56  58  58  LEU LEU B . n 
B 1 57  ILE 57  59  59  ILE ILE B . n 
B 1 58  ARG 58  60  60  ARG ARG B . n 
B 1 59  LYS 59  61  61  LYS LYS B . n 
B 1 60  SER 60  62  62  SER SER B . n 
B 1 61  ASN 61  63  63  ASN ASN B . n 
B 1 62  HIS 62  64  64  HIS HIS B . n 
B 1 63  ASN 63  65  65  ASN ASN B . n 
B 1 64  PHE 64  66  66  PHE PHE B . n 
B 1 65  LEU 65  67  67  LEU LEU B . n 
B 1 66  VAL 66  68  68  VAL VAL B . n 
B 1 67  GLN 67  69  69  GLN GLN B . n 
B 1 68  ALA 68  70  70  ALA ALA B . n 
B 1 69  GLY 69  71  71  GLY GLY B . n 
B 1 70  ASN 70  72  72  ASN ASN B . n 
B 1 71  VAL 71  73  73  VAL VAL B . n 
B 1 72  GLN 72  74  74  GLN GLN B . n 
B 1 73  LEU 73  75  75  LEU LEU B . n 
B 1 74  ARG 74  76  76  ARG ARG B . n 
B 1 75  VAL 75  77  77  VAL VAL B . n 
B 1 76  ILE 76  78  78  ILE ILE B . n 
B 1 77  GLY 77  79  79  GLY GLY B . n 
B 1 78  HIS 78  80  80  HIS HIS B . n 
B 1 79  SER 79  81  81  SER SER B . n 
B 1 80  MET 80  82  82  MET MET B . n 
B 1 81  GLN 81  83  83  GLN GLN B . n 
B 1 82  ASN 82  84  84  ASN ASN B . n 
B 1 83  CYS 83  85  85  CYS CYS B . n 
B 1 84  VAL 84  86  86  VAL VAL B . n 
B 1 85  LEU 85  87  87  LEU LEU B . n 
B 1 86  LYS 86  88  88  LYS LYS B . n 
B 1 87  LEU 87  89  89  LEU LEU B . n 
B 1 88  LYS 88  90  90  LYS LYS B . n 
B 1 89  VAL 89  91  91  VAL VAL B . n 
B 1 90  ASP 90  92  92  ASP ASP B . n 
B 1 91  THR 91  93  93  THR THR B . n 
B 1 92  ALA 92  94  94  ALA ALA B . n 
B 1 93  ASN 93  95  95  ASN ASN B . n 
B 1 94  PRO 94  96  96  PRO PRO B . n 
B 1 95  LYS 95  97  97  LYS LYS B . n 
B 1 96  THR 96  98  98  THR THR B . n 
B 1 97  PRO 97  99  99  PRO PRO B . n 
B 1 98  LYS 98  100 100 LYS LYS B . n 
B 1 99  TYR 99  101 101 TYR TYR B . n 
B 1 100 LYS 100 102 102 LYS LYS B . n 
B 1 101 PHE 101 103 103 PHE PHE B . n 
B 1 102 VAL 102 104 104 VAL VAL B . n 
B 1 103 ARG 103 105 105 ARG ARG B . n 
B 1 104 ILE 104 106 106 ILE ILE B . n 
B 1 105 GLN 105 107 107 GLN GLN B . n 
B 1 106 PRO 106 108 108 PRO PRO B . n 
B 1 107 GLY 107 109 109 GLY GLY B . n 
B 1 108 GLN 108 110 110 GLN GLN B . n 
B 1 109 THR 109 111 111 THR THR B . n 
B 1 110 PHE 110 112 112 PHE PHE B . n 
B 1 111 SER 111 113 113 SER SER B . n 
B 1 112 VAL 112 114 114 VAL VAL B . n 
B 1 113 LEU 113 115 115 LEU LEU B . n 
B 1 114 ALA 114 116 116 ALA ALA B . n 
B 1 115 CYS 115 117 117 CYS CYS B . n 
B 1 116 TYR 116 118 118 TYR TYR B . n 
B 1 117 ASN 117 119 119 ASN ASN B . n 
B 1 118 GLY 118 120 120 GLY GLY B . n 
B 1 119 SER 119 121 121 SER SER B . n 
B 1 120 PRO 120 122 122 PRO PRO B . n 
B 1 121 SER 121 123 123 SER SER B . n 
B 1 122 GLY 122 124 124 GLY GLY B . n 
B 1 123 VAL 123 125 125 VAL VAL B . n 
B 1 124 TYR 124 126 126 TYR TYR B . n 
B 1 125 GLN 125 127 127 GLN GLN B . n 
B 1 126 CYS 126 128 128 CYS CYS B . n 
B 1 127 ALA 127 129 129 ALA ALA B . n 
B 1 128 MET 128 130 130 MET MET B . n 
B 1 129 ARG 129 131 131 ARG ARG B . n 
B 1 130 PRO 130 132 132 PRO PRO B . n 
B 1 131 ASN 131 133 133 ASN ASN B . n 
B 1 132 PHE 132 134 134 PHE PHE B . n 
B 1 133 THR 133 135 135 THR THR B . n 
B 1 134 ILE 134 136 136 ILE ILE B . n 
B 1 135 LYS 135 137 137 LYS LYS B . n 
B 1 136 GLY 136 138 138 GLY GLY B . n 
B 1 137 SER 137 139 139 SER SER B . n 
B 1 138 PHE 138 140 140 PHE PHE B . n 
B 1 139 LEU 139 141 141 LEU LEU B . n 
B 1 140 ASN 140 142 142 ASN ASN B . n 
B 1 141 GLY 141 143 143 GLY GLY B . n 
B 1 142 SER 142 144 144 SER SER B . n 
B 1 143 CYS 143 145 145 CYS CYS B . n 
B 1 144 GLY 144 146 146 GLY GLY B . n 
B 1 145 SER 145 147 147 SER SER B . n 
B 1 146 VAL 146 148 148 VAL VAL B . n 
B 1 147 GLY 147 149 149 GLY GLY B . n 
B 1 148 PHE 148 150 150 PHE PHE B . n 
B 1 149 ASN 149 151 151 ASN ASN B . n 
B 1 150 ILE 150 152 152 ILE ILE B . n 
B 1 151 ASP 151 153 153 ASP ASP B . n 
B 1 152 TYR 152 154 154 TYR TYR B . n 
B 1 153 ASP 153 155 155 ASP ASP B . n 
B 1 154 CYS 154 156 156 CYS CYS B . n 
B 1 155 VAL 155 157 157 VAL VAL B . n 
B 1 156 SER 156 158 158 SER SER B . n 
B 1 157 PHE 157 159 159 PHE PHE B . n 
B 1 158 CYS 158 160 160 CYS CYS B . n 
B 1 159 TYR 159 161 161 TYR TYR B . n 
B 1 160 MET 160 162 162 MET MET B . n 
B 1 161 HIS 161 163 163 HIS HIS B . n 
B 1 162 HIS 162 164 164 HIS HIS B . n 
B 1 163 MET 163 165 165 MET MET B . n 
B 1 164 GLU 164 166 166 GLU GLU B . n 
B 1 165 LEU 165 167 167 LEU LEU B . n 
B 1 166 PRO 166 168 168 PRO PRO B . n 
B 1 167 THR 167 169 169 THR THR B . n 
B 1 168 GLY 168 170 170 GLY GLY B . n 
B 1 169 VAL 169 171 171 VAL VAL B . n 
B 1 170 HIS 170 172 172 HIS HIS B . n 
B 1 171 ALA 171 173 173 ALA ALA B . n 
B 1 172 GLY 172 174 174 GLY GLY B . n 
B 1 173 THR 173 175 175 THR THR B . n 
B 1 174 ASP 174 176 176 ASP ASP B . n 
B 1 175 LEU 175 177 177 LEU LEU B . n 
B 1 176 GLU 176 178 178 GLU GLU B . n 
B 1 177 GLY 177 179 179 GLY GLY B . n 
B 1 178 ASN 178 180 180 ASN ASN B . n 
B 1 179 PHE 179 181 181 PHE PHE B . n 
B 1 180 TYR 180 182 182 TYR TYR B . n 
B 1 181 GLY 181 183 183 GLY GLY B . n 
B 1 182 PRO 182 184 184 PRO PRO B . n 
B 1 183 PHE 183 185 185 PHE PHE B . n 
B 1 184 VAL 184 186 186 VAL VAL B . n 
B 1 185 ASP 185 187 187 ASP ASP B . n 
B 1 186 ARG 186 188 188 ARG ARG B . n 
B 1 187 GLN 187 189 189 GLN GLN B . n 
B 1 188 THR 188 190 190 THR THR B . n 
B 1 189 ALA 189 191 191 ALA ALA B . n 
B 1 190 GLN 190 192 192 GLN GLN B . n 
B 1 191 ALA 191 193 193 ALA ALA B . n 
B 1 192 ALA 192 194 194 ALA ALA B . n 
B 1 193 GLY 193 195 195 GLY GLY B . n 
B 1 194 THR 194 196 196 THR THR B . n 
B 1 195 ASP 195 197 197 ASP ASP B . n 
B 1 196 THR 196 198 198 THR THR B . n 
B 1 197 THR 197 199 199 THR THR B . n 
B 1 198 ILE 198 200 200 ILE ILE B . n 
B 1 199 THR 199 201 201 THR THR B . n 
B 1 200 VAL 200 202 202 VAL VAL B . n 
B 1 201 ASN 201 203 203 ASN ASN B . n 
B 1 202 VAL 202 204 204 VAL VAL B . n 
B 1 203 LEU 203 205 205 LEU LEU B . n 
B 1 204 ALA 204 206 206 ALA ALA B . n 
B 1 205 TRP 205 207 207 TRP TRP B . n 
B 1 206 LEU 206 208 208 LEU LEU B . n 
B 1 207 TYR 207 209 209 TYR TYR B . n 
B 1 208 ALA 208 210 210 ALA ALA B . n 
B 1 209 ALA 209 211 211 ALA ALA B . n 
B 1 210 VAL 210 212 212 VAL VAL B . n 
B 1 211 ILE 211 213 213 ILE ILE B . n 
B 1 212 ASN 212 214 214 ASN ASN B . n 
B 1 213 GLY 213 215 215 GLY GLY B . n 
B 1 214 ASP 214 216 216 ASP ASP B . n 
B 1 215 ARG 215 217 217 ARG ARG B . n 
B 1 216 TRP 216 218 218 TRP TRP B . n 
B 1 217 PHE 217 219 219 PHE PHE B . n 
B 1 218 LEU 218 220 220 LEU LEU B . n 
B 1 219 ASN 219 221 221 ASN ASN B . n 
B 1 220 ARG 220 222 222 ARG ARG B . n 
B 1 221 PHE 221 223 223 PHE PHE B . n 
B 1 222 THR 222 224 224 THR THR B . n 
B 1 223 THR 223 225 225 THR THR B . n 
B 1 224 THR 224 226 226 THR THR B . n 
B 1 225 LEU 225 227 227 LEU LEU B . n 
B 1 226 ASN 226 228 228 ASN ASN B . n 
B 1 227 ASP 227 229 229 ASP ASP B . n 
B 1 228 PHE 228 230 230 PHE PHE B . n 
B 1 229 ASN 229 231 231 ASN ASN B . n 
B 1 230 LEU 230 232 232 LEU LEU B . n 
B 1 231 VAL 231 233 233 VAL VAL B . n 
B 1 232 ALA 232 234 234 ALA ALA B . n 
B 1 233 MET 233 235 235 MET MET B . n 
B 1 234 LYS 234 236 236 LYS LYS B . n 
B 1 235 TYR 235 237 237 TYR TYR B . n 
B 1 236 ASN 236 238 238 ASN ASN B . n 
B 1 237 TYR 237 239 239 TYR TYR B . n 
B 1 238 GLU 238 240 240 GLU GLU B . n 
B 1 239 PRO 239 241 241 PRO PRO B . n 
B 1 240 LEU 240 242 242 LEU LEU B . n 
B 1 241 THR 241 243 243 THR THR B . n 
B 1 242 GLN 242 244 244 GLN GLN B . n 
B 1 243 ASP 243 245 245 ASP ASP B . n 
B 1 244 HIS 244 246 246 HIS HIS B . n 
B 1 245 VAL 245 247 247 VAL VAL B . n 
B 1 246 ASP 246 248 248 ASP ASP B . n 
B 1 247 ILE 247 249 249 ILE ILE B . n 
B 1 248 LEU 248 250 250 LEU LEU B . n 
B 1 249 GLY 249 251 251 GLY GLY B . n 
B 1 250 PRO 250 252 252 PRO PRO B . n 
B 1 251 LEU 251 253 253 LEU LEU B . n 
B 1 252 SER 252 254 254 SER SER B . n 
B 1 253 ALA 253 255 255 ALA ALA B . n 
B 1 254 GLN 254 256 256 GLN GLN B . n 
B 1 255 THR 255 257 257 THR THR B . n 
B 1 256 GLY 256 258 258 GLY GLY B . n 
B 1 257 ILE 257 259 259 ILE ILE B . n 
B 1 258 ALA 258 260 260 ALA ALA B . n 
B 1 259 VAL 259 261 261 VAL VAL B . n 
B 1 260 LEU 260 262 262 LEU LEU B . n 
B 1 261 ASP 261 263 263 ASP ASP B . n 
B 1 262 MET 262 264 264 MET MET B . n 
B 1 263 CYS 263 265 265 CYS CYS B . n 
B 1 264 ALA 264 266 266 ALA ALA B . n 
B 1 265 SER 265 267 267 SER SER B . n 
B 1 266 LEU 266 268 268 LEU LEU B . n 
B 1 267 LYS 267 269 269 LYS LYS B . n 
B 1 268 GLU 268 270 270 GLU GLU B . n 
B 1 269 LEU 269 271 271 LEU LEU B . n 
B 1 270 LEU 270 272 272 LEU LEU B . n 
B 1 271 GLN 271 273 273 GLN GLN B . n 
B 1 272 ASN 272 274 274 ASN ASN B . n 
B 1 273 GLY 273 275 275 GLY GLY B . n 
B 1 274 MET 274 276 276 MET MET B . n 
B 1 275 ASN 275 277 277 ASN ASN B . n 
B 1 276 GLY 276 278 278 GLY GLY B . n 
B 1 277 ARG 277 279 279 ARG ARG B . n 
B 1 278 THR 278 280 280 THR THR B . n 
B 1 279 ILE 279 281 281 ILE ILE B . n 
B 1 280 LEU 280 282 282 LEU LEU B . n 
B 1 281 GLY 281 283 283 GLY GLY B . n 
B 1 282 SER 282 284 284 SER SER B . n 
B 1 283 ALA 283 285 285 ALA ALA B . n 
B 1 284 LEU 284 286 286 LEU LEU B . n 
B 1 285 LEU 285 287 287 LEU LEU B . n 
B 1 286 GLU 286 288 288 GLU GLU B . n 
B 1 287 ASP 287 289 289 ASP ASP B . n 
B 1 288 GLU 288 290 290 GLU GLU B . n 
B 1 289 PHE 289 291 291 PHE PHE B . n 
B 1 290 THR 290 292 292 THR THR B . n 
B 1 291 PRO 291 293 293 PRO PRO B . n 
B 1 292 PHE 292 294 294 PHE PHE B . n 
B 1 293 ASP 293 295 295 ASP ASP B . n 
B 1 294 VAL 294 296 296 VAL VAL B . n 
B 1 295 VAL 295 297 297 VAL VAL B . n 
B 1 296 ARG 296 298 298 ARG ARG B . n 
B 1 297 GLN 297 299 299 GLN GLN B . n 
B 1 298 CYS 298 300 300 CYS CYS B . n 
B 1 299 SER 299 301 301 SER SER B . n 
B 1 300 GLY 300 302 302 GLY GLY B . n 
B 1 301 VAL 301 303 303 VAL VAL B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        X77 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   X77 
_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 2 X77 1  401 1   X77 LIG A . 
D 2 X77 1  401 2   X77 LIG B . 
E 3 HOH 1  501 20  HOH HOH A . 
E 3 HOH 2  502 8   HOH HOH A . 
E 3 HOH 3  503 99  HOH HOH A . 
E 3 HOH 4  504 85  HOH HOH A . 
E 3 HOH 5  505 13  HOH HOH A . 
E 3 HOH 6  506 101 HOH HOH A . 
E 3 HOH 7  507 16  HOH HOH A . 
E 3 HOH 8  508 69  HOH HOH A . 
E 3 HOH 9  509 66  HOH HOH A . 
E 3 HOH 10 510 31  HOH HOH A . 
E 3 HOH 11 511 45  HOH HOH A . 
E 3 HOH 12 512 33  HOH HOH A . 
E 3 HOH 13 513 17  HOH HOH A . 
E 3 HOH 14 514 2   HOH HOH A . 
E 3 HOH 15 515 28  HOH HOH A . 
E 3 HOH 16 516 100 HOH HOH A . 
E 3 HOH 17 517 88  HOH HOH A . 
E 3 HOH 18 518 29  HOH HOH A . 
E 3 HOH 19 519 32  HOH HOH A . 
E 3 HOH 20 520 78  HOH HOH A . 
E 3 HOH 21 521 24  HOH HOH A . 
E 3 HOH 22 522 30  HOH HOH A . 
E 3 HOH 23 523 89  HOH HOH A . 
E 3 HOH 24 524 65  HOH HOH A . 
E 3 HOH 25 525 25  HOH HOH A . 
E 3 HOH 26 526 7   HOH HOH A . 
E 3 HOH 27 527 64  HOH HOH A . 
E 3 HOH 28 528 42  HOH HOH A . 
E 3 HOH 29 529 37  HOH HOH A . 
E 3 HOH 30 530 18  HOH HOH A . 
E 3 HOH 31 531 97  HOH HOH A . 
E 3 HOH 32 532 51  HOH HOH A . 
E 3 HOH 33 533 92  HOH HOH A . 
E 3 HOH 34 534 62  HOH HOH A . 
E 3 HOH 35 535 71  HOH HOH A . 
E 3 HOH 36 536 38  HOH HOH A . 
E 3 HOH 37 537 41  HOH HOH A . 
E 3 HOH 38 538 84  HOH HOH A . 
E 3 HOH 39 539 90  HOH HOH A . 
E 3 HOH 40 540 82  HOH HOH A . 
E 3 HOH 41 541 36  HOH HOH A . 
E 3 HOH 42 542 81  HOH HOH A . 
E 3 HOH 43 543 40  HOH HOH A . 
E 3 HOH 44 544 23  HOH HOH A . 
E 3 HOH 45 545 63  HOH HOH A . 
E 3 HOH 46 546 4   HOH HOH A . 
E 3 HOH 47 547 102 HOH HOH A . 
E 3 HOH 48 548 76  HOH HOH A . 
E 3 HOH 49 549 98  HOH HOH A . 
E 3 HOH 50 550 39  HOH HOH A . 
E 3 HOH 51 551 44  HOH HOH A . 
E 3 HOH 52 552 79  HOH HOH A . 
E 3 HOH 53 553 46  HOH HOH A . 
E 3 HOH 54 554 96  HOH HOH A . 
E 3 HOH 55 555 104 HOH HOH A . 
E 3 HOH 56 556 80  HOH HOH A . 
E 3 HOH 57 557 67  HOH HOH A . 
E 3 HOH 58 558 74  HOH HOH A . 
E 3 HOH 59 559 35  HOH HOH A . 
E 3 HOH 60 560 105 HOH HOH A . 
E 3 HOH 61 561 106 HOH HOH A . 
E 3 HOH 62 562 14  HOH HOH A . 
E 3 HOH 63 563 107 HOH HOH A . 
E 3 HOH 64 564 22  HOH HOH A . 
E 3 HOH 65 565 86  HOH HOH A . 
F 3 HOH 1  501 93  HOH HOH B . 
F 3 HOH 2  502 26  HOH HOH B . 
F 3 HOH 3  503 59  HOH HOH B . 
F 3 HOH 4  504 21  HOH HOH B . 
F 3 HOH 5  505 49  HOH HOH B . 
F 3 HOH 6  506 15  HOH HOH B . 
F 3 HOH 7  507 91  HOH HOH B . 
F 3 HOH 8  508 58  HOH HOH B . 
F 3 HOH 9  509 57  HOH HOH B . 
F 3 HOH 10 510 27  HOH HOH B . 
F 3 HOH 11 511 70  HOH HOH B . 
F 3 HOH 12 512 54  HOH HOH B . 
F 3 HOH 13 513 52  HOH HOH B . 
F 3 HOH 14 514 3   HOH HOH B . 
F 3 HOH 15 515 1   HOH HOH B . 
F 3 HOH 16 516 5   HOH HOH B . 
F 3 HOH 17 517 12  HOH HOH B . 
F 3 HOH 18 518 10  HOH HOH B . 
F 3 HOH 19 519 53  HOH HOH B . 
F 3 HOH 20 520 103 HOH HOH B . 
F 3 HOH 21 521 95  HOH HOH B . 
F 3 HOH 22 522 77  HOH HOH B . 
F 3 HOH 23 523 61  HOH HOH B . 
F 3 HOH 24 524 68  HOH HOH B . 
F 3 HOH 25 525 87  HOH HOH B . 
F 3 HOH 26 526 60  HOH HOH B . 
F 3 HOH 27 527 34  HOH HOH B . 
F 3 HOH 28 528 94  HOH HOH B . 
F 3 HOH 29 529 72  HOH HOH B . 
F 3 HOH 30 530 75  HOH HOH B . 
F 3 HOH 31 531 9   HOH HOH B . 
F 3 HOH 32 532 11  HOH HOH B . 
F 3 HOH 33 533 50  HOH HOH B . 
F 3 HOH 34 534 48  HOH HOH B . 
F 3 HOH 35 535 73  HOH HOH B . 
F 3 HOH 36 536 43  HOH HOH B . 
F 3 HOH 37 537 83  HOH HOH B . 
F 3 HOH 38 538 56  HOH HOH B . 
F 3 HOH 39 539 19  HOH HOH B . 
F 3 HOH 40 540 47  HOH HOH B . 
F 3 HOH 41 541 6   HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASN 72  ? CG  ? A ASN 70  CG  
2  1 Y 1 A ASN 72  ? OD1 ? A ASN 70  OD1 
3  1 Y 1 A ASN 72  ? ND2 ? A ASN 70  ND2 
4  1 Y 1 A GLN 74  ? CG  ? A GLN 72  CG  
5  1 Y 1 A GLN 74  ? CD  ? A GLN 72  CD  
6  1 Y 1 A GLN 74  ? OE1 ? A GLN 72  OE1 
7  1 Y 1 A GLN 74  ? NE2 ? A GLN 72  NE2 
8  1 Y 1 A ARG 76  ? CG  ? A ARG 74  CG  
9  1 Y 1 A ARG 76  ? CD  ? A ARG 74  CD  
10 1 Y 1 A ARG 76  ? NE  ? A ARG 74  NE  
11 1 Y 1 A ARG 76  ? CZ  ? A ARG 74  CZ  
12 1 Y 1 A ARG 76  ? NH1 ? A ARG 74  NH1 
13 1 Y 1 A ARG 76  ? NH2 ? A ARG 74  NH2 
14 1 Y 1 A LYS 100 ? CG  ? A LYS 98  CG  
15 1 Y 1 A LYS 100 ? CD  ? A LYS 98  CD  
16 1 Y 1 A LYS 100 ? CE  ? A LYS 98  CE  
17 1 Y 1 A LYS 100 ? NZ  ? A LYS 98  NZ  
18 1 Y 1 A LYS 137 ? CG  ? A LYS 135 CG  
19 1 Y 1 A LYS 137 ? CD  ? A LYS 135 CD  
20 1 Y 1 A LYS 137 ? CE  ? A LYS 135 CE  
21 1 Y 1 A LYS 137 ? NZ  ? A LYS 135 NZ  
22 1 Y 1 A TYR 154 ? CG  ? A TYR 152 CG  
23 1 Y 1 A TYR 154 ? CD1 ? A TYR 152 CD1 
24 1 Y 1 A TYR 154 ? CD2 ? A TYR 152 CD2 
25 1 Y 1 A TYR 154 ? CE1 ? A TYR 152 CE1 
26 1 Y 1 A TYR 154 ? CE2 ? A TYR 152 CE2 
27 1 Y 1 A TYR 154 ? CZ  ? A TYR 152 CZ  
28 1 Y 1 A TYR 154 ? OH  ? A TYR 152 OH  
29 1 Y 1 A ARG 298 ? CG  ? A ARG 296 CG  
30 1 Y 1 A ARG 298 ? CD  ? A ARG 296 CD  
31 1 Y 1 A ARG 298 ? NE  ? A ARG 296 NE  
32 1 Y 1 A ARG 298 ? CZ  ? A ARG 296 CZ  
33 1 Y 1 A ARG 298 ? NH1 ? A ARG 296 NH1 
34 1 Y 1 A ARG 298 ? NH2 ? A ARG 296 NH2 
35 1 Y 1 B ASN 72  ? CG  ? B ASN 70  CG  
36 1 Y 1 B ASN 72  ? OD1 ? B ASN 70  OD1 
37 1 Y 1 B ASN 72  ? ND2 ? B ASN 70  ND2 
38 1 Y 1 B GLN 74  ? CG  ? B GLN 72  CG  
39 1 Y 1 B GLN 74  ? CD  ? B GLN 72  CD  
40 1 Y 1 B GLN 74  ? OE1 ? B GLN 72  OE1 
41 1 Y 1 B GLN 74  ? NE2 ? B GLN 72  NE2 
42 1 Y 1 B ARG 76  ? CG  ? B ARG 74  CG  
43 1 Y 1 B ARG 76  ? CD  ? B ARG 74  CD  
44 1 Y 1 B ARG 76  ? NE  ? B ARG 74  NE  
45 1 Y 1 B ARG 76  ? CZ  ? B ARG 74  CZ  
46 1 Y 1 B ARG 76  ? NH1 ? B ARG 74  NH1 
47 1 Y 1 B ARG 76  ? NH2 ? B ARG 74  NH2 
48 1 Y 1 B LYS 100 ? CG  ? B LYS 98  CG  
49 1 Y 1 B LYS 100 ? CD  ? B LYS 98  CD  
50 1 Y 1 B LYS 100 ? CE  ? B LYS 98  CE  
51 1 Y 1 B LYS 100 ? NZ  ? B LYS 98  NZ  
52 1 Y 1 B LYS 137 ? CG  ? B LYS 135 CG  
53 1 Y 1 B LYS 137 ? CD  ? B LYS 135 CD  
54 1 Y 1 B LYS 137 ? CE  ? B LYS 135 CE  
55 1 Y 1 B LYS 137 ? NZ  ? B LYS 135 NZ  
56 1 Y 1 B TYR 154 ? CG  ? B TYR 152 CG  
57 1 Y 1 B TYR 154 ? CD1 ? B TYR 152 CD1 
58 1 Y 1 B TYR 154 ? CD2 ? B TYR 152 CD2 
59 1 Y 1 B TYR 154 ? CE1 ? B TYR 152 CE1 
60 1 Y 1 B TYR 154 ? CE2 ? B TYR 152 CE2 
61 1 Y 1 B TYR 154 ? CZ  ? B TYR 152 CZ  
62 1 Y 1 B TYR 154 ? OH  ? B TYR 152 OH  
63 1 Y 1 B GLN 189 ? CG  ? B GLN 187 CG  
64 1 Y 1 B GLN 189 ? CD  ? B GLN 187 CD  
65 1 Y 1 B GLN 189 ? OE1 ? B GLN 187 OE1 
66 1 Y 1 B GLN 189 ? NE2 ? B GLN 187 NE2 
67 1 Y 1 B ARG 298 ? CG  ? B ARG 296 CG  
68 1 Y 1 B ARG 298 ? CD  ? B ARG 296 CD  
69 1 Y 1 B ARG 298 ? NE  ? B ARG 296 NE  
70 1 Y 1 B ARG 298 ? CZ  ? B ARG 296 CZ  
71 1 Y 1 B ARG 298 ? NH1 ? B ARG 296 NH1 
72 1 Y 1 B ARG 298 ? NH2 ? B ARG 296 NH2 
73 1 Y 1 B GLN 299 ? CG  ? B GLN 297 CG  
74 1 Y 1 B GLN 299 ? CD  ? B GLN 297 CD  
75 1 Y 1 B GLN 299 ? OE1 ? B GLN 297 OE1 
76 1 Y 1 B GLN 299 ? NE2 ? B GLN 297 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.12_2829 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YKJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     104.414 
_cell.length_a_esd                 ? 
_cell.length_b                     67.768 
_cell.length_b_esd                 ? 
_cell.length_c                     101.130 
_cell.length_c_esd                 ? 
_cell.volume                       715588.594 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8YKJ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8YKJ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.70 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.52 
_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              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M HEPES 7.5, 20% PEG 10000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2023-09-13 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          31.7395940104 
_reflns.entry_id                                       8YKJ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.99 
_reflns.d_resolution_low                               41.36 
_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                                     48714 
_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                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.087 
_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                                    1.99 
_reflns_shell.d_res_low                                     2.10 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7085 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.595 
_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                               37.5065554342 
_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                                 8YKJ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.99 
_refine.ls_d_res_low                             41.36 
_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                     48636 
_refine.ls_number_reflns_R_free                  2431 
_refine.ls_number_reflns_R_work                  46205 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.2836740409 
_refine.ls_percent_reflns_R_free                 4.99835512789 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.214129304282 
_refine.ls_R_factor_R_free                       0.252223193374 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.212175778191 
_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                          1.35124783836 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9 
_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                 26.6900815641 
_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                            0.237569882714 
_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                       1.99 
_refine_hist.d_res_low                        41.36 
_refine_hist.number_atoms_solvent             106 
_refine_hist.number_atoms_total               4735 
_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        4561 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         68 
_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' ? 0.00732175050757 ? 4729 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.00361819904    ? 6445 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0542756841793  ? 733  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.00648824183978 ? 833  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 6.5016790558     ? 2745 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.99   2.0298 . . 156 2662 97.0719944885 . . . . 0.290663797491 . . . . . . . . . . . 0.324029699319 
'X-RAY DIFFRACTION' 2.0298 2.074  . . 140 2730 99.1706979959 . . . . 0.278419682916 . . . . . . . . . . . 0.322567678568 
'X-RAY DIFFRACTION' 2.074  2.1222 . . 139 2728 99.0670352453 . . . . 0.264145201191 . . . . . . . . . . . 0.31265381898  
'X-RAY DIFFRACTION' 2.1222 2.1753 . . 128 2760 98.904109589  . . . . 0.249827959081 . . . . . . . . . . . 0.263939489025 
'X-RAY DIFFRACTION' 2.1753 2.2341 . . 139 2714 98.8908145581 . . . . 0.242683038034 . . . . . . . . . . . 0.2973136141   
'X-RAY DIFFRACTION' 2.2341 2.2998 . . 141 2732 98.6946066644 . . . . 0.23566250941  . . . . . . . . . . . 0.284811949007 
'X-RAY DIFFRACTION' 2.2998 2.374  . . 154 2718 98.6941580756 . . . . 0.236784185059 . . . . . . . . . . . 0.283292359385 
'X-RAY DIFFRACTION' 2.374  2.4589 . . 172 2676 98.3765112263 . . . . 0.230584983853 . . . . . . . . . . . 0.282396560109 
'X-RAY DIFFRACTION' 2.4589 2.5573 . . 154 2718 98.0539433254 . . . . 0.227769806319 . . . . . . . . . . . 0.269709035406 
'X-RAY DIFFRACTION' 2.5573 2.6737 . . 147 2712 97.5767918089 . . . . 0.241712031118 . . . . . . . . . . . 0.333890350344 
'X-RAY DIFFRACTION' 2.6737 2.8146 . . 148 2737 97.598105548  . . . . 0.240661082076 . . . . . . . . . . . 0.30380459267  
'X-RAY DIFFRACTION' 2.8146 2.9909 . . 131 2702 97.4879559532 . . . . 0.238950780454 . . . . . . . . . . . 0.273863562446 
'X-RAY DIFFRACTION' 2.9909 3.2218 . . 145 2722 97.0219966159 . . . . 0.232244001438 . . . . . . . . . . . 0.255588630059 
'X-RAY DIFFRACTION' 3.2218 3.5458 . . 137 2720 96.130551817  . . . . 0.219028229827 . . . . . . . . . . . 0.277229734714 
'X-RAY DIFFRACTION' 3.5458 4.0585 . . 128 2714 95.6902356902 . . . . 0.194988474835 . . . . . . . . . . . 0.223789024483 
'X-RAY DIFFRACTION' 4.0585 5.1118 . . 154 2687 94.5109780439 . . . . 0.158358335115 . . . . . . . . . . . 0.19866729717  
'X-RAY DIFFRACTION' 5.1118 41.36  . . 118 2773 91.6323296355 . . . . 0.179567434554 . . . . . . . . . . . 0.190053604651 
# 
_struct.entry_id                     8YKJ 
_struct.title                        'Crystal structure of SARS-Cov-2 main protease in complex with X77' 
_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        8YKJ 
_struct_keywords.text            'VIRAL PROTEIN-INHIBITOR COMPLEX' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN/INHIBITOR' 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1A_SARS2 
_struct_ref.pdbx_db_accession          P0DTC1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;FRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSM
QNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYM
HHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPL
TQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGV
;
_struct_ref.pdbx_align_begin           3266 
# 
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 8YKJ A 1 ? 301 ? P0DTC1 3266 ? 3566 ? 3 303 
2 1 8YKJ B 1 ? 301 ? P0DTC1 3266 ? 3566 ? 3 303 
# 
_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)' 2260  ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  25060 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 8   ? GLY A 13  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 39  ? CYS A 42  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 ASN A 51  ? ARG A 58  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P4  AA4 SER A 60  ? PHE A 64  ? SER A 62  PHE A 66  5 ? 5  
HELX_P HELX_P5  AA5 ILE A 198 ? ASN A 212 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P6  AA6 THR A 224 ? MET A 233 ? THR A 226 MET A 235 1 ? 10 
HELX_P HELX_P7  AA7 LYS A 234 ? ASN A 236 ? LYS A 236 ASN A 238 5 ? 3  
HELX_P HELX_P8  AA8 THR A 241 ? GLY A 256 ? THR A 243 GLY A 258 1 ? 16 
HELX_P HELX_P9  AA9 ALA A 258 ? GLY A 273 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P10 AB1 THR A 290 ? GLN A 297 ? THR A 292 GLN A 299 1 ? 8  
HELX_P HELX_P11 AB2 SER B 8   ? GLY B 13  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P12 AB3 HIS B 39  ? CYS B 42  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P13 AB4 ASN B 51  ? LYS B 59  ? ASN B 53  LYS B 61  1 ? 9  
HELX_P HELX_P14 AB5 SER B 60  ? HIS B 62  ? SER B 62  HIS B 64  5 ? 3  
HELX_P HELX_P15 AB6 ILE B 198 ? ASN B 212 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P16 AB7 THR B 224 ? TYR B 235 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P17 AB8 THR B 241 ? LEU B 248 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P18 AB9 LEU B 248 ? GLY B 256 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P19 AC1 ALA B 258 ? GLY B 273 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P20 AC2 THR B 290 ? GLY B 300 ? THR B 292 GLY B 302 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 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 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 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 VAL A 71  ? LEU A 73  ? VAL A 73  LEU A 75  
AA1 2 LEU A 65  ? ALA A 68  ? LEU A 67  ALA A 70  
AA1 3 MET A 15  ? CYS A 20  ? MET A 17  CYS A 22  
AA1 4 THR A 23  ? LEU A 30  ? THR A 25  LEU A 32  
AA1 5 VAL A 33  ? PRO A 37  ? VAL A 35  PRO A 39  
AA1 6 VAL A 84  ? VAL A 89  ? VAL A 86  VAL A 91  
AA1 7 VAL A 75  ? GLN A 81  ? VAL A 77  GLN A 83  
AA2 1 TYR A 99  ? PHE A 101 ? TYR A 101 PHE A 103 
AA2 2 CYS A 154 ? GLU A 164 ? CYS A 156 GLU A 166 
AA2 3 VAL A 146 ? ASP A 151 ? VAL A 148 ASP A 153 
AA2 4 THR A 109 ? TYR A 116 ? THR A 111 TYR A 118 
AA2 5 SER A 119 ? ALA A 127 ? SER A 121 ALA A 129 
AA3 1 TYR A 99  ? PHE A 101 ? TYR A 101 PHE A 103 
AA3 2 CYS A 154 ? GLU A 164 ? CYS A 156 GLU A 166 
AA3 3 HIS A 170 ? THR A 173 ? HIS A 172 THR A 175 
AA4 1 VAL B 71  ? LEU B 73  ? VAL B 73  LEU B 75  
AA4 2 PHE B 64  ? ALA B 68  ? PHE B 66  ALA B 70  
AA4 3 MET B 15  ? CYS B 20  ? MET B 17  CYS B 22  
AA4 4 THR B 23  ? LEU B 30  ? THR B 25  LEU B 32  
AA4 5 VAL B 33  ? PRO B 37  ? VAL B 35  PRO B 39  
AA4 6 VAL B 84  ? VAL B 89  ? VAL B 86  VAL B 91  
AA4 7 VAL B 75  ? GLN B 81  ? VAL B 77  GLN B 83  
AA5 1 LYS B 98  ? PHE B 101 ? LYS B 100 PHE B 103 
AA5 2 CYS B 154 ? GLU B 164 ? CYS B 156 GLU B 166 
AA5 3 VAL B 146 ? ASP B 151 ? VAL B 148 ASP B 153 
AA5 4 THR B 109 ? TYR B 116 ? THR B 111 TYR B 118 
AA5 5 SER B 119 ? ALA B 127 ? SER B 121 ALA B 129 
AA6 1 LYS B 98  ? PHE B 101 ? LYS B 100 PHE B 103 
AA6 2 CYS B 154 ? GLU B 164 ? CYS B 156 GLU B 166 
AA6 3 HIS B 170 ? THR B 173 ? HIS B 172 THR B 175 
# 
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 O LEU A 73  ? O LEU A 75  N VAL A 66  ? N VAL A 68  
AA1 2 3 O LEU A 65  ? O LEU A 67  N THR A 19  ? N THR A 21  
AA1 3 4 N VAL A 18  ? N VAL A 20  O LEU A 25  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 32  O VAL A 33  ? O VAL A 35  
AA1 5 6 N VAL A 34  ? N VAL A 36  O LEU A 87  ? O LEU A 89  
AA1 6 7 O LYS A 86  ? O LYS A 88  N SER A 79  ? N SER A 81  
AA2 1 2 N LYS A 100 ? N LYS A 102 O PHE A 157 ? O PHE A 159 
AA2 2 3 O SER A 156 ? O SER A 158 N ASN A 149 ? N ASN A 151 
AA2 3 4 O PHE A 148 ? O PHE A 150 N SER A 111 ? N SER A 113 
AA2 4 5 N ALA A 114 ? N ALA A 116 O SER A 121 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 102 O PHE A 157 ? O PHE A 159 
AA3 2 3 N MET A 160 ? N MET A 162 O THR A 173 ? O THR A 175 
AA4 1 2 O LEU B 73  ? O LEU B 75  N VAL B 66  ? N VAL B 68  
AA4 2 3 O GLN B 67  ? O GLN B 69  N GLN B 17  ? N GLN B 19  
AA4 3 4 N VAL B 18  ? N VAL B 20  O LEU B 25  ? O LEU B 27  
AA4 4 5 N LEU B 28  ? N LEU B 30  O TYR B 35  ? O TYR B 37  
AA4 5 6 N VAL B 34  ? N VAL B 36  O LEU B 87  ? O LEU B 89  
AA4 6 7 O LYS B 86  ? O LYS B 88  N SER B 79  ? N SER B 81  
AA5 1 2 N LYS B 98  ? N LYS B 100 O VAL B 155 ? O VAL B 157 
AA5 2 3 O SER B 156 ? O SER B 158 N ASN B 149 ? N ASN B 151 
AA5 3 4 O PHE B 148 ? O PHE B 150 N SER B 111 ? N SER B 113 
AA5 4 5 N PHE B 110 ? N PHE B 112 O CYS B 126 ? O CYS B 128 
AA6 1 2 N LYS B 98  ? N LYS B 100 O VAL B 155 ? O VAL B 157 
AA6 2 3 N MET B 163 ? N MET B 165 O ALA B 171 ? O ALA B 173 
# 
_pdbx_entry_details.entry_id                   8YKJ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 5   ? ? -64.73  92.87   
2  1 ASP A 33  ? ? 52.94   -129.59 
3  1 ASN A 84  ? ? 48.14   -116.31 
4  1 PRO A 184 ? ? -85.00  43.63   
5  1 ARG A 188 ? ? -171.65 144.96  
6  1 ASP B 33  ? ? 51.25   -128.37 
7  1 SER B 46  ? ? -64.20  71.05   
8  1 GLU B 47  ? ? 170.13  -50.34  
9  1 ASN B 84  ? ? 52.25   -121.59 
10 1 TYR B 154 ? ? 35.43   73.21   
11 1 ASP B 155 ? ? 84.69   -5.60   
12 1 ASN B 214 ? ? -86.08  -145.16 
13 1 LEU B 282 ? ? -124.22 -106.30 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 CYS 300 ? A CYS 298 
2 1 Y 1 A SER 301 ? A SER 299 
3 1 Y 1 A GLY 302 ? A GLY 300 
4 1 Y 1 A VAL 303 ? A VAL 301 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
X77 C02  C N N 391 
X77 C04  C N R 392 
X77 C05  C N N 393 
X77 C07  C N N 394 
X77 C08  C N N 395 
X77 C09  C N N 396 
X77 C10  C N N 397 
X77 C11  C N N 398 
X77 C12  C N N 399 
X77 C14  C Y N 400 
X77 C15  C Y N 401 
X77 C16  C Y N 402 
X77 C17  C Y N 403 
X77 C19  C Y N 404 
X77 C20  C Y N 405 
X77 C21  C Y N 406 
X77 C22  C Y N 407 
X77 C23  C Y N 408 
X77 C24  C N N 409 
X77 C25  C N N 410 
X77 C26  C N N 411 
X77 C27  C N N 412 
X77 C28  C Y N 413 
X77 C29  C Y N 414 
X77 C30  C Y N 415 
X77 C31  C Y N 416 
X77 C33  C Y N 417 
X77 N03  N N N 418 
X77 N06  N N N 419 
X77 N18  N Y N 420 
X77 N32  N Y N 421 
X77 N34  N Y N 422 
X77 O01  O N N 423 
X77 O13  O N N 424 
X77 H041 H N N 425 
X77 H071 H N N 426 
X77 H081 H N N 427 
X77 H082 H N N 428 
X77 H091 H N N 429 
X77 H092 H N N 430 
X77 H101 H N N 431 
X77 H102 H N N 432 
X77 H112 H N N 433 
X77 H111 H N N 434 
X77 H121 H N N 435 
X77 H122 H N N 436 
X77 H151 H N N 437 
X77 H161 H N N 438 
X77 H171 H N N 439 
X77 H191 H N N 440 
X77 H211 H N N 441 
X77 H221 H N N 442 
X77 H251 H N N 443 
X77 H252 H N N 444 
X77 H253 H N N 445 
X77 H261 H N N 446 
X77 H263 H N N 447 
X77 H262 H N N 448 
X77 H272 H N N 449 
X77 H273 H N N 450 
X77 H271 H N N 451 
X77 H281 H N N 452 
X77 H291 H N N 453 
X77 H311 H N N 454 
X77 H331 H N N 455 
X77 H061 H N N 456 
X77 H1   H N N 457 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
X77 C33 N32  sing Y N 376 
X77 C33 N34  doub Y N 377 
X77 N32 C31  sing Y N 378 
X77 N34 C30  sing Y N 379 
X77 C31 C30  doub Y N 380 
X77 C30 C02  sing N N 381 
X77 C27 C24  sing N N 382 
X77 C02 O01  doub N N 383 
X77 C02 N03  sing N N 384 
X77 C26 C24  sing N N 385 
X77 C28 C29  doub Y N 386 
X77 C28 C23  sing Y N 387 
X77 C24 C23  sing N N 388 
X77 C24 C25  sing N N 389 
X77 C29 C20  sing Y N 390 
X77 C23 C22  doub Y N 391 
X77 C20 N03  sing N N 392 
X77 C20 C21  doub Y N 393 
X77 C22 C21  sing Y N 394 
X77 N03 C04  sing N N 395 
X77 C19 N18  doub Y N 396 
X77 C19 C14  sing Y N 397 
X77 C04 C14  sing N N 398 
X77 C04 C05  sing N N 399 
X77 N18 C17  sing Y N 400 
X77 C14 C15  doub Y N 401 
X77 O13 C05  doub N N 402 
X77 C17 C16  doub Y N 403 
X77 C05 N06  sing N N 404 
X77 C15 C16  sing Y N 405 
X77 N06 C07  sing N N 406 
X77 C12 C07  sing N N 407 
X77 C12 C11  sing N N 408 
X77 C07 C08  sing N N 409 
X77 C11 C10  sing N N 410 
X77 C08 C09  sing N N 411 
X77 C10 C09  sing N N 412 
X77 C04 H041 sing N N 413 
X77 C07 H071 sing N N 414 
X77 C08 H081 sing N N 415 
X77 C08 H082 sing N N 416 
X77 C09 H091 sing N N 417 
X77 C09 H092 sing N N 418 
X77 C10 H101 sing N N 419 
X77 C10 H102 sing N N 420 
X77 C11 H112 sing N N 421 
X77 C11 H111 sing N N 422 
X77 C12 H121 sing N N 423 
X77 C12 H122 sing N N 424 
X77 C15 H151 sing N N 425 
X77 C16 H161 sing N N 426 
X77 C17 H171 sing N N 427 
X77 C19 H191 sing N N 428 
X77 C21 H211 sing N N 429 
X77 C22 H221 sing N N 430 
X77 C25 H251 sing N N 431 
X77 C25 H252 sing N N 432 
X77 C25 H253 sing N N 433 
X77 C26 H261 sing N N 434 
X77 C26 H263 sing N N 435 
X77 C26 H262 sing N N 436 
X77 C27 H272 sing N N 437 
X77 C27 H273 sing N N 438 
X77 C27 H271 sing N N 439 
X77 C28 H281 sing N N 440 
X77 C29 H291 sing N N 441 
X77 C31 H311 sing N N 442 
X77 C33 H331 sing N N 443 
X77 N06 H061 sing N N 444 
X77 N32 H1   sing N N 445 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_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   8J32 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8YKJ 
_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]   0.009577 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014756 
_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]   0.009888 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 25.62398 1.50364  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 19.97189 1.75589  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 15.80542 1.70748  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 1.23737  29.19336 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . PHE A 1 1   ? -17.17900 -10.41000 -4.41700  1.000 53.71000 ? 3   PHE A N   1 
ATOM   2    C CA  . PHE A 1 1   ? -18.03700 -9.43200  -5.09100  1.000 48.35000 ? 3   PHE A CA  1 
ATOM   3    C C   . PHE A 1 1   ? -18.11400 -8.11900  -4.31200  1.000 52.08000 ? 3   PHE A C   1 
ATOM   4    O O   . PHE A 1 1   ? -18.70100 -8.04100  -3.22800  1.000 52.31000 ? 3   PHE A O   1 
ATOM   5    C CB  . PHE A 1 1   ? -19.44300 -9.99500  -5.29200  1.000 46.41000 ? 3   PHE A CB  1 
ATOM   6    C CG  . PHE A 1 1   ? -20.10300 -9.53600  -6.56300  1.000 44.22000 ? 3   PHE A CG  1 
ATOM   7    C CD1 . PHE A 1 1   ? -19.59400 -9.91600  -7.79500  1.000 45.66000 ? 3   PHE A CD1 1 
ATOM   8    C CD2 . PHE A 1 1   ? -21.23700 -8.72900  -6.52500  1.000 46.36000 ? 3   PHE A CD2 1 
ATOM   9    C CE1 . PHE A 1 1   ? -20.19500 -9.50300  -8.96800  1.000 47.77000 ? 3   PHE A CE1 1 
ATOM   10   C CE2 . PHE A 1 1   ? -21.85400 -8.30600  -7.69800  1.000 39.73000 ? 3   PHE A CE2 1 
ATOM   11   C CZ  . PHE A 1 1   ? -21.32800 -8.69500  -8.92500  1.000 44.14000 ? 3   PHE A CZ  1 
ATOM   12   N N   . ARG A 1 2   ? -17.51300 -7.07700  -4.86100  1.000 46.20000 ? 4   ARG A N   1 
ATOM   13   C CA  . ARG A 1 2   ? -17.45300 -5.80300  -4.17600  1.000 46.84000 ? 4   ARG A CA  1 
ATOM   14   C C   . ARG A 1 2   ? -18.39700 -4.82200  -4.85300  1.000 37.99000 ? 4   ARG A C   1 
ATOM   15   O O   . ARG A 1 2   ? -18.54700 -4.82700  -6.07800  1.000 36.02000 ? 4   ARG A O   1 
ATOM   16   C CB  . ARG A 1 2   ? -16.02800 -5.24500  -4.15500  1.000 43.04000 ? 4   ARG A CB  1 
ATOM   17   C CG  . ARG A 1 2   ? -15.04900 -6.05600  -3.29800  1.000 45.14000 ? 4   ARG A CG  1 
ATOM   18   C CD  . ARG A 1 2   ? -14.76600 -5.37700  -1.94800  1.000 42.97000 ? 4   ARG A CD  1 
ATOM   19   N NE  . ARG A 1 2   ? -13.96500 -6.23000  -1.07300  1.000 44.19000 ? 4   ARG A NE  1 
ATOM   20   C CZ  . ARG A 1 2   ? -13.85500 -6.06400  0.24200   1.000 43.48000 ? 4   ARG A CZ  1 
ATOM   21   N NH1 . ARG A 1 2   ? -14.50600 -5.07600  0.83600   1.000 44.63000 ? 4   ARG A NH1 1 
ATOM   22   N NH2 . ARG A 1 2   ? -13.10600 -6.89800  0.96700   1.000 35.27000 ? 4   ARG A NH2 1 
ATOM   23   N N   . LYS A 1 3   ? -19.07300 -4.03400  -4.03600  1.000 39.75000 ? 5   LYS A N   1 
ATOM   24   C CA  . LYS A 1 3   ? -19.63700 -2.77200  -4.48000  1.000 41.61000 ? 5   LYS A CA  1 
ATOM   25   C C   . LYS A 1 3   ? -18.47900 -1.85500  -4.86200  1.000 38.55000 ? 5   LYS A C   1 
ATOM   26   O O   . LYS A 1 3   ? -17.92500 -1.17900  -3.99000  1.000 43.93000 ? 5   LYS A O   1 
ATOM   27   C CB  . LYS A 1 3   ? -20.46400 -2.15000  -3.35300  1.000 43.21000 ? 5   LYS A CB  1 
ATOM   28   C CG  . LYS A 1 3   ? -21.89400 -1.78800  -3.69800  1.000 46.58000 ? 5   LYS A CG  1 
ATOM   29   C CD  . LYS A 1 3   ? -22.63400 -1.39300  -2.42600  1.000 43.61000 ? 5   LYS A CD  1 
ATOM   30   C CE  . LYS A 1 3   ? -23.77900 -2.34200  -2.15600  1.000 37.24000 ? 5   LYS A CE  1 
ATOM   31   N NZ  . LYS A 1 3   ? -24.63600 -1.86700  -1.04800  1.000 48.02000 ? 5   LYS A NZ  1 
ATOM   32   N N   . MET A 1 4   ? -18.06800 -1.82600  -6.12500  1.000 36.38000 ? 6   MET A N   1 
ATOM   33   C CA  . MET A 1 4   ? -16.94900 -0.96200  -6.45600  1.000 36.47000 ? 6   MET A CA  1 
ATOM   34   C C   . MET A 1 4   ? -17.40900 0.27700   -7.21700  1.000 35.13000 ? 6   MET A C   1 
ATOM   35   O O   . MET A 1 4   ? -18.38900 0.25800   -7.96800  1.000 31.28000 ? 6   MET A O   1 
ATOM   36   C CB  . MET A 1 4   ? -15.84100 -1.70800  -7.21700  1.000 38.17000 ? 6   MET A CB  1 
ATOM   37   C CG  . MET A 1 4   ? -16.12200 -2.16900  -8.61900  1.000 44.27000 ? 6   MET A CG  1 
ATOM   38   S SD  . MET A 1 4   ? -14.62200 -3.03700  -9.18500  1.000 54.43000 ? 6   MET A SD  1 
ATOM   39   C CE  . MET A 1 4   ? -14.61500 -4.43300  -8.08000  1.000 44.94000 ? 6   MET A CE  1 
ATOM   40   N N   . ALA A 1 5   ? -16.70300 1.36800   -6.96800  1.000 31.86000 ? 7   ALA A N   1 
ATOM   41   C CA  . ALA A 1 5   ? -17.00500 2.66000   -7.55200  1.000 30.20000 ? 7   ALA A CA  1 
ATOM   42   C C   . ALA A 1 5   ? -16.12900 2.88300   -8.78000  1.000 32.27000 ? 7   ALA A C   1 
ATOM   43   O O   . ALA A 1 5   ? -15.13300 2.18800   -9.00000  1.000 30.69000 ? 7   ALA A O   1 
ATOM   44   C CB  . ALA A 1 5   ? -16.78000 3.76500   -6.51700  1.000 28.35000 ? 7   ALA A CB  1 
ATOM   45   N N   . PHE A 1 6   ? -16.51300 3.86500   -9.58700  1.000 30.65000 ? 8   PHE A N   1 
ATOM   46   C CA  . PHE A 1 6   ? -15.68400 4.22600   -10.72200 1.000 30.53000 ? 8   PHE A CA  1 
ATOM   47   C C   . PHE A 1 6   ? -14.44900 4.96100   -10.21900 1.000 29.94000 ? 8   PHE A C   1 
ATOM   48   O O   . PHE A 1 6   ? -14.49300 5.60000   -9.16600  1.000 28.72000 ? 8   PHE A O   1 
ATOM   49   C CB  . PHE A 1 6   ? -16.46300 5.09700   -11.70900 1.000 29.03000 ? 8   PHE A CB  1 
ATOM   50   C CG  . PHE A 1 6   ? -17.45100 4.31100   -12.52800 1.000 31.33000 ? 8   PHE A CG  1 
ATOM   51   C CD1 . PHE A 1 6   ? -17.02800 3.57600   -13.61900 1.000 34.71000 ? 8   PHE A CD1 1 
ATOM   52   C CD2 . PHE A 1 6   ? -18.78600 4.26700   -12.17100 1.000 31.01000 ? 8   PHE A CD2 1 
ATOM   53   C CE1 . PHE A 1 6   ? -17.92900 2.81900   -14.36300 1.000 39.47000 ? 8   PHE A CE1 1 
ATOM   54   C CE2 . PHE A 1 6   ? -19.69900 3.50800   -12.90900 1.000 33.47000 ? 8   PHE A CE2 1 
ATOM   55   C CZ  . PHE A 1 6   ? -19.26400 2.79100   -14.00500 1.000 36.21000 ? 8   PHE A CZ  1 
ATOM   56   N N   . PRO A 1 7   ? -13.32500 4.84500   -10.92300 1.000 27.29000 ? 9   PRO A N   1 
ATOM   57   C CA  . PRO A 1 7   ? -12.15400 5.65800   -10.56700 1.000 27.78000 ? 9   PRO A CA  1 
ATOM   58   C C   . PRO A 1 7   ? -12.53800 7.13400   -10.59100 1.000 29.08000 ? 9   PRO A C   1 
ATOM   59   O O   . PRO A 1 7   ? -13.22100 7.59400   -11.50600 1.000 29.41000 ? 9   PRO A O   1 
ATOM   60   C CB  . PRO A 1 7   ? -11.13600 5.31200   -11.65900 1.000 27.64000 ? 9   PRO A CB  1 
ATOM   61   C CG  . PRO A 1 7   ? -11.64900 4.03900   -12.29700 1.000 31.58000 ? 9   PRO A CG  1 
ATOM   62   C CD  . PRO A 1 7   ? -13.14000 4.13300   -12.19500 1.000 31.07000 ? 9   PRO A CD  1 
ATOM   63   N N   . SER A 1 8   ? -12.12500 7.86400   -9.56200  1.000 25.64000 ? 10  SER A N   1 
ATOM   64   C CA  . SER A 1 8   ? -12.68100 9.18000   -9.29000  1.000 28.66000 ? 10  SER A CA  1 
ATOM   65   C C   . SER A 1 8   ? -11.86800 10.31900  -9.89900  1.000 27.60000 ? 10  SER A C   1 
ATOM   66   O O   . SER A 1 8   ? -12.29300 11.47200  -9.80400  1.000 28.92000 ? 10  SER A O   1 
ATOM   67   C CB  . SER A 1 8   ? -12.81400 9.37900   -7.77800  1.000 27.98000 ? 10  SER A CB  1 
ATOM   68   O OG  . SER A 1 8   ? -11.53700 9.43800   -7.16000  1.000 30.30000 ? 10  SER A OG  1 
ATOM   69   N N   . GLY A 1 9   ? -10.76300 10.00800  -10.58100 1.000 27.54000 ? 11  GLY A N   1 
ATOM   70   C CA  . GLY A 1 9   ? -9.81200  11.03300  -10.98800 1.000 27.48000 ? 11  GLY A CA  1 
ATOM   71   C C   . GLY A 1 9   ? -10.40300 12.09100  -11.89900 1.000 28.47000 ? 11  GLY A C   1 
ATOM   72   O O   . GLY A 1 9   ? -10.15000 13.28100  -11.71800 1.000 27.63000 ? 11  GLY A O   1 
ATOM   73   N N   . LYS A 1 10  ? -11.18200 11.66900  -12.89700 1.000 29.73000 ? 12  LYS A N   1 
ATOM   74   C CA  . LYS A 1 10  ? -11.79200 12.62500  -13.82000 1.000 30.90000 ? 12  LYS A CA  1 
ATOM   75   C C   . LYS A 1 10  ? -12.72900 13.58900  -13.10600 1.000 31.08000 ? 12  LYS A C   1 
ATOM   76   O O   . LYS A 1 10  ? -12.89100 14.74100  -13.54000 1.000 33.20000 ? 12  LYS A O   1 
ATOM   77   C CB  . LYS A 1 10  ? -12.54400 11.87800  -14.91900 1.000 30.84000 ? 12  LYS A CB  1 
ATOM   78   C CG  . LYS A 1 10  ? -11.63500 11.17800  -15.92700 1.000 34.39000 ? 12  LYS A CG  1 
ATOM   79   C CD  . LYS A 1 10  ? -12.45900 10.42000  -16.95600 1.000 37.00000 ? 12  LYS A CD  1 
ATOM   80   C CE  . LYS A 1 10  ? -11.57500 9.70200   -17.97400 1.000 43.97000 ? 12  LYS A CE  1 
ATOM   81   N NZ  . LYS A 1 10  ? -10.45100 8.97000   -17.32300 1.000 45.63000 ? 12  LYS A NZ  1 
ATOM   82   N N   . VAL A 1 11  ? -13.34500 13.15200  -12.00900 1.000 25.46000 ? 13  VAL A N   1 
ATOM   83   C CA  . VAL A 1 11  ? -14.24000 14.04700  -11.28800 1.000 28.15000 ? 13  VAL A CA  1 
ATOM   84   C C   . VAL A 1 11  ? -13.44300 14.89400  -10.30500 1.000 29.44000 ? 13  VAL A C   1 
ATOM   85   O O   . VAL A 1 11  ? -13.76600 16.07300  -10.09000 1.000 28.10000 ? 13  VAL A O   1 
ATOM   86   C CB  . VAL A 1 11  ? -15.37000 13.25000  -10.60100 1.000 23.58000 ? 13  VAL A CB  1 
ATOM   87   C CG1 . VAL A 1 11  ? -16.33300 14.17900  -9.82400  1.000 25.74000 ? 13  VAL A CG1 1 
ATOM   88   C CG2 . VAL A 1 11  ? -16.15500 12.43800  -11.62700 1.000 26.58000 ? 13  VAL A CG2 1 
ATOM   89   N N   . GLU A 1 12  ? -12.36500 14.33800  -9.74200  1.000 29.27000 ? 14  GLU A N   1 
ATOM   90   C CA  . GLU A 1 12  ? -11.54500 15.09000  -8.79100  1.000 25.81000 ? 14  GLU A CA  1 
ATOM   91   C C   . GLU A 1 12  ? -11.05900 16.40500  -9.37300  1.000 26.89000 ? 14  GLU A C   1 
ATOM   92   O O   . GLU A 1 12  ? -11.05400 17.42700  -8.68100  1.000 25.41000 ? 14  GLU A O   1 
ATOM   93   C CB  . GLU A 1 12  ? -10.33300 14.26700  -8.35100  1.000 28.10000 ? 14  GLU A CB  1 
ATOM   94   C CG  . GLU A 1 12  ? -10.66300 13.15000  -7.41500  1.000 26.13000 ? 14  GLU A CG  1 
ATOM   95   C CD  . GLU A 1 12  ? -9.48400  12.19700  -7.23200  1.000 28.17000 ? 14  GLU A CD  1 
ATOM   96   O OE1 . GLU A 1 12  ? -9.68300  10.96700  -7.33600  1.000 28.42000 ? 14  GLU A OE1 1 
ATOM   97   O OE2 . GLU A 1 12  ? -8.38700  12.69000  -6.94900  1.000 30.72000 ? 14  GLU A OE2 1 
ATOM   98   N N   . GLY A 1 13  ? -10.60700 16.38600  -10.62500 1.000 25.88000 ? 15  GLY A N   1 
ATOM   99   C CA  . GLY A 1 13  ? -10.07500 17.56500  -11.26100 1.000 31.63000 ? 15  GLY A CA  1 
ATOM   100  C C   . GLY A 1 13  ? -11.10900 18.61800  -11.59400 1.000 30.15000 ? 15  GLY A C   1 
ATOM   101  O O   . GLY A 1 13  ? -10.76000 19.63000  -12.20500 1.000 30.06000 ? 15  GLY A O   1 
ATOM   102  N N   . CYS A 1 14  ? -12.37400 18.38900  -11.22900 1.000 29.49000 ? 16  CYS A N   1 
ATOM   103  C CA  . CYS A 1 14  ? -13.44900 19.34000  -11.45600 1.000 28.54000 ? 16  CYS A CA  1 
ATOM   104  C C   . CYS A 1 14  ? -14.00000 19.95200  -10.18200 1.000 30.75000 ? 16  CYS A C   1 
ATOM   105  O O   . CYS A 1 14  ? -14.81400 20.88500  -10.26900 1.000 30.88000 ? 16  CYS A O   1 
ATOM   106  C CB  . CYS A 1 14  ? -14.60800 18.67300  -12.19800 1.000 29.12000 ? 16  CYS A CB  1 
ATOM   107  S SG  . CYS A 1 14  ? -14.18500 17.95600  -13.76000 1.000 32.43000 ? 16  CYS A SG  1 
ATOM   108  N N   . MET A 1 15  ? -13.60000 19.46400  -9.01100  1.000 27.13000 ? 17  MET A N   1 
ATOM   109  C CA  . MET A 1 15  ? -14.21300 19.93800  -7.78000  1.000 26.82000 ? 17  MET A CA  1 
ATOM   110  C C   . MET A 1 15  ? -13.60100 21.26600  -7.34800  1.000 29.76000 ? 17  MET A C   1 
ATOM   111  O O   . MET A 1 15  ? -12.37800 21.43600  -7.35700  1.000 29.77000 ? 17  MET A O   1 
ATOM   112  C CB  . MET A 1 15  ? -14.07600 18.90100  -6.67100  1.000 30.03000 ? 17  MET A CB  1 
ATOM   113  C CG  . MET A 1 15  ? -14.76100 17.56900  -7.00400  1.000 27.63000 ? 17  MET A CG  1 
ATOM   114  S SD  . MET A 1 15  ? -16.44400 17.79200  -7.58300  1.000 30.86000 ? 17  MET A SD  1 
ATOM   115  C CE  . MET A 1 15  ? -17.19200 18.60800  -6.17400  1.000 26.16000 ? 17  MET A CE  1 
ATOM   116  N N   . VAL A 1 16  ? -14.45700 22.21400  -6.98300  1.000 29.33000 ? 18  VAL A N   1 
ATOM   117  C CA  . VAL A 1 16  ? -14.01600 23.50900  -6.48800  1.000 27.54000 ? 18  VAL A CA  1 
ATOM   118  C C   . VAL A 1 16  ? -14.82600 23.85400  -5.24900  1.000 32.35000 ? 18  VAL A C   1 
ATOM   119  O O   . VAL A 1 16  ? -15.85300 23.23300  -4.93800  1.000 27.26000 ? 18  VAL A O   1 
ATOM   120  C CB  . VAL A 1 16  ? -14.14700 24.63200  -7.53700  1.000 28.75000 ? 18  VAL A CB  1 
ATOM   121  C CG1 . VAL A 1 16  ? -13.20000 24.39900  -8.69500  1.000 29.84000 ? 18  VAL A CG1 1 
ATOM   122  C CG2 . VAL A 1 16  ? -15.59800 24.76200  -8.03400  1.000 27.11000 ? 18  VAL A CG2 1 
ATOM   123  N N   . GLN A 1 17  ? -14.33100 24.85900  -4.54000  1.000 27.56000 ? 19  GLN A N   1 
ATOM   124  C CA  . GLN A 1 17  ? -14.99900 25.44200  -3.38800  1.000 33.12000 ? 19  GLN A CA  1 
ATOM   125  C C   . GLN A 1 17  ? -15.77000 26.69100  -3.81300  1.000 31.45000 ? 19  GLN A C   1 
ATOM   126  O O   . GLN A 1 17  ? -15.26300 27.50500  -4.58800  1.000 31.15000 ? 19  GLN A O   1 
ATOM   127  C CB  . GLN A 1 17  ? -13.95200 25.79200  -2.33400  1.000 34.28000 ? 19  GLN A CB  1 
ATOM   128  C CG  . GLN A 1 17  ? -14.48500 26.18300  -0.99700  1.000 37.29000 ? 19  GLN A CG  1 
ATOM   129  C CD  . GLN A 1 17  ? -13.36000 26.34500  0.00500   1.000 40.85000 ? 19  GLN A CD  1 
ATOM   130  O OE1 . GLN A 1 17  ? -13.56500 26.23900  1.21000   1.000 46.09000 ? 19  GLN A OE1 1 
ATOM   131  N NE2 . GLN A 1 17  ? -12.15500 26.59200  -0.49700  1.000 43.57000 ? 19  GLN A NE2 1 
ATOM   132  N N   . VAL A 1 18  ? -17.00000 26.83900  -3.32900  1.000 31.30000 ? 20  VAL A N   1 
ATOM   133  C CA  . VAL A 1 18  ? -17.79500 28.03800  -3.58900  1.000 29.98000 ? 20  VAL A CA  1 
ATOM   134  C C   . VAL A 1 18  ? -18.19900 28.64500  -2.25900  1.000 31.28000 ? 20  VAL A C   1 
ATOM   135  O O   . VAL A 1 18  ? -18.73900 27.94900  -1.39200  1.000 29.66000 ? 20  VAL A O   1 
ATOM   136  C CB  . VAL A 1 18  ? -19.04700 27.75600  -4.43900  1.000 31.81000 ? 20  VAL A CB  1 
ATOM   137  C CG1 . VAL A 1 18  ? -19.82500 29.07600  -4.68600  1.000 30.05000 ? 20  VAL A CG1 1 
ATOM   138  C CG2 . VAL A 1 18  ? -18.68000 27.07700  -5.73900  1.000 26.39000 ? 20  VAL A CG2 1 
ATOM   139  N N   . THR A 1 19  ? -17.97600 29.94800  -2.11800  1.000 31.66000 ? 21  THR A N   1 
ATOM   140  C CA  . THR A 1 19  ? -18.31900 30.68000  -0.90800  1.000 34.48000 ? 21  THR A CA  1 
ATOM   141  C C   . THR A 1 19  ? -19.20400 31.86500  -1.25900  1.000 34.31000 ? 21  THR A C   1 
ATOM   142  O O   . THR A 1 19  ? -18.89100 32.62300  -2.18100  1.000 34.90000 ? 21  THR A O   1 
ATOM   143  C CB  . THR A 1 19  ? -17.07000 31.18400  -0.18900  1.000 37.06000 ? 21  THR A CB  1 
ATOM   144  O OG1 . THR A 1 19  ? -16.22600 30.07400  0.12600   1.000 39.91000 ? 21  THR A OG1 1 
ATOM   145  C CG2 . THR A 1 19  ? -17.46800 31.92300  1.10000   1.000 36.29000 ? 21  THR A CG2 1 
ATOM   146  N N   . CYS A 1 20  ? -20.30500 32.01500  -0.52500  1.000 34.74000 ? 22  CYS A N   1 
ATOM   147  C CA  . CYS A 1 20  ? -21.17400 33.18200  -0.63800  1.000 36.30000 ? 22  CYS A CA  1 
ATOM   148  C C   . CYS A 1 20  ? -21.59800 33.55700  0.77100   1.000 39.12000 ? 22  CYS A C   1 
ATOM   149  O O   . CYS A 1 20  ? -22.17400 32.73000  1.48800   1.000 37.18000 ? 22  CYS A O   1 
ATOM   150  C CB  . CYS A 1 20  ? -22.39000 32.89600  -1.52400  1.000 32.44000 ? 22  CYS A CB  1 
ATOM   151  S SG  . CYS A 1 20  ? -23.45800 34.34300  -1.85500  1.000 42.68000 ? 22  CYS A SG  1 
ATOM   152  N N   . GLY A 1 21  ? -21.28100 34.77800  1.18500   1.000 44.46000 ? 23  GLY A N   1 
ATOM   153  C CA  . GLY A 1 21  ? -21.59900 35.16500  2.55200   1.000 40.90000 ? 23  GLY A CA  1 
ATOM   154  C C   . GLY A 1 21  ? -20.77300 34.33700  3.51300   1.000 38.84000 ? 23  GLY A C   1 
ATOM   155  O O   . GLY A 1 21  ? -19.55300 34.22900  3.37500   1.000 40.94000 ? 23  GLY A O   1 
ATOM   156  N N   . THR A 1 22  ? -21.43600 33.71600  4.48300   1.000 34.95000 ? 24  THR A N   1 
ATOM   157  C CA  . THR A 1 22  ? -20.76200 32.85900  5.44800   1.000 40.67000 ? 24  THR A CA  1 
ATOM   158  C C   . THR A 1 22  ? -20.83100 31.38400  5.07200   1.000 37.39000 ? 24  THR A C   1 
ATOM   159  O O   . THR A 1 22  ? -20.41600 30.53000  5.86100   1.000 37.04000 ? 24  THR A O   1 
ATOM   160  C CB  . THR A 1 22  ? -21.36700 33.05900  6.82800   1.000 40.05000 ? 24  THR A CB  1 
ATOM   161  O OG1 . THR A 1 22  ? -22.78300 32.88600  6.73500   1.000 47.18000 ? 24  THR A OG1 1 
ATOM   162  C CG2 . THR A 1 22  ? -21.05800 34.46200  7.32900   1.000 39.13000 ? 24  THR A CG2 1 
ATOM   163  N N   . THR A 1 23  ? -21.35600 31.07100  3.89300   1.000 36.66000 ? 25  THR A N   1 
ATOM   164  C CA  . THR A 1 23  ? -21.67900 29.70500  3.50600   1.000 35.27000 ? 25  THR A CA  1 
ATOM   165  C C   . THR A 1 23  ? -20.68200 29.22500  2.47000   1.000 32.09000 ? 25  THR A C   1 
ATOM   166  O O   . THR A 1 23  ? -20.47300 29.89300  1.45300   1.000 31.98000 ? 25  THR A O   1 
ATOM   167  C CB  . THR A 1 23  ? -23.10100 29.61200  2.94100   1.000 30.93000 ? 25  THR A CB  1 
ATOM   168  O OG1 . THR A 1 23  ? -24.04100 29.87400  3.98300   1.000 35.57000 ? 25  THR A OG1 1 
ATOM   169  C CG2 . THR A 1 23  ? -23.36100 28.22300  2.38200   1.000 34.54000 ? 25  THR A CG2 1 
ATOM   170  N N   . THR A 1 24  ? -20.09200 28.06200  2.72300   1.000 33.54000 ? 26  THR A N   1 
ATOM   171  C CA  . THR A 1 24  ? -19.17700 27.41200  1.79700   1.000 33.37000 ? 26  THR A CA  1 
ATOM   172  C C   . THR A 1 24  ? -19.70200 26.01400  1.47200   1.000 28.89000 ? 26  THR A C   1 
ATOM   173  O O   . THR A 1 24  ? -20.23200 25.33000  2.34000   1.000 27.96000 ? 26  THR A O   1 
ATOM   174  C CB  . THR A 1 24  ? -17.75800 27.34300  2.39800   1.000 34.93000 ? 26  THR A CB  1 
ATOM   175  O OG1 . THR A 1 24  ? -17.21200 28.67100  2.51000   1.000 36.36000 ? 26  THR A OG1 1 
ATOM   176  C CG2 . THR A 1 24  ? -16.83400 26.51500  1.53900   1.000 35.55000 ? 26  THR A CG2 1 
ATOM   177  N N   . LEU A 1 25  ? -19.58800 25.61900  0.21000   1.000 29.47000 ? 27  LEU A N   1 
ATOM   178  C CA  . LEU A 1 25  ? -19.90700 24.27700  -0.25900  1.000 28.12000 ? 27  LEU A CA  1 
ATOM   179  C C   . LEU A 1 25  ? -19.05200 24.00900  -1.49300  1.000 28.71000 ? 27  LEU A C   1 
ATOM   180  O O   . LEU A 1 25  ? -18.15900 24.79900  -1.83600  1.000 29.02000 ? 27  LEU A O   1 
ATOM   181  C CB  . LEU A 1 25  ? -21.41900 24.12200  -0.51200  1.000 29.31000 ? 27  LEU A CB  1 
ATOM   182  C CG  . LEU A 1 25  ? -22.22800 25.26900  -1.13800  1.000 28.59000 ? 27  LEU A CG  1 
ATOM   183  C CD1 . LEU A 1 25  ? -21.77300 25.63000  -2.53200  1.000 27.94000 ? 27  LEU A CD1 1 
ATOM   184  C CD2 . LEU A 1 25  ? -23.69100 24.85600  -1.15800  1.000 25.51000 ? 27  LEU A CD2 1 
ATOM   185  N N   . ASN A 1 26  ? -19.35500 22.91700  -2.18100  1.000 24.08000 ? 28  ASN A N   1 
ATOM   186  C CA  . ASN A 1 26  ? -18.60200 22.45600  -3.33500  1.000 24.88000 ? 28  ASN A CA  1 
ATOM   187  C C   . ASN A 1 26  ? -19.28900 22.84300  -4.63400  1.000 23.44000 ? 28  ASN A C   1 
ATOM   188  O O   . ASN A 1 26  ? -20.51200 22.91700  -4.71700  1.000 24.36000 ? 28  ASN A O   1 
ATOM   189  C CB  . ASN A 1 26  ? -18.43800 20.92200  -3.32200  1.000 24.81000 ? 28  ASN A CB  1 
ATOM   190  C CG  . ASN A 1 26  ? -17.89000 20.39900  -2.02000  1.000 25.76000 ? 28  ASN A CG  1 
ATOM   191  O OD1 . ASN A 1 26  ? -16.69700 20.51800  -1.75100  1.000 26.80000 ? 28  ASN A OD1 1 
ATOM   192  N ND2 . ASN A 1 26  ? -18.75600 19.80800  -1.19800  1.000 24.68000 ? 28  ASN A ND2 1 
ATOM   193  N N   . GLY A 1 27  ? -18.48500 23.02700  -5.67500  1.000 27.75000 ? 29  GLY A N   1 
ATOM   194  C CA  . GLY A 1 27  ? -19.00800 23.20900  -7.00500  1.000 25.23000 ? 29  GLY A CA  1 
ATOM   195  C C   . GLY A 1 27  ? -18.29200 22.29100  -7.97400  1.000 28.70000 ? 29  GLY A C   1 
ATOM   196  O O   . GLY A 1 27  ? -17.22800 21.74100  -7.68200  1.000 28.09000 ? 29  GLY A O   1 
ATOM   197  N N   . LEU A 1 28  ? -18.90400 22.13700  -9.14200  1.000 28.39000 ? 30  LEU A N   1 
ATOM   198  C CA  . LEU A 1 28  ? -18.38500 21.29400  -10.20700 1.000 30.06000 ? 30  LEU A CA  1 
ATOM   199  C C   . LEU A 1 28  ? -17.96700 22.20200  -11.35700 1.000 31.37000 ? 30  LEU A C   1 
ATOM   200  O O   . LEU A 1 28  ? -18.81000 22.89700  -11.93500 1.000 28.80000 ? 30  LEU A O   1 
ATOM   201  C CB  . LEU A 1 28  ? -19.44100 20.28000  -10.65500 1.000 27.57000 ? 30  LEU A CB  1 
ATOM   202  C CG  . LEU A 1 28  ? -19.00200 19.30400  -11.73300 1.000 27.06000 ? 30  LEU A CG  1 
ATOM   203  C CD1 . LEU A 1 28  ? -18.01300 18.26800  -11.16900 1.000 25.25000 ? 30  LEU A CD1 1 
ATOM   204  C CD2 . LEU A 1 28  ? -20.21700 18.61800  -12.33600 1.000 28.32000 ? 30  LEU A CD2 1 
ATOM   205  N N   . TRP A 1 29  ? -16.66700 22.20400  -11.67000 1.000 33.39000 ? 31  TRP A N   1 
ATOM   206  C CA  . TRP A 1 29  ? -16.06100 23.13100  -12.63200 1.000 32.20000 ? 31  TRP A CA  1 
ATOM   207  C C   . TRP A 1 29  ? -15.85900 22.40100  -13.95600 1.000 31.25000 ? 31  TRP A C   1 
ATOM   208  O O   . TRP A 1 29  ? -14.95000 21.57400  -14.09500 1.000 31.75000 ? 31  TRP A O   1 
ATOM   209  C CB  . TRP A 1 29  ? -14.74200 23.66400  -12.07800 1.000 30.12000 ? 31  TRP A CB  1 
ATOM   210  C CG  . TRP A 1 29  ? -14.00500 24.63900  -12.95600 1.000 30.80000 ? 31  TRP A CG  1 
ATOM   211  C CD1 . TRP A 1 29  ? -14.52500 25.42000  -13.96200 1.000 33.31000 ? 31  TRP A CD1 1 
ATOM   212  C CD2 . TRP A 1 29  ? -12.61100 24.95400  -12.88700 1.000 33.28000 ? 31  TRP A CD2 1 
ATOM   213  N NE1 . TRP A 1 29  ? -13.53100 26.19600  -14.52000 1.000 34.00000 ? 31  TRP A NE1 1 
ATOM   214  C CE2 . TRP A 1 29  ? -12.34800 25.93000  -13.87600 1.000 37.87000 ? 31  TRP A CE2 1 
ATOM   215  C CE3 . TRP A 1 29  ? -11.55800 24.51100  -12.08000 1.000 31.88000 ? 31  TRP A CE3 1 
ATOM   216  C CZ2 . TRP A 1 29  ? -11.07200 26.46100  -14.07700 1.000 36.97000 ? 31  TRP A CZ2 1 
ATOM   217  C CZ3 . TRP A 1 29  ? -10.30100 25.03000  -12.28400 1.000 33.20000 ? 31  TRP A CZ3 1 
ATOM   218  C CH2 . TRP A 1 29  ? -10.06400 25.99200  -13.27500 1.000 34.95000 ? 31  TRP A CH2 1 
ATOM   219  N N   . LEU A 1 30  ? -16.71700 22.69700  -14.92600 1.000 27.71000 ? 32  LEU A N   1 
ATOM   220  C CA  . LEU A 1 30  ? -16.64200 22.09600  -16.25200 1.000 31.82000 ? 32  LEU A CA  1 
ATOM   221  C C   . LEU A 1 30  ? -16.58300 23.21100  -17.28400 1.000 37.30000 ? 32  LEU A C   1 
ATOM   222  O O   . LEU A 1 30  ? -17.45400 24.08800  -17.29700 1.000 33.61000 ? 32  LEU A O   1 
ATOM   223  C CB  . LEU A 1 30  ? -17.84500 21.19200  -16.52600 1.000 29.84000 ? 32  LEU A CB  1 
ATOM   224  C CG  . LEU A 1 30  ? -18.11600 20.06300  -15.52500 1.000 31.50000 ? 32  LEU A CG  1 
ATOM   225  C CD1 . LEU A 1 30  ? -19.51200 19.47700  -15.75300 1.000 33.20000 ? 32  LEU A CD1 1 
ATOM   226  C CD2 . LEU A 1 30  ? -17.07700 18.98800  -15.63500 1.000 27.27000 ? 32  LEU A CD2 1 
ATOM   227  N N   . ASP A 1 31  ? -15.57100 23.17000  -18.15400 1.000 34.02000 ? 33  ASP A N   1 
ATOM   228  C CA  . ASP A 1 31  ? -15.32000 24.26000  -19.11100 1.000 35.34000 ? 33  ASP A CA  1 
ATOM   229  C C   . ASP A 1 31  ? -15.24700 25.55200  -18.30000 1.000 35.75000 ? 33  ASP A C   1 
ATOM   230  O O   . ASP A 1 31  ? -14.53000 25.59400  -17.28500 1.000 32.58000 ? 33  ASP A O   1 
ATOM   231  C CB  . ASP A 1 31  ? -16.36900 24.23500  -20.22000 1.000 36.81000 ? 33  ASP A CB  1 
ATOM   232  C CG  . ASP A 1 31  ? -16.38800 22.92200  -20.97500 1.000 41.28000 ? 33  ASP A CG  1 
ATOM   233  O OD1 . ASP A 1 31  ? -15.30200 22.44000  -21.33400 1.000 43.03000 ? 33  ASP A OD1 1 
ATOM   234  O OD2 . ASP A 1 31  ? -17.48500 22.36900  -21.20900 1.000 43.86000 ? 33  ASP A OD2 1 
ATOM   235  N N   . ASP A 1 32  ? -15.97700 26.60700  -18.67400 1.000 35.59000 ? 34  ASP A N   1 
ATOM   236  C CA  . ASP A 1 32  ? -15.92900 27.88400  -17.97200 1.000 36.42000 ? 34  ASP A CA  1 
ATOM   237  C C   . ASP A 1 32  ? -17.15300 28.11300  -17.08400 1.000 37.17000 ? 34  ASP A C   1 
ATOM   238  O O   . ASP A 1 32  ? -17.55700 29.26700  -16.86500 1.000 35.09000 ? 34  ASP A O   1 
ATOM   239  C CB  . ASP A 1 32  ? -15.77000 29.02700  -18.98100 1.000 39.35000 ? 34  ASP A CB  1 
ATOM   240  C CG  . ASP A 1 32  ? -16.96200 29.14400  -19.94200 1.000 40.75000 ? 34  ASP A CG  1 
ATOM   241  O OD1 . ASP A 1 32  ? -17.63600 28.12900  -20.22200 1.000 40.67000 ? 34  ASP A OD1 1 
ATOM   242  O OD2 . ASP A 1 32  ? -17.22200 30.26100  -20.42600 1.000 48.43000 ? 34  ASP A OD2 1 
ATOM   243  N N   . VAL A 1 33  ? -17.74500 27.03900  -16.55800 1.000 34.06000 ? 35  VAL A N   1 
ATOM   244  C CA  . VAL A 1 33  ? -18.94100 27.11600  -15.72400 1.000 29.90000 ? 35  VAL A CA  1 
ATOM   245  C C   . VAL A 1 33  ? -18.71400 26.33200  -14.44100 1.000 32.38000 ? 35  VAL A C   1 
ATOM   246  O O   . VAL A 1 33  ? -18.27900 25.16900  -14.48200 1.000 29.88000 ? 35  VAL A O   1 
ATOM   247  C CB  . VAL A 1 33  ? -20.18600 26.56800  -16.44200 1.000 31.96000 ? 35  VAL A CB  1 
ATOM   248  C CG1 . VAL A 1 33  ? -21.42000 26.68900  -15.51800 1.000 28.24000 ? 35  VAL A CG1 1 
ATOM   249  C CG2 . VAL A 1 33  ? -20.42000 27.29800  -17.75600 1.000 38.38000 ? 35  VAL A CG2 1 
ATOM   250  N N   . VAL A 1 34  ? -19.06600 26.94500  -13.31200 1.000 31.37000 ? 36  VAL A N   1 
ATOM   251  C CA  . VAL A 1 34  ? -19.12000 26.26400  -12.02100 1.000 30.92000 ? 36  VAL A CA  1 
ATOM   252  C C   . VAL A 1 34  ? -20.59000 26.04200  -11.67000 1.000 30.01000 ? 36  VAL A C   1 
ATOM   253  O O   . VAL A 1 34  ? -21.38100 26.99800  -11.63500 1.000 31.26000 ? 36  VAL A O   1 
ATOM   254  C CB  . VAL A 1 34  ? -18.37600 27.06200  -10.93400 1.000 32.25000 ? 36  VAL A CB  1 
ATOM   255  C CG1 . VAL A 1 34  ? -18.55200 26.41800  -9.56300  1.000 29.45000 ? 36  VAL A CG1 1 
ATOM   256  C CG2 . VAL A 1 34  ? -16.89800 27.13300  -11.28800 1.000 33.51000 ? 36  VAL A CG2 1 
ATOM   257  N N   . TYR A 1 35  ? -20.95800 24.77500  -11.44400 1.000 26.63000 ? 37  TYR A N   1 
ATOM   258  C CA  . TYR A 1 35  ? -22.30100 24.38600  -11.04200 1.000 29.28000 ? 37  TYR A CA  1 
ATOM   259  C C   . TYR A 1 35  ? -22.30900 24.13000  -9.54400  1.000 29.60000 ? 37  TYR A C   1 
ATOM   260  O O   . TYR A 1 35  ? -21.41100 23.47600  -9.01600  1.000 30.30000 ? 37  TYR A O   1 
ATOM   261  C CB  . TYR A 1 35  ? -22.76800 23.12200  -11.77800 1.000 27.92000 ? 37  TYR A CB  1 
ATOM   262  C CG  . TYR A 1 35  ? -22.70500 23.20400  -13.29100 1.000 29.19000 ? 37  TYR A CG  1 
ATOM   263  C CD1 . TYR A 1 35  ? -21.49900 23.04700  -13.96600 1.000 29.27000 ? 37  TYR A CD1 1 
ATOM   264  C CD2 . TYR A 1 35  ? -23.85200 23.43300  -14.04700 1.000 29.13000 ? 37  TYR A CD2 1 
ATOM   265  C CE1 . TYR A 1 35  ? -21.43000 23.12800  -15.34300 1.000 28.67000 ? 37  TYR A CE1 1 
ATOM   266  C CE2 . TYR A 1 35  ? -23.79000 23.51700  -15.43800 1.000 28.84000 ? 37  TYR A CE2 1 
ATOM   267  C CZ  . TYR A 1 35  ? -22.57600 23.37100  -16.07300 1.000 30.08000 ? 37  TYR A CZ  1 
ATOM   268  O OH  . TYR A 1 35  ? -22.49500 23.44800  -17.44300 1.000 30.17000 ? 37  TYR A OH  1 
ATOM   269  N N   . CYS A 1 36  ? -23.32300 24.63300  -8.85500  1.000 28.55000 ? 38  CYS A N   1 
ATOM   270  C CA  . CYS A 1 36  ? -23.42200 24.35400  -7.42400  1.000 29.28000 ? 38  CYS A CA  1 
ATOM   271  C C   . CYS A 1 36  ? -24.88700 24.48800  -7.02200  1.000 28.35000 ? 38  CYS A C   1 
ATOM   272  O O   . CYS A 1 36  ? -25.70700 25.02100  -7.78300  1.000 29.12000 ? 38  CYS A O   1 
ATOM   273  C CB  . CYS A 1 36  ? -22.50800 25.29200  -6.61400  1.000 26.23000 ? 38  CYS A CB  1 
ATOM   274  S SG  . CYS A 1 36  ? -23.03800 27.01600  -6.58700  1.000 28.85000 ? 38  CYS A SG  1 
ATOM   275  N N   . PRO A 1 37  ? -25.24500 23.97900  -5.83300  1.000 26.54000 ? 39  PRO A N   1 
ATOM   276  C CA  . PRO A 1 37  ? -26.61900 24.19600  -5.34700  1.000 25.82000 ? 39  PRO A CA  1 
ATOM   277  C C   . PRO A 1 37  ? -26.91100 25.68100  -5.16600  1.000 27.32000 ? 39  PRO A C   1 
ATOM   278  O O   . PRO A 1 37  ? -26.09700 26.43900  -4.62900  1.000 27.35000 ? 39  PRO A O   1 
ATOM   279  C CB  . PRO A 1 37  ? -26.64700 23.45400  -4.00600  1.000 24.02000 ? 39  PRO A CB  1 
ATOM   280  C CG  . PRO A 1 37  ? -25.47200 22.44100  -4.10200  1.000 26.70000 ? 39  PRO A CG  1 
ATOM   281  C CD  . PRO A 1 37  ? -24.43300 23.18200  -4.89100  1.000 23.81000 ? 39  PRO A CD  1 
ATOM   282  N N   . ARG A 1 38  ? -28.10100 26.09300  -5.60300  1.000 27.04000 ? 40  ARG A N   1 
ATOM   283  C CA  . ARG A 1 38  ? -28.46400 27.50000  -5.47100  1.000 27.70000 ? 40  ARG A CA  1 
ATOM   284  C C   . ARG A 1 38  ? -28.63100 27.91500  -4.01900  1.000 28.66000 ? 40  ARG A C   1 
ATOM   285  O O   . ARG A 1 38  ? -28.58500 29.11600  -3.72500  1.000 27.92000 ? 40  ARG A O   1 
ATOM   286  C CB  . ARG A 1 38  ? -29.73500 27.80500  -6.25500  1.000 25.17000 ? 40  ARG A CB  1 
ATOM   287  C CG  . ARG A 1 38  ? -31.02000 27.24300  -5.67300  1.000 30.81000 ? 40  ARG A CG  1 
ATOM   288  C CD  . ARG A 1 38  ? -32.24300 27.77900  -6.42500  1.000 28.01000 ? 40  ARG A CD  1 
ATOM   289  N NE  . ARG A 1 38  ? -33.46100 27.10900  -5.97800  1.000 27.76000 ? 40  ARG A NE  1 
ATOM   290  C CZ  . ARG A 1 38  ? -34.68200 27.42300  -6.39100  1.000 30.41000 ? 40  ARG A CZ  1 
ATOM   291  N NH1 . ARG A 1 38  ? -34.86100 28.40300  -7.28100  1.000 25.69000 ? 40  ARG A NH1 1 
ATOM   292  N NH2 . ARG A 1 38  ? -35.71800 26.75900  -5.90700  1.000 25.86000 ? 40  ARG A NH2 1 
ATOM   293  N N   . HIS A 1 39  ? -28.78100 26.95900  -3.09600  1.000 26.91000 ? 41  HIS A N   1 
ATOM   294  C CA  . HIS A 1 39  ? -28.96800 27.36400  -1.70900  1.000 27.03000 ? 41  HIS A CA  1 
ATOM   295  C C   . HIS A 1 39  ? -27.68300 27.89000  -1.06700  1.000 28.67000 ? 41  HIS A C   1 
ATOM   296  O O   . HIS A 1 39  ? -27.71600 28.31300  0.09800   1.000 25.09000 ? 41  HIS A O   1 
ATOM   297  C CB  . HIS A 1 39  ? -29.60400 26.22200  -0.88800  1.000 29.12000 ? 41  HIS A CB  1 
ATOM   298  C CG  . HIS A 1 39  ? -28.74400 25.00300  -0.68000  1.000 27.41000 ? 41  HIS A CG  1 
ATOM   299  N ND1 . HIS A 1 39  ? -27.55900 25.02500  0.02500   1.000 27.79000 ? 41  HIS A ND1 1 
ATOM   300  C CD2 . HIS A 1 39  ? -28.97400 23.69900  -0.98000  1.000 29.66000 ? 41  HIS A CD2 1 
ATOM   301  C CE1 . HIS A 1 39  ? -27.06800 23.79600  0.10000   1.000 27.30000 ? 41  HIS A CE1 1 
ATOM   302  N NE2 . HIS A 1 39  ? -27.91400 22.97400  -0.49400  1.000 29.33000 ? 41  HIS A NE2 1 
ATOM   303  N N   . VAL A 1 40  ? -26.57400 27.93700  -1.80700  1.000 25.49000 ? 42  VAL A N   1 
ATOM   304  C CA  . VAL A 1 40  ? -25.41200 28.65000  -1.30500  1.000 28.57000 ? 42  VAL A CA  1 
ATOM   305  C C   . VAL A 1 40  ? -25.73500 30.13100  -1.08400  1.000 29.01000 ? 42  VAL A C   1 
ATOM   306  O O   . VAL A 1 40  ? -25.11200 30.76700  -0.23500  1.000 31.28000 ? 42  VAL A O   1 
ATOM   307  C CB  . VAL A 1 40  ? -24.20200 28.47800  -2.24800  1.000 26.97000 ? 42  VAL A CB  1 
ATOM   308  C CG1 . VAL A 1 40  ? -24.43000 29.18900  -3.58400  1.000 28.51000 ? 42  VAL A CG1 1 
ATOM   309  C CG2 . VAL A 1 40  ? -22.92900 29.00500  -1.58200  1.000 28.91000 ? 42  VAL A CG2 1 
ATOM   310  N N   . ILE A 1 41  ? -26.72200 30.68800  -1.80200  1.000 28.62000 ? 43  ILE A N   1 
ATOM   311  C CA  . ILE A 1 41  ? -27.07700 32.09900  -1.62300  1.000 33.34000 ? 43  ILE A CA  1 
ATOM   312  C C   . ILE A 1 41  ? -28.11100 32.30500  -0.53300  1.000 35.50000 ? 43  ILE A C   1 
ATOM   313  O O   . ILE A 1 41  ? -28.53900 33.44500  -0.30200  1.000 32.38000 ? 43  ILE A O   1 
ATOM   314  C CB  . ILE A 1 41  ? -27.56900 32.74900  -2.93800  1.000 34.00000 ? 43  ILE A CB  1 
ATOM   315  C CG1 . ILE A 1 41  ? -28.96500 32.25100  -3.35600  1.000 31.26000 ? 43  ILE A CG1 1 
ATOM   316  C CG2 . ILE A 1 41  ? -26.53000 32.56800  -4.04000  1.000 30.37000 ? 43  ILE A CG2 1 
ATOM   317  C CD1 . ILE A 1 41  ? -29.56600 33.09100  -4.49500  1.000 30.86000 ? 43  ILE A CD1 1 
ATOM   318  N N   . CYS A 1 42  ? -28.52200 31.24500  0.15100   1.000 30.33000 ? 44  CYS A N   1 
ATOM   319  C CA  . CYS A 1 42  ? -29.49500 31.34700  1.22600   1.000 34.37000 ? 44  CYS A CA  1 
ATOM   320  C C   . CYS A 1 42  ? -28.83100 31.86700  2.49900   1.000 40.22000 ? 44  CYS A C   1 
ATOM   321  O O   . CYS A 1 42  ? -27.68800 31.51600  2.79400   1.000 34.87000 ? 44  CYS A O   1 
ATOM   322  C CB  . CYS A 1 42  ? -30.11400 29.96700  1.45500   1.000 32.49000 ? 44  CYS A CB  1 
ATOM   323  S SG  . CYS A 1 42  ? -31.60400 29.90800  2.39100   1.000 43.53000 ? 44  CYS A SG  1 
ATOM   324  N N   . THR A 1 43  ? -29.53800 32.72200  3.24900   1.000 39.79000 ? 45  THR A N   1 
ATOM   325  C CA  . THR A 1 43  ? -29.03100 33.19000  4.53600   1.000 43.01000 ? 45  THR A CA  1 
ATOM   326  C C   . THR A 1 43  ? -29.64400 32.38200  5.67600   1.000 44.27000 ? 45  THR A C   1 
ATOM   327  O O   . THR A 1 43  ? -30.61400 31.64300  5.49700   1.000 45.68000 ? 45  THR A O   1 
ATOM   328  C CB  . THR A 1 43  ? -29.30700 34.68600  4.74100   1.000 40.91000 ? 45  THR A CB  1 
ATOM   329  O OG1 . THR A 1 43  ? -30.70600 34.87300  4.97700   1.000 37.80000 ? 45  THR A OG1 1 
ATOM   330  C CG2 . THR A 1 43  ? -28.87600 35.48800  3.52300   1.000 41.94000 ? 45  THR A CG2 1 
ATOM   331  N N   . SER A 1 44  ? -29.08100 32.57200  6.87500   1.000 46.06000 ? 46  SER A N   1 
ATOM   332  C CA  . SER A 1 44  ? -29.41300 31.72500  8.02200   1.000 48.92000 ? 46  SER A CA  1 
ATOM   333  C C   . SER A 1 44  ? -30.88300 31.82300  8.43000   1.000 54.54000 ? 46  SER A C   1 
ATOM   334  O O   . SER A 1 44  ? -31.42000 30.87400  9.01600   1.000 60.48000 ? 46  SER A O   1 
ATOM   335  C CB  . SER A 1 44  ? -28.50100 32.06500  9.20000   1.000 57.65000 ? 46  SER A CB  1 
ATOM   336  O OG  . SER A 1 44  ? -27.15400 32.16100  8.79300   1.000 56.54000 ? 46  SER A OG  1 
ATOM   337  N N   . GLU A 1 45  ? -31.55500 32.94300  8.14100   1.000 56.73000 ? 47  GLU A N   1 
ATOM   338  C CA  . GLU A 1 45  ? -33.00300 33.00700  8.31700   1.000 51.81000 ? 47  GLU A CA  1 
ATOM   339  C C   . GLU A 1 45  ? -33.73700 33.20100  7.00000   1.000 52.54000 ? 47  GLU A C   1 
ATOM   340  O O   . GLU A 1 45  ? -34.91000 33.57600  6.99400   1.000 54.05000 ? 47  GLU A O   1 
ATOM   341  C CB  . GLU A 1 45  ? -33.41300 34.08800  9.31900   1.000 53.62000 ? 47  GLU A CB  1 
ATOM   342  C CG  . GLU A 1 45  ? -32.81500 35.46300  9.07300   1.000 63.69000 ? 47  GLU A CG  1 
ATOM   343  C CD  . GLU A 1 45  ? -31.34300 35.53800  9.43900   1.000 61.23000 ? 47  GLU A CD  1 
ATOM   344  O OE1 . GLU A 1 45  ? -30.73000 34.48100  9.71300   1.000 63.31000 ? 47  GLU A OE1 1 
ATOM   345  O OE2 . GLU A 1 45  ? -30.79300 36.65400  9.46500   1.000 66.79000 ? 47  GLU A OE2 1 
ATOM   346  N N   . ASP A 1 46  ? -33.05500 32.98500  5.88500   1.000 54.78000 ? 48  ASP A N   1 
ATOM   347  C CA  . ASP A 1 46  ? -33.73200 32.68500  4.63600   1.000 50.51000 ? 48  ASP A CA  1 
ATOM   348  C C   . ASP A 1 46  ? -34.14800 31.23900  4.55700   1.000 43.28000 ? 48  ASP A C   1 
ATOM   349  O O   . ASP A 1 46  ? -34.85600 30.87800  3.61600   1.000 49.39000 ? 48  ASP A O   1 
ATOM   350  C CB  . ASP A 1 46  ? -32.84500 32.98100  3.41800   1.000 43.78000 ? 48  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 46  ? -32.95900 34.40300  2.95400   1.000 50.80000 ? 48  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 46  ? -34.08400 34.85600  2.59400   1.000 51.99000 ? 48  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 46  ? -31.90500 35.06900  2.94100   1.000 57.52000 ? 48  ASP A OD2 1 
ATOM   354  N N   . MET A 1 47  ? -33.74200 30.41000  5.52500   1.000 46.55000 ? 49  MET A N   1 
ATOM   355  C CA  . MET A 1 47  ? -33.72200 28.96900  5.29100   1.000 40.93000 ? 49  MET A CA  1 
ATOM   356  C C   . MET A 1 47  ? -35.12300 28.38800  5.16700   1.000 42.02000 ? 49  MET A C   1 
ATOM   357  O O   . MET A 1 47  ? -35.31300 27.38200  4.47200   1.000 38.38000 ? 49  MET A O   1 
ATOM   358  C CB  . MET A 1 47  ? -32.94000 28.25800  6.40000   1.000 45.03000 ? 49  MET A CB  1 
ATOM   359  C CG  . MET A 1 47  ? -31.47200 28.67800  6.49500   1.000 45.00000 ? 49  MET A CG  1 
ATOM   360  S SD  . MET A 1 47  ? -30.40100 27.43600  7.27200   1.000 47.98000 ? 49  MET A SD  1 
ATOM   361  C CE  . MET A 1 47  ? -31.24600 27.17500  8.83300   1.000 49.89000 ? 49  MET A CE  1 
ATOM   362  N N   . LEU A 1 48  ? -36.11500 29.01300  5.80700   1.000 41.44000 ? 50  LEU A N   1 
ATOM   363  C CA  . LEU A 1 48  ? -37.46700 28.46400  5.77300   1.000 36.88000 ? 50  LEU A CA  1 
ATOM   364  C C   . LEU A 1 48  ? -38.19900 28.85000  4.49100   1.000 32.20000 ? 50  LEU A C   1 
ATOM   365  O O   . LEU A 1 48  ? -38.80500 28.00100  3.84100   1.000 33.43000 ? 50  LEU A O   1 
ATOM   366  C CB  . LEU A 1 48  ? -38.24400 28.91800  7.00600   1.000 35.24000 ? 50  LEU A CB  1 
ATOM   367  C CG  . LEU A 1 48  ? -37.81200 28.22600  8.30300   1.000 39.64000 ? 50  LEU A CG  1 
ATOM   368  C CD1 . LEU A 1 48  ? -38.24800 29.03900  9.50800   1.000 43.36000 ? 50  LEU A CD1 1 
ATOM   369  C CD2 . LEU A 1 48  ? -38.36200 26.80100  8.40500   1.000 41.37000 ? 50  LEU A CD2 1 
ATOM   370  N N   . ASN A 1 49  ? -38.14700 30.11400  4.08100   1.000 37.82000 ? 51  ASN A N   1 
ATOM   371  C CA  . ASN A 1 49  ? -38.87700 30.55500  2.89100   1.000 33.64000 ? 51  ASN A CA  1 
ATOM   372  C C   . ASN A 1 49  ? -38.02500 31.50400  2.07000   1.000 37.64000 ? 51  ASN A C   1 
ATOM   373  O O   . ASN A 1 49  ? -38.35900 32.68200  1.89500   1.000 35.72000 ? 51  ASN A O   1 
ATOM   374  C CB  . ASN A 1 49  ? -40.21400 31.18100  3.28800   1.000 33.52000 ? 51  ASN A CB  1 
ATOM   375  C CG  . ASN A 1 49  ? -41.20500 30.13400  3.76300   1.000 31.39000 ? 51  ASN A CG  1 
ATOM   376  O OD1 . ASN A 1 49  ? -41.82300 29.45200  2.95400   1.000 31.59000 ? 51  ASN A OD1 1 
ATOM   377  N ND2 . ASN A 1 49  ? -41.32600 29.97400  5.06900   1.000 28.43000 ? 51  ASN A ND2 1 
ATOM   378  N N   . PRO A 1 50  ? -36.90700 31.01800  1.53300   1.000 38.12000 ? 52  PRO A N   1 
ATOM   379  C CA  . PRO A 1 50  ? -36.09600 31.87000  0.67000   1.000 36.07000 ? 52  PRO A CA  1 
ATOM   380  C C   . PRO A 1 50  ? -36.81400 32.09400  -0.64800  1.000 34.73000 ? 52  PRO A C   1 
ATOM   381  O O   . PRO A 1 50  ? -37.50800 31.20800  -1.15000  1.000 31.23000 ? 52  PRO A O   1 
ATOM   382  C CB  . PRO A 1 50  ? -34.80300 31.06500  0.48100   1.000 37.27000 ? 52  PRO A CB  1 
ATOM   383  C CG  . PRO A 1 50  ? -35.21300 29.63200  0.65800   1.000 34.11000 ? 52  PRO A CG  1 
ATOM   384  C CD  . PRO A 1 50  ? -36.47800 29.60000  1.48200   1.000 38.30000 ? 52  PRO A CD  1 
ATOM   385  N N   . ASN A 1 51  ? -36.67300 33.30100  -1.18900  1.000 28.81000 ? 53  ASN A N   1 
ATOM   386  C CA  . ASN A 1 51  ? -37.04800 33.56800  -2.57500  1.000 30.33000 ? 53  ASN A CA  1 
ATOM   387  C C   . ASN A 1 51  ? -35.74900 33.70000  -3.35800  1.000 32.55000 ? 53  ASN A C   1 
ATOM   388  O O   . ASN A 1 51  ? -35.07200 34.73100  -3.29300  1.000 29.43000 ? 53  ASN A O   1 
ATOM   389  C CB  . ASN A 1 51  ? -37.91500 34.81800  -2.71600  1.000 31.47000 ? 53  ASN A CB  1 
ATOM   390  C CG  . ASN A 1 51  ? -38.43000 34.99200  -4.13200  1.000 32.46000 ? 53  ASN A CG  1 
ATOM   391  O OD1 . ASN A 1 51  ? -37.66400 35.25500  -5.05400  1.000 34.87000 ? 53  ASN A OD1 1 
ATOM   392  N ND2 . ASN A 1 51  ? -39.72000 34.80200  -4.31800  1.000 38.74000 ? 53  ASN A ND2 1 
ATOM   393  N N   . TYR A 1 52  ? -35.41300 32.65200  -4.10600  1.000 33.49000 ? 54  TYR A N   1 
ATOM   394  C CA  . TYR A 1 52  ? -34.10100 32.59600  -4.73300  1.000 31.28000 ? 54  TYR A CA  1 
ATOM   395  C C   . TYR A 1 52  ? -33.95500 33.61200  -5.86000  1.000 28.73000 ? 54  TYR A C   1 
ATOM   396  O O   . TYR A 1 52  ? -32.85400 34.12800  -6.07700  1.000 29.98000 ? 54  TYR A O   1 
ATOM   397  C CB  . TYR A 1 52  ? -33.83300 31.17700  -5.23800  1.000 28.33000 ? 54  TYR A CB  1 
ATOM   398  C CG  . TYR A 1 52  ? -33.49600 30.23600  -4.10900  1.000 30.09000 ? 54  TYR A CG  1 
ATOM   399  C CD1 . TYR A 1 52  ? -32.28400 30.34400  -3.44400  1.000 30.80000 ? 54  TYR A CD1 1 
ATOM   400  C CD2 . TYR A 1 52  ? -34.39200 29.25500  -3.69300  1.000 30.79000 ? 54  TYR A CD2 1 
ATOM   401  C CE1 . TYR A 1 52  ? -31.96400 29.51000  -2.40400  1.000 31.81000 ? 54  TYR A CE1 1 
ATOM   402  C CE2 . TYR A 1 52  ? -34.08100 28.41700  -2.64800  1.000 32.11000 ? 54  TYR A CE2 1 
ATOM   403  C CZ  . TYR A 1 52  ? -32.86500 28.54900  -2.01200  1.000 30.50000 ? 54  TYR A CZ  1 
ATOM   404  O OH  . TYR A 1 52  ? -32.54000 27.72500  -0.97200  1.000 31.02000 ? 54  TYR A OH  1 
ATOM   405  N N   . GLU A 1 53  ? -35.02300 33.87600  -6.60900  1.000 30.73000 ? 55  GLU A N   1 
ATOM   406  C CA  . GLU A 1 53  ? -34.94600 34.90100  -7.64300  1.000 33.21000 ? 55  GLU A CA  1 
ATOM   407  C C   . GLU A 1 53  ? -34.62800 36.26400  -7.03300  1.000 32.96000 ? 55  GLU A C   1 
ATOM   408  O O   . GLU A 1 53  ? -33.77000 36.99700  -7.54200  1.000 28.03000 ? 55  GLU A O   1 
ATOM   409  C CB  . GLU A 1 53  ? -36.25300 34.94700  -8.43300  1.000 33.58000 ? 55  GLU A CB  1 
ATOM   410  C CG  . GLU A 1 53  ? -36.23400 35.91500  -9.64000  1.000 42.58000 ? 55  GLU A CG  1 
ATOM   411  C CD  . GLU A 1 53  ? -37.64200 36.33100  -10.08300 1.000 45.88000 ? 55  GLU A CD  1 
ATOM   412  O OE1 . GLU A 1 53  ? -37.79400 37.40100  -10.70500 1.000 48.23000 ? 55  GLU A OE1 1 
ATOM   413  O OE2 . GLU A 1 53  ? -38.60100 35.58200  -9.79800  1.000 47.32000 ? 55  GLU A OE2 1 
ATOM   414  N N   . ASP A 1 54  ? -35.28600 36.59800  -5.92100  1.000 31.35000 ? 56  ASP A N   1 
ATOM   415  C CA  . ASP A 1 54  ? -34.99500 37.84600  -5.22400  1.000 31.29000 ? 56  ASP A CA  1 
ATOM   416  C C   . ASP A 1 54  ? -33.60300 37.81500  -4.60300  1.000 32.70000 ? 56  ASP A C   1 
ATOM   417  O O   . ASP A 1 54  ? -32.88200 38.81900  -4.62000  1.000 29.30000 ? 56  ASP A O   1 
ATOM   418  C CB  . ASP A 1 54  ? -36.05000 38.10700  -4.14800  1.000 28.99000 ? 56  ASP A CB  1 
ATOM   419  C CG  . ASP A 1 54  ? -36.03700 39.54700  -3.66400  1.000 34.54000 ? 56  ASP A CG  1 
ATOM   420  O OD1 . ASP A 1 54  ? -36.50800 40.42400  -4.40900  1.000 32.88000 ? 56  ASP A OD1 1 
ATOM   421  O OD2 . ASP A 1 54  ? -35.56100 39.79600  -2.54000  1.000 35.58000 ? 56  ASP A OD2 1 
ATOM   422  N N   . LEU A 1 55  ? -33.21200 36.67900  -4.02900  1.000 29.10000 ? 57  LEU A N   1 
ATOM   423  C CA  . LEU A 1 55  ? -31.87400 36.61800  -3.45700  1.000 28.71000 ? 57  LEU A CA  1 
ATOM   424  C C   . LEU A 1 55  ? -30.80800 36.74000  -4.53900  1.000 30.27000 ? 57  LEU A C   1 
ATOM   425  O O   . LEU A 1 55  ? -29.75800 37.34700  -4.30800  1.000 33.67000 ? 57  LEU A O   1 
ATOM   426  C CB  . LEU A 1 55  ? -31.70100 35.32200  -2.66800  1.000 33.72000 ? 57  LEU A CB  1 
ATOM   427  C CG  . LEU A 1 55  ? -32.44000 35.21300  -1.33500  1.000 35.91000 ? 57  LEU A CG  1 
ATOM   428  C CD1 . LEU A 1 55  ? -32.29500 33.80000  -0.76400  1.000 37.62000 ? 57  LEU A CD1 1 
ATOM   429  C CD2 . LEU A 1 55  ? -31.92600 36.25900  -0.36000  1.000 38.24000 ? 57  LEU A CD2 1 
ATOM   430  N N   . LEU A 1 56  ? -31.06300 36.19900  -5.73000  1.000 29.82000 ? 58  LEU A N   1 
ATOM   431  C CA  . LEU A 1 56  ? -30.01700 36.19400  -6.74600  1.000 31.14000 ? 58  LEU A CA  1 
ATOM   432  C C   . LEU A 1 56  ? -29.85900 37.57200  -7.38200  1.000 29.46000 ? 58  LEU A C   1 
ATOM   433  O O   . LEU A 1 56  ? -28.73900 38.00300  -7.67000  1.000 32.49000 ? 58  LEU A O   1 
ATOM   434  C CB  . LEU A 1 56  ? -30.32700 35.14700  -7.81200  1.000 30.85000 ? 58  LEU A CB  1 
ATOM   435  C CG  . LEU A 1 56  ? -29.20700 34.88100  -8.81200  1.000 32.26000 ? 58  LEU A CG  1 
ATOM   436  C CD1 . LEU A 1 56  ? -27.90000 34.48500  -8.12100  1.000 33.55000 ? 58  LEU A CD1 1 
ATOM   437  C CD2 . LEU A 1 56  ? -29.64700 33.80900  -9.79200  1.000 32.36000 ? 58  LEU A CD2 1 
ATOM   438  N N   . ILE A 1 57  ? -30.96700 38.28100  -7.59200  1.000 32.13000 ? 59  ILE A N   1 
ATOM   439  C CA  . ILE A 1 57  ? -30.90300 39.57900  -8.25300  1.000 30.37000 ? 59  ILE A CA  1 
ATOM   440  C C   . ILE A 1 57  ? -30.04800 40.56300  -7.46400  1.000 30.12000 ? 59  ILE A C   1 
ATOM   441  O O   . ILE A 1 57  ? -29.47800 41.48800  -8.04900  1.000 30.53000 ? 59  ILE A O   1 
ATOM   442  C CB  . ILE A 1 57  ? -32.33600 40.10300  -8.50400  1.000 29.83000 ? 59  ILE A CB  1 
ATOM   443  C CG1 . ILE A 1 57  ? -32.35100 41.11400  -9.66500  1.000 33.79000 ? 59  ILE A CG1 1 
ATOM   444  C CG2 . ILE A 1 57  ? -32.92200 40.73200  -7.24200  1.000 33.24000 ? 59  ILE A CG2 1 
ATOM   445  C CD1 . ILE A 1 57  ? -33.74000 41.56500  -10.07000 1.000 32.95000 ? 59  ILE A CD1 1 
ATOM   446  N N   . ARG A 1 58  ? -29.92100 40.36700  -6.14800  1.000 29.13000 ? 60  ARG A N   1 
ATOM   447  C CA  . ARG A 1 58  ? -29.17800 41.24800  -5.26200  1.000 29.68000 ? 60  ARG A CA  1 
ATOM   448  C C   . ARG A 1 58  ? -27.68700 40.94400  -5.22400  1.000 33.73000 ? 60  ARG A C   1 
ATOM   449  O O   . ARG A 1 58  ? -26.93000 41.73400  -4.65100  1.000 30.58000 ? 60  ARG A O   1 
ATOM   450  C CB  . ARG A 1 58  ? -29.74200 41.16100  -3.83700  1.000 29.97000 ? 60  ARG A CB  1 
ATOM   451  C CG  . ARG A 1 58  ? -31.22700 41.48100  -3.72200  1.000 26.01000 ? 60  ARG A CG  1 
ATOM   452  C CD  . ARG A 1 58  ? -31.73200 41.25900  -2.29900  1.000 24.74000 ? 60  ARG A CD  1 
ATOM   453  N NE  . ARG A 1 58  ? -33.18300 41.43600  -2.22200  1.000 27.01000 ? 60  ARG A NE  1 
ATOM   454  C CZ  . ARG A 1 58  ? -33.79100 42.56300  -1.85900  1.000 29.24000 ? 60  ARG A CZ  1 
ATOM   455  N NH1 . ARG A 1 58  ? -33.07200 43.63900  -1.54200  1.000 26.10000 ? 60  ARG A NH1 1 
ATOM   456  N NH2 . ARG A 1 58  ? -35.12300 42.62000  -1.81800  1.000 25.85000 ? 60  ARG A NH2 1 
ATOM   457  N N   . LYS A 1 59  ? -27.26000 39.82400  -5.80500  1.000 31.12000 ? 61  LYS A N   1 
ATOM   458  C CA  . LYS A 1 59  ? -25.86200 39.43200  -5.84800  1.000 32.34000 ? 61  LYS A CA  1 
ATOM   459  C C   . LYS A 1 59  ? -25.21800 40.03000  -7.08500  1.000 32.94000 ? 61  LYS A C   1 
ATOM   460  O O   . LYS A 1 59  ? -25.85400 40.14300  -8.13700  1.000 31.60000 ? 61  LYS A O   1 
ATOM   461  C CB  . LYS A 1 59  ? -25.71400 37.90200  -5.90100  1.000 33.80000 ? 61  LYS A CB  1 
ATOM   462  C CG  . LYS A 1 59  ? -26.32300 37.14700  -4.74200  1.000 35.87000 ? 61  LYS A CG  1 
ATOM   463  C CD  . LYS A 1 59  ? -25.53900 37.42500  -3.48700  1.000 38.87000 ? 61  LYS A CD  1 
ATOM   464  C CE  . LYS A 1 59  ? -26.29200 36.98100  -2.26000  1.000 37.92000 ? 61  LYS A CE  1 
ATOM   465  N NZ  . LYS A 1 59  ? -25.30600 36.87700  -1.15700  1.000 43.19000 ? 61  LYS A NZ  1 
ATOM   466  N N   . SER A 1 60  ? -23.95800 40.41200  -6.95700  1.000 30.69000 ? 62  SER A N   1 
ATOM   467  C CA  . SER A 1 60  ? -23.13100 40.61600  -8.13200  1.000 37.73000 ? 62  SER A CA  1 
ATOM   468  C C   . SER A 1 60  ? -22.07100 39.52600  -8.20200  1.000 37.47000 ? 62  SER A C   1 
ATOM   469  O O   . SER A 1 60  ? -21.85700 38.76000  -7.25500  1.000 34.79000 ? 62  SER A O   1 
ATOM   470  C CB  . SER A 1 60  ? -22.49600 42.01900  -8.15100  1.000 42.06000 ? 62  SER A CB  1 
ATOM   471  O OG  . SER A 1 60  ? -22.16200 42.48000  -6.85500  1.000 47.99000 ? 62  SER A OG  1 
ATOM   472  N N   . ASN A 1 61  ? -21.42200 39.47000  -9.36400  1.000 35.48000 ? 63  ASN A N   1 
ATOM   473  C CA  . ASN A 1 61  ? -20.39200 38.47300  -9.62200  1.000 40.86000 ? 63  ASN A CA  1 
ATOM   474  C C   . ASN A 1 61  ? -19.42300 38.34700  -8.45600  1.000 38.41000 ? 63  ASN A C   1 
ATOM   475  O O   . ASN A 1 61  ? -19.10800 37.23500  -8.01100  1.000 36.78000 ? 63  ASN A O   1 
ATOM   476  C CB  . ASN A 1 61  ? -19.66300 38.83400  -10.91200 1.000 35.13000 ? 63  ASN A CB  1 
ATOM   477  C CG  . ASN A 1 61  ? -20.51100 38.56900  -12.11700 1.000 38.64000 ? 63  ASN A CG  1 
ATOM   478  O OD1 . ASN A 1 61  ? -21.40800 37.71500  -12.07300 1.000 38.52000 ? 63  ASN A OD1 1 
ATOM   479  N ND2 . ASN A 1 61  ? -20.25700 39.29300  -13.20200 1.000 34.79000 ? 63  ASN A ND2 1 
ATOM   480  N N   . HIS A 1 62  ? -18.96900 39.47400  -7.91800  1.000 37.71000 ? 64  HIS A N   1 
ATOM   481  C CA  . HIS A 1 62  ? -17.91800 39.39600  -6.91400  1.000 39.34000 ? 64  HIS A CA  1 
ATOM   482  C C   . HIS A 1 62  ? -18.41100 38.92800  -5.54800  1.000 37.05000 ? 64  HIS A C   1 
ATOM   483  O O   . HIS A 1 62  ? -17.58000 38.73300  -4.65500  1.000 34.37000 ? 64  HIS A O   1 
ATOM   484  C CB  . HIS A 1 62  ? -17.20000 40.74400  -6.79100  1.000 40.98000 ? 64  HIS A CB  1 
ATOM   485  C CG  . HIS A 1 62  ? -18.09100 41.87500  -6.39000  1.000 42.87000 ? 64  HIS A CG  1 
ATOM   486  N ND1 . HIS A 1 62  ? -18.40200 42.14400  -5.07400  1.000 43.91000 ? 64  HIS A ND1 1 
ATOM   487  C CD2 . HIS A 1 62  ? -18.72300 42.81900  -7.12800  1.000 44.03000 ? 64  HIS A CD2 1 
ATOM   488  C CE1 . HIS A 1 62  ? -19.19500 43.20100  -5.01900  1.000 46.92000 ? 64  HIS A CE1 1 
ATOM   489  N NE2 . HIS A 1 62  ? -19.40100 43.63300  -6.25000  1.000 47.66000 ? 64  HIS A NE2 1 
ATOM   490  N N   . ASN A 1 63  ? -19.72000 38.71300  -5.35900  1.000 36.41000 ? 65  ASN A N   1 
ATOM   491  C CA  . ASN A 1 63  ? -20.18500 38.08600  -4.12200  1.000 34.72000 ? 65  ASN A CA  1 
ATOM   492  C C   . ASN A 1 63  ? -19.91000 36.57800  -4.07100  1.000 34.59000 ? 65  ASN A C   1 
ATOM   493  O O   . ASN A 1 63  ? -20.08500 35.97500  -3.00800  1.000 33.95000 ? 65  ASN A O   1 
ATOM   494  C CB  . ASN A 1 63  ? -21.68600 38.32500  -3.91400  1.000 34.51000 ? 65  ASN A CB  1 
ATOM   495  C CG  . ASN A 1 63  ? -22.02400 39.78500  -3.66100  1.000 42.48000 ? 65  ASN A CG  1 
ATOM   496  O OD1 . ASN A 1 63  ? -22.78100 40.39900  -4.42400  1.000 41.12000 ? 65  ASN A OD1 1 
ATOM   497  N ND2 . ASN A 1 63  ? -21.47100 40.34900  -2.58600  1.000 38.89000 ? 65  ASN A ND2 1 
ATOM   498  N N   . PHE A 1 64  ? -19.48900 35.96400  -5.18000  1.000 35.75000 ? 66  PHE A N   1 
ATOM   499  C CA  . PHE A 1 64  ? -19.16500 34.54100  -5.23600  1.000 35.65000 ? 66  PHE A CA  1 
ATOM   500  C C   . PHE A 1 64  ? -17.64900 34.36000  -5.23300  1.000 37.35000 ? 66  PHE A C   1 
ATOM   501  O O   . PHE A 1 64  ? -16.96100 34.81500  -6.15700  1.000 36.94000 ? 66  PHE A O   1 
ATOM   502  C CB  . PHE A 1 64  ? -19.78000 33.89500  -6.47900  1.000 31.40000 ? 66  PHE A CB  1 
ATOM   503  C CG  . PHE A 1 64  ? -21.27300 33.98300  -6.51800  1.000 32.34000 ? 66  PHE A CG  1 
ATOM   504  C CD1 . PHE A 1 64  ? -22.04300 33.16900  -5.71800  1.000 29.72000 ? 66  PHE A CD1 1 
ATOM   505  C CD2 . PHE A 1 64  ? -21.91000 34.91600  -7.33900  1.000 37.91000 ? 66  PHE A CD2 1 
ATOM   506  C CE1 . PHE A 1 64  ? -23.42400 33.26500  -5.73900  1.000 34.72000 ? 66  PHE A CE1 1 
ATOM   507  C CE2 . PHE A 1 64  ? -23.28500 35.01400  -7.36600  1.000 31.21000 ? 66  PHE A CE2 1 
ATOM   508  C CZ  . PHE A 1 64  ? -24.04700 34.19100  -6.56600  1.000 32.78000 ? 66  PHE A CZ  1 
ATOM   509  N N   . LEU A 1 65  ? -17.13700 33.70400  -4.19300  1.000 35.97000 ? 67  LEU A N   1 
ATOM   510  C CA  . LEU A 1 65  ? -15.72400 33.35200  -4.07600  1.000 32.61000 ? 67  LEU A CA  1 
ATOM   511  C C   . LEU A 1 65  ? -15.56200 31.89900  -4.52000  1.000 36.92000 ? 67  LEU A C   1 
ATOM   512  O O   . LEU A 1 65  ? -16.05000 30.97800  -3.84900  1.000 36.15000 ? 67  LEU A O   1 
ATOM   513  C CB  . LEU A 1 65  ? -15.24500 33.54500  -2.63800  1.000 34.34000 ? 67  LEU A CB  1 
ATOM   514  C CG  . LEU A 1 65  ? -13.79900 33.14900  -2.31700  1.000 44.73000 ? 67  LEU A CG  1 
ATOM   515  C CD1 . LEU A 1 65  ? -12.83200 33.87700  -3.26100  1.000 41.93000 ? 67  LEU A CD1 1 
ATOM   516  C CD2 . LEU A 1 65  ? -13.43600 33.41800  -0.84600  1.000 40.37000 ? 67  LEU A CD2 1 
ATOM   517  N N   . VAL A 1 66  ? -14.92800 31.69600  -5.67100  1.000 29.58000 ? 68  VAL A N   1 
ATOM   518  C CA  . VAL A 1 66  ? -14.68500 30.36800  -6.22000  1.000 34.95000 ? 68  VAL A CA  1 
ATOM   519  C C   . VAL A 1 66  ? -13.19300 30.08600  -6.11100  1.000 37.54000 ? 68  VAL A C   1 
ATOM   520  O O   . VAL A 1 66  ? -12.37700 30.88500  -6.58300  1.000 34.39000 ? 68  VAL A O   1 
ATOM   521  C CB  . VAL A 1 66  ? -15.16300 30.25900  -7.67800  1.000 30.25000 ? 68  VAL A CB  1 
ATOM   522  C CG1 . VAL A 1 66  ? -14.93600 28.84900  -8.19300  1.000 35.70000 ? 68  VAL A CG1 1 
ATOM   523  C CG2 . VAL A 1 66  ? -16.62900 30.61500  -7.77800  1.000 35.22000 ? 68  VAL A CG2 1 
ATOM   524  N N   . GLN A 1 67  ? -12.83700 28.96500  -5.47900  1.000 30.98000 ? 69  GLN A N   1 
ATOM   525  C CA  . GLN A 1 67  ? -11.43500 28.59100  -5.28500  1.000 35.16000 ? 69  GLN A CA  1 
ATOM   526  C C   . GLN A 1 67  ? -11.21100 27.18000  -5.81200  1.000 35.43000 ? 69  GLN A C   1 
ATOM   527  O O   . GLN A 1 67  ? -11.81800 26.22700  -5.30800  1.000 32.31000 ? 69  GLN A O   1 
ATOM   528  C CB  . GLN A 1 67  ? -11.02900 28.66900  -3.80700  1.000 36.14000 ? 69  GLN A CB  1 
ATOM   529  C CG  . GLN A 1 67  ? -11.26900 30.02100  -3.12900  1.000 45.89000 ? 69  GLN A CG  1 
ATOM   530  C CD  . GLN A 1 67  ? -11.03700 29.97900  -1.61800  1.000 49.42000 ? 69  GLN A CD  1 
ATOM   531  O OE1 . GLN A 1 67  ? -9.92200  29.72200  -1.15200  1.000 51.60000 ? 69  GLN A OE1 1 
ATOM   532  N NE2 . GLN A 1 67  ? -12.10000 30.22200  -0.84700  1.000 49.68000 ? 69  GLN A NE2 1 
ATOM   533  N N   . ALA A 1 68  ? -10.34700 27.04800  -6.82100  1.000 36.57000 ? 70  ALA A N   1 
ATOM   534  C CA  . ALA A 1 68  ? -9.89800  25.74700  -7.32300  1.000 38.24000 ? 70  ALA A CA  1 
ATOM   535  C C   . ALA A 1 68  ? -8.54300  25.46900  -6.69000  1.000 43.24000 ? 70  ALA A C   1 
ATOM   536  O O   . ALA A 1 68  ? -7.52600  26.00900  -7.12900  1.000 46.97000 ? 70  ALA A O   1 
ATOM   537  C CB  . ALA A 1 68  ? -9.80900  25.72900  -8.84400  1.000 33.07000 ? 70  ALA A CB  1 
ATOM   538  N N   . GLY A 1 69  ? -8.53300  24.63200  -5.65400  1.000 38.97000 ? 71  GLY A N   1 
ATOM   539  C CA  . GLY A 1 69  ? -7.30500  24.42000  -4.90300  1.000 45.84000 ? 71  GLY A CA  1 
ATOM   540  C C   . GLY A 1 69  ? -6.81800  25.74100  -4.33200  1.000 45.38000 ? 71  GLY A C   1 
ATOM   541  O O   . GLY A 1 69  ? -7.50900  26.40400  -3.54500  1.000 47.99000 ? 71  GLY A O   1 
ATOM   542  N N   . ASN A 1 70  ? -5.62300  26.16300  -4.74100  1.000 46.88000 ? 72  ASN A N   1 
ATOM   543  C CA  . ASN A 1 70  ? -5.04400  27.40300  -4.23800  1.000 49.91000 ? 72  ASN A CA  1 
ATOM   544  C C   . ASN A 1 70  ? -5.42000  28.63900  -5.05300  1.000 52.13000 ? 72  ASN A C   1 
ATOM   545  O O   . ASN A 1 70  ? -5.17100  29.75600  -4.58700  1.000 56.27000 ? 72  ASN A O   1 
ATOM   546  C CB  . ASN A 1 70  ? -3.51200  27.29800  -4.18200  1.000 52.13000 ? 72  ASN A CB  1 
ATOM   547  N N   . VAL A 1 71  ? -6.01000  28.49400  -6.24700  1.000 46.03000 ? 73  VAL A N   1 
ATOM   548  C CA  . VAL A 1 71  ? -6.21500  29.63800  -7.13500  1.000 47.64000 ? 73  VAL A CA  1 
ATOM   549  C C   . VAL A 1 71  ? -7.66700  30.08500  -7.06300  1.000 45.79000 ? 73  VAL A C   1 
ATOM   550  O O   . VAL A 1 71  ? -8.58400  29.25500  -7.04400  1.000 38.10000 ? 73  VAL A O   1 
ATOM   551  C CB  . VAL A 1 71  ? -5.80300  29.31800  -8.58700  1.000 48.34000 ? 73  VAL A CB  1 
ATOM   552  C CG1 . VAL A 1 71  ? -6.45100  28.05100  -9.06300  1.000 50.45000 ? 73  VAL A CG1 1 
ATOM   553  C CG2 . VAL A 1 71  ? -6.17100  30.46700  -9.51400  1.000 48.35000 ? 73  VAL A CG2 1 
ATOM   554  N N   . GLN A 1 72  ? -7.87300  31.40300  -7.00200  1.000 39.22000 ? 74  GLN A N   1 
ATOM   555  C CA  . GLN A 1 72  ? -9.20700  31.98100  -7.05400  1.000 40.68000 ? 74  GLN A CA  1 
ATOM   556  C C   . GLN A 1 72  ? -9.64900  32.09300  -8.50500  1.000 40.75000 ? 74  GLN A C   1 
ATOM   557  O O   . GLN A 1 72  ? -8.87400  32.51000  -9.36700  1.000 44.81000 ? 74  GLN A O   1 
ATOM   558  C CB  . GLN A 1 72  ? -9.22800  33.35700  -6.38200  1.000 38.71000 ? 74  GLN A CB  1 
ATOM   559  N N   . LEU A 1 73  ? -10.88400 31.70400  -8.77700  1.000 36.93000 ? 75  LEU A N   1 
ATOM   560  C CA  . LEU A 1 73  ? -11.45600 31.77800  -10.11300 1.000 36.14000 ? 75  LEU A CA  1 
ATOM   561  C C   . LEU A 1 73  ? -12.35100 33.00600  -10.16700 1.000 39.41000 ? 75  LEU A C   1 
ATOM   562  O O   . LEU A 1 73  ? -13.19500 33.20200  -9.28400  1.000 42.69000 ? 75  LEU A O   1 
ATOM   563  C CB  . LEU A 1 73  ? -12.26500 30.52000  -10.45200 1.000 36.35000 ? 75  LEU A CB  1 
ATOM   564  C CG  . LEU A 1 73  ? -11.56400 29.16100  -10.56100 1.000 33.01000 ? 75  LEU A CG  1 
ATOM   565  C CD1 . LEU A 1 73  ? -12.48500 28.15900  -11.24000 1.000 37.40000 ? 75  LEU A CD1 1 
ATOM   566  C CD2 . LEU A 1 73  ? -10.26700 29.27300  -11.33200 1.000 34.97000 ? 75  LEU A CD2 1 
ATOM   567  N N   . ARG A 1 74  ? -12.15700 33.83100  -11.19000 1.000 37.71000 ? 76  ARG A N   1 
ATOM   568  C CA  . ARG A 1 74  ? -12.91600 35.06900  -11.31200 1.000 38.65000 ? 76  ARG A CA  1 
ATOM   569  C C   . ARG A 1 74  ? -14.28200 34.77000  -11.91200 1.000 34.25000 ? 76  ARG A C   1 
ATOM   570  O O   . ARG A 1 74  ? -14.37500 34.29100  -13.04700 1.000 37.93000 ? 76  ARG A O   1 
ATOM   571  C CB  . ARG A 1 74  ? -12.15300 36.08100  -12.16800 1.000 42.88000 ? 76  ARG A CB  1 
ATOM   572  N N   . VAL A 1 75  ? -15.33500 35.05200  -11.15400 1.000 33.19000 ? 77  VAL A N   1 
ATOM   573  C CA  . VAL A 1 75  ? -16.70600 34.93700  -11.64300 1.000 35.95000 ? 77  VAL A CA  1 
ATOM   574  C C   . VAL A 1 75  ? -17.03900 36.14200  -12.52400 1.000 39.39000 ? 77  VAL A C   1 
ATOM   575  O O   . VAL A 1 75  ? -16.93200 37.29100  -12.08000 1.000 35.98000 ? 77  VAL A O   1 
ATOM   576  C CB  . VAL A 1 75  ? -17.69100 34.83200  -10.47100 1.000 37.26000 ? 77  VAL A CB  1 
ATOM   577  C CG1 . VAL A 1 75  ? -19.13200 34.84100  -10.98000 1.000 36.30000 ? 77  VAL A CG1 1 
ATOM   578  C CG2 . VAL A 1 75  ? -17.39500 33.58700  -9.63900  1.000 39.52000 ? 77  VAL A CG2 1 
ATOM   579  N N   . ILE A 1 76  ? -17.47700 35.88000  -13.75800 1.000 37.50000 ? 78  ILE A N   1 
ATOM   580  C CA  . ILE A 1 76  ? -17.83500 36.92900  -14.71100 1.000 38.24000 ? 78  ILE A CA  1 
ATOM   581  C C   . ILE A 1 76  ? -19.31500 36.91900  -15.06100 1.000 40.36000 ? 78  ILE A C   1 
ATOM   582  O O   . ILE A 1 76  ? -19.76500 37.80100  -15.80400 1.000 39.25000 ? 78  ILE A O   1 
ATOM   583  C CB  . ILE A 1 76  ? -16.99100 36.83700  -15.99800 1.000 42.88000 ? 78  ILE A CB  1 
ATOM   584  C CG1 . ILE A 1 76  ? -17.18400 35.45700  -16.64600 1.000 38.77000 ? 78  ILE A CG1 1 
ATOM   585  C CG2 . ILE A 1 76  ? -15.51400 37.12400  -15.69900 1.000 39.73000 ? 78  ILE A CG2 1 
ATOM   586  C CD1 . ILE A 1 76  ? -16.52500 35.31600  -18.00800 1.000 37.12000 ? 78  ILE A CD1 1 
ATOM   587  N N   . GLY A 1 77  ? -20.08300 35.95000  -14.56700 1.000 37.16000 ? 79  GLY A N   1 
ATOM   588  C CA  . GLY A 1 77  ? -21.51500 35.92200  -14.80500 1.000 38.85000 ? 79  GLY A CA  1 
ATOM   589  C C   . GLY A 1 77  ? -22.16500 34.83500  -13.97900 1.000 37.89000 ? 79  GLY A C   1 
ATOM   590  O O   . GLY A 1 77  ? -21.49400 33.92600  -13.48200 1.000 35.29000 ? 79  GLY A O   1 
ATOM   591  N N   . HIS A 1 78  ? -23.48300 34.94700  -13.81700 1.000 36.57000 ? 80  HIS A N   1 
ATOM   592  C CA  . HIS A 1 78  ? -24.19200 33.94500  -13.03300 1.000 35.86000 ? 80  HIS A CA  1 
ATOM   593  C C   . HIS A 1 78  ? -25.64500 33.88100  -13.47200 1.000 39.18000 ? 80  HIS A C   1 
ATOM   594  O O   . HIS A 1 78  ? -26.25500 34.90800  -13.80000 1.000 36.02000 ? 80  HIS A O   1 
ATOM   595  C CB  . HIS A 1 78  ? -24.11300 34.25200  -11.53200 1.000 35.46000 ? 80  HIS A CB  1 
ATOM   596  C CG  . HIS A 1 78  ? -24.68300 35.59100  -11.16400 1.000 37.95000 ? 80  HIS A CG  1 
ATOM   597  N ND1 . HIS A 1 78  ? -23.90600 36.72200  -11.05100 1.000 38.31000 ? 80  HIS A ND1 1 
ATOM   598  C CD2 . HIS A 1 78  ? -25.95100 35.97900  -10.87900 1.000 36.80000 ? 80  HIS A CD2 1 
ATOM   599  C CE1 . HIS A 1 78  ? -24.66800 37.75400  -10.72400 1.000 37.62000 ? 80  HIS A CE1 1 
ATOM   600  N NE2 . HIS A 1 78  ? -25.91100 37.32900  -10.60400 1.000 37.51000 ? 80  HIS A NE2 1 
ATOM   601  N N   . SER A 1 79  ? -26.19300 32.67000  -13.46400 1.000 34.35000 ? 81  SER A N   1 
ATOM   602  C CA  . SER A 1 79  ? -27.60900 32.46700  -13.72600 1.000 34.47000 ? 81  SER A CA  1 
ATOM   603  C C   . SER A 1 79  ? -28.07600 31.27100  -12.91600 1.000 33.95000 ? 81  SER A C   1 
ATOM   604  O O   . SER A 1 79  ? -27.27600 30.45600  -12.44300 1.000 33.76000 ? 81  SER A O   1 
ATOM   605  C CB  . SER A 1 79  ? -27.90100 32.24600  -15.21600 1.000 31.64000 ? 81  SER A CB  1 
ATOM   606  O OG  . SER A 1 79  ? -27.23200 31.09200  -15.70300 1.000 38.47000 ? 81  SER A OG  1 
ATOM   607  N N   . MET A 1 80  ? -29.38500 31.16900  -12.78000 1.000 28.88000 ? 82  MET A N   1 
ATOM   608  C CA  . MET A 1 80  ? -30.02300 30.09800  -12.03800 1.000 33.86000 ? 82  MET A CA  1 
ATOM   609  C C   . MET A 1 80  ? -30.75300 29.20300  -13.02400 1.000 32.08000 ? 82  MET A C   1 
ATOM   610  O O   . MET A 1 80  ? -31.45200 29.69900  -13.91000 1.000 35.84000 ? 82  MET A O   1 
ATOM   611  C CB  . MET A 1 80  ? -30.98400 30.68000  -11.00300 1.000 33.57000 ? 82  MET A CB  1 
ATOM   612  C CG  . MET A 1 80  ? -31.71700 29.66400  -10.17000 1.000 31.80000 ? 82  MET A CG  1 
ATOM   613  S SD  . MET A 1 80  ? -32.44100 30.44400  -8.71700  1.000 34.96000 ? 82  MET A SD  1 
ATOM   614  C CE  . MET A 1 80  ? -33.79100 31.39200  -9.46600  1.000 33.30000 ? 82  MET A CE  1 
ATOM   615  N N   . GLN A 1 81  ? -30.56600 27.89000  -12.90000 1.000 31.29000 ? 83  GLN A N   1 
ATOM   616  C CA  . GLN A 1 81  ? -31.34100 26.92600  -13.67500 1.000 29.81000 ? 83  GLN A CA  1 
ATOM   617  C C   . GLN A 1 81  ? -31.97400 25.95800  -12.68800 1.000 33.70000 ? 83  GLN A C   1 
ATOM   618  O O   . GLN A 1 81  ? -31.26800 25.14200  -12.07800 1.000 29.30000 ? 83  GLN A O   1 
ATOM   619  C CB  . GLN A 1 81  ? -30.49400 26.17800  -14.69800 1.000 30.55000 ? 83  GLN A CB  1 
ATOM   620  C CG  . GLN A 1 81  ? -31.30400 25.16900  -15.53700 1.000 29.69000 ? 83  GLN A CG  1 
ATOM   621  C CD  . GLN A 1 81  ? -30.42300 24.41600  -16.52100 1.000 31.43000 ? 83  GLN A CD  1 
ATOM   622  O OE1 . GLN A 1 81  ? -29.19500 24.45900  -16.42900 1.000 33.36000 ? 83  GLN A OE1 1 
ATOM   623  N NE2 . GLN A 1 81  ? -31.04100 23.74200  -17.47600 1.000 31.45000 ? 83  GLN A NE2 1 
ATOM   624  N N   . ASN A 1 82  ? -33.29700 26.07800  -12.52500 1.000 29.17000 ? 84  ASN A N   1 
ATOM   625  C CA  . ASN A 1 82  ? -34.02700 25.37400  -11.48300 1.000 29.24000 ? 84  ASN A CA  1 
ATOM   626  C C   . ASN A 1 82  ? -33.29600 25.56000  -10.15600 1.000 29.79000 ? 84  ASN A C   1 
ATOM   627  O O   . ASN A 1 82  ? -33.14400 26.69700  -9.70000  1.000 29.29000 ? 84  ASN A O   1 
ATOM   628  C CB  . ASN A 1 82  ? -34.20600 23.90300  -11.89000 1.000 25.64000 ? 84  ASN A CB  1 
ATOM   629  C CG  . ASN A 1 82  ? -34.86800 23.78000  -13.26200 1.000 28.84000 ? 84  ASN A CG  1 
ATOM   630  O OD1 . ASN A 1 82  ? -35.99800 24.21400  -13.45000 1.000 31.68000 ? 84  ASN A OD1 1 
ATOM   631  N ND2 . ASN A 1 82  ? -34.15300 23.23700  -14.22500 1.000 30.43000 ? 84  ASN A ND2 1 
ATOM   632  N N   . CYS A 1 83  ? -32.78600 24.48300  -9.55100  1.000 29.16000 ? 85  CYS A N   1 
ATOM   633  C CA  . CYS A 1 83  ? -32.17800 24.59900  -8.23000  1.000 27.20000 ? 85  CYS A CA  1 
ATOM   634  C C   . CYS A 1 83  ? -30.65500 24.59100  -8.25700  1.000 26.62000 ? 85  CYS A C   1 
ATOM   635  O O   . CYS A 1 83  ? -30.02900 24.46100  -7.19800  1.000 24.22000 ? 85  CYS A O   1 
ATOM   636  C CB  . CYS A 1 83  ? -32.67100 23.49100  -7.30800  1.000 25.68000 ? 85  CYS A CB  1 
ATOM   637  S SG  . CYS A 1 83  ? -34.41800 23.53900  -6.93600  1.000 28.71000 ? 85  CYS A SG  1 
ATOM   638  N N   . VAL A 1 84  ? -30.03100 24.75500  -9.41800  1.000 25.66000 ? 86  VAL A N   1 
ATOM   639  C CA  . VAL A 1 84  ? -28.58300 24.87200  -9.46200  1.000 26.61000 ? 86  VAL A CA  1 
ATOM   640  C C   . VAL A 1 84  ? -28.19900 26.27500  -9.90800  1.000 28.91000 ? 86  VAL A C   1 
ATOM   641  O O   . VAL A 1 84  ? -28.87500 26.91200  -10.72700 1.000 27.36000 ? 86  VAL A O   1 
ATOM   642  C CB  . VAL A 1 84  ? -27.90500 23.79600  -10.34000 1.000 31.70000 ? 86  VAL A CB  1 
ATOM   643  C CG1 . VAL A 1 84  ? -28.12900 22.39300  -9.71800  1.000 28.14000 ? 86  VAL A CG1 1 
ATOM   644  C CG2 . VAL A 1 84  ? -28.38800 23.85100  -11.77200 1.000 31.73000 ? 86  VAL A CG2 1 
ATOM   645  N N   . LEU A 1 85  ? -27.13900 26.76700  -9.30700  1.000 28.95000 ? 87  LEU A N   1 
ATOM   646  C CA  . LEU A 1 85  ? -26.53500 28.02300  -9.69200  1.000 27.10000 ? 87  LEU A CA  1 
ATOM   647  C C   . LEU A 1 85  ? -25.42900 27.71300  -10.68300 1.000 32.68000 ? 87  LEU A C   1 
ATOM   648  O O   . LEU A 1 85  ? -24.69600 26.72400  -10.52000 1.000 28.87000 ? 87  LEU A O   1 
ATOM   649  C CB  . LEU A 1 85  ? -25.99300 28.71700  -8.45300  1.000 27.55000 ? 87  LEU A CB  1 
ATOM   650  C CG  . LEU A 1 85  ? -25.38500 30.10300  -8.58100  1.000 34.07000 ? 87  LEU A CG  1 
ATOM   651  C CD1 . LEU A 1 85  ? -26.42600 31.11900  -9.06600  1.000 34.89000 ? 87  LEU A CD1 1 
ATOM   652  C CD2 . LEU A 1 85  ? -24.84000 30.48800  -7.22000  1.000 35.70000 ? 87  LEU A CD2 1 
ATOM   653  N N   . LYS A 1 86  ? -25.36000 28.50500  -11.74900 1.000 28.91000 ? 88  LYS A N   1 
ATOM   654  C CA  . LYS A 1 86  ? -24.32300 28.35100  -12.76600 1.000 29.95000 ? 88  LYS A CA  1 
ATOM   655  C C   . LYS A 1 86  ? -23.46900 29.61200  -12.77600 1.000 34.07000 ? 88  LYS A C   1 
ATOM   656  O O   . LYS A 1 86  ? -23.94200 30.68400  -13.17100 1.000 32.64000 ? 88  LYS A O   1 
ATOM   657  C CB  . LYS A 1 86  ? -24.93800 28.08800  -14.13700 1.000 30.88000 ? 88  LYS A CB  1 
ATOM   658  C CG  . LYS A 1 86  ? -25.42900 26.66600  -14.32500 1.000 35.06000 ? 88  LYS A CG  1 
ATOM   659  C CD  . LYS A 1 86  ? -26.67500 26.59700  -15.17500 1.000 36.21000 ? 88  LYS A CD  1 
ATOM   660  C CE  . LYS A 1 86  ? -26.41300 26.95600  -16.62200 1.000 40.71000 ? 88  LYS A CE  1 
ATOM   661  N NZ  . LYS A 1 86  ? -27.67600 26.84400  -17.42300 1.000 40.61000 ? 88  LYS A NZ  1 
ATOM   662  N N   . LEU A 1 87  ? -22.22400 29.49400  -12.31300 1.000 32.92000 ? 89  LEU A N   1 
ATOM   663  C CA  . LEU A 1 87  ? -21.29300 30.61200  -12.25100 1.000 33.16000 ? 89  LEU A CA  1 
ATOM   664  C C   . LEU A 1 87  ? -20.35300 30.53900  -13.45000 1.000 35.24000 ? 89  LEU A C   1 
ATOM   665  O O   . LEU A 1 87  ? -19.57900 29.58800  -13.57400 1.000 31.69000 ? 89  LEU A O   1 
ATOM   666  C CB  . LEU A 1 87  ? -20.50600 30.59200  -10.93900 1.000 32.21000 ? 89  LEU A CB  1 
ATOM   667  C CG  . LEU A 1 87  ? -21.31800 30.57100  -9.64300  1.000 32.33000 ? 89  LEU A CG  1 
ATOM   668  C CD1 . LEU A 1 87  ? -20.41500 30.53400  -8.41900  1.000 30.85000 ? 89  LEU A CD1 1 
ATOM   669  C CD2 . LEU A 1 87  ? -22.23500 31.80000  -9.57500  1.000 36.84000 ? 89  LEU A CD2 1 
ATOM   670  N N   . LYS A 1 88  ? -20.43500 31.52700  -14.34200 1.000 36.56000 ? 90  LYS A N   1 
ATOM   671  C CA  . LYS A 1 88  ? -19.46500 31.62800  -15.42700 1.000 38.06000 ? 90  LYS A CA  1 
ATOM   672  C C   . LYS A 1 88  ? -18.15900 32.16900  -14.86600 1.000 35.15000 ? 90  LYS A C   1 
ATOM   673  O O   . LYS A 1 88  ? -18.16600 33.14000  -14.10600 1.000 35.48000 ? 90  LYS A O   1 
ATOM   674  C CB  . LYS A 1 88  ? -19.97600 32.53900  -16.54500 1.000 41.33000 ? 90  LYS A CB  1 
ATOM   675  C CG  . LYS A 1 88  ? -19.09200 32.52900  -17.78900 1.000 39.92000 ? 90  LYS A CG  1 
ATOM   676  C CD  . LYS A 1 88  ? -19.88700 32.83000  -19.05700 1.000 49.99000 ? 90  LYS A CD  1 
ATOM   677  C CE  . LYS A 1 88  ? -21.10100 31.90700  -19.20800 1.000 48.23000 ? 90  LYS A CE  1 
ATOM   678  N NZ  . LYS A 1 88  ? -20.72700 30.49800  -19.55100 1.000 55.98000 ? 90  LYS A NZ  1 
ATOM   679  N N   . VAL A 1 89  ? -17.04000 31.53100  -15.21700 1.000 36.67000 ? 91  VAL A N   1 
ATOM   680  C CA  . VAL A 1 89  ? -15.75200 31.94700  -14.68100 1.000 36.11000 ? 91  VAL A CA  1 
ATOM   681  C C   . VAL A 1 89  ? -14.80000 32.33700  -15.80300 1.000 38.06000 ? 91  VAL A C   1 
ATOM   682  O O   . VAL A 1 89  ? -15.01600 32.04400  -16.98100 1.000 37.11000 ? 91  VAL A O   1 
ATOM   683  C CB  . VAL A 1 89  ? -15.09500 30.88100  -13.77000 1.000 37.05000 ? 91  VAL A CB  1 
ATOM   684  C CG1 . VAL A 1 89  ? -15.85600 30.77800  -12.43000 1.000 35.12000 ? 91  VAL A CG1 1 
ATOM   685  C CG2 . VAL A 1 89  ? -14.98500 29.52100  -14.48100 1.000 34.67000 ? 91  VAL A CG2 1 
ATOM   686  N N   . ASP A 1 90  ? -13.72500 33.01500  -15.37900 1.000 39.88000 ? 92  ASP A N   1 
ATOM   687  C CA  . ASP A 1 90  ? -12.68500 33.57200  -16.24900 1.000 47.42000 ? 92  ASP A CA  1 
ATOM   688  C C   . ASP A 1 90  ? -12.04000 32.52500  -17.14200 1.000 46.61000 ? 92  ASP A C   1 
ATOM   689  O O   . ASP A 1 90  ? -11.65100 32.82000  -18.28100 1.000 45.63000 ? 92  ASP A O   1 
ATOM   690  C CB  . ASP A 1 90  ? -11.59800 34.19900  -15.37100 1.000 47.86000 ? 92  ASP A CB  1 
ATOM   691  C CG  . ASP A 1 90  ? -11.07200 35.48400  -15.92500 1.000 55.60000 ? 92  ASP A CG  1 
ATOM   692  O OD1 . ASP A 1 90  ? -11.38800 35.79200  -17.09300 1.000 61.21000 ? 92  ASP A OD1 1 
ATOM   693  O OD2 . ASP A 1 90  ? -10.33900 36.18300  -15.19300 1.000 64.64000 ? 92  ASP A OD2 1 
ATOM   694  N N   . THR A 1 91  ? -11.87500 31.31200  -16.62200 1.000 40.91000 ? 93  THR A N   1 
ATOM   695  C CA  . THR A 1 91  ? -10.97700 30.30700  -17.17000 1.000 36.54000 ? 93  THR A CA  1 
ATOM   696  C C   . THR A 1 91  ? -11.75100 29.01600  -17.37700 1.000 39.85000 ? 93  THR A C   1 
ATOM   697  O O   . THR A 1 91  ? -12.51200 28.60000  -16.50100 1.000 38.43000 ? 93  THR A O   1 
ATOM   698  C CB  . THR A 1 91  ? -9.79900  30.05900  -16.21400 1.000 39.53000 ? 93  THR A CB  1 
ATOM   699  O OG1 . THR A 1 91  ? -9.22600  31.31000  -15.82100 1.000 44.78000 ? 93  THR A OG1 1 
ATOM   700  C CG2 . THR A 1 91  ? -8.72300  29.18100  -16.86200 1.000 39.53000 ? 93  THR A CG2 1 
ATOM   701  N N   . ALA A 1 92  ? -11.57300 28.39800  -18.53700 1.000 38.63000 ? 94  ALA A N   1 
ATOM   702  C CA  . ALA A 1 92  ? -12.09700 27.06200  -18.74700 1.000 37.31000 ? 94  ALA A CA  1 
ATOM   703  C C   . ALA A 1 92  ? -11.22800 26.06700  -17.98600 1.000 37.53000 ? 94  ALA A C   1 
ATOM   704  O O   . ALA A 1 92  ? -10.00800 26.23300  -17.90000 1.000 35.16000 ? 94  ALA A O   1 
ATOM   705  C CB  . ALA A 1 92  ? -12.12200 26.72700  -20.23800 1.000 39.44000 ? 94  ALA A CB  1 
ATOM   706  N N   . ASN A 1 93  ? -11.86300 25.05800  -17.39400 1.000 35.14000 ? 95  ASN A N   1 
ATOM   707  C CA  . ASN A 1 93  ? -11.12500 24.06100  -16.62200 1.000 32.54000 ? 95  ASN A CA  1 
ATOM   708  C C   . ASN A 1 93  ? -10.26700 23.25700  -17.58700 1.000 32.25000 ? 95  ASN A C   1 
ATOM   709  O O   . ASN A 1 93  ? -10.81200 22.62700  -18.49700 1.000 34.41000 ? 95  ASN A O   1 
ATOM   710  C CB  . ASN A 1 93  ? -12.08500 23.13500  -15.85100 1.000 35.68000 ? 95  ASN A CB  1 
ATOM   711  C CG  . ASN A 1 93  ? -11.35300 22.13800  -14.93000 1.000 36.71000 ? 95  ASN A CG  1 
ATOM   712  O OD1 . ASN A 1 93  ? -10.12700 22.16100  -14.79800 1.000 36.46000 ? 95  ASN A OD1 1 
ATOM   713  N ND2 . ASN A 1 93  ? -12.12100 21.26800  -14.28400 1.000 33.80000 ? 95  ASN A ND2 1 
ATOM   714  N N   . PRO A 1 94  ? -8.94000  23.28000  -17.45700 1.000 33.79000 ? 96  PRO A N   1 
ATOM   715  C CA  . PRO A 1 94  ? -8.11500  22.45500  -18.35600 1.000 35.46000 ? 96  PRO A CA  1 
ATOM   716  C C   . PRO A 1 94  ? -8.29900  20.96400  -18.12800 1.000 37.83000 ? 96  PRO A C   1 
ATOM   717  O O   . PRO A 1 94  ? -8.08000  20.17600  -19.05700 1.000 36.97000 ? 96  PRO A O   1 
ATOM   718  C CB  . PRO A 1 94  ? -6.68500  22.90300  -18.02800 1.000 34.99000 ? 96  PRO A CB  1 
ATOM   719  C CG  . PRO A 1 94  ? -6.75500  23.37600  -16.62000 1.000 37.99000 ? 96  PRO A CG  1 
ATOM   720  C CD  . PRO A 1 94  ? -8.13400  23.96900  -16.43600 1.000 35.84000 ? 96  PRO A CD  1 
ATOM   721  N N   . LYS A 1 95  ? -8.73800  20.55500  -16.93900 1.000 37.47000 ? 97  LYS A N   1 
ATOM   722  C CA  . LYS A 1 95  ? -8.95800  19.14900  -16.63800 1.000 35.69000 ? 97  LYS A CA  1 
ATOM   723  C C   . LYS A 1 95  ? -10.36900 18.68400  -16.97500 1.000 39.92000 ? 97  LYS A C   1 
ATOM   724  O O   . LYS A 1 95  ? -10.75900 17.58600  -16.55400 1.000 36.46000 ? 97  LYS A O   1 
ATOM   725  C CB  . LYS A 1 95  ? -8.65700  18.87900  -15.15900 1.000 38.34000 ? 97  LYS A CB  1 
ATOM   726  C CG  . LYS A 1 95  ? -7.20100  19.10700  -14.77800 1.000 38.95000 ? 97  LYS A CG  1 
ATOM   727  C CD  . LYS A 1 95  ? -7.02700  19.11100  -13.27000 1.000 43.08000 ? 97  LYS A CD  1 
ATOM   728  C CE  . LYS A 1 95  ? -5.55600  19.08600  -12.88200 1.000 54.14000 ? 97  LYS A CE  1 
ATOM   729  N NZ  . LYS A 1 95  ? -5.33900  19.60100  -11.50200 1.000 55.55000 ? 97  LYS A NZ  1 
ATOM   730  N N   . THR A 1 96  ? -11.13900 19.48000  -17.72700 1.000 36.60000 ? 98  THR A N   1 
ATOM   731  C CA  . THR A 1 96  ? -12.49700 19.08200  -18.06900 1.000 34.37000 ? 98  THR A CA  1 
ATOM   732  C C   . THR A 1 96  ? -12.48100 17.74900  -18.81200 1.000 36.15000 ? 98  THR A C   1 
ATOM   733  O O   . THR A 1 96  ? -11.84600 17.64600  -19.87000 1.000 35.90000 ? 98  THR A O   1 
ATOM   734  C CB  . THR A 1 96  ? -13.20600 20.14600  -18.91700 1.000 35.44000 ? 98  THR A CB  1 
ATOM   735  O OG1 . THR A 1 96  ? -13.31400 21.37000  -18.17800 1.000 35.66000 ? 98  THR A OG1 1 
ATOM   736  C CG2 . THR A 1 96  ? -14.61200 19.68000  -19.29400 1.000 35.16000 ? 98  THR A CG2 1 
ATOM   737  N N   . PRO A 1 97  ? -13.14400 16.71600  -18.30300 1.000 35.30000 ? 99  PRO A N   1 
ATOM   738  C CA  . PRO A 1 97  ? -13.25000 15.45800  -19.04400 1.000 35.30000 ? 99  PRO A CA  1 
ATOM   739  C C   . PRO A 1 97  ? -14.37600 15.51000  -20.06900 1.000 37.01000 ? 99  PRO A C   1 
ATOM   740  O O   . PRO A 1 97  ? -15.22800 16.39800  -20.06900 1.000 37.22000 ? 99  PRO A O   1 
ATOM   741  C CB  . PRO A 1 97  ? -13.56300 14.43700  -17.94500 1.000 35.46000 ? 99  PRO A CB  1 
ATOM   742  C CG  . PRO A 1 97  ? -14.37300 15.23500  -16.95900 1.000 34.57000 ? 99  PRO A CG  1 
ATOM   743  C CD  . PRO A 1 97  ? -13.77300 16.63000  -16.97300 1.000 34.64000 ? 99  PRO A CD  1 
ATOM   744  N N   . LYS A 1 98  ? -14.36400 14.53100  -20.96400 1.000 35.75000 ? 100 LYS A N   1 
ATOM   745  C CA  . LYS A 1 98  ? -15.56000 14.27000  -21.74000 1.000 37.01000 ? 100 LYS A CA  1 
ATOM   746  C C   . LYS A 1 98  ? -16.68600 13.97100  -20.76000 1.000 38.01000 ? 100 LYS A C   1 
ATOM   747  O O   . LYS A 1 98  ? -16.51400 13.17700  -19.83000 1.000 35.64000 ? 100 LYS A O   1 
ATOM   748  C CB  . LYS A 1 98  ? -15.33000 13.09700  -22.69600 1.000 39.12000 ? 100 LYS A CB  1 
ATOM   749  N N   . TYR A 1 99  ? -17.81600 14.65600  -20.91500 1.000 34.22000 ? 101 TYR A N   1 
ATOM   750  C CA  . TYR A 1 99  ? -18.89500 14.48500  -19.95400 1.000 36.14000 ? 101 TYR A CA  1 
ATOM   751  C C   . TYR A 1 99  ? -20.24200 14.62100  -20.64500 1.000 38.49000 ? 101 TYR A C   1 
ATOM   752  O O   . TYR A 1 99  ? -20.34000 15.05000  -21.79600 1.000 39.20000 ? 101 TYR A O   1 
ATOM   753  C CB  . TYR A 1 99  ? -18.79600 15.47900  -18.79500 1.000 33.21000 ? 101 TYR A CB  1 
ATOM   754  C CG  . TYR A 1 99  ? -19.16300 16.90900  -19.15500 1.000 34.61000 ? 101 TYR A CG  1 
ATOM   755  C CD1 . TYR A 1 99  ? -18.21900 17.76400  -19.71800 1.000 36.60000 ? 101 TYR A CD1 1 
ATOM   756  C CD2 . TYR A 1 99  ? -20.44100 17.40300  -18.93000 1.000 34.78000 ? 101 TYR A CD2 1 
ATOM   757  C CE1 . TYR A 1 99  ? -18.53500 19.07500  -20.05200 1.000 37.12000 ? 101 TYR A CE1 1 
ATOM   758  C CE2 . TYR A 1 99  ? -20.77200 18.72200  -19.27400 1.000 34.62000 ? 101 TYR A CE2 1 
ATOM   759  C CZ  . TYR A 1 99  ? -19.81100 19.54100  -19.83300 1.000 35.78000 ? 101 TYR A CZ  1 
ATOM   760  O OH  . TYR A 1 99  ? -20.10900 20.83700  -20.16300 1.000 45.30000 ? 101 TYR A OH  1 
ATOM   761  N N   . LYS A 1 100 ? -21.27700 14.21100  -19.91200 1.000 39.25000 ? 102 LYS A N   1 
ATOM   762  C CA  . LYS A 1 100 ? -22.67500 14.40300  -20.25100 1.000 36.44000 ? 102 LYS A CA  1 
ATOM   763  C C   . LYS A 1 100 ? -23.42700 14.61500  -18.94600 1.000 37.04000 ? 102 LYS A C   1 
ATOM   764  O O   . LYS A 1 100 ? -22.95000 14.24400  -17.86800 1.000 34.54000 ? 102 LYS A O   1 
ATOM   765  C CB  . LYS A 1 100 ? -23.27500 13.19800  -21.00200 1.000 41.42000 ? 102 LYS A CB  1 
ATOM   766  C CG  . LYS A 1 100 ? -22.62800 12.84800  -22.33600 1.000 48.76000 ? 102 LYS A CG  1 
ATOM   767  C CD  . LYS A 1 100 ? -22.92000 11.37700  -22.72400 1.000 52.38000 ? 102 LYS A CD  1 
ATOM   768  C CE  . LYS A 1 100 ? -22.09100 10.92400  -23.93600 1.000 54.76000 ? 102 LYS A CE  1 
ATOM   769  N NZ  . LYS A 1 100 ? -20.99300 11.89800  -24.27500 1.000 56.79000 ? 102 LYS A NZ  1 
ATOM   770  N N   . PHE A 1 101 ? -24.61500 15.20600  -19.05800 1.000 34.21000 ? 103 PHE A N   1 
ATOM   771  C CA  . PHE A 1 101 ? -25.55700 15.36000  -17.95700 1.000 32.01000 ? 103 PHE A CA  1 
ATOM   772  C C   . PHE A 1 101 ? -26.71300 14.41100  -18.22600 1.000 32.29000 ? 103 PHE A C   1 
ATOM   773  O O   . PHE A 1 101 ? -27.35300 14.49900  -19.27700 1.000 36.38000 ? 103 PHE A O   1 
ATOM   774  C CB  . PHE A 1 101 ? -26.08900 16.79000  -17.85600 1.000 30.92000 ? 103 PHE A CB  1 
ATOM   775  C CG  . PHE A 1 101 ? -25.09900 17.80400  -17.34300 1.000 31.60000 ? 103 PHE A CG  1 
ATOM   776  C CD1 . PHE A 1 101 ? -23.87500 17.42600  -16.80600 1.000 31.88000 ? 103 PHE A CD1 1 
ATOM   777  C CD2 . PHE A 1 101 ? -25.41300 19.16100  -17.39400 1.000 33.28000 ? 103 PHE A CD2 1 
ATOM   778  C CE1 . PHE A 1 101 ? -22.98800 18.38000  -16.34300 1.000 29.45000 ? 103 PHE A CE1 1 
ATOM   779  C CE2 . PHE A 1 101 ? -24.52800 20.11500  -16.93600 1.000 32.07000 ? 103 PHE A CE2 1 
ATOM   780  C CZ  . PHE A 1 101 ? -23.30900 19.72400  -16.41100 1.000 32.01000 ? 103 PHE A CZ  1 
ATOM   781  N N   . VAL A 1 102 ? -26.98000 13.51000  -17.28800 1.000 28.04000 ? 104 VAL A N   1 
ATOM   782  C CA  . VAL A 1 102 ? -27.99800 12.48400  -17.45000 1.000 32.27000 ? 104 VAL A CA  1 
ATOM   783  C C   . VAL A 1 102 ? -28.90100 12.53300  -16.22700 1.000 30.40000 ? 104 VAL A C   1 
ATOM   784  O O   . VAL A 1 102 ? -28.42500 12.77000  -15.11600 1.000 32.32000 ? 104 VAL A O   1 
ATOM   785  C CB  . VAL A 1 102 ? -27.34200 11.09000  -17.60800 1.000 34.13000 ? 104 VAL A CB  1 
ATOM   786  C CG1 . VAL A 1 102 ? -28.38100 9.98600   -17.73600 1.000 40.45000 ? 104 VAL A CG1 1 
ATOM   787  C CG2 . VAL A 1 102 ? -26.39000 11.09800  -18.79800 1.000 37.87000 ? 104 VAL A CG2 1 
ATOM   788  N N   . ARG A 1 103 ? -30.20000 12.32400  -16.42500 1.000 30.37000 ? 105 ARG A N   1 
ATOM   789  C CA  . ARG A 1 103 ? -31.13300 12.12500  -15.32300 1.000 29.04000 ? 105 ARG A CA  1 
ATOM   790  C C   . ARG A 1 103 ? -31.43300 10.63900  -15.21700 1.000 31.73000 ? 105 ARG A C   1 
ATOM   791  O O   . ARG A 1 103 ? -31.77300 10.00600  -16.21900 1.000 32.49000 ? 105 ARG A O   1 
ATOM   792  C CB  . ARG A 1 103 ? -32.42700 12.91600  -15.53100 1.000 29.75000 ? 105 ARG A CB  1 
ATOM   793  C CG  . ARG A 1 103 ? -33.42600 12.74700  -14.39500 1.000 31.44000 ? 105 ARG A CG  1 
ATOM   794  C CD  . ARG A 1 103 ? -34.48100 13.84800  -14.38200 1.000 32.62000 ? 105 ARG A CD  1 
ATOM   795  N NE  . ARG A 1 103 ? -35.44400 13.62900  -13.29900 1.000 31.94000 ? 105 ARG A NE  1 
ATOM   796  C CZ  . ARG A 1 103 ? -35.44900 14.29600  -12.14500 1.000 30.97000 ? 105 ARG A CZ  1 
ATOM   797  N NH1 . ARG A 1 103 ? -34.53800 15.24100  -11.90100 1.000 30.06000 ? 105 ARG A NH1 1 
ATOM   798  N NH2 . ARG A 1 103 ? -36.36700 14.01600  -11.23400 1.000 29.98000 ? 105 ARG A NH2 1 
ATOM   799  N N   . ILE A 1 104 ? -31.28900 10.08000  -14.02100 1.000 31.83000 ? 106 ILE A N   1 
ATOM   800  C CA  . ILE A 1 104 ? -31.41900 8.63800   -13.82900 1.000 33.49000 ? 106 ILE A CA  1 
ATOM   801  C C   . ILE A 1 104 ? -32.75000 8.32700   -13.16400 1.000 35.09000 ? 106 ILE A C   1 
ATOM   802  O O   . ILE A 1 104 ? -33.40800 9.19100   -12.58100 1.000 29.82000 ? 106 ILE A O   1 
ATOM   803  C CB  . ILE A 1 104 ? -30.26100 8.06900   -12.99100 1.000 34.61000 ? 106 ILE A CB  1 
ATOM   804  C CG1 . ILE A 1 104 ? -30.17700 8.82900   -11.66200 1.000 29.79000 ? 106 ILE A CG1 1 
ATOM   805  C CG2 . ILE A 1 104 ? -28.96300 8.16200   -13.76600 1.000 32.66000 ? 106 ILE A CG2 1 
ATOM   806  C CD1 . ILE A 1 104 ? -29.46500 8.10100   -10.56600 1.000 31.75000 ? 106 ILE A CD1 1 
ATOM   807  N N   . GLN A 1 105 ? -33.14500 7.06200   -13.24000 1.000 32.12000 ? 107 GLN A N   1 
ATOM   808  C CA  . GLN A 1 105 ? -34.37500 6.57900   -12.63600 1.000 36.52000 ? 107 GLN A CA  1 
ATOM   809  C C   . GLN A 1 105 ? -34.08100 5.78100   -11.37500 1.000 32.15000 ? 107 GLN A C   1 
ATOM   810  O O   . GLN A 1 105 ? -32.96500 5.26700   -11.19600 1.000 31.41000 ? 107 GLN A O   1 
ATOM   811  C CB  . GLN A 1 105 ? -35.16400 5.71200   -13.63700 1.000 38.99000 ? 107 GLN A CB  1 
ATOM   812  C CG  . GLN A 1 105 ? -35.65900 6.49000   -14.86600 1.000 41.64000 ? 107 GLN A CG  1 
ATOM   813  C CD  . GLN A 1 105 ? -36.52900 7.68400   -14.50300 1.000 44.77000 ? 107 GLN A CD  1 
ATOM   814  O OE1 . GLN A 1 105 ? -37.52100 7.53900   -13.78800 1.000 46.80000 ? 107 GLN A OE1 1 
ATOM   815  N NE2 . GLN A 1 105 ? -36.16800 8.87500   -15.00500 1.000 42.65000 ? 107 GLN A NE2 1 
ATOM   816  N N   . PRO A 1 106 ? -35.03800 5.69000   -10.45100 1.000 32.58000 ? 108 PRO A N   1 
ATOM   817  C CA  . PRO A 1 106 ? -34.89400 4.81300   -9.28400  1.000 33.12000 ? 108 PRO A CA  1 
ATOM   818  C C   . PRO A 1 106 ? -34.37100 3.43500   -9.65800  1.000 33.22000 ? 108 PRO A C   1 
ATOM   819  O O   . PRO A 1 106 ? -34.79900 2.83800   -10.64500 1.000 30.61000 ? 108 PRO A O   1 
ATOM   820  C CB  . PRO A 1 106 ? -36.32100 4.72200   -8.73200  1.000 33.34000 ? 108 PRO A CB  1 
ATOM   821  C CG  . PRO A 1 106 ? -36.93200 6.00000   -9.12600  1.000 32.63000 ? 108 PRO A CG  1 
ATOM   822  C CD  . PRO A 1 106 ? -36.31200 6.43700   -10.42000 1.000 33.26000 ? 108 PRO A CD  1 
ATOM   823  N N   . GLY A 1 107 ? -33.42800 2.94000   -8.85800  1.000 31.63000 ? 109 GLY A N   1 
ATOM   824  C CA  . GLY A 1 107 ? -32.80000 1.66000   -9.08900  1.000 33.43000 ? 109 GLY A CA  1 
ATOM   825  C C   . GLY A 1 107 ? -31.44900 1.75400   -9.76000  1.000 32.57000 ? 109 GLY A C   1 
ATOM   826  O O   . GLY A 1 107 ? -30.66900 0.79500   -9.70600  1.000 31.30000 ? 109 GLY A O   1 
ATOM   827  N N   . GLN A 1 108 ? -31.15900 2.88400   -10.39200 1.000 28.17000 ? 110 GLN A N   1 
ATOM   828  C CA  . GLN A 1 108 ? -29.88200 3.06700   -11.06300 1.000 27.33000 ? 110 GLN A CA  1 
ATOM   829  C C   . GLN A 1 108 ? -28.78800 3.30400   -10.02700 1.000 28.20000 ? 110 GLN A C   1 
ATOM   830  O O   . GLN A 1 108 ? -29.03100 3.87100   -8.95900  1.000 29.38000 ? 110 GLN A O   1 
ATOM   831  C CB  . GLN A 1 108 ? -29.98200 4.23700   -12.04300 1.000 34.26000 ? 110 GLN A CB  1 
ATOM   832  C CG  . GLN A 1 108 ? -28.77000 4.46600   -12.90400 1.000 32.43000 ? 110 GLN A CG  1 
ATOM   833  C CD  . GLN A 1 108 ? -28.45600 3.28400   -13.78600 1.000 40.90000 ? 110 GLN A CD  1 
ATOM   834  O OE1 . GLN A 1 108 ? -27.64100 2.42200   -13.42600 1.000 33.81000 ? 110 GLN A OE1 1 
ATOM   835  N NE2 . GLN A 1 108 ? -29.09100 3.23800   -14.95600 1.000 41.47000 ? 110 GLN A NE2 1 
ATOM   836  N N   . THR A 1 109 ? -27.58700 2.81200   -10.32200 1.000 30.64000 ? 111 THR A N   1 
ATOM   837  C CA  . THR A 1 109 ? -26.44000 3.03100   -9.45200  1.000 30.77000 ? 111 THR A CA  1 
ATOM   838  C C   . THR A 1 109 ? -25.51000 4.10400   -10.01100 1.000 27.19000 ? 111 THR A C   1 
ATOM   839  O O   . THR A 1 109 ? -25.54100 4.44700   -11.19500 1.000 26.94000 ? 111 THR A O   1 
ATOM   840  C CB  . THR A 1 109 ? -25.64600 1.73100   -9.23300  1.000 28.89000 ? 111 THR A CB  1 
ATOM   841  O OG1 . THR A 1 109 ? -25.35200 1.13200   -10.49700 1.000 26.90000 ? 111 THR A OG1 1 
ATOM   842  C CG2 . THR A 1 109 ? -26.45600 0.78800   -8.38200  1.000 29.27000 ? 111 THR A CG2 1 
ATOM   843  N N   . PHE A 1 110 ? -24.65600 4.61600   -9.13700  1.000 27.53000 ? 112 PHE A N   1 
ATOM   844  C CA  . PHE A 1 110 ? -23.63800 5.57200   -9.55100  1.000 27.62000 ? 112 PHE A CA  1 
ATOM   845  C C   . PHE A 1 110 ? -22.61500 5.69400   -8.43200  1.000 27.42000 ? 112 PHE A C   1 
ATOM   846  O O   . PHE A 1 110 ? -22.83900 5.25500   -7.29900  1.000 28.86000 ? 112 PHE A O   1 
ATOM   847  C CB  . PHE A 1 110 ? -24.23900 6.94400   -9.88400  1.000 27.13000 ? 112 PHE A CB  1 
ATOM   848  C CG  . PHE A 1 110 ? -25.10700 7.49900   -8.79600  1.000 28.43000 ? 112 PHE A CG  1 
ATOM   849  C CD1 . PHE A 1 110 ? -26.43500 7.09000   -8.66200  1.000 27.28000 ? 112 PHE A CD1 1 
ATOM   850  C CD2 . PHE A 1 110 ? -24.60000 8.42100   -7.90000  1.000 29.21000 ? 112 PHE A CD2 1 
ATOM   851  C CE1 . PHE A 1 110 ? -27.24000 7.60500   -7.66100  1.000 31.40000 ? 112 PHE A CE1 1 
ATOM   852  C CE2 . PHE A 1 110 ? -25.40600 8.95400   -6.89400  1.000 32.01000 ? 112 PHE A CE2 1 
ATOM   853  C CZ  . PHE A 1 110 ? -26.73100 8.55400   -6.78000  1.000 32.13000 ? 112 PHE A CZ  1 
ATOM   854  N N   . SER A 1 111 ? -21.49200 6.30800   -8.77000  1.000 26.48000 ? 113 SER A N   1 
ATOM   855  C CA  . SER A 1 111 ? -20.44900 6.59500   -7.80100  1.000 27.58000 ? 113 SER A CA  1 
ATOM   856  C C   . SER A 1 111 ? -20.62600 8.00600   -7.26400  1.000 26.38000 ? 113 SER A C   1 
ATOM   857  O O   . SER A 1 111 ? -21.02100 8.91100   -7.99600  1.000 24.53000 ? 113 SER A O   1 
ATOM   858  C CB  . SER A 1 111 ? -19.06800 6.44700   -8.44700  1.000 28.77000 ? 113 SER A CB  1 
ATOM   859  O OG  . SER A 1 111 ? -18.85900 5.08600   -8.78200  1.000 27.82000 ? 113 SER A OG  1 
ATOM   860  N N   . VAL A 1 112 ? -20.30500 8.19500   -5.99100  1.000 25.28000 ? 114 VAL A N   1 
ATOM   861  C CA  . VAL A 1 112 ? -20.31300 9.51100   -5.36800  1.000 26.00000 ? 114 VAL A CA  1 
ATOM   862  C C   . VAL A 1 112 ? -18.89300 9.84300   -4.93800  1.000 27.45000 ? 114 VAL A C   1 
ATOM   863  O O   . VAL A 1 112 ? -18.24100 9.04300   -4.25800  1.000 24.42000 ? 114 VAL A O   1 
ATOM   864  C CB  . VAL A 1 112 ? -21.27700 9.56500   -4.16700  1.000 27.79000 ? 114 VAL A CB  1 
ATOM   865  C CG1 . VAL A 1 112 ? -21.10300 10.88000  -3.41000  1.000 26.17000 ? 114 VAL A CG1 1 
ATOM   866  C CG2 . VAL A 1 112 ? -22.71300 9.40700   -4.63400  1.000 26.74000 ? 114 VAL A CG2 1 
ATOM   867  N N   . LEU A 1 113 ? -18.41500 11.02000  -5.32400  1.000 25.57000 ? 115 LEU A N   1 
ATOM   868  C CA  . LEU A 1 113 ? -17.18900 11.57400  -4.76400  1.000 25.35000 ? 115 LEU A CA  1 
ATOM   869  C C   . LEU A 1 113 ? -17.60000 12.55800  -3.68000  1.000 25.77000 ? 115 LEU A C   1 
ATOM   870  O O   . LEU A 1 113 ? -17.97100 13.70100  -3.96700  1.000 25.72000 ? 115 LEU A O   1 
ATOM   871  C CB  . LEU A 1 113 ? -16.33500 12.24100  -5.83700  1.000 25.76000 ? 115 LEU A CB  1 
ATOM   872  C CG  . LEU A 1 113 ? -14.98100 12.80500  -5.37100  1.000 29.20000 ? 115 LEU A CG  1 
ATOM   873  C CD1 . LEU A 1 113 ? -14.04600 11.65300  -4.96000  1.000 23.48000 ? 115 LEU A CD1 1 
ATOM   874  C CD2 . LEU A 1 113 ? -14.35700 13.59900  -6.49200  1.000 25.45000 ? 115 LEU A CD2 1 
ATOM   875  N N   . ALA A 1 114 ? -17.55000 12.11300  -2.43200  1.000 24.36000 ? 116 ALA A N   1 
ATOM   876  C CA  . ALA A 1 114 ? -17.83400 13.01800  -1.33000  1.000 26.26000 ? 116 ALA A CA  1 
ATOM   877  C C   . ALA A 1 114 ? -16.69100 14.02700  -1.17200  1.000 29.64000 ? 116 ALA A C   1 
ATOM   878  O O   . ALA A 1 114 ? -15.50700 13.65300  -1.12900  1.000 28.14000 ? 116 ALA A O   1 
ATOM   879  C CB  . ALA A 1 114 ? -18.05500 12.23200  -0.03900  1.000 26.24000 ? 116 ALA A CB  1 
ATOM   880  N N   . CYS A 1 115 ? -17.05300 15.30700  -1.08300  1.000 27.13000 ? 117 CYS A N   1 
ATOM   881  C CA  . CYS A 1 115 ? -16.09400 16.40300  -1.00600  1.000 29.33000 ? 117 CYS A CA  1 
ATOM   882  C C   . CYS A 1 115 ? -16.48300 17.38400  0.09200   1.000 29.53000 ? 117 CYS A C   1 
ATOM   883  O O   . CYS A 1 115 ? -17.66300 17.54200  0.42800   1.000 28.24000 ? 117 CYS A O   1 
ATOM   884  C CB  . CYS A 1 115 ? -16.00100 17.16800  -2.31600  1.000 29.55000 ? 117 CYS A CB  1 
ATOM   885  S SG  . CYS A 1 115 ? -15.36600 16.24000  -3.69500  1.000 30.39000 ? 117 CYS A SG  1 
ATOM   886  N N   . TYR A 1 116 ? -15.46800 18.04600  0.64600   1.000 29.30000 ? 118 TYR A N   1 
ATOM   887  C CA  . TYR A 1 116 ? -15.66400 19.08900  1.64300   1.000 32.01000 ? 118 TYR A CA  1 
ATOM   888  C C   . TYR A 1 116 ? -14.71800 20.23100  1.32400   1.000 30.39000 ? 118 TYR A C   1 
ATOM   889  O O   . TYR A 1 116 ? -13.53900 20.00700  1.03700   1.000 28.26000 ? 118 TYR A O   1 
ATOM   890  C CB  . TYR A 1 116 ? -15.44800 18.55200  3.06700   1.000 29.87000 ? 118 TYR A CB  1 
ATOM   891  C CG  . TYR A 1 116 ? -16.46700 17.46900  3.36700   1.000 35.82000 ? 118 TYR A CG  1 
ATOM   892  C CD1 . TYR A 1 116 ? -17.74100 17.79100  3.84600   1.000 26.84000 ? 118 TYR A CD1 1 
ATOM   893  C CD2 . TYR A 1 116 ? -16.17900 16.13100  3.10900   1.000 29.37000 ? 118 TYR A CD2 1 
ATOM   894  C CE1 . TYR A 1 116 ? -18.68000 16.80700  4.07800   1.000 29.31000 ? 118 TYR A CE1 1 
ATOM   895  C CE2 . TYR A 1 116 ? -17.11600 15.14600  3.33200   1.000 31.18000 ? 118 TYR A CE2 1 
ATOM   896  C CZ  . TYR A 1 116 ? -18.35600 15.48000  3.81900   1.000 32.16000 ? 118 TYR A CZ  1 
ATOM   897  O OH  . TYR A 1 116 ? -19.28300 14.48900  4.04000   1.000 30.37000 ? 118 TYR A OH  1 
ATOM   898  N N   . ASN A 1 117 ? -15.25700 21.44700  1.31700   1.000 31.77000 ? 119 ASN A N   1 
ATOM   899  C CA  . ASN A 1 117 ? -14.46100 22.63400  1.02700   1.000 34.13000 ? 119 ASN A CA  1 
ATOM   900  C C   . ASN A 1 117 ? -13.73100 22.49000  -0.30400  1.000 33.49000 ? 119 ASN A C   1 
ATOM   901  O O   . ASN A 1 117 ? -12.58700 22.90900  -0.46300  1.000 30.43000 ? 119 ASN A O   1 
ATOM   902  C CB  . ASN A 1 117 ? -13.49500 22.91100  2.17400   1.000 33.77000 ? 119 ASN A CB  1 
ATOM   903  C CG  . ASN A 1 117 ? -14.23300 23.14400  3.48800   1.000 39.68000 ? 119 ASN A CG  1 
ATOM   904  O OD1 . ASN A 1 117 ? -14.94600 24.13100  3.63300   1.000 43.58000 ? 119 ASN A OD1 1 
ATOM   905  N ND2 . ASN A 1 117 ? -14.08900 22.22300  4.43500   1.000 41.93000 ? 119 ASN A ND2 1 
ATOM   906  N N   . GLY A 1 118 ? -14.40700 21.87400  -1.27000  1.000 28.03000 ? 120 GLY A N   1 
ATOM   907  C CA  . GLY A 1 118 ? -13.82300 21.66100  -2.57300  1.000 29.80000 ? 120 GLY A CA  1 
ATOM   908  C C   . GLY A 1 118 ? -12.76400 20.57500  -2.66600  1.000 30.25000 ? 120 GLY A C   1 
ATOM   909  O O   . GLY A 1 118 ? -12.15300 20.43600  -3.73100  1.000 29.15000 ? 120 GLY A O   1 
ATOM   910  N N   . SER A 1 119 ? -12.49200 19.80600  -1.57000  1.000 29.04000 ? 121 SER A N   1 
ATOM   911  C CA  . SER A 1 119 ? -11.50400 18.74700  -1.73800  1.000 29.98000 ? 121 SER A CA  1 
ATOM   912  C C   . SER A 1 119 ? -12.12400 17.36500  -1.55100  1.000 31.91000 ? 121 SER A C   1 
ATOM   913  O O   . SER A 1 119 ? -12.95400 17.15700  -0.65000  1.000 30.01000 ? 121 SER A O   1 
ATOM   914  C CB  . SER A 1 119 ? -10.31100 18.90500  -0.78200  1.000 34.68000 ? 121 SER A CB  1 
ATOM   915  O OG  . SER A 1 119 ? -10.71800 19.37100  0.48500   1.000 44.06000 ? 121 SER A OG  1 
ATOM   916  N N   . PRO A 1 120 ? -11.75600 16.42000  -2.41400  1.000 33.28000 ? 122 PRO A N   1 
ATOM   917  C CA  . PRO A 1 120 ? -12.33600 15.07000  -2.34300  1.000 31.82000 ? 122 PRO A CA  1 
ATOM   918  C C   . PRO A 1 120 ? -11.95600 14.35000  -1.05700  1.000 29.97000 ? 122 PRO A C   1 
ATOM   919  O O   . PRO A 1 120 ? -10.78000 14.25600  -0.69500  1.000 35.31000 ? 122 PRO A O   1 
ATOM   920  C CB  . PRO A 1 120 ? -11.75000 14.36700  -3.57100  1.000 32.45000 ? 122 PRO A CB  1 
ATOM   921  C CG  . PRO A 1 120 ? -10.52400 15.15600  -3.91700  1.000 40.81000 ? 122 PRO A CG  1 
ATOM   922  C CD  . PRO A 1 120 ? -10.85600 16.58100  -3.57500  1.000 36.47000 ? 122 PRO A CD  1 
ATOM   923  N N   . SER A 1 121 ? -12.97100 13.82900  -0.38000  1.000 31.96000 ? 123 SER A N   1 
ATOM   924  C CA  . SER A 1 121 ? -12.81300 13.04200  0.83200   1.000 30.98000 ? 123 SER A CA  1 
ATOM   925  C C   . SER A 1 121 ? -12.81900 11.53600  0.55700   1.000 34.63000 ? 123 SER A C   1 
ATOM   926  O O   . SER A 1 121 ? -11.95000 10.81300  1.05400   1.000 33.53000 ? 123 SER A O   1 
ATOM   927  C CB  . SER A 1 121 ? -13.92700 13.43100  1.80700   1.000 30.15000 ? 123 SER A CB  1 
ATOM   928  O OG  . SER A 1 121 ? -13.84800 12.74200  3.03300   1.000 39.44000 ? 123 SER A OG  1 
ATOM   929  N N   . GLY A 1 122 ? -13.77300 11.04400  -0.23000  1.000 26.80000 ? 124 GLY A N   1 
ATOM   930  C CA  . GLY A 1 122 ? -13.85200 9.61200   -0.47900  1.000 32.67000 ? 124 GLY A CA  1 
ATOM   931  C C   . GLY A 1 122 ? -14.78300 9.32900   -1.63700  1.000 29.37000 ? 124 GLY A C   1 
ATOM   932  O O   . GLY A 1 122 ? -15.45900 10.22500  -2.15300  1.000 27.85000 ? 124 GLY A O   1 
ATOM   933  N N   . VAL A 1 123 ? -14.79600 8.06300   -2.05200  1.000 25.76000 ? 125 VAL A N   1 
ATOM   934  C CA  . VAL A 1 123 ? -15.59900 7.62800   -3.18300  1.000 24.15000 ? 125 VAL A CA  1 
ATOM   935  C C   . VAL A 1 123 ? -16.34200 6.35800   -2.78700  1.000 30.01000 ? 125 VAL A C   1 
ATOM   936  O O   . VAL A 1 123 ? -15.77800 5.45900   -2.15300  1.000 27.56000 ? 125 VAL A O   1 
ATOM   937  C CB  . VAL A 1 123 ? -14.73700 7.42500   -4.45400  1.000 28.19000 ? 125 VAL A CB  1 
ATOM   938  C CG1 . VAL A 1 123 ? -13.76800 6.31200   -4.29200  1.000 33.12000 ? 125 VAL A CG1 1 
ATOM   939  C CG2 . VAL A 1 123 ? -15.59700 7.19600   -5.70100  1.000 28.18000 ? 125 VAL A CG2 1 
ATOM   940  N N   . TYR A 1 124 ? -17.62500 6.29800   -3.12100  1.000 26.85000 ? 126 TYR A N   1 
ATOM   941  C CA  . TYR A 1 124 ? -18.37000 5.08200   -2.82900  1.000 29.91000 ? 126 TYR A CA  1 
ATOM   942  C C   . TYR A 1 124 ? -19.48100 4.94000   -3.85400  1.000 30.25000 ? 126 TYR A C   1 
ATOM   943  O O   . TYR A 1 124 ? -19.85300 5.90200   -4.53600  1.000 24.92000 ? 126 TYR A O   1 
ATOM   944  C CB  . TYR A 1 124 ? -18.93800 5.07600   -1.39900  1.000 29.57000 ? 126 TYR A CB  1 
ATOM   945  C CG  . TYR A 1 124 ? -19.79800 6.28300   -1.06800  1.000 30.91000 ? 126 TYR A CG  1 
ATOM   946  C CD1 . TYR A 1 124 ? -21.13200 6.32700   -1.43700  1.000 34.52000 ? 126 TYR A CD1 1 
ATOM   947  C CD2 . TYR A 1 124 ? -19.27400 7.36900   -0.38800  1.000 33.11000 ? 126 TYR A CD2 1 
ATOM   948  C CE1 . TYR A 1 124 ? -21.92800 7.41800   -1.14100  1.000 36.80000 ? 126 TYR A CE1 1 
ATOM   949  C CE2 . TYR A 1 124 ? -20.06300 8.47800   -0.08300  1.000 36.55000 ? 126 TYR A CE2 1 
ATOM   950  C CZ  . TYR A 1 124 ? -21.39100 8.49000   -0.47000  1.000 36.63000 ? 126 TYR A CZ  1 
ATOM   951  O OH  . TYR A 1 124 ? -22.19600 9.57000   -0.17800  1.000 41.18000 ? 126 TYR A OH  1 
ATOM   952  N N   . GLN A 1 125 ? -20.00100 3.72100   -3.94200  1.000 27.91000 ? 127 GLN A N   1 
ATOM   953  C CA  . GLN A 1 125 ? -21.01400 3.35200   -4.91300  1.000 28.02000 ? 127 GLN A CA  1 
ATOM   954  C C   . GLN A 1 125 ? -22.37200 3.46300   -4.24300  1.000 32.93000 ? 127 GLN A C   1 
ATOM   955  O O   . GLN A 1 125 ? -22.51700 3.16000   -3.05800  1.000 34.03000 ? 127 GLN A O   1 
ATOM   956  C CB  . GLN A 1 125 ? -20.75900 1.93300   -5.43300  1.000 34.94000 ? 127 GLN A CB  1 
ATOM   957  C CG  . GLN A 1 125 ? -21.67400 1.48600   -6.55800  1.000 33.67000 ? 127 GLN A CG  1 
ATOM   958  C CD  . GLN A 1 125 ? -21.40800 2.19400   -7.88800  1.000 35.95000 ? 127 GLN A CD  1 
ATOM   959  O OE1 . GLN A 1 125 ? -20.56400 3.09800   -7.98800  1.000 31.72000 ? 127 GLN A OE1 1 
ATOM   960  N NE2 . GLN A 1 125 ? -22.15000 1.79200   -8.91800  1.000 36.28000 ? 127 GLN A NE2 1 
ATOM   961  N N   . CYS A 1 126 ? -23.35200 3.95200   -4.99500  1.000 30.73000 ? 128 CYS A N   1 
ATOM   962  C CA  . CYS A 1 126 ? -24.61400 4.39100   -4.43400  1.000 35.06000 ? 128 CYS A CA  1 
ATOM   963  C C   . CYS A 1 126 ? -25.71900 3.91200   -5.35400  1.000 33.76000 ? 128 CYS A C   1 
ATOM   964  O O   . CYS A 1 126 ? -25.47700 3.60400   -6.52100  1.000 32.15000 ? 128 CYS A O   1 
ATOM   965  C CB  . CYS A 1 126 ? -24.66000 5.93500   -4.34200  1.000 34.24000 ? 128 CYS A CB  1 
ATOM   966  S SG  . CYS A 1 126 ? -25.53100 6.51400   -2.95800  1.000 52.04000 ? 128 CYS A SG  1 
ATOM   967  N N   . ALA A 1 127 ? -26.94600 3.90300   -4.84000  1.000 37.71000 ? 129 ALA A N   1 
ATOM   968  C CA  . ALA A 1 127 ? -28.11900 3.70000   -5.67400  1.000 34.29000 ? 129 ALA A CA  1 
ATOM   969  C C   . ALA A 1 127 ? -29.17900 4.74700   -5.36300  1.000 32.71000 ? 129 ALA A C   1 
ATOM   970  O O   . ALA A 1 127 ? -29.33800 5.19000   -4.22200  1.000 36.06000 ? 129 ALA A O   1 
ATOM   971  C CB  . ALA A 1 127 ? -28.72300 2.30300   -5.50000  1.000 33.16000 ? 129 ALA A CB  1 
ATOM   972  N N   . MET A 1 128 ? -29.89500 5.13700   -6.40600  1.000 29.19000 ? 130 MET A N   1 
ATOM   973  C CA  . MET A 1 128 ? -31.11700 5.91000   -6.27100  1.000 32.05000 ? 130 MET A CA  1 
ATOM   974  C C   . MET A 1 128 ? -32.25800 5.00500   -5.79300  1.000 33.28000 ? 130 MET A C   1 
ATOM   975  O O   . MET A 1 128 ? -32.64700 4.06100   -6.49200  1.000 29.52000 ? 130 MET A O   1 
ATOM   976  C CB  . MET A 1 128 ? -31.42000 6.56200   -7.61500  1.000 32.19000 ? 130 MET A CB  1 
ATOM   977  C CG  . MET A 1 128 ? -32.78600 7.13900   -7.77500  1.000 36.49000 ? 130 MET A CG  1 
ATOM   978  S SD  . MET A 1 128 ? -32.92100 8.84900   -7.32000  1.000 37.04000 ? 130 MET A SD  1 
ATOM   979  C CE  . MET A 1 128 ? -31.42400 9.63800   -7.91600  1.000 35.83000 ? 130 MET A CE  1 
ATOM   980  N N   . ARG A 1 129 ? -32.77200 5.29100   -4.59100  1.000 31.85000 ? 131 ARG A N   1 
ATOM   981  C CA  . ARG A 1 129 ? -33.84000 4.51100   -3.98700  1.000 31.66000 ? 131 ARG A CA  1 
ATOM   982  C C   . ARG A 1 129 ? -35.15800 4.75000   -4.72500  1.000 30.76000 ? 131 ARG A C   1 
ATOM   983  O O   . ARG A 1 129 ? -35.33800 5.78800   -5.35900  1.000 27.08000 ? 131 ARG A O   1 
ATOM   984  C CB  . ARG A 1 129 ? -34.01800 4.88800   -2.51800  1.000 27.94000 ? 131 ARG A CB  1 
ATOM   985  C CG  . ARG A 1 129 ? -32.78100 4.74100   -1.63400  1.000 30.99000 ? 131 ARG A CG  1 
ATOM   986  C CD  . ARG A 1 129 ? -32.16200 3.34600   -1.67400  1.000 29.40000 ? 131 ARG A CD  1 
ATOM   987  N NE  . ARG A 1 129 ? -33.16300 2.29400   -1.50800  1.000 28.66000 ? 131 ARG A NE  1 
ATOM   988  C CZ  . ARG A 1 129 ? -32.90600 0.99500   -1.63800  1.000 32.88000 ? 131 ARG A CZ  1 
ATOM   989  N NH1 . ARG A 1 129 ? -31.67500 0.57900   -1.91600  1.000 27.50000 ? 131 ARG A NH1 1 
ATOM   990  N NH2 . ARG A 1 129 ? -33.88200 0.10800   -1.48800  1.000 28.79000 ? 131 ARG A NH2 1 
ATOM   991  N N   . PRO A 1 130 ? -36.09400 3.79000   -4.66900  1.000 32.20000 ? 132 PRO A N   1 
ATOM   992  C CA  . PRO A 1 130 ? -37.41600 4.03200   -5.28500  1.000 28.65000 ? 132 PRO A CA  1 
ATOM   993  C C   . PRO A 1 130 ? -38.11700 5.28100   -4.76200  1.000 29.26000 ? 132 PRO A C   1 
ATOM   994  O O   . PRO A 1 130 ? -38.93200 5.85800   -5.48500  1.000 30.06000 ? 132 PRO A O   1 
ATOM   995  C CB  . PRO A 1 130 ? -38.20900 2.75600   -4.94800  1.000 27.76000 ? 132 PRO A CB  1 
ATOM   996  C CG  . PRO A 1 130 ? -37.14300 1.69000   -4.75900  1.000 29.38000 ? 132 PRO A CG  1 
ATOM   997  C CD  . PRO A 1 130 ? -35.96700 2.42300   -4.13100  1.000 28.46000 ? 132 PRO A CD  1 
ATOM   998  N N   . ASN A 1 131 ? -37.83800 5.72000   -3.53800  1.000 27.96000 ? 133 ASN A N   1 
ATOM   999  C CA  . ASN A 1 131 ? -38.44200 6.93500   -3.02000  1.000 32.95000 ? 133 ASN A CA  1 
ATOM   1000 C C   . ASN A 1 131 ? -37.61500 8.18800   -3.34700  1.000 35.40000 ? 133 ASN A C   1 
ATOM   1001 O O   . ASN A 1 131 ? -37.79000 9.22300   -2.69300  1.000 29.75000 ? 133 ASN A O   1 
ATOM   1002 C CB  . ASN A 1 131 ? -38.68400 6.80400   -1.51300  1.000 30.92000 ? 133 ASN A CB  1 
ATOM   1003 C CG  . ASN A 1 131 ? -37.40500 6.82100   -0.69500  1.000 34.52000 ? 133 ASN A CG  1 
ATOM   1004 O OD1 . ASN A 1 131 ? -36.29000 6.93300   -1.22300  1.000 34.02000 ? 133 ASN A OD1 1 
ATOM   1005 N ND2 . ASN A 1 131 ? -37.56600 6.72100   0.62200   1.000 35.26000 ? 133 ASN A ND2 1 
ATOM   1006 N N   . PHE A 1 132 ? -36.72000 8.09800   -4.33700  1.000 30.38000 ? 134 PHE A N   1 
ATOM   1007 C CA  . PHE A 1 132 ? -35.95600 9.19900   -4.91500  1.000 31.86000 ? 134 PHE A CA  1 
ATOM   1008 C C   . PHE A 1 132 ? -34.93900 9.79100   -3.96100  1.000 32.31000 ? 134 PHE A C   1 
ATOM   1009 O O   . PHE A 1 132 ? -34.40000 10.86800  -4.23200  1.000 35.93000 ? 134 PHE A O   1 
ATOM   1010 C CB  . PHE A 1 132 ? -36.86500 10.31400  -5.43700  1.000 29.77000 ? 134 PHE A CB  1 
ATOM   1011 C CG  . PHE A 1 132 ? -37.75000 9.86900   -6.53200  1.000 32.05000 ? 134 PHE A CG  1 
ATOM   1012 C CD1 . PHE A 1 132 ? -37.26800 9.77200   -7.82300  1.000 34.13000 ? 134 PHE A CD1 1 
ATOM   1013 C CD2 . PHE A 1 132 ? -39.05600 9.49000   -6.27200  1.000 29.87000 ? 134 PHE A CD2 1 
ATOM   1014 C CE1 . PHE A 1 132 ? -38.08600 9.31800   -8.84500  1.000 34.34000 ? 134 PHE A CE1 1 
ATOM   1015 C CE2 . PHE A 1 132 ? -39.86600 9.03400   -7.28600  1.000 33.45000 ? 134 PHE A CE2 1 
ATOM   1016 C CZ  . PHE A 1 132 ? -39.38100 8.95500   -8.57400  1.000 29.59000 ? 134 PHE A CZ  1 
ATOM   1017 N N   . THR A 1 133 ? -34.65700 9.12400   -2.86100  1.000 31.90000 ? 135 THR A N   1 
ATOM   1018 C CA  . THR A 1 133 ? -33.59000 9.52700   -1.97800  1.000 30.67000 ? 135 THR A CA  1 
ATOM   1019 C C   . THR A 1 133 ? -32.34900 8.70100   -2.26500  1.000 33.53000 ? 135 THR A C   1 
ATOM   1020 O O   . THR A 1 133 ? -32.34300 7.76200   -3.07000  1.000 34.16000 ? 135 THR A O   1 
ATOM   1021 C CB  . THR A 1 133 ? -33.99900 9.37000   -0.51400  1.000 31.81000 ? 135 THR A CB  1 
ATOM   1022 O OG1 . THR A 1 133 ? -34.19700 7.98000   -0.23000  1.000 35.01000 ? 135 THR A OG1 1 
ATOM   1023 C CG2 . THR A 1 133 ? -35.28000 10.12700  -0.24200  1.000 32.11000 ? 135 THR A CG2 1 
ATOM   1024 N N   . ILE A 1 134 ? -31.29000 9.05300   -1.55500  1.000 31.35000 ? 136 ILE A N   1 
ATOM   1025 C CA  . ILE A 1 134 ? -29.97200 8.45300   -1.66600  1.000 26.48000 ? 136 ILE A CA  1 
ATOM   1026 C C   . ILE A 1 134 ? -29.55200 8.12400   -0.24800  1.000 30.53000 ? 136 ILE A C   1 
ATOM   1027 O O   . ILE A 1 134 ? -29.58500 8.99900   0.62200   1.000 31.29000 ? 136 ILE A O   1 
ATOM   1028 C CB  . ILE A 1 134 ? -28.97100 9.44400   -2.30600  1.000 33.34000 ? 136 ILE A CB  1 
ATOM   1029 C CG1 . ILE A 1 134 ? -29.30700 9.71500   -3.77400  1.000 33.84000 ? 136 ILE A CG1 1 
ATOM   1030 C CG2 . ILE A 1 134 ? -27.53300 9.01400   -2.11000  1.000 35.27000 ? 136 ILE A CG2 1 
ATOM   1031 C CD1 . ILE A 1 134 ? -29.50100 8.49700   -4.59700  1.000 35.87000 ? 136 ILE A CD1 1 
ATOM   1032 N N   . LYS A 1 135 ? -29.16900 6.87200   -0.00200  1.000 30.27000 ? 137 LYS A N   1 
ATOM   1033 C CA  . LYS A 1 135 ? -28.65500 6.49000   1.31000   1.000 32.17000 ? 137 LYS A CA  1 
ATOM   1034 C C   . LYS A 1 135 ? -27.14900 6.71500   1.26600   1.000 34.60000 ? 137 LYS A C   1 
ATOM   1035 O O   . LYS A 1 135 ? -26.35600 5.80300   1.04000   1.000 35.20000 ? 137 LYS A O   1 
ATOM   1036 C CB  . LYS A 1 135 ? -29.01900 5.04000   1.63700   1.000 38.62000 ? 137 LYS A CB  1 
ATOM   1037 N N   . GLY A 1 136 ? -26.75400 7.97600   1.45000   1.000 35.78000 ? 138 GLY A N   1 
ATOM   1038 C CA  . GLY A 1 136 ? -25.38000 8.38200   1.28800   1.000 34.87000 ? 138 GLY A CA  1 
ATOM   1039 C C   . GLY A 1 136 ? -24.64200 8.50300   2.61000   1.000 35.68000 ? 138 GLY A C   1 
ATOM   1040 O O   . GLY A 1 136 ? -25.18400 8.31500   3.69600   1.000 37.83000 ? 138 GLY A O   1 
ATOM   1041 N N   . SER A 1 137 ? -23.36300 8.82900   2.49300   1.000 35.59000 ? 139 SER A N   1 
ATOM   1042 C CA  . SER A 1 137 ? -22.52900 9.16400   3.63700   1.000 36.44000 ? 139 SER A CA  1 
ATOM   1043 C C   . SER A 1 137 ? -22.09200 10.59900  3.39000   1.000 35.56000 ? 139 SER A C   1 
ATOM   1044 O O   . SER A 1 137 ? -21.09600 10.86500  2.71400   1.000 39.90000 ? 139 SER A O   1 
ATOM   1045 C CB  . SER A 1 137 ? -21.34500 8.19800   3.79100   1.000 36.33000 ? 139 SER A CB  1 
ATOM   1046 O OG  . SER A 1 137 ? -20.26200 8.83400   4.44200   1.000 44.01000 ? 139 SER A OG  1 
ATOM   1047 N N   . PHE A 1 138 ? -22.88600 11.50300  3.91700   1.000 35.82000 ? 140 PHE A N   1 
ATOM   1048 C CA  . PHE A 1 138 ? -22.65900 12.93800  3.67800   1.000 31.62000 ? 140 PHE A CA  1 
ATOM   1049 C C   . PHE A 1 138 ? -22.74500 13.68300  4.99800   1.000 33.21000 ? 140 PHE A C   1 
ATOM   1050 O O   . PHE A 1 138 ? -23.66600 13.45300  5.77600   1.000 31.52000 ? 140 PHE A O   1 
ATOM   1051 C CB  . PHE A 1 138 ? -23.74200 13.47000  2.74900   1.000 30.30000 ? 140 PHE A CB  1 
ATOM   1052 C CG  . PHE A 1 138 ? -23.57400 13.15100  1.28900   1.000 29.61000 ? 140 PHE A CG  1 
ATOM   1053 C CD1 . PHE A 1 138 ? -22.35300 13.31100  0.66300   1.000 32.85000 ? 140 PHE A CD1 1 
ATOM   1054 C CD2 . PHE A 1 138 ? -24.64900 12.71800  0.53600   1.000 31.85000 ? 140 PHE A CD2 1 
ATOM   1055 C CE1 . PHE A 1 138 ? -22.20800 13.03900  -0.68500  1.000 30.32000 ? 140 PHE A CE1 1 
ATOM   1056 C CE2 . PHE A 1 138 ? -24.50400 12.44500  -0.81100  1.000 30.43000 ? 140 PHE A CE2 1 
ATOM   1057 C CZ  . PHE A 1 138 ? -23.28500 12.60900  -1.41700  1.000 31.17000 ? 140 PHE A CZ  1 
ATOM   1058 N N   . LEU A 1 139 ? -21.77400 14.55300  5.21300   1.000 30.25000 ? 141 LEU A N   1 
ATOM   1059 C CA  . LEU A 1 139 ? -21.78900 15.38700  6.42100   1.000 33.73000 ? 141 LEU A CA  1 
ATOM   1060 C C   . LEU A 1 139 ? -22.07300 16.83000  6.02500   1.000 32.48000 ? 141 LEU A C   1 
ATOM   1061 O O   . LEU A 1 139 ? -22.19300 17.10100  4.83600   1.000 31.82000 ? 141 LEU A O   1 
ATOM   1062 C CB  . LEU A 1 139 ? -20.42700 15.28000  7.09600   1.000 33.67000 ? 141 LEU A CB  1 
ATOM   1063 C CG  . LEU A 1 139 ? -19.93200 13.87000  7.41200   1.000 40.71000 ? 141 LEU A CG  1 
ATOM   1064 C CD1 . LEU A 1 139 ? -18.51500 13.91400  7.95200   1.000 36.04000 ? 141 LEU A CD1 1 
ATOM   1065 C CD2 . LEU A 1 139 ? -20.85300 13.17700  8.40000   1.000 40.05000 ? 141 LEU A CD2 1 
ATOM   1066 N N   . ASN A 1 140 ? -22.11200 17.70800  7.00700   1.000 33.76000 ? 142 ASN A N   1 
ATOM   1067 C CA  . ASN A 1 140 ? -22.30200 19.14600  6.73800   1.000 34.79000 ? 142 ASN A CA  1 
ATOM   1068 C C   . ASN A 1 140 ? -21.18900 19.59800  5.79100   1.000 35.20000 ? 142 ASN A C   1 
ATOM   1069 O O   . ASN A 1 140 ? -20.04000 19.22800  6.00400   1.000 44.07000 ? 142 ASN A O   1 
ATOM   1070 C CB  . ASN A 1 140 ? -22.36300 19.94400  8.03700   1.000 30.00000 ? 142 ASN A CB  1 
ATOM   1071 C CG  . ASN A 1 140 ? -23.54300 19.58500  8.91200   1.000 30.00000 ? 142 ASN A CG  1 
ATOM   1072 O OD1 . ASN A 1 140 ? -24.59800 19.21200  8.41400   1.000 30.00000 ? 142 ASN A OD1 1 
ATOM   1073 N ND2 . ASN A 1 140 ? -23.38000 19.70800  10.21700  1.000 30.00000 ? 142 ASN A ND2 1 
ATOM   1074 N N   . GLY A 1 141 ? -21.58200 20.34100  4.76000   1.000 44.77000 ? 143 GLY A N   1 
ATOM   1075 C CA  . GLY A 1 141 ? -20.66600 20.90600  3.76100   1.000 31.35000 ? 143 GLY A CA  1 
ATOM   1076 C C   . GLY A 1 141 ? -20.46200 20.00200  2.57100   1.000 32.26000 ? 143 GLY A C   1 
ATOM   1077 O O   . GLY A 1 141 ? -19.69200 20.37500  1.72300   1.000 32.54000 ? 143 GLY A O   1 
ATOM   1078 N N   . SER A 1 142 ? -21.13800 18.86000  2.53000   1.000 29.48000 ? 144 SER A N   1 
ATOM   1079 C CA  . SER A 1 142 ? -21.01500 17.87800  1.41800   1.000 29.02000 ? 144 SER A CA  1 
ATOM   1080 C C   . SER A 1 142 ? -21.75500 18.40600  0.19700   1.000 26.59000 ? 144 SER A C   1 
ATOM   1081 O O   . SER A 1 142 ? -21.53800 17.90600  -0.88300  1.000 24.54000 ? 144 SER A O   1 
ATOM   1082 C CB  . SER A 1 142 ? -21.60300 16.56500  1.82500   1.000 26.25000 ? 144 SER A CB  1 
ATOM   1083 O OG  . SER A 1 142 ? -22.93100 16.71800  2.27200   1.000 31.37000 ? 144 SER A OG  1 
ATOM   1084 N N   . CYS A 1 143 ? -22.63600 19.36000  0.42500   1.000 27.60000 ? 145 CYS A N   1 
ATOM   1085 C CA  . CYS A 1 143 ? -23.48900 19.93200  -0.64800  1.000 24.47000 ? 145 CYS A CA  1 
ATOM   1086 C C   . CYS A 1 143 ? -22.66300 20.24600  -1.89800  1.000 24.44000 ? 145 CYS A C   1 
ATOM   1087 O O   . CYS A 1 143 ? -21.59300 20.82400  -1.77900  1.000 24.97000 ? 145 CYS A O   1 
ATOM   1088 C CB  . CYS A 1 143 ? -24.26800 21.12700  -0.11700  1.000 27.24000 ? 145 CYS A CB  1 
ATOM   1089 S SG  . CYS A 1 143 ? -25.12100 20.85400  1.45700   1.000 30.05000 ? 145 CYS A SG  1 
ATOM   1090 N N   . GLY A 1 144 ? -23.17600 19.86300  -3.05600  1.000 26.58000 ? 146 GLY A N   1 
ATOM   1091 C CA  . GLY A 1 144 ? -22.44300 20.07000  -4.27600  1.000 25.12000 ? 146 GLY A CA  1 
ATOM   1092 C C   . GLY A 1 144 ? -21.51800 18.93500  -4.66100  1.000 24.77000 ? 146 GLY A C   1 
ATOM   1093 O O   . GLY A 1 144 ? -20.96500 18.97000  -5.76700  1.000 25.81000 ? 146 GLY A O   1 
ATOM   1094 N N   . SER A 1 145 ? -21.30200 17.95400  -3.77800  1.000 24.76000 ? 147 SER A N   1 
ATOM   1095 C CA  . SER A 1 145 ? -20.69900 16.69200  -4.20200  1.000 25.57000 ? 147 SER A CA  1 
ATOM   1096 C C   . SER A 1 145 ? -21.57900 16.05700  -5.27200  1.000 24.25000 ? 147 SER A C   1 
ATOM   1097 O O   . SER A 1 145 ? -22.79600 16.24800  -5.28600  1.000 26.45000 ? 147 SER A O   1 
ATOM   1098 C CB  . SER A 1 145 ? -20.53800 15.73100  -3.01600  1.000 25.97000 ? 147 SER A CB  1 
ATOM   1099 O OG  . SER A 1 145 ? -19.60800 16.23200  -2.06200  1.000 25.83000 ? 147 SER A OG  1 
ATOM   1100 N N   . VAL A 1 146 ? -20.96500 15.30800  -6.19000  1.000 25.15000 ? 148 VAL A N   1 
ATOM   1101 C CA  . VAL A 1 146 ? -21.73200 14.82000  -7.32900  1.000 24.33000 ? 148 VAL A CA  1 
ATOM   1102 C C   . VAL A 1 146 ? -21.63900 13.30400  -7.45200  1.000 26.93000 ? 148 VAL A C   1 
ATOM   1103 O O   . VAL A 1 146 ? -20.69600 12.65300  -6.98700  1.000 26.08000 ? 148 VAL A O   1 
ATOM   1104 C CB  . VAL A 1 146 ? -21.32300 15.48500  -8.65900  1.000 27.33000 ? 148 VAL A CB  1 
ATOM   1105 C CG1 . VAL A 1 146 ? -21.67200 17.00200  -8.63600  1.000 27.56000 ? 148 VAL A CG1 1 
ATOM   1106 C CG2 . VAL A 1 146 ? -19.83900 15.26300  -8.97800  1.000 27.83000 ? 148 VAL A CG2 1 
ATOM   1107 N N   . GLY A 1 147 ? -22.66700 12.75100  -8.09100  1.000 24.93000 ? 149 GLY A N   1 
ATOM   1108 C CA  . GLY A 1 147 ? -22.73600 11.34000  -8.40900  1.000 26.26000 ? 149 GLY A CA  1 
ATOM   1109 C C   . GLY A 1 147 ? -22.56400 11.16300  -9.90300  1.000 27.27000 ? 149 GLY A C   1 
ATOM   1110 O O   . GLY A 1 147 ? -22.97500 12.02000  -10.69300 1.000 25.05000 ? 149 GLY A O   1 
ATOM   1111 N N   . PHE A 1 148 ? -21.96500 10.04300  -10.30000 1.000 25.34000 ? 150 PHE A N   1 
ATOM   1112 C CA  . PHE A 1 148 ? -21.55700 9.94000   -11.69400 1.000 30.80000 ? 150 PHE A CA  1 
ATOM   1113 C C   . PHE A 1 148 ? -21.35500 8.48200   -12.07900 1.000 29.56000 ? 150 PHE A C   1 
ATOM   1114 O O   . PHE A 1 148 ? -21.15700 7.61000   -11.22900 1.000 30.23000 ? 150 PHE A O   1 
ATOM   1115 C CB  . PHE A 1 148 ? -20.26600 10.73800  -11.96800 1.000 26.66000 ? 150 PHE A CB  1 
ATOM   1116 C CG  . PHE A 1 148 ? -19.09900 10.28300  -11.15300 1.000 27.55000 ? 150 PHE A CG  1 
ATOM   1117 C CD1 . PHE A 1 148 ? -18.93100 10.73400  -9.85100  1.000 28.84000 ? 150 PHE A CD1 1 
ATOM   1118 C CD2 . PHE A 1 148 ? -18.17700 9.38600   -11.67200 1.000 27.14000 ? 150 PHE A CD2 1 
ATOM   1119 C CE1 . PHE A 1 148 ? -17.85900 10.29200  -9.07800  1.000 28.00000 ? 150 PHE A CE1 1 
ATOM   1120 C CE2 . PHE A 1 148 ? -17.11400 8.94100   -10.90900 1.000 29.05000 ? 150 PHE A CE2 1 
ATOM   1121 C CZ  . PHE A 1 148 ? -16.95100 9.40800   -9.60900  1.000 31.67000 ? 150 PHE A CZ  1 
ATOM   1122 N N   . ASN A 1 149 ? -21.40900 8.24100   -13.38500 1.000 30.28000 ? 151 ASN A N   1 
ATOM   1123 C CA  . ASN A 1 149 ? -20.92100 7.02200   -14.00700 1.000 32.71000 ? 151 ASN A CA  1 
ATOM   1124 C C   . ASN A 1 149 ? -19.86000 7.38700   -15.03800 1.000 35.72000 ? 151 ASN A C   1 
ATOM   1125 O O   . ASN A 1 149 ? -19.76500 8.53500   -15.48800 1.000 35.80000 ? 151 ASN A O   1 
ATOM   1126 C CB  . ASN A 1 149 ? -22.06500 6.23600   -14.65500 1.000 34.25000 ? 151 ASN A CB  1 
ATOM   1127 C CG  . ASN A 1 149 ? -22.96500 5.61300   -13.63000 1.000 33.60000 ? 151 ASN A CG  1 
ATOM   1128 O OD1 . ASN A 1 149 ? -22.64100 4.58100   -13.07100 1.000 37.71000 ? 151 ASN A OD1 1 
ATOM   1129 N ND2 . ASN A 1 149 ? -24.08300 6.26600   -13.33500 1.000 32.94000 ? 151 ASN A ND2 1 
ATOM   1130 N N   . ILE A 1 150 ? -19.02400 6.41200   -15.38900 1.000 34.11000 ? 152 ILE A N   1 
ATOM   1131 C CA  . ILE A 1 150 ? -18.03300 6.60300   -16.44100 1.000 37.28000 ? 152 ILE A CA  1 
ATOM   1132 C C   . ILE A 1 150 ? -18.17300 5.46300   -17.43300 1.000 43.12000 ? 152 ILE A C   1 
ATOM   1133 O O   . ILE A 1 150 ? -18.24300 4.29600   -17.03600 1.000 41.21000 ? 152 ILE A O   1 
ATOM   1134 C CB  . ILE A 1 150 ? -16.59400 6.67400   -15.89600 1.000 34.16000 ? 152 ILE A CB  1 
ATOM   1135 C CG1 . ILE A 1 150 ? -16.54600 7.58700   -14.66800 1.000 31.93000 ? 152 ILE A CG1 1 
ATOM   1136 C CG2 . ILE A 1 150 ? -15.65400 7.16100   -16.99400 1.000 38.24000 ? 152 ILE A CG2 1 
ATOM   1137 C CD1 . ILE A 1 150 ? -15.15900 8.06400   -14.27100 1.000 31.12000 ? 152 ILE A CD1 1 
ATOM   1138 N N   . ASP A 1 151 ? -18.21600 5.79600   -18.71900 1.000 46.58000 ? 153 ASP A N   1 
ATOM   1139 C CA  . ASP A 1 151 ? -18.32700 4.77900   -19.75700 1.000 48.47000 ? 153 ASP A CA  1 
ATOM   1140 C C   . ASP A 1 151 ? -17.49200 5.21700   -20.94800 1.000 51.98000 ? 153 ASP A C   1 
ATOM   1141 O O   . ASP A 1 151 ? -17.85400 6.17300   -21.63900 1.000 54.24000 ? 153 ASP A O   1 
ATOM   1142 C CB  . ASP A 1 151 ? -19.78300 4.54600   -20.13900 1.000 50.46000 ? 153 ASP A CB  1 
ATOM   1143 C CG  . ASP A 1 151 ? -20.38000 3.36100   -19.39900 1.000 57.35000 ? 153 ASP A CG  1 
ATOM   1144 O OD1 . ASP A 1 151 ? -19.93600 2.22400   -19.67200 1.000 61.76000 ? 153 ASP A OD1 1 
ATOM   1145 O OD2 . ASP A 1 151 ? -21.26200 3.56200   -18.52900 1.000 57.20000 ? 153 ASP A OD2 1 
ATOM   1146 N N   . TYR A 1 152 ? -16.37000 4.52300   -21.16300 1.000 53.53000 ? 154 TYR A N   1 
ATOM   1147 C CA  . TYR A 1 152 ? -15.45000 4.80000   -22.26600 1.000 52.94000 ? 154 TYR A CA  1 
ATOM   1148 C C   . TYR A 1 152 ? -14.89400 6.21900   -22.17100 1.000 53.84000 ? 154 TYR A C   1 
ATOM   1149 O O   . TYR A 1 152 ? -14.93500 6.99400   -23.12900 1.000 55.75000 ? 154 TYR A O   1 
ATOM   1150 C CB  . TYR A 1 152 ? -16.12200 4.56300   -23.62100 1.000 54.44000 ? 154 TYR A CB  1 
ATOM   1151 N N   . ASP A 1 153 ? -14.36800 6.55300   -20.99300 1.000 51.28000 ? 155 ASP A N   1 
ATOM   1152 C CA  . ASP A 1 153 ? -13.75400 7.83600   -20.65800 1.000 51.10000 ? 155 ASP A CA  1 
ATOM   1153 C C   . ASP A 1 153 ? -14.74200 8.99900   -20.61500 1.000 46.32000 ? 155 ASP A C   1 
ATOM   1154 O O   . ASP A 1 153 ? -14.31000 10.15000  -20.42000 1.000 42.40000 ? 155 ASP A O   1 
ATOM   1155 C CB  . ASP A 1 153 ? -12.60700 8.20000   -21.61200 1.000 52.42000 ? 155 ASP A CB  1 
ATOM   1156 C CG  . ASP A 1 153 ? -11.35900 7.36700   -21.36500 1.000 63.18000 ? 155 ASP A CG  1 
ATOM   1157 O OD1 . ASP A 1 153 ? -10.96800 7.19400   -20.18600 1.000 61.46000 ? 155 ASP A OD1 1 
ATOM   1158 O OD2 . ASP A 1 153 ? -10.77500 6.86900   -22.35400 1.000 68.07000 ? 155 ASP A OD2 1 
ATOM   1159 N N   . CYS A 1 154 ? -16.04300 8.75800   -20.77900 1.000 45.52000 ? 156 CYS A N   1 
ATOM   1160 C CA  . CYS A 1 154 ? -17.04000 9.82400   -20.69000 1.000 44.80000 ? 156 CYS A CA  1 
ATOM   1161 C C   . CYS A 1 154 ? -17.71800 9.77800   -19.32800 1.000 38.09000 ? 156 CYS A C   1 
ATOM   1162 O O   . CYS A 1 154 ? -18.23800 8.73500   -18.92500 1.000 41.83000 ? 156 CYS A O   1 
ATOM   1163 C CB  . CYS A 1 154 ? -18.09300 9.71300   -21.79300 1.000 44.12000 ? 156 CYS A CB  1 
ATOM   1164 S SG  . CYS A 1 154 ? -19.36000 11.02300  -21.71800 1.000 45.44000 ? 156 CYS A SG  1 
ATOM   1165 N N   . VAL A 1 155 ? -17.70700 10.90300  -18.62400 1.000 35.59000 ? 157 VAL A N   1 
ATOM   1166 C CA  . VAL A 1 155 ? -18.29300 10.98200  -17.29400 1.000 34.36000 ? 157 VAL A CA  1 
ATOM   1167 C C   . VAL A 1 155 ? -19.75000 11.41700  -17.42300 1.000 36.68000 ? 157 VAL A C   1 
ATOM   1168 O O   . VAL A 1 155 ? -20.04200 12.50800  -17.92500 1.000 35.07000 ? 157 VAL A O   1 
ATOM   1169 C CB  . VAL A 1 155 ? -17.51100 11.94600  -16.39400 1.000 34.85000 ? 157 VAL A CB  1 
ATOM   1170 C CG1 . VAL A 1 155 ? -18.13900 11.97700  -15.01000 1.000 33.33000 ? 157 VAL A CG1 1 
ATOM   1171 C CG2 . VAL A 1 155 ? -16.04100 11.53600  -16.30800 1.000 33.05000 ? 157 VAL A CG2 1 
ATOM   1172 N N   . SER A 1 156 ? -20.66000 10.57100  -16.94700 1.000 30.40000 ? 158 SER A N   1 
ATOM   1173 C CA  . SER A 1 156 ? -22.08300 10.88800  -16.89600 1.000 34.16000 ? 158 SER A CA  1 
ATOM   1174 C C   . SER A 1 156 ? -22.41500 11.42500  -15.50600 1.000 33.95000 ? 158 SER A C   1 
ATOM   1175 O O   . SER A 1 156 ? -22.50500 10.65900  -14.54200 1.000 31.45000 ? 158 SER A O   1 
ATOM   1176 C CB  . SER A 1 156 ? -22.90300 9.64600   -17.21300 1.000 38.01000 ? 158 SER A CB  1 
ATOM   1177 O OG  . SER A 1 156 ? -23.20900 9.60500   -18.58600 1.000 47.05000 ? 158 SER A OG  1 
ATOM   1178 N N   . PHE A 1 157 ? -22.60200 12.74300  -15.39200 1.000 31.21000 ? 159 PHE A N   1 
ATOM   1179 C CA  . PHE A 1 157 ? -23.03400 13.33400  -14.13000 1.000 29.64000 ? 159 PHE A CA  1 
ATOM   1180 C C   . PHE A 1 157 ? -24.54300 13.17900  -13.98300 1.000 29.63000 ? 159 PHE A C   1 
ATOM   1181 O O   . PHE A 1 157 ? -25.30500 13.62800  -14.84600 1.000 33.20000 ? 159 PHE A O   1 
ATOM   1182 C CB  . PHE A 1 157 ? -22.63400 14.80500  -14.05700 1.000 31.88000 ? 159 PHE A CB  1 
ATOM   1183 C CG  . PHE A 1 157 ? -21.15600 15.01600  -13.98300 1.000 28.99000 ? 159 PHE A CG  1 
ATOM   1184 C CD1 . PHE A 1 157 ? -20.47200 14.78800  -12.79900 1.000 27.72000 ? 159 PHE A CD1 1 
ATOM   1185 C CD2 . PHE A 1 157 ? -20.44300 15.40700  -15.10500 1.000 30.05000 ? 159 PHE A CD2 1 
ATOM   1186 C CE1 . PHE A 1 157 ? -19.10400 14.97200  -12.73000 1.000 26.62000 ? 159 PHE A CE1 1 
ATOM   1187 C CE2 . PHE A 1 157 ? -19.06200 15.59100  -15.03800 1.000 27.77000 ? 159 PHE A CE2 1 
ATOM   1188 C CZ  . PHE A 1 157 ? -18.40600 15.37900  -13.84700 1.000 29.84000 ? 159 PHE A CZ  1 
ATOM   1189 N N   . CYS A 1 158 ? -24.98300 12.55000  -12.89200 1.000 27.27000 ? 160 CYS A N   1 
ATOM   1190 C CA  . CYS A 1 158 ? -26.39600 12.28800  -12.70500 1.000 27.53000 ? 160 CYS A CA  1 
ATOM   1191 C C   . CYS A 1 158 ? -26.96500 12.81300  -11.39600 1.000 27.60000 ? 160 CYS A C   1 
ATOM   1192 O O   . CYS A 1 158 ? -28.19300 12.81900  -11.23900 1.000 27.35000 ? 160 CYS A O   1 
ATOM   1193 C CB  . CYS A 1 158 ? -26.68200 10.78200  -12.80600 1.000 28.57000 ? 160 CYS A CB  1 
ATOM   1194 S SG  . CYS A 1 158 ? -25.81700 9.79300   -11.58600 1.000 30.66000 ? 160 CYS A SG  1 
ATOM   1195 N N   . TYR A 1 159 ? -26.13100 13.28600  -10.47500 1.000 26.81000 ? 161 TYR A N   1 
ATOM   1196 C CA  . TYR A 1 159 ? -26.62400 13.68200  -9.16400  1.000 25.86000 ? 161 TYR A CA  1 
ATOM   1197 C C   . TYR A 1 159 ? -25.73100 14.77700  -8.61300  1.000 26.25000 ? 161 TYR A C   1 
ATOM   1198 O O   . TYR A 1 159 ? -24.50800 14.65000  -8.66400  1.000 24.28000 ? 161 TYR A O   1 
ATOM   1199 C CB  . TYR A 1 159 ? -26.64400 12.48300  -8.20300  1.000 23.51000 ? 161 TYR A CB  1 
ATOM   1200 C CG  . TYR A 1 159 ? -27.08100 12.81700  -6.79100  1.000 25.24000 ? 161 TYR A CG  1 
ATOM   1201 C CD1 . TYR A 1 159 ? -28.42100 12.86000  -6.45900  1.000 24.33000 ? 161 TYR A CD1 1 
ATOM   1202 C CD2 . TYR A 1 159 ? -26.15200 13.10300  -5.79400  1.000 25.27000 ? 161 TYR A CD2 1 
ATOM   1203 C CE1 . TYR A 1 159 ? -28.83500 13.16800  -5.16500  1.000 26.09000 ? 161 TYR A CE1 1 
ATOM   1204 C CE2 . TYR A 1 159 ? -26.55300 13.38600  -4.49300  1.000 22.36000 ? 161 TYR A CE2 1 
ATOM   1205 C CZ  . TYR A 1 159 ? -27.89900 13.42300  -4.19200  1.000 25.49000 ? 161 TYR A CZ  1 
ATOM   1206 O OH  . TYR A 1 159 ? -28.32400 13.72000  -2.92200  1.000 28.28000 ? 161 TYR A OH  1 
ATOM   1207 N N   . MET A 1 160 ? -26.33500 15.84600  -8.08900  1.000 24.49000 ? 162 MET A N   1 
ATOM   1208 C CA  . MET A 1 160 ? -25.62200 16.77900  -7.22900  1.000 23.13000 ? 162 MET A CA  1 
ATOM   1209 C C   . MET A 1 160 ? -26.31800 16.80300  -5.87600  1.000 23.86000 ? 162 MET A C   1 
ATOM   1210 O O   . MET A 1 160 ? -27.53800 16.94200  -5.80500  1.000 25.12000 ? 162 MET A O   1 
ATOM   1211 C CB  . MET A 1 160 ? -25.55500 18.19700  -7.83000  1.000 22.90000 ? 162 MET A CB  1 
ATOM   1212 C CG  . MET A 1 160 ? -24.88400 19.19300  -6.89900  1.000 25.15000 ? 162 MET A CG  1 
ATOM   1213 S SD  . MET A 1 160 ? -24.70300 20.85400  -7.62700  1.000 31.48000 ? 162 MET A SD  1 
ATOM   1214 C CE  . MET A 1 160 ? -23.06100 20.71600  -8.32600  1.000 24.97000 ? 162 MET A CE  1 
ATOM   1215 N N   . HIS A 1 161 ? -25.54100 16.69700  -4.81200  1.000 25.54000 ? 163 HIS A N   1 
ATOM   1216 C CA  . HIS A 1 161 ? -26.10000 16.61400  -3.47300  1.000 24.47000 ? 163 HIS A CA  1 
ATOM   1217 C C   . HIS A 1 161 ? -26.53400 17.98300  -2.95600  1.000 27.52000 ? 163 HIS A C   1 
ATOM   1218 O O   . HIS A 1 161 ? -25.79100 18.96400  -3.06700  1.000 25.29000 ? 163 HIS A O   1 
ATOM   1219 C CB  . HIS A 1 161 ? -25.06600 16.01500  -2.52200  1.000 24.58000 ? 163 HIS A CB  1 
ATOM   1220 C CG  . HIS A 1 161 ? -25.54700 15.93800  -1.11800  1.000 24.22000 ? 163 HIS A CG  1 
ATOM   1221 N ND1 . HIS A 1 161 ? -26.74600 15.34600  -0.78600  1.000 24.18000 ? 163 HIS A ND1 1 
ATOM   1222 C CD2 . HIS A 1 161 ? -25.02200 16.40900  0.03300   1.000 26.97000 ? 163 HIS A CD2 1 
ATOM   1223 C CE1 . HIS A 1 161 ? -26.93300 15.44700  0.51500   1.000 30.05000 ? 163 HIS A CE1 1 
ATOM   1224 N NE2 . HIS A 1 161 ? -25.90400 16.09500  1.03500   1.000 29.08000 ? 163 HIS A NE2 1 
ATOM   1225 N N   . HIS A 1 162 ? -27.73700 18.04500  -2.36800  1.000 23.93000 ? 164 HIS A N   1 
ATOM   1226 C CA  . HIS A 1 162 ? -28.26200 19.29900  -1.82800  1.000 25.34000 ? 164 HIS A CA  1 
ATOM   1227 C C   . HIS A 1 162 ? -28.50100 19.25600  -0.32600  1.000 28.40000 ? 164 HIS A C   1 
ATOM   1228 O O   . HIS A 1 162 ? -28.12000 20.20000  0.38500   1.000 29.67000 ? 164 HIS A O   1 
ATOM   1229 C CB  . HIS A 1 162 ? -29.58400 19.68200  -2.53800  1.000 24.93000 ? 164 HIS A CB  1 
ATOM   1230 C CG  . HIS A 1 162 ? -29.39400 20.26000  -3.90600  1.000 26.12000 ? 164 HIS A CG  1 
ATOM   1231 N ND1 . HIS A 1 162 ? -29.78100 21.54300  -4.23400  1.000 25.79000 ? 164 HIS A ND1 1 
ATOM   1232 C CD2 . HIS A 1 162 ? -28.83500 19.73700  -5.02300  1.000 25.71000 ? 164 HIS A CD2 1 
ATOM   1233 C CE1 . HIS A 1 162 ? -29.48500 21.77700  -5.50100  1.000 27.45000 ? 164 HIS A CE1 1 
ATOM   1234 N NE2 . HIS A 1 162 ? -28.91100 20.69800  -6.00200  1.000 28.12000 ? 164 HIS A NE2 1 
ATOM   1235 N N   . MET A 1 163 ? -29.14600 18.21000  0.19400   1.000 28.29000 ? 165 MET A N   1 
ATOM   1236 C CA  . MET A 1 163 ? -29.60900 18.31600  1.57100   1.000 30.36000 ? 165 MET A CA  1 
ATOM   1237 C C   . MET A 1 163 ? -29.81000 16.96000  2.22100   1.000 29.05000 ? 165 MET A C   1 
ATOM   1238 O O   . MET A 1 163 ? -29.96600 15.93200  1.55900   1.000 27.29000 ? 165 MET A O   1 
ATOM   1239 C CB  . MET A 1 163 ? -30.92000 19.07800  1.65300   1.000 26.22000 ? 165 MET A CB  1 
ATOM   1240 C CG  . MET A 1 163 ? -32.00500 18.43100  0.85000   1.000 24.69000 ? 165 MET A CG  1 
ATOM   1241 S SD  . MET A 1 163 ? -33.24500 19.66000  0.41900   1.000 41.32000 ? 165 MET A SD  1 
ATOM   1242 C CE  . MET A 1 163 ? -33.58900 20.39100  2.03300   1.000 38.20000 ? 165 MET A CE  1 
ATOM   1243 N N   . GLU A 1 164 ? -29.86100 17.00300  3.54500   1.000 29.92000 ? 166 GLU A N   1 
ATOM   1244 C CA  . GLU A 1 164 ? -30.16700 15.85400  4.37400   1.000 33.52000 ? 166 GLU A CA  1 
ATOM   1245 C C   . GLU A 1 164 ? -31.64000 15.90200  4.75400   1.000 32.59000 ? 166 GLU A C   1 
ATOM   1246 O O   . GLU A 1 164 ? -32.18100 16.97600  5.01500   1.000 32.02000 ? 166 GLU A O   1 
ATOM   1247 C CB  . GLU A 1 164 ? -29.30100 15.85000  5.63200   1.000 30.65000 ? 166 GLU A CB  1 
ATOM   1248 C CG  . GLU A 1 164 ? -29.34500 14.54800  6.38500   1.000 36.49000 ? 166 GLU A CG  1 
ATOM   1249 C CD  . GLU A 1 164 ? -28.37900 14.54500  7.53400   1.000 41.57000 ? 166 GLU A CD  1 
ATOM   1250 O OE1 . GLU A 1 164 ? -28.55100 15.39200  8.43700   1.000 51.11000 ? 166 GLU A OE1 1 
ATOM   1251 O OE2 . GLU A 1 164 ? -27.43100 13.73100  7.50300   1.000 45.51000 ? 166 GLU A OE2 1 
ATOM   1252 N N   . LEU A 1 165 ? -32.28500 14.74700  4.75400   1.000 32.71000 ? 167 LEU A N   1 
ATOM   1253 C CA  . LEU A 1 165 ? -33.67200 14.60100  5.17700   1.000 36.92000 ? 167 LEU A CA  1 
ATOM   1254 C C   . LEU A 1 165 ? -33.73000 14.04100  6.59200   1.000 36.45000 ? 167 LEU A C   1 
ATOM   1255 O O   . LEU A 1 165 ? -32.74700 13.48100  7.08400   1.000 37.44000 ? 167 LEU A O   1 
ATOM   1256 C CB  . LEU A 1 165 ? -34.43600 13.68200  4.20500   1.000 31.66000 ? 167 LEU A CB  1 
ATOM   1257 C CG  . LEU A 1 165 ? -34.64800 14.31300  2.82400   1.000 30.72000 ? 167 LEU A CG  1 
ATOM   1258 C CD1 . LEU A 1 165 ? -35.07600 13.29900  1.77700   1.000 33.85000 ? 167 LEU A CD1 1 
ATOM   1259 C CD2 . LEU A 1 165 ? -35.66600 15.46400  2.89600   1.000 36.43000 ? 167 LEU A CD2 1 
ATOM   1260 N N   . PRO A 1 166 ? -34.87000 14.17900  7.28100   1.000 41.50000 ? 168 PRO A N   1 
ATOM   1261 C CA  . PRO A 1 166 ? -34.93100 13.78300  8.70300   1.000 40.53000 ? 168 PRO A CA  1 
ATOM   1262 C C   . PRO A 1 166 ? -34.47800 12.36400  9.02000   1.000 44.32000 ? 168 PRO A C   1 
ATOM   1263 O O   . PRO A 1 166 ? -33.95400 12.13700  10.11900  1.000 46.89000 ? 168 PRO A O   1 
ATOM   1264 C CB  . PRO A 1 166 ? -36.41500 13.98100  9.05500   1.000 43.57000 ? 168 PRO A CB  1 
ATOM   1265 C CG  . PRO A 1 166 ? -37.06300 14.65500  7.85000   1.000 47.02000 ? 168 PRO A CG  1 
ATOM   1266 C CD  . PRO A 1 166 ? -35.98000 15.08300  6.92700   1.000 42.55000 ? 168 PRO A CD  1 
ATOM   1267 N N   . THR A 1 167 ? -34.65200 11.40400  8.11200   1.000 37.02000 ? 169 THR A N   1 
ATOM   1268 C CA  . THR A 1 167 ? -34.27800 10.02600  8.39900   1.000 43.25000 ? 169 THR A CA  1 
ATOM   1269 C C   . THR A 1 167 ? -32.78800 9.77300   8.24200   1.000 44.72000 ? 169 THR A C   1 
ATOM   1270 O O   . THR A 1 167 ? -32.33800 8.64500   8.46600   1.000 42.71000 ? 169 THR A O   1 
ATOM   1271 C CB  . THR A 1 167 ? -35.05800 9.07000   7.48700   1.000 46.55000 ? 169 THR A CB  1 
ATOM   1272 O OG1 . THR A 1 167 ? -35.20500 9.66700   6.19000   1.000 48.78000 ? 169 THR A OG1 1 
ATOM   1273 C CG2 . THR A 1 167 ? -36.44000 8.80100   8.05900   1.000 40.11000 ? 169 THR A CG2 1 
ATOM   1274 N N   . GLY A 1 168 ? -32.01700 10.78600  7.86600   1.000 38.80000 ? 170 GLY A N   1 
ATOM   1275 C CA  . GLY A 1 168 ? -30.61200 10.60900  7.58700   1.000 39.94000 ? 170 GLY A CA  1 
ATOM   1276 C C   . GLY A 1 168 ? -30.29300 10.24700  6.15700   1.000 38.25000 ? 170 GLY A C   1 
ATOM   1277 O O   . GLY A 1 168 ? -29.14900 9.87800   5.87200   1.000 42.71000 ? 170 GLY A O   1 
ATOM   1278 N N   . VAL A 1 169 ? -31.26900 10.31200  5.25300   1.000 36.15000 ? 171 VAL A N   1 
ATOM   1279 C CA  . VAL A 1 169 ? -31.01300 10.02400  3.84600   1.000 35.35000 ? 171 VAL A CA  1 
ATOM   1280 C C   . VAL A 1 169 ? -30.92400 11.35800  3.11400   1.000 33.34000 ? 171 VAL A C   1 
ATOM   1281 O O   . VAL A 1 169 ? -31.10300 12.42300  3.71600   1.000 30.40000 ? 171 VAL A O   1 
ATOM   1282 C CB  . VAL A 1 169 ? -32.09600 9.10500   3.25000   1.000 35.19000 ? 171 VAL A CB  1 
ATOM   1283 C CG1 . VAL A 1 169 ? -32.12000 7.77300   3.99600   1.000 34.73000 ? 171 VAL A CG1 1 
ATOM   1284 C CG2 . VAL A 1 169 ? -33.45200 9.76000   3.32400   1.000 34.22000 ? 171 VAL A CG2 1 
ATOM   1285 N N   . HIS A 1 170 ? -30.64700 11.32100  1.81900   1.000 31.57000 ? 172 HIS A N   1 
ATOM   1286 C CA  . HIS A 1 170 ? -30.17900 12.52100  1.14500   1.000 32.82000 ? 172 HIS A CA  1 
ATOM   1287 C C   . HIS A 1 170 ? -30.95300 12.77500  -0.14200  1.000 29.17000 ? 172 HIS A C   1 
ATOM   1288 O O   . HIS A 1 170 ? -31.39000 11.84500  -0.82800  1.000 28.88000 ? 172 HIS A O   1 
ATOM   1289 C CB  . HIS A 1 170 ? -28.66700 12.40400  0.91300   1.000 27.16000 ? 172 HIS A CB  1 
ATOM   1290 C CG  . HIS A 1 170 ? -27.89900 12.21000  2.18400   1.000 29.24000 ? 172 HIS A CG  1 
ATOM   1291 N ND1 . HIS A 1 170 ? -27.33900 11.00100  2.54500   1.000 32.39000 ? 172 HIS A ND1 1 
ATOM   1292 C CD2 . HIS A 1 170 ? -27.64700 13.05900  3.20900   1.000 29.13000 ? 172 HIS A CD2 1 
ATOM   1293 C CE1 . HIS A 1 170 ? -26.75900 11.12100  3.72700   1.000 32.62000 ? 172 HIS A CE1 1 
ATOM   1294 N NE2 . HIS A 1 170 ? -26.92600 12.36400  4.14900   1.000 32.33000 ? 172 HIS A NE2 1 
ATOM   1295 N N   . ALA A 1 171 ? -31.12800 14.06100  -0.44900  1.000 28.44000 ? 173 ALA A N   1 
ATOM   1296 C CA  . ALA A 1 171 ? -31.87000 14.50000  -1.61600  1.000 25.13000 ? 173 ALA A CA  1 
ATOM   1297 C C   . ALA A 1 171 ? -31.01400 15.44800  -2.43700  1.000 25.05000 ? 173 ALA A C   1 
ATOM   1298 O O   . ALA A 1 171 ? -30.18000 16.18500  -1.90600  1.000 24.23000 ? 173 ALA A O   1 
ATOM   1299 C CB  . ALA A 1 171 ? -33.19700 15.20300  -1.22300  1.000 27.10000 ? 173 ALA A CB  1 
ATOM   1300 N N   . GLY A 1 172 ? -31.23000 15.42100  -3.73800  1.000 25.69000 ? 174 GLY A N   1 
ATOM   1301 C CA  . GLY A 1 172 ? -30.43300 16.24000  -4.62500  1.000 22.10000 ? 174 GLY A CA  1 
ATOM   1302 C C   . GLY A 1 172 ? -31.08600 16.31400  -5.98400  1.000 25.54000 ? 174 GLY A C   1 
ATOM   1303 O O   . GLY A 1 172 ? -32.23200 15.88500  -6.17100  1.000 27.02000 ? 174 GLY A O   1 
ATOM   1304 N N   . THR A 1 173 ? -30.33300 16.84700  -6.94500  1.000 24.65000 ? 175 THR A N   1 
ATOM   1305 C CA  . THR A 1 173 ? -30.87400 17.16000  -8.26100  1.000 24.30000 ? 175 THR A CA  1 
ATOM   1306 C C   . THR A 1 173 ? -30.04100 16.49500  -9.34400  1.000 25.09000 ? 175 THR A C   1 
ATOM   1307 O O   . THR A 1 173 ? -28.92200 16.03600  -9.10100  1.000 25.66000 ? 175 THR A O   1 
ATOM   1308 C CB  . THR A 1 173 ? -30.89800 18.68200  -8.50100  1.000 26.89000 ? 175 THR A CB  1 
ATOM   1309 O OG1 . THR A 1 173 ? -29.55400 19.16500  -8.57900  1.000 27.12000 ? 175 THR A OG1 1 
ATOM   1310 C CG2 . THR A 1 173 ? -31.63300 19.39800  -7.37000  1.000 25.66000 ? 175 THR A CG2 1 
ATOM   1311 N N   . ASP A 1 174 ? -30.57800 16.47300  -10.56100 1.000 23.79000 ? 176 ASP A N   1 
ATOM   1312 C CA  . ASP A 1 174 ? -29.71300 16.25600  -11.70900 1.000 26.71000 ? 176 ASP A CA  1 
ATOM   1313 C C   . ASP A 1 174 ? -28.88500 17.52300  -11.93800 1.000 26.11000 ? 176 ASP A C   1 
ATOM   1314 O O   . ASP A 1 174 ? -29.04200 18.52600  -11.24500 1.000 26.66000 ? 176 ASP A O   1 
ATOM   1315 C CB  . ASP A 1 174 ? -30.52700 15.86200  -12.94500 1.000 25.54000 ? 176 ASP A CB  1 
ATOM   1316 C CG  . ASP A 1 174 ? -31.60600 16.87900  -13.31300 1.000 31.37000 ? 176 ASP A CG  1 
ATOM   1317 O OD1 . ASP A 1 174 ? -31.45000 18.09600  -13.03600 1.000 30.65000 ? 176 ASP A OD1 1 
ATOM   1318 O OD2 . ASP A 1 174 ? -32.62400 16.44000  -13.89300 1.000 32.66000 ? 176 ASP A OD2 1 
ATOM   1319 N N   . LEU A 1 175 ? -27.99500 17.49500  -12.92200 1.000 24.53000 ? 177 LEU A N   1 
ATOM   1320 C CA  . LEU A 1 175 ? -27.11800 18.64500  -13.12300 1.000 26.33000 ? 177 LEU A CA  1 
ATOM   1321 C C   . LEU A 1 175 ? -27.81300 19.79700  -13.83300 1.000 29.07000 ? 177 LEU A C   1 
ATOM   1322 O O   . LEU A 1 175 ? -27.19300 20.85700  -14.02200 1.000 28.93000 ? 177 LEU A O   1 
ATOM   1323 C CB  . LEU A 1 175 ? -25.85800 18.23800  -13.88700 1.000 26.20000 ? 177 LEU A CB  1 
ATOM   1324 C CG  . LEU A 1 175 ? -24.69000 17.88900  -12.95800 1.000 30.21000 ? 177 LEU A CG  1 
ATOM   1325 C CD1 . LEU A 1 175 ? -24.24900 19.11800  -12.18500 1.000 30.06000 ? 177 LEU A CD1 1 
ATOM   1326 C CD2 . LEU A 1 175 ? -25.08200 16.77100  -11.98200 1.000 28.60000 ? 177 LEU A CD2 1 
ATOM   1327 N N   . GLU A 1 176 ? -29.07800 19.62400  -14.21500 1.000 28.39000 ? 178 GLU A N   1 
ATOM   1328 C CA  . GLU A 1 176 ? -29.92000 20.73800  -14.63600 1.000 30.84000 ? 178 GLU A CA  1 
ATOM   1329 C C   . GLU A 1 176 ? -30.73800 21.30900  -13.48500 1.000 29.64000 ? 178 GLU A C   1 
ATOM   1330 O O   . GLU A 1 176 ? -31.61500 22.15000  -13.71500 1.000 28.94000 ? 178 GLU A O   1 
ATOM   1331 C CB  . GLU A 1 176 ? -30.83900 20.30200  -15.77900 1.000 33.24000 ? 178 GLU A CB  1 
ATOM   1332 C CG  . GLU A 1 176 ? -30.11400 20.25400  -17.11900 1.000 36.97000 ? 178 GLU A CG  1 
ATOM   1333 C CD  . GLU A 1 176 ? -30.95500 19.65600  -18.23900 1.000 45.15000 ? 178 GLU A CD  1 
ATOM   1334 O OE1 . GLU A 1 176 ? -30.72100 20.03700  -19.40400 1.000 55.19000 ? 178 GLU A OE1 1 
ATOM   1335 O OE2 . GLU A 1 176 ? -31.83200 18.81000  -17.96400 1.000 43.03000 ? 178 GLU A OE2 1 
ATOM   1336 N N   . GLY A 1 177 ? -30.48400 20.86400  -12.25500 1.000 26.69000 ? 179 GLY A N   1 
ATOM   1337 C CA  . GLY A 1 177 ? -31.12000 21.46100  -11.09600 1.000 25.78000 ? 179 GLY A CA  1 
ATOM   1338 C C   . GLY A 1 177 ? -32.52200 20.99400  -10.77500 1.000 28.90000 ? 179 GLY A C   1 
ATOM   1339 O O   . GLY A 1 177 ? -33.14800 21.57700  -9.88500  1.000 27.19000 ? 179 GLY A O   1 
ATOM   1340 N N   . ASN A 1 178 ? -33.02600 19.94300  -11.43200 1.000 28.79000 ? 180 ASN A N   1 
ATOM   1341 C CA  . ASN A 1 178 ? -34.34100 19.39300  -11.11700 1.000 27.89000 ? 180 ASN A CA  1 
ATOM   1342 C C   . ASN A 1 178 ? -34.19900 18.32600  -10.04600 1.000 29.03000 ? 180 ASN A C   1 
ATOM   1343 O O   . ASN A 1 178 ? -33.46600 17.34600  -10.23200 1.000 28.24000 ? 180 ASN A O   1 
ATOM   1344 C CB  . ASN A 1 178 ? -34.99900 18.80800  -12.36300 1.000 31.01000 ? 180 ASN A CB  1 
ATOM   1345 C CG  . ASN A 1 178 ? -35.43200 19.88200  -13.32900 1.000 31.09000 ? 180 ASN A CG  1 
ATOM   1346 O OD1 . ASN A 1 178 ? -36.11700 20.82100  -12.94600 1.000 32.45000 ? 180 ASN A OD1 1 
ATOM   1347 N ND2 . ASN A 1 178 ? -35.00700 19.76500  -14.57400 1.000 36.21000 ? 180 ASN A ND2 1 
ATOM   1348 N N   . PHE A 1 179 ? -34.91000 18.50400  -8.93800  1.000 27.44000 ? 181 PHE A N   1 
ATOM   1349 C CA  . PHE A 1 179 ? -34.78900 17.55900  -7.84400  1.000 27.88000 ? 181 PHE A CA  1 
ATOM   1350 C C   . PHE A 1 179 ? -35.23000 16.16900  -8.28300  1.000 27.52000 ? 181 PHE A C   1 
ATOM   1351 O O   . PHE A 1 179 ? -36.06600 16.00300  -9.17900  1.000 27.33000 ? 181 PHE A O   1 
ATOM   1352 C CB  . PHE A 1 179 ? -35.62400 18.00200  -6.65400  1.000 26.23000 ? 181 PHE A CB  1 
ATOM   1353 C CG  . PHE A 1 179 ? -34.82600 18.64600  -5.56900  1.000 27.25000 ? 181 PHE A CG  1 
ATOM   1354 C CD1 . PHE A 1 179 ? -34.20800 17.88000  -4.59600  1.000 24.82000 ? 181 PHE A CD1 1 
ATOM   1355 C CD2 . PHE A 1 179 ? -34.68100 20.03800  -5.53400  1.000 27.56000 ? 181 PHE A CD2 1 
ATOM   1356 C CE1 . PHE A 1 179 ? -33.46400 18.46700  -3.59300  1.000 25.99000 ? 181 PHE A CE1 1 
ATOM   1357 C CE2 . PHE A 1 179 ? -33.94600 20.64300  -4.53000  1.000 27.96000 ? 181 PHE A CE2 1 
ATOM   1358 C CZ  . PHE A 1 179 ? -33.33200 19.86700  -3.55700  1.000 27.16000 ? 181 PHE A CZ  1 
ATOM   1359 N N   . TYR A 1 180 ? -34.63300 15.16600  -7.65400  1.000 27.57000 ? 182 TYR A N   1 
ATOM   1360 C CA  . TYR A 1 180 ? -35.16500 13.81000  -7.67500  1.000 29.49000 ? 182 TYR A CA  1 
ATOM   1361 C C   . TYR A 1 180 ? -36.15800 13.70800  -6.52900  1.000 29.49000 ? 182 TYR A C   1 
ATOM   1362 O O   . TYR A 1 180 ? -35.80900 14.00000  -5.37800  1.000 30.30000 ? 182 TYR A O   1 
ATOM   1363 C CB  . TYR A 1 180 ? -34.05300 12.77300  -7.52000  1.000 28.98000 ? 182 TYR A CB  1 
ATOM   1364 C CG  . TYR A 1 180 ? -33.11100 12.65600  -8.69900  1.000 29.33000 ? 182 TYR A CG  1 
ATOM   1365 C CD1 . TYR A 1 180 ? -33.48800 11.95400  -9.85000  1.000 29.20000 ? 182 TYR A CD1 1 
ATOM   1366 C CD2 . TYR A 1 180 ? -31.82600 13.20800  -8.64900  1.000 24.87000 ? 182 TYR A CD2 1 
ATOM   1367 C CE1 . TYR A 1 180 ? -32.62200 11.83400  -10.92700 1.000 29.04000 ? 182 TYR A CE1 1 
ATOM   1368 C CE2 . TYR A 1 180 ? -30.94800 13.09000  -9.72100  1.000 25.37000 ? 182 TYR A CE2 1 
ATOM   1369 C CZ  . TYR A 1 180 ? -31.34900 12.39400  -10.85400 1.000 28.71000 ? 182 TYR A CZ  1 
ATOM   1370 O OH  . TYR A 1 180 ? -30.47600 12.26300  -11.90800 1.000 26.27000 ? 182 TYR A OH  1 
ATOM   1371 N N   . GLY A 1 181 ? -37.39500 13.33300  -6.84100  1.000 27.75000 ? 183 GLY A N   1 
ATOM   1372 C CA  . GLY A 1 181 ? -38.41800 13.20800  -5.83600  1.000 28.45000 ? 183 GLY A CA  1 
ATOM   1373 C C   . GLY A 1 181 ? -39.08600 14.51600  -5.44700  1.000 36.01000 ? 183 GLY A C   1 
ATOM   1374 O O   . GLY A 1 181 ? -38.76700 15.59800  -5.94700  1.000 31.76000 ? 183 GLY A O   1 
ATOM   1375 N N   . PRO A 1 182 ? -40.02500 14.43000  -4.52800  1.000 34.89000 ? 184 PRO A N   1 
ATOM   1376 C CA  . PRO A 1 182 ? -40.84000 15.60600  -4.19300  1.000 35.90000 ? 184 PRO A CA  1 
ATOM   1377 C C   . PRO A 1 182 ? -40.20300 16.52500  -3.16200  1.000 38.25000 ? 184 PRO A C   1 
ATOM   1378 O O   . PRO A 1 182 ? -40.89300 16.98000  -2.24700  1.000 42.40000 ? 184 PRO A O   1 
ATOM   1379 C CB  . PRO A 1 182 ? -42.12400 14.97100  -3.64800  1.000 37.08000 ? 184 PRO A CB  1 
ATOM   1380 C CG  . PRO A 1 182 ? -41.64300 13.67400  -3.02600  1.000 33.75000 ? 184 PRO A CG  1 
ATOM   1381 C CD  . PRO A 1 182 ? -40.52400 13.19100  -3.90000  1.000 32.60000 ? 184 PRO A CD  1 
ATOM   1382 N N   . PHE A 1 183 ? -38.91000 16.81300  -3.27600  1.000 34.09000 ? 185 PHE A N   1 
ATOM   1383 C CA  . PHE A 1 183 ? -38.23400 17.60700  -2.26600  1.000 33.36000 ? 185 PHE A CA  1 
ATOM   1384 C C   . PHE A 1 183 ? -37.92400 19.00600  -2.79600  1.000 30.05000 ? 185 PHE A C   1 
ATOM   1385 O O   . PHE A 1 183 ? -37.94100 19.25600  -4.00400  1.000 27.70000 ? 185 PHE A O   1 
ATOM   1386 C CB  . PHE A 1 183 ? -36.96800 16.88500  -1.78600  1.000 33.48000 ? 185 PHE A CB  1 
ATOM   1387 C CG  . PHE A 1 183 ? -37.21100 15.44600  -1.45900  1.000 34.18000 ? 185 PHE A CG  1 
ATOM   1388 C CD1 . PHE A 1 183 ? -37.98900 15.10000  -0.36400  1.000 34.44000 ? 185 PHE A CD1 1 
ATOM   1389 C CD2 . PHE A 1 183 ? -36.70500 14.43500  -2.26200  1.000 34.96000 ? 185 PHE A CD2 1 
ATOM   1390 C CE1 . PHE A 1 183 ? -38.25100 13.75900  -0.06500  1.000 36.51000 ? 185 PHE A CE1 1 
ATOM   1391 C CE2 . PHE A 1 183 ? -36.95900 13.11200  -1.96500  1.000 33.98000 ? 185 PHE A CE2 1 
ATOM   1392 C CZ  . PHE A 1 183 ? -37.74300 12.77600  -0.85800  1.000 33.53000 ? 185 PHE A CZ  1 
ATOM   1393 N N   . VAL A 1 184 ? -37.68400 19.92800  -1.85800  1.000 31.02000 ? 186 VAL A N   1 
ATOM   1394 C CA  . VAL A 1 184 ? -37.40500 21.33000  -2.15500  1.000 33.06000 ? 186 VAL A CA  1 
ATOM   1395 C C   . VAL A 1 184 ? -36.18700 21.76500  -1.35300  1.000 31.43000 ? 186 VAL A C   1 
ATOM   1396 O O   . VAL A 1 184 ? -35.90600 21.22300  -0.27900  1.000 32.80000 ? 186 VAL A O   1 
ATOM   1397 C CB  . VAL A 1 184 ? -38.61800 22.24700  -1.83900  1.000 31.86000 ? 186 VAL A CB  1 
ATOM   1398 C CG1 . VAL A 1 184 ? -39.83600 21.84200  -2.65300  1.000 31.07000 ? 186 VAL A CG1 1 
ATOM   1399 C CG2 . VAL A 1 184 ? -38.93400 22.21600  -0.34900  1.000 33.23000 ? 186 VAL A CG2 1 
ATOM   1400 N N   . ASP A 1 185 ? -35.46300 22.76400  -1.87500  1.000 32.41000 ? 187 ASP A N   1 
ATOM   1401 C CA  . ASP A 1 185 ? -34.20600 23.21300  -1.26300  1.000 30.29000 ? 187 ASP A CA  1 
ATOM   1402 C C   . ASP A 1 185 ? -34.50500 24.36100  -0.30400  1.000 39.12000 ? 187 ASP A C   1 
ATOM   1403 O O   . ASP A 1 185 ? -34.21700 25.53600  -0.54900  1.000 35.57000 ? 187 ASP A O   1 
ATOM   1404 C CB  . ASP A 1 185 ? -33.18700 23.60600  -2.32400  1.000 30.18000 ? 187 ASP A CB  1 
ATOM   1405 C CG  . ASP A 1 185 ? -33.70100 24.64800  -3.29800  1.000 30.58000 ? 187 ASP A CG  1 
ATOM   1406 O OD1 . ASP A 1 185 ? -34.90400 24.98000  -3.27400  1.000 31.94000 ? 187 ASP A OD1 1 
ATOM   1407 O OD2 . ASP A 1 185 ? -32.88200 25.12400  -4.10700  1.000 28.54000 ? 187 ASP A OD2 1 
ATOM   1408 N N   . ARG A 1 186 ? -35.01800 23.98000  0.85400   1.000 38.30000 ? 188 ARG A N   1 
ATOM   1409 C CA  . ARG A 1 186 ? -35.62400 24.89400  1.80300   1.000 39.58000 ? 188 ARG A CA  1 
ATOM   1410 C C   . ARG A 1 186 ? -35.89000 24.09700  3.07000   1.000 40.84000 ? 188 ARG A C   1 
ATOM   1411 O O   . ARG A 1 186 ? -36.14900 22.89600  2.99100   1.000 35.36000 ? 188 ARG A O   1 
ATOM   1412 C CB  . ARG A 1 186 ? -36.90200 25.46600  1.16300   1.000 43.48000 ? 188 ARG A CB  1 
ATOM   1413 C CG  . ARG A 1 186 ? -37.99000 25.97500  2.02300   1.000 43.47000 ? 188 ARG A CG  1 
ATOM   1414 C CD  . ARG A 1 186 ? -39.06700 26.52500  1.09100   1.000 40.38000 ? 188 ARG A CD  1 
ATOM   1415 N NE  . ARG A 1 186 ? -40.22700 25.66900  0.87900   1.000 38.54000 ? 188 ARG A NE  1 
ATOM   1416 C CZ  . ARG A 1 186 ? -41.40900 25.84400  1.48600   1.000 48.17000 ? 188 ARG A CZ  1 
ATOM   1417 N NH1 . ARG A 1 186 ? -41.57500 26.82600  2.36300   1.000 42.83000 ? 188 ARG A NH1 1 
ATOM   1418 N NH2 . ARG A 1 186 ? -42.43800 25.04900  1.21700   1.000 52.98000 ? 188 ARG A NH2 1 
ATOM   1419 N N   . GLN A 1 187 ? -35.75100 24.73800  4.22700   1.000 38.82000 ? 189 GLN A N   1 
ATOM   1420 C CA  . GLN A 1 187 ? -35.97700 24.05400  5.49700   1.000 41.54000 ? 189 GLN A CA  1 
ATOM   1421 C C   . GLN A 1 187 ? -37.47800 23.89600  5.70900   1.000 43.02000 ? 189 GLN A C   1 
ATOM   1422 O O   . GLN A 1 187 ? -38.19900 24.88800  5.87300   1.000 42.14000 ? 189 GLN A O   1 
ATOM   1423 C CB  . GLN A 1 187 ? -35.33100 24.82100  6.64700   1.000 42.96000 ? 189 GLN A CB  1 
ATOM   1424 C CG  . GLN A 1 187 ? -35.34800 24.06000  7.97300   1.000 44.70000 ? 189 GLN A CG  1 
ATOM   1425 C CD  . GLN A 1 187 ? -35.03300 24.95600  9.15400   1.000 44.36000 ? 189 GLN A CD  1 
ATOM   1426 O OE1 . GLN A 1 187 ? -34.32800 25.94600  9.02100   1.000 49.57000 ? 189 GLN A OE1 1 
ATOM   1427 N NE2 . GLN A 1 187 ? -35.56400 24.61300  10.31800  1.000 50.66000 ? 189 GLN A NE2 1 
ATOM   1428 N N   . THR A 1 188 ? -37.95500 22.65400  5.67700   1.000 38.02000 ? 190 THR A N   1 
ATOM   1429 C CA  . THR A 1 188 ? -39.37600 22.35000  5.78700   1.000 43.17000 ? 190 THR A CA  1 
ATOM   1430 C C   . THR A 1 188 ? -39.55100 21.11100  6.65500   1.000 48.71000 ? 190 THR A C   1 
ATOM   1431 O O   . THR A 1 188 ? -38.59700 20.58700  7.24100   1.000 45.12000 ? 190 THR A O   1 
ATOM   1432 C CB  . THR A 1 188 ? -40.01400 22.05000  4.43000   1.000 46.32000 ? 190 THR A CB  1 
ATOM   1433 O OG1 . THR A 1 188 ? -39.39800 20.86400  3.91100   1.000 44.76000 ? 190 THR A OG1 1 
ATOM   1434 C CG2 . THR A 1 188 ? -39.84300 23.19300  3.46000   1.000 44.27000 ? 190 THR A CG2 1 
ATOM   1435 N N   . ALA A 1 189 ? -40.78900 20.62000  6.67900   1.000 46.30000 ? 191 ALA A N   1 
ATOM   1436 C CA  . ALA A 1 189 ? -41.16500 19.39300  7.35800   1.000 50.84000 ? 191 ALA A CA  1 
ATOM   1437 C C   . ALA A 1 189 ? -41.06200 18.17000  6.45700   1.000 48.83000 ? 191 ALA A C   1 
ATOM   1438 O O   . ALA A 1 189 ? -41.47500 17.08500  6.86800   1.000 53.55000 ? 191 ALA A O   1 
ATOM   1439 C CB  . ALA A 1 189 ? -42.59600 19.51300  7.90200   1.000 44.91000 ? 191 ALA A CB  1 
ATOM   1440 N N   . GLN A 1 190 ? -40.51900 18.31800  5.24900   1.000 51.60000 ? 192 GLN A N   1 
ATOM   1441 C CA  . GLN A 1 190 ? -40.56800 17.24800  4.26100   1.000 46.22000 ? 192 GLN A CA  1 
ATOM   1442 C C   . GLN A 1 190 ? -39.83900 15.99800  4.75500   1.000 46.81000 ? 192 GLN A C   1 
ATOM   1443 O O   . GLN A 1 190 ? -38.86800 16.06900  5.51300   1.000 46.91000 ? 192 GLN A O   1 
ATOM   1444 C CB  . GLN A 1 190 ? -39.96800 17.73100  2.93600   1.000 45.27000 ? 192 GLN A CB  1 
ATOM   1445 C CG  . GLN A 1 190 ? -38.47300 18.00100  2.97700   1.000 38.81000 ? 192 GLN A CG  1 
ATOM   1446 C CD  . GLN A 1 190 ? -37.97700 18.79700  1.77000   1.000 39.88000 ? 192 GLN A CD  1 
ATOM   1447 O OE1 . GLN A 1 190 ? -38.55300 18.73500  0.68100   1.000 34.52000 ? 192 GLN A OE1 1 
ATOM   1448 N NE2 . GLN A 1 190 ? -36.89500 19.53900  1.96200   1.000 36.92000 ? 192 GLN A NE2 1 
ATOM   1449 N N   . ALA A 1 191 ? -40.33000 14.84200  4.31700   1.000 48.82000 ? 193 ALA A N   1 
ATOM   1450 C CA  . ALA A 1 191 ? -39.78100 13.54700  4.69500   1.000 46.23000 ? 193 ALA A CA  1 
ATOM   1451 C C   . ALA A 1 191 ? -39.90200 12.59500  3.51700   1.000 40.07000 ? 193 ALA A C   1 
ATOM   1452 O O   . ALA A 1 191 ? -40.86400 12.65200  2.74800   1.000 42.53000 ? 193 ALA A O   1 
ATOM   1453 C CB  . ALA A 1 191 ? -40.49900 12.95000  5.91400   1.000 44.35000 ? 193 ALA A CB  1 
ATOM   1454 N N   . ALA A 1 192 ? -38.91700 11.71200  3.38900   1.000 46.23000 ? 194 ALA A N   1 
ATOM   1455 C CA  . ALA A 1 192 ? -38.94000 10.71200  2.32700   1.000 41.15000 ? 194 ALA A CA  1 
ATOM   1456 C C   . ALA A 1 192 ? -40.14700 9.79000   2.46600   1.000 45.65000 ? 194 ALA A C   1 
ATOM   1457 O O   . ALA A 1 192 ? -40.53300 9.40400   3.57300   1.000 43.05000 ? 194 ALA A O   1 
ATOM   1458 C CB  . ALA A 1 192 ? -37.65700 9.88900   2.35300   1.000 45.05000 ? 194 ALA A CB  1 
ATOM   1459 N N   . GLY A 1 193 ? -40.74600 9.44700   1.32900   1.000 43.37000 ? 195 GLY A N   1 
ATOM   1460 C CA  . GLY A 1 193 ? -41.79500 8.45400   1.30300   1.000 42.00000 ? 195 GLY A CA  1 
ATOM   1461 C C   . GLY A 1 193 ? -41.28300 7.08700   1.72400   1.000 46.70000 ? 195 GLY A C   1 
ATOM   1462 O O   . GLY A 1 193 ? -40.09300 6.86500   1.97100   1.000 40.01000 ? 195 GLY A O   1 
ATOM   1463 N N   . THR A 1 194 ? -42.22400 6.14400   1.80800   1.000 47.70000 ? 196 THR A N   1 
ATOM   1464 C CA  . THR A 1 194 ? -41.87900 4.79300   2.23900   1.000 41.37000 ? 196 THR A CA  1 
ATOM   1465 C C   . THR A 1 194 ? -40.93500 4.14600   1.23200   1.000 42.91000 ? 196 THR A C   1 
ATOM   1466 O O   . THR A 1 194 ? -41.19200 4.15300   0.02500   1.000 47.44000 ? 196 THR A O   1 
ATOM   1467 C CB  . THR A 1 194 ? -43.14200 3.94300   2.42400   1.000 43.41000 ? 196 THR A CB  1 
ATOM   1468 O OG1 . THR A 1 194 ? -42.78200 2.64200   2.90900   1.000 51.83000 ? 196 THR A OG1 1 
ATOM   1469 C CG2 . THR A 1 194 ? -43.91300 3.78400   1.11700   1.000 43.89000 ? 196 THR A CG2 1 
ATOM   1470 N N   . ASP A 1 195 ? -39.81600 3.62500   1.71200   1.000 37.31000 ? 197 ASP A N   1 
ATOM   1471 C CA  . ASP A 1 195 ? -38.90300 3.03900   0.75300   1.000 40.42000 ? 197 ASP A CA  1 
ATOM   1472 C C   . ASP A 1 195 ? -39.21800 1.56100   0.53400   1.000 38.31000 ? 197 ASP A C   1 
ATOM   1473 O O   . ASP A 1 195 ? -39.91900 0.92300   1.32000   1.000 39.70000 ? 197 ASP A O   1 
ATOM   1474 C CB  . ASP A 1 195 ? -37.45300 3.20200   1.17600   1.000 35.68000 ? 197 ASP A CB  1 
ATOM   1475 C CG  . ASP A 1 195 ? -36.53600 3.19600   -0.01500  1.000 37.59000 ? 197 ASP A CG  1 
ATOM   1476 O OD1 . ASP A 1 195 ? -37.03500 3.58300   -1.10400  1.000 37.76000 ? 197 ASP A OD1 1 
ATOM   1477 O OD2 . ASP A 1 195 ? -35.36600 2.79300   0.11100   1.000 32.04000 ? 197 ASP A OD2 1 
ATOM   1478 N N   . THR A 1 196 ? -38.72300 1.04200   -0.58100  1.000 32.11000 ? 198 THR A N   1 
ATOM   1479 C CA  . THR A 1 196 ? -38.96000 -0.33200  -0.98100  1.000 33.16000 ? 198 THR A CA  1 
ATOM   1480 C C   . THR A 1 196 ? -37.66400 -0.88800  -1.54600  1.000 33.18000 ? 198 THR A C   1 
ATOM   1481 O O   . THR A 1 196 ? -36.75400 -0.13700  -1.90700  1.000 29.72000 ? 198 THR A O   1 
ATOM   1482 C CB  . THR A 1 196 ? -40.07200 -0.43600  -2.02600  1.000 33.68000 ? 198 THR A CB  1 
ATOM   1483 O OG1 . THR A 1 196 ? -39.77900 0.43300   -3.12500  1.000 33.17000 ? 198 THR A OG1 1 
ATOM   1484 C CG2 . THR A 1 196 ? -41.43800 -0.04800  -1.42900  1.000 37.21000 ? 198 THR A CG2 1 
ATOM   1485 N N   . THR A 1 197 ? -37.59700 -2.21700  -1.62900  1.000 27.46000 ? 199 THR A N   1 
ATOM   1486 C CA  . THR A 1 197 ? -36.41300 -2.88500  -2.13400  1.000 27.47000 ? 199 THR A CA  1 
ATOM   1487 C C   . THR A 1 197 ? -36.47200 -2.92100  -3.65100  1.000 28.05000 ? 199 THR A C   1 
ATOM   1488 O O   . THR A 1 197 ? -37.55400 -3.04000  -4.23700  1.000 28.45000 ? 199 THR A O   1 
ATOM   1489 C CB  . THR A 1 197 ? -36.31900 -4.29000  -1.53900  1.000 29.55000 ? 199 THR A CB  1 
ATOM   1490 O OG1 . THR A 1 197 ? -36.28700 -4.17000  -0.11300  1.000 30.49000 ? 199 THR A OG1 1 
ATOM   1491 C CG2 . THR A 1 197 ? -35.05200 -5.02000  -2.00200  1.000 26.01000 ? 199 THR A CG2 1 
ATOM   1492 N N   . ILE A 1 198 ? -35.31000 -2.75900  -4.28700  1.000 23.04000 ? 200 ILE A N   1 
ATOM   1493 C CA  . ILE A 1 198 ? -35.22400 -2.70400  -5.74500  1.000 24.92000 ? 200 ILE A CA  1 
ATOM   1494 C C   . ILE A 1 198 ? -35.18200 -4.13400  -6.27000  1.000 28.13000 ? 200 ILE A C   1 
ATOM   1495 O O   . ILE A 1 198 ? -34.11200 -4.74400  -6.35600  1.000 28.83000 ? 200 ILE A O   1 
ATOM   1496 C CB  . ILE A 1 198 ? -33.99400 -1.90500  -6.21700  1.000 27.47000 ? 200 ILE A CB  1 
ATOM   1497 C CG1 . ILE A 1 198 ? -33.99700 -0.49400  -5.59600  1.000 26.92000 ? 200 ILE A CG1 1 
ATOM   1498 C CG2 . ILE A 1 198 ? -33.97200 -1.80300  -7.72900  1.000 26.30000 ? 200 ILE A CG2 1 
ATOM   1499 C CD1 . ILE A 1 198 ? -32.65800 0.24500   -5.74200  1.000 27.25000 ? 200 ILE A CD1 1 
ATOM   1500 N N   . THR A 1 199 ? -36.35500 -4.66800  -6.61300  1.000 27.68000 ? 201 THR A N   1 
ATOM   1501 C CA  . THR A 1 199 ? -36.48800 -6.09500  -6.89900  1.000 27.03000 ? 201 THR A CA  1 
ATOM   1502 C C   . THR A 1 199 ? -35.62800 -6.52200  -8.07800  1.000 26.45000 ? 201 THR A C   1 
ATOM   1503 O O   . THR A 1 199 ? -35.01100 -7.60000  -8.04700  1.000 24.99000 ? 201 THR A O   1 
ATOM   1504 C CB  . THR A 1 199 ? -37.95700 -6.42600  -7.17800  1.000 28.87000 ? 201 THR A CB  1 
ATOM   1505 O OG1 . THR A 1 199 ? -38.78600 -5.86100  -6.14800  1.000 26.05000 ? 201 THR A OG1 1 
ATOM   1506 C CG2 . THR A 1 199 ? -38.14900 -7.94300  -7.28300  1.000 21.35000 ? 201 THR A CG2 1 
ATOM   1507 N N   . VAL A 1 200 ? -35.58700 -5.70700  -9.13800  1.000 24.33000 ? 202 VAL A N   1 
ATOM   1508 C CA  . VAL A 1 200 ? -34.82500 -6.10600  -10.31700 1.000 26.14000 ? 202 VAL A CA  1 
ATOM   1509 C C   . VAL A 1 200 ? -33.34500 -6.21800  -9.98900  1.000 28.81000 ? 202 VAL A C   1 
ATOM   1510 O O   . VAL A 1 200 ? -32.63900 -7.07100  -10.55400 1.000 27.42000 ? 202 VAL A O   1 
ATOM   1511 C CB  . VAL A 1 200 ? -35.07200 -5.16200  -11.51000 1.000 30.03000 ? 202 VAL A CB  1 
ATOM   1512 C CG1 . VAL A 1 200 ? -34.50100 -3.74000  -11.24600 1.000 25.97000 ? 202 VAL A CG1 1 
ATOM   1513 C CG2 . VAL A 1 200 ? -34.44700 -5.77800  -12.77600 1.000 28.75000 ? 202 VAL A CG2 1 
ATOM   1514 N N   . ASN A 1 201 ? -32.86700 -5.43300  -9.02300  1.000 26.14000 ? 203 ASN A N   1 
ATOM   1515 C CA  . ASN A 1 201 ? -31.45900 -5.47500  -8.64100  1.000 29.26000 ? 203 ASN A CA  1 
ATOM   1516 C C   . ASN A 1 201 ? -31.14000 -6.69800  -7.78500  1.000 27.70000 ? 203 ASN A C   1 
ATOM   1517 O O   . ASN A 1 201 ? -30.05200 -7.27200  -7.90700  1.000 26.89000 ? 203 ASN A O   1 
ATOM   1518 C CB  . ASN A 1 201 ? -31.09000 -4.20300  -7.87800  1.000 28.51000 ? 203 ASN A CB  1 
ATOM   1519 C CG  . ASN A 1 201 ? -30.96700 -2.97900  -8.79200  1.000 30.62000 ? 203 ASN A CG  1 
ATOM   1520 O OD1 . ASN A 1 201 ? -31.17300 -3.06700  -9.99900  1.000 26.94000 ? 203 ASN A OD1 1 
ATOM   1521 N ND2 . ASN A 1 201 ? -30.63200 -1.83200  -8.20400  1.000 25.61000 ? 203 ASN A ND2 1 
ATOM   1522 N N   . VAL A 1 202 ? -32.03300 -7.06300  -6.86100  1.000 27.29000 ? 204 VAL A N   1 
ATOM   1523 C CA  . VAL A 1 202 ? -31.82200 -8.28100  -6.07500  1.000 28.88000 ? 204 VAL A CA  1 
ATOM   1524 C C   . VAL A 1 202 ? -31.71700 -9.48900  -6.99400  1.000 26.63000 ? 204 VAL A C   1 
ATOM   1525 O O   . VAL A 1 202 ? -30.91200 -10.40500 -6.76300  1.000 30.37000 ? 204 VAL A O   1 
ATOM   1526 C CB  . VAL A 1 202 ? -32.95300 -8.48000  -5.04900  1.000 29.17000 ? 204 VAL A CB  1 
ATOM   1527 C CG1 . VAL A 1 202 ? -32.81100 -9.85300  -4.34200  1.000 29.82000 ? 204 VAL A CG1 1 
ATOM   1528 C CG2 . VAL A 1 202 ? -32.98200 -7.33200  -4.04100  1.000 26.83000 ? 204 VAL A CG2 1 
ATOM   1529 N N   . LEU A 1 203 ? -32.53700 -9.51700  -8.04200  1.000 26.30000 ? 205 LEU A N   1 
ATOM   1530 C CA  . LEU A 1 203 ? -32.50900 -10.64900 -8.96400  1.000 28.95000 ? 205 LEU A CA  1 
ATOM   1531 C C   . LEU A 1 203 ? -31.21500 -10.67000 -9.76000  1.000 29.73000 ? 205 LEU A C   1 
ATOM   1532 O O   . LEU A 1 203 ? -30.66700 -11.74400 -10.04300 1.000 28.37000 ? 205 LEU A O   1 
ATOM   1533 C CB  . LEU A 1 203 ? -33.70700 -10.58800 -9.90700  1.000 26.12000 ? 205 LEU A CB  1 
ATOM   1534 C CG  . LEU A 1 203 ? -35.07700 -10.88000 -9.29200  1.000 27.13000 ? 205 LEU A CG  1 
ATOM   1535 C CD1 . LEU A 1 203 ? -36.12400 -10.52500 -10.30600 1.000 25.66000 ? 205 LEU A CD1 1 
ATOM   1536 C CD2 . LEU A 1 203 ? -35.20300 -12.39000 -8.88700  1.000 25.76000 ? 205 LEU A CD2 1 
ATOM   1537 N N   . ALA A 1 204 ? -30.74000 -9.49200  -10.16900 1.000 25.40000 ? 206 ALA A N   1 
ATOM   1538 C CA  . ALA A 1 204 ? -29.44100 -9.39500  -10.81900 1.000 28.19000 ? 206 ALA A CA  1 
ATOM   1539 C C   . ALA A 1 204 ? -28.34900 -9.97600  -9.92700  1.000 28.33000 ? 206 ALA A C   1 
ATOM   1540 O O   . ALA A 1 204 ? -27.49500 -10.74500 -10.37700 1.000 27.96000 ? 206 ALA A O   1 
ATOM   1541 C CB  . ALA A 1 204 ? -29.14900 -7.92500  -11.16000 1.000 28.20000 ? 206 ALA A CB  1 
ATOM   1542 N N   . TRP A 1 205 ? -28.38300 -9.61500  -8.64700  1.000 27.79000 ? 207 TRP A N   1 
ATOM   1543 C CA  . TRP A 1 205 ? -27.38900 -10.06100 -7.68700  1.000 29.90000 ? 207 TRP A CA  1 
ATOM   1544 C C   . TRP A 1 205 ? -27.49900 -11.56900 -7.42600  1.000 29.30000 ? 207 TRP A C   1 
ATOM   1545 O O   . TRP A 1 205 ? -26.48000 -12.24800 -7.22500  1.000 30.91000 ? 207 TRP A O   1 
ATOM   1546 C CB  . TRP A 1 205 ? -27.58100 -9.22300  -6.42200  1.000 28.38000 ? 207 TRP A CB  1 
ATOM   1547 C CG  . TRP A 1 205 ? -26.76800 -9.56600  -5.21900  1.000 31.61000 ? 207 TRP A CG  1 
ATOM   1548 C CD1 . TRP A 1 205 ? -25.46100 -9.21500  -4.96600  1.000 35.40000 ? 207 TRP A CD1 1 
ATOM   1549 C CD2 . TRP A 1 205 ? -27.23100 -10.24800 -4.05400  1.000 32.20000 ? 207 TRP A CD2 1 
ATOM   1550 N NE1 . TRP A 1 205 ? -25.08900 -9.66200  -3.72100  1.000 32.39000 ? 207 TRP A NE1 1 
ATOM   1551 C CE2 . TRP A 1 205 ? -26.15600 -10.30600 -3.14700  1.000 35.47000 ? 207 TRP A CE2 1 
ATOM   1552 C CE3 . TRP A 1 205 ? -28.44700 -10.83900 -3.69900  1.000 35.14000 ? 207 TRP A CE3 1 
ATOM   1553 C CZ2 . TRP A 1 205 ? -26.26700 -10.92900 -1.90900  1.000 38.81000 ? 207 TRP A CZ2 1 
ATOM   1554 C CZ3 . TRP A 1 205 ? -28.55500 -11.45100 -2.46700  1.000 35.78000 ? 207 TRP A CZ3 1 
ATOM   1555 C CH2 . TRP A 1 205 ? -27.47200 -11.49100 -1.58800  1.000 36.12000 ? 207 TRP A CH2 1 
ATOM   1556 N N   . LEU A 1 206 ? -28.71800 -12.12000 -7.43700  1.000 29.75000 ? 208 LEU A N   1 
ATOM   1557 C CA  . LEU A 1 206 ? -28.85300 -13.57700 -7.36200  1.000 29.74000 ? 208 LEU A CA  1 
ATOM   1558 C C   . LEU A 1 206 ? -28.22500 -14.23700 -8.58200  1.000 30.30000 ? 208 LEU A C   1 
ATOM   1559 O O   . LEU A 1 206 ? -27.53500 -15.25500 -8.45800  1.000 28.61000 ? 208 LEU A O   1 
ATOM   1560 C CB  . LEU A 1 206 ? -30.32600 -13.98600 -7.21000  1.000 25.72000 ? 208 LEU A CB  1 
ATOM   1561 C CG  . LEU A 1 206 ? -30.92900 -13.64000 -5.83500  1.000 27.50000 ? 208 LEU A CG  1 
ATOM   1562 C CD1 . LEU A 1 206 ? -32.40700 -14.05300 -5.74700  1.000 25.38000 ? 208 LEU A CD1 1 
ATOM   1563 C CD2 . LEU A 1 206 ? -30.13400 -14.28400 -4.70100  1.000 29.20000 ? 208 LEU A CD2 1 
ATOM   1564 N N   . TYR A 1 207 ? -28.42000 -13.64900 -9.76800  1.000 30.51000 ? 209 TYR A N   1 
ATOM   1565 C CA  . TYR A 1 207 ? -27.75700 -14.17100 -10.96300 1.000 31.77000 ? 209 TYR A CA  1 
ATOM   1566 C C   . TYR A 1 207 ? -26.24200 -14.07900 -10.83100 1.000 33.77000 ? 209 TYR A C   1 
ATOM   1567 O O   . TYR A 1 207 ? -25.51500 -14.98700 -11.25800 1.000 35.69000 ? 209 TYR A O   1 
ATOM   1568 C CB  . TYR A 1 207 ? -28.23200 -13.42000 -12.21100 1.000 31.51000 ? 209 TYR A CB  1 
ATOM   1569 C CG  . TYR A 1 207 ? -29.52600 -13.94500 -12.78700 1.000 32.48000 ? 209 TYR A CG  1 
ATOM   1570 C CD1 . TYR A 1 207 ? -29.61200 -15.25000 -13.26600 1.000 34.61000 ? 209 TYR A CD1 1 
ATOM   1571 C CD2 . TYR A 1 207 ? -30.66400 -13.14500 -12.84900 1.000 34.90000 ? 209 TYR A CD2 1 
ATOM   1572 C CE1 . TYR A 1 207 ? -30.77800 -15.74500 -13.79300 1.000 33.49000 ? 209 TYR A CE1 1 
ATOM   1573 C CE2 . TYR A 1 207 ? -31.85800 -13.64200 -13.37300 1.000 35.71000 ? 209 TYR A CE2 1 
ATOM   1574 C CZ  . TYR A 1 207 ? -31.90300 -14.94400 -13.84600 1.000 35.54000 ? 209 TYR A CZ  1 
ATOM   1575 O OH  . TYR A 1 207 ? -33.07200 -15.44900 -14.37600 1.000 34.83000 ? 209 TYR A OH  1 
ATOM   1576 N N   . ALA A 1 208 ? -25.74500 -12.98900 -10.24000 1.000 35.77000 ? 210 ALA A N   1 
ATOM   1577 C CA  . ALA A 1 208 ? -24.31200 -12.87600 -9.99600  1.000 33.48000 ? 210 ALA A CA  1 
ATOM   1578 C C   . ALA A 1 208 ? -23.82300 -13.98200 -9.06200  1.000 33.72000 ? 210 ALA A C   1 
ATOM   1579 O O   . ALA A 1 208 ? -22.72700 -14.52300 -9.24300  1.000 32.49000 ? 210 ALA A O   1 
ATOM   1580 C CB  . ALA A 1 208 ? -23.99300 -11.49800 -9.42000  1.000 33.96000 ? 210 ALA A CB  1 
ATOM   1581 N N   . ALA A 1 209 ? -24.62100 -14.32600 -8.05000  1.000 33.52000 ? 211 ALA A N   1 
ATOM   1582 C CA  . ALA A 1 209 ? -24.22800 -15.38400 -7.12600  1.000 37.30000 ? 211 ALA A CA  1 
ATOM   1583 C C   . ALA A 1 209 ? -24.12500 -16.73200 -7.84000  1.000 36.33000 ? 211 ALA A C   1 
ATOM   1584 O O   . ALA A 1 209 ? -23.24300 -17.53600 -7.53200  1.000 37.18000 ? 211 ALA A O   1 
ATOM   1585 C CB  . ALA A 1 209 ? -25.22100 -15.45700 -5.96200  1.000 32.64000 ? 211 ALA A CB  1 
ATOM   1586 N N   . VAL A 1 210 ? -25.01000 -16.97900 -8.81300  1.000 36.59000 ? 212 VAL A N   1 
ATOM   1587 C CA  . VAL A 1 210 ? -24.98500 -18.19900 -9.61500  1.000 37.56000 ? 212 VAL A CA  1 
ATOM   1588 C C   . VAL A 1 210 ? -23.83200 -18.19400 -10.61500 1.000 39.93000 ? 212 VAL A C   1 
ATOM   1589 O O   . VAL A 1 210 ? -23.24200 -19.24900 -10.89500 1.000 35.47000 ? 212 VAL A O   1 
ATOM   1590 C CB  . VAL A 1 210 ? -26.33500 -18.37900 -10.33400 1.000 34.11000 ? 212 VAL A CB  1 
ATOM   1591 C CG1 . VAL A 1 210 ? -26.25100 -19.49400 -11.38100 1.000 35.18000 ? 212 VAL A CG1 1 
ATOM   1592 C CG2 . VAL A 1 210 ? -27.44300 -18.66900 -9.31800  1.000 33.92000 ? 212 VAL A CG2 1 
ATOM   1593 N N   . ILE A 1 211 ? -23.50100 -17.03100 -11.18100 1.000 36.22000 ? 213 ILE A N   1 
ATOM   1594 C CA  . ILE A 1 211 ? -22.34200 -16.93100 -12.06700 1.000 37.94000 ? 213 ILE A CA  1 
ATOM   1595 C C   . ILE A 1 211 ? -21.06600 -17.23900 -11.30300 1.000 38.01000 ? 213 ILE A C   1 
ATOM   1596 O O   . ILE A 1 211 ? -20.15700 -17.90800 -11.82100 1.000 35.08000 ? 213 ILE A O   1 
ATOM   1597 C CB  . ILE A 1 211 ? -22.29700 -15.53800 -12.72500 1.000 36.37000 ? 213 ILE A CB  1 
ATOM   1598 C CG1 . ILE A 1 211 ? -23.32400 -15.46700 -13.85600 1.000 36.24000 ? 213 ILE A CG1 1 
ATOM   1599 C CG2 . ILE A 1 211 ? -20.91300 -15.21600 -13.24700 1.000 38.88000 ? 213 ILE A CG2 1 
ATOM   1600 C CD1 . ILE A 1 211 ? -23.74100 -14.07200 -14.23600 1.000 34.26000 ? 213 ILE A CD1 1 
ATOM   1601 N N   . ASN A 1 212 ? -20.96900 -16.75800 -10.06400 1.000 35.60000 ? 214 ASN A N   1 
ATOM   1602 C CA  . ASN A 1 212 ? -20.05100 -17.37400 -9.12600  1.000 43.82000 ? 214 ASN A CA  1 
ATOM   1603 C C   . ASN A 1 212 ? -20.62300 -18.74300 -8.72400  1.000 44.94000 ? 214 ASN A C   1 
ATOM   1604 O O   . ASN A 1 212 ? -21.73500 -19.11400 -9.08800  1.000 47.62000 ? 214 ASN A O   1 
ATOM   1605 C CB  . ASN A 1 212 ? -19.79200 -16.41400 -7.96500  1.000 43.86000 ? 214 ASN A CB  1 
ATOM   1606 C CG  . ASN A 1 212 ? -19.25500 -17.12100 -6.71300  1.000 58.47000 ? 214 ASN A CG  1 
ATOM   1607 O OD1 . ASN A 1 212 ? -18.65000 -18.20300 -6.80000  1.000 50.61000 ? 214 ASN A OD1 1 
ATOM   1608 N ND2 . ASN A 1 212 ? -19.43400 -16.48800 -5.54900  1.000 58.64000 ? 214 ASN A ND2 1 
ATOM   1609 N N   . GLY A 1 213 ? -19.87800 -19.54000 -7.99500  1.000 47.21000 ? 215 GLY A N   1 
ATOM   1610 C CA  . GLY A 1 213 ? -20.40200 -20.88400 -7.82700  1.000 44.58000 ? 215 GLY A CA  1 
ATOM   1611 C C   . GLY A 1 213 ? -21.39500 -21.14800 -6.70800  1.000 49.62000 ? 215 GLY A C   1 
ATOM   1612 O O   . GLY A 1 213 ? -21.21000 -22.13600 -5.98700  1.000 47.09000 ? 215 GLY A O   1 
ATOM   1613 N N   . ASP A 1 214 ? -22.45300 -20.33500 -6.53300  1.000 44.20000 ? 216 ASP A N   1 
ATOM   1614 C CA  . ASP A 1 214 ? -23.37100 -20.53700 -5.40800  1.000 42.26000 ? 216 ASP A CA  1 
ATOM   1615 C C   . ASP A 1 214 ? -24.80400 -20.75500 -5.89100  1.000 43.40000 ? 216 ASP A C   1 
ATOM   1616 O O   . ASP A 1 214 ? -25.45800 -19.81400 -6.35400  1.000 41.15000 ? 216 ASP A O   1 
ATOM   1617 C CB  . ASP A 1 214 ? -23.29500 -19.36900 -4.42500  1.000 45.27000 ? 216 ASP A CB  1 
ATOM   1618 C CG  . ASP A 1 214 ? -23.42100 -19.82800 -2.97900  1.000 51.80000 ? 216 ASP A CG  1 
ATOM   1619 O OD1 . ASP A 1 214 ? -23.83100 -20.99800 -2.78500  1.000 52.94000 ? 216 ASP A OD1 1 
ATOM   1620 O OD2 . ASP A 1 214 ? -23.10300 -19.04500 -2.04900  1.000 51.60000 ? 216 ASP A OD2 1 
ATOM   1621 N N   . ARG A 1 215 ? -25.30800 -21.99000 -5.74500  1.000 38.42000 ? 217 ARG A N   1 
ATOM   1622 C CA  . ARG A 1 215 ? -26.65600 -22.34500 -6.18200  1.000 37.02000 ? 217 ARG A CA  1 
ATOM   1623 C C   . ARG A 1 215 ? -27.58400 -22.75700 -5.04200  1.000 33.42000 ? 217 ARG A C   1 
ATOM   1624 O O   . ARG A 1 215 ? -28.67600 -23.27300 -5.31200  1.000 28.33000 ? 217 ARG A O   1 
ATOM   1625 C CB  . ARG A 1 215 ? -26.60200 -23.47800 -7.21300  1.000 36.21000 ? 217 ARG A CB  1 
ATOM   1626 C CG  . ARG A 1 215 ? -26.01300 -23.10400 -8.54800  1.000 35.61000 ? 217 ARG A CG  1 
ATOM   1627 C CD  . ARG A 1 215 ? -25.92300 -24.31800 -9.46100  1.000 31.24000 ? 217 ARG A CD  1 
ATOM   1628 N NE  . ARG A 1 215 ? -27.21800 -24.96800 -9.66400  1.000 32.41000 ? 217 ARG A NE  1 
ATOM   1629 C CZ  . ARG A 1 215 ? -27.91700 -24.88200 -10.79200 1.000 35.39000 ? 217 ARG A CZ  1 
ATOM   1630 N NH1 . ARG A 1 215 ? -29.07700 -25.49600 -10.90300 1.000 31.12000 ? 217 ARG A NH1 1 
ATOM   1631 N NH2 . ARG A 1 215 ? -27.45900 -24.15500 -11.80600 1.000 37.90000 ? 217 ARG A NH2 1 
ATOM   1632 N N   . TRP A 1 216 ? -27.19700 -22.53000 -3.77900  1.000 33.04000 ? 218 TRP A N   1 
ATOM   1633 C CA  . TRP A 1 216 ? -27.89100 -23.18600 -2.67000  1.000 30.12000 ? 218 TRP A CA  1 
ATOM   1634 C C   . TRP A 1 216 ? -29.34000 -22.72000 -2.51000  1.000 33.65000 ? 218 TRP A C   1 
ATOM   1635 O O   . TRP A 1 216 ? -30.16900 -23.47400 -1.97500  1.000 28.88000 ? 218 TRP A O   1 
ATOM   1636 C CB  . TRP A 1 216 ? -27.11600 -22.97800 -1.37000  1.000 28.61000 ? 218 TRP A CB  1 
ATOM   1637 C CG  . TRP A 1 216 ? -27.07600 -21.57300 -0.82500  1.000 32.64000 ? 218 TRP A CG  1 
ATOM   1638 C CD1 . TRP A 1 216 ? -26.01800 -20.70100 -0.89200  1.000 36.32000 ? 218 TRP A CD1 1 
ATOM   1639 C CD2 . TRP A 1 216 ? -28.09900 -20.89300 -0.06900  1.000 34.03000 ? 218 TRP A CD2 1 
ATOM   1640 N NE1 . TRP A 1 216 ? -26.32700 -19.53000 -0.25300  1.000 34.79000 ? 218 TRP A NE1 1 
ATOM   1641 C CE2 . TRP A 1 216 ? -27.59600 -19.61300 0.25600   1.000 36.63000 ? 218 TRP A CE2 1 
ATOM   1642 C CE3 . TRP A 1 216 ? -29.39800 -21.22700 0.33900   1.000 31.20000 ? 218 TRP A CE3 1 
ATOM   1643 C CZ2 . TRP A 1 216 ? -28.34100 -18.67400 0.97600   1.000 32.74000 ? 218 TRP A CZ2 1 
ATOM   1644 C CZ3 . TRP A 1 216 ? -30.13200 -20.29900 1.06600   1.000 32.65000 ? 218 TRP A CZ3 1 
ATOM   1645 C CH2 . TRP A 1 216 ? -29.60100 -19.03200 1.36900   1.000 39.33000 ? 218 TRP A CH2 1 
ATOM   1646 N N   . PHE A 1 217 ? -29.65700 -21.48500 -2.94200  1.000 26.99000 ? 219 PHE A N   1 
ATOM   1647 C CA  . PHE A 1 217 ? -30.96600 -20.86400 -2.76100  1.000 28.71000 ? 219 PHE A CA  1 
ATOM   1648 C C   . PHE A 1 217 ? -31.95600 -21.18300 -3.86500  1.000 25.02000 ? 219 PHE A C   1 
ATOM   1649 O O   . PHE A 1 217 ? -33.12100 -20.77100 -3.77100  1.000 30.10000 ? 219 PHE A O   1 
ATOM   1650 C CB  . PHE A 1 217 ? -30.81300 -19.33100 -2.69500  1.000 28.31000 ? 219 PHE A CB  1 
ATOM   1651 C CG  . PHE A 1 217 ? -29.90600 -18.78700 -3.76200  1.000 28.96000 ? 219 PHE A CG  1 
ATOM   1652 C CD1 . PHE A 1 217 ? -30.40000 -18.48200 -5.02200  1.000 26.70000 ? 219 PHE A CD1 1 
ATOM   1653 C CD2 . PHE A 1 217 ? -28.55100 -18.64400 -3.53000  1.000 29.40000 ? 219 PHE A CD2 1 
ATOM   1654 C CE1 . PHE A 1 217 ? -29.56000 -18.02300 -6.01500  1.000 26.99000 ? 219 PHE A CE1 1 
ATOM   1655 C CE2 . PHE A 1 217 ? -27.70900 -18.18000 -4.51900  1.000 30.50000 ? 219 PHE A CE2 1 
ATOM   1656 C CZ  . PHE A 1 217 ? -28.21300 -17.87000 -5.76300  1.000 28.95000 ? 219 PHE A CZ  1 
ATOM   1657 N N   . LEU A 1 218 ? -31.51900 -21.82400 -4.93800  1.000 27.35000 ? 220 LEU A N   1 
ATOM   1658 C CA  . LEU A 1 218 ? -32.44000 -22.19500 -5.99600  1.000 28.39000 ? 220 LEU A CA  1 
ATOM   1659 C C   . LEU A 1 218 ? -33.41800 -23.26000 -5.48700  1.000 30.02000 ? 220 LEU A C   1 
ATOM   1660 O O   . LEU A 1 218 ? -33.18900 -23.90500 -4.45800  1.000 26.75000 ? 220 LEU A O   1 
ATOM   1661 C CB  . LEU A 1 218 ? -31.66400 -22.71100 -7.21200  1.000 29.93000 ? 220 LEU A CB  1 
ATOM   1662 C CG  . LEU A 1 218 ? -30.66000 -21.74000 -7.83500  1.000 33.02000 ? 220 LEU A CG  1 
ATOM   1663 C CD1 . LEU A 1 218 ? -29.94400 -22.39900 -9.02200  1.000 30.75000 ? 220 LEU A CD1 1 
ATOM   1664 C CD2 . LEU A 1 218 ? -31.35500 -20.41900 -8.24900  1.000 32.58000 ? 220 LEU A CD2 1 
ATOM   1665 N N   . ASN A 1 219 ? -34.55000 -23.39900 -6.18400  1.000 29.76000 ? 221 ASN A N   1 
ATOM   1666 C CA  . ASN A 1 219 ? -35.49100 -24.48300 -5.90200  1.000 27.86000 ? 221 ASN A CA  1 
ATOM   1667 C C   . ASN A 1 219 ? -36.08800 -24.96900 -7.21700  1.000 30.36000 ? 221 ASN A C   1 
ATOM   1668 O O   . ASN A 1 219 ? -35.78200 -24.44700 -8.29200  1.000 28.34000 ? 221 ASN A O   1 
ATOM   1669 C CB  . ASN A 1 219 ? -36.56400 -24.06200 -4.88500  1.000 26.10000 ? 221 ASN A CB  1 
ATOM   1670 C CG  . ASN A 1 219 ? -37.55300 -23.02200 -5.43700  1.000 30.24000 ? 221 ASN A CG  1 
ATOM   1671 O OD1 . ASN A 1 219 ? -37.68900 -22.82700 -6.64400  1.000 28.68000 ? 221 ASN A OD1 1 
ATOM   1672 N ND2 . ASN A 1 219 ? -38.26500 -22.37000 -4.53400  1.000 30.59000 ? 221 ASN A ND2 1 
ATOM   1673 N N   . ARG A 1 220 ? -36.95900 -25.97500 -7.13900  1.000 32.16000 ? 222 ARG A N   1 
ATOM   1674 C CA  . ARG A 1 220 ? -37.50900 -26.58700 -8.34000  1.000 28.23000 ? 222 ARG A CA  1 
ATOM   1675 C C   . ARG A 1 220 ? -38.78300 -25.91600 -8.82300  1.000 33.02000 ? 222 ARG A C   1 
ATOM   1676 O O   . ARG A 1 220 ? -39.42500 -26.43800 -9.73400  1.000 31.77000 ? 222 ARG A O   1 
ATOM   1677 C CB  . ARG A 1 220 ? -37.76600 -28.08900 -8.10400  1.000 36.16000 ? 222 ARG A CB  1 
ATOM   1678 C CG  . ARG A 1 220 ? -38.81300 -28.36800 -7.04200  1.000 36.89000 ? 222 ARG A CG  1 
ATOM   1679 C CD  . ARG A 1 220 ? -39.03600 -29.86500 -6.77100  1.000 42.21000 ? 222 ARG A CD  1 
ATOM   1680 N NE  . ARG A 1 220 ? -40.13000 -30.02100 -5.81300  1.000 37.46000 ? 222 ARG A NE  1 
ATOM   1681 C CZ  . ARG A 1 220 ? -41.40400 -30.16300 -6.15800  1.000 41.59000 ? 222 ARG A CZ  1 
ATOM   1682 N NH1 . ARG A 1 220 ? -41.74900 -30.18600 -7.44300  1.000 40.28000 ? 222 ARG A NH1 1 
ATOM   1683 N NH2 . ARG A 1 220 ? -42.33800 -30.26500 -5.22100  1.000 43.82000 ? 222 ARG A NH2 1 
ATOM   1684 N N   . PHE A 1 221 ? -39.14900 -24.75600 -8.27400  1.000 31.60000 ? 223 PHE A N   1 
ATOM   1685 C CA  . PHE A 1 221 ? -40.42300 -24.13100 -8.59900  1.000 31.58000 ? 223 PHE A CA  1 
ATOM   1686 C C   . PHE A 1 221 ? -40.27900 -23.03100 -9.64800  1.000 32.33000 ? 223 PHE A C   1 
ATOM   1687 O O   . PHE A 1 221 ? -39.18600 -22.58300 -9.99700  1.000 31.41000 ? 223 PHE A O   1 
ATOM   1688 C CB  . PHE A 1 221 ? -41.08000 -23.56000 -7.33400  1.000 32.64000 ? 223 PHE A CB  1 
ATOM   1689 C CG  . PHE A 1 221 ? -41.53200 -24.61400 -6.36900  1.000 34.64000 ? 223 PHE A CG  1 
ATOM   1690 C CD1 . PHE A 1 221 ? -42.16800 -25.75800 -6.82700  1.000 34.49000 ? 223 PHE A CD1 1 
ATOM   1691 C CD2 . PHE A 1 221 ? -41.30300 -24.47500 -5.01400  1.000 35.85000 ? 223 PHE A CD2 1 
ATOM   1692 C CE1 . PHE A 1 221 ? -42.58500 -26.73400 -5.94700  1.000 36.98000 ? 223 PHE A CE1 1 
ATOM   1693 C CE2 . PHE A 1 221 ? -41.71300 -25.45500 -4.12800  1.000 37.05000 ? 223 PHE A CE2 1 
ATOM   1694 C CZ  . PHE A 1 221 ? -42.35300 -26.58600 -4.59300  1.000 35.13000 ? 223 PHE A CZ  1 
ATOM   1695 N N   . THR A 1 222 ? -41.42400 -22.60100 -10.15600 1.000 33.65000 ? 224 THR A N   1 
ATOM   1696 C CA  . THR A 1 222 ? -41.52000 -21.37800 -10.93200 1.000 30.61000 ? 224 THR A CA  1 
ATOM   1697 C C   . THR A 1 222 ? -42.68200 -20.56300 -10.38600 1.000 31.49000 ? 224 THR A C   1 
ATOM   1698 O O   . THR A 1 222 ? -43.30800 -20.91400 -9.37900  1.000 32.91000 ? 224 THR A O   1 
ATOM   1699 C CB  . THR A 1 222 ? -41.67200 -21.67600 -12.43000 1.000 34.03000 ? 224 THR A CB  1 
ATOM   1700 O OG1 . THR A 1 222 ? -41.37700 -20.49000 -13.18600 1.000 35.45000 ? 224 THR A OG1 1 
ATOM   1701 C CG2 . THR A 1 222 ? -43.08400 -22.20900 -12.76200 1.000 31.83000 ? 224 THR A CG2 1 
ATOM   1702 N N   . THR A 1 223 ? -42.95700 -19.44300 -11.04300 1.000 31.25000 ? 225 THR A N   1 
ATOM   1703 C CA  . THR A 1 223 ? -44.03300 -18.57900 -10.59700 1.000 28.85000 ? 225 THR A CA  1 
ATOM   1704 C C   . THR A 1 223 ? -44.51400 -17.78800 -11.79700 1.000 30.62000 ? 225 THR A C   1 
ATOM   1705 O O   . THR A 1 223 ? -43.76900 -17.58600 -12.75500 1.000 34.00000 ? 225 THR A O   1 
ATOM   1706 C CB  . THR A 1 223 ? -43.57400 -17.63100 -9.47700  1.000 30.39000 ? 225 THR A CB  1 
ATOM   1707 O OG1 . THR A 1 223 ? -44.67700 -16.81900 -9.05300  1.000 26.24000 ? 225 THR A OG1 1 
ATOM   1708 C CG2 . THR A 1 223 ? -42.42800 -16.73000 -9.97300  1.000 27.16000 ? 225 THR A CG2 1 
ATOM   1709 N N   . THR A 1 224 ? -45.77200 -17.37900 -11.75900 1.000 29.02000 ? 226 THR A N   1 
ATOM   1710 C CA  . THR A 1 224 ? -46.17200 -16.35100 -12.70000 1.000 31.76000 ? 226 THR A CA  1 
ATOM   1711 C C   . THR A 1 224 ? -45.65100 -14.99900 -12.21700 1.000 31.08000 ? 226 THR A C   1 
ATOM   1712 O O   . THR A 1 224 ? -45.32400 -14.81900 -11.03900 1.000 26.15000 ? 226 THR A O   1 
ATOM   1713 C CB  . THR A 1 224 ? -47.69100 -16.29900 -12.83400 1.000 28.65000 ? 226 THR A CB  1 
ATOM   1714 O OG1 . THR A 1 224 ? -48.24500 -15.81200 -11.60800 1.000 28.72000 ? 226 THR A OG1 1 
ATOM   1715 C CG2 . THR A 1 224 ? -48.27000 -17.70300 -13.14000 1.000 30.10000 ? 226 THR A CG2 1 
ATOM   1716 N N   . LEU A 1 225 ? -45.59400 -14.03600 -13.14100 1.000 30.80000 ? 227 LEU A N   1 
ATOM   1717 C CA  . LEU A 1 225 ? -45.19600 -12.68600 -12.75400 1.000 32.03000 ? 227 LEU A CA  1 
ATOM   1718 C C   . LEU A 1 225 ? -46.17900 -12.08000 -11.75800 1.000 29.22000 ? 227 LEU A C   1 
ATOM   1719 O O   . LEU A 1 225 ? -45.77100 -11.39400 -10.81100 1.000 29.91000 ? 227 LEU A O   1 
ATOM   1720 C CB  . LEU A 1 225 ? -45.07000 -11.79600 -13.99200 1.000 35.72000 ? 227 LEU A CB  1 
ATOM   1721 C CG  . LEU A 1 225 ? -44.47900 -10.40300 -13.77900 1.000 36.29000 ? 227 LEU A CG  1 
ATOM   1722 C CD1 . LEU A 1 225 ? -43.09200 -10.50500 -13.17400 1.000 35.74000 ? 227 LEU A CD1 1 
ATOM   1723 C CD2 . LEU A 1 225 ? -44.44300 -9.62600  -15.09500 1.000 38.53000 ? 227 LEU A CD2 1 
ATOM   1724 N N   . ASN A 1 226 ? -47.48000 -12.30400 -11.94600 1.000 28.64000 ? 228 ASN A N   1 
ATOM   1725 C CA  . ASN A 1 226 ? -48.41600 -11.66200 -11.02400 1.000 32.92000 ? 228 ASN A CA  1 
ATOM   1726 C C   . ASN A 1 226 ? -48.33000 -12.27600 -9.63700  1.000 31.55000 ? 228 ASN A C   1 
ATOM   1727 O O   . ASN A 1 226 ? -48.35100 -11.55100 -8.63400  1.000 29.69000 ? 228 ASN A O   1 
ATOM   1728 C CB  . ASN A 1 226 ? -49.85500 -11.72800 -11.52900 1.000 32.02000 ? 228 ASN A CB  1 
ATOM   1729 C CG  . ASN A 1 226 ? -50.74500 -10.73500 -10.80000 1.000 38.38000 ? 228 ASN A CG  1 
ATOM   1730 O OD1 . ASN A 1 226 ? -50.58300 -9.50100  -10.92900 1.000 44.08000 ? 228 ASN A OD1 1 
ATOM   1731 N ND2 . ASN A 1 226 ? -51.64200 -11.25100 -9.98200  1.000 38.13000 ? 228 ASN A ND2 1 
ATOM   1732 N N   . ASP A 1 227 ? -48.23100 -13.61300 -9.55800  1.000 29.83000 ? 229 ASP A N   1 
ATOM   1733 C CA  . ASP A 1 227 ? -48.05800 -14.26700 -8.26600  1.000 28.62000 ? 229 ASP A CA  1 
ATOM   1734 C C   . ASP A 1 227 ? -46.77000 -13.81900 -7.59100  1.000 27.91000 ? 229 ASP A C   1 
ATOM   1735 O O   . ASP A 1 227 ? -46.74700 -13.59700 -6.37400  1.000 27.34000 ? 229 ASP A O   1 
ATOM   1736 C CB  . ASP A 1 227 ? -48.06600 -15.78800 -8.43300  1.000 28.53000 ? 229 ASP A CB  1 
ATOM   1737 C CG  . ASP A 1 227 ? -49.48000 -16.34600 -8.60500  1.000 30.50000 ? 229 ASP A CG  1 
ATOM   1738 O OD1 . ASP A 1 227 ? -50.44500 -15.57000 -8.45000  1.000 31.99000 ? 229 ASP A OD1 1 
ATOM   1739 O OD2 . ASP A 1 227 ? -49.60600 -17.54800 -8.87900  1.000 32.20000 ? 229 ASP A OD2 1 
ATOM   1740 N N   . PHE A 1 228 ? -45.67700 -13.71300 -8.35300  1.000 26.71000 ? 230 PHE A N   1 
ATOM   1741 C CA  . PHE A 1 228 ? -44.45100 -13.16900 -7.76700  1.000 29.25000 ? 230 PHE A CA  1 
ATOM   1742 C C   . PHE A 1 228 ? -44.69800 -11.79000 -7.15400  1.000 29.14000 ? 230 PHE A C   1 
ATOM   1743 O O   . PHE A 1 228 ? -44.34600 -11.54300 -5.99300  1.000 26.95000 ? 230 PHE A O   1 
ATOM   1744 C CB  . PHE A 1 228 ? -43.32600 -13.08900 -8.79900  1.000 25.92000 ? 230 PHE A CB  1 
ATOM   1745 C CG  . PHE A 1 228 ? -42.09400 -12.40600 -8.26200  1.000 27.21000 ? 230 PHE A CG  1 
ATOM   1746 C CD1 . PHE A 1 228 ? -41.24300 -13.08100 -7.39400  1.000 25.84000 ? 230 PHE A CD1 1 
ATOM   1747 C CD2 . PHE A 1 228 ? -41.84100 -11.06300 -8.55200  1.000 28.76000 ? 230 PHE A CD2 1 
ATOM   1748 C CE1 . PHE A 1 228 ? -40.11000 -12.43100 -6.85900  1.000 29.18000 ? 230 PHE A CE1 1 
ATOM   1749 C CE2 . PHE A 1 228 ? -40.73500 -10.41400 -8.02400  1.000 32.79000 ? 230 PHE A CE2 1 
ATOM   1750 C CZ  . PHE A 1 228 ? -39.86400 -11.10600 -7.18400  1.000 31.39000 ? 230 PHE A CZ  1 
ATOM   1751 N N   . ASN A 1 229 ? -45.33800 -10.88600 -7.90800  1.000 28.56000 ? 231 ASN A N   1 
ATOM   1752 C CA  . ASN A 1 229 ? -45.51100 -9.51800  -7.41600  1.000 28.03000 ? 231 ASN A CA  1 
ATOM   1753 C C   . ASN A 1 229 ? -46.44000 -9.46100  -6.20700  1.000 27.48000 ? 231 ASN A C   1 
ATOM   1754 O O   . ASN A 1 229 ? -46.15400 -8.74600  -5.23800  1.000 28.87000 ? 231 ASN A O   1 
ATOM   1755 C CB  . ASN A 1 229 ? -46.01400 -8.60800  -8.53900  1.000 30.95000 ? 231 ASN A CB  1 
ATOM   1756 C CG  . ASN A 1 229 ? -44.90800 -8.19900  -9.48900  1.000 30.49000 ? 231 ASN A CG  1 
ATOM   1757 O OD1 . ASN A 1 229 ? -43.76900 -7.98900  -9.07700  1.000 30.90000 ? 231 ASN A OD1 1 
ATOM   1758 N ND2 . ASN A 1 229 ? -45.23000 -8.09400  -10.76700 1.000 33.03000 ? 231 ASN A ND2 1 
ATOM   1759 N N   . LEU A 1 230 ? -47.54900 -10.21500 -6.22700  1.000 28.32000 ? 232 LEU A N   1 
ATOM   1760 C CA  . LEU A 1 230 ? -48.42400 -10.28000 -5.05500  1.000 28.15000 ? 232 LEU A CA  1 
ATOM   1761 C C   . LEU A 1 230 ? -47.66500 -10.70100 -3.79300  1.000 27.63000 ? 232 LEU A C   1 
ATOM   1762 O O   . LEU A 1 230 ? -47.90400 -10.15300 -2.71000  1.000 29.81000 ? 232 LEU A O   1 
ATOM   1763 C CB  . LEU A 1 230 ? -49.60200 -11.23500 -5.31500  1.000 30.47000 ? 232 LEU A CB  1 
ATOM   1764 C CG  . LEU A 1 230 ? -50.70400 -10.82100 -6.31000  1.000 27.81000 ? 232 LEU A CG  1 
ATOM   1765 C CD1 . LEU A 1 230 ? -51.69100 -11.96600 -6.51400  1.000 28.37000 ? 232 LEU A CD1 1 
ATOM   1766 C CD2 . LEU A 1 230 ? -51.44700 -9.51800  -5.89800  1.000 28.27000 ? 232 LEU A CD2 1 
ATOM   1767 N N   . VAL A 1 231 ? -46.73500 -11.65600 -3.90800  1.000 26.37000 ? 233 VAL A N   1 
ATOM   1768 C CA  . VAL A 1 231 ? -45.95000 -12.06800 -2.73800  1.000 27.31000 ? 233 VAL A CA  1 
ATOM   1769 C C   . VAL A 1 231 ? -44.90700 -11.01100 -2.37400  1.000 27.30000 ? 233 VAL A C   1 
ATOM   1770 O O   . VAL A 1 231 ? -44.77500 -10.61600 -1.20600  1.000 25.63000 ? 233 VAL A O   1 
ATOM   1771 C CB  . VAL A 1 231 ? -45.28100 -13.42800 -2.98400  1.000 28.32000 ? 233 VAL A CB  1 
ATOM   1772 C CG1 . VAL A 1 231 ? -44.29700 -13.73900 -1.84800  1.000 29.26000 ? 233 VAL A CG1 1 
ATOM   1773 C CG2 . VAL A 1 231 ? -46.33900 -14.52300 -3.08200  1.000 27.59000 ? 233 VAL A CG2 1 
ATOM   1774 N N   . ALA A 1 232 ? -44.12600 -10.56600 -3.36000  1.000 27.76000 ? 234 ALA A N   1 
ATOM   1775 C CA  . ALA A 1 232 ? -42.98800 -9.69100  -3.08100  1.000 29.37000 ? 234 ALA A CA  1 
ATOM   1776 C C   . ALA A 1 232 ? -43.43200 -8.37300  -2.46200  1.000 29.89000 ? 234 ALA A C   1 
ATOM   1777 O O   . ALA A 1 232 ? -42.76700 -7.84200  -1.56500  1.000 31.10000 ? 234 ALA A O   1 
ATOM   1778 C CB  . ALA A 1 232 ? -42.19000 -9.43300  -4.36400  1.000 28.63000 ? 234 ALA A CB  1 
ATOM   1779 N N   . MET A 1 233 ? -44.55700 -7.82700  -2.92200  1.000 29.53000 ? 235 MET A N   1 
ATOM   1780 C CA  . MET A 1 233 ? -45.02200 -6.57100  -2.35400  1.000 31.04000 ? 235 MET A CA  1 
ATOM   1781 C C   . MET A 1 233 ? -45.35300 -6.70000  -0.87600  1.000 30.37000 ? 235 MET A C   1 
ATOM   1782 O O   . MET A 1 233 ? -45.29900 -5.70300  -0.15800  1.000 31.15000 ? 235 MET A O   1 
ATOM   1783 C CB  . MET A 1 233 ? -46.21900 -6.05700  -3.14100  1.000 33.46000 ? 235 MET A CB  1 
ATOM   1784 C CG  . MET A 1 233 ? -45.83100 -5.65600  -4.54800  1.000 37.57000 ? 235 MET A CG  1 
ATOM   1785 S SD  . MET A 1 233 ? -47.09100 -4.70200  -5.39800  1.000 57.35000 ? 235 MET A SD  1 
ATOM   1786 C CE  . MET A 1 233 ? -46.93800 -5.41500  -7.03000  1.000 34.86000 ? 235 MET A CE  1 
ATOM   1787 N N   . LYS A 1 234 ? -45.64400 -7.90900  -0.38700  1.000 31.09000 ? 236 LYS A N   1 
ATOM   1788 C CA  . LYS A 1 234 ? -45.85700 -8.05900  1.05100   1.000 31.47000 ? 236 LYS A CA  1 
ATOM   1789 C C   . LYS A 1 234 ? -44.57200 -7.94000  1.85500   1.000 27.27000 ? 236 LYS A C   1 
ATOM   1790 O O   . LYS A 1 234 ? -44.63500 -7.87700  3.08800   1.000 29.63000 ? 236 LYS A O   1 
ATOM   1791 C CB  . LYS A 1 234 ? -46.51700 -9.40200  1.35600   1.000 27.39000 ? 236 LYS A CB  1 
ATOM   1792 C CG  . LYS A 1 234 ? -47.94900 -9.45700  0.89300   1.000 32.17000 ? 236 LYS A CG  1 
ATOM   1793 C CD  . LYS A 1 234 ? -48.51800 -10.85800 0.94900   1.000 32.35000 ? 236 LYS A CD  1 
ATOM   1794 C CE  . LYS A 1 234 ? -49.76800 -10.92400 0.10000   1.000 33.76000 ? 236 LYS A CE  1 
ATOM   1795 N NZ  . LYS A 1 234 ? -49.93800 -12.31800 -0.38100  1.000 38.98000 ? 236 LYS A NZ  1 
ATOM   1796 N N   . TYR A 1 235 ? -43.41800 -7.94600  1.20500   1.000 26.21000 ? 237 TYR A N   1 
ATOM   1797 C CA  . TYR A 1 235 ? -42.14800 -7.68500  1.87400   1.000 29.28000 ? 237 TYR A CA  1 
ATOM   1798 C C   . TYR A 1 235 ? -41.59100 -6.31100  1.52900   1.000 30.67000 ? 237 TYR A C   1 
ATOM   1799 O O   . TYR A 1 235 ? -40.39900 -6.05800  1.76100   1.000 26.45000 ? 237 TYR A O   1 
ATOM   1800 C CB  . TYR A 1 235 ? -41.11600 -8.75100  1.50700   1.000 26.22000 ? 237 TYR A CB  1 
ATOM   1801 C CG  . TYR A 1 235 ? -41.52300 -10.18200 1.82200   1.000 27.23000 ? 237 TYR A CG  1 
ATOM   1802 C CD1 . TYR A 1 235 ? -42.26600 -10.93400 0.92200   1.000 28.30000 ? 237 TYR A CD1 1 
ATOM   1803 C CD2 . TYR A 1 235 ? -41.11100 -10.79300 3.00400   1.000 26.40000 ? 237 TYR A CD2 1 
ATOM   1804 C CE1 . TYR A 1 235 ? -42.61400 -12.26700 1.20400   1.000 25.44000 ? 237 TYR A CE1 1 
ATOM   1805 C CE2 . TYR A 1 235 ? -41.44400 -12.10100 3.29200   1.000 27.93000 ? 237 TYR A CE2 1 
ATOM   1806 C CZ  . TYR A 1 235 ? -42.20200 -12.83600 2.39900   1.000 29.67000 ? 237 TYR A CZ  1 
ATOM   1807 O OH  . TYR A 1 235 ? -42.51100 -14.15400 2.71200   1.000 29.39000 ? 237 TYR A OH  1 
ATOM   1808 N N   . ASN A 1 236 ? -42.41000 -5.44400  0.93600   1.000 32.41000 ? 238 ASN A N   1 
ATOM   1809 C CA  . ASN A 1 236 ? -42.00600 -4.09700  0.55300   1.000 32.62000 ? 238 ASN A CA  1 
ATOM   1810 C C   . ASN A 1 236 ? -41.02000 -4.10400  -0.60400  1.000 32.97000 ? 238 ASN A C   1 
ATOM   1811 O O   . ASN A 1 236 ? -40.15000 -3.23600  -0.68600  1.000 28.48000 ? 238 ASN A O   1 
ATOM   1812 C CB  . ASN A 1 236 ? -41.42400 -3.33000  1.73800   1.000 36.66000 ? 238 ASN A CB  1 
ATOM   1813 C CG  . ASN A 1 236 ? -42.49000 -2.77000  2.62100   1.000 46.28000 ? 238 ASN A CG  1 
ATOM   1814 O OD1 . ASN A 1 236 ? -43.34800 -2.01200  2.16200   1.000 48.88000 ? 238 ASN A OD1 1 
ATOM   1815 N ND2 . ASN A 1 236 ? -42.46600 -3.14700  3.89700   1.000 46.55000 ? 238 ASN A ND2 1 
ATOM   1816 N N   . TYR A 1 237 ? -41.14400 -5.09100  -1.48800  1.000 29.11000 ? 239 TYR A N   1 
ATOM   1817 C CA  . TYR A 1 237 ? -40.37700 -5.14000  -2.72200  1.000 28.56000 ? 239 TYR A CA  1 
ATOM   1818 C C   . TYR A 1 237 ? -41.10800 -4.37300  -3.81400  1.000 32.17000 ? 239 TYR A C   1 
ATOM   1819 O O   . TYR A 1 237 ? -42.33900 -4.43600  -3.90500  1.000 31.99000 ? 239 TYR A O   1 
ATOM   1820 C CB  . TYR A 1 237 ? -40.15800 -6.59500  -3.15200  1.000 26.97000 ? 239 TYR A CB  1 
ATOM   1821 C CG  . TYR A 1 237 ? -38.88500 -7.16900  -2.60800  1.000 25.26000 ? 239 TYR A CG  1 
ATOM   1822 C CD1 . TYR A 1 237 ? -38.63600 -7.16700  -1.24700  1.000 25.47000 ? 239 TYR A CD1 1 
ATOM   1823 C CD2 . TYR A 1 237 ? -37.92000 -7.68800  -3.45500  1.000 24.08000 ? 239 TYR A CD2 1 
ATOM   1824 C CE1 . TYR A 1 237 ? -37.46000 -7.67800  -0.74400  1.000 29.59000 ? 239 TYR A CE1 1 
ATOM   1825 C CE2 . TYR A 1 237 ? -36.75300 -8.19700  -2.96700  1.000 27.90000 ? 239 TYR A CE2 1 
ATOM   1826 C CZ  . TYR A 1 237 ? -36.52400 -8.19100  -1.61100  1.000 29.03000 ? 239 TYR A CZ  1 
ATOM   1827 O OH  . TYR A 1 237 ? -35.34700 -8.69100  -1.12800  1.000 29.45000 ? 239 TYR A OH  1 
ATOM   1828 N N   . GLU A 1 238 ? -40.34400 -3.63600  -4.62300  1.000 31.86000 ? 240 GLU A N   1 
ATOM   1829 C CA  . GLU A 1 238 ? -40.90200 -2.95900  -5.78500  1.000 31.86000 ? 240 GLU A CA  1 
ATOM   1830 C C   . GLU A 1 238 ? -41.50200 -3.98500  -6.74200  1.000 31.17000 ? 240 GLU A C   1 
ATOM   1831 O O   . GLU A 1 238 ? -40.93800 -5.06900  -6.92200  1.000 30.83000 ? 240 GLU A O   1 
ATOM   1832 C CB  . GLU A 1 238 ? -39.82500 -2.16200  -6.53000  1.000 31.15000 ? 240 GLU A CB  1 
ATOM   1833 C CG  . GLU A 1 238 ? -39.59400 -0.75300  -6.02600  1.000 39.74000 ? 240 GLU A CG  1 
ATOM   1834 C CD  . GLU A 1 238 ? -40.73400 0.18200   -6.39800  1.000 42.67000 ? 240 GLU A CD  1 
ATOM   1835 O OE1 . GLU A 1 238 ? -41.45600 0.61600   -5.47400  1.000 39.98000 ? 240 GLU A OE1 1 
ATOM   1836 O OE2 . GLU A 1 238 ? -40.91100 0.46900   -7.60600  1.000 41.96000 ? 240 GLU A OE2 1 
ATOM   1837 N N   . PRO A 1 239 ? -42.62000 -3.67300  -7.39200  1.000 35.75000 ? 241 PRO A N   1 
ATOM   1838 C CA  . PRO A 1 239 ? -43.13900 -4.59300  -8.41000  1.000 33.97000 ? 241 PRO A CA  1 
ATOM   1839 C C   . PRO A 1 239 ? -42.10500 -4.81200  -9.50300  1.000 34.90000 ? 241 PRO A C   1 
ATOM   1840 O O   . PRO A 1 239 ? -41.33300 -3.91300  -9.84900  1.000 31.87000 ? 241 PRO A O   1 
ATOM   1841 C CB  . PRO A 1 239 ? -44.39400 -3.88700  -8.94700  1.000 34.89000 ? 241 PRO A CB  1 
ATOM   1842 C CG  . PRO A 1 239 ? -44.44000 -2.54200  -8.30500  1.000 37.32000 ? 241 PRO A CG  1 
ATOM   1843 C CD  . PRO A 1 239 ? -43.53900 -2.55800  -7.10500  1.000 36.07000 ? 241 PRO A CD  1 
ATOM   1844 N N   . LEU A 1 240 ? -42.07500 -6.03700  -10.01300 1.000 31.00000 ? 242 LEU A N   1 
ATOM   1845 C CA  . LEU A 1 240 ? -41.23100 -6.41000  -11.14000 1.000 31.32000 ? 242 LEU A CA  1 
ATOM   1846 C C   . LEU A 1 240 ? -42.06500 -6.30300  -12.41500 1.000 35.29000 ? 242 LEU A C   1 
ATOM   1847 O O   . LEU A 1 240 ? -43.11700 -6.94300  -12.52400 1.000 35.80000 ? 242 LEU A O   1 
ATOM   1848 C CB  . LEU A 1 240 ? -40.69600 -7.83400  -10.95100 1.000 29.23000 ? 242 LEU A CB  1 
ATOM   1849 C CG  . LEU A 1 240 ? -39.59100 -8.33900  -11.88300 1.000 29.93000 ? 242 LEU A CG  1 
ATOM   1850 C CD1 . LEU A 1 240 ? -38.20600 -7.71600  -11.55000 1.000 27.90000 ? 242 LEU A CD1 1 
ATOM   1851 C CD2 . LEU A 1 240 ? -39.53700 -9.87400  -11.87900 1.000 28.47000 ? 242 LEU A CD2 1 
ATOM   1852 N N   . THR A 1 241 ? -41.60400 -5.49700  -13.36700 1.000 34.34000 ? 243 THR A N   1 
ATOM   1853 C CA  . THR A 1 241 ? -42.30500 -5.26300  -14.62000 1.000 34.03000 ? 243 THR A CA  1 
ATOM   1854 C C   . THR A 1 241 ? -41.74800 -6.15400  -15.72700 1.000 34.05000 ? 243 THR A C   1 
ATOM   1855 O O   . THR A 1 241 ? -40.69300 -6.78100  -15.59500 1.000 34.09000 ? 243 THR A O   1 
ATOM   1856 C CB  . THR A 1 241 ? -42.18300 -3.78900  -15.04400 1.000 35.41000 ? 243 THR A CB  1 
ATOM   1857 O OG1 . THR A 1 241 ? -40.81400 -3.51100  -15.37400 1.000 33.08000 ? 243 THR A OG1 1 
ATOM   1858 C CG2 . THR A 1 241 ? -42.64900 -2.84600  -13.94000 1.000 32.89000 ? 243 THR A CG2 1 
ATOM   1859 N N   . GLN A 1 242 ? -42.46000 -6.16200  -16.85700 1.000 37.27000 ? 244 GLN A N   1 
ATOM   1860 C CA  . GLN A 1 242 ? -41.98400 -6.89100  -18.02800 1.000 38.92000 ? 244 GLN A CA  1 
ATOM   1861 C C   . GLN A 1 242 ? -40.67200 -6.31400  -18.53800 1.000 37.59000 ? 244 GLN A C   1 
ATOM   1862 O O   . GLN A 1 242 ? -39.79700 -7.05600  -19.00600 1.000 37.58000 ? 244 GLN A O   1 
ATOM   1863 C CB  . GLN A 1 242 ? -43.04600 -6.87000  -19.13100 1.000 38.54000 ? 244 GLN A CB  1 
ATOM   1864 C CG  . GLN A 1 242 ? -42.78700 -7.89100  -20.22700 1.000 39.14000 ? 244 GLN A CG  1 
ATOM   1865 C CD  . GLN A 1 242 ? -42.45700 -9.26000  -19.66300 1.000 41.16000 ? 244 GLN A CD  1 
ATOM   1866 O OE1 . GLN A 1 242 ? -43.23000 -9.82900  -18.88300 1.000 44.80000 ? 244 GLN A OE1 1 
ATOM   1867 N NE2 . GLN A 1 242 ? -41.31500 -9.80300  -20.06100 1.000 38.79000 ? 244 GLN A NE2 1 
ATOM   1868 N N   . ASP A 1 243 ? -40.51600 -4.98900  -18.45700 1.000 37.72000 ? 245 ASP A N   1 
ATOM   1869 C CA  . ASP A 1 243 ? -39.23000 -4.36700  -18.75000 1.000 36.78000 ? 245 ASP A CA  1 
ATOM   1870 C C   . ASP A 1 243 ? -38.12800 -4.99500  -17.90800 1.000 36.51000 ? 245 ASP A C   1 
ATOM   1871 O O   . ASP A 1 243 ? -37.04900 -5.34100  -18.41000 1.000 34.07000 ? 245 ASP A O   1 
ATOM   1872 C CB  . ASP A 1 243 ? -39.30200 -2.85700  -18.47700 1.000 38.80000 ? 245 ASP A CB  1 
ATOM   1873 C CG  . ASP A 1 243 ? -39.97200 -2.08100  -19.60000 1.000 43.80000 ? 245 ASP A CG  1 
ATOM   1874 O OD1 . ASP A 1 243 ? -40.80400 -2.66000  -20.32300 1.000 47.10000 ? 245 ASP A OD1 1 
ATOM   1875 O OD2 . ASP A 1 243 ? -39.68200 -0.87300  -19.74100 1.000 46.34000 ? 245 ASP A OD2 1 
ATOM   1876 N N   . HIS A 1 244 ? -38.37400 -5.11400  -16.60600 1.000 33.38000 ? 246 HIS A N   1 
ATOM   1877 C CA  . HIS A 1 244 ? -37.37200 -5.70800  -15.73100 1.000 34.56000 ? 246 HIS A CA  1 
ATOM   1878 C C   . HIS A 1 244 ? -37.04700 -7.13600  -16.16900 1.000 33.72000 ? 246 HIS A C   1 
ATOM   1879 O O   . HIS A 1 244 ? -35.87700 -7.53600  -16.18600 1.000 31.34000 ? 246 HIS A O   1 
ATOM   1880 C CB  . HIS A 1 244 ? -37.86300 -5.66600  -14.28500 1.000 30.78000 ? 246 HIS A CB  1 
ATOM   1881 C CG  . HIS A 1 244 ? -38.00000 -4.28200  -13.72700 1.000 35.92000 ? 246 HIS A CG  1 
ATOM   1882 N ND1 . HIS A 1 244 ? -38.74700 -4.00500  -12.60100 1.000 33.65000 ? 246 HIS A ND1 1 
ATOM   1883 C CD2 . HIS A 1 244 ? -37.48600 -3.09500  -14.13800 1.000 33.52000 ? 246 HIS A CD2 1 
ATOM   1884 C CE1 . HIS A 1 244 ? -38.69100 -2.70900  -12.34800 1.000 35.51000 ? 246 HIS A CE1 1 
ATOM   1885 N NE2 . HIS A 1 244 ? -37.92500 -2.13800  -13.26000 1.000 33.35000 ? 246 HIS A NE2 1 
ATOM   1886 N N   . VAL A 1 245 ? -38.06900 -7.89200  -16.58600 1.000 33.75000 ? 247 VAL A N   1 
ATOM   1887 C CA  . VAL A 1 245 ? -37.87000 -9.26800  -17.03700 1.000 37.23000 ? 247 VAL A CA  1 
ATOM   1888 C C   . VAL A 1 245 ? -37.03400 -9.30200  -18.31400 1.000 39.36000 ? 247 VAL A C   1 
ATOM   1889 O O   . VAL A 1 245 ? -36.11100 -10.11200 -18.44200 1.000 35.46000 ? 247 VAL A O   1 
ATOM   1890 C CB  . VAL A 1 245 ? -39.23600 -9.95500  -17.22400 1.000 37.38000 ? 247 VAL A CB  1 
ATOM   1891 C CG1 . VAL A 1 245 ? -39.07900 -11.34400 -17.83900 1.000 37.12000 ? 247 VAL A CG1 1 
ATOM   1892 C CG2 . VAL A 1 245 ? -39.98000 -10.03200 -15.88300 1.000 33.90000 ? 247 VAL A CG2 1 
ATOM   1893 N N   . ASP A 1 246 ? -37.31800 -8.40000  -19.26400 1.000 39.73000 ? 248 ASP A N   1 
ATOM   1894 C CA  . ASP A 1 246 ? -36.51600 -8.33800  -20.48600 1.000 40.28000 ? 248 ASP A CA  1 
ATOM   1895 C C   . ASP A 1 246 ? -35.06900 -7.98600  -20.17800 1.000 37.72000 ? 248 ASP A C   1 
ATOM   1896 O O   . ASP A 1 246 ? -34.13900 -8.56800  -20.75000 1.000 39.18000 ? 248 ASP A O   1 
ATOM   1897 C CB  . ASP A 1 246 ? -37.09400 -7.30100  -21.44900 1.000 42.66000 ? 248 ASP A CB  1 
ATOM   1898 C CG  . ASP A 1 246 ? -38.48000 -7.64700  -21.92400 1.000 42.93000 ? 248 ASP A CG  1 
ATOM   1899 O OD1 . ASP A 1 246 ? -38.90800 -8.81300  -21.76200 1.000 46.37000 ? 248 ASP A OD1 1 
ATOM   1900 O OD2 . ASP A 1 246 ? -39.14900 -6.74500  -22.46700 1.000 42.33000 ? 248 ASP A OD2 1 
ATOM   1901 N N   . ILE A 1 247 ? -34.86500 -7.01700  -19.28100 1.000 37.12000 ? 249 ILE A N   1 
ATOM   1902 C CA  . ILE A 1 247 ? -33.53000 -6.55600  -18.92400 1.000 39.84000 ? 249 ILE A CA  1 
ATOM   1903 C C   . ILE A 1 247 ? -32.70000 -7.68400  -18.31700 1.000 38.15000 ? 249 ILE A C   1 
ATOM   1904 O O   . ILE A 1 247 ? -31.47300 -7.72600  -18.47900 1.000 35.80000 ? 249 ILE A O   1 
ATOM   1905 C CB  . ILE A 1 247 ? -33.67100 -5.34200  -17.98100 1.000 38.15000 ? 249 ILE A CB  1 
ATOM   1906 C CG1 . ILE A 1 247 ? -33.79900 -4.04800  -18.80000 1.000 44.45000 ? 249 ILE A CG1 1 
ATOM   1907 C CG2 . ILE A 1 247 ? -32.53600 -5.26300  -17.00800 1.000 38.18000 ? 249 ILE A CG2 1 
ATOM   1908 C CD1 . ILE A 1 247 ? -34.29400 -2.83700  -17.98900 1.000 49.31000 ? 249 ILE A CD1 1 
ATOM   1909 N N   . LEU A 1 248 ? -33.34400 -8.61900  -17.62300 1.000 38.34000 ? 250 LEU A N   1 
ATOM   1910 C CA  . LEU A 1 248 ? -32.61200 -9.72500  -17.02000 1.000 38.09000 ? 250 LEU A CA  1 
ATOM   1911 C C   . LEU A 1 248 ? -32.34100 -10.85600 -18.00600 1.000 37.83000 ? 250 LEU A C   1 
ATOM   1912 O O   . LEU A 1 248 ? -31.60800 -11.78900 -17.66300 1.000 37.79000 ? 250 LEU A O   1 
ATOM   1913 C CB  . LEU A 1 248 ? -33.38400 -10.26400 -15.81200 1.000 33.79000 ? 250 LEU A CB  1 
ATOM   1914 C CG  . LEU A 1 248 ? -33.48300 -9.36300  -14.58000 1.000 31.98000 ? 250 LEU A CG  1 
ATOM   1915 C CD1 . LEU A 1 248 ? -34.62700 -9.81200  -13.67800 1.000 32.24000 ? 250 LEU A CD1 1 
ATOM   1916 C CD2 . LEU A 1 248 ? -32.14800 -9.30200  -13.80900 1.000 30.05000 ? 250 LEU A CD2 1 
ATOM   1917 N N   . GLY A 1 249 ? -32.90400 -10.79000 -19.21000 1.000 37.90000 ? 251 GLY A N   1 
ATOM   1918 C CA  . GLY A 1 249 ? -32.75900 -11.83000 -20.20500 1.000 41.47000 ? 251 GLY A CA  1 
ATOM   1919 C C   . GLY A 1 249 ? -31.33100 -12.29000 -20.43000 1.000 43.23000 ? 251 GLY A C   1 
ATOM   1920 O O   . GLY A 1 249 ? -31.04200 -13.49000 -20.43100 1.000 46.97000 ? 251 GLY A O   1 
ATOM   1921 N N   . PRO A 1 250 ? -30.40500 -11.34800 -20.63700 1.000 43.36000 ? 252 PRO A N   1 
ATOM   1922 C CA  . PRO A 1 250 ? -28.99400 -11.74900 -20.79100 1.000 40.93000 ? 252 PRO A CA  1 
ATOM   1923 C C   . PRO A 1 250 ? -28.42500 -12.56000 -19.62800 1.000 42.76000 ? 252 PRO A C   1 
ATOM   1924 O O   . PRO A 1 250 ? -27.73500 -13.55600 -19.87000 1.000 42.10000 ? 252 PRO A O   1 
ATOM   1925 C CB  . PRO A 1 250 ? -28.28600 -10.39800 -20.97300 1.000 39.99000 ? 252 PRO A CB  1 
ATOM   1926 C CG  . PRO A 1 250 ? -29.27800 -9.58100  -21.69300 1.000 40.46000 ? 252 PRO A CG  1 
ATOM   1927 C CD  . PRO A 1 250 ? -30.62600 -9.96200  -21.10000 1.000 42.32000 ? 252 PRO A CD  1 
ATOM   1928 N N   . LEU A 1 251 ? -28.67300 -12.16200 -18.37600 1.000 38.96000 ? 253 LEU A N   1 
ATOM   1929 C CA  . LEU A 1 251 ? -28.18300 -12.95300 -17.24800 1.000 36.79000 ? 253 LEU A CA  1 
ATOM   1930 C C   . LEU A 1 251 ? -28.87800 -14.31300 -17.18000 1.000 40.64000 ? 253 LEU A C   1 
ATOM   1931 O O   . LEU A 1 251 ? -28.25300 -15.32900 -16.82900 1.000 35.33000 ? 253 LEU A O   1 
ATOM   1932 C CB  . LEU A 1 251 ? -28.39100 -12.18900 -15.94400 1.000 34.68000 ? 253 LEU A CB  1 
ATOM   1933 C CG  . LEU A 1 251 ? -27.58200 -10.90500 -15.78300 1.000 37.76000 ? 253 LEU A CG  1 
ATOM   1934 C CD1 . LEU A 1 251 ? -28.02700 -10.18500 -14.52700 1.000 32.17000 ? 253 LEU A CD1 1 
ATOM   1935 C CD2 . LEU A 1 251 ? -26.10500 -11.23400 -15.71600 1.000 36.40000 ? 253 LEU A CD2 1 
ATOM   1936 N N   . SER A 1 252 ? -30.17500 -14.34100 -17.49400 1.000 36.08000 ? 254 SER A N   1 
ATOM   1937 C CA  . SER A 1 252 ? -30.90100 -15.60100 -17.58000 1.000 40.87000 ? 254 SER A CA  1 
ATOM   1938 C C   . SER A 1 252 ? -30.25100 -16.53900 -18.58800 1.000 41.43000 ? 254 SER A C   1 
ATOM   1939 O O   . SER A 1 252 ? -30.08800 -17.73700 -18.32500 1.000 40.19000 ? 254 SER A O   1 
ATOM   1940 C CB  . SER A 1 252 ? -32.36200 -15.34200 -17.96200 1.000 38.11000 ? 254 SER A CB  1 
ATOM   1941 O OG  . SER A 1 252 ? -33.09500 -16.56300 -17.96300 1.000 40.42000 ? 254 SER A OG  1 
ATOM   1942 N N   . ALA A 1 253 ? -29.88200 -16.00400 -19.75800 1.000 44.02000 ? 255 ALA A N   1 
ATOM   1943 C CA  . ALA A 1 253 ? -29.32500 -16.83200 -20.82400 1.000 43.46000 ? 255 ALA A CA  1 
ATOM   1944 C C   . ALA A 1 253 ? -27.92300 -17.30400 -20.47500 1.000 43.24000 ? 255 ALA A C   1 
ATOM   1945 O O   . ALA A 1 253 ? -27.54000 -18.43400 -20.79800 1.000 45.90000 ? 255 ALA A O   1 
ATOM   1946 C CB  . ALA A 1 253 ? -29.31500 -16.05800 -22.14500 1.000 42.68000 ? 255 ALA A CB  1 
ATOM   1947 N N   . GLN A 1 254 ? -27.14300 -16.45400 -19.81300 1.000 43.93000 ? 256 GLN A N   1 
ATOM   1948 C CA  . GLN A 1 254 ? -25.79700 -16.86000 -19.44500 1.000 44.39000 ? 256 GLN A CA  1 
ATOM   1949 C C   . GLN A 1 254 ? -25.82100 -18.00100 -18.43400 1.000 43.34000 ? 256 GLN A C   1 
ATOM   1950 O O   . GLN A 1 254 ? -24.98500 -18.91400 -18.50300 1.000 43.95000 ? 256 GLN A O   1 
ATOM   1951 C CB  . GLN A 1 254 ? -25.02300 -15.66500 -18.90100 1.000 45.16000 ? 256 GLN A CB  1 
ATOM   1952 C CG  . GLN A 1 254 ? -23.56300 -15.97100 -18.67700 1.000 48.20000 ? 256 GLN A CG  1 
ATOM   1953 C CD  . GLN A 1 254 ? -22.84100 -14.84100 -18.00200 1.000 46.07000 ? 256 GLN A CD  1 
ATOM   1954 O OE1 . GLN A 1 254 ? -23.30100 -13.70200 -18.02200 1.000 49.97000 ? 256 GLN A OE1 1 
ATOM   1955 N NE2 . GLN A 1 254 ? -21.70200 -15.14300 -17.39600 1.000 42.57000 ? 256 GLN A NE2 1 
ATOM   1956 N N   . THR A 1 255 ? -26.78100 -17.98400 -17.50200 1.000 38.39000 ? 257 THR A N   1 
ATOM   1957 C CA  . THR A 1 255 ? -26.81000 -18.96900 -16.42600 1.000 39.00000 ? 257 THR A CA  1 
ATOM   1958 C C   . THR A 1 255 ? -27.75500 -20.13600 -16.68000 1.000 35.15000 ? 257 THR A C   1 
ATOM   1959 O O   . THR A 1 255 ? -27.69200 -21.11600 -15.93700 1.000 39.73000 ? 257 THR A O   1 
ATOM   1960 C CB  . THR A 1 255 ? -27.21600 -18.32300 -15.09400 1.000 37.37000 ? 257 THR A CB  1 
ATOM   1961 O OG1 . THR A 1 255 ? -28.56800 -17.86900 -15.18600 1.000 32.38000 ? 257 THR A OG1 1 
ATOM   1962 C CG2 . THR A 1 255 ? -26.30600 -17.17600 -14.74900 1.000 39.95000 ? 257 THR A CG2 1 
ATOM   1963 N N   . GLY A 1 256 ? -28.64900 -20.04300 -17.66400 1.000 36.20000 ? 258 GLY A N   1 
ATOM   1964 C CA  . GLY A 1 256 ? -29.62000 -21.09500 -17.90000 1.000 38.95000 ? 258 GLY A CA  1 
ATOM   1965 C C   . GLY A 1 256 ? -30.78500 -21.14500 -16.93400 1.000 41.33000 ? 258 GLY A C   1 
ATOM   1966 O O   . GLY A 1 256 ? -31.49000 -22.16000 -16.87800 1.000 36.36000 ? 258 GLY A O   1 
ATOM   1967 N N   . ILE A 1 257 ? -31.01500 -20.08900 -16.16000 1.000 37.39000 ? 259 ILE A N   1 
ATOM   1968 C CA  . ILE A 1 257 ? -32.10500 -20.05400 -15.19100 1.000 34.21000 ? 259 ILE A CA  1 
ATOM   1969 C C   . ILE A 1 257 ? -33.11400 -19.02000 -15.66200 1.000 38.38000 ? 259 ILE A C   1 
ATOM   1970 O O   . ILE A 1 257 ? -32.79100 -17.82500 -15.77300 1.000 32.05000 ? 259 ILE A O   1 
ATOM   1971 C CB  . ILE A 1 257 ? -31.59100 -19.73600 -13.78000 1.000 35.69000 ? 259 ILE A CB  1 
ATOM   1972 C CG1 . ILE A 1 257 ? -30.55700 -20.78000 -13.35400 1.000 34.82000 ? 259 ILE A CG1 1 
ATOM   1973 C CG2 . ILE A 1 257 ? -32.73800 -19.69400 -12.78900 1.000 36.09000 ? 259 ILE A CG2 1 
ATOM   1974 C CD1 . ILE A 1 257 ? -29.75900 -20.37700 -12.13300 1.000 33.47000 ? 259 ILE A CD1 1 
ATOM   1975 N N   . ALA A 1 258 ? -34.32700 -19.48200 -15.96500 1.000 30.98000 ? 260 ALA A N   1 
ATOM   1976 C CA  . ALA A 1 258 ? -35.38100 -18.57800 -16.40300 1.000 34.44000 ? 260 ALA A CA  1 
ATOM   1977 C C   . ALA A 1 258 ? -35.63400 -17.49900 -15.35000 1.000 31.89000 ? 260 ALA A C   1 
ATOM   1978 O O   . ALA A 1 258 ? -35.50100 -17.72900 -14.14200 1.000 29.71000 ? 260 ALA A O   1 
ATOM   1979 C CB  . ALA A 1 258 ? -36.67400 -19.36000 -16.67900 1.000 34.00000 ? 260 ALA A CB  1 
ATOM   1980 N N   . VAL A 1 259 ? -36.01200 -16.30900 -15.82000 1.000 32.22000 ? 261 VAL A N   1 
ATOM   1981 C CA  . VAL A 1 259 ? -36.20700 -15.17800 -14.91100 1.000 30.86000 ? 261 VAL A CA  1 
ATOM   1982 C C   . VAL A 1 259 ? -37.24700 -15.51400 -13.84800 1.000 30.70000 ? 261 VAL A C   1 
ATOM   1983 O O   . VAL A 1 259 ? -37.01700 -15.32600 -12.64600 1.000 29.99000 ? 261 VAL A O   1 
ATOM   1984 C CB  . VAL A 1 259 ? -36.59100 -13.91200 -15.69800 1.000 33.20000 ? 261 VAL A CB  1 
ATOM   1985 C CG1 . VAL A 1 259 ? -37.08000 -12.83100 -14.74600 1.000 29.43000 ? 261 VAL A CG1 1 
ATOM   1986 C CG2 . VAL A 1 259 ? -35.38400 -13.41700 -16.52800 1.000 30.62000 ? 261 VAL A CG2 1 
ATOM   1987 N N   . LEU A 1 260 ? -38.40100 -16.03200 -14.27000 1.000 27.55000 ? 262 LEU A N   1 
ATOM   1988 C CA  . LEU A 1 260 ? -39.42100 -16.45200 -13.30800 1.000 30.61000 ? 262 LEU A CA  1 
ATOM   1989 C C   . LEU A 1 260 ? -38.98900 -17.63600 -12.43900 1.000 29.88000 ? 262 LEU A C   1 
ATOM   1990 O O   . LEU A 1 260 ? -39.55600 -17.82400 -11.35800 1.000 29.80000 ? 262 LEU A O   1 
ATOM   1991 C CB  . LEU A 1 260 ? -40.71600 -16.79300 -14.04200 1.000 31.35000 ? 262 LEU A CB  1 
ATOM   1992 C CG  . LEU A 1 260 ? -41.25100 -15.60400 -14.84100 1.000 36.26000 ? 262 LEU A CG  1 
ATOM   1993 C CD1 . LEU A 1 260 ? -42.49900 -15.98300 -15.62600 1.000 35.60000 ? 262 LEU A CD1 1 
ATOM   1994 C CD2 . LEU A 1 260 ? -41.54400 -14.45000 -13.88700 1.000 33.81000 ? 262 LEU A CD2 1 
ATOM   1995 N N   . ASP A 1 261 ? -38.00100 -18.43500 -12.86300 1.000 27.87000 ? 263 ASP A N   1 
ATOM   1996 C CA  . ASP A 1 261 ? -37.47200 -19.44200 -11.94800 1.000 28.25000 ? 263 ASP A CA  1 
ATOM   1997 C C   . ASP A 1 261 ? -36.64700 -18.77500 -10.85500 1.000 30.79000 ? 263 ASP A C   1 
ATOM   1998 O O   . ASP A 1 261 ? -36.74200 -19.14100 -9.67600  1.000 28.36000 ? 263 ASP A O   1 
ATOM   1999 C CB  . ASP A 1 261 ? -36.64100 -20.48000 -12.70600 1.000 30.23000 ? 263 ASP A CB  1 
ATOM   2000 C CG  . ASP A 1 261 ? -37.50400 -21.43200 -13.55900 1.000 33.94000 ? 263 ASP A CG  1 
ATOM   2001 O OD1 . ASP A 1 261 ? -38.74800 -21.33700 -13.52000 1.000 32.84000 ? 263 ASP A OD1 1 
ATOM   2002 O OD2 . ASP A 1 261 ? -36.92200 -22.26600 -14.28100 1.000 34.88000 ? 263 ASP A OD2 1 
ATOM   2003 N N   . MET A 1 262 ? -35.84700 -17.76900 -11.22300 1.000 31.74000 ? 264 MET A N   1 
ATOM   2004 C CA  . MET A 1 262 ? -35.14100 -16.99700 -10.20500 1.000 31.11000 ? 264 MET A CA  1 
ATOM   2005 C C   . MET A 1 262 ? -36.11500 -16.26400 -9.29600  1.000 27.69000 ? 264 MET A C   1 
ATOM   2006 O O   . MET A 1 262 ? -35.85800 -16.13300 -8.09300  1.000 25.75000 ? 264 MET A O   1 
ATOM   2007 C CB  . MET A 1 262 ? -34.16500 -16.01200 -10.85700 1.000 27.68000 ? 264 MET A CB  1 
ATOM   2008 C CG  . MET A 1 262 ? -33.11200 -15.46900 -9.89800  1.000 29.79000 ? 264 MET A CG  1 
ATOM   2009 S SD  . MET A 1 262 ? -32.07900 -16.72400 -9.07200  1.000 33.33000 ? 264 MET A SD  1 
ATOM   2010 C CE  . MET A 1 262 ? -30.63900 -16.75000 -10.12900 1.000 31.93000 ? 264 MET A CE  1 
ATOM   2011 N N   . CYS A 1 263 ? -37.25000 -15.80800 -9.83900  1.000 27.87000 ? 265 CYS A N   1 
ATOM   2012 C CA  . CYS A 1 263 ? -38.26600 -15.18300 -8.99800  1.000 28.77000 ? 265 CYS A CA  1 
ATOM   2013 C C   . CYS A 1 263 ? -38.78500 -16.15700 -7.94500  1.000 26.42000 ? 265 CYS A C   1 
ATOM   2014 O O   . CYS A 1 263 ? -38.99900 -15.77000 -6.78600  1.000 27.47000 ? 265 CYS A O   1 
ATOM   2015 C CB  . CYS A 1 263 ? -39.41300 -14.64800 -9.85800  1.000 28.94000 ? 265 CYS A CB  1 
ATOM   2016 S SG  . CYS A 1 263 ? -39.00500 -13.13500 -10.80300 1.000 30.16000 ? 265 CYS A SG  1 
ATOM   2017 N N   . ALA A 1 264 ? -38.98300 -17.42600 -8.32500  1.000 26.05000 ? 266 ALA A N   1 
ATOM   2018 C CA  . ALA A 1 264 ? -39.40800 -18.44400 -7.36400  1.000 27.07000 ? 266 ALA A CA  1 
ATOM   2019 C C   . ALA A 1 264 ? -38.39000 -18.61500 -6.24100  1.000 28.50000 ? 266 ALA A C   1 
ATOM   2020 O O   . ALA A 1 264 ? -38.76400 -18.75400 -5.06900  1.000 26.80000 ? 266 ALA A O   1 
ATOM   2021 C CB  . ALA A 1 264 ? -39.63500 -19.78700 -8.07600  1.000 28.36000 ? 266 ALA A CB  1 
ATOM   2022 N N   . SER A 1 265 ? -37.09800 -18.62400 -6.58700  1.000 25.78000 ? 267 SER A N   1 
ATOM   2023 C CA  . SER A 1 265 ? -36.04300 -18.64900 -5.57700  1.000 26.75000 ? 267 SER A CA  1 
ATOM   2024 C C   . SER A 1 265 ? -36.16000 -17.46000 -4.61600  1.000 26.72000 ? 267 SER A C   1 
ATOM   2025 O O   . SER A 1 265 ? -36.17500 -17.63800 -3.39000  1.000 25.78000 ? 267 SER A O   1 
ATOM   2026 C CB  . SER A 1 265 ? -34.67600 -18.67700 -6.27200  1.000 27.70000 ? 267 SER A CB  1 
ATOM   2027 O OG  . SER A 1 265 ? -33.60600 -18.59900 -5.32700  1.000 33.85000 ? 267 SER A OG  1 
ATOM   2028 N N   . LEU A 1 266 ? -36.25900 -16.23500 -5.15300  1.000 25.71000 ? 268 LEU A N   1 
ATOM   2029 C CA  . LEU A 1 266 ? -36.39500 -15.05300 -4.30000  1.000 24.89000 ? 268 LEU A CA  1 
ATOM   2030 C C   . LEU A 1 266 ? -37.58900 -15.18000 -3.35800  1.000 23.16000 ? 268 LEU A C   1 
ATOM   2031 O O   . LEU A 1 266 ? -37.48500 -14.89700 -2.15800  1.000 23.74000 ? 268 LEU A O   1 
ATOM   2032 C CB  . LEU A 1 266 ? -36.52700 -13.78500 -5.15500  1.000 22.70000 ? 268 LEU A CB  1 
ATOM   2033 C CG  . LEU A 1 266 ? -36.65700 -12.46900 -4.38000  1.000 29.59000 ? 268 LEU A CG  1 
ATOM   2034 C CD1 . LEU A 1 266 ? -35.58900 -12.33700 -3.28500  1.000 25.20000 ? 268 LEU A CD1 1 
ATOM   2035 C CD2 . LEU A 1 266 ? -36.60300 -11.25400 -5.31200  1.000 26.41000 ? 268 LEU A CD2 1 
ATOM   2036 N N   . LYS A 1 267 ? -38.73400 -15.61000 -3.88800  1.000 22.64000 ? 269 LYS A N   1 
ATOM   2037 C CA  . LYS A 1 267 ? -39.91400 -15.78800 -3.05200  1.000 26.26000 ? 269 LYS A CA  1 
ATOM   2038 C C   . LYS A 1 267 ? -39.61500 -16.67400 -1.85500  1.000 25.43000 ? 269 LYS A C   1 
ATOM   2039 O O   . LYS A 1 267 ? -40.04700 -16.38400 -0.73300  1.000 29.77000 ? 269 LYS A O   1 
ATOM   2040 C CB  . LYS A 1 267 ? -41.05400 -16.39100 -3.88100  1.000 28.49000 ? 269 LYS A CB  1 
ATOM   2041 C CG  . LYS A 1 267 ? -41.80500 -15.41000 -4.73800  1.000 31.31000 ? 269 LYS A CG  1 
ATOM   2042 C CD  . LYS A 1 267 ? -42.69500 -16.09900 -5.76700  1.000 31.74000 ? 269 LYS A CD  1 
ATOM   2043 C CE  . LYS A 1 267 ? -43.92000 -16.74300 -5.13300  1.000 30.22000 ? 269 LYS A CE  1 
ATOM   2044 N NZ  . LYS A 1 267 ? -44.77400 -17.36600 -6.20300  1.000 29.69000 ? 269 LYS A NZ  1 
ATOM   2045 N N   . GLU A 1 268 ? -38.87100 -17.76300 -2.07900  1.000 25.16000 ? 270 GLU A N   1 
ATOM   2046 C CA  . GLU A 1 268 ? -38.53500 -18.68100 -0.99300  1.000 27.30000 ? 270 GLU A CA  1 
ATOM   2047 C C   . GLU A 1 268 ? -37.51200 -18.06000 -0.05000  1.000 24.25000 ? 270 GLU A C   1 
ATOM   2048 O O   . GLU A 1 268 ? -37.60800 -18.20700 1.17600   1.000 24.60000 ? 270 GLU A O   1 
ATOM   2049 C CB  . GLU A 1 268 ? -38.00300 -19.99000 -1.58000  1.000 27.78000 ? 270 GLU A CB  1 
ATOM   2050 C CG  . GLU A 1 268 ? -37.65900 -21.02200 -0.54400  1.000 29.41000 ? 270 GLU A CG  1 
ATOM   2051 C CD  . GLU A 1 268 ? -37.39600 -22.38700 -1.16200  1.000 33.18000 ? 270 GLU A CD  1 
ATOM   2052 O OE1 . GLU A 1 268 ? -38.36700 -23.10300 -1.52700  1.000 28.79000 ? 270 GLU A OE1 1 
ATOM   2053 O OE2 . GLU A 1 268 ? -36.21000 -22.73400 -1.28200  1.000 32.05000 ? 270 GLU A OE2 1 
ATOM   2054 N N   . LEU A 1 269 ? -36.52600 -17.36100 -0.60900  1.000 27.35000 ? 271 LEU A N   1 
ATOM   2055 C CA  . LEU A 1 269 ? -35.57000 -16.62600 0.21800   1.000 27.10000 ? 271 LEU A CA  1 
ATOM   2056 C C   . LEU A 1 269 ? -36.27100 -15.64700 1.15000   1.000 27.92000 ? 271 LEU A C   1 
ATOM   2057 O O   . LEU A 1 269 ? -35.90100 -15.53400 2.32500   1.000 28.79000 ? 271 LEU A O   1 
ATOM   2058 C CB  . LEU A 1 269 ? -34.56700 -15.89700 -0.67400  1.000 29.32000 ? 271 LEU A CB  1 
ATOM   2059 C CG  . LEU A 1 269 ? -33.38100 -16.74800 -1.15500  1.000 29.30000 ? 271 LEU A CG  1 
ATOM   2060 C CD1 . LEU A 1 269 ? -32.54300 -15.97500 -2.16700  1.000 31.94000 ? 271 LEU A CD1 1 
ATOM   2061 C CD2 . LEU A 1 269 ? -32.52300 -17.19100 0.03100   1.000 30.47000 ? 271 LEU A CD2 1 
ATOM   2062 N N   . LEU A 1 270 ? -37.29900 -14.94300 0.65800   1.000 27.41000 ? 272 LEU A N   1 
ATOM   2063 C CA  . LEU A 1 270 ? -38.00500 -14.00900 1.53200   1.000 24.78000 ? 272 LEU A CA  1 
ATOM   2064 C C   . LEU A 1 270 ? -38.75800 -14.75600 2.61700   1.000 26.76000 ? 272 LEU A C   1 
ATOM   2065 O O   . LEU A 1 270 ? -38.87900 -14.28000 3.74900   1.000 24.74000 ? 272 LEU A O   1 
ATOM   2066 C CB  . LEU A 1 270 ? -38.96300 -13.12900 0.71400   1.000 26.20000 ? 272 LEU A CB  1 
ATOM   2067 C CG  . LEU A 1 270 ? -38.27300 -12.18700 -0.28200  1.000 25.46000 ? 272 LEU A CG  1 
ATOM   2068 C CD1 . LEU A 1 270 ? -39.25400 -11.66300 -1.31200  1.000 27.61000 ? 272 LEU A CD1 1 
ATOM   2069 C CD2 . LEU A 1 270 ? -37.61600 -11.05600 0.44500   1.000 25.18000 ? 272 LEU A CD2 1 
ATOM   2070 N N   . GLN A 1 271 ? -39.24600 -15.94600 2.29500   1.000 26.64000 ? 273 GLN A N   1 
ATOM   2071 C CA  . GLN A 1 271 ? -40.03100 -16.72300 3.25000   1.000 25.46000 ? 273 GLN A CA  1 
ATOM   2072 C C   . GLN A 1 271 ? -39.15100 -17.34100 4.33700   1.000 25.92000 ? 273 GLN A C   1 
ATOM   2073 O O   . GLN A 1 271 ? -39.54900 -17.39200 5.50300   1.000 29.17000 ? 273 GLN A O   1 
ATOM   2074 C CB  . GLN A 1 271 ? -40.80100 -17.78500 2.47000   1.000 26.42000 ? 273 GLN A CB  1 
ATOM   2075 C CG  . GLN A 1 271 ? -41.34200 -18.95600 3.22700   1.000 26.91000 ? 273 GLN A CG  1 
ATOM   2076 C CD  . GLN A 1 271 ? -41.76900 -20.03500 2.25400   1.000 27.43000 ? 273 GLN A CD  1 
ATOM   2077 O OE1 . GLN A 1 271 ? -42.84400 -19.96600 1.65900   1.000 30.51000 ? 273 GLN A OE1 1 
ATOM   2078 N NE2 . GLN A 1 271 ? -40.90900 -21.00800 2.05500   1.000 27.58000 ? 273 GLN A NE2 1 
ATOM   2079 N N   . ASN A 1 272 ? -37.95000 -17.81200 3.98200   1.000 29.07000 ? 274 ASN A N   1 
ATOM   2080 C CA  . ASN A 1 272 ? -37.09500 -18.54700 4.91600   1.000 30.10000 ? 274 ASN A CA  1 
ATOM   2081 C C   . ASN A 1 272 ? -35.95400 -17.72600 5.50000   1.000 33.69000 ? 274 ASN A C   1 
ATOM   2082 O O   . ASN A 1 272 ? -35.36600 -18.15100 6.50100   1.000 34.15000 ? 274 ASN A O   1 
ATOM   2083 C CB  . ASN A 1 272 ? -36.45600 -19.77700 4.23800   1.000 31.10000 ? 274 ASN A CB  1 
ATOM   2084 C CG  . ASN A 1 272 ? -37.48300 -20.73600 3.66500   1.000 29.22000 ? 274 ASN A CG  1 
ATOM   2085 O OD1 . ASN A 1 272 ? -38.66000 -20.66800 4.00400   1.000 27.79000 ? 274 ASN A OD1 1 
ATOM   2086 N ND2 . ASN A 1 272 ? -37.03900 -21.62700 2.78500   1.000 27.57000 ? 274 ASN A ND2 1 
ATOM   2087 N N   . GLY A 1 273 ? -35.60800 -16.59000 4.89900   1.000 32.48000 ? 275 GLY A N   1 
ATOM   2088 C CA  . GLY A 1 273 ? -34.33600 -15.99300 5.30200   1.000 37.88000 ? 275 GLY A CA  1 
ATOM   2089 C C   . GLY A 1 273 ? -33.18600 -16.85900 4.79400   1.000 36.61000 ? 275 GLY A C   1 
ATOM   2090 O O   . GLY A 1 273 ? -33.33900 -17.67800 3.88400   1.000 33.14000 ? 275 GLY A O   1 
ATOM   2091 N N   . MET A 1 274 ? -32.02000 -16.68400 5.41700   1.000 38.60000 ? 276 MET A N   1 
ATOM   2092 C CA  . MET A 1 274 ? -30.79300 -17.31000 4.93900   1.000 37.38000 ? 276 MET A CA  1 
ATOM   2093 C C   . MET A 1 274 ? -30.41200 -18.57500 5.68500   1.000 37.37000 ? 276 MET A C   1 
ATOM   2094 O O   . MET A 1 274 ? -29.55900 -19.32200 5.19500   1.000 41.69000 ? 276 MET A O   1 
ATOM   2095 C CB  . MET A 1 274 ? -29.62300 -16.32400 5.05100   1.000 38.84000 ? 276 MET A CB  1 
ATOM   2096 C CG  . MET A 1 274 ? -29.89900 -15.03300 4.34600   1.000 43.99000 ? 276 MET A CG  1 
ATOM   2097 S SD  . MET A 1 274 ? -29.60500 -15.27300 2.59600   1.000 46.61000 ? 276 MET A SD  1 
ATOM   2098 C CE  . MET A 1 274 ? -28.15300 -14.23900 2.45100   1.000 40.18000 ? 276 MET A CE  1 
ATOM   2099 N N   . ASN A 1 275 ? -30.98400 -18.79600 6.86400   1.000 39.26000 ? 277 ASN A N   1 
ATOM   2100 C CA  . ASN A 1 275 ? -30.65800 -19.92600 7.72900   1.000 40.16000 ? 277 ASN A CA  1 
ATOM   2101 C C   . ASN A 1 275 ? -29.14500 -20.00600 7.96000   1.000 43.45000 ? 277 ASN A C   1 
ATOM   2102 O O   . ASN A 1 275 ? -28.48500 -21.00700 7.68200   1.000 39.72000 ? 277 ASN A O   1 
ATOM   2103 C CB  . ASN A 1 275 ? -31.24200 -21.21800 7.15700   1.000 44.67000 ? 277 ASN A CB  1 
ATOM   2104 C CG  . ASN A 1 275 ? -32.75800 -21.11600 6.94300   1.000 46.99000 ? 277 ASN A CG  1 
ATOM   2105 O OD1 . ASN A 1 275 ? -33.25200 -21.19200 5.81200   1.000 44.70000 ? 277 ASN A OD1 1 
ATOM   2106 N ND2 . ASN A 1 275 ? -33.49500 -20.89100 8.03400   1.000 45.67000 ? 277 ASN A ND2 1 
ATOM   2107 N N   . GLY A 1 276 ? -28.60400 -18.89500 8.46100   1.000 42.51000 ? 278 GLY A N   1 
ATOM   2108 C CA  . GLY A 1 276 ? -27.19900 -18.82300 8.81600   1.000 41.53000 ? 278 GLY A CA  1 
ATOM   2109 C C   . GLY A 1 276 ? -26.24300 -18.81100 7.64900   1.000 43.08000 ? 278 GLY A C   1 
ATOM   2110 O O   . GLY A 1 276 ? -25.03200 -18.92500 7.85900   1.000 46.82000 ? 278 GLY A O   1 
ATOM   2111 N N   . ARG A 1 277 ? -26.73600 -18.67600 6.42300   1.000 40.67000 ? 279 ARG A N   1 
ATOM   2112 C CA  . ARG A 1 277 ? -25.86100 -18.70000 5.26700   1.000 38.67000 ? 279 ARG A CA  1 
ATOM   2113 C C   . ARG A 1 277 ? -25.64700 -17.29200 4.71400   1.000 39.69000 ? 279 ARG A C   1 
ATOM   2114 O O   . ARG A 1 277 ? -26.18400 -16.29200 5.20100   1.000 36.91000 ? 279 ARG A O   1 
ATOM   2115 C CB  . ARG A 1 277 ? -26.41200 -19.61300 4.17200   1.000 37.46000 ? 279 ARG A CB  1 
ATOM   2116 C CG  . ARG A 1 277 ? -25.94100 -21.04900 4.24300   1.000 38.17000 ? 279 ARG A CG  1 
ATOM   2117 C CD  . ARG A 1 277 ? -26.76200 -21.90000 3.33400   1.000 36.16000 ? 279 ARG A CD  1 
ATOM   2118 N NE  . ARG A 1 277 ? -28.18400 -21.68000 3.57700   1.000 44.23000 ? 279 ARG A NE  1 
ATOM   2119 C CZ  . ARG A 1 277 ? -29.14200 -22.55100 3.27100   1.000 43.88000 ? 279 ARG A CZ  1 
ATOM   2120 N NH1 . ARG A 1 277 ? -28.82400 -23.70300 2.69900   1.000 39.25000 ? 279 ARG A NH1 1 
ATOM   2121 N NH2 . ARG A 1 277 ? -30.41900 -22.26500 3.52900   1.000 40.18000 ? 279 ARG A NH2 1 
ATOM   2122 N N   . THR A 1 278 ? -24.87400 -17.25000 3.63800   1.000 35.81000 ? 280 THR A N   1 
ATOM   2123 C CA  . THR A 1 278 ? -24.38100 -16.04000 3.02400   1.000 41.50000 ? 280 THR A CA  1 
ATOM   2124 C C   . THR A 1 278 ? -24.54400 -16.16000 1.51500   1.000 38.84000 ? 280 THR A C   1 
ATOM   2125 O O   . THR A 1 278 ? -24.47200 -17.25800 0.95400   1.000 37.37000 ? 280 THR A O   1 
ATOM   2126 C CB  . THR A 1 278 ? -22.90800 -15.83900 3.44500   1.000 39.97000 ? 280 THR A CB  1 
ATOM   2127 O OG1 . THR A 1 278 ? -22.79600 -14.63100 4.20100   1.000 42.82000 ? 280 THR A OG1 1 
ATOM   2128 C CG2 . THR A 1 278 ? -21.96100 -15.85400 2.24800   1.000 37.75000 ? 280 THR A CG2 1 
ATOM   2129 N N   . ILE A 1 279 ? -24.80700 -15.03000 0.86700   1.000 36.80000 ? 281 ILE A N   1 
ATOM   2130 C CA  . ILE A 1 279 ? -24.79800 -14.94700 -0.58800  1.000 36.41000 ? 281 ILE A CA  1 
ATOM   2131 C C   . ILE A 1 279 ? -23.86500 -13.80600 -0.96900  1.000 36.75000 ? 281 ILE A C   1 
ATOM   2132 O O   . ILE A 1 279 ? -24.04200 -12.67200 -0.50300  1.000 37.50000 ? 281 ILE A O   1 
ATOM   2133 C CB  . ILE A 1 279 ? -26.20500 -14.72800 -1.17500  1.000 37.82000 ? 281 ILE A CB  1 
ATOM   2134 C CG1 . ILE A 1 279 ? -27.10400 -15.92800 -0.89600  1.000 32.11000 ? 281 ILE A CG1 1 
ATOM   2135 C CG2 . ILE A 1 279 ? -26.12500 -14.47300 -2.67300  1.000 34.73000 ? 281 ILE A CG2 1 
ATOM   2136 C CD1 . ILE A 1 279 ? -28.57100 -15.73700 -1.32800  1.000 33.05000 ? 281 ILE A CD1 1 
ATOM   2137 N N   . LEU A 1 280 ? -22.87200 -14.10700 -1.80900  1.000 39.57000 ? 282 LEU A N   1 
ATOM   2138 C CA  . LEU A 1 280 ? -21.84300 -13.13200 -2.19900  1.000 43.88000 ? 282 LEU A CA  1 
ATOM   2139 C C   . LEU A 1 280 ? -21.32900 -12.35000 -0.99300  1.000 38.10000 ? 282 LEU A C   1 
ATOM   2140 O O   . LEU A 1 280 ? -21.16400 -11.12400 -1.03300  1.000 38.04000 ? 282 LEU A O   1 
ATOM   2141 C CB  . LEU A 1 280 ? -22.35600 -12.18100 -3.28200  1.000 36.51000 ? 282 LEU A CB  1 
ATOM   2142 C CG  . LEU A 1 280 ? -22.57800 -12.87800 -4.62400  1.000 36.48000 ? 282 LEU A CG  1 
ATOM   2143 C CD1 . LEU A 1 280 ? -23.37400 -12.01500 -5.55600  1.000 32.42000 ? 282 LEU A CD1 1 
ATOM   2144 C CD2 . LEU A 1 280 ? -21.24100 -13.28500 -5.24500  1.000 42.32000 ? 282 LEU A CD2 1 
ATOM   2145 N N   . GLY A 1 281 ? -21.11500 -13.06500 0.10600   1.000 35.30000 ? 283 GLY A N   1 
ATOM   2146 C CA  . GLY A 1 281 ? -20.58900 -12.47500 1.31700   1.000 39.10000 ? 283 GLY A CA  1 
ATOM   2147 C C   . GLY A 1 281 ? -21.56800 -11.67900 2.14800   1.000 38.05000 ? 283 GLY A C   1 
ATOM   2148 O O   . GLY A 1 281 ? -21.16100 -11.10800 3.16800   1.000 39.18000 ? 283 GLY A O   1 
ATOM   2149 N N   . SER A 1 282 ? -22.84400 -11.63100 1.77900   1.000 38.58000 ? 284 SER A N   1 
ATOM   2150 C CA  . SER A 1 282 ? -23.81500 -10.82200 2.50100   1.000 39.02000 ? 284 SER A CA  1 
ATOM   2151 C C   . SER A 1 282 ? -24.87000 -11.70700 3.15400   1.000 36.97000 ? 284 SER A C   1 
ATOM   2152 O O   . SER A 1 282 ? -25.29400 -12.71500 2.58200   1.000 34.73000 ? 284 SER A O   1 
ATOM   2153 C CB  . SER A 1 282 ? -24.49000 -9.80600  1.57000   1.000 32.75000 ? 284 SER A CB  1 
ATOM   2154 O OG  . SER A 1 282 ? -25.51300 -9.09600  2.25900   1.000 38.56000 ? 284 SER A OG  1 
ATOM   2155 N N   . ALA A 1 283 ? -25.29300 -11.32200 4.35600   1.000 37.54000 ? 285 ALA A N   1 
ATOM   2156 C CA  . ALA A 1 283 ? -26.39600 -11.98500 5.03500   1.000 36.55000 ? 285 ALA A CA  1 
ATOM   2157 C C   . ALA A 1 283 ? -27.74500 -11.33600 4.74600   1.000 34.28000 ? 285 ALA A C   1 
ATOM   2158 O O   . ALA A 1 283 ? -28.73500 -11.71100 5.37400   1.000 34.51000 ? 285 ALA A O   1 
ATOM   2159 C CB  . ALA A 1 283 ? -26.15100 -12.01900 6.54500   1.000 38.22000 ? 285 ALA A CB  1 
ATOM   2160 N N   . LEU A 1 284 ? -27.80200 -10.35400 3.83900   1.000 35.35000 ? 286 LEU A N   1 
ATOM   2161 C CA  . LEU A 1 284 ? -29.05200 -9.72100  3.42900   1.000 35.63000 ? 286 LEU A CA  1 
ATOM   2162 C C   . LEU A 1 284 ? -29.14600 -9.76800  1.91300   1.000 33.32000 ? 286 LEU A C   1 
ATOM   2163 O O   . LEU A 1 284 ? -28.13900 -9.91800  1.21800   1.000 33.95000 ? 286 LEU A O   1 
ATOM   2164 C CB  . LEU A 1 284 ? -29.15300 -8.25700  3.89800   1.000 37.28000 ? 286 LEU A CB  1 
ATOM   2165 C CG  . LEU A 1 284 ? -29.04400 -7.96600  5.38900   1.000 39.75000 ? 286 LEU A CG  1 
ATOM   2166 C CD1 . LEU A 1 284 ? -29.10100 -6.46600  5.65000   1.000 45.53000 ? 286 LEU A CD1 1 
ATOM   2167 C CD2 . LEU A 1 284 ? -30.15000 -8.68200  6.13300   1.000 41.33000 ? 286 LEU A CD2 1 
ATOM   2168 N N   . LEU A 1 285 ? -30.36200 -9.61200  1.39600   1.000 28.20000 ? 287 LEU A N   1 
ATOM   2169 C CA  . LEU A 1 285 ? -30.54400 -9.55300  -0.04900  1.000 29.80000 ? 287 LEU A CA  1 
ATOM   2170 C C   . LEU A 1 285 ? -30.14700 -8.16300  -0.53600  1.000 34.61000 ? 287 LEU A C   1 
ATOM   2171 O O   . LEU A 1 285 ? -30.70300 -7.15900  -0.09000  1.000 31.05000 ? 287 LEU A O   1 
ATOM   2172 C CB  . LEU A 1 285 ? -31.98200 -9.89100  -0.42500  1.000 30.54000 ? 287 LEU A CB  1 
ATOM   2173 C CG  . LEU A 1 285 ? -32.44200 -11.24500 0.13200   1.000 30.41000 ? 287 LEU A CG  1 
ATOM   2174 C CD1 . LEU A 1 285 ? -33.92800 -11.46200 -0.14200  1.000 31.13000 ? 287 LEU A CD1 1 
ATOM   2175 C CD2 . LEU A 1 285 ? -31.60400 -12.38800 -0.44600  1.000 30.97000 ? 287 LEU A CD2 1 
ATOM   2176 N N   . GLU A 1 286 ? -29.15100 -8.10800  -1.41300  1.000 37.60000 ? 288 GLU A N   1 
ATOM   2177 C CA  . GLU A 1 286 ? -28.51000 -6.85900  -1.80700  1.000 35.03000 ? 288 GLU A CA  1 
ATOM   2178 C C   . GLU A 1 286 ? -29.21800 -6.26700  -3.02200  1.000 31.33000 ? 288 GLU A C   1 
ATOM   2179 O O   . GLU A 1 286 ? -29.43800 -6.97300  -4.00700  1.000 29.36000 ? 288 GLU A O   1 
ATOM   2180 C CB  . GLU A 1 286 ? -27.03900 -7.13300  -2.12000  1.000 34.47000 ? 288 GLU A CB  1 
ATOM   2181 C CG  . GLU A 1 286 ? -26.32900 -5.96400  -2.73200  1.000 40.61000 ? 288 GLU A CG  1 
ATOM   2182 C CD  . GLU A 1 286 ? -26.33000 -4.75800  -1.80900  1.000 45.83000 ? 288 GLU A CD  1 
ATOM   2183 O OE1 . GLU A 1 286 ? -25.85700 -4.90700  -0.65100  1.000 46.46000 ? 288 GLU A OE1 1 
ATOM   2184 O OE2 . GLU A 1 286 ? -26.83100 -3.68700  -2.23600  1.000 40.80000 ? 288 GLU A OE2 1 
ATOM   2185 N N   . ASP A 1 287 ? -29.56800 -4.96900  -2.97000  1.000 32.27000 ? 289 ASP A N   1 
ATOM   2186 C CA  . ASP A 1 287 ? -30.32200 -4.37600  -4.07700  1.000 29.38000 ? 289 ASP A CA  1 
ATOM   2187 C C   . ASP A 1 287 ? -29.65000 -3.15800  -4.71600  1.000 30.12000 ? 289 ASP A C   1 
ATOM   2188 O O   . ASP A 1 287 ? -30.30000 -2.44500  -5.48300  1.000 28.30000 ? 289 ASP A O   1 
ATOM   2189 C CB  . ASP A 1 287 ? -31.75900 -4.03300  -3.64500  1.000 30.89000 ? 289 ASP A CB  1 
ATOM   2190 C CG  . ASP A 1 287 ? -31.86500 -2.78200  -2.77200  1.000 29.24000 ? 289 ASP A CG  1 
ATOM   2191 O OD1 . ASP A 1 287 ? -30.85200 -2.27600  -2.25200  1.000 28.26000 ? 289 ASP A OD1 1 
ATOM   2192 O OD2 . ASP A 1 287 ? -33.00700 -2.31900  -2.58500  1.000 28.17000 ? 289 ASP A OD2 1 
ATOM   2193 N N   . GLU A 1 288 ? -28.36100 -2.91700  -4.47800  1.000 28.21000 ? 290 GLU A N   1 
ATOM   2194 C CA  . GLU A 1 288 ? -27.70700 -1.77200  -5.10600  1.000 34.77000 ? 290 GLU A CA  1 
ATOM   2195 C C   . GLU A 1 288 ? -26.67700 -2.21100  -6.14800  1.000 33.63000 ? 290 GLU A C   1 
ATOM   2196 O O   . GLU A 1 288 ? -25.69200 -1.51200  -6.38800  1.000 32.12000 ? 290 GLU A O   1 
ATOM   2197 C CB  . GLU A 1 288 ? -27.12100 -0.82500  -4.04100  1.000 30.26000 ? 290 GLU A CB  1 
ATOM   2198 C CG  . GLU A 1 288 ? -28.24300 -0.28300  -3.07100  1.000 32.52000 ? 290 GLU A CG  1 
ATOM   2199 C CD  . GLU A 1 288 ? -27.99000 1.10400   -2.43700  1.000 40.86000 ? 290 GLU A CD  1 
ATOM   2200 O OE1 . GLU A 1 288 ? -26.81300 1.52900   -2.37900  1.000 33.47000 ? 290 GLU A OE1 1 
ATOM   2201 O OE2 . GLU A 1 288 ? -28.98300 1.76300   -1.98000  1.000 36.20000 ? 290 GLU A OE2 1 
ATOM   2202 N N   . PHE A 1 289 ? -26.91500 -3.36200  -6.79000  1.000 32.52000 ? 291 PHE A N   1 
ATOM   2203 C CA  . PHE A 1 289 ? -26.25400 -3.76900  -8.03100  1.000 30.99000 ? 291 PHE A CA  1 
ATOM   2204 C C   . PHE A 1 289 ? -27.30600 -3.93300  -9.12200  1.000 32.32000 ? 291 PHE A C   1 
ATOM   2205 O O   . PHE A 1 289 ? -28.26400 -4.69200  -8.94300  1.000 33.09000 ? 291 PHE A O   1 
ATOM   2206 C CB  . PHE A 1 289 ? -25.52500 -5.11600  -7.89400  1.000 30.16000 ? 291 PHE A CB  1 
ATOM   2207 C CG  . PHE A 1 289 ? -24.42700 -5.13500  -6.88200  1.000 35.68000 ? 291 PHE A CG  1 
ATOM   2208 C CD1 . PHE A 1 289 ? -23.16200 -4.65800  -7.19700  1.000 40.14000 ? 291 PHE A CD1 1 
ATOM   2209 C CD2 . PHE A 1 289 ? -24.64000 -5.68000  -5.62600  1.000 39.23000 ? 291 PHE A CD2 1 
ATOM   2210 C CE1 . PHE A 1 289 ? -22.12900 -4.69500  -6.26000  1.000 40.57000 ? 291 PHE A CE1 1 
ATOM   2211 C CE2 . PHE A 1 289 ? -23.61400 -5.71600  -4.68300  1.000 44.04000 ? 291 PHE A CE2 1 
ATOM   2212 C CZ  . PHE A 1 289 ? -22.35500 -5.21100  -5.00600  1.000 40.98000 ? 291 PHE A CZ  1 
ATOM   2213 N N   . THR A 1 290 ? -27.11100 -3.29200  -10.26300 1.000 31.27000 ? 292 THR A N   1 
ATOM   2214 C CA  . THR A 1 290 ? -28.05500 -3.41100  -11.37000 1.000 31.73000 ? 292 THR A CA  1 
ATOM   2215 C C   . THR A 1 290 ? -27.68000 -4.57300  -12.27900 1.000 33.56000 ? 292 THR A C   1 
ATOM   2216 O O   . THR A 1 290 ? -26.56300 -5.10900  -12.22200 1.000 33.25000 ? 292 THR A O   1 
ATOM   2217 C CB  . THR A 1 290 ? -28.07100 -2.12200  -12.17800 1.000 33.10000 ? 292 THR A CB  1 
ATOM   2218 O OG1 . THR A 1 290 ? -26.80800 -1.99600  -12.84300 1.000 31.25000 ? 292 THR A OG1 1 
ATOM   2219 C CG2 . THR A 1 290 ? -28.33500 -0.90700  -11.27700 1.000 29.55000 ? 292 THR A CG2 1 
ATOM   2220 N N   . PRO A 1 291 ? -28.60500 -4.99900  -13.15100 1.000 29.68000 ? 293 PRO A N   1 
ATOM   2221 C CA  . PRO A 1 291 ? -28.22400 -5.96400  -14.20100 1.000 33.88000 ? 293 PRO A CA  1 
ATOM   2222 C C   . PRO A 1 291 ? -26.97500 -5.55500  -14.96700 1.000 35.09000 ? 293 PRO A C   1 
ATOM   2223 O O   . PRO A 1 291 ? -26.12500 -6.40100  -15.28200 1.000 34.42000 ? 293 PRO A O   1 
ATOM   2224 C CB  . PRO A 1 291 ? -29.46400 -5.98900  -15.09900 1.000 35.94000 ? 293 PRO A CB  1 
ATOM   2225 C CG  . PRO A 1 291 ? -30.59600 -5.65700  -14.17100 1.000 33.90000 ? 293 PRO A CG  1 
ATOM   2226 C CD  . PRO A 1 291 ? -30.05900 -4.73200  -13.13000 1.000 29.00000 ? 293 PRO A CD  1 
ATOM   2227 N N   . PHE A 1 292 ? -26.84300 -4.26200  -15.27300 1.000 36.86000 ? 294 PHE A N   1 
ATOM   2228 C CA  . PHE A 1 292 ? -25.64500 -3.75800  -15.93900 1.000 34.93000 ? 294 PHE A CA  1 
ATOM   2229 C C   . PHE A 1 292 ? -24.40200 -3.93000  -15.06500 1.000 34.46000 ? 294 PHE A C   1 
ATOM   2230 O O   . PHE A 1 292 ? -23.37200 -4.42900  -15.53000 1.000 39.02000 ? 294 PHE A O   1 
ATOM   2231 C CB  . PHE A 1 292 ? -25.86600 -2.29000  -16.31500 1.000 41.36000 ? 294 PHE A CB  1 
ATOM   2232 C CG  . PHE A 1 292 ? -24.79800 -1.71500  -17.20900 1.000 45.37000 ? 294 PHE A CG  1 
ATOM   2233 C CD1 . PHE A 1 292 ? -23.58300 -1.29400  -16.68400 1.000 46.50000 ? 294 PHE A CD1 1 
ATOM   2234 C CD2 . PHE A 1 292 ? -25.01900 -1.57000  -18.57400 1.000 50.10000 ? 294 PHE A CD2 1 
ATOM   2235 C CE1 . PHE A 1 292 ? -22.59300 -0.76200  -17.50800 1.000 47.26000 ? 294 PHE A CE1 1 
ATOM   2236 C CE2 . PHE A 1 292 ? -24.03500 -1.02400  -19.40000 1.000 50.56000 ? 294 PHE A CE2 1 
ATOM   2237 C CZ  . PHE A 1 292 ? -22.82600 -0.62400  -18.86400 1.000 45.49000 ? 294 PHE A CZ  1 
ATOM   2238 N N   . ASP A 1 293 ? -24.45900 -3.59900  -13.79700 1.000 32.35000 ? 295 ASP A N   1 
ATOM   2239 C CA  . ASP A 1 293 ? -23.25200 -3.66900  -12.94300 1.000 33.41000 ? 295 ASP A CA  1 
ATOM   2240 C C   . ASP A 1 293 ? -22.75500 -5.11300  -12.81400 1.000 36.26000 ? 295 ASP A C   1 
ATOM   2241 O O   . ASP A 1 293 ? -21.55200 -5.31500  -12.75800 1.000 34.66000 ? 295 ASP A O   1 
ATOM   2242 C CB  . ASP A 1 293 ? -23.53500 -3.10700  -11.56000 1.000 31.76000 ? 295 ASP A CB  1 
ATOM   2243 C CG  . ASP A 1 293 ? -24.06800 -1.69100  -11.52600 1.000 34.04000 ? 295 ASP A CG  1 
ATOM   2244 O OD1 . ASP A 1 293 ? -23.79000 -0.93100  -12.46000 1.000 33.10000 ? 295 ASP A OD1 1 
ATOM   2245 O OD2 . ASP A 1 293 ? -24.76500 -1.37800  -10.56000 1.000 31.22000 ? 295 ASP A OD2 1 
ATOM   2246 N N   . VAL A 1 294 ? -23.67600 -6.06000  -12.73200 1.000 35.77000 ? 296 VAL A N   1 
ATOM   2247 C CA  . VAL A 1 294 ? -23.32200 -7.49300  -12.56200 1.000 35.94000 ? 296 VAL A CA  1 
ATOM   2248 C C   . VAL A 1 294 ? -22.53800 -7.97200  -13.78500 1.000 41.19000 ? 296 VAL A C   1 
ATOM   2249 O O   . VAL A 1 294 ? -21.50200 -8.60500  -13.61200 1.000 42.29000 ? 296 VAL A O   1 
ATOM   2250 C CB  . VAL A 1 294 ? -24.58900 -8.32800  -12.29700 1.000 32.88000 ? 296 VAL A CB  1 
ATOM   2251 C CG1 . VAL A 1 294 ? -24.36900 -9.80800  -12.54100 1.000 35.81000 ? 296 VAL A CG1 1 
ATOM   2252 C CG2 . VAL A 1 294 ? -25.14900 -8.07500  -10.90800 1.000 28.36000 ? 296 VAL A CG2 1 
ATOM   2253 N N   . VAL A 1 295 ? -22.99000 -7.60500  -14.96800 1.000 42.94000 ? 297 VAL A N   1 
ATOM   2254 C CA  . VAL A 1 295 ? -22.28600 -8.01500  -16.20500 1.000 47.00000 ? 297 VAL A CA  1 
ATOM   2255 C C   . VAL A 1 295 ? -20.86900 -7.42800  -16.19700 1.000 47.27000 ? 297 VAL A C   1 
ATOM   2256 O O   . VAL A 1 295 ? -19.92700 -8.13900  -16.51400 1.000 53.80000 ? 297 VAL A O   1 
ATOM   2257 C CB  . VAL A 1 295 ? -23.08900 -7.59300  -17.44400 1.000 46.18000 ? 297 VAL A CB  1 
ATOM   2258 C CG1 . VAL A 1 295 ? -22.33200 -7.87000  -18.73200 1.000 48.80000 ? 297 VAL A CG1 1 
ATOM   2259 C CG2 . VAL A 1 295 ? -24.44700 -8.26900  -17.47800 1.000 45.38000 ? 297 VAL A CG2 1 
ATOM   2260 N N   . ARG A 1 296 ? -20.72100 -6.18500  -15.78600 1.000 48.65000 ? 298 ARG A N   1 
ATOM   2261 C CA  . ARG A 1 296 ? -19.39900 -5.52500  -15.80000 1.000 50.56000 ? 298 ARG A CA  1 
ATOM   2262 C C   . ARG A 1 296 ? -18.43500 -6.21200  -14.84600 1.000 48.32000 ? 298 ARG A C   1 
ATOM   2263 O O   . ARG A 1 296 ? -17.27800 -6.34600  -15.19500 1.000 55.82000 ? 298 ARG A O   1 
ATOM   2264 C CB  . ARG A 1 296 ? -19.56200 -4.07000  -15.36400 1.000 45.21000 ? 298 ARG A CB  1 
ATOM   2265 N N   . GLN A 1 297 ? -18.89600 -6.58100  -13.66500 1.000 30.00000 ? 299 GLN A N   1 
ATOM   2266 C CA  . GLN A 1 297 ? -18.00100 -7.17000  -12.63900 1.000 30.00000 ? 299 GLN A CA  1 
ATOM   2267 C C   . GLN A 1 297 ? -17.92000 -8.70000  -12.79500 1.000 30.00000 ? 299 GLN A C   1 
ATOM   2268 O O   . GLN A 1 297 ? -18.24600 -9.20600  -13.87900 1.000 30.00000 ? 299 GLN A O   1 
ATOM   2269 C CB  . GLN A 1 297 ? -18.48700 -6.73000  -11.26300 1.000 30.00000 ? 299 GLN A CB  1 
ATOM   2270 C CG  . GLN A 1 297 ? -17.54600 -7.12000  -10.13800 1.000 30.00000 ? 299 GLN A CG  1 
ATOM   2271 C CD  . GLN A 1 297 ? -18.06000 -6.68600  -8.79100  1.000 30.00000 ? 299 GLN A CD  1 
ATOM   2272 O OE1 . GLN A 1 297 ? -17.61100 -7.16000  -7.75400  1.000 30.00000 ? 299 GLN A OE1 1 
ATOM   2273 N NE2 . GLN A 1 297 ? -19.02400 -5.78400  -8.80100  1.000 30.00000 ? 299 GLN A NE2 1 
ATOM   2274 N N   . PHE B 1 1   ? -23.36600 5.35500   6.92900   1.000 55.29000 ? 3   PHE B N   1 
ATOM   2275 C CA  . PHE B 1 1   ? -22.02000 4.78200   7.01400   1.000 50.70000 ? 3   PHE B CA  1 
ATOM   2276 C C   . PHE B 1 1   ? -21.75600 3.78700   5.89300   1.000 47.83000 ? 3   PHE B C   1 
ATOM   2277 O O   . PHE B 1 1   ? -22.30200 2.68700   5.87800   1.000 52.56000 ? 3   PHE B O   1 
ATOM   2278 C CB  . PHE B 1 1   ? -21.78800 4.10000   8.36500   1.000 49.31000 ? 3   PHE B CB  1 
ATOM   2279 C CG  . PHE B 1 1   ? -20.36000 4.14000   8.80700   1.000 47.30000 ? 3   PHE B CG  1 
ATOM   2280 C CD1 . PHE B 1 1   ? -19.75000 5.35300   9.07800   1.000 44.58000 ? 3   PHE B CD1 1 
ATOM   2281 C CD2 . PHE B 1 1   ? -19.61100 2.97700   8.91400   1.000 44.90000 ? 3   PHE B CD2 1 
ATOM   2282 C CE1 . PHE B 1 1   ? -18.43400 5.41800   9.47400   1.000 44.07000 ? 3   PHE B CE1 1 
ATOM   2283 C CE2 . PHE B 1 1   ? -18.28400 3.03900   9.30800   1.000 43.66000 ? 3   PHE B CE2 1 
ATOM   2284 C CZ  . PHE B 1 1   ? -17.69800 4.27200   9.58800   1.000 43.55000 ? 3   PHE B CZ  1 
ATOM   2285 N N   . ARG B 1 2   ? -20.91000 4.20200   4.96100   1.000 42.94000 ? 4   ARG B N   1 
ATOM   2286 C CA  . ARG B 1 2   ? -20.54900 3.42900   3.78600   1.000 41.92000 ? 4   ARG B CA  1 
ATOM   2287 C C   . ARG B 1 2   ? -19.07200 3.05900   3.85700   1.000 37.28000 ? 4   ARG B C   1 
ATOM   2288 O O   . ARG B 1 2   ? -18.27800 3.74900   4.49400   1.000 35.62000 ? 4   ARG B O   1 
ATOM   2289 C CB  . ARG B 1 2   ? -20.81600 4.23900   2.51100   1.000 42.29000 ? 4   ARG B CB  1 
ATOM   2290 C CG  . ARG B 1 2   ? -22.28800 4.57100   2.25300   1.000 43.07000 ? 4   ARG B CG  1 
ATOM   2291 C CD  . ARG B 1 2   ? -22.67700 4.04500   0.89000   1.000 37.20000 ? 4   ARG B CD  1 
ATOM   2292 N NE  . ARG B 1 2   ? -24.08600 4.23400   0.56300   1.000 34.02000 ? 4   ARG B NE  1 
ATOM   2293 C CZ  . ARG B 1 2   ? -24.80800 3.32900   -0.09700  1.000 37.77000 ? 4   ARG B CZ  1 
ATOM   2294 N NH1 . ARG B 1 2   ? -24.24900 2.17700   -0.47300  1.000 39.98000 ? 4   ARG B NH1 1 
ATOM   2295 N NH2 . ARG B 1 2   ? -26.08100 3.55900   -0.37600  1.000 35.32000 ? 4   ARG B NH2 1 
ATOM   2296 N N   . LYS B 1 3   ? -18.71100 1.95700   3.21300   1.000 38.25000 ? 5   LYS B N   1 
ATOM   2297 C CA  . LYS B 1 3   ? -17.30700 1.63300   3.00600   1.000 42.11000 ? 5   LYS B CA  1 
ATOM   2298 C C   . LYS B 1 3   ? -16.77300 2.56900   1.93000   1.000 39.21000 ? 5   LYS B C   1 
ATOM   2299 O O   . LYS B 1 3   ? -17.15800 2.46800   0.75900   1.000 40.79000 ? 5   LYS B O   1 
ATOM   2300 C CB  . LYS B 1 3   ? -17.13700 0.17000   2.61500   1.000 38.06000 ? 5   LYS B CB  1 
ATOM   2301 C CG  . LYS B 1 3   ? -15.78600 -0.40500  3.03200   1.000 44.98000 ? 5   LYS B CG  1 
ATOM   2302 C CD  . LYS B 1 3   ? -15.81500 -1.91400  3.07600   1.000 43.49000 ? 5   LYS B CD  1 
ATOM   2303 C CE  . LYS B 1 3   ? -16.59200 -2.42400  4.28400   1.000 48.01000 ? 5   LYS B CE  1 
ATOM   2304 N NZ  . LYS B 1 3   ? -16.59500 -3.92100  4.34800   1.000 48.00000 ? 5   LYS B NZ  1 
ATOM   2305 N N   . MET B 1 4   ? -15.92200 3.50500   2.32500   1.000 35.33000 ? 6   MET B N   1 
ATOM   2306 C CA  . MET B 1 4   ? -15.45100 4.54400   1.42000   1.000 33.36000 ? 6   MET B CA  1 
ATOM   2307 C C   . MET B 1 4   ? -14.01300 4.26000   1.00600   1.000 31.90000 ? 6   MET B C   1 
ATOM   2308 O O   . MET B 1 4   ? -13.15700 3.98400   1.85400   1.000 31.23000 ? 6   MET B O   1 
ATOM   2309 C CB  . MET B 1 4   ? -15.54800 5.92400   2.06600   1.000 37.03000 ? 6   MET B CB  1 
ATOM   2310 C CG  . MET B 1 4   ? -16.93000 6.26800   2.61200   1.000 41.96000 ? 6   MET B CG  1 
ATOM   2311 S SD  . MET B 1 4   ? -17.09300 8.04600   2.94200   1.000 55.24000 ? 6   MET B SD  1 
ATOM   2312 C CE  . MET B 1 4   ? -16.65900 8.72600   1.35400   1.000 37.26000 ? 6   MET B CE  1 
ATOM   2313 N N   . ALA B 1 5   ? -13.75300 4.33400   -0.29000  1.000 28.85000 ? 7   ALA B N   1 
ATOM   2314 C CA  . ALA B 1 5   ? -12.39800 4.25300   -0.80400  1.000 27.25000 ? 7   ALA B CA  1 
ATOM   2315 C C   . ALA B 1 5   ? -11.79000 5.64600   -0.90600  1.000 30.28000 ? 7   ALA B C   1 
ATOM   2316 O O   . ALA B 1 5   ? -12.50100 6.65400   -0.95500  1.000 27.95000 ? 7   ALA B O   1 
ATOM   2317 C CB  . ALA B 1 5   ? -12.38800 3.57300   -2.17000  1.000 26.36000 ? 7   ALA B CB  1 
ATOM   2318 N N   . PHE B 1 6   ? -10.45600 5.70400   -0.94100  1.000 28.16000 ? 8   PHE B N   1 
ATOM   2319 C CA  . PHE B 1 6   ? -9.81600  6.99100   -1.18800  1.000 28.53000 ? 8   PHE B CA  1 
ATOM   2320 C C   . PHE B 1 6   ? -10.09200 7.43800   -2.62200  1.000 27.89000 ? 8   PHE B C   1 
ATOM   2321 O O   . PHE B 1 6   ? -10.29100 6.60600   -3.50900  1.000 27.65000 ? 8   PHE B O   1 
ATOM   2322 C CB  . PHE B 1 6   ? -8.29500  6.92600   -0.95500  1.000 28.51000 ? 8   PHE B CB  1 
ATOM   2323 C CG  . PHE B 1 6   ? -7.90700  6.84200   0.49400   1.000 27.33000 ? 8   PHE B CG  1 
ATOM   2324 C CD1 . PHE B 1 6   ? -7.93100  7.96400   1.29700   1.000 31.70000 ? 8   PHE B CD1 1 
ATOM   2325 C CD2 . PHE B 1 6   ? -7.54500  5.62500   1.05800   1.000 32.11000 ? 8   PHE B CD2 1 
ATOM   2326 C CE1 . PHE B 1 6   ? -7.58600  7.89300   2.64500   1.000 35.31000 ? 8   PHE B CE1 1 
ATOM   2327 C CE2 . PHE B 1 6   ? -7.20000  5.53700   2.41100   1.000 33.99000 ? 8   PHE B CE2 1 
ATOM   2328 C CZ  . PHE B 1 6   ? -7.21800  6.67700   3.19700   1.000 35.43000 ? 8   PHE B CZ  1 
ATOM   2329 N N   . PRO B 1 7   ? -10.11700 8.74600   -2.88000  1.000 28.61000 ? 9   PRO B N   1 
ATOM   2330 C CA  . PRO B 1 7   ? -10.10700 9.20300   -4.27500  1.000 29.64000 ? 9   PRO B CA  1 
ATOM   2331 C C   . PRO B 1 7   ? -8.86500  8.65600   -4.96100  1.000 27.56000 ? 9   PRO B C   1 
ATOM   2332 O O   . PRO B 1 7   ? -7.76800  8.70500   -4.41100  1.000 29.09000 ? 9   PRO B O   1 
ATOM   2333 C CB  . PRO B 1 7   ? -10.06800 10.73600  -4.16300  1.000 27.68000 ? 9   PRO B CB  1 
ATOM   2334 C CG  . PRO B 1 7   ? -10.39300 11.05000  -2.72300  1.000 31.59000 ? 9   PRO B CG  1 
ATOM   2335 C CD  . PRO B 1 7   ? -9.98600  9.85800   -1.91900  1.000 29.39000 ? 9   PRO B CD  1 
ATOM   2336 N N   . SER B 1 8   ? -9.03900  8.13500   -6.16300  1.000 30.39000 ? 10  SER B N   1 
ATOM   2337 C CA  . SER B 1 8   ? -8.00600  7.31400   -6.78200  1.000 26.29000 ? 10  SER B CA  1 
ATOM   2338 C C   . SER B 1 8   ? -7.22000  8.03000   -7.86800  1.000 28.96000 ? 10  SER B C   1 
ATOM   2339 O O   . SER B 1 8   ? -6.34600  7.40800   -8.47900  1.000 28.53000 ? 10  SER B O   1 
ATOM   2340 C CB  . SER B 1 8   ? -8.63500  6.04700   -7.36400  1.000 28.84000 ? 10  SER B CB  1 
ATOM   2341 O OG  . SER B 1 8   ? -9.57300  6.36200   -8.37700  1.000 29.92000 ? 10  SER B OG  1 
ATOM   2342 N N   . GLY B 1 9   ? -7.49900  9.32200   -8.11400  1.000 27.90000 ? 11  GLY B N   1 
ATOM   2343 C CA  . GLY B 1 9   ? -6.87100  10.00800  -9.23300  1.000 29.23000 ? 11  GLY B CA  1 
ATOM   2344 C C   . GLY B 1 9   ? -5.35100  9.97000   -9.20600  1.000 30.46000 ? 11  GLY B C   1 
ATOM   2345 O O   . GLY B 1 9   ? -4.70800  9.78400   -10.24200 1.000 31.75000 ? 11  GLY B O   1 
ATOM   2346 N N   . LYS B 1 10  ? -4.75300  10.15900  -8.03100  1.000 27.33000 ? 12  LYS B N   1 
ATOM   2347 C CA  . LYS B 1 10  ? -3.29600  10.17500  -7.95500  1.000 28.04000 ? 12  LYS B CA  1 
ATOM   2348 C C   . LYS B 1 10  ? -2.69100  8.85200   -8.40800  1.000 30.45000 ? 12  LYS B C   1 
ATOM   2349 O O   . LYS B 1 10  ? -1.58100  8.83100   -8.95400  1.000 30.67000 ? 12  LYS B O   1 
ATOM   2350 C CB  . LYS B 1 10  ? -2.85400  10.51000  -6.53100  1.000 30.20000 ? 12  LYS B CB  1 
ATOM   2351 C CG  . LYS B 1 10  ? -3.03200  11.99000  -6.19200  1.000 30.80000 ? 12  LYS B CG  1 
ATOM   2352 C CD  . LYS B 1 10  ? -2.36700  12.36600  -4.87700  1.000 35.24000 ? 12  LYS B CD  1 
ATOM   2353 C CE  . LYS B 1 10  ? -2.39000  13.89700  -4.65900  1.000 36.38000 ? 12  LYS B CE  1 
ATOM   2354 N NZ  . LYS B 1 10  ? -3.71500  14.48900  -5.04100  1.000 39.38000 ? 12  LYS B NZ  1 
ATOM   2355 N N   . VAL B 1 11  ? -3.42200  7.75500   -8.23000  1.000 28.15000 ? 13  VAL B N   1 
ATOM   2356 C CA  . VAL B 1 11  ? -2.95600  6.42900   -8.60800  1.000 29.35000 ? 13  VAL B CA  1 
ATOM   2357 C C   . VAL B 1 11  ? -3.30700  6.09900   -10.05800 1.000 29.85000 ? 13  VAL B C   1 
ATOM   2358 O O   . VAL B 1 11  ? -2.53700  5.42300   -10.74800 1.000 30.19000 ? 13  VAL B O   1 
ATOM   2359 C CB  . VAL B 1 11  ? -3.55800  5.40000   -7.62500  1.000 26.77000 ? 13  VAL B CB  1 
ATOM   2360 C CG1 . VAL B 1 11  ? -3.18900  3.97200   -8.03000  1.000 29.59000 ? 13  VAL B CG1 1 
ATOM   2361 C CG2 . VAL B 1 11  ? -3.11900  5.71700   -6.19400  1.000 27.15000 ? 13  VAL B CG2 1 
ATOM   2362 N N   . GLU B 1 12  ? -4.46900  6.55700   -10.54200 1.000 28.28000 ? 14  GLU B N   1 
ATOM   2363 C CA  . GLU B 1 12  ? -4.85600  6.29400   -11.93100 1.000 29.54000 ? 14  GLU B CA  1 
ATOM   2364 C C   . GLU B 1 12  ? -3.77300  6.73600   -12.90900 1.000 29.89000 ? 14  GLU B C   1 
ATOM   2365 O O   . GLU B 1 12  ? -3.48700  6.04500   -13.89300 1.000 32.34000 ? 14  GLU B O   1 
ATOM   2366 C CB  . GLU B 1 12  ? -6.17100  7.01800   -12.26700 1.000 29.71000 ? 14  GLU B CB  1 
ATOM   2367 C CG  . GLU B 1 12  ? -7.41900  6.44300   -11.60300 1.000 29.55000 ? 14  GLU B CG  1 
ATOM   2368 C CD  . GLU B 1 12  ? -8.61100  7.41100   -11.67800 1.000 30.51000 ? 14  GLU B CD  1 
ATOM   2369 O OE1 . GLU B 1 12  ? -9.18400  7.78200   -10.62600 1.000 29.25000 ? 14  GLU B OE1 1 
ATOM   2370 O OE2 . GLU B 1 12  ? -8.97600  7.79900   -12.80000 1.000 31.23000 ? 14  GLU B OE2 1 
ATOM   2371 N N   . GLY B 1 13  ? -3.17200  7.89500   -12.65600 1.000 27.00000 ? 15  GLY B N   1 
ATOM   2372 C CA  . GLY B 1 13  ? -2.10900  8.43600   -13.47100 1.000 32.91000 ? 15  GLY B CA  1 
ATOM   2373 C C   . GLY B 1 13  ? -0.82100  7.64300   -13.46500 1.000 31.10000 ? 15  GLY B C   1 
ATOM   2374 O O   . GLY B 1 13  ? 0.08800   7.98800   -14.22100 1.000 35.45000 ? 15  GLY B O   1 
ATOM   2375 N N   . CYS B 1 14  ? -0.71400  6.59000   -12.65200 1.000 32.88000 ? 16  CYS B N   1 
ATOM   2376 C CA  . CYS B 1 14  ? 0.47300   5.73700   -12.63300 1.000 31.12000 ? 16  CYS B CA  1 
ATOM   2377 C C   . CYS B 1 14  ? 0.26700   4.37600   -13.28700 1.000 32.06000 ? 16  CYS B C   1 
ATOM   2378 O O   . CYS B 1 14  ? 1.22300   3.59400   -13.35600 1.000 33.97000 ? 16  CYS B O   1 
ATOM   2379 C CB  . CYS B 1 14  ? 0.94600   5.51600   -11.19500 1.000 30.80000 ? 16  CYS B CB  1 
ATOM   2380 S SG  . CYS B 1 14  ? 1.12300   7.00400   -10.22800 1.000 33.15000 ? 16  CYS B SG  1 
ATOM   2381 N N   . MET B 1 15  ? -0.94100  4.05600   -13.75100 1.000 34.70000 ? 17  MET B N   1 
ATOM   2382 C CA  . MET B 1 15  ? -1.24700  2.70100   -14.20300 1.000 31.04000 ? 17  MET B CA  1 
ATOM   2383 C C   . MET B 1 15  ? -0.86500  2.52900   -15.66700 1.000 35.28000 ? 17  MET B C   1 
ATOM   2384 O O   . MET B 1 15  ? -1.26600  3.32700   -16.51900 1.000 36.81000 ? 17  MET B O   1 
ATOM   2385 C CB  . MET B 1 15  ? -2.72900  2.38700   -14.01700 1.000 33.34000 ? 17  MET B CB  1 
ATOM   2386 C CG  . MET B 1 15  ? -3.18000  2.26400   -12.56800 1.000 32.86000 ? 17  MET B CG  1 
ATOM   2387 S SD  . MET B 1 15  ? -1.98100  1.47300   -11.47800 1.000 32.92000 ? 17  MET B SD  1 
ATOM   2388 C CE  . MET B 1 15  ? -1.94400  -0.21500  -12.08900 1.000 28.57000 ? 17  MET B CE  1 
ATOM   2389 N N   . VAL B 1 16  ? -0.09300  1.48100   -15.95600 1.000 33.27000 ? 18  VAL B N   1 
ATOM   2390 C CA  . VAL B 1 16  ? 0.32200   1.16300   -17.31600 1.000 36.58000 ? 18  VAL B CA  1 
ATOM   2391 C C   . VAL B 1 16  ? 0.07300   -0.31600  -17.58500 1.000 35.67000 ? 18  VAL B C   1 
ATOM   2392 O O   . VAL B 1 16  ? -0.17700  -1.10800  -16.67700 1.000 33.65000 ? 18  VAL B O   1 
ATOM   2393 C CB  . VAL B 1 16  ? 1.80700   1.51300   -17.57400 1.000 36.44000 ? 18  VAL B CB  1 
ATOM   2394 C CG1 . VAL B 1 16  ? 2.07900   2.97400   -17.22400 1.000 37.91000 ? 18  VAL B CG1 1 
ATOM   2395 C CG2 . VAL B 1 16  ? 2.72500   0.58400   -16.78600 1.000 35.19000 ? 18  VAL B CG2 1 
ATOM   2396 N N   . GLN B 1 17  ? 0.11700   -0.67800  -18.85800 1.000 38.01000 ? 19  GLN B N   1 
ATOM   2397 C CA  . GLN B 1 17  ? 0.01800   -2.06700  -19.27800 1.000 38.69000 ? 19  GLN B CA  1 
ATOM   2398 C C   . GLN B 1 17  ? 1.41800   -2.60800  -19.52800 1.000 40.09000 ? 19  GLN B C   1 
ATOM   2399 O O   . GLN B 1 17  ? 2.27200   -1.89900  -20.06900 1.000 43.43000 ? 19  GLN B O   1 
ATOM   2400 C CB  . GLN B 1 17  ? -0.82000  -2.19200  -20.55000 1.000 41.93000 ? 19  GLN B CB  1 
ATOM   2401 C CG  . GLN B 1 17  ? -1.03400  -3.61500  -21.03600 1.000 42.19000 ? 19  GLN B CG  1 
ATOM   2402 C CD  . GLN B 1 17  ? -1.78500  -3.64400  -22.35200 1.000 50.27000 ? 19  GLN B CD  1 
ATOM   2403 O OE1 . GLN B 1 17  ? -2.56300  -4.55300  -22.61900 1.000 52.48000 ? 19  GLN B OE1 1 
ATOM   2404 N NE2 . GLN B 1 17  ? -1.55300  -2.63500  -23.18300 1.000 58.11000 ? 19  GLN B NE2 1 
ATOM   2405 N N   . VAL B 1 18  ? 1.66000   -3.85200  -19.11600 1.000 39.30000 ? 20  VAL B N   1 
ATOM   2406 C CA  . VAL B 1 18  ? 2.94600   -4.51000  -19.34200 1.000 42.13000 ? 20  VAL B CA  1 
ATOM   2407 C C   . VAL B 1 18  ? 2.67600   -5.85000  -20.00200 1.000 43.39000 ? 20  VAL B C   1 
ATOM   2408 O O   . VAL B 1 18  ? 1.95300   -6.68600  -19.44700 1.000 43.88000 ? 20  VAL B O   1 
ATOM   2409 C CB  . VAL B 1 18  ? 3.74800   -4.71400  -18.04600 1.000 38.18000 ? 20  VAL B CB  1 
ATOM   2410 C CG1 . VAL B 1 18  ? 5.06300   -5.42500  -18.34600 1.000 38.42000 ? 20  VAL B CG1 1 
ATOM   2411 C CG2 . VAL B 1 18  ? 4.00600   -3.39400  -17.36900 1.000 34.32000 ? 20  VAL B CG2 1 
ATOM   2412 N N   . THR B 1 19  ? 3.26000   -6.06100  -21.17500 1.000 47.22000 ? 21  THR B N   1 
ATOM   2413 C CA  . THR B 1 19  ? 3.13200   -7.32300  -21.88800 1.000 48.76000 ? 21  THR B CA  1 
ATOM   2414 C C   . THR B 1 19  ? 4.50600   -7.95000  -22.02400 1.000 47.96000 ? 21  THR B C   1 
ATOM   2415 O O   . THR B 1 19  ? 5.45200   -7.29000  -22.46600 1.000 48.69000 ? 21  THR B O   1 
ATOM   2416 C CB  . THR B 1 19  ? 2.50700   -7.12800  -23.26800 1.000 50.58000 ? 21  THR B CB  1 
ATOM   2417 O OG1 . THR B 1 19  ? 1.13000   -6.76000  -23.11900 1.000 49.86000 ? 21  THR B OG1 1 
ATOM   2418 C CG2 . THR B 1 19  ? 2.60300   -8.42100  -24.07800 1.000 51.07000 ? 21  THR B CG2 1 
ATOM   2419 N N   . CYS B 1 20  ? 4.62300   -9.20900  -21.61600 1.000 48.68000 ? 22  CYS B N   1 
ATOM   2420 C CA  . CYS B 1 20  ? 5.83800   -9.98300  -21.83400 1.000 51.57000 ? 22  CYS B CA  1 
ATOM   2421 C C   . CYS B 1 20  ? 5.43800   -11.20800 -22.64000 1.000 51.98000 ? 22  CYS B C   1 
ATOM   2422 O O   . CYS B 1 20  ? 4.75700   -12.10400 -22.12500 1.000 49.82000 ? 22  CYS B O   1 
ATOM   2423 C CB  . CYS B 1 20  ? 6.51600   -10.36700 -20.52000 1.000 50.42000 ? 22  CYS B CB  1 
ATOM   2424 S SG  . CYS B 1 20  ? 8.13800   -11.16800 -20.74000 1.000 50.14000 ? 22  CYS B SG  1 
ATOM   2425 N N   . GLY B 1 21  ? 5.84100   -11.22800 -23.90700 1.000 52.93000 ? 23  GLY B N   1 
ATOM   2426 C CA  . GLY B 1 21  ? 5.44300   -12.27900 -24.81600 1.000 50.43000 ? 23  GLY B CA  1 
ATOM   2427 C C   . GLY B 1 21  ? 3.94400   -12.35800 -24.97800 1.000 51.49000 ? 23  GLY B C   1 
ATOM   2428 O O   . GLY B 1 21  ? 3.32400   -11.47600 -25.57700 1.000 54.51000 ? 23  GLY B O   1 
ATOM   2429 N N   . THR B 1 22  ? 3.34000   -13.40300 -24.42700 1.000 53.16000 ? 24  THR B N   1 
ATOM   2430 C CA  . THR B 1 22  ? 1.91300   -13.62000 -24.59300 1.000 54.34000 ? 24  THR B CA  1 
ATOM   2431 C C   . THR B 1 22  ? 1.07700   -13.09700 -23.42800 1.000 52.36000 ? 24  THR B C   1 
ATOM   2432 O O   . THR B 1 22  ? -0.14000  -12.96600 -23.57800 1.000 54.01000 ? 24  THR B O   1 
ATOM   2433 C CB  . THR B 1 22  ? 1.63600   -15.11400 -24.79800 1.000 54.12000 ? 24  THR B CB  1 
ATOM   2434 O OG1 . THR B 1 22  ? 0.30000   -15.29100 -25.28000 1.000 56.99000 ? 24  THR B OG1 1 
ATOM   2435 C CG2 . THR B 1 22  ? 1.82400   -15.88600 -23.49200 1.000 54.46000 ? 24  THR B CG2 1 
ATOM   2436 N N   . THR B 1 23  ? 1.69500   -12.77600 -22.29200 1.000 52.05000 ? 25  THR B N   1 
ATOM   2437 C CA  . THR B 1 23  ? 0.98000   -12.41300 -21.07400 1.000 49.47000 ? 25  THR B CA  1 
ATOM   2438 C C   . THR B 1 23  ? 0.92700   -10.89900 -20.90700 1.000 48.72000 ? 25  THR B C   1 
ATOM   2439 O O   . THR B 1 23  ? 1.92100   -10.20000 -21.13200 1.000 46.58000 ? 25  THR B O   1 
ATOM   2440 C CB  . THR B 1 23  ? 1.64300   -13.04100 -19.84200 1.000 49.68000 ? 25  THR B CB  1 
ATOM   2441 O OG1 . THR B 1 23  ? 1.44200   -14.45600 -19.85900 1.000 50.03000 ? 25  THR B OG1 1 
ATOM   2442 C CG2 . THR B 1 23  ? 1.06300   -12.47300 -18.54700 1.000 45.47000 ? 25  THR B CG2 1 
ATOM   2443 N N   . THR B 1 24  ? -0.24100  -10.40800 -20.49600 1.000 48.34000 ? 26  THR B N   1 
ATOM   2444 C CA  . THR B 1 24  ? -0.47300  -9.00300  -20.20600 1.000 43.20000 ? 26  THR B CA  1 
ATOM   2445 C C   . THR B 1 24  ? -0.99700  -8.84500  -18.78400 1.000 40.26000 ? 26  THR B C   1 
ATOM   2446 O O   . THR B 1 24  ? -1.84400  -9.62200  -18.33600 1.000 42.33000 ? 26  THR B O   1 
ATOM   2447 C CB  . THR B 1 24  ? -1.47800  -8.40900  -21.19100 1.000 44.75000 ? 26  THR B CB  1 
ATOM   2448 O OG1 . THR B 1 24  ? -0.85200  -8.25500  -22.46500 1.000 50.25000 ? 26  THR B OG1 1 
ATOM   2449 C CG2 . THR B 1 24  ? -1.97000  -7.05100  -20.71200 1.000 45.51000 ? 26  THR B CG2 1 
ATOM   2450 N N   . LEU B 1 25  ? -0.48500  -7.84200  -18.07700 1.000 42.30000 ? 27  LEU B N   1 
ATOM   2451 C CA  . LEU B 1 25  ? -1.03500  -7.44300  -16.79000 1.000 33.87000 ? 27  LEU B CA  1 
ATOM   2452 C C   . LEU B 1 25  ? -0.73700  -5.95600  -16.60400 1.000 36.03000 ? 27  LEU B C   1 
ATOM   2453 O O   . LEU B 1 25  ? -0.36000  -5.26100  -17.55100 1.000 36.43000 ? 27  LEU B O   1 
ATOM   2454 C CB  . LEU B 1 25  ? -0.47900  -8.32700  -15.66300 1.000 34.93000 ? 27  LEU B CB  1 
ATOM   2455 C CG  . LEU B 1 25  ? 1.00100   -8.73600  -15.69600 1.000 34.52000 ? 27  LEU B CG  1 
ATOM   2456 C CD1 . LEU B 1 25  ? 1.93600   -7.52700  -15.49300 1.000 33.00000 ? 27  LEU B CD1 1 
ATOM   2457 C CD2 . LEU B 1 25  ? 1.27900   -9.83000  -14.65900 1.000 30.44000 ? 27  LEU B CD2 1 
ATOM   2458 N N   . ASN B 1 26  ? -0.91400  -5.47000  -15.38000 1.000 29.30000 ? 28  ASN B N   1 
ATOM   2459 C CA  . ASN B 1 26  ? -0.79000  -4.05800  -15.06500 1.000 32.62000 ? 28  ASN B CA  1 
ATOM   2460 C C   . ASN B 1 26  ? 0.54800   -3.78300  -14.40600 1.000 30.86000 ? 28  ASN B C   1 
ATOM   2461 O O   . ASN B 1 26  ? 1.11400   -4.64900  -13.74000 1.000 31.74000 ? 28  ASN B O   1 
ATOM   2462 C CB  . ASN B 1 26  ? -1.91100  -3.61000  -14.12800 1.000 28.55000 ? 28  ASN B CB  1 
ATOM   2463 C CG  . ASN B 1 26  ? -3.26400  -4.00200  -14.63300 1.000 31.38000 ? 28  ASN B CG  1 
ATOM   2464 O OD1 . ASN B 1 26  ? -3.78100  -3.37500  -15.55600 1.000 34.62000 ? 28  ASN B OD1 1 
ATOM   2465 N ND2 . ASN B 1 26  ? -3.85100  -5.05200  -14.04800 1.000 31.63000 ? 28  ASN B ND2 1 
ATOM   2466 N N   . GLY B 1 27  ? 1.03700   -2.55400  -14.59100 1.000 31.60000 ? 29  GLY B N   1 
ATOM   2467 C CA  . GLY B 1 27  ? 2.22100   -2.09800  -13.90200 1.000 31.82000 ? 29  GLY B CA  1 
ATOM   2468 C C   . GLY B 1 27  ? 2.01700   -0.71400  -13.30500 1.000 33.66000 ? 29  GLY B C   1 
ATOM   2469 O O   . GLY B 1 27  ? 1.11100   0.03600   -13.68700 1.000 31.25000 ? 29  GLY B O   1 
ATOM   2470 N N   . LEU B 1 28  ? 2.87900   -0.39800  -12.34000 1.000 30.29000 ? 30  LEU B N   1 
ATOM   2471 C CA  . LEU B 1 28  ? 2.85600   0.87700   -11.64000 1.000 32.82000 ? 30  LEU B CA  1 
ATOM   2472 C C   . LEU B 1 28  ? 4.04800   1.71200   -12.09300 1.000 34.24000 ? 30  LEU B C   1 
ATOM   2473 O O   . LEU B 1 28  ? 5.19300   1.31100   -11.88000 1.000 29.40000 ? 30  LEU B O   1 
ATOM   2474 C CB  . LEU B 1 28  ? 2.88800   0.66800   -10.12500 1.000 31.31000 ? 30  LEU B CB  1 
ATOM   2475 C CG  . LEU B 1 28  ? 2.59000   1.97200   -9.34700  1.000 29.24000 ? 30  LEU B CG  1 
ATOM   2476 C CD1 . LEU B 1 28  ? 1.14600   2.42700   -9.54300  1.000 27.80000 ? 30  LEU B CD1 1 
ATOM   2477 C CD2 . LEU B 1 28  ? 2.89700   1.75900   -7.87900  1.000 27.48000 ? 30  LEU B CD2 1 
ATOM   2478 N N   . TRP B 1 29  ? 3.77200   2.87400   -12.71000 1.000 31.53000 ? 31  TRP B N   1 
ATOM   2479 C CA  . TRP B 1 29  ? 4.80300   3.73100   -13.30700 1.000 30.82000 ? 31  TRP B CA  1 
ATOM   2480 C C   . TRP B 1 29  ? 5.04500   4.90500   -12.37200 1.000 31.66000 ? 31  TRP B C   1 
ATOM   2481 O O   . TRP B 1 29  ? 4.22900   5.82500   -12.29200 1.000 33.53000 ? 31  TRP B O   1 
ATOM   2482 C CB  . TRP B 1 29  ? 4.36700   4.20900   -14.68700 1.000 32.14000 ? 31  TRP B CB  1 
ATOM   2483 C CG  . TRP B 1 29  ? 5.33700   5.10200   -15.41100 1.000 34.30000 ? 31  TRP B CG  1 
ATOM   2484 C CD1 . TRP B 1 29  ? 6.68700   5.20100   -15.20300 1.000 34.73000 ? 31  TRP B CD1 1 
ATOM   2485 C CD2 . TRP B 1 29  ? 5.03100   6.00100   -16.48500 1.000 37.43000 ? 31  TRP B CD2 1 
ATOM   2486 N NE1 . TRP B 1 29  ? 7.23500   6.11100   -16.07800 1.000 34.77000 ? 31  TRP B NE1 1 
ATOM   2487 C CE2 . TRP B 1 29  ? 6.24100   6.61000   -16.87900 1.000 37.22000 ? 31  TRP B CE2 1 
ATOM   2488 C CE3 . TRP B 1 29  ? 3.85100   6.34400   -17.15800 1.000 39.11000 ? 31  TRP B CE3 1 
ATOM   2489 C CZ2 . TRP B 1 29  ? 6.30200   7.56300   -17.90500 1.000 40.31000 ? 31  TRP B CZ2 1 
ATOM   2490 C CZ3 . TRP B 1 29  ? 3.91500   7.28200   -18.18500 1.000 39.58000 ? 31  TRP B CZ3 1 
ATOM   2491 C CH2 . TRP B 1 29  ? 5.13600   7.88200   -18.54600 1.000 37.27000 ? 31  TRP B CH2 1 
ATOM   2492 N N   . LEU B 1 30  ? 6.16300   4.86600   -11.65500 1.000 31.22000 ? 32  LEU B N   1 
ATOM   2493 C CA  . LEU B 1 30  ? 6.55800   5.92000   -10.73800 1.000 30.19000 ? 32  LEU B CA  1 
ATOM   2494 C C   . LEU B 1 30  ? 7.94500   6.39700   -11.13700 1.000 34.67000 ? 32  LEU B C   1 
ATOM   2495 O O   . LEU B 1 30  ? 8.88600   5.59800   -11.16800 1.000 31.99000 ? 32  LEU B O   1 
ATOM   2496 C CB  . LEU B 1 30  ? 6.56400   5.42500   -9.29700  1.000 30.10000 ? 32  LEU B CB  1 
ATOM   2497 C CG  . LEU B 1 30  ? 5.23200   4.89100   -8.77700  1.000 30.79000 ? 32  LEU B CG  1 
ATOM   2498 C CD1 . LEU B 1 30  ? 5.46400   4.21000   -7.45600  1.000 27.06000 ? 32  LEU B CD1 1 
ATOM   2499 C CD2 . LEU B 1 30  ? 4.27600   6.05500   -8.62400  1.000 29.12000 ? 32  LEU B CD2 1 
ATOM   2500 N N   . ASP B 1 31  ? 8.06900   7.69800   -11.41900 1.000 35.14000 ? 33  ASP B N   1 
ATOM   2501 C CA  . ASP B 1 31  ? 9.29200   8.27000   -11.99800 1.000 35.31000 ? 33  ASP B CA  1 
ATOM   2502 C C   . ASP B 1 31  ? 9.64900   7.43000   -13.22600 1.000 35.07000 ? 33  ASP B C   1 
ATOM   2503 O O   . ASP B 1 31  ? 8.78100   7.19300   -14.07700 1.000 32.87000 ? 33  ASP B O   1 
ATOM   2504 C CB  . ASP B 1 31  ? 10.34800  8.35800   -10.91900 1.000 37.62000 ? 33  ASP B CB  1 
ATOM   2505 C CG  . ASP B 1 31  ? 9.99100   9.37700   -9.85800  1.000 38.98000 ? 33  ASP B CG  1 
ATOM   2506 O OD1 . ASP B 1 31  ? 9.60200   10.50700  -10.23200 1.000 45.98000 ? 33  ASP B OD1 1 
ATOM   2507 O OD2 . ASP B 1 31  ? 10.09400  9.05000   -8.66100  1.000 41.79000 ? 33  ASP B OD2 1 
ATOM   2508 N N   . ASP B 1 32  ? 10.87600  6.93200   -13.36100 1.000 35.35000 ? 34  ASP B N   1 
ATOM   2509 C CA  . ASP B 1 32  ? 11.22200  6.19400   -14.57000 1.000 36.10000 ? 34  ASP B CA  1 
ATOM   2510 C C   . ASP B 1 32  ? 11.32400  4.68900   -14.32600 1.000 37.68000 ? 34  ASP B C   1 
ATOM   2511 O O   . ASP B 1 32  ? 12.13500  4.00800   -14.95700 1.000 38.72000 ? 34  ASP B O   1 
ATOM   2512 C CB  . ASP B 1 32  ? 12.50500  6.74700   -15.19600 1.000 34.46000 ? 34  ASP B CB  1 
ATOM   2513 C CG  . ASP B 1 32  ? 13.72100  6.61700   -14.28400 1.000 42.94000 ? 34  ASP B CG  1 
ATOM   2514 O OD1 . ASP B 1 32  ? 13.59800  6.06900   -13.16800 1.000 41.31000 ? 34  ASP B OD1 1 
ATOM   2515 O OD2 . ASP B 1 32  ? 14.80800  7.07800   -14.68800 1.000 43.86000 ? 34  ASP B OD2 1 
ATOM   2516 N N   . VAL B 1 33  ? 10.49900  4.14400   -13.43200 1.000 35.91000 ? 35  VAL B N   1 
ATOM   2517 C CA  . VAL B 1 33  ? 10.46400  2.69900   -13.20300 1.000 33.15000 ? 35  VAL B CA  1 
ATOM   2518 C C   . VAL B 1 33  ? 9.02100   2.22100   -13.23800 1.000 33.29000 ? 35  VAL B C   1 
ATOM   2519 O O   . VAL B 1 33  ? 8.12500   2.85100   -12.65800 1.000 29.77000 ? 35  VAL B O   1 
ATOM   2520 C CB  . VAL B 1 33  ? 11.12000  2.29000   -11.87000 1.000 33.17000 ? 35  VAL B CB  1 
ATOM   2521 C CG1 . VAL B 1 33  ? 10.94500  0.77500   -11.63700 1.000 30.97000 ? 35  VAL B CG1 1 
ATOM   2522 C CG2 . VAL B 1 33  ? 12.59500  2.64500   -11.87300 1.000 35.15000 ? 35  VAL B CG2 1 
ATOM   2523 N N   . VAL B 1 34  ? 8.79700   1.10900   -13.92200 1.000 29.70000 ? 36  VAL B N   1 
ATOM   2524 C CA  . VAL B 1 34  ? 7.51800   0.40900   -13.88800 1.000 33.98000 ? 36  VAL B CA  1 
ATOM   2525 C C   . VAL B 1 34  ? 7.66500   -0.82300  -13.00600 1.000 30.49000 ? 36  VAL B C   1 
ATOM   2526 O O   . VAL B 1 34  ? 8.58800   -1.61800  -13.19200 1.000 32.61000 ? 36  VAL B O   1 
ATOM   2527 C CB  . VAL B 1 34  ? 7.05300   0.02800   -15.30200 1.000 32.10000 ? 36  VAL B CB  1 
ATOM   2528 C CG1 . VAL B 1 34  ? 5.77200   -0.77700  -15.23100 1.000 32.02000 ? 36  VAL B CG1 1 
ATOM   2529 C CG2 . VAL B 1 34  ? 6.84800   1.28700   -16.14700 1.000 31.72000 ? 36  VAL B CG2 1 
ATOM   2530 N N   . TYR B 1 35  ? 6.75700   -0.97400  -12.04400 1.000 31.56000 ? 37  TYR B N   1 
ATOM   2531 C CA  . TYR B 1 35  ? 6.71300   -2.09500  -11.11700 1.000 31.46000 ? 37  TYR B CA  1 
ATOM   2532 C C   . TYR B 1 35  ? 5.54400   -3.00400  -11.49000 1.000 32.67000 ? 37  TYR B C   1 
ATOM   2533 O O   . TYR B 1 35  ? 4.43800   -2.51600  -11.74700 1.000 30.39000 ? 37  TYR B O   1 
ATOM   2534 C CB  . TYR B 1 35  ? 6.55300   -1.59800  -9.67600  1.000 29.78000 ? 37  TYR B CB  1 
ATOM   2535 C CG  . TYR B 1 35  ? 7.58300   -0.57100  -9.23800  1.000 29.28000 ? 37  TYR B CG  1 
ATOM   2536 C CD1 . TYR B 1 35  ? 7.44800   0.77600   -9.57000  1.000 30.67000 ? 37  TYR B CD1 1 
ATOM   2537 C CD2 . TYR B 1 35  ? 8.67600   -0.94800  -8.46400  1.000 29.43000 ? 37  TYR B CD2 1 
ATOM   2538 C CE1 . TYR B 1 35  ? 8.40400   1.71700   -9.16700  1.000 31.22000 ? 37  TYR B CE1 1 
ATOM   2539 C CE2 . TYR B 1 35  ? 9.63000   -0.01700  -8.04500  1.000 31.35000 ? 37  TYR B CE2 1 
ATOM   2540 C CZ  . TYR B 1 35  ? 9.48800   1.30800   -8.39600  1.000 32.76000 ? 37  TYR B CZ  1 
ATOM   2541 O OH  . TYR B 1 35  ? 10.44500  2.20900   -7.98800  1.000 35.55000 ? 37  TYR B OH  1 
ATOM   2542 N N   . CYS B 1 36  ? 5.78600   -4.31100  -11.51400 1.000 31.45000 ? 38  CYS B N   1 
ATOM   2543 C CA  . CYS B 1 36  ? 4.75100   -5.29300  -11.83300 1.000 32.11000 ? 38  CYS B CA  1 
ATOM   2544 C C   . CYS B 1 36  ? 5.18800   -6.64900  -11.28400 1.000 28.95000 ? 38  CYS B C   1 
ATOM   2545 O O   . CYS B 1 36  ? 6.34800   -6.82300  -10.90400 1.000 31.64000 ? 38  CYS B O   1 
ATOM   2546 C CB  . CYS B 1 36  ? 4.50200   -5.35800  -13.34600 1.000 31.06000 ? 38  CYS B CB  1 
ATOM   2547 S SG  . CYS B 1 36  ? 5.74700   -6.29300  -14.28900 1.000 34.62000 ? 38  CYS B SG  1 
ATOM   2548 N N   . PRO B 1 37  ? 4.27200   -7.61800  -11.17800 1.000 31.31000 ? 39  PRO B N   1 
ATOM   2549 C CA  . PRO B 1 37  ? 4.66400   -8.93100  -10.63400 1.000 30.56000 ? 39  PRO B CA  1 
ATOM   2550 C C   . PRO B 1 37  ? 5.72400   -9.61000  -11.49900 1.000 29.43000 ? 39  PRO B C   1 
ATOM   2551 O O   . PRO B 1 37  ? 5.67600   -9.56200  -12.72600 1.000 29.97000 ? 39  PRO B O   1 
ATOM   2552 C CB  . PRO B 1 37  ? 3.35000   -9.71900  -10.62300 1.000 28.32000 ? 39  PRO B CB  1 
ATOM   2553 C CG  . PRO B 1 37  ? 2.27500   -8.61900  -10.55700 1.000 30.27000 ? 39  PRO B CG  1 
ATOM   2554 C CD  . PRO B 1 37  ? 2.81700   -7.52900  -11.40300 1.000 24.82000 ? 39  PRO B CD  1 
ATOM   2555 N N   . ARG B 1 38  ? 6.70600   -10.22900 -10.84700 1.000 28.25000 ? 40  ARG B N   1 
ATOM   2556 C CA  . ARG B 1 38  ? 7.71900   -10.94400 -11.61500 1.000 30.23000 ? 40  ARG B CA  1 
ATOM   2557 C C   . ARG B 1 38  ? 7.13500   -12.13100 -12.37100 1.000 34.63000 ? 40  ARG B C   1 
ATOM   2558 O O   . ARG B 1 38  ? 7.74300   -12.57600 -13.35100 1.000 33.82000 ? 40  ARG B O   1 
ATOM   2559 C CB  . ARG B 1 38  ? 8.85600   -11.41800 -10.71000 1.000 32.90000 ? 40  ARG B CB  1 
ATOM   2560 C CG  . ARG B 1 38  ? 8.50900   -12.56800 -9.80100  1.000 31.56000 ? 40  ARG B CG  1 
ATOM   2561 C CD  . ARG B 1 38  ? 9.74600   -13.11100 -9.09400  1.000 31.62000 ? 40  ARG B CD  1 
ATOM   2562 N NE  . ARG B 1 38  ? 9.35000   -14.17200 -8.18200  1.000 32.77000 ? 40  ARG B NE  1 
ATOM   2563 C CZ  . ARG B 1 38  ? 10.17500  -14.89600 -7.43000  1.000 30.96000 ? 40  ARG B CZ  1 
ATOM   2564 N NH1 . ARG B 1 38  ? 11.48300  -14.68100 -7.46500  1.000 29.97000 ? 40  ARG B NH1 1 
ATOM   2565 N NH2 . ARG B 1 38  ? 9.67700   -15.85700 -6.64900  1.000 29.30000 ? 40  ARG B NH2 1 
ATOM   2566 N N   . HIS B 1 39  ? 5.95500   -12.62600 -11.97200 1.000 27.47000 ? 41  HIS B N   1 
ATOM   2567 C CA  . HIS B 1 39  ? 5.41000   -13.78400 -12.67200 1.000 34.84000 ? 41  HIS B CA  1 
ATOM   2568 C C   . HIS B 1 39  ? 4.92500   -13.44100 -14.07300 1.000 34.04000 ? 41  HIS B C   1 
ATOM   2569 O O   . HIS B 1 39  ? 4.47600   -14.34700 -14.78300 1.000 35.87000 ? 41  HIS B O   1 
ATOM   2570 C CB  . HIS B 1 39  ? 4.30100   -14.47500 -11.84400 1.000 33.32000 ? 41  HIS B CB  1 
ATOM   2571 C CG  . HIS B 1 39  ? 2.99000   -13.73600 -11.76200 1.000 33.20000 ? 41  HIS B CG  1 
ATOM   2572 N ND1 . HIS B 1 39  ? 2.24200   -13.39300 -12.87000 1.000 35.02000 ? 41  HIS B ND1 1 
ATOM   2573 C CD2 . HIS B 1 39  ? 2.25700   -13.35100 -10.68500 1.000 28.88000 ? 41  HIS B CD2 1 
ATOM   2574 C CE1 . HIS B 1 39  ? 1.12700   -12.79400 -12.48300 1.000 33.48000 ? 41  HIS B CE1 1 
ATOM   2575 N NE2 . HIS B 1 39  ? 1.11300   -12.75400 -11.16200 1.000 30.64000 ? 41  HIS B NE2 1 
ATOM   2576 N N   . VAL B 1 40  ? 5.04900   -12.18100 -14.50100 1.000 31.40000 ? 42  VAL B N   1 
ATOM   2577 C CA  . VAL B 1 40  ? 4.77300   -11.83600 -15.89500 1.000 35.43000 ? 42  VAL B CA  1 
ATOM   2578 C C   . VAL B 1 40  ? 5.76400   -12.48400 -16.86300 1.000 42.20000 ? 42  VAL B C   1 
ATOM   2579 O O   . VAL B 1 40  ? 5.45600   -12.61100 -18.05500 1.000 43.14000 ? 42  VAL B O   1 
ATOM   2580 C CB  . VAL B 1 40  ? 4.77500   -10.30900 -16.09500 1.000 36.94000 ? 42  VAL B CB  1 
ATOM   2581 C CG1 . VAL B 1 40  ? 6.20100   -9.74400  -16.02000 1.000 36.37000 ? 42  VAL B CG1 1 
ATOM   2582 C CG2 . VAL B 1 40  ? 4.07600   -9.91800  -17.41600 1.000 38.66000 ? 42  VAL B CG2 1 
ATOM   2583 N N   . ILE B 1 41  ? 6.95600   -12.88300 -16.39900 1.000 36.19000 ? 43  ILE B N   1 
ATOM   2584 C CA  . ILE B 1 41  ? 7.90300   -13.58100 -17.27200 1.000 41.67000 ? 43  ILE B CA  1 
ATOM   2585 C C   . ILE B 1 41  ? 7.68400   -15.08900 -17.26400 1.000 42.72000 ? 43  ILE B C   1 
ATOM   2586 O O   . ILE B 1 41  ? 8.38800   -15.81800 -17.97300 1.000 45.57000 ? 43  ILE B O   1 
ATOM   2587 C CB  . ILE B 1 41  ? 9.37200   -13.26000 -16.91200 1.000 38.16000 ? 43  ILE B CB  1 
ATOM   2588 C CG1 . ILE B 1 41  ? 9.75900   -13.83200 -15.54700 1.000 35.70000 ? 43  ILE B CG1 1 
ATOM   2589 C CG2 . ILE B 1 41  ? 9.62800   -11.76500 -16.96800 1.000 42.84000 ? 43  ILE B CG2 1 
ATOM   2590 C CD1 . ILE B 1 41  ? 11.17600  -13.47200 -15.13300 1.000 37.12000 ? 43  ILE B CD1 1 
ATOM   2591 N N   . CYS B 1 42  ? 6.72000   -15.57800 -16.49400 1.000 41.90000 ? 44  CYS B N   1 
ATOM   2592 C CA  . CYS B 1 42  ? 6.39400   -16.99200 -16.47600 1.000 45.10000 ? 44  CYS B CA  1 
ATOM   2593 C C   . CYS B 1 42  ? 5.54500   -17.32200 -17.69400 1.000 50.87000 ? 44  CYS B C   1 
ATOM   2594 O O   . CYS B 1 42  ? 4.72200   -16.51400 -18.12800 1.000 52.53000 ? 44  CYS B O   1 
ATOM   2595 C CB  . CYS B 1 42  ? 5.64200   -17.32100 -15.18900 1.000 44.43000 ? 44  CYS B CB  1 
ATOM   2596 S SG  . CYS B 1 42  ? 5.54900   -19.03300 -14.74200 1.000 58.88000 ? 44  CYS B SG  1 
ATOM   2597 N N   . THR B 1 43  ? 5.75300   -18.49800 -18.26900 1.000 59.10000 ? 45  THR B N   1 
ATOM   2598 C CA  . THR B 1 43  ? 4.94600   -18.89000 -19.41200 1.000 61.15000 ? 45  THR B CA  1 
ATOM   2599 C C   . THR B 1 43  ? 4.02400   -20.03900 -19.03000 1.000 62.62000 ? 45  THR B C   1 
ATOM   2600 O O   . THR B 1 43  ? 4.23100   -20.72200 -18.02400 1.000 62.72000 ? 45  THR B O   1 
ATOM   2601 C CB  . THR B 1 43  ? 5.82400   -19.27000 -20.61000 1.000 65.23000 ? 45  THR B CB  1 
ATOM   2602 O OG1 . THR B 1 43  ? 5.09500   -19.03700 -21.82200 1.000 72.00000 ? 45  THR B OG1 1 
ATOM   2603 C CG2 . THR B 1 43  ? 6.22600   -20.72600 -20.54600 1.000 63.38000 ? 45  THR B CG2 1 
ATOM   2604 N N   . SER B 1 44  ? 2.97300   -20.22300 -19.83300 1.000 66.61000 ? 46  SER B N   1 
ATOM   2605 C CA  . SER B 1 44  ? 2.04900   -21.33500 -19.63800 1.000 67.23000 ? 46  SER B CA  1 
ATOM   2606 C C   . SER B 1 44  ? 2.77000   -22.65800 -19.85200 1.000 68.72000 ? 46  SER B C   1 
ATOM   2607 O O   . SER B 1 44  ? 2.51900   -23.35600 -20.83900 1.000 77.88000 ? 46  SER B O   1 
ATOM   2608 C CB  . SER B 1 44  ? 0.85600   -21.21800 -20.58700 1.000 68.36000 ? 46  SER B CB  1 
ATOM   2609 O OG  . SER B 1 44  ? 1.28900   -21.16000 -21.93600 1.000 71.37000 ? 46  SER B OG  1 
ATOM   2610 N N   . GLU B 1 45  ? 3.64700   -23.01000 -18.91300 1.000 66.93000 ? 47  GLU B N   1 
ATOM   2611 C CA  . GLU B 1 45  ? 4.58600   -24.11800 -19.02600 1.000 66.14000 ? 47  GLU B CA  1 
ATOM   2612 C C   . GLU B 1 45  ? 5.54500   -24.00200 -17.85300 1.000 65.73000 ? 47  GLU B C   1 
ATOM   2613 O O   . GLU B 1 45  ? 5.76900   -24.96600 -17.11100 1.000 65.70000 ? 47  GLU B O   1 
ATOM   2614 C CB  . GLU B 1 45  ? 5.35100   -24.07800 -20.35300 1.000 69.78000 ? 47  GLU B CB  1 
ATOM   2615 C CG  . GLU B 1 45  ? 5.97600   -25.39700 -20.80500 1.000 75.04000 ? 47  GLU B CG  1 
ATOM   2616 C CD  . GLU B 1 45  ? 5.24200   -26.63200 -20.29700 1.000 78.14000 ? 47  GLU B CD  1 
ATOM   2617 O OE1 . GLU B 1 45  ? 4.10800   -26.89000 -20.76000 1.000 80.35000 ? 47  GLU B OE1 1 
ATOM   2618 O OE2 . GLU B 1 45  ? 5.81300   -27.35700 -19.45200 1.000 79.07000 ? 47  GLU B OE2 1 
ATOM   2619 N N   . ASP B 1 46  ? 6.10200   -22.80100 -17.67700 1.000 65.08000 ? 48  ASP B N   1 
ATOM   2620 C CA  . ASP B 1 46  ? 6.90000   -22.47200 -16.50400 1.000 62.55000 ? 48  ASP B CA  1 
ATOM   2621 C C   . ASP B 1 46  ? 6.07600   -22.40500 -15.23000 1.000 59.23000 ? 48  ASP B C   1 
ATOM   2622 O O   . ASP B 1 46  ? 6.66800   -22.32100 -14.14800 1.000 57.56000 ? 48  ASP B O   1 
ATOM   2623 C CB  . ASP B 1 46  ? 7.59100   -21.11900 -16.68200 1.000 59.26000 ? 48  ASP B CB  1 
ATOM   2624 C CG  . ASP B 1 46  ? 8.63100   -21.12900 -17.77100 1.000 65.38000 ? 48  ASP B CG  1 
ATOM   2625 O OD1 . ASP B 1 46  ? 9.50500   -22.02600 -17.74600 1.000 68.99000 ? 48  ASP B OD1 1 
ATOM   2626 O OD2 . ASP B 1 46  ? 8.58200   -20.22500 -18.63700 1.000 67.97000 ? 48  ASP B OD2 1 
ATOM   2627 N N   . MET B 1 47  ? 4.74200   -22.42700 -15.33800 1.000 58.71000 ? 49  MET B N   1 
ATOM   2628 C CA  . MET B 1 47  ? 3.88600   -22.05400 -14.21400 1.000 53.10000 ? 49  MET B CA  1 
ATOM   2629 C C   . MET B 1 47  ? 4.18400   -22.89100 -12.98300 1.000 48.02000 ? 49  MET B C   1 
ATOM   2630 O O   . MET B 1 47  ? 4.22600   -22.36400 -11.86300 1.000 40.25000 ? 49  MET B O   1 
ATOM   2631 C CB  . MET B 1 47  ? 2.41500   -22.19600 -14.59800 1.000 54.22000 ? 49  MET B CB  1 
ATOM   2632 C CG  . MET B 1 47  ? 1.98900   -21.36100 -15.78500 1.000 56.73000 ? 49  MET B CG  1 
ATOM   2633 S SD  . MET B 1 47  ? 0.20800   -21.09100 -15.76500 1.000 65.59000 ? 49  MET B SD  1 
ATOM   2634 C CE  . MET B 1 47  ? 0.12000   -19.34700 -16.15500 1.000 56.93000 ? 49  MET B CE  1 
ATOM   2635 N N   . LEU B 1 48  ? 4.43000   -24.19000 -13.17600 1.000 43.47000 ? 50  LEU B N   1 
ATOM   2636 C CA  . LEU B 1 48  ? 4.51500   -25.10400 -12.04400 1.000 43.07000 ? 50  LEU B CA  1 
ATOM   2637 C C   . LEU B 1 48  ? 5.76700   -24.85800 -11.21100 1.000 42.26000 ? 50  LEU B C   1 
ATOM   2638 O O   . LEU B 1 48  ? 5.69800   -24.81000 -9.97800  1.000 44.51000 ? 50  LEU B O   1 
ATOM   2639 C CB  . LEU B 1 48  ? 4.46000   -26.55500 -12.53800 1.000 47.72000 ? 50  LEU B CB  1 
ATOM   2640 C CG  . LEU B 1 48  ? 3.04300   -27.01900 -12.88700 1.000 46.27000 ? 50  LEU B CG  1 
ATOM   2641 C CD1 . LEU B 1 48  ? 3.05400   -28.40000 -13.51300 1.000 47.43000 ? 50  LEU B CD1 1 
ATOM   2642 C CD2 . LEU B 1 48  ? 2.15000   -26.97800 -11.64800 1.000 47.63000 ? 50  LEU B CD2 1 
ATOM   2643 N N   . ASN B 1 49  ? 6.92300   -24.71100 -11.84800 1.000 44.50000 ? 51  ASN B N   1 
ATOM   2644 C CA  . ASN B 1 49  ? 8.17300   -24.48300 -11.11800 1.000 49.00000 ? 51  ASN B CA  1 
ATOM   2645 C C   . ASN B 1 49  ? 9.06800   -23.50200 -11.86300 1.000 46.24000 ? 51  ASN B C   1 
ATOM   2646 O O   . ASN B 1 49  ? 10.12500  -23.86900 -12.38900 1.000 43.43000 ? 51  ASN B O   1 
ATOM   2647 C CB  . ASN B 1 49  ? 8.90000   -25.80200 -10.86300 1.000 49.02000 ? 51  ASN B CB  1 
ATOM   2648 C CG  . ASN B 1 49  ? 9.79800   -25.72900 -9.65300  1.000 55.74000 ? 51  ASN B CG  1 
ATOM   2649 O OD1 . ASN B 1 49  ? 10.44500  -24.70600 -9.40700  1.000 59.70000 ? 51  ASN B OD1 1 
ATOM   2650 N ND2 . ASN B 1 49  ? 9.83100   -26.80500 -8.87500  1.000 62.83000 ? 51  ASN B ND2 1 
ATOM   2651 N N   . PRO B 1 50  ? 8.69000   -22.22500 -11.89000 1.000 46.28000 ? 52  PRO B N   1 
ATOM   2652 C CA  . PRO B 1 50  ? 9.53700   -21.22500 -12.55000 1.000 43.64000 ? 52  PRO B CA  1 
ATOM   2653 C C   . PRO B 1 50  ? 10.86700  -21.06800 -11.83300 1.000 39.68000 ? 52  PRO B C   1 
ATOM   2654 O O   . PRO B 1 50  ? 10.94900  -21.14900 -10.60700 1.000 42.83000 ? 52  PRO B O   1 
ATOM   2655 C CB  . PRO B 1 50  ? 8.70100   -19.93600 -12.47200 1.000 44.67000 ? 52  PRO B CB  1 
ATOM   2656 C CG  . PRO B 1 50  ? 7.79900   -20.14300 -11.29900 1.000 43.14000 ? 52  PRO B CG  1 
ATOM   2657 C CD  . PRO B 1 50  ? 7.51500   -21.62100 -11.23900 1.000 45.70000 ? 52  PRO B CD  1 
ATOM   2658 N N   . ASN B 1 51  ? 11.91600  -20.88000 -12.61700 1.000 39.89000 ? 53  ASN B N   1 
ATOM   2659 C CA  . ASN B 1 51  ? 13.22800  -20.46600 -12.12500 1.000 42.41000 ? 53  ASN B CA  1 
ATOM   2660 C C   . ASN B 1 51  ? 13.34500  -19.01200 -12.57200 1.000 43.70000 ? 53  ASN B C   1 
ATOM   2661 O O   . ASN B 1 51  ? 13.73300  -18.72200 -13.70500 1.000 45.53000 ? 53  ASN B O   1 
ATOM   2662 C CB  . ASN B 1 51  ? 14.35000  -21.36500 -12.68300 1.000 47.69000 ? 53  ASN B CB  1 
ATOM   2663 C CG  . ASN B 1 51  ? 15.72200  -21.05000 -12.09200 1.000 48.74000 ? 53  ASN B CG  1 
ATOM   2664 O OD1 . ASN B 1 51  ? 16.04900  -19.89900 -11.79600 1.000 48.90000 ? 53  ASN B OD1 1 
ATOM   2665 N ND2 . ASN B 1 51  ? 16.53500  -22.08700 -11.92600 1.000 54.56000 ? 53  ASN B ND2 1 
ATOM   2666 N N   . TYR B 1 52  ? 12.95300  -18.09300 -11.68700 1.000 41.91000 ? 54  TYR B N   1 
ATOM   2667 C CA  . TYR B 1 52  ? 12.78300  -16.71000 -12.11100 1.000 41.32000 ? 54  TYR B CA  1 
ATOM   2668 C C   . TYR B 1 52  ? 14.11800  -16.05900 -12.42800 1.000 41.72000 ? 54  TYR B C   1 
ATOM   2669 O O   . TYR B 1 52  ? 14.21300  -15.26700 -13.37100 1.000 39.72000 ? 54  TYR B O   1 
ATOM   2670 C CB  . TYR B 1 52  ? 12.02100  -15.91700 -11.04800 1.000 37.07000 ? 54  TYR B CB  1 
ATOM   2671 C CG  . TYR B 1 52  ? 10.53100  -16.15500 -11.10800 1.000 35.43000 ? 54  TYR B CG  1 
ATOM   2672 C CD1 . TYR B 1 52  ? 9.78800   -15.76500 -12.22200 1.000 37.03000 ? 54  TYR B CD1 1 
ATOM   2673 C CD2 . TYR B 1 52  ? 9.87300   -16.78800 -10.07500 1.000 32.13000 ? 54  TYR B CD2 1 
ATOM   2674 C CE1 . TYR B 1 52  ? 8.42600   -15.99300 -12.29300 1.000 32.67000 ? 54  TYR B CE1 1 
ATOM   2675 C CE2 . TYR B 1 52  ? 8.50400   -17.00500 -10.12900 1.000 33.50000 ? 54  TYR B CE2 1 
ATOM   2676 C CZ  . TYR B 1 52  ? 7.79300   -16.60700 -11.23900 1.000 33.48000 ? 54  TYR B CZ  1 
ATOM   2677 O OH  . TYR B 1 52  ? 6.44000   -16.83200 -11.29200 1.000 32.49000 ? 54  TYR B OH  1 
ATOM   2678 N N   . GLU B 1 53  ? 15.16600  -16.37900 -11.66600 1.000 46.10000 ? 55  GLU B N   1 
ATOM   2679 C CA  . GLU B 1 53  ? 16.47000  -15.81200 -11.99400 1.000 46.48000 ? 55  GLU B CA  1 
ATOM   2680 C C   . GLU B 1 53  ? 16.90100  -16.24800 -13.39100 1.000 47.12000 ? 55  GLU B C   1 
ATOM   2681 O O   . GLU B 1 53  ? 17.41100  -15.43500 -14.17400 1.000 48.22000 ? 55  GLU B O   1 
ATOM   2682 C CB  . GLU B 1 53  ? 17.50700  -16.19100 -10.92900 1.000 43.82000 ? 55  GLU B CB  1 
ATOM   2683 C CG  . GLU B 1 53  ? 18.33800  -17.42600 -11.21700 1.000 55.65000 ? 55  GLU B CG  1 
ATOM   2684 C CD  . GLU B 1 53  ? 19.35400  -17.71800 -10.12500 1.000 58.51000 ? 55  GLU B CD  1 
ATOM   2685 O OE1 . GLU B 1 53  ? 19.22400  -17.13900 -9.01900  1.000 57.55000 ? 55  GLU B OE1 1 
ATOM   2686 O OE2 . GLU B 1 53  ? 20.26900  -18.53800 -10.36800 1.000 64.97000 ? 55  GLU B OE2 1 
ATOM   2687 N N   . ASP B 1 54  ? 16.62600  -17.50800 -13.75000 1.000 47.53000 ? 56  ASP B N   1 
ATOM   2688 C CA  . ASP B 1 54  ? 16.99200  -18.00300 -15.07200 1.000 48.44000 ? 56  ASP B CA  1 
ATOM   2689 C C   . ASP B 1 54  ? 16.12500  -17.37300 -16.15700 1.000 48.98000 ? 56  ASP B C   1 
ATOM   2690 O O   . ASP B 1 54  ? 16.63500  -16.93600 -17.19700 1.000 50.14000 ? 56  ASP B O   1 
ATOM   2691 C CB  . ASP B 1 54  ? 16.87800  -19.52800 -15.11400 1.000 51.07000 ? 56  ASP B CB  1 
ATOM   2692 C CG  . ASP B 1 54  ? 17.17800  -20.09300 -16.49100 1.000 57.37000 ? 56  ASP B CG  1 
ATOM   2693 O OD1 . ASP B 1 54  ? 18.34000  -19.98200 -16.93400 1.000 57.00000 ? 56  ASP B OD1 1 
ATOM   2694 O OD2 . ASP B 1 54  ? 16.25200  -20.63300 -17.13500 1.000 62.36000 ? 56  ASP B OD2 1 
ATOM   2695 N N   . LEU B 1 55  ? 14.80600  -17.31900 -15.93200 1.000 45.50000 ? 57  LEU B N   1 
ATOM   2696 C CA  . LEU B 1 55  ? 13.90900  -16.70600 -16.90900 1.000 46.49000 ? 57  LEU B CA  1 
ATOM   2697 C C   . LEU B 1 55  ? 14.25300  -15.24000 -17.15600 1.000 46.58000 ? 57  LEU B C   1 
ATOM   2698 O O   . LEU B 1 55  ? 14.07900  -14.74400 -18.27300 1.000 48.40000 ? 57  LEU B O   1 
ATOM   2699 C CB  . LEU B 1 55  ? 12.45200  -16.83000 -16.44500 1.000 45.98000 ? 57  LEU B CB  1 
ATOM   2700 C CG  . LEU B 1 55  ? 11.85000  -18.23400 -16.34000 1.000 49.00000 ? 57  LEU B CG  1 
ATOM   2701 C CD1 . LEU B 1 55  ? 10.58100  -18.22000 -15.51500 1.000 44.79000 ? 57  LEU B CD1 1 
ATOM   2702 C CD2 . LEU B 1 55  ? 11.57500  -18.80600 -17.72000 1.000 52.98000 ? 57  LEU B CD2 1 
ATOM   2703 N N   . LEU B 1 56  ? 14.74200  -14.53600 -16.13400 1.000 46.49000 ? 58  LEU B N   1 
ATOM   2704 C CA  . LEU B 1 56  ? 15.08500  -13.12300 -16.27800 1.000 48.09000 ? 58  LEU B CA  1 
ATOM   2705 C C   . LEU B 1 56  ? 16.42700  -12.92800 -16.98500 1.000 51.11000 ? 58  LEU B C   1 
ATOM   2706 O O   . LEU B 1 56  ? 16.57700  -11.99000 -17.77900 1.000 53.16000 ? 58  LEU B O   1 
ATOM   2707 C CB  . LEU B 1 56  ? 15.09900  -12.44400 -14.90500 1.000 45.04000 ? 58  LEU B CB  1 
ATOM   2708 C CG  . LEU B 1 56  ? 15.14300  -10.91000 -14.91000 1.000 47.33000 ? 58  LEU B CG  1 
ATOM   2709 C CD1 . LEU B 1 56  ? 14.17000  -10.36000 -15.93500 1.000 49.44000 ? 58  LEU B CD1 1 
ATOM   2710 C CD2 . LEU B 1 56  ? 14.81200  -10.35600 -13.53300 1.000 42.95000 ? 58  LEU B CD2 1 
ATOM   2711 N N   . ILE B 1 57  ? 17.41400  -13.78600 -16.70200 1.000 53.24000 ? 59  ILE B N   1 
ATOM   2712 C CA  . ILE B 1 57  ? 18.67900  -13.74100 -17.44200 1.000 53.14000 ? 59  ILE B CA  1 
ATOM   2713 C C   . ILE B 1 57  ? 18.42400  -13.89100 -18.93800 1.000 53.04000 ? 59  ILE B C   1 
ATOM   2714 O O   . ILE B 1 57  ? 19.03200  -13.19100 -19.75800 1.000 57.80000 ? 59  ILE B O   1 
ATOM   2715 C CB  . ILE B 1 57  ? 19.64700  -14.82400 -16.92400 1.000 55.75000 ? 59  ILE B CB  1 
ATOM   2716 C CG1 . ILE B 1 57  ? 20.14000  -14.47100 -15.52300 1.000 53.81000 ? 59  ILE B CG1 1 
ATOM   2717 C CG2 . ILE B 1 57  ? 20.83000  -15.01100 -17.88100 1.000 54.18000 ? 59  ILE B CG2 1 
ATOM   2718 C CD1 . ILE B 1 57  ? 21.31300  -13.50700 -15.51700 1.000 52.03000 ? 59  ILE B CD1 1 
ATOM   2719 N N   . ARG B 1 58  ? 17.51000  -14.79500 -19.30900 1.000 55.63000 ? 60  ARG B N   1 
ATOM   2720 C CA  . ARG B 1 58  ? 17.08600  -14.94500 -20.70100 1.000 57.36000 ? 60  ARG B CA  1 
ATOM   2721 C C   . ARG B 1 58  ? 16.66700  -13.60900 -21.30600 1.000 60.16000 ? 60  ARG B C   1 
ATOM   2722 O O   . ARG B 1 58  ? 17.09700  -13.24500 -22.40500 1.000 61.17000 ? 60  ARG B O   1 
ATOM   2723 C CB  . ARG B 1 58  ? 15.91500  -15.92700 -20.78300 1.000 57.64000 ? 60  ARG B CB  1 
ATOM   2724 C CG  . ARG B 1 58  ? 16.23700  -17.32900 -21.27600 1.000 63.18000 ? 60  ARG B CG  1 
ATOM   2725 C CD  . ARG B 1 58  ? 15.55300  -18.36000 -20.37900 1.000 62.69000 ? 60  ARG B CD  1 
ATOM   2726 N NE  . ARG B 1 58  ? 15.91400  -19.73600 -20.70600 1.000 65.91000 ? 60  ARG B NE  1 
ATOM   2727 C CZ  . ARG B 1 58  ? 17.01300  -20.34100 -20.26400 1.000 71.63000 ? 60  ARG B CZ  1 
ATOM   2728 N NH1 . ARG B 1 58  ? 17.86700  -19.67700 -19.49300 1.000 67.85000 ? 60  ARG B NH1 1 
ATOM   2729 N NH2 . ARG B 1 58  ? 17.26900  -21.60200 -20.60500 1.000 69.57000 ? 60  ARG B NH2 1 
ATOM   2730 N N   . LYS B 1 59  ? 15.82700  -12.86400 -20.59000 1.000 60.62000 ? 61  LYS B N   1 
ATOM   2731 C CA  . LYS B 1 59  ? 15.13300  -11.70800 -21.14500 1.000 56.35000 ? 61  LYS B CA  1 
ATOM   2732 C C   . LYS B 1 59  ? 16.08500  -10.55900 -21.44600 1.000 56.80000 ? 61  LYS B C   1 
ATOM   2733 O O   . LYS B 1 59  ? 17.08000  -10.33700 -20.74600 1.000 57.97000 ? 61  LYS B O   1 
ATOM   2734 C CB  . LYS B 1 59  ? 14.05400  -11.21800 -20.17300 1.000 55.74000 ? 61  LYS B CB  1 
ATOM   2735 C CG  . LYS B 1 59  ? 12.99800  -12.24900 -19.83700 1.000 52.95000 ? 61  LYS B CG  1 
ATOM   2736 C CD  . LYS B 1 59  ? 11.95100  -12.31500 -20.92300 1.000 51.74000 ? 61  LYS B CD  1 
ATOM   2737 C CE  . LYS B 1 59  ? 11.23300  -13.64100 -20.92900 1.000 52.66000 ? 61  LYS B CE  1 
ATOM   2738 N NZ  . LYS B 1 59  ? 10.37300  -13.71900 -22.14300 1.000 52.42000 ? 61  LYS B NZ  1 
ATOM   2739 N N   . SER B 1 60  ? 15.75400  -9.81700  -22.49700 1.000 55.99000 ? 62  SER B N   1 
ATOM   2740 C CA  . SER B 1 60  ? 16.36500  -8.53600  -22.81300 1.000 55.45000 ? 62  SER B CA  1 
ATOM   2741 C C   . SER B 1 60  ? 15.32700  -7.43100  -22.65800 1.000 53.91000 ? 62  SER B C   1 
ATOM   2742 O O   . SER B 1 60  ? 14.13600  -7.68600  -22.46900 1.000 53.23000 ? 62  SER B O   1 
ATOM   2743 C CB  . SER B 1 60  ? 16.94100  -8.53300  -24.23400 1.000 58.38000 ? 62  SER B CB  1 
ATOM   2744 O OG  . SER B 1 60  ? 18.15200  -9.27400  -24.31400 1.000 60.24000 ? 62  SER B OG  1 
ATOM   2745 N N   . ASN B 1 61  ? 15.79600  -6.18600  -22.74200 1.000 52.44000 ? 63  ASN B N   1 
ATOM   2746 C CA  . ASN B 1 61  ? 14.89000  -5.05100  -22.59900 1.000 52.52000 ? 63  ASN B CA  1 
ATOM   2747 C C   . ASN B 1 61  ? 13.73900  -5.12500  -23.59300 1.000 53.45000 ? 63  ASN B C   1 
ATOM   2748 O O   . ASN B 1 61  ? 12.58300  -4.85500  -23.23900 1.000 50.30000 ? 63  ASN B O   1 
ATOM   2749 C CB  . ASN B 1 61  ? 15.66200  -3.74800  -22.76400 1.000 45.46000 ? 63  ASN B CB  1 
ATOM   2750 C CG  . ASN B 1 61  ? 16.51100  -3.44600  -21.57000 1.000 47.97000 ? 63  ASN B CG  1 
ATOM   2751 O OD1 . ASN B 1 61  ? 16.20000  -3.88500  -20.46100 1.000 49.37000 ? 63  ASN B OD1 1 
ATOM   2752 N ND2 . ASN B 1 61  ? 17.59700  -2.70700  -21.77700 1.000 49.08000 ? 63  ASN B ND2 1 
ATOM   2753 N N   . HIS B 1 62  ? 14.03100  -5.50400  -24.83700 1.000 54.49000 ? 64  HIS B N   1 
ATOM   2754 C CA  . HIS B 1 62  ? 13.00200  -5.49500  -25.87000 1.000 56.06000 ? 64  HIS B CA  1 
ATOM   2755 C C   . HIS B 1 62  ? 11.93000  -6.55000  -25.63700 1.000 55.56000 ? 64  HIS B C   1 
ATOM   2756 O O   . HIS B 1 62  ? 10.88600  -6.50000  -26.29500 1.000 58.93000 ? 64  HIS B O   1 
ATOM   2757 C CB  . HIS B 1 62  ? 13.64500  -5.68800  -27.24800 1.000 58.23000 ? 64  HIS B CB  1 
ATOM   2758 C CG  . HIS B 1 62  ? 14.68800  -6.76400  -27.28200 1.000 56.66000 ? 64  HIS B CG  1 
ATOM   2759 N ND1 . HIS B 1 62  ? 14.38400  -8.10000  -27.11800 1.000 57.42000 ? 64  HIS B ND1 1 
ATOM   2760 C CD2 . HIS B 1 62  ? 16.03100  -6.70300  -27.46100 1.000 53.89000 ? 64  HIS B CD2 1 
ATOM   2761 C CE1 . HIS B 1 62  ? 15.49400  -8.81500  -27.19400 1.000 56.50000 ? 64  HIS B CE1 1 
ATOM   2762 N NE2 . HIS B 1 62  ? 16.50800  -7.99100  -27.40100 1.000 57.47000 ? 64  HIS B NE2 1 
ATOM   2763 N N   . ASN B 1 63  ? 12.15500  -7.48600  -24.71000 1.000 54.55000 ? 65  ASN B N   1 
ATOM   2764 C CA  . ASN B 1 63  ? 11.16300  -8.50300  -24.37900 1.000 52.75000 ? 65  ASN B CA  1 
ATOM   2765 C C   . ASN B 1 63  ? 9.93700   -7.94700  -23.66000 1.000 51.82000 ? 65  ASN B C   1 
ATOM   2766 O O   . ASN B 1 63  ? 8.97900   -8.69800  -23.44800 1.000 50.76000 ? 65  ASN B O   1 
ATOM   2767 C CB  . ASN B 1 63  ? 11.79700  -9.59400  -23.50800 1.000 55.45000 ? 65  ASN B CB  1 
ATOM   2768 C CG  . ASN B 1 63  ? 12.69300  -10.53900 -24.30000 1.000 57.05000 ? 65  ASN B CG  1 
ATOM   2769 O OD1 . ASN B 1 63  ? 13.92100  -10.53900 -24.14500 1.000 56.69000 ? 65  ASN B OD1 1 
ATOM   2770 N ND2 . ASN B 1 63  ? 12.08000  -11.35000 -25.15100 1.000 51.44000 ? 65  ASN B ND2 1 
ATOM   2771 N N   . PHE B 1 64  ? 9.93800   -6.67600  -23.26400 1.000 48.71000 ? 66  PHE B N   1 
ATOM   2772 C CA  . PHE B 1 64  ? 8.83500   -6.08800  -22.50700 1.000 49.70000 ? 66  PHE B CA  1 
ATOM   2773 C C   . PHE B 1 64  ? 8.25400   -4.91000  -23.27500 1.000 49.24000 ? 66  PHE B C   1 
ATOM   2774 O O   . PHE B 1 64  ? 8.97200   -3.95900  -23.59900 1.000 51.48000 ? 66  PHE B O   1 
ATOM   2775 C CB  . PHE B 1 64  ? 9.29100   -5.61800  -21.12400 1.000 47.16000 ? 66  PHE B CB  1 
ATOM   2776 C CG  . PHE B 1 64  ? 9.97700   -6.66900  -20.32400 1.000 49.10000 ? 66  PHE B CG  1 
ATOM   2777 C CD1 . PHE B 1 64  ? 9.24600   -7.54300  -19.53600 1.000 45.57000 ? 66  PHE B CD1 1 
ATOM   2778 C CD2 . PHE B 1 64  ? 11.35800  -6.78600  -20.35400 1.000 46.01000 ? 66  PHE B CD2 1 
ATOM   2779 C CE1 . PHE B 1 64  ? 9.88300   -8.51700  -18.79700 1.000 45.96000 ? 66  PHE B CE1 1 
ATOM   2780 C CE2 . PHE B 1 64  ? 12.00100  -7.75600  -19.61600 1.000 46.35000 ? 66  PHE B CE2 1 
ATOM   2781 C CZ  . PHE B 1 64  ? 11.26300  -8.62200  -18.83400 1.000 46.25000 ? 66  PHE B CZ  1 
ATOM   2782 N N   . LEU B 1 65  ? 6.95700   -4.96600  -23.54300 1.000 51.64000 ? 67  LEU B N   1 
ATOM   2783 C CA  . LEU B 1 65  ? 6.22500   -3.85400  -24.13000 1.000 50.19000 ? 67  LEU B CA  1 
ATOM   2784 C C   . LEU B 1 65  ? 5.43500   -3.15800  -23.02300 1.000 51.20000 ? 67  LEU B C   1 
ATOM   2785 O O   . LEU B 1 65  ? 4.56300   -3.77200  -22.39400 1.000 48.87000 ? 67  LEU B O   1 
ATOM   2786 C CB  . LEU B 1 65  ? 5.30000   -4.34300  -25.24400 1.000 49.40000 ? 67  LEU B CB  1 
ATOM   2787 C CG  . LEU B 1 65  ? 4.11300   -3.44500  -25.60900 1.000 57.17000 ? 67  LEU B CG  1 
ATOM   2788 C CD1 . LEU B 1 65  ? 4.57000   -2.11900  -26.21600 1.000 55.96000 ? 67  LEU B CD1 1 
ATOM   2789 C CD2 . LEU B 1 65  ? 3.14500   -4.17700  -26.54200 1.000 59.76000 ? 67  LEU B CD2 1 
ATOM   2790 N N   . VAL B 1 66  ? 5.75400   -1.88700  -22.78200 1.000 47.24000 ? 68  VAL B N   1 
ATOM   2791 C CA  . VAL B 1 66  ? 5.10300   -1.07000  -21.76200 1.000 48.05000 ? 68  VAL B CA  1 
ATOM   2792 C C   . VAL B 1 66  ? 4.32300   0.03400   -22.46300 1.000 48.63000 ? 68  VAL B C   1 
ATOM   2793 O O   . VAL B 1 66  ? 4.90300   0.84000   -23.20100 1.000 50.65000 ? 68  VAL B O   1 
ATOM   2794 C CB  . VAL B 1 66  ? 6.12200   -0.48000  -20.77500 1.000 41.82000 ? 68  VAL B CB  1 
ATOM   2795 C CG1 . VAL B 1 66  ? 5.44100   0.47700   -19.80800 1.000 42.31000 ? 68  VAL B CG1 1 
ATOM   2796 C CG2 . VAL B 1 66  ? 6.80500   -1.60200  -20.01600 1.000 45.15000 ? 68  VAL B CG2 1 
ATOM   2797 N N   . GLN B 1 67  ? 3.01300   0.07900   -22.22800 1.000 47.32000 ? 69  GLN B N   1 
ATOM   2798 C CA  . GLN B 1 67  ? 2.14500   1.08700   -22.82600 1.000 48.08000 ? 69  GLN B CA  1 
ATOM   2799 C C   . GLN B 1 67  ? 1.44700   1.86800   -21.72400 1.000 44.72000 ? 69  GLN B C   1 
ATOM   2800 O O   . GLN B 1 67  ? 0.76700   1.28200   -20.87600 1.000 42.60000 ? 69  GLN B O   1 
ATOM   2801 C CB  . GLN B 1 67  ? 1.10900   0.45600   -23.75300 1.000 49.12000 ? 69  GLN B CB  1 
ATOM   2802 C CG  . GLN B 1 67  ? 1.68700   -0.38300  -24.86800 1.000 53.31000 ? 69  GLN B CG  1 
ATOM   2803 C CD  . GLN B 1 67  ? 0.62600   -1.24400  -25.54100 1.000 55.58000 ? 69  GLN B CD  1 
ATOM   2804 O OE1 . GLN B 1 67  ? 0.62000   -2.46800  -25.40500 1.000 58.00000 ? 69  GLN B OE1 1 
ATOM   2805 N NE2 . GLN B 1 67  ? -0.28200  -0.60200  -26.26800 1.000 59.55000 ? 69  GLN B NE2 1 
ATOM   2806 N N   . ALA B 1 68  ? 1.61900   3.18300   -21.74100 1.000 46.24000 ? 70  ALA B N   1 
ATOM   2807 C CA  . ALA B 1 68  ? 0.90000   4.09600   -20.85900 1.000 48.04000 ? 70  ALA B CA  1 
ATOM   2808 C C   . ALA B 1 68  ? -0.22700  4.69000   -21.69100 1.000 52.43000 ? 70  ALA B C   1 
ATOM   2809 O O   . ALA B 1 68  ? 0.00700   5.54600   -22.54800 1.000 53.92000 ? 70  ALA B O   1 
ATOM   2810 C CB  . ALA B 1 68  ? 1.82900   5.16900   -20.30500 1.000 43.93000 ? 70  ALA B CB  1 
ATOM   2811 N N   . GLY B 1 69  ? -1.45000  4.22300   -21.45100 1.000 52.24000 ? 71  GLY B N   1 
ATOM   2812 C CA  . GLY B 1 69  ? -2.53100  4.54100   -22.35800 1.000 53.34000 ? 71  GLY B CA  1 
ATOM   2813 C C   . GLY B 1 69  ? -2.16700  4.12100   -23.76800 1.000 58.13000 ? 71  GLY B C   1 
ATOM   2814 O O   . GLY B 1 69  ? -2.09900  2.92300   -24.07000 1.000 57.81000 ? 71  GLY B O   1 
ATOM   2815 N N   . ASN B 1 70  ? -1.88200  5.09700   -24.62900 1.000 57.54000 ? 72  ASN B N   1 
ATOM   2816 C CA  . ASN B 1 70  ? -1.57800  4.82900   -26.02700 1.000 57.60000 ? 72  ASN B CA  1 
ATOM   2817 C C   . ASN B 1 70  ? -0.13500  5.13000   -26.41300 1.000 59.54000 ? 72  ASN B C   1 
ATOM   2818 O O   . ASN B 1 70  ? 0.22600   4.92300   -27.57600 1.000 61.68000 ? 72  ASN B O   1 
ATOM   2819 C CB  . ASN B 1 70  ? -2.52800  5.62400   -26.93400 1.000 60.76000 ? 72  ASN B CB  1 
ATOM   2820 N N   . VAL B 1 71  ? 0.70500   5.60800   -25.49000 1.000 57.35000 ? 73  VAL B N   1 
ATOM   2821 C CA  . VAL B 1 71  ? 2.11400   5.86000   -25.78900 1.000 57.19000 ? 73  VAL B CA  1 
ATOM   2822 C C   . VAL B 1 71  ? 2.94600   4.67800   -25.31300 1.000 56.01000 ? 73  VAL B C   1 
ATOM   2823 O O   . VAL B 1 71  ? 2.82400   4.23900   -24.16200 1.000 54.88000 ? 73  VAL B O   1 
ATOM   2824 C CB  . VAL B 1 71  ? 2.61400   7.17800   -25.16500 1.000 56.44000 ? 73  VAL B CB  1 
ATOM   2825 C CG1 . VAL B 1 71  ? 2.27700   7.26500   -23.68800 1.000 59.30000 ? 73  VAL B CG1 1 
ATOM   2826 C CG2 . VAL B 1 71  ? 4.12100   7.31500   -25.36600 1.000 50.62000 ? 73  VAL B CG2 1 
ATOM   2827 N N   . GLN B 1 72  ? 3.78100   4.15300   -26.20700 1.000 56.45000 ? 74  GLN B N   1 
ATOM   2828 C CA  . GLN B 1 72  ? 4.70200   3.08500   -25.85400 1.000 52.28000 ? 74  GLN B CA  1 
ATOM   2829 C C   . GLN B 1 72  ? 5.87900   3.66800   -25.09100 1.000 52.23000 ? 74  GLN B C   1 
ATOM   2830 O O   . GLN B 1 72  ? 6.50800   4.62700   -25.54400 1.000 56.40000 ? 74  GLN B O   1 
ATOM   2831 C CB  . GLN B 1 72  ? 5.18800   2.35700   -27.10600 1.000 50.89000 ? 74  GLN B CB  1 
ATOM   2832 N N   . LEU B 1 73  ? 6.16300   3.10500   -23.92200 1.000 52.72000 ? 75  LEU B N   1 
ATOM   2833 C CA  . LEU B 1 73  ? 7.34300   3.48500   -23.16000 1.000 49.80000 ? 75  LEU B CA  1 
ATOM   2834 C C   . LEU B 1 73  ? 8.49200   2.55500   -23.52900 1.000 49.81000 ? 75  LEU B C   1 
ATOM   2835 O O   . LEU B 1 73  ? 8.33800   1.32700   -23.50700 1.000 49.67000 ? 75  LEU B O   1 
ATOM   2836 C CB  . LEU B 1 73  ? 7.06600   3.41600   -21.65900 1.000 44.88000 ? 75  LEU B CB  1 
ATOM   2837 C CG  . LEU B 1 73  ? 5.96000   4.30900   -21.10500 1.000 46.47000 ? 75  LEU B CG  1 
ATOM   2838 C CD1 . LEU B 1 73  ? 5.94400   4.22100   -19.58900 1.000 41.56000 ? 75  LEU B CD1 1 
ATOM   2839 C CD2 . LEU B 1 73  ? 6.14500   5.75700   -21.56700 1.000 47.39000 ? 75  LEU B CD2 1 
ATOM   2840 N N   . ARG B 1 74  ? 9.63900   3.13700   -23.86700 1.000 48.05000 ? 76  ARG B N   1 
ATOM   2841 C CA  . ARG B 1 74  ? 10.82000  2.34800   -24.19100 1.000 49.92000 ? 76  ARG B CA  1 
ATOM   2842 C C   . ARG B 1 74  ? 11.46200  1.84800   -22.90300 1.000 45.28000 ? 76  ARG B C   1 
ATOM   2843 O O   . ARG B 1 74  ? 11.82300  2.64600   -22.03100 1.000 44.48000 ? 76  ARG B O   1 
ATOM   2844 C CB  . ARG B 1 74  ? 11.81600  3.17400   -25.00200 1.000 49.94000 ? 76  ARG B CB  1 
ATOM   2845 N N   . VAL B 1 75  ? 11.59400  0.53000   -22.79000 1.000 45.86000 ? 77  VAL B N   1 
ATOM   2846 C CA  . VAL B 1 75  ? 12.25700  -0.11100  -21.65800 1.000 46.09000 ? 77  VAL B CA  1 
ATOM   2847 C C   . VAL B 1 75  ? 13.76100  -0.10200  -21.90800 1.000 46.68000 ? 77  VAL B C   1 
ATOM   2848 O O   . VAL B 1 75  ? 14.23100  -0.62600  -22.92400 1.000 49.47000 ? 77  VAL B O   1 
ATOM   2849 C CB  . VAL B 1 75  ? 11.74600  -1.54500  -21.46300 1.000 44.42000 ? 77  VAL B CB  1 
ATOM   2850 C CG1 . VAL B 1 75  ? 12.41200  -2.19700  -20.26000 1.000 44.99000 ? 77  VAL B CG1 1 
ATOM   2851 C CG2 . VAL B 1 75  ? 10.22900  -1.55700  -21.32600 1.000 50.10000 ? 77  VAL B CG2 1 
ATOM   2852 N N   . ILE B 1 76  ? 14.51700  0.47500   -20.97000 1.000 46.69000 ? 78  ILE B N   1 
ATOM   2853 C CA  . ILE B 1 76  ? 15.96600  0.59600   -21.05600 1.000 43.43000 ? 78  ILE B CA  1 
ATOM   2854 C C   . ILE B 1 76  ? 16.67700  -0.18400  -19.95400 1.000 46.55000 ? 78  ILE B C   1 
ATOM   2855 O O   . ILE B 1 76  ? 17.87900  -0.00900  -19.75600 1.000 48.11000 ? 78  ILE B O   1 
ATOM   2856 C CB  . ILE B 1 76  ? 16.41000  2.07300   -21.03400 1.000 46.21000 ? 78  ILE B CB  1 
ATOM   2857 C CG1 . ILE B 1 76  ? 16.02800  2.71900   -19.69800 1.000 46.46000 ? 78  ILE B CG1 1 
ATOM   2858 C CG2 . ILE B 1 76  ? 15.79800  2.84200   -22.19000 1.000 46.67000 ? 78  ILE B CG2 1 
ATOM   2859 C CD1 . ILE B 1 76  ? 16.53200  4.13000   -19.52600 1.000 47.09000 ? 78  ILE B CD1 1 
ATOM   2860 N N   . GLY B 1 77  ? 15.96100  -1.03500  -19.22900 1.000 41.19000 ? 79  GLY B N   1 
ATOM   2861 C CA  . GLY B 1 77  ? 16.57300  -1.80300  -18.15900 1.000 41.99000 ? 79  GLY B CA  1 
ATOM   2862 C C   . GLY B 1 77  ? 15.52100  -2.64600  -17.46700 1.000 44.69000 ? 79  GLY B C   1 
ATOM   2863 O O   . GLY B 1 77  ? 14.32500  -2.33700  -17.49800 1.000 40.72000 ? 79  GLY B O   1 
ATOM   2864 N N   . HIS B 1 78  ? 15.99300  -3.72000  -16.83900 1.000 41.87000 ? 80  HIS B N   1 
ATOM   2865 C CA  . HIS B 1 78  ? 15.10700  -4.62400  -16.11900 1.000 40.78000 ? 80  HIS B CA  1 
ATOM   2866 C C   . HIS B 1 78  ? 15.85300  -5.22000  -14.93700 1.000 43.48000 ? 80  HIS B C   1 
ATOM   2867 O O   . HIS B 1 78  ? 17.04700  -5.51600  -15.02600 1.000 41.68000 ? 80  HIS B O   1 
ATOM   2868 C CB  . HIS B 1 78  ? 14.57800  -5.74400  -17.02400 1.000 44.60000 ? 80  HIS B CB  1 
ATOM   2869 C CG  . HIS B 1 78  ? 15.65900  -6.55300  -17.66900 1.000 47.01000 ? 80  HIS B CG  1 
ATOM   2870 N ND1 . HIS B 1 78  ? 16.41400  -6.07800  -18.72000 1.000 50.26000 ? 80  HIS B ND1 1 
ATOM   2871 C CD2 . HIS B 1 78  ? 16.12000  -7.79900  -17.40600 1.000 50.35000 ? 80  HIS B CD2 1 
ATOM   2872 C CE1 . HIS B 1 78  ? 17.29300  -6.99900  -19.07900 1.000 51.99000 ? 80  HIS B CE1 1 
ATOM   2873 N NE2 . HIS B 1 78  ? 17.13700  -8.05200  -18.29600 1.000 51.46000 ? 80  HIS B NE2 1 
ATOM   2874 N N   . SER B 1 79  ? 15.14000  -5.39000  -13.83100 1.000 39.86000 ? 81  SER B N   1 
ATOM   2875 C CA  . SER B 1 79  ? 15.70500  -6.05600  -12.66900 1.000 40.32000 ? 81  SER B CA  1 
ATOM   2876 C C   . SER B 1 79  ? 14.55900  -6.59500  -11.83100 1.000 40.99000 ? 81  SER B C   1 
ATOM   2877 O O   . SER B 1 79  ? 13.39300  -6.24700  -12.03200 1.000 37.00000 ? 81  SER B O   1 
ATOM   2878 C CB  . SER B 1 79  ? 16.58100  -5.11300  -11.85000 1.000 38.15000 ? 81  SER B CB  1 
ATOM   2879 O OG  . SER B 1 79  ? 15.81400  -4.02400  -11.38100 1.000 39.76000 ? 81  SER B OG  1 
ATOM   2880 N N   . MET B 1 80  ? 14.91300  -7.45300  -10.88600 1.000 38.37000 ? 82  MET B N   1 
ATOM   2881 C CA  . MET B 1 80  ? 13.96900  -8.07200  -9.97700  1.000 37.88000 ? 82  MET B CA  1 
ATOM   2882 C C   . MET B 1 80  ? 14.29400  -7.61900  -8.56100  1.000 36.79000 ? 82  MET B C   1 
ATOM   2883 O O   . MET B 1 80  ? 15.46700  -7.50300  -8.19000  1.000 34.58000 ? 82  MET B O   1 
ATOM   2884 C CB  . MET B 1 80  ? 14.05300  -9.59600  -10.08100 1.000 36.28000 ? 82  MET B CB  1 
ATOM   2885 C CG  . MET B 1 80  ? 12.75700  -10.35300 -9.90700  1.000 34.87000 ? 82  MET B CG  1 
ATOM   2886 S SD  . MET B 1 80  ? 12.91700  -12.04100 -10.57500 1.000 45.33000 ? 82  MET B SD  1 
ATOM   2887 C CE  . MET B 1 80  ? 14.52100  -12.51000 -9.94000  1.000 44.46000 ? 82  MET B CE  1 
ATOM   2888 N N   . GLN B 1 81  ? 13.25700  -7.33400  -7.78200  1.000 28.83000 ? 83  GLN B N   1 
ATOM   2889 C CA  . GLN B 1 81  ? 13.39300  -7.19900  -6.33700  1.000 30.21000 ? 83  GLN B CA  1 
ATOM   2890 C C   . GLN B 1 81  ? 12.38100  -8.13800  -5.71400  1.000 27.84000 ? 83  GLN B C   1 
ATOM   2891 O O   . GLN B 1 81  ? 11.16900  -7.89100  -5.79100  1.000 27.95000 ? 83  GLN B O   1 
ATOM   2892 C CB  . GLN B 1 81  ? 13.17800  -5.77300  -5.84000  1.000 30.16000 ? 83  GLN B CB  1 
ATOM   2893 C CG  . GLN B 1 81  ? 13.43000  -5.69200  -4.33500  1.000 29.36000 ? 83  GLN B CG  1 
ATOM   2894 C CD  . GLN B 1 81  ? 13.18600  -4.33000  -3.77000  1.000 34.70000 ? 83  GLN B CD  1 
ATOM   2895 O OE1 . GLN B 1 81  ? 12.64300  -3.45500  -4.44500  1.000 32.00000 ? 83  GLN B OE1 1 
ATOM   2896 N NE2 . GLN B 1 81  ? 13.62300  -4.11800  -2.52900  1.000 37.10000 ? 83  GLN B NE2 1 
ATOM   2897 N N   . ASN B 1 82  ? 12.88000  -9.22500  -5.12600  1.000 30.88000 ? 84  ASN B N   1 
ATOM   2898 C CA  . ASN B 1 82  ? 11.99900  -10.22900 -4.56100  1.000 29.34000 ? 84  ASN B CA  1 
ATOM   2899 C C   . ASN B 1 82  ? 10.98800  -10.63500 -5.62500  1.000 30.26000 ? 84  ASN B C   1 
ATOM   2900 O O   . ASN B 1 82  ? 11.38900  -11.02900 -6.72700  1.000 28.03000 ? 84  ASN B O   1 
ATOM   2901 C CB  . ASN B 1 82  ? 11.35900  -9.67400  -3.29100  1.000 28.43000 ? 84  ASN B CB  1 
ATOM   2902 C CG  . ASN B 1 82  ? 12.40200  -9.36700  -2.21900  1.000 29.89000 ? 84  ASN B CG  1 
ATOM   2903 O OD1 . ASN B 1 82  ? 13.32800  -10.15800 -1.98900  1.000 27.48000 ? 84  ASN B OD1 1 
ATOM   2904 N ND2 . ASN B 1 82  ? 12.26600  -8.22100  -1.56900  1.000 26.49000 ? 84  ASN B ND2 1 
ATOM   2905 N N   . CYS B 1 83  ? 9.68500   -10.48100 -5.36600  1.000 28.83000 ? 85  CYS B N   1 
ATOM   2906 C CA  . CYS B 1 83  ? 8.70900   -10.97400 -6.32900  1.000 30.15000 ? 85  CYS B CA  1 
ATOM   2907 C C   . CYS B 1 83  ? 8.15000   -9.90000  -7.25400  1.000 31.24000 ? 85  CYS B C   1 
ATOM   2908 O O   . CYS B 1 83  ? 7.13900   -10.15800 -7.92200  1.000 32.86000 ? 85  CYS B O   1 
ATOM   2909 C CB  . CYS B 1 83  ? 7.56000   -11.68100 -5.61500  1.000 30.59000 ? 85  CYS B CB  1 
ATOM   2910 S SG  . CYS B 1 83  ? 8.08900   -13.11300 -4.67300  1.000 26.68000 ? 85  CYS B SG  1 
ATOM   2911 N N   . VAL B 1 84  ? 8.77200   -8.71900  -7.33500  1.000 29.10000 ? 86  VAL B N   1 
ATOM   2912 C CA  . VAL B 1 84  ? 8.34100   -7.68400  -8.27400  1.000 28.06000 ? 86  VAL B CA  1 
ATOM   2913 C C   . VAL B 1 84  ? 9.42800   -7.44500  -9.31300  1.000 32.79000 ? 86  VAL B C   1 
ATOM   2914 O O   . VAL B 1 84  ? 10.62300  -7.33600  -8.98400  1.000 30.95000 ? 86  VAL B O   1 
ATOM   2915 C CB  . VAL B 1 84  ? 7.94500   -6.36400  -7.58400  1.000 32.97000 ? 86  VAL B CB  1 
ATOM   2916 C CG1 . VAL B 1 84  ? 6.65300   -6.54300  -6.81100  1.000 32.31000 ? 86  VAL B CG1 1 
ATOM   2917 C CG2 . VAL B 1 84  ? 9.03400   -5.82600  -6.71100  1.000 34.77000 ? 86  VAL B CG2 1 
ATOM   2918 N N   . LEU B 1 85  ? 9.00100   -7.36700  -10.57100 1.000 28.16000 ? 87  LEU B N   1 
ATOM   2919 C CA  . LEU B 1 85  ? 9.86700   -6.93800  -11.66200 1.000 30.68000 ? 87  LEU B CA  1 
ATOM   2920 C C   . LEU B 1 85  ? 9.90400   -5.41400  -11.71500 1.000 30.99000 ? 87  LEU B C   1 
ATOM   2921 O O   . LEU B 1 85  ? 8.88400   -4.75900  -11.50600 1.000 29.89000 ? 87  LEU B O   1 
ATOM   2922 C CB  . LEU B 1 85  ? 9.34200   -7.50100  -12.98200 1.000 30.09000 ? 87  LEU B CB  1 
ATOM   2923 C CG  . LEU B 1 85  ? 10.12500  -7.26700  -14.26900 1.000 38.48000 ? 87  LEU B CG  1 
ATOM   2924 C CD1 . LEU B 1 85  ? 11.41700  -8.07400  -14.25800 1.000 40.42000 ? 87  LEU B CD1 1 
ATOM   2925 C CD2 . LEU B 1 85  ? 9.24500   -7.67600  -15.44500 1.000 36.98000 ? 87  LEU B CD2 1 
ATOM   2926 N N   . LYS B 1 86  ? 11.08600  -4.85200  -11.98400 1.000 34.21000 ? 88  LYS B N   1 
ATOM   2927 C CA  . LYS B 1 86  ? 11.27600  -3.40900  -12.12600 1.000 32.33000 ? 88  LYS B CA  1 
ATOM   2928 C C   . LYS B 1 86  ? 11.79500  -3.12500  -13.53000 1.000 38.28000 ? 88  LYS B C   1 
ATOM   2929 O O   . LYS B 1 86  ? 12.91900  -3.50800  -13.87800 1.000 33.66000 ? 88  LYS B O   1 
ATOM   2930 C CB  . LYS B 1 86  ? 12.24800  -2.86500  -11.08200 1.000 31.75000 ? 88  LYS B CB  1 
ATOM   2931 C CG  . LYS B 1 86  ? 11.65700  -2.63700  -9.70900  1.000 36.01000 ? 88  LYS B CG  1 
ATOM   2932 C CD  . LYS B 1 86  ? 12.73300  -2.77100  -8.63700  1.000 35.55000 ? 88  LYS B CD  1 
ATOM   2933 C CE  . LYS B 1 86  ? 12.87100  -1.51900  -7.80600  1.000 41.96000 ? 88  LYS B CE  1 
ATOM   2934 N NZ  . LYS B 1 86  ? 13.83300  -1.75200  -6.67800  1.000 45.15000 ? 88  LYS B NZ  1 
ATOM   2935 N N   . LEU B 1 87  ? 10.99000  -2.44700  -14.33200 1.000 34.83000 ? 89  LEU B N   1 
ATOM   2936 C CA  . LEU B 1 87  ? 11.37300  -2.07700  -15.68500 1.000 36.56000 ? 89  LEU B CA  1 
ATOM   2937 C C   . LEU B 1 87  ? 11.76700  -0.61100  -15.67800 1.000 39.47000 ? 89  LEU B C   1 
ATOM   2938 O O   . LEU B 1 87  ? 10.92900  0.25500   -15.42300 1.000 36.23000 ? 89  LEU B O   1 
ATOM   2939 C CB  . LEU B 1 87  ? 10.23600  -2.33600  -16.66500 1.000 37.77000 ? 89  LEU B CB  1 
ATOM   2940 C CG  . LEU B 1 87  ? 9.85400   -3.80700  -16.75600 1.000 37.00000 ? 89  LEU B CG  1 
ATOM   2941 C CD1 . LEU B 1 87  ? 8.70900   -4.01400  -17.74500 1.000 42.81000 ? 89  LEU B CD1 1 
ATOM   2942 C CD2 . LEU B 1 87  ? 11.07700  -4.59900  -17.15100 1.000 37.52000 ? 89  LEU B CD2 1 
ATOM   2943 N N   . LYS B 1 88  ? 13.05100  -0.34500  -15.91800 1.000 37.19000 ? 90  LYS B N   1 
ATOM   2944 C CA  . LYS B 1 88  ? 13.52000  1.01300   -16.14500 1.000 43.27000 ? 90  LYS B CA  1 
ATOM   2945 C C   . LYS B 1 88  ? 13.07400  1.48200   -17.52400 1.000 42.28000 ? 90  LYS B C   1 
ATOM   2946 O O   . LYS B 1 88  ? 13.32200  0.80700   -18.53000 1.000 40.52000 ? 90  LYS B O   1 
ATOM   2947 C CB  . LYS B 1 88  ? 15.04800  1.08300   -16.02600 1.000 39.18000 ? 90  LYS B CB  1 
ATOM   2948 C CG  . LYS B 1 88  ? 15.60300  2.49400   -15.81200 1.000 41.64000 ? 90  LYS B CG  1 
ATOM   2949 C CD  . LYS B 1 88  ? 15.21400  3.04600   -14.44000 1.000 42.70000 ? 90  LYS B CD  1 
ATOM   2950 C CE  . LYS B 1 88  ? 16.22100  4.05900   -13.92000 1.000 44.49000 ? 90  LYS B CE  1 
ATOM   2951 N NZ  . LYS B 1 88  ? 15.83900  4.59000   -12.56500 1.000 41.82000 ? 90  LYS B NZ  1 
ATOM   2952 N N   . VAL B 1 89  ? 12.40600  2.63400   -17.56600 1.000 37.84000 ? 91  VAL B N   1 
ATOM   2953 C CA  . VAL B 1 89  ? 11.93800  3.22700   -18.81100 1.000 42.29000 ? 91  VAL B CA  1 
ATOM   2954 C C   . VAL B 1 89  ? 12.61900  4.58400   -18.99400 1.000 41.83000 ? 91  VAL B C   1 
ATOM   2955 O O   . VAL B 1 89  ? 13.19600  5.14600   -18.06000 1.000 41.65000 ? 91  VAL B O   1 
ATOM   2956 C CB  . VAL B 1 89  ? 10.39800  3.35400   -18.84400 1.000 40.30000 ? 91  VAL B CB  1 
ATOM   2957 C CG1 . VAL B 1 89  ? 9.77800   1.98400   -18.82800 1.000 39.08000 ? 91  VAL B CG1 1 
ATOM   2958 C CG2 . VAL B 1 89  ? 9.89500   4.18300   -17.65100 1.000 41.26000 ? 91  VAL B CG2 1 
ATOM   2959 N N   . ASP B 1 90  ? 12.56600  5.10200   -20.22400 1.000 42.82000 ? 92  ASP B N   1 
ATOM   2960 C CA  . ASP B 1 90  ? 13.34800  6.29200   -20.55500 1.000 44.65000 ? 92  ASP B CA  1 
ATOM   2961 C C   . ASP B 1 90  ? 12.67300  7.59400   -20.14900 1.000 46.42000 ? 92  ASP B C   1 
ATOM   2962 O O   . ASP B 1 90  ? 13.28300  8.65700   -20.29800 1.000 47.55000 ? 92  ASP B O   1 
ATOM   2963 C CB  . ASP B 1 90  ? 13.65900  6.33600   -22.05700 1.000 44.15000 ? 92  ASP B CB  1 
ATOM   2964 C CG  . ASP B 1 90  ? 12.40800  6.36100   -22.92800 1.000 49.13000 ? 92  ASP B CG  1 
ATOM   2965 O OD1 . ASP B 1 90  ? 11.28200  6.57200   -22.42100 1.000 51.05000 ? 92  ASP B OD1 1 
ATOM   2966 O OD2 . ASP B 1 90  ? 12.55600  6.16400   -24.15000 1.000 56.57000 ? 92  ASP B OD2 1 
ATOM   2967 N N   . THR B 1 91  ? 11.43500  7.54600   -19.66100 1.000 45.46000 ? 93  THR B N   1 
ATOM   2968 C CA  . THR B 1 91  ? 10.68800  8.74900   -19.32700 1.000 47.42000 ? 93  THR B CA  1 
ATOM   2969 C C   . THR B 1 91  ? 10.18600  8.66100   -17.89700 1.000 42.61000 ? 93  THR B C   1 
ATOM   2970 O O   . THR B 1 91  ? 9.54800   7.67600   -17.52100 1.000 39.56000 ? 93  THR B O   1 
ATOM   2971 C CB  . THR B 1 91  ? 9.50200   8.94700   -20.27000 1.000 47.39000 ? 93  THR B CB  1 
ATOM   2972 O OG1 . THR B 1 91  ? 9.94900   8.83500   -21.62700 1.000 53.49000 ? 93  THR B OG1 1 
ATOM   2973 C CG2 . THR B 1 91  ? 8.88100   10.32400  -20.04600 1.000 44.07000 ? 93  THR B CG2 1 
ATOM   2974 N N   . ALA B 1 92  ? 10.46700  9.69000   -17.10700 1.000 40.55000 ? 94  ALA B N   1 
ATOM   2975 C CA  . ALA B 1 92  ? 9.85400   9.79400   -15.79500 1.000 40.64000 ? 94  ALA B CA  1 
ATOM   2976 C C   . ALA B 1 92  ? 8.36700   10.09800  -15.95000 1.000 42.52000 ? 94  ALA B C   1 
ATOM   2977 O O   . ALA B 1 92  ? 7.96800   10.92200  -16.78100 1.000 40.65000 ? 94  ALA B O   1 
ATOM   2978 C CB  . ALA B 1 92  ? 10.54200  10.88100  -14.97200 1.000 38.72000 ? 94  ALA B CB  1 
ATOM   2979 N N   . ASN B 1 93  ? 7.53400   9.39900   -15.16800 1.000 36.37000 ? 95  ASN B N   1 
ATOM   2980 C CA  . ASN B 1 93  ? 6.10100   9.67700   -15.19100 1.000 35.30000 ? 95  ASN B CA  1 
ATOM   2981 C C   . ASN B 1 93  ? 5.83800   11.10200  -14.71000 1.000 32.93000 ? 95  ASN B C   1 
ATOM   2982 O O   . ASN B 1 93  ? 6.04400   11.40500  -13.53200 1.000 32.77000 ? 95  ASN B O   1 
ATOM   2983 C CB  . ASN B 1 93  ? 5.34700   8.66900   -14.31900 1.000 33.12000 ? 95  ASN B CB  1 
ATOM   2984 C CG  . ASN B 1 93  ? 3.83500   8.81000   -14.42900 1.000 36.62000 ? 95  ASN B CG  1 
ATOM   2985 O OD1 . ASN B 1 93  ? 3.32400   9.71200   -15.10400 1.000 33.91000 ? 95  ASN B OD1 1 
ATOM   2986 N ND2 . ASN B 1 93  ? 3.10600   7.91000   -13.75700 1.000 33.44000 ? 95  ASN B ND2 1 
ATOM   2987 N N   . PRO B 1 94  ? 5.37700   12.00600  -15.58100 1.000 35.08000 ? 96  PRO B N   1 
ATOM   2988 C CA  . PRO B 1 94  ? 5.12100   13.38300  -15.12600 1.000 36.90000 ? 96  PRO B CA  1 
ATOM   2989 C C   . PRO B 1 94  ? 3.95000   13.48500  -14.15600 1.000 35.21000 ? 96  PRO B C   1 
ATOM   2990 O O   . PRO B 1 94  ? 3.78200   14.53200  -13.52300 1.000 35.41000 ? 96  PRO B O   1 
ATOM   2991 C CB  . PRO B 1 94  ? 4.84600   14.13700  -16.43100 1.000 36.17000 ? 96  PRO B CB  1 
ATOM   2992 C CG  . PRO B 1 94  ? 4.27500   13.09300  -17.34900 1.000 38.07000 ? 96  PRO B CG  1 
ATOM   2993 C CD  . PRO B 1 94  ? 4.89800   11.76700  -16.95400 1.000 34.89000 ? 96  PRO B CD  1 
ATOM   2994 N N   . LYS B 1 95  ? 3.16200   12.42500  -14.00100 1.000 34.48000 ? 97  LYS B N   1 
ATOM   2995 C CA  . LYS B 1 95  ? 2.06800   12.36400  -13.04300 1.000 35.15000 ? 97  LYS B CA  1 
ATOM   2996 C C   . LYS B 1 95  ? 2.45700   11.68100  -11.73300 1.000 36.82000 ? 97  LYS B C   1 
ATOM   2997 O O   . LYS B 1 95  ? 1.57800   11.40300  -10.91100 1.000 36.09000 ? 97  LYS B O   1 
ATOM   2998 C CB  . LYS B 1 95  ? 0.87500   11.63300  -13.66300 1.000 34.97000 ? 97  LYS B CB  1 
ATOM   2999 C CG  . LYS B 1 95  ? 0.18000   12.38800  -14.79500 1.000 39.94000 ? 97  LYS B CG  1 
ATOM   3000 C CD  . LYS B 1 95  ? -0.82300  11.46300  -15.48700 1.000 43.10000 ? 97  LYS B CD  1 
ATOM   3001 C CE  . LYS B 1 95  ? -1.33400  12.04000  -16.80700 1.000 50.40000 ? 97  LYS B CE  1 
ATOM   3002 N NZ  . LYS B 1 95  ? -1.80400  10.94700  -17.71600 1.000 49.00000 ? 97  LYS B NZ  1 
ATOM   3003 N N   . THR B 1 96  ? 3.73700   11.39100  -11.51700 1.000 34.36000 ? 98  THR B N   1 
ATOM   3004 C CA  . THR B 1 96  ? 4.12400   10.69200  -10.29400 1.000 34.06000 ? 98  THR B CA  1 
ATOM   3005 C C   . THR B 1 96  ? 3.70300   11.51400  -9.07500  1.000 32.69000 ? 98  THR B C   1 
ATOM   3006 O O   . THR B 1 96  ? 4.07700   12.69000  -8.97600  1.000 31.13000 ? 98  THR B O   1 
ATOM   3007 C CB  . THR B 1 96  ? 5.63500   10.44000  -10.25500 1.000 35.01000 ? 98  THR B CB  1 
ATOM   3008 O OG1 . THR B 1 96  ? 6.05000   9.82000   -11.47700 1.000 33.87000 ? 98  THR B OG1 1 
ATOM   3009 C CG2 . THR B 1 96  ? 5.98500   9.52500   -9.08900  1.000 30.14000 ? 98  THR B CG2 1 
ATOM   3010 N N   . PRO B 1 97  ? 2.92400   10.96200  -8.15300  1.000 30.34000 ? 99  PRO B N   1 
ATOM   3011 C CA  . PRO B 1 97  ? 2.55400   11.71900  -6.95100  1.000 29.88000 ? 99  PRO B CA  1 
ATOM   3012 C C   . PRO B 1 97  ? 3.68600   11.66100  -5.93400  1.000 33.08000 ? 99  PRO B C   1 
ATOM   3013 O O   . PRO B 1 97  ? 4.64000   10.89900  -6.08300  1.000 32.73000 ? 99  PRO B O   1 
ATOM   3014 C CB  . PRO B 1 97  ? 1.30900   10.97900  -6.44900  1.000 33.32000 ? 99  PRO B CB  1 
ATOM   3015 C CG  . PRO B 1 97  ? 1.55800   9.53900   -6.86000  1.000 30.93000 ? 99  PRO B CG  1 
ATOM   3016 C CD  . PRO B 1 97  ? 2.35200   9.60300   -8.16000  1.000 29.53000 ? 99  PRO B CD  1 
ATOM   3017 N N   . LYS B 1 98  ? 3.59000   12.49700  -4.89900  1.000 27.33000 ? 100 LYS B N   1 
ATOM   3018 C CA  . LYS B 1 98  ? 4.34100   12.17500  -3.69100  1.000 31.03000 ? 100 LYS B CA  1 
ATOM   3019 C C   . LYS B 1 98  ? 3.90300   10.78800  -3.23500  1.000 29.27000 ? 100 LYS B C   1 
ATOM   3020 O O   . LYS B 1 98  ? 2.70200   10.50800  -3.16900  1.000 29.40000 ? 100 LYS B O   1 
ATOM   3021 C CB  . LYS B 1 98  ? 4.08300   13.19200  -2.58200  1.000 28.19000 ? 100 LYS B CB  1 
ATOM   3022 N N   . TYR B 1 99  ? 4.86200   9.91000   -2.94300  1.000 28.47000 ? 101 TYR B N   1 
ATOM   3023 C CA  . TYR B 1 99  ? 4.48400   8.54500   -2.58000  1.000 28.53000 ? 101 TYR B CA  1 
ATOM   3024 C C   . TYR B 1 99  ? 5.50200   7.94800   -1.62600  1.000 29.87000 ? 101 TYR B C   1 
ATOM   3025 O O   . TYR B 1 99  ? 6.64300   8.40500   -1.54200  1.000 28.72000 ? 101 TYR B O   1 
ATOM   3026 C CB  . TYR B 1 99  ? 4.32300   7.65100   -3.82300  1.000 28.07000 ? 101 TYR B CB  1 
ATOM   3027 C CG  . TYR B 1 99  ? 5.63000   7.22500   -4.47300  1.000 32.01000 ? 101 TYR B CG  1 
ATOM   3028 C CD1 . TYR B 1 99  ? 6.27000   8.04000   -5.41100  1.000 29.33000 ? 101 TYR B CD1 1 
ATOM   3029 C CD2 . TYR B 1 99  ? 6.21800   6.01500   -4.15500  1.000 30.57000 ? 101 TYR B CD2 1 
ATOM   3030 C CE1 . TYR B 1 99  ? 7.46000   7.65500   -6.00000  1.000 30.67000 ? 101 TYR B CE1 1 
ATOM   3031 C CE2 . TYR B 1 99  ? 7.40600   5.62800   -4.73200  1.000 26.74000 ? 101 TYR B CE2 1 
ATOM   3032 C CZ  . TYR B 1 99  ? 8.01500   6.43100   -5.64600  1.000 33.19000 ? 101 TYR B CZ  1 
ATOM   3033 O OH  . TYR B 1 99  ? 9.18400   6.00600   -6.20200  1.000 33.65000 ? 101 TYR B OH  1 
ATOM   3034 N N   . LYS B 1 100 ? 5.06100   6.91000   -0.90300  1.000 32.30000 ? 102 LYS B N   1 
ATOM   3035 C CA  . LYS B 1 100 ? 5.91800   6.01900   -0.12900  1.000 31.66000 ? 102 LYS B CA  1 
ATOM   3036 C C   . LYS B 1 100 ? 5.52200   4.57700   -0.41100  1.000 28.73000 ? 102 LYS B C   1 
ATOM   3037 O O   . LYS B 1 100 ? 4.36700   4.29400   -0.74800  1.000 26.90000 ? 102 LYS B O   1 
ATOM   3038 C CB  . LYS B 1 100 ? 5.79300   6.25100   1.38300   1.000 33.28000 ? 102 LYS B CB  1 
ATOM   3039 C CG  . LYS B 1 100 ? 6.10100   7.66400   1.82000   1.000 38.38000 ? 102 LYS B CG  1 
ATOM   3040 C CD  . LYS B 1 100 ? 5.37500   7.99400   3.10400   1.000 39.51000 ? 102 LYS B CD  1 
ATOM   3041 C CE  . LYS B 1 100 ? 5.72500   7.01100   4.20500   1.000 45.63000 ? 102 LYS B CE  1 
ATOM   3042 N NZ  . LYS B 1 100 ? 5.34400   7.57900   5.53300   1.000 58.38000 ? 102 LYS B NZ  1 
ATOM   3043 N N   . PHE B 1 101 ? 6.48500   3.66700   -0.26600  1.000 24.45000 ? 103 PHE B N   1 
ATOM   3044 C CA  . PHE B 1 101 ? 6.19400   2.23800   -0.19100  1.000 25.67000 ? 103 PHE B CA  1 
ATOM   3045 C C   . PHE B 1 101 ? 6.09600   1.86600   1.28400   1.000 27.39000 ? 103 PHE B C   1 
ATOM   3046 O O   . PHE B 1 101 ? 7.02900   2.11700   2.04800   1.000 29.40000 ? 103 PHE B O   1 
ATOM   3047 C CB  . PHE B 1 101 ? 7.28900   1.40600   -0.86500  1.000 28.67000 ? 103 PHE B CB  1 
ATOM   3048 C CG  . PHE B 1 101 ? 7.31900   1.50000   -2.36900  1.000 26.78000 ? 103 PHE B CG  1 
ATOM   3049 C CD1 . PHE B 1 101 ? 6.28000   2.09500   -3.07700  1.000 22.72000 ? 103 PHE B CD1 1 
ATOM   3050 C CD2 . PHE B 1 101 ? 8.40000   0.95900   -3.07800  1.000 27.56000 ? 103 PHE B CD2 1 
ATOM   3051 C CE1 . PHE B 1 101 ? 6.32400   2.16800   -4.47800  1.000 26.55000 ? 103 PHE B CE1 1 
ATOM   3052 C CE2 . PHE B 1 101 ? 8.45500   1.02400   -4.47200  1.000 26.92000 ? 103 PHE B CE2 1 
ATOM   3053 C CZ  . PHE B 1 101 ? 7.41400   1.62000   -5.17700  1.000 28.21000 ? 103 PHE B CZ  1 
ATOM   3054 N N   . VAL B 1 102 ? 4.97100   1.28000   1.69600   1.000 30.32000 ? 104 VAL B N   1 
ATOM   3055 C CA  . VAL B 1 102 ? 4.81200   0.87000   3.08600   1.000 25.40000 ? 104 VAL B CA  1 
ATOM   3056 C C   . VAL B 1 102 ? 4.33700   -0.57300  3.11000   1.000 25.50000 ? 104 VAL B C   1 
ATOM   3057 O O   . VAL B 1 102 ? 3.71500   -1.06900  2.16700   1.000 30.10000 ? 104 VAL B O   1 
ATOM   3058 C CB  . VAL B 1 102 ? 3.82800   1.76600   3.87200   1.000 26.95000 ? 104 VAL B CB  1 
ATOM   3059 C CG1 . VAL B 1 102 ? 4.21500   3.25900   3.76300   1.000 29.64000 ? 104 VAL B CG1 1 
ATOM   3060 C CG2 . VAL B 1 102 ? 2.41800   1.56100   3.36900   1.000 27.64000 ? 104 VAL B CG2 1 
ATOM   3061 N N   . ARG B 1 103 ? 4.62000   -1.23900  4.21400   1.000 24.46000 ? 105 ARG B N   1 
ATOM   3062 C CA  . ARG B 1 103 ? 4.14600   -2.60200  4.43200   1.000 28.53000 ? 105 ARG B CA  1 
ATOM   3063 C C   . ARG B 1 103 ? 3.16000   -2.55800  5.58500   1.000 29.61000 ? 105 ARG B C   1 
ATOM   3064 O O   . ARG B 1 103 ? 3.49200   -2.07100  6.66600   1.000 28.94000 ? 105 ARG B O   1 
ATOM   3065 C CB  . ARG B 1 103 ? 5.31200   -3.54700  4.72400   1.000 29.11000 ? 105 ARG B CB  1 
ATOM   3066 C CG  . ARG B 1 103 ? 4.85100   -4.96800  5.03700   1.000 26.05000 ? 105 ARG B CG  1 
ATOM   3067 C CD  . ARG B 1 103 ? 5.99000   -5.97900  5.07800   1.000 30.14000 ? 105 ARG B CD  1 
ATOM   3068 N NE  . ARG B 1 103 ? 5.48400   -7.35300  5.25100   1.000 24.12000 ? 105 ARG B NE  1 
ATOM   3069 C CZ  . ARG B 1 103 ? 5.15900   -8.16500  4.24500   1.000 27.63000 ? 105 ARG B CZ  1 
ATOM   3070 N NH1 . ARG B 1 103 ? 5.28500   -7.76100  2.98400   1.000 25.35000 ? 105 ARG B NH1 1 
ATOM   3071 N NH2 . ARG B 1 103 ? 4.72000   -9.40400  4.49600   1.000 29.22000 ? 105 ARG B NH2 1 
ATOM   3072 N N   . ILE B 1 104 ? 1.94100   -3.04400  5.35700   1.000 26.47000 ? 106 ILE B N   1 
ATOM   3073 C CA  . ILE B 1 104 ? 0.88400   -2.91200  6.34600   1.000 31.56000 ? 106 ILE B CA  1 
ATOM   3074 C C   . ILE B 1 104 ? 0.77200   -4.19400  7.15700   1.000 31.10000 ? 106 ILE B C   1 
ATOM   3075 O O   . ILE B 1 104 ? 1.35500   -5.22300  6.82300   1.000 29.89000 ? 106 ILE B O   1 
ATOM   3076 C CB  . ILE B 1 104 ? -0.46500  -2.52500  5.69300   1.000 32.76000 ? 106 ILE B CB  1 
ATOM   3077 C CG1 . ILE B 1 104 ? -0.77100  -3.47100  4.53100   1.000 32.21000 ? 106 ILE B CG1 1 
ATOM   3078 C CG2 . ILE B 1 104 ? -0.39600  -1.10000  5.20000   1.000 29.72000 ? 106 ILE B CG2 1 
ATOM   3079 C CD1 . ILE B 1 104 ? -2.22200  -3.58000  4.22000   1.000 30.32000 ? 106 ILE B CD1 1 
ATOM   3080 N N   . GLN B 1 105 ? 0.06500   -4.12000  8.28000   1.000 31.59000 ? 107 GLN B N   1 
ATOM   3081 C CA  . GLN B 1 105 ? -0.16900  -5.23800  9.18200   1.000 34.54000 ? 107 GLN B CA  1 
ATOM   3082 C C   . GLN B 1 105 ? -1.57100  -5.79500  8.97300   1.000 33.36000 ? 107 GLN B C   1 
ATOM   3083 O O   . GLN B 1 105 ? -2.47500  -5.06000  8.55800   1.000 33.94000 ? 107 GLN B O   1 
ATOM   3084 C CB  . GLN B 1 105 ? -0.01000  -4.78400  10.64000  1.000 38.33000 ? 107 GLN B CB  1 
ATOM   3085 C CG  . GLN B 1 105 ? 1.45500   -4.63300  11.10600  1.000 45.38000 ? 107 GLN B CG  1 
ATOM   3086 C CD  . GLN B 1 105 ? 2.09500   -5.97100  11.44700  1.000 49.29000 ? 107 GLN B CD  1 
ATOM   3087 O OE1 . GLN B 1 105 ? 3.12500   -6.34800  10.87900  1.000 57.47000 ? 107 GLN B OE1 1 
ATOM   3088 N NE2 . GLN B 1 105 ? 1.47500   -6.70900  12.36800  1.000 54.96000 ? 107 GLN B NE2 1 
ATOM   3089 N N   . PRO B 1 106 ? -1.79000  -7.08000  9.25400   1.000 35.86000 ? 108 PRO B N   1 
ATOM   3090 C CA  . PRO B 1 106 ? -3.14800  -7.63200  9.16000   1.000 32.44000 ? 108 PRO B CA  1 
ATOM   3091 C C   . PRO B 1 106 ? -4.11700  -6.80900  9.98800   1.000 30.98000 ? 108 PRO B C   1 
ATOM   3092 O O   . PRO B 1 106 ? -3.77900  -6.33400  11.07000  1.000 35.03000 ? 108 PRO B O   1 
ATOM   3093 C CB  . PRO B 1 106 ? -3.00500  -9.04800  9.72400   1.000 33.79000 ? 108 PRO B CB  1 
ATOM   3094 C CG  . PRO B 1 106 ? -1.57600  -9.37500  9.60200   1.000 34.98000 ? 108 PRO B CG  1 
ATOM   3095 C CD  . PRO B 1 106 ? -0.81200  -8.08600  9.71100   1.000 33.79000 ? 108 PRO B CD  1 
ATOM   3096 N N   . GLY B 1 107 ? -5.32800  -6.62500  9.46200   1.000 34.51000 ? 109 GLY B N   1 
ATOM   3097 C CA  . GLY B 1 107 ? -6.30700  -5.78200  10.11200  1.000 30.77000 ? 109 GLY B CA  1 
ATOM   3098 C C   . GLY B 1 107 ? -6.30800  -4.33700  9.67000   1.000 36.04000 ? 109 GLY B C   1 
ATOM   3099 O O   . GLY B 1 107 ? -7.24500  -3.59300  10.01900  1.000 33.65000 ? 109 GLY B O   1 
ATOM   3100 N N   . GLN B 1 108 ? -5.29700  -3.90500  8.92100   1.000 30.00000 ? 110 GLN B N   1 
ATOM   3101 C CA  . GLN B 1 108 ? -5.27100  -2.55200  8.38900   1.000 30.00000 ? 110 GLN B CA  1 
ATOM   3102 C C   . GLN B 1 108 ? -5.96200  -2.52400  7.03000   1.000 29.32000 ? 110 GLN B C   1 
ATOM   3103 O O   . GLN B 1 108 ? -5.98500  -3.52100  6.30400   1.000 29.81000 ? 110 GLN B O   1 
ATOM   3104 C CB  . GLN B 1 108 ? -3.83300  -2.04500  8.26300   1.000 28.88000 ? 110 GLN B CB  1 
ATOM   3105 C CG  . GLN B 1 108 ? -3.12900  -1.78300  9.60200   1.000 32.04000 ? 110 GLN B CG  1 
ATOM   3106 C CD  . GLN B 1 108 ? -1.75400  -1.13500  9.42300   1.000 35.03000 ? 110 GLN B CD  1 
ATOM   3107 O OE1 . GLN B 1 108 ? -0.78800  -1.79700  9.04700   1.000 38.62000 ? 110 GLN B OE1 1 
ATOM   3108 N NE2 . GLN B 1 108 ? -1.66600  0.16700   9.69000   1.000 44.26000 ? 110 GLN B NE2 1 
ATOM   3109 N N   . THR B 1 109 ? -6.53600  -1.37400  6.69300   1.000 31.03000 ? 111 THR B N   1 
ATOM   3110 C CA  . THR B 1 109 ? -7.35300  -1.25700  5.49600   1.000 28.77000 ? 111 THR B CA  1 
ATOM   3111 C C   . THR B 1 109 ? -6.63000  -0.44000  4.43200   1.000 30.53000 ? 111 THR B C   1 
ATOM   3112 O O   . THR B 1 109 ? -5.70400  0.32100   4.72300   1.000 31.34000 ? 111 THR B O   1 
ATOM   3113 C CB  . THR B 1 109 ? -8.70700  -0.61800  5.82500   1.000 29.37000 ? 111 THR B CB  1 
ATOM   3114 O OG1 . THR B 1 109 ? -8.50500  0.66500   6.43000   1.000 28.87000 ? 111 THR B OG1 1 
ATOM   3115 C CG2 . THR B 1 109 ? -9.51000  -1.52200  6.77400   1.000 30.36000 ? 111 THR B CG2 1 
ATOM   3116 N N   . PHE B 1 110 ? -7.07400  -0.59200  3.18800   1.000 26.27000 ? 112 PHE B N   1 
ATOM   3117 C CA  . PHE B 1 110 ? -6.52500  0.20800   2.10100   1.000 30.75000 ? 112 PHE B CA  1 
ATOM   3118 C C   . PHE B 1 110 ? -7.52300  0.20000   0.95300   1.000 31.14000 ? 112 PHE B C   1 
ATOM   3119 O O   . PHE B 1 110 ? -8.45000  -0.61100  0.91700   1.000 30.13000 ? 112 PHE B O   1 
ATOM   3120 C CB  . PHE B 1 110 ? -5.16000  -0.32100  1.64500   1.000 26.04000 ? 112 PHE B CB  1 
ATOM   3121 C CG  . PHE B 1 110 ? -5.16300  -1.78900  1.32200   1.000 27.06000 ? 112 PHE B CG  1 
ATOM   3122 C CD1 . PHE B 1 110 ? -5.00000  -2.72900  2.32300   1.000 29.78000 ? 112 PHE B CD1 1 
ATOM   3123 C CD2 . PHE B 1 110 ? -5.33500  -2.23100  0.01500   1.000 25.80000 ? 112 PHE B CD2 1 
ATOM   3124 C CE1 . PHE B 1 110 ? -5.00100  -4.09300  2.02600   1.000 32.16000 ? 112 PHE B CE1 1 
ATOM   3125 C CE2 . PHE B 1 110 ? -5.34200  -3.58700  -0.28700  1.000 34.13000 ? 112 PHE B CE2 1 
ATOM   3126 C CZ  . PHE B 1 110 ? -5.16500  -4.52100  0.71700   1.000 33.51000 ? 112 PHE B CZ  1 
ATOM   3127 N N   . SER B 1 111 ? -7.30500  1.10300   0.00600   1.000 27.91000 ? 113 SER B N   1 
ATOM   3128 C CA  . SER B 1 111 ? -8.09700  1.16600   -1.21200  1.000 27.44000 ? 113 SER B CA  1 
ATOM   3129 C C   . SER B 1 111 ? -7.37400  0.43500   -2.32800  1.000 27.16000 ? 113 SER B C   1 
ATOM   3130 O O   . SER B 1 111 ? -6.15100  0.49400   -2.41800  1.000 26.35000 ? 113 SER B O   1 
ATOM   3131 C CB  . SER B 1 111 ? -8.34300  2.61800   -1.63200  1.000 26.98000 ? 113 SER B CB  1 
ATOM   3132 O OG  . SER B 1 111 ? -9.19800  3.24100   -0.70400  1.000 31.02000 ? 113 SER B OG  1 
ATOM   3133 N N   . VAL B 1 112 ? -8.13700  -0.23900  -3.18100  1.000 25.99000 ? 114 VAL B N   1 
ATOM   3134 C CA  . VAL B 1 112 ? -7.60300  -0.98500  -4.31200  1.000 26.51000 ? 114 VAL B CA  1 
ATOM   3135 C C   . VAL B 1 112 ? -8.14600  -0.35200  -5.58200  1.000 28.01000 ? 114 VAL B C   1 
ATOM   3136 O O   . VAL B 1 112 ? -9.35400  -0.13200  -5.69900  1.000 31.24000 ? 114 VAL B O   1 
ATOM   3137 C CB  . VAL B 1 112 ? -7.99600  -2.47200  -4.23300  1.000 30.34000 ? 114 VAL B CB  1 
ATOM   3138 C CG1 . VAL B 1 112 ? -8.01800  -3.10500  -5.62100  1.000 30.36000 ? 114 VAL B CG1 1 
ATOM   3139 C CG2 . VAL B 1 112 ? -7.06100  -3.20100  -3.30600  1.000 30.28000 ? 114 VAL B CG2 1 
ATOM   3140 N N   . LEU B 1 113 ? -7.26500  -0.04400  -6.51600  1.000 27.96000 ? 115 LEU B N   1 
ATOM   3141 C CA  . LEU B 1 113 ? -7.66600  0.39200   -7.85000  1.000 28.09000 ? 115 LEU B CA  1 
ATOM   3142 C C   . LEU B 1 113 ? -7.52300  -0.80000  -8.79900  1.000 32.69000 ? 115 LEU B C   1 
ATOM   3143 O O   . LEU B 1 113 ? -6.42900  -1.09400  -9.30400  1.000 27.33000 ? 115 LEU B O   1 
ATOM   3144 C CB  . LEU B 1 113 ? -6.83400  1.58300   -8.30500  1.000 27.97000 ? 115 LEU B CB  1 
ATOM   3145 C CG  . LEU B 1 113 ? -7.27600  2.18500   -9.62900  1.000 32.56000 ? 115 LEU B CG  1 
ATOM   3146 C CD1 . LEU B 1 113 ? -8.71200  2.75100   -9.49800  1.000 28.75000 ? 115 LEU B CD1 1 
ATOM   3147 C CD2 . LEU B 1 113 ? -6.30100  3.27500   -10.04700 1.000 29.57000 ? 115 LEU B CD2 1 
ATOM   3148 N N   . ALA B 1 114 ? -8.63500  -1.48800  -9.04300  1.000 31.58000 ? 116 ALA B N   1 
ATOM   3149 C CA  . ALA B 1 114 ? -8.60800  -2.65600  -9.91600  1.000 28.32000 ? 116 ALA B CA  1 
ATOM   3150 C C   . ALA B 1 114 ? -8.43800  -2.20200  -11.36000 1.000 36.62000 ? 116 ALA B C   1 
ATOM   3151 O O   . ALA B 1 114 ? -9.14300  -1.29000  -11.82800 1.000 35.55000 ? 116 ALA B O   1 
ATOM   3152 C CB  . ALA B 1 114 ? -9.89500  -3.47400  -9.75900  1.000 34.35000 ? 116 ALA B CB  1 
ATOM   3153 N N   . CYS B 1 115 ? -7.48100  -2.81000  -12.06000 1.000 31.74000 ? 117 CYS B N   1 
ATOM   3154 C CA  . CYS B 1 115 ? -7.17000  -2.42500  -13.42700 1.000 33.06000 ? 117 CYS B CA  1 
ATOM   3155 C C   . CYS B 1 115 ? -7.11100  -3.65400  -14.32000 1.000 36.70000 ? 117 CYS B C   1 
ATOM   3156 O O   . CYS B 1 115 ? -6.92400  -4.78500  -13.85900 1.000 35.61000 ? 117 CYS B O   1 
ATOM   3157 C CB  . CYS B 1 115 ? -5.84700  -1.65600  -13.52900 1.000 32.02000 ? 117 CYS B CB  1 
ATOM   3158 S SG  . CYS B 1 115 ? -5.73400  -0.20000  -12.47300 1.000 36.79000 ? 117 CYS B SG  1 
ATOM   3159 N N   . TYR B 1 116 ? -7.30600  -3.41000  -15.61200 1.000 36.98000 ? 118 TYR B N   1 
ATOM   3160 C CA  . TYR B 1 116 ? -7.21700  -4.43900  -16.63100 1.000 37.98000 ? 118 TYR B CA  1 
ATOM   3161 C C   . TYR B 1 116 ? -6.62600  -3.78900  -17.86700 1.000 38.27000 ? 118 TYR B C   1 
ATOM   3162 O O   . TYR B 1 116 ? -7.09400  -2.72900  -18.29800 1.000 36.80000 ? 118 TYR B O   1 
ATOM   3163 C CB  . TYR B 1 116 ? -8.58900  -5.06900  -16.90200 1.000 37.40000 ? 118 TYR B CB  1 
ATOM   3164 C CG  . TYR B 1 116 ? -9.15100  -5.70200  -15.64600 1.000 37.95000 ? 118 TYR B CG  1 
ATOM   3165 C CD1 . TYR B 1 116 ? -8.75600  -6.97500  -15.24600 1.000 37.50000 ? 118 TYR B CD1 1 
ATOM   3166 C CD2 . TYR B 1 116 ? -10.03900 -5.00700  -14.83500 1.000 38.62000 ? 118 TYR B CD2 1 
ATOM   3167 C CE1 . TYR B 1 116 ? -9.23900  -7.53800  -14.08600 1.000 35.03000 ? 118 TYR B CE1 1 
ATOM   3168 C CE2 . TYR B 1 116 ? -10.52800 -5.56100  -13.67900 1.000 35.13000 ? 118 TYR B CE2 1 
ATOM   3169 C CZ  . TYR B 1 116 ? -10.12600 -6.82400  -13.30600 1.000 34.88000 ? 118 TYR B CZ  1 
ATOM   3170 O OH  . TYR B 1 116 ? -10.62000 -7.35800  -12.14600 1.000 37.28000 ? 118 TYR B OH  1 
ATOM   3171 N N   . ASN B 1 117 ? -5.55000  -4.39000  -18.37600 1.000 38.40000 ? 119 ASN B N   1 
ATOM   3172 C CA  . ASN B 1 117 ? -4.81500  -3.88700  -19.53900 1.000 39.42000 ? 119 ASN B CA  1 
ATOM   3173 C C   . ASN B 1 117 ? -4.26200  -2.48500  -19.29400 1.000 41.52000 ? 119 ASN B C   1 
ATOM   3174 O O   . ASN B 1 117 ? -4.17400  -1.65700  -20.21000 1.000 39.75000 ? 119 ASN B O   1 
ATOM   3175 C CB  . ASN B 1 117 ? -5.69200  -3.93900  -20.79400 1.000 43.87000 ? 119 ASN B CB  1 
ATOM   3176 C CG  . ASN B 1 117 ? -6.21000  -5.34900  -21.08100 1.000 46.23000 ? 119 ASN B CG  1 
ATOM   3177 O OD1 . ASN B 1 117 ? -5.44200  -6.24300  -21.43300 1.000 48.80000 ? 119 ASN B OD1 1 
ATOM   3178 N ND2 . ASN B 1 117 ? -7.51400  -5.55100  -20.91900 1.000 48.59000 ? 119 ASN B ND2 1 
ATOM   3179 N N   . GLY B 1 118 ? -3.86700  -2.21600  -18.04900 1.000 38.58000 ? 120 GLY B N   1 
ATOM   3180 C CA  . GLY B 1 118 ? -3.36700  -0.91800  -17.66900 1.000 36.66000 ? 120 GLY B CA  1 
ATOM   3181 C C   . GLY B 1 118 ? -4.40800  0.16900   -17.50600 1.000 37.80000 ? 120 GLY B C   1 
ATOM   3182 O O   . GLY B 1 118 ? -4.03700  1.32500   -17.29000 1.000 35.80000 ? 120 GLY B O   1 
ATOM   3183 N N   . SER B 1 119 ? -5.69600  -0.14100  -17.60400 1.000 37.87000 ? 121 SER B N   1 
ATOM   3184 C CA  . SER B 1 119 ? -6.70300  0.91500   -17.53700 1.000 40.50000 ? 121 SER B CA  1 
ATOM   3185 C C   . SER B 1 119 ? -7.54900  0.75100   -16.28000 1.000 34.02000 ? 121 SER B C   1 
ATOM   3186 O O   . SER B 1 119 ? -8.14300  -0.31500  -16.07000 1.000 32.11000 ? 121 SER B O   1 
ATOM   3187 C CB  . SER B 1 119 ? -7.59100  0.94500   -18.78400 1.000 37.41000 ? 121 SER B CB  1 
ATOM   3188 O OG  . SER B 1 119 ? -7.99100  -0.34800  -19.14600 1.000 44.55000 ? 121 SER B OG  1 
ATOM   3189 N N   . PRO B 1 120 ? -7.60400  1.77300   -15.42700 1.000 36.55000 ? 122 PRO B N   1 
ATOM   3190 C CA  . PRO B 1 120 ? -8.36700  1.66000   -14.17400 1.000 34.02000 ? 122 PRO B CA  1 
ATOM   3191 C C   . PRO B 1 120 ? -9.82700  1.33300   -14.43600 1.000 36.57000 ? 122 PRO B C   1 
ATOM   3192 O O   . PRO B 1 120 ? -10.47900 1.94000   -15.29100 1.000 36.48000 ? 122 PRO B O   1 
ATOM   3193 C CB  . PRO B 1 120 ? -8.21100  3.04600   -13.54100 1.000 34.65000 ? 122 PRO B CB  1 
ATOM   3194 C CG  . PRO B 1 120 ? -6.99800  3.64500   -14.17400 1.000 37.86000 ? 122 PRO B CG  1 
ATOM   3195 C CD  . PRO B 1 120 ? -6.76100  2.97400   -15.49300 1.000 33.69000 ? 122 PRO B CD  1 
ATOM   3196 N N   . SER B 1 121 ? -10.35000 0.37300   -13.67000 1.000 32.07000 ? 123 SER B N   1 
ATOM   3197 C CA  . SER B 1 121 ? -11.71300 -0.09700  -13.84700 1.000 34.88000 ? 123 SER B CA  1 
ATOM   3198 C C   . SER B 1 121 ? -12.63100 0.21500   -12.67300 1.000 34.36000 ? 123 SER B C   1 
ATOM   3199 O O   . SER B 1 121 ? -13.82600 0.43200   -12.88100 1.000 31.79000 ? 123 SER B O   1 
ATOM   3200 C CB  . SER B 1 121 ? -11.71600 -1.61200  -14.08500 1.000 37.46000 ? 123 SER B CB  1 
ATOM   3201 O OG  . SER B 1 121 ? -13.03300 -2.07400  -14.28200 1.000 44.05000 ? 123 SER B OG  1 
ATOM   3202 N N   . GLY B 1 122 ? -12.11000 0.23200   -11.45200 1.000 29.87000 ? 124 GLY B N   1 
ATOM   3203 C CA  . GLY B 1 122 ? -12.94200 0.44400   -10.28800 1.000 30.34000 ? 124 GLY B CA  1 
ATOM   3204 C C   . GLY B 1 122 ? -12.07000 0.59500   -9.06400  1.000 27.94000 ? 124 GLY B C   1 
ATOM   3205 O O   . GLY B 1 122 ? -10.89200 0.25600   -9.08500  1.000 29.69000 ? 124 GLY B O   1 
ATOM   3206 N N   . VAL B 1 123 ? -12.66100 1.14300   -8.01300  1.000 29.57000 ? 125 VAL B N   1 
ATOM   3207 C CA  . VAL B 1 123 ? -11.95100 1.34700   -6.75800  1.000 31.47000 ? 125 VAL B CA  1 
ATOM   3208 C C   . VAL B 1 123 ? -12.83300 0.86400   -5.61800  1.000 31.44000 ? 125 VAL B C   1 
ATOM   3209 O O   . VAL B 1 123 ? -14.05400 1.04200   -5.64300  1.000 31.66000 ? 125 VAL B O   1 
ATOM   3210 C CB  . VAL B 1 123 ? -11.51400 2.82300   -6.56500  1.000 29.29000 ? 125 VAL B CB  1 
ATOM   3211 C CG1 . VAL B 1 123 ? -12.71100 3.77900   -6.51600  1.000 30.95000 ? 125 VAL B CG1 1 
ATOM   3212 C CG2 . VAL B 1 123 ? -10.60700 2.96300   -5.32400  1.000 27.65000 ? 125 VAL B CG2 1 
ATOM   3213 N N   . TYR B 1 124 ? -12.20300 0.21900   -4.64700  1.000 29.16000 ? 126 TYR B N   1 
ATOM   3214 C CA  . TYR B 1 124 ? -12.93900 -0.32100  -3.49000  1.000 28.14000 ? 126 TYR B CA  1 
ATOM   3215 C C   . TYR B 1 124 ? -12.05100 -0.36600  -2.25100  1.000 30.32000 ? 126 TYR B C   1 
ATOM   3216 O O   . TYR B 1 124 ? -10.84800 -0.44500  -2.39200  1.000 32.86000 ? 126 TYR B O   1 
ATOM   3217 C CB  . TYR B 1 124 ? -13.55500 -1.68300  -3.79300  1.000 33.18000 ? 126 TYR B CB  1 
ATOM   3218 C CG  . TYR B 1 124 ? -12.63500 -2.77100  -4.27200  1.000 34.84000 ? 126 TYR B CG  1 
ATOM   3219 C CD1 . TYR B 1 124 ? -12.02500 -3.62700  -3.37600  1.000 37.31000 ? 126 TYR B CD1 1 
ATOM   3220 C CD2 . TYR B 1 124 ? -12.43000 -2.98700  -5.62100  1.000 36.02000 ? 126 TYR B CD2 1 
ATOM   3221 C CE1 . TYR B 1 124 ? -11.20700 -4.65300  -3.81000  1.000 41.94000 ? 126 TYR B CE1 1 
ATOM   3222 C CE2 . TYR B 1 124 ? -11.60800 -4.00400  -6.07300  1.000 37.20000 ? 126 TYR B CE2 1 
ATOM   3223 C CZ  . TYR B 1 124 ? -10.99600 -4.84200  -5.16200  1.000 39.92000 ? 126 TYR B CZ  1 
ATOM   3224 O OH  . TYR B 1 124 ? -10.18200 -5.84800  -5.58100  1.000 42.85000 ? 126 TYR B OH  1 
ATOM   3225 N N   . GLN B 1 125 ? -12.67800 -0.33900  -1.08700  1.000 28.64000 ? 127 GLN B N   1 
ATOM   3226 C CA  . GLN B 1 125 ? -11.94800 -0.39500  0.19900   1.000 35.07000 ? 127 GLN B CA  1 
ATOM   3227 C C   . GLN B 1 125 ? -11.79600 -1.85500  0.62400   1.000 34.32000 ? 127 GLN B C   1 
ATOM   3228 O O   . GLN B 1 125 ? -12.77100 -2.59300  0.53600   1.000 34.51000 ? 127 GLN B O   1 
ATOM   3229 C CB  . GLN B 1 125 ? -12.59200 0.51800   1.23500   1.000 33.28000 ? 127 GLN B CB  1 
ATOM   3230 C CG  . GLN B 1 125 ? -11.83500 0.61300   2.54500   1.000 34.66000 ? 127 GLN B CG  1 
ATOM   3231 C CD  . GLN B 1 125 ? -10.73800 1.64400   2.50000   1.000 33.48000 ? 127 GLN B CD  1 
ATOM   3232 O OE1 . GLN B 1 125 ? -10.33700 2.11100   1.44200   1.000 32.68000 ? 127 GLN B OE1 1 
ATOM   3233 N NE2 . GLN B 1 125 ? -10.24400 2.01000   3.66800   1.000 38.56000 ? 127 GLN B NE2 1 
ATOM   3234 N N   . CYS B 1 126 ? -10.60800 -2.21700  1.07500   1.000 30.71000 ? 128 CYS B N   1 
ATOM   3235 C CA  . CYS B 1 126 ? -10.28300 -3.61200  1.41300   1.000 36.74000 ? 128 CYS B CA  1 
ATOM   3236 C C   . CYS B 1 126 ? -9.56500  -3.64500  2.75300   1.000 33.19000 ? 128 CYS B C   1 
ATOM   3237 O O   . CYS B 1 126 ? -9.16300  -2.61100  3.23400   1.000 33.38000 ? 128 CYS B O   1 
ATOM   3238 C CB  . CYS B 1 126 ? -9.22600  -4.14800  0.44800   1.000 33.93000 ? 128 CYS B CB  1 
ATOM   3239 S SG  . CYS B 1 126 ? -9.83000  -5.27600  -0.81800  1.000 56.50000 ? 128 CYS B SG  1 
ATOM   3240 N N   . ALA B 1 127 ? -9.44700  -4.83000  3.31100   1.000 35.91000 ? 129 ALA B N   1 
ATOM   3241 C CA  . ALA B 1 127 ? -8.66300  -5.01200  4.52900   1.000 31.56000 ? 129 ALA B CA  1 
ATOM   3242 C C   . ALA B 1 127 ? -7.74100  -6.20900  4.37300   1.000 35.52000 ? 129 ALA B C   1 
ATOM   3243 O O   . ALA B 1 127 ? -8.08200  -7.13500  3.66000   1.000 31.69000 ? 129 ALA B O   1 
ATOM   3244 C CB  . ALA B 1 127 ? -9.56900  -5.20800  5.68500   1.000 37.43000 ? 129 ALA B CB  1 
ATOM   3245 N N   . MET B 1 128 ? -6.56900  -6.09800  4.93900   1.000 33.33000 ? 130 MET B N   1 
ATOM   3246 C CA  . MET B 1 128 ? -5.65200  -7.22800  5.03000   1.000 31.47000 ? 130 MET B CA  1 
ATOM   3247 C C   . MET B 1 128 ? -6.18900  -8.18700  6.09100   1.000 32.33000 ? 130 MET B C   1 
ATOM   3248 O O   . MET B 1 128 ? -6.27100  -7.82300  7.26700   1.000 34.30000 ? 130 MET B O   1 
ATOM   3249 C CB  . MET B 1 128 ? -4.25400  -6.71300  5.37000   1.000 30.89000 ? 130 MET B CB  1 
ATOM   3250 C CG  . MET B 1 128 ? -3.17200  -7.76600  5.64100   1.000 37.83000 ? 130 MET B CG  1 
ATOM   3251 S SD  . MET B 1 128 ? -2.58300  -8.57000  4.15300   1.000 39.58000 ? 130 MET B SD  1 
ATOM   3252 C CE  . MET B 1 128 ? -1.94900  -7.20000  3.22300   1.000 28.69000 ? 130 MET B CE  1 
ATOM   3253 N N   . ARG B 1 129 ? -6.58300  -9.40100  5.68700   1.000 29.07000 ? 131 ARG B N   1 
ATOM   3254 C CA  . ARG B 1 129 ? -7.13800  -10.35600 6.64300   1.000 31.46000 ? 131 ARG B CA  1 
ATOM   3255 C C   . ARG B 1 129 ? -6.04900  -10.83400 7.60800   1.000 34.12000 ? 131 ARG B C   1 
ATOM   3256 O O   . ARG B 1 129 ? -4.85300  -10.77700 7.29500   1.000 28.92000 ? 131 ARG B O   1 
ATOM   3257 C CB  . ARG B 1 129 ? -7.74200  -11.57300 5.93600   1.000 31.87000 ? 131 ARG B CB  1 
ATOM   3258 C CG  . ARG B 1 129 ? -8.79300  -11.28700 4.86800   1.000 36.82000 ? 131 ARG B CG  1 
ATOM   3259 C CD  . ARG B 1 129 ? -9.98300  -10.52400 5.41400   1.000 30.46000 ? 131 ARG B CD  1 
ATOM   3260 N NE  . ARG B 1 129 ? -10.47100 -11.07900 6.68200   1.000 29.88000 ? 131 ARG B NE  1 
ATOM   3261 C CZ  . ARG B 1 129 ? -11.37400 -10.47500 7.45200   1.000 32.06000 ? 131 ARG B CZ  1 
ATOM   3262 N NH1 . ARG B 1 129 ? -11.88000 -9.29700  7.07700   1.000 26.73000 ? 131 ARG B NH1 1 
ATOM   3263 N NH2 . ARG B 1 129 ? -11.75700 -11.03100 8.59700   1.000 27.43000 ? 131 ARG B NH2 1 
ATOM   3264 N N   . PRO B 1 130 ? -6.43900  -11.32000 8.79100   1.000 35.71000 ? 132 PRO B N   1 
ATOM   3265 C CA  . PRO B 1 130 ? -5.44100  -11.91800 9.69700   1.000 32.51000 ? 132 PRO B CA  1 
ATOM   3266 C C   . PRO B 1 130 ? -4.62800  -13.02600 9.05900   1.000 32.54000 ? 132 PRO B C   1 
ATOM   3267 O O   . PRO B 1 130 ? -3.48100  -13.24000 9.46000   1.000 32.80000 ? 132 PRO B O   1 
ATOM   3268 C CB  . PRO B 1 130 ? -6.29300  -12.44600 10.85600  1.000 35.84000 ? 132 PRO B CB  1 
ATOM   3269 C CG  . PRO B 1 130 ? -7.49200  -11.53800 10.87300  1.000 36.31000 ? 132 PRO B CG  1 
ATOM   3270 C CD  . PRO B 1 130 ? -7.76800  -11.20900 9.42200   1.000 35.03000 ? 132 PRO B CD  1 
ATOM   3271 N N   . ASN B 1 131 ? -5.17600  -13.73300 8.07600   1.000 29.76000 ? 133 ASN B N   1 
ATOM   3272 C CA  . ASN B 1 131 ? -4.44300  -14.79300 7.40100   1.000 33.57000 ? 133 ASN B CA  1 
ATOM   3273 C C   . ASN B 1 131 ? -3.70500  -14.28000 6.17700   1.000 30.93000 ? 133 ASN B C   1 
ATOM   3274 O O   . ASN B 1 131 ? -3.32300  -15.07500 5.30500   1.000 29.96000 ? 133 ASN B O   1 
ATOM   3275 C CB  . ASN B 1 131 ? -5.37900  -15.95000 7.03300   1.000 31.16000 ? 133 ASN B CB  1 
ATOM   3276 C CG  . ASN B 1 131 ? -6.40300  -15.58500 5.97300   1.000 34.77000 ? 133 ASN B CG  1 
ATOM   3277 O OD1 . ASN B 1 131 ? -6.45400  -14.45600 5.50300   1.000 33.17000 ? 133 ASN B OD1 1 
ATOM   3278 N ND2 . ASN B 1 131 ? -7.25400  -16.55000 5.61000   1.000 35.89000 ? 133 ASN B ND2 1 
ATOM   3279 N N   . PHE B 1 132 ? -3.53300  -12.96600 6.08800   1.000 30.06000 ? 134 PHE B N   1 
ATOM   3280 C CA  . PHE B 1 132 ? -2.76500  -12.24100 5.07800   1.000 31.10000 ? 134 PHE B CA  1 
ATOM   3281 C C   . PHE B 1 132 ? -3.36100  -12.30700 3.68100   1.000 31.08000 ? 134 PHE B C   1 
ATOM   3282 O O   . PHE B 1 132 ? -2.67300  -11.96900 2.70800   1.000 32.59000 ? 134 PHE B O   1 
ATOM   3283 C CB  . PHE B 1 132 ? -1.31600  -12.72500 5.02700   1.000 28.56000 ? 134 PHE B CB  1 
ATOM   3284 C CG  . PHE B 1 132 ? -0.50500  -12.29800 6.20600   1.000 28.76000 ? 134 PHE B CG  1 
ATOM   3285 C CD1 . PHE B 1 132 ? -0.12000  -10.97400 6.34100   1.000 32.91000 ? 134 PHE B CD1 1 
ATOM   3286 C CD2 . PHE B 1 132 ? -0.16700  -13.19900 7.19800   1.000 30.64000 ? 134 PHE B CD2 1 
ATOM   3287 C CE1 . PHE B 1 132 ? 0.62000   -10.56400 7.42800   1.000 33.26000 ? 134 PHE B CE1 1 
ATOM   3288 C CE2 . PHE B 1 132 ? 0.56900   -12.79300 8.29100   1.000 28.87000 ? 134 PHE B CE2 1 
ATOM   3289 C CZ  . PHE B 1 132 ? 0.96000   -11.46900 8.40300   1.000 34.37000 ? 134 PHE B CZ  1 
ATOM   3290 N N   . THR B 1 133 ? -4.60500  -12.73700 3.54000   1.000 31.17000 ? 135 THR B N   1 
ATOM   3291 C CA  . THR B 1 133 ? -5.24300  -12.67900 2.23600   1.000 30.42000 ? 135 THR B CA  1 
ATOM   3292 C C   . THR B 1 133 ? -6.07100  -11.40500 2.12700   1.000 33.23000 ? 135 THR B C   1 
ATOM   3293 O O   . THR B 1 133 ? -6.31400  -10.71300 3.11700   1.000 33.27000 ? 135 THR B O   1 
ATOM   3294 C CB  . THR B 1 133 ? -6.10800  -13.91900 1.98900   1.000 33.37000 ? 135 THR B CB  1 
ATOM   3295 O OG1 . THR B 1 133 ? -7.20000  -13.95200 2.91700   1.000 30.53000 ? 135 THR B OG1 1 
ATOM   3296 C CG2 . THR B 1 133 ? -5.27100  -15.17300 2.16100   1.000 32.10000 ? 135 THR B CG2 1 
ATOM   3297 N N   . ILE B 1 134 ? -6.46400  -11.08400 0.89500   1.000 29.82000 ? 136 ILE B N   1 
ATOM   3298 C CA  . ILE B 1 134 ? -7.36600  -9.98100  0.59500   1.000 32.69000 ? 136 ILE B CA  1 
ATOM   3299 C C   . ILE B 1 134 ? -8.63700  -10.58500 0.02400   1.000 34.34000 ? 136 ILE B C   1 
ATOM   3300 O O   . ILE B 1 134 ? -8.57800  -11.38400 -0.91700  1.000 35.47000 ? 136 ILE B O   1 
ATOM   3301 C CB  . ILE B 1 134 ? -6.74700  -8.99100  -0.41000  1.000 31.75000 ? 136 ILE B CB  1 
ATOM   3302 C CG1 . ILE B 1 134 ? -5.42500  -8.42400  0.10900   1.000 33.43000 ? 136 ILE B CG1 1 
ATOM   3303 C CG2 . ILE B 1 134 ? -7.70300  -7.87000  -0.68700  1.000 38.00000 ? 136 ILE B CG2 1 
ATOM   3304 C CD1 . ILE B 1 134 ? -5.51900  -7.87900  1.50400   1.000 33.90000 ? 136 ILE B CD1 1 
ATOM   3305 N N   . LYS B 1 135 ? -9.78400  -10.22600 0.59100   1.000 36.44000 ? 137 LYS B N   1 
ATOM   3306 C CA  . LYS B 1 135 ? -11.05700 -10.61100 -0.00700  1.000 35.62000 ? 137 LYS B CA  1 
ATOM   3307 C C   . LYS B 1 135 ? -11.37800 -9.53000  -1.03100  1.000 40.47000 ? 137 LYS B C   1 
ATOM   3308 O O   . LYS B 1 135 ? -12.15700 -8.60700  -0.80100  1.000 43.47000 ? 137 LYS B O   1 
ATOM   3309 C CB  . LYS B 1 135 ? -12.14200 -10.76900 1.05300   1.000 41.51000 ? 137 LYS B CB  1 
ATOM   3310 N N   . GLY B 1 136 ? -10.71300 -9.62500  -2.18000  1.000 39.96000 ? 138 GLY B N   1 
ATOM   3311 C CA  . GLY B 1 136 ? -10.82700 -8.61900  -3.20800  1.000 43.59000 ? 138 GLY B CA  1 
ATOM   3312 C C   . GLY B 1 136 ? -11.82600 -9.01700  -4.28000  1.000 42.96000 ? 138 GLY B C   1 
ATOM   3313 O O   . GLY B 1 136 ? -12.39900 -10.10500 -4.27800  1.000 44.23000 ? 138 GLY B O   1 
ATOM   3314 N N   . SER B 1 137 ? -12.03800 -8.09100  -5.20500  1.000 39.74000 ? 139 SER B N   1 
ATOM   3315 C CA  . SER B 1 137 ? -12.79400 -8.36700  -6.42400  1.000 44.33000 ? 139 SER B CA  1 
ATOM   3316 C C   . SER B 1 137 ? -11.80300 -8.13800  -7.55400  1.000 45.44000 ? 139 SER B C   1 
ATOM   3317 O O   . SER B 1 137 ? -11.53500 -6.99100  -7.94900  1.000 43.15000 ? 139 SER B O   1 
ATOM   3318 C CB  . SER B 1 137 ? -14.04000 -7.49100  -6.54700  1.000 48.96000 ? 139 SER B CB  1 
ATOM   3319 O OG  . SER B 1 137 ? -14.87200 -7.94100  -7.60600  1.000 45.26000 ? 139 SER B OG  1 
ATOM   3320 N N   . PHE B 1 138 ? -11.22000 -9.24400  -8.00400  1.000 38.90000 ? 140 PHE B N   1 
ATOM   3321 C CA  . PHE B 1 138 ? -10.12300 -9.27600  -8.95300  1.000 38.08000 ? 140 PHE B CA  1 
ATOM   3322 C C   . PHE B 1 138 ? -10.43800 -10.37800 -9.94700  1.000 41.45000 ? 140 PHE B C   1 
ATOM   3323 O O   . PHE B 1 138 ? -10.72600 -11.51300 -9.54600  1.000 40.11000 ? 140 PHE B O   1 
ATOM   3324 C CB  . PHE B 1 138 ? -8.77700  -9.57200  -8.25700  1.000 36.39000 ? 140 PHE B CB  1 
ATOM   3325 C CG  . PHE B 1 138 ? -8.13700  -8.38100  -7.59100  1.000 36.12000 ? 140 PHE B CG  1 
ATOM   3326 C CD1 . PHE B 1 138 ? -8.07700  -7.14800  -8.22500  1.000 38.53000 ? 140 PHE B CD1 1 
ATOM   3327 C CD2 . PHE B 1 138 ? -7.57700  -8.50500  -6.33100  1.000 35.81000 ? 140 PHE B CD2 1 
ATOM   3328 C CE1 . PHE B 1 138 ? -7.47500  -6.06300  -7.61300  1.000 34.71000 ? 140 PHE B CE1 1 
ATOM   3329 C CE2 . PHE B 1 138 ? -6.95600  -7.43400  -5.71200  1.000 34.57000 ? 140 PHE B CE2 1 
ATOM   3330 C CZ  . PHE B 1 138 ? -6.90200  -6.20700  -6.35500  1.000 33.33000 ? 140 PHE B CZ  1 
ATOM   3331 N N   . LEU B 1 139 ? -10.36400 -10.05200 -11.21100 1.000 39.27000 ? 141 LEU B N   1 
ATOM   3332 C CA  . LEU B 1 139 ? -10.60300 -11.08100 -12.22000 1.000 40.06000 ? 141 LEU B CA  1 
ATOM   3333 C C   . LEU B 1 139 ? -9.26500  -11.40800 -12.88700 1.000 39.70000 ? 141 LEU B C   1 
ATOM   3334 O O   . LEU B 1 139 ? -8.25200  -10.88200 -12.47700 1.000 36.79000 ? 141 LEU B O   1 
ATOM   3335 C CB  . LEU B 1 139 ? -11.65400 -10.54200 -13.19000 1.000 39.47000 ? 141 LEU B CB  1 
ATOM   3336 C CG  . LEU B 1 139 ? -13.00500 -10.20100 -12.56800 1.000 44.09000 ? 141 LEU B CG  1 
ATOM   3337 C CD1 . LEU B 1 139 ? -13.94400 -9.61900  -13.60800 1.000 44.24000 ? 141 LEU B CD1 1 
ATOM   3338 C CD2 . LEU B 1 139 ? -13.62500 -11.42500 -11.91400 1.000 43.83000 ? 141 LEU B CD2 1 
ATOM   3339 N N   . ASN B 1 140 ? -9.29300  -12.23600 -13.90600 1.000 38.44000 ? 142 ASN B N   1 
ATOM   3340 C CA  . ASN B 1 140 ? -8.04500  -12.53900 -14.62700 1.000 38.38000 ? 142 ASN B CA  1 
ATOM   3341 C C   . ASN B 1 140 ? -7.45800  -11.24800 -15.19900 1.000 36.15000 ? 142 ASN B C   1 
ATOM   3342 O O   . ASN B 1 140 ? -8.22200  -10.39800 -15.63500 1.000 36.38000 ? 142 ASN B O   1 
ATOM   3343 C CB  . ASN B 1 140 ? -8.23100  -13.63800 -15.67000 1.000 30.00000 ? 142 ASN B CB  1 
ATOM   3344 C CG  . ASN B 1 140 ? -8.79600  -14.92100 -15.10300 1.000 30.00000 ? 142 ASN B CG  1 
ATOM   3345 O OD1 . ASN B 1 140 ? -8.07100  -15.72100 -14.52200 1.000 30.00000 ? 142 ASN B OD1 1 
ATOM   3346 N ND2 . ASN B 1 140 ? -10.08800 -15.13600 -15.28100 1.000 30.00000 ? 142 ASN B ND2 1 
ATOM   3347 N N   . GLY B 1 141 ? -6.13900  -11.11900 -15.15700 1.000 37.49000 ? 143 GLY B N   1 
ATOM   3348 C CA  . GLY B 1 141 ? -5.45600  -9.93400  -15.69400 1.000 34.66000 ? 143 GLY B CA  1 
ATOM   3349 C C   . GLY B 1 141 ? -5.46600  -8.75600  -14.74300 1.000 36.35000 ? 143 GLY B C   1 
ATOM   3350 O O   . GLY B 1 141 ? -4.96500  -7.71900  -15.13900 1.000 33.94000 ? 143 GLY B O   1 
ATOM   3351 N N   . SER B 1 142 ? -6.00600  -8.94000  -13.53400 1.000 36.93000 ? 144 SER B N   1 
ATOM   3352 C CA  . SER B 1 142 ? -5.96600  -7.86700  -12.54300 1.000 32.61000 ? 144 SER B CA  1 
ATOM   3353 C C   . SER B 1 142 ? -4.60300  -7.71900  -11.88400 1.000 32.86000 ? 144 SER B C   1 
ATOM   3354 O O   . SER B 1 142 ? -4.36800  -6.69800  -11.22100 1.000 31.83000 ? 144 SER B O   1 
ATOM   3355 C CB  . SER B 1 142 ? -7.01300  -8.11800  -11.45500 1.000 33.63000 ? 144 SER B CB  1 
ATOM   3356 O OG  . SER B 1 142 ? -6.87900  -9.43200  -10.92800 1.000 34.67000 ? 144 SER B OG  1 
ATOM   3357 N N   . CYS B 1 143 ? -3.72100  -8.71300  -12.03500 1.000 29.27000 ? 145 CYS B N   1 
ATOM   3358 C CA  . CYS B 1 143 ? -2.37200  -8.65500  -11.48000 1.000 28.26000 ? 145 CYS B CA  1 
ATOM   3359 C C   . CYS B 1 143 ? -1.70000  -7.33600  -11.81300 1.000 27.15000 ? 145 CYS B C   1 
ATOM   3360 O O   . CYS B 1 143 ? -1.82800  -6.81700  -12.92400 1.000 29.57000 ? 145 CYS B O   1 
ATOM   3361 C CB  . CYS B 1 143 ? -1.52000  -9.80400  -12.02900 1.000 28.66000 ? 145 CYS B CB  1 
ATOM   3362 S SG  . CYS B 1 143 ? -2.38300  -11.33900 -12.18200 1.000 36.62000 ? 145 CYS B SG  1 
ATOM   3363 N N   . GLY B 1 144 ? -0.95300  -6.80900  -10.85100 1.000 26.56000 ? 146 GLY B N   1 
ATOM   3364 C CA  . GLY B 1 144 ? -0.35700  -5.50500  -10.98000 1.000 29.59000 ? 146 GLY B CA  1 
ATOM   3365 C C   . GLY B 1 144 ? -1.19600  -4.35500  -10.44300 1.000 30.73000 ? 146 GLY B C   1 
ATOM   3366 O O   . GLY B 1 144 ? -0.65300  -3.25800  -10.25100 1.000 28.15000 ? 146 GLY B O   1 
ATOM   3367 N N   . SER B 1 145 ? -2.50100  -4.56400  -10.22600 1.000 28.41000 ? 147 SER B N   1 
ATOM   3368 C CA  . SER B 1 145 ? -3.32600  -3.59100  -9.50800  1.000 27.64000 ? 147 SER B CA  1 
ATOM   3369 C C   . SER B 1 145 ? -2.74700  -3.36200  -8.12100  1.000 29.32000 ? 147 SER B C   1 
ATOM   3370 O O   . SER B 1 145 ? -2.19900  -4.27500  -7.50200  1.000 27.34000 ? 147 SER B O   1 
ATOM   3371 C CB  . SER B 1 145 ? -4.77600  -4.08600  -9.37200  1.000 28.58000 ? 147 SER B CB  1 
ATOM   3372 O OG  . SER B 1 145 ? -5.45300  -4.13000  -10.61800 1.000 31.17000 ? 147 SER B OG  1 
ATOM   3373 N N   . VAL B 1 146 ? -2.89200  -2.14400  -7.60300  1.000 25.54000 ? 148 VAL B N   1 
ATOM   3374 C CA  . VAL B 1 146 ? -2.27500  -1.84700  -6.32100  1.000 26.19000 ? 148 VAL B CA  1 
ATOM   3375 C C   . VAL B 1 146 ? -3.31800  -1.40900  -5.29900  1.000 26.85000 ? 148 VAL B C   1 
ATOM   3376 O O   . VAL B 1 146 ? -4.41500  -0.95600  -5.63500  1.000 26.65000 ? 148 VAL B O   1 
ATOM   3377 C CB  . VAL B 1 146 ? -1.15400  -0.79300  -6.43600  1.000 28.26000 ? 148 VAL B CB  1 
ATOM   3378 C CG1 . VAL B 1 146 ? 0.04300   -1.38700  -7.21600  1.000 29.36000 ? 148 VAL B CG1 1 
ATOM   3379 C CG2 . VAL B 1 146 ? -1.66600  0.51200   -7.06300  1.000 26.59000 ? 148 VAL B CG2 1 
ATOM   3380 N N   . GLY B 1 147 ? -2.95100  -1.59400  -4.03000  1.000 24.84000 ? 149 GLY B N   1 
ATOM   3381 C CA  . GLY B 1 147 ? -3.65800  -1.02400  -2.89900  1.000 24.73000 ? 149 GLY B CA  1 
ATOM   3382 C C   . GLY B 1 147 ? -2.86200  0.11900   -2.29000  1.000 28.76000 ? 149 GLY B C   1 
ATOM   3383 O O   . GLY B 1 147 ? -1.62700  0.16200   -2.38400  1.000 25.63000 ? 149 GLY B O   1 
ATOM   3384 N N   . PHE B 1 148 ? -3.57000  1.05800   -1.66600  1.000 26.39000 ? 150 PHE B N   1 
ATOM   3385 C CA  . PHE B 1 148 ? -2.92100  2.28800   -1.23500  1.000 28.25000 ? 150 PHE B CA  1 
ATOM   3386 C C   . PHE B 1 148 ? -3.77200  2.97900   -0.18000  1.000 27.87000 ? 150 PHE B C   1 
ATOM   3387 O O   . PHE B 1 148 ? -4.97400  2.72300   -0.04900  1.000 26.23000 ? 150 PHE B O   1 
ATOM   3388 C CB  . PHE B 1 148 ? -2.67700  3.24900   -2.41700  1.000 27.09000 ? 150 PHE B CB  1 
ATOM   3389 C CG  . PHE B 1 148 ? -3.93300  3.68600   -3.09700  1.000 26.80000 ? 150 PHE B CG  1 
ATOM   3390 C CD1 . PHE B 1 148 ? -4.56800  2.85600   -4.00600  1.000 26.77000 ? 150 PHE B CD1 1 
ATOM   3391 C CD2 . PHE B 1 148 ? -4.49400  4.91800   -2.82300  1.000 27.34000 ? 150 PHE B CD2 1 
ATOM   3392 C CE1 . PHE B 1 148 ? -5.74300  3.24700   -4.63100  1.000 27.98000 ? 150 PHE B CE1 1 
ATOM   3393 C CE2 . PHE B 1 148 ? -5.67500  5.30900   -3.44800  1.000 27.64000 ? 150 PHE B CE2 1 
ATOM   3394 C CZ  . PHE B 1 148 ? -6.28900  4.48000   -4.35000  1.000 27.82000 ? 150 PHE B CZ  1 
ATOM   3395 N N   . ASN B 1 149 ? -3.11000  3.85900   0.57700   1.000 25.12000 ? 151 ASN B N   1 
ATOM   3396 C CA  . ASN B 1 149 ? -3.74700  4.83100   1.45200   1.000 27.98000 ? 151 ASN B CA  1 
ATOM   3397 C C   . ASN B 1 149 ? -3.21600  6.19800   1.04000   1.000 29.84000 ? 151 ASN B C   1 
ATOM   3398 O O   . ASN B 1 149 ? -2.11300  6.31000   0.49400   1.000 28.64000 ? 151 ASN B O   1 
ATOM   3399 C CB  . ASN B 1 149 ? -3.44600  4.56700   2.94500   1.000 26.83000 ? 151 ASN B CB  1 
ATOM   3400 C CG  . ASN B 1 149 ? -4.26900  3.41500   3.52900   1.000 32.95000 ? 151 ASN B CG  1 
ATOM   3401 O OD1 . ASN B 1 149 ? -5.38600  3.61600   4.02200   1.000 29.94000 ? 151 ASN B OD1 1 
ATOM   3402 N ND2 . ASN B 1 149 ? -3.71100  2.20300   3.48300   1.000 27.43000 ? 151 ASN B ND2 1 
ATOM   3403 N N   . ILE B 1 150 ? -4.00500  7.23900   1.26600   1.000 31.44000 ? 152 ILE B N   1 
ATOM   3404 C CA  . ILE B 1 150 ? -3.53900  8.60100   1.03700   1.000 33.44000 ? 152 ILE B CA  1 
ATOM   3405 C C   . ILE B 1 150 ? -3.52200  9.33300   2.37200   1.000 40.59000 ? 152 ILE B C   1 
ATOM   3406 O O   . ILE B 1 150 ? -4.46000  9.22500   3.16800   1.000 40.54000 ? 152 ILE B O   1 
ATOM   3407 C CB  . ILE B 1 150 ? -4.40100  9.35700   0.00900   1.000 35.18000 ? 152 ILE B CB  1 
ATOM   3408 C CG1 . ILE B 1 150 ? -4.41700  8.64000   -1.33700  1.000 30.80000 ? 152 ILE B CG1 1 
ATOM   3409 C CG2 . ILE B 1 150 ? -3.88900  10.80300  -0.16200  1.000 36.66000 ? 152 ILE B CG2 1 
ATOM   3410 C CD1 . ILE B 1 150 ? -5.31800  9.34100   -2.34500  1.000 35.18000 ? 152 ILE B CD1 1 
ATOM   3411 N N   . ASP B 1 151 ? -2.44200  10.05700  2.62500   1.000 41.79000 ? 153 ASP B N   1 
ATOM   3412 C CA  . ASP B 1 151 ? -2.31200  10.87700  3.82600   1.000 43.89000 ? 153 ASP B CA  1 
ATOM   3413 C C   . ASP B 1 151 ? -1.94600  12.28400  3.35900   1.000 44.56000 ? 153 ASP B C   1 
ATOM   3414 O O   . ASP B 1 151 ? -0.78400  12.55000  3.04900   1.000 45.79000 ? 153 ASP B O   1 
ATOM   3415 C CB  . ASP B 1 151 ? -1.27300  10.28100  4.77200   1.000 47.39000 ? 153 ASP B CB  1 
ATOM   3416 C CG  . ASP B 1 151 ? -1.65000  8.87400   5.23700   1.000 53.62000 ? 153 ASP B CG  1 
ATOM   3417 O OD1 . ASP B 1 151 ? -2.66200  8.76100   5.96400   1.000 60.16000 ? 153 ASP B OD1 1 
ATOM   3418 O OD2 . ASP B 1 151 ? -0.97600  7.87300   4.85500   1.000 53.36000 ? 153 ASP B OD2 1 
ATOM   3419 N N   . TYR B 1 152 ? -2.95700  13.16000  3.26200   1.000 44.78000 ? 154 TYR B N   1 
ATOM   3420 C CA  . TYR B 1 152 ? -2.82600  14.56200  2.87100   1.000 44.83000 ? 154 TYR B CA  1 
ATOM   3421 C C   . TYR B 1 152 ? -1.75100  14.78800  1.81900   1.000 50.91000 ? 154 TYR B C   1 
ATOM   3422 O O   . TYR B 1 152 ? -0.67300  15.29300  2.14400   1.000 54.45000 ? 154 TYR B O   1 
ATOM   3423 C CB  . TYR B 1 152 ? -2.52900  15.44100  4.08900   1.000 52.16000 ? 154 TYR B CB  1 
ATOM   3424 N N   . ASP B 1 153 ? -2.03700  14.38000  0.58100   1.000 49.17000 ? 155 ASP B N   1 
ATOM   3425 C CA  . ASP B 1 153 ? -1.27900  14.53000  -0.67100  1.000 44.23000 ? 155 ASP B CA  1 
ATOM   3426 C C   . ASP B 1 153 ? -0.21000  13.44600  -0.89400  1.000 41.04000 ? 155 ASP B C   1 
ATOM   3427 O O   . ASP B 1 153 ? 0.40400   13.43100  -1.98600  1.000 38.08000 ? 155 ASP B O   1 
ATOM   3428 C CB  . ASP B 1 153 ? -0.66300  15.94100  -0.82300  1.000 44.95000 ? 155 ASP B CB  1 
ATOM   3429 C CG  . ASP B 1 153 ? 0.65800   16.14400  -0.06500  1.000 50.03000 ? 155 ASP B CG  1 
ATOM   3430 O OD1 . ASP B 1 153 ? 0.90300   15.52900  0.99300   1.000 50.15000 ? 155 ASP B OD1 1 
ATOM   3431 O OD2 . ASP B 1 153 ? 1.48000   16.94400  -0.56400  1.000 51.54000 ? 155 ASP B OD2 1 
ATOM   3432 N N   . CYS B 1 154 ? 0.04500   12.54400  0.05500   1.000 41.79000 ? 156 CYS B N   1 
ATOM   3433 C CA  . CYS B 1 154 ? 1.04600   11.49800  -0.14400  1.000 34.58000 ? 156 CYS B CA  1 
ATOM   3434 C C   . CYS B 1 154 ? 0.37500   10.13200  -0.24100  1.000 33.06000 ? 156 CYS B C   1 
ATOM   3435 O O   . CYS B 1 154 ? -0.31100  9.71200   0.69400   1.000 33.16000 ? 156 CYS B O   1 
ATOM   3436 C CB  . CYS B 1 154 ? 2.07600   11.49700  0.98100   1.000 35.40000 ? 156 CYS B CB  1 
ATOM   3437 S SG  . CYS B 1 154 ? 3.35000   10.19300  0.78800   1.000 37.76000 ? 156 CYS B SG  1 
ATOM   3438 N N   . VAL B 1 155 ? 0.62100   9.43100   -1.34900  1.000 30.87000 ? 157 VAL B N   1 
ATOM   3439 C CA  . VAL B 1 155 ? 0.07800   8.09500   -1.60000  1.000 30.20000 ? 157 VAL B CA  1 
ATOM   3440 C C   . VAL B 1 155 ? 1.01300   7.05500   -0.99400  1.000 27.00000 ? 157 VAL B C   1 
ATOM   3441 O O   . VAL B 1 155 ? 2.17800   6.95400   -1.39200  1.000 31.75000 ? 157 VAL B O   1 
ATOM   3442 C CB  . VAL B 1 155 ? -0.09700  7.83800   -3.10400  1.000 30.13000 ? 157 VAL B CB  1 
ATOM   3443 C CG1 . VAL B 1 155 ? -0.65000  6.38400   -3.35900  1.000 30.41000 ? 157 VAL B CG1 1 
ATOM   3444 C CG2 . VAL B 1 155 ? -1.00800  8.88100   -3.71500  1.000 29.63000 ? 157 VAL B CG2 1 
ATOM   3445 N N   . SER B 1 156 ? 0.51200   6.26300   -0.05500  1.000 25.96000 ? 158 SER B N   1 
ATOM   3446 C CA  . SER B 1 156 ? 1.31100   5.19700   0.55300   1.000 28.76000 ? 158 SER B CA  1 
ATOM   3447 C C   . SER B 1 156 ? 0.86700   3.87000   -0.06500  1.000 27.07000 ? 158 SER B C   1 
ATOM   3448 O O   . SER B 1 156 ? -0.17200  3.32000   0.30400   1.000 27.69000 ? 158 SER B O   1 
ATOM   3449 C CB  . SER B 1 156 ? 1.16300   5.20600   2.07400   1.000 27.50000 ? 158 SER B CB  1 
ATOM   3450 O OG  . SER B 1 156 ? 1.90900   6.28400   2.65200   1.000 30.45000 ? 158 SER B OG  1 
ATOM   3451 N N   . PHE B 1 157 ? 1.65000   3.37100   -1.02800  1.000 26.58000 ? 159 PHE B N   1 
ATOM   3452 C CA  . PHE B 1 157 ? 1.35200   2.09600   -1.67800  1.000 29.12000 ? 159 PHE B CA  1 
ATOM   3453 C C   . PHE B 1 157 ? 1.70200   0.93400   -0.75500  1.000 24.50000 ? 159 PHE B C   1 
ATOM   3454 O O   . PHE B 1 157 ? 2.82800   0.84500   -0.26500  1.000 23.55000 ? 159 PHE B O   1 
ATOM   3455 C CB  . PHE B 1 157 ? 2.14900   1.95100   -2.97500  1.000 24.69000 ? 159 PHE B CB  1 
ATOM   3456 C CG  . PHE B 1 157 ? 1.79900   2.95900   -4.03200  1.000 26.71000 ? 159 PHE B CG  1 
ATOM   3457 C CD1 . PHE B 1 157 ? 0.66200   2.80200   -4.80300  1.000 27.41000 ? 159 PHE B CD1 1 
ATOM   3458 C CD2 . PHE B 1 157 ? 2.63500   4.03900   -4.28300  1.000 28.70000 ? 159 PHE B CD2 1 
ATOM   3459 C CE1 . PHE B 1 157 ? 0.35600   3.70200   -5.78700  1.000 26.16000 ? 159 PHE B CE1 1 
ATOM   3460 C CE2 . PHE B 1 157 ? 2.34000   4.95400   -5.27000  1.000 28.70000 ? 159 PHE B CE2 1 
ATOM   3461 C CZ  . PHE B 1 157 ? 1.20000   4.79500   -6.01900  1.000 29.27000 ? 159 PHE B CZ  1 
ATOM   3462 N N   . CYS B 1 158 ? 0.75000   0.02800   -0.53600  1.000 25.78000 ? 160 CYS B N   1 
ATOM   3463 C CA  . CYS B 1 158 ? 0.97300   -1.08100  0.38200   1.000 25.56000 ? 160 CYS B CA  1 
ATOM   3464 C C   . CYS B 1 158 ? 0.78400   -2.45400  -0.22400  1.000 25.94000 ? 160 CYS B C   1 
ATOM   3465 O O   . CYS B 1 158 ? 1.16600   -3.44000  0.41700   1.000 27.58000 ? 160 CYS B O   1 
ATOM   3466 C CB  . CYS B 1 158 ? 0.04600   -0.98200  1.60600   1.000 23.22000 ? 160 CYS B CB  1 
ATOM   3467 S SG  . CYS B 1 158 ? -1.71700  -0.88500  1.19300   1.000 28.44000 ? 160 CYS B SG  1 
ATOM   3468 N N   . TYR B 1 159 ? 0.20100   -2.56100  -1.41500  1.000 24.03000 ? 161 TYR B N   1 
ATOM   3469 C CA  . TYR B 1 159 ? -0.17800  -3.85800  -1.94700  1.000 22.17000 ? 161 TYR B CA  1 
ATOM   3470 C C   . TYR B 1 159 ? -0.06900  -3.83400  -3.46200  1.000 24.52000 ? 161 TYR B C   1 
ATOM   3471 O O   . TYR B 1 159 ? -0.46800  -2.86400  -4.10200  1.000 24.05000 ? 161 TYR B O   1 
ATOM   3472 C CB  . TYR B 1 159 ? -1.61800  -4.21700  -1.53500  1.000 25.27000 ? 161 TYR B CB  1 
ATOM   3473 C CG  . TYR B 1 159 ? -2.11800  -5.55300  -2.04300  1.000 26.46000 ? 161 TYR B CG  1 
ATOM   3474 C CD1 . TYR B 1 159 ? -1.73600  -6.73400  -1.41400  1.000 26.44000 ? 161 TYR B CD1 1 
ATOM   3475 C CD2 . TYR B 1 159 ? -2.99300  -5.63900  -3.12200  1.000 26.26000 ? 161 TYR B CD2 1 
ATOM   3476 C CE1 . TYR B 1 159 ? -2.19000  -7.96900  -1.85900  1.000 26.86000 ? 161 TYR B CE1 1 
ATOM   3477 C CE2 . TYR B 1 159 ? -3.47500  -6.88800  -3.57300  1.000 23.92000 ? 161 TYR B CE2 1 
ATOM   3478 C CZ  . TYR B 1 159 ? -3.06200  -8.04500  -2.92800  1.000 26.26000 ? 161 TYR B CZ  1 
ATOM   3479 O OH  . TYR B 1 159 ? -3.49700  -9.28800  -3.34800  1.000 25.89000 ? 161 TYR B OH  1 
ATOM   3480 N N   . MET B 1 160 ? 0.45800   -4.90800  -4.03300  1.000 25.52000 ? 162 MET B N   1 
ATOM   3481 C CA  . MET B 1 160 ? 0.36400   -5.13700  -5.46700  1.000 24.40000 ? 162 MET B CA  1 
ATOM   3482 C C   . MET B 1 160 ? -0.20100  -6.52700  -5.66400  1.000 27.38000 ? 162 MET B C   1 
ATOM   3483 O O   . MET B 1 160 ? 0.27500   -7.47800  -5.04300  1.000 26.18000 ? 162 MET B O   1 
ATOM   3484 C CB  . MET B 1 160 ? 1.72000   -5.04000  -6.16800  1.000 28.00000 ? 162 MET B CB  1 
ATOM   3485 C CG  . MET B 1 160 ? 1.64000   -5.57500  -7.57700  1.000 29.41000 ? 162 MET B CG  1 
ATOM   3486 S SD  . MET B 1 160 ? 3.12400   -5.33800  -8.54500  1.000 37.02000 ? 162 MET B SD  1 
ATOM   3487 C CE  . MET B 1 160 ? 2.95000   -3.58800  -8.98500  1.000 35.58000 ? 162 MET B CE  1 
ATOM   3488 N N   . HIS B 1 161 ? -1.22100  -6.64300  -6.51000  1.000 28.32000 ? 163 HIS B N   1 
ATOM   3489 C CA  . HIS B 1 161 ? -1.92300  -7.90200  -6.65500  1.000 28.01000 ? 163 HIS B CA  1 
ATOM   3490 C C   . HIS B 1 161 ? -1.12200  -8.90700  -7.48200  1.000 25.46000 ? 163 HIS B C   1 
ATOM   3491 O O   . HIS B 1 161 ? -0.64500  -8.57700  -8.57000  1.000 26.85000 ? 163 HIS B O   1 
ATOM   3492 C CB  . HIS B 1 161 ? -3.27700  -7.67600  -7.30700  1.000 25.90000 ? 163 HIS B CB  1 
ATOM   3493 C CG  . HIS B 1 161 ? -4.07100  -8.92900  -7.38900  1.000 26.71000 ? 163 HIS B CG  1 
ATOM   3494 N ND1 . HIS B 1 161 ? -4.28600  -9.72400  -6.28400  1.000 28.06000 ? 163 HIS B ND1 1 
ATOM   3495 C CD2 . HIS B 1 161 ? -4.64600  -9.56200  -8.43600  1.000 28.33000 ? 163 HIS B CD2 1 
ATOM   3496 C CE1 . HIS B 1 161 ? -4.99000  -10.78400 -6.64500  1.000 32.96000 ? 163 HIS B CE1 1 
ATOM   3497 N NE2 . HIS B 1 161 ? -5.22300  -10.70800 -7.94300  1.000 30.48000 ? 163 HIS B NE2 1 
ATOM   3498 N N   . HIS B 1 162 ? -1.03400  -10.15500 -7.00200  1.000 26.50000 ? 164 HIS B N   1 
ATOM   3499 C CA  . HIS B 1 162 ? -0.33900  -11.21200 -7.73200  1.000 26.67000 ? 164 HIS B CA  1 
ATOM   3500 C C   . HIS B 1 162 ? -1.23200  -12.37500 -8.15100  1.000 31.38000 ? 164 HIS B C   1 
ATOM   3501 O O   . HIS B 1 162 ? -1.15800  -12.81100 -9.30400  1.000 31.88000 ? 164 HIS B O   1 
ATOM   3502 C CB  . HIS B 1 162 ? 0.84400   -11.74800 -6.90300  1.000 26.00000 ? 164 HIS B CB  1 
ATOM   3503 C CG  . HIS B 1 162 ? 2.01400   -10.81600 -6.85700  1.000 26.46000 ? 164 HIS B CG  1 
ATOM   3504 N ND1 . HIS B 1 162 ? 3.25200   -11.14200 -7.36600  1.000 28.17000 ? 164 HIS B ND1 1 
ATOM   3505 C CD2 . HIS B 1 162 ? 2.12400   -9.54800  -6.39100  1.000 30.24000 ? 164 HIS B CD2 1 
ATOM   3506 C CE1 . HIS B 1 162 ? 4.08000   -10.12500 -7.19500  1.000 31.57000 ? 164 HIS B CE1 1 
ATOM   3507 N NE2 . HIS B 1 162 ? 3.42000   -9.14400  -6.60600  1.000 30.18000 ? 164 HIS B NE2 1 
ATOM   3508 N N   . MET B 1 163 ? -2.02700  -12.94500 -7.24400  1.000 27.66000 ? 165 MET B N   1 
ATOM   3509 C CA  . MET B 1 163 ? -2.66300  -14.22400 -7.53200  1.000 31.97000 ? 165 MET B CA  1 
ATOM   3510 C C   . MET B 1 163 ? -4.00900  -14.35600 -6.84400  1.000 30.28000 ? 165 MET B C   1 
ATOM   3511 O O   . MET B 1 163 ? -4.31200  -13.65400 -5.88100  1.000 31.82000 ? 165 MET B O   1 
ATOM   3512 C CB  . MET B 1 163 ? -1.82800  -15.41600 -7.06600  1.000 28.26000 ? 165 MET B CB  1 
ATOM   3513 C CG  . MET B 1 163 ? -0.37200  -15.18900 -7.02200  1.000 37.02000 ? 165 MET B CG  1 
ATOM   3514 S SD  . MET B 1 163 ? 0.36000   -16.51100 -6.12100  1.000 37.56000 ? 165 MET B SD  1 
ATOM   3515 C CE  . MET B 1 163 ? -0.10400  -17.91000 -7.14800  1.000 36.69000 ? 165 MET B CE  1 
ATOM   3516 N N   . GLU B 1 164 ? -4.77200  -15.34700 -7.30300  1.000 35.34000 ? 166 GLU B N   1 
ATOM   3517 C CA  . GLU B 1 164 ? -5.99700  -15.77400 -6.65000  1.000 36.03000 ? 166 GLU B CA  1 
ATOM   3518 C C   . GLU B 1 164 ? -5.78400  -17.14400 -6.01900  1.000 37.34000 ? 166 GLU B C   1 
ATOM   3519 O O   . GLU B 1 164 ? -5.17000  -18.02700 -6.62300  1.000 35.64000 ? 166 GLU B O   1 
ATOM   3520 C CB  . GLU B 1 164 ? -7.16200  -15.81700 -7.64400  1.000 37.24000 ? 166 GLU B CB  1 
ATOM   3521 C CG  . GLU B 1 164 ? -8.49100  -16.18300 -7.00300  1.000 39.90000 ? 166 GLU B CG  1 
ATOM   3522 C CD  . GLU B 1 164 ? -9.67000  -15.93600 -7.92600  1.000 45.81000 ? 166 GLU B CD  1 
ATOM   3523 O OE1 . GLU B 1 164 ? -10.03300 -16.86700 -8.68000  1.000 44.45000 ? 166 GLU B OE1 1 
ATOM   3524 O OE2 . GLU B 1 164 ? -10.22500 -14.81000 -7.89100  1.000 45.65000 ? 166 GLU B OE2 1 
ATOM   3525 N N   . LEU B 1 165 ? -6.27400  -17.30800 -4.78700  1.000 37.05000 ? 167 LEU B N   1 
ATOM   3526 C CA  . LEU B 1 165 ? -6.24400  -18.57400 -4.07000  1.000 36.65000 ? 167 LEU B CA  1 
ATOM   3527 C C   . LEU B 1 165 ? -7.54900  -19.33800 -4.29800  1.000 38.69000 ? 167 LEU B C   1 
ATOM   3528 O O   . LEU B 1 165 ? -8.58900  -18.73900 -4.60300  1.000 39.32000 ? 167 LEU B O   1 
ATOM   3529 C CB  . LEU B 1 165 ? -6.01600  -18.32200 -2.57800  1.000 36.98000 ? 167 LEU B CB  1 
ATOM   3530 C CG  . LEU B 1 165 ? -4.71200  -17.55600 -2.27400  1.000 35.79000 ? 167 LEU B CG  1 
ATOM   3531 C CD1 . LEU B 1 165 ? -4.59400  -17.18800 -0.80500  1.000 33.05000 ? 167 LEU B CD1 1 
ATOM   3532 C CD2 . LEU B 1 165 ? -3.49100  -18.34400 -2.72900  1.000 35.52000 ? 167 LEU B CD2 1 
ATOM   3533 N N   . PRO B 1 166 ? -7.52200  -20.66800 -4.14700  1.000 39.51000 ? 168 PRO B N   1 
ATOM   3534 C CA  . PRO B 1 166 ? -8.67500  -21.49400 -4.56700  1.000 41.96000 ? 168 PRO B CA  1 
ATOM   3535 C C   . PRO B 1 166 ? -9.97900  -21.18000 -3.86200  1.000 45.19000 ? 168 PRO B C   1 
ATOM   3536 O O   . PRO B 1 166 ? -11.04500 -21.52300 -4.38800  1.000 46.20000 ? 168 PRO B O   1 
ATOM   3537 C CB  . PRO B 1 166 ? -8.21100  -22.92600 -4.25900  1.000 46.23000 ? 168 PRO B CB  1 
ATOM   3538 C CG  . PRO B 1 166 ? -7.04000  -22.77400 -3.32700  1.000 44.93000 ? 168 PRO B CG  1 
ATOM   3539 C CD  . PRO B 1 166 ? -6.37800  -21.50300 -3.74300  1.000 37.53000 ? 168 PRO B CD  1 
ATOM   3540 N N   . THR B 1 167 ? -9.94400  -20.55100 -2.69700  1.000 41.02000 ? 169 THR B N   1 
ATOM   3541 C CA  . THR B 1 167 ? -11.17600 -20.10200 -2.07300  1.000 38.84000 ? 169 THR B CA  1 
ATOM   3542 C C   . THR B 1 167 ? -11.70400 -18.80900 -2.69200  1.000 44.10000 ? 169 THR B C   1 
ATOM   3543 O O   . THR B 1 167 ? -12.71500 -18.27500 -2.22500  1.000 40.07000 ? 169 THR B O   1 
ATOM   3544 C CB  . THR B 1 167 ? -10.93200 -19.93800 -0.57700  1.000 41.55000 ? 169 THR B CB  1 
ATOM   3545 O OG1 . THR B 1 167 ? -12.09300 -19.40600 0.05400   1.000 54.52000 ? 169 THR B OG1 1 
ATOM   3546 C CG2 . THR B 1 167 ? -9.76700  -19.02300 -0.33800  1.000 35.87000 ? 169 THR B CG2 1 
ATOM   3547 N N   . GLY B 1 168 ? -11.05400 -18.30000 -3.73800  1.000 42.18000 ? 170 GLY B N   1 
ATOM   3548 C CA  . GLY B 1 168 ? -11.44100 -17.03900 -4.33200  1.000 40.35000 ? 170 GLY B CA  1 
ATOM   3549 C C   . GLY B 1 168 ? -10.96900 -15.79700 -3.60600  1.000 40.65000 ? 170 GLY B C   1 
ATOM   3550 O O   . GLY B 1 168 ? -11.44000 -14.70400 -3.92800  1.000 39.59000 ? 170 GLY B O   1 
ATOM   3551 N N   . VAL B 1 169 ? -10.07800 -15.92100 -2.62300  1.000 40.93000 ? 171 VAL B N   1 
ATOM   3552 C CA  . VAL B 1 169 ? -9.49200  -14.74600 -1.98600  1.000 36.94000 ? 171 VAL B CA  1 
ATOM   3553 C C   . VAL B 1 169 ? -8.17000  -14.47200 -2.69100  1.000 35.82000 ? 171 VAL B C   1 
ATOM   3554 O O   . VAL B 1 169 ? -7.80100  -15.20200 -3.61500  1.000 33.30000 ? 171 VAL B O   1 
ATOM   3555 C CB  . VAL B 1 169 ? -9.31300  -14.94200 -0.47000  1.000 36.20000 ? 171 VAL B CB  1 
ATOM   3556 C CG1 . VAL B 1 169 ? -10.64300 -15.35400 0.17200   1.000 41.18000 ? 171 VAL B CG1 1 
ATOM   3557 C CG2 . VAL B 1 169 ? -8.22700  -15.95800 -0.18800  1.000 33.91000 ? 171 VAL B CG2 1 
ATOM   3558 N N   . HIS B 1 170 ? -7.45400  -13.41700 -2.29400  1.000 32.65000 ? 172 HIS B N   1 
ATOM   3559 C CA  . HIS B 1 170 ? -6.32700  -12.96100 -3.10000  1.000 33.65000 ? 172 HIS B CA  1 
ATOM   3560 C C   . HIS B 1 170 ? -5.05300  -12.76600 -2.28100  1.000 30.81000 ? 172 HIS B C   1 
ATOM   3561 O O   . HIS B 1 170 ? -5.08900  -12.52300 -1.07200  1.000 29.46000 ? 172 HIS B O   1 
ATOM   3562 C CB  . HIS B 1 170 ? -6.73000  -11.69600 -3.85600  1.000 31.84000 ? 172 HIS B CB  1 
ATOM   3563 C CG  . HIS B 1 170 ? -7.95900  -11.89300 -4.69200  1.000 38.73000 ? 172 HIS B CG  1 
ATOM   3564 N ND1 . HIS B 1 170 ? -9.19500  -11.39900 -4.33100  1.000 37.54000 ? 172 HIS B ND1 1 
ATOM   3565 C CD2 . HIS B 1 170 ? -8.15500  -12.60400 -5.83000  1.000 37.13000 ? 172 HIS B CD2 1 
ATOM   3566 C CE1 . HIS B 1 170 ? -10.09000 -11.75500 -5.23600  1.000 39.60000 ? 172 HIS B CE1 1 
ATOM   3567 N NE2 . HIS B 1 170 ? -9.48700  -12.49100 -6.15300  1.000 40.92000 ? 172 HIS B NE2 1 
ATOM   3568 N N   . ALA B 1 171 ? -3.91600  -12.91400 -2.96900  1.000 27.95000 ? 173 ALA B N   1 
ATOM   3569 C CA  . ALA B 1 171 ? -2.59300  -12.87500 -2.37200  1.000 27.30000 ? 173 ALA B CA  1 
ATOM   3570 C C   . ALA B 1 171 ? -1.71400  -11.95600 -3.20300  1.000 25.53000 ? 173 ALA B C   1 
ATOM   3571 O O   . ALA B 1 171 ? -1.79200  -11.96800 -4.43800  1.000 25.82000 ? 173 ALA B O   1 
ATOM   3572 C CB  . ALA B 1 171 ? -1.95400  -14.30800 -2.28900  1.000 25.93000 ? 173 ALA B CB  1 
ATOM   3573 N N   . GLY B 1 172 ? -0.89600  -11.15500 -2.52500  1.000 26.00000 ? 174 GLY B N   1 
ATOM   3574 C CA  . GLY B 1 172 ? -0.00000  -10.24800 -3.20400  1.000 23.16000 ? 174 GLY B CA  1 
ATOM   3575 C C   . GLY B 1 172 ? 1.17300   -9.87100  -2.33000  1.000 25.49000 ? 174 GLY B C   1 
ATOM   3576 O O   . GLY B 1 172 ? 1.40500   -10.46500 -1.27900  1.000 25.74000 ? 174 GLY B O   1 
ATOM   3577 N N   . THR B 1 173 ? 1.90800   -8.85500  -2.77300  1.000 25.33000 ? 175 THR B N   1 
ATOM   3578 C CA  . THR B 1 173 ? 3.14200   -8.42800  -2.13400  1.000 27.12000 ? 175 THR B CA  1 
ATOM   3579 C C   . THR B 1 173 ? 3.04700   -6.96500  -1.71600  1.000 25.96000 ? 175 THR B C   1 
ATOM   3580 O O   . THR B 1 173 ? 2.12000   -6.24300  -2.10100  1.000 26.71000 ? 175 THR B O   1 
ATOM   3581 C CB  . THR B 1 173 ? 4.33900   -8.59800  -3.07700  1.000 28.56000 ? 175 THR B CB  1 
ATOM   3582 O OG1 . THR B 1 173 ? 4.14600   -7.76900  -4.23200  1.000 29.32000 ? 175 THR B OG1 1 
ATOM   3583 C CG2 . THR B 1 173 ? 4.47900   -10.03100 -3.51200  1.000 25.50000 ? 175 THR B CG2 1 
ATOM   3584 N N   . ASP B 1 174 ? 4.02600   -6.52000  -0.92100  1.000 27.47000 ? 176 ASP B N   1 
ATOM   3585 C CA  . ASP B 1 174 ? 4.24700   -5.08600  -0.83400  1.000 25.42000 ? 176 ASP B CA  1 
ATOM   3586 C C   . ASP B 1 174 ? 4.96400   -4.64000  -2.09900  1.000 25.03000 ? 176 ASP B C   1 
ATOM   3587 O O   . ASP B 1 174 ? 5.29300   -5.45100  -2.97400  1.000 25.83000 ? 176 ASP B O   1 
ATOM   3588 C CB  . ASP B 1 174 ? 5.02400   -4.70800  0.43400   1.000 27.54000 ? 176 ASP B CB  1 
ATOM   3589 C CG  . ASP B 1 174 ? 6.40100   -5.38000  0.53100   1.000 27.18000 ? 176 ASP B CG  1 
ATOM   3590 O OD1 . ASP B 1 174 ? 7.09800   -5.55400  -0.49000  1.000 27.24000 ? 176 ASP B OD1 1 
ATOM   3591 O OD2 . ASP B 1 174 ? 6.78400   -5.73500  1.65400   1.000 28.86000 ? 176 ASP B OD2 1 
ATOM   3592 N N   . LEU B 1 175 ? 5.23700   -3.33800  -2.20200  1.000 26.10000 ? 177 LEU B N   1 
ATOM   3593 C CA  . LEU B 1 175 ? 5.83700   -2.84000  -3.43500  1.000 23.73000 ? 177 LEU B CA  1 
ATOM   3594 C C   . LEU B 1 175 ? 7.33300   -3.14000  -3.51900  1.000 28.89000 ? 177 LEU B C   1 
ATOM   3595 O O   . LEU B 1 175 ? 7.93700   -2.87600  -4.56600  1.000 27.88000 ? 177 LEU B O   1 
ATOM   3596 C CB  . LEU B 1 175 ? 5.55900   -1.33000  -3.58200  1.000 27.08000 ? 177 LEU B CB  1 
ATOM   3597 C CG  . LEU B 1 175 ? 4.26600   -0.99100  -4.33100  1.000 26.88000 ? 177 LEU B CG  1 
ATOM   3598 C CD1 . LEU B 1 175 ? 4.44200   -1.22600  -5.82300  1.000 28.11000 ? 177 LEU B CD1 1 
ATOM   3599 C CD2 . LEU B 1 175 ? 3.06300   -1.82800  -3.81500  1.000 24.23000 ? 177 LEU B CD2 1 
ATOM   3600 N N   . GLU B 1 176 ? 7.93400   -3.68500  -2.45300  1.000 27.42000 ? 178 GLU B N   1 
ATOM   3601 C CA  . GLU B 1 176 ? 9.28200   -4.25800  -2.49000  1.000 27.00000 ? 178 GLU B CA  1 
ATOM   3602 C C   . GLU B 1 176 ? 9.28300   -5.75100  -2.82800  1.000 31.23000 ? 178 GLU B C   1 
ATOM   3603 O O   . GLU B 1 176 ? 10.33300  -6.40600  -2.74500  1.000 26.64000 ? 178 GLU B O   1 
ATOM   3604 C CB  . GLU B 1 176 ? 9.99500   -4.00800  -1.15400  1.000 28.30000 ? 178 GLU B CB  1 
ATOM   3605 C CG  . GLU B 1 176 ? 10.30000  -2.49700  -0.97000  1.000 32.70000 ? 178 GLU B CG  1 
ATOM   3606 C CD  . GLU B 1 176 ? 10.94400  -2.13600  0.36500   1.000 36.96000 ? 178 GLU B CD  1 
ATOM   3607 O OE1 . GLU B 1 176 ? 10.62000  -1.05800  0.90000   1.000 47.03000 ? 178 GLU B OE1 1 
ATOM   3608 O OE2 . GLU B 1 176 ? 11.79900  -2.88900  0.86300   1.000 42.67000 ? 178 GLU B OE2 1 
ATOM   3609 N N   . GLY B 1 177 ? 8.13400   -6.29400  -3.21400  1.000 25.08000 ? 179 GLY B N   1 
ATOM   3610 C CA  . GLY B 1 177 ? 8.03900   -7.66200  -3.68200  1.000 26.52000 ? 179 GLY B CA  1 
ATOM   3611 C C   . GLY B 1 177 ? 7.98400   -8.71600  -2.60700  1.000 25.80000 ? 179 GLY B C   1 
ATOM   3612 O O   . GLY B 1 177 ? 8.12900   -9.89700  -2.92800  1.000 26.87000 ? 179 GLY B O   1 
ATOM   3613 N N   . ASN B 1 178 ? 7.80800   -8.33600  -1.34300  1.000 25.13000 ? 180 ASN B N   1 
ATOM   3614 C CA  . ASN B 1 178 ? 7.66300   -9.31100  -0.26900  1.000 25.05000 ? 180 ASN B CA  1 
ATOM   3615 C C   . ASN B 1 178 ? 6.21300   -9.74700  -0.15400  1.000 27.78000 ? 180 ASN B C   1 
ATOM   3616 O O   . ASN B 1 178 ? 5.32100   -8.90000  -0.02800  1.000 26.30000 ? 180 ASN B O   1 
ATOM   3617 C CB  . ASN B 1 178 ? 8.12000   -8.70600  1.05000   1.000 26.86000 ? 180 ASN B CB  1 
ATOM   3618 C CG  . ASN B 1 178 ? 9.51600   -8.13500  0.96700   1.000 29.69000 ? 180 ASN B CG  1 
ATOM   3619 O OD1 . ASN B 1 178 ? 10.48900  -8.88300  0.90100   1.000 29.07000 ? 180 ASN B OD1 1 
ATOM   3620 N ND2 . ASN B 1 178 ? 9.62500   -6.80700  0.97100   1.000 28.46000 ? 180 ASN B ND2 1 
ATOM   3621 N N   . PHE B 1 179 ? 5.97200   -11.06300 -0.17400  1.000 29.71000 ? 181 PHE B N   1 
ATOM   3622 C CA  . PHE B 1 179 ? 4.59700   -11.54400 -0.10400  1.000 28.94000 ? 181 PHE B CA  1 
ATOM   3623 C C   . PHE B 1 179 ? 3.98900   -11.23900 1.24900   1.000 26.09000 ? 181 PHE B C   1 
ATOM   3624 O O   . PHE B 1 179 ? 4.67800   -11.20300 2.26700   1.000 25.30000 ? 181 PHE B O   1 
ATOM   3625 C CB  . PHE B 1 179 ? 4.49900   -13.04800 -0.35800  1.000 25.84000 ? 181 PHE B CB  1 
ATOM   3626 C CG  . PHE B 1 179 ? 3.97800   -13.38000 -1.71800  1.000 27.68000 ? 181 PHE B CG  1 
ATOM   3627 C CD1 . PHE B 1 179 ? 2.61900   -13.31700 -1.98900  1.000 26.53000 ? 181 PHE B CD1 1 
ATOM   3628 C CD2 . PHE B 1 179 ? 4.86300   -13.68400 -2.75000  1.000 27.04000 ? 181 PHE B CD2 1 
ATOM   3629 C CE1 . PHE B 1 179 ? 2.14700   -13.57200 -3.25000  1.000 28.07000 ? 181 PHE B CE1 1 
ATOM   3630 C CE2 . PHE B 1 179 ? 4.40200   -13.95300 -4.01100  1.000 28.08000 ? 181 PHE B CE2 1 
ATOM   3631 C CZ  . PHE B 1 179 ? 3.04100   -13.89900 -4.26700  1.000 28.67000 ? 181 PHE B CZ  1 
ATOM   3632 N N   . TYR B 1 180 ? 2.68700   -10.97200 1.23300   1.000 24.38000 ? 182 TYR B N   1 
ATOM   3633 C CA  . TYR B 1 180 ? 1.86300   -11.02300 2.42600   1.000 25.39000 ? 182 TYR B CA  1 
ATOM   3634 C C   . TYR B 1 180 ? 1.35300   -12.44800 2.54500   1.000 25.94000 ? 182 TYR B C   1 
ATOM   3635 O O   . TYR B 1 180 ? 0.74300   -12.96800 1.60600   1.000 26.77000 ? 182 TYR B O   1 
ATOM   3636 C CB  . TYR B 1 180 ? 0.69300   -10.04200 2.33100   1.000 26.99000 ? 182 TYR B CB  1 
ATOM   3637 C CG  . TYR B 1 180 ? 1.06800   -8.56900  2.39500   1.000 24.57000 ? 182 TYR B CG  1 
ATOM   3638 C CD1 . TYR B 1 180 ? 1.38400   -7.96400  3.60800   1.000 24.83000 ? 182 TYR B CD1 1 
ATOM   3639 C CD2 . TYR B 1 180 ? 1.05700   -7.78200  1.25600   1.000 26.15000 ? 182 TYR B CD2 1 
ATOM   3640 C CE1 . TYR B 1 180 ? 1.70100   -6.60100  3.67800   1.000 27.22000 ? 182 TYR B CE1 1 
ATOM   3641 C CE2 . TYR B 1 180 ? 1.35800   -6.41200  1.31000   1.000 25.19000 ? 182 TYR B CE2 1 
ATOM   3642 C CZ  . TYR B 1 180 ? 1.68300   -5.83600  2.53200   1.000 26.49000 ? 182 TYR B CZ  1 
ATOM   3643 O OH  . TYR B 1 180 ? 1.97200   -4.49500  2.62200   1.000 28.14000 ? 182 TYR B OH  1 
ATOM   3644 N N   . GLY B 1 181 ? 1.63300   -13.09400 3.66700   1.000 27.96000 ? 183 GLY B N   1 
ATOM   3645 C CA  . GLY B 1 181 ? 1.16700   -14.44300 3.88200   1.000 26.10000 ? 183 GLY B CA  1 
ATOM   3646 C C   . GLY B 1 181 ? 2.08200   -15.49200 3.28200   1.000 27.73000 ? 183 GLY B C   1 
ATOM   3647 O O   . GLY B 1 181 ? 2.97400   -15.19400 2.48000   1.000 28.86000 ? 183 GLY B O   1 
ATOM   3648 N N   . PRO B 1 182 ? 1.85300   -16.75000 3.65000   1.000 26.17000 ? 184 PRO B N   1 
ATOM   3649 C CA  . PRO B 1 182 ? 2.77300   -17.85100 3.27800   1.000 28.87000 ? 184 PRO B CA  1 
ATOM   3650 C C   . PRO B 1 182 ? 2.49800   -18.39600 1.87900   1.000 31.06000 ? 184 PRO B C   1 
ATOM   3651 O O   . PRO B 1 182 ? 2.18000   -19.58000 1.68900   1.000 29.26000 ? 184 PRO B O   1 
ATOM   3652 C CB  . PRO B 1 182 ? 2.50000   -18.89000 4.37500   1.000 29.43000 ? 184 PRO B CB  1 
ATOM   3653 C CG  . PRO B 1 182 ? 1.02400   -18.69400 4.72500   1.000 28.94000 ? 184 PRO B CG  1 
ATOM   3654 C CD  . PRO B 1 182 ? 0.78400   -17.17500 4.57700   1.000 24.78000 ? 184 PRO B CD  1 
ATOM   3655 N N   . PHE B 1 183 ? 2.61600   -17.52400 0.87700   1.000 26.93000 ? 185 PHE B N   1 
ATOM   3656 C CA  . PHE B 1 183 ? 2.21300   -17.82000 -0.49000  1.000 28.08000 ? 185 PHE B CA  1 
ATOM   3657 C C   . PHE B 1 183 ? 3.38100   -17.60000 -1.44500  1.000 29.26000 ? 185 PHE B C   1 
ATOM   3658 O O   . PHE B 1 183 ? 4.31100   -16.84500 -1.14800  1.000 32.24000 ? 185 PHE B O   1 
ATOM   3659 C CB  . PHE B 1 183 ? 0.99300   -16.95800 -0.89100  1.000 29.32000 ? 185 PHE B CB  1 
ATOM   3660 C CG  . PHE B 1 183 ? -0.12100  -17.01500 0.11300   1.000 27.37000 ? 185 PHE B CG  1 
ATOM   3661 C CD1 . PHE B 1 183 ? -0.70300  -18.23100 0.44600   1.000 29.82000 ? 185 PHE B CD1 1 
ATOM   3662 C CD2 . PHE B 1 183 ? -0.55000  -15.87100 0.75700   1.000 26.46000 ? 185 PHE B CD2 1 
ATOM   3663 C CE1 . PHE B 1 183 ? -1.70300  -18.30700 1.39000   1.000 32.48000 ? 185 PHE B CE1 1 
ATOM   3664 C CE2 . PHE B 1 183 ? -1.55800  -15.93500 1.70000   1.000 28.69000 ? 185 PHE B CE2 1 
ATOM   3665 C CZ  . PHE B 1 183 ? -2.13800  -17.14500 2.02200   1.000 27.70000 ? 185 PHE B CZ  1 
ATOM   3666 N N   . VAL B 1 184 ? 3.35300   -18.30600 -2.58000  1.000 29.47000 ? 186 VAL B N   1 
ATOM   3667 C CA  . VAL B 1 184 ? 4.44200   -18.26300 -3.54700  1.000 31.15000 ? 186 VAL B CA  1 
ATOM   3668 C C   . VAL B 1 184 ? 3.85300   -18.00400 -4.92200  1.000 31.97000 ? 186 VAL B C   1 
ATOM   3669 O O   . VAL B 1 184 ? 2.70600   -18.36800 -5.20300  1.000 33.13000 ? 186 VAL B O   1 
ATOM   3670 C CB  . VAL B 1 184 ? 5.29200   -19.55600 -3.54300  1.000 33.35000 ? 186 VAL B CB  1 
ATOM   3671 C CG1 . VAL B 1 184 ? 5.99600   -19.72200 -2.20000  1.000 34.52000 ? 186 VAL B CG1 1 
ATOM   3672 C CG2 . VAL B 1 184 ? 4.44700   -20.80000 -3.87800  1.000 33.07000 ? 186 VAL B CG2 1 
ATOM   3673 N N   . ASP B 1 185 ? 4.63100   -17.33700 -5.77900  1.000 31.65000 ? 187 ASP B N   1 
ATOM   3674 C CA  . ASP B 1 185 ? 4.13000   -16.96600 -7.10200  1.000 32.81000 ? 187 ASP B CA  1 
ATOM   3675 C C   . ASP B 1 185 ? 4.43200   -18.06700 -8.12400  1.000 32.37000 ? 187 ASP B C   1 
ATOM   3676 O O   . ASP B 1 185 ? 5.20900   -17.90800 -9.06500  1.000 34.67000 ? 187 ASP B O   1 
ATOM   3677 C CB  . ASP B 1 185 ? 4.68900   -15.61600 -7.53400  1.000 32.10000 ? 187 ASP B CB  1 
ATOM   3678 C CG  . ASP B 1 185 ? 6.20800   -15.53300 -7.43800  1.000 32.22000 ? 187 ASP B CG  1 
ATOM   3679 O OD1 . ASP B 1 185 ? 6.85900   -16.43000 -6.85100  1.000 33.04000 ? 187 ASP B OD1 1 
ATOM   3680 O OD2 . ASP B 1 185 ? 6.74500   -14.53400 -7.95000  1.000 30.02000 ? 187 ASP B OD2 1 
ATOM   3681 N N   . ARG B 1 186 ? 3.74200   -19.18900 -7.95000  1.000 33.74000 ? 188 ARG B N   1 
ATOM   3682 C CA  . ARG B 1 186 ? 3.72100   -20.24200 -8.95900  1.000 37.56000 ? 188 ARG B CA  1 
ATOM   3683 C C   . ARG B 1 186 ? 2.44300   -21.05800 -8.79500  1.000 38.24000 ? 188 ARG B C   1 
ATOM   3684 O O   . ARG B 1 186 ? 1.69800   -20.89800 -7.82300  1.000 35.72000 ? 188 ARG B O   1 
ATOM   3685 C CB  . ARG B 1 186 ? 4.96800   -21.14100 -8.86800  1.000 37.90000 ? 188 ARG B CB  1 
ATOM   3686 C CG  . ARG B 1 186 ? 5.20500   -21.78900 -7.52000  1.000 34.87000 ? 188 ARG B CG  1 
ATOM   3687 C CD  . ARG B 1 186 ? 6.55700   -22.51500 -7.53900  1.000 39.86000 ? 188 ARG B CD  1 
ATOM   3688 N NE  . ARG B 1 186 ? 6.84300   -23.20600 -6.28500  1.000 37.98000 ? 188 ARG B NE  1 
ATOM   3689 C CZ  . ARG B 1 186 ? 7.45800   -22.63100 -5.25500  1.000 35.95000 ? 188 ARG B CZ  1 
ATOM   3690 N NH1 . ARG B 1 186 ? 7.83500   -21.36000 -5.34500  1.000 34.36000 ? 188 ARG B NH1 1 
ATOM   3691 N NH2 . ARG B 1 186 ? 7.70000   -23.32300 -4.14300  1.000 33.93000 ? 188 ARG B NH2 1 
ATOM   3692 N N   . GLN B 1 187 ? 2.19800   -21.93800 -9.76700  1.000 38.05000 ? 189 GLN B N   1 
ATOM   3693 C CA  . GLN B 1 187 ? 1.01700   -22.79500 -9.74800  1.000 41.07000 ? 189 GLN B CA  1 
ATOM   3694 C C   . GLN B 1 187 ? 1.25300   -23.91100 -8.73600  1.000 43.59000 ? 189 GLN B C   1 
ATOM   3695 O O   . GLN B 1 187 ? 2.10000   -24.79200 -8.94700  1.000 42.62000 ? 189 GLN B O   1 
ATOM   3696 C CB  . GLN B 1 187 ? 0.71400   -23.34900 -11.14100 1.000 42.78000 ? 189 GLN B CB  1 
ATOM   3697 N N   . THR B 1 188 ? 0.49600   -23.86500 -7.64000  1.000 42.09000 ? 190 THR B N   1 
ATOM   3698 C CA  . THR B 1 188 ? 0.63200   -24.78600 -6.52300  1.000 44.52000 ? 190 THR B CA  1 
ATOM   3699 C C   . THR B 1 188 ? -0.73000  -24.96800 -5.86800  1.000 46.67000 ? 190 THR B C   1 
ATOM   3700 O O   . THR B 1 188 ? -1.70000  -24.27300 -6.18600  1.000 46.79000 ? 190 THR B O   1 
ATOM   3701 C CB  . THR B 1 188 ? 1.65000   -24.27900 -5.48500  1.000 48.01000 ? 190 THR B CB  1 
ATOM   3702 O OG1 . THR B 1 188 ? 1.96300   -25.33100 -4.57300  1.000 56.20000 ? 190 THR B OG1 1 
ATOM   3703 C CG2 . THR B 1 188 ? 1.06000   -23.16900 -4.69100  1.000 42.78000 ? 190 THR B CG2 1 
ATOM   3704 N N   . ALA B 1 189 ? -0.79600  -25.91400 -4.93300  1.000 43.34000 ? 191 ALA B N   1 
ATOM   3705 C CA  . ALA B 1 189 ? -2.04400  -26.22900 -4.25700  1.000 45.39000 ? 191 ALA B CA  1 
ATOM   3706 C C   . ALA B 1 189 ? -2.29300  -25.36000 -3.02400  1.000 47.48000 ? 191 ALA B C   1 
ATOM   3707 O O   . ALA B 1 189 ? -3.14500  -25.70900 -2.19800  1.000 47.53000 ? 191 ALA B O   1 
ATOM   3708 C CB  . ALA B 1 189 ? -2.06500  -27.70600 -3.87000  1.000 45.08000 ? 191 ALA B CB  1 
ATOM   3709 N N   . GLN B 1 190 ? -1.61200  -24.22400 -2.90200  1.000 39.80000 ? 192 GLN B N   1 
ATOM   3710 C CA  . GLN B 1 190 ? -1.64300  -23.47000 -1.65400  1.000 40.90000 ? 192 GLN B CA  1 
ATOM   3711 C C   . GLN B 1 190 ? -3.04600  -22.95000 -1.35900  1.000 37.17000 ? 192 GLN B C   1 
ATOM   3712 O O   . GLN B 1 190 ? -3.83500  -22.66400 -2.26000  1.000 36.99000 ? 192 GLN B O   1 
ATOM   3713 C CB  . GLN B 1 190 ? -0.66300  -22.29600 -1.70700  1.000 40.87000 ? 192 GLN B CB  1 
ATOM   3714 C CG  . GLN B 1 190 ? -0.97500  -21.25800 -2.78000  1.000 38.49000 ? 192 GLN B CG  1 
ATOM   3715 C CD  . GLN B 1 190 ? 0.25200   -20.38600 -3.09000  1.000 38.22000 ? 192 GLN B CD  1 
ATOM   3716 O OE1 . GLN B 1 190 ? 1.19000   -20.35000 -2.31500  1.000 32.62000 ? 192 GLN B OE1 1 
ATOM   3717 N NE2 . GLN B 1 190 ? 0.23600   -19.69400 -4.22200  1.000 39.06000 ? 192 GLN B NE2 1 
ATOM   3718 N N   . ALA B 1 191 ? -3.34900  -22.83900 -0.07100  1.000 34.69000 ? 193 ALA B N   1 
ATOM   3719 C CA  . ALA B 1 191 ? -4.64000  -22.36500 0.39300   1.000 39.72000 ? 193 ALA B CA  1 
ATOM   3720 C C   . ALA B 1 191 ? -4.41700  -21.36100 1.51100   1.000 39.20000 ? 193 ALA B C   1 
ATOM   3721 O O   . ALA B 1 191 ? -3.44300  -21.45200 2.26500   1.000 40.42000 ? 193 ALA B O   1 
ATOM   3722 C CB  . ALA B 1 191 ? -5.53500  -23.52000 0.88800   1.000 37.84000 ? 193 ALA B CB  1 
ATOM   3723 N N   . ALA B 1 192 ? -5.32300  -20.39300 1.59600   1.000 39.70000 ? 194 ALA B N   1 
ATOM   3724 C CA  . ALA B 1 192 ? -5.36200  -19.52800 2.76000   1.000 42.28000 ? 194 ALA B CA  1 
ATOM   3725 C C   . ALA B 1 192 ? -5.59800  -20.35500 4.01900   1.000 43.44000 ? 194 ALA B C   1 
ATOM   3726 O O   . ALA B 1 192 ? -6.31100  -21.36400 3.99800   1.000 41.56000 ? 194 ALA B O   1 
ATOM   3727 C CB  . ALA B 1 192 ? -6.46800  -18.48200 2.60000   1.000 41.11000 ? 194 ALA B CB  1 
ATOM   3728 N N   . GLY B 1 193 ? -4.98400  -19.93200 5.11700   1.000 44.58000 ? 195 GLY B N   1 
ATOM   3729 C CA  . GLY B 1 193 ? -5.28100  -20.52100 6.40300   1.000 41.87000 ? 195 GLY B CA  1 
ATOM   3730 C C   . GLY B 1 193 ? -6.65100  -20.10800 6.91600   1.000 41.92000 ? 195 GLY B C   1 
ATOM   3731 O O   . GLY B 1 193 ? -7.35200  -19.26300 6.34700   1.000 39.70000 ? 195 GLY B O   1 
ATOM   3732 N N   . THR B 1 194 ? -7.04100  -20.73000 8.02400   1.000 37.78000 ? 196 THR B N   1 
ATOM   3733 C CA  . THR B 1 194 ? -8.32100  -20.39900 8.62500   1.000 46.10000 ? 196 THR B CA  1 
ATOM   3734 C C   . THR B 1 194 ? -8.32200  -18.93500 9.01900   1.000 41.66000 ? 196 THR B C   1 
ATOM   3735 O O   . THR B 1 194 ? -7.46800  -18.47600 9.78200   1.000 47.80000 ? 196 THR B O   1 
ATOM   3736 C CB  . THR B 1 194 ? -8.61600  -21.27300 9.84300   1.000 49.32000 ? 196 THR B CB  1 
ATOM   3737 O OG1 . THR B 1 194 ? -9.72700  -20.70300 10.55000  1.000 53.37000 ? 196 THR B OG1 1 
ATOM   3738 C CG2 . THR B 1 194 ? -7.42100  -21.32600 10.76700  1.000 47.17000 ? 196 THR B CG2 1 
ATOM   3739 N N   . ASP B 1 195 ? -9.26000  -18.19700 8.47400   1.000 41.37000 ? 197 ASP B N   1 
ATOM   3740 C CA  . ASP B 1 195 ? -9.27200  -16.79100 8.78300   1.000 42.51000 ? 197 ASP B CA  1 
ATOM   3741 C C   . ASP B 1 195 ? -9.95500  -16.56200 10.12200  1.000 43.67000 ? 197 ASP B C   1 
ATOM   3742 O O   . ASP B 1 195 ? -10.66000 -17.42500 10.65000  1.000 42.95000 ? 197 ASP B O   1 
ATOM   3743 C CB  . ASP B 1 195 ? -9.96400  -16.02100 7.68000   1.000 36.69000 ? 197 ASP B CB  1 
ATOM   3744 C CG  . ASP B 1 195 ? -9.55600  -14.56200 7.65100   1.000 40.36000 ? 197 ASP B CG  1 
ATOM   3745 O OD1 . ASP B 1 195 ? -8.40700  -14.21900 8.06300   1.000 35.75000 ? 197 ASP B OD1 1 
ATOM   3746 O OD2 . ASP B 1 195 ? -10.41000 -13.76300 7.23500   1.000 33.38000 ? 197 ASP B OD2 1 
ATOM   3747 N N   . THR B 1 196 ? -9.70200  -15.39400 10.68600  1.000 37.33000 ? 198 THR B N   1 
ATOM   3748 C CA  . THR B 1 196 ? -10.32300 -14.96000 11.92000  1.000 36.76000 ? 198 THR B CA  1 
ATOM   3749 C C   . THR B 1 196 ? -10.85100 -13.55400 11.69200  1.000 37.52000 ? 198 THR B C   1 
ATOM   3750 O O   . THR B 1 196 ? -10.51100 -12.89800 10.70100  1.000 36.05000 ? 198 THR B O   1 
ATOM   3751 C CB  . THR B 1 196 ? -9.33600  -14.97700 13.09400  1.000 41.98000 ? 198 THR B CB  1 
ATOM   3752 O OG1 . THR B 1 196 ? -8.13200  -14.30400 12.71300  1.000 38.50000 ? 198 THR B OG1 1 
ATOM   3753 C CG2 . THR B 1 196 ? -9.00100  -16.39100 13.50300  1.000 41.33000 ? 198 THR B CG2 1 
ATOM   3754 N N   . THR B 1 197 ? -11.68000 -13.09300 12.62100  1.000 34.28000 ? 199 THR B N   1 
ATOM   3755 C CA  . THR B 1 197 ? -12.32000 -11.79100 12.50200  1.000 34.18000 ? 199 THR B CA  1 
ATOM   3756 C C   . THR B 1 197 ? -11.50600 -10.75100 13.25200  1.000 33.11000 ? 199 THR B C   1 
ATOM   3757 O O   . THR B 1 197 ? -10.94600 -11.03700 14.31400  1.000 32.13000 ? 199 THR B O   1 
ATOM   3758 C CB  . THR B 1 197 ? -13.74800 -11.84000 13.05000  1.000 34.21000 ? 199 THR B CB  1 
ATOM   3759 O OG1 . THR B 1 197 ? -14.50900 -12.76800 12.28500  1.000 32.76000 ? 199 THR B OG1 1 
ATOM   3760 C CG2 . THR B 1 197 ? -14.40800 -10.46600 12.95900  1.000 30.87000 ? 199 THR B CG2 1 
ATOM   3761 N N   . ILE B 1 198 ? -11.44600 -9.54100  12.69100  1.000 31.41000 ? 200 ILE B N   1 
ATOM   3762 C CA  . ILE B 1 198 ? -10.59600 -8.47900  13.20900  1.000 28.62000 ? 200 ILE B CA  1 
ATOM   3763 C C   . ILE B 1 198 ? -11.37300 -7.77400  14.31400  1.000 33.74000 ? 200 ILE B C   1 
ATOM   3764 O O   . ILE B 1 198 ? -12.16000 -6.85900  14.05800  1.000 30.09000 ? 200 ILE B O   1 
ATOM   3765 C CB  . ILE B 1 198 ? -10.16500 -7.51200  12.10600  1.000 29.58000 ? 200 ILE B CB  1 
ATOM   3766 C CG1 . ILE B 1 198 ? -9.55100  -8.31000  10.95100  1.000 32.15000 ? 200 ILE B CG1 1 
ATOM   3767 C CG2 . ILE B 1 198 ? -9.20900  -6.45000  12.65100  1.000 28.65000 ? 200 ILE B CG2 1 
ATOM   3768 C CD1 . ILE B 1 198 ? -9.69300  -7.62800  9.61200   1.000 33.02000 ? 200 ILE B CD1 1 
ATOM   3769 N N   . THR B 1 199 ? -11.08700 -8.16500  15.55600  1.000 32.99000 ? 201 THR B N   1 
ATOM   3770 C CA  . THR B 1 199 ? -11.89400 -7.76600  16.70400  1.000 36.03000 ? 201 THR B CA  1 
ATOM   3771 C C   . THR B 1 199 ? -11.88700 -6.25300  16.92100  1.000 32.92000 ? 201 THR B C   1 
ATOM   3772 O O   . THR B 1 199 ? -12.93800 -5.65200  17.17500  1.000 33.77000 ? 201 THR B O   1 
ATOM   3773 C CB  . THR B 1 199 ? -11.38600 -8.49800  17.94300  1.000 34.67000 ? 201 THR B CB  1 
ATOM   3774 O OG1 . THR B 1 199 ? -11.31900 -9.89600  17.65100  1.000 32.74000 ? 201 THR B OG1 1 
ATOM   3775 C CG2 . THR B 1 199 ? -12.31700 -8.26700  19.11900  1.000 38.44000 ? 201 THR B CG2 1 
ATOM   3776 N N   . VAL B 1 200 ? -10.71100 -5.61900  16.86200  1.000 32.71000 ? 202 VAL B N   1 
ATOM   3777 C CA  . VAL B 1 200 ? -10.65500 -4.18000  17.12600  1.000 30.40000 ? 202 VAL B CA  1 
ATOM   3778 C C   . VAL B 1 200 ? -11.42900 -3.40100  16.06400  1.000 32.05000 ? 202 VAL B C   1 
ATOM   3779 O O   . VAL B 1 200 ? -11.98200 -2.32900  16.34600  1.000 31.95000 ? 202 VAL B O   1 
ATOM   3780 C CB  . VAL B 1 200 ? -9.19500  -3.69400  17.24800  1.000 36.61000 ? 202 VAL B CB  1 
ATOM   3781 C CG1 . VAL B 1 200 ? -8.40300  -3.96600  15.97300  1.000 31.42000 ? 202 VAL B CG1 1 
ATOM   3782 C CG2 . VAL B 1 200 ? -9.16000  -2.21400  17.62400  1.000 30.73000 ? 202 VAL B CG2 1 
ATOM   3783 N N   . ASN B 1 201 ? -11.51000 -3.93500  14.84700  1.000 29.07000 ? 203 ASN B N   1 
ATOM   3784 C CA  . ASN B 1 201 ? -12.31300 -3.30400  13.81000  1.000 32.81000 ? 203 ASN B CA  1 
ATOM   3785 C C   . ASN B 1 201 ? -13.80800 -3.46200  14.08500  1.000 30.84000 ? 203 ASN B C   1 
ATOM   3786 O O   . ASN B 1 201 ? -14.57200 -2.51100  13.89200  1.000 28.22000 ? 203 ASN B O   1 
ATOM   3787 C CB  . ASN B 1 201 ? -11.94400 -3.88400  12.44400  1.000 30.48000 ? 203 ASN B CB  1 
ATOM   3788 C CG  . ASN B 1 201 ? -10.58200 -3.37800  11.92400  1.000 32.22000 ? 203 ASN B CG  1 
ATOM   3789 O OD1 . ASN B 1 201 ? -9.85100  -2.65000  12.61400  1.000 29.04000 ? 203 ASN B OD1 1 
ATOM   3790 N ND2 . ASN B 1 201 ? -10.24500 -3.77300  10.69800  1.000 26.78000 ? 203 ASN B ND2 1 
ATOM   3791 N N   . VAL B 1 202 ? -14.25000 -4.65000  14.53000  1.000 31.82000 ? 204 VAL B N   1 
ATOM   3792 C CA  . VAL B 1 202 ? -15.66000 -4.82100  14.89300  1.000 31.08000 ? 204 VAL B CA  1 
ATOM   3793 C C   . VAL B 1 202 ? -16.04200 -3.84600  15.99600  1.000 32.27000 ? 204 VAL B C   1 
ATOM   3794 O O   . VAL B 1 202 ? -17.11600 -3.24200  15.96300  1.000 32.75000 ? 204 VAL B O   1 
ATOM   3795 C CB  . VAL B 1 202 ? -15.97200 -6.27100  15.31200  1.000 30.84000 ? 204 VAL B CB  1 
ATOM   3796 C CG1 . VAL B 1 202 ? -17.45500 -6.39500  15.70800  1.000 29.92000 ? 204 VAL B CG1 1 
ATOM   3797 C CG2 . VAL B 1 202 ? -15.65000 -7.24700  14.19700  1.000 30.36000 ? 204 VAL B CG2 1 
ATOM   3798 N N   . LEU B 1 203 ? -15.17400 -3.68800  16.99400  1.000 32.95000 ? 205 LEU B N   1 
ATOM   3799 C CA  . LEU B 1 203 ? -15.43600 -2.72400  18.05100  1.000 34.22000 ? 205 LEU B CA  1 
ATOM   3800 C C   . LEU B 1 203 ? -15.52100 -1.30500  17.49500  1.000 34.31000 ? 205 LEU B C   1 
ATOM   3801 O O   . LEU B 1 203 ? -16.43500 -0.55200  17.84700  1.000 31.67000 ? 205 LEU B O   1 
ATOM   3802 C CB  . LEU B 1 203 ? -14.35500 -2.84200  19.12600  1.000 32.01000 ? 205 LEU B CB  1 
ATOM   3803 C CG  . LEU B 1 203 ? -14.47300 -4.17600  19.88100  1.000 36.00000 ? 205 LEU B CG  1 
ATOM   3804 C CD1 . LEU B 1 203 ? -13.19000 -4.51400  20.64000  1.000 32.82000 ? 205 LEU B CD1 1 
ATOM   3805 C CD2 . LEU B 1 203 ? -15.66500 -4.13700  20.83000  1.000 35.18000 ? 205 LEU B CD2 1 
ATOM   3806 N N   . ALA B 1 204 ? -14.60200 -0.93800  16.59600  1.000 32.43000 ? 206 ALA B N   1 
ATOM   3807 C CA  . ALA B 1 204 ? -14.65000 0.38500   15.97400  1.000 31.11000 ? 206 ALA B CA  1 
ATOM   3808 C C   . ALA B 1 204 ? -15.97300 0.60900   15.25100  1.000 33.10000 ? 206 ALA B C   1 
ATOM   3809 O O   . ALA B 1 204 ? -16.57100 1.69300   15.33500  1.000 32.77000 ? 206 ALA B O   1 
ATOM   3810 C CB  . ALA B 1 204 ? -13.48200 0.53800   14.99900  1.000 32.63000 ? 206 ALA B CB  1 
ATOM   3811 N N   . TRP B 1 205 ? -16.43200 -0.40900  14.52700  1.000 32.71000 ? 207 TRP B N   1 
ATOM   3812 C CA  . TRP B 1 205 ? -17.67300 -0.32400  13.77300  1.000 33.15000 ? 207 TRP B CA  1 
ATOM   3813 C C   . TRP B 1 205 ? -18.87400 -0.19600  14.70400  1.000 35.10000 ? 207 TRP B C   1 
ATOM   3814 O O   . TRP B 1 205 ? -19.81600 0.55200   14.41300  1.000 34.61000 ? 207 TRP B O   1 
ATOM   3815 C CB  . TRP B 1 205 ? -17.77400 -1.56000  12.88600  1.000 34.07000 ? 207 TRP B CB  1 
ATOM   3816 C CG  . TRP B 1 205 ? -19.01200 -1.71900  12.05500  1.000 34.67000 ? 207 TRP B CG  1 
ATOM   3817 C CD1 . TRP B 1 205 ? -19.32800 -1.05500  10.90600  1.000 34.01000 ? 207 TRP B CD1 1 
ATOM   3818 C CD2 . TRP B 1 205 ? -20.06000 -2.66600  12.27400  1.000 37.32000 ? 207 TRP B CD2 1 
ATOM   3819 N NE1 . TRP B 1 205 ? -20.52900 -1.51200  10.41400  1.000 35.90000 ? 207 TRP B NE1 1 
ATOM   3820 C CE2 . TRP B 1 205 ? -20.99900 -2.49800  11.23600  1.000 35.78000 ? 207 TRP B CE2 1 
ATOM   3821 C CE3 . TRP B 1 205 ? -20.30600 -3.62400  13.25900  1.000 34.80000 ? 207 TRP B CE3 1 
ATOM   3822 C CZ2 . TRP B 1 205 ? -22.15600 -3.25800  11.15100  1.000 38.84000 ? 207 TRP B CZ2 1 
ATOM   3823 C CZ3 . TRP B 1 205 ? -21.45500 -4.37800  13.17200  1.000 41.14000 ? 207 TRP B CZ3 1 
ATOM   3824 C CH2 . TRP B 1 205 ? -22.36900 -4.18900  12.12600  1.000 39.94000 ? 207 TRP B CH2 1 
ATOM   3825 N N   . LEU B 1 206 ? -18.84400 -0.90400  15.83700  1.000 31.23000 ? 208 LEU B N   1 
ATOM   3826 C CA  . LEU B 1 206 ? -19.88100 -0.71900  16.84500  1.000 36.93000 ? 208 LEU B CA  1 
ATOM   3827 C C   . LEU B 1 206 ? -19.87800 0.71300   17.36800  1.000 35.77000 ? 208 LEU B C   1 
ATOM   3828 O O   . LEU B 1 206 ? -20.94300 1.29300   17.59100  1.000 33.82000 ? 208 LEU B O   1 
ATOM   3829 C CB  . LEU B 1 206 ? -19.70500 -1.72800  17.99000  1.000 30.42000 ? 208 LEU B CB  1 
ATOM   3830 C CG  . LEU B 1 206 ? -19.94700 -3.19500  17.62100  1.000 34.94000 ? 208 LEU B CG  1 
ATOM   3831 C CD1 . LEU B 1 206 ? -19.74800 -4.14000  18.81300  1.000 35.84000 ? 208 LEU B CD1 1 
ATOM   3832 C CD2 . LEU B 1 206 ? -21.34400 -3.39100  17.02800  1.000 39.44000 ? 208 LEU B CD2 1 
ATOM   3833 N N   . TYR B 1 207 ? -18.68900 1.30200   17.56100  1.000 33.40000 ? 209 TYR B N   1 
ATOM   3834 C CA  . TYR B 1 207 ? -18.62300 2.71000   17.94500  1.000 36.94000 ? 209 TYR B CA  1 
ATOM   3835 C C   . TYR B 1 207 ? -19.20600 3.59200   16.85000  1.000 38.83000 ? 209 TYR B C   1 
ATOM   3836 O O   . TYR B 1 207 ? -19.90900 4.56600   17.13700  1.000 38.13000 ? 209 TYR B O   1 
ATOM   3837 C CB  . TYR B 1 207 ? -17.18000 3.12600   18.25000  1.000 36.19000 ? 209 TYR B CB  1 
ATOM   3838 C CG  . TYR B 1 207 ? -16.71300 2.78100   19.65200  1.000 39.62000 ? 209 TYR B CG  1 
ATOM   3839 C CD1 . TYR B 1 207 ? -17.16300 3.49600   20.76300  1.000 43.24000 ? 209 TYR B CD1 1 
ATOM   3840 C CD2 . TYR B 1 207 ? -15.82400 1.73500   19.86400  1.000 38.39000 ? 209 TYR B CD2 1 
ATOM   3841 C CE1 . TYR B 1 207 ? -16.73400 3.17300   22.04300  1.000 43.43000 ? 209 TYR B CE1 1 
ATOM   3842 C CE2 . TYR B 1 207 ? -15.39800 1.40000   21.13500  1.000 41.07000 ? 209 TYR B CE2 1 
ATOM   3843 C CZ  . TYR B 1 207 ? -15.84800 2.11700   22.22100  1.000 47.36000 ? 209 TYR B CZ  1 
ATOM   3844 O OH  . TYR B 1 207 ? -15.40800 1.76500   23.48100  1.000 43.96000 ? 209 TYR B OH  1 
ATOM   3845 N N   . ALA B 1 208 ? -18.92900 3.25900   15.58500  1.000 38.35000 ? 210 ALA B N   1 
ATOM   3846 C CA  . ALA B 1 208 ? -19.53400 3.98600   14.47400  1.000 39.12000 ? 210 ALA B CA  1 
ATOM   3847 C C   . ALA B 1 208 ? -21.05100 3.84200   14.48000  1.000 40.88000 ? 210 ALA B C   1 
ATOM   3848 O O   . ALA B 1 208 ? -21.77600 4.79100   14.14900  1.000 40.79000 ? 210 ALA B O   1 
ATOM   3849 C CB  . ALA B 1 208 ? -18.96400 3.49100   13.14800  1.000 35.12000 ? 210 ALA B CB  1 
ATOM   3850 N N   . ALA B 1 209 ? -21.55300 2.65600   14.83400  1.000 39.62000 ? 211 ALA B N   1 
ATOM   3851 C CA  . ALA B 1 209 ? -22.99900 2.47500   14.94100  1.000 40.15000 ? 211 ALA B CA  1 
ATOM   3852 C C   . ALA B 1 209 ? -23.58700 3.38300   16.01500  1.000 42.49000 ? 211 ALA B C   1 
ATOM   3853 O O   . ALA B 1 209 ? -24.59100 4.06700   15.78600  1.000 40.21000 ? 211 ALA B O   1 
ATOM   3854 C CB  . ALA B 1 209 ? -23.33100 1.01700   15.24300  1.000 38.68000 ? 211 ALA B CB  1 
ATOM   3855 N N   . VAL B 1 210 ? -22.97200 3.39200   17.20200  1.000 40.58000 ? 212 VAL B N   1 
ATOM   3856 C CA  . VAL B 1 210 ? -23.44800 4.24100   18.29200  1.000 43.65000 ? 212 VAL B CA  1 
ATOM   3857 C C   . VAL B 1 210 ? -23.38300 5.71100   17.89200  1.000 44.18000 ? 212 VAL B C   1 
ATOM   3858 O O   . VAL B 1 210 ? -24.30000 6.48700   18.18200  1.000 47.68000 ? 212 VAL B O   1 
ATOM   3859 C CB  . VAL B 1 210 ? -22.64000 3.97100   19.57700  1.000 43.75000 ? 212 VAL B CB  1 
ATOM   3860 C CG1 . VAL B 1 210 ? -22.97200 5.02100   20.64700  1.000 44.10000 ? 212 VAL B CG1 1 
ATOM   3861 C CG2 . VAL B 1 210 ? -22.91900 2.57700   20.09700  1.000 39.02000 ? 212 VAL B CG2 1 
ATOM   3862 N N   . ILE B 1 211 ? -22.30000 6.11500   17.22300  1.000 42.20000 ? 213 ILE B N   1 
ATOM   3863 C CA  . ILE B 1 211 ? -22.15400 7.50100   16.78300  1.000 43.27000 ? 213 ILE B CA  1 
ATOM   3864 C C   . ILE B 1 211 ? -23.32700 7.89900   15.89600  1.000 47.64000 ? 213 ILE B C   1 
ATOM   3865 O O   . ILE B 1 211 ? -23.82700 9.03000   15.96700  1.000 48.28000 ? 213 ILE B O   1 
ATOM   3866 C CB  . ILE B 1 211 ? -20.79900 7.69000   16.07400  1.000 41.55000 ? 213 ILE B CB  1 
ATOM   3867 C CG1 . ILE B 1 211 ? -19.66800 7.66500   17.10200  1.000 43.63000 ? 213 ILE B CG1 1 
ATOM   3868 C CG2 . ILE B 1 211 ? -20.76300 8.99100   15.28400  1.000 46.71000 ? 213 ILE B CG2 1 
ATOM   3869 C CD1 . ILE B 1 211 ? -18.29200 7.85000   16.51800  1.000 44.31000 ? 213 ILE B CD1 1 
ATOM   3870 N N   . ASN B 1 212 ? -23.80400 6.97100   15.07400  1.000 42.94000 ? 214 ASN B N   1 
ATOM   3871 C CA  . ASN B 1 212 ? -25.02100 7.19300   14.30700  1.000 44.68000 ? 214 ASN B CA  1 
ATOM   3872 C C   . ASN B 1 212 ? -26.23000 6.80600   15.16000  1.000 45.15000 ? 214 ASN B C   1 
ATOM   3873 O O   . ASN B 1 212 ? -26.21200 6.97700   16.38100  1.000 50.04000 ? 214 ASN B O   1 
ATOM   3874 C CB  . ASN B 1 212 ? -24.95800 6.40700   12.99300  1.000 43.95000 ? 214 ASN B CB  1 
ATOM   3875 C CG  . ASN B 1 212 ? -23.88200 6.93500   12.04300  1.000 50.32000 ? 214 ASN B CG  1 
ATOM   3876 O OD1 . ASN B 1 212 ? -22.67700 6.84700   12.32100  1.000 53.89000 ? 214 ASN B OD1 1 
ATOM   3877 N ND2 . ASN B 1 212 ? -24.31400 7.50300   10.92100  1.000 53.24000 ? 214 ASN B ND2 1 
ATOM   3878 N N   . GLY B 1 213 ? -27.27800 6.26200   14.55300  1.000 48.58000 ? 215 GLY B N   1 
ATOM   3879 C CA  . GLY B 1 213 ? -28.49700 6.00900   15.31200  1.000 55.07000 ? 215 GLY B CA  1 
ATOM   3880 C C   . GLY B 1 213 ? -28.40500 4.87100   16.32000  1.000 52.53000 ? 215 GLY B C   1 
ATOM   3881 O O   . GLY B 1 213 ? -28.95200 4.96900   17.42400  1.000 50.78000 ? 215 GLY B O   1 
ATOM   3882 N N   . ASP B 1 214 ? -27.70700 3.78700   15.96900  1.000 49.72000 ? 216 ASP B N   1 
ATOM   3883 C CA  . ASP B 1 214 ? -27.99000 2.46900   16.54000  1.000 49.34000 ? 216 ASP B CA  1 
ATOM   3884 C C   . ASP B 1 214 ? -27.30800 2.23900   17.88700  1.000 48.93000 ? 216 ASP B C   1 
ATOM   3885 O O   . ASP B 1 214 ? -26.08000 2.14400   17.96300  1.000 50.44000 ? 216 ASP B O   1 
ATOM   3886 C CB  . ASP B 1 214 ? -27.58100 1.38900   15.54400  1.000 51.81000 ? 216 ASP B CB  1 
ATOM   3887 C CG  . ASP B 1 214 ? -28.46600 1.37300   14.32300  1.000 55.83000 ? 216 ASP B CG  1 
ATOM   3888 O OD1 . ASP B 1 214 ? -28.99900 2.44800   13.97100  1.000 63.97000 ? 216 ASP B OD1 1 
ATOM   3889 O OD2 . ASP B 1 214 ? -28.65600 0.29900   13.72800  1.000 58.53000 ? 216 ASP B OD2 1 
ATOM   3890 N N   . ARG B 1 215 ? -28.11900 2.08000   18.94000  1.000 47.34000 ? 217 ARG B N   1 
ATOM   3891 C CA  . ARG B 1 215 ? -27.62800 1.88500   20.29800  1.000 48.69000 ? 217 ARG B CA  1 
ATOM   3892 C C   . ARG B 1 215 ? -28.24600 0.67500   20.98800  1.000 49.00000 ? 217 ARG B C   1 
ATOM   3893 O O   . ARG B 1 215 ? -28.04100 0.50100   22.19400  1.000 51.79000 ? 217 ARG B O   1 
ATOM   3894 C CB  . ARG B 1 215 ? -27.89300 3.12200   21.17200  1.000 50.92000 ? 217 ARG B CB  1 
ATOM   3895 C CG  . ARG B 1 215 ? -27.39500 4.44000   20.61900  1.000 52.41000 ? 217 ARG B CG  1 
ATOM   3896 C CD  . ARG B 1 215 ? -27.69100 5.58100   21.58700  1.000 56.81000 ? 217 ARG B CD  1 
ATOM   3897 N NE  . ARG B 1 215 ? -27.09500 5.38000   22.91000  1.000 57.52000 ? 217 ARG B NE  1 
ATOM   3898 C CZ  . ARG B 1 215 ? -26.03200 6.04300   23.36700  1.000 56.45000 ? 217 ARG B CZ  1 
ATOM   3899 N NH1 . ARG B 1 215 ? -25.56900 5.79700   24.58800  1.000 58.91000 ? 217 ARG B NH1 1 
ATOM   3900 N NH2 . ARG B 1 215 ? -25.42500 6.94900   22.60900  1.000 53.58000 ? 217 ARG B NH2 1 
ATOM   3901 N N   . TRP B 1 216 ? -29.00900 -0.15400  20.27400  1.000 45.92000 ? 218 TRP B N   1 
ATOM   3902 C CA  . TRP B 1 216 ? -29.79400 -1.18200  20.94500  1.000 48.37000 ? 218 TRP B CA  1 
ATOM   3903 C C   . TRP B 1 216 ? -28.93100 -2.28100  21.55400  1.000 49.55000 ? 218 TRP B C   1 
ATOM   3904 O O   . TRP B 1 216 ? -29.39000 -2.96500  22.47600  1.000 48.86000 ? 218 TRP B O   1 
ATOM   3905 C CB  . TRP B 1 216 ? -30.80800 -1.79400  19.97000  1.000 45.17000 ? 218 TRP B CB  1 
ATOM   3906 C CG  . TRP B 1 216 ? -30.18100 -2.51400  18.82600  1.000 48.26000 ? 218 TRP B CG  1 
ATOM   3907 C CD1 . TRP B 1 216 ? -30.01700 -2.04300  17.55700  1.000 47.84000 ? 218 TRP B CD1 1 
ATOM   3908 C CD2 . TRP B 1 216 ? -29.61700 -3.83500  18.84200  1.000 49.53000 ? 218 TRP B CD2 1 
ATOM   3909 N NE1 . TRP B 1 216 ? -29.39200 -2.99300  16.77800  1.000 50.56000 ? 218 TRP B NE1 1 
ATOM   3910 C CE2 . TRP B 1 216 ? -29.14000 -4.10100  17.54400  1.000 50.42000 ? 218 TRP B CE2 1 
ATOM   3911 C CE3 . TRP B 1 216 ? -29.48200 -4.82300  19.82400  1.000 50.98000 ? 218 TRP B CE3 1 
ATOM   3912 C CZ2 . TRP B 1 216 ? -28.52900 -5.31100  17.20600  1.000 52.37000 ? 218 TRP B CZ2 1 
ATOM   3913 C CZ3 . TRP B 1 216 ? -28.86800 -6.02100  19.48600  1.000 51.89000 ? 218 TRP B CZ3 1 
ATOM   3914 C CH2 . TRP B 1 216 ? -28.40600 -6.25600  18.18900  1.000 49.72000 ? 218 TRP B CH2 1 
ATOM   3915 N N   . PHE B 1 217 ? -27.70500 -2.47700  21.05200  1.000 47.79000 ? 219 PHE B N   1 
ATOM   3916 C CA  . PHE B 1 217 ? -26.82900 -3.55100  21.51000  1.000 45.31000 ? 219 PHE B CA  1 
ATOM   3917 C C   . PHE B 1 217 ? -26.03900 -3.18300  22.75600  1.000 48.57000 ? 219 PHE B C   1 
ATOM   3918 O O   . PHE B 1 217 ? -25.32700 -4.03800  23.29100  1.000 46.36000 ? 219 PHE B O   1 
ATOM   3919 C CB  . PHE B 1 217 ? -25.85500 -3.94400  20.39200  1.000 46.93000 ? 219 PHE B CB  1 
ATOM   3920 C CG  . PHE B 1 217 ? -25.15100 -2.77000  19.77200  1.000 43.72000 ? 219 PHE B CG  1 
ATOM   3921 C CD1 . PHE B 1 217 ? -24.07100 -2.17000  20.41500  1.000 43.85000 ? 219 PHE B CD1 1 
ATOM   3922 C CD2 . PHE B 1 217 ? -25.58200 -2.24400  18.56200  1.000 44.66000 ? 219 PHE B CD2 1 
ATOM   3923 C CE1 . PHE B 1 217 ? -23.42600 -1.06600  19.85600  1.000 43.28000 ? 219 PHE B CE1 1 
ATOM   3924 C CE2 . PHE B 1 217 ? -24.94700 -1.14400  17.99500  1.000 40.37000 ? 219 PHE B CE2 1 
ATOM   3925 C CZ  . PHE B 1 217 ? -23.86100 -0.55600  18.64000  1.000 40.22000 ? 219 PHE B CZ  1 
ATOM   3926 N N   . LEU B 1 218 ? -26.11200 -1.93600  23.21400  1.000 49.65000 ? 220 LEU B N   1 
ATOM   3927 C CA  . LEU B 1 218 ? -25.39000 -1.56200  24.41700  1.000 51.39000 ? 220 LEU B CA  1 
ATOM   3928 C C   . LEU B 1 218 ? -26.13500 -2.02600  25.66000  1.000 53.89000 ? 220 LEU B C   1 
ATOM   3929 O O   . LEU B 1 218 ? -27.36800 -2.10900  25.68100  1.000 50.80000 ? 220 LEU B O   1 
ATOM   3930 C CB  . LEU B 1 218 ? -25.18200 -0.05700  24.48400  1.000 48.28000 ? 220 LEU B CB  1 
ATOM   3931 C CG  . LEU B 1 218 ? -24.60300 0.59200   23.23400  1.000 53.01000 ? 220 LEU B CG  1 
ATOM   3932 C CD1 . LEU B 1 218 ? -24.99400 2.04800   23.19700  1.000 48.97000 ? 220 LEU B CD1 1 
ATOM   3933 C CD2 . LEU B 1 218 ? -23.08800 0.42100   23.21100  1.000 48.99000 ? 220 LEU B CD2 1 
ATOM   3934 N N   . ASN B 1 219 ? -25.36800 -2.30900  26.71300  1.000 54.59000 ? 221 ASN B N   1 
ATOM   3935 C CA  . ASN B 1 219 ? -25.93500 -2.71400  27.98800  1.000 54.30000 ? 221 ASN B CA  1 
ATOM   3936 C C   . ASN B 1 219 ? -25.22800 -1.96900  29.11800  1.000 56.32000 ? 221 ASN B C   1 
ATOM   3937 O O   . ASN B 1 219 ? -24.38200 -1.09300  28.89600  1.000 50.26000 ? 221 ASN B O   1 
ATOM   3938 C CB  . ASN B 1 219 ? -25.85000 -4.23300  28.16700  1.000 51.63000 ? 221 ASN B CB  1 
ATOM   3939 C CG  . ASN B 1 219 ? -24.46300 -4.77900  27.88400  1.000 50.95000 ? 221 ASN B CG  1 
ATOM   3940 O OD1 . ASN B 1 219 ? -23.46000 -4.11400  28.12100  1.000 53.23000 ? 221 ASN B OD1 1 
ATOM   3941 N ND2 . ASN B 1 219 ? -24.40400 -6.00400  27.38000  1.000 52.06000 ? 221 ASN B ND2 1 
ATOM   3942 N N   . ARG B 1 220 ? -25.59100 -2.33100  30.34600  1.000 55.92000 ? 222 ARG B N   1 
ATOM   3943 C CA  . ARG B 1 220 ? -25.03800 -1.73000  31.55100  1.000 52.21000 ? 222 ARG B CA  1 
ATOM   3944 C C   . ARG B 1 220 ? -23.75600 -2.40500  32.02900  1.000 54.10000 ? 222 ARG B C   1 
ATOM   3945 O O   . ARG B 1 220 ? -23.15500 -1.93100  33.00300  1.000 52.50000 ? 222 ARG B O   1 
ATOM   3946 C CB  . ARG B 1 220 ? -26.08800 -1.79700  32.66400  1.000 51.23000 ? 222 ARG B CB  1 
ATOM   3947 C CG  . ARG B 1 220 ? -26.66000 -3.21400  32.79100  1.000 52.18000 ? 222 ARG B CG  1 
ATOM   3948 C CD  . ARG B 1 220 ? -26.95900 -3.62100  34.23200  1.000 51.34000 ? 222 ARG B CD  1 
ATOM   3949 N NE  . ARG B 1 220 ? -27.59000 -2.56300  35.01300  1.000 47.74000 ? 222 ARG B NE  1 
ATOM   3950 C CZ  . ARG B 1 220 ? -28.86500 -2.22600  34.89700  1.000 47.30000 ? 222 ARG B CZ  1 
ATOM   3951 N NH1 . ARG B 1 220 ? -29.64200 -2.86300  34.02500  1.000 52.37000 ? 222 ARG B NH1 1 
ATOM   3952 N NH2 . ARG B 1 220 ? -29.36400 -1.26200  35.65400  1.000 50.08000 ? 222 ARG B NH2 1 
ATOM   3953 N N   . PHE B 1 221 ? -23.32600 -3.48700  31.38400  1.000 50.14000 ? 223 PHE B N   1 
ATOM   3954 C CA  . PHE B 1 221 ? -22.29800 -4.36400  31.92800  1.000 52.80000 ? 223 PHE B CA  1 
ATOM   3955 C C   . PHE B 1 221 ? -20.91200 -4.03600  31.37800  1.000 58.57000 ? 223 PHE B C   1 
ATOM   3956 O O   . PHE B 1 221 ? -20.74500 -3.25100  30.43900  1.000 56.93000 ? 223 PHE B O   1 
ATOM   3957 C CB  . PHE B 1 221 ? -22.64600 -5.82900  31.64100  1.000 49.56000 ? 223 PHE B CB  1 
ATOM   3958 C CG  . PHE B 1 221 ? -24.01600 -6.23200  32.13500  1.000 52.05000 ? 223 PHE B CG  1 
ATOM   3959 C CD1 . PHE B 1 221 ? -24.29700 -6.25600  33.49700  1.000 46.39000 ? 223 PHE B CD1 1 
ATOM   3960 C CD2 . PHE B 1 221 ? -25.02700 -6.56100  31.23800  1.000 50.42000 ? 223 PHE B CD2 1 
ATOM   3961 C CE1 . PHE B 1 221 ? -25.55200 -6.61800  33.95600  1.000 47.40000 ? 223 PHE B CE1 1 
ATOM   3962 C CE2 . PHE B 1 221 ? -26.28700 -6.92300  31.68900  1.000 46.17000 ? 223 PHE B CE2 1 
ATOM   3963 C CZ  . PHE B 1 221 ? -26.55500 -6.94900  33.04900  1.000 46.67000 ? 223 PHE B CZ  1 
ATOM   3964 N N   . THR B 1 222 ? -19.90800 -4.64700  32.00900  1.000 53.71000 ? 224 THR B N   1 
ATOM   3965 C CA  . THR B 1 222 ? -18.51900 -4.61000  31.58100  1.000 52.40000 ? 224 THR B CA  1 
ATOM   3966 C C   . THR B 1 222 ? -17.97500 -6.03300  31.68400  1.000 55.43000 ? 224 THR B C   1 
ATOM   3967 O O   . THR B 1 222 ? -18.52700 -6.87700  32.39700  1.000 55.81000 ? 224 THR B O   1 
ATOM   3968 C CB  . THR B 1 222 ? -17.69600 -3.60600  32.43400  1.000 56.51000 ? 224 THR B CB  1 
ATOM   3969 O OG1 . THR B 1 222 ? -18.03700 -2.26800  32.06200  1.000 58.66000 ? 224 THR B OG1 1 
ATOM   3970 C CG2 . THR B 1 222 ? -16.19900 -3.76500  32.24000  1.000 54.53000 ? 224 THR B CG2 1 
ATOM   3971 N N   . THR B 1 223 ? -16.92300 -6.31500  30.92500  1.000 55.12000 ? 225 THR B N   1 
ATOM   3972 C CA  . THR B 1 223 ? -16.22900 -7.59500  30.96100  1.000 49.10000 ? 225 THR B CA  1 
ATOM   3973 C C   . THR B 1 223 ? -14.78400 -7.35700  31.40100  1.000 54.98000 ? 225 THR B C   1 
ATOM   3974 O O   . THR B 1 223 ? -14.41100 -6.25500  31.81900  1.000 54.80000 ? 225 THR B O   1 
ATOM   3975 C CB  . THR B 1 223 ? -16.32200 -8.27900  29.59300  1.000 48.44000 ? 225 THR B CB  1 
ATOM   3976 O OG1 . THR B 1 223 ? -15.92000 -9.65100  29.69900  1.000 55.05000 ? 225 THR B OG1 1 
ATOM   3977 C CG2 . THR B 1 223 ? -15.44800 -7.55400  28.57100  1.000 53.91000 ? 225 THR B CG2 1 
ATOM   3978 N N   . THR B 1 224 ? -13.96400 -8.40100  31.32700  1.000 52.29000 ? 226 THR B N   1 
ATOM   3979 C CA  . THR B 1 224 ? -12.52900 -8.22200  31.46900  1.000 55.49000 ? 226 THR B CA  1 
ATOM   3980 C C   . THR B 1 224 ? -11.84400 -8.63200  30.17200  1.000 49.01000 ? 226 THR B C   1 
ATOM   3981 O O   . THR B 1 224 ? -12.39200 -9.38900  29.36300  1.000 47.61000 ? 226 THR B O   1 
ATOM   3982 C CB  . THR B 1 224 ? -11.95200 -9.00900  32.66100  1.000 51.22000 ? 226 THR B CB  1 
ATOM   3983 O OG1 . THR B 1 224 ? -12.26200 -10.40400 32.53400  1.000 54.02000 ? 226 THR B OG1 1 
ATOM   3984 C CG2 . THR B 1 224 ? -12.51500 -8.47300  33.96200  1.000 51.92000 ? 226 THR B CG2 1 
ATOM   3985 N N   . LEU B 1 225 ? -10.64400 -8.08400  29.97200  1.000 52.32000 ? 227 LEU B N   1 
ATOM   3986 C CA  . LEU B 1 225 ? -9.84100  -8.46600  28.81500  1.000 50.65000 ? 227 LEU B CA  1 
ATOM   3987 C C   . LEU B 1 225 ? -9.67300  -9.98300  28.74000  1.000 50.23000 ? 227 LEU B C   1 
ATOM   3988 O O   . LEU B 1 225 ? -9.86300  -10.58500 27.67700  1.000 48.93000 ? 227 LEU B O   1 
ATOM   3989 C CB  . LEU B 1 225 ? -8.48500  -7.76200  28.87000  1.000 52.10000 ? 227 LEU B CB  1 
ATOM   3990 C CG  . LEU B 1 225 ? -7.75400  -7.53200  27.54200  1.000 52.07000 ? 227 LEU B CG  1 
ATOM   3991 C CD1 . LEU B 1 225 ? -8.71800  -7.11200  26.43400  1.000 48.65000 ? 227 LEU B CD1 1 
ATOM   3992 C CD2 . LEU B 1 225 ? -6.65100  -6.49200  27.71500  1.000 50.46000 ? 227 LEU B CD2 1 
ATOM   3993 N N   . ASN B 1 226 ? -9.37400  -10.62400 29.87400  1.000 51.80000 ? 228 ASN B N   1 
ATOM   3994 C CA  . ASN B 1 226 ? -9.20600  -12.07700 29.88600  1.000 51.77000 ? 228 ASN B CA  1 
ATOM   3995 C C   . ASN B 1 226 ? -10.51700 -12.79300 29.57000  1.000 50.24000 ? 228 ASN B C   1 
ATOM   3996 O O   . ASN B 1 226 ? -10.54900 -13.70800 28.73900  1.000 50.20000 ? 228 ASN B O   1 
ATOM   3997 C CB  . ASN B 1 226 ? -8.66000  -12.54000 31.24000  1.000 54.28000 ? 228 ASN B CB  1 
ATOM   3998 C CG  . ASN B 1 226 ? -7.29600  -11.95200 31.55800  1.000 58.87000 ? 228 ASN B CG  1 
ATOM   3999 O OD1 . ASN B 1 226 ? -6.52600  -11.60700 30.65900  1.000 59.36000 ? 228 ASN B OD1 1 
ATOM   4000 N ND2 . ASN B 1 226 ? -6.98600  -11.84600 32.84700  1.000 61.63000 ? 228 ASN B ND2 1 
ATOM   4001 N N   . ASP B 1 227 ? -11.61100 -12.38900 30.22500  1.000 53.77000 ? 229 ASP B N   1 
ATOM   4002 C CA  . ASP B 1 227 ? -12.90600 -13.02500 29.98400  1.000 52.68000 ? 229 ASP B CA  1 
ATOM   4003 C C   . ASP B 1 227 ? -13.33600 -12.87600 28.53300  1.000 49.31000 ? 229 ASP B C   1 
ATOM   4004 O O   . ASP B 1 227 ? -13.89100 -13.80900 27.93800  1.000 46.69000 ? 229 ASP B O   1 
ATOM   4005 C CB  . ASP B 1 227 ? -13.97300 -12.41700 30.89400  1.000 55.85000 ? 229 ASP B CB  1 
ATOM   4006 C CG  . ASP B 1 227 ? -13.90900 -12.94700 32.30800  1.000 58.12000 ? 229 ASP B CG  1 
ATOM   4007 O OD1 . ASP B 1 227 ? -13.52500 -14.11900 32.48700  1.000 60.44000 ? 229 ASP B OD1 1 
ATOM   4008 O OD2 . ASP B 1 227 ? -14.24500 -12.18300 33.23700  1.000 60.96000 ? 229 ASP B OD2 1 
ATOM   4009 N N   . PHE B 1 228 ? -13.11700 -11.69500 27.95400  1.000 50.42000 ? 230 PHE B N   1 
ATOM   4010 C CA  . PHE B 1 228 ? -13.55700 -11.47300 26.58200  1.000 47.92000 ? 230 PHE B CA  1 
ATOM   4011 C C   . PHE B 1 228 ? -12.73300 -12.29800 25.60100  1.000 46.12000 ? 230 PHE B C   1 
ATOM   4012 O O   . PHE B 1 228 ? -13.28000 -12.89600 24.66800  1.000 46.27000 ? 230 PHE B O   1 
ATOM   4013 C CB  . PHE B 1 228 ? -13.48000 -9.98900  26.22900  1.000 46.27000 ? 230 PHE B CB  1 
ATOM   4014 C CG  . PHE B 1 228 ? -13.77200 -9.71900  24.78700  1.000 47.08000 ? 230 PHE B CG  1 
ATOM   4015 C CD1 . PHE B 1 228 ? -15.07800 -9.72100  24.32300  1.000 45.47000 ? 230 PHE B CD1 1 
ATOM   4016 C CD2 . PHE B 1 228 ? -12.74100 -9.51900  23.88300  1.000 47.26000 ? 230 PHE B CD2 1 
ATOM   4017 C CE1 . PHE B 1 228 ? -15.35100 -9.50700  22.99300  1.000 44.25000 ? 230 PHE B CE1 1 
ATOM   4018 C CE2 . PHE B 1 228 ? -13.00800 -9.30700  22.54800  1.000 45.94000 ? 230 PHE B CE2 1 
ATOM   4019 C CZ  . PHE B 1 228 ? -14.31200 -9.29900  22.10000  1.000 43.67000 ? 230 PHE B CZ  1 
ATOM   4020 N N   . ASN B 1 229 ? -11.41700 -12.35600 25.80400  1.000 48.54000 ? 231 ASN B N   1 
ATOM   4021 C CA  . ASN B 1 229 ? -10.57600 -13.12400 24.89200  1.000 43.51000 ? 231 ASN B CA  1 
ATOM   4022 C C   . ASN B 1 229 ? -10.91000 -14.60600 24.94100  1.000 47.88000 ? 231 ASN B C   1 
ATOM   4023 O O   . ASN B 1 229 ? -10.75100 -15.31500 23.93900  1.000 45.33000 ? 231 ASN B O   1 
ATOM   4024 C CB  . ASN B 1 229 ? -9.10800  -12.86900 25.21100  1.000 45.90000 ? 231 ASN B CB  1 
ATOM   4025 C CG  . ASN B 1 229 ? -8.64200  -11.52200 24.69400  1.000 47.76000 ? 231 ASN B CG  1 
ATOM   4026 O OD1 . ASN B 1 229 ? -8.99400  -11.12600 23.58000  1.000 45.73000 ? 231 ASN B OD1 1 
ATOM   4027 N ND2 . ASN B 1 229 ? -7.86700  -10.80200 25.50100  1.000 49.82000 ? 231 ASN B ND2 1 
ATOM   4028 N N   . LEU B 1 230 ? -11.40700 -15.09100 26.07800  1.000 45.18000 ? 232 LEU B N   1 
ATOM   4029 C CA  . LEU B 1 230 ? -11.89700 -16.46100 26.10800  1.000 47.83000 ? 232 LEU B CA  1 
ATOM   4030 C C   . LEU B 1 230 ? -13.06400 -16.65100 25.14900  1.000 46.40000 ? 232 LEU B C   1 
ATOM   4031 O O   . LEU B 1 230 ? -13.19600 -17.70800 24.52100  1.000 43.40000 ? 232 LEU B O   1 
ATOM   4032 C CB  . LEU B 1 230 ? -12.29800 -16.84700 27.52700  1.000 52.90000 ? 232 LEU B CB  1 
ATOM   4033 C CG  . LEU B 1 230 ? -11.75100 -18.21700 27.90100  1.000 58.05000 ? 232 LEU B CG  1 
ATOM   4034 C CD1 . LEU B 1 230 ? -10.24300 -18.25100 27.61100  1.000 53.92000 ? 232 LEU B CD1 1 
ATOM   4035 C CD2 . LEU B 1 230 ? -12.05500 -18.52300 29.35900  1.000 55.92000 ? 232 LEU B CD2 1 
ATOM   4036 N N   . VAL B 1 231 ? -13.92500 -15.63900 25.02100  1.000 47.31000 ? 233 VAL B N   1 
ATOM   4037 C CA  . VAL B 1 231 ? -15.01600 -15.72800 24.05500  1.000 48.50000 ? 233 VAL B CA  1 
ATOM   4038 C C   . VAL B 1 231 ? -14.48900 -15.50200 22.64300  1.000 44.24000 ? 233 VAL B C   1 
ATOM   4039 O O   . VAL B 1 231 ? -14.89800 -16.18300 21.69300  1.000 45.40000 ? 233 VAL B O   1 
ATOM   4040 C CB  . VAL B 1 231 ? -16.13400 -14.72800 24.41500  1.000 52.11000 ? 233 VAL B CB  1 
ATOM   4041 C CG1 . VAL B 1 231 ? -17.31600 -14.88500 23.47100  1.000 51.50000 ? 233 VAL B CG1 1 
ATOM   4042 C CG2 . VAL B 1 231 ? -16.57700 -14.92400 25.85900  1.000 53.68000 ? 233 VAL B CG2 1 
ATOM   4043 N N   . ALA B 1 232 ? -13.57700 -14.53800 22.48400  1.000 45.47000 ? 234 ALA B N   1 
ATOM   4044 C CA  . ALA B 1 232 ? -12.95800 -14.28700 21.18500  1.000 44.90000 ? 234 ALA B CA  1 
ATOM   4045 C C   . ALA B 1 232 ? -12.36000 -15.56200 20.60000  1.000 45.27000 ? 234 ALA B C   1 
ATOM   4046 O O   . ALA B 1 232 ? -12.53900 -15.85800 19.41300  1.000 44.15000 ? 234 ALA B O   1 
ATOM   4047 C CB  . ALA B 1 232 ? -11.88500 -13.20200 21.31500  1.000 42.83000 ? 234 ALA B CB  1 
ATOM   4048 N N   . MET B 1 233 ? -11.66100 -16.34200 21.42900  1.000 45.49000 ? 235 MET B N   1 
ATOM   4049 C CA  . MET B 1 233 ? -11.07200 -17.58100 20.93400  1.000 44.81000 ? 235 MET B CA  1 
ATOM   4050 C C   . MET B 1 233 ? -12.14600 -18.54700 20.47100  1.000 45.32000 ? 235 MET B C   1 
ATOM   4051 O O   . MET B 1 233 ? -12.00900 -19.18000 19.41900  1.000 41.63000 ? 235 MET B O   1 
ATOM   4052 C CB  . MET B 1 233 ? -10.20000 -18.22800 22.00800  1.000 46.37000 ? 235 MET B CB  1 
ATOM   4053 C CG  . MET B 1 233 ? -9.07600  -19.07700 21.42900  1.000 56.44000 ? 235 MET B CG  1 
ATOM   4054 S SD  . MET B 1 233 ? -8.09200  -19.88100 22.70700  1.000 72.26000 ? 235 MET B SD  1 
ATOM   4055 C CE  . MET B 1 233 ? -8.09200  -18.61000 23.97600  1.000 50.82000 ? 235 MET B CE  1 
ATOM   4056 N N   . LYS B 1 234 ? -13.24300 -18.64400 21.22500  1.000 45.44000 ? 236 LYS B N   1 
ATOM   4057 C CA  . LYS B 1 234 ? -14.29900 -19.57900 20.86000  1.000 44.37000 ? 236 LYS B CA  1 
ATOM   4058 C C   . LYS B 1 234 ? -14.93400 -19.22400 19.52200  1.000 47.18000 ? 236 LYS B C   1 
ATOM   4059 O O   . LYS B 1 234 ? -15.34900 -20.11900 18.77500  1.000 46.42000 ? 236 LYS B O   1 
ATOM   4060 C CB  . LYS B 1 234 ? -15.35700 -19.62500 21.96100  1.000 46.02000 ? 236 LYS B CB  1 
ATOM   4061 C CG  . LYS B 1 234 ? -16.48800 -20.58500 21.68000  1.000 52.17000 ? 236 LYS B CG  1 
ATOM   4062 C CD  . LYS B 1 234 ? -17.47000 -20.64500 22.83500  1.000 56.37000 ? 236 LYS B CD  1 
ATOM   4063 C CE  . LYS B 1 234 ? -18.49900 -21.74900 22.62100  1.000 60.81000 ? 236 LYS B CE  1 
ATOM   4064 N NZ  . LYS B 1 234 ? -19.49500 -21.79700 23.73000  1.000 64.51000 ? 236 LYS B NZ  1 
ATOM   4065 N N   . TYR B 1 235 ? -15.01600 -17.93300 19.19600  1.000 47.51000 ? 237 TYR B N   1 
ATOM   4066 C CA  . TYR B 1 235 ? -15.67500 -17.49600 17.97400  1.000 46.31000 ? 237 TYR B CA  1 
ATOM   4067 C C   . TYR B 1 235 ? -14.69400 -17.16800 16.85400  1.000 41.82000 ? 237 TYR B C   1 
ATOM   4068 O O   . TYR B 1 235 ? -15.10100 -16.59300 15.84400  1.000 41.00000 ? 237 TYR B O   1 
ATOM   4069 C CB  . TYR B 1 235 ? -16.59200 -16.30700 18.28200  1.000 46.61000 ? 237 TYR B CB  1 
ATOM   4070 C CG  . TYR B 1 235 ? -17.78700 -16.75700 19.09200  1.000 47.07000 ? 237 TYR B CG  1 
ATOM   4071 C CD1 . TYR B 1 235 ? -18.89400 -17.32400 18.47400  1.000 49.01000 ? 237 TYR B CD1 1 
ATOM   4072 C CD2 . TYR B 1 235 ? -17.77700 -16.67900 20.47900  1.000 48.51000 ? 237 TYR B CD2 1 
ATOM   4073 C CE1 . TYR B 1 235 ? -19.98200 -17.77500 19.21700  1.000 52.27000 ? 237 TYR B CE1 1 
ATOM   4074 C CE2 . TYR B 1 235 ? -18.85800 -17.12500 21.23000  1.000 52.19000 ? 237 TYR B CE2 1 
ATOM   4075 C CZ  . TYR B 1 235 ? -19.95500 -17.67100 20.59300  1.000 53.01000 ? 237 TYR B CZ  1 
ATOM   4076 O OH  . TYR B 1 235 ? -21.02800 -18.11400 21.33600  1.000 56.92000 ? 237 TYR B OH  1 
ATOM   4077 N N   . ASN B 1 236 ? -13.43000 -17.57000 16.99500  1.000 42.91000 ? 238 ASN B N   1 
ATOM   4078 C CA  . ASN B 1 236 ? -12.38100 -17.30600 16.00900  1.000 43.30000 ? 238 ASN B CA  1 
ATOM   4079 C C   . ASN B 1 236 ? -12.28900 -15.81100 15.72300  1.000 41.72000 ? 238 ASN B C   1 
ATOM   4080 O O   . ASN B 1 236 ? -12.29700 -15.36300 14.57400  1.000 36.41000 ? 238 ASN B O   1 
ATOM   4081 C CB  . ASN B 1 236 ? -12.59800 -18.10700 14.72500  1.000 43.72000 ? 238 ASN B CB  1 
ATOM   4082 C CG  . ASN B 1 236 ? -12.22500 -19.55600 14.88700  1.000 49.61000 ? 238 ASN B CG  1 
ATOM   4083 O OD1 . ASN B 1 236 ? -13.09100 -20.42400 14.94400  1.000 56.42000 ? 238 ASN B OD1 1 
ATOM   4084 N ND2 . ASN B 1 236 ? -10.92900 -19.82700 14.98300  1.000 53.09000 ? 238 ASN B ND2 1 
ATOM   4085 N N   . TYR B 1 237 ? -12.24100 -15.04200 16.80000  1.000 38.21000 ? 239 TYR B N   1 
ATOM   4086 C CA  . TYR B 1 237 ? -11.95700 -13.62500 16.76200  1.000 40.53000 ? 239 TYR B CA  1 
ATOM   4087 C C   . TYR B 1 237 ? -10.52000 -13.44000 17.22000  1.000 40.26000 ? 239 TYR B C   1 
ATOM   4088 O O   . TYR B 1 237 ? -10.05900 -14.14300 18.12500  1.000 40.89000 ? 239 TYR B O   1 
ATOM   4089 C CB  . TYR B 1 237 ? -12.91900 -12.85800 17.67300  1.000 38.07000 ? 239 TYR B CB  1 
ATOM   4090 C CG  . TYR B 1 237 ? -14.14600 -12.31000 16.96900  1.000 36.51000 ? 239 TYR B CG  1 
ATOM   4091 C CD1 . TYR B 1 237 ? -14.99300 -13.14300 16.23900  1.000 39.34000 ? 239 TYR B CD1 1 
ATOM   4092 C CD2 . TYR B 1 237 ? -14.46800 -10.95400 17.05400  1.000 34.89000 ? 239 TYR B CD2 1 
ATOM   4093 C CE1 . TYR B 1 237 ? -16.13100 -12.62500 15.59100  1.000 36.79000 ? 239 TYR B CE1 1 
ATOM   4094 C CE2 . TYR B 1 237 ? -15.58600 -10.43800 16.42800  1.000 33.56000 ? 239 TYR B CE2 1 
ATOM   4095 C CZ  . TYR B 1 237 ? -16.41000 -11.26300 15.69900  1.000 35.28000 ? 239 TYR B CZ  1 
ATOM   4096 O OH  . TYR B 1 237 ? -17.51000 -10.71600 15.07800  1.000 37.20000 ? 239 TYR B OH  1 
ATOM   4097 N N   . GLU B 1 238 ? -9.81200  -12.51800 16.58100  1.000 37.14000 ? 240 GLU B N   1 
ATOM   4098 C CA  . GLU B 1 238 ? -8.47100  -12.19100 17.03300  1.000 37.18000 ? 240 GLU B CA  1 
ATOM   4099 C C   . GLU B 1 238 ? -8.51900  -11.75300 18.49300  1.000 41.86000 ? 240 GLU B C   1 
ATOM   4100 O O   . GLU B 1 238 ? -9.47700  -11.09200 18.91500  1.000 40.73000 ? 240 GLU B O   1 
ATOM   4101 C CB  . GLU B 1 238 ? -7.85900  -11.08100 16.17700  1.000 38.57000 ? 240 GLU B CB  1 
ATOM   4102 C CG  . GLU B 1 238 ? -7.43100  -11.53800 14.79600  1.000 41.71000 ? 240 GLU B CG  1 
ATOM   4103 C CD  . GLU B 1 238 ? -6.24600  -12.49300 14.84100  1.000 40.18000 ? 240 GLU B CD  1 
ATOM   4104 O OE1 . GLU B 1 238 ? -6.39900  -13.66100 14.42600  1.000 41.15000 ? 240 GLU B OE1 1 
ATOM   4105 O OE2 . GLU B 1 238 ? -5.16300  -12.06600 15.27900  1.000 47.49000 ? 240 GLU B OE2 1 
ATOM   4106 N N   . PRO B 1 239 ? -7.51700  -12.11100 19.29500  1.000 43.15000 ? 241 PRO B N   1 
ATOM   4107 C CA  . PRO B 1 239 ? -7.48800  -11.60700 20.67300  1.000 43.11000 ? 241 PRO B CA  1 
ATOM   4108 C C   . PRO B 1 239 ? -7.35200  -10.09100 20.68500  1.000 44.55000 ? 241 PRO B C   1 
ATOM   4109 O O   . PRO B 1 239 ? -6.81600  -9.47800  19.75400  1.000 40.66000 ? 241 PRO B O   1 
ATOM   4110 C CB  . PRO B 1 239 ? -6.26900  -12.30600 21.29600  1.000 45.61000 ? 241 PRO B CB  1 
ATOM   4111 C CG  . PRO B 1 239 ? -5.54000  -12.95600 20.17100  1.000 45.00000 ? 241 PRO B CG  1 
ATOM   4112 C CD  . PRO B 1 239 ? -6.47200  -13.11000 19.02000  1.000 40.39000 ? 241 PRO B CD  1 
ATOM   4113 N N   . LEU B 1 240 ? -7.90200  -9.48100  21.73400  1.000 44.82000 ? 242 LEU B N   1 
ATOM   4114 C CA  . LEU B 1 240 ? -7.88100  -8.03500  21.91200  1.000 41.35000 ? 242 LEU B CA  1 
ATOM   4115 C C   . LEU B 1 240 ? -6.76900  -7.67700  22.87900  1.000 40.31000 ? 242 LEU B C   1 
ATOM   4116 O O   . LEU B 1 240 ? -6.67500  -8.25900  23.96300  1.000 43.28000 ? 242 LEU B O   1 
ATOM   4117 C CB  . LEU B 1 240 ? -9.21800  -7.53100  22.45200  1.000 41.71000 ? 242 LEU B CB  1 
ATOM   4118 C CG  . LEU B 1 240 ? -9.43500  -6.01900  22.37400  1.000 41.51000 ? 242 LEU B CG  1 
ATOM   4119 C CD1 . LEU B 1 240 ? -9.72400  -5.63000  20.93400  1.000 36.53000 ? 242 LEU B CD1 1 
ATOM   4120 C CD2 . LEU B 1 240 ? -10.57500 -5.59400  23.28500  1.000 41.12000 ? 242 LEU B CD2 1 
ATOM   4121 N N   . THR B 1 241 ? -5.93900  -6.71900  22.49700  1.000 40.05000 ? 243 THR B N   1 
ATOM   4122 C CA  . THR B 1 241 ? -4.77300  -6.35900  23.28600  1.000 44.78000 ? 243 THR B CA  1 
ATOM   4123 C C   . THR B 1 241 ? -4.93900  -4.97300  23.89000  1.000 47.97000 ? 243 THR B C   1 
ATOM   4124 O O   . THR B 1 241 ? -5.72100  -4.14400  23.41200  1.000 45.55000 ? 243 THR B O   1 
ATOM   4125 C CB  . THR B 1 241 ? -3.50000  -6.40200  22.43200  1.000 44.95000 ? 243 THR B CB  1 
ATOM   4126 O OG1 . THR B 1 241 ? -3.40600  -5.20000  21.65600  1.000 45.09000 ? 243 THR B OG1 1 
ATOM   4127 C CG2 . THR B 1 241 ? -3.52200  -7.61800  21.50500  1.000 43.19000 ? 243 THR B CG2 1 
ATOM   4128 N N   . GLN B 1 242 ? -4.17500  -4.72700  24.95600  1.000 47.20000 ? 244 GLN B N   1 
ATOM   4129 C CA  . GLN B 1 242 ? -4.17200  -3.40600  25.56900  1.000 48.56000 ? 244 GLN B CA  1 
ATOM   4130 C C   . GLN B 1 242 ? -3.90700  -2.31400  24.54200  1.000 51.53000 ? 244 GLN B C   1 
ATOM   4131 O O   . GLN B 1 242 ? -4.42800  -1.19700  24.67000  1.000 49.31000 ? 244 GLN B O   1 
ATOM   4132 C CB  . GLN B 1 242 ? -3.12900  -3.34500  26.68200  1.000 49.38000 ? 244 GLN B CB  1 
ATOM   4133 C CG  . GLN B 1 242 ? -3.14400  -2.02500  27.41800  1.000 51.23000 ? 244 GLN B CG  1 
ATOM   4134 C CD  . GLN B 1 242 ? -4.52800  -1.69600  27.93500  1.000 48.90000 ? 244 GLN B CD  1 
ATOM   4135 O OE1 . GLN B 1 242 ? -5.17500  -2.53200  28.55700  1.000 49.43000 ? 244 GLN B OE1 1 
ATOM   4136 N NE2 . GLN B 1 242 ? -4.99100  -0.47800  27.67700  1.000 50.80000 ? 244 GLN B NE2 1 
ATOM   4137 N N   . ASP B 1 243 ? -3.12300  -2.62000  23.50400  1.000 50.10000 ? 245 ASP B N   1 
ATOM   4138 C CA  . ASP B 1 243 ? -2.88500  -1.62600  22.46300  1.000 50.65000 ? 245 ASP B CA  1 
ATOM   4139 C C   . ASP B 1 243 ? -4.16300  -1.32200  21.69100  1.000 49.49000 ? 245 ASP B C   1 
ATOM   4140 O O   . ASP B 1 243 ? -4.47000  -0.15300  21.43100  1.000 52.10000 ? 245 ASP B O   1 
ATOM   4141 C CB  . ASP B 1 243 ? -1.78100  -2.10000  21.51600  1.000 52.28000 ? 245 ASP B CB  1 
ATOM   4142 C CG  . ASP B 1 243 ? -1.31400  -1.00200  20.57300  1.000 56.79000 ? 245 ASP B CG  1 
ATOM   4143 O OD1 . ASP B 1 243 ? -1.56700  0.19200   20.87000  1.000 60.95000 ? 245 ASP B OD1 1 
ATOM   4144 O OD2 . ASP B 1 243 ? -0.69100  -1.32600  19.53800  1.000 62.19000 ? 245 ASP B OD2 1 
ATOM   4145 N N   . HIS B 1 244 ? -4.91900  -2.36000  21.32200  1.000 47.53000 ? 246 HIS B N   1 
ATOM   4146 C CA  . HIS B 1 244 ? -6.22800  -2.15900  20.70900  1.000 45.51000 ? 246 HIS B CA  1 
ATOM   4147 C C   . HIS B 1 244 ? -7.09900  -1.25800  21.57100  1.000 47.85000 ? 246 HIS B C   1 
ATOM   4148 O O   . HIS B 1 244 ? -7.69500  -0.29000  21.08200  1.000 44.27000 ? 246 HIS B O   1 
ATOM   4149 C CB  . HIS B 1 244 ? -6.91700  -3.50400  20.49200  1.000 42.56000 ? 246 HIS B CB  1 
ATOM   4150 C CG  . HIS B 1 244 ? -6.19700  -4.40800  19.54200  1.000 42.77000 ? 246 HIS B CG  1 
ATOM   4151 N ND1 . HIS B 1 244 ? -6.27200  -5.78500  19.62200  1.000 42.28000 ? 246 HIS B ND1 1 
ATOM   4152 C CD2 . HIS B 1 244 ? -5.40000  -4.13300  18.48300  1.000 38.66000 ? 246 HIS B CD2 1 
ATOM   4153 C CE1 . HIS B 1 244 ? -5.54700  -6.31700  18.65400  1.000 42.06000 ? 246 HIS B CE1 1 
ATOM   4154 N NE2 . HIS B 1 244 ? -5.01200  -5.33700  17.94700  1.000 44.10000 ? 246 HIS B NE2 1 
ATOM   4155 N N   . VAL B 1 245 ? -7.16700  -1.56200  22.86900  1.000 48.08000 ? 247 VAL B N   1 
ATOM   4156 C CA  . VAL B 1 245 ? -7.99000  -0.78300  23.78800  1.000 48.11000 ? 247 VAL B CA  1 
ATOM   4157 C C   . VAL B 1 245 ? -7.57700  0.68100   23.76900  1.000 47.28000 ? 247 VAL B C   1 
ATOM   4158 O O   . VAL B 1 245 ? -8.42600  1.57800   23.75600  1.000 46.61000 ? 247 VAL B O   1 
ATOM   4159 C CB  . VAL B 1 245 ? -7.90700  -1.38100  25.20400  1.000 49.78000 ? 247 VAL B CB  1 
ATOM   4160 C CG1 . VAL B 1 245 ? -8.55600  -0.45400  26.21800  1.000 45.61000 ? 247 VAL B CG1 1 
ATOM   4161 C CG2 . VAL B 1 245 ? -8.53800  -2.77300  25.22900  1.000 46.06000 ? 247 VAL B CG2 1 
ATOM   4162 N N   . ASP B 1 246 ? -6.26900  0.95000   23.75100  1.000 49.81000 ? 248 ASP B N   1 
ATOM   4163 C CA  . ASP B 1 246 ? -5.81000  2.33700   23.71000  1.000 50.09000 ? 248 ASP B CA  1 
ATOM   4164 C C   . ASP B 1 246 ? -6.19900  3.00700   22.39700  1.000 48.64000 ? 248 ASP B C   1 
ATOM   4165 O O   . ASP B 1 246 ? -6.66000  4.15400   22.39300  1.000 46.81000 ? 248 ASP B O   1 
ATOM   4166 C CB  . ASP B 1 246 ? -4.29500  2.40200   23.91600  1.000 52.08000 ? 248 ASP B CB  1 
ATOM   4167 C CG  . ASP B 1 246 ? -3.85700  1.80500   25.24000  1.000 53.25000 ? 248 ASP B CG  1 
ATOM   4168 O OD1 . ASP B 1 246 ? -4.61200  1.90700   26.23800  1.000 52.21000 ? 248 ASP B OD1 1 
ATOM   4169 O OD2 . ASP B 1 246 ? -2.74700  1.22900   25.27900  1.000 55.16000 ? 248 ASP B OD2 1 
ATOM   4170 N N   . ILE B 1 247 ? -6.03800  2.29600   21.27600  1.000 49.66000 ? 249 ILE B N   1 
ATOM   4171 C CA  . ILE B 1 247 ? -6.39900  2.85100   19.97300  1.000 48.73000 ? 249 ILE B CA  1 
ATOM   4172 C C   . ILE B 1 247 ? -7.86700  3.26200   19.95400  1.000 48.16000 ? 249 ILE B C   1 
ATOM   4173 O O   . ILE B 1 247 ? -8.23700  4.26900   19.33500  1.000 51.01000 ? 249 ILE B O   1 
ATOM   4174 C CB  . ILE B 1 247 ? -6.07800  1.84000   18.85400  1.000 48.61000 ? 249 ILE B CB  1 
ATOM   4175 C CG1 . ILE B 1 247 ? -4.58300  1.51500   18.83600  1.000 55.33000 ? 249 ILE B CG1 1 
ATOM   4176 C CG2 . ILE B 1 247 ? -6.45500  2.40800   17.50300  1.000 49.38000 ? 249 ILE B CG2 1 
ATOM   4177 C CD1 . ILE B 1 247 ? -4.20800  0.42300   17.84500  1.000 52.53000 ? 249 ILE B CD1 1 
ATOM   4178 N N   . LEU B 1 248 ? -8.72300  2.50300   20.64000  1.000 44.25000 ? 250 LEU B N   1 
ATOM   4179 C CA  . LEU B 1 248 ? -10.14700 2.80600   20.71700  1.000 44.84000 ? 250 LEU B CA  1 
ATOM   4180 C C   . LEU B 1 248 ? -10.47000 3.92400   21.70400  1.000 44.63000 ? 250 LEU B C   1 
ATOM   4181 O O   . LEU B 1 248 ? -11.63800 4.31700   21.80700  1.000 45.50000 ? 250 LEU B O   1 
ATOM   4182 C CB  . LEU B 1 248 ? -10.92800 1.54200   21.09200  1.000 43.98000 ? 250 LEU B CB  1 
ATOM   4183 C CG  . LEU B 1 248 ? -11.06100 0.49200   19.98700  1.000 39.19000 ? 250 LEU B CG  1 
ATOM   4184 C CD1 . LEU B 1 248 ? -11.44400 -0.85700  20.57100  1.000 31.92000 ? 250 LEU B CD1 1 
ATOM   4185 C CD2 . LEU B 1 248 ? -12.07000 0.94600   18.94000  1.000 38.46000 ? 250 LEU B CD2 1 
ATOM   4186 N N   . GLY B 1 249 ? -9.47700  4.42600   22.43200  1.000 45.42000 ? 251 GLY B N   1 
ATOM   4187 C CA  . GLY B 1 249 ? -9.64400  5.53200   23.35000  1.000 48.46000 ? 251 GLY B CA  1 
ATOM   4188 C C   . GLY B 1 249 ? -10.46100 6.71200   22.84600  1.000 44.30000 ? 251 GLY B C   1 
ATOM   4189 O O   . GLY B 1 249 ? -11.41200 7.13900   23.50100  1.000 49.18000 ? 251 GLY B O   1 
ATOM   4190 N N   . PRO B 1 250 ? -10.09600 7.28100   21.69100  1.000 45.92000 ? 252 PRO B N   1 
ATOM   4191 C CA  . PRO B 1 250 ? -10.86500 8.43300   21.17700  1.000 45.87000 ? 252 PRO B CA  1 
ATOM   4192 C C   . PRO B 1 250 ? -12.34800 8.16100   21.02700  1.000 47.94000 ? 252 PRO B C   1 
ATOM   4193 O O   . PRO B 1 250 ? -13.17100 9.02800   21.35000  1.000 47.98000 ? 252 PRO B O   1 
ATOM   4194 C CB  . PRO B 1 250 ? -10.20500 8.70800   19.82000  1.000 45.33000 ? 252 PRO B CB  1 
ATOM   4195 C CG  . PRO B 1 250 ? -8.79700  8.25600   20.00600  1.000 44.52000 ? 252 PRO B CG  1 
ATOM   4196 C CD  . PRO B 1 250 ? -8.88400  7.03500   20.88900  1.000 47.76000 ? 252 PRO B CD  1 
ATOM   4197 N N   . LEU B 1 251 ? -12.71300 6.96700   20.55500  1.000 50.00000 ? 253 LEU B N   1 
ATOM   4198 C CA  . LEU B 1 251 ? -14.12100 6.62900   20.37300  1.000 46.25000 ? 253 LEU B CA  1 
ATOM   4199 C C   . LEU B 1 251 ? -14.81400 6.34700   21.70000  1.000 47.92000 ? 253 LEU B C   1 
ATOM   4200 O O   . LEU B 1 251 ? -16.00300 6.65900   21.85300  1.000 47.16000 ? 253 LEU B O   1 
ATOM   4201 C CB  . LEU B 1 251 ? -14.24200 5.42800   19.43100  1.000 45.13000 ? 253 LEU B CB  1 
ATOM   4202 C CG  . LEU B 1 251 ? -13.64500 5.69000   18.04500  1.000 42.09000 ? 253 LEU B CG  1 
ATOM   4203 C CD1 . LEU B 1 251 ? -13.51100 4.40300   17.22900  1.000 39.14000 ? 253 LEU B CD1 1 
ATOM   4204 C CD2 . LEU B 1 251 ? -14.47600 6.73500   17.29800  1.000 44.23000 ? 253 LEU B CD2 1 
ATOM   4205 N N   . SER B 1 252 ? -14.09500 5.75900   22.66300  1.000 46.41000 ? 254 SER B N   1 
ATOM   4206 C CA  . SER B 1 252 ? -14.65900 5.56200   23.99400  1.000 47.29000 ? 254 SER B CA  1 
ATOM   4207 C C   . SER B 1 252 ? -15.00800 6.89900   24.64400  1.000 49.28000 ? 254 SER B C   1 
ATOM   4208 O O   . SER B 1 252 ? -16.07900 7.04700   25.25000  1.000 49.05000 ? 254 SER B O   1 
ATOM   4209 C CB  . SER B 1 252 ? -13.68000 4.77800   24.87100  1.000 45.83000 ? 254 SER B CB  1 
ATOM   4210 O OG  . SER B 1 252 ? -14.17900 4.63400   26.19300  1.000 46.55000 ? 254 SER B OG  1 
ATOM   4211 N N   . ALA B 1 253 ? -14.12000 7.88500   24.52000  1.000 47.67000 ? 255 ALA B N   1 
ATOM   4212 C CA  . ALA B 1 253 ? -14.38200 9.19700   25.10000  1.000 49.99000 ? 255 ALA B CA  1 
ATOM   4213 C C   . ALA B 1 253 ? -15.55200 9.87800   24.40300  1.000 52.62000 ? 255 ALA B C   1 
ATOM   4214 O O   . ALA B 1 253 ? -16.44100 10.43500  25.05900  1.000 55.48000 ? 255 ALA B O   1 
ATOM   4215 C CB  . ALA B 1 253 ? -13.12500 10.06600  25.02800  1.000 50.63000 ? 255 ALA B CB  1 
ATOM   4216 N N   . GLN B 1 254 ? -15.57900 9.83300   23.06900  1.000 51.95000 ? 256 GLN B N   1 
ATOM   4217 C CA  . GLN B 1 254 ? -16.64100 10.52000  22.34100  1.000 52.16000 ? 256 GLN B CA  1 
ATOM   4218 C C   . GLN B 1 254 ? -18.01200 9.95800   22.69300  1.000 48.55000 ? 256 GLN B C   1 
ATOM   4219 O O   . GLN B 1 254 ? -18.99000 10.70700  22.80300  1.000 51.23000 ? 256 GLN B O   1 
ATOM   4220 C CB  . GLN B 1 254 ? -16.39900 10.42700  20.83700  1.000 51.99000 ? 256 GLN B CB  1 
ATOM   4221 C CG  . GLN B 1 254 ? -17.48200 11.09100  20.00000  1.000 53.36000 ? 256 GLN B CG  1 
ATOM   4222 C CD  . GLN B 1 254 ? -17.26100 10.90200  18.51400  1.000 54.69000 ? 256 GLN B CD  1 
ATOM   4223 O OE1 . GLN B 1 254 ? -16.16200 10.54700  18.08000  1.000 58.31000 ? 256 GLN B OE1 1 
ATOM   4224 N NE2 . GLN B 1 254 ? -18.30400 11.14500  17.72200  1.000 52.66000 ? 256 GLN B NE2 1 
ATOM   4225 N N   . THR B 1 255 ? -18.10300 8.65100   22.90700  1.000 46.73000 ? 257 THR B N   1 
ATOM   4226 C CA  . THR B 1 255 ? -19.40100 8.00800   23.04300  1.000 46.55000 ? 257 THR B CA  1 
ATOM   4227 C C   . THR B 1 255 ? -19.81700 7.75800   24.48500  1.000 47.09000 ? 257 THR B C   1 
ATOM   4228 O O   . THR B 1 255 ? -21.00700 7.54000   24.73700  1.000 48.58000 ? 257 THR B O   1 
ATOM   4229 C CB  . THR B 1 255 ? -19.41500 6.66800   22.29200  1.000 47.66000 ? 257 THR B CB  1 
ATOM   4230 O OG1 . THR B 1 255 ? -18.52000 5.74900   22.93500  1.000 50.37000 ? 257 THR B OG1 1 
ATOM   4231 C CG2 . THR B 1 255 ? -18.99300 6.86000   20.84000  1.000 45.57000 ? 257 THR B CG2 1 
ATOM   4232 N N   . GLY B 1 256 ? -18.88100 7.77800   25.43100  1.000 47.78000 ? 258 GLY B N   1 
ATOM   4233 C CA  . GLY B 1 256 ? -19.20300 7.41000   26.79400  1.000 46.78000 ? 258 GLY B CA  1 
ATOM   4234 C C   . GLY B 1 256 ? -19.26800 5.91800   27.06400  1.000 52.34000 ? 258 GLY B C   1 
ATOM   4235 O O   . GLY B 1 256 ? -19.62400 5.52200   28.18100  1.000 47.92000 ? 258 GLY B O   1 
ATOM   4236 N N   . ILE B 1 257 ? -18.93800 5.07700   26.08500  1.000 47.55000 ? 259 ILE B N   1 
ATOM   4237 C CA  . ILE B 1 257 ? -18.89800 3.62700   26.26400  1.000 52.25000 ? 259 ILE B CA  1 
ATOM   4238 C C   . ILE B 1 257 ? -17.43700 3.19900   26.27100  1.000 49.56000 ? 259 ILE B C   1 
ATOM   4239 O O   . ILE B 1 257 ? -16.70800 3.44400   25.30000  1.000 46.28000 ? 259 ILE B O   1 
ATOM   4240 C CB  . ILE B 1 257 ? -19.68000 2.88800   25.16600  1.000 51.26000 ? 259 ILE B CB  1 
ATOM   4241 C CG1 . ILE B 1 257 ? -21.14000 3.33200   25.14200  1.000 50.45000 ? 259 ILE B CG1 1 
ATOM   4242 C CG2 . ILE B 1 257 ? -19.62200 1.39900   25.39300  1.000 49.30000 ? 259 ILE B CG2 1 
ATOM   4243 C CD1 . ILE B 1 257 ? -21.45600 4.32900   24.06300  1.000 53.72000 ? 259 ILE B CD1 1 
ATOM   4244 N N   . ALA B 1 258 ? -17.00500 2.59000   27.37200  1.000 46.94000 ? 260 ALA B N   1 
ATOM   4245 C CA  . ALA B 1 258 ? -15.63700 2.11200   27.49200  1.000 49.53000 ? 260 ALA B CA  1 
ATOM   4246 C C   . ALA B 1 258 ? -15.45500 0.83300   26.68300  1.000 49.83000 ? 260 ALA B C   1 
ATOM   4247 O O   . ALA B 1 258 ? -16.41400 0.12600   26.36200  1.000 47.11000 ? 260 ALA B O   1 
ATOM   4248 C CB  . ALA B 1 258 ? -15.27200 1.86400   28.95500  1.000 47.43000 ? 260 ALA B CB  1 
ATOM   4249 N N   . VAL B 1 259 ? -14.19900 0.53000   26.35500  1.000 48.84000 ? 261 VAL B N   1 
ATOM   4250 C CA  . VAL B 1 259 ? -13.95600 -0.57500  25.43200  1.000 45.22000 ? 261 VAL B CA  1 
ATOM   4251 C C   . VAL B 1 259 ? -14.51000 -1.87500  25.99600  1.000 44.60000 ? 261 VAL B C   1 
ATOM   4252 O O   . VAL B 1 259 ? -15.24500 -2.59900  25.31400  1.000 46.97000 ? 261 VAL B O   1 
ATOM   4253 C CB  . VAL B 1 259 ? -12.46000 -0.67600  25.09900  1.000 39.81000 ? 261 VAL B CB  1 
ATOM   4254 C CG1 . VAL B 1 259 ? -12.21100 -1.87800  24.21200  1.000 44.74000 ? 261 VAL B CG1 1 
ATOM   4255 C CG2 . VAL B 1 259 ? -12.00700 0.59100   24.41300  1.000 43.24000 ? 261 VAL B CG2 1 
ATOM   4256 N N   . LEU B 1 260 ? -14.19700 -2.17800  27.25900  1.000 44.33000 ? 262 LEU B N   1 
ATOM   4257 C CA  . LEU B 1 260 ? -14.69300 -3.41600  27.85400  1.000 45.78000 ? 262 LEU B CA  1 
ATOM   4258 C C   . LEU B 1 260 ? -16.21100 -3.38900  28.01800  1.000 49.94000 ? 262 LEU B C   1 
ATOM   4259 O O   . LEU B 1 260 ? -16.85400 -4.44600  28.00200  1.000 50.83000 ? 262 LEU B O   1 
ATOM   4260 C CB  . LEU B 1 260 ? -13.99900 -3.66600  29.19100  1.000 48.18000 ? 262 LEU B CB  1 
ATOM   4261 C CG  . LEU B 1 260 ? -12.49900 -3.96200  29.06000  1.000 50.25000 ? 262 LEU B CG  1 
ATOM   4262 C CD1 . LEU B 1 260 ? -11.75400 -3.59900  30.34200  1.000 50.13000 ? 262 LEU B CD1 1 
ATOM   4263 C CD2 . LEU B 1 260 ? -12.24800 -5.42000  28.67200  1.000 48.02000 ? 262 LEU B CD2 1 
ATOM   4264 N N   . ASP B 1 261 ? -16.78800 -2.19400  28.17900  1.000 51.35000 ? 263 ASP B N   1 
ATOM   4265 C CA  . ASP B 1 261 ? -18.22900 -2.00500  28.03800  1.000 51.87000 ? 263 ASP B CA  1 
ATOM   4266 C C   . ASP B 1 261 ? -18.69800 -2.50400  26.67500  1.000 48.37000 ? 263 ASP B C   1 
ATOM   4267 O O   . ASP B 1 261 ? -19.62400 -3.32000  26.57800  1.000 47.23000 ? 263 ASP B O   1 
ATOM   4268 C CB  . ASP B 1 261 ? -18.55000 -0.51500  28.20900  1.000 53.67000 ? 263 ASP B CB  1 
ATOM   4269 C CG  . ASP B 1 261 ? -19.80300 -0.24500  29.01400  1.000 61.03000 ? 263 ASP B CG  1 
ATOM   4270 O OD1 . ASP B 1 261 ? -20.83700 -0.91800  28.78900  1.000 57.93000 ? 263 ASP B OD1 1 
ATOM   4271 O OD2 . ASP B 1 261 ? -19.74900 0.69200   29.85000  1.000 61.31000 ? 263 ASP B OD2 1 
ATOM   4272 N N   . MET B 1 262 ? -18.05100 -2.03000  25.60300  1.000 47.66000 ? 264 MET B N   1 
ATOM   4273 C CA  . MET B 1 262 ? -18.42600 -2.46200  24.25700  1.000 47.68000 ? 264 MET B CA  1 
ATOM   4274 C C   . MET B 1 262 ? -18.09600 -3.93300  24.02100  1.000 46.71000 ? 264 MET B C   1 
ATOM   4275 O O   . MET B 1 262 ? -18.82500 -4.62300  23.29600  1.000 43.34000 ? 264 MET B O   1 
ATOM   4276 C CB  . MET B 1 262 ? -17.73700 -1.57800  23.21200  1.000 44.00000 ? 264 MET B CB  1 
ATOM   4277 C CG  . MET B 1 262 ? -18.30300 -1.72600  21.80600  1.000 42.35000 ? 264 MET B CG  1 
ATOM   4278 S SD  . MET B 1 262 ? -19.93600 -0.94200  21.62600  1.000 43.02000 ? 264 MET B SD  1 
ATOM   4279 C CE  . MET B 1 262 ? -19.43800 0.73200   21.25600  1.000 39.19000 ? 264 MET B CE  1 
ATOM   4280 N N   . CYS B 1 263 ? -17.00900 -4.43100  24.62200  1.000 44.83000 ? 265 CYS B N   1 
ATOM   4281 C CA  . CYS B 1 263 ? -16.71400 -5.85700  24.53800  1.000 47.11000 ? 265 CYS B CA  1 
ATOM   4282 C C   . CYS B 1 263 ? -17.85600 -6.68600  25.10900  1.000 45.19000 ? 265 CYS B C   1 
ATOM   4283 O O   . CYS B 1 263 ? -18.23900 -7.70900  24.53000  1.000 45.45000 ? 265 CYS B O   1 
ATOM   4284 C CB  . CYS B 1 263 ? -15.41000 -6.16900  25.26600  1.000 47.22000 ? 265 CYS B CB  1 
ATOM   4285 S SG  . CYS B 1 263 ? -13.93800 -5.59700  24.41500  1.000 44.20000 ? 265 CYS B SG  1 
ATOM   4286 N N   . ALA B 1 264 ? -18.42300 -6.25100  26.23800  1.000 48.56000 ? 266 ALA B N   1 
ATOM   4287 C CA  . ALA B 1 264 ? -19.60600 -6.92300  26.77300  1.000 49.28000 ? 266 ALA B CA  1 
ATOM   4288 C C   . ALA B 1 264 ? -20.73500 -6.95100  25.74700  1.000 48.23000 ? 266 ALA B C   1 
ATOM   4289 O O   . ALA B 1 264 ? -21.40300 -7.97700  25.57600  1.000 48.60000 ? 266 ALA B O   1 
ATOM   4290 C CB  . ALA B 1 264 ? -20.06300 -6.23600  28.06000  1.000 52.66000 ? 266 ALA B CB  1 
ATOM   4291 N N   . SER B 1 265 ? -20.94400 -5.84000  25.03400  1.000 48.05000 ? 267 SER B N   1 
ATOM   4292 C CA  . SER B 1 265 ? -21.95800 -5.81100  23.98100  1.000 49.51000 ? 267 SER B CA  1 
ATOM   4293 C C   . SER B 1 265 ? -21.62900 -6.81100  22.88000  1.000 44.63000 ? 267 SER B C   1 
ATOM   4294 O O   . SER B 1 265 ? -22.49000 -7.59200  22.45900  1.000 42.57000 ? 267 SER B O   1 
ATOM   4295 C CB  . SER B 1 265 ? -22.07900 -4.39700  23.40100  1.000 46.27000 ? 267 SER B CB  1 
ATOM   4296 O OG  . SER B 1 265 ? -22.55800 -3.47900  24.37000  1.000 47.63000 ? 267 SER B OG  1 
ATOM   4297 N N   . LEU B 1 266 ? -20.38300 -6.78700  22.39000  1.000 42.01000 ? 268 LEU B N   1 
ATOM   4298 C CA  . LEU B 1 266 ? -19.96700 -7.71400  21.33700  1.000 42.53000 ? 268 LEU B CA  1 
ATOM   4299 C C   . LEU B 1 266 ? -20.00300 -9.16400  21.81400  1.000 42.62000 ? 268 LEU B C   1 
ATOM   4300 O O   . LEU B 1 266 ? -20.36000 -10.07300 21.05100  1.000 38.46000 ? 268 LEU B O   1 
ATOM   4301 C CB  . LEU B 1 266 ? -18.56300 -7.34700  20.84700  1.000 36.66000 ? 268 LEU B CB  1 
ATOM   4302 C CG  . LEU B 1 266 ? -17.83500 -8.34700  19.94400  1.000 36.29000 ? 268 LEU B CG  1 
ATOM   4303 C CD1 . LEU B 1 266 ? -18.60400 -8.55600  18.66300  1.000 34.40000 ? 268 LEU B CD1 1 
ATOM   4304 C CD2 . LEU B 1 266 ? -16.43100 -7.86000  19.62900  1.000 32.09000 ? 268 LEU B CD2 1 
ATOM   4305 N N   . LYS B 1 267 ? -19.61200 -9.41000  23.06500  1.000 44.82000 ? 269 LYS B N   1 
ATOM   4306 C CA  . LYS B 1 267 ? -19.67200 -10.76900 23.58500  1.000 50.05000 ? 269 LYS B CA  1 
ATOM   4307 C C   . LYS B 1 267 ? -21.11000 -11.28200 23.57600  1.000 51.28000 ? 269 LYS B C   1 
ATOM   4308 O O   . LYS B 1 267 ? -21.37400 -12.40700 23.14300  1.000 54.53000 ? 269 LYS B O   1 
ATOM   4309 C CB  . LYS B 1 267 ? -19.04700 -10.82200 24.98300  1.000 53.96000 ? 269 LYS B CB  1 
ATOM   4310 C CG  . LYS B 1 267 ? -19.00100 -12.22100 25.59800  1.000 59.98000 ? 269 LYS B CG  1 
ATOM   4311 C CD  . LYS B 1 267 ? -19.45800 -12.22100 27.05800  1.000 62.41000 ? 269 LYS B CD  1 
ATOM   4312 C CE  . LYS B 1 267 ? -19.67000 -13.64800 27.57700  1.000 62.69000 ? 269 LYS B CE  1 
ATOM   4313 N NZ  . LYS B 1 267 ? -21.10800 -14.08300 27.57900  1.000 65.42000 ? 269 LYS B NZ  1 
ATOM   4314 N N   . GLU B 1 268 ? -22.05600 -10.43800 24.01100  1.000 55.98000 ? 270 GLU B N   1 
ATOM   4315 C CA  . GLU B 1 268 ? -23.47500 -10.78800 23.91300  1.000 52.72000 ? 270 GLU B CA  1 
ATOM   4316 C C   . GLU B 1 268 ? -23.87500 -11.06100 22.47100  1.000 52.55000 ? 270 GLU B C   1 
ATOM   4317 O O   . GLU B 1 268 ? -24.61400 -12.01500 22.19300  1.000 54.02000 ? 270 GLU B O   1 
ATOM   4318 C CB  . GLU B 1 268 ? -24.33700 -9.66500  24.50000  1.000 55.29000 ? 270 GLU B CB  1 
ATOM   4319 C CG  . GLU B 1 268 ? -24.12500 -9.41300  25.98500  1.000 57.43000 ? 270 GLU B CG  1 
ATOM   4320 C CD  . GLU B 1 268 ? -24.22100 -10.68400 26.82500  1.000 63.92000 ? 270 GLU B CD  1 
ATOM   4321 O OE1 . GLU B 1 268 ? -23.23800 -11.00600 27.53800  1.000 63.33000 ? 270 GLU B OE1 1 
ATOM   4322 O OE2 . GLU B 1 268 ? -25.27700 -11.35700 26.76700  1.000 60.70000 ? 270 GLU B OE2 1 
ATOM   4323 N N   . LEU B 1 269 ? -23.38800 -10.23900 21.53700  1.000 50.32000 ? 271 LEU B N   1 
ATOM   4324 C CA  . LEU B 1 269 ? -23.72200 -10.42000 20.12800  1.000 49.29000 ? 271 LEU B CA  1 
ATOM   4325 C C   . LEU B 1 269 ? -23.16500 -11.72600 19.57800  1.000 50.13000 ? 271 LEU B C   1 
ATOM   4326 O O   . LEU B 1 269 ? -23.76900 -12.33600 18.69000  1.000 48.46000 ? 271 LEU B O   1 
ATOM   4327 C CB  . LEU B 1 269 ? -23.19100 -9.23700  19.31300  1.000 46.70000 ? 271 LEU B CB  1 
ATOM   4328 C CG  . LEU B 1 269 ? -23.85700 -7.87900  19.54800  1.000 46.63000 ? 271 LEU B CG  1 
ATOM   4329 C CD1 . LEU B 1 269 ? -23.26300 -6.82000  18.62300  1.000 45.20000 ? 271 LEU B CD1 1 
ATOM   4330 C CD2 . LEU B 1 269 ? -25.36300 -7.96600  19.36500  1.000 47.05000 ? 271 LEU B CD2 1 
ATOM   4331 N N   . LEU B 1 270 ? -22.00900 -12.16400 20.07700  1.000 51.20000 ? 272 LEU B N   1 
ATOM   4332 C CA  . LEU B 1 270 ? -21.40700 -13.37900 19.54300  1.000 51.41000 ? 272 LEU B CA  1 
ATOM   4333 C C   . LEU B 1 270 ? -22.22900 -14.61100 19.91600  1.000 50.95000 ? 272 LEU B C   1 
ATOM   4334 O O   . LEU B 1 270 ? -22.42700 -15.50500 19.08600  1.000 50.04000 ? 272 LEU B O   1 
ATOM   4335 C CB  . LEU B 1 270 ? -19.96100 -13.48800 20.03300  1.000 48.95000 ? 272 LEU B CB  1 
ATOM   4336 C CG  . LEU B 1 270 ? -19.00500 -12.53300 19.29300  1.000 48.75000 ? 272 LEU B CG  1 
ATOM   4337 C CD1 . LEU B 1 270 ? -17.57700 -12.58900 19.83100  1.000 44.45000 ? 272 LEU B CD1 1 
ATOM   4338 C CD2 . LEU B 1 270 ? -19.02700 -12.82900 17.79500  1.000 45.35000 ? 272 LEU B CD2 1 
ATOM   4339 N N   . GLN B 1 271 ? -22.75500 -14.65400 21.14200  1.000 55.12000 ? 273 GLN B N   1 
ATOM   4340 C CA  . GLN B 1 271 ? -23.50000 -15.82200 21.61100  1.000 56.87000 ? 273 GLN B CA  1 
ATOM   4341 C C   . GLN B 1 271 ? -24.94900 -15.79500 21.14500  1.000 58.61000 ? 273 GLN B C   1 
ATOM   4342 O O   . GLN B 1 271 ? -25.41100 -16.72400 20.47000  1.000 60.09000 ? 273 GLN B O   1 
ATOM   4343 C CB  . GLN B 1 271 ? -23.43400 -15.91200 23.14000  1.000 55.63000 ? 273 GLN B CB  1 
ATOM   4344 C CG  . GLN B 1 271 ? -22.08100 -16.37100 23.65400  1.000 54.71000 ? 273 GLN B CG  1 
ATOM   4345 C CD  . GLN B 1 271 ? -21.55100 -15.53600 24.80000  1.000 56.99000 ? 273 GLN B CD  1 
ATOM   4346 O OE1 . GLN B 1 271 ? -21.95100 -14.39300 24.98500  1.000 61.75000 ? 273 GLN B OE1 1 
ATOM   4347 N NE2 . GLN B 1 271 ? -20.60100 -16.08500 25.54000  1.000 57.77000 ? 273 GLN B NE2 1 
ATOM   4348 N N   . ASN B 1 272 ? -25.67700 -14.73700 21.49900  1.000 54.45000 ? 274 ASN B N   1 
ATOM   4349 C CA  . ASN B 1 272 ? -27.11900 -14.67800 21.29300  1.000 57.19000 ? 274 ASN B CA  1 
ATOM   4350 C C   . ASN B 1 272 ? -27.50500 -14.26500 19.88000  1.000 59.00000 ? 274 ASN B C   1 
ATOM   4351 O O   . ASN B 1 272 ? -28.69900 -14.24800 19.55900  1.000 60.12000 ? 274 ASN B O   1 
ATOM   4352 C CB  . ASN B 1 272 ? -27.74600 -13.71500 22.30500  1.000 57.31000 ? 274 ASN B CB  1 
ATOM   4353 C CG  . ASN B 1 272 ? -27.25800 -13.96300 23.72500  1.000 57.90000 ? 274 ASN B CG  1 
ATOM   4354 O OD1 . ASN B 1 272 ? -27.11700 -15.10700 24.14800  1.000 66.10000 ? 274 ASN B OD1 1 
ATOM   4355 N ND2 . ASN B 1 272 ? -26.99500 -12.89300 24.46300  1.000 59.39000 ? 274 ASN B ND2 1 
ATOM   4356 N N   . GLY B 1 273 ? -26.53700 -13.93900 19.03400  1.000 59.26000 ? 275 GLY B N   1 
ATOM   4357 C CA  . GLY B 1 273 ? -26.86000 -13.41300 17.72900  1.000 56.37000 ? 275 GLY B CA  1 
ATOM   4358 C C   . GLY B 1 273 ? -27.35800 -11.98200 17.83500  1.000 56.24000 ? 275 GLY B C   1 
ATOM   4359 O O   . GLY B 1 273 ? -27.22300 -11.30600 18.86100  1.000 53.07000 ? 275 GLY B O   1 
ATOM   4360 N N   . MET B 1 274 ? -27.95600 -11.52600 16.73600  1.000 57.53000 ? 276 MET B N   1 
ATOM   4361 C CA  . MET B 1 274 ? -28.49200 -10.17400 16.65400  1.000 57.75000 ? 276 MET B CA  1 
ATOM   4362 C C   . MET B 1 274 ? -29.99400 -10.11500 16.88600  1.000 60.16000 ? 276 MET B C   1 
ATOM   4363 O O   . MET B 1 274 ? -30.56800 -9.01800  16.85200  1.000 56.50000 ? 276 MET B O   1 
ATOM   4364 C CB  . MET B 1 274 ? -28.15900 -9.55400  15.29900  1.000 56.50000 ? 276 MET B CB  1 
ATOM   4365 C CG  . MET B 1 274 ? -26.67900 -9.30800  15.09800  1.000 56.96000 ? 276 MET B CG  1 
ATOM   4366 S SD  . MET B 1 274 ? -26.36100 -7.98800  13.91900  1.000 62.11000 ? 276 MET B SD  1 
ATOM   4367 C CE  . MET B 1 274 ? -24.76300 -8.53800  13.33300  1.000 49.71000 ? 276 MET B CE  1 
ATOM   4368 N N   . ASN B 1 275 ? -30.63700 -11.26100 17.11000  1.000 59.00000 ? 277 ASN B N   1 
ATOM   4369 C CA  . ASN B 1 275 ? -32.05800 -11.33200 17.44500  1.000 62.05000 ? 277 ASN B CA  1 
ATOM   4370 C C   . ASN B 1 275 ? -32.91000 -10.57100 16.43100  1.000 58.64000 ? 277 ASN B C   1 
ATOM   4371 O O   . ASN B 1 275 ? -33.80000 -9.79400  16.78400  1.000 61.99000 ? 277 ASN B O   1 
ATOM   4372 C CB  . ASN B 1 275 ? -32.29900 -10.83000 18.87000  1.000 64.32000 ? 277 ASN B CB  1 
ATOM   4373 C CG  . ASN B 1 275 ? -31.68400 -11.74800 19.92100  1.000 67.45000 ? 277 ASN B CG  1 
ATOM   4374 O OD1 . ASN B 1 275 ? -31.57000 -12.96400 19.71500  1.000 68.01000 ? 277 ASN B OD1 1 
ATOM   4375 N ND2 . ASN B 1 275 ? -31.27000 -11.16600 21.04700  1.000 67.91000 ? 277 ASN B ND2 1 
ATOM   4376 N N   . GLY B 1 276 ? -32.62000 -10.80300 15.14900  1.000 56.87000 ? 278 GLY B N   1 
ATOM   4377 C CA  . GLY B 1 276 ? -33.34600 -10.19100 14.05300  1.000 57.07000 ? 278 GLY B CA  1 
ATOM   4378 C C   . GLY B 1 276 ? -32.92700 -8.78000  13.70400  1.000 61.28000 ? 278 GLY B C   1 
ATOM   4379 O O   . GLY B 1 276 ? -33.32800 -8.27400  12.64700  1.000 62.58000 ? 278 GLY B O   1 
ATOM   4380 N N   . ARG B 1 277 ? -32.13000 -8.12800  14.54200  1.000 59.68000 ? 279 ARG B N   1 
ATOM   4381 C CA  . ARG B 1 277 ? -31.79400 -6.73100  14.33900  1.000 56.46000 ? 279 ARG B CA  1 
ATOM   4382 C C   . ARG B 1 277 ? -30.68200 -6.58300  13.29500  1.000 56.89000 ? 279 ARG B C   1 
ATOM   4383 O O   . ARG B 1 277 ? -30.03300 -7.54700  12.88300  1.000 52.33000 ? 279 ARG B O   1 
ATOM   4384 C CB  . ARG B 1 277 ? -31.36800 -6.09900  15.66400  1.000 57.33000 ? 279 ARG B CB  1 
ATOM   4385 C CG  . ARG B 1 277 ? -32.50200 -5.59000  16.55400  1.000 57.46000 ? 279 ARG B CG  1 
ATOM   4386 C CD  . ARG B 1 277 ? -33.15900 -6.70000  17.36700  1.000 61.03000 ? 279 ARG B CD  1 
ATOM   4387 N NE  . ARG B 1 277 ? -32.33100 -7.21100  18.46400  1.000 64.45000 ? 279 ARG B NE  1 
ATOM   4388 C CZ  . ARG B 1 277 ? -32.28300 -6.68800  19.69000  1.000 64.44000 ? 279 ARG B CZ  1 
ATOM   4389 N NH1 . ARG B 1 277 ? -33.00100 -5.60600  19.99000  1.000 60.69000 ? 279 ARG B NH1 1 
ATOM   4390 N NH2 . ARG B 1 277 ? -31.50000 -7.24000  20.61500  1.000 61.52000 ? 279 ARG B NH2 1 
ATOM   4391 N N   . THR B 1 278 ? -30.48300 -5.34800  12.85000  1.000 52.84000 ? 280 THR B N   1 
ATOM   4392 C CA  . THR B 1 278 ? -29.30000 -4.95600  12.10200  1.000 51.10000 ? 280 THR B CA  1 
ATOM   4393 C C   . THR B 1 278 ? -28.58400 -3.88100  12.90100  1.000 51.44000 ? 280 THR B C   1 
ATOM   4394 O O   . THR B 1 278 ? -29.12300 -3.34600  13.87800  1.000 49.48000 ? 280 THR B O   1 
ATOM   4395 C CB  . THR B 1 278 ? -29.65900 -4.45400  10.70000  1.000 50.28000 ? 280 THR B CB  1 
ATOM   4396 O OG1 . THR B 1 278 ? -30.71000 -3.49000  10.80700  1.000 50.07000 ? 280 THR B OG1 1 
ATOM   4397 C CG2 . THR B 1 278 ? -30.11600 -5.61300  9.81500   1.000 48.86000 ? 280 THR B CG2 1 
ATOM   4398 N N   . ILE B 1 279 ? -27.35000 -3.55600  12.50400  1.000 47.28000 ? 281 ILE B N   1 
ATOM   4399 C CA  . ILE B 1 279 ? -26.50700 -2.65400  13.25400  1.000 47.91000 ? 281 ILE B CA  1 
ATOM   4400 C C   . ILE B 1 279 ? -26.15600 -1.39400  12.46100  1.000 50.22000 ? 281 ILE B C   1 
ATOM   4401 O O   . ILE B 1 279 ? -26.29500 -0.27600  12.94800  1.000 51.36000 ? 281 ILE B O   1 
ATOM   4402 C CB  . ILE B 1 279 ? -25.23300 -3.34600  13.76100  1.000 45.42000 ? 281 ILE B CB  1 
ATOM   4403 C CG1 . ILE B 1 279 ? -25.62400 -4.44500  14.75400  1.000 44.41000 ? 281 ILE B CG1 1 
ATOM   4404 C CG2 . ILE B 1 279 ? -24.29200 -2.30500  14.36300  1.000 38.85000 ? 281 ILE B CG2 1 
ATOM   4405 C CD1 . ILE B 1 279 ? -24.57400 -4.76700  15.78200  1.000 46.92000 ? 281 ILE B CD1 1 
ATOM   4406 N N   . LEU B 1 280 ? -25.67900 -1.57600  11.24000  1.000 50.37000 ? 282 LEU B N   1 
ATOM   4407 C CA  . LEU B 1 280 ? -25.70700 -0.39700  10.38000  1.000 43.37000 ? 282 LEU B CA  1 
ATOM   4408 C C   . LEU B 1 280 ? -26.48300 -0.81900  9.15000   1.000 44.07000 ? 282 LEU B C   1 
ATOM   4409 O O   . LEU B 1 280 ? -27.69700 -1.01600  9.22800   1.000 47.29000 ? 282 LEU B O   1 
ATOM   4410 C CB  . LEU B 1 280 ? -24.29000 0.12700   10.07700  1.000 46.15000 ? 282 LEU B CB  1 
ATOM   4411 C CG  . LEU B 1 280 ? -23.88100 1.19900   11.08900  1.000 45.32000 ? 282 LEU B CG  1 
ATOM   4412 C CD1 . LEU B 1 280 ? -22.36100 1.29900   11.31000  1.000 42.29000 ? 282 LEU B CD1 1 
ATOM   4413 C CD2 . LEU B 1 280 ? -24.47400 2.57400   10.72300  1.000 43.22000 ? 282 LEU B CD2 1 
ATOM   4414 N N   . GLY B 1 281 ? -25.82200 -1.02700  8.03100   1.000 44.79000 ? 283 GLY B N   1 
ATOM   4415 C CA  . GLY B 1 281 ? -26.57100 -1.66500  6.96600   1.000 51.78000 ? 283 GLY B CA  1 
ATOM   4416 C C   . GLY B 1 281 ? -26.56200 -3.18700  6.99300   1.000 49.69000 ? 283 GLY B C   1 
ATOM   4417 O O   . GLY B 1 281 ? -26.95700 -3.80900  6.00300   1.000 51.32000 ? 283 GLY B O   1 
ATOM   4418 N N   . SER B 1 282 ? -26.13300 -3.81300  8.09600   1.000 47.88000 ? 284 SER B N   1 
ATOM   4419 C CA  . SER B 1 282 ? -25.65900 -5.19300  8.02300   1.000 48.02000 ? 284 SER B CA  1 
ATOM   4420 C C   . SER B 1 282 ? -26.28300 -6.11500  9.06500   1.000 42.70000 ? 284 SER B C   1 
ATOM   4421 O O   . SER B 1 282 ? -26.45100 -5.74800  10.23300  1.000 43.66000 ? 284 SER B O   1 
ATOM   4422 C CB  . SER B 1 282 ? -24.13300 -5.24700  8.16800   1.000 43.16000 ? 284 SER B CB  1 
ATOM   4423 O OG  . SER B 1 282 ? -23.64200 -6.55200  7.88200   1.000 43.84000 ? 284 SER B OG  1 
ATOM   4424 N N   . ALA B 1 283 ? -26.58400 -7.33400  8.62300   1.000 42.95000 ? 285 ALA B N   1 
ATOM   4425 C CA  . ALA B 1 283 ? -26.89700 -8.45100  9.50400   1.000 42.02000 ? 285 ALA B CA  1 
ATOM   4426 C C   . ALA B 1 283 ? -25.64700 -9.17400  9.99900   1.000 44.91000 ? 285 ALA B C   1 
ATOM   4427 O O   . ALA B 1 283 ? -25.76400 -10.07600 10.83400  1.000 45.97000 ? 285 ALA B O   1 
ATOM   4428 C CB  . ALA B 1 283 ? -27.81500 -9.44600  8.78700   1.000 42.53000 ? 285 ALA B CB  1 
ATOM   4429 N N   . LEU B 1 284 ? -24.46800 -8.80100  9.50700   1.000 37.96000 ? 286 LEU B N   1 
ATOM   4430 C CA  . LEU B 1 284 ? -23.19000 -9.35500  9.93200   1.000 41.11000 ? 286 LEU B CA  1 
ATOM   4431 C C   . LEU B 1 284 ? -22.38700 -8.31300  10.70900  1.000 39.49000 ? 286 LEU B C   1 
ATOM   4432 O O   . LEU B 1 284 ? -22.55900 -7.10400  10.53000  1.000 38.33000 ? 286 LEU B O   1 
ATOM   4433 C CB  . LEU B 1 284 ? -22.37800 -9.82000  8.71600   1.000 41.55000 ? 286 LEU B CB  1 
ATOM   4434 C CG  . LEU B 1 284 ? -22.94000 -10.98900 7.92100   1.000 39.90000 ? 286 LEU B CG  1 
ATOM   4435 C CD1 . LEU B 1 284 ? -21.99600 -11.40700 6.78600   1.000 41.85000 ? 286 LEU B CD1 1 
ATOM   4436 C CD2 . LEU B 1 284 ? -23.24500 -12.15900 8.85700   1.000 41.86000 ? 286 LEU B CD2 1 
ATOM   4437 N N   . LEU B 1 285 ? -21.48900 -8.79100  11.57100  1.000 36.07000 ? 287 LEU B N   1 
ATOM   4438 C CA  . LEU B 1 285 ? -20.55100 -7.90000  12.25600  1.000 38.24000 ? 287 LEU B CA  1 
ATOM   4439 C C   . LEU B 1 285 ? -19.41500 -7.54300  11.29700  1.000 36.06000 ? 287 LEU B C   1 
ATOM   4440 O O   . LEU B 1 285 ? -18.63700 -8.41100  10.89200  1.000 37.87000 ? 287 LEU B O   1 
ATOM   4441 C CB  . LEU B 1 285 ? -20.03500 -8.55100  13.53800  1.000 34.96000 ? 287 LEU B CB  1 
ATOM   4442 C CG  . LEU B 1 285 ? -21.11000 -8.78400  14.60700  1.000 39.59000 ? 287 LEU B CG  1 
ATOM   4443 C CD1 . LEU B 1 285 ? -20.55900 -9.50900  15.82000  1.000 42.98000 ? 287 LEU B CD1 1 
ATOM   4444 C CD2 . LEU B 1 285 ? -21.75700 -7.47800  15.03800  1.000 40.35000 ? 287 LEU B CD2 1 
ATOM   4445 N N   . GLU B 1 286 ? -19.32500 -6.26500  10.92700  1.000 37.72000 ? 288 GLU B N   1 
ATOM   4446 C CA  . GLU B 1 286 ? -18.36700 -5.80200  9.92700   1.000 36.99000 ? 288 GLU B CA  1 
ATOM   4447 C C   . GLU B 1 286 ? -16.99900 -5.57500  10.55500  1.000 34.01000 ? 288 GLU B C   1 
ATOM   4448 O O   . GLU B 1 286 ? -16.89000 -4.91000  11.59100  1.000 31.13000 ? 288 GLU B O   1 
ATOM   4449 C CB  . GLU B 1 286 ? -18.85900 -4.49800  9.29000   1.000 39.79000 ? 288 GLU B CB  1 
ATOM   4450 C CG  . GLU B 1 286 ? -19.98200 -4.69400  8.27900   1.000 47.62000 ? 288 GLU B CG  1 
ATOM   4451 C CD  . GLU B 1 286 ? -19.50000 -5.39700  7.01400   1.000 54.75000 ? 288 GLU B CD  1 
ATOM   4452 O OE1 . GLU B 1 286 ? -18.50100 -4.92500  6.41700   1.000 58.55000 ? 288 GLU B OE1 1 
ATOM   4453 O OE2 . GLU B 1 286 ? -20.11500 -6.41800  6.63000   1.000 50.75000 ? 288 GLU B OE2 1 
ATOM   4454 N N   . ASP B 1 287 ? -15.94200 -6.09100  9.91200   1.000 31.70000 ? 289 ASP B N   1 
ATOM   4455 C CA  . ASP B 1 287 ? -14.60200 -5.93200  10.47500  1.000 30.79000 ? 289 ASP B CA  1 
ATOM   4456 C C   . ASP B 1 287 ? -13.58900 -5.33400  9.49800   1.000 33.32000 ? 289 ASP B C   1 
ATOM   4457 O O   . ASP B 1 287 ? -12.37800 -5.47100  9.71700   1.000 33.26000 ? 289 ASP B O   1 
ATOM   4458 C CB  . ASP B 1 287 ? -14.08800 -7.26800  11.04000  1.000 33.55000 ? 289 ASP B CB  1 
ATOM   4459 C CG  . ASP B 1 287 ? -13.60500 -8.25300  9.96800   1.000 33.10000 ? 289 ASP B CG  1 
ATOM   4460 O OD1 . ASP B 1 287 ? -13.95900 -8.13300  8.78100   1.000 29.86000 ? 289 ASP B OD1 1 
ATOM   4461 O OD2 . ASP B 1 287 ? -12.84500 -9.17500  10.34200  1.000 33.70000 ? 289 ASP B OD2 1 
ATOM   4462 N N   . GLU B 1 288 ? -14.03400 -4.64100  8.44700   1.000 31.21000 ? 290 GLU B N   1 
ATOM   4463 C CA  . GLU B 1 288 ? -13.10400 -3.95500  7.55800   1.000 34.28000 ? 290 GLU B CA  1 
ATOM   4464 C C   . GLU B 1 288 ? -13.12300 -2.43000  7.73500   1.000 32.28000 ? 290 GLU B C   1 
ATOM   4465 O O   . GLU B 1 288 ? -12.79100 -1.69900  6.80300   1.000 36.20000 ? 290 GLU B O   1 
ATOM   4466 C CB  . GLU B 1 288 ? -13.36000 -4.34000  6.09400   1.000 35.53000 ? 290 GLU B CB  1 
ATOM   4467 C CG  . GLU B 1 288 ? -13.52500 -5.85600  5.84900   1.000 35.42000 ? 290 GLU B CG  1 
ATOM   4468 C CD  . GLU B 1 288 ? -12.60900 -6.44300  4.74400   1.000 38.40000 ? 290 GLU B CD  1 
ATOM   4469 O OE1 . GLU B 1 288 ? -12.07800 -7.57700  4.91800   1.000 38.45000 ? 290 GLU B OE1 1 
ATOM   4470 O OE2 . GLU B 1 288 ? -12.44400 -5.80300  3.68200   1.000 34.35000 ? 290 GLU B OE2 1 
ATOM   4471 N N   . PHE B 1 289 ? -13.48400 -1.92600  8.92300   1.000 32.19000 ? 291 PHE B N   1 
ATOM   4472 C CA  . PHE B 1 289 ? -13.28100 -0.52000  9.28200   1.000 30.49000 ? 291 PHE B CA  1 
ATOM   4473 C C   . PHE B 1 289 ? -12.35300 -0.44100  10.48500  1.000 32.24000 ? 291 PHE B C   1 
ATOM   4474 O O   . PHE B 1 289 ? -12.67600 -0.97200  11.55000  1.000 29.57000 ? 291 PHE B O   1 
ATOM   4475 C CB  . PHE B 1 289 ? -14.59000 0.20000   9.63900   1.000 32.69000 ? 291 PHE B CB  1 
ATOM   4476 C CG  . PHE B 1 289 ? -15.60300 0.23800   8.54100   1.000 37.73000 ? 291 PHE B CG  1 
ATOM   4477 C CD1 . PHE B 1 289 ? -15.64300 1.30100   7.65500   1.000 40.52000 ? 291 PHE B CD1 1 
ATOM   4478 C CD2 . PHE B 1 289 ? -16.55300 -0.76500  8.42100   1.000 38.18000 ? 291 PHE B CD2 1 
ATOM   4479 C CE1 . PHE B 1 289 ? -16.59700 1.35400   6.65300   1.000 40.31000 ? 291 PHE B CE1 1 
ATOM   4480 C CE2 . PHE B 1 289 ? -17.51800 -0.71200  7.41800   1.000 42.00000 ? 291 PHE B CE2 1 
ATOM   4481 C CZ  . PHE B 1 289 ? -17.53200 0.34700   6.53400   1.000 36.62000 ? 291 PHE B CZ  1 
ATOM   4482 N N   . THR B 1 290 ? -11.23500 0.26000   10.34300  1.000 30.20000 ? 292 THR B N   1 
ATOM   4483 C CA  . THR B 1 290 ? -10.32700 0.45500   11.46400  1.000 32.40000 ? 292 THR B CA  1 
ATOM   4484 C C   . THR B 1 290 ? -10.84400 1.55600   12.38100  1.000 34.26000 ? 292 THR B C   1 
ATOM   4485 O O   . THR B 1 290 ? -11.73900 2.32100   12.01300  1.000 34.36000 ? 292 THR B O   1 
ATOM   4486 C CB  . THR B 1 290 ? -8.93100  0.80300   10.95400  1.000 33.95000 ? 292 THR B CB  1 
ATOM   4487 O OG1 . THR B 1 290 ? -8.96500  2.08300   10.31800  1.000 33.29000 ? 292 THR B OG1 1 
ATOM   4488 C CG2 . THR B 1 290 ? -8.43000  -0.25300  9.96300   1.000 30.83000 ? 292 THR B CG2 1 
ATOM   4489 N N   . PRO B 1 291 ? -10.29700 1.66400   13.60200  1.000 36.09000 ? 293 PRO B N   1 
ATOM   4490 C CA  . PRO B 1 291 ? -10.59700 2.85300   14.42000  1.000 38.19000 ? 293 PRO B CA  1 
ATOM   4491 C C   . PRO B 1 291 ? -10.35600 4.15400   13.67500  1.000 39.54000 ? 293 PRO B C   1 
ATOM   4492 O O   . PRO B 1 291 ? -11.18000 5.07300   13.74900  1.000 35.89000 ? 293 PRO B O   1 
ATOM   4493 C CB  . PRO B 1 291 ? -9.64800  2.70200   15.61600  1.000 33.38000 ? 293 PRO B CB  1 
ATOM   4494 C CG  . PRO B 1 291 ? -9.49300  1.22700   15.76500  1.000 33.97000 ? 293 PRO B CG  1 
ATOM   4495 C CD  . PRO B 1 291 ? -9.48100  0.68400   14.34500  1.000 33.15000 ? 293 PRO B CD  1 
ATOM   4496 N N   . PHE B 1 292 ? -9.25100  4.23900   12.93300  1.000 39.33000 ? 294 PHE B N   1 
ATOM   4497 C CA  . PHE B 1 292 ? -8.94200  5.46300   12.20100  1.000 40.96000 ? 294 PHE B CA  1 
ATOM   4498 C C   . PHE B 1 292 ? -9.96300  5.71800   11.09900  1.000 42.30000 ? 294 PHE B C   1 
ATOM   4499 O O   . PHE B 1 292 ? -10.38900 6.86200   10.90000  1.000 42.09000 ? 294 PHE B O   1 
ATOM   4500 C CB  . PHE B 1 292 ? -7.52300  5.38200   11.63800  1.000 38.59000 ? 294 PHE B CB  1 
ATOM   4501 C CG  . PHE B 1 292 ? -7.12300  6.57500   10.81500  1.000 49.05000 ? 294 PHE B CG  1 
ATOM   4502 C CD1 . PHE B 1 292 ? -7.42100  7.86400   11.23600  1.000 51.91000 ? 294 PHE B CD1 1 
ATOM   4503 C CD2 . PHE B 1 292 ? -6.43700  6.40800   9.62200   1.000 53.13000 ? 294 PHE B CD2 1 
ATOM   4504 C CE1 . PHE B 1 292 ? -7.05200  8.96700   10.47100  1.000 52.39000 ? 294 PHE B CE1 1 
ATOM   4505 C CE2 . PHE B 1 292 ? -6.06100  7.50200   8.85400   1.000 49.45000 ? 294 PHE B CE2 1 
ATOM   4506 C CZ  . PHE B 1 292 ? -6.37100  8.78400   9.28000   1.000 51.28000 ? 294 PHE B CZ  1 
ATOM   4507 N N   . ASP B 1 293 ? -10.37400 4.66500   10.37800  1.000 38.74000 ? 295 ASP B N   1 
ATOM   4508 C CA  . ASP B 1 293 ? -11.40500 4.81300   9.35200   1.000 38.30000 ? 295 ASP B CA  1 
ATOM   4509 C C   . ASP B 1 293 ? -12.67100 5.43700   9.92900   1.000 41.02000 ? 295 ASP B C   1 
ATOM   4510 O O   . ASP B 1 293 ? -13.25100 6.35400   9.33300   1.000 44.04000 ? 295 ASP B O   1 
ATOM   4511 C CB  . ASP B 1 293 ? -11.74600 3.45800   8.72700   1.000 37.50000 ? 295 ASP B CB  1 
ATOM   4512 C CG  . ASP B 1 293 ? -10.59700 2.85700   7.91200   1.000 38.11000 ? 295 ASP B CG  1 
ATOM   4513 O OD1 . ASP B 1 293 ? -9.67000  3.60300   7.53000   1.000 39.41000 ? 295 ASP B OD1 1 
ATOM   4514 O OD2 . ASP B 1 293 ? -10.63100 1.62700   7.65400   1.000 33.79000 ? 295 ASP B OD2 1 
ATOM   4515 N N   . VAL B 1 294 ? -13.10400 4.96000   11.09800  1.000 39.30000 ? 296 VAL B N   1 
ATOM   4516 C CA  . VAL B 1 294 ? -14.35400 5.43200   11.68600  1.000 37.44000 ? 296 VAL B CA  1 
ATOM   4517 C C   . VAL B 1 294 ? -14.26400 6.92200   12.01200  1.000 44.34000 ? 296 VAL B C   1 
ATOM   4518 O O   . VAL B 1 294 ? -15.21400 7.67800   11.79000  1.000 43.01000 ? 296 VAL B O   1 
ATOM   4519 C CB  . VAL B 1 294 ? -14.70900 4.59500   12.93200  1.000 36.26000 ? 296 VAL B CB  1 
ATOM   4520 C CG1 . VAL B 1 294 ? -15.85300 5.22500   13.70100  1.000 38.32000 ? 296 VAL B CG1 1 
ATOM   4521 C CG2 . VAL B 1 294 ? -15.08000 3.16300   12.53400  1.000 35.47000 ? 296 VAL B CG2 1 
ATOM   4522 N N   . VAL B 1 295 ? -13.12300 7.36900   12.53500  1.000 44.87000 ? 297 VAL B N   1 
ATOM   4523 C CA  . VAL B 1 295 ? -13.00400 8.77800   12.89400  1.000 45.15000 ? 297 VAL B CA  1 
ATOM   4524 C C   . VAL B 1 295 ? -12.82100 9.63700   11.64800  1.000 47.55000 ? 297 VAL B C   1 
ATOM   4525 O O   . VAL B 1 295 ? -13.40100 10.72500  11.54400  1.000 45.93000 ? 297 VAL B O   1 
ATOM   4526 C CB  . VAL B 1 295 ? -11.87300 8.99000   13.92400  1.000 47.15000 ? 297 VAL B CB  1 
ATOM   4527 C CG1 . VAL B 1 295 ? -11.93900 7.94500   15.02600  1.000 43.41000 ? 297 VAL B CG1 1 
ATOM   4528 C CG2 . VAL B 1 295 ? -10.49700 8.99200   13.26500  1.000 51.64000 ? 297 VAL B CG2 1 
ATOM   4529 N N   . ARG B 1 296 ? -12.03600 9.16500   10.67500  1.000 47.01000 ? 298 ARG B N   1 
ATOM   4530 C CA  . ARG B 1 296 ? -11.85800 9.93100   9.44700   1.000 47.27000 ? 298 ARG B CA  1 
ATOM   4531 C C   . ARG B 1 296 ? -13.18300 10.08800  8.71200   1.000 49.91000 ? 298 ARG B C   1 
ATOM   4532 O O   . ARG B 1 296 ? -13.49200 11.16700  8.18900   1.000 49.62000 ? 298 ARG B O   1 
ATOM   4533 C CB  . ARG B 1 296 ? -10.81600 9.26400   8.54800   1.000 46.71000 ? 298 ARG B CB  1 
ATOM   4534 N N   . GLN B 1 297 ? -13.99900 9.03200   8.70000   1.000 44.86000 ? 299 GLN B N   1 
ATOM   4535 C CA  . GLN B 1 297 ? -15.27400 9.08000   7.99300   1.000 47.10000 ? 299 GLN B CA  1 
ATOM   4536 C C   . GLN B 1 297 ? -16.29200 9.94000   8.73300   1.000 49.81000 ? 299 GLN B C   1 
ATOM   4537 O O   . GLN B 1 297 ? -17.04900 10.69700  8.10900   1.000 49.39000 ? 299 GLN B O   1 
ATOM   4538 C CB  . GLN B 1 297 ? -15.81100 7.66400   7.80000   1.000 47.39000 ? 299 GLN B CB  1 
ATOM   4539 N N   . CYS B 1 298 ? -16.33100 9.83600   10.05800  1.000 47.22000 ? 300 CYS B N   1 
ATOM   4540 C CA  . CYS B 1 298 ? -17.27600 10.61800  10.84300  1.000 48.30000 ? 300 CYS B CA  1 
ATOM   4541 C C   . CYS B 1 298 ? -16.80300 12.05600  11.08400  1.000 51.64000 ? 300 CYS B C   1 
ATOM   4542 O O   . CYS B 1 298 ? -17.53700 12.83800  11.70100  1.000 50.09000 ? 300 CYS B O   1 
ATOM   4543 C CB  . CYS B 1 298 ? -17.55600 9.90000   12.17000  1.000 48.64000 ? 300 CYS B CB  1 
ATOM   4544 S SG  . CYS B 1 298 ? -18.25800 8.19300   12.00500  1.000 49.77000 ? 300 CYS B SG  1 
ATOM   4545 N N   . SER B 1 299 ? -15.64500 12.44100  10.51700  1.000 50.02000 ? 301 SER B N   1 
ATOM   4546 C CA  . SER B 1 299 ? -15.05300 13.79900  10.68900  1.000 50.40000 ? 301 SER B CA  1 
ATOM   4547 C C   . SER B 1 299 ? -14.80800 14.51500  9.35400   1.000 48.94000 ? 301 SER B C   1 
ATOM   4548 O O   . SER B 1 299 ? -14.36300 15.66800  9.40200   1.000 49.20000 ? 301 SER B O   1 
ATOM   4549 C CB  . SER B 1 299 ? -13.78300 13.73800  11.47800  1.000 47.44000 ? 301 SER B CB  1 
ATOM   4550 O OG  . SER B 1 299 ? -12.72600 13.20200  10.70500  1.000 49.89000 ? 301 SER B OG  1 
ATOM   4551 N N   . GLY B 1 300 ? -15.07700 13.86800  8.22000   1.000 48.50000 ? 302 GLY B N   1 
ATOM   4552 C CA  . GLY B 1 300 ? -14.89700 14.44800  6.87300   1.000 44.15000 ? 302 GLY B CA  1 
ATOM   4553 C C   . GLY B 1 300 ? -13.48400 14.84900  6.48900   1.000 47.71000 ? 302 GLY B C   1 
ATOM   4554 O O   . GLY B 1 300 ? -13.34100 15.88900  5.84100   1.000 46.16000 ? 302 GLY B O   1 
ATOM   4555 N N   . VAL B 1 301 ? -12.47700 14.05000  6.84900   1.000 46.89000 ? 303 VAL B N   1 
ATOM   4556 C CA  . VAL B 1 301 ? -11.06100 14.34900  6.47100   1.000 47.31000 ? 303 VAL B CA  1 
ATOM   4557 C C   . VAL B 1 301 ? -10.93200 14.56400  4.95200   1.000 48.23000 ? 303 VAL B C   1 
ATOM   4558 O O   . VAL B 1 301 ? -11.34000 13.65200  4.22500   1.000 43.18000 ? 303 VAL B O   1 
ATOM   4559 C CB  . VAL B 1 301 ? -10.09800 13.26400  6.98000   1.000 48.72000 ? 303 VAL B CB  1 
ATOM   4560 C CG1 . VAL B 1 301 ? -8.74100  13.32700  6.30000   1.000 44.24000 ? 303 VAL B CG1 1 
ATOM   4561 C CG2 . VAL B 1 301 ? -9.94300  13.32900  8.49100   1.000 46.85000 ? 303 VAL B CG2 1 
HETATM 4562 C C02 . X77 C 2 .   ? -25.33700 21.55800  4.92400   1.000 31.33000 ? 401 X77 A C02 1 
HETATM 4563 C C04 . X77 C 2 .   ? -27.27800 20.06800  5.86100   1.000 34.35000 ? 401 X77 A C04 1 
HETATM 4564 C C05 . X77 C 2 .   ? -28.74600 19.82600  5.52400   1.000 31.07000 ? 401 X77 A C05 1 
HETATM 4565 C C07 . X77 C 2 .   ? -30.15600 20.60600  7.64200   1.000 41.50000 ? 401 X77 A C07 1 
HETATM 4566 C C08 . X77 C 2 .   ? -30.93500 21.84700  7.24800   1.000 44.59000 ? 401 X77 A C08 1 
HETATM 4567 C C09 . X77 C 2 .   ? -32.11900 21.35400  6.42700   1.000 43.97000 ? 401 X77 A C09 1 
HETATM 4568 C C10 . X77 C 2 .   ? -33.13900 20.76900  7.39700   1.000 40.08000 ? 401 X77 A C10 1 
HETATM 4569 C C11 . X77 C 2 .   ? -32.54000 19.66400  8.26900   1.000 39.10000 ? 401 X77 A C11 1 
HETATM 4570 C C12 . X77 C 2 .   ? -31.01300 19.63200  8.45300   1.000 39.17000 ? 401 X77 A C12 1 
HETATM 4571 C C14 . X77 C 2 .   ? -26.60400 18.74500  5.49200   1.000 32.93000 ? 401 X77 A C14 1 
HETATM 4572 C C15 . X77 C 2 .   ? -26.10900 17.85300  6.58200   1.000 30.73000 ? 401 X77 A C15 1 
HETATM 4573 C C16 . X77 C 2 .   ? -25.47900 16.52700  6.23100   1.000 30.42000 ? 401 X77 A C16 1 
HETATM 4574 C C17 . X77 C 2 .   ? -25.35000 16.13700  4.76000   1.000 31.34000 ? 401 X77 A C17 1 
HETATM 4575 C C19 . X77 C 2 .   ? -26.46500 18.34300  4.02400   1.000 31.48000 ? 401 X77 A C19 1 
HETATM 4576 C C20 . X77 C 2 .   ? -27.82000 22.07500  4.51900   1.000 32.18000 ? 401 X77 A C20 1 
HETATM 4577 C C21 . X77 C 2 .   ? -28.33300 21.90800  3.08700   1.000 30.29000 ? 401 X77 A C21 1 
HETATM 4578 C C22 . X77 C 2 .   ? -29.45200 22.82000  2.59400   1.000 30.20000 ? 401 X77 A C22 1 
HETATM 4579 C C23 . X77 C 2 .   ? -30.00500 23.87700  3.53500   1.000 31.60000 ? 401 X77 A C23 1 
HETATM 4580 C C24 . X77 C 2 .   ? -31.11800 24.79300  3.04600   1.000 37.19000 ? 401 X77 A C24 1 
HETATM 4581 C C25 . X77 C 2 .   ? -30.56300 26.21200  2.98000   1.000 32.28000 ? 401 X77 A C25 1 
HETATM 4582 C C26 . X77 C 2 .   ? -32.23800 24.65100  4.05600   1.000 36.86000 ? 401 X77 A C26 1 
HETATM 4583 C C27 . X77 C 2 .   ? -31.60400 24.30100  1.65700   1.000 33.80000 ? 401 X77 A C27 1 
HETATM 4584 C C28 . X77 C 2 .   ? -29.49000 24.05600  4.96800   1.000 33.57000 ? 401 X77 A C28 1 
HETATM 4585 C C29 . X77 C 2 .   ? -28.37500 23.12400  5.46400   1.000 34.83000 ? 401 X77 A C29 1 
HETATM 4586 C C30 . X77 C 2 .   ? -24.81400 22.79600  4.15100   1.000 32.25000 ? 401 X77 A C30 1 
HETATM 4587 C C31 . X77 C 2 .   ? -25.54400 23.82200  3.59500   1.000 30.04000 ? 401 X77 A C31 1 
HETATM 4588 C C33 . X77 C 2 .   ? -23.45100 24.19300  3.23100   1.000 33.13000 ? 401 X77 A C33 1 
HETATM 4589 N N03 . X77 C 2 .   ? -26.76700 21.21500  5.07500   1.000 32.31000 ? 401 X77 A N03 1 
HETATM 4590 N N06 . X77 C 2 .   ? -29.95700 20.04100  6.32400   1.000 41.68000 ? 401 X77 A N06 1 
HETATM 4591 N N18 . X77 C 2 .   ? -25.86200 17.02500  3.67600   1.000 27.29000 ? 401 X77 A N18 1 
HETATM 4592 N N32 . X77 C 2 .   ? -24.69600 24.65700  3.04200   1.000 32.41000 ? 401 X77 A N32 1 
HETATM 4593 N N34 . X77 C 2 .   ? -23.54200 23.03900  3.91700   1.000 30.37000 ? 401 X77 A N34 1 
HETATM 4594 O O01 . X77 C 2 .   ? -24.55000 20.86300  5.43100   1.000 34.19000 ? 401 X77 A O01 1 
HETATM 4595 O O13 . X77 C 2 .   ? -29.01500 19.36800  4.47800   1.000 34.29000 ? 401 X77 A O13 1 
HETATM 4596 C C02 . X77 D 2 .   ? -4.13900  -14.10500 -13.82100 1.000 37.62000 ? 401 X77 B C02 1 
HETATM 4597 C C04 . X77 D 2 .   ? -5.13200  -15.67400 -12.02500 1.000 38.16000 ? 401 X77 B C04 1 
HETATM 4598 C C05 . X77 D 2 .   ? -4.63300  -16.60900 -10.93600 1.000 37.63000 ? 401 X77 B C05 1 
HETATM 4599 C C07 . X77 D 2 .   ? -4.28800  -18.91000 -10.02300 1.000 42.16000 ? 401 X77 B C07 1 
HETATM 4600 C C08 . X77 D 2 .   ? -5.09000  -20.22100 -10.01600 1.000 42.18000 ? 401 X77 B C08 1 
HETATM 4601 C C09 . X77 D 2 .   ? -4.18500  -21.45100 -10.08600 1.000 44.76000 ? 401 X77 B C09 1 
HETATM 4602 C C10 . X77 D 2 .   ? -2.98700  -21.34100 -9.14300  1.000 43.24000 ? 401 X77 B C10 1 
HETATM 4603 C C11 . X77 D 2 .   ? -2.07500  -20.15500 -9.48400  1.000 42.73000 ? 401 X77 B C11 1 
HETATM 4604 C C12 . X77 D 2 .   ? -2.78300  -19.06400 -10.30100 1.000 39.90000 ? 401 X77 B C12 1 
HETATM 4605 C C14 . X77 D 2 .   ? -5.97600  -14.64500 -11.32100 1.000 35.92000 ? 401 X77 B C14 1 
HETATM 4606 C C15 . X77 D 2 .   ? -5.32400  -13.52800 -10.58200 1.000 33.87000 ? 401 X77 B C15 1 
HETATM 4607 C C16 . X77 D 2 .   ? -6.21300  -12.56900 -9.89200  1.000 34.61000 ? 401 X77 B C16 1 
HETATM 4608 C C17 . X77 D 2 .   ? -7.72600  -12.70800 -9.93400  1.000 36.73000 ? 401 X77 B C17 1 
HETATM 4609 C C19 . X77 D 2 .   ? -7.48600  -14.81000 -11.37200 1.000 38.48000 ? 401 X77 B C19 1 
HETATM 4610 C C20 . X77 D 2 .   ? -2.67200  -15.70100 -12.46800 1.000 39.66000 ? 401 X77 B C20 1 
HETATM 4611 C C21 . X77 D 2 .   ? -1.74300  -15.14900 -11.37100 1.000 35.10000 ? 401 X77 B C21 1 
HETATM 4612 C C22 . X77 D 2 .   ? -0.38600  -15.83300 -11.14000 1.000 36.93000 ? 401 X77 B C22 1 
HETATM 4613 C C23 . X77 D 2 .   ? 0.00400   -17.02700 -12.00500 1.000 38.48000 ? 401 X77 B C23 1 
HETATM 4614 C C24 . X77 D 2 .   ? 1.35700   -17.72000 -11.81100 1.000 39.64000 ? 401 X77 B C24 1 
HETATM 4615 C C25 . X77 D 2 .   ? 2.22600   -17.29200 -12.98700 1.000 41.60000 ? 401 X77 B C25 1 
HETATM 4616 C C26 . X77 D 2 .   ? 1.12700   -19.22700 -11.80400 1.000 40.37000 ? 401 X77 B C26 1 
HETATM 4617 C C27 . X77 D 2 .   ? 1.98400   -17.23100 -10.47800 1.000 34.64000 ? 401 X77 B C27 1 
HETATM 4618 C C28 . X77 D 2 .   ? -0.92500  -17.55900 -13.10500 1.000 40.63000 ? 401 X77 B C28 1 
HETATM 4619 C C29 . X77 D 2 .   ? -2.28000  -16.89200 -13.32900 1.000 38.09000 ? 401 X77 B C29 1 
HETATM 4620 C C30 . X77 D 2 .   ? -2.94400  -13.57800 -14.64500 1.000 38.30000 ? 401 X77 B C30 1 
HETATM 4621 C C31 . X77 D 2 .   ? -1.60400  -13.84100 -14.48400 1.000 37.41000 ? 401 X77 B C31 1 
HETATM 4622 C C33 . X77 D 2 .   ? -1.83600  -12.54900 -16.17500 1.000 39.56000 ? 401 X77 B C33 1 
HETATM 4623 N N03 . X77 D 2 .   ? -3.98400  -15.11800 -12.75500 1.000 38.05000 ? 401 X77 B N03 1 
HETATM 4624 N N06 . X77 D 2 .   ? -4.79900  -18.05300 -11.10000 1.000 39.80000 ? 401 X77 B N06 1 
HETATM 4625 N N18 . X77 D 2 .   ? -8.35400  -13.82700 -10.67500 1.000 37.41000 ? 401 X77 B N18 1 
HETATM 4626 N N32 . X77 D 2 .   ? -0.94600  -13.20500 -15.41500 1.000 33.92000 ? 401 X77 B N32 1 
HETATM 4627 N N34 . X77 D 2 .   ? -3.06300  -12.79800 -15.68500 1.000 38.42000 ? 401 X77 B N34 1 
HETATM 4628 O O01 . X77 D 2 .   ? -5.22200  -13.68300 -14.05300 1.000 39.44000 ? 401 X77 B O01 1 
HETATM 4629 O O13 . X77 D 2 .   ? -4.13300  -16.19300 -9.94500  1.000 35.64000 ? 401 X77 B O13 1 
HETATM 4630 O O   . HOH E 3 .   ? -47.01800 -17.71500 -5.28300  1.000 29.44000 ? 501 HOH A O   1 
HETATM 4631 O O   . HOH E 3 .   ? -14.56100 29.63000  -1.64200  1.000 33.79000 ? 502 HOH A O   1 
HETATM 4632 O O   . HOH E 3 .   ? -43.574   -29.986   -3.053    1.000 34.40000 ? 503 HOH A O   1 
HETATM 4633 O O   . HOH E 3 .   ? -18.63800 12.08300  3.71000   1.000 33.46000 ? 504 HOH A O   1 
HETATM 4634 O O   . HOH E 3 .   ? -28.75800 4.70700   -1.80100  1.000 32.03000 ? 505 HOH A O   1 
HETATM 4635 O O   . HOH E 3 .   ? -39.68900 -29.32700 -3.33800  1.000 40.23000 ? 506 HOH A O   1 
HETATM 4636 O O   . HOH E 3 .   ? -36.78800 32.48500  5.52500   1.000 40.67000 ? 507 HOH A O   1 
HETATM 4637 O O   . HOH E 3 .   ? -34.78800 38.36500  -0.47300  1.000 38.17000 ? 508 HOH A O   1 
HETATM 4638 O O   . HOH E 3 .   ? -29.59000 -16.49300 8.88400   1.000 41.33000 ? 509 HOH A O   1 
HETATM 4639 O O   . HOH E 3 .   ? -34.98000 -8.30500  1.45700   1.000 27.76000 ? 510 HOH A O   1 
HETATM 4640 O O   . HOH E 3 .   ? -18.01500 15.38300  -6.00300  1.000 28.88000 ? 511 HOH A O   1 
HETATM 4641 O O   . HOH E 3 .   ? -17.88900 22.30100  1.90800   1.000 29.46000 ? 512 HOH A O   1 
HETATM 4642 O O   . HOH E 3 .   ? -42.63500 -15.52900 0.44700   1.000 29.46000 ? 513 HOH A O   1 
HETATM 4643 O O   . HOH E 3 .   ? -30.35900 24.40400  -3.71100  1.000 26.96000 ? 514 HOH A O   1 
HETATM 4644 O O   . HOH E 3 .   ? -27.68400 15.27800  -14.63600 1.000 31.78000 ? 515 HOH A O   1 
HETATM 4645 O O   . HOH E 3 .   ? -49.57400 -8.09500  -2.38300  1.000 37.84000 ? 516 HOH A O   1 
HETATM 4646 O O   . HOH E 3 .   ? -10.65100 15.87000  -14.46300 1.000 34.31000 ? 517 HOH A O   1 
HETATM 4647 O O   . HOH E 3 .   ? -44.17800 -17.65400 1.42700   1.000 30.88000 ? 518 HOH A O   1 
HETATM 4648 O O   . HOH E 3 .   ? -51.70100 -17.94900 -10.51800 1.000 36.27000 ? 519 HOH A O   1 
HETATM 4649 O O   . HOH E 3 .   ? -36.44000 -16.35600 -18.48500 1.000 40.52000 ? 520 HOH A O   1 
HETATM 4650 O O   . HOH E 3 .   ? -23.02900 2.41500   -11.47700 1.000 30.30000 ? 521 HOH A O   1 
HETATM 4651 O O   . HOH E 3 .   ? -43.10000 -15.64400 4.90800   1.000 31.43000 ? 522 HOH A O   1 
HETATM 4652 O O   . HOH E 3 .   ? -39.85900 -22.13500 -15.88100 1.000 41.58000 ? 523 HOH A O   1 
HETATM 4653 O O   . HOH E 3 .   ? -49.25000 -19.03400 -6.61700  1.000 32.98000 ? 524 HOH A O   1 
HETATM 4654 O O   . HOH E 3 .   ? -11.64500 8.73700   -13.43500 1.000 32.05000 ? 525 HOH A O   1 
HETATM 4655 O O   . HOH E 3 .   ? -28.29800 -5.77500  -6.41700  1.000 27.46000 ? 526 HOH A O   1 
HETATM 4656 O O   . HOH E 3 .   ? -50.98400 -15.57700 -11.58400 1.000 34.35000 ? 527 HOH A O   1 
HETATM 4657 O O   . HOH E 3 .   ? -27.17600 22.57200  -16.51900 1.000 34.62000 ? 528 HOH A O   1 
HETATM 4658 O O   . HOH E 3 .   ? -46.09300 -14.68300 -15.78900 1.000 34.61000 ? 529 HOH A O   1 
HETATM 4659 O O   . HOH E 3 .   ? -33.37200 13.44400  -4.17500  1.000 27.81000 ? 530 HOH A O   1 
HETATM 4660 O O   . HOH E 3 .   ? -37.12800 26.16700  -2.06700  1.000 33.94000 ? 531 HOH A O   1 
HETATM 4661 O O   . HOH E 3 .   ? -32.10000 -1.17300  -11.83700 1.000 32.88000 ? 532 HOH A O   1 
HETATM 4662 O O   . HOH E 3 .   ? -44.30100 -18.92500 -15.16000 1.000 37.64000 ? 533 HOH A O   1 
HETATM 4663 O O   . HOH E 3 .   ? -26.00900 26.75500  1.69800   1.000 32.60000 ? 534 HOH A O   1 
HETATM 4664 O O   . HOH E 3 .   ? -37.78300 -3.98500  -9.53200  1.000 31.97000 ? 535 HOH A O   1 
HETATM 4665 O O   . HOH E 3 .   ? -36.64200 20.64200  -8.31500  1.000 30.73000 ? 536 HOH A O   1 
HETATM 4666 O O   . HOH E 3 .   ? -35.92100 -21.56300 -8.44600  1.000 32.63000 ? 537 HOH A O   1 
HETATM 4667 O O   . HOH E 3 .   ? -47.78800 -7.95200  -12.00500 1.000 34.17000 ? 538 HOH A O   1 
HETATM 4668 O O   . HOH E 3 .   ? -27.93500 7.78900   4.34300   1.000 37.22000 ? 539 HOH A O   1 
HETATM 4669 O O   . HOH E 3 .   ? -38.96000 -16.38800 -17.06600 1.000 36.80000 ? 540 HOH A O   1 
HETATM 4670 O O   . HOH E 3 .   ? -24.88400 8.71600   -14.61000 1.000 34.75000 ? 541 HOH A O   1 
HETATM 4671 O O   . HOH E 3 .   ? -43.06700 -3.17800  -18.62000 1.000 43.12000 ? 542 HOH A O   1 
HETATM 4672 O O   . HOH E 3 .   ? -47.26300 -18.97000 -9.77600  1.000 29.52000 ? 543 HOH A O   1 
HETATM 4673 O O   . HOH E 3 .   ? -41.03400 -20.54800 -4.75700  1.000 27.72000 ? 544 HOH A O   1 
HETATM 4674 O O   . HOH E 3 .   ? -18.36300 1.43200   -2.73100  1.000 33.85000 ? 545 HOH A O   1 
HETATM 4675 O O   . HOH E 3 .   ? -43.95900 -21.17700 -0.78900  1.000 28.22000 ? 546 HOH A O   1 
HETATM 4676 O O   . HOH E 3 .   ? -43.84200 -24.16200 -9.48700  1.000 31.74000 ? 547 HOH A O   1 
HETATM 4677 O O   . HOH E 3 .   ? -32.83000 -9.45500  3.05100   1.000 34.51000 ? 548 HOH A O   1 
HETATM 4678 O O   . HOH E 3 .   ? -24.88500 37.39600  -14.82800 1.000 37.80000 ? 549 HOH A O   1 
HETATM 4679 O O   . HOH E 3 .   ? -37.76400 21.30700  -6.21800  1.000 32.54000 ? 550 HOH A O   1 
HETATM 4680 O O   . HOH E 3 .   ? -37.62700 32.32100  -6.76400  1.000 37.22000 ? 551 HOH A O   1 
HETATM 4681 O O   . HOH E 3 .   ? -48.57200 -13.39200 -14.60100 1.000 35.29000 ? 552 HOH A O   1 
HETATM 4682 O O   . HOH E 3 .   ? -45.68000 -19.87900 -7.71800  1.000 30.56000 ? 553 HOH A O   1 
HETATM 4683 O O   . HOH E 3 .   ? -37.69300 30.68900  -4.73300  1.000 34.74000 ? 554 HOH A O   1 
HETATM 4684 O O   . HOH E 3 .   ? -44.443   23.220    -0.343    1.000 41.83000 ? 555 HOH A O   1 
HETATM 4685 O O   . HOH E 3 .   ? -37.27000 23.48500  -4.80100  1.000 32.81000 ? 556 HOH A O   1 
HETATM 4686 O O   . HOH E 3 .   ? -12.04500 8.04400   2.66500   1.000 36.49000 ? 557 HOH A O   1 
HETATM 4687 O O   . HOH E 3 .   ? -34.20200 -21.19600 1.34600   1.000 33.27000 ? 558 HOH A O   1 
HETATM 4688 O O   . HOH E 3 .   ? -42.73200 -19.86800 -6.36500  1.000 30.01000 ? 559 HOH A O   1 
HETATM 4689 O O   . HOH E 3 .   ? -7.22100  14.37000  -10.40500 1.000 44.01000 ? 560 HOH A O   1 
HETATM 4690 O O   . HOH E 3 .   ? -34.71000 -0.43900  -11.95300 1.000 40.29000 ? 561 HOH A O   1 
HETATM 4691 O O   . HOH E 3 .   ? -41.57900 -20.47100 -2.19400  1.000 31.93000 ? 562 HOH A O   1 
HETATM 4692 O O   . HOH E 3 .   ? -37.08500 -1.09800  -9.44400  1.000 36.68000 ? 563 HOH A O   1 
HETATM 4693 O O   . HOH E 3 .   ? -47.84000 -20.96900 -11.26700 1.000 33.12000 ? 564 HOH A O   1 
HETATM 4694 O O   . HOH E 3 .   ? -40.58400 -18.83100 -17.63800 1.000 45.00000 ? 565 HOH A O   1 
HETATM 4695 O O   . HOH F 3 .   ? -2.46300  -12.17400 11.41000  1.000 38.18000 ? 501 HOH B O   1 
HETATM 4696 O O   . HOH F 3 .   ? -10.05700 -8.09400  2.51000   1.000 35.98000 ? 502 HOH B O   1 
HETATM 4697 O O   . HOH F 3 .   ? 0.56600   8.38300   2.76100   1.000 36.14000 ? 503 HOH B O   1 
HETATM 4698 O O   . HOH F 3 .   ? 4.86000   -1.34400  -0.03300  1.000 27.84000 ? 504 HOH B O   1 
HETATM 4699 O O   . HOH F 3 .   ? 7.53200   -0.93500  -24.25800 1.000 50.68000 ? 505 HOH B O   1 
HETATM 4700 O O   . HOH F 3 .   ? -7.66700  2.91800   4.78200   1.000 31.51000 ? 506 HOH B O   1 
HETATM 4701 O O   . HOH F 3 .   ? -6.87500  2.85300   9.00800   1.000 40.77000 ? 507 HOH B O   1 
HETATM 4702 O O   . HOH F 3 .   ? -7.26600  -2.78900  12.50400  1.000 31.49000 ? 508 HOH B O   1 
HETATM 4703 O O   . HOH F 3 .   ? -12.25800 0.93700   5.72600   1.000 34.71000 ? 509 HOH B O   1 
HETATM 4704 O O   . HOH F 3 .   ? 5.60000   -15.27400 2.82100   1.000 29.75000 ? 510 HOH B O   1 
HETATM 4705 O O   . HOH F 3 .   ? -0.70100  -21.61400 -6.85200  1.000 39.66000 ? 511 HOH B O   1 
HETATM 4706 O O   . HOH F 3 .   ? 10.19200  4.78000   -8.98100  1.000 33.36000 ? 512 HOH B O   1 
HETATM 4707 O O   . HOH F 3 .   ? 6.26000   -16.40400 0.68100   1.000 31.16000 ? 513 HOH B O   1 
HETATM 4708 O O   . HOH F 3 .   ? -1.40900  -11.80600 0.31500   1.000 28.96000 ? 514 HOH B O   1 
HETATM 4709 O O   . HOH F 3 .   ? 5.08800   -12.57200 -9.39700  1.000 27.44000 ? 515 HOH B O   1 
HETATM 4710 O O   . HOH F 3 .   ? 11.36300  -11.40200 0.33300   1.000 27.71000 ? 516 HOH B O   1 
HETATM 4711 O O   . HOH F 3 .   ? -0.87500  2.11800   2.67300   1.000 27.14000 ? 517 HOH B O   1 
HETATM 4712 O O   . HOH F 3 .   ? -15.13300 -2.83300  11.13400  1.000 30.83000 ? 518 HOH B O   1 
HETATM 4713 O O   . HOH F 3 .   ? 13.82200  -12.33700 -6.73400  1.000 29.92000 ? 519 HOH B O   1 
HETATM 4714 O O   . HOH F 3 .   ? 1.52700   9.97200   -17.20100 1.000 43.33000 ? 520 HOH B O   1 
HETATM 4715 O O   . HOH F 3 .   ? -2.30800  2.26900   -19.66800 1.000 47.26000 ? 521 HOH B O   1 
HETATM 4716 O O   . HOH F 3 .   ? 7.76800   -19.17500 -7.10900  1.000 34.86000 ? 522 HOH B O   1 
HETATM 4717 O O   . HOH F 3 .   ? 1.12200   14.13700  -4.61300  1.000 33.19000 ? 523 HOH B O   1 
HETATM 4718 O O   . HOH F 3 .   ? -9.27100  -15.86900 3.23100   1.000 39.02000 ? 524 HOH B O   1 
HETATM 4719 O O   . HOH F 3 .   ? -1.80400  -15.54000 9.70900   1.000 34.34000 ? 525 HOH B O   1 
HETATM 4720 O O   . HOH F 3 .   ? 7.52800   11.01400  -3.34900  1.000 31.00000 ? 526 HOH B O   1 
HETATM 4721 O O   . HOH F 3 .   ? -17.58800 6.13600   6.02100   1.000 50.52000 ? 527 HOH B O   1 
HETATM 4722 O O   . HOH F 3 .   ? -15.50000 0.40200   -1.07700  1.000 35.12000 ? 528 HOH B O   1 
HETATM 4723 O O   . HOH F 3 .   ? 2.66800   -7.52400  8.05700   1.000 32.79000 ? 529 HOH B O   1 
HETATM 4724 O O   . HOH F 3 .   ? 15.98400  -8.93600  -1.74500  1.000 32.18000 ? 530 HOH B O   1 
HETATM 4725 O O   . HOH F 3 .   ? 12.54400  -5.72200  1.09300   1.000 32.55000 ? 531 HOH B O   1 
HETATM 4726 O O   . HOH F 3 .   ? 3.52400   -12.25200 5.75500   1.000 27.52000 ? 532 HOH B O   1 
HETATM 4727 O O   . HOH F 3 .   ? 7.30800   -16.63300 -3.91600  1.000 29.62000 ? 533 HOH B O   1 
HETATM 4728 O O   . HOH F 3 .   ? 15.82100  -9.28800  -4.61900  1.000 33.75000 ? 534 HOH B O   1 
HETATM 4729 O O   . HOH F 3 .   ? -5.19200  1.19800   7.53500   1.000 35.45000 ? 535 HOH B O   1 
HETATM 4730 O O   . HOH F 3 .   ? -8.22300  -7.27200  17.17700  1.000 32.81000 ? 536 HOH B O   1 
HETATM 4731 O O   . HOH F 3 .   ? 15.33900  -6.16100  -0.94300  1.000 37.04000 ? 537 HOH B O   1 
HETATM 4732 O O   . HOH F 3 .   ? -10.78000 5.73700   3.00400   1.000 37.98000 ? 538 HOH B O   1 
HETATM 4733 O O   . HOH F 3 .   ? 4.37300   -10.13100 7.90500   1.000 39.08000 ? 539 HOH B O   1 
HETATM 4734 O O   . HOH F 3 .   ? 6.26800   -12.37800 5.77900   1.000 31.37000 ? 540 HOH B O   1 
HETATM 4735 O O   . HOH F 3 .   ? 7.55900   -13.23600 3.07400   1.000 34.50000 ? 541 HOH B O   1 
# 
