data_8YKM
# 
_entry.id   8YKM 
# 
_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   8YKM         pdb_00008ykm 10.2210/pdb8ykm/pdb 
WWPDB D_1300043864 ?            ?                   
# 
_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                        8YKM 
_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 
'Zeng, P.'  1 ? 
'Zhang, J.' 2 ? 
'Li, J.'    3 ? 
# 
_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 '3C-like proteinase nsp5'                                                                                    
33091.777 2   3.4.22.69 G15S ? ? 
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    113 ?         ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_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       
;FRKMAFPSGKVESCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSM
QNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYM
HHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPL
TQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQC
;
_entity_poly.pdbx_seq_one_letter_code_can   
;FRKMAFPSGKVESCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSM
QNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYM
HHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPL
TQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQC
;
_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  SER 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 
# 
_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                   298 
_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  SER 13  15  15  SER SER 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 298 300 300 CYS CYS 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  SER 13  15  15  SER SER 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 
# 
_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 39  HOH HOH A . 
E 3 HOH 2  502 68  HOH HOH A . 
E 3 HOH 3  503 74  HOH HOH A . 
E 3 HOH 4  504 25  HOH HOH A . 
E 3 HOH 5  505 88  HOH HOH A . 
E 3 HOH 6  506 90  HOH HOH A . 
E 3 HOH 7  507 65  HOH HOH A . 
E 3 HOH 8  508 26  HOH HOH A . 
E 3 HOH 9  509 19  HOH HOH A . 
E 3 HOH 10 510 55  HOH HOH A . 
E 3 HOH 11 511 12  HOH HOH A . 
E 3 HOH 12 512 80  HOH HOH A . 
E 3 HOH 13 513 21  HOH HOH A . 
E 3 HOH 14 514 6   HOH HOH A . 
E 3 HOH 15 515 7   HOH HOH A . 
E 3 HOH 16 516 45  HOH HOH A . 
E 3 HOH 17 517 76  HOH HOH A . 
E 3 HOH 18 518 37  HOH HOH A . 
E 3 HOH 19 519 59  HOH HOH A . 
E 3 HOH 20 520 108 HOH HOH A . 
E 3 HOH 21 521 43  HOH HOH A . 
E 3 HOH 22 522 104 HOH HOH A . 
E 3 HOH 23 523 33  HOH HOH A . 
E 3 HOH 24 524 46  HOH HOH A . 
E 3 HOH 25 525 58  HOH HOH A . 
E 3 HOH 26 526 34  HOH HOH A . 
E 3 HOH 27 527 60  HOH HOH A . 
E 3 HOH 28 528 22  HOH HOH A . 
E 3 HOH 29 529 83  HOH HOH A . 
E 3 HOH 30 530 53  HOH HOH A . 
E 3 HOH 31 531 93  HOH HOH A . 
E 3 HOH 32 532 38  HOH HOH A . 
E 3 HOH 33 533 71  HOH HOH A . 
E 3 HOH 34 534 98  HOH HOH A . 
E 3 HOH 35 535 84  HOH HOH A . 
E 3 HOH 36 536 94  HOH HOH A . 
E 3 HOH 37 537 20  HOH HOH A . 
E 3 HOH 38 538 105 HOH HOH A . 
E 3 HOH 39 539 103 HOH HOH A . 
E 3 HOH 40 540 14  HOH HOH A . 
E 3 HOH 41 541 109 HOH HOH A . 
E 3 HOH 42 542 78  HOH HOH A . 
E 3 HOH 43 543 86  HOH HOH A . 
E 3 HOH 44 544 75  HOH HOH A . 
E 3 HOH 45 545 18  HOH HOH A . 
E 3 HOH 46 546 8   HOH HOH A . 
E 3 HOH 47 547 99  HOH HOH A . 
E 3 HOH 48 548 87  HOH HOH A . 
E 3 HOH 49 549 9   HOH HOH A . 
E 3 HOH 50 550 57  HOH HOH A . 
E 3 HOH 51 551 35  HOH HOH A . 
E 3 HOH 52 552 91  HOH HOH A . 
E 3 HOH 53 553 49  HOH HOH A . 
E 3 HOH 54 554 41  HOH HOH A . 
E 3 HOH 55 555 16  HOH HOH A . 
E 3 HOH 56 556 97  HOH HOH A . 
E 3 HOH 57 557 48  HOH HOH A . 
E 3 HOH 58 558 47  HOH HOH A . 
E 3 HOH 59 559 64  HOH HOH A . 
E 3 HOH 60 560 52  HOH HOH A . 
E 3 HOH 61 561 101 HOH HOH A . 
E 3 HOH 62 562 111 HOH HOH A . 
E 3 HOH 63 563 73  HOH HOH A . 
E 3 HOH 64 564 4   HOH HOH A . 
E 3 HOH 65 565 61  HOH HOH A . 
E 3 HOH 66 566 42  HOH HOH A . 
E 3 HOH 67 567 67  HOH HOH A . 
E 3 HOH 68 568 85  HOH HOH A . 
E 3 HOH 69 569 110 HOH HOH A . 
F 3 HOH 1  501 81  HOH HOH B . 
F 3 HOH 2  502 31  HOH HOH B . 
F 3 HOH 3  503 100 HOH HOH B . 
F 3 HOH 4  504 62  HOH HOH B . 
F 3 HOH 5  505 24  HOH HOH B . 
F 3 HOH 6  506 113 HOH HOH B . 
F 3 HOH 7  507 32  HOH HOH B . 
F 3 HOH 8  508 102 HOH HOH B . 
F 3 HOH 9  509 2   HOH HOH B . 
F 3 HOH 10 510 69  HOH HOH B . 
F 3 HOH 11 511 11  HOH HOH B . 
F 3 HOH 12 512 15  HOH HOH B . 
F 3 HOH 13 513 66  HOH HOH B . 
F 3 HOH 14 514 70  HOH HOH B . 
F 3 HOH 15 515 92  HOH HOH B . 
F 3 HOH 16 516 10  HOH HOH B . 
F 3 HOH 17 517 36  HOH HOH B . 
F 3 HOH 18 518 96  HOH HOH B . 
F 3 HOH 19 519 3   HOH HOH B . 
F 3 HOH 20 520 5   HOH HOH B . 
F 3 HOH 21 521 56  HOH HOH B . 
F 3 HOH 22 522 23  HOH HOH B . 
F 3 HOH 23 523 17  HOH HOH B . 
F 3 HOH 24 524 30  HOH HOH B . 
F 3 HOH 25 525 29  HOH HOH B . 
F 3 HOH 26 526 51  HOH HOH B . 
F 3 HOH 27 527 72  HOH HOH B . 
F 3 HOH 28 528 89  HOH HOH B . 
F 3 HOH 29 529 63  HOH HOH B . 
F 3 HOH 30 530 44  HOH HOH B . 
F 3 HOH 31 531 107 HOH HOH B . 
F 3 HOH 32 532 13  HOH HOH B . 
F 3 HOH 33 533 1   HOH HOH B . 
F 3 HOH 34 534 54  HOH HOH B . 
F 3 HOH 35 535 112 HOH HOH B . 
F 3 HOH 36 536 27  HOH HOH B . 
F 3 HOH 37 537 79  HOH HOH B . 
F 3 HOH 38 538 95  HOH HOH B . 
F 3 HOH 39 539 28  HOH HOH B . 
F 3 HOH 40 540 106 HOH HOH B . 
F 3 HOH 41 541 40  HOH HOH B . 
F 3 HOH 42 542 77  HOH HOH B . 
F 3 HOH 43 543 82  HOH HOH B . 
F 3 HOH 44 544 50  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 ARG 76  ? CG  ? A ARG 74  CG  
5  1 Y 1 A ARG 76  ? CD  ? A ARG 74  CD  
6  1 Y 1 A ARG 76  ? NE  ? A ARG 74  NE  
7  1 Y 1 A ARG 76  ? CZ  ? A ARG 74  CZ  
8  1 Y 1 A ARG 76  ? NH1 ? A ARG 74  NH1 
9  1 Y 1 A ARG 76  ? NH2 ? A ARG 74  NH2 
10 1 Y 1 A LYS 100 ? CG  ? A LYS 98  CG  
11 1 Y 1 A LYS 100 ? CD  ? A LYS 98  CD  
12 1 Y 1 A LYS 100 ? CE  ? A LYS 98  CE  
13 1 Y 1 A LYS 100 ? NZ  ? A LYS 98  NZ  
14 1 Y 1 A LYS 137 ? CG  ? A LYS 135 CG  
15 1 Y 1 A LYS 137 ? CD  ? A LYS 135 CD  
16 1 Y 1 A LYS 137 ? CE  ? A LYS 135 CE  
17 1 Y 1 A LYS 137 ? NZ  ? A LYS 135 NZ  
18 1 Y 1 A TYR 154 ? CG  ? A TYR 152 CG  
19 1 Y 1 A TYR 154 ? CD1 ? A TYR 152 CD1 
20 1 Y 1 A TYR 154 ? CD2 ? A TYR 152 CD2 
21 1 Y 1 A TYR 154 ? CE1 ? A TYR 152 CE1 
22 1 Y 1 A TYR 154 ? CE2 ? A TYR 152 CE2 
23 1 Y 1 A TYR 154 ? CZ  ? A TYR 152 CZ  
24 1 Y 1 A TYR 154 ? OH  ? A TYR 152 OH  
25 1 Y 1 B ASN 72  ? CG  ? B ASN 70  CG  
26 1 Y 1 B ASN 72  ? OD1 ? B ASN 70  OD1 
27 1 Y 1 B ASN 72  ? ND2 ? B ASN 70  ND2 
28 1 Y 1 B GLN 74  ? CG  ? B GLN 72  CG  
29 1 Y 1 B GLN 74  ? CD  ? B GLN 72  CD  
30 1 Y 1 B GLN 74  ? OE1 ? B GLN 72  OE1 
31 1 Y 1 B GLN 74  ? NE2 ? B GLN 72  NE2 
32 1 Y 1 B ARG 76  ? CG  ? B ARG 74  CG  
33 1 Y 1 B ARG 76  ? CD  ? B ARG 74  CD  
34 1 Y 1 B ARG 76  ? NE  ? B ARG 74  NE  
35 1 Y 1 B ARG 76  ? CZ  ? B ARG 74  CZ  
36 1 Y 1 B ARG 76  ? NH1 ? B ARG 74  NH1 
37 1 Y 1 B ARG 76  ? NH2 ? B ARG 74  NH2 
38 1 Y 1 B LYS 100 ? CG  ? B LYS 98  CG  
39 1 Y 1 B LYS 100 ? CD  ? B LYS 98  CD  
40 1 Y 1 B LYS 100 ? CE  ? B LYS 98  CE  
41 1 Y 1 B LYS 100 ? NZ  ? B LYS 98  NZ  
42 1 Y 1 B LYS 137 ? CG  ? B LYS 135 CG  
43 1 Y 1 B LYS 137 ? CD  ? B LYS 135 CD  
44 1 Y 1 B LYS 137 ? CE  ? B LYS 135 CE  
45 1 Y 1 B LYS 137 ? NZ  ? B LYS 135 NZ  
46 1 Y 1 B TYR 154 ? CG  ? B TYR 152 CG  
47 1 Y 1 B TYR 154 ? CD1 ? B TYR 152 CD1 
48 1 Y 1 B TYR 154 ? CD2 ? B TYR 152 CD2 
49 1 Y 1 B TYR 154 ? CE1 ? B TYR 152 CE1 
50 1 Y 1 B TYR 154 ? CE2 ? B TYR 152 CE2 
51 1 Y 1 B TYR 154 ? CZ  ? B TYR 152 CZ  
52 1 Y 1 B TYR 154 ? OH  ? B TYR 152 OH  
53 1 Y 1 B ARG 298 ? CG  ? B ARG 296 CG  
54 1 Y 1 B ARG 298 ? CD  ? B ARG 296 CD  
55 1 Y 1 B ARG 298 ? NE  ? B ARG 296 NE  
56 1 Y 1 B ARG 298 ? CZ  ? B ARG 296 CZ  
57 1 Y 1 B ARG 298 ? NH1 ? B ARG 296 NH1 
58 1 Y 1 B ARG 298 ? NH2 ? B ARG 296 NH2 
# 
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                     8YKM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.810 
_cell.length_a_esd                 ? 
_cell.length_b                     101.039 
_cell.length_b_esd                 ? 
_cell.length_c                     104.448 
_cell.length_c_esd                 ? 
_cell.volume                       715620.729 
_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                         8YKM 
_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                   8YKM 
_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             2.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.56 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20~24%PEG3350,0.12~0.21M sodium sulfate' 
_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         2023-04-30 
_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   0.979183 
_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        0.979183 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          29.1134745389 
_reflns.entry_id                                       8YKM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.84 
_reflns.d_resolution_low                               72.62 
_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                                     60848 
_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                           96.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.7 
_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                              0.076 
_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                                    1.84 
_reflns_shell.d_res_low                                     1.94 
_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                             9063 
_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                                  0.863 
_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                               34.1673857708 
_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                                 8YKM 
_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                            1.84 
_refine.ls_d_res_low                             72.62 
_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                     60730 
_refine.ls_number_reflns_R_free                  3038 
_refine.ls_number_reflns_R_work                  57692 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.4243752183 
_refine.ls_percent_reflns_R_free                 5.00246994895 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.209345398504 
_refine.ls_R_factor_R_free                       0.236968352824 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.207895368139 
_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                          1.34409479497 
_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                 25.1734640527 
_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                            0.172629420856 
_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                       1.84 
_refine_hist.d_res_low                        72.62 
_refine_hist.number_atoms_solvent             113 
_refine_hist.number_atoms_total               4753 
_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        4572 
_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' ? 0.00672139384333 ? 4742 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.881363675649   ? 6460 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0528747991182  ? 732  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.00626864407295 ? 836  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 8.01876775965    ? 2762 ? 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' 1.84   1.8682 . . 136 2650 99.9641191245 . . . . 0.264775507508 . . . . . . . . . . . 0.29709782462  
'X-RAY DIFFRACTION' 1.8682 1.8988 . . 151 2677 99.8587570621 . . . . 0.262667553726 . . . . . . . . . . . 0.345558298571 
'X-RAY DIFFRACTION' 1.8988 1.9315 . . 148 2683 99.7182106375 . . . . 0.274721757162 . . . . . . . . . . . 0.263548839869 
'X-RAY DIFFRACTION' 1.9315 1.9667 . . 127 2672 99.6085409253 . . . . 0.250209369647 . . . . . . . . . . . 0.272192016649 
'X-RAY DIFFRACTION' 1.9667 2.0045 . . 142 2693 99.6835443038 . . . . 0.232330546903 . . . . . . . . . . . 0.296859555644 
'X-RAY DIFFRACTION' 2.0045 2.0454 . . 147 2677 99.8938804386 . . . . 0.236390160523 . . . . . . . . . . . 0.244220966597 
'X-RAY DIFFRACTION' 2.0454 2.0899 . . 106 1995 74.768683274  . . . . 0.229898026315 . . . . . . . . . . . 0.259323572785 
'X-RAY DIFFRACTION' 2.0899 2.1385 . . 171 2696 99.9302892994 . . . . 0.224268381966 . . . . . . . . . . . 0.25781655627  
'X-RAY DIFFRACTION' 2.1385 2.192  . . 154 2668 99.9645766915 . . . . 0.216173798517 . . . . . . . . . . . 0.243196640007 
'X-RAY DIFFRACTION' 2.192  2.2513 . . 119 2363 99.1214057508 . . . . 0.226696797546 . . . . . . . . . . . 0.264293054259 
'X-RAY DIFFRACTION' 2.2513 2.3175 . . 129 2562 99.7405485545 . . . . 0.230330634522 . . . . . . . . . . . 0.259032296194 
'X-RAY DIFFRACTION' 2.3175 2.3923 . . 139 2714 99.8250524843 . . . . 0.235489832621 . . . . . . . . . . . 0.306010687151 
'X-RAY DIFFRACTION' 2.3923 2.4778 . . 127 2700 99.9293036409 . . . . 0.234503057671 . . . . . . . . . . . 0.247063120003 
'X-RAY DIFFRACTION' 2.4778 2.577  . . 138 2709 99.9297999298 . . . . 0.234749593235 . . . . . . . . . . . 0.274559322184 
'X-RAY DIFFRACTION' 2.577  2.6943 . . 108 2471 90.0803353126 . . . . 0.244795830041 . . . . . . . . . . . 0.27702579159  
'X-RAY DIFFRACTION' 2.6943 2.8364 . . 121 2756 100.0         . . . . 0.237180574736 . . . . . . . . . . . 0.216987895403 
'X-RAY DIFFRACTION' 2.8364 3.0141 . . 156 2700 99.9649982499 . . . . 0.239660457382 . . . . . . . . . . . 0.269610043685 
'X-RAY DIFFRACTION' 3.0141 3.2468 . . 162 2729 99.9654218534 . . . . 0.248828189836 . . . . . . . . . . . 0.264889827137 
'X-RAY DIFFRACTION' 3.2468 3.5735 . . 130 2448 88.7741046832 . . . . 0.21052946531  . . . . . . . . . . . 0.236593343976 
'X-RAY DIFFRACTION' 3.5735 4.0906 . . 127 2421 88.1966078228 . . . . 0.186551503981 . . . . . . . . . . . 0.207670332227 
'X-RAY DIFFRACTION' 4.0906 5.1535 . . 142 2806 99.9660902001 . . . . 0.147826480557 . . . . . . . . . . . 0.187713110013 
'X-RAY DIFFRACTION' 5.1535 72.62  . . 158 2902 98.8691437803 . . . . 0.167758427511 . . . . . . . . . . . 0.193235308548 
# 
_struct.entry_id                     8YKM 
_struct.title                        'Crystal structure of SARS-Cov-2 main protease G15S mutant 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        8YKM 
_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
TQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQC
;
_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 8YKM A 1 ? 298 ? P0DTC1 3266 ? 3563 ? 3 300 
2 1 8YKM B 1 ? 298 ? P0DTC1 3266 ? 3563 ? 3 300 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8YKM SER A 13 ? UNP P0DTC1 GLY 3278 'engineered mutation' 15 1 
2 8YKM SER B 13 ? UNP P0DTC1 GLY 3278 'engineered mutation' 15 2 
# 
_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)' 2110  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  24760 ? 
# 
_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   ? SER A 13  ? SER A 10  SER 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  ? HIS A 62  ? SER A 62  HIS A 64  5 ? 3  
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 ? LEU A 248 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 248 ? GLY A 256 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 258 ? GLY A 273 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 290 ? CYS A 298 ? THR A 292 CYS A 300 1 ? 9  
HELX_P HELX_P12 AB3 SER B 8   ? SER B 13  ? SER B 10  SER B 15  1 ? 6  
HELX_P HELX_P13 AB4 HIS B 39  ? CYS B 42  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P14 AB5 ASN B 51  ? LYS B 59  ? ASN B 53  LYS B 61  1 ? 9  
HELX_P HELX_P15 AB6 SER B 60  ? HIS B 62  ? SER B 62  HIS B 64  5 ? 3  
HELX_P HELX_P16 AB7 ILE B 198 ? ASN B 212 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P17 AB8 THR B 224 ? TYR B 235 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P18 AB9 THR B 241 ? LEU B 248 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P19 AC1 LEU B 248 ? THR B 255 ? LEU B 250 THR B 257 1 ? 8  
HELX_P HELX_P20 AC2 ALA B 258 ? GLY B 273 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P21 AC3 THR B 290 ? GLN B 297 ? THR B 292 GLN B 299 1 ? 8  
# 
_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 PHE A 64  ? ALA A 68  ? PHE A 66  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 VAL A 155 ? GLU A 164 ? VAL A 157 GLU A 166 
AA2 3 VAL A 146 ? ASN A 149 ? VAL A 148 ASN A 151 
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 VAL A 155 ? GLU A 164 ? VAL A 157 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 VAL A 71  ? O VAL A 73  N ALA A 68  ? N ALA A 70  
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 28  ? N LEU A 30  O TYR A 35  ? O TYR A 37  
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 163 ? N MET A 165 O ALA A 171 ? O ALA A 173 
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 ALA B 114 ? N ALA B 116 O SER B 121 ? O SER B 123 
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                   8YKM 
_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 ASP A 33  ? ? 56.78  -131.42 
2  1 ASN A 84  ? ? 49.16  -118.72 
3  1 ASP A 155 ? ? 71.27  -17.84  
4  1 PRO A 184 ? ? -94.12 36.98   
5  1 ASP B 33  ? ? 48.79  -132.99 
6  1 ASN B 84  ? ? 55.23  -126.47 
7  1 TYR B 154 ? ? 32.03  75.11   
8  1 ASP B 155 ? ? 81.88  -6.86   
9  1 ALA B 191 ? ? -88.91 34.52   
10 1 ASN B 214 ? ? -80.42 -141.46 
# 
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_
_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   7C2Q 
_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                    8YKM 
_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]   0.014747 
_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]   0.009897 
_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]   0.009574 
_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   ? 10.44200  4.59400   -17.07300 1.000 43.00000 ? 3   PHE A N   1 
ATOM   2    C CA  . PHE A 1 1   ? 9.40000   5.01200   -18.01600 1.000 44.37000 ? 3   PHE A CA  1 
ATOM   3    C C   . PHE A 1 1   ? 8.16500   4.09600   -18.01700 1.000 47.49000 ? 3   PHE A C   1 
ATOM   4    O O   . PHE A 1 1   ? 8.25800   2.89400   -18.28900 1.000 48.75000 ? 3   PHE A O   1 
ATOM   5    C CB  . PHE A 1 1   ? 9.97000   5.08500   -19.42700 1.000 43.92000 ? 3   PHE A CB  1 
ATOM   6    C CG  . PHE A 1 1   ? 9.38900   6.18500   -20.25200 1.000 41.63000 ? 3   PHE A CG  1 
ATOM   7    C CD1 . PHE A 1 1   ? 9.65300   7.50700   -19.94000 1.000 42.51000 ? 3   PHE A CD1 1 
ATOM   8    C CD2 . PHE A 1 1   ? 8.57700   5.90200   -21.34000 1.000 40.89000 ? 3   PHE A CD2 1 
ATOM   9    C CE1 . PHE A 1 1   ? 9.12300   8.53400   -20.69900 1.000 40.86000 ? 3   PHE A CE1 1 
ATOM   10   C CE2 . PHE A 1 1   ? 8.04400   6.92200   -22.10300 1.000 40.69000 ? 3   PHE A CE2 1 
ATOM   11   C CZ  . PHE A 1 1   ? 8.31600   8.24500   -21.77800 1.000 38.87000 ? 3   PHE A CZ  1 
ATOM   12   N N   . ARG A 1 2   ? 7.00500   4.68400   -17.73700 1.000 36.82000 ? 4   ARG A N   1 
ATOM   13   C CA  . ARG A 1 2   ? 5.75000   3.95500   -17.65700 1.000 39.83000 ? 4   ARG A CA  1 
ATOM   14   C C   . ARG A 1 2   ? 4.72500   4.64100   -18.54300 1.000 37.67000 ? 4   ARG A C   1 
ATOM   15   O O   . ARG A 1 2   ? 4.73200   5.86400   -18.69400 1.000 38.96000 ? 4   ARG A O   1 
ATOM   16   C CB  . ARG A 1 2   ? 5.20600   3.89200   -16.20900 1.000 38.09000 ? 4   ARG A CB  1 
ATOM   17   C CG  . ARG A 1 2   ? 6.03900   3.04500   -15.24000 1.000 36.40000 ? 4   ARG A CG  1 
ATOM   18   C CD  . ARG A 1 2   ? 5.31300   1.74000   -14.89500 1.000 38.53000 ? 4   ARG A CD  1 
ATOM   19   N NE  . ARG A 1 2   ? 6.09500   0.87200   -14.01500 1.000 41.76000 ? 4   ARG A NE  1 
ATOM   20   C CZ  . ARG A 1 2   ? 6.04100   -0.45900  -14.03200 1.000 43.00000 ? 4   ARG A CZ  1 
ATOM   21   N NH1 . ARG A 1 2   ? 5.23900   -1.07900  -14.89000 1.000 37.86000 ? 4   ARG A NH1 1 
ATOM   22   N NH2 . ARG A 1 2   ? 6.78900   -1.17300  -13.19200 1.000 36.92000 ? 4   ARG A NH2 1 
ATOM   23   N N   . LYS A 1 3   ? 3.84600   3.84800   -19.13600 1.000 39.49000 ? 5   LYS A N   1 
ATOM   24   C CA  . LYS A 1 3   ? 2.63900   4.42500   -19.70400 1.000 39.42000 ? 5   LYS A CA  1 
ATOM   25   C C   . LYS A 1 3   ? 1.77100   4.89600   -18.54700 1.000 36.67000 ? 5   LYS A C   1 
ATOM   26   O O   . LYS A 1 3   ? 1.22100   4.08300   -17.80000 1.000 42.95000 ? 5   LYS A O   1 
ATOM   27   C CB  . LYS A 1 3   ? 1.91400   3.41900   -20.58700 1.000 42.54000 ? 5   LYS A CB  1 
ATOM   28   C CG  . LYS A 1 3   ? 1.63500   3.97800   -21.97200 1.000 43.09000 ? 5   LYS A CG  1 
ATOM   29   C CD  . LYS A 1 3   ? 1.09700   2.92300   -22.90100 1.000 44.25000 ? 5   LYS A CD  1 
ATOM   30   C CE  . LYS A 1 3   ? 2.19300   2.29600   -23.72000 1.000 39.44000 ? 5   LYS A CE  1 
ATOM   31   N NZ  . LYS A 1 3   ? 1.61600   1.25300   -24.60000 1.000 44.65000 ? 5   LYS A NZ  1 
ATOM   32   N N   . MET A 1 4   ? 1.69900   6.20800   -18.36500 1.000 34.82000 ? 6   MET A N   1 
ATOM   33   C CA  . MET A 1 4   ? 1.02400   6.82200   -17.23100 1.000 33.54000 ? 6   MET A CA  1 
ATOM   34   C C   . MET A 1 4   ? -0.32800  7.35300   -17.67000 1.000 30.23000 ? 6   MET A C   1 
ATOM   35   O O   . MET A 1 4   ? -0.41400  8.10100   -18.65000 1.000 29.49000 ? 6   MET A O   1 
ATOM   36   C CB  . MET A 1 4   ? 1.85500   7.97100   -16.67000 1.000 35.71000 ? 6   MET A CB  1 
ATOM   37   C CG  . MET A 1 4   ? 1.92400   8.03100   -15.16800 1.000 38.92000 ? 6   MET A CG  1 
ATOM   38   S SD  . MET A 1 4   ? 3.41600   8.91300   -14.69900 1.000 51.33000 ? 6   MET A SD  1 
ATOM   39   C CE  . MET A 1 4   ? 3.28300   10.35600  -15.75200 1.000 38.57000 ? 6   MET A CE  1 
ATOM   40   N N   . ALA A 1 5   ? -1.36800  6.97600   -16.94200 1.000 30.11000 ? 7   ALA A N   1 
ATOM   41   C CA  . ALA A 1 5   ? -2.69100  7.52900   -17.17200 1.000 26.86000 ? 7   ALA A CA  1 
ATOM   42   C C   . ALA A 1 5   ? -2.87000  8.79200   -16.33600 1.000 29.59000 ? 7   ALA A C   1 
ATOM   43   O O   . ALA A 1 5   ? -2.10300  9.07500   -15.41100 1.000 27.23000 ? 7   ALA A O   1 
ATOM   44   C CB  . ALA A 1 5   ? -3.76800  6.49700   -16.82700 1.000 25.25000 ? 7   ALA A CB  1 
ATOM   45   N N   . PHE A 1 6   ? -3.89900  9.56500   -16.67400 1.000 26.43000 ? 8   PHE A N   1 
ATOM   46   C CA  . PHE A 1 6   ? -4.24000  10.67800  -15.80700 1.000 28.81000 ? 8   PHE A CA  1 
ATOM   47   C C   . PHE A 1 6   ? -5.00800  10.18100  -14.58600 1.000 26.89000 ? 8   PHE A C   1 
ATOM   48   O O   . PHE A 1 6   ? -5.70800  9.16800   -14.65800 1.000 27.06000 ? 8   PHE A O   1 
ATOM   49   C CB  . PHE A 1 6   ? -5.07600  11.71200  -16.55900 1.000 25.05000 ? 8   PHE A CB  1 
ATOM   50   C CG  . PHE A 1 6   ? -4.26400  12.55100  -17.49400 1.000 26.00000 ? 8   PHE A CG  1 
ATOM   51   C CD1 . PHE A 1 6   ? -3.48000  13.57600  -17.00800 1.000 32.30000 ? 8   PHE A CD1 1 
ATOM   52   C CD2 . PHE A 1 6   ? -4.23800  12.27400  -18.85400 1.000 27.70000 ? 8   PHE A CD2 1 
ATOM   53   C CE1 . PHE A 1 6   ? -2.69500  14.34100  -17.86600 1.000 33.43000 ? 8   PHE A CE1 1 
ATOM   54   C CE2 . PHE A 1 6   ? -3.46400  13.02900  -19.71500 1.000 28.72000 ? 8   PHE A CE2 1 
ATOM   55   C CZ  . PHE A 1 6   ? -2.68900  14.06800  -19.21500 1.000 33.23000 ? 8   PHE A CZ  1 
ATOM   56   N N   . PRO A 1 7   ? -4.84800  10.85500  -13.44900 1.000 24.51000 ? 9   PRO A N   1 
ATOM   57   C CA  . PRO A 1 7   ? -5.67300  10.54600  -12.27400 1.000 25.05000 ? 9   PRO A CA  1 
ATOM   58   C C   . PRO A 1 7   ? -7.15000  10.59900  -12.66200 1.000 23.92000 ? 9   PRO A C   1 
ATOM   59   O O   . PRO A 1 7   ? -7.58600  11.51200  -13.35700 1.000 25.45000 ? 9   PRO A O   1 
ATOM   60   C CB  . PRO A 1 7   ? -5.29200  11.64700  -11.27700 1.000 24.42000 ? 9   PRO A CB  1 
ATOM   61   C CG  . PRO A 1 7   ? -3.91800  12.14200  -11.73400 1.000 29.90000 ? 9   PRO A CG  1 
ATOM   62   C CD  . PRO A 1 7   ? -3.89100  11.95700  -13.22500 1.000 27.53000 ? 9   PRO A CD  1 
ATOM   63   N N   . SER A 1 8   ? -7.90500  9.58100   -12.27000 1.000 23.26000 ? 10  SER A N   1 
ATOM   64   C CA  . SER A 1 8   ? -9.23100  9.36700   -12.84700 1.000 25.87000 ? 10  SER A CA  1 
ATOM   65   C C   . SER A 1 8   ? -10.36400 9.98600   -12.04000 1.000 26.13000 ? 10  SER A C   1 
ATOM   66   O O   . SER A 1 8   ? -11.51200 9.92800   -12.48900 1.000 27.04000 ? 10  SER A O   1 
ATOM   67   C CB  . SER A 1 8   ? -9.49300  7.86800   -13.02700 1.000 26.29000 ? 10  SER A CB  1 
ATOM   68   O OG  . SER A 1 8   ? -9.40900  7.20300   -11.77900 1.000 28.47000 ? 10  SER A OG  1 
ATOM   69   N N   . GLY A 1 9   ? -10.06200 10.61100  -10.89900 1.000 25.69000 ? 11  GLY A N   1 
ATOM   70   C CA  . GLY A 1 9   ? -11.10200 10.97100  -9.94400  1.000 27.00000 ? 11  GLY A CA  1 
ATOM   71   C C   . GLY A 1 9   ? -12.14300 11.91700  -10.51100 1.000 26.38000 ? 11  GLY A C   1 
ATOM   72   O O   . GLY A 1 9   ? -13.33800 11.76900  -10.24400 1.000 28.15000 ? 11  GLY A O   1 
ATOM   73   N N   . LYS A 1 10  ? -11.70500 12.90500  -11.29400 1.000 26.97000 ? 12  LYS A N   1 
ATOM   74   C CA  . LYS A 1 10  ? -12.64700 13.84600  -11.89100 1.000 29.92000 ? 12  LYS A CA  1 
ATOM   75   C C   . LYS A 1 10  ? -13.65400 13.14200  -12.79300 1.000 28.11000 ? 12  LYS A C   1 
ATOM   76   O O   . LYS A 1 10  ? -14.81000 13.57100  -12.88200 1.000 33.15000 ? 12  LYS A O   1 
ATOM   77   C CB  . LYS A 1 10  ? -11.89200 14.91700  -12.67600 1.000 28.57000 ? 12  LYS A CB  1 
ATOM   78   C CG  . LYS A 1 10  ? -11.20400 15.97100  -11.81400 1.000 32.51000 ? 12  LYS A CG  1 
ATOM   79   C CD  . LYS A 1 10  ? -10.35400 16.89900  -12.69300 1.000 32.17000 ? 12  LYS A CD  1 
ATOM   80   C CE  . LYS A 1 10  ? -9.64600  17.95500  -11.87100 1.000 39.84000 ? 12  LYS A CE  1 
ATOM   81   N NZ  . LYS A 1 10  ? -8.90500  17.33700  -10.73700 1.000 41.19000 ? 12  LYS A NZ  1 
ATOM   82   N N   . VAL A 1 11  ? -13.24800 12.06000  -13.45200 1.000 24.63000 ? 13  VAL A N   1 
ATOM   83   C CA  . VAL A 1 11  ? -14.14900 11.34600  -14.34900 1.000 27.72000 ? 13  VAL A CA  1 
ATOM   84   C C   . VAL A 1 11  ? -14.98200 10.32900  -13.57900 1.000 26.17000 ? 13  VAL A C   1 
ATOM   85   O O   . VAL A 1 11  ? -16.14800 10.10400  -13.92000 1.000 25.63000 ? 13  VAL A O   1 
ATOM   86   C CB  . VAL A 1 11  ? -13.35500 10.67200  -15.48800 1.000 23.65000 ? 13  VAL A CB  1 
ATOM   87   C CG1 . VAL A 1 11  ? -14.28000 9.89400   -16.43700 1.000 27.47000 ? 13  VAL A CG1 1 
ATOM   88   C CG2 . VAL A 1 11  ? -12.50700 11.70600  -16.25600 1.000 25.67000 ? 13  VAL A CG2 1 
ATOM   89   N N   . GLU A 1 12  ? -14.40300 9.71900   -12.53700 1.000 26.33000 ? 14  GLU A N   1 
ATOM   90   C CA  . GLU A 1 12  ? -15.13700 8.75800   -11.71800 1.000 23.51000 ? 14  GLU A CA  1 
ATOM   91   C C   . GLU A 1 12  ? -16.43000 9.35000   -11.20000 1.000 27.29000 ? 14  GLU A C   1 
ATOM   92   O O   . GLU A 1 12  ? -17.44600 8.66000   -11.13300 1.000 24.24000 ? 14  GLU A O   1 
ATOM   93   C CB  . GLU A 1 12  ? -14.30500 8.29700   -10.52200 1.000 27.89000 ? 14  GLU A CB  1 
ATOM   94   C CG  . GLU A 1 12  ? -13.12000 7.44200   -10.87600 1.000 26.43000 ? 14  GLU A CG  1 
ATOM   95   C CD  . GLU A 1 12  ? -12.18700 7.24700   -9.68700  1.000 29.34000 ? 14  GLU A CD  1 
ATOM   96   O OE1 . GLU A 1 12  ? -10.97900 7.41900   -9.88000  1.000 28.37000 ? 14  GLU A OE1 1 
ATOM   97   O OE2 . GLU A 1 12  ? -12.66200 6.89500   -8.58000  1.000 30.70000 ? 14  GLU A OE2 1 
ATOM   98   N N   . SER A 1 13  ? -16.39900 10.62800  -10.82500 1.000 25.12000 ? 15  SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? -17.55200 11.30800  -10.27100 1.000 29.80000 ? 15  SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? -18.64400 11.55100  -11.30100 1.000 28.85000 ? 15  SER A C   1 
ATOM   101  O O   . SER A 1 13  ? -19.72700 11.99600  -10.91900 1.000 28.91000 ? 15  SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? -17.11000 12.63800  -9.66300  1.000 30.95000 ? 15  SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? -16.19500 12.42000  -8.61100  1.000 33.77000 ? 15  SER A OG  1 
ATOM   104  N N   . CYS A 1 14  ? -18.37400 11.31000  -12.58500 1.000 27.48000 ? 16  CYS A N   1 
ATOM   105  C CA  . CYS A 1 14  ? -19.34700 11.53000  -13.64300 1.000 28.68000 ? 16  CYS A CA  1 
ATOM   106  C C   . CYS A 1 14  ? -19.96100 10.25000  -14.18800 1.000 28.86000 ? 16  CYS A C   1 
ATOM   107  O O   . CYS A 1 14  ? -20.87200 10.33500  -15.02600 1.000 26.89000 ? 16  CYS A O   1 
ATOM   108  C CB  . CYS A 1 14  ? -18.70400 12.30600  -14.79200 1.000 28.50000 ? 16  CYS A CB  1 
ATOM   109  S SG  . CYS A 1 14  ? -17.96300 13.86100  -14.30800 1.000 31.23000 ? 16  CYS A SG  1 
ATOM   110  N N   . MET A 1 15  ? -19.51200 9.07500   -13.74300 1.000 25.42000 ? 17  MET A N   1 
ATOM   111  C CA  . MET A 1 15  ? -19.98300 7.82500   -14.33500 1.000 28.34000 ? 17  MET A CA  1 
ATOM   112  C C   . MET A 1 15  ? -21.29100 7.39300   -13.69500 1.000 30.23000 ? 17  MET A C   1 
ATOM   113  O O   . MET A 1 15  ? -21.40700 7.33900   -12.46400 1.000 29.21000 ? 17  MET A O   1 
ATOM   114  C CB  . MET A 1 15  ? -18.94300 6.71000   -14.19300 1.000 27.06000 ? 17  MET A CB  1 
ATOM   115  C CG  . MET A 1 15  ? -17.63600 7.00300   -14.89500 1.000 24.18000 ? 17  MET A CG  1 
ATOM   116  S SD  . MET A 1 15  ? -17.80700 7.58500   -16.59400 1.000 27.93000 ? 17  MET A SD  1 
ATOM   117  C CE  . MET A 1 15  ? -18.64800 6.19900   -17.34000 1.000 25.30000 ? 17  MET A CE  1 
ATOM   118  N N   . VAL A 1 16  ? -22.27100 7.07500   -14.53900 1.000 28.58000 ? 18  VAL A N   1 
ATOM   119  C CA  . VAL A 1 16  ? -23.57300 6.59300   -14.10200 1.000 26.14000 ? 18  VAL A CA  1 
ATOM   120  C C   . VAL A 1 16  ? -23.92500 5.35000   -14.90900 1.000 28.79000 ? 18  VAL A C   1 
ATOM   121  O O   . VAL A 1 16  ? -23.24900 4.99000   -15.87700 1.000 25.26000 ? 18  VAL A O   1 
ATOM   122  C CB  . VAL A 1 16  ? -24.66600 7.67200   -14.24400 1.000 28.22000 ? 18  VAL A CB  1 
ATOM   123  C CG1 . VAL A 1 16  ? -24.32200 8.87400   -13.37600 1.000 28.25000 ? 18  VAL A CG1 1 
ATOM   124  C CG2 . VAL A 1 16  ? -24.82100 8.09800   -15.69700 1.000 25.52000 ? 18  VAL A CG2 1 
ATOM   125  N N   . GLN A 1 17  ? -24.99700 4.68900   -14.48300 1.000 28.79000 ? 19  GLN A N   1 
ATOM   126  C CA  . GLN A 1 17  ? -25.52900 3.51000   -15.14900 1.000 27.92000 ? 19  GLN A CA  1 
ATOM   127  C C   . GLN A 1 17  ? -26.81100 3.90800   -15.87000 1.000 28.63000 ? 19  GLN A C   1 
ATOM   128  O O   . GLN A 1 17  ? -27.63800 4.62900   -15.30400 1.000 28.94000 ? 19  GLN A O   1 
ATOM   129  C CB  . GLN A 1 17  ? -25.79600 2.40800   -14.12500 1.000 29.45000 ? 19  GLN A CB  1 
ATOM   130  C CG  . GLN A 1 17  ? -26.29700 1.11000   -14.69000 1.000 31.70000 ? 19  GLN A CG  1 
ATOM   131  C CD  . GLN A 1 17  ? -26.39100 0.02600   -13.62600 1.000 36.17000 ? 19  GLN A CD  1 
ATOM   132  O OE1 . GLN A 1 17  ? -26.47100 -1.16000  -13.93600 1.000 42.79000 ? 19  GLN A OE1 1 
ATOM   133  N NE2 . GLN A 1 17  ? -26.38300 0.43500   -12.36100 1.000 41.91000 ? 19  GLN A NE2 1 
ATOM   134  N N   . VAL A 1 18  ? -26.95900 3.47800   -17.12200 1.000 27.36000 ? 20  VAL A N   1 
ATOM   135  C CA  . VAL A 1 18  ? -28.16200 3.73300   -17.91200 1.000 29.36000 ? 20  VAL A CA  1 
ATOM   136  C C   . VAL A 1 18  ? -28.77200 2.39900   -18.29600 1.000 29.25000 ? 20  VAL A C   1 
ATOM   137  O O   . VAL A 1 18  ? -28.08700 1.53700   -18.85900 1.000 28.86000 ? 20  VAL A O   1 
ATOM   138  C CB  . VAL A 1 18  ? -27.87000 4.55800   -19.18100 1.000 28.19000 ? 20  VAL A CB  1 
ATOM   139  C CG1 . VAL A 1 18  ? -29.16700 4.81300   -19.95700 1.000 29.51000 ? 20  VAL A CG1 1 
ATOM   140  C CG2 . VAL A 1 18  ? -27.15700 5.86300   -18.84300 1.000 27.77000 ? 20  VAL A CG2 1 
ATOM   141  N N   . THR A 1 19  ? -30.06700 2.24100   -18.03400 1.000 30.92000 ? 21  THR A N   1 
ATOM   142  C CA  . THR A 1 19  ? -30.77800 1.03100   -18.40600 1.000 29.78000 ? 21  THR A CA  1 
ATOM   143  C C   . THR A 1 19  ? -31.96200 1.39400   -19.29100 1.000 33.18000 ? 21  THR A C   1 
ATOM   144  O O   . THR A 1 19  ? -32.71000 2.32800   -18.98600 1.000 31.55000 ? 21  THR A O   1 
ATOM   145  C CB  . THR A 1 19  ? -31.24500 0.25900   -17.17000 1.000 35.03000 ? 21  THR A CB  1 
ATOM   146  O OG1 . THR A 1 19  ? -30.10400 -0.10600  -16.38200 1.000 36.25000 ? 21  THR A OG1 1 
ATOM   147  C CG2 . THR A 1 19  ? -31.99400 -1.01100  -17.58600 1.000 33.11000 ? 21  THR A CG2 1 
ATOM   148  N N   . CYS A 1 20  ? -32.10400 0.66900   -20.39800 1.000 32.69000 ? 22  CYS A N   1 
ATOM   149  C CA  . CYS A 1 20  ? -33.28200 0.75700   -21.25300 1.000 33.96000 ? 22  CYS A CA  1 
ATOM   150  C C   . CYS A 1 20  ? -33.68800 -0.66500  -21.59700 1.000 35.26000 ? 22  CYS A C   1 
ATOM   151  O O   . CYS A 1 20  ? -32.90200 -1.40700  -22.19500 1.000 35.91000 ? 22  CYS A O   1 
ATOM   152  C CB  . CYS A 1 20  ? -32.99200 1.58300   -22.51000 1.000 31.73000 ? 22  CYS A CB  1 
ATOM   153  S SG  . CYS A 1 20  ? -34.41400 1.96800   -23.55400 1.000 41.77000 ? 22  CYS A SG  1 
ATOM   154  N N   . GLY A 1 21  ? -34.89400 -1.05800  -21.18900 1.000 36.63000 ? 23  GLY A N   1 
ATOM   155  C CA  . GLY A 1 21  ? -35.31500 -2.43200  -21.42600 1.000 37.67000 ? 23  GLY A CA  1 
ATOM   156  C C   . GLY A 1 21  ? -34.42600 -3.39800  -20.66800 1.000 36.01000 ? 23  GLY A C   1 
ATOM   157  O O   . GLY A 1 21  ? -34.22000 -3.26800  -19.45800 1.000 40.22000 ? 23  GLY A O   1 
ATOM   158  N N   . THR A 1 22  ? -33.85700 -4.36300  -21.38700 1.000 35.56000 ? 24  THR A N   1 
ATOM   159  C CA  . THR A 1 22  ? -32.96900 -5.35600  -20.79300 1.000 39.63000 ? 24  THR A CA  1 
ATOM   160  C C   . THR A 1 22  ? -31.49700 -4.98000  -20.90700 1.000 35.30000 ? 24  THR A C   1 
ATOM   161  O O   . THR A 1 22  ? -30.63300 -5.76500  -20.48900 1.000 40.28000 ? 24  THR A O   1 
ATOM   162  C CB  . THR A 1 22  ? -33.19400 -6.71800  -21.44900 1.000 38.35000 ? 24  THR A CB  1 
ATOM   163  O OG1 . THR A 1 22  ? -33.08900 -6.58100  -22.87100 1.000 44.40000 ? 24  THR A OG1 1 
ATOM   164  C CG2 . THR A 1 22  ? -34.58400 -7.25100  -21.10500 1.000 39.92000 ? 24  THR A CG2 1 
ATOM   165  N N   . THR A 1 23  ? -31.18500 -3.81000  -21.45400 1.000 36.27000 ? 25  THR A N   1 
ATOM   166  C CA  . THR A 1 23  ? -29.80200 -3.41600  -21.71100 1.000 32.99000 ? 25  THR A CA  1 
ATOM   167  C C   . THR A 1 23  ? -29.33600 -2.40000  -20.68100 1.000 32.96000 ? 25  THR A C   1 
ATOM   168  O O   . THR A 1 23  ? -30.01500 -1.40000  -20.43600 1.000 29.04000 ? 25  THR A O   1 
ATOM   169  C CB  . THR A 1 23  ? -29.65100 -2.83100  -23.11400 1.000 32.01000 ? 25  THR A CB  1 
ATOM   170  O OG1 . THR A 1 23  ? -30.18300 -3.75200  -24.06900 1.000 38.29000 ? 25  THR A OG1 1 
ATOM   171  C CG2 . THR A 1 23  ? -28.17500 -2.55500  -23.44100 1.000 33.91000 ? 25  THR A CG2 1 
ATOM   172  N N   . THR A 1 24  ? -28.16200 -2.64600  -20.10500 1.000 30.04000 ? 26  THR A N   1 
ATOM   173  C CA  . THR A 1 24  ? -27.50400 -1.70800  -19.21100 1.000 30.32000 ? 26  THR A CA  1 
ATOM   174  C C   . THR A 1 24  ? -26.13000 -1.37500  -19.77800 1.000 30.50000 ? 26  THR A C   1 
ATOM   175  O O   . THR A 1 24  ? -25.45800 -2.24400  -20.33500 1.000 29.27000 ? 26  THR A O   1 
ATOM   176  C CB  . THR A 1 24  ? -27.36600 -2.29500  -17.79900 1.000 31.88000 ? 26  THR A CB  1 
ATOM   177  O OG1 . THR A 1 24  ? -28.64700 -2.31200  -17.16000 1.000 35.39000 ? 26  THR A OG1 1 
ATOM   178  C CG2 . THR A 1 24  ? -26.44700 -1.46700  -16.97400 1.000 35.88000 ? 26  THR A CG2 1 
ATOM   179  N N   . LEU A 1 25  ? -25.73000 -0.11300  -19.66500 1.000 29.60000 ? 27  LEU A N   1 
ATOM   180  C CA  . LEU A 1 25  ? -24.37800 0.31100   -20.00900 1.000 27.18000 ? 27  LEU A CA  1 
ATOM   181  C C   . LEU A 1 25  ? -24.07700 1.57100   -19.20000 1.000 26.82000 ? 27  LEU A C   1 
ATOM   182  O O   . LEU A 1 25  ? -24.83300 1.94400   -18.29300 1.000 26.90000 ? 27  LEU A O   1 
ATOM   183  C CB  . LEU A 1 25  ? -24.22000 0.50700   -21.52500 1.000 25.05000 ? 27  LEU A CB  1 
ATOM   184  C CG  . LEU A 1 25  ? -25.30900 1.19900   -22.35200 1.000 25.84000 ? 27  LEU A CG  1 
ATOM   185  C CD1 . LEU A 1 25  ? -25.52700 2.63300   -21.89500 1.000 24.12000 ? 27  LEU A CD1 1 
ATOM   186  C CD2 . LEU A 1 25  ? -24.94800 1.16900   -23.84600 1.000 24.64000 ? 27  LEU A CD2 1 
ATOM   187  N N   . ASN A 1 26  ? -22.98100 2.23600   -19.53400 1.000 22.34000 ? 28  ASN A N   1 
ATOM   188  C CA  . ASN A 1 26  ? -22.51400 3.39100   -18.78500 1.000 21.46000 ? 28  ASN A CA  1 
ATOM   189  C C   . ASN A 1 26  ? -22.90600 4.69000   -19.47100 1.000 23.48000 ? 28  ASN A C   1 
ATOM   190  O O   . ASN A 1 26  ? -23.02900 4.76300   -20.69800 1.000 24.64000 ? 28  ASN A O   1 
ATOM   191  C CB  . ASN A 1 26  ? -20.97700 3.35800   -18.61700 1.000 20.92000 ? 28  ASN A CB  1 
ATOM   192  C CG  . ASN A 1 26  ? -20.49400 2.06300   -18.00200 1.000 25.22000 ? 28  ASN A CG  1 
ATOM   193  O OD1 . ASN A 1 26  ? -20.55200 1.88500   -16.79600 1.000 26.92000 ? 28  ASN A OD1 1 
ATOM   194  N ND2 . ASN A 1 26  ? -20.05000 1.13200   -18.84200 1.000 25.17000 ? 28  ASN A ND2 1 
ATOM   195  N N   . GLY A 1 27  ? -23.10200 5.72500   -18.65200 1.000 26.12000 ? 29  GLY A N   1 
ATOM   196  C CA  . GLY A 1 27  ? -23.30200 7.06300   -19.15500 1.000 25.42000 ? 29  GLY A CA  1 
ATOM   197  C C   . GLY A 1 27  ? -22.37400 8.03800   -18.45900 1.000 26.25000 ? 29  GLY A C   1 
ATOM   198  O O   . GLY A 1 27  ? -21.75900 7.73400   -17.43500 1.000 24.65000 ? 29  GLY A O   1 
ATOM   199  N N   . LEU A 1 28  ? -22.26600 9.22400   -19.05200 1.000 24.50000 ? 30  LEU A N   1 
ATOM   200  C CA  . LEU A 1 28  ? -21.37700 10.27300  -18.57000 1.000 27.49000 ? 30  LEU A CA  1 
ATOM   201  C C   . LEU A 1 28  ? -22.23800 11.45400  -18.16500 1.000 25.92000 ? 30  LEU A C   1 
ATOM   202  O O   . LEU A 1 28  ? -22.86900 12.07800  -19.02200 1.000 27.52000 ? 30  LEU A O   1 
ATOM   203  C CB  . LEU A 1 28  ? -20.36500 10.68800  -19.64400 1.000 24.70000 ? 30  LEU A CB  1 
ATOM   204  C CG  . LEU A 1 28  ? -19.36700 11.77000  -19.22200 1.000 26.02000 ? 30  LEU A CG  1 
ATOM   205  C CD1 . LEU A 1 28  ? -18.33400 11.23600  -18.20700 1.000 25.00000 ? 30  LEU A CD1 1 
ATOM   206  C CD2 . LEU A 1 28  ? -18.66200 12.37800  -20.43300 1.000 23.93000 ? 30  LEU A CD2 1 
ATOM   207  N N   . TRP A 1 29  ? -22.23300 11.77300  -16.87600 1.000 27.60000 ? 31  TRP A N   1 
ATOM   208  C CA  . TRP A 1 29  ? -23.14000 12.75300  -16.27100 1.000 28.92000 ? 31  TRP A CA  1 
ATOM   209  C C   . TRP A 1 29  ? -22.38500 14.06300  -16.06200 1.000 28.91000 ? 31  TRP A C   1 
ATOM   210  O O   . TRP A 1 29  ? -21.57800 14.19300  -15.13700 1.000 29.20000 ? 31  TRP A O   1 
ATOM   211  C CB  . TRP A 1 29  ? -23.67200 12.20200  -14.95500 1.000 27.26000 ? 31  TRP A CB  1 
ATOM   212  C CG  . TRP A 1 29  ? -24.62900 13.04600  -14.18500 1.000 27.62000 ? 31  TRP A CG  1 
ATOM   213  C CD1 . TRP A 1 29  ? -25.50000 13.99300  -14.67500 1.000 29.71000 ? 31  TRP A CD1 1 
ATOM   214  C CD2 . TRP A 1 29  ? -24.85100 12.98500  -12.77500 1.000 28.81000 ? 31  TRP A CD2 1 
ATOM   215  N NE1 . TRP A 1 29  ? -26.23600 14.52700  -13.63900 1.000 32.46000 ? 31  TRP A NE1 1 
ATOM   216  C CE2 . TRP A 1 29  ? -25.86300 13.92100  -12.46700 1.000 33.29000 ? 31  TRP A CE2 1 
ATOM   217  C CE3 . TRP A 1 29  ? -24.28800 12.23200  -11.73800 1.000 31.38000 ? 31  TRP A CE3 1 
ATOM   218  C CZ2 . TRP A 1 29  ? -26.32100 14.12400  -11.16400 1.000 33.18000 ? 31  TRP A CZ2 1 
ATOM   219  C CZ3 . TRP A 1 29  ? -24.75300 12.42800  -10.44500 1.000 31.51000 ? 31  TRP A CZ3 1 
ATOM   220  C CH2 . TRP A 1 29  ? -25.75500 13.37500  -10.17100 1.000 32.14000 ? 31  TRP A CH2 1 
ATOM   221  N N   . LEU A 1 30  ? -22.66600 15.04000  -16.91000 1.000 27.96000 ? 32  LEU A N   1 
ATOM   222  C CA  . LEU A 1 30  ? -22.05300 16.35500  -16.84300 1.000 28.10000 ? 32  LEU A CA  1 
ATOM   223  C C   . LEU A 1 30  ? -23.17600 17.37800  -16.77300 1.000 32.08000 ? 32  LEU A C   1 
ATOM   224  O O   . LEU A 1 30  ? -24.04100 17.40500  -17.65500 1.000 29.71000 ? 32  LEU A O   1 
ATOM   225  C CB  . LEU A 1 30  ? -21.17600 16.61200  -18.06600 1.000 29.69000 ? 32  LEU A CB  1 
ATOM   226  C CG  . LEU A 1 30  ? -20.05900 15.60900  -18.30800 1.000 27.95000 ? 32  LEU A CG  1 
ATOM   227  C CD1 . LEU A 1 30  ? -19.49700 15.81000  -19.72100 1.000 29.80000 ? 32  LEU A CD1 1 
ATOM   228  C CD2 . LEU A 1 30  ? -18.96600 15.79400  -17.27100 1.000 27.10000 ? 32  LEU A CD2 1 
ATOM   229  N N   . ASP A 1 31  ? -23.16400 18.21300  -15.73500 1.000 32.41000 ? 33  ASP A N   1 
ATOM   230  C CA  . ASP A 1 31  ? -24.24600 19.19400  -15.52500 1.000 33.15000 ? 33  ASP A CA  1 
ATOM   231  C C   . ASP A 1 31  ? -25.55000 18.40100  -15.45700 1.000 30.98000 ? 33  ASP A C   1 
ATOM   232  O O   . ASP A 1 31  ? -25.61400 17.38200  -14.74900 1.000 29.89000 ? 33  ASP A O   1 
ATOM   233  C CB  . ASP A 1 31  ? -24.16800 20.27300  -16.60900 1.000 30.29000 ? 33  ASP A CB  1 
ATOM   234  C CG  . ASP A 1 31  ? -22.91400 21.13400  -16.48600 1.000 37.28000 ? 33  ASP A CG  1 
ATOM   235  O OD1 . ASP A 1 31  ? -22.58800 21.55200  -15.36200 1.000 38.14000 ? 33  ASP A OD1 1 
ATOM   236  O OD2 . ASP A 1 31  ? -22.26000 21.40500  -17.51000 1.000 37.57000 ? 33  ASP A OD2 1 
ATOM   237  N N   . ASP A 1 32  ? -26.60100 18.78600  -16.18200 1.000 32.50000 ? 34  ASP A N   1 
ATOM   238  C CA  . ASP A 1 32  ? -27.86600 18.06700  -16.11800 1.000 31.69000 ? 34  ASP A CA  1 
ATOM   239  C C   . ASP A 1 32  ? -28.09200 17.15500  -17.32500 1.000 34.06000 ? 34  ASP A C   1 
ATOM   240  O O   . ASP A 1 32  ? -29.24200 16.87400  -17.67600 1.000 29.99000 ? 34  ASP A O   1 
ATOM   241  C CB  . ASP A 1 32  ? -29.02800 19.05700  -15.96400 1.000 37.50000 ? 34  ASP A CB  1 
ATOM   242  C CG  . ASP A 1 32  ? -29.15300 20.01800  -17.15200 1.000 37.41000 ? 34  ASP A CG  1 
ATOM   243  O OD1 . ASP A 1 32  ? -28.15500 20.24600  -17.85800 1.000 37.87000 ? 34  ASP A OD1 1 
ATOM   244  O OD2 . ASP A 1 32  ? -30.25400 20.56800  -17.36500 1.000 41.43000 ? 34  ASP A OD2 1 
ATOM   245  N N   . VAL A 1 33  ? -27.02200 16.68300  -17.97200 1.000 31.09000 ? 35  VAL A N   1 
ATOM   246  C CA  . VAL A 1 33  ? -27.14100 15.81000  -19.13600 1.000 28.09000 ? 35  VAL A CA  1 
ATOM   247  C C   . VAL A 1 33  ? -26.36100 14.52400  -18.88900 1.000 29.20000 ? 35  VAL A C   1 
ATOM   248  O O   . VAL A 1 33  ? -25.23400 14.56200  -18.38700 1.000 28.87000 ? 35  VAL A O   1 
ATOM   249  C CB  . VAL A 1 33  ? -26.64500 16.50100  -20.42200 1.000 31.20000 ? 35  VAL A CB  1 
ATOM   250  C CG1 . VAL A 1 33  ? -26.86700 15.58800  -21.62100 1.000 28.27000 ? 35  VAL A CG1 1 
ATOM   251  C CG2 . VAL A 1 33  ? -27.37900 17.84700  -20.62900 1.000 35.83000 ? 35  VAL A CG2 1 
ATOM   252  N N   . VAL A 1 34  ? -26.96000 13.38500  -19.24200 1.000 28.98000 ? 36  VAL A N   1 
ATOM   253  C CA  . VAL A 1 34  ? -26.25900 12.10100  -19.26800 1.000 25.40000 ? 36  VAL A CA  1 
ATOM   254  C C   . VAL A 1 34  ? -26.03200 11.72600  -20.73000 1.000 28.40000 ? 36  VAL A C   1 
ATOM   255  O O   . VAL A 1 34  ? -26.98600 11.63700  -21.51400 1.000 26.71000 ? 36  VAL A O   1 
ATOM   256  C CB  . VAL A 1 34  ? -27.02700 11.00600  -18.51200 1.000 28.48000 ? 36  VAL A CB  1 
ATOM   257  C CG1 . VAL A 1 34  ? -26.34300 9.65800   -18.67700 1.000 27.30000 ? 36  VAL A CG1 1 
ATOM   258  C CG2 . VAL A 1 34  ? -27.15000 11.35500  -17.01100 1.000 28.53000 ? 36  VAL A CG2 1 
ATOM   259  N N   . TYR A 1 35  ? -24.76300 11.55800  -21.11200 1.000 24.81000 ? 37  TYR A N   1 
ATOM   260  C CA  . TYR A 1 35  ? -24.38100 11.13400  -22.45800 1.000 25.08000 ? 37  TYR A CA  1 
ATOM   261  C C   . TYR A 1 35  ? -24.14500 9.62800   -22.45800 1.000 28.95000 ? 37  TYR A C   1 
ATOM   262  O O   . TYR A 1 35  ? -23.46200 9.10900   -21.56800 1.000 27.65000 ? 37  TYR A O   1 
ATOM   263  C CB  . TYR A 1 35  ? -23.11500 11.85500  -22.93300 1.000 24.20000 ? 37  TYR A CB  1 
ATOM   264  C CG  . TYR A 1 35  ? -23.20000 13.36800  -22.86900 1.000 27.04000 ? 37  TYR A CG  1 
ATOM   265  C CD1 . TYR A 1 35  ? -23.08400 14.05000  -21.65100 1.000 26.41000 ? 37  TYR A CD1 1 
ATOM   266  C CD2 . TYR A 1 35  ? -23.40200 14.11500  -24.02300 1.000 28.67000 ? 37  TYR A CD2 1 
ATOM   267  C CE1 . TYR A 1 35  ? -23.17800 15.44000  -21.59300 1.000 27.74000 ? 37  TYR A CE1 1 
ATOM   268  C CE2 . TYR A 1 35  ? -23.49200 15.50400  -23.97500 1.000 28.18000 ? 37  TYR A CE2 1 
ATOM   269  C CZ  . TYR A 1 35  ? -23.38800 16.15200  -22.76100 1.000 26.00000 ? 37  TYR A CZ  1 
ATOM   270  O OH  . TYR A 1 35  ? -23.49400 17.52400  -22.71600 1.000 31.56000 ? 37  TYR A OH  1 
ATOM   271  N N   . CYS A 1 36  ? -24.70100 8.92300   -23.44000 1.000 24.95000 ? 38  CYS A N   1 
ATOM   272  C CA  . CYS A 1 36  ? -24.42300 7.49500   -23.53300 1.000 27.89000 ? 38  CYS A CA  1 
ATOM   273  C C   . CYS A 1 36  ? -24.59700 7.04100   -24.96900 1.000 27.88000 ? 38  CYS A C   1 
ATOM   274  O O   . CYS A 1 36  ? -25.12500 7.79200   -25.80600 1.000 26.24000 ? 38  CYS A O   1 
ATOM   275  C CB  . CYS A 1 36  ? -25.31400 6.69600   -22.57900 1.000 26.62000 ? 38  CYS A CB  1 
ATOM   276  S SG  . CYS A 1 36  ? -27.04500 6.56900   -23.13500 1.000 30.90000 ? 38  CYS A SG  1 
ATOM   277  N N   . PRO A 1 37  ? -24.11200 5.84100   -25.32100 1.000 26.48000 ? 39  PRO A N   1 
ATOM   278  C CA  . PRO A 1 37  ? -24.32000 5.33800   -26.68500 1.000 27.18000 ? 39  PRO A CA  1 
ATOM   279  C C   . PRO A 1 37  ? -25.79900 5.13800   -26.97500 1.000 26.75000 ? 39  PRO A C   1 
ATOM   280  O O   . PRO A 1 37  ? -26.53600 4.59300   -26.15200 1.000 25.55000 ? 39  PRO A O   1 
ATOM   281  C CB  . PRO A 1 37  ? -23.56800 4.00200   -26.70000 1.000 25.12000 ? 39  PRO A CB  1 
ATOM   282  C CG  . PRO A 1 37  ? -22.54700 4.12000   -25.60800 1.000 24.11000 ? 39  PRO A CG  1 
ATOM   283  C CD  . PRO A 1 37  ? -23.21900 4.95500   -24.53600 1.000 25.36000 ? 39  PRO A CD  1 
ATOM   284  N N   . ARG A 1 38  ? -26.22300 5.56700   -28.16400 1.000 25.28000 ? 40  ARG A N   1 
ATOM   285  C CA  . ARG A 1 38  ? -27.63600 5.42800   -28.51500 1.000 27.11000 ? 40  ARG A CA  1 
ATOM   286  C C   . ARG A 1 38  ? -28.04100 3.97600   -28.71100 1.000 28.92000 ? 40  ARG A C   1 
ATOM   287  O O   . ARG A 1 38  ? -29.24000 3.67700   -28.67200 1.000 25.86000 ? 40  ARG A O   1 
ATOM   288  C CB  . ARG A 1 38  ? -27.97300 6.23700   -29.76700 1.000 25.62000 ? 40  ARG A CB  1 
ATOM   289  C CG  . ARG A 1 38  ? -27.39500 5.68200   -31.07200 1.000 28.78000 ? 40  ARG A CG  1 
ATOM   290  C CD  . ARG A 1 38  ? -27.85200 6.47400   -32.30900 1.000 25.12000 ? 40  ARG A CD  1 
ATOM   291  N NE  . ARG A 1 38  ? -27.21400 5.94000   -33.51500 1.000 27.32000 ? 40  ARG A NE  1 
ATOM   292  C CZ  . ARG A 1 38  ? -27.50700 6.30300   -34.76100 1.000 29.08000 ? 40  ARG A CZ  1 
ATOM   293  N NH1 . ARG A 1 38  ? -28.46400 7.19500   -35.00400 1.000 28.02000 ? 40  ARG A NH1 1 
ATOM   294  N NH2 . ARG A 1 38  ? -26.86200 5.74300   -35.76800 1.000 28.17000 ? 40  ARG A NH2 1 
ATOM   295  N N   . HIS A 1 39  ? -27.07800 3.05500   -28.87400 1.000 25.95000 ? 41  HIS A N   1 
ATOM   296  C CA  . HIS A 1 39  ? -27.48400 1.66600   -29.04400 1.000 27.50000 ? 41  HIS A CA  1 
ATOM   297  C C   . HIS A 1 39  ? -28.02600 1.04300   -27.76000 1.000 25.74000 ? 41  HIS A C   1 
ATOM   298  O O   . HIS A 1 39  ? -28.49800 -0.09900  -27.81000 1.000 28.14000 ? 41  HIS A O   1 
ATOM   299  C CB  . HIS A 1 39  ? -26.34100 0.82700   -29.66400 1.000 26.78000 ? 41  HIS A CB  1 
ATOM   300  C CG  . HIS A 1 39  ? -25.13500 0.60700   -28.78800 1.000 27.25000 ? 41  HIS A CG  1 
ATOM   301  N ND1 . HIS A 1 39  ? -25.16600 -0.15100  -27.63700 1.000 28.67000 ? 41  HIS A ND1 1 
ATOM   302  C CD2 . HIS A 1 39  ? -23.83800 0.95500   -28.96900 1.000 26.22000 ? 41  HIS A CD2 1 
ATOM   303  C CE1 . HIS A 1 39  ? -23.95100 -0.22200  -27.12300 1.000 27.34000 ? 41  HIS A CE1 1 
ATOM   304  N NE2 . HIS A 1 39  ? -23.12700 0.44400   -27.91000 1.000 27.93000 ? 41  HIS A NE2 1 
ATOM   305  N N   . VAL A 1 40  ? -28.05500 1.78300   -26.64400 1.000 27.64000 ? 42  VAL A N   1 
ATOM   306  C CA  . VAL A 1 40  ? -28.79200 1.32800   -25.46300 1.000 27.33000 ? 42  VAL A CA  1 
ATOM   307  C C   . VAL A 1 40  ? -30.26400 1.06300   -25.78800 1.000 29.12000 ? 42  VAL A C   1 
ATOM   308  O O   . VAL A 1 40  ? -30.90000 0.21600   -25.14400 1.000 29.47000 ? 42  VAL A O   1 
ATOM   309  C CB  . VAL A 1 40  ? -28.64400 2.34400   -24.30500 1.000 25.24000 ? 42  VAL A CB  1 
ATOM   310  C CG1 . VAL A 1 40  ? -29.48900 3.58600   -24.54500 1.000 29.00000 ? 42  VAL A CG1 1 
ATOM   311  C CG2 . VAL A 1 40  ? -29.01500 1.69900   -22.96900 1.000 27.76000 ? 42  VAL A CG2 1 
ATOM   312  N N   . ILE A 1 41  ? -30.83100 1.76200   -26.78400 1.000 28.65000 ? 43  ILE A N   1 
ATOM   313  C CA  . ILE A 1 41  ? -32.24400 1.57400   -27.13200 1.000 30.70000 ? 43  ILE A CA  1 
ATOM   314  C C   . ILE A 1 41  ? -32.44200 0.50600   -28.20100 1.000 34.30000 ? 43  ILE A C   1 
ATOM   315  O O   . ILE A 1 41  ? -33.58300 0.24800   -28.61500 1.000 29.63000 ? 43  ILE A O   1 
ATOM   316  C CB  . ILE A 1 41  ? -32.90900 2.89400   -27.58900 1.000 31.90000 ? 43  ILE A CB  1 
ATOM   317  C CG1 . ILE A 1 41  ? -32.46900 3.29800   -28.99700 1.000 28.63000 ? 43  ILE A CG1 1 
ATOM   318  C CG2 . ILE A 1 41  ? -32.64800 4.01100   -26.60500 1.000 27.31000 ? 43  ILE A CG2 1 
ATOM   319  C CD1 . ILE A 1 41  ? -33.21100 4.50700   -29.51500 1.000 31.34000 ? 43  ILE A CD1 1 
ATOM   320  N N   . CYS A 1 42  ? -31.36300 -0.13100  -28.65300 1.000 28.00000 ? 44  CYS A N   1 
ATOM   321  C CA  . CYS A 1 42  ? -31.45200 -1.24300  -29.58800 1.000 29.30000 ? 44  CYS A CA  1 
ATOM   322  C C   . CYS A 1 42  ? -31.96900 -2.48800  -28.86500 1.000 38.87000 ? 44  CYS A C   1 
ATOM   323  O O   . CYS A 1 42  ? -31.54500 -2.78900  -27.74500 1.000 36.91000 ? 44  CYS A O   1 
ATOM   324  C CB  . CYS A 1 42  ? -30.06800 -1.50000  -30.19600 1.000 34.02000 ? 44  CYS A CB  1 
ATOM   325  S SG  . CYS A 1 42  ? -30.04800 -2.39500  -31.74200 1.000 40.81000 ? 44  CYS A SG  1 
ATOM   326  N N   . THR A 1 43  ? -32.88900 -3.21500  -29.49800 1.000 37.86000 ? 45  THR A N   1 
ATOM   327  C CA  . THR A 1 43  ? -33.36500 -4.45700  -28.90300 1.000 42.09000 ? 45  THR A CA  1 
ATOM   328  C C   . THR A 1 43  ? -32.60800 -5.66500  -29.45600 1.000 41.46000 ? 45  THR A C   1 
ATOM   329  O O   . THR A 1 43  ? -31.93600 -5.59500  -30.48400 1.000 40.64000 ? 45  THR A O   1 
ATOM   330  C CB  . THR A 1 43  ? -34.86300 -4.63700  -29.14300 1.000 40.26000 ? 45  THR A CB  1 
ATOM   331  O OG1 . THR A 1 43  ? -35.06500 -4.98400  -30.51400 1.000 38.21000 ? 45  THR A OG1 1 
ATOM   332  C CG2 . THR A 1 43  ? -35.62100 -3.36100  -28.80300 1.000 43.04000 ? 45  THR A CG2 1 
ATOM   333  N N   . SER A 1 44  ? -32.79300 -6.80100  -28.77500 1.000 46.02000 ? 46  SER A N   1 
ATOM   334  C CA  . SER A 1 44  ? -32.06000 -8.03000  -29.07000 1.000 45.13000 ? 46  SER A CA  1 
ATOM   335  C C   . SER A 1 44  ? -32.21800 -8.49400  -30.51900 1.000 50.19000 ? 46  SER A C   1 
ATOM   336  O O   . SER A 1 44  ? -31.34000 -9.19000  -31.03900 1.000 52.09000 ? 46  SER A O   1 
ATOM   337  C CB  . SER A 1 44  ? -32.51100 -9.12800  -28.10700 1.000 51.77000 ? 46  SER A CB  1 
ATOM   338  O OG  . SER A 1 44  ? -31.46200 -10.03500 -27.83500 1.000 60.50000 ? 46  SER A OG  1 
ATOM   339  N N   . GLU A 1 45  ? -33.31600 -8.14600  -31.19300 1.000 53.53000 ? 47  GLU A N   1 
ATOM   340  C CA  . GLU A 1 45  ? -33.43600 -8.45200  -32.61600 1.000 50.31000 ? 47  GLU A CA  1 
ATOM   341  C C   . GLU A 1 45  ? -33.36900 -7.20900  -33.49300 1.000 47.93000 ? 47  GLU A C   1 
ATOM   342  O O   . GLU A 1 45  ? -33.44800 -7.32400  -34.72200 1.000 53.76000 ? 47  GLU A O   1 
ATOM   343  C CB  . GLU A 1 45  ? -34.72700 -9.22400  -32.91300 1.000 56.48000 ? 47  GLU A CB  1 
ATOM   344  C CG  . GLU A 1 45  ? -35.98100 -8.75600  -32.17700 1.000 56.01000 ? 47  GLU A CG  1 
ATOM   345  C CD  . GLU A 1 45  ? -36.05700 -9.27900  -30.75600 1.000 57.74000 ? 47  GLU A CD  1 
ATOM   346  O OE1 . GLU A 1 45  ? -37.18000 -9.47800  -30.25200 1.000 65.07000 ? 47  GLU A OE1 1 
ATOM   347  O OE2 . GLU A 1 45  ? -34.99800 -9.48300  -30.13000 1.000 61.30000 ? 47  GLU A OE2 1 
ATOM   348  N N   . ASP A 1 46  ? -33.22800 -6.02100  -32.90000 1.000 50.53000 ? 48  ASP A N   1 
ATOM   349  C CA  . ASP A 1 46  ? -32.97900 -4.82000  -33.69000 1.000 49.02000 ? 48  ASP A CA  1 
ATOM   350  C C   . ASP A 1 46  ? -31.56600 -4.77200  -34.23500 1.000 39.61000 ? 48  ASP A C   1 
ATOM   351  O O   . ASP A 1 46  ? -31.29900 -3.94400  -35.11000 1.000 46.58000 ? 48  ASP A O   1 
ATOM   352  C CB  . ASP A 1 46  ? -33.21500 -3.54500  -32.86100 1.000 42.65000 ? 48  ASP A CB  1 
ATOM   353  C CG  . ASP A 1 46  ? -34.65000 -3.07100  -32.89200 1.000 51.60000 ? 48  ASP A CG  1 
ATOM   354  O OD1 . ASP A 1 46  ? -35.19000 -2.78400  -33.99500 1.000 52.14000 ? 48  ASP A OD1 1 
ATOM   355  O OD2 . ASP A 1 46  ? -35.24900 -2.96600  -31.79800 1.000 53.84000 ? 48  ASP A OD2 1 
ATOM   356  N N   . MET A 1 47  ? -30.67400 -5.66500  -33.78800 1.000 44.87000 ? 49  MET A N   1 
ATOM   357  C CA  . MET A 1 47  ? -29.24700 -5.35000  -33.78600 1.000 38.51000 ? 49  MET A CA  1 
ATOM   358  C C   . MET A 1 47  ? -28.64800 -5.21900  -35.18300 1.000 38.10000 ? 49  MET A C   1 
ATOM   359  O O   . MET A 1 47  ? -27.63600 -4.52700  -35.33700 1.000 33.51000 ? 49  MET A O   1 
ATOM   360  C CB  . MET A 1 47  ? -28.47700 -6.39600  -32.96800 1.000 39.01000 ? 49  MET A CB  1 
ATOM   361  C CG  . MET A 1 47  ? -28.83100 -6.38200  -31.47200 1.000 38.23000 ? 49  MET A CG  1 
ATOM   362  S SD  . MET A 1 47  ? -27.64100 -7.19100  -30.37000 1.000 41.53000 ? 49  MET A SD  1 
ATOM   363  C CE  . MET A 1 47  ? -27.89400 -8.92000  -30.78300 1.000 41.92000 ? 49  MET A CE  1 
ATOM   364  N N   . LEU A 1 48  ? -29.25900 -5.81700  -36.21000 1.000 37.13000 ? 50  LEU A N   1 
ATOM   365  C CA  . LEU A 1 48  ? -28.63500 -5.76300  -37.52900 1.000 33.55000 ? 50  LEU A CA  1 
ATOM   366  C C   . LEU A 1 48  ? -28.97300 -4.49100  -38.29400 1.000 33.14000 ? 50  LEU A C   1 
ATOM   367  O O   . LEU A 1 48  ? -28.08800 -3.89900  -38.91100 1.000 31.63000 ? 50  LEU A O   1 
ATOM   368  C CB  . LEU A 1 48  ? -29.02600 -6.98900  -38.35200 1.000 33.88000 ? 50  LEU A CB  1 
ATOM   369  C CG  . LEU A 1 48  ? -28.38900 -8.28100  -37.83900 1.000 36.19000 ? 50  LEU A CG  1 
ATOM   370  C CD1 . LEU A 1 48  ? -29.32500 -9.42700  -38.11900 1.000 41.51000 ? 50  LEU A CD1 1 
ATOM   371  C CD2 . LEU A 1 48  ? -27.03800 -8.53500  -38.48700 1.000 40.50000 ? 50  LEU A CD2 1 
ATOM   372  N N   . ASN A 1 49  ? -30.22700 -4.03900  -38.27400 1.000 33.83000 ? 51  ASN A N   1 
ATOM   373  C CA  . ASN A 1 49  ? -30.61600 -2.83600  -39.01600 1.000 32.51000 ? 51  ASN A CA  1 
ATOM   374  C C   . ASN A 1 49  ? -31.58500 -1.98800  -38.20600 1.000 36.81000 ? 51  ASN A C   1 
ATOM   375  O O   . ASN A 1 49  ? -32.72800 -1.75900  -38.61500 1.000 34.61000 ? 51  ASN A O   1 
ATOM   376  C CB  . ASN A 1 49  ? -31.21700 -3.21900  -40.36600 1.000 33.33000 ? 51  ASN A CB  1 
ATOM   377  C CG  . ASN A 1 49  ? -30.16700 -3.73900  -41.32400 1.000 30.54000 ? 51  ASN A CG  1 
ATOM   378  O OD1 . ASN A 1 49  ? -29.37700 -2.96700  -41.85900 1.000 32.10000 ? 51  ASN A OD1 1 
ATOM   379  N ND2 . ASN A 1 49  ? -30.14800 -5.04800  -41.53800 1.000 31.80000 ? 51  ASN A ND2 1 
ATOM   380  N N   . PRO A 1 50  ? -31.15200 -1.47600  -37.05300 1.000 35.87000 ? 52  PRO A N   1 
ATOM   381  C CA  . PRO A 1 50  ? -32.05500 -0.62100  -36.27800 1.000 32.13000 ? 52  PRO A CA  1 
ATOM   382  C C   . PRO A 1 50  ? -32.23600 0.72300   -36.96800 1.000 31.63000 ? 52  PRO A C   1 
ATOM   383  O O   . PRO A 1 50  ? -31.32100 1.25200   -37.60000 1.000 27.63000 ? 52  PRO A O   1 
ATOM   384  C CB  . PRO A 1 50  ? -31.34000 -0.47600  -34.92900 1.000 35.97000 ? 52  PRO A CB  1 
ATOM   385  C CG  . PRO A 1 50  ? -29.88300 -0.59500  -35.27900 1.000 32.96000 ? 52  PRO A CG  1 
ATOM   386  C CD  . PRO A 1 50  ? -29.81300 -1.56800  -36.43100 1.000 35.41000 ? 52  PRO A CD  1 
ATOM   387  N N   . ASN A 1 51  ? -33.44900 1.25300   -36.88200 1.000 30.65000 ? 53  ASN A N   1 
ATOM   388  C CA  . ASN A 1 51  ? -33.71800 2.64200   -37.23500 1.000 27.49000 ? 53  ASN A CA  1 
ATOM   389  C C   . ASN A 1 51  ? -33.81600 3.39300   -35.91600 1.000 31.34000 ? 53  ASN A C   1 
ATOM   390  O O   . ASN A 1 51  ? -34.82800 3.31400   -35.21400 1.000 26.65000 ? 53  ASN A O   1 
ATOM   391  C CB  . ASN A 1 51  ? -35.00000 2.79100   -38.05700 1.000 30.50000 ? 53  ASN A CB  1 
ATOM   392  C CG  . ASN A 1 51  ? -35.17200 4.20200   -38.59000 1.000 31.43000 ? 53  ASN A CG  1 
ATOM   393  O OD1 . ASN A 1 51  ? -35.38400 5.14100   -37.82800 1.000 30.92000 ? 53  ASN A OD1 1 
ATOM   394  N ND2 . ASN A 1 51  ? -35.06300 4.36200   -39.90300 1.000 37.83000 ? 53  ASN A ND2 1 
ATOM   395  N N   . TYR A 1 52  ? -32.75800 4.12300   -35.57300 1.000 29.44000 ? 54  TYR A N   1 
ATOM   396  C CA  . TYR A 1 52  ? -32.70600 4.74400   -34.25900 1.000 28.58000 ? 54  TYR A CA  1 
ATOM   397  C C   . TYR A 1 52  ? -33.72200 5.87400   -34.10900 1.000 29.81000 ? 54  TYR A C   1 
ATOM   398  O O   . TYR A 1 52  ? -34.23700 6.09400   -33.00300 1.000 26.37000 ? 54  TYR A O   1 
ATOM   399  C CB  . TYR A 1 52  ? -31.27900 5.23300   -33.99500 1.000 28.19000 ? 54  TYR A CB  1 
ATOM   400  C CG  . TYR A 1 52  ? -30.35400 4.09400   -33.62900 1.000 28.10000 ? 54  TYR A CG  1 
ATOM   401  C CD1 . TYR A 1 52  ? -30.48900 3.43500   -32.42000 1.000 30.82000 ? 54  TYR A CD1 1 
ATOM   402  C CD2 . TYR A 1 52  ? -29.36100 3.65500   -34.50900 1.000 30.11000 ? 54  TYR A CD2 1 
ATOM   403  C CE1 . TYR A 1 52  ? -29.64500 2.38200   -32.07600 1.000 30.27000 ? 54  TYR A CE1 1 
ATOM   404  C CE2 . TYR A 1 52  ? -28.51700 2.60900   -34.17100 1.000 28.88000 ? 54  TYR A CE2 1 
ATOM   405  C CZ  . TYR A 1 52  ? -28.67200 1.97900   -32.96000 1.000 29.49000 ? 54  TYR A CZ  1 
ATOM   406  O OH  . TYR A 1 52  ? -27.84700 0.94100   -32.61200 1.000 31.87000 ? 54  TYR A OH  1 
ATOM   407  N N   . GLU A 1 53  ? -34.00900 6.61000   -35.18600 1.000 29.64000 ? 55  GLU A N   1 
ATOM   408  C CA  . GLU A 1 53  ? -35.03800 7.64200   -35.11300 1.000 29.69000 ? 55  GLU A CA  1 
ATOM   409  C C   . GLU A 1 53  ? -36.38900 7.03400   -34.74000 1.000 28.09000 ? 55  GLU A C   1 
ATOM   410  O O   . GLU A 1 53  ? -37.10300 7.56200   -33.88000 1.000 28.99000 ? 55  GLU A O   1 
ATOM   411  C CB  . GLU A 1 53  ? -35.12200 8.39000   -36.44600 1.000 34.35000 ? 55  GLU A CB  1 
ATOM   412  C CG  . GLU A 1 53  ? -36.24800 9.45200   -36.51700 1.000 38.87000 ? 55  GLU A CG  1 
ATOM   413  C CD  . GLU A 1 53  ? -36.48000 9.98200   -37.93900 1.000 43.79000 ? 55  GLU A CD  1 
ATOM   414  O OE1 . GLU A 1 53  ? -37.41200 10.80600  -38.13500 1.000 40.31000 ? 55  GLU A OE1 1 
ATOM   415  O OE2 . GLU A 1 53  ? -35.72700 9.57200   -38.85800 1.000 43.16000 ? 55  GLU A OE2 1 
ATOM   416  N N   . ASP A 1 54  ? -36.72400 5.89600   -35.34500 1.000 26.03000 ? 56  ASP A N   1 
ATOM   417  C CA  . ASP A 1 54  ? -37.99200 5.22600   -35.06800 1.000 30.15000 ? 56  ASP A CA  1 
ATOM   418  C C   . ASP A 1 54  ? -37.98400 4.56700   -33.69000 1.000 30.43000 ? 56  ASP A C   1 
ATOM   419  O O   . ASP A 1 54  ? -39.00800 4.54800   -32.99600 1.000 28.98000 ? 56  ASP A O   1 
ATOM   420  C CB  . ASP A 1 54  ? -38.27800 4.20200   -36.17000 1.000 25.80000 ? 56  ASP A CB  1 
ATOM   421  C CG  . ASP A 1 54  ? -39.74000 3.79700   -36.22500 1.000 32.62000 ? 56  ASP A CG  1 
ATOM   422  O OD1 . ASP A 1 54  ? -40.56800 4.61700   -36.67400 1.000 31.93000 ? 56  ASP A OD1 1 
ATOM   423  O OD2 . ASP A 1 54  ? -40.06100 2.66700   -35.81200 1.000 32.29000 ? 56  ASP A OD2 1 
ATOM   424  N N   . LEU A 1 55  ? -36.84100 4.01300   -33.27300 1.000 25.62000 ? 57  LEU A N   1 
ATOM   425  C CA  . LEU A 1 55  ? -36.76900 3.44000   -31.93400 1.000 25.89000 ? 57  LEU A CA  1 
ATOM   426  C C   . LEU A 1 55  ? -36.94400 4.51500   -30.86800 1.000 27.72000 ? 57  LEU A C   1 
ATOM   427  O O   . LEU A 1 55  ? -37.60800 4.28400   -29.84900 1.000 30.55000 ? 57  LEU A O   1 
ATOM   428  C CB  . LEU A 1 55  ? -35.43200 2.71300   -31.74000 1.000 28.95000 ? 57  LEU A CB  1 
ATOM   429  C CG  . LEU A 1 55  ? -35.29100 1.38100   -32.48000 1.000 29.84000 ? 57  LEU A CG  1 
ATOM   430  C CD1 . LEU A 1 55  ? -33.83900 0.86500   -32.39100 1.000 32.31000 ? 57  LEU A CD1 1 
ATOM   431  C CD2 . LEU A 1 55  ? -36.27600 0.36000   -31.93200 1.000 34.34000 ? 57  LEU A CD2 1 
ATOM   432  N N   . LEU A 1 56  ? -36.34300 5.69100   -31.07700 1.000 25.74000 ? 58  LEU A N   1 
ATOM   433  C CA  . LEU A 1 56  ? -36.35600 6.72000   -30.04000 1.000 25.43000 ? 58  LEU A CA  1 
ATOM   434  C C   . LEU A 1 56  ? -37.73200 7.37100   -29.90700 1.000 27.18000 ? 58  LEU A C   1 
ATOM   435  O O   . LEU A 1 56  ? -38.18700 7.64100   -28.79000 1.000 28.46000 ? 58  LEU A O   1 
ATOM   436  C CB  . LEU A 1 56  ? -35.30000 7.78100   -30.33000 1.000 30.93000 ? 58  LEU A CB  1 
ATOM   437  C CG  . LEU A 1 56  ? -35.04900 8.76400   -29.17900 1.000 29.06000 ? 58  LEU A CG  1 
ATOM   438  C CD1 . LEU A 1 56  ? -34.71900 8.03500   -27.87600 1.000 27.58000 ? 58  LEU A CD1 1 
ATOM   439  C CD2 . LEU A 1 56  ? -33.95700 9.77800   -29.53900 1.000 28.81000 ? 58  LEU A CD2 1 
ATOM   440  N N   . ILE A 1 57  ? -38.40500 7.64200   -31.02800 1.000 27.24000 ? 59  ILE A N   1 
ATOM   441  C CA  . ILE A 1 57  ? -39.71500 8.29300   -30.94000 1.000 29.73000 ? 59  ILE A CA  1 
ATOM   442  C C   . ILE A 1 57  ? -40.69800 7.48300   -30.10200 1.000 28.75000 ? 59  ILE A C   1 
ATOM   443  O O   . ILE A 1 57  ? -41.64700 8.04900   -29.53800 1.000 30.18000 ? 59  ILE A O   1 
ATOM   444  C CB  . ILE A 1 57  ? -40.26900 8.58500   -32.35500 1.000 27.21000 ? 59  ILE A CB  1 
ATOM   445  C CG1 . ILE A 1 57  ? -41.34800 9.68300   -32.29400 1.000 30.11000 ? 59  ILE A CG1 1 
ATOM   446  C CG2 . ILE A 1 57  ? -40.79200 7.31400   -33.02900 1.000 29.60000 ? 59  ILE A CG2 1 
ATOM   447  C CD1 . ILE A 1 57  ? -41.66600 10.32000  -33.64900 1.000 29.25000 ? 59  ILE A CD1 1 
ATOM   448  N N   . ARG A 1 58  ? -40.48500 6.17300   -29.98900 1.000 26.51000 ? 60  ARG A N   1 
ATOM   449  C CA  . ARG A 1 58  ? -41.35400 5.29300   -29.22000 1.000 28.68000 ? 60  ARG A CA  1 
ATOM   450  C C   . ARG A 1 58  ? -41.01100 5.25700   -27.73600 1.000 31.21000 ? 60  ARG A C   1 
ATOM   451  O O   . ARG A 1 58  ? -41.74500 4.63800   -26.96100 1.000 32.40000 ? 60  ARG A O   1 
ATOM   452  C CB  . ARG A 1 58  ? -41.28000 3.87100   -29.77800 1.000 28.18000 ? 60  ARG A CB  1 
ATOM   453  C CG  . ARG A 1 58  ? -41.63100 3.74700   -31.25700 1.000 24.47000 ? 60  ARG A CG  1 
ATOM   454  C CD  . ARG A 1 58  ? -41.37700 2.33000   -31.74400 1.000 26.29000 ? 60  ARG A CD  1 
ATOM   455  N NE  . ARG A 1 58  ? -41.50000 2.22300   -33.19500 1.000 28.39000 ? 60  ARG A NE  1 
ATOM   456  C CZ  . ARG A 1 58  ? -42.59700 1.80800   -33.82600 1.000 28.74000 ? 60  ARG A CZ  1 
ATOM   457  N NH1 . ARG A 1 58  ? -43.67800 1.44700   -33.13900 1.000 30.35000 ? 60  ARG A NH1 1 
ATOM   458  N NH2 . ARG A 1 58  ? -42.61200 1.74700   -35.15200 1.000 26.63000 ? 60  ARG A NH2 1 
ATOM   459  N N   . LYS A 1 59  ? -39.91800 5.88200   -27.32500 1.000 30.94000 ? 61  LYS A N   1 
ATOM   460  C CA  . LYS A 1 59  ? -39.54600 5.90300   -25.92200 1.000 33.11000 ? 61  LYS A CA  1 
ATOM   461  C C   . LYS A 1 59  ? -40.12400 7.13600   -25.24100 1.000 32.67000 ? 61  LYS A C   1 
ATOM   462  O O   . LYS A 1 59  ? -40.18500 8.22100   -25.82800 1.000 31.23000 ? 61  LYS A O   1 
ATOM   463  C CB  . LYS A 1 59  ? -38.02600 5.89500   -25.76600 1.000 33.53000 ? 61  LYS A CB  1 
ATOM   464  C CG  . LYS A 1 59  ? -37.33300 4.67000   -26.36300 1.000 32.25000 ? 61  LYS A CG  1 
ATOM   465  C CD  . LYS A 1 59  ? -37.56900 3.43900   -25.51100 1.000 37.82000 ? 61  LYS A CD  1 
ATOM   466  C CE  . LYS A 1 59  ? -36.94300 2.21200   -26.16500 1.000 36.86000 ? 61  LYS A CE  1 
ATOM   467  N NZ  . LYS A 1 59  ? -37.54600 1.97100   -27.51200 1.000 40.07000 ? 61  LYS A NZ  1 
ATOM   468  N N   . SER A 1 60  ? -40.53100 6.97000   -23.99300 1.000 31.46000 ? 62  SER A N   1 
ATOM   469  C CA  . SER A 1 60  ? -40.76800 8.12100   -23.13900 1.000 35.98000 ? 62  SER A CA  1 
ATOM   470  C C   . SER A 1 60  ? -39.65600 8.21100   -22.10400 1.000 34.59000 ? 62  SER A C   1 
ATOM   471  O O   . SER A 1 60  ? -38.82500 7.30700   -21.96400 1.000 34.24000 ? 62  SER A O   1 
ATOM   472  C CB  . SER A 1 60  ? -42.15100 8.06500   -22.47000 1.000 40.59000 ? 62  SER A CB  1 
ATOM   473  O OG  . SER A 1 60  ? -42.55600 6.74500   -22.16100 1.000 47.35000 ? 62  SER A OG  1 
ATOM   474  N N   . ASN A 1 61  ? -39.64700 9.33600   -21.39200 1.000 34.56000 ? 63  ASN A N   1 
ATOM   475  C CA  . ASN A 1 61  ? -38.60400 9.58600   -20.40300 1.000 36.34000 ? 63  ASN A CA  1 
ATOM   476  C C   . ASN A 1 61  ? -38.49900 8.44800   -19.39600 1.000 35.50000 ? 63  ASN A C   1 
ATOM   477  O O   . ASN A 1 61  ? -37.39300 8.05800   -19.00600 1.000 37.45000 ? 63  ASN A O   1 
ATOM   478  C CB  . ASN A 1 61  ? -38.87700 10.91200  -19.69900 1.000 34.23000 ? 63  ASN A CB  1 
ATOM   479  C CG  . ASN A 1 61  ? -38.66800 12.09700  -20.60600 1.000 36.54000 ? 63  ASN A CG  1 
ATOM   480  O OD1 . ASN A 1 61  ? -37.79700 12.08000  -21.48100 1.000 39.05000 ? 63  ASN A OD1 1 
ATOM   481  N ND2 . ASN A 1 61  ? -39.45800 13.14200  -20.40300 1.000 32.88000 ? 63  ASN A ND2 1 
ATOM   482  N N   . HIS A 1 62  ? -39.63800 7.88500   -18.97300 1.000 34.67000 ? 64  HIS A N   1 
ATOM   483  C CA  . HIS A 1 62  ? -39.58200 6.85700   -17.93400 1.000 36.20000 ? 64  HIS A CA  1 
ATOM   484  C C   . HIS A 1 62  ? -39.08700 5.50300   -18.43900 1.000 35.64000 ? 64  HIS A C   1 
ATOM   485  O O   . HIS A 1 62  ? -38.92900 4.58900   -17.61900 1.000 37.00000 ? 64  HIS A O   1 
ATOM   486  C CB  . HIS A 1 62  ? -40.95000 6.69300   -17.26200 1.000 41.01000 ? 64  HIS A CB  1 
ATOM   487  C CG  . HIS A 1 62  ? -42.05900 6.37100   -18.21000 1.000 38.85000 ? 64  HIS A CG  1 
ATOM   488  N ND1 . HIS A 1 62  ? -42.27200 5.10100   -18.70300 1.000 42.44000 ? 64  HIS A ND1 1 
ATOM   489  C CD2 . HIS A 1 62  ? -43.02900 7.15100   -18.74500 1.000 43.22000 ? 64  HIS A CD2 1 
ATOM   490  C CE1 . HIS A 1 62  ? -43.32200 5.11300   -19.50500 1.000 43.30000 ? 64  HIS A CE1 1 
ATOM   491  N NE2 . HIS A 1 62  ? -43.80100 6.34500   -19.54600 1.000 41.17000 ? 64  HIS A NE2 1 
ATOM   492  N N   . ASN A 1 63  ? -38.81100 5.35000   -19.73700 1.000 33.26000 ? 65  ASN A N   1 
ATOM   493  C CA  . ASN A 1 63  ? -38.16800 4.14100   -20.24500 1.000 32.35000 ? 65  ASN A CA  1 
ATOM   494  C C   . ASN A 1 63  ? -36.65500 4.12900   -19.99900 1.000 33.66000 ? 65  ASN A C   1 
ATOM   495  O O   . ASN A 1 63  ? -36.01100 3.09900   -20.22500 1.000 30.10000 ? 65  ASN A O   1 
ATOM   496  C CB  . ASN A 1 63  ? -38.44900 3.98200   -21.74900 1.000 31.94000 ? 65  ASN A CB  1 
ATOM   497  C CG  . ASN A 1 63  ? -39.94400 3.79100   -22.06500 1.000 38.91000 ? 65  ASN A CG  1 
ATOM   498  O OD1 . ASN A 1 63  ? -40.48200 4.41400   -22.98700 1.000 37.91000 ? 65  ASN A OD1 1 
ATOM   499  N ND2 . ASN A 1 63  ? -40.60800 2.92300   -21.31100 1.000 38.21000 ? 65  ASN A ND2 1 
ATOM   500  N N   . PHE A 1 64  ? -36.08300 5.23400   -19.53100 1.000 30.08000 ? 66  PHE A N   1 
ATOM   501  C CA  . PHE A 1 64  ? -34.66000 5.33800   -19.21400 1.000 28.74000 ? 66  PHE A CA  1 
ATOM   502  C C   . PHE A 1 64  ? -34.47700 5.35900   -17.70200 1.000 34.04000 ? 66  PHE A C   1 
ATOM   503  O O   . PHE A 1 64  ? -35.00100 6.24900   -17.01900 1.000 36.72000 ? 66  PHE A O   1 
ATOM   504  C CB  . PHE A 1 64  ? -34.07100 6.59800   -19.84200 1.000 26.63000 ? 66  PHE A CB  1 
ATOM   505  C CG  . PHE A 1 64  ? -34.12600 6.59700   -21.34300 1.000 28.21000 ? 66  PHE A CG  1 
ATOM   506  C CD1 . PHE A 1 64  ? -33.26200 5.79700   -22.07700 1.000 29.43000 ? 66  PHE A CD1 1 
ATOM   507  C CD2 . PHE A 1 64  ? -35.05500 7.38500   -22.02300 1.000 30.81000 ? 66  PHE A CD2 1 
ATOM   508  C CE1 . PHE A 1 64  ? -33.31200 5.79000   -23.46100 1.000 32.62000 ? 66  PHE A CE1 1 
ATOM   509  C CE2 . PHE A 1 64  ? -35.11500 7.38600   -23.40000 1.000 30.45000 ? 66  PHE A CE2 1 
ATOM   510  C CZ  . PHE A 1 64  ? -34.24900 6.58600   -24.12700 1.000 32.03000 ? 66  PHE A CZ  1 
ATOM   511  N N   . LEU A 1 65  ? -33.73800 4.38600   -17.18200 1.000 30.81000 ? 67  LEU A N   1 
ATOM   512  C CA  . LEU A 1 65  ? -33.38500 4.33200   -15.77200 1.000 31.90000 ? 67  LEU A CA  1 
ATOM   513  C C   . LEU A 1 65  ? -31.92100 4.74500   -15.65700 1.000 33.95000 ? 67  LEU A C   1 
ATOM   514  O O   . LEU A 1 65  ? -31.04700 4.10000   -16.24800 1.000 30.80000 ? 67  LEU A O   1 
ATOM   515  C CB  . LEU A 1 65  ? -33.62000 2.92600   -15.21600 1.000 35.43000 ? 67  LEU A CB  1 
ATOM   516  C CG  . LEU A 1 65  ? -33.19300 2.58400   -13.78500 1.000 42.66000 ? 67  LEU A CG  1 
ATOM   517  C CD1 . LEU A 1 65  ? -33.95000 3.42700   -12.78200 1.000 42.62000 ? 67  LEU A CD1 1 
ATOM   518  C CD2 . LEU A 1 65  ? -33.40400 1.09000   -13.50200 1.000 45.74000 ? 67  LEU A CD2 1 
ATOM   519  N N   . VAL A 1 66  ? -31.66900 5.85500   -14.96400 1.000 31.76000 ? 68  VAL A N   1 
ATOM   520  C CA  . VAL A 1 66  ? -30.32300 6.36300   -14.72600 1.000 32.49000 ? 68  VAL A CA  1 
ATOM   521  C C   . VAL A 1 66  ? -30.04700 6.27300   -13.23500 1.000 36.28000 ? 68  VAL A C   1 
ATOM   522  O O   . VAL A 1 66  ? -30.85800 6.72900   -12.41700 1.000 32.67000 ? 68  VAL A O   1 
ATOM   523  C CB  . VAL A 1 66  ? -30.16100 7.80600   -15.23200 1.000 31.48000 ? 68  VAL A CB  1 
ATOM   524  C CG1 . VAL A 1 66  ? -28.71700 8.29800   -15.03500 1.000 30.68000 ? 68  VAL A CG1 1 
ATOM   525  C CG2 . VAL A 1 66  ? -30.58400 7.89500   -16.68800 1.000 32.00000 ? 68  VAL A CG2 1 
ATOM   526  N N   . GLN A 1 67  ? -28.90500 5.68000   -12.88000 1.000 30.67000 ? 69  GLN A N   1 
ATOM   527  C CA  . GLN A 1 67  ? -28.53000 5.49500   -11.48500 1.000 31.24000 ? 69  GLN A CA  1 
ATOM   528  C C   . GLN A 1 67  ? -27.10900 6.00100   -11.28300 1.000 33.35000 ? 69  GLN A C   1 
ATOM   529  O O   . GLN A 1 67  ? -26.18000 5.53200   -11.94600 1.000 29.91000 ? 69  GLN A O   1 
ATOM   530  C CB  . GLN A 1 67  ? -28.64700 4.02600   -11.07700 1.000 36.74000 ? 69  GLN A CB  1 
ATOM   531  C CG  . GLN A 1 67  ? -29.49600 3.83200   -9.83600  1.000 48.85000 ? 69  GLN A CG  1 
ATOM   532  C CD  . GLN A 1 67  ? -29.75700 2.36800   -9.52200  1.000 53.72000 ? 69  GLN A CD  1 
ATOM   533  O OE1 . GLN A 1 67  ? -30.75200 1.79000   -9.97200  1.000 55.85000 ? 69  GLN A OE1 1 
ATOM   534  N NE2 . GLN A 1 67  ? -28.85800 1.75900   -8.74800  1.000 53.29000 ? 69  GLN A NE2 1 
ATOM   535  N N   . ALA A 1 68  ? -26.95100 6.95300   -10.37400 1.000 36.68000 ? 70  ALA A N   1 
ATOM   536  C CA  . ALA A 1 68  ? -25.65100 7.49200   -9.98400  1.000 35.04000 ? 70  ALA A CA  1 
ATOM   537  C C   . ALA A 1 68  ? -25.34000 6.95600   -8.58800  1.000 39.85000 ? 70  ALA A C   1 
ATOM   538  O O   . ALA A 1 68  ? -25.86000 7.46300   -7.58900  1.000 40.68000 ? 70  ALA A O   1 
ATOM   539  C CB  . ALA A 1 68  ? -25.66400 9.01900   -10.01900 1.000 32.83000 ? 70  ALA A CB  1 
ATOM   540  N N   . GLY A 1 69  ? -24.48700 5.93400   -8.52400  1.000 38.05000 ? 71  GLY A N   1 
ATOM   541  C CA  . GLY A 1 69  ? -24.31700 5.20800   -7.27500  1.000 41.50000 ? 71  GLY A CA  1 
ATOM   542  C C   . GLY A 1 69  ? -25.64800 4.61000   -6.85100  1.000 40.80000 ? 71  GLY A C   1 
ATOM   543  O O   . GLY A 1 69  ? -26.29800 3.87400   -7.60900  1.000 40.82000 ? 71  GLY A O   1 
ATOM   544  N N   . ASN A 1 70  ? -26.08900 4.93600   -5.63800  1.000 43.61000 ? 72  ASN A N   1 
ATOM   545  C CA  . ASN A 1 70  ? -27.34700 4.40900   -5.12500  1.000 48.15000 ? 72  ASN A CA  1 
ATOM   546  C C   . ASN A 1 70  ? -28.55000 5.29300   -5.44800  1.000 46.85000 ? 72  ASN A C   1 
ATOM   547  O O   . ASN A 1 70  ? -29.66900 4.92800   -5.08200  1.000 51.82000 ? 72  ASN A O   1 
ATOM   548  C CB  . ASN A 1 70  ? -27.25700 4.20600   -3.60600  1.000 47.49000 ? 72  ASN A CB  1 
ATOM   549  N N   . VAL A 1 71  ? -28.36100 6.42600   -6.13500  1.000 43.45000 ? 73  VAL A N   1 
ATOM   550  C CA  . VAL A 1 71  ? -29.41900 7.41700   -6.34600  1.000 45.04000 ? 73  VAL A CA  1 
ATOM   551  C C   . VAL A 1 71  ? -29.96400 7.28500   -7.76300  1.000 43.69000 ? 73  VAL A C   1 
ATOM   552  O O   . VAL A 1 71  ? -29.18900 7.21000   -8.72600  1.000 40.21000 ? 73  VAL A O   1 
ATOM   553  C CB  . VAL A 1 71  ? -28.89300 8.84400   -6.10100  1.000 42.84000 ? 73  VAL A CB  1 
ATOM   554  C CG1 . VAL A 1 71  ? -30.04000 9.84700   -6.11700  1.000 50.57000 ? 73  VAL A CG1 1 
ATOM   555  C CG2 . VAL A 1 71  ? -28.11800 8.91200   -4.79100  1.000 48.38000 ? 73  VAL A CG2 1 
ATOM   556  N N   . GLN A 1 72  ? -31.29600 7.27600   -7.89800  1.000 38.33000 ? 74  GLN A N   1 
ATOM   557  C CA  . GLN A 1 72  ? -31.94400 7.27500   -9.20500  1.000 39.58000 ? 74  GLN A CA  1 
ATOM   558  C C   . GLN A 1 72  ? -32.12000 8.71300   -9.68100  1.000 39.50000 ? 74  GLN A C   1 
ATOM   559  O O   . GLN A 1 72  ? -32.72700 9.53300   -8.98500  1.000 46.52000 ? 74  GLN A O   1 
ATOM   560  C CB  . GLN A 1 72  ? -33.29700 6.55800   -9.15800  1.000 40.89000 ? 74  GLN A CB  1 
ATOM   561  C CG  . GLN A 1 72  ? -33.80700 6.09600   -10.52600 1.000 44.76000 ? 74  GLN A CG  1 
ATOM   562  C CD  . GLN A 1 72  ? -35.33300 6.01200   -10.62200 1.000 52.09000 ? 74  GLN A CD  1 
ATOM   563  O OE1 . GLN A 1 72  ? -35.95700 6.64300   -11.48500 1.000 50.79000 ? 74  GLN A OE1 1 
ATOM   564  N NE2 . GLN A 1 72  ? -35.93600 5.22100   -9.74100  1.000 53.78000 ? 74  GLN A NE2 1 
ATOM   565  N N   . LEU A 1 73  ? -31.58800 9.01900   -10.85900 1.000 35.76000 ? 75  LEU A N   1 
ATOM   566  C CA  . LEU A 1 73  ? -31.77100 10.32400  -11.47900 1.000 33.27000 ? 75  LEU A CA  1 
ATOM   567  C C   . LEU A 1 73  ? -32.99000 10.26200  -12.38600 1.000 37.49000 ? 75  LEU A C   1 
ATOM   568  O O   . LEU A 1 73  ? -33.11300 9.34000   -13.19700 1.000 40.57000 ? 75  LEU A O   1 
ATOM   569  C CB  . LEU A 1 73  ? -30.54000 10.72400  -12.29400 1.000 35.79000 ? 75  LEU A CB  1 
ATOM   570  C CG  . LEU A 1 73  ? -29.20400 10.74700  -11.55100 1.000 32.32000 ? 75  LEU A CG  1 
ATOM   571  C CD1 . LEU A 1 73  ? -28.12900 11.37400  -12.42600 1.000 35.56000 ? 75  LEU A CD1 1 
ATOM   572  C CD2 . LEU A 1 73  ? -29.35500 11.50900  -10.25500 1.000 34.82000 ? 75  LEU A CD2 1 
ATOM   573  N N   . ARG A 1 74  ? -33.87600 11.24500  -12.26100 1.000 33.22000 ? 76  ARG A N   1 
ATOM   574  C CA  . ARG A 1 74  ? -35.10300 11.26300  -13.05800 1.000 34.79000 ? 76  ARG A CA  1 
ATOM   575  C C   . ARG A 1 74  ? -34.82800 11.87800  -14.42700 1.000 31.15000 ? 76  ARG A C   1 
ATOM   576  O O   . ARG A 1 74  ? -34.35000 13.01200  -14.52100 1.000 34.47000 ? 76  ARG A O   1 
ATOM   577  C CB  . ARG A 1 74  ? -36.19700 12.03800  -12.32900 1.000 37.16000 ? 76  ARG A CB  1 
ATOM   578  N N   . VAL A 1 75  ? -35.12900 11.13700  -15.48800 1.000 28.84000 ? 77  VAL A N   1 
ATOM   579  C CA  . VAL A 1 75  ? -34.96700 11.65300  -16.84500 1.000 32.05000 ? 77  VAL A CA  1 
ATOM   580  C C   . VAL A 1 75  ? -36.15900 12.54500  -17.18800 1.000 33.78000 ? 77  VAL A C   1 
ATOM   581  O O   . VAL A 1 75  ? -37.31200 12.11700  -17.08200 1.000 32.05000 ? 77  VAL A O   1 
ATOM   582  C CB  . VAL A 1 75  ? -34.82300 10.50500  -17.85400 1.000 34.73000 ? 77  VAL A CB  1 
ATOM   583  C CG1 . VAL A 1 75  ? -34.68100 11.05400  -19.26800 1.000 33.39000 ? 77  VAL A CG1 1 
ATOM   584  C CG2 . VAL A 1 75  ? -33.61700 9.63600   -17.49800 1.000 33.38000 ? 77  VAL A CG2 1 
ATOM   585  N N   . ILE A 1 76  ? -35.88400 13.78600  -17.59800 1.000 33.96000 ? 78  ILE A N   1 
ATOM   586  C CA  . ILE A 1 76  ? -36.92600 14.75700  -17.93900 1.000 36.73000 ? 78  ILE A CA  1 
ATOM   587  C C   . ILE A 1 76  ? -36.90200 15.15100  -19.40600 1.000 36.69000 ? 78  ILE A C   1 
ATOM   588  O O   . ILE A 1 76  ? -37.65600 16.04900  -19.81100 1.000 35.46000 ? 78  ILE A O   1 
ATOM   589  C CB  . ILE A 1 76  ? -36.83200 16.01600  -17.05500 1.000 34.48000 ? 78  ILE A CB  1 
ATOM   590  C CG1 . ILE A 1 76  ? -35.50600 16.75100  -17.31100 1.000 35.59000 ? 78  ILE A CG1 1 
ATOM   591  C CG2 . ILE A 1 76  ? -36.95700 15.64300  -15.58100 1.000 36.27000 ? 78  ILE A CG2 1 
ATOM   592  C CD1 . ILE A 1 76  ? -35.35900 18.02600  -16.50700 1.000 35.73000 ? 78  ILE A CD1 1 
ATOM   593  N N   . GLY A 1 77  ? -36.05500 14.52900  -20.21300 1.000 33.71000 ? 79  GLY A N   1 
ATOM   594  C CA  . GLY A 1 77  ? -36.01700 14.83200  -21.62800 1.000 36.00000 ? 79  GLY A CA  1 
ATOM   595  C C   . GLY A 1 77  ? -34.94600 13.98700  -22.27800 1.000 35.75000 ? 79  GLY A C   1 
ATOM   596  O O   . GLY A 1 77  ? -34.01400 13.51400  -21.62100 1.000 31.33000 ? 79  GLY A O   1 
ATOM   597  N N   . HIS A 1 78  ? -35.10800 13.77700  -23.58100 1.000 35.12000 ? 80  HIS A N   1 
ATOM   598  C CA  . HIS A 1 78  ? -34.09200 13.00500  -24.28700 1.000 35.41000 ? 80  HIS A CA  1 
ATOM   599  C C   . HIS A 1 78  ? -33.97500 13.51200  -25.71400 1.000 40.39000 ? 80  HIS A C   1 
ATOM   600  O O   . HIS A 1 78  ? -34.91500 14.08500  -26.27600 1.000 37.26000 ? 80  HIS A O   1 
ATOM   601  C CB  . HIS A 1 78  ? -34.40600 11.50500  -24.26300 1.000 34.47000 ? 80  HIS A CB  1 
ATOM   602  C CG  . HIS A 1 78  ? -35.74100 11.16000  -24.84900 1.000 35.81000 ? 80  HIS A CG  1 
ATOM   603  N ND1 . HIS A 1 78  ? -36.85800 10.93700  -24.07400 1.000 38.74000 ? 80  HIS A ND1 1 
ATOM   604  C CD2 . HIS A 1 78  ? -36.13700 11.00000  -26.13500 1.000 37.51000 ? 80  HIS A CD2 1 
ATOM   605  C CE1 . HIS A 1 78  ? -37.88800 10.65600  -24.85700 1.000 38.64000 ? 80  HIS A CE1 1 
ATOM   606  N NE2 . HIS A 1 78  ? -37.47700 10.68900  -26.11100 1.000 37.50000 ? 80  HIS A NE2 1 
ATOM   607  N N   . SER A 1 79  ? -32.80600 13.27300  -26.29800 1.000 31.45000 ? 81  SER A N   1 
ATOM   608  C CA  . SER A 1 79  ? -32.47000 13.79700  -27.60900 1.000 34.32000 ? 81  SER A CA  1 
ATOM   609  C C   . SER A 1 79  ? -31.29200 12.99000  -28.14000 1.000 34.73000 ? 81  SER A C   1 
ATOM   610  O O   . SER A 1 79  ? -30.50600 12.43800  -27.36700 1.000 34.95000 ? 81  SER A O   1 
ATOM   611  C CB  . SER A 1 79  ? -32.15600 15.29600  -27.50600 1.000 36.12000 ? 81  SER A CB  1 
ATOM   612  O OG  . SER A 1 79  ? -31.19800 15.72400  -28.44000 1.000 46.86000 ? 81  SER A OG  1 
ATOM   613  N N   . MET A 1 80  ? -31.20100 12.88900  -29.45600 1.000 29.50000 ? 82  MET A N   1 
ATOM   614  C CA  . MET A 1 80  ? -30.16500 12.09800  -30.10400 1.000 32.70000 ? 82  MET A CA  1 
ATOM   615  C C   . MET A 1 80  ? -29.27400 13.02800  -30.90900 1.000 32.22000 ? 82  MET A C   1 
ATOM   616  O O   . MET A 1 80  ? -29.76800 13.86400  -31.67500 1.000 33.56000 ? 82  MET A O   1 
ATOM   617  C CB  . MET A 1 80  ? -30.79400 11.02200  -30.99600 1.000 33.27000 ? 82  MET A CB  1 
ATOM   618  C CG  . MET A 1 80  ? -29.80800 10.15400  -31.74700 1.000 31.20000 ? 82  MET A CG  1 
ATOM   619  S SD  . MET A 1 80  ? -30.55100 8.68100   -32.48500 1.000 33.30000 ? 82  MET A SD  1 
ATOM   620  C CE  . MET A 1 80  ? -31.53800 9.39300   -33.81400 1.000 34.27000 ? 82  MET A CE  1 
ATOM   621  N N   . GLN A 1 81  ? -27.96800 12.91600  -30.70800 1.000 30.19000 ? 83  GLN A N   1 
ATOM   622  C CA  . GLN A 1 81  ? -27.00000 13.68600  -31.47500 1.000 31.01000 ? 83  GLN A CA  1 
ATOM   623  C C   . GLN A 1 81  ? -26.05300 12.68800  -32.12300 1.000 31.74000 ? 83  GLN A C   1 
ATOM   624  O O   . GLN A 1 81  ? -25.25700 12.05300  -31.42900 1.000 27.59000 ? 83  GLN A O   1 
ATOM   625  C CB  . GLN A 1 81  ? -26.23500 14.67200  -30.60000 1.000 30.04000 ? 83  GLN A CB  1 
ATOM   626  C CG  . GLN A 1 81  ? -25.22400 15.48000  -31.39900 1.000 29.70000 ? 83  GLN A CG  1 
ATOM   627  C CD  . GLN A 1 81  ? -24.46300 16.45600  -30.54300 1.000 33.51000 ? 83  GLN A CD  1 
ATOM   628  O OE1 . GLN A 1 81  ? -24.56600 16.43500  -29.31300 1.000 35.95000 ? 83  GLN A OE1 1 
ATOM   629  N NE2 . GLN A 1 81  ? -23.72200 17.34300  -31.18300 1.000 35.80000 ? 83  GLN A NE2 1 
ATOM   630  N N   . ASN A 1 82  ? -26.16100 12.53900  -33.44400 1.000 28.44000 ? 84  ASN A N   1 
ATOM   631  C CA  . ASN A 1 82  ? -25.43600 11.49600  -34.15500 1.000 28.22000 ? 84  ASN A CA  1 
ATOM   632  C C   . ASN A 1 82  ? -25.64500 10.16100  -33.44300 1.000 28.73000 ? 84  ASN A C   1 
ATOM   633  O O   . ASN A 1 82  ? -26.78900 9.71400   -33.31100 1.000 28.45000 ? 84  ASN A O   1 
ATOM   634  C CB  . ASN A 1 82  ? -23.96600 11.91200  -34.29500 1.000 26.11000 ? 84  ASN A CB  1 
ATOM   635  C CG  . ASN A 1 82  ? -23.84200 13.26200  -34.96600 1.000 27.21000 ? 84  ASN A CG  1 
ATOM   636  O OD1 . ASN A 1 82  ? -24.28100 13.42700  -36.10400 1.000 30.44000 ? 84  ASN A OD1 1 
ATOM   637  N ND2 . ASN A 1 82  ? -23.34100 14.24800  -34.25000 1.000 29.69000 ? 84  ASN A ND2 1 
ATOM   638  N N   . CYS A 1 83  ? -24.58800 9.52600   -32.94800 1.000 25.51000 ? 85  CYS A N   1 
ATOM   639  C CA  . CYS A 1 83  ? -24.73400 8.22800   -32.30000 1.000 25.91000 ? 85  CYS A CA  1 
ATOM   640  C C   . CYS A 1 83  ? -24.68400 8.29300   -30.77600 1.000 25.86000 ? 85  CYS A C   1 
ATOM   641  O O   . CYS A 1 83  ? -24.51100 7.24900   -30.13300 1.000 24.73000 ? 85  CYS A O   1 
ATOM   642  C CB  . CYS A 1 83  ? -23.65700 7.25000   -32.78700 1.000 25.67000 ? 85  CYS A CB  1 
ATOM   643  S SG  . CYS A 1 83  ? -23.57900 6.98000   -34.55900 1.000 28.53000 ? 85  CYS A SG  1 
ATOM   644  N N   . VAL A 1 84  ? -24.81600 9.46800   -30.16200 1.000 23.33000 ? 86  VAL A N   1 
ATOM   645  C CA  . VAL A 1 84  ? -24.96100 9.51400   -28.70900 1.000 24.11000 ? 86  VAL A CA  1 
ATOM   646  C C   . VAL A 1 84  ? -26.36200 9.98100   -28.35200 1.000 29.02000 ? 86  VAL A C   1 
ATOM   647  O O   . VAL A 1 84  ? -26.97300 10.79200  -29.06000 1.000 27.46000 ? 86  VAL A O   1 
ATOM   648  C CB  . VAL A 1 84  ? -23.89500 10.37100  -27.98900 1.000 27.44000 ? 86  VAL A CB  1 
ATOM   649  C CG1 . VAL A 1 84  ? -22.51000 9.71400   -28.14700 1.000 26.81000 ? 86  VAL A CG1 1 
ATOM   650  C CG2 . VAL A 1 84  ? -23.90700 11.80700  -28.44400 1.000 30.64000 ? 86  VAL A CG2 1 
ATOM   651  N N   . LEU A 1 85  ? -26.88100 9.40500   -27.28000 1.000 24.12000 ? 87  LEU A N   1 
ATOM   652  C CA  . LEU A 1 85  ? -28.11900 9.82200   -26.66000 1.000 28.35000 ? 87  LEU A CA  1 
ATOM   653  C C   . LEU A 1 85  ? -27.77700 10.83700  -25.58100 1.000 31.86000 ? 87  LEU A C   1 
ATOM   654  O O   . LEU A 1 85  ? -26.75800 10.70700  -24.88000 1.000 26.04000 ? 87  LEU A O   1 
ATOM   655  C CB  . LEU A 1 85  ? -28.80900 8.59600   -26.07300 1.000 27.99000 ? 87  LEU A CB  1 
ATOM   656  C CG  . LEU A 1 85  ? -30.24900 8.53700   -25.61400 1.000 33.57000 ? 87  LEU A CG  1 
ATOM   657  C CD1 . LEU A 1 85  ? -31.20900 9.04600   -26.68700 1.000 33.57000 ? 87  LEU A CD1 1 
ATOM   658  C CD2 . LEU A 1 85  ? -30.50400 7.07300   -25.30800 1.000 30.42000 ? 87  LEU A CD2 1 
ATOM   659  N N   . LYS A 1 86  ? -28.58500 11.88300  -25.49600 1.000 28.90000 ? 88  LYS A N   1 
ATOM   660  C CA  . LYS A 1 86  ? -28.44500 12.89800  -24.45700 1.000 26.98000 ? 88  LYS A CA  1 
ATOM   661  C C   . LYS A 1 86  ? -29.69200 12.87200  -23.58900 1.000 31.38000 ? 88  LYS A C   1 
ATOM   662  O O   . LYS A 1 86  ? -30.77400 13.29300  -24.02900 1.000 30.87000 ? 88  LYS A O   1 
ATOM   663  C CB  . LYS A 1 86  ? -28.21600 14.27300  -25.07000 1.000 31.56000 ? 88  LYS A CB  1 
ATOM   664  C CG  . LYS A 1 86  ? -26.76300 14.48900  -25.45400 1.000 32.82000 ? 88  LYS A CG  1 
ATOM   665  C CD  . LYS A 1 86  ? -26.61800 15.22200  -26.76100 1.000 36.30000 ? 88  LYS A CD  1 
ATOM   666  C CE  . LYS A 1 86  ? -26.93800 16.69300  -26.63900 1.000 38.37000 ? 88  LYS A CE  1 
ATOM   667  N NZ  . LYS A 1 86  ? -26.97500 17.31000  -27.99900 1.000 38.95000 ? 88  LYS A NZ  1 
ATOM   668  N N   . LEU A 1 87  ? -29.55600 12.35400  -22.36600 1.000 27.94000 ? 89  LEU A N   1 
ATOM   669  C CA  . LEU A 1 87  ? -30.67400 12.25800  -21.43800 1.000 28.81000 ? 89  LEU A CA  1 
ATOM   670  C C   . LEU A 1 87  ? -30.64000 13.45300  -20.49700 1.000 31.65000 ? 89  LEU A C   1 
ATOM   671  O O   . LEU A 1 87  ? -29.68500 13.61500  -19.73500 1.000 29.72000 ? 89  LEU A O   1 
ATOM   672  C CB  . LEU A 1 87  ? -30.63400 10.95500  -20.64300 1.000 28.82000 ? 89  LEU A CB  1 
ATOM   673  C CG  . LEU A 1 87  ? -30.56400 9.67300   -21.46000 1.000 30.35000 ? 89  LEU A CG  1 
ATOM   674  C CD1 . LEU A 1 87  ? -30.57700 8.50400   -20.50300 1.000 32.14000 ? 89  LEU A CD1 1 
ATOM   675  C CD2 . LEU A 1 87  ? -31.75900 9.60000   -22.42800 1.000 30.50000 ? 89  LEU A CD2 1 
ATOM   676  N N   . LYS A 1 88  ? -31.67400 14.29500  -20.55800 1.000 27.26000 ? 90  LYS A N   1 
ATOM   677  C CA  . LYS A 1 88  ? -31.77500 15.40300  -19.61900 1.000 33.23000 ? 90  LYS A CA  1 
ATOM   678  C C   . LYS A 1 88  ? -32.27100 14.85700  -18.28800 1.000 32.44000 ? 90  LYS A C   1 
ATOM   679  O O   . LYS A 1 88  ? -33.25200 14.10800  -18.25800 1.000 32.25000 ? 90  LYS A O   1 
ATOM   680  C CB  . LYS A 1 88  ? -32.73000 16.47400  -20.15500 1.000 37.64000 ? 90  LYS A CB  1 
ATOM   681  C CG  . LYS A 1 88  ? -32.48200 17.86700  -19.60200 1.000 37.81000 ? 90  LYS A CG  1 
ATOM   682  C CD  . LYS A 1 88  ? -31.29700 18.53300  -20.31500 1.000 43.65000 ? 90  LYS A CD  1 
ATOM   683  C CE  . LYS A 1 88  ? -31.75800 19.42900  -21.46500 1.000 50.86000 ? 90  LYS A CE  1 
ATOM   684  N NZ  . LYS A 1 88  ? -30.61400 19.85200  -22.34100 1.000 55.70000 ? 90  LYS A NZ  1 
ATOM   685  N N   . VAL A 1 89  ? -31.58000 15.19700  -17.19400 1.000 31.33000 ? 91  VAL A N   1 
ATOM   686  C CA  . VAL A 1 89  ? -31.96500 14.70900  -15.87600 1.000 31.14000 ? 91  VAL A CA  1 
ATOM   687  C C   . VAL A 1 89  ? -32.32900 15.88000  -14.96800 1.000 34.39000 ? 91  VAL A C   1 
ATOM   688  O O   . VAL A 1 89  ? -32.01900 17.04400  -15.23800 1.000 34.01000 ? 91  VAL A O   1 
ATOM   689  C CB  . VAL A 1 89  ? -30.89300 13.82400  -15.20900 1.000 33.60000 ? 91  VAL A CB  1 
ATOM   690  C CG1 . VAL A 1 89  ? -30.83200 12.44800  -15.89900 1.000 33.44000 ? 91  VAL A CG1 1 
ATOM   691  C CG2 . VAL A 1 89  ? -29.52500 14.51900  -15.19100 1.000 34.41000 ? 91  VAL A CG2 1 
ATOM   692  N N   . ASP A 1 90  ? -33.01400 15.53600  -13.87300 1.000 35.65000 ? 92  ASP A N   1 
ATOM   693  C CA  . ASP A 1 90  ? -33.59800 16.50700  -12.95300 1.000 42.86000 ? 92  ASP A CA  1 
ATOM   694  C C   . ASP A 1 90  ? -32.56700 17.16700  -12.04900 1.000 40.98000 ? 92  ASP A C   1 
ATOM   695  O O   . ASP A 1 90  ? -32.87800 18.18700  -11.42300 1.000 41.68000 ? 92  ASP A O   1 
ATOM   696  C CB  . ASP A 1 90  ? -34.68100 15.82900  -12.09400 1.000 40.81000 ? 92  ASP A CB  1 
ATOM   697  C CG  . ASP A 1 90  ? -34.13100 14.70600  -11.19100 1.000 44.59000 ? 92  ASP A CG  1 
ATOM   698  O OD1 . ASP A 1 90  ? -33.05500 14.12300  -11.47700 1.000 43.79000 ? 92  ASP A OD1 1 
ATOM   699  O OD2 . ASP A 1 90  ? -34.80400 14.38500  -10.18400 1.000 51.07000 ? 92  ASP A OD2 1 
ATOM   700  N N   . THR A 1 91  ? -31.35600 16.61600  -11.97100 1.000 38.57000 ? 93  THR A N   1 
ATOM   701  C CA  . THR A 1 91  ? -30.31900 17.08600  -11.06300 1.000 33.69000 ? 93  THR A CA  1 
ATOM   702  C C   . THR A 1 91  ? -29.04100 17.30600  -11.85300 1.000 35.93000 ? 93  THR A C   1 
ATOM   703  O O   . THR A 1 91  ? -28.62100 16.42300  -12.60400 1.000 35.51000 ? 93  THR A O   1 
ATOM   704  C CB  . THR A 1 91  ? -30.05600 16.06400  -9.94500  1.000 37.94000 ? 93  THR A CB  1 
ATOM   705  O OG1 . THR A 1 91  ? -31.29800 15.60700  -9.40000  1.000 41.30000 ? 93  THR A OG1 1 
ATOM   706  C CG2 . THR A 1 91  ? -29.19100 16.66600  -8.83000  1.000 34.63000 ? 93  THR A CG2 1 
ATOM   707  N N   . ALA A 1 92  ? -28.43400 18.47400  -11.69800 1.000 32.24000 ? 94  ALA A N   1 
ATOM   708  C CA  . ALA A 1 92  ? -27.09600 18.66900  -12.23000 1.000 32.85000 ? 94  ALA A CA  1 
ATOM   709  C C   . ALA A 1 92  ? -26.10100 17.90400  -11.36700 1.000 30.99000 ? 94  ALA A C   1 
ATOM   710  O O   . ALA A 1 92  ? -26.27800 17.77900  -10.15400 1.000 31.32000 ? 94  ALA A O   1 
ATOM   711  C CB  . ALA A 1 92  ? -26.74300 20.15100  -12.26400 1.000 37.70000 ? 94  ALA A CB  1 
ATOM   712  N N   . ASN A 1 93  ? -25.07000 17.36200  -12.00200 1.000 31.37000 ? 95  ASN A N   1 
ATOM   713  C CA  . ASN A 1 93  ? -24.02000 16.67200  -11.25800 1.000 31.79000 ? 95  ASN A CA  1 
ATOM   714  C C   . ASN A 1 93  ? -23.26100 17.69800  -10.43800 1.000 27.84000 ? 95  ASN A C   1 
ATOM   715  O O   . ASN A 1 93  ? -22.61000 18.57100  -11.01700 1.000 30.44000 ? 95  ASN A O   1 
ATOM   716  C CB  . ASN A 1 93  ? -23.08700 15.94200  -12.21400 1.000 28.70000 ? 95  ASN A CB  1 
ATOM   717  C CG  . ASN A 1 93  ? -21.94400 15.20000  -11.50100 1.000 31.93000 ? 95  ASN A CG  1 
ATOM   718  O OD1 . ASN A 1 93  ? -21.79600 15.24700  -10.28000 1.000 32.14000 ? 95  ASN A OD1 1 
ATOM   719  N ND2 . ASN A 1 93  ? -21.13800 14.50300  -12.28300 1.000 30.65000 ? 95  ASN A ND2 1 
ATOM   720  N N   . PRO A 1 94  ? -23.30700 17.63200  -9.10300  1.000 28.86000 ? 96  PRO A N   1 
ATOM   721  C CA  . PRO A 1 94  ? -22.60200 18.62800  -8.28600  1.000 27.97000 ? 96  PRO A CA  1 
ATOM   722  C C   . PRO A 1 94  ? -21.09700 18.51800  -8.37400  1.000 31.70000 ? 96  PRO A C   1 
ATOM   723  O O   . PRO A 1 94  ? -20.39800 19.42800  -7.91600  1.000 32.13000 ? 96  PRO A O   1 
ATOM   724  C CB  . PRO A 1 94  ? -23.07800 18.31200  -6.86800  1.000 29.87000 ? 96  PRO A CB  1 
ATOM   725  C CG  . PRO A 1 94  ? -23.32700 16.84200  -6.90200  1.000 34.65000 ? 96  PRO A CG  1 
ATOM   726  C CD  . PRO A 1 94  ? -23.87500 16.54600  -8.28200  1.000 29.94000 ? 96  PRO A CD  1 
ATOM   727  N N   . LYS A 1 95  ? -20.58100 17.43300  -8.94300  1.000 31.15000 ? 97  LYS A N   1 
ATOM   728  C CA  . LYS A 1 95  ? -19.15000 17.21900  -9.07200  1.000 29.68000 ? 97  LYS A CA  1 
ATOM   729  C C   . LYS A 1 95  ? -18.69300 17.30900  -10.52500 1.000 33.89000 ? 97  LYS A C   1 
ATOM   730  O O   . LYS A 1 95  ? -17.66200 16.73300  -10.88800 1.000 34.53000 ? 97  LYS A O   1 
ATOM   731  C CB  . LYS A 1 95  ? -18.78000 15.86800  -8.47000  1.000 34.50000 ? 97  LYS A CB  1 
ATOM   732  C CG  . LYS A 1 95  ? -18.83600 15.84500  -6.95700  1.000 34.94000 ? 97  LYS A CG  1 
ATOM   733  C CD  . LYS A 1 95  ? -18.65400 14.43700  -6.44000  1.000 33.69000 ? 97  LYS A CD  1 
ATOM   734  C CE  . LYS A 1 95  ? -18.29300 14.45400  -4.97500  1.000 41.74000 ? 97  LYS A CE  1 
ATOM   735  N NZ  . LYS A 1 95  ? -18.30800 13.06900  -4.41000  1.000 48.62000 ? 97  LYS A NZ  1 
ATOM   736  N N   . THR A 1 96  ? -19.44600 18.01500  -11.36300 1.000 31.55000 ? 98  THR A N   1 
ATOM   737  C CA  . THR A 1 96  ? -19.03000 18.22800  -12.73800 1.000 30.63000 ? 98  THR A CA  1 
ATOM   738  C C   . THR A 1 96  ? -17.68900 18.95700  -12.75300 1.000 30.92000 ? 98  THR A C   1 
ATOM   739  O O   . THR A 1 96  ? -17.56200 20.01700  -12.12800 1.000 30.62000 ? 98  THR A O   1 
ATOM   740  C CB  . THR A 1 96  ? -20.08600 19.04000  -13.49600 1.000 28.00000 ? 98  THR A CB  1 
ATOM   741  O OG1 . THR A 1 96  ? -21.30000 18.29200  -13.55600 1.000 29.85000 ? 98  THR A OG1 1 
ATOM   742  C CG2 . THR A 1 96  ? -19.62700 19.33600  -14.92600 1.000 29.17000 ? 98  THR A CG2 1 
ATOM   743  N N   . PRO A 1 97  ? -16.67300 18.42700  -13.42300 1.000 29.18000 ? 99  PRO A N   1 
ATOM   744  C CA  . PRO A 1 97  ? -15.39700 19.13900  -13.51900 1.000 30.60000 ? 99  PRO A CA  1 
ATOM   745  C C   . PRO A 1 97  ? -15.44300 20.20000  -14.61000 1.000 30.74000 ? 99  PRO A C   1 
ATOM   746  O O   . PRO A 1 97  ? -16.34500 20.23900  -15.44400 1.000 29.21000 ? 99  PRO A O   1 
ATOM   747  C CB  . PRO A 1 97  ? -14.39900 18.03100  -13.87700 1.000 30.53000 ? 99  PRO A CB  1 
ATOM   748  C CG  . PRO A 1 97  ? -15.22400 17.06200  -14.66300 1.000 28.72000 ? 99  PRO A CG  1 
ATOM   749  C CD  . PRO A 1 97  ? -16.60700 17.08800  -14.03500 1.000 31.20000 ? 99  PRO A CD  1 
ATOM   750  N N   . LYS A 1 98  ? -14.44800 21.08300  -14.58900 1.000 30.62000 ? 100 LYS A N   1 
ATOM   751  C CA  . LYS A 1 98  ? -14.18800 21.86700  -15.79000 1.000 32.32000 ? 100 LYS A CA  1 
ATOM   752  C C   . LYS A 1 98  ? -13.89600 20.88300  -16.91000 1.000 34.43000 ? 100 LYS A C   1 
ATOM   753  O O   . LYS A 1 98  ? -13.07600 19.97700  -16.74000 1.000 32.07000 ? 100 LYS A O   1 
ATOM   754  C CB  . LYS A 1 98  ? -13.00100 22.81300  -15.57900 1.000 35.50000 ? 100 LYS A CB  1 
ATOM   755  N N   . TYR A 1 99  ? -14.59700 21.01000  -18.03500 1.000 30.07000 ? 101 TYR A N   1 
ATOM   756  C CA  . TYR A 1 99  ? -14.41200 20.02500  -19.09300 1.000 33.78000 ? 101 TYR A CA  1 
ATOM   757  C C   . TYR A 1 99  ? -14.62900 20.65700  -20.45900 1.000 36.83000 ? 101 TYR A C   1 
ATOM   758  O O   . TYR A 1 99  ? -15.19900 21.74400  -20.58800 1.000 34.98000 ? 101 TYR A O   1 
ATOM   759  C CB  . TYR A 1 99  ? -15.35200 18.82000  -18.92300 1.000 28.17000 ? 101 TYR A CB  1 
ATOM   760  C CG  . TYR A 1 99  ? -16.78500 19.11500  -19.34400 1.000 29.58000 ? 101 TYR A CG  1 
ATOM   761  C CD1 . TYR A 1 99  ? -17.70200 19.62900  -18.43500 1.000 31.65000 ? 101 TYR A CD1 1 
ATOM   762  C CD2 . TYR A 1 99  ? -17.19600 18.91700  -20.65800 1.000 29.47000 ? 101 TYR A CD2 1 
ATOM   763  C CE1 . TYR A 1 99  ? -19.00700 19.92600  -18.81900 1.000 33.22000 ? 101 TYR A CE1 1 
ATOM   764  C CE2 . TYR A 1 99  ? -18.48400 19.22000  -21.05500 1.000 29.17000 ? 101 TYR A CE2 1 
ATOM   765  C CZ  . TYR A 1 99  ? -19.38600 19.71500  -20.13500 1.000 31.30000 ? 101 TYR A CZ  1 
ATOM   766  O OH  . TYR A 1 99  ? -20.67000 20.00200  -20.54800 1.000 34.53000 ? 101 TYR A OH  1 
ATOM   767  N N   . LYS A 1 100 ? -14.17000 19.93500  -21.48300 1.000 30.96000 ? 102 LYS A N   1 
ATOM   768  C CA  . LYS A 1 100 ? -14.41900 20.24700  -22.88000 1.000 32.08000 ? 102 LYS A CA  1 
ATOM   769  C C   . LYS A 1 100 ? -14.51300 18.93500  -23.65500 1.000 33.42000 ? 102 LYS A C   1 
ATOM   770  O O   . LYS A 1 100 ? -14.01900 17.88900  -23.21500 1.000 30.74000 ? 102 LYS A O   1 
ATOM   771  C CB  . LYS A 1 100 ? -13.31400 21.14500  -23.46700 1.000 32.87000 ? 102 LYS A CB  1 
ATOM   772  C CG  . LYS A 1 100 ? -11.95000 20.48100  -23.50300 1.000 37.51000 ? 102 LYS A CG  1 
ATOM   773  C CD  . LYS A 1 100 ? -10.85400 21.33800  -24.16800 1.000 41.00000 ? 102 LYS A CD  1 
ATOM   774  C CE  . LYS A 1 100 ? -10.70500 22.70300  -23.51700 1.000 41.54000 ? 102 LYS A CE  1 
ATOM   775  N NZ  . LYS A 1 100 ? -9.27200  23.13700  -23.52900 1.000 52.53000 ? 102 LYS A NZ  1 
ATOM   776  N N   . PHE A 1 101 ? -15.16700 19.00200  -24.81200 1.000 28.64000 ? 103 PHE A N   1 
ATOM   777  C CA  . PHE A 1 101 ? -15.25500 17.89200  -25.75100 1.000 28.28000 ? 103 PHE A CA  1 
ATOM   778  C C   . PHE A 1 101 ? -14.28300 18.16900  -26.89100 1.000 31.66000 ? 103 PHE A C   1 
ATOM   779  O O   . PHE A 1 101 ? -14.30300 19.26100  -27.46800 1.000 32.52000 ? 103 PHE A O   1 
ATOM   780  C CB  . PHE A 1 101 ? -16.67400 17.74000  -26.31800 1.000 28.10000 ? 103 PHE A CB  1 
ATOM   781  C CG  . PHE A 1 101 ? -17.71000 17.28600  -25.32000 1.000 27.66000 ? 103 PHE A CG  1 
ATOM   782  C CD1 . PHE A 1 101 ? -17.34800 16.76500  -24.08700 1.000 27.64000 ? 103 PHE A CD1 1 
ATOM   783  C CD2 . PHE A 1 101 ? -19.06300 17.37300  -25.63700 1.000 29.69000 ? 103 PHE A CD2 1 
ATOM   784  C CE1 . PHE A 1 101 ? -18.31400 16.34800  -23.18600 1.000 28.56000 ? 103 PHE A CE1 1 
ATOM   785  C CE2 . PHE A 1 101 ? -20.03200 16.95500  -24.74000 1.000 29.17000 ? 103 PHE A CE2 1 
ATOM   786  C CZ  . PHE A 1 101 ? -19.65300 16.44400  -23.51000 1.000 28.78000 ? 103 PHE A CZ  1 
ATOM   787  N N   . VAL A 1 102 ? -13.42600 17.20200  -27.21200 1.000 27.44000 ? 104 VAL A N   1 
ATOM   788  C CA  . VAL A 1 102 ? -12.45100 17.38900  -28.28400 1.000 28.60000 ? 104 VAL A CA  1 
ATOM   789  C C   . VAL A 1 102 ? -12.43000 16.13800  -29.15500 1.000 30.76000 ? 104 VAL A C   1 
ATOM   790  O O   . VAL A 1 102 ? -12.43700 15.01600  -28.64300 1.000 32.29000 ? 104 VAL A O   1 
ATOM   791  C CB  . VAL A 1 102 ? -11.04100 17.69800  -27.72100 1.000 31.38000 ? 104 VAL A CB  1 
ATOM   792  C CG1 . VAL A 1 102 ? -10.58700 16.60400  -26.75500 1.000 31.58000 ? 104 VAL A CG1 1 
ATOM   793  C CG2 . VAL A 1 102 ? -10.03000 17.84700  -28.85200 1.000 34.90000 ? 104 VAL A CG2 1 
ATOM   794  N N   . ARG A 1 103 ? -12.40500 16.32500  -30.47300 1.000 28.24000 ? 105 ARG A N   1 
ATOM   795  C CA  . ARG A 1 103 ? -12.19700 15.21500  -31.39300 1.000 25.50000 ? 105 ARG A CA  1 
ATOM   796  C C   . ARG A 1 103 ? -10.70900 15.11400  -31.68200 1.000 26.76000 ? 105 ARG A C   1 
ATOM   797  O O   . ARG A 1 103 ? -10.07900 16.11500  -32.02600 1.000 28.64000 ? 105 ARG A O   1 
ATOM   798  C CB  . ARG A 1 103 ? -12.97300 15.40900  -32.69600 1.000 28.62000 ? 105 ARG A CB  1 
ATOM   799  C CG  . ARG A 1 103 ? -12.81800 14.24700  -33.66600 1.000 25.88000 ? 105 ARG A CG  1 
ATOM   800  C CD  . ARG A 1 103 ? -13.83100 14.30500  -34.78200 1.000 31.92000 ? 105 ARG A CD  1 
ATOM   801  N NE  . ARG A 1 103 ? -13.67700 13.19900  -35.72500 1.000 31.62000 ? 105 ARG A NE  1 
ATOM   802  C CZ  . ARG A 1 103 ? -14.36400 12.06000  -35.64900 1.000 29.41000 ? 105 ARG A CZ  1 
ATOM   803  N NH1 . ARG A 1 103 ? -15.20900 11.87100  -34.64900 1.000 27.46000 ? 105 ARG A NH1 1 
ATOM   804  N NH2 . ARG A 1 103 ? -14.18300 11.10300  -36.55100 1.000 30.07000 ? 105 ARG A NH2 1 
ATOM   805  N N   . ILE A 1 104 ? -10.14800 13.91900  -31.52400 1.000 25.92000 ? 106 ILE A N   1 
ATOM   806  C CA  . ILE A 1 104 ? -8.71500  13.72900  -31.65200 1.000 28.14000 ? 106 ILE A CA  1 
ATOM   807  C C   . ILE A 1 104 ? -8.38700  13.11500  -33.00600 1.000 29.35000 ? 106 ILE A C   1 
ATOM   808  O O   . ILE A 1 104 ? -9.24900  12.60300  -33.71900 1.000 27.30000 ? 106 ILE A O   1 
ATOM   809  C CB  . ILE A 1 104 ? -8.15700  12.86400  -30.50100 1.000 27.03000 ? 106 ILE A CB  1 
ATOM   810  C CG1 . ILE A 1 104 ? -8.80200  11.47100  -30.50600 1.000 27.09000 ? 106 ILE A CG1 1 
ATOM   811  C CG2 . ILE A 1 104 ? -8.37200  13.56700  -29.17900 1.000 25.48000 ? 106 ILE A CG2 1 
ATOM   812  C CD1 . ILE A 1 104 ? -8.05200  10.42400  -29.67400 1.000 28.49000 ? 106 ILE A CD1 1 
ATOM   813  N N   . GLN A 1 105 ? -7.11000  13.17400  -33.37300 1.000 28.26000 ? 107 GLN A N   1 
ATOM   814  C CA  . GLN A 1 105 ? -6.63100  12.55000  -34.59900 1.000 26.66000 ? 107 GLN A CA  1 
ATOM   815  C C   . GLN A 1 105 ? -5.87800  11.25800  -34.28600 1.000 28.89000 ? 107 GLN A C   1 
ATOM   816  O O   . GLN A 1 105 ? -5.41900  11.05600  -33.15800 1.000 27.33000 ? 107 GLN A O   1 
ATOM   817  C CB  . GLN A 1 105 ? -5.71800  13.52600  -35.35100 1.000 34.25000 ? 107 GLN A CB  1 
ATOM   818  C CG  . GLN A 1 105 ? -6.44200  14.78900  -35.76700 1.000 34.61000 ? 107 GLN A CG  1 
ATOM   819  C CD  . GLN A 1 105 ? -7.53700  14.51100  -36.76400 1.000 41.69000 ? 107 GLN A CD  1 
ATOM   820  O OE1 . GLN A 1 105 ? -7.31500  13.82500  -37.76200 1.000 45.01000 ? 107 GLN A OE1 1 
ATOM   821  N NE2 . GLN A 1 105 ? -8.73200  15.03200  -36.50100 1.000 39.25000 ? 107 GLN A NE2 1 
ATOM   822  N N   . PRO A 1 106 ? -5.77600  10.34200  -35.25400 1.000 28.59000 ? 108 PRO A N   1 
ATOM   823  C CA  . PRO A 1 106 ? -4.95300  9.13600   -35.06400 1.000 29.46000 ? 108 PRO A CA  1 
ATOM   824  C C   . PRO A 1 106 ? -3.55200  9.47400   -34.59300 1.000 28.89000 ? 108 PRO A C   1 
ATOM   825  O O   . PRO A 1 106 ? -2.93600  10.43200  -35.05700 1.000 28.17000 ? 108 PRO A O   1 
ATOM   826  C CB  . PRO A 1 106 ? -4.91900  8.50700   -36.45900 1.000 30.13000 ? 108 PRO A CB  1 
ATOM   827  C CG  . PRO A 1 106 ? -6.15100  8.97400   -37.10900 1.000 33.06000 ? 108 PRO A CG  1 
ATOM   828  C CD  . PRO A 1 106 ? -6.46000  10.34100  -36.55700 1.000 31.89000 ? 108 PRO A CD  1 
ATOM   829  N N   . GLY A 1 107 ? -3.03500  8.65400   -33.67700 1.000 27.79000 ? 109 GLY A N   1 
ATOM   830  C CA  . GLY A 1 107 ? -1.75500  8.87600   -33.05100 1.000 28.06000 ? 109 GLY A CA  1 
ATOM   831  C C   . GLY A 1 107 ? -1.86100  9.50800   -31.68100 1.000 29.73000 ? 109 GLY A C   1 
ATOM   832  O O   . GLY A 1 107 ? -0.95900  9.33400   -30.85100 1.000 26.38000 ? 109 GLY A O   1 
ATOM   833  N N   . GLN A 1 108 ? -2.95300  10.22300  -31.42500 1.000 24.85000 ? 110 GLN A N   1 
ATOM   834  C CA  . GLN A 1 108 ? -3.18900  10.84000  -30.13000 1.000 25.60000 ? 110 GLN A CA  1 
ATOM   835  C C   . GLN A 1 108 ? -3.48000  9.77800   -29.07400 1.000 22.39000 ? 110 GLN A C   1 
ATOM   836  O O   . GLN A 1 108 ? -4.06200  8.72800   -29.35900 1.000 24.44000 ? 110 GLN A O   1 
ATOM   837  C CB  . GLN A 1 108 ? -4.36500  11.81700  -30.22500 1.000 26.70000 ? 110 GLN A CB  1 
ATOM   838  C CG  . GLN A 1 108 ? -4.60000  12.65100  -28.98000 1.000 28.36000 ? 110 GLN A CG  1 
ATOM   839  C CD  . GLN A 1 108 ? -3.44400  13.55400  -28.64600 1.000 32.18000 ? 110 GLN A CD  1 
ATOM   840  O OE1 . GLN A 1 108 ? -2.55800  13.19100  -27.85400 1.000 31.48000 ? 110 GLN A OE1 1 
ATOM   841  N NE2 . GLN A 1 108 ? -3.43100  14.74500  -29.25300 1.000 31.03000 ? 110 GLN A NE2 1 
ATOM   842  N N   . THR A 1 109 ? -3.06400  10.06500  -27.85000 1.000 23.78000 ? 111 THR A N   1 
ATOM   843  C CA  . THR A 1 109 ? -3.24500  9.19000   -26.70600 1.000 24.66000 ? 111 THR A CA  1 
ATOM   844  C C   . THR A 1 109 ? -4.25400  9.78900   -25.73600 1.000 24.98000 ? 111 THR A C   1 
ATOM   845  O O   . THR A 1 109 ? -4.58200  10.97900  -25.79000 1.000 26.74000 ? 111 THR A O   1 
ATOM   846  C CB  . THR A 1 109 ? -1.90800  8.95200   -25.98700 1.000 28.67000 ? 111 THR A CB  1 
ATOM   847  O OG1 . THR A 1 109 ? -1.33700  10.20600  -25.58600 1.000 27.15000 ? 111 THR A OG1 1 
ATOM   848  C CG2 . THR A 1 109 ? -0.95100  8.20900   -26.90500 1.000 26.42000 ? 111 THR A CG2 1 
ATOM   849  N N   . PHE A 1 110 ? -4.73500  8.95000   -24.82800 1.000 24.73000 ? 112 PHE A N   1 
ATOM   850  C CA  . PHE A 1 110 ? -5.68400  9.38500   -23.81800 1.000 26.50000 ? 112 PHE A CA  1 
ATOM   851  C C   . PHE A 1 110 ? -5.78500  8.28500   -22.77300 1.000 24.56000 ? 112 PHE A C   1 
ATOM   852  O O   . PHE A 1 110 ? -5.36700  7.14300   -23.00200 1.000 25.51000 ? 112 PHE A O   1 
ATOM   853  C CB  . PHE A 1 110 ? -7.06100  9.70700   -24.43000 1.000 23.48000 ? 112 PHE A CB  1 
ATOM   854  C CG  . PHE A 1 110 ? -7.59700  8.62300   -25.31900 1.000 24.63000 ? 112 PHE A CG  1 
ATOM   855  C CD1 . PHE A 1 110 ? -7.24800  8.56700   -26.66600 1.000 25.23000 ? 112 PHE A CD1 1 
ATOM   856  C CD2 . PHE A 1 110 ? -8.44800  7.66000   -24.81000 1.000 25.08000 ? 112 PHE A CD2 1 
ATOM   857  C CE1 . PHE A 1 110 ? -7.73900  7.56500   -27.48500 1.000 29.83000 ? 112 PHE A CE1 1 
ATOM   858  C CE2 . PHE A 1 110 ? -8.96000  6.66100   -25.62400 1.000 25.74000 ? 112 PHE A CE2 1 
ATOM   859  C CZ  . PHE A 1 110 ? -8.61600  6.61200   -26.96000 1.000 30.37000 ? 112 PHE A CZ  1 
ATOM   860  N N   . SER A 1 111 ? -6.29500  8.65400   -21.61000 1.000 22.40000 ? 113 SER A N   1 
ATOM   861  C CA  . SER A 1 111 ? -6.60700  7.68700   -20.56800 1.000 23.05000 ? 113 SER A CA  1 
ATOM   862  C C   . SER A 1 111 ? -8.03400  7.17600   -20.73600 1.000 23.28000 ? 113 SER A C   1 
ATOM   863  O O   . SER A 1 111 ? -8.93200  7.92700   -21.12100 1.000 25.46000 ? 113 SER A O   1 
ATOM   864  C CB  . SER A 1 111 ? -6.45300  8.31200   -19.18400 1.000 25.95000 ? 113 SER A CB  1 
ATOM   865  O OG  . SER A 1 111 ? -5.17200  8.86600   -19.03300 1.000 26.71000 ? 113 SER A OG  1 
ATOM   866  N N   . VAL A 1 112 ? -8.24000  5.90200   -20.41300 1.000 21.86000 ? 114 VAL A N   1 
ATOM   867  C CA  . VAL A 1 112 ? -9.55800  5.27800   -20.45500 1.000 21.13000 ? 114 VAL A CA  1 
ATOM   868  C C   . VAL A 1 112 ? -9.91200  4.85600   -19.03900 1.000 24.44000 ? 114 VAL A C   1 
ATOM   869  O O   . VAL A 1 112 ? -9.10200  4.22700   -18.35000 1.000 23.48000 ? 114 VAL A O   1 
ATOM   870  C CB  . VAL A 1 112 ? -9.58800  4.07200   -21.41000 1.000 24.50000 ? 114 VAL A CB  1 
ATOM   871  C CG1 . VAL A 1 112 ? -10.89900 3.27900   -21.23900 1.000 27.14000 ? 114 VAL A CG1 1 
ATOM   872  C CG2 . VAL A 1 112 ? -9.40000  4.53300   -22.84900 1.000 25.41000 ? 114 VAL A CG2 1 
ATOM   873  N N   . LEU A 1 113 ? -11.10500 5.21200   -18.59600 1.000 23.87000 ? 115 LEU A N   1 
ATOM   874  C CA  . LEU A 1 113 ? -11.62800 4.70600   -17.33300 1.000 25.84000 ? 115 LEU A CA  1 
ATOM   875  C C   . LEU A 1 113 ? -12.64600 3.61900   -17.68300 1.000 25.79000 ? 115 LEU A C   1 
ATOM   876  O O   . LEU A 1 113 ? -13.77700 3.91400   -18.07200 1.000 25.71000 ? 115 LEU A O   1 
ATOM   877  C CB  . LEU A 1 113 ? -12.24000 5.83300   -16.50500 1.000 25.70000 ? 115 LEU A CB  1 
ATOM   878  C CG  . LEU A 1 113 ? -12.83600 5.47200   -15.14100 1.000 26.17000 ? 115 LEU A CG  1 
ATOM   879  C CD1 . LEU A 1 113 ? -11.75900 5.04200   -14.14800 1.000 25.80000 ? 115 LEU A CD1 1 
ATOM   880  C CD2 . LEU A 1 113 ? -13.63400 6.65700   -14.60200 1.000 27.05000 ? 115 LEU A CD2 1 
ATOM   881  N N   . ALA A 1 114 ? -12.23100 2.35500   -17.58300 1.000 23.05000 ? 116 ALA A N   1 
ATOM   882  C CA  . ALA A 1 114 ? -13.14400 1.25600   -17.87100 1.000 24.09000 ? 116 ALA A CA  1 
ATOM   883  C C   . ALA A 1 114 ? -14.16400 1.12800   -16.74200 1.000 26.75000 ? 116 ALA A C   1 
ATOM   884  O O   . ALA A 1 114 ? -13.80000 1.08600   -15.56200 1.000 27.05000 ? 116 ALA A O   1 
ATOM   885  C CB  . ALA A 1 114 ? -12.37600 -0.05700  -18.05400 1.000 27.98000 ? 116 ALA A CB  1 
ATOM   886  N N   . CYS A 1 115 ? -15.44500 1.07200   -17.11200 1.000 25.44000 ? 117 CYS A N   1 
ATOM   887  C CA  . CYS A 1 115 ? -16.54300 1.01100   -16.16000 1.000 26.44000 ? 117 CYS A CA  1 
ATOM   888  C C   . CYS A 1 115 ? -17.53900 -0.06400  -16.56800 1.000 25.95000 ? 117 CYS A C   1 
ATOM   889  O O   . CYS A 1 115 ? -17.71900 -0.35900  -17.75700 1.000 24.69000 ? 117 CYS A O   1 
ATOM   890  C CB  . CYS A 1 115 ? -17.28600 2.34900   -16.06300 1.000 29.20000 ? 117 CYS A CB  1 
ATOM   891  S SG  . CYS A 1 115 ? -16.25800 3.72800   -15.60900 1.000 32.71000 ? 117 CYS A SG  1 
ATOM   892  N N   . TYR A 1 116 ? -18.20900 -0.62500  -15.56100 1.000 29.49000 ? 118 TYR A N   1 
ATOM   893  C CA  . TYR A 1 116 ? -19.26100 -1.61100  -15.76600 1.000 28.75000 ? 118 TYR A CA  1 
ATOM   894  C C   . TYR A 1 116 ? -20.38400 -1.28300  -14.80100 1.000 28.82000 ? 118 TYR A C   1 
ATOM   895  O O   . TYR A 1 116 ? -20.13800 -1.07000  -13.61000 1.000 29.74000 ? 118 TYR A O   1 
ATOM   896  C CB  . TYR A 1 116 ? -18.72700 -3.04400  -15.55900 1.000 29.01000 ? 118 TYR A CB  1 
ATOM   897  C CG  . TYR A 1 116 ? -17.61500 -3.34500  -16.54800 1.000 31.16000 ? 118 TYR A CG  1 
ATOM   898  C CD1 . TYR A 1 116 ? -17.91100 -3.83200  -17.81900 1.000 29.16000 ? 118 TYR A CD1 1 
ATOM   899  C CD2 . TYR A 1 116 ? -16.28200 -3.07400  -16.24000 1.000 29.22000 ? 118 TYR A CD2 1 
ATOM   900  C CE1 . TYR A 1 116 ? -16.91500 -4.06300  -18.74000 1.000 28.41000 ? 118 TYR A CE1 1 
ATOM   901  C CE2 . TYR A 1 116 ? -15.27700 -3.30400  -17.15600 1.000 31.92000 ? 118 TYR A CE2 1 
ATOM   902  C CZ  . TYR A 1 116 ? -15.60200 -3.80000  -18.40600 1.000 29.45000 ? 118 TYR A CZ  1 
ATOM   903  O OH  . TYR A 1 116 ? -14.62500 -4.03300  -19.33900 1.000 28.24000 ? 118 TYR A OH  1 
ATOM   904  N N   . ASN A 1 117 ? -21.60400 -1.18700  -15.32600 1.000 33.33000 ? 119 ASN A N   1 
ATOM   905  C CA  . ASN A 1 117 ? -22.77800 -0.88800  -14.50300 1.000 32.38000 ? 119 ASN A CA  1 
ATOM   906  C C   . ASN A 1 117 ? -22.62000 0.45400   -13.78800 1.000 32.23000 ? 119 ASN A C   1 
ATOM   907  O O   . ASN A 1 117 ? -23.03300 0.62700   -12.64000 1.000 32.98000 ? 119 ASN A O   1 
ATOM   908  C CB  . ASN A 1 117 ? -23.04200 -2.02200  -13.51200 1.000 33.71000 ? 119 ASN A CB  1 
ATOM   909  C CG  . ASN A 1 117 ? -23.19500 -3.35900  -14.20800 1.000 38.88000 ? 119 ASN A CG  1 
ATOM   910  O OD1 . ASN A 1 117 ? -24.11100 -3.54500  -15.00600 1.000 40.81000 ? 119 ASN A OD1 1 
ATOM   911  N ND2 . ASN A 1 117 ? -22.29900 -4.29200  -13.91900 1.000 40.85000 ? 119 ASN A ND2 1 
ATOM   912  N N   . GLY A 1 118 ? -21.99500 1.41000   -14.47000 1.000 28.76000 ? 120 GLY A N   1 
ATOM   913  C CA  . GLY A 1 118 ? -21.79900 2.72400   -13.90300 1.000 27.04000 ? 120 GLY A CA  1 
ATOM   914  C C   . GLY A 1 118 ? -20.71800 2.83400   -12.84700 1.000 30.85000 ? 120 GLY A C   1 
ATOM   915  O O   . GLY A 1 118 ? -20.57800 3.90500   -12.24600 1.000 32.19000 ? 120 GLY A O   1 
ATOM   916  N N   . SER A 1 119 ? -19.95500 1.76900   -12.59100 1.000 29.33000 ? 121 SER A N   1 
ATOM   917  C CA  . SER A 1 119 ? -18.91500 1.82800   -11.57200 1.000 30.51000 ? 121 SER A CA  1 
ATOM   918  C C   . SER A 1 119 ? -17.54200 1.61000   -12.19900 1.000 32.00000 ? 121 SER A C   1 
ATOM   919  O O   . SER A 1 119 ? -17.35300 0.65900   -12.97100 1.000 29.19000 ? 121 SER A O   1 
ATOM   920  C CB  . SER A 1 119 ? -19.16600 0.80100   -10.45500 1.000 34.06000 ? 121 SER A CB  1 
ATOM   921  O OG  . SER A 1 119 ? -18.79100 -0.49900  -10.85900 1.000 40.80000 ? 121 SER A OG  1 
ATOM   922  N N   . PRO A 1 120 ? -16.57100 2.46900   -11.90300 1.000 29.48000 ? 122 PRO A N   1 
ATOM   923  C CA  . PRO A 1 120 ? -15.26200 2.36600   -12.55700 1.000 32.56000 ? 122 PRO A CA  1 
ATOM   924  C C   . PRO A 1 120 ? -14.48700 1.13300   -12.11800 1.000 29.59000 ? 122 PRO A C   1 
ATOM   925  O O   . PRO A 1 120 ? -14.47000 0.76500   -10.94000 1.000 33.22000 ? 122 PRO A O   1 
ATOM   926  C CB  . PRO A 1 120 ? -14.55300 3.65700   -12.13100 1.000 30.44000 ? 122 PRO A CB  1 
ATOM   927  C CG  . PRO A 1 120 ? -15.24600 4.09600   -10.90600 1.000 36.43000 ? 122 PRO A CG  1 
ATOM   928  C CD  . PRO A 1 120 ? -16.67600 3.66300   -11.04500 1.000 32.79000 ? 122 PRO A CD  1 
ATOM   929  N N   . SER A 1 121 ? -13.84200 0.49200   -13.09000 1.000 27.66000 ? 123 SER A N   1 
ATOM   930  C CA  . SER A 1 121 ? -13.10000 -0.74300  -12.87700 1.000 28.25000 ? 123 SER A CA  1 
ATOM   931  C C   . SER A 1 121 ? -11.58800 -0.54700  -12.88700 1.000 28.22000 ? 123 SER A C   1 
ATOM   932  O O   . SER A 1 121 ? -10.88100 -1.08900  -12.02500 1.000 30.29000 ? 123 SER A O   1 
ATOM   933  C CB  . SER A 1 121 ? -13.49900 -1.76100  -13.94800 1.000 26.68000 ? 123 SER A CB  1 
ATOM   934  O OG  . SER A 1 121 ? -12.71600 -2.93300  -13.83300 1.000 40.95000 ? 123 SER A OG  1 
ATOM   935  N N   . GLY A 1 122 ? -11.06300 0.20900   -13.84600 1.000 27.20000 ? 124 GLY A N   1 
ATOM   936  C CA  . GLY A 1 122 ? -9.62900  0.45300   -13.90400 1.000 28.07000 ? 124 GLY A CA  1 
ATOM   937  C C   . GLY A 1 122 ? -9.33600  1.59600   -14.84900 1.000 27.45000 ? 124 GLY A C   1 
ATOM   938  O O   . GLY A 1 122 ? -10.21400 2.08300   -15.56600 1.000 25.07000 ? 124 GLY A O   1 
ATOM   939  N N   . VAL A 1 123 ? -8.07700  2.02000   -14.85400 1.000 23.63000 ? 125 VAL A N   1 
ATOM   940  C CA  . VAL A 1 123 ? -7.66200  3.12600   -15.70100 1.000 25.16000 ? 125 VAL A CA  1 
ATOM   941  C C   . VAL A 1 123 ? -6.40200  2.70200   -16.43700 1.000 29.43000 ? 125 VAL A C   1 
ATOM   942  O O   . VAL A 1 123 ? -5.52000  2.05400   -15.86300 1.000 25.54000 ? 125 VAL A O   1 
ATOM   943  C CB  . VAL A 1 123 ? -7.45100  4.42900   -14.88600 1.000 28.57000 ? 125 VAL A CB  1 
ATOM   944  C CG1 . VAL A 1 123 ? -6.22200  4.33800   -14.01100 1.000 31.46000 ? 125 VAL A CG1 1 
ATOM   945  C CG2 . VAL A 1 123 ? -7.34700  5.64000   -15.79300 1.000 29.08000 ? 125 VAL A CG2 1 
ATOM   946  N N   . TYR A 1 124 ? -6.35000  2.99700   -17.72900 1.000 24.78000 ? 126 TYR A N   1 
ATOM   947  C CA  . TYR A 1 124 ? -5.15000  2.68000   -18.47900 1.000 30.06000 ? 126 TYR A CA  1 
ATOM   948  C C   . TYR A 1 124 ? -5.01000  3.69300   -19.59400 1.000 28.45000 ? 126 TYR A C   1 
ATOM   949  O O   . TYR A 1 124 ? -5.94300  4.42300   -19.92700 1.000 25.53000 ? 126 TYR A O   1 
ATOM   950  C CB  . TYR A 1 124 ? -5.18000  1.24900   -19.03300 1.000 28.42000 ? 126 TYR A CB  1 
ATOM   951  C CG  . TYR A 1 124 ? -6.43500  0.91000   -19.81700 1.000 25.95000 ? 126 TYR A CG  1 
ATOM   952  C CD1 . TYR A 1 124 ? -6.49900  1.12900   -21.18900 1.000 30.60000 ? 126 TYR A CD1 1 
ATOM   953  C CD2 . TYR A 1 124 ? -7.54200  0.35900   -19.18600 1.000 30.20000 ? 126 TYR A CD2 1 
ATOM   954  C CE1 . TYR A 1 124 ? -7.63700  0.81800   -21.91200 1.000 32.28000 ? 126 TYR A CE1 1 
ATOM   955  C CE2 . TYR A 1 124 ? -8.69000  0.03600   -19.90200 1.000 31.72000 ? 126 TYR A CE2 1 
ATOM   956  C CZ  . TYR A 1 124 ? -8.72700  0.26900   -21.26400 1.000 32.32000 ? 126 TYR A CZ  1 
ATOM   957  O OH  . TYR A 1 124 ? -9.84800  -0.03700  -21.99400 1.000 36.38000 ? 126 TYR A OH  1 
ATOM   958  N N   . GLN A 1 125 ? -3.82500  3.73600   -20.15900 1.000 24.41000 ? 127 GLN A N   1 
ATOM   959  C CA  . GLN A 1 125 ? -3.51700  4.67000   -21.21800 1.000 28.34000 ? 127 GLN A CA  1 
ATOM   960  C C   . GLN A 1 125 ? -3.75700  3.99900   -22.56200 1.000 31.10000 ? 127 GLN A C   1 
ATOM   961  O O   . GLN A 1 125 ? -3.52700  2.79800   -22.72200 1.000 32.16000 ? 127 GLN A O   1 
ATOM   962  C CB  . GLN A 1 125 ? -2.07000  5.14100   -21.06300 1.000 30.23000 ? 127 GLN A CB  1 
ATOM   963  C CG  . GLN A 1 125 ? -1.69100  6.31300   -21.90600 1.000 34.70000 ? 127 GLN A CG  1 
ATOM   964  C CD  . GLN A 1 125 ? -2.29100  7.62700   -21.45400 1.000 30.18000 ? 127 GLN A CD  1 
ATOM   965  O OE1 . GLN A 1 125 ? -3.17500  7.69000   -20.57600 1.000 32.17000 ? 127 GLN A OE1 1 
ATOM   966  N NE2 . GLN A 1 125 ? -1.82800  8.70400   -22.08300 1.000 35.67000 ? 127 GLN A NE2 1 
ATOM   967  N N   . CYS A 1 126 ? -4.26500  4.76900   -23.51900 1.000 28.61000 ? 128 CYS A N   1 
ATOM   968  C CA  . CYS A 1 126 ? -4.68000  4.22500   -24.79500 1.000 31.33000 ? 128 CYS A CA  1 
ATOM   969  C C   . CYS A 1 126 ? -4.22000  5.16900   -25.89800 1.000 31.21000 ? 128 CYS A C   1 
ATOM   970  O O   . CYS A 1 126 ? -3.72100  6.26500   -25.63400 1.000 32.64000 ? 128 CYS A O   1 
ATOM   971  C CB  . CYS A 1 126 ? -6.20400  4.04100   -24.82300 1.000 29.35000 ? 128 CYS A CB  1 
ATOM   972  S SG  . CYS A 1 126 ? -6.67500  2.62400   -25.74500 1.000 45.14000 ? 128 CYS A SG  1 
ATOM   973  N N   . ALA A 1 127 ? -4.37300  4.73100   -27.14400 1.000 34.43000 ? 129 ALA A N   1 
ATOM   974  C CA  . ALA A 1 127 ? -4.08200  5.58300   -28.28700 1.000 31.40000 ? 129 ALA A CA  1 
ATOM   975  C C   . ALA A 1 127 ? -5.05500  5.27200   -29.40500 1.000 26.53000 ? 129 ALA A C   1 
ATOM   976  O O   . ALA A 1 127 ? -5.50200  4.13800   -29.56500 1.000 30.04000 ? 129 ALA A O   1 
ATOM   977  C CB  . ALA A 1 127 ? -2.66000  5.40700   -28.81400 1.000 28.61000 ? 129 ALA A CB  1 
ATOM   978  N N   . MET A 1 128 ? -5.33100  6.28500   -30.20400 1.000 26.32000 ? 130 MET A N   1 
ATOM   979  C CA  . MET A 1 128 ? -6.10800  6.11300   -31.41800 1.000 29.20000 ? 130 MET A CA  1 
ATOM   980  C C   . MET A 1 128 ? -5.19200  5.61000   -32.53100 1.000 29.01000 ? 130 MET A C   1 
ATOM   981  O O   . MET A 1 128 ? -4.25700  6.31300   -32.93000 1.000 27.28000 ? 130 MET A O   1 
ATOM   982  C CB  . MET A 1 128 ? -6.75700  7.43800   -31.79200 1.000 26.33000 ? 130 MET A CB  1 
ATOM   983  C CG  . MET A 1 128 ? -7.48500  7.42700   -33.10600 1.000 32.48000 ? 130 MET A CG  1 
ATOM   984  S SD  . MET A 1 128 ? -9.05100  6.62100   -32.91200 1.000 35.97000 ? 130 MET A SD  1 
ATOM   985  C CE  . MET A 1 128 ? -9.79800  7.58900   -31.57900 1.000 30.59000 ? 130 MET A CE  1 
ATOM   986  N N   . ARG A 1 129 ? -5.45500  4.39200   -33.02500 1.000 27.59000 ? 131 ARG A N   1 
ATOM   987  C CA  . ARG A 1 129 ? -4.64800  3.80000   -34.08900 1.000 26.62000 ? 131 ARG A CA  1 
ATOM   988  C C   . ARG A 1 129 ? -4.87400  4.53400   -35.40800 1.000 25.89000 ? 131 ARG A C   1 
ATOM   989  O O   . ARG A 1 129 ? -5.91400  5.16900   -35.60800 1.000 26.22000 ? 131 ARG A O   1 
ATOM   990  C CB  . ARG A 1 129 ? -4.98800  2.32000   -34.27100 1.000 25.39000 ? 131 ARG A CB  1 
ATOM   991  C CG  . ARG A 1 129 ? -4.86300  1.46000   -33.02100 1.000 23.20000 ? 131 ARG A CG  1 
ATOM   992  C CD  . ARG A 1 129 ? -3.47400  1.58300   -32.36000 1.000 26.79000 ? 131 ARG A CD  1 
ATOM   993  N NE  . ARG A 1 129 ? -2.38400  1.35800   -33.31500 1.000 27.91000 ? 131 ARG A NE  1 
ATOM   994  C CZ  . ARG A 1 129 ? -1.09300  1.47600   -33.00100 1.000 28.89000 ? 131 ARG A CZ  1 
ATOM   995  N NH1 . ARG A 1 129 ? -0.74400  1.80300   -31.76500 1.000 27.61000 ? 131 ARG A NH1 1 
ATOM   996  N NH2 . ARG A 1 129 ? -0.14900  1.26800   -33.91600 1.000 27.12000 ? 131 ARG A NH2 1 
ATOM   997  N N   . PRO A 1 130 ? -3.90700  4.46300   -36.33200 1.000 30.15000 ? 132 PRO A N   1 
ATOM   998  C CA  . PRO A 1 130 ? -4.13000  5.06200   -37.65900 1.000 25.84000 ? 132 PRO A CA  1 
ATOM   999  C C   . PRO A 1 130 ? -5.39100  4.55300   -38.33900 1.000 28.44000 ? 132 PRO A C   1 
ATOM   1000 O O   . PRO A 1 130 ? -5.99200  5.28200   -39.13700 1.000 31.07000 ? 132 PRO A O   1 
ATOM   1001 C CB  . PRO A 1 130 ? -2.86100  4.67000   -38.43400 1.000 29.57000 ? 132 PRO A CB  1 
ATOM   1002 C CG  . PRO A 1 130 ? -1.80300  4.55400   -37.37200 1.000 27.79000 ? 132 PRO A CG  1 
ATOM   1003 C CD  . PRO A 1 130 ? -2.52900  3.96000   -36.17200 1.000 25.55000 ? 132 PRO A CD  1 
ATOM   1004 N N   . ASN A 1 131 ? -5.83400  3.34000   -38.03000 1.000 26.49000 ? 133 ASN A N   1 
ATOM   1005 C CA  . ASN A 1 131 ? -7.04500  2.82100   -38.64300 1.000 27.64000 ? 133 ASN A CA  1 
ATOM   1006 C C   . ASN A 1 131 ? -8.30500  3.17800   -37.85300 1.000 32.47000 ? 133 ASN A C   1 
ATOM   1007 O O   . ASN A 1 131 ? -9.36500  2.59400   -38.11300 1.000 29.83000 ? 133 ASN A O   1 
ATOM   1008 C CB  . ASN A 1 131 ? -6.93200  1.30700   -38.85400 1.000 28.51000 ? 133 ASN A CB  1 
ATOM   1009 C CG  . ASN A 1 131 ? -6.96600  0.50600   -37.56900 1.000 32.02000 ? 133 ASN A CG  1 
ATOM   1010 O OD1 . ASN A 1 131 ? -7.01400  1.04600   -36.45300 1.000 32.09000 ? 133 ASN A OD1 1 
ATOM   1011 N ND2 . ASN A 1 131 ? -6.96300  -0.81300  -37.72300 1.000 30.94000 ? 133 ASN A ND2 1 
ATOM   1012 N N   . PHE A 1 132 ? -8.19400  4.11300   -36.90000 1.000 27.21000 ? 134 PHE A N   1 
ATOM   1013 C CA  . PHE A 1 132 ? -9.29900  4.71200   -36.15000 1.000 30.72000 ? 134 PHE A CA  1 
ATOM   1014 C C   . PHE A 1 132 ? -9.91300  3.76400   -35.13500 1.000 31.51000 ? 134 PHE A C   1 
ATOM   1015 O O   . PHE A 1 132 ? -11.01200 4.02100   -34.62600 1.000 33.37000 ? 134 PHE A O   1 
ATOM   1016 C CB  . PHE A 1 132 ? -10.37700 5.26900   -37.08700 1.000 29.66000 ? 134 PHE A CB  1 
ATOM   1017 C CG  . PHE A 1 132 ? -9.91100  6.45800   -37.87000 1.000 33.39000 ? 134 PHE A CG  1 
ATOM   1018 C CD1 . PHE A 1 132 ? -9.82000  7.70500   -37.26800 1.000 35.84000 ? 134 PHE A CD1 1 
ATOM   1019 C CD2 . PHE A 1 132 ? -9.51400  6.32300   -39.18600 1.000 31.66000 ? 134 PHE A CD2 1 
ATOM   1020 C CE1 . PHE A 1 132 ? -9.36800  8.80300   -37.98500 1.000 36.14000 ? 134 PHE A CE1 1 
ATOM   1021 C CE2 . PHE A 1 132 ? -9.06200  7.41400   -39.90300 1.000 35.45000 ? 134 PHE A CE2 1 
ATOM   1022 C CZ  . PHE A 1 132 ? -8.99500  8.65900   -39.30200 1.000 30.67000 ? 134 PHE A CZ  1 
ATOM   1023 N N   . THR A 1 133 ? -9.21600  2.69100   -34.79900 1.000 26.19000 ? 135 THR A N   1 
ATOM   1024 C CA  . THR A 1 133 ? -9.64100  1.80200   -33.73600 1.000 28.86000 ? 135 THR A CA  1 
ATOM   1025 C C   . THR A 1 133 ? -8.83900  2.08800   -32.48300 1.000 28.60000 ? 135 THR A C   1 
ATOM   1026 O O   . THR A 1 133 ? -7.85000  2.82700   -32.49000 1.000 31.35000 ? 135 THR A O   1 
ATOM   1027 C CB  . THR A 1 133 ? -9.49600  0.32900   -34.13700 1.000 28.34000 ? 135 THR A CB  1 
ATOM   1028 O OG1 . THR A 1 133 ? -8.11000  -0.00800  -34.30600 1.000 30.06000 ? 135 THR A OG1 1 
ATOM   1029 C CG2 . THR A 1 133 ? -10.27000 0.06000   -35.41800 1.000 30.43000 ? 135 THR A CG2 1 
ATOM   1030 N N   . ILE A 1 134 ? -9.27800  1.46900   -31.40000 1.000 28.59000 ? 136 ILE A N   1 
ATOM   1031 C CA  . ILE A 1 134 ? -8.66000  1.56600   -30.08800 1.000 26.40000 ? 136 ILE A CA  1 
ATOM   1032 C C   . ILE A 1 134 ? -8.28200  0.14800   -29.68300 1.000 28.64000 ? 136 ILE A C   1 
ATOM   1033 O O   . ILE A 1 134 ? -9.11800  -0.75500  -29.75700 1.000 29.07000 ? 136 ILE A O   1 
ATOM   1034 C CB  . ILE A 1 134 ? -9.65200  2.19000   -29.08300 1.000 32.67000 ? 136 ILE A CB  1 
ATOM   1035 C CG1 . ILE A 1 134 ? -9.98000  3.64100   -29.45700 1.000 35.62000 ? 136 ILE A CG1 1 
ATOM   1036 C CG2 . ILE A 1 134 ? -9.18200  2.06500   -27.68000 1.000 35.13000 ? 136 ILE A CG2 1 
ATOM   1037 C CD1 . ILE A 1 134 ? -8.78100  4.47300   -29.73500 1.000 31.74000 ? 136 ILE A CD1 1 
ATOM   1038 N N   . LYS A 1 135 ? -7.02700  -0.06600  -29.28300 1.000 29.62000 ? 137 LYS A N   1 
ATOM   1039 C CA  . LYS A 1 135 ? -6.64100  -1.35900  -28.71300 1.000 29.71000 ? 137 LYS A CA  1 
ATOM   1040 C C   . LYS A 1 135 ? -6.88300  -1.32400  -27.20400 1.000 30.42000 ? 137 LYS A C   1 
ATOM   1041 O O   . LYS A 1 135 ? -5.96900  -1.22000  -26.38400 1.000 34.91000 ? 137 LYS A O   1 
ATOM   1042 C CB  . LYS A 1 135 ? -5.18600  -1.69100  -29.05300 1.000 31.95000 ? 137 LYS A CB  1 
ATOM   1043 N N   . GLY A 1 136 ? -8.16600  -1.40500  -26.83800 1.000 33.07000 ? 138 GLY A N   1 
ATOM   1044 C CA  . GLY A 1 136 ? -8.57000  -1.25900  -25.45800 1.000 30.68000 ? 138 GLY A CA  1 
ATOM   1045 C C   . GLY A 1 136 ? -8.66800  -2.58600  -24.73700 1.000 32.70000 ? 138 GLY A C   1 
ATOM   1046 O O   . GLY A 1 136 ? -8.46200  -3.66100  -25.29900 1.000 35.26000 ? 138 GLY A O   1 
ATOM   1047 N N   . SER A 1 137 ? -8.97200  -2.49500  -23.44800 1.000 31.50000 ? 139 SER A N   1 
ATOM   1048 C CA  . SER A 1 137 ? -9.26600  -3.65700  -22.62200 1.000 31.82000 ? 139 SER A CA  1 
ATOM   1049 C C   . SER A 1 137 ? -10.70200 -3.45000  -22.15800 1.000 35.79000 ? 139 SER A C   1 
ATOM   1050 O O   . SER A 1 137 ? -10.96700 -2.87000  -21.10200 1.000 39.61000 ? 139 SER A O   1 
ATOM   1051 C CB  . SER A 1 137 ? -8.29400  -3.79700  -21.46600 1.000 37.98000 ? 139 SER A CB  1 
ATOM   1052 O OG  . SER A 1 137 ? -8.69400  -4.86100  -20.61900 1.000 40.39000 ? 139 SER A OG  1 
ATOM   1053 N N   . PHE A 1 138 ? -11.63300 -3.89500  -22.98200 1.000 31.41000 ? 140 PHE A N   1 
ATOM   1054 C CA  . PHE A 1 138 ? -13.05400 -3.71700  -22.73500 1.000 31.02000 ? 140 PHE A CA  1 
ATOM   1055 C C   . PHE A 1 138 ? -13.73300 -5.07400  -22.76500 1.000 33.06000 ? 140 PHE A C   1 
ATOM   1056 O O   . PHE A 1 138 ? -13.42400 -5.91200  -23.62000 1.000 31.31000 ? 140 PHE A O   1 
ATOM   1057 C CB  . PHE A 1 138 ? -13.70200 -2.82400  -23.78700 1.000 32.65000 ? 140 PHE A CB  1 
ATOM   1058 C CG  . PHE A 1 138 ? -13.33200 -1.36900  -23.69200 1.000 31.17000 ? 140 PHE A CG  1 
ATOM   1059 C CD1 . PHE A 1 138 ? -13.48600 -0.66900  -22.50800 1.000 32.92000 ? 140 PHE A CD1 1 
ATOM   1060 C CD2 . PHE A 1 138 ? -12.89500 -0.68500  -24.82000 1.000 30.53000 ? 140 PHE A CD2 1 
ATOM   1061 C CE1 . PHE A 1 138 ? -13.18400 0.68300   -22.44100 1.000 32.06000 ? 140 PHE A CE1 1 
ATOM   1062 C CE2 . PHE A 1 138 ? -12.59800 0.66600   -24.76200 1.000 28.51000 ? 140 PHE A CE2 1 
ATOM   1063 C CZ  . PHE A 1 138 ? -12.74200 1.34700   -23.57100 1.000 27.46000 ? 140 PHE A CZ  1 
ATOM   1064 N N   . LEU A 1 139 ? -14.64900 -5.28100  -21.82700 1.000 30.31000 ? 141 LEU A N   1 
ATOM   1065 C CA  . LEU A 1 139 ? -15.49800 -6.45700  -21.74700 1.000 29.24000 ? 141 LEU A CA  1 
ATOM   1066 C C   . LEU A 1 139 ? -16.93300 -6.05600  -22.06400 1.000 31.93000 ? 141 LEU A C   1 
ATOM   1067 O O   . LEU A 1 139 ? -17.23300 -4.87700  -22.26500 1.000 30.03000 ? 141 LEU A O   1 
ATOM   1068 C CB  . LEU A 1 139 ? -15.41300 -7.08200  -20.34900 1.000 31.62000 ? 141 LEU A CB  1 
ATOM   1069 C CG  . LEU A 1 139 ? -13.98800 -7.45200  -19.92300 1.000 35.27000 ? 141 LEU A CG  1 
ATOM   1070 C CD1 . LEU A 1 139 ? -13.99200 -8.10600  -18.53500 1.000 37.65000 ? 141 LEU A CD1 1 
ATOM   1071 C CD2 . LEU A 1 139 ? -13.35100 -8.35500  -20.96400 1.000 36.65000 ? 141 LEU A CD2 1 
ATOM   1072 N N   . ASN A 1 140 ? -17.81600 -7.05400  -22.13700 1.000 31.67000 ? 142 ASN A N   1 
ATOM   1073 C CA  . ASN A 1 140 ? -19.23200 -6.78200  -22.34000 1.000 27.96000 ? 142 ASN A CA  1 
ATOM   1074 C C   . ASN A 1 140 ? -19.73800 -5.78600  -21.30300 1.000 30.38000 ? 142 ASN A C   1 
ATOM   1075 O O   . ASN A 1 140 ? -19.36300 -5.84600  -20.12600 1.000 29.97000 ? 142 ASN A O   1 
ATOM   1076 C CB  . ASN A 1 140 ? -20.05000 -8.07400  -22.29000 1.000 30.00000 ? 142 ASN A CB  1 
ATOM   1077 C CG  . ASN A 1 140 ? -19.83600 -8.94700  -23.51100 1.000 30.00000 ? 142 ASN A CG  1 
ATOM   1078 O OD1 . ASN A 1 140 ? -19.43900 -8.46500  -24.57100 1.000 30.00000 ? 142 ASN A OD1 1 
ATOM   1079 N ND2 . ASN A 1 140 ? -20.09900 -10.24100 -23.36700 1.000 30.00000 ? 142 ASN A ND2 1 
ATOM   1080 N N   . GLY A 1 141 ? -20.59200 -4.85500  -21.74900 1.000 25.07000 ? 143 GLY A N   1 
ATOM   1081 C CA  . GLY A 1 141 ? -21.13700 -3.85000  -20.85600 1.000 27.88000 ? 143 GLY A CA  1 
ATOM   1082 C C   . GLY A 1 141 ? -20.22500 -2.67100  -20.56700 1.000 27.98000 ? 143 GLY A C   1 
ATOM   1083 O O   . GLY A 1 141 ? -20.60300 -1.79800  -19.77300 1.000 28.29000 ? 143 GLY A O   1 
ATOM   1084 N N   . SER A 1 142 ? -19.02600 -2.63500  -21.15600 1.000 25.74000 ? 144 SER A N   1 
ATOM   1085 C CA  . SER A 1 142 ? -18.12000 -1.49800  -21.03300 1.000 24.95000 ? 144 SER A CA  1 
ATOM   1086 C C   . SER A 1 142 ? -18.57300 -0.29700  -21.83800 1.000 24.91000 ? 144 SER A C   1 
ATOM   1087 O O   . SER A 1 142 ? -18.01800 0.78900   -21.65900 1.000 22.05000 ? 144 SER A O   1 
ATOM   1088 C CB  . SER A 1 142 ? -16.73800 -1.89300  -21.51800 1.000 25.67000 ? 144 SER A CB  1 
ATOM   1089 O OG  . SER A 1 142 ? -16.85700 -2.36700  -22.85400 1.000 26.13000 ? 144 SER A OG  1 
ATOM   1090 N N   . CYS A 1 143 ? -19.54900 -0.47500  -22.73100 1.000 26.71000 ? 145 CYS A N   1 
ATOM   1091 C CA  . CYS A 1 143 ? -20.01500 0.61300   -23.58000 1.000 24.92000 ? 145 CYS A CA  1 
ATOM   1092 C C   . CYS A 1 143 ? -20.33300 1.84600   -22.75600 1.000 23.31000 ? 145 CYS A C   1 
ATOM   1093 O O   . CYS A 1 143 ? -20.89800 1.75500   -21.66500 1.000 24.46000 ? 145 CYS A O   1 
ATOM   1094 C CB  . CYS A 1 143 ? -21.25700 0.17300   -24.35100 1.000 26.03000 ? 145 CYS A CB  1 
ATOM   1095 S SG  . CYS A 1 143 ? -21.04400 -1.39700  -25.21200 1.000 29.59000 ? 145 CYS A SG  1 
ATOM   1096 N N   . GLY A 1 144 ? -19.94300 3.00400   -23.27600 1.000 23.44000 ? 146 GLY A N   1 
ATOM   1097 C CA  . GLY A 1 144 ? -20.15600 4.24100   -22.57500 1.000 25.98000 ? 146 GLY A CA  1 
ATOM   1098 C C   . GLY A 1 144 ? -19.01900 4.65500   -21.66800 1.000 25.41000 ? 146 GLY A C   1 
ATOM   1099 O O   . GLY A 1 144 ? -19.04900 5.77800   -21.15000 1.000 24.18000 ? 146 GLY A O   1 
ATOM   1100 N N   . SER A 1 145 ? -18.02300 3.79400   -21.45300 1.000 25.57000 ? 147 SER A N   1 
ATOM   1101 C CA  . SER A 1 145 ? -16.77400 4.24200   -20.83800 1.000 23.74000 ? 147 SER A CA  1 
ATOM   1102 C C   . SER A 1 145 ? -16.12900 5.31800   -21.70800 1.000 23.17000 ? 147 SER A C   1 
ATOM   1103 O O   . SER A 1 145 ? -16.27400 5.32100   -22.93000 1.000 23.12000 ? 147 SER A O   1 
ATOM   1104 C CB  . SER A 1 145 ? -15.80100 3.06700   -20.66000 1.000 23.31000 ? 147 SER A CB  1 
ATOM   1105 O OG  . SER A 1 145 ? -16.31600 2.10900   -19.73100 1.000 25.51000 ? 147 SER A OG  1 
ATOM   1106 N N   . VAL A 1 146 ? -15.41700 6.25400   -21.07600 1.000 21.33000 ? 148 VAL A N   1 
ATOM   1107 C CA  . VAL A 1 146 ? -14.88600 7.37500   -21.84200 1.000 22.53000 ? 148 VAL A CA  1 
ATOM   1108 C C   . VAL A 1 146 ? -13.36900 7.41400   -21.75800 1.000 25.47000 ? 148 VAL A C   1 
ATOM   1109 O O   . VAL A 1 146 ? -12.74100 6.85800   -20.84300 1.000 26.16000 ? 148 VAL A O   1 
ATOM   1110 C CB  . VAL A 1 146 ? -15.49500 8.74200   -21.42500 1.000 21.85000 ? 148 VAL A CB  1 
ATOM   1111 C CG1 . VAL A 1 146 ? -16.96800 8.80400   -21.87400 1.000 23.93000 ? 148 VAL A CG1 1 
ATOM   1112 C CG2 . VAL A 1 146 ? -15.38300 8.98000   -19.92200 1.000 21.47000 ? 148 VAL A CG2 1 
ATOM   1113 N N   . GLY A 1 147 ? -12.78800 8.03700   -22.78000 1.000 24.62000 ? 149 GLY A N   1 
ATOM   1114 C CA  . GLY A 1 147 ? -11.36500 8.33900   -22.83400 1.000 22.59000 ? 149 GLY A CA  1 
ATOM   1115 C C   . GLY A 1 147 ? -11.17700 9.83700   -22.69300 1.000 24.38000 ? 149 GLY A C   1 
ATOM   1116 O O   . GLY A 1 147 ? -12.00600 10.62800  -23.17100 1.000 24.39000 ? 149 GLY A O   1 
ATOM   1117 N N   . PHE A 1 148 ? -10.09300 10.23500  -22.03600 1.000 23.27000 ? 150 PHE A N   1 
ATOM   1118 C CA  . PHE A 1 148 ? -9.96200  11.63600  -21.64400 1.000 24.69000 ? 150 PHE A CA  1 
ATOM   1119 C C   . PHE A 1 148 ? -8.49800  11.99000  -21.46100 1.000 24.98000 ? 150 PHE A C   1 
ATOM   1120 O O   . PHE A 1 148 ? -7.65200  11.11700  -21.24900 1.000 23.42000 ? 150 PHE A O   1 
ATOM   1121 C CB  . PHE A 1 148 ? -10.72800 11.93700  -20.34200 1.000 23.37000 ? 150 PHE A CB  1 
ATOM   1122 C CG  . PHE A 1 148 ? -10.31400 11.08200  -19.18900 1.000 26.47000 ? 150 PHE A CG  1 
ATOM   1123 C CD1 . PHE A 1 148 ? -10.82300 9.79500   -19.05000 1.000 26.63000 ? 150 PHE A CD1 1 
ATOM   1124 C CD2 . PHE A 1 148 ? -9.41800  11.55500  -18.24000 1.000 26.09000 ? 150 PHE A CD2 1 
ATOM   1125 C CE1 . PHE A 1 148 ? -10.43800 8.99500   -18.00100 1.000 25.70000 ? 150 PHE A CE1 1 
ATOM   1126 C CE2 . PHE A 1 148 ? -9.02600  10.75000  -17.17600 1.000 29.08000 ? 150 PHE A CE2 1 
ATOM   1127 C CZ  . PHE A 1 148 ? -9.55300  9.46600   -17.05500 1.000 28.14000 ? 150 PHE A CZ  1 
ATOM   1128 N N   . ASN A 1 149 ? -8.22400  13.29300  -21.51600 1.000 24.77000 ? 151 ASN A N   1 
ATOM   1129 C CA  . ASN A 1 149 ? -6.97200  13.86000  -21.03700 1.000 26.98000 ? 151 ASN A CA  1 
ATOM   1130 C C   . ASN A 1 149 ? -7.28600  14.94400  -20.01600 1.000 30.40000 ? 151 ASN A C   1 
ATOM   1131 O O   . ASN A 1 149 ? -8.40700  15.45900  -19.95300 1.000 30.21000 ? 151 ASN A O   1 
ATOM   1132 C CB  . ASN A 1 149 ? -6.12800  14.43600  -22.17900 1.000 29.79000 ? 151 ASN A CB  1 
ATOM   1133 C CG  . ASN A 1 149 ? -5.58900  13.36100  -23.09400 1.000 29.00000 ? 151 ASN A CG  1 
ATOM   1134 O OD1 . ASN A 1 149 ? -4.67000  12.62700  -22.73300 1.000 30.07000 ? 151 ASN A OD1 1 
ATOM   1135 N ND2 . ASN A 1 149 ? -6.18000  13.24200  -24.28000 1.000 27.96000 ? 151 ASN A ND2 1 
ATOM   1136 N N   . ILE A 1 150 ? -6.29400  15.26200  -19.18600 1.000 29.33000 ? 152 ILE A N   1 
ATOM   1137 C CA  . ILE A 1 150 ? -6.44800  16.31400  -18.18700 1.000 29.92000 ? 152 ILE A CA  1 
ATOM   1138 C C   . ILE A 1 150 ? -5.15500  17.11400  -18.10400 1.000 36.51000 ? 152 ILE A C   1 
ATOM   1139 O O   . ILE A 1 150 ? -4.42200  17.02800  -17.11200 1.000 38.79000 ? 152 ILE A O   1 
ATOM   1140 C CB  . ILE A 1 150 ? -6.79000  15.76000  -16.79100 1.000 29.49000 ? 152 ILE A CB  1 
ATOM   1141 C CG1 . ILE A 1 150 ? -7.78000  14.58900  -16.85800 1.000 26.73000 ? 152 ILE A CG1 1 
ATOM   1142 C CG2 . ILE A 1 150 ? -7.30500  16.88700  -15.88800 1.000 33.74000 ? 152 ILE A CG2 1 
ATOM   1143 C CD1 . ILE A 1 150 ? -8.30700  14.16000  -15.48700 1.000 26.97000 ? 152 ILE A CD1 1 
ATOM   1144 N N   . ASP A 1 151 ? -4.86500  17.90000  -19.12600 1.000 40.57000 ? 153 ASP A N   1 
ATOM   1145 C CA  . ASP A 1 151 ? -3.78600  18.87400  -19.02800 1.000 46.79000 ? 153 ASP A CA  1 
ATOM   1146 C C   . ASP A 1 151 ? -4.34200  20.13300  -18.36300 1.000 47.20000 ? 153 ASP A C   1 
ATOM   1147 O O   . ASP A 1 151 ? -5.32500  20.71000  -18.84100 1.000 47.55000 ? 153 ASP A O   1 
ATOM   1148 C CB  . ASP A 1 151 ? -3.20100  19.17500  -20.41100 1.000 44.47000 ? 153 ASP A CB  1 
ATOM   1149 C CG  . ASP A 1 151 ? -2.99600  17.91000  -21.26300 1.000 44.43000 ? 153 ASP A CG  1 
ATOM   1150 O OD1 . ASP A 1 151 ? -2.34200  16.94300  -20.80900 1.000 42.24000 ? 153 ASP A OD1 1 
ATOM   1151 O OD2 . ASP A 1 151 ? -3.48100  17.87600  -22.41500 1.000 39.34000 ? 153 ASP A OD2 1 
ATOM   1152 N N   . TYR A 1 152 ? -3.73700  20.52400  -17.23700 1.000 51.28000 ? 154 TYR A N   1 
ATOM   1153 C CA  . TYR A 1 152 ? -4.07800  21.74900  -16.50900 1.000 52.58000 ? 154 TYR A CA  1 
ATOM   1154 C C   . TYR A 1 152 ? -5.56600  21.82000  -16.15100 1.000 50.47000 ? 154 TYR A C   1 
ATOM   1155 O O   . TYR A 1 152 ? -6.32900  22.61100  -16.70700 1.000 53.78000 ? 154 TYR A O   1 
ATOM   1156 C CB  . TYR A 1 152 ? -3.63700  22.98500  -17.30700 1.000 53.20000 ? 154 TYR A CB  1 
ATOM   1157 N N   . ASP A 1 153 ? -5.97000  20.95200  -15.22000 1.000 49.54000 ? 155 ASP A N   1 
ATOM   1158 C CA  . ASP A 1 153 ? -7.21900  21.11300  -14.47500 1.000 53.22000 ? 155 ASP A CA  1 
ATOM   1159 C C   . ASP A 1 153 ? -8.49200  20.86900  -15.29500 1.000 48.95000 ? 155 ASP A C   1 
ATOM   1160 O O   . ASP A 1 153 ? -9.55900  20.61400  -14.72100 1.000 48.75000 ? 155 ASP A O   1 
ATOM   1161 C CB  . ASP A 1 153 ? -7.24100  22.51400  -13.83700 1.000 59.03000 ? 155 ASP A CB  1 
ATOM   1162 C CG  . ASP A 1 153 ? -8.56600  22.85100  -13.16900 1.000 60.11000 ? 155 ASP A CG  1 
ATOM   1163 O OD1 . ASP A 1 153 ? -9.05100  22.05100  -12.34400 1.000 63.66000 ? 155 ASP A OD1 1 
ATOM   1164 O OD2 . ASP A 1 153 ? -9.10100  23.94900  -13.46100 1.000 61.29000 ? 155 ASP A OD2 1 
ATOM   1165 N N   . CYS A 1 154 ? -8.39800  20.90000  -16.62500 1.000 44.27000 ? 156 CYS A N   1 
ATOM   1166 C CA  . CYS A 1 154 ? -9.55600  20.76700  -17.50900 1.000 43.19000 ? 156 CYS A CA  1 
ATOM   1167 C C   . CYS A 1 154 ? -9.60100  19.36900  -18.11900 1.000 35.70000 ? 156 CYS A C   1 
ATOM   1168 O O   . CYS A 1 154 ? -8.64800  18.95200  -18.78500 1.000 35.77000 ? 156 CYS A O   1 
ATOM   1169 C CB  . CYS A 1 154 ? -9.52000  21.81400  -18.62400 1.000 41.62000 ? 156 CYS A CB  1 
ATOM   1170 S SG  . CYS A 1 154 ? -10.97900 21.76200  -19.70800 1.000 39.95000 ? 156 CYS A SG  1 
ATOM   1171 N N   . VAL A 1 155 ? -10.72200 18.67000  -17.93100 1.000 31.21000 ? 157 VAL A N   1 
ATOM   1172 C CA  . VAL A 1 155 ? -10.90300 17.34200  -18.51400 1.000 28.88000 ? 157 VAL A CA  1 
ATOM   1173 C C   . VAL A 1 155 ? -11.35200 17.47700  -19.96500 1.000 30.31000 ? 157 VAL A C   1 
ATOM   1174 O O   . VAL A 1 155 ? -12.44500 17.98700  -20.24200 1.000 32.98000 ? 157 VAL A O   1 
ATOM   1175 C CB  . VAL A 1 155 ? -11.91900 16.51300  -17.71500 1.000 27.73000 ? 157 VAL A CB  1 
ATOM   1176 C CG1 . VAL A 1 155 ? -12.11100 15.16400  -18.37500 1.000 28.46000 ? 157 VAL A CG1 1 
ATOM   1177 C CG2 . VAL A 1 155 ? -11.48600 16.33700  -16.26400 1.000 26.85000 ? 157 VAL A CG2 1 
ATOM   1178 N N   . SER A 1 156 ? -10.55500 16.94300  -20.89100 1.000 26.20000 ? 158 SER A N   1 
ATOM   1179 C CA  . SER A 1 156 ? -10.92200 16.90400  -22.30500 1.000 28.92000 ? 158 SER A CA  1 
ATOM   1180 C C   . SER A 1 156 ? -11.41200 15.49300  -22.63900 1.000 28.97000 ? 158 SER A C   1 
ATOM   1181 O O   . SER A 1 156 ? -10.62000 14.54500  -22.67800 1.000 28.92000 ? 158 SER A O   1 
ATOM   1182 C CB  . SER A 1 156 ? -9.75900  17.33200  -23.20600 1.000 30.06000 ? 158 SER A CB  1 
ATOM   1183 O OG  . SER A 1 156 ? -8.53000  16.70500  -22.85900 1.000 34.95000 ? 158 SER A OG  1 
ATOM   1184 N N   . PHE A 1 157 ? -12.72300 15.35300  -22.85200 1.000 26.35000 ? 159 PHE A N   1 
ATOM   1185 C CA  . PHE A 1 157 ? -13.31500 14.07400  -23.23400 1.000 23.87000 ? 159 PHE A CA  1 
ATOM   1186 C C   . PHE A 1 157 ? -13.18700 13.89500  -24.74300 1.000 24.70000 ? 159 PHE A C   1 
ATOM   1187 O O   . PHE A 1 157 ? -13.67200 14.72300  -25.52400 1.000 28.09000 ? 159 PHE A O   1 
ATOM   1188 C CB  . PHE A 1 157 ? -14.78500 14.00500  -22.80400 1.000 25.44000 ? 159 PHE A CB  1 
ATOM   1189 C CG  . PHE A 1 157 ? -14.98200 13.96800  -21.29800 1.000 25.36000 ? 159 PHE A CG  1 
ATOM   1190 C CD1 . PHE A 1 157 ? -14.73200 12.80400  -20.56800 1.000 21.66000 ? 159 PHE A CD1 1 
ATOM   1191 C CD2 . PHE A 1 157 ? -15.38500 15.10300  -20.61500 1.000 27.27000 ? 159 PHE A CD2 1 
ATOM   1192 C CE1 . PHE A 1 157 ? -14.90200 12.77100  -19.18900 1.000 24.10000 ? 159 PHE A CE1 1 
ATOM   1193 C CE2 . PHE A 1 157 ? -15.56700 15.07300  -19.22600 1.000 26.28000 ? 159 PHE A CE2 1 
ATOM   1194 C CZ  . PHE A 1 157 ? -15.33000 13.91500  -18.52100 1.000 27.24000 ? 159 PHE A CZ  1 
ATOM   1195 N N   . CYS A 1 158 ? -12.56400 12.80900  -25.16400 1.000 23.81000 ? 160 CYS A N   1 
ATOM   1196 C CA  . CYS A 1 158 ? -12.28200 12.61900  -26.57200 1.000 24.51000 ? 160 CYS A CA  1 
ATOM   1197 C C   . CYS A 1 158 ? -12.77500 11.30000  -27.13200 1.000 22.92000 ? 160 CYS A C   1 
ATOM   1198 O O   . CYS A 1 158 ? -12.75200 11.13400  -28.35700 1.000 28.57000 ? 160 CYS A O   1 
ATOM   1199 C CB  . CYS A 1 158 ? -10.77400 12.73200  -26.83300 1.000 28.66000 ? 160 CYS A CB  1 
ATOM   1200 S SG  . CYS A 1 158 ? -9.80900  11.47800  -25.99100 1.000 30.78000 ? 160 CYS A SG  1 
ATOM   1201 N N   . TYR A 1 159 ? -13.23900 10.37200  -26.29900 1.000 25.76000 ? 161 TYR A N   1 
ATOM   1202 C CA  . TYR A 1 159 ? -13.68700 9.07700   -26.79400 1.000 25.58000 ? 161 TYR A CA  1 
ATOM   1203 C C   . TYR A 1 159 ? -14.80200 8.54500   -25.90900 1.000 23.35000 ? 161 TYR A C   1 
ATOM   1204 O O   . TYR A 1 159 ? -14.70700 8.61700   -24.68200 1.000 22.98000 ? 161 TYR A O   1 
ATOM   1205 C CB  . TYR A 1 159 ? -12.52300 8.07900   -26.80400 1.000 22.60000 ? 161 TYR A CB  1 
ATOM   1206 C CG  . TYR A 1 159 ? -12.90300 6.67500   -27.21000 1.000 21.02000 ? 161 TYR A CG  1 
ATOM   1207 C CD1 . TYR A 1 159 ? -12.98200 6.32600   -28.55100 1.000 23.79000 ? 161 TYR A CD1 1 
ATOM   1208 C CD2 . TYR A 1 159 ? -13.13700 5.68400   -26.25300 1.000 20.22000 ? 161 TYR A CD2 1 
ATOM   1209 C CE1 . TYR A 1 159 ? -13.29100 5.02800   -28.94400 1.000 25.33000 ? 161 TYR A CE1 1 
ATOM   1210 C CE2 . TYR A 1 159 ? -13.45100 4.37800   -26.63800 1.000 23.47000 ? 161 TYR A CE2 1 
ATOM   1211 C CZ  . TYR A 1 159 ? -13.54300 4.07100   -27.98400 1.000 24.25000 ? 161 TYR A CZ  1 
ATOM   1212 O OH  . TYR A 1 159 ? -13.86000 2.80100   -28.38100 1.000 27.18000 ? 161 TYR A OH  1 
ATOM   1213 N N   . MET A 1 160 ? -15.85100 8.00700   -26.52800 1.000 23.40000 ? 162 MET A N   1 
ATOM   1214 C CA  . MET A 1 160 ? -16.84900 7.21000   -25.81800 1.000 19.01000 ? 162 MET A CA  1 
ATOM   1215 C C   . MET A 1 160 ? -16.92900 5.84700   -26.48500 1.000 20.16000 ? 162 MET A C   1 
ATOM   1216 O O   . MET A 1 160 ? -17.04300 5.76100   -27.70800 1.000 21.96000 ? 162 MET A O   1 
ATOM   1217 C CB  . MET A 1 160 ? -18.23500 7.86000   -25.80500 1.000 23.17000 ? 162 MET A CB  1 
ATOM   1218 C CG  . MET A 1 160 ? -19.24100 6.93600   -25.14100 1.000 20.48000 ? 162 MET A CG  1 
ATOM   1219 S SD  . MET A 1 160 ? -20.86300 7.71900   -24.90400 1.000 28.47000 ? 162 MET A SD  1 
ATOM   1220 C CE  . MET A 1 160 ? -20.60400 8.49000   -23.32300 1.000 25.87000 ? 162 MET A CE  1 
ATOM   1221 N N   . HIS A 1 161 ? -16.86700 4.78600   -25.68800 1.000 22.45000 ? 163 HIS A N   1 
ATOM   1222 C CA  . HIS A 1 161 ? -16.74900 3.44500   -26.24600 1.000 23.28000 ? 163 HIS A CA  1 
ATOM   1223 C C   . HIS A 1 161 ? -18.11600 2.91800   -26.67800 1.000 23.94000 ? 163 HIS A C   1 
ATOM   1224 O O   . HIS A 1 161 ? -19.09200 3.04500   -25.94100 1.000 23.25000 ? 163 HIS A O   1 
ATOM   1225 C CB  . HIS A 1 161 ? -16.12700 2.50400   -25.22300 1.000 23.71000 ? 163 HIS A CB  1 
ATOM   1226 C CG  . HIS A 1 161 ? -16.05400 1.10000   -25.70500 1.000 24.24000 ? 163 HIS A CG  1 
ATOM   1227 N ND1 . HIS A 1 161 ? -15.45800 0.77000   -26.90000 1.000 24.93000 ? 163 HIS A ND1 1 
ATOM   1228 C CD2 . HIS A 1 161 ? -16.56300 -0.04700  -25.20100 1.000 24.51000 ? 163 HIS A CD2 1 
ATOM   1229 C CE1 . HIS A 1 161 ? -15.59000 -0.52700  -27.10800 1.000 25.80000 ? 163 HIS A CE1 1 
ATOM   1230 N NE2 . HIS A 1 161 ? -16.24700 -1.04700  -26.08700 1.000 24.20000 ? 163 HIS A NE2 1 
ATOM   1231 N N   . HIS A 1 162 ? -18.19100 2.34100   -27.88700 1.000 25.42000 ? 164 HIS A N   1 
ATOM   1232 C CA  . HIS A 1 162 ? -19.45200 1.77300   -28.36600 1.000 25.80000 ? 164 HIS A CA  1 
ATOM   1233 C C   . HIS A 1 162 ? -19.39700 0.27000   -28.60300 1.000 28.62000 ? 164 HIS A C   1 
ATOM   1234 O O   . HIS A 1 162 ? -20.34900 -0.43200  -28.23100 1.000 28.04000 ? 164 HIS A O   1 
ATOM   1235 C CB  . HIS A 1 162 ? -19.92900 2.46200   -29.67000 1.000 24.38000 ? 164 HIS A CB  1 
ATOM   1236 C CG  . HIS A 1 162 ? -20.42300 3.86400   -29.47800 1.000 25.18000 ? 164 HIS A CG  1 
ATOM   1237 N ND1 . HIS A 1 162 ? -21.71800 4.25400   -29.77300 1.000 27.43000 ? 164 HIS A ND1 1 
ATOM   1238 C CD2 . HIS A 1 162 ? -19.79000 4.97100   -29.02900 1.000 25.28000 ? 164 HIS A CD2 1 
ATOM   1239 C CE1 . HIS A 1 162 ? -21.85500 5.54200   -29.51300 1.000 26.42000 ? 164 HIS A CE1 1 
ATOM   1240 N NE2 . HIS A 1 162 ? -20.70200 6.00000   -29.05100 1.000 24.90000 ? 164 HIS A NE2 1 
ATOM   1241 N N   . MET A 1 163 ? -18.33600 -0.26200  -29.22200 1.000 23.19000 ? 165 MET A N   1 
ATOM   1242 C CA  . MET A 1 163 ? -18.43300 -1.64100  -29.69300 1.000 26.20000 ? 165 MET A CA  1 
ATOM   1243 C C   . MET A 1 163 ? -17.07400 -2.29100  -29.88600 1.000 28.09000 ? 165 MET A C   1 
ATOM   1244 O O   . MET A 1 163 ? -16.04600 -1.62500  -30.01700 1.000 24.97000 ? 165 MET A O   1 
ATOM   1245 C CB  . MET A 1 163 ? -19.17900 -1.72100  -31.01400 1.000 30.64000 ? 165 MET A CB  1 
ATOM   1246 C CG  . MET A 1 163 ? -18.54700 -0.90500  -32.11100 1.000 27.86000 ? 165 MET A CG  1 
ATOM   1247 S SD  . MET A 1 163 ? -19.83800 -0.54700  -33.32400 1.000 38.42000 ? 165 MET A SD  1 
ATOM   1248 C CE  . MET A 1 163 ? -20.47900 -2.21600  -33.58400 1.000 36.58000 ? 165 MET A CE  1 
ATOM   1249 N N   . GLU A 1 164 ? -17.11200 -3.61700  -29.97900 1.000 28.31000 ? 166 GLU A N   1 
ATOM   1250 C CA  . GLU A 1 164 ? -15.95100 -4.43600  -30.28700 1.000 30.33000 ? 166 GLU A CA  1 
ATOM   1251 C C   . GLU A 1 164 ? -16.02200 -4.89700  -31.74100 1.000 33.78000 ? 166 GLU A C   1 
ATOM   1252 O O   . GLU A 1 164 ? -17.09900 -5.23200  -32.24500 1.000 31.98000 ? 166 GLU A O   1 
ATOM   1253 C CB  . GLU A 1 164 ? -15.88400 -5.64300  -29.34600 1.000 29.42000 ? 166 GLU A CB  1 
ATOM   1254 C CG  . GLU A 1 164 ? -14.53300 -6.34500  -29.34500 1.000 34.60000 ? 166 GLU A CG  1 
ATOM   1255 C CD  . GLU A 1 164 ? -14.34100 -7.21200  -28.12000 1.000 38.53000 ? 166 GLU A CD  1 
ATOM   1256 O OE1 . GLU A 1 164 ? -14.94300 -8.30800  -28.08000 1.000 45.44000 ? 166 GLU A OE1 1 
ATOM   1257 O OE2 . GLU A 1 164 ? -13.61800 -6.78200  -27.18400 1.000 38.56000 ? 166 GLU A OE2 1 
ATOM   1258 N N   . LEU A 1 165 ? -14.87900 -4.88800  -32.41500 1.000 29.26000 ? 167 LEU A N   1 
ATOM   1259 C CA  . LEU A 1 165 ? -14.72300 -5.37200  -33.78100 1.000 32.52000 ? 167 LEU A CA  1 
ATOM   1260 C C   . LEU A 1 165 ? -14.19200 -6.79800  -33.77100 1.000 35.28000 ? 167 LEU A C   1 
ATOM   1261 O O   . LEU A 1 165 ? -13.72400 -7.29100  -32.74200 1.000 35.79000 ? 167 LEU A O   1 
ATOM   1262 C CB  . LEU A 1 165 ? -13.76300 -4.46000  -34.55800 1.000 32.79000 ? 167 LEU A CB  1 
ATOM   1263 C CG  . LEU A 1 165 ? -14.11600 -2.99300  -34.78800 1.000 31.27000 ? 167 LEU A CG  1 
ATOM   1264 C CD1 . LEU A 1 165 ? -15.55900 -2.81700  -35.24700 1.000 39.14000 ? 167 LEU A CD1 1 
ATOM   1265 C CD2 . LEU A 1 165 ? -13.84600 -2.19000  -33.55500 1.000 41.52000 ? 167 LEU A CD2 1 
ATOM   1266 N N   . PRO A 1 166 ? -14.21700 -7.49100  -34.92100 1.000 37.96000 ? 168 PRO A N   1 
ATOM   1267 C CA  . PRO A 1 166 ? -13.83800 -8.91800  -34.92700 1.000 36.85000 ? 168 PRO A CA  1 
ATOM   1268 C C   . PRO A 1 166 ? -12.41400 -9.22200  -34.48600 1.000 39.11000 ? 168 PRO A C   1 
ATOM   1269 O O   . PRO A 1 166 ? -12.16900 -10.32200 -33.97600 1.000 39.83000 ? 168 PRO A O   1 
ATOM   1270 C CB  . PRO A 1 166 ? -14.05900 -9.31900  -36.39000 1.000 41.48000 ? 168 PRO A CB  1 
ATOM   1271 C CG  . PRO A 1 166 ? -15.16200 -8.42000  -36.83600 1.000 42.10000 ? 168 PRO A CG  1 
ATOM   1272 C CD  . PRO A 1 166 ? -14.83800 -7.10000  -36.20200 1.000 40.37000 ? 168 PRO A CD  1 
ATOM   1273 N N   . THR A 1 167 ? -11.46400 -8.30900  -34.67300 1.000 35.95000 ? 169 THR A N   1 
ATOM   1274 C CA  . THR A 1 167 ? -10.09500 -8.57600  -34.25200 1.000 36.66000 ? 169 THR A CA  1 
ATOM   1275 C C   . THR A 1 167 ? -9.87700  -8.34000  -32.76600 1.000 38.12000 ? 169 THR A C   1 
ATOM   1276 O O   . THR A 1 167 ? -8.74900  -8.49900  -32.29100 1.000 34.90000 ? 169 THR A O   1 
ATOM   1277 C CB  . THR A 1 167 ? -9.11300  -7.72000  -35.06000 1.000 39.15000 ? 169 THR A CB  1 
ATOM   1278 O OG1 . THR A 1 167 ? -9.64600  -6.39900  -35.22900 1.000 36.93000 ? 169 THR A OG1 1 
ATOM   1279 C CG2 . THR A 1 167 ? -8.88300  -8.34200  -36.43300 1.000 36.96000 ? 169 THR A CG2 1 
ATOM   1280 N N   . GLY A 1 168 ? -10.91500 -7.97200  -32.02000 1.000 33.93000 ? 170 GLY A N   1 
ATOM   1281 C CA  . GLY A 1 168 ? -10.76700 -7.66700  -30.61500 1.000 34.77000 ? 170 GLY A CA  1 
ATOM   1282 C C   . GLY A 1 168 ? -10.40200 -6.23300  -30.30100 1.000 35.81000 ? 170 GLY A C   1 
ATOM   1283 O O   . GLY A 1 168 ? -10.18200 -5.91000  -29.12500 1.000 40.00000 ? 170 GLY A O   1 
ATOM   1284 N N   . VAL A 1 169 ? -10.32600 -5.36200  -31.30500 1.000 32.87000 ? 171 VAL A N   1 
ATOM   1285 C CA  . VAL A 1 169 ? -10.08700 -3.94400  -31.06300 1.000 32.29000 ? 171 VAL A CA  1 
ATOM   1286 C C   . VAL A 1 169 ? -11.43700 -3.24300  -30.99000 1.000 30.96000 ? 171 VAL A C   1 
ATOM   1287 O O   . VAL A 1 169 ? -12.48400 -3.87700  -31.16300 1.000 30.43000 ? 171 VAL A O   1 
ATOM   1288 C CB  . VAL A 1 169 ? -9.19000  -3.34200  -32.15400 1.000 27.69000 ? 171 VAL A CB  1 
ATOM   1289 C CG1 . VAL A 1 169 ? -7.84700  -4.11900  -32.19400 1.000 29.37000 ? 171 VAL A CG1 1 
ATOM   1290 C CG2 . VAL A 1 169 ? -9.89400  -3.41300  -33.49400 1.000 30.58000 ? 171 VAL A CG2 1 
ATOM   1291 N N   . HIS A 1 170 ? -11.43200 -1.94000  -30.73900 1.000 28.81000 ? 172 HIS A N   1 
ATOM   1292 C CA  . HIS A 1 170 ? -12.63700 -1.27100  -30.26500 1.000 27.00000 ? 172 HIS A CA  1 
ATOM   1293 C C   . HIS A 1 170 ? -12.91400 -0.00500  -31.05800 1.000 30.54000 ? 172 HIS A C   1 
ATOM   1294 O O   . HIS A 1 170 ? -11.99600 0.65600   -31.54300 1.000 28.09000 ? 172 HIS A O   1 
ATOM   1295 C CB  . HIS A 1 170 ? -12.50700 -0.97800  -28.76900 1.000 28.31000 ? 172 HIS A CB  1 
ATOM   1296 C CG  . HIS A 1 170 ? -12.25000 -2.21000  -27.95900 1.000 28.91000 ? 172 HIS A CG  1 
ATOM   1297 N ND1 . HIS A 1 170 ? -11.00900 -2.52400  -27.44500 1.000 30.97000 ? 172 HIS A ND1 1 
ATOM   1298 C CD2 . HIS A 1 170 ? -13.06100 -3.25000  -27.64600 1.000 29.01000 ? 172 HIS A CD2 1 
ATOM   1299 C CE1 . HIS A 1 170 ? -11.07800 -3.68100  -26.81100 1.000 31.34000 ? 172 HIS A CE1 1 
ATOM   1300 N NE2 . HIS A 1 170 ? -12.31400 -4.14300  -26.92000 1.000 32.21000 ? 172 HIS A NE2 1 
ATOM   1301 N N   . ALA A 1 171 ? -14.20900 0.30600   -31.22000 1.000 26.62000 ? 173 ALA A N   1 
ATOM   1302 C CA  . ALA A 1 171 ? -14.63300 1.47100   -31.98000 1.000 25.26000 ? 173 ALA A CA  1 
ATOM   1303 C C   . ALA A 1 171 ? -15.57600 2.31600   -31.14100 1.000 27.01000 ? 173 ALA A C   1 
ATOM   1304 O O   . ALA A 1 171 ? -16.35400 1.79500   -30.33300 1.000 23.28000 ? 173 ALA A O   1 
ATOM   1305 C CB  . ALA A 1 171 ? -15.32600 1.07900   -33.29600 1.000 28.21000 ? 173 ALA A CB  1 
ATOM   1306 N N   . GLY A 1 172 ? -15.50500 3.62300   -31.34100 1.000 25.02000 ? 174 GLY A N   1 
ATOM   1307 C CA  . GLY A 1 172 ? -16.31200 4.51600   -30.54500 1.000 23.35000 ? 174 GLY A CA  1 
ATOM   1308 C C   . GLY A 1 172 ? -16.41400 5.86900   -31.20900 1.000 25.34000 ? 174 GLY A C   1 
ATOM   1309 O O   . GLY A 1 172 ? -16.00900 6.04800   -32.36200 1.000 26.91000 ? 174 GLY A O   1 
ATOM   1310 N N   . THR A 1 173 ? -16.94600 6.83200   -30.45900 1.000 24.99000 ? 175 THR A N   1 
ATOM   1311 C CA  . THR A 1 173 ? -17.26300 8.14600   -31.01000 1.000 23.45000 ? 175 THR A CA  1 
ATOM   1312 C C   . THR A 1 173 ? -16.55500 9.23400   -30.21800 1.000 24.29000 ? 175 THR A C   1 
ATOM   1313 O O   . THR A 1 173 ? -16.03200 8.99800   -29.12400 1.000 24.73000 ? 175 THR A O   1 
ATOM   1314 C CB  . THR A 1 173 ? -18.78000 8.40100   -31.00700 1.000 24.16000 ? 175 THR A CB  1 
ATOM   1315 O OG1 . THR A 1 173 ? -19.26900 8.41300   -29.65400 1.000 23.40000 ? 175 THR A OG1 1 
ATOM   1316 C CG2 . THR A 1 173 ? -19.50300 7.31200   -31.80800 1.000 23.55000 ? 175 THR A CG2 1 
ATOM   1317 N N   . ASP A 1 174 ? -16.54200 10.43900  -30.78000 1.000 22.51000 ? 176 ASP A N   1 
ATOM   1318 C CA  . ASP A 1 174 ? -16.33100 11.61000  -29.94300 1.000 25.56000 ? 176 ASP A CA  1 
ATOM   1319 C C   . ASP A 1 174 ? -17.61300 11.86300  -29.13500 1.000 25.25000 ? 176 ASP A C   1 
ATOM   1320 O O   . ASP A 1 174 ? -18.62600 11.17800  -29.30300 1.000 26.81000 ? 176 ASP A O   1 
ATOM   1321 C CB  . ASP A 1 174 ? -15.91000 12.82200  -30.78400 1.000 24.62000 ? 176 ASP A CB  1 
ATOM   1322 C CG  . ASP A 1 174 ? -16.92100 13.19600  -31.88200 1.000 29.22000 ? 176 ASP A CG  1 
ATOM   1323 O OD1 . ASP A 1 174 ? -18.13800 12.96800  -31.73400 1.000 27.17000 ? 176 ASP A OD1 1 
ATOM   1324 O OD2 . ASP A 1 174 ? -16.49200 13.74600  -32.91600 1.000 30.90000 ? 176 ASP A OD2 1 
ATOM   1325 N N   . LEU A 1 175 ? -17.56100 12.82800  -28.21700 1.000 23.81000 ? 177 LEU A N   1 
ATOM   1326 C CA  . LEU A 1 175 ? -18.69900 13.10800  -27.34500 1.000 27.24000 ? 177 LEU A CA  1 
ATOM   1327 C C   . LEU A 1 175 ? -19.81000 13.87400  -28.05200 1.000 27.31000 ? 177 LEU A C   1 
ATOM   1328 O O   . LEU A 1 175 ? -20.85700 14.11400  -27.44100 1.000 28.03000 ? 177 LEU A O   1 
ATOM   1329 C CB  . LEU A 1 175 ? -18.24900 13.86700  -26.08900 1.000 26.08000 ? 177 LEU A CB  1 
ATOM   1330 C CG  . LEU A 1 175 ? -17.89900 12.97300  -24.89300 1.000 28.46000 ? 177 LEU A CG  1 
ATOM   1331 C CD1 . LEU A 1 175 ? -19.13000 12.23600  -24.40500 1.000 27.35000 ? 177 LEU A CD1 1 
ATOM   1332 C CD2 . LEU A 1 175 ? -16.80500 11.97700  -25.25900 1.000 27.45000 ? 177 LEU A CD2 1 
ATOM   1333 N N   . GLU A 1 176 ? -19.62100 14.23600  -29.31600 1.000 25.91000 ? 178 GLU A N   1 
ATOM   1334 C CA  . GLU A 1 176 ? -20.71900 14.65300  -30.17900 1.000 32.36000 ? 178 GLU A CA  1 
ATOM   1335 C C   . GLU A 1 176 ? -21.33600 13.48500  -30.92800 1.000 30.69000 ? 178 GLU A C   1 
ATOM   1336 O O   . GLU A 1 176 ? -22.22300 13.69800  -31.76500 1.000 30.39000 ? 178 GLU A O   1 
ATOM   1337 C CB  . GLU A 1 176 ? -20.24100 15.70300  -31.18200 1.000 32.75000 ? 178 GLU A CB  1 
ATOM   1338 C CG  . GLU A 1 176 ? -19.90600 17.03500  -30.54500 1.000 40.14000 ? 178 GLU A CG  1 
ATOM   1339 C CD  . GLU A 1 176 ? -19.15000 17.93700  -31.49400 1.000 49.45000 ? 178 GLU A CD  1 
ATOM   1340 O OE1 . GLU A 1 176 ? -19.40300 19.15800  -31.47300 1.000 54.60000 ? 178 GLU A OE1 1 
ATOM   1341 O OE2 . GLU A 1 176 ? -18.30900 17.41800  -32.26400 1.000 53.37000 ? 178 GLU A OE2 1 
ATOM   1342 N N   . GLY A 1 177 ? -20.86700 12.26500  -30.66700 1.000 27.91000 ? 179 GLY A N   1 
ATOM   1343 C CA  . GLY A 1 177 ? -21.46000 11.07900  -31.24300 1.000 27.04000 ? 179 GLY A CA  1 
ATOM   1344 C C   . GLY A 1 177 ? -21.03400 10.73000  -32.65000 1.000 28.05000 ? 179 GLY A C   1 
ATOM   1345 O O   . GLY A 1 177 ? -21.64200 9.83900   -33.25000 1.000 27.40000 ? 179 GLY A O   1 
ATOM   1346 N N   . ASN A 1 178 ? -20.02700 11.39700  -33.20900 1.000 24.89000 ? 180 ASN A N   1 
ATOM   1347 C CA  . ASN A 1 178 ? -19.50500 11.02800  -34.52000 1.000 26.68000 ? 180 ASN A CA  1 
ATOM   1348 C C   . ASN A 1 178 ? -18.43300 9.95900   -34.36200 1.000 27.89000 ? 180 ASN A C   1 
ATOM   1349 O O   . ASN A 1 178 ? -17.46600 10.14700  -33.61100 1.000 26.64000 ? 180 ASN A O   1 
ATOM   1350 C CB  . ASN A 1 178 ? -18.93000 12.24300  -35.24700 1.000 26.12000 ? 180 ASN A CB  1 
ATOM   1351 C CG  . ASN A 1 178 ? -20.00400 13.18600  -35.71600 1.000 32.90000 ? 180 ASN A CG  1 
ATOM   1352 O OD1 . ASN A 1 178 ? -20.89600 12.79300  -36.46800 1.000 35.65000 ? 180 ASN A OD1 1 
ATOM   1353 N ND2 . ASN A 1 178 ? -19.94100 14.43300  -35.26400 1.000 33.57000 ? 180 ASN A ND2 1 
ATOM   1354 N N   . PHE A 1 179 ? -18.59900 8.84700   -35.07600 1.000 25.21000 ? 181 PHE A N   1 
ATOM   1355 C CA  . PHE A 1 179 ? -17.64700 7.75200   -34.95100 1.000 26.45000 ? 181 PHE A CA  1 
ATOM   1356 C C   . PHE A 1 179 ? -16.26300 8.18100   -35.41400 1.000 26.12000 ? 181 PHE A C   1 
ATOM   1357 O O   . PHE A 1 179 ? -16.10100 9.01400   -36.31400 1.000 26.16000 ? 181 PHE A O   1 
ATOM   1358 C CB  . PHE A 1 179 ? -18.09000 6.54000   -35.76400 1.000 24.40000 ? 181 PHE A CB  1 
ATOM   1359 C CG  . PHE A 1 179 ? -18.76500 5.45900   -34.94600 1.000 28.48000 ? 181 PHE A CG  1 
ATOM   1360 C CD1 . PHE A 1 179 ? -18.01700 4.48400   -34.29600 1.000 25.95000 ? 181 PHE A CD1 1 
ATOM   1361 C CD2 . PHE A 1 179 ? -20.14600 5.42100   -34.83200 1.000 26.48000 ? 181 PHE A CD2 1 
ATOM   1362 C CE1 . PHE A 1 179 ? -18.63300 3.49600   -33.53900 1.000 26.93000 ? 181 PHE A CE1 1 
ATOM   1363 C CE2 . PHE A 1 179 ? -20.77600 4.43200   -34.08200 1.000 27.03000 ? 181 PHE A CE2 1 
ATOM   1364 C CZ  . PHE A 1 179 ? -20.02700 3.46400   -33.43900 1.000 27.31000 ? 181 PHE A CZ  1 
ATOM   1365 N N   . TYR A 1 180 ? -15.25800 7.59600   -34.78200 1.000 25.40000 ? 182 TYR A N   1 
ATOM   1366 C CA  . TYR A 1 180 ? -13.91900 7.57300   -35.34400 1.000 24.49000 ? 182 TYR A CA  1 
ATOM   1367 C C   . TYR A 1 180 ? -13.86300 6.44000   -36.35600 1.000 27.91000 ? 182 TYR A C   1 
ATOM   1368 O O   . TYR A 1 180 ? -14.20800 5.30000   -36.02900 1.000 29.70000 ? 182 TYR A O   1 
ATOM   1369 C CB  . TYR A 1 180 ? -12.88500 7.37600   -34.23900 1.000 27.74000 ? 182 TYR A CB  1 
ATOM   1370 C CG  . TYR A 1 180 ? -12.74000 8.55500   -33.30400 1.000 25.27000 ? 182 TYR A CG  1 
ATOM   1371 C CD1 . TYR A 1 180 ? -12.07400 9.71100   -33.71100 1.000 27.69000 ? 182 TYR A CD1 1 
ATOM   1372 C CD2 . TYR A 1 180 ? -13.24700 8.51200   -32.00300 1.000 26.62000 ? 182 TYR A CD2 1 
ATOM   1373 C CE1 . TYR A 1 180 ? -11.93600 10.79600  -32.85600 1.000 23.98000 ? 182 TYR A CE1 1 
ATOM   1374 C CE2 . TYR A 1 180 ? -13.09900 9.58700   -31.13900 1.000 23.82000 ? 182 TYR A CE2 1 
ATOM   1375 C CZ  . TYR A 1 180 ? -12.43400 10.72100  -31.57400 1.000 23.92000 ? 182 TYR A CZ  1 
ATOM   1376 O OH  . TYR A 1 180 ? -12.29400 11.78800  -30.71600 1.000 21.88000 ? 182 TYR A OH  1 
ATOM   1377 N N   . GLY A 1 181 ? -13.46900 6.75000   -37.58600 1.000 27.72000 ? 183 GLY A N   1 
ATOM   1378 C CA  . GLY A 1 181 ? -13.39600 5.74900   -38.62500 1.000 29.13000 ? 183 GLY A CA  1 
ATOM   1379 C C   . GLY A 1 181 ? -14.73300 5.44100   -39.26600 1.000 33.45000 ? 183 GLY A C   1 
ATOM   1380 O O   . GLY A 1 181 ? -15.75700 6.06900   -38.97900 1.000 31.31000 ? 183 GLY A O   1 
ATOM   1381 N N   . PRO A 1 182 ? -14.74300 4.44300   -40.13400 1.000 33.59000 ? 184 PRO A N   1 
ATOM   1382 C CA  . PRO A 1 182 ? -15.93500 4.17200   -40.94600 1.000 32.53000 ? 184 PRO A CA  1 
ATOM   1383 C C   . PRO A 1 182 ? -16.85700 3.12800   -40.33400 1.000 33.96000 ? 184 PRO A C   1 
ATOM   1384 O O   . PRO A 1 182 ? -17.43300 2.31500   -41.05900 1.000 40.51000 ? 184 PRO A O   1 
ATOM   1385 C CB  . PRO A 1 182 ? -15.33500 3.67800   -42.26600 1.000 36.14000 ? 184 PRO A CB  1 
ATOM   1386 C CG  . PRO A 1 182 ? -14.03900 3.01100   -41.85600 1.000 35.58000 ? 184 PRO A CG  1 
ATOM   1387 C CD  . PRO A 1 182 ? -13.55300 3.71100   -40.61000 1.000 34.52000 ? 184 PRO A CD  1 
ATOM   1388 N N   . PHE A 1 183 ? -16.99700 3.12300   -39.01600 1.000 28.45000 ? 185 PHE A N   1 
ATOM   1389 C CA  . PHE A 1 183 ? -17.78500 2.11500   -38.33200 1.000 27.86000 ? 185 PHE A CA  1 
ATOM   1390 C C   . PHE A 1 183 ? -19.15100 2.68400   -37.98600 1.000 28.36000 ? 185 PHE A C   1 
ATOM   1391 O O   . PHE A 1 183 ? -19.35100 3.90200   -37.95900 1.000 26.21000 ? 185 PHE A O   1 
ATOM   1392 C CB  . PHE A 1 183 ? -17.06900 1.62100   -37.07400 1.000 25.98000 ? 185 PHE A CB  1 
ATOM   1393 C CG  . PHE A 1 183 ? -15.63700 1.27200   -37.32300 1.000 29.50000 ? 185 PHE A CG  1 
ATOM   1394 C CD1 . PHE A 1 183 ? -15.31400 0.21200   -38.15800 1.000 29.98000 ? 185 PHE A CD1 1 
ATOM   1395 C CD2 . PHE A 1 183 ? -14.61600 2.02300   -36.77100 1.000 32.29000 ? 185 PHE A CD2 1 
ATOM   1396 C CE1 . PHE A 1 183 ? -13.98600 -0.10600  -38.42900 1.000 32.71000 ? 185 PHE A CE1 1 
ATOM   1397 C CE2 . PHE A 1 183 ? -13.28400 1.70400   -37.02800 1.000 29.76000 ? 185 PHE A CE2 1 
ATOM   1398 C CZ  . PHE A 1 183 ? -12.97800 0.63800   -37.86200 1.000 29.29000 ? 185 PHE A CZ  1 
ATOM   1399 N N   . VAL A 1 184 ? -20.09000 1.77500   -37.73700 1.000 28.99000 ? 186 VAL A N   1 
ATOM   1400 C CA  . VAL A 1 184 ? -21.48500 2.10900   -37.47500 1.000 30.17000 ? 186 VAL A CA  1 
ATOM   1401 C C   . VAL A 1 184 ? -21.95300 1.30900   -36.26700 1.000 32.03000 ? 186 VAL A C   1 
ATOM   1402 O O   . VAL A 1 184 ? -21.42100 0.23400   -35.97000 1.000 29.19000 ? 186 VAL A O   1 
ATOM   1403 C CB  . VAL A 1 184 ? -22.36600 1.81300   -38.70500 1.000 29.61000 ? 186 VAL A CB  1 
ATOM   1404 C CG1 . VAL A 1 184 ? -22.00200 2.73300   -39.85600 1.000 29.79000 ? 186 VAL A CG1 1 
ATOM   1405 C CG2 . VAL A 1 184 ? -22.19400 0.36200   -39.11100 1.000 32.05000 ? 186 VAL A CG2 1 
ATOM   1406 N N   . ASP A 1 185 ? -22.97100 1.81900   -35.57000 1.000 29.45000 ? 187 ASP A N   1 
ATOM   1407 C CA  . ASP A 1 185 ? -23.45000 1.12600   -34.37400 1.000 28.68000 ? 187 ASP A CA  1 
ATOM   1408 C C   . ASP A 1 185 ? -24.56700 0.14900   -34.75700 1.000 32.32000 ? 187 ASP A C   1 
ATOM   1409 O O   . ASP A 1 185 ? -25.73100 0.29500   -34.38500 1.000 31.65000 ? 187 ASP A O   1 
ATOM   1410 C CB  . ASP A 1 185 ? -23.88800 2.12000   -33.30000 1.000 28.67000 ? 187 ASP A CB  1 
ATOM   1411 C CG  . ASP A 1 185 ? -24.77800 3.24800   -33.82900 1.000 25.99000 ? 187 ASP A CG  1 
ATOM   1412 O OD1 . ASP A 1 185 ? -25.02600 3.34100   -35.04800 1.000 28.85000 ? 187 ASP A OD1 1 
ATOM   1413 O OD2 . ASP A 1 185 ? -25.22900 4.05700   -32.99300 1.000 26.56000 ? 187 ASP A OD2 1 
ATOM   1414 N N   . ARG A 1 186 ? -24.17200 -0.86100  -35.53100 1.000 30.77000 ? 188 ARG A N   1 
ATOM   1415 C CA  . ARG A 1 186 ? -25.03000 -1.94600  -36.00000 1.000 38.70000 ? 188 ARG A CA  1 
ATOM   1416 C C   . ARG A 1 186 ? -24.25300 -3.24900  -35.89700 1.000 36.95000 ? 188 ARG A C   1 
ATOM   1417 O O   . ARG A 1 186 ? -23.02200 -3.26100  -36.01300 1.000 32.19000 ? 188 ARG A O   1 
ATOM   1418 C CB  . ARG A 1 186 ? -25.45800 -1.82300  -37.48900 1.000 39.41000 ? 188 ARG A CB  1 
ATOM   1419 C CG  . ARG A 1 186 ? -26.23500 -0.61000  -37.94800 1.000 39.53000 ? 188 ARG A CG  1 
ATOM   1420 C CD  . ARG A 1 186 ? -25.96800 -0.34500  -39.45700 1.000 37.92000 ? 188 ARG A CD  1 
ATOM   1421 N NE  . ARG A 1 186 ? -26.50300 -1.42700  -40.27800 1.000 39.61000 ? 188 ARG A NE  1 
ATOM   1422 C CZ  . ARG A 1 186 ? -26.23100 -1.63400  -41.56600 1.000 43.45000 ? 188 ARG A CZ  1 
ATOM   1423 N NH1 . ARG A 1 186 ? -25.40600 -0.82900  -42.22900 1.000 41.97000 ? 188 ARG A NH1 1 
ATOM   1424 N NH2 . ARG A 1 186 ? -26.80200 -2.65600  -42.20200 1.000 38.97000 ? 188 ARG A NH2 1 
ATOM   1425 N N   . GLN A 1 187 ? -24.97400 -4.35300  -35.72900 1.000 34.14000 ? 189 GLN A N   1 
ATOM   1426 C CA  . GLN A 1 187 ? -24.34700 -5.66500  -35.87300 1.000 37.13000 ? 189 GLN A CA  1 
ATOM   1427 C C   . GLN A 1 187 ? -24.09900 -5.91600  -37.35600 1.000 39.00000 ? 189 GLN A C   1 
ATOM   1428 O O   . GLN A 1 187 ? -25.04400 -6.13000  -38.11700 1.000 38.38000 ? 189 GLN A O   1 
ATOM   1429 C CB  . GLN A 1 187 ? -25.23300 -6.75300  -35.27500 1.000 38.66000 ? 189 GLN A CB  1 
ATOM   1430 C CG  . GLN A 1 187 ? -24.60900 -8.15200  -35.29600 1.000 41.16000 ? 189 GLN A CG  1 
ATOM   1431 C CD  . GLN A 1 187 ? -25.59300 -9.22600  -34.86600 1.000 41.67000 ? 189 GLN A CD  1 
ATOM   1432 O OE1 . GLN A 1 187 ? -26.37700 -9.02900  -33.94100 1.000 44.83000 ? 189 GLN A OE1 1 
ATOM   1433 N NE2 . GLN A 1 187 ? -25.56300 -10.36700 -35.54500 1.000 44.31000 ? 189 GLN A NE2 1 
ATOM   1434 N N   . THR A 1 188 ? -22.84300 -5.85000  -37.78800 1.000 38.02000 ? 190 THR A N   1 
ATOM   1435 C CA  . THR A 1 188 ? -22.51600 -6.01900  -39.20300 1.000 39.91000 ? 190 THR A CA  1 
ATOM   1436 C C   . THR A 1 188 ? -21.28600 -6.90300  -39.32200 1.000 44.21000 ? 190 THR A C   1 
ATOM   1437 O O   . THR A 1 188 ? -20.75600 -7.41200  -38.32800 1.000 41.00000 ? 190 THR A O   1 
ATOM   1438 C CB  . THR A 1 188 ? -22.24100 -4.68700  -39.91000 1.000 42.10000 ? 190 THR A CB  1 
ATOM   1439 O OG1 . THR A 1 188 ? -20.96700 -4.19200  -39.47100 1.000 45.12000 ? 190 THR A OG1 1 
ATOM   1440 C CG2 . THR A 1 188 ? -23.32100 -3.66400  -39.62400 1.000 42.28000 ? 190 THR A CG2 1 
ATOM   1441 N N   . ALA A 1 189 ? -20.81700 -7.04400  -40.55900 1.000 44.92000 ? 191 ALA A N   1 
ATOM   1442 C CA  . ALA A 1 189 ? -19.58000 -7.73600  -40.88100 1.000 45.24000 ? 191 ALA A CA  1 
ATOM   1443 C C   . ALA A 1 189 ? -18.36400 -6.82000  -40.85100 1.000 45.28000 ? 191 ALA A C   1 
ATOM   1444 O O   . ALA A 1 189 ? -17.26500 -7.26600  -41.20200 1.000 43.98000 ? 191 ALA A O   1 
ATOM   1445 C CB  . ALA A 1 189 ? -19.69400 -8.38700  -42.26400 1.000 45.18000 ? 191 ALA A CB  1 
ATOM   1446 N N   . GLN A 1 190 ? -18.53200 -5.56100  -40.44300 1.000 44.19000 ? 192 GLN A N   1 
ATOM   1447 C CA  . GLN A 1 190 ? -17.45700 -4.57800  -40.54300 1.000 36.86000 ? 192 GLN A CA  1 
ATOM   1448 C C   . GLN A 1 190 ? -16.20500 -5.05400  -39.81200 1.000 40.34000 ? 192 GLN A C   1 
ATOM   1449 O O   . GLN A 1 190 ? -16.26800 -5.78300  -38.81900 1.000 38.60000 ? 192 GLN A O   1 
ATOM   1450 C CB  . GLN A 1 190 ? -17.91600 -3.21700  -39.99500 1.000 38.92000 ? 192 GLN A CB  1 
ATOM   1451 C CG  . GLN A 1 190 ? -18.05000 -3.14400  -38.47400 1.000 38.05000 ? 192 GLN A CG  1 
ATOM   1452 C CD  . GLN A 1 190 ? -18.87900 -1.95100  -37.98100 1.000 36.76000 ? 192 GLN A CD  1 
ATOM   1453 O OE1 . GLN A 1 190 ? -18.94900 -0.90300  -38.62600 1.000 30.53000 ? 192 GLN A OE1 1 
ATOM   1454 N NE2 . GLN A 1 190 ? -19.50500 -2.11500  -36.82200 1.000 35.53000 ? 192 GLN A NE2 1 
ATOM   1455 N N   . ALA A 1 191 ? -15.05300 -4.65400  -40.33700 1.000 40.88000 ? 193 ALA A N   1 
ATOM   1456 C CA  . ALA A 1 191 ? -13.77100 -5.03400  -39.76900 1.000 39.81000 ? 193 ALA A CA  1 
ATOM   1457 C C   . ALA A 1 191 ? -12.81900 -3.85800  -39.89700 1.000 38.49000 ? 193 ALA A C   1 
ATOM   1458 O O   . ALA A 1 191 ? -12.92700 -3.05400  -40.82400 1.000 37.89000 ? 193 ALA A O   1 
ATOM   1459 C CB  . ALA A 1 191 ? -13.17300 -6.26600  -40.46700 1.000 40.47000 ? 193 ALA A CB  1 
ATOM   1460 N N   . ALA A 1 192 ? -11.88400 -3.77000  -38.96100 1.000 40.54000 ? 194 ALA A N   1 
ATOM   1461 C CA  . ALA A 1 192 ? -10.88500 -2.71400  -39.01600 1.000 39.33000 ? 194 ALA A CA  1 
ATOM   1462 C C   . ALA A 1 192 ? -9.96600  -2.91100  -40.21600 1.000 45.51000 ? 194 ALA A C   1 
ATOM   1463 O O   . ALA A 1 192 ? -9.65400  -4.04000  -40.60700 1.000 42.27000 ? 194 ALA A O   1 
ATOM   1464 C CB  . ALA A 1 192 ? -10.07000 -2.69100  -37.72700 1.000 42.11000 ? 194 ALA A CB  1 
ATOM   1465 N N   . GLY A 1 193 ? -9.55300  -1.79700  -40.81700 1.000 41.94000 ? 195 GLY A N   1 
ATOM   1466 C CA  . GLY A 1 193 ? -8.57900  -1.84000  -41.88500 1.000 42.73000 ? 195 GLY A CA  1 
ATOM   1467 C C   . GLY A 1 193 ? -7.20000  -2.24600  -41.38300 1.000 44.47000 ? 195 GLY A C   1 
ATOM   1468 O O   . GLY A 1 193 ? -6.94600  -2.40100  -40.18500 1.000 42.74000 ? 195 GLY A O   1 
ATOM   1469 N N   . THR A 1 194 ? -6.28900  -2.43700  -42.33700 1.000 43.17000 ? 196 THR A N   1 
ATOM   1470 C CA  . THR A 1 194 ? -4.90200  -2.72200  -41.98400 1.000 42.51000 ? 196 THR A CA  1 
ATOM   1471 C C   . THR A 1 194 ? -4.33500  -1.56100  -41.18200 1.000 37.80000 ? 196 THR A C   1 
ATOM   1472 O O   . THR A 1 194 ? -4.44600  -0.40100  -41.58500 1.000 43.27000 ? 196 THR A O   1 
ATOM   1473 C CB  . THR A 1 194 ? -4.05400  -2.95900  -43.23800 1.000 45.74000 ? 196 THR A CB  1 
ATOM   1474 O OG1 . THR A 1 194 ? -4.25100  -1.88000  -44.16500 1.000 48.96000 ? 196 THR A OG1 1 
ATOM   1475 C CG2 . THR A 1 194 ? -4.44100  -4.27300  -43.89300 1.000 43.89000 ? 196 THR A CG2 1 
ATOM   1476 N N   . ASP A 1 195 ? -3.76100  -1.87300  -40.02800 1.000 36.91000 ? 197 ASP A N   1 
ATOM   1477 C CA  . ASP A 1 195 ? -3.19500  -0.84900  -39.17000 1.000 37.37000 ? 197 ASP A CA  1 
ATOM   1478 C C   . ASP A 1 195 ? -1.72000  -0.62100  -39.50100 1.000 35.51000 ? 197 ASP A C   1 
ATOM   1479 O O   . ASP A 1 195 ? -1.07900  -1.42300  -40.18300 1.000 37.92000 ? 197 ASP A O   1 
ATOM   1480 C CB  . ASP A 1 195 ? -3.35000  -1.22500  -37.69700 1.000 33.44000 ? 197 ASP A CB  1 
ATOM   1481 C CG  . ASP A 1 195 ? -3.30500  -0.00800  -36.79100 1.000 32.62000 ? 197 ASP A CG  1 
ATOM   1482 O OD1 . ASP A 1 195 ? -3.66500  1.09100   -37.28100 1.000 33.23000 ? 197 ASP A OD1 1 
ATOM   1483 O OD2 . ASP A 1 195 ? -2.89300  -0.14300  -35.61800 1.000 31.55000 ? 197 ASP A OD2 1 
ATOM   1484 N N   . THR A 1 196 ? -1.19400  0.49700   -39.01500 1.000 31.40000 ? 198 THR A N   1 
ATOM   1485 C CA  . THR A 1 196 ? 0.20000   0.88000   -39.22300 1.000 30.51000 ? 198 THR A CA  1 
ATOM   1486 C C   . THR A 1 196 ? 0.79600   1.32000   -37.89300 1.000 27.97000 ? 198 THR A C   1 
ATOM   1487 O O   . THR A 1 196 ? 0.08200   1.58300   -36.92600 1.000 27.68000 ? 198 THR A O   1 
ATOM   1488 C CB  . THR A 1 196 ? 0.32500   2.01700   -40.24700 1.000 33.00000 ? 198 THR A CB  1 
ATOM   1489 O OG1 . THR A 1 196 ? -0.78200  2.91100   -40.09100 1.000 33.70000 ? 198 THR A OG1 1 
ATOM   1490 C CG2 . THR A 1 196 ? 0.32400   1.48400   -41.67900 1.000 33.83000 ? 198 THR A CG2 1 
ATOM   1491 N N   . THR A 1 197 ? 2.12300   1.42200   -37.84900 1.000 26.41000 ? 199 THR A N   1 
ATOM   1492 C CA  . THR A 1 197 ? 2.80900   1.90200   -36.66500 1.000 26.13000 ? 199 THR A CA  1 
ATOM   1493 C C   . THR A 1 197 ? 2.87500   3.42600   -36.70400 1.000 23.70000 ? 199 THR A C   1 
ATOM   1494 O O   . THR A 1 197 ? 3.03500   4.01800   -37.77300 1.000 25.31000 ? 199 THR A O   1 
ATOM   1495 C CB  . THR A 1 197 ? 4.20600   1.27400   -36.59100 1.000 26.32000 ? 199 THR A CB  1 
ATOM   1496 O OG1 . THR A 1 197 ? 4.05300   -0.15000  -36.51500 1.000 28.10000 ? 199 THR A OG1 1 
ATOM   1497 C CG2 . THR A 1 197 ? 4.96000   1.75000   -35.37500 1.000 25.49000 ? 199 THR A CG2 1 
ATOM   1498 N N   . ILE A 1 198 ? 2.72100   4.05800   -35.54000 1.000 22.61000 ? 200 ILE A N   1 
ATOM   1499 C CA  . ILE A 1 198 ? 2.64800   5.53100   -35.44700 1.000 24.51000 ? 200 ILE A CA  1 
ATOM   1500 C C   . ILE A 1 198 ? 4.07900   6.05800   -35.36400 1.000 25.25000 ? 200 ILE A C   1 
ATOM   1501 O O   . ILE A 1 198 ? 4.64100   6.22000   -34.28100 1.000 23.87000 ? 200 ILE A O   1 
ATOM   1502 C CB  . ILE A 1 198 ? 1.80700   5.99500   -34.26100 1.000 25.94000 ? 200 ILE A CB  1 
ATOM   1503 C CG1 . ILE A 1 198 ? 0.41200   5.36100   -34.29200 1.000 25.79000 ? 200 ILE A CG1 1 
ATOM   1504 C CG2 . ILE A 1 198 ? 1.67700   7.52900   -34.26700 1.000 26.92000 ? 200 ILE A CG2 1 
ATOM   1505 C CD1 . ILE A 1 198 ? -0.28500  5.46700   -32.94400 1.000 26.91000 ? 200 ILE A CD1 1 
ATOM   1506 N N   . THR A 1 199 ? 4.63600   6.40300   -36.53000 1.000 24.72000 ? 201 THR A N   1 
ATOM   1507 C CA  . THR A 1 199 ? 6.06400   6.71600   -36.64700 1.000 25.21000 ? 201 THR A CA  1 
ATOM   1508 C C   . THR A 1 199 ? 6.47800   7.87100   -35.74300 1.000 25.29000 ? 201 THR A C   1 
ATOM   1509 O O   . THR A 1 199 ? 7.53100   7.81400   -35.09000 1.000 25.05000 ? 201 THR A O   1 
ATOM   1510 C CB  . THR A 1 199 ? 6.38300   7.04100   -38.10700 1.000 25.43000 ? 201 THR A CB  1 
ATOM   1511 O OG1 . THR A 1 199 ? 5.85500   5.99900   -38.93300 1.000 27.84000 ? 201 THR A OG1 1 
ATOM   1512 C CG2 . THR A 1 199 ? 7.89900   7.16100   -38.33500 1.000 23.21000 ? 201 THR A CG2 1 
ATOM   1513 N N   . VAL A 1 200 ? 5.68800   8.94700   -35.71800 1.000 23.20000 ? 202 VAL A N   1 
ATOM   1514 C CA  . VAL A 1 200 ? 6.08500   10.11200  -34.93600 1.000 23.68000 ? 202 VAL A CA  1 
ATOM   1515 C C   . VAL A 1 200 ? 6.16800   9.76300   -33.45600 1.000 24.92000 ? 202 VAL A C   1 
ATOM   1516 O O   . VAL A 1 200 ? 7.03600   10.27900  -32.73400 1.000 23.21000 ? 202 VAL A O   1 
ATOM   1517 C CB  . VAL A 1 200 ? 5.13900   11.30100  -35.21700 1.000 24.01000 ? 202 VAL A CB  1 
ATOM   1518 C CG1 . VAL A 1 200 ? 3.73600   11.03800  -34.66100 1.000 26.67000 ? 202 VAL A CG1 1 
ATOM   1519 C CG2 . VAL A 1 200 ? 5.70800   12.57900  -34.62700 1.000 24.72000 ? 202 VAL A CG2 1 
ATOM   1520 N N   . ASN A 1 201 ? 5.31600   8.84000   -32.98900 1.000 24.20000 ? 203 ASN A N   1 
ATOM   1521 C CA  . ASN A 1 201 ? 5.36300   8.41800   -31.59400 1.000 23.61000 ? 203 ASN A CA  1 
ATOM   1522 C C   . ASN A 1 201 ? 6.58700   7.55000   -31.30800 1.000 23.80000 ? 203 ASN A C   1 
ATOM   1523 O O   . ASN A 1 201 ? 7.18900   7.67100   -30.23700 1.000 21.85000 ? 203 ASN A O   1 
ATOM   1524 C CB  . ASN A 1 201 ? 4.07800   7.66500   -31.22400 1.000 24.79000 ? 203 ASN A CB  1 
ATOM   1525 C CG  . ASN A 1 201 ? 2.87000   8.57700   -31.11900 1.000 23.82000 ? 203 ASN A CG  1 
ATOM   1526 O OD1 . ASN A 1 201 ? 2.96400   9.79300   -31.30400 1.000 22.55000 ? 203 ASN A OD1 1 
ATOM   1527 N ND2 . ASN A 1 201 ? 1.71500   7.98700   -30.82000 1.000 24.21000 ? 203 ASN A ND2 1 
ATOM   1528 N N   . VAL A 1 202 ? 6.95300   6.64700   -32.22800 1.000 22.64000 ? 204 VAL A N   1 
ATOM   1529 C CA  . VAL A 1 202 ? 8.16400   5.84600   -32.01800 1.000 23.99000 ? 204 VAL A CA  1 
ATOM   1530 C C   . VAL A 1 202 ? 9.38100   6.75300   -31.88400 1.000 24.36000 ? 204 VAL A C   1 
ATOM   1531 O O   . VAL A 1 202 ? 10.25300  6.53300   -31.03200 1.000 25.11000 ? 204 VAL A O   1 
ATOM   1532 C CB  . VAL A 1 202 ? 8.34600   4.82100   -33.15700 1.000 23.80000 ? 204 VAL A CB  1 
ATOM   1533 C CG1 . VAL A 1 202 ? 9.68200   4.04000   -33.00500 1.000 25.68000 ? 204 VAL A CG1 1 
ATOM   1534 C CG2 . VAL A 1 202 ? 7.15900   3.87000   -33.23000 1.000 24.30000 ? 204 VAL A CG2 1 
ATOM   1535 N N   . LEU A 1 203 ? 9.45900   7.78600   -32.72600 1.000 24.59000 ? 205 LEU A N   1 
ATOM   1536 C CA  . LEU A 1 203 ? 10.57700  8.72100   -32.64800 1.000 25.15000 ? 205 LEU A CA  1 
ATOM   1537 C C   . LEU A 1 203 ? 10.56200  9.48400   -31.33200 1.000 25.35000 ? 205 LEU A C   1 
ATOM   1538 O O   . LEU A 1 203 ? 11.61700  9.71800   -30.73200 1.000 23.77000 ? 205 LEU A O   1 
ATOM   1539 C CB  . LEU A 1 203 ? 10.52500  9.69100   -33.82300 1.000 22.47000 ? 205 LEU A CB  1 
ATOM   1540 C CG  . LEU A 1 203 ? 10.81000  9.04400   -35.16900 1.000 21.87000 ? 205 LEU A CG  1 
ATOM   1541 C CD1 . LEU A 1 203 ? 10.38700  10.02300  -36.22600 1.000 24.53000 ? 205 LEU A CD1 1 
ATOM   1542 C CD2 . LEU A 1 203 ? 12.32800  8.65500   -35.33000 1.000 21.14000 ? 205 LEU A CD2 1 
ATOM   1543 N N   . ALA A 1 204 ? 9.37200   9.88500   -30.86800 1.000 24.08000 ? 206 ALA A N   1 
ATOM   1544 C CA  . ALA A 1 204 ? 9.27300   10.53700  -29.56800 1.000 21.34000 ? 206 ALA A CA  1 
ATOM   1545 C C   . ALA A 1 204 ? 9.80600   9.63000   -28.46400 1.000 26.40000 ? 206 ALA A C   1 
ATOM   1546 O O   . ALA A 1 204 ? 10.55600  10.06800  -27.58100 1.000 24.92000 ? 206 ALA A O   1 
ATOM   1547 C CB  . ALA A 1 204 ? 7.81400   10.92900  -29.29300 1.000 24.32000 ? 206 ALA A CB  1 
ATOM   1548 N N   . TRP A 1 205 ? 9.45000   8.35100   -28.52300 1.000 24.25000 ? 207 TRP A N   1 
ATOM   1549 C CA  . TRP A 1 205 ? 9.86800   7.40000   -27.50300 1.000 23.96000 ? 207 TRP A CA  1 
ATOM   1550 C C   . TRP A 1 205 ? 11.37500  7.14300   -27.57300 1.000 24.04000 ? 207 TRP A C   1 
ATOM   1551 O O   . TRP A 1 205 ? 12.03700  6.99900   -26.53300 1.000 26.68000 ? 207 TRP A O   1 
ATOM   1552 C CB  . TRP A 1 205 ? 9.03600   6.13500   -27.69100 1.000 28.29000 ? 207 TRP A CB  1 
ATOM   1553 C CG  . TRP A 1 205 ? 9.38900   4.93200   -26.89700 1.000 29.76000 ? 207 TRP A CG  1 
ATOM   1554 C CD1 . TRP A 1 205 ? 9.03200   4.64900   -25.59600 1.000 32.23000 ? 207 TRP A CD1 1 
ATOM   1555 C CD2 . TRP A 1 205 ? 10.10100  3.79300   -27.37600 1.000 28.66000 ? 207 TRP A CD2 1 
ATOM   1556 N NE1 . TRP A 1 205 ? 9.51400   3.40700   -25.24200 1.000 31.20000 ? 207 TRP A NE1 1 
ATOM   1557 C CE2 . TRP A 1 205 ? 10.17000  2.86400   -26.32000 1.000 30.42000 ? 207 TRP A CE2 1 
ATOM   1558 C CE3 . TRP A 1 205 ? 10.69200  3.47100   -28.60200 1.000 30.30000 ? 207 TRP A CE3 1 
ATOM   1559 C CZ2 . TRP A 1 205 ? 10.81100  1.63300   -26.45600 1.000 33.83000 ? 207 TRP A CZ2 1 
ATOM   1560 C CZ3 . TRP A 1 205 ? 11.32200  2.25100   -28.73400 1.000 30.31000 ? 207 TRP A CZ3 1 
ATOM   1561 C CH2 . TRP A 1 205 ? 11.38400  1.35000   -27.66500 1.000 29.96000 ? 207 TRP A CH2 1 
ATOM   1562 N N   . LEU A 1 206 ? 11.94900  7.13700   -28.77900 1.000 25.09000 ? 208 LEU A N   1 
ATOM   1563 C CA  . LEU A 1 206 ? 13.41400  7.06100   -28.87800 1.000 25.69000 ? 208 LEU A CA  1 
ATOM   1564 C C   . LEU A 1 206 ? 14.07800  8.29600   -28.27000 1.000 25.17000 ? 208 LEU A C   1 
ATOM   1565 O O   . LEU A 1 206 ? 15.14300  8.19300   -27.64200 1.000 25.93000 ? 208 LEU A O   1 
ATOM   1566 C CB  . LEU A 1 206 ? 13.84600  6.88600   -30.33700 1.000 23.45000 ? 208 LEU A CB  1 
ATOM   1567 C CG  . LEU A 1 206 ? 13.53200  5.55000   -31.02100 1.000 25.26000 ? 208 LEU A CG  1 
ATOM   1568 C CD1 . LEU A 1 206 ? 14.03200  5.53500   -32.45900 1.000 24.40000 ? 208 LEU A CD1 1 
ATOM   1569 C CD2 . LEU A 1 206 ? 14.13500  4.37900   -30.25700 1.000 30.65000 ? 208 LEU A CD2 1 
ATOM   1570 N N   . TYR A 1 207 ? 13.48300  9.47800   -28.46700 1.000 25.93000 ? 209 TYR A N   1 
ATOM   1571 C CA  . TYR A 1 207 ? 13.97600  10.67600  -27.78900 1.000 26.74000 ? 209 TYR A CA  1 
ATOM   1572 C C   . TYR A 1 207 ? 13.87700  10.52900  -26.27300 1.000 29.72000 ? 209 TYR A C   1 
ATOM   1573 O O   . TYR A 1 207 ? 14.80400  10.89700  -25.53700 1.000 27.58000 ? 209 TYR A O   1 
ATOM   1574 C CB  . TYR A 1 207 ? 13.20000  11.90900  -28.26700 1.000 27.77000 ? 209 TYR A CB  1 
ATOM   1575 C CG  . TYR A 1 207 ? 13.74700  12.52100  -29.54100 1.000 26.81000 ? 209 TYR A CG  1 
ATOM   1576 C CD1 . TYR A 1 207 ? 15.01500  13.09300  -29.57200 1.000 29.65000 ? 209 TYR A CD1 1 
ATOM   1577 C CD2 . TYR A 1 207 ? 12.99800  12.52500  -30.71400 1.000 26.85000 ? 209 TYR A CD2 1 
ATOM   1578 C CE1 . TYR A 1 207 ? 15.52300  13.65200  -30.73200 1.000 27.73000 ? 209 TYR A CE1 1 
ATOM   1579 C CE2 . TYR A 1 207 ? 13.50000  13.07800  -31.88300 1.000 26.52000 ? 209 TYR A CE2 1 
ATOM   1580 C CZ  . TYR A 1 207 ? 14.76500  13.63700  -31.88000 1.000 30.09000 ? 209 TYR A CZ  1 
ATOM   1581 O OH  . TYR A 1 207 ? 15.27700  14.18800  -33.03100 1.000 28.45000 ? 209 TYR A OH  1 
ATOM   1582 N N   . ALA A 1 208 ? 12.76600  9.97500   -25.78400 1.000 26.84000 ? 210 ALA A N   1 
ATOM   1583 C CA  . ALA A 1 208 ? 12.64500  9.71100   -24.35300 1.000 26.40000 ? 210 ALA A CA  1 
ATOM   1584 C C   . ALA A 1 208 ? 13.75400  8.78400   -23.87100 1.000 29.67000 ? 210 ALA A C   1 
ATOM   1585 O O   . ALA A 1 208 ? 14.30600  8.97400   -22.77900 1.000 28.29000 ? 210 ALA A O   1 
ATOM   1586 C CB  . ALA A 1 208 ? 11.27100  9.11100   -24.03900 1.000 29.37000 ? 210 ALA A CB  1 
ATOM   1587 N N   . ALA A 1 209 ? 14.08700  7.76800   -24.66800 1.000 28.97000 ? 211 ALA A N   1 
ATOM   1588 C CA  . ALA A 1 209 ? 15.15600  6.85700   -24.28500 1.000 31.00000 ? 211 ALA A CA  1 
ATOM   1589 C C   . ALA A 1 209 ? 16.47900  7.59800   -24.13900 1.000 26.85000 ? 211 ALA A C   1 
ATOM   1590 O O   . ALA A 1 209 ? 17.23000  7.35600   -23.18800 1.000 31.57000 ? 211 ALA A O   1 
ATOM   1591 C CB  . ALA A 1 209 ? 15.28500  5.72900   -25.30600 1.000 27.48000 ? 211 ALA A CB  1 
ATOM   1592 N N   . VAL A 1 210 ? 16.77500  8.51300   -25.06600 1.000 27.49000 ? 212 VAL A N   1 
ATOM   1593 C CA  . VAL A 1 210 ? 18.01900  9.28300   -24.98200 1.000 30.87000 ? 212 VAL A CA  1 
ATOM   1594 C C   . VAL A 1 210 ? 17.99800  10.18000  -23.75200 1.000 31.81000 ? 212 VAL A C   1 
ATOM   1595 O O   . VAL A 1 210 ? 18.98800  10.27400  -23.00300 1.000 29.70000 ? 212 VAL A O   1 
ATOM   1596 C CB  . VAL A 1 210 ? 18.23000  10.10300  -26.27100 1.000 32.05000 ? 212 VAL A CB  1 
ATOM   1597 C CG1 . VAL A 1 210 ? 19.43300  11.03200  -26.12400 1.000 33.85000 ? 212 VAL A CG1 1 
ATOM   1598 C CG2 . VAL A 1 210 ? 18.38900  9.18600   -27.48400 1.000 29.86000 ? 212 VAL A CG2 1 
ATOM   1599 N N   . ILE A 1 211 ? 16.86400  10.84400  -23.52300 1.000 28.05000 ? 213 ILE A N   1 
ATOM   1600 C CA  . ILE A 1 211 ? 16.69900  11.70800  -22.35700 1.000 31.48000 ? 213 ILE A CA  1 
ATOM   1601 C C   . ILE A 1 211 ? 16.99800  10.94100  -21.07700 1.000 30.26000 ? 213 ILE A C   1 
ATOM   1602 O O   . ILE A 1 211 ? 17.64200  11.46300  -20.15000 1.000 29.84000 ? 213 ILE A O   1 
ATOM   1603 C CB  . ILE A 1 211 ? 15.27600  12.30800  -22.34400 1.000 29.69000 ? 213 ILE A CB  1 
ATOM   1604 C CG1 . ILE A 1 211 ? 15.18800  13.50300  -23.30300 1.000 28.80000 ? 213 ILE A CG1 1 
ATOM   1605 C CG2 . ILE A 1 211 ? 14.88300  12.71100  -20.92800 1.000 32.18000 ? 213 ILE A CG2 1 
ATOM   1606 C CD1 . ILE A 1 211 ? 13.76600  13.89600  -23.69100 1.000 34.55000 ? 213 ILE A CD1 1 
ATOM   1607 N N   . ASN A 1 212 ? 16.54800  9.69000   -21.00000 1.000 28.36000 ? 214 ASN A N   1 
ATOM   1608 C CA  . ASN A 1 212 ? 16.77500  8.87400   -19.81700 1.000 33.13000 ? 214 ASN A CA  1 
ATOM   1609 C C   . ASN A 1 212 ? 18.09500  8.10500   -19.86000 1.000 35.78000 ? 214 ASN A C   1 
ATOM   1610 O O   . ASN A 1 212 ? 18.29700  7.20000   -19.04100 1.000 35.21000 ? 214 ASN A O   1 
ATOM   1611 C CB  . ASN A 1 212 ? 15.60400  7.92300   -19.61000 1.000 36.30000 ? 214 ASN A CB  1 
ATOM   1612 C CG  . ASN A 1 212 ? 14.39800  8.63300   -19.01200 1.000 42.71000 ? 214 ASN A CG  1 
ATOM   1613 O OD1 . ASN A 1 212 ? 14.51300  9.31100   -17.98800 1.000 47.14000 ? 214 ASN A OD1 1 
ATOM   1614 N ND2 . ASN A 1 212 ? 13.24500  8.50900   -19.66400 1.000 42.35000 ? 214 ASN A ND2 1 
ATOM   1615 N N   . GLY A 1 213 ? 18.98000  8.43700   -20.79200 1.000 32.03000 ? 215 GLY A N   1 
ATOM   1616 C CA  . GLY A 1 213 ? 20.37200  8.01700   -20.72500 1.000 33.52000 ? 215 GLY A CA  1 
ATOM   1617 C C   . GLY A 1 213 ? 20.79900  6.85100   -21.59700 1.000 37.35000 ? 215 GLY A C   1 
ATOM   1618 O O   . GLY A 1 213 ? 21.87300  6.28300   -21.34700 1.000 36.08000 ? 215 GLY A O   1 
ATOM   1619 N N   . ASP A 1 214 ? 20.01800  6.48300   -22.61200 1.000 29.89000 ? 216 ASP A N   1 
ATOM   1620 C CA  . ASP A 1 214 ? 20.31200  5.32700   -23.46000 1.000 35.63000 ? 216 ASP A CA  1 
ATOM   1621 C C   . ASP A 1 214 ? 20.56600  5.80600   -24.88700 1.000 38.57000 ? 216 ASP A C   1 
ATOM   1622 O O   . ASP A 1 214 ? 19.66000  6.35400   -25.52600 1.000 34.86000 ? 216 ASP A O   1 
ATOM   1623 C CB  . ASP A 1 214 ? 19.15600  4.31900   -23.41800 1.000 38.92000 ? 216 ASP A CB  1 
ATOM   1624 C CG  . ASP A 1 214 ? 19.62900  2.87000   -23.46800 1.000 45.17000 ? 216 ASP A CG  1 
ATOM   1625 O OD1 . ASP A 1 214 ? 20.86000  2.64600   -23.53400 1.000 49.25000 ? 216 ASP A OD1 1 
ATOM   1626 O OD2 . ASP A 1 214 ? 18.76600  1.95100   -23.44600 1.000 45.66000 ? 216 ASP A OD2 1 
ATOM   1627 N N   . ARG A 1 215 ? 21.79500  5.58800   -25.38700 1.000 32.82000 ? 217 ARG A N   1 
ATOM   1628 C CA  . ARG A 1 215 ? 22.22200  6.05900   -26.70600 1.000 32.81000 ? 217 ARG A CA  1 
ATOM   1629 C C   . ARG A 1 215 ? 22.65500  4.93400   -27.64500 1.000 28.44000 ? 217 ARG A C   1 
ATOM   1630 O O   . ARG A 1 215 ? 23.13500  5.22300   -28.74700 1.000 29.36000 ? 217 ARG A O   1 
ATOM   1631 C CB  . ARG A 1 215 ? 23.39000  7.05300   -26.57400 1.000 34.64000 ? 217 ARG A CB  1 
ATOM   1632 C CG  . ARG A 1 215 ? 23.03400  8.38300   -25.94600 1.000 33.85000 ? 217 ARG A CG  1 
ATOM   1633 C CD  . ARG A 1 215 ? 24.21500  9.32700   -25.90400 1.000 31.17000 ? 217 ARG A CD  1 
ATOM   1634 N NE  . ARG A 1 215 ? 24.81700  9.54800   -27.22400 1.000 35.05000 ? 217 ARG A NE  1 
ATOM   1635 C CZ  . ARG A 1 215 ? 24.65900  10.65400  -27.95100 1.000 35.16000 ? 217 ARG A CZ  1 
ATOM   1636 N NH1 . ARG A 1 215 ? 25.25700  10.76700  -29.12900 1.000 30.23000 ? 217 ARG A NH1 1 
ATOM   1637 N NH2 . ARG A 1 215 ? 23.88100  11.64100  -27.51000 1.000 33.65000 ? 217 ARG A NH2 1 
ATOM   1638 N N   . TRP A 1 216 ? 22.51400  3.66600   -27.24200 1.000 31.57000 ? 218 TRP A N   1 
ATOM   1639 C CA  . TRP A 1 216 ? 23.17700  2.57600   -27.96400 1.000 29.21000 ? 218 TRP A CA  1 
ATOM   1640 C C   . TRP A 1 216 ? 22.68900  2.40300   -29.39900 1.000 31.32000 ? 218 TRP A C   1 
ATOM   1641 O O   . TRP A 1 216 ? 23.42300  1.84000   -30.22700 1.000 26.17000 ? 218 TRP A O   1 
ATOM   1642 C CB  . TRP A 1 216 ? 23.00600  1.25900   -27.20900 1.000 29.82000 ? 218 TRP A CB  1 
ATOM   1643 C CG  . TRP A 1 216 ? 21.58800  0.70900   -27.12700 1.000 32.92000 ? 218 TRP A CG  1 
ATOM   1644 C CD1 . TRP A 1 216 ? 20.74300  0.78400   -26.05500 1.000 32.41000 ? 218 TRP A CD1 1 
ATOM   1645 C CD2 . TRP A 1 216 ? 20.88300  -0.02600  -28.14000 1.000 31.89000 ? 218 TRP A CD2 1 
ATOM   1646 N NE1 . TRP A 1 216 ? 19.55800  0.15300   -26.34000 1.000 34.60000 ? 218 TRP A NE1 1 
ATOM   1647 C CE2 . TRP A 1 216 ? 19.61600  -0.35100  -27.61300 1.000 35.62000 ? 218 TRP A CE2 1 
ATOM   1648 C CE3 . TRP A 1 216 ? 21.19700  -0.43500  -29.44400 1.000 31.26000 ? 218 TRP A CE3 1 
ATOM   1649 C CZ2 . TRP A 1 216 ? 18.67000  -1.06300  -28.34000 1.000 31.58000 ? 218 TRP A CZ2 1 
ATOM   1650 C CZ3 . TRP A 1 216 ? 20.25300  -1.14300  -30.16700 1.000 32.68000 ? 218 TRP A CZ3 1 
ATOM   1651 C CH2 . TRP A 1 216 ? 19.00400  -1.45100  -29.61200 1.000 36.93000 ? 218 TRP A CH2 1 
ATOM   1652 N N   . PHE A 1 217 ? 21.46700  2.84400   -29.70700 1.000 24.87000 ? 219 PHE A N   1 
ATOM   1653 C CA  . PHE A 1 217 ? 20.84500  2.65000   -31.01100 1.000 27.37000 ? 219 PHE A CA  1 
ATOM   1654 C C   . PHE A 1 217 ? 21.12900  3.77800   -31.98900 1.000 24.63000 ? 219 PHE A C   1 
ATOM   1655 O O   . PHE A 1 217 ? 20.69700  3.69700   -33.14400 1.000 27.10000 ? 219 PHE A O   1 
ATOM   1656 C CB  . PHE A 1 217 ? 19.32200  2.50900   -30.83100 1.000 25.06000 ? 219 PHE A CB  1 
ATOM   1657 C CG  . PHE A 1 217 ? 18.74400  3.56700   -29.93800 1.000 27.42000 ? 219 PHE A CG  1 
ATOM   1658 C CD1 . PHE A 1 217 ? 18.43900  4.82200   -30.44300 1.000 26.74000 ? 219 PHE A CD1 1 
ATOM   1659 C CD2 . PHE A 1 217 ? 18.56500  3.33100   -28.58700 1.000 28.00000 ? 219 PHE A CD2 1 
ATOM   1660 C CE1 . PHE A 1 217 ? 17.93400  5.81400   -29.62300 1.000 26.44000 ? 219 PHE A CE1 1 
ATOM   1661 C CE2 . PHE A 1 217 ? 18.06400  4.31300   -27.76300 1.000 28.46000 ? 219 PHE A CE2 1 
ATOM   1662 C CZ  . PHE A 1 217 ? 17.74900  5.55300   -28.27900 1.000 26.58000 ? 219 PHE A CZ  1 
ATOM   1663 N N   . LEU A 1 218 ? 21.80200  4.83900   -31.55800 1.000 25.68000 ? 220 LEU A N   1 
ATOM   1664 C CA  . LEU A 1 218 ? 22.15200  5.92200   -32.45800 1.000 24.52000 ? 220 LEU A CA  1 
ATOM   1665 C C   . LEU A 1 218 ? 23.23300  5.46600   -33.44300 1.000 29.49000 ? 220 LEU A C   1 
ATOM   1666 O O   . LEU A 1 218 ? 23.93000  4.48200   -33.21500 1.000 29.17000 ? 220 LEU A O   1 
ATOM   1667 C CB  . LEU A 1 218 ? 22.63800  7.13000   -31.66200 1.000 27.02000 ? 220 LEU A CB  1 
ATOM   1668 C CG  . LEU A 1 218 ? 21.64900  7.74000   -30.65800 1.000 27.59000 ? 220 LEU A CG  1 
ATOM   1669 C CD1 . LEU A 1 218 ? 22.22500  9.03300   -30.09800 1.000 29.99000 ? 220 LEU A CD1 1 
ATOM   1670 C CD2 . LEU A 1 218 ? 20.29000  7.98200   -31.32300 1.000 31.84000 ? 220 LEU A CD2 1 
ATOM   1671 N N   . ASN A 1 219 ? 23.35000  6.17400   -34.56900 1.000 29.12000 ? 221 ASN A N   1 
ATOM   1672 C CA  . ASN A 1 219 ? 24.40900  5.87300   -35.52700 1.000 28.89000 ? 221 ASN A CA  1 
ATOM   1673 C C   . ASN A 1 219 ? 24.88700  7.17600   -36.15100 1.000 27.49000 ? 221 ASN A C   1 
ATOM   1674 O O   . ASN A 1 219 ? 24.35800  8.25300   -35.86200 1.000 30.00000 ? 221 ASN A O   1 
ATOM   1675 C CB  . ASN A 1 219 ? 23.96700  4.82300   -36.56800 1.000 26.82000 ? 221 ASN A CB  1 
ATOM   1676 C CG  . ASN A 1 219 ? 22.92000  5.33800   -37.56500 1.000 30.14000 ? 221 ASN A CG  1 
ATOM   1677 O OD1 . ASN A 1 219 ? 22.71100  6.53800   -37.73100 1.000 28.89000 ? 221 ASN A OD1 1 
ATOM   1678 N ND2 . ASN A 1 219 ? 22.25800  4.40100   -38.24100 1.000 31.80000 ? 221 ASN A ND2 1 
ATOM   1679 N N   . ARG A 1 220 ? 25.91200  7.07800   -37.00300 1.000 27.13000 ? 222 ARG A N   1 
ATOM   1680 C CA  . ARG A 1 220 ? 26.58600  8.24900   -37.54700 1.000 25.84000 ? 222 ARG A CA  1 
ATOM   1681 C C   . ARG A 1 220 ? 25.92100  8.77900   -38.80100 1.000 28.31000 ? 222 ARG A C   1 
ATOM   1682 O O   . ARG A 1 220 ? 26.43600  9.72300   -39.40700 1.000 29.44000 ? 222 ARG A O   1 
ATOM   1683 C CB  . ARG A 1 220 ? 28.07000  7.92000   -37.82900 1.000 31.38000 ? 222 ARG A CB  1 
ATOM   1684 C CG  . ARG A 1 220 ? 28.28200  6.98900   -39.02100 1.000 29.87000 ? 222 ARG A CG  1 
ATOM   1685 C CD  . ARG A 1 220 ? 29.79200  6.68900   -39.27600 1.000 33.95000 ? 222 ARG A CD  1 
ATOM   1686 N NE  . ARG A 1 220 ? 29.96000  5.90600   -40.50100 1.000 35.27000 ? 222 ARG A NE  1 
ATOM   1687 C CZ  . ARG A 1 220 ? 30.00600  6.43100   -41.72500 1.000 38.90000 ? 222 ARG A CZ  1 
ATOM   1688 N NH1 . ARG A 1 220 ? 29.90400  7.74500   -41.89100 1.000 37.75000 ? 222 ARG A NH1 1 
ATOM   1689 N NH2 . ARG A 1 220 ? 30.13600  5.64300   -42.79000 1.000 39.11000 ? 222 ARG A NH2 1 
ATOM   1690 N N   . PHE A 1 221 ? 24.76400  8.23200   -39.17700 1.000 31.04000 ? 223 PHE A N   1 
ATOM   1691 C CA  . PHE A 1 221 ? 24.11600  8.53900   -40.43900 1.000 28.83000 ? 223 PHE A CA  1 
ATOM   1692 C C   . PHE A 1 221 ? 22.99200  9.55800   -40.27500 1.000 28.03000 ? 223 PHE A C   1 
ATOM   1693 O O   . PHE A 1 221 ? 22.46500  9.78600   -39.18000 1.000 28.20000 ? 223 PHE A O   1 
ATOM   1694 C CB  . PHE A 1 221 ? 23.54800  7.26500   -41.06500 1.000 31.11000 ? 223 PHE A CB  1 
ATOM   1695 C CG  . PHE A 1 221 ? 24.59200  6.34400   -41.58900 1.000 30.17000 ? 223 PHE A CG  1 
ATOM   1696 C CD1 . PHE A 1 221 ? 25.65300  6.83400   -42.32500 1.000 32.77000 ? 223 PHE A CD1 1 
ATOM   1697 C CD2 . PHE A 1 221 ? 24.52900  4.99000   -41.32900 1.000 33.45000 ? 223 PHE A CD2 1 
ATOM   1698 C CE1 . PHE A 1 221 ? 26.62000  5.98800   -42.80700 1.000 36.76000 ? 223 PHE A CE1 1 
ATOM   1699 C CE2 . PHE A 1 221 ? 25.49800  4.13700   -41.80700 1.000 36.57000 ? 223 PHE A CE2 1 
ATOM   1700 C CZ  . PHE A 1 221 ? 26.54800  4.63600   -42.54300 1.000 34.98000 ? 223 PHE A CZ  1 
ATOM   1701 N N   . THR A 1 222 ? 22.62700  10.16100  -41.39000 1.000 30.82000 ? 224 THR A N   1 
ATOM   1702 C CA  . THR A 1 222 ? 21.39300  10.93000  -41.50900 1.000 29.10000 ? 224 THR A CA  1 
ATOM   1703 C C   . THR A 1 222 ? 20.57600  10.35700  -42.66000 1.000 27.23000 ? 224 THR A C   1 
ATOM   1704 O O   . THR A 1 222 ? 20.95500  9.36300   -43.28600 1.000 30.43000 ? 224 THR A O   1 
ATOM   1705 C CB  . THR A 1 222 ? 21.68400  12.42500  -41.70500 1.000 29.17000 ? 224 THR A CB  1 
ATOM   1706 O OG1 . THR A 1 222 ? 20.47900  13.18400  -41.47800 1.000 33.60000 ? 224 THR A OG1 1 
ATOM   1707 C CG2 . THR A 1 222 ? 22.21900  12.69500  -43.10900 1.000 29.96000 ? 224 THR A CG2 1 
ATOM   1708 N N   . THR A 1 223 ? 19.42000  10.96400  -42.91800 1.000 30.21000 ? 225 THR A N   1 
ATOM   1709 C CA  . THR A 1 223 ? 18.54500  10.50200  -43.98600 1.000 28.94000 ? 225 THR A CA  1 
ATOM   1710 C C   . THR A 1 223 ? 17.76500  11.69900  -44.49300 1.000 26.05000 ? 225 THR A C   1 
ATOM   1711 O O   . THR A 1 223 ? 17.59900  12.68300  -43.77100 1.000 27.81000 ? 225 THR A O   1 
ATOM   1712 C CB  . THR A 1 223 ? 17.60400  9.37000   -43.51600 1.000 28.77000 ? 225 THR A CB  1 
ATOM   1713 O OG1 . THR A 1 223 ? 16.82800  8.88900   -44.62300 1.000 26.12000 ? 225 THR A OG1 1 
ATOM   1714 C CG2 . THR A 1 223 ? 16.64100  9.85000   -42.40400 1.000 25.60000 ? 225 THR A CG2 1 
ATOM   1715 N N   . THR A 1 224 ? 17.34600  11.64200  -45.75800 1.000 25.66000 ? 226 THR A N   1 
ATOM   1716 C CA  . THR A 1 224 ? 16.32700  12.58100  -46.20000 1.000 27.57000 ? 226 THR A CA  1 
ATOM   1717 C C   . THR A 1 224 ? 14.97100  12.08100  -45.71700 1.000 26.28000 ? 226 THR A C   1 
ATOM   1718 O O   . THR A 1 224 ? 14.80600  10.89900  -45.40300 1.000 24.91000 ? 226 THR A O   1 
ATOM   1719 C CB  . THR A 1 224 ? 16.30200  12.72600  -47.72500 1.000 29.83000 ? 226 THR A CB  1 
ATOM   1720 O OG1 . THR A 1 224 ? 15.75300  11.53500  -48.31300 1.000 26.17000 ? 226 THR A OG1 1 
ATOM   1721 C CG2 . THR A 1 224 ? 17.71200  12.98800  -48.30300 1.000 25.77000 ? 226 THR A CG2 1 
ATOM   1722 N N   . LEU A 1 225 ? 13.99700  12.99700  -45.65100 1.000 26.27000 ? 227 LEU A N   1 
ATOM   1723 C CA  . LEU A 1 225 ? 12.63800  12.60600  -45.28000 1.000 25.57000 ? 227 LEU A CA  1 
ATOM   1724 C C   . LEU A 1 225 ? 12.06000  11.59900  -46.26200 1.000 28.51000 ? 227 LEU A C   1 
ATOM   1725 O O   . LEU A 1 225 ? 11.40700  10.62600  -45.85700 1.000 27.45000 ? 227 LEU A O   1 
ATOM   1726 C CB  . LEU A 1 225 ? 11.73400  13.84100  -45.20500 1.000 28.84000 ? 227 LEU A CB  1 
ATOM   1727 C CG  . LEU A 1 225 ? 10.34100  13.60600  -44.61200 1.000 31.51000 ? 227 LEU A CG  1 
ATOM   1728 C CD1 . LEU A 1 225 ? 10.45800  13.01400  -43.22700 1.000 29.61000 ? 227 LEU A CD1 1 
ATOM   1729 C CD2 . LEU A 1 225 ? 9.49300   14.88800  -44.58500 1.000 33.24000 ? 227 LEU A CD2 1 
ATOM   1730 N N   . ASN A 1 226 ? 12.25600  11.82300  -47.56400 1.000 28.36000 ? 228 ASN A N   1 
ATOM   1731 C CA  . ASN A 1 226 ? 11.63900  10.91700  -48.52600 1.000 30.46000 ? 228 ASN A CA  1 
ATOM   1732 C C   . ASN A 1 226 ? 12.25300  9.52500   -48.46600 1.000 28.97000 ? 228 ASN A C   1 
ATOM   1733 O O   . ASN A 1 226 ? 11.54100  8.52200   -48.60600 1.000 24.04000 ? 228 ASN A O   1 
ATOM   1734 C CB  . ASN A 1 226 ? 11.74000  11.47000  -49.94100 1.000 30.41000 ? 228 ASN A CB  1 
ATOM   1735 C CG  . ASN A 1 226 ? 10.80400  10.75600  -50.87800 1.000 33.25000 ? 228 ASN A CG  1 
ATOM   1736 O OD1 . ASN A 1 226 ? 9.57400   10.91600  -50.78700 1.000 44.72000 ? 228 ASN A OD1 1 
ATOM   1737 N ND2 . ASN A 1 226 ? 11.35600  9.92300   -51.73900 1.000 35.61000 ? 228 ASN A ND2 1 
ATOM   1738 N N   . ASP A 1 227 ? 13.57800  9.44200   -48.27400 1.000 25.80000 ? 229 ASP A N   1 
ATOM   1739 C CA  . ASP A 1 227 ? 14.21700  8.13600   -48.15900 1.000 28.52000 ? 229 ASP A CA  1 
ATOM   1740 C C   . ASP A 1 227 ? 13.80000  7.43300   -46.87400 1.000 27.52000 ? 229 ASP A C   1 
ATOM   1741 O O   . ASP A 1 227 ? 13.64000  6.20600   -46.85500 1.000 26.14000 ? 229 ASP A O   1 
ATOM   1742 C CB  . ASP A 1 227 ? 15.74300  8.27700   -48.20900 1.000 26.63000 ? 229 ASP A CB  1 
ATOM   1743 C CG  . ASP A 1 227 ? 16.28800  8.41600   -49.62700 1.000 32.51000 ? 229 ASP A CG  1 
ATOM   1744 O OD1 . ASP A 1 227 ? 15.57000  8.14800   -50.62300 1.000 29.72000 ? 229 ASP A OD1 1 
ATOM   1745 O OD2 . ASP A 1 227 ? 17.46300  8.80300   -49.73300 1.000 32.41000 ? 229 ASP A OD2 1 
ATOM   1746 N N   . PHE A 1 228 ? 13.64600  8.18400   -45.78100 1.000 25.58000 ? 230 PHE A N   1 
ATOM   1747 C CA  . PHE A 1 228 ? 13.11100  7.57800   -44.56500 1.000 27.28000 ? 230 PHE A CA  1 
ATOM   1748 C C   . PHE A 1 228 ? 11.73600  6.96800   -44.83000 1.000 25.74000 ? 230 PHE A C   1 
ATOM   1749 O O   . PHE A 1 228 ? 11.48300  5.79800   -44.51100 1.000 23.36000 ? 230 PHE A O   1 
ATOM   1750 C CB  . PHE A 1 228 ? 13.01900  8.60700   -43.43500 1.000 23.59000 ? 230 PHE A CB  1 
ATOM   1751 C CG  . PHE A 1 228 ? 12.33700  8.06600   -42.22600 1.000 28.22000 ? 230 PHE A CG  1 
ATOM   1752 C CD1 . PHE A 1 228 ? 13.02900  7.26500   -41.33300 1.000 25.49000 ? 230 PHE A CD1 1 
ATOM   1753 C CD2 . PHE A 1 228 ? 10.97200  8.27200   -42.03200 1.000 27.32000 ? 230 PHE A CD2 1 
ATOM   1754 C CE1 . PHE A 1 228 ? 12.38100  6.72000   -40.22600 1.000 29.64000 ? 230 PHE A CE1 1 
ATOM   1755 C CE2 . PHE A 1 228 ? 10.32200  7.72100   -40.94400 1.000 28.37000 ? 230 PHE A CE2 1 
ATOM   1756 C CZ  . PHE A 1 228 ? 11.03700  6.95200   -40.03400 1.000 28.48000 ? 230 PHE A CZ  1 
ATOM   1757 N N   . ASN A 1 229 ? 10.84700  7.74200   -45.45200 1.000 26.57000 ? 231 ASN A N   1 
ATOM   1758 C CA  . ASN A 1 229 ? 9.48700   7.26800   -45.67100 1.000 24.74000 ? 231 ASN A CA  1 
ATOM   1759 C C   . ASN A 1 229 ? 9.45000   6.07300   -46.61200 1.000 26.35000 ? 231 ASN A C   1 
ATOM   1760 O O   . ASN A 1 229 ? 8.64500   5.15500   -46.41700 1.000 27.82000 ? 231 ASN A O   1 
ATOM   1761 C CB  . ASN A 1 229 ? 8.61700   8.41800   -46.17700 1.000 26.97000 ? 231 ASN A CB  1 
ATOM   1762 C CG  . ASN A 1 229 ? 8.19800   9.33200   -45.05300 1.000 29.63000 ? 231 ASN A CG  1 
ATOM   1763 O OD1 . ASN A 1 229 ? 7.89000   8.86400   -43.95100 1.000 30.60000 ? 231 ASN A OD1 1 
ATOM   1764 N ND2 . ASN A 1 229 ? 8.19200   10.63400  -45.30700 1.000 29.25000 ? 231 ASN A ND2 1 
ATOM   1765 N N   . LEU A 1 230 ? 10.32800  6.04300   -47.61900 1.000 24.46000 ? 232 LEU A N   1 
ATOM   1766 C CA  . LEU A 1 230 ? 10.35700  4.89700   -48.52600 1.000 23.93000 ? 232 LEU A CA  1 
ATOM   1767 C C   . LEU A 1 230 ? 10.74900  3.62000   -47.79300 1.000 24.99000 ? 232 LEU A C   1 
ATOM   1768 O O   . LEU A 1 230 ? 10.20500  2.54100   -48.07300 1.000 27.95000 ? 232 LEU A O   1 
ATOM   1769 C CB  . LEU A 1 230 ? 11.31300  5.16200   -49.69800 1.000 28.17000 ? 232 LEU A CB  1 
ATOM   1770 C CG  . LEU A 1 230 ? 10.85600  6.12100   -50.81100 1.000 26.27000 ? 232 LEU A CG  1 
ATOM   1771 C CD1 . LEU A 1 230 ? 12.03200  6.46200   -51.73000 1.000 30.32000 ? 232 LEU A CD1 1 
ATOM   1772 C CD2 . LEU A 1 230 ? 9.66300   5.54800   -51.58800 1.000 29.90000 ? 232 LEU A CD2 1 
ATOM   1773 N N   . VAL A 1 231 ? 11.68800  3.71500   -46.85200 1.000 27.33000 ? 233 VAL A N   1 
ATOM   1774 C CA  . VAL A 1 231 ? 12.08900  2.54200   -46.08000 1.000 24.94000 ? 233 VAL A CA  1 
ATOM   1775 C C   . VAL A 1 231 ? 11.02200  2.17500   -45.05300 1.000 24.11000 ? 233 VAL A C   1 
ATOM   1776 O O   . VAL A 1 231 ? 10.59000  1.02000   -44.96900 1.000 26.91000 ? 233 VAL A O   1 
ATOM   1777 C CB  . VAL A 1 231 ? 13.43900  2.78600   -45.39000 1.000 24.29000 ? 233 VAL A CB  1 
ATOM   1778 C CG1 . VAL A 1 231 ? 13.74700  1.62200   -44.45000 1.000 26.77000 ? 233 VAL A CG1 1 
ATOM   1779 C CG2 . VAL A 1 231 ? 14.54900  2.92800   -46.40800 1.000 26.32000 ? 233 VAL A CG2 1 
ATOM   1780 N N   . ALA A 1 232 ? 10.61600  3.14400   -44.23100 1.000 24.95000 ? 234 ALA A N   1 
ATOM   1781 C CA  . ALA A 1 232 ? 9.71200   2.85500   -43.11600 1.000 26.20000 ? 234 ALA A CA  1 
ATOM   1782 C C   . ALA A 1 232 ? 8.38700   2.26400   -43.58300 1.000 28.33000 ? 234 ALA A C   1 
ATOM   1783 O O   . ALA A 1 232 ? 7.78600   1.44100   -42.87900 1.000 26.13000 ? 234 ALA A O   1 
ATOM   1784 C CB  . ALA A 1 232 ? 9.45300   4.12800   -42.30700 1.000 29.26000 ? 234 ALA A CB  1 
ATOM   1785 N N   . MET A 1 233 ? 7.89700   2.68000   -44.74600 1.000 28.48000 ? 235 MET A N   1 
ATOM   1786 C CA  . MET A 1 233 ? 6.63800   2.13000   -45.22600 1.000 27.86000 ? 235 MET A CA  1 
ATOM   1787 C C   . MET A 1 233 ? 6.75500   0.65300   -45.57200 1.000 28.00000 ? 235 MET A C   1 
ATOM   1788 O O   . MET A 1 233 ? 5.75200   -0.05300  -45.55200 1.000 27.66000 ? 235 MET A O   1 
ATOM   1789 C CB  . MET A 1 233 ? 6.15200   2.95000   -46.41100 1.000 31.23000 ? 235 MET A CB  1 
ATOM   1790 C CG  . MET A 1 233 ? 5.75100   4.34800   -45.95600 1.000 37.29000 ? 235 MET A CG  1 
ATOM   1791 S SD  . MET A 1 233 ? 4.66300   5.23000   -47.07800 1.000 56.30000 ? 235 MET A SD  1 
ATOM   1792 C CE  . MET A 1 233 ? 5.42100   6.85200   -47.07100 1.000 38.75000 ? 235 MET A CE  1 
ATOM   1793 N N   . LYS A 1 234 ? 7.96600   0.15500   -45.82900 1.000 26.82000 ? 236 LYS A N   1 
ATOM   1794 C CA  . LYS A 1 234 ? 8.12200   -1.27900  -46.03300 1.000 26.16000 ? 236 LYS A CA  1 
ATOM   1795 C C   . LYS A 1 234 ? 8.01300   -2.07000  -44.74000 1.000 27.41000 ? 236 LYS A C   1 
ATOM   1796 O O   . LYS A 1 234 ? 7.95600   -3.30100  -44.79100 1.000 26.62000 ? 236 LYS A O   1 
ATOM   1797 C CB  . LYS A 1 234 ? 9.45400   -1.57400  -46.72600 1.000 24.82000 ? 236 LYS A CB  1 
ATOM   1798 C CG  . LYS A 1 234 ? 9.49200   -1.03700  -48.14000 1.000 29.96000 ? 236 LYS A CG  1 
ATOM   1799 C CD  . LYS A 1 234 ? 10.91200  -1.01800  -48.69200 1.000 31.61000 ? 236 LYS A CD  1 
ATOM   1800 C CE  . LYS A 1 234 ? 10.94900  -0.22100  -49.98700 1.000 31.42000 ? 236 LYS A CE  1 
ATOM   1801 N NZ  . LYS A 1 234 ? 12.35900  0.14800   -50.25100 1.000 32.48000 ? 236 LYS A NZ  1 
ATOM   1802 N N   . TYR A 1 235 ? 7.97800   -1.40400  -43.58900 1.000 24.66000 ? 237 TYR A N   1 
ATOM   1803 C CA  . TYR A 1 235 ? 7.71300   -2.06700  -42.32100 1.000 25.90000 ? 237 TYR A CA  1 
ATOM   1804 C C   . TYR A 1 235 ? 6.32800   -1.73900  -41.78200 1.000 25.68000 ? 237 TYR A C   1 
ATOM   1805 O O   . TYR A 1 235 ? 6.07600   -1.95200  -40.59300 1.000 23.69000 ? 237 TYR A O   1 
ATOM   1806 C CB  . TYR A 1 235 ? 8.75300   -1.67700  -41.27700 1.000 26.30000 ? 237 TYR A CB  1 
ATOM   1807 C CG  . TYR A 1 235 ? 10.18600  -2.02000  -41.65700 1.000 25.53000 ? 237 TYR A CG  1 
ATOM   1808 C CD1 . TYR A 1 235 ? 10.95400  -1.15700  -42.42700 1.000 27.48000 ? 237 TYR A CD1 1 
ATOM   1809 C CD2 . TYR A 1 235 ? 10.76100  -3.20700  -41.23000 1.000 26.74000 ? 237 TYR A CD2 1 
ATOM   1810 C CE1 . TYR A 1 235 ? 12.26400  -1.47700  -42.76600 1.000 25.40000 ? 237 TYR A CE1 1 
ATOM   1811 C CE2 . TYR A 1 235 ? 12.06400  -3.52500  -41.55000 1.000 25.59000 ? 237 TYR A CE2 1 
ATOM   1812 C CZ  . TYR A 1 235 ? 12.81000  -2.66300  -42.32200 1.000 29.56000 ? 237 TYR A CZ  1 
ATOM   1813 O OH  . TYR A 1 235 ? 14.11900  -2.99900  -42.62100 1.000 27.57000 ? 237 TYR A OH  1 
ATOM   1814 N N   . ASN A 1 236 ? 5.45300   -1.17900  -42.61400 1.000 27.81000 ? 238 ASN A N   1 
ATOM   1815 C CA  . ASN A 1 236 ? 4.08500   -0.81600  -42.22700 1.000 28.41000 ? 238 ASN A CA  1 
ATOM   1816 C C   . ASN A 1 236 ? 4.04800   0.33200   -41.21200 1.000 30.42000 ? 238 ASN A C   1 
ATOM   1817 O O   . ASN A 1 236 ? 3.15400   0.39400   -40.34800 1.000 27.54000 ? 238 ASN A O   1 
ATOM   1818 C CB  . ASN A 1 236 ? 3.32200   -2.03200  -41.69800 1.000 33.29000 ? 238 ASN A CB  1 
ATOM   1819 C CG  . ASN A 1 236 ? 1.92900   -2.10700  -42.25000 1.000 40.53000 ? 238 ASN A CG  1 
ATOM   1820 O OD1 . ASN A 1 236 ? 1.72600   -1.92000  -43.44900 1.000 50.55000 ? 238 ASN A OD1 1 
ATOM   1821 N ND2 . ASN A 1 236 ? 0.95300   -2.36200  -41.38400 1.000 43.95000 ? 238 ASN A ND2 1 
ATOM   1822 N N   . TYR A 1 237 ? 5.00500   1.25100   -41.33100 1.000 25.10000 ? 239 TYR A N   1 
ATOM   1823 C CA  . TYR A 1 237 ? 5.02500   2.50300   -40.58600 1.000 25.19000 ? 239 TYR A CA  1 
ATOM   1824 C C   . TYR A 1 237 ? 4.26000   3.60200   -41.31900 1.000 30.49000 ? 239 TYR A C   1 
ATOM   1825 O O   . TYR A 1 237 ? 4.30900   3.69600   -42.55100 1.000 28.01000 ? 239 TYR A O   1 
ATOM   1826 C CB  . TYR A 1 237 ? 6.47100   2.94900   -40.34700 1.000 25.95000 ? 239 TYR A CB  1 
ATOM   1827 C CG  . TYR A 1 237 ? 7.05000   2.37800   -39.09000 1.000 23.76000 ? 239 TYR A CG  1 
ATOM   1828 C CD1 . TYR A 1 237 ? 7.08300   1.00000   -38.87700 1.000 26.05000 ? 239 TYR A CD1 1 
ATOM   1829 C CD2 . TYR A 1 237 ? 7.55100   3.20500   -38.10000 1.000 23.46000 ? 239 TYR A CD2 1 
ATOM   1830 C CE1 . TYR A 1 237 ? 7.63300   0.47200   -37.70800 1.000 25.78000 ? 239 TYR A CE1 1 
ATOM   1831 C CE2 . TYR A 1 237 ? 8.09200   2.69300   -36.94600 1.000 26.13000 ? 239 TYR A CE2 1 
ATOM   1832 C CZ  . TYR A 1 237 ? 8.13100   1.33100   -36.75300 1.000 23.32000 ? 239 TYR A CZ  1 
ATOM   1833 O OH  . TYR A 1 237 ? 8.64700   0.86000   -35.57200 1.000 25.54000 ? 239 TYR A OH  1 
ATOM   1834 N N   . GLU A 1 238 ? 3.53900   4.42000   -40.54500 1.000 30.31000 ? 240 GLU A N   1 
ATOM   1835 C CA  . GLU A 1 238 ? 2.87600   5.60100   -41.08700 1.000 30.53000 ? 240 GLU A CA  1 
ATOM   1836 C C   . GLU A 1 238 ? 3.90800   6.54100   -41.70300 1.000 32.45000 ? 240 GLU A C   1 
ATOM   1837 O O   . GLU A 1 238 ? 5.01000   6.70300   -41.15300 1.000 27.86000 ? 240 GLU A O   1 
ATOM   1838 C CB  . GLU A 1 238 ? 2.11000   6.35000   -39.98300 1.000 28.43000 ? 240 GLU A CB  1 
ATOM   1839 C CG  . GLU A 1 238 ? 0.74700   5.79000   -39.67100 1.000 36.29000 ? 240 GLU A CG  1 
ATOM   1840 C CD  . GLU A 1 238 ? -0.25400  6.08100   -40.77700 1.000 39.73000 ? 240 GLU A CD  1 
ATOM   1841 O OE1 . GLU A 1 238 ? -0.56800  5.14600   -41.54800 1.000 38.41000 ? 240 GLU A OE1 1 
ATOM   1842 O OE2 . GLU A 1 238 ? -0.71500  7.24200   -40.87700 1.000 45.52000 ? 240 GLU A OE2 1 
ATOM   1843 N N   . PRO A 1 239 ? 3.59800   7.18400   -42.82700 1.000 33.15000 ? 241 PRO A N   1 
ATOM   1844 C CA  . PRO A 1 239 ? 4.51400   8.20600   -43.34000 1.000 35.18000 ? 241 PRO A CA  1 
ATOM   1845 C C   . PRO A 1 239 ? 4.70400   9.31600   -42.31700 1.000 34.11000 ? 241 PRO A C   1 
ATOM   1846 O O   . PRO A 1 239 ? 3.78100   9.67300   -41.57300 1.000 29.85000 ? 241 PRO A O   1 
ATOM   1847 C CB  . PRO A 1 239 ? 3.81900   8.71600   -44.60900 1.000 36.17000 ? 241 PRO A CB  1 
ATOM   1848 C CG  . PRO A 1 239 ? 2.43500   8.21300   -44.54800 1.000 37.26000 ? 241 PRO A CG  1 
ATOM   1849 C CD  . PRO A 1 239 ? 2.45800   6.96100   -43.73000 1.000 39.13000 ? 241 PRO A CD  1 
ATOM   1850 N N   . LEU A 1 240 ? 5.92100   9.84200   -42.27700 1.000 28.03000 ? 242 LEU A N   1 
ATOM   1851 C CA  . LEU A 1 240 ? 6.28300   10.96000  -41.42000 1.000 24.85000 ? 242 LEU A CA  1 
ATOM   1852 C C   . LEU A 1 240 ? 6.21400   12.23700  -42.24600 1.000 31.18000 ? 242 LEU A C   1 
ATOM   1853 O O   . LEU A 1 240 ? 6.79600   12.31100  -43.33300 1.000 28.55000 ? 242 LEU A O   1 
ATOM   1854 C CB  . LEU A 1 240 ? 7.68900   10.76500  -40.83900 1.000 26.74000 ? 242 LEU A CB  1 
ATOM   1855 C CG  . LEU A 1 240 ? 8.17800   11.70000  -39.72800 1.000 25.17000 ? 242 LEU A CG  1 
ATOM   1856 C CD1 . LEU A 1 240 ? 7.54800   11.36300  -38.36200 1.000 25.37000 ? 242 LEU A CD1 1 
ATOM   1857 C CD2 . LEU A 1 240 ? 9.69700   11.64300  -39.63900 1.000 26.70000 ? 242 LEU A CD2 1 
ATOM   1858 N N   . THR A 1 241 ? 5.49600   13.22800  -41.74100 1.000 28.69000 ? 243 THR A N   1 
ATOM   1859 C CA  . THR A 1 241 ? 5.25600   14.46500  -42.46600 1.000 32.28000 ? 243 THR A CA  1 
ATOM   1860 C C   . THR A 1 241 ? 6.11800   15.59000  -41.91600 1.000 30.40000 ? 243 THR A C   1 
ATOM   1861 O O   . THR A 1 241 ? 6.67500   15.50700  -40.82000 1.000 27.89000 ? 243 THR A O   1 
ATOM   1862 C CB  . THR A 1 241 ? 3.78000   14.86700  -42.36800 1.000 30.79000 ? 243 THR A CB  1 
ATOM   1863 O OG1 . THR A 1 241 ? 3.47900   15.19600  -41.00300 1.000 30.29000 ? 243 THR A OG1 1 
ATOM   1864 C CG2 . THR A 1 241 ? 2.88700   13.73500  -42.83200 1.000 28.10000 ? 243 THR A CG2 1 
ATOM   1865 N N   . GLN A 1 242 ? 6.16600   16.69000  -42.66900 1.000 31.02000 ? 244 GLN A N   1 
ATOM   1866 C CA  . GLN A 1 242 ? 6.86600   17.86200  -42.16300 1.000 34.39000 ? 244 GLN A CA  1 
ATOM   1867 C C   . GLN A 1 242 ? 6.22000   18.36700  -40.88200 1.000 31.23000 ? 244 GLN A C   1 
ATOM   1868 O O   . GLN A 1 242 ? 6.91100   18.89100  -40.00400 1.000 30.64000 ? 244 GLN A O   1 
ATOM   1869 C CB  . GLN A 1 242 ? 6.90000   18.96700  -43.22000 1.000 34.11000 ? 244 GLN A CB  1 
ATOM   1870 C CG  . GLN A 1 242 ? 7.87300   20.09700  -42.88400 1.000 37.07000 ? 244 GLN A CG  1 
ATOM   1871 C CD  . GLN A 1 242 ? 9.27400   19.60000  -42.53000 1.000 38.69000 ? 244 GLN A CD  1 
ATOM   1872 O OE1 . GLN A 1 242 ? 9.84700   18.75100  -43.22800 1.000 39.17000 ? 244 GLN A OE1 1 
ATOM   1873 N NE2 . GLN A 1 242 ? 9.83300   20.13000  -41.44600 1.000 35.34000 ? 244 GLN A NE2 1 
ATOM   1874 N N   . ASP A 1 243 ? 4.90300   18.19000  -40.74500 1.000 31.68000 ? 245 ASP A N   1 
ATOM   1875 C CA  . ASP A 1 243 ? 4.25100   18.51200  -39.48000 1.000 33.50000 ? 245 ASP A CA  1 
ATOM   1876 C C   . ASP A 1 243 ? 4.84200   17.70000  -38.33600 1.000 32.12000 ? 245 ASP A C   1 
ATOM   1877 O O   . ASP A 1 243 ? 5.11400   18.23900  -37.25700 1.000 34.61000 ? 245 ASP A O   1 
ATOM   1878 C CB  . ASP A 1 243 ? 2.74500   18.26600  -39.58600 1.000 31.67000 ? 245 ASP A CB  1 
ATOM   1879 C CG  . ASP A 1 243 ? 1.99500   19.47100  -40.12000 1.000 39.39000 ? 245 ASP A CG  1 
ATOM   1880 O OD1 . ASP A 1 243 ? 2.64400   20.37500  -40.69200 1.000 36.50000 ? 245 ASP A OD1 1 
ATOM   1881 O OD2 . ASP A 1 243 ? 0.75700   19.51300  -39.96500 1.000 39.36000 ? 245 ASP A OD2 1 
ATOM   1882 N N   . HIS A 1 244 ? 5.03600   16.39900  -38.54400 1.000 31.95000 ? 246 HIS A N   1 
ATOM   1883 C CA  . HIS A 1 244 ? 5.62700   15.57500  -37.49500 1.000 30.39000 ? 246 HIS A CA  1 
ATOM   1884 C C   . HIS A 1 244 ? 7.05800   16.01200  -37.19200 1.000 29.20000 ? 246 HIS A C   1 
ATOM   1885 O O   . HIS A 1 244 ? 7.48900   15.98600  -36.03400 1.000 28.33000 ? 246 HIS A O   1 
ATOM   1886 C CB  . HIS A 1 244 ? 5.59900   14.10200  -37.90000 1.000 28.68000 ? 246 HIS A CB  1 
ATOM   1887 C CG  . HIS A 1 244 ? 4.22200   13.54200  -38.08200 1.000 32.22000 ? 246 HIS A CG  1 
ATOM   1888 N ND1 . HIS A 1 244 ? 3.92100   12.60900  -39.05100 1.000 30.94000 ? 246 HIS A ND1 1 
ATOM   1889 C CD2 . HIS A 1 244 ? 3.06600   13.78200  -37.41900 1.000 32.90000 ? 246 HIS A CD2 1 
ATOM   1890 C CE1 . HIS A 1 244 ? 2.63900   12.30100  -38.97800 1.000 31.42000 ? 246 HIS A CE1 1 
ATOM   1891 N NE2 . HIS A 1 244 ? 2.10000   12.99400  -37.99100 1.000 30.03000 ? 246 HIS A NE2 1 
ATOM   1892 N N   . VAL A 1 245 ? 7.81000   16.40700  -38.22200 1.000 31.41000 ? 247 VAL A N   1 
ATOM   1893 C CA  . VAL A 1 245 ? 9.18400   16.85300  -38.00800 1.000 30.75000 ? 247 VAL A CA  1 
ATOM   1894 C C   . VAL A 1 245 ? 9.20600   18.12400  -37.16800 1.000 32.47000 ? 247 VAL A C   1 
ATOM   1895 O O   . VAL A 1 245 ? 10.02700  18.26500  -36.25300 1.000 30.85000 ? 247 VAL A O   1 
ATOM   1896 C CB  . VAL A 1 245 ? 9.90200   17.06000  -39.35300 1.000 30.93000 ? 247 VAL A CB  1 
ATOM   1897 C CG1 . VAL A 1 245 ? 11.27200  17.69900  -39.12500 1.000 33.15000 ? 247 VAL A CG1 1 
ATOM   1898 C CG2 . VAL A 1 245 ? 10.02600  15.74100  -40.11000 1.000 31.07000 ? 247 VAL A CG2 1 
ATOM   1899 N N   . ASP A 1 246 ? 8.30700   19.06800  -37.46200 1.000 32.41000 ? 248 ASP A N   1 
ATOM   1900 C CA  . ASP A 1 246 ? 8.20600   20.28000  -36.64700 1.000 32.45000 ? 248 ASP A CA  1 
ATOM   1901 C C   . ASP A 1 246 ? 7.83800   19.94500  -35.20400 1.000 30.58000 ? 248 ASP A C   1 
ATOM   1902 O O   . ASP A 1 246 ? 8.39300   20.52400  -34.26000 1.000 34.37000 ? 248 ASP A O   1 
ATOM   1903 C CB  . ASP A 1 246 ? 7.16300   21.23400  -37.24300 1.000 37.80000 ? 248 ASP A CB  1 
ATOM   1904 C CG  . ASP A 1 246 ? 7.52900   21.74700  -38.63900 1.000 39.34000 ? 248 ASP A CG  1 
ATOM   1905 O OD1 . ASP A 1 246 ? 8.69300   21.61900  -39.08200 1.000 35.92000 ? 248 ASP A OD1 1 
ATOM   1906 O OD2 . ASP A 1 246 ? 6.63000   22.30100  -39.30400 1.000 37.79000 ? 248 ASP A OD2 1 
ATOM   1907 N N   . ILE A 1 247 ? 6.89500   19.01400  -35.02100 1.000 33.24000 ? 249 ILE A N   1 
ATOM   1908 C CA  . ILE A 1 247 ? 6.39300   18.64800  -33.69600 1.000 32.45000 ? 249 ILE A CA  1 
ATOM   1909 C C   . ILE A 1 247 ? 7.51900   18.08500  -32.83600 1.000 34.63000 ? 249 ILE A C   1 
ATOM   1910 O O   . ILE A 1 247 ? 7.56300   18.29300  -31.61400 1.000 31.14000 ? 249 ILE A O   1 
ATOM   1911 C CB  . ILE A 1 247 ? 5.22100   17.65200  -33.84800 1.000 35.55000 ? 249 ILE A CB  1 
ATOM   1912 C CG1 . ILE A 1 247 ? 3.94100   18.39700  -34.24700 1.000 36.71000 ? 249 ILE A CG1 1 
ATOM   1913 C CG2 . ILE A 1 247 ? 5.00700   16.83200  -32.59200 1.000 36.38000 ? 249 ILE A CG2 1 
ATOM   1914 C CD1 . ILE A 1 247 ? 2.80900   17.50800  -34.81700 1.000 41.39000 ? 249 ILE A CD1 1 
ATOM   1915 N N   . LEU A 1 248 ? 8.45000   17.37200  -33.45900 1.000 30.57000 ? 250 LEU A N   1 
ATOM   1916 C CA  . LEU A 1 248 ? 9.56000   16.78200  -32.72800 1.000 30.71000 ? 250 LEU A CA  1 
ATOM   1917 C C   . LEU A 1 248 ? 10.70500  17.76400  -32.49000 1.000 32.04000 ? 250 LEU A C   1 
ATOM   1918 O O   . LEU A 1 248 ? 11.71600  17.37100  -31.90100 1.000 30.86000 ? 250 LEU A O   1 
ATOM   1919 C CB  . LEU A 1 248 ? 10.07600  15.54700  -33.47600 1.000 29.87000 ? 250 LEU A CB  1 
ATOM   1920 C CG  . LEU A 1 248 ? 9.23200   14.27500  -33.52500 1.000 26.07000 ? 250 LEU A CG  1 
ATOM   1921 C CD1 . LEU A 1 248 ? 9.72600   13.36000  -34.65500 1.000 24.31000 ? 250 LEU A CD1 1 
ATOM   1922 C CD2 . LEU A 1 248 ? 9.26100   13.54000  -32.17000 1.000 25.68000 ? 250 LEU A CD2 1 
ATOM   1923 N N   . GLY A 1 249 ? 10.57200  19.02200  -32.91300 1.000 33.57000 ? 251 GLY A N   1 
ATOM   1924 C CA  . GLY A 1 249 ? 11.62300  20.00600  -32.76700 1.000 34.75000 ? 251 GLY A CA  1 
ATOM   1925 C C   . GLY A 1 249 ? 12.11400  20.24500  -31.34500 1.000 37.33000 ? 251 GLY A C   1 
ATOM   1926 O O   . GLY A 1 249 ? 13.32200  20.34200  -31.09700 1.000 35.86000 ? 251 GLY A O   1 
ATOM   1927 N N   . PRO A 1 250 ? 11.19400  20.38300  -30.38400 1.000 38.22000 ? 252 PRO A N   1 
ATOM   1928 C CA  . PRO A 1 250 ? 11.64100  20.58600  -28.99300 1.000 37.78000 ? 252 PRO A CA  1 
ATOM   1929 C C   . PRO A 1 250 ? 12.41300  19.41200  -28.40400 1.000 36.43000 ? 252 PRO A C   1 
ATOM   1930 O O   . PRO A 1 250 ? 13.39200  19.63200  -27.67900 1.000 36.05000 ? 252 PRO A O   1 
ATOM   1931 C CB  . PRO A 1 250 ? 10.32300  20.84200  -28.25000 1.000 38.74000 ? 252 PRO A CB  1 
ATOM   1932 C CG  . PRO A 1 250 ? 9.45700   21.44400  -29.26500 1.000 32.57000 ? 252 PRO A CG  1 
ATOM   1933 C CD  . PRO A 1 250 ? 9.77100   20.73100  -30.54200 1.000 34.07000 ? 252 PRO A CD  1 
ATOM   1934 N N   . LEU A 1 251 ? 12.00500  18.17000  -28.67700 1.000 33.21000 ? 253 LEU A N   1 
ATOM   1935 C CA  . LEU A 1 251 ? 12.80800  17.03900  -28.22100 1.000 30.37000 ? 253 LEU A CA  1 
ATOM   1936 C C   . LEU A 1 251 ? 14.15500  16.97500  -28.93900 1.000 32.30000 ? 253 LEU A C   1 
ATOM   1937 O O   . LEU A 1 251 ? 15.16000  16.57300  -28.33500 1.000 30.19000 ? 253 LEU A O   1 
ATOM   1938 C CB  . LEU A 1 251 ? 12.04300  15.73500  -28.42100 1.000 28.16000 ? 253 LEU A CB  1 
ATOM   1939 C CG  . LEU A 1 251 ? 10.81900  15.55300  -27.52800 1.000 32.24000 ? 253 LEU A CG  1 
ATOM   1940 C CD1 . LEU A 1 251 ? 9.94700   14.48300  -28.12100 1.000 27.97000 ? 253 LEU A CD1 1 
ATOM   1941 C CD2 . LEU A 1 251 ? 11.24800  15.17500  -26.11200 1.000 30.60000 ? 253 LEU A CD2 1 
ATOM   1942 N N   . SER A 1 252 ? 14.20300  17.36600  -30.21400 1.000 28.67000 ? 254 SER A N   1 
ATOM   1943 C CA  . SER A 1 252 ? 15.48900  17.42900  -30.91400 1.000 31.77000 ? 254 SER A CA  1 
ATOM   1944 C C   . SER A 1 252 ? 16.42800  18.44800  -30.26900 1.000 33.71000 ? 254 SER A C   1 
ATOM   1945 O O   . SER A 1 252 ? 17.63100  18.19300  -30.11600 1.000 32.30000 ? 254 SER A O   1 
ATOM   1946 C CB  . SER A 1 252 ? 15.27000  17.77200  -32.38900 1.000 32.44000 ? 254 SER A CB  1 
ATOM   1947 O OG  . SER A 1 252 ? 16.51400  17.77500  -33.08600 1.000 35.53000 ? 254 SER A OG  1 
ATOM   1948 N N   . ALA A 1 253 ? 15.89800  19.61800  -29.90100 1.000 34.08000 ? 255 ALA A N   1 
ATOM   1949 C CA  . ALA A 1 253 ? 16.72600  20.65100  -29.29100 1.000 37.41000 ? 255 ALA A CA  1 
ATOM   1950 C C   . ALA A 1 253 ? 17.17300  20.25400  -27.89300 1.000 37.58000 ? 255 ALA A C   1 
ATOM   1951 O O   . ALA A 1 253 ? 18.30700  20.56000  -27.49300 1.000 38.59000 ? 255 ALA A O   1 
ATOM   1952 C CB  . ALA A 1 253 ? 15.96700  21.97900  -29.25600 1.000 38.25000 ? 255 ALA A CB  1 
ATOM   1953 N N   . GLN A 1 254 ? 16.31400  19.56500  -27.14200 1.000 35.20000 ? 256 GLN A N   1 
ATOM   1954 C CA  . GLN A 1 254 ? 16.68800  19.16500  -25.79000 1.000 36.11000 ? 256 GLN A CA  1 
ATOM   1955 C C   . GLN A 1 254 ? 17.80600  18.12600  -25.80500 1.000 35.59000 ? 256 GLN A C   1 
ATOM   1956 O O   . GLN A 1 254 ? 18.70900  18.17300  -24.96300 1.000 38.59000 ? 256 GLN A O   1 
ATOM   1957 C CB  . GLN A 1 254 ? 15.46800  18.63200  -25.03200 1.000 36.40000 ? 256 GLN A CB  1 
ATOM   1958 C CG  . GLN A 1 254 ? 15.79800  18.19100  -23.60100 1.000 39.14000 ? 256 GLN A CG  1 
ATOM   1959 C CD  . GLN A 1 254 ? 14.62800  17.54300  -22.89800 1.000 40.09000 ? 256 GLN A CD  1 
ATOM   1960 O OE1 . GLN A 1 254 ? 13.48000  17.76100  -23.26300 1.000 43.98000 ? 256 GLN A OE1 1 
ATOM   1961 N NE2 . GLN A 1 254 ? 14.91600  16.73900  -21.88000 1.000 40.76000 ? 256 GLN A NE2 1 
ATOM   1962 N N   . THR A 1 255 ? 17.77300  17.18300  -26.75000 1.000 32.64000 ? 257 THR A N   1 
ATOM   1963 C CA  . THR A 1 255 ? 18.76500  16.11200  -26.79600 1.000 34.58000 ? 257 THR A CA  1 
ATOM   1964 C C   . THR A 1 255 ? 19.94200  16.41300  -27.71800 1.000 30.44000 ? 257 THR A C   1 
ATOM   1965 O O   . THR A 1 255 ? 20.96800  15.71800  -27.63800 1.000 31.61000 ? 257 THR A O   1 
ATOM   1966 C CB  . THR A 1 255 ? 18.10900  14.78900  -27.23400 1.000 33.66000 ? 257 THR A CB  1 
ATOM   1967 O OG1 . THR A 1 255 ? 17.61400  14.91600  -28.57400 1.000 28.78000 ? 257 THR A OG1 1 
ATOM   1968 C CG2 . THR A 1 255 ? 16.96800  14.41900  -26.29300 1.000 34.78000 ? 257 THR A CG2 1 
ATOM   1969 N N   . GLY A 1 256 ? 19.82500  17.42200  -28.57900 1.000 31.42000 ? 258 GLY A N   1 
ATOM   1970 C CA  . GLY A 1 256 ? 20.85100  17.74000  -29.54800 1.000 35.54000 ? 258 GLY A CA  1 
ATOM   1971 C C   . GLY A 1 256 ? 20.91100  16.82300  -30.74800 1.000 37.37000 ? 258 GLY A C   1 
ATOM   1972 O O   . GLY A 1 256 ? 21.88000  16.89200  -31.51300 1.000 38.16000 ? 258 GLY A O   1 
ATOM   1973 N N   . ILE A 1 257 ? 19.91900  15.95600  -30.93100 1.000 29.30000 ? 259 ILE A N   1 
ATOM   1974 C CA  . ILE A 1 257 ? 19.90600  14.97300  -32.00800 1.000 31.60000 ? 259 ILE A CA  1 
ATOM   1975 C C   . ILE A 1 257 ? 18.89100  15.44100  -33.03900 1.000 30.77000 ? 259 ILE A C   1 
ATOM   1976 O O   . ILE A 1 257 ? 17.68800  15.50900  -32.74700 1.000 30.88000 ? 259 ILE A O   1 
ATOM   1977 C CB  . ILE A 1 257 ? 19.57000  13.57100  -31.48700 1.000 28.67000 ? 259 ILE A CB  1 
ATOM   1978 C CG1 . ILE A 1 257 ? 20.68500  13.07600  -30.55900 1.000 34.26000 ? 259 ILE A CG1 1 
ATOM   1979 C CG2 . ILE A 1 257 ? 19.35000  12.60600  -32.64400 1.000 31.01000 ? 259 ILE A CG2 1 
ATOM   1980 C CD1 . ILE A 1 257 ? 20.24200  11.96800  -29.63900 1.000 32.06000 ? 259 ILE A CD1 1 
ATOM   1981 N N   . ALA A 1 258 ? 19.37300  15.76900  -34.23900 1.000 27.52000 ? 260 ALA A N   1 
ATOM   1982 C CA  . ALA A 1 258 ? 18.50200  16.23800  -35.31100 1.000 30.69000 ? 260 ALA A CA  1 
ATOM   1983 C C   . ALA A 1 258 ? 17.41900  15.20400  -35.60500 1.000 26.84000 ? 260 ALA A C   1 
ATOM   1984 O O   . ALA A 1 258 ? 17.63600  13.99600  -35.49200 1.000 24.34000 ? 260 ALA A O   1 
ATOM   1985 C CB  . ALA A 1 258 ? 19.31500  16.51800  -36.57800 1.000 28.95000 ? 260 ALA A CB  1 
ATOM   1986 N N   . VAL A 1 259 ? 16.23500  15.68800  -35.97900 1.000 28.94000 ? 261 VAL A N   1 
ATOM   1987 C CA  . VAL A 1 259 ? 15.11300  14.77900  -36.21000 1.000 27.57000 ? 261 VAL A CA  1 
ATOM   1988 C C   . VAL A 1 259 ? 15.46400  13.74400  -37.27200 1.000 27.24000 ? 261 VAL A C   1 
ATOM   1989 O O   . VAL A 1 259 ? 15.25700  12.54000  -37.07800 1.000 26.31000 ? 261 VAL A O   1 
ATOM   1990 C CB  . VAL A 1 259 ? 13.84700  15.57000  -36.57200 1.000 28.24000 ? 261 VAL A CB  1 
ATOM   1991 C CG1 . VAL A 1 259 ? 12.73100  14.61200  -36.96600 1.000 27.59000 ? 261 VAL A CG1 1 
ATOM   1992 C CG2 . VAL A 1 259 ? 13.44400  16.45700  -35.38500 1.000 25.89000 ? 261 VAL A CG2 1 
ATOM   1993 N N   . LEU A 1 260 ? 16.04300  14.18000  -38.39100 1.000 25.93000 ? 262 LEU A N   1 
ATOM   1994 C CA  . LEU A 1 260 ? 16.39900  13.21400  -39.42800 1.000 27.84000 ? 262 LEU A CA  1 
ATOM   1995 C C   . LEU A 1 260 ? 17.56100  12.30700  -39.01900 1.000 28.80000 ? 262 LEU A C   1 
ATOM   1996 O O   . LEU A 1 260 ? 17.70500  11.21600  -39.58500 1.000 26.95000 ? 262 LEU A O   1 
ATOM   1997 C CB  . LEU A 1 260 ? 16.72300  13.94600  -40.73100 1.000 30.83000 ? 262 LEU A CB  1 
ATOM   1998 C CG  . LEU A 1 260 ? 15.50500  14.59200  -41.38900 1.000 31.14000 ? 262 LEU A CG  1 
ATOM   1999 C CD1 . LEU A 1 260 ? 15.93900  15.41700  -42.59100 1.000 35.79000 ? 262 LEU A CD1 1 
ATOM   2000 C CD2 . LEU A 1 260 ? 14.48100  13.53300  -41.79200 1.000 28.87000 ? 262 LEU A CD2 1 
ATOM   2001 N N   . ASP A 1 261 ? 18.39200  12.71800  -38.04900 1.000 28.85000 ? 263 ASP A N   1 
ATOM   2002 C CA  . ASP A 1 261 ? 19.36400  11.78100  -37.49100 1.000 26.75000 ? 263 ASP A CA  1 
ATOM   2003 C C   . ASP A 1 261 ? 18.67100  10.69900  -36.66100 1.000 26.75000 ? 263 ASP A C   1 
ATOM   2004 O O   . ASP A 1 261 ? 19.08000  9.53100   -36.68100 1.000 24.83000 ? 263 ASP A O   1 
ATOM   2005 C CB  . ASP A 1 261 ? 20.41100  12.51900  -36.64200 1.000 30.46000 ? 263 ASP A CB  1 
ATOM   2006 C CG  . ASP A 1 261 ? 21.41600  13.32700  -37.48800 1.000 32.22000 ? 263 ASP A CG  1 
ATOM   2007 O OD1 . ASP A 1 261 ? 21.34900  13.27200  -38.73300 1.000 33.58000 ? 263 ASP A OD1 1 
ATOM   2008 O OD2 . ASP A 1 261 ? 22.27700  14.02300  -36.89600 1.000 35.34000 ? 263 ASP A OD2 1 
ATOM   2009 N N   . MET A 1 262 ? 17.63100  11.06000  -35.90700 1.000 25.65000 ? 264 MET A N   1 
ATOM   2010 C CA  . MET A 1 262 ? 16.88600  10.01400  -35.21500 1.000 25.62000 ? 264 MET A CA  1 
ATOM   2011 C C   . MET A 1 262 ? 16.16300  9.10200   -36.20300 1.000 24.97000 ? 264 MET A C   1 
ATOM   2012 O O   . MET A 1 262 ? 16.04000  7.89400   -35.95600 1.000 25.61000 ? 264 MET A O   1 
ATOM   2013 C CB  . MET A 1 262 ? 15.90900  10.62900  -34.21000 1.000 24.12000 ? 264 MET A CB  1 
ATOM   2014 C CG  . MET A 1 262 ? 15.32800  9.60900   -33.22700 1.000 26.96000 ? 264 MET A CG  1 
ATOM   2015 S SD  . MET A 1 262 ? 16.54800  8.88300   -32.10100 1.000 27.40000 ? 264 MET A SD  1 
ATOM   2016 C CE  . MET A 1 262 ? 16.49800  10.06100  -30.75500 1.000 26.03000 ? 264 MET A CE  1 
ATOM   2017 N N   . CYS A 1 263 ? 15.68000  9.65300   -37.32300 1.000 26.73000 ? 265 CYS A N   1 
ATOM   2018 C CA  . CYS A 1 263 ? 15.08300  8.81700   -38.36200 1.000 25.51000 ? 265 CYS A CA  1 
ATOM   2019 C C   . CYS A 1 263 ? 16.07200  7.77800   -38.87800 1.000 24.40000 ? 265 CYS A C   1 
ATOM   2020 O O   . CYS A 1 263 ? 15.69300  6.62900   -39.15000 1.000 24.14000 ? 265 CYS A O   1 
ATOM   2021 C CB  . CYS A 1 263 ? 14.57600  9.69000   -39.51100 1.000 25.30000 ? 265 CYS A CB  1 
ATOM   2022 S SG  . CYS A 1 263 ? 13.11600  10.66900  -39.05800 1.000 25.79000 ? 265 CYS A SG  1 
ATOM   2023 N N   . ALA A 1 264 ? 17.34100  8.16600   -39.03800 1.000 22.84000 ? 266 ALA A N   1 
ATOM   2024 C CA  . ALA A 1 264 ? 18.35700  7.20700   -39.46600 1.000 21.96000 ? 266 ALA A CA  1 
ATOM   2025 C C   . ALA A 1 264 ? 18.54800  6.10400   -38.42800 1.000 22.17000 ? 266 ALA A C   1 
ATOM   2026 O O   . ALA A 1 264 ? 18.75900  4.93300   -38.78100 1.000 24.25000 ? 266 ALA A O   1 
ATOM   2027 C CB  . ALA A 1 264 ? 19.68200  7.93400   -39.73500 1.000 26.91000 ? 266 ALA A CB  1 
ATOM   2028 N N   . SER A 1 265 ? 18.48000  6.45900   -37.14200 1.000 22.28000 ? 267 SER A N   1 
ATOM   2029 C CA  . SER A 1 265 ? 18.52100  5.45400   -36.08500 1.000 27.46000 ? 267 SER A CA  1 
ATOM   2030 C C   . SER A 1 265 ? 17.35100  4.48500   -36.20700 1.000 25.27000 ? 267 SER A C   1 
ATOM   2031 O O   . SER A 1 265 ? 17.52600  3.26300   -36.12000 1.000 22.42000 ? 267 SER A O   1 
ATOM   2032 C CB  . SER A 1 265 ? 18.52800  6.13800   -34.71600 1.000 26.79000 ? 267 SER A CB  1 
ATOM   2033 O OG  . SER A 1 265 ? 18.50200  5.18300   -33.67000 1.000 31.17000 ? 267 SER A OG  1 
ATOM   2034 N N   . LEU A 1 266 ? 16.14300  5.01600   -36.42700 1.000 23.96000 ? 268 LEU A N   1 
ATOM   2035 C CA  . LEU A 1 266 ? 14.97800  4.14800   -36.54900 1.000 23.35000 ? 268 LEU A CA  1 
ATOM   2036 C C   . LEU A 1 266 ? 15.11100  3.19900   -37.73500 1.000 21.51000 ? 268 LEU A C   1 
ATOM   2037 O O   . LEU A 1 266 ? 14.78600  2.01200   -37.62400 1.000 23.51000 ? 268 LEU A O   1 
ATOM   2038 C CB  . LEU A 1 266 ? 13.70400  5.00400   -36.64400 1.000 23.66000 ? 268 LEU A CB  1 
ATOM   2039 C CG  . LEU A 1 266 ? 12.36300  4.28500   -36.78800 1.000 23.65000 ? 268 LEU A CG  1 
ATOM   2040 C CD1 . LEU A 1 266 ? 12.21500  3.16300   -35.76200 1.000 25.64000 ? 268 LEU A CD1 1 
ATOM   2041 C CD2 . LEU A 1 266 ? 11.16800  5.26100   -36.69300 1.000 25.98000 ? 268 LEU A CD2 1 
ATOM   2042 N N   . LYS A 1 267 ? 15.61200  3.69300   -38.87500 1.000 24.64000 ? 269 LYS A N   1 
ATOM   2043 C CA  . LYS A 1 267 ? 15.81000  2.82100   -40.03300 1.000 24.37000 ? 269 LYS A CA  1 
ATOM   2044 C C   . LYS A 1 267 ? 16.71000  1.65200   -39.68300 1.000 22.33000 ? 269 LYS A C   1 
ATOM   2045 O O   . LYS A 1 267 ? 16.45100  0.51200   -40.08900 1.000 23.21000 ? 269 LYS A O   1 
ATOM   2046 C CB  . LYS A 1 267 ? 16.42100  3.59600   -41.21300 1.000 25.64000 ? 269 LYS A CB  1 
ATOM   2047 C CG  . LYS A 1 267 ? 15.42400  4.31100   -42.10300 1.000 30.39000 ? 269 LYS A CG  1 
ATOM   2048 C CD  . LYS A 1 267 ? 16.10300  5.45000   -42.85700 1.000 30.82000 ? 269 LYS A CD  1 
ATOM   2049 C CE  . LYS A 1 267 ? 16.79600  4.95800   -44.11900 1.000 30.85000 ? 269 LYS A CE  1 
ATOM   2050 N NZ  . LYS A 1 267 ? 17.39500  6.12000   -44.86100 1.000 30.81000 ? 269 LYS A NZ  1 
ATOM   2051 N N   . GLU A 1 268 ? 17.78400  1.91700   -38.94100 1.000 22.25000 ? 270 GLU A N   1 
ATOM   2052 C CA  . GLU A 1 268 ? 18.70200  0.84800   -38.56600 1.000 24.84000 ? 270 GLU A CA  1 
ATOM   2053 C C   . GLU A 1 268 ? 18.07500  -0.09400  -37.54800 1.000 23.82000 ? 270 GLU A C   1 
ATOM   2054 O O   . GLU A 1 268 ? 18.30800  -1.30700  -37.59500 1.000 24.43000 ? 270 GLU A O   1 
ATOM   2055 C CB  . GLU A 1 268 ? 19.99700  1.44400   -38.02100 1.000 23.62000 ? 270 GLU A CB  1 
ATOM   2056 C CG  . GLU A 1 268 ? 21.00900  0.39700   -37.63200 1.000 30.55000 ? 270 GLU A CG  1 
ATOM   2057 C CD  . GLU A 1 268 ? 22.38600  1.00300   -37.38400 1.000 31.51000 ? 270 GLU A CD  1 
ATOM   2058 O OE1 . GLU A 1 268 ? 23.15300  1.21200   -38.36300 1.000 31.04000 ? 270 GLU A OE1 1 
ATOM   2059 O OE2 . GLU A 1 268 ? 22.69000  1.28400   -36.20700 1.000 31.70000 ? 270 GLU A OE2 1 
ATOM   2060 N N   . LEU A 1 269 ? 17.27200  0.44400   -36.62300 1.000 25.02000 ? 271 LEU A N   1 
ATOM   2061 C CA  . LEU A 1 269 ? 16.55200  -0.40600  -35.67400 1.000 24.41000 ? 271 LEU A CA  1 
ATOM   2062 C C   . LEU A 1 269 ? 15.58800  -1.34700  -36.38100 1.000 28.03000 ? 271 LEU A C   1 
ATOM   2063 O O   . LEU A 1 269 ? 15.45000  -2.51400  -35.98400 1.000 24.43000 ? 271 LEU A O   1 
ATOM   2064 C CB  . LEU A 1 269 ? 15.80700  0.45700   -34.65400 1.000 29.05000 ? 271 LEU A CB  1 
ATOM   2065 C CG  . LEU A 1 269 ? 16.69100  1.00800   -33.53100 1.000 25.82000 ? 271 LEU A CG  1 
ATOM   2066 C CD1 . LEU A 1 269 ? 15.93200  2.13800   -32.78800 1.000 26.73000 ? 271 LEU A CD1 1 
ATOM   2067 C CD2 . LEU A 1 269 ? 17.08900  -0.12300  -32.57000 1.000 26.62000 ? 271 LEU A CD2 1 
ATOM   2068 N N   . LEU A 1 270 ? 14.89200  -0.85900  -37.42100 1.000 24.85000 ? 272 LEU A N   1 
ATOM   2069 C CA  . LEU A 1 270 ? 13.99200  -1.73900  -38.16100 1.000 23.91000 ? 272 LEU A CA  1 
ATOM   2070 C C   . LEU A 1 270 ? 14.77600  -2.79100  -38.93300 1.000 25.62000 ? 272 LEU A C   1 
ATOM   2071 O O   . LEU A 1 270 ? 14.32300  -3.93600  -39.06000 1.000 24.43000 ? 272 LEU A O   1 
ATOM   2072 C CB  . LEU A 1 270 ? 13.09100  -0.93100  -39.11300 1.000 22.76000 ? 272 LEU A CB  1 
ATOM   2073 C CG  . LEU A 1 270 ? 12.16600  0.08400   -38.43900 1.000 24.28000 ? 272 LEU A CG  1 
ATOM   2074 C CD1 . LEU A 1 270 ? 11.60000  1.08400   -39.44100 1.000 26.89000 ? 272 LEU A CD1 1 
ATOM   2075 C CD2 . LEU A 1 270 ? 11.02100  -0.65100  -37.75800 1.000 28.83000 ? 272 LEU A CD2 1 
ATOM   2076 N N   . GLN A 1 271 ? 15.96700  -2.42500  -39.41300 1.000 25.38000 ? 273 GLN A N   1 
ATOM   2077 C CA  . GLN A 1 271 ? 16.81800  -3.34600  -40.16200 1.000 23.00000 ? 273 GLN A CA  1 
ATOM   2078 C C   . GLN A 1 271 ? 17.37200  -4.46200  -39.27700 1.000 25.85000 ? 273 GLN A C   1 
ATOM   2079 O O   . GLN A 1 271 ? 17.42500  -5.62600  -39.69500 1.000 25.18000 ? 273 GLN A O   1 
ATOM   2080 C CB  . GLN A 1 271 ? 17.95500  -2.53900  -40.79000 1.000 25.93000 ? 273 GLN A CB  1 
ATOM   2081 C CG  . GLN A 1 271 ? 19.03000  -3.31800  -41.49100 1.000 24.12000 ? 273 GLN A CG  1 
ATOM   2082 C CD  . GLN A 1 271 ? 20.13300  -2.38900  -41.90600 1.000 24.92000 ? 273 GLN A CD  1 
ATOM   2083 O OE1 . GLN A 1 271 ? 20.07100  -1.77000  -42.96000 1.000 26.43000 ? 273 GLN A OE1 1 
ATOM   2084 N NE2 . GLN A 1 271 ? 21.09900  -2.21100  -41.03100 1.000 26.09000 ? 273 GLN A NE2 1 
ATOM   2085 N N   . ASN A 1 272 ? 17.81700  -4.12200  -38.06200 1.000 28.02000 ? 274 ASN A N   1 
ATOM   2086 C CA  . ASN A 1 272 ? 18.60500  -5.01500  -37.21800 1.000 24.81000 ? 274 ASN A CA  1 
ATOM   2087 C C   . ASN A 1 272 ? 17.83200  -5.64100  -36.07400 1.000 33.39000 ? 274 ASN A C   1 
ATOM   2088 O O   . ASN A 1 272 ? 18.29200  -6.64900  -35.52400 1.000 32.37000 ? 274 ASN A O   1 
ATOM   2089 C CB  . ASN A 1 272 ? 19.78200  -4.26000  -36.59000 1.000 29.41000 ? 274 ASN A CB  1 
ATOM   2090 C CG  . ASN A 1 272 ? 20.73600  -3.73100  -37.61300 1.000 27.38000 ? 274 ASN A CG  1 
ATOM   2091 O OD1 . ASN A 1 272 ? 20.65200  -4.09100  -38.77700 1.000 26.96000 ? 274 ASN A OD1 1 
ATOM   2092 N ND2 . ASN A 1 272 ? 21.65200  -2.86700  -37.18500 1.000 24.83000 ? 274 ASN A ND2 1 
ATOM   2093 N N   . GLY A 1 273 ? 16.70100  -5.06400  -35.68300 1.000 30.49000 ? 275 GLY A N   1 
ATOM   2094 C CA  . GLY A 1 273 ? 16.13500  -5.52500  -34.43000 1.000 34.76000 ? 275 GLY A CA  1 
ATOM   2095 C C   . GLY A 1 273 ? 16.94700  -4.99300  -33.25300 1.000 36.53000 ? 275 GLY A C   1 
ATOM   2096 O O   . GLY A 1 273 ? 17.79800  -4.10600  -33.38700 1.000 34.46000 ? 275 GLY A O   1 
ATOM   2097 N N   . MET A 1 274 ? 16.68100  -5.56800  -32.07900 1.000 34.60000 ? 276 MET A N   1 
ATOM   2098 C CA  . MET A 1 274 ? 17.28800  -5.08900  -30.84200 1.000 38.96000 ? 276 MET A CA  1 
ATOM   2099 C C   . MET A 1 274 ? 18.58800  -5.79500  -30.48100 1.000 37.27000 ? 276 MET A C   1 
ATOM   2100 O O   . MET A 1 274 ? 19.34900  -5.27200  -29.65800 1.000 39.22000 ? 276 MET A O   1 
ATOM   2101 C CB  . MET A 1 274 ? 16.29700  -5.25200  -29.68200 1.000 38.93000 ? 276 MET A CB  1 
ATOM   2102 C CG  . MET A 1 274 ? 14.97600  -4.54100  -29.91700 1.000 44.05000 ? 276 MET A CG  1 
ATOM   2103 S SD  . MET A 1 274 ? 15.08100  -2.84900  -29.32900 1.000 46.76000 ? 276 MET A SD  1 
ATOM   2104 C CE  . MET A 1 274 ? 13.34100  -2.39400  -29.26900 1.000 36.95000 ? 276 MET A CE  1 
ATOM   2105 N N   . ASN A 1 275 ? 18.83100  -6.97500  -31.05000 1.000 40.42000 ? 277 ASN A N   1 
ATOM   2106 C CA  . ASN A 1 275 ? 19.99900  -7.80000  -30.74300 1.000 41.01000 ? 277 ASN A CA  1 
ATOM   2107 C C   . ASN A 1 275 ? 20.11700  -8.04900  -29.23900 1.000 41.12000 ? 277 ASN A C   1 
ATOM   2108 O O   . ASN A 1 275 ? 21.16000  -7.82400  -28.62300 1.000 43.21000 ? 277 ASN A O   1 
ATOM   2109 C CB  . ASN A 1 275 ? 21.27900  -7.17200  -31.30200 1.000 44.41000 ? 277 ASN A CB  1 
ATOM   2110 C CG  . ASN A 1 275 ? 21.22900  -6.99100  -32.81900 1.000 46.20000 ? 277 ASN A CG  1 
ATOM   2111 O OD1 . ASN A 1 275 ? 21.71200  -5.98800  -33.34900 1.000 46.63000 ? 277 ASN A OD1 1 
ATOM   2112 N ND2 . ASN A 1 275 ? 20.64900  -7.96500  -33.52100 1.000 43.64000 ? 277 ASN A ND2 1 
ATOM   2113 N N   . GLY A 1 276 ? 19.01800  -8.50900  -28.64600 1.000 43.46000 ? 278 GLY A N   1 
ATOM   2114 C CA  . GLY A 1 276 ? 18.99000  -8.87100  -27.24400 1.000 41.61000 ? 278 GLY A CA  1 
ATOM   2115 C C   . GLY A 1 276 ? 18.79600  -7.72700  -26.27500 1.000 40.41000 ? 278 GLY A C   1 
ATOM   2116 O O   . GLY A 1 276 ? 18.61200  -7.97900  -25.07600 1.000 39.30000 ? 278 GLY A O   1 
ATOM   2117 N N   . ARG A 1 277 ? 18.82200  -6.48600  -26.73700 1.000 37.23000 ? 279 ARG A N   1 
ATOM   2118 C CA  . ARG A 1 277 ? 18.72500  -5.34800  -25.84100 1.000 34.70000 ? 279 ARG A CA  1 
ATOM   2119 C C   . ARG A 1 277 ? 17.27700  -4.88900  -25.73400 1.000 36.55000 ? 279 ARG A C   1 
ATOM   2120 O O   . ARG A 1 277 ? 16.37900  -5.39500  -26.40900 1.000 33.21000 ? 279 ARG A O   1 
ATOM   2121 C CB  . ARG A 1 277 ? 19.62100  -4.20200  -26.31600 1.000 35.35000 ? 279 ARG A CB  1 
ATOM   2122 C CG  . ARG A 1 277 ? 21.11100  -4.52400  -26.20000 1.000 39.37000 ? 279 ARG A CG  1 
ATOM   2123 C CD  . ARG A 1 277 ? 21.95200  -3.55600  -26.99500 1.000 36.12000 ? 279 ARG A CD  1 
ATOM   2124 N NE  . ARG A 1 277 ? 21.81300  -3.78300  -28.43100 1.000 41.07000 ? 279 ARG A NE  1 
ATOM   2125 C CZ  . ARG A 1 277 ? 22.68500  -3.36800  -29.34600 1.000 45.21000 ? 279 ARG A CZ  1 
ATOM   2126 N NH1 . ARG A 1 277 ? 23.77900  -2.70100  -28.97600 1.000 41.93000 ? 279 ARG A NH1 1 
ATOM   2127 N NH2 . ARG A 1 277 ? 22.46100  -3.61700  -30.63400 1.000 44.29000 ? 279 ARG A NH2 1 
ATOM   2128 N N   . THR A 1 278 ? 17.05700  -3.93600  -24.83800 1.000 33.27000 ? 280 THR A N   1 
ATOM   2129 C CA  . THR A 1 278 ? 15.75800  -3.31900  -24.65700 1.000 35.92000 ? 280 THR A CA  1 
ATOM   2130 C C   . THR A 1 278 ? 15.93800  -1.80900  -24.67700 1.000 35.10000 ? 280 THR A C   1 
ATOM   2131 O O   . THR A 1 278 ? 17.04400  -1.28800  -24.50600 1.000 35.76000 ? 280 THR A O   1 
ATOM   2132 C CB  . THR A 1 278 ? 15.07500  -3.77100  -23.34500 1.000 38.51000 ? 280 THR A CB  1 
ATOM   2133 O OG1 . THR A 1 278 ? 15.86000  -3.35400  -22.22500 1.000 37.72000 ? 280 THR A OG1 1 
ATOM   2134 C CG2 . THR A 1 278 ? 14.90700  -5.29500  -23.30200 1.000 35.35000 ? 280 THR A CG2 1 
ATOM   2135 N N   . ILE A 1 279 ? 14.83900  -1.10700  -24.92400 1.000 32.47000 ? 281 ILE A N   1 
ATOM   2136 C CA  . ILE A 1 279 ? 14.81900  0.34700   -24.89700 1.000 32.01000 ? 281 ILE A CA  1 
ATOM   2137 C C   . ILE A 1 279 ? 13.69400  0.74700   -23.96000 1.000 34.40000 ? 281 ILE A C   1 
ATOM   2138 O O   . ILE A 1 279 ? 12.54400  0.34700   -24.17200 1.000 32.99000 ? 281 ILE A O   1 
ATOM   2139 C CB  . ILE A 1 279 ? 14.61000  0.95400   -26.29500 1.000 31.41000 ? 281 ILE A CB  1 
ATOM   2140 C CG1 . ILE A 1 279 ? 15.84800  0.75500   -27.17400 1.000 28.75000 ? 281 ILE A CG1 1 
ATOM   2141 C CG2 . ILE A 1 279 ? 14.28100  2.43500   -26.17900 1.000 32.24000 ? 281 ILE A CG2 1 
ATOM   2142 C CD1 . ILE A 1 279 ? 15.59100  1.05300   -28.66500 1.000 30.43000 ? 281 ILE A CD1 1 
ATOM   2143 N N   . LEU A 1 280 ? 14.02400  1.50400   -22.91200 1.000 33.50000 ? 282 LEU A N   1 
ATOM   2144 C CA  . LEU A 1 280 ? 13.04900  1.85100   -21.87400 1.000 39.32000 ? 282 LEU A CA  1 
ATOM   2145 C C   . LEU A 1 280 ? 12.27500  0.61300   -21.42400 1.000 36.81000 ? 282 LEU A C   1 
ATOM   2146 O O   . LEU A 1 280 ? 11.05600  0.64400   -21.23500 1.000 41.85000 ? 282 LEU A O   1 
ATOM   2147 C CB  . LEU A 1 280 ? 12.10000  2.94900   -22.35800 1.000 34.81000 ? 282 LEU A CB  1 
ATOM   2148 C CG  . LEU A 1 280 ? 12.77700  4.28500   -22.67100 1.000 31.25000 ? 282 LEU A CG  1 
ATOM   2149 C CD1 . LEU A 1 280 ? 11.84400  5.21100   -23.41500 1.000 30.34000 ? 282 LEU A CD1 1 
ATOM   2150 C CD2 . LEU A 1 280 ? 13.26500  4.94000   -21.39700 1.000 34.01000 ? 282 LEU A CD2 1 
ATOM   2151 N N   . GLY A 1 281 ? 12.99000  -0.50600  -21.31100 1.000 35.02000 ? 283 GLY A N   1 
ATOM   2152 C CA  . GLY A 1 281 ? 12.41000  -1.73500  -20.81000 1.000 38.32000 ? 283 GLY A CA  1 
ATOM   2153 C C   . GLY A 1 281 ? 11.56000  -2.52100  -21.78500 1.000 36.65000 ? 283 GLY A C   1 
ATOM   2154 O O   . GLY A 1 281 ? 10.95700  -3.52100  -21.38300 1.000 38.91000 ? 283 GLY A O   1 
ATOM   2155 N N   . SER A 1 282 ? 11.50400  -2.12900  -23.05300 1.000 33.54000 ? 284 SER A N   1 
ATOM   2156 C CA  . SER A 1 282 ? 10.70500  -2.82400  -24.04900 1.000 35.66000 ? 284 SER A CA  1 
ATOM   2157 C C   . SER A 1 282 ? 11.61100  -3.49100  -25.08000 1.000 33.36000 ? 284 SER A C   1 
ATOM   2158 O O   . SER A 1 282 ? 12.62500  -2.92100  -25.48800 1.000 31.51000 ? 284 SER A O   1 
ATOM   2159 C CB  . SER A 1 282 ? 9.74300   -1.84700  -24.73700 1.000 32.77000 ? 284 SER A CB  1 
ATOM   2160 O OG  . SER A 1 282 ? 8.91900   -2.50900  -25.68600 1.000 38.53000 ? 284 SER A OG  1 
ATOM   2161 N N   . ALA A 1 283 ? 11.23300  -4.69300  -25.51700 1.000 30.83000 ? 285 ALA A N   1 
ATOM   2162 C CA  . ALA A 1 283 ? 11.94000  -5.35100  -26.61100 1.000 36.11000 ? 285 ALA A CA  1 
ATOM   2163 C C   . ALA A 1 283 ? 11.28400  -5.10700  -27.96800 1.000 36.84000 ? 285 ALA A C   1 
ATOM   2164 O O   . ALA A 1 283 ? 11.69400  -5.71800  -28.96100 1.000 35.40000 ? 285 ALA A O   1 
ATOM   2165 C CB  . ALA A 1 283 ? 12.04600  -6.85400  -26.34500 1.000 38.70000 ? 285 ALA A CB  1 
ATOM   2166 N N   . LEU A 1 284 ? 10.26500  -4.25100  -28.02500 1.000 32.64000 ? 286 LEU A N   1 
ATOM   2167 C CA  . LEU A 1 284 ? 9.63600   -3.81900  -29.26700 1.000 32.72000 ? 286 LEU A CA  1 
ATOM   2168 C C   . LEU A 1 284 ? 9.66000   -2.29400  -29.32600 1.000 30.17000 ? 286 LEU A C   1 
ATOM   2169 O O   . LEU A 1 284 ? 9.79500   -1.62100  -28.30000 1.000 28.52000 ? 286 LEU A O   1 
ATOM   2170 C CB  . LEU A 1 284 ? 8.18900   -4.33300  -29.35700 1.000 32.33000 ? 286 LEU A CB  1 
ATOM   2171 C CG  . LEU A 1 284 ? 7.95500   -5.84100  -29.47600 1.000 37.73000 ? 286 LEU A CG  1 
ATOM   2172 C CD1 . LEU A 1 284 ? 6.45500   -6.13000  -29.50200 1.000 38.42000 ? 286 LEU A CD1 1 
ATOM   2173 C CD2 . LEU A 1 284 ? 8.61400   -6.42300  -30.71700 1.000 42.50000 ? 286 LEU A CD2 1 
ATOM   2174 N N   . LEU A 1 285 ? 9.51900   -1.74300  -30.53100 1.000 26.99000 ? 287 LEU A N   1 
ATOM   2175 C CA  . LEU A 1 285 ? 9.43600   -0.29400  -30.68700 1.000 25.59000 ? 287 LEU A CA  1 
ATOM   2176 C C   . LEU A 1 285 ? 8.03700   0.17300   -30.28100 1.000 26.19000 ? 287 LEU A C   1 
ATOM   2177 O O   . LEU A 1 285 ? 7.03900   -0.26100  -30.86200 1.000 29.19000 ? 287 LEU A O   1 
ATOM   2178 C CB  . LEU A 1 285 ? 9.74900   0.10300   -32.12500 1.000 26.84000 ? 287 LEU A CB  1 
ATOM   2179 C CG  . LEU A 1 285 ? 11.13100  -0.35700  -32.59700 1.000 29.09000 ? 287 LEU A CG  1 
ATOM   2180 C CD1 . LEU A 1 285 ? 11.34000  0.01700   -34.06000 1.000 29.17000 ? 287 LEU A CD1 1 
ATOM   2181 C CD2 . LEU A 1 285 ? 12.19800  0.24000   -31.71500 1.000 30.74000 ? 287 LEU A CD2 1 
ATOM   2182 N N   . GLU A 1 286 ? 7.97100   1.04300   -29.27700 1.000 30.72000 ? 288 GLU A N   1 
ATOM   2183 C CA  . GLU A 1 286 ? 6.71300   1.47900   -28.68100 1.000 31.33000 ? 288 GLU A CA  1 
ATOM   2184 C C   . GLU A 1 286 ? 6.15300   2.68700   -29.42300 1.000 28.74000 ? 288 GLU A C   1 
ATOM   2185 O O   . GLU A 1 286 ? 6.88400   3.64400   -29.69100 1.000 22.99000 ? 288 GLU A O   1 
ATOM   2186 C CB  . GLU A 1 286 ? 6.94400   1.82300   -27.21200 1.000 30.41000 ? 288 GLU A CB  1 
ATOM   2187 C CG  . GLU A 1 286 ? 5.72500   2.35900   -26.52300 1.000 36.47000 ? 288 GLU A CG  1 
ATOM   2188 C CD  . GLU A 1 286 ? 4.58300   1.36300   -26.53200 1.000 41.37000 ? 288 GLU A CD  1 
ATOM   2189 O OE1 . GLU A 1 286 ? 4.84700   0.17400   -26.21600 1.000 35.86000 ? 288 GLU A OE1 1 
ATOM   2190 O OE2 . GLU A 1 286 ? 3.43700   1.77400   -26.86000 1.000 35.70000 ? 288 GLU A OE2 1 
ATOM   2191 N N   . ASP A 1 287 ? 4.84700   2.66200   -29.73500 1.000 28.89000 ? 289 ASP A N   1 
ATOM   2192 C CA  . ASP A 1 287 ? 4.28500   3.75400   -30.52900 1.000 27.09000 ? 289 ASP A CA  1 
ATOM   2193 C C   . ASP A 1 287 ? 3.04900   4.40100   -29.90500 1.000 25.79000 ? 289 ASP A C   1 
ATOM   2194 O O   . ASP A 1 287 ? 2.31100   5.10700   -30.60900 1.000 25.91000 ? 289 ASP A O   1 
ATOM   2195 C CB  . ASP A 1 287 ? 3.98300   3.29400   -31.96500 1.000 28.06000 ? 289 ASP A CB  1 
ATOM   2196 C CG  . ASP A 1 287 ? 2.70000   2.48900   -32.09800 1.000 27.21000 ? 289 ASP A CG  1 
ATOM   2197 O OD1 . ASP A 1 287 ? 2.21200   1.89600   -31.10800 1.000 27.98000 ? 289 ASP A OD1 1 
ATOM   2198 O OD2 . ASP A 1 287 ? 2.19300   2.42400   -33.23700 1.000 29.00000 ? 289 ASP A OD2 1 
ATOM   2199 N N   . GLU A 1 288 ? 2.80200   4.21700   -28.60700 1.000 26.95000 ? 290 GLU A N   1 
ATOM   2200 C CA  . GLU A 1 288 ? 1.65300   4.87700   -27.98100 1.000 29.99000 ? 290 GLU A CA  1 
ATOM   2201 C C   . GLU A 1 288 ? 2.08000   5.91000   -26.92800 1.000 29.30000 ? 290 GLU A C   1 
ATOM   2202 O O   . GLU A 1 288 ? 1.33400   6.19000   -25.98000 1.000 27.29000 ? 290 GLU A O   1 
ATOM   2203 C CB  . GLU A 1 288 ? 0.67700   3.83300   -27.41400 1.000 30.77000 ? 290 GLU A CB  1 
ATOM   2204 C CG  . GLU A 1 288 ? 0.11100   2.89900   -28.53200 1.000 32.61000 ? 290 GLU A CG  1 
ATOM   2205 C CD  . GLU A 1 288 ? -1.23500  2.21800   -28.21200 1.000 35.56000 ? 290 GLU A CD  1 
ATOM   2206 O OE1 . GLU A 1 288 ? -1.86800  1.65800   -29.15600 1.000 33.81000 ? 290 GLU A OE1 1 
ATOM   2207 O OE2 . GLU A 1 288 ? -1.66000  2.22300   -27.03400 1.000 32.08000 ? 290 GLU A OE2 1 
ATOM   2208 N N   . PHE A 1 289 ? 3.27200   6.50000   -27.09300 1.000 27.93000 ? 291 PHE A N   1 
ATOM   2209 C CA  . PHE A 1 289 ? 3.67200   7.73600   -26.41500 1.000 23.62000 ? 291 PHE A CA  1 
ATOM   2210 C C   . PHE A 1 289 ? 3.85300   8.83500   -27.45300 1.000 26.94000 ? 291 PHE A C   1 
ATOM   2211 O O   . PHE A 1 289 ? 4.70500   8.71000   -28.33900 1.000 26.64000 ? 291 PHE A O   1 
ATOM   2212 C CB  . PHE A 1 289 ? 4.99100   7.59200   -25.65600 1.000 26.84000 ? 291 PHE A CB  1 
ATOM   2213 C CG  . PHE A 1 289 ? 4.97600   6.58100   -24.57400 1.000 29.77000 ? 291 PHE A CG  1 
ATOM   2214 C CD1 . PHE A 1 289 ? 4.54600   6.91700   -23.30600 1.000 31.00000 ? 291 PHE A CD1 1 
ATOM   2215 C CD2 . PHE A 1 289 ? 5.44200   5.29600   -24.81000 1.000 34.02000 ? 291 PHE A CD2 1 
ATOM   2216 C CE1 . PHE A 1 289 ? 4.54800   5.97500   -22.28700 1.000 37.57000 ? 291 PHE A CE1 1 
ATOM   2217 C CE2 . PHE A 1 289 ? 5.44800   4.33800   -23.79500 1.000 36.82000 ? 291 PHE A CE2 1 
ATOM   2218 C CZ  . PHE A 1 289 ? 5.00100   4.68100   -22.53100 1.000 36.62000 ? 291 PHE A CZ  1 
ATOM   2219 N N   . THR A 1 290 ? 3.11400   9.93600   -27.30400 1.000 25.34000 ? 292 THR A N   1 
ATOM   2220 C CA  . THR A 1 290 ? 3.26700   11.06200  -28.21700 1.000 25.92000 ? 292 THR A CA  1 
ATOM   2221 C C   . THR A 1 290 ? 4.42000   11.96600  -27.79300 1.000 26.85000 ? 292 THR A C   1 
ATOM   2222 O O   . THR A 1 290 ? 4.92000   11.87600  -26.66400 1.000 26.00000 ? 292 THR A O   1 
ATOM   2223 C CB  . THR A 1 290 ? 1.98500   11.88400  -28.26300 1.000 28.72000 ? 292 THR A CB  1 
ATOM   2224 O OG1 . THR A 1 290 ? 1.83700   12.57800  -27.02000 1.000 28.95000 ? 292 THR A OG1 1 
ATOM   2225 C CG2 . THR A 1 290 ? 0.78200   10.99300  -28.50900 1.000 24.94000 ? 292 THR A CG2 1 
ATOM   2226 N N   . PRO A 1 291 ? 4.85000   12.86800  -28.68200 1.000 26.16000 ? 293 PRO A N   1 
ATOM   2227 C CA  . PRO A 1 291 ? 5.83400   13.88700  -28.26800 1.000 29.37000 ? 293 PRO A CA  1 
ATOM   2228 C C   . PRO A 1 291 ? 5.38800   14.68900  -27.05700 1.000 30.07000 ? 293 PRO A C   1 
ATOM   2229 O O   . PRO A 1 291 ? 6.20500   15.02100  -26.19000 1.000 29.47000 ? 293 PRO A O   1 
ATOM   2230 C CB  . PRO A 1 291 ? 5.95500   14.76300  -29.52500 1.000 26.36000 ? 293 PRO A CB  1 
ATOM   2231 C CG  . PRO A 1 291 ? 5.69600   13.82000  -30.65300 1.000 24.98000 ? 293 PRO A CG  1 
ATOM   2232 C CD  . PRO A 1 291 ? 4.60500   12.89900  -30.13800 1.000 26.33000 ? 293 PRO A CD  1 
ATOM   2233 N N   . PHE A 1 292 ? 4.09700   15.00800  -26.97800 1.000 28.69000 ? 294 PHE A N   1 
ATOM   2234 C CA  . PHE A 1 292 ? 3.54800   15.67100  -25.79700 1.000 30.10000 ? 294 PHE A CA  1 
ATOM   2235 C C   . PHE A 1 292 ? 3.68300   14.79600  -24.55000 1.000 28.45000 ? 294 PHE A C   1 
ATOM   2236 O O   . PHE A 1 292 ? 4.05200   15.28500  -23.47900 1.000 31.39000 ? 294 PHE A O   1 
ATOM   2237 C CB  . PHE A 1 292 ? 2.08400   16.01600  -26.07500 1.000 30.99000 ? 294 PHE A CB  1 
ATOM   2238 C CG  . PHE A 1 292 ? 1.50400   17.08900  -25.18800 1.000 39.10000 ? 294 PHE A CG  1 
ATOM   2239 C CD1 . PHE A 1 292 ? 0.91300   16.76300  -23.97000 1.000 37.83000 ? 294 PHE A CD1 1 
ATOM   2240 C CD2 . PHE A 1 292 ? 1.46900   18.41400  -25.61000 1.000 40.23000 ? 294 PHE A CD2 1 
ATOM   2241 C CE1 . PHE A 1 292 ? 0.34900   17.75300  -23.16200 1.000 37.34000 ? 294 PHE A CE1 1 
ATOM   2242 C CE2 . PHE A 1 292 ? 0.89500   19.40500  -24.81300 1.000 39.93000 ? 294 PHE A CE2 1 
ATOM   2243 C CZ  . PHE A 1 292 ? 0.33900   19.07100  -23.58600 1.000 36.23000 ? 294 PHE A CZ  1 
ATOM   2244 N N   . ASP A 1 293 ? 3.38800   13.49700  -24.67100 1.000 26.49000 ? 295 ASP A N   1 
ATOM   2245 C CA  . ASP A 1 293 ? 3.47300   12.59000  -23.52500 1.000 25.99000 ? 295 ASP A CA  1 
ATOM   2246 C C   . ASP A 1 293 ? 4.89000   12.49800  -22.98300 1.000 32.22000 ? 295 ASP A C   1 
ATOM   2247 O O   . ASP A 1 293 ? 5.09500   12.37800  -21.76800 1.000 30.13000 ? 295 ASP A O   1 
ATOM   2248 C CB  . ASP A 1 293 ? 3.03100   11.18700  -23.91800 1.000 26.88000 ? 295 ASP A CB  1 
ATOM   2249 C CG  . ASP A 1 293 ? 1.57000   11.09900  -24.24200 1.000 30.13000 ? 295 ASP A CG  1 
ATOM   2250 O OD1 . ASP A 1 293 ? 0.81200   12.00200  -23.83200 1.000 32.79000 ? 295 ASP A OD1 1 
ATOM   2251 O OD2 . ASP A 1 293 ? 1.19800   10.11700  -24.92300 1.000 26.26000 ? 295 ASP A OD2 1 
ATOM   2252 N N   . VAL A 1 294 ? 5.87600   12.47300  -23.88100 1.000 29.01000 ? 296 VAL A N   1 
ATOM   2253 C CA  . VAL A 1 294 ? 7.26800   12.37000  -23.46000 1.000 29.48000 ? 296 VAL A CA  1 
ATOM   2254 C C   . VAL A 1 294 ? 7.66500   13.59800  -22.65700 1.000 31.93000 ? 296 VAL A C   1 
ATOM   2255 O O   . VAL A 1 294 ? 8.26800   13.48800  -21.58300 1.000 35.25000 ? 296 VAL A O   1 
ATOM   2256 C CB  . VAL A 1 294 ? 8.17000   12.15900  -24.68900 1.000 31.24000 ? 296 VAL A CB  1 
ATOM   2257 C CG1 . VAL A 1 294 ? 9.63300   12.34900  -24.32600 1.000 30.88000 ? 296 VAL A CG1 1 
ATOM   2258 C CG2 . VAL A 1 294 ? 7.93100   10.77100  -25.26900 1.000 27.53000 ? 296 VAL A CG2 1 
ATOM   2259 N N   . VAL A 1 295 ? 7.30200   14.78600  -23.14300 1.000 32.05000 ? 297 VAL A N   1 
ATOM   2260 C CA  . VAL A 1 295 ? 7.60500   16.01200  -22.40700 1.000 37.10000 ? 297 VAL A CA  1 
ATOM   2261 C C   . VAL A 1 295 ? 6.89600   16.02500  -21.05300 1.000 39.62000 ? 297 VAL A C   1 
ATOM   2262 O O   . VAL A 1 295 ? 7.47800   16.43900  -20.04000 1.000 40.94000 ? 297 VAL A O   1 
ATOM   2263 C CB  . VAL A 1 295 ? 7.25300   17.23900  -23.26600 1.000 37.62000 ? 297 VAL A CB  1 
ATOM   2264 C CG1 . VAL A 1 295 ? 7.34600   18.51200  -22.45000 1.000 38.41000 ? 297 VAL A CG1 1 
ATOM   2265 C CG2 . VAL A 1 295 ? 8.20300   17.31300  -24.47600 1.000 35.41000 ? 297 VAL A CG2 1 
ATOM   2266 N N   . ARG A 1 296 ? 5.64500   15.54400  -21.00200 1.000 37.17000 ? 298 ARG A N   1 
ATOM   2267 C CA  . ARG A 1 296 ? 4.92600   15.45700  -19.72800 1.000 38.14000 ? 298 ARG A CA  1 
ATOM   2268 C C   . ARG A 1 296 ? 5.66600   14.57200  -18.72300 1.000 40.92000 ? 298 ARG A C   1 
ATOM   2269 O O   . ARG A 1 296 ? 5.83600   14.94500  -17.55600 1.000 42.85000 ? 298 ARG A O   1 
ATOM   2270 C CB  . ARG A 1 296 ? 3.49400   14.93600  -19.95200 1.000 39.03000 ? 298 ARG A CB  1 
ATOM   2271 C CG  . ARG A 1 296 ? 2.85700   14.28200  -18.70800 1.000 38.83000 ? 298 ARG A CG  1 
ATOM   2272 C CD  . ARG A 1 296 ? 1.33100   14.05200  -18.83500 1.000 42.49000 ? 298 ARG A CD  1 
ATOM   2273 N NE  . ARG A 1 296 ? 0.81600   13.35300  -17.65300 1.000 40.75000 ? 298 ARG A NE  1 
ATOM   2274 C CZ  . ARG A 1 296 ? 0.19700   12.17300  -17.67900 1.000 36.03000 ? 298 ARG A CZ  1 
ATOM   2275 N NH1 . ARG A 1 296 ? -0.21100  11.61500  -16.54900 1.000 32.64000 ? 298 ARG A NH1 1 
ATOM   2276 N NH2 . ARG A 1 296 ? -0.01000  11.54500  -18.83100 1.000 40.37000 ? 298 ARG A NH2 1 
ATOM   2277 N N   . GLN A 1 297 ? 6.12400   13.39300  -19.15900 1.000 37.14000 ? 299 GLN A N   1 
ATOM   2278 C CA  . GLN A 1 297 ? 6.64300   12.41000  -18.21100 1.000 35.86000 ? 299 GLN A CA  1 
ATOM   2279 C C   . GLN A 1 297 ? 8.11300   12.63700  -17.86600 1.000 41.30000 ? 299 GLN A C   1 
ATOM   2280 O O   . GLN A 1 297 ? 8.54200   12.27800  -16.76100 1.000 38.96000 ? 299 GLN A O   1 
ATOM   2281 C CB  . GLN A 1 297 ? 6.45100   10.98700  -18.75400 1.000 39.86000 ? 299 GLN A CB  1 
ATOM   2282 C CG  . GLN A 1 297 ? 6.93900   9.90600   -17.79200 1.000 39.81000 ? 299 GLN A CG  1 
ATOM   2283 C CD  . GLN A 1 297 ? 6.46400   8.50600   -18.12400 1.000 40.99000 ? 299 GLN A CD  1 
ATOM   2284 O OE1 . GLN A 1 297 ? 6.99600   7.52400   -17.59400 1.000 40.60000 ? 299 GLN A OE1 1 
ATOM   2285 N NE2 . GLN A 1 297 ? 5.45300   8.39800   -18.98900 1.000 38.87000 ? 299 GLN A NE2 1 
ATOM   2286 N N   . CYS A 1 298 ? 8.89200   13.22200  -18.77300 1.000 40.58000 ? 300 CYS A N   1 
ATOM   2287 C CA  . CYS A 1 298 ? 10.33200  13.39600  -18.55000 1.000 41.14000 ? 300 CYS A CA  1 
ATOM   2288 C C   . CYS A 1 298 ? 10.62200  14.69600  -17.81300 1.000 43.67000 ? 300 CYS A C   1 
ATOM   2289 O O   . CYS A 1 298 ? 9.77600   15.58800  -17.76700 1.000 45.43000 ? 300 CYS A O   1 
ATOM   2290 C CB  . CYS A 1 298 ? 11.09800  13.36700  -19.87600 1.000 40.87000 ? 300 CYS A CB  1 
ATOM   2291 S SG  . CYS A 1 298 ? 11.07000  11.76900  -20.72400 1.000 47.88000 ? 300 CYS A SG  1 
ATOM   2292 N N   . PHE B 1 1   ? -5.30200  -7.37400  -23.40200 1.000 55.70000 ? 3   PHE B N   1 
ATOM   2293 C CA  . PHE B 1 1   ? -4.70200  -7.28700  -22.07000 1.000 49.37000 ? 3   PHE B CA  1 
ATOM   2294 C C   . PHE B 1 1   ? -3.78200  -6.07600  -21.92400 1.000 45.84000 ? 3   PHE B C   1 
ATOM   2295 O O   . PHE B 1 1   ? -2.82800  -5.91300  -22.67800 1.000 50.18000 ? 3   PHE B O   1 
ATOM   2296 C CB  . PHE B 1 1   ? -3.91800  -8.55900  -21.73900 1.000 47.54000 ? 3   PHE B CB  1 
ATOM   2297 C CG  . PHE B 1 1   ? -4.12200  -9.02600  -20.33500 1.000 43.41000 ? 3   PHE B CG  1 
ATOM   2298 C CD1 . PHE B 1 1   ? -5.38900  -9.34900  -19.88900 1.000 45.02000 ? 3   PHE B CD1 1 
ATOM   2299 C CD2 . PHE B 1 1   ? -3.06400  -9.11200  -19.45300 1.000 43.17000 ? 3   PHE B CD2 1 
ATOM   2300 C CE1 . PHE B 1 1   ? -5.60000  -9.76800  -18.59700 1.000 46.32000 ? 3   PHE B CE1 1 
ATOM   2301 C CE2 . PHE B 1 1   ? -3.27100  -9.53400  -18.15500 1.000 42.43000 ? 3   PHE B CE2 1 
ATOM   2302 C CZ  . PHE B 1 1   ? -4.54700  -9.85500  -17.72700 1.000 43.28000 ? 3   PHE B CZ  1 
ATOM   2303 N N   . ARG B 1 2   ? -4.08800  -5.23500  -20.94000 1.000 43.17000 ? 4   ARG B N   1 
ATOM   2304 C CA  . ARG B 1 2   ? -3.33600  -4.02200  -20.66400 1.000 42.35000 ? 4   ARG B CA  1 
ATOM   2305 C C   . ARG B 1 2   ? -2.98300  -3.98100  -19.18400 1.000 37.40000 ? 4   ARG B C   1 
ATOM   2306 O O   . ARG B 1 2   ? -3.65100  -4.59400  -18.35000 1.000 37.03000 ? 4   ARG B O   1 
ATOM   2307 C CB  . ARG B 1 2   ? -4.14200  -2.76700  -21.04100 1.000 42.84000 ? 4   ARG B CB  1 
ATOM   2308 C CG  . ARG B 1 2   ? -4.13700  -2.44400  -22.52900 1.000 42.29000 ? 4   ARG B CG  1 
ATOM   2309 C CD  . ARG B 1 2   ? -4.32300  -0.96500  -22.72400 1.000 37.89000 ? 4   ARG B CD  1 
ATOM   2310 N NE  . ARG B 1 2   ? -4.38700  -0.57900  -24.12800 1.000 36.80000 ? 4   ARG B NE  1 
ATOM   2311 C CZ  . ARG B 1 2   ? -3.35300  -0.10800  -24.82300 1.000 37.64000 ? 4   ARG B CZ  1 
ATOM   2312 N NH1 . ARG B 1 2   ? -2.16600  0.04700   -24.23800 1.000 40.15000 ? 4   ARG B NH1 1 
ATOM   2313 N NH2 . ARG B 1 2   ? -3.50400  0.22700   -26.10000 1.000 33.61000 ? 4   ARG B NH2 1 
ATOM   2314 N N   . LYS B 1 3   ? -1.91400  -3.26100  -18.86000 1.000 37.64000 ? 5   LYS B N   1 
ATOM   2315 C CA  . LYS B 1 3   ? -1.62000  -2.98500  -17.46200 1.000 38.82000 ? 5   LYS B CA  1 
ATOM   2316 C C   . LYS B 1 3   ? -2.62800  -1.96200  -16.96100 1.000 33.63000 ? 5   LYS B C   1 
ATOM   2317 O O   . LYS B 1 3   ? -2.70700  -0.85200  -17.49600 1.000 34.31000 ? 5   LYS B O   1 
ATOM   2318 C CB  . LYS B 1 3   ? -0.19300  -2.46900  -17.29500 1.000 39.10000 ? 5   LYS B CB  1 
ATOM   2319 C CG  . LYS B 1 3   ? 0.73800   -3.44800  -16.58200 1.000 40.08000 ? 5   LYS B CG  1 
ATOM   2320 C CD  . LYS B 1 3   ? 2.16800   -2.95100  -16.64300 1.000 44.76000 ? 5   LYS B CD  1 
ATOM   2321 C CE  . LYS B 1 3   ? 3.19400   -4.05800  -16.41500 1.000 44.20000 ? 5   LYS B CE  1 
ATOM   2322 N NZ  . LYS B 1 3   ? 3.79900   -4.09600  -15.01400 1.000 52.77000 ? 5   LYS B NZ  1 
ATOM   2323 N N   . MET B 1 4   ? -3.41100  -2.33300  -15.95300 1.000 30.13000 ? 6   MET B N   1 
ATOM   2324 C CA  . MET B 1 4   ? -4.53500  -1.52300  -15.50200 1.000 30.71000 ? 6   MET B CA  1 
ATOM   2325 C C   . MET B 1 4   ? -4.33000  -1.10000  -14.05700 1.000 29.37000 ? 6   MET B C   1 
ATOM   2326 O O   . MET B 1 4   ? -4.02800  -1.93600  -13.20100 1.000 30.97000 ? 6   MET B O   1 
ATOM   2327 C CB  . MET B 1 4   ? -5.84400  -2.29900  -15.63200 1.000 32.16000 ? 6   MET B CB  1 
ATOM   2328 C CG  . MET B 1 4   ? -6.95400  -1.48900  -16.21000 1.000 38.53000 ? 6   MET B CG  1 
ATOM   2329 S SD  . MET B 1 4   ? -8.41400  -2.49700  -16.47700 1.000 47.23000 ? 6   MET B SD  1 
ATOM   2330 C CE  . MET B 1 4   ? -7.96800  -3.31600  -17.98100 1.000 38.95000 ? 6   MET B CE  1 
ATOM   2331 N N   . ALA B 1 5   ? -4.51100  0.18400   -13.78200 1.000 26.67000 ? 7   ALA B N   1 
ATOM   2332 C CA  . ALA B 1 5   ? -4.40900  0.69500   -12.42500 1.000 26.36000 ? 7   ALA B CA  1 
ATOM   2333 C C   . ALA B 1 5   ? -5.79800  0.85300   -11.82700 1.000 26.95000 ? 7   ALA B C   1 
ATOM   2334 O O   . ALA B 1 5   ? -6.79700  0.92000   -12.54900 1.000 26.55000 ? 7   ALA B O   1 
ATOM   2335 C CB  . ALA B 1 5   ? -3.65600  2.03400   -12.40600 1.000 25.77000 ? 7   ALA B CB  1 
ATOM   2336 N N   . PHE B 1 6   ? -5.86700  0.88100   -10.49300 1.000 27.11000 ? 8   PHE B N   1 
ATOM   2337 C CA  . PHE B 1 6   ? -7.15500  1.14400   -9.86300  1.000 27.11000 ? 8   PHE B CA  1 
ATOM   2338 C C   . PHE B 1 6   ? -7.57200  2.58500   -10.14900 1.000 24.64000 ? 8   PHE B C   1 
ATOM   2339 O O   . PHE B 1 6   ? -6.72200  3.45600   -10.33100 1.000 25.21000 ? 8   PHE B O   1 
ATOM   2340 C CB  . PHE B 1 6   ? -7.10000  0.91400   -8.34600  1.000 26.42000 ? 8   PHE B CB  1 
ATOM   2341 C CG  . PHE B 1 6   ? -7.02800  -0.53900  -7.95800  1.000 27.73000 ? 8   PHE B CG  1 
ATOM   2342 C CD1 . PHE B 1 6   ? -8.15900  -1.33900  -8.00600  1.000 31.59000 ? 8   PHE B CD1 1 
ATOM   2343 C CD2 . PHE B 1 6   ? -5.81400  -1.11200  -7.58500  1.000 30.20000 ? 8   PHE B CD2 1 
ATOM   2344 C CE1 . PHE B 1 6   ? -8.09400  -2.68500  -7.66300  1.000 35.47000 ? 8   PHE B CE1 1 
ATOM   2345 C CE2 . PHE B 1 6   ? -5.74600  -2.46400  -7.24600  1.000 31.43000 ? 8   PHE B CE2 1 
ATOM   2346 C CZ  . PHE B 1 6   ? -6.88500  -3.24300  -7.28600  1.000 32.20000 ? 8   PHE B CZ  1 
ATOM   2347 N N   . PRO B 1 7   ? -8.87600  2.86000   -10.20900 1.000 27.40000 ? 9   PRO B N   1 
ATOM   2348 C CA  . PRO B 1 7   ? -9.32500  4.26000   -10.19400 1.000 27.12000 ? 9   PRO B CA  1 
ATOM   2349 C C   . PRO B 1 7   ? -8.78400  4.95700   -8.95600  1.000 26.68000 ? 9   PRO B C   1 
ATOM   2350 O O   . PRO B 1 7   ? -8.87900  4.43400   -7.84300  1.000 29.67000 ? 9   PRO B O   1 
ATOM   2351 C CB  . PRO B 1 7   ? -10.85500 4.15200   -10.16300 1.000 27.98000 ? 9   PRO B CB  1 
ATOM   2352 C CG  . PRO B 1 7   ? -11.17700 2.72600   -10.50500 1.000 30.61000 ? 9   PRO B CG  1 
ATOM   2353 C CD  . PRO B 1 7   ? -9.99100  1.91900   -10.04000 1.000 29.28000 ? 9   PRO B CD  1 
ATOM   2354 N N   . SER B 1 8   ? -8.20900  6.13800   -9.15800  1.000 28.54000 ? 10  SER B N   1 
ATOM   2355 C CA  . SER B 1 8   ? -7.37300  6.78800   -8.15400  1.000 24.26000 ? 10  SER B CA  1 
ATOM   2356 C C   . SER B 1 8   ? -8.09900  7.88000   -7.37400  1.000 27.82000 ? 10  SER B C   1 
ATOM   2357 O O   . SER B 1 8   ? -7.49400  8.49300   -6.49200  1.000 25.93000 ? 10  SER B O   1 
ATOM   2358 C CB  . SER B 1 8   ? -6.12000  7.36300   -8.82000  1.000 30.36000 ? 10  SER B CB  1 
ATOM   2359 O OG  . SER B 1 8   ? -6.44200  8.37600   -9.75300  1.000 28.47000 ? 10  SER B OG  1 
ATOM   2360 N N   . GLY B 1 9   ? -9.38600  8.11400   -7.65800  1.000 28.71000 ? 11  GLY B N   1 
ATOM   2361 C CA  . GLY B 1 9   ? -10.09100 9.23300   -7.04600  1.000 27.16000 ? 11  GLY B CA  1 
ATOM   2362 C C   . GLY B 1 9   ? -10.08200 9.22600   -5.52500  1.000 26.85000 ? 11  GLY B C   1 
ATOM   2363 O O   . GLY B 1 9   ? -9.96500  10.28000  -4.89700  1.000 28.55000 ? 11  GLY B O   1 
ATOM   2364 N N   . LYS B 1 10  ? -10.26400 8.05300   -4.90800  1.000 24.00000 ? 12  LYS B N   1 
ATOM   2365 C CA  . LYS B 1 10  ? -10.30800 8.00000   -3.44900  1.000 25.76000 ? 12  LYS B CA  1 
ATOM   2366 C C   . LYS B 1 10  ? -8.97900  8.42900   -2.82400  1.000 28.59000 ? 12  LYS B C   1 
ATOM   2367 O O   . LYS B 1 10  ? -8.95600  8.95300   -1.70500  1.000 28.67000 ? 12  LYS B O   1 
ATOM   2368 C CB  . LYS B 1 10  ? -10.68400 6.59000   -2.99400  1.000 27.55000 ? 12  LYS B CB  1 
ATOM   2369 C CG  . LYS B 1 10  ? -12.19600 6.31900   -3.02600  1.000 28.27000 ? 12  LYS B CG  1 
ATOM   2370 C CD  . LYS B 1 10  ? -12.52100 4.91100   -2.54200  1.000 34.96000 ? 12  LYS B CD  1 
ATOM   2371 C CE  . LYS B 1 10  ? -14.03000 4.69400   -2.45200  1.000 38.36000 ? 12  LYS B CE  1 
ATOM   2372 N NZ  . LYS B 1 10  ? -14.67800 4.93000   -3.78200  1.000 40.29000 ? 12  LYS B NZ  1 
ATOM   2373 N N   . VAL B 1 11  ? -7.87900  8.23800   -3.53800  1.000 23.40000 ? 13  VAL B N   1 
ATOM   2374 C CA  . VAL B 1 11  ? -6.55200  8.62400   -3.05300  1.000 25.07000 ? 13  VAL B CA  1 
ATOM   2375 C C   . VAL B 1 11  ? -6.19500  10.06000  -3.42300  1.000 24.58000 ? 13  VAL B C   1 
ATOM   2376 O O   . VAL B 1 11  ? -5.54500  10.75400  -2.63500  1.000 25.03000 ? 13  VAL B O   1 
ATOM   2377 C CB  . VAL B 1 11  ? -5.51400  7.63700   -3.60600  1.000 22.19000 ? 13  VAL B CB  1 
ATOM   2378 C CG1 . VAL B 1 11  ? -4.04500  8.02200   -3.19300  1.000 23.24000 ? 13  VAL B CG1 1 
ATOM   2379 C CG2 . VAL B 1 11  ? -5.87100  6.24400   -3.17000  1.000 24.52000 ? 13  VAL B CG2 1 
ATOM   2380 N N   . GLU B 1 12  ? -6.62100  10.52900  -4.60000  1.000 25.91000 ? 14  GLU B N   1 
ATOM   2381 C CA  . GLU B 1 12  ? -6.37100  11.91900  -4.97900  1.000 26.28000 ? 14  GLU B CA  1 
ATOM   2382 C C   . GLU B 1 12  ? -6.84800  12.89100  -3.90600  1.000 27.88000 ? 14  GLU B C   1 
ATOM   2383 O O   . GLU B 1 12  ? -6.16700  13.87900  -3.60500  1.000 28.66000 ? 14  GLU B O   1 
ATOM   2384 C CB  . GLU B 1 12  ? -7.06200  12.24400  -6.30500  1.000 26.74000 ? 14  GLU B CB  1 
ATOM   2385 C CG  . GLU B 1 12  ? -6.46300  11.60100  -7.57000  1.000 29.32000 ? 14  GLU B CG  1 
ATOM   2386 C CD  . GLU B 1 12  ? -7.44500  11.68100  -8.74600  1.000 30.03000 ? 14  GLU B CD  1 
ATOM   2387 O OE1 . GLU B 1 12  ? -7.79200  10.63700  -9.34800  1.000 25.95000 ? 14  GLU B OE1 1 
ATOM   2388 O OE2 . GLU B 1 12  ? -7.87500  12.80700  -9.06300  1.000 27.66000 ? 14  GLU B OE2 1 
ATOM   2389 N N   . SER B 1 13  ? -8.03000  12.64700  -3.33600  1.000 29.17000 ? 15  SER B N   1 
ATOM   2390 C CA  . SER B 1 13  ? -8.55600  13.56000  -2.32100  1.000 28.65000 ? 15  SER B CA  1 
ATOM   2391 C C   . SER B 1 13  ? -7.77500  13.50800  -1.01100  1.000 30.13000 ? 15  SER B C   1 
ATOM   2392 O O   . SER B 1 13  ? -8.11600  14.23900  -0.07500  1.000 28.32000 ? 15  SER B O   1 
ATOM   2393 C CB  . SER B 1 13  ? -10.03300 13.26000  -2.05500  1.000 34.44000 ? 15  SER B CB  1 
ATOM   2394 O OG  . SER B 1 13  ? -10.18400 11.92600  -1.61300  1.000 39.28000 ? 15  SER B OG  1 
ATOM   2395 N N   . CYS B 1 14  ? -6.75600  12.66100  -0.90400  1.000 28.24000 ? 16  CYS B N   1 
ATOM   2396 C CA  . CYS B 1 14  ? -5.94100  12.59000  0.30100   1.000 27.52000 ? 16  CYS B CA  1 
ATOM   2397 C C   . CYS B 1 14  ? -4.57300  13.23700  0.14800   1.000 27.45000 ? 16  CYS B C   1 
ATOM   2398 O O   . CYS B 1 14  ? -3.83500  13.31900  1.13400   1.000 27.50000 ? 16  CYS B O   1 
ATOM   2399 C CB  . CYS B 1 14  ? -5.76700  11.12600  0.73900   1.000 27.14000 ? 16  CYS B CB  1 
ATOM   2400 S SG  . CYS B 1 14  ? -7.31000  10.29700  1.11800   1.000 29.20000 ? 16  CYS B SG  1 
ATOM   2401 N N   . MET B 1 15  ? -4.20800  13.70700  -1.04200  1.000 28.71000 ? 17  MET B N   1 
ATOM   2402 C CA  . MET B 1 15  ? -2.83300  14.15300  -1.27700  1.000 25.78000 ? 17  MET B CA  1 
ATOM   2403 C C   . MET B 1 15  ? -2.70600  15.62900  -0.91800  1.000 31.73000 ? 17  MET B C   1 
ATOM   2404 O O   . MET B 1 15  ? -3.57100  16.44400  -1.26900  1.000 28.98000 ? 17  MET B O   1 
ATOM   2405 C CB  . MET B 1 15  ? -2.41200  13.92000  -2.72600  1.000 25.70000 ? 17  MET B CB  1 
ATOM   2406 C CG  . MET B 1 15  ? -2.45300  12.46100  -3.18000  1.000 26.55000 ? 17  MET B CG  1 
ATOM   2407 S SD  . MET B 1 15  ? -1.57700  11.31200  -2.07300  1.000 29.65000 ? 17  MET B SD  1 
ATOM   2408 C CE  . MET B 1 15  ? 0.05800   12.00400  -2.10200  1.000 28.71000 ? 17  MET B CE  1 
ATOM   2409 N N   . VAL B 1 16  ? -1.65000  15.95800  -0.18000  1.000 26.63000 ? 18  VAL B N   1 
ATOM   2410 C CA  . VAL B 1 16  ? -1.37500  17.32300  0.24400   1.000 31.16000 ? 18  VAL B CA  1 
ATOM   2411 C C   . VAL B 1 16  ? 0.10200   17.61100  -0.00000  1.000 32.54000 ? 18  VAL B C   1 
ATOM   2412 O O   . VAL B 1 16  ? 0.90400   16.71300  -0.27800  1.000 29.33000 ? 18  VAL B O   1 
ATOM   2413 C CB  . VAL B 1 16  ? -1.74500  17.56500  1.72600   1.000 27.79000 ? 18  VAL B CB  1 
ATOM   2414 C CG1 . VAL B 1 16  ? -3.23200  17.34300  1.95700   1.000 30.05000 ? 18  VAL B CG1 1 
ATOM   2415 C CG2 . VAL B 1 16  ? -0.92300  16.67200  2.63800   1.000 28.95000 ? 18  VAL B CG2 1 
ATOM   2416 N N   . GLN B 1 17  ? 0.45300   18.88900  0.08200   1.000 33.81000 ? 19  GLN B N   1 
ATOM   2417 C CA  . GLN B 1 17  ? 1.83000   19.33800  -0.05600  1.000 35.26000 ? 19  GLN B CA  1 
ATOM   2418 C C   . GLN B 1 17  ? 2.38900   19.60300  1.33500   1.000 34.67000 ? 19  GLN B C   1 
ATOM   2419 O O   . GLN B 1 17  ? 1.70800   20.21000  2.16700   1.000 37.00000 ? 19  GLN B O   1 
ATOM   2420 C CB  . GLN B 1 17  ? 1.89700   20.60800  -0.90700  1.000 38.66000 ? 19  GLN B CB  1 
ATOM   2421 C CG  . GLN B 1 17  ? 3.30500   21.15700  -1.12900  1.000 38.42000 ? 19  GLN B CG  1 
ATOM   2422 C CD  . GLN B 1 17  ? 3.30100   22.35400  -2.07400  1.000 43.36000 ? 19  GLN B CD  1 
ATOM   2423 O OE1 . GLN B 1 17  ? 4.32100   22.70300  -2.66200  1.000 46.92000 ? 19  GLN B OE1 1 
ATOM   2424 N NE2 . GLN B 1 17  ? 2.13800   22.97600  -2.22700  1.000 46.97000 ? 19  GLN B NE2 1 
ATOM   2425 N N   . VAL B 1 18  ? 3.60600   19.12300  1.59900   1.000 33.79000 ? 20  VAL B N   1 
ATOM   2426 C CA  . VAL B 1 18  ? 4.28800   19.36000  2.86900   1.000 35.76000 ? 20  VAL B CA  1 
ATOM   2427 C C   . VAL B 1 18  ? 5.59000   20.09600  2.58100   1.000 37.00000 ? 20  VAL B C   1 
ATOM   2428 O O   . VAL B 1 18  ? 6.39400   19.64700  1.75700   1.000 35.21000 ? 20  VAL B O   1 
ATOM   2429 C CB  . VAL B 1 18  ? 4.56500   18.05300  3.63900   1.000 34.49000 ? 20  VAL B CB  1 
ATOM   2430 C CG1 . VAL B 1 18  ? 5.28700   18.35300  4.93000   1.000 32.85000 ? 20  VAL B CG1 1 
ATOM   2431 C CG2 . VAL B 1 18  ? 3.26500   17.32500  3.94700   1.000 28.62000 ? 20  VAL B CG2 1 
ATOM   2432 N N   . THR B 1 19  ? 5.79800   21.21700  3.26400   1.000 39.75000 ? 21  THR B N   1 
ATOM   2433 C CA  . THR B 1 19  ? 7.00100   22.02600  3.11000   1.000 41.29000 ? 21  THR B CA  1 
ATOM   2434 C C   . THR B 1 19  ? 7.68400   22.17500  4.45900   1.000 39.36000 ? 21  THR B C   1 
ATOM   2435 O O   . THR B 1 19  ? 7.05800   22.61000  5.43100   1.000 41.69000 ? 21  THR B O   1 
ATOM   2436 C CB  . THR B 1 19  ? 6.67200   23.40900  2.54400   1.000 41.43000 ? 21  THR B CB  1 
ATOM   2437 O OG1 . THR B 1 19  ? 6.01100   23.26500  1.28000   1.000 46.44000 ? 21  THR B OG1 1 
ATOM   2438 C CG2 . THR B 1 19  ? 7.94900   24.22600  2.36200   1.000 43.77000 ? 21  THR B CG2 1 
ATOM   2439 N N   . CYS B 1 20  ? 8.96200   21.81400  4.52400   1.000 38.89000 ? 22  CYS B N   1 
ATOM   2440 C CA  . CYS B 1 20  ? 9.76800   22.05800  5.71400   1.000 43.90000 ? 22  CYS B CA  1 
ATOM   2441 C C   . CYS B 1 20  ? 10.99900  22.83700  5.27000   1.000 43.18000 ? 22  CYS B C   1 
ATOM   2442 O O   . CYS B 1 20  ? 11.88100  22.28400  4.60300   1.000 42.77000 ? 22  CYS B O   1 
ATOM   2443 C CB  . CYS B 1 20  ? 10.15100  20.75700  6.42200   1.000 43.14000 ? 22  CYS B CB  1 
ATOM   2444 S SG  . CYS B 1 20  ? 11.05700  20.98000  7.98400   1.000 46.70000 ? 22  CYS B SG  1 
ATOM   2445 N N   . GLY B 1 21  ? 11.03600  24.12000  5.61400   1.000 44.84000 ? 23  GLY B N   1 
ATOM   2446 C CA  . GLY B 1 21  ? 12.12800  24.97300  5.17500   1.000 42.78000 ? 23  GLY B CA  1 
ATOM   2447 C C   . GLY B 1 21  ? 12.13100  25.09800  3.66900   1.000 41.68000 ? 23  GLY B C   1 
ATOM   2448 O O   . GLY B 1 21  ? 11.15900  25.54900  3.05100   1.000 46.10000 ? 23  GLY B O   1 
ATOM   2449 N N   . THR B 1 22  ? 13.22600  24.66900  3.05700   1.000 40.43000 ? 24  THR B N   1 
ATOM   2450 C CA  . THR B 1 22  ? 13.40500  24.77400  1.61700   1.000 44.61000 ? 24  THR B CA  1 
ATOM   2451 C C   . THR B 1 22  ? 12.88000  23.56300  0.85000   1.000 44.72000 ? 24  THR B C   1 
ATOM   2452 O O   . THR B 1 22  ? 12.82300  23.61200  -0.38500  1.000 44.93000 ? 24  THR B O   1 
ATOM   2453 C CB  . THR B 1 22  ? 14.89200  24.98100  1.29900   1.000 46.29000 ? 24  THR B CB  1 
ATOM   2454 O OG1 . THR B 1 22  ? 15.04900  25.29400  -0.09000  1.000 50.88000 ? 24  THR B OG1 1 
ATOM   2455 C CG2 . THR B 1 22  ? 15.69700  23.73000  1.62800   1.000 45.26000 ? 24  THR B CG2 1 
ATOM   2456 N N   . THR B 1 23  ? 12.49000  22.48900  1.54100   1.000 42.84000 ? 25  THR B N   1 
ATOM   2457 C CA  . THR B 1 23  ? 12.13000  21.22800  0.90400   1.000 40.67000 ? 25  THR B CA  1 
ATOM   2458 C C   . THR B 1 23  ? 10.61900  21.09200  0.83100   1.000 39.48000 ? 25  THR B C   1 
ATOM   2459 O O   . THR B 1 23  ? 9.92300   21.35300  1.81200   1.000 39.60000 ? 25  THR B O   1 
ATOM   2460 C CB  . THR B 1 23  ? 12.70200  20.03400  1.67600   1.000 44.05000 ? 25  THR B CB  1 
ATOM   2461 O OG1 . THR B 1 23  ? 14.11500  19.96000  1.47800   1.000 43.99000 ? 25  THR B OG1 1 
ATOM   2462 C CG2 . THR B 1 23  ? 12.06300  18.71700  1.21800   1.000 37.23000 ? 25  THR B CG2 1 
ATOM   2463 N N   . THR B 1 24  ? 10.12500  20.67500  -0.33400  1.000 38.23000 ? 26  THR B N   1 
ATOM   2464 C CA  . THR B 1 24  ? 8.72200   20.35800  -0.55000  1.000 39.31000 ? 26  THR B CA  1 
ATOM   2465 C C   . THR B 1 24  ? 8.59200   18.92100  -1.04600  1.000 33.41000 ? 26  THR B C   1 
ATOM   2466 O O   . THR B 1 24  ? 9.41300   18.45200  -1.83700  1.000 32.06000 ? 26  THR B O   1 
ATOM   2467 C CB  . THR B 1 24  ? 8.09100   21.33300  -1.56100  1.000 41.28000 ? 26  THR B CB  1 
ATOM   2468 O OG1 . THR B 1 24  ? 7.81000   22.57900  -0.91000  1.000 46.04000 ? 26  THR B OG1 1 
ATOM   2469 C CG2 . THR B 1 24  ? 6.78200   20.77900  -2.14100  1.000 42.29000 ? 26  THR B CG2 1 
ATOM   2470 N N   . LEU B 1 25  ? 7.56500   18.22200  -0.57100  1.000 36.99000 ? 27  LEU B N   1 
ATOM   2471 C CA  . LEU B 1 25  ? 7.21600   16.90600  -1.09200  1.000 31.02000 ? 27  LEU B CA  1 
ATOM   2472 C C   . LEU B 1 25  ? 5.75100   16.65300  -0.74000  1.000 29.13000 ? 27  LEU B C   1 
ATOM   2473 O O   . LEU B 1 25  ? 5.05600   17.54200  -0.23700  1.000 30.75000 ? 27  LEU B O   1 
ATOM   2474 C CB  . LEU B 1 25  ? 8.17100   15.83100  -0.55500  1.000 31.04000 ? 27  LEU B CB  1 
ATOM   2475 C CG  . LEU B 1 25  ? 8.60000   15.79800  0.91900   1.000 30.21000 ? 27  LEU B CG  1 
ATOM   2476 C CD1 . LEU B 1 25  ? 7.42000   15.55800  1.86400   1.000 30.10000 ? 27  LEU B CD1 1 
ATOM   2477 C CD2 . LEU B 1 25  ? 9.68200   14.72800  1.15100   1.000 27.93000 ? 27  LEU B CD2 1 
ATOM   2478 N N   . ASN B 1 26  ? 5.28300   15.43500  -0.98400  1.000 26.87000 ? 28  ASN B N   1 
ATOM   2479 C CA  . ASN B 1 26  ? 3.87600   15.09700  -0.84500  1.000 26.66000 ? 28  ASN B CA  1 
ATOM   2480 C C   . ASN B 1 26  ? 3.59200   14.44700  0.49900   1.000 28.28000 ? 28  ASN B C   1 
ATOM   2481 O O   . ASN B 1 26  ? 4.43700   13.75100  1.06100   1.000 27.40000 ? 28  ASN B O   1 
ATOM   2482 C CB  . ASN B 1 26  ? 3.44500   14.14700  -1.96100  1.000 27.36000 ? 28  ASN B CB  1 
ATOM   2483 C CG  . ASN B 1 26  ? 3.83300   14.65300  -3.32200  1.000 27.22000 ? 28  ASN B CG  1 
ATOM   2484 O OD1 . ASN B 1 26  ? 3.17300   15.53400  -3.87100  1.000 29.27000 ? 28  ASN B OD1 1 
ATOM   2485 N ND2 . ASN B 1 26  ? 4.89900   14.10200  -3.88000  1.000 27.61000 ? 28  ASN B ND2 1 
ATOM   2486 N N   . GLY B 1 27  ? 2.36600   14.65000  0.98400   1.000 26.82000 ? 29  GLY B N   1 
ATOM   2487 C CA  . GLY B 1 27  ? 1.90000   13.97300  2.17000   1.000 25.39000 ? 29  GLY B CA  1 
ATOM   2488 C C   . GLY B 1 27  ? 0.55700   13.32000  1.91100   1.000 27.13000 ? 29  GLY B C   1 
ATOM   2489 O O   . GLY B 1 27  ? -0.15200  13.64900  0.96100   1.000 26.17000 ? 29  GLY B O   1 
ATOM   2490 N N   . LEU B 1 28  ? 0.22900   12.36600  2.77300   1.000 25.42000 ? 30  LEU B N   1 
ATOM   2491 C CA  . LEU B 1 28  ? -1.02400  11.62100  2.73100   1.000 26.88000 ? 30  LEU B CA  1 
ATOM   2492 C C   . LEU B 1 28  ? -1.84000  12.04600  3.94000   1.000 25.72000 ? 30  LEU B C   1 
ATOM   2493 O O   . LEU B 1 28  ? -1.43800  11.79400  5.07900   1.000 24.92000 ? 30  LEU B O   1 
ATOM   2494 C CB  . LEU B 1 28  ? -0.76500  10.11300  2.74000   1.000 26.28000 ? 30  LEU B CB  1 
ATOM   2495 C CG  . LEU B 1 28  ? -2.00300  9.22600   2.47600   1.000 24.09000 ? 30  LEU B CG  1 
ATOM   2496 C CD1 . LEU B 1 28  ? -2.48400  9.32600   1.02600   1.000 27.15000 ? 30  LEU B CD1 1 
ATOM   2497 C CD2 . LEU B 1 28  ? -1.69600  7.80500   2.83400   1.000 22.76000 ? 30  LEU B CD2 1 
ATOM   2498 N N   . TRP B 1 29  ? -2.98700  12.66800  3.68400   1.000 25.16000 ? 31  TRP B N   1 
ATOM   2499 C CA  . TRP B 1 29  ? -3.86300  13.22200  4.71600   1.000 24.80000 ? 31  TRP B CA  1 
ATOM   2500 C C   . TRP B 1 29  ? -5.02900  12.26600  4.94700   1.000 26.94000 ? 31  TRP B C   1 
ATOM   2501 O O   . TRP B 1 29  ? -5.90200  12.13100  4.08900   1.000 28.50000 ? 31  TRP B O   1 
ATOM   2502 C CB  . TRP B 1 29  ? -4.35800  14.59100  4.26300   1.000 27.31000 ? 31  TRP B CB  1 
ATOM   2503 C CG  . TRP B 1 29  ? -5.26800  15.33300  5.19800   1.000 28.46000 ? 31  TRP B CG  1 
ATOM   2504 C CD1 . TRP B 1 29  ? -5.36800  15.20400  6.55600   1.000 29.96000 ? 31  TRP B CD1 1 
ATOM   2505 C CD2 . TRP B 1 29  ? -6.18800  16.36200  4.82200   1.000 30.39000 ? 31  TRP B CD2 1 
ATOM   2506 N NE1 . TRP B 1 29  ? -6.30100  16.09500  7.04500   1.000 33.36000 ? 31  TRP B NE1 1 
ATOM   2507 C CE2 . TRP B 1 29  ? -6.81200  16.82000  5.99900   1.000 33.70000 ? 31  TRP B CE2 1 
ATOM   2508 C CE3 . TRP B 1 29  ? -6.53700  16.94600  3.59800   1.000 32.86000 ? 31  TRP B CE3 1 
ATOM   2509 C CZ2 . TRP B 1 29  ? -7.78800  17.82400  5.98700   1.000 33.70000 ? 31  TRP B CZ2 1 
ATOM   2510 C CZ3 . TRP B 1 29  ? -7.49900  17.94800  3.58900   1.000 33.94000 ? 31  TRP B CZ3 1 
ATOM   2511 C CH2 . TRP B 1 29  ? -8.10900  18.37600  4.77600   1.000 33.89000 ? 31  TRP B CH2 1 
ATOM   2512 N N   . LEU B 1 30  ? -5.03600  11.60500  6.10000   1.000 26.23000 ? 32  LEU B N   1 
ATOM   2513 C CA  . LEU B 1 30  ? -6.08900  10.68500  6.49900   1.000 27.66000 ? 32  LEU B CA  1 
ATOM   2514 C C   . LEU B 1 30  ? -6.52900  11.08500  7.89400   1.000 32.75000 ? 32  LEU B C   1 
ATOM   2515 O O   . LEU B 1 30  ? -5.69100  11.22800  8.78900   1.000 28.04000 ? 32  LEU B O   1 
ATOM   2516 C CB  . LEU B 1 30  ? -5.60600  9.22800   6.48600   1.000 25.88000 ? 32  LEU B CB  1 
ATOM   2517 C CG  . LEU B 1 30  ? -5.02800  8.75500   5.14900   1.000 28.25000 ? 32  LEU B CG  1 
ATOM   2518 C CD1 . LEU B 1 30  ? -4.29800  7.40800   5.30600   1.000 25.96000 ? 32  LEU B CD1 1 
ATOM   2519 C CD2 . LEU B 1 30  ? -6.14000  8.66700   4.10900   1.000 28.74000 ? 32  LEU B CD2 1 
ATOM   2520 N N   . ASP B 1 31  ? -7.83900  11.26600  8.07700   1.000 31.79000 ? 33  ASP B N   1 
ATOM   2521 C CA  . ASP B 1 31  ? -8.39200  11.80800  9.32400   1.000 32.06000 ? 33  ASP B CA  1 
ATOM   2522 C C   . ASP B 1 31  ? -7.58900  13.06400  9.66500   1.000 29.46000 ? 33  ASP B C   1 
ATOM   2523 O O   . ASP B 1 31  ? -7.38100  13.90500  8.78200   1.000 30.28000 ? 33  ASP B O   1 
ATOM   2524 C CB  . ASP B 1 31  ? -8.41800  10.70900  10.36600  1.000 34.06000 ? 33  ASP B CB  1 
ATOM   2525 C CG  . ASP B 1 31  ? -9.50600  9.68700   10.07500  1.000 38.45000 ? 33  ASP B CG  1 
ATOM   2526 O OD1 . ASP B 1 31  ? -10.62300 10.10900  9.67900   1.000 42.25000 ? 33  ASP B OD1 1 
ATOM   2527 O OD2 . ASP B 1 31  ? -9.24500  8.47800   10.21200  1.000 39.67000 ? 33  ASP B OD2 1 
ATOM   2528 N N   . ASP B 1 32  ? -7.13000  13.25500  10.90000  1.000 28.39000 ? 34  ASP B N   1 
ATOM   2529 C CA  . ASP B 1 32  ? -6.42400  14.49400  11.21200  1.000 30.84000 ? 34  ASP B CA  1 
ATOM   2530 C C   . ASP B 1 32  ? -4.90600  14.31200  11.26900  1.000 30.30000 ? 34  ASP B C   1 
ATOM   2531 O O   . ASP B 1 32  ? -4.23900  14.99700  12.04900  1.000 32.41000 ? 34  ASP B O   1 
ATOM   2532 C CB  . ASP B 1 32  ? -6.93800  15.10500  12.51600  1.000 30.83000 ? 34  ASP B CB  1 
ATOM   2533 C CG  . ASP B 1 32  ? -6.75800  14.19100  13.71500  1.000 36.04000 ? 34  ASP B CG  1 
ATOM   2534 O OD1 . ASP B 1 32  ? -6.36600  13.01300  13.54800  1.000 34.51000 ? 34  ASP B OD1 1 
ATOM   2535 O OD2 . ASP B 1 32  ? -7.03000  14.65900  14.84500  1.000 41.31000 ? 34  ASP B OD2 1 
ATOM   2536 N N   . VAL B 1 33  ? -4.34400  13.42800  10.44100  1.000 29.94000 ? 35  VAL B N   1 
ATOM   2537 C CA  . VAL B 1 33  ? -2.89600  13.19600  10.40700  1.000 27.11000 ? 35  VAL B CA  1 
ATOM   2538 C C   . VAL B 1 33  ? -2.41600  13.18800  8.96200   1.000 29.20000 ? 35  VAL B C   1 
ATOM   2539 O O   . VAL B 1 33  ? -3.04800  12.57700  8.09300   1.000 26.80000 ? 35  VAL B O   1 
ATOM   2540 C CB  . VAL B 1 33  ? -2.50400  11.87600  11.10100  1.000 27.09000 ? 35  VAL B CB  1 
ATOM   2541 C CG1 . VAL B 1 33  ? -0.98000  11.59100  10.89500  1.000 26.40000 ? 35  VAL B CG1 1 
ATOM   2542 C CG2 . VAL B 1 33  ? -2.82400  11.95400  12.57800  1.000 31.15000 ? 35  VAL B CG2 1 
ATOM   2543 N N   . VAL B 1 34  ? -1.29800  13.86600  8.70900   1.000 27.34000 ? 36  VAL B N   1 
ATOM   2544 C CA  . VAL B 1 34  ? -0.62300  13.85100  7.41500   1.000 28.69000 ? 36  VAL B CA  1 
ATOM   2545 C C   . VAL B 1 34  ? 0.63900   13.00700  7.55800   1.000 25.48000 ? 36  VAL B C   1 
ATOM   2546 O O   . VAL B 1 34  ? 1.40500   13.19200  8.50400   1.000 27.07000 ? 36  VAL B O   1 
ATOM   2547 C CB  . VAL B 1 34  ? -0.30200  15.27800  6.93600   1.000 26.42000 ? 36  VAL B CB  1 
ATOM   2548 C CG1 . VAL B 1 34  ? 0.49800   15.24800  5.66100   1.000 27.96000 ? 36  VAL B CG1 1 
ATOM   2549 C CG2 . VAL B 1 34  ? -1.61700  16.07100  6.71800   1.000 28.03000 ? 36  VAL B CG2 1 
ATOM   2550 N N   . TYR B 1 35  ? 0.83300   12.07000  6.63400   1.000 27.37000 ? 37  TYR B N   1 
ATOM   2551 C CA  . TYR B 1 35  ? 1.97200   11.15500  6.60800   1.000 26.25000 ? 37  TYR B CA  1 
ATOM   2552 C C   . TYR B 1 35  ? 2.89700   11.54600  5.46700   1.000 26.82000 ? 37  TYR B C   1 
ATOM   2553 O O   . TYR B 1 35  ? 2.42800   11.80400  4.35900   1.000 26.32000 ? 37  TYR B O   1 
ATOM   2554 C CB  . TYR B 1 35  ? 1.50100   9.70500   6.41400   1.000 24.94000 ? 37  TYR B CB  1 
ATOM   2555 C CG  . TYR B 1 35  ? 0.51200   9.24800   7.45800   1.000 24.50000 ? 37  TYR B CG  1 
ATOM   2556 C CD1 . TYR B 1 35  ? -0.85100  9.52600   7.32100   1.000 27.89000 ? 37  TYR B CD1 1 
ATOM   2557 C CD2 . TYR B 1 35  ? 0.93000   8.55900   8.58800   1.000 28.63000 ? 37  TYR B CD2 1 
ATOM   2558 C CE1 . TYR B 1 35  ? -1.76800  9.13100   8.28800   1.000 28.28000 ? 37  TYR B CE1 1 
ATOM   2559 C CE2 . TYR B 1 35  ? 0.01200   8.14700   9.55900   1.000 29.82000 ? 37  TYR B CE2 1 
ATOM   2560 C CZ  . TYR B 1 35  ? -1.32300  8.43700   9.40100   1.000 30.01000 ? 37  TYR B CZ  1 
ATOM   2561 O OH  . TYR B 1 35  ? -2.22900  8.04600   10.35200  1.000 31.55000 ? 37  TYR B OH  1 
ATOM   2562 N N   . CYS B 1 36  ? 4.20100   11.58500  5.72600   1.000 24.56000 ? 38  CYS B N   1 
ATOM   2563 C CA  . CYS B 1 36  ? 5.16700   11.88400  4.67100   1.000 24.22000 ? 38  CYS B CA  1 
ATOM   2564 C C   . CYS B 1 36  ? 6.52600   11.32500  5.08400   1.000 25.97000 ? 38  CYS B C   1 
ATOM   2565 O O   . CYS B 1 36  ? 6.71200   10.93000  6.23500   1.000 25.47000 ? 38  CYS B O   1 
ATOM   2566 C CB  . CYS B 1 36  ? 5.23900   13.39500  4.39200   1.000 25.01000 ? 38  CYS B CB  1 
ATOM   2567 S SG  . CYS B 1 36  ? 6.06800   14.37300  5.67000   1.000 30.15000 ? 38  CYS B SG  1 
ATOM   2568 N N   . PRO B 1 37  ? 7.49600   11.26000  4.15200   1.000 26.09000 ? 39  PRO B N   1 
ATOM   2569 C CA  . PRO B 1 37  ? 8.82200   10.73100  4.51100   1.000 26.19000 ? 39  PRO B CA  1 
ATOM   2570 C C   . PRO B 1 37  ? 9.50900   11.59800  5.55800   1.000 26.84000 ? 39  PRO B C   1 
ATOM   2571 O O   . PRO B 1 37  ? 9.49600   12.82700  5.48300   1.000 28.25000 ? 39  PRO B O   1 
ATOM   2572 C CB  . PRO B 1 37  ? 9.58600   10.75400  3.18100   1.000 25.93000 ? 39  PRO B CB  1 
ATOM   2573 C CG  . PRO B 1 37  ? 8.48500   10.73500  2.11500   1.000 25.84000 ? 39  PRO B CG  1 
ATOM   2574 C CD  . PRO B 1 37  ? 7.39300   11.53300  2.70600   1.000 25.92000 ? 39  PRO B CD  1 
ATOM   2575 N N   . ARG B 1 38  ? 10.12600  10.94700  6.54500   1.000 24.19000 ? 40  ARG B N   1 
ATOM   2576 C CA  . ARG B 1 38  ? 10.77700  11.73500  7.57500   1.000 26.80000 ? 40  ARG B CA  1 
ATOM   2577 C C   . ARG B 1 38  ? 11.95700  12.51800  7.01900   1.000 28.85000 ? 40  ARG B C   1 
ATOM   2578 O O   . ARG B 1 38  ? 12.39800  13.47200  7.66500   1.000 31.27000 ? 40  ARG B O   1 
ATOM   2579 C CB  . ARG B 1 38  ? 11.22200  10.84200  8.73700   1.000 30.78000 ? 40  ARG B CB  1 
ATOM   2580 C CG  . ARG B 1 38  ? 12.44700  10.00200  8.42400   1.000 26.51000 ? 40  ARG B CG  1 
ATOM   2581 C CD  . ARG B 1 38  ? 12.96300  9.27500   9.65600   1.000 27.31000 ? 40  ARG B CD  1 
ATOM   2582 N NE  . ARG B 1 38  ? 14.01800  8.34500   9.27800   1.000 27.83000 ? 40  ARG B NE  1 
ATOM   2583 C CZ  . ARG B 1 38  ? 14.74500  7.63300   10.12800  1.000 26.98000 ? 40  ARG B CZ  1 
ATOM   2584 N NH1 . ARG B 1 38  ? 14.53700  7.74000   11.43200  1.000 27.07000 ? 40  ARG B NH1 1 
ATOM   2585 N NH2 . ARG B 1 38  ? 15.69600  6.82700   9.66400   1.000 27.11000 ? 40  ARG B NH2 1 
ATOM   2586 N N   . HIS B 1 39  ? 12.45000  12.17800  5.81400   1.000 27.82000 ? 41  HIS B N   1 
ATOM   2587 C CA  . HIS B 1 39  ? 13.60600  12.91900  5.31300   1.000 29.52000 ? 41  HIS B CA  1 
ATOM   2588 C C   . HIS B 1 39  ? 13.24800  14.31100  4.83500   1.000 30.89000 ? 41  HIS B C   1 
ATOM   2589 O O   . HIS B 1 39  ? 14.13700  15.02100  4.35400   1.000 34.99000 ? 41  HIS B O   1 
ATOM   2590 C CB  . HIS B 1 39  ? 14.34100  12.14400  4.21000   1.000 28.53000 ? 41  HIS B CB  1 
ATOM   2591 C CG  . HIS B 1 39  ? 13.60100  12.01000  2.90900   1.000 27.82000 ? 41  HIS B CG  1 
ATOM   2592 N ND1 . HIS B 1 39  ? 13.21600  13.09000  2.14100   1.000 26.10000 ? 41  HIS B ND1 1 
ATOM   2593 C CD2 . HIS B 1 39  ? 13.25100  10.90600  2.20300   1.000 26.09000 ? 41  HIS B CD2 1 
ATOM   2594 C CE1 . HIS B 1 39  ? 12.63700  12.65900  1.03300   1.000 29.13000 ? 41  HIS B CE1 1 
ATOM   2595 N NE2 . HIS B 1 39  ? 12.65100  11.33700  1.04300   1.000 30.31000 ? 41  HIS B NE2 1 
ATOM   2596 N N   . VAL B 1 40  ? 11.98100  14.71200  4.96000   1.000 29.64000 ? 42  VAL B N   1 
ATOM   2597 C CA  . VAL B 1 40  ? 11.60500  16.09000  4.65800   1.000 32.93000 ? 42  VAL B CA  1 
ATOM   2598 C C   . VAL B 1 40  ? 12.30900  17.06100  5.60300   1.000 37.34000 ? 42  VAL B C   1 
ATOM   2599 O O   . VAL B 1 40  ? 12.52300  18.22900  5.25500   1.000 35.92000 ? 42  VAL B O   1 
ATOM   2600 C CB  . VAL B 1 40  ? 10.07300  16.24800  4.71900   1.000 31.24000 ? 42  VAL B CB  1 
ATOM   2601 C CG1 . VAL B 1 40  ? 9.58100   16.25400  6.16100   1.000 30.42000 ? 42  VAL B CG1 1 
ATOM   2602 C CG2 . VAL B 1 40  ? 9.63000   17.50800  3.95800   1.000 35.28000 ? 42  VAL B CG2 1 
ATOM   2603 N N   . ILE B 1 41  ? 12.68400  16.60000  6.80500   1.000 32.99000 ? 43  ILE B N   1 
ATOM   2604 C CA  . ILE B 1 41  ? 13.38700  17.45300  7.76600   1.000 36.34000 ? 43  ILE B CA  1 
ATOM   2605 C C   . ILE B 1 41  ? 14.89800  17.43800  7.56600   1.000 40.31000 ? 43  ILE B C   1 
ATOM   2606 O O   . ILE B 1 41  ? 15.60800  18.20300  8.23400   1.000 41.28000 ? 43  ILE B O   1 
ATOM   2607 C CB  . ILE B 1 41  ? 13.06300  17.05000  9.21800   1.000 32.32000 ? 43  ILE B CB  1 
ATOM   2608 C CG1 . ILE B 1 41  ? 13.68000  15.69400  9.54400   1.000 33.01000 ? 43  ILE B CG1 1 
ATOM   2609 C CG2 . ILE B 1 41  ? 11.54800  17.01500  9.45100   1.000 35.75000 ? 43  ILE B CG2 1 
ATOM   2610 C CD1 . ILE B 1 41  ? 13.56700  15.29900  10.98000  1.000 34.99000 ? 43  ILE B CD1 1 
ATOM   2611 N N   . CYS B 1 42  ? 15.41100  16.59200  6.67300   1.000 36.78000 ? 44  CYS B N   1 
ATOM   2612 C CA  . CYS B 1 42  ? 16.83000  16.60300  6.34000   1.000 41.51000 ? 44  CYS B CA  1 
ATOM   2613 C C   . CYS B 1 42  ? 17.14900  17.82300  5.47700   1.000 44.25000 ? 44  CYS B C   1 
ATOM   2614 O O   . CYS B 1 42  ? 16.36900  18.20400  4.60100   1.000 46.70000 ? 44  CYS B O   1 
ATOM   2615 C CB  . CYS B 1 42  ? 17.19200  15.30300  5.61000   1.000 34.52000 ? 44  CYS B CB  1 
ATOM   2616 S SG  . CYS B 1 42  ? 18.94400  14.90300  5.45600   1.000 49.52000 ? 44  CYS B SG  1 
ATOM   2617 N N   . THR B 1 43  ? 18.28400  18.46500  5.74700   1.000 51.60000 ? 45  THR B N   1 
ATOM   2618 C CA  . THR B 1 43  ? 18.75800  19.55900  4.90700   1.000 51.87000 ? 45  THR B CA  1 
ATOM   2619 C C   . THR B 1 43  ? 19.90900  19.07000  4.04000   1.000 54.00000 ? 45  THR B C   1 
ATOM   2620 O O   . THR B 1 43  ? 20.48500  18.00300  4.28100   1.000 53.26000 ? 45  THR B O   1 
ATOM   2621 C CB  . THR B 1 43  ? 19.19600  20.76700  5.74700   1.000 56.67000 ? 45  THR B CB  1 
ATOM   2622 O OG1 . THR B 1 43  ? 20.54300  20.57800  6.20200   1.000 53.65000 ? 45  THR B OG1 1 
ATOM   2623 C CG2 . THR B 1 43  ? 18.27400  20.95300  6.94900   1.000 55.00000 ? 45  THR B CG2 1 
ATOM   2624 N N   . SER B 1 44  ? 20.24300  19.87100  3.02000   1.000 57.19000 ? 46  SER B N   1 
ATOM   2625 C CA  . SER B 1 44  ? 21.30000  19.48900  2.08300   1.000 59.06000 ? 46  SER B CA  1 
ATOM   2626 C C   . SER B 1 44  ? 22.62800  19.24000  2.78900   1.000 57.18000 ? 46  SER B C   1 
ATOM   2627 O O   . SER B 1 44  ? 23.45400  18.45800  2.30100   1.000 59.75000 ? 46  SER B O   1 
ATOM   2628 C CB  . SER B 1 44  ? 21.46000  20.56200  1.00400   1.000 60.14000 ? 46  SER B CB  1 
ATOM   2629 O OG  . SER B 1 44  ? 21.24100  21.85700  1.53900   1.000 65.25000 ? 46  SER B OG  1 
ATOM   2630 N N   . GLU B 1 45  ? 22.85000  19.88000  3.93900   1.000 59.00000 ? 47  GLU B N   1 
ATOM   2631 C CA  . GLU B 1 45  ? 24.07300  19.63100  4.69800   1.000 59.24000 ? 47  GLU B CA  1 
ATOM   2632 C C   . GLU B 1 45  ? 24.00100  18.30400  5.45000   1.000 59.17000 ? 47  GLU B C   1 
ATOM   2633 O O   . GLU B 1 45  ? 24.99700  17.57500  5.54000   1.000 60.51000 ? 47  GLU B O   1 
ATOM   2634 C CB  . GLU B 1 45  ? 24.33300  20.76300  5.69600   1.000 61.76000 ? 47  GLU B CB  1 
ATOM   2635 C CG  . GLU B 1 45  ? 24.56800  22.15200  5.10000   1.000 63.11000 ? 47  GLU B CG  1 
ATOM   2636 C CD  . GLU B 1 45  ? 23.33200  22.77200  4.47600   1.000 63.58000 ? 47  GLU B CD  1 
ATOM   2637 O OE1 . GLU B 1 45  ? 23.47600  23.79700  3.78200   1.000 68.03000 ? 47  GLU B OE1 1 
ATOM   2638 O OE2 . GLU B 1 45  ? 22.21700  22.24100  4.68000   1.000 66.95000 ? 47  GLU B OE2 1 
ATOM   2639 N N   . ASP B 1 46  ? 22.83400  17.98200  6.01100   1.000 56.80000 ? 48  ASP B N   1 
ATOM   2640 C CA  . ASP B 1 46  ? 22.67000  16.80400  6.85100   1.000 56.82000 ? 48  ASP B CA  1 
ATOM   2641 C C   . ASP B 1 46  ? 22.45200  15.53100  6.05200   1.000 51.94000 ? 48  ASP B C   1 
ATOM   2642 O O   . ASP B 1 46  ? 22.28000  14.47600  6.66500   1.000 51.73000 ? 48  ASP B O   1 
ATOM   2643 C CB  . ASP B 1 46  ? 21.49000  17.00400  7.81000   1.000 55.82000 ? 48  ASP B CB  1 
ATOM   2644 C CG  . ASP B 1 46  ? 21.93200  17.33700  9.22800   1.000 59.26000 ? 48  ASP B CG  1 
ATOM   2645 O OD1 . ASP B 1 46  ? 22.94600  16.77000  9.69500   1.000 60.18000 ? 48  ASP B OD1 1 
ATOM   2646 O OD2 . ASP B 1 46  ? 21.26600  18.18000  9.86900   1.000 64.53000 ? 48  ASP B OD2 1 
ATOM   2647 N N   . MET B 1 47  ? 22.48200  15.59100  4.71500   1.000 52.88000 ? 49  MET B N   1 
ATOM   2648 C CA  . MET B 1 47  ? 22.01600  14.45400  3.92000   1.000 48.39000 ? 49  MET B CA  1 
ATOM   2649 C C   . MET B 1 47  ? 22.89300  13.22200  4.08000   1.000 44.00000 ? 49  MET B C   1 
ATOM   2650 O O   . MET B 1 47  ? 22.41200  12.09700  3.88400   1.000 38.06000 ? 49  MET B O   1 
ATOM   2651 C CB  . MET B 1 47  ? 21.91900  14.83400  2.44300   1.000 48.83000 ? 49  MET B CB  1 
ATOM   2652 C CG  . MET B 1 47  ? 20.72800  15.71600  2.09400   1.000 54.02000 ? 49  MET B CG  1 
ATOM   2653 S SD  . MET B 1 47  ? 20.58000  15.95300  0.31300   1.000 58.28000 ? 49  MET B SD  1 
ATOM   2654 C CE  . MET B 1 47  ? 22.26900  16.42000  -0.06100  1.000 49.73000 ? 49  MET B CE  1 
ATOM   2655 N N   . LEU B 1 48  ? 24.17400  13.40400  4.42400   1.000 38.57000 ? 50  LEU B N   1 
ATOM   2656 C CA  . LEU B 1 48  ? 25.06900  12.25700  4.48700   1.000 40.70000 ? 50  LEU B CA  1 
ATOM   2657 C C   . LEU B 1 48  ? 24.80800  11.39400  5.71000   1.000 38.22000 ? 50  LEU B C   1 
ATOM   2658 O O   . LEU B 1 48  ? 24.74200  10.16800  5.59000   1.000 42.71000 ? 50  LEU B O   1 
ATOM   2659 C CB  . LEU B 1 48  ? 26.53200  12.70800  4.46100   1.000 42.66000 ? 50  LEU B CB  1 
ATOM   2660 C CG  . LEU B 1 48  ? 27.04200  13.07800  3.06600   1.000 43.97000 ? 50  LEU B CG  1 
ATOM   2661 C CD1 . LEU B 1 48  ? 28.37900  13.84100  3.11300   1.000 44.28000 ? 50  LEU B CD1 1 
ATOM   2662 C CD2 . LEU B 1 48  ? 27.13900  11.81300  2.21700   1.000 46.54000 ? 50  LEU B CD2 1 
ATOM   2663 N N   . ASN B 1 49  ? 24.65700  11.99600  6.88500   1.000 38.97000 ? 51  ASN B N   1 
ATOM   2664 C CA  . ASN B 1 49  ? 24.35000  11.25000  8.10800   1.000 40.68000 ? 51  ASN B CA  1 
ATOM   2665 C C   . ASN B 1 49  ? 23.40500  12.09200  8.94800   1.000 44.56000 ? 51  ASN B C   1 
ATOM   2666 O O   . ASN B 1 49  ? 23.80600  12.72600  9.93200   1.000 42.17000 ? 51  ASN B O   1 
ATOM   2667 C CB  . ASN B 1 49  ? 25.62300  10.87500  8.87600   1.000 47.79000 ? 51  ASN B CB  1 
ATOM   2668 C CG  . ASN B 1 49  ? 25.37300  9.77100   9.90300   1.000 51.65000 ? 51  ASN B CG  1 
ATOM   2669 O OD1 . ASN B 1 49  ? 25.18600  10.03100  11.09000  1.000 58.44000 ? 51  ASN B OD1 1 
ATOM   2670 N ND2 . ASN B 1 49  ? 25.31900  8.52400   9.42600   1.000 53.11000 ? 51  ASN B ND2 1 
ATOM   2671 N N   . PRO B 1 50  ? 22.12000  12.12800  8.59700   1.000 41.00000 ? 52  PRO B N   1 
ATOM   2672 C CA  . PRO B 1 50  ? 21.16000  12.86200  9.42900   1.000 42.23000 ? 52  PRO B CA  1 
ATOM   2673 C C   . PRO B 1 50  ? 20.93500  12.14800  10.75300  1.000 38.70000 ? 52  PRO B C   1 
ATOM   2674 O O   . PRO B 1 50  ? 20.92800  10.91900  10.82800  1.000 39.22000 ? 52  PRO B O   1 
ATOM   2675 C CB  . PRO B 1 50  ? 19.87700  12.90200  8.58000   1.000 40.87000 ? 52  PRO B CB  1 
ATOM   2676 C CG  . PRO B 1 50  ? 20.00900  11.71400  7.69100   1.000 35.49000 ? 52  PRO B CG  1 
ATOM   2677 C CD  . PRO B 1 50  ? 21.47200  11.46000  7.46300   1.000 42.56000 ? 52  PRO B CD  1 
ATOM   2678 N N   . ASN B 1 51  ? 20.77500  12.93300  11.80900  1.000 38.76000 ? 53  ASN B N   1 
ATOM   2679 C CA  . ASN B 1 51  ? 20.36900  12.41600  13.11500  1.000 42.00000 ? 53  ASN B CA  1 
ATOM   2680 C C   . ASN B 1 51  ? 18.90700  12.82300  13.25200  1.000 40.00000 ? 53  ASN B C   1 
ATOM   2681 O O   . ASN B 1 51  ? 18.58700  13.94000  13.65400  1.000 41.17000 ? 53  ASN B O   1 
ATOM   2682 C CB  . ASN B 1 51  ? 21.25900  12.97900  14.22200  1.000 45.55000 ? 53  ASN B CB  1 
ATOM   2683 C CG  . ASN B 1 51  ? 20.96800  12.37600  15.59200  1.000 45.95000 ? 53  ASN B CG  1 
ATOM   2684 O OD1 . ASN B 1 51  ? 19.85000  11.95400  15.88200  1.000 43.69000 ? 53  ASN B OD1 1 
ATOM   2685 N ND2 . ASN B 1 51  ? 21.98400  12.35200  16.44700  1.000 47.06000 ? 53  ASN B ND2 1 
ATOM   2686 N N   . TYR B 1 52  ? 18.00600  11.91300  12.87600  1.000 41.49000 ? 54  TYR B N   1 
ATOM   2687 C CA  . TYR B 1 52  ? 16.61500  12.31200  12.68400  1.000 37.62000 ? 54  TYR B CA  1 
ATOM   2688 C C   . TYR B 1 52  ? 15.93600  12.65700  14.00100  1.000 40.95000 ? 54  TYR B C   1 
ATOM   2689 O O   . TYR B 1 52  ? 15.14300  13.60300  14.06200  1.000 41.70000 ? 54  TYR B O   1 
ATOM   2690 C CB  . TYR B 1 52  ? 15.84900  11.21900  11.94100  1.000 34.26000 ? 54  TYR B CB  1 
ATOM   2691 C CG  . TYR B 1 52  ? 16.05800  11.29100  10.44900  1.000 31.02000 ? 54  TYR B CG  1 
ATOM   2692 C CD1 . TYR B 1 52  ? 15.63000  12.39600  9.72200   1.000 32.35000 ? 54  TYR B CD1 1 
ATOM   2693 C CD2 . TYR B 1 52  ? 16.70200  10.26600  9.76800   1.000 31.33000 ? 54  TYR B CD2 1 
ATOM   2694 C CE1 . TYR B 1 52  ? 15.82800  12.47000  8.35000   1.000 31.92000 ? 54  TYR B CE1 1 
ATOM   2695 C CE2 . TYR B 1 52  ? 16.89200  10.32600  8.39900   1.000 30.38000 ? 54  TYR B CE2 1 
ATOM   2696 C CZ  . TYR B 1 52  ? 16.45000  11.42800  7.69600   1.000 28.18000 ? 54  TYR B CZ  1 
ATOM   2697 O OH  . TYR B 1 52  ? 16.65800  11.50400  6.33900   1.000 28.74000 ? 54  TYR B OH  1 
ATOM   2698 N N   . GLU B 1 53  ? 16.23100  11.92300  15.06900  1.000 45.35000 ? 55  GLU B N   1 
ATOM   2699 C CA  . GLU B 1 53  ? 15.58000  12.26900  16.32300  1.000 44.38000 ? 55  GLU B CA  1 
ATOM   2700 C C   . GLU B 1 53  ? 16.09200  13.60000  16.86000  1.000 45.60000 ? 55  GLU B C   1 
ATOM   2701 O O   . GLU B 1 53  ? 15.32600  14.34600  17.48100  1.000 46.08000 ? 55  GLU B O   1 
ATOM   2702 C CB  . GLU B 1 53  ? 15.73900  11.13600  17.33500  1.000 49.60000 ? 55  GLU B CB  1 
ATOM   2703 C CG  . GLU B 1 53  ? 17.03200  11.08600  18.11400  1.000 50.40000 ? 55  GLU B CG  1 
ATOM   2704 C CD  . GLU B 1 53  ? 16.90000  10.18200  19.32300  1.000 55.14000 ? 55  GLU B CD  1 
ATOM   2705 O OE1 . GLU B 1 53  ? 16.89200  8.94200   19.13500  1.000 51.30000 ? 55  GLU B OE1 1 
ATOM   2706 O OE2 . GLU B 1 53  ? 16.78500  10.71100  20.45300  1.000 58.24000 ? 55  GLU B OE2 1 
ATOM   2707 N N   . ASP B 1 54  ? 17.35600  13.94400  16.58400  1.000 44.93000 ? 56  ASP B N   1 
ATOM   2708 C CA  . ASP B 1 54  ? 17.85400  15.26600  16.95700  1.000 46.25000 ? 56  ASP B CA  1 
ATOM   2709 C C   . ASP B 1 54  ? 17.27400  16.35400  16.05700  1.000 44.49000 ? 56  ASP B C   1 
ATOM   2710 O O   . ASP B 1 54  ? 16.88800  17.42400  16.54000  1.000 46.08000 ? 56  ASP B O   1 
ATOM   2711 C CB  . ASP B 1 54  ? 19.38400  15.29400  16.90800  1.000 45.97000 ? 56  ASP B CB  1 
ATOM   2712 C CG  . ASP B 1 54  ? 19.94700  16.68400  17.15900  1.000 52.44000 ? 56  ASP B CG  1 
ATOM   2713 O OD1 . ASP B 1 54  ? 19.85800  17.15600  18.31500  1.000 53.03000 ? 56  ASP B OD1 1 
ATOM   2714 O OD2 . ASP B 1 54  ? 20.46100  17.30800  16.20400  1.000 56.00000 ? 56  ASP B OD2 1 
ATOM   2715 N N   . LEU B 1 55  ? 17.21200  16.10500  14.74400  1.000 43.73000 ? 57  LEU B N   1 
ATOM   2716 C CA  . LEU B 1 55  ? 16.57800  17.06100  13.83800  1.000 45.00000 ? 57  LEU B CA  1 
ATOM   2717 C C   . LEU B 1 55  ? 15.10100  17.25800  14.16500  1.000 45.71000 ? 57  LEU B C   1 
ATOM   2718 O O   . LEU B 1 55  ? 14.56500  18.35500  13.97100  1.000 43.96000 ? 57  LEU B O   1 
ATOM   2719 C CB  . LEU B 1 55  ? 16.73400  16.60000  12.38600  1.000 41.95000 ? 57  LEU B CB  1 
ATOM   2720 C CG  . LEU B 1 55  ? 18.14200  16.73900  11.79700  1.000 47.88000 ? 57  LEU B CG  1 
ATOM   2721 C CD1 . LEU B 1 55  ? 18.24800  16.00000  10.48000  1.000 43.34000 ? 57  LEU B CD1 1 
ATOM   2722 C CD2 . LEU B 1 55  ? 18.48300  18.20800  11.61700  1.000 49.89000 ? 57  LEU B CD2 1 
ATOM   2723 N N   . LEU B 1 56  ? 14.42900  16.21600  14.66100  1.000 42.36000 ? 58  LEU B N   1 
ATOM   2724 C CA  . LEU B 1 56  ? 13.01000  16.34000  14.98200  1.000 45.00000 ? 58  LEU B CA  1 
ATOM   2725 C C   . LEU B 1 56  ? 12.79000  17.08700  16.29300  1.000 47.78000 ? 58  LEU B C   1 
ATOM   2726 O O   . LEU B 1 56  ? 11.87000  17.90700  16.39000  1.000 47.41000 ? 58  LEU B O   1 
ATOM   2727 C CB  . LEU B 1 56  ? 12.35600  14.96000  15.04500  1.000 39.27000 ? 58  LEU B CB  1 
ATOM   2728 C CG  . LEU B 1 56  ? 10.83100  14.96600  15.17400  1.000 43.85000 ? 58  LEU B CG  1 
ATOM   2729 C CD1 . LEU B 1 56  ? 10.22700  15.89100  14.12900  1.000 43.34000 ? 58  LEU B CD1 1 
ATOM   2730 C CD2 . LEU B 1 56  ? 10.28200  13.54900  15.04300  1.000 37.83000 ? 58  LEU B CD2 1 
ATOM   2731 N N   . ILE B 1 57  ? 13.61600  16.80900  17.31000  1.000 49.54000 ? 59  ILE B N   1 
ATOM   2732 C CA  . ILE B 1 57  ? 13.54600  17.55700  18.56700  1.000 47.88000 ? 59  ILE B CA  1 
ATOM   2733 C C   . ILE B 1 57  ? 13.71400  19.04800  18.30500  1.000 47.80000 ? 59  ILE B C   1 
ATOM   2734 O O   . ILE B 1 57  ? 13.02000  19.88300  18.90100  1.000 49.15000 ? 59  ILE B O   1 
ATOM   2735 C CB  . ILE B 1 57  ? 14.60300  17.03100  19.55900  1.000 50.28000 ? 59  ILE B CB  1 
ATOM   2736 C CG1 . ILE B 1 57  ? 14.16900  15.69200  20.15200  1.000 46.75000 ? 59  ILE B CG1 1 
ATOM   2737 C CG2 . ILE B 1 57  ? 14.86300  18.04300  20.67200  1.000 50.53000 ? 59  ILE B CG2 1 
ATOM   2738 C CD1 . ILE B 1 57  ? 15.27400  14.97700  20.89600  1.000 51.83000 ? 59  ILE B CD1 1 
ATOM   2739 N N   . ARG B 1 58  ? 14.60900  19.39900  17.37600  1.000 50.35000 ? 60  ARG B N   1 
ATOM   2740 C CA  . ARG B 1 58  ? 14.85100  20.79900  17.03100  1.000 52.52000 ? 60  ARG B CA  1 
ATOM   2741 C C   . ARG B 1 58  ? 13.64500  21.44800  16.35200  1.000 53.48000 ? 60  ARG B C   1 
ATOM   2742 O O   . ARG B 1 58  ? 13.46000  22.66500  16.46700  1.000 54.29000 ? 60  ARG B O   1 
ATOM   2743 C CB  . ARG B 1 58  ? 16.08500  20.91100  16.13000  1.000 51.29000 ? 60  ARG B CB  1 
ATOM   2744 C CG  . ARG B 1 58  ? 17.41900  20.54100  16.79900  1.000 55.63000 ? 60  ARG B CG  1 
ATOM   2745 C CD  . ARG B 1 58  ? 18.58800  20.67900  15.82600  1.000 56.23000 ? 60  ARG B CD  1 
ATOM   2746 N NE  . ARG B 1 58  ? 18.17600  21.36100  14.59900  1.000 63.53000 ? 60  ARG B NE  1 
ATOM   2747 C CZ  . ARG B 1 58  ? 18.91100  21.44500  13.49200  1.000 64.13000 ? 60  ARG B CZ  1 
ATOM   2748 N NH1 . ARG B 1 58  ? 20.11600  20.88600  13.44000  1.000 65.64000 ? 60  ARG B NH1 1 
ATOM   2749 N NH2 . ARG B 1 58  ? 18.43400  22.09200  12.43400  1.000 62.28000 ? 60  ARG B NH2 1 
ATOM   2750 N N   . LYS B 1 59  ? 12.83300  20.67200  15.62900  1.000 50.70000 ? 61  LYS B N   1 
ATOM   2751 C CA  . LYS B 1 59  ? 11.66900  21.21900  14.94100  1.000 50.84000 ? 61  LYS B CA  1 
ATOM   2752 C C   . LYS B 1 59  ? 10.51400  21.44100  15.91200  1.000 48.27000 ? 61  LYS B C   1 
ATOM   2753 O O   . LYS B 1 59  ? 10.39400  20.76400  16.93900  1.000 48.84000 ? 61  LYS B O   1 
ATOM   2754 C CB  . LYS B 1 59  ? 11.19300  20.28700  13.81700  1.000 49.55000 ? 61  LYS B CB  1 
ATOM   2755 C CG  . LYS B 1 59  ? 12.19900  20.01100  12.70600  1.000 45.81000 ? 61  LYS B CG  1 
ATOM   2756 C CD  . LYS B 1 59  ? 12.36300  21.20000  11.78200  1.000 42.79000 ? 61  LYS B CD  1 
ATOM   2757 C CE  . LYS B 1 59  ? 13.55400  20.99500  10.87300  1.000 45.89000 ? 61  LYS B CE  1 
ATOM   2758 N NZ  . LYS B 1 59  ? 14.75800  20.54200  11.64300  1.000 50.42000 ? 61  LYS B NZ  1 
ATOM   2759 N N   . SER B 1 60  ? 9.65200   22.39300  15.56700  1.000 46.53000 ? 62  SER B N   1 
ATOM   2760 C CA  . SER B 1 60  ? 8.37700   22.58900  16.24100  1.000 49.48000 ? 62  SER B CA  1 
ATOM   2761 C C   . SER B 1 60  ? 7.26600   22.63700  15.19800  1.000 46.86000 ? 62  SER B C   1 
ATOM   2762 O O   . SER B 1 60  ? 7.51900   22.66100  13.99000  1.000 48.29000 ? 62  SER B O   1 
ATOM   2763 C CB  . SER B 1 60  ? 8.37400   23.86600  17.08900  1.000 51.40000 ? 62  SER B CB  1 
ATOM   2764 O OG  . SER B 1 60  ? 8.55900   24.99700  16.26600  1.000 55.94000 ? 62  SER B OG  1 
ATOM   2765 N N   . ASN B 1 61  ? 6.02100   22.66400  15.68100  1.000 45.11000 ? 63  ASN B N   1 
ATOM   2766 C CA  . ASN B 1 61  ? 4.86600   22.54200  14.79300  1.000 45.26000 ? 63  ASN B CA  1 
ATOM   2767 C C   . ASN B 1 61  ? 4.91800   23.54500  13.64500  1.000 46.14000 ? 63  ASN B C   1 
ATOM   2768 O O   . ASN B 1 61  ? 4.68900   23.18600  12.48400  1.000 44.17000 ? 63  ASN B O   1 
ATOM   2769 C CB  . ASN B 1 61  ? 3.57900   22.70300  15.60200  1.000 39.98000 ? 63  ASN B CB  1 
ATOM   2770 C CG  . ASN B 1 61  ? 3.30000   21.50200  16.47500  1.000 42.28000 ? 63  ASN B CG  1 
ATOM   2771 O OD1 . ASN B 1 61  ? 3.79400   20.40800  16.20500  1.000 45.33000 ? 63  ASN B OD1 1 
ATOM   2772 N ND2 . ASN B 1 61  ? 2.53100   21.69600  17.53700  1.000 40.69000 ? 63  ASN B ND2 1 
ATOM   2773 N N   . HIS B 1 62  ? 5.25400   24.80200  13.93900  1.000 49.74000 ? 64  HIS B N   1 
ATOM   2774 C CA  . HIS B 1 62  ? 5.22500   25.83800  12.90800  1.000 48.25000 ? 64  HIS B CA  1 
ATOM   2775 C C   . HIS B 1 62  ? 6.33400   25.68400  11.86200  1.000 48.30000 ? 64  HIS B C   1 
ATOM   2776 O O   . HIS B 1 62  ? 6.34000   26.43800  10.88100  1.000 47.44000 ? 64  HIS B O   1 
ATOM   2777 C CB  . HIS B 1 62  ? 5.31100   27.21600  13.56900  1.000 50.05000 ? 64  HIS B CB  1 
ATOM   2778 C CG  . HIS B 1 62  ? 6.46100   27.34900  14.51700  1.000 50.56000 ? 64  HIS B CG  1 
ATOM   2779 N ND1 . HIS B 1 62  ? 7.75200   27.57800  14.08800  1.000 46.85000 ? 64  HIS B ND1 1 
ATOM   2780 C CD2 . HIS B 1 62  ? 6.52100   27.26200  15.86800  1.000 48.12000 ? 64  HIS B CD2 1 
ATOM   2781 C CE1 . HIS B 1 62  ? 8.55600   27.63200  15.13500  1.000 47.80000 ? 64  HIS B CE1 1 
ATOM   2782 N NE2 . HIS B 1 62  ? 7.83500   27.44400  16.22700  1.000 50.89000 ? 64  HIS B NE2 1 
ATOM   2783 N N   . ASN B 1 63  ? 7.25800   24.73200  12.02700  1.000 47.20000 ? 65  ASN B N   1 
ATOM   2784 C CA  . ASN B 1 63  ? 8.26200   24.47600  10.99900  1.000 46.59000 ? 65  ASN B CA  1 
ATOM   2785 C C   . ASN B 1 63  ? 7.69300   23.75900  9.77400   1.000 45.50000 ? 65  ASN B C   1 
ATOM   2786 O O   . ASN B 1 63  ? 8.36900   23.70500  8.74200   1.000 44.25000 ? 65  ASN B O   1 
ATOM   2787 C CB  . ASN B 1 63  ? 9.41900   23.65200  11.58300  1.000 47.12000 ? 65  ASN B CB  1 
ATOM   2788 C CG  . ASN B 1 63  ? 10.28200  24.45200  12.55900  1.000 51.74000 ? 65  ASN B CG  1 
ATOM   2789 O OD1 . ASN B 1 63  ? 10.42300  24.09100  13.73400  1.000 50.08000 ? 65  ASN B OD1 1 
ATOM   2790 N ND2 . ASN B 1 63  ? 10.86400  25.53900  12.07100  1.000 48.87000 ? 65  ASN B ND2 1 
ATOM   2791 N N   . PHE B 1 64  ? 6.48100   23.21700  9.85300   1.000 43.48000 ? 66  PHE B N   1 
ATOM   2792 C CA  . PHE B 1 64  ? 5.88700   22.46000  8.75700   1.000 41.89000 ? 66  PHE B CA  1 
ATOM   2793 C C   . PHE B 1 64  ? 4.70200   23.21400  8.18600   1.000 40.25000 ? 66  PHE B C   1 
ATOM   2794 O O   . PHE B 1 64  ? 3.78200   23.58500  8.92000   1.000 44.67000 ? 66  PHE B O   1 
ATOM   2795 C CB  . PHE B 1 64  ? 5.42100   21.08300  9.21700   1.000 41.96000 ? 66  PHE B CB  1 
ATOM   2796 C CG  . PHE B 1 64  ? 6.46300   20.31400  9.93700   1.000 40.45000 ? 66  PHE B CG  1 
ATOM   2797 C CD1 . PHE B 1 64  ? 7.40000   19.57300  9.23500   1.000 40.47000 ? 66  PHE B CD1 1 
ATOM   2798 C CD2 . PHE B 1 64  ? 6.51200   20.33000  11.31500  1.000 39.45000 ? 66  PHE B CD2 1 
ATOM   2799 C CE1 . PHE B 1 64  ? 8.36300   18.86100  9.90300   1.000 37.54000 ? 66  PHE B CE1 1 
ATOM   2800 C CE2 . PHE B 1 64  ? 7.47600   19.62300  11.98600  1.000 42.57000 ? 66  PHE B CE2 1 
ATOM   2801 C CZ  . PHE B 1 64  ? 8.40400   18.88600  11.27700  1.000 38.81000 ? 66  PHE B CZ  1 
ATOM   2802 N N   . LEU B 1 65  ? 4.70400   23.40100  6.87900   1.000 41.89000 ? 67  LEU B N   1 
ATOM   2803 C CA  . LEU B 1 65  ? 3.60300   24.04500  6.18500   1.000 41.41000 ? 67  LEU B CA  1 
ATOM   2804 C C   . LEU B 1 65  ? 2.91400   22.99700  5.31400   1.000 42.62000 ? 67  LEU B C   1 
ATOM   2805 O O   . LEU B 1 65  ? 3.53900   22.42900  4.41100   1.000 43.80000 ? 67  LEU B O   1 
ATOM   2806 C CB  . LEU B 1 65  ? 4.12000   25.21800  5.35800   1.000 44.67000 ? 67  LEU B CB  1 
ATOM   2807 C CG  . LEU B 1 65  ? 3.04700   26.15500  4.81900   1.000 51.77000 ? 67  LEU B CG  1 
ATOM   2808 C CD1 . LEU B 1 65  ? 3.46600   27.63500  5.04500   1.000 54.29000 ? 67  LEU B CD1 1 
ATOM   2809 C CD2 . LEU B 1 65  ? 2.76700   25.84100  3.35500   1.000 46.97000 ? 67  LEU B CD2 1 
ATOM   2810 N N   . VAL B 1 66  ? 1.64400   22.73000  5.60600   1.000 40.00000 ? 68  VAL B N   1 
ATOM   2811 C CA  . VAL B 1 66  ? 0.84900   21.70000  4.93800   1.000 40.84000 ? 68  VAL B CA  1 
ATOM   2812 C C   . VAL B 1 66  ? -0.27100  22.38600  4.16000   1.000 39.99000 ? 68  VAL B C   1 
ATOM   2813 O O   . VAL B 1 66  ? -1.06400  23.13200  4.74500   1.000 42.14000 ? 68  VAL B O   1 
ATOM   2814 C CB  . VAL B 1 66  ? 0.27500   20.69900  5.95400   1.000 37.38000 ? 68  VAL B CB  1 
ATOM   2815 C CG1 . VAL B 1 66  ? -0.62900  19.69400  5.25600   1.000 36.34000 ? 68  VAL B CG1 1 
ATOM   2816 C CG2 . VAL B 1 66  ? 1.40000   19.98700  6.70100   1.000 37.22000 ? 68  VAL B CG2 1 
ATOM   2817 N N   . GLN B 1 67  ? -0.35000  22.13200  2.84900   1.000 40.87000 ? 69  GLN B N   1 
ATOM   2818 C CA  . GLN B 1 67  ? -1.39100  22.72000  2.00500   1.000 42.64000 ? 69  GLN B CA  1 
ATOM   2819 C C   . GLN B 1 67  ? -2.16000  21.63600  1.26700   1.000 41.16000 ? 69  GLN B C   1 
ATOM   2820 O O   . GLN B 1 67  ? -1.56400  20.84200  0.53000   1.000 38.14000 ? 69  GLN B O   1 
ATOM   2821 C CB  . GLN B 1 67  ? -0.81900  23.69500  0.97400   1.000 43.90000 ? 69  GLN B CB  1 
ATOM   2822 C CG  . GLN B 1 67  ? -0.02600  24.84800  1.53900   1.000 49.50000 ? 69  GLN B CG  1 
ATOM   2823 C CD  . GLN B 1 67  ? 0.66800   25.63300  0.44100   1.000 52.94000 ? 69  GLN B CD  1 
ATOM   2824 O OE1 . GLN B 1 67  ? 0.01700   26.32500  -0.34800  1.000 55.74000 ? 69  GLN B OE1 1 
ATOM   2825 N NE2 . GLN B 1 67  ? 1.99000   25.47800  0.34300   1.000 50.91000 ? 69  GLN B NE2 1 
ATOM   2826 N N   . ALA B 1 68  ? -3.48500  21.65000  1.41200   1.000 39.47000 ? 70  ALA B N   1 
ATOM   2827 C CA  . ALA B 1 68  ? -4.38300  20.76700  0.66500   1.000 41.26000 ? 70  ALA B CA  1 
ATOM   2828 C C   . ALA B 1 68  ? -4.94900  21.57400  -0.50000  1.000 47.46000 ? 70  ALA B C   1 
ATOM   2829 O O   . ALA B 1 68  ? -5.96200  22.26200  -0.37000  1.000 48.95000 ? 70  ALA B O   1 
ATOM   2830 C CB  . ALA B 1 68  ? -5.48100  20.22100  1.56900   1.000 40.44000 ? 70  ALA B CB  1 
ATOM   2831 N N   . GLY B 1 69  ? -4.29000  21.48700  -1.65200  1.000 48.75000 ? 71  GLY B N   1 
ATOM   2832 C CA  . GLY B 1 69  ? -4.61900  22.37900  -2.74600  1.000 49.42000 ? 71  GLY B CA  1 
ATOM   2833 C C   . GLY B 1 69  ? -4.34800  23.82200  -2.37200  1.000 52.00000 ? 71  GLY B C   1 
ATOM   2834 O O   . GLY B 1 69  ? -3.18900  24.21200  -2.20300  1.000 52.52000 ? 71  GLY B O   1 
ATOM   2835 N N   . ASN B 1 70  ? -5.40800  24.61700  -2.20300  1.000 53.96000 ? 72  ASN B N   1 
ATOM   2836 C CA  . ASN B 1 70  ? -5.26200  26.03000  -1.87800  1.000 53.31000 ? 72  ASN B CA  1 
ATOM   2837 C C   . ASN B 1 70  ? -5.38700  26.33900  -0.39000  1.000 54.34000 ? 72  ASN B C   1 
ATOM   2838 O O   . ASN B 1 70  ? -4.88600  27.38200  0.04200   1.000 57.33000 ? 72  ASN B O   1 
ATOM   2839 C CB  . ASN B 1 70  ? -6.29300  26.86500  -2.65100  1.000 55.40000 ? 72  ASN B CB  1 
ATOM   2840 N N   . VAL B 1 71  ? -6.03800  25.46500  0.41400   1.000 53.15000 ? 73  VAL B N   1 
ATOM   2841 C CA  . VAL B 1 71  ? -6.22400  25.71000  1.84500   1.000 50.88000 ? 73  VAL B CA  1 
ATOM   2842 C C   . VAL B 1 71  ? -5.00800  25.22300  2.62400   1.000 50.91000 ? 73  VAL B C   1 
ATOM   2843 O O   . VAL B 1 71  ? -4.49500  24.12200  2.38700   1.000 49.84000 ? 73  VAL B O   1 
ATOM   2844 C CB  . VAL B 1 71  ? -7.51200  25.04000  2.36600   1.000 51.35000 ? 73  VAL B CB  1 
ATOM   2845 C CG1 . VAL B 1 71  ? -7.62000  23.61000  1.87200   1.000 51.71000 ? 73  VAL B CG1 1 
ATOM   2846 C CG2 . VAL B 1 71  ? -7.55700  25.07500  3.89300   1.000 48.24000 ? 73  VAL B CG2 1 
ATOM   2847 N N   . GLN B 1 72  ? -4.55200  26.04400  3.56900   1.000 48.23000 ? 74  GLN B N   1 
ATOM   2848 C CA  . GLN B 1 72  ? -3.47100  25.66300  4.46800   1.000 47.02000 ? 74  GLN B CA  1 
ATOM   2849 C C   . GLN B 1 72  ? -4.04300  24.91500  5.66200   1.000 45.65000 ? 74  GLN B C   1 
ATOM   2850 O O   . GLN B 1 72  ? -5.06800  25.30800  6.22500   1.000 49.24000 ? 74  GLN B O   1 
ATOM   2851 C CB  . GLN B 1 72  ? -2.69100  26.89200  4.93900   1.000 43.91000 ? 74  GLN B CB  1 
ATOM   2852 N N   . LEU B 1 73  ? -3.39100  23.81400  6.02400   1.000 45.51000 ? 75  LEU B N   1 
ATOM   2853 C CA  . LEU B 1 73  ? -3.72700  23.05300  7.21900   1.000 43.36000 ? 75  LEU B CA  1 
ATOM   2854 C C   . LEU B 1 73  ? -2.74400  23.41300  8.32600   1.000 42.46000 ? 75  LEU B C   1 
ATOM   2855 O O   . LEU B 1 73  ? -1.52500  23.36700  8.11600   1.000 45.58000 ? 75  LEU B O   1 
ATOM   2856 C CB  . LEU B 1 73  ? -3.67900  21.54900  6.94300   1.000 39.99000 ? 75  LEU B CB  1 
ATOM   2857 C CG  . LEU B 1 73  ? -4.53100  21.01300  5.79700   1.000 42.62000 ? 75  LEU B CG  1 
ATOM   2858 C CD1 . LEU B 1 73  ? -4.26400  19.53200  5.63700   1.000 39.31000 ? 75  LEU B CD1 1 
ATOM   2859 C CD2 . LEU B 1 73  ? -6.02200  21.27600  6.05200   1.000 39.31000 ? 75  LEU B CD2 1 
ATOM   2860 N N   . ARG B 1 74  ? -3.26600  23.76800  9.49800   1.000 42.95000 ? 76  ARG B N   1 
ATOM   2861 C CA  . ARG B 1 74  ? -2.39900  24.14900  10.60500  1.000 44.47000 ? 76  ARG B CA  1 
ATOM   2862 C C   . ARG B 1 74  ? -1.92800  22.90200  11.34500  1.000 40.60000 ? 76  ARG B C   1 
ATOM   2863 O O   . ARG B 1 74  ? -2.74100  22.06700  11.75400  1.000 39.97000 ? 76  ARG B O   1 
ATOM   2864 C CB  . ARG B 1 74  ? -3.11600  25.10200  11.55900  1.000 45.95000 ? 76  ARG B CB  1 
ATOM   2865 N N   . VAL B 1 75  ? -0.61300  22.77400  11.49900  1.000 37.88000 ? 77  VAL B N   1 
ATOM   2866 C CA  . VAL B 1 75  ? -0.01100  21.63900  12.19700  1.000 39.22000 ? 77  VAL B CA  1 
ATOM   2867 C C   . VAL B 1 75  ? -0.08500  21.88000  13.70100  1.000 38.74000 ? 77  VAL B C   1 
ATOM   2868 O O   . VAL B 1 75  ? 0.40900   22.89600  14.19900  1.000 42.38000 ? 77  VAL B O   1 
ATOM   2869 C CB  . VAL B 1 75  ? 1.44300   21.42700  11.75200  1.000 37.92000 ? 77  VAL B CB  1 
ATOM   2870 C CG1 . VAL B 1 75  ? 2.03500   20.18900  12.42600  1.000 33.60000 ? 77  VAL B CG1 1 
ATOM   2871 C CG2 . VAL B 1 75  ? 1.52900   21.32700  10.23500  1.000 40.29000 ? 77  VAL B CG2 1 
ATOM   2872 N N   . ILE B 1 76  ? -0.67900  20.93400  14.42900  1.000 40.30000 ? 78  ILE B N   1 
ATOM   2873 C CA  . ILE B 1 76  ? -0.81000  21.02600  15.88100  1.000 40.13000 ? 78  ILE B CA  1 
ATOM   2874 C C   . ILE B 1 76  ? -0.00800  19.95700  16.60800  1.000 38.28000 ? 78  ILE B C   1 
ATOM   2875 O O   . ILE B 1 76  ? -0.07800  19.88000  17.84100  1.000 38.13000 ? 78  ILE B O   1 
ATOM   2876 C CB  . ILE B 1 76  ? -2.29000  20.98700  16.31700  1.000 39.88000 ? 78  ILE B CB  1 
ATOM   2877 C CG1 . ILE B 1 76  ? -2.93200  19.62000  16.04200  1.000 38.73000 ? 78  ILE B CG1 1 
ATOM   2878 C CG2 . ILE B 1 76  ? -3.08000  22.04700  15.58000  1.000 41.18000 ? 78  ILE B CG2 1 
ATOM   2879 C CD1 . ILE B 1 76  ? -4.35900  19.48900  16.57200  1.000 42.34000 ? 78  ILE B CD1 1 
ATOM   2880 N N   . GLY B 1 77  ? 0.76600   19.14700  15.89300  1.000 34.54000 ? 79  GLY B N   1 
ATOM   2881 C CA  . GLY B 1 77  ? 1.54500   18.10200  16.52400  1.000 37.50000 ? 79  GLY B CA  1 
ATOM   2882 C C   . GLY B 1 77  ? 2.46900   17.45800  15.51600  1.000 37.54000 ? 79  GLY B C   1 
ATOM   2883 O O   . GLY B 1 77  ? 2.24900   17.53300  14.30100  1.000 34.78000 ? 79  GLY B O   1 
ATOM   2884 N N   . HIS B 1 78  ? 3.51400   16.82300  16.03100  1.000 36.86000 ? 80  HIS B N   1 
ATOM   2885 C CA  . HIS B 1 78  ? 4.41200   16.09800  15.14700  1.000 36.44000 ? 80  HIS B CA  1 
ATOM   2886 C C   . HIS B 1 78  ? 5.03400   14.94300  15.91000  1.000 40.46000 ? 80  HIS B C   1 
ATOM   2887 O O   . HIS B 1 78  ? 5.24600   15.01500  17.12300  1.000 39.70000 ? 80  HIS B O   1 
ATOM   2888 C CB  . HIS B 1 78  ? 5.50000   17.00200  14.54400  1.000 38.74000 ? 80  HIS B CB  1 
ATOM   2889 C CG  . HIS B 1 78  ? 6.41100   17.61900  15.55800  1.000 41.16000 ? 80  HIS B CG  1 
ATOM   2890 N ND1 . HIS B 1 78  ? 6.15000   18.83500  16.15100  1.000 42.87000 ? 80  HIS B ND1 1 
ATOM   2891 C CD2 . HIS B 1 78  ? 7.58000   17.18500  16.08700  1.000 44.18000 ? 80  HIS B CD2 1 
ATOM   2892 C CE1 . HIS B 1 78  ? 7.12000   19.12400  17.00400  1.000 47.24000 ? 80  HIS B CE1 1 
ATOM   2893 N NE2 . HIS B 1 78  ? 7.99900   18.13800  16.98500  1.000 45.02000 ? 80  HIS B NE2 1 
ATOM   2894 N N   . SER B 1 79  ? 5.28900   13.86000  15.18500  1.000 36.92000 ? 81  SER B N   1 
ATOM   2895 C CA  . SER B 1 79  ? 5.95700   12.69800  15.75100  1.000 34.89000 ? 81  SER B CA  1 
ATOM   2896 C C   . SER B 1 79  ? 6.48900   11.86900  14.59700  1.000 34.12000 ? 81  SER B C   1 
ATOM   2897 O O   . SER B 1 79  ? 6.14700   12.09200  13.43200  1.000 34.64000 ? 81  SER B O   1 
ATOM   2898 C CB  . SER B 1 79  ? 5.01400   11.87200  16.62700  1.000 34.52000 ? 81  SER B CB  1 
ATOM   2899 O OG  . SER B 1 79  ? 3.88800   11.46200  15.88400  1.000 36.18000 ? 81  SER B OG  1 
ATOM   2900 N N   . MET B 1 80  ? 7.34300   10.91300  14.92900  1.000 32.54000 ? 82  MET B N   1 
ATOM   2901 C CA  . MET B 1 80  ? 7.94800   10.04600  13.93800  1.000 31.22000 ? 82  MET B CA  1 
ATOM   2902 C C   . MET B 1 80  ? 7.58400   8.60900   14.26200  1.000 29.20000 ? 82  MET B C   1 
ATOM   2903 O O   . MET B 1 80  ? 7.53500   8.22500   15.43300  1.000 30.89000 ? 82  MET B O   1 
ATOM   2904 C CB  . MET B 1 80  ? 9.47600   10.21100  13.94500  1.000 33.24000 ? 82  MET B CB  1 
ATOM   2905 C CG  . MET B 1 80  ? 10.13900  10.07000  12.61600  1.000 33.88000 ? 82  MET B CG  1 
ATOM   2906 S SD  . MET B 1 80  ? 11.80500  10.73300  12.74300  1.000 41.38000 ? 82  MET B SD  1 
ATOM   2907 C CE  . MET B 1 80  ? 12.34000  10.03700  14.30600  1.000 40.68000 ? 82  MET B CE  1 
ATOM   2908 N N   . GLN B 1 81  ? 7.32300   7.81700   13.23100  1.000 27.59000 ? 83  GLN B N   1 
ATOM   2909 C CA  . GLN B 1 81  ? 7.19500   6.37100   13.37200  1.000 28.74000 ? 83  GLN B CA  1 
ATOM   2910 C C   . GLN B 1 81  ? 8.11700   5.77200   12.33000  1.000 26.69000 ? 83  GLN B C   1 
ATOM   2911 O O   . GLN B 1 81  ? 7.82200   5.84800   11.13300  1.000 22.88000 ? 83  GLN B O   1 
ATOM   2912 C CB  . GLN B 1 81  ? 5.76000   5.88000   13.15700  1.000 29.21000 ? 83  GLN B CB  1 
ATOM   2913 C CG  . GLN B 1 81  ? 5.67800   4.34800   13.22200  1.000 28.63000 ? 83  GLN B CG  1 
ATOM   2914 C CD  . GLN B 1 81  ? 4.28300   3.81100   13.06700  1.000 34.87000 ? 83  GLN B CD  1 
ATOM   2915 O OE1 . GLN B 1 81  ? 3.39300   4.49900   12.56800  1.000 35.85000 ? 83  GLN B OE1 1 
ATOM   2916 N NE2 . GLN B 1 81  ? 4.07400   2.57000   13.50400  1.000 36.05000 ? 83  GLN B NE2 1 
ATOM   2917 N N   . ASN B 1 82  ? 9.24300   5.21700   12.77600  1.000 28.68000 ? 84  ASN B N   1 
ATOM   2918 C CA  . ASN B 1 82  ? 10.22800  4.65300   11.85700  1.000 25.06000 ? 84  ASN B CA  1 
ATOM   2919 C C   . ASN B 1 82  ? 10.60000  5.75300   10.86400  1.000 28.29000 ? 84  ASN B C   1 
ATOM   2920 O O   . ASN B 1 82  ? 10.93500  6.86200   11.30900  1.000 26.41000 ? 84  ASN B O   1 
ATOM   2921 C CB  . ASN B 1 82  ? 9.66800   3.38000   11.25900  1.000 24.65000 ? 84  ASN B CB  1 
ATOM   2922 C CG  . ASN B 1 82  ? 9.31700   2.34700   12.31700  1.000 27.59000 ? 84  ASN B CG  1 
ATOM   2923 O OD1 . ASN B 1 82  ? 10.08700  2.11500   13.23900  1.000 28.87000 ? 84  ASN B OD1 1 
ATOM   2924 N ND2 . ASN B 1 82  ? 8.13700   1.73300   12.19700  1.000 25.73000 ? 84  ASN B ND2 1 
ATOM   2925 N N   . CYS B 1 83  ? 10.51000  5.52300   9.54900   1.000 23.83000 ? 85  CYS B N   1 
ATOM   2926 C CA  . CYS B 1 83  ? 10.95100  6.52500   8.59000   1.000 25.99000 ? 85  CYS B CA  1 
ATOM   2927 C C   . CYS B 1 83  ? 9.80700   7.39200   8.06400   1.000 25.48000 ? 85  CYS B C   1 
ATOM   2928 O O   . CYS B 1 83  ? 9.95600   8.03400   7.02100   1.000 28.13000 ? 85  CYS B O   1 
ATOM   2929 C CB  . CYS B 1 83  ? 11.68800  5.86200   7.42600   1.000 27.92000 ? 85  CYS B CB  1 
ATOM   2930 S SG  . CYS B 1 83  ? 13.12300  4.85200   7.91100   1.000 27.96000 ? 85  CYS B SG  1 
ATOM   2931 N N   . VAL B 1 84  ? 8.67800   7.43900   8.76500   1.000 25.72000 ? 86  VAL B N   1 
ATOM   2932 C CA  . VAL B 1 84  ? 7.54200   8.26100   8.36200   1.000 26.66000 ? 86  VAL B CA  1 
ATOM   2933 C C   . VAL B 1 84  ? 7.30600   9.33800   9.41200   1.000 26.72000 ? 86  VAL B C   1 
ATOM   2934 O O   . VAL B 1 84  ? 7.23700   9.04600   10.61400  1.000 27.36000 ? 86  VAL B O   1 
ATOM   2935 C CB  . VAL B 1 84  ? 6.28200   7.40800   8.12700   1.000 26.52000 ? 86  VAL B CB  1 
ATOM   2936 C CG1 . VAL B 1 84  ? 4.99100   8.21500   8.37700   1.000 29.60000 ? 86  VAL B CG1 1 
ATOM   2937 C CG2 . VAL B 1 84  ? 6.30700   6.88500   6.69000   1.000 26.99000 ? 86  VAL B CG2 1 
ATOM   2938 N N   . LEU B 1 85  ? 7.19800   10.58200  8.95600   1.000 24.77000 ? 87  LEU B N   1 
ATOM   2939 C CA  . LEU B 1 85  ? 6.79800   11.69300  9.81200   1.000 26.48000 ? 87  LEU B CA  1 
ATOM   2940 C C   . LEU B 1 85  ? 5.27300   11.76800  9.85500   1.000 26.44000 ? 87  LEU B C   1 
ATOM   2941 O O   . LEU B 1 85  ? 4.61500   11.64500  8.82000   1.000 25.96000 ? 87  LEU B O   1 
ATOM   2942 C CB  . LEU B 1 85  ? 7.39600   13.00000  9.27400   1.000 25.54000 ? 87  LEU B CB  1 
ATOM   2943 C CG  . LEU B 1 85  ? 7.10800   14.29000  10.04900  1.000 32.28000 ? 87  LEU B CG  1 
ATOM   2944 C CD1 . LEU B 1 85  ? 7.81600   14.27100  11.39100  1.000 36.94000 ? 87  LEU B CD1 1 
ATOM   2945 C CD2 . LEU B 1 85  ? 7.53700   15.52300  9.23200   1.000 30.22000 ? 87  LEU B CD2 1 
ATOM   2946 N N   . LYS B 1 86  ? 4.71000   11.94300  11.06000  1.000 26.23000 ? 88  LYS B N   1 
ATOM   2947 C CA  . LYS B 1 86  ? 3.26200   12.05700  11.24900  1.000 26.06000 ? 88  LYS B CA  1 
ATOM   2948 C C   . LYS B 1 86  ? 2.95200   13.45900  11.76000  1.000 30.90000 ? 88  LYS B C   1 
ATOM   2949 O O   . LYS B 1 86  ? 3.36500   13.82800  12.86500  1.000 31.46000 ? 88  LYS B O   1 
ATOM   2950 C CB  . LYS B 1 86  ? 2.74800   10.99400  12.21900  1.000 30.96000 ? 88  LYS B CB  1 
ATOM   2951 C CG  . LYS B 1 86  ? 2.76500   9.56100   11.65800  1.000 31.24000 ? 88  LYS B CG  1 
ATOM   2952 C CD  . LYS B 1 86  ? 2.83900   8.51800   12.78100  1.000 31.48000 ? 88  LYS B CD  1 
ATOM   2953 C CE  . LYS B 1 86  ? 1.50700   7.85100   13.04800  1.000 42.12000 ? 88  LYS B CE  1 
ATOM   2954 N NZ  . LYS B 1 86  ? 1.63300   6.91800   14.20300  1.000 46.55000 ? 88  LYS B NZ  1 
ATOM   2955 N N   . LEU B 1 87  ? 2.24700   14.24300  10.95300  1.000 27.51000 ? 89  LEU B N   1 
ATOM   2956 C CA  . LEU B 1 87  ? 1.88800   15.60900  11.30300  1.000 30.86000 ? 89  LEU B CA  1 
ATOM   2957 C C   . LEU B 1 87  ? 0.41800   15.62800  11.68400  1.000 31.50000 ? 89  LEU B C   1 
ATOM   2958 O O   . LEU B 1 87  ? -0.44000  15.30000  10.86100  1.000 31.60000 ? 89  LEU B O   1 
ATOM   2959 C CB  . LEU B 1 87  ? 2.15600   16.56800  10.14600  1.000 31.47000 ? 89  LEU B CB  1 
ATOM   2960 C CG  . LEU B 1 87  ? 3.62200   16.58300  9.70300   1.000 32.39000 ? 89  LEU B CG  1 
ATOM   2961 C CD1 . LEU B 1 87  ? 3.83900   17.42300  8.43600   1.000 35.46000 ? 89  LEU B CD1 1 
ATOM   2962 C CD2 . LEU B 1 87  ? 4.53400   17.04700  10.83100  1.000 30.23000 ? 89  LEU B CD2 1 
ATOM   2963 N N   . LYS B 1 88  ? 0.13900   15.97000  12.94000  1.000 31.61000 ? 90  LYS B N   1 
ATOM   2964 C CA  . LYS B 1 88  ? -1.23300  16.12700  13.40200  1.000 34.02000 ? 90  LYS B CA  1 
ATOM   2965 C C   . LYS B 1 88  ? -1.72600  17.51200  12.99600  1.000 37.10000 ? 90  LYS B C   1 
ATOM   2966 O O   . LYS B 1 88  ? -1.05800  18.51900  13.25700  1.000 34.22000 ? 90  LYS B O   1 
ATOM   2967 C CB  . LYS B 1 88  ? -1.32000  15.93100  14.92100  1.000 34.15000 ? 90  LYS B CB  1 
ATOM   2968 C CG  . LYS B 1 88  ? -2.74500  15.69600  15.44800  1.000 35.22000 ? 90  LYS B CG  1 
ATOM   2969 C CD  . LYS B 1 88  ? -2.87100  14.32000  16.11300  1.000 43.03000 ? 90  LYS B CD  1 
ATOM   2970 C CE  . LYS B 1 88  ? -4.32000  13.84100  16.22900  1.000 43.58000 ? 90  LYS B CE  1 
ATOM   2971 N NZ  . LYS B 1 88  ? -4.56100  12.40600  15.84500  1.000 39.47000 ? 90  LYS B NZ  1 
ATOM   2972 N N   . VAL B 1 89  ? -2.88100  17.56500  12.33500  1.000 34.63000 ? 91  VAL B N   1 
ATOM   2973 C CA  . VAL B 1 89  ? -3.42400  18.82500  11.85400  1.000 36.76000 ? 91  VAL B CA  1 
ATOM   2974 C C   . VAL B 1 89  ? -4.75900  19.08200  12.55400  1.000 35.87000 ? 91  VAL B C   1 
ATOM   2975 O O   . VAL B 1 89  ? -5.32600  18.20800  13.21200  1.000 36.22000 ? 91  VAL B O   1 
ATOM   2976 C CB  . VAL B 1 89  ? -3.56300  18.85200  10.32000  1.000 37.05000 ? 91  VAL B CB  1 
ATOM   2977 C CG1 . VAL B 1 89  ? -2.18100  18.81600  9.67100   1.000 36.38000 ? 91  VAL B CG1 1 
ATOM   2978 C CG2 . VAL B 1 89  ? -4.40000  17.67800  9.82600   1.000 35.31000 ? 91  VAL B CG2 1 
ATOM   2979 N N   . ASP B 1 90  ? -5.24000  20.31900  12.43200  1.000 39.47000 ? 92  ASP B N   1 
ATOM   2980 C CA  . ASP B 1 90  ? -6.42300  20.74000  13.17400  1.000 41.22000 ? 92  ASP B CA  1 
ATOM   2981 C C   . ASP B 1 90  ? -7.72400  20.26400  12.54100  1.000 45.36000 ? 92  ASP B C   1 
ATOM   2982 O O   . ASP B 1 90  ? -8.77400  20.33200  13.18700  1.000 41.63000 ? 92  ASP B O   1 
ATOM   2983 C CB  . ASP B 1 90  ? -6.44800  22.26700  13.29800  1.000 44.04000 ? 92  ASP B CB  1 
ATOM   2984 C CG  . ASP B 1 90  ? -6.35200  22.97300  11.94400  1.000 50.52000 ? 92  ASP B CG  1 
ATOM   2985 O OD1 . ASP B 1 90  ? -6.54700  22.33000  10.88300  1.000 49.00000 ? 92  ASP B OD1 1 
ATOM   2986 O OD2 . ASP B 1 90  ? -6.07600  24.19300  11.94000  1.000 54.99000 ? 92  ASP B OD2 1 
ATOM   2987 N N   . THR B 1 91  ? -7.68000  19.79600  11.29700  1.000 44.52000 ? 93  THR B N   1 
ATOM   2988 C CA  . THR B 1 91  ? -8.87600  19.45400  10.53800  1.000 42.90000 ? 93  THR B CA  1 
ATOM   2989 C C   . THR B 1 91  ? -8.78100  18.01600  10.05600  1.000 41.59000 ? 93  THR B C   1 
ATOM   2990 O O   . THR B 1 91  ? -7.79500  17.64000  9.41200   1.000 34.30000 ? 93  THR B O   1 
ATOM   2991 C CB  . THR B 1 91  ? -9.04100  20.38600  9.33700   1.000 44.33000 ? 93  THR B CB  1 
ATOM   2992 O OG1 . THR B 1 91  ? -9.03300  21.74700  9.78500   1.000 47.68000 ? 93  THR B OG1 1 
ATOM   2993 C CG2 . THR B 1 91  ? -10.34600 20.09500  8.60800   1.000 42.22000 ? 93  THR B CG2 1 
ATOM   2994 N N   . ALA B 1 92  ? -9.79700  17.21600  10.36800  1.000 37.39000 ? 94  ALA B N   1 
ATOM   2995 C CA  . ALA B 1 92  ? -9.89500  15.89400  9.77400   1.000 36.15000 ? 94  ALA B CA  1 
ATOM   2996 C C   . ALA B 1 92  ? -10.21100 16.02900  8.28500   1.000 38.25000 ? 94  ALA B C   1 
ATOM   2997 O O   . ALA B 1 92  ? -11.00700 16.88000  7.87800   1.000 39.01000 ? 94  ALA B O   1 
ATOM   2998 C CB  . ALA B 1 92  ? -10.96500 15.06800  10.49000  1.000 35.76000 ? 94  ALA B CB  1 
ATOM   2999 N N   . ASN B 1 93  ? -9.54000  15.21800  7.46100   1.000 33.01000 ? 95  ASN B N   1 
ATOM   3000 C CA  . ASN B 1 93  ? -9.82900  15.17300  6.03100   1.000 33.40000 ? 95  ASN B CA  1 
ATOM   3001 C C   . ASN B 1 93  ? -11.25700 14.68700  5.84200   1.000 29.70000 ? 95  ASN B C   1 
ATOM   3002 O O   . ASN B 1 93  ? -11.55300 13.52900  6.14900   1.000 29.71000 ? 95  ASN B O   1 
ATOM   3003 C CB  . ASN B 1 93  ? -8.84000  14.25100  5.30100   1.000 28.56000 ? 95  ASN B CB  1 
ATOM   3004 C CG  . ASN B 1 93  ? -9.05600  14.21200  3.78200   1.000 33.91000 ? 95  ASN B CG  1 
ATOM   3005 O OD1 . ASN B 1 93  ? -10.00700 14.79300  3.24300   1.000 33.61000 ? 95  ASN B OD1 1 
ATOM   3006 N ND2 . ASN B 1 93  ? -8.16400  13.50700  3.08600   1.000 32.77000 ? 95  ASN B ND2 1 
ATOM   3007 N N   . PRO B 1 94  ? -12.16600 15.53100  5.33600   1.000 34.99000 ? 96  PRO B N   1 
ATOM   3008 C CA  . PRO B 1 94  ? -13.56500 15.09600  5.16700   1.000 33.02000 ? 96  PRO B CA  1 
ATOM   3009 C C   . PRO B 1 94  ? -13.77600 14.10600  4.03000   1.000 33.23000 ? 96  PRO B C   1 
ATOM   3010 O O   . PRO B 1 94  ? -14.89700 13.58800  3.88500   1.000 31.94000 ? 96  PRO B O   1 
ATOM   3011 C CB  . PRO B 1 94  ? -14.30900 16.41200  4.89500   1.000 36.66000 ? 96  PRO B CB  1 
ATOM   3012 C CG  . PRO B 1 94  ? -13.28400 17.27000  4.21500   1.000 36.63000 ? 96  PRO B CG  1 
ATOM   3013 C CD  . PRO B 1 94  ? -11.93100 16.88100  4.79500   1.000 33.54000 ? 96  PRO B CD  1 
ATOM   3014 N N   . LYS B 1 95  ? -12.77000 13.85600  3.19500   1.000 29.80000 ? 97  LYS B N   1 
ATOM   3015 C CA  . LYS B 1 95  ? -12.83500 12.81700  2.17500   1.000 32.24000 ? 97  LYS B CA  1 
ATOM   3016 C C   . LYS B 1 95  ? -11.93800 11.62500  2.51000   1.000 32.52000 ? 97  LYS B C   1 
ATOM   3017 O O   . LYS B 1 95  ? -11.49600 10.91000  1.61000   1.000 33.06000 ? 97  LYS B O   1 
ATOM   3018 C CB  . LYS B 1 95  ? -12.46400 13.37900  0.80200   1.000 34.06000 ? 97  LYS B CB  1 
ATOM   3019 C CG  . LYS B 1 95  ? -13.48100 14.35800  0.22300   1.000 38.07000 ? 97  LYS B CG  1 
ATOM   3020 C CD  . LYS B 1 95  ? -12.80500 15.62400  -0.23800  1.000 42.33000 ? 97  LYS B CD  1 
ATOM   3021 C CE  . LYS B 1 95  ? -13.65400 16.36800  -1.24000  1.000 47.05000 ? 97  LYS B CE  1 
ATOM   3022 N NZ  . LYS B 1 95  ? -13.52300 15.75500  -2.58800  1.000 50.86000 ? 97  LYS B NZ  1 
ATOM   3023 N N   . THR B 1 96  ? -11.66400 11.39300  3.78800   1.000 30.01000 ? 98  THR B N   1 
ATOM   3024 C CA  . THR B 1 96  ? -10.93500 10.18900  4.17200   1.000 28.09000 ? 98  THR B CA  1 
ATOM   3025 C C   . THR B 1 96  ? -11.70300 8.93800   3.74700   1.000 29.45000 ? 98  THR B C   1 
ATOM   3026 O O   . THR B 1 96  ? -12.87000 8.76400   4.14800   1.000 28.77000 ? 98  THR B O   1 
ATOM   3027 C CB  . THR B 1 96  ? -10.67700 10.17200  5.67800   1.000 32.19000 ? 98  THR B CB  1 
ATOM   3028 O OG1 . THR B 1 96  ? -10.07100 11.41000  6.06600   1.000 30.52000 ? 98  THR B OG1 1 
ATOM   3029 C CG2 . THR B 1 96  ? -9.71200  9.04300   6.03800   1.000 30.41000 ? 98  THR B CG2 1 
ATOM   3030 N N   . PRO B 1 97  ? -11.11500 8.06200   2.93800   1.000 28.45000 ? 99  PRO B N   1 
ATOM   3031 C CA  . PRO B 1 97  ? -11.80500 6.82400   2.55400   1.000 29.28000 ? 99  PRO B CA  1 
ATOM   3032 C C   . PRO B 1 97  ? -11.72700 5.78700   3.66500   1.000 29.16000 ? 99  PRO B C   1 
ATOM   3033 O O   . PRO B 1 97  ? -10.95100 5.91500   4.61400   1.000 28.78000 ? 99  PRO B O   1 
ATOM   3034 C CB  . PRO B 1 97  ? -11.02600 6.36000   1.31700   1.000 30.04000 ? 99  PRO B CB  1 
ATOM   3035 C CG  . PRO B 1 97  ? -9.61000  6.90400   1.54100   1.000 29.43000 ? 99  PRO B CG  1 
ATOM   3036 C CD  . PRO B 1 97  ? -9.77900  8.19200   2.31700   1.000 26.18000 ? 99  PRO B CD  1 
ATOM   3037 N N   . LYS B 1 98  ? -12.55900 4.74600   3.55100   1.000 26.75000 ? 100 LYS B N   1 
ATOM   3038 C CA  . LYS B 1 98  ? -12.26500 3.53000   4.30500   1.000 28.67000 ? 100 LYS B CA  1 
ATOM   3039 C C   . LYS B 1 98  ? -10.87800 3.04700   3.88400   1.000 24.74000 ? 100 LYS B C   1 
ATOM   3040 O O   . LYS B 1 98  ? -10.59100 2.95100   2.68700   1.000 26.80000 ? 100 LYS B O   1 
ATOM   3041 C CB  . LYS B 1 98  ? -13.30000 2.43900   4.03700   1.000 27.84000 ? 100 LYS B CB  1 
ATOM   3042 N N   . TYR B 1 99  ? -10.01500 2.75100   4.85300   1.000 26.02000 ? 101 TYR B N   1 
ATOM   3043 C CA  . TYR B 1 99  ? -8.63500  2.41800   4.47100   1.000 24.91000 ? 101 TYR B CA  1 
ATOM   3044 C C   . TYR B 1 99  ? -7.97700  1.51900   5.50900   1.000 27.87000 ? 101 TYR B C   1 
ATOM   3045 O O   . TYR B 1 99  ? -8.36600  1.49700   6.68200   1.000 25.51000 ? 101 TYR B O   1 
ATOM   3046 C CB  . TYR B 1 99  ? -7.77400  3.68500   4.26000   1.000 27.88000 ? 101 TYR B CB  1 
ATOM   3047 C CG  . TYR B 1 99  ? -7.29500  4.34600   5.55200   1.000 28.43000 ? 101 TYR B CG  1 
ATOM   3048 C CD1 . TYR B 1 99  ? -8.06400  5.31000   6.18500   1.000 28.12000 ? 101 TYR B CD1 1 
ATOM   3049 C CD2 . TYR B 1 99  ? -6.09500  3.99400   6.13700   1.000 28.51000 ? 101 TYR B CD2 1 
ATOM   3050 C CE1 . TYR B 1 99  ? -7.65300  5.89800   7.36200   1.000 28.39000 ? 101 TYR B CE1 1 
ATOM   3051 C CE2 . TYR B 1 99  ? -5.67400  4.58500   7.32100   1.000 26.42000 ? 101 TYR B CE2 1 
ATOM   3052 C CZ  . TYR B 1 99  ? -6.44300  5.53600   7.91600   1.000 28.68000 ? 101 TYR B CZ  1 
ATOM   3053 O OH  . TYR B 1 99  ? -6.03400  6.12700   9.08600   1.000 26.70000 ? 101 TYR B OH  1 
ATOM   3054 N N   . LYS B 1 100 ? -6.94100  0.79400   5.05300   1.000 27.69000 ? 102 LYS B N   1 
ATOM   3055 C CA  . LYS B 1 100 ? -6.02300  0.06100   5.91400   1.000 29.24000 ? 102 LYS B CA  1 
ATOM   3056 C C   . LYS B 1 100 ? -4.58800  0.34100   5.48300   1.000 25.04000 ? 102 LYS B C   1 
ATOM   3057 O O   . LYS B 1 100 ? -4.31400  0.65400   4.31600   1.000 23.06000 ? 102 LYS B O   1 
ATOM   3058 C CB  . LYS B 1 100 ? -6.22700  -1.46500  5.87300   1.000 30.75000 ? 102 LYS B CB  1 
ATOM   3059 C CG  . LYS B 1 100 ? -7.64700  -1.96600  5.72500   1.000 38.24000 ? 102 LYS B CG  1 
ATOM   3060 C CD  . LYS B 1 100 ? -7.61900  -3.47400  5.45000   1.000 39.33000 ? 102 LYS B CD  1 
ATOM   3061 C CE  . LYS B 1 100 ? -8.96800  -3.96400  4.92300   1.000 48.35000 ? 102 LYS B CE  1 
ATOM   3062 N NZ  . LYS B 1 100 ? -9.44900  -5.15600  5.67300   1.000 50.35000 ? 102 LYS B NZ  1 
ATOM   3063 N N   . PHE B 1 101 ? -3.66800  0.20900   6.43400   1.000 26.21000 ? 103 PHE B N   1 
ATOM   3064 C CA  . PHE B 1 101 ? -2.24000  0.16100   6.13100   1.000 24.45000 ? 103 PHE B CA  1 
ATOM   3065 C C   . PHE B 1 101 ? -1.83600  -1.30700  6.05900   1.000 28.11000 ? 103 PHE B C   1 
ATOM   3066 O O   . PHE B 1 101 ? -2.07400  -2.06300  7.00900   1.000 29.61000 ? 103 PHE B O   1 
ATOM   3067 C CB  . PHE B 1 101 ? -1.40400  0.87700   7.19400   1.000 25.65000 ? 103 PHE B CB  1 
ATOM   3068 C CG  . PHE B 1 101 ? -1.54600  2.37500   7.19700   1.000 26.15000 ? 103 PHE B CG  1 
ATOM   3069 C CD1 . PHE B 1 101 ? -2.16500  3.04100   6.14700   1.000 22.73000 ? 103 PHE B CD1 1 
ATOM   3070 C CD2 . PHE B 1 101 ? -1.03500  3.11600   8.26600   1.000 26.79000 ? 103 PHE B CD2 1 
ATOM   3071 C CE1 . PHE B 1 101 ? -2.28000  4.44200   6.16100   1.000 27.36000 ? 103 PHE B CE1 1 
ATOM   3072 C CE2 . PHE B 1 101 ? -1.14100  4.49700   8.29600   1.000 25.24000 ? 103 PHE B CE2 1 
ATOM   3073 C CZ  . PHE B 1 101 ? -1.75200  5.16600   7.24300   1.000 26.89000 ? 103 PHE B CZ  1 
ATOM   3074 N N   . VAL B 1 102 ? -1.27700  -1.72100  4.92500   1.000 24.94000 ? 104 VAL B N   1 
ATOM   3075 C CA  . VAL B 1 102 ? -0.86600  -3.10600  4.72700   1.000 24.11000 ? 104 VAL B CA  1 
ATOM   3076 C C   . VAL B 1 102 ? 0.57100   -3.12000  4.23800   1.000 25.53000 ? 104 VAL B C   1 
ATOM   3077 O O   . VAL B 1 102 ? 1.04300   -2.17400  3.60000   1.000 28.83000 ? 104 VAL B O   1 
ATOM   3078 C CB  . VAL B 1 102 ? -1.77500  -3.85500  3.72600   1.000 24.53000 ? 104 VAL B CB  1 
ATOM   3079 C CG1 . VAL B 1 102 ? -3.26400  -3.67800  4.10500   1.000 27.04000 ? 104 VAL B CG1 1 
ATOM   3080 C CG2 . VAL B 1 102 ? -1.50500  -3.40100  2.31500   1.000 25.15000 ? 104 VAL B CG2 1 
ATOM   3081 N N   . ARG B 1 103 ? 1.27000   -4.19800  4.53100   1.000 24.10000 ? 105 ARG B N   1 
ATOM   3082 C CA  . ARG B 1 103 ? 2.62800   -4.38500  4.03200   1.000 22.59000 ? 105 ARG B CA  1 
ATOM   3083 C C   . ARG B 1 103 ? 2.61100   -5.55300  3.05900   1.000 27.54000 ? 105 ARG B C   1 
ATOM   3084 O O   . ARG B 1 103 ? 2.17400   -6.64900  3.42300   1.000 28.86000 ? 105 ARG B O   1 
ATOM   3085 C CB  . ARG B 1 103 ? 3.60200   -4.64100  5.18200   1.000 26.63000 ? 105 ARG B CB  1 
ATOM   3086 C CG  . ARG B 1 103 ? 5.02300   -4.88600  4.70100   1.000 24.41000 ? 105 ARG B CG  1 
ATOM   3087 C CD  . ARG B 1 103 ? 6.00400   -5.02600  5.86100   1.000 25.97000 ? 105 ARG B CD  1 
ATOM   3088 N NE  . ARG B 1 103 ? 7.37500   -5.19600  5.36900   1.000 24.62000 ? 105 ARG B NE  1 
ATOM   3089 C CZ  . ARG B 1 103 ? 8.18400   -4.18700  5.05300   1.000 28.25000 ? 105 ARG B CZ  1 
ATOM   3090 N NH1 . ARG B 1 103 ? 7.76300   -2.93500  5.17100   1.000 23.62000 ? 105 ARG B NH1 1 
ATOM   3091 N NH2 . ARG B 1 103 ? 9.41700   -4.43000  4.61300   1.000 26.32000 ? 105 ARG B NH2 1 
ATOM   3092 N N   . ILE B 1 104 ? 3.05000   -5.32500  1.82500   1.000 24.94000 ? 106 ILE B N   1 
ATOM   3093 C CA  . ILE B 1 104 ? 2.94000   -6.33600  0.78300   1.000 30.29000 ? 106 ILE B CA  1 
ATOM   3094 C C   . ILE B 1 104 ? 4.24200   -7.12200  0.68400   1.000 33.03000 ? 106 ILE B C   1 
ATOM   3095 O O   . ILE B 1 104 ? 5.24300   -6.79100  1.31600   1.000 29.60000 ? 106 ILE B O   1 
ATOM   3096 C CB  . ILE B 1 104 ? 2.53600   -5.72400  -0.57900  1.000 30.05000 ? 106 ILE B CB  1 
ATOM   3097 C CG1 . ILE B 1 104 ? 3.51700   -4.62600  -1.00600  1.000 28.91000 ? 106 ILE B CG1 1 
ATOM   3098 C CG2 . ILE B 1 104 ? 1.09100   -5.21400  -0.50100  1.000 29.81000 ? 106 ILE B CG2 1 
ATOM   3099 C CD1 . ILE B 1 104 ? 3.51700   -4.36800  -2.49700  1.000 29.42000 ? 106 ILE B CD1 1 
ATOM   3100 N N   . GLN B 1 105 ? 4.21300   -8.20700  -0.08700  1.000 31.89000 ? 107 GLN B N   1 
ATOM   3101 C CA  . GLN B 1 105 ? 5.35000   -9.08200  -0.35200  1.000 31.60000 ? 107 GLN B CA  1 
ATOM   3102 C C   . GLN B 1 105 ? 5.87400   -8.86200  -1.76000  1.000 29.26000 ? 107 GLN B C   1 
ATOM   3103 O O   . GLN B 1 105 ? 5.12900   -8.43100  -2.64900  1.000 29.78000 ? 107 GLN B O   1 
ATOM   3104 C CB  . GLN B 1 105 ? 4.95600   -10.56100 -0.21900  1.000 34.42000 ? 107 GLN B CB  1 
ATOM   3105 C CG  . GLN B 1 105 ? 3.98000   -10.85800 0.88900   1.000 43.40000 ? 107 GLN B CG  1 
ATOM   3106 C CD  . GLN B 1 105 ? 4.63900   -10.83100 2.24200   1.000 43.95000 ? 107 GLN B CD  1 
ATOM   3107 O OE1 . GLN B 1 105 ? 5.58700   -11.57300 2.50600   1.000 51.72000 ? 107 GLN B OE1 1 
ATOM   3108 N NE2 . GLN B 1 105 ? 4.13500   -9.96700  3.12000   1.000 46.98000 ? 107 GLN B NE2 1 
ATOM   3109 N N   . PRO B 1 106 ? 7.14300   -9.18200  -2.01500  1.000 32.05000 ? 108 PRO B N   1 
ATOM   3110 C CA  . PRO B 1 106 ? 7.64300   -9.13900  -3.39300  1.000 30.38000 ? 108 PRO B CA  1 
ATOM   3111 C C   . PRO B 1 106 ? 6.79300   -9.99900  -4.31000  1.000 28.44000 ? 108 PRO B C   1 
ATOM   3112 O O   . PRO B 1 106 ? 6.35100   -11.08700 -3.93800  1.000 30.27000 ? 108 PRO B O   1 
ATOM   3113 C CB  . PRO B 1 106 ? 9.06800   -9.69300  -3.27500  1.000 28.52000 ? 108 PRO B CB  1 
ATOM   3114 C CG  . PRO B 1 106 ? 9.46200   -9.44300  -1.87900  1.000 29.86000 ? 108 PRO B CG  1 
ATOM   3115 C CD  . PRO B 1 106 ? 8.19700   -9.56300  -1.05600  1.000 30.76000 ? 108 PRO B CD  1 
ATOM   3116 N N   . GLY B 1 107 ? 6.56100   -9.49700  -5.52000  1.000 29.35000 ? 109 GLY B N   1 
ATOM   3117 C CA  . GLY B 1 107 ? 5.67600   -10.13600 -6.46100  1.000 26.08000 ? 109 GLY B CA  1 
ATOM   3118 C C   . GLY B 1 107 ? 4.27700   -9.56700  -6.48800  1.000 29.50000 ? 109 GLY B C   1 
ATOM   3119 O O   . GLY B 1 107 ? 3.55500   -9.78500  -7.46600  1.000 32.03000 ? 109 GLY B O   1 
ATOM   3120 N N   . GLN B 1 108 ? 3.87000   -8.85000  -5.44300  1.000 26.66000 ? 110 GLN B N   1 
ATOM   3121 C CA  . GLN B 1 108 ? 2.53600   -8.28000  -5.40100  1.000 27.96000 ? 110 GLN B CA  1 
ATOM   3122 C C   . GLN B 1 108 ? 2.52300   -6.94200  -6.12100  1.000 28.61000 ? 110 GLN B C   1 
ATOM   3123 O O   . GLN B 1 108 ? 3.53300   -6.23800  -6.18900  1.000 25.92000 ? 110 GLN B O   1 
ATOM   3124 C CB  . GLN B 1 108 ? 2.05100   -8.09600  -3.96200  1.000 30.18000 ? 110 GLN B CB  1 
ATOM   3125 C CG  . GLN B 1 108 ? 1.84500   -9.40400  -3.20200  1.000 36.07000 ? 110 GLN B CG  1 
ATOM   3126 C CD  . GLN B 1 108 ? 1.21300   -9.18200  -1.83000  1.000 35.53000 ? 110 GLN B CD  1 
ATOM   3127 O OE1 . GLN B 1 108 ? 1.89200   -9.22300  -0.81100  1.000 39.02000 ? 110 GLN B OE1 1 
ATOM   3128 N NE2 . GLN B 1 108 ? -0.09500  -8.94900  -1.80800  1.000 45.00000 ? 110 GLN B NE2 1 
ATOM   3129 N N   . THR B 1 109 ? 1.36300   -6.59900  -6.66700  1.000 26.28000 ? 111 THR B N   1 
ATOM   3130 C CA  . THR B 1 109 ? 1.23000   -5.40800  -7.49300  1.000 28.45000 ? 111 THR B CA  1 
ATOM   3131 C C   . THR B 1 109 ? 0.41100   -4.35400  -6.75100  1.000 28.72000 ? 111 THR B C   1 
ATOM   3132 O O   . THR B 1 109 ? -0.22200  -4.63300  -5.73100  1.000 25.92000 ? 111 THR B O   1 
ATOM   3133 C CB  . THR B 1 109 ? 0.57500   -5.75500  -8.83400  1.000 28.44000 ? 111 THR B CB  1 
ATOM   3134 O OG1 . THR B 1 109 ? -0.66400  -6.42700  -8.58700  1.000 29.61000 ? 111 THR B OG1 1 
ATOM   3135 C CG2 . THR B 1 109 ? 1.50600   -6.66600  -9.64900  1.000 28.85000 ? 111 THR B CG2 1 
ATOM   3136 N N   . PHE B 1 110 ? 0.46400   -3.12200  -7.25600  1.000 26.41000 ? 112 PHE B N   1 
ATOM   3137 C CA  . PHE B 1 110 ? -0.29600  -2.03000  -6.66100  1.000 28.40000 ? 112 PHE B CA  1 
ATOM   3138 C C   . PHE B 1 110 ? -0.30300  -0.86900  -7.64300  1.000 26.09000 ? 112 PHE B C   1 
ATOM   3139 O O   . PHE B 1 110 ? 0.51500   -0.81000  -8.56200  1.000 25.88000 ? 112 PHE B O   1 
ATOM   3140 C CB  . PHE B 1 110 ? 0.28100   -1.59100  -5.30400  1.000 24.02000 ? 112 PHE B CB  1 
ATOM   3141 C CG  . PHE B 1 110 ? 1.75500   -1.24800  -5.33000  1.000 25.95000 ? 112 PHE B CG  1 
ATOM   3142 C CD1 . PHE B 1 110 ? 2.71700   -2.23600  -5.18400  1.000 25.48000 ? 112 PHE B CD1 1 
ATOM   3143 C CD2 . PHE B 1 110 ? 2.17500   0.06300   -5.45300  1.000 22.60000 ? 112 PHE B CD2 1 
ATOM   3144 C CE1 . PHE B 1 110 ? 4.06600   -1.91400  -5.18400  1.000 29.48000 ? 112 PHE B CE1 1 
ATOM   3145 C CE2 . PHE B 1 110 ? 3.51900   0.38300   -5.44900  1.000 29.38000 ? 112 PHE B CE2 1 
ATOM   3146 C CZ  . PHE B 1 110 ? 4.46700   -0.60400  -5.31900  1.000 27.90000 ? 112 PHE B CZ  1 
ATOM   3147 N N   . SER B 1 111 ? -1.25000  0.04000   -7.44600  1.000 25.53000 ? 113 SER B N   1 
ATOM   3148 C CA  . SER B 1 111 ? -1.30900  1.26000   -8.23300  1.000 22.87000 ? 113 SER B CA  1 
ATOM   3149 C C   . SER B 1 111 ? -0.50900  2.33300   -7.51700  1.000 21.96000 ? 113 SER B C   1 
ATOM   3150 O O   . SER B 1 111 ? -0.56100  2.43600   -6.29500  1.000 22.69000 ? 113 SER B O   1 
ATOM   3151 C CB  . SER B 1 111 ? -2.75300  1.72200   -8.40900  1.000 23.30000 ? 113 SER B CB  1 
ATOM   3152 O OG  . SER B 1 111 ? -3.45500  0.75600   -9.15200  1.000 25.18000 ? 113 SER B OG  1 
ATOM   3153 N N   . VAL B 1 112 ? 0.20700   3.14200   -8.28400  1.000 25.66000 ? 114 VAL B N   1 
ATOM   3154 C CA  . VAL B 1 112 ? 0.94700   4.28300   -7.76300  1.000 23.44000 ? 114 VAL B CA  1 
ATOM   3155 C C   . VAL B 1 112 ? 0.29200   5.54800   -8.29800  1.000 26.35000 ? 114 VAL B C   1 
ATOM   3156 O O   . VAL B 1 112 ? 0.07800   5.67700   -9.51000  1.000 28.56000 ? 114 VAL B O   1 
ATOM   3157 C CB  . VAL B 1 112 ? 2.42300   4.21800   -8.17900  1.000 28.69000 ? 114 VAL B CB  1 
ATOM   3158 C CG1 . VAL B 1 112 ? 3.12200   5.52000   -7.82500  1.000 28.57000 ? 114 VAL B CG1 1 
ATOM   3159 C CG2 . VAL B 1 112 ? 3.09100   3.02900   -7.50000  1.000 26.75000 ? 114 VAL B CG2 1 
ATOM   3160 N N   . LEU B 1 113 ? -0.01700  6.47400   -7.40800  1.000 23.03000 ? 115 LEU B N   1 
ATOM   3161 C CA  . LEU B 1 113 ? -0.46500  7.81200   -7.78800  1.000 25.43000 ? 115 LEU B CA  1 
ATOM   3162 C C   . LEU B 1 113 ? 0.72200   8.76400   -7.64900  1.000 25.76000 ? 115 LEU B C   1 
ATOM   3163 O O   . LEU B 1 113 ? 1.03600   9.22600   -6.54600  1.000 25.63000 ? 115 LEU B O   1 
ATOM   3164 C CB  . LEU B 1 113 ? -1.62400  8.25700   -6.91400  1.000 26.44000 ? 115 LEU B CB  1 
ATOM   3165 C CG  . LEU B 1 113 ? -2.25100  9.58200   -7.33400  1.000 29.05000 ? 115 LEU B CG  1 
ATOM   3166 C CD1 . LEU B 1 113 ? -2.88300  9.46900   -8.72300  1.000 24.33000 ? 115 LEU B CD1 1 
ATOM   3167 C CD2 . LEU B 1 113 ? -3.28400  9.96600   -6.31200  1.000 27.02000 ? 115 LEU B CD2 1 
ATOM   3168 N N   . ALA B 1 114 ? 1.35900   9.07800   -8.77400  1.000 26.35000 ? 116 ALA B N   1 
ATOM   3169 C CA  . ALA B 1 114 ? 2.51400   9.96900   -8.78000  1.000 27.19000 ? 116 ALA B CA  1 
ATOM   3170 C C   . ALA B 1 114 ? 2.06600   11.41700  -8.59300  1.000 30.90000 ? 116 ALA B C   1 
ATOM   3171 O O   . ALA B 1 114 ? 1.17500   11.89900  -9.30500  1.000 30.96000 ? 116 ALA B O   1 
ATOM   3172 C CB  . ALA B 1 114 ? 3.28500   9.81300   -10.08900 1.000 28.11000 ? 116 ALA B CB  1 
ATOM   3173 N N   . CYS B 1 115 ? 2.66600   12.10100  -7.61800  1.000 27.95000 ? 117 CYS B N   1 
ATOM   3174 C CA  . CYS B 1 115 ? 2.28200   13.46500  -7.26800  1.000 30.29000 ? 117 CYS B CA  1 
ATOM   3175 C C   . CYS B 1 115 ? 3.50800   14.35300  -7.17600  1.000 31.21000 ? 117 CYS B C   1 
ATOM   3176 O O   . CYS B 1 115 ? 4.62300   13.88700  -6.93400  1.000 31.11000 ? 117 CYS B O   1 
ATOM   3177 C CB  . CYS B 1 115 ? 1.54500   13.53900  -5.92700  1.000 31.30000 ? 117 CYS B CB  1 
ATOM   3178 S SG  . CYS B 1 115 ? 0.10900   12.51200  -5.81700  1.000 34.62000 ? 117 CYS B SG  1 
ATOM   3179 N N   . TYR B 1 116 ? 3.27400   15.65100  -7.35800  1.000 29.57000 ? 118 TYR B N   1 
ATOM   3180 C CA  . TYR B 1 116 ? 4.31200   16.66600  -7.24800  1.000 30.57000 ? 118 TYR B CA  1 
ATOM   3181 C C   . TYR B 1 116 ? 3.66700   17.89900  -6.64600  1.000 33.44000 ? 118 TYR B C   1 
ATOM   3182 O O   . TYR B 1 116 ? 2.60600   18.32700  -7.11000  1.000 32.74000 ? 118 TYR B O   1 
ATOM   3183 C CB  . TYR B 1 116 ? 4.94700   16.97500  -8.61300  1.000 30.45000 ? 118 TYR B CB  1 
ATOM   3184 C CG  . TYR B 1 116 ? 5.59400   15.74800  -9.21600  1.000 33.72000 ? 118 TYR B CG  1 
ATOM   3185 C CD1 . TYR B 1 116 ? 6.90300   15.39400  -8.89400  1.000 33.98000 ? 118 TYR B CD1 1 
ATOM   3186 C CD2 . TYR B 1 116 ? 4.88000   14.91600  -10.07200 1.000 35.46000 ? 118 TYR B CD2 1 
ATOM   3187 C CE1 . TYR B 1 116 ? 7.48900   14.25000  -9.42600  1.000 33.04000 ? 118 TYR B CE1 1 
ATOM   3188 C CE2 . TYR B 1 116 ? 5.45000   13.78200  -10.60800 1.000 33.82000 ? 118 TYR B CE2 1 
ATOM   3189 C CZ  . TYR B 1 116 ? 6.74200   13.44600  -10.27500 1.000 28.99000 ? 118 TYR B CZ  1 
ATOM   3190 O OH  . TYR B 1 116 ? 7.29600   12.31400  -10.80200 1.000 35.46000 ? 118 TYR B OH  1 
ATOM   3191 N N   . ASN B 1 117 ? 4.28200   18.42500  -5.58100  1.000 32.32000 ? 119 ASN B N   1 
ATOM   3192 C CA  . ASN B 1 117 ? 3.77200   19.59400  -4.86000  1.000 34.86000 ? 119 ASN B CA  1 
ATOM   3193 C C   . ASN B 1 117 ? 2.34100   19.36900  -4.36800  1.000 36.86000 ? 119 ASN B C   1 
ATOM   3194 O O   . ASN B 1 117 ? 1.50900   20.28100  -4.37800  1.000 34.75000 ? 119 ASN B O   1 
ATOM   3195 C CB  . ASN B 1 117 ? 3.86600   20.85700  -5.72700  1.000 38.63000 ? 119 ASN B CB  1 
ATOM   3196 C CG  . ASN B 1 117 ? 5.27200   21.08300  -6.27200  1.000 40.50000 ? 119 ASN B CG  1 
ATOM   3197 O OD1 . ASN B 1 117 ? 6.22600   21.23200  -5.50900  1.000 41.11000 ? 119 ASN B OD1 1 
ATOM   3198 N ND2 . ASN B 1 117 ? 5.40500   21.09500  -7.59700  1.000 42.06000 ? 119 ASN B ND2 1 
ATOM   3199 N N   . GLY B 1 118 ? 2.05500   18.13900  -3.93300  1.000 31.28000 ? 120 GLY B N   1 
ATOM   3200 C CA  . GLY B 1 118 ? 0.75000   17.78800  -3.41900  1.000 32.66000 ? 120 GLY B CA  1 
ATOM   3201 C C   . GLY B 1 118 ? -0.31400  17.57800  -4.46800  1.000 31.34000 ? 120 GLY B C   1 
ATOM   3202 O O   . GLY B 1 118 ? -1.47600  17.34900  -4.10900  1.000 30.86000 ? 120 GLY B O   1 
ATOM   3203 N N   . SER B 1 119 ? 0.05100   17.62500  -5.75000  1.000 34.07000 ? 121 SER B N   1 
ATOM   3204 C CA  . SER B 1 119 ? -0.89500  17.58600  -6.85800  1.000 36.36000 ? 121 SER B CA  1 
ATOM   3205 C C   . SER B 1 119 ? -0.76600  16.28500  -7.63600  1.000 30.91000 ? 121 SER B C   1 
ATOM   3206 O O   . SER B 1 119 ? 0.29700   16.02800  -8.22400  1.000 30.54000 ? 121 SER B O   1 
ATOM   3207 C CB  . SER B 1 119 ? -0.65800  18.78000  -7.78200  1.000 36.07000 ? 121 SER B CB  1 
ATOM   3208 O OG  . SER B 1 119 ? -1.62300  18.79800  -8.81500  1.000 45.00000 ? 121 SER B OG  1 
ATOM   3209 N N   . PRO B 1 120 ? -1.80500  15.44900  -7.66800  1.000 33.42000 ? 122 PRO B N   1 
ATOM   3210 C CA  . PRO B 1 120 ? -1.74200  14.19700  -8.43900  1.000 31.71000 ? 122 PRO B CA  1 
ATOM   3211 C C   . PRO B 1 120 ? -1.44500  14.45600  -9.90900  1.000 34.22000 ? 122 PRO B C   1 
ATOM   3212 O O   . PRO B 1 120 ? -2.10600  15.27100  -10.55800 1.000 34.28000 ? 122 PRO B O   1 
ATOM   3213 C CB  . PRO B 1 120 ? -3.14000  13.59400  -8.24400  1.000 33.24000 ? 122 PRO B CB  1 
ATOM   3214 C CG  . PRO B 1 120 ? -3.59200  14.14300  -6.92400  1.000 35.56000 ? 122 PRO B CG  1 
ATOM   3215 C CD  . PRO B 1 120 ? -3.03800  15.54800  -6.87100  1.000 32.01000 ? 122 PRO B CD  1 
ATOM   3216 N N   . SER B 1 121 ? -0.44900  13.73900  -10.43700 1.000 31.14000 ? 123 SER B N   1 
ATOM   3217 C CA  . SER B 1 121 ? 0.01800   13.93200  -11.80200 1.000 29.69000 ? 123 SER B CA  1 
ATOM   3218 C C   . SER B 1 121 ? -0.22100  12.74100  -12.72400 1.000 30.82000 ? 123 SER B C   1 
ATOM   3219 O O   . SER B 1 121 ? -0.45300  12.94200  -13.91700 1.000 30.24000 ? 123 SER B O   1 
ATOM   3220 C CB  . SER B 1 121 ? 1.51900   14.26800  -11.78900 1.000 33.17000 ? 123 SER B CB  1 
ATOM   3221 O OG  . SER B 1 121 ? 2.11000   13.99600  -13.04000 1.000 40.62000 ? 123 SER B OG  1 
ATOM   3222 N N   . GLY B 1 122 ? -0.17200  11.51300  -12.21600 1.000 28.18000 ? 124 GLY B N   1 
ATOM   3223 C CA  . GLY B 1 122 ? -0.38100  10.35000  -13.06000 1.000 29.85000 ? 124 GLY B CA  1 
ATOM   3224 C C   . GLY B 1 122 ? -0.60600  9.12800   -12.20200 1.000 28.31000 ? 124 GLY B C   1 
ATOM   3225 O O   . GLY B 1 122 ? -0.32300  9.13600   -11.00200 1.000 26.58000 ? 124 GLY B O   1 
ATOM   3226 N N   . VAL B 1 123 ? -1.13200  8.07800   -12.82900 1.000 26.58000 ? 125 VAL B N   1 
ATOM   3227 C CA  . VAL B 1 123 ? -1.38800  6.81300   -12.14700 1.000 26.31000 ? 125 VAL B CA  1 
ATOM   3228 C C   . VAL B 1 123 ? -0.88600  5.67100   -13.02500 1.000 30.49000 ? 125 VAL B C   1 
ATOM   3229 O O   . VAL B 1 123 ? -1.02300  5.71200   -14.25400 1.000 28.39000 ? 125 VAL B O   1 
ATOM   3230 C CB  . VAL B 1 123 ? -2.88500  6.65400   -11.78300 1.000 28.77000 ? 125 VAL B CB  1 
ATOM   3231 C CG1 . VAL B 1 123 ? -3.75500  6.62000   -13.02100 1.000 30.09000 ? 125 VAL B CG1 1 
ATOM   3232 C CG2 . VAL B 1 123 ? -3.10400  5.41300   -10.89200 1.000 28.03000 ? 125 VAL B CG2 1 
ATOM   3233 N N   . TYR B 1 124 ? -0.24400  4.68000   -12.40200 1.000 27.67000 ? 126 TYR B N   1 
ATOM   3234 C CA  . TYR B 1 124 ? 0.19800   3.50700   -13.14100 1.000 26.54000 ? 126 TYR B CA  1 
ATOM   3235 C C   . TYR B 1 124 ? 0.32800   2.32900   -12.18700 1.000 24.02000 ? 126 TYR B C   1 
ATOM   3236 O O   . TYR B 1 124 ? 0.40700   2.48900   -10.96900 1.000 25.90000 ? 126 TYR B O   1 
ATOM   3237 C CB  . TYR B 1 124 ? 1.52100   3.76100   -13.87400 1.000 28.75000 ? 126 TYR B CB  1 
ATOM   3238 C CG  . TYR B 1 124 ? 2.60700   4.26100   -12.96500 1.000 30.56000 ? 126 TYR B CG  1 
ATOM   3239 C CD1 . TYR B 1 124 ? 3.42000   3.37100   -12.28200 1.000 33.90000 ? 126 TYR B CD1 1 
ATOM   3240 C CD2 . TYR B 1 124 ? 2.80100   5.62500   -12.76100 1.000 31.27000 ? 126 TYR B CD2 1 
ATOM   3241 C CE1 . TYR B 1 124 ? 4.41700   3.81900   -11.44100 1.000 32.31000 ? 126 TYR B CE1 1 
ATOM   3242 C CE2 . TYR B 1 124 ? 3.80900   6.08700   -11.91600 1.000 36.63000 ? 126 TYR B CE2 1 
ATOM   3243 C CZ  . TYR B 1 124 ? 4.60500   5.17600   -11.25800 1.000 31.91000 ? 126 TYR B CZ  1 
ATOM   3244 O OH  . TYR B 1 124 ? 5.60200   5.59800   -10.41000 1.000 40.44000 ? 126 TYR B OH  1 
ATOM   3245 N N   . GLN B 1 125 ? 0.36500   1.14000   -12.76900 1.000 24.17000 ? 127 GLN B N   1 
ATOM   3246 C CA  . GLN B 1 125 ? 0.47200   -0.10400  -12.02300 1.000 28.05000 ? 127 GLN B CA  1 
ATOM   3247 C C   . GLN B 1 125 ? 1.94200   -0.49900  -11.87000 1.000 31.12000 ? 127 GLN B C   1 
ATOM   3248 O O   . GLN B 1 125 ? 2.73400   -0.35800  -12.80900 1.000 32.66000 ? 127 GLN B O   1 
ATOM   3249 C CB  . GLN B 1 125 ? -0.33600  -1.19100  -12.75300 1.000 32.73000 ? 127 GLN B CB  1 
ATOM   3250 C CG  . GLN B 1 125 ? -0.47000  -2.48500  -12.01300 1.000 34.71000 ? 127 GLN B CG  1 
ATOM   3251 C CD  . GLN B 1 125 ? -1.53600  -2.44300  -10.95600 1.000 33.05000 ? 127 GLN B CD  1 
ATOM   3252 O OE1 . GLN B 1 125 ? -2.02300  -1.36700  -10.58500 1.000 32.70000 ? 127 GLN B OE1 1 
ATOM   3253 N NE2 . GLN B 1 125 ? -1.91800  -3.61400  -10.45700 1.000 32.35000 ? 127 GLN B NE2 1 
ATOM   3254 N N   . CYS B 1 126 ? 2.30400   -0.96600  -10.66700 1.000 27.88000 ? 128 CYS B N   1 
ATOM   3255 C CA  . CYS B 1 126 ? 3.66700   -1.33600  -10.30400 1.000 32.57000 ? 128 CYS B CA  1 
ATOM   3256 C C   . CYS B 1 126 ? 3.66600   -2.70900  -9.64600  1.000 28.41000 ? 128 CYS B C   1 
ATOM   3257 O O   . CYS B 1 126 ? 2.63200   -3.20300  -9.20300  1.000 30.31000 ? 128 CYS B O   1 
ATOM   3258 C CB  . CYS B 1 126 ? 4.28100   -0.32100  -9.31700  1.000 28.91000 ? 128 CYS B CB  1 
ATOM   3259 S SG  . CYS B 1 126 ? 5.32100   0.85000   -10.11700 1.000 54.09000 ? 128 CYS B SG  1 
ATOM   3260 N N   . ALA B 1 127 ? 4.84600   -3.32200  -9.57100  1.000 32.25000 ? 129 ALA B N   1 
ATOM   3261 C CA  . ALA B 1 127 ? 5.03300   -4.52700  -8.77800  1.000 28.19000 ? 129 ALA B CA  1 
ATOM   3262 C C   . ALA B 1 127 ? 6.20300   -4.32800  -7.82900  1.000 27.30000 ? 129 ALA B C   1 
ATOM   3263 O O   . ALA B 1 127 ? 7.18700   -3.67000  -8.17500  1.000 28.22000 ? 129 ALA B O   1 
ATOM   3264 C CB  . ALA B 1 127 ? 5.28700   -5.75400  -9.65800  1.000 30.51000 ? 129 ALA B CB  1 
ATOM   3265 N N   . MET B 1 128 ? 6.09500   -4.90600  -6.63900  1.000 27.88000 ? 130 MET B N   1 
ATOM   3266 C CA  . MET B 1 128 ? 7.24200   -4.98800  -5.74100  1.000 26.78000 ? 130 MET B CA  1 
ATOM   3267 C C   . MET B 1 128 ? 8.18900   -6.05800  -6.26900  1.000 28.39000 ? 130 MET B C   1 
ATOM   3268 O O   . MET B 1 128 ? 7.81400   -7.23300  -6.35900  1.000 27.88000 ? 130 MET B O   1 
ATOM   3269 C CB  . MET B 1 128 ? 6.76800   -5.29900  -4.31900  1.000 30.32000 ? 130 MET B CB  1 
ATOM   3270 C CG  . MET B 1 128 ? 7.87200   -5.45500  -3.25000  1.000 30.29000 ? 130 MET B CG  1 
ATOM   3271 S SD  . MET B 1 128 ? 8.75200   -3.92400  -2.89600  1.000 36.26000 ? 130 MET B SD  1 
ATOM   3272 C CE  . MET B 1 128 ? 7.42100   -2.87800  -2.28300  1.000 27.35000 ? 130 MET B CE  1 
ATOM   3273 N N   . ARG B 1 129 ? 9.40000   -5.65300  -6.65300  1.000 27.98000 ? 131 ARG B N   1 
ATOM   3274 C CA  . ARG B 1 129 ? 10.35500  -6.58800  -7.22900  1.000 25.48000 ? 131 ARG B CA  1 
ATOM   3275 C C   . ARG B 1 129 ? 10.87200  -7.53700  -6.15100  1.000 27.41000 ? 131 ARG B C   1 
ATOM   3276 O O   . ARG B 1 129 ? 10.84700  -7.21600  -4.95800  1.000 25.91000 ? 131 ARG B O   1 
ATOM   3277 C CB  . ARG B 1 129 ? 11.53600  -5.84700  -7.86400  1.000 29.29000 ? 131 ARG B CB  1 
ATOM   3278 C CG  . ARG B 1 129 ? 11.17800  -4.85100  -8.97400  1.000 31.23000 ? 131 ARG B CG  1 
ATOM   3279 C CD  . ARG B 1 129 ? 10.35500  -5.49900  -10.07600 1.000 30.72000 ? 131 ARG B CD  1 
ATOM   3280 N NE  . ARG B 1 129 ? 10.97000  -6.73500  -10.56500 1.000 33.07000 ? 131 ARG B NE  1 
ATOM   3281 C CZ  . ARG B 1 129 ? 10.39600  -7.54400  -11.45400 1.000 32.54000 ? 131 ARG B CZ  1 
ATOM   3282 N NH1 . ARG B 1 129 ? 9.21300   -7.22400  -11.96100 1.000 29.10000 ? 131 ARG B NH1 1 
ATOM   3283 N NH2 . ARG B 1 129 ? 11.00700  -8.66100  -11.84200 1.000 29.17000 ? 131 ARG B NH2 1 
ATOM   3284 N N   . PRO B 1 130 ? 11.34700  -8.71800  -6.54700  1.000 27.96000 ? 132 PRO B N   1 
ATOM   3285 C CA  . PRO B 1 130 ? 11.99100  -9.60500  -5.56600  1.000 28.03000 ? 132 PRO B CA  1 
ATOM   3286 C C   . PRO B 1 130 ? 13.10500  -8.93800  -4.78800  1.000 28.10000 ? 132 PRO B C   1 
ATOM   3287 O O   . PRO B 1 130 ? 13.34900  -9.32400  -3.63800  1.000 28.18000 ? 132 PRO B O   1 
ATOM   3288 C CB  . PRO B 1 130 ? 12.51600  -10.75500 -6.43300  1.000 31.39000 ? 132 PRO B CB  1 
ATOM   3289 C CG  . PRO B 1 130 ? 11.53500  -10.83300 -7.56500  1.000 31.25000 ? 132 PRO B CG  1 
ATOM   3290 C CD  . PRO B 1 130 ? 11.09800  -9.39700  -7.83200  1.000 32.32000 ? 132 PRO B CD  1 
ATOM   3291 N N   . ASN B 1 131 ? 13.78300  -7.94300  -5.36100  1.000 27.07000 ? 133 ASN B N   1 
ATOM   3292 C CA  . ASN B 1 131 ? 14.85300  -7.25300  -4.64100  1.000 28.66000 ? 133 ASN B CA  1 
ATOM   3293 C C   . ASN B 1 131 ? 14.34600  -6.05800  -3.85000  1.000 28.90000 ? 133 ASN B C   1 
ATOM   3294 O O   . ASN B 1 131 ? 15.15600  -5.24300  -3.38600  1.000 25.81000 ? 133 ASN B O   1 
ATOM   3295 C CB  . ASN B 1 131 ? 15.97500  -6.83200  -5.59600  1.000 27.18000 ? 133 ASN B CB  1 
ATOM   3296 C CG  . ASN B 1 131 ? 15.56200  -5.76700  -6.60200  1.000 28.90000 ? 133 ASN B CG  1 
ATOM   3297 O OD1 . ASN B 1 131 ? 14.44000  -5.28600  -6.60900  1.000 28.74000 ? 133 ASN B OD1 1 
ATOM   3298 N ND2 . ASN B 1 131 ? 16.50300  -5.38500  -7.45900  1.000 32.60000 ? 133 ASN B ND2 1 
ATOM   3299 N N   . PHE B 1 132 ? 13.02300  -5.94600  -3.71600  1.000 25.84000 ? 134 PHE B N   1 
ATOM   3300 C CA  . PHE B 1 132 ? 12.29700  -4.96400  -2.91300  1.000 26.58000 ? 134 PHE B CA  1 
ATOM   3301 C C   . PHE B 1 132 ? 12.34000  -3.55700  -3.48900  1.000 28.62000 ? 134 PHE B C   1 
ATOM   3302 O O   . PHE B 1 132 ? 12.05800  -2.59400  -2.77300  1.000 30.83000 ? 134 PHE B O   1 
ATOM   3303 C CB  . PHE B 1 132 ? 12.79000  -4.94500  -1.46200  1.000 23.99000 ? 134 PHE B CB  1 
ATOM   3304 C CG  . PHE B 1 132 ? 12.30700  -6.10500  -0.65000  1.000 28.12000 ? 134 PHE B CG  1 
ATOM   3305 C CD1 . PHE B 1 132 ? 10.97000  -6.20700  -0.29800  1.000 27.91000 ? 134 PHE B CD1 1 
ATOM   3306 C CD2 . PHE B 1 132 ? 13.17800  -7.11500  -0.26600  1.000 30.57000 ? 134 PHE B CD2 1 
ATOM   3307 C CE1 . PHE B 1 132 ? 10.50100  -7.28300  0.45100   1.000 29.74000 ? 134 PHE B CE1 1 
ATOM   3308 C CE2 . PHE B 1 132 ? 12.71100  -8.19700  0.48100   1.000 28.49000 ? 134 PHE B CE2 1 
ATOM   3309 C CZ  . PHE B 1 132 ? 11.37100  -8.28000  0.82900   1.000 29.87000 ? 134 PHE B CZ  1 
ATOM   3310 N N   . THR B 1 133 ? 12.70300  -3.39200  -4.75700  1.000 26.63000 ? 135 THR B N   1 
ATOM   3311 C CA  . THR B 1 133 ? 12.60700  -2.09000  -5.39800  1.000 26.07000 ? 135 THR B CA  1 
ATOM   3312 C C   . THR B 1 133 ? 11.32900  -2.01800  -6.22400  1.000 28.22000 ? 135 THR B C   1 
ATOM   3313 O O   . THR B 1 133 ? 10.66700  -3.02300  -6.47700  1.000 26.22000 ? 135 THR B O   1 
ATOM   3314 C CB  . THR B 1 133 ? 13.80500  -1.81600  -6.30300  1.000 29.48000 ? 135 THR B CB  1 
ATOM   3315 O OG1 . THR B 1 133 ? 13.78500  -2.74000  -7.40000  1.000 29.11000 ? 135 THR B OG1 1 
ATOM   3316 C CG2 . THR B 1 133 ? 15.10300  -1.94100  -5.51800  1.000 26.95000 ? 135 THR B CG2 1 
ATOM   3317 N N   . ILE B 1 134 ? 11.02300  -0.80500  -6.67000  1.000 26.92000 ? 136 ILE B N   1 
ATOM   3318 C CA  . ILE B 1 134 ? 9.90500   -0.51200  -7.55500  1.000 31.99000 ? 136 ILE B CA  1 
ATOM   3319 C C   . ILE B 1 134 ? 10.47300  0.07300   -8.84300  1.000 31.49000 ? 136 ILE B C   1 
ATOM   3320 O O   . ILE B 1 134 ? 11.29600  0.99600   -8.80100  1.000 31.93000 ? 136 ILE B O   1 
ATOM   3321 C CB  . ILE B 1 134 ? 8.92200   0.48100   -6.90400  1.000 32.75000 ? 136 ILE B CB  1 
ATOM   3322 C CG1 . ILE B 1 134 ? 8.32000   -0.10800  -5.62900  1.000 33.80000 ? 136 ILE B CG1 1 
ATOM   3323 C CG2 . ILE B 1 134 ? 7.84500   0.82600   -7.85800  1.000 34.90000 ? 136 ILE B CG2 1 
ATOM   3324 C CD1 . ILE B 1 134 ? 7.75200   -1.45300  -5.83600  1.000 32.71000 ? 136 ILE B CD1 1 
ATOM   3325 N N   . LYS B 1 135 ? 10.06200  -0.47400  -9.98400  1.000 31.98000 ? 137 LYS B N   1 
ATOM   3326 C CA  . LYS B 1 135 ? 10.43300  0.11500   -11.26700 1.000 31.73000 ? 137 LYS B CA  1 
ATOM   3327 C C   . LYS B 1 135 ? 9.38900   1.18100   -11.56900 1.000 34.55000 ? 137 LYS B C   1 
ATOM   3328 O O   . LYS B 1 135 ? 8.45400   0.99000   -12.34200 1.000 35.75000 ? 137 LYS B O   1 
ATOM   3329 C CB  . LYS B 1 135 ? 10.51500  -0.94600  -12.36000 1.000 34.03000 ? 137 LYS B CB  1 
ATOM   3330 N N   . GLY B 1 136 ? 9.53700   2.32600   -10.90600 1.000 34.54000 ? 138 GLY B N   1 
ATOM   3331 C CA  . GLY B 1 136 ? 8.56500   3.38800   -11.00300 1.000 35.73000 ? 138 GLY B CA  1 
ATOM   3332 C C   . GLY B 1 136 ? 8.94000   4.43000   -12.04400 1.000 35.20000 ? 138 GLY B C   1 
ATOM   3333 O O   . GLY B 1 136 ? 9.97600   4.36600   -12.70600 1.000 37.46000 ? 138 GLY B O   1 
ATOM   3334 N N   . SER B 1 137 ? 8.05600   5.40800   -12.17200 1.000 33.72000 ? 139 SER B N   1 
ATOM   3335 C CA  . SER B 1 137 ? 8.27300   6.59700   -12.98700 1.000 36.83000 ? 139 SER B CA  1 
ATOM   3336 C C   . SER B 1 137 ? 8.07900   7.76600   -12.03400 1.000 37.76000 ? 139 SER B C   1 
ATOM   3337 O O   . SER B 1 137 ? 6.94600   8.19100   -11.76900 1.000 34.74000 ? 139 SER B O   1 
ATOM   3338 C CB  . SER B 1 137 ? 7.32300   6.65900   -14.18000 1.000 39.27000 ? 139 SER B CB  1 
ATOM   3339 O OG  . SER B 1 137 ? 7.80200   7.59200   -15.13300 1.000 42.07000 ? 139 SER B OG  1 
ATOM   3340 N N   . PHE B 1 138 ? 9.19800   8.24300   -11.50000 1.000 33.56000 ? 140 PHE B N   1 
ATOM   3341 C CA  . PHE B 1 138 ? 9.24100   9.20200   -10.41000 1.000 32.39000 ? 140 PHE B CA  1 
ATOM   3342 C C   . PHE B 1 138 ? 10.32000  10.21400  -10.74400 1.000 35.87000 ? 140 PHE B C   1 
ATOM   3343 O O   . PHE B 1 138 ? 11.43800  9.83000   -11.09600 1.000 35.09000 ? 140 PHE B O   1 
ATOM   3344 C CB  . PHE B 1 138 ? 9.58600   8.52300   -9.07100  1.000 35.12000 ? 140 PHE B CB  1 
ATOM   3345 C CG  . PHE B 1 138 ? 8.44600   7.77400   -8.43600  1.000 32.43000 ? 140 PHE B CG  1 
ATOM   3346 C CD1 . PHE B 1 138 ? 7.22700   8.39100   -8.20900  1.000 32.60000 ? 140 PHE B CD1 1 
ATOM   3347 C CD2 . PHE B 1 138 ? 8.61600   6.45700   -8.03600  1.000 31.27000 ? 140 PHE B CD2 1 
ATOM   3348 C CE1 . PHE B 1 138 ? 6.18800   7.70300   -7.60400  1.000 32.43000 ? 140 PHE B CE1 1 
ATOM   3349 C CE2 . PHE B 1 138 ? 7.59100   5.76200   -7.43300  1.000 32.11000 ? 140 PHE B CE2 1 
ATOM   3350 C CZ  . PHE B 1 138 ? 6.37500   6.38700   -7.20900  1.000 33.23000 ? 140 PHE B CZ  1 
ATOM   3351 N N   . LEU B 1 139 ? 9.99100   11.48700  -10.64900 1.000 34.12000 ? 141 LEU B N   1 
ATOM   3352 C CA  . LEU B 1 139 ? 10.95400  12.55800  -10.83200 1.000 35.12000 ? 141 LEU B CA  1 
ATOM   3353 C C   . LEU B 1 139 ? 11.24100  13.17900  -9.46700  1.000 37.88000 ? 141 LEU B C   1 
ATOM   3354 O O   . LEU B 1 139 ? 10.62300  12.81500  -8.46000  1.000 33.25000 ? 141 LEU B O   1 
ATOM   3355 C CB  . LEU B 1 139 ? 10.41700  13.58500  -11.83200 1.000 36.05000 ? 141 LEU B CB  1 
ATOM   3356 C CG  . LEU B 1 139 ? 10.08700  13.00100  -13.21100 1.000 37.10000 ? 141 LEU B CG  1 
ATOM   3357 C CD1 . LEU B 1 139 ? 9.24100   13.96600  -14.04700 1.000 38.16000 ? 141 LEU B CD1 1 
ATOM   3358 C CD2 . LEU B 1 139 ? 11.38500  12.64500  -13.93900 1.000 39.28000 ? 141 LEU B CD2 1 
ATOM   3359 N N   . ASN B 1 140 ? 12.17900  14.12700  -9.43300  1.000 30.55000 ? 142 ASN B N   1 
ATOM   3360 C CA  . ASN B 1 140 ? 12.45900  14.83800  -8.19400  1.000 32.56000 ? 142 ASN B CA  1 
ATOM   3361 C C   . ASN B 1 140 ? 11.17800  15.42800  -7.60400  1.000 33.43000 ? 142 ASN B C   1 
ATOM   3362 O O   . ASN B 1 140 ? 10.30000  15.90800  -8.32700  1.000 32.28000 ? 142 ASN B O   1 
ATOM   3363 C CB  . ASN B 1 140 ? 13.50000  15.93500  -8.41900  1.000 30.00000 ? 142 ASN B CB  1 
ATOM   3364 C CG  . ASN B 1 140 ? 14.89100  15.38000  -8.65600  1.000 30.00000 ? 142 ASN B CG  1 
ATOM   3365 O OD1 . ASN B 1 140 ? 15.20000  14.25700  -8.25800  1.000 30.00000 ? 142 ASN B OD1 1 
ATOM   3366 N ND2 . ASN B 1 140 ? 15.74000  16.16600  -9.30800  1.000 30.00000 ? 142 ASN B ND2 1 
ATOM   3367 N N   . GLY B 1 141 ? 11.05400  15.35500  -6.27800  1.000 33.63000 ? 143 GLY B N   1 
ATOM   3368 C CA  . GLY B 1 141 ? 9.86900   15.84700  -5.60000  1.000 32.15000 ? 143 GLY B CA  1 
ATOM   3369 C C   . GLY B 1 141 ? 8.68500   14.89700  -5.58200  1.000 31.77000 ? 143 GLY B C   1 
ATOM   3370 O O   . GLY B 1 141 ? 7.62400   15.26400  -5.06000  1.000 28.60000 ? 143 GLY B O   1 
ATOM   3371 N N   . SER B 1 142 ? 8.83000   13.69100  -6.12500  1.000 32.54000 ? 144 SER B N   1 
ATOM   3372 C CA  . SER B 1 142 ? 7.76700   12.69800  -6.09700  1.000 29.86000 ? 144 SER B CA  1 
ATOM   3373 C C   . SER B 1 142 ? 7.61400   12.02900  -4.74100  1.000 27.40000 ? 144 SER B C   1 
ATOM   3374 O O   . SER B 1 142 ? 6.60800   11.33300  -4.53000  1.000 25.70000 ? 144 SER B O   1 
ATOM   3375 C CB  . SER B 1 142 ? 8.03700   11.62400  -7.14900  1.000 30.82000 ? 144 SER B CB  1 
ATOM   3376 O OG  . SER B 1 142 ? 9.32700   11.07700  -6.94500  1.000 31.45000 ? 144 SER B OG  1 
ATOM   3377 N N   . CYS B 1 143 ? 8.59900   12.19700  -3.85000  1.000 29.17000 ? 145 CYS B N   1 
ATOM   3378 C CA  . CYS B 1 143 ? 8.56900   11.61000  -2.51200  1.000 27.13000 ? 145 CYS B CA  1 
ATOM   3379 C C   . CYS B 1 143 ? 7.25400   11.89100  -1.81600  1.000 25.07000 ? 145 CYS B C   1 
ATOM   3380 O O   . CYS B 1 143 ? 6.72400   13.00500  -1.88200  1.000 26.57000 ? 145 CYS B O   1 
ATOM   3381 C CB  . CYS B 1 143 ? 9.70400   12.17700  -1.66000  1.000 27.17000 ? 145 CYS B CB  1 
ATOM   3382 S SG  . CYS B 1 143 ? 11.28100  12.12100  -2.47000  1.000 30.97000 ? 145 CYS B SG  1 
ATOM   3383 N N   . GLY B 1 144 ? 6.74000   10.87400  -1.12100  1.000 24.42000 ? 146 GLY B N   1 
ATOM   3384 C CA  . GLY B 1 144 ? 5.43600   10.94800  -0.50300  1.000 25.94000 ? 146 GLY B CA  1 
ATOM   3385 C C   . GLY B 1 144 ? 4.29000   10.43300  -1.35400  1.000 25.49000 ? 146 GLY B C   1 
ATOM   3386 O O   . GLY B 1 144 ? 3.18000   10.25300  -0.82500  1.000 24.87000 ? 146 GLY B O   1 
ATOM   3387 N N   . SER B 1 145 ? 4.50200   10.24300  -2.66000  1.000 25.47000 ? 147 SER B N   1 
ATOM   3388 C CA  . SER B 1 145 ? 3.50900   9.56100   -3.48200  1.000 25.80000 ? 147 SER B CA  1 
ATOM   3389 C C   . SER B 1 145 ? 3.29900   8.16300   -2.91700  1.000 27.41000 ? 147 SER B C   1 
ATOM   3390 O O   . SER B 1 145 ? 4.22500   7.54900   -2.38000  1.000 24.48000 ? 147 SER B O   1 
ATOM   3391 C CB  . SER B 1 145 ? 3.96800   9.47300   -4.94500  1.000 27.81000 ? 147 SER B CB  1 
ATOM   3392 O OG  . SER B 1 145 ? 4.12100   10.75300  -5.56200  1.000 27.24000 ? 147 SER B OG  1 
ATOM   3393 N N   . VAL B 1 146 ? 2.07500   7.65400   -3.03600  1.000 22.53000 ? 148 VAL B N   1 
ATOM   3394 C CA  . VAL B 1 146 ? 1.73700   6.40200   -2.37600  1.000 26.43000 ? 148 VAL B CA  1 
ATOM   3395 C C   . VAL B 1 146 ? 1.29900   5.35700   -3.39400  1.000 26.25000 ? 148 VAL B C   1 
ATOM   3396 O O   . VAL B 1 146 ? 0.81800   5.67000   -4.49200  1.000 24.68000 ? 148 VAL B O   1 
ATOM   3397 C CB  . VAL B 1 146 ? 0.64700   6.57400   -1.29800  1.000 31.11000 ? 148 VAL B CB  1 
ATOM   3398 C CG1 . VAL B 1 146 ? 1.16800   7.41200   -0.11400  1.000 30.87000 ? 148 VAL B CG1 1 
ATOM   3399 C CG2 . VAL B 1 146 ? -0.62100  7.15600   -1.89700  1.000 27.87000 ? 148 VAL B CG2 1 
ATOM   3400 N N   . GLY B 1 147 ? 1.48200   4.09300   -3.00000  1.000 25.29000 ? 149 GLY B N   1 
ATOM   3401 C CA  . GLY B 1 147 ? 0.97700   2.95100   -3.73800  1.000 25.81000 ? 149 GLY B CA  1 
ATOM   3402 C C   . GLY B 1 147 ? -0.16100  2.29800   -2.97300  1.000 24.85000 ? 149 GLY B C   1 
ATOM   3403 O O   . GLY B 1 147 ? -0.19000  2.31300   -1.73700  1.000 23.00000 ? 149 GLY B O   1 
ATOM   3404 N N   . PHE B 1 148 ? -1.09700  1.70200   -3.70500  1.000 23.48000 ? 150 PHE B N   1 
ATOM   3405 C CA  . PHE B 1 148 ? -2.31200  1.24400   -3.04600  1.000 23.62000 ? 150 PHE B CA  1 
ATOM   3406 C C   . PHE B 1 148 ? -3.03100  0.20900   -3.89500  1.000 23.91000 ? 150 PHE B C   1 
ATOM   3407 O O   . PHE B 1 148 ? -2.84200  0.11700   -5.11300  1.000 23.05000 ? 150 PHE B O   1 
ATOM   3408 C CB  . PHE B 1 148 ? -3.27500  2.41200   -2.75600  1.000 24.20000 ? 150 PHE B CB  1 
ATOM   3409 C CG  . PHE B 1 148 ? -3.75200  3.11000   -3.99000  1.000 25.44000 ? 150 PHE B CG  1 
ATOM   3410 C CD1 . PHE B 1 148 ? -2.94800  4.04500   -4.62000  1.000 24.61000 ? 150 PHE B CD1 1 
ATOM   3411 C CD2 . PHE B 1 148 ? -5.00200  2.81700   -4.53800  1.000 26.68000 ? 150 PHE B CD2 1 
ATOM   3412 C CE1 . PHE B 1 148 ? -3.37600  4.68100   -5.78100  1.000 26.05000 ? 150 PHE B CE1 1 
ATOM   3413 C CE2 . PHE B 1 148 ? -5.43100  3.45200   -5.69900  1.000 24.78000 ? 150 PHE B CE2 1 
ATOM   3414 C CZ  . PHE B 1 148 ? -4.62400  4.37500   -6.31700  1.000 27.03000 ? 150 PHE B CZ  1 
ATOM   3415 N N   . ASN B 1 149 ? -3.90300  -0.53600  -3.21600  1.000 23.28000 ? 151 ASN B N   1 
ATOM   3416 C CA  . ASN B 1 149 ? -4.87000  -1.42500  -3.83500  1.000 27.37000 ? 151 ASN B CA  1 
ATOM   3417 C C   . ASN B 1 149 ? -6.23700  -1.02000  -3.30700  1.000 26.39000 ? 151 ASN B C   1 
ATOM   3418 O O   . ASN B 1 149 ? -6.34800  -0.45900  -2.20900  1.000 25.69000 ? 151 ASN B O   1 
ATOM   3419 C CB  . ASN B 1 149 ? -4.58400  -2.89800  -3.49300  1.000 26.51000 ? 151 ASN B CB  1 
ATOM   3420 C CG  . ASN B 1 149 ? -3.40300  -3.46300  -4.26700  1.000 29.40000 ? 151 ASN B CG  1 
ATOM   3421 O OD1 . ASN B 1 149 ? -3.53700  -3.87800  -5.42100  1.000 32.65000 ? 151 ASN B OD1 1 
ATOM   3422 N ND2 . ASN B 1 149 ? -2.24400  -3.48800  -3.63100  1.000 28.44000 ? 151 ASN B ND2 1 
ATOM   3423 N N   . ILE B 1 150 ? -7.28400  -1.30500  -4.07000  1.000 29.15000 ? 152 ILE B N   1 
ATOM   3424 C CA  . ILE B 1 150 ? -8.64200  -1.05200  -3.61100  1.000 30.25000 ? 152 ILE B CA  1 
ATOM   3425 C C   . ILE B 1 150 ? -9.41200  -2.36900  -3.61900  1.000 37.94000 ? 152 ILE B C   1 
ATOM   3426 O O   . ILE B 1 150 ? -9.34200  -3.13500  -4.58900  1.000 34.00000 ? 152 ILE B O   1 
ATOM   3427 C CB  . ILE B 1 150 ? -9.34800  0.01600   -4.46600  1.000 33.54000 ? 152 ILE B CB  1 
ATOM   3428 C CG1 . ILE B 1 150 ? -8.54200  1.31900   -4.47500  1.000 32.74000 ? 152 ILE B CG1 1 
ATOM   3429 C CG2 . ILE B 1 150 ? -10.76700 0.25700   -3.95300  1.000 37.57000 ? 152 ILE B CG2 1 
ATOM   3430 C CD1 . ILE B 1 150 ? -9.23000  2.45200   -5.20200  1.000 34.67000 ? 152 ILE B CD1 1 
ATOM   3431 N N   . ASP B 1 151 ? -10.12600 -2.63700  -2.52900  1.000 40.06000 ? 153 ASP B N   1 
ATOM   3432 C CA  . ASP B 1 151 ? -10.97500 -3.82100  -2.39100  1.000 41.93000 ? 153 ASP B CA  1 
ATOM   3433 C C   . ASP B 1 151 ? -12.36700 -3.31900  -2.02500  1.000 47.27000 ? 153 ASP B C   1 
ATOM   3434 O O   . ASP B 1 151 ? -12.60900 -2.98000  -0.86500  1.000 48.01000 ? 153 ASP B O   1 
ATOM   3435 C CB  . ASP B 1 151 ? -10.40300 -4.76300  -1.32600  1.000 49.05000 ? 153 ASP B CB  1 
ATOM   3436 C CG  . ASP B 1 151 ? -11.41500 -5.79600  -0.80200  1.000 55.10000 ? 153 ASP B CG  1 
ATOM   3437 O OD1 . ASP B 1 151 ? -12.50200 -5.98000  -1.40100  1.000 58.91000 ? 153 ASP B OD1 1 
ATOM   3438 O OD2 . ASP B 1 151 ? -11.12200 -6.43200  0.24200   1.000 59.29000 ? 153 ASP B OD2 1 
ATOM   3439 N N   . TYR B 1 152 ? -13.26500 -3.28200  -3.01500  1.000 48.78000 ? 154 TYR B N   1 
ATOM   3440 C CA  . TYR B 1 152 ? -14.65000 -2.85300  -2.85700  1.000 47.85000 ? 154 TYR B CA  1 
ATOM   3441 C C   . TYR B 1 152 ? -14.78800 -1.77800  -1.78400  1.000 50.48000 ? 154 TYR B C   1 
ATOM   3442 O O   . TYR B 1 152 ? -15.19300 -2.07800  -0.65800  1.000 53.50000 ? 154 TYR B O   1 
ATOM   3443 C CB  . TYR B 1 152 ? -15.54200 -4.05100  -2.52600  1.000 49.94000 ? 154 TYR B CB  1 
ATOM   3444 N N   . ASP B 1 153 ? -14.37900 -0.55200  -2.10800  1.000 48.07000 ? 155 ASP B N   1 
ATOM   3445 C CA  . ASP B 1 153 ? -14.52000 0.69800   -1.36700  1.000 46.81000 ? 155 ASP B CA  1 
ATOM   3446 C C   . ASP B 1 153 ? -13.44600 0.89300   -0.26300  1.000 44.08000 ? 155 ASP B C   1 
ATOM   3447 O O   . ASP B 1 153 ? -13.34900 2.00000   0.28200   1.000 41.59000 ? 155 ASP B O   1 
ATOM   3448 C CB  . ASP B 1 153 ? -15.94800 0.90100   -0.79500  1.000 49.55000 ? 155 ASP B CB  1 
ATOM   3449 C CG  . ASP B 1 153 ? -16.17100 0.31400   0.61700   1.000 52.73000 ? 155 ASP B CG  1 
ATOM   3450 O OD1 . ASP B 1 153 ? -15.80600 -0.83500  0.93900   1.000 50.58000 ? 155 ASP B OD1 1 
ATOM   3451 O OD2 . ASP B 1 153 ? -16.77500 1.02700   1.43700   1.000 55.59000 ? 155 ASP B OD2 1 
ATOM   3452 N N   . CYS B 1 154 ? -12.59200 -0.09300  0.03100   1.000 39.55000 ? 156 CYS B N   1 
ATOM   3453 C CA  . CYS B 1 154 ? -11.54000 0.07400   1.03600   1.000 34.05000 ? 156 CYS B CA  1 
ATOM   3454 C C   . CYS B 1 154 ? -10.18600 0.18900   0.34500   1.000 35.02000 ? 156 CYS B C   1 
ATOM   3455 O O   . CYS B 1 154 ? -9.77600  -0.72500  -0.37900  1.000 34.29000 ? 156 CYS B O   1 
ATOM   3456 C CB  . CYS B 1 154 ? -11.52100 -1.08200  2.03600   1.000 35.08000 ? 156 CYS B CB  1 
ATOM   3457 S SG  . CYS B 1 154 ? -10.20800 -0.98400  3.30300   1.000 39.48000 ? 156 CYS B SG  1 
ATOM   3458 N N   . VAL B 1 155 ? -9.48900  1.29600   0.58900   1.000 29.48000 ? 157 VAL B N   1 
ATOM   3459 C CA  . VAL B 1 155 ? -8.16100  1.53500   0.02700   1.000 26.48000 ? 157 VAL B CA  1 
ATOM   3460 C C   . VAL B 1 155 ? -7.11700  0.94300   0.96800   1.000 26.57000 ? 157 VAL B C   1 
ATOM   3461 O O   . VAL B 1 155 ? -7.03300  1.33100   2.13600   1.000 27.03000 ? 157 VAL B O   1 
ATOM   3462 C CB  . VAL B 1 155 ? -7.91200  3.03600   -0.17800  1.000 29.75000 ? 157 VAL B CB  1 
ATOM   3463 C CG1 . VAL B 1 155 ? -6.52400  3.27300   -0.76700  1.000 26.90000 ? 157 VAL B CG1 1 
ATOM   3464 C CG2 . VAL B 1 155 ? -9.00400  3.64200   -1.05000  1.000 31.99000 ? 157 VAL B CG2 1 
ATOM   3465 N N   . SER B 1 156 ? -6.31500  0.00800   0.47000   1.000 26.79000 ? 158 SER B N   1 
ATOM   3466 C CA  . SER B 1 156 ? -5.22600  -0.57300  1.24700   1.000 27.38000 ? 158 SER B CA  1 
ATOM   3467 C C   . SER B 1 156 ? -3.93700  0.08600   0.78000   1.000 23.57000 ? 158 SER B C   1 
ATOM   3468 O O   . SER B 1 156 ? -3.45500  -0.20400  -0.31200  1.000 24.39000 ? 158 SER B O   1 
ATOM   3469 C CB  . SER B 1 156 ? -5.16500  -2.09000  1.07600   1.000 28.34000 ? 158 SER B CB  1 
ATOM   3470 O OG  . SER B 1 156 ? -6.20200  -2.70800  1.83300   1.000 32.97000 ? 158 SER B OG  1 
ATOM   3471 N N   . PHE B 1 157 ? -3.40100  0.99000   1.60100   1.000 24.30000 ? 159 PHE B N   1 
ATOM   3472 C CA  . PHE B 1 157 ? -2.15600  1.68300   1.29700   1.000 24.68000 ? 159 PHE B CA  1 
ATOM   3473 C C   . PHE B 1 157 ? -0.97900  0.77200   1.63300   1.000 24.53000 ? 159 PHE B C   1 
ATOM   3474 O O   . PHE B 1 157 ? -0.90400  0.24100   2.74800   1.000 24.51000 ? 159 PHE B O   1 
ATOM   3475 C CB  . PHE B 1 157 ? -2.05600  2.97600   2.11300   1.000 23.60000 ? 159 PHE B CB  1 
ATOM   3476 C CG  . PHE B 1 157 ? -3.04200  4.03100   1.71500   1.000 24.29000 ? 159 PHE B CG  1 
ATOM   3477 C CD1 . PHE B 1 157 ? -2.86000  4.75000   0.54000   1.000 26.76000 ? 159 PHE B CD1 1 
ATOM   3478 C CD2 . PHE B 1 157 ? -4.11700  4.33600   2.53400   1.000 25.71000 ? 159 PHE B CD2 1 
ATOM   3479 C CE1 . PHE B 1 157 ? -3.76600  5.73600   0.17500   1.000 26.31000 ? 159 PHE B CE1 1 
ATOM   3480 C CE2 . PHE B 1 157 ? -5.02000  5.33100   2.18300   1.000 28.46000 ? 159 PHE B CE2 1 
ATOM   3481 C CZ  . PHE B 1 157 ? -4.83900  6.02500   1.00100   1.000 26.17000 ? 159 PHE B CZ  1 
ATOM   3482 N N   . CYS B 1 158 ? -0.06700  0.58200   0.67600   1.000 22.04000 ? 160 CYS B N   1 
ATOM   3483 C CA  . CYS B 1 158 ? 1.05800   -0.32400  0.87800   1.000 23.85000 ? 160 CYS B CA  1 
ATOM   3484 C C   . CYS B 1 158 ? 2.42400   0.29800   0.65400   1.000 25.93000 ? 160 CYS B C   1 
ATOM   3485 O O   . CYS B 1 158 ? 3.42900   -0.33600  0.99400   1.000 25.48000 ? 160 CYS B O   1 
ATOM   3486 C CB  . CYS B 1 158 ? 0.94300   -1.54900  -0.04500  1.000 23.04000 ? 160 CYS B CB  1 
ATOM   3487 S SG  . CYS B 1 158 ? 0.80600   -1.15800  -1.79800  1.000 25.53000 ? 160 CYS B SG  1 
ATOM   3488 N N   . TYR B 1 159 ? 2.51000   1.47800   0.05000   1.000 21.32000 ? 161 TYR B N   1 
ATOM   3489 C CA  . TYR B 1 159 ? 3.82100   1.99700   -0.31900  1.000 20.65000 ? 161 TYR B CA  1 
ATOM   3490 C C   . TYR B 1 159 ? 3.80200   3.50800   -0.18300  1.000 22.89000 ? 161 TYR B C   1 
ATOM   3491 O O   . TYR B 1 159 ? 2.83000   4.15600   -0.56700  1.000 22.37000 ? 161 TYR B O   1 
ATOM   3492 C CB  . TYR B 1 159 ? 4.18600   1.60500   -1.76100  1.000 22.97000 ? 161 TYR B CB  1 
ATOM   3493 C CG  . TYR B 1 159 ? 5.53000   2.13200   -2.26700  1.000 24.50000 ? 161 TYR B CG  1 
ATOM   3494 C CD1 . TYR B 1 159 ? 6.72100   1.49800   -1.93400  1.000 25.21000 ? 161 TYR B CD1 1 
ATOM   3495 C CD2 . TYR B 1 159 ? 5.59300   3.25000   -3.10300  1.000 22.75000 ? 161 TYR B CD2 1 
ATOM   3496 C CE1 . TYR B 1 159 ? 7.94400   1.97000   -2.40100  1.000 23.84000 ? 161 TYR B CE1 1 
ATOM   3497 C CE2 . TYR B 1 159 ? 6.80900   3.71900   -3.58700  1.000 23.95000 ? 161 TYR B CE2 1 
ATOM   3498 C CZ  . TYR B 1 159 ? 7.98000   3.08200   -3.22700  1.000 25.79000 ? 161 TYR B CZ  1 
ATOM   3499 O OH  . TYR B 1 159 ? 9.20200   3.53500   -3.68300  1.000 27.42000 ? 161 TYR B OH  1 
ATOM   3500 N N   . MET B 1 160 ? 4.88100   4.06300   0.35400   1.000 24.28000 ? 162 MET B N   1 
ATOM   3501 C CA  . MET B 1 160 ? 5.12100   5.49300   0.26900   1.000 25.36000 ? 162 MET B CA  1 
ATOM   3502 C C   . MET B 1 160 ? 6.50700   5.67800   -0.32200  1.000 23.03000 ? 162 MET B C   1 
ATOM   3503 O O   . MET B 1 160 ? 7.46800   5.05300   0.13500   1.000 20.59000 ? 162 MET B O   1 
ATOM   3504 C CB  . MET B 1 160 ? 5.02300   6.18400   1.63300   1.000 23.58000 ? 162 MET B CB  1 
ATOM   3505 C CG  . MET B 1 160 ? 5.46800   7.63000   1.52700   1.000 27.28000 ? 162 MET B CG  1 
ATOM   3506 S SD  . MET B 1 160 ? 5.22900   8.56000   3.02400   1.000 34.22000 ? 162 MET B SD  1 
ATOM   3507 C CE  . MET B 1 160 ? 3.50100   9.03000   2.86900   1.000 36.98000 ? 162 MET B CE  1 
ATOM   3508 N N   . HIS B 1 161 ? 6.60500   6.49700   -1.36100  1.000 24.65000 ? 163 HIS B N   1 
ATOM   3509 C CA  . HIS B 1 161 ? 7.85300   6.61400   -2.09100  1.000 24.87000 ? 163 HIS B CA  1 
ATOM   3510 C C   . HIS B 1 161 ? 8.86600   7.47000   -1.32300  1.000 24.01000 ? 163 HIS B C   1 
ATOM   3511 O O   . HIS B 1 161 ? 8.51900   8.56000   -0.85800  1.000 23.87000 ? 163 HIS B O   1 
ATOM   3512 C CB  . HIS B 1 161 ? 7.58400   7.23300   -3.45400  1.000 25.07000 ? 163 HIS B CB  1 
ATOM   3513 C CG  . HIS B 1 161 ? 8.83300   7.45500   -4.23200  1.000 26.08000 ? 163 HIS B CG  1 
ATOM   3514 N ND1 . HIS B 1 161 ? 9.73700   6.44300   -4.46700  1.000 25.80000 ? 163 HIS B ND1 1 
ATOM   3515 C CD2 . HIS B 1 161 ? 9.36300   8.57400   -4.77500  1.000 27.47000 ? 163 HIS B CD2 1 
ATOM   3516 C CE1 . HIS B 1 161 ? 10.76000  6.92500   -5.14800  1.000 28.41000 ? 163 HIS B CE1 1 
ATOM   3517 N NE2 . HIS B 1 161 ? 10.55000  8.21100   -5.36100  1.000 27.18000 ? 163 HIS B NE2 1 
ATOM   3518 N N   . HIS B 1 162 ? 10.12700  7.00500   -1.22000  1.000 25.08000 ? 164 HIS B N   1 
ATOM   3519 C CA  . HIS B 1 162 ? 11.15200  7.77100   -0.50600  1.000 24.20000 ? 164 HIS B CA  1 
ATOM   3520 C C   . HIS B 1 162 ? 12.30000  8.23300   -1.38700  1.000 29.18000 ? 164 HIS B C   1 
ATOM   3521 O O   . HIS B 1 162 ? 12.69800  9.40000   -1.30400  1.000 28.45000 ? 164 HIS B O   1 
ATOM   3522 C CB  . HIS B 1 162 ? 11.72400  6.98000   0.69000   1.000 22.79000 ? 164 HIS B CB  1 
ATOM   3523 C CG  . HIS B 1 162 ? 10.82200  6.96100   1.88500   1.000 25.98000 ? 164 HIS B CG  1 
ATOM   3524 N ND1 . HIS B 1 162 ? 11.16100  7.53400   3.09300   1.000 27.26000 ? 164 HIS B ND1 1 
ATOM   3525 C CD2 . HIS B 1 162 ? 9.58600   6.44000   2.05000   1.000 23.66000 ? 164 HIS B CD2 1 
ATOM   3526 C CE1 . HIS B 1 162 ? 10.17200  7.36400   3.95100   1.000 26.30000 ? 164 HIS B CE1 1 
ATOM   3527 N NE2 . HIS B 1 162 ? 9.20200   6.70300   3.34200   1.000 27.55000 ? 164 HIS B NE2 1 
ATOM   3528 N N   . MET B 1 163 ? 12.88200  7.36500   -2.20800  1.000 27.56000 ? 165 MET B N   1 
ATOM   3529 C CA  . MET B 1 163 ? 14.10900  7.78600   -2.86600  1.000 31.52000 ? 165 MET B CA  1 
ATOM   3530 C C   . MET B 1 163 ? 14.35400  6.99100   -4.13500  1.000 29.89000 ? 165 MET B C   1 
ATOM   3531 O O   . MET B 1 163 ? 13.75400  5.94100   -4.36700  1.000 23.49000 ? 165 MET B O   1 
ATOM   3532 C CB  . MET B 1 163 ? 15.29900  7.62700   -1.93300  1.000 31.50000 ? 165 MET B CB  1 
ATOM   3533 C CG  . MET B 1 163 ? 15.40700  6.23200   -1.36200  1.000 31.06000 ? 165 MET B CG  1 
ATOM   3534 S SD  . MET B 1 163 ? 16.38700  6.26300   0.14800   1.000 39.18000 ? 165 MET B SD  1 
ATOM   3535 C CE  . MET B 1 163 ? 17.76800  7.31600   -0.34800  1.000 32.97000 ? 165 MET B CE  1 
ATOM   3536 N N   . GLU B 1 164 ? 15.31100  7.48500   -4.92200  1.000 30.12000 ? 166 GLU B N   1 
ATOM   3537 C CA  . GLU B 1 164 ? 15.72900  6.86000   -6.16400  1.000 32.68000 ? 166 GLU B CA  1 
ATOM   3538 C C   . GLU B 1 164 ? 17.08000  6.19000   -5.97400  1.000 32.99000 ? 166 GLU B C   1 
ATOM   3539 O O   . GLU B 1 164 ? 17.98200  6.75400   -5.34500  1.000 29.18000 ? 166 GLU B O   1 
ATOM   3540 C CB  . GLU B 1 164 ? 15.81400  7.88600   -7.29800  1.000 33.06000 ? 166 GLU B CB  1 
ATOM   3541 C CG  . GLU B 1 164 ? 16.12600  7.26200   -8.63600  1.000 36.79000 ? 166 GLU B CG  1 
ATOM   3542 C CD  . GLU B 1 164 ? 15.80800  8.18200   -9.80400  1.000 41.80000 ? 166 GLU B CD  1 
ATOM   3543 O OE1 . GLU B 1 164 ? 16.64300  9.05500   -10.12400 1.000 43.44000 ? 166 GLU B OE1 1 
ATOM   3544 O OE2 . GLU B 1 164 ? 14.71100  8.03400   -10.39500 1.000 42.75000 ? 166 GLU B OE2 1 
ATOM   3545 N N   . LEU B 1 165 ? 17.21100  4.99200   -6.50800  1.000 33.75000 ? 167 LEU B N   1 
ATOM   3546 C CA  . LEU B 1 165 ? 18.46400  4.25200   -6.47600  1.000 32.26000 ? 167 LEU B CA  1 
ATOM   3547 C C   . LEU B 1 165 ? 19.23000  4.46800   -7.77900  1.000 34.69000 ? 167 LEU B C   1 
ATOM   3548 O O   . LEU B 1 165 ? 18.63200  4.76700   -8.81700  1.000 32.55000 ? 167 LEU B O   1 
ATOM   3549 C CB  . LEU B 1 165 ? 18.18900  2.75900   -6.25100  1.000 30.12000 ? 167 LEU B CB  1 
ATOM   3550 C CG  . LEU B 1 165 ? 17.55600  2.48300   -4.87900  1.000 32.16000 ? 167 LEU B CG  1 
ATOM   3551 C CD1 . LEU B 1 165 ? 17.13800  1.02200   -4.72600  1.000 31.15000 ? 167 LEU B CD1 1 
ATOM   3552 C CD2 . LEU B 1 165 ? 18.48800  2.92300   -3.74900  1.000 31.76000 ? 167 LEU B CD2 1 
ATOM   3553 N N   . PRO B 1 166 ? 20.56000  4.32500   -7.76700  1.000 33.75000 ? 168 PRO B N   1 
ATOM   3554 C CA  . PRO B 1 166 ? 21.36100  4.79400   -8.91900  1.000 33.97000 ? 168 PRO B CA  1 
ATOM   3555 C C   . PRO B 1 166 ? 21.03100  4.11400   -10.23200 1.000 38.49000 ? 168 PRO B C   1 
ATOM   3556 O O   . PRO B 1 166 ? 21.30800  4.68800   -11.29600 1.000 37.85000 ? 168 PRO B O   1 
ATOM   3557 C CB  . PRO B 1 166 ? 22.80900  4.50200   -8.48800  1.000 39.41000 ? 168 PRO B CB  1 
ATOM   3558 C CG  . PRO B 1 166 ? 22.69900  3.50900   -7.37100  1.000 38.76000 ? 168 PRO B CG  1 
ATOM   3559 C CD  . PRO B 1 166 ? 21.41400  3.84500   -6.66900  1.000 35.04000 ? 168 PRO B CD  1 
ATOM   3560 N N   . THR B 1 167 ? 20.44100  2.92300   -10.20400 1.000 35.17000 ? 169 THR B N   1 
ATOM   3561 C CA  . THR B 1 167 ? 20.02100  2.27300   -11.43100 1.000 35.60000 ? 169 THR B CA  1 
ATOM   3562 C C   . THR B 1 167 ? 18.67700  2.78600   -11.94800 1.000 38.50000 ? 169 THR B C   1 
ATOM   3563 O O   . THR B 1 167 ? 18.15700  2.24000   -12.92700 1.000 38.14000 ? 169 THR B O   1 
ATOM   3564 C CB  . THR B 1 167 ? 19.99000  0.75900   -11.20000 1.000 40.39000 ? 169 THR B CB  1 
ATOM   3565 O OG1 . THR B 1 167 ? 19.69200  0.08500   -12.42300 1.000 51.84000 ? 169 THR B OG1 1 
ATOM   3566 C CG2 . THR B 1 167 ? 18.97600  0.39500   -10.14300 1.000 26.85000 ? 169 THR B CG2 1 
ATOM   3567 N N   . GLY B 1 168 ? 18.10300  3.81700   -11.32300 1.000 34.52000 ? 170 GLY B N   1 
ATOM   3568 C CA  . GLY B 1 168 ? 16.85200  4.39000   -11.77200 1.000 36.01000 ? 170 GLY B CA  1 
ATOM   3569 C C   . GLY B 1 168 ? 15.59400  3.75100   -11.21100 1.000 32.09000 ? 170 GLY B C   1 
ATOM   3570 O O   . GLY B 1 168 ? 14.48800  4.16700   -11.58700 1.000 37.17000 ? 170 GLY B O   1 
ATOM   3571 N N   . VAL B 1 169 ? 15.71800  2.74500   -10.34800 1.000 30.95000 ? 171 VAL B N   1 
ATOM   3572 C CA  . VAL B 1 169 ? 14.56600  2.14300   -9.67800  1.000 30.35000 ? 171 VAL B CA  1 
ATOM   3573 C C   . VAL B 1 169 ? 14.38800  2.84700   -8.33800  1.000 30.35000 ? 171 VAL B C   1 
ATOM   3574 O O   . VAL B 1 169 ? 15.19100  3.71800   -7.97400  1.000 29.81000 ? 171 VAL B O   1 
ATOM   3575 C CB  . VAL B 1 169 ? 14.73900  0.62200   -9.50300  1.000 31.99000 ? 171 VAL B CB  1 
ATOM   3576 C CG1 . VAL B 1 169 ? 15.04500  -0.02700  -10.85000 1.000 33.27000 ? 171 VAL B CG1 1 
ATOM   3577 C CG2 . VAL B 1 169 ? 15.85400  0.33500   -8.50100  1.000 28.35000 ? 171 VAL B CG2 1 
ATOM   3578 N N   . HIS B 1 170 ? 13.34800  2.47900   -7.59100  1.000 29.04000 ? 172 HIS B N   1 
ATOM   3579 C CA  . HIS B 1 170 ? 12.89100  3.30600   -6.48200  1.000 28.68000 ? 172 HIS B CA  1 
ATOM   3580 C C   . HIS B 1 170 ? 12.69800  2.49100   -5.21100  1.000 26.55000 ? 172 HIS B C   1 
ATOM   3581 O O   . HIS B 1 170 ? 12.42200  1.29100   -5.25100  1.000 26.65000 ? 172 HIS B O   1 
ATOM   3582 C CB  . HIS B 1 170 ? 11.59500  4.02600   -6.87800  1.000 27.80000 ? 172 HIS B CB  1 
ATOM   3583 C CG  . HIS B 1 170 ? 11.75100  4.83300   -8.12700  1.000 33.76000 ? 172 HIS B CG  1 
ATOM   3584 N ND1 . HIS B 1 170 ? 11.25100  4.42700   -9.34500  1.000 30.82000 ? 172 HIS B ND1 1 
ATOM   3585 C CD2 . HIS B 1 170 ? 12.43300  5.97900   -8.36200  1.000 32.09000 ? 172 HIS B CD2 1 
ATOM   3586 C CE1 . HIS B 1 170 ? 11.58000  5.31300   -10.26900 1.000 33.18000 ? 172 HIS B CE1 1 
ATOM   3587 N NE2 . HIS B 1 170 ? 12.29200  6.26800   -9.69900  1.000 32.55000 ? 172 HIS B NE2 1 
ATOM   3588 N N   . ALA B 1 171 ? 12.83800  3.16800   -4.07500  1.000 23.27000 ? 173 ALA B N   1 
ATOM   3589 C CA  . ALA B 1 171 ? 12.81500  2.52000   -2.77300  1.000 23.72000 ? 173 ALA B CA  1 
ATOM   3590 C C   . ALA B 1 171 ? 11.90100  3.31400   -1.86000  1.000 22.38000 ? 173 ALA B C   1 
ATOM   3591 O O   . ALA B 1 171 ? 11.85700  4.54800   -1.94000  1.000 23.79000 ? 173 ALA B O   1 
ATOM   3592 C CB  . ALA B 1 171 ? 14.23800  2.42400   -2.15800  1.000 23.78000 ? 173 ALA B CB  1 
ATOM   3593 N N   . GLY B 1 172 ? 11.17800  2.61100   -0.99800  1.000 22.99000 ? 174 GLY B N   1 
ATOM   3594 C CA  . GLY B 1 172 ? 10.17100  3.25600   -0.18400  1.000 23.57000 ? 174 GLY B CA  1 
ATOM   3595 C C   . GLY B 1 172 ? 9.80700   2.39200   1.00200   1.000 23.05000 ? 174 GLY B C   1 
ATOM   3596 O O   . GLY B 1 172 ? 10.40800  1.34300   1.23400   1.000 23.04000 ? 174 GLY B O   1 
ATOM   3597 N N   . THR B 1 173 ? 8.80700   2.85000   1.75500   1.000 23.60000 ? 175 THR B N   1 
ATOM   3598 C CA  . THR B 1 173 ? 8.39900   2.21500   3.00000   1.000 22.74000 ? 175 THR B CA  1 
ATOM   3599 C C   . THR B 1 173 ? 6.94300   1.80200   2.90400   1.000 21.00000 ? 175 THR B C   1 
ATOM   3600 O O   . THR B 1 173 ? 6.21400   2.23200   2.01100   1.000 20.61000 ? 175 THR B O   1 
ATOM   3601 C CB  . THR B 1 173 ? 8.54200   3.16200   4.19400   1.000 25.65000 ? 175 THR B CB  1 
ATOM   3602 O OG1 . THR B 1 173 ? 7.65500   4.27400   4.00900   1.000 23.76000 ? 175 THR B OG1 1 
ATOM   3603 C CG2 . THR B 1 173 ? 9.96400   3.65500   4.32700   1.000 25.77000 ? 175 THR B CG2 1 
ATOM   3604 N N   . ASP B 1 174 ? 6.51300   0.98500   3.86100   1.000 21.56000 ? 176 ASP B N   1 
ATOM   3605 C CA  . ASP B 1 174 ? 5.08300   0.88600   4.09100   1.000 24.11000 ? 176 ASP B CA  1 
ATOM   3606 C C   . ASP B 1 174 ? 4.62300   2.14800   4.82800   1.000 23.99000 ? 176 ASP B C   1 
ATOM   3607 O O   . ASP B 1 174 ? 5.41100   3.05100   5.11800   1.000 23.95000 ? 176 ASP B O   1 
ATOM   3608 C CB  . ASP B 1 174 ? 4.74800   -0.42400  4.82100   1.000 23.78000 ? 176 ASP B CB  1 
ATOM   3609 C CG  . ASP B 1 174 ? 5.36200   -0.53100  6.23000   1.000 24.35000 ? 176 ASP B CG  1 
ATOM   3610 O OD1 . ASP B 1 174 ? 5.59500   0.49100   6.91600   1.000 24.33000 ? 176 ASP B OD1 1 
ATOM   3611 O OD2 . ASP B 1 174 ? 5.57900   -1.67800  6.67700   1.000 25.99000 ? 176 ASP B OD2 1 
ATOM   3612 N N   . LEU B 1 175 ? 3.33700   2.22800   5.14700   1.000 23.67000 ? 177 LEU B N   1 
ATOM   3613 C CA  . LEU B 1 175 ? 2.82900   3.45700   5.74500   1.000 20.84000 ? 177 LEU B CA  1 
ATOM   3614 C C   . LEU B 1 175 ? 3.07000   3.53200   7.24500   1.000 24.50000 ? 177 LEU B C   1 
ATOM   3615 O O   . LEU B 1 175 ? 2.68400   4.53000   7.86900   1.000 25.52000 ? 177 LEU B O   1 
ATOM   3616 C CB  . LEU B 1 175 ? 1.32800   3.59800   5.44500   1.000 24.56000 ? 177 LEU B CB  1 
ATOM   3617 C CG  . LEU B 1 175 ? 0.99200   4.39500   4.18400   1.000 27.63000 ? 177 LEU B CG  1 
ATOM   3618 C CD1 . LEU B 1 175 ? 1.26000   5.88100   4.40600   1.000 28.12000 ? 177 LEU B CD1 1 
ATOM   3619 C CD2 . LEU B 1 175 ? 1.76900   3.88700   2.96500   1.000 24.68000 ? 177 LEU B CD2 1 
ATOM   3620 N N   . GLU B 1 176 ? 3.66300   2.49800   7.83500   1.000 24.22000 ? 178 GLU B N   1 
ATOM   3621 C CA  . GLU B 1 176 ? 4.19100   2.55500   9.19200   1.000 25.54000 ? 178 GLU B CA  1 
ATOM   3622 C C   . GLU B 1 176 ? 5.67400   2.91200   9.21300   1.000 25.15000 ? 178 GLU B C   1 
ATOM   3623 O O   . GLU B 1 176 ? 6.30200   2.84000   10.27000  1.000 25.80000 ? 178 GLU B O   1 
ATOM   3624 C CB  . GLU B 1 176 ? 3.95200   1.21900   9.90700   1.000 24.89000 ? 178 GLU B CB  1 
ATOM   3625 C CG  . GLU B 1 176 ? 2.46100   0.96300   10.24100  1.000 32.45000 ? 178 GLU B CG  1 
ATOM   3626 C CD  . GLU B 1 176 ? 2.17100   -0.48100  10.65900  1.000 37.40000 ? 178 GLU B CD  1 
ATOM   3627 O OE1 . GLU B 1 176 ? 1.00100   -0.77800  10.96000  1.000 44.06000 ? 178 GLU B OE1 1 
ATOM   3628 O OE2 . GLU B 1 176 ? 3.10200   -1.31600  10.68300  1.000 46.63000 ? 178 GLU B OE2 1 
ATOM   3629 N N   . GLY B 1 177 ? 6.23700   3.26800   8.06200   1.000 23.49000 ? 179 GLY B N   1 
ATOM   3630 C CA  . GLY B 1 177 ? 7.58400   3.76900   7.93100   1.000 26.74000 ? 179 GLY B CA  1 
ATOM   3631 C C   . GLY B 1 177 ? 8.66300   2.71400   7.86100   1.000 23.37000 ? 179 GLY B C   1 
ATOM   3632 O O   . GLY B 1 177 ? 9.82400   3.05600   8.01900   1.000 25.71000 ? 179 GLY B O   1 
ATOM   3633 N N   . ASN B 1 178 ? 8.31600   1.43900   7.65200   1.000 24.74000 ? 180 ASN B N   1 
ATOM   3634 C CA  . ASN B 1 178 ? 9.30500   0.36500   7.54200   1.000 23.93000 ? 180 ASN B CA  1 
ATOM   3635 C C   . ASN B 1 178 ? 9.74500   0.22600   6.09000   1.000 23.82000 ? 180 ASN B C   1 
ATOM   3636 O O   . ASN B 1 178 ? 8.91200   0.00900   5.20100   1.000 22.97000 ? 180 ASN B O   1 
ATOM   3637 C CB  . ASN B 1 178 ? 8.70900   -0.95600  8.03200   1.000 24.25000 ? 180 ASN B CB  1 
ATOM   3638 C CG  . ASN B 1 178 ? 8.17300   -0.86600  9.43800   1.000 25.52000 ? 180 ASN B CG  1 
ATOM   3639 O OD1 . ASN B 1 178 ? 8.94500   -0.83500  10.38700  1.000 29.72000 ? 180 ASN B OD1 1 
ATOM   3640 N ND2 . ASN B 1 178 ? 6.84000   -0.84700  9.58400   1.000 25.74000 ? 180 ASN B ND2 1 
ATOM   3641 N N   . PHE B 1 179 ? 11.04800  0.33500   5.84200   1.000 24.35000 ? 181 PHE B N   1 
ATOM   3642 C CA  . PHE B 1 179 ? 11.52200  0.23800   4.46900   1.000 22.76000 ? 181 PHE B CA  1 
ATOM   3643 C C   . PHE B 1 179 ? 11.20200  -1.13200  3.89900   1.000 23.10000 ? 181 PHE B C   1 
ATOM   3644 O O   . PHE B 1 179 ? 11.17000  -2.13300  4.61900   1.000 21.86000 ? 181 PHE B O   1 
ATOM   3645 C CB  . PHE B 1 179 ? 13.03700  0.50100   4.38400   1.000 22.65000 ? 181 PHE B CB  1 
ATOM   3646 C CG  . PHE B 1 179 ? 13.35500  1.84800   3.82500   1.000 24.58000 ? 181 PHE B CG  1 
ATOM   3647 C CD1 . PHE B 1 179 ? 13.30900  2.06800   2.45700   1.000 23.43000 ? 181 PHE B CD1 1 
ATOM   3648 C CD2 . PHE B 1 179 ? 13.59800  2.92100   4.67700   1.000 25.11000 ? 181 PHE B CD2 1 
ATOM   3649 C CE1 . PHE B 1 179 ? 13.54900  3.33200   1.93300   1.000 27.15000 ? 181 PHE B CE1 1 
ATOM   3650 C CE2 . PHE B 1 179 ? 13.82100  4.18800   4.16800   1.000 24.34000 ? 181 PHE B CE2 1 
ATOM   3651 C CZ  . PHE B 1 179 ? 13.81100  4.39700   2.79900   1.000 25.68000 ? 181 PHE B CZ  1 
ATOM   3652 N N   . TYR B 1 180 ? 10.90100  -1.15300  2.60000   1.000 23.22000 ? 182 TYR B N   1 
ATOM   3653 C CA  . TYR B 1 180 ? 10.99700  -2.36200  1.79700   1.000 22.81000 ? 182 TYR B CA  1 
ATOM   3654 C C   . TYR B 1 180 ? 12.42800  -2.45400  1.29200   1.000 22.27000 ? 182 TYR B C   1 
ATOM   3655 O O   . TYR B 1 180 ? 12.90700  -1.53500  0.62000   1.000 24.43000 ? 182 TYR B O   1 
ATOM   3656 C CB  . TYR B 1 180 ? 10.04900  -2.32900  0.60300   1.000 22.82000 ? 182 TYR B CB  1 
ATOM   3657 C CG  . TYR B 1 180 ? 8.58300   -2.38900  0.94900   1.000 23.05000 ? 182 TYR B CG  1 
ATOM   3658 C CD1 . TYR B 1 180 ? 7.97900   -3.59800  1.26600   1.000 22.55000 ? 182 TYR B CD1 1 
ATOM   3659 C CD2 . TYR B 1 180 ? 7.80100   -1.23900  0.93600   1.000 22.16000 ? 182 TYR B CD2 1 
ATOM   3660 C CE1 . TYR B 1 180 ? 6.61600   -3.66300  1.56900   1.000 25.04000 ? 182 TYR B CE1 1 
ATOM   3661 C CE2 . TYR B 1 180 ? 6.42600   -1.29800  1.23600   1.000 21.85000 ? 182 TYR B CE2 1 
ATOM   3662 C CZ  . TYR B 1 180 ? 5.85500   -2.50700  1.55200   1.000 24.32000 ? 182 TYR B CZ  1 
ATOM   3663 O OH  . TYR B 1 180 ? 4.50000   -2.56500  1.84100   1.000 23.51000 ? 182 TYR B OH  1 
ATOM   3664 N N   . GLY B 1 181 ? 13.09300  -3.56300  1.58000   1.000 23.09000 ? 183 GLY B N   1 
ATOM   3665 C CA  . GLY B 1 181 ? 14.45800  -3.75700  1.12700   1.000 24.46000 ? 183 GLY B CA  1 
ATOM   3666 C C   . GLY B 1 181 ? 15.50200  -3.14800  2.04300   1.000 26.67000 ? 183 GLY B C   1 
ATOM   3667 O O   . GLY B 1 181 ? 15.19900  -2.35700  2.95200   1.000 26.61000 ? 183 GLY B O   1 
ATOM   3668 N N   . PRO B 1 182 ? 16.77600  -3.48400  1.77900   1.000 23.92000 ? 184 PRO B N   1 
ATOM   3669 C CA  . PRO B 1 182 ? 17.89900  -3.09200  2.65400   1.000 26.20000 ? 184 PRO B CA  1 
ATOM   3670 C C   . PRO B 1 182 ? 18.38800  -1.67200  2.37800   1.000 30.93000 ? 184 PRO B C   1 
ATOM   3671 O O   . PRO B 1 182 ? 19.56100  -1.43500  2.06700   1.000 28.33000 ? 184 PRO B O   1 
ATOM   3672 C CB  . PRO B 1 182 ? 18.95800  -4.15300  2.31700   1.000 25.96000 ? 184 PRO B CB  1 
ATOM   3673 C CG  . PRO B 1 182 ? 18.71000  -4.49400  0.87900   1.000 26.95000 ? 184 PRO B CG  1 
ATOM   3674 C CD  . PRO B 1 182 ? 17.19800  -4.39100  0.69400   1.000 24.50000 ? 184 PRO B CD  1 
ATOM   3675 N N   . PHE B 1 183 ? 17.48500  -0.70400  2.50000   1.000 24.68000 ? 185 PHE B N   1 
ATOM   3676 C CA  . PHE B 1 183 ? 17.76900  0.66800   2.11200   1.000 25.72000 ? 185 PHE B CA  1 
ATOM   3677 C C   . PHE B 1 183 ? 17.56400  1.60500   3.29500   1.000 27.48000 ? 185 PHE B C   1 
ATOM   3678 O O   . PHE B 1 183 ? 16.80800  1.30600   4.22100   1.000 29.89000 ? 185 PHE B O   1 
ATOM   3679 C CB  . PHE B 1 183 ? 16.89300  1.07700   0.91600   1.000 24.05000 ? 185 PHE B CB  1 
ATOM   3680 C CG  . PHE B 1 183 ? 16.94100  0.09900   -0.21300  1.000 24.19000 ? 185 PHE B CG  1 
ATOM   3681 C CD1 . PHE B 1 183 ? 18.14200  -0.15800  -0.86900  1.000 29.59000 ? 185 PHE B CD1 1 
ATOM   3682 C CD2 . PHE B 1 183 ? 15.80900  -0.58400  -0.61100  1.000 25.18000 ? 185 PHE B CD2 1 
ATOM   3683 C CE1 . PHE B 1 183 ? 18.20200  -1.07400  -1.91400  1.000 31.72000 ? 185 PHE B CE1 1 
ATOM   3684 C CE2 . PHE B 1 183 ? 15.85900  -1.50200  -1.65700  1.000 27.53000 ? 185 PHE B CE2 1 
ATOM   3685 C CZ  . PHE B 1 183 ? 17.06300  -1.74700  -2.31000  1.000 28.69000 ? 185 PHE B CZ  1 
ATOM   3686 N N   . VAL B 1 184 ? 18.25700  2.74800   3.26000   1.000 25.94000 ? 186 VAL B N   1 
ATOM   3687 C CA  . VAL B 1 184 ? 18.20400  3.73100   4.33600   1.000 27.90000 ? 186 VAL B CA  1 
ATOM   3688 C C   . VAL B 1 184 ? 17.91800  5.10200   3.73600   1.000 27.51000 ? 186 VAL B C   1 
ATOM   3689 O O   . VAL B 1 184 ? 18.25200  5.36400   2.57800   1.000 31.53000 ? 186 VAL B O   1 
ATOM   3690 C CB  . VAL B 1 184 ? 19.50900  3.74100   5.17000   1.000 27.51000 ? 186 VAL B CB  1 
ATOM   3691 C CG1 . VAL B 1 184 ? 19.66000  2.42400   5.90900   1.000 29.87000 ? 186 VAL B CG1 1 
ATOM   3692 C CG2 . VAL B 1 184 ? 20.74500  4.01600   4.29100   1.000 28.71000 ? 186 VAL B CG2 1 
ATOM   3693 N N   . ASP B 1 185 ? 17.30000  5.98900   4.53200   1.000 26.35000 ? 187 ASP B N   1 
ATOM   3694 C CA  . ASP B 1 185 ? 16.90000  7.30800   4.01300   1.000 28.76000 ? 187 ASP B CA  1 
ATOM   3695 C C   . ASP B 1 185 ? 17.99500  8.33900   4.28700   1.000 31.62000 ? 187 ASP B C   1 
ATOM   3696 O O   . ASP B 1 185 ? 17.84400  9.29900   5.04700   1.000 30.69000 ? 187 ASP B O   1 
ATOM   3697 C CB  . ASP B 1 185 ? 15.55200  7.75200   4.57400   1.000 28.14000 ? 187 ASP B CB  1 
ATOM   3698 C CG  . ASP B 1 185 ? 15.42500  7.58500   6.08300   1.000 29.19000 ? 187 ASP B CG  1 
ATOM   3699 O OD1 . ASP B 1 185 ? 16.32600  6.99800   6.72600   1.000 30.36000 ? 187 ASP B OD1 1 
ATOM   3700 O OD2 . ASP B 1 185 ? 14.36700  8.02000   6.62300   1.000 28.02000 ? 187 ASP B OD2 1 
ATOM   3701 N N   . ARG B 1 186 ? 19.11400  8.13000   3.61200   1.000 30.45000 ? 188 ARG B N   1 
ATOM   3702 C CA  . ARG B 1 186 ? 20.23400  9.05000   3.68400   1.000 33.53000 ? 188 ARG B CA  1 
ATOM   3703 C C   . ARG B 1 186 ? 20.97400  8.99100   2.35500   1.000 35.11000 ? 188 ARG B C   1 
ATOM   3704 O O   . ARG B 1 186 ? 20.74700  8.08900   1.54000   1.000 33.09000 ? 188 ARG B O   1 
ATOM   3705 C CB  . ARG B 1 186 ? 21.14900  8.71300   4.87500   1.000 34.12000 ? 188 ARG B CB  1 
ATOM   3706 C CG  . ARG B 1 186 ? 22.17300  7.61600   4.59800   1.000 35.59000 ? 188 ARG B CG  1 
ATOM   3707 C CD  . ARG B 1 186 ? 23.02000  7.32500   5.84000   1.000 42.07000 ? 188 ARG B CD  1 
ATOM   3708 N NE  . ARG B 1 186 ? 22.11800  6.88900   6.88000   1.000 43.01000 ? 188 ARG B NE  1 
ATOM   3709 C CZ  . ARG B 1 186 ? 22.17800  5.72100   7.50900   1.000 41.71000 ? 188 ARG B CZ  1 
ATOM   3710 N NH1 . ARG B 1 186 ? 23.15700  4.84800   7.26100   1.000 33.65000 ? 188 ARG B NH1 1 
ATOM   3711 N NH2 . ARG B 1 186 ? 21.24500  5.44300   8.40800   1.000 40.89000 ? 188 ARG B NH2 1 
ATOM   3712 N N   . GLN B 1 187 ? 21.84800  9.97300   2.12600   1.000 34.69000 ? 189 GLN B N   1 
ATOM   3713 C CA  . GLN B 1 187 ? 22.67000  9.97400   0.92000   1.000 35.12000 ? 189 GLN B CA  1 
ATOM   3714 C C   . GLN B 1 187 ? 23.82100  8.99100   1.09300   1.000 39.51000 ? 189 GLN B C   1 
ATOM   3715 O O   . GLN B 1 187 ? 24.70000  9.18300   1.94500   1.000 40.88000 ? 189 GLN B O   1 
ATOM   3716 C CB  . GLN B 1 187 ? 23.19500  11.37000  0.59100   1.000 36.96000 ? 189 GLN B CB  1 
ATOM   3717 C CG  . GLN B 1 187 ? 23.89600  11.40700  -0.76900  1.000 44.29000 ? 189 GLN B CG  1 
ATOM   3718 C CD  . GLN B 1 187 ? 24.63600  12.70400  -1.03400  1.000 48.92000 ? 189 GLN B CD  1 
ATOM   3719 O OE1 . GLN B 1 187 ? 24.18100  13.78800  -0.66100  1.000 51.12000 ? 189 GLN B OE1 1 
ATOM   3720 N NE2 . GLN B 1 187 ? 25.79200  12.59700  -1.67900  1.000 51.91000 ? 189 GLN B NE2 1 
ATOM   3721 N N   . THR B 1 188 ? 23.82100  7.95000   0.26600   1.000 36.85000 ? 190 THR B N   1 
ATOM   3722 C CA  . THR B 1 188 ? 24.71800  6.81800   0.42600   1.000 40.30000 ? 190 THR B CA  1 
ATOM   3723 C C   . THR B 1 188 ? 24.92200  6.18000   -0.94300  1.000 40.66000 ? 190 THR B C   1 
ATOM   3724 O O   . THR B 1 188 ? 24.21500  6.49100   -1.90500  1.000 44.19000 ? 190 THR B O   1 
ATOM   3725 C CB  . THR B 1 188 ? 24.14300  5.81300   1.43400   1.000 43.12000 ? 190 THR B CB  1 
ATOM   3726 O OG1 . THR B 1 188 ? 25.16400  4.90600   1.86600   1.000 52.01000 ? 190 THR B OG1 1 
ATOM   3727 C CG2 . THR B 1 188 ? 23.03600  5.02800   0.78700   1.000 39.81000 ? 190 THR B CG2 1 
ATOM   3728 N N   . ALA B 1 189 ? 25.90100  5.28200   -1.02800  1.000 39.41000 ? 191 ALA B N   1 
ATOM   3729 C CA  . ALA B 1 189 ? 26.14900  4.55600   -2.27400  1.000 41.97000 ? 191 ALA B CA  1 
ATOM   3730 C C   . ALA B 1 189 ? 25.33500  3.26600   -2.37200  1.000 45.19000 ? 191 ALA B C   1 
ATOM   3731 O O   . ALA B 1 189 ? 25.79900  2.27500   -2.94600  1.000 46.65000 ? 191 ALA B O   1 
ATOM   3732 C CB  . ALA B 1 189 ? 27.64000  4.26800   -2.41500  1.000 40.60000 ? 191 ALA B CB  1 
ATOM   3733 N N   . GLN B 1 190 ? 24.11600  3.23800   -1.84500  1.000 36.68000 ? 192 GLN B N   1 
ATOM   3734 C CA  . GLN B 1 190 ? 23.36000  1.99600   -1.84500  1.000 35.67000 ? 192 GLN B CA  1 
ATOM   3735 C C   . GLN B 1 190 ? 22.82200  1.69500   -3.23700  1.000 32.27000 ? 192 GLN B C   1 
ATOM   3736 O O   . GLN B 1 190 ? 22.63800  2.58800   -4.06500  1.000 34.90000 ? 192 GLN B O   1 
ATOM   3737 C CB  . GLN B 1 190 ? 22.20600  2.05500   -0.84800  1.000 36.84000 ? 192 GLN B CB  1 
ATOM   3738 C CG  . GLN B 1 190 ? 21.10600  3.01300   -1.21500  1.000 34.95000 ? 192 GLN B CG  1 
ATOM   3739 C CD  . GLN B 1 190 ? 20.23200  3.34800   -0.01200  1.000 35.37000 ? 192 GLN B CD  1 
ATOM   3740 O OE1 . GLN B 1 190 ? 20.32800  2.69900   1.02700   1.000 29.15000 ? 192 GLN B OE1 1 
ATOM   3741 N NE2 . GLN B 1 190 ? 19.37100  4.35800   -0.15500  1.000 38.68000 ? 192 GLN B NE2 1 
ATOM   3742 N N   . ALA B 1 191 ? 22.57100  0.41000   -3.48700  1.000 29.52000 ? 193 ALA B N   1 
ATOM   3743 C CA  . ALA B 1 191 ? 22.21000  -0.05100  -4.81900  1.000 36.03000 ? 193 ALA B CA  1 
ATOM   3744 C C   . ALA B 1 191 ? 21.25300  -1.22900  -4.70100  1.000 34.86000 ? 193 ALA B C   1 
ATOM   3745 O O   . ALA B 1 191 ? 21.30500  -1.99200  -3.73600  1.000 37.46000 ? 193 ALA B O   1 
ATOM   3746 C CB  . ALA B 1 191 ? 23.45300  -0.45200  -5.63400  1.000 38.13000 ? 193 ALA B CB  1 
ATOM   3747 N N   . ALA B 1 192 ? 20.37800  -1.35900  -5.69500  1.000 36.54000 ? 194 ALA B N   1 
ATOM   3748 C CA  . ALA B 1 192 ? 19.49900  -2.51800  -5.77500  1.000 37.44000 ? 194 ALA B CA  1 
ATOM   3749 C C   . ALA B 1 192 ? 20.32600  -3.79100  -5.90200  1.000 38.08000 ? 194 ALA B C   1 
ATOM   3750 O O   . ALA B 1 192 ? 21.34900  -3.82000  -6.59200  1.000 37.18000 ? 194 ALA B O   1 
ATOM   3751 C CB  . ALA B 1 192 ? 18.54900  -2.38200  -6.97000  1.000 36.56000 ? 194 ALA B CB  1 
ATOM   3752 N N   . GLY B 1 193 ? 19.89600  -4.84100  -5.20600  1.000 39.70000 ? 195 GLY B N   1 
ATOM   3753 C CA  . GLY B 1 193 ? 20.48800  -6.14800  -5.40200  1.000 37.94000 ? 195 GLY B CA  1 
ATOM   3754 C C   . GLY B 1 193 ? 20.11800  -6.71900  -6.75700  1.000 39.73000 ? 195 GLY B C   1 
ATOM   3755 O O   . GLY B 1 193 ? 19.23800  -6.22200  -7.46400  1.000 34.71000 ? 195 GLY B O   1 
ATOM   3756 N N   . THR B 1 194 ? 20.81400  -7.78300  -7.14200  1.000 31.95000 ? 196 THR B N   1 
ATOM   3757 C CA  . THR B 1 194 ? 20.47700  -8.43200  -8.39800  1.000 39.05000 ? 196 THR B CA  1 
ATOM   3758 C C   . THR B 1 194 ? 19.02900  -8.91400  -8.33800  1.000 35.21000 ? 196 THR B C   1 
ATOM   3759 O O   . THR B 1 194 ? 18.61600  -9.57500  -7.38000  1.000 37.45000 ? 196 THR B O   1 
ATOM   3760 C CB  . THR B 1 194 ? 21.44600  -9.58500  -8.68700  1.000 45.52000 ? 196 THR B CB  1 
ATOM   3761 O OG1 . THR B 1 194 ? 20.94500  -10.37400 -9.77500  1.000 47.99000 ? 196 THR B OG1 1 
ATOM   3762 C CG2 . THR B 1 194 ? 21.63900  -10.46000 -7.46300  1.000 44.55000 ? 196 THR B CG2 1 
ATOM   3763 N N   . ASP B 1 195 ? 18.24400  -8.51200  -9.32600  1.000 35.42000 ? 197 ASP B N   1 
ATOM   3764 C CA  . ASP B 1 195 ? 16.82500  -8.81700  -9.34900  1.000 35.46000 ? 197 ASP B CA  1 
ATOM   3765 C C   . ASP B 1 195 ? 16.57900  -10.14200 -10.05800 1.000 36.85000 ? 197 ASP B C   1 
ATOM   3766 O O   . ASP B 1 195 ? 17.43100  -10.66200 -10.78500 1.000 33.58000 ? 197 ASP B O   1 
ATOM   3767 C CB  . ASP B 1 195 ? 16.04200  -7.69900  -10.03700 1.000 32.03000 ? 197 ASP B CB  1 
ATOM   3768 C CG  . ASP B 1 195 ? 14.57100  -7.69400  -9.65200  1.000 33.86000 ? 197 ASP B CG  1 
ATOM   3769 O OD1 . ASP B 1 195 ? 14.21000  -8.25800  -8.58200  1.000 31.40000 ? 197 ASP B OD1 1 
ATOM   3770 O OD2 . ASP B 1 195 ? 13.78000  -7.13500  -10.43600 1.000 28.43000 ? 197 ASP B OD2 1 
ATOM   3771 N N   . THR B 1 196 ? 15.38800  -10.68300 -9.83800  1.000 31.62000 ? 198 THR B N   1 
ATOM   3772 C CA  . THR B 1 196 ? 14.96000  -11.93600 -10.42800 1.000 30.92000 ? 198 THR B CA  1 
ATOM   3773 C C   . THR B 1 196 ? 13.56000  -11.73500 -10.98600 1.000 30.75000 ? 198 THR B C   1 
ATOM   3774 O O   . THR B 1 196 ? 12.90100  -10.73500 -10.69800 1.000 30.59000 ? 198 THR B O   1 
ATOM   3775 C CB  . THR B 1 196 ? 14.98000  -13.07200 -9.39800  1.000 34.77000 ? 198 THR B CB  1 
ATOM   3776 O OG1 . THR B 1 196 ? 14.38900  -12.60700 -8.18400  1.000 35.84000 ? 198 THR B OG1 1 
ATOM   3777 C CG2 . THR B 1 196 ? 16.41100  -13.51500 -9.10200  1.000 36.59000 ? 198 THR B CG2 1 
ATOM   3778 N N   . THR B 1 197 ? 13.12000  -12.68200 -11.80700 1.000 30.48000 ? 199 THR B N   1 
ATOM   3779 C CA  . THR B 1 197 ? 11.80100  -12.61200 -12.43600 1.000 29.28000 ? 199 THR B CA  1 
ATOM   3780 C C   . THR B 1 197 ? 10.78300  -13.35600 -11.58000 1.000 28.78000 ? 199 THR B C   1 
ATOM   3781 O O   . THR B 1 197 ? 11.08600  -14.40800 -11.01300 1.000 27.62000 ? 199 THR B O   1 
ATOM   3782 C CB  . THR B 1 197 ? 11.86400  -13.18900 -13.86100 1.000 29.43000 ? 199 THR B CB  1 
ATOM   3783 O OG1 . THR B 1 197 ? 12.73300  -12.37700 -14.64700 1.000 29.73000 ? 199 THR B OG1 1 
ATOM   3784 C CG2 . THR B 1 197 ? 10.49400  -13.17800 -14.53000 1.000 29.58000 ? 199 THR B CG2 1 
ATOM   3785 N N   . ILE B 1 198 ? 9.57600   -12.79300 -11.48000 1.000 28.40000 ? 200 ILE B N   1 
ATOM   3786 C CA  . ILE B 1 198 ? 8.52300   -13.30800 -10.60600 1.000 27.03000 ? 200 ILE B CA  1 
ATOM   3787 C C   . ILE B 1 198 ? 7.81000   -14.42400 -11.36300 1.000 27.82000 ? 200 ILE B C   1 
ATOM   3788 O O   . ILE B 1 198 ? 6.92400   -14.16200 -12.17700 1.000 25.03000 ? 200 ILE B O   1 
ATOM   3789 C CB  . ILE B 1 198 ? 7.55000   -12.20700 -10.18300 1.000 26.79000 ? 200 ILE B CB  1 
ATOM   3790 C CG1 . ILE B 1 198 ? 8.31300   -11.01900 -9.58400  1.000 28.88000 ? 200 ILE B CG1 1 
ATOM   3791 C CG2 . ILE B 1 198 ? 6.48700   -12.75100 -9.22600  1.000 26.05000 ? 200 ILE B CG2 1 
ATOM   3792 C CD1 . ILE B 1 198 ? 7.57900   -9.69400  -9.76600  1.000 27.32000 ? 200 ILE B CD1 1 
ATOM   3793 N N   . THR B 1 199 ? 8.15400   -15.67400 -11.04300 1.000 29.40000 ? 201 THR B N   1 
ATOM   3794 C CA  . THR B 1 199 ? 7.72100   -16.82100 -11.83900 1.000 29.60000 ? 201 THR B CA  1 
ATOM   3795 C C   . THR B 1 199 ? 6.20200   -16.99200 -11.84700 1.000 29.31000 ? 201 THR B C   1 
ATOM   3796 O O   . THR B 1 199 ? 5.60300   -17.22300 -12.90500 1.000 30.78000 ? 201 THR B O   1 
ATOM   3797 C CB  . THR B 1 199 ? 8.40300   -18.08500 -11.31300 1.000 29.42000 ? 201 THR B CB  1 
ATOM   3798 O OG1 . THR B 1 199 ? 9.81800   -17.86900 -11.26600 1.000 28.35000 ? 201 THR B OG1 1 
ATOM   3799 C CG2 . THR B 1 199 ? 8.10500   -19.28200 -12.21500 1.000 34.02000 ? 201 THR B CG2 1 
ATOM   3800 N N   . VAL B 1 200 ? 5.56100   -16.94300 -10.67200 1.000 27.55000 ? 202 VAL B N   1 
ATOM   3801 C CA  . VAL B 1 200 ? 4.11500   -17.15700 -10.61000 1.000 29.05000 ? 202 VAL B CA  1 
ATOM   3802 C C   . VAL B 1 200 ? 3.37400   -16.12500 -11.45600 1.000 28.58000 ? 202 VAL B C   1 
ATOM   3803 O O   . VAL B 1 200 ? 2.33500   -16.43200 -12.05600 1.000 26.71000 ? 202 VAL B O   1 
ATOM   3804 C CB  . VAL B 1 200 ? 3.62500   -17.16000 -9.14000  1.000 29.21000 ? 202 VAL B CB  1 
ATOM   3805 C CG1 . VAL B 1 200 ? 3.92000   -15.82200 -8.45100  1.000 27.22000 ? 202 VAL B CG1 1 
ATOM   3806 C CG2 . VAL B 1 200 ? 2.12000   -17.50100 -9.06300  1.000 31.54000 ? 202 VAL B CG2 1 
ATOM   3807 N N   . ASN B 1 201 ? 3.90300   -14.89800 -11.53700 1.000 24.68000 ? 203 ASN B N   1 
ATOM   3808 C CA  . ASN B 1 201 ? 3.26800   -13.85500 -12.33800 1.000 26.16000 ? 203 ASN B CA  1 
ATOM   3809 C C   . ASN B 1 201 ? 3.42800   -14.12100 -13.83600 1.000 24.88000 ? 203 ASN B C   1 
ATOM   3810 O O   . ASN B 1 201 ? 2.49800   -13.87600 -14.61300 1.000 25.29000 ? 203 ASN B O   1 
ATOM   3811 C CB  . ASN B 1 201 ? 3.85900   -12.48600 -11.97500 1.000 25.49000 ? 203 ASN B CB  1 
ATOM   3812 C CG  . ASN B 1 201 ? 3.38000   -11.96900 -10.61600 1.000 28.17000 ? 203 ASN B CG  1 
ATOM   3813 O OD1 . ASN B 1 201 ? 2.65500   -12.65400 -9.88400  1.000 25.25000 ? 203 ASN B OD1 1 
ATOM   3814 N ND2 . ASN B 1 201 ? 3.79500   -10.74900 -10.27200 1.000 25.10000 ? 203 ASN B ND2 1 
ATOM   3815 N N   . VAL B 1 202 ? 4.60700   -14.59300 -14.26500 1.000 25.66000 ? 204 VAL B N   1 
ATOM   3816 C CA  . VAL B 1 202 ? 4.79300   -14.95500 -15.67400 1.000 26.31000 ? 204 VAL B CA  1 
ATOM   3817 C C   . VAL B 1 202 ? 3.82100   -16.06100 -16.05900 1.000 28.33000 ? 204 VAL B C   1 
ATOM   3818 O O   . VAL B 1 202 ? 3.22200   -16.03400 -17.13900 1.000 26.86000 ? 204 VAL B O   1 
ATOM   3819 C CB  . VAL B 1 202 ? 6.25200   -15.36800 -15.96200 1.000 25.43000 ? 204 VAL B CB  1 
ATOM   3820 C CG1 . VAL B 1 202 ? 6.38500   -15.91300 -17.38900 1.000 28.88000 ? 204 VAL B CG1 1 
ATOM   3821 C CG2 . VAL B 1 202 ? 7.20500   -14.20800 -15.78700 1.000 27.11000 ? 204 VAL B CG2 1 
ATOM   3822 N N   . LEU B 1 203 ? 3.62800   -17.03900 -15.17000 1.000 28.34000 ? 205 LEU B N   1 
ATOM   3823 C CA  . LEU B 1 203 ? 2.64100   -18.08400 -15.43500 1.000 29.58000 ? 205 LEU B CA  1 
ATOM   3824 C C   . LEU B 1 203 ? 1.23300   -17.50900 -15.50700 1.000 29.77000 ? 205 LEU B C   1 
ATOM   3825 O O   . LEU B 1 203 ? 0.46200   -17.86100 -16.40500 1.000 28.39000 ? 205 LEU B O   1 
ATOM   3826 C CB  . LEU B 1 203 ? 2.73800   -19.17400 -14.36900 1.000 27.15000 ? 205 LEU B CB  1 
ATOM   3827 C CG  . LEU B 1 203 ? 4.05300   -19.95800 -14.45100 1.000 31.86000 ? 205 LEU B CG  1 
ATOM   3828 C CD1 . LEU B 1 203 ? 4.32000   -20.72300 -13.15500 1.000 32.57000 ? 205 LEU B CD1 1 
ATOM   3829 C CD2 . LEU B 1 203 ? 4.04700   -20.91100 -15.66000 1.000 34.68000 ? 205 LEU B CD2 1 
ATOM   3830 N N   . ALA B 1 204 ? 0.88500   -16.60900 -14.58100 1.000 25.59000 ? 206 ALA B N   1 
ATOM   3831 C CA  . ALA B 1 204 ? -0.41900  -15.95200 -14.64000 1.000 27.25000 ? 206 ALA B CA  1 
ATOM   3832 C C   . ALA B 1 204 ? -0.62300  -15.26100 -15.98100 1.000 29.84000 ? 206 ALA B C   1 
ATOM   3833 O O   . ALA B 1 204 ? -1.71500  -15.30900 -16.56000 1.000 27.80000 ? 206 ALA B O   1 
ATOM   3834 C CB  . ALA B 1 204 ? -0.54900  -14.94200 -13.49600 1.000 26.03000 ? 206 ALA B CB  1 
ATOM   3835 N N   . TRP B 1 205 ? 0.42300   -14.61400 -16.48800 1.000 27.51000 ? 207 TRP B N   1 
ATOM   3836 C CA  . TRP B 1 205 ? 0.32500   -13.88300 -17.74400 1.000 27.99000 ? 207 TRP B CA  1 
ATOM   3837 C C   . TRP B 1 205 ? 0.21600   -14.83500 -18.93500 1.000 30.62000 ? 207 TRP B C   1 
ATOM   3838 O O   . TRP B 1 205 ? -0.48200  -14.54000 -19.91400 1.000 28.29000 ? 207 TRP B O   1 
ATOM   3839 C CB  . TRP B 1 205 ? 1.54200   -12.97400 -17.86100 1.000 28.99000 ? 207 TRP B CB  1 
ATOM   3840 C CG  . TRP B 1 205 ? 1.67600   -12.18800 -19.11000 1.000 30.44000 ? 207 TRP B CG  1 
ATOM   3841 C CD1 . TRP B 1 205 ? 1.00300   -11.05100 -19.44900 1.000 33.54000 ? 207 TRP B CD1 1 
ATOM   3842 C CD2 . TRP B 1 205 ? 2.58800   -12.44700 -20.17100 1.000 31.30000 ? 207 TRP B CD2 1 
ATOM   3843 N NE1 . TRP B 1 205 ? 1.44000   -10.59300 -20.67000 1.000 30.01000 ? 207 TRP B NE1 1 
ATOM   3844 C CE2 . TRP B 1 205 ? 2.40000   -11.44200 -21.13900 1.000 30.91000 ? 207 TRP B CE2 1 
ATOM   3845 C CE3 . TRP B 1 205 ? 3.54200   -13.44200 -20.40500 1.000 33.04000 ? 207 TRP B CE3 1 
ATOM   3846 C CZ2 . TRP B 1 205 ? 3.13500   -11.39600 -22.31100 1.000 36.60000 ? 207 TRP B CZ2 1 
ATOM   3847 C CZ3 . TRP B 1 205 ? 4.26000   -13.40100 -21.56900 1.000 35.09000 ? 207 TRP B CZ3 1 
ATOM   3848 C CH2 . TRP B 1 205 ? 4.05800   -12.38200 -22.50900 1.000 37.80000 ? 207 TRP B CH2 1 
ATOM   3849 N N   . LEU B 1 206 ? 0.89200   -15.98500 -18.86900 1.000 29.30000 ? 208 LEU B N   1 
ATOM   3850 C CA  . LEU B 1 206 ? 0.70600   -16.99600 -19.90900 1.000 28.76000 ? 208 LEU B CA  1 
ATOM   3851 C C   . LEU B 1 206 ? -0.72900  -17.51800 -19.91400 1.000 28.25000 ? 208 LEU B C   1 
ATOM   3852 O O   . LEU B 1 206 ? -1.30200  -17.75100 -20.98300 1.000 31.32000 ? 208 LEU B O   1 
ATOM   3853 C CB  . LEU B 1 206 ? 1.70400   -18.14800 -19.72800 1.000 26.65000 ? 208 LEU B CB  1 
ATOM   3854 C CG  . LEU B 1 206 ? 3.18300   -17.82400 -19.95600 1.000 27.82000 ? 208 LEU B CG  1 
ATOM   3855 C CD1 . LEU B 1 206 ? 4.05800   -19.05600 -19.71000 1.000 28.62000 ? 208 LEU B CD1 1 
ATOM   3856 C CD2 . LEU B 1 206 ? 3.43200   -17.27800 -21.36600 1.000 25.97000 ? 208 LEU B CD2 1 
ATOM   3857 N N   . TYR B 1 207 ? -1.33500  -17.69700 -18.73400 1.000 27.94000 ? 209 TYR B N   1 
ATOM   3858 C CA  . TYR B 1 207 ? -2.75700  -18.05100 -18.69000 1.000 30.14000 ? 209 TYR B CA  1 
ATOM   3859 C C   . TYR B 1 207 ? -3.61200  -16.94200 -19.29600 1.000 33.36000 ? 209 TYR B C   1 
ATOM   3860 O O   . TYR B 1 207 ? -4.53600  -17.21300 -20.07600 1.000 33.60000 ? 209 TYR B O   1 
ATOM   3861 C CB  . TYR B 1 207 ? -3.19700  -18.34300 -17.25100 1.000 32.62000 ? 209 TYR B CB  1 
ATOM   3862 C CG  . TYR B 1 207 ? -2.84000  -19.73500 -16.75500 1.000 33.23000 ? 209 TYR B CG  1 
ATOM   3863 C CD1 . TYR B 1 207 ? -3.51900  -20.86800 -17.21000 1.000 41.58000 ? 209 TYR B CD1 1 
ATOM   3864 C CD2 . TYR B 1 207 ? -1.82900  -19.91300 -15.83000 1.000 33.46000 ? 209 TYR B CD2 1 
ATOM   3865 C CE1 . TYR B 1 207 ? -3.18500  -22.14200 -16.74900 1.000 39.80000 ? 209 TYR B CE1 1 
ATOM   3866 C CE2 . TYR B 1 207 ? -1.48200  -21.16800 -15.37100 1.000 37.38000 ? 209 TYR B CE2 1 
ATOM   3867 C CZ  . TYR B 1 207 ? -2.15900  -22.28200 -15.82600 1.000 43.26000 ? 209 TYR B CZ  1 
ATOM   3868 O OH  . TYR B 1 207 ? -1.78900  -23.53100 -15.35400 1.000 40.20000 ? 209 TYR B OH  1 
ATOM   3869 N N   . ALA B 1 208 ? -3.31700  -15.68500 -18.94900 1.000 32.09000 ? 210 ALA B N   1 
ATOM   3870 C CA  . ALA B 1 208 ? -4.00100  -14.55800 -19.57500 1.000 33.53000 ? 210 ALA B CA  1 
ATOM   3871 C C   . ALA B 1 208 ? -3.89100  -14.61900 -21.09300 1.000 35.63000 ? 210 ALA B C   1 
ATOM   3872 O O   . ALA B 1 208 ? -4.86400  -14.33100 -21.80400 1.000 35.79000 ? 210 ALA B O   1 
ATOM   3873 C CB  . ALA B 1 208 ? -3.43600  -13.23500 -19.05600 1.000 32.26000 ? 210 ALA B CB  1 
ATOM   3874 N N   . ALA B 1 209 ? -2.71700  -14.99600 -21.60900 1.000 33.59000 ? 211 ALA B N   1 
ATOM   3875 C CA  . ALA B 1 209 ? -2.54300  -15.10000 -23.05500 1.000 34.86000 ? 211 ALA B CA  1 
ATOM   3876 C C   . ALA B 1 209 ? -3.45500  -16.16500 -23.64900 1.000 38.83000 ? 211 ALA B C   1 
ATOM   3877 O O   . ALA B 1 209 ? -4.04800  -15.95600 -24.71400 1.000 36.79000 ? 211 ALA B O   1 
ATOM   3878 C CB  . ALA B 1 209 ? -1.08700  -15.40700 -23.39900 1.000 34.94000 ? 211 ALA B CB  1 
ATOM   3879 N N   . VAL B 1 210 ? -3.55600  -17.32100 -22.98600 1.000 36.68000 ? 212 VAL B N   1 
ATOM   3880 C CA  . VAL B 1 210 ? -4.39300  -18.41100 -23.48600 1.000 39.06000 ? 212 VAL B CA  1 
ATOM   3881 C C   . VAL B 1 210 ? -5.86400  -18.02500 -23.42800 1.000 40.39000 ? 212 VAL B C   1 
ATOM   3882 O O   . VAL B 1 210 ? -6.63600  -18.34400 -24.33800 1.000 42.82000 ? 212 VAL B O   1 
ATOM   3883 C CB  . VAL B 1 210 ? -4.11800  -19.70500 -22.69300 1.000 36.57000 ? 212 VAL B CB  1 
ATOM   3884 C CG1 . VAL B 1 210 ? -5.12800  -20.78600 -23.06600 1.000 39.12000 ? 212 VAL B CG1 1 
ATOM   3885 C CG2 . VAL B 1 210 ? -2.70200  -20.18700 -22.93300 1.000 34.52000 ? 212 VAL B CG2 1 
ATOM   3886 N N   . ILE B 1 211 ? -6.27500  -17.34600 -22.35400 1.000 37.55000 ? 213 ILE B N   1 
ATOM   3887 C CA  . ILE B 1 211 ? -7.65900  -16.90000 -22.21800 1.000 39.90000 ? 213 ILE B CA  1 
ATOM   3888 C C   . ILE B 1 211 ? -8.02100  -15.95100 -23.35200 1.000 45.15000 ? 213 ILE B C   1 
ATOM   3889 O O   . ILE B 1 211 ? -9.13800  -15.98600 -23.88000 1.000 44.36000 ? 213 ILE B O   1 
ATOM   3890 C CB  . ILE B 1 211 ? -7.87200  -16.26100 -20.83400 1.000 37.22000 ? 213 ILE B CB  1 
ATOM   3891 C CG1 . ILE B 1 211 ? -7.77200  -17.33800 -19.75100 1.000 38.89000 ? 213 ILE B CG1 1 
ATOM   3892 C CG2 . ILE B 1 211 ? -9.21200  -15.51200 -20.75900 1.000 39.52000 ? 213 ILE B CG2 1 
ATOM   3893 C CD1 . ILE B 1 211 ? -7.78700  -16.79100 -18.35100 1.000 40.12000 ? 213 ILE B CD1 1 
ATOM   3894 N N   . ASN B 1 212 ? -7.07500  -15.11400 -23.77200 1.000 41.98000 ? 214 ASN B N   1 
ATOM   3895 C CA  . ASN B 1 212 ? -7.26300  -14.35400 -25.00000 1.000 43.34000 ? 214 ASN B CA  1 
ATOM   3896 C C   . ASN B 1 212 ? -6.93500  -15.27100 -26.17900 1.000 43.46000 ? 214 ASN B C   1 
ATOM   3897 O O   . ASN B 1 212 ? -7.26000  -16.45900 -26.14300 1.000 49.05000 ? 214 ASN B O   1 
ATOM   3898 C CB  . ASN B 1 212 ? -6.41500  -13.07800 -24.97700 1.000 41.96000 ? 214 ASN B CB  1 
ATOM   3899 C CG  . ASN B 1 212 ? -6.84700  -12.11400 -23.88000 1.000 47.37000 ? 214 ASN B CG  1 
ATOM   3900 O OD1 . ASN B 1 212 ? -7.59500  -11.16300 -24.12600 1.000 52.60000 ? 214 ASN B OD1 1 
ATOM   3901 N ND2 . ASN B 1 212 ? -6.39200  -12.36500 -22.65500 1.000 46.04000 ? 214 ASN B ND2 1 
ATOM   3902 N N   . GLY B 1 213 ? -6.29500  -14.76800 -27.22200 1.000 48.38000 ? 215 GLY B N   1 
ATOM   3903 C CA  . GLY B 1 213 ? -6.11100  -15.61500 -28.38900 1.000 50.54000 ? 215 GLY B CA  1 
ATOM   3904 C C   . GLY B 1 213 ? -4.90400  -16.53700 -28.43700 1.000 47.97000 ? 215 GLY B C   1 
ATOM   3905 O O   . GLY B 1 213 ? -4.91700  -17.52200 -29.18100 1.000 43.65000 ? 215 GLY B O   1 
ATOM   3906 N N   . ASP B 1 214 ? -3.87800  -16.25400 -27.63100 1.000 42.91000 ? 216 ASP B N   1 
ATOM   3907 C CA  . ASP B 1 214 ? -2.51700  -16.72800 -27.87000 1.000 43.52000 ? 216 ASP B CA  1 
ATOM   3908 C C   . ASP B 1 214 ? -2.29700  -18.12500 -27.28800 1.000 43.44000 ? 216 ASP B C   1 
ATOM   3909 O O   . ASP B 1 214 ? -2.32800  -18.30200 -26.06500 1.000 45.61000 ? 216 ASP B O   1 
ATOM   3910 C CB  . ASP B 1 214 ? -1.52600  -15.73800 -27.26000 1.000 43.78000 ? 216 ASP B CB  1 
ATOM   3911 C CG  . ASP B 1 214 ? -0.96100  -14.76900 -28.28200 1.000 49.67000 ? 216 ASP B CG  1 
ATOM   3912 O OD1 . ASP B 1 214 ? -0.68700  -15.20600 -29.42200 1.000 51.13000 ? 216 ASP B OD1 1 
ATOM   3913 O OD2 . ASP B 1 214 ? -0.78300  -13.57400 -27.93900 1.000 47.16000 ? 216 ASP B OD2 1 
ATOM   3914 N N   . ARG B 1 215 ? -2.02000  -19.10600 -28.15700 1.000 42.68000 ? 217 ARG B N   1 
ATOM   3915 C CA  . ARG B 1 215 ? -1.87800  -20.49600 -27.73700 1.000 41.42000 ? 217 ARG B CA  1 
ATOM   3916 C C   . ARG B 1 215 ? -0.66300  -21.20900 -28.31200 1.000 41.30000 ? 217 ARG B C   1 
ATOM   3917 O O   . ARG B 1 215 ? -0.48500  -22.40100 -28.03800 1.000 43.54000 ? 217 ARG B O   1 
ATOM   3918 C CB  . ARG B 1 215 ? -3.12900  -21.30600 -28.11600 1.000 44.14000 ? 217 ARG B CB  1 
ATOM   3919 C CG  . ARG B 1 215 ? -4.33300  -21.05300 -27.23300 1.000 46.25000 ? 217 ARG B CG  1 
ATOM   3920 C CD  . ARG B 1 215 ? -5.52000  -21.89300 -27.68000 1.000 46.94000 ? 217 ARG B CD  1 
ATOM   3921 N NE  . ARG B 1 215 ? -5.44800  -23.26000 -27.17400 1.000 48.03000 ? 217 ARG B NE  1 
ATOM   3922 C CZ  . ARG B 1 215 ? -6.10500  -23.69200 -26.10100 1.000 47.05000 ? 217 ARG B CZ  1 
ATOM   3923 N NH1 . ARG B 1 215 ? -5.98500  -24.95500 -25.71500 1.000 48.54000 ? 217 ARG B NH1 1 
ATOM   3924 N NH2 . ARG B 1 215 ? -6.89100  -22.86200 -25.42000 1.000 47.06000 ? 217 ARG B NH2 1 
ATOM   3925 N N   . TRP B 1 216 ? 0.17700   -20.52600 -29.09400 1.000 39.16000 ? 218 TRP B N   1 
ATOM   3926 C CA  . TRP B 1 216 ? 1.21700   -21.21300 -29.85300 1.000 39.92000 ? 218 TRP B CA  1 
ATOM   3927 C C   . TRP B 1 216 ? 2.30300   -21.81900 -28.97000 1.000 40.61000 ? 218 TRP B C   1 
ATOM   3928 O O   . TRP B 1 216 ? 3.03400   -22.70700 -29.43000 1.000 41.61000 ? 218 TRP B O   1 
ATOM   3929 C CB  . TRP B 1 216 ? 1.84600   -20.24600 -30.85800 1.000 41.61000 ? 218 TRP B CB  1 
ATOM   3930 C CG  . TRP B 1 216 ? 2.50300   -19.04400 -30.22700 1.000 42.17000 ? 218 TRP B CG  1 
ATOM   3931 C CD1 . TRP B 1 216 ? 1.97300   -17.79100 -30.10000 1.000 41.11000 ? 218 TRP B CD1 1 
ATOM   3932 C CD2 . TRP B 1 216 ? 3.81100   -18.98800 -29.64300 1.000 42.01000 ? 218 TRP B CD2 1 
ATOM   3933 N NE1 . TRP B 1 216 ? 2.87100   -16.95800 -29.47400 1.000 43.78000 ? 218 TRP B NE1 1 
ATOM   3934 C CE2 . TRP B 1 216 ? 4.00700   -17.66900 -29.18300 1.000 40.83000 ? 218 TRP B CE2 1 
ATOM   3935 C CE3 . TRP B 1 216 ? 4.83600   -19.92400 -29.46500 1.000 43.29000 ? 218 TRP B CE3 1 
ATOM   3936 C CZ2 . TRP B 1 216 ? 5.18300   -17.26300 -28.55300 1.000 43.95000 ? 218 TRP B CZ2 1 
ATOM   3937 C CZ3 . TRP B 1 216 ? 6.01000   -19.51900 -28.83600 1.000 44.89000 ? 218 TRP B CZ3 1 
ATOM   3938 C CH2 . TRP B 1 216 ? 6.17100   -18.20000 -28.38900 1.000 45.11000 ? 218 TRP B CH2 1 
ATOM   3939 N N   . PHE B 1 217 ? 2.44800   -21.34800 -27.72900 1.000 38.09000 ? 219 PHE B N   1 
ATOM   3940 C CA  . PHE B 1 217 ? 3.50700   -21.83100 -26.84700 1.000 40.25000 ? 219 PHE B CA  1 
ATOM   3941 C C   . PHE B 1 217 ? 3.11100   -23.07500 -26.06400 1.000 40.47000 ? 219 PHE B C   1 
ATOM   3942 O O   . PHE B 1 217 ? 3.97900   -23.68700 -25.42700 1.000 40.37000 ? 219 PHE B O   1 
ATOM   3943 C CB  . PHE B 1 217 ? 3.92700   -20.72700 -25.86600 1.000 38.28000 ? 219 PHE B CB  1 
ATOM   3944 C CG  . PHE B 1 217 ? 2.76800   -20.07200 -25.16300 1.000 36.56000 ? 219 PHE B CG  1 
ATOM   3945 C CD1 . PHE B 1 217 ? 2.22800   -20.63500 -24.01600 1.000 34.95000 ? 219 PHE B CD1 1 
ATOM   3946 C CD2 . PHE B 1 217 ? 2.21000   -18.90100 -25.65800 1.000 36.90000 ? 219 PHE B CD2 1 
ATOM   3947 C CE1 . PHE B 1 217 ? 1.15400   -20.04100 -23.37100 1.000 34.37000 ? 219 PHE B CE1 1 
ATOM   3948 C CE2 . PHE B 1 217 ? 1.13400   -18.29900 -25.02000 1.000 34.95000 ? 219 PHE B CE2 1 
ATOM   3949 C CZ  . PHE B 1 217 ? 0.60100   -18.86800 -23.87600 1.000 34.76000 ? 219 PHE B CZ  1 
ATOM   3950 N N   . LEU B 1 218 ? 1.83400   -23.45000 -26.08300 1.000 39.06000 ? 220 LEU B N   1 
ATOM   3951 C CA  . LEU B 1 218 ? 1.40200   -24.66400 -25.41500 1.000 40.22000 ? 220 LEU B CA  1 
ATOM   3952 C C   . LEU B 1 218 ? 1.99000   -25.88700 -26.11600 1.000 42.45000 ? 220 LEU B C   1 
ATOM   3953 O O   . LEU B 1 218 ? 2.34300   -25.85200 -27.30000 1.000 40.29000 ? 220 LEU B O   1 
ATOM   3954 C CB  . LEU B 1 218 ? -0.12300  -24.73900 -25.38000 1.000 40.54000 ? 220 LEU B CB  1 
ATOM   3955 C CG  . LEU B 1 218 ? -0.81000  -23.57200 -24.66900 1.000 43.08000 ? 220 LEU B CG  1 
ATOM   3956 C CD1 . LEU B 1 218 ? -2.31700  -23.68000 -24.79200 1.000 40.37000 ? 220 LEU B CD1 1 
ATOM   3957 C CD2 . LEU B 1 218 ? -0.38500  -23.51100 -23.20200 1.000 39.01000 ? 220 LEU B CD2 1 
ATOM   3958 N N   . ASN B 1 219 ? 2.11500   -26.97400 -25.36000 1.000 42.49000 ? 221 ASN B N   1 
ATOM   3959 C CA  . ASN B 1 219 ? 2.64700   -28.21700 -25.89700 1.000 36.92000 ? 221 ASN B CA  1 
ATOM   3960 C C   . ASN B 1 219 ? 2.03800   -29.37500 -25.11700 1.000 37.76000 ? 221 ASN B C   1 
ATOM   3961 O O   . ASN B 1 219 ? 1.29400   -29.17900 -24.15200 1.000 34.53000 ? 221 ASN B O   1 
ATOM   3962 C CB  . ASN B 1 219 ? 4.18400   -28.22700 -25.86500 1.000 36.84000 ? 221 ASN B CB  1 
ATOM   3963 C CG  . ASN B 1 219 ? 4.75100   -28.10800 -24.46000 1.000 36.66000 ? 221 ASN B CG  1 
ATOM   3964 O OD1 . ASN B 1 219 ? 4.14300   -28.53900 -23.48000 1.000 37.27000 ? 221 ASN B OD1 1 
ATOM   3965 N ND2 . ASN B 1 219 ? 5.93100   -27.51800 -24.36200 1.000 39.68000 ? 221 ASN B ND2 1 
ATOM   3966 N N   . ARG B 1 220 ? 2.38600   -30.59200 -25.53500 1.000 35.76000 ? 222 ARG B N   1 
ATOM   3967 C CA  . ARG B 1 220 ? 1.81100   -31.81000 -24.97700 1.000 36.23000 ? 222 ARG B CA  1 
ATOM   3968 C C   . ARG B 1 220 ? 2.42200   -32.22800 -23.64000 1.000 35.71000 ? 222 ARG B C   1 
ATOM   3969 O O   . ARG B 1 220 ? 1.89400   -33.14800 -23.00300 1.000 33.56000 ? 222 ARG B O   1 
ATOM   3970 C CB  . ARG B 1 220 ? 1.98600   -32.95200 -25.96800 1.000 34.43000 ? 222 ARG B CB  1 
ATOM   3971 C CG  . ARG B 1 220 ? 3.41200   -33.49100 -25.88800 1.000 35.87000 ? 222 ARG B CG  1 
ATOM   3972 C CD  . ARG B 1 220 ? 3.55000   -34.87600 -26.49700 1.000 35.28000 ? 222 ARG B CD  1 
ATOM   3973 N NE  . ARG B 1 220 ? 2.88200   -34.99600 -27.79300 1.000 36.79000 ? 222 ARG B NE  1 
ATOM   3974 C CZ  . ARG B 1 220 ? 2.01000   -35.93800 -28.12900 1.000 34.56000 ? 222 ARG B CZ  1 
ATOM   3975 N NH1 . ARG B 1 220 ? 1.66200   -36.88800 -27.28300 1.000 40.79000 ? 222 ARG B NH1 1 
ATOM   3976 N NH2 . ARG B 1 220 ? 1.50100   -35.93800 -29.34100 1.000 33.61000 ? 222 ARG B NH2 1 
ATOM   3977 N N   . PHE B 1 221 ? 3.50800   -31.60000 -23.20700 1.000 34.43000 ? 223 PHE B N   1 
ATOM   3978 C CA  . PHE B 1 221 ? 4.34700   -32.12400 -22.13500 1.000 37.39000 ? 223 PHE B CA  1 
ATOM   3979 C C   . PHE B 1 221 ? 3.96900   -31.51300 -20.79200 1.000 42.41000 ? 223 PHE B C   1 
ATOM   3980 O O   . PHE B 1 221 ? 3.29100   -30.48700 -20.71900 1.000 38.76000 ? 223 PHE B O   1 
ATOM   3981 C CB  . PHE B 1 221 ? 5.83100   -31.85700 -22.42100 1.000 32.27000 ? 223 PHE B CB  1 
ATOM   3982 C CG  . PHE B 1 221 ? 6.27800   -32.32500 -23.77900 1.000 35.06000 ? 223 PHE B CG  1 
ATOM   3983 C CD1 . PHE B 1 221 ? 6.46300   -33.68200 -24.03900 1.000 31.95000 ? 223 PHE B CD1 1 
ATOM   3984 C CD2 . PHE B 1 221 ? 6.48700   -31.41500 -24.80600 1.000 32.52000 ? 223 PHE B CD2 1 
ATOM   3985 C CE1 . PHE B 1 221 ? 6.85000   -34.11100 -25.29300 1.000 32.69000 ? 223 PHE B CE1 1 
ATOM   3986 C CE2 . PHE B 1 221 ? 6.87200   -31.83600 -26.05900 1.000 32.08000 ? 223 PHE B CE2 1 
ATOM   3987 C CZ  . PHE B 1 221 ? 7.05500   -33.18400 -26.31200 1.000 32.46000 ? 223 PHE B CZ  1 
ATOM   3988 N N   . THR B 1 222 ? 4.41500   -32.17700 -19.72700 1.000 39.93000 ? 224 THR B N   1 
ATOM   3989 C CA  . THR B 1 222 ? 4.38400   -31.66400 -18.36700 1.000 44.23000 ? 224 THR B CA  1 
ATOM   3990 C C   . THR B 1 222 ? 5.78100   -31.85200 -17.77100 1.000 43.45000 ? 224 THR B C   1 
ATOM   3991 O O   . THR B 1 222 ? 6.65700   -32.49200 -18.36200 1.000 43.83000 ? 224 THR B O   1 
ATOM   3992 C CB  . THR B 1 222 ? 3.29000   -32.36000 -17.53400 1.000 45.17000 ? 224 THR B CB  1 
ATOM   3993 O OG1 . THR B 1 222 ? 2.02100   -32.23200 -18.18900 1.000 48.62000 ? 224 THR B OG1 1 
ATOM   3994 C CG2 . THR B 1 222 ? 3.15100   -31.72700 -16.15900 1.000 49.14000 ? 224 THR B CG2 1 
ATOM   3995 N N   . THR B 1 223 ? 6.00900   -31.26100 -16.60400 1.000 48.73000 ? 225 THR B N   1 
ATOM   3996 C CA  . THR B 1 223 ? 7.28700   -31.34200 -15.92100 1.000 45.89000 ? 225 THR B CA  1 
ATOM   3997 C C   . THR B 1 223 ? 7.00800   -31.60800 -14.44700 1.000 46.16000 ? 225 THR B C   1 
ATOM   3998 O O   . THR B 1 223 ? 5.85400   -31.77300 -14.03500 1.000 45.64000 ? 225 THR B O   1 
ATOM   3999 C CB  . THR B 1 223 ? 8.10000   -30.05500 -16.12700 1.000 47.41000 ? 225 THR B CB  1 
ATOM   4000 O OG1 . THR B 1 223 ? 9.40200   -30.19800 -15.55400 1.000 51.25000 ? 225 THR B OG1 1 
ATOM   4001 C CG2 . THR B 1 223 ? 7.39000   -28.87100 -15.48100 1.000 47.92000 ? 225 THR B CG2 1 
ATOM   4002 N N   . THR B 1 224 ? 8.06900   -31.65500 -13.64500 1.000 50.08000 ? 226 THR B N   1 
ATOM   4003 C CA  . THR B 1 224 ? 7.93600   -31.73200 -12.19700 1.000 53.36000 ? 226 THR B CA  1 
ATOM   4004 C C   . THR B 1 224 ? 8.36600   -30.41300 -11.57000 1.000 47.55000 ? 226 THR B C   1 
ATOM   4005 O O   . THR B 1 224 ? 9.15000   -29.65700 -12.15100 1.000 45.74000 ? 226 THR B O   1 
ATOM   4006 C CB  . THR B 1 224 ? 8.76900   -32.87600 -11.61000 1.000 47.21000 ? 226 THR B CB  1 
ATOM   4007 O OG1 . THR B 1 224 ? 10.15500  -32.64800 -11.88400 1.000 51.00000 ? 226 THR B OG1 1 
ATOM   4008 C CG2 . THR B 1 224 ? 8.34700   -34.19900 -12.22600 1.000 52.35000 ? 226 THR B CG2 1 
ATOM   4009 N N   . LEU B 1 225 ? 7.82600   -30.14100 -10.37900 1.000 49.37000 ? 227 LEU B N   1 
ATOM   4010 C CA  . LEU B 1 225 ? 8.22800   -28.94900 -9.64200  1.000 46.32000 ? 227 LEU B CA  1 
ATOM   4011 C C   . LEU B 1 225 ? 9.73800   -28.89900 -9.48200  1.000 47.00000 ? 227 LEU B C   1 
ATOM   4012 O O   . LEU B 1 225 ? 10.36400  -27.85900 -9.71900  1.000 45.74000 ? 227 LEU B O   1 
ATOM   4013 C CB  . LEU B 1 225 ? 7.53300   -28.92200 -8.28100  1.000 47.57000 ? 227 LEU B CB  1 
ATOM   4014 C CG  . LEU B 1 225 ? 7.40200   -27.55500 -7.61100  1.000 46.67000 ? 227 LEU B CG  1 
ATOM   4015 C CD1 . LEU B 1 225 ? 7.11400   -26.47800 -8.64700  1.000 44.02000 ? 227 LEU B CD1 1 
ATOM   4016 C CD2 . LEU B 1 225 ? 6.30700   -27.58800 -6.54600  1.000 45.40000 ? 227 LEU B CD2 1 
ATOM   4017 N N   . ASN B 1 226 ? 10.34700  -30.03100 -9.11700  1.000 49.46000 ? 228 ASN B N   1 
ATOM   4018 C CA  . ASN B 1 226 ? 11.79600  -30.06800 -8.94600  1.000 48.28000 ? 228 ASN B CA  1 
ATOM   4019 C C   . ASN B 1 226 ? 12.52100  -29.79100 -10.26000 1.000 49.87000 ? 228 ASN B C   1 
ATOM   4020 O O   . ASN B 1 226 ? 13.48400  -29.01600 -10.29000 1.000 47.72000 ? 228 ASN B O   1 
ATOM   4021 C CB  . ASN B 1 226 ? 12.21800  -31.42000 -8.36300  1.000 52.14000 ? 228 ASN B CB  1 
ATOM   4022 C CG  . ASN B 1 226 ? 13.73000  -31.56600 -8.25700  1.000 60.08000 ? 228 ASN B CG  1 
ATOM   4023 O OD1 . ASN B 1 226 ? 14.34200  -31.13900 -7.27400  1.000 62.83000 ? 228 ASN B OD1 1 
ATOM   4024 N ND2 . ASN B 1 226 ? 14.33900  -32.17600 -9.27200  1.000 59.59000 ? 228 ASN B ND2 1 
ATOM   4025 N N   . ASP B 1 227 ? 12.07100  -30.40600 -11.35900 1.000 49.78000 ? 229 ASP B N   1 
ATOM   4026 C CA  . ASP B 1 227 ? 12.74000  -30.20200 -12.64100 1.000 48.64000 ? 229 ASP B CA  1 
ATOM   4027 C C   . ASP B 1 227 ? 12.62800  -28.75400 -13.10000 1.000 46.57000 ? 229 ASP B C   1 
ATOM   4028 O O   . ASP B 1 227 ? 13.59700  -28.17600 -13.60800 1.000 47.88000 ? 229 ASP B O   1 
ATOM   4029 C CB  . ASP B 1 227 ? 12.15600  -31.13700 -13.70300 1.000 50.30000 ? 229 ASP B CB  1 
ATOM   4030 C CG  . ASP B 1 227 ? 12.65900  -32.56800 -13.56600 1.000 54.80000 ? 229 ASP B CG  1 
ATOM   4031 O OD1 . ASP B 1 227 ? 13.56700  -32.80800 -12.74200 1.000 53.68000 ? 229 ASP B OD1 1 
ATOM   4032 O OD2 . ASP B 1 227 ? 12.14600  -33.45200 -14.28800 1.000 53.60000 ? 229 ASP B OD2 1 
ATOM   4033 N N   . PHE B 1 228 ? 11.45000  -28.15300 -12.93300 1.000 48.41000 ? 230 PHE B N   1 
ATOM   4034 C CA  . PHE B 1 228 ? 11.26100  -26.78000 -13.39100 1.000 45.98000 ? 230 PHE B CA  1 
ATOM   4035 C C   . PHE B 1 228 ? 12.10800  -25.80800 -12.58200 1.000 47.08000 ? 230 PHE B C   1 
ATOM   4036 O O   . PHE B 1 228 ? 12.73400  -24.90100 -13.14500 1.000 47.74000 ? 230 PHE B O   1 
ATOM   4037 C CB  . PHE B 1 228 ? 9.78600   -26.39000 -13.31400 1.000 46.12000 ? 230 PHE B CB  1 
ATOM   4038 C CG  . PHE B 1 228 ? 9.54100   -24.94800 -13.64200 1.000 48.06000 ? 230 PHE B CG  1 
ATOM   4039 C CD1 . PHE B 1 228 ? 9.62900   -24.50100 -14.95300 1.000 46.98000 ? 230 PHE B CD1 1 
ATOM   4040 C CD2 . PHE B 1 228 ? 9.26300   -24.02900 -12.63700 1.000 46.94000 ? 230 PHE B CD2 1 
ATOM   4041 C CE1 . PHE B 1 228 ? 9.43000   -23.16800 -15.26100 1.000 46.53000 ? 230 PHE B CE1 1 
ATOM   4042 C CE2 . PHE B 1 228 ? 9.06200   -22.69400 -12.93700 1.000 46.29000 ? 230 PHE B CE2 1 
ATOM   4043 C CZ  . PHE B 1 228 ? 9.14900   -22.26200 -14.25200 1.000 45.87000 ? 230 PHE B CZ  1 
ATOM   4044 N N   . ASN B 1 229 ? 12.16000  -25.99800 -11.26100 1.000 49.20000 ? 231 ASN B N   1 
ATOM   4045 C CA  . ASN B 1 229 ? 12.90400  -25.07500 -10.41200 1.000 45.71000 ? 231 ASN B CA  1 
ATOM   4046 C C   . ASN B 1 229 ? 14.39600  -25.12500 -10.69400 1.000 48.04000 ? 231 ASN B C   1 
ATOM   4047 O O   . ASN B 1 229 ? 15.10100  -24.13200 -10.47700 1.000 49.82000 ? 231 ASN B O   1 
ATOM   4048 C CB  . ASN B 1 229 ? 12.60000  -25.37100 -8.94600  1.000 46.71000 ? 231 ASN B CB  1 
ATOM   4049 C CG  . ASN B 1 229 ? 11.30300  -24.73700 -8.50000  1.000 46.37000 ? 231 ASN B CG  1 
ATOM   4050 O OD1 . ASN B 1 229 ? 11.00000  -23.60800 -8.88800  1.000 47.48000 ? 231 ASN B OD1 1 
ATOM   4051 N ND2 . ASN B 1 229 ? 10.51700  -25.45800 -7.70600  1.000 45.28000 ? 231 ASN B ND2 1 
ATOM   4052 N N   . LEU B 1 230 ? 14.89900  -26.25600 -11.19200 1.000 48.84000 ? 232 LEU B N   1 
ATOM   4053 C CA  . LEU B 1 230 ? 16.28000  -26.28300 -11.65400 1.000 48.81000 ? 232 LEU B CA  1 
ATOM   4054 C C   . LEU B 1 230 ? 16.47100  -25.36600 -12.85500 1.000 47.39000 ? 232 LEU B C   1 
ATOM   4055 O O   . LEU B 1 230 ? 17.51300  -24.71200 -12.98600 1.000 49.59000 ? 232 LEU B O   1 
ATOM   4056 C CB  . LEU B 1 230 ? 16.69600  -27.71500 -11.98700 1.000 49.07000 ? 232 LEU B CB  1 
ATOM   4057 C CG  . LEU B 1 230 ? 17.14100  -28.50800 -10.76100 1.000 52.76000 ? 232 LEU B CG  1 
ATOM   4058 C CD1 . LEU B 1 230 ? 17.27800  -29.99100 -11.09000 1.000 56.76000 ? 232 LEU B CD1 1 
ATOM   4059 C CD2 . LEU B 1 230 ? 18.43900  -27.94100 -10.20600 1.000 53.82000 ? 232 LEU B CD2 1 
ATOM   4060 N N   . VAL B 1 231 ? 15.47100  -25.29400 -13.73400 1.000 46.94000 ? 233 VAL B N   1 
ATOM   4061 C CA  . VAL B 1 231 ? 15.55400  -24.38600 -14.87300 1.000 49.84000 ? 233 VAL B CA  1 
ATOM   4062 C C   . VAL B 1 231 ? 15.29400  -22.95100 -14.43600 1.000 44.60000 ? 233 VAL B C   1 
ATOM   4063 O O   . VAL B 1 231 ? 15.96200  -22.02100 -14.90300 1.000 45.38000 ? 233 VAL B O   1 
ATOM   4064 C CB  . VAL B 1 231 ? 14.58600  -24.84100 -15.98200 1.000 50.98000 ? 233 VAL B CB  1 
ATOM   4065 C CG1 . VAL B 1 231 ? 14.53000  -23.80800 -17.10900 1.000 50.41000 ? 233 VAL B CG1 1 
ATOM   4066 C CG2 . VAL B 1 231 ? 15.02800  -26.19500 -16.52100 1.000 49.81000 ? 233 VAL B CG2 1 
ATOM   4067 N N   . ALA B 1 232 ? 14.33300  -22.74900 -13.52900 1.000 41.59000 ? 234 ALA B N   1 
ATOM   4068 C CA  . ALA B 1 232 ? 14.11400  -21.41400 -12.98000 1.000 41.36000 ? 234 ALA B CA  1 
ATOM   4069 C C   . ALA B 1 232 ? 15.40200  -20.84000 -12.40000 1.000 43.58000 ? 234 ALA B C   1 
ATOM   4070 O O   . ALA B 1 232 ? 15.75200  -19.68600 -12.67500 1.000 40.85000 ? 234 ALA B O   1 
ATOM   4071 C CB  . ALA B 1 232 ? 13.01400  -21.45400 -11.91700 1.000 41.37000 ? 234 ALA B CB  1 
ATOM   4072 N N   . MET B 1 233 ? 16.13600  -21.64700 -11.62100 1.000 44.99000 ? 235 MET B N   1 
ATOM   4073 C CA  . MET B 1 233 ? 17.40000  -21.19900 -11.03900 1.000 44.38000 ? 235 MET B CA  1 
ATOM   4074 C C   . MET B 1 233 ? 18.36700  -20.73600 -12.11600 1.000 42.71000 ? 235 MET B C   1 
ATOM   4075 O O   . MET B 1 233 ? 18.99100  -19.67900 -11.99200 1.000 39.71000 ? 235 MET B O   1 
ATOM   4076 C CB  . MET B 1 233 ? 18.02200  -22.32500 -10.20900 1.000 45.52000 ? 235 MET B CB  1 
ATOM   4077 C CG  . MET B 1 233 ? 18.84900  -21.84900 -9.02600  1.000 55.93000 ? 235 MET B CG  1 
ATOM   4078 S SD  . MET B 1 233 ? 19.10600  -23.15600 -7.80100  1.000 68.37000 ? 235 MET B SD  1 
ATOM   4079 C CE  . MET B 1 233 ? 19.95100  -22.26200 -6.49800  1.000 61.68000 ? 235 MET B CE  1 
ATOM   4080 N N   . LYS B 1 234 ? 18.48400  -21.50700 -13.19800 1.000 43.61000 ? 236 LYS B N   1 
ATOM   4081 C CA  . LYS B 1 234 ? 19.43600  -21.16600 -14.24800 1.000 44.44000 ? 236 LYS B CA  1 
ATOM   4082 C C   . LYS B 1 234 ? 19.09900  -19.83100 -14.90000 1.000 43.75000 ? 236 LYS B C   1 
ATOM   4083 O O   . LYS B 1 234 ? 20.00000  -19.08000 -15.29200 1.000 44.57000 ? 236 LYS B O   1 
ATOM   4084 C CB  . LYS B 1 234 ? 19.47300  -22.27400 -15.29800 1.000 48.96000 ? 236 LYS B CB  1 
ATOM   4085 C CG  . LYS B 1 234 ? 20.70400  -22.22500 -16.20600 1.000 52.84000 ? 236 LYS B CG  1 
ATOM   4086 C CD  . LYS B 1 234 ? 20.41700  -22.82400 -17.58100 1.000 54.33000 ? 236 LYS B CD  1 
ATOM   4087 C CE  . LYS B 1 234 ? 19.80600  -24.22400 -17.48900 1.000 57.18000 ? 236 LYS B CE  1 
ATOM   4088 N NZ  . LYS B 1 234 ? 20.32900  -25.04200 -16.34900 1.000 61.97000 ? 236 LYS B NZ  1 
ATOM   4089 N N   . TYR B 1 235 ? 17.80900  -19.51200 -15.02700 1.000 41.65000 ? 237 TYR B N   1 
ATOM   4090 C CA  . TYR B 1 235 ? 17.40100  -18.32100 -15.75600 1.000 41.32000 ? 237 TYR B CA  1 
ATOM   4091 C C   . TYR B 1 235 ? 17.02500  -17.16900 -14.83500 1.000 40.08000 ? 237 TYR B C   1 
ATOM   4092 O O   . TYR B 1 235 ? 16.34900  -16.23200 -15.27300 1.000 37.89000 ? 237 TYR B O   1 
ATOM   4093 C CB  . TYR B 1 235 ? 16.26000  -18.66400 -16.71400 1.000 41.58000 ? 237 TYR B CB  1 
ATOM   4094 C CG  . TYR B 1 235 ? 16.77100  -19.46200 -17.89200 1.000 43.44000 ? 237 TYR B CG  1 
ATOM   4095 C CD1 . TYR B 1 235 ? 17.40300  -18.83200 -18.96000 1.000 46.42000 ? 237 TYR B CD1 1 
ATOM   4096 C CD2 . TYR B 1 235 ? 16.68200  -20.85100 -17.90700 1.000 46.78000 ? 237 TYR B CD2 1 
ATOM   4097 C CE1 . TYR B 1 235 ? 17.90300  -19.56200 -20.03100 1.000 47.86000 ? 237 TYR B CE1 1 
ATOM   4098 C CE2 . TYR B 1 235 ? 17.17500  -21.59100 -18.97300 1.000 47.10000 ? 237 TYR B CE2 1 
ATOM   4099 C CZ  . TYR B 1 235 ? 17.78100  -20.94100 -20.02900 1.000 48.62000 ? 237 TYR B CZ  1 
ATOM   4100 O OH  . TYR B 1 235 ? 18.27000  -21.67500 -21.08600 1.000 54.96000 ? 237 TYR B OH  1 
ATOM   4101 N N   . ASN B 1 236 ? 17.47400  -17.20300 -13.57900 1.000 41.08000 ? 238 ASN B N   1 
ATOM   4102 C CA  . ASN B 1 236 ? 17.26800  -16.08800 -12.66100 1.000 36.06000 ? 238 ASN B CA  1 
ATOM   4103 C C   . ASN B 1 236 ? 15.77500  -15.85200 -12.42700 1.000 35.78000 ? 238 ASN B C   1 
ATOM   4104 O O   . ASN B 1 236 ? 15.29600  -14.71800 -12.43600 1.000 33.17000 ? 238 ASN B O   1 
ATOM   4105 C CB  . ASN B 1 236 ? 17.94800  -14.82600 -13.19500 1.000 38.43000 ? 238 ASN B CB  1 
ATOM   4106 C CG  . ASN B 1 236 ? 18.79400  -14.14100 -12.16700 1.000 46.66000 ? 238 ASN B CG  1 
ATOM   4107 O OD1 . ASN B 1 236 ? 19.71300  -14.74000 -11.60300 1.000 46.66000 ? 238 ASN B OD1 1 
ATOM   4108 N ND2 . ASN B 1 236 ? 18.51300  -12.86700 -11.92900 1.000 44.91000 ? 238 ASN B ND2 1 
ATOM   4109 N N   . TYR B 1 237 ? 15.03100  -16.94000 -12.26100 1.000 33.01000 ? 239 TYR B N   1 
ATOM   4110 C CA  . TYR B 1 237 ? 13.61300  -16.90300 -11.95100 1.000 34.21000 ? 239 TYR B CA  1 
ATOM   4111 C C   . TYR B 1 237 ? 13.41500  -17.33000 -10.50600 1.000 34.30000 ? 239 TYR B C   1 
ATOM   4112 O O   . TYR B 1 237 ? 14.10900  -18.22700 -10.02000 1.000 34.91000 ? 239 TYR B O   1 
ATOM   4113 C CB  . TYR B 1 237 ? 12.82300  -17.83100 -12.87800 1.000 32.38000 ? 239 TYR B CB  1 
ATOM   4114 C CG  . TYR B 1 237 ? 12.24800  -17.17800 -14.12100 1.000 30.20000 ? 239 TYR B CG  1 
ATOM   4115 C CD1 . TYR B 1 237 ? 13.05600  -16.47500 -15.01100 1.000 32.21000 ? 239 TYR B CD1 1 
ATOM   4116 C CD2 . TYR B 1 237 ? 10.88100  -17.28900 -14.41500 1.000 30.01000 ? 239 TYR B CD2 1 
ATOM   4117 C CE1 . TYR B 1 237 ? 12.51800  -15.88800 -16.16600 1.000 30.78000 ? 239 TYR B CE1 1 
ATOM   4118 C CE2 . TYR B 1 237 ? 10.34300  -16.71200 -15.55300 1.000 27.99000 ? 239 TYR B CE2 1 
ATOM   4119 C CZ  . TYR B 1 237 ? 11.16100  -16.01900 -16.42800 1.000 31.71000 ? 239 TYR B CZ  1 
ATOM   4120 O OH  . TYR B 1 237 ? 10.59800  -15.44800 -17.55400 1.000 29.79000 ? 239 TYR B OH  1 
ATOM   4121 N N   . GLU B 1 238 ? 12.46000  -16.69600 -9.82900  1.000 32.77000 ? 240 GLU B N   1 
ATOM   4122 C CA  . GLU B 1 238 ? 12.14400  -17.09300 -8.46800  1.000 36.01000 ? 240 GLU B CA  1 
ATOM   4123 C C   . GLU B 1 238 ? 11.69100  -18.55300 -8.44800  1.000 37.67000 ? 240 GLU B C   1 
ATOM   4124 O O   . GLU B 1 238 ? 11.07000  -19.03400 -9.40200  1.000 35.65000 ? 240 GLU B O   1 
ATOM   4125 C CB  . GLU B 1 238 ? 11.05500  -16.19200 -7.87400  1.000 33.38000 ? 240 GLU B CB  1 
ATOM   4126 C CG  . GLU B 1 238 ? 11.54000  -14.78400 -7.50900  1.000 35.76000 ? 240 GLU B CG  1 
ATOM   4127 C CD  . GLU B 1 238 ? 12.51800  -14.76500 -6.32800  1.000 41.27000 ? 240 GLU B CD  1 
ATOM   4128 O OE1 . GLU B 1 238 ? 12.09000  -15.03600 -5.18600  1.000 45.19000 ? 240 GLU B OE1 1 
ATOM   4129 O OE2 . GLU B 1 238 ? 13.71900  -14.46700 -6.54200  1.000 40.07000 ? 240 GLU B OE2 1 
ATOM   4130 N N   . PRO B 1 239 ? 12.01300  -19.29000 -7.38500  1.000 42.85000 ? 241 PRO B N   1 
ATOM   4131 C CA  . PRO B 1 239 ? 11.50600  -20.66200 -7.26600  1.000 41.87000 ? 241 PRO B CA  1 
ATOM   4132 C C   . PRO B 1 239 ? 9.98600   -20.68600 -7.22300  1.000 41.01000 ? 241 PRO B C   1 
ATOM   4133 O O   . PRO B 1 239 ? 9.33900   -19.78100 -6.69100  1.000 38.71000 ? 241 PRO B O   1 
ATOM   4134 C CB  . PRO B 1 239 ? 12.11500  -21.15900 -5.94600  1.000 41.11000 ? 241 PRO B CB  1 
ATOM   4135 C CG  . PRO B 1 239 ? 13.31900  -20.29900 -5.73200  1.000 39.93000 ? 241 PRO B CG  1 
ATOM   4136 C CD  . PRO B 1 239 ? 12.97000  -18.95200 -6.31300  1.000 39.95000 ? 241 PRO B CD  1 
ATOM   4137 N N   . LEU B 1 240 ? 9.41700   -21.73400 -7.81000  1.000 42.60000 ? 242 LEU B N   1 
ATOM   4138 C CA  . LEU B 1 240 ? 7.97900   -21.95400 -7.79500  1.000 37.59000 ? 242 LEU B CA  1 
ATOM   4139 C C   . LEU B 1 240 ? 7.63000   -22.91500 -6.66400  1.000 38.27000 ? 242 LEU B C   1 
ATOM   4140 O O   . LEU B 1 240 ? 8.18500   -24.01500 -6.58400  1.000 40.52000 ? 242 LEU B O   1 
ATOM   4141 C CB  . LEU B 1 240 ? 7.49800   -22.50800 -9.13500  1.000 39.39000 ? 242 LEU B CB  1 
ATOM   4142 C CG  . LEU B 1 240 ? 5.98500   -22.47100 -9.34500  1.000 37.31000 ? 242 LEU B CG  1 
ATOM   4143 C CD1 . LEU B 1 240 ? 5.53400   -21.04000 -9.62200  1.000 36.93000 ? 242 LEU B CD1 1 
ATOM   4144 C CD2 . LEU B 1 240 ? 5.58900   -23.39200 -10.48100 1.000 38.00000 ? 242 LEU B CD2 1 
ATOM   4145 N N   . THR B 1 241 ? 6.72700   -22.49200 -5.79100  1.000 37.46000 ? 243 THR B N   1 
ATOM   4146 C CA  . THR B 1 241 ? 6.32700   -23.26900 -4.62600  1.000 42.88000 ? 243 THR B CA  1 
ATOM   4147 C C   . THR B 1 241 ? 4.95200   -23.88500 -4.84900  1.000 42.72000 ? 243 THR B C   1 
ATOM   4148 O O   . THR B 1 241 ? 4.22600   -23.53300 -5.78400  1.000 38.42000 ? 243 THR B O   1 
ATOM   4149 C CB  . THR B 1 241 ? 6.30300   -22.40000 -3.36100  1.000 40.40000 ? 243 THR B CB  1 
ATOM   4150 O OG1 . THR B 1 241 ? 5.15500   -21.53900 -3.38900  1.000 40.77000 ? 243 THR B OG1 1 
ATOM   4151 C CG2 . THR B 1 241 ? 7.56700   -21.56100 -3.26100  1.000 44.59000 ? 243 THR B CG2 1 
ATOM   4152 N N   . GLN B 1 242 ? 4.60000   -24.82300 -3.96200  1.000 39.20000 ? 244 GLN B N   1 
ATOM   4153 C CA  . GLN B 1 242 ? 3.27800   -25.43600 -4.02800  1.000 44.66000 ? 244 GLN B CA  1 
ATOM   4154 C C   . GLN B 1 242 ? 2.18500   -24.39500 -3.83400  1.000 44.87000 ? 244 GLN B C   1 
ATOM   4155 O O   . GLN B 1 242 ? 1.12400   -24.46800 -4.46700  1.000 43.87000 ? 244 GLN B O   1 
ATOM   4156 C CB  . GLN B 1 242 ? 3.15200   -26.54100 -2.98000  1.000 44.51000 ? 244 GLN B CB  1 
ATOM   4157 C CG  . GLN B 1 242 ? 1.81900   -27.26300 -3.02400  1.000 48.28000 ? 244 GLN B CG  1 
ATOM   4158 C CD  . GLN B 1 242 ? 1.59400   -27.94300 -4.35300  1.000 44.07000 ? 244 GLN B CD  1 
ATOM   4159 O OE1 . GLN B 1 242 ? 2.48100   -28.62000 -4.86800  1.000 45.89000 ? 244 GLN B OE1 1 
ATOM   4160 N NE2 . GLN B 1 242 ? 0.41400   -27.76100 -4.92300  1.000 48.22000 ? 244 GLN B NE2 1 
ATOM   4161 N N   . ASP B 1 243 ? 2.43100   -23.40500 -2.97400  1.000 43.37000 ? 245 ASP B N   1 
ATOM   4162 C CA  . ASP B 1 243 ? 1.42700   -22.37300 -2.75100  1.000 45.10000 ? 245 ASP B CA  1 
ATOM   4163 C C   . ASP B 1 243 ? 1.18100   -21.54500 -4.00700  1.000 45.64000 ? 245 ASP B C   1 
ATOM   4164 O O   . ASP B 1 243 ? 0.06200   -21.06600 -4.22100  1.000 47.47000 ? 245 ASP B O   1 
ATOM   4165 C CB  . ASP B 1 243 ? 1.84600   -21.47700 -1.58700  1.000 48.90000 ? 245 ASP B CB  1 
ATOM   4166 C CG  . ASP B 1 243 ? 0.80900   -20.42300 -1.26200  1.000 51.85000 ? 245 ASP B CG  1 
ATOM   4167 O OD1 . ASP B 1 243 ? -0.40000  -20.76000 -1.20800  1.000 60.76000 ? 245 ASP B OD1 1 
ATOM   4168 O OD2 . ASP B 1 243 ? 1.20100   -19.25500 -1.06000  1.000 56.87000 ? 245 ASP B OD2 1 
ATOM   4169 N N   . HIS B 1 244 ? 2.20200   -21.36600 -4.84700  1.000 42.41000 ? 246 HIS B N   1 
ATOM   4170 C CA  . HIS B 1 244 ? 1.98600   -20.72200 -6.14000  1.000 42.94000 ? 246 HIS B CA  1 
ATOM   4171 C C   . HIS B 1 244 ? 1.11100   -21.58800 -7.03200  1.000 42.57000 ? 246 HIS B C   1 
ATOM   4172 O O   . HIS B 1 244 ? 0.17600   -21.09700 -7.67600  1.000 39.88000 ? 246 HIS B O   1 
ATOM   4173 C CB  . HIS B 1 244 ? 3.32200   -20.44700 -6.82700  1.000 41.18000 ? 246 HIS B CB  1 
ATOM   4174 C CG  . HIS B 1 244 ? 4.17300   -19.43300 -6.12800  1.000 40.13000 ? 246 HIS B CG  1 
ATOM   4175 N ND1 . HIS B 1 244 ? 5.55000   -19.48500 -6.14900  1.000 38.33000 ? 246 HIS B ND1 1 
ATOM   4176 C CD2 . HIS B 1 244 ? 3.84900   -18.33100 -5.41000  1.000 40.11000 ? 246 HIS B CD2 1 
ATOM   4177 C CE1 . HIS B 1 244 ? 6.03800   -18.46500 -5.46700  1.000 40.57000 ? 246 HIS B CE1 1 
ATOM   4178 N NE2 . HIS B 1 244 ? 5.02800   -17.74800 -5.01000  1.000 40.79000 ? 246 HIS B NE2 1 
ATOM   4179 N N   . VAL B 1 245 ? 1.41300   -22.88900 -7.08600  1.000 42.68000 ? 247 VAL B N   1 
ATOM   4180 C CA  . VAL B 1 245 ? 0.61700   -23.80900 -7.89400  1.000 42.34000 ? 247 VAL B CA  1 
ATOM   4181 C C   . VAL B 1 245 ? -0.84500  -23.77000 -7.46400  1.000 42.63000 ? 247 VAL B C   1 
ATOM   4182 O O   . VAL B 1 245 ? -1.75400  -23.80100 -8.30200  1.000 43.90000 ? 247 VAL B O   1 
ATOM   4183 C CB  . VAL B 1 245 ? 1.20800   -25.23100 -7.81300  1.000 43.82000 ? 247 VAL B CB  1 
ATOM   4184 C CG1 . VAL B 1 245 ? 0.31900   -26.23600 -8.53300  1.000 41.65000 ? 247 VAL B CG1 1 
ATOM   4185 C CG2 . VAL B 1 245 ? 2.61400   -25.25200 -8.39600  1.000 41.92000 ? 247 VAL B CG2 1 
ATOM   4186 N N   . ASP B 1 246 ? -1.09900  -23.66100 -6.15600  1.000 45.03000 ? 248 ASP B N   1 
ATOM   4187 C CA  . ASP B 1 246 ? -2.48200  -23.60800 -5.67900  1.000 46.96000 ? 248 ASP B CA  1 
ATOM   4188 C C   . ASP B 1 246 ? -3.15600  -22.29800 -6.07400  1.000 45.32000 ? 248 ASP B C   1 
ATOM   4189 O O   . ASP B 1 246 ? -4.32700  -22.29200 -6.47400  1.000 43.39000 ? 248 ASP B O   1 
ATOM   4190 C CB  . ASP B 1 246 ? -2.53200  -23.79000 -4.15900  1.000 46.44000 ? 248 ASP B CB  1 
ATOM   4191 C CG  . ASP B 1 246 ? -1.93400  -25.10600 -3.70100  1.000 48.53000 ? 248 ASP B CG  1 
ATOM   4192 O OD1 . ASP B 1 246 ? -1.93500  -26.08600 -4.48000  1.000 50.00000 ? 248 ASP B OD1 1 
ATOM   4193 O OD2 . ASP B 1 246 ? -1.46200  -25.15900 -2.54400  1.000 52.95000 ? 248 ASP B OD2 1 
ATOM   4194 N N   . ILE B 1 247 ? -2.43000  -21.18000 -5.96200  1.000 43.69000 ? 249 ILE B N   1 
ATOM   4195 C CA  . ILE B 1 247 ? -2.97100  -19.87200 -6.33200  1.000 43.35000 ? 249 ILE B CA  1 
ATOM   4196 C C   . ILE B 1 247 ? -3.32800  -19.82500 -7.81600  1.000 41.79000 ? 249 ILE B C   1 
ATOM   4197 O O   . ILE B 1 247 ? -4.27300  -19.13500 -8.21400  1.000 44.36000 ? 249 ILE B O   1 
ATOM   4198 C CB  . ILE B 1 247 ? -1.96200  -18.76700 -5.95800  1.000 45.77000 ? 249 ILE B CB  1 
ATOM   4199 C CG1 . ILE B 1 247 ? -1.86300  -18.61500 -4.43800  1.000 48.52000 ? 249 ILE B CG1 1 
ATOM   4200 C CG2 . ILE B 1 247 ? -2.35100  -17.43700 -6.58200  1.000 46.75000 ? 249 ILE B CG2 1 
ATOM   4201 C CD1 . ILE B 1 247 ? -0.84300  -17.57400 -3.99700  1.000 48.66000 ? 249 ILE B CD1 1 
ATOM   4202 N N   . LEU B 1 248 ? -2.59100  -20.55100 -8.65300  1.000 41.16000 ? 250 LEU B N   1 
ATOM   4203 C CA  . LEU B 1 248 ? -2.91300  -20.63600 -10.07300 1.000 40.48000 ? 250 LEU B CA  1 
ATOM   4204 C C   . LEU B 1 248 ? -4.01400  -21.64400 -10.37400 1.000 42.87000 ? 250 LEU B C   1 
ATOM   4205 O O   . LEU B 1 248 ? -4.33800  -21.84900 -11.55200 1.000 43.82000 ? 250 LEU B O   1 
ATOM   4206 C CB  . LEU B 1 248 ? -1.66600  -21.00400 -10.87200 1.000 38.34000 ? 250 LEU B CB  1 
ATOM   4207 C CG  . LEU B 1 248 ? -0.61000  -19.90600 -10.96700 1.000 38.27000 ? 250 LEU B CG  1 
ATOM   4208 C CD1 . LEU B 1 248 ? 0.71800   -20.49600 -11.39100 1.000 32.48000 ? 250 LEU B CD1 1 
ATOM   4209 C CD2 . LEU B 1 248 ? -1.07400  -18.83600 -11.95000 1.000 31.44000 ? 250 LEU B CD2 1 
ATOM   4210 N N   . GLY B 1 249 ? -4.56800  -22.28800 -9.35000  1.000 44.98000 ? 251 GLY B N   1 
ATOM   4211 C CA  . GLY B 1 249 ? -5.64000  -23.24500 -9.50500  1.000 45.90000 ? 251 GLY B CA  1 
ATOM   4212 C C   . GLY B 1 249 ? -6.76500  -22.81200 -10.42700 1.000 46.16000 ? 251 GLY B C   1 
ATOM   4213 O O   . GLY B 1 249 ? -7.04200  -23.47300 -11.43400 1.000 47.99000 ? 251 GLY B O   1 
ATOM   4214 N N   . PRO B 1 250 ? -7.45200  -21.70600 -10.09700 1.000 43.94000 ? 252 PRO B N   1 
ATOM   4215 C CA  . PRO B 1 250 ? -8.59100  -21.27800 -10.93000 1.000 46.33000 ? 252 PRO B CA  1 
ATOM   4216 C C   . PRO B 1 250 ? -8.25800  -21.12000 -12.40200 1.000 48.20000 ? 252 PRO B C   1 
ATOM   4217 O O   . PRO B 1 250 ? -9.05800  -21.52400 -13.25500 1.000 48.59000 ? 252 PRO B O   1 
ATOM   4218 C CB  . PRO B 1 250 ? -9.01000  -19.94000 -10.29600 1.000 45.48000 ? 252 PRO B CB  1 
ATOM   4219 C CG  . PRO B 1 250 ? -7.92400  -19.58900 -9.32300  1.000 43.36000 ? 252 PRO B CG  1 
ATOM   4220 C CD  . PRO B 1 250 ? -7.33600  -20.88200 -8.88500  1.000 45.63000 ? 252 PRO B CD  1 
ATOM   4221 N N   . LEU B 1 251 ? -7.09300  -20.55100 -12.72700 1.000 45.58000 ? 253 LEU B N   1 
ATOM   4222 C CA  . LEU B 1 251 ? -6.71500  -20.38500 -14.12700 1.000 43.70000 ? 253 LEU B CA  1 
ATOM   4223 C C   . LEU B 1 251 ? -6.39300  -21.72000 -14.78300 1.000 45.55000 ? 253 LEU B C   1 
ATOM   4224 O O   . LEU B 1 251 ? -6.61800  -21.89200 -15.98800 1.000 44.41000 ? 253 LEU B O   1 
ATOM   4225 C CB  . LEU B 1 251 ? -5.51900  -19.43400 -14.23400 1.000 43.63000 ? 253 LEU B CB  1 
ATOM   4226 C CG  . LEU B 1 251 ? -5.77100  -18.01000 -13.73400 1.000 38.28000 ? 253 LEU B CG  1 
ATOM   4227 C CD1 . LEU B 1 251 ? -4.45700  -17.29600 -13.50200 1.000 38.10000 ? 253 LEU B CD1 1 
ATOM   4228 C CD2 . LEU B 1 251 ? -6.61300  -17.26000 -14.74400 1.000 40.37000 ? 253 LEU B CD2 1 
ATOM   4229 N N   . SER B 1 252 ? -5.86800  -22.67300 -14.01000 1.000 43.39000 ? 254 SER B N   1 
ATOM   4230 C CA  . SER B 1 252 ? -5.61900  -24.00100 -14.55200 1.000 46.29000 ? 254 SER B CA  1 
ATOM   4231 C C   . SER B 1 252 ? -6.92700  -24.70200 -14.89500 1.000 45.78000 ? 254 SER B C   1 
ATOM   4232 O O   . SER B 1 252 ? -7.02300  -25.37500 -15.92600 1.000 44.90000 ? 254 SER B O   1 
ATOM   4233 C CB  . SER B 1 252 ? -4.80600  -24.83000 -13.55700 1.000 46.26000 ? 254 SER B CB  1 
ATOM   4234 O OG  . SER B 1 252 ? -4.71400  -26.18000 -13.98500 1.000 46.80000 ? 254 SER B OG  1 
ATOM   4235 N N   . ALA B 1 253 ? -7.94500  -24.54800 -14.04400 1.000 46.72000 ? 255 ALA B N   1 
ATOM   4236 C CA  . ALA B 1 253 ? -9.24000  -25.16300 -14.31900 1.000 48.84000 ? 255 ALA B CA  1 
ATOM   4237 C C   . ALA B 1 253 ? -9.92800  -24.49700 -15.50500 1.000 52.23000 ? 255 ALA B C   1 
ATOM   4238 O O   . ALA B 1 253 ? -10.51400 -25.18000 -16.35500 1.000 50.92000 ? 255 ALA B O   1 
ATOM   4239 C CB  . ALA B 1 253 ? -10.12600 -25.09300 -13.07400 1.000 48.92000 ? 255 ALA B CB  1 
ATOM   4240 N N   . GLN B 1 254 ? -9.86200  -23.16400 -15.58000 1.000 52.80000 ? 256 GLN B N   1 
ATOM   4241 C CA  . GLN B 1 254 ? -10.57700 -22.43900 -16.62800 1.000 51.51000 ? 256 GLN B CA  1 
ATOM   4242 C C   . GLN B 1 254 ? -9.99600  -22.73900 -18.00500 1.000 49.44000 ? 256 GLN B C   1 
ATOM   4243 O O   . GLN B 1 254 ? -10.74100 -22.93600 -18.97100 1.000 50.85000 ? 256 GLN B O   1 
ATOM   4244 C CB  . GLN B 1 254 ? -10.54800 -20.94200 -16.33100 1.000 51.68000 ? 256 GLN B CB  1 
ATOM   4245 C CG  . GLN B 1 254 ? -11.24300 -20.07400 -17.36800 1.000 51.35000 ? 256 GLN B CG  1 
ATOM   4246 C CD  . GLN B 1 254 ? -10.91100 -18.60700 -17.18900 1.000 50.80000 ? 256 GLN B CD  1 
ATOM   4247 O OE1 . GLN B 1 254 ? -10.54900 -18.17500 -16.09300 1.000 53.49000 ? 256 GLN B OE1 1 
ATOM   4248 N NE2 . GLN B 1 254 ? -11.01400 -17.83500 -18.26800 1.000 45.80000 ? 256 GLN B NE2 1 
ATOM   4249 N N   . THR B 1 255 ? -8.67800  -22.77700 -18.12100 1.000 48.94000 ? 257 THR B N   1 
ATOM   4250 C CA  . THR B 1 255 ? -8.06200  -23.32200 -19.31700 1.000 47.33000 ? 257 THR B CA  1 
ATOM   4251 C C   . THR B 1 255 ? -7.95600  -24.83600 -19.14600 1.000 50.18000 ? 257 THR B C   1 
ATOM   4252 O O   . THR B 1 255 ? -8.38800  -25.40200 -18.14200 1.000 53.16000 ? 257 THR B O   1 
ATOM   4253 C CB  . THR B 1 255 ? -6.69600  -22.67700 -19.56900 1.000 47.06000 ? 257 THR B CB  1 
ATOM   4254 O OG1 . THR B 1 255 ? -5.69900  -23.31500 -18.75900 1.000 45.98000 ? 257 THR B OG1 1 
ATOM   4255 C CG2 . THR B 1 255 ? -6.73500  -21.19400 -19.23400 1.000 43.17000 ? 257 THR B CG2 1 
ATOM   4256 N N   . GLY B 1 256 ? -7.39500  -25.51400 -20.13400 1.000 45.34000 ? 258 GLY B N   1 
ATOM   4257 C CA  . GLY B 1 256 ? -7.17000  -26.93400 -19.94900 1.000 49.28000 ? 258 GLY B CA  1 
ATOM   4258 C C   . GLY B 1 256 ? -5.73100  -27.23100 -19.57600 1.000 49.08000 ? 258 GLY B C   1 
ATOM   4259 O O   . GLY B 1 256 ? -5.24900  -28.34800 -19.79600 1.000 44.92000 ? 258 GLY B O   1 
ATOM   4260 N N   . ILE B 1 257 ? -5.04800  -26.24300 -18.99200 1.000 43.46000 ? 259 ILE B N   1 
ATOM   4261 C CA  . ILE B 1 257 ? -3.60100  -26.26400 -18.80300 1.000 47.92000 ? 259 ILE B CA  1 
ATOM   4262 C C   . ILE B 1 257 ? -3.30400  -26.34300 -17.31000 1.000 49.04000 ? 259 ILE B C   1 
ATOM   4263 O O   . ILE B 1 257 ? -3.55400  -25.38300 -16.56900 1.000 48.35000 ? 259 ILE B O   1 
ATOM   4264 C CB  . ILE B 1 257 ? -2.93200  -25.02800 -19.42200 1.000 44.76000 ? 259 ILE B CB  1 
ATOM   4265 C CG1 . ILE B 1 257 ? -3.56300  -24.68000 -20.77200 1.000 48.67000 ? 259 ILE B CG1 1 
ATOM   4266 C CG2 . ILE B 1 257 ? -1.43500  -25.25600 -19.57200 1.000 45.62000 ? 259 ILE B CG2 1 
ATOM   4267 C CD1 . ILE B 1 257 ? -3.28900  -25.70400 -21.84300 1.000 46.71000 ? 259 ILE B CD1 1 
ATOM   4268 N N   . ALA B 1 258 ? -2.75700  -27.47100 -16.86700 1.000 45.63000 ? 260 ALA B N   1 
ATOM   4269 C CA  . ALA B 1 258 ? -2.29200  -27.57800 -15.49200 1.000 46.01000 ? 260 ALA B CA  1 
ATOM   4270 C C   . ALA B 1 258 ? -0.99900  -26.79000 -15.31600 1.000 44.35000 ? 260 ALA B C   1 
ATOM   4271 O O   . ALA B 1 258 ? -0.21500  -26.62900 -16.25700 1.000 43.72000 ? 260 ALA B O   1 
ATOM   4272 C CB  . ALA B 1 258 ? -2.07500  -29.03900 -15.10500 1.000 45.26000 ? 260 ALA B CB  1 
ATOM   4273 N N   . VAL B 1 259 ? -0.77400  -26.30800 -14.09000 1.000 45.03000 ? 261 VAL B N   1 
ATOM   4274 C CA  . VAL B 1 259 ? 0.35200   -25.40800 -13.83700 1.000 43.54000 ? 261 VAL B CA  1 
ATOM   4275 C C   . VAL B 1 259 ? 1.65700   -26.02200 -14.32500 1.000 41.45000 ? 261 VAL B C   1 
ATOM   4276 O O   . VAL B 1 259 ? 2.44700   -25.36700 -15.01400 1.000 42.30000 ? 261 VAL B O   1 
ATOM   4277 C CB  . VAL B 1 259 ? 0.41700   -25.03900 -12.34400 1.000 40.50000 ? 261 VAL B CB  1 
ATOM   4278 C CG1 . VAL B 1 259 ? 1.66700   -24.21200 -12.06300 1.000 43.07000 ? 261 VAL B CG1 1 
ATOM   4279 C CG2 . VAL B 1 259 ? -0.82600  -24.29400 -11.94800 1.000 40.40000 ? 261 VAL B CG2 1 
ATOM   4280 N N   . LEU B 1 260 ? 1.89000   -27.30100 -14.01400 1.000 43.87000 ? 262 LEU B N   1 
ATOM   4281 C CA  . LEU B 1 260 ? 3.12100   -27.94900 -14.45600 1.000 42.35000 ? 262 LEU B CA  1 
ATOM   4282 C C   . LEU B 1 260 ? 3.12600   -28.24100 -15.95600 1.000 43.10000 ? 262 LEU B C   1 
ATOM   4283 O O   . LEU B 1 260 ? 4.20600   -28.40200 -16.54000 1.000 42.14000 ? 262 LEU B O   1 
ATOM   4284 C CB  . LEU B 1 260 ? 3.34400   -29.22900 -13.65000 1.000 43.01000 ? 262 LEU B CB  1 
ATOM   4285 C CG  . LEU B 1 260 ? 3.62900   -28.95300 -12.17100 1.000 41.58000 ? 262 LEU B CG  1 
ATOM   4286 C CD1 . LEU B 1 260 ? 2.88100   -29.93500 -11.27400 1.000 46.09000 ? 262 LEU B CD1 1 
ATOM   4287 C CD2 . LEU B 1 260 ? 5.12700   -28.98700 -11.89000 1.000 41.58000 ? 262 LEU B CD2 1 
ATOM   4288 N N   . ASP B 1 261 ? 1.95400   -28.32000 -16.59200 1.000 44.56000 ? 263 ASP B N   1 
ATOM   4289 C CA  . ASP B 1 261 ? 1.91300   -28.32400 -18.05400 1.000 45.71000 ? 263 ASP B CA  1 
ATOM   4290 C C   . ASP B 1 261 ? 2.32400   -26.96100 -18.60300 1.000 41.09000 ? 263 ASP B C   1 
ATOM   4291 O O   . ASP B 1 261 ? 3.06600   -26.87900 -19.58800 1.000 43.08000 ? 263 ASP B O   1 
ATOM   4292 C CB  . ASP B 1 261 ? 0.51000   -28.73800 -18.52400 1.000 45.36000 ? 263 ASP B CB  1 
ATOM   4293 C CG  . ASP B 1 261 ? 0.29700   -28.60000 -20.04600 1.000 46.55000 ? 263 ASP B CG  1 
ATOM   4294 O OD1 . ASP B 1 261 ? 1.25000   -28.72600 -20.85400 1.000 48.83000 ? 263 ASP B OD1 1 
ATOM   4295 O OD2 . ASP B 1 261 ? -0.86700  -28.37600 -20.43000 1.000 54.14000 ? 263 ASP B OD2 1 
ATOM   4296 N N   . MET B 1 262 ? 1.88400   -25.87900 -17.95200 1.000 42.98000 ? 264 MET B N   1 
ATOM   4297 C CA  . MET B 1 262 ? 2.30400   -24.54100 -18.36400 1.000 40.64000 ? 264 MET B CA  1 
ATOM   4298 C C   . MET B 1 262 ? 3.78200   -24.30400 -18.05600 1.000 41.64000 ? 264 MET B C   1 
ATOM   4299 O O   . MET B 1 262 ? 4.47400   -23.62100 -18.81900 1.000 38.76000 ? 264 MET B O   1 
ATOM   4300 C CB  . MET B 1 262 ? 1.41600   -23.48800 -17.69100 1.000 39.74000 ? 264 MET B CB  1 
ATOM   4301 C CG  . MET B 1 262 ? 1.56000   -22.06700 -18.24600 1.000 40.19000 ? 264 MET B CG  1 
ATOM   4302 S SD  . MET B 1 262 ? 0.92400   -21.83600 -19.93200 1.000 38.08000 ? 264 MET B SD  1 
ATOM   4303 C CE  . MET B 1 262 ? -0.74500  -21.33400 -19.57300 1.000 36.40000 ? 264 MET B CE  1 
ATOM   4304 N N   . CYS B 1 263 ? 4.29300   -24.86900 -16.95300 1.000 40.57000 ? 265 CYS B N   1 
ATOM   4305 C CA  . CYS B 1 263 ? 5.72800   -24.78100 -16.68500 1.000 44.15000 ? 265 CYS B CA  1 
ATOM   4306 C C   . CYS B 1 263 ? 6.53100   -25.41200 -17.81000 1.000 38.91000 ? 265 CYS B C   1 
ATOM   4307 O O   . CYS B 1 263 ? 7.59800   -24.90800 -18.17700 1.000 43.16000 ? 265 CYS B O   1 
ATOM   4308 C CB  . CYS B 1 263 ? 6.07100   -25.44800 -15.35600 1.000 45.23000 ? 265 CYS B CB  1 
ATOM   4309 S SG  . CYS B 1 263 ? 5.40800   -24.63200 -13.90400 1.000 43.31000 ? 265 CYS B SG  1 
ATOM   4310 N N   . ALA B 1 264 ? 6.02000   -26.50700 -18.38400 1.000 43.89000 ? 266 ALA B N   1 
ATOM   4311 C CA  . ALA B 1 264 ? 6.66600   -27.09500 -19.55200 1.000 41.15000 ? 266 ALA B CA  1 
ATOM   4312 C C   . ALA B 1 264 ? 6.72200   -26.09900 -20.70400 1.000 39.23000 ? 266 ALA B C   1 
ATOM   4313 O O   . ALA B 1 264 ? 7.74300   -25.99600 -21.39200 1.000 41.48000 ? 266 ALA B O   1 
ATOM   4314 C CB  . ALA B 1 264 ? 5.93900   -28.37400 -19.97300 1.000 41.18000 ? 266 ALA B CB  1 
ATOM   4315 N N   . SER B 1 265 ? 5.64100   -25.34100 -20.91500 1.000 41.84000 ? 267 SER B N   1 
ATOM   4316 C CA  . SER B 1 265 ? 5.67100   -24.26200 -21.90400 1.000 43.43000 ? 267 SER B CA  1 
ATOM   4317 C C   . SER B 1 265 ? 6.72300   -23.21700 -21.54700 1.000 41.51000 ? 267 SER B C   1 
ATOM   4318 O O   . SER B 1 265 ? 7.53700   -22.82500 -22.39200 1.000 35.94000 ? 267 SER B O   1 
ATOM   4319 C CB  . SER B 1 265 ? 4.29000   -23.60600 -22.02200 1.000 39.05000 ? 267 SER B CB  1 
ATOM   4320 O OG  . SER B 1 265 ? 3.33200   -24.47500 -22.60400 1.000 41.87000 ? 267 SER B OG  1 
ATOM   4321 N N   . LEU B 1 266 ? 6.71700   -22.74900 -20.29000 1.000 41.48000 ? 268 LEU B N   1 
ATOM   4322 C CA  . LEU B 1 266 ? 7.66100   -21.70800 -19.87400 1.000 38.09000 ? 268 LEU B CA  1 
ATOM   4323 C C   . LEU B 1 266 ? 9.10400   -22.19700 -19.93500 1.000 39.92000 ? 268 LEU B C   1 
ATOM   4324 O O   . LEU B 1 266 ? 10.00000  -21.45200 -20.34300 1.000 39.30000 ? 268 LEU B O   1 
ATOM   4325 C CB  . LEU B 1 266 ? 7.32100   -21.21300 -18.46100 1.000 39.57000 ? 268 LEU B CB  1 
ATOM   4326 C CG  . LEU B 1 266 ? 8.25300   -20.15200 -17.84700 1.000 33.52000 ? 268 LEU B CG  1 
ATOM   4327 C CD1 . LEU B 1 266 ? 8.34900   -18.92500 -18.73000 1.000 35.32000 ? 268 LEU B CD1 1 
ATOM   4328 C CD2 . LEU B 1 266 ? 7.81200   -19.75200 -16.44900 1.000 34.24000 ? 268 LEU B CD2 1 
ATOM   4329 N N   . LYS B 1 267 ? 9.35200   -23.44300 -19.52200 1.000 42.84000 ? 269 LYS B N   1 
ATOM   4330 C CA  . LYS B 1 267 ? 10.68700  -24.01400 -19.67200 1.000 45.56000 ? 269 LYS B CA  1 
ATOM   4331 C C   . LYS B 1 267 ? 11.17200  -23.87600 -21.11200 1.000 43.86000 ? 269 LYS B C   1 
ATOM   4332 O O   . LYS B 1 267 ? 12.27700  -23.38800 -21.36400 1.000 45.06000 ? 269 LYS B O   1 
ATOM   4333 C CB  . LYS B 1 267 ? 10.66800  -25.47800 -19.23200 1.000 48.75000 ? 269 LYS B CB  1 
ATOM   4334 C CG  . LYS B 1 267 ? 12.02200  -26.14800 -19.20700 1.000 52.84000 ? 269 LYS B CG  1 
ATOM   4335 C CD  . LYS B 1 267 ? 12.08200  -27.17900 -18.08600 1.000 55.22000 ? 269 LYS B CD  1 
ATOM   4336 C CE  . LYS B 1 267 ? 11.51000  -28.52400 -18.51600 1.000 57.69000 ? 269 LYS B CE  1 
ATOM   4337 N NZ  . LYS B 1 267 ? 12.25700  -29.64400 -17.86700 1.000 56.12000 ? 269 LYS B NZ  1 
ATOM   4338 N N   . GLU B 1 268 ? 10.31900  -24.24300 -22.07500 1.000 47.26000 ? 270 GLU B N   1 
ATOM   4339 C CA  . GLU B 1 268 ? 10.69700  -24.15200 -23.48400 1.000 46.59000 ? 270 GLU B CA  1 
ATOM   4340 C C   . GLU B 1 268 ? 11.00300  -22.71500 -23.88600 1.000 46.58000 ? 270 GLU B C   1 
ATOM   4341 O O   . GLU B 1 268 ? 12.01200  -22.45100 -24.55500 1.000 48.42000 ? 270 GLU B O   1 
ATOM   4342 C CB  . GLU B 1 268 ? 9.58600   -24.73000 -24.36700 1.000 47.60000 ? 270 GLU B CB  1 
ATOM   4343 C CG  . GLU B 1 268 ? 9.23800   -26.18800 -24.07100 1.000 50.27000 ? 270 GLU B CG  1 
ATOM   4344 C CD  . GLU B 1 268 ? 10.45700  -27.11400 -24.07200 1.000 56.11000 ? 270 GLU B CD  1 
ATOM   4345 O OE1 . GLU B 1 268 ? 11.31700  -26.97400 -24.97600 1.000 52.71000 ? 270 GLU B OE1 1 
ATOM   4346 O OE2 . GLU B 1 268 ? 10.55300  -27.97600 -23.16200 1.000 54.25000 ? 270 GLU B OE2 1 
ATOM   4347 N N   . LEU B 1 269 ? 10.15000  -21.76900 -23.47100 1.000 43.48000 ? 271 LEU B N   1 
ATOM   4348 C CA  . LEU B 1 269 ? 10.38400  -20.36600 -23.80000 1.000 43.92000 ? 271 LEU B CA  1 
ATOM   4349 C C   . LEU B 1 269 ? 11.69900  -19.85600 -23.21700 1.000 43.81000 ? 271 LEU B C   1 
ATOM   4350 O O   . LEU B 1 269 ? 12.35000  -18.99400 -23.81700 1.000 44.80000 ? 271 LEU B O   1 
ATOM   4351 C CB  . LEU B 1 269 ? 9.21600   -19.51000 -23.29700 1.000 39.21000 ? 271 LEU B CB  1 
ATOM   4352 C CG  . LEU B 1 269 ? 7.86500   -19.72200 -23.98000 1.000 41.61000 ? 271 LEU B CG  1 
ATOM   4353 C CD1 . LEU B 1 269 ? 6.72100   -19.15400 -23.13700 1.000 37.18000 ? 271 LEU B CD1 1 
ATOM   4354 C CD2 . LEU B 1 269 ? 7.86800   -19.10000 -25.36700 1.000 43.25000 ? 271 LEU B CD2 1 
ATOM   4355 N N   . LEU B 1 270 ? 12.10700  -20.36800 -22.05200 1.000 43.09000 ? 272 LEU B N   1 
ATOM   4356 C CA  . LEU B 1 270 ? 13.27700  -19.81300 -21.37900 1.000 44.15000 ? 272 LEU B CA  1 
ATOM   4357 C C   . LEU B 1 270 ? 14.57200  -20.12700 -22.12500 1.000 46.73000 ? 272 LEU B C   1 
ATOM   4358 O O   . LEU B 1 270 ? 15.51100  -19.32400 -22.09800 1.000 50.41000 ? 272 LEU B O   1 
ATOM   4359 C CB  . LEU B 1 270 ? 13.34000  -20.32300 -19.93500 1.000 44.63000 ? 272 LEU B CB  1 
ATOM   4360 C CG  . LEU B 1 270 ? 12.35200  -19.62000 -18.98800 1.000 40.59000 ? 272 LEU B CG  1 
ATOM   4361 C CD1 . LEU B 1 270 ? 12.33000  -20.23300 -17.59000 1.000 37.45000 ? 272 LEU B CD1 1 
ATOM   4362 C CD2 . LEU B 1 270 ? 12.65900  -18.13600 -18.92100 1.000 38.72000 ? 272 LEU B CD2 1 
ATOM   4363 N N   . GLN B 1 271 ? 14.63800  -21.26300 -22.81600 1.000 50.43000 ? 273 GLN B N   1 
ATOM   4364 C CA  . GLN B 1 271 ? 15.84300  -21.64000 -23.55100 1.000 53.33000 ? 273 GLN B CA  1 
ATOM   4365 C C   . GLN B 1 271 ? 15.76900  -21.26000 -25.02700 1.000 55.28000 ? 273 GLN B C   1 
ATOM   4366 O O   . GLN B 1 271 ? 16.63200  -20.53200 -25.53000 1.000 60.44000 ? 273 GLN B O   1 
ATOM   4367 C CB  . GLN B 1 271 ? 16.09100  -23.14100 -23.40200 1.000 51.36000 ? 273 GLN B CB  1 
ATOM   4368 C CG  . GLN B 1 271 ? 15.79700  -23.65600 -22.01200 1.000 52.29000 ? 273 GLN B CG  1 
ATOM   4369 C CD  . GLN B 1 271 ? 15.53300  -25.13600 -22.00100 1.000 54.85000 ? 273 GLN B CD  1 
ATOM   4370 O OE1 . GLN B 1 271 ? 14.57600  -25.60800 -21.39000 1.000 55.52000 ? 273 GLN B OE1 1 
ATOM   4371 N NE2 . GLN B 1 271 ? 16.38500  -25.88700 -22.69100 1.000 60.76000 ? 273 GLN B NE2 1 
ATOM   4372 N N   . ASN B 1 272 ? 14.75200  -21.75100 -25.73200 1.000 51.30000 ? 274 ASN B N   1 
ATOM   4373 C CA  . ASN B 1 272 ? 14.63000  -21.53200 -27.16700 1.000 52.21000 ? 274 ASN B CA  1 
ATOM   4374 C C   . ASN B 1 272 ? 14.14000  -20.13600 -27.51500 1.000 53.65000 ? 274 ASN B C   1 
ATOM   4375 O O   . ASN B 1 272 ? 14.14300  -19.77300 -28.69800 1.000 54.23000 ? 274 ASN B O   1 
ATOM   4376 C CB  . ASN B 1 272 ? 13.68500  -22.57700 -27.76800 1.000 53.10000 ? 274 ASN B CB  1 
ATOM   4377 C CG  . ASN B 1 272 ? 13.95400  -23.97000 -27.23900 1.000 53.30000 ? 274 ASN B CG  1 
ATOM   4378 O OD1 . ASN B 1 272 ? 15.10700  -24.37600 -27.10400 1.000 58.39000 ? 274 ASN B OD1 1 
ATOM   4379 N ND2 . ASN B 1 272 ? 12.89400  -24.70400 -26.92300 1.000 52.74000 ? 274 ASN B ND2 1 
ATOM   4380 N N   . GLY B 1 273 ? 13.72500  -19.34800 -26.52600 1.000 52.33000 ? 275 GLY B N   1 
ATOM   4381 C CA  . GLY B 1 273 ? 13.17100  -18.04600 -26.81200 1.000 50.94000 ? 275 GLY B CA  1 
ATOM   4382 C C   . GLY B 1 273 ? 11.76200  -18.16100 -27.36500 1.000 49.41000 ? 275 GLY B C   1 
ATOM   4383 O O   . GLY B 1 273 ? 11.07900  -19.18100 -27.22000 1.000 47.90000 ? 275 GLY B O   1 
ATOM   4384 N N   . MET B 1 274 ? 11.32800  -17.08500 -28.01700 1.000 53.04000 ? 276 MET B N   1 
ATOM   4385 C CA  . MET B 1 274 ? 10.00500  -17.01700 -28.61900 1.000 51.74000 ? 276 MET B CA  1 
ATOM   4386 C C   . MET B 1 274 ? 10.02400  -17.25600 -30.12100 1.000 53.92000 ? 276 MET B C   1 
ATOM   4387 O O   . MET B 1 274 ? 8.95900   -17.24100 -30.74800 1.000 51.10000 ? 276 MET B O   1 
ATOM   4388 C CB  . MET B 1 274 ? 9.35700   -15.66200 -28.31800 1.000 50.95000 ? 276 MET B CB  1 
ATOM   4389 C CG  . MET B 1 274 ? 8.77100   -15.55900 -26.92600 1.000 50.80000 ? 276 MET B CG  1 
ATOM   4390 S SD  . MET B 1 274 ? 7.75800   -14.08600 -26.70200 1.000 53.88000 ? 276 MET B SD  1 
ATOM   4391 C CE  . MET B 1 274 ? 8.30000   -13.63200 -25.05800 1.000 44.65000 ? 276 MET B CE  1 
ATOM   4392 N N   . ASN B 1 275 ? 11.20500  -17.47200 -30.70600 1.000 53.02000 ? 277 ASN B N   1 
ATOM   4393 C CA  . ASN B 1 275 ? 11.35400  -17.77600 -32.13000 1.000 55.32000 ? 277 ASN B CA  1 
ATOM   4394 C C   . ASN B 1 275 ? 10.61800  -16.75600 -33.00000 1.000 52.25000 ? 277 ASN B C   1 
ATOM   4395 O O   . ASN B 1 275 ? 9.87400   -17.10300 -33.91900 1.000 54.94000 ? 277 ASN B O   1 
ATOM   4396 C CB  . ASN B 1 275 ? 10.88500  -19.20100 -32.43100 1.000 56.94000 ? 277 ASN B CB  1 
ATOM   4397 C CG  . ASN B 1 275 ? 11.68800  -20.24600 -31.67700 1.000 60.25000 ? 277 ASN B CG  1 
ATOM   4398 O OD1 . ASN B 1 275 ? 12.88400  -20.41800 -31.92000 1.000 62.54000 ? 277 ASN B OD1 1 
ATOM   4399 N ND2 . ASN B 1 275 ? 11.03600  -20.94000 -30.74100 1.000 60.95000 ? 277 ASN B ND2 1 
ATOM   4400 N N   . GLY B 1 276 ? 10.83500  -15.47700 -32.69100 1.000 49.89000 ? 278 GLY B N   1 
ATOM   4401 C CA  . GLY B 1 276 ? 10.24700  -14.38400 -33.43200 1.000 52.05000 ? 278 GLY B CA  1 
ATOM   4402 C C   . GLY B 1 276 ? 8.81400   -14.07000 -33.08400 1.000 52.92000 ? 278 GLY B C   1 
ATOM   4403 O O   . GLY B 1 276 ? 8.31000   -13.01800 -33.50200 1.000 54.49000 ? 278 GLY B O   1 
ATOM   4404 N N   . ARG B 1 277 ? 8.14200   -14.93200 -32.32500 1.000 52.51000 ? 279 ARG B N   1 
ATOM   4405 C CA  . ARG B 1 277 ? 6.72500   -14.75900 -32.05600 1.000 48.77000 ? 279 ARG B CA  1 
ATOM   4406 C C   . ARG B 1 277 ? 6.50800   -13.80300 -30.87800 1.000 47.41000 ? 279 ARG B C   1 
ATOM   4407 O O   . ARG B 1 277 ? 7.44400   -13.36500 -30.20200 1.000 47.90000 ? 279 ARG B O   1 
ATOM   4408 C CB  . ARG B 1 277 ? 6.06400   -16.11500 -31.79700 1.000 48.41000 ? 279 ARG B CB  1 
ATOM   4409 C CG  . ARG B 1 277 ? 5.63200   -16.83900 -33.07200 1.000 51.47000 ? 279 ARG B CG  1 
ATOM   4410 C CD  . ARG B 1 277 ? 5.58700   -18.35300 -32.90000 1.000 50.67000 ? 279 ARG B CD  1 
ATOM   4411 N NE  . ARG B 1 277 ? 6.79800   -18.86900 -32.26600 1.000 55.38000 ? 279 ARG B NE  1 
ATOM   4412 C CZ  . ARG B 1 277 ? 7.00900   -20.15300 -31.97700 1.000 55.50000 ? 279 ARG B CZ  1 
ATOM   4413 N NH1 . ARG B 1 277 ? 6.08700   -21.06600 -32.26300 1.000 55.40000 ? 279 ARG B NH1 1 
ATOM   4414 N NH2 . ARG B 1 277 ? 8.13600   -20.52600 -31.38700 1.000 58.43000 ? 279 ARG B NH2 1 
ATOM   4415 N N   . THR B 1 278 ? 5.24500   -13.47100 -30.65000 1.000 46.18000 ? 280 THR B N   1 
ATOM   4416 C CA  . THR B 1 278 ? 4.84000   -12.48700 -29.66100 1.000 44.03000 ? 280 THR B CA  1 
ATOM   4417 C C   . THR B 1 278 ? 3.76300   -13.10600 -28.77400 1.000 44.20000 ? 280 THR B C   1 
ATOM   4418 O O   . THR B 1 278 ? 2.97600   -13.94500 -29.22700 1.000 38.70000 ? 280 THR B O   1 
ATOM   4419 C CB  . THR B 1 278 ? 4.33100   -11.19600 -30.37500 1.000 44.37000 ? 280 THR B CB  1 
ATOM   4420 O OG1 . THR B 1 278 ? 5.08800   -10.05700 -29.94400 1.000 44.64000 ? 280 THR B OG1 1 
ATOM   4421 C CG2 . THR B 1 278 ? 2.86300   -10.95000 -30.12300 1.000 44.00000 ? 280 THR B CG2 1 
ATOM   4422 N N   . ILE B 1 279 ? 3.74500   -12.71300 -27.49800 1.000 38.58000 ? 281 ILE B N   1 
ATOM   4423 C CA  . ILE B 1 279 ? 2.71800   -13.15600 -26.55600 1.000 39.47000 ? 281 ILE B CA  1 
ATOM   4424 C C   . ILE B 1 279 ? 2.03100   -11.92400 -25.99200 1.000 38.94000 ? 281 ILE B C   1 
ATOM   4425 O O   . ILE B 1 279 ? 2.67100   -11.10400 -25.32600 1.000 42.53000 ? 281 ILE B O   1 
ATOM   4426 C CB  . ILE B 1 279 ? 3.29400   -14.01300 -25.41700 1.000 36.60000 ? 281 ILE B CB  1 
ATOM   4427 C CG1 . ILE B 1 279 ? 4.13500   -15.16100 -25.96500 1.000 40.93000 ? 281 ILE B CG1 1 
ATOM   4428 C CG2 . ILE B 1 279 ? 2.16100   -14.53600 -24.52300 1.000 37.87000 ? 281 ILE B CG2 1 
ATOM   4429 C CD1 . ILE B 1 279 ? 4.46500   -16.20400 -24.93500 1.000 38.65000 ? 281 ILE B CD1 1 
ATOM   4430 N N   . LEU B 1 280 ? 0.72900   -11.80500 -26.24200 1.000 35.90000 ? 282 LEU B N   1 
ATOM   4431 C CA  . LEU B 1 280 ? -0.04500  -10.63800 -25.81800 1.000 39.46000 ? 282 LEU B CA  1 
ATOM   4432 C C   . LEU B 1 280 ? 0.67100   -9.33400  -26.17700 1.000 35.51000 ? 282 LEU B C   1 
ATOM   4433 O O   . LEU B 1 280 ? 0.74400   -8.39600  -25.38000 1.000 37.45000 ? 282 LEU B O   1 
ATOM   4434 C CB  . LEU B 1 280 ? -0.35500  -10.70000 -24.32200 1.000 38.76000 ? 282 LEU B CB  1 
ATOM   4435 C CG  . LEU B 1 280 ? -1.52500  -11.60200 -23.90600 1.000 38.67000 ? 282 LEU B CG  1 
ATOM   4436 C CD1 . LEU B 1 280 ? -1.60400  -11.72500 -22.39300 1.000 38.57000 ? 282 LEU B CD1 1 
ATOM   4437 C CD2 . LEU B 1 280 ? -2.86600  -11.11700 -24.48000 1.000 37.83000 ? 282 LEU B CD2 1 
ATOM   4438 N N   . GLY B 1 281 ? 1.21400   -9.27700  -27.38900 1.000 35.43000 ? 283 GLY B N   1 
ATOM   4439 C CA  . GLY B 1 281 ? 1.82700   -8.04800  -27.85400 1.000 38.10000 ? 283 GLY B CA  1 
ATOM   4440 C C   . GLY B 1 281 ? 3.15500   -7.71500  -27.21700 1.000 41.42000 ? 283 GLY B C   1 
ATOM   4441 O O   . GLY B 1 281 ? 3.59100   -6.56000  -27.27400 1.000 43.95000 ? 283 GLY B O   1 
ATOM   4442 N N   . SER B 1 282 ? 3.81700   -8.69300  -26.61100 1.000 38.29000 ? 284 SER B N   1 
ATOM   4443 C CA  . SER B 1 282 ? 5.09300   -8.46500  -25.95500 1.000 38.84000 ? 284 SER B CA  1 
ATOM   4444 C C   . SER B 1 282 ? 6.12300   -9.43800  -26.50100 1.000 36.45000 ? 284 SER B C   1 
ATOM   4445 O O   . SER B 1 282 ? 5.81100   -10.60500 -26.75600 1.000 37.51000 ? 284 SER B O   1 
ATOM   4446 C CB  . SER B 1 282 ? 4.97300   -8.62900  -24.43100 1.000 36.44000 ? 284 SER B CB  1 
ATOM   4447 O OG  . SER B 1 282 ? 6.23500   -8.49200  -23.79700 1.000 40.17000 ? 284 SER B OG  1 
ATOM   4448 N N   . ALA B 1 283 ? 7.35100   -8.95400  -26.67700 1.000 36.95000 ? 285 ALA B N   1 
ATOM   4449 C CA  . ALA B 1 283 ? 8.46500   -9.82300  -27.02200 1.000 37.38000 ? 285 ALA B CA  1 
ATOM   4450 C C   . ALA B 1 283 ? 9.20400   -10.33600 -25.79200 1.000 40.59000 ? 285 ALA B C   1 
ATOM   4451 O O   . ALA B 1 283 ? 10.10900  -11.16700 -25.93100 1.000 40.87000 ? 285 ALA B O   1 
ATOM   4452 C CB  . ALA B 1 283 ? 9.43900   -9.09100  -27.95300 1.000 42.78000 ? 285 ALA B CB  1 
ATOM   4453 N N   . LEU B 1 284 ? 8.84300   -9.86100  -24.60100 1.000 34.38000 ? 286 LEU B N   1 
ATOM   4454 C CA  . LEU B 1 284 ? 9.41300   -10.29300 -23.33300 1.000 36.47000 ? 286 LEU B CA  1 
ATOM   4455 C C   . LEU B 1 284 ? 8.37300   -11.05700 -22.51900 1.000 35.85000 ? 286 LEU B C   1 
ATOM   4456 O O   . LEU B 1 284 ? 7.16900   -10.95100 -22.75900 1.000 31.52000 ? 286 LEU B O   1 
ATOM   4457 C CB  . LEU B 1 284 ? 9.91100   -9.08800  -22.52600 1.000 38.95000 ? 286 LEU B CB  1 
ATOM   4458 C CG  . LEU B 1 284 ? 11.09900  -8.32500  -23.10600 1.000 39.55000 ? 286 LEU B CG  1 
ATOM   4459 C CD1 . LEU B 1 284 ? 11.38000  -7.06700  -22.28400 1.000 42.68000 ? 286 LEU B CD1 1 
ATOM   4460 C CD2 . LEU B 1 284 ? 12.33400  -9.21500  -23.17600 1.000 43.29000 ? 286 LEU B CD2 1 
ATOM   4461 N N   . LEU B 1 285 ? 8.84200   -11.84200 -21.54700 1.000 30.66000 ? 287 LEU B N   1 
ATOM   4462 C CA  . LEU B 1 285 ? 7.91600   -12.50900 -20.63600 1.000 33.64000 ? 287 LEU B CA  1 
ATOM   4463 C C   . LEU B 1 285 ? 7.56300   -11.54800 -19.50500 1.000 30.97000 ? 287 LEU B C   1 
ATOM   4464 O O   . LEU B 1 285 ? 8.43200   -11.13000 -18.73400 1.000 33.88000 ? 287 LEU B O   1 
ATOM   4465 C CB  . LEU B 1 285 ? 8.51200   -13.80900 -20.10300 1.000 33.52000 ? 287 LEU B CB  1 
ATOM   4466 C CG  . LEU B 1 285 ? 8.80800   -14.84800 -21.19200 1.000 32.70000 ? 287 LEU B CG  1 
ATOM   4467 C CD1 . LEU B 1 285 ? 9.56800   -16.04700 -20.63400 1.000 36.18000 ? 287 LEU B CD1 1 
ATOM   4468 C CD2 . LEU B 1 285 ? 7.51700   -15.28600 -21.83800 1.000 33.86000 ? 287 LEU B CD2 1 
ATOM   4469 N N   . GLU B 1 286 ? 6.29200   -11.19000 -19.41900 1.000 28.40000 ? 288 GLU B N   1 
ATOM   4470 C CA  . GLU B 1 286 ? 5.85300   -10.14000 -18.51000 1.000 30.49000 ? 288 GLU B CA  1 
ATOM   4471 C C   . GLU B 1 286 ? 5.61200   -10.70800 -17.11200 1.000 31.26000 ? 288 GLU B C   1 
ATOM   4472 O O   . GLU B 1 286 ? 4.94200   -11.73400 -16.96600 1.000 29.61000 ? 288 GLU B O   1 
ATOM   4473 C CB  . GLU B 1 286 ? 4.58100   -9.50900  -19.07500 1.000 33.27000 ? 288 GLU B CB  1 
ATOM   4474 C CG  . GLU B 1 286 ? 3.93400   -8.45300  -18.20000 1.000 38.82000 ? 288 GLU B CG  1 
ATOM   4475 C CD  . GLU B 1 286 ? 4.85000   -7.27400  -17.94000 1.000 43.61000 ? 288 GLU B CD  1 
ATOM   4476 O OE1 . GLU B 1 286 ? 5.51400   -6.81600  -18.90800 1.000 48.00000 ? 288 GLU B OE1 1 
ATOM   4477 O OE2 . GLU B 1 286 ? 4.88900   -6.80800  -16.77500 1.000 39.04000 ? 288 GLU B OE2 1 
ATOM   4478 N N   . ASP B 1 287 ? 6.15000   -10.04600 -16.07600 1.000 25.81000 ? 289 ASP B N   1 
ATOM   4479 C CA  . ASP B 1 287 ? 6.01700   -10.58600 -14.72500 1.000 27.76000 ? 289 ASP B CA  1 
ATOM   4480 C C   . ASP B 1 287 ? 5.38400   -9.61000  -13.73200 1.000 26.36000 ? 289 ASP B C   1 
ATOM   4481 O O   . ASP B 1 287 ? 5.49600   -9.81400  -12.51700 1.000 26.31000 ? 289 ASP B O   1 
ATOM   4482 C CB  . ASP B 1 287 ? 7.37800   -11.09500 -14.21000 1.000 27.71000 ? 289 ASP B CB  1 
ATOM   4483 C CG  . ASP B 1 287 ? 8.30000   -9.99400  -13.72200 1.000 29.44000 ? 289 ASP B CG  1 
ATOM   4484 O OD1 . ASP B 1 287 ? 8.15000   -8.81500  -14.11800 1.000 28.87000 ? 289 ASP B OD1 1 
ATOM   4485 O OD2 . ASP B 1 287 ? 9.22000   -10.33400 -12.93800 1.000 32.35000 ? 289 ASP B OD2 1 
ATOM   4486 N N   . GLU B 1 288 ? 4.69200   -8.56500  -14.19300 1.000 26.54000 ? 290 GLU B N   1 
ATOM   4487 C CA  . GLU B 1 288 ? 4.04800   -7.65900  -13.25000 1.000 28.75000 ? 290 GLU B CA  1 
ATOM   4488 C C   . GLU B 1 288 ? 2.52400   -7.78400  -13.27900 1.000 30.55000 ? 290 GLU B C   1 
ATOM   4489 O O   . GLU B 1 288 ? 1.81800   -6.82500  -12.95400 1.000 33.03000 ? 290 GLU B O   1 
ATOM   4490 C CB  . GLU B 1 288 ? 4.50900   -6.21100  -13.48700 1.000 31.86000 ? 290 GLU B CB  1 
ATOM   4491 C CG  . GLU B 1 288 ? 6.03800   -6.04800  -13.46000 1.000 35.43000 ? 290 GLU B CG  1 
ATOM   4492 C CD  . GLU B 1 288 ? 6.55400   -4.77600  -12.75400 1.000 36.41000 ? 290 GLU B CD  1 
ATOM   4493 O OE1 . GLU B 1 288 ? 7.73100   -4.77200  -12.30100 1.000 35.01000 ? 290 GLU B OE1 1 
ATOM   4494 O OE2 . GLU B 1 288 ? 5.80900   -3.78100  -12.64900 1.000 32.96000 ? 290 GLU B OE2 1 
ATOM   4495 N N   . PHE B 1 289 ? 2.00300   -8.96500  -13.61700 1.000 26.13000 ? 291 PHE B N   1 
ATOM   4496 C CA  . PHE B 1 289 ? 0.58500   -9.29500  -13.44400 1.000 26.99000 ? 291 PHE B CA  1 
ATOM   4497 C C   . PHE B 1 289 ? 0.46900   -10.45500 -12.46500 1.000 28.58000 ? 291 PHE B C   1 
ATOM   4498 O O   . PHE B 1 289 ? 0.99200   -11.53800 -12.74000 1.000 27.04000 ? 291 PHE B O   1 
ATOM   4499 C CB  . PHE B 1 289 ? -0.06200  -9.71600  -14.76300 1.000 28.90000 ? 291 PHE B CB  1 
ATOM   4500 C CG  . PHE B 1 289 ? -0.19100  -8.62100  -15.77400 1.000 34.53000 ? 291 PHE B CG  1 
ATOM   4501 C CD1 . PHE B 1 289 ? -1.28700  -7.76700  -15.74700 1.000 31.77000 ? 291 PHE B CD1 1 
ATOM   4502 C CD2 . PHE B 1 289 ? 0.73200   -8.48200  -16.79000 1.000 33.21000 ? 291 PHE B CD2 1 
ATOM   4503 C CE1 . PHE B 1 289 ? -1.42900  -6.76700  -16.69400 1.000 34.22000 ? 291 PHE B CE1 1 
ATOM   4504 C CE2 . PHE B 1 289 ? 0.59300   -7.47800  -17.75200 1.000 37.39000 ? 291 PHE B CE2 1 
ATOM   4505 C CZ  . PHE B 1 289 ? -0.48600  -6.62200  -17.69900 1.000 38.69000 ? 291 PHE B CZ  1 
ATOM   4506 N N   . THR B 1 290 ? -0.25800  -10.25600 -11.36100 1.000 28.42000 ? 292 THR B N   1 
ATOM   4507 C CA  . THR B 1 290 ? -0.48600  -11.35600 -10.43600 1.000 26.29000 ? 292 THR B CA  1 
ATOM   4508 C C   . THR B 1 290 ? -1.62500  -12.25400 -10.91800 1.000 31.04000 ? 292 THR B C   1 
ATOM   4509 O O   . THR B 1 290 ? -2.40000  -11.88000 -11.80600 1.000 30.18000 ? 292 THR B O   1 
ATOM   4510 C CB  . THR B 1 290 ? -0.81200  -10.83800 -9.03900  1.000 29.52000 ? 292 THR B CB  1 
ATOM   4511 O OG1 . THR B 1 290 ? -2.10000  -10.20500 -9.04800  1.000 31.64000 ? 292 THR B OG1 1 
ATOM   4512 C CG2 . THR B 1 290 ? 0.23700   -9.86300  -8.56600  1.000 23.55000 ? 292 THR B CG2 1 
ATOM   4513 N N   . PRO B 1 291 ? -1.73100  -13.46500 -10.36400 1.000 31.65000 ? 293 PRO B N   1 
ATOM   4514 C CA  . PRO B 1 291 ? -2.90600  -14.29800 -10.67400 1.000 34.03000 ? 293 PRO B CA  1 
ATOM   4515 C C   . PRO B 1 291 ? -4.22000  -13.57300 -10.44000 1.000 35.53000 ? 293 PRO B C   1 
ATOM   4516 O O   . PRO B 1 291 ? -5.15000  -13.68600 -11.24900 1.000 34.35000 ? 293 PRO B O   1 
ATOM   4517 C CB  . PRO B 1 291 ? -2.72900  -15.49200 -9.73100  1.000 28.61000 ? 293 PRO B CB  1 
ATOM   4518 C CG  . PRO B 1 291 ? -1.24700  -15.63700 -9.59900  1.000 33.28000 ? 293 PRO B CG  1 
ATOM   4519 C CD  . PRO B 1 291 ? -0.68000  -14.23000 -9.66300  1.000 32.41000 ? 293 PRO B CD  1 
ATOM   4520 N N   . PHE B 1 292 ? -4.31000  -12.80000 -9.35700  1.000 36.71000 ? 294 PHE B N   1 
ATOM   4521 C CA  . PHE B 1 292 ? -5.52200  -12.03200 -9.10100  1.000 38.38000 ? 294 PHE B CA  1 
ATOM   4522 C C   . PHE B 1 292 ? -5.73200  -10.95200 -10.16100 1.000 39.89000 ? 294 PHE B C   1 
ATOM   4523 O O   . PHE B 1 292 ? -6.86400  -10.73900 -10.61700 1.000 41.85000 ? 294 PHE B O   1 
ATOM   4524 C CB  . PHE B 1 292 ? -5.45200  -11.43000 -7.69700  1.000 40.27000 ? 294 PHE B CB  1 
ATOM   4525 C CG  . PHE B 1 292 ? -6.62800  -10.57700 -7.34600  1.000 48.34000 ? 294 PHE B CG  1 
ATOM   4526 C CD1 . PHE B 1 292 ? -7.83800  -11.15600 -6.99600  1.000 51.89000 ? 294 PHE B CD1 1 
ATOM   4527 C CD2 . PHE B 1 292 ? -6.53000  -9.19200  -7.37000  1.000 51.58000 ? 294 PHE B CD2 1 
ATOM   4528 C CE1 . PHE B 1 292 ? -8.93200  -10.36600 -6.67700  1.000 51.62000 ? 294 PHE B CE1 1 
ATOM   4529 C CE2 . PHE B 1 292 ? -7.62300  -8.39700  -7.05100  1.000 49.84000 ? 294 PHE B CE2 1 
ATOM   4530 C CZ  . PHE B 1 292 ? -8.82000  -8.98500  -6.70300  1.000 50.14000 ? 294 PHE B CZ  1 
ATOM   4531 N N   . ASP B 1 293 ? -4.65700  -10.26200 -10.56500 1.000 36.33000 ? 295 ASP B N   1 
ATOM   4532 C CA  . ASP B 1 293 ? -4.75900  -9.24900  -11.61600 1.000 35.02000 ? 295 ASP B CA  1 
ATOM   4533 C C   . ASP B 1 293 ? -5.31700  -9.83600  -12.90500 1.000 36.36000 ? 295 ASP B C   1 
ATOM   4534 O O   . ASP B 1 293 ? -6.06900  -9.17000  -13.62700 1.000 40.74000 ? 295 ASP B O   1 
ATOM   4535 C CB  . ASP B 1 293 ? -3.39000  -8.62000  -11.90500 1.000 34.07000 ? 295 ASP B CB  1 
ATOM   4536 C CG  . ASP B 1 293 ? -2.83500  -7.81600  -10.73800 1.000 33.37000 ? 295 ASP B CG  1 
ATOM   4537 O OD1 . ASP B 1 293 ? -3.61600  -7.41700  -9.85000  1.000 36.30000 ? 295 ASP B OD1 1 
ATOM   4538 O OD2 . ASP B 1 293 ? -1.60400  -7.58200  -10.71500 1.000 30.31000 ? 295 ASP B OD2 1 
ATOM   4539 N N   . VAL B 1 294 ? -4.93500  -11.07100 -13.22900 1.000 32.66000 ? 296 VAL B N   1 
ATOM   4540 C CA  . VAL B 1 294 ? -5.40400  -11.69100 -14.45900 1.000 34.56000 ? 296 VAL B CA  1 
ATOM   4541 C C   . VAL B 1 294 ? -6.89500  -12.00400 -14.34500 1.000 42.03000 ? 296 VAL B C   1 
ATOM   4542 O O   . VAL B 1 294 ? -7.62800  -11.96300 -15.34200 1.000 40.72000 ? 296 VAL B O   1 
ATOM   4543 C CB  . VAL B 1 294 ? -4.54700  -12.93600 -14.76800 1.000 34.94000 ? 296 VAL B CB  1 
ATOM   4544 C CG1 . VAL B 1 294 ? -5.14200  -13.75400 -15.88900 1.000 35.98000 ? 296 VAL B CG1 1 
ATOM   4545 C CG2 . VAL B 1 294 ? -3.11300  -12.51300 -15.13700 1.000 30.14000 ? 296 VAL B CG2 1 
ATOM   4546 N N   . VAL B 1 295 ? -7.37400  -12.26100 -13.13000 1.000 39.71000 ? 297 VAL B N   1 
ATOM   4547 C CA  . VAL B 1 295 ? -8.78700  -12.56900 -12.92100 1.000 40.64000 ? 297 VAL B CA  1 
ATOM   4548 C C   . VAL B 1 295 ? -9.64000  -11.30600 -12.74900 1.000 43.69000 ? 297 VAL B C   1 
ATOM   4549 O O   . VAL B 1 295 ? -10.79200 -11.27600 -13.20000 1.000 47.38000 ? 297 VAL B O   1 
ATOM   4550 C CB  . VAL B 1 295 ? -8.91700  -13.52100 -11.71800 1.000 41.73000 ? 297 VAL B CB  1 
ATOM   4551 C CG1 . VAL B 1 295 ? -10.34500 -13.51800 -11.14900 1.000 44.19000 ? 297 VAL B CG1 1 
ATOM   4552 C CG2 . VAL B 1 295 ? -8.48200  -14.92600 -12.11800 1.000 37.73000 ? 297 VAL B CG2 1 
ATOM   4553 N N   . ARG B 1 296 ? -9.10400  -10.25300 -12.11800 1.000 44.82000 ? 298 ARG B N   1 
ATOM   4554 C CA  . ARG B 1 296 ? -9.81900  -8.97500  -12.05000 1.000 44.84000 ? 298 ARG B CA  1 
ATOM   4555 C C   . ARG B 1 296 ? -9.97700  -8.35100  -13.43700 1.000 47.62000 ? 298 ARG B C   1 
ATOM   4556 O O   . ARG B 1 296 ? -11.03400 -7.79200  -13.75800 1.000 52.29000 ? 298 ARG B O   1 
ATOM   4557 C CB  . ARG B 1 296 ? -9.09700  -8.01200  -11.10500 1.000 43.73000 ? 298 ARG B CB  1 
ATOM   4558 N N   . GLN B 1 297 ? -8.93600  -8.41100  -14.26400 1.000 43.38000 ? 299 GLN B N   1 
ATOM   4559 C CA  . GLN B 1 297 ? -9.11700  -8.26000  -15.70100 1.000 46.64000 ? 299 GLN B CA  1 
ATOM   4560 C C   . GLN B 1 297 ? -9.71900  -9.55900  -16.24500 1.000 46.93000 ? 299 GLN B C   1 
ATOM   4561 O O   . GLN B 1 297 ? -10.01000 -10.48700 -15.49600 1.000 52.72000 ? 299 GLN B O   1 
ATOM   4562 C CB  . GLN B 1 297 ? -7.78700  -7.90400  -16.37100 1.000 44.52000 ? 299 GLN B CB  1 
ATOM   4563 C CG  . GLN B 1 297 ? -7.92300  -6.97100  -17.57100 1.000 45.98000 ? 299 GLN B CG  1 
ATOM   4564 C CD  . GLN B 1 297 ? -6.60500  -6.38400  -18.05000 1.000 47.18000 ? 299 GLN B CD  1 
ATOM   4565 O OE1 . GLN B 1 297 ? -6.49000  -5.96300  -19.21300 1.000 43.85000 ? 299 GLN B OE1 1 
ATOM   4566 N NE2 . GLN B 1 297 ? -5.60900  -6.33200  -17.16100 1.000 38.90000 ? 299 GLN B NE2 1 
ATOM   4567 N N   . CYS B 1 298 ? -9.92100  -9.63400  -17.55800 1.000 52.63000 ? 300 CYS B N   1 
ATOM   4568 C CA  . CYS B 1 298 ? -10.52900 -10.81900 -18.19200 1.000 50.45000 ? 300 CYS B CA  1 
ATOM   4569 C C   . CYS B 1 298 ? -12.01200 -10.98300 -17.80100 1.000 51.83000 ? 300 CYS B C   1 
ATOM   4570 O O   . CYS B 1 298 ? -12.37600 -11.06300 -16.62200 1.000 51.30000 ? 300 CYS B O   1 
ATOM   4571 C CB  . CYS B 1 298 ? -9.75200  -12.11300 -17.85000 1.000 48.10000 ? 300 CYS B CB  1 
ATOM   4572 S SG  . CYS B 1 298 ? -8.00500  -12.23100 -18.40800 1.000 52.88000 ? 300 CYS B SG  1 
HETATM 4573 C C02 . X77 C 2 .   ? -21.75000 -4.95800  -25.37200 1.000 31.54000 ? 401 X77 A C02 1 
HETATM 4574 C C04 . X77 C 2 .   ? -20.20100 -5.89900  -27.17900 1.000 30.61000 ? 401 X77 A C04 1 
HETATM 4575 C C05 . X77 C 2 .   ? -19.99700 -5.80700  -28.68200 1.000 31.87000 ? 401 X77 A C05 1 
HETATM 4576 C C07 . X77 C 2 .   ? -20.17200 -6.91300  -30.93100 1.000 33.59000 ? 401 X77 A C07 1 
HETATM 4577 C C08 . X77 C 2 .   ? -20.03800 -8.35700  -31.40700 1.000 38.43000 ? 401 X77 A C08 1 
HETATM 4578 C C09 . X77 C 2 .   ? -20.05200 -8.47900  -32.92700 1.000 38.84000 ? 401 X77 A C09 1 
HETATM 4579 C C10 . X77 C 2 .   ? -21.23900 -7.74800  -33.54900 1.000 34.58000 ? 401 X77 A C10 1 
HETATM 4580 C C11 . X77 C 2 .   ? -21.38000 -6.29800  -33.07500 1.000 38.93000 ? 401 X77 A C11 1 
HETATM 4581 C C12 . X77 C 2 .   ? -21.32900 -6.13600  -31.55400 1.000 34.36000 ? 401 X77 A C12 1 
HETATM 4582 C C14 . X77 C 2 .   ? -18.87700 -5.46500  -26.55300 1.000 28.90000 ? 401 X77 A C14 1 
HETATM 4583 C C15 . X77 C 2 .   ? -18.49000 -4.02900  -26.46900 1.000 26.89000 ? 401 X77 A C15 1 
HETATM 4584 C C16 . X77 C 2 .   ? -17.16300 -3.69700  -25.88900 1.000 26.11000 ? 401 X77 A C16 1 
HETATM 4585 C C17 . X77 C 2 .   ? -16.21000 -4.77900  -25.38000 1.000 30.99000 ? 401 X77 A C17 1 
HETATM 4586 C C19 . X77 C 2 .   ? -17.94100 -6.56000  -26.07100 1.000 28.77000 ? 401 X77 A C19 1 
HETATM 4587 C C20 . X77 C 2 .   ? -22.19600 -4.54100  -27.86500 1.000 29.30000 ? 401 X77 A C20 1 
HETATM 4588 C C21 . X77 C 2 .   ? -21.99300 -3.12000  -28.41600 1.000 28.77000 ? 401 X77 A C21 1 
HETATM 4589 C C22 . X77 C 2 .   ? -22.93500 -2.61600  -29.52800 1.000 30.80000 ? 401 X77 A C22 1 
HETATM 4590 C C23 . X77 C 2 .   ? -24.04100 -3.53100  -30.05000 1.000 30.17000 ? 401 X77 A C23 1 
HETATM 4591 C C24 . X77 C 2 .   ? -25.00400 -3.08000  -31.15400 1.000 33.62000 ? 401 X77 A C24 1 
HETATM 4592 C C25 . X77 C 2 .   ? -26.39300 -3.00200  -30.53400 1.000 30.86000 ? 401 X77 A C25 1 
HETATM 4593 C C26 . X77 C 2 .   ? -24.97200 -4.13100  -32.24500 1.000 35.55000 ? 401 X77 A C26 1 
HETATM 4594 C C27 . X77 C 2 .   ? -24.54600 -1.71400  -31.72500 1.000 32.35000 ? 401 X77 A C27 1 
HETATM 4595 C C28 . X77 C 2 .   ? -24.22900 -4.94500  -29.48800 1.000 31.21000 ? 401 X77 A C28 1 
HETATM 4596 C C29 . X77 C 2 .   ? -23.30100 -5.44700  -28.38300 1.000 31.12000 ? 401 X77 A C29 1 
HETATM 4597 C C30 . X77 C 2 .   ? -22.99600 -4.18000  -24.88400 1.000 28.26000 ? 401 X77 A C30 1 
HETATM 4598 C C31 . X77 C 2 .   ? -23.91700 -3.48600  -25.62900 1.000 30.00000 ? 401 X77 A C31 1 
HETATM 4599 C C33 . X77 C 2 .   ? -24.48400 -3.35800  -23.55300 1.000 33.04000 ? 401 X77 A C33 1 
HETATM 4600 N N03 . X77 C 2 .   ? -21.36500 -5.10400  -26.79200 1.000 32.36000 ? 401 X77 A N03 1 
HETATM 4601 N N06 . X77 C 2 .   ? -20.36700 -6.97000  -29.48300 1.000 31.10000 ? 401 X77 A N06 1 
HETATM 4602 N N18 . X77 C 2 .   ? -16.61800 -6.20400  -25.48800 1.000 31.47000 ? 401 X77 A N18 1 
HETATM 4603 N N32 . X77 C 2 .   ? -24.81500 -2.99200  -24.80800 1.000 31.74000 ? 401 X77 A N32 1 
HETATM 4604 N N34 . X77 C 2 .   ? -23.35100 -4.09800  -23.62200 1.000 32.46000 ? 401 X77 A N34 1 
HETATM 4605 O O01 . X77 C 2 .   ? -21.08200 -5.46300  -24.55800 1.000 31.48000 ? 401 X77 A O01 1 
HETATM 4606 O O13 . X77 C 2 .   ? -19.53000 -4.83900  -29.20800 1.000 28.39000 ? 401 X77 A O13 1 
HETATM 4607 C C02 . X77 D 2 .   ? 13.91000  14.03900  -4.26700  1.000 32.49000 ? 401 X77 B C02 1 
HETATM 4608 C C04 . X77 D 2 .   ? 15.49400  12.23900  -5.25700  1.000 32.92000 ? 401 X77 B C04 1 
HETATM 4609 C C05 . X77 D 2 .   ? 16.43500  11.16200  -4.74200  1.000 34.35000 ? 401 X77 B C05 1 
HETATM 4610 C C07 . X77 D 2 .   ? 18.78500  10.30300  -4.41400  1.000 35.25000 ? 401 X77 B C07 1 
HETATM 4611 C C08 . X77 D 2 .   ? 20.05100  10.33900  -5.28100  1.000 36.71000 ? 401 X77 B C08 1 
HETATM 4612 C C09 . X77 D 2 .   ? 21.34600  10.33900  -4.47600  1.000 41.81000 ? 401 X77 B C09 1 
HETATM 4613 C C10 . X77 D 2 .   ? 21.26400  9.44000   -3.24700  1.000 37.48000 ? 401 X77 B C10 1 
HETATM 4614 C C11 . X77 D 2 .   ? 20.18300  9.89900   -2.26300  1.000 41.04000 ? 401 X77 B C11 1 
HETATM 4615 C C12 . X77 D 2 .   ? 18.99100  10.60300  -2.92400  1.000 35.94000 ? 401 X77 B C12 1 
HETATM 4616 C C14 . X77 D 2 .   ? 14.47900  11.51300  -6.13300  1.000 33.85000 ? 401 X77 B C14 1 
HETATM 4617 C C15 . X77 D 2 .   ? 14.61200  11.59900  -7.62100  1.000 34.07000 ? 401 X77 B C15 1 
HETATM 4618 C C16 . X77 D 2 .   ? 13.66500  10.88300  -8.52200  1.000 32.47000 ? 401 X77 B C16 1 
HETATM 4619 C C17 . X77 D 2 .   ? 12.55600  10.05200  -7.88800  1.000 33.51000 ? 401 X77 B C17 1 
HETATM 4620 C C19 . X77 D 2 .   ? 13.37700  10.68300  -5.49700  1.000 30.83000 ? 401 X77 B C19 1 
HETATM 4621 C C20 . X77 D 2 .   ? 15.52100  12.69600  -2.78900  1.000 29.95000 ? 401 X77 B C20 1 
HETATM 4622 C C21 . X77 D 2 .   ? 14.95600  11.64500  -1.82000  1.000 29.58000 ? 401 X77 B C21 1 
HETATM 4623 C C22 . X77 D 2 .   ? 15.65600  11.42300  -0.47300  1.000 31.47000 ? 401 X77 B C22 1 
HETATM 4624 C C23 . X77 D 2 .   ? 16.89900  12.23200  -0.11300  1.000 33.46000 ? 401 X77 B C23 1 
HETATM 4625 C C24 . X77 D 2 .   ? 17.60900  12.04000  1.23100   1.000 32.81000 ? 401 X77 B C24 1 
HETATM 4626 C C25 . X77 D 2 .   ? 17.12000  10.76400  1.90000   1.000 28.64000 ? 401 X77 B C25 1 
HETATM 4627 C C26 . X77 D 2 .   ? 17.30000  13.24400  2.09100   1.000 34.63000 ? 401 X77 B C26 1 
HETATM 4628 C C27 . X77 D 2 .   ? 19.14200  11.96100  0.97600   1.000 37.24000 ? 401 X77 B C27 1 
HETATM 4629 C C28 . X77 D 2 .   ? 17.45600  13.28300  -1.08000  1.000 32.40000 ? 401 X77 B C28 1 
HETATM 4630 C C29 . X77 D 2 .   ? 16.76600  13.50600  -2.43000  1.000 30.84000 ? 401 X77 B C29 1 
HETATM 4631 C C30 . X77 D 2 .   ? 13.37400  14.84700  -3.06500  1.000 29.50000 ? 401 X77 B C30 1 
HETATM 4632 C C31 . X77 D 2 .   ? 12.38600  15.79300  -3.13000  1.000 31.96000 ? 401 X77 B C31 1 
HETATM 4633 C C33 . X77 D 2 .   ? 13.06900  15.67200  -1.08900  1.000 29.28000 ? 401 X77 B C33 1 
HETATM 4634 N N03 . X77 D 2 .   ? 14.93700  12.97700  -4.10600  1.000 31.51000 ? 401 X77 B N03 1 
HETATM 4635 N N06 . X77 D 2 .   ? 17.87700  11.34500  -4.91900  1.000 33.33000 ? 401 X77 B N06 1 
HETATM 4636 N N18 . X77 D 2 .   ? 12.44900  9.97000   -6.40800  1.000 32.04000 ? 401 X77 B N18 1 
HETATM 4637 N N32 . X77 D 2 .   ? 12.20600  16.27500  -1.92300  1.000 37.14000 ? 401 X77 B N32 1 
HETATM 4638 N N34 . X77 D 2 .   ? 13.78300  14.79100  -1.81600  1.000 33.83000 ? 401 X77 B N34 1 
HETATM 4639 O O01 . X77 D 2 .   ? 13.50100  14.27200  -5.35200  1.000 33.64000 ? 401 X77 B O01 1 
HETATM 4640 O O13 . X77 D 2 .   ? 16.03200  10.17800  -4.20600  1.000 30.35000 ? 401 X77 B O13 1 
HETATM 4641 O O   . HOH E 3 .   ? 13.63600  9.81000   -51.99000 1.000 33.85000 ? 501 HOH A O   1 
HETATM 4642 O O   . HOH E 3 .   ? 22.03900  15.14000  -34.80600 1.000 30.54000 ? 502 HOH A O   1 
HETATM 4643 O O   . HOH E 3 .   ? -33.99900 7.19700   -13.92300 1.000 34.13000 ? 503 HOH A O   1 
HETATM 4644 O O   . HOH E 3 .   ? -2.57700  10.88400  -22.97300 1.000 28.01000 ? 504 HOH A O   1 
HETATM 4645 O O   . HOH E 3 .   ? -22.43500 -1.83200  -17.91500 1.000 29.23000 ? 505 HOH A O   1 
HETATM 4646 O O   . HOH E 3 .   ? -15.31700 15.63100  -11.24200 1.000 32.84000 ? 506 HOH A O   1 
HETATM 4647 O O   . HOH E 3 .   ? 20.31400  -3.81600  -32.72400 1.000 35.94000 ? 507 HOH A O   1 
HETATM 4648 O O   . HOH E 3 .   ? -24.55800 9.56500   -6.70400  1.000 45.40000 ? 508 HOH A O   1 
HETATM 4649 O O   . HOH E 3 .   ? -12.09700 -3.73700  -18.66100 1.000 32.66000 ? 509 HOH A O   1 
HETATM 4650 O O   . HOH E 3 .   ? 18.97100  14.81700  -44.49600 1.000 37.27000 ? 510 HOH A O   1 
HETATM 4651 O O   . HOH E 3 .   ? -4.71600  1.68700   -28.96900 1.000 30.30000 ? 511 HOH A O   1 
HETATM 4652 O O   . HOH E 3 .   ? -3.55900  19.96400  -24.03700 1.000 37.78000 ? 512 HOH A O   1 
HETATM 4653 O O   . HOH E 3 .   ? -15.36300 6.04600   -18.28400 1.000 27.52000 ? 513 HOH A O   1 
HETATM 4654 O O   . HOH E 3 .   ? 0.90600   15.15200  -40.29100 1.000 30.87000 ? 514 HOH A O   1 
HETATM 4655 O O   . HOH E 3 .   ? 17.68400  5.12000   -47.33100 1.000 32.61000 ? 515 HOH A O   1 
HETATM 4656 O O   . HOH E 3 .   ? -0.08300  14.34800  -27.62600 1.000 31.28000 ? 516 HOH A O   1 
HETATM 4657 O O   . HOH E 3 .   ? -24.47800 3.72900   -30.43700 1.000 24.46000 ? 517 HOH A O   1 
HETATM 4658 O O   . HOH E 3 .   ? -0.47900  11.91300  -21.48000 1.000 35.72000 ? 518 HOH A O   1 
HETATM 4659 O O   . HOH E 3 .   ? -32.40400 -5.55300  -36.97900 1.000 40.39000 ? 519 HOH A O   1 
HETATM 4660 O O   . HOH E 3 .   ? 11.90600  -4.78700  -38.19200 1.000 32.02000 ? 520 HOH A O   1 
HETATM 4661 O O   . HOH E 3 .   ? -22.76200 16.03400  -27.31600 1.000 33.12000 ? 521 HOH A O   1 
HETATM 4662 O O   . HOH E 3 .   ? -12.92700 9.14700   -38.74400 1.000 36.39000 ? 522 HOH A O   1 
HETATM 4663 O O   . HOH E 3 .   ? 1.16400   11.58700  -32.28700 1.000 27.95000 ? 523 HOH A O   1 
HETATM 4664 O O   . HOH E 3 .   ? -10.18100 0.92900   -40.12500 1.000 35.77000 ? 524 HOH A O   1 
HETATM 4665 O O   . HOH E 3 .   ? -26.92900 19.68600  -8.29600  1.000 36.59000 ? 525 HOH A O   1 
HETATM 4666 O O   . HOH E 3 .   ? -38.45700 0.65400   -34.83700 1.000 33.69000 ? 526 HOH A O   1 
HETATM 4667 O O   . HOH E 3 .   ? -28.67500 10.63000  -35.09900 1.000 31.73000 ? 527 HOH A O   1 
HETATM 4668 O O   . HOH E 3 .   ? 16.474    -8.861    -29.659   1.000 42.22000 ? 528 HOH A O   1 
HETATM 4669 O O   . HOH E 3 .   ? 21.31200  0.40900   -44.13100 1.000 31.87000 ? 529 HOH A O   1 
HETATM 4670 O O   . HOH E 3 .   ? -13.58000 3.98800   -33.58100 1.000 28.19000 ? 530 HOH A O   1 
HETATM 4671 O O   . HOH E 3 .   ? -29.66800 1.88400   -14.49300 1.000 32.74000 ? 531 HOH A O   1 
HETATM 4672 O O   . HOH E 3 .   ? 15.67700  11.52200  -51.09100 1.000 31.04000 ? 532 HOH A O   1 
HETATM 4673 O O   . HOH E 3 .   ? 24.12800  4.65400   -24.19600 1.000 40.53000 ? 533 HOH A O   1 
HETATM 4674 O O   . HOH E 3 .   ? -26.36600 2.25700   -37.23100 1.000 33.47000 ? 534 HOH A O   1 
HETATM 4675 O O   . HOH E 3 .   ? -0.84900  -0.93300  -29.16100 1.000 41.16000 ? 535 HOH A O   1 
HETATM 4676 O O   . HOH E 3 .   ? 18.90100  9.62600   -47.49500 1.000 26.97000 ? 536 HOH A O   1 
HETATM 4677 O O   . HOH E 3 .   ? 17.66600  -1.64900  -44.36300 1.000 28.67000 ? 537 HOH A O   1 
HETATM 4678 O O   . HOH E 3 .   ? -23.80100 18.66200  -20.13200 1.000 35.00000 ? 538 HOH A O   1 
HETATM 4679 O O   . HOH E 3 .   ? -38.72900 10.19700  -40.54000 1.000 36.80000 ? 539 HOH A O   1 
HETATM 4680 O O   . HOH E 3 .   ? 21.51900  8.46700   -35.72600 1.000 33.58000 ? 540 HOH A O   1 
HETATM 4681 O O   . HOH E 3 .   ? -7.92500  -4.48800  -27.95100 1.000 36.37000 ? 541 HOH A O   1 
HETATM 4682 O O   . HOH E 3 .   ? 5.65000   5.91400   -28.53100 1.000 23.87000 ? 542 HOH A O   1 
HETATM 4683 O O   . HOH E 3 .   ? -20.81300 8.41200   -36.80600 1.000 28.42000 ? 543 HOH A O   1 
HETATM 4684 O O   . HOH E 3 .   ? 13.11100  14.33100  -48.67600 1.000 31.96000 ? 544 HOH A O   1 
HETATM 4685 O O   . HOH E 3 .   ? 8.88700   1.86100   -22.90200 1.000 37.94000 ? 545 HOH A O   1 
HETATM 4686 O O   . HOH E 3 .   ? -15.36500 14.68900  -28.14500 1.000 30.56000 ? 546 HOH A O   1 
HETATM 4687 O O   . HOH E 3 .   ? 16.28800  16.96000  -39.10900 1.000 30.71000 ? 547 HOH A O   1 
HETATM 4688 O O   . HOH E 3 .   ? 19.05900  6.42200   -49.36400 1.000 31.26000 ? 548 HOH A O   1 
HETATM 4689 O O   . HOH E 3 .   ? 15.60800  -0.51300  -42.75500 1.000 29.06000 ? 549 HOH A O   1 
HETATM 4690 O O   . HOH E 3 .   ? 20.44300  4.55200   -41.12700 1.000 25.51000 ? 550 HOH A O   1 
HETATM 4691 O O   . HOH E 3 .   ? 22.83900  12.12700  -24.81100 1.000 34.17000 ? 551 HOH A O   1 
HETATM 4692 O O   . HOH E 3 .   ? 0.75700   7.58000   -23.44900 1.000 31.14000 ? 552 HOH A O   1 
HETATM 4693 O O   . HOH E 3 .   ? -13.42600 10.95600  -7.39600  1.000 35.08000 ? 553 HOH A O   1 
HETATM 4694 O O   . HOH E 3 .   ? 1.72700   8.13700   -20.71000 1.000 36.13000 ? 554 HOH A O   1 
HETATM 4695 O O   . HOH E 3 .   ? -32.75900 6.76200   -37.90000 1.000 35.99000 ? 555 HOH A O   1 
HETATM 4696 O O   . HOH E 3 .   ? 24.23300  9.65800   -43.87900 1.000 29.20000 ? 556 HOH A O   1 
HETATM 4697 O O   . HOH E 3 .   ? -12.17200 20.78200  -12.63100 1.000 39.08000 ? 557 HOH A O   1 
HETATM 4698 O O   . HOH E 3 .   ? 3.86000   9.39900   -38.09300 1.000 28.20000 ? 558 HOH A O   1 
HETATM 4699 O O   . HOH E 3 .   ? 21.36800  -1.80400  -34.35400 1.000 35.32000 ? 559 HOH A O   1 
HETATM 4700 O O   . HOH E 3 .   ? -35.94200 -0.22800  -35.93200 1.000 30.82000 ? 560 HOH A O   1 
HETATM 4701 O O   . HOH E 3 .   ? -34.43800 -4.15500  -36.62700 1.000 44.94000 ? 561 HOH A O   1 
HETATM 4702 O O   . HOH E 3 .   ? 19.96600  7.71000   -45.75200 1.000 32.57000 ? 562 HOH A O   1 
HETATM 4703 O O   . HOH E 3 .   ? -30.82500 4.90800   -37.92900 1.000 30.41000 ? 563 HOH A O   1 
HETATM 4704 O O   . HOH E 3 .   ? 19.83800  6.24000   -42.79300 1.000 29.58000 ? 564 HOH A O   1 
HETATM 4705 O O   . HOH E 3 .   ? 0.37000   11.85700  -34.77000 1.000 30.67000 ? 565 HOH A O   1 
HETATM 4706 O O   . HOH E 3 .   ? 20.43800  1.99300   -41.69200 1.000 30.27000 ? 566 HOH A O   1 
HETATM 4707 O O   . HOH E 3 .   ? 1.03100   9.25500   -37.17800 1.000 36.63000 ? 567 HOH A O   1 
HETATM 4708 O O   . HOH E 3 .   ? 21.01200  11.12300  -47.98000 1.000 29.80000 ? 568 HOH A O   1 
HETATM 4709 O O   . HOH E 3 .   ? 18.73200  17.53200  -40.37200 1.000 36.57000 ? 569 HOH A O   1 
HETATM 4710 O O   . HOH F 3 .   ? 0.40700   24.34300  7.52700   1.000 42.81000 ? 501 HOH B O   1 
HETATM 4711 O O   . HOH F 3 .   ? 3.52200   -8.69100  4.89000   1.000 40.61000 ? 502 HOH B O   1 
HETATM 4712 O O   . HOH F 3 .   ? 5.99900   10.97300  -12.41600 1.000 35.29000 ? 503 HOH B O   1 
HETATM 4713 O O   . HOH F 3 .   ? 13.59800  15.49800  1.70200   1.000 34.78000 ? 504 HOH B O   1 
HETATM 4714 O O   . HOH F 3 .   ? 11.955    -35.987   -14.412   1.000 42.31000 ? 505 HOH B O   1 
HETATM 4715 O O   . HOH F 3 .   ? 15.268    -2.724    5.508     1.000 32.38000 ? 506 HOH B O   1 
HETATM 4716 O O   . HOH F 3 .   ? -8.46600  -2.80700  0.42500   1.000 33.65000 ? 507 HOH B O   1 
HETATM 4717 O O   . HOH F 3 .   ? -6.59500  15.08800  -8.75900  1.000 38.79000 ? 508 HOH B O   1 
HETATM 4718 O O   . HOH F 3 .   ? 1.34000   0.17600   4.78500   1.000 27.52000 ? 509 HOH B O   1 
HETATM 4719 O O   . HOH F 3 .   ? -11.47300 9.54700   -0.66100  1.000 30.61000 ? 510 HOH B O   1 
HETATM 4720 O O   . HOH F 3 .   ? 8.18500   -2.52500  -10.36800 1.000 31.66000 ? 511 HOH B O   1 
HETATM 4721 O O   . HOH F 3 .   ? 11.37500  -0.33500  11.38500  1.000 27.06000 ? 512 HOH B O   1 
HETATM 4722 O O   . HOH F 3 .   ? 3.89400   -2.72200  8.47600   1.000 32.85000 ? 513 HOH B O   1 
HETATM 4723 O O   . HOH F 3 .   ? 3.33400   23.13800  1.38400   1.000 43.20000 ? 514 HOH B O   1 
HETATM 4724 O O   . HOH F 3 .   ? 12.49100  -11.63400 -2.57200  1.000 34.46000 ? 515 HOH B O   1 
HETATM 4725 O O   . HOH F 3 .   ? 12.346    6.876     13.600    1.000 29.59000 ? 516 HOH B O   1 
HETATM 4726 O O   . HOH F 3 .   ? 2.81300   -12.65600 -7.18100  1.000 31.90000 ? 517 HOH B O   1 
HETATM 4727 O O   . HOH F 3 .   ? 21.29000  7.02600   -0.90000  1.000 38.72000 ? 518 HOH B O   1 
HETATM 4728 O O   . HOH F 3 .   ? 11.79100  -0.17400  -1.52400  1.000 24.44000 ? 519 HOH B O   1 
HETATM 4729 O O   . HOH F 3 .   ? -10.75700 5.73400   -6.31400  1.000 36.24000 ? 520 HOH B O   1 
HETATM 4730 O O   . HOH F 3 .   ? 2.86700   -11.16500 -15.21100 1.000 27.31000 ? 521 HOH B O   1 
HETATM 4731 O O   . HOH F 3 .   ? -2.79000  -4.59700  -7.99900  1.000 31.73000 ? 522 HOH B O   1 
HETATM 4732 O O   . HOH F 3 .   ? -8.77500  13.44900  -11.61900 1.000 28.13000 ? 523 HOH B O   1 
HETATM 4733 O O   . HOH F 3 .   ? 15.50500  -9.55900  -1.88300  1.000 30.67000 ? 524 HOH B O   1 
HETATM 4734 O O   . HOH F 3 .   ? -2.28700  -2.83400  -0.89900  1.000 28.34000 ? 525 HOH B O   1 
HETATM 4735 O O   . HOH F 3 .   ? -10.22800 16.69700  1.17600   1.000 40.62000 ? 526 HOH B O   1 
HETATM 4736 O O   . HOH F 3 .   ? 8.88800   1.68700   15.76600  1.000 33.11000 ? 527 HOH B O   1 
HETATM 4737 O O   . HOH F 3 .   ? 4.44700   -3.10600  12.41900  1.000 40.94000 ? 528 HOH B O   1 
HETATM 4738 O O   . HOH F 3 .   ? 15.70100  -3.28100  -9.45500  1.000 35.38000 ? 529 HOH B O   1 
HETATM 4739 O O   . HOH F 3 .   ? -14.29900 4.54000   1.20800   1.000 31.23000 ? 530 HOH B O   1 
HETATM 4740 O O   . HOH F 3 .   ? 19.10400  7.17000   7.53600   1.000 33.62000 ? 531 HOH B O   1 
HETATM 4741 O O   . HOH F 3 .   ? 7.50100   -8.03500  2.64200   1.000 31.98000 ? 532 HOH B O   1 
HETATM 4742 O O   . HOH F 3 .   ? 12.50900  9.41100   4.88100   1.000 26.90000 ? 533 HOH B O   1 
HETATM 4743 O O   . HOH F 3 .   ? -0.86500  -5.44800  -12.55300 1.000 31.32000 ? 534 HOH B O   1 
HETATM 4744 O O   . HOH F 3 .   ? -5.22000  16.51200  -4.42400  1.000 39.46000 ? 535 HOH B O   1 
HETATM 4745 O O   . HOH F 3 .   ? 12.24500  -5.76200  3.32700   1.000 26.01000 ? 536 HOH B O   1 
HETATM 4746 O O   . HOH F 3 .   ? 16.599    4.077     7.293     1.000 29.17000 ? 537 HOH B O   1 
HETATM 4747 O O   . HOH F 3 .   ? 11.62000  7.34700   -13.01100 1.000 33.55000 ? 538 HOH B O   1 
HETATM 4748 O O   . HOH F 3 .   ? -3.10600  -4.66000  -14.09600 1.000 31.93000 ? 539 HOH B O   1 
HETATM 4749 O O   . HOH F 3 .   ? 12.28800  2.41900   -12.67500 1.000 33.82000 ? 540 HOH B O   1 
HETATM 4750 O O   . HOH F 3 .   ? 7.36000   -17.03300 -8.23100  1.000 32.66000 ? 541 HOH B O   1 
HETATM 4751 O O   . HOH F 3 .   ? 5.74200   -0.99900  12.57200  1.000 31.25000 ? 542 HOH B O   1 
HETATM 4752 O O   . HOH F 3 .   ? 13.128    -2.847    7.525     1.000 38.18000 ? 543 HOH B O   1 
HETATM 4753 O O   . HOH F 3 .   ? -3.26000  -5.06900  -0.26800  1.000 38.00000 ? 544 HOH B O   1 
# 
