data_7I1H
# 
_entry.id   7I1H 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7I1H         pdb_00007i1h 10.2210/pdb7i1h/pdb 
WWPDB D_1001408196 ?            ?                   
# 
_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       2025-05-21 
_pdbx_audit_revision_history.part_number         ? 
# 
_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.entry_id                        7I1H 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-03 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.name_last          Weiss 
_pdbx_contact_author.name_first         Manfred 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              manfred.weiss@helmholtz-berlin.de 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2362-7047 
# 
loop_
_audit_author.pdbx_ordinal 
_audit_author.name 
1 'Barthel, T.'     
2 'Benz, L.S.'      
3 'Wollenhaupt, J.' 
4 'Weiss, M.S.'     
# 
_citation.id                        primary 
_citation.title                     
'Orthorhombic SARS-CoV-2 main protease crystals provide higher success rate in fragment screening' 
_citation.journal_abbrev            'To be published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.ordinal 
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
1  primary 'Barthel, T.'     ? 
2  primary 'Wollenhaupt, J.' ? 
3  primary 'Benz, L.S.'      ? 
4  primary 'Reincke, P.'     ? 
5  primary 'Zhang, L.'       ? 
6  primary 'Lennartz, F.'    ? 
7  primary 'Tabermann, H.'   ? 
8  primary 'Mueller, U.'     ? 
9  primary 'Meente, A.'      ? 
10 primary 'Hilgenfeld, R.'  ? 
11 primary 'Weiss, M.S.'     ? 
# 
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' 33825.547 2  3.4.22.69 ? ? ? 
2 non-polymer syn 'CHLORIDE ION'            35.453    2  ?         ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'      78.133    3  ?         ? ? ? 
4 non-polymer syn 1-phenyl-1H-tetrazole     146.149   1  ?         ? ? ? 
5 water       nat water                     18.015    84 ?         ? ? ? 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_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 'CHLORIDE ION'        CL    
3 'DIMETHYL SULFOXIDE'  DMS   
4 1-phenyl-1H-tetrazole A1BVY 
5 water                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN 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                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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               ? 
_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          plasmid 
_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 
A1BVY non-polymer         . 1-phenyl-1H-tetrazole ? 'C7 H6 N4'       146.149 
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 
CL    non-polymer         . 'CHLORIDE ION'        ? 'Cl -1'          35.453  
CYS   'L-peptide linking' y CYSTEINE              ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'  ? 'C2 H6 O S'      78.133  
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 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 ?   ?   ?   A . n 
A 1 303 VAL 303 303 ?   ?   ?   A . n 
A 1 304 THR 304 304 ?   ?   ?   A . n 
A 1 305 PHE 305 305 ?   ?   ?   A . n 
A 1 306 GLN 306 306 ?   ?   ?   A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   GLY 2   2   2   GLY GLY B . n 
B 1 3   PHE 3   3   3   PHE PHE B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   MET 6   6   6   MET MET B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  CYS 16  16  16  CYS CYS B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  TRP 31  31  31  TRP TRP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  CYS 38  38  38  CYS CYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  HIS 41  41  41  HIS HIS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  CYS 44  44  44  CYS CYS B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  MET 49  49  49  MET MET B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  ASN 51  51  51  ASN ASN B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 CYS 117 117 117 CYS CYS B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 GLN 127 127 127 GLN GLN B . n 
B 1 128 CYS 128 128 128 CYS CYS B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 MET 130 130 130 MET MET B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 CYS 145 145 145 CYS CYS B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 CYS 160 160 160 CYS CYS B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 MET 162 162 162 MET MET B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 MET 165 165 165 MET MET B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 HIS 172 172 172 HIS HIS B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 TRP 207 207 207 TRP TRP B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 TYR 209 209 209 TYR TYR B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 ASP 216 216 216 ASP ASP B . n 
B 1 217 ARG 217 217 217 ARG ARG B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 ASN 221 221 221 ASN ASN B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 ASN 228 228 228 ASN ASN B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 MET 235 235 235 MET MET B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 GLU 240 240 240 GLU GLU B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 HIS 246 246 246 HIS HIS B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 MET 264 264 264 MET MET B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 GLN 273 273 273 GLN GLN B . n 
B 1 274 ASN 274 274 274 ASN ASN B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 MET 276 276 276 MET MET B . n 
B 1 277 ASN 277 277 277 ASN ASN B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 PHE 291 291 291 PHE PHE B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 PRO 293 293 293 PRO PRO B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLN 299 299 299 GLN GLN B . n 
B 1 300 CYS 300 300 300 CYS CYS B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 GLY 302 302 ?   ?   ?   B . n 
B 1 303 VAL 303 303 ?   ?   ?   B . n 
B 1 304 THR 304 304 ?   ?   ?   B . n 
B 1 305 PHE 305 305 ?   ?   ?   B . n 
B 1 306 GLN 306 306 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BVY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BVY 
_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 CL    1  401 410 CL    CL  A . 
D 3 DMS   1  402 601 DMS   DMS A . 
E 4 A1BVY 1  403 602 A1BVY DRG A . 
F 2 CL    1  404 1   CL    CL  A . 
G 3 DMS   1  501 501 DMS   DMS B . 
H 3 DMS   1  502 601 DMS   DMS B . 
I 5 HOH   1  501 46  HOH   HOH A . 
I 5 HOH   2  502 80  HOH   HOH A . 
I 5 HOH   3  503 43  HOH   HOH A . 
I 5 HOH   4  504 78  HOH   HOH A . 
I 5 HOH   5  505 28  HOH   HOH A . 
I 5 HOH   6  506 84  HOH   HOH A . 
I 5 HOH   7  507 25  HOH   HOH A . 
I 5 HOH   8  508 35  HOH   HOH A . 
I 5 HOH   9  509 4   HOH   HOH A . 
I 5 HOH   10 510 77  HOH   HOH A . 
I 5 HOH   11 511 31  HOH   HOH A . 
I 5 HOH   12 512 59  HOH   HOH A . 
I 5 HOH   13 513 7   HOH   HOH A . 
I 5 HOH   14 514 50  HOH   HOH A . 
I 5 HOH   15 515 74  HOH   HOH A . 
I 5 HOH   16 516 49  HOH   HOH A . 
I 5 HOH   17 517 3   HOH   HOH A . 
I 5 HOH   18 518 8   HOH   HOH A . 
I 5 HOH   19 519 30  HOH   HOH A . 
I 5 HOH   20 520 23  HOH   HOH A . 
I 5 HOH   21 521 63  HOH   HOH A . 
I 5 HOH   22 522 48  HOH   HOH A . 
I 5 HOH   23 523 72  HOH   HOH A . 
I 5 HOH   24 524 69  HOH   HOH A . 
I 5 HOH   25 525 81  HOH   HOH A . 
I 5 HOH   26 526 47  HOH   HOH A . 
I 5 HOH   27 527 38  HOH   HOH A . 
I 5 HOH   28 528 14  HOH   HOH A . 
I 5 HOH   29 529 18  HOH   HOH A . 
I 5 HOH   30 530 2   HOH   HOH A . 
I 5 HOH   31 531 42  HOH   HOH A . 
I 5 HOH   32 532 65  HOH   HOH A . 
I 5 HOH   33 533 41  HOH   HOH A . 
I 5 HOH   34 534 27  HOH   HOH A . 
I 5 HOH   35 535 21  HOH   HOH A . 
I 5 HOH   36 536 62  HOH   HOH A . 
I 5 HOH   37 537 60  HOH   HOH A . 
I 5 HOH   38 538 34  HOH   HOH A . 
I 5 HOH   39 539 44  HOH   HOH A . 
I 5 HOH   40 540 52  HOH   HOH A . 
I 5 HOH   41 541 19  HOH   HOH A . 
I 5 HOH   42 542 68  HOH   HOH A . 
I 5 HOH   43 543 83  HOH   HOH A . 
I 5 HOH   44 544 26  HOH   HOH A . 
I 5 HOH   45 545 61  HOH   HOH A . 
I 5 HOH   46 546 64  HOH   HOH A . 
I 5 HOH   47 547 55  HOH   HOH A . 
I 5 HOH   48 548 53  HOH   HOH A . 
J 5 HOH   1  601 6   HOH   HOH B . 
J 5 HOH   2  602 33  HOH   HOH B . 
J 5 HOH   3  603 10  HOH   HOH B . 
J 5 HOH   4  604 76  HOH   HOH B . 
J 5 HOH   5  605 36  HOH   HOH B . 
J 5 HOH   6  606 24  HOH   HOH B . 
J 5 HOH   7  607 85  HOH   HOH B . 
J 5 HOH   8  608 5   HOH   HOH B . 
J 5 HOH   9  609 17  HOH   HOH B . 
J 5 HOH   10 610 22  HOH   HOH B . 
J 5 HOH   11 611 39  HOH   HOH B . 
J 5 HOH   12 612 58  HOH   HOH B . 
J 5 HOH   13 613 9   HOH   HOH B . 
J 5 HOH   14 614 40  HOH   HOH B . 
J 5 HOH   15 615 37  HOH   HOH B . 
J 5 HOH   16 616 66  HOH   HOH B . 
J 5 HOH   17 617 11  HOH   HOH B . 
J 5 HOH   18 618 29  HOH   HOH B . 
J 5 HOH   19 619 15  HOH   HOH B . 
J 5 HOH   20 620 45  HOH   HOH B . 
J 5 HOH   21 621 56  HOH   HOH B . 
J 5 HOH   22 622 70  HOH   HOH B . 
J 5 HOH   23 623 13  HOH   HOH B . 
J 5 HOH   24 624 79  HOH   HOH B . 
J 5 HOH   25 625 20  HOH   HOH B . 
J 5 HOH   26 626 51  HOH   HOH B . 
J 5 HOH   27 627 32  HOH   HOH B . 
J 5 HOH   28 628 71  HOH   HOH B . 
J 5 HOH   29 629 67  HOH   HOH B . 
J 5 HOH   30 630 75  HOH   HOH B . 
J 5 HOH   31 631 16  HOH   HOH B . 
J 5 HOH   32 632 73  HOH   HOH B . 
J 5 HOH   33 633 54  HOH   HOH B . 
J 5 HOH   34 634 12  HOH   HOH B . 
J 5 HOH   35 635 82  HOH   HOH B . 
J 5 HOH   36 636 57  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC 5.8.0425 ? 1 
'data scaling'   XDS    .        ? 2 
'data reduction' XDS    .        ? 3 
phasing          PHASER .        ? 4 
# 
_cell.entry_id           7I1H 
_cell.length_a           68.810 
_cell.length_b           100.700 
_cell.length_c           105.350 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I1H 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
_exptl.entry_id          7I1H 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.70 
_exptl_crystal.density_percent_sol   54.47 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pdbx_details    
;0.2 M MIB (sodium malonate, imidazole, and boric acid in the molar ratios 2:3:3) pH 7.7, 23.5 % PEG 1500, 5 % DMSO, 1 mM DTT. Crystal seeds were used to ensure reproducible crystal growth.
;
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pH              7.7 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.pdbx_collection_date   2022-12-06 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9184 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.pdbx_wavelength_list        0.9184 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'BESSY BEAMLINE 14.1' 
_diffrn_source.pdbx_synchrotron_site       BESSY 
_diffrn_source.pdbx_synchrotron_beamline   14.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I1H 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             46.68 
_reflns.d_resolution_high            1.98 
_reflns.number_obs                   51345 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.14300000000000002 
_reflns.pdbx_netI_over_sigmaI        8.73 
_reflns.pdbx_Rrim_I_all              0.157 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     293700 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
1 1 1.98 2.1  45083 8181 1.3159999999999998   99.8  1.23  1.455               0.465              ? ? ? ? 
1 2 2.10 2.25 44285 7700 0.8270000000000001   99.9  2.06  0.91                0.675              ? ? ? ? 
1 3 2.25 2.43 41595 7187 0.537                100.0 3.16  0.591               0.855              ? ? ? ? 
1 4 2.43 2.66 36910 6658 0.34                 99.8  4.76  0.375               0.9279999999999999 ? ? ? ? 
1 5 2.66 2.97 37134 6046 0.21600000000000003  99.9  7.80  0.23600000000000002 0.975              ? ? ? ? 
1 6 2.97 3.43 31529 5336 0.126                99.9  12.93 0.139               0.991              ? ? ? ? 
1 7 3.43 4.2  25081 4560 0.07400000000000001  99.5  20.36 0.08199999999999999 0.996              ? ? ? ? 
1 8 4.20 5.91 20869 3582 0.055999999999999994 99.9  27.57 0.062               0.997              ? ? ? ? 
1 9 5.91 ?    11214 2095 0.044000000000000004 98.8  28.80 0.048               0.998              ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7I1H 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     49245 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             46.68 
_refine.ls_d_res_high                            1.98 
_refine.ls_percent_reflns_obs                    99.80 
_refine.ls_R_factor_obs                          0.22176 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.22028 
_refine.ls_R_factor_R_free                       0.25649 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.1 
_refine.ls_number_reflns_R_free                  2100 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.950 
_refine.correlation_coeff_Fo_to_Fc_free          0.930 
_refine.B_iso_mean                               35.723 
_refine.aniso_B[1][1]                            -0.96 
_refine.aniso_B[2][2]                            0.70 
_refine.aniso_B[3][3]                            0.26 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.180 
_refine.pdbx_overall_ESU_R_Free                  0.162 
_refine.overall_SU_ML                            0.155 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             5.996 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        4658 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.number_atoms_solvent             84 
_refine_hist.number_atoms_total               4767 
_refine_hist.d_res_high                       1.98 
_refine_hist.d_res_low                        46.68 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.007  0.011  ? 5074  'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.016  ? 4522  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.665  1.800  ? 6694  'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.561  1.735  ? 10402 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.206  5.000  ? 630   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       19.423 7.308  ? 26    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.595 10.000 ? 781   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.078  0.200  ? 751   'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 5923  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 1172  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_it                  2.828  3.403  ? 2561  'X-RAY DIFFRACTION' ? 
r_mcbond_other               2.825  3.404  ? 2561  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.219  6.126  ? 3124  'X-RAY DIFFRACTION' ? 
r_mcangle_other              4.219  6.128  ? 3125  'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.730  3.844  ? 2513  'X-RAY DIFFRACTION' ? 
r_scbond_other               3.730  3.845  ? 2514  'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_other              5.678  6.882  ? 3569  'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       7.396  33.57  ? 5029  'X-RAY DIFFRACTION' ? 
r_long_range_B_other         7.395  33.58  ? 5023  'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.983 
_refine_ls_shell.d_res_low                        2.034 
_refine_ls_shell.number_reflns_R_work             3576 
_refine_ls_shell.R_factor_R_work                  0.335 
_refine_ls_shell.percent_reflns_obs               99.57 
_refine_ls_shell.R_factor_R_free                  0.333 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             152 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7I1H 
_struct.title                     
;PanDDA analysis group deposition -- Main Protease (SARS-CoV-2) in complex with fragment G10 from the F2X-Entry Screen in orthorhombic space group
;
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I1H 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SARS-CoV-2, fragment screen, main protease, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
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 7I1H A 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
2 1 7I1H B 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              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)' 3480  ? 
1 MORE         -16   ? 
1 'SSA (A^2)'  26610 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 THR A 45  ? MET A 49  ? THR A 45  MET A 49  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? PHE A 66  ? SER A 62  PHE A 66  5 ? 5  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? MET A 235 ? THR A 226 MET A 235 1 ? 10 
HELX_P HELX_P8  AA8 LYS A 236 ? ASN A 238 ? LYS A 236 ASN A 238 5 ? 3  
HELX_P HELX_P9  AA9 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P10 AB1 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P11 AB2 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P12 AB3 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
HELX_P HELX_P13 AB4 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P14 AB5 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P15 AB6 THR B 45  ? ASN B 51  ? THR B 45  ASN B 51  1 ? 7  
HELX_P HELX_P16 AB7 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P17 AB8 SER B 62  ? PHE B 66  ? SER B 62  PHE B 66  5 ? 5  
HELX_P HELX_P18 AB9 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P19 AC1 THR B 226 ? TYR B 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P20 AC2 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P21 AC3 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P22 AC4 ALA B 260 ? ASN B 274 ? ALA B 260 ASN B 274 1 ? 15 
HELX_P HELX_P23 AC5 THR B 292 ? SER B 301 ? THR B 292 SER B 301 1 ? 10 
# 
_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 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 LEU A 67  ? ALA A 70  ? LEU A 67  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
AA4 1 VAL B 73  ? LEU B 75  ? VAL B 73  LEU B 75  
AA4 2 LEU B 67  ? ALA B 70  ? LEU B 67  ALA B 70  
AA4 3 MET B 17  ? CYS B 22  ? MET B 17  CYS B 22  
AA4 4 THR B 25  ? LEU B 32  ? THR B 25  LEU B 32  
AA4 5 VAL B 35  ? PRO B 39  ? VAL B 35  PRO B 39  
AA4 6 VAL B 86  ? VAL B 91  ? VAL B 86  VAL B 91  
AA4 7 VAL B 77  ? GLN B 83  ? VAL B 77  GLN B 83  
AA5 1 TYR B 101 ? PHE B 103 ? TYR B 101 PHE B 103 
AA5 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA5 3 VAL B 148 ? ASP B 153 ? VAL B 148 ASP B 153 
AA5 4 THR B 111 ? TYR B 118 ? THR B 111 TYR B 118 
AA5 5 SER B 121 ? ALA B 129 ? SER B 121 ALA B 129 
AA6 1 TYR B 101 ? PHE B 103 ? TYR B 101 PHE B 103 
AA6 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA6 3 HIS B 172 ? THR B 175 ? 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 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O GLN A 69  ? O GLN A 69  N GLN A 19  ? N GLN A 19  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 32  ? N LEU A 32  O VAL A 35  ? O VAL A 35  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 90  ? O LYS A 90  N GLY A 79  ? N GLY A 79  
AA2 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
AA4 1 2 O LEU B 75  ? O LEU B 75  N VAL B 68  ? N VAL B 68  
AA4 2 3 O LEU B 67  ? O LEU B 67  N THR B 21  ? N THR B 21  
AA4 3 4 N VAL B 20  ? N VAL B 20  O LEU B 27  ? O LEU B 27  
AA4 4 5 N LEU B 30  ? N LEU B 30  O TYR B 37  ? O TYR B 37  
AA4 5 6 N VAL B 36  ? N VAL B 36  O LEU B 89  ? O LEU B 89  
AA4 6 7 O LYS B 88  ? O LYS B 88  N SER B 81  ? N SER B 81  
AA5 1 2 N LYS B 102 ? N LYS B 102 O PHE B 159 ? O PHE B 159 
AA5 2 3 O CYS B 156 ? O CYS B 156 N ASP B 153 ? N ASP B 153 
AA5 3 4 O PHE B 150 ? O PHE B 150 N SER B 113 ? N SER B 113 
AA5 4 5 N ALA B 116 ? N ALA B 116 O SER B 123 ? O SER B 123 
AA6 1 2 N LYS B 102 ? N LYS B 102 O PHE B 159 ? O PHE B 159 
AA6 2 3 N MET B 165 ? N MET B 165 O ALA B 173 ? O ALA B 173 
# 
_pdbx_entry_details.entry_id                   7I1H 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 4   ? ? CZ A ARG 4   ? ? NH2 A ARG 4   ? ? 116.87 120.30 -3.43  0.50 N 
2 1 CG A MET 49  ? ? SD A MET 49  ? ? CE  A MET 49  ? ? 112.88 100.20 12.68  1.60 N 
3 1 CB A ASP 153 ? ? CA A ASP 153 ? ? C   A ASP 153 ? ? 125.46 110.40 15.06  2.00 N 
4 1 N  B GLN 127 ? ? CA B GLN 127 ? ? CB  B GLN 127 ? ? 98.27  110.60 -12.33 1.80 N 
5 1 CG B MET 264 ? ? SD B MET 264 ? ? CE  B MET 264 ? ? 89.54  100.20 -10.66 1.60 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  ? ? 44.66   -123.39 
2  1 THR A 45  ? ? -114.49 -169.46 
3  1 GLU A 47  ? ? -96.75  35.98   
4  1 ASN A 84  ? ? 54.89   -119.68 
5  1 ASP B 33  ? ? 52.78   -131.45 
6  1 ASN B 51  ? ? -155.06 74.13   
7  1 ASN B 84  ? ? 49.34   -125.60 
8  1 TYR B 154 ? ? 66.41   -101.90 
9  1 ARG B 217 ? ? -144.00 -2.28   
10 1 ARG B 279 ? ? -45.23  -168.09 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 4 ? ? 0.080 'SIDE CHAIN' 
2 1 ARG B 4 ? ? 0.137 'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 302 ? A GLY 302 
2  1 Y 1 A VAL 303 ? A VAL 303 
3  1 Y 1 A THR 304 ? A THR 304 
4  1 Y 1 A PHE 305 ? A PHE 305 
5  1 Y 1 A GLN 306 ? A GLN 306 
6  1 Y 1 B GLY 302 ? B GLY 302 
7  1 Y 1 B VAL 303 ? B VAL 303 
8  1 Y 1 B THR 304 ? B THR 304 
9  1 Y 1 B PHE 305 ? B PHE 305 
10 1 Y 1 B GLN 306 ? B GLN 306 
# 
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 
A1BVY C4   C  Y N 1   
A1BVY C5   C  Y N 2   
A1BVY C6   C  Y N 3   
A1BVY C7   C  Y N 4   
A1BVY N1   N  Y N 5   
A1BVY N2   N  Y N 6   
A1BVY C3   C  Y N 7   
A1BVY N3   N  Y N 8   
A1BVY C1   C  Y N 9   
A1BVY N4   N  Y N 10  
A1BVY C2   C  Y N 11  
A1BVY H1   H  N N 12  
A1BVY H2   H  N N 13  
A1BVY H3   H  N N 14  
A1BVY H4   H  N N 15  
A1BVY H5   H  N N 16  
A1BVY H6   H  N N 17  
ALA   N    N  N N 18  
ALA   CA   C  N S 19  
ALA   C    C  N N 20  
ALA   O    O  N N 21  
ALA   CB   C  N N 22  
ALA   OXT  O  N N 23  
ALA   H    H  N N 24  
ALA   H2   H  N N 25  
ALA   HA   H  N N 26  
ALA   HB1  H  N N 27  
ALA   HB2  H  N N 28  
ALA   HB3  H  N N 29  
ALA   HXT  H  N N 30  
ARG   N    N  N N 31  
ARG   CA   C  N S 32  
ARG   C    C  N N 33  
ARG   O    O  N N 34  
ARG   CB   C  N N 35  
ARG   CG   C  N N 36  
ARG   CD   C  N N 37  
ARG   NE   N  N N 38  
ARG   CZ   C  N N 39  
ARG   NH1  N  N N 40  
ARG   NH2  N  N N 41  
ARG   OXT  O  N N 42  
ARG   H    H  N N 43  
ARG   H2   H  N N 44  
ARG   HA   H  N N 45  
ARG   HB2  H  N N 46  
ARG   HB3  H  N N 47  
ARG   HG2  H  N N 48  
ARG   HG3  H  N N 49  
ARG   HD2  H  N N 50  
ARG   HD3  H  N N 51  
ARG   HE   H  N N 52  
ARG   HH11 H  N N 53  
ARG   HH12 H  N N 54  
ARG   HH21 H  N N 55  
ARG   HH22 H  N N 56  
ARG   HXT  H  N N 57  
ASN   N    N  N N 58  
ASN   CA   C  N S 59  
ASN   C    C  N N 60  
ASN   O    O  N N 61  
ASN   CB   C  N N 62  
ASN   CG   C  N N 63  
ASN   OD1  O  N N 64  
ASN   ND2  N  N N 65  
ASN   OXT  O  N N 66  
ASN   H    H  N N 67  
ASN   H2   H  N N 68  
ASN   HA   H  N N 69  
ASN   HB2  H  N N 70  
ASN   HB3  H  N N 71  
ASN   HD21 H  N N 72  
ASN   HD22 H  N N 73  
ASN   HXT  H  N N 74  
ASP   N    N  N N 75  
ASP   CA   C  N S 76  
ASP   C    C  N N 77  
ASP   O    O  N N 78  
ASP   CB   C  N N 79  
ASP   CG   C  N N 80  
ASP   OD1  O  N N 81  
ASP   OD2  O  N N 82  
ASP   OXT  O  N N 83  
ASP   H    H  N N 84  
ASP   H2   H  N N 85  
ASP   HA   H  N N 86  
ASP   HB2  H  N N 87  
ASP   HB3  H  N N 88  
ASP   HD2  H  N N 89  
ASP   HXT  H  N N 90  
CL    CL   CL N N 91  
CYS   N    N  N N 92  
CYS   CA   C  N R 93  
CYS   C    C  N N 94  
CYS   O    O  N N 95  
CYS   CB   C  N N 96  
CYS   SG   S  N N 97  
CYS   OXT  O  N N 98  
CYS   H    H  N N 99  
CYS   H2   H  N N 100 
CYS   HA   H  N N 101 
CYS   HB2  H  N N 102 
CYS   HB3  H  N N 103 
CYS   HG   H  N N 104 
CYS   HXT  H  N N 105 
DMS   S    S  N N 106 
DMS   O    O  N N 107 
DMS   C1   C  N N 108 
DMS   C2   C  N N 109 
DMS   H11  H  N N 110 
DMS   H12  H  N N 111 
DMS   H13  H  N N 112 
DMS   H21  H  N N 113 
DMS   H22  H  N N 114 
DMS   H23  H  N N 115 
GLN   N    N  N N 116 
GLN   CA   C  N S 117 
GLN   C    C  N N 118 
GLN   O    O  N N 119 
GLN   CB   C  N N 120 
GLN   CG   C  N N 121 
GLN   CD   C  N N 122 
GLN   OE1  O  N N 123 
GLN   NE2  N  N N 124 
GLN   OXT  O  N N 125 
GLN   H    H  N N 126 
GLN   H2   H  N N 127 
GLN   HA   H  N N 128 
GLN   HB2  H  N N 129 
GLN   HB3  H  N N 130 
GLN   HG2  H  N N 131 
GLN   HG3  H  N N 132 
GLN   HE21 H  N N 133 
GLN   HE22 H  N N 134 
GLN   HXT  H  N N 135 
GLU   N    N  N N 136 
GLU   CA   C  N S 137 
GLU   C    C  N N 138 
GLU   O    O  N N 139 
GLU   CB   C  N N 140 
GLU   CG   C  N N 141 
GLU   CD   C  N N 142 
GLU   OE1  O  N N 143 
GLU   OE2  O  N N 144 
GLU   OXT  O  N N 145 
GLU   H    H  N N 146 
GLU   H2   H  N N 147 
GLU   HA   H  N N 148 
GLU   HB2  H  N N 149 
GLU   HB3  H  N N 150 
GLU   HG2  H  N N 151 
GLU   HG3  H  N N 152 
GLU   HE2  H  N N 153 
GLU   HXT  H  N N 154 
GLY   N    N  N N 155 
GLY   CA   C  N N 156 
GLY   C    C  N N 157 
GLY   O    O  N N 158 
GLY   OXT  O  N N 159 
GLY   H    H  N N 160 
GLY   H2   H  N N 161 
GLY   HA2  H  N N 162 
GLY   HA3  H  N N 163 
GLY   HXT  H  N N 164 
HIS   N    N  N N 165 
HIS   CA   C  N S 166 
HIS   C    C  N N 167 
HIS   O    O  N N 168 
HIS   CB   C  N N 169 
HIS   CG   C  Y N 170 
HIS   ND1  N  Y N 171 
HIS   CD2  C  Y N 172 
HIS   CE1  C  Y N 173 
HIS   NE2  N  Y N 174 
HIS   OXT  O  N N 175 
HIS   H    H  N N 176 
HIS   H2   H  N N 177 
HIS   HA   H  N N 178 
HIS   HB2  H  N N 179 
HIS   HB3  H  N N 180 
HIS   HD1  H  N N 181 
HIS   HD2  H  N N 182 
HIS   HE1  H  N N 183 
HIS   HE2  H  N N 184 
HIS   HXT  H  N N 185 
HOH   O    O  N N 186 
HOH   H1   H  N N 187 
HOH   H2   H  N N 188 
ILE   N    N  N N 189 
ILE   CA   C  N S 190 
ILE   C    C  N N 191 
ILE   O    O  N N 192 
ILE   CB   C  N S 193 
ILE   CG1  C  N N 194 
ILE   CG2  C  N N 195 
ILE   CD1  C  N N 196 
ILE   OXT  O  N N 197 
ILE   H    H  N N 198 
ILE   H2   H  N N 199 
ILE   HA   H  N N 200 
ILE   HB   H  N N 201 
ILE   HG12 H  N N 202 
ILE   HG13 H  N N 203 
ILE   HG21 H  N N 204 
ILE   HG22 H  N N 205 
ILE   HG23 H  N N 206 
ILE   HD11 H  N N 207 
ILE   HD12 H  N N 208 
ILE   HD13 H  N N 209 
ILE   HXT  H  N N 210 
LEU   N    N  N N 211 
LEU   CA   C  N S 212 
LEU   C    C  N N 213 
LEU   O    O  N N 214 
LEU   CB   C  N N 215 
LEU   CG   C  N N 216 
LEU   CD1  C  N N 217 
LEU   CD2  C  N N 218 
LEU   OXT  O  N N 219 
LEU   H    H  N N 220 
LEU   H2   H  N N 221 
LEU   HA   H  N N 222 
LEU   HB2  H  N N 223 
LEU   HB3  H  N N 224 
LEU   HG   H  N N 225 
LEU   HD11 H  N N 226 
LEU   HD12 H  N N 227 
LEU   HD13 H  N N 228 
LEU   HD21 H  N N 229 
LEU   HD22 H  N N 230 
LEU   HD23 H  N N 231 
LEU   HXT  H  N N 232 
LYS   N    N  N N 233 
LYS   CA   C  N S 234 
LYS   C    C  N N 235 
LYS   O    O  N N 236 
LYS   CB   C  N N 237 
LYS   CG   C  N N 238 
LYS   CD   C  N N 239 
LYS   CE   C  N N 240 
LYS   NZ   N  N N 241 
LYS   OXT  O  N N 242 
LYS   H    H  N N 243 
LYS   H2   H  N N 244 
LYS   HA   H  N N 245 
LYS   HB2  H  N N 246 
LYS   HB3  H  N N 247 
LYS   HG2  H  N N 248 
LYS   HG3  H  N N 249 
LYS   HD2  H  N N 250 
LYS   HD3  H  N N 251 
LYS   HE2  H  N N 252 
LYS   HE3  H  N N 253 
LYS   HZ1  H  N N 254 
LYS   HZ2  H  N N 255 
LYS   HZ3  H  N N 256 
LYS   HXT  H  N N 257 
MET   N    N  N N 258 
MET   CA   C  N S 259 
MET   C    C  N N 260 
MET   O    O  N N 261 
MET   CB   C  N N 262 
MET   CG   C  N N 263 
MET   SD   S  N N 264 
MET   CE   C  N N 265 
MET   OXT  O  N N 266 
MET   H    H  N N 267 
MET   H2   H  N N 268 
MET   HA   H  N N 269 
MET   HB2  H  N N 270 
MET   HB3  H  N N 271 
MET   HG2  H  N N 272 
MET   HG3  H  N N 273 
MET   HE1  H  N N 274 
MET   HE2  H  N N 275 
MET   HE3  H  N N 276 
MET   HXT  H  N N 277 
PHE   N    N  N N 278 
PHE   CA   C  N S 279 
PHE   C    C  N N 280 
PHE   O    O  N N 281 
PHE   CB   C  N N 282 
PHE   CG   C  Y N 283 
PHE   CD1  C  Y N 284 
PHE   CD2  C  Y N 285 
PHE   CE1  C  Y N 286 
PHE   CE2  C  Y N 287 
PHE   CZ   C  Y N 288 
PHE   OXT  O  N N 289 
PHE   H    H  N N 290 
PHE   H2   H  N N 291 
PHE   HA   H  N N 292 
PHE   HB2  H  N N 293 
PHE   HB3  H  N N 294 
PHE   HD1  H  N N 295 
PHE   HD2  H  N N 296 
PHE   HE1  H  N N 297 
PHE   HE2  H  N N 298 
PHE   HZ   H  N N 299 
PHE   HXT  H  N N 300 
PRO   N    N  N N 301 
PRO   CA   C  N S 302 
PRO   C    C  N N 303 
PRO   O    O  N N 304 
PRO   CB   C  N N 305 
PRO   CG   C  N N 306 
PRO   CD   C  N N 307 
PRO   OXT  O  N N 308 
PRO   H    H  N N 309 
PRO   HA   H  N N 310 
PRO   HB2  H  N N 311 
PRO   HB3  H  N N 312 
PRO   HG2  H  N N 313 
PRO   HG3  H  N N 314 
PRO   HD2  H  N N 315 
PRO   HD3  H  N N 316 
PRO   HXT  H  N N 317 
SER   N    N  N N 318 
SER   CA   C  N S 319 
SER   C    C  N N 320 
SER   O    O  N N 321 
SER   CB   C  N N 322 
SER   OG   O  N N 323 
SER   OXT  O  N N 324 
SER   H    H  N N 325 
SER   H2   H  N N 326 
SER   HA   H  N N 327 
SER   HB2  H  N N 328 
SER   HB3  H  N N 329 
SER   HG   H  N N 330 
SER   HXT  H  N N 331 
THR   N    N  N N 332 
THR   CA   C  N S 333 
THR   C    C  N N 334 
THR   O    O  N N 335 
THR   CB   C  N R 336 
THR   OG1  O  N N 337 
THR   CG2  C  N N 338 
THR   OXT  O  N N 339 
THR   H    H  N N 340 
THR   H2   H  N N 341 
THR   HA   H  N N 342 
THR   HB   H  N N 343 
THR   HG1  H  N N 344 
THR   HG21 H  N N 345 
THR   HG22 H  N N 346 
THR   HG23 H  N N 347 
THR   HXT  H  N N 348 
TRP   N    N  N N 349 
TRP   CA   C  N S 350 
TRP   C    C  N N 351 
TRP   O    O  N N 352 
TRP   CB   C  N N 353 
TRP   CG   C  Y N 354 
TRP   CD1  C  Y N 355 
TRP   CD2  C  Y N 356 
TRP   NE1  N  Y N 357 
TRP   CE2  C  Y N 358 
TRP   CE3  C  Y N 359 
TRP   CZ2  C  Y N 360 
TRP   CZ3  C  Y N 361 
TRP   CH2  C  Y N 362 
TRP   OXT  O  N N 363 
TRP   H    H  N N 364 
TRP   H2   H  N N 365 
TRP   HA   H  N N 366 
TRP   HB2  H  N N 367 
TRP   HB3  H  N N 368 
TRP   HD1  H  N N 369 
TRP   HE1  H  N N 370 
TRP   HE3  H  N N 371 
TRP   HZ2  H  N N 372 
TRP   HZ3  H  N N 373 
TRP   HH2  H  N N 374 
TRP   HXT  H  N N 375 
TYR   N    N  N N 376 
TYR   CA   C  N S 377 
TYR   C    C  N N 378 
TYR   O    O  N N 379 
TYR   CB   C  N N 380 
TYR   CG   C  Y N 381 
TYR   CD1  C  Y N 382 
TYR   CD2  C  Y N 383 
TYR   CE1  C  Y N 384 
TYR   CE2  C  Y N 385 
TYR   CZ   C  Y N 386 
TYR   OH   O  N N 387 
TYR   OXT  O  N N 388 
TYR   H    H  N N 389 
TYR   H2   H  N N 390 
TYR   HA   H  N N 391 
TYR   HB2  H  N N 392 
TYR   HB3  H  N N 393 
TYR   HD1  H  N N 394 
TYR   HD2  H  N N 395 
TYR   HE1  H  N N 396 
TYR   HE2  H  N N 397 
TYR   HH   H  N N 398 
TYR   HXT  H  N N 399 
VAL   N    N  N N 400 
VAL   CA   C  N S 401 
VAL   C    C  N N 402 
VAL   O    O  N N 403 
VAL   CB   C  N N 404 
VAL   CG1  C  N N 405 
VAL   CG2  C  N N 406 
VAL   OXT  O  N N 407 
VAL   H    H  N N 408 
VAL   H2   H  N N 409 
VAL   HA   H  N N 410 
VAL   HB   H  N N 411 
VAL   HG11 H  N N 412 
VAL   HG12 H  N N 413 
VAL   HG13 H  N N 414 
VAL   HG21 H  N N 415 
VAL   HG22 H  N N 416 
VAL   HG23 H  N N 417 
VAL   HXT  H  N N 418 
# 
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 
A1BVY C5  C4   doub Y N 1   
A1BVY C5  C6   sing Y N 2   
A1BVY C4  C3   sing Y N 3   
A1BVY C6  C7   doub Y N 4   
A1BVY C3  C2   doub Y N 5   
A1BVY C7  C2   sing Y N 6   
A1BVY C2  N4   sing N N 7   
A1BVY N4  C1   sing Y N 8   
A1BVY N4  N3   sing Y N 9   
A1BVY C1  N1   doub Y N 10  
A1BVY N3  N2   doub Y N 11  
A1BVY N1  N2   sing Y N 12  
A1BVY C4  H1   sing N N 13  
A1BVY C5  H2   sing N N 14  
A1BVY C6  H3   sing N N 15  
A1BVY C7  H4   sing N N 16  
A1BVY C3  H5   sing N N 17  
A1BVY C1  H6   sing N N 18  
ALA   N   CA   sing N N 19  
ALA   N   H    sing N N 20  
ALA   N   H2   sing N N 21  
ALA   CA  C    sing N N 22  
ALA   CA  CB   sing N N 23  
ALA   CA  HA   sing N N 24  
ALA   C   O    doub N N 25  
ALA   C   OXT  sing N N 26  
ALA   CB  HB1  sing N N 27  
ALA   CB  HB2  sing N N 28  
ALA   CB  HB3  sing N N 29  
ALA   OXT HXT  sing N N 30  
ARG   N   CA   sing N N 31  
ARG   N   H    sing N N 32  
ARG   N   H2   sing N N 33  
ARG   CA  C    sing N N 34  
ARG   CA  CB   sing N N 35  
ARG   CA  HA   sing N N 36  
ARG   C   O    doub N N 37  
ARG   C   OXT  sing N N 38  
ARG   CB  CG   sing N N 39  
ARG   CB  HB2  sing N N 40  
ARG   CB  HB3  sing N N 41  
ARG   CG  CD   sing N N 42  
ARG   CG  HG2  sing N N 43  
ARG   CG  HG3  sing N N 44  
ARG   CD  NE   sing N N 45  
ARG   CD  HD2  sing N N 46  
ARG   CD  HD3  sing N N 47  
ARG   NE  CZ   sing N N 48  
ARG   NE  HE   sing N N 49  
ARG   CZ  NH1  sing N N 50  
ARG   CZ  NH2  doub N N 51  
ARG   NH1 HH11 sing N N 52  
ARG   NH1 HH12 sing N N 53  
ARG   NH2 HH21 sing N N 54  
ARG   NH2 HH22 sing N N 55  
ARG   OXT HXT  sing N N 56  
ASN   N   CA   sing N N 57  
ASN   N   H    sing N N 58  
ASN   N   H2   sing N N 59  
ASN   CA  C    sing N N 60  
ASN   CA  CB   sing N N 61  
ASN   CA  HA   sing N N 62  
ASN   C   O    doub N N 63  
ASN   C   OXT  sing N N 64  
ASN   CB  CG   sing N N 65  
ASN   CB  HB2  sing N N 66  
ASN   CB  HB3  sing N N 67  
ASN   CG  OD1  doub N N 68  
ASN   CG  ND2  sing N N 69  
ASN   ND2 HD21 sing N N 70  
ASN   ND2 HD22 sing N N 71  
ASN   OXT HXT  sing N N 72  
ASP   N   CA   sing N N 73  
ASP   N   H    sing N N 74  
ASP   N   H2   sing N N 75  
ASP   CA  C    sing N N 76  
ASP   CA  CB   sing N N 77  
ASP   CA  HA   sing N N 78  
ASP   C   O    doub N N 79  
ASP   C   OXT  sing N N 80  
ASP   CB  CG   sing N N 81  
ASP   CB  HB2  sing N N 82  
ASP   CB  HB3  sing N N 83  
ASP   CG  OD1  doub N N 84  
ASP   CG  OD2  sing N N 85  
ASP   OD2 HD2  sing N N 86  
ASP   OXT HXT  sing N N 87  
CYS   N   CA   sing N N 88  
CYS   N   H    sing N N 89  
CYS   N   H2   sing N N 90  
CYS   CA  C    sing N N 91  
CYS   CA  CB   sing N N 92  
CYS   CA  HA   sing N N 93  
CYS   C   O    doub N N 94  
CYS   C   OXT  sing N N 95  
CYS   CB  SG   sing N N 96  
CYS   CB  HB2  sing N N 97  
CYS   CB  HB3  sing N N 98  
CYS   SG  HG   sing N N 99  
CYS   OXT HXT  sing N N 100 
DMS   S   O    doub N N 101 
DMS   S   C1   sing N N 102 
DMS   S   C2   sing N N 103 
DMS   C1  H11  sing N N 104 
DMS   C1  H12  sing N N 105 
DMS   C1  H13  sing N N 106 
DMS   C2  H21  sing N N 107 
DMS   C2  H22  sing N N 108 
DMS   C2  H23  sing N N 109 
GLN   N   CA   sing N N 110 
GLN   N   H    sing N N 111 
GLN   N   H2   sing N N 112 
GLN   CA  C    sing N N 113 
GLN   CA  CB   sing N N 114 
GLN   CA  HA   sing N N 115 
GLN   C   O    doub N N 116 
GLN   C   OXT  sing N N 117 
GLN   CB  CG   sing N N 118 
GLN   CB  HB2  sing N N 119 
GLN   CB  HB3  sing N N 120 
GLN   CG  CD   sing N N 121 
GLN   CG  HG2  sing N N 122 
GLN   CG  HG3  sing N N 123 
GLN   CD  OE1  doub N N 124 
GLN   CD  NE2  sing N N 125 
GLN   NE2 HE21 sing N N 126 
GLN   NE2 HE22 sing N N 127 
GLN   OXT HXT  sing N N 128 
GLU   N   CA   sing N N 129 
GLU   N   H    sing N N 130 
GLU   N   H2   sing N N 131 
GLU   CA  C    sing N N 132 
GLU   CA  CB   sing N N 133 
GLU   CA  HA   sing N N 134 
GLU   C   O    doub N N 135 
GLU   C   OXT  sing N N 136 
GLU   CB  CG   sing N N 137 
GLU   CB  HB2  sing N N 138 
GLU   CB  HB3  sing N N 139 
GLU   CG  CD   sing N N 140 
GLU   CG  HG2  sing N N 141 
GLU   CG  HG3  sing N N 142 
GLU   CD  OE1  doub N N 143 
GLU   CD  OE2  sing N N 144 
GLU   OE2 HE2  sing N N 145 
GLU   OXT HXT  sing N N 146 
GLY   N   CA   sing N N 147 
GLY   N   H    sing N N 148 
GLY   N   H2   sing N N 149 
GLY   CA  C    sing N N 150 
GLY   CA  HA2  sing N N 151 
GLY   CA  HA3  sing N N 152 
GLY   C   O    doub N N 153 
GLY   C   OXT  sing N N 154 
GLY   OXT HXT  sing N N 155 
HIS   N   CA   sing N N 156 
HIS   N   H    sing N N 157 
HIS   N   H2   sing N N 158 
HIS   CA  C    sing N N 159 
HIS   CA  CB   sing N N 160 
HIS   CA  HA   sing N N 161 
HIS   C   O    doub N N 162 
HIS   C   OXT  sing N N 163 
HIS   CB  CG   sing N N 164 
HIS   CB  HB2  sing N N 165 
HIS   CB  HB3  sing N N 166 
HIS   CG  ND1  sing Y N 167 
HIS   CG  CD2  doub Y N 168 
HIS   ND1 CE1  doub Y N 169 
HIS   ND1 HD1  sing N N 170 
HIS   CD2 NE2  sing Y N 171 
HIS   CD2 HD2  sing N N 172 
HIS   CE1 NE2  sing Y N 173 
HIS   CE1 HE1  sing N N 174 
HIS   NE2 HE2  sing N N 175 
HIS   OXT HXT  sing N N 176 
HOH   O   H1   sing N N 177 
HOH   O   H2   sing N N 178 
ILE   N   CA   sing N N 179 
ILE   N   H    sing N N 180 
ILE   N   H2   sing N N 181 
ILE   CA  C    sing N N 182 
ILE   CA  CB   sing N N 183 
ILE   CA  HA   sing N N 184 
ILE   C   O    doub N N 185 
ILE   C   OXT  sing N N 186 
ILE   CB  CG1  sing N N 187 
ILE   CB  CG2  sing N N 188 
ILE   CB  HB   sing N N 189 
ILE   CG1 CD1  sing N N 190 
ILE   CG1 HG12 sing N N 191 
ILE   CG1 HG13 sing N N 192 
ILE   CG2 HG21 sing N N 193 
ILE   CG2 HG22 sing N N 194 
ILE   CG2 HG23 sing N N 195 
ILE   CD1 HD11 sing N N 196 
ILE   CD1 HD12 sing N N 197 
ILE   CD1 HD13 sing N N 198 
ILE   OXT HXT  sing N N 199 
LEU   N   CA   sing N N 200 
LEU   N   H    sing N N 201 
LEU   N   H2   sing N N 202 
LEU   CA  C    sing N N 203 
LEU   CA  CB   sing N N 204 
LEU   CA  HA   sing N N 205 
LEU   C   O    doub N N 206 
LEU   C   OXT  sing N N 207 
LEU   CB  CG   sing N N 208 
LEU   CB  HB2  sing N N 209 
LEU   CB  HB3  sing N N 210 
LEU   CG  CD1  sing N N 211 
LEU   CG  CD2  sing N N 212 
LEU   CG  HG   sing N N 213 
LEU   CD1 HD11 sing N N 214 
LEU   CD1 HD12 sing N N 215 
LEU   CD1 HD13 sing N N 216 
LEU   CD2 HD21 sing N N 217 
LEU   CD2 HD22 sing N N 218 
LEU   CD2 HD23 sing N N 219 
LEU   OXT HXT  sing N N 220 
LYS   N   CA   sing N N 221 
LYS   N   H    sing N N 222 
LYS   N   H2   sing N N 223 
LYS   CA  C    sing N N 224 
LYS   CA  CB   sing N N 225 
LYS   CA  HA   sing N N 226 
LYS   C   O    doub N N 227 
LYS   C   OXT  sing N N 228 
LYS   CB  CG   sing N N 229 
LYS   CB  HB2  sing N N 230 
LYS   CB  HB3  sing N N 231 
LYS   CG  CD   sing N N 232 
LYS   CG  HG2  sing N N 233 
LYS   CG  HG3  sing N N 234 
LYS   CD  CE   sing N N 235 
LYS   CD  HD2  sing N N 236 
LYS   CD  HD3  sing N N 237 
LYS   CE  NZ   sing N N 238 
LYS   CE  HE2  sing N N 239 
LYS   CE  HE3  sing N N 240 
LYS   NZ  HZ1  sing N N 241 
LYS   NZ  HZ2  sing N N 242 
LYS   NZ  HZ3  sing N N 243 
LYS   OXT HXT  sing N N 244 
MET   N   CA   sing N N 245 
MET   N   H    sing N N 246 
MET   N   H2   sing N N 247 
MET   CA  C    sing N N 248 
MET   CA  CB   sing N N 249 
MET   CA  HA   sing N N 250 
MET   C   O    doub N N 251 
MET   C   OXT  sing N N 252 
MET   CB  CG   sing N N 253 
MET   CB  HB2  sing N N 254 
MET   CB  HB3  sing N N 255 
MET   CG  SD   sing N N 256 
MET   CG  HG2  sing N N 257 
MET   CG  HG3  sing N N 258 
MET   SD  CE   sing N N 259 
MET   CE  HE1  sing N N 260 
MET   CE  HE2  sing N N 261 
MET   CE  HE3  sing N N 262 
MET   OXT HXT  sing N N 263 
PHE   N   CA   sing N N 264 
PHE   N   H    sing N N 265 
PHE   N   H2   sing N N 266 
PHE   CA  C    sing N N 267 
PHE   CA  CB   sing N N 268 
PHE   CA  HA   sing N N 269 
PHE   C   O    doub N N 270 
PHE   C   OXT  sing N N 271 
PHE   CB  CG   sing N N 272 
PHE   CB  HB2  sing N N 273 
PHE   CB  HB3  sing N N 274 
PHE   CG  CD1  doub Y N 275 
PHE   CG  CD2  sing Y N 276 
PHE   CD1 CE1  sing Y N 277 
PHE   CD1 HD1  sing N N 278 
PHE   CD2 CE2  doub Y N 279 
PHE   CD2 HD2  sing N N 280 
PHE   CE1 CZ   doub Y N 281 
PHE   CE1 HE1  sing N N 282 
PHE   CE2 CZ   sing Y N 283 
PHE   CE2 HE2  sing N N 284 
PHE   CZ  HZ   sing N N 285 
PHE   OXT HXT  sing N N 286 
PRO   N   CA   sing N N 287 
PRO   N   CD   sing N N 288 
PRO   N   H    sing N N 289 
PRO   CA  C    sing N N 290 
PRO   CA  CB   sing N N 291 
PRO   CA  HA   sing N N 292 
PRO   C   O    doub N N 293 
PRO   C   OXT  sing N N 294 
PRO   CB  CG   sing N N 295 
PRO   CB  HB2  sing N N 296 
PRO   CB  HB3  sing N N 297 
PRO   CG  CD   sing N N 298 
PRO   CG  HG2  sing N N 299 
PRO   CG  HG3  sing N N 300 
PRO   CD  HD2  sing N N 301 
PRO   CD  HD3  sing N N 302 
PRO   OXT HXT  sing N N 303 
SER   N   CA   sing N N 304 
SER   N   H    sing N N 305 
SER   N   H2   sing N N 306 
SER   CA  C    sing N N 307 
SER   CA  CB   sing N N 308 
SER   CA  HA   sing N N 309 
SER   C   O    doub N N 310 
SER   C   OXT  sing N N 311 
SER   CB  OG   sing N N 312 
SER   CB  HB2  sing N N 313 
SER   CB  HB3  sing N N 314 
SER   OG  HG   sing N N 315 
SER   OXT HXT  sing N N 316 
THR   N   CA   sing N N 317 
THR   N   H    sing N N 318 
THR   N   H2   sing N N 319 
THR   CA  C    sing N N 320 
THR   CA  CB   sing N N 321 
THR   CA  HA   sing N N 322 
THR   C   O    doub N N 323 
THR   C   OXT  sing N N 324 
THR   CB  OG1  sing N N 325 
THR   CB  CG2  sing N N 326 
THR   CB  HB   sing N N 327 
THR   OG1 HG1  sing N N 328 
THR   CG2 HG21 sing N N 329 
THR   CG2 HG22 sing N N 330 
THR   CG2 HG23 sing N N 331 
THR   OXT HXT  sing N N 332 
TRP   N   CA   sing N N 333 
TRP   N   H    sing N N 334 
TRP   N   H2   sing N N 335 
TRP   CA  C    sing N N 336 
TRP   CA  CB   sing N N 337 
TRP   CA  HA   sing N N 338 
TRP   C   O    doub N N 339 
TRP   C   OXT  sing N N 340 
TRP   CB  CG   sing N N 341 
TRP   CB  HB2  sing N N 342 
TRP   CB  HB3  sing N N 343 
TRP   CG  CD1  doub Y N 344 
TRP   CG  CD2  sing Y N 345 
TRP   CD1 NE1  sing Y N 346 
TRP   CD1 HD1  sing N N 347 
TRP   CD2 CE2  doub Y N 348 
TRP   CD2 CE3  sing Y N 349 
TRP   NE1 CE2  sing Y N 350 
TRP   NE1 HE1  sing N N 351 
TRP   CE2 CZ2  sing Y N 352 
TRP   CE3 CZ3  doub Y N 353 
TRP   CE3 HE3  sing N N 354 
TRP   CZ2 CH2  doub Y N 355 
TRP   CZ2 HZ2  sing N N 356 
TRP   CZ3 CH2  sing Y N 357 
TRP   CZ3 HZ3  sing N N 358 
TRP   CH2 HH2  sing N N 359 
TRP   OXT HXT  sing N N 360 
TYR   N   CA   sing N N 361 
TYR   N   H    sing N N 362 
TYR   N   H2   sing N N 363 
TYR   CA  C    sing N N 364 
TYR   CA  CB   sing N N 365 
TYR   CA  HA   sing N N 366 
TYR   C   O    doub N N 367 
TYR   C   OXT  sing N N 368 
TYR   CB  CG   sing N N 369 
TYR   CB  HB2  sing N N 370 
TYR   CB  HB3  sing N N 371 
TYR   CG  CD1  doub Y N 372 
TYR   CG  CD2  sing Y N 373 
TYR   CD1 CE1  sing Y N 374 
TYR   CD1 HD1  sing N N 375 
TYR   CD2 CE2  doub Y N 376 
TYR   CD2 HD2  sing N N 377 
TYR   CE1 CZ   doub Y N 378 
TYR   CE1 HE1  sing N N 379 
TYR   CE2 CZ   sing Y N 380 
TYR   CE2 HE2  sing N N 381 
TYR   CZ  OH   sing N N 382 
TYR   OH  HH   sing N N 383 
TYR   OXT HXT  sing N N 384 
VAL   N   CA   sing N N 385 
VAL   N   H    sing N N 386 
VAL   N   H2   sing N N 387 
VAL   CA  C    sing N N 388 
VAL   CA  CB   sing N N 389 
VAL   CA  HA   sing N N 390 
VAL   C   O    doub N N 391 
VAL   C   OXT  sing N N 392 
VAL   CB  CG1  sing N N 393 
VAL   CB  CG2  sing N N 394 
VAL   CB  HB   sing N N 395 
VAL   CG1 HG11 sing N N 396 
VAL   CG1 HG12 sing N N 397 
VAL   CG1 HG13 sing N N 398 
VAL   CG2 HG21 sing N N 399 
VAL   CG2 HG22 sing N N 400 
VAL   CG2 HG23 sing N N 401 
VAL   OXT HXT  sing N N 402 
# 
_pdbx_audit_support.ordinal                1 
_pdbx_audit_support.funding_organization   'European Commission' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           871037 
# 
_pdbx_deposit_group.group_id            G_1002335 
_pdbx_deposit_group.group_description   
;Main Protease (SARS-CoV-2) complexed with fragments of the F2X-Entry Screen in the orthorhombic space group. PanDDA analysis of F2X-Entry Screen vs. the main protease of SARS-CoV-2, including auto-refined models with ligands placed according to PanDDA-map. The event maps are included in the mmcif and are the determining evidence for the ligands. 2Fo-Fc and Fo-Fc maps will be mostly not useful to consider here.
;
_pdbx_deposit_group.group_title         
;PanDDA analysis group deposition -- Main Protease (SARS-CoV-2) in complex with fragments from the F2X-Entry Screen in orthorhombic space group
;
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.accession_code   7BB2 
_pdbx_initial_refinement_model.source_name      PDB 
# 
_atom_sites.entry_id                    7I1H 
_atom_sites.fract_transf_matrix[1][1]   0.014533 
_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]   0.009930 
_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]   0.009492 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? -13.727 -9.845  -12.579 1.00 34.82  ? 1   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? -13.804 -9.121  -13.870 1.00 34.22  ? 1   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? -12.830 -7.941  -13.864 1.00 34.01  ? 1   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? -11.990 -7.840  -12.958 1.00 32.46  ? 1   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? -15.221 -8.699  -14.137 1.00 40.63  ? 1   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? -15.584 -7.617  -13.294 1.00 42.05  ? 1   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? -12.954 -7.078  -14.888 1.00 33.27  ? 2   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? -11.997 -6.024  -15.191 1.00 34.46  ? 2   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? -11.057 -6.493  -16.299 1.00 33.59  ? 2   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? -10.964 -7.685  -16.585 1.00 36.02  ? 2   GLY   A O   1 
ATOM   11   N  N   . PHE   A 1 3   ? -10.387 -5.552  -16.961 1.00 34.01  ? 3   PHE   A N   1 
ATOM   12   C  CA  . PHE   A 1 3   ? -9.434  -5.912  -17.997 1.00 32.89  ? 3   PHE   A CA  1 
ATOM   13   C  C   . PHE   A 1 3   ? -8.385  -4.802  -18.045 1.00 35.35  ? 3   PHE   A C   1 
ATOM   14   O  O   . PHE   A 1 3   ? -8.745  -3.628  -18.165 1.00 37.32  ? 3   PHE   A O   1 
ATOM   15   C  CB  . PHE   A 1 3   ? -10.181 -6.189  -19.314 1.00 33.44  ? 3   PHE   A CB  1 
ATOM   16   C  CG  . PHE   A 1 3   ? -9.372  -6.993  -20.319 1.00 33.14  ? 3   PHE   A CG  1 
ATOM   17   C  CD1 . PHE   A 1 3   ? -9.311  -8.382  -20.235 1.00 34.60  ? 3   PHE   A CD1 1 
ATOM   18   C  CD2 . PHE   A 1 3   ? -8.629  -6.355  -21.314 1.00 33.80  ? 3   PHE   A CD2 1 
ATOM   19   C  CE1 . PHE   A 1 3   ? -8.530  -9.113  -21.129 1.00 37.05  ? 3   PHE   A CE1 1 
ATOM   20   C  CE2 . PHE   A 1 3   ? -7.859  -7.086  -22.213 1.00 33.20  ? 3   PHE   A CE2 1 
ATOM   21   C  CZ  . PHE   A 1 3   ? -7.797  -8.461  -22.114 1.00 34.63  ? 3   PHE   A CZ  1 
ATOM   22   N  N   . ARG   A 1 4   ? -7.102  -5.194  -17.924 1.00 31.63  ? 4   ARG   A N   1 
ATOM   23   C  CA  . ARG   A 1 4   ? -5.981  -4.277  -17.787 1.00 29.71  ? 4   ARG   A CA  1 
ATOM   24   C  C   . ARG   A 1 4   ? -4.758  -4.818  -18.514 1.00 28.91  ? 4   ARG   A C   1 
ATOM   25   O  O   . ARG   A 1 4   ? -4.493  -6.030  -18.507 1.00 24.42  ? 4   ARG   A O   1 
ATOM   26   C  CB  . ARG   A 1 4   ? -5.561  -4.194  -16.314 1.00 33.08  ? 4   ARG   A CB  1 
ATOM   27   C  CG  . ARG   A 1 4   ? -6.555  -3.461  -15.432 1.00 33.25  ? 4   ARG   A CG  1 
ATOM   28   C  CD  . ARG   A 1 4   ? -6.529  -2.003  -15.851 1.00 37.32  ? 4   ARG   A CD  1 
ATOM   29   N  NE  . ARG   A 1 4   ? -6.315  -1.330  -14.577 1.00 40.80  ? 4   ARG   A NE  1 
ATOM   30   C  CZ  . ARG   A 1 4   ? -5.172  -0.862  -14.145 1.00 43.16  ? 4   ARG   A CZ  1 
ATOM   31   N  NH1 . ARG   A 1 4   ? -4.145  -0.619  -14.946 1.00 41.16  ? 4   ARG   A NH1 1 
ATOM   32   N  NH2 . ARG   A 1 4   ? -5.089  -0.589  -12.865 1.00 52.07  ? 4   ARG   A NH2 1 
ATOM   33   N  N   . LYS   A 1 5   ? -3.988  -3.893  -19.084 1.00 28.23  ? 5   LYS   A N   1 
ATOM   34   C  CA  . LYS   A 1 5   ? -2.601  -4.154  -19.446 1.00 33.85  ? 5   LYS   A CA  1 
ATOM   35   C  C   . LYS   A 1 5   ? -1.817  -4.706  -18.247 1.00 32.51  ? 5   LYS   A C   1 
ATOM   36   O  O   . LYS   A 1 5   ? -1.568  -4.005  -17.277 1.00 31.70  ? 5   LYS   A O   1 
ATOM   37   C  CB  . LYS   A 1 5   ? -1.974  -2.827  -19.868 1.00 33.82  ? 5   LYS   A CB  1 
ATOM   38   C  CG  . LYS   A 1 5   ? -2.078  -2.549  -21.313 1.00 38.84  ? 5   LYS   A CG  1 
ATOM   39   C  CD  . LYS   A 1 5   ? -1.004  -3.294  -22.083 1.00 44.05  ? 5   LYS   A CD  1 
ATOM   40   C  CE  . LYS   A 1 5   ? -1.236  -3.184  -23.544 1.00 47.58  ? 5   LYS   A CE  1 
ATOM   41   N  NZ  . LYS   A 1 5   ? -1.576  -1.806  -23.903 1.00 43.47  ? 5   LYS   A NZ  1 
ATOM   42   N  N   . MET   A 1 6   ? -1.436  -5.974  -18.290 1.00 30.70  ? 6   MET   A N   1 
ATOM   43   C  CA  . MET   A 1 6   ? -0.883  -6.623  -17.111 1.00 32.46  ? 6   MET   A CA  1 
ATOM   44   C  C   . MET   A 1 6   ? 0.485   -7.202  -17.498 1.00 30.10  ? 6   MET   A C   1 
ATOM   45   O  O   . MET   A 1 6   ? 0.590   -7.905  -18.504 1.00 29.82  ? 6   MET   A O   1 
ATOM   46   C  CB  . MET   A 1 6   ? -1.912  -7.674  -16.670 1.00 34.26  ? 6   MET   A CB  1 
ATOM   47   C  CG  . MET   A 1 6   ? -1.564  -8.521  -15.481 1.00 40.19  ? 6   MET   A CG  1 
ATOM   48   S  SD  . MET   A 1 6   ? -2.903  -9.656  -15.035 1.00 42.98  ? 6   MET   A SD  1 
ATOM   49   C  CE  . MET   A 1 6   ? -4.358  -8.661  -14.688 1.00 40.44  ? 6   MET   A CE  1 
ATOM   50   N  N   . ALA   A 1 7   ? 1.527   -6.876  -16.724 1.00 25.21  ? 7   ALA   A N   1 
ATOM   51   C  CA  . ALA   A 1 7   ? 2.872   -7.395  -16.966 1.00 25.80  ? 7   ALA   A CA  1 
ATOM   52   C  C   . ALA   A 1 7   ? 3.114   -8.662  -16.145 1.00 22.90  ? 7   ALA   A C   1 
ATOM   53   O  O   . ALA   A 1 7   ? 2.406   -8.904  -15.168 1.00 21.85  ? 7   ALA   A O   1 
ATOM   54   C  CB  . ALA   A 1 7   ? 3.920   -6.339  -16.629 1.00 25.75  ? 7   ALA   A CB  1 
ATOM   55   N  N   . PHE   A 1 8   ? 4.128   -9.451  -16.529 1.00 23.31  ? 8   PHE   A N   1 
ATOM   56   C  CA  . PHE   A 1 8   ? 4.547   -10.593 -15.722 1.00 25.13  ? 8   PHE   A CA  1 
ATOM   57   C  C   . PHE   A 1 8   ? 5.213   -10.115 -14.434 1.00 23.86  ? 8   PHE   A C   1 
ATOM   58   O  O   . PHE   A 1 8   ? 5.842   -9.057  -14.390 1.00 22.63  ? 8   PHE   A O   1 
ATOM   59   C  CB  . PHE   A 1 8   ? 5.442   -11.567 -16.496 1.00 25.64  ? 8   PHE   A CB  1 
ATOM   60   C  CG  . PHE   A 1 8   ? 4.623   -12.456 -17.428 1.00 27.27  ? 8   PHE   A CG  1 
ATOM   61   C  CD1 . PHE   A 1 8   ? 3.924   -13.548 -16.927 1.00 30.31  ? 8   PHE   A CD1 1 
ATOM   62   C  CD2 . PHE   A 1 8   ? 4.518   -12.167 -18.786 1.00 27.59  ? 8   PHE   A CD2 1 
ATOM   63   C  CE1 . PHE   A 1 8   ? 3.177   -14.356 -17.772 1.00 33.25  ? 8   PHE   A CE1 1 
ATOM   64   C  CE2 . PHE   A 1 8   ? 3.756   -12.962 -19.623 1.00 29.80  ? 8   PHE   A CE2 1 
ATOM   65   C  CZ  . PHE   A 1 8   ? 3.094   -14.057 -19.121 1.00 34.01  ? 8   PHE   A CZ  1 
ATOM   66   N  N   . PRO   A 1 9   ? 5.088   -10.882 -13.325 1.00 24.44  ? 9   PRO   A N   1 
ATOM   67   C  CA  . PRO   A 1 9   ? 5.896   -10.618 -12.129 1.00 26.25  ? 9   PRO   A CA  1 
ATOM   68   C  C   . PRO   A 1 9   ? 7.391   -10.627 -12.487 1.00 26.64  ? 9   PRO   A C   1 
ATOM   69   O  O   . PRO   A 1 9   ? 7.866   -11.571 -13.108 1.00 27.21  ? 9   PRO   A O   1 
ATOM   70   C  CB  . PRO   A 1 9   ? 5.519   -11.784 -11.186 1.00 27.63  ? 9   PRO   A CB  1 
ATOM   71   C  CG  . PRO   A 1 9   ? 4.160   -12.254 -11.704 1.00 28.71  ? 9   PRO   A CG  1 
ATOM   72   C  CD  . PRO   A 1 9   ? 4.239   -12.077 -13.210 1.00 26.32  ? 9   PRO   A CD  1 
ATOM   73   N  N   . SER   A 1 10  ? 8.123   -9.593  -12.064 1.00 24.03  ? 10  SER   A N   1 
ATOM   74   C  CA  . SER   A 1 10  ? 9.456   -9.312  -12.563 1.00 24.27  ? 10  SER   A CA  1 
ATOM   75   C  C   . SER   A 1 10  ? 10.589  -9.912  -11.720 1.00 25.70  ? 10  SER   A C   1 
ATOM   76   O  O   . SER   A 1 10  ? 11.747  -9.853  -12.154 1.00 26.30  ? 10  SER   A O   1 
ATOM   77   C  CB  . SER   A 1 10  ? 9.636   -7.812  -12.704 1.00 24.80  ? 10  SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 10  ? 9.603   -7.166  -11.433 1.00 23.95  ? 10  SER   A OG  1 
ATOM   79   N  N   . GLY   A 1 11  ? 10.287  -10.509 -10.557 1.00 24.09  ? 11  GLY   A N   1 
ATOM   80   C  CA  . GLY   A 1 11  ? 11.319  -10.929 -9.603  1.00 26.75  ? 11  GLY   A CA  1 
ATOM   81   C  C   . GLY   A 1 11  ? 12.441  -11.807 -10.188 1.00 25.17  ? 11  GLY   A C   1 
ATOM   82   O  O   . GLY   A 1 11  ? 13.625  -11.617 -9.895  1.00 22.01  ? 11  GLY   A O   1 
ATOM   83   N  N   . LYS   A 1 12  ? 12.077  -12.795 -11.004 1.00 25.65  ? 12  LYS   A N   1 
ATOM   84   C  CA  . LYS   A 1 12  ? 13.065  -13.716 -11.545 1.00 28.80  ? 12  LYS   A CA  1 
ATOM   85   C  C   . LYS   A 1 12  ? 14.039  -13.015 -12.501 1.00 30.15  ? 12  LYS   A C   1 
ATOM   86   O  O   . LYS   A 1 12  ? 15.160  -13.493 -12.669 1.00 33.69  ? 12  LYS   A O   1 
ATOM   87   C  CB  . LYS   A 1 12  ? 12.391  -14.861 -12.308 1.00 28.09  ? 12  LYS   A CB  1 
ATOM   88   C  CG  . LYS   A 1 12  ? 11.474  -15.776 -11.503 1.00 29.61  ? 12  LYS   A CG  1 
ATOM   89   C  CD  . LYS   A 1 12  ? 10.888  -16.885 -12.367 1.00 31.96  ? 12  LYS   A CD  1 
ATOM   90   C  CE  . LYS   A 1 12  ? 10.329  -18.029 -11.605 1.00 35.38  ? 12  LYS   A CE  1 
ATOM   91   N  NZ  . LYS   A 1 12  ? 9.186   -17.592 -10.809 1.00 37.49  ? 12  LYS   A NZ  1 
ATOM   92   N  N   . VAL   A 1 13  ? 13.609  -11.924 -13.163 1.00 27.58  ? 13  VAL   A N   1 
ATOM   93   C  CA  . VAL   A 1 13  ? 14.469  -11.186 -14.083 1.00 25.44  ? 13  VAL   A CA  1 
ATOM   94   C  C   . VAL   A 1 13  ? 15.344  -10.210 -13.308 1.00 24.56  ? 13  VAL   A C   1 
ATOM   95   O  O   . VAL   A 1 13  ? 16.494  -9.999  -13.677 1.00 23.66  ? 13  VAL   A O   1 
ATOM   96   C  CB  . VAL   A 1 13  ? 13.714  -10.440 -15.205 1.00 26.16  ? 13  VAL   A CB  1 
ATOM   97   C  CG1 . VAL   A 1 13  ? 14.661  -9.601  -16.068 1.00 25.10  ? 13  VAL   A CG1 1 
ATOM   98   C  CG2 . VAL   A 1 13  ? 12.921  -11.388 -16.090 1.00 26.57  ? 13  VAL   A CG2 1 
ATOM   99   N  N   . GLU   A 1 14  ? 14.753  -9.563  -12.286 1.00 24.58  ? 14  GLU   A N   1 
ATOM   100  C  CA  . GLU   A 1 14  ? 15.451  -8.677  -11.372 1.00 22.16  ? 14  GLU   A CA  1 
ATOM   101  C  C   . GLU   A 1 14  ? 16.761  -9.290  -10.855 1.00 25.01  ? 14  GLU   A C   1 
ATOM   102  O  O   . GLU   A 1 14  ? 17.754  -8.591  -10.762 1.00 25.30  ? 14  GLU   A O   1 
ATOM   103  C  CB  . GLU   A 1 14  ? 14.571  -8.369  -10.158 1.00 24.62  ? 14  GLU   A CB  1 
ATOM   104  C  CG  . GLU   A 1 14  ? 13.396  -7.422  -10.413 1.00 25.00  ? 14  GLU   A CG  1 
ATOM   105  C  CD  . GLU   A 1 14  ? 12.404  -7.248  -9.278  1.00 25.57  ? 14  GLU   A CD  1 
ATOM   106  O  OE1 . GLU   A 1 14  ? 12.843  -6.859  -8.195  1.00 28.71  ? 14  GLU   A OE1 1 
ATOM   107  O  OE2 . GLU   A 1 14  ? 11.188  -7.445  -9.466  1.00 25.08  ? 14  GLU   A OE2 1 
ATOM   108  N  N   . GLY   A 1 15  ? 16.763  -10.559 -10.435 1.00 24.68  ? 15  GLY   A N   1 
ATOM   109  C  CA  . GLY   A 1 15  ? 17.957  -11.151 -9.844  1.00 27.58  ? 15  GLY   A CA  1 
ATOM   110  C  C   . GLY   A 1 15  ? 19.056  -11.407 -10.881 1.00 29.62  ? 15  GLY   A C   1 
ATOM   111  O  O   . GLY   A 1 15  ? 20.105  -11.950 -10.525 1.00 31.09  ? 15  GLY   A O   1 
ATOM   112  N  N   . CYS   A 1 16  ? 18.795  -11.045 -12.155 1.00 26.35  ? 16  CYS   A N   1 
ATOM   113  C  CA  . CYS   A 1 16  ? 19.725  -11.271 -13.250 1.00 28.12  ? 16  CYS   A CA  1 
ATOM   114  C  C   . CYS   A 1 16  ? 20.416  -9.995  -13.756 1.00 28.58  ? 16  CYS   A C   1 
ATOM   115  O  O   . CYS   A 1 16  ? 21.348  -10.106 -14.574 1.00 25.21  ? 16  CYS   A O   1 
ATOM   116  C  CB  . CYS   A 1 16  ? 19.040  -11.961 -14.424 1.00 26.25  ? 16  CYS   A CB  1 
ATOM   117  S  SG  . CYS   A 1 16  ? 18.433  -13.622 -14.048 1.00 33.23  ? 16  CYS   A SG  1 
ATOM   118  N  N   . MET   A 1 17  ? 19.989  -8.800  -13.293 1.00 26.36  ? 17  MET   A N   1 
ATOM   119  C  CA  . MET   A 1 17  ? 20.443  -7.550  -13.908 1.00 27.20  ? 17  MET   A CA  1 
ATOM   120  C  C   . MET   A 1 17  ? 21.732  -7.035  -13.246 1.00 28.39  ? 17  MET   A C   1 
ATOM   121  O  O   . MET   A 1 17  ? 21.817  -6.969  -12.014 1.00 26.81  ? 17  MET   A O   1 
ATOM   122  C  CB  . MET   A 1 17  ? 19.397  -6.425  -13.819 1.00 27.01  ? 17  MET   A CB  1 
ATOM   123  C  CG  . MET   A 1 17  ? 18.080  -6.668  -14.532 1.00 24.69  ? 17  MET   A CG  1 
ATOM   124  S  SD  . MET   A 1 17  ? 18.176  -7.278  -16.227 1.00 25.96  ? 17  MET   A SD  1 
ATOM   125  C  CE  . MET   A 1 17  ? 18.968  -5.873  -17.026 1.00 23.26  ? 17  MET   A CE  1 
ATOM   126  N  N   . VAL   A 1 18  ? 22.703  -6.624  -14.080 1.00 27.80  ? 18  VAL   A N   1 
ATOM   127  C  CA  . VAL   A 1 18  ? 23.988  -6.092  -13.635 1.00 28.29  ? 18  VAL   A CA  1 
ATOM   128  C  C   . VAL   A 1 18  ? 24.347  -4.837  -14.439 1.00 29.52  ? 18  VAL   A C   1 
ATOM   129  O  O   . VAL   A 1 18  ? 23.659  -4.481  -15.406 1.00 27.38  ? 18  VAL   A O   1 
ATOM   130  C  CB  . VAL   A 1 18  ? 25.103  -7.155  -13.761 1.00 29.87  ? 18  VAL   A CB  1 
ATOM   131  C  CG1 . VAL   A 1 18  ? 24.802  -8.413  -12.950 1.00 30.08  ? 18  VAL   A CG1 1 
ATOM   132  C  CG2 . VAL   A 1 18  ? 25.389  -7.549  -15.207 1.00 29.42  ? 18  VAL   A CG2 1 
ATOM   133  N  N   . GLN   A 1 19  ? 25.434  -4.166  -14.014 1.00 28.60  ? 19  GLN   A N   1 
ATOM   134  C  CA  . GLN   A 1 19  ? 25.971  -2.989  -14.684 1.00 30.55  ? 19  GLN   A CA  1 
ATOM   135  C  C   . GLN   A 1 19  ? 27.283  -3.331  -15.399 1.00 33.26  ? 19  GLN   A C   1 
ATOM   136  O  O   . GLN   A 1 19  ? 28.160  -3.937  -14.792 1.00 31.50  ? 19  GLN   A O   1 
ATOM   137  C  CB  . GLN   A 1 19  ? 26.192  -1.942  -13.595 1.00 34.85  ? 19  GLN   A CB  1 
ATOM   138  C  CG  . GLN   A 1 19  ? 26.709  -0.607  -14.114 1.00 37.96  ? 19  GLN   A CG  1 
ATOM   139  C  CD  . GLN   A 1 19  ? 26.856  0.410   -13.012 1.00 45.52  ? 19  GLN   A CD  1 
ATOM   140  O  OE1 . GLN   A 1 19  ? 25.988  1.267   -12.812 1.00 50.66  ? 19  GLN   A OE1 1 
ATOM   141  N  NE2 . GLN   A 1 19  ? 27.951  0.309   -12.273 1.00 46.42  ? 19  GLN   A NE2 1 
ATOM   142  N  N   . VAL   A 1 20  ? 27.398  -2.984  -16.697 1.00 33.92  ? 20  VAL   A N   1 
ATOM   143  C  CA  . VAL   A 1 20  ? 28.615  -3.171  -17.486 1.00 30.88  ? 20  VAL   A CA  1 
ATOM   144  C  C   . VAL   A 1 20  ? 29.224  -1.813  -17.861 1.00 32.82  ? 20  VAL   A C   1 
ATOM   145  O  O   . VAL   A 1 20  ? 28.526  -0.947  -18.402 1.00 28.25  ? 20  VAL   A O   1 
ATOM   146  C  CB  . VAL   A 1 20  ? 28.309  -3.997  -18.752 1.00 30.52  ? 20  VAL   A CB  1 
ATOM   147  C  CG1 . VAL   A 1 20  ? 29.558  -4.248  -19.594 1.00 31.84  ? 20  VAL   A CG1 1 
ATOM   148  C  CG2 . VAL   A 1 20  ? 27.633  -5.323  -18.425 1.00 29.69  ? 20  VAL   A CG2 1 
ATOM   149  N  N   . THR   A 1 21  ? 30.539  -1.638  -17.611 1.00 31.17  ? 21  THR   A N   1 
ATOM   150  C  CA  . THR   A 1 21  ? 31.233  -0.432  -18.034 1.00 32.76  ? 21  THR   A CA  1 
ATOM   151  C  C   . THR   A 1 21  ? 32.424  -0.769  -18.937 1.00 37.31  ? 21  THR   A C   1 
ATOM   152  O  O   . THR   A 1 21  ? 33.119  -1.761  -18.735 1.00 35.16  ? 21  THR   A O   1 
ATOM   153  C  CB  . THR   A 1 21  ? 31.668  0.389   -16.826 1.00 36.58  ? 21  THR   A CB  1 
ATOM   154  O  OG1 . THR   A 1 21  ? 30.501  0.485   -16.017 1.00 31.59  ? 21  THR   A OG1 1 
ATOM   155  C  CG2 . THR   A 1 21  ? 32.153  1.777   -17.220 1.00 37.06  ? 21  THR   A CG2 1 
ATOM   156  N  N   . CYS   A 1 22  ? 32.630  0.066   -19.965 1.00 38.79  ? 22  CYS   A N   1 
ATOM   157  C  CA  . CYS   A 1 22  ? 33.763  -0.057  -20.874 1.00 39.58  ? 22  CYS   A CA  1 
ATOM   158  C  C   . CYS   A 1 22  ? 34.067  1.352   -21.358 1.00 40.00  ? 22  CYS   A C   1 
ATOM   159  O  O   . CYS   A 1 22  ? 33.167  2.029   -21.850 1.00 36.24  ? 22  CYS   A O   1 
ATOM   160  C  CB  . CYS   A 1 22  ? 33.422  -1.011  -22.012 1.00 40.21  ? 22  CYS   A CB  1 
ATOM   161  S  SG  . CYS   A 1 22  ? 34.737  -1.234  -23.232 1.00 52.14  ? 22  CYS   A SG  1 
ATOM   162  N  N   . GLY   A 1 23  ? 35.295  1.837   -21.139 1.00 40.25  ? 23  GLY   A N   1 
ATOM   163  C  CA  . GLY   A 1 23  ? 35.598  3.220   -21.466 1.00 36.00  ? 23  GLY   A CA  1 
ATOM   164  C  C   . GLY   A 1 23  ? 34.800  4.163   -20.571 1.00 37.26  ? 23  GLY   A C   1 
ATOM   165  O  O   . GLY   A 1 23  ? 34.731  3.934   -19.363 1.00 35.54  ? 23  GLY   A O   1 
ATOM   166  N  N   . THR   A 1 24  ? 34.166  5.195   -21.157 1.00 38.94  ? 24  THR   A N   1 
ATOM   167  C  CA  . THR   A 1 24  ? 33.327  6.109   -20.380 1.00 41.62  ? 24  THR   A CA  1 
ATOM   168  C  C   . THR   A 1 24  ? 31.828  5.751   -20.447 1.00 38.24  ? 24  THR   A C   1 
ATOM   169  O  O   . THR   A 1 24  ? 30.996  6.566   -20.039 1.00 37.42  ? 24  THR   A O   1 
ATOM   170  C  CB  . THR   A 1 24  ? 33.568  7.553   -20.835 1.00 38.91  ? 24  THR   A CB  1 
ATOM   171  O  OG1 . THR   A 1 24  ? 33.154  7.654   -22.186 1.00 37.89  ? 24  THR   A OG1 1 
ATOM   172  C  CG2 . THR   A 1 24  ? 35.023  7.984   -20.753 1.00 42.35  ? 24  THR   A CG2 1 
ATOM   173  N  N   . THR   A 1 25  ? 31.482  4.531   -20.897 1.00 35.69  ? 25  THR   A N   1 
ATOM   174  C  CA  . THR   A 1 25  ? 30.105  4.133   -21.195 1.00 35.02  ? 25  THR   A CA  1 
ATOM   175  C  C   . THR   A 1 25  ? 29.639  3.057   -20.218 1.00 32.72  ? 25  THR   A C   1 
ATOM   176  O  O   . THR   A 1 25  ? 30.267  2.003   -20.109 1.00 30.06  ? 25  THR   A O   1 
ATOM   177  C  CB  . THR   A 1 25  ? 30.023  3.589   -22.628 1.00 37.55  ? 25  THR   A CB  1 
ATOM   178  O  OG1 . THR   A 1 25  ? 30.445  4.602   -23.527 1.00 43.21  ? 25  THR   A OG1 1 
ATOM   179  C  CG2 . THR   A 1 25  ? 28.619  3.210   -23.062 1.00 38.62  ? 25  THR   A CG2 1 
ATOM   180  N  N   . THR   A 1 26  ? 28.482  3.301   -19.586 1.00 33.63  ? 26  THR   A N   1 
ATOM   181  C  CA  . THR   A 1 26  ? 27.841  2.340   -18.703 1.00 32.67  ? 26  THR   A CA  1 
ATOM   182  C  C   . THR   A 1 26  ? 26.449  1.988   -19.241 1.00 28.62  ? 26  THR   A C   1 
ATOM   183  O  O   . THR   A 1 26  ? 25.671  2.862   -19.563 1.00 27.40  ? 26  THR   A O   1 
ATOM   184  C  CB  . THR   A 1 26  ? 27.749  2.951   -17.298 1.00 35.36  ? 26  THR   A CB  1 
ATOM   185  O  OG1 . THR   A 1 26  ? 29.076  3.185   -16.834 1.00 37.26  ? 26  THR   A OG1 1 
ATOM   186  C  CG2 . THR   A 1 26  ? 27.082  2.024   -16.302 1.00 34.43  ? 26  THR   A CG2 1 
ATOM   187  N  N   . LEU   A 1 27  ? 26.115  0.699   -19.267 1.00 28.37  ? 27  LEU   A N   1 
ATOM   188  C  CA  . LEU   A 1 27  ? 24.758  0.248   -19.532 1.00 27.36  ? 27  LEU   A CA  1 
ATOM   189  C  C   . LEU   A 1 27  ? 24.499  -1.063  -18.781 1.00 27.75  ? 27  LEU   A C   1 
ATOM   190  O  O   . LEU   A 1 27  ? 25.324  -1.494  -17.964 1.00 29.20  ? 27  LEU   A O   1 
ATOM   191  C  CB  . LEU   A 1 27  ? 24.577  0.148   -21.051 1.00 24.52  ? 27  LEU   A CB  1 
ATOM   192  C  CG  . LEU   A 1 27  ? 25.635  -0.608  -21.866 1.00 25.92  ? 27  LEU   A CG  1 
ATOM   193  C  CD1 . LEU   A 1 27  ? 25.797  -2.134  -21.601 1.00 23.85  ? 27  LEU   A CD1 1 
ATOM   194  C  CD2 . LEU   A 1 27  ? 25.296  -0.370  -23.351 1.00 26.63  ? 27  LEU   A CD2 1 
ATOM   195  N  N   . ASN   A 1 28  ? 23.326  -1.668  -19.024 1.00 23.83  ? 28  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 28  ? 22.854  -2.855  -18.320 1.00 25.43  ? 28  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 28  ? 23.308  -4.137  -19.015 1.00 24.08  ? 28  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 28  ? 23.421  -4.195  -20.234 1.00 27.96  ? 28  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 28  ? 21.325  -2.878  -18.217 1.00 23.42  ? 28  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 28  ? 20.800  -1.566  -17.680 1.00 25.76  ? 28  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 28  ? 20.923  -1.296  -16.478 1.00 26.19  ? 28  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 28  ? 20.231  -0.735  -18.549 1.00 24.16  ? 28  ASN   A ND2 1 
ATOM   203  N  N   . GLY   A 1 29  ? 23.459  -5.211  -18.233 1.00 25.40  ? 29  GLY   A N   1 
ATOM   204  C  CA  . GLY   A 1 29  ? 23.697  -6.537  -18.778 1.00 24.19  ? 29  GLY   A CA  1 
ATOM   205  C  C   . GLY   A 1 29  ? 22.840  -7.594  -18.091 1.00 25.21  ? 29  GLY   A C   1 
ATOM   206  O  O   . GLY   A 1 29  ? 22.227  -7.345  -17.045 1.00 25.89  ? 29  GLY   A O   1 
ATOM   207  N  N   . LEU   A 1 30  ? 22.786  -8.767  -18.718 1.00 25.28  ? 30  LEU   A N   1 
ATOM   208  C  CA  . LEU   A 1 30  ? 21.928  -9.848  -18.262 1.00 27.81  ? 30  LEU   A CA  1 
ATOM   209  C  C   . LEU   A 1 30  ? 22.801  -11.040 -17.863 1.00 29.95  ? 30  LEU   A C   1 
ATOM   210  O  O   . LEU   A 1 30  ? 23.437  -11.642 -18.742 1.00 28.82  ? 30  LEU   A O   1 
ATOM   211  C  CB  . LEU   A 1 30  ? 20.936  -10.224 -19.360 1.00 27.49  ? 30  LEU   A CB  1 
ATOM   212  C  CG  . LEU   A 1 30  ? 19.948  -11.330 -18.982 1.00 29.17  ? 30  LEU   A CG  1 
ATOM   213  C  CD1 . LEU   A 1 30  ? 18.910  -10.854 -17.959 1.00 29.76  ? 30  LEU   A CD1 1 
ATOM   214  C  CD2 . LEU   A 1 30  ? 19.253  -11.872 -20.185 1.00 29.51  ? 30  LEU   A CD2 1 
ATOM   215  N  N   . TRP   A 1 31  ? 22.831  -11.331 -16.544 1.00 30.67  ? 31  TRP   A N   1 
ATOM   216  C  CA  . TRP   A 1 31  ? 23.699  -12.338 -15.923 1.00 32.40  ? 31  TRP   A CA  1 
ATOM   217  C  C   . TRP   A 1 31  ? 22.943  -13.648 -15.726 1.00 33.87  ? 31  TRP   A C   1 
ATOM   218  O  O   . TRP   A 1 31  ? 22.088  -13.747 -14.837 1.00 34.78  ? 31  TRP   A O   1 
ATOM   219  C  CB  . TRP   A 1 31  ? 24.256  -11.832 -14.583 1.00 35.47  ? 31  TRP   A CB  1 
ATOM   220  C  CG  . TRP   A 1 31  ? 25.239  -12.735 -13.871 1.00 40.05  ? 31  TRP   A CG  1 
ATOM   221  C  CD1 . TRP   A 1 31  ? 26.014  -13.725 -14.408 1.00 44.10  ? 31  TRP   A CD1 1 
ATOM   222  C  CD2 . TRP   A 1 31  ? 25.587  -12.692 -12.467 1.00 40.55  ? 31  TRP   A CD2 1 
ATOM   223  N  NE1 . TRP   A 1 31  ? 26.802  -14.309 -13.447 1.00 43.69  ? 31  TRP   A NE1 1 
ATOM   224  C  CE2 . TRP   A 1 31  ? 26.571  -13.692 -12.247 1.00 41.23  ? 31  TRP   A CE2 1 
ATOM   225  C  CE3 . TRP   A 1 31  ? 25.167  -11.915 -11.380 1.00 38.48  ? 31  TRP   A CE3 1 
ATOM   226  C  CZ2 . TRP   A 1 31  ? 27.120  -13.936 -10.988 1.00 37.38  ? 31  TRP   A CZ2 1 
ATOM   227  C  CZ3 . TRP   A 1 31  ? 25.721  -12.146 -10.136 1.00 36.79  ? 31  TRP   A CZ3 1 
ATOM   228  C  CH2 . TRP   A 1 31  ? 26.676  -13.151 -9.944  1.00 35.74  ? 31  TRP   A CH2 1 
ATOM   229  N  N   . LEU   A 1 32  ? 23.261  -14.616 -16.599 1.00 31.98  ? 32  LEU   A N   1 
ATOM   230  C  CA  . LEU   A 1 32  ? 22.742  -15.969 -16.553 1.00 33.01  ? 32  LEU   A CA  1 
ATOM   231  C  C   . LEU   A 1 32  ? 23.936  -16.923 -16.482 1.00 37.73  ? 32  LEU   A C   1 
ATOM   232  O  O   . LEU   A 1 32  ? 24.872  -16.786 -17.276 1.00 33.66  ? 32  LEU   A O   1 
ATOM   233  C  CB  . LEU   A 1 32  ? 21.893  -16.259 -17.790 1.00 34.42  ? 32  LEU   A CB  1 
ATOM   234  C  CG  . LEU   A 1 32  ? 20.667  -15.362 -18.002 1.00 37.43  ? 32  LEU   A CG  1 
ATOM   235  C  CD1 . LEU   A 1 32  ? 20.119  -15.565 -19.401 1.00 37.52  ? 32  LEU   A CD1 1 
ATOM   236  C  CD2 . LEU   A 1 32  ? 19.578  -15.614 -16.956 1.00 35.92  ? 32  LEU   A CD2 1 
ATOM   237  N  N   . ASP   A 1 33  ? 23.888  -17.890 -15.543 1.00 35.79  ? 33  ASP   A N   1 
ATOM   238  C  CA  . ASP   A 1 33  ? 25.004  -18.799 -15.272 1.00 34.32  ? 33  ASP   A CA  1 
ATOM   239  C  C   . ASP   A 1 33  ? 26.286  -17.977 -15.225 1.00 34.26  ? 33  ASP   A C   1 
ATOM   240  O  O   . ASP   A 1 33  ? 26.341  -16.972 -14.503 1.00 33.12  ? 33  ASP   A O   1 
ATOM   241  C  CB  . ASP   A 1 33  ? 24.963  -19.988 -16.220 1.00 34.80  ? 33  ASP   A CB  1 
ATOM   242  C  CG  . ASP   A 1 33  ? 23.620  -20.698 -16.215 1.00 39.54  ? 33  ASP   A CG  1 
ATOM   243  O  OD1 . ASP   A 1 33  ? 23.092  -20.915 -15.114 1.00 53.99  ? 33  ASP   A OD1 1 
ATOM   244  O  OD2 . ASP   A 1 33  ? 23.076  -21.000 -17.294 1.00 44.96  ? 33  ASP   A OD2 1 
ATOM   245  N  N   . ASP   A 1 34  ? 27.273  -18.329 -16.063 1.00 36.27  ? 34  ASP   A N   1 
ATOM   246  C  CA  . ASP   A 1 34  ? 28.575  -17.678 -16.000 1.00 39.54  ? 34  ASP   A CA  1 
ATOM   247  C  C   . ASP   A 1 34  ? 28.788  -16.678 -17.150 1.00 41.84  ? 34  ASP   A C   1 
ATOM   248  O  O   . ASP   A 1 34  ? 29.920  -16.237 -17.374 1.00 35.11  ? 34  ASP   A O   1 
ATOM   249  C  CB  . ASP   A 1 34  ? 29.662  -18.730 -15.840 1.00 42.76  ? 34  ASP   A CB  1 
ATOM   250  C  CG  . ASP   A 1 34  ? 29.960  -19.615 -17.043 1.00 44.52  ? 34  ASP   A CG  1 
ATOM   251  O  OD1 . ASP   A 1 34  ? 29.013  -20.036 -17.740 1.00 42.33  ? 34  ASP   A OD1 1 
ATOM   252  O  OD2 . ASP   A 1 34  ? 31.157  -19.909 -17.253 1.00 54.41  ? 34  ASP   A OD2 1 
ATOM   253  N  N   . VAL   A 1 35  ? 27.691  -16.232 -17.799 1.00 38.70  ? 35  VAL   A N   1 
ATOM   254  C  CA  . VAL   A 1 35  ? 27.744  -15.269 -18.898 1.00 33.75  ? 35  VAL   A CA  1 
ATOM   255  C  C   . VAL   A 1 35  ? 26.885  -14.038 -18.606 1.00 36.29  ? 35  VAL   A C   1 
ATOM   256  O  O   . VAL   A 1 35  ? 25.751  -14.152 -18.113 1.00 30.41  ? 35  VAL   A O   1 
ATOM   257  C  CB  . VAL   A 1 35  ? 27.226  -15.927 -20.186 1.00 34.96  ? 35  VAL   A CB  1 
ATOM   258  C  CG1 . VAL   A 1 35  ? 27.318  -14.960 -21.364 1.00 36.10  ? 35  VAL   A CG1 1 
ATOM   259  C  CG2 . VAL   A 1 35  ? 27.950  -17.237 -20.483 1.00 37.26  ? 35  VAL   A CG2 1 
ATOM   260  N  N   . VAL   A 1 36  ? 27.437  -12.873 -18.967 1.00 33.25  ? 36  VAL   A N   1 
ATOM   261  C  CA  . VAL   A 1 36  ? 26.717  -11.610 -19.001 1.00 30.17  ? 36  VAL   A CA  1 
ATOM   262  C  C   . VAL   A 1 36  ? 26.539  -11.214 -20.464 1.00 29.05  ? 36  VAL   A C   1 
ATOM   263  O  O   . VAL   A 1 36  ? 27.546  -11.074 -21.171 1.00 29.84  ? 36  VAL   A O   1 
ATOM   264  C  CB  . VAL   A 1 36  ? 27.501  -10.529 -18.231 1.00 31.65  ? 36  VAL   A CB  1 
ATOM   265  C  CG1 . VAL   A 1 36  ? 26.909  -9.134  -18.390 1.00 31.86  ? 36  VAL   A CG1 1 
ATOM   266  C  CG2 . VAL   A 1 36  ? 27.632  -10.856 -16.752 1.00 36.08  ? 36  VAL   A CG2 1 
ATOM   267  N  N   . TYR   A 1 37  ? 25.274  -11.021 -20.889 1.00 26.09  ? 37  TYR   A N   1 
ATOM   268  C  CA  . TYR   A 1 37  ? 24.926  -10.575 -22.235 1.00 25.84  ? 37  TYR   A CA  1 
ATOM   269  C  C   . TYR   A 1 37  ? 24.675  -9.063  -22.241 1.00 24.54  ? 37  TYR   A C   1 
ATOM   270  O  O   . TYR   A 1 37  ? 23.927  -8.569  -21.414 1.00 26.05  ? 37  TYR   A O   1 
ATOM   271  C  CB  . TYR   A 1 37  ? 23.685  -11.310 -22.745 1.00 26.48  ? 37  TYR   A CB  1 
ATOM   272  C  CG  . TYR   A 1 37  ? 23.777  -12.831 -22.747 1.00 31.92  ? 37  TYR   A CG  1 
ATOM   273  C  CD1 . TYR   A 1 37  ? 23.636  -13.555 -21.560 1.00 33.19  ? 37  TYR   A CD1 1 
ATOM   274  C  CD2 . TYR   A 1 37  ? 24.015  -13.549 -23.921 1.00 30.47  ? 37  TYR   A CD2 1 
ATOM   275  C  CE1 . TYR   A 1 37  ? 23.712  -14.937 -21.545 1.00 31.21  ? 37  TYR   A CE1 1 
ATOM   276  C  CE2 . TYR   A 1 37  ? 24.107  -14.933 -23.910 1.00 32.20  ? 37  TYR   A CE2 1 
ATOM   277  C  CZ  . TYR   A 1 37  ? 23.972  -15.629 -22.718 1.00 32.97  ? 37  TYR   A CZ  1 
ATOM   278  O  OH  . TYR   A 1 37  ? 24.062  -17.001 -22.679 1.00 35.58  ? 37  TYR   A OH  1 
ATOM   279  N  N   . CYS   A 1 38  ? 25.264  -8.316  -23.185 1.00 25.05  ? 38  CYS   A N   1 
ATOM   280  C  CA  . CYS   A 1 38  ? 24.990  -6.886  -23.306 1.00 24.23  ? 38  CYS   A CA  1 
ATOM   281  C  C   . CYS   A 1 38  ? 25.128  -6.450  -24.767 1.00 26.75  ? 38  CYS   A C   1 
ATOM   282  O  O   . CYS   A 1 38  ? 25.676  -7.186  -25.586 1.00 27.42  ? 38  CYS   A O   1 
ATOM   283  C  CB  . CYS   A 1 38  ? 25.864  -6.049  -22.377 1.00 28.18  ? 38  CYS   A CB  1 
ATOM   284  S  SG  . CYS   A 1 38  ? 27.613  -5.881  -22.868 1.00 29.56  ? 38  CYS   A SG  1 
ATOM   285  N  N   . PRO   A 1 39  ? 24.613  -5.253  -25.161 1.00 27.03  ? 39  PRO   A N   1 
ATOM   286  C  CA  . PRO   A 1 39  ? 24.826  -4.737  -26.519 1.00 25.91  ? 39  PRO   A CA  1 
ATOM   287  C  C   . PRO   A 1 39  ? 26.318  -4.553  -26.791 1.00 22.95  ? 39  PRO   A C   1 
ATOM   288  O  O   . PRO   A 1 39  ? 27.031  -3.983  -25.978 1.00 23.73  ? 39  PRO   A O   1 
ATOM   289  C  CB  . PRO   A 1 39  ? 24.069  -3.372  -26.533 1.00 26.10  ? 39  PRO   A CB  1 
ATOM   290  C  CG  . PRO   A 1 39  ? 23.050  -3.502  -25.400 1.00 26.31  ? 39  PRO   A CG  1 
ATOM   291  C  CD  . PRO   A 1 39  ? 23.744  -4.370  -24.359 1.00 27.01  ? 39  PRO   A CD  1 
ATOM   292  N  N   . ARG   A 1 40  ? 26.742  -4.954  -27.984 1.00 23.41  ? 40  ARG   A N   1 
ATOM   293  C  CA  . ARG   A 1 40  ? 28.117  -4.818  -28.429 1.00 23.75  ? 40  ARG   A CA  1 
ATOM   294  C  C   . ARG   A 1 40  ? 28.535  -3.355  -28.622 1.00 25.05  ? 40  ARG   A C   1 
ATOM   295  O  O   . ARG   A 1 40  ? 29.728  -3.079  -28.580 1.00 25.61  ? 40  ARG   A O   1 
ATOM   296  C  CB  . ARG   A 1 40  ? 28.330  -5.631  -29.710 1.00 25.37  ? 40  ARG   A CB  1 
ATOM   297  C  CG  . ARG   A 1 40  ? 27.781  -5.070  -31.008 1.00 23.91  ? 40  ARG   A CG  1 
ATOM   298  C  CD  . ARG   A 1 40  ? 28.225  -5.977  -32.143 1.00 25.85  ? 40  ARG   A CD  1 
ATOM   299  N  NE  . ARG   A 1 40  ? 27.598  -5.575  -33.401 1.00 26.05  ? 40  ARG   A NE  1 
ATOM   300  C  CZ  . ARG   A 1 40  ? 27.967  -5.971  -34.619 1.00 28.40  ? 40  ARG   A CZ  1 
ATOM   301  N  NH1 . ARG   A 1 40  ? 28.943  -6.859  -34.777 1.00 26.73  ? 40  ARG   A NH1 1 
ATOM   302  N  NH2 . ARG   A 1 40  ? 27.358  -5.451  -35.669 1.00 25.36  ? 40  ARG   A NH2 1 
ATOM   303  N  N   . HIS   A 1 41  ? 27.594  -2.404  -28.735 1.00 24.40  ? 41  HIS   A N   1 
ATOM   304  C  CA  . HIS   A 1 41  ? 27.967  -1.005  -28.929 1.00 25.32  ? 41  HIS   A CA  1 
ATOM   305  C  C   . HIS   A 1 41  ? 28.588  -0.352  -27.687 1.00 24.83  ? 41  HIS   A C   1 
ATOM   306  O  O   . HIS   A 1 41  ? 29.054  0.787   -27.772 1.00 26.52  ? 41  HIS   A O   1 
ATOM   307  C  CB  . HIS   A 1 41  ? 26.815  -0.203  -29.550 1.00 25.54  ? 41  HIS   A CB  1 
ATOM   308  C  CG  . HIS   A 1 41  ? 25.651  0.138   -28.672 1.00 27.50  ? 41  HIS   A CG  1 
ATOM   309  N  ND1 . HIS   A 1 41  ? 25.700  0.788   -27.456 1.00 28.13  ? 41  HIS   A ND1 1 
ATOM   310  C  CD2 . HIS   A 1 41  ? 24.354  -0.025  -28.951 1.00 29.53  ? 41  HIS   A CD2 1 
ATOM   311  C  CE1 . HIS   A 1 41  ? 24.461  0.945   -27.003 1.00 32.09  ? 41  HIS   A CE1 1 
ATOM   312  N  NE2 . HIS   A 1 41  ? 23.626  0.448   -27.894 1.00 30.45  ? 41  HIS   A NE2 1 
ATOM   313  N  N   . VAL   A 1 42  ? 28.621  -1.067  -26.557 1.00 23.60  ? 42  VAL   A N   1 
ATOM   314  C  CA  . VAL   A 1 42  ? 29.271  -0.625  -25.335 1.00 25.78  ? 42  VAL   A CA  1 
ATOM   315  C  C   . VAL   A 1 42  ? 30.763  -0.380  -25.591 1.00 30.02  ? 42  VAL   A C   1 
ATOM   316  O  O   . VAL   A 1 42  ? 31.358  0.436   -24.879 1.00 30.95  ? 42  VAL   A O   1 
ATOM   317  C  CB  . VAL   A 1 42  ? 29.044  -1.650  -24.193 1.00 26.26  ? 42  VAL   A CB  1 
ATOM   318  C  CG1 . VAL   A 1 42  ? 29.766  -2.984  -24.394 1.00 26.01  ? 42  VAL   A CG1 1 
ATOM   319  C  CG2 . VAL   A 1 42  ? 29.402  -1.102  -22.816 1.00 27.83  ? 42  VAL   A CG2 1 
ATOM   320  N  N   . ILE   A 1 43  ? 31.356  -1.063  -26.592 1.00 32.14  ? 43  ILE   A N   1 
ATOM   321  C  CA  . ILE   A 1 43  ? 32.783  -0.924  -26.889 1.00 34.81  ? 43  ILE   A CA  1 
ATOM   322  C  C   . ILE   A 1 43  ? 33.085  0.218   -27.867 1.00 35.42  ? 43  ILE   A C   1 
ATOM   323  O  O   . ILE   A 1 43  ? 34.240  0.377   -28.207 1.00 38.53  ? 43  ILE   A O   1 
ATOM   324  C  CB  . ILE   A 1 43  ? 33.411  -2.225  -27.424 1.00 31.98  ? 43  ILE   A CB  1 
ATOM   325  C  CG1 . ILE   A 1 43  ? 33.019  -2.523  -28.880 1.00 33.22  ? 43  ILE   A CG1 1 
ATOM   326  C  CG2 . ILE   A 1 43  ? 33.140  -3.411  -26.508 1.00 32.24  ? 43  ILE   A CG2 1 
ATOM   327  C  CD1 . ILE   A 1 43  ? 33.643  -3.798  -29.432 1.00 30.38  ? 43  ILE   A CD1 1 
ATOM   328  N  N   . CYS   A 1 44  ? 32.093  0.986   -28.345 1.00 36.80  ? 44  CYS   A N   1 
ATOM   329  C  CA  . CYS   A 1 44  ? 32.337  2.098   -29.261 1.00 36.21  ? 44  CYS   A CA  1 
ATOM   330  C  C   . CYS   A 1 44  ? 32.697  3.371   -28.505 1.00 36.83  ? 44  CYS   A C   1 
ATOM   331  O  O   . CYS   A 1 44  ? 32.224  3.559   -27.400 1.00 33.41  ? 44  CYS   A O   1 
ATOM   332  C  CB  . CYS   A 1 44  ? 31.094  2.440   -30.073 1.00 37.42  ? 44  CYS   A CB  1 
ATOM   333  S  SG  . CYS   A 1 44  ? 30.534  1.079   -31.126 1.00 43.73  ? 44  CYS   A SG  1 
ATOM   334  N  N   . THR   A 1 45  ? 33.480  4.256   -29.142 1.00 40.33  ? 45  THR   A N   1 
ATOM   335  C  CA  . THR   A 1 45  ? 33.763  5.605   -28.660 1.00 41.04  ? 45  THR   A CA  1 
ATOM   336  C  C   . THR   A 1 45  ? 33.156  6.620   -29.634 1.00 45.23  ? 45  THR   A C   1 
ATOM   337  O  O   . THR   A 1 45  ? 32.420  6.238   -30.550 1.00 43.39  ? 45  THR   A O   1 
ATOM   338  C  CB  . THR   A 1 45  ? 35.280  5.794   -28.538 1.00 40.61  ? 45  THR   A CB  1 
ATOM   339  O  OG1 . THR   A 1 45  ? 35.757  5.603   -29.864 1.00 40.88  ? 45  THR   A OG1 1 
ATOM   340  C  CG2 . THR   A 1 45  ? 35.979  4.748   -27.693 1.00 42.79  ? 45  THR   A CG2 1 
ATOM   341  N  N   . SER   A 1 46  ? 33.515  7.905   -29.452 1.00 48.23  ? 46  SER   A N   1 
ATOM   342  C  CA  . SER   A 1 46  ? 33.012  9.032   -30.237 1.00 55.76  ? 46  SER   A CA  1 
ATOM   343  C  C   . SER   A 1 46  ? 33.004  8.767   -31.742 1.00 55.48  ? 46  SER   A C   1 
ATOM   344  O  O   . SER   A 1 46  ? 31.949  8.858   -32.363 1.00 59.45  ? 46  SER   A O   1 
ATOM   345  C  CB  . SER   A 1 46  ? 33.805  10.290  -29.969 1.00 59.77  ? 46  SER   A CB  1 
ATOM   346  O  OG  . SER   A 1 46  ? 33.951  10.518  -28.579 1.00 63.11  ? 46  SER   A OG  1 
ATOM   347  N  N   . GLU   A 1 47  ? 34.172  8.492   -32.344 1.00 59.79  ? 47  GLU   A N   1 
ATOM   348  C  CA  . GLU   A 1 47  ? 34.224  8.289   -33.790 1.00 63.05  ? 47  GLU   A CA  1 
ATOM   349  C  C   . GLU   A 1 47  ? 34.178  6.796   -34.127 1.00 51.00  ? 47  GLU   A C   1 
ATOM   350  O  O   . GLU   A 1 47  ? 34.798  6.340   -35.078 1.00 49.36  ? 47  GLU   A O   1 
ATOM   351  C  CB  . GLU   A 1 47  ? 35.421  8.894   -34.534 1.00 74.99  ? 47  GLU   A CB  1 
ATOM   352  C  CG  . GLU   A 1 47  ? 35.937  10.233  -34.014 1.00 80.31  ? 47  GLU   A CG  1 
ATOM   353  C  CD  . GLU   A 1 47  ? 37.241  10.124  -33.247 1.00 83.54  ? 47  GLU   A CD  1 
ATOM   354  O  OE1 . GLU   A 1 47  ? 37.770  8.999   -33.110 1.00 81.83  ? 47  GLU   A OE1 1 
ATOM   355  O  OE2 . GLU   A 1 47  ? 37.738  11.177  -32.798 1.00 92.98  ? 47  GLU   A OE2 1 
ATOM   356  N  N   . ASP   A 1 48  ? 33.420  6.024   -33.358 1.00 46.89  ? 48  ASP   A N   1 
ATOM   357  C  CA  . ASP   A 1 48  ? 33.076  4.670   -33.745 1.00 44.86  ? 48  ASP   A CA  1 
ATOM   358  C  C   . ASP   A 1 48  ? 31.562  4.565   -33.853 1.00 43.09  ? 48  ASP   A C   1 
ATOM   359  O  O   . ASP   A 1 48  ? 31.006  3.492   -33.630 1.00 45.06  ? 48  ASP   A O   1 
ATOM   360  C  CB  . ASP   A 1 48  ? 33.558  3.636   -32.737 1.00 43.85  ? 48  ASP   A CB  1 
ATOM   361  C  CG  . ASP   A 1 48  ? 35.058  3.593   -32.502 1.00 44.00  ? 48  ASP   A CG  1 
ATOM   362  O  OD1 . ASP   A 1 48  ? 35.813  3.634   -33.499 1.00 46.87  ? 48  ASP   A OD1 1 
ATOM   363  O  OD2 . ASP   A 1 48  ? 35.454  3.503   -31.325 1.00 37.20  ? 48  ASP   A OD2 1 
ATOM   364  N  N   . MET   A 1 49  ? 30.887  5.686   -34.122 1.00 41.04  ? 49  MET   A N   1 
ATOM   365  C  CA  . MET   A 1 49  ? 29.437  5.678   -34.023 1.00 44.17  ? 49  MET   A CA  1 
ATOM   366  C  C   . MET   A 1 49  ? 28.817  5.434   -35.408 1.00 41.63  ? 49  MET   A C   1 
ATOM   367  O  O   . MET   A 1 49  ? 27.784  4.768   -35.499 1.00 36.40  ? 49  MET   A O   1 
ATOM   368  C  CB  . MET   A 1 49  ? 28.936  6.953   -33.323 1.00 55.00  ? 49  MET   A CB  1 
ATOM   369  C  CG  . MET   A 1 49  ? 29.247  7.061   -31.803 1.00 62.57  ? 49  MET   A CG  1 
ATOM   370  S  SD  . MET   A 1 49  ? 28.867  5.674   -30.695 1.00 78.22  ? 49  MET   A SD  1 
ATOM   371  C  CE  . MET   A 1 49  ? 27.288  4.891   -31.069 1.00 71.46  ? 49  MET   A CE  1 
ATOM   372  N  N   . LEU   A 1 50  ? 29.474  5.918   -36.481 1.00 33.29  ? 50  LEU   A N   1 
ATOM   373  C  CA  . LEU   A 1 50  ? 28.948  5.850   -37.844 1.00 33.12  ? 50  LEU   A CA  1 
ATOM   374  C  C   . LEU   A 1 50  ? 29.262  4.513   -38.526 1.00 27.15  ? 50  LEU   A C   1 
ATOM   375  O  O   . LEU   A 1 50  ? 28.403  3.918   -39.145 1.00 27.83  ? 50  LEU   A O   1 
ATOM   376  C  CB  . LEU   A 1 50  ? 29.515  6.993   -38.696 1.00 37.07  ? 50  LEU   A CB  1 
ATOM   377  C  CG  . LEU   A 1 50  ? 28.829  8.364   -38.620 1.00 44.96  ? 50  LEU   A CG  1 
ATOM   378  C  CD1 . LEU   A 1 50  ? 27.310  8.236   -38.690 1.00 48.12  ? 50  LEU   A CD1 1 
ATOM   379  C  CD2 . LEU   A 1 50  ? 29.236  9.131   -37.385 1.00 51.16  ? 50  LEU   A CD2 1 
ATOM   380  N  N   . ASN   A 1 51  ? 30.525  4.098   -38.515 1.00 25.70  ? 51  ASN   A N   1 
ATOM   381  C  CA  . ASN   A 1 51  ? 30.970  2.947   -39.270 1.00 26.55  ? 51  ASN   A CA  1 
ATOM   382  C  C   . ASN   A 1 51  ? 31.909  2.103   -38.411 1.00 28.71  ? 51  ASN   A C   1 
ATOM   383  O  O   . ASN   A 1 51  ? 33.036  1.836   -38.799 1.00 27.64  ? 51  ASN   A O   1 
ATOM   384  C  CB  . ASN   A 1 51  ? 31.599  3.412   -40.576 1.00 25.98  ? 51  ASN   A CB  1 
ATOM   385  C  CG  . ASN   A 1 51  ? 30.563  4.029   -41.483 1.00 25.78  ? 51  ASN   A CG  1 
ATOM   386  O  OD1 . ASN   A 1 51  ? 29.830  3.296   -42.148 1.00 26.97  ? 51  ASN   A OD1 1 
ATOM   387  N  ND2 . ASN   A 1 51  ? 30.496  5.353   -41.552 1.00 25.80  ? 51  ASN   A ND2 1 
ATOM   388  N  N   . PRO   A 1 52  ? 31.471  1.630   -37.227 1.00 28.72  ? 52  PRO   A N   1 
ATOM   389  C  CA  . PRO   A 1 52  ? 32.308  0.772   -36.389 1.00 28.42  ? 52  PRO   A CA  1 
ATOM   390  C  C   . PRO   A 1 52  ? 32.651  -0.559  -37.047 1.00 27.76  ? 52  PRO   A C   1 
ATOM   391  O  O   . PRO   A 1 52  ? 31.812  -1.155  -37.719 1.00 28.39  ? 52  PRO   A O   1 
ATOM   392  C  CB  . PRO   A 1 52  ? 31.419  0.607   -35.138 1.00 28.20  ? 52  PRO   A CB  1 
ATOM   393  C  CG  . PRO   A 1 52  ? 30.018  0.701   -35.690 1.00 27.40  ? 52  PRO   A CG  1 
ATOM   394  C  CD  . PRO   A 1 52  ? 30.138  1.865   -36.644 1.00 28.93  ? 52  PRO   A CD  1 
ATOM   395  N  N   . ASN   A 1 53  ? 33.917  -0.977  -36.904 1.00 25.72  ? 53  ASN   A N   1 
ATOM   396  C  CA  . ASN   A 1 53  ? 34.346  -2.316  -37.263 1.00 27.66  ? 53  ASN   A CA  1 
ATOM   397  C  C   . ASN   A 1 53  ? 34.478  -3.128  -35.976 1.00 29.47  ? 53  ASN   A C   1 
ATOM   398  O  O   . ASN   A 1 53  ? 35.520  -3.126  -35.321 1.00 30.60  ? 53  ASN   A O   1 
ATOM   399  C  CB  . ASN   A 1 53  ? 35.640  -2.243  -38.067 1.00 29.99  ? 53  ASN   A CB  1 
ATOM   400  C  CG  . ASN   A 1 53  ? 36.033  -3.579  -38.648 1.00 34.40  ? 53  ASN   A CG  1 
ATOM   401  O  OD1 . ASN   A 1 53  ? 36.010  -4.607  -37.964 1.00 32.40  ? 53  ASN   A OD1 1 
ATOM   402  N  ND2 . ASN   A 1 53  ? 36.416  -3.575  -39.915 1.00 41.42  ? 53  ASN   A ND2 1 
ATOM   403  N  N   . TYR   A 1 54  ? 33.399  -3.809  -35.588 1.00 31.79  ? 54  TYR   A N   1 
ATOM   404  C  CA  . TYR   A 1 54  ? 33.302  -4.383  -34.255 1.00 30.17  ? 54  TYR   A CA  1 
ATOM   405  C  C   . TYR   A 1 54  ? 34.384  -5.442  -34.026 1.00 29.31  ? 54  TYR   A C   1 
ATOM   406  O  O   . TYR   A 1 54  ? 34.912  -5.521  -32.914 1.00 28.52  ? 54  TYR   A O   1 
ATOM   407  C  CB  . TYR   A 1 54  ? 31.886  -4.924  -34.011 1.00 27.68  ? 54  TYR   A CB  1 
ATOM   408  C  CG  . TYR   A 1 54  ? 30.854  -3.837  -33.734 1.00 26.76  ? 54  TYR   A CG  1 
ATOM   409  C  CD1 . TYR   A 1 54  ? 30.810  -3.192  -32.508 1.00 26.57  ? 54  TYR   A CD1 1 
ATOM   410  C  CD2 . TYR   A 1 54  ? 29.930  -3.453  -34.701 1.00 27.15  ? 54  TYR   A CD2 1 
ATOM   411  C  CE1 . TYR   A 1 54  ? 29.883  -2.201  -32.245 1.00 29.63  ? 54  TYR   A CE1 1 
ATOM   412  C  CE2 . TYR   A 1 54  ? 29.001  -2.460  -34.457 1.00 25.71  ? 54  TYR   A CE2 1 
ATOM   413  C  CZ  . TYR   A 1 54  ? 28.969  -1.839  -33.223 1.00 28.31  ? 54  TYR   A CZ  1 
ATOM   414  O  OH  . TYR   A 1 54  ? 28.066  -0.850  -32.993 1.00 25.99  ? 54  TYR   A OH  1 
ATOM   415  N  N   . GLU   A 1 55  ? 34.693  -6.240  -35.059 1.00 29.70  ? 55  GLU   A N   1 
ATOM   416  C  CA  . GLU   A 1 55  ? 35.691  -7.305  -34.964 1.00 34.94  ? 55  GLU   A CA  1 
ATOM   417  C  C   . GLU   A 1 55  ? 37.060  -6.679  -34.657 1.00 30.78  ? 55  GLU   A C   1 
ATOM   418  O  O   . GLU   A 1 55  ? 37.779  -7.133  -33.770 1.00 30.55  ? 55  GLU   A O   1 
ATOM   419  C  CB  . GLU   A 1 55  ? 35.571  -8.195  -36.209 1.00 37.67  ? 55  GLU   A CB  1 
ATOM   420  C  CG  . GLU   A 1 55  ? 36.530  -9.385  -36.255 1.00 50.95  ? 55  GLU   A CG  1 
ATOM   421  C  CD  . GLU   A 1 55  ? 37.019  -9.878  -37.631 1.00 64.19  ? 55  GLU   A CD  1 
ATOM   422  O  OE1 . GLU   A 1 55  ? 36.749  -9.223  -38.675 1.00 67.70  ? 55  GLU   A OE1 1 
ATOM   423  O  OE2 . GLU   A 1 55  ? 37.701  -10.941 -37.674 1.00 67.76  ? 55  GLU   A OE2 1 
ATOM   424  N  N   . ASP   A 1 56  ? 37.368  -5.546  -35.295 1.00 29.89  ? 56  ASP   A N   1 
ATOM   425  C  CA  . ASP   A 1 56  ? 38.616  -4.832  -35.046 1.00 28.85  ? 56  ASP   A CA  1 
ATOM   426  C  C   . ASP   A 1 56  ? 38.648  -4.209  -33.641 1.00 29.05  ? 56  ASP   A C   1 
ATOM   427  O  O   . ASP   A 1 56  ? 39.707  -4.181  -33.020 1.00 26.17  ? 56  ASP   A O   1 
ATOM   428  C  CB  . ASP   A 1 56  ? 38.881  -3.791  -36.129 1.00 29.50  ? 56  ASP   A CB  1 
ATOM   429  C  CG  . ASP   A 1 56  ? 40.272  -3.157  -36.099 1.00 31.21  ? 56  ASP   A CG  1 
ATOM   430  O  OD1 . ASP   A 1 56  ? 41.236  -3.870  -36.353 1.00 28.45  ? 56  ASP   A OD1 1 
ATOM   431  O  OD2 . ASP   A 1 56  ? 40.380  -1.965  -35.779 1.00 37.30  ? 56  ASP   A OD2 1 
ATOM   432  N  N   . LEU   A 1 57  ? 37.535  -3.639  -33.147 1.00 28.63  ? 57  LEU   A N   1 
ATOM   433  C  CA  . LEU   A 1 57  ? 37.525  -2.987  -31.835 1.00 28.19  ? 57  LEU   A CA  1 
ATOM   434  C  C   . LEU   A 1 57  ? 37.627  -4.019  -30.706 1.00 31.03  ? 57  LEU   A C   1 
ATOM   435  O  O   . LEU   A 1 57  ? 38.222  -3.736  -29.666 1.00 32.97  ? 57  LEU   A O   1 
ATOM   436  C  CB  . LEU   A 1 57  ? 36.259  -2.149  -31.665 1.00 28.41  ? 57  LEU   A CB  1 
ATOM   437  C  CG  . LEU   A 1 57  ? 36.098  -0.998  -32.656 1.00 30.94  ? 57  LEU   A CG  1 
ATOM   438  C  CD1 . LEU   A 1 57  ? 34.689  -0.433  -32.656 1.00 33.07  ? 57  LEU   A CD1 1 
ATOM   439  C  CD2 . LEU   A 1 57  ? 37.121  0.108   -32.405 1.00 30.38  ? 57  LEU   A CD2 1 
ATOM   440  N  N   . LEU   A 1 58  ? 37.021  -5.203  -30.885 1.00 29.41  ? 58  LEU   A N   1 
ATOM   441  C  CA  . LEU   A 1 58  ? 36.988  -6.219  -29.832 1.00 31.05  ? 58  LEU   A CA  1 
ATOM   442  C  C   . LEU   A 1 58  ? 38.359  -6.880  -29.635 1.00 33.55  ? 58  LEU   A C   1 
ATOM   443  O  O   . LEU   A 1 58  ? 38.769  -7.130  -28.502 1.00 30.74  ? 58  LEU   A O   1 
ATOM   444  C  CB  . LEU   A 1 58  ? 35.937  -7.288  -30.142 1.00 31.94  ? 58  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A 1 58  ? 35.578  -8.246  -28.997 1.00 33.19  ? 58  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A 1 58  ? 35.153  -7.516  -27.723 1.00 35.90  ? 58  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A 1 58  ? 34.454  -9.187  -29.409 1.00 33.28  ? 58  LEU   A CD2 1 
ATOM   448  N  N   . ILE   A 1 59  ? 39.065  -7.195  -30.733 1.00 34.52  ? 59  ILE   A N   1 
ATOM   449  C  CA  . ILE   A 1 59  ? 40.339  -7.901  -30.642 1.00 37.70  ? 59  ILE   A CA  1 
ATOM   450  C  C   . ILE   A 1 59  ? 41.347  -7.080  -29.822 1.00 35.58  ? 59  ILE   A C   1 
ATOM   451  O  O   . ILE   A 1 59  ? 42.247  -7.640  -29.201 1.00 38.26  ? 59  ILE   A O   1 
ATOM   452  C  CB  . ILE   A 1 59  ? 40.864  -8.270  -32.045 1.00 41.40  ? 59  ILE   A CB  1 
ATOM   453  C  CG1 . ILE   A 1 59  ? 41.840  -9.461  -32.009 1.00 44.83  ? 59  ILE   A CG1 1 
ATOM   454  C  CG2 . ILE   A 1 59  ? 41.489  -7.058  -32.723 1.00 40.13  ? 59  ILE   A CG2 1 
ATOM   455  C  CD1 . ILE   A 1 59  ? 42.158  -10.046 -33.375 1.00 43.67  ? 59  ILE   A CD1 1 
ATOM   456  N  N   . ARG   A 1 60  ? 41.151  -5.761  -29.753 1.00 32.03  ? 60  ARG   A N   1 
ATOM   457  C  CA  . ARG   A 1 60  ? 42.053  -4.860  -29.049 1.00 32.25  ? 60  ARG   A CA  1 
ATOM   458  C  C   . ARG   A 1 60  ? 41.765  -4.778  -27.550 1.00 35.27  ? 60  ARG   A C   1 
ATOM   459  O  O   . ARG   A 1 60  ? 42.506  -4.104  -26.835 1.00 36.77  ? 60  ARG   A O   1 
ATOM   460  C  CB  . ARG   A 1 60  ? 41.914  -3.450  -29.639 1.00 31.78  ? 60  ARG   A CB  1 
ATOM   461  C  CG  . ARG   A 1 60  ? 42.203  -3.386  -31.136 1.00 29.85  ? 60  ARG   A CG  1 
ATOM   462  C  CD  . ARG   A 1 60  ? 42.079  -1.971  -31.725 1.00 28.35  ? 60  ARG   A CD  1 
ATOM   463  N  NE  . ARG   A 1 60  ? 42.309  -1.970  -33.175 1.00 28.48  ? 60  ARG   A NE  1 
ATOM   464  C  CZ  . ARG   A 1 60  ? 43.447  -1.672  -33.808 1.00 28.96  ? 60  ARG   A CZ  1 
ATOM   465  N  NH1 . ARG   A 1 60  ? 44.512  -1.337  -33.117 1.00 27.83  ? 60  ARG   A NH1 1 
ATOM   466  N  NH2 . ARG   A 1 60  ? 43.526  -1.700  -35.127 1.00 25.10  ? 60  ARG   A NH2 1 
ATOM   467  N  N   . LYS   A 1 61  ? 40.703  -5.452  -27.086 1.00 34.51  ? 61  LYS   A N   1 
ATOM   468  C  CA  . LYS   A 1 61  ? 40.289  -5.408  -25.693 1.00 38.39  ? 61  LYS   A CA  1 
ATOM   469  C  C   . LYS   A 1 61  ? 40.845  -6.594  -24.906 1.00 38.30  ? 61  LYS   A C   1 
ATOM   470  O  O   . LYS   A 1 61  ? 40.908  -7.717  -25.397 1.00 38.53  ? 61  LYS   A O   1 
ATOM   471  C  CB  . LYS   A 1 61  ? 38.765  -5.506  -25.544 1.00 39.41  ? 61  LYS   A CB  1 
ATOM   472  C  CG  . LYS   A 1 61  ? 38.013  -4.371  -26.187 1.00 42.38  ? 61  LYS   A CG  1 
ATOM   473  C  CD  . LYS   A 1 61  ? 38.179  -3.027  -25.501 1.00 43.84  ? 61  LYS   A CD  1 
ATOM   474  C  CE  . LYS   A 1 61  ? 37.847  -1.925  -26.444 1.00 45.37  ? 61  LYS   A CE  1 
ATOM   475  N  NZ  . LYS   A 1 61  ? 37.674  -0.693  -25.682 1.00 48.19  ? 61  LYS   A NZ  1 
ATOM   476  N  N   . SER   A 1 62  ? 41.216  -6.328  -23.653 1.00 40.18  ? 62  SER   A N   1 
ATOM   477  C  CA  . SER   A 1 62  ? 41.440  -7.389  -22.680 1.00 48.64  ? 62  SER   A CA  1 
ATOM   478  C  C   . SER   A 1 62  ? 40.247  -7.473  -21.724 1.00 48.06  ? 62  SER   A C   1 
ATOM   479  O  O   . SER   A 1 62  ? 39.438  -6.540  -21.621 1.00 42.32  ? 62  SER   A O   1 
ATOM   480  C  CB  . SER   A 1 62  ? 42.717  -7.156  -21.922 1.00 48.95  ? 62  SER   A CB  1 
ATOM   481  O  OG  . SER   A 1 62  ? 42.667  -5.884  -21.282 1.00 57.16  ? 62  SER   A OG  1 
ATOM   482  N  N   . ASN   A 1 63  ? 40.190  -8.595  -20.999 1.00 47.83  ? 63  ASN   A N   1 
ATOM   483  C  CA  . ASN   A 1 63  ? 39.142  -8.886  -20.037 1.00 45.30  ? 63  ASN   A CA  1 
ATOM   484  C  C   . ASN   A 1 63  ? 39.011  -7.795  -18.975 1.00 46.37  ? 63  ASN   A C   1 
ATOM   485  O  O   . ASN   A 1 63  ? 37.903  -7.466  -18.552 1.00 41.25  ? 63  ASN   A O   1 
ATOM   486  C  CB  . ASN   A 1 63  ? 39.406  -10.240 -19.402 1.00 49.22  ? 63  ASN   A CB  1 
ATOM   487  C  CG  . ASN   A 1 63  ? 39.261  -11.356 -20.403 1.00 50.86  ? 63  ASN   A CG  1 
ATOM   488  O  OD1 . ASN   A 1 63  ? 38.509  -11.228 -21.374 1.00 54.53  ? 63  ASN   A OD1 1 
ATOM   489  N  ND2 . ASN   A 1 63  ? 39.937  -12.469 -20.164 1.00 50.58  ? 63  ASN   A ND2 1 
ATOM   490  N  N   . HIS   A 1 64  ? 40.144  -7.226  -18.557 1.00 46.67  ? 64  HIS   A N   1 
ATOM   491  C  CA  . HIS   A 1 64  ? 40.169  -6.248  -17.482 1.00 46.25  ? 64  HIS   A CA  1 
ATOM   492  C  C   . HIS   A 1 64  ? 39.720  -4.881  -17.982 1.00 45.89  ? 64  HIS   A C   1 
ATOM   493  O  O   . HIS   A 1 64  ? 39.631  -3.945  -17.199 1.00 51.84  ? 64  HIS   A O   1 
ATOM   494  C  CB  . HIS   A 1 64  ? 41.550  -6.224  -16.810 1.00 54.64  ? 64  HIS   A CB  1 
ATOM   495  C  CG  . HIS   A 1 64  ? 42.710  -5.911  -17.712 1.00 58.43  ? 64  HIS   A CG  1 
ATOM   496  N  ND1 . HIS   A 1 64  ? 43.469  -6.900  -18.311 1.00 62.35  ? 64  HIS   A ND1 1 
ATOM   497  C  CD2 . HIS   A 1 64  ? 43.259  -4.742  -18.092 1.00 61.40  ? 64  HIS   A CD2 1 
ATOM   498  C  CE1 . HIS   A 1 64  ? 44.439  -6.343  -19.028 1.00 62.38  ? 64  HIS   A CE1 1 
ATOM   499  N  NE2 . HIS   A 1 64  ? 44.328  -5.030  -18.916 1.00 62.21  ? 64  HIS   A NE2 1 
ATOM   500  N  N   . ASN   A 1 65  ? 39.453  -4.751  -19.286 1.00 46.40  ? 65  ASN   A N   1 
ATOM   501  C  CA  . ASN   A 1 65  ? 38.854  -3.540  -19.829 1.00 45.69  ? 65  ASN   A CA  1 
ATOM   502  C  C   . ASN   A 1 65  ? 37.363  -3.447  -19.462 1.00 43.32  ? 65  ASN   A C   1 
ATOM   503  O  O   . ASN   A 1 65  ? 36.799  -2.364  -19.494 1.00 38.33  ? 65  ASN   A O   1 
ATOM   504  C  CB  . ASN   A 1 65  ? 39.021  -3.474  -21.347 1.00 49.20  ? 65  ASN   A CB  1 
ATOM   505  C  CG  . ASN   A 1 65  ? 40.446  -3.248  -21.812 1.00 49.79  ? 65  ASN   A CG  1 
ATOM   506  O  OD1 . ASN   A 1 65  ? 40.991  -4.034  -22.598 1.00 52.73  ? 65  ASN   A OD1 1 
ATOM   507  N  ND2 . ASN   A 1 65  ? 41.049  -2.147  -21.400 1.00 46.40  ? 65  ASN   A ND2 1 
ATOM   508  N  N   . PHE   A 1 66  ? 36.719  -4.579  -19.139 1.00 43.73  ? 66  PHE   A N   1 
ATOM   509  C  CA  . PHE   A 1 66  ? 35.297  -4.636  -18.813 1.00 43.13  ? 66  PHE   A CA  1 
ATOM   510  C  C   . PHE   A 1 66  ? 35.057  -4.737  -17.298 1.00 43.85  ? 66  PHE   A C   1 
ATOM   511  O  O   . PHE   A 1 66  ? 35.354  -5.776  -16.709 1.00 41.05  ? 66  PHE   A O   1 
ATOM   512  C  CB  . PHE   A 1 66  ? 34.689  -5.878  -19.478 1.00 42.07  ? 66  PHE   A CB  1 
ATOM   513  C  CG  . PHE   A 1 66  ? 34.773  -5.891  -20.996 1.00 47.39  ? 66  PHE   A CG  1 
ATOM   514  C  CD1 . PHE   A 1 66  ? 33.982  -5.033  -21.761 1.00 50.32  ? 66  PHE   A CD1 1 
ATOM   515  C  CD2 . PHE   A 1 66  ? 35.627  -6.766  -21.659 1.00 50.90  ? 66  PHE   A CD2 1 
ATOM   516  C  CE1 . PHE   A 1 66  ? 34.059  -5.040  -23.152 1.00 51.50  ? 66  PHE   A CE1 1 
ATOM   517  C  CE2 . PHE   A 1 66  ? 35.697  -6.773  -23.052 1.00 52.31  ? 66  PHE   A CE2 1 
ATOM   518  C  CZ  . PHE   A 1 66  ? 34.918  -5.907  -23.793 1.00 49.48  ? 66  PHE   A CZ  1 
ATOM   519  N  N   . LEU   A 1 67  ? 34.437  -3.695  -16.708 1.00 39.98  ? 67  LEU   A N   1 
ATOM   520  C  CA  . LEU   A 1 67  ? 34.013  -3.655  -15.305 1.00 43.68  ? 67  LEU   A CA  1 
ATOM   521  C  C   . LEU   A 1 67  ? 32.551  -4.084  -15.125 1.00 41.03  ? 67  LEU   A C   1 
ATOM   522  O  O   . LEU   A 1 67  ? 31.636  -3.331  -15.448 1.00 42.50  ? 67  LEU   A O   1 
ATOM   523  C  CB  . LEU   A 1 67  ? 34.218  -2.235  -14.781 1.00 44.69  ? 67  LEU   A CB  1 
ATOM   524  C  CG  . LEU   A 1 67  ? 35.661  -1.720  -14.836 1.00 56.90  ? 67  LEU   A CG  1 
ATOM   525  C  CD1 . LEU   A 1 67  ? 35.759  -0.201  -14.713 1.00 62.12  ? 67  LEU   A CD1 1 
ATOM   526  C  CD2 . LEU   A 1 67  ? 36.502  -2.408  -13.761 1.00 62.27  ? 67  LEU   A CD2 1 
ATOM   527  N  N   . VAL   A 1 68  ? 32.344  -5.292  -14.584 1.00 42.05  ? 68  VAL   A N   1 
ATOM   528  C  CA  . VAL   A 1 68  ? 31.019  -5.814  -14.273 1.00 43.94  ? 68  VAL   A CA  1 
ATOM   529  C  C   . VAL   A 1 68  ? 30.790  -5.732  -12.766 1.00 45.48  ? 68  VAL   A C   1 
ATOM   530  O  O   . VAL   A 1 68  ? 31.673  -6.086  -11.988 1.00 41.62  ? 68  VAL   A O   1 
ATOM   531  C  CB  . VAL   A 1 68  ? 30.799  -7.263  -14.737 1.00 39.93  ? 68  VAL   A CB  1 
ATOM   532  C  CG1 . VAL   A 1 68  ? 29.357  -7.695  -14.526 1.00 43.25  ? 68  VAL   A CG1 1 
ATOM   533  C  CG2 . VAL   A 1 68  ? 31.213  -7.471  -16.184 1.00 43.95  ? 68  VAL   A CG2 1 
ATOM   534  N  N   . GLN   A 1 69  ? 29.565  -5.345  -12.383 1.00 42.14  ? 69  GLN   A N   1 
ATOM   535  C  CA  . GLN   A 1 69  ? 29.192  -5.130  -10.995 1.00 43.98  ? 69  GLN   A CA  1 
ATOM   536  C  C   . GLN   A 1 69  ? 27.744  -5.574  -10.735 1.00 43.86  ? 69  GLN   A C   1 
ATOM   537  O  O   . GLN   A 1 69  ? 26.819  -5.100  -11.391 1.00 36.08  ? 69  GLN   A O   1 
ATOM   538  C  CB  . GLN   A 1 69  ? 29.445  -3.641  -10.795 1.00 48.71  ? 69  GLN   A CB  1 
ATOM   539  C  CG  . GLN   A 1 69  ? 29.311  -3.161  -9.357  1.00 58.07  ? 69  GLN   A CG  1 
ATOM   540  C  CD  . GLN   A 1 69  ? 29.623  -1.688  -9.229  1.00 60.95  ? 69  GLN   A CD  1 
ATOM   541  O  OE1 . GLN   A 1 69  ? 30.545  -1.174  -9.876  1.00 58.74  ? 69  GLN   A OE1 1 
ATOM   542  N  NE2 . GLN   A 1 69  ? 28.834  -0.990  -8.425  1.00 65.12  ? 69  GLN   A NE2 1 
ATOM   543  N  N   . ALA   A 1 70  ? 27.561  -6.505  -9.786  1.00 44.02  ? 70  ALA   A N   1 
ATOM   544  C  CA  . ALA   A 1 70  ? 26.253  -6.949  -9.332  1.00 43.75  ? 70  ALA   A CA  1 
ATOM   545  C  C   . ALA   A 1 70  ? 26.050  -6.450  -7.907  1.00 47.13  ? 70  ALA   A C   1 
ATOM   546  O  O   . ALA   A 1 70  ? 26.678  -6.971  -6.988  1.00 47.97  ? 70  ALA   A O   1 
ATOM   547  C  CB  . ALA   A 1 70  ? 26.147  -8.455  -9.404  1.00 41.77  ? 70  ALA   A CB  1 
ATOM   548  N  N   . GLY   A 1 71  ? 25.170  -5.453  -7.747  1.00 46.97  ? 71  GLY   A N   1 
ATOM   549  C  CA  . GLY   A 1 71  ? 25.100  -4.649  -6.537  1.00 52.23  ? 71  GLY   A CA  1 
ATOM   550  C  C   . GLY   A 1 71  ? 26.468  -4.075  -6.178  1.00 57.67  ? 71  GLY   A C   1 
ATOM   551  O  O   . GLY   A 1 71  ? 27.036  -3.292  -6.928  1.00 64.42  ? 71  GLY   A O   1 
ATOM   552  N  N   . ASN   A 1 72  ? 27.004  -4.495  -5.029  1.00 68.01  ? 72  ASN   A N   1 
ATOM   553  C  CA  . ASN   A 1 72  ? 28.316  -4.063  -4.576  1.00 66.03  ? 72  ASN   A CA  1 
ATOM   554  C  C   . ASN   A 1 72  ? 29.414  -4.969  -5.124  1.00 63.27  ? 72  ASN   A C   1 
ATOM   555  O  O   . ASN   A 1 72  ? 30.528  -4.517  -5.344  1.00 69.02  ? 72  ASN   A O   1 
ATOM   556  C  CB  . ASN   A 1 72  ? 28.402  -4.041  -3.056  1.00 71.15  ? 72  ASN   A CB  1 
ATOM   557  C  CG  . ASN   A 1 72  ? 27.771  -2.797  -2.484  1.00 78.56  ? 72  ASN   A CG  1 
ATOM   558  O  OD1 . ASN   A 1 72  ? 27.044  -2.080  -3.184  1.00 79.95  ? 72  ASN   A OD1 1 
ATOM   559  N  ND2 . ASN   A 1 72  ? 28.040  -2.526  -1.216  1.00 79.44  ? 72  ASN   A ND2 1 
ATOM   560  N  N   . VAL   A 1 73  ? 29.112  -6.251  -5.314  1.00 61.53  ? 73  VAL   A N   1 
ATOM   561  C  CA  . VAL   A 1 73  ? 30.115  -7.194  -5.777  1.00 59.76  ? 73  VAL   A CA  1 
ATOM   562  C  C   . VAL   A 1 73  ? 30.638  -6.732  -7.141  1.00 60.87  ? 73  VAL   A C   1 
ATOM   563  O  O   . VAL   A 1 73  ? 29.876  -6.336  -8.019  1.00 51.65  ? 73  VAL   A O   1 
ATOM   564  C  CB  . VAL   A 1 73  ? 29.592  -8.646  -5.855  1.00 58.65  ? 73  VAL   A CB  1 
ATOM   565  C  CG1 . VAL   A 1 73  ? 30.676  -9.639  -6.280  1.00 58.36  ? 73  VAL   A CG1 1 
ATOM   566  C  CG2 . VAL   A 1 73  ? 28.951  -9.102  -4.550  1.00 60.38  ? 73  VAL   A CG2 1 
ATOM   567  N  N   . GLN   A 1 74  ? 31.961  -6.805  -7.311  1.00 56.24  ? 74  GLN   A N   1 
ATOM   568  C  CA  . GLN   A 1 74  ? 32.575  -6.738  -8.621  1.00 52.23  ? 74  GLN   A CA  1 
ATOM   569  C  C   . GLN   A 1 74  ? 32.823  -8.167  -9.096  1.00 45.12  ? 74  GLN   A C   1 
ATOM   570  O  O   . GLN   A 1 74  ? 33.507  -8.919  -8.423  1.00 49.10  ? 74  GLN   A O   1 
ATOM   571  C  CB  . GLN   A 1 74  ? 33.809  -5.860  -8.442  1.00 57.33  ? 74  GLN   A CB  1 
ATOM   572  C  CG  . GLN   A 1 74  ? 34.480  -5.435  -9.739  1.00 62.88  ? 74  GLN   A CG  1 
ATOM   573  C  CD  . GLN   A 1 74  ? 35.815  -4.765  -9.495  1.00 75.93  ? 74  GLN   A CD  1 
ATOM   574  O  OE1 . GLN   A 1 74  ? 36.860  -5.203  -9.994  1.00 77.01  ? 74  GLN   A OE1 1 
ATOM   575  N  NE2 . GLN   A 1 74  ? 35.789  -3.703  -8.699  1.00 81.00  ? 74  GLN   A NE2 1 
ATOM   576  N  N   . LEU   A 1 75  ? 32.207  -8.547  -10.224 1.00 46.28  ? 75  LEU   A N   1 
ATOM   577  C  CA  . LEU   A 1 75  ? 32.459  -9.814  -10.889 1.00 47.42  ? 75  LEU   A CA  1 
ATOM   578  C  C   . LEU   A 1 75  ? 33.711  -9.651  -11.738 1.00 48.75  ? 75  LEU   A C   1 
ATOM   579  O  O   . LEU   A 1 75  ? 34.081  -8.537  -12.092 1.00 53.97  ? 75  LEU   A O   1 
ATOM   580  C  CB  . LEU   A 1 75  ? 31.295  -10.242 -11.784 1.00 51.17  ? 75  LEU   A CB  1 
ATOM   581  C  CG  . LEU   A 1 75  ? 30.040  -10.769 -11.090 1.00 55.28  ? 75  LEU   A CG  1 
ATOM   582  C  CD1 . LEU   A 1 75  ? 28.891  -10.782 -12.076 1.00 54.77  ? 75  LEU   A CD1 1 
ATOM   583  C  CD2 . LEU   A 1 75  ? 30.276  -12.169 -10.538 1.00 56.93  ? 75  LEU   A CD2 1 
ATOM   584  N  N   . ARG   A 1 76  ? 34.340  -10.774 -12.081 1.00 47.31  ? 76  ARG   A N   1 
ATOM   585  C  CA  . ARG   A 1 76  ? 35.605  -10.724 -12.791 1.00 48.30  ? 76  ARG   A CA  1 
ATOM   586  C  C   . ARG   A 1 76  ? 35.440  -11.482 -14.107 1.00 41.57  ? 76  ARG   A C   1 
ATOM   587  O  O   . ARG   A 1 76  ? 34.999  -12.634 -14.114 1.00 39.70  ? 76  ARG   A O   1 
ATOM   588  C  CB  . ARG   A 1 76  ? 36.686  -11.255 -11.842 1.00 55.90  ? 76  ARG   A CB  1 
ATOM   589  C  CG  . ARG   A 1 76  ? 38.113  -11.182 -12.364 1.00 60.71  ? 76  ARG   A CG  1 
ATOM   590  C  CD  . ARG   A 1 76  ? 39.124  -11.810 -11.411 1.00 64.83  ? 76  ARG   A CD  1 
ATOM   591  N  NE  . ARG   A 1 76  ? 40.077  -12.612 -12.187 1.00 66.86  ? 76  ARG   A NE  1 
ATOM   592  C  CZ  . ARG   A 1 76  ? 40.020  -13.940 -12.345 1.00 74.91  ? 76  ARG   A CZ  1 
ATOM   593  N  NH1 . ARG   A 1 76  ? 39.078  -14.648 -11.731 1.00 77.11  ? 76  ARG   A NH1 1 
ATOM   594  N  NH2 . ARG   A 1 76  ? 40.915  -14.560 -13.105 1.00 68.99  ? 76  ARG   A NH2 1 
ATOM   595  N  N   . VAL   A 1 77  ? 35.797  -10.808 -15.210 1.00 42.40  ? 77  VAL   A N   1 
ATOM   596  C  CA  . VAL   A 1 77  ? 35.624  -11.343 -16.554 1.00 40.18  ? 77  VAL   A CA  1 
ATOM   597  C  C   . VAL   A 1 77  ? 36.857  -12.160 -16.920 1.00 38.53  ? 77  VAL   A C   1 
ATOM   598  O  O   . VAL   A 1 77  ? 37.962  -11.687 -16.709 1.00 39.31  ? 77  VAL   A O   1 
ATOM   599  C  CB  . VAL   A 1 77  ? 35.413  -10.186 -17.554 1.00 44.80  ? 77  VAL   A CB  1 
ATOM   600  C  CG1 . VAL   A 1 77  ? 35.350  -10.672 -19.006 1.00 43.72  ? 77  VAL   A CG1 1 
ATOM   601  C  CG2 . VAL   A 1 77  ? 34.199  -9.322  -17.207 1.00 42.07  ? 77  VAL   A CG2 1 
ATOM   602  N  N   . ILE   A 1 78  ? 36.652  -13.344 -17.506 1.00 42.46  ? 78  ILE   A N   1 
ATOM   603  C  CA  . ILE   A 1 78  ? 37.730  -14.266 -17.836 1.00 48.32  ? 78  ILE   A CA  1 
ATOM   604  C  C   . ILE   A 1 78  ? 37.703  -14.654 -19.322 1.00 52.09  ? 78  ILE   A C   1 
ATOM   605  O  O   . ILE   A 1 78  ? 38.390  -15.589 -19.725 1.00 44.30  ? 78  ILE   A O   1 
ATOM   606  C  CB  . ILE   A 1 78  ? 37.656  -15.518 -16.931 1.00 49.44  ? 78  ILE   A CB  1 
ATOM   607  C  CG1 . ILE   A 1 78  ? 36.330  -16.262 -17.060 1.00 47.21  ? 78  ILE   A CG1 1 
ATOM   608  C  CG2 . ILE   A 1 78  ? 37.937  -15.155 -15.475 1.00 50.66  ? 78  ILE   A CG2 1 
ATOM   609  C  CD1 . ILE   A 1 78  ? 36.303  -17.594 -16.333 1.00 44.85  ? 78  ILE   A CD1 1 
ATOM   610  N  N   . GLY   A 1 79  ? 36.936  -13.938 -20.159 1.00 53.88  ? 79  GLY   A N   1 
ATOM   611  C  CA  . GLY   A 1 79  ? 36.789  -14.315 -21.562 1.00 51.23  ? 79  GLY   A CA  1 
ATOM   612  C  C   . GLY   A 1 79  ? 35.699  -13.489 -22.244 1.00 49.99  ? 79  GLY   A C   1 
ATOM   613  O  O   . GLY   A 1 79  ? 34.778  -13.039 -21.572 1.00 43.49  ? 79  GLY   A O   1 
ATOM   614  N  N   . HIS   A 1 80  ? 35.824  -13.264 -23.564 1.00 48.03  ? 80  HIS   A N   1 
ATOM   615  C  CA  . HIS   A 1 80  ? 34.834  -12.494 -24.304 1.00 43.69  ? 80  HIS   A CA  1 
ATOM   616  C  C   . HIS   A 1 80  ? 34.710  -13.035 -25.724 1.00 42.97  ? 80  HIS   A C   1 
ATOM   617  O  O   . HIS   A 1 80  ? 35.696  -13.483 -26.290 1.00 37.37  ? 80  HIS   A O   1 
ATOM   618  C  CB  . HIS   A 1 80  ? 35.147  -10.995 -24.251 1.00 43.07  ? 80  HIS   A CB  1 
ATOM   619  C  CG  . HIS   A 1 80  ? 36.415  -10.562 -24.923 1.00 52.30  ? 80  HIS   A CG  1 
ATOM   620  N  ND1 . HIS   A 1 80  ? 37.587  -10.344 -24.231 1.00 60.12  ? 80  HIS   A ND1 1 
ATOM   621  C  CD2 . HIS   A 1 80  ? 36.694  -10.264 -26.202 1.00 53.28  ? 80  HIS   A CD2 1 
ATOM   622  C  CE1 . HIS   A 1 80  ? 38.533  -9.945  -25.072 1.00 59.57  ? 80  HIS   A CE1 1 
ATOM   623  N  NE2 . HIS   A 1 80  ? 38.010  -9.883  -26.273 1.00 56.24  ? 80  HIS   A NE2 1 
ATOM   624  N  N   . SER   A 1 81  ? 33.478  -13.020 -26.257 1.00 37.61  ? 81  SER   A N   1 
ATOM   625  C  CA  . SER   A 1 81  ? 33.195  -13.280 -27.659 1.00 35.41  ? 81  SER   A CA  1 
ATOM   626  C  C   . SER   A 1 81  ? 31.955  -12.491 -28.098 1.00 37.75  ? 81  SER   A C   1 
ATOM   627  O  O   . SER   A 1 81  ? 31.225  -11.947 -27.276 1.00 38.19  ? 81  SER   A O   1 
ATOM   628  C  CB  . SER   A 1 81  ? 33.007  -14.736 -27.889 1.00 37.60  ? 81  SER   A CB  1 
ATOM   629  O  OG  . SER   A 1 81  ? 31.725  -15.143 -27.441 1.00 39.27  ? 81  SER   A OG  1 
ATOM   630  N  N   . MET   A 1 82  ? 31.697  -12.476 -29.403 1.00 33.76  ? 82  MET   A N   1 
ATOM   631  C  CA  . MET   A 1 82  ? 30.611  -11.723 -29.997 1.00 37.76  ? 82  MET   A CA  1 
ATOM   632  C  C   . MET   A 1 82  ? 29.712  -12.716 -30.722 1.00 35.08  ? 82  MET   A C   1 
ATOM   633  O  O   . MET   A 1 82  ? 30.251  -13.598 -31.382 1.00 33.34  ? 82  MET   A O   1 
ATOM   634  C  CB  . MET   A 1 82  ? 31.226  -10.719 -30.981 1.00 37.84  ? 82  MET   A CB  1 
ATOM   635  C  CG  . MET   A 1 82  ? 30.267  -9.827  -31.742 1.00 40.42  ? 82  MET   A CG  1 
ATOM   636  S  SD  . MET   A 1 82  ? 31.122  -8.338  -32.313 1.00 37.44  ? 82  MET   A SD  1 
ATOM   637  C  CE  . MET   A 1 82  ? 32.191  -9.000  -33.605 1.00 39.86  ? 82  MET   A CE  1 
ATOM   638  N  N   . GLN   A 1 83  ? 28.378  -12.567 -30.602 1.00 30.59  ? 83  GLN   A N   1 
ATOM   639  C  CA  . GLN   A 1 83  ? 27.441  -13.280 -31.458 1.00 28.33  ? 83  GLN   A CA  1 
ATOM   640  C  C   . GLN   A 1 83  ? 26.429  -12.305 -32.059 1.00 28.21  ? 83  GLN   A C   1 
ATOM   641  O  O   . GLN   A 1 83  ? 25.545  -11.806 -31.353 1.00 25.88  ? 83  GLN   A O   1 
ATOM   642  C  CB  . GLN   A 1 83  ? 26.697  -14.366 -30.684 1.00 31.07  ? 83  GLN   A CB  1 
ATOM   643  C  CG  . GLN   A 1 83  ? 25.683  -15.166 -31.503 1.00 29.54  ? 83  GLN   A CG  1 
ATOM   644  C  CD  . GLN   A 1 83  ? 24.905  -16.125 -30.633 1.00 31.33  ? 83  GLN   A CD  1 
ATOM   645  O  OE1 . GLN   A 1 83  ? 25.047  -16.129 -29.405 1.00 31.71  ? 83  GLN   A OE1 1 
ATOM   646  N  NE2 . GLN   A 1 83  ? 24.082  -16.954 -31.258 1.00 30.37  ? 83  GLN   A NE2 1 
ATOM   647  N  N   . ASN   A 1 84  ? 26.582  -12.059 -33.368 1.00 25.15  ? 84  ASN   A N   1 
ATOM   648  C  CA  . ASN   A 1 84  ? 25.835  -11.047 -34.092 1.00 25.65  ? 84  ASN   A CA  1 
ATOM   649  C  C   . ASN   A 1 84  ? 26.038  -9.716  -33.369 1.00 24.86  ? 84  ASN   A C   1 
ATOM   650  O  O   . ASN   A 1 84  ? 27.184  -9.314  -33.209 1.00 27.35  ? 84  ASN   A O   1 
ATOM   651  C  CB  . ASN   A 1 84  ? 24.389  -11.486 -34.314 1.00 24.70  ? 84  ASN   A CB  1 
ATOM   652  C  CG  . ASN   A 1 84  ? 24.304  -12.818 -35.015 1.00 25.76  ? 84  ASN   A CG  1 
ATOM   653  O  OD1 . ASN   A 1 84  ? 24.777  -12.968 -36.143 1.00 27.37  ? 84  ASN   A OD1 1 
ATOM   654  N  ND2 . ASN   A 1 84  ? 23.703  -13.803 -34.374 1.00 27.44  ? 84  ASN   A ND2 1 
ATOM   655  N  N   . CYS   A 1 85  ? 24.951  -9.075  -32.872 1.00 24.74  ? 85  CYS   A N   1 
ATOM   656  C  CA  . CYS   A 1 85  ? 25.040  -7.743  -32.271 1.00 24.08  ? 85  CYS   A CA  1 
ATOM   657  C  C   . CYS   A 1 85  ? 25.075  -7.768  -30.730 1.00 23.55  ? 85  CYS   A C   1 
ATOM   658  O  O   . CYS   A 1 85  ? 24.974  -6.718  -30.078 1.00 22.80  ? 85  CYS   A O   1 
ATOM   659  C  CB  . CYS   A 1 85  ? 23.916  -6.850  -32.786 1.00 25.10  ? 85  CYS   A CB  1 
ATOM   660  S  SG  . CYS   A 1 85  ? 23.949  -6.524  -34.569 1.00 26.50  ? 85  CYS   A SG  1 
ATOM   661  N  N   . VAL   A 1 86  ? 25.260  -8.959  -30.141 1.00 23.98  ? 86  VAL   A N   1 
ATOM   662  C  CA  . VAL   A 1 86  ? 25.345  -9.140  -28.701 1.00 27.69  ? 86  VAL   A CA  1 
ATOM   663  C  C   . VAL   A 1 86  ? 26.774  -9.530  -28.282 1.00 28.91  ? 86  VAL   A C   1 
ATOM   664  O  O   . VAL   A 1 86  ? 27.410  -10.376 -28.915 1.00 25.45  ? 86  VAL   A O   1 
ATOM   665  C  CB  . VAL   A 1 86  ? 24.298  -10.186 -28.255 1.00 31.33  ? 86  VAL   A CB  1 
ATOM   666  C  CG1 . VAL   A 1 86  ? 24.621  -10.834 -26.918 1.00 34.88  ? 86  VAL   A CG1 1 
ATOM   667  C  CG2 . VAL   A 1 86  ? 22.904  -9.560  -28.188 1.00 34.51  ? 86  VAL   A CG2 1 
ATOM   668  N  N   . LEU   A 1 87  ? 27.222  -8.938  -27.162 1.00 28.88  ? 87  LEU   A N   1 
ATOM   669  C  CA  . LEU   A 1 87  ? 28.479  -9.282  -26.518 1.00 32.63  ? 87  LEU   A CA  1 
ATOM   670  C  C   . LEU   A 1 87  ? 28.259  -10.258 -25.355 1.00 36.29  ? 87  LEU   A C   1 
ATOM   671  O  O   . LEU   A 1 87  ? 27.304  -10.118 -24.592 1.00 31.60  ? 87  LEU   A O   1 
ATOM   672  C  CB  . LEU   A 1 87  ? 29.093  -7.981  -26.022 1.00 32.26  ? 87  LEU   A CB  1 
ATOM   673  C  CG  . LEU   A 1 87  ? 30.529  -8.095  -25.490 1.00 39.46  ? 87  LEU   A CG  1 
ATOM   674  C  CD1 . LEU   A 1 87  ? 31.531  -8.484  -26.577 1.00 39.68  ? 87  LEU   A CD1 1 
ATOM   675  C  CD2 . LEU   A 1 87  ? 30.928  -6.781  -24.841 1.00 42.41  ? 87  LEU   A CD2 1 
ATOM   676  N  N   . LYS   A 1 88  ? 29.172  -11.234 -25.222 1.00 35.98  ? 88  LYS   A N   1 
ATOM   677  C  CA  . LYS   A 1 88  ? 29.126  -12.273 -24.197 1.00 35.93  ? 88  LYS   A CA  1 
ATOM   678  C  C   . LYS   A 1 88  ? 30.398  -12.215 -23.355 1.00 37.43  ? 88  LYS   A C   1 
ATOM   679  O  O   . LYS   A 1 88  ? 31.469  -12.592 -23.833 1.00 38.58  ? 88  LYS   A O   1 
ATOM   680  C  CB  . LYS   A 1 88  ? 28.971  -13.651 -24.853 1.00 34.21  ? 88  LYS   A CB  1 
ATOM   681  C  CG  . LYS   A 1 88  ? 27.704  -13.744 -25.681 1.00 38.04  ? 88  LYS   A CG  1 
ATOM   682  C  CD  . LYS   A 1 88  ? 27.110  -15.129 -25.924 1.00 37.26  ? 88  LYS   A CD  1 
ATOM   683  C  CE  . LYS   A 1 88  ? 27.797  -15.816 -27.039 1.00 42.24  ? 88  LYS   A CE  1 
ATOM   684  N  NZ  . LYS   A 1 88  ? 26.959  -16.892 -27.552 1.00 47.65  ? 88  LYS   A NZ  1 
ATOM   685  N  N   . LEU   A 1 89  ? 30.277  -11.686 -22.126 1.00 36.10  ? 89  LEU   A N   1 
ATOM   686  C  CA  . LEU   A 1 89  ? 31.370  -11.652 -21.169 1.00 34.26  ? 89  LEU   A CA  1 
ATOM   687  C  C   . LEU   A 1 89  ? 31.301  -12.888 -20.271 1.00 40.21  ? 89  LEU   A C   1 
ATOM   688  O  O   . LEU   A 1 89  ? 30.303  -13.079 -19.575 1.00 46.15  ? 89  LEU   A O   1 
ATOM   689  C  CB  . LEU   A 1 89  ? 31.290  -10.378 -20.340 1.00 32.78  ? 89  LEU   A CB  1 
ATOM   690  C  CG  . LEU   A 1 89  ? 31.234  -9.072  -21.123 1.00 31.60  ? 89  LEU   A CG  1 
ATOM   691  C  CD1 . LEU   A 1 89  ? 31.158  -7.964  -20.108 1.00 31.95  ? 89  LEU   A CD1 1 
ATOM   692  C  CD2 . LEU   A 1 89  ? 32.422  -8.889  -22.051 1.00 33.78  ? 89  LEU   A CD2 1 
ATOM   693  N  N   . LYS   A 1 90  ? 32.357  -13.722 -20.283 1.00 40.14  ? 90  LYS   A N   1 
ATOM   694  C  CA  . LYS   A 1 90  ? 32.434  -14.872 -19.394 1.00 41.01  ? 90  LYS   A CA  1 
ATOM   695  C  C   . LYS   A 1 90  ? 32.995  -14.420 -18.053 1.00 41.06  ? 90  LYS   A C   1 
ATOM   696  O  O   . LYS   A 1 90  ? 33.946  -13.628 -18.019 1.00 37.16  ? 90  LYS   A O   1 
ATOM   697  C  CB  . LYS   A 1 90  ? 33.323  -15.975 -19.965 1.00 47.02  ? 90  LYS   A CB  1 
ATOM   698  C  CG  . LYS   A 1 90  ? 33.093  -17.318 -19.313 1.00 52.82  ? 90  LYS   A CG  1 
ATOM   699  C  CD  . LYS   A 1 90  ? 33.552  -18.481 -20.175 1.00 63.55  ? 90  LYS   A CD  1 
ATOM   700  C  CE  . LYS   A 1 90  ? 32.969  -19.769 -19.699 1.00 74.11  ? 90  LYS   A CE  1 
ATOM   701  N  NZ  . LYS   A 1 90  ? 33.470  -20.903 -20.480 1.00 80.59  ? 90  LYS   A NZ  1 
ATOM   702  N  N   . VAL   A 1 91  ? 32.388  -14.912 -16.956 1.00 40.50  ? 91  VAL   A N   1 
ATOM   703  C  CA  . VAL   A 1 91  ? 32.777  -14.474 -15.622 1.00 42.06  ? 91  VAL   A CA  1 
ATOM   704  C  C   . VAL   A 1 91  ? 33.101  -15.686 -14.746 1.00 40.89  ? 91  VAL   A C   1 
ATOM   705  O  O   . VAL   A 1 91  ? 32.690  -16.803 -15.050 1.00 40.89  ? 91  VAL   A O   1 
ATOM   706  C  CB  . VAL   A 1 91  ? 31.728  -13.556 -14.962 1.00 45.49  ? 91  VAL   A CB  1 
ATOM   707  C  CG1 . VAL   A 1 91  ? 31.811  -12.132 -15.504 1.00 50.32  ? 91  VAL   A CG1 1 
ATOM   708  C  CG2 . VAL   A 1 91  ? 30.314  -14.110 -15.075 1.00 44.85  ? 91  VAL   A CG2 1 
ATOM   709  N  N   . ASP   A 1 92  ? 33.830  -15.430 -13.648 1.00 45.38  ? 92  ASP   A N   1 
ATOM   710  C  CA  . ASP   A 1 92  ? 34.348  -16.478 -12.772 1.00 49.61  ? 92  ASP   A CA  1 
ATOM   711  C  C   . ASP   A 1 92  ? 33.318  -16.979 -11.755 1.00 51.96  ? 92  ASP   A C   1 
ATOM   712  O  O   . ASP   A 1 92  ? 33.651  -17.894 -11.019 1.00 46.34  ? 92  ASP   A O   1 
ATOM   713  C  CB  . ASP   A 1 92  ? 35.587  -16.030 -12.007 1.00 51.19  ? 92  ASP   A CB  1 
ATOM   714  C  CG  . ASP   A 1 92  ? 35.391  -14.873 -11.037 1.00 54.02  ? 92  ASP   A CG  1 
ATOM   715  O  OD1 . ASP   A 1 92  ? 34.296  -14.258 -11.054 1.00 52.97  ? 92  ASP   A OD1 1 
ATOM   716  O  OD2 . ASP   A 1 92  ? 36.334  -14.602 -10.263 1.00 54.79  ? 92  ASP   A OD2 1 
ATOM   717  N  N   . THR   A 1 93  ? 32.109  -16.379 -11.680 1.00 51.46  ? 93  THR   A N   1 
ATOM   718  C  CA  . THR   A 1 93  ? 31.028  -16.874 -10.825 1.00 44.09  ? 93  THR   A CA  1 
ATOM   719  C  C   . THR   A 1 93  ? 29.778  -17.137 -11.663 1.00 42.31  ? 93  THR   A C   1 
ATOM   720  O  O   . THR   A 1 93  ? 29.391  -16.316 -12.496 1.00 37.92  ? 93  THR   A O   1 
ATOM   721  C  CB  . THR   A 1 93  ? 30.668  -15.859 -9.739  1.00 47.94  ? 93  THR   A CB  1 
ATOM   722  O  OG1 . THR   A 1 93  ? 31.824  -15.268 -9.161  1.00 45.49  ? 93  THR   A OG1 1 
ATOM   723  C  CG2 . THR   A 1 93  ? 29.844  -16.483 -8.627  1.00 48.64  ? 93  THR   A CG2 1 
ATOM   724  N  N   . ALA   A 1 94  ? 29.114  -18.259 -11.391 1.00 35.94  ? 94  ALA   A N   1 
ATOM   725  C  CA  . ALA   A 1 94  ? 27.769  -18.513 -11.880 1.00 34.71  ? 94  ALA   A CA  1 
ATOM   726  C  C   . ALA   A 1 94  ? 26.754  -17.806 -10.970 1.00 37.48  ? 94  ALA   A C   1 
ATOM   727  O  O   . ALA   A 1 94  ? 26.939  -17.765 -9.750  1.00 36.48  ? 94  ALA   A O   1 
ATOM   728  C  CB  . ALA   A 1 94  ? 27.531  -19.995 -11.934 1.00 34.28  ? 94  ALA   A CB  1 
ATOM   729  N  N   . ASN   A 1 95  ? 25.698  -17.223 -11.570 1.00 39.29  ? 95  ASN   A N   1 
ATOM   730  C  CA  . ASN   A 1 95  ? 24.707  -16.439 -10.834 1.00 37.53  ? 95  ASN   A CA  1 
ATOM   731  C  C   . ASN   A 1 95  ? 23.836  -17.394 -10.015 1.00 33.19  ? 95  ASN   A C   1 
ATOM   732  O  O   . ASN   A 1 95  ? 23.084  -18.200 -10.581 1.00 29.95  ? 95  ASN   A O   1 
ATOM   733  C  CB  . ASN   A 1 95  ? 23.840  -15.587 -11.763 1.00 39.24  ? 95  ASN   A CB  1 
ATOM   734  C  CG  . ASN   A 1 95  ? 22.777  -14.770 -11.049 1.00 40.45  ? 95  ASN   A CG  1 
ATOM   735  O  OD1 . ASN   A 1 95  ? 22.745  -14.713 -9.814  1.00 37.52  ? 95  ASN   A OD1 1 
ATOM   736  N  ND2 . ASN   A 1 95  ? 21.914  -14.096 -11.804 1.00 37.70  ? 95  ASN   A ND2 1 
ATOM   737  N  N   . PRO   A 1 96  ? 23.870  -17.313 -8.665  1.00 34.86  ? 96  PRO   A N   1 
ATOM   738  C  CA  . PRO   A 1 96  ? 23.051  -18.211 -7.841  1.00 37.84  ? 96  PRO   A CA  1 
ATOM   739  C  C   . PRO   A 1 96  ? 21.538  -18.053 -8.026  1.00 37.21  ? 96  PRO   A C   1 
ATOM   740  O  O   . PRO   A 1 96  ? 20.810  -19.009 -7.816  1.00 39.89  ? 96  PRO   A O   1 
ATOM   741  C  CB  . PRO   A 1 96  ? 23.525  -17.930 -6.399  1.00 37.45  ? 96  PRO   A CB  1 
ATOM   742  C  CG  . PRO   A 1 96  ? 24.181  -16.559 -6.447  1.00 38.16  ? 96  PRO   A CG  1 
ATOM   743  C  CD  . PRO   A 1 96  ? 24.663  -16.352 -7.875  1.00 36.80  ? 96  PRO   A CD  1 
ATOM   744  N  N   . LYS   A 1 97  ? 21.070  -16.894 -8.520  1.00 39.79  ? 97  LYS   A N   1 
ATOM   745  C  CA  . LYS   A 1 97  ? 19.642  -16.634 -8.732  1.00 39.51  ? 97  LYS   A CA  1 
ATOM   746  C  C   . LYS   A 1 97  ? 19.171  -16.905 -10.167 1.00 38.37  ? 97  LYS   A C   1 
ATOM   747  O  O   . LYS   A 1 97  ? 18.074  -16.481 -10.546 1.00 36.50  ? 97  LYS   A O   1 
ATOM   748  C  CB  . LYS   A 1 97  ? 19.370  -15.149 -8.461  1.00 41.08  ? 97  LYS   A CB  1 
ATOM   749  C  CG  . LYS   A 1 97  ? 19.901  -14.627 -7.137  1.00 43.87  ? 97  LYS   A CG  1 
ATOM   750  C  CD  . LYS   A 1 97  ? 19.407  -13.227 -6.811  1.00 47.38  ? 97  LYS   A CD  1 
ATOM   751  C  CE  . LYS   A 1 97  ? 20.084  -12.662 -5.606  1.00 52.49  ? 97  LYS   A CE  1 
ATOM   752  N  NZ  . LYS   A 1 97  ? 19.172  -11.774 -4.882  1.00 56.45  ? 97  LYS   A NZ  1 
ATOM   753  N  N   . THR   A 1 98  ? 20.004  -17.561 -10.991 1.00 33.21  ? 98  THR   A N   1 
ATOM   754  C  CA  . THR   A 1 98  ? 19.648  -17.855 -12.368 1.00 32.76  ? 98  THR   A CA  1 
ATOM   755  C  C   . THR   A 1 98  ? 18.370  -18.677 -12.368 1.00 34.15  ? 98  THR   A C   1 
ATOM   756  O  O   . THR   A 1 98  ? 18.322  -19.691 -11.700 1.00 40.56  ? 98  THR   A O   1 
ATOM   757  C  CB  . THR   A 1 98  ? 20.785  -18.602 -13.068 1.00 33.11  ? 98  THR   A CB  1 
ATOM   758  O  OG1 . THR   A 1 98  ? 21.907  -17.722 -13.110 1.00 31.08  ? 98  THR   A OG1 1 
ATOM   759  C  CG2 . THR   A 1 98  ? 20.416  -19.021 -14.475 1.00 31.92  ? 98  THR   A CG2 1 
ATOM   760  N  N   . PRO   A 1 99  ? 17.284  -18.246 -13.047 1.00 33.95  ? 99  PRO   A N   1 
ATOM   761  C  CA  . PRO   A 1 99  ? 16.068  -19.046 -13.145 1.00 31.89  ? 99  PRO   A CA  1 
ATOM   762  C  C   . PRO   A 1 99  ? 16.150  -20.101 -14.236 1.00 34.45  ? 99  PRO   A C   1 
ATOM   763  O  O   . PRO   A 1 99  ? 17.109  -20.131 -14.989 1.00 38.57  ? 99  PRO   A O   1 
ATOM   764  C  CB  . PRO   A 1 99  ? 15.014  -17.969 -13.469 1.00 34.04  ? 99  PRO   A CB  1 
ATOM   765  C  CG  . PRO   A 1 99  ? 15.772  -16.976 -14.329 1.00 34.31  ? 99  PRO   A CG  1 
ATOM   766  C  CD  . PRO   A 1 99  ? 17.156  -16.934 -13.713 1.00 35.49  ? 99  PRO   A CD  1 
ATOM   767  N  N   . LYS   A 1 100 ? 15.126  -20.947 -14.334 1.00 35.04  ? 100 LYS   A N   1 
ATOM   768  C  CA  . LYS   A 1 100 ? 14.903  -21.699 -15.550 1.00 38.23  ? 100 LYS   A CA  1 
ATOM   769  C  C   . LYS   A 1 100 ? 14.554  -20.710 -16.650 1.00 38.73  ? 100 LYS   A C   1 
ATOM   770  O  O   . LYS   A 1 100 ? 13.701  -19.854 -16.434 1.00 34.88  ? 100 LYS   A O   1 
ATOM   771  C  CB  . LYS   A 1 100 ? 13.685  -22.620 -15.509 1.00 42.88  ? 100 LYS   A CB  1 
ATOM   772  C  CG  . LYS   A 1 100 ? 13.727  -23.751 -14.505 1.00 52.64  ? 100 LYS   A CG  1 
ATOM   773  C  CD  . LYS   A 1 100 ? 12.621  -24.774 -14.756 1.00 56.89  ? 100 LYS   A CD  1 
ATOM   774  C  CE  . LYS   A 1 100 ? 12.726  -25.979 -13.865 1.00 62.94  ? 100 LYS   A CE  1 
ATOM   775  N  NZ  . LYS   A 1 100 ? 11.732  -26.991 -14.232 1.00 65.22  ? 100 LYS   A NZ  1 
ATOM   776  N  N   . TYR   A 1 101 ? 15.175  -20.862 -17.831 1.00 41.05  ? 101 TYR   A N   1 
ATOM   777  C  CA  . TYR   A 1 101 ? 15.047  -19.856 -18.878 1.00 40.25  ? 101 TYR   A CA  1 
ATOM   778  C  C   . TYR   A 1 101 ? 15.302  -20.428 -20.264 1.00 39.88  ? 101 TYR   A C   1 
ATOM   779  O  O   . TYR   A 1 101 ? 15.800  -21.532 -20.396 1.00 41.57  ? 101 TYR   A O   1 
ATOM   780  C  CB  . TYR   A 1 101 ? 16.039  -18.718 -18.647 1.00 38.00  ? 101 TYR   A CB  1 
ATOM   781  C  CG  . TYR   A 1 101 ? 17.495  -19.002 -18.989 1.00 37.93  ? 101 TYR   A CG  1 
ATOM   782  C  CD1 . TYR   A 1 101 ? 17.984  -18.804 -20.277 1.00 38.66  ? 101 TYR   A CD1 1 
ATOM   783  C  CD2 . TYR   A 1 101 ? 18.390  -19.431 -18.016 1.00 38.18  ? 101 TYR   A CD2 1 
ATOM   784  C  CE1 . TYR   A 1 101 ? 19.314  -19.047 -20.588 1.00 37.99  ? 101 TYR   A CE1 1 
ATOM   785  C  CE2 . TYR   A 1 101 ? 19.727  -19.664 -18.308 1.00 39.52  ? 101 TYR   A CE2 1 
ATOM   786  C  CZ  . TYR   A 1 101 ? 20.186  -19.466 -19.598 1.00 38.05  ? 101 TYR   A CZ  1 
ATOM   787  O  OH  . TYR   A 1 101 ? 21.486  -19.708 -19.884 1.00 34.61  ? 101 TYR   A OH  1 
ATOM   788  N  N   . LYS   A 1 102 ? 14.944  -19.651 -21.287 1.00 39.51  ? 102 LYS   A N   1 
ATOM   789  C  CA  . LYS   A 1 102 ? 15.266  -19.968 -22.669 1.00 40.00  ? 102 LYS   A CA  1 
ATOM   790  C  C   . LYS   A 1 102 ? 15.233  -18.690 -23.512 1.00 37.33  ? 102 LYS   A C   1 
ATOM   791  O  O   . LYS   A 1 102 ? 14.665  -17.700 -23.066 1.00 33.62  ? 102 LYS   A O   1 
ATOM   792  C  CB  . LYS   A 1 102 ? 14.274  -20.990 -23.216 1.00 42.41  ? 102 LYS   A CB  1 
ATOM   793  C  CG  . LYS   A 1 102 ? 12.886  -20.425 -23.431 1.00 52.02  ? 102 LYS   A CG  1 
ATOM   794  C  CD  . LYS   A 1 102 ? 11.891  -21.383 -24.070 1.00 54.35  ? 102 LYS   A CD  1 
ATOM   795  C  CE  . LYS   A 1 102 ? 11.733  -22.657 -23.328 1.00 58.33  ? 102 LYS   A CE  1 
ATOM   796  N  NZ  . LYS   A 1 102 ? 10.650  -23.416 -23.959 1.00 69.54  ? 102 LYS   A NZ  1 
ATOM   797  N  N   . PHE   A 1 103 ? 15.872  -18.727 -24.697 1.00 33.15  ? 103 PHE   A N   1 
ATOM   798  C  CA  . PHE   A 1 103 ? 15.844  -17.650 -25.677 1.00 34.19  ? 103 PHE   A CA  1 
ATOM   799  C  C   . PHE   A 1 103 ? 14.869  -17.997 -26.796 1.00 33.20  ? 103 PHE   A C   1 
ATOM   800  O  O   . PHE   A 1 103 ? 14.910  -19.111 -27.309 1.00 36.47  ? 103 PHE   A O   1 
ATOM   801  C  CB  . PHE   A 1 103 ? 17.221  -17.391 -26.285 1.00 30.50  ? 103 PHE   A CB  1 
ATOM   802  C  CG  . PHE   A 1 103 ? 18.322  -16.977 -25.315 1.00 30.88  ? 103 PHE   A CG  1 
ATOM   803  C  CD1 . PHE   A 1 103 ? 18.038  -16.525 -24.033 1.00 29.10  ? 103 PHE   A CD1 1 
ATOM   804  C  CD2 . PHE   A 1 103 ? 19.651  -17.022 -25.707 1.00 31.19  ? 103 PHE   A CD2 1 
ATOM   805  C  CE1 . PHE   A 1 103 ? 19.048  -16.160 -23.168 1.00 29.49  ? 103 PHE   A CE1 1 
ATOM   806  C  CE2 . PHE   A 1 103 ? 20.659  -16.626 -24.847 1.00 32.49  ? 103 PHE   A CE2 1 
ATOM   807  C  CZ  . PHE   A 1 103 ? 20.357  -16.194 -23.577 1.00 31.95  ? 103 PHE   A CZ  1 
ATOM   808  N  N   . VAL   A 1 104 ? 14.003  -17.040 -27.163 1.00 31.58  ? 104 VAL   A N   1 
ATOM   809  C  CA  . VAL   A 1 104 ? 13.006  -17.215 -28.215 1.00 31.70  ? 104 VAL   A CA  1 
ATOM   810  C  C   . VAL   A 1 104 ? 12.889  -15.927 -29.037 1.00 30.24  ? 104 VAL   A C   1 
ATOM   811  O  O   . VAL   A 1 104 ? 12.766  -14.840 -28.473 1.00 31.74  ? 104 VAL   A O   1 
ATOM   812  C  CB  . VAL   A 1 104 ? 11.627  -17.585 -27.622 1.00 40.65  ? 104 VAL   A CB  1 
ATOM   813  C  CG1 . VAL   A 1 104 ? 11.652  -18.897 -26.841 1.00 43.42  ? 104 VAL   A CG1 1 
ATOM   814  C  CG2 . VAL   A 1 104 ? 11.074  -16.482 -26.724 1.00 43.98  ? 104 VAL   A CG2 1 
ATOM   815  N  N   . ARG   A 1 105 ? 12.858  -16.055 -30.367 1.00 25.51  ? 105 ARG   A N   1 
ATOM   816  C  CA  . ARG   A 1 105 ? 12.531  -14.961 -31.268 1.00 28.82  ? 105 ARG   A CA  1 
ATOM   817  C  C   . ARG   A 1 105 ? 11.028  -14.910 -31.520 1.00 30.51  ? 105 ARG   A C   1 
ATOM   818  O  O   . ARG   A 1 105 ? 10.481  -15.921 -31.932 1.00 35.97  ? 105 ARG   A O   1 
ATOM   819  C  CB  . ARG   A 1 105 ? 13.228  -15.143 -32.619 1.00 27.52  ? 105 ARG   A CB  1 
ATOM   820  C  CG  . ARG   A 1 105 ? 13.316  -13.879 -33.469 1.00 27.44  ? 105 ARG   A CG  1 
ATOM   821  C  CD  . ARG   A 1 105 ? 14.081  -14.126 -34.760 1.00 25.46  ? 105 ARG   A CD  1 
ATOM   822  N  NE  . ARG   A 1 105 ? 14.053  -12.963 -35.649 1.00 27.54  ? 105 ARG   A NE  1 
ATOM   823  C  CZ  . ARG   A 1 105 ? 14.756  -11.828 -35.510 1.00 27.35  ? 105 ARG   A CZ  1 
ATOM   824  N  NH1 . ARG   A 1 105 ? 15.670  -11.717 -34.562 1.00 30.33  ? 105 ARG   A NH1 1 
ATOM   825  N  NH2 . ARG   A 1 105 ? 14.580  -10.834 -36.358 1.00 25.55  ? 105 ARG   A NH2 1 
ATOM   826  N  N   . ILE   A 1 106 ? 10.391  -13.732 -31.321 1.00 28.96  ? 106 ILE   A N   1 
ATOM   827  C  CA  . ILE   A 1 106 ? 8.953   -13.532 -31.521 1.00 26.96  ? 106 ILE   A CA  1 
ATOM   828  C  C   . ILE   A 1 106 ? 8.667   -12.941 -32.896 1.00 24.65  ? 106 ILE   A C   1 
ATOM   829  O  O   . ILE   A 1 106 ? 9.584   -12.469 -33.532 1.00 27.01  ? 106 ILE   A O   1 
ATOM   830  C  CB  . ILE   A 1 106 ? 8.381   -12.614 -30.431 1.00 28.00  ? 106 ILE   A CB  1 
ATOM   831  C  CG1 . ILE   A 1 106 ? 9.093   -11.240 -30.403 1.00 28.93  ? 106 ILE   A CG1 1 
ATOM   832  C  CG2 . ILE   A 1 106 ? 8.420   -13.313 -29.066 1.00 30.30  ? 106 ILE   A CG2 1 
ATOM   833  C  CD1 . ILE   A 1 106 ? 8.455   -10.247 -29.449 1.00 30.75  ? 106 ILE   A CD1 1 
ATOM   834  N  N   . GLN   A 1 107 ? 7.397   -12.966 -33.330 1.00 25.78  ? 107 GLN   A N   1 
ATOM   835  C  CA  . GLN   A 1 107 ? 6.881   -12.358 -34.555 1.00 28.14  ? 107 GLN   A CA  1 
ATOM   836  C  C   . GLN   A 1 107 ? 5.999   -11.136 -34.267 1.00 26.80  ? 107 GLN   A C   1 
ATOM   837  O  O   . GLN   A 1 107 ? 5.454   -10.993 -33.174 1.00 26.34  ? 107 GLN   A O   1 
ATOM   838  C  CB  . GLN   A 1 107 ? 5.894   -13.314 -35.227 1.00 30.56  ? 107 GLN   A CB  1 
ATOM   839  C  CG  . GLN   A 1 107 ? 6.530   -14.605 -35.723 1.00 34.88  ? 107 GLN   A CG  1 
ATOM   840  C  CD  . GLN   A 1 107 ? 7.437   -14.333 -36.891 1.00 39.67  ? 107 GLN   A CD  1 
ATOM   841  O  OE1 . GLN   A 1 107 ? 6.990   -13.873 -37.943 1.00 48.44  ? 107 GLN   A OE1 1 
ATOM   842  N  NE2 . GLN   A 1 107 ? 8.724   -14.538 -36.686 1.00 38.96  ? 107 GLN   A NE2 1 
ATOM   843  N  N   . PRO   A 1 108 ? 5.815   -10.231 -35.257 1.00 27.21  ? 108 PRO   A N   1 
ATOM   844  C  CA  . PRO   A 1 108 ? 4.934   -9.071  -35.111 1.00 26.13  ? 108 PRO   A CA  1 
ATOM   845  C  C   . PRO   A 1 108 ? 3.555   -9.464  -34.581 1.00 26.49  ? 108 PRO   A C   1 
ATOM   846  O  O   . PRO   A 1 108 ? 2.938   -10.401 -35.073 1.00 24.44  ? 108 PRO   A O   1 
ATOM   847  C  CB  . PRO   A 1 108 ? 4.822   -8.481  -36.530 1.00 27.61  ? 108 PRO   A CB  1 
ATOM   848  C  CG  . PRO   A 1 108 ? 6.015   -9.024  -37.282 1.00 29.73  ? 108 PRO   A CG  1 
ATOM   849  C  CD  . PRO   A 1 108 ? 6.464   -10.292 -36.581 1.00 28.58  ? 108 PRO   A CD  1 
ATOM   850  N  N   . GLY   A 1 109 ? 3.062   -8.718  -33.595 1.00 23.86  ? 109 GLY   A N   1 
ATOM   851  C  CA  . GLY   A 1 109 ? 1.780   -9.018  -32.991 1.00 24.15  ? 109 GLY   A CA  1 
ATOM   852  C  C   . GLY   A 1 109 ? 1.919   -9.571  -31.578 1.00 22.35  ? 109 GLY   A C   1 
ATOM   853  O  O   . GLY   A 1 109 ? 1.038   -9.350  -30.756 1.00 24.70  ? 109 GLY   A O   1 
ATOM   854  N  N   . GLN   A 1 110 ? 3.025   -10.266 -31.303 1.00 22.95  ? 110 GLN   A N   1 
ATOM   855  C  CA  . GLN   A 1 110 ? 3.267   -10.869 -30.003 1.00 24.59  ? 110 GLN   A CA  1 
ATOM   856  C  C   . GLN   A 1 110 ? 3.541   -9.783  -28.954 1.00 25.61  ? 110 GLN   A C   1 
ATOM   857  O  O   . GLN   A 1 110 ? 4.087   -8.714  -29.271 1.00 24.90  ? 110 GLN   A O   1 
ATOM   858  C  CB  . GLN   A 1 110 ? 4.429   -11.845 -30.178 1.00 27.95  ? 110 GLN   A CB  1 
ATOM   859  C  CG  . GLN   A 1 110 ? 4.727   -12.691 -28.949 1.00 29.65  ? 110 GLN   A CG  1 
ATOM   860  C  CD  . GLN   A 1 110 ? 3.528   -13.499 -28.502 1.00 34.36  ? 110 GLN   A CD  1 
ATOM   861  O  OE1 . GLN   A 1 110 ? 2.731   -13.052 -27.660 1.00 30.42  ? 110 GLN   A OE1 1 
ATOM   862  N  NE2 . GLN   A 1 110 ? 3.390   -14.686 -29.090 1.00 34.98  ? 110 GLN   A NE2 1 
ATOM   863  N  N   . THR   A 1 111 ? 3.163   -10.087 -27.709 1.00 23.70  ? 111 THR   A N   1 
ATOM   864  C  CA  . THR   A 1 111 ? 3.389   -9.225  -26.557 1.00 22.79  ? 111 THR   A CA  1 
ATOM   865  C  C   . THR   A 1 111 ? 4.425   -9.839  -25.609 1.00 23.04  ? 111 THR   A C   1 
ATOM   866  O  O   . THR   A 1 111 ? 4.706   -11.058 -25.658 1.00 22.43  ? 111 THR   A O   1 
ATOM   867  C  CB  . THR   A 1 111 ? 2.059   -8.946  -25.836 1.00 22.00  ? 111 THR   A CB  1 
ATOM   868  O  OG1 . THR   A 1 111 ? 1.519   -10.186 -25.393 1.00 22.85  ? 111 THR   A OG1 1 
ATOM   869  C  CG2 . THR   A 1 111 ? 1.053   -8.224  -26.708 1.00 22.52  ? 111 THR   A CG2 1 
ATOM   870  N  N   . PHE   A 1 112 ? 4.984   -8.962  -24.742 1.00 23.46  ? 112 PHE   A N   1 
ATOM   871  C  CA  . PHE   A 1 112 ? 5.964   -9.315  -23.717 1.00 24.85  ? 112 PHE   A CA  1 
ATOM   872  C  C   . PHE   A 1 112 ? 6.057   -8.206  -22.657 1.00 25.90  ? 112 PHE   A C   1 
ATOM   873  O  O   . PHE   A 1 112 ? 5.623   -7.068  -22.889 1.00 22.55  ? 112 PHE   A O   1 
ATOM   874  C  CB  . PHE   A 1 112 ? 7.362   -9.586  -24.292 1.00 25.80  ? 112 PHE   A CB  1 
ATOM   875  C  CG  . PHE   A 1 112 ? 7.929   -8.478  -25.170 1.00 27.07  ? 112 PHE   A CG  1 
ATOM   876  C  CD1 . PHE   A 1 112 ? 7.543   -8.347  -26.504 1.00 27.69  ? 112 PHE   A CD1 1 
ATOM   877  C  CD2 . PHE   A 1 112 ? 8.808   -7.539  -24.654 1.00 27.40  ? 112 PHE   A CD2 1 
ATOM   878  C  CE1 . PHE   A 1 112 ? 8.073   -7.341  -27.307 1.00 30.28  ? 112 PHE   A CE1 1 
ATOM   879  C  CE2 . PHE   A 1 112 ? 9.315   -6.517  -25.456 1.00 26.32  ? 112 PHE   A CE2 1 
ATOM   880  C  CZ  . PHE   A 1 112 ? 8.955   -6.420  -26.776 1.00 28.44  ? 112 PHE   A CZ  1 
ATOM   881  N  N   . SER   A 1 113 ? 6.692   -8.537  -21.519 1.00 23.64  ? 113 SER   A N   1 
ATOM   882  C  CA  . SER   A 1 113 ? 6.941   -7.584  -20.440 1.00 25.74  ? 113 SER   A CA  1 
ATOM   883  C  C   . SER   A 1 113 ? 8.348   -6.996  -20.564 1.00 26.02  ? 113 SER   A C   1 
ATOM   884  O  O   . SER   A 1 113 ? 9.290   -7.739  -20.811 1.00 25.25  ? 113 SER   A O   1 
ATOM   885  C  CB  . SER   A 1 113 ? 6.748   -8.248  -19.077 1.00 26.77  ? 113 SER   A CB  1 
ATOM   886  O  OG  . SER   A 1 113 ? 5.388   -8.628  -18.852 1.00 24.76  ? 113 SER   A OG  1 
ATOM   887  N  N   . VAL   A 1 114 ? 8.494   -5.674  -20.346 1.00 23.43  ? 114 VAL   A N   1 
ATOM   888  C  CA  . VAL   A 1 114 ? 9.804   -5.030  -20.316 1.00 21.89  ? 114 VAL   A CA  1 
ATOM   889  C  C   . VAL   A 1 114 ? 10.125  -4.632  -18.878 1.00 20.90  ? 114 VAL   A C   1 
ATOM   890  O  O   . VAL   A 1 114 ? 9.299   -4.003  -18.217 1.00 20.03  ? 114 VAL   A O   1 
ATOM   891  C  CB  . VAL   A 1 114 ? 9.876   -3.805  -21.258 1.00 23.27  ? 114 VAL   A CB  1 
ATOM   892  C  CG1 . VAL   A 1 114 ? 11.151  -2.989  -21.054 1.00 24.25  ? 114 VAL   A CG1 1 
ATOM   893  C  CG2 . VAL   A 1 114 ? 9.741   -4.190  -22.723 1.00 22.88  ? 114 VAL   A CG2 1 
ATOM   894  N  N   . LEU   A 1 115 ? 11.354  -4.946  -18.425 1.00 20.70  ? 115 LEU   A N   1 
ATOM   895  C  CA  . LEU   A 1 115 ? 11.867  -4.467  -17.144 1.00 21.03  ? 115 LEU   A CA  1 
ATOM   896  C  C   . LEU   A 1 115 ? 12.868  -3.335  -17.390 1.00 23.51  ? 115 LEU   A C   1 
ATOM   897  O  O   . LEU   A 1 115 ? 14.039  -3.578  -17.696 1.00 21.04  ? 115 LEU   A O   1 
ATOM   898  C  CB  . LEU   A 1 115 ? 12.507  -5.597  -16.339 1.00 21.14  ? 115 LEU   A CB  1 
ATOM   899  C  CG  . LEU   A 1 115 ? 13.024  -5.195  -14.951 1.00 22.33  ? 115 LEU   A CG  1 
ATOM   900  C  CD1 . LEU   A 1 115 ? 11.876  -4.889  -14.007 1.00 24.41  ? 115 LEU   A CD1 1 
ATOM   901  C  CD2 . LEU   A 1 115 ? 13.898  -6.252  -14.346 1.00 23.28  ? 115 LEU   A CD2 1 
ATOM   902  N  N   . ALA   A 1 116 ? 12.408  -2.080  -17.271 1.00 23.29  ? 116 ALA   A N   1 
ATOM   903  C  CA  . ALA   A 1 116 ? 13.291  -0.942  -17.517 1.00 24.03  ? 116 ALA   A CA  1 
ATOM   904  C  C   . ALA   A 1 116 ? 14.303  -0.798  -16.375 1.00 22.66  ? 116 ALA   A C   1 
ATOM   905  O  O   . ALA   A 1 116 ? 13.912  -0.857  -15.209 1.00 20.67  ? 116 ALA   A O   1 
ATOM   906  C  CB  . ALA   A 1 116 ? 12.497  0.339   -17.690 1.00 24.11  ? 116 ALA   A CB  1 
ATOM   907  N  N   . CYS   A 1 117 ? 15.579  -0.564  -16.726 1.00 21.88  ? 117 CYS   A N   1 
ATOM   908  C  CA  . CYS   A 1 117 ? 16.689  -0.582  -15.788 1.00 25.18  ? 117 CYS   A CA  1 
ATOM   909  C  C   . CYS   A 1 117 ? 17.729  0.493   -16.121 1.00 24.80  ? 117 CYS   A C   1 
ATOM   910  O  O   . CYS   A 1 117 ? 17.988  0.778   -17.296 1.00 24.41  ? 117 CYS   A O   1 
ATOM   911  C  CB  . CYS   A 1 117 ? 17.478  -1.882  -15.857 1.00 29.42  ? 117 CYS   A CB  1 
ATOM   912  S  SG  . CYS   A 1 117 ? 16.560  -3.332  -15.294 1.00 38.47  ? 117 CYS   A SG  1 
ATOM   913  N  N   . TYR   A 1 118 ? 18.346  1.051   -15.059 1.00 25.05  ? 118 TYR   A N   1 
ATOM   914  C  CA  . TYR   A 1 118 ? 19.367  2.089   -15.155 1.00 25.13  ? 118 TYR   A CA  1 
ATOM   915  C  C   . TYR   A 1 118 ? 20.489  1.738   -14.175 1.00 28.23  ? 118 TYR   A C   1 
ATOM   916  O  O   . TYR   A 1 118 ? 20.221  1.431   -13.013 1.00 26.48  ? 118 TYR   A O   1 
ATOM   917  C  CB  . TYR   A 1 118 ? 18.756  3.464   -14.858 1.00 26.39  ? 118 TYR   A CB  1 
ATOM   918  C  CG  . TYR   A 1 118 ? 17.665  3.827   -15.856 1.00 28.37  ? 118 TYR   A CG  1 
ATOM   919  C  CD1 . TYR   A 1 118 ? 17.967  4.467   -17.056 1.00 25.82  ? 118 TYR   A CD1 1 
ATOM   920  C  CD2 . TYR   A 1 118 ? 16.340  3.450   -15.632 1.00 28.07  ? 118 TYR   A CD2 1 
ATOM   921  C  CE1 . TYR   A 1 118 ? 16.986  4.737   -17.990 1.00 25.08  ? 118 TYR   A CE1 1 
ATOM   922  C  CE2 . TYR   A 1 118 ? 15.355  3.707   -16.566 1.00 26.50  ? 118 TYR   A CE2 1 
ATOM   923  C  CZ  . TYR   A 1 118 ? 15.671  4.378   -17.735 1.00 26.96  ? 118 TYR   A CZ  1 
ATOM   924  O  OH  . TYR   A 1 118 ? 14.686  4.628   -18.655 1.00 24.19  ? 118 TYR   A OH  1 
ATOM   925  N  N   . ASN   A 1 119 ? 21.738  1.724   -14.664 1.00 29.25  ? 119 ASN   A N   1 
ATOM   926  C  CA  . ASN   A 1 119 ? 22.905  1.395   -13.861 1.00 30.59  ? 119 ASN   A CA  1 
ATOM   927  C  C   . ASN   A 1 119 ? 22.783  0.024   -13.203 1.00 30.14  ? 119 ASN   A C   1 
ATOM   928  O  O   . ASN   A 1 119 ? 23.279  -0.154  -12.104 1.00 32.74  ? 119 ASN   A O   1 
ATOM   929  C  CB  . ASN   A 1 119 ? 23.136  2.433   -12.774 1.00 32.03  ? 119 ASN   A CB  1 
ATOM   930  C  CG  . ASN   A 1 119 ? 23.578  3.747   -13.359 1.00 34.29  ? 119 ASN   A CG  1 
ATOM   931  O  OD1 . ASN   A 1 119 ? 22.930  4.774   -13.157 1.00 36.87  ? 119 ASN   A OD1 1 
ATOM   932  N  ND2 . ASN   A 1 119 ? 24.674  3.732   -14.094 1.00 37.98  ? 119 ASN   A ND2 1 
ATOM   933  N  N   . GLY   A 1 120 ? 22.126  -0.943  -13.859 1.00 30.16  ? 120 GLY   A N   1 
ATOM   934  C  CA  . GLY   A 1 120 ? 21.966  -2.276  -13.291 1.00 27.93  ? 120 GLY   A CA  1 
ATOM   935  C  C   . GLY   A 1 120 ? 20.805  -2.403  -12.293 1.00 28.43  ? 120 GLY   A C   1 
ATOM   936  O  O   . GLY   A 1 120 ? 20.578  -3.497  -11.766 1.00 29.31  ? 120 GLY   A O   1 
ATOM   937  N  N   . SER   A 1 121 ? 20.051  -1.319  -12.055 1.00 27.16  ? 121 SER   A N   1 
ATOM   938  C  CA  . SER   A 1 121 ? 18.948  -1.357  -11.097 1.00 31.14  ? 121 SER   A CA  1 
ATOM   939  C  C   . SER   A 1 121 ? 17.589  -1.216  -11.781 1.00 29.74  ? 121 SER   A C   1 
ATOM   940  O  O   . SER   A 1 121 ? 17.349  -0.245  -12.505 1.00 29.39  ? 121 SER   A O   1 
ATOM   941  C  CB  . SER   A 1 121 ? 19.110  -0.317  -10.052 1.00 31.33  ? 121 SER   A CB  1 
ATOM   942  O  OG  . SER   A 1 121 ? 20.301  -0.586  -9.327  1.00 41.75  ? 121 SER   A OG  1 
ATOM   943  N  N   . PRO   A 1 122 ? 16.648  -2.151  -11.521 1.00 30.98  ? 122 PRO   A N   1 
ATOM   944  C  CA  . PRO   A 1 122 ? 15.320  -2.107  -12.140 1.00 32.02  ? 122 PRO   A CA  1 
ATOM   945  C  C   . PRO   A 1 122 ? 14.551  -0.872  -11.709 1.00 30.33  ? 122 PRO   A C   1 
ATOM   946  O  O   . PRO   A 1 122 ? 14.660  -0.447  -10.567 1.00 30.15  ? 122 PRO   A O   1 
ATOM   947  C  CB  . PRO   A 1 122 ? 14.647  -3.413  -11.685 1.00 32.00  ? 122 PRO   A CB  1 
ATOM   948  C  CG  . PRO   A 1 122 ? 15.833  -4.298  -11.322 1.00 35.04  ? 122 PRO   A CG  1 
ATOM   949  C  CD  . PRO   A 1 122 ? 16.804  -3.327  -10.647 1.00 34.71  ? 122 PRO   A CD  1 
ATOM   950  N  N   . SER   A 1 123 ? 13.766  -0.319  -12.636 1.00 28.80  ? 123 SER   A N   1 
ATOM   951  C  CA  . SER   A 1 123 ? 13.030  0.908   -12.389 1.00 31.46  ? 123 SER   A CA  1 
ATOM   952  C  C   . SER   A 1 123 ? 11.511  0.701   -12.465 1.00 28.19  ? 123 SER   A C   1 
ATOM   953  O  O   . SER   A 1 123 ? 10.774  1.364   -11.740 1.00 26.79  ? 123 SER   A O   1 
ATOM   954  C  CB  . SER   A 1 123 ? 13.483  1.968   -13.352 1.00 33.15  ? 123 SER   A CB  1 
ATOM   955  O  OG  . SER   A 1 123 ? 12.935  3.212   -12.975 1.00 40.39  ? 123 SER   A OG  1 
ATOM   956  N  N   . GLY   A 1 124 ? 11.044  -0.157  -13.384 1.00 24.99  ? 124 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 124 ? 9.622   -0.417  -13.578 1.00 24.47  ? 124 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 124 ? 9.368   -1.505  -14.627 1.00 21.40  ? 124 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 124 ? 10.283  -1.909  -15.356 1.00 19.56  ? 124 GLY   A O   1 
ATOM   960  N  N   . VAL   A 1 125 ? 8.100   -1.935  -14.721 1.00 20.81  ? 125 VAL   A N   1 
ATOM   961  C  CA  . VAL   A 1 125 ? 7.735   -3.007  -15.621 1.00 23.11  ? 125 VAL   A CA  1 
ATOM   962  C  C   . VAL   A 1 125 ? 6.428   -2.668  -16.337 1.00 24.42  ? 125 VAL   A C   1 
ATOM   963  O  O   . VAL   A 1 125 ? 5.498   -2.175  -15.692 1.00 21.67  ? 125 VAL   A O   1 
ATOM   964  C  CB  . VAL   A 1 125 ? 7.707   -4.326  -14.815 1.00 26.84  ? 125 VAL   A CB  1 
ATOM   965  C  CG1 . VAL   A 1 125 ? 6.679   -4.334  -13.701 1.00 29.01  ? 125 VAL   A CG1 1 
ATOM   966  C  CG2 . VAL   A 1 125 ? 7.531   -5.561  -15.704 1.00 29.60  ? 125 VAL   A CG2 1 
ATOM   967  N  N   . TYR   A 1 126 ? 6.379   -2.932  -17.661 1.00 23.25  ? 126 TYR   A N   1 
ATOM   968  C  CA  . TYR   A 1 126 ? 5.186   -2.683  -18.476 1.00 24.81  ? 126 TYR   A CA  1 
ATOM   969  C  C   . TYR   A 1 126 ? 5.127   -3.631  -19.674 1.00 25.63  ? 126 TYR   A C   1 
ATOM   970  O  O   . TYR   A 1 126 ? 6.127   -4.263  -20.040 1.00 25.01  ? 126 TYR   A O   1 
ATOM   971  C  CB  . TYR   A 1 126 ? 5.193   -1.202  -18.885 1.00 27.28  ? 126 TYR   A CB  1 
ATOM   972  C  CG  . TYR   A 1 126 ? 6.459   -0.735  -19.601 1.00 27.00  ? 126 TYR   A CG  1 
ATOM   973  C  CD1 . TYR   A 1 126 ? 7.548   -0.239  -18.900 1.00 27.07  ? 126 TYR   A CD1 1 
ATOM   974  C  CD2 . TYR   A 1 126 ? 6.579   -0.821  -20.981 1.00 24.81  ? 126 TYR   A CD2 1 
ATOM   975  C  CE1 . TYR   A 1 126 ? 8.700   0.184   -19.552 1.00 27.95  ? 126 TYR   A CE1 1 
ATOM   976  C  CE2 . TYR   A 1 126 ? 7.741   -0.447  -21.635 1.00 26.20  ? 126 TYR   A CE2 1 
ATOM   977  C  CZ  . TYR   A 1 126 ? 8.800   0.077   -20.925 1.00 27.30  ? 126 TYR   A CZ  1 
ATOM   978  O  OH  . TYR   A 1 126 ? 9.939   0.487   -21.568 1.00 33.19  ? 126 TYR   A OH  1 
ATOM   979  N  N   . GLN   A 1 127 ? 3.945   -3.697  -20.308 1.00 25.28  ? 127 GLN   A N   1 
ATOM   980  C  CA  . GLN   A 1 127 ? 3.713   -4.494  -21.504 1.00 27.02  ? 127 GLN   A CA  1 
ATOM   981  C  C   . GLN   A 1 127 ? 3.947   -3.701  -22.789 1.00 26.67  ? 127 GLN   A C   1 
ATOM   982  O  O   . GLN   A 1 127 ? 3.595   -2.527  -22.869 1.00 26.09  ? 127 GLN   A O   1 
ATOM   983  C  CB  . GLN   A 1 127 ? 2.264   -4.968  -21.672 1.00 28.39  ? 127 GLN   A CB  1 
ATOM   984  C  CG  . GLN   A 1 127 ? 1.880   -6.059  -20.692 1.00 26.99  ? 127 GLN   A CG  1 
ATOM   985  C  CD  . GLN   A 1 127 ? 2.630   -7.346  -20.966 1.00 29.38  ? 127 GLN   A CD  1 
ATOM   986  O  OE1 . GLN   A 1 127 ? 3.626   -7.677  -20.310 1.00 27.60  ? 127 GLN   A OE1 1 
ATOM   987  N  NE2 . GLN   A 1 127 ? 2.158   -8.071  -21.972 1.00 27.80  ? 127 GLN   A NE2 1 
ATOM   988  N  N   A CYS   A 1 128 ? 4.587   -4.364  -23.769 0.38 25.54  ? 128 CYS   A N   1 
ATOM   989  N  N   B CYS   A 1 128 ? 4.496   -4.374  -23.801 0.12 26.03  ? 128 CYS   A N   1 
ATOM   990  N  N   C CYS   A 1 128 ? 4.591   -4.361  -23.768 0.38 25.55  ? 128 CYS   A N   1 
ATOM   991  N  N   D CYS   A 1 128 ? 4.496   -4.374  -23.801 0.12 26.03  ? 128 CYS   A N   1 
ATOM   992  C  CA  A CYS   A 1 128 ? 4.725   -3.889  -25.139 0.38 24.53  ? 128 CYS   A CA  1 
ATOM   993  C  CA  B CYS   A 1 128 ? 4.518   -3.832  -25.145 0.12 25.41  ? 128 CYS   A CA  1 
ATOM   994  C  CA  C CYS   A 1 128 ? 4.729   -3.885  -25.139 0.38 24.53  ? 128 CYS   A CA  1 
ATOM   995  C  CA  D CYS   A 1 128 ? 4.518   -3.832  -25.145 0.12 25.41  ? 128 CYS   A CA  1 
ATOM   996  C  C   A CYS   A 1 128 ? 4.311   -4.985  -26.122 0.38 24.98  ? 128 CYS   A C   1 
ATOM   997  C  C   B CYS   A 1 128 ? 4.415   -4.972  -26.151 0.12 25.28  ? 128 CYS   A C   1 
ATOM   998  C  C   C CYS   A 1 128 ? 4.318   -4.981  -26.122 0.38 24.98  ? 128 CYS   A C   1 
ATOM   999  C  C   D CYS   A 1 128 ? 4.415   -4.972  -26.151 0.12 25.28  ? 128 CYS   A C   1 
ATOM   1000 O  O   A CYS   A 1 128 ? 4.225   -6.155  -25.739 0.38 24.10  ? 128 CYS   A O   1 
ATOM   1001 O  O   B CYS   A 1 128 ? 4.610   -6.139  -25.813 0.12 24.55  ? 128 CYS   A O   1 
ATOM   1002 O  O   C CYS   A 1 128 ? 4.229   -6.153  -25.738 0.38 24.10  ? 128 CYS   A O   1 
ATOM   1003 O  O   D CYS   A 1 128 ? 4.610   -6.139  -25.813 0.12 24.55  ? 128 CYS   A O   1 
ATOM   1004 C  CB  A CYS   A 1 128 ? 6.178   -3.599  -25.497 0.38 24.61  ? 128 CYS   A CB  1 
ATOM   1005 C  CB  B CYS   A 1 128 ? 5.775   -3.007  -25.387 0.12 25.71  ? 128 CYS   A CB  1 
ATOM   1006 C  CB  C CYS   A 1 128 ? 6.181   -3.596  -25.499 0.38 24.61  ? 128 CYS   A CB  1 
ATOM   1007 C  CB  D CYS   A 1 128 ? 5.775   -3.007  -25.387 0.12 25.71  ? 128 CYS   A CB  1 
ATOM   1008 S  SG  A CYS   A 1 128 ? 6.876   -2.144  -24.680 0.38 27.39  ? 128 CYS   A SG  1 
ATOM   1009 S  SG  B CYS   A 1 128 ? 7.294   -3.957  -25.135 0.12 26.37  ? 128 CYS   A SG  1 
ATOM   1010 S  SG  C CYS   A 1 128 ? 6.879   -2.141  -24.681 0.38 27.39  ? 128 CYS   A SG  1 
ATOM   1011 S  SG  D CYS   A 1 128 ? 7.294   -3.957  -25.135 0.12 26.37  ? 128 CYS   A SG  1 
ATOM   1012 N  N   . ALA   A 1 129 ? 4.115   -4.591  -27.393 1.00 24.69  ? 129 ALA   A N   1 
ATOM   1013 C  CA  . ALA   A 1 129 ? 3.966   -5.518  -28.512 1.00 26.23  ? 129 ALA   A CA  1 
ATOM   1014 C  C   . ALA   A 1 129 ? 5.041   -5.217  -29.552 1.00 26.03  ? 129 ALA   A C   1 
ATOM   1015 O  O   . ALA   A 1 129 ? 5.415   -4.053  -29.747 1.00 30.03  ? 129 ALA   A O   1 
ATOM   1016 C  CB  . ALA   A 1 129 ? 2.602   -5.374  -29.142 1.00 24.92  ? 129 ALA   A CB  1 
ATOM   1017 N  N   . MET   A 1 130 ? 5.507   -6.261  -30.230 1.00 23.64  ? 130 MET   A N   1 
ATOM   1018 C  CA  . MET   A 1 130 ? 6.275   -6.100  -31.464 1.00 25.03  ? 130 MET   A CA  1 
ATOM   1019 C  C   . MET   A 1 130 ? 5.341   -5.588  -32.560 1.00 26.80  ? 130 MET   A C   1 
ATOM   1020 O  O   . MET   A 1 130 ? 4.392   -6.281  -32.950 1.00 27.25  ? 130 MET   A O   1 
ATOM   1021 C  CB  . MET   A 1 130 ? 6.936   -7.420  -31.878 1.00 26.03  ? 130 MET   A CB  1 
ATOM   1022 C  CG  . MET   A 1 130 ? 7.869   -7.355  -33.088 1.00 28.16  ? 130 MET   A CG  1 
ATOM   1023 S  SD  . MET   A 1 130 ? 9.241   -6.194  -32.924 1.00 28.86  ? 130 MET   A SD  1 
ATOM   1024 C  CE  . MET   A 1 130 ? 10.050  -6.901  -31.485 1.00 27.24  ? 130 MET   A CE  1 
ATOM   1025 N  N   . ARG   A 1 131 ? 5.594   -4.349  -33.022 1.00 23.46  ? 131 ARG   A N   1 
ATOM   1026 C  CA  . ARG   A 1 131 ? 4.779   -3.746  -34.054 1.00 24.36  ? 131 ARG   A CA  1 
ATOM   1027 C  C   . ARG   A 1 131 ? 5.049   -4.404  -35.416 1.00 25.76  ? 131 ARG   A C   1 
ATOM   1028 O  O   . ARG   A 1 131 ? 6.108   -4.989  -35.646 1.00 24.69  ? 131 ARG   A O   1 
ATOM   1029 C  CB  . ARG   A 1 131 ? 5.016   -2.239  -34.141 1.00 24.95  ? 131 ARG   A CB  1 
ATOM   1030 C  CG  . ARG   A 1 131 ? 4.808   -1.389  -32.904 1.00 25.81  ? 131 ARG   A CG  1 
ATOM   1031 C  CD  . ARG   A 1 131 ? 3.430   -1.487  -32.316 1.00 27.97  ? 131 ARG   A CD  1 
ATOM   1032 N  NE  . ARG   A 1 131 ? 2.374   -1.108  -33.254 1.00 29.05  ? 131 ARG   A NE  1 
ATOM   1033 C  CZ  . ARG   A 1 131 ? 1.081   -1.282  -32.986 1.00 28.33  ? 131 ARG   A CZ  1 
ATOM   1034 N  NH1 . ARG   A 1 131 ? 0.684   -1.691  -31.809 1.00 25.45  ? 131 ARG   A NH1 1 
ATOM   1035 N  NH2 . ARG   A 1 131 ? 0.191   -1.075  -33.926 1.00 32.24  ? 131 ARG   A NH2 1 
ATOM   1036 N  N   . PRO   A 1 132 ? 4.095   -4.334  -36.378 1.00 23.96  ? 132 PRO   A N   1 
ATOM   1037 C  CA  . PRO   A 1 132 ? 4.336   -4.834  -37.736 1.00 25.09  ? 132 PRO   A CA  1 
ATOM   1038 C  C   . PRO   A 1 132 ? 5.568   -4.257  -38.441 1.00 24.95  ? 132 PRO   A C   1 
ATOM   1039 O  O   . PRO   A 1 132 ? 6.101   -4.875  -39.341 1.00 24.20  ? 132 PRO   A O   1 
ATOM   1040 C  CB  . PRO   A 1 132 ? 3.045   -4.458  -38.470 1.00 25.24  ? 132 PRO   A CB  1 
ATOM   1041 C  CG  . PRO   A 1 132 ? 1.996   -4.390  -37.374 1.00 24.00  ? 132 PRO   A CG  1 
ATOM   1042 C  CD  . PRO   A 1 132 ? 2.752   -3.767  -36.209 1.00 23.76  ? 132 PRO   A CD  1 
ATOM   1043 N  N   . ASN   A 1 133 ? 6.001   -3.054  -38.056 1.00 25.98  ? 133 ASN   A N   1 
ATOM   1044 C  CA  . ASN   A 1 133 ? 7.192   -2.443  -38.633 1.00 23.96  ? 133 ASN   A CA  1 
ATOM   1045 C  C   . ASN   A 1 133 ? 8.461   -2.760  -37.832 1.00 24.82  ? 133 ASN   A C   1 
ATOM   1046 O  O   . ASN   A 1 133 ? 9.473   -2.116  -38.059 1.00 23.57  ? 133 ASN   A O   1 
ATOM   1047 C  CB  . ASN   A 1 133 ? 7.011   -0.942  -38.776 1.00 25.21  ? 133 ASN   A CB  1 
ATOM   1048 C  CG  . ASN   A 1 133 ? 6.951   -0.203  -37.455 1.00 24.76  ? 133 ASN   A CG  1 
ATOM   1049 O  OD1 . ASN   A 1 133 ? 7.077   -0.791  -36.372 1.00 25.72  ? 133 ASN   A OD1 1 
ATOM   1050 N  ND2 . ASN   A 1 133 ? 6.748   1.102   -37.538 1.00 25.61  ? 133 ASN   A ND2 1 
ATOM   1051 N  N   . PHE   A 1 134 ? 8.381   -3.706  -36.878 1.00 23.83  ? 134 PHE   A N   1 
ATOM   1052 C  CA  . PHE   A 1 134 ? 9.511   -4.301  -36.182 1.00 24.25  ? 134 PHE   A CA  1 
ATOM   1053 C  C   . PHE   A 1 134 ? 10.095  -3.333  -35.152 1.00 26.15  ? 134 PHE   A C   1 
ATOM   1054 O  O   . PHE   A 1 134 ? 11.275  -3.468  -34.829 1.00 27.72  ? 134 PHE   A O   1 
ATOM   1055 C  CB  . PHE   A 1 134 ? 10.585  -4.834  -37.147 1.00 25.73  ? 134 PHE   A CB  1 
ATOM   1056 C  CG  . PHE   A 1 134 ? 10.108  -6.006  -37.996 1.00 27.52  ? 134 PHE   A CG  1 
ATOM   1057 C  CD1 . PHE   A 1 134 ? 10.069  -7.296  -37.467 1.00 29.15  ? 134 PHE   A CD1 1 
ATOM   1058 C  CD2 . PHE   A 1 134 ? 9.664   -5.816  -39.300 1.00 29.49  ? 134 PHE   A CD2 1 
ATOM   1059 C  CE1 . PHE   A 1 134 ? 9.579   -8.359  -38.221 1.00 29.50  ? 134 PHE   A CE1 1 
ATOM   1060 C  CE2 . PHE   A 1 134 ? 9.211   -6.891  -40.061 1.00 29.46  ? 134 PHE   A CE2 1 
ATOM   1061 C  CZ  . PHE   A 1 134 ? 9.157   -8.150  -39.520 1.00 27.01  ? 134 PHE   A CZ  1 
ATOM   1062 N  N   . THR   A 1 135 ? 9.296   -2.364  -34.653 1.00 25.46  ? 135 THR   A N   1 
ATOM   1063 C  CA  . THR   A 1 135 ? 9.696   -1.496  -33.544 1.00 23.42  ? 135 THR   A CA  1 
ATOM   1064 C  C   . THR   A 1 135 ? 8.781   -1.766  -32.349 1.00 23.77  ? 135 THR   A C   1 
ATOM   1065 O  O   . THR   A 1 135 ? 7.753   -2.411  -32.495 1.00 23.33  ? 135 THR   A O   1 
ATOM   1066 C  CB  . THR   A 1 135 ? 9.619   -0.017  -33.953 1.00 26.11  ? 135 THR   A CB  1 
ATOM   1067 O  OG1 . THR   A 1 135 ? 8.282   0.370   -34.275 1.00 23.91  ? 135 THR   A OG1 1 
ATOM   1068 C  CG2 . THR   A 1 135 ? 10.441  0.332   -35.180 1.00 27.12  ? 135 THR   A CG2 1 
ATOM   1069 N  N   . ILE   A 1 136 ? 9.109   -1.207  -31.172 1.00 24.89  ? 136 ILE   A N   1 
ATOM   1070 C  CA  . ILE   A 1 136 ? 8.234   -1.263  -30.012 1.00 22.11  ? 136 ILE   A CA  1 
ATOM   1071 C  C   . ILE   A 1 136 ? 8.044   0.161   -29.496 1.00 21.54  ? 136 ILE   A C   1 
ATOM   1072 O  O   . ILE   A 1 136 ? 8.912   1.012   -29.694 1.00 20.53  ? 136 ILE   A O   1 
ATOM   1073 C  CB  . ILE   A 1 136 ? 8.765   -2.215  -28.917 1.00 25.15  ? 136 ILE   A CB  1 
ATOM   1074 C  CG1 . ILE   A 1 136 ? 9.932   -1.625  -28.139 1.00 23.99  ? 136 ILE   A CG1 1 
ATOM   1075 C  CG2 . ILE   A 1 136 ? 9.140   -3.578  -29.513 1.00 27.45  ? 136 ILE   A CG2 1 
ATOM   1076 C  CD1 . ILE   A 1 136 ? 10.415  -2.500  -27.000 1.00 24.49  ? 136 ILE   A CD1 1 
ATOM   1077 N  N   . LYS   A 1 137 ? 6.902   0.410   -28.849 1.00 23.99  ? 137 LYS   A N   1 
ATOM   1078 C  CA  . LYS   A 1 137 ? 6.592   1.740   -28.318 1.00 26.44  ? 137 LYS   A CA  1 
ATOM   1079 C  C   . LYS   A 1 137 ? 6.802   1.756   -26.810 1.00 25.32  ? 137 LYS   A C   1 
ATOM   1080 O  O   . LYS   A 1 137 ? 5.916   1.442   -26.030 1.00 25.46  ? 137 LYS   A O   1 
ATOM   1081 C  CB  . LYS   A 1 137 ? 5.153   2.145   -28.656 1.00 27.46  ? 137 LYS   A CB  1 
ATOM   1082 C  CG  . LYS   A 1 137 ? 5.024   2.363   -30.148 1.00 32.88  ? 137 LYS   A CG  1 
ATOM   1083 C  CD  . LYS   A 1 137 ? 3.599   2.581   -30.645 1.00 39.84  ? 137 LYS   A CD  1 
ATOM   1084 C  CE  . LYS   A 1 137 ? 3.632   2.935   -32.098 1.00 48.60  ? 137 LYS   A CE  1 
ATOM   1085 N  NZ  . LYS   A 1 137 ? 2.485   3.774   -32.447 1.00 54.84  ? 137 LYS   A NZ  1 
ATOM   1086 N  N   . GLY   A 1 138 ? 8.010   2.089   -26.381 1.00 26.89  ? 138 GLY   A N   1 
ATOM   1087 C  CA  . GLY   A 1 138 ? 8.327   1.901   -24.983 1.00 26.06  ? 138 GLY   A CA  1 
ATOM   1088 C  C   . GLY   A 1 138 ? 8.554   3.221   -24.272 1.00 24.59  ? 138 GLY   A C   1 
ATOM   1089 O  O   . GLY   A 1 138 ? 8.155   4.281   -24.744 1.00 24.58  ? 138 GLY   A O   1 
ATOM   1090 N  N   . SER   A 1 139 ? 9.213   3.091   -23.122 1.00 23.63  ? 139 SER   A N   1 
ATOM   1091 C  CA  . SER   A 1 139 ? 9.604   4.197   -22.271 1.00 24.94  ? 139 SER   A CA  1 
ATOM   1092 C  C   . SER   A 1 139 ? 11.027  3.922   -21.802 1.00 24.44  ? 139 SER   A C   1 
ATOM   1093 O  O   . SER   A 1 139 ? 11.234  3.153   -20.873 1.00 25.66  ? 139 SER   A O   1 
ATOM   1094 C  CB  . SER   A 1 139 ? 8.648   4.366   -21.118 1.00 25.57  ? 139 SER   A CB  1 
ATOM   1095 O  OG  . SER   A 1 139 ? 9.117   5.378   -20.234 1.00 28.26  ? 139 SER   A OG  1 
ATOM   1096 N  N   . PHE   A 1 140 ? 11.980  4.524   -22.518 1.00 24.91  ? 140 PHE   A N   1 
ATOM   1097 C  CA  . PHE   A 1 140 ? 13.406  4.326   -22.327 1.00 28.52  ? 140 PHE   A CA  1 
ATOM   1098 C  C   . PHE   A 1 140 ? 14.086  5.695   -22.279 1.00 31.22  ? 140 PHE   A C   1 
ATOM   1099 O  O   . PHE   A 1 140 ? 13.846  6.525   -23.159 1.00 34.39  ? 140 PHE   A O   1 
ATOM   1100 C  CB  . PHE   A 1 140 ? 13.959  3.502   -23.499 1.00 26.88  ? 140 PHE   A CB  1 
ATOM   1101 C  CG  . PHE   A 1 140 ? 13.532  2.041   -23.514 1.00 27.08  ? 140 PHE   A CG  1 
ATOM   1102 C  CD1 . PHE   A 1 140 ? 14.024  1.141   -22.573 1.00 28.38  ? 140 PHE   A CD1 1 
ATOM   1103 C  CD2 . PHE   A 1 140 ? 12.624  1.569   -24.450 1.00 25.61  ? 140 PHE   A CD2 1 
ATOM   1104 C  CE1 . PHE   A 1 140 ? 13.639  -0.201  -22.590 1.00 27.93  ? 140 PHE   A CE1 1 
ATOM   1105 C  CE2 . PHE   A 1 140 ? 12.243  0.227   -24.461 1.00 27.38  ? 140 PHE   A CE2 1 
ATOM   1106 C  CZ  . PHE   A 1 140 ? 12.766  -0.659  -23.553 1.00 24.59  ? 140 PHE   A CZ  1 
ATOM   1107 N  N   . LEU   A 1 141 ? 14.949  5.907   -21.278 1.00 31.92  ? 141 LEU   A N   1 
ATOM   1108 C  CA  . LEU   A 1 141 ? 15.749  7.119   -21.193 1.00 33.28  ? 141 LEU   A CA  1 
ATOM   1109 C  C   . LEU   A 1 141 ? 17.224  6.755   -21.358 1.00 31.87  ? 141 LEU   A C   1 
ATOM   1110 O  O   . LEU   A 1 141 ? 17.552  5.588   -21.527 1.00 28.90  ? 141 LEU   A O   1 
ATOM   1111 C  CB  . LEU   A 1 141 ? 15.493  7.825   -19.861 1.00 35.43  ? 141 LEU   A CB  1 
ATOM   1112 C  CG  . LEU   A 1 141 ? 14.071  8.322   -19.574 1.00 40.21  ? 141 LEU   A CG  1 
ATOM   1113 C  CD1 . LEU   A 1 141 ? 14.073  8.905   -18.165 1.00 41.71  ? 141 LEU   A CD1 1 
ATOM   1114 C  CD2 . LEU   A 1 141 ? 13.517  9.350   -20.562 1.00 39.18  ? 141 LEU   A CD2 1 
ATOM   1115 N  N   . ASN   A 1 142 ? 18.118  7.757   -21.275 1.00 34.66  ? 142 ASN   A N   1 
ATOM   1116 C  CA  . ASN   A 1 142 ? 19.553  7.523   -21.367 1.00 36.63  ? 142 ASN   A CA  1 
ATOM   1117 C  C   . ASN   A 1 142 ? 19.983  6.521   -20.299 1.00 32.02  ? 142 ASN   A C   1 
ATOM   1118 O  O   . ASN   A 1 142 ? 19.578  6.623   -19.150 1.00 29.98  ? 142 ASN   A O   1 
ATOM   1119 C  CB  . ASN   A 1 142 ? 20.370  8.815   -21.352 1.00 42.44  ? 142 ASN   A CB  1 
ATOM   1120 C  CG  . ASN   A 1 142 ? 20.878  9.166   -22.733 1.00 54.56  ? 142 ASN   A CG  1 
ATOM   1121 O  OD1 . ASN   A 1 142 ? 21.174  10.334  -23.022 1.00 64.17  ? 142 ASN   A OD1 1 
ATOM   1122 N  ND2 . ASN   A 1 142 ? 20.965  8.182   -23.622 1.00 56.90  ? 142 ASN   A ND2 1 
ATOM   1123 N  N   . GLY   A 1 143 ? 20.754  5.512   -20.707 1.00 29.57  ? 143 GLY   A N   1 
ATOM   1124 C  CA  . GLY   A 1 143 ? 21.266  4.530   -19.764 1.00 27.51  ? 143 GLY   A CA  1 
ATOM   1125 C  C   . GLY   A 1 143 ? 20.455  3.234   -19.734 1.00 27.28  ? 143 GLY   A C   1 
ATOM   1126 O  O   . GLY   A 1 143 ? 20.804  2.334   -18.968 1.00 25.92  ? 143 GLY   A O   1 
ATOM   1127 N  N   . SER   A 1 144 ? 19.388  3.139   -20.551 1.00 26.20  ? 144 SER   A N   1 
ATOM   1128 C  CA  . SER   A 1 144 ? 18.484  1.997   -20.520 1.00 25.30  ? 144 SER   A CA  1 
ATOM   1129 C  C   . SER   A 1 144 ? 18.893  0.867   -21.458 1.00 24.48  ? 144 SER   A C   1 
ATOM   1130 O  O   . SER   A 1 144 ? 18.279  -0.197  -21.414 1.00 22.95  ? 144 SER   A O   1 
ATOM   1131 C  CB  . SER   A 1 144 ? 17.039  2.413   -20.779 1.00 25.30  ? 144 SER   A CB  1 
ATOM   1132 O  OG  . SER   A 1 144 ? 16.912  3.132   -22.000 1.00 25.44  ? 144 SER   A OG  1 
ATOM   1133 N  N   A CYS   A 1 145 ? 19.914  1.102   -22.294 0.12 24.90  ? 145 CYS   A N   1 
ATOM   1134 N  N   B CYS   A 1 145 ? 19.914  1.102   -22.294 0.12 24.90  ? 145 CYS   A N   1 
ATOM   1135 N  N   C CYS   A 1 145 ? 19.919  1.101   -22.294 0.38 25.11  ? 145 CYS   A N   1 
ATOM   1136 N  N   D CYS   A 1 145 ? 19.916  1.098   -22.292 0.38 25.09  ? 145 CYS   A N   1 
ATOM   1137 C  CA  A CYS   A 1 145 ? 20.427  0.079   -23.195 0.12 24.72  ? 145 CYS   A CA  1 
ATOM   1138 C  CA  B CYS   A 1 145 ? 20.427  0.079   -23.195 0.12 24.72  ? 145 CYS   A CA  1 
ATOM   1139 C  CA  C CYS   A 1 145 ? 20.434  0.076   -23.192 0.38 24.66  ? 145 CYS   A CA  1 
ATOM   1140 C  CA  D CYS   A 1 145 ? 20.432  0.077   -23.194 0.38 24.60  ? 145 CYS   A CA  1 
ATOM   1141 C  C   A CYS   A 1 145 ? 20.753  -1.183  -22.393 0.12 23.50  ? 145 CYS   A C   1 
ATOM   1142 C  C   B CYS   A 1 145 ? 20.753  -1.183  -22.393 0.12 23.50  ? 145 CYS   A C   1 
ATOM   1143 C  C   C CYS   A 1 145 ? 20.760  -1.187  -22.390 0.38 23.25  ? 145 CYS   A C   1 
ATOM   1144 C  C   D CYS   A 1 145 ? 20.761  -1.186  -22.394 0.38 23.23  ? 145 CYS   A C   1 
ATOM   1145 O  O   A CYS   A 1 145 ? 21.162  -1.115  -21.241 0.12 23.01  ? 145 CYS   A O   1 
ATOM   1146 O  O   B CYS   A 1 145 ? 21.162  -1.115  -21.241 0.12 23.01  ? 145 CYS   A O   1 
ATOM   1147 O  O   C CYS   A 1 145 ? 21.168  -1.116  -21.240 0.38 22.59  ? 145 CYS   A O   1 
ATOM   1148 O  O   D CYS   A 1 145 ? 21.165  -1.111  -21.242 0.38 22.59  ? 145 CYS   A O   1 
ATOM   1149 C  CB  A CYS   A 1 145 ? 21.608  0.607   -24.001 0.12 27.01  ? 145 CYS   A CB  1 
ATOM   1150 C  CB  B CYS   A 1 145 ? 21.608  0.607   -24.001 0.12 27.01  ? 145 CYS   A CB  1 
ATOM   1151 C  CB  C CYS   A 1 145 ? 21.609  0.604   -23.996 0.38 27.94  ? 145 CYS   A CB  1 
ATOM   1152 C  CB  D CYS   A 1 145 ? 21.612  0.609   -24.003 0.38 27.67  ? 145 CYS   A CB  1 
ATOM   1153 S  SG  A CYS   A 1 145 ? 21.120  1.753   -25.319 0.12 29.48  ? 145 CYS   A SG  1 
ATOM   1154 S  SG  B CYS   A 1 145 ? 21.120  1.753   -25.319 0.12 29.48  ? 145 CYS   A SG  1 
ATOM   1155 S  SG  C CYS   A 1 145 ? 21.131  1.767   -25.323 0.38 31.33  ? 145 CYS   A SG  1 
ATOM   1156 S  SG  D CYS   A 1 145 ? 21.127  1.761   -25.325 0.38 31.44  ? 145 CYS   A SG  1 
ATOM   1157 N  N   . GLY   A 1 146 ? 20.462  -2.354  -22.965 1.00 22.72  ? 146 GLY   A N   1 
ATOM   1158 C  CA  . GLY   A 1 146 ? 20.642  -3.622  -22.259 1.00 23.81  ? 146 GLY   A CA  1 
ATOM   1159 C  C   . GLY   A 1 146 ? 19.434  -4.099  -21.431 1.00 22.52  ? 146 GLY   A C   1 
ATOM   1160 O  O   . GLY   A 1 146 ? 19.368  -5.283  -21.062 1.00 21.55  ? 146 GLY   A O   1 
ATOM   1161 N  N   . SER   A 1 147 ? 18.458  -3.232  -21.138 1.00 22.45  ? 147 SER   A N   1 
ATOM   1162 C  CA  . SER   A 1 147 ? 17.161  -3.690  -20.605 1.00 20.51  ? 147 SER   A CA  1 
ATOM   1163 C  C   . SER   A 1 147 ? 16.540  -4.821  -21.450 1.00 20.56  ? 147 SER   A C   1 
ATOM   1164 O  O   . SER   A 1 147 ? 16.670  -4.795  -22.661 1.00 22.14  ? 147 SER   A O   1 
ATOM   1165 C  CB  . SER   A 1 147 ? 16.191  -2.519  -20.493 1.00 19.79  ? 147 SER   A CB  1 
ATOM   1166 O  OG  . SER   A 1 147 ? 16.617  -1.499  -19.589 1.00 18.72  ? 147 SER   A OG  1 
ATOM   1167 N  N   . VAL   A 1 148 ? 15.758  -5.769  -20.875 1.00 19.46  ? 148 VAL   A N   1 
ATOM   1168 C  CA  . VAL   A 1 148 ? 15.233  -6.892  -21.650 1.00 18.04  ? 148 VAL   A CA  1 
ATOM   1169 C  C   . VAL   A 1 148 ? 13.714  -7.010  -21.573 1.00 19.49  ? 148 VAL   A C   1 
ATOM   1170 O  O   . VAL   A 1 148 ? 13.081  -6.486  -20.657 1.00 19.50  ? 148 VAL   A O   1 
ATOM   1171 C  CB  . VAL   A 1 148 ? 15.873  -8.243  -21.262 1.00 20.86  ? 148 VAL   A CB  1 
ATOM   1172 C  CG1 . VAL   A 1 148 ? 17.359  -8.253  -21.548 1.00 20.80  ? 148 VAL   A CG1 1 
ATOM   1173 C  CG2 . VAL   A 1 148 ? 15.639  -8.615  -19.806 1.00 21.91  ? 148 VAL   A CG2 1 
ATOM   1174 N  N   . GLY   A 1 149 ? 13.153  -7.699  -22.590 1.00 20.25  ? 149 GLY   A N   1 
ATOM   1175 C  CA  . GLY   A 1 149 ? 11.761  -8.123  -22.661 1.00 19.45  ? 149 GLY   A CA  1 
ATOM   1176 C  C   . GLY   A 1 149 ? 11.626  -9.644  -22.526 1.00 23.05  ? 149 GLY   A C   1 
ATOM   1177 O  O   . GLY   A 1 149 ? 12.526  -10.397 -22.954 1.00 23.14  ? 149 GLY   A O   1 
ATOM   1178 N  N   . PHE   A 1 150 ? 10.511  -10.097 -21.914 1.00 22.90  ? 150 PHE   A N   1 
ATOM   1179 C  CA  . PHE   A 1 150 ? 10.378  -11.496 -21.521 1.00 24.67  ? 150 PHE   A CA  1 
ATOM   1180 C  C   . PHE   A 1 150 ? 8.906   -11.884 -21.364 1.00 27.81  ? 150 PHE   A C   1 
ATOM   1181 O  O   . PHE   A 1 150 ? 8.052   -11.020 -21.178 1.00 23.39  ? 150 PHE   A O   1 
ATOM   1182 C  CB  . PHE   A 1 150 ? 11.131  -11.819 -20.221 1.00 24.32  ? 150 PHE   A CB  1 
ATOM   1183 C  CG  . PHE   A 1 150 ? 10.661  -10.999 -19.027 1.00 26.61  ? 150 PHE   A CG  1 
ATOM   1184 C  CD1 . PHE   A 1 150 ? 11.071  -9.676  -18.868 1.00 26.91  ? 150 PHE   A CD1 1 
ATOM   1185 C  CD2 . PHE   A 1 150 ? 9.769   -11.525 -18.102 1.00 27.40  ? 150 PHE   A CD2 1 
ATOM   1186 C  CE1 . PHE   A 1 150 ? 10.587  -8.889  -17.836 1.00 28.07  ? 150 PHE   A CE1 1 
ATOM   1187 C  CE2 . PHE   A 1 150 ? 9.289   -10.728 -17.058 1.00 28.89  ? 150 PHE   A CE2 1 
ATOM   1188 C  CZ  . PHE   A 1 150 ? 9.710   -9.424  -16.919 1.00 28.65  ? 150 PHE   A CZ  1 
ATOM   1189 N  N   . ASN   A 1 151 ? 8.641   -13.208 -21.459 1.00 29.22  ? 151 ASN   A N   1 
ATOM   1190 C  CA  . ASN   A 1 151 ? 7.430   -13.836 -20.962 1.00 30.57  ? 151 ASN   A CA  1 
ATOM   1191 C  C   . ASN   A 1 151 ? 7.822   -14.880 -19.910 1.00 33.53  ? 151 ASN   A C   1 
ATOM   1192 O  O   . ASN   A 1 151 ? 8.999   -15.268 -19.799 1.00 28.80  ? 151 ASN   A O   1 
ATOM   1193 C  CB  . ASN   A 1 151 ? 6.582   -14.443 -22.072 1.00 30.69  ? 151 ASN   A CB  1 
ATOM   1194 C  CG  . ASN   A 1 151 ? 5.992   -13.403 -22.991 1.00 33.40  ? 151 ASN   A CG  1 
ATOM   1195 O  OD1 . ASN   A 1 151 ? 4.982   -12.777 -22.651 1.00 31.45  ? 151 ASN   A OD1 1 
ATOM   1196 N  ND2 . ASN   A 1 151 ? 6.567   -13.236 -24.176 1.00 32.68  ? 151 ASN   A ND2 1 
ATOM   1197 N  N   . ILE   A 1 152 ? 6.831   -15.253 -19.078 1.00 31.00  ? 152 ILE   A N   1 
ATOM   1198 C  CA  . ILE   A 1 152 ? 6.998   -16.307 -18.094 1.00 34.48  ? 152 ILE   A CA  1 
ATOM   1199 C  C   . ILE   A 1 152 ? 5.773   -17.213 -18.177 1.00 42.84  ? 152 ILE   A C   1 
ATOM   1200 O  O   . ILE   A 1 152 ? 4.717   -16.904 -17.645 1.00 39.55  ? 152 ILE   A O   1 
ATOM   1201 C  CB  . ILE   A 1 152 ? 7.185   -15.766 -16.666 1.00 35.75  ? 152 ILE   A CB  1 
ATOM   1202 C  CG1 . ILE   A 1 152 ? 8.204   -14.627 -16.581 1.00 32.95  ? 152 ILE   A CG1 1 
ATOM   1203 C  CG2 . ILE   A 1 152 ? 7.538   -16.911 -15.713 1.00 35.62  ? 152 ILE   A CG2 1 
ATOM   1204 C  CD1 . ILE   A 1 152 ? 8.574   -14.247 -15.159 1.00 32.08  ? 152 ILE   A CD1 1 
ATOM   1205 N  N   . ASP   A 1 153 ? 5.914   -18.335 -18.871 1.00 53.86  ? 153 ASP   A N   1 
ATOM   1206 C  CA  . ASP   A 1 153 ? 4.836   -19.297 -18.929 1.00 60.74  ? 153 ASP   A CA  1 
ATOM   1207 C  C   . ASP   A 1 153 ? 5.353   -20.470 -18.099 1.00 67.41  ? 153 ASP   A C   1 
ATOM   1208 O  O   . ASP   A 1 153 ? 6.459   -20.947 -18.339 1.00 70.23  ? 153 ASP   A O   1 
ATOM   1209 C  CB  . ASP   A 1 153 ? 4.303   -19.389 -20.361 1.00 64.83  ? 153 ASP   A CB  1 
ATOM   1210 C  CG  . ASP   A 1 153 ? 3.591   -18.134 -20.891 1.00 68.54  ? 153 ASP   A CG  1 
ATOM   1211 O  OD1 . ASP   A 1 153 ? 3.533   -17.126 -20.166 1.00 75.05  ? 153 ASP   A OD1 1 
ATOM   1212 O  OD2 . ASP   A 1 153 ? 3.087   -18.135 -22.035 1.00 64.33  ? 153 ASP   A OD2 1 
ATOM   1213 N  N   . TYR   A 1 154 ? 4.625   -20.777 -17.011 1.00 72.40  ? 154 TYR   A N   1 
ATOM   1214 C  CA  . TYR   A 1 154 ? 4.779   -21.996 -16.225 1.00 77.56  ? 154 TYR   A CA  1 
ATOM   1215 C  C   . TYR   A 1 154 ? 6.183   -22.063 -15.608 1.00 73.83  ? 154 TYR   A C   1 
ATOM   1216 O  O   . TYR   A 1 154 ? 6.855   -23.088 -15.690 1.00 79.76  ? 154 TYR   A O   1 
ATOM   1217 C  CB  . TYR   A 1 154 ? 4.391   -23.194 -17.112 1.00 86.39  ? 154 TYR   A CB  1 
ATOM   1218 C  CG  . TYR   A 1 154 ? 3.150   -22.998 -17.984 1.00 99.09  ? 154 TYR   A CG  1 
ATOM   1219 C  CD1 . TYR   A 1 154 ? 1.867   -23.303 -17.526 1.00 101.49 ? 154 TYR   A CD1 1 
ATOM   1220 C  CD2 . TYR   A 1 154 ? 3.264   -22.500 -19.281 1.00 105.89 ? 154 TYR   A CD2 1 
ATOM   1221 C  CE1 . TYR   A 1 154 ? 0.749   -23.108 -18.327 1.00 106.01 ? 154 TYR   A CE1 1 
ATOM   1222 C  CE2 . TYR   A 1 154 ? 2.154   -22.299 -20.089 1.00 104.66 ? 154 TYR   A CE2 1 
ATOM   1223 C  CZ  . TYR   A 1 154 ? 0.893   -22.603 -19.611 1.00 107.12 ? 154 TYR   A CZ  1 
ATOM   1224 O  OH  . TYR   A 1 154 ? -0.181  -22.393 -20.426 1.00 110.37 ? 154 TYR   A OH  1 
ATOM   1225 N  N   . ASP   A 1 155 ? 6.621   -20.959 -14.986 1.00 71.05  ? 155 ASP   A N   1 
ATOM   1226 C  CA  . ASP   A 1 155 ? 7.846   -20.898 -14.188 1.00 65.91  ? 155 ASP   A CA  1 
ATOM   1227 C  C   . ASP   A 1 155 ? 9.132   -20.835 -15.018 1.00 54.45  ? 155 ASP   A C   1 
ATOM   1228 O  O   . ASP   A 1 155 ? 10.216  -20.746 -14.449 1.00 49.59  ? 155 ASP   A O   1 
ATOM   1229 C  CB  . ASP   A 1 155 ? 7.931   -22.009 -13.151 1.00 72.93  ? 155 ASP   A CB  1 
ATOM   1230 C  CG  . ASP   A 1 155 ? 7.668   -21.568 -11.717 1.00 78.40  ? 155 ASP   A CG  1 
ATOM   1231 O  OD1 . ASP   A 1 155 ? 8.456   -20.750 -11.211 1.00 81.92  ? 155 ASP   A OD1 1 
ATOM   1232 O  OD2 . ASP   A 1 155 ? 6.675   -22.034 -11.117 1.00 89.02  ? 155 ASP   A OD2 1 
ATOM   1233 N  N   . CYS   A 1 156 ? 9.037   -20.835 -16.352 1.00 52.30  ? 156 CYS   A N   1 
ATOM   1234 C  CA  . CYS   A 1 156 ? 10.226  -20.707 -17.183 1.00 44.27  ? 156 CYS   A CA  1 
ATOM   1235 C  C   . CYS   A 1 156 ? 10.275  -19.331 -17.856 1.00 35.46  ? 156 CYS   A C   1 
ATOM   1236 O  O   . CYS   A 1 156 ? 9.326   -18.951 -18.512 1.00 31.90  ? 156 CYS   A O   1 
ATOM   1237 C  CB  . CYS   A 1 156 ? 10.239  -21.788 -18.251 1.00 41.55  ? 156 CYS   A CB  1 
ATOM   1238 S  SG  . CYS   A 1 156 ? 11.597  -21.569 -19.428 1.00 41.22  ? 156 CYS   A SG  1 
ATOM   1239 N  N   . VAL   A 1 157 ? 11.382  -18.590 -17.717 1.00 32.05  ? 157 VAL   A N   1 
ATOM   1240 C  CA  . VAL   A 1 157 ? 11.478  -17.263 -18.307 1.00 30.00  ? 157 VAL   A CA  1 
ATOM   1241 C  C   . VAL   A 1 157 ? 11.933  -17.384 -19.771 1.00 29.70  ? 157 VAL   A C   1 
ATOM   1242 O  O   . VAL   A 1 157 ? 13.041  -17.830 -20.029 1.00 29.99  ? 157 VAL   A O   1 
ATOM   1243 C  CB  . VAL   A 1 157 ? 12.438  -16.337 -17.538 1.00 27.79  ? 157 VAL   A CB  1 
ATOM   1244 C  CG1 . VAL   A 1 157 ? 12.463  -14.935 -18.139 1.00 29.03  ? 157 VAL   A CG1 1 
ATOM   1245 C  CG2 . VAL   A 1 157 ? 12.165  -16.252 -16.042 1.00 27.09  ? 157 VAL   A CG2 1 
ATOM   1246 N  N   . SER   A 1 158 ? 11.108  -16.932 -20.728 1.00 27.82  ? 158 SER   A N   1 
ATOM   1247 C  CA  . SER   A 1 158 ? 11.535  -16.831 -22.118 1.00 28.45  ? 158 SER   A CA  1 
ATOM   1248 C  C   . SER   A 1 158 ? 11.970  -15.396 -22.474 1.00 28.52  ? 158 SER   A C   1 
ATOM   1249 O  O   . SER   A 1 158 ? 11.124  -14.492 -22.539 1.00 26.77  ? 158 SER   A O   1 
ATOM   1250 C  CB  . SER   A 1 158 ? 10.448  -17.319 -23.012 1.00 28.45  ? 158 SER   A CB  1 
ATOM   1251 O  OG  . SER   A 1 158 ? 9.244   -16.623 -22.751 1.00 38.21  ? 158 SER   A OG  1 
ATOM   1252 N  N   . PHE   A 1 159 ? 13.278  -15.195 -22.743 1.00 24.72  ? 159 PHE   A N   1 
ATOM   1253 C  CA  . PHE   A 1 159 ? 13.788  -13.890 -23.132 1.00 23.97  ? 159 PHE   A CA  1 
ATOM   1254 C  C   . PHE   A 1 159 ? 13.669  -13.703 -24.642 1.00 26.15  ? 159 PHE   A C   1 
ATOM   1255 O  O   . PHE   A 1 159 ? 14.141  -14.559 -25.391 1.00 28.26  ? 159 PHE   A O   1 
ATOM   1256 C  CB  . PHE   A 1 159 ? 15.242  -13.700 -22.701 1.00 24.01  ? 159 PHE   A CB  1 
ATOM   1257 C  CG  . PHE   A 1 159 ? 15.474  -13.697 -21.197 1.00 24.92  ? 159 PHE   A CG  1 
ATOM   1258 C  CD1 . PHE   A 1 159 ? 15.288  -12.539 -20.446 1.00 28.00  ? 159 PHE   A CD1 1 
ATOM   1259 C  CD2 . PHE   A 1 159 ? 15.916  -14.839 -20.544 1.00 24.76  ? 159 PHE   A CD2 1 
ATOM   1260 C  CE1 . PHE   A 1 159 ? 15.535  -12.527 -19.076 1.00 28.21  ? 159 PHE   A CE1 1 
ATOM   1261 C  CE2 . PHE   A 1 159 ? 16.145  -14.834 -19.176 1.00 25.81  ? 159 PHE   A CE2 1 
ATOM   1262 C  CZ  . PHE   A 1 159 ? 15.962  -13.680 -18.444 1.00 29.70  ? 159 PHE   A CZ  1 
ATOM   1263 N  N   . CYS   A 1 160 ? 13.107  -12.543 -25.069 1.00 26.72  ? 160 CYS   A N   1 
ATOM   1264 C  CA  . CYS   A 1 160 ? 12.770  -12.295 -26.466 1.00 25.18  ? 160 CYS   A CA  1 
ATOM   1265 C  C   . CYS   A 1 160 ? 13.294  -10.957 -27.015 1.00 25.66  ? 160 CYS   A C   1 
ATOM   1266 O  O   . CYS   A 1 160 ? 13.253  -10.793 -28.237 1.00 27.73  ? 160 CYS   A O   1 
ATOM   1267 C  CB  . CYS   A 1 160 ? 11.269  -12.446 -26.713 1.00 24.84  ? 160 CYS   A CB  1 
ATOM   1268 S  SG  . CYS   A 1 160 ? 10.227  -11.275 -25.793 1.00 25.73  ? 160 CYS   A SG  1 
ATOM   1269 N  N   . TYR   A 1 161 ? 13.775  -10.028 -26.162 1.00 23.11  ? 161 TYR   A N   1 
ATOM   1270 C  CA  . TYR   A 1 161 ? 14.174  -8.691  -26.592 1.00 22.09  ? 161 TYR   A CA  1 
ATOM   1271 C  C   . TYR   A 1 161 ? 15.282  -8.131  -25.703 1.00 21.89  ? 161 TYR   A C   1 
ATOM   1272 O  O   . TYR   A 1 161 ? 15.236  -8.292  -24.492 1.00 20.98  ? 161 TYR   A O   1 
ATOM   1273 C  CB  . TYR   A 1 161 ? 12.996  -7.702  -26.602 1.00 20.82  ? 161 TYR   A CB  1 
ATOM   1274 C  CG  . TYR   A 1 161 ? 13.277  -6.250  -27.007 1.00 19.05  ? 161 TYR   A CG  1 
ATOM   1275 C  CD1 . TYR   A 1 161 ? 13.235  -5.849  -28.338 1.00 20.00  ? 161 TYR   A CD1 1 
ATOM   1276 C  CD2 . TYR   A 1 161 ? 13.525  -5.252  -26.070 1.00 20.06  ? 161 TYR   A CD2 1 
ATOM   1277 C  CE1 . TYR   A 1 161 ? 13.476  -4.534  -28.718 1.00 19.43  ? 161 TYR   A CE1 1 
ATOM   1278 C  CE2 . TYR   A 1 161 ? 13.752  -3.920  -26.435 1.00 18.95  ? 161 TYR   A CE2 1 
ATOM   1279 C  CZ  . TYR   A 1 161 ? 13.746  -3.563  -27.774 1.00 19.07  ? 161 TYR   A CZ  1 
ATOM   1280 O  OH  . TYR   A 1 161 ? 13.944  -2.266  -28.218 1.00 21.84  ? 161 TYR   A OH  1 
ATOM   1281 N  N   . MET   A 1 162 ? 16.282  -7.475  -26.332 1.00 23.00  ? 162 MET   A N   1 
ATOM   1282 C  CA  . MET   A 1 162 ? 17.266  -6.646  -25.650 1.00 21.90  ? 162 MET   A CA  1 
ATOM   1283 C  C   . MET   A 1 162 ? 17.314  -5.265  -26.325 1.00 20.04  ? 162 MET   A C   1 
ATOM   1284 O  O   . MET   A 1 162 ? 17.497  -5.172  -27.541 1.00 19.33  ? 162 MET   A O   1 
ATOM   1285 C  CB  . MET   A 1 162 ? 18.653  -7.309  -25.670 1.00 24.17  ? 162 MET   A CB  1 
ATOM   1286 C  CG  . MET   A 1 162 ? 19.728  -6.488  -24.944 1.00 26.43  ? 162 MET   A CG  1 
ATOM   1287 S  SD  . MET   A 1 162 ? 21.365  -7.219  -24.688 1.00 30.05  ? 162 MET   A SD  1 
ATOM   1288 C  CE  . MET   A 1 162 ? 21.104  -8.066  -23.123 1.00 30.06  ? 162 MET   A CE  1 
ATOM   1289 N  N   . HIS   A 1 163 ? 17.211  -4.195  -25.525 1.00 19.00  ? 163 HIS   A N   1 
ATOM   1290 C  CA  . HIS   A 1 163 ? 17.111  -2.832  -26.040 1.00 20.53  ? 163 HIS   A CA  1 
ATOM   1291 C  C   . HIS   A 1 163 ? 18.475  -2.288  -26.501 1.00 22.55  ? 163 HIS   A C   1 
ATOM   1292 O  O   . HIS   A 1 163 ? 19.424  -2.225  -25.704 1.00 20.89  ? 163 HIS   A O   1 
ATOM   1293 C  CB  . HIS   A 1 163 ? 16.488  -1.907  -24.987 1.00 20.06  ? 163 HIS   A CB  1 
ATOM   1294 C  CG  . HIS   A 1 163 ? 16.270  -0.510  -25.472 1.00 20.67  ? 163 HIS   A CG  1 
ATOM   1295 N  ND1 . HIS   A 1 163 ? 15.518  -0.192  -26.585 1.00 22.59  ? 163 HIS   A ND1 1 
ATOM   1296 C  CD2 . HIS   A 1 163 ? 16.704  0.661   -24.965 1.00 21.07  ? 163 HIS   A CD2 1 
ATOM   1297 C  CE1 . HIS   A 1 163 ? 15.537  1.135   -26.757 1.00 23.68  ? 163 HIS   A CE1 1 
ATOM   1298 N  NE2 . HIS   A 1 163 ? 16.247  1.678   -25.776 1.00 23.21  ? 163 HIS   A NE2 1 
ATOM   1299 N  N   . HIS   A 1 164 ? 18.524  -1.786  -27.763 1.00 22.59  ? 164 HIS   A N   1 
ATOM   1300 C  CA  . HIS   A 1 164 ? 19.727  -1.155  -28.310 1.00 23.93  ? 164 HIS   A CA  1 
ATOM   1301 C  C   . HIS   A 1 164 ? 19.587  0.350   -28.589 1.00 24.07  ? 164 HIS   A C   1 
ATOM   1302 O  O   . HIS   A 1 164 ? 20.588  1.032   -28.423 1.00 27.68  ? 164 HIS   A O   1 
ATOM   1303 C  CB  . HIS   A 1 164 ? 20.238  -1.847  -29.589 1.00 23.03  ? 164 HIS   A CB  1 
ATOM   1304 C  CG  . HIS   A 1 164 ? 20.786  -3.245  -29.419 1.00 24.66  ? 164 HIS   A CG  1 
ATOM   1305 N  ND1 . HIS   A 1 164 ? 22.060  -3.616  -29.821 1.00 23.01  ? 164 HIS   A ND1 1 
ATOM   1306 C  CD2 . HIS   A 1 164 ? 20.249  -4.329  -28.857 1.00 23.65  ? 164 HIS   A CD2 1 
ATOM   1307 C  CE1 . HIS   A 1 164 ? 22.248  -4.891  -29.515 1.00 24.29  ? 164 HIS   A CE1 1 
ATOM   1308 N  NE2 . HIS   A 1 164 ? 21.149  -5.360  -28.959 1.00 24.48  ? 164 HIS   A NE2 1 
ATOM   1309 N  N   . MET   A 1 165 ? 18.431  0.889   -29.041 1.00 24.92  ? 165 MET   A N   1 
ATOM   1310 C  CA  . MET   A 1 165 ? 18.406  2.277   -29.527 1.00 28.02  ? 165 MET   A CA  1 
ATOM   1311 C  C   . MET   A 1 165 ? 17.008  2.883   -29.736 1.00 26.23  ? 165 MET   A C   1 
ATOM   1312 O  O   . MET   A 1 165 ? 16.015  2.180   -29.889 1.00 21.39  ? 165 MET   A O   1 
ATOM   1313 C  CB  . MET   A 1 165 ? 19.161  2.387   -30.860 1.00 29.76  ? 165 MET   A CB  1 
ATOM   1314 C  CG  . MET   A 1 165 ? 18.713  1.387   -31.906 1.00 33.22  ? 165 MET   A CG  1 
ATOM   1315 S  SD  . MET   A 1 165 ? 19.639  1.584   -33.438 1.00 43.15  ? 165 MET   A SD  1 
ATOM   1316 C  CE  . MET   A 1 165 ? 18.540  0.880   -34.670 1.00 42.06  ? 165 MET   A CE  1 
ATOM   1317 N  N   . GLU   A 1 166 ? 16.953  4.227   -29.762 1.00 26.00  ? 166 GLU   A N   1 
ATOM   1318 C  CA  . GLU   A 1 166 ? 15.733  4.973   -30.076 1.00 27.52  ? 166 GLU   A CA  1 
ATOM   1319 C  C   . GLU   A 1 166 ? 15.865  5.625   -31.463 1.00 26.98  ? 166 GLU   A C   1 
ATOM   1320 O  O   . GLU   A 1 166 ? 16.922  6.171   -31.794 1.00 25.76  ? 166 GLU   A O   1 
ATOM   1321 C  CB  . GLU   A 1 166 ? 15.415  5.972   -28.958 1.00 28.87  ? 166 GLU   A CB  1 
ATOM   1322 C  CG  . GLU   A 1 166 ? 14.110  6.745   -29.171 1.00 28.84  ? 166 GLU   A CG  1 
ATOM   1323 C  CD  . GLU   A 1 166 ? 13.711  7.684   -28.044 1.00 30.77  ? 166 GLU   A CD  1 
ATOM   1324 O  OE1 . GLU   A 1 166 ? 13.533  7.295   -26.859 1.00 28.04  ? 166 GLU   A OE1 1 
ATOM   1325 O  OE2 . GLU   A 1 166 ? 13.561  8.859   -28.384 1.00 29.28  ? 166 GLU   A OE2 1 
ATOM   1326 N  N   . LEU   A 1 167 ? 14.818  5.482   -32.296 1.00 25.35  ? 167 LEU   A N   1 
ATOM   1327 C  CA  . LEU   A 1 167 ? 14.784  6.008   -33.655 1.00 27.58  ? 167 LEU   A CA  1 
ATOM   1328 C  C   . LEU   A 1 167 ? 14.150  7.401   -33.651 1.00 31.05  ? 167 LEU   A C   1 
ATOM   1329 O  O   . LEU   A 1 167 ? 13.549  7.797   -32.656 1.00 28.51  ? 167 LEU   A O   1 
ATOM   1330 C  CB  . LEU   A 1 167 ? 14.014  5.042   -34.562 1.00 27.73  ? 167 LEU   A CB  1 
ATOM   1331 C  CG  . LEU   A 1 167 ? 14.656  3.668   -34.806 1.00 30.67  ? 167 LEU   A CG  1 
ATOM   1332 C  CD1 . LEU   A 1 167 ? 13.624  2.636   -35.242 1.00 31.18  ? 167 LEU   A CD1 1 
ATOM   1333 C  CD2 . LEU   A 1 167 ? 15.764  3.730   -35.836 1.00 31.33  ? 167 LEU   A CD2 1 
ATOM   1334 N  N   . PRO   A 1 168 ? 14.269  8.200   -34.741 1.00 33.85  ? 168 PRO   A N   1 
ATOM   1335 C  CA  . PRO   A 1 168 ? 13.854  9.612   -34.703 1.00 35.56  ? 168 PRO   A CA  1 
ATOM   1336 C  C   . PRO   A 1 168 ? 12.396  9.887   -34.352 1.00 34.50  ? 168 PRO   A C   1 
ATOM   1337 O  O   . PRO   A 1 168 ? 12.109  10.911  -33.747 1.00 39.90  ? 168 PRO   A O   1 
ATOM   1338 C  CB  . PRO   A 1 168 ? 14.221  10.165  -36.099 1.00 35.38  ? 168 PRO   A CB  1 
ATOM   1339 C  CG  . PRO   A 1 168 ? 15.335  9.228   -36.571 1.00 38.13  ? 168 PRO   A CG  1 
ATOM   1340 C  CD  . PRO   A 1 168 ? 14.948  7.849   -36.001 1.00 34.59  ? 168 PRO   A CD  1 
ATOM   1341 N  N   . THR   A 1 169 ? 11.481  8.977   -34.698 1.00 31.81  ? 169 THR   A N   1 
ATOM   1342 C  CA  . THR   A 1 169 ? 10.075  9.188   -34.381 1.00 30.60  ? 169 THR   A CA  1 
ATOM   1343 C  C   . THR   A 1 169 ? 9.752   8.879   -32.925 1.00 29.56  ? 169 THR   A C   1 
ATOM   1344 O  O   . THR   A 1 169 ? 8.580   8.901   -32.564 1.00 30.32  ? 169 THR   A O   1 
ATOM   1345 C  CB  . THR   A 1 169 ? 9.191   8.358   -35.311 1.00 33.13  ? 169 THR   A CB  1 
ATOM   1346 O  OG1 . THR   A 1 169 ? 9.640   7.005   -35.277 1.00 36.04  ? 169 THR   A OG1 1 
ATOM   1347 C  CG2 . THR   A 1 169 ? 9.265   8.859   -36.740 1.00 31.77  ? 169 THR   A CG2 1 
ATOM   1348 N  N   . GLY   A 1 170 ? 10.740  8.568   -32.079 1.00 28.06  ? 170 GLY   A N   1 
ATOM   1349 C  CA  . GLY   A 1 170 ? 10.444  8.303   -30.674 1.00 28.20  ? 170 GLY   A CA  1 
ATOM   1350 C  C   . GLY   A 1 170 ? 10.127  6.830   -30.341 1.00 28.37  ? 170 GLY   A C   1 
ATOM   1351 O  O   . GLY   A 1 170 ? 9.764   6.554   -29.203 1.00 32.69  ? 170 GLY   A O   1 
ATOM   1352 N  N   . VAL   A 1 171 ? 10.311  5.888   -31.284 1.00 26.28  ? 171 VAL   A N   1 
ATOM   1353 C  CA  . VAL   A 1 171 ? 10.078  4.461   -31.052 1.00 26.56  ? 171 VAL   A CA  1 
ATOM   1354 C  C   . VAL   A 1 171 ? 11.407  3.699   -30.944 1.00 25.05  ? 171 VAL   A C   1 
ATOM   1355 O  O   . VAL   A 1 171 ? 12.473  4.240   -31.254 1.00 22.60  ? 171 VAL   A O   1 
ATOM   1356 C  CB  . VAL   A 1 171 ? 9.153   3.890   -32.156 1.00 26.63  ? 171 VAL   A CB  1 
ATOM   1357 C  CG1 . VAL   A 1 171 ? 7.833   4.657   -32.212 1.00 27.82  ? 171 VAL   A CG1 1 
ATOM   1358 C  CG2 . VAL   A 1 171 ? 9.778   3.870   -33.540 1.00 25.62  ? 171 VAL   A CG2 1 
ATOM   1359 N  N   . HIS   A 1 172 ? 11.331  2.414   -30.527 1.00 25.25  ? 172 HIS   A N   1 
ATOM   1360 C  CA  . HIS   A 1 172 ? 12.488  1.685   -29.999 1.00 23.72  ? 172 HIS   A CA  1 
ATOM   1361 C  C   . HIS   A 1 172 ? 12.824  0.462   -30.865 1.00 24.16  ? 172 HIS   A C   1 
ATOM   1362 O  O   . HIS   A 1 172 ? 11.925  -0.139  -31.473 1.00 21.23  ? 172 HIS   A O   1 
ATOM   1363 C  CB  . HIS   A 1 172 ? 12.248  1.429   -28.502 1.00 23.38  ? 172 HIS   A CB  1 
ATOM   1364 C  CG  . HIS   A 1 172 ? 12.033  2.704   -27.735 1.00 21.68  ? 172 HIS   A CG  1 
ATOM   1365 N  ND1 . HIS   A 1 172 ? 10.822  3.093   -27.207 1.00 19.83  ? 172 HIS   A ND1 1 
ATOM   1366 C  CD2 . HIS   A 1 172 ? 12.885  3.721   -27.486 1.00 21.18  ? 172 HIS   A CD2 1 
ATOM   1367 C  CE1 . HIS   A 1 172 ? 10.955  4.287   -26.631 1.00 21.01  ? 172 HIS   A CE1 1 
ATOM   1368 N  NE2 . HIS   A 1 172 ? 12.195  4.690   -26.797 1.00 21.25  ? 172 HIS   A NE2 1 
ATOM   1369 N  N   . ALA   A 1 173 ? 14.136  0.138   -30.961 1.00 22.22  ? 173 ALA   A N   1 
ATOM   1370 C  CA  . ALA   A 1 173 ? 14.636  -0.986  -31.750 1.00 19.51  ? 173 ALA   A CA  1 
ATOM   1371 C  C   . ALA   A 1 173 ? 15.698  -1.787  -30.987 1.00 21.02  ? 173 ALA   A C   1 
ATOM   1372 O  O   . ALA   A 1 173 ? 16.440  -1.237  -30.164 1.00 19.95  ? 173 ALA   A O   1 
ATOM   1373 C  CB  . ALA   A 1 173 ? 15.171  -0.504  -33.072 1.00 20.76  ? 173 ALA   A CB  1 
ATOM   1374 N  N   . GLY   A 1 174 ? 15.719  -3.113  -31.226 1.00 20.74  ? 174 GLY   A N   1 
ATOM   1375 C  CA  . GLY   A 1 174 ? 16.624  -4.011  -30.521 1.00 20.19  ? 174 GLY   A CA  1 
ATOM   1376 C  C   . GLY   A 1 174 ? 16.763  -5.379  -31.209 1.00 20.04  ? 174 GLY   A C   1 
ATOM   1377 O  O   . GLY   A 1 174 ? 16.292  -5.571  -32.341 1.00 22.56  ? 174 GLY   A O   1 
ATOM   1378 N  N   . THR   A 1 175 ? 17.353  -6.342  -30.468 1.00 20.23  ? 175 THR   A N   1 
ATOM   1379 C  CA  . THR   A 1 175 ? 17.669  -7.686  -30.948 1.00 21.23  ? 175 THR   A CA  1 
ATOM   1380 C  C   . THR   A 1 175 ? 16.946  -8.744  -30.125 1.00 21.42  ? 175 THR   A C   1 
ATOM   1381 O  O   . THR   A 1 175 ? 16.473  -8.478  -29.025 1.00 20.36  ? 175 THR   A O   1 
ATOM   1382 C  CB  . THR   A 1 175 ? 19.177  -7.959  -30.860 1.00 22.47  ? 175 THR   A CB  1 
ATOM   1383 O  OG1 . THR   A 1 175 ? 19.600  -7.945  -29.501 1.00 22.25  ? 175 THR   A OG1 1 
ATOM   1384 C  CG2 . THR   A 1 175 ? 19.993  -6.915  -31.590 1.00 25.10  ? 175 THR   A CG2 1 
ATOM   1385 N  N   . ASP   A 1 176 ? 16.937  -9.986  -30.643 1.00 22.79  ? 176 ASP   A N   1 
ATOM   1386 C  CA  . ASP   A 1 176 ? 16.736  -11.158 -29.801 1.00 22.18  ? 176 ASP   A CA  1 
ATOM   1387 C  C   . ASP   A 1 176 ? 18.002  -11.426 -28.980 1.00 23.50  ? 176 ASP   A C   1 
ATOM   1388 O  O   . ASP   A 1 176 ? 19.003  -10.695 -29.091 1.00 21.00  ? 176 ASP   A O   1 
ATOM   1389 C  CB  . ASP   A 1 176 ? 16.290  -12.340 -30.643 1.00 24.80  ? 176 ASP   A CB  1 
ATOM   1390 C  CG  . ASP   A 1 176 ? 17.301  -12.854 -31.656 1.00 24.64  ? 176 ASP   A CG  1 
ATOM   1391 O  OD1 . ASP   A 1 176 ? 18.530  -12.631 -31.472 1.00 27.69  ? 176 ASP   A OD1 1 
ATOM   1392 O  OD2 . ASP   A 1 176 ? 16.847  -13.428 -32.636 1.00 25.89  ? 176 ASP   A OD2 1 
ATOM   1393 N  N   . LEU   A 1 177 ? 17.959  -12.483 -28.146 1.00 23.57  ? 177 LEU   A N   1 
ATOM   1394 C  CA  . LEU   A 1 177 ? 19.065  -12.792 -27.252 1.00 24.89  ? 177 LEU   A CA  1 
ATOM   1395 C  C   . LEU   A 1 177 ? 20.169  -13.543 -27.987 1.00 25.03  ? 177 LEU   A C   1 
ATOM   1396 O  O   . LEU   A 1 177 ? 21.209  -13.798 -27.382 1.00 28.67  ? 177 LEU   A O   1 
ATOM   1397 C  CB  . LEU   A 1 177 ? 18.640  -13.526 -25.975 1.00 27.00  ? 177 LEU   A CB  1 
ATOM   1398 C  CG  . LEU   A 1 177 ? 18.294  -12.598 -24.810 1.00 28.55  ? 177 LEU   A CG  1 
ATOM   1399 C  CD1 . LEU   A 1 177 ? 19.523  -11.874 -24.300 1.00 30.84  ? 177 LEU   A CD1 1 
ATOM   1400 C  CD2 . LEU   A 1 177 ? 17.255  -11.555 -25.227 1.00 29.80  ? 177 LEU   A CD2 1 
ATOM   1401 N  N   . GLU   A 1 178 ? 19.972  -13.840 -29.280 1.00 26.59  ? 178 GLU   A N   1 
ATOM   1402 C  CA  . GLU   A 1 178 ? 21.064  -14.327 -30.127 1.00 28.34  ? 178 GLU   A CA  1 
ATOM   1403 C  C   . GLU   A 1 178 ? 21.691  -13.182 -30.927 1.00 25.92  ? 178 GLU   A C   1 
ATOM   1404 O  O   . GLU   A 1 178 ? 22.552  -13.440 -31.768 1.00 25.18  ? 178 GLU   A O   1 
ATOM   1405 C  CB  . GLU   A 1 178 ? 20.635  -15.455 -31.069 1.00 28.85  ? 178 GLU   A CB  1 
ATOM   1406 C  CG  . GLU   A 1 178 ? 20.134  -16.687 -30.316 1.00 32.82  ? 178 GLU   A CG  1 
ATOM   1407 C  CD  . GLU   A 1 178 ? 19.590  -17.779 -31.216 1.00 37.84  ? 178 GLU   A CD  1 
ATOM   1408 O  OE1 . GLU   A 1 178 ? 18.813  -17.470 -32.152 1.00 47.01  ? 178 GLU   A OE1 1 
ATOM   1409 O  OE2 . GLU   A 1 178 ? 19.962  -18.943 -30.979 1.00 44.35  ? 178 GLU   A OE2 1 
ATOM   1410 N  N   . GLY   A 1 179 ? 21.240  -11.939 -30.686 1.00 24.24  ? 179 GLY   A N   1 
ATOM   1411 C  CA  . GLY   A 1 179 ? 21.897  -10.742 -31.191 1.00 22.54  ? 179 GLY   A CA  1 
ATOM   1412 C  C   . GLY   A 1 179 ? 21.446  -10.317 -32.589 1.00 24.32  ? 179 GLY   A C   1 
ATOM   1413 O  O   . GLY   A 1 179 ? 22.094  -9.447  -33.182 1.00 25.55  ? 179 GLY   A O   1 
ATOM   1414 N  N   . ASN   A 1 180 ? 20.363  -10.917 -33.125 1.00 26.16  ? 180 ASN   A N   1 
ATOM   1415 C  CA  . ASN   A 1 180 ? 19.832  -10.557 -34.437 1.00 26.32  ? 180 ASN   A CA  1 
ATOM   1416 C  C   . ASN   A 1 180 ? 18.734  -9.520  -34.259 1.00 26.00  ? 180 ASN   A C   1 
ATOM   1417 O  O   . ASN   A 1 180 ? 17.802  -9.737  -33.471 1.00 26.10  ? 180 ASN   A O   1 
ATOM   1418 C  CB  . ASN   A 1 180 ? 19.227  -11.740 -35.182 1.00 28.02  ? 180 ASN   A CB  1 
ATOM   1419 C  CG  . ASN   A 1 180 ? 20.230  -12.847 -35.418 1.00 32.02  ? 180 ASN   A CG  1 
ATOM   1420 O  OD1 . ASN   A 1 180 ? 20.149  -13.917 -34.799 1.00 32.95  ? 180 ASN   A OD1 1 
ATOM   1421 N  ND2 . ASN   A 1 180 ? 21.187  -12.601 -36.295 1.00 30.39  ? 180 ASN   A ND2 1 
ATOM   1422 N  N   . PHE   A 1 181 ? 18.868  -8.403  -34.986 1.00 25.06  ? 181 PHE   A N   1 
ATOM   1423 C  CA  . PHE   A 1 181 ? 17.925  -7.292  -34.919 1.00 24.46  ? 181 PHE   A CA  1 
ATOM   1424 C  C   . PHE   A 1 181 ? 16.545  -7.745  -35.404 1.00 23.20  ? 181 PHE   A C   1 
ATOM   1425 O  O   . PHE   A 1 181 ? 16.426  -8.497  -36.383 1.00 22.70  ? 181 PHE   A O   1 
ATOM   1426 C  CB  . PHE   A 1 181 ? 18.377  -6.083  -35.761 1.00 22.65  ? 181 PHE   A CB  1 
ATOM   1427 C  CG  . PHE   A 1 181 ? 19.078  -4.991  -34.976 1.00 21.53  ? 181 PHE   A CG  1 
ATOM   1428 C  CD1 . PHE   A 1 181 ? 18.350  -3.963  -34.385 1.00 21.51  ? 181 PHE   A CD1 1 
ATOM   1429 C  CD2 . PHE   A 1 181 ? 20.463  -5.018  -34.782 1.00 22.36  ? 181 PHE   A CD2 1 
ATOM   1430 C  CE1 . PHE   A 1 181 ? 18.973  -3.009  -33.588 1.00 20.59  ? 181 PHE   A CE1 1 
ATOM   1431 C  CE2 . PHE   A 1 181 ? 21.087  -4.021  -34.035 1.00 21.75  ? 181 PHE   A CE2 1 
ATOM   1432 C  CZ  . PHE   A 1 181 ? 20.337  -3.020  -33.443 1.00 19.69  ? 181 PHE   A CZ  1 
ATOM   1433 N  N   . TYR   A 1 182 ? 15.498  -7.208  -34.761 1.00 22.28  ? 182 TYR   A N   1 
ATOM   1434 C  CA  . TYR   A 1 182 ? 14.175  -7.218  -35.368 1.00 21.89  ? 182 TYR   A CA  1 
ATOM   1435 C  C   . TYR   A 1 182 ? 14.116  -6.074  -36.396 1.00 23.17  ? 182 TYR   A C   1 
ATOM   1436 O  O   . TYR   A 1 182 ? 14.492  -4.940  -36.105 1.00 23.80  ? 182 TYR   A O   1 
ATOM   1437 C  CB  . TYR   A 1 182 ? 13.112  -7.095  -34.261 1.00 23.93  ? 182 TYR   A CB  1 
ATOM   1438 C  CG  . TYR   A 1 182 ? 12.989  -8.261  -33.283 1.00 24.95  ? 182 TYR   A CG  1 
ATOM   1439 C  CD1 . TYR   A 1 182 ? 12.298  -9.427  -33.638 1.00 24.09  ? 182 TYR   A CD1 1 
ATOM   1440 C  CD2 . TYR   A 1 182 ? 13.541  -8.204  -31.995 1.00 25.75  ? 182 TYR   A CD2 1 
ATOM   1441 C  CE1 . TYR   A 1 182 ? 12.169  -10.491 -32.760 1.00 22.56  ? 182 TYR   A CE1 1 
ATOM   1442 C  CE2 . TYR   A 1 182 ? 13.412  -9.275  -31.108 1.00 26.59  ? 182 TYR   A CE2 1 
ATOM   1443 C  CZ  . TYR   A 1 182 ? 12.703  -10.418 -31.483 1.00 25.02  ? 182 TYR   A CZ  1 
ATOM   1444 O  OH  . TYR   A 1 182 ? 12.544  -11.502 -30.627 1.00 22.57  ? 182 TYR   A OH  1 
ATOM   1445 N  N   . GLY   A 1 183 ? 13.658  -6.369  -37.616 1.00 24.81  ? 183 GLY   A N   1 
ATOM   1446 C  CA  . GLY   A 1 183 ? 13.503  -5.388  -38.680 1.00 25.17  ? 183 GLY   A CA  1 
ATOM   1447 C  C   . GLY   A 1 183 ? 14.802  -5.116  -39.439 1.00 29.27  ? 183 GLY   A C   1 
ATOM   1448 O  O   . GLY   A 1 183 ? 15.848  -5.704  -39.173 1.00 32.67  ? 183 GLY   A O   1 
ATOM   1449 N  N   . PRO   A 1 184 ? 14.817  -4.159  -40.388 1.00 29.21  ? 184 PRO   A N   1 
ATOM   1450 C  CA  . PRO   A 1 184 ? 16.053  -3.870  -41.122 1.00 28.65  ? 184 PRO   A CA  1 
ATOM   1451 C  C   . PRO   A 1 184 ? 17.101  -2.967  -40.449 1.00 26.61  ? 184 PRO   A C   1 
ATOM   1452 O  O   . PRO   A 1 184 ? 17.924  -2.385  -41.124 1.00 30.27  ? 184 PRO   A O   1 
ATOM   1453 C  CB  . PRO   A 1 184 ? 15.429  -3.237  -42.385 1.00 27.97  ? 184 PRO   A CB  1 
ATOM   1454 C  CG  . PRO   A 1 184 ? 14.256  -2.432  -41.856 1.00 31.02  ? 184 PRO   A CG  1 
ATOM   1455 C  CD  . PRO   A 1 184 ? 13.683  -3.294  -40.752 1.00 30.39  ? 184 PRO   A CD  1 
ATOM   1456 N  N   . PHE   A 1 185 ? 17.090  -2.834  -39.120 1.00 26.36  ? 185 PHE   A N   1 
ATOM   1457 C  CA  . PHE   A 1 185 ? 17.944  -1.861  -38.451 1.00 26.64  ? 185 PHE   A CA  1 
ATOM   1458 C  C   . PHE   A 1 185 ? 19.344  -2.433  -38.176 1.00 26.57  ? 185 PHE   A C   1 
ATOM   1459 O  O   . PHE   A 1 185 ? 19.569  -3.655  -38.200 1.00 25.38  ? 185 PHE   A O   1 
ATOM   1460 C  CB  . PHE   A 1 185 ? 17.235  -1.362  -37.185 1.00 25.69  ? 185 PHE   A CB  1 
ATOM   1461 C  CG  . PHE   A 1 185 ? 15.802  -0.951  -37.462 1.00 25.33  ? 185 PHE   A CG  1 
ATOM   1462 C  CD1 . PHE   A 1 185 ? 15.532  0.160   -38.259 1.00 25.95  ? 185 PHE   A CD1 1 
ATOM   1463 C  CD2 . PHE   A 1 185 ? 14.733  -1.678  -36.949 1.00 26.80  ? 185 PHE   A CD2 1 
ATOM   1464 C  CE1 . PHE   A 1 185 ? 14.227  0.524   -38.557 1.00 25.59  ? 185 PHE   A CE1 1 
ATOM   1465 C  CE2 . PHE   A 1 185 ? 13.422  -1.299  -37.242 1.00 26.91  ? 185 PHE   A CE2 1 
ATOM   1466 C  CZ  . PHE   A 1 185 ? 13.174  -0.202  -38.048 1.00 24.78  ? 185 PHE   A CZ  1 
ATOM   1467 N  N   . VAL   A 1 186 ? 20.279  -1.499  -37.941 1.00 27.95  ? 186 VAL   A N   1 
ATOM   1468 C  CA  . VAL   A 1 186 ? 21.687  -1.779  -37.694 1.00 26.46  ? 186 VAL   A CA  1 
ATOM   1469 C  C   . VAL   A 1 186 ? 22.197  -0.934  -36.520 1.00 26.46  ? 186 VAL   A C   1 
ATOM   1470 O  O   . VAL   A 1 186 ? 21.688  0.162   -36.251 1.00 26.54  ? 186 VAL   A O   1 
ATOM   1471 C  CB  . VAL   A 1 186 ? 22.563  -1.522  -38.943 1.00 26.28  ? 186 VAL   A CB  1 
ATOM   1472 C  CG1 . VAL   A 1 186 ? 22.235  -2.450  -40.097 1.00 26.03  ? 186 VAL   A CG1 1 
ATOM   1473 C  CG2 . VAL   A 1 186 ? 22.506  -0.065  -39.394 1.00 28.10  ? 186 VAL   A CG2 1 
ATOM   1474 N  N   . ASP   A 1 187 ? 23.252  -1.437  -35.852 1.00 24.85  ? 187 ASP   A N   1 
ATOM   1475 C  CA  . ASP   A 1 187 ? 23.837  -0.773  -34.694 1.00 23.80  ? 187 ASP   A CA  1 
ATOM   1476 C  C   . ASP   A 1 187 ? 24.935  0.194   -35.138 1.00 25.40  ? 187 ASP   A C   1 
ATOM   1477 O  O   . ASP   A 1 187 ? 26.083  0.043   -34.735 1.00 22.88  ? 187 ASP   A O   1 
ATOM   1478 C  CB  . ASP   A 1 187 ? 24.248  -1.760  -33.616 1.00 22.93  ? 187 ASP   A CB  1 
ATOM   1479 C  CG  . ASP   A 1 187 ? 25.208  -2.884  -33.989 1.00 22.95  ? 187 ASP   A CG  1 
ATOM   1480 O  OD1 . ASP   A 1 187 ? 25.517  -3.079  -35.196 1.00 23.68  ? 187 ASP   A OD1 1 
ATOM   1481 O  OD2 . ASP   A 1 187 ? 25.628  -3.580  -33.062 1.00 23.58  ? 187 ASP   A OD2 1 
ATOM   1482 N  N   . ARG   A 1 188 ? 24.513  1.221   -35.899 1.00 25.45  ? 188 ARG   A N   1 
ATOM   1483 C  CA  . ARG   A 1 188 ? 25.325  2.337   -36.369 1.00 25.55  ? 188 ARG   A CA  1 
ATOM   1484 C  C   . ARG   A 1 188 ? 24.464  3.601   -36.331 1.00 24.97  ? 188 ARG   A C   1 
ATOM   1485 O  O   . ARG   A 1 188 ? 23.256  3.533   -36.511 1.00 22.65  ? 188 ARG   A O   1 
ATOM   1486 C  CB  . ARG   A 1 188 ? 25.713  2.177   -37.852 1.00 26.95  ? 188 ARG   A CB  1 
ATOM   1487 C  CG  . ARG   A 1 188 ? 26.696  1.091   -38.256 1.00 29.10  ? 188 ARG   A CG  1 
ATOM   1488 C  CD  . ARG   A 1 188 ? 26.609  0.685   -39.739 1.00 30.61  ? 188 ARG   A CD  1 
ATOM   1489 N  NE  . ARG   A 1 188 ? 26.860  1.828   -40.620 1.00 28.82  ? 188 ARG   A NE  1 
ATOM   1490 C  CZ  . ARG   A 1 188 ? 26.620  1.882   -41.926 1.00 29.82  ? 188 ARG   A CZ  1 
ATOM   1491 N  NH1 . ARG   A 1 188 ? 25.978  0.897   -42.524 1.00 28.35  ? 188 ARG   A NH1 1 
ATOM   1492 N  NH2 . ARG   A 1 188 ? 26.970  2.954   -42.630 1.00 28.21  ? 188 ARG   A NH2 1 
ATOM   1493 N  N   . GLN   A 1 189 ? 25.083  4.775   -36.179 1.00 27.64  ? 189 GLN   A N   1 
ATOM   1494 C  CA  . GLN   A 1 189 ? 24.323  6.006   -36.055 1.00 32.74  ? 189 GLN   A CA  1 
ATOM   1495 C  C   . GLN   A 1 189 ? 24.065  6.684   -37.397 1.00 34.18  ? 189 GLN   A C   1 
ATOM   1496 O  O   . GLN   A 1 189 ? 23.794  7.879   -37.415 1.00 33.81  ? 189 GLN   A O   1 
ATOM   1497 C  CB  . GLN   A 1 189 ? 25.025  6.939   -35.072 1.00 39.14  ? 189 GLN   A CB  1 
ATOM   1498 C  CG  . GLN   A 1 189 ? 25.096  6.322   -33.678 1.00 47.78  ? 189 GLN   A CG  1 
ATOM   1499 C  CD  . GLN   A 1 189 ? 24.563  7.239   -32.602 1.00 58.96  ? 189 GLN   A CD  1 
ATOM   1500 O  OE1 . GLN   A 1 189 ? 25.100  8.327   -32.358 1.00 61.68  ? 189 GLN   A OE1 1 
ATOM   1501 N  NE2 . GLN   A 1 189 ? 23.473  6.812   -31.974 1.00 60.19  ? 189 GLN   A NE2 1 
ATOM   1502 N  N   . THR   A 1 190 ? 24.138  5.924   -38.500 1.00 33.30  ? 190 THR   A N   1 
ATOM   1503 C  CA  . THR   A 1 190 ? 23.733  6.399   -39.816 1.00 31.66  ? 190 THR   A CA  1 
ATOM   1504 C  C   . THR   A 1 190 ? 22.218  6.538   -39.821 1.00 29.79  ? 190 THR   A C   1 
ATOM   1505 O  O   . THR   A 1 190 ? 21.537  5.853   -39.066 1.00 27.80  ? 190 THR   A O   1 
ATOM   1506 C  CB  . THR   A 1 190 ? 24.214  5.426   -40.897 1.00 31.37  ? 190 THR   A CB  1 
ATOM   1507 O  OG1 . THR   A 1 190 ? 24.106  6.125   -42.138 1.00 32.22  ? 190 THR   A OG1 1 
ATOM   1508 C  CG2 . THR   A 1 190 ? 23.435  4.120   -40.891 1.00 30.10  ? 190 THR   A CG2 1 
ATOM   1509 N  N   . ALA   A 1 191 ? 21.704  7.408   -40.692 1.00 30.89  ? 191 ALA   A N   1 
ATOM   1510 C  CA  . ALA   A 1 191 ? 20.283  7.742   -40.699 1.00 33.37  ? 191 ALA   A CA  1 
ATOM   1511 C  C   . ALA   A 1 191 ? 19.422  6.526   -41.042 1.00 30.79  ? 191 ALA   A C   1 
ATOM   1512 O  O   . ALA   A 1 191 ? 19.695  5.808   -42.002 1.00 30.99  ? 191 ALA   A O   1 
ATOM   1513 C  CB  . ALA   A 1 191 ? 20.014  8.873   -41.673 1.00 35.64  ? 191 ALA   A CB  1 
ATOM   1514 N  N   . GLN   A 1 192 ? 18.379  6.322   -40.232 1.00 31.30  ? 192 GLN   A N   1 
ATOM   1515 C  CA  . GLN   A 1 192 ? 17.514  5.157   -40.304 1.00 30.82  ? 192 GLN   A CA  1 
ATOM   1516 C  C   . GLN   A 1 192 ? 16.136  5.594   -39.815 1.00 29.79  ? 192 GLN   A C   1 
ATOM   1517 O  O   . GLN   A 1 192 ? 16.034  6.415   -38.907 1.00 31.23  ? 192 GLN   A O   1 
ATOM   1518 C  CB  . GLN   A 1 192 ? 17.918  4.022   -39.363 1.00 29.94  ? 192 GLN   A CB  1 
ATOM   1519 C  CG  . GLN   A 1 192 ? 19.330  3.490   -39.517 1.00 30.51  ? 192 GLN   A CG  1 
ATOM   1520 C  CD  . GLN   A 1 192 ? 19.614  2.326   -38.590 1.00 33.34  ? 192 GLN   A CD  1 
ATOM   1521 O  OE1 . GLN   A 1 192 ? 19.055  1.233   -38.728 1.00 30.14  ? 192 GLN   A OE1 1 
ATOM   1522 N  NE2 . GLN   A 1 192 ? 20.492  2.541   -37.621 1.00 35.95  ? 192 GLN   A NE2 1 
ATOM   1523 N  N   . ALA   A 1 193 ? 15.088  5.009   -40.391 1.00 30.53  ? 193 ALA   A N   1 
ATOM   1524 C  CA  . ALA   A 1 193 ? 13.728  5.341   -40.001 1.00 33.07  ? 193 ALA   A CA  1 
ATOM   1525 C  C   . ALA   A 1 193 ? 12.844  4.110   -40.171 1.00 34.20  ? 193 ALA   A C   1 
ATOM   1526 O  O   . ALA   A 1 193 ? 13.043  3.289   -41.066 1.00 29.40  ? 193 ALA   A O   1 
ATOM   1527 C  CB  . ALA   A 1 193 ? 13.213  6.515   -40.814 1.00 30.46  ? 193 ALA   A CB  1 
ATOM   1528 N  N   . ALA   A 1 194 ? 11.846  4.005   -39.293 1.00 38.35  ? 194 ALA   A N   1 
ATOM   1529 C  CA  . ALA   A 1 194 ? 10.894  2.910   -39.349 1.00 35.80  ? 194 ALA   A CA  1 
ATOM   1530 C  C   . ALA   A 1 194 ? 9.912   3.138   -40.500 1.00 36.50  ? 194 ALA   A C   1 
ATOM   1531 O  O   . ALA   A 1 194 ? 9.587   4.292   -40.813 1.00 31.70  ? 194 ALA   A O   1 
ATOM   1532 C  CB  . ALA   A 1 194 ? 10.192  2.842   -38.016 1.00 40.84  ? 194 ALA   A CB  1 
ATOM   1533 N  N   . GLY   A 1 195 ? 9.481   2.035   -41.132 1.00 38.74  ? 195 GLY   A N   1 
ATOM   1534 C  CA  . GLY   A 1 195 ? 8.352   2.021   -42.052 1.00 39.32  ? 195 GLY   A CA  1 
ATOM   1535 C  C   . GLY   A 1 195 ? 7.061   2.506   -41.379 1.00 39.21  ? 195 GLY   A C   1 
ATOM   1536 O  O   . GLY   A 1 195 ? 6.987   2.574   -40.150 1.00 34.54  ? 195 GLY   A O   1 
ATOM   1537 N  N   . THR   A 1 196 ? 6.061   2.879   -42.202 1.00 38.80  ? 196 THR   A N   1 
ATOM   1538 C  CA  . THR   A 1 196 ? 4.763   3.337   -41.715 1.00 38.56  ? 196 THR   A CA  1 
ATOM   1539 C  C   . THR   A 1 196 ? 4.141   2.176   -40.937 1.00 34.65  ? 196 THR   A C   1 
ATOM   1540 O  O   . THR   A 1 196 ? 4.240   1.031   -41.352 1.00 36.36  ? 196 THR   A O   1 
ATOM   1541 C  CB  . THR   A 1 196 ? 3.864   3.789   -42.874 1.00 39.53  ? 196 THR   A CB  1 
ATOM   1542 O  OG1 . THR   A 1 196 ? 3.848   2.633   -43.695 1.00 40.19  ? 196 THR   A OG1 1 
ATOM   1543 C  CG2 . THR   A 1 196 ? 4.413   4.942   -43.702 1.00 41.35  ? 196 THR   A CG2 1 
ATOM   1544 N  N   . ASP   A 1 197 ? 3.528   2.451   -39.791 1.00 36.43  ? 197 ASP   A N   1 
ATOM   1545 C  CA  . ASP   A 1 197 ? 3.042   1.367   -38.950 1.00 37.89  ? 197 ASP   A CA  1 
ATOM   1546 C  C   . ASP   A 1 197 ? 1.589   1.050   -39.310 1.00 37.09  ? 197 ASP   A C   1 
ATOM   1547 O  O   . ASP   A 1 197 ? 0.924   1.863   -39.944 1.00 37.80  ? 197 ASP   A O   1 
ATOM   1548 C  CB  . ASP   A 1 197 ? 3.185   1.665   -37.466 1.00 38.12  ? 197 ASP   A CB  1 
ATOM   1549 C  CG  . ASP   A 1 197 ? 3.182   0.422   -36.579 1.00 39.08  ? 197 ASP   A CG  1 
ATOM   1550 O  OD1 . ASP   A 1 197 ? 3.547   -0.675  -37.099 1.00 35.11  ? 197 ASP   A OD1 1 
ATOM   1551 O  OD2 . ASP   A 1 197 ? 2.816   0.561   -35.394 1.00 33.80  ? 197 ASP   A OD2 1 
ATOM   1552 N  N   . THR   A 1 198 ? 1.126   -0.144  -38.911 1.00 32.21  ? 198 THR   A N   1 
ATOM   1553 C  CA  . THR   A 1 198 ? -0.240  -0.558  -39.155 1.00 32.26  ? 198 THR   A CA  1 
ATOM   1554 C  C   . THR   A 1 198 ? -0.813  -1.145  -37.865 1.00 29.20  ? 198 THR   A C   1 
ATOM   1555 O  O   . THR   A 1 198 ? -0.068  -1.420  -36.921 1.00 30.49  ? 198 THR   A O   1 
ATOM   1556 C  CB  . THR   A 1 198 ? -0.216  -1.529  -40.331 1.00 33.96  ? 198 THR   A CB  1 
ATOM   1557 O  OG1 . THR   A 1 198 ? 0.727   -2.537  -39.990 1.00 34.82  ? 198 THR   A OG1 1 
ATOM   1558 C  CG2 . THR   A 1 198 ? 0.241   -0.855  -41.609 1.00 33.60  ? 198 THR   A CG2 1 
ATOM   1559 N  N   . THR   A 1 199 ? -2.142  -1.273  -37.807 1.00 25.07  ? 199 THR   A N   1 
ATOM   1560 C  CA  . THR   A 1 199 ? -2.813  -1.822  -36.644 1.00 23.39  ? 199 THR   A CA  1 
ATOM   1561 C  C   . THR   A 1 199 ? -2.860  -3.341  -36.743 1.00 21.52  ? 199 THR   A C   1 
ATOM   1562 O  O   . THR   A 1 199 ? -3.036  -3.879  -37.830 1.00 22.61  ? 199 THR   A O   1 
ATOM   1563 C  CB  . THR   A 1 199 ? -4.221  -1.255  -36.517 1.00 26.63  ? 199 THR   A CB  1 
ATOM   1564 O  OG1 . THR   A 1 199 ? -4.101  0.163   -36.516 1.00 24.03  ? 199 THR   A OG1 1 
ATOM   1565 C  CG2 . THR   A 1 199 ? -4.925  -1.775  -35.276 1.00 26.53  ? 199 THR   A CG2 1 
ATOM   1566 N  N   . ILE   A 1 200 ? -2.744  -4.014  -35.585 1.00 21.14  ? 200 ILE   A N   1 
ATOM   1567 C  CA  . ILE   A 1 200 ? -2.682  -5.467  -35.500 1.00 22.61  ? 200 ILE   A CA  1 
ATOM   1568 C  C   . ILE   A 1 200 ? -4.099  -6.051  -35.380 1.00 22.40  ? 200 ILE   A C   1 
ATOM   1569 O  O   . ILE   A 1 200 ? -4.614  -6.241  -34.275 1.00 22.34  ? 200 ILE   A O   1 
ATOM   1570 C  CB  . ILE   A 1 200 ? -1.797  -5.896  -34.319 1.00 22.90  ? 200 ILE   A CB  1 
ATOM   1571 C  CG1 . ILE   A 1 200 ? -0.417  -5.197  -34.321 1.00 24.70  ? 200 ILE   A CG1 1 
ATOM   1572 C  CG2 . ILE   A 1 200 ? -1.647  -7.426  -34.284 1.00 23.09  ? 200 ILE   A CG2 1 
ATOM   1573 C  CD1 . ILE   A 1 200 ? 0.345   -5.365  -33.013 1.00 24.06  ? 200 ILE   A CD1 1 
ATOM   1574 N  N   . THR   A 1 201 ? -4.682  -6.396  -36.531 1.00 23.71  ? 201 THR   A N   1 
ATOM   1575 C  CA  . THR   A 1 201 ? -6.110  -6.676  -36.662 1.00 23.87  ? 201 THR   A CA  1 
ATOM   1576 C  C   . THR   A 1 201 ? -6.537  -7.857  -35.780 1.00 24.53  ? 201 THR   A C   1 
ATOM   1577 O  O   . THR   A 1 201 ? -7.534  -7.770  -35.055 1.00 26.72  ? 201 THR   A O   1 
ATOM   1578 C  CB  . THR   A 1 201 ? -6.416  -6.902  -38.148 1.00 23.22  ? 201 THR   A CB  1 
ATOM   1579 O  OG1 . THR   A 1 201 ? -5.911  -5.805  -38.908 1.00 20.74  ? 201 THR   A OG1 1 
ATOM   1580 C  CG2 . THR   A 1 201 ? -7.905  -7.017  -38.428 1.00 22.33  ? 201 THR   A CG2 1 
ATOM   1581 N  N   . VAL   A 1 202 ? -5.779  -8.960  -35.797 1.00 26.29  ? 202 VAL   A N   1 
ATOM   1582 C  CA  . VAL   A 1 202 ? -6.144  -10.136 -35.019 1.00 26.09  ? 202 VAL   A CA  1 
ATOM   1583 C  C   . VAL   A 1 202 ? -6.245  -9.790  -33.526 1.00 26.63  ? 202 VAL   A C   1 
ATOM   1584 O  O   . VAL   A 1 202 ? -7.122  -10.304 -32.823 1.00 25.92  ? 202 VAL   A O   1 
ATOM   1585 C  CB  . VAL   A 1 202 ? -5.214  -11.330 -35.310 1.00 26.47  ? 202 VAL   A CB  1 
ATOM   1586 C  CG1 . VAL   A 1 202 ? -3.758  -11.115 -34.897 1.00 29.61  ? 202 VAL   A CG1 1 
ATOM   1587 C  CG2 . VAL   A 1 202 ? -5.745  -12.597 -34.673 1.00 27.41  ? 202 VAL   A CG2 1 
ATOM   1588 N  N   . ASN   A 1 203 ? -5.406  -8.866  -33.048 1.00 26.12  ? 203 ASN   A N   1 
ATOM   1589 C  CA  . ASN   A 1 203 ? -5.393  -8.468  -31.638 1.00 24.40  ? 203 ASN   A CA  1 
ATOM   1590 C  C   . ASN   A 1 203 ? -6.615  -7.606  -31.281 1.00 23.84  ? 203 ASN   A C   1 
ATOM   1591 O  O   . ASN   A 1 203 ? -7.219  -7.779  -30.207 1.00 23.08  ? 203 ASN   A O   1 
ATOM   1592 C  CB  . ASN   A 1 203 ? -4.091  -7.750  -31.287 1.00 24.53  ? 203 ASN   A CB  1 
ATOM   1593 C  CG  . ASN   A 1 203 ? -2.915  -8.675  -31.084 1.00 22.96  ? 203 ASN   A CG  1 
ATOM   1594 O  OD1 . ASN   A 1 203 ? -3.003  -9.888  -31.318 1.00 22.34  ? 203 ASN   A OD1 1 
ATOM   1595 N  ND2 . ASN   A 1 203 ? -1.788  -8.106  -30.673 1.00 25.83  ? 203 ASN   A ND2 1 
ATOM   1596 N  N   . VAL   A 1 204 ? -6.992  -6.689  -32.181 1.00 23.96  ? 204 VAL   A N   1 
ATOM   1597 C  CA  . VAL   A 1 204 ? -8.201  -5.887  -31.998 1.00 24.59  ? 204 VAL   A CA  1 
ATOM   1598 C  C   . VAL   A 1 204 ? -9.434  -6.792  -31.884 1.00 26.62  ? 204 VAL   A C   1 
ATOM   1599 O  O   . VAL   A 1 204 ? -10.268 -6.607  -30.996 1.00 28.38  ? 204 VAL   A O   1 
ATOM   1600 C  CB  . VAL   A 1 204 ? -8.395  -4.841  -33.109 1.00 24.69  ? 204 VAL   A CB  1 
ATOM   1601 C  CG1 . VAL   A 1 204 ? -9.668  -4.039  -32.890 1.00 26.40  ? 204 VAL   A CG1 1 
ATOM   1602 C  CG2 . VAL   A 1 204 ? -7.204  -3.883  -33.223 1.00 22.62  ? 204 VAL   A CG2 1 
ATOM   1603 N  N   . LEU   A 1 205 ? -9.545  -7.785  -32.767 1.00 24.94  ? 205 LEU   A N   1 
ATOM   1604 C  CA  . LEU   A 1 205 ? -10.640 -8.741  -32.679 1.00 26.11  ? 205 LEU   A CA  1 
ATOM   1605 C  C   . LEU   A 1 205 ? -10.637 -9.461  -31.327 1.00 24.38  ? 205 LEU   A C   1 
ATOM   1606 O  O   . LEU   A 1 205 ? -11.711 -9.641  -30.740 1.00 22.53  ? 205 LEU   A O   1 
ATOM   1607 C  CB  . LEU   A 1 205 ? -10.645 -9.720  -33.855 1.00 26.20  ? 205 LEU   A CB  1 
ATOM   1608 C  CG  . LEU   A 1 205 ? -10.981 -9.094  -35.220 1.00 25.67  ? 205 LEU   A CG  1 
ATOM   1609 C  CD1 . LEU   A 1 205 ? -10.674 -10.033 -36.372 1.00 26.86  ? 205 LEU   A CD1 1 
ATOM   1610 C  CD2 . LEU   A 1 205 ? -12.439 -8.632  -35.282 1.00 25.35  ? 205 LEU   A CD2 1 
ATOM   1611 N  N   . ALA   A 1 206 ? -9.463  -9.867  -30.812 1.00 23.37  ? 206 ALA   A N   1 
ATOM   1612 C  CA  . ALA   A 1 206 ? -9.411  -10.597 -29.547 1.00 24.80  ? 206 ALA   A CA  1 
ATOM   1613 C  C   . ALA   A 1 206 ? -9.931  -9.735  -28.392 1.00 24.54  ? 206 ALA   A C   1 
ATOM   1614 O  O   . ALA   A 1 206 ? -10.655 -10.217 -27.522 1.00 26.47  ? 206 ALA   A O   1 
ATOM   1615 C  CB  . ALA   A 1 206 ? -8.010  -11.112 -29.272 1.00 27.85  ? 206 ALA   A CB  1 
ATOM   1616 N  N   . TRP   A 1 207 ? -9.613  -8.442  -28.447 1.00 24.56  ? 207 TRP   A N   1 
ATOM   1617 C  CA  . TRP   A 1 207 ? -10.025 -7.470  -27.452 1.00 24.46  ? 207 TRP   A CA  1 
ATOM   1618 C  C   . TRP   A 1 207 ? -11.533 -7.218  -27.486 1.00 26.98  ? 207 TRP   A C   1 
ATOM   1619 O  O   . TRP   A 1 207 ? -12.131 -7.044  -26.426 1.00 30.33  ? 207 TRP   A O   1 
ATOM   1620 C  CB  . TRP   A 1 207 ? -9.212  -6.199  -27.711 1.00 24.01  ? 207 TRP   A CB  1 
ATOM   1621 C  CG  . TRP   A 1 207 ? -9.494  -5.018  -26.826 1.00 25.80  ? 207 TRP   A CG  1 
ATOM   1622 C  CD1 . TRP   A 1 207 ? -9.097  -4.813  -25.536 1.00 28.04  ? 207 TRP   A CD1 1 
ATOM   1623 C  CD2 . TRP   A 1 207 ? -10.153 -3.805  -27.237 1.00 27.14  ? 207 TRP   A CD2 1 
ATOM   1624 N  NE1 . TRP   A 1 207 ? -9.496  -3.571  -25.112 1.00 26.85  ? 207 TRP   A NE1 1 
ATOM   1625 C  CE2 . TRP   A 1 207 ? -10.122 -2.922  -26.135 1.00 28.89  ? 207 TRP   A CE2 1 
ATOM   1626 C  CE3 . TRP   A 1 207 ? -10.760 -3.385  -28.421 1.00 28.31  ? 207 TRP   A CE3 1 
ATOM   1627 C  CZ2 . TRP   A 1 207 ? -10.680 -1.646  -26.184 1.00 30.28  ? 207 TRP   A CZ2 1 
ATOM   1628 C  CZ3 . TRP   A 1 207 ? -11.309 -2.120  -28.469 1.00 32.30  ? 207 TRP   A CZ3 1 
ATOM   1629 C  CH2 . TRP   A 1 207 ? -11.234 -1.253  -27.375 1.00 30.06  ? 207 TRP   A CH2 1 
ATOM   1630 N  N   . LEU   A 1 208 ? -12.152 -7.206  -28.681 1.00 27.92  ? 208 LEU   A N   1 
ATOM   1631 C  CA  . LEU   A 1 208 ? -13.612 -7.123  -28.810 1.00 25.12  ? 208 LEU   A CA  1 
ATOM   1632 C  C   . LEU   A 1 208 ? -14.252 -8.373  -28.186 1.00 24.77  ? 208 LEU   A C   1 
ATOM   1633 O  O   . LEU   A 1 208 ? -15.264 -8.284  -27.492 1.00 26.13  ? 208 LEU   A O   1 
ATOM   1634 C  CB  . LEU   A 1 208 ? -14.045 -6.931  -30.263 1.00 25.49  ? 208 LEU   A CB  1 
ATOM   1635 C  CG  . LEU   A 1 208 ? -13.735 -5.583  -30.930 1.00 26.63  ? 208 LEU   A CG  1 
ATOM   1636 C  CD1 . LEU   A 1 208 ? -14.305 -5.590  -32.342 1.00 26.36  ? 208 LEU   A CD1 1 
ATOM   1637 C  CD2 . LEU   A 1 208 ? -14.225 -4.332  -30.228 1.00 30.19  ? 208 LEU   A CD2 1 
ATOM   1638 N  N   . TYR   A 1 209 ? -13.648 -9.547  -28.375 1.00 25.98  ? 209 TYR   A N   1 
ATOM   1639 C  CA  . TYR   A 1 209 ? -14.128 -10.761 -27.721 1.00 29.56  ? 209 TYR   A CA  1 
ATOM   1640 C  C   . TYR   A 1 209 ? -14.035 -10.612 -26.190 1.00 32.41  ? 209 TYR   A C   1 
ATOM   1641 O  O   . TYR   A 1 209 ? -14.958 -11.023 -25.479 1.00 31.19  ? 209 TYR   A O   1 
ATOM   1642 C  CB  . TYR   A 1 209 ? -13.441 -12.038 -28.241 1.00 28.22  ? 209 TYR   A CB  1 
ATOM   1643 C  CG  . TYR   A 1 209 ? -14.016 -12.639 -29.517 1.00 28.40  ? 209 TYR   A CG  1 
ATOM   1644 C  CD1 . TYR   A 1 209 ? -15.293 -13.197 -29.546 1.00 28.53  ? 209 TYR   A CD1 1 
ATOM   1645 C  CD2 . TYR   A 1 209 ? -13.276 -12.683 -30.691 1.00 29.53  ? 209 TYR   A CD2 1 
ATOM   1646 C  CE1 . TYR   A 1 209 ? -15.832 -13.722 -30.710 1.00 28.60  ? 209 TYR   A CE1 1 
ATOM   1647 C  CE2 . TYR   A 1 209 ? -13.800 -13.213 -31.858 1.00 30.01  ? 209 TYR   A CE2 1 
ATOM   1648 C  CZ  . TYR   A 1 209 ? -15.084 -13.733 -31.875 1.00 29.22  ? 209 TYR   A CZ  1 
ATOM   1649 O  OH  . TYR   A 1 209 ? -15.557 -14.312 -33.028 1.00 28.24  ? 209 TYR   A OH  1 
ATOM   1650 N  N   . ALA   A 1 210 ? -12.968 -9.969  -25.686 1.00 31.58  ? 210 ALA   A N   1 
ATOM   1651 C  CA  . ALA   A 1 210 ? -12.800 -9.738  -24.252 1.00 33.13  ? 210 ALA   A CA  1 
ATOM   1652 C  C   . ALA   A 1 210 ? -13.910 -8.840  -23.702 1.00 35.02  ? 210 ALA   A C   1 
ATOM   1653 O  O   . ALA   A 1 210 ? -14.380 -9.044  -22.575 1.00 32.72  ? 210 ALA   A O   1 
ATOM   1654 C  CB  . ALA   A 1 210 ? -11.458 -9.103  -23.951 1.00 31.15  ? 210 ALA   A CB  1 
ATOM   1655 N  N   . ALA   A 1 211 ? -14.251 -7.801  -24.465 1.00 32.96  ? 211 ALA   A N   1 
ATOM   1656 C  CA  . ALA   A 1 211 ? -15.312 -6.887  -24.077 1.00 35.19  ? 211 ALA   A CA  1 
ATOM   1657 C  C   . ALA   A 1 211 ? -16.639 -7.635  -23.948 1.00 34.98  ? 211 ALA   A C   1 
ATOM   1658 O  O   . ALA   A 1 211 ? -17.367 -7.391  -22.993 1.00 29.74  ? 211 ALA   A O   1 
ATOM   1659 C  CB  . ALA   A 1 211 ? -15.437 -5.751  -25.065 1.00 35.94  ? 211 ALA   A CB  1 
ATOM   1660 N  N   . VAL   A 1 212 ? -16.927 -8.560  -24.880 1.00 33.83  ? 212 VAL   A N   1 
ATOM   1661 C  CA  . VAL   A 1 212 ? -18.180 -9.297  -24.841 1.00 33.85  ? 212 VAL   A CA  1 
ATOM   1662 C  C   . VAL   A 1 212 ? -18.221 -10.229 -23.626 1.00 38.46  ? 212 VAL   A C   1 
ATOM   1663 O  O   . VAL   A 1 212 ? -19.244 -10.334 -22.940 1.00 36.59  ? 212 VAL   A O   1 
ATOM   1664 C  CB  . VAL   A 1 212 ? -18.419 -10.045 -26.165 1.00 31.46  ? 212 VAL   A CB  1 
ATOM   1665 C  CG1 . VAL   A 1 212 ? -19.526 -11.101 -26.059 1.00 29.82  ? 212 VAL   A CG1 1 
ATOM   1666 C  CG2 . VAL   A 1 212 ? -18.713 -9.058  -27.289 1.00 30.57  ? 212 VAL   A CG2 1 
ATOM   1667 N  N   . ILE   A 1 213 ? -17.102 -10.904 -23.363 1.00 37.00  ? 213 ILE   A N   1 
ATOM   1668 C  CA  . ILE   A 1 213 ? -16.941 -11.714 -22.165 1.00 34.53  ? 213 ILE   A CA  1 
ATOM   1669 C  C   . ILE   A 1 213 ? -17.170 -10.870 -20.908 1.00 34.65  ? 213 ILE   A C   1 
ATOM   1670 O  O   . ILE   A 1 213 ? -17.752 -11.367 -19.951 1.00 36.37  ? 213 ILE   A O   1 
ATOM   1671 C  CB  . ILE   A 1 213 ? -15.560 -12.397 -22.157 1.00 35.47  ? 213 ILE   A CB  1 
ATOM   1672 C  CG1 . ILE   A 1 213 ? -15.494 -13.536 -23.191 1.00 33.60  ? 213 ILE   A CG1 1 
ATOM   1673 C  CG2 . ILE   A 1 213 ? -15.193 -12.874 -20.749 1.00 35.96  ? 213 ILE   A CG2 1 
ATOM   1674 C  CD1 . ILE   A 1 213 ? -14.099 -14.074 -23.462 1.00 33.45  ? 213 ILE   A CD1 1 
ATOM   1675 N  N   . ASN   A 1 214 ? -16.748 -9.600  -20.898 1.00 34.43  ? 214 ASN   A N   1 
ATOM   1676 C  CA  . ASN   A 1 214 ? -16.894 -8.753  -19.721 1.00 38.30  ? 214 ASN   A CA  1 
ATOM   1677 C  C   . ASN   A 1 214 ? -18.235 -8.012  -19.685 1.00 39.79  ? 214 ASN   A C   1 
ATOM   1678 O  O   . ASN   A 1 214 ? -18.434 -7.174  -18.809 1.00 41.48  ? 214 ASN   A O   1 
ATOM   1679 C  CB  . ASN   A 1 214 ? -15.723 -7.785  -19.590 1.00 43.88  ? 214 ASN   A CB  1 
ATOM   1680 C  CG  . ASN   A 1 214 ? -14.520 -8.455  -18.966 1.00 50.11  ? 214 ASN   A CG  1 
ATOM   1681 O  OD1 . ASN   A 1 214 ? -13.866 -9.299  -19.593 1.00 57.58  ? 214 ASN   A OD1 1 
ATOM   1682 N  ND2 . ASN   A 1 214 ? -14.237 -8.123  -17.719 1.00 47.83  ? 214 ASN   A ND2 1 
ATOM   1683 N  N   . GLY   A 1 215 ? -19.129 -8.279  -20.646 1.00 39.74  ? 215 GLY   A N   1 
ATOM   1684 C  CA  . GLY   A 1 215 ? -20.522 -7.856  -20.556 1.00 41.31  ? 215 GLY   A CA  1 
ATOM   1685 C  C   . GLY   A 1 215 ? -20.944 -6.675  -21.440 1.00 42.22  ? 215 GLY   A C   1 
ATOM   1686 O  O   . GLY   A 1 215 ? -22.023 -6.128  -21.220 1.00 45.72  ? 215 GLY   A O   1 
ATOM   1687 N  N   A ASP   A 1 216 ? -20.076 -6.277  -22.388 0.28 40.85  ? 216 ASP   A N   1 
ATOM   1688 N  N   B ASP   A 1 216 ? -20.139 -6.322  -22.449 0.22 40.47  ? 216 ASP   A N   1 
ATOM   1689 N  N   C ASP   A 1 216 ? -20.076 -6.277  -22.388 0.28 40.85  ? 216 ASP   A N   1 
ATOM   1690 N  N   D ASP   A 1 216 ? -20.139 -6.322  -22.449 0.22 40.47  ? 216 ASP   A N   1 
ATOM   1691 C  CA  A ASP   A 1 216 ? -20.355 -5.216  -23.348 0.28 40.35  ? 216 ASP   A CA  1 
ATOM   1692 C  CA  B ASP   A 1 216 ? -20.473 -5.185  -23.290 0.22 39.62  ? 216 ASP   A CA  1 
ATOM   1693 C  CA  C ASP   A 1 216 ? -20.355 -5.216  -23.348 0.28 40.35  ? 216 ASP   A CA  1 
ATOM   1694 C  CA  D ASP   A 1 216 ? -20.473 -5.185  -23.290 0.22 39.62  ? 216 ASP   A CA  1 
ATOM   1695 C  C   A ASP   A 1 216 ? -20.904 -5.846  -24.628 0.28 39.45  ? 216 ASP   A C   1 
ATOM   1696 C  C   B ASP   A 1 216 ? -20.824 -5.681  -24.691 0.22 38.75  ? 216 ASP   A C   1 
ATOM   1697 C  C   C ASP   A 1 216 ? -20.904 -5.846  -24.628 0.28 39.45  ? 216 ASP   A C   1 
ATOM   1698 C  C   D ASP   A 1 216 ? -20.824 -5.681  -24.691 0.22 38.75  ? 216 ASP   A C   1 
ATOM   1699 O  O   A ASP   A 1 216 ? -20.297 -6.779  -25.148 0.28 39.92  ? 216 ASP   A O   1 
ATOM   1700 O  O   B ASP   A 1 216 ? -20.005 -6.317  -25.350 0.22 38.10  ? 216 ASP   A O   1 
ATOM   1701 O  O   C ASP   A 1 216 ? -20.297 -6.779  -25.148 0.28 39.92  ? 216 ASP   A O   1 
ATOM   1702 O  O   D ASP   A 1 216 ? -20.005 -6.317  -25.350 0.22 38.10  ? 216 ASP   A O   1 
ATOM   1703 C  CB  A ASP   A 1 216 ? -19.098 -4.427  -23.700 0.28 40.75  ? 216 ASP   A CB  1 
ATOM   1704 C  CB  B ASP   A 1 216 ? -19.384 -4.125  -23.255 0.22 39.19  ? 216 ASP   A CB  1 
ATOM   1705 C  CB  C ASP   A 1 216 ? -19.098 -4.427  -23.700 0.28 40.75  ? 216 ASP   A CB  1 
ATOM   1706 C  CB  D ASP   A 1 216 ? -19.384 -4.125  -23.255 0.22 39.19  ? 216 ASP   A CB  1 
ATOM   1707 C  CG  A ASP   A 1 216 ? -18.489 -3.533  -22.623 0.28 40.98  ? 216 ASP   A CG  1 
ATOM   1708 C  CG  B ASP   A 1 216 ? -19.883 -2.696  -23.411 0.22 39.10  ? 216 ASP   A CG  1 
ATOM   1709 C  CG  C ASP   A 1 216 ? -18.489 -3.533  -22.623 0.28 40.98  ? 216 ASP   A CG  1 
ATOM   1710 C  CG  D ASP   A 1 216 ? -19.883 -2.696  -23.411 0.22 39.10  ? 216 ASP   A CG  1 
ATOM   1711 O  OD1 A ASP   A 1 216 ? -19.206 -3.185  -21.662 0.28 41.92  ? 216 ASP   A OD1 1 
ATOM   1712 O  OD1 B ASP   A 1 216 ? -21.089 -2.534  -23.710 0.22 37.94  ? 216 ASP   A OD1 1 
ATOM   1713 O  OD1 C ASP   A 1 216 ? -19.206 -3.185  -21.662 0.28 41.92  ? 216 ASP   A OD1 1 
ATOM   1714 O  OD1 D ASP   A 1 216 ? -21.089 -2.534  -23.710 0.22 37.94  ? 216 ASP   A OD1 1 
ATOM   1715 O  OD2 A ASP   A 1 216 ? -17.288 -3.193  -22.749 0.28 38.22  ? 216 ASP   A OD2 1 
ATOM   1716 O  OD2 B ASP   A 1 216 ? -19.074 -1.760  -23.205 0.22 38.16  ? 216 ASP   A OD2 1 
ATOM   1717 O  OD2 C ASP   A 1 216 ? -17.288 -3.193  -22.749 0.28 38.22  ? 216 ASP   A OD2 1 
ATOM   1718 O  OD2 D ASP   A 1 216 ? -19.074 -1.760  -23.205 0.22 38.16  ? 216 ASP   A OD2 1 
ATOM   1719 N  N   . ARG   A 1 217 ? -22.045 -5.350  -25.134 1.00 38.83  ? 217 ARG   A N   1 
ATOM   1720 C  CA  . ARG   A 1 217 ? -22.616 -5.872  -26.383 1.00 37.75  ? 217 ARG   A CA  1 
ATOM   1721 C  C   . ARG   A 1 217 ? -23.003 -4.794  -27.390 1.00 35.01  ? 217 ARG   A C   1 
ATOM   1722 O  O   . ARG   A 1 217 ? -23.446 -5.115  -28.512 1.00 33.14  ? 217 ARG   A O   1 
ATOM   1723 C  CB  . ARG   A 1 217 ? -23.850 -6.740  -26.123 1.00 42.60  ? 217 ARG   A CB  1 
ATOM   1724 C  CG  . ARG   A 1 217 ? -23.475 -8.008  -25.373 1.00 43.85  ? 217 ARG   A CG  1 
ATOM   1725 C  CD  . ARG   A 1 217 ? -24.552 -9.043  -25.376 1.00 44.78  ? 217 ARG   A CD  1 
ATOM   1726 N  NE  . ARG   A 1 217 ? -25.037 -9.337  -26.734 1.00 49.55  ? 217 ARG   A NE  1 
ATOM   1727 C  CZ  . ARG   A 1 217 ? -24.899 -10.486 -27.410 1.00 48.99  ? 217 ARG   A CZ  1 
ATOM   1728 N  NH1 . ARG   A 1 217 ? -24.203 -11.490 -26.902 1.00 46.35  ? 217 ARG   A NH1 1 
ATOM   1729 N  NH2 . ARG   A 1 217 ? -25.465 -10.633 -28.600 1.00 52.87  ? 217 ARG   A NH2 1 
ATOM   1730 N  N   . TRP   A 1 218 ? -22.789 -3.525  -27.031 1.00 30.20  ? 218 TRP   A N   1 
ATOM   1731 C  CA  . TRP   A 1 218 ? -23.391 -2.436  -27.776 1.00 27.56  ? 218 TRP   A CA  1 
ATOM   1732 C  C   . TRP   A 1 218 ? -22.916 -2.355  -29.231 1.00 28.75  ? 218 TRP   A C   1 
ATOM   1733 O  O   . TRP   A 1 218 ? -23.626 -1.784  -30.061 1.00 29.36  ? 218 TRP   A O   1 
ATOM   1734 C  CB  . TRP   A 1 218 ? -23.182 -1.107  -27.037 1.00 29.50  ? 218 TRP   A CB  1 
ATOM   1735 C  CG  . TRP   A 1 218 ? -21.773 -0.571  -26.979 1.00 31.14  ? 218 TRP   A CG  1 
ATOM   1736 C  CD1 . TRP   A 1 218 ? -20.962 -0.584  -25.879 1.00 32.22  ? 218 TRP   A CD1 1 
ATOM   1737 C  CD2 . TRP   A 1 218 ? -21.030 0.139   -27.999 1.00 31.47  ? 218 TRP   A CD2 1 
ATOM   1738 N  NE1 . TRP   A 1 218 ? -19.779 0.060   -26.136 1.00 30.73  ? 218 TRP   A NE1 1 
ATOM   1739 C  CE2 . TRP   A 1 218 ? -19.781 0.502   -27.429 1.00 32.28  ? 218 TRP   A CE2 1 
ATOM   1740 C  CE3 . TRP   A 1 218 ? -21.273 0.492   -29.331 1.00 33.23  ? 218 TRP   A CE3 1 
ATOM   1741 C  CZ2 . TRP   A 1 218 ? -18.804 1.193   -28.142 1.00 31.37  ? 218 TRP   A CZ2 1 
ATOM   1742 C  CZ3 . TRP   A 1 218 ? -20.319 1.206   -30.025 1.00 33.77  ? 218 TRP   A CZ3 1 
ATOM   1743 C  CH2 . TRP   A 1 218 ? -19.091 1.528   -29.443 1.00 31.91  ? 218 TRP   A CH2 1 
ATOM   1744 N  N   . PHE   A 1 219 ? -21.729 -2.896  -29.558 1.00 25.56  ? 219 PHE   A N   1 
ATOM   1745 C  CA  . PHE   A 1 219 ? -21.106 -2.646  -30.845 1.00 26.42  ? 219 PHE   A CA  1 
ATOM   1746 C  C   . PHE   A 1 219 ? -21.393 -3.789  -31.821 1.00 28.45  ? 219 PHE   A C   1 
ATOM   1747 O  O   . PHE   A 1 219 ? -20.982 -3.723  -32.978 1.00 32.87  ? 219 PHE   A O   1 
ATOM   1748 C  CB  . PHE   A 1 219 ? -19.588 -2.414  -30.683 1.00 27.81  ? 219 PHE   A CB  1 
ATOM   1749 C  CG  . PHE   A 1 219 ? -18.921 -3.429  -29.766 1.00 27.24  ? 219 PHE   A CG  1 
ATOM   1750 C  CD1 . PHE   A 1 219 ? -18.592 -4.696  -30.227 1.00 27.37  ? 219 PHE   A CD1 1 
ATOM   1751 C  CD2 . PHE   A 1 219 ? -18.693 -3.132  -28.428 1.00 28.22  ? 219 PHE   A CD2 1 
ATOM   1752 C  CE1 . PHE   A 1 219 ? -18.059 -5.650  -29.371 1.00 29.23  ? 219 PHE   A CE1 1 
ATOM   1753 C  CE2 . PHE   A 1 219 ? -18.142 -4.080  -27.581 1.00 29.01  ? 219 PHE   A CE2 1 
ATOM   1754 C  CZ  . PHE   A 1 219 ? -17.828 -5.335  -28.049 1.00 30.56  ? 219 PHE   A CZ  1 
ATOM   1755 N  N   . LEU   A 1 220 ? -22.058 -4.858  -31.387 1.00 30.72  ? 220 LEU   A N   1 
ATOM   1756 C  CA  . LEU   A 1 220 ? -22.376 -5.953  -32.295 1.00 32.22  ? 220 LEU   A CA  1 
ATOM   1757 C  C   . LEU   A 1 220 ? -23.412 -5.506  -33.321 1.00 33.44  ? 220 LEU   A C   1 
ATOM   1758 O  O   . LEU   A 1 220 ? -24.001 -4.436  -33.179 1.00 33.94  ? 220 LEU   A O   1 
ATOM   1759 C  CB  . LEU   A 1 220 ? -22.897 -7.146  -31.506 1.00 36.72  ? 220 LEU   A CB  1 
ATOM   1760 C  CG  . LEU   A 1 220 ? -21.943 -7.764  -30.482 1.00 39.77  ? 220 LEU   A CG  1 
ATOM   1761 C  CD1 . LEU   A 1 220 ? -22.625 -8.995  -29.921 1.00 41.79  ? 220 LEU   A CD1 1 
ATOM   1762 C  CD2 . LEU   A 1 220 ? -20.597 -8.104  -31.101 1.00 38.46  ? 220 LEU   A CD2 1 
ATOM   1763 N  N   . ASN   A 1 221 ? -23.640 -6.331  -34.351 1.00 32.02  ? 221 ASN   A N   1 
ATOM   1764 C  CA  . ASN   A 1 221 ? -24.624 -6.005  -35.373 1.00 32.51  ? 221 ASN   A CA  1 
ATOM   1765 C  C   . ASN   A 1 221 ? -25.115 -7.275  -36.043 1.00 32.74  ? 221 ASN   A C   1 
ATOM   1766 O  O   . ASN   A 1 221 ? -24.548 -8.346  -35.854 1.00 34.72  ? 221 ASN   A O   1 
ATOM   1767 C  CB  . ASN   A 1 221 ? -24.099 -5.015  -36.409 1.00 34.14  ? 221 ASN   A CB  1 
ATOM   1768 C  CG  . ASN   A 1 221 ? -23.065 -5.585  -37.366 1.00 37.55  ? 221 ASN   A CG  1 
ATOM   1769 O  OD1 . ASN   A 1 221 ? -22.924 -6.803  -37.558 1.00 36.60  ? 221 ASN   A OD1 1 
ATOM   1770 N  ND2 . ASN   A 1 221 ? -22.344 -4.697  -38.025 1.00 36.84  ? 221 ASN   A ND2 1 
ATOM   1771 N  N   . ARG   A 1 222 ? -26.147 -7.125  -36.880 1.00 38.38  ? 222 ARG   A N   1 
ATOM   1772 C  CA  . ARG   A 1 222 ? -26.811 -8.276  -37.462 1.00 40.79  ? 222 ARG   A CA  1 
ATOM   1773 C  C   . ARG   A 1 222 ? -26.140 -8.720  -38.759 1.00 35.97  ? 222 ARG   A C   1 
ATOM   1774 O  O   . ARG   A 1 222 ? -26.619 -9.658  -39.377 1.00 35.57  ? 222 ARG   A O   1 
ATOM   1775 C  CB  . ARG   A 1 222 ? -28.293 -7.956  -37.690 1.00 49.68  ? 222 ARG   A CB  1 
ATOM   1776 C  CG  . ARG   A 1 222 ? -28.590 -6.877  -38.726 1.00 58.56  ? 222 ARG   A CG  1 
ATOM   1777 C  CD  . ARG   A 1 222 ? -30.074 -6.895  -39.136 1.00 64.39  ? 222 ARG   A CD  1 
ATOM   1778 N  NE  . ARG   A 1 222 ? -30.389 -6.030  -40.278 1.00 65.15  ? 222 ARG   A NE  1 
ATOM   1779 C  CZ  . ARG   A 1 222 ? -30.135 -6.295  -41.563 1.00 73.60  ? 222 ARG   A CZ  1 
ATOM   1780 N  NH1 . ARG   A 1 222 ? -29.607 -7.454  -41.927 1.00 76.95  ? 222 ARG   A NH1 1 
ATOM   1781 N  NH2 . ARG   A 1 222 ? -30.426 -5.402  -42.501 1.00 70.14  ? 222 ARG   A NH2 1 
ATOM   1782 N  N   . PHE   A 1 223 ? -25.039 -8.077  -39.172 1.00 35.73  ? 223 PHE   A N   1 
ATOM   1783 C  CA  . PHE   A 1 223 ? -24.366 -8.419  -40.420 1.00 36.38  ? 223 PHE   A CA  1 
ATOM   1784 C  C   . PHE   A 1 223 ? -23.206 -9.399  -40.242 1.00 34.54  ? 223 PHE   A C   1 
ATOM   1785 O  O   . PHE   A 1 223 ? -22.731 -9.608  -39.131 1.00 30.50  ? 223 PHE   A O   1 
ATOM   1786 C  CB  . PHE   A 1 223 ? -23.818 -7.136  -41.047 1.00 39.74  ? 223 PHE   A CB  1 
ATOM   1787 C  CG  . PHE   A 1 223 ? -24.932 -6.199  -41.468 1.00 43.93  ? 223 PHE   A CG  1 
ATOM   1788 C  CD1 . PHE   A 1 223 ? -25.770 -6.538  -42.524 1.00 46.58  ? 223 PHE   A CD1 1 
ATOM   1789 C  CD2 . PHE   A 1 223 ? -25.136 -4.990  -40.813 1.00 49.99  ? 223 PHE   A CD2 1 
ATOM   1790 C  CE1 . PHE   A 1 223 ? -26.791 -5.685  -42.913 1.00 54.66  ? 223 PHE   A CE1 1 
ATOM   1791 C  CE2 . PHE   A 1 223 ? -26.160 -4.138  -41.206 1.00 54.12  ? 223 PHE   A CE2 1 
ATOM   1792 C  CZ  . PHE   A 1 223 ? -26.982 -4.484  -42.260 1.00 53.76  ? 223 PHE   A CZ  1 
ATOM   1793 N  N   . THR   A 1 224 ? -22.752 -9.952  -41.382 1.00 34.04  ? 224 THR   A N   1 
ATOM   1794 C  CA  . THR   A 1 224 ? -21.508 -10.700 -41.518 1.00 35.05  ? 224 THR   A CA  1 
ATOM   1795 C  C   . THR   A 1 224 ? -20.746 -10.172 -42.743 1.00 32.02  ? 224 THR   A C   1 
ATOM   1796 O  O   . THR   A 1 224 ? -21.168 -9.192  -43.355 1.00 30.93  ? 224 THR   A O   1 
ATOM   1797 C  CB  . THR   A 1 224 ? -21.808 -12.197 -41.611 1.00 37.38  ? 224 THR   A CB  1 
ATOM   1798 O  OG1 . THR   A 1 224 ? -20.516 -12.793 -41.520 1.00 37.65  ? 224 THR   A OG1 1 
ATOM   1799 C  CG2 . THR   A 1 224 ? -22.494 -12.598 -42.908 1.00 37.01  ? 224 THR   A CG2 1 
ATOM   1800 N  N   . THR   A 1 225 ? -19.598 -10.788 -43.078 1.00 31.84  ? 225 THR   A N   1 
ATOM   1801 C  CA  . THR   A 1 225 ? -18.770 -10.337 -44.192 1.00 28.61  ? 225 THR   A CA  1 
ATOM   1802 C  C   . THR   A 1 225 ? -17.964 -11.515 -44.718 1.00 25.13  ? 225 THR   A C   1 
ATOM   1803 O  O   . THR   A 1 225 ? -17.752 -12.457 -43.989 1.00 29.13  ? 225 THR   A O   1 
ATOM   1804 C  CB  . THR   A 1 225 ? -17.853 -9.184  -43.775 1.00 29.66  ? 225 THR   A CB  1 
ATOM   1805 O  OG1 . THR   A 1 225 ? -17.126 -8.793  -44.941 1.00 28.81  ? 225 THR   A OG1 1 
ATOM   1806 C  CG2 . THR   A 1 225 ? -16.843 -9.562  -42.702 1.00 29.90  ? 225 THR   A CG2 1 
ATOM   1807 N  N   . THR   A 1 226 ? -17.536 -11.477 -45.986 1.00 24.84  ? 226 THR   A N   1 
ATOM   1808 C  CA  . THR   A 1 226 ? -16.505 -12.401 -46.452 1.00 27.34  ? 226 THR   A CA  1 
ATOM   1809 C  C   . THR   A 1 226 ? -15.139 -11.911 -45.958 1.00 25.74  ? 226 THR   A C   1 
ATOM   1810 O  O   . THR   A 1 226 ? -14.922 -10.711 -45.727 1.00 24.18  ? 226 THR   A O   1 
ATOM   1811 C  CB  . THR   A 1 226 ? -16.498 -12.586 -47.976 1.00 29.00  ? 226 THR   A CB  1 
ATOM   1812 O  OG1 . THR   A 1 226 ? -16.188 -11.319 -48.560 1.00 26.79  ? 226 THR   A OG1 1 
ATOM   1813 C  CG2 . THR   A 1 226 ? -17.802 -13.180 -48.496 1.00 27.66  ? 226 THR   A CG2 1 
ATOM   1814 N  N   . LEU   A 1 227 ? -14.221 -12.870 -45.827 1.00 27.94  ? 227 LEU   A N   1 
ATOM   1815 C  CA  . LEU   A 1 227 ? -12.859 -12.592 -45.414 1.00 28.35  ? 227 LEU   A CA  1 
ATOM   1816 C  C   . LEU   A 1 227 ? -12.215 -11.612 -46.386 1.00 29.30  ? 227 LEU   A C   1 
ATOM   1817 O  O   . LEU   A 1 227 ? -11.480 -10.718 -45.962 1.00 28.99  ? 227 LEU   A O   1 
ATOM   1818 C  CB  . LEU   A 1 227 ? -12.052 -13.887 -45.304 1.00 31.34  ? 227 LEU   A CB  1 
ATOM   1819 C  CG  . LEU   A 1 227 ? -10.599 -13.733 -44.830 1.00 30.65  ? 227 LEU   A CG  1 
ATOM   1820 C  CD1 . LEU   A 1 227 ? -10.497 -12.883 -43.563 1.00 30.40  ? 227 LEU   A CD1 1 
ATOM   1821 C  CD2 . LEU   A 1 227 ? -9.960  -15.091 -44.606 1.00 30.62  ? 227 LEU   A CD2 1 
ATOM   1822 N  N   . ASN   A 1 228 ? -12.477 -11.791 -47.690 1.00 27.95  ? 228 ASN   A N   1 
ATOM   1823 C  CA  . ASN   A 1 228 ? -11.875 -10.920 -48.695 1.00 29.89  ? 228 ASN   A CA  1 
ATOM   1824 C  C   . ASN   A 1 228 ? -12.407 -9.479  -48.609 1.00 27.59  ? 228 ASN   A C   1 
ATOM   1825 O  O   . ASN   A 1 228 ? -11.641 -8.514  -48.695 1.00 26.03  ? 228 ASN   A O   1 
ATOM   1826 C  CB  . ASN   A 1 228 ? -12.101 -11.445 -50.106 1.00 33.34  ? 228 ASN   A CB  1 
ATOM   1827 C  CG  . ASN   A 1 228 ? -11.184 -10.752 -51.083 1.00 42.55  ? 228 ASN   A CG  1 
ATOM   1828 O  OD1 . ASN   A 1 228 ? -11.644 -10.036 -51.982 1.00 46.91  ? 228 ASN   A OD1 1 
ATOM   1829 N  ND2 . ASN   A 1 228 ? -9.879  -10.910 -50.893 1.00 44.79  ? 228 ASN   A ND2 1 
ATOM   1830 N  N   . ASP   A 1 229 ? -13.735 -9.312  -48.498 1.00 26.74  ? 229 ASP   A N   1 
ATOM   1831 C  CA  . ASP   A 1 229 ? -14.322 -7.979  -48.421 1.00 25.07  ? 229 ASP   A CA  1 
ATOM   1832 C  C   . ASP   A 1 229 ? -13.854 -7.251  -47.148 1.00 23.51  ? 229 ASP   A C   1 
ATOM   1833 O  O   . ASP   A 1 229 ? -13.688 -6.035  -47.145 1.00 22.85  ? 229 ASP   A O   1 
ATOM   1834 C  CB  . ASP   A 1 229 ? -15.843 -8.057  -48.532 1.00 26.24  ? 229 ASP   A CB  1 
ATOM   1835 C  CG  . ASP   A 1 229 ? -16.430 -8.317  -49.918 1.00 28.31  ? 229 ASP   A CG  1 
ATOM   1836 O  OD1 . ASP   A 1 229 ? -15.675 -8.204  -50.901 1.00 26.75  ? 229 ASP   A OD1 1 
ATOM   1837 O  OD2 . ASP   A 1 229 ? -17.657 -8.610  -49.994 1.00 26.62  ? 229 ASP   A OD2 1 
ATOM   1838 N  N   . PHE   A 1 230 ? -13.698 -7.986  -46.045 1.00 25.40  ? 230 PHE   A N   1 
ATOM   1839 C  CA  . PHE   A 1 230 ? -13.145 -7.437  -44.816 1.00 25.98  ? 230 PHE   A CA  1 
ATOM   1840 C  C   . PHE   A 1 230 ? -11.763 -6.831  -45.070 1.00 26.05  ? 230 PHE   A C   1 
ATOM   1841 O  O   . PHE   A 1 230 ? -11.505 -5.691  -44.675 1.00 26.98  ? 230 PHE   A O   1 
ATOM   1842 C  CB  . PHE   A 1 230 ? -13.089 -8.489  -43.696 1.00 27.64  ? 230 PHE   A CB  1 
ATOM   1843 C  CG  . PHE   A 1 230 ? -12.417 -7.905  -42.465 1.00 29.48  ? 230 PHE   A CG  1 
ATOM   1844 C  CD1 . PHE   A 1 230 ? -13.069 -6.945  -41.700 1.00 29.82  ? 230 PHE   A CD1 1 
ATOM   1845 C  CD2 . PHE   A 1 230 ? -11.112 -8.251  -42.135 1.00 29.77  ? 230 PHE   A CD2 1 
ATOM   1846 C  CE1 . PHE   A 1 230 ? -12.446 -6.374  -40.606 1.00 30.91  ? 230 PHE   A CE1 1 
ATOM   1847 C  CE2 . PHE   A 1 230 ? -10.474 -7.650  -41.069 1.00 30.96  ? 230 PHE   A CE2 1 
ATOM   1848 C  CZ  . PHE   A 1 230 ? -11.133 -6.703  -40.313 1.00 33.40  ? 230 PHE   A CZ  1 
ATOM   1849 N  N   . ASN   A 1 231 ? -10.878 -7.577  -45.746 1.00 26.69  ? 231 ASN   A N   1 
ATOM   1850 C  CA  . ASN   A 1 231 ? -9.501  -7.122  -45.948 1.00 26.73  ? 231 ASN   A CA  1 
ATOM   1851 C  C   . ASN   A 1 231 ? -9.449  -5.893  -46.854 1.00 27.00  ? 231 ASN   A C   1 
ATOM   1852 O  O   . ASN   A 1 231 ? -8.664  -4.990  -46.585 1.00 25.83  ? 231 ASN   A O   1 
ATOM   1853 C  CB  . ASN   A 1 231 ? -8.561  -8.247  -46.381 1.00 27.60  ? 231 ASN   A CB  1 
ATOM   1854 C  CG  . ASN   A 1 231 ? -8.188  -9.128  -45.207 1.00 29.91  ? 231 ASN   A CG  1 
ATOM   1855 O  OD1 . ASN   A 1 231 ? -8.120  -8.651  -44.069 1.00 31.48  ? 231 ASN   A OD1 1 
ATOM   1856 N  ND2 . ASN   A 1 231 ? -7.998  -10.418 -45.425 1.00 28.44  ? 231 ASN   A ND2 1 
ATOM   1857 N  N   . LEU   A 1 232 ? -10.313 -5.831  -47.883 1.00 26.17  ? 232 LEU   A N   1 
ATOM   1858 C  CA  . LEU   A 1 232 ? -10.363 -4.690  -48.791 1.00 24.92  ? 232 LEU   A CA  1 
ATOM   1859 C  C   . LEU   A 1 232 ? -10.794 -3.425  -48.052 1.00 26.94  ? 232 LEU   A C   1 
ATOM   1860 O  O   . LEU   A 1 232 ? -10.294 -2.343  -48.344 1.00 27.80  ? 232 LEU   A O   1 
ATOM   1861 C  CB  . LEU   A 1 232 ? -11.309 -4.967  -49.958 1.00 27.66  ? 232 LEU   A CB  1 
ATOM   1862 C  CG  . LEU   A 1 232 ? -10.843 -5.989  -51.004 1.00 28.64  ? 232 LEU   A CG  1 
ATOM   1863 C  CD1 . LEU   A 1 232 ? -12.000 -6.285  -51.947 1.00 30.00  ? 232 LEU   A CD1 1 
ATOM   1864 C  CD2 . LEU   A 1 232 ? -9.615  -5.511  -51.794 1.00 27.13  ? 232 LEU   A CD2 1 
ATOM   1865 N  N   . VAL   A 1 233 ? -11.733 -3.547  -47.102 1.00 27.48  ? 233 VAL   A N   1 
ATOM   1866 C  CA  . VAL   A 1 233 ? -12.138 -2.415  -46.266 1.00 29.54  ? 233 VAL   A CA  1 
ATOM   1867 C  C   . VAL   A 1 233 ? -11.038 -2.049  -45.255 1.00 26.00  ? 233 VAL   A C   1 
ATOM   1868 O  O   . VAL   A 1 233 ? -10.687 -0.874  -45.112 1.00 25.99  ? 233 VAL   A O   1 
ATOM   1869 C  CB  . VAL   A 1 233 ? -13.458 -2.701  -45.522 1.00 28.89  ? 233 VAL   A CB  1 
ATOM   1870 C  CG1 . VAL   A 1 233 ? -13.784 -1.614  -44.505 1.00 28.73  ? 233 VAL   A CG1 1 
ATOM   1871 C  CG2 . VAL   A 1 233 ? -14.610 -2.887  -46.506 1.00 30.85  ? 233 VAL   A CG2 1 
ATOM   1872 N  N   . ALA   A 1 234 ? -10.532 -3.041  -44.525 1.00 26.44  ? 234 ALA   A N   1 
ATOM   1873 C  CA  . ALA   A 1 234 ? -9.690  -2.757  -43.369 1.00 29.81  ? 234 ALA   A CA  1 
ATOM   1874 C  C   . ALA   A 1 234 ? -8.358  -2.139  -43.806 1.00 31.57  ? 234 ALA   A C   1 
ATOM   1875 O  O   . ALA   A 1 234 ? -7.786  -1.316  -43.097 1.00 34.35  ? 234 ALA   A O   1 
ATOM   1876 C  CB  . ALA   A 1 234 ? -9.480  -4.008  -42.546 1.00 30.27  ? 234 ALA   A CB  1 
ATOM   1877 N  N   . MET   A 1 235 ? -7.868  -2.494  -44.993 1.00 31.42  ? 235 MET   A N   1 
ATOM   1878 C  CA  . MET   A 1 235 ? -6.600  -1.954  -45.446 1.00 33.41  ? 235 MET   A CA  1 
ATOM   1879 C  C   . MET   A 1 235 ? -6.706  -0.461  -45.746 1.00 31.43  ? 235 MET   A C   1 
ATOM   1880 O  O   . MET   A 1 235 ? -5.694  0.232   -45.797 1.00 29.03  ? 235 MET   A O   1 
ATOM   1881 C  CB  . MET   A 1 235 ? -6.084  -2.752  -46.642 1.00 41.37  ? 235 MET   A CB  1 
ATOM   1882 C  CG  . MET   A 1 235 ? -5.700  -4.165  -46.198 1.00 54.12  ? 235 MET   A CG  1 
ATOM   1883 S  SD  . MET   A 1 235 ? -4.919  -5.196  -47.452 1.00 66.28  ? 235 MET   A SD  1 
ATOM   1884 C  CE  . MET   A 1 235 ? -3.541  -4.108  -47.858 1.00 60.93  ? 235 MET   A CE  1 
ATOM   1885 N  N   . LYS   A 1 236 ? -7.920  0.057   -45.912 1.00 26.23  ? 236 LYS   A N   1 
ATOM   1886 C  CA  . LYS   A 1 236 ? -8.046  1.461   -46.236 1.00 28.02  ? 236 LYS   A CA  1 
ATOM   1887 C  C   . LYS   A 1 236 ? -7.874  2.299   -44.978 1.00 26.91  ? 236 LYS   A C   1 
ATOM   1888 O  O   . LYS   A 1 236 ? -7.810  3.524   -45.106 1.00 27.01  ? 236 LYS   A O   1 
ATOM   1889 C  CB  . LYS   A 1 236 ? -9.370  1.807   -46.925 1.00 29.93  ? 236 LYS   A CB  1 
ATOM   1890 C  CG  . LYS   A 1 236 ? -9.555  1.171   -48.298 1.00 31.40  ? 236 LYS   A CG  1 
ATOM   1891 C  CD  . LYS   A 1 236 ? -10.957 1.287   -48.892 1.00 32.61  ? 236 LYS   A CD  1 
ATOM   1892 C  CE  . LYS   A 1 236 ? -11.050 0.435   -50.134 1.00 34.89  ? 236 LYS   A CE  1 
ATOM   1893 N  NZ  . LYS   A 1 236 ? -12.384 0.487   -50.735 1.00 38.51  ? 236 LYS   A NZ  1 
ATOM   1894 N  N   . TYR   A 1 237 ? -7.863  1.640   -43.800 1.00 25.56  ? 237 TYR   A N   1 
ATOM   1895 C  CA  . TYR   A 1 237 ? -7.573  2.303   -42.530 1.00 27.44  ? 237 TYR   A CA  1 
ATOM   1896 C  C   . TYR   A 1 237 ? -6.205  1.901   -41.960 1.00 27.23  ? 237 TYR   A C   1 
ATOM   1897 O  O   . TYR   A 1 237 ? -5.985  2.056   -40.762 1.00 26.95  ? 237 TYR   A O   1 
ATOM   1898 C  CB  . TYR   A 1 237 ? -8.625  1.983   -41.464 1.00 25.50  ? 237 TYR   A CB  1 
ATOM   1899 C  CG  . TYR   A 1 237 ? -10.070 2.298   -41.841 1.00 26.29  ? 237 TYR   A CG  1 
ATOM   1900 C  CD1 . TYR   A 1 237 ? -10.869 1.395   -42.551 1.00 27.67  ? 237 TYR   A CD1 1 
ATOM   1901 C  CD2 . TYR   A 1 237 ? -10.643 3.509   -41.473 1.00 25.70  ? 237 TYR   A CD2 1 
ATOM   1902 C  CE1 . TYR   A 1 237 ? -12.195 1.688   -42.872 1.00 29.74  ? 237 TYR   A CE1 1 
ATOM   1903 C  CE2 . TYR   A 1 237 ? -11.958 3.818   -41.802 1.00 27.81  ? 237 TYR   A CE2 1 
ATOM   1904 C  CZ  . TYR   A 1 237 ? -12.744 2.914   -42.505 1.00 31.08  ? 237 TYR   A CZ  1 
ATOM   1905 O  OH  . TYR   A 1 237 ? -14.055 3.271   -42.773 1.00 30.38  ? 237 TYR   A OH  1 
ATOM   1906 N  N   . ASN   A 1 238 ? -5.294  1.391   -42.799 1.00 27.16  ? 238 ASN   A N   1 
ATOM   1907 C  CA  . ASN   A 1 238 ? -3.967  0.982   -42.352 1.00 30.02  ? 238 ASN   A CA  1 
ATOM   1908 C  C   . ASN   A 1 238 ? -4.004  -0.168  -41.335 1.00 29.77  ? 238 ASN   A C   1 
ATOM   1909 O  O   . ASN   A 1 238 ? -3.113  -0.267  -40.483 1.00 25.22  ? 238 ASN   A O   1 
ATOM   1910 C  CB  . ASN   A 1 238 ? -3.180  2.169   -41.800 1.00 32.69  ? 238 ASN   A CB  1 
ATOM   1911 C  CG  . ASN   A 1 238 ? -2.455  2.901   -42.898 1.00 36.68  ? 238 ASN   A CG  1 
ATOM   1912 O  OD1 . ASN   A 1 238 ? -2.126  2.305   -43.921 1.00 39.47  ? 238 ASN   A OD1 1 
ATOM   1913 N  ND2 . ASN   A 1 238 ? -2.194  4.182   -42.713 1.00 43.30  ? 238 ASN   A ND2 1 
ATOM   1914 N  N   . TYR   A 1 239 ? -4.990  -1.069  -41.468 1.00 25.29  ? 239 TYR   A N   1 
ATOM   1915 C  CA  . TYR   A 1 239 ? -5.020  -2.308  -40.705 1.00 24.50  ? 239 TYR   A CA  1 
ATOM   1916 C  C   . TYR   A 1 239 ? -4.263  -3.402  -41.453 1.00 25.44  ? 239 TYR   A C   1 
ATOM   1917 O  O   . TYR   A 1 239 ? -4.332  -3.462  -42.675 1.00 28.55  ? 239 TYR   A O   1 
ATOM   1918 C  CB  . TYR   A 1 239 ? -6.470  -2.733  -40.459 1.00 21.99  ? 239 TYR   A CB  1 
ATOM   1919 C  CG  . TYR   A 1 239 ? -7.055  -2.171  -39.180 1.00 21.54  ? 239 TYR   A CG  1 
ATOM   1920 C  CD1 . TYR   A 1 239 ? -7.176  -0.797  -38.977 1.00 22.27  ? 239 TYR   A CD1 1 
ATOM   1921 C  CD2 . TYR   A 1 239 ? -7.476  -3.019  -38.175 1.00 22.65  ? 239 TYR   A CD2 1 
ATOM   1922 C  CE1 . TYR   A 1 239 ? -7.693  -0.291  -37.797 1.00 24.07  ? 239 TYR   A CE1 1 
ATOM   1923 C  CE2 . TYR   A 1 239 ? -7.992  -2.525  -36.995 1.00 23.60  ? 239 TYR   A CE2 1 
ATOM   1924 C  CZ  . TYR   A 1 239 ? -8.101  -1.163  -36.805 1.00 22.67  ? 239 TYR   A CZ  1 
ATOM   1925 O  OH  . TYR   A 1 239 ? -8.614  -0.730  -35.616 1.00 25.38  ? 239 TYR   A OH  1 
ATOM   1926 N  N   . GLU   A 1 240 ? -3.584  -4.283  -40.708 1.00 26.46  ? 240 GLU   A N   1 
ATOM   1927 C  CA  . GLU   A 1 240 ? -2.917  -5.447  -41.278 1.00 28.85  ? 240 GLU   A CA  1 
ATOM   1928 C  C   . GLU   A 1 240 ? -3.942  -6.423  -41.860 1.00 29.43  ? 240 GLU   A C   1 
ATOM   1929 O  O   . GLU   A 1 240 ? -5.064  -6.506  -41.364 1.00 29.51  ? 240 GLU   A O   1 
ATOM   1930 C  CB  . GLU   A 1 240 ? -2.160  -6.266  -40.231 1.00 29.36  ? 240 GLU   A CB  1 
ATOM   1931 C  CG  . GLU   A 1 240 ? -0.848  -5.646  -39.790 1.00 33.45  ? 240 GLU   A CG  1 
ATOM   1932 C  CD  . GLU   A 1 240 ? 0.229   -5.816  -40.842 1.00 35.57  ? 240 GLU   A CD  1 
ATOM   1933 O  OE1 . GLU   A 1 240 ? 0.573   -6.989  -41.111 1.00 35.40  ? 240 GLU   A OE1 1 
ATOM   1934 O  OE2 . GLU   A 1 240 ? 0.691   -4.781  -41.388 1.00 36.07  ? 240 GLU   A OE2 1 
ATOM   1935 N  N   . PRO   A 1 241 ? -3.594  -7.175  -42.937 1.00 31.80  ? 241 PRO   A N   1 
ATOM   1936 C  CA  . PRO   A 1 241 ? -4.465  -8.229  -43.468 1.00 31.31  ? 241 PRO   A CA  1 
ATOM   1937 C  C   . PRO   A 1 241 ? -4.719  -9.325  -42.434 1.00 29.33  ? 241 PRO   A C   1 
ATOM   1938 O  O   . PRO   A 1 241 ? -3.817  -9.697  -41.695 1.00 27.62  ? 241 PRO   A O   1 
ATOM   1939 C  CB  . PRO   A 1 241 ? -3.694  -8.756  -44.688 1.00 34.13  ? 241 PRO   A CB  1 
ATOM   1940 C  CG  . PRO   A 1 241 ? -2.737  -7.635  -45.072 1.00 33.61  ? 241 PRO   A CG  1 
ATOM   1941 C  CD  . PRO   A 1 241 ? -2.376  -6.995  -43.749 1.00 33.40  ? 241 PRO   A CD  1 
ATOM   1942 N  N   . LEU   A 1 242 ? -5.979  -9.757  -42.325 1.00 27.26  ? 242 LEU   A N   1 
ATOM   1943 C  CA  . LEU   A 1 242 ? -6.360  -10.927 -41.540 1.00 27.07  ? 242 LEU   A CA  1 
ATOM   1944 C  C   . LEU   A 1 242 ? -6.219  -12.188 -42.401 1.00 27.58  ? 242 LEU   A C   1 
ATOM   1945 O  O   . LEU   A 1 242 ? -6.808  -12.262 -43.477 1.00 28.49  ? 242 LEU   A O   1 
ATOM   1946 C  CB  . LEU   A 1 242 ? -7.813  -10.721 -41.088 1.00 27.51  ? 242 LEU   A CB  1 
ATOM   1947 C  CG  . LEU   A 1 242 ? -8.336  -11.649 -39.985 1.00 26.66  ? 242 LEU   A CG  1 
ATOM   1948 C  CD1 . LEU   A 1 242 ? -7.694  -11.262 -38.669 1.00 28.22  ? 242 LEU   A CD1 1 
ATOM   1949 C  CD2 . LEU   A 1 242 ? -9.848  -11.656 -39.822 1.00 27.32  ? 242 LEU   A CD2 1 
ATOM   1950 N  N   . THR   A 1 243 ? -5.495  -13.199 -41.902 1.00 27.78  ? 243 THR   A N   1 
ATOM   1951 C  CA  . THR   A 1 243 ? -5.271  -14.445 -42.626 1.00 29.17  ? 243 THR   A CA  1 
ATOM   1952 C  C   . THR   A 1 243 ? -6.130  -15.577 -42.059 1.00 29.83  ? 243 THR   A C   1 
ATOM   1953 O  O   . THR   A 1 243 ? -6.747  -15.472 -41.003 1.00 27.02  ? 243 THR   A O   1 
ATOM   1954 C  CB  . THR   A 1 243 ? -3.800  -14.855 -42.569 1.00 27.66  ? 243 THR   A CB  1 
ATOM   1955 O  OG1 . THR   A 1 243 ? -3.520  -15.259 -41.219 1.00 26.60  ? 243 THR   A OG1 1 
ATOM   1956 C  CG2 . THR   A 1 243 ? -2.885  -13.752 -43.072 1.00 27.35  ? 243 THR   A CG2 1 
ATOM   1957 N  N   . GLN   A 1 244 ? -6.153  -16.697 -42.783 1.00 31.03  ? 244 GLN   A N   1 
ATOM   1958 C  CA  . GLN   A 1 244 ? -6.915  -17.841 -42.328 1.00 30.72  ? 244 GLN   A CA  1 
ATOM   1959 C  C   . GLN   A 1 244 ? -6.314  -18.344 -41.019 1.00 29.55  ? 244 GLN   A C   1 
ATOM   1960 O  O   . GLN   A 1 244 ? -7.036  -18.805 -40.130 1.00 31.76  ? 244 GLN   A O   1 
ATOM   1961 C  CB  . GLN   A 1 244 ? -6.970  -18.937 -43.390 1.00 32.52  ? 244 GLN   A CB  1 
ATOM   1962 C  CG  . GLN   A 1 244 ? -7.808  -20.140 -42.964 1.00 32.31  ? 244 GLN   A CG  1 
ATOM   1963 C  CD  . GLN   A 1 244 ? -9.241  -19.746 -42.691 1.00 33.43  ? 244 GLN   A CD  1 
ATOM   1964 O  OE1 . GLN   A 1 244 ? -9.868  -19.018 -43.466 1.00 38.90  ? 244 GLN   A OE1 1 
ATOM   1965 N  NE2 . GLN   A 1 244 ? -9.755  -20.153 -41.543 1.00 34.66  ? 244 GLN   A NE2 1 
ATOM   1966 N  N   . ASP   A 1 245 ? -4.988  -18.224 -40.886 1.00 29.79  ? 245 ASP   A N   1 
ATOM   1967 C  CA  . ASP   A 1 245 ? -4.321  -18.517 -39.625 1.00 29.95  ? 245 ASP   A CA  1 
ATOM   1968 C  C   . ASP   A 1 245 ? -4.982  -17.773 -38.462 1.00 29.17  ? 245 ASP   A C   1 
ATOM   1969 O  O   . ASP   A 1 245 ? -5.310  -18.375 -37.430 1.00 28.85  ? 245 ASP   A O   1 
ATOM   1970 C  CB  . ASP   A 1 245 ? -2.839  -18.180 -39.682 1.00 32.51  ? 245 ASP   A CB  1 
ATOM   1971 C  CG  . ASP   A 1 245 ? -1.923  -19.338 -40.055 1.00 36.11  ? 245 ASP   A CG  1 
ATOM   1972 O  OD1 . ASP   A 1 245 ? -2.419  -20.363 -40.548 1.00 33.97  ? 245 ASP   A OD1 1 
ATOM   1973 O  OD2 . ASP   A 1 245 ? -0.713  -19.221 -39.807 1.00 37.62  ? 245 ASP   A OD2 1 
ATOM   1974 N  N   . HIS   A 1 246 ? -5.127  -16.452 -38.622 1.00 26.44  ? 246 HIS   A N   1 
ATOM   1975 C  CA  . HIS   A 1 246 ? -5.699  -15.596 -37.593 1.00 27.56  ? 246 HIS   A CA  1 
ATOM   1976 C  C   . HIS   A 1 246 ? -7.152  -16.009 -37.289 1.00 27.24  ? 246 HIS   A C   1 
ATOM   1977 O  O   . HIS   A 1 246 ? -7.568  -16.062 -36.128 1.00 28.13  ? 246 HIS   A O   1 
ATOM   1978 C  CB  . HIS   A 1 246 ? -5.615  -14.130 -38.035 1.00 26.47  ? 246 HIS   A CB  1 
ATOM   1979 C  CG  . HIS   A 1 246 ? -4.237  -13.588 -38.270 1.00 27.01  ? 246 HIS   A CG  1 
ATOM   1980 N  ND1 . HIS   A 1 246 ? -4.022  -12.591 -39.200 1.00 25.11  ? 246 HIS   A ND1 1 
ATOM   1981 C  CD2 . HIS   A 1 246 ? -3.042  -13.811 -37.690 1.00 24.68  ? 246 HIS   A CD2 1 
ATOM   1982 C  CE1 . HIS   A 1 246 ? -2.741  -12.274 -39.205 1.00 24.89  ? 246 HIS   A CE1 1 
ATOM   1983 N  NE2 . HIS   A 1 246 ? -2.135  -12.980 -38.284 1.00 22.72  ? 246 HIS   A NE2 1 
ATOM   1984 N  N   . VAL   A 1 247 ? -7.917  -16.319 -38.336 1.00 27.43  ? 247 VAL   A N   1 
ATOM   1985 C  CA  . VAL   A 1 247 ? -9.274  -16.816 -38.161 1.00 30.85  ? 247 VAL   A CA  1 
ATOM   1986 C  C   . VAL   A 1 247 ? -9.268  -18.077 -37.292 1.00 32.95  ? 247 VAL   A C   1 
ATOM   1987 O  O   . VAL   A 1 247 ? -10.047 -18.152 -36.345 1.00 30.08  ? 247 VAL   A O   1 
ATOM   1988 C  CB  . VAL   A 1 247 ? -9.989  -17.038 -39.509 1.00 32.19  ? 247 VAL   A CB  1 
ATOM   1989 C  CG1 . VAL   A 1 247 ? -11.374 -17.657 -39.337 1.00 34.27  ? 247 VAL   A CG1 1 
ATOM   1990 C  CG2 . VAL   A 1 247 ? -10.135 -15.738 -40.283 1.00 32.18  ? 247 VAL   A CG2 1 
ATOM   1991 N  N   . ASP   A 1 248 ? -8.367  -19.039 -37.574 1.00 33.18  ? 248 ASP   A N   1 
ATOM   1992 C  CA  . ASP   A 1 248 ? -8.295  -20.277 -36.803 1.00 31.78  ? 248 ASP   A CA  1 
ATOM   1993 C  C   . ASP   A 1 248 ? -7.993  -19.977 -35.332 1.00 36.12  ? 248 ASP   A C   1 
ATOM   1994 O  O   . ASP   A 1 248 ? -8.621  -20.545 -34.432 1.00 33.89  ? 248 ASP   A O   1 
ATOM   1995 C  CB  . ASP   A 1 248 ? -7.271  -21.262 -37.367 1.00 32.44  ? 248 ASP   A CB  1 
ATOM   1996 C  CG  . ASP   A 1 248 ? -7.560  -21.867 -38.743 1.00 29.83  ? 248 ASP   A CG  1 
ATOM   1997 O  OD1 . ASP   A 1 248 ? -8.675  -21.661 -39.284 1.00 29.28  ? 248 ASP   A OD1 1 
ATOM   1998 O  OD2 . ASP   A 1 248 ? -6.653  -22.524 -39.298 1.00 28.15  ? 248 ASP   A OD2 1 
ATOM   1999 N  N   . ILE   A 1 249 ? -7.031  -19.070 -35.102 1.00 33.46  ? 249 ILE   A N   1 
ATOM   2000 C  CA  . ILE   A 1 249 ? -6.569  -18.713 -33.768 1.00 35.65  ? 249 ILE   A CA  1 
ATOM   2001 C  C   . ILE   A 1 249 ? -7.707  -18.142 -32.900 1.00 33.16  ? 249 ILE   A C   1 
ATOM   2002 O  O   . ILE   A 1 249 ? -7.687  -18.302 -31.681 1.00 27.01  ? 249 ILE   A O   1 
ATOM   2003 C  CB  . ILE   A 1 249 ? -5.353  -17.764 -33.894 1.00 41.95  ? 249 ILE   A CB  1 
ATOM   2004 C  CG1 . ILE   A 1 249 ? -4.072  -18.532 -34.314 1.00 46.11  ? 249 ILE   A CG1 1 
ATOM   2005 C  CG2 . ILE   A 1 249 ? -5.105  -16.967 -32.622 1.00 40.10  ? 249 ILE   A CG2 1 
ATOM   2006 C  CD1 . ILE   A 1 249 ? -2.937  -17.656 -34.836 1.00 47.28  ? 249 ILE   A CD1 1 
ATOM   2007 N  N   . LEU   A 1 250 ? -8.714  -17.487 -33.496 1.00 32.57  ? 250 LEU   A N   1 
ATOM   2008 C  CA  . LEU   A 1 250 ? -9.810  -16.906 -32.724 1.00 29.40  ? 250 LEU   A CA  1 
ATOM   2009 C  C   . LEU   A 1 250 ? -10.938 -17.913 -32.475 1.00 29.44  ? 250 LEU   A C   1 
ATOM   2010 O  O   . LEU   A 1 250 ? -11.908 -17.564 -31.810 1.00 29.11  ? 250 LEU   A O   1 
ATOM   2011 C  CB  . LEU   A 1 250 ? -10.330 -15.665 -33.444 1.00 27.13  ? 250 LEU   A CB  1 
ATOM   2012 C  CG  . LEU   A 1 250 ? -9.379  -14.467 -33.497 1.00 30.29  ? 250 LEU   A CG  1 
ATOM   2013 C  CD1 . LEU   A 1 250 ? -9.706  -13.577 -34.694 1.00 31.83  ? 250 LEU   A CD1 1 
ATOM   2014 C  CD2 . LEU   A 1 250 ? -9.403  -13.624 -32.219 1.00 31.97  ? 250 LEU   A CD2 1 
ATOM   2015 N  N   . GLY   A 1 251 ? -10.801 -19.155 -32.979 1.00 33.08  ? 251 GLY   A N   1 
ATOM   2016 C  CA  . GLY   A 1 251 ? -11.786 -20.223 -32.830 1.00 31.49  ? 251 GLY   A CA  1 
ATOM   2017 C  C   . GLY   A 1 251 ? -12.298 -20.391 -31.397 1.00 32.79  ? 251 GLY   A C   1 
ATOM   2018 O  O   . GLY   A 1 251 ? -13.501 -20.341 -31.144 1.00 33.44  ? 251 GLY   A O   1 
ATOM   2019 N  N   . PRO   A 1 252 ? -11.417 -20.626 -30.404 1.00 32.79  ? 252 PRO   A N   1 
ATOM   2020 C  CA  . PRO   A 1 252 ? -11.851 -20.719 -29.002 1.00 31.15  ? 252 PRO   A CA  1 
ATOM   2021 C  C   . PRO   A 1 252 ? -12.658 -19.546 -28.437 1.00 33.48  ? 252 PRO   A C   1 
ATOM   2022 O  O   . PRO   A 1 252 ? -13.670 -19.761 -27.780 1.00 32.61  ? 252 PRO   A O   1 
ATOM   2023 C  CB  . PRO   A 1 252 ? -10.525 -20.919 -28.262 1.00 29.99  ? 252 PRO   A CB  1 
ATOM   2024 C  CG  . PRO   A 1 252 ? -9.644  -21.598 -29.279 1.00 30.88  ? 252 PRO   A CG  1 
ATOM   2025 C  CD  . PRO   A 1 252 ? -9.986  -20.912 -30.596 1.00 30.44  ? 252 PRO   A CD  1 
ATOM   2026 N  N   . LEU   A 1 253 ? -12.241 -18.299 -28.694 1.00 32.60  ? 253 LEU   A N   1 
ATOM   2027 C  CA  . LEU   A 1 253 ? -12.996 -17.155 -28.199 1.00 31.44  ? 253 LEU   A CA  1 
ATOM   2028 C  C   . LEU   A 1 253 ? -14.371 -17.100 -28.875 1.00 34.21  ? 253 LEU   A C   1 
ATOM   2029 O  O   . LEU   A 1 253 ? -15.364 -16.736 -28.244 1.00 36.17  ? 253 LEU   A O   1 
ATOM   2030 C  CB  . LEU   A 1 253 ? -12.201 -15.864 -28.395 1.00 28.51  ? 253 LEU   A CB  1 
ATOM   2031 C  CG  . LEU   A 1 253 ? -11.022 -15.651 -27.428 1.00 31.49  ? 253 LEU   A CG  1 
ATOM   2032 C  CD1 . LEU   A 1 253 ? -9.986  -14.690 -27.997 1.00 28.12  ? 253 LEU   A CD1 1 
ATOM   2033 C  CD2 . LEU   A 1 253 ? -11.473 -15.135 -26.053 1.00 30.95  ? 253 LEU   A CD2 1 
ATOM   2034 N  N   . SER   A 1 254 ? -14.406 -17.420 -30.173 1.00 35.68  ? 254 SER   A N   1 
ATOM   2035 C  CA  . SER   A 1 254 ? -15.641 -17.572 -30.929 1.00 37.14  ? 254 SER   A CA  1 
ATOM   2036 C  C   . SER   A 1 254 ? -16.605 -18.520 -30.207 1.00 36.13  ? 254 SER   A C   1 
ATOM   2037 O  O   . SER   A 1 254 ? -17.787 -18.215 -30.016 1.00 32.21  ? 254 SER   A O   1 
ATOM   2038 C  CB  . SER   A 1 254 ? -15.326 -18.094 -32.321 1.00 35.24  ? 254 SER   A CB  1 
ATOM   2039 O  OG  . SER   A 1 254 ? -16.396 -17.888 -33.233 1.00 40.09  ? 254 SER   A OG  1 
ATOM   2040 N  N   . ALA   A 1 255 ? -16.091 -19.704 -29.854 1.00 37.73  ? 255 ALA   A N   1 
ATOM   2041 C  CA  . ALA   A 1 255 ? -16.896 -20.786 -29.313 1.00 38.43  ? 255 ALA   A CA  1 
ATOM   2042 C  C   . ALA   A 1 255 ? -17.396 -20.416 -27.921 1.00 39.32  ? 255 ALA   A C   1 
ATOM   2043 O  O   . ALA   A 1 255 ? -18.550 -20.637 -27.584 1.00 42.84  ? 255 ALA   A O   1 
ATOM   2044 C  CB  . ALA   A 1 255 ? -16.089 -22.068 -29.290 1.00 40.51  ? 255 ALA   A CB  1 
ATOM   2045 N  N   . GLN   A 1 256 ? -16.543 -19.792 -27.116 1.00 39.71  ? 256 GLN   A N   1 
ATOM   2046 C  CA  . GLN   A 1 256 ? -16.965 -19.367 -25.795 1.00 41.83  ? 256 GLN   A CA  1 
ATOM   2047 C  C   . GLN   A 1 256 ? -18.089 -18.319 -25.846 1.00 40.47  ? 256 GLN   A C   1 
ATOM   2048 O  O   . GLN   A 1 256 ? -18.946 -18.300 -24.970 1.00 40.37  ? 256 GLN   A O   1 
ATOM   2049 C  CB  . GLN   A 1 256 ? -15.714 -18.902 -25.053 1.00 50.12  ? 256 GLN   A CB  1 
ATOM   2050 C  CG  . GLN   A 1 256 ? -15.968 -18.455 -23.620 1.00 49.43  ? 256 GLN   A CG  1 
ATOM   2051 C  CD  . GLN   A 1 256 ? -14.717 -17.935 -22.959 1.00 53.22  ? 256 GLN   A CD  1 
ATOM   2052 O  OE1 . GLN   A 1 256 ? -13.597 -18.197 -23.411 1.00 54.43  ? 256 GLN   A OE1 1 
ATOM   2053 N  NE2 . GLN   A 1 256 ? -14.903 -17.188 -21.882 1.00 53.40  ? 256 GLN   A NE2 1 
ATOM   2054 N  N   . THR   A 1 257 ? -18.089 -17.408 -26.823 1.00 36.27  ? 257 THR   A N   1 
ATOM   2055 C  CA  . THR   A 1 257 ? -19.048 -16.314 -26.805 1.00 35.63  ? 257 THR   A CA  1 
ATOM   2056 C  C   . THR   A 1 257 ? -20.229 -16.615 -27.731 1.00 37.67  ? 257 THR   A C   1 
ATOM   2057 O  O   . THR   A 1 257 ? -21.250 -15.938 -27.629 1.00 36.01  ? 257 THR   A O   1 
ATOM   2058 C  CB  . THR   A 1 257 ? -18.412 -14.980 -27.199 1.00 33.58  ? 257 THR   A CB  1 
ATOM   2059 O  OG1 . THR   A 1 257 ? -18.006 -15.194 -28.550 1.00 30.85  ? 257 THR   A OG1 1 
ATOM   2060 C  CG2 . THR   A 1 257 ? -17.289 -14.571 -26.268 1.00 34.06  ? 257 THR   A CG2 1 
ATOM   2061 N  N   . GLY   A 1 258 ? -20.057 -17.570 -28.659 1.00 36.65  ? 258 GLY   A N   1 
ATOM   2062 C  CA  . GLY   A 1 258 ? -21.061 -17.884 -29.660 1.00 37.87  ? 258 GLY   A CA  1 
ATOM   2063 C  C   . GLY   A 1 258 ? -21.215 -16.807 -30.741 1.00 39.64  ? 258 GLY   A C   1 
ATOM   2064 O  O   . GLY   A 1 258 ? -22.300 -16.662 -31.304 1.00 40.20  ? 258 GLY   A O   1 
ATOM   2065 N  N   . ILE   A 1 259 ? -20.140 -16.073 -31.060 1.00 36.42  ? 259 ILE   A N   1 
ATOM   2066 C  CA  . ILE   A 1 259 ? -20.152 -15.113 -32.158 1.00 33.81  ? 259 ILE   A CA  1 
ATOM   2067 C  C   . ILE   A 1 259 ? -19.057 -15.512 -33.146 1.00 35.25  ? 259 ILE   A C   1 
ATOM   2068 O  O   . ILE   A 1 259 ? -17.877 -15.590 -32.779 1.00 34.97  ? 259 ILE   A O   1 
ATOM   2069 C  CB  . ILE   A 1 259 ? -19.956 -13.678 -31.644 1.00 34.16  ? 259 ILE   A CB  1 
ATOM   2070 C  CG1 . ILE   A 1 259 ? -20.986 -13.322 -30.566 1.00 33.41  ? 259 ILE   A CG1 1 
ATOM   2071 C  CG2 . ILE   A 1 259 ? -19.981 -12.683 -32.804 1.00 33.48  ? 259 ILE   A CG2 1 
ATOM   2072 C  CD1 . ILE   A 1 259 ? -20.712 -12.014 -29.830 1.00 32.79  ? 259 ILE   A CD1 1 
ATOM   2073 N  N   . ALA   A 1 260 ? -19.465 -15.822 -34.382 1.00 31.85  ? 260 ALA   A N   1 
ATOM   2074 C  CA  . ALA   A 1 260 ? -18.545 -16.356 -35.379 1.00 33.38  ? 260 ALA   A CA  1 
ATOM   2075 C  C   . ALA   A 1 260 ? -17.519 -15.275 -35.741 1.00 30.57  ? 260 ALA   A C   1 
ATOM   2076 O  O   . ALA   A 1 260 ? -17.789 -14.079 -35.589 1.00 26.67  ? 260 ALA   A O   1 
ATOM   2077 C  CB  . ALA   A 1 260 ? -19.323 -16.845 -36.586 1.00 33.81  ? 260 ALA   A CB  1 
ATOM   2078 N  N   . VAL   A 1 261 ? -16.332 -15.697 -36.203 1.00 29.56  ? 261 VAL   A N   1 
ATOM   2079 C  CA  . VAL   A 1 261 ? -15.233 -14.762 -36.416 1.00 30.72  ? 261 VAL   A CA  1 
ATOM   2080 C  C   . VAL   A 1 261 ? -15.636 -13.691 -37.433 1.00 27.32  ? 261 VAL   A C   1 
ATOM   2081 O  O   . VAL   A 1 261 ? -15.444 -12.509 -37.185 1.00 28.52  ? 261 VAL   A O   1 
ATOM   2082 C  CB  . VAL   A 1 261 ? -13.922 -15.466 -36.825 1.00 31.77  ? 261 VAL   A CB  1 
ATOM   2083 C  CG1 . VAL   A 1 261 ? -12.839 -14.463 -37.218 1.00 31.07  ? 261 VAL   A CG1 1 
ATOM   2084 C  CG2 . VAL   A 1 261 ? -13.423 -16.401 -35.722 1.00 32.12  ? 261 VAL   A CG2 1 
ATOM   2085 N  N   . LEU   A 1 262 ? -16.240 -14.087 -38.554 1.00 27.30  ? 262 LEU   A N   1 
ATOM   2086 C  CA  . LEU   A 1 262 ? -16.627 -13.144 -39.599 1.00 27.53  ? 262 LEU   A CA  1 
ATOM   2087 C  C   . LEU   A 1 262 ? -17.777 -12.214 -39.197 1.00 29.89  ? 262 LEU   A C   1 
ATOM   2088 O  O   . LEU   A 1 262 ? -17.853 -11.105 -39.733 1.00 30.59  ? 262 LEU   A O   1 
ATOM   2089 C  CB  . LEU   A 1 262 ? -16.929 -13.910 -40.887 1.00 27.76  ? 262 LEU   A CB  1 
ATOM   2090 C  CG  . LEU   A 1 262 ? -15.712 -14.542 -41.566 1.00 29.06  ? 262 LEU   A CG  1 
ATOM   2091 C  CD1 . LEU   A 1 262 ? -16.190 -15.266 -42.814 1.00 30.96  ? 262 LEU   A CD1 1 
ATOM   2092 C  CD2 . LEU   A 1 262 ? -14.597 -13.548 -41.950 1.00 27.90  ? 262 LEU   A CD2 1 
ATOM   2093 N  N   . ASP   A 1 263 ? -18.625 -12.591 -38.224 1.00 29.31  ? 263 ASP   A N   1 
ATOM   2094 C  CA  . ASP   A 1 263 ? -19.601 -11.656 -37.680 1.00 31.46  ? 263 ASP   A CA  1 
ATOM   2095 C  C   . ASP   A 1 263 ? -18.905 -10.549 -36.897 1.00 30.89  ? 263 ASP   A C   1 
ATOM   2096 O  O   . ASP   A 1 263 ? -19.294 -9.378  -36.974 1.00 24.95  ? 263 ASP   A O   1 
ATOM   2097 C  CB  . ASP   A 1 263 ? -20.564 -12.245 -36.658 1.00 38.13  ? 263 ASP   A CB  1 
ATOM   2098 C  CG  . ASP   A 1 263 ? -21.677 -13.137 -37.182 1.00 45.76  ? 263 ASP   A CG  1 
ATOM   2099 O  OD1 . ASP   A 1 263 ? -21.649 -13.493 -38.383 1.00 48.76  ? 263 ASP   A OD1 1 
ATOM   2100 O  OD2 . ASP   A 1 263 ? -22.570 -13.463 -36.376 1.00 47.48  ? 263 ASP   A OD2 1 
ATOM   2101 N  N   . MET   A 1 264 ? -17.932 -10.948 -36.070 1.00 30.67  ? 264 MET   A N   1 
ATOM   2102 C  CA  . MET   A 1 264 ? -17.172 -9.976  -35.306 1.00 29.79  ? 264 MET   A CA  1 
ATOM   2103 C  C   . MET   A 1 264 ? -16.403 -9.049  -36.249 1.00 29.13  ? 264 MET   A C   1 
ATOM   2104 O  O   . MET   A 1 264 ? -16.298 -7.863  -35.937 1.00 29.79  ? 264 MET   A O   1 
ATOM   2105 C  CB  . MET   A 1 264 ? -16.258 -10.643 -34.272 1.00 31.34  ? 264 MET   A CB  1 
ATOM   2106 C  CG  . MET   A 1 264 ? -15.697 -9.664  -33.257 1.00 31.78  ? 264 MET   A CG  1 
ATOM   2107 S  SD  . MET   A 1 264 ? -16.886 -8.883  -32.140 1.00 27.75  ? 264 MET   A SD  1 
ATOM   2108 C  CE  . MET   A 1 264 ? -16.775 -10.033 -30.762 1.00 29.59  ? 264 MET   A CE  1 
ATOM   2109 N  N   . CYS   A 1 265 ? -15.943 -9.559  -37.410 1.00 27.06  ? 265 CYS   A N   1 
ATOM   2110 C  CA  . CYS   A 1 265 ? -15.282 -8.729  -38.411 1.00 26.04  ? 265 CYS   A CA  1 
ATOM   2111 C  C   . CYS   A 1 265 ? -16.224 -7.624  -38.908 1.00 27.92  ? 265 CYS   A C   1 
ATOM   2112 O  O   . CYS   A 1 265 ? -15.771 -6.496  -39.163 1.00 25.15  ? 265 CYS   A O   1 
ATOM   2113 C  CB  . CYS   A 1 265 ? -14.708 -9.569  -39.556 1.00 28.37  ? 265 CYS   A CB  1 
ATOM   2114 S  SG  . CYS   A 1 265 ? -13.250 -10.576 -39.120 1.00 30.03  ? 265 CYS   A SG  1 
ATOM   2115 N  N   . ALA   A 1 266 ? -17.530 -7.949  -39.073 1.00 25.87  ? 266 ALA   A N   1 
ATOM   2116 C  CA  . ALA   A 1 266 ? -18.536 -6.980  -39.497 1.00 25.74  ? 266 ALA   A CA  1 
ATOM   2117 C  C   . ALA   A 1 266 ? -18.672 -5.838  -38.497 1.00 26.19  ? 266 ALA   A C   1 
ATOM   2118 O  O   . ALA   A 1 266 ? -18.735 -4.678  -38.885 1.00 26.83  ? 266 ALA   A O   1 
ATOM   2119 C  CB  . ALA   A 1 266 ? -19.890 -7.636  -39.722 1.00 27.24  ? 266 ALA   A CB  1 
ATOM   2120 N  N   . SER   A 1 267 ? -18.699 -6.184  -37.203 1.00 28.27  ? 267 SER   A N   1 
ATOM   2121 C  CA  . SER   A 1 267 ? -18.695 -5.210  -36.126 1.00 27.99  ? 267 SER   A CA  1 
ATOM   2122 C  C   . SER   A 1 267 ? -17.474 -4.287  -36.199 1.00 25.95  ? 267 SER   A C   1 
ATOM   2123 O  O   . SER   A 1 267 ? -17.594 -3.063  -36.137 1.00 24.81  ? 267 SER   A O   1 
ATOM   2124 C  CB  . SER   A 1 267 ? -18.804 -5.965  -34.810 1.00 32.85  ? 267 SER   A CB  1 
ATOM   2125 O  OG  . SER   A 1 267 ? -18.884 -5.085  -33.709 1.00 42.35  ? 267 SER   A OG  1 
ATOM   2126 N  N   . LEU   A 1 268 ? -16.275 -4.862  -36.334 1.00 28.05  ? 268 LEU   A N   1 
ATOM   2127 C  CA  . LEU   A 1 268 ? -15.075 -4.057  -36.530 1.00 25.15  ? 268 LEU   A CA  1 
ATOM   2128 C  C   . LEU   A 1 268 ? -15.227 -3.108  -37.728 1.00 25.96  ? 268 LEU   A C   1 
ATOM   2129 O  O   . LEU   A 1 268 ? -14.867 -1.922  -37.617 1.00 22.85  ? 268 LEU   A O   1 
ATOM   2130 C  CB  . LEU   A 1 268 ? -13.827 -4.936  -36.621 1.00 23.95  ? 268 LEU   A CB  1 
ATOM   2131 C  CG  . LEU   A 1 268 ? -12.508 -4.197  -36.863 1.00 24.95  ? 268 LEU   A CG  1 
ATOM   2132 C  CD1 . LEU   A 1 268 ? -12.311 -3.001  -35.935 1.00 25.08  ? 268 LEU   A CD1 1 
ATOM   2133 C  CD2 . LEU   A 1 268 ? -11.337 -5.137  -36.716 1.00 25.53  ? 268 LEU   A CD2 1 
ATOM   2134 N  N   . LYS   A 1 269 ? -15.790 -3.579  -38.862 1.00 26.70  ? 269 LYS   A N   1 
ATOM   2135 C  CA  . LYS   A 1 269 ? -15.889 -2.726  -40.046 1.00 26.96  ? 269 LYS   A CA  1 
ATOM   2136 C  C   . LYS   A 1 269 ? -16.740 -1.497  -39.742 1.00 26.50  ? 269 LYS   A C   1 
ATOM   2137 O  O   . LYS   A 1 269 ? -16.462 -0.393  -40.231 1.00 24.31  ? 269 LYS   A O   1 
ATOM   2138 C  CB  . LYS   A 1 269 ? -16.535 -3.364  -41.288 1.00 34.63  ? 269 LYS   A CB  1 
ATOM   2139 C  CG  . LYS   A 1 269 ? -15.719 -4.417  -42.024 1.00 39.67  ? 269 LYS   A CG  1 
ATOM   2140 C  CD  . LYS   A 1 269 ? -16.499 -5.469  -42.828 1.00 40.86  ? 269 LYS   A CD  1 
ATOM   2141 C  CE  . LYS   A 1 269 ? -16.808 -5.065  -44.246 1.00 39.75  ? 269 LYS   A CE  1 
ATOM   2142 N  NZ  . LYS   A 1 269 ? -17.591 -6.089  -44.959 1.00 39.97  ? 269 LYS   A NZ  1 
ATOM   2143 N  N   . GLU   A 1 270 ? -17.805 -1.718  -38.947 1.00 28.61  ? 270 GLU   A N   1 
ATOM   2144 C  CA  . GLU   A 1 270 ? -18.754 -0.676  -38.569 1.00 27.40  ? 270 GLU   A CA  1 
ATOM   2145 C  C   . GLU   A 1 270 ? -18.108 0.338   -37.622 1.00 25.85  ? 270 GLU   A C   1 
ATOM   2146 O  O   . GLU   A 1 270 ? -18.243 1.550   -37.817 1.00 22.56  ? 270 GLU   A O   1 
ATOM   2147 C  CB  . GLU   A 1 270 ? -20.004 -1.301  -37.949 1.00 27.90  ? 270 GLU   A CB  1 
ATOM   2148 C  CG  . GLU   A 1 270 ? -21.042 -0.272  -37.510 1.00 29.30  ? 270 GLU   A CG  1 
ATOM   2149 C  CD  . GLU   A 1 270 ? -22.443 -0.870  -37.414 1.00 33.94  ? 270 GLU   A CD  1 
ATOM   2150 O  OE1 . GLU   A 1 270 ? -23.130 -1.067  -38.453 1.00 33.59  ? 270 GLU   A OE1 1 
ATOM   2151 O  OE2 . GLU   A 1 270 ? -22.850 -1.162  -36.285 1.00 32.76  ? 270 GLU   A OE2 1 
ATOM   2152 N  N   . LEU   A 1 271 ? -17.399 -0.159  -36.600 1.00 25.95  ? 271 LEU   A N   1 
ATOM   2153 C  CA  . LEU   A 1 271 ? -16.682 0.712   -35.670 1.00 26.24  ? 271 LEU   A CA  1 
ATOM   2154 C  C   . LEU   A 1 271 ? -15.731 1.624   -36.440 1.00 27.22  ? 271 LEU   A C   1 
ATOM   2155 O  O   . LEU   A 1 271 ? -15.646 2.807   -36.130 1.00 28.80  ? 271 LEU   A O   1 
ATOM   2156 C  CB  . LEU   A 1 271 ? -15.926 -0.115  -34.631 1.00 26.75  ? 271 LEU   A CB  1 
ATOM   2157 C  CG  . LEU   A 1 271 ? -16.753 -0.702  -33.487 1.00 24.60  ? 271 LEU   A CG  1 
ATOM   2158 C  CD1 . LEU   A 1 271 ? -16.080 -1.863  -32.808 1.00 25.16  ? 271 LEU   A CD1 1 
ATOM   2159 C  CD2 . LEU   A 1 271 ? -17.095 0.384   -32.495 1.00 25.56  ? 271 LEU   A CD2 1 
ATOM   2160 N  N   . LEU   A 1 272 ? -15.053 1.084   -37.468 1.00 27.90  ? 272 LEU   A N   1 
ATOM   2161 C  CA  . LEU   A 1 272 ? -14.083 1.864   -38.225 1.00 27.77  ? 272 LEU   A CA  1 
ATOM   2162 C  C   . LEU   A 1 272 ? -14.779 3.017   -38.954 1.00 29.81  ? 272 LEU   A C   1 
ATOM   2163 O  O   . LEU   A 1 272 ? -14.236 4.118   -39.035 1.00 26.97  ? 272 LEU   A O   1 
ATOM   2164 C  CB  . LEU   A 1 272 ? -13.273 0.990   -39.190 1.00 27.71  ? 272 LEU   A CB  1 
ATOM   2165 C  CG  . LEU   A 1 272 ? -12.206 0.092   -38.552 1.00 29.16  ? 272 LEU   A CG  1 
ATOM   2166 C  CD1 . LEU   A 1 272 ? -11.623 -0.957  -39.470 1.00 30.15  ? 272 LEU   A CD1 1 
ATOM   2167 C  CD2 . LEU   A 1 272 ? -11.068 0.944   -38.031 1.00 32.28  ? 272 LEU   A CD2 1 
ATOM   2168 N  N   . GLN   A 1 273 ? -15.967 2.748   -39.517 1.00 28.91  ? 273 GLN   A N   1 
ATOM   2169 C  CA  . GLN   A 1 273 ? -16.752 3.733   -40.252 1.00 25.25  ? 273 GLN   A CA  1 
ATOM   2170 C  C   . GLN   A 1 273 ? -17.387 4.802   -39.362 1.00 25.14  ? 273 GLN   A C   1 
ATOM   2171 O  O   . GLN   A 1 273 ? -17.518 5.949   -39.797 1.00 24.26  ? 273 GLN   A O   1 
ATOM   2172 C  CB  . GLN   A 1 273 ? -17.829 2.915   -40.960 1.00 28.11  ? 273 GLN   A CB  1 
ATOM   2173 C  CG  . GLN   A 1 273 ? -19.042 3.680   -41.471 1.00 27.57  ? 273 GLN   A CG  1 
ATOM   2174 C  CD  . GLN   A 1 273 ? -20.149 2.737   -41.907 1.00 29.33  ? 273 GLN   A CD  1 
ATOM   2175 O  OE1 . GLN   A 1 273 ? -21.130 2.472   -41.191 1.00 31.25  ? 273 GLN   A OE1 1 
ATOM   2176 N  NE2 . GLN   A 1 273 ? -19.968 2.178   -43.084 1.00 26.55  ? 273 GLN   A NE2 1 
ATOM   2177 N  N   . ASN   A 1 274 ? -17.835 4.416   -38.153 1.00 25.63  ? 274 ASN   A N   1 
ATOM   2178 C  CA  . ASN   A 1 274 ? -18.659 5.263   -37.302 1.00 28.65  ? 274 ASN   A CA  1 
ATOM   2179 C  C   . ASN   A 1 274 ? -17.883 5.906   -36.141 1.00 34.52  ? 274 ASN   A C   1 
ATOM   2180 O  O   . ASN   A 1 274 ? -18.315 6.945   -35.650 1.00 32.83  ? 274 ASN   A O   1 
ATOM   2181 C  CB  . ASN   A 1 274 ? -19.821 4.484   -36.684 1.00 26.71  ? 274 ASN   A CB  1 
ATOM   2182 C  CG  . ASN   A 1 274 ? -20.826 3.997   -37.706 1.00 26.00  ? 274 ASN   A CG  1 
ATOM   2183 O  OD1 . ASN   A 1 274 ? -20.767 4.392   -38.875 1.00 24.82  ? 274 ASN   A OD1 1 
ATOM   2184 N  ND2 . ASN   A 1 274 ? -21.774 3.163   -37.289 1.00 25.53  ? 274 ASN   A ND2 1 
ATOM   2185 N  N   . GLY   A 1 275 ? -16.791 5.292   -35.654 1.00 34.22  ? 275 GLY   A N   1 
ATOM   2186 C  CA  . GLY   A 1 275 ? -16.245 5.663   -34.352 1.00 34.02  ? 275 GLY   A CA  1 
ATOM   2187 C  C   . GLY   A 1 275 ? -17.110 5.149   -33.195 1.00 34.92  ? 275 GLY   A C   1 
ATOM   2188 O  O   . GLY   A 1 275 ? -17.855 4.180   -33.350 1.00 31.99  ? 275 GLY   A O   1 
ATOM   2189 N  N   . MET   A 1 276 ? -16.996 5.777   -32.013 1.00 35.31  ? 276 MET   A N   1 
ATOM   2190 C  CA  . MET   A 1 276 ? -17.597 5.215   -30.806 1.00 38.49  ? 276 MET   A CA  1 
ATOM   2191 C  C   . MET   A 1 276 ? -18.775 6.038   -30.295 1.00 36.82  ? 276 MET   A C   1 
ATOM   2192 O  O   . MET   A 1 276 ? -19.528 5.561   -29.437 1.00 38.04  ? 276 MET   A O   1 
ATOM   2193 C  CB  . MET   A 1 276 ? -16.551 5.077   -29.694 1.00 40.74  ? 276 MET   A CB  1 
ATOM   2194 C  CG  . MET   A 1 276 ? -15.431 4.135   -30.075 1.00 42.77  ? 276 MET   A CG  1 
ATOM   2195 S  SD  . MET   A 1 276 ? -14.752 3.306   -28.636 1.00 54.77  ? 276 MET   A SD  1 
ATOM   2196 C  CE  . MET   A 1 276 ? -14.176 1.845   -29.504 1.00 56.80  ? 276 MET   A CE  1 
ATOM   2197 N  N   . ASN   A 1 277 ? -18.890 7.279   -30.781 1.00 36.20  ? 277 ASN   A N   1 
ATOM   2198 C  CA  . ASN   A 1 277 ? -20.020 8.131   -30.461 1.00 40.91  ? 277 ASN   A CA  1 
ATOM   2199 C  C   . ASN   A 1 277 ? -20.138 8.254   -28.943 1.00 39.72  ? 277 ASN   A C   1 
ATOM   2200 O  O   . ASN   A 1 277 ? -21.155 7.890   -28.364 1.00 40.70  ? 277 ASN   A O   1 
ATOM   2201 C  CB  . ASN   A 1 277 ? -21.283 7.578   -31.116 1.00 45.41  ? 277 ASN   A CB  1 
ATOM   2202 C  CG  . ASN   A 1 277 ? -22.468 8.506   -31.001 1.00 56.56  ? 277 ASN   A CG  1 
ATOM   2203 O  OD1 . ASN   A 1 277 ? -22.306 9.720   -30.828 1.00 65.27  ? 277 ASN   A OD1 1 
ATOM   2204 N  ND2 . ASN   A 1 277 ? -23.668 7.959   -31.126 1.00 62.35  ? 277 ASN   A ND2 1 
ATOM   2205 N  N   . GLY   A 1 278 ? -19.065 8.709   -28.291 1.00 43.64  ? 278 GLY   A N   1 
ATOM   2206 C  CA  . GLY   A 1 278 ? -19.104 9.013   -26.868 1.00 38.31  ? 278 GLY   A CA  1 
ATOM   2207 C  C   . GLY   A 1 278 ? -18.902 7.796   -25.968 1.00 39.34  ? 278 GLY   A C   1 
ATOM   2208 O  O   . GLY   A 1 278 ? -18.659 7.965   -24.787 1.00 42.29  ? 278 GLY   A O   1 
ATOM   2209 N  N   . ARG   A 1 279 ? -19.008 6.567   -26.472 1.00 36.71  ? 279 ARG   A N   1 
ATOM   2210 C  CA  . ARG   A 1 279 ? -18.916 5.409   -25.590 1.00 39.35  ? 279 ARG   A CA  1 
ATOM   2211 C  C   . ARG   A 1 279 ? -17.455 4.988   -25.470 1.00 38.31  ? 279 ARG   A C   1 
ATOM   2212 O  O   . ARG   A 1 279 ? -16.590 5.618   -26.075 1.00 40.34  ? 279 ARG   A O   1 
ATOM   2213 C  CB  . ARG   A 1 279 ? -19.833 4.281   -26.067 1.00 39.24  ? 279 ARG   A CB  1 
ATOM   2214 C  CG  . ARG   A 1 279 ? -21.281 4.689   -25.829 1.00 47.20  ? 279 ARG   A CG  1 
ATOM   2215 C  CD  . ARG   A 1 279 ? -22.254 3.949   -26.694 1.00 48.49  ? 279 ARG   A CD  1 
ATOM   2216 N  NE  . ARG   A 1 279 ? -22.024 4.361   -28.079 1.00 57.41  ? 279 ARG   A NE  1 
ATOM   2217 C  CZ  . ARG   A 1 279 ? -22.711 3.899   -29.117 1.00 64.08  ? 279 ARG   A CZ  1 
ATOM   2218 N  NH1 . ARG   A 1 279 ? -23.787 3.159   -28.922 1.00 64.25  ? 279 ARG   A NH1 1 
ATOM   2219 N  NH2 . ARG   A 1 279 ? -22.333 4.194   -30.349 1.00 59.69  ? 279 ARG   A NH2 1 
ATOM   2220 N  N   . THR   A 1 280 ? -17.215 3.957   -24.645 1.00 38.10  ? 280 THR   A N   1 
ATOM   2221 C  CA  . THR   A 1 280 ? -15.892 3.389   -24.422 1.00 41.53  ? 280 THR   A CA  1 
ATOM   2222 C  C   . THR   A 1 280 ? -16.028 1.873   -24.475 1.00 37.97  ? 280 THR   A C   1 
ATOM   2223 O  O   . THR   A 1 280 ? -17.134 1.340   -24.383 1.00 39.99  ? 280 THR   A O   1 
ATOM   2224 C  CB  . THR   A 1 280 ? -15.267 3.866   -23.101 1.00 42.13  ? 280 THR   A CB  1 
ATOM   2225 O  OG1 . THR   A 1 280 ? -16.087 3.506   -21.994 1.00 40.36  ? 280 THR   A OG1 1 
ATOM   2226 C  CG2 . THR   A 1 280 ? -15.054 5.370   -23.052 1.00 37.99  ? 280 THR   A CG2 1 
ATOM   2227 N  N   . ILE   A 1 281 ? -14.905 1.200   -24.714 1.00 37.70  ? 281 ILE   A N   1 
ATOM   2228 C  CA  . ILE   A 1 281 ? -14.847 -0.250  -24.621 1.00 34.29  ? 281 ILE   A CA  1 
ATOM   2229 C  C   . ILE   A 1 281 ? -13.721 -0.596  -23.657 1.00 33.63  ? 281 ILE   A C   1 
ATOM   2230 O  O   . ILE   A 1 281 ? -12.599 -0.137  -23.837 1.00 36.61  ? 281 ILE   A O   1 
ATOM   2231 C  CB  . ILE   A 1 281 ? -14.659 -0.911  -26.004 1.00 33.50  ? 281 ILE   A CB  1 
ATOM   2232 C  CG1 . ILE   A 1 281 ? -15.829 -0.635  -26.924 1.00 32.07  ? 281 ILE   A CG1 1 
ATOM   2233 C  CG2 . ILE   A 1 281 ? -14.432 -2.422  -25.874 1.00 37.67  ? 281 ILE   A CG2 1 
ATOM   2234 C  CD1 . ILE   A 1 281 ? -15.609 -1.132  -28.338 1.00 32.58  ? 281 ILE   A CD1 1 
ATOM   2235 N  N   . LEU   A 1 282 ? -14.046 -1.366  -22.614 1.00 37.80  ? 282 LEU   A N   1 
ATOM   2236 C  CA  . LEU   A 1 282 ? -13.100 -1.700  -21.561 1.00 36.02  ? 282 LEU   A CA  1 
ATOM   2237 C  C   . LEU   A 1 282 ? -12.276 -0.478  -21.161 1.00 39.06  ? 282 LEU   A C   1 
ATOM   2238 O  O   . LEU   A 1 282 ? -11.065 -0.570  -21.003 1.00 41.55  ? 282 LEU   A O   1 
ATOM   2239 C  CB  . LEU   A 1 282 ? -12.224 -2.845  -22.067 1.00 35.82  ? 282 LEU   A CB  1 
ATOM   2240 C  CG  . LEU   A 1 282 ? -12.968 -4.154  -22.356 1.00 33.94  ? 282 LEU   A CG  1 
ATOM   2241 C  CD1 . LEU   A 1 282 ? -12.125 -5.145  -23.128 1.00 32.76  ? 282 LEU   A CD1 1 
ATOM   2242 C  CD2 . LEU   A 1 282 ? -13.454 -4.783  -21.069 1.00 36.37  ? 282 LEU   A CD2 1 
ATOM   2243 N  N   . GLY   A 1 283 ? -12.924 0.683   -21.027 1.00 40.60  ? 283 GLY   A N   1 
ATOM   2244 C  CA  . GLY   A 1 283 ? -12.254 1.850   -20.483 1.00 40.88  ? 283 GLY   A CA  1 
ATOM   2245 C  C   . GLY   A 1 283 ? -11.389 2.574   -21.509 1.00 43.78  ? 283 GLY   A C   1 
ATOM   2246 O  O   . GLY   A 1 283 ? -10.573 3.423   -21.146 1.00 48.74  ? 283 GLY   A O   1 
ATOM   2247 N  N   . SER   A 1 284 ? -11.567 2.245   -22.793 1.00 40.63  ? 284 SER   A N   1 
ATOM   2248 C  CA  . SER   A 1 284 ? -10.797 2.891   -23.843 1.00 37.48  ? 284 SER   A CA  1 
ATOM   2249 C  C   . SER   A 1 284 ? -11.729 3.520   -24.872 1.00 35.42  ? 284 SER   A C   1 
ATOM   2250 O  O   . SER   A 1 284 ? -12.771 2.948   -25.180 1.00 38.86  ? 284 SER   A O   1 
ATOM   2251 C  CB  . SER   A 1 284 ? -9.874  1.936   -24.512 1.00 33.18  ? 284 SER   A CB  1 
ATOM   2252 O  OG  . SER   A 1 284 ? -9.007  2.682   -25.351 1.00 33.93  ? 284 SER   A OG  1 
ATOM   2253 N  N   . ALA   A 1 285 ? -11.317 4.674   -25.408 1.00 33.70  ? 285 ALA   A N   1 
ATOM   2254 C  CA  . ALA   A 1 285 ? -12.063 5.342   -26.465 1.00 34.50  ? 285 ALA   A CA  1 
ATOM   2255 C  C   . ALA   A 1 285 ? -11.404 5.132   -27.836 1.00 37.84  ? 285 ALA   A C   1 
ATOM   2256 O  O   . ALA   A 1 285 ? -11.794 5.788   -28.793 1.00 34.97  ? 285 ALA   A O   1 
ATOM   2257 C  CB  . ALA   A 1 285 ? -12.198 6.809   -26.116 1.00 33.90  ? 285 ALA   A CB  1 
ATOM   2258 N  N   . LEU   A 1 286 ? -10.424 4.209   -27.928 1.00 39.14  ? 286 LEU   A N   1 
ATOM   2259 C  CA  . LEU   A 1 286 ? -9.794  3.785   -29.177 1.00 35.24  ? 286 LEU   A CA  1 
ATOM   2260 C  C   . LEU   A 1 286 ? -9.893  2.267   -29.286 1.00 32.26  ? 286 LEU   A C   1 
ATOM   2261 O  O   . LEU   A 1 286 ? -10.096 1.574   -28.288 1.00 32.09  ? 286 LEU   A O   1 
ATOM   2262 C  CB  . LEU   A 1 286 ? -8.311  4.161   -29.184 1.00 42.04  ? 286 LEU   A CB  1 
ATOM   2263 C  CG  . LEU   A 1 286 ? -7.954  5.632   -29.381 1.00 45.40  ? 286 LEU   A CG  1 
ATOM   2264 C  CD1 . LEU   A 1 286 ? -6.461  5.756   -29.519 1.00 43.04  ? 286 LEU   A CD1 1 
ATOM   2265 C  CD2 . LEU   A 1 286 ? -8.663  6.223   -30.591 1.00 51.14  ? 286 LEU   A CD2 1 
ATOM   2266 N  N   . LEU   A 1 287 ? -9.620  1.724   -30.477 1.00 27.86  ? 287 LEU   A N   1 
ATOM   2267 C  CA  . LEU   A 1 287 ? -9.507  0.275   -30.621 1.00 27.55  ? 287 LEU   A CA  1 
ATOM   2268 C  C   . LEU   A 1 287 ? -8.084  -0.176  -30.248 1.00 27.35  ? 287 LEU   A C   1 
ATOM   2269 O  O   . LEU   A 1 287 ? -7.126  0.286   -30.845 1.00 28.08  ? 287 LEU   A O   1 
ATOM   2270 C  CB  . LEU   A 1 287 ? -9.876  -0.075  -32.063 1.00 27.38  ? 287 LEU   A CB  1 
ATOM   2271 C  CG  . LEU   A 1 287 ? -11.218 0.497   -32.556 1.00 28.63  ? 287 LEU   A CG  1 
ATOM   2272 C  CD1 . LEU   A 1 287 ? -11.534 0.217   -34.018 1.00 29.03  ? 287 LEU   A CD1 1 
ATOM   2273 C  CD2 . LEU   A 1 287 ? -12.339 -0.008  -31.675 1.00 29.19  ? 287 LEU   A CD2 1 
ATOM   2274 N  N   . GLU   A 1 288 ? -7.954  -1.099  -29.292 1.00 27.64  ? 288 GLU   A N   1 
ATOM   2275 C  CA  . GLU   A 1 288 ? -6.665  -1.498  -28.735 1.00 29.61  ? 288 GLU   A CA  1 
ATOM   2276 C  C   . GLU   A 1 288 ? -6.138  -2.734  -29.453 1.00 29.18  ? 288 GLU   A C   1 
ATOM   2277 O  O   . GLU   A 1 288 ? -6.894  -3.704  -29.633 1.00 26.01  ? 288 GLU   A O   1 
ATOM   2278 C  CB  . GLU   A 1 288 ? -6.790  -1.872  -27.256 1.00 35.59  ? 288 GLU   A CB  1 
ATOM   2279 C  CG  . GLU   A 1 288 ? -7.153  -0.703  -26.336 1.00 44.50  ? 288 GLU   A CG  1 
ATOM   2280 C  CD  . GLU   A 1 288 ? -6.106  0.417   -26.247 1.00 52.71  ? 288 GLU   A CD  1 
ATOM   2281 O  OE1 . GLU   A 1 288 ? -4.888  0.088   -26.204 1.00 43.19  ? 288 GLU   A OE1 1 
ATOM   2282 O  OE2 . GLU   A 1 288 ? -6.499  1.621   -26.226 1.00 54.34  ? 288 GLU   A OE2 1 
ATOM   2283 N  N   . ASP   A 1 289 ? -4.820  -2.719  -29.755 1.00 24.93  ? 289 ASP   A N   1 
ATOM   2284 C  CA  . ASP   A 1 289 ? -4.192  -3.745  -30.572 1.00 24.94  ? 289 ASP   A CA  1 
ATOM   2285 C  C   . ASP   A 1 289 ? -2.978  -4.382  -29.894 1.00 23.45  ? 289 ASP   A C   1 
ATOM   2286 O  O   . ASP   A 1 289 ? -2.269  -5.147  -30.563 1.00 22.90  ? 289 ASP   A O   1 
ATOM   2287 C  CB  . ASP   A 1 289 ? -3.860  -3.246  -31.978 1.00 25.46  ? 289 ASP   A CB  1 
ATOM   2288 C  CG  . ASP   A 1 289 ? -2.637  -2.350  -32.124 1.00 27.17  ? 289 ASP   A CG  1 
ATOM   2289 O  OD1 . ASP   A 1 289 ? -2.135  -1.846  -31.074 1.00 23.59  ? 289 ASP   A OD1 1 
ATOM   2290 O  OD2 . ASP   A 1 289 ? -2.188  -2.174  -33.285 1.00 24.12  ? 289 ASP   A OD2 1 
ATOM   2291 N  N   . GLU   A 1 290 ? -2.795  -4.185  -28.573 1.00 20.71  ? 290 GLU   A N   1 
ATOM   2292 C  CA  . GLU   A 1 290 ? -1.648  -4.773  -27.887 1.00 23.77  ? 290 GLU   A CA  1 
ATOM   2293 C  C   . GLU   A 1 290 ? -2.056  -5.882  -26.894 1.00 23.87  ? 290 GLU   A C   1 
ATOM   2294 O  O   . GLU   A 1 290 ? -1.290  -6.190  -25.978 1.00 25.51  ? 290 GLU   A O   1 
ATOM   2295 C  CB  . GLU   A 1 290 ? -0.723  -3.678  -27.325 1.00 23.39  ? 290 GLU   A CB  1 
ATOM   2296 C  CG  . GLU   A 1 290 ? -0.011  -2.858  -28.401 1.00 24.98  ? 290 GLU   A CG  1 
ATOM   2297 C  CD  . GLU   A 1 290 ? 1.316   -2.156  -28.047 1.00 27.03  ? 290 GLU   A CD  1 
ATOM   2298 O  OE1 . GLU   A 1 290 ? 1.690   -2.165  -26.852 1.00 24.62  ? 290 GLU   A OE1 1 
ATOM   2299 O  OE2 . GLU   A 1 290 ? 1.989   -1.582  -28.965 1.00 24.21  ? 290 GLU   A OE2 1 
ATOM   2300 N  N   . PHE   A 1 291 ? -3.184  -6.582  -27.124 1.00 26.91  ? 291 PHE   A N   1 
ATOM   2301 C  CA  . PHE   A 1 291 ? -3.541  -7.801  -26.382 1.00 27.23  ? 291 PHE   A CA  1 
ATOM   2302 C  C   . PHE   A 1 291 ? -3.732  -8.976  -27.348 1.00 24.71  ? 291 PHE   A C   1 
ATOM   2303 O  O   . PHE   A 1 291 ? -4.573  -8.883  -28.237 1.00 28.09  ? 291 PHE   A O   1 
ATOM   2304 C  CB  . PHE   A 1 291 ? -4.857  -7.676  -25.590 1.00 29.55  ? 291 PHE   A CB  1 
ATOM   2305 C  CG  . PHE   A 1 291 ? -4.933  -6.601  -24.511 1.00 30.17  ? 291 PHE   A CG  1 
ATOM   2306 C  CD1 . PHE   A 1 291 ? -4.550  -6.871  -23.200 1.00 35.48  ? 291 PHE   A CD1 1 
ATOM   2307 C  CD2 . PHE   A 1 291 ? -5.418  -5.331  -24.797 1.00 31.37  ? 291 PHE   A CD2 1 
ATOM   2308 C  CE1 . PHE   A 1 291 ? -4.620  -5.882  -22.217 1.00 34.52  ? 291 PHE   A CE1 1 
ATOM   2309 C  CE2 . PHE   A 1 291 ? -5.477  -4.347  -23.818 1.00 33.27  ? 291 PHE   A CE2 1 
ATOM   2310 C  CZ  . PHE   A 1 291 ? -5.084  -4.624  -22.529 1.00 32.20  ? 291 PHE   A CZ  1 
ATOM   2311 N  N   . THR   A 1 292 ? -2.984  -10.075 -27.179 1.00 25.70  ? 292 THR   A N   1 
ATOM   2312 C  CA  . THR   A 1 292 ? -3.114  -11.234 -28.060 1.00 25.03  ? 292 THR   A CA  1 
ATOM   2313 C  C   . THR   A 1 292 ? -4.318  -12.098 -27.668 1.00 25.94  ? 292 THR   A C   1 
ATOM   2314 O  O   . THR   A 1 292 ? -4.867  -11.978 -26.576 1.00 26.02  ? 292 THR   A O   1 
ATOM   2315 C  CB  . THR   A 1 292 ? -1.867  -12.112 -28.097 1.00 25.64  ? 292 THR   A CB  1 
ATOM   2316 O  OG1 . THR   A 1 292 ? -1.707  -12.729 -26.829 1.00 26.10  ? 292 THR   A OG1 1 
ATOM   2317 C  CG2 . THR   A 1 292 ? -0.591  -11.370 -28.462 1.00 30.11  ? 292 THR   A CG2 1 
ATOM   2318 N  N   . PRO   A 1 293 ? -4.797  -12.997 -28.566 1.00 26.68  ? 293 PRO   A N   1 
ATOM   2319 C  CA  . PRO   A 1 293 ? -5.771  -14.028 -28.183 1.00 27.90  ? 293 PRO   A CA  1 
ATOM   2320 C  C   . PRO   A 1 293 ? -5.371  -14.812 -26.932 1.00 31.76  ? 293 PRO   A C   1 
ATOM   2321 O  O   . PRO   A 1 293 ? -6.221  -15.110 -26.079 1.00 27.16  ? 293 PRO   A O   1 
ATOM   2322 C  CB  . PRO   A 1 293 ? -5.850  -14.910 -29.431 1.00 27.87  ? 293 PRO   A CB  1 
ATOM   2323 C  CG  . PRO   A 1 293 ? -5.621  -13.919 -30.555 1.00 31.07  ? 293 PRO   A CG  1 
ATOM   2324 C  CD  . PRO   A 1 293 ? -4.532  -12.980 -30.019 1.00 27.68  ? 293 PRO   A CD  1 
ATOM   2325 N  N   . PHE   A 1 294 ? -4.066  -15.103 -26.798 1.00 31.22  ? 294 PHE   A N   1 
ATOM   2326 C  CA  . PHE   A 1 294 ? -3.593  -15.851 -25.641 1.00 34.39  ? 294 PHE   A CA  1 
ATOM   2327 C  C   . PHE   A 1 294 ? -3.678  -14.965 -24.391 1.00 31.49  ? 294 PHE   A C   1 
ATOM   2328 O  O   . PHE   A 1 294 ? -4.115  -15.435 -23.347 1.00 34.82  ? 294 PHE   A O   1 
ATOM   2329 C  CB  . PHE   A 1 294 ? -2.222  -16.440 -25.989 1.00 41.10  ? 294 PHE   A CB  1 
ATOM   2330 C  CG  . PHE   A 1 294 ? -1.595  -17.377 -24.957 1.00 48.80  ? 294 PHE   A CG  1 
ATOM   2331 C  CD1 . PHE   A 1 294 ? -1.096  -16.887 -23.747 1.00 53.17  ? 294 PHE   A CD1 1 
ATOM   2332 C  CD2 . PHE   A 1 294 ? -1.426  -18.738 -25.228 1.00 52.84  ? 294 PHE   A CD2 1 
ATOM   2333 C  CE1 . PHE   A 1 294 ? -0.498  -17.738 -22.816 1.00 55.90  ? 294 PHE   A CE1 1 
ATOM   2334 C  CE2 . PHE   A 1 294 ? -0.824  -19.585 -24.298 1.00 53.96  ? 294 PHE   A CE2 1 
ATOM   2335 C  CZ  . PHE   A 1 294 ? -0.361  -19.085 -23.095 1.00 57.10  ? 294 PHE   A CZ  1 
ATOM   2336 N  N   . ASP   A 1 295 ? -3.307  -13.680 -24.488 1.00 29.17  ? 295 ASP   A N   1 
ATOM   2337 C  CA  . ASP   A 1 295 ? -3.408  -12.756 -23.364 1.00 28.29  ? 295 ASP   A CA  1 
ATOM   2338 C  C   . ASP   A 1 295 ? -4.866  -12.677 -22.863 1.00 33.40  ? 295 ASP   A C   1 
ATOM   2339 O  O   . ASP   A 1 295 ? -5.092  -12.586 -21.655 1.00 30.01  ? 295 ASP   A O   1 
ATOM   2340 C  CB  . ASP   A 1 295 ? -2.892  -11.375 -23.747 1.00 30.01  ? 295 ASP   A CB  1 
ATOM   2341 C  CG  . ASP   A 1 295 ? -1.403  -11.245 -24.064 1.00 30.08  ? 295 ASP   A CG  1 
ATOM   2342 O  OD1 . ASP   A 1 295 ? -0.661  -12.185 -23.765 1.00 29.93  ? 295 ASP   A OD1 1 
ATOM   2343 O  OD2 . ASP   A 1 295 ? -0.994  -10.208 -24.639 1.00 28.81  ? 295 ASP   A OD2 1 
ATOM   2344 N  N   . VAL   A 1 296 ? -5.858  -12.730 -23.780 1.00 31.44  ? 296 VAL   A N   1 
ATOM   2345 C  CA  . VAL   A 1 296 ? -7.273  -12.566 -23.441 1.00 31.33  ? 296 VAL   A CA  1 
ATOM   2346 C  C   . VAL   A 1 296 ? -7.754  -13.754 -22.611 1.00 32.89  ? 296 VAL   A C   1 
ATOM   2347 O  O   . VAL   A 1 296 ? -8.418  -13.575 -21.583 1.00 33.41  ? 296 VAL   A O   1 
ATOM   2348 C  CB  . VAL   A 1 296 ? -8.169  -12.337 -24.680 1.00 30.66  ? 296 VAL   A CB  1 
ATOM   2349 C  CG1 . VAL   A 1 296 ? -9.661  -12.447 -24.390 1.00 30.47  ? 296 VAL   A CG1 1 
ATOM   2350 C  CG2 . VAL   A 1 296 ? -7.921  -10.969 -25.299 1.00 31.22  ? 296 VAL   A CG2 1 
ATOM   2351 N  N   . VAL   A 1 297 ? -7.401  -14.973 -23.036 1.00 36.45  ? 297 VAL   A N   1 
ATOM   2352 C  CA  . VAL   A 1 297 ? -7.843  -16.164 -22.323 1.00 37.49  ? 297 VAL   A CA  1 
ATOM   2353 C  C   . VAL   A 1 297 ? -7.180  -16.218 -20.948 1.00 40.51  ? 297 VAL   A C   1 
ATOM   2354 O  O   . VAL   A 1 297 ? -7.832  -16.513 -19.952 1.00 42.11  ? 297 VAL   A O   1 
ATOM   2355 C  CB  . VAL   A 1 297 ? -7.588  -17.439 -23.143 1.00 36.40  ? 297 VAL   A CB  1 
ATOM   2356 C  CG1 . VAL   A 1 297 ? -7.786  -18.694 -22.310 1.00 40.30  ? 297 VAL   A CG1 1 
ATOM   2357 C  CG2 . VAL   A 1 297 ? -8.488  -17.475 -24.368 1.00 37.80  ? 297 VAL   A CG2 1 
ATOM   2358 N  N   . ARG   A 1 298 ? -5.886  -15.896 -20.888 1.00 45.84  ? 298 ARG   A N   1 
ATOM   2359 C  CA  . ARG   A 1 298 ? -5.161  -15.905 -19.626 1.00 47.89  ? 298 ARG   A CA  1 
ATOM   2360 C  C   . ARG   A 1 298 ? -5.846  -14.986 -18.612 1.00 42.29  ? 298 ARG   A C   1 
ATOM   2361 O  O   . ARG   A 1 298 ? -5.998  -15.355 -17.458 1.00 40.01  ? 298 ARG   A O   1 
ATOM   2362 C  CB  . ARG   A 1 298 ? -3.696  -15.487 -19.802 1.00 55.90  ? 298 ARG   A CB  1 
ATOM   2363 C  CG  . ARG   A 1 298 ? -2.768  -16.243 -18.867 1.00 73.24  ? 298 ARG   A CG  1 
ATOM   2364 C  CD  . ARG   A 1 298 ? -2.492  -17.658 -19.392 1.00 89.05  ? 298 ARG   A CD  1 
ATOM   2365 N  NE  . ARG   A 1 298 ? -2.234  -18.633 -18.323 1.00 104.28 ? 298 ARG   A NE  1 
ATOM   2366 C  CZ  . ARG   A 1 298 ? -1.249  -18.598 -17.420 1.00 107.65 ? 298 ARG   A CZ  1 
ATOM   2367 N  NH1 . ARG   A 1 298 ? -0.331  -17.641 -17.437 1.00 105.23 ? 298 ARG   A NH1 1 
ATOM   2368 N  NH2 . ARG   A 1 298 ? -1.185  -19.540 -16.493 1.00 110.33 ? 298 ARG   A NH2 1 
ATOM   2369 N  N   . GLN   A 1 299 ? -6.256  -13.782 -19.034 1.00 41.74  ? 299 GLN   A N   1 
ATOM   2370 C  CA  . GLN   A 1 299 ? -6.730  -12.776 -18.097 1.00 38.67  ? 299 GLN   A CA  1 
ATOM   2371 C  C   . GLN   A 1 299 ? -8.208  -13.004 -17.762 1.00 41.66  ? 299 GLN   A C   1 
ATOM   2372 O  O   . GLN   A 1 299 ? -8.613  -12.744 -16.629 1.00 42.45  ? 299 GLN   A O   1 
ATOM   2373 C  CB  . GLN   A 1 299 ? -6.415  -11.344 -18.554 1.00 39.48  ? 299 GLN   A CB  1 
ATOM   2374 C  CG  . GLN   A 1 299 ? -6.999  -10.295 -17.610 1.00 39.95  ? 299 GLN   A CG  1 
ATOM   2375 C  CD  . GLN   A 1 299 ? -6.490  -8.875  -17.756 1.00 39.01  ? 299 GLN   A CD  1 
ATOM   2376 O  OE1 . GLN   A 1 299 ? -6.950  -7.985  -17.044 1.00 38.12  ? 299 GLN   A OE1 1 
ATOM   2377 N  NE2 . GLN   A 1 299 ? -5.550  -8.611  -18.646 1.00 40.44  ? 299 GLN   A NE2 1 
ATOM   2378 N  N   . CYS   A 1 300 ? -9.007  -13.497 -18.723 1.00 43.15  ? 300 CYS   A N   1 
ATOM   2379 C  CA  . CYS   A 1 300 ? -10.448 -13.658 -18.546 1.00 45.41  ? 300 CYS   A CA  1 
ATOM   2380 C  C   . CYS   A 1 300 ? -10.802 -15.030 -17.964 1.00 52.48  ? 300 CYS   A C   1 
ATOM   2381 O  O   . CYS   A 1 300 ? -10.025 -15.977 -18.039 1.00 55.02  ? 300 CYS   A O   1 
ATOM   2382 C  CB  . CYS   A 1 300 ? -11.194 -13.509 -19.867 1.00 42.67  ? 300 CYS   A CB  1 
ATOM   2383 S  SG  . CYS   A 1 300 ? -11.166 -11.819 -20.510 1.00 45.05  ? 300 CYS   A SG  1 
ATOM   2384 N  N   . SER   A 1 301 ? -12.016 -15.128 -17.417 1.00 65.52  ? 301 SER   A N   1 
ATOM   2385 C  CA  . SER   A 1 301 ? -12.537 -16.381 -16.895 1.00 78.43  ? 301 SER   A CA  1 
ATOM   2386 C  C   . SER   A 1 301 ? -12.592 -17.428 -18.021 1.00 80.76  ? 301 SER   A C   1 
ATOM   2387 O  O   . SER   A 1 301 ? -11.493 -17.797 -18.511 1.00 75.43  ? 301 SER   A O   1 
ATOM   2388 C  CB  . SER   A 1 301 ? -13.897 -16.179 -16.240 1.00 77.77  ? 301 SER   A CB  1 
ATOM   2389 O  OG  . SER   A 1 301 ? -14.882 -15.783 -17.185 1.00 68.18  ? 301 SER   A OG  1 
ATOM   2390 N  N   . SER   B 1 1   ? 12.927  8.647   -24.552 1.00 29.50  ? 1   SER   B N   1 
ATOM   2391 C  CA  . SER   B 1 1   ? 11.542  9.176   -24.438 1.00 28.46  ? 1   SER   B CA  1 
ATOM   2392 C  C   . SER   B 1 1   ? 10.504  8.056   -24.544 1.00 26.41  ? 1   SER   B C   1 
ATOM   2393 O  O   . SER   B 1 1   ? 10.850  6.874   -24.587 1.00 25.81  ? 1   SER   B O   1 
ATOM   2394 C  CB  . SER   B 1 1   ? 11.318  10.247  -25.468 1.00 31.38  ? 1   SER   B CB  1 
ATOM   2395 O  OG  . SER   B 1 1   ? 11.269  9.694   -26.768 1.00 28.47  ? 1   SER   B OG  1 
ATOM   2396 N  N   . GLY   B 1 2   ? 9.225   8.465   -24.501 1.00 26.75  ? 2   GLY   B N   1 
ATOM   2397 C  CA  . GLY   B 1 2   ? 8.076   7.575   -24.433 1.00 26.68  ? 2   GLY   B CA  1 
ATOM   2398 C  C   . GLY   B 1 2   ? 7.399   7.680   -23.064 1.00 28.87  ? 2   GLY   B C   1 
ATOM   2399 O  O   . GLY   B 1 2   ? 8.031   8.073   -22.100 1.00 31.60  ? 2   GLY   B O   1 
ATOM   2400 N  N   . PHE   B 1 3   ? 6.134   7.267   -22.959 1.00 29.87  ? 3   PHE   B N   1 
ATOM   2401 C  CA  . PHE   B 1 3   ? 5.407   7.371   -21.703 1.00 30.72  ? 3   PHE   B CA  1 
ATOM   2402 C  C   . PHE   B 1 3   ? 4.455   6.188   -21.590 1.00 27.85  ? 3   PHE   B C   1 
ATOM   2403 O  O   . PHE   B 1 3   ? 3.614   5.999   -22.448 1.00 27.07  ? 3   PHE   B O   1 
ATOM   2404 C  CB  . PHE   B 1 3   ? 4.615   8.676   -21.542 1.00 29.70  ? 3   PHE   B CB  1 
ATOM   2405 C  CG  . PHE   B 1 3   ? 4.240   8.923   -20.085 1.00 28.69  ? 3   PHE   B CG  1 
ATOM   2406 C  CD1 . PHE   B 1 3   ? 5.211   9.284   -19.172 1.00 26.48  ? 3   PHE   B CD1 1 
ATOM   2407 C  CD2 . PHE   B 1 3   ? 2.940   8.734   -19.627 1.00 30.80  ? 3   PHE   B CD2 1 
ATOM   2408 C  CE1 . PHE   B 1 3   ? 4.901   9.474   -17.831 1.00 31.88  ? 3   PHE   B CE1 1 
ATOM   2409 C  CE2 . PHE   B 1 3   ? 2.622   8.929   -18.289 1.00 31.65  ? 3   PHE   B CE2 1 
ATOM   2410 C  CZ  . PHE   B 1 3   ? 3.608   9.290   -17.388 1.00 32.57  ? 3   PHE   B CZ  1 
ATOM   2411 N  N   . ARG   B 1 4   ? 4.622   5.382   -20.538 1.00 29.20  ? 4   ARG   B N   1 
ATOM   2412 C  CA  . ARG   B 1 4   ? 3.845   4.164   -20.349 1.00 28.65  ? 4   ARG   B CA  1 
ATOM   2413 C  C   . ARG   B 1 4   ? 3.402   4.052   -18.885 1.00 28.65  ? 4   ARG   B C   1 
ATOM   2414 O  O   . ARG   B 1 4   ? 4.072   4.523   -17.966 1.00 28.97  ? 4   ARG   B O   1 
ATOM   2415 C  CB  . ARG   B 1 4   ? 4.679   2.967   -20.831 1.00 31.44  ? 4   ARG   B CB  1 
ATOM   2416 C  CG  . ARG   B 1 4   ? 4.478   2.641   -22.306 1.00 37.57  ? 4   ARG   B CG  1 
ATOM   2417 C  CD  . ARG   B 1 4   ? 3.468   1.482   -22.536 1.00 38.35  ? 4   ARG   B CD  1 
ATOM   2418 N  NE  . ARG   B 1 4   ? 3.850   0.730   -23.738 1.00 40.80  ? 4   ARG   B NE  1 
ATOM   2419 C  CZ  . ARG   B 1 4   ? 2.993   0.223   -24.626 1.00 50.10  ? 4   ARG   B CZ  1 
ATOM   2420 N  NH1 . ARG   B 1 4   ? 1.806   -0.198  -24.219 1.00 54.55  ? 4   ARG   B NH1 1 
ATOM   2421 N  NH2 . ARG   B 1 4   ? 3.343   0.048   -25.899 1.00 41.42  ? 4   ARG   B NH2 1 
ATOM   2422 N  N   . LYS   B 1 5   ? 2.244   3.431   -18.676 1.00 27.89  ? 5   LYS   B N   1 
ATOM   2423 C  CA  . LYS   B 1 5   ? 1.847   3.018   -17.344 1.00 29.82  ? 5   LYS   B CA  1 
ATOM   2424 C  C   . LYS   B 1 5   ? 2.729   1.852   -16.904 1.00 27.92  ? 5   LYS   B C   1 
ATOM   2425 O  O   . LYS   B 1 5   ? 2.779   0.812   -17.565 1.00 24.99  ? 5   LYS   B O   1 
ATOM   2426 C  CB  . LYS   B 1 5   ? 0.363   2.657   -17.372 1.00 30.42  ? 5   LYS   B CB  1 
ATOM   2427 C  CG  . LYS   B 1 5   ? -0.230  2.433   -16.003 1.00 31.70  ? 5   LYS   B CG  1 
ATOM   2428 C  CD  . LYS   B 1 5   ? -1.732  2.306   -16.090 1.00 35.60  ? 5   LYS   B CD  1 
ATOM   2429 C  CE  . LYS   B 1 5   ? -2.343  3.656   -16.166 1.00 39.83  ? 5   LYS   B CE  1 
ATOM   2430 N  NZ  . LYS   B 1 5   ? -3.775  3.496   -16.393 1.00 46.25  ? 5   LYS   B NZ  1 
ATOM   2431 N  N   . MET   B 1 6   ? 3.360   2.035   -15.745 1.00 27.00  ? 6   MET   B N   1 
ATOM   2432 C  CA  . MET   B 1 6   ? 4.511   1.252   -15.319 1.00 27.34  ? 6   MET   B CA  1 
ATOM   2433 C  C   . MET   B 1 6   ? 4.304   0.867   -13.854 1.00 22.58  ? 6   MET   B C   1 
ATOM   2434 O  O   . MET   B 1 6   ? 4.125   1.756   -13.035 1.00 19.93  ? 6   MET   B O   1 
ATOM   2435 C  CB  . MET   B 1 6   ? 5.725   2.188   -15.440 1.00 30.58  ? 6   MET   B CB  1 
ATOM   2436 C  CG  . MET   B 1 6   ? 7.064   1.550   -15.590 1.00 34.86  ? 6   MET   B CG  1 
ATOM   2437 S  SD  . MET   B 1 6   ? 8.368   2.800   -15.707 1.00 34.31  ? 6   MET   B SD  1 
ATOM   2438 C  CE  . MET   B 1 6   ? 8.369   3.127   -17.472 1.00 34.45  ? 6   MET   B CE  1 
ATOM   2439 N  N   . ALA   B 1 7   ? 4.358   -0.423  -13.504 1.00 20.62  ? 7   ALA   B N   1 
ATOM   2440 C  CA  . ALA   B 1 7   ? 4.333   -0.849  -12.108 1.00 21.16  ? 7   ALA   B CA  1 
ATOM   2441 C  C   . ALA   B 1 7   ? 5.745   -0.840  -11.530 1.00 21.45  ? 7   ALA   B C   1 
ATOM   2442 O  O   . ALA   B 1 7   ? 6.713   -0.883  -12.286 1.00 22.53  ? 7   ALA   B O   1 
ATOM   2443 C  CB  . ALA   B 1 7   ? 3.753   -2.242  -11.987 1.00 23.02  ? 7   ALA   B CB  1 
ATOM   2444 N  N   . PHE   B 1 8   ? 5.851   -0.844  -10.198 1.00 19.77  ? 8   PHE   B N   1 
ATOM   2445 C  CA  . PHE   B 1 8   ? 7.135   -1.085  -9.548  1.00 21.90  ? 8   PHE   B CA  1 
ATOM   2446 C  C   . PHE   B 1 8   ? 7.562   -2.542  -9.741  1.00 21.02  ? 8   PHE   B C   1 
ATOM   2447 O  O   . PHE   B 1 8   ? 6.711   -3.434  -9.801  1.00 20.20  ? 8   PHE   B O   1 
ATOM   2448 C  CB  . PHE   B 1 8   ? 7.105   -0.814  -8.043  1.00 22.76  ? 8   PHE   B CB  1 
ATOM   2449 C  CG  . PHE   B 1 8   ? 7.058   0.655   -7.659  1.00 26.26  ? 8   PHE   B CG  1 
ATOM   2450 C  CD1 . PHE   B 1 8   ? 8.221   1.415   -7.597  1.00 27.89  ? 8   PHE   B CD1 1 
ATOM   2451 C  CD2 . PHE   B 1 8   ? 5.855   1.264   -7.307  1.00 29.37  ? 8   PHE   B CD2 1 
ATOM   2452 C  CE1 . PHE   B 1 8   ? 8.184   2.760   -7.233  1.00 29.95  ? 8   PHE   B CE1 1 
ATOM   2453 C  CE2 . PHE   B 1 8   ? 5.823   2.601   -6.934  1.00 29.49  ? 8   PHE   B CE2 1 
ATOM   2454 C  CZ  . PHE   B 1 8   ? 6.988   3.345   -6.893  1.00 30.28  ? 8   PHE   B CZ  1 
ATOM   2455 N  N   . PRO   B 1 9   ? 8.886   -2.837  -9.772  1.00 23.32  ? 9   PRO   B N   1 
ATOM   2456 C  CA  . PRO   B 1 9   ? 9.385   -4.220  -9.864  1.00 24.43  ? 9   PRO   B CA  1 
ATOM   2457 C  C   . PRO   B 1 9   ? 8.914   -4.988  -8.624  1.00 25.73  ? 9   PRO   B C   1 
ATOM   2458 O  O   . PRO   B 1 9   ? 9.067   -4.488  -7.517  1.00 27.54  ? 9   PRO   B O   1 
ATOM   2459 C  CB  . PRO   B 1 9   ? 10.929  -4.126  -9.924  1.00 25.99  ? 9   PRO   B CB  1 
ATOM   2460 C  CG  . PRO   B 1 9   ? 11.262  -2.633  -9.950  1.00 25.17  ? 9   PRO   B CG  1 
ATOM   2461 C  CD  . PRO   B 1 9   ? 9.969   -1.849  -9.700  1.00 23.92  ? 9   PRO   B CD  1 
ATOM   2462 N  N   . SER   B 1 10  ? 8.388   -6.205  -8.807  1.00 26.67  ? 10  SER   B N   1 
ATOM   2463 C  CA  . SER   B 1 10  ? 7.533   -6.844  -7.806  1.00 27.16  ? 10  SER   B CA  1 
ATOM   2464 C  C   . SER   B 1 10  ? 8.244   -7.910  -6.960  1.00 26.48  ? 10  SER   B C   1 
ATOM   2465 O  O   . SER   B 1 10  ? 7.644   -8.483  -6.049  1.00 28.47  ? 10  SER   B O   1 
ATOM   2466 C  CB  . SER   B 1 10  ? 6.302   -7.422  -8.467  1.00 26.64  ? 10  SER   B CB  1 
ATOM   2467 O  OG  . SER   B 1 10  ? 6.625   -8.352  -9.495  1.00 25.54  ? 10  SER   B OG  1 
ATOM   2468 N  N   . GLY   B 1 11  ? 9.535   -8.140  -7.191  1.00 27.16  ? 11  GLY   B N   1 
ATOM   2469 C  CA  . GLY   B 1 11  ? 10.249  -9.255  -6.573  1.00 29.37  ? 11  GLY   B CA  1 
ATOM   2470 C  C   . GLY   B 1 11  ? 10.271  -9.238  -5.039  1.00 26.98  ? 11  GLY   B C   1 
ATOM   2471 O  O   . GLY   B 1 11  ? 10.129  -10.273 -4.413  1.00 29.36  ? 11  GLY   B O   1 
ATOM   2472 N  N   . LYS   B 1 12  ? 10.458  -8.077  -4.407  1.00 27.76  ? 12  LYS   B N   1 
ATOM   2473 C  CA  . LYS   B 1 12  ? 10.468  -8.009  -2.948  1.00 26.92  ? 12  LYS   B CA  1 
ATOM   2474 C  C   . LYS   B 1 12  ? 9.133   -8.465  -2.360  1.00 27.61  ? 12  LYS   B C   1 
ATOM   2475 O  O   . LYS   B 1 12  ? 9.065   -8.924  -1.228  1.00 27.76  ? 12  LYS   B O   1 
ATOM   2476 C  CB  . LYS   B 1 12  ? 10.763  -6.582  -2.477  1.00 28.34  ? 12  LYS   B CB  1 
ATOM   2477 C  CG  . LYS   B 1 12  ? 12.221  -6.126  -2.588  1.00 29.14  ? 12  LYS   B CG  1 
ATOM   2478 C  CD  . LYS   B 1 12  ? 12.386  -4.658  -2.212  1.00 32.48  ? 12  LYS   B CD  1 
ATOM   2479 C  CE  . LYS   B 1 12  ? 13.781  -4.256  -1.832  1.00 37.94  ? 12  LYS   B CE  1 
ATOM   2480 N  NZ  . LYS   B 1 12  ? 14.671  -4.440  -2.977  1.00 38.29  ? 12  LYS   B NZ  1 
ATOM   2481 N  N   . VAL   B 1 13  ? 8.048   -8.337  -3.123  1.00 29.31  ? 13  VAL   B N   1 
ATOM   2482 C  CA  . VAL   B 1 13  ? 6.740   -8.752  -2.648  1.00 26.93  ? 13  VAL   B CA  1 
ATOM   2483 C  C   . VAL   B 1 13  ? 6.468   -10.201 -3.048  1.00 28.96  ? 13  VAL   B C   1 
ATOM   2484 O  O   . VAL   B 1 13  ? 5.892   -10.940 -2.261  1.00 26.58  ? 13  VAL   B O   1 
ATOM   2485 C  CB  . VAL   B 1 13  ? 5.666   -7.805  -3.185  1.00 25.11  ? 13  VAL   B CB  1 
ATOM   2486 C  CG1 . VAL   B 1 13  ? 4.281   -8.200  -2.688  1.00 26.83  ? 13  VAL   B CG1 1 
ATOM   2487 C  CG2 . VAL   B 1 13  ? 6.004   -6.359  -2.844  1.00 25.32  ? 13  VAL   B CG2 1 
ATOM   2488 N  N   . GLU   B 1 14  ? 6.877   -10.614 -4.255  1.00 26.97  ? 14  GLU   B N   1 
ATOM   2489 C  CA  . GLU   B 1 14  ? 6.703   -11.998 -4.676  1.00 27.71  ? 14  GLU   B CA  1 
ATOM   2490 C  C   . GLU   B 1 14  ? 7.191   -12.965 -3.591  1.00 28.38  ? 14  GLU   B C   1 
ATOM   2491 O  O   . GLU   B 1 14  ? 6.559   -13.980 -3.354  1.00 28.63  ? 14  GLU   B O   1 
ATOM   2492 C  CB  . GLU   B 1 14  ? 7.462   -12.303 -5.972  1.00 28.16  ? 14  GLU   B CB  1 
ATOM   2493 C  CG  . GLU   B 1 14  ? 6.792   -11.779 -7.239  1.00 29.68  ? 14  GLU   B CG  1 
ATOM   2494 C  CD  . GLU   B 1 14  ? 7.699   -11.776 -8.463  1.00 29.81  ? 14  GLU   B CD  1 
ATOM   2495 O  OE1 . GLU   B 1 14  ? 8.139   -12.877 -8.860  1.00 30.66  ? 14  GLU   B OE1 1 
ATOM   2496 O  OE2 . GLU   B 1 14  ? 7.953   -10.697 -9.043  1.00 28.39  ? 14  GLU   B OE2 1 
ATOM   2497 N  N   . GLY   B 1 15  ? 8.291   -12.633 -2.906  1.00 30.91  ? 15  GLY   B N   1 
ATOM   2498 C  CA  . GLY   B 1 15  ? 8.870   -13.478 -1.871  1.00 30.16  ? 15  GLY   B CA  1 
ATOM   2499 C  C   . GLY   B 1 15  ? 8.032   -13.586 -0.593  1.00 30.42  ? 15  GLY   B C   1 
ATOM   2500 O  O   . GLY   B 1 15  ? 8.409   -14.332 0.302   1.00 28.67  ? 15  GLY   B O   1 
ATOM   2501 N  N   . CYS   B 1 16  ? 6.901   -12.870 -0.493  1.00 29.01  ? 16  CYS   B N   1 
ATOM   2502 C  CA  . CYS   B 1 16  ? 6.117   -12.846 0.736   1.00 27.57  ? 16  CYS   B CA  1 
ATOM   2503 C  C   . CYS   B 1 16  ? 4.762   -13.538 0.591   1.00 24.94  ? 16  CYS   B C   1 
ATOM   2504 O  O   . CYS   B 1 16  ? 4.002   -13.588 1.555   1.00 29.16  ? 16  CYS   B O   1 
ATOM   2505 C  CB  . CYS   B 1 16  ? 5.872   -11.415 1.215   1.00 27.97  ? 16  CYS   B CB  1 
ATOM   2506 S  SG  . CYS   B 1 16  ? 7.396   -10.479 1.529   1.00 26.31  ? 16  CYS   B SG  1 
ATOM   2507 N  N   . MET   B 1 17  ? 4.417   -14.060 -0.596  1.00 25.81  ? 17  MET   B N   1 
ATOM   2508 C  CA  . MET   B 1 17  ? 3.050   -14.512 -0.813  1.00 24.84  ? 17  MET   B CA  1 
ATOM   2509 C  C   . MET   B 1 17  ? 2.920   -16.007 -0.468  1.00 26.26  ? 17  MET   B C   1 
ATOM   2510 O  O   . MET   B 1 17  ? 3.763   -16.796 -0.846  1.00 25.54  ? 17  MET   B O   1 
ATOM   2511 C  CB  . MET   B 1 17  ? 2.607   -14.310 -2.263  1.00 24.85  ? 17  MET   B CB  1 
ATOM   2512 C  CG  . MET   B 1 17  ? 2.659   -12.882 -2.766  1.00 26.31  ? 17  MET   B CG  1 
ATOM   2513 S  SD  . MET   B 1 17  ? 1.785   -11.704 -1.722  1.00 24.30  ? 17  MET   B SD  1 
ATOM   2514 C  CE  . MET   B 1 17  ? 0.097   -12.332 -1.691  1.00 24.96  ? 17  MET   B CE  1 
ATOM   2515 N  N   . VAL   B 1 18  ? 1.829   -16.374 0.211   1.00 26.91  ? 18  VAL   B N   1 
ATOM   2516 C  CA  . VAL   B 1 18  ? 1.517   -17.749 0.575   1.00 28.78  ? 18  VAL   B CA  1 
ATOM   2517 C  C   . VAL   B 1 18  ? 0.040   -18.047 0.290   1.00 29.51  ? 18  VAL   B C   1 
ATOM   2518 O  O   . VAL   B 1 18  ? -0.767  -17.149 0.054   1.00 31.97  ? 18  VAL   B O   1 
ATOM   2519 C  CB  . VAL   B 1 18  ? 1.873   -18.005 2.061   1.00 28.43  ? 18  VAL   B CB  1 
ATOM   2520 C  CG1 . VAL   B 1 18  ? 3.348   -17.768 2.359   1.00 29.87  ? 18  VAL   B CG1 1 
ATOM   2521 C  CG2 . VAL   B 1 18  ? 1.028   -17.190 3.038   1.00 29.61  ? 18  VAL   B CG2 1 
ATOM   2522 N  N   . GLN   B 1 19  ? -0.322  -19.335 0.367   1.00 32.19  ? 19  GLN   B N   1 
ATOM   2523 C  CA  . GLN   B 1 19  ? -1.701  -19.804 0.308   1.00 33.65  ? 19  GLN   B CA  1 
ATOM   2524 C  C   . GLN   B 1 19  ? -2.244  -20.085 1.710   1.00 31.44  ? 19  GLN   B C   1 
ATOM   2525 O  O   . GLN   B 1 19  ? -1.549  -20.685 2.522   1.00 34.69  ? 19  GLN   B O   1 
ATOM   2526 C  CB  . GLN   B 1 19  ? -1.693  -21.117 -0.473  1.00 40.86  ? 19  GLN   B CB  1 
ATOM   2527 C  CG  . GLN   B 1 19  ? -3.072  -21.745 -0.624  1.00 47.76  ? 19  GLN   B CG  1 
ATOM   2528 C  CD  . GLN   B 1 19  ? -3.063  -22.973 -1.510  1.00 50.63  ? 19  GLN   B CD  1 
ATOM   2529 O  OE1 . GLN   B 1 19  ? -3.739  -23.015 -2.546  1.00 51.61  ? 19  GLN   B OE1 1 
ATOM   2530 N  NE2 . GLN   B 1 19  ? -2.295  -23.977 -1.105  1.00 46.13  ? 19  GLN   B NE2 1 
ATOM   2531 N  N   . VAL   B 1 20  ? -3.510  -19.721 1.955   1.00 30.44  ? 20  VAL   B N   1 
ATOM   2532 C  CA  . VAL   B 1 20  ? -4.191  -19.956 3.218   1.00 31.90  ? 20  VAL   B CA  1 
ATOM   2533 C  C   . VAL   B 1 20  ? -5.527  -20.673 2.980   1.00 36.74  ? 20  VAL   B C   1 
ATOM   2534 O  O   . VAL   B 1 20  ? -6.304  -20.278 2.118   1.00 38.48  ? 20  VAL   B O   1 
ATOM   2535 C  CB  . VAL   B 1 20  ? -4.407  -18.608 3.937   1.00 33.27  ? 20  VAL   B CB  1 
ATOM   2536 C  CG1 . VAL   B 1 20  ? -5.154  -18.791 5.253   1.00 32.89  ? 20  VAL   B CG1 1 
ATOM   2537 C  CG2 . VAL   B 1 20  ? -3.091  -17.859 4.159   1.00 32.16  ? 20  VAL   B CG2 1 
ATOM   2538 N  N   . THR   B 1 21  ? -5.803  -21.726 3.771   1.00 39.03  ? 21  THR   B N   1 
ATOM   2539 C  CA  . THR   B 1 21  ? -7.024  -22.516 3.645   1.00 39.81  ? 21  THR   B CA  1 
ATOM   2540 C  C   . THR   B 1 21  ? -7.678  -22.701 5.019   1.00 41.46  ? 21  THR   B C   1 
ATOM   2541 O  O   . THR   B 1 21  ? -7.011  -23.018 6.003   1.00 44.72  ? 21  THR   B O   1 
ATOM   2542 C  CB  . THR   B 1 21  ? -6.746  -23.888 3.023   1.00 38.04  ? 21  THR   B CB  1 
ATOM   2543 O  OG1 . THR   B 1 21  ? -6.157  -23.798 1.727   1.00 31.95  ? 21  THR   B OG1 1 
ATOM   2544 C  CG2 . THR   B 1 21  ? -8.030  -24.683 2.869   1.00 38.34  ? 21  THR   B CG2 1 
ATOM   2545 N  N   . CYS   B 1 22  ? -8.995  -22.485 5.067   1.00 43.64  ? 22  CYS   B N   1 
ATOM   2546 C  CA  . CYS   B 1 22  ? -9.823  -22.712 6.246   1.00 44.88  ? 22  CYS   B CA  1 
ATOM   2547 C  C   . CYS   B 1 22  ? -11.095 -23.378 5.735   1.00 46.57  ? 22  CYS   B C   1 
ATOM   2548 O  O   . CYS   B 1 22  ? -11.884 -22.740 5.042   1.00 45.37  ? 22  CYS   B O   1 
ATOM   2549 C  CB  . CYS   B 1 22  ? -10.116 -21.398 6.969   1.00 44.73  ? 22  CYS   B CB  1 
ATOM   2550 S  SG  . CYS   B 1 22  ? -10.934 -21.546 8.582   1.00 49.24  ? 22  CYS   B SG  1 
ATOM   2551 N  N   . GLY   B 1 23  ? -11.246 -24.679 6.007   1.00 49.28  ? 23  GLY   B N   1 
ATOM   2552 C  CA  . GLY   B 1 23  ? -12.341 -25.458 5.445   1.00 45.38  ? 23  GLY   B CA  1 
ATOM   2553 C  C   . GLY   B 1 23  ? -12.166 -25.635 3.941   1.00 41.82  ? 23  GLY   B C   1 
ATOM   2554 O  O   . GLY   B 1 23  ? -11.124 -26.099 3.489   1.00 44.50  ? 23  GLY   B O   1 
ATOM   2555 N  N   . THR   B 1 24  ? -13.171 -25.204 3.173   1.00 42.22  ? 24  THR   B N   1 
ATOM   2556 C  CA  . THR   B 1 24  ? -13.133 -25.309 1.721   1.00 44.94  ? 24  THR   B CA  1 
ATOM   2557 C  C   . THR   B 1 24  ? -12.629 -24.016 1.079   1.00 45.26  ? 24  THR   B C   1 
ATOM   2558 O  O   . THR   B 1 24  ? -12.425 -24.017 -0.132  1.00 52.77  ? 24  THR   B O   1 
ATOM   2559 C  CB  . THR   B 1 24  ? -14.502 -25.661 1.123   1.00 44.23  ? 24  THR   B CB  1 
ATOM   2560 O  OG1 . THR   B 1 24  ? -15.475 -24.912 1.850   1.00 41.64  ? 24  THR   B OG1 1 
ATOM   2561 C  CG2 . THR   B 1 24  ? -14.784 -27.154 1.148   1.00 46.48  ? 24  THR   B CG2 1 
ATOM   2562 N  N   . THR   B 1 25  ? -12.451 -22.925 1.837   1.00 44.19  ? 25  THR   B N   1 
ATOM   2563 C  CA  . THR   B 1 25  ? -11.958 -21.686 1.243   1.00 42.53  ? 25  THR   B CA  1 
ATOM   2564 C  C   . THR   B 1 25  ? -10.433 -21.709 1.180   1.00 41.95  ? 25  THR   B C   1 
ATOM   2565 O  O   . THR   B 1 25  ? -9.784  -21.940 2.197   1.00 44.66  ? 25  THR   B O   1 
ATOM   2566 C  CB  . THR   B 1 25  ? -12.410 -20.456 2.030   1.00 46.79  ? 25  THR   B CB  1 
ATOM   2567 O  OG1 . THR   B 1 25  ? -13.783 -20.625 2.356   1.00 44.09  ? 25  THR   B OG1 1 
ATOM   2568 C  CG2 . THR   B 1 25  ? -12.227 -19.169 1.241   1.00 44.72  ? 25  THR   B CG2 1 
ATOM   2569 N  N   . THR   B 1 26  ? -9.879  -21.449 -0.017  1.00 42.74  ? 26  THR   B N   1 
ATOM   2570 C  CA  . THR   B 1 26  ? -8.487  -21.047 -0.174  1.00 42.16  ? 26  THR   B CA  1 
ATOM   2571 C  C   . THR   B 1 26  ? -8.402  -19.620 -0.738  1.00 39.14  ? 26  THR   B C   1 
ATOM   2572 O  O   . THR   B 1 26  ? -9.190  -19.254 -1.599  1.00 36.51  ? 26  THR   B O   1 
ATOM   2573 C  CB  . THR   B 1 26  ? -7.809  -22.071 -1.079  1.00 41.73  ? 26  THR   B CB  1 
ATOM   2574 O  OG1 . THR   B 1 26  ? -7.856  -23.226 -0.249  1.00 47.42  ? 26  THR   B OG1 1 
ATOM   2575 C  CG2 . THR   B 1 26  ? -6.358  -21.755 -1.395  1.00 41.23  ? 26  THR   B CG2 1 
ATOM   2576 N  N   . LEU   B 1 27  ? -7.409  -18.843 -0.271  1.00 34.13  ? 27  LEU   B N   1 
ATOM   2577 C  CA  . LEU   B 1 27  ? -7.046  -17.556 -0.849  1.00 34.03  ? 27  LEU   B CA  1 
ATOM   2578 C  C   . LEU   B 1 27  ? -5.588  -17.233 -0.490  1.00 33.09  ? 27  LEU   B C   1 
ATOM   2579 O  O   . LEU   B 1 27  ? -4.852  -18.126 -0.071  1.00 30.63  ? 27  LEU   B O   1 
ATOM   2580 C  CB  . LEU   B 1 27  ? -8.040  -16.490 -0.382  1.00 32.64  ? 27  LEU   B CB  1 
ATOM   2581 C  CG  . LEU   B 1 27  ? -8.406  -16.510 1.111   1.00 31.09  ? 27  LEU   B CG  1 
ATOM   2582 C  CD1 . LEU   B 1 27  ? -7.268  -16.202 2.049   1.00 29.22  ? 27  LEU   B CD1 1 
ATOM   2583 C  CD2 . LEU   B 1 27  ? -9.550  -15.572 1.356   1.00 31.40  ? 27  LEU   B CD2 1 
ATOM   2584 N  N   . ASN   B 1 28  ? -5.170  -15.964 -0.661  1.00 27.40  ? 28  ASN   B N   1 
ATOM   2585 C  CA  . ASN   B 1 28  ? -3.760  -15.585 -0.579  1.00 25.31  ? 28  ASN   B CA  1 
ATOM   2586 C  C   . ASN   B 1 28  ? -3.457  -14.934 0.768   1.00 24.70  ? 28  ASN   B C   1 
ATOM   2587 O  O   . ASN   B 1 28  ? -4.323  -14.321 1.377   1.00 28.01  ? 28  ASN   B O   1 
ATOM   2588 C  CB  . ASN   B 1 28  ? -3.358  -14.656 -1.721  1.00 25.45  ? 28  ASN   B CB  1 
ATOM   2589 C  CG  . ASN   B 1 28  ? -3.658  -15.230 -3.090  1.00 24.31  ? 28  ASN   B CG  1 
ATOM   2590 O  OD1 . ASN   B 1 28  ? -2.855  -15.980 -3.643  1.00 23.36  ? 28  ASN   B OD1 1 
ATOM   2591 N  ND2 . ASN   B 1 28  ? -4.788  -14.859 -3.677  1.00 26.65  ? 28  ASN   B ND2 1 
ATOM   2592 N  N   . GLY   B 1 29  ? -2.203  -15.028 1.223   1.00 24.38  ? 29  GLY   B N   1 
ATOM   2593 C  CA  . GLY   B 1 29  ? -1.794  -14.333 2.431   1.00 24.27  ? 29  GLY   B CA  1 
ATOM   2594 C  C   . GLY   B 1 29  ? -0.437  -13.647 2.261   1.00 23.61  ? 29  GLY   B C   1 
ATOM   2595 O  O   . GLY   B 1 29  ? 0.324   -14.003 1.363   1.00 22.28  ? 29  GLY   B O   1 
ATOM   2596 N  N   . LEU   B 1 30  ? -0.133  -12.698 3.159   1.00 22.56  ? 30  LEU   B N   1 
ATOM   2597 C  CA  . LEU   B 1 30  ? 1.129   -11.963 3.138   1.00 24.54  ? 30  LEU   B CA  1 
ATOM   2598 C  C   . LEU   B 1 30  ? 1.949   -12.371 4.368   1.00 25.30  ? 30  LEU   B C   1 
ATOM   2599 O  O   . LEU   B 1 30  ? 1.501   -12.169 5.494   1.00 25.42  ? 30  LEU   B O   1 
ATOM   2600 C  CB  . LEU   B 1 30  ? 0.804   -10.454 3.102   1.00 23.66  ? 30  LEU   B CB  1 
ATOM   2601 C  CG  . LEU   B 1 30  ? 1.977   -9.464  2.952   1.00 22.61  ? 30  LEU   B CG  1 
ATOM   2602 C  CD1 . LEU   B 1 30  ? 2.681   -9.540  1.582   1.00 22.54  ? 30  LEU   B CD1 1 
ATOM   2603 C  CD2 . LEU   B 1 30  ? 1.601   -8.013  3.191   1.00 21.19  ? 30  LEU   B CD2 1 
ATOM   2604 N  N   . TRP   B 1 31  ? 3.149   -12.951 4.142   1.00 28.58  ? 31  TRP   B N   1 
ATOM   2605 C  CA  . TRP   B 1 31  ? 4.020   -13.494 5.187   1.00 27.42  ? 31  TRP   B CA  1 
ATOM   2606 C  C   . TRP   B 1 31  ? 5.208   -12.557 5.442   1.00 27.15  ? 31  TRP   B C   1 
ATOM   2607 O  O   . TRP   B 1 31  ? 6.130   -12.483 4.642   1.00 27.53  ? 31  TRP   B O   1 
ATOM   2608 C  CB  . TRP   B 1 31  ? 4.514   -14.892 4.760   1.00 27.88  ? 31  TRP   B CB  1 
ATOM   2609 C  CG  . TRP   B 1 31  ? 5.402   -15.614 5.748   1.00 31.97  ? 31  TRP   B CG  1 
ATOM   2610 C  CD1 . TRP   B 1 31  ? 5.495   -15.420 7.102   1.00 36.96  ? 31  TRP   B CD1 1 
ATOM   2611 C  CD2 . TRP   B 1 31  ? 6.311   -16.694 5.454   1.00 33.92  ? 31  TRP   B CD2 1 
ATOM   2612 N  NE1 . TRP   B 1 31  ? 6.406   -16.278 7.665   1.00 32.72  ? 31  TRP   B NE1 1 
ATOM   2613 C  CE2 . TRP   B 1 31  ? 6.924   -17.067 6.673   1.00 36.07  ? 31  TRP   B CE2 1 
ATOM   2614 C  CE3 . TRP   B 1 31  ? 6.681   -17.357 4.277   1.00 32.85  ? 31  TRP   B CE3 1 
ATOM   2615 C  CZ2 . TRP   B 1 31  ? 7.879   -18.075 6.741   1.00 35.36  ? 31  TRP   B CZ2 1 
ATOM   2616 C  CZ3 . TRP   B 1 31  ? 7.628   -18.345 4.348   1.00 33.57  ? 31  TRP   B CZ3 1 
ATOM   2617 C  CH2 . TRP   B 1 31  ? 8.211   -18.705 5.566   1.00 35.64  ? 31  TRP   B CH2 1 
ATOM   2618 N  N   . LEU   B 1 32  ? 5.213   -11.890 6.594   1.00 28.01  ? 32  LEU   B N   1 
ATOM   2619 C  CA  . LEU   B 1 32  ? 6.238   -10.933 6.982   1.00 28.40  ? 32  LEU   B CA  1 
ATOM   2620 C  C   . LEU   B 1 32  ? 6.627   -11.209 8.430   1.00 25.92  ? 32  LEU   B C   1 
ATOM   2621 O  O   . LEU   B 1 32  ? 5.763   -11.305 9.283   1.00 26.91  ? 32  LEU   B O   1 
ATOM   2622 C  CB  . LEU   B 1 32  ? 5.703   -9.502  6.883   1.00 28.13  ? 32  LEU   B CB  1 
ATOM   2623 C  CG  . LEU   B 1 32  ? 5.214   -9.045  5.505   1.00 28.57  ? 32  LEU   B CG  1 
ATOM   2624 C  CD1 . LEU   B 1 32  ? 4.323   -7.819  5.612   1.00 25.94  ? 32  LEU   B CD1 1 
ATOM   2625 C  CD2 . LEU   B 1 32  ? 6.408   -8.802  4.612   1.00 27.46  ? 32  LEU   B CD2 1 
ATOM   2626 N  N   . ASP   B 1 33  ? 7.931   -11.239 8.706   1.00 25.94  ? 33  ASP   B N   1 
ATOM   2627 C  CA  . ASP   B 1 33  ? 8.420   -11.626 10.015  1.00 27.84  ? 33  ASP   B CA  1 
ATOM   2628 C  C   . ASP   B 1 33  ? 7.771   -12.984 10.326  1.00 28.88  ? 33  ASP   B C   1 
ATOM   2629 O  O   . ASP   B 1 33  ? 7.733   -13.852 9.452   1.00 27.74  ? 33  ASP   B O   1 
ATOM   2630 C  CB  . ASP   B 1 33  ? 8.265   -10.467 10.988  1.00 28.07  ? 33  ASP   B CB  1 
ATOM   2631 C  CG  . ASP   B 1 33  ? 8.871   -9.136  10.564  1.00 28.73  ? 33  ASP   B CG  1 
ATOM   2632 O  OD1 . ASP   B 1 33  ? 10.103  -9.071  10.401  1.00 31.75  ? 33  ASP   B OD1 1 
ATOM   2633 O  OD2 . ASP   B 1 33  ? 8.110   -8.156  10.438  1.00 33.98  ? 33  ASP   B OD2 1 
ATOM   2634 N  N   . ASP   B 1 34  ? 7.184   -13.161 11.519  1.00 29.49  ? 34  ASP   B N   1 
ATOM   2635 C  CA  . ASP   B 1 34  ? 6.560   -14.436 11.859  1.00 33.22  ? 34  ASP   B CA  1 
ATOM   2636 C  C   . ASP   B 1 34  ? 5.018   -14.378 11.880  1.00 30.53  ? 34  ASP   B C   1 
ATOM   2637 O  O   . ASP   B 1 34  ? 4.399   -15.156 12.619  1.00 32.43  ? 34  ASP   B O   1 
ATOM   2638 C  CB  . ASP   B 1 34  ? 7.158   -14.952 13.164  1.00 36.01  ? 34  ASP   B CB  1 
ATOM   2639 C  CG  . ASP   B 1 34  ? 6.848   -14.112 14.393  1.00 38.92  ? 34  ASP   B CG  1 
ATOM   2640 O  OD1 . ASP   B 1 34  ? 6.347   -12.976 14.232  1.00 37.55  ? 34  ASP   B OD1 1 
ATOM   2641 O  OD2 . ASP   B 1 34  ? 7.096   -14.603 15.503  1.00 40.63  ? 34  ASP   B OD2 1 
ATOM   2642 N  N   . VAL   B 1 35  ? 4.392   -13.506 11.061  1.00 28.42  ? 35  VAL   B N   1 
ATOM   2643 C  CA  . VAL   B 1 35  ? 2.932   -13.404 10.965  1.00 25.35  ? 35  VAL   B CA  1 
ATOM   2644 C  C   . VAL   B 1 35  ? 2.463   -13.516 9.509   1.00 27.09  ? 35  VAL   B C   1 
ATOM   2645 O  O   . VAL   B 1 35  ? 3.152   -13.040 8.601   1.00 26.01  ? 35  VAL   B O   1 
ATOM   2646 C  CB  . VAL   B 1 35  ? 2.455   -12.062 11.558  1.00 27.29  ? 35  VAL   B CB  1 
ATOM   2647 C  CG1 . VAL   B 1 35  ? 0.958   -11.869 11.360  1.00 25.83  ? 35  VAL   B CG1 1 
ATOM   2648 C  CG2 . VAL   B 1 35  ? 2.824   -11.901 13.030  1.00 27.94  ? 35  VAL   B CG2 1 
ATOM   2649 N  N   . VAL   B 1 36  ? 1.269   -14.110 9.295   1.00 25.95  ? 36  VAL   B N   1 
ATOM   2650 C  CA  . VAL   B 1 36  ? 0.625   -14.180 7.986   1.00 28.25  ? 36  VAL   B CA  1 
ATOM   2651 C  C   . VAL   B 1 36  ? -0.697  -13.400 8.057   1.00 29.66  ? 36  VAL   B C   1 
ATOM   2652 O  O   . VAL   B 1 36  ? -1.482  -13.674 8.969   1.00 26.67  ? 36  VAL   B O   1 
ATOM   2653 C  CB  . VAL   B 1 36  ? 0.402   -15.638 7.524   1.00 28.48  ? 36  VAL   B CB  1 
ATOM   2654 C  CG1 . VAL   B 1 36  ? -0.346  -15.707 6.192   1.00 27.68  ? 36  VAL   B CG1 1 
ATOM   2655 C  CG2 . VAL   B 1 36  ? 1.714   -16.405 7.429   1.00 26.10  ? 36  VAL   B CG2 1 
ATOM   2656 N  N   . TYR   B 1 37  ? -0.901  -12.429 7.123   1.00 28.29  ? 37  TYR   B N   1 
ATOM   2657 C  CA  . TYR   B 1 37  ? -2.053  -11.525 7.076   1.00 25.95  ? 37  TYR   B CA  1 
ATOM   2658 C  C   . TYR   B 1 37  ? -2.983  -11.918 5.929   1.00 25.61  ? 37  TYR   B C   1 
ATOM   2659 O  O   . TYR   B 1 37  ? -2.502  -12.133 4.825   1.00 28.73  ? 37  TYR   B O   1 
ATOM   2660 C  CB  . TYR   B 1 37  ? -1.627  -10.053 6.868   1.00 23.73  ? 37  TYR   B CB  1 
ATOM   2661 C  CG  . TYR   B 1 37  ? -0.676  -9.531  7.932   1.00 23.83  ? 37  TYR   B CG  1 
ATOM   2662 C  CD1 . TYR   B 1 37  ? 0.667   -9.858  7.899   1.00 29.14  ? 37  TYR   B CD1 1 
ATOM   2663 C  CD2 . TYR   B 1 37  ? -1.119  -8.787  9.017   1.00 23.97  ? 37  TYR   B CD2 1 
ATOM   2664 C  CE1 . TYR   B 1 37  ? 1.543   -9.425  8.882   1.00 29.58  ? 37  TYR   B CE1 1 
ATOM   2665 C  CE2 . TYR   B 1 37  ? -0.255  -8.316  9.991   1.00 25.08  ? 37  TYR   B CE2 1 
ATOM   2666 C  CZ  . TYR   B 1 37  ? 1.086   -8.650  9.935   1.00 27.93  ? 37  TYR   B CZ  1 
ATOM   2667 O  OH  . TYR   B 1 37  ? 1.982   -8.253  10.884  1.00 28.18  ? 37  TYR   B OH  1 
ATOM   2668 N  N   . CYS   B 1 38  ? -4.307  -12.003 6.165   1.00 24.63  ? 38  CYS   B N   1 
ATOM   2669 C  CA  . CYS   B 1 38  ? -5.265  -12.349 5.117   1.00 23.36  ? 38  CYS   B CA  1 
ATOM   2670 C  C   . CYS   B 1 38  ? -6.647  -11.810 5.483   1.00 23.30  ? 38  CYS   B C   1 
ATOM   2671 O  O   . CYS   B 1 38  ? -6.860  -11.365 6.607   1.00 24.06  ? 38  CYS   B O   1 
ATOM   2672 C  CB  . CYS   B 1 38  ? -5.298  -13.857 4.867   1.00 28.69  ? 38  CYS   B CB  1 
ATOM   2673 S  SG  . CYS   B 1 38  ? -6.188  -14.842 6.120   1.00 28.93  ? 38  CYS   B SG  1 
ATOM   2674 N  N   . PRO   B 1 39  ? -7.634  -11.753 4.555   1.00 23.35  ? 39  PRO   B N   1 
ATOM   2675 C  CA  . PRO   B 1 39  ? -8.973  -11.274 4.900   1.00 24.99  ? 39  PRO   B CA  1 
ATOM   2676 C  C   . PRO   B 1 39  ? -9.669  -12.170 5.925   1.00 27.29  ? 39  PRO   B C   1 
ATOM   2677 O  O   . PRO   B 1 39  ? -9.593  -13.394 5.816   1.00 25.93  ? 39  PRO   B O   1 
ATOM   2678 C  CB  . PRO   B 1 39  ? -9.695  -11.281 3.546   1.00 26.28  ? 39  PRO   B CB  1 
ATOM   2679 C  CG  . PRO   B 1 39  ? -8.579  -11.245 2.503   1.00 24.61  ? 39  PRO   B CG  1 
ATOM   2680 C  CD  . PRO   B 1 39  ? -7.515  -12.094 3.130   1.00 23.99  ? 39  PRO   B CD  1 
ATOM   2681 N  N   . ARG   B 1 40  ? -10.355 -11.552 6.899   1.00 26.22  ? 40  ARG   B N   1 
ATOM   2682 C  CA  . ARG   B 1 40  ? -11.005 -12.316 7.951   1.00 30.55  ? 40  ARG   B CA  1 
ATOM   2683 C  C   . ARG   B 1 40  ? -12.133 -13.174 7.368   1.00 33.21  ? 40  ARG   B C   1 
ATOM   2684 O  O   . ARG   B 1 40  ? -12.525 -14.162 7.991   1.00 36.08  ? 40  ARG   B O   1 
ATOM   2685 C  CB  . ARG   B 1 40  ? -11.504 -11.438 9.109   1.00 30.89  ? 40  ARG   B CB  1 
ATOM   2686 C  CG  . ARG   B 1 40  ? -12.690 -10.517 8.836   1.00 31.89  ? 40  ARG   B CG  1 
ATOM   2687 C  CD  . ARG   B 1 40  ? -13.191 -9.813  10.086  1.00 31.70  ? 40  ARG   B CD  1 
ATOM   2688 N  NE  . ARG   B 1 40  ? -14.218 -8.809  9.809   1.00 30.36  ? 40  ARG   B NE  1 
ATOM   2689 C  CZ  . ARG   B 1 40  ? -14.909 -8.127  10.718  1.00 32.96  ? 40  ARG   B CZ  1 
ATOM   2690 N  NH1 . ARG   B 1 40  ? -14.674 -8.270  12.009  1.00 34.22  ? 40  ARG   B NH1 1 
ATOM   2691 N  NH2 . ARG   B 1 40  ? -15.848 -7.280  10.332  1.00 31.71  ? 40  ARG   B NH2 1 
ATOM   2692 N  N   . HIS   B 1 41  ? -12.617 -12.858 6.154   1.00 30.55  ? 41  HIS   B N   1 
ATOM   2693 C  CA  . HIS   B 1 41  ? -13.741 -13.600 5.605   1.00 31.24  ? 41  HIS   B CA  1 
ATOM   2694 C  C   . HIS   B 1 41  ? -13.378 -15.048 5.249   1.00 33.15  ? 41  HIS   B C   1 
ATOM   2695 O  O   . HIS   B 1 41  ? -14.283 -15.826 4.972   1.00 33.42  ? 41  HIS   B O   1 
ATOM   2696 C  CB  . HIS   B 1 41  ? -14.486 -12.811 4.521   1.00 30.92  ? 41  HIS   B CB  1 
ATOM   2697 C  CG  . HIS   B 1 41  ? -13.855 -12.656 3.174   1.00 29.69  ? 41  HIS   B CG  1 
ATOM   2698 N  ND1 . HIS   B 1 41  ? -13.369 -13.687 2.398   1.00 33.65  ? 41  HIS   B ND1 1 
ATOM   2699 C  CD2 . HIS   B 1 41  ? -13.731 -11.537 2.432   1.00 32.17  ? 41  HIS   B CD2 1 
ATOM   2700 C  CE1 . HIS   B 1 41  ? -12.948 -13.203 1.228   1.00 33.68  ? 41  HIS   B CE1 1 
ATOM   2701 N  NE2 . HIS   B 1 41  ? -13.163 -11.896 1.225   1.00 34.81  ? 41  HIS   B NE2 1 
ATOM   2702 N  N   . VAL   B 1 42  ? -12.099 -15.429 5.317   1.00 31.79  ? 42  VAL   B N   1 
ATOM   2703 C  CA  . VAL   B 1 42  ? -11.657 -16.792 5.035   1.00 35.46  ? 42  VAL   B CA  1 
ATOM   2704 C  C   . VAL   B 1 42  ? -12.345 -17.803 5.965   1.00 43.42  ? 42  VAL   B C   1 
ATOM   2705 O  O   . VAL   B 1 42  ? -12.414 -18.983 5.613   1.00 48.70  ? 42  VAL   B O   1 
ATOM   2706 C  CB  . VAL   B 1 42  ? -10.121 -16.933 5.133   1.00 32.19  ? 42  VAL   B CB  1 
ATOM   2707 C  CG1 . VAL   B 1 42  ? -9.587  -16.760 6.546   1.00 29.26  ? 42  VAL   B CG1 1 
ATOM   2708 C  CG2 . VAL   B 1 42  ? -9.592  -18.253 4.562   1.00 33.60  ? 42  VAL   B CG2 1 
ATOM   2709 N  N   . ILE   B 1 43  ? -12.811 -17.359 7.148   1.00 42.02  ? 43  ILE   B N   1 
ATOM   2710 C  CA  . ILE   B 1 43  ? -13.410 -18.256 8.135   1.00 44.01  ? 43  ILE   B CA  1 
ATOM   2711 C  C   . ILE   B 1 43  ? -14.903 -18.491 7.873   1.00 44.60  ? 43  ILE   B C   1 
ATOM   2712 O  O   . ILE   B 1 43  ? -15.513 -19.210 8.648   1.00 47.97  ? 43  ILE   B O   1 
ATOM   2713 C  CB  . ILE   B 1 43  ? -13.211 -17.765 9.590   1.00 37.49  ? 43  ILE   B CB  1 
ATOM   2714 C  CG1 . ILE   B 1 43  ? -14.152 -16.606 9.954   1.00 33.86  ? 43  ILE   B CG1 1 
ATOM   2715 C  CG2 . ILE   B 1 43  ? -11.745 -17.450 9.878   1.00 40.50  ? 43  ILE   B CG2 1 
ATOM   2716 C  CD1 . ILE   B 1 43  ? -13.927 -16.003 11.334  1.00 34.58  ? 43  ILE   B CD1 1 
ATOM   2717 N  N   . CYS   B 1 44  ? -15.501 -17.891 6.834   1.00 46.75  ? 44  CYS   B N   1 
ATOM   2718 C  CA  . CYS   B 1 44  ? -16.952 -17.867 6.667   1.00 42.33  ? 44  CYS   B CA  1 
ATOM   2719 C  C   . CYS   B 1 44  ? -17.436 -18.880 5.630   1.00 47.27  ? 44  CYS   B C   1 
ATOM   2720 O  O   . CYS   B 1 44  ? -16.870 -18.959 4.548   1.00 47.54  ? 44  CYS   B O   1 
ATOM   2721 C  CB  . CYS   B 1 44  ? -17.412 -16.487 6.224   1.00 36.66  ? 44  CYS   B CB  1 
ATOM   2722 S  SG  . CYS   B 1 44  ? -17.324 -15.275 7.568   1.00 40.28  ? 44  CYS   B SG  1 
ATOM   2723 N  N   . THR   B 1 45  ? -18.509 -19.626 5.950   1.00 47.84  ? 45  THR   B N   1 
ATOM   2724 C  CA  . THR   B 1 45  ? -19.220 -20.392 4.934   1.00 53.10  ? 45  THR   B CA  1 
ATOM   2725 C  C   . THR   B 1 45  ? -20.058 -19.405 4.129   1.00 49.43  ? 45  THR   B C   1 
ATOM   2726 O  O   . THR   B 1 45  ? -20.222 -18.261 4.547   1.00 49.40  ? 45  THR   B O   1 
ATOM   2727 C  CB  . THR   B 1 45  ? -20.102 -21.492 5.540   1.00 51.19  ? 45  THR   B CB  1 
ATOM   2728 O  OG1 . THR   B 1 45  ? -21.106 -20.814 6.296   1.00 50.48  ? 45  THR   B OG1 1 
ATOM   2729 C  CG2 . THR   B 1 45  ? -19.320 -22.467 6.402   1.00 47.26  ? 45  THR   B CG2 1 
ATOM   2730 N  N   . SER   B 1 46  ? -20.561 -19.867 2.976   1.00 54.54  ? 46  SER   B N   1 
ATOM   2731 C  CA  . SER   B 1 46  ? -21.584 -19.172 2.209   1.00 56.66  ? 46  SER   B CA  1 
ATOM   2732 C  C   . SER   B 1 46  ? -22.650 -18.575 3.117   1.00 55.74  ? 46  SER   B C   1 
ATOM   2733 O  O   . SER   B 1 46  ? -22.965 -17.393 3.008   1.00 51.62  ? 46  SER   B O   1 
ATOM   2734 C  CB  . SER   B 1 46  ? -22.242 -20.100 1.243   1.00 61.28  ? 46  SER   B CB  1 
ATOM   2735 O  OG  . SER   B 1 46  ? -21.256 -20.751 0.465   1.00 70.10  ? 46  SER   B OG  1 
ATOM   2736 N  N   . GLU   B 1 47  ? -23.209 -19.421 3.989   1.00 58.95  ? 47  GLU   B N   1 
ATOM   2737 C  CA  . GLU   B 1 47  ? -24.326 -19.029 4.830   1.00 61.34  ? 47  GLU   B CA  1 
ATOM   2738 C  C   . GLU   B 1 47  ? -23.881 -17.983 5.853   1.00 51.55  ? 47  GLU   B C   1 
ATOM   2739 O  O   . GLU   B 1 47  ? -24.631 -17.056 6.161   1.00 47.62  ? 47  GLU   B O   1 
ATOM   2740 C  CB  . GLU   B 1 47  ? -24.934 -20.252 5.514   1.00 67.93  ? 47  GLU   B CB  1 
ATOM   2741 C  CG  . GLU   B 1 47  ? -25.481 -21.282 4.528   1.00 81.28  ? 47  GLU   B CG  1 
ATOM   2742 C  CD  . GLU   B 1 47  ? -26.582 -22.174 5.084   1.00 87.71  ? 47  GLU   B CD  1 
ATOM   2743 O  OE1 . GLU   B 1 47  ? -27.106 -21.871 6.178   1.00 88.03  ? 47  GLU   B OE1 1 
ATOM   2744 O  OE2 . GLU   B 1 47  ? -26.918 -23.181 4.424   1.00 93.37  ? 47  GLU   B OE2 1 
ATOM   2745 N  N   . ASP   B 1 48  ? -22.667 -18.146 6.388   1.00 44.92  ? 48  ASP   B N   1 
ATOM   2746 C  CA  . ASP   B 1 48  ? -22.141 -17.191 7.351   1.00 46.45  ? 48  ASP   B CA  1 
ATOM   2747 C  C   . ASP   B 1 48  ? -22.061 -15.796 6.725   1.00 43.50  ? 48  ASP   B C   1 
ATOM   2748 O  O   . ASP   B 1 48  ? -22.384 -14.813 7.386   1.00 42.29  ? 48  ASP   B O   1 
ATOM   2749 C  CB  . ASP   B 1 48  ? -20.797 -17.633 7.908   1.00 49.15  ? 48  ASP   B CB  1 
ATOM   2750 C  CG  . ASP   B 1 48  ? -20.799 -18.912 8.737   1.00 50.67  ? 48  ASP   B CG  1 
ATOM   2751 O  OD1 . ASP   B 1 48  ? -21.642 -19.017 9.665   1.00 50.97  ? 48  ASP   B OD1 1 
ATOM   2752 O  OD2 . ASP   B 1 48  ? -19.952 -19.789 8.453   1.00 45.90  ? 48  ASP   B OD2 1 
ATOM   2753 N  N   . MET   B 1 49  ? -21.668 -15.727 5.441   1.00 49.36  ? 49  MET   B N   1 
ATOM   2754 C  CA  . MET   B 1 49  ? -21.399 -14.465 4.760   1.00 47.15  ? 49  MET   B CA  1 
ATOM   2755 C  C   . MET   B 1 49  ? -22.660 -13.612 4.662   1.00 46.04  ? 49  MET   B C   1 
ATOM   2756 O  O   . MET   B 1 49  ? -22.561 -12.392 4.524   1.00 41.33  ? 49  MET   B O   1 
ATOM   2757 C  CB  . MET   B 1 49  ? -20.839 -14.659 3.344   1.00 47.96  ? 49  MET   B CB  1 
ATOM   2758 C  CG  . MET   B 1 49  ? -19.331 -14.860 3.268   1.00 52.72  ? 49  MET   B CG  1 
ATOM   2759 S  SD  . MET   B 1 49  ? -18.345 -13.543 4.013   1.00 53.54  ? 49  MET   B SD  1 
ATOM   2760 C  CE  . MET   B 1 49  ? -18.414 -12.169 2.854   1.00 55.41  ? 49  MET   B CE  1 
ATOM   2761 N  N   . LEU   B 1 50  ? -23.840 -14.244 4.711   1.00 44.90  ? 50  LEU   B N   1 
ATOM   2762 C  CA  . LEU   B 1 50  ? -25.074 -13.480 4.635   1.00 48.19  ? 50  LEU   B CA  1 
ATOM   2763 C  C   . LEU   B 1 50  ? -25.107 -12.475 5.787   1.00 45.72  ? 50  LEU   B C   1 
ATOM   2764 O  O   . LEU   B 1 50  ? -25.401 -11.306 5.576   1.00 41.18  ? 50  LEU   B O   1 
ATOM   2765 C  CB  . LEU   B 1 50  ? -26.299 -14.397 4.605   1.00 55.87  ? 50  LEU   B CB  1 
ATOM   2766 C  CG  . LEU   B 1 50  ? -26.659 -15.022 3.246   1.00 62.39  ? 50  LEU   B CG  1 
ATOM   2767 C  CD1 . LEU   B 1 50  ? -25.453 -15.551 2.466   1.00 63.74  ? 50  LEU   B CD1 1 
ATOM   2768 C  CD2 . LEU   B 1 50  ? -27.691 -16.149 3.402   1.00 60.14  ? 50  LEU   B CD2 1 
ATOM   2769 N  N   . ASN   B 1 51  ? -24.768 -12.917 7.003   1.00 48.18  ? 51  ASN   B N   1 
ATOM   2770 C  CA  . ASN   B 1 51  ? -24.842 -12.044 8.169   1.00 46.51  ? 51  ASN   B CA  1 
ATOM   2771 C  C   . ASN   B 1 51  ? -23.864 -12.540 9.242   1.00 40.96  ? 51  ASN   B C   1 
ATOM   2772 O  O   . ASN   B 1 51  ? -24.269 -13.095 10.251  1.00 37.95  ? 51  ASN   B O   1 
ATOM   2773 C  CB  . ASN   B 1 51  ? -26.298 -11.931 8.611   1.00 53.48  ? 51  ASN   B CB  1 
ATOM   2774 C  CG  . ASN   B 1 51  ? -26.561 -10.844 9.630   1.00 56.74  ? 51  ASN   B CG  1 
ATOM   2775 O  OD1 . ASN   B 1 51  ? -27.064 -11.129 10.722  1.00 61.33  ? 51  ASN   B OD1 1 
ATOM   2776 N  ND2 . ASN   B 1 51  ? -26.280 -9.596  9.289   1.00 58.63  ? 51  ASN   B ND2 1 
ATOM   2777 N  N   . PRO   B 1 52  ? -22.534 -12.346 9.084   1.00 39.37  ? 52  PRO   B N   1 
ATOM   2778 C  CA  . PRO   B 1 52  ? -21.543 -12.991 9.958   1.00 35.99  ? 52  PRO   B CA  1 
ATOM   2779 C  C   . PRO   B 1 52  ? -21.331 -12.324 11.315  1.00 35.92  ? 52  PRO   B C   1 
ATOM   2780 O  O   . PRO   B 1 52  ? -21.416 -11.102 11.434  1.00 35.85  ? 52  PRO   B O   1 
ATOM   2781 C  CB  . PRO   B 1 52  ? -20.299 -12.870 9.083   1.00 40.43  ? 52  PRO   B CB  1 
ATOM   2782 C  CG  . PRO   B 1 52  ? -20.459 -11.498 8.446   1.00 41.49  ? 52  PRO   B CG  1 
ATOM   2783 C  CD  . PRO   B 1 52  ? -21.924 -11.466 8.071   1.00 41.65  ? 52  PRO   B CD  1 
ATOM   2784 N  N   . ASN   B 1 53  ? -21.082 -13.135 12.346  1.00 36.32  ? 53  ASN   B N   1 
ATOM   2785 C  CA  . ASN   B 1 53  ? -20.583 -12.633 13.618  1.00 40.57  ? 53  ASN   B CA  1 
ATOM   2786 C  C   . ASN   B 1 53  ? -19.171 -13.189 13.791  1.00 41.74  ? 53  ASN   B C   1 
ATOM   2787 O  O   . ASN   B 1 53  ? -18.987 -14.359 14.126  1.00 41.05  ? 53  ASN   B O   1 
ATOM   2788 C  CB  . ASN   B 1 53  ? -21.562 -12.934 14.750  1.00 45.30  ? 53  ASN   B CB  1 
ATOM   2789 C  CG  . ASN   B 1 53  ? -21.017 -12.653 16.138  1.00 48.24  ? 53  ASN   B CG  1 
ATOM   2790 O  OD1 . ASN   B 1 53  ? -19.834 -12.329 16.333  1.00 45.07  ? 53  ASN   B OD1 1 
ATOM   2791 N  ND2 . ASN   B 1 53  ? -21.874 -12.825 17.132  1.00 46.71  ? 53  ASN   B ND2 1 
ATOM   2792 N  N   . TYR   B 1 54  ? -18.182 -12.346 13.474  1.00 41.50  ? 54  TYR   B N   1 
ATOM   2793 C  CA  . TYR   B 1 54  ? -16.798 -12.780 13.381  1.00 41.14  ? 54  TYR   B CA  1 
ATOM   2794 C  C   . TYR   B 1 54  ? -16.261 -13.074 14.786  1.00 40.86  ? 54  TYR   B C   1 
ATOM   2795 O  O   . TYR   B 1 54  ? -15.502 -14.033 14.955  1.00 36.72  ? 54  TYR   B O   1 
ATOM   2796 C  CB  . TYR   B 1 54  ? -15.966 -11.742 12.610  1.00 38.23  ? 54  TYR   B CB  1 
ATOM   2797 C  CG  . TYR   B 1 54  ? -16.217 -11.643 11.105  1.00 35.59  ? 54  TYR   B CG  1 
ATOM   2798 C  CD1 . TYR   B 1 54  ? -15.620 -12.535 10.220  1.00 37.05  ? 54  TYR   B CD1 1 
ATOM   2799 C  CD2 . TYR   B 1 54  ? -17.022 -10.643 10.556  1.00 31.25  ? 54  TYR   B CD2 1 
ATOM   2800 C  CE1 . TYR   B 1 54  ? -15.835 -12.462 8.847   1.00 34.92  ? 54  TYR   B CE1 1 
ATOM   2801 C  CE2 . TYR   B 1 54  ? -17.239 -10.560 9.190   1.00 31.87  ? 54  TYR   B CE2 1 
ATOM   2802 C  CZ  . TYR   B 1 54  ? -16.644 -11.469 8.326   1.00 33.45  ? 54  TYR   B CZ  1 
ATOM   2803 O  OH  . TYR   B 1 54  ? -16.823 -11.391 6.962   1.00 32.96  ? 54  TYR   B OH  1 
ATOM   2804 N  N   . GLU   B 1 55  ? -16.687 -12.262 15.777  1.00 48.47  ? 55  GLU   B N   1 
ATOM   2805 C  CA  . GLU   B 1 55  ? -16.334 -12.469 17.184  1.00 52.12  ? 55  GLU   B CA  1 
ATOM   2806 C  C   . GLU   B 1 55  ? -16.538 -13.946 17.522  1.00 54.93  ? 55  GLU   B C   1 
ATOM   2807 O  O   . GLU   B 1 55  ? -15.614 -14.600 18.008  1.00 54.48  ? 55  GLU   B O   1 
ATOM   2808 C  CB  . GLU   B 1 55  ? -17.125 -11.681 18.244  1.00 54.05  ? 55  GLU   B CB  1 
ATOM   2809 C  CG  . GLU   B 1 55  ? -17.320 -10.184 17.990  1.00 60.28  ? 55  GLU   B CG  1 
ATOM   2810 C  CD  . GLU   B 1 55  ? -17.703 -9.316  19.197  1.00 60.83  ? 55  GLU   B CD  1 
ATOM   2811 O  OE1 . GLU   B 1 55  ? -16.806 -8.945  19.984  1.00 52.18  ? 55  GLU   B OE1 1 
ATOM   2812 O  OE2 . GLU   B 1 55  ? -18.904 -9.003  19.383  1.00 64.09  ? 55  GLU   B OE2 1 
ATOM   2813 N  N   . ASP   B 1 56  ? -17.746 -14.452 17.196  1.00 51.73  ? 56  ASP   B N   1 
ATOM   2814 C  CA  . ASP   B 1 56  ? -18.218 -15.745 17.657  1.00 49.23  ? 56  ASP   B CA  1 
ATOM   2815 C  C   . ASP   B 1 56  ? -17.693 -16.864 16.764  1.00 46.90  ? 56  ASP   B C   1 
ATOM   2816 O  O   . ASP   B 1 56  ? -17.301 -17.921 17.251  1.00 51.64  ? 56  ASP   B O   1 
ATOM   2817 C  CB  . ASP   B 1 56  ? -19.732 -15.773 17.784  1.00 49.76  ? 56  ASP   B CB  1 
ATOM   2818 C  CG  . ASP   B 1 56  ? -20.261 -16.993 18.523  1.00 48.14  ? 56  ASP   B CG  1 
ATOM   2819 O  OD1 . ASP   B 1 56  ? -19.903 -17.151 19.709  1.00 50.32  ? 56  ASP   B OD1 1 
ATOM   2820 O  OD2 . ASP   B 1 56  ? -20.965 -17.804 17.890  1.00 46.02  ? 56  ASP   B OD2 1 
ATOM   2821 N  N   . LEU   B 1 57  ? -17.676 -16.642 15.452  1.00 47.77  ? 57  LEU   B N   1 
ATOM   2822 C  CA  . LEU   B 1 57  ? -17.104 -17.627 14.550  1.00 46.98  ? 57  LEU   B CA  1 
ATOM   2823 C  C   . LEU   B 1 57  ? -15.631 -17.870 14.882  1.00 46.00  ? 57  LEU   B C   1 
ATOM   2824 O  O   . LEU   B 1 57  ? -15.135 -18.974 14.676  1.00 48.47  ? 57  LEU   B O   1 
ATOM   2825 C  CB  . LEU   B 1 57  ? -17.272 -17.174 13.103  1.00 53.20  ? 57  LEU   B CB  1 
ATOM   2826 C  CG  . LEU   B 1 57  ? -18.702 -17.185 12.558  1.00 57.00  ? 57  LEU   B CG  1 
ATOM   2827 C  CD1 . LEU   B 1 57  ? -18.744 -16.442 11.236  1.00 58.98  ? 57  LEU   B CD1 1 
ATOM   2828 C  CD2 . LEU   B 1 57  ? -19.239 -18.602 12.388  1.00 54.83  ? 57  LEU   B CD2 1 
ATOM   2829 N  N   . LEU   B 1 58  ? -14.923 -16.841 15.360  1.00 47.23  ? 58  LEU   B N   1 
ATOM   2830 C  CA  . LEU   B 1 58  ? -13.484 -16.957 15.541  1.00 52.40  ? 58  LEU   B CA  1 
ATOM   2831 C  C   . LEU   B 1 58  ? -13.155 -17.719 16.834  1.00 52.87  ? 58  LEU   B C   1 
ATOM   2832 O  O   . LEU   B 1 58  ? -12.351 -18.647 16.795  1.00 47.06  ? 58  LEU   B O   1 
ATOM   2833 C  CB  . LEU   B 1 58  ? -12.815 -15.584 15.476  1.00 49.35  ? 58  LEU   B CB  1 
ATOM   2834 C  CG  . LEU   B 1 58  ? -11.281 -15.569 15.547  1.00 51.92  ? 58  LEU   B CG  1 
ATOM   2835 C  CD1 . LEU   B 1 58  ? -10.589 -16.481 14.542  1.00 52.19  ? 58  LEU   B CD1 1 
ATOM   2836 C  CD2 . LEU   B 1 58  ? -10.768 -14.149 15.374  1.00 55.57  ? 58  LEU   B CD2 1 
ATOM   2837 N  N   . ILE   B 1 59  ? -13.792 -17.378 17.968  1.00 60.93  ? 59  ILE   B N   1 
ATOM   2838 C  CA  . ILE   B 1 59  ? -13.511 -18.085 19.217  1.00 63.81  ? 59  ILE   B CA  1 
ATOM   2839 C  C   . ILE   B 1 59  ? -13.727 -19.589 19.032  1.00 57.41  ? 59  ILE   B C   1 
ATOM   2840 O  O   . ILE   B 1 59  ? -13.049 -20.382 19.672  1.00 59.11  ? 59  ILE   B O   1 
ATOM   2841 C  CB  . ILE   B 1 59  ? -14.300 -17.563 20.440  1.00 67.07  ? 59  ILE   B CB  1 
ATOM   2842 C  CG1 . ILE   B 1 59  ? -15.808 -17.724 20.292  1.00 71.44  ? 59  ILE   B CG1 1 
ATOM   2843 C  CG2 . ILE   B 1 59  ? -13.925 -16.123 20.796  1.00 66.16  ? 59  ILE   B CG2 1 
ATOM   2844 C  CD1 . ILE   B 1 59  ? -16.540 -17.806 21.623  1.00 73.70  ? 59  ILE   B CD1 1 
ATOM   2845 N  N   . ARG   B 1 60  ? -14.637 -19.978 18.138  1.00 54.12  ? 60  ARG   B N   1 
ATOM   2846 C  CA  . ARG   B 1 60  ? -14.886 -21.379 17.842  1.00 59.16  ? 60  ARG   B CA  1 
ATOM   2847 C  C   . ARG   B 1 60  ? -13.814 -22.034 16.971  1.00 57.48  ? 60  ARG   B C   1 
ATOM   2848 O  O   . ARG   B 1 60  ? -13.904 -23.226 16.703  1.00 56.85  ? 60  ARG   B O   1 
ATOM   2849 C  CB  . ARG   B 1 60  ? -16.161 -21.513 17.012  1.00 68.97  ? 60  ARG   B CB  1 
ATOM   2850 C  CG  . ARG   B 1 60  ? -17.459 -21.107 17.690  1.00 76.96  ? 60  ARG   B CG  1 
ATOM   2851 C  CD  . ARG   B 1 60  ? -18.502 -21.123 16.594  1.00 85.91  ? 60  ARG   B CD  1 
ATOM   2852 N  NE  . ARG   B 1 60  ? -19.891 -21.070 17.052  1.00 98.39  ? 60  ARG   B NE  1 
ATOM   2853 C  CZ  . ARG   B 1 60  ? -20.921 -21.116 16.213  1.00 109.95 ? 60  ARG   B CZ  1 
ATOM   2854 N  NH1 . ARG   B 1 60  ? -20.703 -21.144 14.906  1.00 111.20 ? 60  ARG   B NH1 1 
ATOM   2855 N  NH2 . ARG   B 1 60  ? -22.160 -21.124 16.680  1.00 108.60 ? 60  ARG   B NH2 1 
ATOM   2856 N  N   . LYS   B 1 61  ? -12.839 -21.268 16.472  1.00 61.04  ? 61  LYS   B N   1 
ATOM   2857 C  CA  . LYS   B 1 61  ? -11.767 -21.833 15.665  1.00 59.79  ? 61  LYS   B CA  1 
ATOM   2858 C  C   . LYS   B 1 61  ? -10.537 -22.072 16.528  1.00 56.81  ? 61  LYS   B C   1 
ATOM   2859 O  O   . LYS   B 1 61  ? -10.392 -21.453 17.584  1.00 60.04  ? 61  LYS   B O   1 
ATOM   2860 C  CB  . LYS   B 1 61  ? -11.284 -20.869 14.577  1.00 64.29  ? 61  LYS   B CB  1 
ATOM   2861 C  CG  . LYS   B 1 61  ? -12.304 -20.529 13.524  1.00 63.50  ? 61  LYS   B CG  1 
ATOM   2862 C  CD  . LYS   B 1 61  ? -12.547 -21.668 12.549  1.00 59.86  ? 61  LYS   B CD  1 
ATOM   2863 C  CE  . LYS   B 1 61  ? -13.759 -21.353 11.754  1.00 61.63  ? 61  LYS   B CE  1 
ATOM   2864 N  NZ  . LYS   B 1 61  ? -13.993 -22.391 10.754  1.00 63.83  ? 61  LYS   B NZ  1 
ATOM   2865 N  N   . SER   B 1 62  ? -9.632  -22.918 16.022  1.00 52.88  ? 62  SER   B N   1 
ATOM   2866 C  CA  . SER   B 1 62  ? -8.319  -23.085 16.622  1.00 57.19  ? 62  SER   B CA  1 
ATOM   2867 C  C   . SER   B 1 62  ? -7.227  -23.155 15.553  1.00 52.06  ? 62  SER   B C   1 
ATOM   2868 O  O   . SER   B 1 62  ? -7.491  -23.451 14.390  1.00 50.07  ? 62  SER   B O   1 
ATOM   2869 C  CB  . SER   B 1 62  ? -8.282  -24.312 17.491  1.00 59.88  ? 62  SER   B CB  1 
ATOM   2870 O  OG  . SER   B 1 62  ? -7.996  -25.459 16.704  1.00 62.19  ? 62  SER   B OG  1 
ATOM   2871 N  N   . ASN   B 1 63  ? -5.982  -22.973 16.012  1.00 49.25  ? 63  ASN   B N   1 
ATOM   2872 C  CA  . ASN   B 1 63  ? -4.787  -22.933 15.183  1.00 48.09  ? 63  ASN   B CA  1 
ATOM   2873 C  C   . ASN   B 1 63  ? -4.761  -23.971 14.070  1.00 52.64  ? 63  ASN   B C   1 
ATOM   2874 O  O   . ASN   B 1 63  ? -4.295  -23.677 12.969  1.00 48.66  ? 63  ASN   B O   1 
ATOM   2875 C  CB  . ASN   B 1 63  ? -3.536  -23.160 16.011  1.00 42.77  ? 63  ASN   B CB  1 
ATOM   2876 C  CG  . ASN   B 1 63  ? -3.254  -21.975 16.887  1.00 44.54  ? 63  ASN   B CG  1 
ATOM   2877 O  OD1 . ASN   B 1 63  ? -3.839  -20.904 16.689  1.00 46.04  ? 63  ASN   B OD1 1 
ATOM   2878 N  ND2 . ASN   B 1 63  ? -2.344  -22.140 17.832  1.00 50.63  ? 63  ASN   B ND2 1 
ATOM   2879 N  N   . HIS   B 1 64  ? -5.208  -25.189 14.377  1.00 63.64  ? 64  HIS   B N   1 
ATOM   2880 C  CA  . HIS   B 1 64  ? -5.123  -26.306 13.445  1.00 67.63  ? 64  HIS   B CA  1 
ATOM   2881 C  C   . HIS   B 1 64  ? -6.239  -26.220 12.398  1.00 60.28  ? 64  HIS   B C   1 
ATOM   2882 O  O   . HIS   B 1 64  ? -6.233  -26.987 11.441  1.00 61.48  ? 64  HIS   B O   1 
ATOM   2883 C  CB  . HIS   B 1 64  ? -5.078  -27.633 14.220  1.00 80.77  ? 64  HIS   B CB  1 
ATOM   2884 C  CG  . HIS   B 1 64  ? -5.912  -27.631 15.468  1.00 91.99  ? 64  HIS   B CG  1 
ATOM   2885 N  ND1 . HIS   B 1 64  ? -5.382  -27.505 16.737  1.00 93.62  ? 64  HIS   B ND1 1 
ATOM   2886 C  CD2 . HIS   B 1 64  ? -7.244  -27.718 15.628  1.00 91.64  ? 64  HIS   B CD2 1 
ATOM   2887 C  CE1 . HIS   B 1 64  ? -6.366  -27.522 17.627  1.00 91.77  ? 64  HIS   B CE1 1 
ATOM   2888 N  NE2 . HIS   B 1 64  ? -7.506  -27.649 16.976  1.00 91.57  ? 64  HIS   B NE2 1 
ATOM   2889 N  N   . ASN   B 1 65  ? -7.175  -25.268 12.555  1.00 52.70  ? 65  ASN   B N   1 
ATOM   2890 C  CA  . ASN   B 1 65  ? -8.180  -24.998 11.532  1.00 54.18  ? 65  ASN   B CA  1 
ATOM   2891 C  C   . ASN   B 1 65  ? -7.603  -24.283 10.302  1.00 49.23  ? 65  ASN   B C   1 
ATOM   2892 O  O   . ASN   B 1 65  ? -8.328  -24.114 9.328   1.00 46.73  ? 65  ASN   B O   1 
ATOM   2893 C  CB  . ASN   B 1 65  ? -9.308  -24.102 12.041  1.00 58.27  ? 65  ASN   B CB  1 
ATOM   2894 C  CG  . ASN   B 1 65  ? -10.170 -24.764 13.090  1.00 62.12  ? 65  ASN   B CG  1 
ATOM   2895 O  OD1 . ASN   B 1 65  ? -10.237 -24.309 14.244  1.00 60.56  ? 65  ASN   B OD1 1 
ATOM   2896 N  ND2 . ASN   B 1 65  ? -10.842 -25.833 12.698  1.00 57.09  ? 65  ASN   B ND2 1 
ATOM   2897 N  N   . PHE   B 1 66  ? -6.334  -23.835 10.343  1.00 47.04  ? 66  PHE   B N   1 
ATOM   2898 C  CA  . PHE   B 1 66  ? -5.768  -23.016 9.274   1.00 45.44  ? 66  PHE   B CA  1 
ATOM   2899 C  C   . PHE   B 1 66  ? -4.543  -23.695 8.658   1.00 41.12  ? 66  PHE   B C   1 
ATOM   2900 O  O   . PHE   B 1 66  ? -3.570  -23.922 9.359   1.00 44.62  ? 66  PHE   B O   1 
ATOM   2901 C  CB  . PHE   B 1 66  ? -5.360  -21.630 9.794   1.00 41.54  ? 66  PHE   B CB  1 
ATOM   2902 C  CG  . PHE   B 1 66  ? -6.462  -20.811 10.451  1.00 40.50  ? 66  PHE   B CG  1 
ATOM   2903 C  CD1 . PHE   B 1 66  ? -7.364  -20.084 9.689   1.00 40.62  ? 66  PHE   B CD1 1 
ATOM   2904 C  CD2 . PHE   B 1 66  ? -6.569  -20.740 11.834  1.00 41.22  ? 66  PHE   B CD2 1 
ATOM   2905 C  CE1 . PHE   B 1 66  ? -8.362  -19.335 10.296  1.00 40.31  ? 66  PHE   B CE1 1 
ATOM   2906 C  CE2 . PHE   B 1 66  ? -7.562  -19.985 12.438  1.00 39.99  ? 66  PHE   B CE2 1 
ATOM   2907 C  CZ  . PHE   B 1 66  ? -8.458  -19.288 11.667  1.00 42.45  ? 66  PHE   B CZ  1 
ATOM   2908 N  N   . LEU   B 1 67  ? -4.579  -23.965 7.341   1.00 42.42  ? 67  LEU   B N   1 
ATOM   2909 C  CA  . LEU   B 1 67  ? -3.458  -24.548 6.611   1.00 43.00  ? 67  LEU   B CA  1 
ATOM   2910 C  C   . LEU   B 1 67  ? -2.750  -23.472 5.786   1.00 44.66  ? 67  LEU   B C   1 
ATOM   2911 O  O   . LEU   B 1 67  ? -3.372  -22.847 4.927   1.00 42.50  ? 67  LEU   B O   1 
ATOM   2912 C  CB  . LEU   B 1 67  ? -3.901  -25.663 5.660   1.00 47.07  ? 67  LEU   B CB  1 
ATOM   2913 C  CG  . LEU   B 1 67  ? -4.763  -26.777 6.258   1.00 53.88  ? 67  LEU   B CG  1 
ATOM   2914 C  CD1 . LEU   B 1 67  ? -6.267  -26.549 6.082   1.00 51.20  ? 67  LEU   B CD1 1 
ATOM   2915 C  CD2 . LEU   B 1 67  ? -4.320  -28.103 5.660   1.00 55.31  ? 67  LEU   B CD2 1 
ATOM   2916 N  N   . VAL   B 1 68  ? -1.428  -23.358 5.976   1.00 42.37  ? 68  VAL   B N   1 
ATOM   2917 C  CA  . VAL   B 1 68  ? -0.635  -22.291 5.393   1.00 40.59  ? 68  VAL   B CA  1 
ATOM   2918 C  C   . VAL   B 1 68  ? 0.515   -22.925 4.629   1.00 39.02  ? 68  VAL   B C   1 
ATOM   2919 O  O   . VAL   B 1 68  ? 1.362   -23.568 5.232   1.00 39.19  ? 68  VAL   B O   1 
ATOM   2920 C  CB  . VAL   B 1 68  ? -0.086  -21.322 6.458   1.00 39.03  ? 68  VAL   B CB  1 
ATOM   2921 C  CG1 . VAL   B 1 68  ? 0.739   -20.195 5.837   1.00 40.63  ? 68  VAL   B CG1 1 
ATOM   2922 C  CG2 . VAL   B 1 68  ? -1.179  -20.773 7.358   1.00 34.64  ? 68  VAL   B CG2 1 
ATOM   2923 N  N   . GLN   B 1 69  ? 0.581   -22.651 3.319   1.00 41.50  ? 69  GLN   B N   1 
ATOM   2924 C  CA  . GLN   B 1 69  ? 1.556   -23.282 2.451   1.00 40.65  ? 69  GLN   B CA  1 
ATOM   2925 C  C   . GLN   B 1 69  ? 2.376   -22.210 1.741   1.00 37.85  ? 69  GLN   B C   1 
ATOM   2926 O  O   . GLN   B 1 69  ? 1.803   -21.346 1.088   1.00 31.93  ? 69  GLN   B O   1 
ATOM   2927 C  CB  . GLN   B 1 69  ? 0.760   -24.194 1.520   1.00 47.48  ? 69  GLN   B CB  1 
ATOM   2928 C  CG  . GLN   B 1 69  ? 1.419   -25.549 1.278   1.00 58.18  ? 69  GLN   B CG  1 
ATOM   2929 C  CD  . GLN   B 1 69  ? 0.508   -26.548 0.594   1.00 61.76  ? 69  GLN   B CD  1 
ATOM   2930 O  OE1 . GLN   B 1 69  ? -0.618  -26.799 1.040   1.00 65.86  ? 69  GLN   B OE1 1 
ATOM   2931 N  NE2 . GLN   B 1 69  ? 0.976   -27.109 -0.513  1.00 63.08  ? 69  GLN   B NE2 1 
ATOM   2932 N  N   . ALA   B 1 70  ? 3.705   -22.273 1.921   1.00 35.78  ? 70  ALA   B N   1 
ATOM   2933 C  CA  . ALA   B 1 70  ? 4.679   -21.479 1.188   1.00 36.91  ? 70  ALA   B CA  1 
ATOM   2934 C  C   . ALA   B 1 70  ? 5.451   -22.380 0.230   1.00 44.33  ? 70  ALA   B C   1 
ATOM   2935 O  O   . ALA   B 1 70  ? 6.406   -23.052 0.637   1.00 47.40  ? 70  ALA   B O   1 
ATOM   2936 C  CB  . ALA   B 1 70  ? 5.630   -20.797 2.150   1.00 37.03  ? 70  ALA   B CB  1 
ATOM   2937 N  N   . GLY   B 1 71  ? 5.033   -22.381 -1.043  1.00 48.53  ? 71  GLY   B N   1 
ATOM   2938 C  CA  . GLY   B 1 71  ? 5.527   -23.338 -2.017  1.00 52.38  ? 71  GLY   B CA  1 
ATOM   2939 C  C   . GLY   B 1 71  ? 4.990   -24.732 -1.716  1.00 57.18  ? 71  GLY   B C   1 
ATOM   2940 O  O   . GLY   B 1 71  ? 3.788   -24.961 -1.825  1.00 62.21  ? 71  GLY   B O   1 
ATOM   2941 N  N   . ASN   B 1 72  ? 5.889   -25.640 -1.309  1.00 69.26  ? 72  ASN   B N   1 
ATOM   2942 C  CA  . ASN   B 1 72  ? 5.541   -27.018 -0.979  1.00 73.65  ? 72  ASN   B CA  1 
ATOM   2943 C  C   . ASN   B 1 72  ? 5.801   -27.275 0.508   1.00 70.27  ? 72  ASN   B C   1 
ATOM   2944 O  O   . ASN   B 1 72  ? 5.877   -28.423 0.939   1.00 77.23  ? 72  ASN   B O   1 
ATOM   2945 C  CB  . ASN   B 1 72  ? 6.324   -27.985 -1.866  1.00 80.92  ? 72  ASN   B CB  1 
ATOM   2946 C  CG  . ASN   B 1 72  ? 5.668   -29.339 -2.029  1.00 86.62  ? 72  ASN   B CG  1 
ATOM   2947 O  OD1 . ASN   B 1 72  ? 4.494   -29.419 -2.412  1.00 94.01  ? 72  ASN   B OD1 1 
ATOM   2948 N  ND2 . ASN   B 1 72  ? 6.411   -30.411 -1.785  1.00 84.56  ? 72  ASN   B ND2 1 
ATOM   2949 N  N   . VAL   B 1 73  ? 5.918   -26.197 1.291   1.00 65.39  ? 73  VAL   B N   1 
ATOM   2950 C  CA  . VAL   B 1 73  ? 6.312   -26.270 2.688   1.00 61.77  ? 73  VAL   B CA  1 
ATOM   2951 C  C   . VAL   B 1 73  ? 5.144   -25.812 3.557   1.00 60.15  ? 73  VAL   B C   1 
ATOM   2952 O  O   . VAL   B 1 73  ? 4.645   -24.704 3.370   1.00 64.73  ? 73  VAL   B O   1 
ATOM   2953 C  CB  . VAL   B 1 73  ? 7.547   -25.372 2.895   1.00 62.37  ? 73  VAL   B CB  1 
ATOM   2954 C  CG1 . VAL   B 1 73  ? 7.907   -25.227 4.372   1.00 62.68  ? 73  VAL   B CG1 1 
ATOM   2955 C  CG2 . VAL   B 1 73  ? 8.738   -25.844 2.062   1.00 60.81  ? 73  VAL   B CG2 1 
ATOM   2956 N  N   . GLN   B 1 74  ? 4.727   -26.660 4.507   1.00 52.32  ? 74  GLN   B N   1 
ATOM   2957 C  CA  . GLN   B 1 74  ? 3.712   -26.297 5.480   1.00 54.83  ? 74  GLN   B CA  1 
ATOM   2958 C  C   . GLN   B 1 74  ? 4.353   -25.377 6.512   1.00 54.37  ? 74  GLN   B C   1 
ATOM   2959 O  O   . GLN   B 1 74  ? 5.430   -25.674 7.024   1.00 58.10  ? 74  GLN   B O   1 
ATOM   2960 C  CB  . GLN   B 1 74  ? 3.138   -27.465 6.288   1.00 64.62  ? 74  GLN   B CB  1 
ATOM   2961 C  CG  . GLN   B 1 74  ? 2.582   -28.625 5.468   1.00 76.70  ? 74  GLN   B CG  1 
ATOM   2962 C  CD  . GLN   B 1 74  ? 1.460   -28.233 4.531   1.00 87.15  ? 74  GLN   B CD  1 
ATOM   2963 O  OE1 . GLN   B 1 74  ? 1.405   -28.662 3.372   1.00 95.76  ? 74  GLN   B OE1 1 
ATOM   2964 N  NE2 . GLN   B 1 74  ? 0.535   -27.429 5.038   1.00 96.59  ? 74  GLN   B NE2 1 
ATOM   2965 N  N   . LEU   B 1 75  ? 3.690   -24.253 6.790   1.00 53.25  ? 75  LEU   B N   1 
ATOM   2966 C  CA  . LEU   B 1 75  ? 3.986   -23.454 7.967   1.00 53.03  ? 75  LEU   B CA  1 
ATOM   2967 C  C   . LEU   B 1 75  ? 3.052   -23.903 9.090   1.00 54.51  ? 75  LEU   B C   1 
ATOM   2968 O  O   . LEU   B 1 75  ? 1.859   -24.113 8.856   1.00 56.06  ? 75  LEU   B O   1 
ATOM   2969 C  CB  . LEU   B 1 75  ? 3.814   -21.958 7.685   1.00 51.57  ? 75  LEU   B CB  1 
ATOM   2970 C  CG  . LEU   B 1 75  ? 4.718   -21.332 6.618   1.00 50.37  ? 75  LEU   B CG  1 
ATOM   2971 C  CD1 . LEU   B 1 75  ? 4.702   -19.816 6.742   1.00 48.38  ? 75  LEU   B CD1 1 
ATOM   2972 C  CD2 . LEU   B 1 75  ? 6.146   -21.842 6.682   1.00 50.34  ? 75  LEU   B CD2 1 
ATOM   2973 N  N   . ARG   B 1 76  ? 3.610   -24.022 10.306  1.00 49.82  ? 76  ARG   B N   1 
ATOM   2974 C  CA  . ARG   B 1 76  ? 2.841   -24.288 11.511  1.00 49.54  ? 76  ARG   B CA  1 
ATOM   2975 C  C   . ARG   B 1 76  ? 2.344   -22.979 12.133  1.00 44.01  ? 76  ARG   B C   1 
ATOM   2976 O  O   . ARG   B 1 76  ? 3.151   -22.104 12.470  1.00 38.44  ? 76  ARG   B O   1 
ATOM   2977 C  CB  . ARG   B 1 76  ? 3.733   -25.031 12.516  1.00 59.10  ? 76  ARG   B CB  1 
ATOM   2978 C  CG  . ARG   B 1 76  ? 3.051   -25.454 13.813  1.00 67.66  ? 76  ARG   B CG  1 
ATOM   2979 C  CD  . ARG   B 1 76  ? 3.960   -26.260 14.734  1.00 77.15  ? 76  ARG   B CD  1 
ATOM   2980 N  NE  . ARG   B 1 76  ? 4.628   -27.357 14.020  1.00 88.58  ? 76  ARG   B NE  1 
ATOM   2981 C  CZ  . ARG   B 1 76  ? 4.034   -28.393 13.417  1.00 95.21  ? 76  ARG   B CZ  1 
ATOM   2982 N  NH1 . ARG   B 1 76  ? 2.723   -28.554 13.486  1.00 99.29  ? 76  ARG   B NH1 1 
ATOM   2983 N  NH2 . ARG   B 1 76  ? 4.756   -29.281 12.753  1.00 94.49  ? 76  ARG   B NH2 1 
ATOM   2984 N  N   . VAL   B 1 77  ? 1.016   -22.900 12.324  1.00 39.45  ? 77  VAL   B N   1 
ATOM   2985 C  CA  . VAL   B 1 77  ? 0.347   -21.797 13.000  1.00 42.79  ? 77  VAL   B CA  1 
ATOM   2986 C  C   . VAL   B 1 77  ? 0.357   -22.046 14.509  1.00 45.22  ? 77  VAL   B C   1 
ATOM   2987 O  O   . VAL   B 1 77  ? -0.161  -23.059 14.966  1.00 46.14  ? 77  VAL   B O   1 
ATOM   2988 C  CB  . VAL   B 1 77  ? -1.114  -21.641 12.526  1.00 42.82  ? 77  VAL   B CB  1 
ATOM   2989 C  CG1 . VAL   B 1 77  ? -1.843  -20.523 13.263  1.00 44.52  ? 77  VAL   B CG1 1 
ATOM   2990 C  CG2 . VAL   B 1 77  ? -1.230  -21.447 11.020  1.00 43.10  ? 77  VAL   B CG2 1 
ATOM   2991 N  N   . ILE   B 1 78  ? 0.857   -21.072 15.276  1.00 39.47  ? 78  ILE   B N   1 
ATOM   2992 C  CA  . ILE   B 1 78  ? 0.945   -21.212 16.715  1.00 39.86  ? 78  ILE   B CA  1 
ATOM   2993 C  C   . ILE   B 1 78  ? 0.036   -20.201 17.420  1.00 42.48  ? 78  ILE   B C   1 
ATOM   2994 O  O   . ILE   B 1 78  ? -0.068  -20.240 18.640  1.00 42.27  ? 78  ILE   B O   1 
ATOM   2995 C  CB  . ILE   B 1 78  ? 2.416   -21.110 17.175  1.00 39.26  ? 78  ILE   B CB  1 
ATOM   2996 C  CG1 . ILE   B 1 78  ? 3.049   -19.763 16.818  1.00 37.78  ? 78  ILE   B CG1 1 
ATOM   2997 C  CG2 . ILE   B 1 78  ? 3.259   -22.268 16.632  1.00 37.15  ? 78  ILE   B CG2 1 
ATOM   2998 C  CD1 . ILE   B 1 78  ? 4.372   -19.485 17.530  1.00 36.69  ? 78  ILE   B CD1 1 
ATOM   2999 N  N   . GLY   B 1 79  ? -0.623  -19.296 16.676  1.00 43.70  ? 79  GLY   B N   1 
ATOM   3000 C  CA  . GLY   B 1 79  ? -1.509  -18.309 17.279  1.00 40.91  ? 79  GLY   B CA  1 
ATOM   3001 C  C   . GLY   B 1 79  ? -2.407  -17.657 16.228  1.00 42.71  ? 79  GLY   B C   1 
ATOM   3002 O  O   . GLY   B 1 79  ? -2.134  -17.762 15.032  1.00 41.35  ? 79  GLY   B O   1 
ATOM   3003 N  N   . HIS   B 1 80  ? -3.482  -16.998 16.680  1.00 41.68  ? 80  HIS   B N   1 
ATOM   3004 C  CA  . HIS   B 1 80  ? -4.434  -16.383 15.767  1.00 40.21  ? 80  HIS   B CA  1 
ATOM   3005 C  C   . HIS   B 1 80  ? -5.182  -15.262 16.473  1.00 41.39  ? 80  HIS   B C   1 
ATOM   3006 O  O   . HIS   B 1 80  ? -5.617  -15.408 17.612  1.00 37.69  ? 80  HIS   B O   1 
ATOM   3007 C  CB  . HIS   B 1 80  ? -5.358  -17.418 15.117  1.00 42.47  ? 80  HIS   B CB  1 
ATOM   3008 C  CG  . HIS   B 1 80  ? -6.271  -18.158 16.037  1.00 49.50  ? 80  HIS   B CG  1 
ATOM   3009 N  ND1 . HIS   B 1 80  ? -5.865  -19.225 16.811  1.00 51.74  ? 80  HIS   B ND1 1 
ATOM   3010 C  CD2 . HIS   B 1 80  ? -7.574  -18.004 16.284  1.00 52.15  ? 80  HIS   B CD2 1 
ATOM   3011 C  CE1 . HIS   B 1 80  ? -6.891  -19.672 17.517  1.00 51.92  ? 80  HIS   B CE1 1 
ATOM   3012 N  NE2 . HIS   B 1 80  ? -7.942  -18.950 17.209  1.00 54.07  ? 80  HIS   B NE2 1 
ATOM   3013 N  N   . SER   B 1 81  ? -5.319  -14.133 15.769  1.00 38.50  ? 81  SER   B N   1 
ATOM   3014 C  CA  . SER   B 1 81  ? -6.152  -13.040 16.232  1.00 35.41  ? 81  SER   B CA  1 
ATOM   3015 C  C   . SER   B 1 81  ? -6.669  -12.218 15.051  1.00 37.34  ? 81  SER   B C   1 
ATOM   3016 O  O   . SER   B 1 81  ? -6.304  -12.460 13.901  1.00 35.84  ? 81  SER   B O   1 
ATOM   3017 C  CB  . SER   B 1 81  ? -5.402  -12.185 17.181  1.00 35.47  ? 81  SER   B CB  1 
ATOM   3018 O  OG  . SER   B 1 81  ? -4.331  -11.554 16.503  1.00 38.63  ? 81  SER   B OG  1 
ATOM   3019 N  N   . MET   B 1 82  ? -7.534  -11.248 15.368  1.00 35.37  ? 82  MET   B N   1 
ATOM   3020 C  CA  . MET   B 1 82  ? -8.207  -10.399 14.404  1.00 36.59  ? 82  MET   B CA  1 
ATOM   3021 C  C   . MET   B 1 82  ? -7.891  -8.933  14.725  1.00 33.93  ? 82  MET   B C   1 
ATOM   3022 O  O   . MET   B 1 82  ? -7.890  -8.523  15.887  1.00 30.99  ? 82  MET   B O   1 
ATOM   3023 C  CB  . MET   B 1 82  ? -9.704  -10.716 14.499  1.00 40.95  ? 82  MET   B CB  1 
ATOM   3024 C  CG  . MET   B 1 82  ? -10.627 -10.017 13.533  1.00 42.37  ? 82  MET   B CG  1 
ATOM   3025 S  SD  . MET   B 1 82  ? -12.336 -10.564 13.785  1.00 45.00  ? 82  MET   B SD  1 
ATOM   3026 C  CE  . MET   B 1 82  ? -12.157 -12.089 12.848  1.00 46.56  ? 82  MET   B CE  1 
ATOM   3027 N  N   . GLN   B 1 83  ? -7.563  -8.160  13.683  1.00 30.61  ? 83  GLN   B N   1 
ATOM   3028 C  CA  . GLN   B 1 83  ? -7.509  -6.714  13.777  1.00 29.82  ? 83  GLN   B CA  1 
ATOM   3029 C  C   . GLN   B 1 83  ? -8.385  -6.125  12.666  1.00 28.60  ? 83  GLN   B C   1 
ATOM   3030 O  O   . GLN   B 1 83  ? -8.103  -6.298  11.476  1.00 24.59  ? 83  GLN   B O   1 
ATOM   3031 C  CB  . GLN   B 1 83  ? -6.061  -6.229  13.741  1.00 31.30  ? 83  GLN   B CB  1 
ATOM   3032 C  CG  . GLN   B 1 83  ? -5.966  -4.707  13.766  1.00 32.20  ? 83  GLN   B CG  1 
ATOM   3033 C  CD  . GLN   B 1 83  ? -4.570  -4.161  13.605  1.00 34.88  ? 83  GLN   B CD  1 
ATOM   3034 O  OE1 . GLN   B 1 83  ? -3.613  -4.868  13.287  1.00 37.45  ? 83  GLN   B OE1 1 
ATOM   3035 N  NE2 . GLN   B 1 83  ? -4.454  -2.862  13.810  1.00 38.65  ? 83  GLN   B NE2 1 
ATOM   3036 N  N   . ASN   B 1 84  ? -9.486  -5.476  13.083  1.00 28.61  ? 84  ASN   B N   1 
ATOM   3037 C  CA  . ASN   B 1 84  ? -10.528 -4.999  12.191  1.00 26.90  ? 84  ASN   B CA  1 
ATOM   3038 C  C   . ASN   B 1 84  ? -10.917 -6.150  11.260  1.00 27.26  ? 84  ASN   B C   1 
ATOM   3039 O  O   . ASN   B 1 84  ? -11.201 -7.244  11.761  1.00 27.68  ? 84  ASN   B O   1 
ATOM   3040 C  CB  . ASN   B 1 84  ? -10.094 -3.690  11.550  1.00 25.93  ? 84  ASN   B CB  1 
ATOM   3041 C  CG  . ASN   B 1 84  ? -9.722  -2.675  12.602  1.00 27.85  ? 84  ASN   B CG  1 
ATOM   3042 O  OD1 . ASN   B 1 84  ? -10.528 -2.314  13.475  1.00 27.09  ? 84  ASN   B OD1 1 
ATOM   3043 N  ND2 . ASN   B 1 84  ? -8.513  -2.160  12.509  1.00 28.91  ? 84  ASN   B ND2 1 
ATOM   3044 N  N   . CYS   B 1 85  ? -10.870 -5.932  9.928   1.00 25.82  ? 85  CYS   B N   1 
ATOM   3045 C  CA  . CYS   B 1 85  ? -11.289 -6.949  8.969   1.00 27.37  ? 85  CYS   B CA  1 
ATOM   3046 C  C   . CYS   B 1 85  ? -10.127 -7.827  8.464   1.00 26.05  ? 85  CYS   B C   1 
ATOM   3047 O  O   . CYS   B 1 85  ? -10.300 -8.601  7.530   1.00 29.75  ? 85  CYS   B O   1 
ATOM   3048 C  CB  . CYS   B 1 85  ? -12.040 -6.340  7.785   1.00 27.03  ? 85  CYS   B CB  1 
ATOM   3049 S  SG  . CYS   B 1 85  ? -13.451 -5.275  8.203   1.00 27.25  ? 85  CYS   B SG  1 
ATOM   3050 N  N   . VAL   B 1 86  ? -8.958  -7.783  9.099   1.00 24.05  ? 86  VAL   B N   1 
ATOM   3051 C  CA  . VAL   B 1 86  ? -7.857  -8.668  8.747   1.00 25.53  ? 86  VAL   B CA  1 
ATOM   3052 C  C   . VAL   B 1 86  ? -7.565  -9.694  9.854   1.00 26.40  ? 86  VAL   B C   1 
ATOM   3053 O  O   . VAL   B 1 86  ? -7.527  -9.353  11.036  1.00 27.80  ? 86  VAL   B O   1 
ATOM   3054 C  CB  . VAL   B 1 86  ? -6.650  -7.759  8.438   1.00 25.81  ? 86  VAL   B CB  1 
ATOM   3055 C  CG1 . VAL   B 1 86  ? -5.337  -8.472  8.617   1.00 29.08  ? 86  VAL   B CG1 1 
ATOM   3056 C  CG2 . VAL   B 1 86  ? -6.736  -7.167  7.040   1.00 25.54  ? 86  VAL   B CG2 1 
ATOM   3057 N  N   . LEU   B 1 87  ? -7.329  -10.953 9.446   1.00 26.36  ? 87  LEU   B N   1 
ATOM   3058 C  CA  . LEU   B 1 87  ? -6.852  -12.039 10.301  1.00 27.32  ? 87  LEU   B CA  1 
ATOM   3059 C  C   . LEU   B 1 87  ? -5.314  -12.106 10.325  1.00 28.00  ? 87  LEU   B C   1 
ATOM   3060 O  O   . LEU   B 1 87  ? -4.671  -12.074 9.271   1.00 25.22  ? 87  LEU   B O   1 
ATOM   3061 C  CB  . LEU   B 1 87  ? -7.479  -13.301 9.689   1.00 29.09  ? 87  LEU   B CB  1 
ATOM   3062 C  CG  . LEU   B 1 87  ? -7.335  -14.619 10.451  1.00 34.39  ? 87  LEU   B CG  1 
ATOM   3063 C  CD1 . LEU   B 1 87  ? -8.177  -14.635 11.724  1.00 33.78  ? 87  LEU   B CD1 1 
ATOM   3064 C  CD2 . LEU   B 1 87  ? -7.716  -15.806 9.576   1.00 38.99  ? 87  LEU   B CD2 1 
ATOM   3065 N  N   . LYS   B 1 88  ? -4.736  -12.247 11.535  1.00 25.97  ? 88  LYS   B N   1 
ATOM   3066 C  CA  . LYS   B 1 88  ? -3.305  -12.380 11.761  1.00 28.10  ? 88  LYS   B CA  1 
ATOM   3067 C  C   . LYS   B 1 88  ? -2.990  -13.785 12.287  1.00 30.71  ? 88  LYS   B C   1 
ATOM   3068 O  O   . LYS   B 1 88  ? -3.444  -14.152 13.372  1.00 31.44  ? 88  LYS   B O   1 
ATOM   3069 C  CB  . LYS   B 1 88  ? -2.842  -11.334 12.779  1.00 27.92  ? 88  LYS   B CB  1 
ATOM   3070 C  CG  . LYS   B 1 88  ? -3.192  -9.911  12.374  1.00 32.36  ? 88  LYS   B CG  1 
ATOM   3071 C  CD  . LYS   B 1 88  ? -2.485  -8.814  13.151  1.00 34.95  ? 88  LYS   B CD  1 
ATOM   3072 C  CE  . LYS   B 1 88  ? -2.637  -8.927  14.605  1.00 40.89  ? 88  LYS   B CE  1 
ATOM   3073 N  NZ  . LYS   B 1 88  ? -1.784  -7.911  15.231  1.00 46.34  ? 88  LYS   B NZ  1 
ATOM   3074 N  N   . LEU   B 1 89  ? -2.263  -14.578 11.488  1.00 29.34  ? 89  LEU   B N   1 
ATOM   3075 C  CA  . LEU   B 1 89  ? -1.906  -15.944 11.843  1.00 30.04  ? 89  LEU   B CA  1 
ATOM   3076 C  C   . LEU   B 1 89  ? -0.425  -15.971 12.201  1.00 30.23  ? 89  LEU   B C   1 
ATOM   3077 O  O   . LEU   B 1 89  ? 0.412   -15.801 11.332  1.00 32.60  ? 89  LEU   B O   1 
ATOM   3078 C  CB  . LEU   B 1 89  ? -2.193  -16.938 10.716  1.00 29.55  ? 89  LEU   B CB  1 
ATOM   3079 C  CG  . LEU   B 1 89  ? -3.654  -17.089 10.292  1.00 33.20  ? 89  LEU   B CG  1 
ATOM   3080 C  CD1 . LEU   B 1 89  ? -3.841  -18.072 9.139   1.00 35.21  ? 89  LEU   B CD1 1 
ATOM   3081 C  CD2 . LEU   B 1 89  ? -4.497  -17.493 11.485  1.00 37.83  ? 89  LEU   B CD2 1 
ATOM   3082 N  N   . LYS   B 1 90  ? -0.124  -16.165 13.493  1.00 31.97  ? 90  LYS   B N   1 
ATOM   3083 C  CA  . LYS   B 1 90  ? 1.228   -16.348 13.985  1.00 33.29  ? 90  LYS   B CA  1 
ATOM   3084 C  C   . LYS   B 1 90  ? 1.710   -17.741 13.601  1.00 33.35  ? 90  LYS   B C   1 
ATOM   3085 O  O   . LYS   B 1 90  ? 0.967   -18.695 13.790  1.00 31.82  ? 90  LYS   B O   1 
ATOM   3086 C  CB  . LYS   B 1 90  ? 1.195   -16.224 15.508  1.00 36.58  ? 90  LYS   B CB  1 
ATOM   3087 C  CG  . LYS   B 1 90  ? 2.535   -16.371 16.199  1.00 45.55  ? 90  LYS   B CG  1 
ATOM   3088 C  CD  . LYS   B 1 90  ? 3.299   -15.095 16.529  1.00 53.22  ? 90  LYS   B CD  1 
ATOM   3089 C  CE  . LYS   B 1 90  ? 4.180   -15.349 17.727  1.00 57.45  ? 90  LYS   B CE  1 
ATOM   3090 N  NZ  . LYS   B 1 90  ? 4.875   -14.153 18.201  1.00 58.79  ? 90  LYS   B NZ  1 
ATOM   3091 N  N   . VAL   B 1 91  ? 2.946   -17.820 13.088  1.00 37.35  ? 91  VAL   B N   1 
ATOM   3092 C  CA  . VAL   B 1 91  ? 3.555   -19.051 12.602  1.00 36.53  ? 91  VAL   B CA  1 
ATOM   3093 C  C   . VAL   B 1 91  ? 4.897   -19.262 13.305  1.00 39.55  ? 91  VAL   B C   1 
ATOM   3094 O  O   . VAL   B 1 91  ? 5.435   -18.346 13.940  1.00 37.83  ? 91  VAL   B O   1 
ATOM   3095 C  CB  . VAL   B 1 91  ? 3.715   -19.010 11.068  1.00 36.89  ? 91  VAL   B CB  1 
ATOM   3096 C  CG1 . VAL   B 1 91  ? 2.369   -18.985 10.371  1.00 34.66  ? 91  VAL   B CG1 1 
ATOM   3097 C  CG2 . VAL   B 1 91  ? 4.559   -17.829 10.587  1.00 40.04  ? 91  VAL   B CG2 1 
ATOM   3098 N  N   . ASP   B 1 92  ? 5.442   -20.485 13.188  1.00 40.33  ? 92  ASP   B N   1 
ATOM   3099 C  CA  . ASP   B 1 92  ? 6.622   -20.859 13.953  1.00 42.33  ? 92  ASP   B CA  1 
ATOM   3100 C  C   . ASP   B 1 92  ? 7.911   -20.342 13.316  1.00 45.20  ? 92  ASP   B C   1 
ATOM   3101 O  O   . ASP   B 1 92  ? 8.951   -20.453 13.943  1.00 46.28  ? 92  ASP   B O   1 
ATOM   3102 C  CB  . ASP   B 1 92  ? 6.738   -22.360 14.166  1.00 47.00  ? 92  ASP   B CB  1 
ATOM   3103 C  CG  . ASP   B 1 92  ? 6.915   -23.222 12.926  1.00 50.67  ? 92  ASP   B CG  1 
ATOM   3104 O  OD1 . ASP   B 1 92  ? 6.857   -22.680 11.801  1.00 57.00  ? 92  ASP   B OD1 1 
ATOM   3105 O  OD2 . ASP   B 1 92  ? 7.105   -24.438 13.098  1.00 59.20  ? 92  ASP   B OD2 1 
ATOM   3106 N  N   . THR   B 1 93  ? 7.854   -19.785 12.093  1.00 43.47  ? 93  THR   B N   1 
ATOM   3107 C  CA  . THR   B 1 93  ? 9.051   -19.440 11.339  1.00 38.25  ? 93  THR   B CA  1 
ATOM   3108 C  C   . THR   B 1 93  ? 8.942   -18.017 10.775  1.00 35.88  ? 93  THR   B C   1 
ATOM   3109 O  O   . THR   B 1 93  ? 7.922   -17.634 10.216  1.00 35.17  ? 93  THR   B O   1 
ATOM   3110 C  CB  . THR   B 1 93  ? 9.246   -20.455 10.214  1.00 37.85  ? 93  THR   B CB  1 
ATOM   3111 O  OG1 . THR   B 1 93  ? 9.447   -21.693 10.885  1.00 38.23  ? 93  THR   B OG1 1 
ATOM   3112 C  CG2 . THR   B 1 93  ? 10.435  -20.125 9.324   1.00 37.87  ? 93  THR   B CG2 1 
ATOM   3113 N  N   . ALA   B 1 94  ? 10.021  -17.244 10.929  1.00 32.11  ? 94  ALA   B N   1 
ATOM   3114 C  CA  . ALA   B 1 94  ? 10.121  -15.921 10.351  1.00 34.20  ? 94  ALA   B CA  1 
ATOM   3115 C  C   . ALA   B 1 94  ? 10.482  -16.053 8.875   1.00 34.41  ? 94  ALA   B C   1 
ATOM   3116 O  O   . ALA   B 1 94  ? 11.254  -16.936 8.512   1.00 37.56  ? 94  ALA   B O   1 
ATOM   3117 C  CB  . ALA   B 1 94  ? 11.146  -15.117 11.109  1.00 32.21  ? 94  ALA   B CB  1 
ATOM   3118 N  N   . ASN   B 1 95  ? 9.920   -15.177 8.031   1.00 34.45  ? 95  ASN   B N   1 
ATOM   3119 C  CA  . ASN   B 1 95  ? 10.155  -15.243 6.594   1.00 32.46  ? 95  ASN   B CA  1 
ATOM   3120 C  C   . ASN   B 1 95  ? 11.581  -14.790 6.313   1.00 30.56  ? 95  ASN   B C   1 
ATOM   3121 O  O   . ASN   B 1 95  ? 11.879  -13.605 6.462   1.00 32.42  ? 95  ASN   B O   1 
ATOM   3122 C  CB  . ASN   B 1 95  ? 9.157   -14.384 5.808   1.00 33.33  ? 95  ASN   B CB  1 
ATOM   3123 C  CG  . ASN   B 1 95  ? 9.293   -14.513 4.302   1.00 33.43  ? 95  ASN   B CG  1 
ATOM   3124 O  OD1 . ASN   B 1 95  ? 10.214  -15.171 3.795   1.00 26.93  ? 95  ASN   B OD1 1 
ATOM   3125 N  ND2 . ASN   B 1 95  ? 8.382   -13.891 3.560   1.00 30.35  ? 95  ASN   B ND2 1 
ATOM   3126 N  N   . PRO   B 1 96  ? 12.493  -15.668 5.825   1.00 27.97  ? 96  PRO   B N   1 
ATOM   3127 C  CA  . PRO   B 1 96  ? 13.870  -15.244 5.575   1.00 30.00  ? 96  PRO   B CA  1 
ATOM   3128 C  C   . PRO   B 1 96  ? 13.969  -14.218 4.451   1.00 32.58  ? 96  PRO   B C   1 
ATOM   3129 O  O   . PRO   B 1 96  ? 15.012  -13.582 4.285   1.00 32.93  ? 96  PRO   B O   1 
ATOM   3130 C  CB  . PRO   B 1 96  ? 14.611  -16.560 5.248   1.00 30.16  ? 96  PRO   B CB  1 
ATOM   3131 C  CG  . PRO   B 1 96  ? 13.529  -17.485 4.722   1.00 30.45  ? 96  PRO   B CG  1 
ATOM   3132 C  CD  . PRO   B 1 96  ? 12.245  -17.067 5.425   1.00 30.17  ? 96  PRO   B CD  1 
ATOM   3133 N  N   . LYS   B 1 97  ? 12.879  -14.066 3.682   1.00 33.01  ? 97  LYS   B N   1 
ATOM   3134 C  CA  . LYS   B 1 97  ? 12.803  -13.094 2.602   1.00 34.02  ? 97  LYS   B CA  1 
ATOM   3135 C  C   . LYS   B 1 97  ? 12.062  -11.808 2.981   1.00 33.62  ? 97  LYS   B C   1 
ATOM   3136 O  O   . LYS   B 1 97  ? 11.805  -10.987 2.111   1.00 32.82  ? 97  LYS   B O   1 
ATOM   3137 C  CB  . LYS   B 1 97  ? 12.084  -13.747 1.419   1.00 35.87  ? 97  LYS   B CB  1 
ATOM   3138 C  CG  . LYS   B 1 97  ? 12.915  -14.789 0.715   1.00 40.01  ? 97  LYS   B CG  1 
ATOM   3139 C  CD  . LYS   B 1 97  ? 12.086  -15.631 -0.238  1.00 43.52  ? 97  LYS   B CD  1 
ATOM   3140 C  CE  . LYS   B 1 97  ? 12.924  -16.706 -0.848  1.00 46.66  ? 97  LYS   B CE  1 
ATOM   3141 N  NZ  . LYS   B 1 97  ? 12.034  -17.591 -1.594  1.00 46.05  ? 97  LYS   B NZ  1 
ATOM   3142 N  N   . THR   B 1 98  ? 11.748  -11.585 4.258   1.00 32.11  ? 98  THR   B N   1 
ATOM   3143 C  CA  . THR   B 1 98  ? 11.088  -10.346 4.654   1.00 31.80  ? 98  THR   B CA  1 
ATOM   3144 C  C   . THR   B 1 98  ? 11.908  -9.136  4.201   1.00 32.33  ? 98  THR   B C   1 
ATOM   3145 O  O   . THR   B 1 98  ? 13.053  -8.963  4.630   1.00 31.18  ? 98  THR   B O   1 
ATOM   3146 C  CB  . THR   B 1 98  ? 10.898  -10.306 6.171   1.00 32.39  ? 98  THR   B CB  1 
ATOM   3147 O  OG1 . THR   B 1 98  ? 10.104  -11.433 6.524   1.00 31.57  ? 98  THR   B OG1 1 
ATOM   3148 C  CG2 . THR   B 1 98  ? 10.173  -9.049  6.621   1.00 32.96  ? 98  THR   B CG2 1 
ATOM   3149 N  N   . PRO   B 1 99  ? 11.364  -8.233  3.353   1.00 28.91  ? 99  PRO   B N   1 
ATOM   3150 C  CA  . PRO   B 1 99  ? 12.061  -6.979  3.040   1.00 27.66  ? 99  PRO   B CA  1 
ATOM   3151 C  C   . PRO   B 1 99  ? 11.972  -5.915  4.130   1.00 26.57  ? 99  PRO   B C   1 
ATOM   3152 O  O   . PRO   B 1 99  ? 11.220  -6.051  5.084   1.00 25.66  ? 99  PRO   B O   1 
ATOM   3153 C  CB  . PRO   B 1 99  ? 11.359  -6.536  1.771   1.00 29.07  ? 99  PRO   B CB  1 
ATOM   3154 C  CG  . PRO   B 1 99  ? 9.950   -7.047  1.939   1.00 30.96  ? 99  PRO   B CG  1 
ATOM   3155 C  CD  . PRO   B 1 99  ? 10.077  -8.378  2.654   1.00 31.11  ? 99  PRO   B CD  1 
ATOM   3156 N  N   . LYS   B 1 100 ? 12.750  -4.840  3.990   1.00 25.81  ? 100 LYS   B N   1 
ATOM   3157 C  CA  . LYS   B 1 100 ? 12.485  -3.628  4.751   1.00 28.07  ? 100 LYS   B CA  1 
ATOM   3158 C  C   . LYS   B 1 100 ? 11.077  -3.160  4.370   1.00 26.96  ? 100 LYS   B C   1 
ATOM   3159 O  O   . LYS   B 1 100 ? 10.840  -2.967  3.178   1.00 28.93  ? 100 LYS   B O   1 
ATOM   3160 C  CB  . LYS   B 1 100 ? 13.594  -2.615  4.439   1.00 31.56  ? 100 LYS   B CB  1 
ATOM   3161 C  CG  . LYS   B 1 100 ? 13.465  -1.260  5.118   1.00 42.63  ? 100 LYS   B CG  1 
ATOM   3162 C  CD  . LYS   B 1 100 ? 14.531  -0.231  4.731   1.00 51.34  ? 100 LYS   B CD  1 
ATOM   3163 C  CE  . LYS   B 1 100 ? 14.274  1.157   5.243   1.00 56.57  ? 100 LYS   B CE  1 
ATOM   3164 N  NZ  . LYS   B 1 100 ? 13.855  1.149   6.653   1.00 64.76  ? 100 LYS   B NZ  1 
ATOM   3165 N  N   . TYR   B 1 101 ? 10.139  -3.023  5.334   1.00 23.70  ? 101 TYR   B N   1 
ATOM   3166 C  CA  . TYR   B 1 101 ? 8.765   -2.642  5.005   1.00 23.73  ? 101 TYR   B CA  1 
ATOM   3167 C  C   . TYR   B 1 101 ? 8.102   -1.780  6.091   1.00 26.57  ? 101 TYR   B C   1 
ATOM   3168 O  O   . TYR   B 1 101 ? 8.544   -1.717  7.251   1.00 23.06  ? 101 TYR   B O   1 
ATOM   3169 C  CB  . TYR   B 1 101 ? 7.899   -3.888  4.765   1.00 24.26  ? 101 TYR   B CB  1 
ATOM   3170 C  CG  . TYR   B 1 101 ? 7.444   -4.607  6.032   1.00 25.13  ? 101 TYR   B CG  1 
ATOM   3171 C  CD1 . TYR   B 1 101 ? 8.208   -5.623  6.608   1.00 25.18  ? 101 TYR   B CD1 1 
ATOM   3172 C  CD2 . TYR   B 1 101 ? 6.252   -4.269  6.655   1.00 22.65  ? 101 TYR   B CD2 1 
ATOM   3173 C  CE1 . TYR   B 1 101 ? 7.803   -6.259  7.773   1.00 25.30  ? 101 TYR   B CE1 1 
ATOM   3174 C  CE2 . TYR   B 1 101 ? 5.838   -4.903  7.813   1.00 23.71  ? 101 TYR   B CE2 1 
ATOM   3175 C  CZ  . TYR   B 1 101 ? 6.608   -5.898  8.381   1.00 26.27  ? 101 TYR   B CZ  1 
ATOM   3176 O  OH  . TYR   B 1 101 ? 6.162   -6.505  9.535   1.00 26.36  ? 101 TYR   B OH  1 
ATOM   3177 N  N   . LYS   B 1 102 ? 7.026   -1.082  5.692   1.00 25.27  ? 102 LYS   B N   1 
ATOM   3178 C  CA  . LYS   B 1 102 ? 6.042   -0.599  6.648   1.00 28.44  ? 102 LYS   B CA  1 
ATOM   3179 C  C   . LYS   B 1 102 ? 4.629   -0.645  6.054   1.00 25.94  ? 102 LYS   B C   1 
ATOM   3180 O  O   . LYS   B 1 102 ? 4.465   -0.753  4.841   1.00 26.22  ? 102 LYS   B O   1 
ATOM   3181 C  CB  . LYS   B 1 102 ? 6.451   0.801   7.105   1.00 33.82  ? 102 LYS   B CB  1 
ATOM   3182 C  CG  . LYS   B 1 102 ? 6.477   1.863   6.045   1.00 38.84  ? 102 LYS   B CG  1 
ATOM   3183 C  CD  . LYS   B 1 102 ? 6.516   3.273   6.621   1.00 46.18  ? 102 LYS   B CD  1 
ATOM   3184 C  CE  . LYS   B 1 102 ? 7.882   3.781   6.913   1.00 50.93  ? 102 LYS   B CE  1 
ATOM   3185 N  NZ  . LYS   B 1 102 ? 8.403   4.485   5.739   1.00 57.24  ? 102 LYS   B NZ  1 
ATOM   3186 N  N   . PHE   B 1 103 ? 3.617   -0.542  6.931   1.00 23.08  ? 103 PHE   B N   1 
ATOM   3187 C  CA  . PHE   B 1 103 ? 2.218   -0.418  6.546   1.00 23.33  ? 103 PHE   B CA  1 
ATOM   3188 C  C   . PHE   B 1 103 ? 1.824   1.065   6.448   1.00 23.67  ? 103 PHE   B C   1 
ATOM   3189 O  O   . PHE   B 1 103 ? 2.078   1.832   7.363   1.00 24.85  ? 103 PHE   B O   1 
ATOM   3190 C  CB  . PHE   B 1 103 ? 1.378   -1.145  7.606   1.00 25.34  ? 103 PHE   B CB  1 
ATOM   3191 C  CG  . PHE   B 1 103 ? 1.486   -2.666  7.667   1.00 23.56  ? 103 PHE   B CG  1 
ATOM   3192 C  CD1 . PHE   B 1 103 ? 2.102   -3.399  6.655   1.00 22.08  ? 103 PHE   B CD1 1 
ATOM   3193 C  CD2 . PHE   B 1 103 ? 0.950   -3.357  8.747   1.00 24.51  ? 103 PHE   B CD2 1 
ATOM   3194 C  CE1 . PHE   B 1 103 ? 2.195   -4.787  6.733   1.00 22.65  ? 103 PHE   B CE1 1 
ATOM   3195 C  CE2 . PHE   B 1 103 ? 1.020   -4.751  8.802   1.00 23.57  ? 103 PHE   B CE2 1 
ATOM   3196 C  CZ  . PHE   B 1 103 ? 1.641   -5.459  7.808   1.00 21.17  ? 103 PHE   B CZ  1 
ATOM   3197 N  N   . VAL   B 1 104 ? 1.200   1.483   5.347   1.00 23.18  ? 104 VAL   B N   1 
ATOM   3198 C  CA  . VAL   B 1 104 ? 0.772   2.874   5.190   1.00 27.84  ? 104 VAL   B CA  1 
ATOM   3199 C  C   . VAL   B 1 104 ? -0.662  2.906   4.659   1.00 26.15  ? 104 VAL   B C   1 
ATOM   3200 O  O   . VAL   B 1 104 ? -1.081  1.970   3.979   1.00 28.65  ? 104 VAL   B O   1 
ATOM   3201 C  CB  . VAL   B 1 104 ? 1.742   3.634   4.261   1.00 33.09  ? 104 VAL   B CB  1 
ATOM   3202 C  CG1 . VAL   B 1 104 ? 1.301   5.072   4.043   1.00 38.77  ? 104 VAL   B CG1 1 
ATOM   3203 C  CG2 . VAL   B 1 104 ? 3.180   3.611   4.798   1.00 33.50  ? 104 VAL   B CG2 1 
ATOM   3204 N  N   . ARG   B 1 105 ? -1.426  3.968   4.976   1.00 23.60  ? 105 ARG   B N   1 
ATOM   3205 C  CA  . ARG   B 1 105 ? -2.743  4.173   4.372   1.00 23.99  ? 105 ARG   B CA  1 
ATOM   3206 C  C   . ARG   B 1 105 ? -2.642  5.282   3.327   1.00 24.79  ? 105 ARG   B C   1 
ATOM   3207 O  O   . ARG   B 1 105 ? -2.105  6.339   3.647   1.00 26.86  ? 105 ARG   B O   1 
ATOM   3208 C  CB  . ARG   B 1 105 ? -3.788  4.569   5.424   1.00 26.03  ? 105 ARG   B CB  1 
ATOM   3209 C  CG  . ARG   B 1 105 ? -5.223  4.640   4.918   1.00 25.62  ? 105 ARG   B CG  1 
ATOM   3210 C  CD  . ARG   B 1 105 ? -6.229  4.814   6.022   1.00 25.35  ? 105 ARG   B CD  1 
ATOM   3211 N  NE  . ARG   B 1 105 ? -7.615  4.924   5.552   1.00 23.46  ? 105 ARG   B NE  1 
ATOM   3212 C  CZ  . ARG   B 1 105 ? -8.454  3.920   5.310   1.00 23.44  ? 105 ARG   B CZ  1 
ATOM   3213 N  NH1 . ARG   B 1 105 ? -8.089  2.667   5.524   1.00 23.14  ? 105 ARG   B NH1 1 
ATOM   3214 N  NH2 . ARG   B 1 105 ? -9.672  4.165   4.820   1.00 25.58  ? 105 ARG   B NH2 1 
ATOM   3215 N  N   . ILE   B 1 106 ? -3.151  5.057   2.101   1.00 24.41  ? 106 ILE   B N   1 
ATOM   3216 C  CA  . ILE   B 1 106 ? -3.040  6.064   1.052   1.00 26.00  ? 106 ILE   B CA  1 
ATOM   3217 C  C   . ILE   B 1 106 ? -4.286  6.942   0.950   1.00 26.49  ? 106 ILE   B C   1 
ATOM   3218 O  O   . ILE   B 1 106 ? -5.355  6.632   1.473   1.00 25.59  ? 106 ILE   B O   1 
ATOM   3219 C  CB  . ILE   B 1 106 ? -2.701  5.464   -0.325  1.00 30.29  ? 106 ILE   B CB  1 
ATOM   3220 C  CG1 . ILE   B 1 106 ? -3.618  4.326   -0.695  1.00 29.50  ? 106 ILE   B CG1 1 
ATOM   3221 C  CG2 . ILE   B 1 106 ? -1.223  5.076   -0.411  1.00 33.64  ? 106 ILE   B CG2 1 
ATOM   3222 C  CD1 . ILE   B 1 106 ? -3.734  4.121   -2.186  1.00 34.39  ? 106 ILE   B CD1 1 
ATOM   3223 N  N   . GLN   B 1 107 ? -4.107  8.074   0.263   1.00 32.86  ? 107 GLN   B N   1 
ATOM   3224 C  CA  . GLN   B 1 107 ? -5.171  9.045   0.034   1.00 36.32  ? 107 GLN   B CA  1 
ATOM   3225 C  C   . GLN   B 1 107 ? -5.786  8.802   -1.340  1.00 32.77  ? 107 GLN   B C   1 
ATOM   3226 O  O   . GLN   B 1 107 ? -5.104  8.280   -2.218  1.00 27.09  ? 107 GLN   B O   1 
ATOM   3227 C  CB  . GLN   B 1 107 ? -4.595  10.463  0.009   1.00 41.40  ? 107 GLN   B CB  1 
ATOM   3228 C  CG  . GLN   B 1 107 ? -3.930  10.896  1.311   1.00 48.90  ? 107 GLN   B CG  1 
ATOM   3229 C  CD  . GLN   B 1 107 ? -4.898  10.798  2.462   1.00 55.65  ? 107 GLN   B CD  1 
ATOM   3230 O  OE1 . GLN   B 1 107 ? -6.024  11.298  2.379   1.00 64.96  ? 107 GLN   B OE1 1 
ATOM   3231 N  NE2 . GLN   B 1 107 ? -4.509  10.072  3.501   1.00 65.82  ? 107 GLN   B NE2 1 
ATOM   3232 N  N   . PRO   B 1 108 ? -7.058  9.207   -1.570  1.00 34.34  ? 108 PRO   B N   1 
ATOM   3233 C  CA  . PRO   B 1 108 ? -7.652  9.229   -2.911  1.00 34.96  ? 108 PRO   B CA  1 
ATOM   3234 C  C   . PRO   B 1 108 ? -6.811  10.072  -3.863  1.00 29.48  ? 108 PRO   B C   1 
ATOM   3235 O  O   . PRO   B 1 108 ? -6.352  11.138  -3.469  1.00 27.92  ? 108 PRO   B O   1 
ATOM   3236 C  CB  . PRO   B 1 108 ? -9.052  9.855   -2.728  1.00 37.10  ? 108 PRO   B CB  1 
ATOM   3237 C  CG  . PRO   B 1 108 ? -9.340  9.764   -1.243  1.00 36.26  ? 108 PRO   B CG  1 
ATOM   3238 C  CD  . PRO   B 1 108 ? -7.997  9.685   -0.538  1.00 37.48  ? 108 PRO   B CD  1 
ATOM   3239 N  N   . GLY   B 1 109 ? -6.618  9.580   -5.095  1.00 27.78  ? 109 GLY   B N   1 
ATOM   3240 C  CA  . GLY   B 1 109 ? -5.776  10.233  -6.095  1.00 26.32  ? 109 GLY   B CA  1 
ATOM   3241 C  C   . GLY   B 1 109 ? -4.359  9.659   -6.185  1.00 26.91  ? 109 GLY   B C   1 
ATOM   3242 O  O   . GLY   B 1 109 ? -3.658  9.889   -7.180  1.00 27.89  ? 109 GLY   B O   1 
ATOM   3243 N  N   . GLN   B 1 110 ? -3.894  8.988   -5.123  1.00 24.82  ? 110 GLN   B N   1 
ATOM   3244 C  CA  . GLN   B 1 110 ? -2.549  8.420   -5.104  1.00 24.68  ? 110 GLN   B CA  1 
ATOM   3245 C  C   . GLN   B 1 110 ? -2.571  7.080   -5.835  1.00 22.23  ? 110 GLN   B C   1 
ATOM   3246 O  O   . GLN   B 1 110 ? -3.619  6.422   -5.866  1.00 20.90  ? 110 GLN   B O   1 
ATOM   3247 C  CB  . GLN   B 1 110 ? -2.008  8.300   -3.673  1.00 29.54  ? 110 GLN   B CB  1 
ATOM   3248 C  CG  . GLN   B 1 110 ? -1.891  9.633   -2.936  1.00 40.86  ? 110 GLN   B CG  1 
ATOM   3249 C  CD  . GLN   B 1 110 ? -1.243  9.541   -1.559  1.00 58.85  ? 110 GLN   B CD  1 
ATOM   3250 O  OE1 . GLN   B 1 110 ? -1.593  8.712   -0.700  1.00 64.53  ? 110 GLN   B OE1 1 
ATOM   3251 N  NE2 . GLN   B 1 110 ? -0.277  10.416  -1.312  1.00 65.46  ? 110 GLN   B NE2 1 
ATOM   3252 N  N   . THR   B 1 111 ? -1.427  6.676   -6.417  1.00 21.70  ? 111 THR   B N   1 
ATOM   3253 C  CA  . THR   B 1 111 ? -1.348  5.427   -7.182  1.00 22.96  ? 111 THR   B CA  1 
ATOM   3254 C  C   . THR   B 1 111 ? -0.550  4.361   -6.411  1.00 22.71  ? 111 THR   B C   1 
ATOM   3255 O  O   . THR   B 1 111 ? 0.142   4.645   -5.431  1.00 23.57  ? 111 THR   B O   1 
ATOM   3256 C  CB  . THR   B 1 111 ? -0.743  5.671   -8.568  1.00 23.09  ? 111 THR   B CB  1 
ATOM   3257 O  OG1 . THR   B 1 111 ? 0.504   6.334   -8.399  1.00 23.46  ? 111 THR   B OG1 1 
ATOM   3258 C  CG2 . THR   B 1 111 ? -1.613  6.521   -9.473  1.00 25.47  ? 111 THR   B CG2 1 
ATOM   3259 N  N   . PHE   B 1 112 ? -0.637  3.116   -6.880  1.00 22.76  ? 112 PHE   B N   1 
ATOM   3260 C  CA  . PHE   B 1 112 ? 0.130   2.014   -6.312  1.00 22.91  ? 112 PHE   B CA  1 
ATOM   3261 C  C   . PHE   B 1 112 ? 0.102   0.820   -7.276  1.00 21.03  ? 112 PHE   B C   1 
ATOM   3262 O  O   . PHE   B 1 112 ? -0.749  0.752   -8.165  1.00 17.42  ? 112 PHE   B O   1 
ATOM   3263 C  CB  . PHE   B 1 112 ? -0.387  1.583   -4.930  1.00 22.24  ? 112 PHE   B CB  1 
ATOM   3264 C  CG  . PHE   B 1 112 ? -1.846  1.124   -4.875  1.00 22.96  ? 112 PHE   B CG  1 
ATOM   3265 C  CD1 . PHE   B 1 112 ? -2.878  2.044   -4.769  1.00 22.87  ? 112 PHE   B CD1 1 
ATOM   3266 C  CD2 . PHE   B 1 112 ? -2.180  -0.233  -4.886  1.00 22.54  ? 112 PHE   B CD2 1 
ATOM   3267 C  CE1 . PHE   B 1 112 ? -4.209  1.626   -4.698  1.00 24.57  ? 112 PHE   B CE1 1 
ATOM   3268 C  CE2 . PHE   B 1 112 ? -3.500  -0.651  -4.796  1.00 24.39  ? 112 PHE   B CE2 1 
ATOM   3269 C  CZ  . PHE   B 1 112 ? -4.515  0.278   -4.708  1.00 25.69  ? 112 PHE   B CZ  1 
ATOM   3270 N  N   . SER   B 1 113 ? 1.041   -0.115  -7.061  1.00 20.47  ? 113 SER   B N   1 
ATOM   3271 C  CA  . SER   B 1 113 ? 1.145   -1.350  -7.842  1.00 20.57  ? 113 SER   B CA  1 
ATOM   3272 C  C   . SER   B 1 113 ? 0.408   -2.488  -7.138  1.00 20.24  ? 113 SER   B C   1 
ATOM   3273 O  O   . SER   B 1 113 ? 0.530   -2.611  -5.920  1.00 18.25  ? 113 SER   B O   1 
ATOM   3274 C  CB  . SER   B 1 113 ? 2.587   -1.735  -8.020  1.00 23.72  ? 113 SER   B CB  1 
ATOM   3275 O  OG  . SER   B 1 113 ? 3.338   -0.710  -8.658  1.00 26.43  ? 113 SER   B OG  1 
ATOM   3276 N  N   . VAL   B 1 114 ? -0.310  -3.325  -7.918  1.00 20.74  ? 114 VAL   B N   1 
ATOM   3277 C  CA  . VAL   B 1 114 ? -1.045  -4.492  -7.453  1.00 22.55  ? 114 VAL   B CA  1 
ATOM   3278 C  C   . VAL   B 1 114 ? -0.339  -5.738  -7.982  1.00 23.77  ? 114 VAL   B C   1 
ATOM   3279 O  O   . VAL   B 1 114 ? -0.165  -5.866  -9.194  1.00 21.64  ? 114 VAL   B O   1 
ATOM   3280 C  CB  . VAL   B 1 114 ? -2.496  -4.485  -7.987  1.00 25.32  ? 114 VAL   B CB  1 
ATOM   3281 C  CG1 . VAL   B 1 114 ? -3.230  -5.811  -7.774  1.00 26.21  ? 114 VAL   B CG1 1 
ATOM   3282 C  CG2 . VAL   B 1 114 ? -3.335  -3.312  -7.478  1.00 26.24  ? 114 VAL   B CG2 1 
ATOM   3283 N  N   . LEU   B 1 115 ? -0.043  -6.700  -7.100  1.00 22.61  ? 115 LEU   B N   1 
ATOM   3284 C  CA  . LEU   B 1 115 ? 0.430   -8.006  -7.543  1.00 22.15  ? 115 LEU   B CA  1 
ATOM   3285 C  C   . LEU   B 1 115 ? -0.716  -9.019  -7.441  1.00 21.97  ? 115 LEU   B C   1 
ATOM   3286 O  O   . LEU   B 1 115 ? -0.989  -9.545  -6.362  1.00 22.02  ? 115 LEU   B O   1 
ATOM   3287 C  CB  . LEU   B 1 115 ? 1.664   -8.390  -6.717  1.00 22.12  ? 115 LEU   B CB  1 
ATOM   3288 C  CG  . LEU   B 1 115 ? 2.327   -9.728  -7.087  1.00 20.75  ? 115 LEU   B CG  1 
ATOM   3289 C  CD1 . LEU   B 1 115 ? 2.914   -9.741  -8.458  1.00 19.91  ? 115 LEU   B CD1 1 
ATOM   3290 C  CD2 . LEU   B 1 115 ? 3.377   -10.078 -6.069  1.00 22.11  ? 115 LEU   B CD2 1 
ATOM   3291 N  N   . ALA   B 1 116 ? -1.421  -9.258  -8.562  1.00 21.73  ? 116 ALA   B N   1 
ATOM   3292 C  CA  . ALA   B 1 116 ? -2.514  -10.223 -8.620  1.00 21.78  ? 116 ALA   B CA  1 
ATOM   3293 C  C   . ALA   B 1 116 ? -1.968  -11.637 -8.414  1.00 26.75  ? 116 ALA   B C   1 
ATOM   3294 O  O   . ALA   B 1 116 ? -0.975  -11.996 -9.062  1.00 29.92  ? 116 ALA   B O   1 
ATOM   3295 C  CB  . ALA   B 1 116 ? -3.233  -10.111 -9.955  1.00 21.05  ? 116 ALA   B CB  1 
ATOM   3296 N  N   . CYS   B 1 117 ? -2.600  -12.405 -7.495  1.00 27.93  ? 117 CYS   B N   1 
ATOM   3297 C  CA  . CYS   B 1 117 ? -2.144  -13.739 -7.098  1.00 30.17  ? 117 CYS   B CA  1 
ATOM   3298 C  C   . CYS   B 1 117 ? -3.313  -14.718 -6.992  1.00 28.57  ? 117 CYS   B C   1 
ATOM   3299 O  O   . CYS   B 1 117 ? -4.452  -14.309 -6.751  1.00 30.07  ? 117 CYS   B O   1 
ATOM   3300 C  CB  . CYS   B 1 117 ? -1.518  -13.751 -5.708  1.00 32.98  ? 117 CYS   B CB  1 
ATOM   3301 S  SG  . CYS   B 1 117 ? -0.006  -12.776 -5.522  1.00 36.11  ? 117 CYS   B SG  1 
ATOM   3302 N  N   . TYR   B 1 118 ? -2.997  -16.013 -7.138  1.00 29.60  ? 118 TYR   B N   1 
ATOM   3303 C  CA  . TYR   B 1 118 ? -3.958  -17.116 -7.190  1.00 30.68  ? 118 TYR   B CA  1 
ATOM   3304 C  C   . TYR   B 1 118 ? -3.290  -18.349 -6.563  1.00 33.14  ? 118 TYR   B C   1 
ATOM   3305 O  O   . TYR   B 1 118 ? -2.167  -18.693 -6.939  1.00 30.96  ? 118 TYR   B O   1 
ATOM   3306 C  CB  . TYR   B 1 118 ? -4.435  -17.454 -8.616  1.00 30.30  ? 118 TYR   B CB  1 
ATOM   3307 C  CG  . TYR   B 1 118 ? -5.228  -16.317 -9.239  1.00 31.57  ? 118 TYR   B CG  1 
ATOM   3308 C  CD1 . TYR   B 1 118 ? -6.581  -16.117 -8.929  1.00 33.63  ? 118 TYR   B CD1 1 
ATOM   3309 C  CD2 . TYR   B 1 118 ? -4.604  -15.371 -10.055 1.00 32.35  ? 118 TYR   B CD2 1 
ATOM   3310 C  CE1 . TYR   B 1 118 ? -7.283  -15.027 -9.433  1.00 31.37  ? 118 TYR   B CE1 1 
ATOM   3311 C  CE2 . TYR   B 1 118 ? -5.297  -14.273 -10.556 1.00 29.78  ? 118 TYR   B CE2 1 
ATOM   3312 C  CZ  . TYR   B 1 118 ? -6.628  -14.100 -10.236 1.00 28.81  ? 118 TYR   B CZ  1 
ATOM   3313 O  OH  . TYR   B 1 118 ? -7.275  -13.027 -10.760 1.00 28.88  ? 118 TYR   B OH  1 
ATOM   3314 N  N   . ASN   B 1 119 ? -3.943  -18.931 -5.539  1.00 35.36  ? 119 ASN   B N   1 
ATOM   3315 C  CA  . ASN   B 1 119 ? -3.422  -20.057 -4.772  1.00 35.75  ? 119 ASN   B CA  1 
ATOM   3316 C  C   . ASN   B 1 119 ? -2.017  -19.778 -4.246  1.00 35.44  ? 119 ASN   B C   1 
ATOM   3317 O  O   . ASN   B 1 119 ? -1.207  -20.687 -4.176  1.00 35.11  ? 119 ASN   B O   1 
ATOM   3318 C  CB  . ASN   B 1 119 ? -3.378  -21.355 -5.579  1.00 41.16  ? 119 ASN   B CB  1 
ATOM   3319 C  CG  . ASN   B 1 119 ? -4.705  -21.706 -6.216  1.00 47.38  ? 119 ASN   B CG  1 
ATOM   3320 O  OD1 . ASN   B 1 119 ? -4.755  -22.061 -7.396  1.00 53.15  ? 119 ASN   B OD1 1 
ATOM   3321 N  ND2 . ASN   B 1 119 ? -5.792  -21.625 -5.462  1.00 51.63  ? 119 ASN   B ND2 1 
ATOM   3322 N  N   . GLY   B 1 120 ? -1.713  -18.524 -3.893  1.00 33.00  ? 120 GLY   B N   1 
ATOM   3323 C  CA  . GLY   B 1 120 ? -0.431  -18.193 -3.301  1.00 29.06  ? 120 GLY   B CA  1 
ATOM   3324 C  C   . GLY   B 1 120 ? 0.641   -17.937 -4.355  1.00 29.67  ? 120 GLY   B C   1 
ATOM   3325 O  O   . GLY   B 1 120 ? 1.775   -17.626 -4.014  1.00 30.56  ? 120 GLY   B O   1 
ATOM   3326 N  N   . SER   B 1 121 ? 0.280   -18.022 -5.629  1.00 29.83  ? 121 SER   B N   1 
ATOM   3327 C  CA  . SER   B 1 121 ? 1.264   -17.884 -6.694  1.00 33.53  ? 121 SER   B CA  1 
ATOM   3328 C  C   . SER   B 1 121 ? 1.067   -16.589 -7.497  1.00 27.81  ? 121 SER   B C   1 
ATOM   3329 O  O   . SER   B 1 121 ? -0.007  -16.367 -8.052  1.00 27.01  ? 121 SER   B O   1 
ATOM   3330 C  CB  . SER   B 1 121 ? 1.224   -19.072 -7.595  1.00 37.74  ? 121 SER   B CB  1 
ATOM   3331 O  OG  . SER   B 1 121 ? 2.442   -19.103 -8.324  1.00 49.13  ? 121 SER   B OG  1 
ATOM   3332 N  N   . PRO   B 1 122 ? 2.074   -15.683 -7.548  1.00 31.01  ? 122 PRO   B N   1 
ATOM   3333 C  CA  . PRO   B 1 122 ? 1.958   -14.429 -8.305  1.00 29.81  ? 122 PRO   B CA  1 
ATOM   3334 C  C   . PRO   B 1 122 ? 1.674   -14.623 -9.789  1.00 30.47  ? 122 PRO   B C   1 
ATOM   3335 O  O   . PRO   B 1 122 ? 2.366   -15.392 -10.442 1.00 29.09  ? 122 PRO   B O   1 
ATOM   3336 C  CB  . PRO   B 1 122 ? 3.314   -13.760 -8.084  1.00 30.20  ? 122 PRO   B CB  1 
ATOM   3337 C  CG  . PRO   B 1 122 ? 3.761   -14.300 -6.753  1.00 30.37  ? 122 PRO   B CG  1 
ATOM   3338 C  CD  . PRO   B 1 122 ? 3.329   -15.752 -6.765  1.00 28.57  ? 122 PRO   B CD  1 
ATOM   3339 N  N   . SER   B 1 123 ? 0.684   -13.887 -10.305 1.00 27.51  ? 123 SER   B N   1 
ATOM   3340 C  CA  . SER   B 1 123 ? 0.192   -14.055 -11.661 1.00 29.79  ? 123 SER   B CA  1 
ATOM   3341 C  C   . SER   B 1 123 ? 0.471   -12.841 -12.569 1.00 27.87  ? 123 SER   B C   1 
ATOM   3342 O  O   . SER   B 1 123 ? 0.732   -13.005 -13.761 1.00 27.70  ? 123 SER   B O   1 
ATOM   3343 C  CB  . SER   B 1 123 ? -1.266  -14.354 -11.572 1.00 32.97  ? 123 SER   B CB  1 
ATOM   3344 O  OG  . SER   B 1 123 ? -1.820  -14.534 -12.860 1.00 42.11  ? 123 SER   B OG  1 
ATOM   3345 N  N   . GLY   B 1 124 ? 0.399   -11.607 -12.039 1.00 25.43  ? 124 GLY   B N   1 
ATOM   3346 C  CA  . GLY   B 1 124 ? 0.594   -10.418 -12.858 1.00 23.88  ? 124 GLY   B CA  1 
ATOM   3347 C  C   . GLY   B 1 124 ? 0.692   -9.160  -12.000 1.00 21.93  ? 124 GLY   B C   1 
ATOM   3348 O  O   . GLY   B 1 124 ? 0.333   -9.197  -10.842 1.00 24.00  ? 124 GLY   B O   1 
ATOM   3349 N  N   A VAL   B 1 125 ? 1.191   -8.074  -12.604 0.13 22.93  ? 125 VAL   B N   1 
ATOM   3350 N  N   B VAL   B 1 125 ? 1.176   -8.056  -12.585 0.37 22.73  ? 125 VAL   B N   1 
ATOM   3351 N  N   C VAL   B 1 125 ? 1.191   -8.074  -12.604 0.13 22.93  ? 125 VAL   B N   1 
ATOM   3352 N  N   D VAL   B 1 125 ? 1.176   -8.056  -12.585 0.37 22.73  ? 125 VAL   B N   1 
ATOM   3353 C  CA  A VAL   B 1 125 ? 1.380   -6.802  -11.924 0.13 23.13  ? 125 VAL   B CA  1 
ATOM   3354 C  CA  B VAL   B 1 125 ? 1.373   -6.806  -11.862 0.37 22.79  ? 125 VAL   B CA  1 
ATOM   3355 C  CA  C VAL   B 1 125 ? 1.380   -6.802  -11.924 0.13 23.13  ? 125 VAL   B CA  1 
ATOM   3356 C  CA  D VAL   B 1 125 ? 1.373   -6.806  -11.862 0.37 22.79  ? 125 VAL   B CA  1 
ATOM   3357 C  C   A VAL   B 1 125 ? 0.742   -5.703  -12.771 0.13 23.54  ? 125 VAL   B C   1 
ATOM   3358 C  C   B VAL   B 1 125 ? 0.899   -5.635  -12.724 0.37 23.40  ? 125 VAL   B C   1 
ATOM   3359 C  C   C VAL   B 1 125 ? 0.742   -5.703  -12.771 0.13 23.54  ? 125 VAL   B C   1 
ATOM   3360 C  C   D VAL   B 1 125 ? 0.899   -5.635  -12.724 0.37 23.40  ? 125 VAL   B C   1 
ATOM   3361 O  O   A VAL   B 1 125 ? 0.766   -5.769  -13.999 0.13 23.61  ? 125 VAL   B O   1 
ATOM   3362 O  O   B VAL   B 1 125 ? 1.217   -5.564  -13.909 0.37 22.51  ? 125 VAL   B O   1 
ATOM   3363 O  O   C VAL   B 1 125 ? 0.766   -5.769  -13.999 0.13 23.61  ? 125 VAL   B O   1 
ATOM   3364 O  O   D VAL   B 1 125 ? 1.217   -5.564  -13.909 0.37 22.51  ? 125 VAL   B O   1 
ATOM   3365 C  CB  A VAL   B 1 125 ? 2.869   -6.487  -11.672 0.13 23.39  ? 125 VAL   B CB  1 
ATOM   3366 C  CB  B VAL   B 1 125 ? 2.839   -6.623  -11.411 0.37 23.52  ? 125 VAL   B CB  1 
ATOM   3367 C  CB  C VAL   B 1 125 ? 2.869   -6.487  -11.672 0.13 23.39  ? 125 VAL   B CB  1 
ATOM   3368 C  CB  D VAL   B 1 125 ? 2.839   -6.623  -11.411 0.37 23.52  ? 125 VAL   B CB  1 
ATOM   3369 C  CG1 A VAL   B 1 125 ? 3.046   -5.397  -10.622 0.13 23.66  ? 125 VAL   B CG1 1 
ATOM   3370 C  CG1 B VAL   B 1 125 ? 3.818   -6.506  -12.579 0.37 24.01  ? 125 VAL   B CG1 1 
ATOM   3371 C  CG1 C VAL   B 1 125 ? 3.046   -5.397  -10.622 0.13 23.66  ? 125 VAL   B CG1 1 
ATOM   3372 C  CG1 D VAL   B 1 125 ? 3.818   -6.506  -12.579 0.37 24.01  ? 125 VAL   B CG1 1 
ATOM   3373 C  CG2 A VAL   B 1 125 ? 3.663   -7.728  -11.283 0.13 23.50  ? 125 VAL   B CG2 1 
ATOM   3374 C  CG2 B VAL   B 1 125 ? 3.002   -5.439  -10.466 0.37 24.35  ? 125 VAL   B CG2 1 
ATOM   3375 C  CG2 C VAL   B 1 125 ? 3.663   -7.728  -11.283 0.13 23.50  ? 125 VAL   B CG2 1 
ATOM   3376 C  CG2 D VAL   B 1 125 ? 3.002   -5.439  -10.466 0.37 24.35  ? 125 VAL   B CG2 1 
ATOM   3377 N  N   . TYR   B 1 126 ? 0.164   -4.698  -12.104 1.00 24.10  ? 126 TYR   B N   1 
ATOM   3378 C  CA  . TYR   B 1 126 ? -0.334  -3.510  -12.797 1.00 22.36  ? 126 TYR   B CA  1 
ATOM   3379 C  C   . TYR   B 1 126 ? -0.522  -2.370  -11.799 1.00 21.68  ? 126 TYR   B C   1 
ATOM   3380 O  O   . TYR   B 1 126 ? -0.661  -2.602  -10.604 1.00 20.00  ? 126 TYR   B O   1 
ATOM   3381 C  CB  . TYR   B 1 126 ? -1.647  -3.788  -13.535 1.00 24.61  ? 126 TYR   B CB  1 
ATOM   3382 C  CG  . TYR   B 1 126 ? -2.753  -4.454  -12.700 1.00 26.30  ? 126 TYR   B CG  1 
ATOM   3383 C  CD1 . TYR   B 1 126 ? -3.698  -3.716  -11.985 1.00 24.98  ? 126 TYR   B CD1 1 
ATOM   3384 C  CD2 . TYR   B 1 126 ? -2.866  -5.838  -12.652 1.00 24.84  ? 126 TYR   B CD2 1 
ATOM   3385 C  CE1 . TYR   B 1 126 ? -4.683  -4.331  -11.222 1.00 26.96  ? 126 TYR   B CE1 1 
ATOM   3386 C  CE2 . TYR   B 1 126 ? -3.855  -6.463  -11.904 1.00 26.59  ? 126 TYR   B CE2 1 
ATOM   3387 C  CZ  . TYR   B 1 126 ? -4.776  -5.719  -11.193 1.00 27.16  ? 126 TYR   B CZ  1 
ATOM   3388 O  OH  . TYR   B 1 126 ? -5.751  -6.404  -10.499 1.00 30.01  ? 126 TYR   B OH  1 
ATOM   3389 N  N   . GLN   B 1 127 ? -0.573  -1.140  -12.326 1.00 20.83  ? 127 GLN   B N   1 
ATOM   3390 C  CA  . GLN   B 1 127 ? -0.772  0.094   -11.570 1.00 23.88  ? 127 GLN   B CA  1 
ATOM   3391 C  C   . GLN   B 1 127 ? -2.272  0.443   -11.441 1.00 25.99  ? 127 GLN   B C   1 
ATOM   3392 O  O   . GLN   B 1 127 ? -3.031  0.248   -12.386 1.00 26.07  ? 127 GLN   B O   1 
ATOM   3393 C  CB  . GLN   B 1 127 ? -0.010  1.043   -12.494 1.00 26.53  ? 127 GLN   B CB  1 
ATOM   3394 C  CG  . GLN   B 1 127 ? 0.594   2.290   -11.873 1.00 30.45  ? 127 GLN   B CG  1 
ATOM   3395 C  CD  . GLN   B 1 127 ? 1.595   2.107   -10.751 1.00 30.18  ? 127 GLN   B CD  1 
ATOM   3396 O  OE1 . GLN   B 1 127 ? 1.982   1.010   -10.300 1.00 25.50  ? 127 GLN   B OE1 1 
ATOM   3397 N  NE2 . GLN   B 1 127 ? 1.964   3.273   -10.241 1.00 31.30  ? 127 GLN   B NE2 1 
ATOM   3398 N  N   A CYS   B 1 128 ? -2.686  0.903   -10.247 0.39 25.94  ? 128 CYS   B N   1 
ATOM   3399 N  N   B CYS   B 1 128 ? -2.673  0.996   -10.293 0.11 25.68  ? 128 CYS   B N   1 
ATOM   3400 N  N   C CYS   B 1 128 ? -2.686  0.903   -10.247 0.39 25.94  ? 128 CYS   B N   1 
ATOM   3401 N  N   D CYS   B 1 128 ? -2.673  0.996   -10.293 0.11 25.68  ? 128 CYS   B N   1 
ATOM   3402 C  CA  A CYS   B 1 128 ? -4.028  1.425   -10.001 0.39 27.12  ? 128 CYS   B CA  1 
ATOM   3403 C  CA  B CYS   B 1 128 ? -4.023  1.516   -10.156 0.11 25.83  ? 128 CYS   B CA  1 
ATOM   3404 C  CA  C CYS   B 1 128 ? -4.028  1.425   -10.001 0.39 27.12  ? 128 CYS   B CA  1 
ATOM   3405 C  CA  D CYS   B 1 128 ? -4.023  1.516   -10.156 0.11 25.83  ? 128 CYS   B CA  1 
ATOM   3406 C  C   A CYS   B 1 128 ? -3.956  2.758   -9.251  0.39 26.15  ? 128 CYS   B C   1 
ATOM   3407 C  C   B CYS   B 1 128 ? -4.049  2.679   -9.170  0.11 25.43  ? 128 CYS   B C   1 
ATOM   3408 C  C   C CYS   B 1 128 ? -3.956  2.758   -9.251  0.39 26.15  ? 128 CYS   B C   1 
ATOM   3409 C  C   D CYS   B 1 128 ? -4.049  2.679   -9.170  0.11 25.43  ? 128 CYS   B C   1 
ATOM   3410 O  O   A CYS   B 1 128 ? -2.986  3.018   -8.540  0.39 26.84  ? 128 CYS   B O   1 
ATOM   3411 O  O   B CYS   B 1 128 ? -3.258  2.735   -8.229  0.11 25.35  ? 128 CYS   B O   1 
ATOM   3412 O  O   C CYS   B 1 128 ? -2.986  3.018   -8.540  0.39 26.84  ? 128 CYS   B O   1 
ATOM   3413 O  O   D CYS   B 1 128 ? -3.258  2.735   -8.229  0.11 25.35  ? 128 CYS   B O   1 
ATOM   3414 C  CB  A CYS   B 1 128 ? -4.859  0.503   -9.106  0.39 28.91  ? 128 CYS   B CB  1 
ATOM   3415 C  CB  B CYS   B 1 128 ? -4.998  0.432   -9.713  0.11 26.43  ? 128 CYS   B CB  1 
ATOM   3416 C  CB  C CYS   B 1 128 ? -4.859  0.503   -9.106  0.39 28.91  ? 128 CYS   B CB  1 
ATOM   3417 C  CB  D CYS   B 1 128 ? -4.998  0.432   -9.713  0.11 26.43  ? 128 CYS   B CB  1 
ATOM   3418 S  SG  A CYS   B 1 128 ? -5.436  -1.023  -9.902  0.39 31.53  ? 128 CYS   B SG  1 
ATOM   3419 S  SG  B CYS   B 1 128 ? -4.701  -0.158  -8.028  0.11 26.08  ? 128 CYS   B SG  1 
ATOM   3420 S  SG  C CYS   B 1 128 ? -5.436  -1.023  -9.902  0.39 31.53  ? 128 CYS   B SG  1 
ATOM   3421 S  SG  D CYS   B 1 128 ? -4.701  -0.158  -8.028  0.11 26.08  ? 128 CYS   B SG  1 
ATOM   3422 N  N   . ALA   B 1 129 ? -4.998  3.590   -9.400  1.00 25.22  ? 129 ALA   B N   1 
ATOM   3423 C  CA  . ALA   B 1 129 ? -5.245  4.718   -8.507  1.00 23.72  ? 129 ALA   B CA  1 
ATOM   3424 C  C   . ALA   B 1 129 ? -6.406  4.367   -7.558  1.00 23.57  ? 129 ALA   B C   1 
ATOM   3425 O  O   . ALA   B 1 129 ? -7.339  3.670   -7.949  1.00 23.03  ? 129 ALA   B O   1 
ATOM   3426 C  CB  . ALA   B 1 129 ? -5.573  5.952   -9.319  1.00 25.15  ? 129 ALA   B CB  1 
ATOM   3427 N  N   . MET   B 1 130 ? -6.307  4.834   -6.306  1.00 22.93  ? 130 MET   B N   1 
ATOM   3428 C  CA  . MET   B 1 130 ? -7.417  4.915   -5.367  1.00 23.56  ? 130 MET   B CA  1 
ATOM   3429 C  C   . MET   B 1 130 ? -8.354  6.020   -5.858  1.00 25.50  ? 130 MET   B C   1 
ATOM   3430 O  O   . MET   B 1 130 ? -7.961  7.181   -5.909  1.00 26.54  ? 130 MET   B O   1 
ATOM   3431 C  CB  . MET   B 1 130 ? -6.878  5.207   -3.960  1.00 24.29  ? 130 MET   B CB  1 
ATOM   3432 C  CG  . MET   B 1 130 ? -7.928  5.250   -2.827  1.00 27.78  ? 130 MET   B CG  1 
ATOM   3433 S  SD  . MET   B 1 130 ? -8.888  3.730   -2.644  1.00 27.53  ? 130 MET   B SD  1 
ATOM   3434 C  CE  . MET   B 1 130 ? -7.613  2.589   -2.099  1.00 28.02  ? 130 MET   B CE  1 
ATOM   3435 N  N   . ARG   B 1 131 ? -9.559  5.643   -6.293  1.00 27.79  ? 131 ARG   B N   1 
ATOM   3436 C  CA  . ARG   B 1 131 ? -10.494 6.576   -6.903  1.00 28.53  ? 131 ARG   B CA  1 
ATOM   3437 C  C   . ARG   B 1 131 ? -11.047 7.473   -5.790  1.00 26.67  ? 131 ARG   B C   1 
ATOM   3438 O  O   . ARG   B 1 131 ? -10.985 7.088   -4.627  1.00 25.09  ? 131 ARG   B O   1 
ATOM   3439 C  CB  . ARG   B 1 131 ? -11.667 5.871   -7.603  1.00 29.28  ? 131 ARG   B CB  1 
ATOM   3440 C  CG  . ARG   B 1 131 ? -11.374 4.864   -8.712  1.00 33.20  ? 131 ARG   B CG  1 
ATOM   3441 C  CD  . ARG   B 1 131 ? -10.705 5.411   -9.948  1.00 29.56  ? 131 ARG   B CD  1 
ATOM   3442 N  NE  . ARG   B 1 131 ? -11.375 6.590   -10.499 1.00 28.30  ? 131 ARG   B NE  1 
ATOM   3443 C  CZ  . ARG   B 1 131 ? -10.749 7.476   -11.278 1.00 28.19  ? 131 ARG   B CZ  1 
ATOM   3444 N  NH1 . ARG   B 1 131 ? -9.571  7.180   -11.789 1.00 25.74  ? 131 ARG   B NH1 1 
ATOM   3445 N  NH2 . ARG   B 1 131 ? -11.285 8.654   -11.537 1.00 26.80  ? 131 ARG   B NH2 1 
ATOM   3446 N  N   . PRO   B 1 132 ? -11.525 8.706   -6.099  1.00 27.69  ? 132 PRO   B N   1 
ATOM   3447 C  CA  . PRO   B 1 132 ? -12.230 9.547   -5.122  1.00 27.07  ? 132 PRO   B CA  1 
ATOM   3448 C  C   . PRO   B 1 132 ? -13.382 8.877   -4.390  1.00 23.94  ? 132 PRO   B C   1 
ATOM   3449 O  O   . PRO   B 1 132 ? -13.652 9.255   -3.278  1.00 26.46  ? 132 PRO   B O   1 
ATOM   3450 C  CB  . PRO   B 1 132 ? -12.743 10.724  -5.991  1.00 28.17  ? 132 PRO   B CB  1 
ATOM   3451 C  CG  . PRO   B 1 132 ? -11.680 10.847  -7.085  1.00 27.45  ? 132 PRO   B CG  1 
ATOM   3452 C  CD  . PRO   B 1 132 ? -11.338 9.398   -7.394  1.00 27.05  ? 132 PRO   B CD  1 
ATOM   3453 N  N   . ASN   B 1 133 ? -14.031 7.887   -5.003  1.00 23.35  ? 133 ASN   B N   1 
ATOM   3454 C  CA  . ASN   B 1 133 ? -15.131 7.157   -4.388  1.00 25.11  ? 133 ASN   B CA  1 
ATOM   3455 C  C   . ASN   B 1 133 ? -14.651 5.899   -3.656  1.00 26.63  ? 133 ASN   B C   1 
ATOM   3456 O  O   . ASN   B 1 133 ? -15.473 5.039   -3.327  1.00 27.46  ? 133 ASN   B O   1 
ATOM   3457 C  CB  . ASN   B 1 133 ? -16.186 6.778   -5.431  1.00 23.14  ? 133 ASN   B CB  1 
ATOM   3458 C  CG  . ASN   B 1 133 ? -15.804 5.619   -6.324  1.00 25.50  ? 133 ASN   B CG  1 
ATOM   3459 O  OD1 . ASN   B 1 133 ? -14.651 5.159   -6.339  1.00 26.09  ? 133 ASN   B OD1 1 
ATOM   3460 N  ND2 . ASN   B 1 133 ? -16.742 5.172   -7.151  1.00 25.67  ? 133 ASN   B ND2 1 
ATOM   3461 N  N   . PHE   B 1 134 ? -13.328 5.728   -3.551  1.00 25.21  ? 134 PHE   B N   1 
ATOM   3462 C  CA  . PHE   B 1 134 ? -12.646 4.724   -2.730  1.00 25.11  ? 134 PHE   B CA  1 
ATOM   3463 C  C   . PHE   B 1 134 ? -12.745 3.306   -3.310  1.00 26.68  ? 134 PHE   B C   1 
ATOM   3464 O  O   . PHE   B 1 134 ? -12.449 2.341   -2.617  1.00 29.62  ? 134 PHE   B O   1 
ATOM   3465 C  CB  . PHE   B 1 134 ? -13.042 4.716   -1.251  1.00 23.91  ? 134 PHE   B CB  1 
ATOM   3466 C  CG  . PHE   B 1 134 ? -12.641 5.944   -0.447  1.00 27.15  ? 134 PHE   B CG  1 
ATOM   3467 C  CD1 . PHE   B 1 134 ? -11.330 6.115   0.004   1.00 28.20  ? 134 PHE   B CD1 1 
ATOM   3468 C  CD2 . PHE   B 1 134 ? -13.574 6.941   -0.156  1.00 29.08  ? 134 PHE   B CD2 1 
ATOM   3469 C  CE1 . PHE   B 1 134 ? -10.976 7.244   0.735   1.00 31.61  ? 134 PHE   B CE1 1 
ATOM   3470 C  CE2 . PHE   B 1 134 ? -13.217 8.069   0.568   1.00 28.31  ? 134 PHE   B CE2 1 
ATOM   3471 C  CZ  . PHE   B 1 134 ? -11.921 8.232   0.992   1.00 30.15  ? 134 PHE   B CZ  1 
ATOM   3472 N  N   . THR   B 1 135 ? -13.025 3.168   -4.608  1.00 27.83  ? 135 THR   B N   1 
ATOM   3473 C  CA  . THR   B 1 135 ? -12.835 1.898   -5.302  1.00 27.03  ? 135 THR   B CA  1 
ATOM   3474 C  C   . THR   B 1 135 ? -11.545 1.988   -6.120  1.00 25.96  ? 135 THR   B C   1 
ATOM   3475 O  O   . THR   B 1 135 ? -11.001 3.084   -6.242  1.00 25.11  ? 135 THR   B O   1 
ATOM   3476 C  CB  . THR   B 1 135 ? -14.033 1.622   -6.213  1.00 27.82  ? 135 THR   B CB  1 
ATOM   3477 O  OG1 . THR   B 1 135 ? -14.102 2.723   -7.121  1.00 27.47  ? 135 THR   B OG1 1 
ATOM   3478 C  CG2 . THR   B 1 135 ? -15.355 1.609   -5.469  1.00 30.39  ? 135 THR   B CG2 1 
ATOM   3479 N  N   . ILE   B 1 136 ? -11.076 0.833   -6.631  1.00 25.11  ? 136 ILE   B N   1 
ATOM   3480 C  CA  . ILE   B 1 136 ? -10.068 0.747   -7.682  1.00 26.60  ? 136 ILE   B CA  1 
ATOM   3481 C  C   . ILE   B 1 136 ? -10.635 -0.035  -8.887  1.00 28.51  ? 136 ILE   B C   1 
ATOM   3482 O  O   . ILE   B 1 136 ? -11.554 -0.853  -8.748  1.00 28.67  ? 136 ILE   B O   1 
ATOM   3483 C  CB  . ILE   B 1 136 ? -8.750  0.139   -7.145  1.00 27.51  ? 136 ILE   B CB  1 
ATOM   3484 C  CG1 . ILE   B 1 136 ? -8.836  -1.344  -6.831  1.00 25.74  ? 136 ILE   B CG1 1 
ATOM   3485 C  CG2 . ILE   B 1 136 ? -8.241  0.906   -5.917  1.00 29.99  ? 136 ILE   B CG2 1 
ATOM   3486 C  CD1 . ILE   B 1 136 ? -7.502  -1.966  -6.455  1.00 27.74  ? 136 ILE   B CD1 1 
ATOM   3487 N  N   . LYS   B 1 137 ? -10.093 0.240   -10.086 1.00 28.65  ? 137 LYS   B N   1 
ATOM   3488 C  CA  . LYS   B 1 137 ? -10.459 -0.452  -11.311 1.00 30.45  ? 137 LYS   B CA  1 
ATOM   3489 C  C   . LYS   B 1 137 ? -9.403  -1.508  -11.615 1.00 28.38  ? 137 LYS   B C   1 
ATOM   3490 O  O   . LYS   B 1 137 ? -8.403  -1.258  -12.291 1.00 26.86  ? 137 LYS   B O   1 
ATOM   3491 C  CB  . LYS   B 1 137 ? -10.608 0.555   -12.454 1.00 37.43  ? 137 LYS   B CB  1 
ATOM   3492 C  CG  . LYS   B 1 137 ? -11.854 1.400   -12.285 1.00 41.70  ? 137 LYS   B CG  1 
ATOM   3493 C  CD  . LYS   B 1 137 ? -12.007 2.584   -13.226 1.00 46.42  ? 137 LYS   B CD  1 
ATOM   3494 C  CE  . LYS   B 1 137 ? -13.284 3.271   -12.865 1.00 54.63  ? 137 LYS   B CE  1 
ATOM   3495 N  NZ  . LYS   B 1 137 ? -13.859 4.054   -13.962 1.00 59.94  ? 137 LYS   B NZ  1 
ATOM   3496 N  N   . GLY   B 1 138 ? -9.615  -2.706  -11.078 1.00 27.19  ? 138 GLY   B N   1 
ATOM   3497 C  CA  . GLY   B 1 138 ? -8.582  -3.728  -11.142 1.00 28.78  ? 138 GLY   B CA  1 
ATOM   3498 C  C   . GLY   B 1 138 ? -8.917  -4.771  -12.193 1.00 27.76  ? 138 GLY   B C   1 
ATOM   3499 O  O   . GLY   B 1 138 ? -9.812  -4.578  -13.011 1.00 31.00  ? 138 GLY   B O   1 
ATOM   3500 N  N   . SER   B 1 139 ? -8.209  -5.891  -12.133 1.00 27.12  ? 139 SER   B N   1 
ATOM   3501 C  CA  . SER   B 1 139 ? -8.597  -7.066  -12.880 1.00 27.67  ? 139 SER   B CA  1 
ATOM   3502 C  C   . SER   B 1 139 ? -8.371  -8.267  -11.970 1.00 30.83  ? 139 SER   B C   1 
ATOM   3503 O  O   . SER   B 1 139 ? -7.233  -8.561  -11.609 1.00 29.59  ? 139 SER   B O   1 
ATOM   3504 C  CB  . SER   B 1 139 ? -7.844  -7.161  -14.168 1.00 30.37  ? 139 SER   B CB  1 
ATOM   3505 O  OG  . SER   B 1 139 ? -7.936  -8.476  -14.695 1.00 31.82  ? 139 SER   B OG  1 
ATOM   3506 N  N   . PHE   B 1 140 ? -9.474  -8.890  -11.539 1.00 30.71  ? 140 PHE   B N   1 
ATOM   3507 C  CA  . PHE   B 1 140 ? -9.432  -9.908  -10.496 1.00 34.57  ? 140 PHE   B CA  1 
ATOM   3508 C  C   . PHE   B 1 140 ? -10.468 -11.002 -10.803 1.00 39.19  ? 140 PHE   B C   1 
ATOM   3509 O  O   . PHE   B 1 140 ? -11.558 -10.717 -11.313 1.00 35.20  ? 140 PHE   B O   1 
ATOM   3510 C  CB  . PHE   B 1 140 ? -9.692  -9.293  -9.113  1.00 36.89  ? 140 PHE   B CB  1 
ATOM   3511 C  CG  . PHE   B 1 140 ? -8.633  -8.361  -8.517  1.00 35.10  ? 140 PHE   B CG  1 
ATOM   3512 C  CD1 . PHE   B 1 140 ? -7.392  -8.851  -8.092  1.00 33.64  ? 140 PHE   B CD1 1 
ATOM   3513 C  CD2 . PHE   B 1 140 ? -8.908  -7.003  -8.317  1.00 34.98  ? 140 PHE   B CD2 1 
ATOM   3514 C  CE1 . PHE   B 1 140 ? -6.446  -8.004  -7.524  1.00 32.09  ? 140 PHE   B CE1 1 
ATOM   3515 C  CE2 . PHE   B 1 140 ? -7.956  -6.154  -7.750  1.00 34.97  ? 140 PHE   B CE2 1 
ATOM   3516 C  CZ  . PHE   B 1 140 ? -6.733  -6.658  -7.344  1.00 34.36  ? 140 PHE   B CZ  1 
ATOM   3517 N  N   . LEU   B 1 141 ? -10.092 -12.262 -10.536 1.00 40.25  ? 141 LEU   B N   1 
ATOM   3518 C  CA  . LEU   B 1 141 ? -10.997 -13.402 -10.636 1.00 43.25  ? 141 LEU   B CA  1 
ATOM   3519 C  C   . LEU   B 1 141 ? -11.070 -14.100 -9.279  1.00 43.01  ? 141 LEU   B C   1 
ATOM   3520 O  O   . LEU   B 1 141 ? -10.269 -13.818 -8.388  1.00 37.64  ? 141 LEU   B O   1 
ATOM   3521 C  CB  . LEU   B 1 141 ? -10.510 -14.370 -11.717 1.00 42.98  ? 141 LEU   B CB  1 
ATOM   3522 C  CG  . LEU   B 1 141 ? -10.274 -13.767 -13.107 1.00 42.26  ? 141 LEU   B CG  1 
ATOM   3523 C  CD1 . LEU   B 1 141 ? -9.632  -14.846 -13.961 1.00 44.19  ? 141 LEU   B CD1 1 
ATOM   3524 C  CD2 . LEU   B 1 141 ? -11.540 -13.228 -13.765 1.00 37.47  ? 141 LEU   B CD2 1 
ATOM   3525 N  N   . ASN   B 1 142 ? -12.018 -15.036 -9.136  1.00 43.04  ? 142 ASN   B N   1 
ATOM   3526 C  CA  . ASN   B 1 142 ? -12.169 -15.773 -7.888  1.00 46.55  ? 142 ASN   B CA  1 
ATOM   3527 C  C   . ASN   B 1 142 ? -10.838 -16.432 -7.537  1.00 36.55  ? 142 ASN   B C   1 
ATOM   3528 O  O   . ASN   B 1 142 ? -10.149 -16.937 -8.423  1.00 35.35  ? 142 ASN   B O   1 
ATOM   3529 C  CB  . ASN   B 1 142 ? -13.348 -16.744 -7.921  1.00 55.22  ? 142 ASN   B CB  1 
ATOM   3530 C  CG  . ASN   B 1 142 ? -14.649 -16.031 -8.229  1.00 68.45  ? 142 ASN   B CG  1 
ATOM   3531 O  OD1 . ASN   B 1 142 ? -14.911 -14.938 -7.705  1.00 72.54  ? 142 ASN   B OD1 1 
ATOM   3532 N  ND2 . ASN   B 1 142 ? -15.463 -16.606 -9.105  1.00 72.30  ? 142 ASN   B ND2 1 
ATOM   3533 N  N   . GLY   B 1 143 ? -10.480 -16.363 -6.245  1.00 33.69  ? 143 GLY   B N   1 
ATOM   3534 C  CA  . GLY   B 1 143 ? -9.189  -16.824 -5.745  1.00 33.65  ? 143 GLY   B CA  1 
ATOM   3535 C  C   . GLY   B 1 143 ? -8.173  -15.694 -5.544  1.00 32.36  ? 143 GLY   B C   1 
ATOM   3536 O  O   . GLY   B 1 143 ? -7.086  -15.950 -5.023  1.00 31.16  ? 143 GLY   B O   1 
ATOM   3537 N  N   . SER   B 1 144 ? -8.523  -14.468 -5.970  1.00 28.80  ? 144 SER   B N   1 
ATOM   3538 C  CA  . SER   B 1 144 ? -7.621  -13.318 -5.943  1.00 31.09  ? 144 SER   B CA  1 
ATOM   3539 C  C   . SER   B 1 144 ? -7.639  -12.584 -4.600  1.00 30.94  ? 144 SER   B C   1 
ATOM   3540 O  O   . SER   B 1 144 ? -6.772  -11.735 -4.381  1.00 27.58  ? 144 SER   B O   1 
ATOM   3541 C  CB  . SER   B 1 144 ? -7.929  -12.322 -7.056  1.00 28.86  ? 144 SER   B CB  1 
ATOM   3542 O  OG  . SER   B 1 144 ? -9.234  -11.783 -6.891  1.00 28.44  ? 144 SER   B OG  1 
ATOM   3543 N  N   . CYS   B 1 145 ? -8.592  -12.907 -3.705  1.00 28.59  ? 145 CYS   B N   1 
ATOM   3544 C  CA  . CYS   B 1 145 ? -8.656  -12.245 -2.409  1.00 26.38  ? 145 CYS   B CA  1 
ATOM   3545 C  C   . CYS   B 1 145 ? -7.326  -12.432 -1.684  1.00 23.69  ? 145 CYS   B C   1 
ATOM   3546 O  O   . CYS   B 1 145 ? -6.693  -13.491 -1.769  1.00 26.58  ? 145 CYS   B O   1 
ATOM   3547 C  CB  . CYS   B 1 145 ? -9.827  -12.722 -1.546  1.00 29.41  ? 145 CYS   B CB  1 
ATOM   3548 S  SG  . CYS   B 1 145 ? -11.468 -12.368 -2.228  1.00 33.63  ? 145 CYS   B SG  1 
ATOM   3549 N  N   . GLY   B 1 146 ? -6.904  -11.380 -0.972  1.00 21.43  ? 146 GLY   B N   1 
ATOM   3550 C  CA  . GLY   B 1 146 ? -5.629  -11.380 -0.269  1.00 20.58  ? 146 GLY   B CA  1 
ATOM   3551 C  C   . GLY   B 1 146 ? -4.434  -10.913 -1.105  1.00 20.40  ? 146 GLY   B C   1 
ATOM   3552 O  O   . GLY   B 1 146 ? -3.325  -10.777 -0.556  1.00 20.91  ? 146 GLY   B O   1 
ATOM   3553 N  N   . SER   B 1 147 ? -4.622  -10.713 -2.424  1.00 22.27  ? 147 SER   B N   1 
ATOM   3554 C  CA  . SER   B 1 147 ? -3.636  -10.031 -3.269  1.00 22.01  ? 147 SER   B CA  1 
ATOM   3555 C  C   . SER   B 1 147 ? -3.380  -8.640  -2.672  1.00 23.96  ? 147 SER   B C   1 
ATOM   3556 O  O   . SER   B 1 147 ? -4.313  -8.055  -2.127  1.00 25.61  ? 147 SER   B O   1 
ATOM   3557 C  CB  . SER   B 1 147 ? -4.137  -9.929  -4.712  1.00 21.89  ? 147 SER   B CB  1 
ATOM   3558 O  OG  . SER   B 1 147 ? -4.185  -11.174 -5.418  1.00 22.69  ? 147 SER   B OG  1 
ATOM   3559 N  N   . VAL   B 1 148 ? -2.167  -8.078  -2.800  1.00 24.36  ? 148 VAL   B N   1 
ATOM   3560 C  CA  . VAL   B 1 148 ? -1.828  -6.807  -2.150  1.00 24.52  ? 148 VAL   B CA  1 
ATOM   3561 C  C   . VAL   B 1 148 ? -1.379  -5.712  -3.133  1.00 24.71  ? 148 VAL   B C   1 
ATOM   3562 O  O   . VAL   B 1 148 ? -0.947  -5.979  -4.263  1.00 24.54  ? 148 VAL   B O   1 
ATOM   3563 C  CB  . VAL   B 1 148 ? -0.764  -6.959  -1.046  1.00 27.45  ? 148 VAL   B CB  1 
ATOM   3564 C  CG1 . VAL   B 1 148 ? -1.249  -7.835  0.110   1.00 28.94  ? 148 VAL   B CG1 1 
ATOM   3565 C  CG2 . VAL   B 1 148 ? 0.574   -7.460  -1.577  1.00 27.76  ? 148 VAL   B CG2 1 
ATOM   3566 N  N   . GLY   B 1 149 ? -1.494  -4.458  -2.656  1.00 24.37  ? 149 GLY   B N   1 
ATOM   3567 C  CA  . GLY   B 1 149 ? -1.000  -3.261  -3.332  1.00 22.32  ? 149 GLY   B CA  1 
ATOM   3568 C  C   . GLY   B 1 149 ? 0.106   -2.578  -2.519  1.00 23.42  ? 149 GLY   B C   1 
ATOM   3569 O  O   . GLY   B 1 149 ? 0.104   -2.671  -1.280  1.00 24.29  ? 149 GLY   B O   1 
ATOM   3570 N  N   . PHE   B 1 150 ? 1.028   -1.880  -3.206  1.00 19.46  ? 150 PHE   B N   1 
ATOM   3571 C  CA  . PHE   B 1 150 ? 2.253   -1.398  -2.579  1.00 21.66  ? 150 PHE   B CA  1 
ATOM   3572 C  C   . PHE   B 1 150 ? 2.967   -0.328  -3.422  1.00 24.31  ? 150 PHE   B C   1 
ATOM   3573 O  O   . PHE   B 1 150 ? 2.757   -0.212  -4.634  1.00 21.34  ? 150 PHE   B O   1 
ATOM   3574 C  CB  . PHE   B 1 150 ? 3.221   -2.558  -2.316  1.00 21.90  ? 150 PHE   B CB  1 
ATOM   3575 C  CG  . PHE   B 1 150 ? 3.809   -3.179  -3.577  1.00 22.73  ? 150 PHE   B CG  1 
ATOM   3576 C  CD1 . PHE   B 1 150 ? 3.132   -4.182  -4.254  1.00 27.34  ? 150 PHE   B CD1 1 
ATOM   3577 C  CD2 . PHE   B 1 150 ? 5.042   -2.774  -4.070  1.00 25.25  ? 150 PHE   B CD2 1 
ATOM   3578 C  CE1 . PHE   B 1 150 ? 3.643   -4.743  -5.416  1.00 26.12  ? 150 PHE   B CE1 1 
ATOM   3579 C  CE2 . PHE   B 1 150 ? 5.546   -3.325  -5.239  1.00 25.71  ? 150 PHE   B CE2 1 
ATOM   3580 C  CZ  . PHE   B 1 150 ? 4.849   -4.315  -5.904  1.00 25.80  ? 150 PHE   B CZ  1 
ATOM   3581 N  N   . ASN   B 1 151 ? 3.836   0.441   -2.742  1.00 23.67  ? 151 ASN   B N   1 
ATOM   3582 C  CA  . ASN   B 1 151 ? 4.794   1.332   -3.377  1.00 25.95  ? 151 ASN   B CA  1 
ATOM   3583 C  C   . ASN   B 1 151 ? 6.194   0.950   -2.889  1.00 27.55  ? 151 ASN   B C   1 
ATOM   3584 O  O   . ASN   B 1 151 ? 6.338   0.306   -1.848  1.00 24.86  ? 151 ASN   B O   1 
ATOM   3585 C  CB  . ASN   B 1 151 ? 4.460   2.802   -3.095  1.00 25.95  ? 151 ASN   B CB  1 
ATOM   3586 C  CG  . ASN   B 1 151 ? 3.275   3.273   -3.903  1.00 28.45  ? 151 ASN   B CG  1 
ATOM   3587 O  OD1 . ASN   B 1 151 ? 3.327   3.344   -5.138  1.00 31.39  ? 151 ASN   B OD1 1 
ATOM   3588 N  ND2 . ASN   B 1 151 ? 2.169   3.552   -3.240  1.00 23.44  ? 151 ASN   B ND2 1 
ATOM   3589 N  N   . ILE   B 1 152 ? 7.229   1.371   -3.620  1.00 26.89  ? 152 ILE   B N   1 
ATOM   3590 C  CA  . ILE   B 1 152 ? 8.598   1.225   -3.142  1.00 29.08  ? 152 ILE   B CA  1 
ATOM   3591 C  C   . ILE   B 1 152 ? 9.264   2.602   -3.104  1.00 36.39  ? 152 ILE   B C   1 
ATOM   3592 O  O   . ILE   B 1 152 ? 9.219   3.357   -4.082  1.00 35.95  ? 152 ILE   B O   1 
ATOM   3593 C  CB  . ILE   B 1 152 ? 9.402   0.247   -4.011  1.00 30.45  ? 152 ILE   B CB  1 
ATOM   3594 C  CG1 . ILE   B 1 152 ? 8.719   -1.100  -4.166  1.00 30.96  ? 152 ILE   B CG1 1 
ATOM   3595 C  CG2 . ILE   B 1 152 ? 10.826  0.105   -3.472  1.00 32.21  ? 152 ILE   B CG2 1 
ATOM   3596 C  CD1 . ILE   B 1 152 ? 9.558   -2.164  -4.858  1.00 34.98  ? 152 ILE   B CD1 1 
ATOM   3597 N  N   . ASP   B 1 153 ? 9.878   2.912   -1.955  1.00 41.76  ? 153 ASP   B N   1 
ATOM   3598 C  CA  . ASP   B 1 153 ? 10.681  4.115   -1.766  1.00 48.84  ? 153 ASP   B CA  1 
ATOM   3599 C  C   . ASP   B 1 153 ? 12.079  3.691   -1.317  1.00 55.39  ? 153 ASP   B C   1 
ATOM   3600 O  O   . ASP   B 1 153 ? 12.240  3.243   -0.184  1.00 60.63  ? 153 ASP   B O   1 
ATOM   3601 C  CB  . ASP   B 1 153 ? 10.035  5.060   -0.767  1.00 53.23  ? 153 ASP   B CB  1 
ATOM   3602 C  CG  . ASP   B 1 153 ? 8.591   5.439   -1.068  1.00 59.84  ? 153 ASP   B CG  1 
ATOM   3603 O  OD1 . ASP   B 1 153 ? 8.364   6.070   -2.119  1.00 71.90  ? 153 ASP   B OD1 1 
ATOM   3604 O  OD2 . ASP   B 1 153 ? 7.694   5.077   -0.268  1.00 60.09  ? 153 ASP   B OD2 1 
ATOM   3605 N  N   . TYR   B 1 154 ? 13.060  3.800   -2.230  1.00 56.11  ? 154 TYR   B N   1 
ATOM   3606 C  CA  . TYR   B 1 154 ? 14.437  3.349   -2.037  1.00 59.29  ? 154 TYR   B CA  1 
ATOM   3607 C  C   . TYR   B 1 154 ? 14.477  1.828   -1.923  1.00 60.69  ? 154 TYR   B C   1 
ATOM   3608 O  O   . TYR   B 1 154 ? 14.422  1.150   -2.943  1.00 60.80  ? 154 TYR   B O   1 
ATOM   3609 C  CB  . TYR   B 1 154 ? 15.098  4.135   -0.900  1.00 67.91  ? 154 TYR   B CB  1 
ATOM   3610 C  CG  . TYR   B 1 154 ? 15.071  5.604   -1.278  1.00 74.17  ? 154 TYR   B CG  1 
ATOM   3611 C  CD1 . TYR   B 1 154 ? 15.900  6.085   -2.289  1.00 76.43  ? 154 TYR   B CD1 1 
ATOM   3612 C  CD2 . TYR   B 1 154 ? 14.146  6.476   -0.712  1.00 76.13  ? 154 TYR   B CD2 1 
ATOM   3613 C  CE1 . TYR   B 1 154 ? 15.842  7.408   -2.695  1.00 78.48  ? 154 TYR   B CE1 1 
ATOM   3614 C  CE2 . TYR   B 1 154 ? 14.090  7.806   -1.098  1.00 80.63  ? 154 TYR   B CE2 1 
ATOM   3615 C  CZ  . TYR   B 1 154 ? 14.943  8.270   -2.089  1.00 78.74  ? 154 TYR   B CZ  1 
ATOM   3616 O  OH  . TYR   B 1 154 ? 14.896  9.575   -2.476  1.00 73.73  ? 154 TYR   B OH  1 
ATOM   3617 N  N   . ASP   B 1 155 ? 14.602  1.300   -0.700  1.00 58.57  ? 155 ASP   B N   1 
ATOM   3618 C  CA  . ASP   B 1 155 ? 14.625  -0.141  -0.483  1.00 59.45  ? 155 ASP   B CA  1 
ATOM   3619 C  C   . ASP   B 1 155 ? 13.407  -0.575  0.346   1.00 51.99  ? 155 ASP   B C   1 
ATOM   3620 O  O   . ASP   B 1 155 ? 13.219  -1.776  0.573   1.00 47.67  ? 155 ASP   B O   1 
ATOM   3621 C  CB  . ASP   B 1 155 ? 15.946  -0.539  0.159   1.00 65.35  ? 155 ASP   B CB  1 
ATOM   3622 C  CG  . ASP   B 1 155 ? 16.228  0.153   1.490   1.00 72.76  ? 155 ASP   B CG  1 
ATOM   3623 O  OD1 . ASP   B 1 155 ? 15.889  1.361   1.619   1.00 71.26  ? 155 ASP   B OD1 1 
ATOM   3624 O  OD2 . ASP   B 1 155 ? 16.794  -0.509  2.389   1.00 70.02  ? 155 ASP   B OD2 1 
ATOM   3625 N  N   . CYS   B 1 156 ? 12.583  0.402   0.778   1.00 42.78  ? 156 CYS   B N   1 
ATOM   3626 C  CA  . CYS   B 1 156 ? 11.474  0.170   1.695   1.00 34.66  ? 156 CYS   B CA  1 
ATOM   3627 C  C   . CYS   B 1 156 ? 10.165  -0.031  0.919   1.00 33.72  ? 156 CYS   B C   1 
ATOM   3628 O  O   . CYS   B 1 156 ? 9.752   0.832   0.146   1.00 30.37  ? 156 CYS   B O   1 
ATOM   3629 C  CB  . CYS   B 1 156 ? 11.318  1.311   2.696   1.00 34.14  ? 156 CYS   B CB  1 
ATOM   3630 S  SG  . CYS   B 1 156 ? 10.000  1.022   3.916   1.00 34.69  ? 156 CYS   B SG  1 
ATOM   3631 N  N   . VAL   B 1 157 ? 9.513   -1.177  1.147   1.00 29.87  ? 157 VAL   B N   1 
ATOM   3632 C  CA  . VAL   B 1 157 ? 8.186   -1.445  0.612   1.00 29.56  ? 157 VAL   B CA  1 
ATOM   3633 C  C   . VAL   B 1 157 ? 7.134   -0.896  1.583   1.00 28.49  ? 157 VAL   B C   1 
ATOM   3634 O  O   . VAL   B 1 157 ? 7.043   -1.313  2.744   1.00 27.21  ? 157 VAL   B O   1 
ATOM   3635 C  CB  . VAL   B 1 157 ? 8.009   -2.957  0.342   1.00 27.83  ? 157 VAL   B CB  1 
ATOM   3636 C  CG1 . VAL   B 1 157 ? 6.633   -3.284  -0.216  1.00 29.35  ? 157 VAL   B CG1 1 
ATOM   3637 C  CG2 . VAL   B 1 157 ? 9.078   -3.485  -0.604  1.00 28.21  ? 157 VAL   B CG2 1 
ATOM   3638 N  N   . SER   B 1 158 ? 6.309   0.024   1.085   1.00 25.53  ? 158 SER   B N   1 
ATOM   3639 C  CA  . SER   B 1 158 ? 5.145   0.501   1.805   1.00 24.91  ? 158 SER   B CA  1 
ATOM   3640 C  C   . SER   B 1 158 ? 3.909   -0.249  1.321   1.00 22.43  ? 158 SER   B C   1 
ATOM   3641 O  O   . SER   B 1 158 ? 3.491   -0.029  0.192   1.00 24.23  ? 158 SER   B O   1 
ATOM   3642 C  CB  . SER   B 1 158 ? 4.979   1.996   1.608   1.00 25.75  ? 158 SER   B CB  1 
ATOM   3643 O  OG  . SER   B 1 158 ? 6.022   2.670   2.287   1.00 28.49  ? 158 SER   B OG  1 
ATOM   3644 N  N   . PHE   B 1 159 ? 3.321   -1.115  2.164   1.00 20.91  ? 159 PHE   B N   1 
ATOM   3645 C  CA  . PHE   B 1 159 ? 2.116   -1.845  1.783   1.00 21.71  ? 159 PHE   B CA  1 
ATOM   3646 C  C   . PHE   B 1 159 ? 0.875   -1.023  2.152   1.00 21.07  ? 159 PHE   B C   1 
ATOM   3647 O  O   . PHE   B 1 159 ? 0.787   -0.537  3.281   1.00 22.53  ? 159 PHE   B O   1 
ATOM   3648 C  CB  . PHE   B 1 159 ? 1.977   -3.208  2.469   1.00 21.55  ? 159 PHE   B CB  1 
ATOM   3649 C  CG  . PHE   B 1 159 ? 3.053   -4.226  2.153   1.00 21.57  ? 159 PHE   B CG  1 
ATOM   3650 C  CD1 . PHE   B 1 159 ? 2.978   -5.009  1.007   1.00 23.81  ? 159 PHE   B CD1 1 
ATOM   3651 C  CD2 . PHE   B 1 159 ? 4.091   -4.471  3.051   1.00 24.93  ? 159 PHE   B CD2 1 
ATOM   3652 C  CE1 . PHE   B 1 159 ? 3.943   -5.977  0.732   1.00 23.96  ? 159 PHE   B CE1 1 
ATOM   3653 C  CE2 . PHE   B 1 159 ? 5.047   -5.446  2.782   1.00 23.32  ? 159 PHE   B CE2 1 
ATOM   3654 C  CZ  . PHE   B 1 159 ? 4.989   -6.172  1.613   1.00 22.94  ? 159 PHE   B CZ  1 
ATOM   3655 N  N   . CYS   B 1 160 ? -0.063  -0.877  1.190   1.00 21.98  ? 160 CYS   B N   1 
ATOM   3656 C  CA  . CYS   B 1 160 ? -1.226  -0.000  1.332   1.00 22.30  ? 160 CYS   B CA  1 
ATOM   3657 C  C   . CYS   B 1 160 ? -2.573  -0.695  1.086   1.00 21.69  ? 160 CYS   B C   1 
ATOM   3658 O  O   . CYS   B 1 160 ? -3.608  -0.105  1.409   1.00 20.68  ? 160 CYS   B O   1 
ATOM   3659 C  CB  . CYS   B 1 160 ? -1.090  1.261   0.467   1.00 20.52  ? 160 CYS   B CB  1 
ATOM   3660 S  SG  . CYS   B 1 160 ? -0.956  0.960   -1.316  1.00 23.73  ? 160 CYS   B SG  1 
ATOM   3661 N  N   . TYR   B 1 161 ? -2.619  -1.914  0.506   1.00 20.67  ? 161 TYR   B N   1 
ATOM   3662 C  CA  . TYR   B 1 161 ? -3.910  -2.441  0.050   1.00 20.84  ? 161 TYR   B CA  1 
ATOM   3663 C  C   . TYR   B 1 161 ? -3.938  -3.960  0.198   1.00 22.06  ? 161 TYR   B C   1 
ATOM   3664 O  O   . TYR   B 1 161 ? -2.924  -4.607  -0.066  1.00 21.85  ? 161 TYR   B O   1 
ATOM   3665 C  CB  . TYR   B 1 161 ? -4.257  -2.057  -1.410  1.00 20.65  ? 161 TYR   B CB  1 
ATOM   3666 C  CG  . TYR   B 1 161 ? -5.588  -2.556  -1.995  1.00 21.11  ? 161 TYR   B CG  1 
ATOM   3667 C  CD1 . TYR   B 1 161 ? -6.781  -1.911  -1.712  1.00 23.95  ? 161 TYR   B CD1 1 
ATOM   3668 C  CD2 . TYR   B 1 161 ? -5.665  -3.652  -2.869  1.00 21.52  ? 161 TYR   B CD2 1 
ATOM   3669 C  CE1 . TYR   B 1 161 ? -7.999  -2.344  -2.236  1.00 25.27  ? 161 TYR   B CE1 1 
ATOM   3670 C  CE2 . TYR   B 1 161 ? -6.869  -4.095  -3.398  1.00 21.39  ? 161 TYR   B CE2 1 
ATOM   3671 C  CZ  . TYR   B 1 161 ? -8.049  -3.455  -3.064  1.00 23.71  ? 161 TYR   B CZ  1 
ATOM   3672 O  OH  . TYR   B 1 161 ? -9.269  -3.864  -3.553  1.00 23.25  ? 161 TYR   B OH  1 
ATOM   3673 N  N   . MET   B 1 162 ? -5.114  -4.494  0.571   1.00 21.45  ? 162 MET   B N   1 
ATOM   3674 C  CA  . MET   B 1 162 ? -5.429  -5.923  0.500   1.00 21.37  ? 162 MET   B CA  1 
ATOM   3675 C  C   . MET   B 1 162 ? -6.825  -6.077  -0.106  1.00 22.46  ? 162 MET   B C   1 
ATOM   3676 O  O   . MET   B 1 162 ? -7.758  -5.400  0.326   1.00 22.88  ? 162 MET   B O   1 
ATOM   3677 C  CB  . MET   B 1 162 ? -5.389  -6.590  1.883   1.00 23.93  ? 162 MET   B CB  1 
ATOM   3678 C  CG  . MET   B 1 162 ? -5.675  -8.085  1.882   1.00 26.62  ? 162 MET   B CG  1 
ATOM   3679 S  SD  . MET   B 1 162 ? -5.392  -8.953  3.440   1.00 33.18  ? 162 MET   B SD  1 
ATOM   3680 C  CE  . MET   B 1 162 ? -3.704  -9.485  3.132   1.00 32.48  ? 162 MET   B CE  1 
ATOM   3681 N  N   . HIS   B 1 163 ? -6.942  -6.935  -1.138  1.00 21.16  ? 163 HIS   B N   1 
ATOM   3682 C  CA  . HIS   B 1 163 ? -8.169  -7.099  -1.909  1.00 22.24  ? 163 HIS   B CA  1 
ATOM   3683 C  C   . HIS   B 1 163 ? -9.172  -7.985  -1.162  1.00 27.57  ? 163 HIS   B C   1 
ATOM   3684 O  O   . HIS   B 1 163 ? -8.842  -9.107  -0.732  1.00 25.93  ? 163 HIS   B O   1 
ATOM   3685 C  CB  . HIS   B 1 163 ? -7.864  -7.680  -3.306  1.00 23.33  ? 163 HIS   B CB  1 
ATOM   3686 C  CG  . HIS   B 1 163 ? -9.088  -7.798  -4.189  1.00 24.63  ? 163 HIS   B CG  1 
ATOM   3687 N  ND1 . HIS   B 1 163 ? -9.899  -6.722  -4.498  1.00 26.37  ? 163 HIS   B ND1 1 
ATOM   3688 C  CD2 . HIS   B 1 163 ? -9.617  -8.840  -4.828  1.00 25.04  ? 163 HIS   B CD2 1 
ATOM   3689 C  CE1 . HIS   B 1 163 ? -10.916 -7.127  -5.245  1.00 24.88  ? 163 HIS   B CE1 1 
ATOM   3690 N  NE2 . HIS   B 1 163 ? -10.758 -8.407  -5.472  1.00 26.14  ? 163 HIS   B NE2 1 
ATOM   3691 N  N   . HIS   B 1 164 ? -10.428 -7.504  -1.092  1.00 26.47  ? 164 HIS   B N   1 
ATOM   3692 C  CA  . HIS   B 1 164 ? -11.489 -8.218  -0.395  1.00 28.32  ? 164 HIS   B CA  1 
ATOM   3693 C  C   . HIS   B 1 164 ? -12.692 -8.569  -1.290  1.00 29.74  ? 164 HIS   B C   1 
ATOM   3694 O  O   . HIS   B 1 164 ? -13.276 -9.609  -1.042  1.00 29.07  ? 164 HIS   B O   1 
ATOM   3695 C  CB  . HIS   B 1 164 ? -11.971 -7.441  0.838   1.00 29.20  ? 164 HIS   B CB  1 
ATOM   3696 C  CG  . HIS   B 1 164 ? -11.101 -7.470  2.067   1.00 29.16  ? 164 HIS   B CG  1 
ATOM   3697 N  ND1 . HIS   B 1 164 ? -11.557 -7.939  3.281   1.00 29.87  ? 164 HIS   B ND1 1 
ATOM   3698 C  CD2 . HIS   B 1 164 ? -9.854  -7.015  2.303   1.00 31.50  ? 164 HIS   B CD2 1 
ATOM   3699 C  CE1 . HIS   B 1 164 ? -10.607 -7.786  4.198   1.00 31.76  ? 164 HIS   B CE1 1 
ATOM   3700 N  NE2 . HIS   B 1 164 ? -9.558  -7.216  3.628   1.00 30.17  ? 164 HIS   B NE2 1 
ATOM   3701 N  N   . MET   B 1 165 ? -13.128 -7.733  -2.269  1.00 27.00  ? 165 MET   B N   1 
ATOM   3702 C  CA  . MET   B 1 165 ? -14.391 -8.019  -2.953  1.00 29.80  ? 165 MET   B CA  1 
ATOM   3703 C  C   . MET   B 1 165 ? -14.550 -7.276  -4.285  1.00 30.77  ? 165 MET   B C   1 
ATOM   3704 O  O   . MET   B 1 165 ? -13.862 -6.278  -4.553  1.00 26.10  ? 165 MET   B O   1 
ATOM   3705 C  CB  . MET   B 1 165 ? -15.584 -7.661  -2.048  1.00 31.93  ? 165 MET   B CB  1 
ATOM   3706 C  CG  . MET   B 1 165 ? -15.607 -6.211  -1.582  1.00 38.52  ? 165 MET   B CG  1 
ATOM   3707 S  SD  . MET   B 1 165 ? -16.927 -5.672  -0.464  1.00 48.24  ? 165 MET   B SD  1 
ATOM   3708 C  CE  . MET   B 1 165 ? -16.853 -7.153  0.552   1.00 52.49  ? 165 MET   B CE  1 
ATOM   3709 N  N   . GLU   B 1 166 ? -15.534 -7.732  -5.088  1.00 30.23  ? 166 GLU   B N   1 
ATOM   3710 C  CA  . GLU   B 1 166 ? -15.945 -7.039  -6.310  1.00 32.51  ? 166 GLU   B CA  1 
ATOM   3711 C  C   . GLU   B 1 166 ? -17.362 -6.480  -6.141  1.00 33.09  ? 166 GLU   B C   1 
ATOM   3712 O  O   . GLU   B 1 166 ? -18.246 -7.190  -5.684  1.00 37.22  ? 166 GLU   B O   1 
ATOM   3713 C  CB  . GLU   B 1 166 ? -15.864 -7.994  -7.507  1.00 34.17  ? 166 GLU   B CB  1 
ATOM   3714 C  CG  . GLU   B 1 166 ? -16.041 -7.314  -8.862  1.00 34.41  ? 166 GLU   B CG  1 
ATOM   3715 C  CD  . GLU   B 1 166 ? -15.715 -8.187  -10.076 1.00 39.29  ? 166 GLU   B CD  1 
ATOM   3716 O  OE1 . GLU   B 1 166 ? -14.549 -8.565  -10.369 1.00 40.55  ? 166 GLU   B OE1 1 
ATOM   3717 O  OE2 . GLU   B 1 166 ? -16.697 -8.524  -10.754 1.00 40.07  ? 166 GLU   B OE2 1 
ATOM   3718 N  N   . LEU   B 1 167 ? -17.600 -5.238  -6.564  1.00 31.03  ? 167 LEU   B N   1 
ATOM   3719 C  CA  . LEU   B 1 167 ? -18.920 -4.609  -6.490  1.00 31.90  ? 167 LEU   B CA  1 
ATOM   3720 C  C   . LEU   B 1 167 ? -19.713 -4.841  -7.786  1.00 38.08  ? 167 LEU   B C   1 
ATOM   3721 O  O   . LEU   B 1 167 ? -19.151 -5.224  -8.815  1.00 35.07  ? 167 LEU   B O   1 
ATOM   3722 C  CB  . LEU   B 1 167 ? -18.750 -3.111  -6.222  1.00 31.69  ? 167 LEU   B CB  1 
ATOM   3723 C  CG  . LEU   B 1 167 ? -18.091 -2.723  -4.894  1.00 32.81  ? 167 LEU   B CG  1 
ATOM   3724 C  CD1 . LEU   B 1 167 ? -17.761 -1.231  -4.832  1.00 34.13  ? 167 LEU   B CD1 1 
ATOM   3725 C  CD2 . LEU   B 1 167 ? -18.990 -3.108  -3.739  1.00 32.14  ? 167 LEU   B CD2 1 
ATOM   3726 N  N   . PRO   B 1 168 ? -21.053 -4.606  -7.798  1.00 42.68  ? 168 PRO   B N   1 
ATOM   3727 C  CA  . PRO   B 1 168 ? -21.888 -4.944  -8.954  1.00 40.58  ? 168 PRO   B CA  1 
ATOM   3728 C  C   . PRO   B 1 168 ? -21.481 -4.298  -10.276 1.00 43.02  ? 168 PRO   B C   1 
ATOM   3729 O  O   . PRO   B 1 168 ? -21.746 -4.876  -11.329 1.00 42.11  ? 168 PRO   B O   1 
ATOM   3730 C  CB  . PRO   B 1 168 ? -23.306 -4.496  -8.535  1.00 40.64  ? 168 PRO   B CB  1 
ATOM   3731 C  CG  . PRO   B 1 168 ? -23.261 -4.525  -7.032  1.00 45.58  ? 168 PRO   B CG  1 
ATOM   3732 C  CD  . PRO   B 1 168 ? -21.850 -4.053  -6.689  1.00 45.15  ? 168 PRO   B CD  1 
ATOM   3733 N  N   . THR   B 1 169 ? -20.860 -3.109  -10.228 1.00 40.10  ? 169 THR   B N   1 
ATOM   3734 C  CA  . THR   B 1 169 ? -20.441 -2.439  -11.451 1.00 41.53  ? 169 THR   B CA  1 
ATOM   3735 C  C   . THR   B 1 169 ? -19.106 -2.965  -11.990 1.00 40.92  ? 169 THR   B C   1 
ATOM   3736 O  O   . THR   B 1 169 ? -18.638 -2.423  -12.979 1.00 41.53  ? 169 THR   B O   1 
ATOM   3737 C  CB  . THR   B 1 169 ? -20.351 -0.939  -11.200 1.00 43.79  ? 169 THR   B CB  1 
ATOM   3738 O  OG1 . THR   B 1 169 ? -19.623 -0.887  -9.976  1.00 46.53  ? 169 THR   B OG1 1 
ATOM   3739 C  CG2 . THR   B 1 169 ? -21.716 -0.289  -11.090 1.00 44.16  ? 169 THR   B CG2 1 
ATOM   3740 N  N   . GLY   B 1 170 ? -18.462 -3.961  -11.352 1.00 42.76  ? 170 GLY   B N   1 
ATOM   3741 C  CA  . GLY   B 1 170 ? -17.186 -4.497  -11.834 1.00 37.69  ? 170 GLY   B CA  1 
ATOM   3742 C  C   . GLY   B 1 170 ? -15.934 -3.859  -11.207 1.00 37.83  ? 170 GLY   B C   1 
ATOM   3743 O  O   . GLY   B 1 170 ? -14.828 -4.284  -11.515 1.00 43.52  ? 170 GLY   B O   1 
ATOM   3744 N  N   . VAL   B 1 171 ? -16.084 -2.862  -10.319 1.00 35.42  ? 171 VAL   B N   1 
ATOM   3745 C  CA  . VAL   B 1 171 ? -14.957 -2.255  -9.608  1.00 31.60  ? 171 VAL   B CA  1 
ATOM   3746 C  C   . VAL   B 1 171 ? -14.664 -2.999  -8.289  1.00 29.99  ? 171 VAL   B C   1 
ATOM   3747 O  O   . VAL   B 1 171 ? -15.419 -3.889  -7.882  1.00 28.10  ? 171 VAL   B O   1 
ATOM   3748 C  CB  . VAL   B 1 171 ? -15.211 -0.740  -9.405  1.00 31.34  ? 171 VAL   B CB  1 
ATOM   3749 C  CG1 . VAL   B 1 171 ? -15.311 -0.006  -10.756 1.00 29.73  ? 171 VAL   B CG1 1 
ATOM   3750 C  CG2 . VAL   B 1 171 ? -16.421 -0.448  -8.507  1.00 29.58  ? 171 VAL   B CG2 1 
ATOM   3751 N  N   . HIS   B 1 172 ? -13.536 -2.660  -7.637  1.00 28.02  ? 172 HIS   B N   1 
ATOM   3752 C  CA  . HIS   B 1 172 ? -12.945 -3.465  -6.560  1.00 27.91  ? 172 HIS   B CA  1 
ATOM   3753 C  C   . HIS   B 1 172 ? -12.817 -2.673  -5.249  1.00 26.07  ? 172 HIS   B C   1 
ATOM   3754 O  O   . HIS   B 1 172 ? -12.652 -1.454  -5.259  1.00 24.25  ? 172 HIS   B O   1 
ATOM   3755 C  CB  . HIS   B 1 172 ? -11.624 -4.077  -7.037  1.00 27.79  ? 172 HIS   B CB  1 
ATOM   3756 C  CG  . HIS   B 1 172 ? -11.828 -4.926  -8.256  1.00 32.20  ? 172 HIS   B CG  1 
ATOM   3757 N  ND1 . HIS   B 1 172 ? -11.408 -4.574  -9.525  1.00 30.76  ? 172 HIS   B ND1 1 
ATOM   3758 C  CD2 . HIS   B 1 172 ? -12.487 -6.096  -8.396  1.00 34.38  ? 172 HIS   B CD2 1 
ATOM   3759 C  CE1 . HIS   B 1 172 ? -11.789 -5.510  -10.387 1.00 32.92  ? 172 HIS   B CE1 1 
ATOM   3760 N  NE2 . HIS   B 1 172 ? -12.452 -6.439  -9.729  1.00 34.52  ? 172 HIS   B NE2 1 
ATOM   3761 N  N   . ALA   B 1 173 ? -12.942 -3.380  -4.109  1.00 24.36  ? 173 ALA   B N   1 
ATOM   3762 C  CA  . ALA   B 1 173 ? -12.881 -2.779  -2.786  1.00 25.17  ? 173 ALA   B CA  1 
ATOM   3763 C  C   . ALA   B 1 173 ? -12.050 -3.649  -1.843  1.00 24.85  ? 173 ALA   B C   1 
ATOM   3764 O  O   . ALA   B 1 173 ? -12.066 -4.870  -1.952  1.00 24.05  ? 173 ALA   B O   1 
ATOM   3765 C  CB  . ALA   B 1 173 ? -14.288 -2.617  -2.232  1.00 27.65  ? 173 ALA   B CB  1 
ATOM   3766 N  N   . GLY   B 1 174 ? -11.345 -3.002  -0.900  1.00 24.69  ? 174 GLY   B N   1 
ATOM   3767 C  CA  . GLY   B 1 174 ? -10.412 -3.674  0.005   1.00 22.82  ? 174 GLY   B CA  1 
ATOM   3768 C  C   . GLY   B 1 174 ? -10.038 -2.783  1.193   1.00 22.36  ? 174 GLY   B C   1 
ATOM   3769 O  O   . GLY   B 1 174 ? -10.635 -1.721  1.371   1.00 21.75  ? 174 GLY   B O   1 
ATOM   3770 N  N   . THR   B 1 175 ? -9.051  -3.237  1.994   1.00 23.12  ? 175 THR   B N   1 
ATOM   3771 C  CA  . THR   B 1 175 ? -8.653  -2.610  3.246   1.00 22.18  ? 175 THR   B CA  1 
ATOM   3772 C  C   . THR   B 1 175 ? -7.201  -2.161  3.153   1.00 22.76  ? 175 THR   B C   1 
ATOM   3773 O  O   . THR   B 1 175 ? -6.486  -2.592  2.256   1.00 21.74  ? 175 THR   B O   1 
ATOM   3774 C  CB  . THR   B 1 175 ? -8.796  -3.594  4.415   1.00 22.74  ? 175 THR   B CB  1 
ATOM   3775 O  OG1 . THR   B 1 175 ? -7.833  -4.641  4.284   1.00 22.21  ? 175 THR   B OG1 1 
ATOM   3776 C  CG2 . THR   B 1 175 ? -10.200 -4.152  4.499   1.00 23.32  ? 175 THR   B CG2 1 
ATOM   3777 N  N   . ASP   B 1 176 ? -6.763  -1.358  4.132   1.00 21.98  ? 176 ASP   B N   1 
ATOM   3778 C  CA  . ASP   B 1 176 ? -5.339  -1.234  4.401   1.00 21.63  ? 176 ASP   B CA  1 
ATOM   3779 C  C   . ASP   B 1 176 ? -4.864  -2.497  5.133   1.00 21.99  ? 176 ASP   B C   1 
ATOM   3780 O  O   . ASP   B 1 176 ? -5.659  -3.405  5.416   1.00 21.18  ? 176 ASP   B O   1 
ATOM   3781 C  CB  . ASP   B 1 176 ? -5.035  0.060   5.131   1.00 20.36  ? 176 ASP   B CB  1 
ATOM   3782 C  CG  . ASP   B 1 176 ? -5.625  0.195   6.528   1.00 21.61  ? 176 ASP   B CG  1 
ATOM   3783 O  OD1 . ASP   B 1 176 ? -5.895  -0.839  7.173   1.00 23.01  ? 176 ASP   B OD1 1 
ATOM   3784 O  OD2 . ASP   B 1 176 ? -5.900  1.333   6.928   1.00 21.13  ? 176 ASP   B OD2 1 
ATOM   3785 N  N   . LEU   B 1 177 ? -3.565  -2.541  5.475   1.00 22.75  ? 177 LEU   B N   1 
ATOM   3786 C  CA  . LEU   B 1 177 ? -2.990  -3.736  6.083   1.00 22.33  ? 177 LEU   B CA  1 
ATOM   3787 C  C   . LEU   B 1 177 ? -3.278  -3.801  7.580   1.00 23.35  ? 177 LEU   B C   1 
ATOM   3788 O  O   . LEU   B 1 177 ? -2.912  -4.800  8.178   1.00 25.17  ? 177 LEU   B O   1 
ATOM   3789 C  CB  . LEU   B 1 177 ? -1.493  -3.913  5.807   1.00 23.38  ? 177 LEU   B CB  1 
ATOM   3790 C  CG  . LEU   B 1 177 ? -1.138  -4.794  4.607   1.00 24.82  ? 177 LEU   B CG  1 
ATOM   3791 C  CD1 . LEU   B 1 177 ? -1.579  -6.256  4.759   1.00 26.46  ? 177 LEU   B CD1 1 
ATOM   3792 C  CD2 . LEU   B 1 177 ? -1.775  -4.174  3.363   1.00 24.97  ? 177 LEU   B CD2 1 
ATOM   3793 N  N   . GLU   B 1 178 ? -3.937  -2.782  8.146   1.00 23.78  ? 178 GLU   B N   1 
ATOM   3794 C  CA  . GLU   B 1 178 ? -4.459  -2.795  9.502   1.00 23.83  ? 178 GLU   B CA  1 
ATOM   3795 C  C   . GLU   B 1 178 ? -5.948  -3.164  9.500   1.00 24.64  ? 178 GLU   B C   1 
ATOM   3796 O  O   . GLU   B 1 178 ? -6.589  -3.149  10.548  1.00 27.05  ? 178 GLU   B O   1 
ATOM   3797 C  CB  . GLU   B 1 178 ? -4.205  -1.428  10.145  1.00 27.32  ? 178 GLU   B CB  1 
ATOM   3798 C  CG  . GLU   B 1 178 ? -2.723  -1.086  10.332  1.00 31.01  ? 178 GLU   B CG  1 
ATOM   3799 C  CD  . GLU   B 1 178 ? -2.418  0.231   11.055  1.00 35.07  ? 178 GLU   B CD  1 
ATOM   3800 O  OE1 . GLU   B 1 178 ? -3.330  0.849   11.615  1.00 39.44  ? 178 GLU   B OE1 1 
ATOM   3801 O  OE2 . GLU   B 1 178 ? -1.253  0.688   11.038  1.00 47.76  ? 178 GLU   B OE2 1 
ATOM   3802 N  N   . GLY   B 1 179 ? -6.514  -3.502  8.330   1.00 25.24  ? 179 GLY   B N   1 
ATOM   3803 C  CA  . GLY   B 1 179 ? -7.874  -4.034  8.233   1.00 23.14  ? 179 GLY   B CA  1 
ATOM   3804 C  C   . GLY   B 1 179 ? -8.983  -2.987  8.109   1.00 23.18  ? 179 GLY   B C   1 
ATOM   3805 O  O   . GLY   B 1 179 ? -10.154 -3.337  8.208   1.00 25.35  ? 179 GLY   B O   1 
ATOM   3806 N  N   . ASN   B 1 180 ? -8.659  -1.708  7.926   1.00 23.75  ? 180 ASN   B N   1 
ATOM   3807 C  CA  . ASN   B 1 180 ? -9.697  -0.701  7.741   1.00 24.39  ? 180 ASN   B CA  1 
ATOM   3808 C  C   . ASN   B 1 180 ? -10.020 -0.547  6.257   1.00 24.06  ? 180 ASN   B C   1 
ATOM   3809 O  O   . ASN   B 1 180 ? -9.121  -0.304  5.448   1.00 20.54  ? 180 ASN   B O   1 
ATOM   3810 C  CB  . ASN   B 1 180 ? -9.273  0.687   8.196   1.00 28.11  ? 180 ASN   B CB  1 
ATOM   3811 C  CG  . ASN   B 1 180 ? -8.699  0.733   9.590   1.00 33.60  ? 180 ASN   B CG  1 
ATOM   3812 O  OD1 . ASN   B 1 180 ? -9.444  0.640   10.574  1.00 33.23  ? 180 ASN   B OD1 1 
ATOM   3813 N  ND2 . ASN   B 1 180 ? -7.399  0.986   9.689   1.00 32.71  ? 180 ASN   B ND2 1 
ATOM   3814 N  N   . PHE   B 1 181 ? -11.316 -0.624  5.914   1.00 23.36  ? 181 PHE   B N   1 
ATOM   3815 C  CA  . PHE   B 1 181 ? -11.786 -0.455  4.539   1.00 22.94  ? 181 PHE   B CA  1 
ATOM   3816 C  C   . PHE   B 1 181 ? -11.432 0.938   4.021   1.00 22.92  ? 181 PHE   B C   1 
ATOM   3817 O  O   . PHE   B 1 181 ? -11.409 1.899   4.790   1.00 23.99  ? 181 PHE   B O   1 
ATOM   3818 C  CB  . PHE   B 1 181 ? -13.307 -0.656  4.352   1.00 22.27  ? 181 PHE   B CB  1 
ATOM   3819 C  CG  . PHE   B 1 181 ? -13.632 -2.087  3.936   1.00 22.68  ? 181 PHE   B CG  1 
ATOM   3820 C  CD1 . PHE   B 1 181 ? -13.623 -2.452  2.599   1.00 23.97  ? 181 PHE   B CD1 1 
ATOM   3821 C  CD2 . PHE   B 1 181 ? -13.852 -3.080  4.883   1.00 24.60  ? 181 PHE   B CD2 1 
ATOM   3822 C  CE1 . PHE   B 1 181 ? -13.840 -3.766  2.216   1.00 25.79  ? 181 PHE   B CE1 1 
ATOM   3823 C  CE2 . PHE   B 1 181 ? -14.082 -4.392  4.496   1.00 27.05  ? 181 PHE   B CE2 1 
ATOM   3824 C  CZ  . PHE   B 1 181 ? -14.076 -4.733  3.163   1.00 26.57  ? 181 PHE   B CZ  1 
ATOM   3825 N  N   . TYR   B 1 182 ? -11.122 1.007   2.710   1.00 21.90  ? 182 TYR   B N   1 
ATOM   3826 C  CA  . TYR   B 1 182 ? -11.245 2.222   1.928   1.00 20.74  ? 182 TYR   B CA  1 
ATOM   3827 C  C   . TYR   B 1 182 ? -12.702 2.292   1.471   1.00 21.08  ? 182 TYR   B C   1 
ATOM   3828 O  O   . TYR   B 1 182 ? -13.178 1.355   0.833   1.00 23.92  ? 182 TYR   B O   1 
ATOM   3829 C  CB  . TYR   B 1 182 ? -10.285 2.239   0.734   1.00 20.55  ? 182 TYR   B CB  1 
ATOM   3830 C  CG  . TYR   B 1 182 ? -8.798  2.272   1.099   1.00 21.98  ? 182 TYR   B CG  1 
ATOM   3831 C  CD1 . TYR   B 1 182 ? -8.151  3.458   1.426   1.00 23.52  ? 182 TYR   B CD1 1 
ATOM   3832 C  CD2 . TYR   B 1 182 ? -8.029  1.106   1.111   1.00 23.51  ? 182 TYR   B CD2 1 
ATOM   3833 C  CE1 . TYR   B 1 182 ? -6.792  3.485   1.741   1.00 23.45  ? 182 TYR   B CE1 1 
ATOM   3834 C  CE2 . TYR   B 1 182 ? -6.680  1.121   1.453   1.00 21.55  ? 182 TYR   B CE2 1 
ATOM   3835 C  CZ  . TYR   B 1 182 ? -6.050  2.313   1.778   1.00 23.18  ? 182 TYR   B CZ  1 
ATOM   3836 O  OH  . TYR   B 1 182 ? -4.690  2.335   2.098   1.00 21.91  ? 182 TYR   B OH  1 
ATOM   3837 N  N   . GLY   B 1 183 ? -13.398 3.370   1.849   1.00 21.84  ? 183 GLY   B N   1 
ATOM   3838 C  CA  . GLY   B 1 183 ? -14.776 3.602   1.408   1.00 23.39  ? 183 GLY   B CA  1 
ATOM   3839 C  C   . GLY   B 1 183 ? -15.827 2.972   2.320   1.00 23.44  ? 183 GLY   B C   1 
ATOM   3840 O  O   . GLY   B 1 183 ? -15.492 2.193   3.219   1.00 21.64  ? 183 GLY   B O   1 
ATOM   3841 N  N   . PRO   B 1 184 ? -17.134 3.263   2.102   1.00 25.34  ? 184 PRO   B N   1 
ATOM   3842 C  CA  . PRO   B 1 184 ? -18.190 2.877   3.047   1.00 27.26  ? 184 PRO   B CA  1 
ATOM   3843 C  C   . PRO   B 1 184 ? -18.754 1.471   2.829   1.00 30.02  ? 184 PRO   B C   1 
ATOM   3844 O  O   . PRO   B 1 184 ? -19.954 1.311   2.584   1.00 27.65  ? 184 PRO   B O   1 
ATOM   3845 C  CB  . PRO   B 1 184 ? -19.271 3.946   2.799   1.00 26.90  ? 184 PRO   B CB  1 
ATOM   3846 C  CG  . PRO   B 1 184 ? -19.150 4.247   1.314   1.00 26.83  ? 184 PRO   B CG  1 
ATOM   3847 C  CD  . PRO   B 1 184 ? -17.656 4.068   0.985   1.00 26.11  ? 184 PRO   B CD  1 
ATOM   3848 N  N   . PHE   B 1 185 ? -17.879 0.468   2.950   1.00 27.42  ? 185 PHE   B N   1 
ATOM   3849 C  CA  . PHE   B 1 185 ? -18.167 -0.895  2.521   1.00 25.64  ? 185 PHE   B CA  1 
ATOM   3850 C  C   . PHE   B 1 185 ? -18.056 -1.814  3.732   1.00 26.13  ? 185 PHE   B C   1 
ATOM   3851 O  O   . PHE   B 1 185 ? -17.418 -1.462  4.710   1.00 27.42  ? 185 PHE   B O   1 
ATOM   3852 C  CB  . PHE   B 1 185 ? -17.218 -1.282  1.370   1.00 26.38  ? 185 PHE   B CB  1 
ATOM   3853 C  CG  . PHE   B 1 185 ? -17.354 -0.396  0.133   1.00 26.94  ? 185 PHE   B CG  1 
ATOM   3854 C  CD1 . PHE   B 1 185 ? -18.595 -0.215  -0.491  1.00 26.71  ? 185 PHE   B CD1 1 
ATOM   3855 C  CD2 . PHE   B 1 185 ? -16.278 0.342   -0.327  1.00 25.45  ? 185 PHE   B CD2 1 
ATOM   3856 C  CE1 . PHE   B 1 185 ? -18.728 0.650   -1.566  1.00 30.26  ? 185 PHE   B CE1 1 
ATOM   3857 C  CE2 . PHE   B 1 185 ? -16.416 1.193   -1.417  1.00 28.43  ? 185 PHE   B CE2 1 
ATOM   3858 C  CZ  . PHE   B 1 185 ? -17.642 1.358   -2.023  1.00 28.79  ? 185 PHE   B CZ  1 
ATOM   3859 N  N   . VAL   B 1 186 ? -18.659 -3.007  3.658   1.00 26.61  ? 186 VAL   B N   1 
ATOM   3860 C  CA  . VAL   B 1 186 ? -18.566 -3.965  4.747   1.00 27.93  ? 186 VAL   B CA  1 
ATOM   3861 C  C   . VAL   B 1 186 ? -18.294 -5.351  4.159   1.00 29.54  ? 186 VAL   B C   1 
ATOM   3862 O  O   . VAL   B 1 186 ? -18.685 -5.651  3.028   1.00 28.35  ? 186 VAL   B O   1 
ATOM   3863 C  CB  . VAL   B 1 186 ? -19.846 -3.943  5.608   1.00 31.48  ? 186 VAL   B CB  1 
ATOM   3864 C  CG1 . VAL   B 1 186 ? -20.084 -2.588  6.265   1.00 31.63  ? 186 VAL   B CG1 1 
ATOM   3865 C  CG2 . VAL   B 1 186 ? -21.080 -4.377  4.830   1.00 30.29  ? 186 VAL   B CG2 1 
ATOM   3866 N  N   . ASP   B 1 187 ? -17.612 -6.199  4.932   1.00 29.06  ? 187 ASP   B N   1 
ATOM   3867 C  CA  . ASP   B 1 187 ? -17.272 -7.550  4.486   1.00 31.75  ? 187 ASP   B CA  1 
ATOM   3868 C  C   . ASP   B 1 187 ? -18.417 -8.527  4.792   1.00 33.24  ? 187 ASP   B C   1 
ATOM   3869 O  O   . ASP   B 1 187 ? -18.295 -9.417  5.645   1.00 31.25  ? 187 ASP   B O   1 
ATOM   3870 C  CB  . ASP   B 1 187 ? -15.921 -7.979  5.041   1.00 30.56  ? 187 ASP   B CB  1 
ATOM   3871 C  CG  . ASP   B 1 187 ? -15.755 -7.936  6.558   1.00 28.77  ? 187 ASP   B CG  1 
ATOM   3872 O  OD1 . ASP   B 1 187 ? -16.661 -7.424  7.255   1.00 28.77  ? 187 ASP   B OD1 1 
ATOM   3873 O  OD2 . ASP   B 1 187 ? -14.720 -8.424  7.038   1.00 28.63  ? 187 ASP   B OD2 1 
ATOM   3874 N  N   . ARG   B 1 188 ? -19.541 -8.344  4.088   1.00 36.47  ? 188 ARG   B N   1 
ATOM   3875 C  CA  . ARG   B 1 188 ? -20.628 -9.312  4.096   1.00 43.47  ? 188 ARG   B CA  1 
ATOM   3876 C  C   . ARG   B 1 188 ? -21.364 -9.313  2.752   1.00 41.88  ? 188 ARG   B C   1 
ATOM   3877 O  O   . ARG   B 1 188 ? -21.356 -8.327  2.015   1.00 36.13  ? 188 ARG   B O   1 
ATOM   3878 C  CB  . ARG   B 1 188 ? -21.594 -9.032  5.257   1.00 50.52  ? 188 ARG   B CB  1 
ATOM   3879 C  CG  . ARG   B 1 188 ? -22.942 -8.425  4.894   1.00 58.62  ? 188 ARG   B CG  1 
ATOM   3880 C  CD  . ARG   B 1 188 ? -23.796 -8.168  6.116   1.00 62.01  ? 188 ARG   B CD  1 
ATOM   3881 N  NE  . ARG   B 1 188 ? -23.240 -7.041  6.873   1.00 79.42  ? 188 ARG   B NE  1 
ATOM   3882 C  CZ  . ARG   B 1 188 ? -22.679 -7.098  8.086   1.00 84.19  ? 188 ARG   B CZ  1 
ATOM   3883 N  NH1 . ARG   B 1 188 ? -22.747 -8.197  8.818   1.00 90.76  ? 188 ARG   B NH1 1 
ATOM   3884 N  NH2 . ARG   B 1 188 ? -22.064 -6.039  8.584   1.00 79.57  ? 188 ARG   B NH2 1 
ATOM   3885 N  N   . GLN   B 1 189 ? -22.057 -10.429 2.496   1.00 48.23  ? 189 GLN   B N   1 
ATOM   3886 C  CA  . GLN   B 1 189 ? -22.884 -10.625 1.315   1.00 52.95  ? 189 GLN   B CA  1 
ATOM   3887 C  C   . GLN   B 1 189 ? -24.198 -9.870  1.493   1.00 55.19  ? 189 GLN   B C   1 
ATOM   3888 O  O   . GLN   B 1 189 ? -25.133 -10.363 2.114   1.00 53.51  ? 189 GLN   B O   1 
ATOM   3889 C  CB  . GLN   B 1 189 ? -23.092 -12.131 1.139   1.00 59.52  ? 189 GLN   B CB  1 
ATOM   3890 C  CG  . GLN   B 1 189 ? -23.822 -12.523 -0.136  1.00 65.43  ? 189 GLN   B CG  1 
ATOM   3891 C  CD  . GLN   B 1 189 ? -23.201 -11.876 -1.352  1.00 80.23  ? 189 GLN   B CD  1 
ATOM   3892 O  OE1 . GLN   B 1 189 ? -23.837 -11.074 -2.047  1.00 89.47  ? 189 GLN   B OE1 1 
ATOM   3893 N  NE2 . GLN   B 1 189 ? -21.930 -12.180 -1.581  1.00 83.82  ? 189 GLN   B NE2 1 
ATOM   3894 N  N   . THR   B 1 190 ? -24.230 -8.635  0.990   1.00 54.82  ? 190 THR   B N   1 
ATOM   3895 C  CA  . THR   B 1 190 ? -25.379 -7.761  1.122   1.00 52.93  ? 190 THR   B CA  1 
ATOM   3896 C  C   . THR   B 1 190 ? -25.282 -6.749  -0.016  1.00 51.50  ? 190 THR   B C   1 
ATOM   3897 O  O   . THR   B 1 190 ? -24.301 -6.759  -0.753  1.00 61.73  ? 190 THR   B O   1 
ATOM   3898 C  CB  . THR   B 1 190 ? -25.408 -7.120  2.512   1.00 53.97  ? 190 THR   B CB  1 
ATOM   3899 O  OG1 . THR   B 1 190 ? -26.765 -6.839  2.827   1.00 53.59  ? 190 THR   B OG1 1 
ATOM   3900 C  CG2 . THR   B 1 190 ? -24.662 -5.799  2.608   1.00 56.19  ? 190 THR   B CG2 1 
ATOM   3901 N  N   . ALA   B 1 191 ? -26.307 -5.905  -0.169  1.00 50.70  ? 191 ALA   B N   1 
ATOM   3902 C  CA  . ALA   B 1 191 ? -26.390 -4.977  -1.288  1.00 48.32  ? 191 ALA   B CA  1 
ATOM   3903 C  C   . ALA   B 1 191 ? -25.495 -3.773  -1.016  1.00 38.64  ? 191 ALA   B C   1 
ATOM   3904 O  O   . ALA   B 1 191 ? -25.686 -3.093  -0.012  1.00 36.60  ? 191 ALA   B O   1 
ATOM   3905 C  CB  . ALA   B 1 191 ? -27.823 -4.544  -1.500  1.00 49.02  ? 191 ALA   B CB  1 
ATOM   3906 N  N   . GLN   B 1 192 ? -24.519 -3.536  -1.900  1.00 35.32  ? 192 GLN   B N   1 
ATOM   3907 C  CA  . GLN   B 1 192 ? -23.593 -2.420  -1.762  1.00 35.30  ? 192 GLN   B CA  1 
ATOM   3908 C  C   . GLN   B 1 192 ? -23.252 -1.878  -3.147  1.00 36.79  ? 192 GLN   B C   1 
ATOM   3909 O  O   . GLN   B 1 192 ? -23.093 -2.657  -4.079  1.00 43.33  ? 192 GLN   B O   1 
ATOM   3910 C  CB  . GLN   B 1 192 ? -22.285 -2.826  -1.078  1.00 32.59  ? 192 GLN   B CB  1 
ATOM   3911 C  CG  . GLN   B 1 192 ? -22.447 -3.600  0.224   1.00 31.40  ? 192 GLN   B CG  1 
ATOM   3912 C  CD  . GLN   B 1 192 ? -21.132 -3.788  0.952   1.00 32.67  ? 192 GLN   B CD  1 
ATOM   3913 O  OE1 . GLN   B 1 192 ? -20.509 -2.816  1.393   1.00 31.39  ? 192 GLN   B OE1 1 
ATOM   3914 N  NE2 . GLN   B 1 192 ? -20.678 -5.033  1.067   1.00 30.25  ? 192 GLN   B NE2 1 
ATOM   3915 N  N   . ALA   B 1 193 ? -23.121 -0.551  -3.274  1.00 30.96  ? 193 ALA   B N   1 
ATOM   3916 C  CA  . ALA   B 1 193 ? -22.809 0.067   -4.556  1.00 36.24  ? 193 ALA   B CA  1 
ATOM   3917 C  C   . ALA   B 1 193 ? -21.754 1.159   -4.398  1.00 36.80  ? 193 ALA   B C   1 
ATOM   3918 O  O   . ALA   B 1 193 ? -21.636 1.793   -3.362  1.00 37.22  ? 193 ALA   B O   1 
ATOM   3919 C  CB  . ALA   B 1 193 ? -24.059 0.635   -5.190  1.00 35.13  ? 193 ALA   B CB  1 
ATOM   3920 N  N   . ALA   B 1 194 ? -21.002 1.386   -5.469  1.00 43.24  ? 194 ALA   B N   1 
ATOM   3921 C  CA  . ALA   B 1 194 ? -20.027 2.458   -5.513  1.00 46.95  ? 194 ALA   B CA  1 
ATOM   3922 C  C   . ALA   B 1 194 ? -20.749 3.793   -5.723  1.00 44.04  ? 194 ALA   B C   1 
ATOM   3923 O  O   . ALA   B 1 194 ? -21.630 3.882   -6.571  1.00 42.06  ? 194 ALA   B O   1 
ATOM   3924 C  CB  . ALA   B 1 194 ? -19.047 2.145   -6.631  1.00 48.73  ? 194 ALA   B CB  1 
ATOM   3925 N  N   . GLY   B 1 195 ? -20.388 4.814   -4.932  1.00 41.89  ? 195 GLY   B N   1 
ATOM   3926 C  CA  . GLY   B 1 195 ? -20.827 6.182   -5.164  1.00 36.68  ? 195 GLY   B CA  1 
ATOM   3927 C  C   . GLY   B 1 195 ? -20.464 6.663   -6.574  1.00 40.50  ? 195 GLY   B C   1 
ATOM   3928 O  O   . GLY   B 1 195 ? -19.574 6.117   -7.227  1.00 35.51  ? 195 GLY   B O   1 
ATOM   3929 N  N   . THR   B 1 196 ? -21.160 7.692   -7.067  1.00 39.84  ? 196 THR   B N   1 
ATOM   3930 C  CA  . THR   B 1 196 ? -20.789 8.262   -8.354  1.00 40.76  ? 196 THR   B CA  1 
ATOM   3931 C  C   . THR   B 1 196 ? -19.344 8.764   -8.219  1.00 37.45  ? 196 THR   B C   1 
ATOM   3932 O  O   . THR   B 1 196 ? -18.969 9.367   -7.219  1.00 38.88  ? 196 THR   B O   1 
ATOM   3933 C  CB  . THR   B 1 196 ? -21.786 9.328   -8.834  1.00 42.05  ? 196 THR   B CB  1 
ATOM   3934 O  OG1 . THR   B 1 196 ? -21.473 10.612  -8.307  1.00 47.10  ? 196 THR   B OG1 1 
ATOM   3935 C  CG2 . THR   B 1 196 ? -23.225 9.043   -8.436  1.00 41.99  ? 196 THR   B CG2 1 
ATOM   3936 N  N   . ASP   B 1 197 ? -18.514 8.454   -9.215  1.00 35.83  ? 197 ASP   B N   1 
ATOM   3937 C  CA  . ASP   B 1 197 ? -17.098 8.766   -9.161  1.00 37.18  ? 197 ASP   B CA  1 
ATOM   3938 C  C   . ASP   B 1 197 ? -16.850 10.139  -9.784  1.00 39.49  ? 197 ASP   B C   1 
ATOM   3939 O  O   . ASP   B 1 197 ? -17.748 10.735  -10.368 1.00 42.67  ? 197 ASP   B O   1 
ATOM   3940 C  CB  . ASP   B 1 197 ? -16.300 7.669   -9.840  1.00 34.67  ? 197 ASP   B CB  1 
ATOM   3941 C  CG  . ASP   B 1 197 ? -14.826 7.577   -9.458  1.00 35.47  ? 197 ASP   B CG  1 
ATOM   3942 O  OD1 . ASP   B 1 197 ? -14.413 8.158   -8.399  1.00 31.75  ? 197 ASP   B OD1 1 
ATOM   3943 O  OD2 . ASP   B 1 197 ? -14.107 6.925   -10.225 1.00 34.08  ? 197 ASP   B OD2 1 
ATOM   3944 N  N   . THR   B 1 198 ? -15.631 10.656  -9.603  1.00 39.80  ? 198 THR   B N   1 
ATOM   3945 C  CA  . THR   B 1 198 ? -15.238 11.956  -10.127 1.00 40.48  ? 198 THR   B CA  1 
ATOM   3946 C  C   . THR   B 1 198 ? -13.832 11.838  -10.717 1.00 38.19  ? 198 THR   B C   1 
ATOM   3947 O  O   . THR   B 1 198 ? -13.123 10.867  -10.442 1.00 36.12  ? 198 THR   B O   1 
ATOM   3948 C  CB  . THR   B 1 198 ? -15.314 13.010  -9.025  1.00 40.25  ? 198 THR   B CB  1 
ATOM   3949 O  OG1 . THR   B 1 198 ? -14.539 12.535  -7.936  1.00 42.94  ? 198 THR   B OG1 1 
ATOM   3950 C  CG2 . THR   B 1 198 ? -16.725 13.243  -8.516  1.00 44.78  ? 198 THR   B CG2 1 
ATOM   3951 N  N   . THR   B 1 199 ? -13.450 12.827  -11.530 1.00 34.09  ? 199 THR   B N   1 
ATOM   3952 C  CA  . THR   B 1 199 ? -12.170 12.809  -12.228 1.00 31.74  ? 199 THR   B CA  1 
ATOM   3953 C  C   . THR   B 1 199 ? -11.116 13.509  -11.373 1.00 30.11  ? 199 THR   B C   1 
ATOM   3954 O  O   . THR   B 1 199 ? -11.379 14.567  -10.775 1.00 30.87  ? 199 THR   B O   1 
ATOM   3955 C  CB  . THR   B 1 199 ? -12.337 13.463  -13.606 1.00 32.00  ? 199 THR   B CB  1 
ATOM   3956 O  OG1 . THR   B 1 199 ? -13.149 12.584  -14.364 1.00 32.05  ? 199 THR   B OG1 1 
ATOM   3957 C  CG2 . THR   B 1 199 ? -11.052 13.542  -14.410 1.00 33.49  ? 199 THR   B CG2 1 
ATOM   3958 N  N   . ILE   B 1 200 ? -9.900  12.948  -11.374 1.00 24.35  ? 200 ILE   B N   1 
ATOM   3959 C  CA  . ILE   B 1 200 ? -8.820  13.480  -10.565 1.00 22.93  ? 200 ILE   B CA  1 
ATOM   3960 C  C   . ILE   B 1 200 ? -8.078  14.558  -11.370 1.00 27.33  ? 200 ILE   B C   1 
ATOM   3961 O  O   . ILE   B 1 200 ? -7.178  14.247  -12.158 1.00 24.13  ? 200 ILE   B O   1 
ATOM   3962 C  CB  . ILE   B 1 200 ? -7.884  12.347  -10.085 1.00 22.05  ? 200 ILE   B CB  1 
ATOM   3963 C  CG1 . ILE   B 1 200 ? -8.639  11.113  -9.529  1.00 21.33  ? 200 ILE   B CG1 1 
ATOM   3964 C  CG2 . ILE   B 1 200 ? -6.852  12.862  -9.075  1.00 21.27  ? 200 ILE   B CG2 1 
ATOM   3965 C  CD1 . ILE   B 1 200 ? -7.790  9.845   -9.443  1.00 20.10  ? 200 ILE   B CD1 1 
ATOM   3966 N  N   . THR   B 1 201 ? -8.352  15.836  -11.043 1.00 28.54  ? 201 THR   B N   1 
ATOM   3967 C  CA  . THR   B 1 201 ? -7.957  16.987  -11.841 1.00 26.98  ? 201 THR   B CA  1 
ATOM   3968 C  C   . THR   B 1 201 ? -6.438  17.155  -11.910 1.00 27.05  ? 201 THR   B C   1 
ATOM   3969 O  O   . THR   B 1 201 ? -5.869  17.419  -12.978 1.00 28.86  ? 201 THR   B O   1 
ATOM   3970 C  CB  . THR   B 1 201 ? -8.625  18.240  -11.266 1.00 28.06  ? 201 THR   B CB  1 
ATOM   3971 O  OG1 . THR   B 1 201 ? -10.023 17.987  -11.251 1.00 24.93  ? 201 THR   B OG1 1 
ATOM   3972 C  CG2 . THR   B 1 201 ? -8.419  19.445  -12.164 1.00 32.68  ? 201 THR   B CG2 1 
ATOM   3973 N  N   . VAL   B 1 202 ? -5.775  17.049  -10.766 1.00 25.35  ? 202 VAL   B N   1 
ATOM   3974 C  CA  . VAL   B 1 202 ? -4.341  17.297  -10.689 1.00 26.41  ? 202 VAL   B CA  1 
ATOM   3975 C  C   . VAL   B 1 202 ? -3.557  16.247  -11.493 1.00 27.49  ? 202 VAL   B C   1 
ATOM   3976 O  O   . VAL   B 1 202 ? -2.461  16.525  -12.004 1.00 27.59  ? 202 VAL   B O   1 
ATOM   3977 C  CB  . VAL   B 1 202 ? -3.905  17.362  -9.210  1.00 25.15  ? 202 VAL   B CB  1 
ATOM   3978 C  CG1 . VAL   B 1 202 ? -4.123  16.040  -8.482  1.00 28.29  ? 202 VAL   B CG1 1 
ATOM   3979 C  CG2 . VAL   B 1 202 ? -2.463  17.824  -9.063  1.00 25.83  ? 202 VAL   B CG2 1 
ATOM   3980 N  N   . ASN   B 1 203 ? -4.116  15.033  -11.588 1.00 25.86  ? 203 ASN   B N   1 
ATOM   3981 C  CA  . ASN   B 1 203 ? -3.483  13.955  -12.336 1.00 25.27  ? 203 ASN   B CA  1 
ATOM   3982 C  C   . ASN   B 1 203 ? -3.666  14.180  -13.842 1.00 22.64  ? 203 ASN   B C   1 
ATOM   3983 O  O   . ASN   B 1 203 ? -2.759  13.915  -14.614 1.00 19.82  ? 203 ASN   B O   1 
ATOM   3984 C  CB  . ASN   B 1 203 ? -4.007  12.577  -11.927 1.00 23.15  ? 203 ASN   B CB  1 
ATOM   3985 C  CG  . ASN   B 1 203 ? -3.575  12.115  -10.550 1.00 24.16  ? 203 ASN   B CG  1 
ATOM   3986 O  OD1 . ASN   B 1 203 ? -2.825  12.786  -9.837  1.00 25.42  ? 203 ASN   B OD1 1 
ATOM   3987 N  ND2 . ASN   B 1 203 ? -4.026  10.937  -10.155 1.00 24.48  ? 203 ASN   B ND2 1 
ATOM   3988 N  N   . VAL   B 1 204 ? -4.851  14.618  -14.272 1.00 25.68  ? 204 VAL   B N   1 
ATOM   3989 C  CA  . VAL   B 1 204 ? -5.071  14.921  -15.683 1.00 28.67  ? 204 VAL   B CA  1 
ATOM   3990 C  C   . VAL   B 1 204 ? -4.023  15.948  -16.141 1.00 32.88  ? 204 VAL   B C   1 
ATOM   3991 O  O   . VAL   B 1 204 ? -3.412  15.809  -17.210 1.00 30.31  ? 204 VAL   B O   1 
ATOM   3992 C  CB  . VAL   B 1 204 ? -6.498  15.407  -16.005 1.00 29.79  ? 204 VAL   B CB  1 
ATOM   3993 C  CG1 . VAL   B 1 204 ? -6.616  15.876  -17.457 1.00 31.69  ? 204 VAL   B CG1 1 
ATOM   3994 C  CG2 . VAL   B 1 204 ? -7.558  14.347  -15.733 1.00 30.44  ? 204 VAL   B CG2 1 
ATOM   3995 N  N   . LEU   B 1 205 ? -3.802  16.980  -15.314 1.00 31.38  ? 205 LEU   B N   1 
ATOM   3996 C  CA  . LEU   B 1 205 ? -2.864  18.035  -15.653 1.00 31.17  ? 205 LEU   B CA  1 
ATOM   3997 C  C   . LEU   B 1 205 ? -1.440  17.479  -15.723 1.00 32.12  ? 205 LEU   B C   1 
ATOM   3998 O  O   . LEU   B 1 205 ? -0.686  17.880  -16.608 1.00 32.33  ? 205 LEU   B O   1 
ATOM   3999 C  CB  . LEU   B 1 205 ? -3.011  19.187  -14.654 1.00 31.64  ? 205 LEU   B CB  1 
ATOM   4000 C  CG  . LEU   B 1 205 ? -4.316  19.990  -14.792 1.00 34.40  ? 205 LEU   B CG  1 
ATOM   4001 C  CD1 . LEU   B 1 205 ? -4.675  20.798  -13.549 1.00 35.95  ? 205 LEU   B CD1 1 
ATOM   4002 C  CD2 . LEU   B 1 205 ? -4.208  20.919  -15.981 1.00 35.42  ? 205 LEU   B CD2 1 
ATOM   4003 N  N   . ALA   B 1 206 ? -1.086  16.547  -14.814 1.00 28.23  ? 206 ALA   B N   1 
ATOM   4004 C  CA  . ALA   B 1 206 ? 0.226   15.911  -14.830 1.00 28.71  ? 206 ALA   B CA  1 
ATOM   4005 C  C   . ALA   B 1 206 ? 0.487   15.223  -16.171 1.00 27.08  ? 206 ALA   B C   1 
ATOM   4006 O  O   . ALA   B 1 206 ? 1.600   15.293  -16.706 1.00 27.39  ? 206 ALA   B O   1 
ATOM   4007 C  CB  . ALA   B 1 206 ? 0.351   14.914  -13.694 1.00 30.02  ? 206 ALA   B CB  1 
ATOM   4008 N  N   . TRP   B 1 207 ? -0.557  14.593  -16.707 1.00 24.49  ? 207 TRP   B N   1 
ATOM   4009 C  CA  . TRP   B 1 207 ? -0.477  13.783  -17.910 1.00 28.25  ? 207 TRP   B CA  1 
ATOM   4010 C  C   . TRP   B 1 207 ? -0.377  14.675  -19.145 1.00 29.84  ? 207 TRP   B C   1 
ATOM   4011 O  O   . TRP   B 1 207 ? 0.305   14.306  -20.103 1.00 28.03  ? 207 TRP   B O   1 
ATOM   4012 C  CB  . TRP   B 1 207 ? -1.686  12.841  -17.963 1.00 28.12  ? 207 TRP   B CB  1 
ATOM   4013 C  CG  . TRP   B 1 207 ? -1.911  12.047  -19.221 1.00 26.31  ? 207 TRP   B CG  1 
ATOM   4014 C  CD1 . TRP   B 1 207 ? -1.325  10.875  -19.599 1.00 28.74  ? 207 TRP   B CD1 1 
ATOM   4015 C  CD2 . TRP   B 1 207 ? -2.913  12.331  -20.217 1.00 28.02  ? 207 TRP   B CD2 1 
ATOM   4016 N  NE1 . TRP   B 1 207 ? -1.855  10.442  -20.788 1.00 28.52  ? 207 TRP   B NE1 1 
ATOM   4017 C  CE2 . TRP   B 1 207 ? -2.833  11.307  -21.187 1.00 27.68  ? 207 TRP   B CE2 1 
ATOM   4018 C  CE3 . TRP   B 1 207 ? -3.851  13.359  -20.386 1.00 28.83  ? 207 TRP   B CE3 1 
ATOM   4019 C  CZ2 . TRP   B 1 207 ? -3.657  11.279  -22.311 1.00 29.06  ? 207 TRP   B CZ2 1 
ATOM   4020 C  CZ3 . TRP   B 1 207 ? -4.688  13.313  -21.481 1.00 32.06  ? 207 TRP   B CZ3 1 
ATOM   4021 C  CH2 . TRP   B 1 207 ? -4.592  12.284  -22.428 1.00 29.70  ? 207 TRP   B CH2 1 
ATOM   4022 N  N   . LEU   B 1 208 ? -1.009  15.855  -19.090 1.00 28.35  ? 208 LEU   B N   1 
ATOM   4023 C  CA  . LEU   B 1 208 ? -0.824  16.862  -20.127 1.00 31.06  ? 208 LEU   B CA  1 
ATOM   4024 C  C   . LEU   B 1 208 ? 0.627   17.361  -20.120 1.00 28.91  ? 208 LEU   B C   1 
ATOM   4025 O  O   . LEU   B 1 208 ? 1.199   17.581  -21.179 1.00 35.66  ? 208 LEU   B O   1 
ATOM   4026 C  CB  . LEU   B 1 208 ? -1.851  17.997  -20.019 1.00 30.40  ? 208 LEU   B CB  1 
ATOM   4027 C  CG  . LEU   B 1 208 ? -3.311  17.587  -20.230 1.00 33.44  ? 208 LEU   B CG  1 
ATOM   4028 C  CD1 . LEU   B 1 208 ? -4.310  18.692  -19.897 1.00 35.98  ? 208 LEU   B CD1 1 
ATOM   4029 C  CD2 . LEU   B 1 208 ? -3.594  17.110  -21.657 1.00 34.70  ? 208 LEU   B CD2 1 
ATOM   4030 N  N   . TYR   B 1 209 ? 1.277   17.482  -18.962 1.00 31.95  ? 209 TYR   B N   1 
ATOM   4031 C  CA  . TYR   B 1 209 ? 2.690   17.841  -18.948 1.00 33.27  ? 209 TYR   B CA  1 
ATOM   4032 C  C   . TYR   B 1 209 ? 3.539   16.754  -19.628 1.00 38.89  ? 209 TYR   B C   1 
ATOM   4033 O  O   . TYR   B 1 209 ? 4.436   17.068  -20.423 1.00 34.93  ? 209 TYR   B O   1 
ATOM   4034 C  CB  . TYR   B 1 209 ? 3.164   18.169  -17.531 1.00 35.45  ? 209 TYR   B CB  1 
ATOM   4035 C  CG  . TYR   B 1 209 ? 2.737   19.574  -17.100 1.00 42.81  ? 209 TYR   B CG  1 
ATOM   4036 C  CD1 . TYR   B 1 209 ? 3.240   20.714  -17.726 1.00 47.10  ? 209 TYR   B CD1 1 
ATOM   4037 C  CD2 . TYR   B 1 209 ? 1.833   19.765  -16.066 1.00 40.22  ? 209 TYR   B CD2 1 
ATOM   4038 C  CE1 . TYR   B 1 209 ? 2.835   21.990  -17.351 1.00 48.82  ? 209 TYR   B CE1 1 
ATOM   4039 C  CE2 . TYR   B 1 209 ? 1.421   21.030  -15.683 1.00 42.60  ? 209 TYR   B CE2 1 
ATOM   4040 C  CZ  . TYR   B 1 209 ? 1.914   22.153  -16.326 1.00 47.08  ? 209 TYR   B CZ  1 
ATOM   4041 O  OH  . TYR   B 1 209 ? 1.465   23.388  -15.923 1.00 37.13  ? 209 TYR   B OH  1 
ATOM   4042 N  N   . ALA   B 1 210 ? 3.269   15.477  -19.307 1.00 36.11  ? 210 ALA   B N   1 
ATOM   4043 C  CA  . ALA   B 1 210 ? 3.985   14.358  -19.909 1.00 32.93  ? 210 ALA   B CA  1 
ATOM   4044 C  C   . ALA   B 1 210 ? 3.830   14.379  -21.428 1.00 30.83  ? 210 ALA   B C   1 
ATOM   4045 O  O   . ALA   B 1 210 ? 4.785   14.087  -22.152 1.00 29.03  ? 210 ALA   B O   1 
ATOM   4046 C  CB  . ALA   B 1 210 ? 3.497   13.045  -19.337 1.00 30.08  ? 210 ALA   B CB  1 
ATOM   4047 N  N   . ALA   B 1 211 ? 2.622   14.698  -21.900 1.00 29.88  ? 211 ALA   B N   1 
ATOM   4048 C  CA  . ALA   B 1 211 ? 2.364   14.742  -23.329 1.00 31.80  ? 211 ALA   B CA  1 
ATOM   4049 C  C   . ALA   B 1 211 ? 3.233   15.810  -23.997 1.00 37.90  ? 211 ALA   B C   1 
ATOM   4050 O  O   . ALA   B 1 211 ? 3.785   15.576  -25.076 1.00 35.81  ? 211 ALA   B O   1 
ATOM   4051 C  CB  . ALA   B 1 211 ? 0.906   14.963  -23.602 1.00 30.15  ? 211 ALA   B CB  1 
ATOM   4052 N  N   . VAL   B 1 212 ? 3.370   16.964  -23.331 1.00 37.24  ? 212 VAL   B N   1 
ATOM   4053 C  CA  . VAL   B 1 212 ? 4.089   18.103  -23.883 1.00 36.41  ? 212 VAL   B CA  1 
ATOM   4054 C  C   . VAL   B 1 212 ? 5.569   17.764  -23.972 1.00 32.66  ? 212 VAL   B C   1 
ATOM   4055 O  O   . VAL   B 1 212 ? 6.184   17.991  -24.990 1.00 36.70  ? 212 VAL   B O   1 
ATOM   4056 C  CB  . VAL   B 1 212 ? 3.845   19.405  -23.084 1.00 35.24  ? 212 VAL   B CB  1 
ATOM   4057 C  CG1 . VAL   B 1 212 ? 4.920   20.459  -23.343 1.00 36.19  ? 212 VAL   B CG1 1 
ATOM   4058 C  CG2 . VAL   B 1 212 ? 2.466   19.971  -23.393 1.00 32.25  ? 212 VAL   B CG2 1 
ATOM   4059 N  N   . ILE   B 1 213 ? 6.121   17.227  -22.894 1.00 35.70  ? 213 ILE   B N   1 
ATOM   4060 C  CA  . ILE   B 1 213 ? 7.493   16.761  -22.817 1.00 36.81  ? 213 ILE   B CA  1 
ATOM   4061 C  C   . ILE   B 1 213 ? 7.834   15.724  -23.892 1.00 38.52  ? 213 ILE   B C   1 
ATOM   4062 O  O   . ILE   B 1 213 ? 8.995   15.617  -24.273 1.00 36.00  ? 213 ILE   B O   1 
ATOM   4063 C  CB  . ILE   B 1 213 ? 7.732   16.199  -21.410 1.00 42.99  ? 213 ILE   B CB  1 
ATOM   4064 C  CG1 . ILE   B 1 213 ? 7.799   17.332  -20.392 1.00 47.75  ? 213 ILE   B CG1 1 
ATOM   4065 C  CG2 . ILE   B 1 213 ? 8.959   15.285  -21.360 1.00 43.15  ? 213 ILE   B CG2 1 
ATOM   4066 C  CD1 . ILE   B 1 213 ? 7.837   16.870  -18.950 1.00 49.41  ? 213 ILE   B CD1 1 
ATOM   4067 N  N   . ASN   B 1 214 ? 6.853   14.936  -24.341 1.00 37.19  ? 214 ASN   B N   1 
ATOM   4068 C  CA  . ASN   B 1 214 ? 7.085   13.918  -25.358 1.00 37.70  ? 214 ASN   B CA  1 
ATOM   4069 C  C   . ASN   B 1 214 ? 6.715   14.423  -26.751 1.00 38.72  ? 214 ASN   B C   1 
ATOM   4070 O  O   . ASN   B 1 214 ? 6.608   13.624  -27.678 1.00 41.00  ? 214 ASN   B O   1 
ATOM   4071 C  CB  . ASN   B 1 214 ? 6.325   12.629  -25.050 1.00 37.48  ? 214 ASN   B CB  1 
ATOM   4072 C  CG  . ASN   B 1 214 ? 7.032   11.848  -23.977 1.00 39.34  ? 214 ASN   B CG  1 
ATOM   4073 O  OD1 . ASN   B 1 214 ? 7.929   11.046  -24.275 1.00 41.14  ? 214 ASN   B OD1 1 
ATOM   4074 N  ND2 . ASN   B 1 214 ? 6.729   12.159  -22.727 1.00 41.19  ? 214 ASN   B ND2 1 
ATOM   4075 N  N   . GLY   B 1 215 ? 6.486   15.734  -26.895 1.00 38.83  ? 215 GLY   B N   1 
ATOM   4076 C  CA  . GLY   B 1 215 ? 6.356   16.357  -28.204 1.00 36.64  ? 215 GLY   B CA  1 
ATOM   4077 C  C   . GLY   B 1 215 ? 4.914   16.428  -28.700 1.00 40.03  ? 215 GLY   B C   1 
ATOM   4078 O  O   . GLY   B 1 215 ? 4.687   16.738  -29.862 1.00 39.37  ? 215 GLY   B O   1 
ATOM   4079 N  N   . ASP   B 1 216 ? 3.935   16.119  -27.839 1.00 41.42  ? 216 ASP   B N   1 
ATOM   4080 C  CA  . ASP   B 1 216 ? 2.542   16.388  -28.160 1.00 45.84  ? 216 ASP   B CA  1 
ATOM   4081 C  C   . ASP   B 1 216 ? 2.187   17.773  -27.625 1.00 46.80  ? 216 ASP   B C   1 
ATOM   4082 O  O   . ASP   B 1 216 ? 2.346   18.018  -26.434 1.00 55.21  ? 216 ASP   B O   1 
ATOM   4083 C  CB  . ASP   B 1 216 ? 1.618   15.336  -27.567 1.00 51.56  ? 216 ASP   B CB  1 
ATOM   4084 C  CG  . ASP   B 1 216 ? 1.008   14.359  -28.551 1.00 48.85  ? 216 ASP   B CG  1 
ATOM   4085 O  OD1 . ASP   B 1 216 ? 1.035   14.669  -29.753 1.00 59.03  ? 216 ASP   B OD1 1 
ATOM   4086 O  OD2 . ASP   B 1 216 ? 0.495   13.316  -28.098 1.00 45.39  ? 216 ASP   B OD2 1 
ATOM   4087 N  N   . ARG   B 1 217 ? 1.704   18.665  -28.492 1.00 43.35  ? 217 ARG   B N   1 
ATOM   4088 C  CA  . ARG   B 1 217 ? 1.609   20.072  -28.135 1.00 45.41  ? 217 ARG   B CA  1 
ATOM   4089 C  C   . ARG   B 1 217 ? 0.383   20.752  -28.714 1.00 43.50  ? 217 ARG   B C   1 
ATOM   4090 O  O   . ARG   B 1 217 ? 0.137   21.916  -28.431 1.00 52.86  ? 217 ARG   B O   1 
ATOM   4091 C  CB  . ARG   B 1 217 ? 2.813   20.840  -28.683 1.00 48.16  ? 217 ARG   B CB  1 
ATOM   4092 C  CG  . ARG   B 1 217 ? 4.116   20.413  -28.031 1.00 47.69  ? 217 ARG   B CG  1 
ATOM   4093 C  CD  . ARG   B 1 217 ? 5.218   21.347  -28.449 1.00 52.81  ? 217 ARG   B CD  1 
ATOM   4094 N  NE  . ARG   B 1 217 ? 4.985   22.703  -27.938 1.00 57.55  ? 217 ARG   B NE  1 
ATOM   4095 C  CZ  . ARG   B 1 217 ? 5.627   23.241  -26.903 1.00 58.16  ? 217 ARG   B CZ  1 
ATOM   4096 N  NH1 . ARG   B 1 217 ? 6.496   22.533  -26.206 1.00 58.14  ? 217 ARG   B NH1 1 
ATOM   4097 N  NH2 . ARG   B 1 217 ? 5.393   24.489  -26.551 1.00 64.37  ? 217 ARG   B NH2 1 
ATOM   4098 N  N   . TRP   B 1 218 ? -0.405  20.024  -29.489 1.00 45.71  ? 218 TRP   B N   1 
ATOM   4099 C  CA  . TRP   B 1 218 ? -1.441  20.632  -30.297 1.00 48.77  ? 218 TRP   B CA  1 
ATOM   4100 C  C   . TRP   B 1 218 ? -2.515  21.347  -29.469 1.00 57.16  ? 218 TRP   B C   1 
ATOM   4101 O  O   . TRP   B 1 218 ? -3.167  22.251  -29.988 1.00 54.14  ? 218 TRP   B O   1 
ATOM   4102 C  CB  . TRP   B 1 218 ? -2.052  19.560  -31.202 1.00 47.24  ? 218 TRP   B CB  1 
ATOM   4103 C  CG  . TRP   B 1 218 ? -2.802  18.440  -30.531 1.00 52.71  ? 218 TRP   B CG  1 
ATOM   4104 C  CD1 . TRP   B 1 218 ? -2.409  17.134  -30.440 1.00 51.73  ? 218 TRP   B CD1 1 
ATOM   4105 C  CD2 . TRP   B 1 218 ? -4.136  18.496  -29.973 1.00 59.67  ? 218 TRP   B CD2 1 
ATOM   4106 N  NE1 . TRP   B 1 218 ? -3.391  16.378  -29.854 1.00 52.75  ? 218 TRP   B NE1 1 
ATOM   4107 C  CE2 . TRP   B 1 218 ? -4.461  17.182  -29.560 1.00 54.20  ? 218 TRP   B CE2 1 
ATOM   4108 C  CE3 . TRP   B 1 218 ? -5.079  19.517  -29.784 1.00 62.86  ? 218 TRP   B CE3 1 
ATOM   4109 C  CZ2 . TRP   B 1 218 ? -5.680  16.876  -28.958 1.00 57.55  ? 218 TRP   B CZ2 1 
ATOM   4110 C  CZ3 . TRP   B 1 218 ? -6.283  19.211  -29.189 1.00 63.59  ? 218 TRP   B CZ3 1 
ATOM   4111 C  CH2 . TRP   B 1 218 ? -6.583  17.904  -28.795 1.00 62.39  ? 218 TRP   B CH2 1 
ATOM   4112 N  N   . PHE   B 1 219 ? -2.706  20.932  -28.204 1.00 55.25  ? 219 PHE   B N   1 
ATOM   4113 C  CA  . PHE   B 1 219 ? -3.834  21.351  -27.382 1.00 47.91  ? 219 PHE   B CA  1 
ATOM   4114 C  C   . PHE   B 1 219 ? -3.487  22.627  -26.621 1.00 43.36  ? 219 PHE   B C   1 
ATOM   4115 O  O   . PHE   B 1 219 ? -4.345  23.178  -25.943 1.00 52.25  ? 219 PHE   B O   1 
ATOM   4116 C  CB  . PHE   B 1 219 ? -4.238  20.242  -26.396 1.00 46.70  ? 219 PHE   B CB  1 
ATOM   4117 C  CG  . PHE   B 1 219 ? -3.051  19.628  -25.659 1.00 44.75  ? 219 PHE   B CG  1 
ATOM   4118 C  CD1 . PHE   B 1 219 ? -2.469  20.271  -24.573 1.00 40.95  ? 219 PHE   B CD1 1 
ATOM   4119 C  CD2 . PHE   B 1 219 ? -2.497  18.416  -26.078 1.00 44.02  ? 219 PHE   B CD2 1 
ATOM   4120 C  CE1 . PHE   B 1 219 ? -1.369  19.721  -23.927 1.00 45.96  ? 219 PHE   B CE1 1 
ATOM   4121 C  CE2 . PHE   B 1 219 ? -1.393  17.873  -25.428 1.00 37.75  ? 219 PHE   B CE2 1 
ATOM   4122 C  CZ  . PHE   B 1 219 ? -0.821  18.530  -24.369 1.00 42.28  ? 219 PHE   B CZ  1 
ATOM   4123 N  N   . LEU   B 1 220 ? -2.226  23.061  -26.671 1.00 39.88  ? 220 LEU   B N   1 
ATOM   4124 C  CA  . LEU   B 1 220 ? -1.810  24.269  -25.982 1.00 44.71  ? 220 LEU   B CA  1 
ATOM   4125 C  C   . LEU   B 1 220 ? -2.483  25.509  -26.585 1.00 46.63  ? 220 LEU   B C   1 
ATOM   4126 O  O   . LEU   B 1 220 ? -3.085  25.421  -27.659 1.00 39.19  ? 220 LEU   B O   1 
ATOM   4127 C  CB  . LEU   B 1 220 ? -0.293  24.370  -26.073 1.00 45.48  ? 220 LEU   B CB  1 
ATOM   4128 C  CG  . LEU   B 1 220 ? 0.499   23.304  -25.319 1.00 48.10  ? 220 LEU   B CG  1 
ATOM   4129 C  CD1 . LEU   B 1 220 ? 1.973   23.666  -25.341 1.00 43.97  ? 220 LEU   B CD1 1 
ATOM   4130 C  CD2 . LEU   B 1 220 ? 0.006   23.117  -23.879 1.00 52.14  ? 220 LEU   B CD2 1 
ATOM   4131 N  N   . ASN   B 1 221 ? -2.365  26.655  -25.873 1.00 50.27  ? 221 ASN   B N   1 
ATOM   4132 C  CA  . ASN   B 1 221 ? -2.964  27.924  -26.290 1.00 43.62  ? 221 ASN   B CA  1 
ATOM   4133 C  C   . ASN   B 1 221 ? -2.369  29.122  -25.549 1.00 45.60  ? 221 ASN   B C   1 
ATOM   4134 O  O   . ASN   B 1 221 ? -1.652  28.979  -24.559 1.00 47.25  ? 221 ASN   B O   1 
ATOM   4135 C  CB  . ASN   B 1 221 ? -4.477  27.926  -26.139 1.00 45.16  ? 221 ASN   B CB  1 
ATOM   4136 C  CG  . ASN   B 1 221 ? -4.942  27.846  -24.703 1.00 42.42  ? 221 ASN   B CG  1 
ATOM   4137 O  OD1 . ASN   B 1 221 ? -4.224  28.199  -23.754 1.00 41.01  ? 221 ASN   B OD1 1 
ATOM   4138 N  ND2 . ASN   B 1 221 ? -6.161  27.368  -24.551 1.00 36.56  ? 221 ASN   B ND2 1 
ATOM   4139 N  N   . ARG   B 1 222 ? -2.710  30.330  -26.034 1.00 46.60  ? 222 ARG   B N   1 
ATOM   4140 C  CA  . ARG   B 1 222 ? -2.116  31.567  -25.533 1.00 43.53  ? 222 ARG   B CA  1 
ATOM   4141 C  C   . ARG   B 1 222 ? -2.710  31.974  -24.184 1.00 38.78  ? 222 ARG   B C   1 
ATOM   4142 O  O   . ARG   B 1 222 ? -2.101  32.783  -23.499 1.00 36.75  ? 222 ARG   B O   1 
ATOM   4143 C  CB  . ARG   B 1 222 ? -2.226  32.757  -26.506 1.00 45.18  ? 222 ARG   B CB  1 
ATOM   4144 C  CG  . ARG   B 1 222 ? -3.617  33.214  -26.951 1.00 46.27  ? 222 ARG   B CG  1 
ATOM   4145 C  CD  . ARG   B 1 222 ? -3.679  34.645  -27.553 1.00 47.42  ? 222 ARG   B CD  1 
ATOM   4146 N  NE  . ARG   B 1 222 ? -2.844  34.861  -28.745 1.00 48.62  ? 222 ARG   B NE  1 
ATOM   4147 C  CZ  . ARG   B 1 222 ? -1.919  35.821  -28.906 1.00 49.07  ? 222 ARG   B CZ  1 
ATOM   4148 N  NH1 . ARG   B 1 222 ? -1.684  36.747  -27.977 1.00 49.61  ? 222 ARG   B NH1 1 
ATOM   4149 N  NH2 . ARG   B 1 222 ? -1.218  35.867  -30.022 1.00 50.74  ? 222 ARG   B NH2 1 
ATOM   4150 N  N   . PHE   B 1 223 ? -3.852  31.391  -23.790 1.00 40.55  ? 223 PHE   B N   1 
ATOM   4151 C  CA  . PHE   B 1 223 ? -4.658  31.887  -22.673 1.00 46.83  ? 223 PHE   B CA  1 
ATOM   4152 C  C   . PHE   B 1 223 ? -4.193  31.419  -21.285 1.00 55.41  ? 223 PHE   B C   1 
ATOM   4153 O  O   . PHE   B 1 223 ? -3.320  30.555  -21.154 1.00 63.79  ? 223 PHE   B O   1 
ATOM   4154 C  CB  . PHE   B 1 223 ? -6.090  31.455  -22.977 1.00 41.41  ? 223 PHE   B CB  1 
ATOM   4155 C  CG  . PHE   B 1 223 ? -6.574  32.031  -24.298 1.00 44.61  ? 223 PHE   B CG  1 
ATOM   4156 C  CD1 . PHE   B 1 223 ? -6.711  33.415  -24.460 1.00 46.28  ? 223 PHE   B CD1 1 
ATOM   4157 C  CD2 . PHE   B 1 223 ? -6.870  31.202  -25.378 1.00 41.16  ? 223 PHE   B CD2 1 
ATOM   4158 C  CE1 . PHE   B 1 223 ? -7.146  33.953  -25.669 1.00 45.50  ? 223 PHE   B CE1 1 
ATOM   4159 C  CE2 . PHE   B 1 223 ? -7.334  31.741  -26.570 1.00 43.04  ? 223 PHE   B CE2 1 
ATOM   4160 C  CZ  . PHE   B 1 223 ? -7.453  33.114  -26.723 1.00 48.43  ? 223 PHE   B CZ  1 
ATOM   4161 N  N   . THR   B 1 224 ? -4.768  32.053  -20.242 1.00 51.27  ? 224 THR   B N   1 
ATOM   4162 C  CA  . THR   B 1 224 ? -4.636  31.602  -18.858 1.00 48.84  ? 224 THR   B CA  1 
ATOM   4163 C  C   . THR   B 1 224 ? -5.978  31.778  -18.130 1.00 48.58  ? 224 THR   B C   1 
ATOM   4164 O  O   . THR   B 1 224 ? -6.994  32.100  -18.746 1.00 41.61  ? 224 THR   B O   1 
ATOM   4165 C  CB  . THR   B 1 224 ? -3.452  32.301  -18.189 1.00 49.11  ? 224 THR   B CB  1 
ATOM   4166 O  OG1 . THR   B 1 224 ? -3.373  31.688  -16.906 1.00 50.91  ? 224 THR   B OG1 1 
ATOM   4167 C  CG2 . THR   B 1 224 ? -3.615  33.804  -18.053 1.00 51.82  ? 224 THR   B CG2 1 
ATOM   4168 N  N   . THR   B 1 225 ? -6.048  31.448  -16.834 1.00 52.60  ? 225 THR   B N   1 
ATOM   4169 C  CA  . THR   B 1 225 ? -7.346  31.450  -16.169 1.00 52.46  ? 225 THR   B CA  1 
ATOM   4170 C  C   . THR   B 1 225 ? -7.152  31.608  -14.668 1.00 51.08  ? 225 THR   B C   1 
ATOM   4171 O  O   . THR   B 1 225 ? -6.045  31.920  -14.226 1.00 49.39  ? 225 THR   B O   1 
ATOM   4172 C  CB  . THR   B 1 225 ? -8.153  30.198  -16.512 1.00 56.63  ? 225 THR   B CB  1 
ATOM   4173 O  OG1 . THR   B 1 225 ? -9.500  30.434  -16.104 1.00 62.24  ? 225 THR   B OG1 1 
ATOM   4174 C  CG2 . THR   B 1 225 ? -7.629  28.956  -15.813 1.00 57.85  ? 225 THR   B CG2 1 
ATOM   4175 N  N   . THR   B 1 226 ? -8.262  31.461  -13.920 1.00 51.82  ? 226 THR   B N   1 
ATOM   4176 C  CA  . THR   B 1 226 ? -8.246  31.559  -12.463 1.00 51.99  ? 226 THR   B CA  1 
ATOM   4177 C  C   . THR   B 1 226 ? -8.780  30.255  -11.874 1.00 42.77  ? 226 THR   B C   1 
ATOM   4178 O  O   . THR   B 1 226 ? -9.646  29.583  -12.464 1.00 40.48  ? 226 THR   B O   1 
ATOM   4179 C  CB  . THR   B 1 226 ? -9.049  32.760  -11.940 1.00 48.59  ? 226 THR   B CB  1 
ATOM   4180 O  OG1 . THR   B 1 226 ? -10.439 32.532  -12.167 1.00 48.27  ? 226 THR   B OG1 1 
ATOM   4181 C  CG2 . THR   B 1 226 ? -8.656  34.066  -12.608 1.00 55.28  ? 226 THR   B CG2 1 
ATOM   4182 N  N   . LEU   B 1 227 ? -8.256  29.959  -10.679 1.00 44.13  ? 227 LEU   B N   1 
ATOM   4183 C  CA  . LEU   B 1 227 ? -8.717  28.864  -9.840  1.00 44.38  ? 227 LEU   B CA  1 
ATOM   4184 C  C   . LEU   B 1 227 ? -10.248 28.863  -9.773  1.00 44.95  ? 227 LEU   B C   1 
ATOM   4185 O  O   . LEU   B 1 227 ? -10.883 27.847  -10.064 1.00 39.94  ? 227 LEU   B O   1 
ATOM   4186 C  CB  . LEU   B 1 227 ? -8.013  29.077  -8.499  1.00 46.44  ? 227 LEU   B CB  1 
ATOM   4187 C  CG  . LEU   B 1 227 ? -7.494  27.827  -7.773  1.00 52.89  ? 227 LEU   B CG  1 
ATOM   4188 C  CD1 . LEU   B 1 227 ? -6.910  26.770  -8.704  1.00 53.11  ? 227 LEU   B CD1 1 
ATOM   4189 C  CD2 . LEU   B 1 227 ? -6.443  28.224  -6.733  1.00 49.41  ? 227 LEU   B CD2 1 
ATOM   4190 N  N   . ASN   B 1 228 ? -10.843 30.043  -9.529  1.00 45.28  ? 228 ASN   B N   1 
ATOM   4191 C  CA  . ASN   B 1 228 ? -12.282 30.176  -9.366  1.00 45.68  ? 228 ASN   B CA  1 
ATOM   4192 C  C   . ASN   B 1 228 ? -13.052 29.857  -10.638 1.00 45.81  ? 228 ASN   B C   1 
ATOM   4193 O  O   . ASN   B 1 228 ? -14.025 29.112  -10.610 1.00 50.05  ? 228 ASN   B O   1 
ATOM   4194 C  CB  . ASN   B 1 228 ? -12.674 31.593  -8.971  1.00 57.81  ? 228 ASN   B CB  1 
ATOM   4195 C  CG  . ASN   B 1 228 ? -12.211 31.921  -7.578  1.00 62.64  ? 228 ASN   B CG  1 
ATOM   4196 O  OD1 . ASN   B 1 228 ? -11.058 31.637  -7.231  1.00 73.84  ? 228 ASN   B OD1 1 
ATOM   4197 N  ND2 . ASN   B 1 228 ? -13.099 32.480  -6.772  1.00 65.93  ? 228 ASN   B ND2 1 
ATOM   4198 N  N   . ASP   B 1 229 ? -12.655 30.474  -11.750 1.00 49.06  ? 229 ASP   B N   1 
ATOM   4199 C  CA  . ASP   B 1 229 ? -13.353 30.256  -13.006 1.00 48.86  ? 229 ASP   B CA  1 
ATOM   4200 C  C   . ASP   B 1 229 ? -13.238 28.785  -13.387 1.00 44.95  ? 229 ASP   B C   1 
ATOM   4201 O  O   . ASP   B 1 229 ? -14.222 28.164  -13.809 1.00 43.73  ? 229 ASP   B O   1 
ATOM   4202 C  CB  . ASP   B 1 229 ? -12.836 31.196  -14.088 1.00 57.40  ? 229 ASP   B CB  1 
ATOM   4203 C  CG  . ASP   B 1 229 ? -13.196 32.665  -13.891 1.00 61.59  ? 229 ASP   B CG  1 
ATOM   4204 O  OD1 . ASP   B 1 229 ? -14.352 33.015  -14.205 1.00 57.04  ? 229 ASP   B OD1 1 
ATOM   4205 O  OD2 . ASP   B 1 229 ? -12.337 33.433  -13.379 1.00 59.51  ? 229 ASP   B OD2 1 
ATOM   4206 N  N   . PHE   B 1 230 ? -12.024 28.243  -13.238 1.00 47.86  ? 230 PHE   B N   1 
ATOM   4207 C  CA  . PHE   B 1 230 ? -11.762 26.872  -13.650 1.00 45.69  ? 230 PHE   B CA  1 
ATOM   4208 C  C   . PHE   B 1 230 ? -12.634 25.940  -12.811 1.00 45.28  ? 230 PHE   B C   1 
ATOM   4209 O  O   . PHE   B 1 230 ? -13.341 25.081  -13.358 1.00 41.53  ? 230 PHE   B O   1 
ATOM   4210 C  CB  . PHE   B 1 230 ? -10.269 26.527  -13.565 1.00 49.15  ? 230 PHE   B CB  1 
ATOM   4211 C  CG  . PHE   B 1 230 ? -10.001 25.072  -13.941 1.00 50.50  ? 230 PHE   B CG  1 
ATOM   4212 C  CD1 . PHE   B 1 230 ? -10.117 24.644  -15.260 1.00 46.92  ? 230 PHE   B CD1 1 
ATOM   4213 C  CD2 . PHE   B 1 230 ? -9.682  24.129  -12.970 1.00 48.78  ? 230 PHE   B CD2 1 
ATOM   4214 C  CE1 . PHE   B 1 230 ? -9.921  23.315  -15.589 1.00 49.70  ? 230 PHE   B CE1 1 
ATOM   4215 C  CE2 . PHE   B 1 230 ? -9.481  22.801  -13.306 1.00 47.29  ? 230 PHE   B CE2 1 
ATOM   4216 C  CZ  . PHE   B 1 230 ? -9.596  22.400  -14.613 1.00 50.78  ? 230 PHE   B CZ  1 
ATOM   4217 N  N   . ASN   B 1 231 ? -12.628 26.167  -11.484 1.00 46.47  ? 231 ASN   B N   1 
ATOM   4218 C  CA  . ASN   B 1 231 ? -13.287 25.256  -10.562 1.00 41.61  ? 231 ASN   B CA  1 
ATOM   4219 C  C   . ASN   B 1 231 ? -14.776 25.194  -10.871 1.00 45.70  ? 231 ASN   B C   1 
ATOM   4220 O  O   . ASN   B 1 231 ? -15.400 24.145  -10.695 1.00 52.59  ? 231 ASN   B O   1 
ATOM   4221 C  CB  . ASN   B 1 231 ? -12.891 25.521  -9.112  1.00 43.51  ? 231 ASN   B CB  1 
ATOM   4222 C  CG  . ASN   B 1 231 ? -11.615 24.790  -8.745  1.00 43.07  ? 231 ASN   B CG  1 
ATOM   4223 O  OD1 . ASN   B 1 231 ? -11.417 23.634  -9.150  1.00 43.45  ? 231 ASN   B OD1 1 
ATOM   4224 N  ND2 . ASN   B 1 231 ? -10.721 25.431  -8.012  1.00 39.03  ? 231 ASN   B ND2 1 
ATOM   4225 N  N   . LEU   B 1 232 ? -15.333 26.272  -11.433 1.00 47.45  ? 232 LEU   B N   1 
ATOM   4226 C  CA  . LEU   B 1 232 ? -16.755 26.285  -11.723 1.00 49.68  ? 232 LEU   B CA  1 
ATOM   4227 C  C   . LEU   B 1 232 ? -17.057 25.516  -13.008 1.00 50.88  ? 232 LEU   B C   1 
ATOM   4228 O  O   . LEU   B 1 232 ? -18.138 24.939  -13.146 1.00 49.23  ? 232 LEU   B O   1 
ATOM   4229 C  CB  . LEU   B 1 232 ? -17.202 27.745  -11.728 1.00 64.01  ? 232 LEU   B CB  1 
ATOM   4230 C  CG  . LEU   B 1 232 ? -17.099 28.437  -10.360 1.00 74.65  ? 232 LEU   B CG  1 
ATOM   4231 C  CD1 . LEU   B 1 232 ? -17.009 29.957  -10.440 1.00 70.67  ? 232 LEU   B CD1 1 
ATOM   4232 C  CD2 . LEU   B 1 232 ? -18.269 28.013  -9.465  1.00 77.00  ? 232 LEU   B CD2 1 
ATOM   4233 N  N   . VAL   B 1 233 ? -16.082 25.453  -13.924 1.00 55.48  ? 233 VAL   B N   1 
ATOM   4234 C  CA  . VAL   B 1 233 ? -16.185 24.588  -15.092 1.00 60.26  ? 233 VAL   B CA  1 
ATOM   4235 C  C   . VAL   B 1 233 ? -16.021 23.130  -14.653 1.00 55.39  ? 233 VAL   B C   1 
ATOM   4236 O  O   . VAL   B 1 233 ? -16.758 22.264  -15.118 1.00 54.68  ? 233 VAL   B O   1 
ATOM   4237 C  CB  . VAL   B 1 233 ? -15.161 24.936  -16.191 1.00 69.59  ? 233 VAL   B CB  1 
ATOM   4238 C  CG1 . VAL   B 1 233 ? -15.419 24.135  -17.465 1.00 69.52  ? 233 VAL   B CG1 1 
ATOM   4239 C  CG2 . VAL   B 1 233 ? -15.126 26.431  -16.491 1.00 67.11  ? 233 VAL   B CG2 1 
ATOM   4240 N  N   . ALA   B 1 234 ? -15.055 22.876  -13.755 1.00 52.88  ? 234 ALA   B N   1 
ATOM   4241 C  CA  . ALA   B 1 234 ? -14.762 21.534  -13.254 1.00 54.41  ? 234 ALA   B CA  1 
ATOM   4242 C  C   . ALA   B 1 234 ? -15.972 20.914  -12.555 1.00 54.76  ? 234 ALA   B C   1 
ATOM   4243 O  O   . ALA   B 1 234 ? -16.318 19.758  -12.809 1.00 52.31  ? 234 ALA   B O   1 
ATOM   4244 C  CB  . ALA   B 1 234 ? -13.572 21.579  -12.312 1.00 52.73  ? 234 ALA   B CB  1 
ATOM   4245 N  N   . MET   B 1 235 ? -16.612 21.693  -11.670 1.00 56.61  ? 235 MET   B N   1 
ATOM   4246 C  CA  . MET   B 1 235 ? -17.763 21.219  -10.925 1.00 54.50  ? 235 MET   B CA  1 
ATOM   4247 C  C   . MET   B 1 235 ? -18.821 20.702  -11.891 1.00 53.08  ? 235 MET   B C   1 
ATOM   4248 O  O   . MET   B 1 235 ? -19.399 19.649  -11.651 1.00 47.40  ? 235 MET   B O   1 
ATOM   4249 C  CB  . MET   B 1 235 ? -18.355 22.323  -10.047 1.00 63.65  ? 235 MET   B CB  1 
ATOM   4250 C  CG  . MET   B 1 235 ? -19.231 21.789  -8.928  1.00 69.96  ? 235 MET   B CG  1 
ATOM   4251 S  SD  . MET   B 1 235 ? -19.677 23.047  -7.714  1.00 83.57  ? 235 MET   B SD  1 
ATOM   4252 C  CE  . MET   B 1 235 ? -18.106 23.731  -7.163  1.00 81.76  ? 235 MET   B CE  1 
ATOM   4253 N  N   . LYS   B 1 236 ? -19.027 21.427  -13.003 1.00 57.78  ? 236 LYS   B N   1 
ATOM   4254 C  CA  . LYS   B 1 236 ? -20.015 21.071  -14.014 1.00 57.26  ? 236 LYS   B CA  1 
ATOM   4255 C  C   . LYS   B 1 236 ? -19.682 19.733  -14.674 1.00 52.31  ? 236 LYS   B C   1 
ATOM   4256 O  O   . LYS   B 1 236 ? -20.589 19.021  -15.101 1.00 52.57  ? 236 LYS   B O   1 
ATOM   4257 C  CB  . LYS   B 1 236 ? -20.090 22.174  -15.082 1.00 67.49  ? 236 LYS   B CB  1 
ATOM   4258 C  CG  . LYS   B 1 236 ? -21.199 22.044  -16.134 1.00 75.02  ? 236 LYS   B CG  1 
ATOM   4259 C  CD  . LYS   B 1 236 ? -21.013 22.912  -17.380 1.00 82.52  ? 236 LYS   B CD  1 
ATOM   4260 C  CE  . LYS   B 1 236 ? -20.744 24.366  -17.100 1.00 84.49  ? 236 LYS   B CE  1 
ATOM   4261 N  NZ  . LYS   B 1 236 ? -21.766 24.971  -16.240 1.00 89.77  ? 236 LYS   B NZ  1 
ATOM   4262 N  N   . TYR   B 1 237 ? -18.386 19.398  -14.777 1.00 55.52  ? 237 TYR   B N   1 
ATOM   4263 C  CA  . TYR   B 1 237 ? -17.965 18.251  -15.568 1.00 56.62  ? 237 TYR   B CA  1 
ATOM   4264 C  C   . TYR   B 1 237 ? -17.630 17.046  -14.688 1.00 54.56  ? 237 TYR   B C   1 
ATOM   4265 O  O   . TYR   B 1 237 ? -17.128 16.052  -15.213 1.00 44.12  ? 237 TYR   B O   1 
ATOM   4266 C  CB  . TYR   B 1 237 ? -16.803 18.649  -16.484 1.00 56.26  ? 237 TYR   B CB  1 
ATOM   4267 C  CG  . TYR   B 1 237 ? -17.275 19.445  -17.694 1.00 60.86  ? 237 TYR   B CG  1 
ATOM   4268 C  CD1 . TYR   B 1 237 ? -17.901 18.815  -18.764 1.00 61.99  ? 237 TYR   B CD1 1 
ATOM   4269 C  CD2 . TYR   B 1 237 ? -17.128 20.826  -17.748 1.00 63.13  ? 237 TYR   B CD2 1 
ATOM   4270 C  CE1 . TYR   B 1 237 ? -18.348 19.535  -19.858 1.00 65.09  ? 237 TYR   B CE1 1 
ATOM   4271 C  CE2 . TYR   B 1 237 ? -17.579 21.559  -18.833 1.00 63.86  ? 237 TYR   B CE2 1 
ATOM   4272 C  CZ  . TYR   B 1 237 ? -18.189 20.909  -19.889 1.00 61.45  ? 237 TYR   B CZ  1 
ATOM   4273 O  OH  . TYR   B 1 237 ? -18.630 21.631  -20.954 1.00 66.70  ? 237 TYR   B OH  1 
ATOM   4274 N  N   . ASN   B 1 238 ? -17.959 17.120  -13.385 1.00 50.06  ? 238 ASN   B N   1 
ATOM   4275 C  CA  . ASN   B 1 238 ? -17.663 16.061  -12.427 1.00 44.65  ? 238 ASN   B CA  1 
ATOM   4276 C  C   . ASN   B 1 238 ? -16.151 15.927  -12.227 1.00 39.76  ? 238 ASN   B C   1 
ATOM   4277 O  O   . ASN   B 1 238 ? -15.637 14.828  -12.012 1.00 38.74  ? 238 ASN   B O   1 
ATOM   4278 C  CB  . ASN   B 1 238 ? -18.289 14.727  -12.827 1.00 48.88  ? 238 ASN   B CB  1 
ATOM   4279 C  CG  . ASN   B 1 238 ? -19.741 14.621  -12.444 1.00 58.88  ? 238 ASN   B CG  1 
ATOM   4280 O  OD1 . ASN   B 1 238 ? -20.182 15.263  -11.486 1.00 56.66  ? 238 ASN   B OD1 1 
ATOM   4281 N  ND2 . ASN   B 1 238 ? -20.487 13.782  -13.146 1.00 63.08  ? 238 ASN   B ND2 1 
ATOM   4282 N  N   . TYR   B 1 239 ? -15.449 17.058  -12.247 1.00 36.15  ? 239 TYR   B N   1 
ATOM   4283 C  CA  . TYR   B 1 239 ? -14.044 17.107  -11.880 1.00 37.57  ? 239 TYR   B CA  1 
ATOM   4284 C  C   . TYR   B 1 239 ? -13.907 17.515  -10.413 1.00 35.95  ? 239 TYR   B C   1 
ATOM   4285 O  O   . TYR   B 1 239 ? -14.658 18.347  -9.930  1.00 41.24  ? 239 TYR   B O   1 
ATOM   4286 C  CB  . TYR   B 1 239 ? -13.255 18.062  -12.793 1.00 37.81  ? 239 TYR   B CB  1 
ATOM   4287 C  CG  . TYR   B 1 239 ? -12.718 17.407  -14.065 1.00 37.34  ? 239 TYR   B CG  1 
ATOM   4288 C  CD1 . TYR   B 1 239 ? -13.549 16.684  -14.911 1.00 37.08  ? 239 TYR   B CD1 1 
ATOM   4289 C  CD2 . TYR   B 1 239 ? -11.364 17.466  -14.388 1.00 35.63  ? 239 TYR   B CD2 1 
ATOM   4290 C  CE1 . TYR   B 1 239 ? -13.064 16.061  -16.052 1.00 34.09  ? 239 TYR   B CE1 1 
ATOM   4291 C  CE2 . TYR   B 1 239 ? -10.863 16.828  -15.512 1.00 34.76  ? 239 TYR   B CE2 1 
ATOM   4292 C  CZ  . TYR   B 1 239 ? -11.715 16.135  -16.352 1.00 36.38  ? 239 TYR   B CZ  1 
ATOM   4293 O  OH  . TYR   B 1 239 ? -11.239 15.526  -17.487 1.00 41.17  ? 239 TYR   B OH  1 
ATOM   4294 N  N   . GLU   B 1 240 ? -12.912 16.939  -9.728  1.00 35.07  ? 240 GLU   B N   1 
ATOM   4295 C  CA  . GLU   B 1 240 ? -12.486 17.376  -8.413  1.00 34.13  ? 240 GLU   B CA  1 
ATOM   4296 C  C   . GLU   B 1 240 ? -12.055 18.833  -8.464  1.00 36.40  ? 240 GLU   B C   1 
ATOM   4297 O  O   . GLU   B 1 240 ? -11.396 19.255  -9.407  1.00 33.65  ? 240 GLU   B O   1 
ATOM   4298 C  CB  . GLU   B 1 240 ? -11.253 16.648  -7.866  1.00 35.49  ? 240 GLU   B CB  1 
ATOM   4299 C  CG  . GLU   B 1 240 ? -11.477 15.173  -7.562  1.00 40.18  ? 240 GLU   B CG  1 
ATOM   4300 C  CD  . GLU   B 1 240 ? -12.156 14.915  -6.233  1.00 49.26  ? 240 GLU   B CD  1 
ATOM   4301 O  OE1 . GLU   B 1 240 ? -11.399 14.921  -5.235  1.00 54.84  ? 240 GLU   B OE1 1 
ATOM   4302 O  OE2 . GLU   B 1 240 ? -13.397 14.717  -6.186  1.00 49.28  ? 240 GLU   B OE2 1 
ATOM   4303 N  N   . PRO   B 1 241 ? -12.371 19.617  -7.407  1.00 39.22  ? 241 PRO   B N   1 
ATOM   4304 C  CA  . PRO   B 1 241 ? -11.771 20.934  -7.203  1.00 38.12  ? 241 PRO   B CA  1 
ATOM   4305 C  C   . PRO   B 1 241 ? -10.248 20.904  -7.207  1.00 39.37  ? 241 PRO   B C   1 
ATOM   4306 O  O   . PRO   B 1 241 ? -9.660  19.992  -6.641  1.00 42.23  ? 241 PRO   B O   1 
ATOM   4307 C  CB  . PRO   B 1 241 ? -12.323 21.303  -5.828  1.00 39.64  ? 241 PRO   B CB  1 
ATOM   4308 C  CG  . PRO   B 1 241 ? -13.678 20.630  -5.812  1.00 40.22  ? 241 PRO   B CG  1 
ATOM   4309 C  CD  . PRO   B 1 241 ? -13.364 19.274  -6.375  1.00 38.74  ? 241 PRO   B CD  1 
ATOM   4310 N  N   . LEU   B 1 242 ? -9.635  21.907  -7.855  1.00 38.87  ? 242 LEU   B N   1 
ATOM   4311 C  CA  . LEU   B 1 242 ? -8.193  22.099  -7.865  1.00 38.03  ? 242 LEU   B CA  1 
ATOM   4312 C  C   . LEU   B 1 242 ? -7.830  23.110  -6.788  1.00 39.92  ? 242 LEU   B C   1 
ATOM   4313 O  O   . LEU   B 1 242 ? -8.400  24.198  -6.752  1.00 42.29  ? 242 LEU   B O   1 
ATOM   4314 C  CB  . LEU   B 1 242 ? -7.784  22.618  -9.243  1.00 40.20  ? 242 LEU   B CB  1 
ATOM   4315 C  CG  . LEU   B 1 242 ? -6.283  22.792  -9.504  1.00 41.59  ? 242 LEU   B CG  1 
ATOM   4316 C  CD1 . LEU   B 1 242 ? -5.545  21.435  -9.519  1.00 43.82  ? 242 LEU   B CD1 1 
ATOM   4317 C  CD2 . LEU   B 1 242 ? -6.098  23.507  -10.831 1.00 39.73  ? 242 LEU   B CD2 1 
ATOM   4318 N  N   . THR   B 1 243 ? -6.841  22.765  -5.963  1.00 41.72  ? 243 THR   B N   1 
ATOM   4319 C  CA  . THR   B 1 243 ? -6.463  23.576  -4.819  1.00 42.16  ? 243 THR   B CA  1 
ATOM   4320 C  C   . THR   B 1 243 ? -5.089  24.167  -5.073  1.00 40.11  ? 243 THR   B C   1 
ATOM   4321 O  O   . THR   B 1 243 ? -4.416  23.781  -6.014  1.00 33.85  ? 243 THR   B O   1 
ATOM   4322 C  CB  . THR   B 1 243 ? -6.471  22.742  -3.536  1.00 39.88  ? 243 THR   B CB  1 
ATOM   4323 O  OG1 . THR   B 1 243 ? -5.366  21.846  -3.550  1.00 39.87  ? 243 THR   B OG1 1 
ATOM   4324 C  CG2 . THR   B 1 243 ? -7.737  21.922  -3.396  1.00 39.95  ? 243 THR   B CG2 1 
ATOM   4325 N  N   . GLN   B 1 244 ? -4.708  25.103  -4.204  1.00 44.23  ? 244 GLN   B N   1 
ATOM   4326 C  CA  . GLN   B 1 244 ? -3.420  25.767  -4.253  1.00 48.69  ? 244 GLN   B CA  1 
ATOM   4327 C  C   . GLN   B 1 244 ? -2.281  24.784  -3.979  1.00 52.33  ? 244 GLN   B C   1 
ATOM   4328 O  O   . GLN   B 1 244 ? -1.134  25.034  -4.358  1.00 54.50  ? 244 GLN   B O   1 
ATOM   4329 C  CB  . GLN   B 1 244 ? -3.369  26.846  -3.168  1.00 47.10  ? 244 GLN   B CB  1 
ATOM   4330 C  CG  . GLN   B 1 244 ? -2.078  27.654  -3.169  1.00 45.66  ? 244 GLN   B CG  1 
ATOM   4331 C  CD  . GLN   B 1 244 ? -1.693  28.090  -4.563  1.00 44.72  ? 244 GLN   B CD  1 
ATOM   4332 O  OE1 . GLN   B 1 244 ? -2.525  28.576  -5.334  1.00 45.33  ? 244 GLN   B OE1 1 
ATOM   4333 N  NE2 . GLN   B 1 244 ? -0.445  27.864  -4.927  1.00 48.07  ? 244 GLN   B NE2 1 
ATOM   4334 N  N   . ASP   B 1 245 ? -2.590  23.700  -3.259  1.00 45.79  ? 245 ASP   B N   1 
ATOM   4335 C  CA  . ASP   B 1 245 ? -1.600  22.677  -2.966  1.00 52.77  ? 245 ASP   B CA  1 
ATOM   4336 C  C   . ASP   B 1 245 ? -1.296  21.854  -4.231  1.00 42.47  ? 245 ASP   B C   1 
ATOM   4337 O  O   . ASP   B 1 245 ? -0.161  21.447  -4.468  1.00 39.03  ? 245 ASP   B O   1 
ATOM   4338 C  CB  . ASP   B 1 245 ? -2.046  21.872  -1.755  1.00 56.30  ? 245 ASP   B CB  1 
ATOM   4339 C  CG  . ASP   B 1 245 ? -1.098  20.756  -1.354  1.00 67.92  ? 245 ASP   B CG  1 
ATOM   4340 O  OD1 . ASP   B 1 245 ? 0.127   21.010  -1.334  1.00 71.87  ? 245 ASP   B OD1 1 
ATOM   4341 O  OD2 . ASP   B 1 245 ? -1.595  19.641  -1.080  1.00 82.85  ? 245 ASP   B OD2 1 
ATOM   4342 N  N   . HIS   B 1 246 ? -2.326  21.619  -5.040  1.00 36.14  ? 246 HIS   B N   1 
ATOM   4343 C  CA  . HIS   B 1 246 ? -2.195  20.907  -6.298  1.00 39.01  ? 246 HIS   B CA  1 
ATOM   4344 C  C   . HIS   B 1 246 ? -1.337  21.721  -7.261  1.00 42.72  ? 246 HIS   B C   1 
ATOM   4345 O  O   . HIS   B 1 246 ? -0.467  21.169  -7.944  1.00 34.33  ? 246 HIS   B O   1 
ATOM   4346 C  CB  . HIS   B 1 246 ? -3.573  20.681  -6.924  1.00 36.02  ? 246 HIS   B CB  1 
ATOM   4347 C  CG  . HIS   B 1 246 ? -4.448  19.707  -6.203  1.00 37.92  ? 246 HIS   B CG  1 
ATOM   4348 N  ND1 . HIS   B 1 246 ? -5.828  19.758  -6.274  1.00 39.73  ? 246 HIS   B ND1 1 
ATOM   4349 C  CD2 . HIS   B 1 246 ? -4.146  18.632  -5.457  1.00 37.19  ? 246 HIS   B CD2 1 
ATOM   4350 C  CE1 . HIS   B 1 246 ? -6.339  18.759  -5.572  1.00 40.46  ? 246 HIS   B CE1 1 
ATOM   4351 N  NE2 . HIS   B 1 246 ? -5.335  18.054  -5.073  1.00 38.15  ? 246 HIS   B NE2 1 
ATOM   4352 N  N   . VAL   B 1 247 ? -1.617  23.036  -7.318  1.00 39.92  ? 247 VAL   B N   1 
ATOM   4353 C  CA  . VAL   B 1 247 ? -0.877  23.927  -8.194  1.00 41.08  ? 247 VAL   B CA  1 
ATOM   4354 C  C   . VAL   B 1 247 ? 0.600   23.877  -7.820  1.00 38.10  ? 247 VAL   B C   1 
ATOM   4355 O  O   . VAL   B 1 247 ? 1.432   23.817  -8.712  1.00 39.32  ? 247 VAL   B O   1 
ATOM   4356 C  CB  . VAL   B 1 247 ? -1.393  25.379  -8.231  1.00 39.39  ? 247 VAL   B CB  1 
ATOM   4357 C  CG1 . VAL   B 1 247 ? -0.475  26.288  -9.043  1.00 37.03  ? 247 VAL   B CG1 1 
ATOM   4358 C  CG2 . VAL   B 1 247 ? -2.820  25.444  -8.758  1.00 40.58  ? 247 VAL   B CG2 1 
ATOM   4359 N  N   . ASP   B 1 248 ? 0.914   23.868  -6.521  1.00 38.38  ? 248 ASP   B N   1 
ATOM   4360 C  CA  . ASP   B 1 248 ? 2.300   23.825  -6.072  1.00 40.97  ? 248 ASP   B CA  1 
ATOM   4361 C  C   . ASP   B 1 248 ? 2.965   22.488  -6.405  1.00 41.76  ? 248 ASP   B C   1 
ATOM   4362 O  O   . ASP   B 1 248 ? 4.158   22.434  -6.699  1.00 48.88  ? 248 ASP   B O   1 
ATOM   4363 C  CB  . ASP   B 1 248 ? 2.418   24.102  -4.578  1.00 43.14  ? 248 ASP   B CB  1 
ATOM   4364 C  CG  . ASP   B 1 248 ? 1.998   25.486  -4.084  1.00 45.08  ? 248 ASP   B CG  1 
ATOM   4365 O  OD1 . ASP   B 1 248 ? 1.607   26.346  -4.899  1.00 40.61  ? 248 ASP   B OD1 1 
ATOM   4366 O  OD2 . ASP   B 1 248 ? 2.033   25.692  -2.866  1.00 46.82  ? 248 ASP   B OD2 1 
ATOM   4367 N  N   . ILE   B 1 249 ? 2.228   21.379  -6.309  1.00 43.72  ? 249 ILE   B N   1 
ATOM   4368 C  CA  . ILE   B 1 249 ? 2.838   20.073  -6.535  1.00 42.22  ? 249 ILE   B CA  1 
ATOM   4369 C  C   . ILE   B 1 249 ? 3.265   19.974  -8.002  1.00 38.75  ? 249 ILE   B C   1 
ATOM   4370 O  O   . ILE   B 1 249 ? 4.298   19.390  -8.299  1.00 41.03  ? 249 ILE   B O   1 
ATOM   4371 C  CB  . ILE   B 1 249 ? 1.883   18.946  -6.092  1.00 41.48  ? 249 ILE   B CB  1 
ATOM   4372 C  CG1 . ILE   B 1 249 ? 1.721   18.916  -4.564  1.00 44.04  ? 249 ILE   B CG1 1 
ATOM   4373 C  CG2 . ILE   B 1 249 ? 2.351   17.594  -6.615  1.00 44.59  ? 249 ILE   B CG2 1 
ATOM   4374 C  CD1 . ILE   B 1 249 ? 0.512   18.136  -4.060  1.00 43.31  ? 249 ILE   B CD1 1 
ATOM   4375 N  N   . LEU   B 1 250 ? 2.496   20.603  -8.906  1.00 39.25  ? 250 LEU   B N   1 
ATOM   4376 C  CA  . LEU   B 1 250 ? 2.772   20.615  -10.341 1.00 39.17  ? 250 LEU   B CA  1 
ATOM   4377 C  C   . LEU   B 1 250 ? 3.917   21.561  -10.714 1.00 45.28  ? 250 LEU   B C   1 
ATOM   4378 O  O   . LEU   B 1 250 ? 4.222   21.690  -11.900 1.00 45.60  ? 250 LEU   B O   1 
ATOM   4379 C  CB  . LEU   B 1 250 ? 1.507   21.009  -11.106 1.00 37.46  ? 250 LEU   B CB  1 
ATOM   4380 C  CG  . LEU   B 1 250 ? 0.396   19.959  -11.187 1.00 35.16  ? 250 LEU   B CG  1 
ATOM   4381 C  CD1 . LEU   B 1 250 ? -0.917  20.587  -11.605 1.00 32.58  ? 250 LEU   B CD1 1 
ATOM   4382 C  CD2 . LEU   B 1 250 ? 0.763   18.846  -12.169 1.00 36.73  ? 250 LEU   B CD2 1 
ATOM   4383 N  N   . GLY   B 1 251 ? 4.529   22.217  -9.713  1.00 45.23  ? 251 GLY   B N   1 
ATOM   4384 C  CA  . GLY   B 1 251 ? 5.570   23.216  -9.911  1.00 45.26  ? 251 GLY   B CA  1 
ATOM   4385 C  C   . GLY   B 1 251 ? 6.729   22.777  -10.813 1.00 47.88  ? 251 GLY   B C   1 
ATOM   4386 O  O   . GLY   B 1 251 ? 7.069   23.508  -11.751 1.00 48.63  ? 251 GLY   B O   1 
ATOM   4387 N  N   . PRO   B 1 252 ? 7.404   21.623  -10.561 1.00 47.73  ? 252 PRO   B N   1 
ATOM   4388 C  CA  . PRO   B 1 252 ? 8.545   21.200  -11.383 1.00 45.68  ? 252 PRO   B CA  1 
ATOM   4389 C  C   . PRO   B 1 252 ? 8.252   21.140  -12.879 1.00 48.32  ? 252 PRO   B C   1 
ATOM   4390 O  O   . PRO   B 1 252 ? 9.111   21.469  -13.696 1.00 54.85  ? 252 PRO   B O   1 
ATOM   4391 C  CB  . PRO   B 1 252 ? 8.899   19.812  -10.825 1.00 44.82  ? 252 PRO   B CB  1 
ATOM   4392 C  CG  . PRO   B 1 252 ? 8.418   19.855  -9.398  1.00 40.81  ? 252 PRO   B CG  1 
ATOM   4393 C  CD  . PRO   B 1 252 ? 7.145   20.680  -9.458  1.00 43.83  ? 252 PRO   B CD  1 
ATOM   4394 N  N   . LEU   B 1 253 ? 7.027   20.727  -13.210 1.00 45.28  ? 253 LEU   B N   1 
ATOM   4395 C  CA  . LEU   B 1 253 ? 6.599   20.504  -14.578 1.00 41.44  ? 253 LEU   B CA  1 
ATOM   4396 C  C   . LEU   B 1 253 ? 6.250   21.820  -15.282 1.00 44.80  ? 253 LEU   B C   1 
ATOM   4397 O  O   . LEU   B 1 253 ? 6.454   21.942  -16.497 1.00 41.47  ? 253 LEU   B O   1 
ATOM   4398 C  CB  . LEU   B 1 253 ? 5.410   19.547  -14.484 1.00 41.12  ? 253 LEU   B CB  1 
ATOM   4399 C  CG  . LEU   B 1 253 ? 5.728   18.132  -13.981 1.00 39.59  ? 253 LEU   B CG  1 
ATOM   4400 C  CD1 . LEU   B 1 253 ? 4.455   17.352  -13.711 1.00 38.12  ? 253 LEU   B CD1 1 
ATOM   4401 C  CD2 . LEU   B 1 253 ? 6.586   17.374  -14.981 1.00 38.33  ? 253 LEU   B CD2 1 
ATOM   4402 N  N   . SER   B 1 254 ? 5.710   22.789  -14.520 1.00 41.63  ? 254 SER   B N   1 
ATOM   4403 C  CA  . SER   B 1 254 ? 5.408   24.117  -15.039 1.00 40.95  ? 254 SER   B CA  1 
ATOM   4404 C  C   . SER   B 1 254 ? 6.709   24.794  -15.469 1.00 44.34  ? 254 SER   B C   1 
ATOM   4405 O  O   . SER   B 1 254 ? 6.808   25.356  -16.571 1.00 46.18  ? 254 SER   B O   1 
ATOM   4406 C  CB  . SER   B 1 254 ? 4.677   24.952  -14.021 1.00 41.38  ? 254 SER   B CB  1 
ATOM   4407 O  OG  . SER   B 1 254 ? 4.591   26.310  -14.436 1.00 43.12  ? 254 SER   B OG  1 
ATOM   4408 N  N   . ALA   B 1 255 ? 7.700   24.710  -14.575 1.00 40.05  ? 255 ALA   B N   1 
ATOM   4409 C  CA  . ALA   B 1 255 ? 9.055   25.149  -14.863 1.00 44.47  ? 255 ALA   B CA  1 
ATOM   4410 C  C   . ALA   B 1 255 ? 9.578   24.459  -16.124 1.00 48.19  ? 255 ALA   B C   1 
ATOM   4411 O  O   . ALA   B 1 255 ? 9.960   25.121  -17.086 1.00 47.95  ? 255 ALA   B O   1 
ATOM   4412 C  CB  . ALA   B 1 255 ? 9.943   24.873  -13.672 1.00 43.28  ? 255 ALA   B CB  1 
ATOM   4413 N  N   . GLN   B 1 256 ? 9.545   23.123  -16.146 1.00 48.24  ? 256 GLN   B N   1 
ATOM   4414 C  CA  . GLN   B 1 256 ? 10.257  22.387  -17.177 1.00 46.17  ? 256 GLN   B CA  1 
ATOM   4415 C  C   . GLN   B 1 256 ? 9.727   22.737  -18.562 1.00 46.35  ? 256 GLN   B C   1 
ATOM   4416 O  O   . GLN   B 1 256 ? 10.497  22.852  -19.504 1.00 46.33  ? 256 GLN   B O   1 
ATOM   4417 C  CB  . GLN   B 1 256 ? 10.190  20.875  -17.013 1.00 50.90  ? 256 GLN   B CB  1 
ATOM   4418 C  CG  . GLN   B 1 256 ? 11.381  20.171  -17.651 1.00 57.44  ? 256 GLN   B CG  1 
ATOM   4419 C  CD  . GLN   B 1 256 ? 11.292  18.666  -17.555 1.00 61.99  ? 256 GLN   B CD  1 
ATOM   4420 O  OE1 . GLN   B 1 256 ? 11.343  18.080  -16.465 1.00 67.00  ? 256 GLN   B OE1 1 
ATOM   4421 N  NE2 . GLN   B 1 256 ? 11.152  18.031  -18.709 1.00 60.16  ? 256 GLN   B NE2 1 
ATOM   4422 N  N   . THR   B 1 257 ? 8.415   22.899  -18.690 1.00 44.30  ? 257 THR   B N   1 
ATOM   4423 C  CA  . THR   B 1 257 ? 7.817   23.085  -19.998 1.00 45.35  ? 257 THR   B CA  1 
ATOM   4424 C  C   . THR   B 1 257 ? 7.619   24.573  -20.330 1.00 45.26  ? 257 THR   B C   1 
ATOM   4425 O  O   . THR   B 1 257 ? 7.432   24.917  -21.484 1.00 42.07  ? 257 THR   B O   1 
ATOM   4426 C  CB  . THR   B 1 257 ? 6.510   22.291  -20.017 1.00 49.35  ? 257 THR   B CB  1 
ATOM   4427 O  OG1 . THR   B 1 257 ? 5.708   22.821  -18.959 1.00 47.33  ? 257 THR   B OG1 1 
ATOM   4428 C  CG2 . THR   B 1 257 ? 6.740   20.794  -19.878 1.00 48.98  ? 257 THR   B CG2 1 
ATOM   4429 N  N   . GLY   B 1 258 ? 7.615   25.469  -19.337 1.00 47.34  ? 258 GLY   B N   1 
ATOM   4430 C  CA  . GLY   B 1 258 ? 7.275   26.860  -19.584 1.00 47.84  ? 258 GLY   B CA  1 
ATOM   4431 C  C   . GLY   B 1 258 ? 5.764   27.115  -19.626 1.00 48.74  ? 258 GLY   B C   1 
ATOM   4432 O  O   . GLY   B 1 258 ? 5.349   28.246  -19.884 1.00 53.22  ? 258 GLY   B O   1 
ATOM   4433 N  N   . ILE   B 1 259 ? 4.943   26.089  -19.347 1.00 46.82  ? 259 ILE   B N   1 
ATOM   4434 C  CA  . ILE   B 1 259 ? 3.495   26.245  -19.310 1.00 49.86  ? 259 ILE   B CA  1 
ATOM   4435 C  C   . ILE   B 1 259 ? 3.047   26.263  -17.852 1.00 52.75  ? 259 ILE   B C   1 
ATOM   4436 O  O   . ILE   B 1 259 ? 3.378   25.350  -17.097 1.00 51.58  ? 259 ILE   B O   1 
ATOM   4437 C  CB  . ILE   B 1 259 ? 2.759   25.145  -20.100 1.00 53.76  ? 259 ILE   B CB  1 
ATOM   4438 C  CG1 . ILE   B 1 259 ? 3.216   25.078  -21.560 1.00 55.46  ? 259 ILE   B CG1 1 
ATOM   4439 C  CG2 . ILE   B 1 259 ? 1.239   25.325  -20.014 1.00 52.19  ? 259 ILE   B CG2 1 
ATOM   4440 C  CD1 . ILE   B 1 259 ? 4.397   24.164  -21.791 1.00 55.65  ? 259 ILE   B CD1 1 
ATOM   4441 N  N   . ALA   B 1 260 ? 2.295   27.312  -17.485 1.00 45.82  ? 260 ALA   B N   1 
ATOM   4442 C  CA  . ALA   B 1 260 ? 1.841   27.509  -16.119 1.00 42.77  ? 260 ALA   B CA  1 
ATOM   4443 C  C   . ALA   B 1 260 ? 0.519   26.783  -15.918 1.00 37.06  ? 260 ALA   B C   1 
ATOM   4444 O  O   . ALA   B 1 260 ? -0.231  26.593  -16.879 1.00 41.16  ? 260 ALA   B O   1 
ATOM   4445 C  CB  . ALA   B 1 260 ? 1.700   28.996  -15.843 1.00 44.19  ? 260 ALA   B CB  1 
ATOM   4446 N  N   . VAL   B 1 261 ? 0.208   26.420  -14.667 1.00 35.57  ? 261 VAL   B N   1 
ATOM   4447 C  CA  . VAL   B 1 261 ? -0.897  25.508  -14.421 1.00 31.07  ? 261 VAL   B CA  1 
ATOM   4448 C  C   . VAL   B 1 261 ? -2.174  26.106  -15.007 1.00 33.25  ? 261 VAL   B C   1 
ATOM   4449 O  O   . VAL   B 1 261 ? -2.882  25.463  -15.809 1.00 32.85  ? 261 VAL   B O   1 
ATOM   4450 C  CB  . VAL   B 1 261 ? -1.067  25.153  -12.930 1.00 32.61  ? 261 VAL   B CB  1 
ATOM   4451 C  CG1 . VAL   B 1 261 ? -2.181  24.120  -12.746 1.00 34.73  ? 261 VAL   B CG1 1 
ATOM   4452 C  CG2 . VAL   B 1 261 ? 0.230   24.655  -12.309 1.00 29.86  ? 261 VAL   B CG2 1 
ATOM   4453 N  N   . LEU   B 1 262 ? -2.416  27.391  -14.688 1.00 35.50  ? 262 LEU   B N   1 
ATOM   4454 C  CA  . LEU   B 1 262 ? -3.645  28.049  -15.104 1.00 35.43  ? 262 LEU   B CA  1 
ATOM   4455 C  C   . LEU   B 1 262 ? -3.696  28.234  -16.627 1.00 35.36  ? 262 LEU   B C   1 
ATOM   4456 O  O   . LEU   B 1 262 ? -4.787  28.219  -17.221 1.00 36.11  ? 262 LEU   B O   1 
ATOM   4457 C  CB  . LEU   B 1 262 ? -3.840  29.335  -14.296 1.00 40.86  ? 262 LEU   B CB  1 
ATOM   4458 C  CG  . LEU   B 1 262 ? -4.123  29.146  -12.795 1.00 41.40  ? 262 LEU   B CG  1 
ATOM   4459 C  CD1 . LEU   B 1 262 ? -4.090  30.452  -12.014 1.00 43.71  ? 262 LEU   B CD1 1 
ATOM   4460 C  CD2 . LEU   B 1 262 ? -5.477  28.492  -12.593 1.00 43.19  ? 262 LEU   B CD2 1 
ATOM   4461 N  N   . ASP   B 1 263 ? -2.523  28.293  -17.272 1.00 41.30  ? 263 ASP   B N   1 
ATOM   4462 C  CA  . ASP   B 1 263 ? -2.413  28.179  -18.729 1.00 43.26  ? 263 ASP   B CA  1 
ATOM   4463 C  C   . ASP   B 1 263 ? -2.874  26.782  -19.172 1.00 40.83  ? 263 ASP   B C   1 
ATOM   4464 O  O   . ASP   B 1 263 ? -3.773  26.638  -20.007 1.00 37.56  ? 263 ASP   B O   1 
ATOM   4465 C  CB  . ASP   B 1 263 ? -1.019  28.620  -19.162 1.00 43.72  ? 263 ASP   B CB  1 
ATOM   4466 C  CG  . ASP   B 1 263 ? -0.662  28.619  -20.645 1.00 44.58  ? 263 ASP   B CG  1 
ATOM   4467 O  OD1 . ASP   B 1 263 ? -1.563  28.487  -21.538 1.00 45.98  ? 263 ASP   B OD1 1 
ATOM   4468 O  OD2 . ASP   B 1 263 ? 0.548   28.764  -20.895 1.00 45.86  ? 263 ASP   B OD2 1 
ATOM   4469 N  N   . MET   B 1 264 ? -2.351  25.731  -18.527 1.00 46.12  ? 264 MET   B N   1 
ATOM   4470 C  CA  . MET   B 1 264 ? -2.778  24.374  -18.852 1.00 36.73  ? 264 MET   B CA  1 
ATOM   4471 C  C   . MET   B 1 264 ? -4.267  24.186  -18.528 1.00 39.09  ? 264 MET   B C   1 
ATOM   4472 O  O   . MET   B 1 264 ? -4.968  23.472  -19.245 1.00 38.46  ? 264 MET   B O   1 
ATOM   4473 C  CB  . MET   B 1 264 ? -1.873  23.355  -18.144 1.00 40.82  ? 264 MET   B CB  1 
ATOM   4474 C  CG  . MET   B 1 264 ? -1.920  21.958  -18.758 1.00 39.44  ? 264 MET   B CG  1 
ATOM   4475 S  SD  . MET   B 1 264 ? -1.202  21.801  -20.410 1.00 36.35  ? 264 MET   B SD  1 
ATOM   4476 C  CE  . MET   B 1 264 ? 0.422   21.659  -19.675 1.00 30.64  ? 264 MET   B CE  1 
ATOM   4477 N  N   . CYS   B 1 265 ? -4.809  24.886  -17.511 1.00 42.13  ? 265 CYS   B N   1 
ATOM   4478 C  CA  . CYS   B 1 265 ? -6.230  24.747  -17.196 1.00 37.17  ? 265 CYS   B CA  1 
ATOM   4479 C  C   . CYS   B 1 265 ? -7.101  25.218  -18.358 1.00 40.01  ? 265 CYS   B C   1 
ATOM   4480 O  O   . CYS   B 1 265 ? -8.128  24.582  -18.689 1.00 40.02  ? 265 CYS   B O   1 
ATOM   4481 C  CB  . CYS   B 1 265 ? -6.588  25.437  -15.883 1.00 44.09  ? 265 CYS   B CB  1 
ATOM   4482 S  SG  . CYS   B 1 265 ? -5.988  24.593  -14.384 1.00 44.69  ? 265 CYS   B SG  1 
ATOM   4483 N  N   . ALA   B 1 266 ? -6.668  26.324  -18.999 1.00 48.81  ? 266 ALA   B N   1 
ATOM   4484 C  CA  . ALA   B 1 266 ? -7.335  26.881  -20.174 1.00 45.52  ? 266 ALA   B CA  1 
ATOM   4485 C  C   . ALA   B 1 266 ? -7.386  25.863  -21.306 1.00 40.59  ? 266 ALA   B C   1 
ATOM   4486 O  O   . ALA   B 1 266 ? -8.443  25.654  -21.902 1.00 43.30  ? 266 ALA   B O   1 
ATOM   4487 C  CB  . ALA   B 1 266 ? -6.656  28.157  -20.628 1.00 52.19  ? 266 ALA   B CB  1 
ATOM   4488 N  N   . SER   B 1 267 ? -6.247  25.205  -21.568 1.00 46.60  ? 267 SER   B N   1 
ATOM   4489 C  CA  . SER   B 1 267 ? -6.199  24.075  -22.488 1.00 40.52  ? 267 SER   B CA  1 
ATOM   4490 C  C   . SER   B 1 267 ? -7.224  23.034  -22.067 1.00 34.72  ? 267 SER   B C   1 
ATOM   4491 O  O   . SER   B 1 267 ? -8.060  22.660  -22.873 1.00 39.65  ? 267 SER   B O   1 
ATOM   4492 C  CB  . SER   B 1 267 ? -4.804  23.475  -22.595 1.00 46.16  ? 267 SER   B CB  1 
ATOM   4493 O  OG  . SER   B 1 267 ? -3.823  24.417  -23.031 1.00 49.49  ? 267 SER   B OG  1 
ATOM   4494 N  N   . LEU   B 1 268 ? -7.221  22.618  -20.789 1.00 42.80  ? 268 LEU   B N   1 
ATOM   4495 C  CA  . LEU   B 1 268 ? -8.157  21.605  -20.284 1.00 40.05  ? 268 LEU   B CA  1 
ATOM   4496 C  C   . LEU   B 1 268 ? -9.622  22.059  -20.348 1.00 39.42  ? 268 LEU   B C   1 
ATOM   4497 O  O   . LEU   B 1 268 ? -10.519 21.276  -20.691 1.00 37.85  ? 268 LEU   B O   1 
ATOM   4498 C  CB  . LEU   B 1 268 ? -7.733  21.234  -18.859 1.00 44.68  ? 268 LEU   B CB  1 
ATOM   4499 C  CG  . LEU   B 1 268 ? -8.610  20.225  -18.095 1.00 43.13  ? 268 LEU   B CG  1 
ATOM   4500 C  CD1 . LEU   B 1 268 ? -8.883  18.945  -18.853 1.00 42.11  ? 268 LEU   B CD1 1 
ATOM   4501 C  CD2 . LEU   B 1 268 ? -7.979  19.900  -16.753 1.00 41.47  ? 268 LEU   B CD2 1 
ATOM   4502 N  N   . LYS   B 1 269 ? -9.886  23.328  -20.012 1.00 48.21  ? 269 LYS   B N   1 
ATOM   4503 C  CA  . LYS   B 1 269 ? -11.227 23.888  -20.151 1.00 50.28  ? 269 LYS   B CA  1 
ATOM   4504 C  C   . LYS   B 1 269 ? -11.773 23.614  -21.554 1.00 48.68  ? 269 LYS   B C   1 
ATOM   4505 O  O   . LYS   B 1 269 ? -12.874 23.081  -21.712 1.00 47.63  ? 269 LYS   B O   1 
ATOM   4506 C  CB  . LYS   B 1 269 ? -11.147 25.381  -19.803 1.00 60.60  ? 269 LYS   B CB  1 
ATOM   4507 C  CG  . LYS   B 1 269 ? -12.442 26.201  -19.918 1.00 70.32  ? 269 LYS   B CG  1 
ATOM   4508 C  CD  . LYS   B 1 269 ? -12.238 27.704  -19.726 1.00 78.80  ? 269 LYS   B CD  1 
ATOM   4509 C  CE  . LYS   B 1 269 ? -11.483 28.031  -18.466 1.00 86.81  ? 269 LYS   B CE  1 
ATOM   4510 N  NZ  . LYS   B 1 269 ? -11.402 29.469  -18.191 1.00 95.16  ? 269 LYS   B NZ  1 
ATOM   4511 N  N   . GLU   B 1 270 ? -10.979 23.959  -22.581 1.00 55.37  ? 270 GLU   B N   1 
ATOM   4512 C  CA  . GLU   B 1 270 ? -11.426 23.873  -23.966 1.00 51.52  ? 270 GLU   B CA  1 
ATOM   4513 C  C   . GLU   B 1 270 ? -11.715 22.421  -24.310 1.00 51.67  ? 270 GLU   B C   1 
ATOM   4514 O  O   . GLU   B 1 270 ? -12.688 22.138  -25.012 1.00 51.32  ? 270 GLU   B O   1 
ATOM   4515 C  CB  . GLU   B 1 270 ? -10.430 24.383  -25.012 1.00 56.61  ? 270 GLU   B CB  1 
ATOM   4516 C  CG  . GLU   B 1 270 ? -9.929  25.815  -24.816 1.00 60.92  ? 270 GLU   B CG  1 
ATOM   4517 C  CD  . GLU   B 1 270 ? -10.980 26.908  -24.687 1.00 65.07  ? 270 GLU   B CD  1 
ATOM   4518 O  OE1 . GLU   B 1 270 ? -11.930 26.933  -25.501 1.00 69.07  ? 270 GLU   B OE1 1 
ATOM   4519 O  OE2 . GLU   B 1 270 ? -10.830 27.744  -23.766 1.00 64.67  ? 270 GLU   B OE2 1 
ATOM   4520 N  N   . LEU   B 1 271 ? -10.869 21.511  -23.795 1.00 51.47  ? 271 LEU   B N   1 
ATOM   4521 C  CA  . LEU   B 1 271 ? -11.002 20.092  -24.086 1.00 44.43  ? 271 LEU   B CA  1 
ATOM   4522 C  C   . LEU   B 1 271 ? -12.304 19.565  -23.494 1.00 42.94  ? 271 LEU   B C   1 
ATOM   4523 O  O   . LEU   B 1 271 ? -12.990 18.769  -24.126 1.00 48.65  ? 271 LEU   B O   1 
ATOM   4524 C  CB  . LEU   B 1 271 ? -9.782  19.322  -23.575 1.00 48.84  ? 271 LEU   B CB  1 
ATOM   4525 C  CG  . LEU   B 1 271 ? -8.447  19.613  -24.277 1.00 50.18  ? 271 LEU   B CG  1 
ATOM   4526 C  CD1 . LEU   B 1 271 ? -7.240  19.224  -23.441 1.00 51.67  ? 271 LEU   B CD1 1 
ATOM   4527 C  CD2 . LEU   B 1 271 ? -8.358  18.910  -25.618 1.00 51.35  ? 271 LEU   B CD2 1 
ATOM   4528 N  N   . LEU   B 1 272 ? -12.671 20.025  -22.292 1.00 48.60  ? 272 LEU   B N   1 
ATOM   4529 C  CA  . LEU   B 1 272 ? -13.942 19.621  -21.699 1.00 48.69  ? 272 LEU   B CA  1 
ATOM   4530 C  C   . LEU   B 1 272 ? -15.127 20.195  -22.485 1.00 52.79  ? 272 LEU   B C   1 
ATOM   4531 O  O   . LEU   B 1 272 ? -16.093 19.488  -22.768 1.00 47.35  ? 272 LEU   B O   1 
ATOM   4532 C  CB  . LEU   B 1 272 ? -13.960 20.055  -20.235 1.00 49.73  ? 272 LEU   B CB  1 
ATOM   4533 C  CG  . LEU   B 1 272 ? -13.015 19.281  -19.307 1.00 47.86  ? 272 LEU   B CG  1 
ATOM   4534 C  CD1 . LEU   B 1 272 ? -12.857 19.961  -17.948 1.00 45.34  ? 272 LEU   B CD1 1 
ATOM   4535 C  CD2 . LEU   B 1 272 ? -13.511 17.834  -19.157 1.00 43.68  ? 272 LEU   B CD2 1 
ATOM   4536 N  N   . GLN   B 1 273 ? -15.055 21.485  -22.842 1.00 63.54  ? 273 GLN   B N   1 
ATOM   4537 C  CA  . GLN   B 1 273 ? -16.123 22.144  -23.586 1.00 65.38  ? 273 GLN   B CA  1 
ATOM   4538 C  C   . GLN   B 1 273 ? -16.176 21.587  -25.010 1.00 67.93  ? 273 GLN   B C   1 
ATOM   4539 O  O   . GLN   B 1 273 ? -17.137 20.902  -25.374 1.00 64.63  ? 273 GLN   B O   1 
ATOM   4540 C  CB  . GLN   B 1 273 ? -15.920 23.661  -23.589 1.00 69.74  ? 273 GLN   B CB  1 
ATOM   4541 C  CG  . GLN   B 1 273 ? -15.887 24.301  -22.203 1.00 75.28  ? 273 GLN   B CG  1 
ATOM   4542 C  CD  . GLN   B 1 273 ? -15.221 25.664  -22.168 1.00 79.93  ? 273 GLN   B CD  1 
ATOM   4543 O  OE1 . GLN   B 1 273 ? -14.256 25.934  -22.892 1.00 83.19  ? 273 GLN   B OE1 1 
ATOM   4544 N  NE2 . GLN   B 1 273 ? -15.717 26.547  -21.314 1.00 79.39  ? 273 GLN   B NE2 1 
ATOM   4545 N  N   . ASN   B 1 274 ? -15.105 21.850  -25.779 1.00 74.43  ? 274 ASN   B N   1 
ATOM   4546 C  CA  . ASN   B 1 274 ? -15.062 21.619  -27.221 1.00 80.45  ? 274 ASN   B CA  1 
ATOM   4547 C  C   . ASN   B 1 274 ? -14.925 20.127  -27.532 1.00 78.24  ? 274 ASN   B C   1 
ATOM   4548 O  O   . ASN   B 1 274 ? -15.652 19.596  -28.366 1.00 85.94  ? 274 ASN   B O   1 
ATOM   4549 C  CB  . ASN   B 1 274 ? -13.923 22.389  -27.893 1.00 79.01  ? 274 ASN   B CB  1 
ATOM   4550 C  CG  . ASN   B 1 274 ? -14.007 23.885  -27.677 1.00 83.84  ? 274 ASN   B CG  1 
ATOM   4551 O  OD1 . ASN   B 1 274 ? -13.087 24.498  -27.118 1.00 75.80  ? 274 ASN   B OD1 1 
ATOM   4552 N  ND2 . ASN   B 1 274 ? -15.094 24.495  -28.125 1.00 88.23  ? 274 ASN   B ND2 1 
ATOM   4553 N  N   . GLY   B 1 275 ? -13.996 19.455  -26.840 1.00 82.54  ? 275 GLY   B N   1 
ATOM   4554 C  CA  . GLY   B 1 275 ? -13.605 18.087  -27.151 1.00 83.24  ? 275 GLY   B CA  1 
ATOM   4555 C  C   . GLY   B 1 275 ? -12.115 18.023  -27.496 1.00 82.33  ? 275 GLY   B C   1 
ATOM   4556 O  O   . GLY   B 1 275 ? -11.405 19.024  -27.405 1.00 66.05  ? 275 GLY   B O   1 
ATOM   4557 N  N   . MET   B 1 276 ? -11.636 16.844  -27.916 1.00 88.85  ? 276 MET   B N   1 
ATOM   4558 C  CA  . MET   B 1 276 ? -10.249 16.709  -28.358 1.00 90.75  ? 276 MET   B CA  1 
ATOM   4559 C  C   . MET   B 1 276 ? -10.116 17.111  -29.835 1.00 87.14  ? 276 MET   B C   1 
ATOM   4560 O  O   . MET   B 1 276 ? -9.032  17.007  -30.416 1.00 85.05  ? 276 MET   B O   1 
ATOM   4561 C  CB  . MET   B 1 276 ? -9.694  15.301  -28.069 1.00 89.78  ? 276 MET   B CB  1 
ATOM   4562 C  CG  . MET   B 1 276 ? -8.697  15.266  -26.903 1.00 86.72  ? 276 MET   B CG  1 
ATOM   4563 S  SD  . MET   B 1 276 ? -8.250  13.649  -26.236 1.00 74.56  ? 276 MET   B SD  1 
ATOM   4564 C  CE  . MET   B 1 276 ? -9.719  13.441  -25.223 1.00 60.77  ? 276 MET   B CE  1 
ATOM   4565 N  N   . ASN   B 1 277 ? -11.211 17.637  -30.411 1.00 75.33  ? 277 ASN   B N   1 
ATOM   4566 C  CA  . ASN   B 1 277 ? -11.300 17.930  -31.829 1.00 75.72  ? 277 ASN   B CA  1 
ATOM   4567 C  C   . ASN   B 1 277 ? -10.628 16.779  -32.578 1.00 73.80  ? 277 ASN   B C   1 
ATOM   4568 O  O   . ASN   B 1 277 ? -9.728  16.987  -33.386 1.00 67.30  ? 277 ASN   B O   1 
ATOM   4569 C  CB  . ASN   B 1 277 ? -10.838 19.357  -32.123 1.00 82.92  ? 277 ASN   B CB  1 
ATOM   4570 C  CG  . ASN   B 1 277 ? -11.870 20.395  -31.720 1.00 90.56  ? 277 ASN   B CG  1 
ATOM   4571 O  OD1 . ASN   B 1 277 ? -11.648 21.166  -30.773 1.00 85.79  ? 277 ASN   B OD1 1 
ATOM   4572 N  ND2 . ASN   B 1 277 ? -13.001 20.436  -32.418 1.00 84.01  ? 277 ASN   B ND2 1 
ATOM   4573 N  N   . GLY   B 1 278 ? -11.081 15.558  -32.252 1.00 80.12  ? 278 GLY   B N   1 
ATOM   4574 C  CA  . GLY   B 1 278 ? -10.696 14.332  -32.937 1.00 78.45  ? 278 GLY   B CA  1 
ATOM   4575 C  C   . GLY   B 1 278 ? -9.546  13.621  -32.230 1.00 75.20  ? 278 GLY   B C   1 
ATOM   4576 O  O   . GLY   B 1 278 ? -9.728  12.571  -31.597 1.00 58.30  ? 278 GLY   B O   1 
ATOM   4577 N  N   . ARG   B 1 279 ? -8.385  14.276  -32.322 1.00 66.91  ? 279 ARG   B N   1 
ATOM   4578 C  CA  . ARG   B 1 279 ? -7.070  13.695  -32.096 1.00 71.39  ? 279 ARG   B CA  1 
ATOM   4579 C  C   . ARG   B 1 279 ? -6.981  12.811  -30.841 1.00 59.77  ? 279 ARG   B C   1 
ATOM   4580 O  O   . ARG   B 1 279 ? -7.973  12.337  -30.270 1.00 48.34  ? 279 ARG   B O   1 
ATOM   4581 C  CB  . ARG   B 1 279 ? -6.072  14.869  -32.117 1.00 73.68  ? 279 ARG   B CB  1 
ATOM   4582 C  CG  . ARG   B 1 279 ? -5.292  15.088  -33.411 1.00 72.09  ? 279 ARG   B CG  1 
ATOM   4583 C  CD  . ARG   B 1 279 ? -5.415  16.490  -34.009 1.00 75.69  ? 279 ARG   B CD  1 
ATOM   4584 N  NE  . ARG   B 1 279 ? -5.757  17.552  -33.054 1.00 88.49  ? 279 ARG   B NE  1 
ATOM   4585 C  CZ  . ARG   B 1 279 ? -5.932  18.843  -33.340 1.00 103.01 ? 279 ARG   B CZ  1 
ATOM   4586 N  NH1 . ARG   B 1 279 ? -5.573  19.335  -34.517 1.00 101.98 ? 279 ARG   B NH1 1 
ATOM   4587 N  NH2 . ARG   B 1 279 ? -6.429  19.653  -32.418 1.00 103.62 ? 279 ARG   B NH2 1 
ATOM   4588 N  N   . THR   B 1 280 ? -5.719  12.502  -30.520 1.00 52.78  ? 280 THR   B N   1 
ATOM   4589 C  CA  . THR   B 1 280 ? -5.318  11.709  -29.381 1.00 41.96  ? 280 THR   B CA  1 
ATOM   4590 C  C   . THR   B 1 280 ? -4.208  12.491  -28.700 1.00 38.14  ? 280 THR   B C   1 
ATOM   4591 O  O   . THR   B 1 280 ? -3.658  13.431  -29.277 1.00 40.37  ? 280 THR   B O   1 
ATOM   4592 C  CB  . THR   B 1 280 ? -4.833  10.330  -29.837 1.00 41.32  ? 280 THR   B CB  1 
ATOM   4593 O  OG1 . THR   B 1 280 ? -3.679  10.623  -30.620 1.00 38.88  ? 280 THR   B OG1 1 
ATOM   4594 C  CG2 . THR   B 1 280 ? -5.878  9.543   -30.610 1.00 37.51  ? 280 THR   B CG2 1 
ATOM   4595 N  N   . ILE   B 1 281 ? -3.920  12.111  -27.457 1.00 32.78  ? 281 ILE   B N   1 
ATOM   4596 C  CA  . ILE   B 1 281 ? -2.814  12.655  -26.698 1.00 30.39  ? 281 ILE   B CA  1 
ATOM   4597 C  C   . ILE   B 1 281 ? -2.126  11.453  -26.071 1.00 30.07  ? 281 ILE   B C   1 
ATOM   4598 O  O   . ILE   B 1 281 ? -2.781  10.669  -25.395 1.00 31.05  ? 281 ILE   B O   1 
ATOM   4599 C  CB  . ILE   B 1 281 ? -3.329  13.635  -25.629 1.00 30.84  ? 281 ILE   B CB  1 
ATOM   4600 C  CG1 . ILE   B 1 281 ? -4.120  14.794  -26.245 1.00 33.31  ? 281 ILE   B CG1 1 
ATOM   4601 C  CG2 . ILE   B 1 281 ? -2.178  14.128  -24.760 1.00 33.70  ? 281 ILE   B CG2 1 
ATOM   4602 C  CD1 . ILE   B 1 281 ? -4.728  15.759  -25.242 1.00 33.80  ? 281 ILE   B CD1 1 
ATOM   4603 N  N   . LEU   B 1 282 ? -0.831  11.294  -26.334 1.00 30.10  ? 282 LEU   B N   1 
ATOM   4604 C  CA  . LEU   B 1 282 ? -0.094  10.126  -25.884 1.00 31.19  ? 282 LEU   B CA  1 
ATOM   4605 C  C   . LEU   B 1 282 ? -0.877  8.842   -26.155 1.00 28.12  ? 282 LEU   B C   1 
ATOM   4606 O  O   . LEU   B 1 282 ? -1.001  7.995   -25.287 1.00 28.49  ? 282 LEU   B O   1 
ATOM   4607 C  CB  . LEU   B 1 282 ? 0.222   10.297  -24.394 1.00 32.58  ? 282 LEU   B CB  1 
ATOM   4608 C  CG  . LEU   B 1 282 ? 1.380   11.232  -24.048 1.00 34.18  ? 282 LEU   B CG  1 
ATOM   4609 C  CD1 . LEU   B 1 282 ? 1.546   11.458  -22.555 1.00 31.78  ? 282 LEU   B CD1 1 
ATOM   4610 C  CD2 . LEU   B 1 282 ? 2.662   10.655  -24.654 1.00 34.95  ? 282 LEU   B CD2 1 
ATOM   4611 N  N   . GLY   B 1 283 ? -1.436  8.694   -27.348 1.00 31.52  ? 283 GLY   B N   1 
ATOM   4612 C  CA  . GLY   B 1 283 ? -2.111  7.460   -27.745 1.00 32.53  ? 283 GLY   B CA  1 
ATOM   4613 C  C   . GLY   B 1 283 ? -3.470  7.224   -27.079 1.00 33.95  ? 283 GLY   B C   1 
ATOM   4614 O  O   . GLY   B 1 283 ? -3.962  6.094   -27.071 1.00 36.12  ? 283 GLY   B O   1 
ATOM   4615 N  N   . SER   B 1 284 ? -4.097  8.275   -26.532 1.00 36.59  ? 284 SER   B N   1 
ATOM   4616 C  CA  . SER   B 1 284 ? -5.400  8.120   -25.904 1.00 33.48  ? 284 SER   B CA  1 
ATOM   4617 C  C   . SER   B 1 284 ? -6.424  9.100   -26.479 1.00 32.50  ? 284 SER   B C   1 
ATOM   4618 O  O   . SER   B 1 284 ? -6.130  10.265  -26.729 1.00 28.77  ? 284 SER   B O   1 
ATOM   4619 C  CB  . SER   B 1 284 ? -5.313  8.268   -24.407 1.00 33.60  ? 284 SER   B CB  1 
ATOM   4620 O  OG  . SER   B 1 284 ? -6.595  8.039   -23.829 1.00 36.90  ? 284 SER   B OG  1 
ATOM   4621 N  N   . ALA   B 1 285 ? -7.660  8.617   -26.592 1.00 34.90  ? 285 ALA   B N   1 
ATOM   4622 C  CA  . ALA   B 1 285 ? -8.787  9.468   -26.938 1.00 42.66  ? 285 ALA   B CA  1 
ATOM   4623 C  C   . ALA   B 1 285 ? -9.592  9.869   -25.693 1.00 41.70  ? 285 ALA   B C   1 
ATOM   4624 O  O   . ALA   B 1 285 ? -10.656 10.463  -25.831 1.00 49.42  ? 285 ALA   B O   1 
ATOM   4625 C  CB  . ALA   B 1 285 ? -9.652  8.751   -27.972 1.00 42.41  ? 285 ALA   B CB  1 
ATOM   4626 N  N   . LEU   B 1 286 ? -9.095  9.553   -24.488 1.00 37.79  ? 286 LEU   B N   1 
ATOM   4627 C  CA  . LEU   B 1 286 ? -9.699  9.983   -23.227 1.00 37.89  ? 286 LEU   B CA  1 
ATOM   4628 C  C   . LEU   B 1 286 ? -8.704  10.875  -22.499 1.00 31.39  ? 286 LEU   B C   1 
ATOM   4629 O  O   . LEU   B 1 286 ? -7.513  10.813  -22.779 1.00 29.64  ? 286 LEU   B O   1 
ATOM   4630 C  CB  . LEU   B 1 286 ? -10.033 8.805   -22.311 1.00 42.73  ? 286 LEU   B CB  1 
ATOM   4631 C  CG  . LEU   B 1 286 ? -11.279 7.989   -22.645 1.00 44.18  ? 286 LEU   B CG  1 
ATOM   4632 C  CD1 . LEU   B 1 286 ? -11.244 6.621   -21.957 1.00 41.97  ? 286 LEU   B CD1 1 
ATOM   4633 C  CD2 . LEU   B 1 286 ? -12.517 8.780   -22.244 1.00 50.83  ? 286 LEU   B CD2 1 
ATOM   4634 N  N   . LEU   B 1 287 ? -9.199  11.652  -21.533 1.00 29.02  ? 287 LEU   B N   1 
ATOM   4635 C  CA  . LEU   B 1 287 ? -8.340  12.407  -20.638 1.00 32.01  ? 287 LEU   B CA  1 
ATOM   4636 C  C   . LEU   B 1 287 ? -7.979  11.510  -19.454 1.00 29.63  ? 287 LEU   B C   1 
ATOM   4637 O  O   . LEU   B 1 287 ? -8.858  11.181  -18.673 1.00 30.75  ? 287 LEU   B O   1 
ATOM   4638 C  CB  . LEU   B 1 287 ? -9.070  13.673  -20.186 1.00 34.51  ? 287 LEU   B CB  1 
ATOM   4639 C  CG  . LEU   B 1 287 ? -9.320  14.720  -21.274 1.00 38.57  ? 287 LEU   B CG  1 
ATOM   4640 C  CD1 . LEU   B 1 287 ? -10.284 15.787  -20.788 1.00 43.68  ? 287 LEU   B CD1 1 
ATOM   4641 C  CD2 . LEU   B 1 287 ? -8.029  15.371  -21.716 1.00 38.98  ? 287 LEU   B CD2 1 
ATOM   4642 N  N   . GLU   B 1 288 ? -6.711  11.091  -19.358 1.00 28.79  ? 288 GLU   B N   1 
ATOM   4643 C  CA  . GLU   B 1 288 ? -6.268  10.065  -18.415 1.00 28.53  ? 288 GLU   B CA  1 
ATOM   4644 C  C   . GLU   B 1 288 ? -5.949  10.680  -17.052 1.00 27.48  ? 288 GLU   B C   1 
ATOM   4645 O  O   . GLU   B 1 288 ? -5.175  11.648  -16.984 1.00 23.61  ? 288 GLU   B O   1 
ATOM   4646 C  CB  . GLU   B 1 288 ? -4.965  9.393   -18.873 1.00 29.37  ? 288 GLU   B CB  1 
ATOM   4647 C  CG  . GLU   B 1 288 ? -5.063  8.640   -20.197 1.00 30.46  ? 288 GLU   B CG  1 
ATOM   4648 C  CD  . GLU   B 1 288 ? -5.891  7.360   -20.195 1.00 34.49  ? 288 GLU   B CD  1 
ATOM   4649 O  OE1 . GLU   B 1 288 ? -6.133  6.730   -19.160 1.00 31.68  ? 288 GLU   B OE1 1 
ATOM   4650 O  OE2 . GLU   B 1 288 ? -6.315  6.976   -21.290 1.00 40.56  ? 288 GLU   B OE2 1 
ATOM   4651 N  N   . ASP   B 1 289 ? -6.448  10.041  -15.967 1.00 28.06  ? 289 ASP   B N   1 
ATOM   4652 C  CA  . ASP   B 1 289 ? -6.363  10.610  -14.625 1.00 27.67  ? 289 ASP   B CA  1 
ATOM   4653 C  C   . ASP   B 1 289 ? -5.709  9.690   -13.589 1.00 27.80  ? 289 ASP   B C   1 
ATOM   4654 O  O   . ASP   B 1 289 ? -5.813  9.988   -12.396 1.00 26.02  ? 289 ASP   B O   1 
ATOM   4655 C  CB  . ASP   B 1 289 ? -7.726  11.088  -14.122 1.00 28.21  ? 289 ASP   B CB  1 
ATOM   4656 C  CG  . ASP   B 1 289 ? -8.716  10.027  -13.654 1.00 27.14  ? 289 ASP   B CG  1 
ATOM   4657 O  OD1 . ASP   B 1 289 ? -8.488  8.824   -13.902 1.00 26.51  ? 289 ASP   B OD1 1 
ATOM   4658 O  OD2 . ASP   B 1 289 ? -9.705  10.406  -12.991 1.00 28.86  ? 289 ASP   B OD2 1 
ATOM   4659 N  N   . GLU   B 1 290 ? -5.020  8.620   -14.016 1.00 25.58  ? 290 GLU   B N   1 
ATOM   4660 C  CA  . GLU   B 1 290 ? -4.397  7.681   -13.097 1.00 24.97  ? 290 GLU   B CA  1 
ATOM   4661 C  C   . GLU   B 1 290 ? -2.862  7.820   -13.090 1.00 26.33  ? 290 GLU   B C   1 
ATOM   4662 O  O   . GLU   B 1 290 ? -2.169  6.896   -12.666 1.00 26.67  ? 290 GLU   B O   1 
ATOM   4663 C  CB  . GLU   B 1 290 ? -4.866  6.241   -13.359 1.00 24.29  ? 290 GLU   B CB  1 
ATOM   4664 C  CG  . GLU   B 1 290 ? -6.366  6.027   -13.106 1.00 27.94  ? 290 GLU   B CG  1 
ATOM   4665 C  CD  . GLU   B 1 290 ? -6.875  4.711   -12.492 1.00 25.39  ? 290 GLU   B CD  1 
ATOM   4666 O  OE1 . GLU   B 1 290 ? -6.094  3.736   -12.484 1.00 25.74  ? 290 GLU   B OE1 1 
ATOM   4667 O  OE2 . GLU   B 1 290 ? -8.059  4.650   -12.023 1.00 25.86  ? 290 GLU   B OE2 1 
ATOM   4668 N  N   . PHE   B 1 291 ? -2.313  8.977   -13.488 1.00 24.85  ? 291 PHE   B N   1 
ATOM   4669 C  CA  . PHE   B 1 291 ? -0.903  9.260   -13.247 1.00 24.14  ? 291 PHE   B CA  1 
ATOM   4670 C  C   . PHE   B 1 291 ? -0.729  10.479  -12.344 1.00 25.90  ? 291 PHE   B C   1 
ATOM   4671 O  O   . PHE   B 1 291 ? -1.234  11.551  -12.668 1.00 24.48  ? 291 PHE   B O   1 
ATOM   4672 C  CB  . PHE   B 1 291 ? -0.132  9.571   -14.531 1.00 24.62  ? 291 PHE   B CB  1 
ATOM   4673 C  CG  . PHE   B 1 291 ? -0.183  8.495   -15.601 1.00 29.20  ? 291 PHE   B CG  1 
ATOM   4674 C  CD1 . PHE   B 1 291 ? -1.193  8.491   -16.564 1.00 33.36  ? 291 PHE   B CD1 1 
ATOM   4675 C  CD2 . PHE   B 1 291 ? 0.808   7.527   -15.677 1.00 32.58  ? 291 PHE   B CD2 1 
ATOM   4676 C  CE1 . PHE   B 1 291 ? -1.213  7.536   -17.575 1.00 38.66  ? 291 PHE   B CE1 1 
ATOM   4677 C  CE2 . PHE   B 1 291 ? 0.784   6.574   -16.690 1.00 40.87  ? 291 PHE   B CE2 1 
ATOM   4678 C  CZ  . PHE   B 1 291 ? -0.228  6.574   -17.631 1.00 40.45  ? 291 PHE   B CZ  1 
ATOM   4679 N  N   . THR   B 1 292 ? 0.022   10.328  -11.236 1.00 25.72  ? 292 THR   B N   1 
ATOM   4680 C  CA  . THR   B 1 292 ? 0.287   11.444  -10.334 1.00 24.00  ? 292 THR   B CA  1 
ATOM   4681 C  C   . THR   B 1 292 ? 1.425   12.304  -10.886 1.00 25.53  ? 292 THR   B C   1 
ATOM   4682 O  O   . THR   B 1 292 ? 2.177   11.890  -11.781 1.00 26.02  ? 292 THR   B O   1 
ATOM   4683 C  CB  . THR   B 1 292 ? 0.649   10.992  -8.915  1.00 23.67  ? 292 THR   B CB  1 
ATOM   4684 O  OG1 . THR   B 1 292 ? 1.958   10.430  -8.988  1.00 24.63  ? 292 THR   B OG1 1 
ATOM   4685 C  CG2 . THR   B 1 292 ? -0.367  10.077  -8.260  1.00 22.70  ? 292 THR   B CG2 1 
ATOM   4686 N  N   . PRO   B 1 293 ? 1.606   13.534  -10.351 1.00 28.11  ? 293 PRO   B N   1 
ATOM   4687 C  CA  . PRO   B 1 293 ? 2.799   14.343  -10.643 1.00 27.96  ? 293 PRO   B CA  1 
ATOM   4688 C  C   . PRO   B 1 293 ? 4.121   13.616  -10.424 1.00 28.71  ? 293 PRO   B C   1 
ATOM   4689 O  O   . PRO   B 1 293 ? 5.014   13.673  -11.262 1.00 26.19  ? 293 PRO   B O   1 
ATOM   4690 C  CB  . PRO   B 1 293 ? 2.640   15.556  -9.714  1.00 26.95  ? 293 PRO   B CB  1 
ATOM   4691 C  CG  . PRO   B 1 293 ? 1.144   15.715  -9.558  1.00 27.83  ? 293 PRO   B CG  1 
ATOM   4692 C  CD  . PRO   B 1 293 ? 0.597   14.282  -9.571  1.00 29.04  ? 293 PRO   B CD  1 
ATOM   4693 N  N   . PHE   B 1 294 ? 4.236   12.945  -9.284  1.00 29.82  ? 294 PHE   B N   1 
ATOM   4694 C  CA  . PHE   B 1 294 ? 5.418   12.171  -8.963  1.00 34.65  ? 294 PHE   B CA  1 
ATOM   4695 C  C   . PHE   B 1 294 ? 5.626   11.097  -10.031 1.00 33.60  ? 294 PHE   B C   1 
ATOM   4696 O  O   . PHE   B 1 294 ? 6.764   10.871  -10.430 1.00 31.68  ? 294 PHE   B O   1 
ATOM   4697 C  CB  . PHE   B 1 294 ? 5.316   11.496  -7.595  1.00 37.89  ? 294 PHE   B CB  1 
ATOM   4698 C  CG  . PHE   B 1 294 ? 6.492   10.575  -7.299  1.00 51.57  ? 294 PHE   B CG  1 
ATOM   4699 C  CD1 . PHE   B 1 294 ? 6.477   9.233   -7.711  1.00 58.52  ? 294 PHE   B CD1 1 
ATOM   4700 C  CD2 . PHE   B 1 294 ? 7.624   11.055  -6.638  1.00 54.05  ? 294 PHE   B CD2 1 
ATOM   4701 C  CE1 . PHE   B 1 294 ? 7.558   8.394   -7.456  1.00 54.95  ? 294 PHE   B CE1 1 
ATOM   4702 C  CE2 . PHE   B 1 294 ? 8.705   10.216  -6.391  1.00 54.82  ? 294 PHE   B CE2 1 
ATOM   4703 C  CZ  . PHE   B 1 294 ? 8.670   8.891   -6.800  1.00 55.41  ? 294 PHE   B CZ  1 
ATOM   4704 N  N   . ASP   B 1 295 ? 4.543   10.418  -10.460 1.00 26.86  ? 295 ASP   B N   1 
ATOM   4705 C  CA  . ASP   B 1 295 ? 4.657   9.362   -11.462 1.00 26.70  ? 295 ASP   B CA  1 
ATOM   4706 C  C   . ASP   B 1 295 ? 5.305   9.913   -12.735 1.00 29.53  ? 295 ASP   B C   1 
ATOM   4707 O  O   . ASP   B 1 295 ? 6.187   9.271   -13.305 1.00 28.75  ? 295 ASP   B O   1 
ATOM   4708 C  CB  . ASP   B 1 295 ? 3.326   8.697   -11.771 1.00 24.19  ? 295 ASP   B CB  1 
ATOM   4709 C  CG  . ASP   B 1 295 ? 2.711   7.882   -10.639 1.00 24.70  ? 295 ASP   B CG  1 
ATOM   4710 O  OD1 . ASP   B 1 295 ? 3.436   7.618   -9.647  1.00 25.79  ? 295 ASP   B OD1 1 
ATOM   4711 O  OD2 . ASP   B 1 295 ? 1.510   7.570   -10.729 1.00 21.64  ? 295 ASP   B OD2 1 
ATOM   4712 N  N   . VAL   B 1 296 ? 4.902   11.129  -13.126 1.00 30.76  ? 296 VAL   B N   1 
ATOM   4713 C  CA  . VAL   B 1 296 ? 5.345   11.766  -14.356 1.00 32.54  ? 296 VAL   B CA  1 
ATOM   4714 C  C   . VAL   B 1 296 ? 6.808   12.185  -14.240 1.00 36.28  ? 296 VAL   B C   1 
ATOM   4715 O  O   . VAL   B 1 296 ? 7.582   11.933  -15.159 1.00 33.58  ? 296 VAL   B O   1 
ATOM   4716 C  CB  . VAL   B 1 296 ? 4.450   12.955  -14.750 1.00 33.83  ? 296 VAL   B CB  1 
ATOM   4717 C  CG1 . VAL   B 1 296 ? 5.036   13.738  -15.922 1.00 34.28  ? 296 VAL   B CG1 1 
ATOM   4718 C  CG2 . VAL   B 1 296 ? 3.026   12.495  -15.071 1.00 31.42  ? 296 VAL   B CG2 1 
ATOM   4719 N  N   . VAL   B 1 297 ? 7.173   12.805  -13.109 1.00 40.60  ? 297 VAL   B N   1 
ATOM   4720 C  CA  . VAL   B 1 297 ? 8.533   13.278  -12.889 1.00 42.34  ? 297 VAL   B CA  1 
ATOM   4721 C  C   . VAL   B 1 297 ? 9.476   12.076  -12.834 1.00 40.37  ? 297 VAL   B C   1 
ATOM   4722 O  O   . VAL   B 1 297 ? 10.521  12.091  -13.474 1.00 39.68  ? 297 VAL   B O   1 
ATOM   4723 C  CB  . VAL   B 1 297 ? 8.615   14.149  -11.615 1.00 43.75  ? 297 VAL   B CB  1 
ATOM   4724 C  CG1 . VAL   B 1 297 ? 10.040  14.296  -11.092 1.00 45.19  ? 297 VAL   B CG1 1 
ATOM   4725 C  CG2 . VAL   B 1 297 ? 7.975   15.520  -11.810 1.00 44.92  ? 297 VAL   B CG2 1 
ATOM   4726 N  N   . ARG   B 1 298 ? 9.116   11.069  -12.028 1.00 43.54  ? 298 ARG   B N   1 
ATOM   4727 C  CA  . ARG   B 1 298 ? 9.824   9.790   -11.929 1.00 48.18  ? 298 ARG   B CA  1 
ATOM   4728 C  C   . ARG   B 1 298 ? 10.165  9.228   -13.312 1.00 46.80  ? 298 ARG   B C   1 
ATOM   4729 O  O   . ARG   B 1 298 ? 11.308  8.877   -13.583 1.00 42.92  ? 298 ARG   B O   1 
ATOM   4730 C  CB  . ARG   B 1 298 ? 8.914   8.828   -11.148 1.00 57.83  ? 298 ARG   B CB  1 
ATOM   4731 C  CG  . ARG   B 1 298 ? 9.278   7.361   -10.946 1.00 66.26  ? 298 ARG   B CG  1 
ATOM   4732 C  CD  . ARG   B 1 298 ? 10.159  7.138   -9.723  1.00 70.61  ? 298 ARG   B CD  1 
ATOM   4733 N  NE  . ARG   B 1 298 ? 10.202  5.780   -9.160  1.00 72.02  ? 298 ARG   B NE  1 
ATOM   4734 C  CZ  . ARG   B 1 298 ? 10.601  4.667   -9.786  1.00 75.12  ? 298 ARG   B CZ  1 
ATOM   4735 N  NH1 . ARG   B 1 298 ? 10.709  4.638   -11.100 1.00 76.50  ? 298 ARG   B NH1 1 
ATOM   4736 N  NH2 . ARG   B 1 298 ? 10.849  3.562   -9.099  1.00 72.58  ? 298 ARG   B NH2 1 
ATOM   4737 N  N   . GLN   B 1 299 ? 9.165   9.144   -14.190 1.00 46.56  ? 299 GLN   B N   1 
ATOM   4738 C  CA  . GLN   B 1 299 ? 9.296   8.381   -15.419 1.00 48.46  ? 299 GLN   B CA  1 
ATOM   4739 C  C   . GLN   B 1 299 ? 10.113  9.181   -16.429 1.00 50.09  ? 299 GLN   B C   1 
ATOM   4740 O  O   . GLN   B 1 299 ? 10.920  8.591   -17.138 1.00 61.83  ? 299 GLN   B O   1 
ATOM   4741 C  CB  . GLN   B 1 299 ? 7.936   7.927   -15.964 1.00 38.97  ? 299 GLN   B CB  1 
ATOM   4742 C  CG  . GLN   B 1 299 ? 8.059   7.045   -17.199 1.00 34.14  ? 299 GLN   B CG  1 
ATOM   4743 C  CD  . GLN   B 1 299 ? 6.783   6.365   -17.639 1.00 31.30  ? 299 GLN   B CD  1 
ATOM   4744 O  OE1 . GLN   B 1 299 ? 6.627   6.008   -18.812 1.00 34.06  ? 299 GLN   B OE1 1 
ATOM   4745 N  NE2 . GLN   B 1 299 ? 5.832   6.207   -16.739 1.00 27.58  ? 299 GLN   B NE2 1 
ATOM   4746 N  N   . CYS   B 1 300 ? 9.917   10.509  -16.447 1.00 55.43  ? 300 CYS   B N   1 
ATOM   4747 C  CA  . CYS   B 1 300 ? 10.420  11.400  -17.485 1.00 52.75  ? 300 CYS   B CA  1 
ATOM   4748 C  C   . CYS   B 1 300 ? 11.801  11.982  -17.149 1.00 67.35  ? 300 CYS   B C   1 
ATOM   4749 O  O   . CYS   B 1 300 ? 12.416  12.591  -18.025 1.00 73.03  ? 300 CYS   B O   1 
ATOM   4750 C  CB  . CYS   B 1 300 ? 9.472   12.571  -17.703 1.00 46.26  ? 300 CYS   B CB  1 
ATOM   4751 S  SG  . CYS   B 1 300 ? 7.926   12.133  -18.542 1.00 56.27  ? 300 CYS   B SG  1 
ATOM   4752 N  N   . SER   B 1 301 ? 12.268  11.815  -15.894 1.00 75.91  ? 301 SER   B N   1 
ATOM   4753 C  CA  . SER   B 1 301 ? 13.568  12.293  -15.427 1.00 74.70  ? 301 SER   B CA  1 
ATOM   4754 C  C   . SER   B 1 301 ? 14.080  11.390  -14.291 1.00 70.45  ? 301 SER   B C   1 
ATOM   4755 O  O   . SER   B 1 301 ? 14.773  10.393  -14.601 1.00 63.38  ? 301 SER   B O   1 
ATOM   4756 C  CB  . SER   B 1 301 ? 13.509  13.733  -14.954 1.00 78.57  ? 301 SER   B CB  1 
ATOM   4757 O  OG  . SER   B 1 301 ? 12.896  14.589  -15.911 1.00 82.95  ? 301 SER   B OG  1 
HETATM 4758 CL CL  . CL    C 2 .   ? 5.682   -15.152 -31.578 1.00 32.96  ? 401 CL    A CL  1 
HETATM 4759 S  S   . DMS   D 3 .   ? -0.446  -11.814 -18.183 1.00 49.50  ? 402 DMS   A S   1 
HETATM 4760 O  O   . DMS   D 3 .   ? 0.391   -11.395 -19.370 1.00 54.05  ? 402 DMS   A O   1 
HETATM 4761 C  C1  . DMS   D 3 .   ? 0.632   -11.691 -16.773 1.00 46.70  ? 402 DMS   A C1  1 
HETATM 4762 C  C2  . DMS   D 3 .   ? -0.603  -13.591 -18.219 1.00 48.43  ? 402 DMS   A C2  1 
HETATM 4763 C  C4  C A1BVY E 4 .   ? 22.292  4.245   -29.036 0.38 37.04  ? 403 A1BVY A C4  1 
HETATM 4764 C  C4  D A1BVY E 4 .   ? 22.296  4.248   -29.038 0.38 37.04  ? 403 A1BVY A C4  1 
HETATM 4765 C  C5  C A1BVY E 4 .   ? 23.514  4.844   -29.273 0.38 40.24  ? 403 A1BVY A C5  1 
HETATM 4766 C  C5  D A1BVY E 4 .   ? 23.517  4.846   -29.271 0.38 40.24  ? 403 A1BVY A C5  1 
HETATM 4767 C  C6  C A1BVY E 4 .   ? 24.275  5.295   -28.218 0.38 37.90  ? 403 A1BVY A C6  1 
HETATM 4768 C  C6  D A1BVY E 4 .   ? 24.274  5.300   -28.214 0.38 37.91  ? 403 A1BVY A C6  1 
HETATM 4769 C  C7  C A1BVY E 4 .   ? 23.826  5.147   -26.915 0.38 37.66  ? 403 A1BVY A C7  1 
HETATM 4770 C  C7  D A1BVY E 4 .   ? 23.825  5.151   -26.911 0.38 37.67  ? 403 A1BVY A C7  1 
HETATM 4771 N  N1  C A1BVY E 4 .   ? 21.338  3.652   -23.462 0.38 33.40  ? 403 A1BVY A N1  1 
HETATM 4772 N  N1  D A1BVY E 4 .   ? 21.333  3.647   -23.469 0.38 33.48  ? 403 A1BVY A N1  1 
HETATM 4773 N  N2  C A1BVY E 4 .   ? 21.757  4.932   -23.323 0.38 39.13  ? 403 A1BVY A N2  1 
HETATM 4774 N  N2  D A1BVY E 4 .   ? 21.752  4.930   -23.328 0.38 39.17  ? 403 A1BVY A N2  1 
HETATM 4775 C  C3  C A1BVY E 4 .   ? 21.822  4.096   -27.741 0.38 34.66  ? 403 A1BVY A C3  1 
HETATM 4776 C  C3  D A1BVY E 4 .   ? 21.828  4.098   -27.743 0.38 34.68  ? 403 A1BVY A C3  1 
HETATM 4777 N  N3  C A1BVY E 4 .   ? 22.235  5.387   -24.436 0.38 37.46  ? 403 A1BVY A N3  1 
HETATM 4778 N  N3  D A1BVY E 4 .   ? 22.234  5.384   -24.437 0.38 37.52  ? 403 A1BVY A N3  1 
HETATM 4779 C  C1  C A1BVY E 4 .   ? 21.571  3.327   -24.704 0.38 34.90  ? 403 A1BVY A C1  1 
HETATM 4780 C  C1  D A1BVY E 4 .   ? 21.574  3.330   -24.724 0.38 35.25  ? 403 A1BVY A C1  1 
HETATM 4781 N  N4  C A1BVY E 4 .   ? 22.139  4.384   -25.334 0.38 34.96  ? 403 A1BVY A N4  1 
HETATM 4782 N  N4  D A1BVY E 4 .   ? 22.135  4.380   -25.342 0.38 35.05  ? 403 A1BVY A N4  1 
HETATM 4783 C  C2  C A1BVY E 4 .   ? 22.599  4.550   -26.688 0.38 36.86  ? 403 A1BVY A C2  1 
HETATM 4784 C  C2  D A1BVY E 4 .   ? 22.599  4.548   -26.683 0.38 36.88  ? 403 A1BVY A C2  1 
HETATM 4785 CL CL  . CL    F 2 .   ? -14.879 8.806   -39.043 1.00 42.12  ? 404 CL    A CL  1 
HETATM 4786 S  S   . DMS   G 3 .   ? 6.573   4.431   -11.180 1.00 49.88  ? 501 DMS   B S   1 
HETATM 4787 O  O   . DMS   G 3 .   ? 7.048   3.009   -11.405 1.00 53.90  ? 501 DMS   B O   1 
HETATM 4788 C  C1  . DMS   G 3 .   ? 4.871   4.313   -10.696 1.00 47.45  ? 501 DMS   B C1  1 
HETATM 4789 C  C2  . DMS   G 3 .   ? 6.369   5.226   -12.761 1.00 52.67  ? 501 DMS   B C2  1 
HETATM 4790 S  S   . DMS   H 3 .   ? -13.317 -10.792 -7.006  1.00 61.83  ? 502 DMS   B S   1 
HETATM 4791 O  O   . DMS   H 3 .   ? -12.481 -9.555  -6.933  1.00 58.20  ? 502 DMS   B O   1 
HETATM 4792 C  C1  . DMS   H 3 .   ? -12.863 -11.828 -5.628  1.00 54.64  ? 502 DMS   B C1  1 
HETATM 4793 C  C2  . DMS   H 3 .   ? -12.634 -11.777 -8.286  1.00 59.28  ? 502 DMS   B C2  1 
HETATM 4794 O  O   . HOH   I 5 .   ? 12.607  1.043   -41.792 1.00 46.40  ? 501 HOH   A O   1 
HETATM 4795 O  O   . HOH   I 5 .   ? -22.009 -9.167  -36.879 1.00 36.46  ? 502 HOH   A O   1 
HETATM 4796 O  O   . HOH   I 5 .   ? 12.412  3.729   -18.428 1.00 28.88  ? 503 HOH   A O   1 
HETATM 4797 O  O   . HOH   I 5 .   ? -18.248 -10.340 -51.815 1.00 25.16  ? 504 HOH   A O   1 
HETATM 4798 O  O   . HOH   I 5 .   ? -1.001  -15.223 -40.458 1.00 31.49  ? 505 HOH   A O   1 
HETATM 4799 O  O   . HOH   I 5 .   ? -15.543 5.227   -43.780 1.00 34.47  ? 506 HOH   A O   1 
HETATM 4800 O  O   . HOH   I 5 .   ? 2.887   -11.127 -22.843 1.00 26.95  ? 507 HOH   A O   1 
HETATM 4801 O  O   . HOH   I 5 .   ? -11.818 4.926   -38.210 1.00 31.45  ? 508 HOH   A O   1 
HETATM 4802 O  O   . HOH   I 5 .   ? 4.708   -1.679  -28.696 1.00 18.81  ? 509 HOH   A O   1 
HETATM 4803 O  O   . HOH   I 5 .   ? -17.922 -5.038  -47.416 1.00 30.16  ? 510 HOH   A O   1 
HETATM 4804 O  O   . HOH   I 5 .   ? 30.109  0.724   -42.917 1.00 23.46  ? 511 HOH   A O   1 
HETATM 4805 O  O   . HOH   I 5 .   ? -8.619  1.948   -35.263 1.00 37.63  ? 512 HOH   A O   1 
HETATM 4806 O  O   . HOH   I 5 .   ? 9.055   -13.314 -11.409 1.00 25.74  ? 513 HOH   A O   1 
HETATM 4807 O  O   . HOH   I 5 .   ? 5.118   -7.205  -40.339 1.00 33.71  ? 514 HOH   A O   1 
HETATM 4808 O  O   . HOH   I 5 .   ? -15.659 0.867   -42.526 1.00 36.47  ? 515 HOH   A O   1 
HETATM 4809 O  O   . HOH   I 5 .   ? -1.060  -11.603 -32.211 1.00 30.91  ? 516 HOH   A O   1 
HETATM 4810 O  O   . HOH   I 5 .   ? -5.735  -5.916  -28.466 1.00 28.19  ? 517 HOH   A O   1 
HETATM 4811 O  O   . HOH   I 5 .   ? 15.954  -5.571  -17.846 1.00 27.38  ? 518 HOH   A O   1 
HETATM 4812 O  O   . HOH   I 5 .   ? -15.881 -11.806 -51.293 1.00 30.02  ? 519 HOH   A O   1 
HETATM 4813 O  O   . HOH   I 5 .   ? -19.118 -6.263  -49.570 1.00 24.12  ? 520 HOH   A O   1 
HETATM 4814 O  O   . HOH   I 5 .   ? -20.406 -4.642  -41.128 1.00 32.41  ? 521 HOH   A O   1 
HETATM 4815 O  O   . HOH   I 5 .   ? -8.903  -1.770  -22.993 1.00 29.70  ? 522 HOH   A O   1 
HETATM 4816 O  O   . HOH   I 5 .   ? -9.408  3.258   -32.868 1.00 36.98  ? 523 HOH   A O   1 
HETATM 4817 O  O   . HOH   I 5 .   ? 23.069  -15.958 -27.331 1.00 33.35  ? 524 HOH   A O   1 
HETATM 4818 O  O   . HOH   I 5 .   ? 21.685  -5.564  -38.055 1.00 26.54  ? 525 HOH   A O   1 
HETATM 4819 O  O   . HOH   I 5 .   ? 26.898  -2.120  -37.528 1.00 24.53  ? 526 HOH   A O   1 
HETATM 4820 O  O   . HOH   I 5 .   ? -22.009 -9.646  -23.441 1.00 40.23  ? 527 HOH   A O   1 
HETATM 4821 O  O   . HOH   I 5 .   ? 13.888  -3.516  -33.583 1.00 20.09  ? 528 HOH   A O   1 
HETATM 4822 O  O   . HOH   I 5 .   ? -19.015 -9.389  -47.533 1.00 26.40  ? 529 HOH   A O   1 
HETATM 4823 O  O   . HOH   I 5 .   ? 25.067  -3.093  -30.237 1.00 23.30  ? 530 HOH   A O   1 
HETATM 4824 O  O   . HOH   I 5 .   ? 11.734  6.413   -37.226 1.00 33.38  ? 531 HOH   A O   1 
HETATM 4825 O  O   . HOH   I 5 .   ? 19.330  -6.204  -10.167 1.00 45.78  ? 532 HOH   A O   1 
HETATM 4826 O  O   . HOH   I 5 .   ? 21.173  -7.977  -36.765 1.00 27.74  ? 533 HOH   A O   1 
HETATM 4827 O  O   . HOH   I 5 .   ? 15.727  -14.399 -27.931 1.00 28.98  ? 534 HOH   A O   1 
HETATM 4828 O  O   . HOH   I 5 .   ? -1.711  -7.809  -20.603 1.00 26.21  ? 535 HOH   A O   1 
HETATM 4829 O  O   . HOH   I 5 .   ? 33.136  -6.739  -37.546 1.00 37.17  ? 536 HOH   A O   1 
HETATM 4830 O  O   . HOH   I 5 .   ? -0.610  -7.579  -23.275 1.00 29.54  ? 537 HOH   A O   1 
HETATM 4831 O  O   . HOH   I 5 .   ? 36.405  0.555   -36.241 1.00 28.01  ? 538 HOH   A O   1 
HETATM 4832 O  O   . HOH   I 5 .   ? -8.596  5.928   -25.294 1.00 28.11  ? 539 HOH   A O   1 
HETATM 4833 O  O   . HOH   I 5 .   ? 23.814  -4.299  -37.343 1.00 25.29  ? 540 HOH   A O   1 
HETATM 4834 O  O   . HOH   I 5 .   ? -3.772  -9.214  -38.013 1.00 20.61  ? 541 HOH   A O   1 
HETATM 4835 O  O   . HOH   I 5 .   ? -20.062 -7.666  -45.859 1.00 32.80  ? 542 HOH   A O   1 
HETATM 4836 O  O   . HOH   I 5 .   ? 31.517  -4.713  -37.843 1.00 34.36  ? 543 HOH   A O   1 
HETATM 4837 O  O   . HOH   I 5 .   ? 16.937  2.604   -11.396 1.00 39.09  ? 544 HOH   A O   1 
HETATM 4838 O  O   . HOH   I 5 .   ? 19.479  5.928   -29.243 1.00 33.87  ? 545 HOH   A O   1 
HETATM 4839 O  O   . HOH   I 5 .   ? -5.009  1.952   -32.793 1.00 44.39  ? 546 HOH   A O   1 
HETATM 4840 O  O   . HOH   I 5 .   ? 16.459  -16.452 -29.998 1.00 35.19  ? 547 HOH   A O   1 
HETATM 4841 O  O   . HOH   I 5 .   ? -1.143  -8.914  -37.685 1.00 37.40  ? 548 HOH   A O   1 
HETATM 4842 O  O   . HOH   J 5 .   ? -10.077 10.334  -32.017 1.00 42.90  ? 601 HOH   B O   1 
HETATM 4843 O  O   . HOH   J 5 .   ? 1.232   -0.156  -19.174 1.00 36.42  ? 602 HOH   B O   1 
HETATM 4844 O  O   . HOH   J 5 .   ? 2.090   27.056  -12.932 1.00 28.57  ? 603 HOH   B O   1 
HETATM 4845 O  O   . HOH   J 5 .   ? -18.095 4.728   -3.126  1.00 40.69  ? 604 HOH   B O   1 
HETATM 4846 O  O   . HOH   J 5 .   ? -3.714  30.254  -28.503 1.00 41.75  ? 605 HOH   B O   1 
HETATM 4847 O  O   . HOH   J 5 .   ? -3.822  2.795   -13.533 1.00 26.68  ? 606 HOH   B O   1 
HETATM 4848 O  O   . HOH   J 5 .   ? -10.281 -18.825 18.505  1.00 41.79  ? 607 HOH   B O   1 
HETATM 4849 O  O   . HOH   J 5 .   ? -3.188  11.190  -15.248 1.00 21.86  ? 608 HOH   B O   1 
HETATM 4850 O  O   . HOH   J 5 .   ? -8.153  2.543   -10.260 1.00 26.61  ? 609 HOH   B O   1 
HETATM 4851 O  O   . HOH   J 5 .   ? -0.074  -9.903  -3.830  1.00 37.52  ? 610 HOH   B O   1 
HETATM 4852 O  O   . HOH   J 5 .   ? 2.761   8.579   -7.153  1.00 31.62  ? 611 HOH   B O   1 
HETATM 4853 O  O   . HOH   J 5 .   ? -12.741 -7.095  14.012  1.00 27.55  ? 612 HOH   B O   1 
HETATM 4854 O  O   . HOH   J 5 .   ? 0.991   5.370   -12.265 1.00 24.83  ? 613 HOH   B O   1 
HETATM 4855 O  O   . HOH   J 5 .   ? -25.851 -6.296  6.511   1.00 50.15  ? 614 HOH   B O   1 
HETATM 4856 O  O   . HOH   J 5 .   ? 11.183  -5.586  -6.147  1.00 34.16  ? 615 HOH   B O   1 
HETATM 4857 O  O   . HOH   J 5 .   ? -7.747  7.336   2.650   1.00 37.26  ? 616 HOH   B O   1 
HETATM 4858 O  O   . HOH   J 5 .   ? -12.046 -0.064  -1.277  1.00 22.18  ? 617 HOH   B O   1 
HETATM 4859 O  O   . HOH   J 5 .   ? 14.447  10.941  -24.119 1.00 38.92  ? 618 HOH   B O   1 
HETATM 4860 O  O   . HOH   J 5 .   ? -1.639  -0.492  5.414   1.00 28.96  ? 619 HOH   B O   1 
HETATM 4861 O  O   . HOH   J 5 .   ? 2.804   4.483   -7.664  1.00 27.63  ? 620 HOH   B O   1 
HETATM 4862 O  O   . HOH   J 5 .   ? -19.405 -7.685  8.082   1.00 29.02  ? 621 HOH   B O   1 
HETATM 4863 O  O   . HOH   J 5 .   ? 0.718   2.813   -21.051 1.00 30.10  ? 622 HOH   B O   1 
HETATM 4864 O  O   . HOH   J 5 .   ? -12.475 5.593   3.454   1.00 28.78  ? 623 HOH   B O   1 
HETATM 4865 O  O   . HOH   J 5 .   ? -12.871 -9.960  5.381   1.00 23.70  ? 624 HOH   B O   1 
HETATM 4866 O  O   . HOH   J 5 .   ? 1.206   7.308   -4.860  1.00 30.51  ? 625 HOH   B O   1 
HETATM 4867 O  O   . HOH   J 5 .   ? -12.304 14.181  -29.969 1.00 30.64  ? 626 HOH   B O   1 
HETATM 4868 O  O   . HOH   J 5 .   ? 10.988  -4.069  7.961   1.00 26.09  ? 627 HOH   B O   1 
HETATM 4869 O  O   . HOH   J 5 .   ? -16.031 9.459   -1.450  1.00 32.84  ? 628 HOH   B O   1 
HETATM 4870 O  O   . HOH   J 5 .   ? -8.882  5.616   -18.640 1.00 39.97  ? 629 HOH   B O   1 
HETATM 4871 O  O   . HOH   J 5 .   ? -10.243 7.032   4.052   1.00 33.37  ? 630 HOH   B O   1 
HETATM 4872 O  O   . HOH   J 5 .   ? -16.269 2.946   -9.235  1.00 29.76  ? 631 HOH   B O   1 
HETATM 4873 O  O   . HOH   J 5 .   ? -11.130 -14.598 -3.740  1.00 35.78  ? 632 HOH   B O   1 
HETATM 4874 O  O   . HOH   J 5 .   ? -16.577 -4.314  7.621   1.00 31.20  ? 633 HOH   B O   1 
HETATM 4875 O  O   . HOH   J 5 .   ? 3.094   4.730   -14.054 1.00 20.73  ? 634 HOH   B O   1 
HETATM 4876 O  O   . HOH   J 5 .   ? 4.601   7.457   -25.811 1.00 35.17  ? 635 HOH   B O   1 
HETATM 4877 O  O   . HOH   J 5 .   ? -1.781  1.156   7.676   1.00 34.31  ? 636 HOH   B O   1 
# 
