data_7I1C
# 
_entry.id   7I1C 
# 
_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   7I1C         pdb_00007i1c 10.2210/pdb7i1c/pdb 
WWPDB D_1001408191 ?            ?                   
# 
_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                        7I1C 
_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           Y 
_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 '[2-(morpholin-4-yl)-1,3-thiazol-5-yl]methanol' 200.258   1  ?         ? ? ? 
4 water       nat water                                           18.015    82 ?         ? ? ? 
# 
_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 '[2-(morpholin-4-yl)-1,3-thiazol-5-yl]methanol' RA7 
4 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 
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 
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 
RA7 non-polymer         . '[2-(morpholin-4-yl)-1,3-thiazol-5-yl]methanol' ? 'C8 H12 N2 O2 S' 200.258 
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 ALA 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        RA7 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   RA7 
_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 RA7 1  402 501 RA7 LIG A . 
E 2 CL  1  401 1   CL  CL  B . 
F 4 HOH 1  501 62  HOH HOH A . 
F 4 HOH 2  502 27  HOH HOH A . 
F 4 HOH 3  503 45  HOH HOH A . 
F 4 HOH 4  504 57  HOH HOH A . 
F 4 HOH 5  505 28  HOH HOH A . 
F 4 HOH 6  506 53  HOH HOH A . 
F 4 HOH 7  507 2   HOH HOH A . 
F 4 HOH 8  508 41  HOH HOH A . 
F 4 HOH 9  509 67  HOH HOH A . 
F 4 HOH 10 510 26  HOH HOH A . 
F 4 HOH 11 511 51  HOH HOH A . 
F 4 HOH 12 512 46  HOH HOH A . 
F 4 HOH 13 513 7   HOH HOH A . 
F 4 HOH 14 514 43  HOH HOH A . 
F 4 HOH 15 515 6   HOH HOH A . 
F 4 HOH 16 516 44  HOH HOH A . 
F 4 HOH 17 517 35  HOH HOH A . 
F 4 HOH 18 518 64  HOH HOH A . 
F 4 HOH 19 519 50  HOH HOH A . 
F 4 HOH 20 520 48  HOH HOH A . 
F 4 HOH 21 521 34  HOH HOH A . 
F 4 HOH 22 522 4   HOH HOH A . 
F 4 HOH 23 523 12  HOH HOH A . 
F 4 HOH 24 524 15  HOH HOH A . 
F 4 HOH 25 525 63  HOH HOH A . 
F 4 HOH 26 526 36  HOH HOH A . 
F 4 HOH 27 527 29  HOH HOH A . 
F 4 HOH 28 528 59  HOH HOH A . 
F 4 HOH 29 529 8   HOH HOH A . 
F 4 HOH 30 530 39  HOH HOH A . 
F 4 HOH 31 531 3   HOH HOH A . 
F 4 HOH 32 532 30  HOH HOH A . 
F 4 HOH 33 533 65  HOH HOH A . 
F 4 HOH 34 534 77  HOH HOH A . 
F 4 HOH 35 535 40  HOH HOH A . 
F 4 HOH 36 536 16  HOH HOH A . 
F 4 HOH 37 537 10  HOH HOH A . 
F 4 HOH 38 538 17  HOH HOH A . 
F 4 HOH 39 539 66  HOH HOH A . 
F 4 HOH 40 540 25  HOH HOH A . 
F 4 HOH 41 541 82  HOH HOH A . 
F 4 HOH 42 542 22  HOH HOH A . 
F 4 HOH 43 543 11  HOH HOH A . 
F 4 HOH 44 544 18  HOH HOH A . 
F 4 HOH 45 545 47  HOH HOH A . 
F 4 HOH 46 546 81  HOH HOH A . 
F 4 HOH 47 547 49  HOH HOH A . 
F 4 HOH 48 548 54  HOH HOH A . 
F 4 HOH 49 549 69  HOH HOH A . 
F 4 HOH 50 550 75  HOH HOH A . 
F 4 HOH 51 551 21  HOH HOH A . 
F 4 HOH 52 552 23  HOH HOH A . 
F 4 HOH 53 553 60  HOH HOH A . 
F 4 HOH 54 554 74  HOH HOH A . 
F 4 HOH 55 555 37  HOH HOH A . 
F 4 HOH 56 556 68  HOH HOH A . 
G 4 HOH 1  501 33  HOH HOH B . 
G 4 HOH 2  502 61  HOH HOH B . 
G 4 HOH 3  503 56  HOH HOH B . 
G 4 HOH 4  504 42  HOH HOH B . 
G 4 HOH 5  505 32  HOH HOH B . 
G 4 HOH 6  506 5   HOH HOH B . 
G 4 HOH 7  507 83  HOH HOH B . 
G 4 HOH 8  508 71  HOH HOH B . 
G 4 HOH 9  509 24  HOH HOH B . 
G 4 HOH 10 510 80  HOH HOH B . 
G 4 HOH 11 511 14  HOH HOH B . 
G 4 HOH 12 512 9   HOH HOH B . 
G 4 HOH 13 513 70  HOH HOH B . 
G 4 HOH 14 514 52  HOH HOH B . 
G 4 HOH 15 515 13  HOH HOH B . 
G 4 HOH 16 516 72  HOH HOH B . 
G 4 HOH 17 517 79  HOH HOH B . 
G 4 HOH 18 518 76  HOH HOH B . 
G 4 HOH 19 519 19  HOH HOH B . 
G 4 HOH 20 520 31  HOH HOH B . 
G 4 HOH 21 521 20  HOH HOH B . 
G 4 HOH 22 522 55  HOH HOH B . 
G 4 HOH 23 523 58  HOH HOH B . 
G 4 HOH 24 524 38  HOH HOH B . 
G 4 HOH 25 525 78  HOH HOH B . 
G 4 HOH 26 526 73  HOH HOH B . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     SER 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      1 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     OG 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    B 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    SER 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     1 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    OG 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC 5.8.0238 ? 1 
'data scaling'   XDS    .        ? 2 
'data reduction' XDS    .        ? 3 
phasing          PHASER .        ? 4 
# 
_cell.entry_id           7I1C 
_cell.length_a           68.110 
_cell.length_b           99.560 
_cell.length_c           103.940 
_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                         7I1C 
_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          7I1C 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.61 
_exptl_crystal.density_percent_sol   52.85 
_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                     7I1C 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             46.07 
_reflns.d_resolution_high            1.95 
_reflns.number_obs                   51844 
_reflns.percent_possible_obs         99.6 
_reflns.pdbx_Rmerge_I_obs            0.126 
_reflns.pdbx_netI_over_sigmaI        10.06 
_reflns.pdbx_Rrim_I_all              0.138 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     307284 
_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 1.95 2.07 49781 8268 1.364                99.6 1.21  1.4909999999999999  0.45899999999999996 ? ? ? ? 
1 2 2.07 2.21 47645 7803 0.835                99.7 2.08  0.912               0.716               ? ? ? ? 
1 3 2.21 2.39 43673 7264 0.52                 99.8 3.25  0.569               0.863               ? ? ? ? 
1 4 2.39 2.62 37988 6700 0.313                99.4 5.11  0.345               0.9440000000000001  ? ? ? ? 
1 5 2.62 2.93 37729 6086 0.191                99.9 8.62  0.20800000000000002 0.983               ? ? ? ? 
1 6 2.93 3.38 32417 5429 0.109                99.7 14.95 0.11900000000000001 0.993               ? ? ? ? 
1 7 3.38 4.13 25492 4582 0.062                99.0 24.27 0.068               0.997               ? ? ? ? 
1 8 4.13 5.82 21240 3623 0.044000000000000004 99.6 33.18 0.049               0.998               ? ? ? ? 
1 9 5.82 ?    11319 2089 0.035                97.5 34.70 0.039               0.998               ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7I1C 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     49743 
_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                             46.07 
_refine.ls_d_res_high                            1.95 
_refine.ls_percent_reflns_obs                    99.52 
_refine.ls_R_factor_obs                          0.22433 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.22307 
_refine.ls_R_factor_R_free                       0.25354 
_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                  2101 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.949 
_refine.correlation_coeff_Fo_to_Fc_free          0.935 
_refine.B_iso_mean                               35.047 
_refine.aniso_B[1][1]                            -1.23 
_refine.aniso_B[2][2]                            0.84 
_refine.aniso_B[3][3]                            0.39 
_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                       0.184 
_refine.pdbx_overall_ESU_R_Free                  0.161 
_refine.overall_SU_ML                            0.159 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             6.001 
_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                         LAST 
_refine_hist.pdbx_number_atoms_protein        4657 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         15 
_refine_hist.number_atoms_solvent             82 
_refine_hist.number_atoms_total               4754 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        46.07 
# 
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             0.008  0.013  ? 5356  'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.004  0.017  ? 4707  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.543  1.640  ? 7017  'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.332  1.575  ? 10597 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.713  5.000  ? 666   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       37.064 23.320 ? 256   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.427 15.000 ? 816   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       17.761 15.000 ? 22    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.071  0.200  ? 659   'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 5951  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 1091  '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                  2.866  3.576  ? 2696  'X-RAY DIFFRACTION' ? 
r_mcbond_other               2.868  3.576  ? 2692  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.346  5.376  ? 3280  'X-RAY DIFFRACTION' ? 
r_mcangle_other              4.345  5.377  ? 3281  'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.444  3.900  ? 2660  'X-RAY DIFFRACTION' ? 
r_scbond_other               3.444  3.900  ? 2660  'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_other              5.475  5.768  ? 3738  'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       7.370  41.904 ? 5374  'X-RAY DIFFRACTION' ? 
r_long_range_B_other         7.371  41.899 ? 5362  '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                       1.952 
_refine_ls_shell.d_res_low                        2.003 
_refine_ls_shell.number_reflns_R_work             3627 
_refine_ls_shell.R_factor_R_work                  0.340 
_refine_ls_shell.percent_reflns_obs               99.16 
_refine_ls_shell.R_factor_R_free                  0.369 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             154 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7I1C 
_struct.title                     
;PanDDA analysis group deposition -- Main Protease (SARS-CoV-2) in complex with fragment E11 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        7I1C 
_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 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_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 7I1C A 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
2 1 7I1C 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)' 2820  ? 
1 MORE         -25   ? 
1 'SSA (A^2)'  25760 ? 
# 
_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 
# 
_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  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
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 ? GLY A 258 ? THR A 243 GLY A 258 1 ? 16 
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
HELX_P HELX_P12 AB3 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P13 AB4 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P14 AB5 GLU B 47  ? ASN B 51  ? GLU B 47  ASN B 51  5 ? 5  
HELX_P HELX_P15 AB6 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P16 AB7 SER B 62  ? PHE B 66  ? SER B 62  PHE B 66  5 ? 5  
HELX_P HELX_P17 AB8 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P18 AB9 THR B 226 ? TYR B 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P19 AC1 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P20 AC2 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P21 AC3 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P22 AC4 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 PHE A 66  ? ALA A 70  ? PHE A 66  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 LYS A 100 ? PHE A 103 ? LYS A 100 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 LYS A 100 ? PHE A 103 ? LYS A 100 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 LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
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 VAL A 86  ? O VAL A 86  N GLN A 83  ? N GLN A 83  
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                   7I1C 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    62 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   NE2 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HIS 
_pdbx_validate_close_contact.auth_seq_id_2    64 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 5   ? ? -64.15  93.04   
2  1 ASP A 33  ? ? 50.06   -127.89 
3  1 ASN A 84  ? ? 53.93   -119.02 
4  1 LEU A 282 ? ? 38.61   42.89   
5  1 CYS A 300 ? ? -108.39 -139.78 
6  1 ASP B 33  ? ? 42.79   -128.35 
7  1 ASN B 51  ? ? -154.29 68.96   
8  1 ASN B 84  ? ? 53.16   -124.58 
9  1 TYR B 118 ? ? -166.77 98.07   
10 1 TYR B 154 ? ? 62.52   -109.99 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
RA7 C4   C  N N 291 
RA7 C5   C  N N 292 
RA7 C6   C  N N 293 
RA7 N1   N  N N 294 
RA7 C7   C  N N 295 
RA7 O1   O  N N 296 
RA7 C1   C  Y N 297 
RA7 S    S  Y N 298 
RA7 C2   C  Y N 299 
RA7 N    N  Y N 300 
RA7 C    C  Y N 301 
RA7 O    O  N N 302 
RA7 C3   C  N N 303 
RA7 H1   H  N N 304 
RA7 H2   H  N N 305 
RA7 H3   H  N N 306 
RA7 H4   H  N N 307 
RA7 H5   H  N N 308 
RA7 H6   H  N N 309 
RA7 H7   H  N N 310 
RA7 H8   H  N N 311 
RA7 H9   H  N N 312 
RA7 H10  H  N N 313 
RA7 H11  H  N N 314 
RA7 H12  H  N N 315 
SER N    N  N N 316 
SER CA   C  N S 317 
SER C    C  N N 318 
SER O    O  N N 319 
SER CB   C  N N 320 
SER OG   O  N N 321 
SER OXT  O  N N 322 
SER H    H  N N 323 
SER H2   H  N N 324 
SER HA   H  N N 325 
SER HB2  H  N N 326 
SER HB3  H  N N 327 
SER HG   H  N N 328 
SER HXT  H  N N 329 
THR N    N  N N 330 
THR CA   C  N S 331 
THR C    C  N N 332 
THR O    O  N N 333 
THR CB   C  N R 334 
THR OG1  O  N N 335 
THR CG2  C  N N 336 
THR OXT  O  N N 337 
THR H    H  N N 338 
THR H2   H  N N 339 
THR HA   H  N N 340 
THR HB   H  N N 341 
THR HG1  H  N N 342 
THR HG21 H  N N 343 
THR HG22 H  N N 344 
THR HG23 H  N N 345 
THR HXT  H  N N 346 
TRP N    N  N N 347 
TRP CA   C  N S 348 
TRP C    C  N N 349 
TRP O    O  N N 350 
TRP CB   C  N N 351 
TRP CG   C  Y N 352 
TRP CD1  C  Y N 353 
TRP CD2  C  Y N 354 
TRP NE1  N  Y N 355 
TRP CE2  C  Y N 356 
TRP CE3  C  Y N 357 
TRP CZ2  C  Y N 358 
TRP CZ3  C  Y N 359 
TRP CH2  C  Y N 360 
TRP OXT  O  N N 361 
TRP H    H  N N 362 
TRP H2   H  N N 363 
TRP HA   H  N N 364 
TRP HB2  H  N N 365 
TRP HB3  H  N N 366 
TRP HD1  H  N N 367 
TRP HE1  H  N N 368 
TRP HE3  H  N N 369 
TRP HZ2  H  N N 370 
TRP HZ3  H  N N 371 
TRP HH2  H  N N 372 
TRP HXT  H  N N 373 
TYR N    N  N N 374 
TYR CA   C  N S 375 
TYR C    C  N N 376 
TYR O    O  N N 377 
TYR CB   C  N N 378 
TYR CG   C  Y N 379 
TYR CD1  C  Y N 380 
TYR CD2  C  Y N 381 
TYR CE1  C  Y N 382 
TYR CE2  C  Y N 383 
TYR CZ   C  Y N 384 
TYR OH   O  N N 385 
TYR OXT  O  N N 386 
TYR H    H  N N 387 
TYR H2   H  N N 388 
TYR HA   H  N N 389 
TYR HB2  H  N N 390 
TYR HB3  H  N N 391 
TYR HD1  H  N N 392 
TYR HD2  H  N N 393 
TYR HE1  H  N N 394 
TYR HE2  H  N N 395 
TYR HH   H  N N 396 
TYR HXT  H  N N 397 
VAL N    N  N N 398 
VAL CA   C  N S 399 
VAL C    C  N N 400 
VAL O    O  N N 401 
VAL CB   C  N N 402 
VAL CG1  C  N N 403 
VAL CG2  C  N N 404 
VAL OXT  O  N N 405 
VAL H    H  N N 406 
VAL H2   H  N N 407 
VAL HA   H  N N 408 
VAL HB   H  N N 409 
VAL HG11 H  N N 410 
VAL HG12 H  N N 411 
VAL HG13 H  N N 412 
VAL HG21 H  N N 413 
VAL HG22 H  N N 414 
VAL HG23 H  N N 415 
VAL HXT  H  N N 416 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
RA7 O   C5   sing N N 277 
RA7 O   C4   sing N N 278 
RA7 C5  C6   sing N N 279 
RA7 C4  C3   sing N N 280 
RA7 C6  N1   sing N N 281 
RA7 C3  N1   sing N N 282 
RA7 N1  C2   sing N N 283 
RA7 C2  S    sing Y N 284 
RA7 C2  N    doub Y N 285 
RA7 S   C1   sing Y N 286 
RA7 N   C    sing Y N 287 
RA7 C1  C    doub Y N 288 
RA7 C1  C7   sing N N 289 
RA7 O1  C7   sing N N 290 
RA7 C4  H1   sing N N 291 
RA7 C4  H2   sing N N 292 
RA7 C5  H3   sing N N 293 
RA7 C5  H4   sing N N 294 
RA7 C6  H5   sing N N 295 
RA7 C6  H6   sing N N 296 
RA7 C7  H7   sing N N 297 
RA7 C7  H8   sing N N 298 
RA7 O1  H9   sing N N 299 
RA7 C   H10  sing N N 300 
RA7 C3  H11  sing N N 301 
RA7 C3  H12  sing N N 302 
SER N   CA   sing N N 303 
SER N   H    sing N N 304 
SER N   H2   sing N N 305 
SER CA  C    sing N N 306 
SER CA  CB   sing N N 307 
SER CA  HA   sing N N 308 
SER C   O    doub N N 309 
SER C   OXT  sing N N 310 
SER CB  OG   sing N N 311 
SER CB  HB2  sing N N 312 
SER CB  HB3  sing N N 313 
SER OG  HG   sing N N 314 
SER OXT HXT  sing N N 315 
THR N   CA   sing N N 316 
THR N   H    sing N N 317 
THR N   H2   sing N N 318 
THR CA  C    sing N N 319 
THR CA  CB   sing N N 320 
THR CA  HA   sing N N 321 
THR C   O    doub N N 322 
THR C   OXT  sing N N 323 
THR CB  OG1  sing N N 324 
THR CB  CG2  sing N N 325 
THR CB  HB   sing N N 326 
THR OG1 HG1  sing N N 327 
THR CG2 HG21 sing N N 328 
THR CG2 HG22 sing N N 329 
THR CG2 HG23 sing N N 330 
THR OXT HXT  sing N N 331 
TRP N   CA   sing N N 332 
TRP N   H    sing N N 333 
TRP N   H2   sing N N 334 
TRP CA  C    sing N N 335 
TRP CA  CB   sing N N 336 
TRP CA  HA   sing N N 337 
TRP C   O    doub N N 338 
TRP C   OXT  sing N N 339 
TRP CB  CG   sing N N 340 
TRP CB  HB2  sing N N 341 
TRP CB  HB3  sing N N 342 
TRP CG  CD1  doub Y N 343 
TRP CG  CD2  sing Y N 344 
TRP CD1 NE1  sing Y N 345 
TRP CD1 HD1  sing N N 346 
TRP CD2 CE2  doub Y N 347 
TRP CD2 CE3  sing Y N 348 
TRP NE1 CE2  sing Y N 349 
TRP NE1 HE1  sing N N 350 
TRP CE2 CZ2  sing Y N 351 
TRP CE3 CZ3  doub Y N 352 
TRP CE3 HE3  sing N N 353 
TRP CZ2 CH2  doub Y N 354 
TRP CZ2 HZ2  sing N N 355 
TRP CZ3 CH2  sing Y N 356 
TRP CZ3 HZ3  sing N N 357 
TRP CH2 HH2  sing N N 358 
TRP OXT HXT  sing N N 359 
TYR N   CA   sing N N 360 
TYR N   H    sing N N 361 
TYR N   H2   sing N N 362 
TYR CA  C    sing N N 363 
TYR CA  CB   sing N N 364 
TYR CA  HA   sing N N 365 
TYR C   O    doub N N 366 
TYR C   OXT  sing N N 367 
TYR CB  CG   sing N N 368 
TYR CB  HB2  sing N N 369 
TYR CB  HB3  sing N N 370 
TYR CG  CD1  doub Y N 371 
TYR CG  CD2  sing Y N 372 
TYR CD1 CE1  sing Y N 373 
TYR CD1 HD1  sing N N 374 
TYR CD2 CE2  doub Y N 375 
TYR CD2 HD2  sing N N 376 
TYR CE1 CZ   doub Y N 377 
TYR CE1 HE1  sing N N 378 
TYR CE2 CZ   sing Y N 379 
TYR CE2 HE2  sing N N 380 
TYR CZ  OH   sing N N 381 
TYR OH  HH   sing N N 382 
TYR OXT HXT  sing N N 383 
VAL N   CA   sing N N 384 
VAL N   H    sing N N 385 
VAL N   H2   sing N N 386 
VAL CA  C    sing N N 387 
VAL CA  CB   sing N N 388 
VAL CA  HA   sing N N 389 
VAL C   O    doub N N 390 
VAL C   OXT  sing N N 391 
VAL CB  CG1  sing N N 392 
VAL CB  CG2  sing N N 393 
VAL CB  HB   sing N N 394 
VAL CG1 HG11 sing N N 395 
VAL CG1 HG12 sing N N 396 
VAL CG1 HG13 sing N N 397 
VAL CG2 HG21 sing N N 398 
VAL CG2 HG22 sing N N 399 
VAL CG2 HG23 sing N N 400 
VAL OXT HXT  sing N N 401 
# 
_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                    7I1C 
_atom_sites.fract_transf_matrix[1][1]   0.014682 
_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]   0.010044 
_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]   0.009621 
_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   ? -13.969 -9.590  -12.408 1.00 58.51  ? 1   SER A N   1 
ATOM   2    C  CA  . SER A 1 1   ? -13.840 -8.893  -13.725 1.00 57.99  ? 1   SER A CA  1 
ATOM   3    C  C   . SER A 1 1   ? -12.826 -7.734  -13.628 1.00 60.96  ? 1   SER A C   1 
ATOM   4    O  O   . SER A 1 1   ? -11.998 -7.719  -12.661 1.00 56.86  ? 1   SER A O   1 
ATOM   5    C  CB  . SER A 1 1   ? -15.209 -8.451  -14.243 1.00 60.68  ? 1   SER A CB  1 
ATOM   6    O  OG  . SER A 1 1   ? -15.716 -7.325  -13.539 1.00 53.02  ? 1   SER A OG  1 
ATOM   7    N  N   . GLY A 1 2   ? -12.887 -6.798  -14.585 1.00 53.93  ? 2   GLY A N   1 
ATOM   8    C  CA  . GLY A 1 2   ? -11.849 -5.788  -14.849 1.00 50.68  ? 2   GLY A CA  1 
ATOM   9    C  C   . GLY A 1 2   ? -10.987 -6.255  -16.005 1.00 50.47  ? 2   GLY A C   1 
ATOM   10   O  O   . GLY A 1 2   ? -10.856 -7.476  -16.188 1.00 53.18  ? 2   GLY A O   1 
ATOM   11   N  N   . PHE A 1 3   ? -10.440 -5.336  -16.797 1.00 46.87  ? 3   PHE A N   1 
ATOM   12   C  CA  . PHE A 1 3   ? -9.473  -5.692  -17.866 1.00 52.52  ? 3   PHE A CA  1 
ATOM   13   C  C   . PHE A 1 3   ? -8.346  -4.659  -17.887 1.00 49.37  ? 3   PHE A C   1 
ATOM   14   O  O   . PHE A 1 3   ? -8.576  -3.474  -18.151 1.00 55.81  ? 3   PHE A O   1 
ATOM   15   C  CB  . PHE A 1 3   ? -10.173 -5.890  -19.213 1.00 51.53  ? 3   PHE A CB  1 
ATOM   16   C  CG  . PHE A 1 3   ? -9.456  -6.889  -20.080 1.00 51.78  ? 3   PHE A CG  1 
ATOM   17   C  CD1 . PHE A 1 3   ? -9.612  -8.249  -19.870 1.00 55.65  ? 3   PHE A CD1 1 
ATOM   18   C  CD2 . PHE A 1 3   ? -8.573  -6.467  -21.060 1.00 50.82  ? 3   PHE A CD2 1 
ATOM   19   C  CE1 . PHE A 1 3   ? -8.912  -9.168  -20.640 1.00 58.77  ? 3   PHE A CE1 1 
ATOM   20   C  CE2 . PHE A 1 3   ? -7.887  -7.383  -21.835 1.00 53.16  ? 3   PHE A CE2 1 
ATOM   21   C  CZ  . PHE A 1 3   ? -8.048  -8.733  -21.620 1.00 56.30  ? 3   PHE A CZ  1 
ATOM   22   N  N   . ARG A 1 4   ? -7.148  -5.140  -17.593 1.00 48.14  ? 4   ARG A N   1 
ATOM   23   C  CA  . ARG A 1 4   ? -5.956  -4.336  -17.258 1.00 43.91  ? 4   ARG A CA  1 
ATOM   24   C  C   . ARG A 1 4   ? -4.787  -4.839  -18.096 1.00 35.03  ? 4   ARG A C   1 
ATOM   25   O  O   . ARG A 1 4   ? -4.650  -6.058  -18.211 1.00 34.05  ? 4   ARG A O   1 
ATOM   26   C  CB  . ARG A 1 4   ? -5.690  -4.508  -15.759 1.00 48.39  ? 4   ARG A CB  1 
ATOM   27   C  CG  . ARG A 1 4   ? -6.479  -3.543  -14.891 1.00 51.95  ? 4   ARG A CG  1 
ATOM   28   C  CD  . ARG A 1 4   ? -5.735  -2.238  -14.934 1.00 56.60  ? 4   ARG A CD  1 
ATOM   29   N  NE  . ARG A 1 4   ? -6.261  -1.249  -14.030 1.00 57.85  ? 4   ARG A NE  1 
ATOM   30   C  CZ  . ARG A 1 4   ? -5.615  -0.139  -13.702 1.00 67.44  ? 4   ARG A CZ  1 
ATOM   31   N  NH1 . ARG A 1 4   ? -4.402  0.086   -14.190 1.00 64.77  ? 4   ARG A NH1 1 
ATOM   32   N  NH2 . ARG A 1 4   ? -6.183  0.730   -12.877 1.00 70.82  ? 4   ARG A NH2 1 
ATOM   33   N  N   . LYS A 1 5   ? -3.996  -3.926  -18.646 1.00 35.00  ? 5   LYS A N   1 
ATOM   34   C  CA  . LYS A 1 5   ? -2.650  -4.213  -19.209 1.00 39.77  ? 5   LYS A CA  1 
ATOM   35   C  C   . LYS A 1 5   ? -1.763  -4.677  -18.053 1.00 38.85  ? 5   LYS A C   1 
ATOM   36   O  O   . LYS A 1 5   ? -1.163  -3.833  -17.371 1.00 41.70  ? 5   LYS A O   1 
ATOM   37   C  CB  . LYS A 1 5   ? -2.005  -2.984  -19.854 1.00 41.47  ? 5   LYS A CB  1 
ATOM   38   C  CG  . LYS A 1 5   ? -2.434  -2.709  -21.279 1.00 51.58  ? 5   LYS A CG  1 
ATOM   39   C  CD  . LYS A 1 5   ? -1.347  -2.860  -22.299 1.00 52.90  ? 5   LYS A CD  1 
ATOM   40   C  CE  . LYS A 1 5   ? -1.740  -2.234  -23.618 1.00 56.37  ? 5   LYS A CE  1 
ATOM   41   N  NZ  . LYS A 1 5   ? -2.038  -0.790  -23.481 1.00 60.74  ? 5   LYS A NZ  1 
ATOM   42   N  N   . MET A 1 6   ? -1.703  -5.977  -17.858 1.00 35.19  ? 6   MET A N   1 
ATOM   43   C  CA  . MET A 1 6   ? -1.038  -6.620  -16.707 1.00 33.83  ? 6   MET A CA  1 
ATOM   44   C  C   . MET A 1 6   ? 0.314   -7.165  -17.189 1.00 29.91  ? 6   MET A C   1 
ATOM   45   O  O   . MET A 1 6   ? 0.354   -7.843  -18.253 1.00 27.96  ? 6   MET A O   1 
ATOM   46   C  CB  . MET A 1 6   ? -1.977  -7.729  -16.255 1.00 36.21  ? 6   MET A CB  1 
ATOM   47   C  CG  . MET A 1 6   ? -1.561  -8.505  -15.069 1.00 47.38  ? 6   MET A CG  1 
ATOM   48   S  SD  . MET A 1 6   ? -2.985  -9.566  -14.635 1.00 54.02  ? 6   MET A SD  1 
ATOM   49   C  CE  . MET A 1 6   ? -4.049  -8.388  -13.825 1.00 42.63  ? 6   MET A CE  1 
ATOM   50   N  N   . ALA A 1 7   ? 1.379   -6.824  -16.476 1.00 24.67  ? 7   ALA A N   1 
ATOM   51   C  CA  . ALA A 1 7   ? 2.750   -7.337  -16.699 1.00 24.97  ? 7   ALA A CA  1 
ATOM   52   C  C   . ALA A 1 7   ? 2.943   -8.580  -15.834 1.00 24.56  ? 7   ALA A C   1 
ATOM   53   O  O   . ALA A 1 7   ? 2.257   -8.704  -14.798 1.00 23.99  ? 7   ALA A O   1 
ATOM   54   C  CB  . ALA A 1 7   ? 3.781   -6.280  -16.370 1.00 22.02  ? 7   ALA A CB  1 
ATOM   55   N  N   . PHE A 1 8   ? 3.866   -9.449  -16.225 1.00 24.36  ? 8   PHE A N   1 
ATOM   56   C  CA  . PHE A 1 8   ? 4.289   -10.610 -15.402 1.00 25.05  ? 8   PHE A CA  1 
ATOM   57   C  C   . PHE A 1 8   ? 5.040   -10.107 -14.185 1.00 22.99  ? 8   PHE A C   1 
ATOM   58   O  O   . PHE A 1 8   ? 5.763   -9.115  -14.254 1.00 21.81  ? 8   PHE A O   1 
ATOM   59   C  CB  . PHE A 1 8   ? 5.161   -11.582 -16.188 1.00 25.87  ? 8   PHE A CB  1 
ATOM   60   C  CG  . PHE A 1 8   ? 4.355   -12.395 -17.168 1.00 27.18  ? 8   PHE A CG  1 
ATOM   61   C  CD1 . PHE A 1 8   ? 3.615   -13.474 -16.729 1.00 28.45  ? 8   PHE A CD1 1 
ATOM   62   C  CD2 . PHE A 1 8   ? 4.336   -12.077 -18.519 1.00 29.18  ? 8   PHE A CD2 1 
ATOM   63   C  CE1 . PHE A 1 8   ? 2.880   -14.237 -17.625 1.00 31.71  ? 8   PHE A CE1 1 
ATOM   64   C  CE2 . PHE A 1 8   ? 3.593   -12.836 -19.418 1.00 27.97  ? 8   PHE A CE2 1 
ATOM   65   C  CZ  . PHE A 1 8   ? 2.858   -13.905 -18.969 1.00 30.46  ? 8   PHE A CZ  1 
ATOM   66   N  N   . PRO A 1 9   ? 4.909   -10.804 -13.034 1.00 23.48  ? 9   PRO A N   1 
ATOM   67   C  CA  . PRO A 1 9   ? 5.736   -10.494 -11.874 1.00 23.56  ? 9   PRO A CA  1 
ATOM   68   C  C   . PRO A 1 9   ? 7.226   -10.519 -12.289 1.00 24.08  ? 9   PRO A C   1 
ATOM   69   O  O   . PRO A 1 9   ? 7.699   -11.490 -12.904 1.00 24.58  ? 9   PRO A O   1 
ATOM   70   C  CB  . PRO A 1 9   ? 5.369   -11.590 -10.863 1.00 24.32  ? 9   PRO A CB  1 
ATOM   71   C  CG  . PRO A 1 9   ? 4.016   -12.104 -11.331 1.00 26.22  ? 9   PRO A CG  1 
ATOM   72   C  CD  . PRO A 1 9   ? 4.016   -11.951 -12.833 1.00 24.59  ? 9   PRO A CD  1 
ATOM   73   N  N   . SER A 1 10  ? 7.943   -9.465  -11.934 1.00 22.18  ? 10  SER A N   1 
ATOM   74   C  CA  . SER A 1 10  ? 9.301   -9.163  -12.421 1.00 21.97  ? 10  SER A CA  1 
ATOM   75   C  C   . SER A 1 10  ? 10.398  -9.815  -11.568 1.00 24.35  ? 10  SER A C   1 
ATOM   76   O  O   . SER A 1 10  ? 11.554  -9.697  -11.995 1.00 24.74  ? 10  SER A O   1 
ATOM   77   C  CB  . SER A 1 10  ? 9.507   -7.684  -12.504 1.00 22.31  ? 10  SER A CB  1 
ATOM   78   O  OG  . SER A 1 10  ? 9.342   -7.073  -11.229 1.00 23.75  ? 10  SER A OG  1 
ATOM   79   N  N   . GLY A 1 11  ? 10.094  -10.407 -10.405 1.00 22.76  ? 11  GLY A N   1 
ATOM   80   C  CA  . GLY A 1 11  ? 11.128  -10.909 -9.459  1.00 24.28  ? 11  GLY A CA  1 
ATOM   81   C  C   . GLY A 1 11  ? 12.177  -11.824 -10.110 1.00 24.10  ? 11  GLY A C   1 
ATOM   82   O  O   . GLY A 1 11  ? 13.399  -11.613 -9.909  1.00 22.47  ? 11  GLY A O   1 
ATOM   83   N  N   . LYS A 1 12  ? 11.749  -12.832 -10.862 1.00 25.12  ? 12  LYS A N   1 
ATOM   84   C  CA  . LYS A 1 12  ? 12.714  -13.788 -11.477 1.00 30.32  ? 12  LYS A CA  1 
ATOM   85   C  C   . LYS A 1 12  ? 13.686  -13.061 -12.422 1.00 31.55  ? 12  LYS A C   1 
ATOM   86   O  O   . LYS A 1 12  ? 14.826  -13.560 -12.575 1.00 30.42  ? 12  LYS A O   1 
ATOM   87   C  CB  . LYS A 1 12  ? 11.978  -14.881 -12.237 1.00 32.60  ? 12  LYS A CB  1 
ATOM   88   C  CG  . LYS A 1 12  ? 11.248  -15.879 -11.357 1.00 32.86  ? 12  LYS A CG  1 
ATOM   89   C  CD  . LYS A 1 12  ? 10.497  -16.877 -12.177 1.00 33.12  ? 12  LYS A CD  1 
ATOM   90   C  CE  . LYS A 1 12  ? 9.906   -17.980 -11.334 1.00 36.12  ? 12  LYS A CE  1 
ATOM   91   N  NZ  . LYS A 1 12  ? 9.026   -17.420 -10.290 1.00 38.82  ? 12  LYS A NZ  1 
ATOM   92   N  N   . VAL A 1 13  ? 13.269  -11.947 -13.038 1.00 26.37  ? 13  VAL A N   1 
ATOM   93   C  CA  . VAL A 1 13  ? 14.143  -11.141 -13.935 1.00 24.63  ? 13  VAL A CA  1 
ATOM   94   C  C   . VAL A 1 13  ? 14.969  -10.184 -13.084 1.00 23.30  ? 13  VAL A C   1 
ATOM   95   O  O   . VAL A 1 13  ? 16.153  -9.994  -13.397 1.00 22.86  ? 13  VAL A O   1 
ATOM   96   C  CB  . VAL A 1 13  ? 13.372  -10.378 -15.031 1.00 23.89  ? 13  VAL A CB  1 
ATOM   97   C  CG1 . VAL A 1 13  ? 14.333  -9.624  -15.946 1.00 23.97  ? 13  VAL A CG1 1 
ATOM   98   C  CG2 . VAL A 1 13  ? 12.504  -11.299 -15.858 1.00 25.52  ? 13  VAL A CG2 1 
ATOM   99   N  N   . GLU A 1 14  ? 14.388  -9.602  -12.036 1.00 22.63  ? 14  GLU A N   1 
ATOM   100  C  CA  . GLU A 1 14  ? 15.146  -8.699  -11.128 1.00 22.41  ? 14  GLU A CA  1 
ATOM   101  C  C   . GLU A 1 14  ? 16.454  -9.364  -10.643 1.00 25.27  ? 14  GLU A C   1 
ATOM   102  O  O   . GLU A 1 14  ? 17.473  -8.671  -10.611 1.00 25.53  ? 14  GLU A O   1 
ATOM   103  C  CB  . GLU A 1 14  ? 14.294  -8.275  -9.934  1.00 22.21  ? 14  GLU A CB  1 
ATOM   104  C  CG  . GLU A 1 14  ? 13.171  -7.295  -10.276 1.00 22.73  ? 14  GLU A CG  1 
ATOM   105  C  CD  . GLU A 1 14  ? 12.156  -7.164  -9.145  1.00 22.86  ? 14  GLU A CD  1 
ATOM   106  O  OE1 . GLU A 1 14  ? 12.559  -6.789  -8.067  1.00 27.56  ? 14  GLU A OE1 1 
ATOM   107  O  OE2 . GLU A 1 14  ? 10.980  -7.472  -9.334  1.00 23.51  ? 14  GLU A OE2 1 
ATOM   108  N  N   . GLY A 1 15  ? 16.450  -10.632 -10.242 1.00 23.14  ? 15  GLY A N   1 
ATOM   109  C  CA  . GLY A 1 15  ? 17.669  -11.272 -9.703  1.00 26.99  ? 15  GLY A CA  1 
ATOM   110  C  C   . GLY A 1 15  ? 18.722  -11.513 -10.786 1.00 27.64  ? 15  GLY A C   1 
ATOM   111  O  O   . GLY A 1 15  ? 19.738  -12.125 -10.476 1.00 27.19  ? 15  GLY A O   1 
ATOM   112  N  N   . CYS A 1 16  ? 18.470  -11.127 -12.045 1.00 27.14  ? 16  CYS A N   1 
ATOM   113  C  CA  . CYS A 1 16  ? 19.411  -11.372 -13.162 1.00 27.40  ? 16  CYS A CA  1 
ATOM   114  C  C   . CYS A 1 16  ? 20.033  -10.070 -13.671 1.00 27.53  ? 16  CYS A C   1 
ATOM   115  O  O   . CYS A 1 16  ? 20.926  -10.153 -14.557 1.00 29.41  ? 16  CYS A O   1 
ATOM   116  C  CB  . CYS A 1 16  ? 18.722  -12.047 -14.329 1.00 26.95  ? 16  CYS A CB  1 
ATOM   117  S  SG  . CYS A 1 16  ? 18.051  -13.672 -13.950 1.00 28.90  ? 16  CYS A SG  1 
ATOM   118  N  N   . MET A 1 17  ? 19.591  -8.912  -13.187 1.00 26.96  ? 17  MET A N   1 
ATOM   119  C  CA  . MET A 1 17  ? 20.013  -7.613  -13.776 1.00 24.97  ? 17  MET A CA  1 
ATOM   120  C  C   . MET A 1 17  ? 21.319  -7.140  -13.111 1.00 26.29  ? 17  MET A C   1 
ATOM   121  O  O   . MET A 1 17  ? 21.421  -7.127  -11.858 1.00 23.07  ? 17  MET A O   1 
ATOM   122  C  CB  . MET A 1 17  ? 18.924  -6.539  -13.640 1.00 27.31  ? 17  MET A CB  1 
ATOM   123  C  CG  . MET A 1 17  ? 17.618  -6.878  -14.353 1.00 24.57  ? 17  MET A CG  1 
ATOM   124  S  SD  . MET A 1 17  ? 17.800  -7.345  -16.092 1.00 26.43  ? 17  MET A SD  1 
ATOM   125  C  CE  . MET A 1 17  ? 18.696  -5.959  -16.784 1.00 29.01  ? 17  MET A CE  1 
ATOM   126  N  N   . VAL A 1 18  ? 22.296  -6.779  -13.929 1.00 25.04  ? 18  VAL A N   1 
ATOM   127  C  CA  . VAL A 1 18  ? 23.617  -6.250  -13.478 1.00 27.03  ? 18  VAL A CA  1 
ATOM   128  C  C   . VAL A 1 18  ? 23.932  -5.004  -14.281 1.00 28.26  ? 18  VAL A C   1 
ATOM   129  O  O   . VAL A 1 18  ? 23.208  -4.730  -15.279 1.00 26.29  ? 18  VAL A O   1 
ATOM   130  C  CB  . VAL A 1 18  ? 24.722  -7.302  -13.640 1.00 28.38  ? 18  VAL A CB  1 
ATOM   131  C  CG1 . VAL A 1 18  ? 24.411  -8.517  -12.791 1.00 29.02  ? 18  VAL A CG1 1 
ATOM   132  C  CG2 . VAL A 1 18  ? 24.933  -7.705  -15.095 1.00 28.95  ? 18  VAL A CG2 1 
ATOM   133  N  N   . GLN A 1 19  ? 24.992  -4.318  -13.863 1.00 30.31  ? 19  GLN A N   1 
ATOM   134  C  CA  . GLN A 1 19  ? 25.540  -3.117  -14.531 1.00 34.08  ? 19  GLN A CA  1 
ATOM   135  C  C   . GLN A 1 19  ? 26.805  -3.535  -15.294 1.00 34.41  ? 19  GLN A C   1 
ATOM   136  O  O   . GLN A 1 19  ? 27.656  -4.168  -14.692 1.00 30.57  ? 19  GLN A O   1 
ATOM   137  C  CB  . GLN A 1 19  ? 25.801  -2.064  -13.454 1.00 38.04  ? 19  GLN A CB  1 
ATOM   138  C  CG  . GLN A 1 19  ? 26.428  -0.788  -13.980 1.00 41.16  ? 19  GLN A CG  1 
ATOM   139  C  CD  . GLN A 1 19  ? 26.746  0.187   -12.872 1.00 45.60  ? 19  GLN A CD  1 
ATOM   140  O  OE1 . GLN A 1 19  ? 26.097  1.222   -12.732 1.00 51.24  ? 19  GLN A OE1 1 
ATOM   141  N  NE2 . GLN A 1 19  ? 27.764  -0.127  -12.088 1.00 39.65  ? 19  GLN A NE2 1 
ATOM   142  N  N   . VAL A 1 20  ? 26.902  -3.213  -16.586 1.00 33.89  ? 20  VAL A N   1 
ATOM   143  C  CA  . VAL A 1 20  ? 28.124  -3.431  -17.404 1.00 29.29  ? 20  VAL A CA  1 
ATOM   144  C  C   . VAL A 1 20  ? 28.714  -2.072  -17.756 1.00 30.77  ? 20  VAL A C   1 
ATOM   145  O  O   . VAL A 1 20  ? 27.982  -1.222  -18.316 1.00 29.15  ? 20  VAL A O   1 
ATOM   146  C  CB  . VAL A 1 20  ? 27.823  -4.258  -18.660 1.00 27.65  ? 20  VAL A CB  1 
ATOM   147  C  CG1 . VAL A 1 20  ? 29.065  -4.473  -19.518 1.00 27.62  ? 20  VAL A CG1 1 
ATOM   148  C  CG2 . VAL A 1 20  ? 27.191  -5.581  -18.289 1.00 28.41  ? 20  VAL A CG2 1 
ATOM   149  N  N   . THR A 1 21  ? 29.995  -1.866  -17.434 1.00 32.53  ? 21  THR A N   1 
ATOM   150  C  CA  . THR A 1 21  ? 30.738  -0.646  -17.829 1.00 31.80  ? 21  THR A CA  1 
ATOM   151  C  C   . THR A 1 21  ? 31.904  -1.029  -18.753 1.00 36.98  ? 21  THR A C   1 
ATOM   152  O  O   . THR A 1 21  ? 32.558  -2.074  -18.538 1.00 36.25  ? 21  THR A O   1 
ATOM   153  C  CB  . THR A 1 21  ? 31.184  0.188   -16.629 1.00 33.53  ? 21  THR A CB  1 
ATOM   154  O  OG1 . THR A 1 21  ? 30.031  0.430   -15.835 1.00 30.34  ? 21  THR A OG1 1 
ATOM   155  C  CG2 . THR A 1 21  ? 31.785  1.514   -17.038 1.00 34.78  ? 21  THR A CG2 1 
ATOM   156  N  N   . CYS A 1 22  ? 32.107  -0.218  -19.789 1.00 36.27  ? 22  CYS A N   1 
ATOM   157  C  CA  . CYS A 1 22  ? 33.233  -0.323  -20.743 1.00 39.40  ? 22  CYS A CA  1 
ATOM   158  C  C   . CYS A 1 22  ? 33.580  1.106   -21.127 1.00 42.08  ? 22  CYS A C   1 
ATOM   159  O  O   . CYS A 1 22  ? 32.663  1.849   -21.549 1.00 41.03  ? 22  CYS A O   1 
ATOM   160  C  CB  . CYS A 1 22  ? 32.826  -1.170  -21.945 1.00 40.10  ? 22  CYS A CB  1 
ATOM   161  S  SG  . CYS A 1 22  ? 34.202  -1.653  -23.009 1.00 45.40  ? 22  CYS A SG  1 
ATOM   162  N  N   . GLY A 1 23  ? 34.815  1.531   -20.894 1.00 43.15  ? 23  GLY A N   1 
ATOM   163  C  CA  . GLY A 1 23  ? 35.176  2.944   -21.108 1.00 38.99  ? 23  GLY A CA  1 
ATOM   164  C  C   . GLY A 1 23  ? 34.332  3.862   -20.236 1.00 36.75  ? 23  GLY A C   1 
ATOM   165  O  O   . GLY A 1 23  ? 34.242  3.609   -19.033 1.00 36.67  ? 23  GLY A O   1 
ATOM   166  N  N   . THR A 1 24  ? 33.701  4.882   -20.826 1.00 39.26  ? 24  THR A N   1 
ATOM   167  C  CA  . THR A 1 24  ? 32.822  5.850   -20.115 1.00 40.53  ? 24  THR A CA  1 
ATOM   168  C  C   . THR A 1 24  ? 31.341  5.436   -20.247 1.00 40.25  ? 24  THR A C   1 
ATOM   169  O  O   . THR A 1 24  ? 30.477  6.240   -19.820 1.00 38.22  ? 24  THR A O   1 
ATOM   170  C  CB  . THR A 1 24  ? 33.062  7.287   -20.616 1.00 42.44  ? 24  THR A CB  1 
ATOM   171  O  OG1 . THR A 1 24  ? 32.468  7.473   -21.898 1.00 42.35  ? 24  THR A OG1 1 
ATOM   172  C  CG2 . THR A 1 24  ? 34.531  7.645   -20.724 1.00 44.15  ? 24  THR A CG2 1 
ATOM   173  N  N   . THR A 1 25  ? 31.059  4.259   -20.827 1.00 35.18  ? 25  THR A N   1 
ATOM   174  C  CA  . THR A 1 25  ? 29.692  3.745   -21.139 1.00 36.85  ? 25  THR A CA  1 
ATOM   175  C  C   . THR A 1 25  ? 29.258  2.701   -20.100 1.00 34.58  ? 25  THR A C   1 
ATOM   176  O  O   . THR A 1 25  ? 29.927  1.646   -19.960 1.00 32.92  ? 25  THR A O   1 
ATOM   177  C  CB  . THR A 1 25  ? 29.607  3.130   -22.545 1.00 38.08  ? 25  THR A CB  1 
ATOM   178  O  OG1 . THR A 1 25  ? 30.061  4.085   -23.496 1.00 39.90  ? 25  THR A OG1 1 
ATOM   179  C  CG2 . THR A 1 25  ? 28.202  2.716   -22.920 1.00 39.79  ? 25  THR A CG2 1 
ATOM   180  N  N   . THR A 1 26  ? 28.141  2.975   -19.433 1.00 38.63  ? 26  THR A N   1 
ATOM   181  C  CA  . THR A 1 26  ? 27.460  2.066   -18.485 1.00 35.62  ? 26  THR A CA  1 
ATOM   182  C  C   . THR A 1 26  ? 26.058  1.749   -19.015 1.00 32.56  ? 26  THR A C   1 
ATOM   183  O  O   . THR A 1 26  ? 25.362  2.671   -19.448 1.00 31.99  ? 26  THR A O   1 
ATOM   184  C  CB  . THR A 1 26  ? 27.426  2.694   -17.085 1.00 38.94  ? 26  THR A CB  1 
ATOM   185  O  OG1 . THR A 1 26  ? 28.758  2.689   -16.565 1.00 41.50  ? 26  THR A OG1 1 
ATOM   186  C  CG2 . THR A 1 26  ? 26.529  1.947   -16.123 1.00 38.54  ? 26  THR A CG2 1 
ATOM   187  N  N   . LEU A 1 27  ? 25.658  0.483   -18.958 1.00 30.62  ? 27  LEU A N   1 
ATOM   188  C  CA  . LEU A 1 27  ? 24.281  0.023   -19.281 1.00 27.65  ? 27  LEU A CA  1 
ATOM   189  C  C   . LEU A 1 27  ? 24.017  -1.301  -18.568 1.00 26.39  ? 27  LEU A C   1 
ATOM   190  O  O   . LEU A 1 27  ? 24.896  -1.766  -17.743 1.00 27.87  ? 27  LEU A O   1 
ATOM   191  C  CB  . LEU A 1 27  ? 24.104  -0.080  -20.801 1.00 26.68  ? 27  LEU A CB  1 
ATOM   192  C  CG  . LEU A 1 27  ? 25.184  -0.788  -21.614 1.00 29.85  ? 27  LEU A CG  1 
ATOM   193  C  CD1 . LEU A 1 27  ? 25.319  -2.289  -21.276 1.00 27.13  ? 27  LEU A CD1 1 
ATOM   194  C  CD2 . LEU A 1 27  ? 24.895  -0.612  -23.103 1.00 29.05  ? 27  LEU A CD2 1 
ATOM   195  N  N   . ASN A 1 28  ? 22.882  -1.907  -18.888 1.00 24.16  ? 28  ASN A N   1 
ATOM   196  C  CA  . ASN A 1 28  ? 22.350  -3.094  -18.182 1.00 24.55  ? 28  ASN A CA  1 
ATOM   197  C  C   . ASN A 1 28  ? 22.825  -4.350  -18.893 1.00 25.44  ? 28  ASN A C   1 
ATOM   198  O  O   . ASN A 1 28  ? 22.920  -4.340  -20.123 1.00 23.40  ? 28  ASN A O   1 
ATOM   199  C  CB  . ASN A 1 28  ? 20.824  -3.018  -18.065 1.00 24.39  ? 28  ASN A CB  1 
ATOM   200  C  CG  . ASN A 1 28  ? 20.405  -1.676  -17.520 1.00 27.35  ? 28  ASN A CG  1 
ATOM   201  O  OD1 . ASN A 1 28  ? 20.599  -1.419  -16.334 1.00 30.09  ? 28  ASN A OD1 1 
ATOM   202  N  ND2 . ASN A 1 28  ? 19.884  -0.799  -18.380 1.00 25.48  ? 28  ASN A ND2 1 
ATOM   203  N  N   . GLY A 1 29  ? 23.061  -5.396  -18.115 1.00 23.71  ? 29  GLY A N   1 
ATOM   204  C  CA  . GLY A 1 29  ? 23.340  -6.759  -18.583 1.00 24.13  ? 29  GLY A CA  1 
ATOM   205  C  C   . GLY A 1 29  ? 22.421  -7.747  -17.919 1.00 23.39  ? 29  GLY A C   1 
ATOM   206  O  O   . GLY A 1 29  ? 21.854  -7.441  -16.862 1.00 25.22  ? 29  GLY A O   1 
ATOM   207  N  N   . LEU A 1 30  ? 22.225  -8.876  -18.567 1.00 26.16  ? 30  LEU A N   1 
ATOM   208  C  CA  . LEU A 1 30  ? 21.374  -9.961  -18.067 1.00 26.33  ? 30  LEU A CA  1 
ATOM   209  C  C   . LEU A 1 30  ? 22.277  -11.121 -17.643 1.00 28.79  ? 30  LEU A C   1 
ATOM   210  O  O   . LEU A 1 30  ? 22.900  -11.723 -18.528 1.00 30.05  ? 30  LEU A O   1 
ATOM   211  C  CB  . LEU A 1 30  ? 20.427  -10.372 -19.183 1.00 26.62  ? 30  LEU A CB  1 
ATOM   212  C  CG  . LEU A 1 30  ? 19.432  -11.444 -18.778 1.00 27.57  ? 30  LEU A CG  1 
ATOM   213  C  CD1 . LEU A 1 30  ? 18.412  -10.881 -17.780 1.00 27.57  ? 30  LEU A CD1 1 
ATOM   214  C  CD2 . LEU A 1 30  ? 18.743  -11.997 -19.998 1.00 28.21  ? 30  LEU A CD2 1 
ATOM   215  N  N   . TRP A 1 31  ? 22.354  -11.391 -16.338 1.00 28.15  ? 31  TRP A N   1 
ATOM   216  C  CA  . TRP A 1 31  ? 23.227  -12.441 -15.736 1.00 29.51  ? 31  TRP A CA  1 
ATOM   217  C  C   . TRP A 1 31  ? 22.454  -13.744 -15.555 1.00 30.13  ? 31  TRP A C   1 
ATOM   218  O  O   . TRP A 1 31  ? 21.538  -13.830 -14.690 1.00 33.13  ? 31  TRP A O   1 
ATOM   219  C  CB  . TRP A 1 31  ? 23.819  -11.936 -14.432 1.00 33.93  ? 31  TRP A CB  1 
ATOM   220  C  CG  . TRP A 1 31  ? 24.790  -12.844 -13.752 1.00 35.17  ? 31  TRP A CG  1 
ATOM   221  C  CD1 . TRP A 1 31  ? 25.547  -13.841 -14.294 1.00 41.36  ? 31  TRP A CD1 1 
ATOM   222  C  CD2 . TRP A 1 31  ? 25.128  -12.795 -12.358 1.00 35.63  ? 31  TRP A CD2 1 
ATOM   223  N  NE1 . TRP A 1 31  ? 26.338  -14.418 -13.328 1.00 39.78  ? 31  TRP A NE1 1 
ATOM   224  C  CE2 . TRP A 1 31  ? 26.119  -13.779 -12.136 1.00 37.32  ? 31  TRP A CE2 1 
ATOM   225  C  CE3 . TRP A 1 31  ? 24.718  -11.989 -11.294 1.00 35.91  ? 31  TRP A CE3 1 
ATOM   226  C  CZ2 . TRP A 1 31  ? 26.662  -14.009 -10.872 1.00 36.70  ? 31  TRP A CZ2 1 
ATOM   227  C  CZ3 . TRP A 1 31  ? 25.263  -12.208 -10.047 1.00 36.25  ? 31  TRP A CZ3 1 
ATOM   228  C  CH2 . TRP A 1 31  ? 26.217  -13.213 -9.840  1.00 36.85  ? 31  TRP A CH2 1 
ATOM   229  N  N   . LEU A 1 32  ? 22.773  -14.709 -16.405 1.00 26.65  ? 32  LEU A N   1 
ATOM   230  C  CA  . LEU A 1 32  ? 22.171  -16.051 -16.399 1.00 28.80  ? 32  LEU A CA  1 
ATOM   231  C  C   . LEU A 1 32  ? 23.332  -17.053 -16.351 1.00 33.51  ? 32  LEU A C   1 
ATOM   232  O  O   . LEU A 1 32  ? 24.271  -16.926 -17.194 1.00 30.53  ? 32  LEU A O   1 
ATOM   233  C  CB  . LEU A 1 32  ? 21.327  -16.209 -17.660 1.00 30.05  ? 32  LEU A CB  1 
ATOM   234  C  CG  . LEU A 1 32  ? 20.132  -15.256 -17.825 1.00 28.63  ? 32  LEU A CG  1 
ATOM   235  C  CD1 . LEU A 1 32  ? 19.559  -15.355 -19.223 1.00 27.30  ? 32  LEU A CD1 1 
ATOM   236  C  CD2 . LEU A 1 32  ? 19.042  -15.546 -16.805 1.00 26.91  ? 32  LEU A CD2 1 
ATOM   237  N  N   . ASP A 1 33  ? 23.307  -17.974 -15.382 1.00 33.08  ? 33  ASP A N   1 
ATOM   238  C  CA  . ASP A 1 33  ? 24.404  -18.951 -15.152 1.00 31.81  ? 33  ASP A CA  1 
ATOM   239  C  C   . ASP A 1 33  ? 25.711  -18.152 -15.103 1.00 30.54  ? 33  ASP A C   1 
ATOM   240  O  O   . ASP A 1 33  ? 25.770  -17.094 -14.393 1.00 30.42  ? 33  ASP A O   1 
ATOM   241  C  CB  . ASP A 1 33  ? 24.316  -20.053 -16.207 1.00 31.17  ? 33  ASP A CB  1 
ATOM   242  C  CG  . ASP A 1 33  ? 23.025  -20.851 -16.145 1.00 36.53  ? 33  ASP A CG  1 
ATOM   243  O  OD1 . ASP A 1 33  ? 22.583  -21.183 -15.014 1.00 51.50  ? 33  ASP A OD1 1 
ATOM   244  O  OD2 . ASP A 1 33  ? 22.474  -21.182 -17.215 1.00 37.84  ? 33  ASP A OD2 1 
ATOM   245  N  N   . ASP A 1 34  ? 26.716  -18.536 -15.887 1.00 34.61  ? 34  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 34  ? 28.042  -17.865 -15.835 1.00 37.46  ? 34  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 34  ? 28.228  -16.920 -17.029 1.00 40.53  ? 34  ASP A C   1 
ATOM   248  O  O   . ASP A 1 34  ? 29.410  -16.633 -17.358 1.00 35.39  ? 34  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 34  ? 29.172  -18.892 -15.739 1.00 40.03  ? 34  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 34  ? 29.277  -19.849 -16.912 1.00 37.95  ? 34  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 34  ? 28.305  -19.971 -17.697 1.00 37.43  ? 34  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 34  ? 30.341  -20.481 -17.030 1.00 50.33  ? 34  ASP A OD2 1 
ATOM   253  N  N   . VAL A 1 35  ? 27.127  -16.390 -17.589 1.00 39.67  ? 35  VAL A N   1 
ATOM   254  C  CA  . VAL A 1 35  ? 27.151  -15.421 -18.731 1.00 34.76  ? 35  VAL A CA  1 
ATOM   255  C  C   . VAL A 1 35  ? 26.322  -14.171 -18.408 1.00 33.88  ? 35  VAL A C   1 
ATOM   256  O  O   . VAL A 1 35  ? 25.167  -14.303 -17.881 1.00 27.95  ? 35  VAL A O   1 
ATOM   257  C  CB  . VAL A 1 35  ? 26.645  -16.068 -20.029 1.00 34.02  ? 35  VAL A CB  1 
ATOM   258  C  CG1 . VAL A 1 35  ? 26.835  -15.144 -21.230 1.00 32.25  ? 35  VAL A CG1 1 
ATOM   259  C  CG2 . VAL A 1 35  ? 27.279  -17.426 -20.274 1.00 34.63  ? 35  VAL A CG2 1 
ATOM   260  N  N   . VAL A 1 36  ? 26.885  -13.009 -18.761 1.00 31.16  ? 36  VAL A N   1 
ATOM   261  C  CA  . VAL A 1 36  ? 26.196  -11.690 -18.795 1.00 29.03  ? 36  VAL A CA  1 
ATOM   262  C  C   . VAL A 1 36  ? 26.002  -11.296 -20.259 1.00 30.65  ? 36  VAL A C   1 
ATOM   263  O  O   . VAL A 1 36  ? 27.024  -11.182 -20.982 1.00 30.46  ? 36  VAL A O   1 
ATOM   264  C  CB  . VAL A 1 36  ? 26.975  -10.613 -18.036 1.00 28.77  ? 36  VAL A CB  1 
ATOM   265  C  CG1 . VAL A 1 36  ? 26.336  -9.252  -18.199 1.00 29.76  ? 36  VAL A CG1 1 
ATOM   266  C  CG2 . VAL A 1 36  ? 27.097  -10.952 -16.561 1.00 32.67  ? 36  VAL A CG2 1 
ATOM   267  N  N   . TYR A 1 37  ? 24.743  -11.128 -20.684 1.00 27.22  ? 37  TYR A N   1 
ATOM   268  C  CA  . TYR A 1 37  ? 24.366  -10.693 -22.050 1.00 25.03  ? 37  TYR A CA  1 
ATOM   269  C  C   . TYR A 1 37  ? 24.139  -9.191  -22.004 1.00 25.59  ? 37  TYR A C   1 
ATOM   270  O  O   . TYR A 1 37  ? 23.433  -8.708  -21.112 1.00 27.22  ? 37  TYR A O   1 
ATOM   271  C  CB  . TYR A 1 37  ? 23.135  -11.424 -22.563 1.00 26.81  ? 37  TYR A CB  1 
ATOM   272  C  CG  . TYR A 1 37  ? 23.226  -12.931 -22.546 1.00 30.34  ? 37  TYR A CG  1 
ATOM   273  C  CD1 . TYR A 1 37  ? 23.107  -13.623 -21.353 1.00 28.42  ? 37  TYR A CD1 1 
ATOM   274  C  CD2 . TYR A 1 37  ? 23.415  -13.666 -23.710 1.00 27.52  ? 37  TYR A CD2 1 
ATOM   275  C  CE1 . TYR A 1 37  ? 23.181  -15.001 -21.312 1.00 29.38  ? 37  TYR A CE1 1 
ATOM   276  C  CE2 . TYR A 1 37  ? 23.496  -15.051 -23.680 1.00 29.63  ? 37  TYR A CE2 1 
ATOM   277  C  CZ  . TYR A 1 37  ? 23.394  -15.719 -22.470 1.00 28.64  ? 37  TYR A CZ  1 
ATOM   278  O  OH  . TYR A 1 37  ? 23.440  -17.075 -22.385 1.00 29.16  ? 37  TYR A OH  1 
ATOM   279  N  N   . CYS A 1 38  ? 24.718  -8.442  -22.937 1.00 25.06  ? 38  CYS A N   1 
ATOM   280  C  CA  . CYS A 1 38  ? 24.405  -6.997  -23.072 1.00 25.71  ? 38  CYS A CA  1 
ATOM   281  C  C   . CYS A 1 38  ? 24.552  -6.569  -24.527 1.00 26.77  ? 38  CYS A C   1 
ATOM   282  O  O   . CYS A 1 38  ? 25.094  -7.315  -25.361 1.00 28.06  ? 38  CYS A O   1 
ATOM   283  C  CB  . CYS A 1 38  ? 25.259  -6.154  -22.141 1.00 27.24  ? 38  CYS A CB  1 
ATOM   284  S  SG  . CYS A 1 38  ? 27.031  -6.087  -22.571 1.00 30.10  ? 38  CYS A SG  1 
ATOM   285  N  N   . PRO A 1 39  ? 24.078  -5.352  -24.880 1.00 26.14  ? 39  PRO A N   1 
ATOM   286  C  CA  . PRO A 1 39  ? 24.262  -4.834  -26.235 1.00 25.65  ? 39  PRO A CA  1 
ATOM   287  C  C   . PRO A 1 39  ? 25.763  -4.686  -26.532 1.00 23.58  ? 39  PRO A C   1 
ATOM   288  O  O   . PRO A 1 39  ? 26.479  -4.181  -25.735 1.00 23.82  ? 39  PRO A O   1 
ATOM   289  C  CB  . PRO A 1 39  ? 23.518  -3.493  -26.230 1.00 25.94  ? 39  PRO A CB  1 
ATOM   290  C  CG  . PRO A 1 39  ? 22.553  -3.617  -25.086 1.00 25.70  ? 39  PRO A CG  1 
ATOM   291  C  CD  . PRO A 1 39  ? 23.322  -4.410  -24.041 1.00 27.53  ? 39  PRO A CD  1 
ATOM   292  N  N   . ARG A 1 40  ? 26.189  -5.152  -27.695 1.00 24.27  ? 40  ARG A N   1 
ATOM   293  C  CA  . ARG A 1 40  ? 27.593  -5.033  -28.151 1.00 23.12  ? 40  ARG A CA  1 
ATOM   294  C  C   . ARG A 1 40  ? 28.012  -3.565  -28.248 1.00 24.87  ? 40  ARG A C   1 
ATOM   295  O  O   . ARG A 1 40  ? 29.222  -3.319  -28.074 1.00 26.28  ? 40  ARG A O   1 
ATOM   296  C  CB  . ARG A 1 40  ? 27.810  -5.799  -29.457 1.00 22.83  ? 40  ARG A CB  1 
ATOM   297  C  CG  . ARG A 1 40  ? 27.221  -5.186  -30.712 1.00 22.31  ? 40  ARG A CG  1 
ATOM   298  C  CD  . ARG A 1 40  ? 27.623  -6.071  -31.894 1.00 23.03  ? 40  ARG A CD  1 
ATOM   299  N  NE  . ARG A 1 40  ? 27.041  -5.611  -33.138 1.00 23.03  ? 40  ARG A NE  1 
ATOM   300  C  CZ  . ARG A 1 40  ? 27.388  -6.049  -34.351 1.00 25.25  ? 40  ARG A CZ  1 
ATOM   301  N  NH1 . ARG A 1 40  ? 28.308  -6.990  -34.494 1.00 25.13  ? 40  ARG A NH1 1 
ATOM   302  N  NH2 . ARG A 1 40  ? 26.818  -5.540  -35.424 1.00 24.11  ? 40  ARG A NH2 1 
ATOM   303  N  N   . HIS A 1 41  ? 27.088  -2.614  -28.420 1.00 24.28  ? 41  HIS A N   1 
ATOM   304  C  CA  . HIS A 1 41  ? 27.445  -1.175  -28.584 1.00 23.56  ? 41  HIS A CA  1 
ATOM   305  C  C   . HIS A 1 41  ? 28.021  -0.562  -27.294 1.00 23.84  ? 41  HIS A C   1 
ATOM   306  O  O   . HIS A 1 41  ? 28.562  0.571   -27.367 1.00 22.88  ? 41  HIS A O   1 
ATOM   307  C  CB  . HIS A 1 41  ? 26.282  -0.363  -29.174 1.00 24.05  ? 41  HIS A CB  1 
ATOM   308  C  CG  . HIS A 1 41  ? 25.103  -0.133  -28.285 1.00 25.76  ? 41  HIS A CG  1 
ATOM   309  N  ND1 . HIS A 1 41  ? 25.170  0.573   -27.091 1.00 27.07  ? 41  HIS A ND1 1 
ATOM   310  C  CD2 . HIS A 1 41  ? 23.808  -0.451  -28.448 1.00 26.00  ? 41  HIS A CD2 1 
ATOM   311  C  CE1 . HIS A 1 41  ? 23.972  0.644   -26.555 1.00 25.45  ? 41  HIS A CE1 1 
ATOM   312  N  NE2 . HIS A 1 41  ? 23.125  0.028   -27.365 1.00 26.85  ? 41  HIS A NE2 1 
ATOM   313  N  N   . VAL A 1 42  ? 27.986  -1.280  -26.183 1.00 25.07  ? 42  VAL A N   1 
ATOM   314  C  CA  . VAL A 1 42  ? 28.718  -0.890  -24.944 1.00 27.58  ? 42  VAL A CA  1 
ATOM   315  C  C   . VAL A 1 42  ? 30.198  -0.680  -25.290 1.00 27.19  ? 42  VAL A C   1 
ATOM   316  O  O   . VAL A 1 42  ? 30.830  0.124   -24.584 1.00 31.27  ? 42  VAL A O   1 
ATOM   317  C  CB  . VAL A 1 42  ? 28.537  -1.930  -23.807 1.00 27.16  ? 42  VAL A CB  1 
ATOM   318  C  CG1 . VAL A 1 42  ? 29.271  -3.236  -24.072 1.00 27.97  ? 42  VAL A CG1 1 
ATOM   319  C  CG2 . VAL A 1 42  ? 28.937  -1.366  -22.448 1.00 27.42  ? 42  VAL A CG2 1 
ATOM   320  N  N   . ILE A 1 43  ? 30.760  -1.378  -26.290 1.00 27.51  ? 43  ILE A N   1 
ATOM   321  C  CA  . ILE A 1 43  ? 32.228  -1.245  -26.595 1.00 31.58  ? 43  ILE A CA  1 
ATOM   322  C  C   . ILE A 1 43  ? 32.515  -0.076  -27.550 1.00 36.00  ? 43  ILE A C   1 
ATOM   323  O  O   . ILE A 1 43  ? 33.691  0.081   -27.904 1.00 37.44  ? 43  ILE A O   1 
ATOM   324  C  CB  . ILE A 1 43  ? 32.837  -2.540  -27.142 1.00 27.23  ? 43  ILE A CB  1 
ATOM   325  C  CG1 . ILE A 1 43  ? 32.464  -2.767  -28.607 1.00 26.14  ? 43  ILE A CG1 1 
ATOM   326  C  CG2 . ILE A 1 43  ? 32.460  -3.700  -26.241 1.00 27.50  ? 43  ILE A CG2 1 
ATOM   327  C  CD1 . ILE A 1 43  ? 33.034  -4.022  -29.171 1.00 27.28  ? 43  ILE A CD1 1 
ATOM   328  N  N   . CYS A 1 44  ? 31.517  0.733   -27.928 1.00 37.43  ? 44  CYS A N   1 
ATOM   329  C  CA  . CYS A 1 44  ? 31.699  1.891   -28.848 1.00 37.63  ? 44  CYS A CA  1 
ATOM   330  C  C   . CYS A 1 44  ? 32.086  3.145   -28.062 1.00 39.23  ? 44  CYS A C   1 
ATOM   331  O  O   . CYS A 1 44  ? 31.688  3.251   -26.915 1.00 36.12  ? 44  CYS A O   1 
ATOM   332  C  CB  . CYS A 1 44  ? 30.422  2.178   -29.621 1.00 38.67  ? 44  CYS A CB  1 
ATOM   333  S  SG  . CYS A 1 44  ? 29.997  0.815   -30.722 1.00 41.22  ? 44  CYS A SG  1 
ATOM   334  N  N   . THR A 1 45  ? 32.831  4.048   -28.694 1.00 43.01  ? 45  THR A N   1 
ATOM   335  C  CA  . THR A 1 45  ? 33.104  5.443   -28.254 1.00 47.91  ? 45  THR A CA  1 
ATOM   336  C  C   . THR A 1 45  ? 32.320  6.396   -29.173 1.00 53.41  ? 45  THR A C   1 
ATOM   337  O  O   . THR A 1 45  ? 31.532  5.875   -30.029 1.00 45.05  ? 45  THR A O   1 
ATOM   338  C  CB  . THR A 1 45  ? 34.616  5.688   -28.300 1.00 51.05  ? 45  THR A CB  1 
ATOM   339  O  OG1 . THR A 1 45  ? 34.988  5.676   -29.676 1.00 54.31  ? 45  THR A OG1 1 
ATOM   340  C  CG2 . THR A 1 45  ? 35.432  4.621   -27.607 1.00 50.23  ? 45  THR A CG2 1 
ATOM   341  N  N   . SER A 1 46  ? 32.546  7.716   -29.048 1.00 58.68  ? 46  SER A N   1 
ATOM   342  C  CA  . SER A 1 46  ? 31.957  8.796   -29.901 1.00 65.52  ? 46  SER A CA  1 
ATOM   343  C  C   . SER A 1 46  ? 32.037  8.441   -31.394 1.00 67.35  ? 46  SER A C   1 
ATOM   344  O  O   . SER A 1 46  ? 30.965  8.270   -32.016 1.00 75.52  ? 46  SER A O   1 
ATOM   345  C  CB  . SER A 1 46  ? 32.624  10.133  -29.676 1.00 65.52  ? 46  SER A CB  1 
ATOM   346  O  OG  . SER A 1 46  ? 32.607  10.484  -28.309 1.00 68.62  ? 46  SER A OG  1 
ATOM   347  N  N   . GLU A 1 47  ? 33.253  8.325   -31.947 1.00 69.93  ? 47  GLU A N   1 
ATOM   348  C  CA  . GLU A 1 47  ? 33.471  8.171   -33.415 1.00 69.27  ? 47  GLU A CA  1 
ATOM   349  C  C   . GLU A 1 47  ? 33.299  6.703   -33.827 1.00 56.42  ? 47  GLU A C   1 
ATOM   350  O  O   . GLU A 1 47  ? 33.632  6.387   -34.969 1.00 55.62  ? 47  GLU A O   1 
ATOM   351  C  CB  . GLU A 1 47  ? 34.855  8.640   -33.887 1.00 79.44  ? 47  GLU A CB  1 
ATOM   352  C  CG  . GLU A 1 47  ? 35.470  9.785   -33.110 1.00 81.19  ? 47  GLU A CG  1 
ATOM   353  C  CD  . GLU A 1 47  ? 36.461  9.296   -32.076 1.00 82.73  ? 47  GLU A CD  1 
ATOM   354  O  OE1 . GLU A 1 47  ? 37.488  8.716   -32.487 1.00 77.95  ? 47  GLU A OE1 1 
ATOM   355  O  OE2 . GLU A 1 47  ? 36.176  9.454   -30.871 1.00 92.27  ? 47  GLU A OE2 1 
ATOM   356  N  N   . ASP A 1 48  ? 32.814  5.833   -32.943 1.00 49.48  ? 48  ASP A N   1 
ATOM   357  C  CA  . ASP A 1 48  ? 32.460  4.432   -33.292 1.00 48.87  ? 48  ASP A CA  1 
ATOM   358  C  C   . ASP A 1 48  ? 30.953  4.317   -33.507 1.00 49.52  ? 48  ASP A C   1 
ATOM   359  O  O   . ASP A 1 48  ? 30.464  3.178   -33.597 1.00 63.71  ? 48  ASP A O   1 
ATOM   360  C  CB  . ASP A 1 48  ? 32.899  3.438   -32.215 1.00 43.55  ? 48  ASP A CB  1 
ATOM   361  C  CG  . ASP A 1 48  ? 34.404  3.349   -32.079 1.00 45.38  ? 48  ASP A CG  1 
ATOM   362  O  OD1 . ASP A 1 48  ? 35.069  3.131   -33.116 1.00 42.95  ? 48  ASP A OD1 1 
ATOM   363  O  OD2 . ASP A 1 48  ? 34.895  3.510   -30.945 1.00 42.77  ? 48  ASP A OD2 1 
ATOM   364  N  N   . MET A 1 49  ? 30.224  5.428   -33.557 1.00 46.77  ? 49  MET A N   1 
ATOM   365  C  CA  . MET A 1 49  ? 28.747  5.340   -33.514 1.00 49.01  ? 49  MET A CA  1 
ATOM   366  C  C   . MET A 1 49  ? 28.196  5.139   -34.933 1.00 41.76  ? 49  MET A C   1 
ATOM   367  O  O   . MET A 1 49  ? 27.215  4.400   -35.058 1.00 37.23  ? 49  MET A O   1 
ATOM   368  C  CB  . MET A 1 49  ? 28.130  6.570   -32.834 1.00 61.20  ? 49  MET A CB  1 
ATOM   369  C  CG  . MET A 1 49  ? 28.309  6.600   -31.308 1.00 70.40  ? 49  MET A CG  1 
ATOM   370  S  SD  . MET A 1 49  ? 28.363  4.961   -30.503 1.00 89.01  ? 49  MET A SD  1 
ATOM   371  C  CE  . MET A 1 49  ? 26.823  4.205   -31.022 1.00 85.13  ? 49  MET A CE  1 
ATOM   372  N  N   . LEU A 1 50  ? 28.798  5.743   -35.964 1.00 35.59  ? 50  LEU A N   1 
ATOM   373  C  CA  . LEU A 1 50  ? 28.222  5.729   -37.336 1.00 34.35  ? 50  LEU A CA  1 
ATOM   374  C  C   . LEU A 1 50  ? 28.548  4.400   -38.015 1.00 29.73  ? 50  LEU A C   1 
ATOM   375  O  O   . LEU A 1 50  ? 27.657  3.816   -38.668 1.00 32.41  ? 50  LEU A O   1 
ATOM   376  C  CB  . LEU A 1 50  ? 28.774  6.898   -38.159 1.00 40.04  ? 50  LEU A CB  1 
ATOM   377  C  CG  . LEU A 1 50  ? 28.132  8.265   -37.917 1.00 45.79  ? 50  LEU A CG  1 
ATOM   378  C  CD1 . LEU A 1 50  ? 26.638  8.227   -38.209 1.00 50.04  ? 50  LEU A CD1 1 
ATOM   379  C  CD2 . LEU A 1 50  ? 28.376  8.738   -36.498 1.00 48.23  ? 50  LEU A CD2 1 
ATOM   380  N  N   . ASN A 1 51  ? 29.794  3.949   -37.907 1.00 26.64  ? 51  ASN A N   1 
ATOM   381  C  CA  . ASN A 1 51  ? 30.288  2.798   -38.709 1.00 27.34  ? 51  ASN A CA  1 
ATOM   382  C  C   . ASN A 1 51  ? 31.167  1.910   -37.844 1.00 28.68  ? 51  ASN A C   1 
ATOM   383  O  O   . ASN A 1 51  ? 32.282  1.588   -38.214 1.00 29.51  ? 51  ASN A O   1 
ATOM   384  C  CB  . ASN A 1 51  ? 31.011  3.305   -39.953 1.00 27.38  ? 51  ASN A CB  1 
ATOM   385  C  CG  . ASN A 1 51  ? 30.023  3.933   -40.910 1.00 30.29  ? 51  ASN A CG  1 
ATOM   386  O  OD1 . ASN A 1 51  ? 29.261  3.212   -41.565 1.00 30.08  ? 51  ASN A OD1 1 
ATOM   387  N  ND2 . ASN A 1 51  ? 29.987  5.258   -40.946 1.00 27.07  ? 51  ASN A ND2 1 
ATOM   388  N  N   . PRO A 1 52  ? 30.712  1.480   -36.658 1.00 28.11  ? 52  PRO A N   1 
ATOM   389  C  CA  . PRO A 1 52  ? 31.554  0.673   -35.787 1.00 29.39  ? 52  PRO A CA  1 
ATOM   390  C  C   . PRO A 1 52  ? 31.932  -0.624  -36.507 1.00 28.35  ? 52  PRO A C   1 
ATOM   391  O  O   . PRO A 1 52  ? 31.107  -1.199  -37.187 1.00 27.68  ? 52  PRO A O   1 
ATOM   392  C  CB  . PRO A 1 52  ? 30.689  0.424   -34.541 1.00 28.47  ? 52  PRO A CB  1 
ATOM   393  C  CG  . PRO A 1 52  ? 29.291  0.645   -35.037 1.00 29.91  ? 52  PRO A CG  1 
ATOM   394  C  CD  . PRO A 1 52  ? 29.394  1.733   -36.081 1.00 29.78  ? 52  PRO A CD  1 
ATOM   395  N  N   . ASN A 1 53  ? 33.196  -1.006  -36.387 1.00 26.06  ? 53  ASN A N   1 
ATOM   396  C  CA  . ASN A 1 53  ? 33.688  -2.315  -36.849 1.00 28.31  ? 53  ASN A CA  1 
ATOM   397  C  C   . ASN A 1 53  ? 33.781  -3.141  -35.575 1.00 28.66  ? 53  ASN A C   1 
ATOM   398  O  O   . ASN A 1 53  ? 34.745  -2.964  -34.833 1.00 25.65  ? 53  ASN A O   1 
ATOM   399  C  CB  . ASN A 1 53  ? 35.008  -2.155  -37.599 1.00 29.63  ? 53  ASN A CB  1 
ATOM   400  C  CG  . ASN A 1 53  ? 35.492  -3.455  -38.197 1.00 32.38  ? 53  ASN A CG  1 
ATOM   401  O  OD1 . ASN A 1 53  ? 35.288  -4.518  -37.622 1.00 32.71  ? 53  ASN A OD1 1 
ATOM   402  N  ND2 . ASN A 1 53  ? 36.165  -3.368  -39.334 1.00 33.64  ? 53  ASN A ND2 1 
ATOM   403  N  N   . TYR A 1 54  ? 32.742  -3.898  -35.253 1.00 30.04  ? 54  TYR A N   1 
ATOM   404  C  CA  . TYR A 1 54  ? 32.623  -4.477  -33.898 1.00 27.23  ? 54  TYR A CA  1 
ATOM   405  C  C   . TYR A 1 54  ? 33.723  -5.521  -33.706 1.00 27.89  ? 54  TYR A C   1 
ATOM   406  O  O   . TYR A 1 54  ? 34.197  -5.637  -32.555 1.00 28.20  ? 54  TYR A O   1 
ATOM   407  C  CB  . TYR A 1 54  ? 31.208  -4.994  -33.662 1.00 27.22  ? 54  TYR A CB  1 
ATOM   408  C  CG  . TYR A 1 54  ? 30.208  -3.902  -33.378 1.00 26.15  ? 54  TYR A CG  1 
ATOM   409  C  CD1 . TYR A 1 54  ? 30.155  -3.318  -32.129 1.00 25.41  ? 54  TYR A CD1 1 
ATOM   410  C  CD2 . TYR A 1 54  ? 29.289  -3.489  -34.335 1.00 25.76  ? 54  TYR A CD2 1 
ATOM   411  C  CE1 . TYR A 1 54  ? 29.214  -2.360  -31.825 1.00 27.04  ? 54  TYR A CE1 1 
ATOM   412  C  CE2 . TYR A 1 54  ? 28.356  -2.506  -34.055 1.00 26.63  ? 54  TYR A CE2 1 
ATOM   413  C  CZ  . TYR A 1 54  ? 28.318  -1.940  -32.792 1.00 25.34  ? 54  TYR A CZ  1 
ATOM   414  O  OH  . TYR A 1 54  ? 27.400  -0.975  -32.490 1.00 24.19  ? 54  TYR A OH  1 
ATOM   415  N  N   . GLU A 1 55  ? 34.074  -6.261  -34.757 1.00 27.59  ? 55  GLU A N   1 
ATOM   416  C  CA  . GLU A 1 55  ? 35.079  -7.355  -34.707 1.00 33.27  ? 55  GLU A CA  1 
ATOM   417  C  C   . GLU A 1 55  ? 36.442  -6.720  -34.366 1.00 31.82  ? 55  GLU A C   1 
ATOM   418  O  O   . GLU A 1 55  ? 37.117  -7.205  -33.450 1.00 31.30  ? 55  GLU A O   1 
ATOM   419  C  CB  . GLU A 1 55  ? 35.047  -8.173  -36.005 1.00 39.90  ? 55  GLU A CB  1 
ATOM   420  C  CG  . GLU A 1 55  ? 35.907  -9.442  -35.987 1.00 51.91  ? 55  GLU A CG  1 
ATOM   421  C  CD  . GLU A 1 55  ? 36.766  -9.782  -37.214 1.00 61.38  ? 55  GLU A CD  1 
ATOM   422  O  OE1 . GLU A 1 55  ? 36.550  -9.207  -38.319 1.00 68.21  ? 55  GLU A OE1 1 
ATOM   423  O  OE2 . GLU A 1 55  ? 37.678  -10.637 -37.067 1.00 69.58  ? 55  GLU A OE2 1 
ATOM   424  N  N   . ASP A 1 56  ? 36.760  -5.587  -34.984 1.00 31.28  ? 56  ASP A N   1 
ATOM   425  C  CA  . ASP A 1 56  ? 37.973  -4.776  -34.701 1.00 29.75  ? 56  ASP A CA  1 
ATOM   426  C  C   . ASP A 1 56  ? 37.936  -4.175  -33.286 1.00 31.92  ? 56  ASP A C   1 
ATOM   427  O  O   . ASP A 1 56  ? 39.009  -4.139  -32.628 1.00 25.73  ? 56  ASP A O   1 
ATOM   428  C  CB  . ASP A 1 56  ? 38.132  -3.672  -35.746 1.00 30.20  ? 56  ASP A CB  1 
ATOM   429  C  CG  . ASP A 1 56  ? 39.446  -2.920  -35.591 1.00 34.84  ? 56  ASP A CG  1 
ATOM   430  O  OD1 . ASP A 1 56  ? 40.519  -3.534  -35.845 1.00 32.21  ? 56  ASP A OD1 1 
ATOM   431  O  OD2 . ASP A 1 56  ? 39.384  -1.753  -35.180 1.00 33.79  ? 56  ASP A OD2 1 
ATOM   432  N  N   . LEU A 1 57  ? 36.788  -3.684  -32.809 1.00 27.86  ? 57  LEU A N   1 
ATOM   433  C  CA  . LEU A 1 57  ? 36.759  -2.994  -31.487 1.00 29.92  ? 57  LEU A CA  1 
ATOM   434  C  C   . LEU A 1 57  ? 36.895  -4.049  -30.389 1.00 31.05  ? 57  LEU A C   1 
ATOM   435  O  O   . LEU A 1 57  ? 37.576  -3.775  -29.379 1.00 35.31  ? 57  LEU A O   1 
ATOM   436  C  CB  . LEU A 1 57  ? 35.475  -2.183  -31.333 1.00 28.17  ? 57  LEU A CB  1 
ATOM   437  C  CG  . LEU A 1 57  ? 35.401  -0.954  -32.228 1.00 31.82  ? 57  LEU A CG  1 
ATOM   438  C  CD1 . LEU A 1 57  ? 33.977  -0.406  -32.298 1.00 34.02  ? 57  LEU A CD1 1 
ATOM   439  C  CD2 . LEU A 1 57  ? 36.376  0.127   -31.768 1.00 32.96  ? 57  LEU A CD2 1 
ATOM   440  N  N   . LEU A 1 58  ? 36.320  -5.227  -30.599 1.00 30.06  ? 58  LEU A N   1 
ATOM   441  C  CA  . LEU A 1 58  ? 36.284  -6.279  -29.555 1.00 32.86  ? 58  LEU A CA  1 
ATOM   442  C  C   . LEU A 1 58  ? 37.638  -7.001  -29.434 1.00 31.41  ? 58  LEU A C   1 
ATOM   443  O  O   . LEU A 1 58  ? 38.003  -7.319  -28.301 1.00 28.18  ? 58  LEU A O   1 
ATOM   444  C  CB  . LEU A 1 58  ? 35.158  -7.269  -29.852 1.00 31.87  ? 58  LEU A CB  1 
ATOM   445  C  CG  . LEU A 1 58  ? 34.913  -8.302  -28.750 1.00 34.31  ? 58  LEU A CG  1 
ATOM   446  C  CD1 . LEU A 1 58  ? 34.356  -7.665  -27.477 1.00 37.62  ? 58  LEU A CD1 1 
ATOM   447  C  CD2 . LEU A 1 58  ? 33.991  -9.402  -29.256 1.00 35.18  ? 58  LEU A CD2 1 
ATOM   448  N  N   . ILE A 1 59  ? 38.324  -7.297  -30.543 1.00 33.71  ? 59  ILE A N   1 
ATOM   449  C  CA  . ILE A 1 59  ? 39.649  -7.994  -30.517 1.00 36.94  ? 59  ILE A CA  1 
ATOM   450  C  C   . ILE A 1 59  ? 40.639  -7.195  -29.656 1.00 35.62  ? 59  ILE A C   1 
ATOM   451  O  O   . ILE A 1 59  ? 41.525  -7.829  -29.070 1.00 41.54  ? 59  ILE A O   1 
ATOM   452  C  CB  . ILE A 1 59  ? 40.210  -8.247  -31.926 1.00 39.83  ? 59  ILE A CB  1 
ATOM   453  C  CG1 . ILE A 1 59  ? 41.241  -9.381  -31.903 1.00 42.33  ? 59  ILE A CG1 1 
ATOM   454  C  CG2 . ILE A 1 59  ? 40.782  -6.969  -32.510 1.00 36.97  ? 59  ILE A CG2 1 
ATOM   455  C  CD1 . ILE A 1 59  ? 41.664  -9.830  -33.281 1.00 44.74  ? 59  ILE A CD1 1 
ATOM   456  N  N   . ARG A 1 60  ? 40.454  -5.882  -29.542 1.00 30.09  ? 60  ARG A N   1 
ATOM   457  C  CA  . ARG A 1 60  ? 41.345  -4.946  -28.802 1.00 31.75  ? 60  ARG A CA  1 
ATOM   458  C  C   . ARG A 1 60  ? 40.993  -4.905  -27.312 1.00 34.16  ? 60  ARG A C   1 
ATOM   459  O  O   . ARG A 1 60  ? 41.679  -4.169  -26.566 1.00 38.14  ? 60  ARG A O   1 
ATOM   460  C  CB  . ARG A 1 60  ? 41.209  -3.541  -29.399 1.00 29.24  ? 60  ARG A CB  1 
ATOM   461  C  CG  . ARG A 1 60  ? 41.633  -3.477  -30.864 1.00 28.47  ? 60  ARG A CG  1 
ATOM   462  C  CD  . ARG A 1 60  ? 41.286  -2.158  -31.532 1.00 29.27  ? 60  ARG A CD  1 
ATOM   463  N  NE  . ARG A 1 60  ? 41.581  -2.163  -32.962 1.00 28.77  ? 60  ARG A NE  1 
ATOM   464  C  CZ  . ARG A 1 60  ? 42.734  -1.807  -33.517 1.00 28.42  ? 60  ARG A CZ  1 
ATOM   465  N  NH1 . ARG A 1 60  ? 43.766  -1.463  -32.765 1.00 28.28  ? 60  ARG A NH1 1 
ATOM   466  N  NH2 . ARG A 1 60  ? 42.854  -1.799  -34.824 1.00 29.32  ? 60  ARG A NH2 1 
ATOM   467  N  N   . LYS A 1 61  ? 39.936  -5.600  -26.900 1.00 34.41  ? 61  LYS A N   1 
ATOM   468  C  CA  . LYS A 1 61  ? 39.467  -5.605  -25.487 1.00 38.56  ? 61  LYS A CA  1 
ATOM   469  C  C   . LYS A 1 61  ? 40.039  -6.834  -24.774 1.00 38.61  ? 61  LYS A C   1 
ATOM   470  O  O   . LYS A 1 61  ? 40.116  -7.927  -25.384 1.00 37.25  ? 61  LYS A O   1 
ATOM   471  C  CB  . LYS A 1 61  ? 37.936  -5.613  -25.395 1.00 38.59  ? 61  LYS A CB  1 
ATOM   472  C  CG  . LYS A 1 61  ? 37.247  -4.380  -25.967 1.00 40.35  ? 61  LYS A CG  1 
ATOM   473  C  CD  . LYS A 1 61  ? 37.311  -3.175  -25.070 1.00 43.33  ? 61  LYS A CD  1 
ATOM   474  C  CE  . LYS A 1 61  ? 37.192  -1.874  -25.838 1.00 45.85  ? 61  LYS A CE  1 
ATOM   475  N  NZ  . LYS A 1 61  ? 36.965  -0.736  -24.924 1.00 51.64  ? 61  LYS A NZ  1 
ATOM   476  N  N   . SER A 1 62  ? 40.436  -6.658  -23.521 1.00 39.79  ? 62  SER A N   1 
ATOM   477  C  CA  . SER A 1 62  ? 40.677  -7.797  -22.605 1.00 48.71  ? 62  SER A CA  1 
ATOM   478  C  C   . SER A 1 62  ? 39.535  -7.830  -21.590 1.00 44.47  ? 62  SER A C   1 
ATOM   479  O  O   . SER A 1 62  ? 38.811  -6.812  -21.436 1.00 43.02  ? 62  SER A O   1 
ATOM   480  C  CB  . SER A 1 62  ? 42.026  -7.716  -21.941 1.00 53.26  ? 62  SER A CB  1 
ATOM   481  O  OG  . SER A 1 62  ? 42.023  -6.705  -20.946 1.00 61.60  ? 62  SER A OG  1 
ATOM   482  N  N   . ASN A 1 63  ? 39.387  -8.977  -20.945 1.00 45.58  ? 63  ASN A N   1 
ATOM   483  C  CA  . ASN A 1 63  ? 38.366  -9.236  -19.907 1.00 42.93  ? 63  ASN A CA  1 
ATOM   484  C  C   . ASN A 1 63  ? 38.336  -8.070  -18.904 1.00 43.06  ? 63  ASN A C   1 
ATOM   485  O  O   . ASN A 1 63  ? 37.229  -7.646  -18.517 1.00 40.06  ? 63  ASN A O   1 
ATOM   486  C  CB  . ASN A 1 63  ? 38.630  -10.602 -19.284 1.00 42.24  ? 63  ASN A CB  1 
ATOM   487  C  CG  . ASN A 1 63  ? 38.573  -11.745 -20.279 1.00 44.34  ? 63  ASN A CG  1 
ATOM   488  O  OD1 . ASN A 1 63  ? 37.710  -11.787 -21.158 1.00 43.73  ? 63  ASN A OD1 1 
ATOM   489  N  ND2 . ASN A 1 63  ? 39.445  -12.724 -20.090 1.00 39.96  ? 63  ASN A ND2 1 
ATOM   490  N  N   . HIS A 1 64  ? 39.481  -7.514  -18.503 1.00 42.78  ? 64  HIS A N   1 
ATOM   491  C  CA  . HIS A 1 64  ? 39.540  -6.527  -17.385 1.00 45.93  ? 64  HIS A CA  1 
ATOM   492  C  C   . HIS A 1 64  ? 39.070  -5.135  -17.820 1.00 42.70  ? 64  HIS A C   1 
ATOM   493  O  O   . HIS A 1 64  ? 38.915  -4.301  -16.929 1.00 40.80  ? 64  HIS A O   1 
ATOM   494  C  CB  . HIS A 1 64  ? 40.929  -6.486  -16.709 1.00 53.05  ? 64  HIS A CB  1 
ATOM   495  C  CG  . HIS A 1 64  ? 42.076  -6.211  -17.627 1.00 59.45  ? 64  HIS A CG  1 
ATOM   496  N  ND1 . HIS A 1 64  ? 42.903  -7.224  -18.095 1.00 64.07  ? 64  HIS A ND1 1 
ATOM   497  C  CD2 . HIS A 1 64  ? 42.546  -5.058  -18.155 1.00 59.14  ? 64  HIS A CD2 1 
ATOM   498  C  CE1 . HIS A 1 64  ? 43.831  -6.709  -18.873 1.00 64.24  ? 64  HIS A CE1 1 
ATOM   499  N  NE2 . HIS A 1 64  ? 43.628  -5.376  -18.933 1.00 61.60  ? 64  HIS A NE2 1 
ATOM   500  N  N   . ASN A 1 65  ? 38.841  -4.888  -19.114 1.00 40.59  ? 65  ASN A N   1 
ATOM   501  C  CA  . ASN A 1 65  ? 38.246  -3.623  -19.634 1.00 42.42  ? 65  ASN A CA  1 
ATOM   502  C  C   . ASN A 1 65  ? 36.749  -3.527  -19.262 1.00 41.06  ? 65  ASN A C   1 
ATOM   503  O  O   . ASN A 1 65  ? 36.215  -2.405  -19.236 1.00 41.15  ? 65  ASN A O   1 
ATOM   504  C  CB  . ASN A 1 65  ? 38.376  -3.529  -21.162 1.00 44.67  ? 65  ASN A CB  1 
ATOM   505  C  CG  . ASN A 1 65  ? 39.810  -3.445  -21.645 1.00 48.25  ? 65  ASN A CG  1 
ATOM   506  O  OD1 . ASN A 1 65  ? 40.262  -4.259  -22.457 1.00 51.27  ? 65  ASN A OD1 1 
ATOM   507  N  ND2 . ASN A 1 65  ? 40.527  -2.459  -21.140 1.00 44.27  ? 65  ASN A ND2 1 
ATOM   508  N  N   . PHE A 1 66  ? 36.090  -4.670  -19.059 1.00 40.16  ? 66  PHE A N   1 
ATOM   509  C  CA  . PHE A 1 66  ? 34.654  -4.815  -18.696 1.00 41.28  ? 66  PHE A CA  1 
ATOM   510  C  C   . PHE A 1 66  ? 34.490  -4.885  -17.173 1.00 43.65  ? 66  PHE A C   1 
ATOM   511  O  O   . PHE A 1 66  ? 34.871  -5.915  -16.589 1.00 44.02  ? 66  PHE A O   1 
ATOM   512  C  CB  . PHE A 1 66  ? 34.088  -6.102  -19.295 1.00 38.98  ? 66  PHE A CB  1 
ATOM   513  C  CG  . PHE A 1 66  ? 34.164  -6.162  -20.796 1.00 40.86  ? 66  PHE A CG  1 
ATOM   514  C  CD1 . PHE A 1 66  ? 33.222  -5.517  -21.585 1.00 41.14  ? 66  PHE A CD1 1 
ATOM   515  C  CD2 . PHE A 1 66  ? 35.173  -6.881  -21.421 1.00 42.56  ? 66  PHE A CD2 1 
ATOM   516  C  CE1 . PHE A 1 66  ? 33.298  -5.586  -22.973 1.00 42.59  ? 66  PHE A CE1 1 
ATOM   517  C  CE2 . PHE A 1 66  ? 35.237  -6.965  -22.806 1.00 41.55  ? 66  PHE A CE2 1 
ATOM   518  C  CZ  . PHE A 1 66  ? 34.316  -6.301  -23.579 1.00 41.78  ? 66  PHE A CZ  1 
ATOM   519  N  N   . LEU A 1 67  ? 33.916  -3.843  -16.571 1.00 44.74  ? 67  LEU A N   1 
ATOM   520  C  CA  . LEU A 1 67  ? 33.503  -3.805  -15.139 1.00 46.12  ? 67  LEU A CA  1 
ATOM   521  C  C   . LEU A 1 67  ? 32.026  -4.218  -15.015 1.00 40.86  ? 67  LEU A C   1 
ATOM   522  O  O   . LEU A 1 67  ? 31.125  -3.463  -15.467 1.00 44.47  ? 67  LEU A O   1 
ATOM   523  C  CB  . LEU A 1 67  ? 33.808  -2.406  -14.591 1.00 54.10  ? 67  LEU A CB  1 
ATOM   524  C  CG  . LEU A 1 67  ? 35.280  -2.001  -14.780 1.00 69.67  ? 67  LEU A CG  1 
ATOM   525  C  CD1 . LEU A 1 67  ? 35.521  -0.519  -14.520 1.00 74.02  ? 67  LEU A CD1 1 
ATOM   526  C  CD2 . LEU A 1 67  ? 36.218  -2.861  -13.926 1.00 73.66  ? 67  LEU A CD2 1 
ATOM   527  N  N   . VAL A 1 68  ? 31.799  -5.426  -14.506 1.00 36.04  ? 68  VAL A N   1 
ATOM   528  C  CA  . VAL A 1 68  ? 30.451  -6.007  -14.236 1.00 37.19  ? 68  VAL A CA  1 
ATOM   529  C  C   . VAL A 1 68  ? 30.204  -5.970  -12.727 1.00 42.14  ? 68  VAL A C   1 
ATOM   530  O  O   . VAL A 1 68  ? 31.087  -6.385  -11.976 1.00 38.60  ? 68  VAL A O   1 
ATOM   531  C  CB  . VAL A 1 68  ? 30.295  -7.443  -14.752 1.00 34.42  ? 68  VAL A CB  1 
ATOM   532  C  CG1 . VAL A 1 68  ? 28.894  -7.961  -14.451 1.00 38.66  ? 68  VAL A CG1 1 
ATOM   533  C  CG2 . VAL A 1 68  ? 30.601  -7.557  -16.234 1.00 35.86  ? 68  VAL A CG2 1 
ATOM   534  N  N   . GLN A 1 69  ? 28.998  -5.571  -12.336 1.00 41.65  ? 69  GLN A N   1 
ATOM   535  C  CA  . GLN A 1 69  ? 28.635  -5.223  -10.945 1.00 40.63  ? 69  GLN A CA  1 
ATOM   536  C  C   . GLN A 1 69  ? 27.214  -5.732  -10.687 1.00 39.22  ? 69  GLN A C   1 
ATOM   537  O  O   . GLN A 1 69  ? 26.272  -5.301  -11.419 1.00 33.86  ? 69  GLN A O   1 
ATOM   538  C  CB  . GLN A 1 69  ? 28.770  -3.712  -10.774 1.00 43.67  ? 69  GLN A CB  1 
ATOM   539  C  CG  . GLN A 1 69  ? 29.553  -3.294  -9.540  1.00 52.17  ? 69  GLN A CG  1 
ATOM   540  C  CD  . GLN A 1 69  ? 29.639  -1.790  -9.425  1.00 54.79  ? 69  GLN A CD  1 
ATOM   541  O  OE1 . GLN A 1 69  ? 29.055  -1.188  -8.531  1.00 64.14  ? 69  GLN A OE1 1 
ATOM   542  N  NE2 . GLN A 1 69  ? 30.336  -1.165  -10.357 1.00 53.88  ? 69  GLN A NE2 1 
ATOM   543  N  N   . ALA A 1 70  ? 27.073  -6.664  -9.738  1.00 40.08  ? 70  ALA A N   1 
ATOM   544  C  CA  . ALA A 1 70  ? 25.783  -7.204  -9.254  1.00 39.10  ? 70  ALA A CA  1 
ATOM   545  C  C   . ALA A 1 70  ? 25.585  -6.668  -7.834  1.00 46.48  ? 70  ALA A C   1 
ATOM   546  O  O   . ALA A 1 70  ? 26.336  -7.097  -6.922  1.00 47.08  ? 70  ALA A O   1 
ATOM   547  C  CB  . ALA A 1 70  ? 25.772  -8.709  -9.344  1.00 38.49  ? 70  ALA A CB  1 
ATOM   548  N  N   . GLY A 1 71  ? 24.671  -5.701  -7.685  1.00 45.93  ? 71  GLY A N   1 
ATOM   549  C  CA  . GLY A 1 71  ? 24.516  -4.863  -6.484  1.00 50.74  ? 71  GLY A CA  1 
ATOM   550  C  C   . GLY A 1 71  ? 25.810  -4.146  -6.152  1.00 58.14  ? 71  GLY A C   1 
ATOM   551  O  O   . GLY A 1 71  ? 26.127  -3.146  -6.815  1.00 66.17  ? 71  GLY A O   1 
ATOM   552  N  N   . ASN A 1 72  ? 26.558  -4.668  -5.181  1.00 65.44  ? 72  ASN A N   1 
ATOM   553  C  CA  . ASN A 1 72  ? 27.891  -4.142  -4.785  1.00 69.00  ? 72  ASN A CA  1 
ATOM   554  C  C   . ASN A 1 72  ? 29.009  -5.084  -5.243  1.00 64.80  ? 72  ASN A C   1 
ATOM   555  O  O   . ASN A 1 72  ? 30.124  -4.592  -5.480  1.00 70.82  ? 72  ASN A O   1 
ATOM   556  C  CB  . ASN A 1 72  ? 27.969  -3.915  -3.277  1.00 71.07  ? 72  ASN A CB  1 
ATOM   557  C  CG  . ASN A 1 72  ? 27.796  -2.460  -2.901  1.00 74.96  ? 72  ASN A CG  1 
ATOM   558  O  OD1 . ASN A 1 72  ? 27.745  -1.586  -3.767  1.00 78.62  ? 72  ASN A OD1 1 
ATOM   559  N  ND2 . ASN A 1 72  ? 27.724  -2.195  -1.608  1.00 73.23  ? 72  ASN A ND2 1 
ATOM   560  N  N   . VAL A 1 73  ? 28.725  -6.381  -5.351  1.00 58.65  ? 73  VAL A N   1 
ATOM   561  C  CA  . VAL A 1 73  ? 29.696  -7.420  -5.806  1.00 52.68  ? 73  VAL A CA  1 
ATOM   562  C  C   . VAL A 1 73  ? 30.174  -7.070  -7.222  1.00 55.02  ? 73  VAL A C   1 
ATOM   563  O  O   . VAL A 1 73  ? 29.299  -6.927  -8.107  1.00 48.18  ? 73  VAL A O   1 
ATOM   564  C  CB  . VAL A 1 73  ? 29.051  -8.816  -5.793  1.00 48.14  ? 73  VAL A CB  1 
ATOM   565  C  CG1 . VAL A 1 73  ? 29.978  -9.882  -6.370  1.00 48.49  ? 73  VAL A CG1 1 
ATOM   566  C  CG2 . VAL A 1 73  ? 28.564  -9.198  -4.403  1.00 49.53  ? 73  VAL A CG2 1 
ATOM   567  N  N   . GLN A 1 74  ? 31.492  -6.941  -7.425  1.00 49.02  ? 74  GLN A N   1 
ATOM   568  C  CA  . GLN A 1 74  ? 32.121  -6.981  -8.771  1.00 48.03  ? 74  GLN A CA  1 
ATOM   569  C  C   . GLN A 1 74  ? 32.201  -8.441  -9.207  1.00 44.86  ? 74  GLN A C   1 
ATOM   570  O  O   . GLN A 1 74  ? 32.630  -9.250  -8.413  1.00 46.15  ? 74  GLN A O   1 
ATOM   571  C  CB  . GLN A 1 74  ? 33.517  -6.364  -8.766  1.00 53.02  ? 74  GLN A CB  1 
ATOM   572  C  CG  . GLN A 1 74  ? 33.519  -4.868  -8.508  1.00 61.68  ? 74  GLN A CG  1 
ATOM   573  C  CD  . GLN A 1 74  ? 34.856  -4.248  -8.844  1.00 73.09  ? 74  GLN A CD  1 
ATOM   574  O  OE1 . GLN A 1 74  ? 35.664  -4.811  -9.589  1.00 71.88  ? 74  GLN A OE1 1 
ATOM   575  N  NE2 . GLN A 1 74  ? 35.099  -3.066  -8.293  1.00 81.85  ? 74  GLN A NE2 1 
ATOM   576  N  N   . LEU A 1 75  ? 31.750  -8.767  -10.412 1.00 44.72  ? 75  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 75  ? 31.983  -10.088 -11.042 1.00 45.03  ? 75  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 75  ? 33.271  -9.986  -11.859 1.00 45.36  ? 75  LEU A C   1 
ATOM   579  O  O   . LEU A 1 75  ? 33.519  -8.936  -12.458 1.00 53.00  ? 75  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 75  ? 30.800  -10.471 -11.935 1.00 48.79  ? 75  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 75  ? 29.486  -10.771 -11.219 1.00 53.28  ? 75  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 75  ? 28.353  -10.897 -12.220 1.00 52.50  ? 75  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 75  ? 29.600  -12.042 -10.387 1.00 54.93  ? 75  LEU A CD2 1 
ATOM   584  N  N   . ARG A 1 76  ? 34.060  -11.045 -11.864 1.00 43.72  ? 76  ARG A N   1 
ATOM   585  C  CA  . ARG A 1 76  ? 35.301  -11.126 -12.666 1.00 48.27  ? 76  ARG A CA  1 
ATOM   586  C  C   . ARG A 1 76  ? 34.920  -11.705 -14.030 1.00 40.37  ? 76  ARG A C   1 
ATOM   587  O  O   . ARG A 1 76  ? 34.367  -12.824 -14.061 1.00 41.20  ? 76  ARG A O   1 
ATOM   588  C  CB  . ARG A 1 76  ? 36.345  -11.982 -11.941 1.00 50.80  ? 76  ARG A CB  1 
ATOM   589  C  CG  . ARG A 1 76  ? 37.727  -11.980 -12.584 1.00 58.42  ? 76  ARG A CG  1 
ATOM   590  C  CD  . ARG A 1 76  ? 38.850  -12.450 -11.663 1.00 61.25  ? 76  ARG A CD  1 
ATOM   591  N  NE  . ARG A 1 76  ? 39.573  -13.585 -12.232 1.00 63.73  ? 76  ARG A NE  1 
ATOM   592  C  CZ  . ARG A 1 76  ? 39.349  -14.866 -11.933 1.00 70.37  ? 76  ARG A CZ  1 
ATOM   593  N  NH1 . ARG A 1 76  ? 38.415  -15.209 -11.056 1.00 65.23  ? 76  ARG A NH1 1 
ATOM   594  N  NH2 . ARG A 1 76  ? 40.072  -15.808 -12.517 1.00 75.82  ? 76  ARG A NH2 1 
ATOM   595  N  N   . VAL A 1 77  ? 35.180  -10.955 -15.101 1.00 37.53  ? 77  VAL A N   1 
ATOM   596  C  CA  . VAL A 1 77  ? 35.025  -11.440 -16.507 1.00 36.88  ? 77  VAL A CA  1 
ATOM   597  C  C   . VAL A 1 77  ? 36.240  -12.327 -16.835 1.00 35.61  ? 77  VAL A C   1 
ATOM   598  O  O   . VAL A 1 77  ? 37.365  -11.857 -16.664 1.00 35.98  ? 77  VAL A O   1 
ATOM   599  C  CB  . VAL A 1 77  ? 34.873  -10.252 -17.484 1.00 38.98  ? 77  VAL A CB  1 
ATOM   600  C  CG1 . VAL A 1 77  ? 34.790  -10.710 -18.938 1.00 38.18  ? 77  VAL A CG1 1 
ATOM   601  C  CG2 . VAL A 1 77  ? 33.689  -9.365  -17.117 1.00 39.34  ? 77  VAL A CG2 1 
ATOM   602  N  N   . ILE A 1 78  ? 36.006  -13.560 -17.277 1.00 40.06  ? 78  ILE A N   1 
ATOM   603  C  CA  . ILE A 1 78  ? 37.060  -14.560 -17.621 1.00 45.65  ? 78  ILE A CA  1 
ATOM   604  C  C   . ILE A 1 78  ? 36.995  -14.908 -19.116 1.00 47.75  ? 78  ILE A C   1 
ATOM   605  O  O   . ILE A 1 78  ? 37.767  -15.767 -19.562 1.00 43.09  ? 78  ILE A O   1 
ATOM   606  C  CB  . ILE A 1 78  ? 36.926  -15.802 -16.717 1.00 46.08  ? 78  ILE A CB  1 
ATOM   607  C  CG1 . ILE A 1 78  ? 35.653  -16.608 -16.996 1.00 46.43  ? 78  ILE A CG1 1 
ATOM   608  C  CG2 . ILE A 1 78  ? 37.024  -15.383 -15.261 1.00 46.16  ? 78  ILE A CG2 1 
ATOM   609  C  CD1 . ILE A 1 78  ? 35.638  -17.973 -16.336 1.00 47.10  ? 78  ILE A CD1 1 
ATOM   610  N  N   . GLY A 1 79  ? 36.148  -14.226 -19.889 1.00 45.22  ? 79  GLY A N   1 
ATOM   611  C  CA  . GLY A 1 79  ? 35.939  -14.553 -21.313 1.00 43.52  ? 79  GLY A CA  1 
ATOM   612  C  C   . GLY A 1 79  ? 34.956  -13.591 -21.945 1.00 42.83  ? 79  GLY A C   1 
ATOM   613  O  O   . GLY A 1 79  ? 34.195  -12.941 -21.216 1.00 41.54  ? 79  GLY A O   1 
ATOM   614  N  N   . HIS A 1 80  ? 34.994  -13.457 -23.260 1.00 45.77  ? 80  HIS A N   1 
ATOM   615  C  CA  . HIS A 1 80  ? 34.022  -12.625 -24.007 1.00 42.42  ? 80  HIS A CA  1 
ATOM   616  C  C   . HIS A 1 80  ? 33.960  -13.141 -25.434 1.00 41.42  ? 80  HIS A C   1 
ATOM   617  O  O   . HIS A 1 80  ? 34.993  -13.617 -25.935 1.00 35.52  ? 80  HIS A O   1 
ATOM   618  C  CB  . HIS A 1 80  ? 34.358  -11.139 -23.901 1.00 42.55  ? 80  HIS A CB  1 
ATOM   619  C  CG  . HIS A 1 80  ? 35.639  -10.745 -24.553 1.00 51.47  ? 80  HIS A CG  1 
ATOM   620  N  ND1 . HIS A 1 80  ? 36.772  -10.459 -23.822 1.00 53.04  ? 80  HIS A ND1 1 
ATOM   621  C  CD2 . HIS A 1 80  ? 35.964  -10.552 -25.852 1.00 48.26  ? 80  HIS A CD2 1 
ATOM   622  C  CE1 . HIS A 1 80  ? 37.742  -10.101 -24.643 1.00 55.77  ? 80  HIS A CE1 1 
ATOM   623  N  NE2 . HIS A 1 80  ? 37.268  -10.143 -25.890 1.00 51.03  ? 80  HIS A NE2 1 
ATOM   624  N  N   . SER A 1 81  ? 32.754  -13.173 -25.985 1.00 37.48  ? 81  SER A N   1 
ATOM   625  C  CA  . SER A 1 81  ? 32.483  -13.435 -27.414 1.00 36.07  ? 81  SER A CA  1 
ATOM   626  C  C   . SER A 1 81  ? 31.288  -12.591 -27.824 1.00 35.55  ? 81  SER A C   1 
ATOM   627  O  O   . SER A 1 81  ? 30.526  -12.134 -26.951 1.00 36.35  ? 81  SER A O   1 
ATOM   628  C  CB  . SER A 1 81  ? 32.253  -14.896 -27.689 1.00 38.37  ? 81  SER A CB  1 
ATOM   629  O  OG  . SER A 1 81  ? 30.957  -15.311 -27.286 1.00 37.06  ? 81  SER A OG  1 
ATOM   630  N  N   . MET A 1 82  ? 31.114  -12.444 -29.120 1.00 34.84  ? 82  MET A N   1 
ATOM   631  C  CA  . MET A 1 82  ? 30.024  -11.661 -29.717 1.00 35.24  ? 82  MET A CA  1 
ATOM   632  C  C   . MET A 1 82  ? 29.136  -12.649 -30.449 1.00 33.56  ? 82  MET A C   1 
ATOM   633  O  O   . MET A 1 82  ? 29.685  -13.539 -31.107 1.00 31.54  ? 82  MET A O   1 
ATOM   634  C  CB  . MET A 1 82  ? 30.630  -10.655 -30.686 1.00 37.90  ? 82  MET A CB  1 
ATOM   635  C  CG  . MET A 1 82  ? 29.638  -9.760  -31.334 1.00 40.88  ? 82  MET A CG  1 
ATOM   636  S  SD  . MET A 1 82  ? 30.477  -8.313  -31.977 1.00 36.28  ? 82  MET A SD  1 
ATOM   637  C  CE  . MET A 1 82  ? 31.670  -9.017  -33.115 1.00 39.89  ? 82  MET A CE  1 
ATOM   638  N  N   . GLN A 1 83  ? 27.823  -12.537 -30.286 1.00 31.04  ? 83  GLN A N   1 
ATOM   639  C  CA  . GLN A 1 83  ? 26.864  -13.312 -31.098 1.00 30.24  ? 83  GLN A CA  1 
ATOM   640  C  C   . GLN A 1 83  ? 25.877  -12.322 -31.718 1.00 32.08  ? 83  GLN A C   1 
ATOM   641  O  O   . GLN A 1 83  ? 25.025  -11.782 -30.967 1.00 28.35  ? 83  GLN A O   1 
ATOM   642  C  CB  . GLN A 1 83  ? 26.130  -14.346 -30.249 1.00 33.07  ? 83  GLN A CB  1 
ATOM   643  C  CG  . GLN A 1 83  ? 25.152  -15.177 -31.056 1.00 31.69  ? 83  GLN A CG  1 
ATOM   644  C  CD  . GLN A 1 83  ? 24.455  -16.158 -30.153 1.00 35.58  ? 83  GLN A CD  1 
ATOM   645  O  OE1 . GLN A 1 83  ? 24.671  -16.161 -28.946 1.00 35.74  ? 83  GLN A OE1 1 
ATOM   646  N  NE2 . GLN A 1 83  ? 23.640  -17.018 -30.742 1.00 31.99  ? 83  GLN A NE2 1 
ATOM   647  N  N   . ASN A 1 84  ? 26.001  -12.104 -33.029 1.00 28.54  ? 84  ASN A N   1 
ATOM   648  C  CA  . ASN A 1 84  ? 25.229  -11.089 -33.773 1.00 28.54  ? 84  ASN A CA  1 
ATOM   649  C  C   . ASN A 1 84  ? 25.461  -9.776  -33.037 1.00 27.01  ? 84  ASN A C   1 
ATOM   650  O  O   . ASN A 1 84  ? 26.625  -9.435  -32.886 1.00 25.74  ? 84  ASN A O   1 
ATOM   651  C  CB  . ASN A 1 84  ? 23.780  -11.544 -33.900 1.00 28.92  ? 84  ASN A CB  1 
ATOM   652  C  CG  . ASN A 1 84  ? 23.711  -12.870 -34.610 1.00 29.36  ? 84  ASN A CG  1 
ATOM   653  O  OD1 . ASN A 1 84  ? 24.252  -12.975 -35.688 1.00 31.28  ? 84  ASN A OD1 1 
ATOM   654  N  ND2 . ASN A 1 84  ? 23.072  -13.875 -34.023 1.00 28.65  ? 84  ASN A ND2 1 
ATOM   655  N  N   . CYS A 1 85  ? 24.414  -9.128  -32.503 1.00 24.52  ? 85  CYS A N   1 
ATOM   656  C  CA  . CYS A 1 85  ? 24.519  -7.766  -31.912 1.00 23.27  ? 85  CYS A CA  1 
ATOM   657  C  C   . CYS A 1 85  ? 24.573  -7.817  -30.393 1.00 22.70  ? 85  CYS A C   1 
ATOM   658  O  O   . CYS A 1 85  ? 24.507  -6.769  -29.749 1.00 22.24  ? 85  CYS A O   1 
ATOM   659  C  CB  . CYS A 1 85  ? 23.353  -6.909  -32.376 1.00 24.13  ? 85  CYS A CB  1 
ATOM   660  S  SG  . CYS A 1 85  ? 23.427  -6.633  -34.157 1.00 24.19  ? 85  CYS A SG  1 
ATOM   661  N  N   . VAL A 1 86  ? 24.738  -9.010  -29.847 1.00 23.70  ? 86  VAL A N   1 
ATOM   662  C  CA  . VAL A 1 86  ? 24.797  -9.242  -28.388 1.00 26.58  ? 86  VAL A CA  1 
ATOM   663  C  C   . VAL A 1 86  ? 26.228  -9.653  -27.999 1.00 28.04  ? 86  VAL A C   1 
ATOM   664  O  O   . VAL A 1 86  ? 26.837  -10.537 -28.674 1.00 25.76  ? 86  VAL A O   1 
ATOM   665  C  CB  . VAL A 1 86  ? 23.725  -10.286 -28.030 1.00 32.58  ? 86  VAL A CB  1 
ATOM   666  C  CG1 . VAL A 1 86  ? 24.126  -11.190 -26.891 1.00 38.29  ? 86  VAL A CG1 1 
ATOM   667  C  CG2 . VAL A 1 86  ? 22.378  -9.604  -27.767 1.00 35.17  ? 86  VAL A CG2 1 
ATOM   668  N  N   . LEU A 1 87  ? 26.750  -8.983  -26.977 1.00 24.97  ? 87  LEU A N   1 
ATOM   669  C  CA  . LEU A 1 87  ? 28.019  -9.347  -26.311 1.00 26.98  ? 87  LEU A CA  1 
ATOM   670  C  C   . LEU A 1 87  ? 27.730  -10.335 -25.173 1.00 31.28  ? 87  LEU A C   1 
ATOM   671  O  O   . LEU A 1 87  ? 26.704  -10.144 -24.449 1.00 28.01  ? 87  LEU A O   1 
ATOM   672  C  CB  . LEU A 1 87  ? 28.648  -8.064  -25.780 1.00 27.37  ? 87  LEU A CB  1 
ATOM   673  C  CG  . LEU A 1 87  ? 29.976  -8.262  -25.064 1.00 32.74  ? 87  LEU A CG  1 
ATOM   674  C  CD1 . LEU A 1 87  ? 31.046  -8.725  -26.039 1.00 36.73  ? 87  LEU A CD1 1 
ATOM   675  C  CD2 . LEU A 1 87  ? 30.392  -6.977  -24.361 1.00 33.77  ? 87  LEU A CD2 1 
ATOM   676  N  N   . LYS A 1 88  ? 28.574  -11.363 -25.038 1.00 30.90  ? 88  LYS A N   1 
ATOM   677  C  CA  . LYS A 1 88  ? 28.495  -12.395 -23.977 1.00 33.35  ? 88  LYS A CA  1 
ATOM   678  C  C   . LYS A 1 88  ? 29.794  -12.388 -23.176 1.00 34.73  ? 88  LYS A C   1 
ATOM   679  O  O   . LYS A 1 88  ? 30.821  -12.794 -23.717 1.00 36.05  ? 88  LYS A O   1 
ATOM   680  C  CB  . LYS A 1 88  ? 28.181  -13.746 -24.612 1.00 33.27  ? 88  LYS A CB  1 
ATOM   681  C  CG  . LYS A 1 88  ? 26.891  -13.705 -25.416 1.00 37.50  ? 88  LYS A CG  1 
ATOM   682  C  CD  . LYS A 1 88  ? 26.289  -15.037 -25.755 1.00 37.83  ? 88  LYS A CD  1 
ATOM   683  C  CE  . LYS A 1 88  ? 27.133  -15.796 -26.736 1.00 40.84  ? 88  LYS A CE  1 
ATOM   684  N  NZ  . LYS A 1 88  ? 26.388  -16.942 -27.297 1.00 44.21  ? 88  LYS A NZ  1 
ATOM   685  N  N   . LEU A 1 89  ? 29.714  -11.889 -21.943 1.00 34.45  ? 89  LEU A N   1 
ATOM   686  C  CA  . LEU A 1 89  ? 30.808  -11.816 -20.961 1.00 32.90  ? 89  LEU A CA  1 
ATOM   687  C  C   . LEU A 1 89  ? 30.727  -13.051 -20.067 1.00 37.32  ? 89  LEU A C   1 
ATOM   688  O  O   . LEU A 1 89  ? 29.703  -13.191 -19.331 1.00 38.17  ? 89  LEU A O   1 
ATOM   689  C  CB  . LEU A 1 89  ? 30.644  -10.540 -20.148 1.00 31.83  ? 89  LEU A CB  1 
ATOM   690  C  CG  . LEU A 1 89  ? 30.594  -9.259  -20.960 1.00 30.82  ? 89  LEU A CG  1 
ATOM   691  C  CD1 . LEU A 1 89  ? 30.554  -8.062  -20.029 1.00 32.48  ? 89  LEU A CD1 1 
ATOM   692  C  CD2 . LEU A 1 89  ? 31.804  -9.164  -21.878 1.00 33.77  ? 89  LEU A CD2 1 
ATOM   693  N  N   . LYS A 1 90  ? 31.725  -13.937 -20.166 1.00 38.54  ? 90  LYS A N   1 
ATOM   694  C  CA  . LYS A 1 90  ? 31.816  -15.119 -19.278 1.00 40.88  ? 90  LYS A CA  1 
ATOM   695  C  C   . LYS A 1 90  ? 32.384  -14.609 -17.954 1.00 40.07  ? 90  LYS A C   1 
ATOM   696  O  O   . LYS A 1 90  ? 33.297  -13.727 -17.972 1.00 36.18  ? 90  LYS A O   1 
ATOM   697  C  CB  . LYS A 1 90  ? 32.599  -16.269 -19.911 1.00 46.46  ? 90  LYS A CB  1 
ATOM   698  C  CG  . LYS A 1 90  ? 32.321  -17.612 -19.264 1.00 49.83  ? 90  LYS A CG  1 
ATOM   699  C  CD  . LYS A 1 90  ? 33.064  -18.754 -19.899 1.00 60.86  ? 90  LYS A CD  1 
ATOM   700  C  CE  . LYS A 1 90  ? 32.769  -20.077 -19.222 1.00 63.97  ? 90  LYS A CE  1 
ATOM   701  N  NZ  . LYS A 1 90  ? 33.788  -21.102 -19.555 1.00 68.32  ? 90  LYS A NZ  1 
ATOM   702  N  N   . VAL A 1 91  ? 31.774  -15.039 -16.849 1.00 37.80  ? 91  VAL A N   1 
ATOM   703  C  CA  . VAL A 1 91  ? 32.178  -14.609 -15.486 1.00 38.26  ? 91  VAL A CA  1 
ATOM   704  C  C   . VAL A 1 91  ? 32.437  -15.869 -14.665 1.00 37.95  ? 91  VAL A C   1 
ATOM   705  O  O   . VAL A 1 91  ? 32.009  -16.956 -15.116 1.00 37.57  ? 91  VAL A O   1 
ATOM   706  C  CB  . VAL A 1 91  ? 31.142  -13.656 -14.865 1.00 40.84  ? 91  VAL A CB  1 
ATOM   707  C  CG1 . VAL A 1 91  ? 31.049  -12.373 -15.682 1.00 43.74  ? 91  VAL A CG1 1 
ATOM   708  C  CG2 . VAL A 1 91  ? 29.767  -14.299 -14.718 1.00 39.65  ? 91  VAL A CG2 1 
ATOM   709  N  N   . ASP A 1 92  ? 33.180  -15.721 -13.566 1.00 45.03  ? 92  ASP A N   1 
ATOM   710  C  CA  . ASP A 1 92  ? 33.698  -16.852 -12.739 1.00 52.41  ? 92  ASP A CA  1 
ATOM   711  C  C   . ASP A 1 92  ? 32.609  -17.393 -11.797 1.00 53.65  ? 92  ASP A C   1 
ATOM   712  O  O   . ASP A 1 92  ? 32.768  -18.548 -11.357 1.00 56.50  ? 92  ASP A O   1 
ATOM   713  C  CB  . ASP A 1 92  ? 34.957  -16.457 -11.962 1.00 51.85  ? 92  ASP A CB  1 
ATOM   714  C  CG  . ASP A 1 92  ? 34.795  -15.246 -11.062 1.00 56.20  ? 92  ASP A CG  1 
ATOM   715  O  OD1 . ASP A 1 92  ? 33.716  -14.606 -11.091 1.00 61.19  ? 92  ASP A OD1 1 
ATOM   716  O  OD2 . ASP A 1 92  ? 35.755  -14.942 -10.338 1.00 58.58  ? 92  ASP A OD2 1 
ATOM   717  N  N   . THR A 1 93  ? 31.542  -16.624 -11.527 1.00 47.40  ? 93  THR A N   1 
ATOM   718  C  CA  . THR A 1 93  ? 30.379  -17.048 -10.695 1.00 42.21  ? 93  THR A CA  1 
ATOM   719  C  C   . THR A 1 93  ? 29.133  -17.260 -11.566 1.00 40.46  ? 93  THR A C   1 
ATOM   720  O  O   . THR A 1 93  ? 28.802  -16.364 -12.348 1.00 37.41  ? 93  THR A O   1 
ATOM   721  C  CB  . THR A 1 93  ? 30.073  -16.004 -9.616  1.00 45.81  ? 93  THR A CB  1 
ATOM   722  O  OG1 . THR A 1 93  ? 31.286  -15.391 -9.177  1.00 44.43  ? 93  THR A OG1 1 
ATOM   723  C  CG2 . THR A 1 93  ? 29.364  -16.608 -8.423  1.00 47.73  ? 93  THR A CG2 1 
ATOM   724  N  N   . ALA A 1 94  ? 28.446  -18.389 -11.418 1.00 41.03  ? 94  ALA A N   1 
ATOM   725  C  CA  . ALA A 1 94  ? 27.100  -18.612 -11.977 1.00 42.65  ? 94  ALA A CA  1 
ATOM   726  C  C   . ALA A 1 94  ? 26.112  -17.886 -11.060 1.00 43.94  ? 94  ALA A C   1 
ATOM   727  O  O   . ALA A 1 94  ? 26.347  -17.860 -9.827  1.00 41.02  ? 94  ALA A O   1 
ATOM   728  C  CB  . ALA A 1 94  ? 26.781  -20.081 -12.094 1.00 45.61  ? 94  ALA A CB  1 
ATOM   729  N  N   . ASN A 1 95  ? 25.095  -17.252 -11.636 1.00 36.65  ? 95  ASN A N   1 
ATOM   730  C  CA  . ASN A 1 95  ? 24.093  -16.471 -10.862 1.00 36.51  ? 95  ASN A CA  1 
ATOM   731  C  C   . ASN A 1 95  ? 23.294  -17.463 -10.024 1.00 30.61  ? 95  ASN A C   1 
ATOM   732  O  O   . ASN A 1 95  ? 22.609  -18.325 -10.570 1.00 29.24  ? 95  ASN A O   1 
ATOM   733  C  CB  . ASN A 1 95  ? 23.181  -15.656 -11.786 1.00 38.69  ? 95  ASN A CB  1 
ATOM   734  C  CG  . ASN A 1 95  ? 22.279  -14.682 -11.056 1.00 38.13  ? 95  ASN A CG  1 
ATOM   735  O  OD1 . ASN A 1 95  ? 22.244  -14.669 -9.827  1.00 35.61  ? 95  ASN A OD1 1 
ATOM   736  N  ND2 . ASN A 1 95  ? 21.552  -13.865 -11.812 1.00 33.62  ? 95  ASN A ND2 1 
ATOM   737  N  N   . PRO A 1 96  ? 23.349  -17.386 -8.679  1.00 33.83  ? 96  PRO A N   1 
ATOM   738  C  CA  . PRO A 1 96  ? 22.549  -18.289 -7.847  1.00 36.88  ? 96  PRO A CA  1 
ATOM   739  C  C   . PRO A 1 96  ? 21.032  -18.037 -7.983  1.00 38.04  ? 96  PRO A C   1 
ATOM   740  O  O   . PRO A 1 96  ? 20.288  -18.938 -7.748  1.00 37.57  ? 96  PRO A O   1 
ATOM   741  C  CB  . PRO A 1 96  ? 23.115  -18.041 -6.441  1.00 35.49  ? 96  PRO A CB  1 
ATOM   742  C  CG  . PRO A 1 96  ? 23.605  -16.625 -6.475  1.00 34.21  ? 96  PRO A CG  1 
ATOM   743  C  CD  . PRO A 1 96  ? 24.114  -16.411 -7.888  1.00 33.22  ? 96  PRO A CD  1 
ATOM   744  N  N   . LYS A 1 97  ? 20.608  -16.868 -8.478  1.00 39.31  ? 97  LYS A N   1 
ATOM   745  C  CA  . LYS A 1 97  ? 19.171  -16.519 -8.693  1.00 39.72  ? 97  LYS A CA  1 
ATOM   746  C  C   . LYS A 1 97  ? 18.711  -16.867 -10.119 1.00 41.09  ? 97  LYS A C   1 
ATOM   747  O  O   . LYS A 1 97  ? 17.581  -16.460 -10.508 1.00 34.18  ? 97  LYS A O   1 
ATOM   748  C  CB  . LYS A 1 97  ? 18.966  -15.021 -8.451  1.00 42.47  ? 97  LYS A CB  1 
ATOM   749  C  CG  . LYS A 1 97  ? 19.315  -14.552 -7.046  1.00 45.50  ? 97  LYS A CG  1 
ATOM   750  C  CD  . LYS A 1 97  ? 19.146  -13.066 -6.854  1.00 49.79  ? 97  LYS A CD  1 
ATOM   751  C  CE  . LYS A 1 97  ? 19.745  -12.558 -5.561  1.00 53.63  ? 97  LYS A CE  1 
ATOM   752  N  NZ  . LYS A 1 97  ? 19.431  -11.127 -5.340  1.00 60.70  ? 97  LYS A NZ  1 
ATOM   753  N  N   . THR A 1 98  ? 19.528  -17.566 -10.910 1.00 35.34  ? 98  THR A N   1 
ATOM   754  C  CA  . THR A 1 98  ? 19.141  -17.931 -12.293 1.00 34.21  ? 98  THR A CA  1 
ATOM   755  C  C   . THR A 1 98  ? 17.825  -18.678 -12.191 1.00 33.88  ? 98  THR A C   1 
ATOM   756  O  O   . THR A 1 98  ? 17.759  -19.668 -11.484 1.00 38.90  ? 98  THR A O   1 
ATOM   757  C  CB  . THR A 1 98  ? 20.231  -18.738 -13.006 1.00 31.52  ? 98  THR A CB  1 
ATOM   758  O  OG1 . THR A 1 98  ? 21.435  -17.973 -12.944 1.00 33.57  ? 98  THR A OG1 1 
ATOM   759  C  CG2 . THR A 1 98  ? 19.898  -19.052 -14.440 1.00 31.59  ? 98  THR A CG2 1 
ATOM   760  N  N   . PRO A 1 99  ? 16.736  -18.225 -12.853 1.00 32.25  ? 99  PRO A N   1 
ATOM   761  C  CA  . PRO A 1 99  ? 15.500  -18.998 -12.904 1.00 31.49  ? 99  PRO A CA  1 
ATOM   762  C  C   . PRO A 1 99  ? 15.548  -20.065 -14.009 1.00 34.54  ? 99  PRO A C   1 
ATOM   763  O  O   . PRO A 1 99  ? 16.455  -20.038 -14.824 1.00 32.81  ? 99  PRO A O   1 
ATOM   764  C  CB  . PRO A 1 99  ? 14.480  -17.907 -13.267 1.00 32.61  ? 99  PRO A CB  1 
ATOM   765  C  CG  . PRO A 1 99  ? 15.260  -17.013 -14.220 1.00 30.91  ? 99  PRO A CG  1 
ATOM   766  C  CD  . PRO A 1 99  ? 16.635  -16.955 -13.596 1.00 32.05  ? 99  PRO A CD  1 
ATOM   767  N  N   . LYS A 1 100 ? 14.538  -20.927 -14.077 1.00 34.85  ? 100 LYS A N   1 
ATOM   768  C  CA  . LYS A 1 100 ? 14.299  -21.712 -15.307 1.00 36.55  ? 100 LYS A CA  1 
ATOM   769  C  C   . LYS A 1 100 ? 14.089  -20.691 -16.423 1.00 35.87  ? 100 LYS A C   1 
ATOM   770  O  O   . LYS A 1 100 ? 13.317  -19.748 -16.209 1.00 32.84  ? 100 LYS A O   1 
ATOM   771  C  CB  . LYS A 1 100 ? 13.066  -22.605 -15.192 1.00 44.13  ? 100 LYS A CB  1 
ATOM   772  C  CG  . LYS A 1 100 ? 13.160  -23.772 -14.216 1.00 55.01  ? 100 LYS A CG  1 
ATOM   773  C  CD  . LYS A 1 100 ? 11.937  -24.676 -14.289 1.00 58.59  ? 100 LYS A CD  1 
ATOM   774  C  CE  . LYS A 1 100 ? 12.129  -26.029 -13.639 1.00 64.37  ? 100 LYS A CE  1 
ATOM   775  N  NZ  . LYS A 1 100 ? 11.115  -27.001 -14.123 1.00 68.25  ? 100 LYS A NZ  1 
ATOM   776  N  N   . TYR A 1 101 ? 14.762  -20.830 -17.561 1.00 36.91  ? 101 TYR A N   1 
ATOM   777  C  CA  . TYR A 1 101 ? 14.634  -19.821 -18.642 1.00 36.88  ? 101 TYR A CA  1 
ATOM   778  C  C   . TYR A 1 101 ? 14.829  -20.428 -20.024 1.00 37.19  ? 101 TYR A C   1 
ATOM   779  O  O   . TYR A 1 101 ? 15.254  -21.557 -20.179 1.00 34.30  ? 101 TYR A O   1 
ATOM   780  C  CB  . TYR A 1 101 ? 15.603  -18.663 -18.420 1.00 33.94  ? 101 TYR A CB  1 
ATOM   781  C  CG  . TYR A 1 101 ? 17.044  -18.950 -18.750 1.00 35.22  ? 101 TYR A CG  1 
ATOM   782  C  CD1 . TYR A 1 101 ? 17.907  -19.416 -17.778 1.00 35.98  ? 101 TYR A CD1 1 
ATOM   783  C  CD2 . TYR A 1 101 ? 17.550  -18.721 -20.022 1.00 35.73  ? 101 TYR A CD2 1 
ATOM   784  C  CE1 . TYR A 1 101 ? 19.252  -19.627 -18.042 1.00 39.69  ? 101 TYR A CE1 1 
ATOM   785  C  CE2 . TYR A 1 101 ? 18.888  -18.936 -20.308 1.00 36.32  ? 101 TYR A CE2 1 
ATOM   786  C  CZ  . TYR A 1 101 ? 19.739  -19.394 -19.315 1.00 36.48  ? 101 TYR A CZ  1 
ATOM   787  O  OH  . TYR A 1 101 ? 21.046  -19.626 -19.583 1.00 37.46  ? 101 TYR A OH  1 
ATOM   788  N  N   . LYS A 1 102 ? 14.485  -19.641 -21.029 1.00 36.77  ? 102 LYS A N   1 
ATOM   789  C  CA  . LYS A 1 102 ? 14.773  -19.961 -22.442 1.00 37.66  ? 102 LYS A CA  1 
ATOM   790  C  C   . LYS A 1 102 ? 14.816  -18.653 -23.218 1.00 34.33  ? 102 LYS A C   1 
ATOM   791  O  O   . LYS A 1 102 ? 14.318  -17.630 -22.694 1.00 34.48  ? 102 LYS A O   1 
ATOM   792  C  CB  . LYS A 1 102 ? 13.733  -20.905 -23.046 1.00 40.15  ? 102 LYS A CB  1 
ATOM   793  C  CG  . LYS A 1 102 ? 12.304  -20.370 -23.115 1.00 49.32  ? 102 LYS A CG  1 
ATOM   794  C  CD  . LYS A 1 102 ? 11.249  -21.437 -23.437 1.00 54.76  ? 102 LYS A CD  1 
ATOM   795  C  CE  . LYS A 1 102 ? 11.404  -22.698 -22.612 1.00 59.16  ? 102 LYS A CE  1 
ATOM   796  N  NZ  . LYS A 1 102 ? 10.101  -23.190 -22.102 1.00 69.70  ? 102 LYS A NZ  1 
ATOM   797  N  N   . PHE A 1 103 ? 15.343  -18.723 -24.431 1.00 27.34  ? 103 PHE A N   1 
ATOM   798  C  CA  . PHE A 1 103 ? 15.393  -17.600 -25.386 1.00 30.72  ? 103 PHE A CA  1 
ATOM   799  C  C   . PHE A 1 103 ? 14.405  -17.915 -26.483 1.00 31.24  ? 103 PHE A C   1 
ATOM   800  O  O   . PHE A 1 103 ? 14.507  -19.015 -27.014 1.00 35.35  ? 103 PHE A O   1 
ATOM   801  C  CB  . PHE A 1 103 ? 16.816  -17.401 -25.919 1.00 28.93  ? 103 PHE A CB  1 
ATOM   802  C  CG  . PHE A 1 103 ? 17.848  -16.995 -24.899 1.00 28.76  ? 103 PHE A CG  1 
ATOM   803  C  CD1 . PHE A 1 103 ? 17.493  -16.581 -23.625 1.00 28.75  ? 103 PHE A CD1 1 
ATOM   804  C  CD2 . PHE A 1 103 ? 19.189  -16.953 -25.242 1.00 29.85  ? 103 PHE A CD2 1 
ATOM   805  C  CE1 . PHE A 1 103 ? 18.448  -16.184 -22.711 1.00 26.63  ? 103 PHE A CE1 1 
ATOM   806  C  CE2 . PHE A 1 103 ? 20.145  -16.546 -24.326 1.00 29.81  ? 103 PHE A CE2 1 
ATOM   807  C  CZ  . PHE A 1 103 ? 19.769  -16.144 -23.066 1.00 28.97  ? 103 PHE A CZ  1 
ATOM   808  N  N   . VAL A 1 104 ? 13.469  -17.008 -26.763 1.00 31.10  ? 104 VAL A N   1 
ATOM   809  C  CA  . VAL A 1 104 ? 12.516  -17.152 -27.894 1.00 32.11  ? 104 VAL A CA  1 
ATOM   810  C  C   . VAL A 1 104 ? 12.520  -15.855 -28.701 1.00 31.60  ? 104 VAL A C   1 
ATOM   811  O  O   . VAL A 1 104 ? 12.608  -14.745 -28.111 1.00 34.85  ? 104 VAL A O   1 
ATOM   812  C  CB  . VAL A 1 104 ? 11.093  -17.529 -27.430 1.00 40.14  ? 104 VAL A CB  1 
ATOM   813  C  CG1 . VAL A 1 104 ? 11.111  -18.664 -26.417 1.00 41.22  ? 104 VAL A CG1 1 
ATOM   814  C  CG2 . VAL A 1 104 ? 10.341  -16.348 -26.851 1.00 42.41  ? 104 VAL A CG2 1 
ATOM   815  N  N   . ARG A 1 105 ? 12.436  -16.002 -30.013 1.00 26.75  ? 105 ARG A N   1 
ATOM   816  C  CA  . ARG A 1 105 ? 12.165  -14.902 -30.955 1.00 27.03  ? 105 ARG A CA  1 
ATOM   817  C  C   . ARG A 1 105 ? 10.647  -14.812 -31.152 1.00 27.94  ? 105 ARG A C   1 
ATOM   818  O  O   . ARG A 1 105 ? 10.062  -15.819 -31.516 1.00 30.29  ? 105 ARG A O   1 
ATOM   819  C  CB  . ARG A 1 105 ? 12.900  -15.157 -32.267 1.00 24.92  ? 105 ARG A CB  1 
ATOM   820  C  CG  . ARG A 1 105 ? 12.967  -13.916 -33.143 1.00 27.30  ? 105 ARG A CG  1 
ATOM   821  C  CD  . ARG A 1 105 ? 13.796  -14.086 -34.389 1.00 27.32  ? 105 ARG A CD  1 
ATOM   822  N  NE  . ARG A 1 105 ? 13.649  -12.898 -35.235 1.00 27.77  ? 105 ARG A NE  1 
ATOM   823  C  CZ  . ARG A 1 105 ? 14.328  -11.775 -35.065 1.00 26.65  ? 105 ARG A CZ  1 
ATOM   824  N  NH1 . ARG A 1 105 ? 15.188  -11.668 -34.071 1.00 26.18  ? 105 ARG A NH1 1 
ATOM   825  N  NH2 . ARG A 1 105 ? 14.159  -10.770 -35.900 1.00 27.26  ? 105 ARG A NH2 1 
ATOM   826  N  N   . ILE A 1 106 ? 10.037  -13.649 -30.929 1.00 26.97  ? 106 ILE A N   1 
ATOM   827  C  CA  . ILE A 1 106 ? 8.562   -13.469 -31.048 1.00 26.65  ? 106 ILE A CA  1 
ATOM   828  C  C   . ILE A 1 106 ? 8.266   -12.898 -32.425 1.00 26.57  ? 106 ILE A C   1 
ATOM   829  O  O   . ILE A 1 106 ? 9.212   -12.440 -33.044 1.00 27.27  ? 106 ILE A O   1 
ATOM   830  C  CB  . ILE A 1 106 ? 7.994   -12.583 -29.935 1.00 29.28  ? 106 ILE A CB  1 
ATOM   831  C  CG1 . ILE A 1 106 ? 8.643   -11.196 -29.910 1.00 30.77  ? 106 ILE A CG1 1 
ATOM   832  C  CG2 . ILE A 1 106 ? 8.105   -13.291 -28.589 1.00 29.28  ? 106 ILE A CG2 1 
ATOM   833  C  CD1 . ILE A 1 106 ? 8.033   -10.261 -28.890 1.00 32.70  ? 106 ILE A CD1 1 
ATOM   834  N  N   . GLN A 1 107 ? 7.012   -12.982 -32.871 1.00 25.13  ? 107 GLN A N   1 
ATOM   835  C  CA  . GLN A 1 107 ? 6.493   -12.353 -34.111 1.00 29.89  ? 107 GLN A CA  1 
ATOM   836  C  C   . GLN A 1 107 ? 5.701   -11.095 -33.778 1.00 28.68  ? 107 GLN A C   1 
ATOM   837  O  O   . GLN A 1 107 ? 5.173   -10.955 -32.668 1.00 28.45  ? 107 GLN A O   1 
ATOM   838  C  CB  . GLN A 1 107 ? 5.563   -13.309 -34.859 1.00 31.51  ? 107 GLN A CB  1 
ATOM   839  C  CG  . GLN A 1 107 ? 6.274   -14.562 -35.347 1.00 35.02  ? 107 GLN A CG  1 
ATOM   840  C  CD  . GLN A 1 107 ? 7.336   -14.213 -36.351 1.00 37.66  ? 107 GLN A CD  1 
ATOM   841  O  OE1 . GLN A 1 107 ? 7.060   -13.611 -37.386 1.00 43.13  ? 107 GLN A OE1 1 
ATOM   842  N  NE2 . GLN A 1 107 ? 8.564   -14.564 -36.028 1.00 36.36  ? 107 GLN A NE2 1 
ATOM   843  N  N   . PRO A 1 108 ? 5.573   -10.169 -34.761 1.00 29.55  ? 108 PRO A N   1 
ATOM   844  C  CA  . PRO A 1 108 ? 4.727   -8.988  -34.605 1.00 27.48  ? 108 PRO A CA  1 
ATOM   845  C  C   . PRO A 1 108 ? 3.340   -9.367  -34.081 1.00 26.75  ? 108 PRO A C   1 
ATOM   846  O  O   . PRO A 1 108 ? 2.771   -10.313 -34.552 1.00 24.57  ? 108 PRO A O   1 
ATOM   847  C  CB  . PRO A 1 108 ? 4.636   -8.408  -36.023 1.00 27.80  ? 108 PRO A CB  1 
ATOM   848  C  CG  . PRO A 1 108 ? 5.890   -8.873  -36.691 1.00 31.17  ? 108 PRO A CG  1 
ATOM   849  C  CD  . PRO A 1 108 ? 6.196   -10.231 -36.096 1.00 29.38  ? 108 PRO A CD  1 
ATOM   850  N  N   . GLY A 1 109 ? 2.853   -8.621  -33.100 1.00 25.42  ? 109 GLY A N   1 
ATOM   851  C  CA  . GLY A 1 109 ? 1.538   -8.841  -32.473 1.00 25.38  ? 109 GLY A CA  1 
ATOM   852  C  C   . GLY A 1 109 ? 1.661   -9.472  -31.108 1.00 23.96  ? 109 GLY A C   1 
ATOM   853  O  O   . GLY A 1 109 ? 0.739   -9.330  -30.307 1.00 24.71  ? 109 GLY A O   1 
ATOM   854  N  N   . GLN A 1 110 ? 2.757   -10.184 -30.861 1.00 25.60  ? 110 GLN A N   1 
ATOM   855  C  CA  . GLN A 1 110 ? 3.010   -10.858 -29.574 1.00 24.06  ? 110 GLN A CA  1 
ATOM   856  C  C   . GLN A 1 110 ? 3.234   -9.775  -28.512 1.00 23.86  ? 110 GLN A C   1 
ATOM   857  O  O   . GLN A 1 110 ? 3.756   -8.712  -28.822 1.00 26.18  ? 110 GLN A O   1 
ATOM   858  C  CB  . GLN A 1 110 ? 4.203   -11.797 -29.696 1.00 27.08  ? 110 GLN A CB  1 
ATOM   859  C  CG  . GLN A 1 110 ? 4.499   -12.561 -28.424 1.00 29.10  ? 110 GLN A CG  1 
ATOM   860  C  CD  . GLN A 1 110 ? 3.316   -13.392 -27.978 1.00 32.68  ? 110 GLN A CD  1 
ATOM   861  O  OE1 . GLN A 1 110 ? 2.586   -13.041 -27.043 1.00 30.60  ? 110 GLN A OE1 1 
ATOM   862  N  NE2 . GLN A 1 110 ? 3.118   -14.499 -28.674 1.00 31.19  ? 110 GLN A NE2 1 
ATOM   863  N  N   . THR A 1 111 ? 2.841   -10.061 -27.291 1.00 25.55  ? 111 THR A N   1 
ATOM   864  C  CA  . THR A 1 111 ? 3.060   -9.199  -26.117 1.00 23.83  ? 111 THR A CA  1 
ATOM   865  C  C   . THR A 1 111 ? 4.155   -9.774  -25.216 1.00 23.98  ? 111 THR A C   1 
ATOM   866  O  O   . THR A 1 111 ? 4.433   -10.994 -25.242 1.00 24.87  ? 111 THR A O   1 
ATOM   867  C  CB  . THR A 1 111 ? 1.735   -9.014  -25.371 1.00 23.80  ? 111 THR A CB  1 
ATOM   868  O  OG1 . THR A 1 111 ? 1.266   -10.320 -25.022 1.00 23.89  ? 111 THR A OG1 1 
ATOM   869  C  CG2 . THR A 1 111 ? 0.730   -8.243  -26.193 1.00 24.38  ? 111 THR A CG2 1 
ATOM   870  N  N   . PHE A 1 112 ? 4.749   -8.903  -24.403 1.00 22.55  ? 112 PHE A N   1 
ATOM   871  C  CA  . PHE A 1 112 ? 5.698   -9.285  -23.343 1.00 22.76  ? 112 PHE A CA  1 
ATOM   872  C  C   . PHE A 1 112 ? 5.721   -8.177  -22.287 1.00 21.86  ? 112 PHE A C   1 
ATOM   873  O  O   . PHE A 1 112 ? 5.230   -7.012  -22.543 1.00 20.75  ? 112 PHE A O   1 
ATOM   874  C  CB  . PHE A 1 112 ? 7.070   -9.592  -23.954 1.00 22.94  ? 112 PHE A CB  1 
ATOM   875  C  CG  . PHE A 1 112 ? 7.640   -8.497  -24.815 1.00 23.34  ? 112 PHE A CG  1 
ATOM   876  C  CD1 . PHE A 1 112 ? 7.283   -8.377  -26.154 1.00 26.92  ? 112 PHE A CD1 1 
ATOM   877  C  CD2 . PHE A 1 112 ? 8.521   -7.580  -24.285 1.00 25.46  ? 112 PHE A CD2 1 
ATOM   878  C  CE1 . PHE A 1 112 ? 7.842   -7.397  -26.957 1.00 27.07  ? 112 PHE A CE1 1 
ATOM   879  C  CE2 . PHE A 1 112 ? 9.048   -6.571  -25.074 1.00 26.28  ? 112 PHE A CE2 1 
ATOM   880  C  CZ  . PHE A 1 112 ? 8.718   -6.487  -26.408 1.00 28.26  ? 112 PHE A CZ  1 
ATOM   881  N  N   . SER A 1 113 ? 6.307   -8.516  -21.143 1.00 20.87  ? 113 SER A N   1 
ATOM   882  C  CA  . SER A 1 113 ? 6.636   -7.550  -20.069 1.00 22.85  ? 113 SER A CA  1 
ATOM   883  C  C   . SER A 1 113 ? 8.050   -7.008  -20.263 1.00 23.11  ? 113 SER A C   1 
ATOM   884  O  O   . SER A 1 113 ? 8.942   -7.780  -20.619 1.00 24.06  ? 113 SER A O   1 
ATOM   885  C  CB  . SER A 1 113 ? 6.461   -8.166  -18.711 1.00 24.84  ? 113 SER A CB  1 
ATOM   886  O  OG  . SER A 1 113 ? 5.140   -8.651  -18.581 1.00 24.87  ? 113 SER A OG  1 
ATOM   887  N  N   . VAL A 1 114 ? 8.238   -5.718  -19.993 1.00 21.97  ? 114 VAL A N   1 
ATOM   888  C  CA  . VAL A 1 114 ? 9.569   -5.068  -20.019 1.00 21.92  ? 114 VAL A CA  1 
ATOM   889  C  C   . VAL A 1 114 ? 9.916   -4.662  -18.594 1.00 21.04  ? 114 VAL A C   1 
ATOM   890  O  O   . VAL A 1 114 ? 9.089   -4.025  -17.974 1.00 22.92  ? 114 VAL A O   1 
ATOM   891  C  CB  . VAL A 1 114 ? 9.594   -3.867  -20.982 1.00 21.98  ? 114 VAL A CB  1 
ATOM   892  C  CG1 . VAL A 1 114 ? 10.884  -3.078  -20.844 1.00 20.78  ? 114 VAL A CG1 1 
ATOM   893  C  CG2 . VAL A 1 114 ? 9.378   -4.308  -22.419 1.00 22.99  ? 114 VAL A CG2 1 
ATOM   894  N  N   . LEU A 1 115 ? 11.113  -5.016  -18.133 1.00 21.14  ? 115 LEU A N   1 
ATOM   895  C  CA  . LEU A 1 115 ? 11.679  -4.537  -16.853 1.00 21.49  ? 115 LEU A CA  1 
ATOM   896  C  C   . LEU A 1 115 ? 12.655  -3.408  -17.183 1.00 23.17  ? 115 LEU A C   1 
ATOM   897  O  O   . LEU A 1 115 ? 13.801  -3.709  -17.605 1.00 23.44  ? 115 LEU A O   1 
ATOM   898  C  CB  . LEU A 1 115 ? 12.362  -5.690  -16.103 1.00 22.12  ? 115 LEU A CB  1 
ATOM   899  C  CG  . LEU A 1 115 ? 12.922  -5.310  -14.727 1.00 23.22  ? 115 LEU A CG  1 
ATOM   900  C  CD1 . LEU A 1 115 ? 11.824  -4.810  -13.816 1.00 23.26  ? 115 LEU A CD1 1 
ATOM   901  C  CD2 . LEU A 1 115 ? 13.649  -6.475  -14.081 1.00 24.26  ? 115 LEU A CD2 1 
ATOM   902  N  N   . ALA A 1 116 ? 12.185  -2.153  -17.146 1.00 23.13  ? 116 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 116 ? 13.052  -0.982  -17.414 1.00 23.53  ? 116 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 116 ? 14.052  -0.819  -16.247 1.00 24.81  ? 116 ALA A C   1 
ATOM   905  O  O   . ALA A 1 116 ? 13.605  -0.861  -15.084 1.00 21.51  ? 116 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 116 ? 12.225  0.266   -17.625 1.00 22.75  ? 116 ALA A CB  1 
ATOM   907  N  N   . CYS A 1 117 ? 15.348  -0.673  -16.558 1.00 25.84  ? 117 CYS A N   1 
ATOM   908  C  CA  . CYS A 1 117 ? 16.490  -0.745  -15.596 1.00 31.20  ? 117 CYS A CA  1 
ATOM   909  C  C   . CYS A 1 117 ? 17.552  0.302   -15.923 1.00 31.74  ? 117 CYS A C   1 
ATOM   910  O  O   . CYS A 1 117 ? 17.755  0.585   -17.110 1.00 31.34  ? 117 CYS A O   1 
ATOM   911  C  CB  . CYS A 1 117 ? 17.227  -2.077  -15.624 1.00 33.30  ? 117 CYS A CB  1 
ATOM   912  S  SG  . CYS A 1 117 ? 16.212  -3.486  -15.120 1.00 38.01  ? 117 CYS A SG  1 
ATOM   913  N  N   . TYR A 1 118 ? 18.197  0.841   -14.889 1.00 33.34  ? 118 TYR A N   1 
ATOM   914  C  CA  . TYR A 1 118 ? 19.237  1.908   -14.978 1.00 35.07  ? 118 TYR A CA  1 
ATOM   915  C  C   . TYR A 1 118 ? 20.361  1.566   -14.004 1.00 36.49  ? 118 TYR A C   1 
ATOM   916  O  O   . TYR A 1 118 ? 20.035  1.297   -12.818 1.00 33.30  ? 118 TYR A O   1 
ATOM   917  C  CB  . TYR A 1 118 ? 18.633  3.275   -14.673 1.00 33.33  ? 118 TYR A CB  1 
ATOM   918  C  CG  . TYR A 1 118 ? 17.546  3.629   -15.655 1.00 35.85  ? 118 TYR A CG  1 
ATOM   919  C  CD1 . TYR A 1 118 ? 17.855  4.244   -16.862 1.00 32.43  ? 118 TYR A CD1 1 
ATOM   920  C  CD2 . TYR A 1 118 ? 16.230  3.250   -15.433 1.00 35.42  ? 118 TYR A CD2 1 
ATOM   921  C  CE1 . TYR A 1 118 ? 16.872  4.525   -17.793 1.00 36.25  ? 118 TYR A CE1 1 
ATOM   922  C  CE2 . TYR A 1 118 ? 15.235  3.533   -16.356 1.00 35.39  ? 118 TYR A CE2 1 
ATOM   923  C  CZ  . TYR A 1 118 ? 15.560  4.167   -17.542 1.00 33.67  ? 118 TYR A CZ  1 
ATOM   924  O  OH  . TYR A 1 118 ? 14.617  4.431   -18.493 1.00 31.95  ? 118 TYR A OH  1 
ATOM   925  N  N   . ASN A 1 119 ? 21.603  1.493   -14.511 1.00 36.16  ? 119 ASN A N   1 
ATOM   926  C  CA  . ASN A 1 119 ? 22.802  1.135   -13.708 1.00 37.65  ? 119 ASN A CA  1 
ATOM   927  C  C   . ASN A 1 119 ? 22.567  -0.230  -13.068 1.00 35.38  ? 119 ASN A C   1 
ATOM   928  O  O   . ASN A 1 119 ? 22.982  -0.421  -11.918 1.00 37.30  ? 119 ASN A O   1 
ATOM   929  C  CB  . ASN A 1 119 ? 23.078  2.204   -12.653 1.00 36.94  ? 119 ASN A CB  1 
ATOM   930  C  CG  . ASN A 1 119 ? 23.433  3.533   -13.278 1.00 40.75  ? 119 ASN A CG  1 
ATOM   931  O  OD1 . ASN A 1 119 ? 24.396  3.628   -14.038 1.00 46.95  ? 119 ASN A OD1 1 
ATOM   932  N  ND2 . ASN A 1 119 ? 22.670  4.563   -12.953 1.00 40.13  ? 119 ASN A ND2 1 
ATOM   933  N  N   . GLY A 1 120 ? 21.883  -1.125  -13.792 1.00 32.56  ? 120 GLY A N   1 
ATOM   934  C  CA  . GLY A 1 120 ? 21.586  -2.492  -13.344 1.00 33.59  ? 120 GLY A CA  1 
ATOM   935  C  C   . GLY A 1 120 ? 20.561  -2.548  -12.221 1.00 35.16  ? 120 GLY A C   1 
ATOM   936  O  O   . GLY A 1 120 ? 20.424  -3.636  -11.641 1.00 34.10  ? 120 GLY A O   1 
ATOM   937  N  N   . SER A 1 121 ? 19.849  -1.451  -11.944 1.00 36.65  ? 121 SER A N   1 
ATOM   938  C  CA  . SER A 1 121 ? 18.762  -1.377  -10.928 1.00 38.29  ? 121 SER A CA  1 
ATOM   939  C  C   . SER A 1 121 ? 17.407  -1.281  -11.622 1.00 33.53  ? 121 SER A C   1 
ATOM   940  O  O   . SER A 1 121 ? 17.141  -0.346  -12.369 1.00 27.99  ? 121 SER A O   1 
ATOM   941  C  CB  . SER A 1 121 ? 18.956  -0.226  -9.979  1.00 37.45  ? 121 SER A CB  1 
ATOM   942  O  OG  . SER A 1 121 ? 20.075  -0.485  -9.147  1.00 44.10  ? 121 SER A OG  1 
ATOM   943  N  N   . PRO A 1 122 ? 16.501  -2.230  -11.348 1.00 32.76  ? 122 PRO A N   1 
ATOM   944  C  CA  . PRO A 1 122 ? 15.193  -2.238  -11.999 1.00 34.51  ? 122 PRO A CA  1 
ATOM   945  C  C   . PRO A 1 122 ? 14.396  -1.041  -11.491 1.00 30.04  ? 122 PRO A C   1 
ATOM   946  O  O   . PRO A 1 122 ? 14.431  -0.783  -10.324 1.00 28.88  ? 122 PRO A O   1 
ATOM   947  C  CB  . PRO A 1 122 ? 14.568  -3.575  -11.570 1.00 33.78  ? 122 PRO A CB  1 
ATOM   948  C  CG  . PRO A 1 122 ? 15.766  -4.392  -11.041 1.00 38.64  ? 122 PRO A CG  1 
ATOM   949  C  CD  . PRO A 1 122 ? 16.690  -3.361  -10.425 1.00 34.52  ? 122 PRO A CD  1 
ATOM   950  N  N   . SER A 1 123 ? 13.733  -0.323  -12.384 1.00 30.05  ? 123 SER A N   1 
ATOM   951  C  CA  . SER A 1 123 ? 12.988  0.907   -12.027 1.00 32.16  ? 123 SER A CA  1 
ATOM   952  C  C   . SER A 1 123 ? 11.478  0.708   -12.243 1.00 29.58  ? 123 SER A C   1 
ATOM   953  O  O   . SER A 1 123 ? 10.716  1.267   -11.467 1.00 25.98  ? 123 SER A O   1 
ATOM   954  C  CB  . SER A 1 123 ? 13.557  2.076   -12.775 1.00 35.90  ? 123 SER A CB  1 
ATOM   955  O  OG  . SER A 1 123 ? 12.542  2.976   -13.188 1.00 49.52  ? 123 SER A OG  1 
ATOM   956  N  N   . GLY A 1 124 ? 11.044  -0.076  -13.236 1.00 26.13  ? 124 GLY A N   1 
ATOM   957  C  CA  . GLY A 1 124 ? 9.614   -0.375  -13.423 1.00 24.62  ? 124 GLY A CA  1 
ATOM   958  C  C   . GLY A 1 124 ? 9.338   -1.501  -14.410 1.00 22.68  ? 124 GLY A C   1 
ATOM   959  O  O   . GLY A 1 124 ? 10.270  -1.942  -15.149 1.00 19.86  ? 124 GLY A O   1 
ATOM   960  N  N   . VAL A 1 125 ? 8.083   -1.940  -14.434 1.00 21.19  ? 125 VAL A N   1 
ATOM   961  C  CA  . VAL A 1 125 ? 7.632   -3.052  -15.305 1.00 23.97  ? 125 VAL A CA  1 
ATOM   962  C  C   . VAL A 1 125 ? 6.376   -2.618  -16.052 1.00 23.86  ? 125 VAL A C   1 
ATOM   963  O  O   . VAL A 1 125 ? 5.513   -1.963  -15.450 1.00 23.45  ? 125 VAL A O   1 
ATOM   964  C  CB  . VAL A 1 125 ? 7.478   -4.363  -14.499 1.00 25.99  ? 125 VAL A CB  1 
ATOM   965  C  CG1 . VAL A 1 125 ? 6.534   -4.237  -13.338 1.00 30.44  ? 125 VAL A CG1 1 
ATOM   966  C  CG2 . VAL A 1 125 ? 7.047   -5.529  -15.376 1.00 28.55  ? 125 VAL A CG2 1 
ATOM   967  N  N   . TYR A 1 126 ? 6.299   -2.910  -17.351 1.00 22.87  ? 126 TYR A N   1 
ATOM   968  C  CA  . TYR A 1 126 ? 5.077   -2.627  -18.146 1.00 24.18  ? 126 TYR A CA  1 
ATOM   969  C  C   . TYR A 1 126 ? 4.936   -3.681  -19.243 1.00 27.29  ? 126 TYR A C   1 
ATOM   970  O  O   . TYR A 1 126 ? 5.917   -4.394  -19.600 1.00 24.46  ? 126 TYR A O   1 
ATOM   971  C  CB  . TYR A 1 126 ? 5.097   -1.181  -18.678 1.00 26.09  ? 126 TYR A CB  1 
ATOM   972  C  CG  . TYR A 1 126 ? 6.334   -0.812  -19.465 1.00 28.00  ? 126 TYR A CG  1 
ATOM   973  C  CD1 . TYR A 1 126 ? 6.417   -1.019  -20.832 1.00 27.49  ? 126 TYR A CD1 1 
ATOM   974  C  CD2 . TYR A 1 126 ? 7.422   -0.238  -18.843 1.00 27.05  ? 126 TYR A CD2 1 
ATOM   975  C  CE1 . TYR A 1 126 ? 7.567   -0.707  -21.543 1.00 28.97  ? 126 TYR A CE1 1 
ATOM   976  C  CE2 . TYR A 1 126 ? 8.559   0.124   -19.547 1.00 29.52  ? 126 TYR A CE2 1 
ATOM   977  C  CZ  . TYR A 1 126 ? 8.644   -0.135  -20.897 1.00 29.91  ? 126 TYR A CZ  1 
ATOM   978  O  OH  . TYR A 1 126 ? 9.776   0.212   -21.583 1.00 34.30  ? 126 TYR A OH  1 
ATOM   979  N  N   . GLN A 1 127 ? 3.718   -3.760  -19.769 1.00 24.93  ? 127 GLN A N   1 
ATOM   980  C  CA  . GLN A 1 127 ? 3.339   -4.630  -20.896 1.00 28.45  ? 127 GLN A CA  1 
ATOM   981  C  C   . GLN A 1 127 ? 3.484   -3.863  -22.200 1.00 27.43  ? 127 GLN A C   1 
ATOM   982  O  O   . GLN A 1 127 ? 3.126   -2.683  -22.250 1.00 28.25  ? 127 GLN A O   1 
ATOM   983  C  CB  . GLN A 1 127 ? 1.860   -5.014  -20.899 1.00 30.05  ? 127 GLN A CB  1 
ATOM   984  C  CG  . GLN A 1 127 ? 1.581   -6.327  -20.242 1.00 32.08  ? 127 GLN A CG  1 
ATOM   985  C  CD  . GLN A 1 127 ? 2.398   -7.481  -20.759 1.00 32.01  ? 127 GLN A CD  1 
ATOM   986  O  OE1 . GLN A 1 127 ? 3.446   -7.787  -20.213 1.00 29.72  ? 127 GLN A OE1 1 
ATOM   987  N  NE2 . GLN A 1 127 ? 1.838   -8.222  -21.696 1.00 29.92  ? 127 GLN A NE2 1 
ATOM   988  N  N   A CYS A 1 128 ? 4.067   -4.531  -23.209 0.30 27.37  ? 128 CYS A N   1 
ATOM   989  N  N   B CYS A 1 128 ? 3.904   -4.544  -23.258 0.20 26.41  ? 128 CYS A N   1 
ATOM   990  N  N   C CYS A 1 128 ? 4.066   -4.530  -23.210 0.30 27.37  ? 128 CYS A N   1 
ATOM   991  N  N   D CYS A 1 128 ? 3.904   -4.544  -23.258 0.20 26.41  ? 128 CYS A N   1 
ATOM   992  C  CA  A CYS A 1 128 ? 4.323   -4.045  -24.598 0.30 27.29  ? 128 CYS A CA  1 
ATOM   993  C  CA  B CYS A 1 128 ? 3.966   -3.945  -24.608 0.20 25.64  ? 128 CYS A CA  1 
ATOM   994  C  CA  C CYS A 1 128 ? 4.320   -4.043  -24.598 0.30 27.29  ? 128 CYS A CA  1 
ATOM   995  C  CA  D CYS A 1 128 ? 3.966   -3.945  -24.608 0.20 25.64  ? 128 CYS A CA  1 
ATOM   996  C  C   A CYS A 1 128 ? 3.736   -5.056  -25.598 0.30 26.17  ? 128 CYS A C   1 
ATOM   997  C  C   B CYS A 1 128 ? 3.963   -5.050  -25.659 0.20 25.55  ? 128 CYS A C   1 
ATOM   998  C  C   C CYS A 1 128 ? 3.735   -5.055  -25.598 0.30 26.17  ? 128 CYS A C   1 
ATOM   999  C  C   D CYS A 1 128 ? 3.963   -5.050  -25.659 0.20 25.55  ? 128 CYS A C   1 
ATOM   1000 O  O   A CYS A 1 128 ? 3.404   -6.165  -25.157 0.30 26.22  ? 128 CYS A O   1 
ATOM   1001 O  O   B CYS A 1 128 ? 4.344   -6.196  -25.341 0.20 25.47  ? 128 CYS A O   1 
ATOM   1002 O  O   C CYS A 1 128 ? 3.404   -6.164  -25.156 0.30 26.22  ? 128 CYS A O   1 
ATOM   1003 O  O   D CYS A 1 128 ? 4.344   -6.196  -25.341 0.20 25.47  ? 128 CYS A O   1 
ATOM   1004 C  CB  A CYS A 1 128 ? 5.819   -3.926  -24.874 0.30 28.01  ? 128 CYS A CB  1 
ATOM   1005 C  CB  B CYS A 1 128 ? 5.213   -3.094  -24.762 0.20 25.28  ? 128 CYS A CB  1 
ATOM   1006 C  CB  C CYS A 1 128 ? 5.816   -3.923  -24.876 0.30 28.00  ? 128 CYS A CB  1 
ATOM   1007 C  CB  D CYS A 1 128 ? 5.213   -3.094  -24.762 0.20 25.28  ? 128 CYS A CB  1 
ATOM   1008 S  SG  A CYS A 1 128 ? 6.550   -2.328  -24.429 0.30 32.03  ? 128 CYS A SG  1 
ATOM   1009 S  SG  B CYS A 1 128 ? 6.701   -4.114  -24.872 0.20 24.38  ? 128 CYS A SG  1 
ATOM   1010 S  SG  C CYS A 1 128 ? 6.550   -2.328  -24.429 0.30 32.02  ? 128 CYS A SG  1 
ATOM   1011 S  SG  D CYS A 1 128 ? 6.701   -4.114  -24.872 0.20 24.38  ? 128 CYS A SG  1 
ATOM   1012 N  N   . ALA A 1 129 ? 3.587   -4.677  -26.875 1.00 26.68  ? 129 ALA A N   1 
ATOM   1013 C  CA  . ALA A 1 129 ? 3.458   -5.601  -28.022 1.00 24.82  ? 129 ALA A CA  1 
ATOM   1014 C  C   . ALA A 1 129 ? 4.562   -5.240  -28.999 1.00 24.48  ? 129 ALA A C   1 
ATOM   1015 O  O   . ALA A 1 129 ? 4.905   -4.032  -29.098 1.00 28.88  ? 129 ALA A O   1 
ATOM   1016 C  CB  . ALA A 1 129 ? 2.117   -5.468  -28.682 1.00 27.36  ? 129 ALA A CB  1 
ATOM   1017 N  N   . MET A 1 130 ? 5.115   -6.239  -29.662 1.00 22.71  ? 130 MET A N   1 
ATOM   1018 C  CA  . MET A 1 130 ? 5.930   -6.064  -30.892 1.00 26.26  ? 130 MET A CA  1 
ATOM   1019 C  C   . MET A 1 130 ? 4.987   -5.547  -31.973 1.00 27.14  ? 130 MET A C   1 
ATOM   1020 O  O   . MET A 1 130 ? 4.064   -6.289  -32.384 1.00 29.15  ? 130 MET A O   1 
ATOM   1021 C  CB  . MET A 1 130 ? 6.572   -7.389  -31.305 1.00 25.10  ? 130 MET A CB  1 
ATOM   1022 C  CG  . MET A 1 130 ? 7.426   -7.364  -32.558 1.00 29.46  ? 130 MET A CG  1 
ATOM   1023 S  SD  . MET A 1 130 ? 8.891   -6.347  -32.416 1.00 33.58  ? 130 MET A SD  1 
ATOM   1024 C  CE  . MET A 1 130 ? 9.715   -6.998  -30.966 1.00 30.48  ? 130 MET A CE  1 
ATOM   1025 N  N   . ARG A 1 131 ? 5.193   -4.307  -32.402 1.00 23.83  ? 131 ARG A N   1 
ATOM   1026 C  CA  . ARG A 1 131 ? 4.401   -3.714  -33.492 1.00 24.60  ? 131 ARG A CA  1 
ATOM   1027 C  C   . ARG A 1 131 ? 4.674   -4.453  -34.801 1.00 24.69  ? 131 ARG A C   1 
ATOM   1028 O  O   . ARG A 1 131 ? 5.745   -5.031  -35.007 1.00 24.18  ? 131 ARG A O   1 
ATOM   1029 C  CB  . ARG A 1 131 ? 4.724   -2.227  -33.630 1.00 24.11  ? 131 ARG A CB  1 
ATOM   1030 C  CG  . ARG A 1 131 ? 4.562   -1.403  -32.358 1.00 25.67  ? 131 ARG A CG  1 
ATOM   1031 C  CD  . ARG A 1 131 ? 3.236   -1.482  -31.645 1.00 25.74  ? 131 ARG A CD  1 
ATOM   1032 N  NE  . ARG A 1 131 ? 2.150   -1.234  -32.583 1.00 27.15  ? 131 ARG A NE  1 
ATOM   1033 C  CZ  . ARG A 1 131 ? 0.859   -1.415  -32.325 1.00 25.76  ? 131 ARG A CZ  1 
ATOM   1034 N  NH1 . ARG A 1 131 ? 0.454   -1.847  -31.151 1.00 23.47  ? 131 ARG A NH1 1 
ATOM   1035 N  NH2 . ARG A 1 131 ? -0.020  -1.235  -33.287 1.00 27.97  ? 131 ARG A NH2 1 
ATOM   1036 N  N   . PRO A 1 132 ? 3.729   -4.409  -35.765 1.00 26.42  ? 132 PRO A N   1 
ATOM   1037 C  CA  . PRO A 1 132 ? 3.967   -4.952  -37.106 1.00 25.28  ? 132 PRO A CA  1 
ATOM   1038 C  C   . PRO A 1 132 ? 5.206   -4.374  -37.815 1.00 24.91  ? 132 PRO A C   1 
ATOM   1039 O  O   . PRO A 1 132 ? 5.742   -5.025  -38.643 1.00 23.50  ? 132 PRO A O   1 
ATOM   1040 C  CB  . PRO A 1 132 ? 2.686   -4.552  -37.867 1.00 25.68  ? 132 PRO A CB  1 
ATOM   1041 C  CG  . PRO A 1 132 ? 1.644   -4.490  -36.782 1.00 25.97  ? 132 PRO A CG  1 
ATOM   1042 C  CD  . PRO A 1 132 ? 2.371   -3.861  -35.614 1.00 25.55  ? 132 PRO A CD  1 
ATOM   1043 N  N   . ASN A 1 133 ? 5.623   -3.153  -37.485 1.00 24.83  ? 133 ASN A N   1 
ATOM   1044 C  CA  . ASN A 1 133 ? 6.825   -2.516  -38.083 1.00 24.59  ? 133 ASN A CA  1 
ATOM   1045 C  C   . ASN A 1 133 ? 8.069   -2.863  -37.247 1.00 26.61  ? 133 ASN A C   1 
ATOM   1046 O  O   . ASN A 1 133 ? 9.124   -2.256  -37.509 1.00 26.52  ? 133 ASN A O   1 
ATOM   1047 C  CB  . ASN A 1 133 ? 6.680   -1.004  -38.254 1.00 25.83  ? 133 ASN A CB  1 
ATOM   1048 C  CG  . ASN A 1 133 ? 6.625   -0.244  -36.941 1.00 24.81  ? 133 ASN A CG  1 
ATOM   1049 O  OD1 . ASN A 1 133 ? 6.760   -0.827  -35.860 1.00 24.97  ? 133 ASN A OD1 1 
ATOM   1050 N  ND2 . ASN A 1 133 ? 6.345   1.042   -37.023 1.00 23.25  ? 133 ASN A ND2 1 
ATOM   1051 N  N   . PHE A 1 134 ? 7.963   -3.806  -36.307 1.00 25.52  ? 134 PHE A N   1 
ATOM   1052 C  CA  . PHE A 1 134 ? 9.099   -4.458  -35.603 1.00 27.08  ? 134 PHE A CA  1 
ATOM   1053 C  C   . PHE A 1 134 ? 9.713   -3.502  -34.570 1.00 29.31  ? 134 PHE A C   1 
ATOM   1054 O  O   . PHE A 1 134 ? 10.854  -3.746  -34.156 1.00 30.76  ? 134 PHE A O   1 
ATOM   1055 C  CB  . PHE A 1 134 ? 10.164  -4.938  -36.591 1.00 27.51  ? 134 PHE A CB  1 
ATOM   1056 C  CG  . PHE A 1 134 ? 9.735   -6.144  -37.383 1.00 28.72  ? 134 PHE A CG  1 
ATOM   1057 C  CD1 . PHE A 1 134 ? 9.718   -7.400  -36.790 1.00 31.66  ? 134 PHE A CD1 1 
ATOM   1058 C  CD2 . PHE A 1 134 ? 9.306   -6.021  -38.689 1.00 28.47  ? 134 PHE A CD2 1 
ATOM   1059 C  CE1 . PHE A 1 134 ? 9.277   -8.512  -37.489 1.00 30.41  ? 134 PHE A CE1 1 
ATOM   1060 C  CE2 . PHE A 1 134 ? 8.901   -7.142  -39.404 1.00 31.42  ? 134 PHE A CE2 1 
ATOM   1061 C  CZ  . PHE A 1 134 ? 8.897   -8.385  -38.804 1.00 28.97  ? 134 PHE A CZ  1 
ATOM   1062 N  N   . THR A 1 135 ? 8.983   -2.455  -34.175 1.00 25.58  ? 135 THR A N   1 
ATOM   1063 C  CA  . THR A 1 135 ? 9.357   -1.564  -33.054 1.00 23.69  ? 135 THR A CA  1 
ATOM   1064 C  C   . THR A 1 135 ? 8.486   -1.863  -31.838 1.00 23.35  ? 135 THR A C   1 
ATOM   1065 O  O   . THR A 1 135 ? 7.464   -2.562  -31.968 1.00 23.28  ? 135 THR A O   1 
ATOM   1066 C  CB  . THR A 1 135 ? 9.244   -0.107  -33.501 1.00 25.37  ? 135 THR A CB  1 
ATOM   1067 O  OG1 . THR A 1 135 ? 7.871   0.236   -33.714 1.00 26.82  ? 135 THR A OG1 1 
ATOM   1068 C  CG2 . THR A 1 135 ? 10.028  0.124   -34.769 1.00 27.17  ? 135 THR A CG2 1 
ATOM   1069 N  N   . ILE A 1 136 ? 8.836   -1.286  -30.700 1.00 21.44  ? 136 ILE A N   1 
ATOM   1070 C  CA  . ILE A 1 136 ? 7.977   -1.314  -29.496 1.00 23.02  ? 136 ILE A CA  1 
ATOM   1071 C  C   . ILE A 1 136 ? 7.786   0.116   -29.015 1.00 24.19  ? 136 ILE A C   1 
ATOM   1072 O  O   . ILE A 1 136 ? 8.681   0.933   -29.204 1.00 21.19  ? 136 ILE A O   1 
ATOM   1073 C  CB  . ILE A 1 136 ? 8.509   -2.287  -28.434 1.00 27.50  ? 136 ILE A CB  1 
ATOM   1074 C  CG1 . ILE A 1 136 ? 9.687   -1.717  -27.657 1.00 29.18  ? 136 ILE A CG1 1 
ATOM   1075 C  CG2 . ILE A 1 136 ? 8.851   -3.642  -29.081 1.00 27.57  ? 136 ILE A CG2 1 
ATOM   1076 C  CD1 . ILE A 1 136 ? 10.137  -2.631  -26.544 1.00 32.99  ? 136 ILE A CD1 1 
ATOM   1077 N  N   . LYS A 1 137 ? 6.591   0.405   -28.522 1.00 26.30  ? 137 LYS A N   1 
ATOM   1078 C  CA  . LYS A 1 137 ? 6.236   1.733   -27.969 1.00 29.59  ? 137 LYS A CA  1 
ATOM   1079 C  C   . LYS A 1 137 ? 6.514   1.641   -26.470 1.00 27.74  ? 137 LYS A C   1 
ATOM   1080 O  O   . LYS A 1 137 ? 5.631   1.331   -25.680 1.00 26.26  ? 137 LYS A O   1 
ATOM   1081 C  CB  . LYS A 1 137 ? 4.799   2.089   -28.364 1.00 30.83  ? 137 LYS A CB  1 
ATOM   1082 C  CG  . LYS A 1 137 ? 4.583   2.204   -29.871 1.00 35.71  ? 137 LYS A CG  1 
ATOM   1083 C  CD  . LYS A 1 137 ? 3.182   2.665   -30.219 1.00 42.03  ? 137 LYS A CD  1 
ATOM   1084 C  CE  . LYS A 1 137 ? 2.900   2.690   -31.703 1.00 53.73  ? 137 LYS A CE  1 
ATOM   1085 N  NZ  . LYS A 1 137 ? 1.438   2.650   -31.962 1.00 60.93  ? 137 LYS A NZ  1 
ATOM   1086 N  N   . GLY A 1 138 ? 7.771   1.802   -26.114 1.00 28.90  ? 138 GLY A N   1 
ATOM   1087 C  CA  . GLY A 1 138 ? 8.209   1.640   -24.726 1.00 25.61  ? 138 GLY A CA  1 
ATOM   1088 C  C   . GLY A 1 138 ? 8.332   2.965   -24.022 1.00 26.65  ? 138 GLY A C   1 
ATOM   1089 O  O   . GLY A 1 138 ? 7.917   4.027   -24.562 1.00 24.94  ? 138 GLY A O   1 
ATOM   1090 N  N   . SER A 1 139 ? 8.902   2.886   -22.824 1.00 26.32  ? 139 SER A N   1 
ATOM   1091 C  CA  . SER A 1 139 ? 9.288   4.026   -21.971 1.00 28.39  ? 139 SER A CA  1 
ATOM   1092 C  C   . SER A 1 139 ? 10.716  3.748   -21.504 1.00 29.50  ? 139 SER A C   1 
ATOM   1093 O  O   . SER A 1 139 ? 10.925  2.882   -20.649 1.00 26.87  ? 139 SER A O   1 
ATOM   1094 C  CB  . SER A 1 139 ? 8.341   4.238   -20.823 1.00 28.65  ? 139 SER A CB  1 
ATOM   1095 O  OG  . SER A 1 139 ? 8.903   5.202   -19.949 1.00 29.07  ? 139 SER A OG  1 
ATOM   1096 N  N   A PHE A 1 140 ? 11.662  4.445   -22.133 0.31 29.35  ? 140 PHE A N   1 
ATOM   1097 N  N   B PHE A 1 140 ? 11.662  4.445   -22.133 0.31 29.35  ? 140 PHE A N   1 
ATOM   1098 N  N   C PHE A 1 140 ? 11.682  4.489   -22.052 0.19 30.72  ? 140 PHE A N   1 
ATOM   1099 N  N   D PHE A 1 140 ? 11.682  4.489   -22.052 0.19 30.72  ? 140 PHE A N   1 
ATOM   1100 C  CA  A PHE A 1 140 ? 13.121  4.202   -22.050 0.31 29.72  ? 140 PHE A CA  1 
ATOM   1101 C  CA  B PHE A 1 140 ? 13.121  4.202   -22.050 0.31 29.72  ? 140 PHE A CA  1 
ATOM   1102 C  CA  C PHE A 1 140 ? 13.130  4.380   -21.733 0.19 32.01  ? 140 PHE A CA  1 
ATOM   1103 C  CA  D PHE A 1 140 ? 13.130  4.380   -21.733 0.19 32.01  ? 140 PHE A CA  1 
ATOM   1104 C  C   A PHE A 1 140 ? 13.856  5.546   -22.055 0.31 31.62  ? 140 PHE A C   1 
ATOM   1105 C  C   B PHE A 1 140 ? 13.856  5.546   -22.055 0.31 31.62  ? 140 PHE A C   1 
ATOM   1106 C  C   C PHE A 1 140 ? 13.798  5.757   -21.873 0.19 33.41  ? 140 PHE A C   1 
ATOM   1107 C  C   D PHE A 1 140 ? 13.798  5.757   -21.873 0.19 33.41  ? 140 PHE A C   1 
ATOM   1108 O  O   A PHE A 1 140 ? 13.679  6.327   -23.019 0.31 31.29  ? 140 PHE A O   1 
ATOM   1109 O  O   B PHE A 1 140 ? 13.679  6.327   -23.019 0.31 31.29  ? 140 PHE A O   1 
ATOM   1110 O  O   C PHE A 1 140 ? 13.557  6.422   -22.904 0.19 33.48  ? 140 PHE A O   1 
ATOM   1111 O  O   D PHE A 1 140 ? 13.557  6.422   -22.904 0.19 33.48  ? 140 PHE A O   1 
ATOM   1112 C  CB  A PHE A 1 140 ? 13.587  3.372   -23.249 0.31 28.20  ? 140 PHE A CB  1 
ATOM   1113 C  CB  B PHE A 1 140 ? 13.587  3.372   -23.249 0.31 28.20  ? 140 PHE A CB  1 
ATOM   1114 C  CB  C PHE A 1 140 ? 13.833  3.418   -22.696 0.19 32.42  ? 140 PHE A CB  1 
ATOM   1115 C  CB  D PHE A 1 140 ? 13.833  3.418   -22.696 0.19 32.42  ? 140 PHE A CB  1 
ATOM   1116 C  CG  A PHE A 1 140 ? 13.207  1.912   -23.219 0.31 28.66  ? 140 PHE A CG  1 
ATOM   1117 C  CG  B PHE A 1 140 ? 13.207  1.912   -23.219 0.31 28.66  ? 140 PHE A CG  1 
ATOM   1118 C  CG  C PHE A 1 140 ? 13.234  2.043   -22.869 0.19 32.62  ? 140 PHE A CG  1 
ATOM   1119 C  CG  D PHE A 1 140 ? 13.234  2.043   -22.869 0.19 32.62  ? 140 PHE A CG  1 
ATOM   1120 C  CD1 A PHE A 1 140 ? 13.625  1.084   -22.187 0.31 28.05  ? 140 PHE A CD1 1 
ATOM   1121 C  CD1 B PHE A 1 140 ? 13.625  1.084   -22.187 0.31 28.05  ? 140 PHE A CD1 1 
ATOM   1122 C  CD1 C PHE A 1 140 ? 13.513  1.017   -21.977 0.19 32.44  ? 140 PHE A CD1 1 
ATOM   1123 C  CD1 D PHE A 1 140 ? 13.513  1.017   -21.977 0.19 32.44  ? 140 PHE A CD1 1 
ATOM   1124 C  CD2 A PHE A 1 140 ? 12.458  1.355   -24.244 0.31 28.02  ? 140 PHE A CD2 1 
ATOM   1125 C  CD2 B PHE A 1 140 ? 12.458  1.355   -24.244 0.31 28.02  ? 140 PHE A CD2 1 
ATOM   1126 C  CD2 C PHE A 1 140 ? 12.447  1.755   -23.974 0.19 32.33  ? 140 PHE A CD2 1 
ATOM   1127 C  CD2 D PHE A 1 140 ? 12.447  1.755   -23.974 0.19 32.33  ? 140 PHE A CD2 1 
ATOM   1128 C  CE1 A PHE A 1 140 ? 13.288  -0.263  -22.176 0.31 28.58  ? 140 PHE A CE1 1 
ATOM   1129 C  CE1 B PHE A 1 140 ? 13.288  -0.263  -22.176 0.31 28.58  ? 140 PHE A CE1 1 
ATOM   1130 C  CE1 C PHE A 1 140 ? 12.987  -0.254  -22.168 0.19 32.88  ? 140 PHE A CE1 1 
ATOM   1131 C  CE1 D PHE A 1 140 ? 12.987  -0.254  -22.168 0.19 32.88  ? 140 PHE A CE1 1 
ATOM   1132 C  CE2 A PHE A 1 140 ? 12.130  0.007   -24.236 0.31 27.76  ? 140 PHE A CE2 1 
ATOM   1133 C  CE2 B PHE A 1 140 ? 12.130  0.007   -24.236 0.31 27.76  ? 140 PHE A CE2 1 
ATOM   1134 C  CE2 C PHE A 1 140 ? 11.922  0.485   -24.165 0.19 32.39  ? 140 PHE A CE2 1 
ATOM   1135 C  CE2 D PHE A 1 140 ? 11.922  0.485   -24.165 0.19 32.39  ? 140 PHE A CE2 1 
ATOM   1136 C  CZ  A PHE A 1 140 ? 12.546  -0.800  -23.202 0.31 27.77  ? 140 PHE A CZ  1 
ATOM   1137 C  CZ  B PHE A 1 140 ? 12.546  -0.800  -23.202 0.31 27.77  ? 140 PHE A CZ  1 
ATOM   1138 C  CZ  C PHE A 1 140 ? 12.197  -0.519  -23.264 0.19 32.68  ? 140 PHE A CZ  1 
ATOM   1139 C  CZ  D PHE A 1 140 ? 12.197  -0.519  -23.264 0.19 32.68  ? 140 PHE A CZ  1 
ATOM   1140 N  N   A LEU A 1 141 ? 14.661  5.801   -21.024 0.31 32.89  ? 141 LEU A N   1 
ATOM   1141 N  N   B LEU A 1 141 ? 14.661  5.801   -21.024 0.31 32.89  ? 141 LEU A N   1 
ATOM   1142 N  N   C LEU A 1 141 ? 14.614  6.168   -20.893 0.19 34.53  ? 141 LEU A N   1 
ATOM   1143 N  N   D LEU A 1 141 ? 14.614  6.168   -20.893 0.19 34.53  ? 141 LEU A N   1 
ATOM   1144 C  CA  A LEU A 1 141 ? 15.551  6.988   -20.958 0.31 35.16  ? 141 LEU A CA  1 
ATOM   1145 C  CA  B LEU A 1 141 ? 15.551  6.988   -20.958 0.31 35.16  ? 141 LEU A CA  1 
ATOM   1146 C  CA  C LEU A 1 141 ? 15.542  7.330   -21.021 0.19 35.18  ? 141 LEU A CA  1 
ATOM   1147 C  CA  D LEU A 1 141 ? 15.542  7.330   -21.021 0.19 35.18  ? 141 LEU A CA  1 
ATOM   1148 C  C   A LEU A 1 141 ? 16.992  6.522   -21.184 0.31 36.27  ? 141 LEU A C   1 
ATOM   1149 C  C   B LEU A 1 141 ? 16.992  6.522   -21.184 0.31 36.27  ? 141 LEU A C   1 
ATOM   1150 C  C   C LEU A 1 141 ? 16.954  6.784   -21.274 0.19 34.80  ? 141 LEU A C   1 
ATOM   1151 C  C   D LEU A 1 141 ? 16.954  6.784   -21.274 0.19 34.80  ? 141 LEU A C   1 
ATOM   1152 O  O   A LEU A 1 141 ? 17.237  5.295   -21.219 0.31 33.16  ? 141 LEU A O   1 
ATOM   1153 O  O   B LEU A 1 141 ? 17.237  5.295   -21.219 0.31 33.16  ? 141 LEU A O   1 
ATOM   1154 O  O   C LEU A 1 141 ? 17.082  5.564   -21.504 0.19 34.13  ? 141 LEU A O   1 
ATOM   1155 O  O   D LEU A 1 141 ? 17.082  5.564   -21.504 0.19 34.13  ? 141 LEU A O   1 
ATOM   1156 C  CB  A LEU A 1 141 ? 15.400  7.690   -19.602 0.31 37.00  ? 141 LEU A CB  1 
ATOM   1157 C  CB  B LEU A 1 141 ? 15.400  7.690   -19.602 0.31 37.00  ? 141 LEU A CB  1 
ATOM   1158 C  CB  C LEU A 1 141 ? 15.498  8.202   -19.757 0.19 36.18  ? 141 LEU A CB  1 
ATOM   1159 C  CB  D LEU A 1 141 ? 15.498  8.202   -19.757 0.19 36.18  ? 141 LEU A CB  1 
ATOM   1160 C  CG  A LEU A 1 141 ? 13.997  8.167   -19.219 0.31 38.02  ? 141 LEU A CG  1 
ATOM   1161 C  CG  B LEU A 1 141 ? 13.997  8.167   -19.219 0.31 38.02  ? 141 LEU A CG  1 
ATOM   1162 C  CG  C LEU A 1 141 ? 14.122  8.689   -19.297 0.19 37.05  ? 141 LEU A CG  1 
ATOM   1163 C  CG  D LEU A 1 141 ? 14.122  8.689   -19.297 0.19 37.05  ? 141 LEU A CG  1 
ATOM   1164 C  CD1 A LEU A 1 141 ? 13.998  8.721   -17.799 0.31 39.04  ? 141 LEU A CD1 1 
ATOM   1165 C  CD1 B LEU A 1 141 ? 13.998  8.721   -17.799 0.31 39.04  ? 141 LEU A CD1 1 
ATOM   1166 C  CD1 C LEU A 1 141 ? 14.058  8.757   -17.776 0.19 37.50  ? 141 LEU A CD1 1 
ATOM   1167 C  CD1 D LEU A 1 141 ? 14.058  8.757   -17.776 0.19 37.50  ? 141 LEU A CD1 1 
ATOM   1168 C  CD2 A LEU A 1 141 ? 13.479  9.218   -20.193 0.31 39.79  ? 141 LEU A CD2 1 
ATOM   1169 C  CD2 B LEU A 1 141 ? 13.479  9.218   -20.193 0.31 39.79  ? 141 LEU A CD2 1 
ATOM   1170 C  CD2 C LEU A 1 141 ? 13.784  10.048  -19.899 0.19 37.59  ? 141 LEU A CD2 1 
ATOM   1171 C  CD2 D LEU A 1 141 ? 13.784  10.048  -19.899 0.19 37.59  ? 141 LEU A CD2 1 
ATOM   1172 N  N   A ASN A 1 142 ? 17.920  7.466   -21.333 0.31 38.15  ? 142 ASN A N   1 
ATOM   1173 N  N   B ASN A 1 142 ? 17.920  7.466   -21.333 0.31 38.15  ? 142 ASN A N   1 
ATOM   1174 N  N   C ASN A 1 142 ? 17.980  7.642   -21.238 0.19 34.13  ? 142 ASN A N   1 
ATOM   1175 N  N   D ASN A 1 142 ? 17.980  7.642   -21.238 0.19 34.13  ? 142 ASN A N   1 
ATOM   1176 C  CA  A ASN A 1 142 ? 19.369  7.160   -21.451 0.31 39.11  ? 142 ASN A CA  1 
ATOM   1177 C  CA  B ASN A 1 142 ? 19.369  7.160   -21.451 0.31 39.11  ? 142 ASN A CA  1 
ATOM   1178 C  CA  C ASN A 1 142 ? 19.404  7.228   -21.372 0.19 33.41  ? 142 ASN A CA  1 
ATOM   1179 C  CA  D ASN A 1 142 ? 19.404  7.228   -21.372 0.19 33.41  ? 142 ASN A CA  1 
ATOM   1180 C  C   A ASN A 1 142 ? 19.760  6.271   -20.261 0.31 35.76  ? 142 ASN A C   1 
ATOM   1181 C  C   B ASN A 1 142 ? 19.760  6.271   -20.261 0.31 35.76  ? 142 ASN A C   1 
ATOM   1182 C  C   C ASN A 1 142 ? 19.737  6.250   -20.238 0.19 32.82  ? 142 ASN A C   1 
ATOM   1183 C  C   D ASN A 1 142 ? 19.737  6.250   -20.238 0.19 32.82  ? 142 ASN A C   1 
ATOM   1184 O  O   A ASN A 1 142 ? 19.280  6.539   -19.134 0.31 32.43  ? 142 ASN A O   1 
ATOM   1185 O  O   B ASN A 1 142 ? 19.280  6.539   -19.134 0.31 32.43  ? 142 ASN A O   1 
ATOM   1186 O  O   C ASN A 1 142 ? 19.233  6.461   -19.111 0.19 31.10  ? 142 ASN A O   1 
ATOM   1187 O  O   D ASN A 1 142 ? 19.233  6.461   -19.111 0.19 31.10  ? 142 ASN A O   1 
ATOM   1188 C  CB  A ASN A 1 142 ? 20.196  8.440   -21.600 0.31 43.69  ? 142 ASN A CB  1 
ATOM   1189 C  CB  B ASN A 1 142 ? 20.196  8.440   -21.600 0.31 43.69  ? 142 ASN A CB  1 
ATOM   1190 C  CB  C ASN A 1 142 ? 20.362  8.425   -21.372 0.19 33.54  ? 142 ASN A CB  1 
ATOM   1191 C  CB  D ASN A 1 142 ? 20.362  8.425   -21.372 0.19 33.54  ? 142 ASN A CB  1 
ATOM   1192 C  CG  A ASN A 1 142 ? 19.981  9.095   -22.952 0.31 47.71  ? 142 ASN A CG  1 
ATOM   1193 C  CG  B ASN A 1 142 ? 19.981  9.095   -22.952 0.31 47.71  ? 142 ASN A CG  1 
ATOM   1194 C  CG  C ASN A 1 142 ? 21.699  8.126   -22.022 0.19 32.95  ? 142 ASN A CG  1 
ATOM   1195 C  CG  D ASN A 1 142 ? 21.699  8.126   -22.022 0.19 32.95  ? 142 ASN A CG  1 
ATOM   1196 O  OD1 A ASN A 1 142 ? 20.590  8.697   -23.944 0.31 51.05  ? 142 ASN A OD1 1 
ATOM   1197 O  OD1 B ASN A 1 142 ? 20.590  8.697   -23.944 0.31 51.05  ? 142 ASN A OD1 1 
ATOM   1198 O  OD1 C ASN A 1 142 ? 22.088  6.971   -22.189 0.19 33.12  ? 142 ASN A OD1 1 
ATOM   1199 O  OD1 D ASN A 1 142 ? 22.088  6.971   -22.189 0.19 33.12  ? 142 ASN A OD1 1 
ATOM   1200 N  ND2 A ASN A 1 142 ? 19.104  10.085  -23.008 0.31 51.54  ? 142 ASN A ND2 1 
ATOM   1201 N  ND2 B ASN A 1 142 ? 19.104  10.085  -23.008 0.31 51.54  ? 142 ASN A ND2 1 
ATOM   1202 N  ND2 C ASN A 1 142 ? 22.412  9.169   -22.407 0.19 33.78  ? 142 ASN A ND2 1 
ATOM   1203 N  ND2 D ASN A 1 142 ? 22.412  9.169   -22.407 0.19 33.78  ? 142 ASN A ND2 1 
ATOM   1204 N  N   . GLY A 1 143 ? 20.522  5.208   -20.537 1.00 31.97  ? 143 GLY A N   1 
ATOM   1205 C  CA  . GLY A 1 143 ? 20.946  4.213   -19.534 1.00 32.75  ? 143 GLY A CA  1 
ATOM   1206 C  C   . GLY A 1 143 ? 20.108  2.932   -19.476 1.00 29.94  ? 143 GLY A C   1 
ATOM   1207 O  O   . GLY A 1 143 ? 20.485  2.009   -18.730 1.00 29.97  ? 143 GLY A O   1 
ATOM   1208 N  N   A SER A 1 144 ? 19.023  2.882   -20.252 0.31 28.63  ? 144 SER A N   1 
ATOM   1209 N  N   B SER A 1 144 ? 19.023  2.882   -20.252 0.31 28.63  ? 144 SER A N   1 
ATOM   1210 N  N   C SER A 1 144 ? 18.994  2.853   -20.215 0.19 30.63  ? 144 SER A N   1 
ATOM   1211 N  N   D SER A 1 144 ? 18.994  2.853   -20.215 0.19 30.63  ? 144 SER A N   1 
ATOM   1212 C  CA  A SER A 1 144 ? 18.035  1.772   -20.252 0.31 26.61  ? 144 SER A CA  1 
ATOM   1213 C  CA  B SER A 1 144 ? 18.035  1.772   -20.252 0.31 26.61  ? 144 SER A CA  1 
ATOM   1214 C  CA  C SER A 1 144 ? 18.065  1.687   -20.187 0.19 30.07  ? 144 SER A CA  1 
ATOM   1215 C  CA  D SER A 1 144 ? 18.065  1.687   -20.187 0.19 30.07  ? 144 SER A CA  1 
ATOM   1216 C  C   A SER A 1 144 ? 18.508  0.628   -21.151 0.31 25.70  ? 144 SER A C   1 
ATOM   1217 C  C   B SER A 1 144 ? 18.508  0.628   -21.151 0.31 25.70  ? 144 SER A C   1 
ATOM   1218 C  C   C SER A 1 144 ? 18.540  0.576   -21.130 0.19 29.80  ? 144 SER A C   1 
ATOM   1219 C  C   D SER A 1 144 ? 18.540  0.576   -21.130 0.19 29.80  ? 144 SER A C   1 
ATOM   1220 O  O   A SER A 1 144 ? 17.921  -0.469  -21.049 0.31 24.54  ? 144 SER A O   1 
ATOM   1221 O  O   B SER A 1 144 ? 17.921  -0.469  -21.049 0.31 24.54  ? 144 SER A O   1 
ATOM   1222 O  O   C SER A 1 144 ? 17.968  -0.531  -21.060 0.19 28.99  ? 144 SER A O   1 
ATOM   1223 O  O   D SER A 1 144 ? 17.968  -0.531  -21.060 0.19 28.99  ? 144 SER A O   1 
ATOM   1224 C  CB  A SER A 1 144 ? 16.680  2.254   -20.683 0.31 25.79  ? 144 SER A CB  1 
ATOM   1225 C  CB  B SER A 1 144 ? 16.680  2.254   -20.683 0.31 25.79  ? 144 SER A CB  1 
ATOM   1226 C  CB  C SER A 1 144 ? 16.641  2.080   -20.499 0.19 30.04  ? 144 SER A CB  1 
ATOM   1227 C  CB  D SER A 1 144 ? 16.641  2.080   -20.499 0.19 30.04  ? 144 SER A CB  1 
ATOM   1228 O  OG  A SER A 1 144 ? 16.741  2.810   -21.986 0.31 25.65  ? 144 SER A OG  1 
ATOM   1229 O  OG  B SER A 1 144 ? 16.741  2.810   -21.986 0.31 25.65  ? 144 SER A OG  1 
ATOM   1230 O  OG  C SER A 1 144 ? 16.572  3.396   -21.017 0.19 30.37  ? 144 SER A OG  1 
ATOM   1231 O  OG  D SER A 1 144 ? 16.572  3.396   -21.017 0.19 30.37  ? 144 SER A OG  1 
ATOM   1232 N  N   A CYS A 1 145 ? 19.485  0.878   -22.033 0.31 25.23  ? 145 CYS A N   1 
ATOM   1233 N  N   B CYS A 1 145 ? 19.485  0.878   -22.033 0.31 25.23  ? 145 CYS A N   1 
ATOM   1234 N  N   C CYS A 1 145 ? 19.518  0.865   -21.995 0.19 30.00  ? 145 CYS A N   1 
ATOM   1235 N  N   D CYS A 1 145 ? 19.518  0.865   -21.995 0.19 30.00  ? 145 CYS A N   1 
ATOM   1236 C  CA  A CYS A 1 145 ? 19.990  -0.149  -22.980 0.31 25.08  ? 145 CYS A CA  1 
ATOM   1237 C  CA  B CYS A 1 145 ? 19.990  -0.149  -22.980 0.31 25.08  ? 145 CYS A CA  1 
ATOM   1238 C  CA  C CYS A 1 145 ? 20.101  -0.098  -22.967 0.19 30.14  ? 145 CYS A CA  1 
ATOM   1239 C  CA  D CYS A 1 145 ? 20.101  -0.098  -22.967 0.19 30.14  ? 145 CYS A CA  1 
ATOM   1240 C  C   A CYS A 1 145 ? 20.375  -1.390  -22.169 0.31 26.14  ? 145 CYS A C   1 
ATOM   1241 C  C   B CYS A 1 145 ? 20.375  -1.390  -22.169 0.31 26.14  ? 145 CYS A C   1 
ATOM   1242 C  C   C CYS A 1 145 ? 20.466  -1.393  -22.214 0.19 29.04  ? 145 CYS A C   1 
ATOM   1243 C  C   D CYS A 1 145 ? 20.466  -1.393  -22.214 0.19 29.04  ? 145 CYS A C   1 
ATOM   1244 O  O   A CYS A 1 145 ? 20.922  -1.238  -21.043 0.31 25.11  ? 145 CYS A O   1 
ATOM   1245 O  O   B CYS A 1 145 ? 20.922  -1.238  -21.043 0.31 25.11  ? 145 CYS A O   1 
ATOM   1246 O  O   C CYS A 1 145 ? 21.134  -1.286  -21.164 0.19 28.64  ? 145 CYS A O   1 
ATOM   1247 O  O   D CYS A 1 145 ? 21.134  -1.286  -21.164 0.19 28.64  ? 145 CYS A O   1 
ATOM   1248 C  CB  A CYS A 1 145 ? 21.138  0.358   -23.845 0.31 24.17  ? 145 CYS A CB  1 
ATOM   1249 C  CB  B CYS A 1 145 ? 21.138  0.358   -23.845 0.31 24.17  ? 145 CYS A CB  1 
ATOM   1250 C  CB  C CYS A 1 145 ? 21.289  0.540   -23.687 0.19 31.41  ? 145 CYS A CB  1 
ATOM   1251 C  CB  D CYS A 1 145 ? 21.289  0.540   -23.687 0.19 31.41  ? 145 CYS A CB  1 
ATOM   1252 S  SG  A CYS A 1 145 ? 20.620  1.614   -25.047 0.31 22.92  ? 145 CYS A SG  1 
ATOM   1253 S  SG  B CYS A 1 145 ? 20.620  1.614   -25.047 0.31 22.92  ? 145 CYS A SG  1 
ATOM   1254 S  SG  C CYS A 1 145 ? 21.088  2.328   -24.012 0.19 33.92  ? 145 CYS A SG  1 
ATOM   1255 S  SG  D CYS A 1 145 ? 21.088  2.328   -24.012 0.19 33.92  ? 145 CYS A SG  1 
ATOM   1256 N  N   . GLY A 1 146 ? 19.980  -2.556  -22.678 1.00 26.33  ? 146 GLY A N   1 
ATOM   1257 C  CA  . GLY A 1 146 ? 20.193  -3.847  -22.001 1.00 28.50  ? 146 GLY A CA  1 
ATOM   1258 C  C   . GLY A 1 146 ? 19.028  -4.267  -21.112 1.00 27.49  ? 146 GLY A C   1 
ATOM   1259 O  O   . GLY A 1 146 ? 19.056  -5.432  -20.667 1.00 24.66  ? 146 GLY A O   1 
ATOM   1260 N  N   . SER A 1 147 ? 18.031  -3.392  -20.873 1.00 25.03  ? 147 SER A N   1 
ATOM   1261 C  CA  . SER A 1 147 ? 16.684  -3.769  -20.353 1.00 24.90  ? 147 SER A CA  1 
ATOM   1262 C  C   . SER A 1 147 ? 16.065  -4.892  -21.204 1.00 21.28  ? 147 SER A C   1 
ATOM   1263 O  O   . SER A 1 147 ? 16.275  -4.935  -22.395 1.00 20.28  ? 147 SER A O   1 
ATOM   1264 C  CB  . SER A 1 147 ? 15.763  -2.562  -20.244 1.00 24.55  ? 147 SER A CB  1 
ATOM   1265 O  OG  . SER A 1 147 ? 16.286  -1.597  -19.319 1.00 21.34  ? 147 SER A OG  1 
ATOM   1266 N  N   . VAL A 1 148 ? 15.328  -5.815  -20.599 1.00 21.81  ? 148 VAL A N   1 
ATOM   1267 C  CA  . VAL A 1 148 ? 14.898  -7.029  -21.331 1.00 21.86  ? 148 VAL A CA  1 
ATOM   1268 C  C   . VAL A 1 148 ? 13.392  -7.137  -21.302 1.00 20.13  ? 148 VAL A C   1 
ATOM   1269 O  O   . VAL A 1 148 ? 12.753  -6.614  -20.360 1.00 22.88  ? 148 VAL A O   1 
ATOM   1270 C  CB  . VAL A 1 148 ? 15.597  -8.306  -20.832 1.00 24.00  ? 148 VAL A CB  1 
ATOM   1271 C  CG1 . VAL A 1 148 ? 17.086  -8.256  -21.158 1.00 24.81  ? 148 VAL A CG1 1 
ATOM   1272 C  CG2 . VAL A 1 148 ? 15.369  -8.595  -19.364 1.00 22.26  ? 148 VAL A CG2 1 
ATOM   1273 N  N   . GLY A 1 149 ? 12.856  -7.788  -22.335 1.00 19.74  ? 149 GLY A N   1 
ATOM   1274 C  CA  . GLY A 1 149 ? 11.453  -8.184  -22.430 1.00 18.94  ? 149 GLY A CA  1 
ATOM   1275 C  C   . GLY A 1 149 ? 11.300  -9.673  -22.259 1.00 21.90  ? 149 GLY A C   1 
ATOM   1276 O  O   . GLY A 1 149 ? 12.168  -10.422 -22.758 1.00 23.65  ? 149 GLY A O   1 
ATOM   1277 N  N   . PHE A 1 150 ? 10.200  -10.103 -21.630 1.00 22.27  ? 150 PHE A N   1 
ATOM   1278 C  CA  . PHE A 1 150 ? 10.030  -11.498 -21.181 1.00 25.79  ? 150 PHE A CA  1 
ATOM   1279 C  C   . PHE A 1 150 ? 8.552   -11.856 -21.059 1.00 25.95  ? 150 PHE A C   1 
ATOM   1280 O  O   . PHE A 1 150 ? 7.702   -10.972 -20.843 1.00 23.28  ? 150 PHE A O   1 
ATOM   1281 C  CB  . PHE A 1 150 ? 10.740  -11.753 -19.843 1.00 27.20  ? 150 PHE A CB  1 
ATOM   1282 C  CG  . PHE A 1 150 ? 10.315  -10.851 -18.713 1.00 26.39  ? 150 PHE A CG  1 
ATOM   1283 C  CD1 . PHE A 1 150 ? 10.771  -9.545  -18.642 1.00 27.49  ? 150 PHE A CD1 1 
ATOM   1284 C  CD2 . PHE A 1 150 ? 9.482   -11.311 -17.717 1.00 27.34  ? 150 PHE A CD2 1 
ATOM   1285 C  CE1 . PHE A 1 150 ? 10.372  -8.695  -17.622 1.00 26.37  ? 150 PHE A CE1 1 
ATOM   1286 C  CE2 . PHE A 1 150 ? 9.098   -10.470 -16.679 1.00 28.56  ? 150 PHE A CE2 1 
ATOM   1287 C  CZ  . PHE A 1 150 ? 9.542   -9.166  -16.633 1.00 27.48  ? 150 PHE A CZ  1 
ATOM   1288 N  N   . ASN A 1 151 ? 8.292   -13.160 -21.171 1.00 26.71  ? 151 ASN A N   1 
ATOM   1289 C  CA  . ASN A 1 151 ? 7.049   -13.809 -20.694 1.00 27.09  ? 151 ASN A CA  1 
ATOM   1290 C  C   . ASN A 1 151 ? 7.432   -14.809 -19.604 1.00 29.69  ? 151 ASN A C   1 
ATOM   1291 O  O   . ASN A 1 151 ? 8.641   -15.201 -19.489 1.00 31.34  ? 151 ASN A O   1 
ATOM   1292 C  CB  . ASN A 1 151 ? 6.256   -14.432 -21.837 1.00 25.75  ? 151 ASN A CB  1 
ATOM   1293 C  CG  . ASN A 1 151 ? 5.670   -13.381 -22.751 1.00 28.83  ? 151 ASN A CG  1 
ATOM   1294 O  OD1 . ASN A 1 151 ? 4.606   -12.803 -22.473 1.00 28.64  ? 151 ASN A OD1 1 
ATOM   1295 N  ND2 . ASN A 1 151 ? 6.356   -13.136 -23.860 1.00 26.85  ? 151 ASN A ND2 1 
ATOM   1296 N  N   . ILE A 1 152 ? 6.455   -15.166 -18.779 1.00 27.16  ? 152 ILE A N   1 
ATOM   1297 C  CA  . ILE A 1 152 ? 6.633   -16.220 -17.750 1.00 30.15  ? 152 ILE A CA  1 
ATOM   1298 C  C   . ILE A 1 152 ? 5.424   -17.140 -17.858 1.00 36.88  ? 152 ILE A C   1 
ATOM   1299 O  O   . ILE A 1 152 ? 4.324   -16.696 -17.571 1.00 40.30  ? 152 ILE A O   1 
ATOM   1300 C  CB  . ILE A 1 152 ? 6.813   -15.655 -16.334 1.00 28.08  ? 152 ILE A CB  1 
ATOM   1301 C  CG1 . ILE A 1 152 ? 7.895   -14.570 -16.282 1.00 29.10  ? 152 ILE A CG1 1 
ATOM   1302 C  CG2 . ILE A 1 152 ? 7.101   -16.804 -15.380 1.00 27.66  ? 152 ILE A CG2 1 
ATOM   1303 C  CD1 . ILE A 1 152 ? 8.236   -14.088 -14.886 1.00 27.66  ? 152 ILE A CD1 1 
ATOM   1304 N  N   . ASP A 1 153 ? 5.661   -18.358 -18.327 1.00 46.50  ? 153 ASP A N   1 
ATOM   1305 C  CA  . ASP A 1 153 ? 4.641   -19.416 -18.457 1.00 52.37  ? 153 ASP A CA  1 
ATOM   1306 C  C   . ASP A 1 153 ? 5.153   -20.544 -17.556 1.00 55.81  ? 153 ASP A C   1 
ATOM   1307 O  O   . ASP A 1 153 ? 6.267   -21.026 -17.816 1.00 55.94  ? 153 ASP A O   1 
ATOM   1308 C  CB  . ASP A 1 153 ? 4.360   -19.674 -19.945 1.00 57.98  ? 153 ASP A CB  1 
ATOM   1309 C  CG  . ASP A 1 153 ? 3.523   -18.577 -20.606 1.00 64.78  ? 153 ASP A CG  1 
ATOM   1310 O  OD1 . ASP A 1 153 ? 2.499   -18.195 -20.019 1.00 72.25  ? 153 ASP A OD1 1 
ATOM   1311 O  OD2 . ASP A 1 153 ? 3.904   -18.089 -21.697 1.00 71.18  ? 153 ASP A OD2 1 
ATOM   1312 N  N   . TYR A 1 154 ? 4.432   -20.820 -16.456 1.00 57.35  ? 154 TYR A N   1 
ATOM   1313 C  CA  . TYR A 1 154 ? 4.614   -21.991 -15.552 1.00 64.70  ? 154 TYR A CA  1 
ATOM   1314 C  C   . TYR A 1 154 ? 6.043   -21.967 -14.965 1.00 63.86  ? 154 TYR A C   1 
ATOM   1315 O  O   . TYR A 1 154 ? 6.750   -22.989 -15.037 1.00 66.83  ? 154 TYR A O   1 
ATOM   1316 C  CB  . TYR A 1 154 ? 4.267   -23.299 -16.293 1.00 74.01  ? 154 TYR A CB  1 
ATOM   1317 C  CG  . TYR A 1 154 ? 3.161   -23.217 -17.328 1.00 86.56  ? 154 TYR A CG  1 
ATOM   1318 C  CD1 . TYR A 1 154 ? 1.825   -23.439 -17.002 1.00 87.04  ? 154 TYR A CD1 1 
ATOM   1319 C  CD2 . TYR A 1 154 ? 3.453   -22.922 -18.654 1.00 93.52  ? 154 TYR A CD2 1 
ATOM   1320 C  CE1 . TYR A 1 154 ? 0.821   -23.352 -17.959 1.00 90.55  ? 154 TYR A CE1 1 
ATOM   1321 C  CE2 . TYR A 1 154 ? 2.461   -22.824 -19.619 1.00 97.03  ? 154 TYR A CE2 1 
ATOM   1322 C  CZ  . TYR A 1 154 ? 1.141   -23.042 -19.274 1.00 97.07  ? 154 TYR A CZ  1 
ATOM   1323 O  OH  . TYR A 1 154 ? 0.193   -22.943 -20.254 1.00 99.39  ? 154 TYR A OH  1 
ATOM   1324 N  N   . ASP A 1 155 ? 6.471   -20.827 -14.402 1.00 59.24  ? 155 ASP A N   1 
ATOM   1325 C  CA  . ASP A 1 155 ? 7.768   -20.641 -13.678 1.00 55.54  ? 155 ASP A CA  1 
ATOM   1326 C  C   . ASP A 1 155 ? 8.977   -20.633 -14.634 1.00 48.73  ? 155 ASP A C   1 
ATOM   1327 O  O   . ASP A 1 155 ? 10.131  -20.490 -14.127 1.00 45.36  ? 155 ASP A O   1 
ATOM   1328 C  CB  . ASP A 1 155 ? 8.003   -21.705 -12.593 1.00 60.57  ? 155 ASP A CB  1 
ATOM   1329 C  CG  . ASP A 1 155 ? 7.242   -21.492 -11.288 1.00 69.84  ? 155 ASP A CG  1 
ATOM   1330 O  OD1 . ASP A 1 155 ? 7.178   -20.335 -10.808 1.00 75.12  ? 155 ASP A OD1 1 
ATOM   1331 O  OD2 . ASP A 1 155 ? 6.727   -22.494 -10.744 1.00 74.70  ? 155 ASP A OD2 1 
ATOM   1332 N  N   . CYS A 1 156 ? 8.778   -20.765 -15.953 1.00 41.43  ? 156 CYS A N   1 
ATOM   1333 C  CA  . CYS A 1 156 ? 9.889   -20.671 -16.944 1.00 39.25  ? 156 CYS A CA  1 
ATOM   1334 C  C   . CYS A 1 156 ? 9.874   -19.274 -17.570 1.00 32.69  ? 156 CYS A C   1 
ATOM   1335 O  O   . CYS A 1 156 ? 8.822   -18.901 -18.117 1.00 29.65  ? 156 CYS A O   1 
ATOM   1336 C  CB  . CYS A 1 156 ? 9.795   -21.704 -18.056 1.00 37.63  ? 156 CYS A CB  1 
ATOM   1337 S  SG  . CYS A 1 156 ? 11.187  -21.579 -19.218 1.00 42.89  ? 156 CYS A SG  1 
ATOM   1338 N  N   . VAL A 1 157 ? 10.988  -18.544 -17.473 1.00 31.06  ? 157 VAL A N   1 
ATOM   1339 C  CA  . VAL A 1 157 ? 11.119  -17.178 -18.060 1.00 27.97  ? 157 VAL A CA  1 
ATOM   1340 C  C   . VAL A 1 157 ? 11.562  -17.324 -19.517 1.00 28.64  ? 157 VAL A C   1 
ATOM   1341 O  O   . VAL A 1 157 ? 12.650  -17.867 -19.766 1.00 30.07  ? 157 VAL A O   1 
ATOM   1342 C  CB  . VAL A 1 157 ? 12.079  -16.299 -17.252 1.00 28.23  ? 157 VAL A CB  1 
ATOM   1343 C  CG1 . VAL A 1 157 ? 12.165  -14.903 -17.848 1.00 29.90  ? 157 VAL A CG1 1 
ATOM   1344 C  CG2 . VAL A 1 157 ? 11.690  -16.242 -15.776 1.00 27.68  ? 157 VAL A CG2 1 
ATOM   1345 N  N   . SER A 1 158 ? 10.753  -16.843 -20.459 1.00 26.09  ? 158 SER A N   1 
ATOM   1346 C  CA  . SER A 1 158 ? 11.153  -16.785 -21.874 1.00 27.03  ? 158 SER A CA  1 
ATOM   1347 C  C   . SER A 1 158 ? 11.610  -15.354 -22.202 1.00 28.73  ? 158 SER A C   1 
ATOM   1348 O  O   . SER A 1 158 ? 10.755  -14.442 -22.290 1.00 27.35  ? 158 SER A O   1 
ATOM   1349 C  CB  . SER A 1 158 ? 10.061  -17.267 -22.738 1.00 27.82  ? 158 SER A CB  1 
ATOM   1350 O  OG  . SER A 1 158 ? 8.913   -16.467 -22.537 1.00 38.44  ? 158 SER A OG  1 
ATOM   1351 N  N   . PHE A 1 159 ? 12.924  -15.154 -22.362 1.00 27.32  ? 159 PHE A N   1 
ATOM   1352 C  CA  . PHE A 1 159 ? 13.503  -13.866 -22.801 1.00 24.20  ? 159 PHE A CA  1 
ATOM   1353 C  C   . PHE A 1 159 ? 13.316  -13.707 -24.314 1.00 24.09  ? 159 PHE A C   1 
ATOM   1354 O  O   . PHE A 1 159 ? 13.739  -14.590 -25.098 1.00 25.52  ? 159 PHE A O   1 
ATOM   1355 C  CB  . PHE A 1 159 ? 14.959  -13.800 -22.360 1.00 25.99  ? 159 PHE A CB  1 
ATOM   1356 C  CG  . PHE A 1 159 ? 15.124  -13.765 -20.871 1.00 26.30  ? 159 PHE A CG  1 
ATOM   1357 C  CD1 . PHE A 1 159 ? 14.859  -12.601 -20.160 1.00 26.87  ? 159 PHE A CD1 1 
ATOM   1358 C  CD2 . PHE A 1 159 ? 15.562  -14.893 -20.191 1.00 26.70  ? 159 PHE A CD2 1 
ATOM   1359 C  CE1 . PHE A 1 159 ? 15.047  -12.562 -18.785 1.00 26.14  ? 159 PHE A CE1 1 
ATOM   1360 C  CE2 . PHE A 1 159 ? 15.746  -14.854 -18.819 1.00 26.42  ? 159 PHE A CE2 1 
ATOM   1361 C  CZ  . PHE A 1 159 ? 15.506  -13.688 -18.118 1.00 29.57  ? 159 PHE A CZ  1 
ATOM   1362 N  N   . CYS A 1 160 ? 12.697  -12.605 -24.736 1.00 24.55  ? 160 CYS A N   1 
ATOM   1363 C  CA  . CYS A 1 160 ? 12.363  -12.371 -26.156 1.00 23.63  ? 160 CYS A CA  1 
ATOM   1364 C  C   . CYS A 1 160 ? 12.872  -11.029 -26.682 1.00 23.94  ? 160 CYS A C   1 
ATOM   1365 O  O   . CYS A 1 160 ? 12.818  -10.863 -27.920 1.00 27.65  ? 160 CYS A O   1 
ATOM   1366 C  CB  . CYS A 1 160 ? 10.865  -12.449 -26.395 1.00 27.11  ? 160 CYS A CB  1 
ATOM   1367 S  SG  . CYS A 1 160 ? 9.903   -11.332 -25.344 1.00 27.39  ? 160 CYS A SG  1 
ATOM   1368 N  N   . TYR A 1 161 ? 13.332  -10.119 -25.821 1.00 24.17  ? 161 TYR A N   1 
ATOM   1369 C  CA  . TYR A 1 161 ? 13.743  -8.749  -26.222 1.00 23.00  ? 161 TYR A CA  1 
ATOM   1370 C  C   . TYR A 1 161 ? 14.886  -8.217  -25.344 1.00 21.36  ? 161 TYR A C   1 
ATOM   1371 O  O   . TYR A 1 161 ? 14.891  -8.386  -24.109 1.00 18.91  ? 161 TYR A O   1 
ATOM   1372 C  CB  . TYR A 1 161 ? 12.534  -7.804  -26.160 1.00 22.98  ? 161 TYR A CB  1 
ATOM   1373 C  CG  . TYR A 1 161 ? 12.814  -6.386  -26.603 1.00 20.68  ? 161 TYR A CG  1 
ATOM   1374 C  CD1 . TYR A 1 161 ? 12.780  -6.025  -27.935 1.00 22.15  ? 161 TYR A CD1 1 
ATOM   1375 C  CD2 . TYR A 1 161 ? 13.165  -5.414  -25.693 1.00 20.53  ? 161 TYR A CD2 1 
ATOM   1376 C  CE1 . TYR A 1 161 ? 13.065  -4.733  -28.351 1.00 20.89  ? 161 TYR A CE1 1 
ATOM   1377 C  CE2 . TYR A 1 161 ? 13.389  -4.097  -26.076 1.00 21.20  ? 161 TYR A CE2 1 
ATOM   1378 C  CZ  . TYR A 1 161 ? 13.368  -3.761  -27.416 1.00 22.30  ? 161 TYR A CZ  1 
ATOM   1379 O  OH  . TYR A 1 161 ? 13.606  -2.480  -27.825 1.00 22.53  ? 161 TYR A OH  1 
ATOM   1380 N  N   . MET A 1 162 ? 15.838  -7.538  -25.982 1.00 21.04  ? 162 MET A N   1 
ATOM   1381 C  CA  . MET A 1 162 ? 16.864  -6.724  -25.294 1.00 22.80  ? 162 MET A CA  1 
ATOM   1382 C  C   . MET A 1 162 ? 16.896  -5.368  -25.999 1.00 21.73  ? 162 MET A C   1 
ATOM   1383 O  O   . MET A 1 162 ? 16.996  -5.329  -27.232 1.00 22.25  ? 162 MET A O   1 
ATOM   1384 C  CB  . MET A 1 162 ? 18.250  -7.368  -25.339 1.00 25.17  ? 162 MET A CB  1 
ATOM   1385 C  CG  . MET A 1 162 ? 19.295  -6.497  -24.662 1.00 27.69  ? 162 MET A CG  1 
ATOM   1386 S  SD  . MET A 1 162 ? 20.904  -7.289  -24.421 1.00 27.22  ? 162 MET A SD  1 
ATOM   1387 C  CE  . MET A 1 162 ? 20.624  -8.048  -22.821 1.00 29.90  ? 162 MET A CE  1 
ATOM   1388 N  N   A HIS A 1 163 ? 16.821  -4.290  -25.220 0.31 22.08  ? 163 HIS A N   1 
ATOM   1389 N  N   B HIS A 1 163 ? 16.821  -4.290  -25.220 0.31 22.08  ? 163 HIS A N   1 
ATOM   1390 N  N   C HIS A 1 163 ? 16.805  -4.286  -25.220 0.19 22.45  ? 163 HIS A N   1 
ATOM   1391 N  N   D HIS A 1 163 ? 16.805  -4.286  -25.220 0.19 22.45  ? 163 HIS A N   1 
ATOM   1392 C  CA  A HIS A 1 163 ? 16.688  -2.900  -25.724 0.31 22.28  ? 163 HIS A CA  1 
ATOM   1393 C  CA  B HIS A 1 163 ? 16.688  -2.900  -25.724 0.31 22.28  ? 163 HIS A CA  1 
ATOM   1394 C  CA  C HIS A 1 163 ? 16.690  -2.881  -25.698 0.19 22.79  ? 163 HIS A CA  1 
ATOM   1395 C  CA  D HIS A 1 163 ? 16.690  -2.881  -25.698 0.19 22.79  ? 163 HIS A CA  1 
ATOM   1396 C  C   A HIS A 1 163 ? 18.051  -2.380  -26.198 0.31 22.67  ? 163 HIS A C   1 
ATOM   1397 C  C   B HIS A 1 163 ? 18.051  -2.380  -26.198 0.31 22.67  ? 163 HIS A C   1 
ATOM   1398 C  C   C HIS A 1 163 ? 18.053  -2.387  -26.199 0.19 22.82  ? 163 HIS A C   1 
ATOM   1399 C  C   D HIS A 1 163 ? 18.053  -2.387  -26.199 0.19 22.82  ? 163 HIS A C   1 
ATOM   1400 O  O   A HIS A 1 163 ? 19.018  -2.421  -25.409 0.31 22.74  ? 163 HIS A O   1 
ATOM   1401 O  O   B HIS A 1 163 ? 19.018  -2.421  -25.409 0.31 22.74  ? 163 HIS A O   1 
ATOM   1402 O  O   C HIS A 1 163 ? 19.032  -2.467  -25.426 0.19 22.75  ? 163 HIS A O   1 
ATOM   1403 O  O   D HIS A 1 163 ? 19.032  -2.467  -25.426 0.19 22.75  ? 163 HIS A O   1 
ATOM   1404 C  CB  A HIS A 1 163 ? 16.068  -1.987  -24.668 0.31 22.47  ? 163 HIS A CB  1 
ATOM   1405 C  CB  B HIS A 1 163 ? 16.068  -1.987  -24.668 0.31 22.47  ? 163 HIS A CB  1 
ATOM   1406 C  CB  C HIS A 1 163 ? 16.122  -1.986  -24.590 0.19 23.37  ? 163 HIS A CB  1 
ATOM   1407 C  CB  D HIS A 1 163 ? 16.122  -1.986  -24.590 0.19 23.37  ? 163 HIS A CB  1 
ATOM   1408 C  CG  A HIS A 1 163 ? 15.924  -0.587  -25.151 0.31 22.44  ? 163 HIS A CG  1 
ATOM   1409 C  CG  B HIS A 1 163 ? 15.924  -0.587  -25.151 0.31 22.44  ? 163 HIS A CG  1 
ATOM   1410 C  CG  C HIS A 1 163 ? 16.044  -0.541  -24.953 0.19 23.82  ? 163 HIS A CG  1 
ATOM   1411 C  CG  D HIS A 1 163 ? 16.044  -0.541  -24.953 0.19 23.82  ? 163 HIS A CG  1 
ATOM   1412 N  ND1 A HIS A 1 163 ? 15.107  -0.255  -26.215 0.31 22.39  ? 163 HIS A ND1 1 
ATOM   1413 N  ND1 B HIS A 1 163 ? 15.107  -0.255  -26.215 0.31 22.39  ? 163 HIS A ND1 1 
ATOM   1414 N  ND1 C HIS A 1 163 ? 15.448  -0.099  -26.119 0.19 24.33  ? 163 HIS A ND1 1 
ATOM   1415 N  ND1 D HIS A 1 163 ? 15.448  -0.099  -26.119 0.19 24.33  ? 163 HIS A ND1 1 
ATOM   1416 C  CD2 A HIS A 1 163 ? 16.503  0.560   -24.736 0.31 23.94  ? 163 HIS A CD2 1 
ATOM   1417 C  CD2 B HIS A 1 163 ? 16.503  0.560   -24.736 0.31 23.94  ? 163 HIS A CD2 1 
ATOM   1418 C  CD2 C HIS A 1 163 ? 16.460  0.563   -24.295 0.19 25.04  ? 163 HIS A CD2 1 
ATOM   1419 C  CD2 D HIS A 1 163 ? 16.460  0.563   -24.295 0.19 25.04  ? 163 HIS A CD2 1 
ATOM   1420 C  CE1 A HIS A 1 163 ? 15.191  1.045   -26.431 0.31 23.44  ? 163 HIS A CE1 1 
ATOM   1421 C  CE1 B HIS A 1 163 ? 15.191  1.045   -26.431 0.31 23.44  ? 163 HIS A CE1 1 
ATOM   1422 C  CE1 C HIS A 1 163 ? 15.522  1.217   -26.173 0.19 24.94  ? 163 HIS A CE1 1 
ATOM   1423 C  CE1 D HIS A 1 163 ? 15.522  1.217   -26.173 0.19 24.94  ? 163 HIS A CE1 1 
ATOM   1424 N  NE2 A HIS A 1 163 ? 16.036  1.570   -25.535 0.31 24.66  ? 163 HIS A NE2 1 
ATOM   1425 N  NE2 B HIS A 1 163 ? 16.036  1.570   -25.535 0.31 24.66  ? 163 HIS A NE2 1 
ATOM   1426 N  NE2 C HIS A 1 163 ? 16.133  1.647   -25.063 0.19 25.45  ? 163 HIS A NE2 1 
ATOM   1427 N  NE2 D HIS A 1 163 ? 16.133  1.647   -25.063 0.19 25.45  ? 163 HIS A NE2 1 
ATOM   1428 N  N   . HIS A 1 164 ? 18.105  -1.892  -27.441 1.00 21.64  ? 164 HIS A N   1 
ATOM   1429 C  CA  . HIS A 1 164 ? 19.340  -1.361  -28.060 1.00 24.02  ? 164 HIS A CA  1 
ATOM   1430 C  C   . HIS A 1 164 ? 19.301  0.143   -28.322 1.00 25.27  ? 164 HIS A C   1 
ATOM   1431 O  O   . HIS A 1 164 ? 20.328  0.798   -28.060 1.00 26.16  ? 164 HIS A O   1 
ATOM   1432 C  CB  . HIS A 1 164 ? 19.704  -2.127  -29.341 1.00 23.16  ? 164 HIS A CB  1 
ATOM   1433 C  CG  . HIS A 1 164 ? 20.296  -3.474  -29.103 1.00 23.30  ? 164 HIS A CG  1 
ATOM   1434 N  ND1 . HIS A 1 164 ? 21.605  -3.809  -29.482 1.00 23.10  ? 164 HIS A ND1 1 
ATOM   1435 C  CD2 . HIS A 1 164 ? 19.781  -4.577  -28.530 1.00 21.62  ? 164 HIS A CD2 1 
ATOM   1436 C  CE1 . HIS A 1 164 ? 21.829  -5.068  -29.160 1.00 21.81  ? 164 HIS A CE1 1 
ATOM   1437 N  NE2 . HIS A 1 164 ? 20.735  -5.559  -28.594 1.00 21.61  ? 164 HIS A NE2 1 
ATOM   1438 N  N   A MET A 1 165 ? 18.165  0.694   -28.763 0.31 26.10  ? 165 MET A N   1 
ATOM   1439 N  N   B MET A 1 165 ? 18.165  0.694   -28.763 0.31 26.10  ? 165 MET A N   1 
ATOM   1440 N  N   C MET A 1 165 ? 18.211  0.683   -28.882 0.19 26.72  ? 165 MET A N   1 
ATOM   1441 N  N   D MET A 1 165 ? 18.211  0.683   -28.882 0.19 26.72  ? 165 MET A N   1 
ATOM   1442 C  CA  A MET A 1 165 ? 18.150  2.096   -29.258 0.31 27.40  ? 165 MET A CA  1 
ATOM   1443 C  CA  B MET A 1 165 ? 18.150  2.096   -29.258 0.31 27.40  ? 165 MET A CA  1 
ATOM   1444 C  CA  C MET A 1 165 ? 18.207  2.087   -29.385 0.19 27.92  ? 165 MET A CA  1 
ATOM   1445 C  CA  D MET A 1 165 ? 18.207  2.087   -29.385 0.19 27.92  ? 165 MET A CA  1 
ATOM   1446 C  C   A MET A 1 165 ? 16.735  2.667   -29.419 0.31 26.17  ? 165 MET A C   1 
ATOM   1447 C  C   B MET A 1 165 ? 16.735  2.667   -29.419 0.31 26.17  ? 165 MET A C   1 
ATOM   1448 C  C   C MET A 1 165 ? 16.790  2.668   -29.509 0.19 27.36  ? 165 MET A C   1 
ATOM   1449 C  C   D MET A 1 165 ? 16.790  2.668   -29.509 0.19 27.36  ? 165 MET A C   1 
ATOM   1450 O  O   A MET A 1 165 ? 15.753  1.904   -29.491 0.31 23.60  ? 165 MET A O   1 
ATOM   1451 O  O   B MET A 1 165 ? 15.753  1.904   -29.491 0.31 23.60  ? 165 MET A O   1 
ATOM   1452 O  O   C MET A 1 165 ? 15.817  1.895   -29.618 0.19 25.84  ? 165 MET A O   1 
ATOM   1453 O  O   D MET A 1 165 ? 15.817  1.895   -29.618 0.19 25.84  ? 165 MET A O   1 
ATOM   1454 C  CB  A MET A 1 165 ? 18.882  2.177   -30.601 0.31 28.93  ? 165 MET A CB  1 
ATOM   1455 C  CB  B MET A 1 165 ? 18.882  2.177   -30.601 0.31 28.93  ? 165 MET A CB  1 
ATOM   1456 C  CB  C MET A 1 165 ? 18.917  2.185   -30.741 0.19 29.25  ? 165 MET A CB  1 
ATOM   1457 C  CB  D MET A 1 165 ? 18.917  2.185   -30.741 0.19 29.25  ? 165 MET A CB  1 
ATOM   1458 C  CG  A MET A 1 165 ? 18.341  1.223   -31.641 0.31 31.25  ? 165 MET A CG  1 
ATOM   1459 C  CG  B MET A 1 165 ? 18.341  1.223   -31.641 0.31 31.25  ? 165 MET A CG  1 
ATOM   1460 C  CG  C MET A 1 165 ? 18.376  1.257   -31.813 0.19 30.98  ? 165 MET A CG  1 
ATOM   1461 C  CG  D MET A 1 165 ? 18.376  1.257   -31.813 0.19 30.98  ? 165 MET A CG  1 
ATOM   1462 S  SD  A MET A 1 165 ? 19.451  1.085   -33.060 0.31 38.44  ? 165 MET A SD  1 
ATOM   1463 S  SD  B MET A 1 165 ? 19.451  1.085   -33.060 0.31 38.44  ? 165 MET A SD  1 
ATOM   1464 S  SD  C MET A 1 165 ? 19.275  1.492   -33.373 0.19 35.19  ? 165 MET A SD  1 
ATOM   1465 S  SD  D MET A 1 165 ? 19.275  1.492   -33.373 0.19 35.19  ? 165 MET A SD  1 
ATOM   1466 C  CE  A MET A 1 165 ? 18.329  0.417   -34.286 0.31 38.00  ? 165 MET A CE  1 
ATOM   1467 C  CE  B MET A 1 165 ? 18.329  0.417   -34.286 0.31 38.00  ? 165 MET A CE  1 
ATOM   1468 C  CE  C MET A 1 165 ? 18.293  0.499   -34.493 0.19 35.16  ? 165 MET A CE  1 
ATOM   1469 C  CE  D MET A 1 165 ? 18.293  0.499   -34.493 0.19 35.16  ? 165 MET A CE  1 
ATOM   1470 N  N   A GLU A 1 166 ? 16.662  3.998   -29.473 0.31 27.49  ? 166 GLU A N   1 
ATOM   1471 N  N   B GLU A 1 166 ? 16.662  3.998   -29.473 0.31 27.49  ? 166 GLU A N   1 
ATOM   1472 N  N   C GLU A 1 166 ? 16.702  4.003   -29.484 0.19 28.26  ? 166 GLU A N   1 
ATOM   1473 N  N   D GLU A 1 166 ? 16.702  4.003   -29.484 0.19 28.26  ? 166 GLU A N   1 
ATOM   1474 C  CA  A GLU A 1 166 ? 15.424  4.770   -29.751 0.31 27.85  ? 166 GLU A CA  1 
ATOM   1475 C  CA  B GLU A 1 166 ? 15.424  4.770   -29.751 0.31 27.85  ? 166 GLU A CA  1 
ATOM   1476 C  CA  C GLU A 1 166 ? 15.469  4.790   -29.762 0.19 28.61  ? 166 GLU A CA  1 
ATOM   1477 C  CA  D GLU A 1 166 ? 15.469  4.790   -29.762 0.19 28.61  ? 166 GLU A CA  1 
ATOM   1478 C  C   A GLU A 1 166 ? 15.557  5.403   -31.137 0.31 27.95  ? 166 GLU A C   1 
ATOM   1479 C  C   B GLU A 1 166 ? 15.557  5.403   -31.137 0.31 27.95  ? 166 GLU A C   1 
ATOM   1480 C  C   C GLU A 1 166 ? 15.579  5.394   -31.161 0.19 28.54  ? 166 GLU A C   1 
ATOM   1481 C  C   D GLU A 1 166 ? 15.579  5.394   -31.161 0.19 28.54  ? 166 GLU A C   1 
ATOM   1482 O  O   A GLU A 1 166 ? 16.576  6.078   -31.380 0.31 27.98  ? 166 GLU A O   1 
ATOM   1483 O  O   B GLU A 1 166 ? 16.576  6.078   -31.380 0.31 27.98  ? 166 GLU A O   1 
ATOM   1484 O  O   C GLU A 1 166 ? 16.600  6.057   -31.434 0.19 28.44  ? 166 GLU A O   1 
ATOM   1485 O  O   D GLU A 1 166 ? 16.600  6.057   -31.434 0.19 28.44  ? 166 GLU A O   1 
ATOM   1486 C  CB  A GLU A 1 166 ? 15.183  5.832   -28.678 0.31 28.70  ? 166 GLU A CB  1 
ATOM   1487 C  CB  B GLU A 1 166 ? 15.183  5.832   -28.678 0.31 28.70  ? 166 GLU A CB  1 
ATOM   1488 C  CB  C GLU A 1 166 ? 15.272  5.919   -28.750 0.19 29.35  ? 166 GLU A CB  1 
ATOM   1489 C  CB  D GLU A 1 166 ? 15.272  5.919   -28.750 0.19 29.35  ? 166 GLU A CB  1 
ATOM   1490 C  CG  A GLU A 1 166 ? 13.866  6.576   -28.878 0.31 28.96  ? 166 GLU A CG  1 
ATOM   1491 C  CG  B GLU A 1 166 ? 13.866  6.576   -28.878 0.31 28.96  ? 166 GLU A CG  1 
ATOM   1492 C  CG  C GLU A 1 166 ? 13.915  6.600   -28.863 0.19 29.80  ? 166 GLU A CG  1 
ATOM   1493 C  CG  D GLU A 1 166 ? 13.915  6.600   -28.863 0.19 29.80  ? 166 GLU A CG  1 
ATOM   1494 C  CD  A GLU A 1 166 ? 13.469  7.498   -27.740 0.31 29.65  ? 166 GLU A CD  1 
ATOM   1495 C  CD  B GLU A 1 166 ? 13.469  7.498   -27.740 0.31 29.65  ? 166 GLU A CD  1 
ATOM   1496 C  CD  C GLU A 1 166 ? 13.532  7.445   -27.660 0.19 30.46  ? 166 GLU A CD  1 
ATOM   1497 C  CD  D GLU A 1 166 ? 13.532  7.445   -27.660 0.19 30.46  ? 166 GLU A CD  1 
ATOM   1498 O  OE1 A GLU A 1 166 ? 13.311  7.009   -26.602 0.31 28.52  ? 166 GLU A OE1 1 
ATOM   1499 O  OE1 B GLU A 1 166 ? 13.311  7.009   -26.602 0.31 28.52  ? 166 GLU A OE1 1 
ATOM   1500 O  OE1 C GLU A 1 166 ? 13.593  6.924   -26.525 0.19 30.16  ? 166 GLU A OE1 1 
ATOM   1501 O  OE1 D GLU A 1 166 ? 13.593  6.924   -26.525 0.19 30.16  ? 166 GLU A OE1 1 
ATOM   1502 O  OE2 A GLU A 1 166 ? 13.341  8.706   -27.993 0.31 30.08  ? 166 GLU A OE2 1 
ATOM   1503 O  OE2 B GLU A 1 166 ? 13.341  8.706   -27.993 0.31 30.08  ? 166 GLU A OE2 1 
ATOM   1504 O  OE2 C GLU A 1 166 ? 13.187  8.623   -27.859 0.19 30.91  ? 166 GLU A OE2 1 
ATOM   1505 O  OE2 D GLU A 1 166 ? 13.187  8.623   -27.859 0.19 30.91  ? 166 GLU A OE2 1 
ATOM   1506 N  N   . LEU A 1 167 ? 14.570  5.171   -32.004 1.00 28.43  ? 167 LEU A N   1 
ATOM   1507 C  CA  . LEU A 1 167 ? 14.551  5.714   -33.383 1.00 30.68  ? 167 LEU A CA  1 
ATOM   1508 C  C   . LEU A 1 167 ? 14.021  7.145   -33.343 1.00 34.02  ? 167 LEU A C   1 
ATOM   1509 O  O   . LEU A 1 167 ? 13.447  7.568   -32.345 1.00 31.26  ? 167 LEU A O   1 
ATOM   1510 C  CB  . LEU A 1 167 ? 13.704  4.778   -34.244 1.00 31.01  ? 167 LEU A CB  1 
ATOM   1511 C  CG  . LEU A 1 167 ? 14.268  3.364   -34.400 1.00 36.13  ? 167 LEU A CG  1 
ATOM   1512 C  CD1 . LEU A 1 167 ? 13.166  2.398   -34.828 1.00 39.49  ? 167 LEU A CD1 1 
ATOM   1513 C  CD2 . LEU A 1 167 ? 15.419  3.337   -35.394 1.00 36.81  ? 167 LEU A CD2 1 
ATOM   1514 N  N   . PRO A 1 168 ? 14.205  7.940   -34.422 1.00 39.45  ? 168 PRO A N   1 
ATOM   1515 C  CA  . PRO A 1 168 ? 13.811  9.353   -34.423 1.00 40.01  ? 168 PRO A CA  1 
ATOM   1516 C  C   . PRO A 1 168 ? 12.365  9.646   -33.999 1.00 38.60  ? 168 PRO A C   1 
ATOM   1517 O  O   . PRO A 1 168 ? 12.154  10.675  -33.423 1.00 40.30  ? 168 PRO A O   1 
ATOM   1518 C  CB  . PRO A 1 168 ? 14.033  9.777   -35.884 1.00 44.88  ? 168 PRO A CB  1 
ATOM   1519 C  CG  . PRO A 1 168 ? 15.183  8.882   -36.351 1.00 46.31  ? 168 PRO A CG  1 
ATOM   1520 C  CD  . PRO A 1 168 ? 14.944  7.560   -35.638 1.00 44.27  ? 168 PRO A CD  1 
ATOM   1521 N  N   . THR A 1 169 ? 11.416  8.745   -34.252 1.00 35.71  ? 169 THR A N   1 
ATOM   1522 C  CA  . THR A 1 169 ? 9.984   8.962   -33.918 1.00 36.01  ? 169 THR A CA  1 
ATOM   1523 C  C   . THR A 1 169 ? 9.668   8.643   -32.445 1.00 34.75  ? 169 THR A C   1 
ATOM   1524 O  O   . THR A 1 169 ? 8.473   8.659   -32.093 1.00 31.23  ? 169 THR A O   1 
ATOM   1525 C  CB  . THR A 1 169 ? 9.116   8.146   -34.876 1.00 40.33  ? 169 THR A CB  1 
ATOM   1526 O  OG1 . THR A 1 169 ? 9.514   6.794   -34.643 1.00 44.25  ? 169 THR A OG1 1 
ATOM   1527 C  CG2 . THR A 1 169 ? 9.304   8.559   -36.326 1.00 36.70  ? 169 THR A CG2 1 
ATOM   1528 N  N   . GLY A 1 170 ? 10.656  8.337   -31.598 1.00 32.07  ? 170 GLY A N   1 
ATOM   1529 C  CA  . GLY A 1 170 ? 10.413  8.045   -30.166 1.00 31.14  ? 170 GLY A CA  1 
ATOM   1530 C  C   . GLY A 1 170 ? 10.030  6.586   -29.856 1.00 33.04  ? 170 GLY A C   1 
ATOM   1531 O  O   . GLY A 1 170 ? 9.710   6.319   -28.671 1.00 37.47  ? 170 GLY A O   1 
ATOM   1532 N  N   . VAL A 1 171 ? 10.088  5.666   -30.834 1.00 29.04  ? 171 VAL A N   1 
ATOM   1533 C  CA  . VAL A 1 171 ? 9.814   4.204   -30.667 1.00 28.01  ? 171 VAL A CA  1 
ATOM   1534 C  C   . VAL A 1 171 ? 11.171  3.481   -30.581 1.00 26.41  ? 171 VAL A C   1 
ATOM   1535 O  O   . VAL A 1 171 ? 12.200  4.055   -30.950 1.00 24.02  ? 171 VAL A O   1 
ATOM   1536 C  CB  . VAL A 1 171 ? 8.940   3.649   -31.805 1.00 29.19  ? 171 VAL A CB  1 
ATOM   1537 C  CG1 . VAL A 1 171 ? 7.596   4.353   -31.865 1.00 34.72  ? 171 VAL A CG1 1 
ATOM   1538 C  CG2 . VAL A 1 171 ? 9.632   3.703   -33.147 1.00 29.85  ? 171 VAL A CG2 1 
ATOM   1539 N  N   A HIS A 1 172 ? 11.144  2.219   -30.151 0.31 25.67  ? 172 HIS A N   1 
ATOM   1540 N  N   B HIS A 1 172 ? 11.144  2.219   -30.151 0.31 25.67  ? 172 HIS A N   1 
ATOM   1541 N  N   C HIS A 1 172 ? 11.170  2.248   -30.069 0.19 25.76  ? 172 HIS A N   1 
ATOM   1542 N  N   D HIS A 1 172 ? 11.170  2.248   -30.069 0.19 25.76  ? 172 HIS A N   1 
ATOM   1543 C  CA  A HIS A 1 172 ? 12.330  1.482   -29.639 0.31 24.76  ? 172 HIS A CA  1 
ATOM   1544 C  CA  B HIS A 1 172 ? 12.330  1.482   -29.639 0.31 24.76  ? 172 HIS A CA  1 
ATOM   1545 C  CA  C HIS A 1 172 ? 12.402  1.531   -29.639 0.19 25.08  ? 172 HIS A CA  1 
ATOM   1546 C  CA  D HIS A 1 172 ? 12.402  1.531   -29.639 0.19 25.08  ? 172 HIS A CA  1 
ATOM   1547 C  C   A HIS A 1 172 ? 12.613  0.252   -30.507 0.31 24.55  ? 172 HIS A C   1 
ATOM   1548 C  C   B HIS A 1 172 ? 12.613  0.252   -30.507 0.31 24.55  ? 172 HIS A C   1 
ATOM   1549 C  C   C HIS A 1 172 ? 12.624  0.276   -30.488 0.19 24.61  ? 172 HIS A C   1 
ATOM   1550 C  C   D HIS A 1 172 ? 12.624  0.276   -30.488 0.19 24.61  ? 172 HIS A C   1 
ATOM   1551 O  O   A HIS A 1 172 ? 11.646  -0.357  -31.027 0.31 21.82  ? 172 HIS A O   1 
ATOM   1552 O  O   B HIS A 1 172 ? 11.646  -0.357  -31.027 0.31 21.82  ? 172 HIS A O   1 
ATOM   1553 O  O   C HIS A 1 172 ? 11.632  -0.329  -30.957 0.19 23.05  ? 172 HIS A O   1 
ATOM   1554 O  O   D HIS A 1 172 ? 11.632  -0.329  -30.957 0.19 23.05  ? 172 HIS A O   1 
ATOM   1555 C  CB  A HIS A 1 172 ? 12.110  1.204   -28.151 0.31 25.49  ? 172 HIS A CB  1 
ATOM   1556 C  CB  B HIS A 1 172 ? 12.110  1.204   -28.151 0.31 25.49  ? 172 HIS A CB  1 
ATOM   1557 C  CB  C HIS A 1 172 ? 12.343  1.269   -28.130 0.19 25.74  ? 172 HIS A CB  1 
ATOM   1558 C  CB  D HIS A 1 172 ? 12.343  1.269   -28.130 0.19 25.74  ? 172 HIS A CB  1 
ATOM   1559 C  CG  A HIS A 1 172 ? 11.878  2.474   -27.402 0.31 26.01  ? 172 HIS A CG  1 
ATOM   1560 C  CG  B HIS A 1 172 ? 11.878  2.474   -27.402 0.31 26.01  ? 172 HIS A CG  1 
ATOM   1561 C  CG  C HIS A 1 172 ? 11.962  2.498   -27.375 0.19 26.06  ? 172 HIS A CG  1 
ATOM   1562 C  CG  D HIS A 1 172 ? 11.962  2.498   -27.375 0.19 26.06  ? 172 HIS A CG  1 
ATOM   1563 N  ND1 A HIS A 1 172 ? 10.639  2.826   -26.914 0.31 25.72  ? 172 HIS A ND1 1 
ATOM   1564 N  ND1 B HIS A 1 172 ? 10.639  2.826   -26.914 0.31 25.72  ? 172 HIS A ND1 1 
ATOM   1565 N  ND1 C HIS A 1 172 ? 10.686  2.699   -26.898 0.19 25.92  ? 172 HIS A ND1 1 
ATOM   1566 N  ND1 D HIS A 1 172 ? 10.686  2.699   -26.898 0.19 25.92  ? 172 HIS A ND1 1 
ATOM   1567 C  CD2 A HIS A 1 172 ? 12.702  3.510   -27.128 0.31 26.30  ? 172 HIS A CD2 1 
ATOM   1568 C  CD2 B HIS A 1 172 ? 12.702  3.510   -27.128 0.31 26.30  ? 172 HIS A CD2 1 
ATOM   1569 C  CD2 C HIS A 1 172 ? 12.661  3.616   -27.078 0.19 26.27  ? 172 HIS A CD2 1 
ATOM   1570 C  CD2 D HIS A 1 172 ? 12.661  3.616   -27.078 0.19 26.27  ? 172 HIS A CD2 1 
ATOM   1571 C  CE1 A HIS A 1 172 ? 10.717  4.008   -26.339 0.31 26.16  ? 172 HIS A CE1 1 
ATOM   1572 C  CE1 B HIS A 1 172 ? 10.717  4.008   -26.339 0.31 26.16  ? 172 HIS A CE1 1 
ATOM   1573 C  CE1 C HIS A 1 172 ? 10.621  3.875   -26.311 0.19 26.22  ? 172 HIS A CE1 1 
ATOM   1574 C  CE1 D HIS A 1 172 ? 10.621  3.875   -26.311 0.19 26.22  ? 172 HIS A CE1 1 
ATOM   1575 N  NE2 A HIS A 1 172 ? 11.972  4.447   -26.453 0.31 25.59  ? 172 HIS A NE2 1 
ATOM   1576 N  NE2 B HIS A 1 172 ? 11.972  4.447   -26.453 0.31 25.59  ? 172 HIS A NE2 1 
ATOM   1577 N  NE2 C HIS A 1 172 ? 11.821  4.456   -26.403 0.19 25.94  ? 172 HIS A NE2 1 
ATOM   1578 N  NE2 D HIS A 1 172 ? 11.821  4.456   -26.403 0.19 25.94  ? 172 HIS A NE2 1 
ATOM   1579 N  N   . ALA A 1 173 ? 13.902  -0.064  -30.678 1.00 23.38  ? 173 ALA A N   1 
ATOM   1580 C  CA  . ALA A 1 173 ? 14.364  -1.183  -31.491 1.00 22.84  ? 173 ALA A CA  1 
ATOM   1581 C  C   . ALA A 1 173 ? 15.377  -1.972  -30.655 1.00 21.27  ? 173 ALA A C   1 
ATOM   1582 O  O   . ALA A 1 173 ? 16.125  -1.378  -29.797 1.00 18.60  ? 173 ALA A O   1 
ATOM   1583 C  CB  . ALA A 1 173 ? 14.920  -0.628  -32.788 1.00 24.00  ? 173 ALA A CB  1 
ATOM   1584 N  N   . GLY A 1 174 ? 15.331  -3.280  -30.837 1.00 19.79  ? 174 GLY A N   1 
ATOM   1585 C  CA  . GLY A 1 174 ? 16.223  -4.197  -30.134 1.00 20.32  ? 174 GLY A CA  1 
ATOM   1586 C  C   . GLY A 1 174 ? 16.265  -5.556  -30.799 1.00 20.95  ? 174 GLY A C   1 
ATOM   1587 O  O   . GLY A 1 174 ? 15.755  -5.722  -31.952 1.00 22.01  ? 174 GLY A O   1 
ATOM   1588 N  N   . THR A 1 175 ? 16.856  -6.501  -30.072 1.00 20.50  ? 175 THR A N   1 
ATOM   1589 C  CA  . THR A 1 175 ? 17.213  -7.846  -30.565 1.00 21.02  ? 175 THR A CA  1 
ATOM   1590 C  C   . THR A 1 175 ? 16.504  -8.875  -29.722 1.00 22.22  ? 175 THR A C   1 
ATOM   1591 O  O   . THR A 1 175 ? 16.136  -8.553  -28.574 1.00 22.68  ? 175 THR A O   1 
ATOM   1592 C  CB  . THR A 1 175 ? 18.727  -8.087  -30.448 1.00 22.10  ? 175 THR A CB  1 
ATOM   1593 O  OG1 . THR A 1 175 ? 19.177  -8.048  -29.083 1.00 20.02  ? 175 THR A OG1 1 
ATOM   1594 C  CG2 . THR A 1 175 ? 19.487  -7.056  -31.238 1.00 20.94  ? 175 THR A CG2 1 
ATOM   1595 N  N   . ASP A 1 176 ? 16.431  -10.098 -30.227 1.00 22.16  ? 176 ASP A N   1 
ATOM   1596 C  CA  . ASP A 1 176 ? 16.256  -11.286 -29.361 1.00 21.23  ? 176 ASP A CA  1 
ATOM   1597 C  C   . ASP A 1 176 ? 17.563  -11.512 -28.582 1.00 21.68  ? 176 ASP A C   1 
ATOM   1598 O  O   . ASP A 1 176 ? 18.565  -10.749 -28.764 1.00 21.09  ? 176 ASP A O   1 
ATOM   1599 C  CB  . ASP A 1 176 ? 15.831  -12.499 -30.192 1.00 24.00  ? 176 ASP A CB  1 
ATOM   1600 C  CG  . ASP A 1 176 ? 16.854  -12.902 -31.248 1.00 25.57  ? 176 ASP A CG  1 
ATOM   1601 O  OD1 . ASP A 1 176 ? 18.081  -12.673 -31.047 1.00 27.03  ? 176 ASP A OD1 1 
ATOM   1602 O  OD2 . ASP A 1 176 ? 16.411  -13.368 -32.291 1.00 27.56  ? 176 ASP A OD2 1 
ATOM   1603 N  N   . LEU A 1 177 ? 17.570  -12.531 -27.723 1.00 22.03  ? 177 LEU A N   1 
ATOM   1604 C  CA  . LEU A 1 177 ? 18.704  -12.805 -26.828 1.00 24.02  ? 177 LEU A CA  1 
ATOM   1605 C  C   . LEU A 1 177 ? 19.752  -13.613 -27.573 1.00 23.40  ? 177 LEU A C   1 
ATOM   1606 O  O   . LEU A 1 177 ? 20.766  -13.874 -26.939 1.00 25.60  ? 177 LEU A O   1 
ATOM   1607 C  CB  . LEU A 1 177 ? 18.241  -13.493 -25.537 1.00 24.98  ? 177 LEU A CB  1 
ATOM   1608 C  CG  . LEU A 1 177 ? 17.852  -12.518 -24.428 1.00 26.55  ? 177 LEU A CG  1 
ATOM   1609 C  CD1 . LEU A 1 177 ? 19.061  -11.850 -23.837 1.00 28.94  ? 177 LEU A CD1 1 
ATOM   1610 C  CD2 . LEU A 1 177 ? 16.864  -11.472 -24.936 1.00 27.51  ? 177 LEU A CD2 1 
ATOM   1611 N  N   . GLU A 1 178 ? 19.566  -13.869 -28.874 1.00 25.14  ? 178 GLU A N   1 
ATOM   1612 C  CA  . GLU A 1 178 ? 20.658  -14.353 -29.775 1.00 27.22  ? 178 GLU A CA  1 
ATOM   1613 C  C   . GLU A 1 178 ? 21.276  -13.190 -30.566 1.00 25.21  ? 178 GLU A C   1 
ATOM   1614 O  O   . GLU A 1 178 ? 22.136  -13.463 -31.455 1.00 23.18  ? 178 GLU A O   1 
ATOM   1615 C  CB  . GLU A 1 178 ? 20.145  -15.446 -30.710 1.00 29.47  ? 178 GLU A CB  1 
ATOM   1616 C  CG  . GLU A 1 178 ? 19.725  -16.698 -29.955 1.00 35.48  ? 178 GLU A CG  1 
ATOM   1617 C  CD  . GLU A 1 178 ? 19.220  -17.863 -30.795 1.00 38.44  ? 178 GLU A CD  1 
ATOM   1618 O  OE1 . GLU A 1 178 ? 18.784  -17.637 -31.952 1.00 41.82  ? 178 GLU A OE1 1 
ATOM   1619 O  OE2 . GLU A 1 178 ? 19.234  -18.992 -30.270 1.00 44.58  ? 178 GLU A OE2 1 
ATOM   1620 N  N   . GLY A 1 179 ? 20.885  -11.943 -30.274 1.00 24.20  ? 179 GLY A N   1 
ATOM   1621 C  CA  . GLY A 1 179 ? 21.522  -10.738 -30.859 1.00 23.26  ? 179 GLY A CA  1 
ATOM   1622 C  C   . GLY A 1 179 ? 20.972  -10.359 -32.221 1.00 24.95  ? 179 GLY A C   1 
ATOM   1623 O  O   . GLY A 1 179 ? 21.542  -9.431  -32.849 1.00 23.69  ? 179 GLY A O   1 
ATOM   1624 N  N   . ASN A 1 180 ? 19.913  -11.016 -32.714 1.00 24.89  ? 180 ASN A N   1 
ATOM   1625 C  CA  . ASN A 1 180 ? 19.338  -10.638 -34.031 1.00 26.53  ? 180 ASN A CA  1 
ATOM   1626 C  C   . ASN A 1 180 ? 18.274  -9.569  -33.816 1.00 26.19  ? 180 ASN A C   1 
ATOM   1627 O  O   . ASN A 1 180 ? 17.352  -9.791  -32.999 1.00 24.82  ? 180 ASN A O   1 
ATOM   1628 C  CB  . ASN A 1 180 ? 18.761  -11.831 -34.774 1.00 31.71  ? 180 ASN A CB  1 
ATOM   1629 C  CG  . ASN A 1 180 ? 19.853  -12.770 -35.233 1.00 32.95  ? 180 ASN A CG  1 
ATOM   1630 O  OD1 . ASN A 1 180 ? 19.831  -13.938 -34.886 1.00 36.60  ? 180 ASN A OD1 1 
ATOM   1631 N  ND2 . ASN A 1 180 ? 20.820  -12.250 -35.960 1.00 33.39  ? 180 ASN A ND2 1 
ATOM   1632 N  N   . PHE A 1 181 ? 18.423  -8.443  -34.508 1.00 24.99  ? 181 PHE A N   1 
ATOM   1633 C  CA  . PHE A 1 181 ? 17.457  -7.326  -34.482 1.00 25.18  ? 181 PHE A CA  1 
ATOM   1634 C  C   . PHE A 1 181 ? 16.082  -7.846  -34.918 1.00 24.98  ? 181 PHE A C   1 
ATOM   1635 O  O   . PHE A 1 181 ? 15.980  -8.738  -35.801 1.00 25.47  ? 181 PHE A O   1 
ATOM   1636 C  CB  . PHE A 1 181 ? 17.917  -6.141  -35.331 1.00 23.49  ? 181 PHE A CB  1 
ATOM   1637 C  CG  . PHE A 1 181 ? 18.607  -5.071  -34.526 1.00 22.09  ? 181 PHE A CG  1 
ATOM   1638 C  CD1 . PHE A 1 181 ? 17.889  -4.088  -33.870 1.00 22.70  ? 181 PHE A CD1 1 
ATOM   1639 C  CD2 . PHE A 1 181 ? 19.982  -5.098  -34.369 1.00 23.19  ? 181 PHE A CD2 1 
ATOM   1640 C  CE1 . PHE A 1 181 ? 18.539  -3.133  -33.101 1.00 22.69  ? 181 PHE A CE1 1 
ATOM   1641 C  CE2 . PHE A 1 181 ? 20.626  -4.137  -33.610 1.00 23.28  ? 181 PHE A CE2 1 
ATOM   1642 C  CZ  . PHE A 1 181 ? 19.900  -3.165  -32.969 1.00 21.50  ? 181 PHE A CZ  1 
ATOM   1643 N  N   . TYR A 1 182 ? 15.047  -7.303  -34.286 1.00 22.10  ? 182 TYR A N   1 
ATOM   1644 C  CA  . TYR A 1 182 ? 13.669  -7.286  -34.828 1.00 21.48  ? 182 TYR A CA  1 
ATOM   1645 C  C   . TYR A 1 182 ? 13.617  -6.181  -35.875 1.00 22.31  ? 182 TYR A C   1 
ATOM   1646 O  O   . TYR A 1 182 ? 13.975  -5.053  -35.577 1.00 24.11  ? 182 TYR A O   1 
ATOM   1647 C  CB  . TYR A 1 182 ? 12.651  -7.063  -33.704 1.00 23.28  ? 182 TYR A CB  1 
ATOM   1648 C  CG  . TYR A 1 182 ? 12.546  -8.225  -32.754 1.00 22.58  ? 182 TYR A CG  1 
ATOM   1649 C  CD1 . TYR A 1 182 ? 11.876  -9.385  -33.137 1.00 22.33  ? 182 TYR A CD1 1 
ATOM   1650 C  CD2 . TYR A 1 182 ? 13.156  -8.200  -31.505 1.00 23.97  ? 182 TYR A CD2 1 
ATOM   1651 C  CE1 . TYR A 1 182 ? 11.783  -10.468 -32.284 1.00 20.82  ? 182 TYR A CE1 1 
ATOM   1652 C  CE2 . TYR A 1 182 ? 13.060  -9.281  -30.634 1.00 21.27  ? 182 TYR A CE2 1 
ATOM   1653 C  CZ  . TYR A 1 182 ? 12.358  -10.415 -31.028 1.00 21.51  ? 182 TYR A CZ  1 
ATOM   1654 O  OH  . TYR A 1 182 ? 12.227  -11.509 -30.212 1.00 20.95  ? 182 TYR A OH  1 
ATOM   1655 N  N   . GLY A 1 183 ? 13.210  -6.504  -37.082 1.00 22.52  ? 183 GLY A N   1 
ATOM   1656 C  CA  . GLY A 1 183 ? 13.009  -5.506  -38.140 1.00 24.33  ? 183 GLY A CA  1 
ATOM   1657 C  C   . GLY A 1 183 ? 14.292  -5.207  -38.890 1.00 26.71  ? 183 GLY A C   1 
ATOM   1658 O  O   . GLY A 1 183 ? 15.323  -5.827  -38.658 1.00 28.87  ? 183 GLY A O   1 
ATOM   1659 N  N   . PRO A 1 184 ? 14.264  -4.220  -39.799 1.00 28.68  ? 184 PRO A N   1 
ATOM   1660 C  CA  . PRO A 1 184 ? 15.429  -3.933  -40.639 1.00 30.86  ? 184 PRO A CA  1 
ATOM   1661 C  C   . PRO A 1 184 ? 16.532  -3.091  -39.970 1.00 31.11  ? 184 PRO A C   1 
ATOM   1662 O  O   . PRO A 1 184 ? 17.290  -2.488  -40.651 1.00 35.35  ? 184 PRO A O   1 
ATOM   1663 C  CB  . PRO A 1 184 ? 14.768  -3.177  -41.811 1.00 30.75  ? 184 PRO A CB  1 
ATOM   1664 C  CG  . PRO A 1 184 ? 13.572  -2.461  -41.183 1.00 30.71  ? 184 PRO A CG  1 
ATOM   1665 C  CD  . PRO A 1 184 ? 13.074  -3.414  -40.118 1.00 29.95  ? 184 PRO A CD  1 
ATOM   1666 N  N   . PHE A 1 185 ? 16.594  -3.045  -38.645 1.00 29.79  ? 185 PHE A N   1 
ATOM   1667 C  CA  . PHE A 1 185 ? 17.434  -2.059  -37.924 1.00 26.76  ? 185 PHE A CA  1 
ATOM   1668 C  C   . PHE A 1 185 ? 18.848  -2.599  -37.701 1.00 23.46  ? 185 PHE A C   1 
ATOM   1669 O  O   . PHE A 1 185 ? 19.097  -3.841  -37.700 1.00 22.88  ? 185 PHE A O   1 
ATOM   1670 C  CB  . PHE A 1 185 ? 16.760  -1.613  -36.622 1.00 26.99  ? 185 PHE A CB  1 
ATOM   1671 C  CG  . PHE A 1 185 ? 15.355  -1.165  -36.864 1.00 27.54  ? 185 PHE A CG  1 
ATOM   1672 C  CD1 . PHE A 1 185 ? 15.121  -0.054  -37.667 1.00 27.44  ? 185 PHE A CD1 1 
ATOM   1673 C  CD2 . PHE A 1 185 ? 14.280  -1.931  -36.430 1.00 25.27  ? 185 PHE A CD2 1 
ATOM   1674 C  CE1 . PHE A 1 185 ? 13.824  0.334   -37.963 1.00 25.62  ? 185 PHE A CE1 1 
ATOM   1675 C  CE2 . PHE A 1 185 ? 12.987  -1.546  -36.740 1.00 27.07  ? 185 PHE A CE2 1 
ATOM   1676 C  CZ  . PHE A 1 185 ? 12.761  -0.411  -37.495 1.00 28.49  ? 185 PHE A CZ  1 
ATOM   1677 N  N   . VAL A 1 186 ? 19.771  -1.660  -37.508 1.00 23.71  ? 186 VAL A N   1 
ATOM   1678 C  CA  . VAL A 1 186 ? 21.207  -1.951  -37.237 1.00 24.12  ? 186 VAL A CA  1 
ATOM   1679 C  C   . VAL A 1 186 ? 21.660  -1.100  -36.048 1.00 26.63  ? 186 VAL A C   1 
ATOM   1680 O  O   . VAL A 1 186 ? 21.125  0.025   -35.870 1.00 26.40  ? 186 VAL A O   1 
ATOM   1681 C  CB  . VAL A 1 186 ? 22.092  -1.698  -38.476 1.00 25.43  ? 186 VAL A CB  1 
ATOM   1682 C  CG1 . VAL A 1 186 ? 21.817  -2.679  -39.591 1.00 25.87  ? 186 VAL A CG1 1 
ATOM   1683 C  CG2 . VAL A 1 186 ? 21.978  -0.267  -38.991 1.00 28.64  ? 186 VAL A CG2 1 
ATOM   1684 N  N   . ASP A 1 187 ? 22.658  -1.596  -35.303 1.00 26.71  ? 187 ASP A N   1 
ATOM   1685 C  CA  . ASP A 1 187 ? 23.287  -0.892  -34.161 1.00 23.41  ? 187 ASP A CA  1 
ATOM   1686 C  C   . ASP A 1 187 ? 24.364  0.057   -34.682 1.00 26.14  ? 187 ASP A C   1 
ATOM   1687 O  O   . ASP A 1 187 ? 25.560  -0.121  -34.344 1.00 22.06  ? 187 ASP A O   1 
ATOM   1688 C  CB  . ASP A 1 187 ? 23.774  -1.881  -33.106 1.00 23.89  ? 187 ASP A CB  1 
ATOM   1689 C  CG  . ASP A 1 187 ? 24.672  -3.035  -33.524 1.00 25.29  ? 187 ASP A CG  1 
ATOM   1690 O  OD1 . ASP A 1 187 ? 24.949  -3.198  -34.737 1.00 24.44  ? 187 ASP A OD1 1 
ATOM   1691 O  OD2 . ASP A 1 187 ? 25.095  -3.786  -32.592 1.00 24.06  ? 187 ASP A OD2 1 
ATOM   1692 N  N   . ARG A 1 188 ? 23.916  1.078   -35.411 1.00 25.55  ? 188 ARG A N   1 
ATOM   1693 C  CA  . ARG A 1 188 ? 24.734  2.185   -35.978 1.00 29.35  ? 188 ARG A CA  1 
ATOM   1694 C  C   . ARG A 1 188 ? 23.910  3.466   -35.895 1.00 28.31  ? 188 ARG A C   1 
ATOM   1695 O  O   . ARG A 1 188 ? 22.715  3.370   -36.121 1.00 27.60  ? 188 ARG A O   1 
ATOM   1696 C  CB  . ARG A 1 188 ? 25.032  1.944   -37.465 1.00 31.41  ? 188 ARG A CB  1 
ATOM   1697 C  CG  . ARG A 1 188 ? 26.011  0.827   -37.760 1.00 33.26  ? 188 ARG A CG  1 
ATOM   1698 C  CD  . ARG A 1 188 ? 26.052  0.533   -39.261 1.00 31.84  ? 188 ARG A CD  1 
ATOM   1699 N  NE  . ARG A 1 188 ? 26.324  1.702   -40.094 1.00 29.28  ? 188 ARG A NE  1 
ATOM   1700 C  CZ  . ARG A 1 188 ? 26.021  1.773   -41.398 1.00 30.04  ? 188 ARG A CZ  1 
ATOM   1701 N  NH1 . ARG A 1 188 ? 25.425  0.759   -41.994 1.00 32.80  ? 188 ARG A NH1 1 
ATOM   1702 N  NH2 . ARG A 1 188 ? 26.318  2.843   -42.114 1.00 30.30  ? 188 ARG A NH2 1 
ATOM   1703 N  N   . GLN A 1 189 ? 24.517  4.630   -35.690 1.00 31.41  ? 189 GLN A N   1 
ATOM   1704 C  CA  . GLN A 1 189 ? 23.739  5.898   -35.621 1.00 36.53  ? 189 GLN A CA  1 
ATOM   1705 C  C   . GLN A 1 189 ? 23.516  6.527   -37.003 1.00 37.19  ? 189 GLN A C   1 
ATOM   1706 O  O   . GLN A 1 189 ? 23.186  7.712   -37.036 1.00 43.64  ? 189 GLN A O   1 
ATOM   1707 C  CB  . GLN A 1 189 ? 24.383  6.851   -34.625 1.00 40.76  ? 189 GLN A CB  1 
ATOM   1708 C  CG  . GLN A 1 189 ? 24.022  6.433   -33.209 1.00 49.60  ? 189 GLN A CG  1 
ATOM   1709 C  CD  . GLN A 1 189 ? 24.446  7.433   -32.166 1.00 56.29  ? 189 GLN A CD  1 
ATOM   1710 O  OE1 . GLN A 1 189 ? 25.040  8.467   -32.473 1.00 62.33  ? 189 GLN A OE1 1 
ATOM   1711 N  NE2 . GLN A 1 189 ? 24.129  7.118   -30.917 1.00 56.80  ? 189 GLN A NE2 1 
ATOM   1712 N  N   . THR A 1 190 ? 23.617  5.758   -38.089 1.00 35.87  ? 190 THR A N   1 
ATOM   1713 C  CA  . THR A 1 190 ? 23.184  6.162   -39.454 1.00 36.62  ? 190 THR A CA  1 
ATOM   1714 C  C   . THR A 1 190 ? 21.659  6.322   -39.420 1.00 36.82  ? 190 THR A C   1 
ATOM   1715 O  O   . THR A 1 190 ? 21.007  5.640   -38.601 1.00 34.90  ? 190 THR A O   1 
ATOM   1716 C  CB  . THR A 1 190 ? 23.660  5.145   -40.512 1.00 38.41  ? 190 THR A CB  1 
ATOM   1717 O  OG1 . THR A 1 190 ? 23.833  5.770   -41.797 1.00 34.96  ? 190 THR A OG1 1 
ATOM   1718 C  CG2 . THR A 1 190 ? 22.715  3.964   -40.620 1.00 37.14  ? 190 THR A CG2 1 
ATOM   1719 N  N   . ALA A 1 191 ? 21.126  7.219   -40.250 1.00 38.72  ? 191 ALA A N   1 
ATOM   1720 C  CA  . ALA A 1 191 ? 19.686  7.539   -40.391 1.00 40.47  ? 191 ALA A CA  1 
ATOM   1721 C  C   . ALA A 1 191 ? 18.905  6.253   -40.632 1.00 39.28  ? 191 ALA A C   1 
ATOM   1722 O  O   . ALA A 1 191 ? 19.220  5.543   -41.581 1.00 39.88  ? 191 ALA A O   1 
ATOM   1723 C  CB  . ALA A 1 191 ? 19.457  8.494   -41.538 1.00 42.27  ? 191 ALA A CB  1 
ATOM   1724 N  N   . GLN A 1 192 ? 17.955  5.950   -39.755 1.00 41.52  ? 192 GLN A N   1 
ATOM   1725 C  CA  . GLN A 1 192 ? 17.031  4.795   -39.915 1.00 38.95  ? 192 GLN A CA  1 
ATOM   1726 C  C   . GLN A 1 192 ? 15.662  5.242   -39.411 1.00 36.83  ? 192 GLN A C   1 
ATOM   1727 O  O   . GLN A 1 192 ? 15.587  6.113   -38.499 1.00 36.32  ? 192 GLN A O   1 
ATOM   1728 C  CB  . GLN A 1 192 ? 17.461  3.557   -39.121 1.00 38.32  ? 192 GLN A CB  1 
ATOM   1729 C  CG  . GLN A 1 192 ? 18.949  3.278   -39.090 1.00 39.94  ? 192 GLN A CG  1 
ATOM   1730 C  CD  . GLN A 1 192 ? 19.250  2.171   -38.104 1.00 39.34  ? 192 GLN A CD  1 
ATOM   1731 O  OE1 . GLN A 1 192 ? 18.676  1.087   -38.167 1.00 32.84  ? 192 GLN A OE1 1 
ATOM   1732 N  NE2 . GLN A 1 192 ? 20.140  2.454   -37.171 1.00 34.93  ? 192 GLN A NE2 1 
ATOM   1733 N  N   . ALA A 1 193 ? 14.615  4.699   -40.002 1.00 37.65  ? 193 ALA A N   1 
ATOM   1734 C  CA  . ALA A 1 193 ? 13.233  5.057   -39.636 1.00 42.48  ? 193 ALA A CA  1 
ATOM   1735 C  C   . ALA A 1 193 ? 12.392  3.796   -39.775 1.00 39.53  ? 193 ALA A C   1 
ATOM   1736 O  O   . ALA A 1 193 ? 12.604  3.049   -40.735 1.00 35.48  ? 193 ALA A O   1 
ATOM   1737 C  CB  . ALA A 1 193 ? 12.729  6.210   -40.481 1.00 42.46  ? 193 ALA A CB  1 
ATOM   1738 N  N   . ALA A 1 194 ? 11.508  3.567   -38.805 1.00 42.83  ? 194 ALA A N   1 
ATOM   1739 C  CA  . ALA A 1 194 ? 10.504  2.482   -38.818 1.00 42.70  ? 194 ALA A CA  1 
ATOM   1740 C  C   . ALA A 1 194 ? 9.592   2.633   -40.039 1.00 41.18  ? 194 ALA A C   1 
ATOM   1741 O  O   . ALA A 1 194 ? 9.274   3.792   -40.393 1.00 44.65  ? 194 ALA A O   1 
ATOM   1742 C  CB  . ALA A 1 194 ? 9.712   2.557   -37.538 1.00 44.92  ? 194 ALA A CB  1 
ATOM   1743 N  N   . GLY A 1 195 ? 9.186   1.512   -40.637 1.00 43.10  ? 195 GLY A N   1 
ATOM   1744 C  CA  . GLY A 1 195 ? 8.022   1.428   -41.536 1.00 44.50  ? 195 GLY A CA  1 
ATOM   1745 C  C   . GLY A 1 195 ? 6.790   2.046   -40.892 1.00 44.11  ? 195 GLY A C   1 
ATOM   1746 O  O   . GLY A 1 195 ? 6.737   2.145   -39.638 1.00 43.31  ? 195 GLY A O   1 
ATOM   1747 N  N   . THR A 1 196 ? 5.833   2.499   -41.705 1.00 46.63  ? 196 THR A N   1 
ATOM   1748 C  CA  . THR A 1 196 ? 4.528   3.021   -41.215 1.00 46.02  ? 196 THR A CA  1 
ATOM   1749 C  C   . THR A 1 196 ? 3.911   1.921   -40.349 1.00 37.92  ? 196 THR A C   1 
ATOM   1750 O  O   . THR A 1 196 ? 3.952   0.758   -40.743 1.00 43.66  ? 196 THR A O   1 
ATOM   1751 C  CB  . THR A 1 196 ? 3.624   3.482   -42.368 1.00 49.63  ? 196 THR A CB  1 
ATOM   1752 O  OG1 . THR A 1 196 ? 3.559   2.402   -43.302 1.00 50.26  ? 196 THR A OG1 1 
ATOM   1753 C  CG2 . THR A 1 196 ? 4.128   4.748   -43.035 1.00 50.21  ? 196 THR A CG2 1 
ATOM   1754 N  N   . ASP A 1 197 ? 3.417   2.268   -39.180 1.00 34.23  ? 197 ASP A N   1 
ATOM   1755 C  CA  . ASP A 1 197 ? 2.875   1.261   -38.239 1.00 36.90  ? 197 ASP A CA  1 
ATOM   1756 C  C   . ASP A 1 197 ? 1.419   0.948   -38.618 1.00 40.61  ? 197 ASP A C   1 
ATOM   1757 O  O   . ASP A 1 197 ? 0.753   1.816   -39.220 1.00 43.91  ? 197 ASP A O   1 
ATOM   1758 C  CB  . ASP A 1 197 ? 2.980   1.694   -36.775 1.00 33.51  ? 197 ASP A CB  1 
ATOM   1759 C  CG  . ASP A 1 197 ? 2.921   0.467   -35.887 1.00 34.92  ? 197 ASP A CG  1 
ATOM   1760 O  OD1 . ASP A 1 197 ? 3.148   -0.667  -36.434 1.00 34.51  ? 197 ASP A OD1 1 
ATOM   1761 O  OD2 . ASP A 1 197 ? 2.635   0.628   -34.713 1.00 31.99  ? 197 ASP A OD2 1 
ATOM   1762 N  N   . THR A 1 198 ? 0.960   -0.260  -38.296 1.00 35.77  ? 198 THR A N   1 
ATOM   1763 C  CA  . THR A 1 198 ? -0.439  -0.681  -38.509 1.00 32.54  ? 198 THR A CA  1 
ATOM   1764 C  C   . THR A 1 198 ? -1.007  -1.206  -37.200 1.00 29.08  ? 198 THR A C   1 
ATOM   1765 O  O   . THR A 1 198 ? -0.214  -1.470  -36.267 1.00 28.51  ? 198 THR A O   1 
ATOM   1766 C  CB  . THR A 1 198 ? -0.505  -1.686  -39.657 1.00 34.15  ? 198 THR A CB  1 
ATOM   1767 O  OG1 . THR A 1 198 ? 0.457   -2.698  -39.382 1.00 35.25  ? 198 THR A OG1 1 
ATOM   1768 C  CG2 . THR A 1 198 ? -0.229  -1.047  -40.998 1.00 35.16  ? 198 THR A CG2 1 
ATOM   1769 N  N   . THR A 1 199 ? -2.333  -1.311  -37.130 1.00 26.78  ? 199 THR A N   1 
ATOM   1770 C  CA  . THR A 1 199 ? -3.069  -1.892  -35.991 1.00 24.34  ? 199 THR A CA  1 
ATOM   1771 C  C   . THR A 1 199 ? -3.044  -3.413  -36.080 1.00 23.82  ? 199 THR A C   1 
ATOM   1772 O  O   . THR A 1 199 ? -3.205  -3.967  -37.185 1.00 24.77  ? 199 THR A O   1 
ATOM   1773 C  CB  . THR A 1 199 ? -4.481  -1.302  -35.894 1.00 30.15  ? 199 THR A CB  1 
ATOM   1774 O  OG1 . THR A 1 199 ? -4.350  0.113   -35.752 1.00 28.87  ? 199 THR A OG1 1 
ATOM   1775 C  CG2 . THR A 1 199 ? -5.256  -1.843  -34.714 1.00 29.45  ? 199 THR A CG2 1 
ATOM   1776 N  N   . ILE A 1 200 ? -2.876  -4.076  -34.929 1.00 23.34  ? 200 ILE A N   1 
ATOM   1777 C  CA  . ILE A 1 200 ? -2.805  -5.561  -34.866 1.00 24.33  ? 200 ILE A CA  1 
ATOM   1778 C  C   . ILE A 1 200 ? -4.253  -6.092  -34.809 1.00 25.70  ? 200 ILE A C   1 
ATOM   1779 O  O   . ILE A 1 200 ? -4.858  -6.167  -33.704 1.00 23.26  ? 200 ILE A O   1 
ATOM   1780 C  CB  . ILE A 1 200 ? -1.945  -6.015  -33.679 1.00 22.92  ? 200 ILE A CB  1 
ATOM   1781 C  CG1 . ILE A 1 200 ? -0.553  -5.373  -33.683 1.00 22.32  ? 200 ILE A CG1 1 
ATOM   1782 C  CG2 . ILE A 1 200 ? -1.845  -7.524  -33.642 1.00 22.82  ? 200 ILE A CG2 1 
ATOM   1783 C  CD1 . ILE A 1 200 ? 0.086   -5.352  -32.302 1.00 21.24  ? 200 ILE A CD1 1 
ATOM   1784 N  N   . THR A 1 201 ? -4.806  -6.417  -35.972 1.00 24.39  ? 201 THR A N   1 
ATOM   1785 C  CA  . THR A 1 201 ? -6.256  -6.680  -36.129 1.00 24.03  ? 201 THR A CA  1 
ATOM   1786 C  C   . THR A 1 201 ? -6.680  -7.855  -35.235 1.00 23.14  ? 201 THR A C   1 
ATOM   1787 O  O   . THR A 1 201 ? -7.695  -7.736  -34.508 1.00 24.43  ? 201 THR A O   1 
ATOM   1788 C  CB  . THR A 1 201 ? -6.588  -6.907  -37.603 1.00 23.07  ? 201 THR A CB  1 
ATOM   1789 O  OG1 . THR A 1 201 ? -6.074  -5.777  -38.316 1.00 21.86  ? 201 THR A OG1 1 
ATOM   1790 C  CG2 . THR A 1 201 ? -8.074  -7.119  -37.781 1.00 23.17  ? 201 THR A CG2 1 
ATOM   1791 N  N   . VAL A 1 202 ? -5.941  -8.951  -35.283 1.00 22.77  ? 202 VAL A N   1 
ATOM   1792 C  CA  . VAL A 1 202 ? -6.245  -10.170 -34.492 1.00 22.89  ? 202 VAL A CA  1 
ATOM   1793 C  C   . VAL A 1 202 ? -6.363  -9.783  -33.013 1.00 22.59  ? 202 VAL A C   1 
ATOM   1794 O  O   . VAL A 1 202 ? -7.250  -10.325 -32.325 1.00 21.32  ? 202 VAL A O   1 
ATOM   1795 C  CB  . VAL A 1 202 ? -5.250  -11.313 -34.767 1.00 24.97  ? 202 VAL A CB  1 
ATOM   1796 C  CG1 . VAL A 1 202 ? -3.817  -11.062 -34.267 1.00 26.53  ? 202 VAL A CG1 1 
ATOM   1797 C  CG2 . VAL A 1 202 ? -5.782  -12.603 -34.181 1.00 25.92  ? 202 VAL A CG2 1 
ATOM   1798 N  N   . ASN A 1 203 ? -5.527  -8.869  -32.520 1.00 24.80  ? 203 ASN A N   1 
ATOM   1799 C  CA  . ASN A 1 203 ? -5.516  -8.511  -31.069 1.00 23.34  ? 203 ASN A CA  1 
ATOM   1800 C  C   . ASN A 1 203 ? -6.778  -7.705  -30.776 1.00 23.00  ? 203 ASN A C   1 
ATOM   1801 O  O   . ASN A 1 203 ? -7.396  -7.953  -29.718 1.00 19.95  ? 203 ASN A O   1 
ATOM   1802 C  CB  . ASN A 1 203 ? -4.245  -7.768  -30.654 1.00 22.33  ? 203 ASN A CB  1 
ATOM   1803 C  CG  . ASN A 1 203 ? -3.008  -8.648  -30.578 1.00 23.56  ? 203 ASN A CG  1 
ATOM   1804 O  OD1 . ASN A 1 203 ? -3.069  -9.862  -30.809 1.00 21.76  ? 203 ASN A OD1 1 
ATOM   1805 N  ND2 . ASN A 1 203 ? -1.884  -8.052  -30.178 1.00 20.48  ? 203 ASN A ND2 1 
ATOM   1806 N  N   . VAL A 1 204 ? -7.150  -6.795  -31.682 1.00 23.32  ? 204 VAL A N   1 
ATOM   1807 C  CA  . VAL A 1 204 ? -8.363  -5.943  -31.495 1.00 26.23  ? 204 VAL A CA  1 
ATOM   1808 C  C   . VAL A 1 204 ? -9.593  -6.841  -31.390 1.00 25.82  ? 204 VAL A C   1 
ATOM   1809 O  O   . VAL A 1 204 ? -10.408 -6.610  -30.477 1.00 27.35  ? 204 VAL A O   1 
ATOM   1810 C  CB  . VAL A 1 204 ? -8.558  -4.908  -32.609 1.00 27.58  ? 204 VAL A CB  1 
ATOM   1811 C  CG1 . VAL A 1 204 ? -9.909  -4.210  -32.466 1.00 30.30  ? 204 VAL A CG1 1 
ATOM   1812 C  CG2 . VAL A 1 204 ? -7.444  -3.879  -32.616 1.00 28.91  ? 204 VAL A CG2 1 
ATOM   1813 N  N   . LEU A 1 205 ? -9.693  -7.844  -32.264 1.00 24.54  ? 205 LEU A N   1 
ATOM   1814 C  CA  . LEU A 1 205 ? -10.821 -8.809  -32.247 1.00 26.31  ? 205 LEU A CA  1 
ATOM   1815 C  C   . LEU A 1 205 ? -10.834 -9.583  -30.933 1.00 28.01  ? 205 LEU A C   1 
ATOM   1816 O  O   . LEU A 1 205 ? -11.931 -9.800  -30.406 1.00 27.49  ? 205 LEU A O   1 
ATOM   1817 C  CB  . LEU A 1 205 ? -10.747 -9.748  -33.450 1.00 24.10  ? 205 LEU A CB  1 
ATOM   1818 C  CG  . LEU A 1 205 ? -11.015 -9.072  -34.796 1.00 24.34  ? 205 LEU A CG  1 
ATOM   1819 C  CD1 . LEU A 1 205 ? -10.631 -10.000 -35.945 1.00 23.28  ? 205 LEU A CD1 1 
ATOM   1820 C  CD2 . LEU A 1 205 ? -12.468 -8.620  -34.889 1.00 23.07  ? 205 LEU A CD2 1 
ATOM   1821 N  N   . ALA A 1 206 ? -9.677  -10.011 -30.436 1.00 29.58  ? 206 ALA A N   1 
ATOM   1822 C  CA  . ALA A 1 206 ? -9.574  -10.771 -29.166 1.00 30.44  ? 206 ALA A CA  1 
ATOM   1823 C  C   . ALA A 1 206 ? -10.133 -9.904  -28.030 1.00 27.27  ? 206 ALA A C   1 
ATOM   1824 O  O   . ALA A 1 206 ? -10.866 -10.413 -27.159 1.00 27.75  ? 206 ALA A O   1 
ATOM   1825 C  CB  . ALA A 1 206 ? -8.136  -11.179 -28.898 1.00 32.28  ? 206 ALA A CB  1 
ATOM   1826 N  N   . TRP A 1 207 ? -9.798  -8.628  -28.074 1.00 25.49  ? 207 TRP A N   1 
ATOM   1827 C  CA  . TRP A 1 207 ? -10.209 -7.627  -27.072 1.00 28.23  ? 207 TRP A CA  1 
ATOM   1828 C  C   . TRP A 1 207 ? -11.714 -7.354  -27.177 1.00 31.13  ? 207 TRP A C   1 
ATOM   1829 O  O   . TRP A 1 207 ? -12.346 -7.184  -26.102 1.00 31.24  ? 207 TRP A O   1 
ATOM   1830 C  CB  . TRP A 1 207 ? -9.352  -6.384  -27.271 1.00 31.22  ? 207 TRP A CB  1 
ATOM   1831 C  CG  . TRP A 1 207 ? -9.669  -5.234  -26.371 1.00 33.75  ? 207 TRP A CG  1 
ATOM   1832 C  CD1 . TRP A 1 207 ? -9.322  -5.053  -25.060 1.00 35.27  ? 207 TRP A CD1 1 
ATOM   1833 C  CD2 . TRP A 1 207 ? -10.360 -4.042  -26.777 1.00 38.04  ? 207 TRP A CD2 1 
ATOM   1834 N  NE1 . TRP A 1 207 ? -9.741  -3.818  -24.632 1.00 34.84  ? 207 TRP A NE1 1 
ATOM   1835 C  CE2 . TRP A 1 207 ? -10.378 -3.177  -25.664 1.00 37.78  ? 207 TRP A CE2 1 
ATOM   1836 C  CE3 . TRP A 1 207 ? -10.950 -3.625  -27.977 1.00 36.45  ? 207 TRP A CE3 1 
ATOM   1837 C  CZ2 . TRP A 1 207 ? -10.999 -1.931  -25.720 1.00 39.70  ? 207 TRP A CZ2 1 
ATOM   1838 C  CZ3 . TRP A 1 207 ? -11.540 -2.384  -28.032 1.00 39.31  ? 207 TRP A CZ3 1 
ATOM   1839 C  CH2 . TRP A 1 207 ? -11.566 -1.552  -26.912 1.00 37.15  ? 207 TRP A CH2 1 
ATOM   1840 N  N   . LEU A 1 208 ? -12.303 -7.404  -28.386 1.00 30.02  ? 208 LEU A N   1 
ATOM   1841 C  CA  . LEU A 1 208 ? -13.783 -7.277  -28.538 1.00 29.07  ? 208 LEU A CA  1 
ATOM   1842 C  C   . LEU A 1 208 ? -14.442 -8.518  -27.926 1.00 30.14  ? 208 LEU A C   1 
ATOM   1843 O  O   . LEU A 1 208 ? -15.414 -8.336  -27.158 1.00 30.44  ? 208 LEU A O   1 
ATOM   1844 C  CB  . LEU A 1 208 ? -14.190 -7.057  -29.996 1.00 25.03  ? 208 LEU A CB  1 
ATOM   1845 C  CG  . LEU A 1 208 ? -13.736 -5.725  -30.577 1.00 25.22  ? 208 LEU A CG  1 
ATOM   1846 C  CD1 . LEU A 1 208 ? -14.094 -5.598  -32.059 1.00 24.74  ? 208 LEU A CD1 1 
ATOM   1847 C  CD2 . LEU A 1 208 ? -14.297 -4.538  -29.800 1.00 26.53  ? 208 LEU A CD2 1 
ATOM   1848 N  N   . TYR A 1 209 ? -13.882 -9.708  -28.146 1.00 28.91  ? 209 TYR A N   1 
ATOM   1849 C  CA  . TYR A 1 209 ? -14.371 -10.967 -27.515 1.00 31.20  ? 209 TYR A CA  1 
ATOM   1850 C  C   . TYR A 1 209 ? -14.276 -10.847 -25.982 1.00 33.67  ? 209 TYR A C   1 
ATOM   1851 O  O   . TYR A 1 209 ? -15.218 -11.280 -25.291 1.00 35.59  ? 209 TYR A O   1 
ATOM   1852 C  CB  . TYR A 1 209 ? -13.634 -12.197 -28.058 1.00 28.48  ? 209 TYR A CB  1 
ATOM   1853 C  CG  . TYR A 1 209 ? -14.173 -12.749 -29.354 1.00 28.36  ? 209 TYR A CG  1 
ATOM   1854 C  CD1 . TYR A 1 209 ? -15.464 -13.255 -29.449 1.00 28.57  ? 209 TYR A CD1 1 
ATOM   1855 C  CD2 . TYR A 1 209 ? -13.399 -12.750 -30.506 1.00 28.85  ? 209 TYR A CD2 1 
ATOM   1856 C  CE1 . TYR A 1 209 ? -15.959 -13.768 -30.637 1.00 30.37  ? 209 TYR A CE1 1 
ATOM   1857 C  CE2 . TYR A 1 209 ? -13.878 -13.249 -31.708 1.00 28.68  ? 209 TYR A CE2 1 
ATOM   1858 C  CZ  . TYR A 1 209 ? -15.160 -13.766 -31.775 1.00 29.93  ? 209 TYR A CZ  1 
ATOM   1859 O  OH  . TYR A 1 209 ? -15.619 -14.261 -32.955 1.00 27.54  ? 209 TYR A OH  1 
ATOM   1860 N  N   . ALA A 1 210 ? -13.225 -10.233 -25.445 1.00 34.17  ? 210 ALA A N   1 
ATOM   1861 C  CA  . ALA A 1 210 ? -13.074 -10.032 -23.982 1.00 38.72  ? 210 ALA A CA  1 
ATOM   1862 C  C   . ALA A 1 210 ? -14.165 -9.077  -23.472 1.00 40.39  ? 210 ALA A C   1 
ATOM   1863 O  O   . ALA A 1 210 ? -14.635 -9.276  -22.334 1.00 37.90  ? 210 ALA A O   1 
ATOM   1864 C  CB  . ALA A 1 210 ? -11.715 -9.486  -23.635 1.00 38.88  ? 210 ALA A CB  1 
ATOM   1865 N  N   . ALA A 1 211 ? -14.489 -8.037  -24.240 1.00 36.90  ? 211 ALA A N   1 
ATOM   1866 C  CA  . ALA A 1 211 ? -15.516 -7.033  -23.874 1.00 39.36  ? 211 ALA A CA  1 
ATOM   1867 C  C   . ALA A 1 211 ? -16.869 -7.744  -23.787 1.00 37.86  ? 211 ALA A C   1 
ATOM   1868 O  O   . ALA A 1 211 ? -17.619 -7.479  -22.842 1.00 42.55  ? 211 ALA A O   1 
ATOM   1869 C  CB  . ALA A 1 211 ? -15.534 -5.878  -24.854 1.00 41.76  ? 211 ALA A CB  1 
ATOM   1870 N  N   . VAL A 1 212 ? -17.128 -8.679  -24.693 1.00 35.07  ? 212 VAL A N   1 
ATOM   1871 C  CA  . VAL A 1 212 ? -18.395 -9.453  -24.733 1.00 37.71  ? 212 VAL A CA  1 
ATOM   1872 C  C   . VAL A 1 212 ? -18.436 -10.417 -23.537 1.00 47.10  ? 212 VAL A C   1 
ATOM   1873 O  O   . VAL A 1 212 ? -19.505 -10.560 -22.903 1.00 47.37  ? 212 VAL A O   1 
ATOM   1874 C  CB  . VAL A 1 212 ? -18.545 -10.172 -26.082 1.00 35.50  ? 212 VAL A CB  1 
ATOM   1875 C  CG1 . VAL A 1 212 ? -19.666 -11.201 -26.040 1.00 35.50  ? 212 VAL A CG1 1 
ATOM   1876 C  CG2 . VAL A 1 212 ? -18.751 -9.161  -27.212 1.00 36.03  ? 212 VAL A CG2 1 
ATOM   1877 N  N   . ILE A 1 213 ? -17.312 -11.044 -23.210 1.00 47.53  ? 213 ILE A N   1 
ATOM   1878 C  CA  . ILE A 1 213 ? -17.207 -11.958 -22.037 1.00 47.59  ? 213 ILE A CA  1 
ATOM   1879 C  C   . ILE A 1 213 ? -17.486 -11.164 -20.749 1.00 46.36  ? 213 ILE A C   1 
ATOM   1880 O  O   . ILE A 1 213 ? -18.162 -11.727 -19.868 1.00 50.09  ? 213 ILE A O   1 
ATOM   1881 C  CB  . ILE A 1 213 ? -15.840 -12.669 -22.017 1.00 52.19  ? 213 ILE A CB  1 
ATOM   1882 C  CG1 . ILE A 1 213 ? -15.722 -13.678 -23.166 1.00 57.22  ? 213 ILE A CG1 1 
ATOM   1883 C  CG2 . ILE A 1 213 ? -15.597 -13.328 -20.669 1.00 56.52  ? 213 ILE A CG2 1 
ATOM   1884 C  CD1 . ILE A 1 213 ? -14.302 -14.139 -23.448 1.00 60.10  ? 213 ILE A CD1 1 
ATOM   1885 N  N   . ASN A 1 214 ? -17.006 -9.918  -20.650 1.00 44.22  ? 214 ASN A N   1 
ATOM   1886 C  CA  . ASN A 1 214 ? -17.184 -9.010  -19.482 1.00 45.98  ? 214 ASN A CA  1 
ATOM   1887 C  C   . ASN A 1 214 ? -18.490 -8.193  -19.563 1.00 45.35  ? 214 ASN A C   1 
ATOM   1888 O  O   . ASN A 1 214 ? -18.645 -7.275  -18.743 1.00 43.84  ? 214 ASN A O   1 
ATOM   1889 C  CB  . ASN A 1 214 ? -16.014 -8.034  -19.349 1.00 53.49  ? 214 ASN A CB  1 
ATOM   1890 C  CG  . ASN A 1 214 ? -14.786 -8.666  -18.728 1.00 63.73  ? 214 ASN A CG  1 
ATOM   1891 O  OD1 . ASN A 1 214 ? -14.598 -8.589  -17.513 1.00 69.00  ? 214 ASN A OD1 1 
ATOM   1892 N  ND2 . ASN A 1 214 ? -13.949 -9.291  -19.547 1.00 68.25  ? 214 ASN A ND2 1 
ATOM   1893 N  N   . GLY A 1 215 ? -19.372 -8.480  -20.525 1.00 43.01  ? 215 GLY A N   1 
ATOM   1894 C  CA  . GLY A 1 215 ? -20.792 -8.075  -20.518 1.00 44.76  ? 215 GLY A CA  1 
ATOM   1895 C  C   . GLY A 1 215 ? -21.163 -6.912  -21.437 1.00 44.92  ? 215 GLY A C   1 
ATOM   1896 O  O   . GLY A 1 215 ? -22.324 -6.482  -21.396 1.00 45.83  ? 215 GLY A O   1 
ATOM   1897 N  N   A ASP A 1 216 ? -20.188 -6.386  -22.191 0.33 44.30  ? 216 ASP A N   1 
ATOM   1898 N  N   B ASP A 1 216 ? -20.231 -6.445  -22.275 0.17 43.41  ? 216 ASP A N   1 
ATOM   1899 N  N   C ASP A 1 216 ? -20.188 -6.386  -22.191 0.33 44.30  ? 216 ASP A N   1 
ATOM   1900 N  N   D ASP A 1 216 ? -20.231 -6.445  -22.275 0.17 43.41  ? 216 ASP A N   1 
ATOM   1901 C  CA  A ASP A 1 216 ? -20.365 -5.304  -23.199 0.33 44.48  ? 216 ASP A CA  1 
ATOM   1902 C  CA  B ASP A 1 216 ? -20.435 -5.263  -23.156 0.17 42.85  ? 216 ASP A CA  1 
ATOM   1903 C  CA  C ASP A 1 216 ? -20.365 -5.304  -23.199 0.33 44.48  ? 216 ASP A CA  1 
ATOM   1904 C  CA  D ASP A 1 216 ? -20.435 -5.263  -23.156 0.17 42.85  ? 216 ASP A CA  1 
ATOM   1905 C  C   A ASP A 1 216 ? -20.924 -5.934  -24.478 0.33 43.03  ? 216 ASP A C   1 
ATOM   1906 C  C   B ASP A 1 216 ? -20.818 -5.741  -24.562 0.17 41.77  ? 216 ASP A C   1 
ATOM   1907 C  C   C ASP A 1 216 ? -20.924 -5.934  -24.478 0.33 43.03  ? 216 ASP A C   1 
ATOM   1908 C  C   D ASP A 1 216 ? -20.818 -5.741  -24.562 0.17 41.77  ? 216 ASP A C   1 
ATOM   1909 O  O   A ASP A 1 216 ? -20.309 -6.906  -24.953 0.33 46.19  ? 216 ASP A O   1 
ATOM   1910 O  O   B ASP A 1 216 ? -19.951 -6.343  -25.228 0.17 42.47  ? 216 ASP A O   1 
ATOM   1911 O  O   C ASP A 1 216 ? -20.309 -6.906  -24.953 0.33 46.19  ? 216 ASP A O   1 
ATOM   1912 O  O   D ASP A 1 216 ? -19.951 -6.343  -25.228 0.17 42.47  ? 216 ASP A O   1 
ATOM   1913 C  CB  A ASP A 1 216 ? -19.045 -4.583  -23.499 0.33 46.39  ? 216 ASP A CB  1 
ATOM   1914 C  CB  B ASP A 1 216 ? -19.199 -4.362  -23.168 0.17 43.43  ? 216 ASP A CB  1 
ATOM   1915 C  CB  C ASP A 1 216 ? -19.045 -4.583  -23.499 0.33 46.39  ? 216 ASP A CB  1 
ATOM   1916 C  CB  D ASP A 1 216 ? -19.199 -4.362  -23.168 0.17 43.43  ? 216 ASP A CB  1 
ATOM   1917 C  CG  A ASP A 1 216 ? -18.624 -3.541  -22.472 0.33 47.09  ? 216 ASP A CG  1 
ATOM   1918 C  CG  B ASP A 1 216 ? -19.551 -2.886  -23.113 0.17 43.63  ? 216 ASP A CG  1 
ATOM   1919 C  CG  C ASP A 1 216 ? -18.624 -3.541  -22.472 0.33 47.09  ? 216 ASP A CG  1 
ATOM   1920 C  CG  D ASP A 1 216 ? -19.551 -2.886  -23.113 0.17 43.63  ? 216 ASP A CG  1 
ATOM   1921 O  OD1 A ASP A 1 216 ? -19.498 -3.081  -21.715 0.33 51.14  ? 216 ASP A OD1 1 
ATOM   1922 O  OD1 B ASP A 1 216 ? -20.758 -2.578  -23.154 0.17 43.81  ? 216 ASP A OD1 1 
ATOM   1923 O  OD1 C ASP A 1 216 ? -19.498 -3.081  -21.715 0.33 51.14  ? 216 ASP A OD1 1 
ATOM   1924 O  OD1 D ASP A 1 216 ? -20.758 -2.578  -23.154 0.17 43.81  ? 216 ASP A OD1 1 
ATOM   1925 O  OD2 A ASP A 1 216 ? -17.418 -3.194  -22.441 0.33 46.70  ? 216 ASP A OD2 1 
ATOM   1926 O  OD2 B ASP A 1 216 ? -18.623 -2.060  -23.012 0.17 45.29  ? 216 ASP A OD2 1 
ATOM   1927 O  OD2 C ASP A 1 216 ? -17.418 -3.194  -22.441 0.33 46.70  ? 216 ASP A OD2 1 
ATOM   1928 O  OD2 D ASP A 1 216 ? -18.623 -2.060  -23.012 0.17 45.29  ? 216 ASP A OD2 1 
ATOM   1929 N  N   . ARG A 1 217 ? -22.048 -5.431  -25.001 1.00 39.90  ? 217 ARG A N   1 
ATOM   1930 C  CA  . ARG A 1 217 ? -22.645 -5.963  -26.268 1.00 38.32  ? 217 ARG A CA  1 
ATOM   1931 C  C   . ARG A 1 217 ? -23.118 -4.871  -27.229 1.00 37.52  ? 217 ARG A C   1 
ATOM   1932 O  O   . ARG A 1 217 ? -23.550 -5.227  -28.369 1.00 31.03  ? 217 ARG A O   1 
ATOM   1933 C  CB  . ARG A 1 217 ? -23.823 -6.883  -25.955 1.00 43.89  ? 217 ARG A CB  1 
ATOM   1934 C  CG  . ARG A 1 217 ? -23.411 -8.188  -25.291 1.00 45.01  ? 217 ARG A CG  1 
ATOM   1935 C  CD  . ARG A 1 217 ? -24.498 -9.222  -25.345 1.00 47.41  ? 217 ARG A CD  1 
ATOM   1936 N  NE  . ARG A 1 217 ? -25.003 -9.429  -26.705 1.00 49.62  ? 217 ARG A NE  1 
ATOM   1937 C  CZ  . ARG A 1 217 ? -24.872 -10.547 -27.433 1.00 53.85  ? 217 ARG A CZ  1 
ATOM   1938 N  NH1 . ARG A 1 217 ? -24.228 -11.605 -26.964 1.00 51.02  ? 217 ARG A NH1 1 
ATOM   1939 N  NH2 . ARG A 1 217 ? -25.399 -10.601 -28.647 1.00 55.74  ? 217 ARG A NH2 1 
ATOM   1940 N  N   . TRP A 1 218 ? -22.974 -3.602  -26.843 1.00 32.78  ? 218 TRP A N   1 
ATOM   1941 C  CA  . TRP A 1 218 ? -23.534 -2.453  -27.583 1.00 30.77  ? 218 TRP A CA  1 
ATOM   1942 C  C   . TRP A 1 218 ? -22.984 -2.349  -29.019 1.00 31.27  ? 218 TRP A C   1 
ATOM   1943 O  O   . TRP A 1 218 ? -23.683 -1.747  -29.824 1.00 28.01  ? 218 TRP A O   1 
ATOM   1944 C  CB  . TRP A 1 218 ? -23.288 -1.163  -26.797 1.00 32.49  ? 218 TRP A CB  1 
ATOM   1945 C  CG  . TRP A 1 218 ? -21.869 -0.694  -26.739 1.00 33.96  ? 218 TRP A CG  1 
ATOM   1946 C  CD1 . TRP A 1 218 ? -21.034 -0.785  -25.658 1.00 33.87  ? 218 TRP A CD1 1 
ATOM   1947 C  CD2 . TRP A 1 218 ? -21.151 0.039   -27.748 1.00 32.21  ? 218 TRP A CD2 1 
ATOM   1948 N  NE1 . TRP A 1 218 ? -19.853 -0.147  -25.926 1.00 36.14  ? 218 TRP A NE1 1 
ATOM   1949 C  CE2 . TRP A 1 218 ? -19.887 0.349   -27.206 1.00 33.66  ? 218 TRP A CE2 1 
ATOM   1950 C  CE3 . TRP A 1 218 ? -21.442 0.476   -29.046 1.00 35.72  ? 218 TRP A CE3 1 
ATOM   1951 C  CZ2 . TRP A 1 218 ? -18.920 1.046   -27.933 1.00 33.27  ? 218 TRP A CZ2 1 
ATOM   1952 C  CZ3 . TRP A 1 218 ? -20.485 1.168   -29.764 1.00 34.50  ? 218 TRP A CZ3 1 
ATOM   1953 C  CH2 . TRP A 1 218 ? -19.238 1.445   -29.210 1.00 31.40  ? 218 TRP A CH2 1 
ATOM   1954 N  N   . PHE A 1 219 ? -21.787 -2.876  -29.331 1.00 27.50  ? 219 PHE A N   1 
ATOM   1955 C  CA  . PHE A 1 219 ? -21.105 -2.647  -30.633 1.00 28.67  ? 219 PHE A CA  1 
ATOM   1956 C  C   . PHE A 1 219 ? -21.374 -3.830  -31.568 1.00 30.31  ? 219 PHE A C   1 
ATOM   1957 O  O   . PHE A 1 219 ? -20.939 -3.775  -32.734 1.00 28.36  ? 219 PHE A O   1 
ATOM   1958 C  CB  . PHE A 1 219 ? -19.591 -2.434  -30.437 1.00 28.97  ? 219 PHE A CB  1 
ATOM   1959 C  CG  . PHE A 1 219 ? -18.953 -3.490  -29.576 1.00 26.59  ? 219 PHE A CG  1 
ATOM   1960 C  CD1 . PHE A 1 219 ? -18.626 -4.732  -30.094 1.00 28.22  ? 219 PHE A CD1 1 
ATOM   1961 C  CD2 . PHE A 1 219 ? -18.780 -3.270  -28.220 1.00 28.37  ? 219 PHE A CD2 1 
ATOM   1962 C  CE1 . PHE A 1 219 ? -18.109 -5.730  -29.275 1.00 28.14  ? 219 PHE A CE1 1 
ATOM   1963 C  CE2 . PHE A 1 219 ? -18.265 -4.268  -27.407 1.00 27.36  ? 219 PHE A CE2 1 
ATOM   1964 C  CZ  . PHE A 1 219 ? -17.928 -5.489  -27.939 1.00 28.15  ? 219 PHE A CZ  1 
ATOM   1965 N  N   . LEU A 1 220 ? -22.036 -4.893  -31.093 1.00 31.26  ? 220 LEU A N   1 
ATOM   1966 C  CA  . LEU A 1 220 ? -22.410 -6.043  -31.965 1.00 29.26  ? 220 LEU A CA  1 
ATOM   1967 C  C   . LEU A 1 220 ? -23.470 -5.598  -32.979 1.00 32.44  ? 220 LEU A C   1 
ATOM   1968 O  O   . LEU A 1 220 ? -24.147 -4.571  -32.734 1.00 30.97  ? 220 LEU A O   1 
ATOM   1969 C  CB  . LEU A 1 220 ? -22.943 -7.187  -31.108 1.00 34.11  ? 220 LEU A CB  1 
ATOM   1970 C  CG  . LEU A 1 220 ? -21.941 -7.829  -30.157 1.00 36.61  ? 220 LEU A CG  1 
ATOM   1971 C  CD1 . LEU A 1 220 ? -22.626 -8.932  -29.380 1.00 38.00  ? 220 LEU A CD1 1 
ATOM   1972 C  CD2 . LEU A 1 220 ? -20.730 -8.373  -30.918 1.00 38.26  ? 220 LEU A CD2 1 
ATOM   1973 N  N   . ASN A 1 221 ? -23.564 -6.292  -34.106 1.00 30.53  ? 221 ASN A N   1 
ATOM   1974 C  CA  . ASN A 1 221 ? -24.541 -5.975  -35.174 1.00 32.99  ? 221 ASN A CA  1 
ATOM   1975 C  C   . ASN A 1 221 ? -25.003 -7.302  -35.772 1.00 34.57  ? 221 ASN A C   1 
ATOM   1976 O  O   . ASN A 1 221 ? -24.445 -8.348  -35.431 1.00 34.26  ? 221 ASN A O   1 
ATOM   1977 C  CB  . ASN A 1 221 ? -23.983 -5.001  -36.222 1.00 32.30  ? 221 ASN A CB  1 
ATOM   1978 C  CG  . ASN A 1 221 ? -22.866 -5.589  -37.071 1.00 33.66  ? 221 ASN A CG  1 
ATOM   1979 O  OD1 . ASN A 1 221 ? -22.696 -6.804  -37.138 1.00 38.17  ? 221 ASN A OD1 1 
ATOM   1980 N  ND2 . ASN A 1 221 ? -22.101 -4.745  -37.744 1.00 33.09  ? 221 ASN A ND2 1 
ATOM   1981 N  N   . ARG A 1 222 ? -25.990 -7.252  -36.649 1.00 39.72  ? 222 ARG A N   1 
ATOM   1982 C  CA  . ARG A 1 222 ? -26.626 -8.467  -37.200 1.00 40.95  ? 222 ARG A CA  1 
ATOM   1983 C  C   . ARG A 1 222 ? -25.864 -8.859  -38.456 1.00 38.33  ? 222 ARG A C   1 
ATOM   1984 O  O   . ARG A 1 222 ? -26.228 -9.863  -39.039 1.00 38.45  ? 222 ARG A O   1 
ATOM   1985 C  CB  . ARG A 1 222 ? -28.112 -8.227  -37.484 1.00 53.18  ? 222 ARG A CB  1 
ATOM   1986 C  CG  . ARG A 1 222 ? -28.414 -6.967  -38.287 1.00 64.07  ? 222 ARG A CG  1 
ATOM   1987 C  CD  . ARG A 1 222 ? -29.835 -6.967  -38.842 1.00 72.52  ? 222 ARG A CD  1 
ATOM   1988 N  NE  . ARG A 1 222 ? -30.110 -5.871  -39.764 1.00 76.37  ? 222 ARG A NE  1 
ATOM   1989 C  CZ  . ARG A 1 222 ? -29.934 -5.899  -41.091 1.00 83.48  ? 222 ARG A CZ  1 
ATOM   1990 N  NH1 . ARG A 1 222 ? -29.469 -6.982  -41.700 1.00 87.26  ? 222 ARG A NH1 1 
ATOM   1991 N  NH2 . ARG A 1 222 ? -30.223 -4.827  -41.813 1.00 78.43  ? 222 ARG A NH2 1 
ATOM   1992 N  N   . PHE A 1 223 ? -24.844 -8.094  -38.853 1.00 34.86  ? 223 PHE A N   1 
ATOM   1993 C  CA  . PHE A 1 223 ? -24.079 -8.356  -40.091 1.00 35.88  ? 223 PHE A CA  1 
ATOM   1994 C  C   . PHE A 1 223 ? -22.963 -9.369  -39.867 1.00 35.04  ? 223 PHE A C   1 
ATOM   1995 O  O   . PHE A 1 223 ? -22.494 -9.564  -38.729 1.00 35.98  ? 223 PHE A O   1 
ATOM   1996 C  CB  . PHE A 1 223 ? -23.501 -7.066  -40.659 1.00 41.68  ? 223 PHE A CB  1 
ATOM   1997 C  CG  . PHE A 1 223 ? -24.594 -6.152  -41.114 1.00 44.00  ? 223 PHE A CG  1 
ATOM   1998 C  CD1 . PHE A 1 223 ? -25.245 -6.397  -42.310 1.00 47.62  ? 223 PHE A CD1 1 
ATOM   1999 C  CD2 . PHE A 1 223 ? -25.012 -5.100  -40.315 1.00 49.46  ? 223 PHE A CD2 1 
ATOM   2000 C  CE1 . PHE A 1 223 ? -26.268 -5.567  -42.730 1.00 52.74  ? 223 PHE A CE1 1 
ATOM   2001 C  CE2 . PHE A 1 223 ? -26.042 -4.275  -40.738 1.00 56.77  ? 223 PHE A CE2 1 
ATOM   2002 C  CZ  . PHE A 1 223 ? -26.664 -4.508  -41.944 1.00 51.43  ? 223 PHE A CZ  1 
ATOM   2003 N  N   . THR A 1 224 ? -22.592 -10.000 -40.976 1.00 33.69  ? 224 THR A N   1 
ATOM   2004 C  CA  . THR A 1 224 ? -21.378 -10.828 -41.142 1.00 38.40  ? 224 THR A CA  1 
ATOM   2005 C  C   . THR A 1 224 ? -20.583 -10.218 -42.293 1.00 35.16  ? 224 THR A C   1 
ATOM   2006 O  O   . THR A 1 224 ? -21.032 -9.197  -42.835 1.00 34.62  ? 224 THR A O   1 
ATOM   2007 C  CB  . THR A 1 224 ? -21.722 -12.307 -41.337 1.00 41.72  ? 224 THR A CB  1 
ATOM   2008 O  OG1 . THR A 1 224 ? -20.555 -13.024 -40.941 1.00 44.79  ? 224 THR A OG1 1 
ATOM   2009 C  CG2 . THR A 1 224 ? -22.096 -12.672 -42.760 1.00 43.29  ? 224 THR A CG2 1 
ATOM   2010 N  N   . THR A 1 225 ? -19.407 -10.763 -42.591 1.00 30.89  ? 225 THR A N   1 
ATOM   2011 C  CA  . THR A 1 225 ? -18.581 -10.322 -43.734 1.00 29.72  ? 225 THR A CA  1 
ATOM   2012 C  C   . THR A 1 225 ? -17.824 -11.538 -44.236 1.00 29.14  ? 225 THR A C   1 
ATOM   2013 O  O   . THR A 1 225 ? -17.690 -12.483 -43.472 1.00 32.19  ? 225 THR A O   1 
ATOM   2014 C  CB  . THR A 1 225 ? -17.650 -9.160  -43.367 1.00 28.16  ? 225 THR A CB  1 
ATOM   2015 O  OG1 . THR A 1 225 ? -16.882 -8.832  -44.526 1.00 27.97  ? 225 THR A OG1 1 
ATOM   2016 C  CG2 . THR A 1 225 ? -16.705 -9.488  -42.227 1.00 30.93  ? 225 THR A CG2 1 
ATOM   2017 N  N   . THR A 1 226 ? -17.398 -11.516 -45.494 1.00 30.55  ? 226 THR A N   1 
ATOM   2018 C  CA  . THR A 1 226 ? -16.371 -12.456 -45.998 1.00 31.60  ? 226 THR A CA  1 
ATOM   2019 C  C   . THR A 1 226 ? -15.029 -11.932 -45.489 1.00 32.90  ? 226 THR A C   1 
ATOM   2020 O  O   . THR A 1 226 ? -14.908 -10.696 -45.274 1.00 28.19  ? 226 THR A O   1 
ATOM   2021 C  CB  . THR A 1 226 ? -16.370 -12.597 -47.523 1.00 30.41  ? 226 THR A CB  1 
ATOM   2022 O  OG1 . THR A 1 226 ? -15.823 -11.398 -48.073 1.00 29.08  ? 226 THR A OG1 1 
ATOM   2023 C  CG2 . THR A 1 226 ? -17.748 -12.901 -48.079 1.00 29.83  ? 226 THR A CG2 1 
ATOM   2024 N  N   . LEU A 1 227 ? -14.074 -12.840 -45.325 1.00 31.49  ? 227 LEU A N   1 
ATOM   2025 C  CA  . LEU A 1 227 ? -12.710 -12.505 -44.886 1.00 33.79  ? 227 LEU A CA  1 
ATOM   2026 C  C   . LEU A 1 227 ? -12.130 -11.490 -45.860 1.00 31.32  ? 227 LEU A C   1 
ATOM   2027 O  O   . LEU A 1 227 ? -11.463 -10.580 -45.395 1.00 27.97  ? 227 LEU A O   1 
ATOM   2028 C  CB  . LEU A 1 227 ? -11.848 -13.766 -44.837 1.00 35.15  ? 227 LEU A CB  1 
ATOM   2029 C  CG  . LEU A 1 227 ? -10.426 -13.562 -44.303 1.00 34.54  ? 227 LEU A CG  1 
ATOM   2030 C  CD1 . LEU A 1 227 ? -10.432 -12.829 -42.958 1.00 31.40  ? 227 LEU A CD1 1 
ATOM   2031 C  CD2 . LEU A 1 227 ? -9.712  -14.900 -44.192 1.00 32.29  ? 227 LEU A CD2 1 
ATOM   2032 N  N   . ASN A 1 228 ? -12.350 -11.673 -47.160 1.00 31.43  ? 228 ASN A N   1 
ATOM   2033 C  CA  . ASN A 1 228 ? -11.719 -10.785 -48.167 1.00 32.08  ? 228 ASN A CA  1 
ATOM   2034 C  C   . ASN A 1 228 ? -12.324 -9.372  -48.083 1.00 28.76  ? 228 ASN A C   1 
ATOM   2035 O  O   . ASN A 1 228 ? -11.550 -8.383  -48.109 1.00 28.93  ? 228 ASN A O   1 
ATOM   2036 C  CB  . ASN A 1 228 ? -11.808 -11.326 -49.593 1.00 36.27  ? 228 ASN A CB  1 
ATOM   2037 C  CG  . ASN A 1 228 ? -10.879 -10.547 -50.500 1.00 44.52  ? 228 ASN A CG  1 
ATOM   2038 O  OD1 . ASN A 1 228 ? -11.334 -9.834  -51.398 1.00 46.18  ? 228 ASN A OD1 1 
ATOM   2039 N  ND2 . ASN A 1 228 ? -9.580  -10.608 -50.214 1.00 42.96  ? 228 ASN A ND2 1 
ATOM   2040 N  N   . ASP A 1 229 ? -13.647 -9.250  -47.974 1.00 28.03  ? 229 ASP A N   1 
ATOM   2041 C  CA  . ASP A 1 229 ? -14.302 -7.917  -47.854 1.00 29.16  ? 229 ASP A CA  1 
ATOM   2042 C  C   . ASP A 1 229 ? -13.796 -7.226  -46.573 1.00 28.61  ? 229 ASP A C   1 
ATOM   2043 O  O   . ASP A 1 229 ? -13.598 -5.979  -46.567 1.00 25.41  ? 229 ASP A O   1 
ATOM   2044 C  CB  . ASP A 1 229 ? -15.827 -8.046  -47.861 1.00 31.17  ? 229 ASP A CB  1 
ATOM   2045 C  CG  . ASP A 1 229 ? -16.443 -8.200  -49.250 1.00 30.98  ? 229 ASP A CG  1 
ATOM   2046 O  OD1 . ASP A 1 229 ? -15.712 -8.038  -50.233 1.00 25.97  ? 229 ASP A OD1 1 
ATOM   2047 O  OD2 . ASP A 1 229 ? -17.671 -8.417  -49.308 1.00 32.40  ? 229 ASP A OD2 1 
ATOM   2048 N  N   . PHE A 1 230 ? -13.608 -7.989  -45.503 1.00 27.77  ? 230 PHE A N   1 
ATOM   2049 C  CA  . PHE A 1 230 ? -13.117 -7.420  -44.223 1.00 28.07  ? 230 PHE A CA  1 
ATOM   2050 C  C   . PHE A 1 230 ? -11.738 -6.793  -44.420 1.00 27.31  ? 230 PHE A C   1 
ATOM   2051 O  O   . PHE A 1 230 ? -11.524 -5.634  -43.980 1.00 27.57  ? 230 PHE A O   1 
ATOM   2052 C  CB  . PHE A 1 230 ? -13.096 -8.450  -43.098 1.00 30.10  ? 230 PHE A CB  1 
ATOM   2053 C  CG  . PHE A 1 230 ? -12.407 -7.873  -41.899 1.00 32.20  ? 230 PHE A CG  1 
ATOM   2054 C  CD1 . PHE A 1 230 ? -13.054 -6.954  -41.087 1.00 32.60  ? 230 PHE A CD1 1 
ATOM   2055 C  CD2 . PHE A 1 230 ? -11.069 -8.158  -41.659 1.00 34.73  ? 230 PHE A CD2 1 
ATOM   2056 C  CE1 . PHE A 1 230 ? -12.389 -6.399  -40.003 1.00 34.69  ? 230 PHE A CE1 1 
ATOM   2057 C  CE2 . PHE A 1 230 ? -10.408 -7.612  -40.574 1.00 32.24  ? 230 PHE A CE2 1 
ATOM   2058 C  CZ  . PHE A 1 230 ? -11.062 -6.716  -39.762 1.00 35.41  ? 230 PHE A CZ  1 
ATOM   2059 N  N   . ASN A 1 231 ? -10.848 -7.475  -45.136 1.00 26.04  ? 231 ASN A N   1 
ATOM   2060 C  CA  . ASN A 1 231 ? -9.451  -6.982  -45.321 1.00 26.44  ? 231 ASN A CA  1 
ATOM   2061 C  C   . ASN A 1 231 ? -9.448  -5.764  -46.248 1.00 28.50  ? 231 ASN A C   1 
ATOM   2062 O  O   . ASN A 1 231 ? -8.661  -4.839  -45.996 1.00 27.17  ? 231 ASN A O   1 
ATOM   2063 C  CB  . ASN A 1 231 ? -8.504  -8.112  -45.747 1.00 27.74  ? 231 ASN A CB  1 
ATOM   2064 C  CG  . ASN A 1 231 ? -8.177  -9.036  -44.587 1.00 29.31  ? 231 ASN A CG  1 
ATOM   2065 O  OD1 . ASN A 1 231 ? -8.077  -8.588  -43.451 1.00 30.85  ? 231 ASN A OD1 1 
ATOM   2066 N  ND2 . ASN A 1 231 ? -8.050  -10.327 -44.837 1.00 27.76  ? 231 ASN A ND2 1 
ATOM   2067 N  N   . LEU A 1 232 ? -10.300 -5.726  -47.275 1.00 26.22  ? 232 LEU A N   1 
ATOM   2068 C  CA  . LEU A 1 232 ? -10.360 -4.546  -48.173 1.00 26.92  ? 232 LEU A CA  1 
ATOM   2069 C  C   . LEU A 1 232 ? -10.789 -3.310  -47.361 1.00 25.78  ? 232 LEU A C   1 
ATOM   2070 O  O   . LEU A 1 232 ? -10.278 -2.223  -47.639 1.00 28.55  ? 232 LEU A O   1 
ATOM   2071 C  CB  . LEU A 1 232 ? -11.304 -4.836  -49.347 1.00 29.22  ? 232 LEU A CB  1 
ATOM   2072 C  CG  . LEU A 1 232 ? -10.819 -5.901  -50.339 1.00 29.55  ? 232 LEU A CG  1 
ATOM   2073 C  CD1 . LEU A 1 232 ? -11.952 -6.270  -51.295 1.00 30.96  ? 232 LEU A CD1 1 
ATOM   2074 C  CD2 . LEU A 1 232 ? -9.593  -5.405  -51.119 1.00 28.58  ? 232 LEU A CD2 1 
ATOM   2075 N  N   . VAL A 1 233 ? -11.693 -3.451  -46.388 1.00 27.55  ? 233 VAL A N   1 
ATOM   2076 C  CA  . VAL A 1 233 ? -12.130 -2.315  -45.510 1.00 28.90  ? 233 VAL A CA  1 
ATOM   2077 C  C   . VAL A 1 233 ? -11.024 -1.983  -44.492 1.00 26.90  ? 233 VAL A C   1 
ATOM   2078 O  O   . VAL A 1 233 ? -10.661 -0.805  -44.373 1.00 26.94  ? 233 VAL A O   1 
ATOM   2079 C  CB  . VAL A 1 233 ? -13.455 -2.631  -44.794 1.00 31.15  ? 233 VAL A CB  1 
ATOM   2080 C  CG1 . VAL A 1 233 ? -13.802 -1.562  -43.761 1.00 32.07  ? 233 VAL A CG1 1 
ATOM   2081 C  CG2 . VAL A 1 233 ? -14.594 -2.803  -45.783 1.00 31.70  ? 233 VAL A CG2 1 
ATOM   2082 N  N   . ALA A 1 234 ? -10.505 -2.997  -43.802 1.00 30.76  ? 234 ALA A N   1 
ATOM   2083 C  CA  . ALA A 1 234 ? -9.631  -2.843  -42.611 1.00 34.97  ? 234 ALA A CA  1 
ATOM   2084 C  C   . ALA A 1 234 ? -8.326  -2.163  -43.030 1.00 34.86  ? 234 ALA A C   1 
ATOM   2085 O  O   . ALA A 1 234 ? -7.797  -1.345  -42.259 1.00 39.93  ? 234 ALA A O   1 
ATOM   2086 C  CB  . ALA A 1 234 ? -9.393  -4.186  -41.961 1.00 36.27  ? 234 ALA A CB  1 
ATOM   2087 N  N   . MET A 1 235 ? -7.847  -2.450  -44.233 1.00 33.61  ? 235 MET A N   1 
ATOM   2088 C  CA  . MET A 1 235 ? -6.576  -1.885  -44.724 1.00 35.48  ? 235 MET A CA  1 
ATOM   2089 C  C   . MET A 1 235 ? -6.738  -0.408  -45.069 1.00 30.83  ? 235 MET A C   1 
ATOM   2090 O  O   . MET A 1 235 ? -5.728  0.288   -45.072 1.00 30.68  ? 235 MET A O   1 
ATOM   2091 C  CB  . MET A 1 235 ? -6.064  -2.673  -45.920 1.00 40.70  ? 235 MET A CB  1 
ATOM   2092 C  CG  . MET A 1 235 ? -5.577  -4.038  -45.468 1.00 49.86  ? 235 MET A CG  1 
ATOM   2093 S  SD  . MET A 1 235 ? -4.655  -4.942  -46.729 1.00 62.59  ? 235 MET A SD  1 
ATOM   2094 C  CE  . MET A 1 235 ? -3.803  -3.613  -47.589 1.00 57.02  ? 235 MET A CE  1 
ATOM   2095 N  N   . LYS A 1 236 ? -7.959  0.083   -45.253 1.00 27.51  ? 236 LYS A N   1 
ATOM   2096 C  CA  . LYS A 1 236 ? -8.153  1.523   -45.516 1.00 30.74  ? 236 LYS A CA  1 
ATOM   2097 C  C   . LYS A 1 236 ? -8.013  2.286   -44.206 1.00 27.75  ? 236 LYS A C   1 
ATOM   2098 O  O   . LYS A 1 236 ? -7.980  3.513   -44.259 1.00 30.12  ? 236 LYS A O   1 
ATOM   2099 C  CB  . LYS A 1 236 ? -9.498  1.794   -46.184 1.00 33.58  ? 236 LYS A CB  1 
ATOM   2100 C  CG  . LYS A 1 236 ? -9.643  1.187   -47.571 1.00 33.12  ? 236 LYS A CG  1 
ATOM   2101 C  CD  . LYS A 1 236 ? -11.091 1.160   -48.042 1.00 34.62  ? 236 LYS A CD  1 
ATOM   2102 C  CE  . LYS A 1 236 ? -11.262 0.323   -49.290 1.00 36.69  ? 236 LYS A CE  1 
ATOM   2103 N  NZ  . LYS A 1 236 ? -12.600 0.522   -49.886 1.00 44.03  ? 236 LYS A NZ  1 
ATOM   2104 N  N   . TYR A 1 237 ? -8.002  1.589   -43.076 1.00 25.79  ? 237 TYR A N   1 
ATOM   2105 C  CA  . TYR A 1 237 ? -7.739  2.221   -41.755 1.00 28.42  ? 237 TYR A CA  1 
ATOM   2106 C  C   . TYR A 1 237 ? -6.368  1.838   -41.198 1.00 27.10  ? 237 TYR A C   1 
ATOM   2107 O  O   . TYR A 1 237 ? -6.185  2.031   -40.013 1.00 26.25  ? 237 TYR A O   1 
ATOM   2108 C  CB  . TYR A 1 237 ? -8.808  1.819   -40.760 1.00 25.47  ? 237 TYR A CB  1 
ATOM   2109 C  CG  . TYR A 1 237 ? -10.196 2.220   -41.160 1.00 28.58  ? 237 TYR A CG  1 
ATOM   2110 C  CD1 . TYR A 1 237 ? -10.982 1.386   -41.935 1.00 29.94  ? 237 TYR A CD1 1 
ATOM   2111 C  CD2 . TYR A 1 237 ? -10.742 3.412   -40.712 1.00 30.66  ? 237 TYR A CD2 1 
ATOM   2112 C  CE1 . TYR A 1 237 ? -12.294 1.712   -42.244 1.00 32.42  ? 237 TYR A CE1 1 
ATOM   2113 C  CE2 . TYR A 1 237 ? -12.053 3.748   -41.007 1.00 32.30  ? 237 TYR A CE2 1 
ATOM   2114 C  CZ  . TYR A 1 237 ? -12.835 2.902   -41.781 1.00 35.07  ? 237 TYR A CZ  1 
ATOM   2115 O  OH  . TYR A 1 237 ? -14.133 3.241   -42.090 1.00 35.36  ? 237 TYR A OH  1 
ATOM   2116 N  N   . ASN A 1 238 ? -5.461  1.325   -42.029 1.00 31.97  ? 238 ASN A N   1 
ATOM   2117 C  CA  . ASN A 1 238 ? -4.078  0.949   -41.626 1.00 32.91  ? 238 ASN A CA  1 
ATOM   2118 C  C   . ASN A 1 238 ? -4.112  -0.242  -40.655 1.00 32.01  ? 238 ASN A C   1 
ATOM   2119 O  O   . ASN A 1 238 ? -3.237  -0.316  -39.766 1.00 29.22  ? 238 ASN A O   1 
ATOM   2120 C  CB  . ASN A 1 238 ? -3.350  2.158   -41.028 1.00 36.02  ? 238 ASN A CB  1 
ATOM   2121 C  CG  . ASN A 1 238 ? -2.580  2.919   -42.080 1.00 39.66  ? 238 ASN A CG  1 
ATOM   2122 O  OD1 . ASN A 1 238 ? -1.987  2.318   -42.962 1.00 47.43  ? 238 ASN A OD1 1 
ATOM   2123 N  ND2 . ASN A 1 238 ? -2.570  4.235   -41.982 1.00 46.53  ? 238 ASN A ND2 1 
ATOM   2124 N  N   . TYR A 1 239 ? -5.081  -1.142  -40.809 1.00 27.64  ? 239 TYR A N   1 
ATOM   2125 C  CA  . TYR A 1 239 ? -5.186  -2.391  -40.024 1.00 27.16  ? 239 TYR A CA  1 
ATOM   2126 C  C   . TYR A 1 239 ? -4.400  -3.453  -40.779 1.00 29.10  ? 239 TYR A C   1 
ATOM   2127 O  O   . TYR A 1 239 ? -4.458  -3.469  -42.020 1.00 30.45  ? 239 TYR A O   1 
ATOM   2128 C  CB  . TYR A 1 239 ? -6.649  -2.792  -39.816 1.00 27.56  ? 239 TYR A CB  1 
ATOM   2129 C  CG  . TYR A 1 239 ? -7.252  -2.244  -38.555 1.00 24.25  ? 239 TYR A CG  1 
ATOM   2130 C  CD1 . TYR A 1 239 ? -7.352  -0.878  -38.338 1.00 27.08  ? 239 TYR A CD1 1 
ATOM   2131 C  CD2 . TYR A 1 239 ? -7.681  -3.091  -37.566 1.00 25.24  ? 239 TYR A CD2 1 
ATOM   2132 C  CE1 . TYR A 1 239 ? -7.859  -0.371  -37.154 1.00 26.58  ? 239 TYR A CE1 1 
ATOM   2133 C  CE2 . TYR A 1 239 ? -8.221  -2.604  -36.391 1.00 27.65  ? 239 TYR A CE2 1 
ATOM   2134 C  CZ  . TYR A 1 239 ? -8.303  -1.243  -36.180 1.00 25.86  ? 239 TYR A CZ  1 
ATOM   2135 O  OH  . TYR A 1 239 ? -8.814  -0.810  -34.995 1.00 26.87  ? 239 TYR A OH  1 
ATOM   2136 N  N   . GLU A 1 240 ? -3.645  -4.255  -40.046 1.00 29.45  ? 240 GLU A N   1 
ATOM   2137 C  CA  . GLU A 1 240 ? -3.016  -5.494  -40.543 1.00 31.68  ? 240 GLU A CA  1 
ATOM   2138 C  C   . GLU A 1 240 ? -4.063  -6.372  -41.221 1.00 30.57  ? 240 GLU A C   1 
ATOM   2139 O  O   . GLU A 1 240 ? -5.186  -6.510  -40.737 1.00 26.24  ? 240 GLU A O   1 
ATOM   2140 C  CB  . GLU A 1 240 ? -2.402  -6.282  -39.381 1.00 34.46  ? 240 GLU A CB  1 
ATOM   2141 C  CG  . GLU A 1 240 ? -1.029  -5.786  -39.000 1.00 37.46  ? 240 GLU A CG  1 
ATOM   2142 C  CD  . GLU A 1 240 ? -0.007  -5.972  -40.103 1.00 40.21  ? 240 GLU A CD  1 
ATOM   2143 O  OE1 . GLU A 1 240 ? 0.444   -7.142  -40.297 1.00 44.34  ? 240 GLU A OE1 1 
ATOM   2144 O  OE2 . GLU A 1 240 ? 0.346   -4.944  -40.759 1.00 38.16  ? 240 GLU A OE2 1 
ATOM   2145 N  N   . PRO A 1 241 ? -3.705  -7.040  -42.334 1.00 31.50  ? 241 PRO A N   1 
ATOM   2146 C  CA  . PRO A 1 241 ? -4.564  -8.067  -42.912 1.00 30.97  ? 241 PRO A CA  1 
ATOM   2147 C  C   . PRO A 1 241 ? -4.816  -9.163  -41.876 1.00 29.87  ? 241 PRO A C   1 
ATOM   2148 O  O   . PRO A 1 241 ? -3.917  -9.505  -41.138 1.00 29.87  ? 241 PRO A O   1 
ATOM   2149 C  CB  . PRO A 1 241 ? -3.744  -8.599  -44.092 1.00 33.80  ? 241 PRO A CB  1 
ATOM   2150 C  CG  . PRO A 1 241 ? -2.880  -7.424  -44.470 1.00 33.83  ? 241 PRO A CG  1 
ATOM   2151 C  CD  . PRO A 1 241 ? -2.502  -6.804  -43.141 1.00 33.52  ? 241 PRO A CD  1 
ATOM   2152 N  N   . LEU A 1 242 ? -6.058  -9.597  -41.781 1.00 26.59  ? 242 LEU A N   1 
ATOM   2153 C  CA  . LEU A 1 242 ? -6.453  -10.779 -40.991 1.00 27.58  ? 242 LEU A CA  1 
ATOM   2154 C  C   . LEU A 1 242 ? -6.291  -11.997 -41.909 1.00 30.70  ? 242 LEU A C   1 
ATOM   2155 O  O   . LEU A 1 242 ? -6.803  -11.930 -43.025 1.00 29.94  ? 242 LEU A O   1 
ATOM   2156 C  CB  . LEU A 1 242 ? -7.909  -10.627 -40.528 1.00 28.06  ? 242 LEU A CB  1 
ATOM   2157 C  CG  . LEU A 1 242 ? -8.338  -11.633 -39.460 1.00 28.45  ? 242 LEU A CG  1 
ATOM   2158 C  CD1 . LEU A 1 242 ? -7.754  -11.263 -38.094 1.00 27.81  ? 242 LEU A CD1 1 
ATOM   2159 C  CD2 . LEU A 1 242 ? -9.853  -11.754 -39.385 1.00 31.00  ? 242 LEU A CD2 1 
ATOM   2160 N  N   . THR A 1 243 ? -5.629  -13.046 -41.427 1.00 29.79  ? 243 THR A N   1 
ATOM   2161 C  CA  . THR A 1 243 ? -5.345  -14.298 -42.164 1.00 29.66  ? 243 THR A CA  1 
ATOM   2162 C  C   . THR A 1 243 ? -6.210  -15.426 -41.607 1.00 29.19  ? 243 THR A C   1 
ATOM   2163 O  O   . THR A 1 243 ? -6.808  -15.277 -40.518 1.00 26.78  ? 243 THR A O   1 
ATOM   2164 C  CB  . THR A 1 243 ? -3.870  -14.710 -42.031 1.00 31.37  ? 243 THR A CB  1 
ATOM   2165 O  OG1 . THR A 1 243 ? -3.675  -15.158 -40.684 1.00 28.84  ? 243 THR A OG1 1 
ATOM   2166 C  CG2 . THR A 1 243 ? -2.906  -13.601 -42.394 1.00 30.68  ? 243 THR A CG2 1 
ATOM   2167 N  N   . GLN A 1 244 ? -6.219  -16.557 -42.298 1.00 30.99  ? 244 GLN A N   1 
ATOM   2168 C  CA  . GLN A 1 244 ? -6.989  -17.736 -41.848 1.00 31.69  ? 244 GLN A CA  1 
ATOM   2169 C  C   . GLN A 1 244 ? -6.398  -18.197 -40.528 1.00 29.84  ? 244 GLN A C   1 
ATOM   2170 O  O   . GLN A 1 244 ? -7.185  -18.579 -39.632 1.00 33.95  ? 244 GLN A O   1 
ATOM   2171 C  CB  . GLN A 1 244 ? -7.000  -18.868 -42.877 1.00 32.88  ? 244 GLN A CB  1 
ATOM   2172 C  CG  . GLN A 1 244 ? -7.864  -20.047 -42.431 1.00 34.35  ? 244 GLN A CG  1 
ATOM   2173 C  CD  . GLN A 1 244 ? -9.307  -19.641 -42.211 1.00 35.29  ? 244 GLN A CD  1 
ATOM   2174 O  OE1 . GLN A 1 244 ? -9.879  -18.863 -42.970 1.00 37.39  ? 244 GLN A OE1 1 
ATOM   2175 N  NE2 . GLN A 1 244 ? -9.900  -20.134 -41.137 1.00 34.85  ? 244 GLN A NE2 1 
ATOM   2176 N  N   . ASP A 1 245 ? -5.069  -18.150 -40.400 1.00 30.41  ? 245 ASP A N   1 
ATOM   2177 C  CA  . ASP A 1 245 ? -4.379  -18.387 -39.105 1.00 32.07  ? 245 ASP A CA  1 
ATOM   2178 C  C   . ASP A 1 245 ? -5.053  -17.593 -37.975 1.00 29.38  ? 245 ASP A C   1 
ATOM   2179 O  O   . ASP A 1 245 ? -5.403  -18.199 -36.946 1.00 29.08  ? 245 ASP A O   1 
ATOM   2180 C  CB  . ASP A 1 245 ? -2.890  -18.046 -39.204 1.00 35.48  ? 245 ASP A CB  1 
ATOM   2181 C  CG  . ASP A 1 245 ? -2.057  -19.254 -39.595 1.00 36.10  ? 245 ASP A CG  1 
ATOM   2182 O  OD1 . ASP A 1 245 ? -2.637  -20.218 -40.094 1.00 35.87  ? 245 ASP A OD1 1 
ATOM   2183 O  OD2 . ASP A 1 245 ? -0.852  -19.214 -39.386 1.00 38.36  ? 245 ASP A OD2 1 
ATOM   2184 N  N   . HIS A 1 246 ? -5.187  -16.280 -38.138 1.00 28.78  ? 246 HIS A N   1 
ATOM   2185 C  CA  . HIS A 1 246 ? -5.803  -15.378 -37.130 1.00 29.15  ? 246 HIS A CA  1 
ATOM   2186 C  C   . HIS A 1 246 ? -7.238  -15.859 -36.826 1.00 30.44  ? 246 HIS A C   1 
ATOM   2187 O  O   . HIS A 1 246 ? -7.618  -15.958 -35.634 1.00 30.91  ? 246 HIS A O   1 
ATOM   2188 C  CB  . HIS A 1 246 ? -5.758  -13.926 -37.625 1.00 28.67  ? 246 HIS A CB  1 
ATOM   2189 C  CG  . HIS A 1 246 ? -4.383  -13.369 -37.793 1.00 27.97  ? 246 HIS A CG  1 
ATOM   2190 N  ND1 . HIS A 1 246 ? -4.115  -12.379 -38.702 1.00 24.14  ? 246 HIS A ND1 1 
ATOM   2191 C  CD2 . HIS A 1 246 ? -3.210  -13.652 -37.166 1.00 26.13  ? 246 HIS A CD2 1 
ATOM   2192 C  CE1 . HIS A 1 246 ? -2.825  -12.089 -38.660 1.00 26.24  ? 246 HIS A CE1 1 
ATOM   2193 N  NE2 . HIS A 1 246 ? -2.249  -12.838 -37.694 1.00 24.97  ? 246 HIS A NE2 1 
ATOM   2194 N  N   . VAL A 1 247 ? -7.994  -16.219 -37.860 1.00 31.51  ? 247 VAL A N   1 
ATOM   2195 C  CA  . VAL A 1 247 ? -9.381  -16.745 -37.704 1.00 31.04  ? 247 VAL A CA  1 
ATOM   2196 C  C   . VAL A 1 247 ? -9.378  -18.027 -36.861 1.00 32.75  ? 247 VAL A C   1 
ATOM   2197 O  O   . VAL A 1 247 ? -10.207 -18.121 -35.930 1.00 34.61  ? 247 VAL A O   1 
ATOM   2198 C  CB  . VAL A 1 247 ? -10.048 -16.941 -39.072 1.00 30.83  ? 247 VAL A CB  1 
ATOM   2199 C  CG1 . VAL A 1 247 ? -11.396 -17.634 -38.942 1.00 30.63  ? 247 VAL A CG1 1 
ATOM   2200 C  CG2 . VAL A 1 247 ? -10.200 -15.607 -39.782 1.00 31.25  ? 247 VAL A CG2 1 
ATOM   2201 N  N   . ASP A 1 248 ? -8.464  -18.964 -37.136 1.00 33.73  ? 248 ASP A N   1 
ATOM   2202 C  CA  . ASP A 1 248 ? -8.331  -20.231 -36.362 1.00 32.12  ? 248 ASP A CA  1 
ATOM   2203 C  C   . ASP A 1 248 ? -8.029  -19.904 -34.893 1.00 33.90  ? 248 ASP A C   1 
ATOM   2204 O  O   . ASP A 1 248 ? -8.637  -20.521 -33.992 1.00 30.63  ? 248 ASP A O   1 
ATOM   2205 C  CB  . ASP A 1 248 ? -7.270  -21.164 -36.973 1.00 31.70  ? 248 ASP A CB  1 
ATOM   2206 C  CG  . ASP A 1 248 ? -7.611  -21.663 -38.378 1.00 31.61  ? 248 ASP A CG  1 
ATOM   2207 O  OD1 . ASP A 1 248 ? -8.764  -21.497 -38.820 1.00 34.68  ? 248 ASP A OD1 1 
ATOM   2208 O  OD2 . ASP A 1 248 ? -6.714  -22.191 -39.034 1.00 33.46  ? 248 ASP A OD2 1 
ATOM   2209 N  N   . ILE A 1 249 ? -7.133  -18.949 -34.654 1.00 33.16  ? 249 ILE A N   1 
ATOM   2210 C  CA  . ILE A 1 249 ? -6.644  -18.595 -33.295 1.00 33.03  ? 249 ILE A CA  1 
ATOM   2211 C  C   . ILE A 1 249 ? -7.812  -18.066 -32.440 1.00 30.46  ? 249 ILE A C   1 
ATOM   2212 O  O   . ILE A 1 249 ? -7.817  -18.301 -31.236 1.00 29.84  ? 249 ILE A O   1 
ATOM   2213 C  CB  . ILE A 1 249 ? -5.485  -17.585 -33.444 1.00 36.99  ? 249 ILE A CB  1 
ATOM   2214 C  CG1 . ILE A 1 249 ? -4.225  -18.261 -34.003 1.00 45.45  ? 249 ILE A CG1 1 
ATOM   2215 C  CG2 . ILE A 1 249 ? -5.190  -16.891 -32.142 1.00 35.39  ? 249 ILE A CG2 1 
ATOM   2216 C  CD1 . ILE A 1 249 ? -3.076  -17.300 -34.338 1.00 47.27  ? 249 ILE A CD1 1 
ATOM   2217 N  N   . LEU A 1 250 ? -8.773  -17.360 -33.033 1.00 31.18  ? 250 LEU A N   1 
ATOM   2218 C  CA  . LEU A 1 250 ? -9.934  -16.775 -32.308 1.00 27.96  ? 250 LEU A CA  1 
ATOM   2219 C  C   . LEU A 1 250 ? -11.040 -17.816 -32.069 1.00 30.42  ? 250 LEU A C   1 
ATOM   2220 O  O   . LEU A 1 250 ? -11.941 -17.494 -31.276 1.00 32.66  ? 250 LEU A O   1 
ATOM   2221 C  CB  . LEU A 1 250 ? -10.445 -15.587 -33.120 1.00 26.88  ? 250 LEU A CB  1 
ATOM   2222 C  CG  . LEU A 1 250 ? -9.486  -14.411 -33.190 1.00 26.41  ? 250 LEU A CG  1 
ATOM   2223 C  CD1 . LEU A 1 250 ? -9.892  -13.434 -34.292 1.00 27.05  ? 250 LEU A CD1 1 
ATOM   2224 C  CD2 . LEU A 1 250 ? -9.387  -13.714 -31.828 1.00 26.80  ? 250 LEU A CD2 1 
ATOM   2225 N  N   . GLY A 1 251 ? -10.946 -19.013 -32.675 1.00 33.02  ? 251 GLY A N   1 
ATOM   2226 C  CA  . GLY A 1 251 ? -11.936 -20.113 -32.597 1.00 31.74  ? 251 GLY A CA  1 
ATOM   2227 C  C   . GLY A 1 251 ? -12.460 -20.330 -31.180 1.00 35.37  ? 251 GLY A C   1 
ATOM   2228 O  O   . GLY A 1 251 ? -13.667 -20.332 -30.937 1.00 38.41  ? 251 GLY A O   1 
ATOM   2229 N  N   . PRO A 1 252 ? -11.574 -20.551 -30.191 1.00 34.70  ? 252 PRO A N   1 
ATOM   2230 C  CA  . PRO A 1 252 ? -12.004 -20.729 -28.799 1.00 35.37  ? 252 PRO A CA  1 
ATOM   2231 C  C   . PRO A 1 252 ? -12.825 -19.571 -28.195 1.00 37.25  ? 252 PRO A C   1 
ATOM   2232 O  O   . PRO A 1 252 ? -13.752 -19.830 -27.445 1.00 32.02  ? 252 PRO A O   1 
ATOM   2233 C  CB  . PRO A 1 252 ? -10.669 -20.884 -28.045 1.00 34.18  ? 252 PRO A CB  1 
ATOM   2234 C  CG  . PRO A 1 252 ? -9.713  -21.420 -29.082 1.00 34.40  ? 252 PRO A CG  1 
ATOM   2235 C  CD  . PRO A 1 252 ? -10.128 -20.758 -30.378 1.00 34.34  ? 252 PRO A CD  1 
ATOM   2236 N  N   . LEU A 1 253 ? -12.466 -18.318 -28.490 1.00 36.33  ? 253 LEU A N   1 
ATOM   2237 C  CA  . LEU A 1 253 ? -13.216 -17.126 -28.010 1.00 35.38  ? 253 LEU A CA  1 
ATOM   2238 C  C   . LEU A 1 253 ? -14.555 -17.026 -28.760 1.00 36.36  ? 253 LEU A C   1 
ATOM   2239 O  O   . LEU A 1 253 ? -15.550 -16.635 -28.130 1.00 37.00  ? 253 LEU A O   1 
ATOM   2240 C  CB  . LEU A 1 253 ? -12.369 -15.862 -28.195 1.00 33.81  ? 253 LEU A CB  1 
ATOM   2241 C  CG  . LEU A 1 253 ? -11.183 -15.710 -27.252 1.00 35.25  ? 253 LEU A CG  1 
ATOM   2242 C  CD1 . LEU A 1 253 ? -10.195 -14.671 -27.783 1.00 33.45  ? 253 LEU A CD1 1 
ATOM   2243 C  CD2 . LEU A 1 253 ? -11.641 -15.332 -25.844 1.00 38.31  ? 253 LEU A CD2 1 
ATOM   2244 N  N   . SER A 1 254 ? -14.567 -17.362 -30.050 1.00 36.70  ? 254 SER A N   1 
ATOM   2245 C  CA  . SER A 1 254 ? -15.776 -17.605 -30.879 1.00 40.57  ? 254 SER A CA  1 
ATOM   2246 C  C   . SER A 1 254 ? -16.712 -18.592 -30.169 1.00 42.26  ? 254 SER A C   1 
ATOM   2247 O  O   . SER A 1 254 ? -17.872 -18.228 -29.902 1.00 40.80  ? 254 SER A O   1 
ATOM   2248 C  CB  . SER A 1 254 ? -15.394 -18.131 -32.228 1.00 39.88  ? 254 SER A CB  1 
ATOM   2249 O  OG  . SER A 1 254 ? -16.495 -18.060 -33.102 1.00 45.61  ? 254 SER A OG  1 
ATOM   2250 N  N   . ALA A 1 255 ? -16.210 -19.792 -29.876 1.00 44.48  ? 255 ALA A N   1 
ATOM   2251 C  CA  . ALA A 1 255 ? -16.960 -20.906 -29.251 1.00 45.46  ? 255 ALA A CA  1 
ATOM   2252 C  C   . ALA A 1 255 ? -17.455 -20.454 -27.875 1.00 44.52  ? 255 ALA A C   1 
ATOM   2253 O  O   . ALA A 1 255 ? -18.640 -20.629 -27.599 1.00 49.28  ? 255 ALA A O   1 
ATOM   2254 C  CB  . ALA A 1 255 ? -16.098 -22.144 -29.153 1.00 45.27  ? 255 ALA A CB  1 
ATOM   2255 N  N   . GLN A 1 256 ? -16.593 -19.852 -27.064 1.00 44.68  ? 256 GLN A N   1 
ATOM   2256 C  CA  . GLN A 1 256 ? -16.971 -19.360 -25.715 1.00 49.58  ? 256 GLN A CA  1 
ATOM   2257 C  C   . GLN A 1 256 ? -18.190 -18.423 -25.811 1.00 53.42  ? 256 GLN A C   1 
ATOM   2258 O  O   . GLN A 1 256 ? -19.160 -18.633 -25.061 1.00 50.45  ? 256 GLN A O   1 
ATOM   2259 C  CB  . GLN A 1 256 ? -15.779 -18.688 -25.032 1.00 54.19  ? 256 GLN A CB  1 
ATOM   2260 C  CG  . GLN A 1 256 ? -16.149 -18.028 -23.712 1.00 54.62  ? 256 GLN A CG  1 
ATOM   2261 C  CD  . GLN A 1 256 ? -14.990 -17.912 -22.758 1.00 53.81  ? 256 GLN A CD  1 
ATOM   2262 O  OE1 . GLN A 1 256 ? -13.849 -18.220 -23.093 1.00 55.53  ? 256 GLN A OE1 1 
ATOM   2263 N  NE2 . GLN A 1 256 ? -15.280 -17.442 -21.556 1.00 52.22  ? 256 GLN A NE2 1 
ATOM   2264 N  N   . THR A 1 257 ? -18.157 -17.411 -26.679 1.00 51.34  ? 257 THR A N   1 
ATOM   2265 C  CA  . THR A 1 257 ? -19.158 -16.311 -26.682 1.00 46.96  ? 257 THR A CA  1 
ATOM   2266 C  C   . THR A 1 257 ? -20.322 -16.642 -27.627 1.00 48.62  ? 257 THR A C   1 
ATOM   2267 O  O   . THR A 1 257 ? -21.336 -15.942 -27.540 1.00 51.32  ? 257 THR A O   1 
ATOM   2268 C  CB  . THR A 1 257 ? -18.524 -14.968 -27.055 1.00 42.40  ? 257 THR A CB  1 
ATOM   2269 O  OG1 . THR A 1 257 ? -18.053 -15.114 -28.394 1.00 37.27  ? 257 THR A OG1 1 
ATOM   2270 C  CG2 . THR A 1 257 ? -17.430 -14.547 -26.098 1.00 41.70  ? 257 THR A CG2 1 
ATOM   2271 N  N   . GLY A 1 258 ? -20.168 -17.645 -28.499 1.00 47.87  ? 258 GLY A N   1 
ATOM   2272 C  CA  . GLY A 1 258 ? -21.152 -18.007 -29.536 1.00 44.26  ? 258 GLY A CA  1 
ATOM   2273 C  C   . GLY A 1 258 ? -21.240 -16.992 -30.676 1.00 46.25  ? 258 GLY A C   1 
ATOM   2274 O  O   . GLY A 1 258 ? -22.201 -17.087 -31.467 1.00 44.50  ? 258 GLY A O   1 
ATOM   2275 N  N   . ILE A 1 259 ? -20.268 -16.082 -30.821 1.00 42.13  ? 259 ILE A N   1 
ATOM   2276 C  CA  . ILE A 1 259 ? -20.197 -15.107 -31.956 1.00 38.83  ? 259 ILE A CA  1 
ATOM   2277 C  C   . ILE A 1 259 ? -19.078 -15.544 -32.912 1.00 37.65  ? 259 ILE A C   1 
ATOM   2278 O  O   . ILE A 1 259 ? -17.905 -15.564 -32.485 1.00 35.50  ? 259 ILE A O   1 
ATOM   2279 C  CB  . ILE A 1 259 ? -19.955 -13.683 -31.419 1.00 37.63  ? 259 ILE A CB  1 
ATOM   2280 C  CG1 . ILE A 1 259 ? -20.999 -13.282 -30.372 1.00 38.77  ? 259 ILE A CG1 1 
ATOM   2281 C  CG2 . ILE A 1 259 ? -19.862 -12.682 -32.557 1.00 35.66  ? 259 ILE A CG2 1 
ATOM   2282 C  CD1 . ILE A 1 259 ? -20.621 -12.043 -29.572 1.00 39.09  ? 259 ILE A CD1 1 
ATOM   2283 N  N   . ALA A 1 260 ? -19.430 -15.898 -34.145 1.00 34.44  ? 260 ALA A N   1 
ATOM   2284 C  CA  . ALA A 1 260 ? -18.497 -16.305 -35.216 1.00 35.15  ? 260 ALA A CA  1 
ATOM   2285 C  C   . ALA A 1 260 ? -17.432 -15.215 -35.399 1.00 35.95  ? 260 ALA A C   1 
ATOM   2286 O  O   . ALA A 1 260 ? -17.720 -14.016 -35.112 1.00 28.12  ? 260 ALA A O   1 
ATOM   2287 C  CB  . ALA A 1 260 ? -19.242 -16.542 -36.501 1.00 33.89  ? 260 ALA A CB  1 
ATOM   2288 N  N   . VAL A 1 261 ? -16.255 -15.613 -35.892 1.00 32.13  ? 261 VAL A N   1 
ATOM   2289 C  CA  . VAL A 1 261 ? -15.117 -14.681 -36.104 1.00 31.99  ? 261 VAL A CA  1 
ATOM   2290 C  C   . VAL A 1 261 ? -15.536 -13.632 -37.133 1.00 28.28  ? 261 VAL A C   1 
ATOM   2291 O  O   . VAL A 1 261 ? -15.329 -12.439 -36.862 1.00 25.77  ? 261 VAL A O   1 
ATOM   2292 C  CB  . VAL A 1 261 ? -13.812 -15.408 -36.471 1.00 31.44  ? 261 VAL A CB  1 
ATOM   2293 C  CG1 . VAL A 1 261 ? -12.749 -14.427 -36.957 1.00 30.94  ? 261 VAL A CG1 1 
ATOM   2294 C  CG2 . VAL A 1 261 ? -13.296 -16.226 -35.284 1.00 33.99  ? 261 VAL A CG2 1 
ATOM   2295 N  N   . LEU A 1 262 ? -16.147 -14.031 -38.244 1.00 29.16  ? 262 LEU A N   1 
ATOM   2296 C  CA  . LEU A 1 262 ? -16.564 -13.050 -39.287 1.00 30.54  ? 262 LEU A CA  1 
ATOM   2297 C  C   . LEU A 1 262 ? -17.782 -12.211 -38.859 1.00 28.66  ? 262 LEU A C   1 
ATOM   2298 O  O   . LEU A 1 262 ? -17.960 -11.115 -39.434 1.00 30.83  ? 262 LEU A O   1 
ATOM   2299 C  CB  . LEU A 1 262 ? -16.780 -13.790 -40.601 1.00 32.74  ? 262 LEU A CB  1 
ATOM   2300 C  CG  . LEU A 1 262 ? -15.498 -14.365 -41.200 1.00 34.89  ? 262 LEU A CG  1 
ATOM   2301 C  CD1 . LEU A 1 262 ? -15.826 -15.327 -42.337 1.00 37.83  ? 262 LEU A CD1 1 
ATOM   2302 C  CD2 . LEU A 1 262 ? -14.571 -13.258 -41.693 1.00 34.93  ? 262 LEU A CD2 1 
ATOM   2303 N  N   . ASP A 1 263 ? -18.528 -12.595 -37.826 1.00 31.77  ? 263 ASP A N   1 
ATOM   2304 C  CA  . ASP A 1 263 ? -19.566 -11.699 -37.253 1.00 33.68  ? 263 ASP A CA  1 
ATOM   2305 C  C   . ASP A 1 263 ? -18.844 -10.614 -36.469 1.00 31.15  ? 263 ASP A C   1 
ATOM   2306 O  O   . ASP A 1 263 ? -19.183 -9.427  -36.637 1.00 29.84  ? 263 ASP A O   1 
ATOM   2307 C  CB  . ASP A 1 263 ? -20.554 -12.382 -36.304 1.00 43.93  ? 263 ASP A CB  1 
ATOM   2308 C  CG  . ASP A 1 263 ? -21.618 -13.228 -36.972 1.00 50.86  ? 263 ASP A CG  1 
ATOM   2309 O  OD1 . ASP A 1 263 ? -21.535 -13.433 -38.221 1.00 56.27  ? 263 ASP A OD1 1 
ATOM   2310 O  OD2 . ASP A 1 263 ? -22.521 -13.680 -36.233 1.00 52.73  ? 263 ASP A OD2 1 
ATOM   2311 N  N   . MET A 1 264 ? -17.898 -11.002 -35.614 1.00 33.09  ? 264 MET A N   1 
ATOM   2312 C  CA  . MET A 1 264 ? -17.139 -9.993  -34.832 1.00 31.34  ? 264 MET A CA  1 
ATOM   2313 C  C   . MET A 1 264 ? -16.423 -9.051  -35.804 1.00 29.38  ? 264 MET A C   1 
ATOM   2314 O  O   . MET A 1 264 ? -16.381 -7.850  -35.500 1.00 28.05  ? 264 MET A O   1 
ATOM   2315 C  CB  . MET A 1 264 ? -16.134 -10.606 -33.856 1.00 32.26  ? 264 MET A CB  1 
ATOM   2316 C  CG  . MET A 1 264 ? -15.617 -9.597  -32.864 1.00 29.29  ? 264 MET A CG  1 
ATOM   2317 S  SD  . MET A 1 264 ? -16.938 -8.922  -31.805 1.00 29.22  ? 264 MET A SD  1 
ATOM   2318 C  CE  . MET A 1 264 ? -17.204 -10.323 -30.723 1.00 29.94  ? 264 MET A CE  1 
ATOM   2319 N  N   . CYS A 1 265 ? -15.942 -9.561  -36.943 1.00 27.73  ? 265 CYS A N   1 
ATOM   2320 C  CA  . CYS A 1 265 ? -15.242 -8.744  -37.960 1.00 28.87  ? 265 CYS A CA  1 
ATOM   2321 C  C   . CYS A 1 265 ? -16.193 -7.661  -38.489 1.00 27.95  ? 265 CYS A C   1 
ATOM   2322 O  O   . CYS A 1 265 ? -15.700 -6.556  -38.802 1.00 28.08  ? 265 CYS A O   1 
ATOM   2323 C  CB  . CYS A 1 265 ? -14.674 -9.586  -39.099 1.00 28.60  ? 265 CYS A CB  1 
ATOM   2324 S  SG  . CYS A 1 265 ? -13.173 -10.507 -38.656 1.00 28.13  ? 265 CYS A SG  1 
ATOM   2325 N  N   . ALA A 1 266 ? -17.490 -7.965  -38.637 1.00 28.92  ? 266 ALA A N   1 
ATOM   2326 C  CA  . ALA A 1 266 ? -18.522 -7.008  -39.126 1.00 28.95  ? 266 ALA A CA  1 
ATOM   2327 C  C   . ALA A 1 266 ? -18.690 -5.870  -38.119 1.00 28.12  ? 266 ALA A C   1 
ATOM   2328 O  O   . ALA A 1 266 ? -18.793 -4.682  -38.514 1.00 29.27  ? 266 ALA A O   1 
ATOM   2329 C  CB  . ALA A 1 266 ? -19.842 -7.710  -39.352 1.00 33.36  ? 266 ALA A CB  1 
ATOM   2330 N  N   . SER A 1 267 ? -18.718 -6.227  -36.842 1.00 29.96  ? 267 SER A N   1 
ATOM   2331 C  CA  . SER A 1 267 ? -18.716 -5.296  -35.687 1.00 30.19  ? 267 SER A CA  1 
ATOM   2332 C  C   . SER A 1 267 ? -17.484 -4.378  -35.754 1.00 28.68  ? 267 SER A C   1 
ATOM   2333 O  O   . SER A 1 267 ? -17.634 -3.170  -35.674 1.00 26.70  ? 267 SER A O   1 
ATOM   2334 C  CB  . SER A 1 267 ? -18.799 -6.140  -34.421 1.00 34.65  ? 267 SER A CB  1 
ATOM   2335 O  OG  . SER A 1 267 ? -19.162 -5.388  -33.304 1.00 43.52  ? 267 SER A OG  1 
ATOM   2336 N  N   . LEU A 1 268 ? -16.274 -4.919  -35.910 1.00 28.70  ? 268 LEU A N   1 
ATOM   2337 C  CA  . LEU A 1 268 ? -15.057 -4.070  -36.047 1.00 24.62  ? 268 LEU A CA  1 
ATOM   2338 C  C   . LEU A 1 268 ? -15.232 -3.115  -37.235 1.00 24.07  ? 268 LEU A C   1 
ATOM   2339 O  O   . LEU A 1 268 ? -14.947 -1.911  -37.093 1.00 23.71  ? 268 LEU A O   1 
ATOM   2340 C  CB  . LEU A 1 268 ? -13.826 -4.959  -36.233 1.00 23.62  ? 268 LEU A CB  1 
ATOM   2341 C  CG  . LEU A 1 268 ? -12.495 -4.217  -36.376 1.00 23.43  ? 268 LEU A CG  1 
ATOM   2342 C  CD1 . LEU A 1 268 ? -12.324 -3.153  -35.295 1.00 22.28  ? 268 LEU A CD1 1 
ATOM   2343 C  CD2 . LEU A 1 268 ? -11.349 -5.216  -36.311 1.00 24.72  ? 268 LEU A CD2 1 
ATOM   2344 N  N   . LYS A 1 269 ? -15.721 -3.587  -38.384 1.00 26.95  ? 269 LYS A N   1 
ATOM   2345 C  CA  . LYS A 1 269 ? -15.828 -2.690  -39.569 1.00 26.53  ? 269 LYS A CA  1 
ATOM   2346 C  C   . LYS A 1 269 ? -16.735 -1.514  -39.221 1.00 25.78  ? 269 LYS A C   1 
ATOM   2347 O  O   . LYS A 1 269 ? -16.451 -0.381  -39.655 1.00 26.65  ? 269 LYS A O   1 
ATOM   2348 C  CB  . LYS A 1 269 ? -16.386 -3.419  -40.790 1.00 32.06  ? 269 LYS A CB  1 
ATOM   2349 C  CG  . LYS A 1 269 ? -15.535 -4.567  -41.293 1.00 38.04  ? 269 LYS A CG  1 
ATOM   2350 C  CD  . LYS A 1 269 ? -16.295 -5.588  -42.148 1.00 40.13  ? 269 LYS A CD  1 
ATOM   2351 C  CE  . LYS A 1 269 ? -16.695 -5.051  -43.501 1.00 36.72  ? 269 LYS A CE  1 
ATOM   2352 N  NZ  . LYS A 1 269 ? -17.513 -6.054  -44.212 1.00 36.06  ? 269 LYS A NZ  1 
ATOM   2353 N  N   . GLU A 1 270 ? -17.796 -1.781  -38.459 1.00 27.54  ? 270 GLU A N   1 
ATOM   2354 C  CA  . GLU A 1 270 ? -18.803 -0.751  -38.076 1.00 29.69  ? 270 GLU A CA  1 
ATOM   2355 C  C   . GLU A 1 270 ? -18.174 0.246   -37.098 1.00 26.63  ? 270 GLU A C   1 
ATOM   2356 O  O   . GLU A 1 270 ? -18.401 1.449   -37.235 1.00 24.47  ? 270 GLU A O   1 
ATOM   2357 C  CB  . GLU A 1 270 ? -20.047 -1.417  -37.503 1.00 28.38  ? 270 GLU A CB  1 
ATOM   2358 C  CG  . GLU A 1 270 ? -21.130 -0.425  -37.143 1.00 32.57  ? 270 GLU A CG  1 
ATOM   2359 C  CD  . GLU A 1 270 ? -22.504 -1.072  -37.047 1.00 33.93  ? 270 GLU A CD  1 
ATOM   2360 O  OE1 . GLU A 1 270 ? -23.116 -1.353  -38.111 1.00 30.48  ? 270 GLU A OE1 1 
ATOM   2361 O  OE2 . GLU A 1 270 ? -22.948 -1.289  -35.922 1.00 31.73  ? 270 GLU A OE2 1 
ATOM   2362 N  N   . LEU A 1 271 ? -17.358 -0.241  -36.169 1.00 28.91  ? 271 LEU A N   1 
ATOM   2363 C  CA  . LEU A 1 271 ? -16.683 0.621   -35.174 1.00 26.25  ? 271 LEU A CA  1 
ATOM   2364 C  C   . LEU A 1 271 ? -15.728 1.550   -35.911 1.00 28.28  ? 271 LEU A C   1 
ATOM   2365 O  O   . LEU A 1 271 ? -15.674 2.729   -35.534 1.00 25.88  ? 271 LEU A O   1 
ATOM   2366 C  CB  . LEU A 1 271 ? -15.950 -0.265  -34.169 1.00 30.44  ? 271 LEU A CB  1 
ATOM   2367 C  CG  . LEU A 1 271 ? -16.798 -0.776  -33.015 1.00 29.27  ? 271 LEU A CG  1 
ATOM   2368 C  CD1 . LEU A 1 271 ? -16.142 -1.970  -32.325 1.00 29.40  ? 271 LEU A CD1 1 
ATOM   2369 C  CD2 . LEU A 1 271 ? -17.092 0.351   -32.042 1.00 29.18  ? 271 LEU A CD2 1 
ATOM   2370 N  N   . LEU A 1 272 ? -15.041 1.059   -36.954 1.00 24.74  ? 272 LEU A N   1 
ATOM   2371 C  CA  . LEU A 1 272 ? -14.064 1.907   -37.703 1.00 27.75  ? 272 LEU A CA  1 
ATOM   2372 C  C   . LEU A 1 272 ? -14.832 2.999   -38.440 1.00 27.76  ? 272 LEU A C   1 
ATOM   2373 O  O   . LEU A 1 272 ? -14.374 4.154   -38.483 1.00 27.05  ? 272 LEU A O   1 
ATOM   2374 C  CB  . LEU A 1 272 ? -13.226 1.045   -38.652 1.00 26.96  ? 272 LEU A CB  1 
ATOM   2375 C  CG  . LEU A 1 272 ? -12.247 0.111   -37.949 1.00 29.18  ? 272 LEU A CG  1 
ATOM   2376 C  CD1 . LEU A 1 272 ? -11.656 -0.903  -38.913 1.00 29.37  ? 272 LEU A CD1 1 
ATOM   2377 C  CD2 . LEU A 1 272 ? -11.151 0.905   -37.256 1.00 31.65  ? 272 LEU A CD2 1 
ATOM   2378 N  N   . GLN A 1 273 ? -16.000 2.651   -38.973 1.00 28.21  ? 273 GLN A N   1 
ATOM   2379 C  CA  . GLN A 1 273 ? -16.885 3.597   -39.711 1.00 26.74  ? 273 GLN A CA  1 
ATOM   2380 C  C   . GLN A 1 273 ? -17.473 4.666   -38.778 1.00 25.20  ? 273 GLN A C   1 
ATOM   2381 O  O   . GLN A 1 273 ? -17.569 5.826   -39.208 1.00 25.67  ? 273 GLN A O   1 
ATOM   2382 C  CB  . GLN A 1 273 ? -17.964 2.762   -40.401 1.00 26.33  ? 273 GLN A CB  1 
ATOM   2383 C  CG  . GLN A 1 273 ? -19.130 3.553   -40.968 1.00 26.68  ? 273 GLN A CG  1 
ATOM   2384 C  CD  . GLN A 1 273 ? -20.209 2.589   -41.410 1.00 28.44  ? 273 GLN A CD  1 
ATOM   2385 O  OE1 . GLN A 1 273 ? -21.115 2.225   -40.649 1.00 30.30  ? 273 GLN A OE1 1 
ATOM   2386 N  NE2 . GLN A 1 273 ? -20.069 2.110   -42.634 1.00 24.83  ? 273 GLN A NE2 1 
ATOM   2387 N  N   . ASN A 1 274 ? -17.914 4.290   -37.577 1.00 27.13  ? 274 ASN A N   1 
ATOM   2388 C  CA  . ASN A 1 274 ? -18.758 5.137   -36.691 1.00 29.56  ? 274 ASN A CA  1 
ATOM   2389 C  C   . ASN A 1 274 ? -17.930 5.735   -35.548 1.00 34.66  ? 274 ASN A C   1 
ATOM   2390 O  O   . ASN A 1 274 ? -18.366 6.774   -35.019 1.00 33.15  ? 274 ASN A O   1 
ATOM   2391 C  CB  . ASN A 1 274 ? -19.931 4.369   -36.058 1.00 28.99  ? 274 ASN A CB  1 
ATOM   2392 C  CG  . ASN A 1 274 ? -20.891 3.822   -37.094 1.00 25.71  ? 274 ASN A CG  1 
ATOM   2393 O  OD1 . ASN A 1 274 ? -20.775 4.157   -38.262 1.00 26.78  ? 274 ASN A OD1 1 
ATOM   2394 N  ND2 . ASN A 1 274 ? -21.831 2.985   -36.692 1.00 23.08  ? 274 ASN A ND2 1 
ATOM   2395 N  N   . GLY A 1 275 ? -16.812 5.119   -35.158 1.00 32.26  ? 275 GLY A N   1 
ATOM   2396 C  CA  . GLY A 1 275 ? -16.154 5.469   -33.886 1.00 35.23  ? 275 GLY A CA  1 
ATOM   2397 C  C   . GLY A 1 275 ? -17.008 4.971   -32.734 1.00 36.06  ? 275 GLY A C   1 
ATOM   2398 O  O   . GLY A 1 275 ? -17.783 4.034   -32.964 1.00 33.66  ? 275 GLY A O   1 
ATOM   2399 N  N   . MET A 1 276 ? -16.898 5.539   -31.534 1.00 37.46  ? 276 MET A N   1 
ATOM   2400 C  CA  . MET A 1 276 ? -17.542 4.933   -30.329 1.00 41.67  ? 276 MET A CA  1 
ATOM   2401 C  C   . MET A 1 276 ? -18.708 5.776   -29.795 1.00 40.91  ? 276 MET A C   1 
ATOM   2402 O  O   . MET A 1 276 ? -19.400 5.307   -28.856 1.00 39.84  ? 276 MET A O   1 
ATOM   2403 C  CB  . MET A 1 276 ? -16.495 4.735   -29.236 1.00 46.60  ? 276 MET A CB  1 
ATOM   2404 C  CG  . MET A 1 276 ? -15.519 3.657   -29.609 1.00 46.25  ? 276 MET A CG  1 
ATOM   2405 S  SD  . MET A 1 276 ? -14.817 2.998   -28.162 1.00 56.05  ? 276 MET A SD  1 
ATOM   2406 C  CE  . MET A 1 276 ? -13.655 1.843   -28.885 1.00 55.45  ? 276 MET A CE  1 
ATOM   2407 N  N   . ASN A 1 277 ? -18.927 6.963   -30.355 1.00 44.78  ? 277 ASN A N   1 
ATOM   2408 C  CA  . ASN A 1 277 ? -20.103 7.813   -30.032 1.00 47.31  ? 277 ASN A CA  1 
ATOM   2409 C  C   . ASN A 1 277 ? -20.145 8.047   -28.515 1.00 45.28  ? 277 ASN A C   1 
ATOM   2410 O  O   . ASN A 1 277 ? -21.160 7.718   -27.905 1.00 45.50  ? 277 ASN A O   1 
ATOM   2411 C  CB  . ASN A 1 277 ? -21.384 7.161   -30.560 1.00 49.84  ? 277 ASN A CB  1 
ATOM   2412 C  CG  . ASN A 1 277 ? -22.523 8.140   -30.762 1.00 60.51  ? 277 ASN A CG  1 
ATOM   2413 O  OD1 . ASN A 1 277 ? -22.396 9.325   -30.456 1.00 61.07  ? 277 ASN A OD1 1 
ATOM   2414 N  ND2 . ASN A 1 277 ? -23.644 7.655   -31.281 1.00 62.36  ? 277 ASN A ND2 1 
ATOM   2415 N  N   . GLY A 1 278 ? -19.057 8.555   -27.927 1.00 47.97  ? 278 GLY A N   1 
ATOM   2416 C  CA  . GLY A 1 278 ? -18.980 8.909   -26.493 1.00 45.07  ? 278 GLY A CA  1 
ATOM   2417 C  C   . GLY A 1 278 ? -18.972 7.696   -25.568 1.00 47.17  ? 278 GLY A C   1 
ATOM   2418 O  O   . GLY A 1 278 ? -18.939 7.887   -24.356 1.00 49.80  ? 278 GLY A O   1 
ATOM   2419 N  N   . ARG A 1 279 ? -18.998 6.470   -26.083 1.00 42.81  ? 279 ARG A N   1 
ATOM   2420 C  CA  . ARG A 1 279 ? -18.936 5.263   -25.222 1.00 44.07  ? 279 ARG A CA  1 
ATOM   2421 C  C   . ARG A 1 279 ? -17.477 4.813   -25.108 1.00 39.51  ? 279 ARG A C   1 
ATOM   2422 O  O   . ARG A 1 279 ? -16.585 5.453   -25.673 1.00 40.37  ? 279 ARG A O   1 
ATOM   2423 C  CB  . ARG A 1 279 ? -19.850 4.154   -25.747 1.00 43.30  ? 279 ARG A CB  1 
ATOM   2424 C  CG  . ARG A 1 279 ? -21.322 4.438   -25.489 1.00 55.04  ? 279 ARG A CG  1 
ATOM   2425 C  CD  . ARG A 1 279 ? -22.285 3.599   -26.301 1.00 58.20  ? 279 ARG A CD  1 
ATOM   2426 N  NE  . ARG A 1 279 ? -22.038 3.803   -27.720 1.00 62.59  ? 279 ARG A NE  1 
ATOM   2427 C  CZ  . ARG A 1 279 ? -22.964 3.790   -28.673 1.00 67.83  ? 279 ARG A CZ  1 
ATOM   2428 N  NH1 . ARG A 1 279 ? -24.238 3.601   -28.368 1.00 67.86  ? 279 ARG A NH1 1 
ATOM   2429 N  NH2 . ARG A 1 279 ? -22.605 3.982   -29.934 1.00 59.61  ? 279 ARG A NH2 1 
ATOM   2430 N  N   . THR A 1 280 ? -17.257 3.773   -24.322 1.00 43.29  ? 280 THR A N   1 
ATOM   2431 C  CA  . THR A 1 280 ? -15.935 3.154   -24.091 1.00 44.52  ? 280 THR A CA  1 
ATOM   2432 C  C   . THR A 1 280 ? -16.156 1.654   -24.161 1.00 43.41  ? 280 THR A C   1 
ATOM   2433 O  O   . THR A 1 280 ? -17.326 1.230   -24.048 1.00 47.80  ? 280 THR A O   1 
ATOM   2434 C  CB  . THR A 1 280 ? -15.325 3.607   -22.757 1.00 44.76  ? 280 THR A CB  1 
ATOM   2435 O  OG1 . THR A 1 280 ? -16.239 3.236   -21.732 1.00 47.79  ? 280 THR A OG1 1 
ATOM   2436 C  CG2 . THR A 1 280 ? -15.051 5.092   -22.691 1.00 42.64  ? 280 THR A CG2 1 
ATOM   2437 N  N   . ILE A 1 281 ? -15.091 0.907   -24.433 1.00 45.84  ? 281 ILE A N   1 
ATOM   2438 C  CA  . ILE A 1 281 ? -15.074 -0.581  -24.361 1.00 41.72  ? 281 ILE A CA  1 
ATOM   2439 C  C   . ILE A 1 281 ? -13.968 -0.937  -23.370 1.00 40.13  ? 281 ILE A C   1 
ATOM   2440 O  O   . ILE A 1 281 ? -12.883 -0.332  -23.465 1.00 41.67  ? 281 ILE A O   1 
ATOM   2441 C  CB  . ILE A 1 281 ? -14.891 -1.217  -25.759 1.00 39.31  ? 281 ILE A CB  1 
ATOM   2442 C  CG1 . ILE A 1 281 ? -15.957 -0.727  -26.737 1.00 34.66  ? 281 ILE A CG1 1 
ATOM   2443 C  CG2 . ILE A 1 281 ? -14.887 -2.738  -25.662 1.00 40.35  ? 281 ILE A CG2 1 
ATOM   2444 C  CD1 . ILE A 1 281 ? -15.833 -1.300  -28.137 1.00 34.03  ? 281 ILE A CD1 1 
ATOM   2445 N  N   . LEU A 1 282 ? -14.291 -1.774  -22.380 1.00 43.61  ? 282 LEU A N   1 
ATOM   2446 C  CA  . LEU A 1 282 ? -13.382 -2.169  -21.274 1.00 40.95  ? 282 LEU A CA  1 
ATOM   2447 C  C   . LEU A 1 282 ? -12.541 -0.965  -20.821 1.00 41.61  ? 282 LEU A C   1 
ATOM   2448 O  O   . LEU A 1 282 ? -11.334 -1.144  -20.624 1.00 42.54  ? 282 LEU A O   1 
ATOM   2449 C  CB  . LEU A 1 282 ? -12.481 -3.302  -21.769 1.00 39.60  ? 282 LEU A CB  1 
ATOM   2450 C  CG  . LEU A 1 282 ? -13.201 -4.587  -22.171 1.00 38.28  ? 282 LEU A CG  1 
ATOM   2451 C  CD1 . LEU A 1 282 ? -12.276 -5.493  -22.939 1.00 36.67  ? 282 LEU A CD1 1 
ATOM   2452 C  CD2 . LEU A 1 282 ? -13.765 -5.324  -20.957 1.00 39.34  ? 282 LEU A CD2 1 
ATOM   2453 N  N   . GLY A 1 283 ? -13.131 0.226   -20.686 1.00 43.56  ? 283 GLY A N   1 
ATOM   2454 C  CA  . GLY A 1 283 ? -12.457 1.393   -20.078 1.00 41.25  ? 283 GLY A CA  1 
ATOM   2455 C  C   . GLY A 1 283 ? -11.666 2.216   -21.077 1.00 44.14  ? 283 GLY A C   1 
ATOM   2456 O  O   . GLY A 1 283 ? -10.974 3.171   -20.664 1.00 48.47  ? 283 GLY A O   1 
ATOM   2457 N  N   . SER A 1 284 ? -11.744 1.892   -22.364 1.00 42.77  ? 284 SER A N   1 
ATOM   2458 C  CA  . SER A 1 284 ? -10.971 2.619   -23.400 1.00 41.97  ? 284 SER A CA  1 
ATOM   2459 C  C   . SER A 1 284 ? -11.927 3.271   -24.402 1.00 37.28  ? 284 SER A C   1 
ATOM   2460 O  O   . SER A 1 284 ? -12.952 2.655   -24.721 1.00 38.18  ? 284 SER A O   1 
ATOM   2461 C  CB  . SER A 1 284 ? -9.992  1.712   -24.081 1.00 39.11  ? 284 SER A CB  1 
ATOM   2462 O  OG  . SER A 1 284 ? -9.197  2.462   -24.988 1.00 42.34  ? 284 SER A OG  1 
ATOM   2463 N  N   . ALA A 1 285 ? -11.562 4.450   -24.901 1.00 34.44  ? 285 ALA A N   1 
ATOM   2464 C  CA  . ALA A 1 285 ? -12.261 5.148   -26.005 1.00 35.99  ? 285 ALA A CA  1 
ATOM   2465 C  C   . ALA A 1 285 ? -11.521 4.940   -27.331 1.00 38.27  ? 285 ALA A C   1 
ATOM   2466 O  O   . ALA A 1 285 ? -11.857 5.667   -28.294 1.00 38.19  ? 285 ALA A O   1 
ATOM   2467 C  CB  . ALA A 1 285 ? -12.388 6.609   -25.665 1.00 38.48  ? 285 ALA A CB  1 
ATOM   2468 N  N   . LEU A 1 286 ? -10.535 4.021   -27.374 1.00 39.57  ? 286 LEU A N   1 
ATOM   2469 C  CA  . LEU A 1 286 ? -9.835  3.573   -28.614 1.00 38.49  ? 286 LEU A CA  1 
ATOM   2470 C  C   . LEU A 1 286 ? -9.956  2.054   -28.712 1.00 34.55  ? 286 LEU A C   1 
ATOM   2471 O  O   . LEU A 1 286 ? -10.162 1.406   -27.678 1.00 32.29  ? 286 LEU A O   1 
ATOM   2472 C  CB  . LEU A 1 286 ? -8.356  3.974   -28.570 1.00 44.74  ? 286 LEU A CB  1 
ATOM   2473 C  CG  . LEU A 1 286 ? -8.046  5.446   -28.844 1.00 50.41  ? 286 LEU A CG  1 
ATOM   2474 C  CD1 . LEU A 1 286 ? -6.540  5.661   -28.950 1.00 50.06  ? 286 LEU A CD1 1 
ATOM   2475 C  CD2 . LEU A 1 286 ? -8.749  5.952   -30.106 1.00 53.29  ? 286 LEU A CD2 1 
ATOM   2476 N  N   . LEU A 1 287 ? -9.798  1.492   -29.912 1.00 29.81  ? 287 LEU A N   1 
ATOM   2477 C  CA  . LEU A 1 287 ? -9.729  0.014   -30.070 1.00 28.59  ? 287 LEU A CA  1 
ATOM   2478 C  C   . LEU A 1 287 ? -8.309  -0.469  -29.681 1.00 27.97  ? 287 LEU A C   1 
ATOM   2479 O  O   . LEU A 1 287 ? -7.359  -0.071  -30.338 1.00 27.31  ? 287 LEU A O   1 
ATOM   2480 C  CB  . LEU A 1 287 ? -10.120 -0.310  -31.516 1.00 29.95  ? 287 LEU A CB  1 
ATOM   2481 C  CG  . LEU A 1 287 ? -11.502 0.231   -31.920 1.00 29.96  ? 287 LEU A CG  1 
ATOM   2482 C  CD1 . LEU A 1 287 ? -11.723 0.146   -33.425 1.00 30.90  ? 287 LEU A CD1 1 
ATOM   2483 C  CD2 . LEU A 1 287 ? -12.601 -0.501  -31.170 1.00 31.43  ? 287 LEU A CD2 1 
ATOM   2484 N  N   . GLU A 1 288 ? -8.190  -1.301  -28.652 1.00 28.68  ? 288 GLU A N   1 
ATOM   2485 C  CA  . GLU A 1 288 ? -6.900  -1.720  -28.021 1.00 32.73  ? 288 GLU A CA  1 
ATOM   2486 C  C   . GLU A 1 288 ? -6.315  -2.914  -28.771 1.00 29.62  ? 288 GLU A C   1 
ATOM   2487 O  O   . GLU A 1 288 ? -7.035  -3.924  -28.874 1.00 27.62  ? 288 GLU A O   1 
ATOM   2488 C  CB  . GLU A 1 288 ? -7.139  -2.131  -26.566 1.00 38.21  ? 288 GLU A CB  1 
ATOM   2489 C  CG  . GLU A 1 288 ? -7.550  -0.970  -25.677 1.00 48.28  ? 288 GLU A CG  1 
ATOM   2490 C  CD  . GLU A 1 288 ? -6.441  0.039   -25.418 1.00 57.71  ? 288 GLU A CD  1 
ATOM   2491 O  OE1 . GLU A 1 288 ? -5.246  -0.370  -25.429 1.00 59.93  ? 288 GLU A OE1 1 
ATOM   2492 O  OE2 . GLU A 1 288 ? -6.771  1.238   -25.233 1.00 65.40  ? 288 GLU A OE2 1 
ATOM   2493 N  N   . ASP A 1 289 ? -5.050  -2.835  -29.207 1.00 28.10  ? 289 ASP A N   1 
ATOM   2494 C  CA  . ASP A 1 289 ? -4.420  -3.915  -30.017 1.00 29.64  ? 289 ASP A CA  1 
ATOM   2495 C  C   . ASP A 1 289 ? -3.208  -4.542  -29.316 1.00 27.54  ? 289 ASP A C   1 
ATOM   2496 O  O   . ASP A 1 289 ? -2.527  -5.306  -30.017 1.00 27.33  ? 289 ASP A O   1 
ATOM   2497 C  CB  . ASP A 1 289 ? -4.087  -3.423  -31.426 1.00 27.25  ? 289 ASP A CB  1 
ATOM   2498 C  CG  . ASP A 1 289 ? -2.861  -2.537  -31.528 1.00 28.71  ? 289 ASP A CG  1 
ATOM   2499 O  OD1 . ASP A 1 289 ? -2.378  -2.055  -30.470 1.00 26.55  ? 289 ASP A OD1 1 
ATOM   2500 O  OD2 . ASP A 1 289 ? -2.439  -2.286  -32.663 1.00 23.83  ? 289 ASP A OD2 1 
ATOM   2501 N  N   . GLU A 1 290 ? -2.997  -4.312  -28.006 1.00 25.53  ? 290 GLU A N   1 
ATOM   2502 C  CA  . GLU A 1 290 ? -1.856  -4.889  -27.231 1.00 27.44  ? 290 GLU A CA  1 
ATOM   2503 C  C   . GLU A 1 290 ? -2.331  -5.985  -26.262 1.00 28.08  ? 290 GLU A C   1 
ATOM   2504 O  O   . GLU A 1 290 ? -1.581  -6.322  -25.329 1.00 28.86  ? 290 GLU A O   1 
ATOM   2505 C  CB  . GLU A 1 290 ? -1.013  -3.759  -26.606 1.00 28.64  ? 290 GLU A CB  1 
ATOM   2506 C  CG  . GLU A 1 290 ? -0.309  -2.915  -27.674 1.00 28.42  ? 290 GLU A CG  1 
ATOM   2507 C  CD  . GLU A 1 290 ? 0.998   -2.185  -27.350 1.00 30.75  ? 290 GLU A CD  1 
ATOM   2508 O  OE1 . GLU A 1 290 ? 1.350   -2.095  -26.178 1.00 27.82  ? 290 GLU A OE1 1 
ATOM   2509 O  OE2 . GLU A 1 290 ? 1.639   -1.632  -28.318 1.00 32.53  ? 290 GLU A OE2 1 
ATOM   2510 N  N   . PHE A 1 291 ? -3.478  -6.631  -26.514 1.00 29.55  ? 291 PHE A N   1 
ATOM   2511 C  CA  . PHE A 1 291 ? -3.861  -7.917  -25.859 1.00 27.20  ? 291 PHE A CA  1 
ATOM   2512 C  C   . PHE A 1 291 ? -4.009  -9.025  -26.906 1.00 28.05  ? 291 PHE A C   1 
ATOM   2513 O  O   . PHE A 1 291 ? -4.819  -8.854  -27.812 1.00 31.67  ? 291 PHE A O   1 
ATOM   2514 C  CB  . PHE A 1 291 ? -5.207  -7.825  -25.141 1.00 31.54  ? 291 PHE A CB  1 
ATOM   2515 C  CG  . PHE A 1 291 ? -5.249  -6.774  -24.075 1.00 33.78  ? 291 PHE A CG  1 
ATOM   2516 C  CD1 . PHE A 1 291 ? -4.779  -7.062  -22.803 1.00 34.55  ? 291 PHE A CD1 1 
ATOM   2517 C  CD2 . PHE A 1 291 ? -5.712  -5.498  -24.354 1.00 35.38  ? 291 PHE A CD2 1 
ATOM   2518 C  CE1 . PHE A 1 291 ? -4.817  -6.088  -21.817 1.00 36.77  ? 291 PHE A CE1 1 
ATOM   2519 C  CE2 . PHE A 1 291 ? -5.719  -4.519  -23.372 1.00 37.08  ? 291 PHE A CE2 1 
ATOM   2520 C  CZ  . PHE A 1 291 ? -5.263  -4.819  -22.110 1.00 38.27  ? 291 PHE A CZ  1 
ATOM   2521 N  N   . THR A 1 292 ? -3.280  -10.124 -26.759 1.00 26.44  ? 292 THR A N   1 
ATOM   2522 C  CA  . THR A 1 292 ? -3.314  -11.289 -27.678 1.00 25.46  ? 292 THR A CA  1 
ATOM   2523 C  C   . THR A 1 292 ? -4.488  -12.194 -27.323 1.00 27.74  ? 292 THR A C   1 
ATOM   2524 O  O   . THR A 1 292 ? -4.997  -12.145 -26.202 1.00 29.54  ? 292 THR A O   1 
ATOM   2525 C  CB  . THR A 1 292 ? -2.045  -12.137 -27.593 1.00 25.22  ? 292 THR A CB  1 
ATOM   2526 O  OG1 . THR A 1 292 ? -1.976  -12.630 -26.258 1.00 28.23  ? 292 THR A OG1 1 
ATOM   2527 C  CG2 . THR A 1 292 ? -0.783  -11.394 -27.957 1.00 26.93  ? 292 THR A CG2 1 
ATOM   2528 N  N   . PRO A 1 293 ? -4.940  -13.065 -28.263 1.00 28.54  ? 293 PRO A N   1 
ATOM   2529 C  CA  . PRO A 1 293 ? -5.954  -14.080 -27.956 1.00 28.45  ? 293 PRO A CA  1 
ATOM   2530 C  C   . PRO A 1 293 ? -5.588  -14.906 -26.713 1.00 30.04  ? 293 PRO A C   1 
ATOM   2531 O  O   . PRO A 1 293 ? -6.429  -15.150 -25.874 1.00 28.88  ? 293 PRO A O   1 
ATOM   2532 C  CB  . PRO A 1 293 ? -5.989  -14.900 -29.253 1.00 29.11  ? 293 PRO A CB  1 
ATOM   2533 C  CG  . PRO A 1 293 ? -5.680  -13.860 -30.325 1.00 30.44  ? 293 PRO A CG  1 
ATOM   2534 C  CD  . PRO A 1 293 ? -4.586  -13.027 -29.697 1.00 28.54  ? 293 PRO A CD  1 
ATOM   2535 N  N   . PHE A 1 294 ? -4.314  -15.249 -26.567 1.00 33.30  ? 294 PHE A N   1 
ATOM   2536 C  CA  . PHE A 1 294 ? -3.800  -16.035 -25.420 1.00 35.73  ? 294 PHE A CA  1 
ATOM   2537 C  C   . PHE A 1 294 ? -3.939  -15.206 -24.125 1.00 35.34  ? 294 PHE A C   1 
ATOM   2538 O  O   . PHE A 1 294 ? -4.429  -15.751 -23.134 1.00 41.99  ? 294 PHE A O   1 
ATOM   2539 C  CB  . PHE A 1 294 ? -2.386  -16.509 -25.763 1.00 39.23  ? 294 PHE A CB  1 
ATOM   2540 C  CG  . PHE A 1 294 ? -1.784  -17.504 -24.797 1.00 46.13  ? 294 PHE A CG  1 
ATOM   2541 C  CD1 . PHE A 1 294 ? -1.353  -17.108 -23.533 1.00 47.47  ? 294 PHE A CD1 1 
ATOM   2542 C  CD2 . PHE A 1 294 ? -1.601  -18.832 -25.168 1.00 47.85  ? 294 PHE A CD2 1 
ATOM   2543 C  CE1 . PHE A 1 294 ? -0.787  -18.022 -22.653 1.00 50.64  ? 294 PHE A CE1 1 
ATOM   2544 C  CE2 . PHE A 1 294 ? -1.029  -19.744 -24.288 1.00 48.32  ? 294 PHE A CE2 1 
ATOM   2545 C  CZ  . PHE A 1 294 ? -0.628  -19.341 -23.032 1.00 49.40  ? 294 PHE A CZ  1 
ATOM   2546 N  N   . ASP A 1 295 ? -3.545  -13.930 -24.135 1.00 34.71  ? 295 ASP A N   1 
ATOM   2547 C  CA  . ASP A 1 295 ? -3.638  -13.005 -22.969 1.00 35.69  ? 295 ASP A CA  1 
ATOM   2548 C  C   . ASP A 1 295 ? -5.111  -12.884 -22.555 1.00 43.14  ? 295 ASP A C   1 
ATOM   2549 O  O   . ASP A 1 295 ? -5.387  -12.823 -21.336 1.00 44.28  ? 295 ASP A O   1 
ATOM   2550 C  CB  . ASP A 1 295 ? -3.174  -11.577 -23.282 1.00 35.91  ? 295 ASP A CB  1 
ATOM   2551 C  CG  . ASP A 1 295 ? -1.714  -11.402 -23.679 1.00 36.10  ? 295 ASP A CG  1 
ATOM   2552 O  OD1 . ASP A 1 295 ? -0.933  -12.339 -23.428 1.00 33.91  ? 295 ASP A OD1 1 
ATOM   2553 O  OD2 . ASP A 1 295 ? -1.372  -10.309 -24.226 1.00 27.43  ? 295 ASP A OD2 1 
ATOM   2554 N  N   . VAL A 1 296 ? -6.026  -12.804 -23.529 1.00 39.44  ? 296 VAL A N   1 
ATOM   2555 C  CA  . VAL A 1 296 ? -7.472  -12.593 -23.237 1.00 38.99  ? 296 VAL A CA  1 
ATOM   2556 C  C   . VAL A 1 296 ? -7.969  -13.788 -22.421 1.00 45.63  ? 296 VAL A C   1 
ATOM   2557 O  O   . VAL A 1 296 ? -8.698  -13.550 -21.448 1.00 45.94  ? 296 VAL A O   1 
ATOM   2558 C  CB  . VAL A 1 296 ? -8.310  -12.317 -24.498 1.00 37.09  ? 296 VAL A CB  1 
ATOM   2559 C  CG1 . VAL A 1 296 ? -9.782  -12.662 -24.316 1.00 37.53  ? 296 VAL A CG1 1 
ATOM   2560 C  CG2 . VAL A 1 296 ? -8.181  -10.861 -24.906 1.00 35.50  ? 296 VAL A CG2 1 
ATOM   2561 N  N   . VAL A 1 297 ? -7.534  -15.014 -22.710 1.00 50.94  ? 297 VAL A N   1 
ATOM   2562 C  CA  . VAL A 1 297 ? -7.971  -16.180 -21.881 1.00 53.59  ? 297 VAL A CA  1 
ATOM   2563 C  C   . VAL A 1 297 ? -7.221  -16.222 -20.542 1.00 55.23  ? 297 VAL A C   1 
ATOM   2564 O  O   . VAL A 1 297 ? -7.876  -16.556 -19.547 1.00 58.31  ? 297 VAL A O   1 
ATOM   2565 C  CB  . VAL A 1 297 ? -7.861  -17.507 -22.634 1.00 52.17  ? 297 VAL A CB  1 
ATOM   2566 C  CG1 . VAL A 1 297 ? -8.508  -18.607 -21.816 1.00 53.37  ? 297 VAL A CG1 1 
ATOM   2567 C  CG2 . VAL A 1 297 ? -8.493  -17.407 -24.012 1.00 49.67  ? 297 VAL A CG2 1 
ATOM   2568 N  N   . ARG A 1 298 ? -5.920  -15.898 -20.501 1.00 63.09  ? 298 ARG A N   1 
ATOM   2569 C  CA  . ARG A 1 298 ? -5.118  -15.843 -19.236 1.00 62.71  ? 298 ARG A CA  1 
ATOM   2570 C  C   . ARG A 1 298 ? -5.851  -14.944 -18.225 1.00 64.50  ? 298 ARG A C   1 
ATOM   2571 O  O   . ARG A 1 298 ? -5.824  -15.283 -17.030 1.00 69.00  ? 298 ARG A O   1 
ATOM   2572 C  CB  . ARG A 1 298 ? -3.669  -15.390 -19.502 1.00 65.28  ? 298 ARG A CB  1 
ATOM   2573 C  CG  . ARG A 1 298 ? -2.880  -14.855 -18.303 1.00 65.45  ? 298 ARG A CG  1 
ATOM   2574 C  CD  . ARG A 1 298 ? -1.738  -13.913 -18.710 1.00 63.80  ? 298 ARG A CD  1 
ATOM   2575 N  NE  . ARG A 1 298 ? -1.068  -13.167 -17.631 1.00 55.96  ? 298 ARG A NE  1 
ATOM   2576 C  CZ  . ARG A 1 298 ? -0.434  -11.999 -17.773 1.00 44.08  ? 298 ARG A CZ  1 
ATOM   2577 N  NH1 . ARG A 1 298 ? -0.355  -11.411 -18.946 1.00 44.09  ? 298 ARG A NH1 1 
ATOM   2578 N  NH2 . ARG A 1 298 ? 0.148   -11.428 -16.737 1.00 47.02  ? 298 ARG A NH2 1 
ATOM   2579 N  N   . GLN A 1 299 ? -6.485  -13.853 -18.674 1.00 62.58  ? 299 GLN A N   1 
ATOM   2580 C  CA  . GLN A 1 299 ? -7.092  -12.825 -17.780 1.00 64.72  ? 299 GLN A CA  1 
ATOM   2581 C  C   . GLN A 1 299 ? -8.620  -13.023 -17.689 1.00 72.45  ? 299 GLN A C   1 
ATOM   2582 O  O   . GLN A 1 299 ? -9.198  -12.512 -16.707 1.00 87.12  ? 299 GLN A O   1 
ATOM   2583 C  CB  . GLN A 1 299 ? -6.657  -11.416 -18.216 1.00 59.51  ? 299 GLN A CB  1 
ATOM   2584 C  CG  . GLN A 1 299 ? -7.290  -10.308 -17.384 1.00 60.42  ? 299 GLN A CG  1 
ATOM   2585 C  CD  . GLN A 1 299 ? -6.600  -8.964  -17.434 1.00 63.19  ? 299 GLN A CD  1 
ATOM   2586 O  OE1 . GLN A 1 299 ? -7.042  -8.003  -16.805 1.00 58.29  ? 299 GLN A OE1 1 
ATOM   2587 N  NE2 . GLN A 1 299 ? -5.508  -8.873  -18.178 1.00 68.23  ? 299 GLN A NE2 1 
ATOM   2588 N  N   . CYS A 1 300 ? -9.256  -13.764 -18.613 1.00 73.80  ? 300 CYS A N   1 
ATOM   2589 C  CA  . CYS A 1 300 ? -10.719 -14.081 -18.592 1.00 75.07  ? 300 CYS A CA  1 
ATOM   2590 C  C   . CYS A 1 300 ? -10.941 -15.559 -18.240 1.00 85.89  ? 300 CYS A C   1 
ATOM   2591 O  O   . CYS A 1 300 ? -10.256 -16.058 -17.318 1.00 85.23  ? 300 CYS A O   1 
ATOM   2592 C  CB  . CYS A 1 300 ? -11.380 -13.754 -19.928 1.00 72.78  ? 300 CYS A CB  1 
ATOM   2593 S  SG  . CYS A 1 300 ? -11.159 -12.025 -20.418 1.00 73.10  ? 300 CYS A SG  1 
ATOM   2594 N  N   . SER A 1 301 ? -11.902 -16.211 -18.912 1.00 88.57  ? 301 SER A N   1 
ATOM   2595 C  CA  . SER A 1 301 ? -12.172 -17.667 -18.823 1.00 86.94  ? 301 SER A CA  1 
ATOM   2596 C  C   . SER A 1 301 ? -12.324 -18.212 -20.246 1.00 83.21  ? 301 SER A C   1 
ATOM   2597 O  O   . SER A 1 301 ? -11.591 -19.098 -20.661 1.00 78.68  ? 301 SER A O   1 
ATOM   2598 C  CB  . SER A 1 301 ? -13.398 -17.949 -17.975 1.00 90.53  ? 301 SER A CB  1 
ATOM   2599 O  OG  . SER A 1 301 ? -13.277 -19.190 -17.290 1.00 85.42  ? 301 SER A OG  1 
ATOM   2600 N  N   . SER B 1 1   ? 10.955  9.567   -25.919 1.00 34.97  ? 1   SER B N   1 
ATOM   2601 C  CA  . SER B 1 1   ? 11.442  8.573   -24.863 1.00 40.08  ? 1   SER B CA  1 
ATOM   2602 C  C   . SER B 1 1   ? 10.307  7.687   -24.338 1.00 34.74  ? 1   SER B C   1 
ATOM   2603 O  O   . SER B 1 1   ? 10.609  6.535   -24.018 1.00 32.17  ? 1   SER B O   1 
ATOM   2604 C  CB  . SER B 1 1   ? 12.176  9.258   -23.760 1.00 41.79  ? 1   SER B CB  1 
ATOM   2605 N  N   . GLY B 1 2   ? 9.064   8.186   -24.314 1.00 33.59  ? 2   GLY B N   1 
ATOM   2606 C  CA  . GLY B 1 2   ? 7.845   7.362   -24.227 1.00 31.09  ? 2   GLY B CA  1 
ATOM   2607 C  C   . GLY B 1 2   ? 7.210   7.441   -22.851 1.00 30.94  ? 2   GLY B C   1 
ATOM   2608 O  O   . GLY B 1 2   ? 7.851   7.882   -21.917 1.00 30.06  ? 2   GLY B O   1 
ATOM   2609 N  N   . PHE B 1 3   ? 5.967   7.017   -22.715 1.00 31.67  ? 3   PHE B N   1 
ATOM   2610 C  CA  . PHE B 1 3   ? 5.237   7.112   -21.429 1.00 31.50  ? 3   PHE B CA  1 
ATOM   2611 C  C   . PHE B 1 3   ? 4.266   5.957   -21.339 1.00 29.19  ? 3   PHE B C   1 
ATOM   2612 O  O   . PHE B 1 3   ? 3.451   5.785   -22.245 1.00 31.62  ? 3   PHE B O   1 
ATOM   2613 C  CB  . PHE B 1 3   ? 4.471   8.430   -21.290 1.00 33.41  ? 3   PHE B CB  1 
ATOM   2614 C  CG  . PHE B 1 3   ? 4.187   8.761   -19.853 1.00 31.01  ? 3   PHE B CG  1 
ATOM   2615 C  CD1 . PHE B 1 3   ? 5.227   9.076   -19.000 1.00 32.59  ? 3   PHE B CD1 1 
ATOM   2616 C  CD2 . PHE B 1 3   ? 2.904   8.675   -19.348 1.00 33.08  ? 3   PHE B CD2 1 
ATOM   2617 C  CE1 . PHE B 1 3   ? 4.981   9.352   -17.661 1.00 34.97  ? 3   PHE B CE1 1 
ATOM   2618 C  CE2 . PHE B 1 3   ? 2.658   8.968   -18.020 1.00 34.36  ? 3   PHE B CE2 1 
ATOM   2619 C  CZ  . PHE B 1 3   ? 3.701   9.294   -17.175 1.00 33.53  ? 3   PHE B CZ  1 
ATOM   2620 N  N   . ARG B 1 4   ? 4.403   5.178   -20.275 1.00 29.22  ? 4   ARG B N   1 
ATOM   2621 C  CA  . ARG B 1 4   ? 3.662   3.914   -20.082 1.00 27.95  ? 4   ARG B CA  1 
ATOM   2622 C  C   . ARG B 1 4   ? 3.177   3.853   -18.641 1.00 25.20  ? 4   ARG B C   1 
ATOM   2623 O  O   . ARG B 1 4   ? 3.853   4.416   -17.763 1.00 24.19  ? 4   ARG B O   1 
ATOM   2624 C  CB  . ARG B 1 4   ? 4.559   2.718   -20.400 1.00 31.14  ? 4   ARG B CB  1 
ATOM   2625 C  CG  . ARG B 1 4   ? 4.649   2.420   -21.884 1.00 35.39  ? 4   ARG B CG  1 
ATOM   2626 C  CD  . ARG B 1 4   ? 3.802   1.185   -22.185 1.00 41.44  ? 4   ARG B CD  1 
ATOM   2627 N  NE  . ARG B 1 4   ? 3.897   0.819   -23.586 1.00 42.26  ? 4   ARG B NE  1 
ATOM   2628 C  CZ  . ARG B 1 4   ? 2.978   0.129   -24.251 1.00 44.06  ? 4   ARG B CZ  1 
ATOM   2629 N  NH1 . ARG B 1 4   ? 1.904   -0.321  -23.623 1.00 46.36  ? 4   ARG B NH1 1 
ATOM   2630 N  NH2 . ARG B 1 4   ? 3.146   -0.118  -25.538 1.00 39.55  ? 4   ARG B NH2 1 
ATOM   2631 N  N   . LYS B 1 5   ? 2.039   3.207   -18.430 1.00 24.67  ? 5   LYS B N   1 
ATOM   2632 C  CA  . LYS B 1 5   ? 1.577   2.873   -17.080 1.00 29.39  ? 5   LYS B CA  1 
ATOM   2633 C  C   . LYS B 1 5   ? 2.531   1.796   -16.566 1.00 30.48  ? 5   LYS B C   1 
ATOM   2634 O  O   . LYS B 1 5   ? 2.552   0.692   -17.112 1.00 31.76  ? 5   LYS B O   1 
ATOM   2635 C  CB  . LYS B 1 5   ? 0.123   2.426   -17.082 1.00 28.94  ? 5   LYS B CB  1 
ATOM   2636 C  CG  . LYS B 1 5   ? -0.484  2.444   -15.694 1.00 33.85  ? 5   LYS B CG  1 
ATOM   2637 C  CD  . LYS B 1 5   ? -1.971  2.495   -15.727 1.00 38.41  ? 5   LYS B CD  1 
ATOM   2638 C  CE  . LYS B 1 5   ? -2.509  3.834   -16.175 1.00 38.51  ? 5   LYS B CE  1 
ATOM   2639 N  NZ  . LYS B 1 5   ? -3.972  3.729   -16.368 1.00 42.21  ? 5   LYS B NZ  1 
ATOM   2640 N  N   . MET B 1 6   ? 3.315   2.156   -15.570 1.00 28.51  ? 6   MET B N   1 
ATOM   2641 C  CA  . MET B 1 6   ? 4.469   1.366   -15.099 1.00 27.71  ? 6   MET B CA  1 
ATOM   2642 C  C   . MET B 1 6   ? 4.232   0.985   -13.644 1.00 22.24  ? 6   MET B C   1 
ATOM   2643 O  O   . MET B 1 6   ? 4.021   1.885   -12.835 1.00 21.62  ? 6   MET B O   1 
ATOM   2644 C  CB  . MET B 1 6   ? 5.698   2.263   -15.211 1.00 29.46  ? 6   MET B CB  1 
ATOM   2645 C  CG  . MET B 1 6   ? 6.981   1.573   -15.110 1.00 36.65  ? 6   MET B CG  1 
ATOM   2646 S  SD  . MET B 1 6   ? 8.281   2.775   -15.525 1.00 39.30  ? 6   MET B SD  1 
ATOM   2647 C  CE  . MET B 1 6   ? 8.162   2.695   -17.301 1.00 37.72  ? 6   MET B CE  1 
ATOM   2648 N  N   . ALA B 1 7   ? 4.353   -0.290  -13.310 1.00 21.70  ? 7   ALA B N   1 
ATOM   2649 C  CA  . ALA B 1 7   ? 4.349   -0.784  -11.912 1.00 21.15  ? 7   ALA B CA  1 
ATOM   2650 C  C   . ALA B 1 7   ? 5.768   -0.792  -11.322 1.00 23.02  ? 7   ALA B C   1 
ATOM   2651 O  O   . ALA B 1 7   ? 6.767   -0.911  -12.074 1.00 20.59  ? 7   ALA B O   1 
ATOM   2652 C  CB  . ALA B 1 7   ? 3.720   -2.165  -11.883 1.00 21.97  ? 7   ALA B CB  1 
ATOM   2653 N  N   . PHE B 1 8   ? 5.875   -0.740  -10.001 1.00 20.27  ? 8   PHE B N   1 
ATOM   2654 C  CA  . PHE B 1 8   ? 7.138   -1.047  -9.301  1.00 21.99  ? 8   PHE B CA  1 
ATOM   2655 C  C   . PHE B 1 8   ? 7.525   -2.485  -9.586  1.00 23.10  ? 8   PHE B C   1 
ATOM   2656 O  O   . PHE B 1 8   ? 6.666   -3.353  -9.768  1.00 24.05  ? 8   PHE B O   1 
ATOM   2657 C  CB  . PHE B 1 8   ? 7.030   -0.803  -7.800  1.00 23.72  ? 8   PHE B CB  1 
ATOM   2658 C  CG  . PHE B 1 8   ? 7.062   0.661   -7.489  1.00 23.52  ? 8   PHE B CG  1 
ATOM   2659 C  CD1 . PHE B 1 8   ? 8.249   1.369   -7.592  1.00 26.88  ? 8   PHE B CD1 1 
ATOM   2660 C  CD2 . PHE B 1 8   ? 5.909   1.333   -7.131  1.00 24.97  ? 8   PHE B CD2 1 
ATOM   2661 C  CE1 . PHE B 1 8   ? 8.295   2.730   -7.317  1.00 28.69  ? 8   PHE B CE1 1 
ATOM   2662 C  CE2 . PHE B 1 8   ? 5.955   2.693   -6.855  1.00 27.45  ? 8   PHE B CE2 1 
ATOM   2663 C  CZ  . PHE B 1 8   ? 7.141   3.392   -6.964  1.00 28.29  ? 8   PHE B CZ  1 
ATOM   2664 N  N   . PRO B 1 9   ? 8.843   -2.776  -9.652  1.00 22.66  ? 9   PRO B N   1 
ATOM   2665 C  CA  . PRO B 1 9   ? 9.294   -4.159  -9.755  1.00 22.15  ? 9   PRO B CA  1 
ATOM   2666 C  C   . PRO B 1 9   ? 8.732   -4.902  -8.521  1.00 22.82  ? 9   PRO B C   1 
ATOM   2667 O  O   . PRO B 1 9   ? 8.865   -4.386  -7.443  1.00 26.80  ? 9   PRO B O   1 
ATOM   2668 C  CB  . PRO B 1 9   ? 10.831  -4.051  -9.753  1.00 23.25  ? 9   PRO B CB  1 
ATOM   2669 C  CG  . PRO B 1 9   ? 11.158  -2.577  -10.012 1.00 23.50  ? 9   PRO B CG  1 
ATOM   2670 C  CD  . PRO B 1 9   ? 9.940   -1.808  -9.525  1.00 23.56  ? 9   PRO B CD  1 
ATOM   2671 N  N   . SER B 1 10  ? 8.120   -6.073  -8.699  1.00 23.36  ? 10  SER B N   1 
ATOM   2672 C  CA  . SER B 1 10  ? 7.303   -6.782  -7.669  1.00 25.09  ? 10  SER B CA  1 
ATOM   2673 C  C   . SER B 1 10  ? 8.087   -7.833  -6.864  1.00 24.81  ? 10  SER B C   1 
ATOM   2674 O  O   . SER B 1 10  ? 7.486   -8.441  -5.961  1.00 24.12  ? 10  SER B O   1 
ATOM   2675 C  CB  . SER B 1 10  ? 6.091   -7.411  -8.305  1.00 25.90  ? 10  SER B CB  1 
ATOM   2676 O  OG  . SER B 1 10  ? 6.449   -8.290  -9.374  1.00 24.98  ? 10  SER B OG  1 
ATOM   2677 N  N   . GLY B 1 11  ? 9.363   -8.083  -7.167  1.00 26.39  ? 11  GLY B N   1 
ATOM   2678 C  CA  . GLY B 1 11  ? 10.137  -9.174  -6.539  1.00 26.63  ? 11  GLY B CA  1 
ATOM   2679 C  C   . GLY B 1 11  ? 10.134  -9.109  -5.012  1.00 27.22  ? 11  GLY B C   1 
ATOM   2680 O  O   . GLY B 1 11  ? 9.980   -10.152 -4.346  1.00 29.48  ? 11  GLY B O   1 
ATOM   2681 N  N   . LYS B 1 12  ? 10.330  -7.943  -4.418  1.00 26.02  ? 12  LYS B N   1 
ATOM   2682 C  CA  . LYS B 1 12  ? 10.349  -7.858  -2.932  1.00 28.05  ? 12  LYS B CA  1 
ATOM   2683 C  C   . LYS B 1 12  ? 9.014   -8.345  -2.334  1.00 27.51  ? 12  LYS B C   1 
ATOM   2684 O  O   . LYS B 1 12  ? 9.016   -8.792  -1.188  1.00 26.91  ? 12  LYS B O   1 
ATOM   2685 C  CB  . LYS B 1 12  ? 10.670  -6.423  -2.524  1.00 31.94  ? 12  LYS B CB  1 
ATOM   2686 C  CG  . LYS B 1 12  ? 12.119  -6.003  -2.727  1.00 31.55  ? 12  LYS B CG  1 
ATOM   2687 C  CD  . LYS B 1 12  ? 12.324  -4.545  -2.415  1.00 36.34  ? 12  LYS B CD  1 
ATOM   2688 C  CE  . LYS B 1 12  ? 13.752  -4.178  -2.071  1.00 39.84  ? 12  LYS B CE  1 
ATOM   2689 N  NZ  . LYS B 1 12  ? 14.651  -4.522  -3.191  1.00 42.95  ? 12  LYS B NZ  1 
ATOM   2690 N  N   . VAL B 1 13  ? 7.911   -8.279  -3.086  1.00 27.71  ? 13  VAL B N   1 
ATOM   2691 C  CA  . VAL B 1 13  ? 6.553   -8.642  -2.610  1.00 26.70  ? 13  VAL B CA  1 
ATOM   2692 C  C   . VAL B 1 13  ? 6.251   -10.096 -2.976  1.00 28.51  ? 13  VAL B C   1 
ATOM   2693 O  O   . VAL B 1 13  ? 5.671   -10.799 -2.112  1.00 27.56  ? 13  VAL B O   1 
ATOM   2694 C  CB  . VAL B 1 13  ? 5.517   -7.655  -3.160  1.00 25.74  ? 13  VAL B CB  1 
ATOM   2695 C  CG1 . VAL B 1 13  ? 4.123   -8.002  -2.686  1.00 26.10  ? 13  VAL B CG1 1 
ATOM   2696 C  CG2 . VAL B 1 13  ? 5.897   -6.223  -2.801  1.00 24.83  ? 13  VAL B CG2 1 
ATOM   2697 N  N   . GLU B 1 14  ? 6.667   -10.556 -4.163  1.00 26.99  ? 14  GLU B N   1 
ATOM   2698 C  CA  . GLU B 1 14  ? 6.555   -11.983 -4.573  1.00 26.34  ? 14  GLU B CA  1 
ATOM   2699 C  C   . GLU B 1 14  ? 7.124   -12.894 -3.463  1.00 26.94  ? 14  GLU B C   1 
ATOM   2700 O  O   . GLU B 1 14  ? 6.480   -13.919 -3.173  1.00 28.66  ? 14  GLU B O   1 
ATOM   2701 C  CB  . GLU B 1 14  ? 7.291   -12.243 -5.893  1.00 25.77  ? 14  GLU B CB  1 
ATOM   2702 C  CG  . GLU B 1 14  ? 6.643   -11.599 -7.105  1.00 25.64  ? 14  GLU B CG  1 
ATOM   2703 C  CD  . GLU B 1 14  ? 7.518   -11.619 -8.345  1.00 25.90  ? 14  GLU B CD  1 
ATOM   2704 O  OE1 . GLU B 1 14  ? 7.944   -12.713 -8.725  1.00 24.30  ? 14  GLU B OE1 1 
ATOM   2705 O  OE2 . GLU B 1 14  ? 7.794   -10.528 -8.916  1.00 25.25  ? 14  GLU B OE2 1 
ATOM   2706 N  N   . GLY B 1 15  ? 8.249   -12.512 -2.848  1.00 28.41  ? 15  GLY B N   1 
ATOM   2707 C  CA  . GLY B 1 15  ? 8.922   -13.231 -1.741  1.00 28.24  ? 15  GLY B CA  1 
ATOM   2708 C  C   . GLY B 1 15  ? 8.053   -13.339 -0.481  1.00 29.42  ? 15  GLY B C   1 
ATOM   2709 O  O   . GLY B 1 15  ? 8.424   -14.087 0.423   1.00 26.90  ? 15  GLY B O   1 
ATOM   2710 N  N   . CYS B 1 16  ? 6.931   -12.624 -0.411  1.00 26.73  ? 16  CYS B N   1 
ATOM   2711 C  CA  . CYS B 1 16  ? 6.073   -12.543 0.793   1.00 26.36  ? 16  CYS B CA  1 
ATOM   2712 C  C   . CYS B 1 16  ? 4.722   -13.203 0.588   1.00 25.01  ? 16  CYS B C   1 
ATOM   2713 O  O   . CYS B 1 16  ? 3.945   -13.213 1.565   1.00 27.77  ? 16  CYS B O   1 
ATOM   2714 C  CB  . CYS B 1 16  ? 5.860   -11.094 1.182   1.00 25.75  ? 16  CYS B CB  1 
ATOM   2715 S  SG  . CYS B 1 16  ? 7.416   -10.318 1.661   1.00 28.77  ? 16  CYS B SG  1 
ATOM   2716 N  N   . MET B 1 17  ? 4.405   -13.710 -0.603  1.00 26.78  ? 17  MET B N   1 
ATOM   2717 C  CA  . MET B 1 17  ? 3.029   -14.189 -0.881  1.00 26.26  ? 17  MET B CA  1 
ATOM   2718 C  C   . MET B 1 17  ? 2.903   -15.667 -0.492  1.00 30.39  ? 17  MET B C   1 
ATOM   2719 O  O   . MET B 1 17  ? 3.700   -16.470 -0.962  1.00 32.43  ? 17  MET B O   1 
ATOM   2720 C  CB  . MET B 1 17  ? 2.642   -14.043 -2.350  1.00 28.74  ? 17  MET B CB  1 
ATOM   2721 C  CG  . MET B 1 17  ? 2.678   -12.621 -2.867  1.00 30.47  ? 17  MET B CG  1 
ATOM   2722 S  SD  . MET B 1 17  ? 1.669   -11.451 -1.958  1.00 31.68  ? 17  MET B SD  1 
ATOM   2723 C  CE  . MET B 1 17  ? 0.110   -12.295 -1.674  1.00 37.22  ? 17  MET B CE  1 
ATOM   2724 N  N   . VAL B 1 18  ? 1.872   -16.008 0.278   1.00 32.05  ? 18  VAL B N   1 
ATOM   2725 C  CA  . VAL B 1 18  ? 1.560   -17.408 0.687   1.00 31.88  ? 18  VAL B CA  1 
ATOM   2726 C  C   . VAL B 1 18  ? 0.086   -17.699 0.400   1.00 34.55  ? 18  VAL B C   1 
ATOM   2727 O  O   . VAL B 1 18  ? -0.711  -16.766 0.119   1.00 32.57  ? 18  VAL B O   1 
ATOM   2728 C  CB  . VAL B 1 18  ? 1.937   -17.668 2.159   1.00 30.70  ? 18  VAL B CB  1 
ATOM   2729 C  CG1 . VAL B 1 18  ? 3.420   -17.412 2.400   1.00 32.05  ? 18  VAL B CG1 1 
ATOM   2730 C  CG2 . VAL B 1 18  ? 1.084   -16.863 3.138   1.00 31.28  ? 18  VAL B CG2 1 
ATOM   2731 N  N   . GLN B 1 19  ? -0.261  -18.983 0.447   1.00 38.97  ? 19  GLN B N   1 
ATOM   2732 C  CA  . GLN B 1 19  ? -1.648  -19.477 0.290   1.00 38.75  ? 19  GLN B CA  1 
ATOM   2733 C  C   . GLN B 1 19  ? -2.163  -19.766 1.698   1.00 35.59  ? 19  GLN B C   1 
ATOM   2734 O  O   . GLN B 1 19  ? -1.424  -20.363 2.481   1.00 38.89  ? 19  GLN B O   1 
ATOM   2735 C  CB  . GLN B 1 19  ? -1.651  -20.663 -0.675  1.00 44.19  ? 19  GLN B CB  1 
ATOM   2736 C  CG  . GLN B 1 19  ? -2.959  -21.443 -0.699  1.00 52.67  ? 19  GLN B CG  1 
ATOM   2737 C  CD  . GLN B 1 19  ? -2.808  -22.803 -1.342  1.00 60.78  ? 19  GLN B CD  1 
ATOM   2738 O  OE1 . GLN B 1 19  ? -3.221  -23.006 -2.484  1.00 64.81  ? 19  GLN B OE1 1 
ATOM   2739 N  NE2 . GLN B 1 19  ? -2.201  -23.741 -0.620  1.00 54.40  ? 19  GLN B NE2 1 
ATOM   2740 N  N   . VAL B 1 20  ? -3.331  -19.237 2.037   1.00 33.39  ? 20  VAL B N   1 
ATOM   2741 C  CA  . VAL B 1 20  ? -4.010  -19.475 3.342   1.00 34.57  ? 20  VAL B CA  1 
ATOM   2742 C  C   . VAL B 1 20  ? -5.310  -20.231 3.044   1.00 36.90  ? 20  VAL B C   1 
ATOM   2743 O  O   . VAL B 1 20  ? -6.040  -19.776 2.155   1.00 37.91  ? 20  VAL B O   1 
ATOM   2744 C  CB  . VAL B 1 20  ? -4.296  -18.153 4.081   1.00 32.85  ? 20  VAL B CB  1 
ATOM   2745 C  CG1 . VAL B 1 20  ? -5.079  -18.392 5.367   1.00 34.94  ? 20  VAL B CG1 1 
ATOM   2746 C  CG2 . VAL B 1 20  ? -3.012  -17.383 4.364   1.00 33.79  ? 20  VAL B CG2 1 
ATOM   2747 N  N   . THR B 1 21  ? -5.576  -21.343 3.746   1.00 41.20  ? 21  THR B N   1 
ATOM   2748 C  CA  . THR B 1 21  ? -6.828  -22.146 3.631   1.00 40.85  ? 21  THR B CA  1 
ATOM   2749 C  C   . THR B 1 21  ? -7.501  -22.277 5.005   1.00 40.54  ? 21  THR B C   1 
ATOM   2750 O  O   . THR B 1 21  ? -6.830  -22.618 5.991   1.00 42.40  ? 21  THR B O   1 
ATOM   2751 C  CB  . THR B 1 21  ? -6.595  -23.552 3.058   1.00 43.36  ? 21  THR B CB  1 
ATOM   2752 O  OG1 . THR B 1 21  ? -5.873  -23.461 1.832   1.00 36.93  ? 21  THR B OG1 1 
ATOM   2753 C  CG2 . THR B 1 21  ? -7.898  -24.290 2.825   1.00 44.27  ? 21  THR B CG2 1 
ATOM   2754 N  N   . CYS B 1 22  ? -8.796  -22.006 5.051   1.00 42.88  ? 22  CYS B N   1 
ATOM   2755 C  CA  . CYS B 1 22  ? -9.671  -22.239 6.226   1.00 46.49  ? 22  CYS B CA  1 
ATOM   2756 C  C   . CYS B 1 22  ? -10.961 -22.899 5.712   1.00 49.60  ? 22  CYS B C   1 
ATOM   2757 O  O   . CYS B 1 22  ? -11.679 -22.271 4.898   1.00 46.35  ? 22  CYS B O   1 
ATOM   2758 C  CB  . CYS B 1 22  ? -9.912  -20.928 6.962   1.00 44.93  ? 22  CYS B CB  1 
ATOM   2759 S  SG  . CYS B 1 22  ? -10.773 -21.125 8.536   1.00 48.00  ? 22  CYS B SG  1 
ATOM   2760 N  N   . GLY B 1 23  ? -11.200 -24.156 6.100   1.00 50.00  ? 23  GLY B N   1 
ATOM   2761 C  CA  . GLY B 1 23  ? -12.266 -25.000 5.529   1.00 45.23  ? 23  GLY B CA  1 
ATOM   2762 C  C   . GLY B 1 23  ? -12.085 -25.148 4.028   1.00 46.65  ? 23  GLY B C   1 
ATOM   2763 O  O   . GLY B 1 23  ? -11.011 -25.598 3.606   1.00 48.38  ? 23  GLY B O   1 
ATOM   2764 N  N   . THR B 1 24  ? -13.084 -24.747 3.243   1.00 51.62  ? 24  THR B N   1 
ATOM   2765 C  CA  . THR B 1 24  ? -13.063 -24.795 1.760   1.00 56.12  ? 24  THR B CA  1 
ATOM   2766 C  C   . THR B 1 24  ? -12.299 -23.589 1.195   1.00 57.54  ? 24  THR B C   1 
ATOM   2767 O  O   . THR B 1 24  ? -11.670 -23.756 0.139   1.00 65.41  ? 24  THR B O   1 
ATOM   2768 C  CB  . THR B 1 24  ? -14.480 -24.828 1.171   1.00 60.96  ? 24  THR B CB  1 
ATOM   2769 O  OG1 . THR B 1 24  ? -15.289 -23.849 1.820   1.00 63.81  ? 24  THR B OG1 1 
ATOM   2770 C  CG2 . THR B 1 24  ? -15.149 -26.173 1.316   1.00 63.81  ? 24  THR B CG2 1 
ATOM   2771 N  N   . THR B 1 25  ? -12.361 -22.424 1.848   1.00 56.87  ? 25  THR B N   1 
ATOM   2772 C  CA  . THR B 1 25  ? -11.819 -21.142 1.317   1.00 51.45  ? 25  THR B CA  1 
ATOM   2773 C  C   . THR B 1 25  ? -10.288 -21.187 1.322   1.00 51.02  ? 25  THR B C   1 
ATOM   2774 O  O   . THR B 1 25  ? -9.675  -21.342 2.417   1.00 52.39  ? 25  THR B O   1 
ATOM   2775 C  CB  . THR B 1 25  ? -12.327 -19.933 2.106   1.00 55.71  ? 25  THR B CB  1 
ATOM   2776 O  OG1 . THR B 1 25  ? -13.723 -20.111 2.325   1.00 57.21  ? 25  THR B OG1 1 
ATOM   2777 C  CG2 . THR B 1 25  ? -12.085 -18.618 1.397   1.00 55.73  ? 25  THR B CG2 1 
ATOM   2778 N  N   . THR B 1 26  ? -9.694  -21.048 0.137   1.00 48.31  ? 26  THR B N   1 
ATOM   2779 C  CA  . THR B 1 26  ? -8.249  -20.768 -0.055  1.00 50.27  ? 26  THR B CA  1 
ATOM   2780 C  C   . THR B 1 26  ? -8.100  -19.363 -0.664  1.00 49.04  ? 26  THR B C   1 
ATOM   2781 O  O   . THR B 1 26  ? -8.898  -19.011 -1.549  1.00 45.50  ? 26  THR B O   1 
ATOM   2782 C  CB  . THR B 1 26  ? -7.603  -21.902 -0.859  1.00 50.16  ? 26  THR B CB  1 
ATOM   2783 O  OG1 . THR B 1 26  ? -7.562  -23.040 0.002   1.00 54.01  ? 26  THR B OG1 1 
ATOM   2784 C  CG2 . THR B 1 26  ? -6.197  -21.603 -1.325  1.00 48.65  ? 26  THR B CG2 1 
ATOM   2785 N  N   . LEU B 1 27  ? -7.139  -18.574 -0.178  1.00 44.22  ? 27  LEU B N   1 
ATOM   2786 C  CA  . LEU B 1 27  ? -6.838  -17.223 -0.725  1.00 38.99  ? 27  LEU B CA  1 
ATOM   2787 C  C   . LEU B 1 27  ? -5.430  -16.796 -0.305  1.00 35.05  ? 27  LEU B C   1 
ATOM   2788 O  O   . LEU B 1 27  ? -4.716  -17.595 0.323   1.00 33.09  ? 27  LEU B O   1 
ATOM   2789 C  CB  . LEU B 1 27  ? -7.928  -16.237 -0.289  1.00 37.18  ? 27  LEU B CB  1 
ATOM   2790 C  CG  . LEU B 1 27  ? -8.280  -16.212 1.196   1.00 36.42  ? 27  LEU B CG  1 
ATOM   2791 C  CD1 . LEU B 1 27  ? -7.088  -15.804 2.038   1.00 35.19  ? 27  LEU B CD1 1 
ATOM   2792 C  CD2 . LEU B 1 27  ? -9.459  -15.291 1.459   1.00 36.23  ? 27  LEU B CD2 1 
ATOM   2793 N  N   . ASN B 1 28  ? -5.041  -15.568 -0.641  1.00 32.93  ? 28  ASN B N   1 
ATOM   2794 C  CA  . ASN B 1 28  ? -3.622  -15.113 -0.589  1.00 30.24  ? 28  ASN B CA  1 
ATOM   2795 C  C   . ASN B 1 28  ? -3.349  -14.449 0.763   1.00 26.11  ? 28  ASN B C   1 
ATOM   2796 O  O   . ASN B 1 28  ? -4.239  -13.797 1.336   1.00 25.88  ? 28  ASN B O   1 
ATOM   2797 C  CB  . ASN B 1 28  ? -3.288  -14.275 -1.827  1.00 33.87  ? 28  ASN B CB  1 
ATOM   2798 C  CG  . ASN B 1 28  ? -3.848  -14.919 -3.087  1.00 38.67  ? 28  ASN B CG  1 
ATOM   2799 O  OD1 . ASN B 1 28  ? -3.158  -15.707 -3.742  1.00 37.53  ? 28  ASN B OD1 1 
ATOM   2800 N  ND2 . ASN B 1 28  ? -5.122  -14.654 -3.390  1.00 39.86  ? 28  ASN B ND2 1 
ATOM   2801 N  N   . GLY B 1 29  ? -2.152  -14.655 1.285   1.00 24.40  ? 29  GLY B N   1 
ATOM   2802 C  CA  . GLY B 1 29  ? -1.728  -14.047 2.549   1.00 24.50  ? 29  GLY B CA  1 
ATOM   2803 C  C   . GLY B 1 29  ? -0.414  -13.358 2.333   1.00 23.39  ? 29  GLY B C   1 
ATOM   2804 O  O   . GLY B 1 29  ? 0.246   -13.668 1.325   1.00 23.06  ? 29  GLY B O   1 
ATOM   2805 N  N   . LEU B 1 30  ? -0.066  -12.435 3.218   1.00 23.92  ? 30  LEU B N   1 
ATOM   2806 C  CA  . LEU B 1 30  ? 1.218   -11.714 3.143   1.00 25.37  ? 30  LEU B CA  1 
ATOM   2807 C  C   . LEU B 1 30  ? 2.044   -12.147 4.353   1.00 27.62  ? 30  LEU B C   1 
ATOM   2808 O  O   . LEU B 1 30  ? 1.605   -11.902 5.493   1.00 26.46  ? 30  LEU B O   1 
ATOM   2809 C  CB  . LEU B 1 30  ? 0.944   -10.208 3.131   1.00 25.83  ? 30  LEU B CB  1 
ATOM   2810 C  CG  . LEU B 1 30  ? 2.153   -9.306  2.836   1.00 25.18  ? 30  LEU B CG  1 
ATOM   2811 C  CD1 . LEU B 1 30  ? 2.660   -9.492  1.407   1.00 22.89  ? 30  LEU B CD1 1 
ATOM   2812 C  CD2 . LEU B 1 30  ? 1.780   -7.851  3.093   1.00 24.92  ? 30  LEU B CD2 1 
ATOM   2813 N  N   . TRP B 1 31  ? 3.183   -12.790 4.101   1.00 28.31  ? 31  TRP B N   1 
ATOM   2814 C  CA  . TRP B 1 31  ? 4.072   -13.348 5.149   1.00 27.28  ? 31  TRP B CA  1 
ATOM   2815 C  C   . TRP B 1 31  ? 5.256   -12.399 5.380   1.00 25.76  ? 31  TRP B C   1 
ATOM   2816 O  O   . TRP B 1 31  ? 6.176   -12.361 4.561   1.00 27.07  ? 31  TRP B O   1 
ATOM   2817 C  CB  . TRP B 1 31  ? 4.488   -14.769 4.744   1.00 29.53  ? 31  TRP B CB  1 
ATOM   2818 C  CG  . TRP B 1 31  ? 5.387   -15.460 5.724   1.00 34.61  ? 31  TRP B CG  1 
ATOM   2819 C  CD1 . TRP B 1 31  ? 5.472   -15.257 7.076   1.00 39.30  ? 31  TRP B CD1 1 
ATOM   2820 C  CD2 . TRP B 1 31  ? 6.329   -16.500 5.418   1.00 37.03  ? 31  TRP B CD2 1 
ATOM   2821 N  NE1 . TRP B 1 31  ? 6.418   -16.085 7.634   1.00 36.43  ? 31  TRP B NE1 1 
ATOM   2822 C  CE2 . TRP B 1 31  ? 6.947   -16.868 6.636   1.00 40.27  ? 31  TRP B CE2 1 
ATOM   2823 C  CE3 . TRP B 1 31  ? 6.700   -17.151 4.236   1.00 34.27  ? 31  TRP B CE3 1 
ATOM   2824 C  CZ2 . TRP B 1 31  ? 7.947   -17.835 6.689   1.00 41.26  ? 31  TRP B CZ2 1 
ATOM   2825 C  CZ3 . TRP B 1 31  ? 7.677   -18.116 4.302   1.00 41.93  ? 31  TRP B CZ3 1 
ATOM   2826 C  CH2 . TRP B 1 31  ? 8.284   -18.458 5.514   1.00 40.38  ? 31  TRP B CH2 1 
ATOM   2827 N  N   . LEU B 1 32  ? 5.233   -11.682 6.490   1.00 27.52  ? 32  LEU B N   1 
ATOM   2828 C  CA  . LEU B 1 32  ? 6.256   -10.703 6.921   1.00 28.77  ? 32  LEU B CA  1 
ATOM   2829 C  C   . LEU B 1 32  ? 6.682   -11.000 8.362   1.00 31.32  ? 32  LEU B C   1 
ATOM   2830 O  O   . LEU B 1 32  ? 5.787   -11.176 9.218   1.00 30.29  ? 32  LEU B O   1 
ATOM   2831 C  CB  . LEU B 1 32  ? 5.650   -9.302  6.851   1.00 28.81  ? 32  LEU B CB  1 
ATOM   2832 C  CG  . LEU B 1 32  ? 5.277   -8.842  5.452   1.00 27.62  ? 32  LEU B CG  1 
ATOM   2833 C  CD1 . LEU B 1 32  ? 4.337   -7.663  5.527   1.00 26.87  ? 32  LEU B CD1 1 
ATOM   2834 C  CD2 . LEU B 1 32  ? 6.528   -8.498  4.665   1.00 28.84  ? 32  LEU B CD2 1 
ATOM   2835 N  N   . ASP B 1 33  ? 7.995   -11.018 8.613   1.00 30.62  ? 33  ASP B N   1 
ATOM   2836 C  CA  . ASP B 1 33  ? 8.553   -11.572 9.863   1.00 30.44  ? 33  ASP B CA  1 
ATOM   2837 C  C   . ASP B 1 33  ? 7.782   -12.881 10.136  1.00 32.01  ? 33  ASP B C   1 
ATOM   2838 O  O   . ASP B 1 33  ? 7.655   -13.723 9.194   1.00 31.85  ? 33  ASP B O   1 
ATOM   2839 C  CB  . ASP B 1 33  ? 8.511   -10.479 10.930  1.00 32.99  ? 33  ASP B CB  1 
ATOM   2840 C  CG  . ASP B 1 33  ? 9.134   -9.176  10.458  1.00 33.10  ? 33  ASP B CG  1 
ATOM   2841 O  OD1 . ASP B 1 33  ? 10.362  -9.162  10.260  1.00 37.11  ? 33  ASP B OD1 1 
ATOM   2842 O  OD2 . ASP B 1 33  ? 8.382   -8.194  10.276  1.00 37.11  ? 33  ASP B OD2 1 
ATOM   2843 N  N   . ASP B 1 34  ? 7.224   -13.075 11.336  1.00 32.73  ? 34  ASP B N   1 
ATOM   2844 C  CA  . ASP B 1 34  ? 6.595   -14.379 11.691  1.00 33.22  ? 34  ASP B CA  1 
ATOM   2845 C  C   . ASP B 1 34  ? 5.062   -14.258 11.709  1.00 34.81  ? 34  ASP B C   1 
ATOM   2846 O  O   . ASP B 1 34  ? 4.420   -15.037 12.484  1.00 38.44  ? 34  ASP B O   1 
ATOM   2847 C  CB  . ASP B 1 34  ? 7.178   -14.906 13.008  1.00 34.66  ? 34  ASP B CB  1 
ATOM   2848 C  CG  . ASP B 1 34  ? 6.930   -14.011 14.210  1.00 34.66  ? 34  ASP B CG  1 
ATOM   2849 O  OD1 . ASP B 1 34  ? 6.515   -12.863 14.014  1.00 34.29  ? 34  ASP B OD1 1 
ATOM   2850 O  OD2 . ASP B 1 34  ? 7.139   -14.480 15.325  1.00 39.96  ? 34  ASP B OD2 1 
ATOM   2851 N  N   . VAL B 1 35  ? 4.472   -13.364 10.898  1.00 30.64  ? 35  VAL B N   1 
ATOM   2852 C  CA  . VAL B 1 35  ? 2.987   -13.175 10.832  1.00 26.44  ? 35  VAL B CA  1 
ATOM   2853 C  C   . VAL B 1 35  ? 2.513   -13.290 9.383   1.00 27.89  ? 35  VAL B C   1 
ATOM   2854 O  O   . VAL B 1 35  ? 3.194   -12.730 8.479   1.00 26.53  ? 35  VAL B O   1 
ATOM   2855 C  CB  . VAL B 1 35  ? 2.562   -11.819 11.430  1.00 28.22  ? 35  VAL B CB  1 
ATOM   2856 C  CG1 . VAL B 1 35  ? 1.060   -11.598 11.297  1.00 28.45  ? 35  VAL B CG1 1 
ATOM   2857 C  CG2 . VAL B 1 35  ? 2.986   -11.676 12.880  1.00 27.61  ? 35  VAL B CG2 1 
ATOM   2858 N  N   . VAL B 1 36  ? 1.372   -13.959 9.176   1.00 25.05  ? 36  VAL B N   1 
ATOM   2859 C  CA  . VAL B 1 36  ? 0.655   -13.991 7.877   1.00 27.57  ? 36  VAL B CA  1 
ATOM   2860 C  C   . VAL B 1 36  ? -0.598  -13.131 8.008   1.00 29.61  ? 36  VAL B C   1 
ATOM   2861 O  O   . VAL B 1 36  ? -1.432  -13.441 8.889   1.00 29.22  ? 36  VAL B O   1 
ATOM   2862 C  CB  . VAL B 1 36  ? 0.330   -15.418 7.408   1.00 27.29  ? 36  VAL B CB  1 
ATOM   2863 C  CG1 . VAL B 1 36  ? -0.440  -15.383 6.104   1.00 26.11  ? 36  VAL B CG1 1 
ATOM   2864 C  CG2 . VAL B 1 36  ? 1.603   -16.233 7.242   1.00 26.27  ? 36  VAL B CG2 1 
ATOM   2865 N  N   . TYR B 1 37  ? -0.705  -12.098 7.167   1.00 27.07  ? 37  TYR B N   1 
ATOM   2866 C  CA  . TYR B 1 37  ? -1.881  -11.201 7.059   1.00 26.51  ? 37  TYR B CA  1 
ATOM   2867 C  C   . TYR B 1 37  ? -2.776  -11.644 5.913   1.00 26.32  ? 37  TYR B C   1 
ATOM   2868 O  O   . TYR B 1 37  ? -2.250  -11.839 4.818   1.00 30.60  ? 37  TYR B O   1 
ATOM   2869 C  CB  . TYR B 1 37  ? -1.440  -9.761  6.814   1.00 25.99  ? 37  TYR B CB  1 
ATOM   2870 C  CG  . TYR B 1 37  ? -0.476  -9.269  7.849   1.00 25.95  ? 37  TYR B CG  1 
ATOM   2871 C  CD1 . TYR B 1 37  ? 0.863   -9.611  7.777   1.00 29.60  ? 37  TYR B CD1 1 
ATOM   2872 C  CD2 . TYR B 1 37  ? -0.903  -8.548  8.949   1.00 27.51  ? 37  TYR B CD2 1 
ATOM   2873 C  CE1 . TYR B 1 37  ? 1.766   -9.180  8.739   1.00 30.37  ? 37  TYR B CE1 1 
ATOM   2874 C  CE2 . TYR B 1 37  ? -0.013  -8.086  9.914   1.00 26.85  ? 37  TYR B CE2 1 
ATOM   2875 C  CZ  . TYR B 1 37  ? 1.325   -8.422  9.814   1.00 30.02  ? 37  TYR B CZ  1 
ATOM   2876 O  OH  . TYR B 1 37  ? 2.221   -8.024  10.750  1.00 27.16  ? 37  TYR B OH  1 
ATOM   2877 N  N   . CYS B 1 38  ? -4.089  -11.737 6.139   1.00 26.64  ? 38  CYS B N   1 
ATOM   2878 C  CA  . CYS B 1 38  ? -5.094  -12.084 5.090   1.00 25.74  ? 38  CYS B CA  1 
ATOM   2879 C  C   . CYS B 1 38  ? -6.447  -11.509 5.489   1.00 24.79  ? 38  CYS B C   1 
ATOM   2880 O  O   . CYS B 1 38  ? -6.621  -11.047 6.615   1.00 23.64  ? 38  CYS B O   1 
ATOM   2881 C  CB  . CYS B 1 38  ? -5.169  -13.591 4.852   1.00 28.39  ? 38  CYS B CB  1 
ATOM   2882 S  SG  . CYS B 1 38  ? -6.022  -14.543 6.155   1.00 30.58  ? 38  CYS B SG  1 
ATOM   2883 N  N   . PRO B 1 39  ? -7.451  -11.473 4.579   1.00 26.09  ? 39  PRO B N   1 
ATOM   2884 C  CA  . PRO B 1 39  ? -8.772  -10.965 4.932   1.00 25.87  ? 39  PRO B CA  1 
ATOM   2885 C  C   . PRO B 1 39  ? -9.457  -11.869 5.976   1.00 27.50  ? 39  PRO B C   1 
ATOM   2886 O  O   . PRO B 1 39  ? -9.414  -13.072 5.824   1.00 23.91  ? 39  PRO B O   1 
ATOM   2887 C  CB  . PRO B 1 39  ? -9.517  -10.928 3.589   1.00 26.15  ? 39  PRO B CB  1 
ATOM   2888 C  CG  . PRO B 1 39  ? -8.402  -10.942 2.544   1.00 26.86  ? 39  PRO B CG  1 
ATOM   2889 C  CD  . PRO B 1 39  ? -7.370  -11.861 3.164   1.00 26.69  ? 39  PRO B CD  1 
ATOM   2890 N  N   . ARG B 1 40  ? -10.074 -11.270 7.002   1.00 28.01  ? 40  ARG B N   1 
ATOM   2891 C  CA  . ARG B 1 40  ? -10.727 -12.044 8.086   1.00 29.70  ? 40  ARG B CA  1 
ATOM   2892 C  C   . ARG B 1 40  ? -11.839 -12.905 7.468   1.00 31.67  ? 40  ARG B C   1 
ATOM   2893 O  O   . ARG B 1 40  ? -12.096 -13.980 8.026   1.00 35.62  ? 40  ARG B O   1 
ATOM   2894 C  CB  . ARG B 1 40  ? -11.190 -11.134 9.239   1.00 31.13  ? 40  ARG B CB  1 
ATOM   2895 C  CG  . ARG B 1 40  ? -12.385 -10.238 8.944   1.00 29.37  ? 40  ARG B CG  1 
ATOM   2896 C  CD  . ARG B 1 40  ? -12.870 -9.511  10.169  1.00 27.81  ? 40  ARG B CD  1 
ATOM   2897 N  NE  . ARG B 1 40  ? -13.933 -8.598  9.801   1.00 28.86  ? 40  ARG B NE  1 
ATOM   2898 C  CZ  . ARG B 1 40  ? -14.647 -7.880  10.661  1.00 30.42  ? 40  ARG B CZ  1 
ATOM   2899 N  NH1 . ARG B 1 40  ? -14.402 -7.955  11.953  1.00 31.19  ? 40  ARG B NH1 1 
ATOM   2900 N  NH2 . ARG B 1 40  ? -15.610 -7.091  10.230  1.00 31.10  ? 40  ARG B NH2 1 
ATOM   2901 N  N   . HIS B 1 41  ? -12.425 -12.532 6.325   1.00 29.68  ? 41  HIS B N   1 
ATOM   2902 C  CA  . HIS B 1 41  ? -13.553 -13.307 5.733   1.00 31.28  ? 41  HIS B CA  1 
ATOM   2903 C  C   . HIS B 1 41  ? -13.134 -14.713 5.293   1.00 30.76  ? 41  HIS B C   1 
ATOM   2904 O  O   . HIS B 1 41  ? -14.046 -15.481 4.943   1.00 31.50  ? 41  HIS B O   1 
ATOM   2905 C  CB  . HIS B 1 41  ? -14.300 -12.586 4.608   1.00 31.63  ? 41  HIS B CB  1 
ATOM   2906 C  CG  . HIS B 1 41  ? -13.539 -12.398 3.339   1.00 33.77  ? 41  HIS B CG  1 
ATOM   2907 N  ND1 . HIS B 1 41  ? -13.153 -13.448 2.519   1.00 37.59  ? 41  HIS B ND1 1 
ATOM   2908 C  CD2 . HIS B 1 41  ? -13.131 -11.267 2.724   1.00 35.51  ? 41  HIS B CD2 1 
ATOM   2909 C  CE1 . HIS B 1 41  ? -12.538 -12.966 1.459   1.00 37.24  ? 41  HIS B CE1 1 
ATOM   2910 N  NE2 . HIS B 1 41  ? -12.514 -11.631 1.563   1.00 36.63  ? 41  HIS B NE2 1 
ATOM   2911 N  N   . VAL B 1 42  ? -11.850 -15.061 5.354   1.00 32.07  ? 42  VAL B N   1 
ATOM   2912 C  CA  . VAL B 1 42  ? -11.339 -16.435 5.052   1.00 34.37  ? 42  VAL B CA  1 
ATOM   2913 C  C   . VAL B 1 42  ? -12.039 -17.457 5.972   1.00 36.29  ? 42  VAL B C   1 
ATOM   2914 O  O   . VAL B 1 42  ? -12.182 -18.615 5.546   1.00 37.41  ? 42  VAL B O   1 
ATOM   2915 C  CB  . VAL B 1 42  ? -9.809  -16.517 5.189   1.00 30.89  ? 42  VAL B CB  1 
ATOM   2916 C  CG1 . VAL B 1 42  ? -9.346  -16.408 6.624   1.00 31.07  ? 42  VAL B CG1 1 
ATOM   2917 C  CG2 . VAL B 1 42  ? -9.239  -17.772 4.547   1.00 32.58  ? 42  VAL B CG2 1 
ATOM   2918 N  N   . ILE B 1 43  ? -12.461 -17.039 7.169   1.00 39.76  ? 43  ILE B N   1 
ATOM   2919 C  CA  . ILE B 1 43  ? -13.058 -17.942 8.205   1.00 44.28  ? 43  ILE B CA  1 
ATOM   2920 C  C   . ILE B 1 43  ? -14.536 -18.240 7.902   1.00 46.83  ? 43  ILE B C   1 
ATOM   2921 O  O   . ILE B 1 43  ? -15.056 -19.184 8.512   1.00 53.24  ? 43  ILE B O   1 
ATOM   2922 C  CB  . ILE B 1 43  ? -12.870 -17.375 9.630   1.00 39.91  ? 43  ILE B CB  1 
ATOM   2923 C  CG1 . ILE B 1 43  ? -13.761 -16.166 9.915   1.00 39.64  ? 43  ILE B CG1 1 
ATOM   2924 C  CG2 . ILE B 1 43  ? -11.397 -17.095 9.884   1.00 41.64  ? 43  ILE B CG2 1 
ATOM   2925 C  CD1 . ILE B 1 43  ? -13.568 -15.585 11.304  1.00 41.26  ? 43  ILE B CD1 1 
ATOM   2926 N  N   . CYS B 1 44  ? -15.179 -17.497 6.998   1.00 45.26  ? 44  CYS B N   1 
ATOM   2927 C  CA  . CYS B 1 44  ? -16.649 -17.530 6.760   1.00 46.74  ? 44  CYS B CA  1 
ATOM   2928 C  C   . CYS B 1 44  ? -17.053 -18.586 5.722   1.00 52.13  ? 44  CYS B C   1 
ATOM   2929 O  O   . CYS B 1 44  ? -16.490 -18.582 4.615   1.00 47.56  ? 44  CYS B O   1 
ATOM   2930 C  CB  . CYS B 1 44  ? -17.157 -16.174 6.292   1.00 42.49  ? 44  CYS B CB  1 
ATOM   2931 S  SG  . CYS B 1 44  ? -17.129 -14.935 7.611   1.00 44.67  ? 44  CYS B SG  1 
ATOM   2932 N  N   . THR B 1 45  ? -18.038 -19.430 6.064   1.00 56.13  ? 45  THR B N   1 
ATOM   2933 C  CA  . THR B 1 45  ? -18.821 -20.220 5.078   1.00 58.22  ? 45  THR B CA  1 
ATOM   2934 C  C   . THR B 1 45  ? -19.663 -19.214 4.288   1.00 61.86  ? 45  THR B C   1 
ATOM   2935 O  O   . THR B 1 45  ? -19.844 -18.092 4.801   1.00 55.93  ? 45  THR B O   1 
ATOM   2936 C  CB  . THR B 1 45  ? -19.715 -21.272 5.747   1.00 53.46  ? 45  THR B CB  1 
ATOM   2937 O  OG1 . THR B 1 45  ? -20.765 -20.551 6.399   1.00 47.09  ? 45  THR B OG1 1 
ATOM   2938 C  CG2 . THR B 1 45  ? -18.960 -22.158 6.713   1.00 49.49  ? 45  THR B CG2 1 
ATOM   2939 N  N   . SER B 1 46  ? -20.150 -19.587 3.100   1.00 67.30  ? 46  SER B N   1 
ATOM   2940 C  CA  . SER B 1 46  ? -21.046 -18.744 2.260   1.00 69.04  ? 46  SER B CA  1 
ATOM   2941 C  C   . SER B 1 46  ? -22.215 -18.228 3.104   1.00 67.97  ? 46  SER B C   1 
ATOM   2942 O  O   . SER B 1 46  ? -22.630 -17.066 2.907   1.00 69.27  ? 46  SER B O   1 
ATOM   2943 C  CB  . SER B 1 46  ? -21.540 -19.486 1.051   1.00 69.22  ? 46  SER B CB  1 
ATOM   2944 O  OG  . SER B 1 46  ? -20.672 -19.262 -0.047  1.00 74.44  ? 46  SER B OG  1 
ATOM   2945 N  N   . GLU B 1 47  ? -22.689 -19.056 4.035   1.00 67.81  ? 47  GLU B N   1 
ATOM   2946 C  CA  . GLU B 1 47  ? -23.864 -18.786 4.903   1.00 64.86  ? 47  GLU B CA  1 
ATOM   2947 C  C   . GLU B 1 47  ? -23.474 -17.730 5.945   1.00 56.72  ? 47  GLU B C   1 
ATOM   2948 O  O   . GLU B 1 47  ? -24.256 -16.784 6.164   1.00 54.13  ? 47  GLU B O   1 
ATOM   2949 C  CB  . GLU B 1 47  ? -24.327 -20.101 5.528   1.00 74.30  ? 47  GLU B CB  1 
ATOM   2950 C  CG  . GLU B 1 47  ? -24.317 -21.257 4.540   1.00 85.06  ? 47  GLU B CG  1 
ATOM   2951 C  CD  . GLU B 1 47  ? -24.579 -22.623 5.140   1.00 94.41  ? 47  GLU B CD  1 
ATOM   2952 O  OE1 . GLU B 1 47  ? -23.724 -23.091 5.922   1.00 97.81  ? 47  GLU B OE1 1 
ATOM   2953 O  OE2 . GLU B 1 47  ? -25.628 -23.216 4.810   1.00 103.69 ? 47  GLU B OE2 1 
ATOM   2954 N  N   . ASP B 1 48  ? -22.288 -17.870 6.539   1.00 50.67  ? 48  ASP B N   1 
ATOM   2955 C  CA  . ASP B 1 48  ? -21.685 -16.855 7.448   1.00 49.51  ? 48  ASP B CA  1 
ATOM   2956 C  C   . ASP B 1 48  ? -21.641 -15.476 6.769   1.00 45.79  ? 48  ASP B C   1 
ATOM   2957 O  O   . ASP B 1 48  ? -21.950 -14.471 7.452   1.00 41.54  ? 48  ASP B O   1 
ATOM   2958 C  CB  . ASP B 1 48  ? -20.283 -17.286 7.883   1.00 52.45  ? 48  ASP B CB  1 
ATOM   2959 C  CG  . ASP B 1 48  ? -20.288 -18.441 8.869   1.00 52.67  ? 48  ASP B CG  1 
ATOM   2960 O  OD1 . ASP B 1 48  ? -21.051 -18.356 9.849   1.00 51.48  ? 48  ASP B OD1 1 
ATOM   2961 O  OD2 . ASP B 1 48  ? -19.548 -19.423 8.630   1.00 53.36  ? 48  ASP B OD2 1 
ATOM   2962 N  N   . MET B 1 49  ? -21.294 -15.428 5.473   1.00 48.26  ? 49  MET B N   1 
ATOM   2963 C  CA  . MET B 1 49  ? -21.008 -14.168 4.726   1.00 47.31  ? 49  MET B CA  1 
ATOM   2964 C  C   . MET B 1 49  ? -22.239 -13.258 4.729   1.00 45.17  ? 49  MET B C   1 
ATOM   2965 O  O   . MET B 1 49  ? -22.046 -12.036 4.624   1.00 36.83  ? 49  MET B O   1 
ATOM   2966 C  CB  . MET B 1 49  ? -20.570 -14.407 3.276   1.00 44.37  ? 49  MET B CB  1 
ATOM   2967 C  CG  . MET B 1 49  ? -19.088 -14.701 3.113   1.00 49.32  ? 49  MET B CG  1 
ATOM   2968 S  SD  . MET B 1 49  ? -18.003 -13.567 4.033   1.00 54.06  ? 49  MET B SD  1 
ATOM   2969 C  CE  . MET B 1 49  ? -17.885 -12.175 2.905   1.00 52.45  ? 49  MET B CE  1 
ATOM   2970 N  N   . LEU B 1 50  ? -23.451 -13.817 4.846   1.00 44.76  ? 50  LEU B N   1 
ATOM   2971 C  CA  . LEU B 1 50  ? -24.691 -13.010 4.758   1.00 47.60  ? 50  LEU B CA  1 
ATOM   2972 C  C   . LEU B 1 50  ? -24.773 -12.088 5.977   1.00 43.42  ? 50  LEU B C   1 
ATOM   2973 O  O   . LEU B 1 50  ? -25.147 -10.927 5.787   1.00 44.10  ? 50  LEU B O   1 
ATOM   2974 C  CB  . LEU B 1 50  ? -25.907 -13.931 4.607   1.00 56.90  ? 50  LEU B CB  1 
ATOM   2975 C  CG  . LEU B 1 50  ? -26.214 -14.380 3.173   1.00 65.50  ? 50  LEU B CG  1 
ATOM   2976 C  CD1 . LEU B 1 50  ? -24.968 -14.897 2.461   1.00 70.14  ? 50  LEU B CD1 1 
ATOM   2977 C  CD2 . LEU B 1 50  ? -27.308 -15.442 3.155   1.00 67.85  ? 50  LEU B CD2 1 
ATOM   2978 N  N   . ASN B 1 51  ? -24.409 -12.564 7.169   1.00 42.77  ? 51  ASN B N   1 
ATOM   2979 C  CA  . ASN B 1 51  ? -24.478 -11.753 8.413   1.00 46.22  ? 51  ASN B CA  1 
ATOM   2980 C  C   . ASN B 1 51  ? -23.453 -12.292 9.411   1.00 42.17  ? 51  ASN B C   1 
ATOM   2981 O  O   . ASN B 1 51  ? -23.806 -12.812 10.461  1.00 40.43  ? 51  ASN B O   1 
ATOM   2982 C  CB  . ASN B 1 51  ? -25.909 -11.703 8.961   1.00 56.02  ? 51  ASN B CB  1 
ATOM   2983 C  CG  . ASN B 1 51  ? -26.222 -10.462 9.780   1.00 59.38  ? 51  ASN B CG  1 
ATOM   2984 O  OD1 . ASN B 1 51  ? -26.281 -10.522 11.006  1.00 71.95  ? 51  ASN B OD1 1 
ATOM   2985 N  ND2 . ASN B 1 51  ? -26.462 -9.342  9.117   1.00 60.50  ? 51  ASN B ND2 1 
ATOM   2986 N  N   . PRO B 1 52  ? -22.140 -12.124 9.141   1.00 41.95  ? 52  PRO B N   1 
ATOM   2987 C  CA  . PRO B 1 52  ? -21.090 -12.740 9.951   1.00 39.88  ? 52  PRO B CA  1 
ATOM   2988 C  C   . PRO B 1 52  ? -20.880 -12.065 11.313  1.00 39.25  ? 52  PRO B C   1 
ATOM   2989 O  O   . PRO B 1 52  ? -20.954 -10.862 11.431  1.00 38.05  ? 52  PRO B O   1 
ATOM   2990 C  CB  . PRO B 1 52  ? -19.837 -12.561 9.077   1.00 43.53  ? 52  PRO B CB  1 
ATOM   2991 C  CG  . PRO B 1 52  ? -20.112 -11.268 8.319   1.00 40.56  ? 52  PRO B CG  1 
ATOM   2992 C  CD  . PRO B 1 52  ? -21.595 -11.300 8.046   1.00 42.21  ? 52  PRO B CD  1 
ATOM   2993 N  N   . ASN B 1 53  ? -20.640 -12.876 12.332  1.00 39.23  ? 53  ASN B N   1 
ATOM   2994 C  CA  . ASN B 1 53  ? -20.169 -12.416 13.660  1.00 41.41  ? 53  ASN B CA  1 
ATOM   2995 C  C   . ASN B 1 53  ? -18.745 -12.952 13.779  1.00 43.96  ? 53  ASN B C   1 
ATOM   2996 O  O   . ASN B 1 53  ? -18.573 -14.163 14.074  1.00 45.58  ? 53  ASN B O   1 
ATOM   2997 C  CB  . ASN B 1 53  ? -21.123 -12.862 14.773  1.00 45.47  ? 53  ASN B CB  1 
ATOM   2998 C  CG  . ASN B 1 53  ? -20.672 -12.469 16.165  1.00 45.58  ? 53  ASN B CG  1 
ATOM   2999 O  OD1 . ASN B 1 53  ? -19.501 -12.174 16.398  1.00 45.56  ? 53  ASN B OD1 1 
ATOM   3000 N  ND2 . ASN B 1 53  ? -21.594 -12.507 17.113  1.00 49.83  ? 53  ASN B ND2 1 
ATOM   3001 N  N   . TYR B 1 54  ? -17.772 -12.109 13.422  1.00 41.22  ? 54  TYR B N   1 
ATOM   3002 C  CA  . TYR B 1 54  ? -16.351 -12.504 13.277  1.00 41.34  ? 54  TYR B CA  1 
ATOM   3003 C  C   . TYR B 1 54  ? -15.823 -12.874 14.663  1.00 39.66  ? 54  TYR B C   1 
ATOM   3004 O  O   . TYR B 1 54  ? -15.151 -13.914 14.761  1.00 42.81  ? 54  TYR B O   1 
ATOM   3005 C  CB  . TYR B 1 54  ? -15.539 -11.401 12.589  1.00 38.14  ? 54  TYR B CB  1 
ATOM   3006 C  CG  . TYR B 1 54  ? -15.782 -11.307 11.106  1.00 33.59  ? 54  TYR B CG  1 
ATOM   3007 C  CD1 . TYR B 1 54  ? -15.220 -12.229 10.242  1.00 31.96  ? 54  TYR B CD1 1 
ATOM   3008 C  CD2 . TYR B 1 54  ? -16.622 -10.340 10.575  1.00 31.78  ? 54  TYR B CD2 1 
ATOM   3009 C  CE1 . TYR B 1 54  ? -15.474 -12.189 8.881   1.00 31.26  ? 54  TYR B CE1 1 
ATOM   3010 C  CE2 . TYR B 1 54  ? -16.868 -10.271 9.213   1.00 30.55  ? 54  TYR B CE2 1 
ATOM   3011 C  CZ  . TYR B 1 54  ? -16.288 -11.198 8.362   1.00 32.01  ? 54  TYR B CZ  1 
ATOM   3012 O  OH  . TYR B 1 54  ? -16.511 -11.175 7.013   1.00 31.30  ? 54  TYR B OH  1 
ATOM   3013 N  N   . GLU B 1 55  ? -16.147 -12.051 15.669  1.00 48.76  ? 55  GLU B N   1 
ATOM   3014 C  CA  . GLU B 1 55  ? -15.794 -12.265 17.105  1.00 56.35  ? 55  GLU B CA  1 
ATOM   3015 C  C   . GLU B 1 55  ? -16.053 -13.728 17.449  1.00 58.27  ? 55  GLU B C   1 
ATOM   3016 O  O   . GLU B 1 55  ? -15.079 -14.437 17.807  1.00 52.18  ? 55  GLU B O   1 
ATOM   3017 C  CB  . GLU B 1 55  ? -16.660 -11.431 18.058  1.00 61.64  ? 55  GLU B CB  1 
ATOM   3018 C  CG  . GLU B 1 55  ? -16.531 -9.928  17.880  1.00 64.89  ? 55  GLU B CG  1 
ATOM   3019 C  CD  . GLU B 1 55  ? -17.006 -9.119  19.076  1.00 64.08  ? 55  GLU B CD  1 
ATOM   3020 O  OE1 . GLU B 1 55  ? -18.230 -9.078  19.316  1.00 67.15  ? 55  GLU B OE1 1 
ATOM   3021 O  OE2 . GLU B 1 55  ? -16.144 -8.549  19.774  1.00 57.10  ? 55  GLU B OE2 1 
ATOM   3022 N  N   . ASP B 1 56  ? -17.320 -14.134 17.259  1.00 55.84  ? 56  ASP B N   1 
ATOM   3023 C  CA  . ASP B 1 56  ? -17.876 -15.466 17.593  1.00 52.13  ? 56  ASP B CA  1 
ATOM   3024 C  C   . ASP B 1 56  ? -17.258 -16.521 16.676  1.00 53.15  ? 56  ASP B C   1 
ATOM   3025 O  O   . ASP B 1 56  ? -16.751 -17.525 17.209  1.00 53.88  ? 56  ASP B O   1 
ATOM   3026 C  CB  . ASP B 1 56  ? -19.404 -15.483 17.504  1.00 55.78  ? 56  ASP B CB  1 
ATOM   3027 C  CG  . ASP B 1 56  ? -19.991 -16.681 18.231  1.00 55.85  ? 56  ASP B CG  1 
ATOM   3028 O  OD1 . ASP B 1 56  ? -19.672 -16.837 19.435  1.00 52.48  ? 56  ASP B OD1 1 
ATOM   3029 O  OD2 . ASP B 1 56  ? -20.704 -17.482 17.577  1.00 49.66  ? 56  ASP B OD2 1 
ATOM   3030 N  N   . LEU B 1 57  ? -17.275 -16.323 15.356  1.00 51.93  ? 57  LEU B N   1 
ATOM   3031 C  CA  . LEU B 1 57  ? -16.694 -17.326 14.421  1.00 52.66  ? 57  LEU B CA  1 
ATOM   3032 C  C   . LEU B 1 57  ? -15.213 -17.583 14.743  1.00 52.33  ? 57  LEU B C   1 
ATOM   3033 O  O   . LEU B 1 57  ? -14.743 -18.701 14.421  1.00 53.00  ? 57  LEU B O   1 
ATOM   3034 C  CB  . LEU B 1 57  ? -16.836 -16.856 12.972  1.00 55.16  ? 57  LEU B CB  1 
ATOM   3035 C  CG  . LEU B 1 57  ? -18.252 -16.846 12.416  1.00 60.31  ? 57  LEU B CG  1 
ATOM   3036 C  CD1 . LEU B 1 57  ? -18.285 -16.125 11.078  1.00 59.64  ? 57  LEU B CD1 1 
ATOM   3037 C  CD2 . LEU B 1 57  ? -18.787 -18.265 12.283  1.00 63.80  ? 57  LEU B CD2 1 
ATOM   3038 N  N   . LEU B 1 58  ? -14.483 -16.596 15.284  1.00 51.56  ? 58  LEU B N   1 
ATOM   3039 C  CA  . LEU B 1 58  ? -13.004 -16.704 15.436  1.00 55.37  ? 58  LEU B CA  1 
ATOM   3040 C  C   . LEU B 1 58  ? -12.666 -17.435 16.747  1.00 55.25  ? 58  LEU B C   1 
ATOM   3041 O  O   . LEU B 1 58  ? -11.744 -18.279 16.728  1.00 57.30  ? 58  LEU B O   1 
ATOM   3042 C  CB  . LEU B 1 58  ? -12.349 -15.318 15.380  1.00 52.39  ? 58  LEU B CB  1 
ATOM   3043 C  CG  . LEU B 1 58  ? -10.830 -15.314 15.591  1.00 55.23  ? 58  LEU B CG  1 
ATOM   3044 C  CD1 . LEU B 1 58  ? -10.106 -16.047 14.466  1.00 56.79  ? 58  LEU B CD1 1 
ATOM   3045 C  CD2 . LEU B 1 58  ? -10.293 -13.900 15.731  1.00 57.70  ? 58  LEU B CD2 1 
ATOM   3046 N  N   . ILE B 1 59  ? -13.353 -17.124 17.851  1.00 60.70  ? 59  ILE B N   1 
ATOM   3047 C  CA  . ILE B 1 59  ? -13.129 -17.845 19.145  1.00 63.28  ? 59  ILE B CA  1 
ATOM   3048 C  C   . ILE B 1 59  ? -13.431 -19.331 18.913  1.00 58.37  ? 59  ILE B C   1 
ATOM   3049 O  O   . ILE B 1 59  ? -12.646 -20.154 19.388  1.00 62.93  ? 59  ILE B O   1 
ATOM   3050 C  CB  . ILE B 1 59  ? -13.921 -17.240 20.328  1.00 63.64  ? 59  ILE B CB  1 
ATOM   3051 C  CG1 . ILE B 1 59  ? -15.437 -17.376 20.164  1.00 67.35  ? 59  ILE B CG1 1 
ATOM   3052 C  CG2 . ILE B 1 59  ? -13.512 -15.795 20.573  1.00 59.33  ? 59  ILE B CG2 1 
ATOM   3053 C  CD1 . ILE B 1 59  ? -16.224 -16.972 21.396  1.00 71.23  ? 59  ILE B CD1 1 
ATOM   3054 N  N   . ARG B 1 60  ? -14.469 -19.639 18.130  1.00 58.36  ? 60  ARG B N   1 
ATOM   3055 C  CA  . ARG B 1 60  ? -14.823 -21.008 17.660  1.00 63.83  ? 60  ARG B CA  1 
ATOM   3056 C  C   . ARG B 1 60  ? -13.667 -21.660 16.889  1.00 59.10  ? 60  ARG B C   1 
ATOM   3057 O  O   . ARG B 1 60  ? -13.752 -22.863 16.688  1.00 55.44  ? 60  ARG B O   1 
ATOM   3058 C  CB  . ARG B 1 60  ? -16.020 -20.991 16.699  1.00 71.61  ? 60  ARG B CB  1 
ATOM   3059 C  CG  . ARG B 1 60  ? -17.376 -20.687 17.318  1.00 75.65  ? 60  ARG B CG  1 
ATOM   3060 C  CD  . ARG B 1 60  ? -18.382 -20.557 16.190  1.00 85.40  ? 60  ARG B CD  1 
ATOM   3061 N  NE  . ARG B 1 60  ? -19.769 -20.463 16.620  1.00 95.94  ? 60  ARG B NE  1 
ATOM   3062 C  CZ  . ARG B 1 60  ? -20.815 -20.418 15.793  1.00 109.31 ? 60  ARG B CZ  1 
ATOM   3063 N  NH1 . ARG B 1 60  ? -20.639 -20.450 14.480  1.00 108.72 ? 60  ARG B NH1 1 
ATOM   3064 N  NH2 . ARG B 1 60  ? -22.040 -20.337 16.289  1.00 114.99 ? 60  ARG B NH2 1 
ATOM   3065 N  N   . LYS B 1 61  ? -12.679 -20.901 16.397  1.00 64.59  ? 61  LYS B N   1 
ATOM   3066 C  CA  . LYS B 1 61  ? -11.557 -21.430 15.567  1.00 62.16  ? 61  LYS B CA  1 
ATOM   3067 C  C   . LYS B 1 61  ? -10.315 -21.655 16.430  1.00 61.08  ? 61  LYS B C   1 
ATOM   3068 O  O   . LYS B 1 61  ? -10.190 -21.004 17.502  1.00 61.43  ? 61  LYS B O   1 
ATOM   3069 C  CB  . LYS B 1 61  ? -11.158 -20.462 14.447  1.00 63.07  ? 61  LYS B CB  1 
ATOM   3070 C  CG  . LYS B 1 61  ? -12.228 -20.196 13.401  1.00 61.39  ? 61  LYS B CG  1 
ATOM   3071 C  CD  . LYS B 1 61  ? -12.261 -21.201 12.284  1.00 58.79  ? 61  LYS B CD  1 
ATOM   3072 C  CE  . LYS B 1 61  ? -13.629 -21.234 11.639  1.00 63.71  ? 61  LYS B CE  1 
ATOM   3073 N  NZ  . LYS B 1 61  ? -13.667 -22.149 10.478  1.00 65.41  ? 61  LYS B NZ  1 
ATOM   3074 N  N   . SER B 1 62  ? -9.415  -22.506 15.937  1.00 56.97  ? 62  SER B N   1 
ATOM   3075 C  CA  . SER B 1 62  ? -8.082  -22.769 16.528  1.00 62.49  ? 62  SER B CA  1 
ATOM   3076 C  C   . SER B 1 62  ? -6.995  -22.727 15.444  1.00 56.73  ? 62  SER B C   1 
ATOM   3077 O  O   . SER B 1 62  ? -7.325  -22.827 14.244  1.00 51.67  ? 62  SER B O   1 
ATOM   3078 C  CB  . SER B 1 62  ? -8.076  -24.086 17.243  1.00 69.67  ? 62  SER B CB  1 
ATOM   3079 O  OG  . SER B 1 62  ? -8.415  -25.124 16.340  1.00 77.67  ? 62  SER B OG  1 
ATOM   3080 N  N   . ASN B 1 63  ? -5.741  -22.625 15.890  1.00 51.93  ? 63  ASN B N   1 
ATOM   3081 C  CA  . ASN B 1 63  ? -4.513  -22.562 15.057  1.00 51.17  ? 63  ASN B CA  1 
ATOM   3082 C  C   . ASN B 1 63  ? -4.581  -23.588 13.922  1.00 54.86  ? 63  ASN B C   1 
ATOM   3083 O  O   . ASN B 1 63  ? -4.433  -23.201 12.751  1.00 54.36  ? 63  ASN B O   1 
ATOM   3084 C  CB  . ASN B 1 63  ? -3.274  -22.745 15.929  1.00 44.43  ? 63  ASN B CB  1 
ATOM   3085 C  CG  . ASN B 1 63  ? -3.018  -21.539 16.800  1.00 45.64  ? 63  ASN B CG  1 
ATOM   3086 O  OD1 . ASN B 1 63  ? -3.390  -20.426 16.441  1.00 46.77  ? 63  ASN B OD1 1 
ATOM   3087 N  ND2 . ASN B 1 63  ? -2.359  -21.733 17.928  1.00 46.87  ? 63  ASN B ND2 1 
ATOM   3088 N  N   . HIS B 1 64  ? -4.816  -24.849 14.267  1.00 63.99  ? 64  HIS B N   1 
ATOM   3089 C  CA  . HIS B 1 64  ? -4.859  -26.006 13.332  1.00 66.63  ? 64  HIS B CA  1 
ATOM   3090 C  C   . HIS B 1 64  ? -5.984  -25.846 12.290  1.00 63.07  ? 64  HIS B C   1 
ATOM   3091 O  O   . HIS B 1 64  ? -5.872  -26.504 11.237  1.00 64.41  ? 64  HIS B O   1 
ATOM   3092 C  CB  . HIS B 1 64  ? -4.971  -27.305 14.139  1.00 77.60  ? 64  HIS B CB  1 
ATOM   3093 C  CG  . HIS B 1 64  ? -5.971  -27.227 15.248  1.00 83.78  ? 64  HIS B CG  1 
ATOM   3094 N  ND1 . HIS B 1 64  ? -5.607  -26.934 16.555  1.00 87.35  ? 64  HIS B ND1 1 
ATOM   3095 C  CD2 . HIS B 1 64  ? -7.315  -27.370 15.247  1.00 87.89  ? 64  HIS B CD2 1 
ATOM   3096 C  CE1 . HIS B 1 64  ? -6.685  -26.924 17.315  1.00 89.32  ? 64  HIS B CE1 1 
ATOM   3097 N  NE2 . HIS B 1 64  ? -7.748  -27.186 16.537  1.00 89.29  ? 64  HIS B NE2 1 
ATOM   3098 N  N   . ASN B 1 65  ? -7.000  -24.997 12.529  1.00 55.13  ? 65  ASN B N   1 
ATOM   3099 C  CA  . ASN B 1 65  ? -8.036  -24.657 11.507  1.00 54.77  ? 65  ASN B CA  1 
ATOM   3100 C  C   . ASN B 1 65  ? -7.442  -23.860 10.339  1.00 50.91  ? 65  ASN B C   1 
ATOM   3101 O  O   . ASN B 1 65  ? -8.233  -23.492 9.457   1.00 49.49  ? 65  ASN B O   1 
ATOM   3102 C  CB  . ASN B 1 65  ? -9.163  -23.752 12.011  1.00 53.57  ? 65  ASN B CB  1 
ATOM   3103 C  CG  . ASN B 1 65  ? -10.094 -24.417 12.997  1.00 60.14  ? 65  ASN B CG  1 
ATOM   3104 O  OD1 . ASN B 1 65  ? -9.874  -24.365 14.208  1.00 66.11  ? 65  ASN B OD1 1 
ATOM   3105 N  ND2 . ASN B 1 65  ? -11.171 -24.985 12.489  1.00 48.10  ? 65  ASN B ND2 1 
ATOM   3106 N  N   . PHE B 1 66  ? -6.141  -23.541 10.359  1.00 50.56  ? 66  PHE B N   1 
ATOM   3107 C  CA  . PHE B 1 66  ? -5.490  -22.629 9.381   1.00 47.74  ? 66  PHE B CA  1 
ATOM   3108 C  C   . PHE B 1 66  ? -4.312  -23.346 8.729   1.00 45.10  ? 66  PHE B C   1 
ATOM   3109 O  O   . PHE B 1 66  ? -3.369  -23.680 9.444   1.00 49.37  ? 66  PHE B O   1 
ATOM   3110 C  CB  . PHE B 1 66  ? -5.063  -21.327 10.067  1.00 45.70  ? 66  PHE B CB  1 
ATOM   3111 C  CG  . PHE B 1 66  ? -6.215  -20.481 10.552  1.00 43.44  ? 66  PHE B CG  1 
ATOM   3112 C  CD1 . PHE B 1 66  ? -7.038  -19.823 9.657   1.00 41.74  ? 66  PHE B CD1 1 
ATOM   3113 C  CD2 . PHE B 1 66  ? -6.468  -20.329 11.905  1.00 43.62  ? 66  PHE B CD2 1 
ATOM   3114 C  CE1 . PHE B 1 66  ? -8.085  -19.036 10.108  1.00 44.08  ? 66  PHE B CE1 1 
ATOM   3115 C  CE2 . PHE B 1 66  ? -7.510  -19.533 12.354  1.00 43.53  ? 66  PHE B CE2 1 
ATOM   3116 C  CZ  . PHE B 1 66  ? -8.323  -18.894 11.456  1.00 43.03  ? 66  PHE B CZ  1 
ATOM   3117 N  N   . LEU B 1 67  ? -4.421  -23.607 7.425   1.00 45.71  ? 67  LEU B N   1 
ATOM   3118 C  CA  . LEU B 1 67  ? -3.347  -24.149 6.555   1.00 50.07  ? 67  LEU B CA  1 
ATOM   3119 C  C   . LEU B 1 67  ? -2.675  -22.986 5.818   1.00 50.47  ? 67  LEU B C   1 
ATOM   3120 O  O   . LEU B 1 67  ? -3.368  -22.311 5.009   1.00 43.04  ? 67  LEU B O   1 
ATOM   3121 C  CB  . LEU B 1 67  ? -3.962  -25.113 5.536   1.00 55.37  ? 67  LEU B CB  1 
ATOM   3122 C  CG  . LEU B 1 67  ? -4.570  -26.379 6.124   1.00 59.46  ? 67  LEU B CG  1 
ATOM   3123 C  CD1 . LEU B 1 67  ? -5.583  -26.998 5.172   1.00 59.03  ? 67  LEU B CD1 1 
ATOM   3124 C  CD2 . LEU B 1 67  ? -3.467  -27.368 6.478   1.00 61.37  ? 67  LEU B CD2 1 
ATOM   3125 N  N   . VAL B 1 68  ? -1.390  -22.768 6.087   1.00 45.28  ? 68  VAL B N   1 
ATOM   3126 C  CA  . VAL B 1 68  ? -0.565  -21.733 5.408   1.00 43.20  ? 68  VAL B CA  1 
ATOM   3127 C  C   . VAL B 1 68  ? 0.513   -22.459 4.615   1.00 43.65  ? 68  VAL B C   1 
ATOM   3128 O  O   . VAL B 1 68  ? 1.273   -23.209 5.222   1.00 42.10  ? 68  VAL B O   1 
ATOM   3129 C  CB  . VAL B 1 68  ? 0.042   -20.725 6.394   1.00 39.26  ? 68  VAL B CB  1 
ATOM   3130 C  CG1 . VAL B 1 68  ? 0.796   -19.616 5.658   1.00 39.66  ? 68  VAL B CG1 1 
ATOM   3131 C  CG2 . VAL B 1 68  ? -1.018  -20.143 7.311   1.00 38.44  ? 68  VAL B CG2 1 
ATOM   3132 N  N   . GLN B 1 69  ? 0.575   -22.193 3.309   1.00 47.07  ? 69  GLN B N   1 
ATOM   3133 C  CA  . GLN B 1 69  ? 1.508   -22.856 2.367   1.00 51.96  ? 69  GLN B CA  1 
ATOM   3134 C  C   . GLN B 1 69  ? 2.377   -21.779 1.704   1.00 48.17  ? 69  GLN B C   1 
ATOM   3135 O  O   . GLN B 1 69  ? 1.809   -20.919 1.012   1.00 42.48  ? 69  GLN B O   1 
ATOM   3136 C  CB  . GLN B 1 69  ? 0.692   -23.694 1.380   1.00 57.96  ? 69  GLN B CB  1 
ATOM   3137 C  CG  . GLN B 1 69  ? 1.555   -24.585 0.497   1.00 72.13  ? 69  GLN B CG  1 
ATOM   3138 C  CD  . GLN B 1 69  ? 1.045   -26.006 0.387   1.00 78.01  ? 69  GLN B CD  1 
ATOM   3139 O  OE1 . GLN B 1 69  ? -0.147  -26.252 0.181   1.00 77.16  ? 69  GLN B OE1 1 
ATOM   3140 N  NE2 . GLN B 1 69  ? 1.957   -26.960 0.528   1.00 73.55  ? 69  GLN B NE2 1 
ATOM   3141 N  N   . ALA B 1 70  ? 3.684   -21.796 1.980   1.00 43.17  ? 70  ALA B N   1 
ATOM   3142 C  CA  . ALA B 1 70  ? 4.727   -21.001 1.294   1.00 45.23  ? 70  ALA B CA  1 
ATOM   3143 C  C   . ALA B 1 70  ? 5.400   -21.889 0.243   1.00 53.82  ? 70  ALA B C   1 
ATOM   3144 O  O   . ALA B 1 70  ? 6.340   -22.646 0.608   1.00 57.09  ? 70  ALA B O   1 
ATOM   3145 C  CB  . ALA B 1 70  ? 5.726   -20.457 2.281   1.00 43.02  ? 70  ALA B CB  1 
ATOM   3146 N  N   . GLY B 1 71  ? 4.932   -21.801 -1.007  1.00 54.58  ? 71  GLY B N   1 
ATOM   3147 C  CA  . GLY B 1 71  ? 5.318   -22.703 -2.108  1.00 55.14  ? 71  GLY B CA  1 
ATOM   3148 C  C   . GLY B 1 71  ? 4.967   -24.146 -1.784  1.00 60.64  ? 71  GLY B C   1 
ATOM   3149 O  O   . GLY B 1 71  ? 3.760   -24.474 -1.784  1.00 59.62  ? 71  GLY B O   1 
ATOM   3150 N  N   . ASN B 1 72  ? 5.978   -24.982 -1.512  1.00 70.31  ? 72  ASN B N   1 
ATOM   3151 C  CA  . ASN B 1 72  ? 5.808   -26.436 -1.225  1.00 81.25  ? 72  ASN B CA  1 
ATOM   3152 C  C   . ASN B 1 72  ? 6.156   -26.738 0.244   1.00 79.11  ? 72  ASN B C   1 
ATOM   3153 O  O   . ASN B 1 72  ? 6.545   -27.887 0.543   1.00 84.17  ? 72  ASN B O   1 
ATOM   3154 C  CB  . ASN B 1 72  ? 6.640   -27.298 -2.185  1.00 86.04  ? 72  ASN B CB  1 
ATOM   3155 C  CG  . ASN B 1 72  ? 6.070   -28.689 -2.376  1.00 91.69  ? 72  ASN B CG  1 
ATOM   3156 O  OD1 . ASN B 1 72  ? 4.861   -28.892 -2.259  1.00 93.37  ? 72  ASN B OD1 1 
ATOM   3157 N  ND2 . ASN B 1 72  ? 6.927   -29.651 -2.683  1.00 96.87  ? 72  ASN B ND2 1 
ATOM   3158 N  N   . VAL B 1 73  ? 6.011   -25.750 1.130   1.00 70.65  ? 73  VAL B N   1 
ATOM   3159 C  CA  . VAL B 1 73  ? 6.276   -25.875 2.592   1.00 64.41  ? 73  VAL B CA  1 
ATOM   3160 C  C   . VAL B 1 73  ? 5.012   -25.448 3.345   1.00 63.78  ? 73  VAL B C   1 
ATOM   3161 O  O   . VAL B 1 73  ? 4.490   -24.339 3.059   1.00 55.75  ? 73  VAL B O   1 
ATOM   3162 C  CB  . VAL B 1 73  ? 7.486   -25.023 3.015   1.00 63.38  ? 73  VAL B CB  1 
ATOM   3163 C  CG1 . VAL B 1 73  ? 7.732   -25.128 4.511   1.00 62.97  ? 73  VAL B CG1 1 
ATOM   3164 C  CG2 . VAL B 1 73  ? 8.738   -25.376 2.218   1.00 61.28  ? 73  VAL B CG2 1 
ATOM   3165 N  N   . GLN B 1 74  ? 4.531   -26.294 4.258   1.00 57.07  ? 74  GLN B N   1 
ATOM   3166 C  CA  . GLN B 1 74  ? 3.489   -25.925 5.246   1.00 58.87  ? 74  GLN B CA  1 
ATOM   3167 C  C   . GLN B 1 74  ? 4.200   -25.113 6.323   1.00 53.32  ? 74  GLN B C   1 
ATOM   3168 O  O   . GLN B 1 74  ? 5.305   -25.512 6.707   1.00 57.86  ? 74  GLN B O   1 
ATOM   3169 C  CB  . GLN B 1 74  ? 2.782   -27.152 5.825   1.00 64.84  ? 74  GLN B CB  1 
ATOM   3170 C  CG  . GLN B 1 74  ? 1.964   -27.945 4.808   1.00 75.19  ? 74  GLN B CG  1 
ATOM   3171 C  CD  . GLN B 1 74  ? 0.827   -27.165 4.186   1.00 88.74  ? 74  GLN B CD  1 
ATOM   3172 O  OE1 . GLN B 1 74  ? 0.772   -26.987 2.970   1.00 101.06 ? 74  GLN B OE1 1 
ATOM   3173 N  NE2 . GLN B 1 74  ? -0.101  -26.699 5.012   1.00 95.43  ? 74  GLN B NE2 1 
ATOM   3174 N  N   . LEU B 1 75  ? 3.653   -23.954 6.679   1.00 51.92  ? 75  LEU B N   1 
ATOM   3175 C  CA  . LEU B 1 75  ? 4.022   -23.212 7.909   1.00 53.25  ? 75  LEU B CA  1 
ATOM   3176 C  C   . LEU B 1 75  ? 3.097   -23.693 9.030   1.00 56.40  ? 75  LEU B C   1 
ATOM   3177 O  O   . LEU B 1 75  ? 1.892   -23.938 8.736   1.00 56.86  ? 75  LEU B O   1 
ATOM   3178 C  CB  . LEU B 1 75  ? 3.871   -21.705 7.676   1.00 55.09  ? 75  LEU B CB  1 
ATOM   3179 C  CG  . LEU B 1 75  ? 4.708   -21.128 6.539   1.00 53.20  ? 75  LEU B CG  1 
ATOM   3180 C  CD1 . LEU B 1 75  ? 4.523   -19.622 6.440   1.00 53.78  ? 75  LEU B CD1 1 
ATOM   3181 C  CD2 . LEU B 1 75  ? 6.176   -21.461 6.738   1.00 56.46  ? 75  LEU B CD2 1 
ATOM   3182 N  N   . ARG B 1 76  ? 3.650   -23.844 10.241  1.00 53.98  ? 76  ARG B N   1 
ATOM   3183 C  CA  . ARG B 1 76  ? 2.881   -24.115 11.482  1.00 50.92  ? 76  ARG B CA  1 
ATOM   3184 C  C   . ARG B 1 76  ? 2.380   -22.773 12.029  1.00 43.08  ? 76  ARG B C   1 
ATOM   3185 O  O   . ARG B 1 76  ? 3.236   -21.887 12.360  1.00 39.16  ? 76  ARG B O   1 
ATOM   3186 C  CB  . ARG B 1 76  ? 3.721   -24.863 12.529  1.00 57.57  ? 76  ARG B CB  1 
ATOM   3187 C  CG  . ARG B 1 76  ? 2.895   -25.566 13.600  1.00 64.98  ? 76  ARG B CG  1 
ATOM   3188 C  CD  . ARG B 1 76  ? 3.720   -26.295 14.644  1.00 71.78  ? 76  ARG B CD  1 
ATOM   3189 N  NE  . ARG B 1 76  ? 4.389   -27.488 14.122  1.00 82.65  ? 76  ARG B NE  1 
ATOM   3190 C  CZ  . ARG B 1 76  ? 3.816   -28.684 13.918  1.00 84.43  ? 76  ARG B CZ  1 
ATOM   3191 N  NH1 . ARG B 1 76  ? 2.528   -28.876 14.165  1.00 85.04  ? 76  ARG B NH1 1 
ATOM   3192 N  NH2 . ARG B 1 76  ? 4.541   -29.692 13.462  1.00 80.08  ? 76  ARG B NH2 1 
ATOM   3193 N  N   . VAL B 1 77  ? 1.054   -22.641 12.113  1.00 40.26  ? 77  VAL B N   1 
ATOM   3194 C  CA  . VAL B 1 77  ? 0.346   -21.511 12.781  1.00 39.90  ? 77  VAL B CA  1 
ATOM   3195 C  C   . VAL B 1 77  ? 0.375   -21.754 14.291  1.00 42.20  ? 77  VAL B C   1 
ATOM   3196 O  O   . VAL B 1 77  ? -0.153  -22.773 14.728  1.00 43.59  ? 77  VAL B O   1 
ATOM   3197 C  CB  . VAL B 1 77  ? -1.096  -21.349 12.267  1.00 42.08  ? 77  VAL B CB  1 
ATOM   3198 C  CG1 . VAL B 1 77  ? -1.877  -20.302 13.051  1.00 43.40  ? 77  VAL B CG1 1 
ATOM   3199 C  CG2 . VAL B 1 77  ? -1.130  -21.025 10.782  1.00 44.80  ? 77  VAL B CG2 1 
ATOM   3200 N  N   . ILE B 1 78  ? 0.941   -20.816 15.048  1.00 42.62  ? 78  ILE B N   1 
ATOM   3201 C  CA  . ILE B 1 78  ? 1.086   -20.911 16.525  1.00 41.40  ? 78  ILE B CA  1 
ATOM   3202 C  C   . ILE B 1 78  ? 0.254   -19.817 17.215  1.00 45.17  ? 78  ILE B C   1 
ATOM   3203 O  O   . ILE B 1 78  ? 0.291   -19.741 18.460  1.00 44.69  ? 78  ILE B O   1 
ATOM   3204 C  CB  . ILE B 1 78  ? 2.580   -20.870 16.894  1.00 43.12  ? 78  ILE B CB  1 
ATOM   3205 C  CG1 . ILE B 1 78  ? 3.219   -19.507 16.623  1.00 46.54  ? 78  ILE B CG1 1 
ATOM   3206 C  CG2 . ILE B 1 78  ? 3.341   -21.982 16.184  1.00 44.78  ? 78  ILE B CG2 1 
ATOM   3207 C  CD1 . ILE B 1 78  ? 4.513   -19.274 17.391  1.00 43.53  ? 78  ILE B CD1 1 
ATOM   3208 N  N   . GLY B 1 79  ? -0.489  -18.995 16.464  1.00 41.05  ? 79  GLY B N   1 
ATOM   3209 C  CA  . GLY B 1 79  ? -1.396  -17.997 17.060  1.00 37.81  ? 79  GLY B CA  1 
ATOM   3210 C  C   . GLY B 1 79  ? -2.278  -17.351 16.014  1.00 38.26  ? 79  GLY B C   1 
ATOM   3211 O  O   . GLY B 1 79  ? -1.946  -17.401 14.820  1.00 35.72  ? 79  GLY B O   1 
ATOM   3212 N  N   . HIS B 1 80  ? -3.388  -16.775 16.439  1.00 38.65  ? 80  HIS B N   1 
ATOM   3213 C  CA  . HIS B 1 80  ? -4.364  -16.123 15.536  1.00 41.15  ? 80  HIS B CA  1 
ATOM   3214 C  C   . HIS B 1 80  ? -4.988  -14.973 16.304  1.00 41.40  ? 80  HIS B C   1 
ATOM   3215 O  O   . HIS B 1 80  ? -5.363  -15.160 17.471  1.00 41.62  ? 80  HIS B O   1 
ATOM   3216 C  CB  . HIS B 1 80  ? -5.410  -17.105 14.997  1.00 43.24  ? 80  HIS B CB  1 
ATOM   3217 C  CG  . HIS B 1 80  ? -6.251  -17.721 16.061  1.00 49.19  ? 80  HIS B CG  1 
ATOM   3218 N  ND1 . HIS B 1 80  ? -5.939  -18.943 16.641  1.00 47.89  ? 80  HIS B ND1 1 
ATOM   3219 C  CD2 . HIS B 1 80  ? -7.380  -17.287 16.668  1.00 53.72  ? 80  HIS B CD2 1 
ATOM   3220 C  CE1 . HIS B 1 80  ? -6.843  -19.230 17.561  1.00 49.71  ? 80  HIS B CE1 1 
ATOM   3221 N  NE2 . HIS B 1 80  ? -7.741  -18.232 17.597  1.00 53.91  ? 80  HIS B NE2 1 
ATOM   3222 N  N   . SER B 1 81  ? -5.042  -13.807 15.688  1.00 37.27  ? 81  SER B N   1 
ATOM   3223 C  CA  . SER B 1 81  ? -5.921  -12.711 16.149  1.00 34.43  ? 81  SER B CA  1 
ATOM   3224 C  C   . SER B 1 81  ? -6.375  -11.909 14.943  1.00 36.15  ? 81  SER B C   1 
ATOM   3225 O  O   . SER B 1 81  ? -5.997  -12.245 13.793  1.00 34.66  ? 81  SER B O   1 
ATOM   3226 C  CB  . SER B 1 81  ? -5.249  -11.838 17.161  1.00 33.00  ? 81  SER B CB  1 
ATOM   3227 O  OG  . SER B 1 81  ? -4.087  -11.274 16.600  1.00 35.50  ? 81  SER B OG  1 
ATOM   3228 N  N   . MET B 1 82  ? -7.229  -10.938 15.237  1.00 36.37  ? 82  MET B N   1 
ATOM   3229 C  CA  . MET B 1 82  ? -7.912  -10.060 14.273  1.00 36.83  ? 82  MET B CA  1 
ATOM   3230 C  C   . MET B 1 82  ? -7.556  -8.611  14.633  1.00 34.50  ? 82  MET B C   1 
ATOM   3231 O  O   . MET B 1 82  ? -7.418  -8.307  15.812  1.00 34.60  ? 82  MET B O   1 
ATOM   3232 C  CB  . MET B 1 82  ? -9.409  -10.329 14.404  1.00 36.01  ? 82  MET B CB  1 
ATOM   3233 C  CG  . MET B 1 82  ? -10.224 -9.922  13.245  1.00 38.56  ? 82  MET B CG  1 
ATOM   3234 S  SD  . MET B 1 82  ? -11.949 -10.375 13.569  1.00 46.35  ? 82  MET B SD  1 
ATOM   3235 C  CE  . MET B 1 82  ? -11.855 -12.103 13.103  1.00 45.21  ? 82  MET B CE  1 
ATOM   3236 N  N   . GLN B 1 83  ? -7.277  -7.793  13.632  1.00 33.21  ? 83  GLN B N   1 
ATOM   3237 C  CA  . GLN B 1 83  ? -7.199  -6.324  13.739  1.00 31.46  ? 83  GLN B CA  1 
ATOM   3238 C  C   . GLN B 1 83  ? -8.121  -5.774  12.658  1.00 29.30  ? 83  GLN B C   1 
ATOM   3239 O  O   . GLN B 1 83  ? -7.870  -6.029  11.450  1.00 26.64  ? 83  GLN B O   1 
ATOM   3240 C  CB  . GLN B 1 83  ? -5.775  -5.817  13.566  1.00 34.84  ? 83  GLN B CB  1 
ATOM   3241 C  CG  . GLN B 1 83  ? -5.674  -4.310  13.720  1.00 34.50  ? 83  GLN B CG  1 
ATOM   3242 C  CD  . GLN B 1 83  ? -4.267  -3.828  13.501  1.00 40.20  ? 83  GLN B CD  1 
ATOM   3243 O  OE1 . GLN B 1 83  ? -3.394  -4.570  13.056  1.00 37.82  ? 83  GLN B OE1 1 
ATOM   3244 N  NE2 . GLN B 1 83  ? -4.043  -2.565  13.811  1.00 40.12  ? 83  GLN B NE2 1 
ATOM   3245 N  N   . ASN B 1 84  ? -9.228  -5.184  13.088  1.00 28.74  ? 84  ASN B N   1 
ATOM   3246 C  CA  . ASN B 1 84  ? -10.257 -4.686  12.158  1.00 26.15  ? 84  ASN B CA  1 
ATOM   3247 C  C   . ASN B 1 84  ? -10.625 -5.854  11.235  1.00 26.26  ? 84  ASN B C   1 
ATOM   3248 O  O   . ASN B 1 84  ? -10.934 -6.963  11.759  1.00 23.40  ? 84  ASN B O   1 
ATOM   3249 C  CB  . ASN B 1 84  ? -9.703  -3.415  11.515  1.00 25.99  ? 84  ASN B CB  1 
ATOM   3250 C  CG  . ASN B 1 84  ? -9.326  -2.379  12.552  1.00 31.31  ? 84  ASN B CG  1 
ATOM   3251 O  OD1 . ASN B 1 84  ? -10.147 -2.010  13.398  1.00 29.27  ? 84  ASN B OD1 1 
ATOM   3252 N  ND2 . ASN B 1 84  ? -8.093  -1.887  12.489  1.00 29.68  ? 84  ASN B ND2 1 
ATOM   3253 N  N   . CYS B 1 85  ? -10.523 -5.674  9.911   1.00 26.87  ? 85  CYS B N   1 
ATOM   3254 C  CA  . CYS B 1 85  ? -10.973 -6.677  8.913   1.00 27.87  ? 85  CYS B CA  1 
ATOM   3255 C  C   . CYS B 1 85  ? -9.826  -7.580  8.441   1.00 26.71  ? 85  CYS B C   1 
ATOM   3256 O  O   . CYS B 1 85  ? -10.058 -8.373  7.528   1.00 26.79  ? 85  CYS B O   1 
ATOM   3257 C  CB  . CYS B 1 85  ? -11.641 -6.012  7.718   1.00 27.68  ? 85  CYS B CB  1 
ATOM   3258 S  SG  . CYS B 1 85  ? -13.108 -5.063  8.205   1.00 27.39  ? 85  CYS B SG  1 
ATOM   3259 N  N   . VAL B 1 86  ? -8.665  -7.513  9.079   1.00 29.00  ? 86  VAL B N   1 
ATOM   3260 C  CA  . VAL B 1 86  ? -7.491  -8.363  8.745   1.00 28.54  ? 86  VAL B CA  1 
ATOM   3261 C  C   . VAL B 1 86  ? -7.277  -9.404  9.851   1.00 30.14  ? 86  VAL B C   1 
ATOM   3262 O  O   . VAL B 1 86  ? -7.338  -9.041  11.047  1.00 29.37  ? 86  VAL B O   1 
ATOM   3263 C  CB  . VAL B 1 86  ? -6.266  -7.462  8.506   1.00 31.33  ? 86  VAL B CB  1 
ATOM   3264 C  CG1 . VAL B 1 86  ? -4.949  -8.144  8.798   1.00 32.92  ? 86  VAL B CG1 1 
ATOM   3265 C  CG2 . VAL B 1 86  ? -6.314  -6.945  7.086   1.00 32.89  ? 86  VAL B CG2 1 
ATOM   3266 N  N   . LEU B 1 87  ? -7.065  -10.651 9.431   1.00 29.79  ? 87  LEU B N   1 
ATOM   3267 C  CA  . LEU B 1 87  ? -6.639  -11.807 10.259  1.00 29.27  ? 87  LEU B CA  1 
ATOM   3268 C  C   . LEU B 1 87  ? -5.107  -11.865 10.288  1.00 29.54  ? 87  LEU B C   1 
ATOM   3269 O  O   . LEU B 1 87  ? -4.498  -11.820 9.190   1.00 29.23  ? 87  LEU B O   1 
ATOM   3270 C  CB  . LEU B 1 87  ? -7.223  -13.070 9.624   1.00 31.14  ? 87  LEU B CB  1 
ATOM   3271 C  CG  . LEU B 1 87  ? -7.172  -14.318 10.494  1.00 37.51  ? 87  LEU B CG  1 
ATOM   3272 C  CD1 . LEU B 1 87  ? -8.147  -14.206 11.660  1.00 38.50  ? 87  LEU B CD1 1 
ATOM   3273 C  CD2 . LEU B 1 87  ? -7.461  -15.556 9.667   1.00 38.22  ? 87  LEU B CD2 1 
ATOM   3274 N  N   . LYS B 1 88  ? -4.512  -11.923 11.487  1.00 26.88  ? 88  LYS B N   1 
ATOM   3275 C  CA  . LYS B 1 88  ? -3.052  -12.091 11.690  1.00 29.19  ? 88  LYS B CA  1 
ATOM   3276 C  C   . LYS B 1 88  ? -2.774  -13.513 12.192  1.00 30.57  ? 88  LYS B C   1 
ATOM   3277 O  O   . LYS B 1 88  ? -3.264  -13.896 13.272  1.00 34.39  ? 88  LYS B O   1 
ATOM   3278 C  CB  . LYS B 1 88  ? -2.531  -11.026 12.644  1.00 30.41  ? 88  LYS B CB  1 
ATOM   3279 C  CG  . LYS B 1 88  ? -2.818  -9.602  12.188  1.00 34.61  ? 88  LYS B CG  1 
ATOM   3280 C  CD  . LYS B 1 88  ? -2.046  -8.582  12.939  1.00 35.56  ? 88  LYS B CD  1 
ATOM   3281 C  CE  . LYS B 1 88  ? -2.515  -8.494  14.359  1.00 41.13  ? 88  LYS B CE  1 
ATOM   3282 N  NZ  . LYS B 1 88  ? -1.565  -7.712  15.170  1.00 45.41  ? 88  LYS B NZ  1 
ATOM   3283 N  N   . LEU B 1 89  ? -2.092  -14.313 11.394  1.00 31.26  ? 89  LEU B N   1 
ATOM   3284 C  CA  . LEU B 1 89  ? -1.740  -15.695 11.783  1.00 31.99  ? 89  LEU B CA  1 
ATOM   3285 C  C   . LEU B 1 89  ? -0.273  -15.714 12.160  1.00 35.90  ? 89  LEU B C   1 
ATOM   3286 O  O   . LEU B 1 89  ? 0.572   -15.508 11.264  1.00 35.82  ? 89  LEU B O   1 
ATOM   3287 C  CB  . LEU B 1 89  ? -2.034  -16.633 10.627  1.00 31.90  ? 89  LEU B CB  1 
ATOM   3288 C  CG  . LEU B 1 89  ? -3.519  -16.775 10.300  1.00 33.63  ? 89  LEU B CG  1 
ATOM   3289 C  CD1 . LEU B 1 89  ? -3.723  -17.605 9.039   1.00 34.32  ? 89  LEU B CD1 1 
ATOM   3290 C  CD2 . LEU B 1 89  ? -4.274  -17.382 11.468  1.00 35.22  ? 89  LEU B CD2 1 
ATOM   3291 N  N   . LYS B 1 90  ? 0.013   -15.895 13.449  1.00 34.75  ? 90  LYS B N   1 
ATOM   3292 C  CA  . LYS B 1 90  ? 1.409   -16.022 13.910  1.00 38.28  ? 90  LYS B CA  1 
ATOM   3293 C  C   . LYS B 1 90  ? 1.870   -17.423 13.521  1.00 39.12  ? 90  LYS B C   1 
ATOM   3294 O  O   . LYS B 1 90  ? 1.079   -18.370 13.741  1.00 35.21  ? 90  LYS B O   1 
ATOM   3295 C  CB  . LYS B 1 90  ? 1.586   -15.784 15.407  1.00 39.81  ? 90  LYS B CB  1 
ATOM   3296 C  CG  . LYS B 1 90  ? 3.040   -15.527 15.765  1.00 46.28  ? 90  LYS B CG  1 
ATOM   3297 C  CD  . LYS B 1 90  ? 3.312   -15.385 17.228  1.00 54.24  ? 90  LYS B CD  1 
ATOM   3298 C  CE  . LYS B 1 90  ? 4.762   -15.053 17.503  1.00 58.72  ? 90  LYS B CE  1 
ATOM   3299 N  NZ  . LYS B 1 90  ? 5.058   -15.153 18.951  1.00 64.86  ? 90  LYS B NZ  1 
ATOM   3300 N  N   . VAL B 1 91  ? 3.063   -17.505 12.921  1.00 38.40  ? 91  VAL B N   1 
ATOM   3301 C  CA  . VAL B 1 91  ? 3.694   -18.756 12.412  1.00 39.35  ? 91  VAL B CA  1 
ATOM   3302 C  C   . VAL B 1 91  ? 5.010   -18.974 13.163  1.00 38.81  ? 91  VAL B C   1 
ATOM   3303 O  O   . VAL B 1 91  ? 5.531   -18.012 13.772  1.00 39.00  ? 91  VAL B O   1 
ATOM   3304 C  CB  . VAL B 1 91  ? 3.897   -18.717 10.880  1.00 41.09  ? 91  VAL B CB  1 
ATOM   3305 C  CG1 . VAL B 1 91  ? 2.570   -18.837 10.153  1.00 38.53  ? 91  VAL B CG1 1 
ATOM   3306 C  CG2 . VAL B 1 91  ? 4.670   -17.486 10.395  1.00 39.36  ? 91  VAL B CG2 1 
ATOM   3307 N  N   . ASP B 1 92  ? 5.537   -20.197 13.101  1.00 43.46  ? 92  ASP B N   1 
ATOM   3308 C  CA  . ASP B 1 92  ? 6.753   -20.611 13.850  1.00 47.70  ? 92  ASP B CA  1 
ATOM   3309 C  C   . ASP B 1 92  ? 8.027   -20.064 13.187  1.00 50.50  ? 92  ASP B C   1 
ATOM   3310 O  O   . ASP B 1 92  ? 9.076   -20.154 13.836  1.00 55.40  ? 92  ASP B O   1 
ATOM   3311 C  CB  . ASP B 1 92  ? 6.839   -22.133 13.969  1.00 50.93  ? 92  ASP B CB  1 
ATOM   3312 C  CG  . ASP B 1 92  ? 6.794   -22.864 12.635  1.00 53.68  ? 92  ASP B CG  1 
ATOM   3313 O  OD1 . ASP B 1 92  ? 7.110   -22.239 11.599  1.00 59.08  ? 92  ASP B OD1 1 
ATOM   3314 O  OD2 . ASP B 1 92  ? 6.415   -24.045 12.636  1.00 56.38  ? 92  ASP B OD2 1 
ATOM   3315 N  N   . THR B 1 93  ? 7.949   -19.536 11.954  1.00 47.67  ? 93  THR B N   1 
ATOM   3316 C  CA  . THR B 1 93  ? 9.116   -19.179 11.102  1.00 41.77  ? 93  THR B CA  1 
ATOM   3317 C  C   . THR B 1 93  ? 9.001   -17.735 10.589  1.00 39.96  ? 93  THR B C   1 
ATOM   3318 O  O   . THR B 1 93  ? 7.981   -17.409 9.976   1.00 35.27  ? 93  THR B O   1 
ATOM   3319 C  CB  . THR B 1 93  ? 9.208   -20.111 9.893   1.00 44.83  ? 93  THR B CB  1 
ATOM   3320 O  OG1 . THR B 1 93  ? 9.139   -21.429 10.436  1.00 44.66  ? 93  THR B OG1 1 
ATOM   3321 C  CG2 . THR B 1 93  ? 10.465  -19.899 9.072   1.00 46.03  ? 93  THR B CG2 1 
ATOM   3322 N  N   . ALA B 1 94  ? 10.034  -16.926 10.822  1.00 34.97  ? 94  ALA B N   1 
ATOM   3323 C  CA  . ALA B 1 94  ? 10.210  -15.594 10.221  1.00 36.34  ? 94  ALA B CA  1 
ATOM   3324 C  C   . ALA B 1 94  ? 10.533  -15.773 8.730   1.00 39.92  ? 94  ALA B C   1 
ATOM   3325 O  O   . ALA B 1 94  ? 11.353  -16.651 8.381   1.00 39.79  ? 94  ALA B O   1 
ATOM   3326 C  CB  . ALA B 1 94  ? 11.264  -14.834 10.963  1.00 34.54  ? 94  ALA B CB  1 
ATOM   3327 N  N   . ASN B 1 95  ? 9.826   -15.051 7.863   1.00 37.26  ? 95  ASN B N   1 
ATOM   3328 C  CA  . ASN B 1 95  ? 10.060  -15.117 6.401   1.00 33.23  ? 95  ASN B CA  1 
ATOM   3329 C  C   . ASN B 1 95  ? 11.493  -14.661 6.154   1.00 32.85  ? 95  ASN B C   1 
ATOM   3330 O  O   . ASN B 1 95  ? 11.784  -13.481 6.358   1.00 32.23  ? 95  ASN B O   1 
ATOM   3331 C  CB  . ASN B 1 95  ? 9.042   -14.261 5.638   1.00 35.14  ? 95  ASN B CB  1 
ATOM   3332 C  CG  . ASN B 1 95  ? 9.196   -14.389 4.137   1.00 36.13  ? 95  ASN B CG  1 
ATOM   3333 O  OD1 . ASN B 1 95  ? 10.148  -15.021 3.681   1.00 30.68  ? 95  ASN B OD1 1 
ATOM   3334 N  ND2 . ASN B 1 95  ? 8.282   -13.791 3.379   1.00 30.20  ? 95  ASN B ND2 1 
ATOM   3335 N  N   . PRO B 1 96  ? 12.423  -15.541 5.697   1.00 33.23  ? 96  PRO B N   1 
ATOM   3336 C  CA  . PRO B 1 96  ? 13.792  -15.117 5.398   1.00 36.58  ? 96  PRO B CA  1 
ATOM   3337 C  C   . PRO B 1 96  ? 13.861  -14.118 4.228   1.00 35.95  ? 96  PRO B C   1 
ATOM   3338 O  O   . PRO B 1 96  ? 14.903  -13.511 4.050   1.00 37.06  ? 96  PRO B O   1 
ATOM   3339 C  CB  . PRO B 1 96  ? 14.505  -16.433 5.033   1.00 36.25  ? 96  PRO B CB  1 
ATOM   3340 C  CG  . PRO B 1 96  ? 13.392  -17.290 4.468   1.00 38.02  ? 96  PRO B CG  1 
ATOM   3341 C  CD  . PRO B 1 96  ? 12.201  -16.955 5.342   1.00 35.95  ? 96  PRO B CD  1 
ATOM   3342 N  N   . LYS B 1 97  ? 12.775  -13.950 3.468   1.00 33.91  ? 97  LYS B N   1 
ATOM   3343 C  CA  . LYS B 1 97  ? 12.704  -12.984 2.338   1.00 35.27  ? 97  LYS B CA  1 
ATOM   3344 C  C   . LYS B 1 97  ? 11.966  -11.707 2.753   1.00 35.96  ? 97  LYS B C   1 
ATOM   3345 O  O   . LYS B 1 97  ? 11.690  -10.901 1.863   1.00 35.17  ? 97  LYS B O   1 
ATOM   3346 C  CB  . LYS B 1 97  ? 12.012  -13.616 1.130   1.00 36.47  ? 97  LYS B CB  1 
ATOM   3347 C  CG  . LYS B 1 97  ? 12.582  -14.957 0.704   1.00 41.27  ? 97  LYS B CG  1 
ATOM   3348 C  CD  . LYS B 1 97  ? 12.539  -15.179 -0.777  1.00 44.48  ? 97  LYS B CD  1 
ATOM   3349 C  CE  . LYS B 1 97  ? 12.636  -16.639 -1.165  1.00 49.40  ? 97  LYS B CE  1 
ATOM   3350 N  NZ  . LYS B 1 97  ? 11.321  -17.309 -1.018  1.00 52.62  ? 97  LYS B NZ  1 
ATOM   3351 N  N   . THR B 1 98  ? 11.683  -11.498 4.042   1.00 32.90  ? 98  THR B N   1 
ATOM   3352 C  CA  . THR B 1 98  ? 11.059  -10.242 4.527   1.00 31.81  ? 98  THR B CA  1 
ATOM   3353 C  C   . THR B 1 98  ? 11.914  -9.056  4.079   1.00 33.11  ? 98  THR B C   1 
ATOM   3354 O  O   . THR B 1 98  ? 13.091  -8.937  4.443   1.00 29.22  ? 98  THR B O   1 
ATOM   3355 C  CB  . THR B 1 98  ? 10.870  -10.202 6.047   1.00 31.72  ? 98  THR B CB  1 
ATOM   3356 O  OG1 . THR B 1 98  ? 10.086  -11.328 6.426   1.00 31.58  ? 98  THR B OG1 1 
ATOM   3357 C  CG2 . THR B 1 98  ? 10.193  -8.926  6.506   1.00 34.48  ? 98  THR B CG2 1 
ATOM   3358 N  N   . PRO B 1 99  ? 11.360  -8.107  3.291   1.00 27.48  ? 99  PRO B N   1 
ATOM   3359 C  CA  . PRO B 1 99  ? 12.108  -6.894  2.965   1.00 28.17  ? 99  PRO B CA  1 
ATOM   3360 C  C   . PRO B 1 99  ? 11.992  -5.825  4.057   1.00 30.24  ? 99  PRO B C   1 
ATOM   3361 O  O   . PRO B 1 99  ? 11.177  -5.969  4.934   1.00 32.01  ? 99  PRO B O   1 
ATOM   3362 C  CB  . PRO B 1 99  ? 11.375  -6.413  1.722   1.00 29.35  ? 99  PRO B CB  1 
ATOM   3363 C  CG  . PRO B 1 99  ? 9.921   -6.786  2.022   1.00 30.59  ? 99  PRO B CG  1 
ATOM   3364 C  CD  . PRO B 1 99  ? 10.017  -8.138  2.697   1.00 29.23  ? 99  PRO B CD  1 
ATOM   3365 N  N   . LYS B 1 100 ? 12.761  -4.754  3.939   1.00 27.89  ? 100 LYS B N   1 
ATOM   3366 C  CA  . LYS B 1 100 ? 12.481  -3.490  4.651   1.00 30.95  ? 100 LYS B CA  1 
ATOM   3367 C  C   . LYS B 1 100 ? 11.052  -3.073  4.260   1.00 30.02  ? 100 LYS B C   1 
ATOM   3368 O  O   . LYS B 1 100 ? 10.779  -2.973  3.019   1.00 28.00  ? 100 LYS B O   1 
ATOM   3369 C  CB  . LYS B 1 100 ? 13.529  -2.437  4.285   1.00 33.70  ? 100 LYS B CB  1 
ATOM   3370 C  CG  . LYS B 1 100 ? 13.702  -1.331  5.312   1.00 44.20  ? 100 LYS B CG  1 
ATOM   3371 C  CD  . LYS B 1 100 ? 14.365  -0.079  4.743   1.00 54.53  ? 100 LYS B CD  1 
ATOM   3372 C  CE  . LYS B 1 100 ? 14.315  1.115   5.678   1.00 61.67  ? 100 LYS B CE  1 
ATOM   3373 N  NZ  . LYS B 1 100 ? 15.560  1.248   6.476   1.00 64.55  ? 100 LYS B NZ  1 
ATOM   3374 N  N   . TYR B 1 101 ? 10.136  -2.938  5.224   1.00 26.11  ? 101 TYR B N   1 
ATOM   3375 C  CA  . TYR B 1 101 ? 8.724   -2.583  4.897   1.00 26.46  ? 101 TYR B CA  1 
ATOM   3376 C  C   . TYR B 1 101 ? 8.113   -1.723  6.001   1.00 26.96  ? 101 TYR B C   1 
ATOM   3377 O  O   . TYR B 1 101 ? 8.592   -1.702  7.161   1.00 25.63  ? 101 TYR B O   1 
ATOM   3378 C  CB  . TYR B 1 101 ? 7.864   -3.828  4.631   1.00 25.65  ? 101 TYR B CB  1 
ATOM   3379 C  CG  . TYR B 1 101 ? 7.437   -4.546  5.890   1.00 27.61  ? 101 TYR B CG  1 
ATOM   3380 C  CD1 . TYR B 1 101 ? 8.260   -5.492  6.487   1.00 26.54  ? 101 TYR B CD1 1 
ATOM   3381 C  CD2 . TYR B 1 101 ? 6.247   -4.234  6.532   1.00 25.23  ? 101 TYR B CD2 1 
ATOM   3382 C  CE1 . TYR B 1 101 ? 7.900   -6.122  7.668   1.00 25.40  ? 101 TYR B CE1 1 
ATOM   3383 C  CE2 . TYR B 1 101 ? 5.885   -4.846  7.722   1.00 25.05  ? 101 TYR B CE2 1 
ATOM   3384 C  CZ  . TYR B 1 101 ? 6.723   -5.777  8.309   1.00 27.26  ? 101 TYR B CZ  1 
ATOM   3385 O  OH  . TYR B 1 101 ? 6.361   -6.395  9.481   1.00 27.68  ? 101 TYR B OH  1 
ATOM   3386 N  N   . LYS B 1 102 ? 7.042   -1.022  5.625   1.00 28.19  ? 102 LYS B N   1 
ATOM   3387 C  CA  . LYS B 1 102 ? 6.080   -0.461  6.590   1.00 29.78  ? 102 LYS B CA  1 
ATOM   3388 C  C   . LYS B 1 102 ? 4.676   -0.529  5.989   1.00 30.86  ? 102 LYS B C   1 
ATOM   3389 O  O   . LYS B 1 102 ? 4.511   -0.637  4.726   1.00 30.17  ? 102 LYS B O   1 
ATOM   3390 C  CB  . LYS B 1 102 ? 6.500   0.946   7.019   1.00 34.29  ? 102 LYS B CB  1 
ATOM   3391 C  CG  . LYS B 1 102 ? 6.735   1.932   5.896   1.00 38.23  ? 102 LYS B CG  1 
ATOM   3392 C  CD  . LYS B 1 102 ? 7.172   3.293   6.375   1.00 44.24  ? 102 LYS B CD  1 
ATOM   3393 C  CE  . LYS B 1 102 ? 7.961   4.019   5.307   1.00 54.36  ? 102 LYS B CE  1 
ATOM   3394 N  NZ  . LYS B 1 102 ? 7.849   5.492   5.417   1.00 60.64  ? 102 LYS B NZ  1 
ATOM   3395 N  N   . PHE B 1 103 ? 3.697   -0.491  6.882   1.00 27.43  ? 103 PHE B N   1 
ATOM   3396 C  CA  . PHE B 1 103 ? 2.251   -0.366  6.575   1.00 26.12  ? 103 PHE B CA  1 
ATOM   3397 C  C   . PHE B 1 103 ? 1.965   1.121   6.501   1.00 27.13  ? 103 PHE B C   1 
ATOM   3398 O  O   . PHE B 1 103 ? 2.374   1.867   7.415   1.00 26.48  ? 103 PHE B O   1 
ATOM   3399 C  CB  . PHE B 1 103 ? 1.402   -1.052  7.653   1.00 28.04  ? 103 PHE B CB  1 
ATOM   3400 C  CG  . PHE B 1 103 ? 1.576   -2.547  7.738   1.00 26.23  ? 103 PHE B CG  1 
ATOM   3401 C  CD1 . PHE B 1 103 ? 2.219   -3.258  6.736   1.00 23.86  ? 103 PHE B CD1 1 
ATOM   3402 C  CD2 . PHE B 1 103 ? 1.031   -3.250  8.803   1.00 26.81  ? 103 PHE B CD2 1 
ATOM   3403 C  CE1 . PHE B 1 103 ? 2.344   -4.637  6.808   1.00 25.93  ? 103 PHE B CE1 1 
ATOM   3404 C  CE2 . PHE B 1 103 ? 1.141   -4.630  8.861   1.00 26.39  ? 103 PHE B CE2 1 
ATOM   3405 C  CZ  . PHE B 1 103 ? 1.791   -5.325  7.870   1.00 24.05  ? 103 PHE B CZ  1 
ATOM   3406 N  N   . VAL B 1 104 ? 1.375   1.545   5.393   1.00 24.77  ? 104 VAL B N   1 
ATOM   3407 C  CA  . VAL B 1 104 ? 1.011   2.965   5.154   1.00 28.00  ? 104 VAL B CA  1 
ATOM   3408 C  C   . VAL B 1 104 ? -0.426  2.974   4.645   1.00 28.44  ? 104 VAL B C   1 
ATOM   3409 O  O   . VAL B 1 104 ? -0.831  2.014   3.974   1.00 33.61  ? 104 VAL B O   1 
ATOM   3410 C  CB  . VAL B 1 104 ? 2.010   3.592   4.162   1.00 34.74  ? 104 VAL B CB  1 
ATOM   3411 C  CG1 . VAL B 1 104 ? 1.577   4.963   3.677   1.00 40.87  ? 104 VAL B CG1 1 
ATOM   3412 C  CG2 . VAL B 1 104 ? 3.412   3.674   4.757   1.00 31.11  ? 104 VAL B CG2 1 
ATOM   3413 N  N   . ARG B 1 105 ? -1.175  4.029   4.926   1.00 27.72  ? 105 ARG B N   1 
ATOM   3414 C  CA  . ARG B 1 105 ? -2.528  4.220   4.372   1.00 27.51  ? 105 ARG B CA  1 
ATOM   3415 C  C   . ARG B 1 105 ? -2.420  5.328   3.322   1.00 28.82  ? 105 ARG B C   1 
ATOM   3416 O  O   . ARG B 1 105 ? -1.880  6.393   3.671   1.00 29.44  ? 105 ARG B O   1 
ATOM   3417 C  CB  . ARG B 1 105 ? -3.515  4.535   5.505   1.00 30.90  ? 105 ARG B CB  1 
ATOM   3418 C  CG  . ARG B 1 105 ? -4.915  4.870   5.008   1.00 29.94  ? 105 ARG B CG  1 
ATOM   3419 C  CD  . ARG B 1 105 ? -5.968  4.820   6.083   1.00 28.99  ? 105 ARG B CD  1 
ATOM   3420 N  NE  . ARG B 1 105 ? -7.298  4.969   5.505   1.00 27.66  ? 105 ARG B NE  1 
ATOM   3421 C  CZ  . ARG B 1 105 ? -8.163  3.987   5.255   1.00 26.23  ? 105 ARG B CZ  1 
ATOM   3422 N  NH1 . ARG B 1 105 ? -7.855  2.727   5.493   1.00 27.97  ? 105 ARG B NH1 1 
ATOM   3423 N  NH2 . ARG B 1 105 ? -9.334  4.265   4.708   1.00 28.80  ? 105 ARG B NH2 1 
ATOM   3424 N  N   . ILE B 1 106 ? -2.899  5.098   2.094   1.00 25.83  ? 106 ILE B N   1 
ATOM   3425 C  CA  . ILE B 1 106 ? -2.802  6.108   0.995   1.00 29.55  ? 106 ILE B CA  1 
ATOM   3426 C  C   . ILE B 1 106 ? -4.094  6.930   0.929   1.00 28.20  ? 106 ILE B C   1 
ATOM   3427 O  O   . ILE B 1 106 ? -5.122  6.494   1.439   1.00 27.08  ? 106 ILE B O   1 
ATOM   3428 C  CB  . ILE B 1 106 ? -2.505  5.475   -0.378  1.00 32.47  ? 106 ILE B CB  1 
ATOM   3429 C  CG1 . ILE B 1 106 ? -3.488  4.344   -0.677  1.00 32.30  ? 106 ILE B CG1 1 
ATOM   3430 C  CG2 . ILE B 1 106 ? -1.054  5.060   -0.505  1.00 34.81  ? 106 ILE B CG2 1 
ATOM   3431 C  CD1 . ILE B 1 106 ? -3.663  4.075   -2.151  1.00 37.49  ? 106 ILE B CD1 1 
ATOM   3432 N  N   . GLN B 1 107 ? -3.988  8.103   0.318   1.00 33.55  ? 107 GLN B N   1 
ATOM   3433 C  CA  . GLN B 1 107 ? -5.067  9.103   0.116   1.00 35.62  ? 107 GLN B CA  1 
ATOM   3434 C  C   . GLN B 1 107 ? -5.654  8.871   -1.265  1.00 33.21  ? 107 GLN B C   1 
ATOM   3435 O  O   . GLN B 1 107 ? -4.930  8.429   -2.158  1.00 28.26  ? 107 GLN B O   1 
ATOM   3436 C  CB  . GLN B 1 107 ? -4.479  10.516  0.164   1.00 39.54  ? 107 GLN B CB  1 
ATOM   3437 C  CG  . GLN B 1 107 ? -3.916  10.913  1.520   1.00 46.34  ? 107 GLN B CG  1 
ATOM   3438 C  CD  . GLN B 1 107 ? -5.023  10.999  2.542   1.00 54.15  ? 107 GLN B CD  1 
ATOM   3439 O  OE1 . GLN B 1 107 ? -6.193  11.204  2.212   1.00 64.88  ? 107 GLN B OE1 1 
ATOM   3440 N  NE2 . GLN B 1 107 ? -4.662  10.805  3.797   1.00 65.82  ? 107 GLN B NE2 1 
ATOM   3441 N  N   . PRO B 1 108 ? -6.946  9.189   -1.487  1.00 33.25  ? 108 PRO B N   1 
ATOM   3442 C  CA  . PRO B 1 108 ? -7.523  9.118   -2.823  1.00 34.18  ? 108 PRO B CA  1 
ATOM   3443 C  C   . PRO B 1 108 ? -6.623  9.939   -3.757  1.00 30.00  ? 108 PRO B C   1 
ATOM   3444 O  O   . PRO B 1 108 ? -6.035  10.874  -3.289  1.00 27.76  ? 108 PRO B O   1 
ATOM   3445 C  CB  . PRO B 1 108 ? -8.932  9.721   -2.696  1.00 35.82  ? 108 PRO B CB  1 
ATOM   3446 C  CG  . PRO B 1 108 ? -9.242  9.649   -1.221  1.00 38.36  ? 108 PRO B CG  1 
ATOM   3447 C  CD  . PRO B 1 108 ? -7.907  9.705   -0.495  1.00 37.02  ? 108 PRO B CD  1 
ATOM   3448 N  N   . GLY B 1 109 ? -6.461  9.486   -5.000  1.00 28.69  ? 109 GLY B N   1 
ATOM   3449 C  CA  . GLY B 1 109 ? -5.652  10.168  -6.021  1.00 27.35  ? 109 GLY B CA  1 
ATOM   3450 C  C   . GLY B 1 109 ? -4.221  9.668   -6.077  1.00 31.15  ? 109 GLY B C   1 
ATOM   3451 O  O   . GLY B 1 109 ? -3.567  9.913   -7.110  1.00 30.83  ? 109 GLY B O   1 
ATOM   3452 N  N   . GLN B 1 110 ? -3.728  9.043   -4.998  1.00 29.81  ? 110 GLN B N   1 
ATOM   3453 C  CA  . GLN B 1 110 ? -2.369  8.447   -4.938  1.00 26.86  ? 110 GLN B CA  1 
ATOM   3454 C  C   . GLN B 1 110 ? -2.397  7.093   -5.668  1.00 23.25  ? 110 GLN B C   1 
ATOM   3455 O  O   . GLN B 1 110 ? -3.444  6.411   -5.672  1.00 24.69  ? 110 GLN B O   1 
ATOM   3456 C  CB  . GLN B 1 110 ? -1.867  8.302   -3.494  1.00 29.70  ? 110 GLN B CB  1 
ATOM   3457 C  CG  . GLN B 1 110 ? -1.638  9.605   -2.744  1.00 36.18  ? 110 GLN B CG  1 
ATOM   3458 C  CD  . GLN B 1 110 ? -0.989  9.398   -1.386  1.00 45.79  ? 110 GLN B CD  1 
ATOM   3459 O  OE1 . GLN B 1 110 ? -1.515  8.734   -0.487  1.00 51.32  ? 110 GLN B OE1 1 
ATOM   3460 N  NE2 . GLN B 1 110 ? 0.186   9.977   -1.201  1.00 54.20  ? 110 GLN B NE2 1 
ATOM   3461 N  N   . THR B 1 111 ? -1.280  6.718   -6.290  1.00 22.90  ? 111 THR B N   1 
ATOM   3462 C  CA  . THR B 1 111 ? -1.156  5.489   -7.113  1.00 22.55  ? 111 THR B CA  1 
ATOM   3463 C  C   . THR B 1 111 ? -0.382  4.426   -6.321  1.00 23.05  ? 111 THR B C   1 
ATOM   3464 O  O   . THR B 1 111 ? 0.361   4.756   -5.370  1.00 23.38  ? 111 THR B O   1 
ATOM   3465 C  CB  . THR B 1 111 ? -0.500  5.789   -8.464  1.00 24.16  ? 111 THR B CB  1 
ATOM   3466 O  OG1 . THR B 1 111 ? 0.760   6.410   -8.213  1.00 22.88  ? 111 THR B OG1 1 
ATOM   3467 C  CG2 . THR B 1 111 ? -1.378  6.656   -9.336  1.00 24.88  ? 111 THR B CG2 1 
ATOM   3468 N  N   . PHE B 1 112 ? -0.510  3.186   -6.736  1.00 22.12  ? 112 PHE B N   1 
ATOM   3469 C  CA  . PHE B 1 112 ? 0.271   2.061   -6.170  1.00 22.28  ? 112 PHE B CA  1 
ATOM   3470 C  C   . PHE B 1 112 ? 0.196   0.910   -7.151  1.00 22.15  ? 112 PHE B C   1 
ATOM   3471 O  O   . PHE B 1 112 ? -0.679  0.922   -8.038  1.00 20.85  ? 112 PHE B O   1 
ATOM   3472 C  CB  . PHE B 1 112 ? -0.262  1.626   -4.799  1.00 22.04  ? 112 PHE B CB  1 
ATOM   3473 C  CG  . PHE B 1 112 ? -1.720  1.210   -4.757  1.00 23.46  ? 112 PHE B CG  1 
ATOM   3474 C  CD1 . PHE B 1 112 ? -2.734  2.153   -4.687  1.00 25.85  ? 112 PHE B CD1 1 
ATOM   3475 C  CD2 . PHE B 1 112 ? -2.085  -0.129  -4.779  1.00 22.20  ? 112 PHE B CD2 1 
ATOM   3476 C  CE1 . PHE B 1 112 ? -4.068  1.775   -4.623  1.00 25.88  ? 112 PHE B CE1 1 
ATOM   3477 C  CE2 . PHE B 1 112 ? -3.415  -0.509  -4.691  1.00 25.36  ? 112 PHE B CE2 1 
ATOM   3478 C  CZ  . PHE B 1 112 ? -4.408  0.440   -4.613  1.00 26.12  ? 112 PHE B CZ  1 
ATOM   3479 N  N   . SER B 1 113 ? 1.108   -0.038  -6.956  1.00 20.87  ? 113 SER B N   1 
ATOM   3480 C  CA  . SER B 1 113 ? 1.243   -1.280  -7.745  1.00 20.79  ? 113 SER B CA  1 
ATOM   3481 C  C   . SER B 1 113 ? 0.508   -2.386  -7.011  1.00 20.23  ? 113 SER B C   1 
ATOM   3482 O  O   . SER B 1 113 ? 0.553   -2.408  -5.798  1.00 19.81  ? 113 SER B O   1 
ATOM   3483 C  CB  . SER B 1 113 ? 2.703   -1.629  -7.918  1.00 22.06  ? 113 SER B CB  1 
ATOM   3484 O  OG  . SER B 1 113 ? 3.371   -0.575  -8.589  1.00 23.46  ? 113 SER B OG  1 
ATOM   3485 N  N   . VAL B 1 114 ? -0.123  -3.270  -7.758  1.00 20.60  ? 114 VAL B N   1 
ATOM   3486 C  CA  . VAL B 1 114 ? -0.931  -4.401  -7.252  1.00 23.27  ? 114 VAL B CA  1 
ATOM   3487 C  C   . VAL B 1 114 ? -0.283  -5.667  -7.780  1.00 22.29  ? 114 VAL B C   1 
ATOM   3488 O  O   . VAL B 1 114 ? -0.106  -5.755  -8.997  1.00 22.15  ? 114 VAL B O   1 
ATOM   3489 C  CB  . VAL B 1 114 ? -2.385  -4.282  -7.730  1.00 24.07  ? 114 VAL B CB  1 
ATOM   3490 C  CG1 . VAL B 1 114 ? -3.209  -5.492  -7.322  1.00 25.75  ? 114 VAL B CG1 1 
ATOM   3491 C  CG2 . VAL B 1 114 ? -3.005  -2.973  -7.248  1.00 27.33  ? 114 VAL B CG2 1 
ATOM   3492 N  N   . LEU B 1 115 ? 0.102   -6.570  -6.890  1.00 21.26  ? 115 LEU B N   1 
ATOM   3493 C  CA  . LEU B 1 115 ? 0.503   -7.938  -7.300  1.00 23.75  ? 115 LEU B CA  1 
ATOM   3494 C  C   . LEU B 1 115 ? -0.713  -8.883  -7.183  1.00 23.45  ? 115 LEU B C   1 
ATOM   3495 O  O   . LEU B 1 115 ? -1.101  -9.256  -6.062  1.00 25.27  ? 115 LEU B O   1 
ATOM   3496 C  CB  . LEU B 1 115 ? 1.691   -8.368  -6.439  1.00 24.38  ? 115 LEU B CB  1 
ATOM   3497 C  CG  . LEU B 1 115 ? 2.322   -9.682  -6.884  1.00 25.44  ? 115 LEU B CG  1 
ATOM   3498 C  CD1 . LEU B 1 115 ? 2.871   -9.583  -8.299  1.00 24.03  ? 115 LEU B CD1 1 
ATOM   3499 C  CD2 . LEU B 1 115 ? 3.405   -10.100 -5.901  1.00 26.73  ? 115 LEU B CD2 1 
ATOM   3500 N  N   . ALA B 1 116 ? -1.360  -9.179  -8.302  1.00 23.46  ? 116 ALA B N   1 
ATOM   3501 C  CA  . ALA B 1 116 ? -2.556  -10.048 -8.383  1.00 26.70  ? 116 ALA B CA  1 
ATOM   3502 C  C   . ALA B 1 116 ? -2.119  -11.506 -8.230  1.00 29.64  ? 116 ALA B C   1 
ATOM   3503 O  O   . ALA B 1 116 ? -1.194  -11.911 -8.945  1.00 30.21  ? 116 ALA B O   1 
ATOM   3504 C  CB  . ALA B 1 116 ? -3.272  -9.836  -9.693  1.00 26.29  ? 116 ALA B CB  1 
ATOM   3505 N  N   . CYS B 1 117 ? -2.744  -12.246 -7.312  1.00 34.49  ? 117 CYS B N   1 
ATOM   3506 C  CA  . CYS B 1 117 ? -2.325  -13.613 -6.900  1.00 45.53  ? 117 CYS B CA  1 
ATOM   3507 C  C   . CYS B 1 117 ? -3.527  -14.548 -6.998  1.00 50.43  ? 117 CYS B C   1 
ATOM   3508 O  O   . CYS B 1 117 ? -4.638  -14.039 -7.231  1.00 54.50  ? 117 CYS B O   1 
ATOM   3509 C  CB  . CYS B 1 117 ? -1.743  -13.633 -5.487  1.00 51.41  ? 117 CYS B CB  1 
ATOM   3510 S  SG  . CYS B 1 117 ? -0.260  -12.606 -5.248  1.00 54.63  ? 117 CYS B SG  1 
ATOM   3511 N  N   . TYR B 1 118 ? -3.275  -15.855 -6.852  1.00 59.86  ? 118 TYR B N   1 
ATOM   3512 C  CA  . TYR B 1 118 ? -4.177  -17.002 -7.159  1.00 59.46  ? 118 TYR B CA  1 
ATOM   3513 C  C   . TYR B 1 118 ? -3.550  -18.239 -6.510  1.00 64.04  ? 118 TYR B C   1 
ATOM   3514 O  O   . TYR B 1 118 ? -2.563  -18.793 -7.056  1.00 57.19  ? 118 TYR B O   1 
ATOM   3515 C  CB  . TYR B 1 118 ? -4.373  -17.188 -8.675  1.00 59.91  ? 118 TYR B CB  1 
ATOM   3516 C  CG  . TYR B 1 118 ? -5.125  -16.050 -9.321  1.00 64.75  ? 118 TYR B CG  1 
ATOM   3517 C  CD1 . TYR B 1 118 ? -6.469  -15.832 -9.028  1.00 67.68  ? 118 TYR B CD1 1 
ATOM   3518 C  CD2 . TYR B 1 118 ? -4.488  -15.141 -10.155 1.00 60.44  ? 118 TYR B CD2 1 
ATOM   3519 C  CE1 . TYR B 1 118 ? -7.160  -14.757 -9.566  1.00 67.97  ? 118 TYR B CE1 1 
ATOM   3520 C  CE2 . TYR B 1 118 ? -5.169  -14.066 -10.709 1.00 62.01  ? 118 TYR B CE2 1 
ATOM   3521 C  CZ  . TYR B 1 118 ? -6.506  -13.874 -10.411 1.00 62.85  ? 118 TYR B CZ  1 
ATOM   3522 O  OH  . TYR B 1 118 ? -7.192  -12.833 -10.953 1.00 62.08  ? 118 TYR B OH  1 
ATOM   3523 N  N   . ASN B 1 119 ? -4.045  -18.597 -5.322  1.00 70.17  ? 119 ASN B N   1 
ATOM   3524 C  CA  . ASN B 1 119 ? -3.520  -19.733 -4.517  1.00 71.35  ? 119 ASN B CA  1 
ATOM   3525 C  C   . ASN B 1 119 ? -2.098  -19.380 -4.043  1.00 63.66  ? 119 ASN B C   1 
ATOM   3526 O  O   . ASN B 1 119 ? -1.166  -20.153 -4.339  1.00 55.81  ? 119 ASN B O   1 
ATOM   3527 C  CB  . ASN B 1 119 ? -3.575  -21.033 -5.336  1.00 79.42  ? 119 ASN B CB  1 
ATOM   3528 C  CG  . ASN B 1 119 ? -4.874  -21.217 -6.101  1.00 82.94  ? 119 ASN B CG  1 
ATOM   3529 O  OD1 . ASN B 1 119 ? -4.988  -20.831 -7.267  1.00 89.85  ? 119 ASN B OD1 1 
ATOM   3530 N  ND2 . ASN B 1 119 ? -5.864  -21.802 -5.448  1.00 78.01  ? 119 ASN B ND2 1 
ATOM   3531 N  N   . GLY B 1 120 ? -1.927  -18.220 -3.393  1.00 55.46  ? 120 GLY B N   1 
ATOM   3532 C  CA  . GLY B 1 120 ? -0.616  -17.692 -2.959  1.00 52.23  ? 120 GLY B CA  1 
ATOM   3533 C  C   . GLY B 1 120 ? 0.414   -17.627 -4.085  1.00 50.65  ? 120 GLY B C   1 
ATOM   3534 O  O   . GLY B 1 120 ? 1.601   -17.475 -3.763  1.00 47.10  ? 120 GLY B O   1 
ATOM   3535 N  N   . SER B 1 121 ? -0.017  -17.706 -5.355  1.00 52.24  ? 121 SER B N   1 
ATOM   3536 C  CA  . SER B 1 121 ? 0.839   -17.729 -6.580  1.00 47.74  ? 121 SER B CA  1 
ATOM   3537 C  C   . SER B 1 121 ? 0.707   -16.429 -7.372  1.00 36.79  ? 121 SER B C   1 
ATOM   3538 O  O   . SER B 1 121 ? -0.296  -16.198 -8.041  1.00 29.71  ? 121 SER B O   1 
ATOM   3539 C  CB  . SER B 1 121 ? 0.503   -18.897 -7.455  1.00 49.88  ? 121 SER B CB  1 
ATOM   3540 O  OG  . SER B 1 121 ? 1.535   -19.092 -8.405  1.00 53.93  ? 121 SER B OG  1 
ATOM   3541 N  N   . PRO B 1 122 ? 1.715   -15.540 -7.320  1.00 39.23  ? 122 PRO B N   1 
ATOM   3542 C  CA  . PRO B 1 122 ? 1.632   -14.248 -8.008  1.00 36.34  ? 122 PRO B CA  1 
ATOM   3543 C  C   . PRO B 1 122 ? 1.511   -14.437 -9.525  1.00 34.12  ? 122 PRO B C   1 
ATOM   3544 O  O   . PRO B 1 122 ? 2.267   -15.217 -10.039 1.00 29.80  ? 122 PRO B O   1 
ATOM   3545 C  CB  . PRO B 1 122 ? 2.965   -13.573 -7.672  1.00 37.22  ? 122 PRO B CB  1 
ATOM   3546 C  CG  . PRO B 1 122 ? 3.491   -14.312 -6.455  1.00 37.89  ? 122 PRO B CG  1 
ATOM   3547 C  CD  . PRO B 1 122 ? 2.988   -15.726 -6.599  1.00 36.88  ? 122 PRO B CD  1 
ATOM   3548 N  N   . SER B 1 123 ? 0.590   -13.734 -10.192 1.00 28.96  ? 123 SER B N   1 
ATOM   3549 C  CA  . SER B 1 123 ? 0.280   -13.938 -11.631 1.00 30.51  ? 123 SER B CA  1 
ATOM   3550 C  C   . SER B 1 123 ? 0.444   -12.676 -12.472 1.00 28.01  ? 123 SER B C   1 
ATOM   3551 O  O   . SER B 1 123 ? 0.706   -12.828 -13.658 1.00 30.05  ? 123 SER B O   1 
ATOM   3552 C  CB  . SER B 1 123 ? -1.085  -14.491 -11.807 1.00 32.64  ? 123 SER B CB  1 
ATOM   3553 O  OG  . SER B 1 123 ? -1.041  -15.869 -11.497 1.00 40.53  ? 123 SER B OG  1 
ATOM   3554 N  N   . GLY B 1 124 ? 0.235   -11.486 -11.915 1.00 25.18  ? 124 GLY B N   1 
ATOM   3555 C  CA  . GLY B 1 124 ? 0.386   -10.239 -12.674 1.00 24.91  ? 124 GLY B CA  1 
ATOM   3556 C  C   . GLY B 1 124 ? 0.620   -9.044  -11.788 1.00 23.66  ? 124 GLY B C   1 
ATOM   3557 O  O   . GLY B 1 124 ? 0.347   -9.111  -10.575 1.00 24.69  ? 124 GLY B O   1 
ATOM   3558 N  N   A VAL B 1 125 ? 1.166   -7.981  -12.381 0.23 23.90  ? 125 VAL B N   1 
ATOM   3559 N  N   B VAL B 1 125 ? 1.103   -7.948  -12.377 0.27 23.14  ? 125 VAL B N   1 
ATOM   3560 N  N   C VAL B 1 125 ? 1.166   -7.981  -12.381 0.23 23.90  ? 125 VAL B N   1 
ATOM   3561 N  N   D VAL B 1 125 ? 1.103   -7.948  -12.377 0.27 23.14  ? 125 VAL B N   1 
ATOM   3562 C  CA  A VAL B 1 125 ? 1.389   -6.661  -11.728 0.23 24.68  ? 125 VAL B CA  1 
ATOM   3563 C  CA  B VAL B 1 125 ? 1.378   -6.668  -11.660 0.27 23.61  ? 125 VAL B CA  1 
ATOM   3564 C  CA  C VAL B 1 125 ? 1.389   -6.661  -11.728 0.23 24.68  ? 125 VAL B CA  1 
ATOM   3565 C  CA  D VAL B 1 125 ? 1.378   -6.668  -11.660 0.27 23.61  ? 125 VAL B CA  1 
ATOM   3566 C  C   A VAL B 1 125 ? 0.709   -5.597  -12.589 0.23 25.14  ? 125 VAL B C   1 
ATOM   3567 C  C   B VAL B 1 125 ? 0.892   -5.503  -12.529 0.27 24.55  ? 125 VAL B C   1 
ATOM   3568 C  C   C VAL B 1 125 ? 0.709   -5.597  -12.589 0.23 25.14  ? 125 VAL B C   1 
ATOM   3569 C  C   D VAL B 1 125 ? 0.892   -5.503  -12.529 0.27 24.55  ? 125 VAL B C   1 
ATOM   3570 O  O   A VAL B 1 125 ? 0.746   -5.721  -13.834 0.23 25.13  ? 125 VAL B O   1 
ATOM   3571 O  O   B VAL B 1 125 ? 1.270   -5.447  -13.724 0.27 24.65  ? 125 VAL B O   1 
ATOM   3572 O  O   C VAL B 1 125 ? 0.746   -5.721  -13.834 0.23 25.13  ? 125 VAL B O   1 
ATOM   3573 O  O   D VAL B 1 125 ? 1.270   -5.447  -13.724 0.27 24.65  ? 125 VAL B O   1 
ATOM   3574 C  CB  A VAL B 1 125 ? 2.885   -6.352  -11.534 0.23 25.09  ? 125 VAL B CB  1 
ATOM   3575 C  CB  B VAL B 1 125 ? 2.866   -6.544  -11.272 0.27 23.15  ? 125 VAL B CB  1 
ATOM   3576 C  CB  C VAL B 1 125 ? 2.885   -6.352  -11.534 0.23 25.09  ? 125 VAL B CB  1 
ATOM   3577 C  CB  D VAL B 1 125 ? 2.866   -6.544  -11.272 0.27 23.15  ? 125 VAL B CB  1 
ATOM   3578 C  CG1 A VAL B 1 125 ? 3.101   -5.294  -10.467 0.23 25.51  ? 125 VAL B CG1 1 
ATOM   3579 C  CG1 B VAL B 1 125 ? 3.769   -6.330  -12.476 0.27 22.88  ? 125 VAL B CG1 1 
ATOM   3580 C  CG1 C VAL B 1 125 ? 3.101   -5.294  -10.467 0.23 25.51  ? 125 VAL B CG1 1 
ATOM   3581 C  CG1 D VAL B 1 125 ? 3.769   -6.330  -12.476 0.27 22.88  ? 125 VAL B CG1 1 
ATOM   3582 C  CG2 A VAL B 1 125 ? 3.684   -7.603  -11.208 0.23 25.65  ? 125 VAL B CG2 1 
ATOM   3583 C  CG2 B VAL B 1 125 ? 3.094   -5.457  -10.236 0.27 23.40  ? 125 VAL B CG2 1 
ATOM   3584 C  CG2 C VAL B 1 125 ? 3.684   -7.603  -11.208 0.23 25.65  ? 125 VAL B CG2 1 
ATOM   3585 C  CG2 D VAL B 1 125 ? 3.094   -5.457  -10.236 0.27 23.40  ? 125 VAL B CG2 1 
ATOM   3586 N  N   . TYR B 1 126 ? 0.076   -4.615  -11.947 1.00 25.13  ? 126 TYR B N   1 
ATOM   3587 C  CA  . TYR B 1 126 ? -0.469  -3.434  -12.650 1.00 26.06  ? 126 TYR B CA  1 
ATOM   3588 C  C   . TYR B 1 126 ? -0.483  -2.272  -11.670 1.00 24.26  ? 126 TYR B C   1 
ATOM   3589 O  O   . TYR B 1 126 ? -0.415  -2.478  -10.447 1.00 22.15  ? 126 TYR B O   1 
ATOM   3590 C  CB  . TYR B 1 126 ? -1.822  -3.747  -13.295 1.00 29.52  ? 126 TYR B CB  1 
ATOM   3591 C  CG  . TYR B 1 126 ? -2.878  -4.212  -12.327 1.00 32.61  ? 126 TYR B CG  1 
ATOM   3592 C  CD1 . TYR B 1 126 ? -3.079  -5.566  -12.076 1.00 35.72  ? 126 TYR B CD1 1 
ATOM   3593 C  CD2 . TYR B 1 126 ? -3.678  -3.295  -11.665 1.00 30.73  ? 126 TYR B CD2 1 
ATOM   3594 C  CE1 . TYR B 1 126 ? -4.046  -5.996  -11.176 1.00 35.52  ? 126 TYR B CE1 1 
ATOM   3595 C  CE2 . TYR B 1 126 ? -4.625  -3.708  -10.744 1.00 37.33  ? 126 TYR B CE2 1 
ATOM   3596 C  CZ  . TYR B 1 126 ? -4.810  -5.058  -10.504 1.00 37.70  ? 126 TYR B CZ  1 
ATOM   3597 O  OH  . TYR B 1 126 ? -5.783  -5.421  -9.624  1.00 50.55  ? 126 TYR B OH  1 
ATOM   3598 N  N   . GLN B 1 127 ? -0.490  -1.078  -12.236 1.00 22.14  ? 127 GLN B N   1 
ATOM   3599 C  CA  . GLN B 1 127 ? -0.479  0.213   -11.520 1.00 24.86  ? 127 GLN B CA  1 
ATOM   3600 C  C   . GLN B 1 127 ? -1.946  0.641   -11.455 1.00 28.10  ? 127 GLN B C   1 
ATOM   3601 O  O   . GLN B 1 127 ? -2.684  0.422   -12.433 1.00 31.16  ? 127 GLN B O   1 
ATOM   3602 C  CB  . GLN B 1 127 ? 0.446   1.143   -12.311 1.00 25.93  ? 127 GLN B CB  1 
ATOM   3603 C  CG  . GLN B 1 127 ? 0.792   2.439   -11.620 1.00 26.16  ? 127 GLN B CG  1 
ATOM   3604 C  CD  . GLN B 1 127 ? 1.677   2.312   -10.417 1.00 23.99  ? 127 GLN B CD  1 
ATOM   3605 O  OE1 . GLN B 1 127 ? 2.091   1.220   -10.002 1.00 26.18  ? 127 GLN B OE1 1 
ATOM   3606 N  NE2 . GLN B 1 127 ? 1.961   3.468   -9.840  1.00 27.18  ? 127 GLN B NE2 1 
ATOM   3607 N  N   A CYS B 1 128 ? -2.369  1.149   -10.286 0.24 27.65  ? 128 CYS B N   1 
ATOM   3608 N  N   B CYS B 1 128 ? -2.359  1.275   -10.364 0.26 27.17  ? 128 CYS B N   1 
ATOM   3609 N  N   C CYS B 1 128 ? -2.369  1.149   -10.286 0.24 27.65  ? 128 CYS B N   1 
ATOM   3610 N  N   D CYS B 1 128 ? -2.359  1.275   -10.364 0.26 27.17  ? 128 CYS B N   1 
ATOM   3611 C  CA  A CYS B 1 128 ? -3.739  1.658   -9.976  0.24 27.36  ? 128 CYS B CA  1 
ATOM   3612 C  CA  B CYS B 1 128 ? -3.733  1.818   -10.247 0.26 26.36  ? 128 CYS B CA  1 
ATOM   3613 C  CA  C CYS B 1 128 ? -3.739  1.658   -9.976  0.24 27.36  ? 128 CYS B CA  1 
ATOM   3614 C  CA  D CYS B 1 128 ? -3.733  1.818   -10.247 0.26 26.36  ? 128 CYS B CA  1 
ATOM   3615 C  C   A CYS B 1 128 ? -3.648  3.063   -9.365  0.24 27.20  ? 128 CYS B C   1 
ATOM   3616 C  C   B CYS B 1 128 ? -3.786  2.902   -9.175  0.26 26.68  ? 128 CYS B C   1 
ATOM   3617 C  C   C CYS B 1 128 ? -3.648  3.063   -9.365  0.24 27.20  ? 128 CYS B C   1 
ATOM   3618 C  C   D CYS B 1 128 ? -3.786  2.902   -9.175  0.26 26.68  ? 128 CYS B C   1 
ATOM   3619 O  O   A CYS B 1 128 ? -2.530  3.476   -9.009  0.24 26.21  ? 128 CYS B O   1 
ATOM   3620 O  O   B CYS B 1 128 ? -2.964  2.876   -8.242  0.26 25.19  ? 128 CYS B O   1 
ATOM   3621 O  O   C CYS B 1 128 ? -2.530  3.476   -9.009  0.24 26.21  ? 128 CYS B O   1 
ATOM   3622 O  O   D CYS B 1 128 ? -2.964  2.876   -8.242  0.26 25.19  ? 128 CYS B O   1 
ATOM   3623 C  CB  A CYS B 1 128 ? -4.467  0.779   -8.962  0.24 26.98  ? 128 CYS B CB  1 
ATOM   3624 C  CB  B CYS B 1 128 ? -4.726  0.729   -9.885  0.26 25.99  ? 128 CYS B CB  1 
ATOM   3625 C  CB  C CYS B 1 128 ? -4.467  0.779   -8.962  0.24 26.98  ? 128 CYS B CB  1 
ATOM   3626 C  CB  D CYS B 1 128 ? -4.726  0.729   -9.885  0.26 25.99  ? 128 CYS B CB  1 
ATOM   3627 S  SG  A CYS B 1 128 ? -5.393  -0.607  -9.677  0.24 29.04  ? 128 CYS B SG  1 
ATOM   3628 S  SG  B CYS B 1 128 ? -4.537  0.203   -8.169  0.26 24.94  ? 128 CYS B SG  1 
ATOM   3629 S  SG  C CYS B 1 128 ? -5.393  -0.607  -9.677  0.24 29.04  ? 128 CYS B SG  1 
ATOM   3630 S  SG  D CYS B 1 128 ? -4.537  0.203   -8.169  0.26 24.94  ? 128 CYS B SG  1 
ATOM   3631 N  N   . ALA B 1 129 ? -4.781  3.774   -9.297  1.00 26.15  ? 129 ALA B N   1 
ATOM   3632 C  CA  . ALA B 1 129 ? -5.009  4.886   -8.369  1.00 26.83  ? 129 ALA B CA  1 
ATOM   3633 C  C   . ALA B 1 129 ? -6.162  4.452   -7.449  1.00 27.08  ? 129 ALA B C   1 
ATOM   3634 O  O   . ALA B 1 129 ? -7.106  3.763   -7.908  1.00 29.68  ? 129 ALA B O   1 
ATOM   3635 C  CB  . ALA B 1 129 ? -5.306  6.148   -9.140  1.00 29.89  ? 129 ALA B CB  1 
ATOM   3636 N  N   . MET B 1 130 ? -6.047  4.798   -6.175  1.00 29.07  ? 130 MET B N   1 
ATOM   3637 C  CA  . MET B 1 130 ? -7.180  4.856   -5.224  1.00 28.42  ? 130 MET B CA  1 
ATOM   3638 C  C   . MET B 1 130 ? -8.136  5.939   -5.765  1.00 27.56  ? 130 MET B C   1 
ATOM   3639 O  O   . MET B 1 130 ? -7.711  7.105   -5.845  1.00 28.56  ? 130 MET B O   1 
ATOM   3640 C  CB  . MET B 1 130 ? -6.629  5.208   -3.836  1.00 28.52  ? 130 MET B CB  1 
ATOM   3641 C  CG  . MET B 1 130 ? -7.676  5.278   -2.688  1.00 30.03  ? 130 MET B CG  1 
ATOM   3642 S  SD  . MET B 1 130 ? -8.642  3.760   -2.524  1.00 33.41  ? 130 MET B SD  1 
ATOM   3643 C  CE  . MET B 1 130 ? -7.359  2.659   -1.921  1.00 33.66  ? 130 MET B CE  1 
ATOM   3644 N  N   . ARG B 1 131 ? -9.325  5.557   -6.227  1.00 27.60  ? 131 ARG B N   1 
ATOM   3645 C  CA  . ARG B 1 131 ? -10.306 6.486   -6.837  1.00 27.98  ? 131 ARG B CA  1 
ATOM   3646 C  C   . ARG B 1 131 ? -10.779 7.440   -5.748  1.00 28.70  ? 131 ARG B C   1 
ATOM   3647 O  O   . ARG B 1 131 ? -10.675 7.109   -4.567  1.00 23.73  ? 131 ARG B O   1 
ATOM   3648 C  CB  . ARG B 1 131 ? -11.506 5.748   -7.434  1.00 30.75  ? 131 ARG B CB  1 
ATOM   3649 C  CG  . ARG B 1 131 ? -11.195 4.833   -8.609  1.00 33.27  ? 131 ARG B CG  1 
ATOM   3650 C  CD  . ARG B 1 131 ? -10.411 5.440   -9.747  1.00 31.30  ? 131 ARG B CD  1 
ATOM   3651 N  NE  . ARG B 1 131 ? -10.965 6.700   -10.208 1.00 33.12  ? 131 ARG B NE  1 
ATOM   3652 C  CZ  . ARG B 1 131 ? -10.343 7.535   -11.037 1.00 32.56  ? 131 ARG B CZ  1 
ATOM   3653 N  NH1 . ARG B 1 131 ? -9.127  7.245   -11.487 1.00 30.64  ? 131 ARG B NH1 1 
ATOM   3654 N  NH2 . ARG B 1 131 ? -10.916 8.680   -11.362 1.00 29.75  ? 131 ARG B NH2 1 
ATOM   3655 N  N   . PRO B 1 132 ? -11.246 8.669   -6.095  1.00 28.59  ? 132 PRO B N   1 
ATOM   3656 C  CA  . PRO B 1 132 ? -11.954 9.522   -5.133  1.00 28.67  ? 132 PRO B CA  1 
ATOM   3657 C  C   . PRO B 1 132 ? -13.086 8.803   -4.386  1.00 25.85  ? 132 PRO B C   1 
ATOM   3658 O  O   . PRO B 1 132 ? -13.224 9.090   -3.279  1.00 24.81  ? 132 PRO B O   1 
ATOM   3659 C  CB  . PRO B 1 132 ? -12.471 10.679  -6.007  1.00 29.37  ? 132 PRO B CB  1 
ATOM   3660 C  CG  . PRO B 1 132 ? -11.357 10.817  -7.045  1.00 27.50  ? 132 PRO B CG  1 
ATOM   3661 C  CD  . PRO B 1 132 ? -10.991 9.376   -7.362  1.00 27.32  ? 132 PRO B CD  1 
ATOM   3662 N  N   . ASN B 1 133 ? -13.767 7.829   -4.985  1.00 24.31  ? 133 ASN B N   1 
ATOM   3663 C  CA  . ASN B 1 133 ? -14.830 7.038   -4.318  1.00 25.33  ? 133 ASN B CA  1 
ATOM   3664 C  C   . ASN B 1 133 ? -14.255 5.800   -3.616  1.00 27.11  ? 133 ASN B C   1 
ATOM   3665 O  O   . ASN B 1 133 ? -15.047 4.878   -3.304  1.00 29.28  ? 133 ASN B O   1 
ATOM   3666 C  CB  . ASN B 1 133 ? -15.929 6.649   -5.308  1.00 25.38  ? 133 ASN B CB  1 
ATOM   3667 C  CG  . ASN B 1 133 ? -15.549 5.547   -6.277  1.00 28.32  ? 133 ASN B CG  1 
ATOM   3668 O  OD1 . ASN B 1 133 ? -14.433 5.029   -6.251  1.00 28.57  ? 133 ASN B OD1 1 
ATOM   3669 N  ND2 . ASN B 1 133 ? -16.464 5.201   -7.170  1.00 26.88  ? 133 ASN B ND2 1 
ATOM   3670 N  N   . PHE B 1 134 ? -12.941 5.740   -3.396  1.00 26.43  ? 134 PHE B N   1 
ATOM   3671 C  CA  . PHE B 1 134 ? -12.245 4.726   -2.560  1.00 25.93  ? 134 PHE B CA  1 
ATOM   3672 C  C   . PHE B 1 134 ? -12.326 3.328   -3.165  1.00 27.63  ? 134 PHE B C   1 
ATOM   3673 O  O   . PHE B 1 134 ? -12.079 2.344   -2.448  1.00 31.58  ? 134 PHE B O   1 
ATOM   3674 C  CB  . PHE B 1 134 ? -12.805 4.688   -1.137  1.00 26.82  ? 134 PHE B CB  1 
ATOM   3675 C  CG  . PHE B 1 134 ? -12.480 5.913   -0.332  1.00 26.73  ? 134 PHE B CG  1 
ATOM   3676 C  CD1 . PHE B 1 134 ? -11.178 6.156   0.087   1.00 29.21  ? 134 PHE B CD1 1 
ATOM   3677 C  CD2 . PHE B 1 134 ? -13.457 6.858   -0.055  1.00 29.33  ? 134 PHE B CD2 1 
ATOM   3678 C  CE1 . PHE B 1 134 ? -10.881 7.302   0.819   1.00 33.97  ? 134 PHE B CE1 1 
ATOM   3679 C  CE2 . PHE B 1 134 ? -13.157 8.007   0.668   1.00 29.20  ? 134 PHE B CE2 1 
ATOM   3680 C  CZ  . PHE B 1 134 ? -11.864 8.236   1.082   1.00 30.75  ? 134 PHE B CZ  1 
ATOM   3681 N  N   . THR B 1 135 ? -12.648 3.204   -4.447  1.00 29.62  ? 135 THR B N   1 
ATOM   3682 C  CA  . THR B 1 135 ? -12.544 1.901   -5.154  1.00 27.98  ? 135 THR B CA  1 
ATOM   3683 C  C   . THR B 1 135 ? -11.239 1.905   -5.956  1.00 29.73  ? 135 THR B C   1 
ATOM   3684 O  O   . THR B 1 135 ? -10.569 2.974   -6.043  1.00 29.55  ? 135 THR B O   1 
ATOM   3685 C  CB  . THR B 1 135 ? -13.769 1.641   -6.037  1.00 30.47  ? 135 THR B CB  1 
ATOM   3686 O  OG1 . THR B 1 135 ? -13.711 2.598   -7.087  1.00 26.42  ? 135 THR B OG1 1 
ATOM   3687 C  CG2 . THR B 1 135 ? -15.084 1.779   -5.305  1.00 32.22  ? 135 THR B CG2 1 
ATOM   3688 N  N   . ILE B 1 136 ? -10.881 0.756   -6.510  1.00 27.41  ? 136 ILE B N   1 
ATOM   3689 C  CA  . ILE B 1 136 ? -9.817  0.653   -7.541  1.00 34.92  ? 136 ILE B CA  1 
ATOM   3690 C  C   . ILE B 1 136 ? -10.370 -0.165  -8.717  1.00 36.62  ? 136 ILE B C   1 
ATOM   3691 O  O   . ILE B 1 136 ? -11.278 -1.024  -8.526  1.00 32.44  ? 136 ILE B O   1 
ATOM   3692 C  CB  . ILE B 1 136 ? -8.483  0.100   -6.986  1.00 38.41  ? 136 ILE B CB  1 
ATOM   3693 C  CG1 . ILE B 1 136 ? -8.525  -1.399  -6.717  1.00 38.35  ? 136 ILE B CG1 1 
ATOM   3694 C  CG2 . ILE B 1 136 ? -8.024  0.871   -5.750  1.00 38.83  ? 136 ILE B CG2 1 
ATOM   3695 C  CD1 . ILE B 1 136 ? -7.172  -1.979  -6.347  1.00 40.15  ? 136 ILE B CD1 1 
ATOM   3696 N  N   . LYS B 1 137 ? -9.892  0.154   -9.914  1.00 38.52  ? 137 LYS B N   1 
ATOM   3697 C  CA  . LYS B 1 137 ? -10.320 -0.512  -11.167 1.00 43.13  ? 137 LYS B CA  1 
ATOM   3698 C  C   . LYS B 1 137 ? -9.261  -1.569  -11.449 1.00 41.44  ? 137 LYS B C   1 
ATOM   3699 O  O   . LYS B 1 137 ? -8.324  -1.307  -12.236 1.00 41.74  ? 137 LYS B O   1 
ATOM   3700 C  CB  . LYS B 1 137 ? -10.563 0.543   -12.250 1.00 49.08  ? 137 LYS B CB  1 
ATOM   3701 C  CG  . LYS B 1 137 ? -11.728 1.468   -11.924 1.00 54.96  ? 137 LYS B CG  1 
ATOM   3702 C  CD  . LYS B 1 137 ? -11.843 2.669   -12.822 1.00 64.52  ? 137 LYS B CD  1 
ATOM   3703 C  CE  . LYS B 1 137 ? -12.795 3.710   -12.271 1.00 74.62  ? 137 LYS B CE  1 
ATOM   3704 N  NZ  . LYS B 1 137 ? -12.899 4.884   -13.171 1.00 81.62  ? 137 LYS B NZ  1 
ATOM   3705 N  N   . GLY B 1 138 ? -9.382  -2.692  -10.745 1.00 41.80  ? 138 GLY B N   1 
ATOM   3706 C  CA  . GLY B 1 138 ? -8.421  -3.804  -10.795 1.00 49.82  ? 138 GLY B CA  1 
ATOM   3707 C  C   . GLY B 1 138 ? -8.777  -4.764  -11.905 1.00 47.29  ? 138 GLY B C   1 
ATOM   3708 O  O   . GLY B 1 138 ? -9.761  -4.522  -12.637 1.00 53.96  ? 138 GLY B O   1 
ATOM   3709 N  N   . SER B 1 139 ? -8.007  -5.828  -12.020 1.00 45.15  ? 139 SER B N   1 
ATOM   3710 C  CA  . SER B 1 139 ? -8.399  -7.044  -12.757 1.00 47.98  ? 139 SER B CA  1 
ATOM   3711 C  C   . SER B 1 139 ? -8.196  -8.201  -11.797 1.00 57.39  ? 139 SER B C   1 
ATOM   3712 O  O   . SER B 1 139 ? -7.018  -8.541  -11.500 1.00 52.38  ? 139 SER B O   1 
ATOM   3713 C  CB  . SER B 1 139 ? -7.648  -7.246  -14.019 1.00 47.84  ? 139 SER B CB  1 
ATOM   3714 O  OG  . SER B 1 139 ? -7.868  -8.568  -14.475 1.00 48.49  ? 139 SER B OG  1 
ATOM   3715 N  N   . PHE B 1 140 ? -9.323  -8.698  -11.284 1.00 58.30  ? 140 PHE B N   1 
ATOM   3716 C  CA  . PHE B 1 140 ? -9.397  -9.792  -10.291 1.00 62.83  ? 140 PHE B CA  1 
ATOM   3717 C  C   . PHE B 1 140 ? -10.454 -10.805 -10.761 1.00 71.88  ? 140 PHE B C   1 
ATOM   3718 O  O   . PHE B 1 140 ? -11.484 -10.388 -11.342 1.00 70.14  ? 140 PHE B O   1 
ATOM   3719 C  CB  . PHE B 1 140 ? -9.689  -9.196  -8.910  1.00 64.02  ? 140 PHE B CB  1 
ATOM   3720 C  CG  . PHE B 1 140 ? -8.626  -8.277  -8.347  1.00 59.48  ? 140 PHE B CG  1 
ATOM   3721 C  CD1 . PHE B 1 140 ? -7.325  -8.719  -8.151  1.00 58.06  ? 140 PHE B CD1 1 
ATOM   3722 C  CD2 . PHE B 1 140 ? -8.938  -6.976  -7.973  1.00 57.47  ? 140 PHE B CD2 1 
ATOM   3723 C  CE1 . PHE B 1 140 ? -6.363  -7.881  -7.609  1.00 56.26  ? 140 PHE B CE1 1 
ATOM   3724 C  CE2 . PHE B 1 140 ? -7.974  -6.135  -7.431  1.00 58.59  ? 140 PHE B CE2 1 
ATOM   3725 C  CZ  . PHE B 1 140 ? -6.690  -6.592  -7.242  1.00 58.28  ? 140 PHE B CZ  1 
ATOM   3726 N  N   . LEU B 1 141 ? -10.161 -12.099 -10.587 1.00 74.16  ? 141 LEU B N   1 
ATOM   3727 C  CA  . LEU B 1 141 ? -11.169 -13.191 -10.534 1.00 74.30  ? 141 LEU B CA  1 
ATOM   3728 C  C   . LEU B 1 141 ? -11.037 -13.869 -9.165  1.00 75.69  ? 141 LEU B C   1 
ATOM   3729 O  O   . LEU B 1 141 ? -10.117 -13.487 -8.398  1.00 65.85  ? 141 LEU B O   1 
ATOM   3730 C  CB  . LEU B 1 141 ? -10.950 -14.189 -11.679 1.00 69.41  ? 141 LEU B CB  1 
ATOM   3731 C  CG  . LEU B 1 141 ? -10.724 -13.595 -13.069 1.00 69.16  ? 141 LEU B CG  1 
ATOM   3732 C  CD1 . LEU B 1 141 ? -10.341 -14.693 -14.049 1.00 71.91  ? 141 LEU B CD1 1 
ATOM   3733 C  CD2 . LEU B 1 141 ? -11.943 -12.833 -13.571 1.00 65.61  ? 141 LEU B CD2 1 
ATOM   3734 N  N   . ASN B 1 142 ? -11.915 -14.838 -8.888  1.00 77.91  ? 142 ASN B N   1 
ATOM   3735 C  CA  . ASN B 1 142 ? -11.917 -15.661 -7.646  1.00 82.01  ? 142 ASN B CA  1 
ATOM   3736 C  C   . ASN B 1 142 ? -10.486 -16.135 -7.359  1.00 76.92  ? 142 ASN B C   1 
ATOM   3737 O  O   . ASN B 1 142 ? -9.752  -16.465 -8.336  1.00 71.11  ? 142 ASN B O   1 
ATOM   3738 C  CB  . ASN B 1 142 ? -12.875 -16.856 -7.739  1.00 86.84  ? 142 ASN B CB  1 
ATOM   3739 C  CG  . ASN B 1 142 ? -14.234 -16.496 -8.304  1.00 95.79  ? 142 ASN B CG  1 
ATOM   3740 O  OD1 . ASN B 1 142 ? -14.611 -15.324 -8.336  1.00 108.57 ? 142 ASN B OD1 1 
ATOM   3741 N  ND2 . ASN B 1 142 ? -14.973 -17.497 -8.756  1.00 90.51  ? 142 ASN B ND2 1 
ATOM   3742 N  N   . GLY B 1 143 ? -10.113 -16.156 -6.072  1.00 71.80  ? 143 GLY B N   1 
ATOM   3743 C  CA  . GLY B 1 143 ? -8.778  -16.553 -5.580  1.00 63.23  ? 143 GLY B CA  1 
ATOM   3744 C  C   . GLY B 1 143 ? -7.833  -15.366 -5.448  1.00 53.51  ? 143 GLY B C   1 
ATOM   3745 O  O   . GLY B 1 143 ? -6.779  -15.532 -4.840  1.00 50.60  ? 143 GLY B O   1 
ATOM   3746 N  N   . SER B 1 144 ? -8.197  -14.203 -5.995  1.00 54.71  ? 144 SER B N   1 
ATOM   3747 C  CA  . SER B 1 144 ? -7.384  -12.952 -5.920  1.00 55.90  ? 144 SER B CA  1 
ATOM   3748 C  C   . SER B 1 144 ? -7.388  -12.354 -4.499  1.00 49.66  ? 144 SER B C   1 
ATOM   3749 O  O   . SER B 1 144 ? -6.443  -11.598 -4.193  1.00 41.01  ? 144 SER B O   1 
ATOM   3750 C  CB  . SER B 1 144 ? -7.812  -11.925 -6.971  1.00 48.50  ? 144 SER B CB  1 
ATOM   3751 O  OG  . SER B 1 144 ? -9.098  -11.396 -6.704  1.00 47.54  ? 144 SER B OG  1 
ATOM   3752 N  N   . CYS B 1 145 ? -8.396  -12.668 -3.665  1.00 53.91  ? 145 CYS B N   1 
ATOM   3753 C  CA  . CYS B 1 145 ? -8.602  -12.066 -2.312  1.00 50.65  ? 145 CYS B CA  1 
ATOM   3754 C  C   . CYS B 1 145 ? -7.327  -12.191 -1.458  1.00 49.93  ? 145 CYS B C   1 
ATOM   3755 O  O   . CYS B 1 145 ? -6.762  -13.310 -1.360  1.00 54.67  ? 145 CYS B O   1 
ATOM   3756 C  CB  . CYS B 1 145 ? -9.791  -12.690 -1.597  1.00 53.17  ? 145 CYS B CB  1 
ATOM   3757 S  SG  . CYS B 1 145 ? -11.376 -12.030 -2.172  1.00 57.54  ? 145 CYS B SG  1 
ATOM   3758 N  N   . GLY B 1 146 ? -6.869  -11.069 -0.889  1.00 42.78  ? 146 GLY B N   1 
ATOM   3759 C  CA  . GLY B 1 146 ? -5.603  -11.013 -0.150  1.00 40.13  ? 146 GLY B CA  1 
ATOM   3760 C  C   . GLY B 1 146 ? -4.422  -10.630 -1.025  1.00 38.48  ? 146 GLY B C   1 
ATOM   3761 O  O   . GLY B 1 146 ? -3.332  -10.545 -0.428  1.00 32.50  ? 146 GLY B O   1 
ATOM   3762 N  N   . SER B 1 147 ? -4.614  -10.464 -2.362  1.00 39.96  ? 147 SER B N   1 
ATOM   3763 C  CA  . SER B 1 147 ? -3.709  -9.745  -3.322  1.00 34.99  ? 147 SER B CA  1 
ATOM   3764 C  C   . SER B 1 147 ? -3.384  -8.344  -2.752  1.00 30.02  ? 147 SER B C   1 
ATOM   3765 O  O   . SER B 1 147 ? -4.259  -7.777  -2.098  1.00 25.61  ? 147 SER B O   1 
ATOM   3766 C  CB  . SER B 1 147 ? -4.331  -9.697  -4.714  1.00 33.50  ? 147 SER B CB  1 
ATOM   3767 O  OG  . SER B 1 147 ? -4.496  -11.024 -5.292  1.00 28.72  ? 147 SER B OG  1 
ATOM   3768 N  N   . VAL B 1 148 ? -2.170  -7.803  -2.922  1.00 31.07  ? 148 VAL B N   1 
ATOM   3769 C  CA  . VAL B 1 148 ? -1.719  -6.613  -2.130  1.00 31.04  ? 148 VAL B CA  1 
ATOM   3770 C  C   . VAL B 1 148 ? -1.187  -5.483  -3.016  1.00 28.87  ? 148 VAL B C   1 
ATOM   3771 O  O   . VAL B 1 148 ? -0.557  -5.735  -4.080  1.00 27.37  ? 148 VAL B O   1 
ATOM   3772 C  CB  . VAL B 1 148 ? -0.699  -6.976  -1.032  1.00 37.16  ? 148 VAL B CB  1 
ATOM   3773 C  CG1 . VAL B 1 148 ? -1.328  -7.835  0.062   1.00 40.61  ? 148 VAL B CG1 1 
ATOM   3774 C  CG2 . VAL B 1 148 ? 0.537   -7.649  -1.586  1.00 35.99  ? 148 VAL B CG2 1 
ATOM   3775 N  N   . GLY B 1 149 ? -1.374  -4.266  -2.522  1.00 25.48  ? 149 GLY B N   1 
ATOM   3776 C  CA  . GLY B 1 149 ? -0.935  -3.012  -3.165  1.00 24.09  ? 149 GLY B CA  1 
ATOM   3777 C  C   . GLY B 1 149 ? 0.218   -2.408  -2.400  1.00 23.33  ? 149 GLY B C   1 
ATOM   3778 O  O   . GLY B 1 149 ? 0.221   -2.511  -1.161  1.00 24.89  ? 149 GLY B O   1 
ATOM   3779 N  N   . PHE B 1 150 ? 1.163   -1.794  -3.099  1.00 21.17  ? 150 PHE B N   1 
ATOM   3780 C  CA  . PHE B 1 150 ? 2.436   -1.332  -2.502  1.00 21.73  ? 150 PHE B CA  1 
ATOM   3781 C  C   . PHE B 1 150 ? 3.078   -0.262  -3.371  1.00 22.92  ? 150 PHE B C   1 
ATOM   3782 O  O   . PHE B 1 150 ? 2.720   -0.147  -4.562  1.00 22.07  ? 150 PHE B O   1 
ATOM   3783 C  CB  . PHE B 1 150 ? 3.415   -2.487  -2.326  1.00 21.30  ? 150 PHE B CB  1 
ATOM   3784 C  CG  . PHE B 1 150 ? 3.867   -3.094  -3.620  1.00 20.44  ? 150 PHE B CG  1 
ATOM   3785 C  CD1 . PHE B 1 150 ? 3.100   -4.055  -4.260  1.00 22.87  ? 150 PHE B CD1 1 
ATOM   3786 C  CD2 . PHE B 1 150 ? 5.072   -2.746  -4.177  1.00 22.02  ? 150 PHE B CD2 1 
ATOM   3787 C  CE1 . PHE B 1 150 ? 3.507   -4.618  -5.458  1.00 23.41  ? 150 PHE B CE1 1 
ATOM   3788 C  CE2 . PHE B 1 150 ? 5.490   -3.325  -5.370  1.00 22.80  ? 150 PHE B CE2 1 
ATOM   3789 C  CZ  . PHE B 1 150 ? 4.707   -4.251  -6.013  1.00 21.65  ? 150 PHE B CZ  1 
ATOM   3790 N  N   . ASN B 1 151 ? 3.929   0.530   -2.720  1.00 23.59  ? 151 ASN B N   1 
ATOM   3791 C  CA  . ASN B 1 151 ? 4.910   1.451   -3.347  1.00 24.97  ? 151 ASN B CA  1 
ATOM   3792 C  C   . ASN B 1 151 ? 6.288   0.996   -2.872  1.00 25.54  ? 151 ASN B C   1 
ATOM   3793 O  O   . ASN B 1 151 ? 6.377   0.270   -1.863  1.00 24.60  ? 151 ASN B O   1 
ATOM   3794 C  CB  . ASN B 1 151 ? 4.601   2.923   -3.049  1.00 24.09  ? 151 ASN B CB  1 
ATOM   3795 C  CG  . ASN B 1 151 ? 3.364   3.386   -3.794  1.00 28.16  ? 151 ASN B CG  1 
ATOM   3796 O  OD1 . ASN B 1 151 ? 3.383   3.494   -5.016  1.00 27.04  ? 151 ASN B OD1 1 
ATOM   3797 N  ND2 . ASN B 1 151 ? 2.245   3.518   -3.094  1.00 24.28  ? 151 ASN B ND2 1 
ATOM   3798 N  N   . ILE B 1 152 ? 7.322   1.357   -3.608  1.00 27.40  ? 152 ILE B N   1 
ATOM   3799 C  CA  . ILE B 1 152 ? 8.724   1.133   -3.173  1.00 30.70  ? 152 ILE B CA  1 
ATOM   3800 C  C   . ILE B 1 152 ? 9.415   2.486   -3.170  1.00 37.98  ? 152 ILE B C   1 
ATOM   3801 O  O   . ILE B 1 152 ? 9.321   3.186   -4.202  1.00 42.62  ? 152 ILE B O   1 
ATOM   3802 C  CB  . ILE B 1 152 ? 9.434   0.111   -4.062  1.00 32.90  ? 152 ILE B CB  1 
ATOM   3803 C  CG1 . ILE B 1 152 ? 8.654   -1.199  -4.149  1.00 32.49  ? 152 ILE B CG1 1 
ATOM   3804 C  CG2 . ILE B 1 152 ? 10.858  -0.088  -3.562  1.00 33.33  ? 152 ILE B CG2 1 
ATOM   3805 C  CD1 . ILE B 1 152 ? 9.294   -2.246  -5.032  1.00 35.64  ? 152 ILE B CD1 1 
ATOM   3806 N  N   . ASP B 1 153 ? 9.990   2.857   -2.026  1.00 41.36  ? 153 ASP B N   1 
ATOM   3807 C  CA  . ASP B 1 153 ? 10.794  4.098   -1.851  1.00 51.66  ? 153 ASP B CA  1 
ATOM   3808 C  C   . ASP B 1 153 ? 12.201  3.684   -1.416  1.00 54.62  ? 153 ASP B C   1 
ATOM   3809 O  O   . ASP B 1 153 ? 12.341  3.254   -0.255  1.00 60.99  ? 153 ASP B O   1 
ATOM   3810 C  CB  . ASP B 1 153 ? 10.113  5.055   -0.873  1.00 52.38  ? 153 ASP B CB  1 
ATOM   3811 C  CG  . ASP B 1 153 ? 8.776   5.544   -1.401  1.00 57.65  ? 153 ASP B CG  1 
ATOM   3812 O  OD1 . ASP B 1 153 ? 8.790   6.322   -2.372  1.00 65.93  ? 153 ASP B OD1 1 
ATOM   3813 O  OD2 . ASP B 1 153 ? 7.728   5.116   -0.869  1.00 58.25  ? 153 ASP B OD2 1 
ATOM   3814 N  N   . TYR B 1 154 ? 13.169  3.754   -2.342  1.00 58.39  ? 154 TYR B N   1 
ATOM   3815 C  CA  . TYR B 1 154 ? 14.563  3.242   -2.211  1.00 56.10  ? 154 TYR B CA  1 
ATOM   3816 C  C   . TYR B 1 154 ? 14.475  1.723   -2.026  1.00 56.15  ? 154 TYR B C   1 
ATOM   3817 O  O   . TYR B 1 154 ? 14.071  1.049   -2.989  1.00 55.56  ? 154 TYR B O   1 
ATOM   3818 C  CB  . TYR B 1 154 ? 15.322  4.086   -1.179  1.00 64.26  ? 154 TYR B CB  1 
ATOM   3819 C  CG  . TYR B 1 154 ? 15.302  5.548   -1.558  1.00 76.20  ? 154 TYR B CG  1 
ATOM   3820 C  CD1 . TYR B 1 154 ? 16.122  6.032   -2.572  1.00 80.45  ? 154 TYR B CD1 1 
ATOM   3821 C  CD2 . TYR B 1 154 ? 14.377  6.425   -1.001  1.00 80.77  ? 154 TYR B CD2 1 
ATOM   3822 C  CE1 . TYR B 1 154 ? 16.067  7.358   -2.978  1.00 81.50  ? 154 TYR B CE1 1 
ATOM   3823 C  CE2 . TYR B 1 154 ? 14.311  7.755   -1.394  1.00 81.17  ? 154 TYR B CE2 1 
ATOM   3824 C  CZ  . TYR B 1 154 ? 15.162  8.223   -2.383  1.00 80.64  ? 154 TYR B CZ  1 
ATOM   3825 O  OH  . TYR B 1 154 ? 15.105  9.530   -2.768  1.00 78.32  ? 154 TYR B OH  1 
ATOM   3826 N  N   . ASP B 1 155 ? 14.779  1.184   -0.849  1.00 52.04  ? 155 ASP B N   1 
ATOM   3827 C  CA  . ASP B 1 155 ? 14.697  -0.286  -0.615  1.00 53.15  ? 155 ASP B CA  1 
ATOM   3828 C  C   . ASP B 1 155 ? 13.425  -0.645  0.177   1.00 46.48  ? 155 ASP B C   1 
ATOM   3829 O  O   . ASP B 1 155 ? 13.151  -1.861  0.299   1.00 45.01  ? 155 ASP B O   1 
ATOM   3830 C  CB  . ASP B 1 155 ? 15.962  -0.790  0.087   1.00 56.75  ? 155 ASP B CB  1 
ATOM   3831 C  CG  . ASP B 1 155 ? 16.272  -0.055  1.385   1.00 59.51  ? 155 ASP B CG  1 
ATOM   3832 O  OD1 . ASP B 1 155 ? 15.683  1.029   1.625   1.00 59.01  ? 155 ASP B OD1 1 
ATOM   3833 O  OD2 . ASP B 1 155 ? 17.096  -0.564  2.143   1.00 64.50  ? 155 ASP B OD2 1 
ATOM   3834 N  N   . CYS B 1 156 ? 12.700  0.348   0.715   1.00 40.67  ? 156 CYS B N   1 
ATOM   3835 C  CA  . CYS B 1 156 ? 11.557  0.152   1.651   1.00 36.89  ? 156 CYS B CA  1 
ATOM   3836 C  C   . CYS B 1 156 ? 10.261  -0.059  0.845   1.00 33.66  ? 156 CYS B C   1 
ATOM   3837 O  O   . CYS B 1 156 ? 9.904   0.830   0.012   1.00 30.56  ? 156 CYS B O   1 
ATOM   3838 C  CB  . CYS B 1 156 ? 11.387  1.319   2.619   1.00 39.40  ? 156 CYS B CB  1 
ATOM   3839 S  SG  . CYS B 1 156 ? 10.122  1.031   3.891   1.00 43.67  ? 156 CYS B SG  1 
ATOM   3840 N  N   . VAL B 1 157 ? 9.618   -1.209  1.047   1.00 26.86  ? 157 VAL B N   1 
ATOM   3841 C  CA  . VAL B 1 157 ? 8.230   -1.474  0.565   1.00 28.98  ? 157 VAL B CA  1 
ATOM   3842 C  C   . VAL B 1 157 ? 7.207   -0.878  1.536   1.00 26.97  ? 157 VAL B C   1 
ATOM   3843 O  O   . VAL B 1 157 ? 7.140   -1.315  2.708   1.00 27.12  ? 157 VAL B O   1 
ATOM   3844 C  CB  . VAL B 1 157 ? 7.952   -2.963  0.342   1.00 25.56  ? 157 VAL B CB  1 
ATOM   3845 C  CG1 . VAL B 1 157 ? 6.534   -3.158  -0.159  1.00 27.81  ? 157 VAL B CG1 1 
ATOM   3846 C  CG2 . VAL B 1 157 ? 8.936   -3.561  -0.639  1.00 28.06  ? 157 VAL B CG2 1 
ATOM   3847 N  N   . SER B 1 158 ? 6.373   0.015   1.030   1.00 23.18  ? 158 SER B N   1 
ATOM   3848 C  CA  . SER B 1 158 ? 5.229   0.586   1.757   1.00 24.29  ? 158 SER B CA  1 
ATOM   3849 C  C   . SER B 1 158 ? 3.971   -0.158  1.311   1.00 23.57  ? 158 SER B C   1 
ATOM   3850 O  O   . SER B 1 158 ? 3.524   0.077   0.199   1.00 23.36  ? 158 SER B O   1 
ATOM   3851 C  CB  . SER B 1 158 ? 5.166   2.067   1.535   1.00 27.41  ? 158 SER B CB  1 
ATOM   3852 O  OG  . SER B 1 158 ? 6.251   2.677   2.208   1.00 30.22  ? 158 SER B OG  1 
ATOM   3853 N  N   . PHE B 1 159 ? 3.445   -1.065  2.139   1.00 23.03  ? 159 PHE B N   1 
ATOM   3854 C  CA  . PHE B 1 159 ? 2.214   -1.826  1.826   1.00 23.30  ? 159 PHE B CA  1 
ATOM   3855 C  C   . PHE B 1 159 ? 0.984   -0.969  2.167   1.00 23.44  ? 159 PHE B C   1 
ATOM   3856 O  O   . PHE B 1 159 ? 0.918   -0.431  3.283   1.00 21.01  ? 159 PHE B O   1 
ATOM   3857 C  CB  . PHE B 1 159 ? 2.174   -3.133  2.612   1.00 25.01  ? 159 PHE B CB  1 
ATOM   3858 C  CG  . PHE B 1 159 ? 3.215   -4.145  2.227   1.00 22.95  ? 159 PHE B CG  1 
ATOM   3859 C  CD1 . PHE B 1 159 ? 3.046   -4.917  1.095   1.00 23.31  ? 159 PHE B CD1 1 
ATOM   3860 C  CD2 . PHE B 1 159 ? 4.325   -4.375  3.021   1.00 24.01  ? 159 PHE B CD2 1 
ATOM   3861 C  CE1 . PHE B 1 159 ? 3.981   -5.874  0.739   1.00 24.18  ? 159 PHE B CE1 1 
ATOM   3862 C  CE2 . PHE B 1 159 ? 5.248   -5.354  2.680   1.00 24.44  ? 159 PHE B CE2 1 
ATOM   3863 C  CZ  . PHE B 1 159 ? 5.073   -6.107  1.540   1.00 22.83  ? 159 PHE B CZ  1 
ATOM   3864 N  N   . CYS B 1 160 ? 0.047   -0.804  1.230   1.00 23.13  ? 160 CYS B N   1 
ATOM   3865 C  CA  . CYS B 1 160 ? -1.093  0.132   1.430   1.00 25.04  ? 160 CYS B CA  1 
ATOM   3866 C  C   . CYS B 1 160 ? -2.444  -0.525  1.145   1.00 23.73  ? 160 CYS B C   1 
ATOM   3867 O  O   . CYS B 1 160 ? -3.461  0.078   1.493   1.00 24.55  ? 160 CYS B O   1 
ATOM   3868 C  CB  . CYS B 1 160 ? -0.944  1.380   0.566   1.00 23.93  ? 160 CYS B CB  1 
ATOM   3869 S  SG  . CYS B 1 160 ? -0.836  0.999   -1.200  1.00 23.23  ? 160 CYS B SG  1 
ATOM   3870 N  N   . TYR B 1 161 ? -2.491  -1.692  0.522   1.00 23.64  ? 161 TYR B N   1 
ATOM   3871 C  CA  . TYR B 1 161 ? -3.784  -2.270  0.094   1.00 23.32  ? 161 TYR B CA  1 
ATOM   3872 C  C   . TYR B 1 161 ? -3.782  -3.786  0.211   1.00 22.12  ? 161 TYR B C   1 
ATOM   3873 O  O   . TYR B 1 161 ? -2.791  -4.427  -0.166  1.00 23.05  ? 161 TYR B O   1 
ATOM   3874 C  CB  . TYR B 1 161 ? -4.115  -1.847  -1.340  1.00 23.92  ? 161 TYR B CB  1 
ATOM   3875 C  CG  . TYR B 1 161 ? -5.434  -2.349  -1.873  1.00 23.36  ? 161 TYR B CG  1 
ATOM   3876 C  CD1 . TYR B 1 161 ? -6.634  -1.736  -1.539  1.00 24.63  ? 161 TYR B CD1 1 
ATOM   3877 C  CD2 . TYR B 1 161 ? -5.486  -3.439  -2.739  1.00 24.56  ? 161 TYR B CD2 1 
ATOM   3878 C  CE1 . TYR B 1 161 ? -7.853  -2.202  -2.033  1.00 25.09  ? 161 TYR B CE1 1 
ATOM   3879 C  CE2 . TYR B 1 161 ? -6.683  -3.903  -3.249  1.00 23.94  ? 161 TYR B CE2 1 
ATOM   3880 C  CZ  . TYR B 1 161 ? -7.868  -3.283  -2.905  1.00 25.68  ? 161 TYR B CZ  1 
ATOM   3881 O  OH  . TYR B 1 161 ? -9.048  -3.763  -3.402  1.00 26.03  ? 161 TYR B OH  1 
ATOM   3882 N  N   . MET B 1 162 ? -4.918  -4.325  0.661   1.00 21.86  ? 162 MET B N   1 
ATOM   3883 C  CA  . MET B 1 162 ? -5.273  -5.752  0.545   1.00 23.26  ? 162 MET B CA  1 
ATOM   3884 C  C   . MET B 1 162 ? -6.687  -5.858  -0.017  1.00 23.74  ? 162 MET B C   1 
ATOM   3885 O  O   . MET B 1 162 ? -7.632  -5.241  0.564   1.00 21.67  ? 162 MET B O   1 
ATOM   3886 C  CB  . MET B 1 162 ? -5.193  -6.448  1.906   1.00 25.64  ? 162 MET B CB  1 
ATOM   3887 C  CG  . MET B 1 162 ? -5.468  -7.944  1.839   1.00 28.02  ? 162 MET B CG  1 
ATOM   3888 S  SD  . MET B 1 162 ? -5.012  -8.779  3.395   1.00 30.51  ? 162 MET B SD  1 
ATOM   3889 C  CE  . MET B 1 162 ? -3.246  -8.982  3.210   1.00 34.17  ? 162 MET B CE  1 
ATOM   3890 N  N   . HIS B 1 163 ? -6.827  -6.637  -1.092  1.00 23.36  ? 163 HIS B N   1 
ATOM   3891 C  CA  . HIS B 1 163 ? -8.104  -6.885  -1.793  1.00 26.80  ? 163 HIS B CA  1 
ATOM   3892 C  C   . HIS B 1 163 ? -9.037  -7.730  -0.908  1.00 29.55  ? 163 HIS B C   1 
ATOM   3893 O  O   . HIS B 1 163 ? -8.615  -8.818  -0.443  1.00 28.61  ? 163 HIS B O   1 
ATOM   3894 C  CB  . HIS B 1 163 ? -7.819  -7.570  -3.134  1.00 27.56  ? 163 HIS B CB  1 
ATOM   3895 C  CG  . HIS B 1 163 ? -9.055  -7.812  -3.931  1.00 32.73  ? 163 HIS B CG  1 
ATOM   3896 N  ND1 . HIS B 1 163 ? -9.853  -6.786  -4.402  1.00 33.23  ? 163 HIS B ND1 1 
ATOM   3897 C  CD2 . HIS B 1 163 ? -9.657  -8.958  -4.309  1.00 37.08  ? 163 HIS B CD2 1 
ATOM   3898 C  CE1 . HIS B 1 163 ? -10.876 -7.296  -5.047  1.00 33.67  ? 163 HIS B CE1 1 
ATOM   3899 N  NE2 . HIS B 1 163 ? -10.774 -8.614  -5.013  1.00 33.28  ? 163 HIS B NE2 1 
ATOM   3900 N  N   . HIS B 1 164 ? -10.285 -7.293  -0.743  1.00 31.36  ? 164 HIS B N   1 
ATOM   3901 C  CA  . HIS B 1 164 ? -11.340 -8.047  -0.020  1.00 31.13  ? 164 HIS B CA  1 
ATOM   3902 C  C   . HIS B 1 164 ? -12.465 -8.476  -0.966  1.00 33.26  ? 164 HIS B C   1 
ATOM   3903 O  O   . HIS B 1 164 ? -12.881 -9.624  -0.840  1.00 34.78  ? 164 HIS B O   1 
ATOM   3904 C  CB  . HIS B 1 164 ? -11.868 -7.247  1.171   1.00 30.27  ? 164 HIS B CB  1 
ATOM   3905 C  CG  . HIS B 1 164 ? -10.931 -7.196  2.327   1.00 29.76  ? 164 HIS B CG  1 
ATOM   3906 N  ND1 . HIS B 1 164 ? -11.253 -7.710  3.562   1.00 28.48  ? 164 HIS B ND1 1 
ATOM   3907 C  CD2 . HIS B 1 164 ? -9.681  -6.687  2.435   1.00 30.25  ? 164 HIS B CD2 1 
ATOM   3908 C  CE1 . HIS B 1 164 ? -10.250 -7.497  4.395   1.00 28.99  ? 164 HIS B CE1 1 
ATOM   3909 N  NE2 . HIS B 1 164 ? -9.270  -6.869  3.719   1.00 29.87  ? 164 HIS B NE2 1 
ATOM   3910 N  N   . MET B 1 165 ? -12.970 -7.624  -1.866  1.00 35.00  ? 165 MET B N   1 
ATOM   3911 C  CA  . MET B 1 165 ? -14.222 -7.972  -2.603  1.00 36.04  ? 165 MET B CA  1 
ATOM   3912 C  C   . MET B 1 165 ? -14.315 -7.270  -3.952  1.00 36.41  ? 165 MET B C   1 
ATOM   3913 O  O   . MET B 1 165 ? -13.656 -6.235  -4.141  1.00 33.02  ? 165 MET B O   1 
ATOM   3914 C  CB  . MET B 1 165 ? -15.451 -7.574  -1.778  1.00 38.24  ? 165 MET B CB  1 
ATOM   3915 C  CG  . MET B 1 165 ? -15.583 -6.065  -1.591  1.00 45.77  ? 165 MET B CG  1 
ATOM   3916 S  SD  . MET B 1 165 ? -16.642 -5.529  -0.203  1.00 55.77  ? 165 MET B SD  1 
ATOM   3917 C  CE  . MET B 1 165 ? -16.373 -6.921  0.899   1.00 56.18  ? 165 MET B CE  1 
ATOM   3918 N  N   . GLU B 1 166 ? -15.166 -7.796  -4.832  1.00 38.77  ? 166 GLU B N   1 
ATOM   3919 C  CA  . GLU B 1 166 ? -15.591 -7.093  -6.069  1.00 43.20  ? 166 GLU B CA  1 
ATOM   3920 C  C   . GLU B 1 166 ? -16.977 -6.474  -5.838  1.00 43.57  ? 166 GLU B C   1 
ATOM   3921 O  O   . GLU B 1 166 ? -17.834 -7.126  -5.220  1.00 44.81  ? 166 GLU B O   1 
ATOM   3922 C  CB  . GLU B 1 166 ? -15.543 -8.030  -7.277  1.00 44.45  ? 166 GLU B CB  1 
ATOM   3923 C  CG  . GLU B 1 166 ? -15.723 -7.281  -8.585  1.00 47.22  ? 166 GLU B CG  1 
ATOM   3924 C  CD  . GLU B 1 166 ? -15.489 -8.086  -9.850  1.00 50.18  ? 166 GLU B CD  1 
ATOM   3925 O  OE1 . GLU B 1 166 ? -14.347 -8.536  -10.071 1.00 52.62  ? 166 GLU B OE1 1 
ATOM   3926 O  OE2 . GLU B 1 166 ? -16.456 -8.259  -10.609 1.00 56.86  ? 166 GLU B OE2 1 
ATOM   3927 N  N   . LEU B 1 167 ? -17.169 -5.232  -6.273  1.00 39.86  ? 167 LEU B N   1 
ATOM   3928 C  CA  . LEU B 1 167 ? -18.496 -4.563  -6.291  1.00 42.87  ? 167 LEU B CA  1 
ATOM   3929 C  C   . LEU B 1 167 ? -19.192 -4.887  -7.615  1.00 49.66  ? 167 LEU B C   1 
ATOM   3930 O  O   . LEU B 1 167 ? -18.539 -5.322  -8.564  1.00 46.59  ? 167 LEU B O   1 
ATOM   3931 C  CB  . LEU B 1 167 ? -18.289 -3.056  -6.104  1.00 43.90  ? 167 LEU B CB  1 
ATOM   3932 C  CG  . LEU B 1 167 ? -17.636 -2.665  -4.780  1.00 43.98  ? 167 LEU B CG  1 
ATOM   3933 C  CD1 . LEU B 1 167 ? -17.305 -1.183  -4.739  1.00 47.10  ? 167 LEU B CD1 1 
ATOM   3934 C  CD2 . LEU B 1 167 ? -18.520 -3.044  -3.612  1.00 42.02  ? 167 LEU B CD2 1 
ATOM   3935 N  N   . PRO B 1 168 ? -20.533 -4.711  -7.712  1.00 52.47  ? 168 PRO B N   1 
ATOM   3936 C  CA  . PRO B 1 168 ? -21.301 -5.169  -8.870  1.00 54.27  ? 168 PRO B CA  1 
ATOM   3937 C  C   . PRO B 1 168 ? -20.756 -4.621  -10.193 1.00 60.00  ? 168 PRO B C   1 
ATOM   3938 O  O   . PRO B 1 168 ? -20.655 -5.373  -11.141 1.00 67.95  ? 168 PRO B O   1 
ATOM   3939 C  CB  . PRO B 1 168 ? -22.704 -4.603  -8.634  1.00 54.31  ? 168 PRO B CB  1 
ATOM   3940 C  CG  . PRO B 1 168 ? -22.787 -4.431  -7.143  1.00 59.92  ? 168 PRO B CG  1 
ATOM   3941 C  CD  . PRO B 1 168 ? -21.385 -4.055  -6.709  1.00 55.22  ? 168 PRO B CD  1 
ATOM   3942 N  N   . THR B 1 169 ? -20.365 -3.345  -10.181 1.00 59.46  ? 169 THR B N   1 
ATOM   3943 C  CA  . THR B 1 169 ? -19.873 -2.562  -11.345 1.00 56.69  ? 169 THR B CA  1 
ATOM   3944 C  C   . THR B 1 169 ? -18.519 -3.060  -11.883 1.00 50.89  ? 169 THR B C   1 
ATOM   3945 O  O   . THR B 1 169 ? -18.049 -2.451  -12.839 1.00 51.28  ? 169 THR B O   1 
ATOM   3946 C  CB  . THR B 1 169 ? -19.767 -1.086  -10.947 1.00 57.22  ? 169 THR B CB  1 
ATOM   3947 O  OG1 . THR B 1 169 ? -19.122 -1.029  -9.672  1.00 63.28  ? 169 THR B OG1 1 
ATOM   3948 C  CG2 . THR B 1 169 ? -21.120 -0.422  -10.867 1.00 57.09  ? 169 THR B CG2 1 
ATOM   3949 N  N   . GLY B 1 170 ? -17.888 -4.083  -11.300 1.00 48.29  ? 170 GLY B N   1 
ATOM   3950 C  CA  . GLY B 1 170 ? -16.565 -4.581  -11.733 1.00 47.00  ? 170 GLY B CA  1 
ATOM   3951 C  C   . GLY B 1 170 ? -15.391 -3.929  -11.000 1.00 49.26  ? 170 GLY B C   1 
ATOM   3952 O  O   . GLY B 1 170 ? -14.234 -4.318  -11.300 1.00 50.30  ? 170 GLY B O   1 
ATOM   3953 N  N   . VAL B 1 171 ? -15.640 -2.979  -10.084 1.00 43.45  ? 171 VAL B N   1 
ATOM   3954 C  CA  . VAL B 1 171 ? -14.568 -2.275  -9.310  1.00 41.13  ? 171 VAL B CA  1 
ATOM   3955 C  C   . VAL B 1 171 ? -14.275 -3.051  -8.016  1.00 35.56  ? 171 VAL B C   1 
ATOM   3956 O  O   . VAL B 1 171 ? -15.063 -3.948  -7.643  1.00 31.28  ? 171 VAL B O   1 
ATOM   3957 C  CB  . VAL B 1 171 ? -14.905 -0.788  -9.052  1.00 45.13  ? 171 VAL B CB  1 
ATOM   3958 C  CG1 . VAL B 1 171 ? -15.108 -0.028  -10.367 1.00 47.52  ? 171 VAL B CG1 1 
ATOM   3959 C  CG2 . VAL B 1 171 ? -16.102 -0.605  -8.127  1.00 43.00  ? 171 VAL B CG2 1 
ATOM   3960 N  N   . HIS B 1 172 ? -13.132 -2.770  -7.384  1.00 32.33  ? 172 HIS B N   1 
ATOM   3961 C  CA  . HIS B 1 172 ? -12.597 -3.583  -6.261  1.00 29.03  ? 172 HIS B CA  1 
ATOM   3962 C  C   . HIS B 1 172 ? -12.541 -2.724  -4.991  1.00 28.02  ? 172 HIS B C   1 
ATOM   3963 O  O   . HIS B 1 172 ? -12.310 -1.489  -5.084  1.00 25.21  ? 172 HIS B O   1 
ATOM   3964 C  CB  . HIS B 1 172 ? -11.322 -4.270  -6.729  1.00 34.46  ? 172 HIS B CB  1 
ATOM   3965 C  CG  . HIS B 1 172 ? -11.583 -5.066  -7.975  1.00 44.10  ? 172 HIS B CG  1 
ATOM   3966 N  ND1 . HIS B 1 172 ? -11.378 -4.545  -9.252  1.00 46.50  ? 172 HIS B ND1 1 
ATOM   3967 C  CD2 . HIS B 1 172 ? -12.128 -6.293  -8.155  1.00 44.45  ? 172 HIS B CD2 1 
ATOM   3968 C  CE1 . HIS B 1 172 ? -11.727 -5.444  -10.153 1.00 50.98  ? 172 HIS B CE1 1 
ATOM   3969 N  NE2 . HIS B 1 172 ? -12.201 -6.524  -9.504  1.00 53.11  ? 172 HIS B NE2 1 
ATOM   3970 N  N   . ALA B 1 173 ? -12.806 -3.343  -3.843  1.00 24.28  ? 173 ALA B N   1 
ATOM   3971 C  CA  . ALA B 1 173 ? -12.744 -2.690  -2.523  1.00 24.97  ? 173 ALA B CA  1 
ATOM   3972 C  C   . ALA B 1 173 ? -11.875 -3.523  -1.596  1.00 24.46  ? 173 ALA B C   1 
ATOM   3973 O  O   . ALA B 1 173 ? -11.878 -4.770  -1.714  1.00 24.82  ? 173 ALA B O   1 
ATOM   3974 C  CB  . ALA B 1 173 ? -14.135 -2.524  -1.968  1.00 30.57  ? 173 ALA B CB  1 
ATOM   3975 N  N   . GLY B 1 174 ? -11.127 -2.848  -0.725  1.00 23.76  ? 174 GLY B N   1 
ATOM   3976 C  CA  . GLY B 1 174 ? -10.203 -3.503  0.204   1.00 23.21  ? 174 GLY B CA  1 
ATOM   3977 C  C   . GLY B 1 174 ? -9.783  -2.608  1.359   1.00 22.06  ? 174 GLY B C   1 
ATOM   3978 O  O   . GLY B 1 174 ? -10.355 -1.516  1.552   1.00 20.93  ? 174 GLY B O   1 
ATOM   3979 N  N   . THR B 1 175 ? -8.778  -3.064  2.104   1.00 20.95  ? 175 THR B N   1 
ATOM   3980 C  CA  . THR B 1 175 ? -8.337  -2.418  3.362   1.00 22.17  ? 175 THR B CA  1 
ATOM   3981 C  C   . THR B 1 175 ? -6.889  -1.981  3.231   1.00 21.04  ? 175 THR B C   1 
ATOM   3982 O  O   . THR B 1 175 ? -6.202  -2.442  2.318   1.00 23.90  ? 175 THR B O   1 
ATOM   3983 C  CB  . THR B 1 175 ? -8.490  -3.368  4.561   1.00 22.35  ? 175 THR B CB  1 
ATOM   3984 O  OG1 . THR B 1 175 ? -7.591  -4.464  4.366   1.00 20.94  ? 175 THR B OG1 1 
ATOM   3985 C  CG2 . THR B 1 175 ? -9.914  -3.851  4.715   1.00 22.98  ? 175 THR B CG2 1 
ATOM   3986 N  N   . ASP B 1 176 ? -6.437  -1.156  4.160   1.00 20.64  ? 176 ASP B N   1 
ATOM   3987 C  CA  . ASP B 1 176 ? -4.999  -1.048  4.453   1.00 21.41  ? 176 ASP B CA  1 
ATOM   3988 C  C   . ASP B 1 176 ? -4.607  -2.337  5.195   1.00 22.62  ? 176 ASP B C   1 
ATOM   3989 O  O   . ASP B 1 176 ? -5.490  -3.227  5.411   1.00 24.30  ? 176 ASP B O   1 
ATOM   3990 C  CB  . ASP B 1 176 ? -4.706  0.266   5.172   1.00 22.16  ? 176 ASP B CB  1 
ATOM   3991 C  CG  . ASP B 1 176 ? -5.345  0.354   6.537   1.00 23.66  ? 176 ASP B CG  1 
ATOM   3992 O  OD1 . ASP B 1 176 ? -5.587  -0.716  7.135   1.00 24.53  ? 176 ASP B OD1 1 
ATOM   3993 O  OD2 . ASP B 1 176 ? -5.592  1.468   6.983   1.00 23.16  ? 176 ASP B OD2 1 
ATOM   3994 N  N   . LEU B 1 177 ? -3.333  -2.459  5.543   1.00 23.16  ? 177 LEU B N   1 
ATOM   3995 C  CA  . LEU B 1 177 ? -2.772  -3.680  6.174   1.00 24.65  ? 177 LEU B CA  1 
ATOM   3996 C  C   . LEU B 1 177 ? -3.092  -3.694  7.672   1.00 26.97  ? 177 LEU B C   1 
ATOM   3997 O  O   . LEU B 1 177 ? -2.745  -4.666  8.297   1.00 28.82  ? 177 LEU B O   1 
ATOM   3998 C  CB  . LEU B 1 177 ? -1.263  -3.730  5.900   1.00 25.61  ? 177 LEU B CB  1 
ATOM   3999 C  CG  . LEU B 1 177 ? -0.893  -4.554  4.673   1.00 27.69  ? 177 LEU B CG  1 
ATOM   4000 C  CD1 . LEU B 1 177 ? -1.176  -6.026  4.924   1.00 29.84  ? 177 LEU B CD1 1 
ATOM   4001 C  CD2 . LEU B 1 177 ? -1.629  -4.079  3.421   1.00 29.01  ? 177 LEU B CD2 1 
ATOM   4002 N  N   . GLU B 1 178 ? -3.742  -2.654  8.196   1.00 27.18  ? 178 GLU B N   1 
ATOM   4003 C  CA  . GLU B 1 178 ? -4.291  -2.618  9.574   1.00 28.51  ? 178 GLU B CA  1 
ATOM   4004 C  C   . GLU B 1 178 ? -5.778  -3.001  9.535   1.00 25.74  ? 178 GLU B C   1 
ATOM   4005 O  O   . GLU B 1 178 ? -6.391  -3.002  10.599  1.00 27.11  ? 178 GLU B O   1 
ATOM   4006 C  CB  . GLU B 1 178 ? -4.079  -1.246  10.200  1.00 29.04  ? 178 GLU B CB  1 
ATOM   4007 C  CG  . GLU B 1 178 ? -2.612  -0.875  10.350  1.00 34.82  ? 178 GLU B CG  1 
ATOM   4008 C  CD  . GLU B 1 178 ? -2.422  0.284   11.305  1.00 37.47  ? 178 GLU B CD  1 
ATOM   4009 O  OE1 . GLU B 1 178 ? -2.000  0.049   12.446  1.00 51.21  ? 178 GLU B OE1 1 
ATOM   4010 O  OE2 . GLU B 1 178 ? -2.786  1.387   10.943  1.00 43.14  ? 178 GLU B OE2 1 
ATOM   4011 N  N   . GLY B 1 179 ? -6.312  -3.335  8.352   1.00 24.68  ? 179 GLY B N   1 
ATOM   4012 C  CA  . GLY B 1 179 ? -7.673  -3.894  8.177   1.00 26.36  ? 179 GLY B CA  1 
ATOM   4013 C  C   . GLY B 1 179 ? -8.749  -2.833  8.156   1.00 25.93  ? 179 GLY B C   1 
ATOM   4014 O  O   . GLY B 1 179 ? -9.924  -3.205  8.291   1.00 27.70  ? 179 GLY B O   1 
ATOM   4015 N  N   . ASN B 1 180 ? -8.388  -1.559  7.986   1.00 26.18  ? 180 ASN B N   1 
ATOM   4016 C  CA  . ASN B 1 180 ? -9.380  -0.464  7.837   1.00 26.00  ? 180 ASN B CA  1 
ATOM   4017 C  C   . ASN B 1 180 ? -9.753  -0.373  6.360   1.00 26.30  ? 180 ASN B C   1 
ATOM   4018 O  O   . ASN B 1 180 ? -8.841  -0.158  5.511   1.00 22.48  ? 180 ASN B O   1 
ATOM   4019 C  CB  . ASN B 1 180 ? -8.859  0.888   8.307   1.00 27.40  ? 180 ASN B CB  1 
ATOM   4020 C  CG  . ASN B 1 180 ? -8.272  0.844   9.694   1.00 32.71  ? 180 ASN B CG  1 
ATOM   4021 O  OD1 . ASN B 1 180 ? -8.995  0.592   10.661  1.00 32.13  ? 180 ASN B OD1 1 
ATOM   4022 N  ND2 . ASN B 1 180 ? -6.975  1.117   9.797   1.00 31.51  ? 180 ASN B ND2 1 
ATOM   4023 N  N   . PHE B 1 181 ? -11.041 -0.502  6.053   1.00 24.38  ? 181 PHE B N   1 
ATOM   4024 C  CA  . PHE B 1 181 ? -11.540 -0.298  4.672   1.00 25.56  ? 181 PHE B CA  1 
ATOM   4025 C  C   . PHE B 1 181 ? -11.129 1.082   4.147   1.00 24.65  ? 181 PHE B C   1 
ATOM   4026 O  O   . PHE B 1 181 ? -11.064 2.084   4.896   1.00 23.31  ? 181 PHE B O   1 
ATOM   4027 C  CB  . PHE B 1 181 ? -13.046 -0.519  4.559   1.00 25.45  ? 181 PHE B CB  1 
ATOM   4028 C  CG  . PHE B 1 181 ? -13.378 -1.909  4.080   1.00 26.73  ? 181 PHE B CG  1 
ATOM   4029 C  CD1 . PHE B 1 181 ? -13.343 -2.212  2.725   1.00 27.35  ? 181 PHE B CD1 1 
ATOM   4030 C  CD2 . PHE B 1 181 ? -13.649 -2.930  4.986   1.00 24.74  ? 181 PHE B CD2 1 
ATOM   4031 C  CE1 . PHE B 1 181 ? -13.609 -3.500  2.290   1.00 27.46  ? 181 PHE B CE1 1 
ATOM   4032 C  CE2 . PHE B 1 181 ? -13.893 -4.218  4.548   1.00 24.62  ? 181 PHE B CE2 1 
ATOM   4033 C  CZ  . PHE B 1 181 ? -13.864 -4.497  3.207   1.00 26.89  ? 181 PHE B CZ  1 
ATOM   4034 N  N   . TYR B 1 182 ? -10.802 1.106   2.859   1.00 23.89  ? 182 TYR B N   1 
ATOM   4035 C  CA  . TYR B 1 182 ? -10.893 2.303   1.998   1.00 24.21  ? 182 TYR B CA  1 
ATOM   4036 C  C   . TYR B 1 182 ? -12.356 2.344   1.553   1.00 24.66  ? 182 TYR B C   1 
ATOM   4037 O  O   . TYR B 1 182 ? -12.806 1.386   0.913   1.00 27.34  ? 182 TYR B O   1 
ATOM   4038 C  CB  . TYR B 1 182 ? -9.909  2.229   0.829   1.00 24.92  ? 182 TYR B CB  1 
ATOM   4039 C  CG  . TYR B 1 182 ? -8.451  2.288   1.209   1.00 24.42  ? 182 TYR B CG  1 
ATOM   4040 C  CD1 . TYR B 1 182 ? -7.849  3.489   1.556   1.00 25.69  ? 182 TYR B CD1 1 
ATOM   4041 C  CD2 . TYR B 1 182 ? -7.666  1.144   1.215   1.00 24.23  ? 182 TYR B CD2 1 
ATOM   4042 C  CE1 . TYR B 1 182 ? -6.499  3.561   1.870   1.00 26.07  ? 182 TYR B CE1 1 
ATOM   4043 C  CE2 . TYR B 1 182 ? -6.330  1.191   1.568   1.00 22.41  ? 182 TYR B CE2 1 
ATOM   4044 C  CZ  . TYR B 1 182 ? -5.736  2.401   1.899   1.00 24.84  ? 182 TYR B CZ  1 
ATOM   4045 O  OH  . TYR B 1 182 ? -4.399  2.473   2.216   1.00 23.04  ? 182 TYR B OH  1 
ATOM   4046 N  N   . GLY B 1 183 ? -13.076 3.377   1.974   1.00 23.47  ? 183 GLY B N   1 
ATOM   4047 C  CA  . GLY B 1 183 ? -14.456 3.642   1.520   1.00 26.50  ? 183 GLY B CA  1 
ATOM   4048 C  C   . GLY B 1 183 ? -15.509 3.011   2.424   1.00 26.97  ? 183 GLY B C   1 
ATOM   4049 O  O   . GLY B 1 183 ? -15.184 2.245   3.341   1.00 24.62  ? 183 GLY B O   1 
ATOM   4050 N  N   . PRO B 1 184 ? -16.798 3.305   2.154   1.00 26.87  ? 184 PRO B N   1 
ATOM   4051 C  CA  . PRO B 1 184 ? -17.890 2.950   3.071   1.00 26.40  ? 184 PRO B CA  1 
ATOM   4052 C  C   . PRO B 1 184 ? -18.415 1.521   2.879   1.00 28.80  ? 184 PRO B C   1 
ATOM   4053 O  O   . PRO B 1 184 ? -19.617 1.337   2.635   1.00 27.67  ? 184 PRO B O   1 
ATOM   4054 C  CB  . PRO B 1 184 ? -18.966 4.002   2.732   1.00 26.60  ? 184 PRO B CB  1 
ATOM   4055 C  CG  . PRO B 1 184 ? -18.737 4.311   1.256   1.00 28.61  ? 184 PRO B CG  1 
ATOM   4056 C  CD  . PRO B 1 184 ? -17.241 4.151   1.030   1.00 26.14  ? 184 PRO B CD  1 
ATOM   4057 N  N   . PHE B 1 185 ? -17.502 0.552   2.960   1.00 27.13  ? 185 PHE B N   1 
ATOM   4058 C  CA  . PHE B 1 185 ? -17.705 -0.861  2.544   1.00 27.38  ? 185 PHE B CA  1 
ATOM   4059 C  C   . PHE B 1 185 ? -17.580 -1.736  3.784   1.00 26.65  ? 185 PHE B C   1 
ATOM   4060 O  O   . PHE B 1 185 ? -16.926 -1.329  4.763   1.00 24.78  ? 185 PHE B O   1 
ATOM   4061 C  CB  . PHE B 1 185 ? -16.758 -1.245  1.394   1.00 29.03  ? 185 PHE B CB  1 
ATOM   4062 C  CG  . PHE B 1 185 ? -16.933 -0.348  0.191   1.00 28.82  ? 185 PHE B CG  1 
ATOM   4063 C  CD1 . PHE B 1 185 ? -18.147 -0.286  -0.482  1.00 29.14  ? 185 PHE B CD1 1 
ATOM   4064 C  CD2 . PHE B 1 185 ? -15.922 0.501   -0.214  1.00 27.33  ? 185 PHE B CD2 1 
ATOM   4065 C  CE1 . PHE B 1 185 ? -18.325 0.579   -1.552  1.00 29.41  ? 185 PHE B CE1 1 
ATOM   4066 C  CE2 . PHE B 1 185 ? -16.101 1.358   -1.286  1.00 27.00  ? 185 PHE B CE2 1 
ATOM   4067 C  CZ  . PHE B 1 185 ? -17.307 1.409   -1.943  1.00 28.09  ? 185 PHE B CZ  1 
ATOM   4068 N  N   . VAL B 1 186 ? -18.254 -2.877  3.762   1.00 27.65  ? 186 VAL B N   1 
ATOM   4069 C  CA  . VAL B 1 186 ? -18.208 -3.858  4.877   1.00 28.51  ? 186 VAL B CA  1 
ATOM   4070 C  C   . VAL B 1 186 ? -17.888 -5.216  4.260   1.00 28.43  ? 186 VAL B C   1 
ATOM   4071 O  O   . VAL B 1 186 ? -18.266 -5.443  3.084   1.00 26.92  ? 186 VAL B O   1 
ATOM   4072 C  CB  . VAL B 1 186 ? -19.513 -3.857  5.686   1.00 32.12  ? 186 VAL B CB  1 
ATOM   4073 C  CG1 . VAL B 1 186 ? -19.704 -2.546  6.439   1.00 31.50  ? 186 VAL B CG1 1 
ATOM   4074 C  CG2 . VAL B 1 186 ? -20.731 -4.156  4.820   1.00 33.74  ? 186 VAL B CG2 1 
ATOM   4075 N  N   . ASP B 1 187 ? -17.217 -6.080  5.015   1.00 28.21  ? 187 ASP B N   1 
ATOM   4076 C  CA  . ASP B 1 187 ? -16.894 -7.459  4.564   1.00 31.01  ? 187 ASP B CA  1 
ATOM   4077 C  C   . ASP B 1 187 ? -18.061 -8.390  4.939   1.00 35.61  ? 187 ASP B C   1 
ATOM   4078 O  O   . ASP B 1 187 ? -17.852 -9.313  5.763   1.00 35.32  ? 187 ASP B O   1 
ATOM   4079 C  CB  . ASP B 1 187 ? -15.531 -7.900  5.102   1.00 30.23  ? 187 ASP B CB  1 
ATOM   4080 C  CG  . ASP B 1 187 ? -15.356 -7.781  6.609   1.00 27.49  ? 187 ASP B CG  1 
ATOM   4081 O  OD1 . ASP B 1 187 ? -16.217 -7.167  7.292   1.00 27.67  ? 187 ASP B OD1 1 
ATOM   4082 O  OD2 . ASP B 1 187 ? -14.334 -8.272  7.078   1.00 25.42  ? 187 ASP B OD2 1 
ATOM   4083 N  N   . ARG B 1 188 ? -19.235 -8.154  4.338   1.00 40.26  ? 188 ARG B N   1 
ATOM   4084 C  CA  . ARG B 1 188 ? -20.428 -9.042  4.422   1.00 46.03  ? 188 ARG B CA  1 
ATOM   4085 C  C   . ARG B 1 188 ? -21.113 -9.105  3.047   1.00 45.46  ? 188 ARG B C   1 
ATOM   4086 O  O   . ARG B 1 188 ? -21.024 -8.131  2.276   1.00 37.70  ? 188 ARG B O   1 
ATOM   4087 C  CB  . ARG B 1 188 ? -21.353 -8.604  5.567   1.00 47.37  ? 188 ARG B CB  1 
ATOM   4088 C  CG  . ARG B 1 188 ? -22.679 -7.966  5.171   1.00 57.08  ? 188 ARG B CG  1 
ATOM   4089 C  CD  . ARG B 1 188 ? -23.483 -7.474  6.373   1.00 61.46  ? 188 ARG B CD  1 
ATOM   4090 N  NE  . ARG B 1 188 ? -22.547 -6.809  7.275   1.00 74.47  ? 188 ARG B NE  1 
ATOM   4091 C  CZ  . ARG B 1 188 ? -22.182 -7.231  8.491   1.00 77.26  ? 188 ARG B CZ  1 
ATOM   4092 N  NH1 . ARG B 1 188 ? -22.722 -8.312  9.039   1.00 84.45  ? 188 ARG B NH1 1 
ATOM   4093 N  NH2 . ARG B 1 188 ? -21.277 -6.540  9.164   1.00 68.13  ? 188 ARG B NH2 1 
ATOM   4094 N  N   . GLN B 1 189 ? -21.751 -10.238 2.750   1.00 48.75  ? 189 GLN B N   1 
ATOM   4095 C  CA  . GLN B 1 189 ? -22.538 -10.450 1.511   1.00 58.09  ? 189 GLN B CA  1 
ATOM   4096 C  C   . GLN B 1 189 ? -23.856 -9.681  1.654   1.00 56.84  ? 189 GLN B C   1 
ATOM   4097 O  O   . GLN B 1 189 ? -24.808 -10.217 2.247   1.00 54.83  ? 189 GLN B O   1 
ATOM   4098 C  CB  . GLN B 1 189 ? -22.758 -11.943 1.263   1.00 67.28  ? 189 GLN B CB  1 
ATOM   4099 C  CG  . GLN B 1 189 ? -23.514 -12.232 -0.021  1.00 73.39  ? 189 GLN B CG  1 
ATOM   4100 C  CD  . GLN B 1 189 ? -22.883 -11.501 -1.182  1.00 85.54  ? 189 GLN B CD  1 
ATOM   4101 O  OE1 . GLN B 1 189 ? -23.565 -10.901 -2.013  1.00 92.36  ? 189 GLN B OE1 1 
ATOM   4102 N  NE2 . GLN B 1 189 ? -21.558 -11.523 -1.228  1.00 87.11  ? 189 GLN B NE2 1 
ATOM   4103 N  N   . THR B 1 190 ? -23.862 -8.440  1.172   1.00 53.42  ? 190 THR B N   1 
ATOM   4104 C  CA  . THR B 1 190 ? -24.957 -7.451  1.310   1.00 49.17  ? 190 THR B CA  1 
ATOM   4105 C  C   . THR B 1 190 ? -24.897 -6.536  0.086   1.00 49.24  ? 190 THR B C   1 
ATOM   4106 O  O   . THR B 1 190 ? -23.895 -6.619  -0.630  1.00 51.79  ? 190 THR B O   1 
ATOM   4107 C  CB  . THR B 1 190 ? -24.807 -6.651  2.604   1.00 49.99  ? 190 THR B CB  1 
ATOM   4108 O  OG1 . THR B 1 190 ? -26.044 -5.991  2.838   1.00 46.71  ? 190 THR B OG1 1 
ATOM   4109 C  CG2 . THR B 1 190 ? -23.696 -5.624  2.540   1.00 52.83  ? 190 THR B CG2 1 
ATOM   4110 N  N   . ALA B 1 191 ? -25.903 -5.677  -0.109  1.00 52.30  ? 191 ALA B N   1 
ATOM   4111 C  CA  . ALA B 1 191 ? -26.006 -4.740  -1.256  1.00 52.89  ? 191 ALA B CA  1 
ATOM   4112 C  C   . ALA B 1 191 ? -25.075 -3.548  -1.014  1.00 44.06  ? 191 ALA B C   1 
ATOM   4113 O  O   . ALA B 1 191 ? -25.329 -2.795  -0.058  1.00 44.32  ? 191 ALA B O   1 
ATOM   4114 C  CB  . ALA B 1 191 ? -27.441 -4.283  -1.429  1.00 53.50  ? 191 ALA B CB  1 
ATOM   4115 N  N   . GLN B 1 192 ? -24.027 -3.400  -1.825  1.00 41.36  ? 192 GLN B N   1 
ATOM   4116 C  CA  . GLN B 1 192 ? -23.066 -2.267  -1.734  1.00 39.13  ? 192 GLN B CA  1 
ATOM   4117 C  C   . GLN B 1 192 ? -22.725 -1.798  -3.151  1.00 40.53  ? 192 GLN B C   1 
ATOM   4118 O  O   . GLN B 1 192 ? -22.469 -2.653  -4.008  1.00 44.32  ? 192 GLN B O   1 
ATOM   4119 C  CB  . GLN B 1 192 ? -21.780 -2.662  -1.009  1.00 36.32  ? 192 GLN B CB  1 
ATOM   4120 C  CG  . GLN B 1 192 ? -21.972 -3.615  0.153   1.00 35.26  ? 192 GLN B CG  1 
ATOM   4121 C  CD  . GLN B 1 192 ? -20.707 -3.785  0.956   1.00 35.25  ? 192 GLN B CD  1 
ATOM   4122 O  OE1 . GLN B 1 192 ? -20.116 -2.812  1.424   1.00 32.33  ? 192 GLN B OE1 1 
ATOM   4123 N  NE2 . GLN B 1 192 ? -20.299 -5.027  1.151   1.00 32.74  ? 192 GLN B NE2 1 
ATOM   4124 N  N   . ALA B 1 193 ? -22.728 -0.486  -3.381  1.00 40.50  ? 193 ALA B N   1 
ATOM   4125 C  CA  . ALA B 1 193 ? -22.399 0.120   -4.689  1.00 40.60  ? 193 ALA B CA  1 
ATOM   4126 C  C   . ALA B 1 193 ? -21.267 1.123   -4.493  1.00 42.49  ? 193 ALA B C   1 
ATOM   4127 O  O   . ALA B 1 193 ? -21.265 1.834   -3.475  1.00 40.73  ? 193 ALA B O   1 
ATOM   4128 C  CB  . ALA B 1 193 ? -23.603 0.797   -5.292  1.00 38.57  ? 193 ALA B CB  1 
ATOM   4129 N  N   . ALA B 1 194 ? -20.370 1.183   -5.470  1.00 45.96  ? 194 ALA B N   1 
ATOM   4130 C  CA  . ALA B 1 194 ? -19.458 2.320   -5.698  1.00 48.22  ? 194 ALA B CA  1 
ATOM   4131 C  C   . ALA B 1 194 ? -20.288 3.614   -5.737  1.00 47.60  ? 194 ALA B C   1 
ATOM   4132 O  O   . ALA B 1 194 ? -21.301 3.636   -6.462  1.00 47.65  ? 194 ALA B O   1 
ATOM   4133 C  CB  . ALA B 1 194 ? -18.700 2.077   -6.982  1.00 45.33  ? 194 ALA B CB  1 
ATOM   4134 N  N   . GLY B 1 195 ? -19.908 4.621   -4.942  1.00 44.73  ? 195 GLY B N   1 
ATOM   4135 C  CA  . GLY B 1 195 ? -20.367 6.018   -5.085  1.00 44.48  ? 195 GLY B CA  1 
ATOM   4136 C  C   . GLY B 1 195 ? -20.028 6.563   -6.467  1.00 44.31  ? 195 GLY B C   1 
ATOM   4137 O  O   . GLY B 1 195 ? -19.191 5.962   -7.170  1.00 37.67  ? 195 GLY B O   1 
ATOM   4138 N  N   . THR B 1 196 ? -20.675 7.639   -6.901  1.00 40.73  ? 196 THR B N   1 
ATOM   4139 C  CA  . THR B 1 196 ? -20.334 8.259   -8.204  1.00 41.83  ? 196 THR B CA  1 
ATOM   4140 C  C   . THR B 1 196 ? -18.884 8.751   -8.059  1.00 39.43  ? 196 THR B C   1 
ATOM   4141 O  O   . THR B 1 196 ? -18.538 9.376   -7.036  1.00 41.74  ? 196 THR B O   1 
ATOM   4142 C  CB  . THR B 1 196 ? -21.372 9.300   -8.667  1.00 46.16  ? 196 THR B CB  1 
ATOM   4143 O  OG1 . THR B 1 196 ? -21.195 10.495  -7.909  1.00 52.82  ? 196 THR B OG1 1 
ATOM   4144 C  CG2 . THR B 1 196 ? -22.808 8.836   -8.551  1.00 42.76  ? 196 THR B CG2 1 
ATOM   4145 N  N   . ASP B 1 197 ? -18.042 8.404   -9.019  1.00 38.97  ? 197 ASP B N   1 
ATOM   4146 C  CA  . ASP B 1 197 ? -16.598 8.717   -8.982  1.00 39.30  ? 197 ASP B CA  1 
ATOM   4147 C  C   . ASP B 1 197 ? -16.388 10.105  -9.574  1.00 39.65  ? 197 ASP B C   1 
ATOM   4148 O  O   . ASP B 1 197 ? -17.303 10.647  -10.208 1.00 45.77  ? 197 ASP B O   1 
ATOM   4149 C  CB  . ASP B 1 197 ? -15.802 7.650   -9.724  1.00 37.82  ? 197 ASP B CB  1 
ATOM   4150 C  CG  . ASP B 1 197 ? -14.368 7.487   -9.249  1.00 32.46  ? 197 ASP B CG  1 
ATOM   4151 O  OD1 . ASP B 1 197 ? -13.973 8.083   -8.190  1.00 30.42  ? 197 ASP B OD1 1 
ATOM   4152 O  OD2 . ASP B 1 197 ? -13.678 6.749   -9.916  1.00 32.50  ? 197 ASP B OD2 1 
ATOM   4153 N  N   . THR B 1 198 ? -15.228 10.676  -9.319  1.00 39.23  ? 198 THR B N   1 
ATOM   4154 C  CA  . THR B 1 198 ? -14.795 11.945  -9.934  1.00 40.29  ? 198 THR B CA  1 
ATOM   4155 C  C   . THR B 1 198 ? -13.424 11.726  -10.565 1.00 38.41  ? 198 THR B C   1 
ATOM   4156 O  O   . THR B 1 198 ? -12.760 10.725  -10.216 1.00 32.95  ? 198 THR B O   1 
ATOM   4157 C  CB  . THR B 1 198 ? -14.808 13.073  -8.905  1.00 39.01  ? 198 THR B CB  1 
ATOM   4158 O  OG1 . THR B 1 198 ? -14.206 12.568  -7.718  1.00 35.52  ? 198 THR B OG1 1 
ATOM   4159 C  CG2 . THR B 1 198 ? -16.208 13.552  -8.599  1.00 44.18  ? 198 THR B CG2 1 
ATOM   4160 N  N   . THR B 1 199 ? -13.039 12.647  -11.442 1.00 33.25  ? 199 THR B N   1 
ATOM   4161 C  CA  . THR B 1 199 ? -11.728 12.666  -12.136 1.00 32.34  ? 199 THR B CA  1 
ATOM   4162 C  C   . THR B 1 199 ? -10.712 13.359  -11.237 1.00 28.59  ? 199 THR B C   1 
ATOM   4163 O  O   . THR B 1 199 ? -11.047 14.411  -10.639 1.00 32.73  ? 199 THR B O   1 
ATOM   4164 C  CB  . THR B 1 199 ? -11.853 13.337  -13.511 1.00 34.16  ? 199 THR B CB  1 
ATOM   4165 O  OG1 . THR B 1 199 ? -12.813 12.578  -14.231 1.00 30.57  ? 199 THR B OG1 1 
ATOM   4166 C  CG2 . THR B 1 199 ? -10.554 13.350  -14.288 1.00 35.02  ? 199 THR B CG2 1 
ATOM   4167 N  N   . ILE B 1 200 ? -9.521  12.776  -11.113 1.00 27.47  ? 200 ILE B N   1 
ATOM   4168 C  CA  . ILE B 1 200 ? -8.425  13.319  -10.273 1.00 26.94  ? 200 ILE B CA  1 
ATOM   4169 C  C   . ILE B 1 200 ? -7.725  14.388  -11.116 1.00 30.85  ? 200 ILE B C   1 
ATOM   4170 O  O   . ILE B 1 200 ? -6.842  14.036  -11.906 1.00 27.06  ? 200 ILE B O   1 
ATOM   4171 C  CB  . ILE B 1 200 ? -7.475  12.204  -9.769  1.00 24.77  ? 200 ILE B CB  1 
ATOM   4172 C  CG1 . ILE B 1 200 ? -8.228  11.029  -9.129  1.00 24.85  ? 200 ILE B CG1 1 
ATOM   4173 C  CG2 . ILE B 1 200 ? -6.461  12.771  -8.805  1.00 25.52  ? 200 ILE B CG2 1 
ATOM   4174 C  CD1 . ILE B 1 200 ? -7.576  9.684   -9.331  1.00 22.99  ? 200 ILE B CD1 1 
ATOM   4175 N  N   . THR B 1 201 ? -8.071  15.660  -10.883 1.00 34.08  ? 201 THR B N   1 
ATOM   4176 C  CA  . THR B 1 201 ? -7.691  16.810  -11.734 1.00 31.58  ? 201 THR B CA  1 
ATOM   4177 C  C   . THR B 1 201 ? -6.168  16.949  -11.778 1.00 32.68  ? 201 THR B C   1 
ATOM   4178 O  O   . THR B 1 201 ? -5.600  17.133  -12.890 1.00 29.60  ? 201 THR B O   1 
ATOM   4179 C  CB  . THR B 1 201 ? -8.362  18.105  -11.254 1.00 30.87  ? 201 THR B CB  1 
ATOM   4180 O  OG1 . THR B 1 201 ? -9.745  17.822  -11.091 1.00 26.95  ? 201 THR B OG1 1 
ATOM   4181 C  CG2 . THR B 1 201 ? -8.199  19.228  -12.254 1.00 32.80  ? 201 THR B CG2 1 
ATOM   4182 N  N   . VAL B 1 202 ? -5.527  16.927  -10.616 1.00 27.04  ? 202 VAL B N   1 
ATOM   4183 C  CA  . VAL B 1 202 ? -4.065  17.143  -10.534 1.00 28.16  ? 202 VAL B CA  1 
ATOM   4184 C  C   . VAL B 1 202 ? -3.324  16.077  -11.363 1.00 27.62  ? 202 VAL B C   1 
ATOM   4185 O  O   . VAL B 1 202 ? -2.253  16.414  -11.925 1.00 27.55  ? 202 VAL B O   1 
ATOM   4186 C  CB  . VAL B 1 202 ? -3.581  17.179  -9.080  1.00 28.01  ? 202 VAL B CB  1 
ATOM   4187 C  CG1 . VAL B 1 202 ? -3.832  15.863  -8.348  1.00 29.84  ? 202 VAL B CG1 1 
ATOM   4188 C  CG2 . VAL B 1 202 ? -2.137  17.611  -9.038  1.00 25.38  ? 202 VAL B CG2 1 
ATOM   4189 N  N   . ASN B 1 203 ? -3.862  14.858  -11.422 1.00 25.10  ? 203 ASN B N   1 
ATOM   4190 C  CA  . ASN B 1 203 ? -3.233  13.730  -12.157 1.00 26.86  ? 203 ASN B CA  1 
ATOM   4191 C  C   . ASN B 1 203 ? -3.403  13.964  -13.665 1.00 25.74  ? 203 ASN B C   1 
ATOM   4192 O  O   . ASN B 1 203 ? -2.458  13.722  -14.405 1.00 24.12  ? 203 ASN B O   1 
ATOM   4193 C  CB  . ASN B 1 203 ? -3.807  12.379  -11.723 1.00 26.16  ? 203 ASN B CB  1 
ATOM   4194 C  CG  . ASN B 1 203 ? -3.356  11.936  -10.343 1.00 25.98  ? 203 ASN B CG  1 
ATOM   4195 O  OD1 . ASN B 1 203 ? -2.619  12.650  -9.668  1.00 25.58  ? 203 ASN B OD1 1 
ATOM   4196 N  ND2 . ASN B 1 203 ? -3.801  10.752  -9.924  1.00 25.59  ? 203 ASN B ND2 1 
ATOM   4197 N  N   . VAL B 1 204 ? -4.567  14.457  -14.098 1.00 27.81  ? 204 VAL B N   1 
ATOM   4198 C  CA  . VAL B 1 204 ? -4.805  14.770  -15.535 1.00 28.11  ? 204 VAL B CA  1 
ATOM   4199 C  C   . VAL B 1 204 ? -3.770  15.812  -15.968 1.00 28.70  ? 204 VAL B C   1 
ATOM   4200 O  O   . VAL B 1 204 ? -3.153  15.643  -17.036 1.00 26.19  ? 204 VAL B O   1 
ATOM   4201 C  CB  . VAL B 1 204 ? -6.247  15.222  -15.833 1.00 29.22  ? 204 VAL B CB  1 
ATOM   4202 C  CG1 . VAL B 1 204 ? -6.363  15.707  -17.268 1.00 29.01  ? 204 VAL B CG1 1 
ATOM   4203 C  CG2 . VAL B 1 204 ? -7.268  14.124  -15.589 1.00 28.73  ? 204 VAL B CG2 1 
ATOM   4204 N  N   . LEU B 1 205 ? -3.522  16.817  -15.139 1.00 26.83  ? 205 LEU B N   1 
ATOM   4205 C  CA  . LEU B 1 205 ? -2.588  17.911  -15.477 1.00 29.27  ? 205 LEU B CA  1 
ATOM   4206 C  C   . LEU B 1 205 ? -1.170  17.335  -15.555 1.00 29.95  ? 205 LEU B C   1 
ATOM   4207 O  O   . LEU B 1 205 ? -0.482  17.629  -16.546 1.00 31.56  ? 205 LEU B O   1 
ATOM   4208 C  CB  . LEU B 1 205 ? -2.740  19.051  -14.461 1.00 30.77  ? 205 LEU B CB  1 
ATOM   4209 C  CG  . LEU B 1 205 ? -4.088  19.779  -14.558 1.00 33.57  ? 205 LEU B CG  1 
ATOM   4210 C  CD1 . LEU B 1 205 ? -4.348  20.682  -13.351 1.00 37.29  ? 205 LEU B CD1 1 
ATOM   4211 C  CD2 . LEU B 1 205 ? -4.159  20.592  -15.841 1.00 35.58  ? 205 LEU B CD2 1 
ATOM   4212 N  N   . ALA B 1 206 ? -0.774  16.501  -14.586 1.00 27.69  ? 206 ALA B N   1 
ATOM   4213 C  CA  . ALA B 1 206 ? 0.528   15.792  -14.568 1.00 26.20  ? 206 ALA B CA  1 
ATOM   4214 C  C   . ALA B 1 206 ? 0.719   15.029  -15.891 1.00 27.81  ? 206 ALA B C   1 
ATOM   4215 O  O   . ALA B 1 206 ? 1.839   15.061  -16.450 1.00 27.85  ? 206 ALA B O   1 
ATOM   4216 C  CB  . ALA B 1 206 ? 0.589   14.873  -13.379 1.00 27.51  ? 206 ALA B CB  1 
ATOM   4217 N  N   . TRP B 1 207 ? -0.333  14.366  -16.365 1.00 24.88  ? 207 TRP B N   1 
ATOM   4218 C  CA  . TRP B 1 207 ? -0.311  13.540  -17.596 1.00 27.42  ? 207 TRP B CA  1 
ATOM   4219 C  C   . TRP B 1 207 ? -0.233  14.447  -18.832 1.00 28.48  ? 207 TRP B C   1 
ATOM   4220 O  O   . TRP B 1 207 ? 0.424   14.041  -19.812 1.00 26.03  ? 207 TRP B O   1 
ATOM   4221 C  CB  . TRP B 1 207 ? -1.528  12.619  -17.644 1.00 27.67  ? 207 TRP B CB  1 
ATOM   4222 C  CG  . TRP B 1 207 ? -1.761  11.877  -18.924 1.00 28.05  ? 207 TRP B CG  1 
ATOM   4223 C  CD1 . TRP B 1 207 ? -1.175  10.717  -19.360 1.00 28.47  ? 207 TRP B CD1 1 
ATOM   4224 C  CD2 . TRP B 1 207 ? -2.790  12.174  -19.879 1.00 29.03  ? 207 TRP B CD2 1 
ATOM   4225 N  NE1 . TRP B 1 207 ? -1.714  10.327  -20.570 1.00 27.26  ? 207 TRP B NE1 1 
ATOM   4226 C  CE2 . TRP B 1 207 ? -2.711  11.199  -20.901 1.00 27.37  ? 207 TRP B CE2 1 
ATOM   4227 C  CE3 . TRP B 1 207 ? -3.707  13.223  -20.005 1.00 29.43  ? 207 TRP B CE3 1 
ATOM   4228 C  CZ2 . TRP B 1 207 ? -3.548  11.224  -22.013 1.00 30.61  ? 207 TRP B CZ2 1 
ATOM   4229 C  CZ3 . TRP B 1 207 ? -4.557  13.220  -21.086 1.00 32.07  ? 207 TRP B CZ3 1 
ATOM   4230 C  CH2 . TRP B 1 207 ? -4.485  12.232  -22.070 1.00 30.08  ? 207 TRP B CH2 1 
ATOM   4231 N  N   . LEU B 1 208 ? -0.821  15.640  -18.783 1.00 27.24  ? 208 LEU B N   1 
ATOM   4232 C  CA  . LEU B 1 208 ? -0.657  16.647  -19.872 1.00 29.44  ? 208 LEU B CA  1 
ATOM   4233 C  C   . LEU B 1 208 ? 0.790   17.118  -19.889 1.00 27.97  ? 208 LEU B C   1 
ATOM   4234 O  O   . LEU B 1 208 ? 1.354   17.251  -20.989 1.00 32.25  ? 208 LEU B O   1 
ATOM   4235 C  CB  . LEU B 1 208 ? -1.633  17.825  -19.730 1.00 29.59  ? 208 LEU B CB  1 
ATOM   4236 C  CG  . LEU B 1 208 ? -3.105  17.474  -19.863 1.00 28.89  ? 208 LEU B CG  1 
ATOM   4237 C  CD1 . LEU B 1 208 ? -3.980  18.719  -19.710 1.00 32.82  ? 208 LEU B CD1 1 
ATOM   4238 C  CD2 . LEU B 1 208 ? -3.394  16.792  -21.186 1.00 33.82  ? 208 LEU B CD2 1 
ATOM   4239 N  N   . TYR B 1 209 ? 1.417   17.283  -18.736 1.00 31.01  ? 209 TYR B N   1 
ATOM   4240 C  CA  . TYR B 1 209 ? 2.854   17.620  -18.668 1.00 32.75  ? 209 TYR B CA  1 
ATOM   4241 C  C   . TYR B 1 209 ? 3.682   16.477  -19.285 1.00 35.64  ? 209 TYR B C   1 
ATOM   4242 O  O   . TYR B 1 209 ? 4.640   16.796  -20.035 1.00 35.23  ? 209 TYR B O   1 
ATOM   4243 C  CB  . TYR B 1 209 ? 3.270   17.968  -17.241 1.00 36.62  ? 209 TYR B CB  1 
ATOM   4244 C  CG  . TYR B 1 209 ? 2.912   19.370  -16.809 1.00 41.13  ? 209 TYR B CG  1 
ATOM   4245 C  CD1 . TYR B 1 209 ? 3.481   20.491  -17.404 1.00 44.69  ? 209 TYR B CD1 1 
ATOM   4246 C  CD2 . TYR B 1 209 ? 2.015   19.577  -15.779 1.00 42.12  ? 209 TYR B CD2 1 
ATOM   4247 C  CE1 . TYR B 1 209 ? 3.153   21.776  -16.993 1.00 44.46  ? 209 TYR B CE1 1 
ATOM   4248 C  CE2 . TYR B 1 209 ? 1.664   20.849  -15.366 1.00 42.18  ? 209 TYR B CE2 1 
ATOM   4249 C  CZ  . TYR B 1 209 ? 2.241   21.957  -15.966 1.00 47.48  ? 209 TYR B CZ  1 
ATOM   4250 O  OH  . TYR B 1 209 ? 1.870   23.199  -15.532 1.00 39.92  ? 209 TYR B OH  1 
ATOM   4251 N  N   . ALA B 1 210 ? 3.343   15.208  -19.013 1.00 32.07  ? 210 ALA B N   1 
ATOM   4252 C  CA  . ALA B 1 210 ? 4.045   14.027  -19.582 1.00 29.95  ? 210 ALA B CA  1 
ATOM   4253 C  C   . ALA B 1 210 ? 3.930   14.065  -21.107 1.00 31.52  ? 210 ALA B C   1 
ATOM   4254 O  O   . ALA B 1 210 ? 4.907   13.686  -21.780 1.00 33.09  ? 210 ALA B O   1 
ATOM   4255 C  CB  . ALA B 1 210 ? 3.483   12.730  -19.057 1.00 29.85  ? 210 ALA B CB  1 
ATOM   4256 N  N   . ALA B 1 211 ? 2.777   14.493  -21.619 1.00 30.61  ? 211 ALA B N   1 
ATOM   4257 C  CA  . ALA B 1 211 ? 2.486   14.515  -23.067 1.00 34.67  ? 211 ALA B CA  1 
ATOM   4258 C  C   . ALA B 1 211 ? 3.393   15.565  -23.714 1.00 36.71  ? 211 ALA B C   1 
ATOM   4259 O  O   . ALA B 1 211 ? 4.070   15.241  -24.706 1.00 34.86  ? 211 ALA B O   1 
ATOM   4260 C  CB  . ALA B 1 211 ? 1.030   14.792  -23.306 1.00 31.30  ? 211 ALA B CB  1 
ATOM   4261 N  N   . VAL B 1 212 ? 3.439   16.765  -23.127 1.00 35.17  ? 212 VAL B N   1 
ATOM   4262 C  CA  . VAL B 1 212 ? 4.263   17.905  -23.641 1.00 37.11  ? 212 VAL B CA  1 
ATOM   4263 C  C   . VAL B 1 212 ? 5.724   17.448  -23.663 1.00 35.01  ? 212 VAL B C   1 
ATOM   4264 O  O   . VAL B 1 212 ? 6.351   17.555  -24.712 1.00 38.14  ? 212 VAL B O   1 
ATOM   4265 C  CB  . VAL B 1 212 ? 4.069   19.195  -22.814 1.00 32.84  ? 212 VAL B CB  1 
ATOM   4266 C  CG1 . VAL B 1 212 ? 5.043   20.285  -23.226 1.00 35.71  ? 212 VAL B CG1 1 
ATOM   4267 C  CG2 . VAL B 1 212 ? 2.644   19.699  -22.917 1.00 33.66  ? 212 VAL B CG2 1 
ATOM   4268 N  N   . ILE B 1 213 ? 6.223   16.921  -22.550 1.00 34.74  ? 213 ILE B N   1 
ATOM   4269 C  CA  . ILE B 1 213 ? 7.616   16.404  -22.418 1.00 36.99  ? 213 ILE B CA  1 
ATOM   4270 C  C   . ILE B 1 213 ? 7.912   15.399  -23.537 1.00 37.16  ? 213 ILE B C   1 
ATOM   4271 O  O   . ILE B 1 213 ? 9.073   15.354  -23.967 1.00 37.75  ? 213 ILE B O   1 
ATOM   4272 C  CB  . ILE B 1 213 ? 7.858   15.810  -21.018 1.00 40.40  ? 213 ILE B CB  1 
ATOM   4273 C  CG1 . ILE B 1 213 ? 7.761   16.897  -19.937 1.00 40.05  ? 213 ILE B CG1 1 
ATOM   4274 C  CG2 . ILE B 1 213 ? 9.185   15.065  -20.980 1.00 40.27  ? 213 ILE B CG2 1 
ATOM   4275 C  CD1 . ILE B 1 213 ? 7.842   16.398  -18.523 1.00 39.62  ? 213 ILE B CD1 1 
ATOM   4276 N  N   . ASN B 1 214 ? 6.917   14.630  -23.990 1.00 36.80  ? 214 ASN B N   1 
ATOM   4277 C  CA  . ASN B 1 214 ? 7.078   13.594  -25.050 1.00 37.91  ? 214 ASN B CA  1 
ATOM   4278 C  C   . ASN B 1 214 ? 6.772   14.148  -26.444 1.00 39.37  ? 214 ASN B C   1 
ATOM   4279 O  O   . ASN B 1 214 ? 6.775   13.345  -27.381 1.00 42.11  ? 214 ASN B O   1 
ATOM   4280 C  CB  . ASN B 1 214 ? 6.211   12.363  -24.778 1.00 37.17  ? 214 ASN B CB  1 
ATOM   4281 C  CG  . ASN B 1 214 ? 6.848   11.527  -23.697 1.00 39.77  ? 214 ASN B CG  1 
ATOM   4282 O  OD1 . ASN B 1 214 ? 7.716   10.709  -23.984 1.00 41.71  ? 214 ASN B OD1 1 
ATOM   4283 N  ND2 . ASN B 1 214 ? 6.528   11.830  -22.450 1.00 39.92  ? 214 ASN B ND2 1 
ATOM   4284 N  N   . GLY B 1 215 ? 6.521   15.454  -26.577 1.00 41.33  ? 215 GLY B N   1 
ATOM   4285 C  CA  . GLY B 1 215 ? 6.354   16.137  -27.874 1.00 39.53  ? 215 GLY B CA  1 
ATOM   4286 C  C   . GLY B 1 215 ? 4.919   16.144  -28.352 1.00 38.91  ? 215 GLY B C   1 
ATOM   4287 O  O   . GLY B 1 215 ? 4.702   16.422  -29.531 1.00 40.29  ? 215 GLY B O   1 
ATOM   4288 N  N   . ASP B 1 216 ? 3.957   15.834  -27.483 1.00 39.25  ? 216 ASP B N   1 
ATOM   4289 C  CA  . ASP B 1 216 ? 2.513   15.932  -27.812 1.00 42.41  ? 216 ASP B CA  1 
ATOM   4290 C  C   . ASP B 1 216 ? 2.039   17.293  -27.280 1.00 46.83  ? 216 ASP B C   1 
ATOM   4291 O  O   . ASP B 1 216 ? 1.725   17.366  -26.086 1.00 43.63  ? 216 ASP B O   1 
ATOM   4292 C  CB  . ASP B 1 216 ? 1.773   14.733  -27.216 1.00 44.78  ? 216 ASP B CB  1 
ATOM   4293 C  CG  . ASP B 1 216 ? 0.851   14.009  -28.165 1.00 43.31  ? 216 ASP B CG  1 
ATOM   4294 O  OD1 . ASP B 1 216 ? 0.610   14.521  -29.269 1.00 49.44  ? 216 ASP B OD1 1 
ATOM   4295 O  OD2 . ASP B 1 216 ? 0.387   12.940  -27.785 1.00 40.14  ? 216 ASP B OD2 1 
ATOM   4296 N  N   . ARG B 1 217 ? 2.021   18.329  -28.128 1.00 45.79  ? 217 ARG B N   1 
ATOM   4297 C  CA  . ARG B 1 217 ? 1.937   19.754  -27.708 1.00 46.50  ? 217 ARG B CA  1 
ATOM   4298 C  C   . ARG B 1 217 ? 0.693   20.452  -28.252 1.00 44.89  ? 217 ARG B C   1 
ATOM   4299 O  O   . ARG B 1 217 ? 0.527   21.637  -27.929 1.00 51.40  ? 217 ARG B O   1 
ATOM   4300 C  CB  . ARG B 1 217 ? 3.140   20.551  -28.221 1.00 47.87  ? 217 ARG B CB  1 
ATOM   4301 C  CG  . ARG B 1 217 ? 4.469   20.138  -27.612 1.00 52.96  ? 217 ARG B CG  1 
ATOM   4302 C  CD  . ARG B 1 217 ? 5.546   21.123  -28.021 1.00 58.59  ? 217 ARG B CD  1 
ATOM   4303 N  NE  . ARG B 1 217 ? 5.321   22.458  -27.470 1.00 62.31  ? 217 ARG B NE  1 
ATOM   4304 C  CZ  . ARG B 1 217 ? 5.935   22.976  -26.399 1.00 61.36  ? 217 ARG B CZ  1 
ATOM   4305 N  NH1 . ARG B 1 217 ? 6.834   22.281  -25.717 1.00 59.14  ? 217 ARG B NH1 1 
ATOM   4306 N  NH2 . ARG B 1 217 ? 5.635   24.202  -26.008 1.00 64.27  ? 217 ARG B NH2 1 
ATOM   4307 N  N   . TRP B 1 218 ? -0.137  19.769  -29.040 1.00 43.08  ? 218 TRP B N   1 
ATOM   4308 C  CA  . TRP B 1 218 ? -1.193  20.398  -29.869 1.00 44.94  ? 218 TRP B CA  1 
ATOM   4309 C  C   . TRP B 1 218 ? -2.223  21.154  -29.022 1.00 51.00  ? 218 TRP B C   1 
ATOM   4310 O  O   . TRP B 1 218 ? -2.760  22.155  -29.537 1.00 50.97  ? 218 TRP B O   1 
ATOM   4311 C  CB  . TRP B 1 218 ? -1.875  19.363  -30.759 1.00 41.29  ? 218 TRP B CB  1 
ATOM   4312 C  CG  . TRP B 1 218 ? -2.574  18.248  -30.058 1.00 45.89  ? 218 TRP B CG  1 
ATOM   4313 C  CD1 . TRP B 1 218 ? -2.107  16.976  -29.898 1.00 47.51  ? 218 TRP B CD1 1 
ATOM   4314 C  CD2 . TRP B 1 218 ? -3.912  18.254  -29.524 1.00 50.84  ? 218 TRP B CD2 1 
ATOM   4315 N  NE1 . TRP B 1 218 ? -3.053  16.193  -29.293 1.00 50.92  ? 218 TRP B NE1 1 
ATOM   4316 C  CE2 . TRP B 1 218 ? -4.172  16.946  -29.056 1.00 48.04  ? 218 TRP B CE2 1 
ATOM   4317 C  CE3 . TRP B 1 218 ? -4.919  19.225  -29.410 1.00 57.70  ? 218 TRP B CE3 1 
ATOM   4318 C  CZ2 . TRP B 1 218 ? -5.376  16.599  -28.449 1.00 52.89  ? 218 TRP B CZ2 1 
ATOM   4319 C  CZ3 . TRP B 1 218 ? -6.120  18.876  -28.822 1.00 57.34  ? 218 TRP B CZ3 1 
ATOM   4320 C  CH2 . TRP B 1 218 ? -6.339  17.583  -28.337 1.00 57.58  ? 218 TRP B CH2 1 
ATOM   4321 N  N   . PHE B 1 219 ? -2.532  20.648  -27.820 1.00 51.17  ? 219 PHE B N   1 
ATOM   4322 C  CA  . PHE B 1 219 ? -3.639  21.101  -26.928 1.00 43.64  ? 219 PHE B CA  1 
ATOM   4323 C  C   . PHE B 1 219 ? -3.177  22.343  -26.182 1.00 40.70  ? 219 PHE B C   1 
ATOM   4324 O  O   . PHE B 1 219 ? -3.976  22.945  -25.459 1.00 48.46  ? 219 PHE B O   1 
ATOM   4325 C  CB  . PHE B 1 219 ? -4.051  19.997  -25.941 1.00 41.25  ? 219 PHE B CB  1 
ATOM   4326 C  CG  . PHE B 1 219 ? -2.882  19.363  -25.226 1.00 39.97  ? 219 PHE B CG  1 
ATOM   4327 C  CD1 . PHE B 1 219 ? -2.269  19.993  -24.152 1.00 39.97  ? 219 PHE B CD1 1 
ATOM   4328 C  CD2 . PHE B 1 219 ? -2.350  18.156  -25.667 1.00 40.31  ? 219 PHE B CD2 1 
ATOM   4329 C  CE1 . PHE B 1 219 ? -1.165  19.431  -23.527 1.00 39.42  ? 219 PHE B CE1 1 
ATOM   4330 C  CE2 . PHE B 1 219 ? -1.243  17.602  -25.042 1.00 33.86  ? 219 PHE B CE2 1 
ATOM   4331 C  CZ  . PHE B 1 219 ? -0.646  18.240  -23.988 1.00 35.89  ? 219 PHE B CZ  1 
ATOM   4332 N  N   . LEU B 1 220 ? -1.898  22.688  -26.274 1.00 38.51  ? 220 LEU B N   1 
ATOM   4333 C  CA  . LEU B 1 220 ? -1.402  23.896  -25.589 1.00 44.63  ? 220 LEU B CA  1 
ATOM   4334 C  C   . LEU B 1 220 ? -2.040  25.126  -26.253 1.00 49.95  ? 220 LEU B C   1 
ATOM   4335 O  O   . LEU B 1 220 ? -2.569  24.996  -27.381 1.00 49.86  ? 220 LEU B O   1 
ATOM   4336 C  CB  . LEU B 1 220 ? 0.121   23.967  -25.654 1.00 47.70  ? 220 LEU B CB  1 
ATOM   4337 C  CG  . LEU B 1 220 ? 0.884   22.966  -24.793 1.00 48.77  ? 220 LEU B CG  1 
ATOM   4338 C  CD1 . LEU B 1 220 ? 2.370   23.191  -24.952 1.00 47.78  ? 220 LEU B CD1 1 
ATOM   4339 C  CD2 . LEU B 1 220 ? 0.494   23.048  -23.322 1.00 50.39  ? 220 LEU B CD2 1 
ATOM   4340 N  N   . ASN B 1 221 ? -2.052  26.256  -25.540 1.00 51.81  ? 221 ASN B N   1 
ATOM   4341 C  CA  . ASN B 1 221 ? -2.640  27.531  -26.028 1.00 47.36  ? 221 ASN B CA  1 
ATOM   4342 C  C   . ASN B 1 221 ? -2.004  28.706  -25.289 1.00 48.06  ? 221 ASN B C   1 
ATOM   4343 O  O   . ASN B 1 221 ? -1.285  28.494  -24.284 1.00 43.80  ? 221 ASN B O   1 
ATOM   4344 C  CB  . ASN B 1 221 ? -4.166  27.549  -25.947 1.00 43.89  ? 221 ASN B CB  1 
ATOM   4345 C  CG  . ASN B 1 221 ? -4.725  27.392  -24.547 1.00 46.35  ? 221 ASN B CG  1 
ATOM   4346 O  OD1 . ASN B 1 221 ? -4.097  27.750  -23.542 1.00 42.23  ? 221 ASN B OD1 1 
ATOM   4347 N  ND2 . ASN B 1 221 ? -5.925  26.847  -24.481 1.00 36.87  ? 221 ASN B ND2 1 
ATOM   4348 N  N   . ARG B 1 222 ? -2.263  29.909  -25.802 1.00 46.26  ? 222 ARG B N   1 
ATOM   4349 C  CA  . ARG B 1 222 ? -1.693  31.189  -25.300 1.00 42.99  ? 222 ARG B CA  1 
ATOM   4350 C  C   . ARG B 1 222 ? -2.342  31.603  -23.970 1.00 37.44  ? 222 ARG B C   1 
ATOM   4351 O  O   . ARG B 1 222 ? -1.812  32.540  -23.348 1.00 36.71  ? 222 ARG B O   1 
ATOM   4352 C  CB  . ARG B 1 222 ? -1.877  32.291  -26.352 1.00 45.21  ? 222 ARG B CB  1 
ATOM   4353 C  CG  . ARG B 1 222 ? -3.327  32.583  -26.724 1.00 46.03  ? 222 ARG B CG  1 
ATOM   4354 C  CD  . ARG B 1 222 ? -3.534  33.883  -27.494 1.00 49.42  ? 222 ARG B CD  1 
ATOM   4355 N  NE  . ARG B 1 222 ? -2.659  34.133  -28.642 1.00 50.55  ? 222 ARG B NE  1 
ATOM   4356 C  CZ  . ARG B 1 222 ? -1.648  35.018  -28.670 1.00 47.96  ? 222 ARG B CZ  1 
ATOM   4357 N  NH1 . ARG B 1 222 ? -1.326  35.737  -27.604 1.00 57.05  ? 222 ARG B NH1 1 
ATOM   4358 N  NH2 . ARG B 1 222 ? -0.947  35.182  -29.776 1.00 49.03  ? 222 ARG B NH2 1 
ATOM   4359 N  N   . PHE B 1 223 ? -3.444  30.975  -23.561 1.00 37.42  ? 223 PHE B N   1 
ATOM   4360 C  CA  . PHE B 1 223 ? -4.339  31.492  -22.485 1.00 42.34  ? 223 PHE B CA  1 
ATOM   4361 C  C   . PHE B 1 223 ? -3.860  31.057  -21.096 1.00 52.89  ? 223 PHE B C   1 
ATOM   4362 O  O   . PHE B 1 223 ? -2.982  30.143  -20.960 1.00 53.44  ? 223 PHE B O   1 
ATOM   4363 C  CB  . PHE B 1 223 ? -5.783  31.061  -22.733 1.00 41.74  ? 223 PHE B CB  1 
ATOM   4364 C  CG  . PHE B 1 223 ? -6.319  31.570  -24.044 1.00 41.18  ? 223 PHE B CG  1 
ATOM   4365 C  CD1 . PHE B 1 223 ? -6.414  32.941  -24.277 1.00 42.01  ? 223 PHE B CD1 1 
ATOM   4366 C  CD2 . PHE B 1 223 ? -6.658  30.695  -25.066 1.00 39.22  ? 223 PHE B CD2 1 
ATOM   4367 C  CE1 . PHE B 1 223 ? -6.870  33.425  -25.498 1.00 40.37  ? 223 PHE B CE1 1 
ATOM   4368 C  CE2 . PHE B 1 223 ? -7.127  31.178  -26.279 1.00 41.37  ? 223 PHE B CE2 1 
ATOM   4369 C  CZ  . PHE B 1 223 ? -7.218  32.542  -26.500 1.00 41.95  ? 223 PHE B CZ  1 
ATOM   4370 N  N   . THR B 1 224 ? -4.410  31.722  -20.075 1.00 50.05  ? 224 THR B N   1 
ATOM   4371 C  CA  . THR B 1 224 ? -4.330  31.275  -18.663 1.00 53.61  ? 224 THR B CA  1 
ATOM   4372 C  C   . THR B 1 224 ? -5.714  31.391  -18.001 1.00 56.05  ? 224 THR B C   1 
ATOM   4373 O  O   . THR B 1 224 ? -6.749  31.505  -18.713 1.00 54.37  ? 224 THR B O   1 
ATOM   4374 C  CB  . THR B 1 224 ? -3.183  31.974  -17.929 1.00 56.11  ? 224 THR B CB  1 
ATOM   4375 O  OG1 . THR B 1 224 ? -3.096  31.282  -16.685 1.00 56.67  ? 224 THR B OG1 1 
ATOM   4376 C  CG2 . THR B 1 224 ? -3.397  33.455  -17.701 1.00 58.46  ? 224 THR B CG2 1 
ATOM   4377 N  N   . THR B 1 225 ? -5.764  31.258  -16.681 1.00 55.16  ? 225 THR B N   1 
ATOM   4378 C  CA  . THR B 1 225 ? -7.048  31.197  -15.953 1.00 54.07  ? 225 THR B CA  1 
ATOM   4379 C  C   . THR B 1 225 ? -6.807  31.333  -14.458 1.00 54.32  ? 225 THR B C   1 
ATOM   4380 O  O   . THR B 1 225 ? -5.647  31.588  -14.071 1.00 49.59  ? 225 THR B O   1 
ATOM   4381 C  CB  . THR B 1 225 ? -7.794  29.891  -16.212 1.00 57.03  ? 225 THR B CB  1 
ATOM   4382 O  OG1 . THR B 1 225 ? -9.115  30.089  -15.707 1.00 59.00  ? 225 THR B OG1 1 
ATOM   4383 C  CG2 . THR B 1 225 ? -7.133  28.702  -15.548 1.00 59.50  ? 225 THR B CG2 1 
ATOM   4384 N  N   . THR B 1 226 ? -7.887  31.173  -13.680 1.00 53.18  ? 226 THR B N   1 
ATOM   4385 C  CA  . THR B 1 226 ? -7.870  31.188  -12.194 1.00 52.15  ? 226 THR B CA  1 
ATOM   4386 C  C   . THR B 1 226 ? -8.415  29.862  -11.654 1.00 44.61  ? 226 THR B C   1 
ATOM   4387 O  O   . THR B 1 226 ? -9.338  29.246  -12.300 1.00 40.73  ? 226 THR B O   1 
ATOM   4388 C  CB  . THR B 1 226 ? -8.670  32.372  -11.639 1.00 45.46  ? 226 THR B CB  1 
ATOM   4389 O  OG1 . THR B 1 226 ? -10.028 32.140  -12.008 1.00 40.46  ? 226 THR B OG1 1 
ATOM   4390 C  CG2 . THR B 1 226 ? -8.190  33.703  -12.173 1.00 49.92  ? 226 THR B CG2 1 
ATOM   4391 N  N   . LEU B 1 227 ? -7.861  29.467  -10.505 1.00 47.86  ? 227 LEU B N   1 
ATOM   4392 C  CA  . LEU B 1 227 ? -8.368  28.365  -9.654  1.00 46.58  ? 227 LEU B CA  1 
ATOM   4393 C  C   . LEU B 1 227 ? -9.900  28.423  -9.648  1.00 49.31  ? 227 LEU B C   1 
ATOM   4394 O  O   . LEU B 1 227 ? -10.531 27.419  -10.061 1.00 48.66  ? 227 LEU B O   1 
ATOM   4395 C  CB  . LEU B 1 227 ? -7.740  28.518  -8.265  1.00 49.69  ? 227 LEU B CB  1 
ATOM   4396 C  CG  . LEU B 1 227 ? -7.175  27.243  -7.625  1.00 52.42  ? 227 LEU B CG  1 
ATOM   4397 C  CD1 . LEU B 1 227 ? -6.590  26.287  -8.658  1.00 52.50  ? 227 LEU B CD1 1 
ATOM   4398 C  CD2 . LEU B 1 227 ? -6.117  27.579  -6.576  1.00 51.56  ? 227 LEU B CD2 1 
ATOM   4399 N  N   . ASN B 1 228 ? -10.474 29.589  -9.325  1.00 52.27  ? 228 ASN B N   1 
ATOM   4400 C  CA  . ASN B 1 228 ? -11.938 29.762  -9.105  1.00 53.85  ? 228 ASN B CA  1 
ATOM   4401 C  C   . ASN B 1 228 ? -12.692 29.542  -10.417 1.00 52.81  ? 228 ASN B C   1 
ATOM   4402 O  O   . ASN B 1 228 ? -13.654 28.747  -10.423 1.00 52.11  ? 228 ASN B O   1 
ATOM   4403 C  CB  . ASN B 1 228 ? -12.271 31.128  -8.503  1.00 61.15  ? 228 ASN B CB  1 
ATOM   4404 C  CG  . ASN B 1 228 ? -11.312 31.502  -7.397  1.00 66.90  ? 228 ASN B CG  1 
ATOM   4405 O  OD1 . ASN B 1 228 ? -10.093 31.425  -7.576  1.00 68.58  ? 228 ASN B OD1 1 
ATOM   4406 N  ND2 . ASN B 1 228 ? -11.855 31.910  -6.264  1.00 71.44  ? 228 ASN B ND2 1 
ATOM   4407 N  N   . ASP B 1 229 ? -12.273 30.206  -11.499 1.00 54.68  ? 229 ASP B N   1 
ATOM   4408 C  CA  . ASP B 1 229 ? -12.910 30.026  -12.828 1.00 53.46  ? 229 ASP B CA  1 
ATOM   4409 C  C   . ASP B 1 229 ? -12.753 28.555  -13.227 1.00 50.41  ? 229 ASP B C   1 
ATOM   4410 O  O   . ASP B 1 229 ? -13.751 27.931  -13.691 1.00 45.01  ? 229 ASP B O   1 
ATOM   4411 C  CB  . ASP B 1 229 ? -12.321 30.985  -13.869 1.00 62.64  ? 229 ASP B CB  1 
ATOM   4412 C  CG  . ASP B 1 229 ? -12.739 32.439  -13.696 1.00 63.85  ? 229 ASP B CG  1 
ATOM   4413 O  OD1 . ASP B 1 229 ? -13.933 32.723  -13.880 1.00 58.47  ? 229 ASP B OD1 1 
ATOM   4414 O  OD2 . ASP B 1 229 ? -11.865 33.273  -13.363 1.00 66.28  ? 229 ASP B OD2 1 
ATOM   4415 N  N   . PHE B 1 230 ? -11.551 27.995  -13.057 1.00 51.61  ? 230 PHE B N   1 
ATOM   4416 C  CA  . PHE B 1 230 ? -11.299 26.580  -13.443 1.00 46.10  ? 230 PHE B CA  1 
ATOM   4417 C  C   . PHE B 1 230 ? -12.210 25.661  -12.611 1.00 45.13  ? 230 PHE B C   1 
ATOM   4418 O  O   . PHE B 1 230 ? -12.911 24.787  -13.189 1.00 48.06  ? 230 PHE B O   1 
ATOM   4419 C  CB  . PHE B 1 230 ? -9.822  26.210  -13.334 1.00 48.93  ? 230 PHE B CB  1 
ATOM   4420 C  CG  . PHE B 1 230 ? -9.594  24.767  -13.708 1.00 49.45  ? 230 PHE B CG  1 
ATOM   4421 C  CD1 . PHE B 1 230 ? -9.829  24.329  -15.004 1.00 48.66  ? 230 PHE B CD1 1 
ATOM   4422 C  CD2 . PHE B 1 230 ? -9.244  23.834  -12.744 1.00 47.20  ? 230 PHE B CD2 1 
ATOM   4423 C  CE1 . PHE B 1 230 ? -9.676  22.993  -15.337 1.00 48.35  ? 230 PHE B CE1 1 
ATOM   4424 C  CE2 . PHE B 1 230 ? -9.094  22.501  -13.080 1.00 44.15  ? 230 PHE B CE2 1 
ATOM   4425 C  CZ  . PHE B 1 230 ? -9.304  22.087  -14.375 1.00 45.87  ? 230 PHE B CZ  1 
ATOM   4426 N  N   . ASN B 1 231 ? -12.279 25.892  -11.296 1.00 46.32  ? 231 ASN B N   1 
ATOM   4427 C  CA  . ASN B 1 231 ? -12.939 24.953  -10.347 1.00 44.88  ? 231 ASN B CA  1 
ATOM   4428 C  C   . ASN B 1 231 ? -14.448 24.940  -10.608 1.00 49.32  ? 231 ASN B C   1 
ATOM   4429 O  O   . ASN B 1 231 ? -15.077 23.863  -10.427 1.00 56.30  ? 231 ASN B O   1 
ATOM   4430 C  CB  . ASN B 1 231 ? -12.486 25.211  -8.905  1.00 48.62  ? 231 ASN B CB  1 
ATOM   4431 C  CG  . ASN B 1 231 ? -11.213 24.453  -8.567  1.00 47.23  ? 231 ASN B CG  1 
ATOM   4432 O  OD1 . ASN B 1 231 ? -11.076 23.284  -8.932  1.00 45.55  ? 231 ASN B OD1 1 
ATOM   4433 N  ND2 . ASN B 1 231 ? -10.270 25.094  -7.891  1.00 42.10  ? 231 ASN B ND2 1 
ATOM   4434 N  N   . LEU B 1 232 ? -15.011 26.038  -11.120 1.00 53.71  ? 232 LEU B N   1 
ATOM   4435 C  CA  . LEU B 1 232 ? -16.440 26.079  -11.525 1.00 55.42  ? 232 LEU B CA  1 
ATOM   4436 C  C   . LEU B 1 232 ? -16.660 25.205  -12.760 1.00 54.48  ? 232 LEU B C   1 
ATOM   4437 O  O   . LEU B 1 232 ? -17.763 24.643  -12.896 1.00 58.03  ? 232 LEU B O   1 
ATOM   4438 C  CB  . LEU B 1 232 ? -16.852 27.530  -11.776 1.00 65.58  ? 232 LEU B CB  1 
ATOM   4439 C  CG  . LEU B 1 232 ? -17.001 28.368  -10.507 1.00 71.45  ? 232 LEU B CG  1 
ATOM   4440 C  CD1 . LEU B 1 232 ? -16.940 29.858  -10.823 1.00 73.83  ? 232 LEU B CD1 1 
ATOM   4441 C  CD2 . LEU B 1 232 ? -18.286 28.007  -9.766  1.00 66.19  ? 232 LEU B CD2 1 
ATOM   4442 N  N   . VAL B 1 233 ? -15.653 25.086  -13.625 1.00 58.24  ? 233 VAL B N   1 
ATOM   4443 C  CA  . VAL B 1 233 ? -15.679 24.165  -14.803 1.00 61.63  ? 233 VAL B CA  1 
ATOM   4444 C  C   . VAL B 1 233 ? -15.517 22.725  -14.296 1.00 56.49  ? 233 VAL B C   1 
ATOM   4445 O  O   . VAL B 1 233 ? -16.362 21.874  -14.645 1.00 54.19  ? 233 VAL B O   1 
ATOM   4446 C  CB  . VAL B 1 233 ? -14.589 24.528  -15.838 1.00 69.40  ? 233 VAL B CB  1 
ATOM   4447 C  CG1 . VAL B 1 233 ? -14.602 23.576  -17.026 1.00 70.21  ? 233 VAL B CG1 1 
ATOM   4448 C  CG2 . VAL B 1 233 ? -14.706 25.974  -16.311 1.00 65.28  ? 233 VAL B CG2 1 
ATOM   4449 N  N   . ALA B 1 234 ? -14.479 22.468  -13.489 1.00 60.23  ? 234 ALA B N   1 
ATOM   4450 C  CA  . ALA B 1 234 ? -14.161 21.134  -12.920 1.00 57.86  ? 234 ALA B CA  1 
ATOM   4451 C  C   . ALA B 1 234 ? -15.412 20.553  -12.248 1.00 61.46  ? 234 ALA B C   1 
ATOM   4452 O  O   . ALA B 1 234 ? -15.904 19.471  -12.691 1.00 55.61  ? 234 ALA B O   1 
ATOM   4453 C  CB  . ALA B 1 234 ? -13.011 21.238  -11.945 1.00 57.19  ? 234 ALA B CB  1 
ATOM   4454 N  N   . MET B 1 235 ? -15.927 21.265  -11.237 1.00 64.46  ? 235 MET B N   1 
ATOM   4455 C  CA  . MET B 1 235 ? -17.147 20.865  -10.494 1.00 62.90  ? 235 MET B CA  1 
ATOM   4456 C  C   . MET B 1 235 ? -18.238 20.487  -11.500 1.00 57.41  ? 235 MET B C   1 
ATOM   4457 O  O   . MET B 1 235 ? -18.952 19.524  -11.224 1.00 49.08  ? 235 MET B O   1 
ATOM   4458 C  CB  . MET B 1 235 ? -17.654 21.980  -9.573  1.00 70.90  ? 235 MET B CB  1 
ATOM   4459 C  CG  . MET B 1 235 ? -18.878 21.565  -8.757  1.00 76.09  ? 235 MET B CG  1 
ATOM   4460 S  SD  . MET B 1 235 ? -19.462 22.817  -7.566  1.00 81.13  ? 235 MET B SD  1 
ATOM   4461 C  CE  . MET B 1 235 ? -18.498 22.421  -6.109  1.00 78.84  ? 235 MET B CE  1 
ATOM   4462 N  N   . LYS B 1 236 ? -18.328 21.192  -12.637 1.00 60.99  ? 236 LYS B N   1 
ATOM   4463 C  CA  . LYS B 1 236 ? -19.355 20.953  -13.691 1.00 60.15  ? 236 LYS B CA  1 
ATOM   4464 C  C   . LYS B 1 236 ? -19.118 19.605  -14.377 1.00 57.04  ? 236 LYS B C   1 
ATOM   4465 O  O   . LYS B 1 236 ? -20.113 18.961  -14.752 1.00 50.45  ? 236 LYS B O   1 
ATOM   4466 C  CB  . LYS B 1 236 ? -19.363 22.073  -14.743 1.00 71.91  ? 236 LYS B CB  1 
ATOM   4467 C  CG  . LYS B 1 236 ? -20.462 21.957  -15.802 1.00 80.06  ? 236 LYS B CG  1 
ATOM   4468 C  CD  . LYS B 1 236 ? -20.486 23.068  -16.857 1.00 88.16  ? 236 LYS B CD  1 
ATOM   4469 C  CE  . LYS B 1 236 ? -20.516 24.477  -16.293 1.00 91.03  ? 236 LYS B CE  1 
ATOM   4470 N  NZ  . LYS B 1 236 ? -21.619 24.668  -15.318 1.00 98.97  ? 236 LYS B NZ  1 
ATOM   4471 N  N   . TYR B 1 237 ? -17.856 19.206  -14.573 1.00 60.40  ? 237 TYR B N   1 
ATOM   4472 C  CA  . TYR B 1 237 ? -17.492 18.003  -15.372 1.00 58.50  ? 237 TYR B CA  1 
ATOM   4473 C  C   . TYR B 1 237 ? -17.230 16.797  -14.455 1.00 58.85  ? 237 TYR B C   1 
ATOM   4474 O  O   . TYR B 1 237 ? -16.817 15.750  -14.993 1.00 46.40  ? 237 TYR B O   1 
ATOM   4475 C  CB  . TYR B 1 237 ? -16.329 18.343  -16.310 1.00 56.85  ? 237 TYR B CB  1 
ATOM   4476 C  CG  . TYR B 1 237 ? -16.750 19.247  -17.443 1.00 60.23  ? 237 TYR B CG  1 
ATOM   4477 C  CD1 . TYR B 1 237 ? -17.361 18.733  -18.576 1.00 61.93  ? 237 TYR B CD1 1 
ATOM   4478 C  CD2 . TYR B 1 237 ? -16.603 20.625  -17.357 1.00 63.76  ? 237 TYR B CD2 1 
ATOM   4479 C  CE1 . TYR B 1 237 ? -17.782 19.556  -19.607 1.00 62.45  ? 237 TYR B CE1 1 
ATOM   4480 C  CE2 . TYR B 1 237 ? -17.020 21.463  -18.379 1.00 61.16  ? 237 TYR B CE2 1 
ATOM   4481 C  CZ  . TYR B 1 237 ? -17.615 20.924  -19.504 1.00 59.14  ? 237 TYR B CZ  1 
ATOM   4482 O  OH  . TYR B 1 237 ? -18.031 21.741  -20.510 1.00 66.06  ? 237 TYR B OH  1 
ATOM   4483 N  N   . ASN B 1 238 ? -17.532 16.913  -13.150 1.00 56.22  ? 238 ASN B N   1 
ATOM   4484 C  CA  . ASN B 1 238 ? -17.251 15.874  -12.119 1.00 52.65  ? 238 ASN B CA  1 
ATOM   4485 C  C   . ASN B 1 238 ? -15.737 15.671  -12.031 1.00 48.87  ? 238 ASN B C   1 
ATOM   4486 O  O   . ASN B 1 238 ? -15.280 14.527  -12.056 1.00 48.33  ? 238 ASN B O   1 
ATOM   4487 C  CB  . ASN B 1 238 ? -17.966 14.556  -12.408 1.00 57.02  ? 238 ASN B CB  1 
ATOM   4488 C  CG  . ASN B 1 238 ? -19.420 14.627  -12.028 1.00 62.05  ? 238 ASN B CG  1 
ATOM   4489 O  OD1 . ASN B 1 238 ? -19.745 14.935  -10.888 1.00 67.09  ? 238 ASN B OD1 1 
ATOM   4490 N  ND2 . ASN B 1 238 ? -20.296 14.369  -12.980 1.00 69.40  ? 238 ASN B ND2 1 
ATOM   4491 N  N   . TYR B 1 239 ? -15.007 16.773  -11.995 1.00 43.74  ? 239 TYR B N   1 
ATOM   4492 C  CA  . TYR B 1 239 ? -13.570 16.831  -11.684 1.00 46.68  ? 239 TYR B CA  1 
ATOM   4493 C  C   . TYR B 1 239 ? -13.466 17.265  -10.230 1.00 48.06  ? 239 TYR B C   1 
ATOM   4494 O  O   . TYR B 1 239 ? -14.246 18.130  -9.812  1.00 53.89  ? 239 TYR B O   1 
ATOM   4495 C  CB  . TYR B 1 239 ? -12.844 17.787  -12.635 1.00 45.40  ? 239 TYR B CB  1 
ATOM   4496 C  CG  . TYR B 1 239 ? -12.330 17.139  -13.894 1.00 41.47  ? 239 TYR B CG  1 
ATOM   4497 C  CD1 . TYR B 1 239 ? -13.185 16.457  -14.740 1.00 42.67  ? 239 TYR B CD1 1 
ATOM   4498 C  CD2 . TYR B 1 239 ? -10.985 17.199  -14.234 1.00 39.03  ? 239 TYR B CD2 1 
ATOM   4499 C  CE1 . TYR B 1 239 ? -12.720 15.844  -15.893 1.00 42.45  ? 239 TYR B CE1 1 
ATOM   4500 C  CE2 . TYR B 1 239 ? -10.502 16.574  -15.369 1.00 37.43  ? 239 TYR B CE2 1 
ATOM   4501 C  CZ  . TYR B 1 239 ? -11.372 15.910  -16.207 1.00 39.03  ? 239 TYR B CZ  1 
ATOM   4502 O  OH  . TYR B 1 239 ? -10.893 15.332  -17.344 1.00 43.80  ? 239 TYR B OH  1 
ATOM   4503 N  N   . GLU B 1 240 ? -12.555 16.635  -9.496  1.00 45.40  ? 240 GLU B N   1 
ATOM   4504 C  CA  . GLU B 1 240 ? -12.119 17.059  -8.149  1.00 43.37  ? 240 GLU B CA  1 
ATOM   4505 C  C   . GLU B 1 240 ? -11.716 18.517  -8.270  1.00 43.05  ? 240 GLU B C   1 
ATOM   4506 O  O   . GLU B 1 240 ? -11.302 18.942  -9.338  1.00 41.54  ? 240 GLU B O   1 
ATOM   4507 C  CB  . GLU B 1 240 ? -10.948 16.208  -7.650  1.00 41.55  ? 240 GLU B CB  1 
ATOM   4508 C  CG  . GLU B 1 240 ? -11.345 14.788  -7.327  1.00 48.49  ? 240 GLU B CG  1 
ATOM   4509 C  CD  . GLU B 1 240 ? -11.999 14.695  -5.965  1.00 51.83  ? 240 GLU B CD  1 
ATOM   4510 O  OE1 . GLU B 1 240 ? -11.270 14.821  -4.955  1.00 52.54  ? 240 GLU B OE1 1 
ATOM   4511 O  OE2 . GLU B 1 240 ? -13.223 14.531  -5.926  1.00 48.50  ? 240 GLU B OE2 1 
ATOM   4512 N  N   . PRO B 1 241 ? -11.873 19.329  -7.204  1.00 42.14  ? 241 PRO B N   1 
ATOM   4513 C  CA  . PRO B 1 241 ? -11.295 20.664  -7.174  1.00 42.28  ? 241 PRO B CA  1 
ATOM   4514 C  C   . PRO B 1 241 ? -9.764  20.619  -7.152  1.00 44.90  ? 241 PRO B C   1 
ATOM   4515 O  O   . PRO B 1 241 ? -9.183  19.753  -6.491  1.00 48.32  ? 241 PRO B O   1 
ATOM   4516 C  CB  . PRO B 1 241 ? -11.828 21.285  -5.875  1.00 42.25  ? 241 PRO B CB  1 
ATOM   4517 C  CG  . PRO B 1 241 ? -13.040 20.441  -5.540  1.00 45.54  ? 241 PRO B CG  1 
ATOM   4518 C  CD  . PRO B 1 241 ? -12.685 19.048  -6.015  1.00 45.81  ? 241 PRO B CD  1 
ATOM   4519 N  N   . LEU B 1 242 ? -9.154  21.547  -7.890  1.00 44.06  ? 242 LEU B N   1 
ATOM   4520 C  CA  . LEU B 1 242 ? -7.711  21.856  -7.823  1.00 40.25  ? 242 LEU B CA  1 
ATOM   4521 C  C   . LEU B 1 242 ? -7.486  22.825  -6.672  1.00 43.27  ? 242 LEU B C   1 
ATOM   4522 O  O   . LEU B 1 242 ? -8.139  23.870  -6.646  1.00 43.72  ? 242 LEU B O   1 
ATOM   4523 C  CB  . LEU B 1 242 ? -7.252  22.491  -9.136  1.00 43.35  ? 242 LEU B CB  1 
ATOM   4524 C  CG  . LEU B 1 242 ? -5.742  22.456  -9.366  1.00 42.19  ? 242 LEU B CG  1 
ATOM   4525 C  CD1 . LEU B 1 242 ? -5.257  21.008  -9.507  1.00 41.20  ? 242 LEU B CD1 1 
ATOM   4526 C  CD2 . LEU B 1 242 ? -5.372  23.265  -10.603 1.00 44.07  ? 242 LEU B CD2 1 
ATOM   4527 N  N   . THR B 1 243 ? -6.571  22.478  -5.778  1.00 48.50  ? 243 THR B N   1 
ATOM   4528 C  CA  . THR B 1 243 ? -6.179  23.302  -4.618  1.00 48.29  ? 243 THR B CA  1 
ATOM   4529 C  C   . THR B 1 243 ? -4.848  23.950  -4.946  1.00 47.42  ? 243 THR B C   1 
ATOM   4530 O  O   . THR B 1 243 ? -4.185  23.498  -5.882  1.00 42.18  ? 243 THR B O   1 
ATOM   4531 C  CB  . THR B 1 243 ? -6.115  22.465  -3.336  1.00 45.67  ? 243 THR B CB  1 
ATOM   4532 O  OG1 . THR B 1 243 ? -5.093  21.485  -3.481  1.00 43.69  ? 243 THR B OG1 1 
ATOM   4533 C  CG2 . THR B 1 243 ? -7.425  21.774  -3.027  1.00 46.41  ? 243 THR B CG2 1 
ATOM   4534 N  N   . GLN B 1 244 ? -4.505  24.982  -4.185  1.00 49.08  ? 244 GLN B N   1 
ATOM   4535 C  CA  . GLN B 1 244 ? -3.174  25.624  -4.195  1.00 50.04  ? 244 GLN B CA  1 
ATOM   4536 C  C   . GLN B 1 244 ? -2.058  24.585  -4.013  1.00 51.87  ? 244 GLN B C   1 
ATOM   4537 O  O   . GLN B 1 244 ? -0.943  24.827  -4.514  1.00 51.42  ? 244 GLN B O   1 
ATOM   4538 C  CB  . GLN B 1 244 ? -3.052  26.635  -3.051  1.00 50.19  ? 244 GLN B CB  1 
ATOM   4539 C  CG  . GLN B 1 244 ? -1.661  27.252  -2.981  1.00 50.37  ? 244 GLN B CG  1 
ATOM   4540 C  CD  . GLN B 1 244 ? -1.242  27.697  -4.359  1.00 49.37  ? 244 GLN B CD  1 
ATOM   4541 O  OE1 . GLN B 1 244 ? -2.044  28.239  -5.118  1.00 48.23  ? 244 GLN B OE1 1 
ATOM   4542 N  NE2 . GLN B 1 244 ? 0.006   27.436  -4.707  1.00 57.94  ? 244 GLN B NE2 1 
ATOM   4543 N  N   . ASP B 1 245 ? -2.301  23.525  -3.241  1.00 48.30  ? 245 ASP B N   1 
ATOM   4544 C  CA  . ASP B 1 245 ? -1.269  22.499  -2.936  1.00 50.70  ? 245 ASP B CA  1 
ATOM   4545 C  C   . ASP B 1 245 ? -0.982  21.678  -4.212  1.00 45.30  ? 245 ASP B C   1 
ATOM   4546 O  O   . ASP B 1 245 ? 0.192   21.393  -4.492  1.00 42.06  ? 245 ASP B O   1 
ATOM   4547 C  CB  . ASP B 1 245 ? -1.708  21.646  -1.744  1.00 52.46  ? 245 ASP B CB  1 
ATOM   4548 C  CG  . ASP B 1 245 ? -0.719  20.552  -1.400  1.00 62.89  ? 245 ASP B CG  1 
ATOM   4549 O  OD1 . ASP B 1 245 ? 0.505   20.819  -1.485  1.00 70.02  ? 245 ASP B OD1 1 
ATOM   4550 O  OD2 . ASP B 1 245 ? -1.179  19.432  -1.078  1.00 68.08  ? 245 ASP B OD2 1 
ATOM   4551 N  N   . HIS B 1 246 ? -2.023  21.323  -4.961  1.00 41.35  ? 246 HIS B N   1 
ATOM   4552 C  CA  . HIS B 1 246 ? -1.919  20.600  -6.254  1.00 41.17  ? 246 HIS B CA  1 
ATOM   4553 C  C   . HIS B 1 246 ? -1.038  21.400  -7.218  1.00 43.37  ? 246 HIS B C   1 
ATOM   4554 O  O   . HIS B 1 246 ? -0.205  20.784  -7.923  1.00 38.61  ? 246 HIS B O   1 
ATOM   4555 C  CB  . HIS B 1 246 ? -3.307  20.381  -6.854  1.00 39.04  ? 246 HIS B CB  1 
ATOM   4556 C  CG  . HIS B 1 246 ? -4.171  19.432  -6.094  1.00 39.69  ? 246 HIS B CG  1 
ATOM   4557 N  ND1 . HIS B 1 246 ? -5.547  19.393  -6.267  1.00 44.50  ? 246 HIS B ND1 1 
ATOM   4558 C  CD2 . HIS B 1 246 ? -3.873  18.461  -5.204  1.00 40.97  ? 246 HIS B CD2 1 
ATOM   4559 C  CE1 . HIS B 1 246 ? -6.061  18.454  -5.499  1.00 44.30  ? 246 HIS B CE1 1 
ATOM   4560 N  NE2 . HIS B 1 246 ? -5.051  17.859  -4.843  1.00 40.07  ? 246 HIS B NE2 1 
ATOM   4561 N  N   . VAL B 1 247 ? -1.239  22.723  -7.258  1.00 44.71  ? 247 VAL B N   1 
ATOM   4562 C  CA  . VAL B 1 247 ? -0.464  23.662  -8.125  1.00 44.60  ? 247 VAL B CA  1 
ATOM   4563 C  C   . VAL B 1 247 ? 1.007   23.622  -7.704  1.00 45.65  ? 247 VAL B C   1 
ATOM   4564 O  O   . VAL B 1 247 ? 1.863   23.645  -8.595  1.00 55.44  ? 247 VAL B O   1 
ATOM   4565 C  CB  . VAL B 1 247 ? -1.049  25.088  -8.083  1.00 44.90  ? 247 VAL B CB  1 
ATOM   4566 C  CG1 . VAL B 1 247 ? -0.137  26.116  -8.738  1.00 40.99  ? 247 VAL B CG1 1 
ATOM   4567 C  CG2 . VAL B 1 247 ? -2.440  25.138  -8.696  1.00 43.14  ? 247 VAL B CG2 1 
ATOM   4568 N  N   . ASP B 1 248 ? 1.288   23.563  -6.401  1.00 47.30  ? 248 ASP B N   1 
ATOM   4569 C  CA  . ASP B 1 248 ? 2.668   23.559  -5.839  1.00 49.38  ? 248 ASP B CA  1 
ATOM   4570 C  C   . ASP B 1 248 ? 3.370   22.231  -6.186  1.00 48.16  ? 248 ASP B C   1 
ATOM   4571 O  O   . ASP B 1 248 ? 4.583   22.250  -6.509  1.00 47.26  ? 248 ASP B O   1 
ATOM   4572 C  CB  . ASP B 1 248 ? 2.635   23.827  -4.326  1.00 51.80  ? 248 ASP B CB  1 
ATOM   4573 C  CG  . ASP B 1 248 ? 2.042   25.175  -3.906  1.00 51.12  ? 248 ASP B CG  1 
ATOM   4574 O  OD1 . ASP B 1 248 ? 1.898   26.071  -4.764  1.00 46.89  ? 248 ASP B OD1 1 
ATOM   4575 O  OD2 . ASP B 1 248 ? 1.713   25.324  -2.717  1.00 50.33  ? 248 ASP B OD2 1 
ATOM   4576 N  N   . ILE B 1 249 ? 2.647   21.107  -6.134  1.00 45.37  ? 249 ILE B N   1 
ATOM   4577 C  CA  . ILE B 1 249 ? 3.190   19.748  -6.450  1.00 42.04  ? 249 ILE B CA  1 
ATOM   4578 C  C   . ILE B 1 249 ? 3.513   19.666  -7.956  1.00 42.55  ? 249 ILE B C   1 
ATOM   4579 O  O   . ILE B 1 249 ? 4.528   19.033  -8.301  1.00 45.33  ? 249 ILE B O   1 
ATOM   4580 C  CB  . ILE B 1 249 ? 2.210   18.662  -5.970  1.00 46.13  ? 249 ILE B CB  1 
ATOM   4581 C  CG1 . ILE B 1 249 ? 1.983   18.753  -4.455  1.00 51.99  ? 249 ILE B CG1 1 
ATOM   4582 C  CG2 . ILE B 1 249 ? 2.706   17.285  -6.364  1.00 50.96  ? 249 ILE B CG2 1 
ATOM   4583 C  CD1 . ILE B 1 249 ? 0.706   18.078  -3.965  1.00 51.34  ? 249 ILE B CD1 1 
ATOM   4584 N  N   . LEU B 1 250 ? 2.734   20.324  -8.825  1.00 39.53  ? 250 LEU B N   1 
ATOM   4585 C  CA  . LEU B 1 250 ? 3.008   20.351  -10.293 1.00 42.27  ? 250 LEU B CA  1 
ATOM   4586 C  C   . LEU B 1 250 ? 4.134   21.342  -10.628 1.00 46.09  ? 250 LEU B C   1 
ATOM   4587 O  O   . LEU B 1 250 ? 4.458   21.444  -11.825 1.00 48.00  ? 250 LEU B O   1 
ATOM   4588 C  CB  . LEU B 1 250 ? 1.743   20.741  -11.057 1.00 41.17  ? 250 LEU B CB  1 
ATOM   4589 C  CG  . LEU B 1 250 ? 0.628   19.703  -11.062 1.00 41.94  ? 250 LEU B CG  1 
ATOM   4590 C  CD1 . LEU B 1 250 ? -0.679  20.328  -11.500 1.00 39.66  ? 250 LEU B CD1 1 
ATOM   4591 C  CD2 . LEU B 1 250 ? 0.987   18.519  -11.956 1.00 44.30  ? 250 LEU B CD2 1 
ATOM   4592 N  N   . GLY B 1 251 ? 4.674   22.065  -9.636  1.00 45.04  ? 251 GLY B N   1 
ATOM   4593 C  CA  . GLY B 1 251 ? 5.753   23.066  -9.789  1.00 46.11  ? 251 GLY B CA  1 
ATOM   4594 C  C   . GLY B 1 251 ? 6.870   22.614  -10.726 1.00 45.23  ? 251 GLY B C   1 
ATOM   4595 O  O   . GLY B 1 251 ? 7.155   23.277  -11.730 1.00 46.59  ? 251 GLY B O   1 
ATOM   4596 N  N   . PRO B 1 252 ? 7.539   21.480  -10.424 1.00 46.73  ? 252 PRO B N   1 
ATOM   4597 C  CA  . PRO B 1 252 ? 8.679   21.005  -11.216 1.00 47.13  ? 252 PRO B CA  1 
ATOM   4598 C  C   . PRO B 1 252 ? 8.406   20.805  -12.714 1.00 55.53  ? 252 PRO B C   1 
ATOM   4599 O  O   . PRO B 1 252 ? 9.276   21.127  -13.516 1.00 59.89  ? 252 PRO B O   1 
ATOM   4600 C  CB  . PRO B 1 252 ? 9.003   19.644  -10.594 1.00 47.94  ? 252 PRO B CB  1 
ATOM   4601 C  CG  . PRO B 1 252 ? 8.504   19.764  -9.170  1.00 45.80  ? 252 PRO B CG  1 
ATOM   4602 C  CD  . PRO B 1 252 ? 7.266   20.629  -9.259  1.00 46.59  ? 252 PRO B CD  1 
ATOM   4603 N  N   . LEU B 1 253 ? 7.225   20.270  -13.042 1.00 54.52  ? 253 LEU B N   1 
ATOM   4604 C  CA  . LEU B 1 253 ? 6.745   20.001  -14.424 1.00 46.42  ? 253 LEU B CA  1 
ATOM   4605 C  C   . LEU B 1 253 ? 6.428   21.327  -15.131 1.00 48.01  ? 253 LEU B C   1 
ATOM   4606 O  O   . LEU B 1 253 ? 6.617   21.417  -16.369 1.00 41.15  ? 253 LEU B O   1 
ATOM   4607 C  CB  . LEU B 1 253 ? 5.504   19.102  -14.333 1.00 46.43  ? 253 LEU B CB  1 
ATOM   4608 C  CG  . LEU B 1 253 ? 5.762   17.670  -13.846 1.00 47.52  ? 253 LEU B CG  1 
ATOM   4609 C  CD1 . LEU B 1 253 ? 4.461   16.949  -13.529 1.00 47.28  ? 253 LEU B CD1 1 
ATOM   4610 C  CD2 . LEU B 1 253 ? 6.553   16.874  -14.873 1.00 45.85  ? 253 LEU B CD2 1 
ATOM   4611 N  N   . SER B 1 254 ? 5.910   22.306  -14.381 1.00 48.65  ? 254 SER B N   1 
ATOM   4612 C  CA  . SER B 1 254 ? 5.558   23.662  -14.877 1.00 46.98  ? 254 SER B CA  1 
ATOM   4613 C  C   . SER B 1 254 ? 6.841   24.383  -15.295 1.00 49.29  ? 254 SER B C   1 
ATOM   4614 O  O   . SER B 1 254 ? 6.850   24.988  -16.397 1.00 50.60  ? 254 SER B O   1 
ATOM   4615 C  CB  . SER B 1 254 ? 4.810   24.467  -13.851 1.00 44.10  ? 254 SER B CB  1 
ATOM   4616 O  OG  . SER B 1 254 ? 4.729   25.824  -14.256 1.00 41.23  ? 254 SER B OG  1 
ATOM   4617 N  N   . ALA B 1 255 ? 7.873   24.298  -14.450 1.00 46.19  ? 255 ALA B N   1 
ATOM   4618 C  CA  . ALA B 1 255 ? 9.235   24.790  -14.743 1.00 51.03  ? 255 ALA B CA  1 
ATOM   4619 C  C   . ALA B 1 255 ? 9.774   24.047  -15.969 1.00 51.81  ? 255 ALA B C   1 
ATOM   4620 O  O   . ALA B 1 255 ? 9.961   24.699  -17.018 1.00 49.90  ? 255 ALA B O   1 
ATOM   4621 C  CB  . ALA B 1 255 ? 10.131  24.637  -13.547 1.00 51.30  ? 255 ALA B CB  1 
ATOM   4622 N  N   . GLN B 1 256 ? 9.926   22.724  -15.891 1.00 49.94  ? 256 GLN B N   1 
ATOM   4623 C  CA  . GLN B 1 256 ? 10.620  21.936  -16.953 1.00 49.51  ? 256 GLN B CA  1 
ATOM   4624 C  C   . GLN B 1 256 ? 10.029  22.227  -18.343 1.00 46.87  ? 256 GLN B C   1 
ATOM   4625 O  O   . GLN B 1 256 ? 10.740  22.035  -19.322 1.00 53.28  ? 256 GLN B O   1 
ATOM   4626 C  CB  . GLN B 1 256 ? 10.575  20.433  -16.676 1.00 52.62  ? 256 GLN B CB  1 
ATOM   4627 C  CG  . GLN B 1 256 ? 11.602  19.646  -17.478 1.00 55.69  ? 256 GLN B CG  1 
ATOM   4628 C  CD  . GLN B 1 256 ? 11.263  18.179  -17.601 1.00 54.83  ? 256 GLN B CD  1 
ATOM   4629 O  OE1 . GLN B 1 256 ? 10.965  17.504  -16.620 1.00 60.03  ? 256 GLN B OE1 1 
ATOM   4630 N  NE2 . GLN B 1 256 ? 11.333  17.666  -18.816 1.00 50.92  ? 256 GLN B NE2 1 
ATOM   4631 N  N   . THR B 1 257 ? 8.779   22.657  -18.452 1.00 43.55  ? 257 THR B N   1 
ATOM   4632 C  CA  . THR B 1 257 ? 8.080   22.753  -19.753 1.00 44.71  ? 257 THR B CA  1 
ATOM   4633 C  C   . THR B 1 257 ? 7.792   24.218  -20.141 1.00 40.30  ? 257 THR B C   1 
ATOM   4634 O  O   . THR B 1 257 ? 7.535   24.449  -21.313 1.00 39.70  ? 257 THR B O   1 
ATOM   4635 C  CB  . THR B 1 257 ? 6.789   21.926  -19.721 1.00 47.68  ? 257 THR B CB  1 
ATOM   4636 O  OG1 . THR B 1 257 ? 5.982   22.452  -18.663 1.00 50.42  ? 257 THR B OG1 1 
ATOM   4637 C  CG2 . THR B 1 257 ? 7.042   20.443  -19.543 1.00 48.06  ? 257 THR B CG2 1 
ATOM   4638 N  N   . GLY B 1 258 ? 7.729   25.157  -19.201 1.00 37.53  ? 258 GLY B N   1 
ATOM   4639 C  CA  . GLY B 1 258 ? 7.346   26.547  -19.508 1.00 39.78  ? 258 GLY B CA  1 
ATOM   4640 C  C   . GLY B 1 258 ? 5.835   26.759  -19.514 1.00 46.16  ? 258 GLY B C   1 
ATOM   4641 O  O   . GLY B 1 258 ? 5.403   27.903  -19.844 1.00 43.10  ? 258 GLY B O   1 
ATOM   4642 N  N   . ILE B 1 259 ? 5.047   25.739  -19.148 1.00 44.33  ? 259 ILE B N   1 
ATOM   4643 C  CA  . ILE B 1 259 ? 3.558   25.856  -19.058 1.00 52.02  ? 259 ILE B CA  1 
ATOM   4644 C  C   . ILE B 1 259 ? 3.158   25.814  -17.583 1.00 52.93  ? 259 ILE B C   1 
ATOM   4645 O  O   . ILE B 1 259 ? 3.359   24.766  -16.945 1.00 50.09  ? 259 ILE B O   1 
ATOM   4646 C  CB  . ILE B 1 259 ? 2.840   24.779  -19.892 1.00 53.52  ? 259 ILE B CB  1 
ATOM   4647 C  CG1 . ILE B 1 259 ? 3.356   24.761  -21.331 1.00 59.19  ? 259 ILE B CG1 1 
ATOM   4648 C  CG2 . ILE B 1 259 ? 1.330   24.964  -19.856 1.00 49.06  ? 259 ILE B CG2 1 
ATOM   4649 C  CD1 . ILE B 1 259 ? 4.500   23.825  -21.539 1.00 61.76  ? 259 ILE B CD1 1 
ATOM   4650 N  N   . ALA B 1 260 ? 2.640   26.932  -17.072 1.00 50.57  ? 260 ALA B N   1 
ATOM   4651 C  CA  . ALA B 1 260 ? 2.203   27.083  -15.672 1.00 49.68  ? 260 ALA B CA  1 
ATOM   4652 C  C   . ALA B 1 260 ? 0.838   26.420  -15.522 1.00 45.10  ? 260 ALA B C   1 
ATOM   4653 O  O   . ALA B 1 260 ? 0.126   26.251  -16.524 1.00 46.21  ? 260 ALA B O   1 
ATOM   4654 C  CB  . ALA B 1 260 ? 2.165   28.545  -15.290 1.00 56.90  ? 260 ALA B CB  1 
ATOM   4655 N  N   . VAL B 1 261 ? 0.494   26.030  -14.309 1.00 44.59  ? 261 VAL B N   1 
ATOM   4656 C  CA  . VAL B 1 261 ? -0.633  25.090  -14.059 1.00 41.31  ? 261 VAL B CA  1 
ATOM   4657 C  C   . VAL B 1 261 ? -1.927  25.687  -14.621 1.00 42.12  ? 261 VAL B C   1 
ATOM   4658 O  O   . VAL B 1 261 ? -2.660  24.980  -15.385 1.00 43.70  ? 261 VAL B O   1 
ATOM   4659 C  CB  . VAL B 1 261 ? -0.712  24.766  -12.554 1.00 41.18  ? 261 VAL B CB  1 
ATOM   4660 C  CG1 . VAL B 1 261 ? -1.908  23.870  -12.234 1.00 43.98  ? 261 VAL B CG1 1 
ATOM   4661 C  CG2 . VAL B 1 261 ? 0.590   24.147  -12.074 1.00 40.02  ? 261 VAL B CG2 1 
ATOM   4662 N  N   . LEU B 1 262 ? -2.192  26.969  -14.338 1.00 45.93  ? 262 LEU B N   1 
ATOM   4663 C  CA  . LEU B 1 262 ? -3.427  27.648  -14.827 1.00 40.94  ? 262 LEU B CA  1 
ATOM   4664 C  C   . LEU B 1 262 ? -3.317  27.883  -16.348 1.00 41.76  ? 262 LEU B C   1 
ATOM   4665 O  O   . LEU B 1 262 ? -4.381  27.846  -17.043 1.00 38.89  ? 262 LEU B O   1 
ATOM   4666 C  CB  . LEU B 1 262 ? -3.668  28.934  -14.028 1.00 43.41  ? 262 LEU B CB  1 
ATOM   4667 C  CG  . LEU B 1 262 ? -3.787  28.749  -12.513 1.00 47.81  ? 262 LEU B CG  1 
ATOM   4668 C  CD1 . LEU B 1 262 ? -3.507  30.052  -11.780 1.00 50.01  ? 262 LEU B CD1 1 
ATOM   4669 C  CD2 . LEU B 1 262 ? -5.164  28.210  -12.145 1.00 50.88  ? 262 LEU B CD2 1 
ATOM   4670 N  N   . ASP B 1 263 ? -2.096  28.072  -16.867 1.00 44.41  ? 263 ASP B N   1 
ATOM   4671 C  CA  . ASP B 1 263 ? -1.787  27.928  -18.323 1.00 48.62  ? 263 ASP B CA  1 
ATOM   4672 C  C   . ASP B 1 263 ? -2.357  26.577  -18.785 1.00 43.97  ? 263 ASP B C   1 
ATOM   4673 O  O   . ASP B 1 263 ? -3.291  26.568  -19.595 1.00 42.45  ? 263 ASP B O   1 
ATOM   4674 C  CB  . ASP B 1 263 ? -0.276  28.069  -18.566 1.00 48.65  ? 263 ASP B CB  1 
ATOM   4675 C  CG  . ASP B 1 263 ? 0.185   28.303  -20.002 1.00 51.36  ? 263 ASP B CG  1 
ATOM   4676 O  OD1 . ASP B 1 263 ? -0.613  28.050  -20.966 1.00 43.77  ? 263 ASP B OD1 1 
ATOM   4677 O  OD2 . ASP B 1 263 ? 1.375   28.697  -20.144 1.00 50.53  ? 263 ASP B OD2 1 
ATOM   4678 N  N   . MET B 1 264 ? -1.891  25.474  -18.180 1.00 46.25  ? 264 MET B N   1 
ATOM   4679 C  CA  . MET B 1 264 ? -2.312  24.093  -18.546 1.00 39.56  ? 264 MET B CA  1 
ATOM   4680 C  C   . MET B 1 264 ? -3.788  23.879  -18.184 1.00 39.09  ? 264 MET B C   1 
ATOM   4681 O  O   . MET B 1 264 ? -4.449  23.108  -18.894 1.00 40.36  ? 264 MET B O   1 
ATOM   4682 C  CB  . MET B 1 264 ? -1.418  23.056  -17.848 1.00 40.12  ? 264 MET B CB  1 
ATOM   4683 C  CG  . MET B 1 264 ? -1.589  21.659  -18.401 1.00 37.75  ? 264 MET B CG  1 
ATOM   4684 S  SD  . MET B 1 264 ? -0.907  21.510  -20.079 1.00 39.01  ? 264 MET B SD  1 
ATOM   4685 C  CE  . MET B 1 264 ? 0.780   21.138  -19.618 1.00 37.10  ? 264 MET B CE  1 
ATOM   4686 N  N   . CYS B 1 265 ? -4.330  24.538  -17.146 1.00 39.70  ? 265 CYS B N   1 
ATOM   4687 C  CA  . CYS B 1 265 ? -5.785  24.417  -16.810 1.00 41.37  ? 265 CYS B CA  1 
ATOM   4688 C  C   . CYS B 1 265 ? -6.628  24.956  -17.970 1.00 41.23  ? 265 CYS B C   1 
ATOM   4689 O  O   . CYS B 1 265 ? -7.666  24.304  -18.358 1.00 38.99  ? 265 CYS B O   1 
ATOM   4690 C  CB  . CYS B 1 265 ? -6.160  25.145  -15.521 1.00 46.42  ? 265 CYS B CB  1 
ATOM   4691 S  SG  . CYS B 1 265 ? -5.604  24.313  -14.009 1.00 45.40  ? 265 CYS B SG  1 
ATOM   4692 N  N   . ALA B 1 266 ? -6.184  26.079  -18.555 1.00 49.79  ? 266 ALA B N   1 
ATOM   4693 C  CA  . ALA B 1 266 ? -6.815  26.675  -19.762 1.00 46.19  ? 266 ALA B CA  1 
ATOM   4694 C  C   . ALA B 1 266 ? -6.898  25.610  -20.863 1.00 40.86  ? 266 ALA B C   1 
ATOM   4695 O  O   . ALA B 1 266 ? -7.996  25.408  -21.395 1.00 39.53  ? 266 ALA B O   1 
ATOM   4696 C  CB  . ALA B 1 266 ? -6.066  27.911  -20.213 1.00 51.85  ? 266 ALA B CB  1 
ATOM   4697 N  N   . SER B 1 267 ? -5.798  24.900  -21.159 1.00 46.62  ? 267 SER B N   1 
ATOM   4698 C  CA  . SER B 1 267 ? -5.787  23.763  -22.126 1.00 41.77  ? 267 SER B CA  1 
ATOM   4699 C  C   . SER B 1 267 ? -6.839  22.745  -21.697 1.00 34.62  ? 267 SER B C   1 
ATOM   4700 O  O   . SER B 1 267 ? -7.700  22.391  -22.509 1.00 36.31  ? 267 SER B O   1 
ATOM   4701 C  CB  . SER B 1 267 ? -4.429  23.119  -22.244 1.00 44.18  ? 267 SER B CB  1 
ATOM   4702 O  OG  . SER B 1 267 ? -3.447  24.055  -22.681 1.00 48.58  ? 267 SER B OG  1 
ATOM   4703 N  N   . LEU B 1 268 ? -6.810  22.322  -20.430 1.00 40.94  ? 268 LEU B N   1 
ATOM   4704 C  CA  . LEU B 1 268 ? -7.744  21.279  -19.907 1.00 36.73  ? 268 LEU B CA  1 
ATOM   4705 C  C   . LEU B 1 268 ? -9.194  21.790  -19.911 1.00 34.21  ? 268 LEU B C   1 
ATOM   4706 O  O   . LEU B 1 268 ? -10.117 21.025  -20.255 1.00 34.46  ? 268 LEU B O   1 
ATOM   4707 C  CB  . LEU B 1 268 ? -7.284  20.894  -18.496 1.00 36.70  ? 268 LEU B CB  1 
ATOM   4708 C  CG  . LEU B 1 268 ? -8.133  19.834  -17.807 1.00 36.46  ? 268 LEU B CG  1 
ATOM   4709 C  CD1 . LEU B 1 268 ? -8.250  18.590  -18.678 1.00 34.67  ? 268 LEU B CD1 1 
ATOM   4710 C  CD2 . LEU B 1 268 ? -7.563  19.511  -16.429 1.00 35.91  ? 268 LEU B CD2 1 
ATOM   4711 N  N   . LYS B 1 269 ? -9.412  23.045  -19.527 1.00 42.55  ? 269 LYS B N   1 
ATOM   4712 C  CA  . LYS B 1 269 ? -10.742 23.715  -19.660 1.00 49.59  ? 269 LYS B CA  1 
ATOM   4713 C  C   . LYS B 1 269 ? -11.279 23.491  -21.078 1.00 45.16  ? 269 LYS B C   1 
ATOM   4714 O  O   . LYS B 1 269 ? -12.397 22.949  -21.226 1.00 47.69  ? 269 LYS B O   1 
ATOM   4715 C  CB  . LYS B 1 269 ? -10.562 25.197  -19.315 1.00 60.59  ? 269 LYS B CB  1 
ATOM   4716 C  CG  . LYS B 1 269 ? -11.796 26.093  -19.385 1.00 69.70  ? 269 LYS B CG  1 
ATOM   4717 C  CD  . LYS B 1 269 ? -11.505 27.529  -18.931 1.00 73.21  ? 269 LYS B CD  1 
ATOM   4718 C  CE  . LYS B 1 269 ? -10.793 27.585  -17.589 1.00 79.11  ? 269 LYS B CE  1 
ATOM   4719 N  NZ  . LYS B 1 269 ? -10.798 28.934  -16.972 1.00 79.93  ? 269 LYS B NZ  1 
ATOM   4720 N  N   . GLU B 1 270 ? -10.476 23.831  -22.094 1.00 51.97  ? 270 GLU B N   1 
ATOM   4721 C  CA  . GLU B 1 270 ? -10.882 23.748  -23.531 1.00 51.60  ? 270 GLU B CA  1 
ATOM   4722 C  C   . GLU B 1 270 ? -11.155 22.284  -23.883 1.00 47.67  ? 270 GLU B C   1 
ATOM   4723 O  O   . GLU B 1 270 ? -12.163 22.038  -24.556 1.00 47.38  ? 270 GLU B O   1 
ATOM   4724 C  CB  . GLU B 1 270 ? -9.832  24.321  -24.493 1.00 56.00  ? 270 GLU B CB  1 
ATOM   4725 C  CG  . GLU B 1 270 ? -9.345  25.734  -24.173 1.00 59.98  ? 270 GLU B CG  1 
ATOM   4726 C  CD  . GLU B 1 270 ? -10.416 26.813  -24.047 1.00 62.69  ? 270 GLU B CD  1 
ATOM   4727 O  OE1 . GLU B 1 270 ? -11.422 26.752  -24.789 1.00 62.36  ? 270 GLU B OE1 1 
ATOM   4728 O  OE2 . GLU B 1 270 ? -10.245 27.709  -23.188 1.00 65.53  ? 270 GLU B OE2 1 
ATOM   4729 N  N   . LEU B 1 271 ? -10.301 21.350  -23.431 1.00 45.50  ? 271 LEU B N   1 
ATOM   4730 C  CA  . LEU B 1 271 ? -10.493 19.893  -23.690 1.00 42.16  ? 271 LEU B CA  1 
ATOM   4731 C  C   . LEU B 1 271 ? -11.825 19.445  -23.082 1.00 42.63  ? 271 LEU B C   1 
ATOM   4732 O  O   . LEU B 1 271 ? -12.521 18.627  -23.701 1.00 43.59  ? 271 LEU B O   1 
ATOM   4733 C  CB  . LEU B 1 271 ? -9.306  19.102  -23.120 1.00 42.74  ? 271 LEU B CB  1 
ATOM   4734 C  CG  . LEU B 1 271 ? -8.005  19.230  -23.912 1.00 42.09  ? 271 LEU B CG  1 
ATOM   4735 C  CD1 . LEU B 1 271 ? -6.833  18.603  -23.181 1.00 44.86  ? 271 LEU B CD1 1 
ATOM   4736 C  CD2 . LEU B 1 271 ? -8.155  18.621  -25.294 1.00 41.46  ? 271 LEU B CD2 1 
ATOM   4737 N  N   . LEU B 1 272 ? -12.167 19.935  -21.892 1.00 45.07  ? 272 LEU B N   1 
ATOM   4738 C  CA  . LEU B 1 272 ? -13.462 19.595  -21.246 1.00 51.54  ? 272 LEU B CA  1 
ATOM   4739 C  C   . LEU B 1 272 ? -14.628 20.163  -22.072 1.00 54.16  ? 272 LEU B C   1 
ATOM   4740 O  O   . LEU B 1 272 ? -15.546 19.396  -22.429 1.00 45.44  ? 272 LEU B O   1 
ATOM   4741 C  CB  . LEU B 1 272 ? -13.464 20.145  -19.816 1.00 50.89  ? 272 LEU B CB  1 
ATOM   4742 C  CG  . LEU B 1 272 ? -12.568 19.393  -18.830 1.00 50.41  ? 272 LEU B CG  1 
ATOM   4743 C  CD1 . LEU B 1 272 ? -12.743 19.923  -17.417 1.00 46.87  ? 272 LEU B CD1 1 
ATOM   4744 C  CD2 . LEU B 1 272 ? -12.848 17.898  -18.881 1.00 52.27  ? 272 LEU B CD2 1 
ATOM   4745 N  N   . GLN B 1 273 ? -14.610 21.468  -22.353 1.00 63.73  ? 273 GLN B N   1 
ATOM   4746 C  CA  . GLN B 1 273 ? -15.686 22.132  -23.144 1.00 65.37  ? 273 GLN B CA  1 
ATOM   4747 C  C   . GLN B 1 273 ? -15.724 21.494  -24.541 1.00 64.39  ? 273 GLN B C   1 
ATOM   4748 O  O   . GLN B 1 273 ? -16.726 20.804  -24.847 1.00 66.85  ? 273 GLN B O   1 
ATOM   4749 C  CB  . GLN B 1 273 ? -15.466 23.649  -23.167 1.00 66.17  ? 273 GLN B CB  1 
ATOM   4750 C  CG  . GLN B 1 273 ? -15.784 24.328  -21.835 1.00 67.40  ? 273 GLN B CG  1 
ATOM   4751 C  CD  . GLN B 1 273 ? -14.830 25.434  -21.433 1.00 69.86  ? 273 GLN B CD  1 
ATOM   4752 O  OE1 . GLN B 1 273 ? -13.778 25.636  -22.034 1.00 70.57  ? 273 GLN B OE1 1 
ATOM   4753 N  NE2 . GLN B 1 273 ? -15.187 26.172  -20.391 1.00 64.66  ? 273 GLN B NE2 1 
ATOM   4754 N  N   . ASN B 1 274 ? -14.623 21.617  -25.294 1.00 66.77  ? 274 ASN B N   1 
ATOM   4755 C  CA  . ASN B 1 274 ? -14.558 21.432  -26.776 1.00 65.95  ? 274 ASN B CA  1 
ATOM   4756 C  C   . ASN B 1 274 ? -14.214 19.986  -27.174 1.00 61.93  ? 274 ASN B C   1 
ATOM   4757 O  O   . ASN B 1 274 ? -14.342 19.697  -28.364 1.00 55.91  ? 274 ASN B O   1 
ATOM   4758 C  CB  . ASN B 1 274 ? -13.525 22.367  -27.421 1.00 59.66  ? 274 ASN B CB  1 
ATOM   4759 C  CG  . ASN B 1 274 ? -13.714 23.825  -27.055 1.00 64.47  ? 274 ASN B CG  1 
ATOM   4760 O  OD1 . ASN B 1 274 ? -14.766 24.397  -27.320 1.00 76.29  ? 274 ASN B OD1 1 
ATOM   4761 N  ND2 . ASN B 1 274 ? -12.703 24.447  -26.466 1.00 62.78  ? 274 ASN B ND2 1 
ATOM   4762 N  N   . GLY B 1 275 ? -13.750 19.133  -26.245 1.00 66.67  ? 275 GLY B N   1 
ATOM   4763 C  CA  . GLY B 1 275 ? -13.252 17.766  -26.533 1.00 63.86  ? 275 GLY B CA  1 
ATOM   4764 C  C   . GLY B 1 275 ? -11.831 17.779  -27.095 1.00 64.25  ? 275 GLY B C   1 
ATOM   4765 O  O   . GLY B 1 275 ? -11.136 18.822  -26.976 1.00 50.18  ? 275 GLY B O   1 
ATOM   4766 N  N   . MET B 1 276 ? -11.402 16.673  -27.715 1.00 66.97  ? 276 MET B N   1 
ATOM   4767 C  CA  . MET B 1 276 ? -10.021 16.494  -28.257 1.00 66.78  ? 276 MET B CA  1 
ATOM   4768 C  C   . MET B 1 276 ? -9.965  16.816  -29.765 1.00 67.14  ? 276 MET B C   1 
ATOM   4769 O  O   . MET B 1 276 ? -8.872  16.665  -30.364 1.00 68.09  ? 276 MET B O   1 
ATOM   4770 C  CB  . MET B 1 276 ? -9.506  15.072  -27.983 1.00 66.35  ? 276 MET B CB  1 
ATOM   4771 C  CG  . MET B 1 276 ? -8.377  15.050  -26.955 1.00 68.97  ? 276 MET B CG  1 
ATOM   4772 S  SD  . MET B 1 276 ? -8.054  13.468  -26.135 1.00 61.12  ? 276 MET B SD  1 
ATOM   4773 C  CE  . MET B 1 276 ? -9.321  13.568  -24.875 1.00 53.07  ? 276 MET B CE  1 
ATOM   4774 N  N   . ASN B 1 277 ? -11.060 17.311  -30.353 1.00 59.68  ? 277 ASN B N   1 
ATOM   4775 C  CA  . ASN B 1 277 ? -11.146 17.597  -31.808 1.00 70.08  ? 277 ASN B CA  1 
ATOM   4776 C  C   . ASN B 1 277 ? -10.562 16.386  -32.551 1.00 66.52  ? 277 ASN B C   1 
ATOM   4777 O  O   . ASN B 1 277 ? -9.793  16.581  -33.502 1.00 70.02  ? 277 ASN B O   1 
ATOM   4778 C  CB  . ASN B 1 277 ? -10.495 18.943  -32.161 1.00 76.55  ? 277 ASN B CB  1 
ATOM   4779 C  CG  . ASN B 1 277 ? -11.377 20.142  -31.849 1.00 83.33  ? 277 ASN B CG  1 
ATOM   4780 O  OD1 . ASN B 1 277 ? -10.901 21.158  -31.337 1.00 84.91  ? 277 ASN B OD1 1 
ATOM   4781 N  ND2 . ASN B 1 277 ? -12.665 20.043  -32.152 1.00 82.76  ? 277 ASN B ND2 1 
ATOM   4782 N  N   . GLY B 1 278 ? -10.896 15.178  -32.081 1.00 67.72  ? 278 GLY B N   1 
ATOM   4783 C  CA  . GLY B 1 278 ? -10.635 13.895  -32.764 1.00 67.19  ? 278 GLY B CA  1 
ATOM   4784 C  C   . GLY B 1 278 ? -9.173  13.492  -32.742 1.00 65.53  ? 278 GLY B C   1 
ATOM   4785 O  O   . GLY B 1 278 ? -8.785  12.648  -33.569 1.00 68.69  ? 278 GLY B O   1 
ATOM   4786 N  N   . ARG B 1 279 ? -8.376  14.059  -31.839 1.00 61.46  ? 279 ARG B N   1 
ATOM   4787 C  CA  . ARG B 1 279 ? -6.938  13.711  -31.717 1.00 62.01  ? 279 ARG B CA  1 
ATOM   4788 C  C   . ARG B 1 279 ? -6.764  12.747  -30.532 1.00 54.20  ? 279 ARG B C   1 
ATOM   4789 O  O   . ARG B 1 279 ? -7.780  12.274  -29.960 1.00 52.58  ? 279 ARG B O   1 
ATOM   4790 C  CB  . ARG B 1 279 ? -6.082  14.986  -31.655 1.00 68.83  ? 279 ARG B CB  1 
ATOM   4791 C  CG  . ARG B 1 279 ? -5.784  15.593  -33.021 1.00 69.19  ? 279 ARG B CG  1 
ATOM   4792 C  CD  . ARG B 1 279 ? -5.176  16.986  -32.976 1.00 76.58  ? 279 ARG B CD  1 
ATOM   4793 N  NE  . ARG B 1 279 ? -6.157  18.021  -32.636 1.00 87.46  ? 279 ARG B NE  1 
ATOM   4794 C  CZ  . ARG B 1 279 ? -5.997  19.337  -32.819 1.00 88.84  ? 279 ARG B CZ  1 
ATOM   4795 N  NH1 . ARG B 1 279 ? -4.885  19.818  -33.356 1.00 90.08  ? 279 ARG B NH1 1 
ATOM   4796 N  NH2 . ARG B 1 279 ? -6.961  20.173  -32.467 1.00 84.92  ? 279 ARG B NH2 1 
ATOM   4797 N  N   . THR B 1 280 ? -5.513  12.370  -30.266 1.00 50.12  ? 280 THR B N   1 
ATOM   4798 C  CA  . THR B 1 280 ? -5.097  11.587  -29.082 1.00 40.54  ? 280 THR B CA  1 
ATOM   4799 C  C   . THR B 1 280 ? -4.005  12.361  -28.366 1.00 38.73  ? 280 THR B C   1 
ATOM   4800 O  O   . THR B 1 280 ? -3.386  13.263  -28.965 1.00 39.18  ? 280 THR B O   1 
ATOM   4801 C  CB  . THR B 1 280 ? -4.551  10.200  -29.433 1.00 38.54  ? 280 THR B CB  1 
ATOM   4802 O  OG1 . THR B 1 280 ? -3.501  10.428  -30.367 1.00 43.50  ? 280 THR B OG1 1 
ATOM   4803 C  CG2 . THR B 1 280 ? -5.582  9.251   -29.996 1.00 36.19  ? 280 THR B CG2 1 
ATOM   4804 N  N   . ILE B 1 281 ? -3.790  11.992  -27.115 1.00 37.18  ? 281 ILE B N   1 
ATOM   4805 C  CA  . ILE B 1 281 ? -2.667  12.460  -26.268 1.00 33.84  ? 281 ILE B CA  1 
ATOM   4806 C  C   . ILE B 1 281 ? -2.041  11.201  -25.673 1.00 30.32  ? 281 ILE B C   1 
ATOM   4807 O  O   . ILE B 1 281 ? -2.779  10.406  -25.041 1.00 29.88  ? 281 ILE B O   1 
ATOM   4808 C  CB  . ILE B 1 281 ? -3.168  13.436  -25.187 1.00 35.53  ? 281 ILE B CB  1 
ATOM   4809 C  CG1 . ILE B 1 281 ? -4.057  14.533  -25.789 1.00 37.18  ? 281 ILE B CG1 1 
ATOM   4810 C  CG2 . ILE B 1 281 ? -1.979  13.990  -24.418 1.00 36.84  ? 281 ILE B CG2 1 
ATOM   4811 C  CD1 . ILE B 1 281 ? -4.578  15.562  -24.802 1.00 39.86  ? 281 ILE B CD1 1 
ATOM   4812 N  N   . LEU B 1 282 ? -0.747  11.008  -25.915 1.00 31.72  ? 282 LEU B N   1 
ATOM   4813 C  CA  . LEU B 1 282 ? 0.004   9.812   -25.466 1.00 31.42  ? 282 LEU B CA  1 
ATOM   4814 C  C   . LEU B 1 282 ? -0.838  8.571   -25.768 1.00 29.74  ? 282 LEU B C   1 
ATOM   4815 O  O   . LEU B 1 282 ? -0.996  7.735   -24.874 1.00 29.21  ? 282 LEU B O   1 
ATOM   4816 C  CB  . LEU B 1 282 ? 0.297   9.935   -23.963 1.00 32.21  ? 282 LEU B CB  1 
ATOM   4817 C  CG  . LEU B 1 282 ? 1.360   10.961  -23.579 1.00 31.93  ? 282 LEU B CG  1 
ATOM   4818 C  CD1 . LEU B 1 282 ? 1.472   11.129  -22.055 1.00 29.43  ? 282 LEU B CD1 1 
ATOM   4819 C  CD2 . LEU B 1 282 ? 2.705   10.573  -24.209 1.00 31.36  ? 282 LEU B CD2 1 
ATOM   4820 N  N   . GLY B 1 283 ? -1.388  8.484   -26.973 1.00 31.47  ? 283 GLY B N   1 
ATOM   4821 C  CA  . GLY B 1 283 ? -2.135  7.312   -27.488 1.00 34.27  ? 283 GLY B CA  1 
ATOM   4822 C  C   . GLY B 1 283 ? -3.404  6.998   -26.704 1.00 35.64  ? 283 GLY B C   1 
ATOM   4823 O  O   . GLY B 1 283 ? -3.790  5.815   -26.619 1.00 35.75  ? 283 GLY B O   1 
ATOM   4824 N  N   . SER B 1 284 ? -4.045  8.008   -26.128 1.00 37.06  ? 284 SER B N   1 
ATOM   4825 C  CA  . SER B 1 284 ? -5.343  7.863   -25.428 1.00 35.89  ? 284 SER B CA  1 
ATOM   4826 C  C   . SER B 1 284 ? -6.346  8.861   -26.022 1.00 34.18  ? 284 SER B C   1 
ATOM   4827 O  O   . SER B 1 284 ? -5.949  9.990   -26.364 1.00 33.93  ? 284 SER B O   1 
ATOM   4828 C  CB  . SER B 1 284 ? -5.150  8.043   -23.952 1.00 35.96  ? 284 SER B CB  1 
ATOM   4829 O  OG  . SER B 1 284 ? -6.399  8.028   -23.294 1.00 38.77  ? 284 SER B OG  1 
ATOM   4830 N  N   . ALA B 1 285 ? -7.594  8.435   -26.151 1.00 37.66  ? 285 ALA B N   1 
ATOM   4831 C  CA  . ALA B 1 285 ? -8.756  9.285   -26.492 1.00 42.91  ? 285 ALA B CA  1 
ATOM   4832 C  C   . ALA B 1 285 ? -9.511  9.684   -25.214 1.00 45.23  ? 285 ALA B C   1 
ATOM   4833 O  O   . ALA B 1 285 ? -10.504 10.423  -25.337 1.00 50.02  ? 285 ALA B O   1 
ATOM   4834 C  CB  . ALA B 1 285 ? -9.657  8.557   -27.468 1.00 40.57  ? 285 ALA B CB  1 
ATOM   4835 N  N   . LEU B 1 286 ? -9.073  9.227   -24.036 1.00 40.80  ? 286 LEU B N   1 
ATOM   4836 C  CA  . LEU B 1 286 ? -9.603  9.700   -22.725 1.00 42.21  ? 286 LEU B CA  1 
ATOM   4837 C  C   . LEU B 1 286 ? -8.557  10.621  -22.081 1.00 37.91  ? 286 LEU B C   1 
ATOM   4838 O  O   . LEU B 1 286 ? -7.375  10.553  -22.459 1.00 38.11  ? 286 LEU B O   1 
ATOM   4839 C  CB  . LEU B 1 286 ? -9.920  8.496   -21.826 1.00 45.59  ? 286 LEU B CB  1 
ATOM   4840 C  CG  . LEU B 1 286 ? -11.220 7.751   -22.129 1.00 49.54  ? 286 LEU B CG  1 
ATOM   4841 C  CD1 . LEU B 1 286 ? -11.457 6.601   -21.144 1.00 51.06  ? 286 LEU B CD1 1 
ATOM   4842 C  CD2 . LEU B 1 286 ? -12.406 8.710   -22.110 1.00 53.28  ? 286 LEU B CD2 1 
ATOM   4843 N  N   . LEU B 1 287 ? -8.981  11.484  -21.166 1.00 33.67  ? 287 LEU B N   1 
ATOM   4844 C  CA  . LEU B 1 287 ? -8.082  12.254  -20.273 1.00 34.48  ? 287 LEU B CA  1 
ATOM   4845 C  C   . LEU B 1 287 ? -7.654  11.333  -19.118 1.00 34.11  ? 287 LEU B C   1 
ATOM   4846 O  O   . LEU B 1 287 ? -8.481  11.075  -18.260 1.00 37.76  ? 287 LEU B O   1 
ATOM   4847 C  CB  . LEU B 1 287 ? -8.828  13.510  -19.802 1.00 34.36  ? 287 LEU B CB  1 
ATOM   4848 C  CG  . LEU B 1 287 ? -9.063  14.557  -20.900 1.00 38.13  ? 287 LEU B CG  1 
ATOM   4849 C  CD1 . LEU B 1 287 ? -9.791  15.783  -20.380 1.00 38.74  ? 287 LEU B CD1 1 
ATOM   4850 C  CD2 . LEU B 1 287 ? -7.754  14.996  -21.527 1.00 38.83  ? 287 LEU B CD2 1 
ATOM   4851 N  N   . GLU B 1 288 ? -6.412  10.848  -19.124 1.00 32.94  ? 288 GLU B N   1 
ATOM   4852 C  CA  . GLU B 1 288 ? -5.874  9.872   -18.136 1.00 33.34  ? 288 GLU B CA  1 
ATOM   4853 C  C   . GLU B 1 288 ? -5.621  10.530  -16.772 1.00 29.90  ? 288 GLU B C   1 
ATOM   4854 O  O   . GLU B 1 288 ? -4.893  11.543  -16.699 1.00 25.77  ? 288 GLU B O   1 
ATOM   4855 C  CB  . GLU B 1 288 ? -4.587  9.239   -18.656 1.00 35.20  ? 288 GLU B CB  1 
ATOM   4856 C  CG  . GLU B 1 288 ? -4.838  8.247   -19.782 1.00 44.33  ? 288 GLU B CG  1 
ATOM   4857 C  CD  . GLU B 1 288 ? -5.492  6.936   -19.357 1.00 46.98  ? 288 GLU B CD  1 
ATOM   4858 O  OE1 . GLU B 1 288 ? -4.933  6.220   -18.470 1.00 51.72  ? 288 GLU B OE1 1 
ATOM   4859 O  OE2 . GLU B 1 288 ? -6.553  6.644   -19.890 1.00 48.57  ? 288 GLU B OE2 1 
ATOM   4860 N  N   . ASP B 1 289 ? -6.146  9.937   -15.697 1.00 28.68  ? 289 ASP B N   1 
ATOM   4861 C  CA  . ASP B 1 289 ? -6.005  10.518  -14.334 1.00 29.49  ? 289 ASP B CA  1 
ATOM   4862 C  C   . ASP B 1 289 ? -5.366  9.524   -13.344 1.00 30.79  ? 289 ASP B C   1 
ATOM   4863 O  O   . ASP B 1 289 ? -5.516  9.745   -12.131 1.00 29.94  ? 289 ASP B O   1 
ATOM   4864 C  CB  . ASP B 1 289 ? -7.368  11.021  -13.851 1.00 30.22  ? 289 ASP B CB  1 
ATOM   4865 C  CG  . ASP B 1 289 ? -8.321  9.945   -13.360 1.00 31.43  ? 289 ASP B CG  1 
ATOM   4866 O  OD1 . ASP B 1 289 ? -8.149  8.773   -13.752 1.00 32.64  ? 289 ASP B OD1 1 
ATOM   4867 O  OD2 . ASP B 1 289 ? -9.252  10.293  -12.576 1.00 32.54  ? 289 ASP B OD2 1 
ATOM   4868 N  N   . GLU B 1 290 ? -4.645  8.496   -13.798 1.00 30.02  ? 290 GLU B N   1 
ATOM   4869 C  CA  . GLU B 1 290 ? -4.007  7.526   -12.857 1.00 32.25  ? 290 GLU B CA  1 
ATOM   4870 C  C   . GLU B 1 290 ? -2.472  7.681   -12.850 1.00 30.04  ? 290 GLU B C   1 
ATOM   4871 O  O   . GLU B 1 290 ? -1.777  6.751   -12.391 1.00 33.48  ? 290 GLU B O   1 
ATOM   4872 C  CB  . GLU B 1 290 ? -4.500  6.101   -13.159 1.00 31.11  ? 290 GLU B CB  1 
ATOM   4873 C  CG  . GLU B 1 290 ? -6.012  5.950   -13.031 1.00 33.85  ? 290 GLU B CG  1 
ATOM   4874 C  CD  . GLU B 1 290 ? -6.548  4.675   -12.360 1.00 35.89  ? 290 GLU B CD  1 
ATOM   4875 O  OE1 . GLU B 1 290 ? -5.828  3.666   -12.327 1.00 30.17  ? 290 GLU B OE1 1 
ATOM   4876 O  OE2 . GLU B 1 290 ? -7.710  4.689   -11.875 1.00 35.60  ? 290 GLU B OE2 1 
ATOM   4877 N  N   . PHE B 1 291 ? -1.932  8.823   -13.280 1.00 27.32  ? 291 PHE B N   1 
ATOM   4878 C  CA  . PHE B 1 291 ? -0.529  9.208   -13.008 1.00 24.21  ? 291 PHE B CA  1 
ATOM   4879 C  C   . PHE B 1 291 ? -0.466  10.454  -12.124 1.00 25.10  ? 291 PHE B C   1 
ATOM   4880 O  O   . PHE B 1 291 ? -1.059  11.494  -12.470 1.00 25.73  ? 291 PHE B O   1 
ATOM   4881 C  CB  . PHE B 1 291 ? 0.202   9.538   -14.296 1.00 26.16  ? 291 PHE B CB  1 
ATOM   4882 C  CG  . PHE B 1 291 ? 0.211   8.423   -15.296 1.00 28.86  ? 291 PHE B CG  1 
ATOM   4883 C  CD1 . PHE B 1 291 ? -0.797  8.299   -16.234 1.00 29.00  ? 291 PHE B CD1 1 
ATOM   4884 C  CD2 . PHE B 1 291 ? 1.250   7.507   -15.295 1.00 30.27  ? 291 PHE B CD2 1 
ATOM   4885 C  CE1 . PHE B 1 291 ? -0.738  7.294   -17.188 1.00 33.35  ? 291 PHE B CE1 1 
ATOM   4886 C  CE2 . PHE B 1 291 ? 1.326   6.525   -16.264 1.00 30.72  ? 291 PHE B CE2 1 
ATOM   4887 C  CZ  . PHE B 1 291 ? 0.318   6.403   -17.191 1.00 33.17  ? 291 PHE B CZ  1 
ATOM   4888 N  N   . THR B 1 292 ? 0.278   10.372  -11.033 1.00 25.60  ? 292 THR B N   1 
ATOM   4889 C  CA  . THR B 1 292 ? 0.496   11.506  -10.107 1.00 26.93  ? 292 THR B CA  1 
ATOM   4890 C  C   . THR B 1 292 ? 1.611   12.358  -10.680 1.00 28.59  ? 292 THR B C   1 
ATOM   4891 O  O   . THR B 1 292 ? 2.312   11.912  -11.587 1.00 29.44  ? 292 THR B O   1 
ATOM   4892 C  CB  . THR B 1 292 ? 0.823   11.030  -8.688  1.00 28.82  ? 292 THR B CB  1 
ATOM   4893 O  OG1 . THR B 1 292 ? 2.156   10.523  -8.738  1.00 27.25  ? 292 THR B OG1 1 
ATOM   4894 C  CG2 . THR B 1 292 ? -0.157  10.006  -8.158  1.00 28.31  ? 292 THR B CG2 1 
ATOM   4895 N  N   . PRO B 1 293 ? 1.795   13.602  -10.185 1.00 29.62  ? 293 PRO B N   1 
ATOM   4896 C  CA  . PRO B 1 293 ? 2.967   14.396  -10.534 1.00 29.91  ? 293 PRO B CA  1 
ATOM   4897 C  C   . PRO B 1 293 ? 4.274   13.655  -10.282 1.00 29.87  ? 293 PRO B C   1 
ATOM   4898 O  O   . PRO B 1 293 ? 5.121   13.735  -11.127 1.00 30.56  ? 293 PRO B O   1 
ATOM   4899 C  CB  . PRO B 1 293 ? 2.848   15.614  -9.626  1.00 30.25  ? 293 PRO B CB  1 
ATOM   4900 C  CG  . PRO B 1 293 ? 1.353   15.784  -9.496  1.00 31.00  ? 293 PRO B CG  1 
ATOM   4901 C  CD  . PRO B 1 293 ? 0.838   14.359  -9.366  1.00 30.75  ? 293 PRO B CD  1 
ATOM   4902 N  N   . PHE B 1 294 ? 4.391   12.978  -9.134  1.00 34.09  ? 294 PHE B N   1 
ATOM   4903 C  CA  . PHE B 1 294 ? 5.568   12.161  -8.753  1.00 35.98  ? 294 PHE B CA  1 
ATOM   4904 C  C   . PHE B 1 294 ? 5.785   11.077  -9.817  1.00 31.80  ? 294 PHE B C   1 
ATOM   4905 O  O   . PHE B 1 294 ? 6.922   10.907  -10.274 1.00 35.72  ? 294 PHE B O   1 
ATOM   4906 C  CB  . PHE B 1 294 ? 5.440   11.517  -7.367  1.00 41.78  ? 294 PHE B CB  1 
ATOM   4907 C  CG  . PHE B 1 294 ? 6.624   10.632  -7.060  1.00 52.42  ? 294 PHE B CG  1 
ATOM   4908 C  CD1 . PHE B 1 294 ? 7.808   11.166  -6.559  1.00 58.53  ? 294 PHE B CD1 1 
ATOM   4909 C  CD2 . PHE B 1 294 ? 6.605   9.276   -7.395  1.00 62.39  ? 294 PHE B CD2 1 
ATOM   4910 C  CE1 . PHE B 1 294 ? 8.916   10.354  -6.343  1.00 59.40  ? 294 PHE B CE1 1 
ATOM   4911 C  CE2 . PHE B 1 294 ? 7.717   8.464   -7.181  1.00 62.22  ? 294 PHE B CE2 1 
ATOM   4912 C  CZ  . PHE B 1 294 ? 8.870   9.008   -6.653  1.00 60.40  ? 294 PHE B CZ  1 
ATOM   4913 N  N   . ASP B 1 295 ? 4.733   10.364  -10.207 1.00 31.21  ? 295 ASP B N   1 
ATOM   4914 C  CA  . ASP B 1 295 ? 4.839   9.299   -11.235 1.00 29.13  ? 295 ASP B CA  1 
ATOM   4915 C  C   . ASP B 1 295 ? 5.448   9.893   -12.522 1.00 31.94  ? 295 ASP B C   1 
ATOM   4916 O  O   . ASP B 1 295 ? 6.317   9.258   -13.116 1.00 33.25  ? 295 ASP B O   1 
ATOM   4917 C  CB  . ASP B 1 295 ? 3.484   8.663   -11.528 1.00 29.07  ? 295 ASP B CB  1 
ATOM   4918 C  CG  . ASP B 1 295 ? 2.874   7.893   -10.370 1.00 28.07  ? 295 ASP B CG  1 
ATOM   4919 O  OD1 . ASP B 1 295 ? 3.620   7.618   -9.410  1.00 28.62  ? 295 ASP B OD1 1 
ATOM   4920 O  OD2 . ASP B 1 295 ? 1.664   7.579   -10.455 1.00 23.73  ? 295 ASP B OD2 1 
ATOM   4921 N  N   . VAL B 1 296 ? 4.980   11.057  -12.958 1.00 31.52  ? 296 VAL B N   1 
ATOM   4922 C  CA  . VAL B 1 296 ? 5.436   11.689  -14.230 1.00 33.32  ? 296 VAL B CA  1 
ATOM   4923 C  C   . VAL B 1 296 ? 6.897   12.105  -14.071 1.00 36.07  ? 296 VAL B C   1 
ATOM   4924 O  O   . VAL B 1 296 ? 7.685   11.853  -15.009 1.00 36.66  ? 296 VAL B O   1 
ATOM   4925 C  CB  . VAL B 1 296 ? 4.530   12.863  -14.633 1.00 32.21  ? 296 VAL B CB  1 
ATOM   4926 C  CG1 . VAL B 1 296 ? 5.055   13.592  -15.860 1.00 36.62  ? 296 VAL B CG1 1 
ATOM   4927 C  CG2 . VAL B 1 296 ? 3.109   12.383  -14.865 1.00 31.42  ? 296 VAL B CG2 1 
ATOM   4928 N  N   . VAL B 1 297 ? 7.251   12.685  -12.920 1.00 37.68  ? 297 VAL B N   1 
ATOM   4929 C  CA  . VAL B 1 297 ? 8.641   13.139  -12.640 1.00 41.15  ? 297 VAL B CA  1 
ATOM   4930 C  C   . VAL B 1 297 ? 9.567   11.917  -12.565 1.00 41.17  ? 297 VAL B C   1 
ATOM   4931 O  O   . VAL B 1 297 ? 10.630  12.001  -13.176 1.00 43.21  ? 297 VAL B O   1 
ATOM   4932 C  CB  . VAL B 1 297 ? 8.717   14.032  -11.383 1.00 41.99  ? 297 VAL B CB  1 
ATOM   4933 C  CG1 . VAL B 1 297 ? 10.154  14.298  -10.963 1.00 43.86  ? 297 VAL B CG1 1 
ATOM   4934 C  CG2 . VAL B 1 297 ? 7.984   15.350  -11.606 1.00 40.64  ? 297 VAL B CG2 1 
ATOM   4935 N  N   . ARG B 1 298 ? 9.194   10.847  -11.844 1.00 44.64  ? 298 ARG B N   1 
ATOM   4936 C  CA  . ARG B 1 298 ? 9.989   9.581   -11.726 1.00 46.98  ? 298 ARG B CA  1 
ATOM   4937 C  C   . ARG B 1 298 ? 10.302  9.031   -13.127 1.00 43.74  ? 298 ARG B C   1 
ATOM   4938 O  O   . ARG B 1 298 ? 11.442  8.606   -13.338 1.00 44.79  ? 298 ARG B O   1 
ATOM   4939 C  CB  . ARG B 1 298 ? 9.295   8.523   -10.843 1.00 53.39  ? 298 ARG B CB  1 
ATOM   4940 C  CG  . ARG B 1 298 ? 9.061   7.163   -11.507 1.00 63.78  ? 298 ARG B CG  1 
ATOM   4941 C  CD  . ARG B 1 298 ? 8.515   6.011   -10.639 1.00 66.90  ? 298 ARG B CD  1 
ATOM   4942 N  NE  . ARG B 1 298 ? 7.115   5.596   -10.885 1.00 62.01  ? 298 ARG B NE  1 
ATOM   4943 C  CZ  . ARG B 1 298 ? 6.657   4.358   -11.118 1.00 43.11  ? 298 ARG B CZ  1 
ATOM   4944 N  NH1 . ARG B 1 298 ? 7.437   3.295   -11.118 1.00 44.71  ? 298 ARG B NH1 1 
ATOM   4945 N  NH2 . ARG B 1 298 ? 5.367   4.183   -11.255 1.00 48.84  ? 298 ARG B NH2 1 
ATOM   4946 N  N   . GLN B 1 299 ? 9.323   9.011   -14.029 1.00 41.10  ? 299 GLN B N   1 
ATOM   4947 C  CA  . GLN B 1 299 ? 9.373   8.240   -15.298 1.00 44.19  ? 299 GLN B CA  1 
ATOM   4948 C  C   . GLN B 1 299 ? 10.094  9.057   -16.377 1.00 51.56  ? 299 GLN B C   1 
ATOM   4949 O  O   . GLN B 1 299 ? 10.708  8.420   -17.255 1.00 55.44  ? 299 GLN B O   1 
ATOM   4950 C  CB  . GLN B 1 299 ? 7.959   7.832   -15.747 1.00 37.87  ? 299 GLN B CB  1 
ATOM   4951 C  CG  . GLN B 1 299 ? 7.986   6.846   -16.900 1.00 32.96  ? 299 GLN B CG  1 
ATOM   4952 C  CD  . GLN B 1 299 ? 6.674   6.254   -17.356 1.00 32.00  ? 299 GLN B CD  1 
ATOM   4953 O  OE1 . GLN B 1 299 ? 6.564   5.843   -18.506 1.00 29.77  ? 299 GLN B OE1 1 
ATOM   4954 N  NE2 . GLN B 1 299 ? 5.680   6.175   -16.482 1.00 26.27  ? 299 GLN B NE2 1 
ATOM   4955 N  N   . CYS B 1 300 ? 10.016  10.396  -16.312 1.00 53.81  ? 300 CYS B N   1 
ATOM   4956 C  CA  . CYS B 1 300 ? 10.440  11.353  -17.377 1.00 57.79  ? 300 CYS B CA  1 
ATOM   4957 C  C   . CYS B 1 300 ? 11.781  12.040  -17.051 1.00 66.92  ? 300 CYS B C   1 
ATOM   4958 O  O   . CYS B 1 300 ? 12.400  12.537  -18.012 1.00 78.57  ? 300 CYS B O   1 
ATOM   4959 C  CB  . CYS B 1 300 ? 9.372   12.415  -17.605 1.00 52.06  ? 300 CYS B CB  1 
ATOM   4960 S  SG  . CYS B 1 300 ? 7.876   11.765  -18.392 1.00 60.00  ? 300 CYS B SG  1 
ATOM   4961 N  N   . SER B 1 301 ? 12.216  12.065  -15.777 1.00 72.24  ? 301 SER B N   1 
ATOM   4962 C  CA  . SER B 1 301 ? 13.453  12.737  -15.271 1.00 71.87  ? 301 SER B CA  1 
ATOM   4963 C  C   . SER B 1 301 ? 14.219  11.797  -14.330 1.00 71.88  ? 301 SER B C   1 
ATOM   4964 O  O   . SER B 1 301 ? 14.133  10.569  -14.406 1.00 72.66  ? 301 SER B O   1 
ATOM   4965 C  CB  . SER B 1 301 ? 13.137  14.046  -14.565 1.00 72.60  ? 301 SER B CB  1 
ATOM   4966 O  OG  . SER B 1 301 ? 12.366  14.918  -15.389 1.00 72.99  ? 301 SER B OG  1 
HETATM 4967 CL CL  . CL  C 2 .   ? 5.331   -15.072 -31.085 1.00 33.78  ? 401 CL  A CL  1 
HETATM 4968 C  C4  C RA7 D 3 .   ? 18.032  4.089   -25.530 0.19 25.54  ? 402 RA7 A C4  1 
HETATM 4969 C  C4  D RA7 D 3 .   ? 18.032  4.089   -25.530 0.19 25.54  ? 402 RA7 A C4  1 
HETATM 4970 C  C5  C RA7 D 3 .   ? 15.991  5.121   -25.537 0.19 24.57  ? 402 RA7 A C5  1 
HETATM 4971 C  C5  D RA7 D 3 .   ? 15.991  5.121   -25.537 0.19 24.57  ? 402 RA7 A C5  1 
HETATM 4972 C  C6  C RA7 D 3 .   ? 16.543  6.534   -25.273 0.19 25.54  ? 402 RA7 A C6  1 
HETATM 4973 C  C6  D RA7 D 3 .   ? 16.543  6.534   -25.273 0.19 25.54  ? 402 RA7 A C6  1 
HETATM 4974 N  N1  C RA7 D 3 .   ? 17.996  6.548   -25.051 0.19 26.50  ? 402 RA7 A N1  1 
HETATM 4975 N  N1  D RA7 D 3 .   ? 17.996  6.548   -25.051 0.19 26.50  ? 402 RA7 A N1  1 
HETATM 4976 C  C7  C RA7 D 3 .   ? 21.485  10.753  -25.150 0.19 32.20  ? 402 RA7 A C7  1 
HETATM 4977 C  C7  D RA7 D 3 .   ? 21.485  10.753  -25.150 0.19 32.20  ? 402 RA7 A C7  1 
HETATM 4978 O  O1  C RA7 D 3 .   ? 21.765  11.227  -23.843 0.19 32.54  ? 402 RA7 A O1  1 
HETATM 4979 O  O1  D RA7 D 3 .   ? 21.765  11.227  -23.843 0.19 32.54  ? 402 RA7 A O1  1 
HETATM 4980 C  C1  C RA7 D 3 .   ? 20.339  9.773   -25.041 0.19 31.41  ? 402 RA7 A C1  1 
HETATM 4981 C  C1  D RA7 D 3 .   ? 20.339  9.773   -25.041 0.19 31.41  ? 402 RA7 A C1  1 
HETATM 4982 S  S   C RA7 D 3 .   ? 20.423  8.083   -25.383 0.19 31.77  ? 402 RA7 A S   1 
HETATM 4983 S  S   D RA7 D 3 .   ? 20.423  8.083   -25.383 0.19 31.77  ? 402 RA7 A S   1 
HETATM 4984 C  C2  C RA7 D 3 .   ? 18.675  7.842   -24.978 0.19 29.21  ? 402 RA7 A C2  1 
HETATM 4985 C  C2  D RA7 D 3 .   ? 18.675  7.842   -24.978 0.19 29.21  ? 402 RA7 A C2  1 
HETATM 4986 N  N   C RA7 D 3 .   ? 18.107  9.018   -24.614 0.19 30.66  ? 402 RA7 A N   1 
HETATM 4987 N  N   D RA7 D 3 .   ? 18.107  9.018   -24.614 0.19 30.66  ? 402 RA7 A N   1 
HETATM 4988 C  C   C RA7 D 3 .   ? 19.029  9.996   -24.670 0.19 31.35  ? 402 RA7 A C   1 
HETATM 4989 C  C   D RA7 D 3 .   ? 19.029  9.996   -24.670 0.19 31.35  ? 402 RA7 A C   1 
HETATM 4990 O  O   C RA7 D 3 .   ? 16.740  4.158   -24.996 0.19 24.70  ? 402 RA7 A O   1 
HETATM 4991 O  O   D RA7 D 3 .   ? 16.740  4.158   -24.996 0.19 24.70  ? 402 RA7 A O   1 
HETATM 4992 C  C3  C RA7 D 3 .   ? 18.606  5.469   -25.844 0.19 25.75  ? 402 RA7 A C3  1 
HETATM 4993 C  C3  D RA7 D 3 .   ? 18.606  5.469   -25.844 0.19 25.75  ? 402 RA7 A C3  1 
HETATM 4994 CL CL  . CL  E 2 .   ? -19.166 -8.620  13.600  1.00 49.44  ? 401 CL  B CL  1 
HETATM 4995 O  O   . HOH F 4 .   ? 38.175  -1.564  -28.548 1.00 42.05  ? 501 HOH A O   1 
HETATM 4996 O  O   . HOH F 4 .   ? -1.376  -11.495 -31.685 1.00 29.38  ? 502 HOH A O   1 
HETATM 4997 O  O   . HOH F 4 .   ? -25.574 -1.827  -38.478 1.00 45.17  ? 503 HOH A O   1 
HETATM 4998 O  O   . HOH F 4 .   ? -22.690 -0.219  -40.336 1.00 38.69  ? 504 HOH A O   1 
HETATM 4999 O  O   . HOH F 4 .   ? 16.049  -14.104 -10.410 1.00 30.80  ? 505 HOH A O   1 
HETATM 5000 O  O   . HOH F 4 .   ? -21.155 0.138   -43.829 1.00 30.30  ? 506 HOH A O   1 
HETATM 5001 O  O   . HOH F 4 .   ? 4.500   -1.663  -28.215 1.00 22.78  ? 507 HOH A O   1 
HETATM 5002 O  O   . HOH F 4 .   ? 22.242  -13.173 -7.718  1.00 40.44  ? 508 HOH A O   1 
HETATM 5003 O  O   . HOH F 4 .   ? 28.616  -1.268  -37.910 1.00 36.56  ? 509 HOH A O   1 
HETATM 5004 O  O   . HOH F 4 .   ? -15.767 -11.742 -50.650 1.00 25.54  ? 510 HOH A O   1 
HETATM 5005 O  O   . HOH F 4 .   ? -8.666  1.777   -34.710 1.00 33.38  ? 511 HOH A O   1 
HETATM 5006 O  O   . HOH F 4 .   ? 12.104  -20.464 -12.421 1.00 36.05  ? 512 HOH A O   1 
HETATM 5007 O  O   . HOH F 4 .   ? 8.884   -13.174 -11.281 1.00 25.66  ? 513 HOH A O   1 
HETATM 5008 O  O   . HOH F 4 .   ? 29.558  0.685   -42.213 1.00 32.80  ? 514 HOH A O   1 
HETATM 5009 O  O   . HOH F 4 .   ? -6.047  -6.185  -27.915 1.00 23.43  ? 515 HOH A O   1 
HETATM 5010 O  O   . HOH F 4 .   ? 36.707  -9.659  -32.447 1.00 31.36  ? 516 HOH A O   1 
HETATM 5011 O  O   . HOH F 4 .   ? 15.464  -5.838  -17.649 1.00 34.61  ? 517 HOH A O   1 
HETATM 5012 O  O   . HOH F 4 .   ? 22.621  2.158   -17.076 1.00 32.82  ? 518 HOH A O   1 
HETATM 5013 O  O   . HOH F 4 .   ? -19.037 -6.174  -48.626 1.00 27.37  ? 519 HOH A O   1 
HETATM 5014 O  O   . HOH F 4 .   ? -3.180  -0.351  -28.514 1.00 43.74  ? 520 HOH A O   1 
HETATM 5015 O  O   . HOH F 4 .   ? -18.918 -9.438  -47.119 1.00 28.52  ? 521 HOH A O   1 
HETATM 5016 O  O   . HOH F 4 .   ? 13.335  -3.702  -33.045 1.00 21.64  ? 522 HOH A O   1 
HETATM 5017 O  O   . HOH F 4 .   ? -1.045  -14.948 -40.012 1.00 27.83  ? 523 HOH A O   1 
HETATM 5018 O  O   . HOH F 4 .   ? 2.429   -11.161 -22.575 1.00 27.54  ? 524 HOH A O   1 
HETATM 5019 O  O   . HOH F 4 .   ? -20.441 -4.590  -40.690 1.00 35.44  ? 525 HOH A O   1 
HETATM 5020 O  O   . HOH F 4 .   ? 26.250  -2.209  -36.956 1.00 31.66  ? 526 HOH A O   1 
HETATM 5021 O  O   . HOH F 4 .   ? -13.278 -14.055 -48.242 1.00 28.30  ? 527 HOH A O   1 
HETATM 5022 O  O   . HOH F 4 .   ? -8.295  -11.307 -47.839 1.00 39.56  ? 528 HOH A O   1 
HETATM 5023 O  O   . HOH F 4 .   ? -0.897  -7.952  -22.796 1.00 30.37  ? 529 HOH A O   1 
HETATM 5024 O  O   . HOH F 4 .   ? -17.921 -5.060  -46.814 1.00 31.31  ? 530 HOH A O   1 
HETATM 5025 O  O   . HOH F 4 .   ? 24.516  -3.226  -29.893 1.00 18.77  ? 531 HOH A O   1 
HETATM 5026 O  O   . HOH F 4 .   ? 23.564  -18.122 -19.766 1.00 45.43  ? 532 HOH A O   1 
HETATM 5027 O  O   . HOH F 4 .   ? -15.666 0.672   -42.167 1.00 32.76  ? 533 HOH A O   1 
HETATM 5028 O  O   . HOH F 4 .   ? -15.686 5.379   -43.116 1.00 35.38  ? 534 HOH A O   1 
HETATM 5029 O  O   . HOH F 4 .   ? 32.580  -6.747  -37.146 1.00 33.39  ? 535 HOH A O   1 
HETATM 5030 O  O   . HOH F 4 .   ? 15.503  -14.512 -27.646 1.00 27.61  ? 536 HOH A O   1 
HETATM 5031 O  O   . HOH F 4 .   ? 11.064  -5.559  -5.956  1.00 30.95  ? 537 HOH A O   1 
HETATM 5032 O  O   . HOH F 4 .   ? 31.086  -4.707  -37.446 1.00 33.21  ? 538 HOH A O   1 
HETATM 5033 O  O   . HOH F 4 .   ? 21.164  -5.831  -37.540 1.00 30.22  ? 539 HOH A O   1 
HETATM 5034 O  O   A HOH F 4 .   ? 19.129  5.411   -28.869 0.31 22.88  ? 540 HOH A O   1 
HETATM 5035 O  O   B HOH F 4 .   ? 19.129  5.411   -28.869 0.31 22.88  ? 540 HOH A O   1 
HETATM 5036 O  O   C HOH F 4 .   ? 19.195  5.332   -29.383 0.19 13.95  ? 540 HOH A O   1 
HETATM 5037 O  O   D HOH F 4 .   ? 19.195  5.332   -29.383 0.19 13.95  ? 540 HOH A O   1 
HETATM 5038 O  O   . HOH F 4 .   ? 6.060   2.449   -34.319 1.00 38.06  ? 541 HOH A O   1 
HETATM 5039 O  O   . HOH F 4 .   ? -1.888  -7.838  -20.149 1.00 29.24  ? 542 HOH A O   1 
HETATM 5040 O  O   . HOH F 4 .   ? 20.587  -8.101  -36.463 1.00 25.29  ? 543 HOH A O   1 
HETATM 5041 O  O   . HOH F 4 .   ? -3.942  -9.117  -37.439 1.00 22.75  ? 544 HOH A O   1 
HETATM 5042 O  O   . HOH F 4 .   ? -16.161 -16.937 -38.873 1.00 30.88  ? 545 HOH A O   1 
HETATM 5043 O  O   . HOH F 4 .   ? 23.010  3.917   -43.972 1.00 30.48  ? 546 HOH A O   1 
HETATM 5044 O  O   . HOH F 4 .   ? 24.978  -2.150  -41.382 1.00 32.87  ? 547 HOH A O   1 
HETATM 5045 O  O   . HOH F 4 .   ? 23.268  -4.418  -36.924 1.00 32.22  ? 548 HOH A O   1 
HETATM 5046 O  O   . HOH F 4 .   ? -20.011 -7.688  -45.269 1.00 34.97  ? 549 HOH A O   1 
HETATM 5047 O  O   . HOH F 4 .   ? -19.988 -6.354  -42.371 1.00 33.09  ? 550 HOH A O   1 
HETATM 5048 O  O   A HOH F 4 .   ? 21.142  3.517   -23.061 0.31 42.39  ? 551 HOH A O   1 
HETATM 5049 O  O   B HOH F 4 .   ? 21.142  3.517   -23.061 0.31 42.39  ? 551 HOH A O   1 
HETATM 5050 O  O   . HOH F 4 .   ? -24.557 -9.849  -43.503 1.00 36.15  ? 552 HOH A O   1 
HETATM 5051 O  O   . HOH F 4 .   ? 25.040  2.290   -31.986 1.00 55.02  ? 553 HOH A O   1 
HETATM 5052 O  O   . HOH F 4 .   ? 15.897  -16.398 -29.468 1.00 34.18  ? 554 HOH A O   1 
HETATM 5053 O  O   . HOH F 4 .   ? -1.417  -8.801  -37.191 1.00 36.57  ? 555 HOH A O   1 
HETATM 5054 O  O   . HOH F 4 .   ? -21.119 -10.868 -47.469 1.00 40.23  ? 556 HOH A O   1 
HETATM 5055 O  O   . HOH G 4 .   ? -3.198  29.894  -28.093 1.00 39.65  ? 501 HOH B O   1 
HETATM 5056 O  O   . HOH G 4 .   ? -1.740  25.869  -22.383 1.00 39.82  ? 502 HOH B O   1 
HETATM 5057 O  O   . HOH G 4 .   ? 6.628   29.216  -21.639 1.00 39.42  ? 503 HOH B O   1 
HETATM 5058 O  O   . HOH G 4 .   ? 8.358   2.816   0.765   1.00 43.81  ? 504 HOH B O   1 
HETATM 5059 O  O   . HOH G 4 .   ? 1.140   5.589   -11.980 1.00 29.37  ? 505 HOH B O   1 
HETATM 5060 O  O   . HOH G 4 .   ? -11.795 0.135   -1.142  1.00 20.80  ? 506 HOH B O   1 
HETATM 5061 O  O   . HOH G 4 .   ? -7.949  2.432   -9.987  1.00 28.12  ? 507 HOH B O   1 
HETATM 5062 O  O   . HOH G 4 .   ? -4.162  2.488   8.961   1.00 37.91  ? 508 HOH B O   1 
HETATM 5063 O  O   . HOH G 4 .   ? -2.884  11.100  -14.981 1.00 25.27  ? 509 HOH B O   1 
HETATM 5064 O  O   . HOH G 4 .   ? -18.988 -7.569  8.035   1.00 30.76  ? 510 HOH B O   1 
HETATM 5065 O  O   . HOH G 4 .   ? 2.938   4.615   -7.491  1.00 26.20  ? 511 HOH B O   1 
HETATM 5066 O  O   . HOH G 4 .   ? -1.411  -0.238  5.458   1.00 24.59  ? 512 HOH B O   1 
HETATM 5067 O  O   . HOH G 4 .   ? 2.016   2.738   -0.449  1.00 29.43  ? 513 HOH B O   1 
HETATM 5068 O  O   . HOH G 4 .   ? 2.969   8.745   -6.763  1.00 34.13  ? 514 HOH B O   1 
HETATM 5069 O  O   . HOH G 4 .   ? -12.211 5.578   3.543   1.00 28.77  ? 515 HOH B O   1 
HETATM 5070 O  O   . HOH G 4 .   ? -16.376 -4.341  7.694   1.00 33.46  ? 516 HOH B O   1 
HETATM 5071 O  O   . HOH G 4 .   ? -12.618 -9.727  5.289   1.00 21.10  ? 517 HOH B O   1 
HETATM 5072 O  O   . HOH G 4 .   ? 5.384   6.431   -13.619 1.00 32.48  ? 518 HOH B O   1 
HETATM 5073 O  O   . HOH G 4 .   ? 1.368   7.399   -4.771  1.00 35.88  ? 519 HOH B O   1 
HETATM 5074 O  O   . HOH G 4 .   ? -7.143  17.251  -8.213  1.00 38.37  ? 520 HOH B O   1 
HETATM 5075 O  O   . HOH G 4 .   ? 3.058   4.621   -13.678 1.00 23.50  ? 521 HOH B O   1 
HETATM 5076 O  O   . HOH G 4 .   ? 10.015  5.062   3.180   1.00 45.22  ? 522 HOH B O   1 
HETATM 5077 O  O   . HOH G 4 .   ? -9.969  7.313   4.082   1.00 42.05  ? 523 HOH B O   1 
HETATM 5078 O  O   . HOH G 4 .   ? 4.297   7.002   -25.525 1.00 41.37  ? 524 HOH B O   1 
HETATM 5079 O  O   . HOH G 4 .   ? 2.937   4.793   -25.470 1.00 38.57  ? 525 HOH B O   1 
HETATM 5080 O  O   . HOH G 4 .   ? 12.655  -3.421  -5.819  1.00 37.99  ? 526 HOH B O   1 
# 
