data_7I1D
# 
_entry.id   7I1D 
# 
_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   7I1D         pdb_00007i1d 10.2210/pdb7i1d/pdb 
WWPDB D_1001408192 ?            ?                   
# 
_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                        7I1D 
_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 
_audit_author.identifier_ORCID 
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    1  ?         ? ? ? 
3 non-polymer syn 'N-[(4-bromo-3-methylphenyl)methyl]-2-(methylsulfonyl)ethan-1-amine' 306.219   1  ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                 78.133    1  ?         ? ? ? 
5 non-polymer syn 'SODIUM ION'                                                         22.990    1  ?         ? ? ? 
6 water       nat water                                                                18.015    61 ?         ? ? ? 
# 
_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 'N-[(4-bromo-3-methylphenyl)methyl]-2-(methylsulfonyl)ethan-1-amine' RB7 
4 'DIMETHYL SULFOXIDE'                                                 DMS 
5 'SODIUM ION'                                                         NA  
6 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 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                 ? 'C2 H6 O S'         78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                            ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                      ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                                              ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                                            ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                                                ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                           ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                                              ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                                               ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                                           ? 'C5 H11 N O2 S'     149.211 
NA  non-polymer         . 'SODIUM ION'                                                         ? 'Na 1'              22.990  
PHE 'L-peptide linking' y PHENYLALANINE                                                        ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                                              ? 'C5 H9 N O2'        115.130 
RB7 non-polymer         . 'N-[(4-bromo-3-methylphenyl)methyl]-2-(methylsulfonyl)ethan-1-amine' ? 'C11 H16 Br N O2 S' 306.219 
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 ?   ?   ?   A . n 
A 1 302 GLY 302 302 ?   ?   ?   A . n 
A 1 303 VAL 303 303 ?   ?   ?   A . n 
A 1 304 THR 304 304 ?   ?   ?   A . n 
A 1 305 PHE 305 305 ?   ?   ?   A . n 
A 1 306 GLN 306 306 ?   ?   ?   A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   GLY 2   2   2   GLY GLY B . n 
B 1 3   PHE 3   3   3   PHE PHE B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   MET 6   6   6   MET MET B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  CYS 16  16  16  CYS CYS B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  TRP 31  31  31  TRP TRP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  CYS 38  38  38  CYS CYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  HIS 41  41  41  HIS HIS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  CYS 44  44  44  CYS CYS B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  MET 49  49  49  MET MET B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  ASN 51  51  51  ASN ASN B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 CYS 117 117 117 CYS CYS B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 GLN 127 127 127 GLN GLN B . n 
B 1 128 CYS 128 128 128 CYS CYS B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 MET 130 130 130 MET MET B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 CYS 145 145 145 CYS CYS B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 CYS 160 160 160 CYS CYS B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 MET 162 162 162 MET MET B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 MET 165 165 165 MET MET B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 HIS 172 172 172 HIS HIS B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 TRP 207 207 207 TRP TRP B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 TYR 209 209 209 TYR TYR B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 ASP 216 216 216 ASP ASP B . n 
B 1 217 ARG 217 217 217 ARG ARG B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 ASN 221 221 221 ASN ASN B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 ASN 228 228 228 ASN ASN B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 MET 235 235 235 MET MET B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 GLU 240 240 240 GLU GLU B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 HIS 246 246 246 HIS HIS B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 MET 264 264 264 MET MET B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 GLN 273 273 273 GLN GLN B . n 
B 1 274 ASN 274 274 274 ASN ASN B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 MET 276 276 276 MET MET B . n 
B 1 277 ASN 277 277 277 ASN ASN B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 PHE 291 291 291 PHE PHE B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 PRO 293 293 293 PRO PRO B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLN 299 299 299 GLN GLN B . n 
B 1 300 CYS 300 300 300 CYS CYS B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 GLY 302 302 ?   ?   ?   B . n 
B 1 303 VAL 303 303 ?   ?   ?   B . n 
B 1 304 THR 304 304 ?   ?   ?   B . n 
B 1 305 PHE 305 305 ?   ?   ?   B . n 
B 1 306 GLN 306 306 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        RB7 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   RB7 
_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 RB7 1  402 501 RB7 LIG A . 
E 4 DMS 1  403 601 DMS DMS A . 
F 5 NA  1  401 406 NA  NA  B . 
G 6 HOH 1  501 39  HOH HOH A . 
G 6 HOH 2  502 58  HOH HOH A . 
G 6 HOH 3  503 28  HOH HOH A . 
G 6 HOH 4  504 27  HOH HOH A . 
G 6 HOH 5  505 51  HOH HOH A . 
G 6 HOH 6  506 63  HOH HOH A . 
G 6 HOH 7  507 29  HOH HOH A . 
G 6 HOH 8  508 50  HOH HOH A . 
G 6 HOH 9  509 48  HOH HOH A . 
G 6 HOH 10 510 25  HOH HOH A . 
G 6 HOH 11 511 62  HOH HOH A . 
G 6 HOH 12 512 42  HOH HOH A . 
G 6 HOH 13 513 61  HOH HOH A . 
G 6 HOH 14 514 7   HOH HOH A . 
G 6 HOH 15 515 14  HOH HOH A . 
G 6 HOH 16 516 24  HOH HOH A . 
G 6 HOH 17 517 37  HOH HOH A . 
G 6 HOH 18 518 53  HOH HOH A . 
G 6 HOH 19 519 5   HOH HOH A . 
G 6 HOH 20 520 57  HOH HOH A . 
G 6 HOH 21 521 30  HOH HOH A . 
G 6 HOH 22 522 33  HOH HOH A . 
G 6 HOH 23 523 4   HOH HOH A . 
G 6 HOH 24 524 10  HOH HOH A . 
G 6 HOH 25 525 47  HOH HOH A . 
G 6 HOH 26 526 22  HOH HOH A . 
G 6 HOH 27 527 32  HOH HOH A . 
G 6 HOH 28 528 17  HOH HOH A . 
G 6 HOH 29 529 18  HOH HOH A . 
G 6 HOH 30 530 2   HOH HOH A . 
G 6 HOH 31 531 41  HOH HOH A . 
G 6 HOH 32 532 11  HOH HOH A . 
G 6 HOH 33 533 59  HOH HOH A . 
G 6 HOH 34 534 46  HOH HOH A . 
G 6 HOH 35 535 34  HOH HOH A . 
G 6 HOH 36 536 12  HOH HOH A . 
G 6 HOH 37 537 54  HOH HOH A . 
G 6 HOH 38 538 52  HOH HOH A . 
H 6 HOH 1  501 49  HOH HOH B . 
H 6 HOH 2  502 40  HOH HOH B . 
H 6 HOH 3  503 36  HOH HOH B . 
H 6 HOH 4  504 6   HOH HOH B . 
H 6 HOH 5  505 21  HOH HOH B . 
H 6 HOH 6  506 13  HOH HOH B . 
H 6 HOH 7  507 26  HOH HOH B . 
H 6 HOH 8  508 43  HOH HOH B . 
H 6 HOH 9  509 16  HOH HOH B . 
H 6 HOH 10 510 35  HOH HOH B . 
H 6 HOH 11 511 20  HOH HOH B . 
H 6 HOH 12 512 8   HOH HOH B . 
H 6 HOH 13 513 60  HOH HOH B . 
H 6 HOH 14 514 9   HOH HOH B . 
H 6 HOH 15 515 56  HOH HOH B . 
H 6 HOH 16 516 3   HOH HOH B . 
H 6 HOH 17 517 23  HOH HOH B . 
H 6 HOH 18 518 55  HOH HOH B . 
H 6 HOH 19 519 15  HOH HOH B . 
H 6 HOH 20 520 45  HOH HOH B . 
H 6 HOH 21 521 31  HOH HOH B . 
H 6 HOH 22 522 38  HOH HOH B . 
H 6 HOH 23 523 44  HOH HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
_software.date 
_software.type 
_software.location 
_software.language 
refinement       REFMAC 5.8.0238 ? 1 ? ? ? ? 
'data scaling'   XDS    .        ? 2 ? ? ? ? 
'data reduction' XDS    .        ? 3 ? ? ? ? 
phasing          PHASER .        ? 4 ? ? ? ? 
# 
_cell.entry_id           7I1D 
_cell.length_a           67.960 
_cell.length_b           99.470 
_cell.length_c           103.930 
_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                         7I1D 
_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          7I1D 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.60 
_exptl_crystal.density_percent_sol   52.70 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_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.pdbx_serial_crystal_experiment   ? 
# 
_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                     7I1D 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             46.06 
_reflns.d_resolution_high            2.0 
_reflns.number_obs                   48096 
_reflns.percent_possible_obs         99.5 
_reflns.pdbx_Rmerge_I_obs            0.168 
_reflns.pdbx_netI_over_sigmaI        9.25 
_reflns.pdbx_Rrim_I_all              0.184 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     286525 
_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              ? 
_reflns.pdbx_CC_star                 ? 
_reflns.pdbx_Rpim_I_all              ? 
# 
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 
_reflns_shell.number_unique_all 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_Rpim_I_all 
1 1 2.00 2.12 47209 7682 1.61                 99.9 1.10  1.7590000000000001   0.38               ? ? ? ? ? ? ? 
1 2 2.12 2.27 43979 7238 0.976                99.9 1.81  1.067                0.609              ? ? ? ? ? ? ? 
1 3 2.27 2.45 39893 6750 0.6579999999999999   99.6 2.67  0.721                0.7759999999999999 ? ? ? ? ? ? ? 
1 4 2.45 2.68 36156 6219 0.419                99.8 4.06  0.461                0.8909999999999999 ? ? ? ? ? ? ? 
1 5 2.68 3.0  35023 5667 0.24                 99.9 7.29  0.262                0.971              ? ? ? ? ? ? ? 
1 6 3.00 3.46 29713 5024 0.125                99.6 13.34 0.13699999999999998  0.991              ? ? ? ? ? ? ? 
1 7 3.46 4.23 24164 4242 0.064                99.0 23.85 0.071                0.997              ? ? ? ? ? ? ? 
1 8 4.23 5.95 19865 3348 0.049                98.8 31.04 0.054000000000000006 0.998              ? ? ? ? ? ? ? 
1 9 5.95 ?    10523 1926 0.037000000000000005 96.3 34.65 0.04                 0.9990000000000001 ? ? ? ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7I1D 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     45996 
_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                             46.06 
_refine.ls_d_res_high                            2.00 
_refine.ls_percent_reflns_obs                    99.49 
_refine.ls_R_factor_obs                          0.22808 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.22627 
_refine.ls_R_factor_R_free                       0.26805 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.4 
_refine.ls_number_reflns_R_free                  2100 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.945 
_refine.correlation_coeff_Fo_to_Fc_free          0.918 
_refine.B_iso_mean                               33.493 
_refine.aniso_B[1][1]                            -0.64 
_refine.aniso_B[2][2]                            0.30 
_refine.aniso_B[3][3]                            0.34 
_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                       0.239 
_refine.pdbx_overall_ESU_R_Free                  0.196 
_refine.overall_SU_ML                            0.191 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             7.494 
_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        4652 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         22 
_refine_hist.number_atoms_solvent             61 
_refine_hist.number_atoms_total               4735 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        46.06 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.details                          ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.007  0.014  ? 6930  'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.002  0.018  ? 5928  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.513  1.641  ? 8415  'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.323  1.574  ? 12388 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       17.775 5.212  ? 849   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       36.028 23.265 ? 291   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.199 15.000 ? 924   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       16.946 15.000 ? 24    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.068  0.200  ? 779   'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.006  0.020  ? 7890  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 1325  '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                  2.374  3.427  ? 3564  'X-RAY DIFFRACTION' ? 
r_mcbond_other               2.375  3.428  ? 3559  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 3.946  5.128  ? 4024  'X-RAY DIFFRACTION' ? 
r_mcangle_other              3.946  5.129  ? 4025  'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.953  3.717  ? 3366  'X-RAY DIFFRACTION' ? 
r_scbond_other               2.951  3.717  ? 3366  'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_other              4.825  5.489  ? 4392  'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       7.046  38.302 ? 6149  'X-RAY DIFFRACTION' ? 
r_long_range_B_other         7.046  38.309 ? 6146  '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                       2.000 
_refine_ls_shell.d_res_low                        2.051 
_refine_ls_shell.number_reflns_R_work             3329 
_refine_ls_shell.R_factor_R_work                  0.349 
_refine_ls_shell.percent_reflns_obs               99.80 
_refine_ls_shell.R_factor_R_free                  0.372 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             152 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  7I1D 
_struct.title                     
;PanDDA analysis group deposition -- Main Protease (SARS-CoV-2) in complex with fragment F04 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        7I1D 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SARS-CoV-2, fragment screen, main protease, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 6 ? 
# 
_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 7I1D A 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
2 1 7I1D 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)' 2940  ? 
1 MORE         -29   ? 
1 'SSA (A^2)'  25880 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P4  AA4 SER A 62  ? PHE A 66  ? SER A 62  PHE A 66  5 ? 5  
HELX_P HELX_P5  AA5 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P6  AA6 THR A 226 ? LYS A 236 ? THR A 226 LYS A 236 1 ? 11 
HELX_P HELX_P7  AA7 THR A 243 ? GLY A 258 ? THR A 243 GLY A 258 1 ? 16 
HELX_P HELX_P8  AA8 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P9  AA9 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
HELX_P HELX_P10 AB1 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P11 AB2 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P12 AB3 GLU B 47  ? ASN B 51  ? GLU B 47  ASN B 51  5 ? 5  
HELX_P HELX_P13 AB4 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P14 AB5 SER B 62  ? PHE B 66  ? SER B 62  PHE B 66  5 ? 5  
HELX_P HELX_P15 AB6 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P16 AB7 THR B 226 ? TYR B 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P17 AB8 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P18 AB9 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P19 AC1 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P20 AC2 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_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? B CYS 117 SG  C ? ? 1_555 B CYS 145 SG C ? B CYS 117 B CYS 145 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
disulf2 disulf ? ? B CYS 117 SG  D ? ? 1_555 B CYS 145 SG D ? B CYS 117 B CYS 145 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc1 metalc ? ? B ASN 221 O   ? ? ? 1_555 F NA  .   NA ? ? B ASN 221 B NA  401 1_555 ? ? ? ? ? ? ? 2.660 ? ? 
metalc2 metalc ? ? B ASN 221 OD1 ? ? ? 1_555 F NA  .   NA ? ? B ASN 221 B NA  401 1_555 ? ? ? ? ? ? ? 2.357 ? ? 
metalc3 metalc ? ? B PHE 223 O   ? ? ? 1_555 F NA  .   NA ? ? B PHE 223 B NA  401 1_555 ? ? ? ? ? ? ? 2.396 ? ? 
metalc4 metalc ? ? B ASP 263 O   ? ? ? 1_555 F NA  .   NA ? ? B ASP 263 B NA  401 1_555 ? ? ? ? ? ? ? 2.918 ? ? 
metalc5 metalc ? ? B ASP 263 OD1 ? ? ? 1_555 F NA  .   NA ? ? B ASP 263 B NA  401 1_555 ? ? ? ? ? ? ? 2.230 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 401 ? 1_555 OD1 ? B ASN 221 ? B ASN 221 ? 1_555 79.1  ? 
2  O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 401 ? 1_555 O   ? B PHE 223 ? B PHE 223 ? 1_555 107.8 ? 
3  OD1 ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 401 ? 1_555 O   ? B PHE 223 ? B PHE 223 ? 1_555 100.1 ? 
4  O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 401 ? 1_555 O   ? B ASP 263 ? B ASP 263 ? 1_555 158.5 ? 
5  OD1 ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 401 ? 1_555 O   ? B ASP 263 ? B ASP 263 ? 1_555 113.3 ? 
6  O   ? B PHE 223 ? B PHE 223 ? 1_555 NA ? F NA . ? B NA 401 ? 1_555 O   ? B ASP 263 ? B ASP 263 ? 1_555 87.9  ? 
7  O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 401 ? 1_555 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 92.9  ? 
8  OD1 ? B ASN 221 ? B ASN 221 ? 1_555 NA ? F NA . ? B NA 401 ? 1_555 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 171.9 ? 
9  O   ? B PHE 223 ? B PHE 223 ? 1_555 NA ? F NA . ? B NA 401 ? 1_555 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 82.9  ? 
10 O   ? B ASP 263 ? B ASP 263 ? 1_555 NA ? F NA . ? B NA 401 ? 1_555 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 74.1  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS B 117 C CYS B 145 C CYS B 117 ? 1_555 CYS B 145 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 117 D CYS B 145 D CYS B 117 ? 1_555 CYS B 145 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 LEU A 67  ? ALA A 70  ? LEU A 67  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
AA4 1 VAL B 73  ? LEU B 75  ? VAL B 73  LEU B 75  
AA4 2 LEU B 67  ? ALA B 70  ? LEU B 67  ALA B 70  
AA4 3 MET B 17  ? CYS B 22  ? MET B 17  CYS B 22  
AA4 4 THR B 25  ? LEU B 32  ? THR B 25  LEU B 32  
AA4 5 VAL B 35  ? PRO B 39  ? VAL B 35  PRO B 39  
AA4 6 VAL B 86  ? VAL B 91  ? VAL B 86  VAL B 91  
AA4 7 VAL B 77  ? GLN B 83  ? VAL B 77  GLN B 83  
AA5 1 TYR B 101 ? PHE B 103 ? TYR B 101 PHE B 103 
AA5 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA5 3 VAL B 148 ? ASP B 153 ? VAL B 148 ASP B 153 
AA5 4 THR B 111 ? TYR B 118 ? THR B 111 TYR B 118 
AA5 5 SER B 121 ? ALA B 129 ? SER B 121 ALA B 129 
AA6 1 TYR B 101 ? PHE B 103 ? TYR B 101 PHE B 103 
AA6 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA6 3 HIS B 172 ? THR B 175 ? HIS B 172 THR B 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 75  ? O LEU A 75  N VAL A 68  ? N VAL A 68  
AA1 2 3 O GLN A 69  ? O GLN A 69  N GLN A 19  ? N GLN A 19  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 32  ? N LEU A 32  O VAL A 35  ? O VAL A 35  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O 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 GLN B 69  ? O GLN B 69  N GLN B 19  ? N GLN B 19  
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 SER B 158 ? O SER B 158 N ASN B 151 ? N ASN B 151 
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                   7I1D 
_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   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 33  ? ? 53.49   -128.17 
2  1 ASN A 84  ? ? 57.06   -126.75 
3  1 ASP A 155 ? ? 79.03   -6.99   
4  1 ASP A 176 ? ? -69.99  -179.59 
5  1 LEU A 282 ? ? 37.25   42.05   
6  1 LEU B 27  ? A -162.91 -169.86 
7  1 LEU B 27  ? B -162.91 -169.86 
8  1 ASP B 33  ? ? 42.32   -127.15 
9  1 ASN B 51  ? ? -151.51 78.22   
10 1 ASN B 84  ? ? 53.85   -124.74 
11 1 ASN B 119 ? C 8.65    78.27   
12 1 ASN B 119 ? D 8.65    78.27   
13 1 SER B 123 ? ? -133.32 -31.11  
14 1 SER B 123 ? ? -133.32 -31.11  
15 1 SER B 139 ? C 127.63  83.38   
16 1 SER B 139 ? D 127.63  83.38   
17 1 TYR B 154 ? ? 71.01   -105.43 
18 1 ARG B 279 ? ? -49.46  175.90  
# 
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 SER 301 ? A SER 301 
2  1 Y 1 A GLY 302 ? A GLY 302 
3  1 Y 1 A VAL 303 ? A VAL 303 
4  1 Y 1 A THR 304 ? A THR 304 
5  1 Y 1 A PHE 305 ? A PHE 305 
6  1 Y 1 A GLN 306 ? A GLN 306 
7  1 Y 1 B GLY 302 ? B GLY 302 
8  1 Y 1 B VAL 303 ? B VAL 303 
9  1 Y 1 B THR 304 ? B THR 304 
10 1 Y 1 B PHE 305 ? B PHE 305 
11 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  
DMS S    S  N N 89  
DMS O    O  N N 90  
DMS C1   C  N N 91  
DMS C2   C  N N 92  
DMS H11  H  N N 93  
DMS H12  H  N N 94  
DMS H13  H  N N 95  
DMS H21  H  N N 96  
DMS H22  H  N N 97  
DMS H23  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  N N 260 
NA  NA   NA N N 261 
PHE N    N  N N 262 
PHE CA   C  N S 263 
PHE C    C  N N 264 
PHE O    O  N N 265 
PHE CB   C  N N 266 
PHE CG   C  Y N 267 
PHE CD1  C  Y N 268 
PHE CD2  C  Y N 269 
PHE CE1  C  Y N 270 
PHE CE2  C  Y N 271 
PHE CZ   C  Y N 272 
PHE OXT  O  N N 273 
PHE H    H  N N 274 
PHE H2   H  N N 275 
PHE HA   H  N N 276 
PHE HB2  H  N N 277 
PHE HB3  H  N N 278 
PHE HD1  H  N N 279 
PHE HD2  H  N N 280 
PHE HE1  H  N N 281 
PHE HE2  H  N N 282 
PHE HZ   H  N N 283 
PHE HXT  H  N N 284 
PRO N    N  N N 285 
PRO CA   C  N S 286 
PRO C    C  N N 287 
PRO O    O  N N 288 
PRO CB   C  N N 289 
PRO CG   C  N N 290 
PRO CD   C  N N 291 
PRO OXT  O  N N 292 
PRO H    H  N N 293 
PRO HA   H  N N 294 
PRO HB2  H  N N 295 
PRO HB3  H  N N 296 
PRO HG2  H  N N 297 
PRO HG3  H  N N 298 
PRO HD2  H  N N 299 
PRO HD3  H  N N 300 
PRO HXT  H  N N 301 
RB7 C4   C  Y N 302 
RB7 C5   C  Y N 303 
RB7 C6   C  Y N 304 
RB7 C7   C  N N 305 
RB7 C8   C  N N 306 
RB7 C9   C  N N 307 
RB7 C10  C  N N 308 
RB7 O1   O  N N 309 
RB7 S    S  N N 310 
RB7 O    O  N N 311 
RB7 N    N  N N 312 
RB7 C3   C  Y N 313 
RB7 C2   C  Y N 314 
RB7 BR   BR N N 315 
RB7 C1   C  Y N 316 
RB7 C    C  N N 317 
RB7 H1   H  N N 318 
RB7 H2   H  N N 319 
RB7 H3   H  N N 320 
RB7 H4   H  N N 321 
RB7 H5   H  N N 322 
RB7 H6   H  N N 323 
RB7 H7   H  N N 324 
RB7 H8   H  N N 325 
RB7 H9   H  N N 326 
RB7 H10  H  N N 327 
RB7 H11  H  N N 328 
RB7 H12  H  N N 329 
RB7 H14  H  N N 330 
RB7 H15  H  N N 331 
RB7 H16  H  N N 332 
RB7 H17  H  N N 333 
SER N    N  N N 334 
SER CA   C  N S 335 
SER C    C  N N 336 
SER O    O  N N 337 
SER CB   C  N N 338 
SER OG   O  N N 339 
SER OXT  O  N N 340 
SER H    H  N N 341 
SER H2   H  N N 342 
SER HA   H  N N 343 
SER HB2  H  N N 344 
SER HB3  H  N N 345 
SER HG   H  N N 346 
SER HXT  H  N N 347 
THR N    N  N N 348 
THR CA   C  N S 349 
THR C    C  N N 350 
THR O    O  N N 351 
THR CB   C  N R 352 
THR OG1  O  N N 353 
THR CG2  C  N N 354 
THR OXT  O  N N 355 
THR H    H  N N 356 
THR H2   H  N N 357 
THR HA   H  N N 358 
THR HB   H  N N 359 
THR HG1  H  N N 360 
THR HG21 H  N N 361 
THR HG22 H  N N 362 
THR HG23 H  N N 363 
THR HXT  H  N N 364 
TRP N    N  N N 365 
TRP CA   C  N S 366 
TRP C    C  N N 367 
TRP O    O  N N 368 
TRP CB   C  N N 369 
TRP CG   C  Y N 370 
TRP CD1  C  Y N 371 
TRP CD2  C  Y N 372 
TRP NE1  N  Y N 373 
TRP CE2  C  Y N 374 
TRP CE3  C  Y N 375 
TRP CZ2  C  Y N 376 
TRP CZ3  C  Y N 377 
TRP CH2  C  Y N 378 
TRP OXT  O  N N 379 
TRP H    H  N N 380 
TRP H2   H  N N 381 
TRP HA   H  N N 382 
TRP HB2  H  N N 383 
TRP HB3  H  N N 384 
TRP HD1  H  N N 385 
TRP HE1  H  N N 386 
TRP HE3  H  N N 387 
TRP HZ2  H  N N 388 
TRP HZ3  H  N N 389 
TRP HH2  H  N N 390 
TRP HXT  H  N N 391 
TYR N    N  N N 392 
TYR CA   C  N S 393 
TYR C    C  N N 394 
TYR O    O  N N 395 
TYR CB   C  N N 396 
TYR CG   C  Y N 397 
TYR CD1  C  Y N 398 
TYR CD2  C  Y N 399 
TYR CE1  C  Y N 400 
TYR CE2  C  Y N 401 
TYR CZ   C  Y N 402 
TYR OH   O  N N 403 
TYR OXT  O  N N 404 
TYR H    H  N N 405 
TYR H2   H  N N 406 
TYR HA   H  N N 407 
TYR HB2  H  N N 408 
TYR HB3  H  N N 409 
TYR HD1  H  N N 410 
TYR HD2  H  N N 411 
TYR HE1  H  N N 412 
TYR HE2  H  N N 413 
TYR HH   H  N N 414 
TYR HXT  H  N N 415 
VAL N    N  N N 416 
VAL CA   C  N S 417 
VAL C    C  N N 418 
VAL O    O  N N 419 
VAL CB   C  N N 420 
VAL CG1  C  N N 421 
VAL CG2  C  N N 422 
VAL OXT  O  N N 423 
VAL H    H  N N 424 
VAL H2   H  N N 425 
VAL HA   H  N N 426 
VAL HB   H  N N 427 
VAL HG11 H  N N 428 
VAL HG12 H  N N 429 
VAL HG13 H  N N 430 
VAL HG21 H  N N 431 
VAL HG22 H  N N 432 
VAL HG23 H  N N 433 
VAL HXT  H  N N 434 
# 
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  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
RB7 C10 S    sing N N 286 
RB7 O   S    doub N N 287 
RB7 S   C9   sing N N 288 
RB7 S   O1   doub N N 289 
RB7 C9  C8   sing N N 290 
RB7 C8  N    sing N N 291 
RB7 N   C7   sing N N 292 
RB7 C   C1   sing N N 293 
RB7 C2  C1   doub Y N 294 
RB7 C2  C3   sing Y N 295 
RB7 C1  C6   sing Y N 296 
RB7 C7  C3   sing N N 297 
RB7 C3  C4   doub Y N 298 
RB7 C6  BR   sing N N 299 
RB7 C6  C5   doub Y N 300 
RB7 C4  C5   sing Y N 301 
RB7 C4  H1   sing N N 302 
RB7 C5  H2   sing N N 303 
RB7 C7  H3   sing N N 304 
RB7 C7  H4   sing N N 305 
RB7 C8  H5   sing N N 306 
RB7 C8  H6   sing N N 307 
RB7 C9  H7   sing N N 308 
RB7 C9  H8   sing N N 309 
RB7 C10 H9   sing N N 310 
RB7 C10 H10  sing N N 311 
RB7 C10 H11  sing N N 312 
RB7 N   H12  sing N N 313 
RB7 C2  H14  sing N N 314 
RB7 C   H15  sing N N 315 
RB7 C   H16  sing N N 316 
RB7 C   H17  sing N N 317 
SER N   CA   sing N N 318 
SER N   H    sing N N 319 
SER N   H2   sing N N 320 
SER CA  C    sing N N 321 
SER CA  CB   sing N N 322 
SER CA  HA   sing N N 323 
SER C   O    doub N N 324 
SER C   OXT  sing N N 325 
SER CB  OG   sing N N 326 
SER CB  HB2  sing N N 327 
SER CB  HB3  sing N N 328 
SER OG  HG   sing N N 329 
SER OXT HXT  sing N N 330 
THR N   CA   sing N N 331 
THR N   H    sing N N 332 
THR N   H2   sing N N 333 
THR CA  C    sing N N 334 
THR CA  CB   sing N N 335 
THR CA  HA   sing N N 336 
THR C   O    doub N N 337 
THR C   OXT  sing N N 338 
THR CB  OG1  sing N N 339 
THR CB  CG2  sing N N 340 
THR CB  HB   sing N N 341 
THR OG1 HG1  sing N N 342 
THR CG2 HG21 sing N N 343 
THR CG2 HG22 sing N N 344 
THR CG2 HG23 sing N N 345 
THR OXT HXT  sing N N 346 
TRP N   CA   sing N N 347 
TRP N   H    sing N N 348 
TRP N   H2   sing N N 349 
TRP CA  C    sing N N 350 
TRP CA  CB   sing N N 351 
TRP CA  HA   sing N N 352 
TRP C   O    doub N N 353 
TRP C   OXT  sing N N 354 
TRP CB  CG   sing N N 355 
TRP CB  HB2  sing N N 356 
TRP CB  HB3  sing N N 357 
TRP CG  CD1  doub Y N 358 
TRP CG  CD2  sing Y N 359 
TRP CD1 NE1  sing Y N 360 
TRP CD1 HD1  sing N N 361 
TRP CD2 CE2  doub Y N 362 
TRP CD2 CE3  sing Y N 363 
TRP NE1 CE2  sing Y N 364 
TRP NE1 HE1  sing N N 365 
TRP CE2 CZ2  sing Y N 366 
TRP CE3 CZ3  doub Y N 367 
TRP CE3 HE3  sing N N 368 
TRP CZ2 CH2  doub Y N 369 
TRP CZ2 HZ2  sing N N 370 
TRP CZ3 CH2  sing Y N 371 
TRP CZ3 HZ3  sing N N 372 
TRP CH2 HH2  sing N N 373 
TRP OXT HXT  sing N N 374 
TYR N   CA   sing N N 375 
TYR N   H    sing N N 376 
TYR N   H2   sing N N 377 
TYR CA  C    sing N N 378 
TYR CA  CB   sing N N 379 
TYR CA  HA   sing N N 380 
TYR C   O    doub N N 381 
TYR C   OXT  sing N N 382 
TYR CB  CG   sing N N 383 
TYR CB  HB2  sing N N 384 
TYR CB  HB3  sing N N 385 
TYR CG  CD1  doub Y N 386 
TYR CG  CD2  sing Y N 387 
TYR CD1 CE1  sing Y N 388 
TYR CD1 HD1  sing N N 389 
TYR CD2 CE2  doub Y N 390 
TYR CD2 HD2  sing N N 391 
TYR CE1 CZ   doub Y N 392 
TYR CE1 HE1  sing N N 393 
TYR CE2 CZ   sing Y N 394 
TYR CE2 HE2  sing N N 395 
TYR CZ  OH   sing N N 396 
TYR OH  HH   sing N N 397 
TYR OXT HXT  sing N N 398 
VAL N   CA   sing N N 399 
VAL N   H    sing N N 400 
VAL N   H2   sing N N 401 
VAL CA  C    sing N N 402 
VAL CA  CB   sing N N 403 
VAL CA  HA   sing N N 404 
VAL C   O    doub N N 405 
VAL C   OXT  sing N N 406 
VAL CB  CG1  sing N N 407 
VAL CB  CG2  sing N N 408 
VAL CB  HB   sing N N 409 
VAL CG1 HG11 sing N N 410 
VAL CG1 HG12 sing N N 411 
VAL CG1 HG13 sing N N 412 
VAL CG2 HG21 sing N N 413 
VAL CG2 HG22 sing N N 414 
VAL CG2 HG23 sing N N 415 
VAL OXT HXT  sing N N 416 
# 
_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 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I1D 
_atom_sites.fract_transf_matrix[1][1]   0.014715 
_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]   0.010053 
_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]   0.009622 
_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 
BR 
C  
CL 
N  
NA 
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   ? -13.972 -9.727  -12.554 1.00 57.36  ? 1   SER A N   1 
ATOM   2    C  CA  . SER A 1 1   ? -14.267 -8.659  -13.545 1.00 56.84  ? 1   SER A CA  1 
ATOM   3    C  C   . SER A 1 1   ? -13.124 -7.623  -13.577 1.00 58.16  ? 1   SER A C   1 
ATOM   4    O  O   . SER A 1 1   ? -12.263 -7.626  -12.654 1.00 57.86  ? 1   SER A O   1 
ATOM   5    C  CB  . SER A 1 1   ? -15.604 -8.035  -13.222 1.00 55.18  ? 1   SER A CB  1 
ATOM   6    O  OG  . SER A 1 1   ? -15.921 -6.955  -14.082 1.00 55.91  ? 1   SER A OG  1 
ATOM   7    N  N   . GLY A 1 2   ? -13.129 -6.758  -14.599 1.00 54.40  ? 2   GLY A N   1 
ATOM   8    C  CA  . GLY A 1 2   ? -12.083 -5.756  -14.878 1.00 52.19  ? 2   GLY A CA  1 
ATOM   9    C  C   . GLY A 1 2   ? -11.095 -6.295  -15.901 1.00 50.15  ? 2   GLY A C   1 
ATOM   10   O  O   . GLY A 1 2   ? -10.960 -7.530  -16.002 1.00 54.52  ? 2   GLY A O   1 
ATOM   11   N  N   . PHE A 1 3   ? -10.485 -5.403  -16.687 1.00 49.84  ? 3   PHE A N   1 
ATOM   12   C  CA  . PHE A 1 3   ? -9.537  -5.743  -17.777 1.00 49.13  ? 3   PHE A CA  1 
ATOM   13   C  C   . PHE A 1 3   ? -8.452  -4.666  -17.863 1.00 50.12  ? 3   PHE A C   1 
ATOM   14   O  O   . PHE A 1 3   ? -8.735  -3.502  -18.200 1.00 56.90  ? 3   PHE A O   1 
ATOM   15   C  CB  . PHE A 1 3   ? -10.266 -5.930  -19.108 1.00 47.15  ? 3   PHE A CB  1 
ATOM   16   C  CG  . PHE A 1 3   ? -9.544  -6.854  -20.047 1.00 46.94  ? 3   PHE A CG  1 
ATOM   17   C  CD1 . PHE A 1 3   ? -9.663  -8.227  -19.903 1.00 51.74  ? 3   PHE A CD1 1 
ATOM   18   C  CD2 . PHE A 1 3   ? -8.717  -6.356  -21.041 1.00 46.22  ? 3   PHE A CD2 1 
ATOM   19   C  CE1 . PHE A 1 3   ? -8.978  -9.090  -20.747 1.00 53.78  ? 3   PHE A CE1 1 
ATOM   20   C  CE2 . PHE A 1 3   ? -8.046  -7.216  -21.892 1.00 48.74  ? 3   PHE A CE2 1 
ATOM   21   C  CZ  . PHE A 1 3   ? -8.170  -8.582  -21.739 1.00 54.47  ? 3   PHE A CZ  1 
ATOM   22   N  N   . ARG A 1 4   ? -7.222  -5.082  -17.588 1.00 45.52  ? 4   ARG A N   1 
ATOM   23   C  CA  . ARG A 1 4   ? -6.049  -4.206  -17.398 1.00 42.72  ? 4   ARG A CA  1 
ATOM   24   C  C   . ARG A 1 4   ? -4.880  -4.769  -18.193 1.00 37.51  ? 4   ARG A C   1 
ATOM   25   O  O   . ARG A 1 4   ? -4.770  -6.012  -18.256 1.00 32.46  ? 4   ARG A O   1 
ATOM   26   C  CB  . ARG A 1 4   ? -5.698  -4.191  -15.910 1.00 48.42  ? 4   ARG A CB  1 
ATOM   27   C  CG  . ARG A 1 4   ? -6.500  -3.184  -15.109 1.00 51.42  ? 4   ARG A CG  1 
ATOM   28   C  CD  . ARG A 1 4   ? -5.724  -1.897  -14.983 1.00 57.20  ? 4   ARG A CD  1 
ATOM   29   N  NE  . ARG A 1 4   ? -6.319  -1.036  -13.987 1.00 62.33  ? 4   ARG A NE  1 
ATOM   30   C  CZ  . ARG A 1 4   ? -5.761  0.072   -13.518 1.00 74.18  ? 4   ARG A CZ  1 
ATOM   31   N  NH1 . ARG A 1 4   ? -4.565  0.447   -13.949 1.00 81.98  ? 4   ARG A NH1 1 
ATOM   32   N  NH2 . ARG A 1 4   ? -6.407  0.803   -12.620 1.00 73.09  ? 4   ARG A NH2 1 
ATOM   33   N  N   . LYS A 1 5   ? -4.039  -3.887  -18.727 1.00 34.05  ? 5   LYS A N   1 
ATOM   34   C  CA  . LYS A 1 5   ? -2.700  -4.245  -19.247 1.00 40.09  ? 5   LYS A CA  1 
ATOM   35   C  C   . LYS A 1 5   ? -1.891  -4.742  -18.056 1.00 41.19  ? 5   LYS A C   1 
ATOM   36   O  O   . LYS A 1 5   ? -1.399  -3.925  -17.252 1.00 46.56  ? 5   LYS A O   1 
ATOM   37   C  CB  . LYS A 1 5   ? -1.964  -3.073  -19.899 1.00 39.64  ? 5   LYS A CB  1 
ATOM   38   C  CG  . LYS A 1 5   ? -2.265  -2.890  -21.367 1.00 47.43  ? 5   LYS A CG  1 
ATOM   39   C  CD  . LYS A 1 5   ? -1.181  -3.357  -22.288 1.00 53.49  ? 5   LYS A CD  1 
ATOM   40   C  CE  . LYS A 1 5   ? -1.344  -2.769  -23.673 1.00 58.47  ? 5   LYS A CE  1 
ATOM   41   N  NZ  . LYS A 1 5   ? -1.600  -1.309  -23.642 1.00 59.23  ? 5   LYS A NZ  1 
ATOM   42   N  N   . MET A 1 6   ? -1.782  -6.045  -17.941 1.00 34.56  ? 6   MET A N   1 
ATOM   43   C  CA  . MET A 1 6   ? -1.108  -6.676  -16.798 1.00 33.20  ? 6   MET A CA  1 
ATOM   44   C  C   . MET A 1 6   ? 0.268   -7.158  -17.273 1.00 28.25  ? 6   MET A C   1 
ATOM   45   O  O   . MET A 1 6   ? 0.355   -7.811  -18.352 1.00 26.96  ? 6   MET A O   1 
ATOM   46   C  CB  . MET A 1 6   ? -2.012  -7.815  -16.346 1.00 40.02  ? 6   MET A CB  1 
ATOM   47   C  CG  . MET A 1 6   ? -1.597  -8.535  -15.105 1.00 47.40  ? 6   MET A CG  1 
ATOM   48   S  SD  . MET A 1 6   ? -2.934  -9.715  -14.656 1.00 57.72  ? 6   MET A SD  1 
ATOM   49   C  CE  . MET A 1 6   ? -4.240  -8.569  -14.230 1.00 44.95  ? 6   MET A CE  1 
ATOM   50   N  N   . ALA A 1 7   ? 1.305   -6.859  -16.508 1.00 23.31  ? 7   ALA A N   1 
ATOM   51   C  CA  . ALA A 1 7   ? 2.674   -7.350  -16.776 1.00 25.11  ? 7   ALA A CA  1 
ATOM   52   C  C   . ALA A 1 7   ? 2.930   -8.600  -15.927 1.00 25.89  ? 7   ALA A C   1 
ATOM   53   O  O   . ALA A 1 7   ? 2.182   -8.847  -14.972 1.00 23.40  ? 7   ALA A O   1 
ATOM   54   C  CB  . ALA A 1 7   ? 3.681   -6.266  -16.510 1.00 23.69  ? 7   ALA A CB  1 
ATOM   55   N  N   . PHE A 1 8   ? 3.943   -9.384  -16.276 1.00 25.57  ? 8   PHE A N   1 
ATOM   56   C  CA  . PHE A 1 8   ? 4.316   -10.576 -15.477 1.00 25.06  ? 8   PHE A CA  1 
ATOM   57   C  C   . PHE A 1 8   ? 5.012   -10.075 -14.233 1.00 24.04  ? 8   PHE A C   1 
ATOM   58   O  O   . PHE A 1 8   ? 5.652   -9.026  -14.258 1.00 22.84  ? 8   PHE A O   1 
ATOM   59   C  CB  . PHE A 1 8   ? 5.195   -11.523 -16.288 1.00 26.77  ? 8   PHE A CB  1 
ATOM   60   C  CG  . PHE A 1 8   ? 4.413   -12.334 -17.288 1.00 26.36  ? 8   PHE A CG  1 
ATOM   61   C  CD1 . PHE A 1 8   ? 3.605   -13.374 -16.875 1.00 28.84  ? 8   PHE A CD1 1 
ATOM   62   C  CD2 . PHE A 1 8   ? 4.422   -11.999 -18.626 1.00 28.77  ? 8   PHE A CD2 1 
ATOM   63   C  CE1 . PHE A 1 8   ? 2.893   -14.126 -17.797 1.00 30.86  ? 8   PHE A CE1 1 
ATOM   64   C  CE2 . PHE A 1 8   ? 3.692   -12.736 -19.546 1.00 28.15  ? 8   PHE A CE2 1 
ATOM   65   C  CZ  . PHE A 1 8   ? 2.920   -13.784 -19.131 1.00 28.54  ? 8   PHE A CZ  1 
ATOM   66   N  N   . PRO A 1 9   ? 4.915   -10.819 -13.116 1.00 22.88  ? 9   PRO A N   1 
ATOM   67   C  CA  . PRO A 1 9   ? 5.734   -10.523 -11.947 1.00 22.95  ? 9   PRO A CA  1 
ATOM   68   C  C   . PRO A 1 9   ? 7.222   -10.512 -12.363 1.00 23.23  ? 9   PRO A C   1 
ATOM   69   O  O   . PRO A 1 9   ? 7.718   -11.449 -13.032 1.00 24.80  ? 9   PRO A O   1 
ATOM   70   C  CB  . PRO A 1 9   ? 5.358   -11.623 -10.943 1.00 23.10  ? 9   PRO A CB  1 
ATOM   71   C  CG  . PRO A 1 9   ? 4.015   -12.136 -11.429 1.00 24.19  ? 9   PRO A CG  1 
ATOM   72   C  CD  . PRO A 1 9   ? 4.043   -11.988 -12.939 1.00 24.11  ? 9   PRO A CD  1 
ATOM   73   N  N   . SER A 1 10  ? 7.932   -9.468  -11.958 1.00 21.55  ? 10  SER A N   1 
ATOM   74   C  CA  . SER A 1 10  ? 9.275   -9.154  -12.488 1.00 20.80  ? 10  SER A CA  1 
ATOM   75   C  C   . SER A 1 10  ? 10.387  -9.803  -11.654 1.00 20.24  ? 10  SER A C   1 
ATOM   76   O  O   . SER A 1 10  ? 11.519  -9.704  -12.080 1.00 21.31  ? 10  SER A O   1 
ATOM   77   C  CB  . SER A 1 10  ? 9.448   -7.686  -12.602 1.00 20.24  ? 10  SER A CB  1 
ATOM   78   O  OG  . SER A 1 10  ? 9.411   -7.089  -11.312 1.00 24.00  ? 10  SER A OG  1 
ATOM   79   N  N   . GLY A 1 11  ? 10.088  -10.457 -10.536 1.00 19.34  ? 11  GLY A N   1 
ATOM   80   C  CA  . GLY A 1 11  ? 11.117  -10.935 -9.579  1.00 20.96  ? 11  GLY A CA  1 
ATOM   81   C  C   . GLY A 1 11  ? 12.181  -11.845 -10.196 1.00 19.93  ? 11  GLY A C   1 
ATOM   82   O  O   . GLY A 1 11  ? 13.362  -11.652 -9.913  1.00 20.26  ? 11  GLY A O   1 
ATOM   83   N  N   . LYS A 1 12  ? 11.788  -12.821 -11.001 1.00 20.57  ? 12  LYS A N   1 
ATOM   84   C  CA  . LYS A 1 12  ? 12.755  -13.781 -11.598 1.00 23.72  ? 12  LYS A CA  1 
ATOM   85   C  C   . LYS A 1 12  ? 13.703  -13.040 -12.547 1.00 25.39  ? 12  LYS A C   1 
ATOM   86   O  O   . LYS A 1 12  ? 14.824  -13.529 -12.741 1.00 29.28  ? 12  LYS A O   1 
ATOM   87   C  CB  . LYS A 1 12  ? 12.038  -14.886 -12.361 1.00 24.53  ? 12  LYS A CB  1 
ATOM   88   C  CG  . LYS A 1 12  ? 11.280  -15.864 -11.481 1.00 25.92  ? 12  LYS A CG  1 
ATOM   89   C  CD  . LYS A 1 12  ? 10.425  -16.787 -12.270 1.00 27.52  ? 12  LYS A CD  1 
ATOM   90   C  CE  . LYS A 1 12  ? 9.905   -17.945 -11.445 1.00 31.71  ? 12  LYS A CE  1 
ATOM   91   N  NZ  . LYS A 1 12  ? 9.031   -17.462 -10.357 1.00 33.06  ? 12  LYS A NZ  1 
ATOM   92   N  N   . VAL A 1 13  ? 13.269  -11.916 -13.125 1.00 21.75  ? 13  VAL A N   1 
ATOM   93   C  CA  . VAL A 1 13  ? 14.123  -11.099 -14.020 1.00 22.55  ? 13  VAL A CA  1 
ATOM   94   C  C   . VAL A 1 13  ? 14.980  -10.160 -13.175 1.00 20.91  ? 13  VAL A C   1 
ATOM   95   O  O   . VAL A 1 13  ? 16.142  -10.017 -13.493 1.00 23.86  ? 13  VAL A O   1 
ATOM   96   C  CB  . VAL A 1 13  ? 13.310  -10.367 -15.111 1.00 21.84  ? 13  VAL A CB  1 
ATOM   97   C  CG1 . VAL A 1 13  ? 14.237  -9.590  -16.057 1.00 21.96  ? 13  VAL A CG1 1 
ATOM   98   C  CG2 . VAL A 1 13  ? 12.467  -11.353 -15.893 1.00 22.20  ? 13  VAL A CG2 1 
ATOM   99   N  N   . GLU A 1 14  ? 14.447  -9.591  -12.106 1.00 22.37  ? 14  GLU A N   1 
ATOM   100  C  CA  . GLU A 1 14  ? 15.205  -8.662  -11.221 1.00 22.23  ? 14  GLU A CA  1 
ATOM   101  C  C   . GLU A 1 14  ? 16.499  -9.325  -10.710 1.00 24.46  ? 14  GLU A C   1 
ATOM   102  O  O   . GLU A 1 14  ? 17.546  -8.655  -10.723 1.00 24.70  ? 14  GLU A O   1 
ATOM   103  C  CB  . GLU A 1 14  ? 14.354  -8.194  -10.047 1.00 21.81  ? 14  GLU A CB  1 
ATOM   104  C  CG  . GLU A 1 14  ? 13.173  -7.333  -10.439 1.00 21.99  ? 14  GLU A CG  1 
ATOM   105  C  CD  . GLU A 1 14  ? 12.191  -7.157  -9.292  1.00 23.50  ? 14  GLU A CD  1 
ATOM   106  O  OE1 . GLU A 1 14  ? 12.616  -6.718  -8.228  1.00 24.90  ? 14  GLU A OE1 1 
ATOM   107  O  OE2 . GLU A 1 14  ? 11.006  -7.473  -9.463  1.00 24.92  ? 14  GLU A OE2 1 
ATOM   108  N  N   . GLY A 1 15  ? 16.466  -10.596 -10.322 1.00 23.99  ? 15  GLY A N   1 
ATOM   109  C  CA  . GLY A 1 15  ? 17.669  -11.278 -9.801  1.00 26.52  ? 15  GLY A CA  1 
ATOM   110  C  C   . GLY A 1 15  ? 18.733  -11.555 -10.867 1.00 26.74  ? 15  GLY A C   1 
ATOM   111  O  O   . GLY A 1 15  ? 19.717  -12.225 -10.504 1.00 26.05  ? 15  GLY A O   1 
ATOM   112  N  N   . CYS A 1 16  ? 18.539  -11.126 -12.131 1.00 24.86  ? 16  CYS A N   1 
ATOM   113  C  CA  . CYS A 1 16  ? 19.454  -11.389 -13.276 1.00 24.60  ? 16  CYS A CA  1 
ATOM   114  C  C   . CYS A 1 16  ? 20.038  -10.076 -13.830 1.00 25.91  ? 16  CYS A C   1 
ATOM   115  O  O   . CYS A 1 16  ? 20.941  -10.131 -14.710 1.00 21.87  ? 16  CYS A O   1 
ATOM   116  C  CB  . CYS A 1 16  ? 18.752  -12.104 -14.420 1.00 23.68  ? 16  CYS A CB  1 
ATOM   117  S  SG  . CYS A 1 16  ? 17.957  -13.666 -13.991 1.00 26.88  ? 16  CYS A SG  1 
ATOM   118  N  N   . MET A 1 17  ? 19.575  -8.930  -13.331 1.00 25.13  ? 17  MET A N   1 
ATOM   119  C  CA  . MET A 1 17  ? 19.980  -7.622  -13.896 1.00 24.65  ? 17  MET A CA  1 
ATOM   120  C  C   . MET A 1 17  ? 21.281  -7.169  -13.228 1.00 24.32  ? 17  MET A C   1 
ATOM   121  O  O   . MET A 1 17  ? 21.334  -7.140  -12.019 1.00 25.10  ? 17  MET A O   1 
ATOM   122  C  CB  . MET A 1 17  ? 18.879  -6.568  -13.733 1.00 24.48  ? 17  MET A CB  1 
ATOM   123  C  CG  . MET A 1 17  ? 17.589  -6.916  -14.453 1.00 23.96  ? 17  MET A CG  1 
ATOM   124  S  SD  . MET A 1 17  ? 17.775  -7.406  -16.177 1.00 25.41  ? 17  MET A SD  1 
ATOM   125  C  CE  . MET A 1 17  ? 18.709  -6.048  -16.892 1.00 25.47  ? 17  MET A CE  1 
ATOM   126  N  N   . VAL A 1 18  ? 22.298  -6.839  -14.021 1.00 26.95  ? 18  VAL A N   1 
ATOM   127  C  CA  . VAL A 1 18  ? 23.601  -6.294  -13.543 1.00 25.48  ? 18  VAL A CA  1 
ATOM   128  C  C   . VAL A 1 18  ? 23.946  -5.051  -14.341 1.00 25.35  ? 18  VAL A C   1 
ATOM   129  O  O   . VAL A 1 18  ? 23.303  -4.804  -15.393 1.00 24.87  ? 18  VAL A O   1 
ATOM   130  C  CB  . VAL A 1 18  ? 24.722  -7.343  -13.633 1.00 26.40  ? 18  VAL A CB  1 
ATOM   131  C  CG1 . VAL A 1 18  ? 24.419  -8.532  -12.741 1.00 26.94  ? 18  VAL A CG1 1 
ATOM   132  C  CG2 . VAL A 1 18  ? 24.977  -7.814  -15.055 1.00 26.91  ? 18  VAL A CG2 1 
ATOM   133  N  N   . GLN A 1 19  ? 24.964  -4.325  -13.875 1.00 28.28  ? 19  GLN A N   1 
ATOM   134  C  CA  . GLN A 1 19  ? 25.541  -3.149  -14.580 1.00 30.93  ? 19  GLN A CA  1 
ATOM   135  C  C   . GLN A 1 19  ? 26.803  -3.583  -15.361 1.00 30.50  ? 19  GLN A C   1 
ATOM   136  O  O   . GLN A 1 19  ? 27.633  -4.302  -14.805 1.00 27.07  ? 19  GLN A O   1 
ATOM   137  C  CB  . GLN A 1 19  ? 25.766  -2.061  -13.537 1.00 34.55  ? 19  GLN A CB  1 
ATOM   138  C  CG  . GLN A 1 19  ? 26.515  -0.857  -14.063 1.00 38.83  ? 19  GLN A CG  1 
ATOM   139  C  CD  . GLN A 1 19  ? 26.690  0.188   -12.983 1.00 46.41  ? 19  GLN A CD  1 
ATOM   140  O  OE1 . GLN A 1 19  ? 25.832  1.050   -12.790 1.00 55.42  ? 19  GLN A OE1 1 
ATOM   141  N  NE2 . GLN A 1 19  ? 27.801  0.118   -12.262 1.00 45.68  ? 19  GLN A NE2 1 
ATOM   142  N  N   . VAL A 1 20  ? 26.912  -3.212  -16.642 1.00 27.29  ? 20  VAL A N   1 
ATOM   143  C  CA  . VAL A 1 20  ? 28.101  -3.484  -17.490 1.00 27.01  ? 20  VAL A CA  1 
ATOM   144  C  C   . VAL A 1 20  ? 28.697  -2.140  -17.895 1.00 27.44  ? 20  VAL A C   1 
ATOM   145  O  O   . VAL A 1 20  ? 27.952  -1.275  -18.418 1.00 28.13  ? 20  VAL A O   1 
ATOM   146  C  CB  . VAL A 1 20  ? 27.734  -4.330  -18.721 1.00 26.84  ? 20  VAL A CB  1 
ATOM   147  C  CG1 . VAL A 1 20  ? 28.938  -4.599  -19.612 1.00 25.45  ? 20  VAL A CG1 1 
ATOM   148  C  CG2 . VAL A 1 20  ? 27.060  -5.628  -18.319 1.00 27.18  ? 20  VAL A CG2 1 
ATOM   149  N  N   . THR A 1 21  ? 29.995  -1.963  -17.657 1.00 29.14  ? 21  THR A N   1 
ATOM   150  C  CA  . THR A 1 21  ? 30.715  -0.724  -18.023 1.00 30.10  ? 21  THR A CA  1 
ATOM   151  C  C   . THR A 1 21  ? 31.891  -1.083  -18.925 1.00 33.42  ? 21  THR A C   1 
ATOM   152  O  O   . THR A 1 21  ? 32.537  -2.126  -18.697 1.00 32.01  ? 21  THR A O   1 
ATOM   153  C  CB  . THR A 1 21  ? 31.146  0.100   -16.814 1.00 31.71  ? 21  THR A CB  1 
ATOM   154  O  OG1 . THR A 1 21  ? 29.988  0.394   -16.043 1.00 30.59  ? 21  THR A OG1 1 
ATOM   155  C  CG2 . THR A 1 21  ? 31.816  1.392   -17.227 1.00 34.97  ? 21  THR A CG2 1 
ATOM   156  N  N   . CYS A 1 22  ? 32.084  -0.275  -19.966 1.00 34.56  ? 22  CYS A N   1 
ATOM   157  C  CA  . CYS A 1 22  ? 33.193  -0.401  -20.937 1.00 37.12  ? 22  CYS A CA  1 
ATOM   158  C  C   . CYS A 1 22  ? 33.503  1.018   -21.400 1.00 38.11  ? 22  CYS A C   1 
ATOM   159  O  O   . CYS A 1 22  ? 32.539  1.732   -21.741 1.00 33.90  ? 22  CYS A O   1 
ATOM   160  C  CB  . CYS A 1 22  ? 32.788  -1.328  -22.078 1.00 36.92  ? 22  CYS A CB  1 
ATOM   161  S  SG  . CYS A 1 22  ? 34.159  -1.785  -23.162 1.00 40.19  ? 22  CYS A SG  1 
ATOM   162  N  N   . GLY A 1 23  ? 34.763  1.453   -21.329 1.00 39.26  ? 23  GLY A N   1 
ATOM   163  C  CA  . GLY A 1 23  ? 35.099  2.874   -21.545 1.00 34.97  ? 23  GLY A CA  1 
ATOM   164  C  C   . GLY A 1 23  ? 34.317  3.727   -20.561 1.00 34.76  ? 23  GLY A C   1 
ATOM   165  O  O   . GLY A 1 23  ? 34.315  3.422   -19.355 1.00 37.17  ? 23  GLY A O   1 
ATOM   166  N  N   A THR A 1 24  ? 33.661  4.773   -21.075 0.20 35.05  ? 24  THR A N   1 
ATOM   167  N  N   B THR A 1 24  ? 33.661  4.773   -21.075 0.20 35.05  ? 24  THR A N   1 
ATOM   168  N  N   C THR A 1 24  ? 33.644  4.772   -21.050 0.30 37.07  ? 24  THR A N   1 
ATOM   169  N  N   D THR A 1 24  ? 33.644  4.772   -21.050 0.30 37.07  ? 24  THR A N   1 
ATOM   170  C  CA  A THR A 1 24  ? 32.798  5.712   -20.308 0.20 35.05  ? 24  THR A CA  1 
ATOM   171  C  CA  B THR A 1 24  ? 32.798  5.712   -20.308 0.20 35.05  ? 24  THR A CA  1 
ATOM   172  C  CA  C THR A 1 24  ? 32.732  5.634   -20.245 0.30 38.65  ? 24  THR A CA  1 
ATOM   173  C  CA  D THR A 1 24  ? 32.732  5.634   -20.245 0.30 38.65  ? 24  THR A CA  1 
ATOM   174  C  C   A THR A 1 24  ? 31.317  5.324   -20.439 0.20 34.32  ? 24  THR A C   1 
ATOM   175  C  C   B THR A 1 24  ? 31.317  5.324   -20.438 0.20 34.32  ? 24  THR A C   1 
ATOM   176  C  C   C THR A 1 24  ? 31.273  5.164   -20.363 0.30 37.22  ? 24  THR A C   1 
ATOM   177  C  C   D THR A 1 24  ? 31.273  5.164   -20.363 0.30 37.22  ? 24  THR A C   1 
ATOM   178  O  O   A THR A 1 24  ? 30.470  6.143   -20.028 0.20 34.91  ? 24  THR A O   1 
ATOM   179  O  O   B THR A 1 24  ? 30.470  6.143   -20.028 0.20 34.91  ? 24  THR A O   1 
ATOM   180  O  O   C THR A 1 24  ? 30.414  5.807   -19.734 0.30 39.28  ? 24  THR A O   1 
ATOM   181  O  O   D THR A 1 24  ? 30.414  5.807   -19.734 0.30 39.28  ? 24  THR A O   1 
ATOM   182  C  CB  A THR A 1 24  ? 32.987  7.154   -20.794 0.20 35.41  ? 24  THR A CB  1 
ATOM   183  C  CB  B THR A 1 24  ? 32.987  7.154   -20.794 0.20 35.41  ? 24  THR A CB  1 
ATOM   184  C  CB  C THR A 1 24  ? 32.841  7.106   -20.661 0.30 40.44  ? 24  THR A CB  1 
ATOM   185  C  CB  D THR A 1 24  ? 32.841  7.106   -20.661 0.30 40.44  ? 24  THR A CB  1 
ATOM   186  O  OG1 A THR A 1 24  ? 32.563  7.224   -22.157 0.20 34.68  ? 24  THR A OG1 1 
ATOM   187  O  OG1 B THR A 1 24  ? 32.563  7.224   -22.157 0.20 34.68  ? 24  THR A OG1 1 
ATOM   188  O  OG1 C THR A 1 24  ? 33.192  7.125   -22.045 0.30 41.72  ? 24  THR A OG1 1 
ATOM   189  O  OG1 D THR A 1 24  ? 33.192  7.125   -22.045 0.30 41.72  ? 24  THR A OG1 1 
ATOM   190  C  CG2 A THR A 1 24  ? 34.415  7.641   -20.662 0.20 35.42  ? 24  THR A CG2 1 
ATOM   191  C  CG2 B THR A 1 24  ? 34.415  7.641   -20.662 0.20 35.42  ? 24  THR A CG2 1 
ATOM   192  C  CG2 C THR A 1 24  ? 33.850  7.879   -19.837 0.30 41.49  ? 24  THR A CG2 1 
ATOM   193  C  CG2 D THR A 1 24  ? 33.850  7.879   -19.837 0.30 41.49  ? 24  THR A CG2 1 
ATOM   194  N  N   A THR A 1 25  ? 31.016  4.144   -20.996 0.20 33.73  ? 25  THR A N   1 
ATOM   195  N  N   B THR A 1 25  ? 31.016  4.144   -20.996 0.20 33.73  ? 25  THR A N   1 
ATOM   196  N  N   C THR A 1 25  ? 30.997  4.104   -21.134 0.30 36.35  ? 25  THR A N   1 
ATOM   197  N  N   D THR A 1 25  ? 30.997  4.104   -21.134 0.30 36.35  ? 25  THR A N   1 
ATOM   198  C  CA  A THR A 1 25  ? 29.637  3.690   -21.326 0.20 34.16  ? 25  THR A CA  1 
ATOM   199  C  CA  B THR A 1 25  ? 29.637  3.690   -21.326 0.20 34.16  ? 25  THR A CA  1 
ATOM   200  C  CA  C THR A 1 25  ? 29.627  3.583   -21.398 0.30 36.46  ? 25  THR A CA  1 
ATOM   201  C  CA  D THR A 1 25  ? 29.627  3.583   -21.398 0.30 36.46  ? 25  THR A CA  1 
ATOM   202  C  C   A THR A 1 25  ? 29.175  2.649   -20.301 0.20 32.91  ? 25  THR A C   1 
ATOM   203  C  C   B THR A 1 25  ? 29.175  2.649   -20.301 0.20 32.91  ? 25  THR A C   1 
ATOM   204  C  C   C THR A 1 25  ? 29.195  2.643   -20.266 0.30 33.78  ? 25  THR A C   1 
ATOM   205  C  C   D THR A 1 25  ? 29.195  2.643   -20.266 0.30 33.78  ? 25  THR A C   1 
ATOM   206  O  O   A THR A 1 25  ? 29.842  1.609   -20.162 0.20 31.49  ? 25  THR A O   1 
ATOM   207  O  O   B THR A 1 25  ? 29.842  1.609   -20.162 0.20 31.49  ? 25  THR A O   1 
ATOM   208  O  O   C THR A 1 25  ? 29.903  1.655   -20.016 0.30 31.89  ? 25  THR A O   1 
ATOM   209  O  O   D THR A 1 25  ? 29.903  1.655   -20.016 0.30 31.89  ? 25  THR A O   1 
ATOM   210  C  CB  A THR A 1 25  ? 29.551  3.143   -22.758 0.20 34.99  ? 25  THR A CB  1 
ATOM   211  C  CB  B THR A 1 25  ? 29.551  3.143   -22.758 0.20 34.99  ? 25  THR A CB  1 
ATOM   212  C  CB  C THR A 1 25  ? 29.539  2.832   -22.736 0.30 38.47  ? 25  THR A CB  1 
ATOM   213  C  CB  D THR A 1 25  ? 29.539  2.832   -22.736 0.30 38.47  ? 25  THR A CB  1 
ATOM   214  O  OG1 A THR A 1 25  ? 29.947  4.176   -23.659 0.20 36.50  ? 25  THR A OG1 1 
ATOM   215  O  OG1 B THR A 1 25  ? 29.947  4.176   -23.659 0.20 36.50  ? 25  THR A OG1 1 
ATOM   216  O  OG1 C THR A 1 25  ? 29.927  3.686   -23.813 0.30 39.84  ? 25  THR A OG1 1 
ATOM   217  O  OG1 D THR A 1 25  ? 29.927  3.686   -23.813 0.30 39.84  ? 25  THR A OG1 1 
ATOM   218  C  CG2 A THR A 1 25  ? 28.160  2.676   -23.130 0.20 35.61  ? 25  THR A CG2 1 
ATOM   219  C  CG2 B THR A 1 25  ? 28.160  2.676   -23.130 0.20 35.61  ? 25  THR A CG2 1 
ATOM   220  C  CG2 C THR A 1 25  ? 28.146  2.309   -23.014 0.30 40.08  ? 25  THR A CG2 1 
ATOM   221  C  CG2 D THR A 1 25  ? 28.146  2.309   -23.014 0.30 40.08  ? 25  THR A CG2 1 
ATOM   222  N  N   . THR A 1 26  ? 28.055  2.930   -19.631 1.00 34.91  ? 26  THR A N   1 
ATOM   223  C  CA  . THR A 1 26  ? 27.403  2.013   -18.665 1.00 32.52  ? 26  THR A CA  1 
ATOM   224  C  C   . THR A 1 26  ? 25.983  1.729   -19.171 1.00 29.65  ? 26  THR A C   1 
ATOM   225  O  O   . THR A 1 26  ? 25.232  2.664   -19.480 1.00 26.73  ? 26  THR A O   1 
ATOM   226  C  CB  . THR A 1 26  ? 27.416  2.602   -17.248 1.00 35.51  ? 26  THR A CB  1 
ATOM   227  O  OG1 . THR A 1 26  ? 28.776  2.652   -16.808 1.00 37.35  ? 26  THR A OG1 1 
ATOM   228  C  CG2 . THR A 1 26  ? 26.587  1.786   -16.276 1.00 35.58  ? 26  THR A CG2 1 
ATOM   229  N  N   A LEU A 1 27  ? 25.627  0.447   -19.242 0.20 28.43  ? 27  LEU A N   1 
ATOM   230  N  N   B LEU A 1 27  ? 25.627  0.447   -19.242 0.20 28.43  ? 27  LEU A N   1 
ATOM   231  N  N   C LEU A 1 27  ? 25.629  0.449   -19.291 0.30 29.33  ? 27  LEU A N   1 
ATOM   232  N  N   D LEU A 1 27  ? 25.629  0.449   -19.291 0.30 29.33  ? 27  LEU A N   1 
ATOM   233  C  CA  A LEU A 1 27  ? 24.236  -0.007  -19.506 0.20 27.07  ? 27  LEU A CA  1 
ATOM   234  C  CA  B LEU A 1 27  ? 24.236  -0.007  -19.506 0.20 27.07  ? 27  LEU A CA  1 
ATOM   235  C  CA  C LEU A 1 27  ? 24.225  0.012   -19.522 0.30 28.13  ? 27  LEU A CA  1 
ATOM   236  C  CA  D LEU A 1 27  ? 24.225  0.012   -19.522 0.30 28.13  ? 27  LEU A CA  1 
ATOM   237  C  C   A LEU A 1 27  ? 23.967  -1.292  -18.714 0.20 26.45  ? 27  LEU A C   1 
ATOM   238  C  C   B LEU A 1 27  ? 23.967  -1.292  -18.714 0.20 26.45  ? 27  LEU A C   1 
ATOM   239  C  C   C LEU A 1 27  ? 23.987  -1.330  -18.814 0.30 27.48  ? 27  LEU A C   1 
ATOM   240  C  C   D LEU A 1 27  ? 23.987  -1.330  -18.814 0.30 27.48  ? 27  LEU A C   1 
ATOM   241  O  O   A LEU A 1 27  ? 24.780  -1.625  -17.817 0.20 26.16  ? 27  LEU A O   1 
ATOM   242  O  O   B LEU A 1 27  ? 24.780  -1.625  -17.817 0.20 26.16  ? 27  LEU A O   1 
ATOM   243  O  O   C LEU A 1 27  ? 24.862  -1.749  -18.019 0.30 27.95  ? 27  LEU A O   1 
ATOM   244  O  O   D LEU A 1 27  ? 24.862  -1.749  -18.019 0.30 27.95  ? 27  LEU A O   1 
ATOM   245  C  CB  A LEU A 1 27  ? 24.026  -0.174  -21.016 0.20 26.62  ? 27  LEU A CB  1 
ATOM   246  C  CB  B LEU A 1 27  ? 24.026  -0.174  -21.016 0.20 26.62  ? 27  LEU A CB  1 
ATOM   247  C  CB  C LEU A 1 27  ? 23.923  -0.015  -21.027 0.30 27.99  ? 27  LEU A CB  1 
ATOM   248  C  CB  D LEU A 1 27  ? 23.923  -0.015  -21.027 0.30 27.99  ? 27  LEU A CB  1 
ATOM   249  C  CG  A LEU A 1 27  ? 25.129  -0.870  -21.814 0.20 26.68  ? 27  LEU A CG  1 
ATOM   250  C  CG  B LEU A 1 27  ? 25.129  -0.870  -21.814 0.20 26.68  ? 27  LEU A CG  1 
ATOM   251  C  CG  C LEU A 1 27  ? 24.835  -0.829  -21.949 0.30 28.56  ? 27  LEU A CG  1 
ATOM   252  C  CG  D LEU A 1 27  ? 24.835  -0.829  -21.949 0.30 28.56  ? 27  LEU A CG  1 
ATOM   253  C  CD1 A LEU A 1 27  ? 25.286  -2.333  -21.416 0.20 26.11  ? 27  LEU A CD1 1 
ATOM   254  C  CD1 B LEU A 1 27  ? 25.286  -2.333  -21.416 0.20 26.11  ? 27  LEU A CD1 1 
ATOM   255  C  CD1 C LEU A 1 27  ? 25.144  -2.218  -21.401 0.30 27.96  ? 27  LEU A CD1 1 
ATOM   256  C  CD1 D LEU A 1 27  ? 25.144  -2.218  -21.401 0.30 27.96  ? 27  LEU A CD1 1 
ATOM   257  C  CD2 A LEU A 1 27  ? 24.832  -0.764  -23.302 0.20 26.67  ? 27  LEU A CD2 1 
ATOM   258  C  CD2 B LEU A 1 27  ? 24.832  -0.764  -23.302 0.20 26.67  ? 27  LEU A CD2 1 
ATOM   259  C  CD2 C LEU A 1 27  ? 24.195  -0.949  -23.327 0.30 29.09  ? 27  LEU A CD2 1 
ATOM   260  C  CD2 D LEU A 1 27  ? 24.195  -0.949  -23.327 0.30 29.09  ? 27  LEU A CD2 1 
ATOM   261  N  N   A ASN A 1 28  ? 22.851  -1.960  -19.004 0.20 25.77  ? 28  ASN A N   1 
ATOM   262  N  N   B ASN A 1 28  ? 22.851  -1.960  -19.004 0.20 25.77  ? 28  ASN A N   1 
ATOM   263  N  N   C ASN A 1 28  ? 22.832  -1.956  -19.044 0.30 26.61  ? 28  ASN A N   1 
ATOM   264  N  N   D ASN A 1 28  ? 22.832  -1.956  -19.044 0.30 26.61  ? 28  ASN A N   1 
ATOM   265  C  CA  A ASN A 1 28  ? 22.364  -3.144  -18.252 0.20 25.25  ? 28  ASN A CA  1 
ATOM   266  C  CA  B ASN A 1 28  ? 22.364  -3.144  -18.252 0.20 25.25  ? 28  ASN A CA  1 
ATOM   267  C  CA  C ASN A 1 28  ? 22.364  -3.137  -18.271 0.30 25.82  ? 28  ASN A CA  1 
ATOM   268  C  CA  D ASN A 1 28  ? 22.364  -3.137  -18.271 0.30 25.82  ? 28  ASN A CA  1 
ATOM   269  C  C   A ASN A 1 28  ? 22.814  -4.420  -18.964 0.20 24.95  ? 28  ASN A C   1 
ATOM   270  C  C   B ASN A 1 28  ? 22.814  -4.420  -18.964 0.20 24.95  ? 28  ASN A C   1 
ATOM   271  C  C   C ASN A 1 28  ? 22.798  -4.426  -18.971 0.30 25.23  ? 28  ASN A C   1 
ATOM   272  C  C   D ASN A 1 28  ? 22.798  -4.426  -18.971 0.30 25.23  ? 28  ASN A C   1 
ATOM   273  O  O   A ASN A 1 28  ? 22.911  -4.413  -20.206 0.20 24.27  ? 28  ASN A O   1 
ATOM   274  O  O   B ASN A 1 28  ? 22.911  -4.413  -20.206 0.20 24.27  ? 28  ASN A O   1 
ATOM   275  O  O   C ASN A 1 28  ? 22.843  -4.441  -20.217 0.30 24.20  ? 28  ASN A O   1 
ATOM   276  O  O   D ASN A 1 28  ? 22.843  -4.441  -20.217 0.30 24.20  ? 28  ASN A O   1 
ATOM   277  C  CB  A ASN A 1 28  ? 20.845  -3.103  -18.086 0.20 25.05  ? 28  ASN A CB  1 
ATOM   278  C  CB  B ASN A 1 28  ? 20.845  -3.103  -18.086 0.20 25.05  ? 28  ASN A CB  1 
ATOM   279  C  CB  C ASN A 1 28  ? 20.848  -3.111  -18.078 0.30 25.68  ? 28  ASN A CB  1 
ATOM   280  C  CB  D ASN A 1 28  ? 20.848  -3.111  -18.078 0.30 25.68  ? 28  ASN A CB  1 
ATOM   281  C  CG  A ASN A 1 28  ? 20.382  -1.794  -17.491 0.20 25.07  ? 28  ASN A CG  1 
ATOM   282  C  CG  B ASN A 1 28  ? 20.382  -1.794  -17.491 0.20 25.07  ? 28  ASN A CG  1 
ATOM   283  C  CG  C ASN A 1 28  ? 20.376  -1.773  -17.560 0.30 25.83  ? 28  ASN A CG  1 
ATOM   284  C  CG  D ASN A 1 28  ? 20.376  -1.773  -17.560 0.30 25.83  ? 28  ASN A CG  1 
ATOM   285  O  OD1 A ASN A 1 28  ? 20.602  -1.542  -16.309 0.20 24.76  ? 28  ASN A OD1 1 
ATOM   286  O  OD1 B ASN A 1 28  ? 20.602  -1.542  -16.309 0.20 24.76  ? 28  ASN A OD1 1 
ATOM   287  O  OD1 C ASN A 1 28  ? 20.513  -1.490  -16.373 0.30 25.79  ? 28  ASN A OD1 1 
ATOM   288  O  OD1 D ASN A 1 28  ? 20.513  -1.490  -16.373 0.30 25.79  ? 28  ASN A OD1 1 
ATOM   289  N  ND2 A ASN A 1 28  ? 19.765  -0.950  -18.305 0.20 24.45  ? 28  ASN A ND2 1 
ATOM   290  N  ND2 B ASN A 1 28  ? 19.765  -0.950  -18.305 0.20 24.45  ? 28  ASN A ND2 1 
ATOM   291  N  ND2 C ASN A 1 28  ? 19.851  -0.940  -18.447 0.30 24.73  ? 28  ASN A ND2 1 
ATOM   292  N  ND2 D ASN A 1 28  ? 19.850  -0.940  -18.447 0.30 24.73  ? 28  ASN A ND2 1 
ATOM   293  N  N   . GLY A 1 29  ? 23.081  -5.466  -18.182 1.00 25.08  ? 29  GLY A N   1 
ATOM   294  C  CA  . GLY A 1 29  ? 23.355  -6.814  -18.684 1.00 24.10  ? 29  GLY A CA  1 
ATOM   295  C  C   . GLY A 1 29  ? 22.416  -7.782  -18.012 1.00 22.76  ? 29  GLY A C   1 
ATOM   296  O  O   . GLY A 1 29  ? 21.845  -7.445  -16.944 1.00 22.84  ? 29  GLY A O   1 
ATOM   297  N  N   . LEU A 1 30  ? 22.240  -8.930  -18.648 1.00 24.13  ? 30  LEU A N   1 
ATOM   298  C  CA  . LEU A 1 30  ? 21.383  -10.018 -18.160 1.00 25.55  ? 30  LEU A CA  1 
ATOM   299  C  C   . LEU A 1 30  ? 22.257  -11.201 -17.734 1.00 27.33  ? 30  LEU A C   1 
ATOM   300  O  O   . LEU A 1 30  ? 22.894  -11.825 -18.603 1.00 26.37  ? 30  LEU A O   1 
ATOM   301  C  CB  . LEU A 1 30  ? 20.438  -10.421 -19.281 1.00 25.68  ? 30  LEU A CB  1 
ATOM   302  C  CG  . LEU A 1 30  ? 19.450  -11.497 -18.864 1.00 24.96  ? 30  LEU A CG  1 
ATOM   303  C  CD1 . LEU A 1 30  ? 18.435  -10.919 -17.891 1.00 27.16  ? 30  LEU A CD1 1 
ATOM   304  C  CD2 . LEU A 1 30  ? 18.777  -12.084 -20.083 1.00 26.49  ? 30  LEU A CD2 1 
ATOM   305  N  N   . TRP A 1 31  ? 22.240  -11.518 -16.446 1.00 29.44  ? 31  TRP A N   1 
ATOM   306  C  CA  . TRP A 1 31  ? 23.142  -12.516 -15.805 1.00 28.19  ? 31  TRP A CA  1 
ATOM   307  C  C   . TRP A 1 31  ? 22.402  -13.837 -15.643 1.00 28.45  ? 31  TRP A C   1 
ATOM   308  O  O   . TRP A 1 31  ? 21.494  -13.916 -14.778 1.00 27.63  ? 31  TRP A O   1 
ATOM   309  C  CB  . TRP A 1 31  ? 23.645  -11.979 -14.478 1.00 31.58  ? 31  TRP A CB  1 
ATOM   310  C  CG  . TRP A 1 31  ? 24.669  -12.844 -13.827 1.00 33.64  ? 31  TRP A CG  1 
ATOM   311  C  CD1 . TRP A 1 31  ? 25.467  -13.797 -14.401 1.00 37.78  ? 31  TRP A CD1 1 
ATOM   312  C  CD2 . TRP A 1 31  ? 25.022  -12.802 -12.446 1.00 31.91  ? 31  TRP A CD2 1 
ATOM   313  N  NE1 . TRP A 1 31  ? 26.278  -14.373 -13.453 1.00 37.45  ? 31  TRP A NE1 1 
ATOM   314  C  CE2 . TRP A 1 31  ? 26.044  -13.761 -12.250 1.00 33.70  ? 31  TRP A CE2 1 
ATOM   315  C  CE3 . TRP A 1 31  ? 24.566  -12.051 -11.362 1.00 31.61  ? 31  TRP A CE3 1 
ATOM   316  C  CZ2 . TRP A 1 31  ? 26.607  -13.989 -10.998 1.00 35.21  ? 31  TRP A CZ2 1 
ATOM   317  C  CZ3 . TRP A 1 31  ? 25.137  -12.264 -10.131 1.00 31.50  ? 31  TRP A CZ3 1 
ATOM   318  C  CH2 . TRP A 1 31  ? 26.142  -13.221 -9.952  1.00 34.39  ? 31  TRP A CH2 1 
ATOM   319  N  N   . LEU A 1 32  ? 22.713  -14.790 -16.521 1.00 25.19  ? 32  LEU A N   1 
ATOM   320  C  CA  . LEU A 1 32  ? 22.106  -16.138 -16.528 1.00 28.93  ? 32  LEU A CA  1 
ATOM   321  C  C   . LEU A 1 32  ? 23.250  -17.155 -16.497 1.00 30.82  ? 32  LEU A C   1 
ATOM   322  O  O   . LEU A 1 32  ? 24.124  -17.072 -17.378 1.00 28.94  ? 32  LEU A O   1 
ATOM   323  C  CB  . LEU A 1 32  ? 21.261  -16.300 -17.791 1.00 29.98  ? 32  LEU A CB  1 
ATOM   324  C  CG  . LEU A 1 32  ? 20.083  -15.332 -17.972 1.00 29.86  ? 32  LEU A CG  1 
ATOM   325  C  CD1 . LEU A 1 32  ? 19.463  -15.535 -19.349 1.00 30.12  ? 32  LEU A CD1 1 
ATOM   326  C  CD2 . LEU A 1 32  ? 19.048  -15.508 -16.870 1.00 27.50  ? 32  LEU A CD2 1 
ATOM   327  N  N   . ASP A 1 33  ? 23.258  -18.045 -15.501 1.00 32.76  ? 33  ASP A N   1 
ATOM   328  C  CA  . ASP A 1 33  ? 24.379  -18.995 -15.266 1.00 30.52  ? 33  ASP A CA  1 
ATOM   329  C  C   . ASP A 1 33  ? 25.678  -18.180 -15.177 1.00 30.40  ? 33  ASP A C   1 
ATOM   330  O  O   . ASP A 1 33  ? 25.708  -17.125 -14.451 1.00 28.11  ? 33  ASP A O   1 
ATOM   331  C  CB  . ASP A 1 33  ? 24.345  -20.057 -16.358 1.00 30.61  ? 33  ASP A CB  1 
ATOM   332  C  CG  . ASP A 1 33  ? 23.007  -20.777 -16.428 1.00 33.64  ? 33  ASP A CG  1 
ATOM   333  O  OD1 . ASP A 1 33  ? 22.488  -21.154 -15.373 1.00 45.45  ? 33  ASP A OD1 1 
ATOM   334  O  OD2 . ASP A 1 33  ? 22.495  -20.978 -17.537 1.00 37.30  ? 33  ASP A OD2 1 
ATOM   335  N  N   . ASP A 1 34  ? 26.699  -18.554 -15.951 1.00 31.01  ? 34  ASP A N   1 
ATOM   336  C  CA  . ASP A 1 34  ? 28.010  -17.865 -15.893 1.00 31.22  ? 34  ASP A CA  1 
ATOM   337  C  C   . ASP A 1 34  ? 28.157  -16.876 -17.057 1.00 33.44  ? 34  ASP A C   1 
ATOM   338  O  O   . ASP A 1 34  ? 29.322  -16.484 -17.323 1.00 32.23  ? 34  ASP A O   1 
ATOM   339  C  CB  . ASP A 1 34  ? 29.151  -18.887 -15.849 1.00 35.49  ? 34  ASP A CB  1 
ATOM   340  C  CG  . ASP A 1 34  ? 29.176  -19.918 -16.965 1.00 33.31  ? 34  ASP A CG  1 
ATOM   341  O  OD1 . ASP A 1 34  ? 28.334  -19.854 -17.890 1.00 33.65  ? 34  ASP A OD1 1 
ATOM   342  O  OD2 . ASP A 1 34  ? 30.048  -20.796 -16.887 1.00 41.74  ? 34  ASP A OD2 1 
ATOM   343  N  N   . VAL A 1 35  ? 27.051  -16.450 -17.690 1.00 31.35  ? 35  VAL A N   1 
ATOM   344  C  CA  . VAL A 1 35  ? 27.082  -15.511 -18.853 1.00 28.97  ? 35  VAL A CA  1 
ATOM   345  C  C   . VAL A 1 35  ? 26.294  -14.230 -18.547 1.00 28.93  ? 35  VAL A C   1 
ATOM   346  O  O   . VAL A 1 35  ? 25.164  -14.300 -17.979 1.00 24.98  ? 35  VAL A O   1 
ATOM   347  C  CB  . VAL A 1 35  ? 26.572  -16.181 -20.136 1.00 29.55  ? 35  VAL A CB  1 
ATOM   348  C  CG1 . VAL A 1 35  ? 26.751  -15.276 -21.345 1.00 30.22  ? 35  VAL A CG1 1 
ATOM   349  C  CG2 . VAL A 1 35  ? 27.249  -17.523 -20.371 1.00 31.22  ? 35  VAL A CG2 1 
ATOM   350  N  N   . VAL A 1 36  ? 26.872  -13.089 -18.935 1.00 28.54  ? 36  VAL A N   1 
ATOM   351  C  CA  . VAL A 1 36  ? 26.191  -11.763 -18.910 1.00 26.42  ? 36  VAL A CA  1 
ATOM   352  C  C   . VAL A 1 36  ? 26.006  -11.330 -20.363 1.00 24.55  ? 36  VAL A C   1 
ATOM   353  O  O   . VAL A 1 36  ? 26.990  -11.258 -21.089 1.00 25.11  ? 36  VAL A O   1 
ATOM   354  C  CB  . VAL A 1 36  ? 26.949  -10.724 -18.065 1.00 28.02  ? 36  VAL A CB  1 
ATOM   355  C  CG1 . VAL A 1 36  ? 26.391  -9.326  -18.253 1.00 27.03  ? 36  VAL A CG1 1 
ATOM   356  C  CG2 . VAL A 1 36  ? 26.918  -11.101 -16.589 1.00 29.57  ? 36  VAL A CG2 1 
ATOM   357  N  N   . TYR A 1 37  ? 24.758  -11.144 -20.775 1.00 24.40  ? 37  TYR A N   1 
ATOM   358  C  CA  . TYR A 1 37  ? 24.367  -10.738 -22.136 1.00 23.15  ? 37  TYR A CA  1 
ATOM   359  C  C   . TYR A 1 37  ? 24.131  -9.240  -22.106 1.00 22.31  ? 37  TYR A C   1 
ATOM   360  O  O   . TYR A 1 37  ? 23.370  -8.784  -21.251 1.00 23.02  ? 37  TYR A O   1 
ATOM   361  C  CB  . TYR A 1 37  ? 23.119  -11.469 -22.604 1.00 23.66  ? 37  TYR A CB  1 
ATOM   362  C  CG  . TYR A 1 37  ? 23.192  -12.971 -22.575 1.00 26.40  ? 37  TYR A CG  1 
ATOM   363  C  CD1 . TYR A 1 37  ? 23.142  -13.657 -21.372 1.00 27.66  ? 37  TYR A CD1 1 
ATOM   364  C  CD2 . TYR A 1 37  ? 23.317  -13.712 -23.740 1.00 26.06  ? 37  TYR A CD2 1 
ATOM   365  C  CE1 . TYR A 1 37  ? 23.237  -15.039 -21.322 1.00 27.76  ? 37  TYR A CE1 1 
ATOM   366  C  CE2 . TYR A 1 37  ? 23.403  -15.099 -23.704 1.00 28.75  ? 37  TYR A CE2 1 
ATOM   367  C  CZ  . TYR A 1 37  ? 23.371  -15.762 -22.488 1.00 28.01  ? 37  TYR A CZ  1 
ATOM   368  O  OH  . TYR A 1 37  ? 23.424  -17.115 -22.401 1.00 28.61  ? 37  TYR A OH  1 
ATOM   369  N  N   . CYS A 1 38  ? 24.724  -8.494  -23.030 1.00 23.13  ? 38  CYS A N   1 
ATOM   370  C  CA  . CYS A 1 38  ? 24.377  -7.070  -23.196 1.00 23.49  ? 38  CYS A CA  1 
ATOM   371  C  C   . CYS A 1 38  ? 24.491  -6.680  -24.665 1.00 23.44  ? 38  CYS A C   1 
ATOM   372  O  O   . CYS A 1 38  ? 24.990  -7.456  -25.482 1.00 24.55  ? 38  CYS A O   1 
ATOM   373  C  CB  . CYS A 1 38  ? 25.236  -6.225  -22.270 1.00 26.21  ? 38  CYS A CB  1 
ATOM   374  S  SG  . CYS A 1 38  ? 26.984  -6.180  -22.758 1.00 28.54  ? 38  CYS A SG  1 
ATOM   375  N  N   A PRO A 1 39  ? 24.022  -5.470  -25.047 0.20 24.07  ? 39  PRO A N   1 
ATOM   376  N  N   B PRO A 1 39  ? 24.022  -5.470  -25.047 0.20 24.07  ? 39  PRO A N   1 
ATOM   377  N  N   C PRO A 1 39  ? 24.013  -5.476  -25.054 0.30 24.28  ? 39  PRO A N   1 
ATOM   378  N  N   D PRO A 1 39  ? 24.013  -5.476  -25.054 0.30 24.28  ? 39  PRO A N   1 
ATOM   379  C  CA  A PRO A 1 39  ? 24.180  -4.977  -26.414 0.20 23.59  ? 39  PRO A CA  1 
ATOM   380  C  CA  B PRO A 1 39  ? 24.180  -4.977  -26.414 0.20 23.59  ? 39  PRO A CA  1 
ATOM   381  C  CA  C PRO A 1 39  ? 24.181  -4.982  -26.420 0.30 23.59  ? 39  PRO A CA  1 
ATOM   382  C  CA  D PRO A 1 39  ? 24.181  -4.982  -26.420 0.30 23.59  ? 39  PRO A CA  1 
ATOM   383  C  C   A PRO A 1 39  ? 25.667  -4.779  -26.733 0.20 23.58  ? 39  PRO A C   1 
ATOM   384  C  C   B PRO A 1 39  ? 25.667  -4.779  -26.733 0.20 23.58  ? 39  PRO A C   1 
ATOM   385  C  C   C PRO A 1 39  ? 25.670  -4.785  -26.732 0.30 23.56  ? 39  PRO A C   1 
ATOM   386  C  C   D PRO A 1 39  ? 25.670  -4.785  -26.732 0.30 23.56  ? 39  PRO A C   1 
ATOM   387  O  O   A PRO A 1 39  ? 26.367  -4.222  -25.910 0.20 23.54  ? 39  PRO A O   1 
ATOM   388  O  O   B PRO A 1 39  ? 26.367  -4.222  -25.910 0.20 23.54  ? 39  PRO A O   1 
ATOM   389  O  O   C PRO A 1 39  ? 26.372  -4.241  -25.905 0.30 23.51  ? 39  PRO A O   1 
ATOM   390  O  O   D PRO A 1 39  ? 26.372  -4.241  -25.905 0.30 23.51  ? 39  PRO A O   1 
ATOM   391  C  CB  A PRO A 1 39  ? 23.418  -3.643  -26.418 0.20 23.80  ? 39  PRO A CB  1 
ATOM   392  C  CB  B PRO A 1 39  ? 23.418  -3.643  -26.418 0.20 23.80  ? 39  PRO A CB  1 
ATOM   393  C  CB  C PRO A 1 39  ? 23.413  -3.652  -26.425 0.30 23.91  ? 39  PRO A CB  1 
ATOM   394  C  CB  D PRO A 1 39  ? 23.413  -3.652  -26.425 0.30 23.91  ? 39  PRO A CB  1 
ATOM   395  C  CG  A PRO A 1 39  ? 22.512  -3.725  -25.210 0.20 24.16  ? 39  PRO A CG  1 
ATOM   396  C  CG  B PRO A 1 39  ? 22.512  -3.725  -25.210 0.20 24.16  ? 39  PRO A CG  1 
ATOM   397  C  CG  C PRO A 1 39  ? 22.468  -3.777  -25.257 0.30 24.40  ? 39  PRO A CG  1 
ATOM   398  C  CG  D PRO A 1 39  ? 22.468  -3.777  -25.257 0.30 24.40  ? 39  PRO A CG  1 
ATOM   399  C  CD  A PRO A 1 39  ? 23.307  -4.511  -24.192 0.20 23.73  ? 39  PRO A CD  1 
ATOM   400  C  CD  B PRO A 1 39  ? 23.307  -4.511  -24.192 0.20 23.73  ? 39  PRO A CD  1 
ATOM   401  C  CD  C PRO A 1 39  ? 23.268  -4.525  -24.213 0.30 23.80  ? 39  PRO A CD  1 
ATOM   402  C  CD  D PRO A 1 39  ? 23.268  -4.525  -24.213 0.30 23.80  ? 39  PRO A CD  1 
ATOM   403  N  N   . ARG A 1 40  ? 26.112  -5.246  -27.902 1.00 23.77  ? 40  ARG A N   1 
ATOM   404  C  CA  . ARG A 1 40  ? 27.534  -5.130  -28.295 1.00 23.54  ? 40  ARG A CA  1 
ATOM   405  C  C   . ARG A 1 40  ? 27.975  -3.664  -28.408 1.00 23.76  ? 40  ARG A C   1 
ATOM   406  O  O   . ARG A 1 40  ? 29.176  -3.415  -28.275 1.00 22.85  ? 40  ARG A O   1 
ATOM   407  C  CB  . ARG A 1 40  ? 27.836  -5.919  -29.564 1.00 22.78  ? 40  ARG A CB  1 
ATOM   408  C  CG  . ARG A 1 40  ? 27.290  -5.328  -30.844 1.00 22.45  ? 40  ARG A CG  1 
ATOM   409  C  CD  . ARG A 1 40  ? 27.561  -6.328  -31.956 1.00 21.46  ? 40  ARG A CD  1 
ATOM   410  N  NE  . ARG A 1 40  ? 26.940  -5.835  -33.161 1.00 21.26  ? 40  ARG A NE  1 
ATOM   411  C  CZ  . ARG A 1 40  ? 27.259  -6.221  -34.392 1.00 22.72  ? 40  ARG A CZ  1 
ATOM   412  N  NH1 . ARG A 1 40  ? 28.164  -7.174  -34.592 1.00 21.04  ? 40  ARG A NH1 1 
ATOM   413  N  NH2 . ARG A 1 40  ? 26.672  -5.633  -35.416 1.00 21.58  ? 40  ARG A NH2 1 
ATOM   414  N  N   A HIS A 1 41  ? 27.046  -2.726  -28.634 0.20 23.50  ? 41  HIS A N   1 
ATOM   415  N  N   B HIS A 1 41  ? 27.046  -2.726  -28.634 0.20 23.50  ? 41  HIS A N   1 
ATOM   416  N  N   C HIS A 1 41  ? 27.028  -2.739  -28.620 0.30 23.66  ? 41  HIS A N   1 
ATOM   417  N  N   D HIS A 1 41  ? 27.028  -2.739  -28.620 0.30 23.66  ? 41  HIS A N   1 
ATOM   418  C  CA  A HIS A 1 41  ? 27.363  -1.281  -28.803 0.20 23.50  ? 41  HIS A CA  1 
ATOM   419  C  CA  B HIS A 1 41  ? 27.363  -1.281  -28.803 0.20 23.50  ? 41  HIS A CA  1 
ATOM   420  C  CA  C HIS A 1 41  ? 27.288  -1.281  -28.778 0.30 23.74  ? 41  HIS A CA  1 
ATOM   421  C  CA  D HIS A 1 41  ? 27.288  -1.281  -28.778 0.30 23.74  ? 41  HIS A CA  1 
ATOM   422  C  C   A HIS A 1 41  ? 27.916  -0.690  -27.495 0.20 23.46  ? 41  HIS A C   1 
ATOM   423  C  C   B HIS A 1 41  ? 27.916  -0.690  -27.495 0.20 23.46  ? 41  HIS A C   1 
ATOM   424  C  C   C HIS A 1 41  ? 27.919  -0.702  -27.501 0.30 23.51  ? 41  HIS A C   1 
ATOM   425  C  C   D HIS A 1 41  ? 27.919  -0.702  -27.501 0.30 23.51  ? 41  HIS A C   1 
ATOM   426  O  O   A HIS A 1 41  ? 28.362  0.475   -27.532 0.20 22.23  ? 41  HIS A O   1 
ATOM   427  O  O   B HIS A 1 41  ? 28.362  0.475   -27.532 0.20 22.23  ? 41  HIS A O   1 
ATOM   428  O  O   C HIS A 1 41  ? 28.423  0.438   -27.570 0.30 21.73  ? 41  HIS A O   1 
ATOM   429  O  O   D HIS A 1 41  ? 28.423  0.438   -27.570 0.30 21.73  ? 41  HIS A O   1 
ATOM   430  C  CB  A HIS A 1 41  ? 26.174  -0.501  -29.401 0.20 23.64  ? 41  HIS A CB  1 
ATOM   431  C  CB  B HIS A 1 41  ? 26.174  -0.501  -29.401 0.20 23.64  ? 41  HIS A CB  1 
ATOM   432  C  CB  C HIS A 1 41  ? 26.025  -0.535  -29.264 0.30 24.22  ? 41  HIS A CB  1 
ATOM   433  C  CB  D HIS A 1 41  ? 26.025  -0.535  -29.264 0.30 24.22  ? 41  HIS A CB  1 
ATOM   434  C  CG  A HIS A 1 41  ? 25.023  -0.221  -28.488 0.20 23.65  ? 41  HIS A CG  1 
ATOM   435  C  CG  B HIS A 1 41  ? 25.023  -0.221  -28.488 0.20 23.65  ? 41  HIS A CG  1 
ATOM   436  C  CG  C HIS A 1 41  ? 24.974  -0.228  -28.243 0.30 24.35  ? 41  HIS A CG  1 
ATOM   437  C  CG  D HIS A 1 41  ? 24.974  -0.227  -28.243 0.30 24.35  ? 41  HIS A CG  1 
ATOM   438  N  ND1 A HIS A 1 41  ? 25.139  0.564   -27.357 0.20 23.87  ? 41  HIS A ND1 1 
ATOM   439  N  ND1 B HIS A 1 41  ? 25.139  0.564   -27.357 0.20 23.87  ? 41  HIS A ND1 1 
ATOM   440  N  ND1 C HIS A 1 41  ? 25.196  0.618   -27.173 0.30 24.94  ? 41  HIS A ND1 1 
ATOM   441  N  ND1 D HIS A 1 41  ? 25.196  0.618   -27.173 0.30 24.94  ? 41  HIS A ND1 1 
ATOM   442  C  CD2 A HIS A 1 41  ? 23.714  -0.543  -28.585 0.20 23.79  ? 41  HIS A CD2 1 
ATOM   443  C  CD2 B HIS A 1 41  ? 23.714  -0.543  -28.585 0.20 23.79  ? 41  HIS A CD2 1 
ATOM   444  C  CD2 C HIS A 1 41  ? 23.667  -0.566  -28.182 0.30 25.00  ? 41  HIS A CD2 1 
ATOM   445  C  CD2 D HIS A 1 41  ? 23.667  -0.566  -28.182 0.30 25.00  ? 41  HIS A CD2 1 
ATOM   446  C  CE1 A HIS A 1 41  ? 23.963  0.671   -26.772 0.20 23.22  ? 41  HIS A CE1 1 
ATOM   447  C  CE1 B HIS A 1 41  ? 23.963  0.671   -26.772 0.20 23.22  ? 41  HIS A CE1 1 
ATOM   448  C  CE1 C HIS A 1 41  ? 24.089  0.740   -26.470 0.30 24.12  ? 41  HIS A CE1 1 
ATOM   449  C  CE1 D HIS A 1 41  ? 24.089  0.740   -26.470 0.30 24.12  ? 41  HIS A CE1 1 
ATOM   450  N  NE2 A HIS A 1 41  ? 23.073  0.004   -27.506 0.20 23.91  ? 41  HIS A NE2 1 
ATOM   451  N  NE2 B HIS A 1 41  ? 23.073  0.004   -27.506 0.20 23.91  ? 41  HIS A NE2 1 
ATOM   452  N  NE2 C HIS A 1 41  ? 23.136  0.031   -27.069 0.30 24.57  ? 41  HIS A NE2 1 
ATOM   453  N  NE2 D HIS A 1 41  ? 23.136  0.031   -27.069 0.30 24.57  ? 41  HIS A NE2 1 
ATOM   454  N  N   . VAL A 1 42  ? 27.921  -1.461  -26.399 1.00 23.30  ? 42  VAL A N   1 
ATOM   455  C  CA  . VAL A 1 42  ? 28.621  -1.074  -25.131 1.00 25.66  ? 42  VAL A CA  1 
ATOM   456  C  C   . VAL A 1 42  ? 30.117  -0.840  -25.419 1.00 28.82  ? 42  VAL A C   1 
ATOM   457  O  O   . VAL A 1 42  ? 30.739  -0.063  -24.673 1.00 27.14  ? 42  VAL A O   1 
ATOM   458  C  CB  . VAL A 1 42  ? 28.483  -2.137  -24.015 1.00 27.58  ? 42  VAL A CB  1 
ATOM   459  C  CG1 . VAL A 1 42  ? 29.296  -3.397  -24.290 1.00 29.57  ? 42  VAL A CG1 1 
ATOM   460  C  CG2 . VAL A 1 42  ? 28.866  -1.567  -22.653 1.00 28.85  ? 42  VAL A CG2 1 
ATOM   461  N  N   . ILE A 1 43  ? 30.695  -1.493  -26.440 1.00 27.99  ? 43  ILE A N   1 
ATOM   462  C  CA  . ILE A 1 43  ? 32.149  -1.333  -26.754 1.00 32.38  ? 43  ILE A CA  1 
ATOM   463  C  C   . ILE A 1 43  ? 32.457  -0.175  -27.721 1.00 34.95  ? 43  ILE A C   1 
ATOM   464  O  O   . ILE A 1 43  ? 33.594  -0.058  -28.131 1.00 37.07  ? 43  ILE A O   1 
ATOM   465  C  CB  . ILE A 1 43  ? 32.731  -2.653  -27.276 1.00 29.34  ? 43  ILE A CB  1 
ATOM   466  C  CG1 . ILE A 1 43  ? 32.271  -2.976  -28.698 1.00 27.67  ? 43  ILE A CG1 1 
ATOM   467  C  CG2 . ILE A 1 43  ? 32.408  -3.757  -26.296 1.00 31.40  ? 43  ILE A CG2 1 
ATOM   468  C  CD1 . ILE A 1 43  ? 32.968  -4.175  -29.304 1.00 26.23  ? 43  ILE A CD1 1 
ATOM   469  N  N   A CYS A 1 44  ? 31.454  0.634   -28.076 0.20 35.55  ? 44  CYS A N   1 
ATOM   470  N  N   B CYS A 1 44  ? 31.454  0.634   -28.076 0.20 35.55  ? 44  CYS A N   1 
ATOM   471  N  N   C CYS A 1 44  ? 31.475  0.678   -28.031 0.30 37.04  ? 44  CYS A N   1 
ATOM   472  N  N   D CYS A 1 44  ? 31.475  0.678   -28.031 0.30 37.04  ? 44  CYS A N   1 
ATOM   473  C  CA  A CYS A 1 44  ? 31.588  1.779   -29.018 0.20 36.55  ? 44  CYS A CA  1 
ATOM   474  C  CA  B CYS A 1 44  ? 31.588  1.779   -29.018 0.20 36.55  ? 44  CYS A CA  1 
ATOM   475  C  CA  C CYS A 1 44  ? 31.627  1.828   -28.965 0.30 39.33  ? 44  CYS A CA  1 
ATOM   476  C  CA  D CYS A 1 44  ? 31.627  1.828   -28.965 0.30 39.33  ? 44  CYS A CA  1 
ATOM   477  C  C   A CYS A 1 44  ? 32.000  3.048   -28.265 0.20 37.47  ? 44  CYS A C   1 
ATOM   478  C  C   B CYS A 1 44  ? 32.000  3.048   -28.265 0.20 37.47  ? 44  CYS A C   1 
ATOM   479  C  C   C CYS A 1 44  ? 31.845  3.139   -28.201 0.30 41.49  ? 44  CYS A C   1 
ATOM   480  C  C   D CYS A 1 44  ? 31.845  3.139   -28.201 0.30 41.49  ? 44  CYS A C   1 
ATOM   481  O  O   A CYS A 1 44  ? 31.635  3.186   -27.083 0.20 36.60  ? 44  CYS A O   1 
ATOM   482  O  O   B CYS A 1 44  ? 31.635  3.186   -27.083 0.20 36.60  ? 44  CYS A O   1 
ATOM   483  O  O   C CYS A 1 44  ? 31.430  3.225   -27.030 0.30 40.64  ? 44  CYS A O   1 
ATOM   484  O  O   D CYS A 1 44  ? 31.430  3.225   -27.030 0.30 40.64  ? 44  CYS A O   1 
ATOM   485  C  CB  A CYS A 1 44  ? 30.290  2.057   -29.768 0.20 37.03  ? 44  CYS A CB  1 
ATOM   486  C  CB  B CYS A 1 44  ? 30.290  2.057   -29.768 0.20 37.03  ? 44  CYS A CB  1 
ATOM   487  C  CB  C CYS A 1 44  ? 30.408  1.983   -29.863 0.30 39.86  ? 44  CYS A CB  1 
ATOM   488  C  CB  D CYS A 1 44  ? 30.408  1.983   -29.863 0.30 39.86  ? 44  CYS A CB  1 
ATOM   489  S  SG  A CYS A 1 44  ? 29.860  0.776   -30.973 0.20 38.34  ? 44  CYS A SG  1 
ATOM   490  S  SG  B CYS A 1 44  ? 29.860  0.776   -30.973 0.20 38.34  ? 44  CYS A SG  1 
ATOM   491  S  SG  C CYS A 1 44  ? 30.179  0.585   -30.990 0.30 41.94  ? 44  CYS A SG  1 
ATOM   492  S  SG  D CYS A 1 44  ? 30.179  0.585   -30.990 0.30 41.94  ? 44  CYS A SG  1 
ATOM   493  N  N   A THR A 1 45  ? 32.744  3.921   -28.950 0.20 39.45  ? 45  THR A N   1 
ATOM   494  N  N   B THR A 1 45  ? 32.744  3.921   -28.950 0.20 39.45  ? 45  THR A N   1 
ATOM   495  N  N   C THR A 1 45  ? 32.471  4.109   -28.878 0.30 46.05  ? 45  THR A N   1 
ATOM   496  N  N   D THR A 1 45  ? 32.471  4.109   -28.878 0.30 46.05  ? 45  THR A N   1 
ATOM   497  C  CA  A THR A 1 45  ? 33.014  5.338   -28.583 0.20 41.61  ? 45  THR A CA  1 
ATOM   498  C  CA  B THR A 1 45  ? 33.014  5.338   -28.583 0.20 41.61  ? 45  THR A CA  1 
ATOM   499  C  CA  C THR A 1 45  ? 32.626  5.533   -28.474 0.30 49.24  ? 45  THR A CA  1 
ATOM   500  C  CA  D THR A 1 45  ? 32.626  5.533   -28.474 0.30 49.24  ? 45  THR A CA  1 
ATOM   501  C  C   A THR A 1 45  ? 32.198  6.237   -29.524 0.20 44.53  ? 45  THR A C   1 
ATOM   502  C  C   B THR A 1 45  ? 32.198  6.237   -29.524 0.20 44.53  ? 45  THR A C   1 
ATOM   503  C  C   C THR A 1 45  ? 31.908  6.419   -29.502 0.30 51.86  ? 45  THR A C   1 
ATOM   504  C  C   D THR A 1 45  ? 31.908  6.419   -29.502 0.30 51.86  ? 45  THR A C   1 
ATOM   505  O  O   A THR A 1 45  ? 31.493  5.682   -30.391 0.20 42.32  ? 45  THR A O   1 
ATOM   506  O  O   B THR A 1 45  ? 31.493  5.682   -30.391 0.20 42.32  ? 45  THR A O   1 
ATOM   507  O  O   C THR A 1 45  ? 31.255  5.857   -30.405 0.30 49.79  ? 45  THR A O   1 
ATOM   508  O  O   D THR A 1 45  ? 31.255  5.857   -30.405 0.30 49.79  ? 45  THR A O   1 
ATOM   509  C  CB  A THR A 1 45  ? 34.519  5.623   -28.654 0.20 40.20  ? 45  THR A CB  1 
ATOM   510  C  CB  B THR A 1 45  ? 34.519  5.623   -28.654 0.20 40.20  ? 45  THR A CB  1 
ATOM   511  C  CB  C THR A 1 45  ? 34.111  5.900   -28.378 0.30 48.75  ? 45  THR A CB  1 
ATOM   512  C  CB  D THR A 1 45  ? 34.111  5.900   -28.378 0.30 48.75  ? 45  THR A CB  1 
ATOM   513  O  OG1 A THR A 1 45  ? 34.894  5.696   -30.029 0.20 39.89  ? 45  THR A OG1 1 
ATOM   514  O  OG1 B THR A 1 45  ? 34.894  5.696   -30.029 0.20 39.89  ? 45  THR A OG1 1 
ATOM   515  O  OG1 C THR A 1 45  ? 34.642  5.905   -29.704 0.30 49.55  ? 45  THR A OG1 1 
ATOM   516  O  OG1 D THR A 1 45  ? 34.642  5.905   -29.704 0.30 49.55  ? 45  THR A OG1 1 
ATOM   517  C  CG2 A THR A 1 45  ? 35.360  4.563   -27.977 0.20 39.12  ? 45  THR A CG2 1 
ATOM   518  C  CG2 B THR A 1 45  ? 35.360  4.563   -27.977 0.20 39.12  ? 45  THR A CG2 1 
ATOM   519  C  CG2 C THR A 1 45  ? 34.918  4.933   -27.540 0.30 48.18  ? 45  THR A CG2 1 
ATOM   520  C  CG2 D THR A 1 45  ? 34.918  4.933   -27.540 0.30 48.18  ? 45  THR A CG2 1 
ATOM   521  N  N   A SER A 1 46  ? 32.297  7.563   -29.370 0.20 50.11  ? 46  SER A N   1 
ATOM   522  N  N   B SER A 1 46  ? 32.297  7.563   -29.370 0.20 50.11  ? 46  SER A N   1 
ATOM   523  N  N   C SER A 1 46  ? 32.042  7.745   -29.381 0.30 56.68  ? 46  SER A N   1 
ATOM   524  N  N   D SER A 1 46  ? 32.042  7.745   -29.381 0.30 56.68  ? 46  SER A N   1 
ATOM   525  C  CA  A SER A 1 46  ? 31.594  8.579   -30.205 0.20 54.16  ? 46  SER A CA  1 
ATOM   526  C  CA  B SER A 1 46  ? 31.594  8.579   -30.205 0.20 54.16  ? 46  SER A CA  1 
ATOM   527  C  CA  C SER A 1 46  ? 31.479  8.753   -30.322 0.30 59.27  ? 46  SER A CA  1 
ATOM   528  C  CA  D SER A 1 46  ? 31.479  8.753   -30.322 0.30 59.27  ? 46  SER A CA  1 
ATOM   529  C  C   A SER A 1 46  ? 31.877  8.328   -31.693 0.20 57.65  ? 46  SER A C   1 
ATOM   530  C  C   B SER A 1 46  ? 31.877  8.328   -31.693 0.20 57.65  ? 46  SER A C   1 
ATOM   531  C  C   C SER A 1 46  ? 31.864  8.402   -31.765 0.30 61.19  ? 46  SER A C   1 
ATOM   532  C  C   D SER A 1 46  ? 31.864  8.402   -31.765 0.30 61.19  ? 46  SER A C   1 
ATOM   533  O  O   A SER A 1 46  ? 30.906  8.194   -32.471 0.20 60.86  ? 46  SER A O   1 
ATOM   534  O  O   B SER A 1 46  ? 30.906  8.194   -32.471 0.20 60.86  ? 46  SER A O   1 
ATOM   535  O  O   C SER A 1 46  ? 30.939  8.263   -32.597 0.30 65.27  ? 46  SER A O   1 
ATOM   536  O  O   D SER A 1 46  ? 30.939  8.263   -32.597 0.30 65.27  ? 46  SER A O   1 
ATOM   537  C  CB  A SER A 1 46  ? 31.996  9.977   -29.808 0.20 54.26  ? 46  SER A CB  1 
ATOM   538  C  CB  B SER A 1 46  ? 31.996  9.977   -29.808 0.20 54.26  ? 46  SER A CB  1 
ATOM   539  C  CB  C SER A 1 46  ? 31.919  10.151  -29.962 0.30 59.29  ? 46  SER A CB  1 
ATOM   540  C  CB  D SER A 1 46  ? 31.919  10.151  -29.962 0.30 59.29  ? 46  SER A CB  1 
ATOM   541  O  OG  A SER A 1 46  ? 32.000  10.116  -28.395 0.20 54.19  ? 46  SER A OG  1 
ATOM   542  O  OG  B SER A 1 46  ? 32.000  10.116  -28.395 0.20 54.19  ? 46  SER A OG  1 
ATOM   543  O  OG  C SER A 1 46  ? 32.233  10.240  -28.579 0.30 59.30  ? 46  SER A OG  1 
ATOM   544  O  OG  D SER A 1 46  ? 32.233  10.240  -28.579 0.30 59.30  ? 46  SER A OG  1 
ATOM   545  N  N   . GLU A 1 47  ? 33.164  8.241   -32.051 1.00 60.08  ? 47  GLU A N   1 
ATOM   546  C  CA  . GLU A 1 47  ? 33.646  8.028   -33.449 1.00 62.22  ? 47  GLU A CA  1 
ATOM   547  C  C   . GLU A 1 47  ? 33.280  6.634   -33.971 1.00 53.05  ? 47  GLU A C   1 
ATOM   548  O  O   . GLU A 1 47  ? 33.412  6.414   -35.175 1.00 58.42  ? 47  GLU A O   1 
ATOM   549  C  CB  . GLU A 1 47  ? 35.165  8.193   -33.586 1.00 76.79  ? 47  GLU A CB  1 
ATOM   550  C  CG  . GLU A 1 47  ? 35.697  9.556   -33.185 1.00 81.24  ? 47  GLU A CG  1 
ATOM   551  C  CD  . GLU A 1 47  ? 36.151  9.603   -31.740 1.00 89.33  ? 47  GLU A CD  1 
ATOM   552  O  OE1 . GLU A 1 47  ? 37.067  8.828   -31.393 1.00 95.73  ? 47  GLU A OE1 1 
ATOM   553  O  OE2 . GLU A 1 47  ? 35.560  10.379  -30.959 1.00 92.28  ? 47  GLU A OE2 1 
ATOM   554  N  N   . ASP A 1 48  ? 32.851  5.710   -33.122 1.00 50.72  ? 48  ASP A N   1 
ATOM   555  C  CA  . ASP A 1 48  ? 32.454  4.349   -33.564 1.00 49.46  ? 48  ASP A CA  1 
ATOM   556  C  C   . ASP A 1 48  ? 30.942  4.255   -33.811 1.00 46.26  ? 48  ASP A C   1 
ATOM   557  O  O   . ASP A 1 48  ? 30.484  3.162   -34.080 1.00 61.50  ? 48  ASP A O   1 
ATOM   558  C  CB  . ASP A 1 48  ? 32.854  3.286   -32.530 1.00 47.89  ? 48  ASP A CB  1 
ATOM   559  C  CG  . ASP A 1 48  ? 34.349  3.187   -32.253 1.00 46.74  ? 48  ASP A CG  1 
ATOM   560  O  OD1 . ASP A 1 48  ? 35.103  2.867   -33.200 1.00 48.56  ? 48  ASP A OD1 1 
ATOM   561  O  OD2 . ASP A 1 48  ? 34.749  3.433   -31.096 1.00 41.35  ? 48  ASP A OD2 1 
ATOM   562  N  N   C MET A 1 49  ? 30.191  5.351   -33.706 0.30 41.57  ? 49  MET A N   1 
ATOM   563  N  N   D MET A 1 49  ? 30.191  5.351   -33.706 0.30 41.57  ? 49  MET A N   1 
ATOM   564  C  CA  C MET A 1 49  ? 28.706  5.287   -33.674 0.30 38.97  ? 49  MET A CA  1 
ATOM   565  C  CA  D MET A 1 49  ? 28.706  5.287   -33.674 0.30 38.97  ? 49  MET A CA  1 
ATOM   566  C  C   C MET A 1 49  ? 28.143  5.010   -35.073 0.30 33.96  ? 49  MET A C   1 
ATOM   567  C  C   D MET A 1 49  ? 28.143  5.010   -35.073 0.30 33.96  ? 49  MET A C   1 
ATOM   568  O  O   C MET A 1 49  ? 27.199  4.222   -35.162 0.30 28.09  ? 49  MET A O   1 
ATOM   569  O  O   D MET A 1 49  ? 27.199  4.222   -35.163 0.30 28.09  ? 49  MET A O   1 
ATOM   570  C  CB  C MET A 1 49  ? 28.108  6.587   -33.136 0.30 41.92  ? 49  MET A CB  1 
ATOM   571  C  CB  D MET A 1 49  ? 28.108  6.587   -33.136 0.30 41.92  ? 49  MET A CB  1 
ATOM   572  C  CG  C MET A 1 49  ? 27.822  6.542   -31.650 0.30 45.32  ? 49  MET A CG  1 
ATOM   573  C  CG  D MET A 1 49  ? 27.822  6.542   -31.650 0.30 45.32  ? 49  MET A CG  1 
ATOM   574  S  SD  C MET A 1 49  ? 27.362  8.176   -31.046 0.30 68.63  ? 49  MET A SD  1 
ATOM   575  S  SD  D MET A 1 49  ? 27.362  8.176   -31.046 0.30 68.63  ? 49  MET A SD  1 
ATOM   576  C  CE  C MET A 1 49  ? 27.951  8.077   -29.359 0.30 48.74  ? 49  MET A CE  1 
ATOM   577  C  CE  D MET A 1 49  ? 27.951  8.077   -29.359 0.30 48.74  ? 49  MET A CE  1 
ATOM   578  N  N   . LEU A 1 50  ? 28.692  5.646   -36.112 1.00 33.81  ? 50  LEU A N   1 
ATOM   579  C  CA  . LEU A 1 50  ? 28.130  5.609   -37.497 1.00 34.78  ? 50  LEU A CA  1 
ATOM   580  C  C   . LEU A 1 50  ? 28.455  4.266   -38.155 1.00 30.71  ? 50  LEU A C   1 
ATOM   581  O  O   . LEU A 1 50  ? 27.574  3.668   -38.772 1.00 31.41  ? 50  LEU A O   1 
ATOM   582  C  CB  . LEU A 1 50  ? 28.700  6.743   -38.355 1.00 38.87  ? 50  LEU A CB  1 
ATOM   583  C  CG  . LEU A 1 50  ? 28.227  8.174   -38.068 1.00 44.78  ? 50  LEU A CG  1 
ATOM   584  C  CD1 . LEU A 1 50  ? 26.715  8.275   -38.001 1.00 45.35  ? 50  LEU A CD1 1 
ATOM   585  C  CD2 . LEU A 1 50  ? 28.844  8.706   -36.791 1.00 48.71  ? 50  LEU A CD2 1 
ATOM   586  N  N   . ASN A 1 51  ? 29.702  3.835   -38.070 1.00 26.35  ? 51  ASN A N   1 
ATOM   587  C  CA  . ASN A 1 51  ? 30.180  2.656   -38.819 1.00 26.33  ? 51  ASN A CA  1 
ATOM   588  C  C   . ASN A 1 51  ? 31.049  1.798   -37.916 1.00 25.65  ? 51  ASN A C   1 
ATOM   589  O  O   . ASN A 1 51  ? 32.181  1.532   -38.248 1.00 26.31  ? 51  ASN A O   1 
ATOM   590  C  CB  . ASN A 1 51  ? 30.919  3.109   -40.079 1.00 26.36  ? 51  ASN A CB  1 
ATOM   591  C  CG  . ASN A 1 51  ? 29.999  3.809   -41.060 1.00 28.16  ? 51  ASN A CG  1 
ATOM   592  O  OD1 . ASN A 1 51  ? 29.256  3.145   -41.787 1.00 26.91  ? 51  ASN A OD1 1 
ATOM   593  N  ND2 . ASN A 1 51  ? 30.002  5.139   -41.062 1.00 25.94  ? 51  ASN A ND2 1 
ATOM   594  N  N   A PRO A 1 52  ? 30.559  1.344   -36.741 0.20 26.13  ? 52  PRO A N   1 
ATOM   595  N  N   B PRO A 1 52  ? 30.559  1.344   -36.741 0.20 26.13  ? 52  PRO A N   1 
ATOM   596  N  N   C PRO A 1 52  ? 30.539  1.305   -36.765 0.30 26.62  ? 52  PRO A N   1 
ATOM   597  N  N   D PRO A 1 52  ? 30.539  1.305   -36.765 0.30 26.62  ? 52  PRO A N   1 
ATOM   598  C  CA  A PRO A 1 52  ? 31.379  0.533   -35.846 0.20 25.66  ? 52  PRO A CA  1 
ATOM   599  C  CA  B PRO A 1 52  ? 31.379  0.533   -35.846 0.20 25.66  ? 52  PRO A CA  1 
ATOM   600  C  CA  C PRO A 1 52  ? 31.359  0.520   -35.849 0.30 26.06  ? 52  PRO A CA  1 
ATOM   601  C  CA  D PRO A 1 52  ? 31.359  0.520   -35.849 0.30 26.06  ? 52  PRO A CA  1 
ATOM   602  C  C   A PRO A 1 52  ? 31.837  -0.727  -36.592 0.20 25.35  ? 52  PRO A C   1 
ATOM   603  C  C   B PRO A 1 52  ? 31.837  -0.727  -36.592 0.20 25.35  ? 52  PRO A C   1 
ATOM   604  C  C   C PRO A 1 52  ? 31.833  -0.737  -36.588 0.30 25.65  ? 52  PRO A C   1 
ATOM   605  C  C   D PRO A 1 52  ? 31.833  -0.737  -36.588 0.30 25.65  ? 52  PRO A C   1 
ATOM   606  O  O   A PRO A 1 52  ? 31.030  -1.297  -37.308 0.20 24.85  ? 52  PRO A O   1 
ATOM   607  O  O   B PRO A 1 52  ? 31.030  -1.297  -37.308 0.20 24.85  ? 52  PRO A O   1 
ATOM   608  O  O   C PRO A 1 52  ? 31.026  -1.317  -37.296 0.30 25.10  ? 52  PRO A O   1 
ATOM   609  O  O   D PRO A 1 52  ? 31.026  -1.317  -37.296 0.30 25.10  ? 52  PRO A O   1 
ATOM   610  C  CB  A PRO A 1 52  ? 30.444  0.194   -34.674 0.20 26.04  ? 52  PRO A CB  1 
ATOM   611  C  CB  B PRO A 1 52  ? 30.444  0.194   -34.674 0.20 26.04  ? 52  PRO A CB  1 
ATOM   612  C  CB  C PRO A 1 52  ? 30.413  0.169   -34.690 0.30 26.64  ? 52  PRO A CB  1 
ATOM   613  C  CB  D PRO A 1 52  ? 30.413  0.169   -34.690 0.30 26.64  ? 52  PRO A CB  1 
ATOM   614  C  CG  A PRO A 1 52  ? 29.053  0.409   -35.235 0.20 25.99  ? 52  PRO A CG  1 
ATOM   615  C  CG  B PRO A 1 52  ? 29.053  0.409   -35.235 0.20 25.99  ? 52  PRO A CG  1 
ATOM   616  C  CG  C PRO A 1 52  ? 29.027  0.306   -35.290 0.30 26.58  ? 52  PRO A CG  1 
ATOM   617  C  CG  D PRO A 1 52  ? 29.027  0.306   -35.290 0.30 26.58  ? 52  PRO A CG  1 
ATOM   618  C  CD  A PRO A 1 52  ? 29.202  1.551   -36.217 0.20 26.30  ? 52  PRO A CD  1 
ATOM   619  C  CD  B PRO A 1 52  ? 29.202  1.551   -36.217 0.20 26.30  ? 52  PRO A CD  1 
ATOM   620  C  CD  C PRO A 1 52  ? 29.149  1.425   -36.302 0.30 27.03  ? 52  PRO A CD  1 
ATOM   621  C  CD  D PRO A 1 52  ? 29.149  1.425   -36.302 0.30 27.03  ? 52  PRO A CD  1 
ATOM   622  N  N   . ASN A 1 53  ? 33.114  -1.089  -36.446 1.00 24.36  ? 53  ASN A N   1 
ATOM   623  C  CA  . ASN A 1 53  ? 33.648  -2.382  -36.917 1.00 25.64  ? 53  ASN A CA  1 
ATOM   624  C  C   . ASN A 1 53  ? 33.764  -3.189  -35.631 1.00 26.34  ? 53  ASN A C   1 
ATOM   625  O  O   . ASN A 1 53  ? 34.753  -3.090  -34.967 1.00 27.28  ? 53  ASN A O   1 
ATOM   626  C  CB  . ASN A 1 53  ? 34.965  -2.222  -37.675 1.00 28.10  ? 53  ASN A CB  1 
ATOM   627  C  CG  . ASN A 1 53  ? 35.409  -3.528  -38.302 1.00 31.17  ? 53  ASN A CG  1 
ATOM   628  O  OD1 . ASN A 1 53  ? 35.265  -4.597  -37.703 1.00 29.98  ? 53  ASN A OD1 1 
ATOM   629  N  ND2 . ASN A 1 53  ? 35.957  -3.447  -39.507 1.00 34.67  ? 53  ASN A ND2 1 
ATOM   630  N  N   A TYR A 1 54  ? 32.725  -3.957  -35.297 0.20 26.55  ? 54  TYR A N   1 
ATOM   631  N  N   B TYR A 1 54  ? 32.725  -3.956  -35.296 0.20 26.55  ? 54  TYR A N   1 
ATOM   632  N  N   C TYR A 1 54  ? 32.730  -3.965  -35.305 0.30 26.60  ? 54  TYR A N   1 
ATOM   633  N  N   D TYR A 1 54  ? 32.726  -3.957  -35.298 0.30 26.60  ? 54  TYR A N   1 
ATOM   634  C  CA  A TYR A 1 54  ? 32.560  -4.610  -33.970 0.20 26.73  ? 54  TYR A CA  1 
ATOM   635  C  CA  B TYR A 1 54  ? 32.557  -4.612  -33.971 0.20 26.73  ? 54  TYR A CA  1 
ATOM   636  C  CA  C TYR A 1 54  ? 32.563  -4.611  -33.978 0.30 26.84  ? 54  TYR A CA  1 
ATOM   637  C  CA  D TYR A 1 54  ? 32.568  -4.612  -33.974 0.30 26.85  ? 54  TYR A CA  1 
ATOM   638  C  C   A TYR A 1 54  ? 33.634  -5.685  -33.758 0.20 26.58  ? 54  TYR A C   1 
ATOM   639  C  C   B TYR A 1 54  ? 33.632  -5.686  -33.758 0.20 26.58  ? 54  TYR A C   1 
ATOM   640  C  C   C TYR A 1 54  ? 33.647  -5.674  -33.763 0.30 26.42  ? 54  TYR A C   1 
ATOM   641  C  C   D TYR A 1 54  ? 33.651  -5.674  -33.763 0.30 26.42  ? 54  TYR A C   1 
ATOM   642  O  O   A TYR A 1 54  ? 34.115  -5.812  -32.618 0.20 26.95  ? 54  TYR A O   1 
ATOM   643  O  O   B TYR A 1 54  ? 34.113  -5.811  -32.617 0.20 26.95  ? 54  TYR A O   1 
ATOM   644  O  O   C TYR A 1 54  ? 34.142  -5.781  -32.629 0.30 27.08  ? 54  TYR A O   1 
ATOM   645  O  O   D TYR A 1 54  ? 34.149  -5.783  -32.630 0.30 27.08  ? 54  TYR A O   1 
ATOM   646  C  CB  A TYR A 1 54  ? 31.138  -5.157  -33.816 0.20 26.48  ? 54  TYR A CB  1 
ATOM   647  C  CB  B TYR A 1 54  ? 31.134  -5.161  -33.832 0.20 26.48  ? 54  TYR A CB  1 
ATOM   648  C  CB  C TYR A 1 54  ? 31.148  -5.181  -33.840 0.30 26.59  ? 54  TYR A CB  1 
ATOM   649  C  CB  D TYR A 1 54  ? 31.155  -5.180  -33.825 0.30 26.58  ? 54  TYR A CB  1 
ATOM   650  C  CG  A TYR A 1 54  ? 30.110  -4.096  -33.514 0.20 25.74  ? 54  TYR A CG  1 
ATOM   651  C  CG  B TYR A 1 54  ? 30.103  -4.105  -33.519 0.20 25.74  ? 54  TYR A CG  1 
ATOM   652  C  CG  C TYR A 1 54  ? 30.125  -4.127  -33.504 0.30 25.65  ? 54  TYR A CG  1 
ATOM   653  C  CG  D TYR A 1 54  ? 30.128  -4.125  -33.503 0.30 25.65  ? 54  TYR A CG  1 
ATOM   654  C  CD1 A TYR A 1 54  ? 30.091  -3.465  -32.282 0.20 25.96  ? 54  TYR A CD1 1 
ATOM   655  C  CD1 B TYR A 1 54  ? 30.100  -3.462  -32.293 0.20 25.96  ? 54  TYR A CD1 1 
ATOM   656  C  CD1 C TYR A 1 54  ? 30.136  -3.500  -32.272 0.30 26.04  ? 54  TYR A CD1 1 
ATOM   657  C  CD1 D TYR A 1 54  ? 30.136  -3.497  -32.271 0.30 26.04  ? 54  TYR A CD1 1 
ATOM   658  C  CD2 A TYR A 1 54  ? 29.176  -3.702  -34.459 0.20 25.41  ? 54  TYR A CD2 1 
ATOM   659  C  CD2 B TYR A 1 54  ? 29.168  -3.708  -34.461 0.20 25.41  ? 54  TYR A CD2 1 
ATOM   660  C  CD2 C TYR A 1 54  ? 29.175  -3.726  -34.429 0.30 25.22  ? 54  TYR A CD2 1 
ATOM   661  C  CD2 D TYR A 1 54  ? 29.179  -3.728  -34.429 0.30 25.22  ? 54  TYR A CD2 1 
ATOM   662  C  CE1 A TYR A 1 54  ? 29.163  -2.483  -31.988 0.20 25.39  ? 54  TYR A CE1 1 
ATOM   663  C  CE1 B TYR A 1 54  ? 29.170  -2.483  -31.994 0.20 25.39  ? 54  TYR A CE1 1 
ATOM   664  C  CE1 C TYR A 1 54  ? 29.217  -2.519  -31.954 0.30 25.20  ? 54  TYR A CE1 1 
ATOM   665  C  CE1 D TYR A 1 54  ? 29.216  -2.516  -31.956 0.30 25.20  ? 54  TYR A CE1 1 
ATOM   666  C  CE2 A TYR A 1 54  ? 28.239  -2.721  -34.181 0.20 25.43  ? 54  TYR A CE2 1 
ATOM   667  C  CE2 B TYR A 1 54  ? 28.233  -2.726  -34.180 0.20 25.43  ? 54  TYR A CE2 1 
ATOM   668  C  CE2 C TYR A 1 54  ? 28.247  -2.746  -34.128 0.30 25.29  ? 54  TYR A CE2 1 
ATOM   669  C  CE2 D TYR A 1 54  ? 28.249  -2.748  -34.131 0.30 25.28  ? 54  TYR A CE2 1 
ATOM   670  C  CZ  A TYR A 1 54  ? 28.232  -2.109  -32.940 0.20 25.50  ? 54  TYR A CZ  1 
ATOM   671  C  CZ  B TYR A 1 54  ? 28.234  -2.111  -32.940 0.20 25.50  ? 54  TYR A CZ  1 
ATOM   672  C  CZ  C TYR A 1 54  ? 28.268  -2.141  -32.884 0.30 25.32  ? 54  TYR A CZ  1 
ATOM   673  C  CZ  D TYR A 1 54  ? 28.268  -2.140  -32.888 0.30 25.32  ? 54  TYR A CZ  1 
ATOM   674  O  OH  A TYR A 1 54  ? 27.314  -1.142  -32.650 0.20 25.19  ? 54  TYR A OH  1 
ATOM   675  O  OH  B TYR A 1 54  ? 27.318  -1.143  -32.647 0.20 25.19  ? 54  TYR A OH  1 
ATOM   676  O  OH  C TYR A 1 54  ? 27.356  -1.176  -32.571 0.30 24.92  ? 54  TYR A OH  1 
ATOM   677  O  OH  D TYR A 1 54  ? 27.356  -1.176  -32.577 0.30 24.92  ? 54  TYR A OH  1 
ATOM   678  N  N   . GLU A 1 55  ? 33.986  -6.433  -34.808 1.00 26.79  ? 55  GLU A N   1 
ATOM   679  C  CA  . GLU A 1 55  ? 35.032  -7.494  -34.739 1.00 29.99  ? 55  GLU A CA  1 
ATOM   680  C  C   . GLU A 1 55  ? 36.385  -6.799  -34.462 1.00 28.72  ? 55  GLU A C   1 
ATOM   681  O  O   . GLU A 1 55  ? 37.142  -7.258  -33.601 1.00 28.52  ? 55  GLU A O   1 
ATOM   682  C  CB  . GLU A 1 55  ? 34.946  -8.372  -36.000 1.00 34.61  ? 55  GLU A CB  1 
ATOM   683  C  CG  . GLU A 1 55  ? 36.103  -9.364  -36.184 1.00 44.74  ? 55  GLU A CG  1 
ATOM   684  C  CD  . GLU A 1 55  ? 36.654  -9.625  -37.603 1.00 53.75  ? 55  GLU A CD  1 
ATOM   685  O  OE1 . GLU A 1 55  ? 36.281  -8.903  -38.583 1.00 54.08  ? 55  GLU A OE1 1 
ATOM   686  O  OE2 . GLU A 1 55  ? 37.495  -10.553 -37.739 1.00 55.53  ? 55  GLU A OE2 1 
ATOM   687  N  N   . ASP A 1 56  ? 36.642  -5.660  -35.092 1.00 28.64  ? 56  ASP A N   1 
ATOM   688  C  CA  . ASP A 1 56  ? 37.865  -4.852  -34.833 1.00 28.41  ? 56  ASP A CA  1 
ATOM   689  C  C   . ASP A 1 56  ? 37.846  -4.276  -33.402 1.00 28.80  ? 56  ASP A C   1 
ATOM   690  O  O   . ASP A 1 56  ? 38.912  -4.280  -32.756 1.00 26.07  ? 56  ASP A O   1 
ATOM   691  C  CB  . ASP A 1 56  ? 38.048  -3.762  -35.896 1.00 27.77  ? 56  ASP A CB  1 
ATOM   692  C  CG  . ASP A 1 56  ? 39.348  -2.984  -35.706 1.00 31.10  ? 56  ASP A CG  1 
ATOM   693  O  OD1 . ASP A 1 56  ? 40.448  -3.585  -35.885 1.00 29.40  ? 56  ASP A OD1 1 
ATOM   694  O  OD2 . ASP A 1 56  ? 39.246  -1.828  -35.283 1.00 32.04  ? 56  ASP A OD2 1 
ATOM   695  N  N   . LEU A 1 57  ? 36.724  -3.736  -32.914 1.00 26.23  ? 57  LEU A N   1 
ATOM   696  C  CA  . LEU A 1 57  ? 36.730  -3.060  -31.587 1.00 27.04  ? 57  LEU A CA  1 
ATOM   697  C  C   . LEU A 1 57  ? 36.854  -4.133  -30.506 1.00 26.98  ? 57  LEU A C   1 
ATOM   698  O  O   . LEU A 1 57  ? 37.505  -3.853  -29.480 1.00 29.81  ? 57  LEU A O   1 
ATOM   699  C  CB  . LEU A 1 57  ? 35.462  -2.230  -31.370 1.00 27.14  ? 57  LEU A CB  1 
ATOM   700  C  CG  . LEU A 1 57  ? 35.287  -1.053  -32.318 1.00 28.44  ? 57  LEU A CG  1 
ATOM   701  C  CD1 . LEU A 1 57  ? 33.872  -0.493  -32.240 1.00 30.56  ? 57  LEU A CD1 1 
ATOM   702  C  CD2 . LEU A 1 57  ? 36.320  0.043   -32.064 1.00 28.43  ? 57  LEU A CD2 1 
ATOM   703  N  N   . LEU A 1 58  ? 36.251  -5.303  -30.720 1.00 24.87  ? 58  LEU A N   1 
ATOM   704  C  CA  . LEU A 1 58  ? 36.202  -6.370  -29.681 1.00 27.47  ? 58  LEU A CA  1 
ATOM   705  C  C   . LEU A 1 58  ? 37.537  -7.129  -29.568 1.00 26.78  ? 58  LEU A C   1 
ATOM   706  O  O   . LEU A 1 58  ? 37.901  -7.485  -28.451 1.00 25.78  ? 58  LEU A O   1 
ATOM   707  C  CB  . LEU A 1 58  ? 35.069  -7.346  -29.982 1.00 27.93  ? 58  LEU A CB  1 
ATOM   708  C  CG  . LEU A 1 58  ? 34.844  -8.394  -28.893 1.00 30.19  ? 58  LEU A CG  1 
ATOM   709  C  CD1 . LEU A 1 58  ? 34.234  -7.766  -27.646 1.00 31.93  ? 58  LEU A CD1 1 
ATOM   710  C  CD2 . LEU A 1 58  ? 33.986  -9.541  -29.416 1.00 30.07  ? 58  LEU A CD2 1 
ATOM   711  N  N   . ILE A 1 59  ? 38.245  -7.386  -30.666 1.00 28.73  ? 59  ILE A N   1 
ATOM   712  C  CA  . ILE A 1 59  ? 39.585  -8.035  -30.575 1.00 32.72  ? 59  ILE A CA  1 
ATOM   713  C  C   . ILE A 1 59  ? 40.552  -7.166  -29.737 1.00 31.42  ? 59  ILE A C   1 
ATOM   714  O  O   . ILE A 1 59  ? 41.460  -7.744  -29.151 1.00 33.11  ? 59  ILE A O   1 
ATOM   715  C  CB  . ILE A 1 59  ? 40.138  -8.377  -31.963 1.00 33.57  ? 59  ILE A CB  1 
ATOM   716  C  CG1 . ILE A 1 59  ? 41.205  -9.465  -31.849 1.00 34.83  ? 59  ILE A CG1 1 
ATOM   717  C  CG2 . ILE A 1 59  ? 40.634  -7.136  -32.675 1.00 34.31  ? 59  ILE A CG2 1 
ATOM   718  C  CD1 . ILE A 1 59  ? 41.580  -10.041 -33.179 1.00 38.72  ? 59  ILE A CD1 1 
ATOM   719  N  N   . ARG A 1 60  ? 40.326  -5.856  -29.599 1.00 30.16  ? 60  ARG A N   1 
ATOM   720  C  CA  . ARG A 1 60  ? 41.257  -4.931  -28.891 1.00 29.00  ? 60  ARG A CA  1 
ATOM   721  C  C   . ARG A 1 60  ? 40.945  -4.873  -27.400 1.00 30.30  ? 60  ARG A C   1 
ATOM   722  O  O   . ARG A 1 60  ? 41.682  -4.171  -26.686 1.00 29.87  ? 60  ARG A O   1 
ATOM   723  C  CB  . ARG A 1 60  ? 41.175  -3.523  -29.468 1.00 28.55  ? 60  ARG A CB  1 
ATOM   724  C  CG  . ARG A 1 60  ? 41.486  -3.483  -30.957 1.00 28.25  ? 60  ARG A CG  1 
ATOM   725  C  CD  . ARG A 1 60  ? 41.154  -2.145  -31.574 1.00 27.57  ? 60  ARG A CD  1 
ATOM   726  N  NE  . ARG A 1 60  ? 41.435  -2.177  -32.998 1.00 28.04  ? 60  ARG A NE  1 
ATOM   727  C  CZ  . ARG A 1 60  ? 42.583  -1.841  -33.574 1.00 26.71  ? 60  ARG A CZ  1 
ATOM   728  N  NH1 . ARG A 1 60  ? 43.606  -1.423  -32.850 1.00 28.03  ? 60  ARG A NH1 1 
ATOM   729  N  NH2 . ARG A 1 60  ? 42.698  -1.887  -34.881 1.00 25.53  ? 60  ARG A NH2 1 
ATOM   730  N  N   . LYS A 1 61  ? 39.903  -5.572  -26.961 1.00 30.47  ? 61  LYS A N   1 
ATOM   731  C  CA  . LYS A 1 61  ? 39.455  -5.602  -25.544 1.00 34.15  ? 61  LYS A CA  1 
ATOM   732  C  C   . LYS A 1 61  ? 40.007  -6.852  -24.863 1.00 34.10  ? 61  LYS A C   1 
ATOM   733  O  O   . LYS A 1 61  ? 39.989  -7.936  -25.474 1.00 32.50  ? 61  LYS A O   1 
ATOM   734  C  CB  . LYS A 1 61  ? 37.926  -5.640  -25.438 1.00 35.64  ? 61  LYS A CB  1 
ATOM   735  C  CG  . LYS A 1 61  ? 37.204  -4.468  -26.086 1.00 35.55  ? 61  LYS A CG  1 
ATOM   736  C  CD  . LYS A 1 61  ? 37.538  -3.149  -25.452 1.00 35.70  ? 61  LYS A CD  1 
ATOM   737  C  CE  . LYS A 1 61  ? 37.294  -1.988  -26.386 1.00 37.10  ? 61  LYS A CE  1 
ATOM   738  N  NZ  . LYS A 1 61  ? 36.890  -0.808  -25.605 1.00 41.65  ? 61  LYS A NZ  1 
ATOM   739  N  N   . SER A 1 62  ? 40.421  -6.698  -23.617 1.00 37.65  ? 62  SER A N   1 
ATOM   740  C  CA  . SER A 1 62  ? 40.676  -7.824  -22.685 1.00 44.01  ? 62  SER A CA  1 
ATOM   741  C  C   . SER A 1 62  ? 39.493  -7.936  -21.717 1.00 43.36  ? 62  SER A C   1 
ATOM   742  O  O   . SER A 1 62  ? 38.726  -6.943  -21.533 1.00 41.17  ? 62  SER A O   1 
ATOM   743  C  CB  . SER A 1 62  ? 41.980  -7.650  -21.948 1.00 46.12  ? 62  SER A CB  1 
ATOM   744  O  OG  . SER A 1 62  ? 41.956  -6.468  -21.156 1.00 53.21  ? 62  SER A OG  1 
ATOM   745  N  N   . ASN A 1 63  ? 39.373  -9.106  -21.104 1.00 43.58  ? 63  ASN A N   1 
ATOM   746  C  CA  . ASN A 1 63  ? 38.387  -9.388  -20.039 1.00 40.54  ? 63  ASN A CA  1 
ATOM   747  C  C   . ASN A 1 63  ? 38.300  -8.194  -19.077 1.00 43.09  ? 63  ASN A C   1 
ATOM   748  O  O   . ASN A 1 63  ? 37.166  -7.796  -18.745 1.00 39.31  ? 63  ASN A O   1 
ATOM   749  C  CB  . ASN A 1 63  ? 38.727  -10.705 -19.358 1.00 39.10  ? 63  ASN A CB  1 
ATOM   750  C  CG  . ASN A 1 63  ? 38.526  -11.880 -20.284 1.00 38.79  ? 63  ASN A CG  1 
ATOM   751  O  OD1 . ASN A 1 63  ? 37.792  -11.787 -21.263 1.00 37.43  ? 63  ASN A OD1 1 
ATOM   752  N  ND2 . ASN A 1 63  ? 39.152  -12.998 -19.959 1.00 38.79  ? 63  ASN A ND2 1 
ATOM   753  N  N   . HIS A 1 64  ? 39.422  -7.593  -18.675 1.00 41.69  ? 64  HIS A N   1 
ATOM   754  C  CA  . HIS A 1 64  ? 39.439  -6.590  -17.575 1.00 45.69  ? 64  HIS A CA  1 
ATOM   755  C  C   . HIS A 1 64  ? 38.996  -5.209  -18.058 1.00 41.37  ? 64  HIS A C   1 
ATOM   756  O  O   . HIS A 1 64  ? 38.893  -4.338  -17.202 1.00 41.92  ? 64  HIS A O   1 
ATOM   757  C  CB  . HIS A 1 64  ? 40.795  -6.536  -16.845 1.00 52.01  ? 64  HIS A CB  1 
ATOM   758  C  CG  . HIS A 1 64  ? 41.966  -6.177  -17.701 1.00 57.69  ? 64  HIS A CG  1 
ATOM   759  N  ND1 . HIS A 1 64  ? 42.780  -7.143  -18.274 1.00 62.32  ? 64  HIS A ND1 1 
ATOM   760  C  CD2 . HIS A 1 64  ? 42.485  -4.980  -18.062 1.00 61.05  ? 64  HIS A CD2 1 
ATOM   761  C  CE1 . HIS A 1 64  ? 43.744  -6.559  -18.953 1.00 61.61  ? 64  HIS A CE1 1 
ATOM   762  N  NE2 . HIS A 1 64  ? 43.579  -5.226  -18.855 1.00 60.73  ? 64  HIS A NE2 1 
ATOM   763  N  N   . ASN A 1 65  ? 38.736  -5.008  -19.353 1.00 43.96  ? 65  ASN A N   1 
ATOM   764  C  CA  . ASN A 1 65  ? 38.107  -3.757  -19.878 1.00 42.84  ? 65  ASN A CA  1 
ATOM   765  C  C   . ASN A 1 65  ? 36.607  -3.693  -19.516 1.00 41.69  ? 65  ASN A C   1 
ATOM   766  O  O   . ASN A 1 65  ? 36.028  -2.591  -19.572 1.00 36.98  ? 65  ASN A O   1 
ATOM   767  C  CB  . ASN A 1 65  ? 38.277  -3.636  -21.395 1.00 42.78  ? 65  ASN A CB  1 
ATOM   768  C  CG  . ASN A 1 65  ? 39.716  -3.406  -21.803 1.00 40.52  ? 65  ASN A CG  1 
ATOM   769  O  OD1 . ASN A 1 65  ? 40.322  -4.241  -22.470 1.00 41.05  ? 65  ASN A OD1 1 
ATOM   770  N  ND2 . ASN A 1 65  ? 40.269  -2.290  -21.370 1.00 37.98  ? 65  ASN A ND2 1 
ATOM   771  N  N   . PHE A 1 66  ? 35.986  -4.838  -19.211 1.00 40.85  ? 66  PHE A N   1 
ATOM   772  C  CA  . PHE A 1 66  ? 34.562  -4.963  -18.806 1.00 39.10  ? 66  PHE A CA  1 
ATOM   773  C  C   . PHE A 1 66  ? 34.452  -5.014  -17.279 1.00 40.45  ? 66  PHE A C   1 
ATOM   774  O  O   . PHE A 1 66  ? 34.951  -5.988  -16.676 1.00 40.42  ? 66  PHE A O   1 
ATOM   775  C  CB  . PHE A 1 66  ? 33.953  -6.223  -19.410 1.00 37.73  ? 66  PHE A CB  1 
ATOM   776  C  CG  . PHE A 1 66  ? 34.028  -6.254  -20.911 1.00 38.65  ? 66  PHE A CG  1 
ATOM   777  C  CD1 . PHE A 1 66  ? 33.207  -5.448  -21.681 1.00 38.58  ? 66  PHE A CD1 1 
ATOM   778  C  CD2 . PHE A 1 66  ? 34.938  -7.079  -21.547 1.00 40.52  ? 66  PHE A CD2 1 
ATOM   779  C  CE1 . PHE A 1 66  ? 33.303  -5.467  -23.063 1.00 39.37  ? 66  PHE A CE1 1 
ATOM   780  C  CE2 . PHE A 1 66  ? 35.026  -7.107  -22.926 1.00 38.76  ? 66  PHE A CE2 1 
ATOM   781  C  CZ  . PHE A 1 66  ? 34.220  -6.290  -23.680 1.00 42.27  ? 66  PHE A CZ  1 
ATOM   782  N  N   . LEU A 1 67  ? 33.810  -4.000  -16.696 1.00 39.94  ? 67  LEU A N   1 
ATOM   783  C  CA  . LEU A 1 67  ? 33.422  -3.910  -15.260 1.00 44.25  ? 67  LEU A CA  1 
ATOM   784  C  C   . LEU A 1 67  ? 31.932  -4.289  -15.114 1.00 41.30  ? 67  LEU A C   1 
ATOM   785  O  O   . LEU A 1 67  ? 31.029  -3.514  -15.508 1.00 38.33  ? 67  LEU A O   1 
ATOM   786  C  CB  . LEU A 1 67  ? 33.781  -2.502  -14.758 1.00 54.17  ? 67  LEU A CB  1 
ATOM   787  C  CG  . LEU A 1 67  ? 35.236  -2.106  -15.058 1.00 69.21  ? 67  LEU A CG  1 
ATOM   788  C  CD1 . LEU A 1 67  ? 35.496  -0.620  -14.836 1.00 73.07  ? 67  LEU A CD1 1 
ATOM   789  C  CD2 . LEU A 1 67  ? 36.235  -2.958  -14.261 1.00 73.22  ? 67  LEU A CD2 1 
ATOM   790  N  N   . VAL A 1 68  ? 31.696  -5.518  -14.665 1.00 36.83  ? 68  VAL A N   1 
ATOM   791  C  CA  . VAL A 1 68  ? 30.356  -6.082  -14.351 1.00 35.57  ? 68  VAL A CA  1 
ATOM   792  C  C   . VAL A 1 68  ? 30.134  -6.005  -12.840 1.00 39.02  ? 68  VAL A C   1 
ATOM   793  O  O   . VAL A 1 68  ? 30.974  -6.521  -12.081 1.00 37.40  ? 68  VAL A O   1 
ATOM   794  C  CB  . VAL A 1 68  ? 30.224  -7.527  -14.834 1.00 32.38  ? 68  VAL A CB  1 
ATOM   795  C  CG1 . VAL A 1 68  ? 28.871  -8.093  -14.450 1.00 34.31  ? 68  VAL A CG1 1 
ATOM   796  C  CG2 . VAL A 1 68  ? 30.477  -7.645  -16.322 1.00 33.57  ? 68  VAL A CG2 1 
ATOM   797  N  N   . GLN A 1 69  ? 29.011  -5.414  -12.444 1.00 36.77  ? 69  GLN A N   1 
ATOM   798  C  CA  . GLN A 1 69  ? 28.641  -5.140  -11.038 1.00 37.30  ? 69  GLN A CA  1 
ATOM   799  C  C   . GLN A 1 69  ? 27.230  -5.690  -10.808 1.00 36.67  ? 69  GLN A C   1 
ATOM   800  O  O   . GLN A 1 69  ? 26.292  -5.230  -11.519 1.00 32.11  ? 69  GLN A O   1 
ATOM   801  C  CB  . GLN A 1 69  ? 28.720  -3.635  -10.829 1.00 41.66  ? 69  GLN A CB  1 
ATOM   802  C  CG  . GLN A 1 69  ? 29.168  -3.213  -9.443  1.00 50.02  ? 69  GLN A CG  1 
ATOM   803  C  CD  . GLN A 1 69  ? 29.237  -1.706  -9.347  1.00 55.99  ? 69  GLN A CD  1 
ATOM   804  O  OE1 . GLN A 1 69  ? 28.491  -1.081  -8.589  1.00 62.46  ? 69  GLN A OE1 1 
ATOM   805  N  NE2 . GLN A 1 69  ? 30.109  -1.108  -10.149 1.00 49.42  ? 69  GLN A NE2 1 
ATOM   806  N  N   . ALA A 1 70  ? 27.087  -6.675  -9.918  1.00 35.26  ? 70  ALA A N   1 
ATOM   807  C  CA  . ALA A 1 70  ? 25.791  -7.228  -9.458  1.00 39.29  ? 70  ALA A CA  1 
ATOM   808  C  C   . ALA A 1 70  ? 25.508  -6.684  -8.054  1.00 42.89  ? 70  ALA A C   1 
ATOM   809  O  O   . ALA A 1 70  ? 26.074  -7.213  -7.106  1.00 45.04  ? 70  ALA A O   1 
ATOM   810  C  CB  . ALA A 1 70  ? 25.824  -8.736  -9.503  1.00 39.23  ? 70  ALA A CB  1 
ATOM   811  N  N   . GLY A 1 71  ? 24.691  -5.633  -7.943  1.00 42.84  ? 71  GLY A N   1 
ATOM   812  C  CA  . GLY A 1 71  ? 24.569  -4.825  -6.719  1.00 46.24  ? 71  GLY A CA  1 
ATOM   813  C  C   . GLY A 1 71  ? 25.933  -4.298  -6.308  1.00 54.28  ? 71  GLY A C   1 
ATOM   814  O  O   . GLY A 1 71  ? 26.566  -3.594  -7.112  1.00 58.84  ? 71  GLY A O   1 
ATOM   815  N  N   . ASN A 1 72  ? 26.421  -4.695  -5.136  1.00 57.64  ? 72  ASN A N   1 
ATOM   816  C  CA  . ASN A 1 72  ? 27.762  -4.296  -4.635  1.00 61.83  ? 72  ASN A CA  1 
ATOM   817  C  C   . ASN A 1 72  ? 28.873  -5.185  -5.196  1.00 59.60  ? 72  ASN A C   1 
ATOM   818  O  O   . ASN A 1 72  ? 29.986  -4.681  -5.348  1.00 67.90  ? 72  ASN A O   1 
ATOM   819  C  CB  . ASN A 1 72  ? 27.824  -4.326  -3.112  1.00 64.31  ? 72  ASN A CB  1 
ATOM   820  C  CG  . ASN A 1 72  ? 27.867  -2.933  -2.538  1.00 66.70  ? 72  ASN A CG  1 
ATOM   821  O  OD1 . ASN A 1 72  ? 27.670  -1.956  -3.258  1.00 74.50  ? 72  ASN A OD1 1 
ATOM   822  N  ND2 . ASN A 1 72  ? 28.146  -2.840  -1.251  1.00 69.95  ? 72  ASN A ND2 1 
ATOM   823  N  N   . VAL A 1 73  ? 28.595  -6.459  -5.453  1.00 58.21  ? 73  VAL A N   1 
ATOM   824  C  CA  . VAL A 1 73  ? 29.617  -7.460  -5.878  1.00 54.95  ? 73  VAL A CA  1 
ATOM   825  C  C   . VAL A 1 73  ? 30.123  -7.073  -7.272  1.00 53.32  ? 73  VAL A C   1 
ATOM   826  O  O   . VAL A 1 73  ? 29.285  -6.821  -8.138  1.00 53.75  ? 73  VAL A O   1 
ATOM   827  C  CB  . VAL A 1 73  ? 29.039  -8.887  -5.874  1.00 53.46  ? 73  VAL A CB  1 
ATOM   828  C  CG1 . VAL A 1 73  ? 30.017  -9.910  -6.448  1.00 49.67  ? 73  VAL A CG1 1 
ATOM   829  C  CG2 . VAL A 1 73  ? 28.574  -9.287  -4.480  1.00 53.20  ? 73  VAL A CG2 1 
ATOM   830  N  N   . GLN A 1 74  ? 31.441  -6.992  -7.450  1.00 47.33  ? 74  GLN A N   1 
ATOM   831  C  CA  . GLN A 1 74  ? 32.099  -6.949  -8.777  1.00 43.00  ? 74  GLN A CA  1 
ATOM   832  C  C   . GLN A 1 74  ? 32.195  -8.396  -9.264  1.00 39.00  ? 74  GLN A C   1 
ATOM   833  O  O   . GLN A 1 74  ? 32.631  -9.234  -8.498  1.00 39.55  ? 74  GLN A O   1 
ATOM   834  C  CB  . GLN A 1 74  ? 33.465  -6.280  -8.645  1.00 48.46  ? 74  GLN A CB  1 
ATOM   835  C  CG  . GLN A 1 74  ? 33.882  -5.462  -9.855  1.00 53.18  ? 74  GLN A CG  1 
ATOM   836  C  CD  . GLN A 1 74  ? 35.328  -5.038  -9.763  1.00 59.83  ? 74  GLN A CD  1 
ATOM   837  O  OE1 . GLN A 1 74  ? 36.202  -5.587  -10.432 1.00 64.53  ? 74  GLN A OE1 1 
ATOM   838  N  NE2 . GLN A 1 74  ? 35.598  -4.075  -8.896  1.00 69.56  ? 74  GLN A NE2 1 
ATOM   839  N  N   . LEU A 1 75  ? 31.734  -8.691  -10.470 1.00 41.17  ? 75  LEU A N   1 
ATOM   840  C  CA  . LEU A 1 75  ? 31.893  -10.019 -11.118 1.00 41.69  ? 75  LEU A CA  1 
ATOM   841  C  C   . LEU A 1 75  ? 33.175  -10.002 -11.955 1.00 41.55  ? 75  LEU A C   1 
ATOM   842  O  O   . LEU A 1 75  ? 33.464  -8.974  -12.578 1.00 45.63  ? 75  LEU A O   1 
ATOM   843  C  CB  . LEU A 1 75  ? 30.686  -10.309 -12.014 1.00 44.09  ? 75  LEU A CB  1 
ATOM   844  C  CG  . LEU A 1 75  ? 29.364  -10.654 -11.335 1.00 42.76  ? 75  LEU A CG  1 
ATOM   845  C  CD1 . LEU A 1 75  ? 28.355  -11.092 -12.389 1.00 42.88  ? 75  LEU A CD1 1 
ATOM   846  C  CD2 . LEU A 1 75  ? 29.552  -11.750 -10.293 1.00 45.07  ? 75  LEU A CD2 1 
ATOM   847  N  N   . ARG A 1 76  ? 33.911  -11.102 -11.970 1.00 41.42  ? 76  ARG A N   1 
ATOM   848  C  CA  . ARG A 1 76  ? 35.156  -11.223 -12.764 1.00 45.52  ? 76  ARG A CA  1 
ATOM   849  C  C   . ARG A 1 76  ? 34.799  -11.795 -14.140 1.00 38.78  ? 76  ARG A C   1 
ATOM   850  O  O   . ARG A 1 76  ? 34.300  -12.950 -14.203 1.00 37.15  ? 76  ARG A O   1 
ATOM   851  C  CB  . ARG A 1 76  ? 36.164  -12.109 -12.027 1.00 53.14  ? 76  ARG A CB  1 
ATOM   852  C  CG  . ARG A 1 76  ? 37.595  -11.993 -12.532 1.00 59.52  ? 76  ARG A CG  1 
ATOM   853  C  CD  . ARG A 1 76  ? 38.458  -13.139 -12.026 1.00 63.32  ? 76  ARG A CD  1 
ATOM   854  N  NE  . ARG A 1 76  ? 39.821  -13.007 -12.521 1.00 68.68  ? 76  ARG A NE  1 
ATOM   855  C  CZ  . ARG A 1 76  ? 40.694  -14.005 -12.658 1.00 69.78  ? 76  ARG A CZ  1 
ATOM   856  N  NH1 . ARG A 1 76  ? 40.352  -15.242 -12.338 1.00 68.64  ? 76  ARG A NH1 1 
ATOM   857  N  NH2 . ARG A 1 76  ? 41.913  -13.757 -13.114 1.00 70.66  ? 76  ARG A NH2 1 
ATOM   858  N  N   . VAL A 1 77  ? 35.053  -11.024 -15.197 1.00 34.78  ? 77  VAL A N   1 
ATOM   859  C  CA  . VAL A 1 77  ? 34.965  -11.499 -16.608 1.00 35.34  ? 77  VAL A CA  1 
ATOM   860  C  C   . VAL A 1 77  ? 36.184  -12.387 -16.893 1.00 34.76  ? 77  VAL A C   1 
ATOM   861  O  O   . VAL A 1 77  ? 37.297  -11.915 -16.666 1.00 36.73  ? 77  VAL A O   1 
ATOM   862  C  CB  . VAL A 1 77  ? 34.880  -10.311 -17.594 1.00 35.97  ? 77  VAL A CB  1 
ATOM   863  C  CG1 . VAL A 1 77  ? 34.863  -10.783 -19.041 1.00 35.76  ? 77  VAL A CG1 1 
ATOM   864  C  CG2 . VAL A 1 77  ? 33.683  -9.415  -17.304 1.00 35.34  ? 77  VAL A CG2 1 
ATOM   865  N  N   . ILE A 1 78  ? 35.972  -13.608 -17.389 1.00 37.13  ? 78  ILE A N   1 
ATOM   866  C  CA  . ILE A 1 78  ? 37.046  -14.590 -17.731 1.00 38.83  ? 78  ILE A CA  1 
ATOM   867  C  C   . ILE A 1 78  ? 36.992  -14.932 -19.229 1.00 40.98  ? 78  ILE A C   1 
ATOM   868  O  O   . ILE A 1 78  ? 37.736  -15.805 -19.673 1.00 38.56  ? 78  ILE A O   1 
ATOM   869  C  CB  . ILE A 1 78  ? 36.915  -15.847 -16.852 1.00 39.66  ? 78  ILE A CB  1 
ATOM   870  C  CG1 . ILE A 1 78  ? 35.601  -16.597 -17.094 1.00 40.08  ? 78  ILE A CG1 1 
ATOM   871  C  CG2 . ILE A 1 78  ? 37.102  -15.479 -15.387 1.00 39.43  ? 78  ILE A CG2 1 
ATOM   872  C  CD1 . ILE A 1 78  ? 35.568  -17.991 -16.489 1.00 37.83  ? 78  ILE A CD1 1 
ATOM   873  N  N   . GLY A 1 79  ? 36.147  -14.252 -19.996 1.00 41.21  ? 79  GLY A N   1 
ATOM   874  C  CA  . GLY A 1 79  ? 35.857  -14.624 -21.390 1.00 39.63  ? 79  GLY A CA  1 
ATOM   875  C  C   . GLY A 1 79  ? 34.878  -13.637 -21.987 1.00 39.92  ? 79  GLY A C   1 
ATOM   876  O  O   . GLY A 1 79  ? 34.102  -13.057 -21.216 1.00 34.44  ? 79  GLY A O   1 
ATOM   877  N  N   . HIS A 1 80  ? 34.976  -13.385 -23.291 1.00 41.05  ? 80  HIS A N   1 
ATOM   878  C  CA  . HIS A 1 80  ? 34.001  -12.572 -24.058 1.00 40.44  ? 80  HIS A CA  1 
ATOM   879  C  C   . HIS A 1 80  ? 33.900  -13.148 -25.463 1.00 38.62  ? 80  HIS A C   1 
ATOM   880  O  O   . HIS A 1 80  ? 34.869  -13.735 -25.926 1.00 37.85  ? 80  HIS A O   1 
ATOM   881  C  CB  . HIS A 1 80  ? 34.353  -11.081 -24.045 1.00 40.96  ? 80  HIS A CB  1 
ATOM   882  C  CG  . HIS A 1 80  ? 35.635  -10.718 -24.718 1.00 44.80  ? 80  HIS A CG  1 
ATOM   883  N  ND1 . HIS A 1 80  ? 36.803  -10.506 -24.013 1.00 48.20  ? 80  HIS A ND1 1 
ATOM   884  C  CD2 . HIS A 1 80  ? 35.933  -10.472 -26.012 1.00 41.97  ? 80  HIS A CD2 1 
ATOM   885  C  CE1 . HIS A 1 80  ? 37.764  -10.156 -24.848 1.00 46.67  ? 80  HIS A CE1 1 
ATOM   886  N  NE2 . HIS A 1 80  ? 37.253  -10.114 -26.071 1.00 41.65  ? 80  HIS A NE2 1 
ATOM   887  N  N   . SER A 1 81  ? 32.711  -13.080 -26.041 1.00 35.40  ? 81  SER A N   1 
ATOM   888  C  CA  . SER A 1 81  ? 32.429  -13.442 -27.446 1.00 33.79  ? 81  SER A CA  1 
ATOM   889  C  C   . SER A 1 81  ? 31.225  -12.626 -27.893 1.00 32.64  ? 81  SER A C   1 
ATOM   890  O  O   . SER A 1 81  ? 30.528  -12.061 -27.043 1.00 34.95  ? 81  SER A O   1 
ATOM   891  C  CB  . SER A 1 81  ? 32.229  -14.910 -27.617 1.00 32.47  ? 81  SER A CB  1 
ATOM   892  O  OG  . SER A 1 81  ? 30.917  -15.306 -27.272 1.00 32.57  ? 81  SER A OG  1 
ATOM   893  N  N   . MET A 1 82  ? 31.021  -12.570 -29.189 1.00 32.91  ? 82  MET A N   1 
ATOM   894  C  CA  . MET A 1 82  ? 29.948  -11.791 -29.826 1.00 33.42  ? 82  MET A CA  1 
ATOM   895  C  C   . MET A 1 82  ? 29.072  -12.784 -30.577 1.00 30.45  ? 82  MET A C   1 
ATOM   896  O  O   . MET A 1 82  ? 29.620  -13.684 -31.223 1.00 30.39  ? 82  MET A O   1 
ATOM   897  C  CB  . MET A 1 82  ? 30.582  -10.775 -30.772 1.00 34.72  ? 82  MET A CB  1 
ATOM   898  C  CG  . MET A 1 82  ? 29.613  -9.948  -31.534 1.00 37.21  ? 82  MET A CG  1 
ATOM   899  S  SD  . MET A 1 82  ? 30.424  -8.447  -32.093 1.00 36.49  ? 82  MET A SD  1 
ATOM   900  C  CE  . MET A 1 82  ? 31.552  -9.098  -33.323 1.00 36.62  ? 82  MET A CE  1 
ATOM   901  N  N   . GLN A 1 83  ? 27.763  -12.705 -30.395 1.00 27.77  ? 83  GLN A N   1 
ATOM   902  C  CA  . GLN A 1 83  ? 26.812  -13.468 -31.221 1.00 27.99  ? 83  GLN A CA  1 
ATOM   903  C  C   . GLN A 1 83  ? 25.839  -12.446 -31.808 1.00 29.85  ? 83  GLN A C   1 
ATOM   904  O  O   . GLN A 1 83  ? 25.038  -11.852 -31.026 1.00 27.20  ? 83  GLN A O   1 
ATOM   905  C  CB  . GLN A 1 83  ? 26.120  -14.552 -30.393 1.00 28.98  ? 83  GLN A CB  1 
ATOM   906  C  CG  . GLN A 1 83  ? 25.090  -15.333 -31.181 1.00 27.80  ? 83  GLN A CG  1 
ATOM   907  C  CD  . GLN A 1 83  ? 24.364  -16.293 -30.277 1.00 29.62  ? 83  GLN A CD  1 
ATOM   908  O  OE1 . GLN A 1 83  ? 24.517  -16.257 -29.053 1.00 34.16  ? 83  GLN A OE1 1 
ATOM   909  N  NE2 . GLN A 1 83  ? 23.595  -17.188 -30.878 1.00 26.15  ? 83  GLN A NE2 1 
ATOM   910  N  N   . ASN A 1 84  ? 25.960  -12.210 -33.116 1.00 26.10  ? 84  ASN A N   1 
ATOM   911  C  CA  . ASN A 1 84  ? 25.127  -11.228 -33.835 1.00 24.33  ? 84  ASN A CA  1 
ATOM   912  C  C   . ASN A 1 84  ? 25.367  -9.912  -33.100 1.00 23.26  ? 84  ASN A C   1 
ATOM   913  O  O   . ASN A 1 84  ? 26.550  -9.588  -32.939 1.00 22.47  ? 84  ASN A O   1 
ATOM   914  C  CB  . ASN A 1 84  ? 23.694  -11.766 -33.927 1.00 24.62  ? 84  ASN A CB  1 
ATOM   915  C  CG  . ASN A 1 84  ? 23.679  -13.077 -34.679 1.00 26.04  ? 84  ASN A CG  1 
ATOM   916  O  OD1 . ASN A 1 84  ? 24.180  -13.140 -35.792 1.00 27.96  ? 84  ASN A OD1 1 
ATOM   917  N  ND2 . ASN A 1 84  ? 23.127  -14.125 -34.094 1.00 24.83  ? 84  ASN A ND2 1 
ATOM   918  N  N   . CYS A 1 85  ? 24.327  -9.199  -32.645 1.00 22.35  ? 85  CYS A N   1 
ATOM   919  C  CA  . CYS A 1 85  ? 24.456  -7.848  -32.022 1.00 22.81  ? 85  CYS A CA  1 
ATOM   920  C  C   . CYS A 1 85  ? 24.515  -7.891  -30.492 1.00 22.86  ? 85  CYS A C   1 
ATOM   921  O  O   . CYS A 1 85  ? 24.434  -6.831  -29.868 1.00 22.31  ? 85  CYS A O   1 
ATOM   922  C  CB  . CYS A 1 85  ? 23.299  -6.970  -32.464 1.00 23.48  ? 85  CYS A CB  1 
ATOM   923  S  SG  . CYS A 1 85  ? 23.329  -6.756  -34.248 1.00 24.28  ? 85  CYS A SG  1 
ATOM   924  N  N   . VAL A 1 86  ? 24.694  -9.071  -29.906 1.00 25.03  ? 86  VAL A N   1 
ATOM   925  C  CA  . VAL A 1 86  ? 24.756  -9.261  -28.434 1.00 25.76  ? 86  VAL A CA  1 
ATOM   926  C  C   . VAL A 1 86  ? 26.180  -9.685  -28.047 1.00 26.39  ? 86  VAL A C   1 
ATOM   927  O  O   . VAL A 1 86  ? 26.776  -10.553 -28.729 1.00 23.46  ? 86  VAL A O   1 
ATOM   928  C  CB  . VAL A 1 86  ? 23.665  -10.254 -27.991 1.00 28.60  ? 86  VAL A CB  1 
ATOM   929  C  CG1 . VAL A 1 86  ? 24.047  -11.091 -26.794 1.00 31.61  ? 86  VAL A CG1 1 
ATOM   930  C  CG2 . VAL A 1 86  ? 22.348  -9.518  -27.744 1.00 30.20  ? 86  VAL A CG2 1 
ATOM   931  N  N   . LEU A 1 87  ? 26.703  -9.057  -26.997 1.00 25.11  ? 87  LEU A N   1 
ATOM   932  C  CA  . LEU A 1 87  ? 27.990  -9.426  -26.362 1.00 26.90  ? 87  LEU A CA  1 
ATOM   933  C  C   . LEU A 1 87  ? 27.678  -10.375 -25.197 1.00 29.58  ? 87  LEU A C   1 
ATOM   934  O  O   . LEU A 1 87  ? 26.665  -10.131 -24.481 1.00 28.47  ? 87  LEU A O   1 
ATOM   935  C  CB  . LEU A 1 87  ? 28.641  -8.126  -25.903 1.00 28.41  ? 87  LEU A CB  1 
ATOM   936  C  CG  . LEU A 1 87  ? 29.997  -8.210  -25.221 1.00 32.80  ? 87  LEU A CG  1 
ATOM   937  C  CD1 . LEU A 1 87  ? 31.084  -8.697  -26.170 1.00 35.07  ? 87  LEU A CD1 1 
ATOM   938  C  CD2 . LEU A 1 87  ? 30.358  -6.845  -24.656 1.00 33.97  ? 87  LEU A CD2 1 
ATOM   939  N  N   . LYS A 1 88  ? 28.453  -11.450 -25.092 1.00 28.09  ? 88  LYS A N   1 
ATOM   940  C  CA  . LYS A 1 88  ? 28.384  -12.488 -24.033 1.00 31.92  ? 88  LYS A CA  1 
ATOM   941  C  C   . LYS A 1 88  ? 29.700  -12.476 -23.261 1.00 32.45  ? 88  LYS A C   1 
ATOM   942  O  O   . LYS A 1 88  ? 30.671  -13.014 -23.779 1.00 33.62  ? 88  LYS A O   1 
ATOM   943  C  CB  . LYS A 1 88  ? 28.121  -13.861 -24.647 1.00 32.24  ? 88  LYS A CB  1 
ATOM   944  C  CG  . LYS A 1 88  ? 26.805  -13.927 -25.401 1.00 33.26  ? 88  LYS A CG  1 
ATOM   945  C  CD  . LYS A 1 88  ? 26.288  -15.318 -25.649 1.00 31.60  ? 88  LYS A CD  1 
ATOM   946  C  CE  . LYS A 1 88  ? 26.827  -15.894 -26.929 1.00 33.55  ? 88  LYS A CE  1 
ATOM   947  N  NZ  . LYS A 1 88  ? 26.336  -17.270 -27.139 1.00 39.67  ? 88  LYS A NZ  1 
ATOM   948  N  N   . LEU A 1 89  ? 29.711  -11.807 -22.109 1.00 33.03  ? 89  LEU A N   1 
ATOM   949  C  CA  . LEU A 1 89  ? 30.810  -11.817 -21.118 1.00 31.85  ? 89  LEU A CA  1 
ATOM   950  C  C   . LEU A 1 89  ? 30.668  -13.075 -20.257 1.00 34.24  ? 89  LEU A C   1 
ATOM   951  O  O   . LEU A 1 89  ? 29.622  -13.233 -19.607 1.00 35.92  ? 89  LEU A O   1 
ATOM   952  C  CB  . LEU A 1 89  ? 30.719  -10.542 -20.285 1.00 29.58  ? 89  LEU A CB  1 
ATOM   953  C  CG  . LEU A 1 89  ? 30.597  -9.257  -21.085 1.00 26.37  ? 89  LEU A CG  1 
ATOM   954  C  CD1 . LEU A 1 89  ? 30.526  -8.068  -20.149 1.00 28.53  ? 89  LEU A CD1 1 
ATOM   955  C  CD2 . LEU A 1 89  ? 31.765  -9.101  -22.036 1.00 27.20  ? 89  LEU A CD2 1 
ATOM   956  N  N   . LYS A 1 90  ? 31.651  -13.977 -20.312 1.00 38.55  ? 90  LYS A N   1 
ATOM   957  C  CA  . LYS A 1 90  ? 31.749  -15.138 -19.385 1.00 39.17  ? 90  LYS A CA  1 
ATOM   958  C  C   . LYS A 1 90  ? 32.283  -14.599 -18.063 1.00 36.93  ? 90  LYS A C   1 
ATOM   959  O  O   . LYS A 1 90  ? 33.217  -13.777 -18.113 1.00 34.84  ? 90  LYS A O   1 
ATOM   960  C  CB  . LYS A 1 90  ? 32.645  -16.243 -19.949 1.00 43.65  ? 90  LYS A CB  1 
ATOM   961  C  CG  . LYS A 1 90  ? 32.282  -17.644 -19.486 1.00 47.71  ? 90  LYS A CG  1 
ATOM   962  C  CD  . LYS A 1 90  ? 33.013  -18.733 -20.243 1.00 53.80  ? 90  LYS A CD  1 
ATOM   963  C  CE  . LYS A 1 90  ? 32.581  -20.116 -19.801 1.00 60.89  ? 90  LYS A CE  1 
ATOM   964  N  NZ  . LYS A 1 90  ? 33.736  -21.043 -19.707 1.00 66.38  ? 90  LYS A NZ  1 
ATOM   965  N  N   . VAL A 1 91  ? 31.676  -15.002 -16.940 1.00 35.51  ? 91  VAL A N   1 
ATOM   966  C  CA  . VAL A 1 91  ? 32.099  -14.586 -15.570 1.00 37.72  ? 91  VAL A CA  1 
ATOM   967  C  C   . VAL A 1 91  ? 32.409  -15.847 -14.763 1.00 36.73  ? 91  VAL A C   1 
ATOM   968  O  O   . VAL A 1 91  ? 31.963  -16.934 -15.183 1.00 36.65  ? 91  VAL A O   1 
ATOM   969  C  CB  . VAL A 1 91  ? 31.027  -13.710 -14.893 1.00 40.64  ? 91  VAL A CB  1 
ATOM   970  C  CG1 . VAL A 1 91  ? 30.853  -12.387 -15.624 1.00 42.95  ? 91  VAL A CG1 1 
ATOM   971  C  CG2 . VAL A 1 91  ? 29.684  -14.425 -14.778 1.00 40.25  ? 91  VAL A CG2 1 
ATOM   972  N  N   . ASP A 1 92  ? 33.157  -15.707 -13.665 1.00 42.29  ? 92  ASP A N   1 
ATOM   973  C  CA  . ASP A 1 92  ? 33.650  -16.859 -12.848 1.00 47.76  ? 92  ASP A CA  1 
ATOM   974  C  C   . ASP A 1 92  ? 32.555  -17.389 -11.902 1.00 47.05  ? 92  ASP A C   1 
ATOM   975  O  O   . ASP A 1 92  ? 32.736  -18.506 -11.396 1.00 48.15  ? 92  ASP A O   1 
ATOM   976  C  CB  . ASP A 1 92  ? 34.949  -16.522 -12.105 1.00 48.96  ? 92  ASP A CB  1 
ATOM   977  C  CG  . ASP A 1 92  ? 34.890  -15.326 -11.176 1.00 49.36  ? 92  ASP A CG  1 
ATOM   978  O  OD1 . ASP A 1 92  ? 33.799  -14.744 -11.004 1.00 55.08  ? 92  ASP A OD1 1 
ATOM   979  O  OD2 . ASP A 1 92  ? 35.946  -14.980 -10.636 1.00 61.16  ? 92  ASP A OD2 1 
ATOM   980  N  N   . THR A 1 93  ? 31.454  -16.648 -11.696 1.00 40.95  ? 93  THR A N   1 
ATOM   981  C  CA  . THR A 1 93  ? 30.340  -17.009 -10.781 1.00 36.38  ? 93  THR A CA  1 
ATOM   982  C  C   . THR A 1 93  ? 29.069  -17.240 -11.599 1.00 36.60  ? 93  THR A C   1 
ATOM   983  O  O   . THR A 1 93  ? 28.716  -16.342 -12.384 1.00 33.17  ? 93  THR A O   1 
ATOM   984  C  CB  . THR A 1 93  ? 30.070  -15.886 -9.768  1.00 39.39  ? 93  THR A CB  1 
ATOM   985  O  OG1 . THR A 1 93  ? 31.295  -15.368 -9.247  1.00 42.55  ? 93  THR A OG1 1 
ATOM   986  C  CG2 . THR A 1 93  ? 29.218  -16.352 -8.611  1.00 37.48  ? 93  THR A CG2 1 
ATOM   987  N  N   . ALA A 1 94  ? 28.406  -18.382 -11.430 1.00 34.83  ? 94  ALA A N   1 
ATOM   988  C  CA  . ALA A 1 94  ? 27.043  -18.629 -11.947 1.00 35.38  ? 94  ALA A CA  1 
ATOM   989  C  C   . ALA A 1 94  ? 26.055  -17.870 -11.063 1.00 35.64  ? 94  ALA A C   1 
ATOM   990  O  O   . ALA A 1 94  ? 26.209  -17.922 -9.823  1.00 36.45  ? 94  ALA A O   1 
ATOM   991  C  CB  . ALA A 1 94  ? 26.714  -20.097 -11.980 1.00 39.18  ? 94  ALA A CB  1 
ATOM   992  N  N   . ASN A 1 95  ? 25.106  -17.161 -11.667 1.00 32.54  ? 95  ASN A N   1 
ATOM   993  C  CA  . ASN A 1 95  ? 24.077  -16.402 -10.911 1.00 33.71  ? 95  ASN A CA  1 
ATOM   994  C  C   . ASN A 1 95  ? 23.284  -17.418 -10.092 1.00 29.79  ? 95  ASN A C   1 
ATOM   995  O  O   . ASN A 1 95  ? 22.626  -18.271 -10.678 1.00 28.65  ? 95  ASN A O   1 
ATOM   996  C  CB  . ASN A 1 95  ? 23.181  -15.621 -11.869 1.00 33.89  ? 95  ASN A CB  1 
ATOM   997  C  CG  . ASN A 1 95  ? 22.134  -14.777 -11.179 1.00 35.22  ? 95  ASN A CG  1 
ATOM   998  O  OD1 . ASN A 1 95  ? 22.044  -14.778 -9.952  1.00 30.78  ? 95  ASN A OD1 1 
ATOM   999  N  ND2 . ASN A 1 95  ? 21.336  -14.066 -11.971 1.00 34.79  ? 95  ASN A ND2 1 
ATOM   1000 N  N   . PRO A 1 96  ? 23.308  -17.371 -8.742  1.00 31.00  ? 96  PRO A N   1 
ATOM   1001 C  CA  . PRO A 1 96  ? 22.533  -18.324 -7.942  1.00 33.86  ? 96  PRO A CA  1 
ATOM   1002 C  C   . PRO A 1 96  ? 21.019  -18.076 -8.088  1.00 34.35  ? 96  PRO A C   1 
ATOM   1003 O  O   . PRO A 1 96  ? 20.261  -18.967 -7.859  1.00 31.45  ? 96  PRO A O   1 
ATOM   1004 C  CB  . PRO A 1 96  ? 23.064  -18.128 -6.514  1.00 33.53  ? 96  PRO A CB  1 
ATOM   1005 C  CG  . PRO A 1 96  ? 23.642  -16.727 -6.490  1.00 32.94  ? 96  PRO A CG  1 
ATOM   1006 C  CD  . PRO A 1 96  ? 24.059  -16.414 -7.912  1.00 32.67  ? 96  PRO A CD  1 
ATOM   1007 N  N   . LYS A 1 97  ? 20.617  -16.900 -8.574  1.00 34.42  ? 97  LYS A N   1 
ATOM   1008 C  CA  . LYS A 1 97  ? 19.186  -16.535 -8.773  1.00 36.19  ? 97  LYS A CA  1 
ATOM   1009 C  C   . LYS A 1 97  ? 18.710  -16.892 -10.189 1.00 34.94  ? 97  LYS A C   1 
ATOM   1010 O  O   . LYS A 1 97  ? 17.566  -16.517 -10.540 1.00 31.79  ? 97  LYS A O   1 
ATOM   1011 C  CB  . LYS A 1 97  ? 18.994  -15.040 -8.500  1.00 39.34  ? 97  LYS A CB  1 
ATOM   1012 C  CG  . LYS A 1 97  ? 19.139  -14.643 -7.036  1.00 42.30  ? 97  LYS A CG  1 
ATOM   1013 C  CD  . LYS A 1 97  ? 19.065  -13.150 -6.829  1.00 47.80  ? 97  LYS A CD  1 
ATOM   1014 C  CE  . LYS A 1 97  ? 19.064  -12.754 -5.370  1.00 54.76  ? 97  LYS A CE  1 
ATOM   1015 N  NZ  . LYS A 1 97  ? 18.714  -11.326 -5.203  1.00 59.89  ? 97  LYS A NZ  1 
ATOM   1016 N  N   . THR A 1 98  ? 19.529  -17.570 -10.997 1.00 30.53  ? 98  THR A N   1 
ATOM   1017 C  CA  . THR A 1 98  ? 19.128  -17.960 -12.373 1.00 29.41  ? 98  THR A CA  1 
ATOM   1018 C  C   . THR A 1 98  ? 17.804  -18.700 -12.279 1.00 27.55  ? 98  THR A C   1 
ATOM   1019 O  O   . THR A 1 98  ? 17.735  -19.741 -11.645 1.00 33.16  ? 98  THR A O   1 
ATOM   1020 C  CB  . THR A 1 98  ? 20.206  -18.787 -13.090 1.00 27.66  ? 98  THR A CB  1 
ATOM   1021 O  OG1 . THR A 1 98  ? 21.398  -18.004 -13.125 1.00 29.59  ? 98  THR A OG1 1 
ATOM   1022 C  CG2 . THR A 1 98  ? 19.826  -19.168 -14.502 1.00 28.69  ? 98  THR A CG2 1 
ATOM   1023 N  N   . PRO A 1 99  ? 16.720  -18.221 -12.919 1.00 26.72  ? 99  PRO A N   1 
ATOM   1024 C  CA  . PRO A 1 99  ? 15.474  -18.973 -12.948 1.00 27.48  ? 99  PRO A CA  1 
ATOM   1025 C  C   . PRO A 1 99  ? 15.556  -20.024 -14.064 1.00 30.10  ? 99  PRO A C   1 
ATOM   1026 O  O   . PRO A 1 99  ? 16.490  -19.954 -14.853 1.00 30.49  ? 99  PRO A O   1 
ATOM   1027 C  CB  . PRO A 1 99  ? 14.442  -17.909 -13.334 1.00 28.40  ? 99  PRO A CB  1 
ATOM   1028 C  CG  . PRO A 1 99  ? 15.233  -16.965 -14.248 1.00 27.92  ? 99  PRO A CG  1 
ATOM   1029 C  CD  . PRO A 1 99  ? 16.642  -16.971 -13.700 1.00 26.21  ? 99  PRO A CD  1 
ATOM   1030 N  N   . LYS A 1 100 ? 14.571  -20.915 -14.151 1.00 28.56  ? 100 LYS A N   1 
ATOM   1031 C  CA  . LYS A 1 100 ? 14.305  -21.691 -15.379 1.00 31.17  ? 100 LYS A CA  1 
ATOM   1032 C  C   . LYS A 1 100 ? 14.070  -20.668 -16.483 1.00 30.47  ? 100 LYS A C   1 
ATOM   1033 O  O   . LYS A 1 100 ? 13.297  -19.710 -16.259 1.00 26.20  ? 100 LYS A O   1 
ATOM   1034 C  CB  . LYS A 1 100 ? 13.080  -22.587 -15.228 1.00 37.60  ? 100 LYS A CB  1 
ATOM   1035 C  CG  . LYS A 1 100 ? 13.201  -23.703 -14.198 1.00 49.44  ? 100 LYS A CG  1 
ATOM   1036 C  CD  . LYS A 1 100 ? 11.943  -24.569 -14.108 1.00 54.72  ? 100 LYS A CD  1 
ATOM   1037 C  CE  . LYS A 1 100 ? 12.203  -25.986 -13.635 1.00 60.45  ? 100 LYS A CE  1 
ATOM   1038 N  NZ  . LYS A 1 100 ? 10.955  -26.793 -13.638 1.00 65.19  ? 100 LYS A NZ  1 
ATOM   1039 N  N   . TYR A 1 101 ? 14.737  -20.811 -17.619 1.00 31.40  ? 101 TYR A N   1 
ATOM   1040 C  CA  . TYR A 1 101 ? 14.569  -19.841 -18.729 1.00 32.08  ? 101 TYR A CA  1 
ATOM   1041 C  C   . TYR A 1 101 ? 14.768  -20.501 -20.077 1.00 30.84  ? 101 TYR A C   1 
ATOM   1042 O  O   . TYR A 1 101 ? 15.196  -21.621 -20.148 1.00 29.12  ? 101 TYR A O   1 
ATOM   1043 C  CB  . TYR A 1 101 ? 15.524  -18.658 -18.583 1.00 30.18  ? 101 TYR A CB  1 
ATOM   1044 C  CG  . TYR A 1 101 ? 16.960  -18.953 -18.921 1.00 31.99  ? 101 TYR A CG  1 
ATOM   1045 C  CD1 . TYR A 1 101 ? 17.803  -19.495 -17.967 1.00 30.88  ? 101 TYR A CD1 1 
ATOM   1046 C  CD2 . TYR A 1 101 ? 17.482  -18.698 -20.181 1.00 31.33  ? 101 TYR A CD2 1 
ATOM   1047 C  CE1 . TYR A 1 101 ? 19.135  -19.754 -18.246 1.00 34.76  ? 101 TYR A CE1 1 
ATOM   1048 C  CE2 . TYR A 1 101 ? 18.808  -18.969 -20.481 1.00 32.26  ? 101 TYR A CE2 1 
ATOM   1049 C  CZ  . TYR A 1 101 ? 19.644  -19.486 -19.502 1.00 33.60  ? 101 TYR A CZ  1 
ATOM   1050 O  OH  . TYR A 1 101 ? 20.964  -19.749 -19.725 1.00 33.09  ? 101 TYR A OH  1 
ATOM   1051 N  N   . LYS A 1 102 ? 14.373  -19.775 -21.110 1.00 32.16  ? 102 LYS A N   1 
ATOM   1052 C  CA  . LYS A 1 102 ? 14.687  -20.051 -22.523 1.00 32.62  ? 102 LYS A CA  1 
ATOM   1053 C  C   . LYS A 1 102 ? 14.722  -18.719 -23.270 1.00 31.02  ? 102 LYS A C   1 
ATOM   1054 O  O   . LYS A 1 102 ? 14.227  -17.674 -22.730 1.00 29.54  ? 102 LYS A O   1 
ATOM   1055 C  CB  . LYS A 1 102 ? 13.681  -21.007 -23.164 1.00 34.80  ? 102 LYS A CB  1 
ATOM   1056 C  CG  . LYS A 1 102 ? 12.246  -20.504 -23.283 1.00 41.75  ? 102 LYS A CG  1 
ATOM   1057 C  CD  . LYS A 1 102 ? 11.233  -21.611 -23.521 1.00 44.83  ? 102 LYS A CD  1 
ATOM   1058 C  CE  . LYS A 1 102 ? 11.396  -22.734 -22.522 1.00 52.70  ? 102 LYS A CE  1 
ATOM   1059 N  NZ  . LYS A 1 102 ? 10.093  -23.280 -22.074 1.00 62.54  ? 102 LYS A NZ  1 
ATOM   1060 N  N   . PHE A 1 103 ? 15.282  -18.769 -24.469 1.00 26.38  ? 103 PHE A N   1 
ATOM   1061 C  CA  . PHE A 1 103 ? 15.289  -17.650 -25.436 1.00 28.61  ? 103 PHE A CA  1 
ATOM   1062 C  C   . PHE A 1 103 ? 14.303  -17.996 -26.533 1.00 28.80  ? 103 PHE A C   1 
ATOM   1063 O  O   . PHE A 1 103 ? 14.385  -19.114 -27.015 1.00 32.16  ? 103 PHE A O   1 
ATOM   1064 C  CB  . PHE A 1 103 ? 16.685  -17.416 -26.006 1.00 26.14  ? 103 PHE A CB  1 
ATOM   1065 C  CG  . PHE A 1 103 ? 17.747  -17.034 -25.009 1.00 25.84  ? 103 PHE A CG  1 
ATOM   1066 C  CD1 . PHE A 1 103 ? 17.428  -16.542 -23.757 1.00 25.01  ? 103 PHE A CD1 1 
ATOM   1067 C  CD2 . PHE A 1 103 ? 19.085  -17.107 -25.358 1.00 25.92  ? 103 PHE A CD2 1 
ATOM   1068 C  CE1 . PHE A 1 103 ? 18.416  -16.181 -22.862 1.00 24.81  ? 103 PHE A CE1 1 
ATOM   1069 C  CE2 . PHE A 1 103 ? 20.069  -16.709 -24.470 1.00 26.24  ? 103 PHE A CE2 1 
ATOM   1070 C  CZ  . PHE A 1 103 ? 19.732  -16.239 -23.224 1.00 24.82  ? 103 PHE A CZ  1 
ATOM   1071 N  N   . VAL A 1 104 ? 13.375  -17.093 -26.848 1.00 29.11  ? 104 VAL A N   1 
ATOM   1072 C  CA  . VAL A 1 104 ? 12.449  -17.245 -28.004 1.00 28.86  ? 104 VAL A CA  1 
ATOM   1073 C  C   . VAL A 1 104 ? 12.419  -15.940 -28.792 1.00 27.44  ? 104 VAL A C   1 
ATOM   1074 O  O   . VAL A 1 104 ? 12.423  -14.841 -28.184 1.00 28.82  ? 104 VAL A O   1 
ATOM   1075 C  CB  . VAL A 1 104 ? 11.016  -17.639 -27.598 1.00 34.78  ? 104 VAL A CB  1 
ATOM   1076 C  CG1 . VAL A 1 104 ? 10.990  -18.903 -26.758 1.00 35.22  ? 104 VAL A CG1 1 
ATOM   1077 C  CG2 . VAL A 1 104 ? 10.306  -16.510 -26.876 1.00 38.29  ? 104 VAL A CG2 1 
ATOM   1078 N  N   . ARG A 1 105 ? 12.360  -16.084 -30.104 1.00 24.89  ? 105 ARG A N   1 
ATOM   1079 C  CA  . ARG A 1 105 ? 12.126  -14.979 -31.048 1.00 26.65  ? 105 ARG A CA  1 
ATOM   1080 C  C   . ARG A 1 105 ? 10.625  -14.909 -31.267 1.00 28.00  ? 105 ARG A C   1 
ATOM   1081 O  O   . ARG A 1 105 ? 10.064  -15.933 -31.655 1.00 29.30  ? 105 ARG A O   1 
ATOM   1082 C  CB  . ARG A 1 105 ? 12.848  -15.223 -32.371 1.00 26.07  ? 105 ARG A CB  1 
ATOM   1083 C  CG  . ARG A 1 105 ? 12.903  -13.974 -33.237 1.00 26.10  ? 105 ARG A CG  1 
ATOM   1084 C  CD  . ARG A 1 105 ? 13.707  -14.184 -34.477 1.00 24.95  ? 105 ARG A CD  1 
ATOM   1085 N  NE  . ARG A 1 105 ? 13.593  -12.999 -35.309 1.00 25.97  ? 105 ARG A NE  1 
ATOM   1086 C  CZ  . ARG A 1 105 ? 14.303  -11.895 -35.143 1.00 24.21  ? 105 ARG A CZ  1 
ATOM   1087 N  NH1 . ARG A 1 105 ? 15.150  -11.802 -34.134 1.00 23.71  ? 105 ARG A NH1 1 
ATOM   1088 N  NH2 . ARG A 1 105 ? 14.150  -10.892 -35.979 1.00 23.96  ? 105 ARG A NH2 1 
ATOM   1089 N  N   . ILE A 1 106 ? 10.006  -13.760 -31.004 1.00 27.60  ? 106 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 106 ? 8.530   -13.585 -31.136 1.00 23.85  ? 106 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 106 ? 8.209   -12.999 -32.496 1.00 22.40  ? 106 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 106 ? 9.127   -12.548 -33.150 1.00 22.16  ? 106 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 106 ? 7.967   -12.703 -30.018 1.00 25.11  ? 106 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 106 ? 8.533   -11.284 -30.066 1.00 24.75  ? 106 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 106 ? 8.197   -13.387 -28.678 1.00 26.55  ? 106 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 106 ? 8.047   -10.397 -28.934 1.00 25.72  ? 106 ILE A CD1 1 
ATOM   1097 N  N   . GLN A 1 107 ? 6.936   -13.041 -32.876 1.00 22.12  ? 107 GLN A N   1 
ATOM   1098 C  CA  . GLN A 1 107 ? 6.398   -12.437 -34.112 1.00 25.11  ? 107 GLN A CA  1 
ATOM   1099 C  C   . GLN A 1 107 ? 5.641   -11.168 -33.762 1.00 24.81  ? 107 GLN A C   1 
ATOM   1100 O  O   . GLN A 1 107 ? 5.127   -11.020 -32.645 1.00 25.35  ? 107 GLN A O   1 
ATOM   1101 C  CB  . GLN A 1 107 ? 5.459   -13.425 -34.802 1.00 27.04  ? 107 GLN A CB  1 
ATOM   1102 C  CG  . GLN A 1 107 ? 6.138   -14.748 -35.119 1.00 30.03  ? 107 GLN A CG  1 
ATOM   1103 C  CD  . GLN A 1 107 ? 7.265   -14.511 -36.079 1.00 33.32  ? 107 GLN A CD  1 
ATOM   1104 O  OE1 . GLN A 1 107 ? 7.078   -13.879 -37.111 1.00 35.79  ? 107 GLN A OE1 1 
ATOM   1105 N  NE2 . GLN A 1 107 ? 8.445   -14.979 -35.721 1.00 38.13  ? 107 GLN A NE2 1 
ATOM   1106 N  N   . PRO A 1 108 ? 5.539   -10.227 -34.723 1.00 27.30  ? 108 PRO A N   1 
ATOM   1107 C  CA  . PRO A 1 108 ? 4.689   -9.050  -34.557 1.00 26.44  ? 108 PRO A CA  1 
ATOM   1108 C  C   . PRO A 1 108 ? 3.301   -9.426  -34.034 1.00 23.44  ? 108 PRO A C   1 
ATOM   1109 O  O   . PRO A 1 108 ? 2.711   -10.336 -34.535 1.00 21.92  ? 108 PRO A O   1 
ATOM   1110 C  CB  . PRO A 1 108 ? 4.552   -8.508  -35.989 1.00 26.97  ? 108 PRO A CB  1 
ATOM   1111 C  CG  . PRO A 1 108 ? 5.810   -8.941  -36.659 1.00 28.32  ? 108 PRO A CG  1 
ATOM   1112 C  CD  . PRO A 1 108 ? 6.192   -10.270 -36.040 1.00 25.65  ? 108 PRO A CD  1 
ATOM   1113 N  N   . GLY A 1 109 ? 2.803   -8.680  -33.058 1.00 24.55  ? 109 GLY A N   1 
ATOM   1114 C  CA  . GLY A 1 109 ? 1.482   -8.907  -32.455 1.00 23.67  ? 109 GLY A CA  1 
ATOM   1115 C  C   . GLY A 1 109 ? 1.597   -9.559  -31.099 1.00 23.41  ? 109 GLY A C   1 
ATOM   1116 O  O   . GLY A 1 109 ? 0.678   -9.414  -30.270 1.00 24.61  ? 109 GLY A O   1 
ATOM   1117 N  N   . GLN A 1 110 ? 2.695   -10.261 -30.867 1.00 23.14  ? 110 GLN A N   1 
ATOM   1118 C  CA  . GLN A 1 110 ? 2.948   -10.929 -29.578 1.00 21.98  ? 110 GLN A CA  1 
ATOM   1119 C  C   . GLN A 1 110 ? 3.224   -9.842  -28.542 1.00 22.04  ? 110 GLN A C   1 
ATOM   1120 O  O   . GLN A 1 110 ? 3.789   -8.785  -28.902 1.00 25.88  ? 110 GLN A O   1 
ATOM   1121 C  CB  . GLN A 1 110 ? 4.143   -11.870 -29.697 1.00 24.76  ? 110 GLN A CB  1 
ATOM   1122 C  CG  . GLN A 1 110 ? 4.478   -12.563 -28.391 1.00 26.02  ? 110 GLN A CG  1 
ATOM   1123 C  CD  . GLN A 1 110 ? 3.336   -13.459 -27.970 1.00 29.89  ? 110 GLN A CD  1 
ATOM   1124 O  OE1 . GLN A 1 110 ? 2.552   -13.123 -27.078 1.00 27.30  ? 110 GLN A OE1 1 
ATOM   1125 N  NE2 . GLN A 1 110 ? 3.226   -14.598 -28.639 1.00 27.21  ? 110 GLN A NE2 1 
ATOM   1126 N  N   . THR A 1 111 ? 2.825   -10.108 -27.313 1.00 22.39  ? 111 THR A N   1 
ATOM   1127 C  CA  . THR A 1 111 ? 3.030   -9.264  -26.125 1.00 21.25  ? 111 THR A CA  1 
ATOM   1128 C  C   . THR A 1 111 ? 4.095   -9.859  -25.203 1.00 21.85  ? 111 THR A C   1 
ATOM   1129 O  O   . THR A 1 111 ? 4.400   -11.098 -25.239 1.00 22.80  ? 111 THR A O   1 
ATOM   1130 C  CB  . THR A 1 111 ? 1.705   -9.101  -25.382 1.00 21.51  ? 111 THR A CB  1 
ATOM   1131 O  OG1 . THR A 1 111 ? 1.180   -10.401 -25.096 1.00 21.81  ? 111 THR A OG1 1 
ATOM   1132 C  CG2 . THR A 1 111 ? 0.713   -8.294  -26.182 1.00 20.90  ? 111 THR A CG2 1 
ATOM   1133 N  N   . PHE A 1 112 ? 4.659   -8.988  -24.380 1.00 21.53  ? 112 PHE A N   1 
ATOM   1134 C  CA  . PHE A 1 112 ? 5.654   -9.346  -23.359 1.00 20.87  ? 112 PHE A CA  1 
ATOM   1135 C  C   . PHE A 1 112 ? 5.719   -8.210  -22.334 1.00 20.36  ? 112 PHE A C   1 
ATOM   1136 O  O   . PHE A 1 112 ? 5.264   -7.052  -22.616 1.00 19.21  ? 112 PHE A O   1 
ATOM   1137 C  CB  . PHE A 1 112 ? 6.984   -9.691  -24.044 1.00 22.61  ? 112 PHE A CB  1 
ATOM   1138 C  CG  . PHE A 1 112 ? 7.569   -8.596  -24.893 1.00 23.27  ? 112 PHE A CG  1 
ATOM   1139 C  CD1 . PHE A 1 112 ? 7.203   -8.456  -26.228 1.00 25.81  ? 112 PHE A CD1 1 
ATOM   1140 C  CD2 . PHE A 1 112 ? 8.428   -7.666  -24.343 1.00 23.67  ? 112 PHE A CD2 1 
ATOM   1141 C  CE1 . PHE A 1 112 ? 7.757   -7.457  -27.014 1.00 26.96  ? 112 PHE A CE1 1 
ATOM   1142 C  CE2 . PHE A 1 112 ? 8.964   -6.657  -25.126 1.00 24.85  ? 112 PHE A CE2 1 
ATOM   1143 C  CZ  . PHE A 1 112 ? 8.623   -6.545  -26.455 1.00 26.14  ? 112 PHE A CZ  1 
ATOM   1144 N  N   . SER A 1 113 ? 6.278   -8.530  -21.172 1.00 19.78  ? 113 SER A N   1 
ATOM   1145 C  CA  . SER A 1 113 ? 6.632   -7.550  -20.123 1.00 21.02  ? 113 SER A CA  1 
ATOM   1146 C  C   . SER A 1 113 ? 8.053   -7.043  -20.352 1.00 23.27  ? 113 SER A C   1 
ATOM   1147 O  O   . SER A 1 113 ? 8.951   -7.865  -20.674 1.00 21.95  ? 113 SER A O   1 
ATOM   1148 C  CB  . SER A 1 113 ? 6.486   -8.138  -18.751 1.00 22.55  ? 113 SER A CB  1 
ATOM   1149 O  OG  . SER A 1 113 ? 5.158   -8.566  -18.523 1.00 22.94  ? 113 SER A OG  1 
ATOM   1150 N  N   . VAL A 1 114 ? 8.254   -5.739  -20.147 1.00 21.84  ? 114 VAL A N   1 
ATOM   1151 C  CA  . VAL A 1 114 ? 9.602   -5.111  -20.107 1.00 20.52  ? 114 VAL A CA  1 
ATOM   1152 C  C   . VAL A 1 114 ? 9.916   -4.701  -18.673 1.00 19.68  ? 114 VAL A C   1 
ATOM   1153 O  O   . VAL A 1 114 ? 9.075   -4.058  -18.050 1.00 19.08  ? 114 VAL A O   1 
ATOM   1154 C  CB  . VAL A 1 114 ? 9.673   -3.900  -21.049 1.00 21.38  ? 114 VAL A CB  1 
ATOM   1155 C  CG1 . VAL A 1 114 ? 10.983  -3.141  -20.873 1.00 20.46  ? 114 VAL A CG1 1 
ATOM   1156 C  CG2 . VAL A 1 114 ? 9.469   -4.333  -22.483 1.00 21.47  ? 114 VAL A CG2 1 
ATOM   1157 N  N   . LEU A 1 115 ? 11.103  -5.046  -18.184 1.00 20.69  ? 115 LEU A N   1 
ATOM   1158 C  CA  . LEU A 1 115 ? 11.644  -4.513  -16.910 1.00 20.96  ? 115 LEU A CA  1 
ATOM   1159 C  C   . LEU A 1 115 ? 12.640  -3.402  -17.273 1.00 20.95  ? 115 LEU A C   1 
ATOM   1160 O  O   . LEU A 1 115 ? 13.774  -3.710  -17.668 1.00 19.68  ? 115 LEU A O   1 
ATOM   1161 C  CB  . LEU A 1 115 ? 12.281  -5.644  -16.093 1.00 21.35  ? 115 LEU A CB  1 
ATOM   1162 C  CG  . LEU A 1 115 ? 12.845  -5.236  -14.728 1.00 23.47  ? 115 LEU A CG  1 
ATOM   1163 C  CD1 . LEU A 1 115 ? 11.757  -4.763  -13.777 1.00 24.42  ? 115 LEU A CD1 1 
ATOM   1164 C  CD2 . LEU A 1 115 ? 13.629  -6.370  -14.091 1.00 25.42  ? 115 LEU A CD2 1 
ATOM   1165 N  N   . ALA A 1 116 ? 12.215  -2.148  -17.197 1.00 20.90  ? 116 ALA A N   1 
ATOM   1166 C  CA  . ALA A 1 116 ? 13.101  -0.992  -17.468 1.00 23.65  ? 116 ALA A CA  1 
ATOM   1167 C  C   . ALA A 1 116 ? 14.080  -0.858  -16.298 1.00 22.20  ? 116 ALA A C   1 
ATOM   1168 O  O   . ALA A 1 116 ? 13.645  -0.910  -15.140 1.00 19.50  ? 116 ALA A O   1 
ATOM   1169 C  CB  . ALA A 1 116 ? 12.323  0.279   -17.697 1.00 23.91  ? 116 ALA A CB  1 
ATOM   1170 N  N   . CYS A 1 117 ? 15.369  -0.771  -16.614 1.00 23.18  ? 117 CYS A N   1 
ATOM   1171 C  CA  . CYS A 1 117 ? 16.503  -0.844  -15.652 1.00 25.13  ? 117 CYS A CA  1 
ATOM   1172 C  C   . CYS A 1 117 ? 17.545  0.216   -16.011 1.00 26.50  ? 117 CYS A C   1 
ATOM   1173 O  O   . CYS A 1 117 ? 17.686  0.553   -17.182 1.00 24.49  ? 117 CYS A O   1 
ATOM   1174 C  CB  . CYS A 1 117 ? 17.224  -2.183  -15.668 1.00 27.60  ? 117 CYS A CB  1 
ATOM   1175 S  SG  . CYS A 1 117 ? 16.173  -3.595  -15.250 1.00 32.78  ? 117 CYS A SG  1 
ATOM   1176 N  N   . TYR A 1 118 ? 18.191  0.768   -14.996 1.00 28.68  ? 118 TYR A N   1 
ATOM   1177 C  CA  . TYR A 1 118 ? 19.208  1.847   -15.108 1.00 29.55  ? 118 TYR A CA  1 
ATOM   1178 C  C   . TYR A 1 118 ? 20.303  1.470   -14.115 1.00 30.57  ? 118 TYR A C   1 
ATOM   1179 O  O   . TYR A 1 118 ? 19.962  1.221   -12.928 1.00 27.45  ? 118 TYR A O   1 
ATOM   1180 C  CB  . TYR A 1 118 ? 18.581  3.216   -14.823 1.00 28.79  ? 118 TYR A CB  1 
ATOM   1181 C  CG  . TYR A 1 118 ? 17.496  3.585   -15.810 1.00 31.48  ? 118 TYR A CG  1 
ATOM   1182 C  CD1 . TYR A 1 118 ? 16.175  3.219   -15.592 1.00 29.68  ? 118 TYR A CD1 1 
ATOM   1183 C  CD2 . TYR A 1 118 ? 17.803  4.214   -17.010 1.00 30.23  ? 118 TYR A CD2 1 
ATOM   1184 C  CE1 . TYR A 1 118 ? 15.186  3.480   -16.532 1.00 30.85  ? 118 TYR A CE1 1 
ATOM   1185 C  CE2 . TYR A 1 118 ? 16.822  4.497   -17.945 1.00 32.65  ? 118 TYR A CE2 1 
ATOM   1186 C  CZ  . TYR A 1 118 ? 15.504  4.139   -17.705 1.00 30.89  ? 118 TYR A CZ  1 
ATOM   1187 O  OH  . TYR A 1 118 ? 14.546  4.425   -18.639 1.00 29.57  ? 118 TYR A OH  1 
ATOM   1188 N  N   . ASN A 1 119 ? 21.543  1.333   -14.597 1.00 33.85  ? 119 ASN A N   1 
ATOM   1189 C  CA  . ASN A 1 119 ? 22.723  1.027   -13.745 1.00 34.76  ? 119 ASN A CA  1 
ATOM   1190 C  C   . ASN A 1 119 ? 22.496  -0.343  -13.108 1.00 34.82  ? 119 ASN A C   1 
ATOM   1191 O  O   . ASN A 1 119 ? 22.868  -0.526  -11.948 1.00 34.83  ? 119 ASN A O   1 
ATOM   1192 C  CB  . ASN A 1 119 ? 22.930  2.105   -12.684 1.00 34.85  ? 119 ASN A CB  1 
ATOM   1193 C  CG  . ASN A 1 119 ? 23.191  3.465   -13.282 1.00 35.45  ? 119 ASN A CG  1 
ATOM   1194 O  OD1 . ASN A 1 119 ? 22.484  4.422   -12.978 1.00 44.19  ? 119 ASN A OD1 1 
ATOM   1195 N  ND2 . ASN A 1 119 ? 24.196  3.562   -14.132 1.00 36.73  ? 119 ASN A ND2 1 
ATOM   1196 N  N   . GLY A 1 120 ? 21.849  -1.251  -13.844 1.00 33.53  ? 120 GLY A N   1 
ATOM   1197 C  CA  . GLY A 1 120 ? 21.550  -2.616  -13.393 1.00 31.38  ? 120 GLY A CA  1 
ATOM   1198 C  C   . GLY A 1 120 ? 20.535  -2.650  -12.270 1.00 30.93  ? 120 GLY A C   1 
ATOM   1199 O  O   . GLY A 1 120 ? 20.332  -3.732  -11.754 1.00 31.25  ? 120 GLY A O   1 
ATOM   1200 N  N   . SER A 1 121 ? 19.907  -1.520  -11.926 1.00 29.96  ? 121 SER A N   1 
ATOM   1201 C  CA  . SER A 1 121 ? 18.793  -1.436  -10.947 1.00 31.80  ? 121 SER A CA  1 
ATOM   1202 C  C   . SER A 1 121 ? 17.453  -1.389  -11.679 1.00 30.75  ? 121 SER A C   1 
ATOM   1203 O  O   . SER A 1 121 ? 17.206  -0.511  -12.501 1.00 27.22  ? 121 SER A O   1 
ATOM   1204 C  CB  . SER A 1 121 ? 18.945  -0.241  -10.044 1.00 31.83  ? 121 SER A CB  1 
ATOM   1205 O  OG  . SER A 1 121 ? 20.077  -0.442  -9.209  1.00 39.30  ? 121 SER A OG  1 
ATOM   1206 N  N   . PRO A 1 122 ? 16.543  -2.334  -11.396 1.00 28.61  ? 122 PRO A N   1 
ATOM   1207 C  CA  . PRO A 1 122 ? 15.232  -2.323  -12.032 1.00 31.43  ? 122 PRO A CA  1 
ATOM   1208 C  C   . PRO A 1 122 ? 14.432  -1.097  -11.577 1.00 30.03  ? 122 PRO A C   1 
ATOM   1209 O  O   . PRO A 1 122 ? 14.383  -0.838  -10.401 1.00 31.11  ? 122 PRO A O   1 
ATOM   1210 C  CB  . PRO A 1 122 ? 14.595  -3.639  -11.551 1.00 32.49  ? 122 PRO A CB  1 
ATOM   1211 C  CG  . PRO A 1 122 ? 15.784  -4.484  -11.081 1.00 32.45  ? 122 PRO A CG  1 
ATOM   1212 C  CD  . PRO A 1 122 ? 16.728  -3.469  -10.479 1.00 31.43  ? 122 PRO A CD  1 
ATOM   1213 N  N   . SER A 1 123 ? 13.793  -0.398  -12.506 1.00 29.15  ? 123 SER A N   1 
ATOM   1214 C  CA  . SER A 1 123 ? 13.025  0.836   -12.214 1.00 29.39  ? 123 SER A CA  1 
ATOM   1215 C  C   . SER A 1 123 ? 11.514  0.609   -12.329 1.00 25.27  ? 123 SER A C   1 
ATOM   1216 O  O   . SER A 1 123 ? 10.771  1.204   -11.557 1.00 23.22  ? 123 SER A O   1 
ATOM   1217 C  CB  . SER A 1 123 ? 13.468  1.932   -13.116 1.00 33.96  ? 123 SER A CB  1 
ATOM   1218 O  OG  . SER A 1 123 ? 13.004  3.181   -12.626 1.00 46.09  ? 123 SER A OG  1 
ATOM   1219 N  N   . GLY A 1 124 ? 11.050  -0.192  -13.282 1.00 23.65  ? 124 GLY A N   1 
ATOM   1220 C  CA  . GLY A 1 124 ? 9.607   -0.421  -13.446 1.00 23.83  ? 124 GLY A CA  1 
ATOM   1221 C  C   . GLY A 1 124 ? 9.326   -1.513  -14.454 1.00 22.10  ? 124 GLY A C   1 
ATOM   1222 O  O   . GLY A 1 124 ? 10.247  -1.895  -15.221 1.00 20.66  ? 124 GLY A O   1 
ATOM   1223 N  N   . VAL A 1 125 ? 8.082   -1.961  -14.480 1.00 20.63  ? 125 VAL A N   1 
ATOM   1224 C  CA  . VAL A 1 125 ? 7.649   -3.039  -15.401 1.00 22.20  ? 125 VAL A CA  1 
ATOM   1225 C  C   . VAL A 1 125 ? 6.378   -2.593  -16.116 1.00 21.94  ? 125 VAL A C   1 
ATOM   1226 O  O   . VAL A 1 125 ? 5.505   -1.990  -15.479 1.00 20.56  ? 125 VAL A O   1 
ATOM   1227 C  CB  . VAL A 1 125 ? 7.495   -4.373  -14.645 1.00 24.01  ? 125 VAL A CB  1 
ATOM   1228 C  CG1 . VAL A 1 125 ? 6.642   -4.244  -13.419 1.00 26.28  ? 125 VAL A CG1 1 
ATOM   1229 C  CG2 . VAL A 1 125 ? 6.966   -5.491  -15.535 1.00 27.91  ? 125 VAL A CG2 1 
ATOM   1230 N  N   . TYR A 1 126 ? 6.282   -2.900  -17.404 1.00 22.05  ? 126 TYR A N   1 
ATOM   1231 C  CA  . TYR A 1 126 ? 5.073   -2.612  -18.212 1.00 22.87  ? 126 TYR A CA  1 
ATOM   1232 C  C   . TYR A 1 126 ? 4.941   -3.670  -19.299 1.00 23.30  ? 126 TYR A C   1 
ATOM   1233 O  O   . TYR A 1 126 ? 5.951   -4.317  -19.639 1.00 20.54  ? 126 TYR A O   1 
ATOM   1234 C  CB  . TYR A 1 126 ? 5.150   -1.179  -18.755 1.00 23.35  ? 126 TYR A CB  1 
ATOM   1235 C  CG  . TYR A 1 126 ? 6.403   -0.850  -19.535 1.00 24.02  ? 126 TYR A CG  1 
ATOM   1236 C  CD1 . TYR A 1 126 ? 6.506   -1.162  -20.876 1.00 23.85  ? 126 TYR A CD1 1 
ATOM   1237 C  CD2 . TYR A 1 126 ? 7.483   -0.218  -18.949 1.00 24.65  ? 126 TYR A CD2 1 
ATOM   1238 C  CE1 . TYR A 1 126 ? 7.640   -0.854  -21.608 1.00 23.50  ? 126 TYR A CE1 1 
ATOM   1239 C  CE2 . TYR A 1 126 ? 8.607   0.137   -19.681 1.00 23.98  ? 126 TYR A CE2 1 
ATOM   1240 C  CZ  . TYR A 1 126 ? 8.693   -0.203  -21.010 1.00 23.66  ? 126 TYR A CZ  1 
ATOM   1241 O  OH  . TYR A 1 126 ? 9.805   0.102   -21.747 1.00 27.00  ? 126 TYR A OH  1 
ATOM   1242 N  N   . GLN A 1 127 ? 3.726   -3.808  -19.825 1.00 25.37  ? 127 GLN A N   1 
ATOM   1243 C  CA  . GLN A 1 127 ? 3.387   -4.678  -20.972 1.00 27.36  ? 127 GLN A CA  1 
ATOM   1244 C  C   . GLN A 1 127 ? 3.533   -3.896  -22.262 1.00 26.93  ? 127 GLN A C   1 
ATOM   1245 O  O   . GLN A 1 127 ? 3.181   -2.704  -22.293 1.00 28.91  ? 127 GLN A O   1 
ATOM   1246 C  CB  . GLN A 1 127 ? 1.924   -5.100  -21.042 1.00 29.56  ? 127 GLN A CB  1 
ATOM   1247 C  CG  . GLN A 1 127 ? 1.611   -6.418  -20.390 1.00 31.68  ? 127 GLN A CG  1 
ATOM   1248 C  CD  . GLN A 1 127 ? 2.428   -7.598  -20.856 1.00 29.79  ? 127 GLN A CD  1 
ATOM   1249 O  OE1 . GLN A 1 127 ? 3.439   -7.905  -20.258 1.00 29.74  ? 127 GLN A OE1 1 
ATOM   1250 N  NE2 . GLN A 1 127 ? 1.921   -8.350  -21.818 1.00 30.79  ? 127 GLN A NE2 1 
ATOM   1251 N  N   A CYS A 1 128 ? 4.087   -4.566  -23.284 0.31 26.99  ? 128 CYS A N   1 
ATOM   1252 N  N   B CYS A 1 128 ? 3.983   -4.556  -23.323 0.19 25.83  ? 128 CYS A N   1 
ATOM   1253 N  N   C CYS A 1 128 ? 4.087   -4.566  -23.284 0.31 26.99  ? 128 CYS A N   1 
ATOM   1254 N  N   D CYS A 1 128 ? 3.983   -4.556  -23.323 0.19 25.83  ? 128 CYS A N   1 
ATOM   1255 C  CA  A CYS A 1 128 ? 4.309   -4.083  -24.676 0.31 27.55  ? 128 CYS A CA  1 
ATOM   1256 C  CA  B CYS A 1 128 ? 4.014   -3.973  -24.683 0.19 25.36  ? 128 CYS A CA  1 
ATOM   1257 C  CA  C CYS A 1 128 ? 4.309   -4.083  -24.676 0.31 27.55  ? 128 CYS A CA  1 
ATOM   1258 C  CA  D CYS A 1 128 ? 4.014   -3.973  -24.683 0.19 25.36  ? 128 CYS A CA  1 
ATOM   1259 C  C   A CYS A 1 128 ? 3.748   -5.109  -25.666 0.31 26.63  ? 128 CYS A C   1 
ATOM   1260 C  C   B CYS A 1 128 ? 3.968   -5.104  -25.706 0.19 25.60  ? 128 CYS A C   1 
ATOM   1261 C  C   C CYS A 1 128 ? 3.748   -5.109  -25.666 0.31 26.63  ? 128 CYS A C   1 
ATOM   1262 C  C   D CYS A 1 128 ? 3.968   -5.104  -25.706 0.19 25.60  ? 128 CYS A C   1 
ATOM   1263 O  O   A CYS A 1 128 ? 3.387   -6.209  -25.214 0.31 26.37  ? 128 CYS A O   1 
ATOM   1264 O  O   B CYS A 1 128 ? 4.215   -6.262  -25.329 0.19 25.23  ? 128 CYS A O   1 
ATOM   1265 O  O   C CYS A 1 128 ? 3.387   -6.209  -25.214 0.31 26.37  ? 128 CYS A O   1 
ATOM   1266 O  O   D CYS A 1 128 ? 4.215   -6.262  -25.329 0.19 25.23  ? 128 CYS A O   1 
ATOM   1267 C  CB  A CYS A 1 128 ? 5.792   -3.952  -24.997 0.31 28.81  ? 128 CYS A CB  1 
ATOM   1268 C  CB  B CYS A 1 128 ? 5.256   -3.119  -24.886 0.19 24.78  ? 128 CYS A CB  1 
ATOM   1269 C  CB  C CYS A 1 128 ? 5.792   -3.952  -24.997 0.31 28.81  ? 128 CYS A CB  1 
ATOM   1270 C  CB  D CYS A 1 128 ? 5.256   -3.119  -24.886 0.19 24.78  ? 128 CYS A CB  1 
ATOM   1271 S  SG  A CYS A 1 128 ? 6.552   -2.426  -24.401 0.31 34.05  ? 128 CYS A SG  1 
ATOM   1272 S  SG  B CYS A 1 128 ? 6.767   -4.109  -24.937 0.19 24.78  ? 128 CYS A SG  1 
ATOM   1273 S  SG  C CYS A 1 128 ? 6.552   -2.426  -24.401 0.31 34.05  ? 128 CYS A SG  1 
ATOM   1274 S  SG  D CYS A 1 128 ? 6.767   -4.109  -24.937 0.19 24.78  ? 128 CYS A SG  1 
ATOM   1275 N  N   . ALA A 1 129 ? 3.678   -4.749  -26.954 1.00 27.36  ? 129 ALA A N   1 
ATOM   1276 C  CA  . ALA A 1 129 ? 3.574   -5.694  -28.087 1.00 26.17  ? 129 ALA A CA  1 
ATOM   1277 C  C   . ALA A 1 129 ? 4.679   -5.349  -29.079 1.00 26.74  ? 129 ALA A C   1 
ATOM   1278 O  O   . ALA A 1 129 ? 5.097   -4.161  -29.154 1.00 31.17  ? 129 ALA A O   1 
ATOM   1279 C  CB  . ALA A 1 129 ? 2.223   -5.601  -28.716 1.00 25.87  ? 129 ALA A CB  1 
ATOM   1280 N  N   . MET A 1 130 ? 5.180   -6.361  -29.767 1.00 25.52  ? 130 MET A N   1 
ATOM   1281 C  CA  . MET A 1 130 ? 5.936   -6.199  -31.026 1.00 26.46  ? 130 MET A CA  1 
ATOM   1282 C  C   . MET A 1 130 ? 4.942   -5.662  -32.062 1.00 26.69  ? 130 MET A C   1 
ATOM   1283 O  O   . MET A 1 130 ? 3.987   -6.392  -32.432 1.00 23.00  ? 130 MET A O   1 
ATOM   1284 C  CB  . MET A 1 130 ? 6.523   -7.546  -31.452 1.00 27.97  ? 130 MET A CB  1 
ATOM   1285 C  CG  . MET A 1 130 ? 7.394   -7.528  -32.701 1.00 30.09  ? 130 MET A CG  1 
ATOM   1286 S  SD  . MET A 1 130 ? 8.873   -6.527  -32.529 1.00 32.92  ? 130 MET A SD  1 
ATOM   1287 C  CE  . MET A 1 130 ? 9.589   -7.171  -31.022 1.00 30.87  ? 130 MET A CE  1 
ATOM   1288 N  N   . ARG A 1 131 ? 5.129   -4.416  -32.490 1.00 22.57  ? 131 ARG A N   1 
ATOM   1289 C  CA  . ARG A 1 131 ? 4.311   -3.824  -33.561 1.00 22.24  ? 131 ARG A CA  1 
ATOM   1290 C  C   . ARG A 1 131 ? 4.599   -4.548  -34.874 1.00 23.43  ? 131 ARG A C   1 
ATOM   1291 O  O   . ARG A 1 131 ? 5.667   -5.138  -35.046 1.00 23.71  ? 131 ARG A O   1 
ATOM   1292 C  CB  . ARG A 1 131 ? 4.633   -2.347  -33.729 1.00 22.35  ? 131 ARG A CB  1 
ATOM   1293 C  CG  . ARG A 1 131 ? 4.525   -1.514  -32.463 1.00 22.65  ? 131 ARG A CG  1 
ATOM   1294 C  CD  . ARG A 1 131 ? 3.213   -1.643  -31.764 1.00 22.03  ? 131 ARG A CD  1 
ATOM   1295 N  NE  . ARG A 1 131 ? 2.129   -1.352  -32.671 1.00 24.82  ? 131 ARG A NE  1 
ATOM   1296 C  CZ  . ARG A 1 131 ? 0.850   -1.578  -32.402 1.00 24.32  ? 131 ARG A CZ  1 
ATOM   1297 N  NH1 . ARG A 1 131 ? 0.481   -2.027  -31.222 1.00 23.43  ? 131 ARG A NH1 1 
ATOM   1298 N  NH2 . ARG A 1 131 ? -0.058  -1.341  -33.326 1.00 25.64  ? 131 ARG A NH2 1 
ATOM   1299 N  N   . PRO A 1 132 ? 3.660   -4.505  -35.847 1.00 23.32  ? 132 PRO A N   1 
ATOM   1300 C  CA  . PRO A 1 132 ? 3.898   -5.058  -37.183 1.00 22.96  ? 132 PRO A CA  1 
ATOM   1301 C  C   . PRO A 1 132 ? 5.160   -4.480  -37.848 1.00 21.20  ? 132 PRO A C   1 
ATOM   1302 O  O   . PRO A 1 132 ? 5.694   -5.120  -38.674 1.00 19.30  ? 132 PRO A O   1 
ATOM   1303 C  CB  . PRO A 1 132 ? 2.609   -4.711  -37.955 1.00 22.68  ? 132 PRO A CB  1 
ATOM   1304 C  CG  . PRO A 1 132 ? 1.566   -4.588  -36.860 1.00 23.87  ? 132 PRO A CG  1 
ATOM   1305 C  CD  . PRO A 1 132 ? 2.312   -3.927  -35.719 1.00 23.66  ? 132 PRO A CD  1 
ATOM   1306 N  N   . ASN A 1 133 ? 5.618   -3.291  -37.470 1.00 20.88  ? 133 ASN A N   1 
ATOM   1307 C  CA  . ASN A 1 133 ? 6.816   -2.695  -38.114 1.00 22.55  ? 133 ASN A CA  1 
ATOM   1308 C  C   . ASN A 1 133 ? 8.073   -3.052  -37.311 1.00 24.84  ? 133 ASN A C   1 
ATOM   1309 O  O   . ASN A 1 133 ? 9.128   -2.454  -37.611 1.00 22.82  ? 133 ASN A O   1 
ATOM   1310 C  CB  . ASN A 1 133 ? 6.729   -1.188  -38.288 1.00 22.33  ? 133 ASN A CB  1 
ATOM   1311 C  CG  . ASN A 1 133 ? 6.693   -0.448  -36.972 1.00 21.93  ? 133 ASN A CG  1 
ATOM   1312 O  OD1 . ASN A 1 133 ? 6.748   -1.050  -35.888 1.00 21.85  ? 133 ASN A OD1 1 
ATOM   1313 N  ND2 . ASN A 1 133 ? 6.529   0.850   -37.076 1.00 20.25  ? 133 ASN A ND2 1 
ATOM   1314 N  N   . PHE A 1 134 ? 7.966   -3.987  -36.356 1.00 24.46  ? 134 PHE A N   1 
ATOM   1315 C  CA  . PHE A 1 134 ? 9.111   -4.612  -35.640 1.00 25.45  ? 134 PHE A CA  1 
ATOM   1316 C  C   . PHE A 1 134 ? 9.731   -3.614  -34.658 1.00 25.74  ? 134 PHE A C   1 
ATOM   1317 O  O   . PHE A 1 134 ? 10.890  -3.794  -34.283 1.00 26.74  ? 134 PHE A O   1 
ATOM   1318 C  CB  . PHE A 1 134 ? 10.163  -5.123  -36.628 1.00 26.19  ? 134 PHE A CB  1 
ATOM   1319 C  CG  . PHE A 1 134 ? 9.698   -6.308  -37.430 1.00 25.12  ? 134 PHE A CG  1 
ATOM   1320 C  CD1 . PHE A 1 134 ? 9.572   -7.556  -36.841 1.00 26.99  ? 134 PHE A CD1 1 
ATOM   1321 C  CD2 . PHE A 1 134 ? 9.346   -6.163  -38.755 1.00 25.89  ? 134 PHE A CD2 1 
ATOM   1322 C  CE1 . PHE A 1 134 ? 9.088   -8.636  -37.565 1.00 26.09  ? 134 PHE A CE1 1 
ATOM   1323 C  CE2 . PHE A 1 134 ? 8.895   -7.246  -39.490 1.00 25.55  ? 134 PHE A CE2 1 
ATOM   1324 C  CZ  . PHE A 1 134 ? 8.799   -8.486  -38.903 1.00 26.31  ? 134 PHE A CZ  1 
ATOM   1325 N  N   . THR A 1 135 ? 8.961   -2.615  -34.226 1.00 22.80  ? 135 THR A N   1 
ATOM   1326 C  CA  . THR A 1 135 ? 9.344   -1.743  -33.107 1.00 22.25  ? 135 THR A CA  1 
ATOM   1327 C  C   . THR A 1 135 ? 8.451   -2.035  -31.914 1.00 22.15  ? 135 THR A C   1 
ATOM   1328 O  O   . THR A 1 135 ? 7.454   -2.793  -32.051 1.00 22.46  ? 135 THR A O   1 
ATOM   1329 C  CB  . THR A 1 135 ? 9.261   -0.287  -33.545 1.00 24.71  ? 135 THR A CB  1 
ATOM   1330 O  OG1 . THR A 1 135 ? 7.900   0.019   -33.853 1.00 25.43  ? 135 THR A OG1 1 
ATOM   1331 C  CG2 . THR A 1 135 ? 10.128  -0.036  -34.751 1.00 25.70  ? 135 THR A CG2 1 
ATOM   1332 N  N   . ILE A 1 136 ? 8.795   -1.436  -30.784 1.00 19.82  ? 136 ILE A N   1 
ATOM   1333 C  CA  . ILE A 1 136 ? 7.970   -1.484  -29.564 1.00 20.85  ? 136 ILE A CA  1 
ATOM   1334 C  C   . ILE A 1 136 ? 7.792   -0.053  -29.081 1.00 21.40  ? 136 ILE A C   1 
ATOM   1335 O  O   . ILE A 1 136 ? 8.664   0.776   -29.316 1.00 20.79  ? 136 ILE A O   1 
ATOM   1336 C  CB  . ILE A 1 136 ? 8.561   -2.452  -28.521 1.00 23.49  ? 136 ILE A CB  1 
ATOM   1337 C  CG1 . ILE A 1 136 ? 9.726   -1.844  -27.752 1.00 24.15  ? 136 ILE A CG1 1 
ATOM   1338 C  CG2 . ILE A 1 136 ? 8.949   -3.780  -29.176 1.00 24.26  ? 136 ILE A CG2 1 
ATOM   1339 C  CD1 . ILE A 1 136 ? 10.184  -2.720  -26.619 1.00 26.47  ? 136 ILE A CD1 1 
ATOM   1340 N  N   . LYS A 1 137 ? 6.613   0.245   -28.573 1.00 24.32  ? 137 LYS A N   1 
ATOM   1341 C  CA  . LYS A 1 137 ? 6.295   1.588   -28.046 1.00 27.06  ? 137 LYS A CA  1 
ATOM   1342 C  C   . LYS A 1 137 ? 6.553   1.492   -26.551 1.00 24.94  ? 137 LYS A C   1 
ATOM   1343 O  O   . LYS A 1 137 ? 5.654   1.187   -25.792 1.00 24.51  ? 137 LYS A O   1 
ATOM   1344 C  CB  . LYS A 1 137 ? 4.878   1.992   -28.457 1.00 32.46  ? 137 LYS A CB  1 
ATOM   1345 C  CG  . LYS A 1 137 ? 4.696   2.206   -29.957 1.00 38.93  ? 137 LYS A CG  1 
ATOM   1346 C  CD  . LYS A 1 137 ? 3.264   2.531   -30.330 1.00 44.57  ? 137 LYS A CD  1 
ATOM   1347 C  CE  . LYS A 1 137 ? 3.020   2.408   -31.817 1.00 55.08  ? 137 LYS A CE  1 
ATOM   1348 N  NZ  . LYS A 1 137 ? 1.582   2.580   -32.141 1.00 63.96  ? 137 LYS A NZ  1 
ATOM   1349 N  N   . GLY A 1 138 ? 7.810   1.648   -26.182 1.00 28.11  ? 138 GLY A N   1 
ATOM   1350 C  CA  . GLY A 1 138 ? 8.263   1.467   -24.801 1.00 25.97  ? 138 GLY A CA  1 
ATOM   1351 C  C   . GLY A 1 138 ? 8.374   2.788   -24.086 1.00 26.10  ? 138 GLY A C   1 
ATOM   1352 O  O   . GLY A 1 138 ? 7.932   3.827   -24.619 1.00 26.68  ? 138 GLY A O   1 
ATOM   1353 N  N   . SER A 1 139 ? 8.935   2.725   -22.888 1.00 25.09  ? 139 SER A N   1 
ATOM   1354 C  CA  . SER A 1 139 ? 9.331   3.880   -22.066 1.00 27.69  ? 139 SER A CA  1 
ATOM   1355 C  C   . SER A 1 139 ? 10.768  3.635   -21.601 1.00 26.95  ? 139 SER A C   1 
ATOM   1356 O  O   . SER A 1 139 ? 11.008  2.738   -20.779 1.00 22.09  ? 139 SER A O   1 
ATOM   1357 C  CB  . SER A 1 139 ? 8.385   4.120   -20.924 1.00 29.36  ? 139 SER A CB  1 
ATOM   1358 O  OG  . SER A 1 139 ? 8.957   5.083   -20.053 1.00 30.93  ? 139 SER A OG  1 
ATOM   1359 N  N   . PHE A 1 140 ? 11.688  4.378   -22.192 1.00 27.09  ? 140 PHE A N   1 
ATOM   1360 C  CA  . PHE A 1 140 ? 13.138  4.119   -22.132 1.00 28.51  ? 140 PHE A CA  1 
ATOM   1361 C  C   . PHE A 1 140 ? 13.870  5.457   -22.132 1.00 32.25  ? 140 PHE A C   1 
ATOM   1362 O  O   . PHE A 1 140 ? 13.666  6.240   -23.078 1.00 32.70  ? 140 PHE A O   1 
ATOM   1363 C  CB  . PHE A 1 140 ? 13.558  3.307   -23.355 1.00 26.47  ? 140 PHE A CB  1 
ATOM   1364 C  CG  . PHE A 1 140 ? 13.220  1.849   -23.266 1.00 26.83  ? 140 PHE A CG  1 
ATOM   1365 C  CD1 . PHE A 1 140 ? 13.665  1.094   -22.191 1.00 29.23  ? 140 PHE A CD1 1 
ATOM   1366 C  CD2 . PHE A 1 140 ? 12.463  1.233   -24.241 1.00 26.06  ? 140 PHE A CD2 1 
ATOM   1367 C  CE1 . PHE A 1 140 ? 13.354  -0.254  -22.092 1.00 30.77  ? 140 PHE A CE1 1 
ATOM   1368 C  CE2 . PHE A 1 140 ? 12.194  -0.122  -24.162 1.00 27.90  ? 140 PHE A CE2 1 
ATOM   1369 C  CZ  . PHE A 1 140 ? 12.634  -0.860  -23.087 1.00 28.04  ? 140 PHE A CZ  1 
ATOM   1370 N  N   . LEU A 1 141 ? 14.665  5.702   -21.094 1.00 32.58  ? 141 LEU A N   1 
ATOM   1371 C  CA  . LEU A 1 141 ? 15.566  6.868   -21.032 1.00 34.60  ? 141 LEU A CA  1 
ATOM   1372 C  C   . LEU A 1 141 ? 16.984  6.375   -21.326 1.00 33.48  ? 141 LEU A C   1 
ATOM   1373 O  O   . LEU A 1 141 ? 17.215  5.160   -21.409 1.00 30.94  ? 141 LEU A O   1 
ATOM   1374 C  CB  . LEU A 1 141 ? 15.461  7.548   -19.660 1.00 38.29  ? 141 LEU A CB  1 
ATOM   1375 C  CG  . LEU A 1 141 ? 14.060  7.952   -19.183 1.00 41.13  ? 141 LEU A CG  1 
ATOM   1376 C  CD1 . LEU A 1 141 ? 14.119  8.482   -17.751 1.00 39.15  ? 141 LEU A CD1 1 
ATOM   1377 C  CD2 . LEU A 1 141 ? 13.418  8.979   -20.116 1.00 43.55  ? 141 LEU A CD2 1 
ATOM   1378 N  N   . ASN A 1 142 ? 17.909  7.305   -21.503 1.00 35.04  ? 142 ASN A N   1 
ATOM   1379 C  CA  . ASN A 1 142 ? 19.354  6.997   -21.594 1.00 33.62  ? 142 ASN A CA  1 
ATOM   1380 C  C   . ASN A 1 142 ? 19.720  6.090   -20.404 1.00 29.46  ? 142 ASN A C   1 
ATOM   1381 O  O   . ASN A 1 142 ? 19.266  6.351   -19.246 1.00 27.41  ? 142 ASN A O   1 
ATOM   1382 C  CB  . ASN A 1 142 ? 20.170  8.292   -21.723 1.00 38.64  ? 142 ASN A CB  1 
ATOM   1383 C  CG  . ASN A 1 142 ? 20.122  8.848   -23.136 1.00 47.45  ? 142 ASN A CG  1 
ATOM   1384 O  OD1 . ASN A 1 142 ? 20.124  8.098   -24.116 1.00 55.00  ? 142 ASN A OD1 1 
ATOM   1385 N  ND2 . ASN A 1 142 ? 20.082  10.162  -23.265 1.00 47.43  ? 142 ASN A ND2 1 
ATOM   1386 N  N   A GLY A 1 143 ? 20.492  5.036   -20.690 0.20 27.42  ? 143 GLY A N   1 
ATOM   1387 N  N   B GLY A 1 143 ? 20.492  5.036   -20.690 0.20 27.42  ? 143 GLY A N   1 
ATOM   1388 N  N   C GLY A 1 143 ? 20.493  5.032   -20.667 0.30 29.71  ? 143 GLY A N   1 
ATOM   1389 N  N   D GLY A 1 143 ? 20.493  5.032   -20.667 0.30 29.71  ? 143 GLY A N   1 
ATOM   1390 C  CA  A GLY A 1 143 ? 21.003  4.070   -19.695 0.20 26.38  ? 143 GLY A CA  1 
ATOM   1391 C  CA  B GLY A 1 143 ? 21.003  4.070   -19.695 0.20 26.38  ? 143 GLY A CA  1 
ATOM   1392 C  CA  C GLY A 1 143 ? 21.014  4.116   -19.630 0.30 30.48  ? 143 GLY A CA  1 
ATOM   1393 C  CA  D GLY A 1 143 ? 21.014  4.116   -19.630 0.30 30.48  ? 143 GLY A CA  1 
ATOM   1394 C  C   A GLY A 1 143 ? 20.175  2.795   -19.649 0.20 24.65  ? 143 GLY A C   1 
ATOM   1395 C  C   B GLY A 1 143 ? 20.175  2.795   -19.649 0.20 24.65  ? 143 GLY A C   1 
ATOM   1396 C  C   C GLY A 1 143 ? 20.160  2.866   -19.480 0.30 30.36  ? 143 GLY A C   1 
ATOM   1397 C  C   D GLY A 1 143 ? 20.160  2.866   -19.480 0.30 30.36  ? 143 GLY A C   1 
ATOM   1398 O  O   A GLY A 1 143 ? 20.568  1.861   -18.915 0.20 24.59  ? 143 GLY A O   1 
ATOM   1399 O  O   B GLY A 1 143 ? 20.568  1.861   -18.915 0.20 24.59  ? 143 GLY A O   1 
ATOM   1400 O  O   C GLY A 1 143 ? 20.587  1.936   -18.758 0.30 30.66  ? 143 GLY A O   1 
ATOM   1401 O  O   D GLY A 1 143 ? 20.587  1.936   -18.758 0.30 30.66  ? 143 GLY A O   1 
ATOM   1402 N  N   A SER A 1 144 ? 19.075  2.739   -20.405 0.20 22.78  ? 144 SER A N   1 
ATOM   1403 N  N   B SER A 1 144 ? 19.075  2.739   -20.405 0.20 22.78  ? 144 SER A N   1 
ATOM   1404 N  N   C SER A 1 144 ? 18.994  2.834   -20.131 0.30 30.07  ? 144 SER A N   1 
ATOM   1405 N  N   D SER A 1 144 ? 18.994  2.834   -20.131 0.30 30.07  ? 144 SER A N   1 
ATOM   1406 C  CA  A SER A 1 144 ? 18.087  1.628   -20.361 0.20 21.10  ? 144 SER A CA  1 
ATOM   1407 C  CA  B SER A 1 144 ? 18.087  1.628   -20.361 0.20 21.10  ? 144 SER A CA  1 
ATOM   1408 C  CA  C SER A 1 144 ? 18.041  1.693   -20.102 0.30 28.94  ? 144 SER A CA  1 
ATOM   1409 C  CA  D SER A 1 144 ? 18.041  1.693   -20.102 0.30 28.94  ? 144 SER A CA  1 
ATOM   1410 C  C   A SER A 1 144 ? 18.503  0.490   -21.299 0.20 19.99  ? 144 SER A C   1 
ATOM   1411 C  C   B SER A 1 144 ? 18.503  0.490   -21.299 0.20 19.99  ? 144 SER A C   1 
ATOM   1412 C  C   C SER A 1 144 ? 18.503  0.616   -21.084 0.30 29.26  ? 144 SER A C   1 
ATOM   1413 C  C   D SER A 1 144 ? 18.503  0.616   -21.084 0.30 29.26  ? 144 SER A C   1 
ATOM   1414 O  O   A SER A 1 144 ? 17.873  -0.589  -21.223 0.20 18.92  ? 144 SER A O   1 
ATOM   1415 O  O   B SER A 1 144 ? 17.873  -0.589  -21.223 0.20 18.92  ? 144 SER A O   1 
ATOM   1416 O  O   C SER A 1 144 ? 18.000  -0.530  -21.004 0.30 27.41  ? 144 SER A O   1 
ATOM   1417 O  O   D SER A 1 144 ? 18.000  -0.530  -21.004 0.30 27.41  ? 144 SER A O   1 
ATOM   1418 C  CB  A SER A 1 144 ? 16.707  2.117   -20.697 0.20 20.90  ? 144 SER A CB  1 
ATOM   1419 C  CB  B SER A 1 144 ? 16.707  2.117   -20.697 0.20 20.90  ? 144 SER A CB  1 
ATOM   1420 C  CB  C SER A 1 144 ? 16.648  2.150   -20.428 0.30 28.49  ? 144 SER A CB  1 
ATOM   1421 C  CB  D SER A 1 144 ? 16.648  2.150   -20.428 0.30 28.49  ? 144 SER A CB  1 
ATOM   1422 O  OG  A SER A 1 144 ? 16.678  2.694   -21.991 0.20 20.99  ? 144 SER A OG  1 
ATOM   1423 O  OG  B SER A 1 144 ? 16.678  2.694   -21.991 0.20 20.99  ? 144 SER A OG  1 
ATOM   1424 O  OG  C SER A 1 144 ? 16.578  2.650   -21.751 0.30 27.59  ? 144 SER A OG  1 
ATOM   1425 O  OG  D SER A 1 144 ? 16.578  2.650   -21.751 0.30 27.59  ? 144 SER A OG  1 
ATOM   1426 N  N   A CYS A 1 145 ? 19.488  0.721   -22.175 0.20 18.50  ? 145 CYS A N   1 
ATOM   1427 N  N   B CYS A 1 145 ? 19.488  0.721   -22.175 0.20 18.50  ? 145 CYS A N   1 
ATOM   1428 N  N   C CYS A 1 145 ? 19.390  1.002   -22.006 0.30 29.68  ? 145 CYS A N   1 
ATOM   1429 N  N   D CYS A 1 145 ? 19.390  1.002   -22.006 0.30 29.68  ? 145 CYS A N   1 
ATOM   1430 C  CA  A CYS A 1 145 ? 19.996  -0.312  -23.115 0.20 17.32  ? 145 CYS A CA  1 
ATOM   1431 C  CA  B CYS A 1 145 ? 19.996  -0.312  -23.115 0.20 17.32  ? 145 CYS A CA  1 
ATOM   1432 C  CA  C CYS A 1 145 ? 19.999  0.124   -23.035 0.30 29.66  ? 145 CYS A CA  1 
ATOM   1433 C  CA  D CYS A 1 145 ? 19.999  0.124   -23.035 0.30 29.66  ? 145 CYS A CA  1 
ATOM   1434 C  C   A CYS A 1 145 ? 20.405  -1.543  -22.289 0.20 17.89  ? 145 CYS A C   1 
ATOM   1435 C  C   B CYS A 1 145 ? 20.405  -1.543  -22.289 0.20 17.89  ? 145 CYS A C   1 
ATOM   1436 C  C   C CYS A 1 145 ? 20.353  -1.223  -22.379 0.30 29.56  ? 145 CYS A C   1 
ATOM   1437 C  C   D CYS A 1 145 ? 20.353  -1.223  -22.379 0.30 29.56  ? 145 CYS A C   1 
ATOM   1438 O  O   A CYS A 1 145 ? 21.000  -1.367  -21.208 0.20 17.65  ? 145 CYS A O   1 
ATOM   1439 O  O   B CYS A 1 145 ? 20.999  -1.367  -21.208 0.20 17.65  ? 145 CYS A O   1 
ATOM   1440 O  O   C CYS A 1 145 ? 20.923  -1.218  -21.268 0.30 28.81  ? 145 CYS A O   1 
ATOM   1441 O  O   D CYS A 1 145 ? 20.923  -1.218  -21.268 0.30 28.81  ? 145 CYS A O   1 
ATOM   1442 C  CB  A CYS A 1 145 ? 21.122  0.229   -23.989 0.20 16.53  ? 145 CYS A CB  1 
ATOM   1443 C  CB  B CYS A 1 145 ? 21.122  0.229   -23.989 0.20 16.53  ? 145 CYS A CB  1 
ATOM   1444 C  CB  C CYS A 1 145 ? 21.186  0.841   -23.669 0.30 32.07  ? 145 CYS A CB  1 
ATOM   1445 C  CB  D CYS A 1 145 ? 21.186  0.841   -23.669 0.30 32.07  ? 145 CYS A CB  1 
ATOM   1446 S  SG  A CYS A 1 145 ? 20.607  1.589   -25.077 0.20 14.42  ? 145 CYS A SG  1 
ATOM   1447 S  SG  B CYS A 1 145 ? 20.607  1.589   -25.077 0.20 14.42  ? 145 CYS A SG  1 
ATOM   1448 S  SG  C CYS A 1 145 ? 20.889  2.611   -23.959 0.30 31.74  ? 145 CYS A SG  1 
ATOM   1449 S  SG  D CYS A 1 145 ? 20.889  2.611   -23.959 0.30 31.74  ? 145 CYS A SG  1 
ATOM   1450 N  N   A GLY A 1 146 ? 20.012  -2.738  -22.737 0.20 18.10  ? 146 GLY A N   1 
ATOM   1451 N  N   B GLY A 1 146 ? 20.012  -2.738  -22.737 0.20 18.10  ? 146 GLY A N   1 
ATOM   1452 N  N   C GLY A 1 146 ? 19.932  -2.337  -22.990 0.30 28.62  ? 146 GLY A N   1 
ATOM   1453 N  N   D GLY A 1 146 ? 19.932  -2.337  -22.990 0.30 28.62  ? 146 GLY A N   1 
ATOM   1454 C  CA  A GLY A 1 146 ? 20.243  -4.005  -22.019 0.20 18.36  ? 146 GLY A CA  1 
ATOM   1455 C  CA  B GLY A 1 146 ? 20.243  -4.005  -22.019 0.20 18.36  ? 146 GLY A CA  1 
ATOM   1456 C  CA  C GLY A 1 146 ? 20.165  -3.704  -22.484 0.30 27.01  ? 146 GLY A CA  1 
ATOM   1457 C  CA  D GLY A 1 146 ? 20.165  -3.704  -22.484 0.30 27.01  ? 146 GLY A CA  1 
ATOM   1458 C  C   A GLY A 1 146 ? 19.043  -4.434  -21.183 0.20 18.44  ? 146 GLY A C   1 
ATOM   1459 C  C   B GLY A 1 146 ? 19.043  -4.434  -21.183 0.20 18.44  ? 146 GLY A C   1 
ATOM   1460 C  C   C GLY A 1 146 ? 19.056  -4.214  -21.567 0.30 25.96  ? 146 GLY A C   1 
ATOM   1461 C  C   D GLY A 1 146 ? 19.056  -4.214  -21.567 0.30 25.96  ? 146 GLY A C   1 
ATOM   1462 O  O   A GLY A 1 146 ? 19.024  -5.597  -20.742 0.20 17.71  ? 146 GLY A O   1 
ATOM   1463 O  O   B GLY A 1 146 ? 19.024  -5.597  -20.742 0.20 17.71  ? 146 GLY A O   1 
ATOM   1464 O  O   C GLY A 1 146 ? 19.187  -5.354  -21.073 0.30 24.97  ? 146 GLY A O   1 
ATOM   1465 O  O   D GLY A 1 146 ? 19.187  -5.354  -21.073 0.30 24.97  ? 146 GLY A O   1 
ATOM   1466 N  N   A SER A 1 147 ? 18.074  -3.539  -20.955 0.20 18.41  ? 147 SER A N   1 
ATOM   1467 N  N   B SER A 1 147 ? 18.074  -3.539  -20.955 0.20 18.41  ? 147 SER A N   1 
ATOM   1468 N  N   C SER A 1 147 ? 17.997  -3.426  -21.334 0.30 24.12  ? 147 SER A N   1 
ATOM   1469 N  N   D SER A 1 147 ? 17.997  -3.426  -21.334 0.30 24.12  ? 147 SER A N   1 
ATOM   1470 C  CA  A SER A 1 147 ? 16.725  -3.883  -20.436 0.20 18.22  ? 147 SER A CA  1 
ATOM   1471 C  CA  B SER A 1 147 ? 16.725  -3.883  -20.436 0.20 18.22  ? 147 SER A CA  1 
ATOM   1472 C  CA  C SER A 1 147 ? 16.759  -3.851  -20.619 0.30 21.49  ? 147 SER A CA  1 
ATOM   1473 C  CA  D SER A 1 147 ? 16.759  -3.851  -20.619 0.30 21.49  ? 147 SER A CA  1 
ATOM   1474 C  C   A SER A 1 147 ? 16.095  -4.969  -21.321 0.20 18.13  ? 147 SER A C   1 
ATOM   1475 C  C   B SER A 1 147 ? 16.095  -4.969  -21.321 0.20 18.13  ? 147 SER A C   1 
ATOM   1476 C  C   C SER A 1 147 ? 16.080  -4.998  -21.386 0.30 19.69  ? 147 SER A C   1 
ATOM   1477 C  C   D SER A 1 147 ? 16.080  -4.997  -21.386 0.30 19.69  ? 147 SER A C   1 
ATOM   1478 O  O   A SER A 1 147 ? 16.288  -4.935  -22.540 0.20 18.11  ? 147 SER A O   1 
ATOM   1479 O  O   B SER A 1 147 ? 16.288  -4.935  -22.540 0.20 18.11  ? 147 SER A O   1 
ATOM   1480 O  O   C SER A 1 147 ? 16.217  -5.043  -22.609 0.30 19.20  ? 147 SER A O   1 
ATOM   1481 O  O   D SER A 1 147 ? 16.217  -5.043  -22.609 0.30 19.20  ? 147 SER A O   1 
ATOM   1482 C  CB  A SER A 1 147 ? 15.841  -2.662  -20.342 0.20 18.39  ? 147 SER A CB  1 
ATOM   1483 C  CB  B SER A 1 147 ? 15.841  -2.662  -20.342 0.20 18.39  ? 147 SER A CB  1 
ATOM   1484 C  CB  C SER A 1 147 ? 15.822  -2.681  -20.426 0.30 21.83  ? 147 SER A CB  1 
ATOM   1485 C  CB  D SER A 1 147 ? 15.822  -2.681  -20.426 0.30 21.83  ? 147 SER A CB  1 
ATOM   1486 O  OG  A SER A 1 147 ? 16.360  -1.732  -19.395 0.20 18.21  ? 147 SER A OG  1 
ATOM   1487 O  OG  B SER A 1 147 ? 16.360  -1.732  -19.395 0.20 18.21  ? 147 SER A OG  1 
ATOM   1488 O  OG  C SER A 1 147 ? 16.321  -1.784  -19.434 0.30 21.73  ? 147 SER A OG  1 
ATOM   1489 O  OG  D SER A 1 147 ? 16.321  -1.784  -19.434 0.30 21.73  ? 147 SER A OG  1 
ATOM   1490 N  N   . VAL A 1 148 ? 15.372  -5.906  -20.714 1.00 18.71  ? 148 VAL A N   1 
ATOM   1491 C  CA  . VAL A 1 148 ? 14.833  -7.090  -21.431 1.00 19.64  ? 148 VAL A CA  1 
ATOM   1492 C  C   . VAL A 1 148 ? 13.328  -7.165  -21.333 1.00 18.94  ? 148 VAL A C   1 
ATOM   1493 O  O   . VAL A 1 148 ? 12.723  -6.601  -20.404 1.00 22.62  ? 148 VAL A O   1 
ATOM   1494 C  CB  . VAL A 1 148 ? 15.501  -8.400  -20.994 1.00 22.76  ? 148 VAL A CB  1 
ATOM   1495 C  CG1 . VAL A 1 148 ? 17.001  -8.335  -21.250 1.00 22.96  ? 148 VAL A CG1 1 
ATOM   1496 C  CG2 . VAL A 1 148 ? 15.172  -8.761  -19.552 1.00 22.25  ? 148 VAL A CG2 1 
ATOM   1497 N  N   . GLY A 1 149 ? 12.792  -7.838  -22.337 1.00 18.22  ? 149 GLY A N   1 
ATOM   1498 C  CA  . GLY A 1 149 ? 11.388  -8.194  -22.490 1.00 18.17  ? 149 GLY A CA  1 
ATOM   1499 C  C   . GLY A 1 149 ? 11.232  -9.669  -22.286 1.00 18.30  ? 149 GLY A C   1 
ATOM   1500 O  O   . GLY A 1 149 ? 12.101  -10.447 -22.732 1.00 19.22  ? 149 GLY A O   1 
ATOM   1501 N  N   . PHE A 1 150 ? 10.156  -10.082 -21.640 1.00 19.20  ? 150 PHE A N   1 
ATOM   1502 C  CA  . PHE A 1 150 ? 10.004  -11.505 -21.296 1.00 20.79  ? 150 PHE A CA  1 
ATOM   1503 C  C   . PHE A 1 150 ? 8.536   -11.872 -21.158 1.00 21.72  ? 150 PHE A C   1 
ATOM   1504 O  O   . PHE A 1 150 ? 7.676   -10.978 -20.956 1.00 20.70  ? 150 PHE A O   1 
ATOM   1505 C  CB  . PHE A 1 150 ? 10.754  -11.808 -19.996 1.00 23.34  ? 150 PHE A CB  1 
ATOM   1506 C  CG  . PHE A 1 150 ? 10.321  -10.952 -18.838 1.00 22.52  ? 150 PHE A CG  1 
ATOM   1507 C  CD1 . PHE A 1 150 ? 10.799  -9.658  -18.699 1.00 23.24  ? 150 PHE A CD1 1 
ATOM   1508 C  CD2 . PHE A 1 150 ? 9.442   -11.446 -17.890 1.00 23.17  ? 150 PHE A CD2 1 
ATOM   1509 C  CE1 . PHE A 1 150 ? 10.399  -8.862  -17.637 1.00 23.43  ? 150 PHE A CE1 1 
ATOM   1510 C  CE2 . PHE A 1 150 ? 9.034   -10.650 -16.833 1.00 23.87  ? 150 PHE A CE2 1 
ATOM   1511 C  CZ  . PHE A 1 150 ? 9.515   -9.359  -16.707 1.00 24.04  ? 150 PHE A CZ  1 
ATOM   1512 N  N   . ASN A 1 151 ? 8.293   -13.181 -21.252 1.00 22.63  ? 151 ASN A N   1 
ATOM   1513 C  CA  . ASN A 1 151 ? 7.063   -13.858 -20.787 1.00 23.20  ? 151 ASN A CA  1 
ATOM   1514 C  C   . ASN A 1 151 ? 7.467   -14.820 -19.653 1.00 25.82  ? 151 ASN A C   1 
ATOM   1515 O  O   . ASN A 1 151 ? 8.679   -15.200 -19.528 1.00 25.55  ? 151 ASN A O   1 
ATOM   1516 C  CB  . ASN A 1 151 ? 6.342   -14.522 -21.957 1.00 22.84  ? 151 ASN A CB  1 
ATOM   1517 C  CG  . ASN A 1 151 ? 5.662   -13.515 -22.864 1.00 26.08  ? 151 ASN A CG  1 
ATOM   1518 O  OD1 . ASN A 1 151 ? 4.596   -12.984 -22.555 1.00 25.25  ? 151 ASN A OD1 1 
ATOM   1519 N  ND2 . ASN A 1 151 ? 6.234   -13.281 -24.029 1.00 26.65  ? 151 ASN A ND2 1 
ATOM   1520 N  N   . ILE A 1 152 ? 6.504   -15.146 -18.802 1.00 25.42  ? 152 ILE A N   1 
ATOM   1521 C  CA  . ILE A 1 152 ? 6.654   -16.176 -17.746 1.00 29.65  ? 152 ILE A CA  1 
ATOM   1522 C  C   . ILE A 1 152 ? 5.456   -17.104 -17.896 1.00 34.31  ? 152 ILE A C   1 
ATOM   1523 O  O   . ILE A 1 152 ? 4.342   -16.660 -17.655 1.00 36.63  ? 152 ILE A O   1 
ATOM   1524 C  CB  . ILE A 1 152 ? 6.771   -15.571 -16.340 1.00 28.43  ? 152 ILE A CB  1 
ATOM   1525 C  CG1 . ILE A 1 152 ? 7.865   -14.502 -16.281 1.00 27.17  ? 152 ILE A CG1 1 
ATOM   1526 C  CG2 . ILE A 1 152 ? 6.996   -16.687 -15.335 1.00 29.12  ? 152 ILE A CG2 1 
ATOM   1527 C  CD1 . ILE A 1 152 ? 8.265   -14.093 -14.897 1.00 27.93  ? 152 ILE A CD1 1 
ATOM   1528 N  N   . ASP A 1 153 ? 5.702   -18.301 -18.400 1.00 41.54  ? 153 ASP A N   1 
ATOM   1529 C  CA  . ASP A 1 153 ? 4.660   -19.324 -18.611 1.00 50.80  ? 153 ASP A CA  1 
ATOM   1530 C  C   . ASP A 1 153 ? 5.094   -20.486 -17.720 1.00 53.70  ? 153 ASP A C   1 
ATOM   1531 O  O   . ASP A 1 153 ? 6.228   -20.965 -17.895 1.00 59.92  ? 153 ASP A O   1 
ATOM   1532 C  CB  . ASP A 1 153 ? 4.416   -19.541 -20.113 1.00 56.28  ? 153 ASP A CB  1 
ATOM   1533 C  CG  . ASP A 1 153 ? 3.455   -18.517 -20.725 1.00 66.31  ? 153 ASP A CG  1 
ATOM   1534 O  OD1 . ASP A 1 153 ? 2.433   -18.211 -20.085 1.00 75.60  ? 153 ASP A OD1 1 
ATOM   1535 O  OD2 . ASP A 1 153 ? 3.738   -18.004 -21.827 1.00 76.55  ? 153 ASP A OD2 1 
ATOM   1536 N  N   . TYR A 1 154 ? 4.280   -20.787 -16.701 1.00 61.65  ? 154 TYR A N   1 
ATOM   1537 C  CA  . TYR A 1 154 ? 4.368   -21.993 -15.834 1.00 67.35  ? 154 TYR A CA  1 
ATOM   1538 C  C   . TYR A 1 154 ? 5.756   -22.020 -15.159 1.00 65.06  ? 154 TYR A C   1 
ATOM   1539 O  O   . TYR A 1 154 ? 6.410   -23.078 -15.176 1.00 64.83  ? 154 TYR A O   1 
ATOM   1540 C  CB  . TYR A 1 154 ? 4.036   -23.261 -16.653 1.00 78.53  ? 154 TYR A CB  1 
ATOM   1541 C  CG  . TYR A 1 154 ? 3.010   -23.118 -17.763 1.00 89.87  ? 154 TYR A CG  1 
ATOM   1542 C  CD1 . TYR A 1 154 ? 1.645   -23.230 -17.523 1.00 89.98  ? 154 TYR A CD1 1 
ATOM   1543 C  CD2 . TYR A 1 154 ? 3.407   -22.894 -19.078 1.00 99.69  ? 154 TYR A CD2 1 
ATOM   1544 C  CE1 . TYR A 1 154 ? 0.714   -23.091 -18.546 1.00 98.98  ? 154 TYR A CE1 1 
ATOM   1545 C  CE2 . TYR A 1 154 ? 2.490   -22.749 -20.110 1.00 104.89 ? 154 TYR A CE2 1 
ATOM   1546 C  CZ  . TYR A 1 154 ? 1.136   -22.848 -19.845 1.00 103.48 ? 154 TYR A CZ  1 
ATOM   1547 O  OH  . TYR A 1 154 ? 0.245   -22.703 -20.869 1.00 100.92 ? 154 TYR A OH  1 
ATOM   1548 N  N   . ASP A 1 155 ? 6.215   -20.884 -14.606 1.00 59.52  ? 155 ASP A N   1 
ATOM   1549 C  CA  . ASP A 1 155 ? 7.495   -20.733 -13.839 1.00 55.26  ? 155 ASP A CA  1 
ATOM   1550 C  C   . ASP A 1 155 ? 8.740   -20.630 -14.740 1.00 47.23  ? 155 ASP A C   1 
ATOM   1551 O  O   . ASP A 1 155 ? 9.832   -20.413 -14.203 1.00 43.08  ? 155 ASP A O   1 
ATOM   1552 C  CB  . ASP A 1 155 ? 7.745   -21.893 -12.869 1.00 63.55  ? 155 ASP A CB  1 
ATOM   1553 C  CG  . ASP A 1 155 ? 7.394   -21.588 -11.420 1.00 76.11  ? 155 ASP A CG  1 
ATOM   1554 O  OD1 . ASP A 1 155 ? 7.531   -20.408 -11.008 1.00 77.61  ? 155 ASP A OD1 1 
ATOM   1555 O  OD2 . ASP A 1 155 ? 6.983   -22.540 -10.706 1.00 82.04  ? 155 ASP A OD2 1 
ATOM   1556 N  N   . CYS A 1 156 ? 8.621   -20.819 -16.055 1.00 43.97  ? 156 CYS A N   1 
ATOM   1557 C  CA  . CYS A 1 156 ? 9.762   -20.689 -16.999 1.00 38.68  ? 156 CYS A CA  1 
ATOM   1558 C  C   . CYS A 1 156 ? 9.794   -19.268 -17.583 1.00 31.54  ? 156 CYS A C   1 
ATOM   1559 O  O   . CYS A 1 156 ? 8.767   -18.850 -18.149 1.00 26.39  ? 156 CYS A O   1 
ATOM   1560 C  CB  . CYS A 1 156 ? 9.643   -21.703 -18.125 1.00 37.00  ? 156 CYS A CB  1 
ATOM   1561 S  SG  . CYS A 1 156 ? 11.030  -21.589 -19.284 1.00 38.54  ? 156 CYS A SG  1 
ATOM   1562 N  N   . VAL A 1 157 ? 10.914  -18.557 -17.450 1.00 27.57  ? 157 VAL A N   1 
ATOM   1563 C  CA  . VAL A 1 157 ? 11.054  -17.188 -18.021 1.00 26.06  ? 157 VAL A CA  1 
ATOM   1564 C  C   . VAL A 1 157 ? 11.515  -17.300 -19.476 1.00 26.02  ? 157 VAL A C   1 
ATOM   1565 O  O   . VAL A 1 157 ? 12.637  -17.796 -19.712 1.00 26.20  ? 157 VAL A O   1 
ATOM   1566 C  CB  . VAL A 1 157 ? 12.023  -16.306 -17.223 1.00 25.68  ? 157 VAL A CB  1 
ATOM   1567 C  CG1 . VAL A 1 157 ? 12.102  -14.907 -17.827 1.00 25.52  ? 157 VAL A CG1 1 
ATOM   1568 C  CG2 . VAL A 1 157 ? 11.658  -16.244 -15.753 1.00 25.21  ? 157 VAL A CG2 1 
ATOM   1569 N  N   . SER A 1 158 ? 10.701  -16.817 -20.412 1.00 22.80  ? 158 SER A N   1 
ATOM   1570 C  CA  . SER A 1 158 ? 11.030  -16.851 -21.845 1.00 24.88  ? 158 SER A CA  1 
ATOM   1571 C  C   . SER A 1 158 ? 11.446  -15.432 -22.268 1.00 25.16  ? 158 SER A C   1 
ATOM   1572 O  O   . SER A 1 158 ? 10.571  -14.498 -22.302 1.00 22.45  ? 158 SER A O   1 
ATOM   1573 C  CB  . SER A 1 158 ? 9.917   -17.464 -22.625 1.00 26.24  ? 158 SER A CB  1 
ATOM   1574 O  OG  . SER A 1 158 ? 9.073   -16.498 -23.205 1.00 38.11  ? 158 SER A OG  1 
ATOM   1575 N  N   . PHE A 1 159 ? 12.758  -15.231 -22.425 1.00 23.39  ? 159 PHE A N   1 
ATOM   1576 C  CA  . PHE A 1 159 ? 13.352  -13.926 -22.811 1.00 22.61  ? 159 PHE A CA  1 
ATOM   1577 C  C   . PHE A 1 159 ? 13.221  -13.731 -24.317 1.00 22.53  ? 159 PHE A C   1 
ATOM   1578 O  O   . PHE A 1 159 ? 13.644  -14.616 -25.105 1.00 26.31  ? 159 PHE A O   1 
ATOM   1579 C  CB  . PHE A 1 159 ? 14.809  -13.862 -22.401 1.00 24.03  ? 159 PHE A CB  1 
ATOM   1580 C  CG  . PHE A 1 159 ? 15.041  -13.831 -20.921 1.00 25.00  ? 159 PHE A CG  1 
ATOM   1581 C  CD1 . PHE A 1 159 ? 14.813  -12.671 -20.194 1.00 24.30  ? 159 PHE A CD1 1 
ATOM   1582 C  CD2 . PHE A 1 159 ? 15.509  -14.953 -20.264 1.00 25.03  ? 159 PHE A CD2 1 
ATOM   1583 C  CE1 . PHE A 1 159 ? 15.058  -12.636 -18.831 1.00 23.70  ? 159 PHE A CE1 1 
ATOM   1584 C  CE2 . PHE A 1 159 ? 15.752  -14.914 -18.904 1.00 26.41  ? 159 PHE A CE2 1 
ATOM   1585 C  CZ  . PHE A 1 159 ? 15.557  -13.748 -18.193 1.00 25.77  ? 159 PHE A CZ  1 
ATOM   1586 N  N   . CYS A 1 160 ? 12.617  -12.625 -24.742 1.00 21.43  ? 160 CYS A N   1 
ATOM   1587 C  CA  . CYS A 1 160 ? 12.288  -12.452 -26.171 1.00 21.61  ? 160 CYS A CA  1 
ATOM   1588 C  C   . CYS A 1 160 ? 12.791  -11.128 -26.737 1.00 21.41  ? 160 CYS A C   1 
ATOM   1589 O  O   . CYS A 1 160 ? 12.661  -10.976 -27.963 1.00 23.20  ? 160 CYS A O   1 
ATOM   1590 C  CB  . CYS A 1 160 ? 10.790  -12.569 -26.393 1.00 23.73  ? 160 CYS A CB  1 
ATOM   1591 S  SG  . CYS A 1 160 ? 9.854   -11.353 -25.430 1.00 25.25  ? 160 CYS A SG  1 
ATOM   1592 N  N   . TYR A 1 161 ? 13.345  -10.232 -25.913 1.00 20.28  ? 161 TYR A N   1 
ATOM   1593 C  CA  . TYR A 1 161 ? 13.743  -8.872  -26.334 1.00 19.92  ? 161 TYR A CA  1 
ATOM   1594 C  C   . TYR A 1 161 ? 14.863  -8.343  -25.435 1.00 18.49  ? 161 TYR A C   1 
ATOM   1595 O  O   . TYR A 1 161 ? 14.812  -8.488  -24.210 1.00 18.58  ? 161 TYR A O   1 
ATOM   1596 C  CB  . TYR A 1 161 ? 12.519  -7.936  -26.332 1.00 19.73  ? 161 TYR A CB  1 
ATOM   1597 C  CG  . TYR A 1 161 ? 12.793  -6.515  -26.753 1.00 17.72  ? 161 TYR A CG  1 
ATOM   1598 C  CD1 . TYR A 1 161 ? 12.759  -6.138  -28.077 1.00 19.02  ? 161 TYR A CD1 1 
ATOM   1599 C  CD2 . TYR A 1 161 ? 13.142  -5.550  -25.833 1.00 19.72  ? 161 TYR A CD2 1 
ATOM   1600 C  CE1 . TYR A 1 161 ? 13.040  -4.843  -28.480 1.00 17.63  ? 161 TYR A CE1 1 
ATOM   1601 C  CE2 . TYR A 1 161 ? 13.386  -4.233  -26.213 1.00 19.24  ? 161 TYR A CE2 1 
ATOM   1602 C  CZ  . TYR A 1 161 ? 13.354  -3.880  -27.547 1.00 19.77  ? 161 TYR A CZ  1 
ATOM   1603 O  OH  . TYR A 1 161 ? 13.625  -2.585  -27.952 1.00 23.14  ? 161 TYR A OH  1 
ATOM   1604 N  N   . MET A 1 162 ? 15.855  -7.706  -26.052 1.00 19.45  ? 162 MET A N   1 
ATOM   1605 C  CA  . MET A 1 162 ? 16.862  -6.875  -25.348 1.00 20.37  ? 162 MET A CA  1 
ATOM   1606 C  C   . MET A 1 162 ? 16.843  -5.537  -26.074 1.00 19.63  ? 162 MET A C   1 
ATOM   1607 O  O   . MET A 1 162 ? 16.876  -5.523  -27.287 1.00 19.41  ? 162 MET A O   1 
ATOM   1608 C  CB  . MET A 1 162 ? 18.271  -7.467  -25.406 1.00 21.78  ? 162 MET A CB  1 
ATOM   1609 C  CG  . MET A 1 162 ? 19.294  -6.624  -24.660 1.00 23.24  ? 162 MET A CG  1 
ATOM   1610 S  SD  . MET A 1 162 ? 20.937  -7.386  -24.568 1.00 26.48  ? 162 MET A SD  1 
ATOM   1611 C  CE  . MET A 1 162 ? 20.790  -8.299  -23.033 1.00 28.11  ? 162 MET A CE  1 
ATOM   1612 N  N   A HIS A 1 163 ? 16.820  -4.443  -25.317 0.20 19.68  ? 163 HIS A N   1 
ATOM   1613 N  N   B HIS A 1 163 ? 16.820  -4.443  -25.317 0.20 19.68  ? 163 HIS A N   1 
ATOM   1614 N  N   C HIS A 1 163 ? 16.775  -4.447  -25.314 0.30 20.35  ? 163 HIS A N   1 
ATOM   1615 N  N   D HIS A 1 163 ? 16.775  -4.447  -25.314 0.30 20.35  ? 163 HIS A N   1 
ATOM   1616 C  CA  A HIS A 1 163 ? 16.664  -3.063  -25.845 0.20 19.96  ? 163 HIS A CA  1 
ATOM   1617 C  CA  B HIS A 1 163 ? 16.663  -3.063  -25.845 0.20 19.96  ? 163 HIS A CA  1 
ATOM   1618 C  CA  C HIS A 1 163 ? 16.658  -3.055  -25.822 0.30 21.18  ? 163 HIS A CA  1 
ATOM   1619 C  CA  D HIS A 1 163 ? 16.658  -3.055  -25.822 0.30 21.18  ? 163 HIS A CA  1 
ATOM   1620 C  C   A HIS A 1 163 ? 18.027  -2.526  -26.291 0.20 19.83  ? 163 HIS A C   1 
ATOM   1621 C  C   B HIS A 1 163 ? 18.027  -2.526  -26.291 0.20 19.83  ? 163 HIS A C   1 
ATOM   1622 C  C   C HIS A 1 163 ? 18.037  -2.577  -26.280 0.30 20.98  ? 163 HIS A C   1 
ATOM   1623 C  C   D HIS A 1 163 ? 18.037  -2.577  -26.280 0.30 20.98  ? 163 HIS A C   1 
ATOM   1624 O  O   A HIS A 1 163 ? 18.965  -2.549  -25.468 0.20 19.96  ? 163 HIS A O   1 
ATOM   1625 O  O   B HIS A 1 163 ? 18.965  -2.549  -25.468 0.20 19.96  ? 163 HIS A O   1 
ATOM   1626 O  O   C HIS A 1 163 ? 18.992  -2.735  -25.501 0.30 21.13  ? 163 HIS A O   1 
ATOM   1627 O  O   D HIS A 1 163 ? 18.992  -2.735  -25.501 0.30 21.13  ? 163 HIS A O   1 
ATOM   1628 C  CB  A HIS A 1 163 ? 16.000  -2.155  -24.806 0.20 19.58  ? 163 HIS A CB  1 
ATOM   1629 C  CB  B HIS A 1 163 ? 16.000  -2.155  -24.806 0.20 19.58  ? 163 HIS A CB  1 
ATOM   1630 C  CB  C HIS A 1 163 ? 16.055  -2.138  -24.748 0.30 20.97  ? 163 HIS A CB  1 
ATOM   1631 C  CB  D HIS A 1 163 ? 16.055  -2.138  -24.748 0.30 20.97  ? 163 HIS A CB  1 
ATOM   1632 C  CG  A HIS A 1 163 ? 15.889  -0.747  -25.276 0.20 19.74  ? 163 HIS A CG  1 
ATOM   1633 C  CG  B HIS A 1 163 ? 15.889  -0.747  -25.276 0.20 19.74  ? 163 HIS A CG  1 
ATOM   1634 C  CG  C HIS A 1 163 ? 15.992  -0.704  -25.152 0.30 21.62  ? 163 HIS A CG  1 
ATOM   1635 C  CG  D HIS A 1 163 ? 15.992  -0.704  -25.152 0.30 21.62  ? 163 HIS A CG  1 
ATOM   1636 N  ND1 A HIS A 1 163 ? 15.043  -0.376  -26.302 0.20 19.41  ? 163 HIS A ND1 1 
ATOM   1637 N  ND1 B HIS A 1 163 ? 15.043  -0.376  -26.302 0.20 19.41  ? 163 HIS A ND1 1 
ATOM   1638 N  ND1 C HIS A 1 163 ? 15.316  -0.281  -26.280 0.30 21.48  ? 163 HIS A ND1 1 
ATOM   1639 N  ND1 D HIS A 1 163 ? 15.316  -0.281  -26.280 0.30 21.48  ? 163 HIS A ND1 1 
ATOM   1640 C  CD2 A HIS A 1 163 ? 16.534  0.373   -24.889 0.20 20.20  ? 163 HIS A CD2 1 
ATOM   1641 C  CD2 B HIS A 1 163 ? 16.534  0.373   -24.889 0.20 20.20  ? 163 HIS A CD2 1 
ATOM   1642 C  CD2 C HIS A 1 163 ? 16.501  0.407   -24.576 0.30 22.71  ? 163 HIS A CD2 1 
ATOM   1643 C  CD2 D HIS A 1 163 ? 16.501  0.407   -24.575 0.30 22.71  ? 163 HIS A CD2 1 
ATOM   1644 C  CE1 A HIS A 1 163 ? 15.166  0.921   -26.512 0.20 19.89  ? 163 HIS A CE1 1 
ATOM   1645 C  CE1 B HIS A 1 163 ? 15.165  0.921   -26.512 0.20 19.89  ? 163 HIS A CE1 1 
ATOM   1646 C  CE1 C HIS A 1 163 ? 15.429  1.031   -26.386 0.30 21.89  ? 163 HIS A CE1 1 
ATOM   1647 C  CE1 D HIS A 1 163 ? 15.429  1.031   -26.386 0.30 21.89  ? 163 HIS A CE1 1 
ATOM   1648 N  NE2 A HIS A 1 163 ? 16.072  1.402   -25.663 0.20 19.80  ? 163 HIS A NE2 1 
ATOM   1649 N  NE2 B HIS A 1 163 ? 16.072  1.402   -25.663 0.20 19.80  ? 163 HIS A NE2 1 
ATOM   1650 N  NE2 C HIS A 1 163 ? 16.145  1.476   -25.356 0.30 22.48  ? 163 HIS A NE2 1 
ATOM   1651 N  NE2 D HIS A 1 163 ? 16.145  1.476   -25.356 0.30 22.48  ? 163 HIS A NE2 1 
ATOM   1652 N  N   A HIS A 1 164 ? 18.120  -2.053  -27.541 0.20 19.95  ? 164 HIS A N   1 
ATOM   1653 N  N   B HIS A 1 164 ? 18.120  -2.053  -27.541 0.20 19.95  ? 164 HIS A N   1 
ATOM   1654 N  N   C HIS A 1 164 ? 18.132  -2.027  -27.497 0.30 21.25  ? 164 HIS A N   1 
ATOM   1655 N  N   D HIS A 1 164 ? 18.132  -2.027  -27.497 0.30 21.25  ? 164 HIS A N   1 
ATOM   1656 C  CA  A HIS A 1 164 ? 19.371  -1.536  -28.158 0.20 20.39  ? 164 HIS A CA  1 
ATOM   1657 C  CA  B HIS A 1 164 ? 19.371  -1.536  -28.158 0.20 20.39  ? 164 HIS A CA  1 
ATOM   1658 C  CA  C HIS A 1 164 ? 19.388  -1.471  -28.069 0.30 21.90  ? 164 HIS A CA  1 
ATOM   1659 C  CA  D HIS A 1 164 ? 19.389  -1.471  -28.069 0.30 21.90  ? 164 HIS A CA  1 
ATOM   1660 C  C   A HIS A 1 164 ? 19.295  -0.024  -28.404 0.20 21.27  ? 164 HIS A C   1 
ATOM   1661 C  C   B HIS A 1 164 ? 19.295  -0.024  -28.404 0.20 21.27  ? 164 HIS A C   1 
ATOM   1662 C  C   C HIS A 1 164 ? 19.264  0.045   -28.285 0.30 22.77  ? 164 HIS A C   1 
ATOM   1663 C  C   D HIS A 1 164 ? 19.264  0.045   -28.285 0.30 22.77  ? 164 HIS A C   1 
ATOM   1664 O  O   A HIS A 1 164 ? 20.332  0.635   -28.209 0.20 21.50  ? 164 HIS A O   1 
ATOM   1665 O  O   B HIS A 1 164 ? 20.332  0.635   -28.209 0.20 21.50  ? 164 HIS A O   1 
ATOM   1666 O  O   C HIS A 1 164 ? 20.173  0.768   -27.830 0.30 22.95  ? 164 HIS A O   1 
ATOM   1667 O  O   D HIS A 1 164 ? 20.173  0.768   -27.830 0.30 22.95  ? 164 HIS A O   1 
ATOM   1668 C  CB  A HIS A 1 164 ? 19.706  -2.302  -29.445 0.20 20.21  ? 164 HIS A CB  1 
ATOM   1669 C  CB  B HIS A 1 164 ? 19.706  -2.302  -29.445 0.20 20.21  ? 164 HIS A CB  1 
ATOM   1670 C  CB  C HIS A 1 164 ? 19.788  -2.223  -29.347 0.30 22.09  ? 164 HIS A CB  1 
ATOM   1671 C  CB  D HIS A 1 164 ? 19.788  -2.223  -29.347 0.30 22.09  ? 164 HIS A CB  1 
ATOM   1672 C  CG  A HIS A 1 164 ? 20.237  -3.676  -29.205 0.20 19.95  ? 164 HIS A CG  1 
ATOM   1673 C  CG  B HIS A 1 164 ? 20.237  -3.676  -29.205 0.20 19.95  ? 164 HIS A CG  1 
ATOM   1674 C  CG  C HIS A 1 164 ? 20.337  -3.597  -29.125 0.30 22.16  ? 164 HIS A CG  1 
ATOM   1675 C  CG  D HIS A 1 164 ? 20.337  -3.597  -29.126 0.30 22.16  ? 164 HIS A CG  1 
ATOM   1676 N  ND1 A HIS A 1 164 ? 21.583  -3.983  -29.315 0.20 19.89  ? 164 HIS A ND1 1 
ATOM   1677 N  ND1 B HIS A 1 164 ? 21.583  -3.983  -29.315 0.20 19.89  ? 164 HIS A ND1 1 
ATOM   1678 N  ND1 C HIS A 1 164 ? 21.509  -4.030  -29.726 0.30 22.32  ? 164 HIS A ND1 1 
ATOM   1679 N  ND1 D HIS A 1 164 ? 21.509  -4.030  -29.726 0.30 22.32  ? 164 HIS A ND1 1 
ATOM   1680 C  CD2 A HIS A 1 164 ? 19.614  -4.823  -28.861 0.20 19.60  ? 164 HIS A CD2 1 
ATOM   1681 C  CD2 B HIS A 1 164 ? 19.614  -4.823  -28.861 0.20 19.60  ? 164 HIS A CD2 1 
ATOM   1682 C  CD2 C HIS A 1 164 ? 19.883  -4.642  -28.397 0.30 21.97  ? 164 HIS A CD2 1 
ATOM   1683 C  CD2 D HIS A 1 164 ? 19.883  -4.642  -28.397 0.30 21.97  ? 164 HIS A CD2 1 
ATOM   1684 C  CE1 A HIS A 1 164 ? 21.757  -5.265  -29.048 0.20 19.77  ? 164 HIS A CE1 1 
ATOM   1685 C  CE1 B HIS A 1 164 ? 21.757  -5.265  -29.048 0.20 19.77  ? 164 HIS A CE1 1 
ATOM   1686 C  CE1 C HIS A 1 164 ? 21.742  -5.282  -29.376 0.30 22.44  ? 164 HIS A CE1 1 
ATOM   1687 C  CE1 D HIS A 1 164 ? 21.742  -5.282  -29.376 0.30 22.44  ? 164 HIS A CE1 1 
ATOM   1688 N  NE2 A HIS A 1 164 ? 20.566  -5.803  -28.771 0.20 19.18  ? 164 HIS A NE2 1 
ATOM   1689 N  NE2 B HIS A 1 164 ? 20.566  -5.803  -28.771 0.20 19.18  ? 164 HIS A NE2 1 
ATOM   1690 N  NE2 C HIS A 1 164 ? 20.764  -5.681  -28.560 0.30 21.32  ? 164 HIS A NE2 1 
ATOM   1691 N  NE2 D HIS A 1 164 ? 20.764  -5.681  -28.560 0.30 21.32  ? 164 HIS A NE2 1 
ATOM   1692 N  N   A MET A 1 165 ? 18.154  0.528   -28.828 0.20 22.52  ? 165 MET A N   1 
ATOM   1693 N  N   B MET A 1 165 ? 18.154  0.528   -28.828 0.20 22.52  ? 165 MET A N   1 
ATOM   1694 N  N   C MET A 1 165 ? 18.199  0.534   -28.930 0.30 23.94  ? 165 MET A N   1 
ATOM   1695 N  N   D MET A 1 165 ? 18.199  0.534   -28.930 0.30 23.94  ? 165 MET A N   1 
ATOM   1696 C  CA  A MET A 1 165 ? 18.137  1.948   -29.279 0.20 23.93  ? 165 MET A CA  1 
ATOM   1697 C  CA  B MET A 1 165 ? 18.137  1.948   -29.279 0.20 23.93  ? 165 MET A CA  1 
ATOM   1698 C  CA  C MET A 1 165 ? 18.169  1.950   -29.402 0.30 25.29  ? 165 MET A CA  1 
ATOM   1699 C  CA  D MET A 1 165 ? 18.169  1.950   -29.402 0.30 25.29  ? 165 MET A CA  1 
ATOM   1700 C  C   A MET A 1 165 ? 16.726  2.524   -29.438 0.20 24.16  ? 165 MET A C   1 
ATOM   1701 C  C   B MET A 1 165 ? 16.726  2.524   -29.438 0.20 24.16  ? 165 MET A C   1 
ATOM   1702 C  C   C MET A 1 165 ? 16.748  2.525   -29.519 0.30 24.79  ? 165 MET A C   1 
ATOM   1703 C  C   D MET A 1 165 ? 16.748  2.525   -29.519 0.30 24.79  ? 165 MET A C   1 
ATOM   1704 O  O   A MET A 1 165 ? 15.746  1.759   -29.548 0.20 23.31  ? 165 MET A O   1 
ATOM   1705 O  O   B MET A 1 165 ? 15.746  1.759   -29.548 0.20 23.31  ? 165 MET A O   1 
ATOM   1706 O  O   C MET A 1 165 ? 15.774  1.759   -29.668 0.30 23.49  ? 165 MET A O   1 
ATOM   1707 O  O   D MET A 1 165 ? 15.774  1.759   -29.668 0.30 23.49  ? 165 MET A O   1 
ATOM   1708 C  CB  A MET A 1 165 ? 18.867  2.081   -30.618 0.20 24.59  ? 165 MET A CB  1 
ATOM   1709 C  CB  B MET A 1 165 ? 18.867  2.081   -30.618 0.20 24.59  ? 165 MET A CB  1 
ATOM   1710 C  CB  C MET A 1 165 ? 18.870  2.070   -30.758 0.30 26.50  ? 165 MET A CB  1 
ATOM   1711 C  CB  D MET A 1 165 ? 18.870  2.070   -30.758 0.30 26.50  ? 165 MET A CB  1 
ATOM   1712 C  CG  A MET A 1 165 ? 18.357  1.136   -31.687 0.20 25.81  ? 165 MET A CG  1 
ATOM   1713 C  CG  B MET A 1 165 ? 18.357  1.136   -31.687 0.20 25.81  ? 165 MET A CG  1 
ATOM   1714 C  CG  C MET A 1 165 ? 18.557  0.936   -31.717 0.30 28.68  ? 165 MET A CG  1 
ATOM   1715 C  CG  D MET A 1 165 ? 18.557  0.936   -31.717 0.30 28.68  ? 165 MET A CG  1 
ATOM   1716 S  SD  A MET A 1 165 ? 19.416  1.195   -33.154 0.20 28.88  ? 165 MET A SD  1 
ATOM   1717 S  SD  B MET A 1 165 ? 19.416  1.195   -33.154 0.20 28.88  ? 165 MET A SD  1 
ATOM   1718 S  SD  C MET A 1 165 ? 19.348  1.212   -33.325 0.30 33.13  ? 165 MET A SD  1 
ATOM   1719 S  SD  D MET A 1 165 ? 19.348  1.212   -33.325 0.30 33.13  ? 165 MET A SD  1 
ATOM   1720 C  CE  A MET A 1 165 ? 18.512  0.118   -34.262 0.20 28.67  ? 165 MET A CE  1 
ATOM   1721 C  CE  B MET A 1 165 ? 18.512  0.118   -34.262 0.20 28.67  ? 165 MET A CE  1 
ATOM   1722 C  CE  C MET A 1 165 ? 18.473  0.030   -34.346 0.30 33.18  ? 165 MET A CE  1 
ATOM   1723 C  CE  D MET A 1 165 ? 18.473  0.030   -34.346 0.30 33.18  ? 165 MET A CE  1 
ATOM   1724 N  N   . GLU A 1 166 ? 16.664  3.859   -29.466 1.00 25.35  ? 166 GLU A N   1 
ATOM   1725 C  CA  . GLU A 1 166 ? 15.433  4.635   -29.758 1.00 26.29  ? 166 GLU A CA  1 
ATOM   1726 C  C   . GLU A 1 166 ? 15.578  5.262   -31.148 1.00 26.39  ? 166 GLU A C   1 
ATOM   1727 O  O   . GLU A 1 166 ? 16.614  5.920   -31.409 1.00 28.74  ? 166 GLU A O   1 
ATOM   1728 C  CB  . GLU A 1 166 ? 15.222  5.725   -28.731 1.00 26.20  ? 166 GLU A CB  1 
ATOM   1729 C  CG  . GLU A 1 166 ? 13.905  6.454   -28.972 1.00 29.36  ? 166 GLU A CG  1 
ATOM   1730 C  CD  . GLU A 1 166 ? 13.463  7.332   -27.813 1.00 30.82  ? 166 GLU A CD  1 
ATOM   1731 O  OE1 . GLU A 1 166 ? 13.267  6.812   -26.680 1.00 29.72  ? 166 GLU A OE1 1 
ATOM   1732 O  OE2 . GLU A 1 166 ? 13.367  8.535   -28.031 1.00 34.53  ? 166 GLU A OE2 1 
ATOM   1733 N  N   . LEU A 1 167 ? 14.602  5.030   -32.018 1.00 26.07  ? 167 LEU A N   1 
ATOM   1734 C  CA  . LEU A 1 167 ? 14.578  5.585   -33.395 1.00 29.64  ? 167 LEU A CA  1 
ATOM   1735 C  C   . LEU A 1 167 ? 14.077  7.014   -33.318 1.00 29.16  ? 167 LEU A C   1 
ATOM   1736 O  O   . LEU A 1 167 ? 13.515  7.388   -32.300 1.00 29.05  ? 167 LEU A O   1 
ATOM   1737 C  CB  . LEU A 1 167 ? 13.686  4.696   -34.267 1.00 29.40  ? 167 LEU A CB  1 
ATOM   1738 C  CG  . LEU A 1 167 ? 14.205  3.270   -34.452 1.00 29.05  ? 167 LEU A CG  1 
ATOM   1739 C  CD1 . LEU A 1 167 ? 13.090  2.333   -34.872 1.00 33.77  ? 167 LEU A CD1 1 
ATOM   1740 C  CD2 . LEU A 1 167 ? 15.325  3.223   -35.461 1.00 28.71  ? 167 LEU A CD2 1 
ATOM   1741 N  N   . PRO A 1 168 ? 14.249  7.846   -34.368 1.00 33.62  ? 168 PRO A N   1 
ATOM   1742 C  CA  . PRO A 1 168 ? 13.850  9.260   -34.320 1.00 34.53  ? 168 PRO A CA  1 
ATOM   1743 C  C   . PRO A 1 168 ? 12.370  9.527   -34.052 1.00 34.31  ? 168 PRO A C   1 
ATOM   1744 O  O   . PRO A 1 168 ? 12.095  10.587  -33.579 1.00 35.85  ? 168 PRO A O   1 
ATOM   1745 C  CB  . PRO A 1 168 ? 14.198  9.817   -35.711 1.00 35.40  ? 168 PRO A CB  1 
ATOM   1746 C  CG  . PRO A 1 168 ? 15.286  8.858   -36.207 1.00 37.09  ? 168 PRO A CG  1 
ATOM   1747 C  CD  . PRO A 1 168 ? 14.864  7.502   -35.655 1.00 36.59  ? 168 PRO A CD  1 
ATOM   1748 N  N   . THR A 1 169 ? 11.470  8.584   -34.325 1.00 32.04  ? 169 THR A N   1 
ATOM   1749 C  CA  . THR A 1 169 ? 10.024  8.761   -34.034 1.00 32.39  ? 169 THR A CA  1 
ATOM   1750 C  C   . THR A 1 169 ? 9.689   8.464   -32.569 1.00 31.87  ? 169 THR A C   1 
ATOM   1751 O  O   . THR A 1 169 ? 8.492   8.480   -32.248 1.00 31.57  ? 169 THR A O   1 
ATOM   1752 C  CB  . THR A 1 169 ? 9.183   7.886   -34.965 1.00 34.85  ? 169 THR A CB  1 
ATOM   1753 O  OG1 . THR A 1 169 ? 9.701   6.564   -34.863 1.00 35.63  ? 169 THR A OG1 1 
ATOM   1754 C  CG2 . THR A 1 169 ? 9.246   8.367   -36.398 1.00 34.81  ? 169 THR A CG2 1 
ATOM   1755 N  N   . GLY A 1 170 ? 10.662  8.139   -31.717 1.00 28.89  ? 170 GLY A N   1 
ATOM   1756 C  CA  . GLY A 1 170 ? 10.401  7.897   -30.284 1.00 30.43  ? 170 GLY A CA  1 
ATOM   1757 C  C   . GLY A 1 170 ? 9.985   6.460   -29.969 1.00 30.19  ? 170 GLY A C   1 
ATOM   1758 O  O   . GLY A 1 170 ? 9.576   6.219   -28.800 1.00 31.27  ? 170 GLY A O   1 
ATOM   1759 N  N   . VAL A 1 171 ? 10.079  5.547   -30.944 1.00 28.74  ? 171 VAL A N   1 
ATOM   1760 C  CA  . VAL A 1 171 ? 9.831   4.088   -30.739 1.00 28.24  ? 171 VAL A CA  1 
ATOM   1761 C  C   . VAL A 1 171 ? 11.185  3.357   -30.640 1.00 26.40  ? 171 VAL A C   1 
ATOM   1762 O  O   . VAL A 1 171 ? 12.248  3.928   -30.963 1.00 24.71  ? 171 VAL A O   1 
ATOM   1763 C  CB  . VAL A 1 171 ? 8.936   3.487   -31.843 1.00 28.33  ? 171 VAL A CB  1 
ATOM   1764 C  CG1 . VAL A 1 171 ? 7.588   4.186   -31.911 1.00 30.39  ? 171 VAL A CG1 1 
ATOM   1765 C  CG2 . VAL A 1 171 ? 9.604   3.492   -33.205 1.00 28.78  ? 171 VAL A CG2 1 
ATOM   1766 N  N   . HIS A 1 172 ? 11.143  2.099   -30.232 1.00 24.75  ? 172 HIS A N   1 
ATOM   1767 C  CA  . HIS A 1 172 ? 12.319  1.370   -29.700 1.00 22.06  ? 172 HIS A CA  1 
ATOM   1768 C  C   . HIS A 1 172 ? 12.599  0.133   -30.538 1.00 21.54  ? 172 HIS A C   1 
ATOM   1769 O  O   . HIS A 1 172 ? 11.635  -0.494  -31.042 1.00 19.01  ? 172 HIS A O   1 
ATOM   1770 C  CB  . HIS A 1 172 ? 12.067  1.094   -28.233 1.00 22.30  ? 172 HIS A CB  1 
ATOM   1771 C  CG  . HIS A 1 172 ? 11.861  2.374   -27.491 1.00 23.68  ? 172 HIS A CG  1 
ATOM   1772 N  ND1 . HIS A 1 172 ? 10.644  2.711   -26.945 1.00 21.78  ? 172 HIS A ND1 1 
ATOM   1773 C  CD2 . HIS A 1 172 ? 12.682  3.426   -27.275 1.00 23.08  ? 172 HIS A CD2 1 
ATOM   1774 C  CE1 . HIS A 1 172 ? 10.742  3.888   -26.372 1.00 24.11  ? 172 HIS A CE1 1 
ATOM   1775 N  NE2 . HIS A 1 172 ? 11.975  4.355   -26.557 1.00 23.14  ? 172 HIS A NE2 1 
ATOM   1776 N  N   . ALA A 1 173 ? 13.882  -0.175  -30.692 1.00 20.26  ? 173 ALA A N   1 
ATOM   1777 C  CA  . ALA A 1 173 ? 14.364  -1.267  -31.543 1.00 18.89  ? 173 ALA A CA  1 
ATOM   1778 C  C   . ALA A 1 173 ? 15.350  -2.106  -30.723 1.00 18.94  ? 173 ALA A C   1 
ATOM   1779 O  O   . ALA A 1 173 ? 16.130  -1.558  -29.899 1.00 16.88  ? 173 ALA A O   1 
ATOM   1780 C  CB  . ALA A 1 173 ? 14.948  -0.676  -32.808 1.00 20.22  ? 173 ALA A CB  1 
ATOM   1781 N  N   . GLY A 1 174 ? 15.255  -3.418  -30.860 1.00 18.07  ? 174 GLY A N   1 
ATOM   1782 C  CA  . GLY A 1 174 ? 16.139  -4.320  -30.112 1.00 19.07  ? 174 GLY A CA  1 
ATOM   1783 C  C   . GLY A 1 174 ? 16.254  -5.649  -30.820 1.00 20.97  ? 174 GLY A C   1 
ATOM   1784 O  O   . GLY A 1 174 ? 15.741  -5.770  -31.987 1.00 19.32  ? 174 GLY A O   1 
ATOM   1785 N  N   . THR A 1 175 ? 16.828  -6.621  -30.109 1.00 21.02  ? 175 THR A N   1 
ATOM   1786 C  CA  . THR A 1 175 ? 17.161  -7.955  -30.657 1.00 22.32  ? 175 THR A CA  1 
ATOM   1787 C  C   . THR A 1 175 ? 16.488  -9.012  -29.796 1.00 21.57  ? 175 THR A C   1 
ATOM   1788 O  O   . THR A 1 175 ? 16.122  -8.702  -28.655 1.00 19.58  ? 175 THR A O   1 
ATOM   1789 C  CB  . THR A 1 175 ? 18.667  -8.223  -30.626 1.00 24.29  ? 175 THR A CB  1 
ATOM   1790 O  OG1 . THR A 1 175 ? 19.079  -8.234  -29.251 1.00 22.85  ? 175 THR A OG1 1 
ATOM   1791 C  CG2 . THR A 1 175 ? 19.450  -7.202  -31.429 1.00 26.83  ? 175 THR A CG2 1 
ATOM   1792 N  N   . ASP A 1 176 ? 16.427  -10.231 -30.305 1.00 21.69  ? 176 ASP A N   1 
ATOM   1793 C  CA  . ASP A 1 176 ? 16.237  -11.412 -29.433 1.00 21.27  ? 176 ASP A CA  1 
ATOM   1794 C  C   . ASP A 1 176 ? 17.532  -11.595 -28.635 1.00 21.48  ? 176 ASP A C   1 
ATOM   1795 O  O   . ASP A 1 176 ? 18.512  -10.780 -28.793 1.00 19.58  ? 176 ASP A O   1 
ATOM   1796 C  CB  . ASP A 1 176 ? 15.789  -12.616 -30.256 1.00 22.66  ? 176 ASP A CB  1 
ATOM   1797 C  CG  . ASP A 1 176 ? 16.785  -13.032 -31.326 1.00 24.17  ? 176 ASP A CG  1 
ATOM   1798 O  OD1 . ASP A 1 176 ? 18.023  -12.877 -31.123 1.00 22.82  ? 176 ASP A OD1 1 
ATOM   1799 O  OD2 . ASP A 1 176 ? 16.324  -13.423 -32.370 1.00 26.68  ? 176 ASP A OD2 1 
ATOM   1800 N  N   . LEU A 1 177 ? 17.563  -12.621 -27.791 1.00 21.85  ? 177 LEU A N   1 
ATOM   1801 C  CA  . LEU A 1 177 ? 18.705  -12.866 -26.888 1.00 22.32  ? 177 LEU A CA  1 
ATOM   1802 C  C   . LEU A 1 177 ? 19.749  -13.683 -27.639 1.00 21.54  ? 177 LEU A C   1 
ATOM   1803 O  O   . LEU A 1 177 ? 20.740  -13.996 -26.999 1.00 23.92  ? 177 LEU A O   1 
ATOM   1804 C  CB  . LEU A 1 177 ? 18.238  -13.563 -25.601 1.00 23.75  ? 177 LEU A CB  1 
ATOM   1805 C  CG  . LEU A 1 177 ? 17.821  -12.607 -24.485 1.00 24.77  ? 177 LEU A CG  1 
ATOM   1806 C  CD1 . LEU A 1 177 ? 19.024  -11.854 -23.952 1.00 26.07  ? 177 LEU A CD1 1 
ATOM   1807 C  CD2 . LEU A 1 177 ? 16.758  -11.618 -24.984 1.00 26.96  ? 177 LEU A CD2 1 
ATOM   1808 N  N   . GLU A 1 178 ? 19.557  -13.954 -28.940 1.00 22.03  ? 178 GLU A N   1 
ATOM   1809 C  CA  . GLU A 1 178 ? 20.644  -14.446 -29.838 1.00 23.63  ? 178 GLU A CA  1 
ATOM   1810 C  C   . GLU A 1 178 ? 21.222  -13.270 -30.631 1.00 22.19  ? 178 GLU A C   1 
ATOM   1811 O  O   . GLU A 1 178 ? 22.061  -13.527 -31.510 1.00 21.86  ? 178 GLU A O   1 
ATOM   1812 C  CB  . GLU A 1 178 ? 20.147  -15.545 -30.767 1.00 26.33  ? 178 GLU A CB  1 
ATOM   1813 C  CG  . GLU A 1 178 ? 19.734  -16.793 -29.990 1.00 31.10  ? 178 GLU A CG  1 
ATOM   1814 C  CD  . GLU A 1 178 ? 19.251  -17.957 -30.838 1.00 32.87  ? 178 GLU A CD  1 
ATOM   1815 O  OE1 . GLU A 1 178 ? 18.760  -17.734 -31.971 1.00 37.59  ? 178 GLU A OE1 1 
ATOM   1816 O  OE2 . GLU A 1 178 ? 19.390  -19.075 -30.368 1.00 38.17  ? 178 GLU A OE2 1 
ATOM   1817 N  N   . GLY A 1 179 ? 20.818  -12.036 -30.309 1.00 22.47  ? 179 GLY A N   1 
ATOM   1818 C  CA  . GLY A 1 179 ? 21.418  -10.805 -30.879 1.00 22.36  ? 179 GLY A CA  1 
ATOM   1819 C  C   . GLY A 1 179 ? 20.910  -10.471 -32.267 1.00 21.86  ? 179 GLY A C   1 
ATOM   1820 O  O   . GLY A 1 179 ? 21.473  -9.560  -32.892 1.00 23.37  ? 179 GLY A O   1 
ATOM   1821 N  N   . ASN A 1 180 ? 19.885  -11.152 -32.782 1.00 23.05  ? 180 ASN A N   1 
ATOM   1822 C  CA  . ASN A 1 180 ? 19.314  -10.786 -34.107 1.00 23.49  ? 180 ASN A CA  1 
ATOM   1823 C  C   . ASN A 1 180 ? 18.266  -9.710  -33.876 1.00 23.46  ? 180 ASN A C   1 
ATOM   1824 O  O   . ASN A 1 180 ? 17.368  -9.944  -33.019 1.00 20.70  ? 180 ASN A O   1 
ATOM   1825 C  CB  . ASN A 1 180 ? 18.673  -11.965 -34.835 1.00 26.21  ? 180 ASN A CB  1 
ATOM   1826 C  CG  . ASN A 1 180 ? 19.673  -13.059 -35.122 1.00 25.63  ? 180 ASN A CG  1 
ATOM   1827 O  OD1 . ASN A 1 180 ? 19.598  -14.127 -34.526 1.00 31.18  ? 180 ASN A OD1 1 
ATOM   1828 N  ND2 . ASN A 1 180 ? 20.649  -12.761 -35.954 1.00 22.84  ? 180 ASN A ND2 1 
ATOM   1829 N  N   . PHE A 1 181 ? 18.364  -8.598  -34.611 1.00 23.22  ? 181 PHE A N   1 
ATOM   1830 C  CA  . PHE A 1 181 ? 17.388  -7.483  -34.565 1.00 22.69  ? 181 PHE A CA  1 
ATOM   1831 C  C   . PHE A 1 181 ? 16.008  -7.981  -34.994 1.00 24.25  ? 181 PHE A C   1 
ATOM   1832 O  O   . PHE A 1 181 ? 15.881  -8.871  -35.846 1.00 24.23  ? 181 PHE A O   1 
ATOM   1833 C  CB  . PHE A 1 181 ? 17.806  -6.282  -35.417 1.00 21.92  ? 181 PHE A CB  1 
ATOM   1834 C  CG  . PHE A 1 181 ? 18.538  -5.243  -34.615 1.00 21.41  ? 181 PHE A CG  1 
ATOM   1835 C  CD1 . PHE A 1 181 ? 19.917  -5.309  -34.483 1.00 22.09  ? 181 PHE A CD1 1 
ATOM   1836 C  CD2 . PHE A 1 181 ? 17.847  -4.244  -33.943 1.00 21.57  ? 181 PHE A CD2 1 
ATOM   1837 C  CE1 . PHE A 1 181 ? 20.599  -4.350  -33.745 1.00 22.54  ? 181 PHE A CE1 1 
ATOM   1838 C  CE2 . PHE A 1 181 ? 18.527  -3.303  -33.174 1.00 21.29  ? 181 PHE A CE2 1 
ATOM   1839 C  CZ  . PHE A 1 181 ? 19.899  -3.356  -33.081 1.00 22.46  ? 181 PHE A CZ  1 
ATOM   1840 N  N   . TYR A 1 182 ? 14.983  -7.422  -34.364 1.00 22.47  ? 182 TYR A N   1 
ATOM   1841 C  CA  . TYR A 1 182 ? 13.598  -7.438  -34.893 1.00 21.69  ? 182 TYR A CA  1 
ATOM   1842 C  C   . TYR A 1 182 ? 13.565  -6.371  -35.971 1.00 21.65  ? 182 TYR A C   1 
ATOM   1843 O  O   . TYR A 1 182 ? 14.050  -5.270  -35.721 1.00 22.44  ? 182 TYR A O   1 
ATOM   1844 C  CB  . TYR A 1 182 ? 12.586  -7.197  -33.775 1.00 21.23  ? 182 TYR A CB  1 
ATOM   1845 C  CG  . TYR A 1 182 ? 12.485  -8.356  -32.817 1.00 23.17  ? 182 TYR A CG  1 
ATOM   1846 C  CD1 . TYR A 1 182 ? 11.820  -9.518  -33.197 1.00 21.62  ? 182 TYR A CD1 1 
ATOM   1847 C  CD2 . TYR A 1 182 ? 13.067  -8.311  -31.560 1.00 21.33  ? 182 TYR A CD2 1 
ATOM   1848 C  CE1 . TYR A 1 182 ? 11.712  -10.592 -32.334 1.00 20.37  ? 182 TYR A CE1 1 
ATOM   1849 C  CE2 . TYR A 1 182 ? 12.952  -9.380  -30.680 1.00 21.40  ? 182 TYR A CE2 1 
ATOM   1850 C  CZ  . TYR A 1 182 ? 12.275  -10.531 -31.080 1.00 21.32  ? 182 TYR A CZ  1 
ATOM   1851 O  OH  . TYR A 1 182 ? 12.166  -11.629 -30.267 1.00 18.36  ? 182 TYR A OH  1 
ATOM   1852 N  N   . GLY A 1 183 ? 13.109  -6.720  -37.158 1.00 22.92  ? 183 GLY A N   1 
ATOM   1853 C  CA  . GLY A 1 183 ? 12.954  -5.739  -38.236 1.00 25.29  ? 183 GLY A CA  1 
ATOM   1854 C  C   . GLY A 1 183 ? 14.269  -5.398  -38.911 1.00 29.05  ? 183 GLY A C   1 
ATOM   1855 O  O   . GLY A 1 183 ? 15.315  -5.980  -38.641 1.00 33.26  ? 183 GLY A O   1 
ATOM   1856 N  N   . PRO A 1 184 ? 14.234  -4.422  -39.831 1.00 30.14  ? 184 PRO A N   1 
ATOM   1857 C  CA  . PRO A 1 184 ? 15.379  -4.149  -40.701 1.00 31.24  ? 184 PRO A CA  1 
ATOM   1858 C  C   . PRO A 1 184 ? 16.481  -3.291  -40.054 1.00 30.12  ? 184 PRO A C   1 
ATOM   1859 O  O   . PRO A 1 184 ? 17.186  -2.643  -40.759 1.00 34.56  ? 184 PRO A O   1 
ATOM   1860 C  CB  . PRO A 1 184 ? 14.679  -3.421  -41.866 1.00 29.98  ? 184 PRO A CB  1 
ATOM   1861 C  CG  . PRO A 1 184 ? 13.520  -2.664  -41.210 1.00 30.59  ? 184 PRO A CG  1 
ATOM   1862 C  CD  . PRO A 1 184 ? 13.073  -3.555  -40.073 1.00 30.35  ? 184 PRO A CD  1 
ATOM   1863 N  N   . PHE A 1 185 ? 16.595  -3.272  -38.729 1.00 28.95  ? 185 PHE A N   1 
ATOM   1864 C  CA  . PHE A 1 185 ? 17.422  -2.253  -38.026 1.00 28.93  ? 185 PHE A CA  1 
ATOM   1865 C  C   . PHE A 1 185 ? 18.831  -2.802  -37.790 1.00 25.17  ? 185 PHE A C   1 
ATOM   1866 O  O   . PHE A 1 185 ? 19.050  -4.010  -37.814 1.00 24.02  ? 185 PHE A O   1 
ATOM   1867 C  CB  . PHE A 1 185 ? 16.748  -1.786  -36.732 1.00 29.06  ? 185 PHE A CB  1 
ATOM   1868 C  CG  . PHE A 1 185 ? 15.338  -1.324  -36.962 1.00 31.01  ? 185 PHE A CG  1 
ATOM   1869 C  CD1 . PHE A 1 185 ? 15.098  -0.240  -37.793 1.00 28.62  ? 185 PHE A CD1 1 
ATOM   1870 C  CD2 . PHE A 1 185 ? 14.259  -2.046  -36.466 1.00 27.70  ? 185 PHE A CD2 1 
ATOM   1871 C  CE1 . PHE A 1 185 ? 13.804  0.175   -38.055 1.00 26.02  ? 185 PHE A CE1 1 
ATOM   1872 C  CE2 . PHE A 1 185 ? 12.965  -1.635  -36.741 1.00 28.58  ? 185 PHE A CE2 1 
ATOM   1873 C  CZ  . PHE A 1 185 ? 12.741  -0.526  -37.530 1.00 28.96  ? 185 PHE A CZ  1 
ATOM   1874 N  N   . VAL A 1 186 ? 19.773  -1.898  -37.559 1.00 24.32  ? 186 VAL A N   1 
ATOM   1875 C  CA  . VAL A 1 186 ? 21.211  -2.226  -37.338 1.00 23.19  ? 186 VAL A CA  1 
ATOM   1876 C  C   . VAL A 1 186 ? 21.688  -1.346  -36.186 1.00 24.73  ? 186 VAL A C   1 
ATOM   1877 O  O   . VAL A 1 186 ? 21.150  -0.189  -36.024 1.00 23.14  ? 186 VAL A O   1 
ATOM   1878 C  CB  . VAL A 1 186 ? 22.026  -1.977  -38.620 1.00 25.11  ? 186 VAL A CB  1 
ATOM   1879 C  CG1 . VAL A 1 186 ? 21.651  -2.931  -39.736 1.00 25.26  ? 186 VAL A CG1 1 
ATOM   1880 C  CG2 . VAL A 1 186 ? 21.904  -0.538  -39.101 1.00 27.58  ? 186 VAL A CG2 1 
ATOM   1881 N  N   A ASP A 1 187 ? 22.654  -1.838  -35.398 0.20 24.21  ? 187 ASP A N   1 
ATOM   1882 N  N   B ASP A 1 187 ? 22.654  -1.838  -35.398 0.20 24.21  ? 187 ASP A N   1 
ATOM   1883 N  N   C ASP A 1 187 ? 22.670  -1.832  -35.415 0.30 24.57  ? 187 ASP A N   1 
ATOM   1884 N  N   D ASP A 1 187 ? 22.670  -1.832  -35.415 0.30 24.57  ? 187 ASP A N   1 
ATOM   1885 C  CA  A ASP A 1 187 ? 23.238  -1.096  -34.245 0.20 24.30  ? 187 ASP A CA  1 
ATOM   1886 C  CA  B ASP A 1 187 ? 23.238  -1.096  -34.245 0.20 24.30  ? 187 ASP A CA  1 
ATOM   1887 C  CA  C ASP A 1 187 ? 23.291  -1.069  -34.298 0.30 24.90  ? 187 ASP A CA  1 
ATOM   1888 C  CA  D ASP A 1 187 ? 23.291  -1.069  -34.298 0.30 24.90  ? 187 ASP A CA  1 
ATOM   1889 C  C   A ASP A 1 187 ? 24.284  -0.104  -34.771 0.20 25.11  ? 187 ASP A C   1 
ATOM   1890 C  C   B ASP A 1 187 ? 24.284  -0.104  -34.770 0.20 25.11  ? 187 ASP A C   1 
ATOM   1891 C  C   C ASP A 1 187 ? 24.348  -0.120  -34.878 0.30 26.15  ? 187 ASP A C   1 
ATOM   1892 C  C   D ASP A 1 187 ? 24.348  -0.120  -34.878 0.30 26.15  ? 187 ASP A C   1 
ATOM   1893 O  O   A ASP A 1 187 ? 25.468  -0.217  -34.396 0.20 24.65  ? 187 ASP A O   1 
ATOM   1894 O  O   B ASP A 1 187 ? 25.468  -0.217  -34.396 0.20 24.65  ? 187 ASP A O   1 
ATOM   1895 O  O   C ASP A 1 187 ? 25.535  -0.256  -34.530 0.30 25.62  ? 187 ASP A O   1 
ATOM   1896 O  O   D ASP A 1 187 ? 25.535  -0.256  -34.530 0.30 25.62  ? 187 ASP A O   1 
ATOM   1897 C  CB  A ASP A 1 187 ? 23.761  -2.032  -33.149 0.20 23.74  ? 187 ASP A CB  1 
ATOM   1898 C  CB  B ASP A 1 187 ? 23.761  -2.032  -33.149 0.20 23.74  ? 187 ASP A CB  1 
ATOM   1899 C  CB  C ASP A 1 187 ? 23.814  -1.984  -33.187 0.30 24.16  ? 187 ASP A CB  1 
ATOM   1900 C  CB  D ASP A 1 187 ? 23.814  -1.984  -33.187 0.30 24.16  ? 187 ASP A CB  1 
ATOM   1901 C  CG  A ASP A 1 187 ? 24.647  -3.179  -33.602 0.20 23.63  ? 187 ASP A CG  1 
ATOM   1902 C  CG  B ASP A 1 187 ? 24.647  -3.179  -33.602 0.20 23.63  ? 187 ASP A CG  1 
ATOM   1903 C  CG  C ASP A 1 187 ? 24.703  -3.136  -33.618 0.30 24.11  ? 187 ASP A CG  1 
ATOM   1904 C  CG  D ASP A 1 187 ? 24.703  -3.136  -33.618 0.30 24.11  ? 187 ASP A CG  1 
ATOM   1905 O  OD1 A ASP A 1 187 ? 24.835  -3.346  -34.822 0.20 23.31  ? 187 ASP A OD1 1 
ATOM   1906 O  OD1 B ASP A 1 187 ? 24.835  -3.346  -34.822 0.20 23.31  ? 187 ASP A OD1 1 
ATOM   1907 O  OD1 C ASP A 1 187 ? 24.993  -3.248  -34.821 0.30 23.86  ? 187 ASP A OD1 1 
ATOM   1908 O  OD1 D ASP A 1 187 ? 24.993  -3.248  -34.821 0.30 23.86  ? 187 ASP A OD1 1 
ATOM   1909 O  OD2 A ASP A 1 187 ? 25.135  -3.912  -32.715 0.20 24.43  ? 187 ASP A OD2 1 
ATOM   1910 O  OD2 B ASP A 1 187 ? 25.135  -3.912  -32.715 0.20 24.43  ? 187 ASP A OD2 1 
ATOM   1911 O  OD2 C ASP A 1 187 ? 25.092  -3.926  -32.731 0.30 25.49  ? 187 ASP A OD2 1 
ATOM   1912 O  OD2 D ASP A 1 187 ? 25.092  -3.926  -32.731 0.30 25.49  ? 187 ASP A OD2 1 
ATOM   1913 N  N   A ARG A 1 188 ? 23.825  0.841   -35.598 0.20 26.12  ? 188 ARG A N   1 
ATOM   1914 N  N   B ARG A 1 188 ? 23.826  0.841   -35.598 0.20 26.12  ? 188 ARG A N   1 
ATOM   1915 N  N   C ARG A 1 188 ? 23.896  0.801   -35.735 0.30 27.91  ? 188 ARG A N   1 
ATOM   1916 N  N   D ARG A 1 188 ? 23.896  0.801   -35.735 0.30 27.91  ? 188 ARG A N   1 
ATOM   1917 C  CA  A ARG A 1 188 ? 24.585  1.999   -36.144 0.20 27.27  ? 188 ARG A CA  1 
ATOM   1918 C  CA  B ARG A 1 188 ? 24.585  1.999   -36.144 0.20 27.27  ? 188 ARG A CA  1 
ATOM   1919 C  CA  C ARG A 1 188 ? 24.640  1.974   -36.269 0.30 29.56  ? 188 ARG A CA  1 
ATOM   1920 C  CA  D ARG A 1 188 ? 24.640  1.974   -36.269 0.30 29.56  ? 188 ARG A CA  1 
ATOM   1921 C  C   A ARG A 1 188 ? 23.712  3.250   -36.011 0.20 28.37  ? 188 ARG A C   1 
ATOM   1922 C  C   B ARG A 1 188 ? 23.712  3.250   -36.011 0.20 28.37  ? 188 ARG A C   1 
ATOM   1923 C  C   C ARG A 1 188 ? 23.765  3.214   -36.073 0.30 30.05  ? 188 ARG A C   1 
ATOM   1924 C  C   D ARG A 1 188 ? 23.765  3.214   -36.073 0.30 30.05  ? 188 ARG A C   1 
ATOM   1925 O  O   A ARG A 1 188 ? 22.498  3.134   -36.243 0.20 26.52  ? 188 ARG A O   1 
ATOM   1926 O  O   B ARG A 1 188 ? 22.498  3.134   -36.243 0.20 26.52  ? 188 ARG A O   1 
ATOM   1927 O  O   C ARG A 1 188 ? 22.549  3.094   -36.277 0.30 26.93  ? 188 ARG A O   1 
ATOM   1928 O  O   D ARG A 1 188 ? 22.549  3.094   -36.277 0.30 26.93  ? 188 ARG A O   1 
ATOM   1929 C  CB  A ARG A 1 188 ? 24.902  1.793   -37.628 0.20 26.62  ? 188 ARG A CB  1 
ATOM   1930 C  CB  B ARG A 1 188 ? 24.902  1.793   -37.628 0.20 26.62  ? 188 ARG A CB  1 
ATOM   1931 C  CB  C ARG A 1 188 ? 24.903  1.825   -37.769 0.30 29.82  ? 188 ARG A CB  1 
ATOM   1932 C  CB  D ARG A 1 188 ? 24.903  1.825   -37.769 0.30 29.82  ? 188 ARG A CB  1 
ATOM   1933 C  CG  A ARG A 1 188 ? 25.922  0.706   -37.923 0.20 26.65  ? 188 ARG A CG  1 
ATOM   1934 C  CG  B ARG A 1 188 ? 25.922  0.706   -37.923 0.20 26.65  ? 188 ARG A CG  1 
ATOM   1935 C  CG  C ARG A 1 188 ? 25.734  0.609   -38.148 0.30 30.95  ? 188 ARG A CG  1 
ATOM   1936 C  CG  D ARG A 1 188 ? 25.734  0.609   -38.148 0.30 30.95  ? 188 ARG A CG  1 
ATOM   1937 C  CD  A ARG A 1 188 ? 25.958  0.381   -39.404 0.20 25.65  ? 188 ARG A CD  1 
ATOM   1938 C  CD  B ARG A 1 188 ? 25.958  0.381   -39.404 0.20 25.65  ? 188 ARG A CD  1 
ATOM   1939 C  CD  C ARG A 1 188 ? 26.137  0.541   -39.612 0.30 30.14  ? 188 ARG A CD  1 
ATOM   1940 C  CD  D ARG A 1 188 ? 26.137  0.541   -39.612 0.30 30.14  ? 188 ARG A CD  1 
ATOM   1941 N  NE  A ARG A 1 188 ? 26.248  1.555   -40.218 0.20 25.05  ? 188 ARG A NE  1 
ATOM   1942 N  NE  B ARG A 1 188 ? 26.248  1.555   -40.218 0.20 25.05  ? 188 ARG A NE  1 
ATOM   1943 N  NE  C ARG A 1 188 ? 26.140  1.811   -40.330 0.30 30.34  ? 188 ARG A NE  1 
ATOM   1944 N  NE  D ARG A 1 188 ? 26.141  1.811   -40.330 0.30 30.34  ? 188 ARG A NE  1 
ATOM   1945 C  CZ  A ARG A 1 188 ? 25.967  1.671   -41.514 0.20 24.31  ? 188 ARG A CZ  1 
ATOM   1946 C  CZ  B ARG A 1 188 ? 25.967  1.671   -41.514 0.20 24.31  ? 188 ARG A CZ  1 
ATOM   1947 C  CZ  C ARG A 1 188 ? 25.840  1.948   -41.620 0.30 30.05  ? 188 ARG A CZ  1 
ATOM   1948 C  CZ  D ARG A 1 188 ? 25.840  1.948   -41.620 0.30 30.05  ? 188 ARG A CZ  1 
ATOM   1949 N  NH1 A ARG A 1 188 ? 25.369  0.685   -42.161 0.20 24.27  ? 188 ARG A NH1 1 
ATOM   1950 N  NH1 B ARG A 1 188 ? 25.369  0.685   -42.161 0.20 24.27  ? 188 ARG A NH1 1 
ATOM   1951 N  NH1 C ARG A 1 188 ? 25.474  0.901   -42.339 0.30 30.48  ? 188 ARG A NH1 1 
ATOM   1952 N  NH1 D ARG A 1 188 ? 25.474  0.901   -42.339 0.30 30.48  ? 188 ARG A NH1 1 
ATOM   1953 N  NH2 A ARG A 1 188 ? 26.279  2.779   -42.162 0.20 23.74  ? 188 ARG A NH2 1 
ATOM   1954 N  NH2 B ARG A 1 188 ? 26.279  2.779   -42.162 0.20 23.74  ? 188 ARG A NH2 1 
ATOM   1955 N  NH2 C ARG A 1 188 ? 25.885  3.139   -42.187 0.30 30.80  ? 188 ARG A NH2 1 
ATOM   1956 N  NH2 D ARG A 1 188 ? 25.885  3.139   -42.187 0.30 30.80  ? 188 ARG A NH2 1 
ATOM   1957 N  N   A GLN A 1 189 ? 24.300  4.406   -35.691 0.20 31.37  ? 189 GLN A N   1 
ATOM   1958 N  N   B GLN A 1 189 ? 24.300  4.406   -35.691 0.20 31.37  ? 189 GLN A N   1 
ATOM   1959 N  N   C GLN A 1 189 ? 24.341  4.366   -35.733 0.30 33.09  ? 189 GLN A N   1 
ATOM   1960 N  N   D GLN A 1 189 ? 24.341  4.366   -35.733 0.30 33.09  ? 189 GLN A N   1 
ATOM   1961 C  CA  A GLN A 1 189 ? 23.542  5.679   -35.541 0.20 34.17  ? 189 GLN A CA  1 
ATOM   1962 C  CA  B GLN A 1 189 ? 23.542  5.679   -35.541 0.20 34.17  ? 189 GLN A CA  1 
ATOM   1963 C  CA  C GLN A 1 189 ? 23.539  5.605   -35.546 0.30 36.17  ? 189 GLN A CA  1 
ATOM   1964 C  CA  D GLN A 1 189 ? 23.539  5.605   -35.546 0.30 36.17  ? 189 GLN A CA  1 
ATOM   1965 C  C   A GLN A 1 189 ? 23.398  6.361   -36.907 0.20 34.92  ? 189 GLN A C   1 
ATOM   1966 C  C   B GLN A 1 189 ? 23.398  6.361   -36.907 0.20 34.92  ? 189 GLN A C   1 
ATOM   1967 C  C   C GLN A 1 189 ? 23.455  6.348   -36.888 0.30 36.18  ? 189 GLN A C   1 
ATOM   1968 C  C   D GLN A 1 189 ? 23.455  6.348   -36.888 0.30 36.18  ? 189 GLN A C   1 
ATOM   1969 O  O   A GLN A 1 189 ? 23.145  7.578   -36.929 0.20 35.01  ? 189 GLN A O   1 
ATOM   1970 O  O   B GLN A 1 189 ? 23.145  7.578   -36.929 0.20 35.01  ? 189 GLN A O   1 
ATOM   1971 O  O   C GLN A 1 189 ? 23.305  7.580   -36.870 0.30 36.71  ? 189 GLN A O   1 
ATOM   1972 O  O   D GLN A 1 189 ? 23.305  7.580   -36.870 0.30 36.71  ? 189 GLN A O   1 
ATOM   1973 C  CB  A GLN A 1 189 ? 24.196  6.579   -34.491 0.20 37.11  ? 189 GLN A CB  1 
ATOM   1974 C  CB  B GLN A 1 189 ? 24.196  6.579   -34.491 0.20 37.11  ? 189 GLN A CB  1 
ATOM   1975 C  CB  C GLN A 1 189 ? 24.079  6.396   -34.350 0.30 40.72  ? 189 GLN A CB  1 
ATOM   1976 C  CB  D GLN A 1 189 ? 24.079  6.396   -34.350 0.30 40.72  ? 189 GLN A CB  1 
ATOM   1977 C  CG  A GLN A 1 189 ? 23.910  6.124   -33.064 0.20 39.27  ? 189 GLN A CG  1 
ATOM   1978 C  CG  B GLN A 1 189 ? 23.910  6.124   -33.064 0.20 39.27  ? 189 GLN A CG  1 
ATOM   1979 C  CG  C GLN A 1 189 ? 23.942  5.616   -33.041 0.30 43.51  ? 189 GLN A CG  1 
ATOM   1980 C  CG  D GLN A 1 189 ? 23.942  5.616   -33.041 0.30 43.51  ? 189 GLN A CG  1 
ATOM   1981 C  CD  A GLN A 1 189 ? 24.209  7.192   -32.041 0.20 41.38  ? 189 GLN A CD  1 
ATOM   1982 C  CD  B GLN A 1 189 ? 24.209  7.192   -32.041 0.20 41.38  ? 189 GLN A CD  1 
ATOM   1983 C  CD  C GLN A 1 189 ? 23.374  6.428   -31.901 0.30 47.20  ? 189 GLN A CD  1 
ATOM   1984 C  CD  D GLN A 1 189 ? 23.374  6.427   -31.901 0.30 47.20  ? 189 GLN A CD  1 
ATOM   1985 O  OE1 A GLN A 1 189 ? 25.074  8.045   -32.240 0.20 42.79  ? 189 GLN A OE1 1 
ATOM   1986 O  OE1 B GLN A 1 189 ? 25.074  8.045   -32.240 0.20 42.79  ? 189 GLN A OE1 1 
ATOM   1987 O  OE1 C GLN A 1 189 ? 23.848  7.522   -31.596 0.30 52.65  ? 189 GLN A OE1 1 
ATOM   1988 O  OE1 D GLN A 1 189 ? 23.848  7.522   -31.596 0.30 52.65  ? 189 GLN A OE1 1 
ATOM   1989 N  NE2 A GLN A 1 189 ? 23.490  7.150   -30.927 0.20 43.29  ? 189 GLN A NE2 1 
ATOM   1990 N  NE2 B GLN A 1 189 ? 23.490  7.150   -30.927 0.20 43.29  ? 189 GLN A NE2 1 
ATOM   1991 N  NE2 C GLN A 1 189 ? 22.356  5.885   -31.245 0.30 46.49  ? 189 GLN A NE2 1 
ATOM   1992 N  NE2 D GLN A 1 189 ? 22.357  5.885   -31.245 0.30 46.49  ? 189 GLN A NE2 1 
ATOM   1993 N  N   . THR A 1 190 ? 23.525  5.598   -37.997 1.00 35.68  ? 190 THR A N   1 
ATOM   1994 C  CA  . THR A 1 190 ? 23.161  6.035   -39.375 1.00 39.20  ? 190 THR A CA  1 
ATOM   1995 C  C   . THR A 1 190 ? 21.638  6.166   -39.432 1.00 39.11  ? 190 THR A C   1 
ATOM   1996 O  O   . THR A 1 190 ? 20.977  5.442   -38.673 1.00 37.20  ? 190 THR A O   1 
ATOM   1997 C  CB  . THR A 1 190 ? 23.604  4.987   -40.415 1.00 41.45  ? 190 THR A CB  1 
ATOM   1998 O  OG1 . THR A 1 190 ? 23.877  5.613   -41.674 1.00 41.18  ? 190 THR A OG1 1 
ATOM   1999 C  CG2 . THR A 1 190 ? 22.601  3.861   -40.585 1.00 36.14  ? 190 THR A CG2 1 
ATOM   2000 N  N   . ALA A 1 191 ? 21.114  7.045   -40.287 1.00 40.22  ? 191 ALA A N   1 
ATOM   2001 C  CA  . ALA A 1 191 ? 19.669  7.341   -40.432 1.00 39.79  ? 191 ALA A CA  1 
ATOM   2002 C  C   . ALA A 1 191 ? 18.927  6.050   -40.758 1.00 39.89  ? 191 ALA A C   1 
ATOM   2003 O  O   . ALA A 1 191 ? 19.286  5.394   -41.752 1.00 39.66  ? 191 ALA A O   1 
ATOM   2004 C  CB  . ALA A 1 191 ? 19.413  8.375   -41.502 1.00 41.31  ? 191 ALA A CB  1 
ATOM   2005 N  N   . GLN A 1 192 ? 17.978  5.680   -39.895 1.00 39.42  ? 192 GLN A N   1 
ATOM   2006 C  CA  . GLN A 1 192 ? 17.052  4.532   -40.092 1.00 36.09  ? 192 GLN A CA  1 
ATOM   2007 C  C   . GLN A 1 192 ? 15.665  4.994   -39.661 1.00 36.57  ? 192 GLN A C   1 
ATOM   2008 O  O   . GLN A 1 192 ? 15.576  5.842   -38.725 1.00 39.22  ? 192 GLN A O   1 
ATOM   2009 C  CB  . GLN A 1 192 ? 17.416  3.302   -39.253 1.00 31.77  ? 192 GLN A CB  1 
ATOM   2010 C  CG  . GLN A 1 192 ? 18.892  2.993   -39.173 1.00 31.71  ? 192 GLN A CG  1 
ATOM   2011 C  CD  . GLN A 1 192 ? 19.166  1.878   -38.192 1.00 29.99  ? 192 GLN A CD  1 
ATOM   2012 O  OE1 . GLN A 1 192 ? 18.617  0.782   -38.294 1.00 28.64  ? 192 GLN A OE1 1 
ATOM   2013 N  NE2 . GLN A 1 192 ? 20.028  2.164   -37.238 1.00 25.80  ? 192 GLN A NE2 1 
ATOM   2014 N  N   . ALA A 1 193 ? 14.635  4.476   -40.323 1.00 37.65  ? 193 ALA A N   1 
ATOM   2015 C  CA  . ALA A 1 193 ? 13.223  4.762   -39.980 1.00 40.48  ? 193 ALA A CA  1 
ATOM   2016 C  C   . ALA A 1 193 ? 12.425  3.462   -40.083 1.00 37.69  ? 193 ALA A C   1 
ATOM   2017 O  O   . ALA A 1 193 ? 12.653  2.664   -40.999 1.00 37.33  ? 193 ALA A O   1 
ATOM   2018 C  CB  . ALA A 1 193 ? 12.663  5.870   -40.850 1.00 41.48  ? 193 ALA A CB  1 
ATOM   2019 N  N   . ALA A 1 194 ? 11.547  3.245   -39.113 1.00 44.50  ? 194 ALA A N   1 
ATOM   2020 C  CA  . ALA A 1 194 ? 10.595  2.116   -39.089 1.00 42.86  ? 194 ALA A CA  1 
ATOM   2021 C  C   . ALA A 1 194 ? 9.588   2.287   -40.231 1.00 41.23  ? 194 ALA A C   1 
ATOM   2022 O  O   . ALA A 1 194 ? 9.295   3.426   -40.586 1.00 43.05  ? 194 ALA A O   1 
ATOM   2023 C  CB  . ALA A 1 194 ? 9.917   2.089   -37.745 1.00 46.70  ? 194 ALA A CB  1 
ATOM   2024 N  N   . GLY A 1 195 ? 9.071   1.181   -40.759 1.00 41.19  ? 195 GLY A N   1 
ATOM   2025 C  CA  . GLY A 1 195 ? 7.922   1.159   -41.675 1.00 40.15  ? 195 GLY A CA  1 
ATOM   2026 C  C   . GLY A 1 195 ? 6.702   1.806   -41.041 1.00 41.03  ? 195 GLY A C   1 
ATOM   2027 O  O   . GLY A 1 195 ? 6.653   1.928   -39.795 1.00 37.88  ? 195 GLY A O   1 
ATOM   2028 N  N   . THR A 1 196 ? 5.765   2.274   -41.868 1.00 44.84  ? 196 THR A N   1 
ATOM   2029 C  CA  . THR A 1 196 ? 4.447   2.775   -41.403 1.00 46.14  ? 196 THR A CA  1 
ATOM   2030 C  C   . THR A 1 196 ? 3.854   1.708   -40.484 1.00 41.12  ? 196 THR A C   1 
ATOM   2031 O  O   . THR A 1 196 ? 3.814   0.535   -40.877 1.00 44.70  ? 196 THR A O   1 
ATOM   2032 C  CB  . THR A 1 196 ? 3.492   3.100   -42.559 1.00 48.30  ? 196 THR A CB  1 
ATOM   2033 O  OG1 . THR A 1 196 ? 3.489   1.951   -43.410 1.00 48.34  ? 196 THR A OG1 1 
ATOM   2034 C  CG2 . THR A 1 196 ? 3.883   4.359   -43.304 1.00 47.06  ? 196 THR A CG2 1 
ATOM   2035 N  N   . ASP A 1 197 ? 3.440   2.099   -39.288 1.00 37.28  ? 197 ASP A N   1 
ATOM   2036 C  CA  . ASP A 1 197 ? 2.875   1.140   -38.309 1.00 36.23  ? 197 ASP A CA  1 
ATOM   2037 C  C   . ASP A 1 197 ? 1.422   0.814   -38.689 1.00 37.57  ? 197 ASP A C   1 
ATOM   2038 O  O   . ASP A 1 197 ? 0.766   1.607   -39.401 1.00 42.84  ? 197 ASP A O   1 
ATOM   2039 C  CB  . ASP A 1 197 ? 2.968   1.651   -36.870 1.00 34.69  ? 197 ASP A CB  1 
ATOM   2040 C  CG  . ASP A 1 197 ? 2.926   0.494   -35.882 1.00 34.29  ? 197 ASP A CG  1 
ATOM   2041 O  OD1 . ASP A 1 197 ? 3.148   -0.662  -36.337 1.00 36.54  ? 197 ASP A OD1 1 
ATOM   2042 O  OD2 . ASP A 1 197 ? 2.663   0.747   -34.700 1.00 33.36  ? 197 ASP A OD2 1 
ATOM   2043 N  N   . THR A 1 198 ? 0.941   -0.338  -38.248 1.00 31.88  ? 198 THR A N   1 
ATOM   2044 C  CA  . THR A 1 198 ? -0.434  -0.785  -38.517 1.00 29.95  ? 198 THR A CA  1 
ATOM   2045 C  C   . THR A 1 198 ? -1.005  -1.313  -37.219 1.00 26.39  ? 198 THR A C   1 
ATOM   2046 O  O   . THR A 1 198 ? -0.229  -1.536  -36.272 1.00 26.53  ? 198 THR A O   1 
ATOM   2047 C  CB  . THR A 1 198 ? -0.445  -1.757  -39.697 1.00 32.68  ? 198 THR A CB  1 
ATOM   2048 O  OG1 . THR A 1 198 ? 0.389   -2.860  -39.352 1.00 34.19  ? 198 THR A OG1 1 
ATOM   2049 C  CG2 . THR A 1 198 ? 0.036   -1.087  -40.965 1.00 32.56  ? 198 THR A CG2 1 
ATOM   2050 N  N   . THR A 1 199 ? -2.320  -1.431  -37.171 1.00 24.70  ? 199 THR A N   1 
ATOM   2051 C  CA  . THR A 1 199 ? -3.047  -1.976  -36.017 1.00 23.57  ? 199 THR A CA  1 
ATOM   2052 C  C   . THR A 1 199 ? -3.056  -3.494  -36.100 1.00 23.23  ? 199 THR A C   1 
ATOM   2053 O  O   . THR A 1 199 ? -3.277  -4.042  -37.205 1.00 23.88  ? 199 THR A O   1 
ATOM   2054 C  CB  . THR A 1 199 ? -4.456  -1.396  -35.955 1.00 24.54  ? 199 THR A CB  1 
ATOM   2055 O  OG1 . THR A 1 199 ? -4.212  0.001   -35.865 1.00 23.87  ? 199 THR A OG1 1 
ATOM   2056 C  CG2 . THR A 1 199 ? -5.260  -1.909  -34.779 1.00 23.91  ? 199 THR A CG2 1 
ATOM   2057 N  N   . ILE A 1 200 ? -2.884  -4.141  -34.949 1.00 22.54  ? 200 ILE A N   1 
ATOM   2058 C  CA  . ILE A 1 200 ? -2.811  -5.619  -34.885 1.00 23.28  ? 200 ILE A CA  1 
ATOM   2059 C  C   . ILE A 1 200 ? -4.266  -6.122  -34.838 1.00 22.75  ? 200 ILE A C   1 
ATOM   2060 O  O   . ILE A 1 200 ? -4.872  -6.205  -33.722 1.00 21.66  ? 200 ILE A O   1 
ATOM   2061 C  CB  . ILE A 1 200 ? -1.960  -6.082  -33.685 1.00 23.22  ? 200 ILE A CB  1 
ATOM   2062 C  CG1 . ILE A 1 200 ? -0.560  -5.447  -33.679 1.00 23.71  ? 200 ILE A CG1 1 
ATOM   2063 C  CG2 . ILE A 1 200 ? -1.900  -7.592  -33.665 1.00 22.70  ? 200 ILE A CG2 1 
ATOM   2064 C  CD1 . ILE A 1 200 ? 0.131   -5.447  -32.320 1.00 23.08  ? 200 ILE A CD1 1 
ATOM   2065 N  N   . THR A 1 201 ? -4.816  -6.452  -35.994 1.00 22.86  ? 201 THR A N   1 
ATOM   2066 C  CA  . THR A 1 201 ? -6.272  -6.767  -36.157 1.00 23.37  ? 201 THR A CA  1 
ATOM   2067 C  C   . THR A 1 201 ? -6.672  -7.960  -35.272 1.00 22.75  ? 201 THR A C   1 
ATOM   2068 O  O   . THR A 1 201 ? -7.721  -7.877  -34.564 1.00 23.03  ? 201 THR A O   1 
ATOM   2069 C  CB  . THR A 1 201 ? -6.587  -7.000  -37.637 1.00 22.39  ? 201 THR A CB  1 
ATOM   2070 O  OG1 . THR A 1 201 ? -6.021  -5.877  -38.319 1.00 19.17  ? 201 THR A OG1 1 
ATOM   2071 C  CG2 . THR A 1 201 ? -8.067  -7.181  -37.892 1.00 22.73  ? 201 THR A CG2 1 
ATOM   2072 N  N   . VAL A 1 202 ? -5.872  -9.025  -35.261 1.00 21.47  ? 202 VAL A N   1 
ATOM   2073 C  CA  . VAL A 1 202 ? -6.202  -10.240 -34.469 1.00 21.27  ? 202 VAL A CA  1 
ATOM   2074 C  C   . VAL A 1 202 ? -6.318  -9.847  -32.990 1.00 21.77  ? 202 VAL A C   1 
ATOM   2075 O  O   . VAL A 1 202 ? -7.219  -10.373 -32.298 1.00 20.47  ? 202 VAL A O   1 
ATOM   2076 C  CB  . VAL A 1 202 ? -5.243  -11.419 -34.723 1.00 22.15  ? 202 VAL A CB  1 
ATOM   2077 C  CG1 . VAL A 1 202 ? -3.797  -11.173 -34.283 1.00 22.81  ? 202 VAL A CG1 1 
ATOM   2078 C  CG2 . VAL A 1 202 ? -5.791  -12.671 -34.062 1.00 23.10  ? 202 VAL A CG2 1 
ATOM   2079 N  N   . ASN A 1 203 ? -5.504  -8.906  -32.513 1.00 21.53  ? 203 ASN A N   1 
ATOM   2080 C  CA  . ASN A 1 203 ? -5.533  -8.511  -31.075 1.00 22.09  ? 203 ASN A CA  1 
ATOM   2081 C  C   . ASN A 1 203 ? -6.818  -7.723  -30.801 1.00 21.99  ? 203 ASN A C   1 
ATOM   2082 O  O   . ASN A 1 203 ? -7.464  -7.986  -29.758 1.00 22.81  ? 203 ASN A O   1 
ATOM   2083 C  CB  . ASN A 1 203 ? -4.265  -7.765  -30.658 1.00 20.58  ? 203 ASN A CB  1 
ATOM   2084 C  CG  . ASN A 1 203 ? -3.039  -8.654  -30.600 1.00 21.73  ? 203 ASN A CG  1 
ATOM   2085 O  OD1 . ASN A 1 203 ? -3.110  -9.865  -30.892 1.00 20.48  ? 203 ASN A OD1 1 
ATOM   2086 N  ND2 . ASN A 1 203 ? -1.918  -8.066  -30.175 1.00 19.86  ? 203 ASN A ND2 1 
ATOM   2087 N  N   . VAL A 1 204 ? -7.172  -6.798  -31.691 1.00 23.20  ? 204 VAL A N   1 
ATOM   2088 C  CA  . VAL A 1 204 ? -8.404  -5.960  -31.551 1.00 23.51  ? 204 VAL A CA  1 
ATOM   2089 C  C   . VAL A 1 204 ? -9.622  -6.877  -31.432 1.00 24.32  ? 204 VAL A C   1 
ATOM   2090 O  O   . VAL A 1 204 ? -10.455 -6.614  -30.527 1.00 24.58  ? 204 VAL A O   1 
ATOM   2091 C  CB  . VAL A 1 204 ? -8.594  -4.989  -32.717 1.00 26.31  ? 204 VAL A CB  1 
ATOM   2092 C  CG1 . VAL A 1 204 ? -9.977  -4.342  -32.646 1.00 27.70  ? 204 VAL A CG1 1 
ATOM   2093 C  CG2 . VAL A 1 204 ? -7.497  -3.920  -32.761 1.00 25.70  ? 204 VAL A CG2 1 
ATOM   2094 N  N   . LEU A 1 205 ? -9.681  -7.931  -32.256 1.00 23.21  ? 205 LEU A N   1 
ATOM   2095 C  CA  . LEU A 1 205 ? -10.812 -8.898  -32.290 1.00 24.58  ? 205 LEU A CA  1 
ATOM   2096 C  C   . LEU A 1 205 ? -10.899 -9.651  -30.965 1.00 28.39  ? 205 LEU A C   1 
ATOM   2097 O  O   . LEU A 1 205 ? -12.035 -9.831  -30.474 1.00 28.32  ? 205 LEU A O   1 
ATOM   2098 C  CB  . LEU A 1 205 ? -10.660 -9.851  -33.474 1.00 22.81  ? 205 LEU A CB  1 
ATOM   2099 C  CG  . LEU A 1 205 ? -10.922 -9.210  -34.838 1.00 23.63  ? 205 LEU A CG  1 
ATOM   2100 C  CD1 . LEU A 1 205 ? -10.712 -10.200 -35.975 1.00 23.64  ? 205 LEU A CD1 1 
ATOM   2101 C  CD2 . LEU A 1 205 ? -12.325 -8.620  -34.901 1.00 23.62  ? 205 LEU A CD2 1 
ATOM   2102 N  N   . ALA A 1 206 ? -9.760  -10.086 -30.419 1.00 28.82  ? 206 ALA A N   1 
ATOM   2103 C  CA  . ALA A 1 206 ? -9.667  -10.827 -29.140 1.00 30.29  ? 206 ALA A CA  1 
ATOM   2104 C  C   . ALA A 1 206 ? -10.210 -9.931  -28.034 1.00 28.23  ? 206 ALA A C   1 
ATOM   2105 O  O   . ALA A 1 206 ? -10.949 -10.420 -27.187 1.00 29.38  ? 206 ALA A O   1 
ATOM   2106 C  CB  . ALA A 1 206 ? -8.237  -11.229 -28.839 1.00 30.53  ? 206 ALA A CB  1 
ATOM   2107 N  N   . TRP A 1 207 ? -9.805  -8.671  -28.066 1.00 27.69  ? 207 TRP A N   1 
ATOM   2108 C  CA  . TRP A 1 207 ? -10.194 -7.649  -27.070 1.00 30.44  ? 207 TRP A CA  1 
ATOM   2109 C  C   . TRP A 1 207 ? -11.690 -7.331  -27.196 1.00 31.56  ? 207 TRP A C   1 
ATOM   2110 O  O   . TRP A 1 207 ? -12.313 -7.079  -26.156 1.00 31.90  ? 207 TRP A O   1 
ATOM   2111 C  CB  . TRP A 1 207 ? -9.308  -6.423  -27.249 1.00 30.15  ? 207 TRP A CB  1 
ATOM   2112 C  CG  . TRP A 1 207 ? -9.676  -5.234  -26.425 1.00 31.68  ? 207 TRP A CG  1 
ATOM   2113 C  CD1 . TRP A 1 207 ? -9.350  -4.984  -25.123 1.00 34.51  ? 207 TRP A CD1 1 
ATOM   2114 C  CD2 . TRP A 1 207 ? -10.392 -4.080  -26.895 1.00 32.76  ? 207 TRP A CD2 1 
ATOM   2115 N  NE1 . TRP A 1 207 ? -9.798  -3.744  -24.754 1.00 32.87  ? 207 TRP A NE1 1 
ATOM   2116 C  CE2 . TRP A 1 207 ? -10.438 -3.165  -25.823 1.00 35.91  ? 207 TRP A CE2 1 
ATOM   2117 C  CE3 . TRP A 1 207 ? -10.963 -3.720  -28.123 1.00 33.05  ? 207 TRP A CE3 1 
ATOM   2118 C  CZ2 . TRP A 1 207 ? -11.084 -1.934  -25.938 1.00 34.62  ? 207 TRP A CZ2 1 
ATOM   2119 C  CZ3 . TRP A 1 207 ? -11.577 -2.489  -28.238 1.00 34.33  ? 207 TRP A CZ3 1 
ATOM   2120 C  CH2 . TRP A 1 207 ? -11.647 -1.618  -27.152 1.00 34.15  ? 207 TRP A CH2 1 
ATOM   2121 N  N   . LEU A 1 208 ? -12.259 -7.387  -28.402 1.00 30.76  ? 208 LEU A N   1 
ATOM   2122 C  CA  . LEU A 1 208 ? -13.724 -7.227  -28.584 1.00 30.01  ? 208 LEU A CA  1 
ATOM   2123 C  C   . LEU A 1 208 ? -14.426 -8.434  -27.953 1.00 31.39  ? 208 LEU A C   1 
ATOM   2124 O  O   . LEU A 1 208 ? -15.350 -8.212  -27.153 1.00 32.57  ? 208 LEU A O   1 
ATOM   2125 C  CB  . LEU A 1 208 ? -14.084 -7.051  -30.059 1.00 26.68  ? 208 LEU A CB  1 
ATOM   2126 C  CG  . LEU A 1 208 ? -13.765 -5.672  -30.635 1.00 26.18  ? 208 LEU A CG  1 
ATOM   2127 C  CD1 . LEU A 1 208 ? -14.203 -5.584  -32.083 1.00 26.15  ? 208 LEU A CD1 1 
ATOM   2128 C  CD2 . LEU A 1 208 ? -14.383 -4.538  -29.818 1.00 27.31  ? 208 LEU A CD2 1 
ATOM   2129 N  N   . TYR A 1 209 ? -13.978 -9.651  -28.253 1.00 30.01  ? 209 TYR A N   1 
ATOM   2130 C  CA  . TYR A 1 209 ? -14.427 -10.903 -27.578 1.00 30.98  ? 209 TYR A CA  1 
ATOM   2131 C  C   . TYR A 1 209 ? -14.307 -10.753 -26.051 1.00 32.10  ? 209 TYR A C   1 
ATOM   2132 O  O   . TYR A 1 209 ? -15.241 -11.110 -25.324 1.00 34.22  ? 209 TYR A O   1 
ATOM   2133 C  CB  . TYR A 1 209 ? -13.644 -12.113 -28.102 1.00 29.96  ? 209 TYR A CB  1 
ATOM   2134 C  CG  . TYR A 1 209 ? -14.176 -12.693 -29.388 1.00 26.93  ? 209 TYR A CG  1 
ATOM   2135 C  CD1 . TYR A 1 209 ? -15.467 -13.198 -29.463 1.00 27.68  ? 209 TYR A CD1 1 
ATOM   2136 C  CD2 . TYR A 1 209 ? -13.392 -12.757 -30.527 1.00 27.13  ? 209 TYR A CD2 1 
ATOM   2137 C  CE1 . TYR A 1 209 ? -15.956 -13.763 -30.634 1.00 29.61  ? 209 TYR A CE1 1 
ATOM   2138 C  CE2 . TYR A 1 209 ? -13.865 -13.299 -31.712 1.00 26.51  ? 209 TYR A CE2 1 
ATOM   2139 C  CZ  . TYR A 1 209 ? -15.156 -13.806 -31.768 1.00 29.48  ? 209 TYR A CZ  1 
ATOM   2140 O  OH  . TYR A 1 209 ? -15.643 -14.347 -32.925 1.00 25.89  ? 209 TYR A OH  1 
ATOM   2141 N  N   . ALA A 1 210 ? -13.207 -10.203 -25.544 1.00 34.59  ? 210 ALA A N   1 
ATOM   2142 C  CA  . ALA A 1 210 ? -13.057 -9.903  -24.098 1.00 34.48  ? 210 ALA A CA  1 
ATOM   2143 C  C   . ALA A 1 210 ? -14.179 -8.967  -23.628 1.00 36.80  ? 210 ALA A C   1 
ATOM   2144 O  O   . ALA A 1 210 ? -14.749 -9.220  -22.547 1.00 39.37  ? 210 ALA A O   1 
ATOM   2145 C  CB  . ALA A 1 210 ? -11.716 -9.290  -23.814 1.00 36.10  ? 210 ALA A CB  1 
ATOM   2146 N  N   . ALA A 1 211 ? -14.476 -7.904  -24.381 1.00 35.06  ? 211 ALA A N   1 
ATOM   2147 C  CA  . ALA A 1 211 ? -15.563 -6.956  -24.037 1.00 35.69  ? 211 ALA A CA  1 
ATOM   2148 C  C   . ALA A 1 211 ? -16.875 -7.742  -23.890 1.00 33.91  ? 211 ALA A C   1 
ATOM   2149 O  O   . ALA A 1 211 ? -17.566 -7.507  -22.897 1.00 35.23  ? 211 ALA A O   1 
ATOM   2150 C  CB  . ALA A 1 211 ? -15.675 -5.841  -25.053 1.00 33.98  ? 211 ALA A CB  1 
ATOM   2151 N  N   . VAL A 1 212 ? -17.172 -8.667  -24.809 1.00 31.79  ? 212 VAL A N   1 
ATOM   2152 C  CA  . VAL A 1 212 ? -18.458 -9.419  -24.804 1.00 35.56  ? 212 VAL A CA  1 
ATOM   2153 C  C   . VAL A 1 212 ? -18.490 -10.317 -23.555 1.00 41.36  ? 212 VAL A C   1 
ATOM   2154 O  O   . VAL A 1 212 ? -19.530 -10.373 -22.881 1.00 41.25  ? 212 VAL A O   1 
ATOM   2155 C  CB  . VAL A 1 212 ? -18.661 -10.194 -26.117 1.00 34.80  ? 212 VAL A CB  1 
ATOM   2156 C  CG1 . VAL A 1 212 ? -19.756 -11.249 -26.007 1.00 35.50  ? 212 VAL A CG1 1 
ATOM   2157 C  CG2 . VAL A 1 212 ? -18.954 -9.241  -27.270 1.00 32.88  ? 212 VAL A CG2 1 
ATOM   2158 N  N   . ILE A 1 213 ? -17.374 -10.961 -23.233 1.00 42.39  ? 213 ILE A N   1 
ATOM   2159 C  CA  . ILE A 1 213 ? -17.238 -11.850 -22.044 1.00 43.57  ? 213 ILE A CA  1 
ATOM   2160 C  C   . ILE A 1 213 ? -17.497 -11.045 -20.758 1.00 42.55  ? 213 ILE A C   1 
ATOM   2161 O  O   . ILE A 1 213 ? -18.178 -11.580 -19.880 1.00 45.66  ? 213 ILE A O   1 
ATOM   2162 C  CB  . ILE A 1 213 ? -15.855 -12.531 -22.041 1.00 45.99  ? 213 ILE A CB  1 
ATOM   2163 C  CG1 . ILE A 1 213 ? -15.744 -13.562 -23.173 1.00 52.04  ? 213 ILE A CG1 1 
ATOM   2164 C  CG2 . ILE A 1 213 ? -15.553 -13.142 -20.678 1.00 47.16  ? 213 ILE A CG2 1 
ATOM   2165 C  CD1 . ILE A 1 213 ? -14.331 -14.089 -23.416 1.00 52.32  ? 213 ILE A CD1 1 
ATOM   2166 N  N   . ASN A 1 214 ? -16.965 -9.827  -20.632 1.00 42.71  ? 214 ASN A N   1 
ATOM   2167 C  CA  . ASN A 1 214 ? -17.134 -8.964  -19.431 1.00 46.83  ? 214 ASN A CA  1 
ATOM   2168 C  C   . ASN A 1 214 ? -18.463 -8.180  -19.525 1.00 43.69  ? 214 ASN A C   1 
ATOM   2169 O  O   . ASN A 1 214 ? -18.668 -7.296  -18.682 1.00 42.19  ? 214 ASN A O   1 
ATOM   2170 C  CB  . ASN A 1 214 ? -15.907 -8.064  -19.223 1.00 55.69  ? 214 ASN A CB  1 
ATOM   2171 C  CG  . ASN A 1 214 ? -14.678 -8.797  -18.691 1.00 66.67  ? 214 ASN A CG  1 
ATOM   2172 O  OD1 . ASN A 1 214 ? -14.495 -8.933  -17.476 1.00 65.69  ? 214 ASN A OD1 1 
ATOM   2173 N  ND2 . ASN A 1 214 ? -13.797 -9.238  -19.584 1.00 66.39  ? 214 ASN A ND2 1 
ATOM   2174 N  N   . GLY A 1 215 ? -19.301 -8.458  -20.536 1.00 40.66  ? 215 GLY A N   1 
ATOM   2175 C  CA  . GLY A 1 215 ? -20.739 -8.114  -20.599 1.00 43.17  ? 215 GLY A CA  1 
ATOM   2176 C  C   . GLY A 1 215 ? -21.122 -6.902  -21.453 1.00 45.15  ? 215 GLY A C   1 
ATOM   2177 O  O   . GLY A 1 215 ? -22.186 -6.327  -21.207 1.00 50.25  ? 215 GLY A O   1 
ATOM   2178 N  N   A ASP A 1 216 ? -20.264 -6.522  -22.411 0.27 45.42  ? 216 ASP A N   1 
ATOM   2179 N  N   B ASP A 1 216 ? -20.305 -6.548  -22.450 0.23 45.28  ? 216 ASP A N   1 
ATOM   2180 N  N   C ASP A 1 216 ? -20.264 -6.522  -22.411 0.27 45.42  ? 216 ASP A N   1 
ATOM   2181 N  N   D ASP A 1 216 ? -20.305 -6.548  -22.450 0.23 45.28  ? 216 ASP A N   1 
ATOM   2182 C  CA  A ASP A 1 216 ? -20.449 -5.370  -23.339 0.27 44.53  ? 216 ASP A CA  1 
ATOM   2183 C  CA  B ASP A 1 216 ? -20.527 -5.351  -23.306 0.23 44.45  ? 216 ASP A CA  1 
ATOM   2184 C  CA  C ASP A 1 216 ? -20.449 -5.370  -23.339 0.27 44.53  ? 216 ASP A CA  1 
ATOM   2185 C  CA  D ASP A 1 216 ? -20.527 -5.351  -23.306 0.23 44.45  ? 216 ASP A CA  1 
ATOM   2186 C  C   A ASP A 1 216 ? -20.869 -5.899  -24.716 0.27 44.51  ? 216 ASP A C   1 
ATOM   2187 C  C   B ASP A 1 216 ? -20.841 -5.801  -24.737 0.23 44.21  ? 216 ASP A C   1 
ATOM   2188 C  C   C ASP A 1 216 ? -20.869 -5.899  -24.716 0.27 44.51  ? 216 ASP A C   1 
ATOM   2189 C  C   D ASP A 1 216 ? -20.841 -5.801  -24.737 0.23 44.21  ? 216 ASP A C   1 
ATOM   2190 O  O   A ASP A 1 216 ? -20.044 -6.605  -25.330 0.27 46.29  ? 216 ASP A O   1 
ATOM   2191 O  O   B ASP A 1 216 ? -19.922 -6.326  -25.399 0.23 45.32  ? 216 ASP A O   1 
ATOM   2192 O  O   C ASP A 1 216 ? -20.044 -6.605  -25.330 0.27 46.29  ? 216 ASP A O   1 
ATOM   2193 O  O   D ASP A 1 216 ? -19.922 -6.326  -25.399 0.23 45.32  ? 216 ASP A O   1 
ATOM   2194 C  CB  A ASP A 1 216 ? -19.155 -4.561  -23.499 0.27 45.37  ? 216 ASP A CB  1 
ATOM   2195 C  CB  B ASP A 1 216 ? -19.327 -4.404  -23.255 0.23 45.16  ? 216 ASP A CB  1 
ATOM   2196 C  CB  C ASP A 1 216 ? -19.155 -4.561  -23.499 0.27 45.37  ? 216 ASP A CB  1 
ATOM   2197 C  CB  D ASP A 1 216 ? -19.327 -4.404  -23.255 0.23 45.16  ? 216 ASP A CB  1 
ATOM   2198 C  CG  A ASP A 1 216 ? -18.743 -3.729  -22.293 0.27 45.33  ? 216 ASP A CG  1 
ATOM   2199 C  CG  B ASP A 1 216 ? -19.738 -2.943  -23.269 0.23 45.24  ? 216 ASP A CG  1 
ATOM   2200 C  CG  C ASP A 1 216 ? -18.743 -3.729  -22.293 0.27 45.33  ? 216 ASP A CG  1 
ATOM   2201 C  CG  D ASP A 1 216 ? -19.738 -2.943  -23.269 0.23 45.24  ? 216 ASP A CG  1 
ATOM   2202 O  OD1 A ASP A 1 216 ? -19.522 -3.672  -21.322 0.27 46.65  ? 216 ASP A OD1 1 
ATOM   2203 O  OD1 B ASP A 1 216 ? -20.921 -2.679  -23.579 0.23 44.75  ? 216 ASP A OD1 1 
ATOM   2204 O  OD1 C ASP A 1 216 ? -19.522 -3.672  -21.322 0.27 46.65  ? 216 ASP A OD1 1 
ATOM   2205 O  OD1 D ASP A 1 216 ? -20.921 -2.679  -23.579 0.23 44.75  ? 216 ASP A OD1 1 
ATOM   2206 O  OD2 A ASP A 1 216 ? -17.637 -3.141  -22.337 0.27 43.36  ? 216 ASP A OD2 1 
ATOM   2207 O  OD2 B ASP A 1 216 ? -18.884 -2.086  -22.953 0.23 44.64  ? 216 ASP A OD2 1 
ATOM   2208 O  OD2 C ASP A 1 216 ? -17.637 -3.141  -22.337 0.27 43.36  ? 216 ASP A OD2 1 
ATOM   2209 O  OD2 D ASP A 1 216 ? -18.884 -2.086  -22.953 0.23 44.64  ? 216 ASP A OD2 1 
ATOM   2210 N  N   . ARG A 1 217 ? -22.082 -5.571  -25.190 1.00 42.68  ? 217 ARG A N   1 
ATOM   2211 C  CA  . ARG A 1 217 ? -22.586 -6.039  -26.526 1.00 39.15  ? 217 ARG A CA  1 
ATOM   2212 C  C   . ARG A 1 217 ? -23.045 -4.891  -27.429 1.00 34.74  ? 217 ARG A C   1 
ATOM   2213 O  O   . ARG A 1 217 ? -23.437 -5.176  -28.606 1.00 28.15  ? 217 ARG A O   1 
ATOM   2214 C  CB  . ARG A 1 217 ? -23.741 -7.022  -26.347 1.00 40.05  ? 217 ARG A CB  1 
ATOM   2215 C  CG  . ARG A 1 217 ? -23.400 -8.162  -25.404 1.00 42.86  ? 217 ARG A CG  1 
ATOM   2216 C  CD  . ARG A 1 217 ? -24.510 -9.169  -25.319 1.00 46.28  ? 217 ARG A CD  1 
ATOM   2217 N  NE  . ARG A 1 217 ? -24.920 -9.609  -26.648 1.00 49.80  ? 217 ARG A NE  1 
ATOM   2218 C  CZ  . ARG A 1 217 ? -24.637 -10.791 -27.204 1.00 52.20  ? 217 ARG A CZ  1 
ATOM   2219 N  NH1 . ARG A 1 217 ? -23.915 -11.697 -26.558 1.00 48.63  ? 217 ARG A NH1 1 
ATOM   2220 N  NH2 . ARG A 1 217 ? -25.095 -11.053 -28.419 1.00 53.16  ? 217 ARG A NH2 1 
ATOM   2221 N  N   . TRP A 1 218 ? -22.946 -3.651  -26.947 1.00 32.23  ? 218 TRP A N   1 
ATOM   2222 C  CA  . TRP A 1 218 ? -23.481 -2.455  -27.642 1.00 29.41  ? 218 TRP A CA  1 
ATOM   2223 C  C   . TRP A 1 218 ? -22.992 -2.366  -29.099 1.00 30.97  ? 218 TRP A C   1 
ATOM   2224 O  O   . TRP A 1 218 ? -23.770 -1.835  -29.916 1.00 32.99  ? 218 TRP A O   1 
ATOM   2225 C  CB  . TRP A 1 218 ? -23.157 -1.182  -26.859 1.00 28.70  ? 218 TRP A CB  1 
ATOM   2226 C  CG  . TRP A 1 218 ? -21.756 -0.664  -26.919 1.00 28.63  ? 218 TRP A CG  1 
ATOM   2227 C  CD1 . TRP A 1 218 ? -20.853 -0.702  -25.895 1.00 29.81  ? 218 TRP A CD1 1 
ATOM   2228 C  CD2 . TRP A 1 218 ? -21.128 0.098   -27.973 1.00 30.97  ? 218 TRP A CD2 1 
ATOM   2229 N  NE1 . TRP A 1 218 ? -19.711 -0.026  -26.237 1.00 31.73  ? 218 TRP A NE1 1 
ATOM   2230 C  CE2 . TRP A 1 218 ? -19.846 0.467   -27.511 1.00 31.81  ? 218 TRP A CE2 1 
ATOM   2231 C  CE3 . TRP A 1 218 ? -21.505 0.498   -29.262 1.00 33.91  ? 218 TRP A CE3 1 
ATOM   2232 C  CZ2 . TRP A 1 218 ? -18.945 1.193   -28.296 1.00 31.30  ? 218 TRP A CZ2 1 
ATOM   2233 C  CZ3 . TRP A 1 218 ? -20.623 1.225   -30.034 1.00 32.78  ? 218 TRP A CZ3 1 
ATOM   2234 C  CH2 . TRP A 1 218 ? -19.352 1.556   -29.560 1.00 31.37  ? 218 TRP A CH2 1 
ATOM   2235 N  N   . PHE A 1 219 ? -21.787 -2.866  -29.419 1.00 27.43  ? 219 PHE A N   1 
ATOM   2236 C  CA  . PHE A 1 219 ? -21.090 -2.650  -30.716 1.00 27.53  ? 219 PHE A CA  1 
ATOM   2237 C  C   . PHE A 1 219 ? -21.321 -3.840  -31.656 1.00 27.67  ? 219 PHE A C   1 
ATOM   2238 O  O   . PHE A 1 219 ? -20.866 -3.793  -32.806 1.00 29.03  ? 219 PHE A O   1 
ATOM   2239 C  CB  . PHE A 1 219 ? -19.582 -2.452  -30.512 1.00 28.81  ? 219 PHE A CB  1 
ATOM   2240 C  CG  . PHE A 1 219 ? -18.955 -3.504  -29.632 1.00 27.31  ? 219 PHE A CG  1 
ATOM   2241 C  CD1 . PHE A 1 219 ? -18.632 -4.754  -30.135 1.00 26.45  ? 219 PHE A CD1 1 
ATOM   2242 C  CD2 . PHE A 1 219 ? -18.781 -3.262  -28.281 1.00 27.10  ? 219 PHE A CD2 1 
ATOM   2243 C  CE1 . PHE A 1 219 ? -18.127 -5.738  -29.303 1.00 25.97  ? 219 PHE A CE1 1 
ATOM   2244 C  CE2 . PHE A 1 219 ? -18.261 -4.246  -27.461 1.00 26.96  ? 219 PHE A CE2 1 
ATOM   2245 C  CZ  . PHE A 1 219 ? -17.951 -5.479  -27.973 1.00 25.76  ? 219 PHE A CZ  1 
ATOM   2246 N  N   . LEU A 1 220 ? -21.988 -4.895  -31.204 1.00 29.26  ? 220 LEU A N   1 
ATOM   2247 C  CA  . LEU A 1 220 ? -22.357 -6.025  -32.102 1.00 30.00  ? 220 LEU A CA  1 
ATOM   2248 C  C   . LEU A 1 220 ? -23.391 -5.548  -33.124 1.00 32.63  ? 220 LEU A C   1 
ATOM   2249 O  O   . LEU A 1 220 ? -24.144 -4.596  -32.831 1.00 33.93  ? 220 LEU A O   1 
ATOM   2250 C  CB  . LEU A 1 220 ? -22.957 -7.152  -31.275 1.00 32.33  ? 220 LEU A CB  1 
ATOM   2251 C  CG  . LEU A 1 220 ? -22.029 -7.793  -30.253 1.00 34.10  ? 220 LEU A CG  1 
ATOM   2252 C  CD1 . LEU A 1 220 ? -22.772 -8.871  -29.491 1.00 33.90  ? 220 LEU A CD1 1 
ATOM   2253 C  CD2 . LEU A 1 220 ? -20.780 -8.366  -30.928 1.00 36.29  ? 220 LEU A CD2 1 
ATOM   2254 N  N   . ASN A 1 221 ? -23.444 -6.181  -34.282 1.00 31.20  ? 221 ASN A N   1 
ATOM   2255 C  CA  . ASN A 1 221 ? -24.485 -5.870  -35.278 1.00 32.93  ? 221 ASN A CA  1 
ATOM   2256 C  C   . ASN A 1 221 ? -25.006 -7.208  -35.807 1.00 33.66  ? 221 ASN A C   1 
ATOM   2257 O  O   . ASN A 1 221 ? -24.527 -8.260  -35.375 1.00 31.28  ? 221 ASN A O   1 
ATOM   2258 C  CB  . ASN A 1 221 ? -23.950 -4.901  -36.329 1.00 31.52  ? 221 ASN A CB  1 
ATOM   2259 C  CG  . ASN A 1 221 ? -22.892 -5.541  -37.204 1.00 35.62  ? 221 ASN A CG  1 
ATOM   2260 O  OD1 . ASN A 1 221 ? -22.765 -6.766  -37.222 1.00 34.03  ? 221 ASN A OD1 1 
ATOM   2261 N  ND2 . ASN A 1 221 ? -22.137 -4.728  -37.933 1.00 34.56  ? 221 ASN A ND2 1 
ATOM   2262 N  N   . ARG A 1 222 ? -25.955 -7.157  -36.721 1.00 36.19  ? 222 ARG A N   1 
ATOM   2263 C  CA  . ARG A 1 222 ? -26.616 -8.367  -37.255 1.00 41.20  ? 222 ARG A CA  1 
ATOM   2264 C  C   . ARG A 1 222 ? -25.879 -8.775  -38.524 1.00 35.16  ? 222 ARG A C   1 
ATOM   2265 O  O   . ARG A 1 222 ? -26.324 -9.702  -39.153 1.00 34.28  ? 222 ARG A O   1 
ATOM   2266 C  CB  . ARG A 1 222 ? -28.103 -8.094  -37.507 1.00 49.55  ? 222 ARG A CB  1 
ATOM   2267 C  CG  . ARG A 1 222 ? -28.374 -6.862  -38.364 1.00 60.63  ? 222 ARG A CG  1 
ATOM   2268 C  CD  . ARG A 1 222 ? -29.803 -6.816  -38.878 1.00 68.62  ? 222 ARG A CD  1 
ATOM   2269 N  NE  . ARG A 1 222 ? -30.044 -5.772  -39.869 1.00 74.66  ? 222 ARG A NE  1 
ATOM   2270 C  CZ  . ARG A 1 222 ? -29.941 -5.911  -41.194 1.00 80.03  ? 222 ARG A CZ  1 
ATOM   2271 N  NH1 . ARG A 1 222 ? -29.576 -7.064  -41.740 1.00 86.19  ? 222 ARG A NH1 1 
ATOM   2272 N  NH2 . ARG A 1 222 ? -30.199 -4.879  -41.978 1.00 75.72  ? 222 ARG A NH2 1 
ATOM   2273 N  N   . PHE A 1 223 ? -24.772 -8.117  -38.875 1.00 34.53  ? 223 PHE A N   1 
ATOM   2274 C  CA  . PHE A 1 223 ? -24.035 -8.418  -40.124 1.00 33.14  ? 223 PHE A CA  1 
ATOM   2275 C  C   . PHE A 1 223 ? -22.946 -9.464  -39.898 1.00 32.31  ? 223 PHE A C   1 
ATOM   2276 O  O   . PHE A 1 223 ? -22.459 -9.677  -38.774 1.00 34.20  ? 223 PHE A O   1 
ATOM   2277 C  CB  . PHE A 1 223 ? -23.451 -7.152  -40.747 1.00 37.48  ? 223 PHE A CB  1 
ATOM   2278 C  CG  . PHE A 1 223 ? -24.526 -6.230  -41.240 1.00 38.83  ? 223 PHE A CG  1 
ATOM   2279 C  CD1 . PHE A 1 223 ? -25.186 -6.492  -42.425 1.00 42.47  ? 223 PHE A CD1 1 
ATOM   2280 C  CD2 . PHE A 1 223 ? -24.932 -5.154  -40.470 1.00 46.61  ? 223 PHE A CD2 1 
ATOM   2281 C  CE1 . PHE A 1 223 ? -26.202 -5.655  -42.860 1.00 51.00  ? 223 PHE A CE1 1 
ATOM   2282 C  CE2 . PHE A 1 223 ? -25.949 -4.316  -40.904 1.00 52.00  ? 223 PHE A CE2 1 
ATOM   2283 C  CZ  . PHE A 1 223 ? -26.581 -4.567  -42.102 1.00 51.16  ? 223 PHE A CZ  1 
ATOM   2284 N  N   . THR A 1 224 ? -22.585 -10.097 -41.007 1.00 30.46  ? 224 THR A N   1 
ATOM   2285 C  CA  . THR A 1 224 ? -21.349 -10.886 -41.169 1.00 32.18  ? 224 THR A CA  1 
ATOM   2286 C  C   . THR A 1 224 ? -20.609 -10.302 -42.364 1.00 30.42  ? 224 THR A C   1 
ATOM   2287 O  O   . THR A 1 224 ? -21.038 -9.260  -42.897 1.00 30.64  ? 224 THR A O   1 
ATOM   2288 C  CB  . THR A 1 224 ? -21.638 -12.382 -41.310 1.00 34.01  ? 224 THR A CB  1 
ATOM   2289 O  OG1 . THR A 1 224 ? -20.405 -13.068 -41.070 1.00 39.23  ? 224 THR A OG1 1 
ATOM   2290 C  CG2 . THR A 1 224 ? -22.198 -12.733 -42.671 1.00 33.15  ? 224 THR A CG2 1 
ATOM   2291 N  N   . THR A 1 225 ? -19.474 -10.891 -42.687 1.00 28.54  ? 225 THR A N   1 
ATOM   2292 C  CA  . THR A 1 225 ? -18.593 -10.419 -43.766 1.00 29.50  ? 225 THR A CA  1 
ATOM   2293 C  C   . THR A 1 225 ? -17.837 -11.625 -44.300 1.00 26.59  ? 225 THR A C   1 
ATOM   2294 O  O   . THR A 1 225 ? -17.752 -12.594 -43.561 1.00 29.60  ? 225 THR A O   1 
ATOM   2295 C  CB  . THR A 1 225 ? -17.666 -9.319  -43.250 1.00 29.61  ? 225 THR A CB  1 
ATOM   2296 O  OG1 . THR A 1 225 ? -16.859 -8.954  -44.368 1.00 25.91  ? 225 THR A OG1 1 
ATOM   2297 C  CG2 . THR A 1 225 ? -16.833 -9.776  -42.070 1.00 33.22  ? 225 THR A CG2 1 
ATOM   2298 N  N   . THR A 1 226 ? -17.347 -11.562 -45.534 1.00 26.72  ? 226 THR A N   1 
ATOM   2299 C  CA  . THR A 1 226 ? -16.326 -12.516 -46.042 1.00 29.19  ? 226 THR A CA  1 
ATOM   2300 C  C   . THR A 1 226 ? -14.977 -12.061 -45.488 1.00 29.83  ? 226 THR A C   1 
ATOM   2301 O  O   . THR A 1 226 ? -14.823 -10.844 -45.188 1.00 27.62  ? 226 THR A O   1 
ATOM   2302 C  CB  . THR A 1 226 ? -16.276 -12.605 -47.573 1.00 28.87  ? 226 THR A CB  1 
ATOM   2303 O  OG1 . THR A 1 226 ? -15.747 -11.385 -48.109 1.00 28.18  ? 226 THR A OG1 1 
ATOM   2304 C  CG2 . THR A 1 226 ? -17.634 -12.934 -48.157 1.00 27.11  ? 226 THR A CG2 1 
ATOM   2305 N  N   . LEU A 1 227 ? -14.050 -12.996 -45.353 1.00 31.37  ? 227 LEU A N   1 
ATOM   2306 C  CA  . LEU A 1 227 ? -12.671 -12.676 -44.940 1.00 34.05  ? 227 LEU A CA  1 
ATOM   2307 C  C   . LEU A 1 227 ? -12.148 -11.618 -45.901 1.00 30.67  ? 227 LEU A C   1 
ATOM   2308 O  O   . LEU A 1 227 ? -11.557 -10.644 -45.423 1.00 28.51  ? 227 LEU A O   1 
ATOM   2309 C  CB  . LEU A 1 227 ? -11.790 -13.931 -44.951 1.00 36.33  ? 227 LEU A CB  1 
ATOM   2310 C  CG  . LEU A 1 227 ? -10.376 -13.723 -44.402 1.00 35.24  ? 227 LEU A CG  1 
ATOM   2311 C  CD1 . LEU A 1 227 ? -10.413 -13.037 -43.041 1.00 33.87  ? 227 LEU A CD1 1 
ATOM   2312 C  CD2 . LEU A 1 227 ? -9.626  -15.041 -44.307 1.00 31.13  ? 227 LEU A CD2 1 
ATOM   2313 N  N   . ASN A 1 228 ? -12.363 -11.811 -47.198 1.00 28.58  ? 228 ASN A N   1 
ATOM   2314 C  CA  . ASN A 1 228 ? -11.741 -10.937 -48.220 1.00 32.21  ? 228 ASN A CA  1 
ATOM   2315 C  C   . ASN A 1 228 ? -12.314 -9.519  -48.121 1.00 29.23  ? 228 ASN A C   1 
ATOM   2316 O  O   . ASN A 1 228 ? -11.542 -8.552  -48.188 1.00 27.30  ? 228 ASN A O   1 
ATOM   2317 C  CB  . ASN A 1 228 ? -11.901 -11.457 -49.645 1.00 33.76  ? 228 ASN A CB  1 
ATOM   2318 C  CG  . ASN A 1 228 ? -10.800 -10.884 -50.502 1.00 39.69  ? 228 ASN A CG  1 
ATOM   2319 O  OD1 . ASN A 1 228 ? -9.630  -11.161 -50.249 1.00 50.40  ? 228 ASN A OD1 1 
ATOM   2320 N  ND2 . ASN A 1 228 ? -11.151 -10.025 -51.447 1.00 41.21  ? 228 ASN A ND2 1 
ATOM   2321 N  N   . ASP A 1 229 ? -13.624 -9.397  -47.964 1.00 30.40  ? 229 ASP A N   1 
ATOM   2322 C  CA  . ASP A 1 229 ? -14.295 -8.080  -47.863 1.00 29.72  ? 229 ASP A CA  1 
ATOM   2323 C  C   . ASP A 1 229 ? -13.806 -7.368  -46.599 1.00 28.69  ? 229 ASP A C   1 
ATOM   2324 O  O   . ASP A 1 229 ? -13.634 -6.134  -46.635 1.00 24.52  ? 229 ASP A O   1 
ATOM   2325 C  CB  . ASP A 1 229 ? -15.811 -8.245  -47.882 1.00 32.91  ? 229 ASP A CB  1 
ATOM   2326 C  CG  . ASP A 1 229 ? -16.394 -8.385  -49.277 1.00 31.02  ? 229 ASP A CG  1 
ATOM   2327 O  OD1 . ASP A 1 229 ? -15.668 -8.117  -50.242 1.00 27.81  ? 229 ASP A OD1 1 
ATOM   2328 O  OD2 . ASP A 1 229 ? -17.587 -8.726  -49.365 1.00 31.70  ? 229 ASP A OD2 1 
ATOM   2329 N  N   . PHE A 1 230 ? -13.598 -8.113  -45.514 1.00 27.93  ? 230 PHE A N   1 
ATOM   2330 C  CA  . PHE A 1 230 ? -13.130 -7.535  -44.225 1.00 28.63  ? 230 PHE A CA  1 
ATOM   2331 C  C   . PHE A 1 230 ? -11.750 -6.881  -44.416 1.00 28.66  ? 230 PHE A C   1 
ATOM   2332 O  O   . PHE A 1 230 ? -11.535 -5.740  -43.961 1.00 29.00  ? 230 PHE A O   1 
ATOM   2333 C  CB  . PHE A 1 230 ? -13.120 -8.567  -43.094 1.00 28.38  ? 230 PHE A CB  1 
ATOM   2334 C  CG  . PHE A 1 230 ? -12.401 -8.002  -41.907 1.00 31.07  ? 230 PHE A CG  1 
ATOM   2335 C  CD1 . PHE A 1 230 ? -13.001 -7.041  -41.111 1.00 31.18  ? 230 PHE A CD1 1 
ATOM   2336 C  CD2 . PHE A 1 230 ? -11.060 -8.301  -41.699 1.00 34.24  ? 230 PHE A CD2 1 
ATOM   2337 C  CE1 . PHE A 1 230 ? -12.302 -6.476  -40.056 1.00 32.38  ? 230 PHE A CE1 1 
ATOM   2338 C  CE2 . PHE A 1 230 ? -10.357 -7.726  -40.655 1.00 31.68  ? 230 PHE A CE2 1 
ATOM   2339 C  CZ  . PHE A 1 230 ? -10.977 -6.805  -39.843 1.00 34.98  ? 230 PHE A CZ  1 
ATOM   2340 N  N   . ASN A 1 231 ? -10.859 -7.560  -45.135 1.00 29.64  ? 231 ASN A N   1 
ATOM   2341 C  CA  . ASN A 1 231 ? -9.465  -7.112  -45.366 1.00 29.64  ? 231 ASN A CA  1 
ATOM   2342 C  C   . ASN A 1 231 ? -9.449  -5.889  -46.293 1.00 32.80  ? 231 ASN A C   1 
ATOM   2343 O  O   . ASN A 1 231 ? -8.708  -4.944  -45.994 1.00 34.15  ? 231 ASN A O   1 
ATOM   2344 C  CB  . ASN A 1 231 ? -8.597  -8.288  -45.823 1.00 30.74  ? 231 ASN A CB  1 
ATOM   2345 C  CG  . ASN A 1 231 ? -8.125  -9.133  -44.657 1.00 31.55  ? 231 ASN A CG  1 
ATOM   2346 O  OD1 . ASN A 1 231 ? -7.952  -8.633  -43.544 1.00 31.69  ? 231 ASN A OD1 1 
ATOM   2347 N  ND2 . ASN A 1 231 ? -7.945  -10.422 -44.882 1.00 30.53  ? 231 ASN A ND2 1 
ATOM   2348 N  N   . LEU A 1 232 ? -10.246 -5.866  -47.359 1.00 29.82  ? 232 LEU A N   1 
ATOM   2349 C  CA  . LEU A 1 232 ? -10.329 -4.677  -48.246 1.00 28.89  ? 232 LEU A CA  1 
ATOM   2350 C  C   . LEU A 1 232 ? -10.741 -3.458  -47.412 1.00 30.24  ? 232 LEU A C   1 
ATOM   2351 O  O   . LEU A 1 232 ? -10.193 -2.351  -47.641 1.00 31.01  ? 232 LEU A O   1 
ATOM   2352 C  CB  . LEU A 1 232 ? -11.349 -4.953  -49.347 1.00 30.80  ? 232 LEU A CB  1 
ATOM   2353 C  CG  . LEU A 1 232 ? -10.913 -5.938  -50.425 1.00 29.52  ? 232 LEU A CG  1 
ATOM   2354 C  CD1 . LEU A 1 232 ? -12.096 -6.220  -51.347 1.00 30.98  ? 232 LEU A CD1 1 
ATOM   2355 C  CD2 . LEU A 1 232 ? -9.724  -5.398  -51.211 1.00 28.99  ? 232 LEU A CD2 1 
ATOM   2356 N  N   . VAL A 1 233 ? -11.662 -3.628  -46.460 1.00 27.62  ? 233 VAL A N   1 
ATOM   2357 C  CA  . VAL A 1 233 ? -12.063 -2.484  -45.583 1.00 28.46  ? 233 VAL A CA  1 
ATOM   2358 C  C   . VAL A 1 233 ? -10.944 -2.167  -44.576 1.00 27.95  ? 233 VAL A C   1 
ATOM   2359 O  O   . VAL A 1 233 ? -10.549 -0.979  -44.482 1.00 25.68  ? 233 VAL A O   1 
ATOM   2360 C  CB  . VAL A 1 233 ? -13.389 -2.740  -44.855 1.00 28.89  ? 233 VAL A CB  1 
ATOM   2361 C  CG1 . VAL A 1 233 ? -13.705 -1.611  -43.866 1.00 26.48  ? 233 VAL A CG1 1 
ATOM   2362 C  CG2 . VAL A 1 233 ? -14.513 -2.933  -45.860 1.00 29.31  ? 233 VAL A CG2 1 
ATOM   2363 N  N   . ALA A 1 234 ? -10.453 -3.180  -43.856 1.00 29.27  ? 234 ALA A N   1 
ATOM   2364 C  CA  . ALA A 1 234 ? -9.547  -3.000  -42.696 1.00 31.14  ? 234 ALA A CA  1 
ATOM   2365 C  C   . ALA A 1 234 ? -8.249  -2.328  -43.165 1.00 30.08  ? 234 ALA A C   1 
ATOM   2366 O  O   . ALA A 1 234 ? -7.682  -1.499  -42.435 1.00 34.87  ? 234 ALA A O   1 
ATOM   2367 C  CB  . ALA A 1 234 ? -9.298  -4.336  -42.038 1.00 32.95  ? 234 ALA A CB  1 
ATOM   2368 N  N   . MET A 1 235 ? -7.818  -2.614  -44.384 1.00 31.77  ? 235 MET A N   1 
ATOM   2369 C  CA  . MET A 1 235 ? -6.553  -2.063  -44.906 1.00 34.59  ? 235 MET A CA  1 
ATOM   2370 C  C   . MET A 1 235 ? -6.706  -0.571  -45.213 1.00 31.90  ? 235 MET A C   1 
ATOM   2371 O  O   . MET A 1 235 ? -5.709  0.152   -45.109 1.00 29.38  ? 235 MET A O   1 
ATOM   2372 C  CB  . MET A 1 235 ? -6.079  -2.900  -46.090 1.00 42.04  ? 235 MET A CB  1 
ATOM   2373 C  CG  . MET A 1 235 ? -5.646  -4.275  -45.542 1.00 52.60  ? 235 MET A CG  1 
ATOM   2374 S  SD  . MET A 1 235 ? -4.824  -5.416  -46.662 1.00 66.30  ? 235 MET A SD  1 
ATOM   2375 C  CE  . MET A 1 235 ? -3.596  -4.331  -47.396 1.00 63.01  ? 235 MET A CE  1 
ATOM   2376 N  N   . LYS A 1 236 ? -7.931  -0.096  -45.411 1.00 29.67  ? 236 LYS A N   1 
ATOM   2377 C  CA  . LYS A 1 236 ? -8.156  1.339   -45.675 1.00 30.87  ? 236 LYS A CA  1 
ATOM   2378 C  C   . LYS A 1 236 ? -7.980  2.128   -44.384 1.00 27.13  ? 236 LYS A C   1 
ATOM   2379 O  O   . LYS A 1 236 ? -7.946  3.345   -44.493 1.00 28.05  ? 236 LYS A O   1 
ATOM   2380 C  CB  . LYS A 1 236 ? -9.525  1.562   -46.308 1.00 31.77  ? 236 LYS A CB  1 
ATOM   2381 C  CG  . LYS A 1 236 ? -9.695  0.893   -47.656 1.00 34.21  ? 236 LYS A CG  1 
ATOM   2382 C  CD  . LYS A 1 236 ? -11.096 1.000   -48.202 1.00 33.57  ? 236 LYS A CD  1 
ATOM   2383 C  CE  . LYS A 1 236 ? -11.176 0.359   -49.563 1.00 36.35  ? 236 LYS A CE  1 
ATOM   2384 N  NZ  . LYS A 1 236 ? -12.581 0.200   -49.989 1.00 39.43  ? 236 LYS A NZ  1 
ATOM   2385 N  N   . TYR A 1 237 ? -7.941  1.469   -43.222 1.00 25.03  ? 237 TYR A N   1 
ATOM   2386 C  CA  . TYR A 1 237 ? -7.658  2.115   -41.908 1.00 27.75  ? 237 TYR A CA  1 
ATOM   2387 C  C   . TYR A 1 237 ? -6.290  1.694   -41.356 1.00 27.04  ? 237 TYR A C   1 
ATOM   2388 O  O   . TYR A 1 237 ? -6.114  1.844   -40.166 1.00 25.84  ? 237 TYR A O   1 
ATOM   2389 C  CB  . TYR A 1 237 ? -8.724  1.771   -40.868 1.00 26.66  ? 237 TYR A CB  1 
ATOM   2390 C  CG  . TYR A 1 237 ? -10.137 2.120   -41.255 1.00 29.36  ? 237 TYR A CG  1 
ATOM   2391 C  CD1 . TYR A 1 237 ? -10.709 3.323   -40.864 1.00 30.68  ? 237 TYR A CD1 1 
ATOM   2392 C  CD2 . TYR A 1 237 ? -10.930 1.228   -41.963 1.00 30.49  ? 237 TYR A CD2 1 
ATOM   2393 C  CE1 . TYR A 1 237 ? -12.023 3.626   -41.187 1.00 31.02  ? 237 TYR A CE1 1 
ATOM   2394 C  CE2 . TYR A 1 237 ? -12.248 1.518   -42.291 1.00 29.33  ? 237 TYR A CE2 1 
ATOM   2395 C  CZ  . TYR A 1 237 ? -12.798 2.726   -41.899 1.00 32.58  ? 237 TYR A CZ  1 
ATOM   2396 O  OH  . TYR A 1 237 ? -14.100 3.032   -42.193 1.00 34.54  ? 237 TYR A OH  1 
ATOM   2397 N  N   . ASN A 1 238 ? -5.387  1.145   -42.176 1.00 28.77  ? 238 ASN A N   1 
ATOM   2398 C  CA  . ASN A 1 238 ? -4.021  0.730   -41.752 1.00 29.10  ? 238 ASN A CA  1 
ATOM   2399 C  C   . ASN A 1 238 ? -4.105  -0.397  -40.715 1.00 26.50  ? 238 ASN A C   1 
ATOM   2400 O  O   . ASN A 1 238 ? -3.296  -0.405  -39.781 1.00 23.30  ? 238 ASN A O   1 
ATOM   2401 C  CB  . ASN A 1 238 ? -3.241  1.927   -41.195 1.00 32.49  ? 238 ASN A CB  1 
ATOM   2402 C  CG  . ASN A 1 238 ? -2.680  2.785   -42.295 1.00 35.25  ? 238 ASN A CG  1 
ATOM   2403 O  OD1 . ASN A 1 238 ? -2.275  2.267   -43.329 1.00 40.41  ? 238 ASN A OD1 1 
ATOM   2404 N  ND2 . ASN A 1 238 ? -2.669  4.089   -42.086 1.00 43.06  ? 238 ASN A ND2 1 
ATOM   2405 N  N   . TYR A 1 239 ? -5.096  -1.270  -40.826 1.00 22.88  ? 239 TYR A N   1 
ATOM   2406 C  CA  . TYR A 1 239 ? -5.182  -2.500  -40.019 1.00 23.47  ? 239 TYR A CA  1 
ATOM   2407 C  C   . TYR A 1 239 ? -4.415  -3.566  -40.788 1.00 24.82  ? 239 TYR A C   1 
ATOM   2408 O  O   . TYR A 1 239 ? -4.484  -3.551  -42.033 1.00 27.85  ? 239 TYR A O   1 
ATOM   2409 C  CB  . TYR A 1 239 ? -6.638  -2.911  -39.790 1.00 22.88  ? 239 TYR A CB  1 
ATOM   2410 C  CG  . TYR A 1 239 ? -7.245  -2.344  -38.536 1.00 22.49  ? 239 TYR A CG  1 
ATOM   2411 C  CD1 . TYR A 1 239 ? -7.341  -0.980  -38.330 1.00 23.02  ? 239 TYR A CD1 1 
ATOM   2412 C  CD2 . TYR A 1 239 ? -7.710  -3.185  -37.551 1.00 22.99  ? 239 TYR A CD2 1 
ATOM   2413 C  CE1 . TYR A 1 239 ? -7.871  -0.465  -37.164 1.00 26.13  ? 239 TYR A CE1 1 
ATOM   2414 C  CE2 . TYR A 1 239 ? -8.275  -2.689  -36.392 1.00 24.90  ? 239 TYR A CE2 1 
ATOM   2415 C  CZ  . TYR A 1 239 ? -8.354  -1.324  -36.194 1.00 24.28  ? 239 TYR A CZ  1 
ATOM   2416 O  OH  . TYR A 1 239 ? -8.881  -0.871  -35.023 1.00 25.39  ? 239 TYR A OH  1 
ATOM   2417 N  N   . GLU A 1 240 ? -3.696  -4.416  -40.076 1.00 23.41  ? 240 GLU A N   1 
ATOM   2418 C  CA  . GLU A 1 240 ? -3.032  -5.615  -40.632 1.00 27.02  ? 240 GLU A CA  1 
ATOM   2419 C  C   . GLU A 1 240 ? -4.057  -6.524  -41.306 1.00 28.26  ? 240 GLU A C   1 
ATOM   2420 O  O   . GLU A 1 240 ? -5.172  -6.693  -40.819 1.00 26.32  ? 240 GLU A O   1 
ATOM   2421 C  CB  . GLU A 1 240 ? -2.372  -6.406  -39.498 1.00 28.85  ? 240 GLU A CB  1 
ATOM   2422 C  CG  . GLU A 1 240 ? -1.083  -5.771  -39.064 1.00 32.60  ? 240 GLU A CG  1 
ATOM   2423 C  CD  . GLU A 1 240 ? -0.012  -5.988  -40.106 1.00 37.14  ? 240 GLU A CD  1 
ATOM   2424 O  OE1 . GLU A 1 240 ? 0.386   -7.170  -40.261 1.00 37.72  ? 240 GLU A OE1 1 
ATOM   2425 O  OE2 . GLU A 1 240 ? 0.411   -4.981  -40.763 1.00 39.06  ? 240 GLU A OE2 1 
ATOM   2426 N  N   . PRO A 1 241 ? -3.701  -7.165  -42.435 1.00 29.74  ? 241 PRO A N   1 
ATOM   2427 C  CA  . PRO A 1 241 ? -4.545  -8.216  -42.997 1.00 29.44  ? 241 PRO A CA  1 
ATOM   2428 C  C   . PRO A 1 241 ? -4.783  -9.292  -41.931 1.00 27.63  ? 241 PRO A C   1 
ATOM   2429 O  O   . PRO A 1 241 ? -3.881  -9.614  -41.163 1.00 25.68  ? 241 PRO A O   1 
ATOM   2430 C  CB  . PRO A 1 241 ? -3.745  -8.766  -44.191 1.00 30.39  ? 241 PRO A CB  1 
ATOM   2431 C  CG  . PRO A 1 241 ? -2.753  -7.667  -44.524 1.00 31.96  ? 241 PRO A CG  1 
ATOM   2432 C  CD  . PRO A 1 241 ? -2.487  -6.926  -43.227 1.00 31.00  ? 241 PRO A CD  1 
ATOM   2433 N  N   . LEU A 1 242 ? -6.015  -9.761  -41.861 1.00 25.91  ? 242 LEU A N   1 
ATOM   2434 C  CA  . LEU A 1 242 ? -6.422  -10.911 -41.031 1.00 27.23  ? 242 LEU A CA  1 
ATOM   2435 C  C   . LEU A 1 242 ? -6.296  -12.164 -41.912 1.00 29.50  ? 242 LEU A C   1 
ATOM   2436 O  O   . LEU A 1 242 ? -6.838  -12.148 -43.007 1.00 31.14  ? 242 LEU A O   1 
ATOM   2437 C  CB  . LEU A 1 242 ? -7.861  -10.699 -40.539 1.00 28.15  ? 242 LEU A CB  1 
ATOM   2438 C  CG  . LEU A 1 242 ? -8.310  -11.655 -39.429 1.00 29.50  ? 242 LEU A CG  1 
ATOM   2439 C  CD1 . LEU A 1 242 ? -7.678  -11.285 -38.098 1.00 27.75  ? 242 LEU A CD1 1 
ATOM   2440 C  CD2 . LEU A 1 242 ? -9.823  -11.685 -39.300 1.00 30.57  ? 242 LEU A CD2 1 
ATOM   2441 N  N   . THR A 1 243 ? -5.589  -13.186 -41.430 1.00 29.05  ? 243 THR A N   1 
ATOM   2442 C  CA  . THR A 1 243 ? -5.271  -14.447 -42.135 1.00 28.34  ? 243 THR A CA  1 
ATOM   2443 C  C   . THR A 1 243 ? -6.180  -15.550 -41.598 1.00 28.25  ? 243 THR A C   1 
ATOM   2444 O  O   . THR A 1 243 ? -6.789  -15.366 -40.521 1.00 26.74  ? 243 THR A O   1 
ATOM   2445 C  CB  . THR A 1 243 ? -3.795  -14.814 -41.928 1.00 29.85  ? 243 THR A CB  1 
ATOM   2446 O  OG1 . THR A 1 243 ? -3.606  -15.238 -40.569 1.00 26.63  ? 243 THR A OG1 1 
ATOM   2447 C  CG2 . THR A 1 243 ? -2.864  -13.664 -42.258 1.00 29.45  ? 243 THR A CG2 1 
ATOM   2448 N  N   . GLN A 1 244 ? -6.229  -16.683 -42.285 1.00 29.34  ? 244 GLN A N   1 
ATOM   2449 C  CA  . GLN A 1 244 ? -7.006  -17.855 -41.820 1.00 30.39  ? 244 GLN A CA  1 
ATOM   2450 C  C   . GLN A 1 244 ? -6.412  -18.308 -40.490 1.00 30.04  ? 244 GLN A C   1 
ATOM   2451 O  O   . GLN A 1 244 ? -7.192  -18.710 -39.594 1.00 36.69  ? 244 GLN A O   1 
ATOM   2452 C  CB  . GLN A 1 244 ? -7.022  -18.986 -42.858 1.00 31.16  ? 244 GLN A CB  1 
ATOM   2453 C  CG  . GLN A 1 244 ? -7.847  -20.184 -42.401 1.00 31.57  ? 244 GLN A CG  1 
ATOM   2454 C  CD  . GLN A 1 244 ? -9.280  -19.788 -42.113 1.00 32.55  ? 244 GLN A CD  1 
ATOM   2455 O  OE1 . GLN A 1 244 ? -9.898  -19.023 -42.848 1.00 35.82  ? 244 GLN A OE1 1 
ATOM   2456 N  NE2 . GLN A 1 244 ? -9.817  -20.273 -41.009 1.00 35.89  ? 244 GLN A NE2 1 
ATOM   2457 N  N   . ASP A 1 245 ? -5.090  -18.200 -40.333 1.00 31.60  ? 245 ASP A N   1 
ATOM   2458 C  CA  . ASP A 1 245 ? -4.403  -18.473 -39.041 1.00 32.96  ? 245 ASP A CA  1 
ATOM   2459 C  C   . ASP A 1 245 ? -5.054  -17.647 -37.919 1.00 30.86  ? 245 ASP A C   1 
ATOM   2460 O  O   . ASP A 1 245 ? -5.355  -18.202 -36.838 1.00 28.01  ? 245 ASP A O   1 
ATOM   2461 C  CB  . ASP A 1 245 ? -2.901  -18.178 -39.123 1.00 35.96  ? 245 ASP A CB  1 
ATOM   2462 C  CG  . ASP A 1 245 ? -2.081  -19.357 -39.619 1.00 38.17  ? 245 ASP A CG  1 
ATOM   2463 O  OD1 . ASP A 1 245 ? -2.642  -20.220 -40.296 1.00 41.41  ? 245 ASP A OD1 1 
ATOM   2464 O  OD2 . ASP A 1 245 ? -0.895  -19.394 -39.315 1.00 40.97  ? 245 ASP A OD2 1 
ATOM   2465 N  N   . HIS A 1 246 ? -5.247  -16.351 -38.139 1.00 30.42  ? 246 HIS A N   1 
ATOM   2466 C  CA  . HIS A 1 246 ? -5.864  -15.452 -37.126 1.00 29.70  ? 246 HIS A CA  1 
ATOM   2467 C  C   . HIS A 1 246 ? -7.278  -15.950 -36.793 1.00 29.74  ? 246 HIS A C   1 
ATOM   2468 O  O   . HIS A 1 246 ? -7.627  -15.988 -35.595 1.00 32.85  ? 246 HIS A O   1 
ATOM   2469 C  CB  . HIS A 1 246 ? -5.817  -14.006 -37.617 1.00 28.70  ? 246 HIS A CB  1 
ATOM   2470 C  CG  . HIS A 1 246 ? -4.426  -13.483 -37.750 1.00 27.79  ? 246 HIS A CG  1 
ATOM   2471 N  ND1 . HIS A 1 246 ? -4.098  -12.485 -38.651 1.00 25.28  ? 246 HIS A ND1 1 
ATOM   2472 C  CD2 . HIS A 1 246 ? -3.285  -13.811 -37.091 1.00 28.74  ? 246 HIS A CD2 1 
ATOM   2473 C  CE1 . HIS A 1 246 ? -2.812  -12.210 -38.535 1.00 27.30  ? 246 HIS A CE1 1 
ATOM   2474 N  NE2 . HIS A 1 246 ? -2.279  -13.019 -37.572 1.00 26.49  ? 246 HIS A NE2 1 
ATOM   2475 N  N   . VAL A 1 247 ? -8.031  -16.390 -37.805 1.00 32.58  ? 247 VAL A N   1 
ATOM   2476 C  CA  . VAL A 1 247 ? -9.428  -16.885 -37.649 1.00 32.46  ? 247 VAL A CA  1 
ATOM   2477 C  C   . VAL A 1 247 ? -9.416  -18.135 -36.773 1.00 31.93  ? 247 VAL A C   1 
ATOM   2478 O  O   . VAL A 1 247 ? -10.231 -18.217 -35.831 1.00 36.00  ? 247 VAL A O   1 
ATOM   2479 C  CB  . VAL A 1 247 ? -10.095 -17.176 -39.001 1.00 35.60  ? 247 VAL A CB  1 
ATOM   2480 C  CG1 . VAL A 1 247 ? -11.519 -17.690 -38.793 1.00 35.97  ? 247 VAL A CG1 1 
ATOM   2481 C  CG2 . VAL A 1 247 ? -10.095 -15.956 -39.912 1.00 35.91  ? 247 VAL A CG2 1 
ATOM   2482 N  N   . ASP A 1 248 ? -8.497  -19.055 -37.057 1.00 31.82  ? 248 ASP A N   1 
ATOM   2483 C  CA  . ASP A 1 248 ? -8.362  -20.325 -36.305 1.00 33.01  ? 248 ASP A CA  1 
ATOM   2484 C  C   . ASP A 1 248 ? -8.047  -19.973 -34.857 1.00 33.35  ? 248 ASP A C   1 
ATOM   2485 O  O   . ASP A 1 248 ? -8.697  -20.527 -33.958 1.00 35.01  ? 248 ASP A O   1 
ATOM   2486 C  CB  . ASP A 1 248 ? -7.298  -21.236 -36.924 1.00 32.98  ? 248 ASP A CB  1 
ATOM   2487 C  CG  . ASP A 1 248 ? -7.658  -21.717 -38.320 1.00 32.75  ? 248 ASP A CG  1 
ATOM   2488 O  OD1 . ASP A 1 248 ? -8.858  -21.731 -38.659 1.00 38.09  ? 248 ASP A OD1 1 
ATOM   2489 O  OD2 . ASP A 1 248 ? -6.743  -22.031 -39.061 1.00 34.03  ? 248 ASP A OD2 1 
ATOM   2490 N  N   . ILE A 1 249 ? -7.089  -19.069 -34.664 1.00 32.54  ? 249 ILE A N   1 
ATOM   2491 C  CA  . ILE A 1 249 ? -6.592  -18.649 -33.325 1.00 33.07  ? 249 ILE A CA  1 
ATOM   2492 C  C   . ILE A 1 249 ? -7.769  -18.110 -32.486 1.00 31.99  ? 249 ILE A C   1 
ATOM   2493 O  O   . ILE A 1 249 ? -7.734  -18.235 -31.259 1.00 29.04  ? 249 ILE A O   1 
ATOM   2494 C  CB  . ILE A 1 249 ? -5.451  -17.624 -33.526 1.00 37.13  ? 249 ILE A CB  1 
ATOM   2495 C  CG1 . ILE A 1 249 ? -4.098  -18.303 -33.804 1.00 41.89  ? 249 ILE A CG1 1 
ATOM   2496 C  CG2 . ILE A 1 249 ? -5.362  -16.677 -32.356 1.00 34.99  ? 249 ILE A CG2 1 
ATOM   2497 C  CD1 . ILE A 1 249 ? -2.948  -17.355 -34.211 1.00 38.66  ? 249 ILE A CD1 1 
ATOM   2498 N  N   . LEU A 1 250 ? -8.778  -17.487 -33.105 1.00 32.60  ? 250 LEU A N   1 
ATOM   2499 C  CA  . LEU A 1 250 ? -9.922  -16.887 -32.360 1.00 28.77  ? 250 LEU A CA  1 
ATOM   2500 C  C   . LEU A 1 250 ? -11.031 -17.925 -32.108 1.00 28.83  ? 250 LEU A C   1 
ATOM   2501 O  O   . LEU A 1 250 ? -11.885 -17.627 -31.279 1.00 28.04  ? 250 LEU A O   1 
ATOM   2502 C  CB  . LEU A 1 250 ? -10.441 -15.688 -33.145 1.00 26.60  ? 250 LEU A CB  1 
ATOM   2503 C  CG  . LEU A 1 250 ? -9.488  -14.501 -33.201 1.00 28.09  ? 250 LEU A CG  1 
ATOM   2504 C  CD1 . LEU A 1 250 ? -9.844  -13.561 -34.345 1.00 26.92  ? 250 LEU A CD1 1 
ATOM   2505 C  CD2 . LEU A 1 250 ? -9.466  -13.760 -31.864 1.00 27.11  ? 250 LEU A CD2 1 
ATOM   2506 N  N   . GLY A 1 251 ? -10.988 -19.111 -32.738 1.00 30.22  ? 251 GLY A N   1 
ATOM   2507 C  CA  . GLY A 1 251 ? -12.013 -20.172 -32.618 1.00 29.85  ? 251 GLY A CA  1 
ATOM   2508 C  C   . GLY A 1 251 ? -12.481 -20.401 -31.178 1.00 33.40  ? 251 GLY A C   1 
ATOM   2509 O  O   . GLY A 1 251 ? -13.676 -20.445 -30.889 1.00 35.86  ? 251 GLY A O   1 
ATOM   2510 N  N   . PRO A 1 252 ? -11.573 -20.593 -30.202 1.00 35.42  ? 252 PRO A N   1 
ATOM   2511 C  CA  . PRO A 1 252 ? -11.970 -20.664 -28.787 1.00 35.83  ? 252 PRO A CA  1 
ATOM   2512 C  C   . PRO A 1 252 ? -12.858 -19.521 -28.251 1.00 37.00  ? 252 PRO A C   1 
ATOM   2513 O  O   . PRO A 1 252 ? -13.873 -19.808 -27.640 1.00 36.50  ? 252 PRO A O   1 
ATOM   2514 C  CB  . PRO A 1 252 ? -10.610 -20.705 -28.075 1.00 32.75  ? 252 PRO A CB  1 
ATOM   2515 C  CG  . PRO A 1 252 ? -9.728  -21.419 -29.075 1.00 33.64  ? 252 PRO A CG  1 
ATOM   2516 C  CD  . PRO A 1 252 ? -10.136 -20.834 -30.406 1.00 33.75  ? 252 PRO A CD  1 
ATOM   2517 N  N   . LEU A 1 253 ? -12.464 -18.265 -28.452 1.00 35.56  ? 253 LEU A N   1 
ATOM   2518 C  CA  . LEU A 1 253 ? -13.232 -17.077 -27.995 1.00 33.51  ? 253 LEU A CA  1 
ATOM   2519 C  C   . LEU A 1 253 ? -14.589 -16.998 -28.729 1.00 34.30  ? 253 LEU A C   1 
ATOM   2520 O  O   . LEU A 1 253 ? -15.582 -16.608 -28.100 1.00 34.86  ? 253 LEU A O   1 
ATOM   2521 C  CB  . LEU A 1 253 ? -12.381 -15.826 -28.225 1.00 32.82  ? 253 LEU A CB  1 
ATOM   2522 C  CG  . LEU A 1 253 ? -11.267 -15.589 -27.213 1.00 32.84  ? 253 LEU A CG  1 
ATOM   2523 C  CD1 . LEU A 1 253 ? -10.193 -14.683 -27.789 1.00 32.78  ? 253 LEU A CD1 1 
ATOM   2524 C  CD2 . LEU A 1 253 ? -11.808 -14.976 -25.939 1.00 36.65  ? 253 LEU A CD2 1 
ATOM   2525 N  N   . SER A 1 254 ? -14.614 -17.328 -30.018 1.00 33.31  ? 254 SER A N   1 
ATOM   2526 C  CA  . SER A 1 254 ? -15.822 -17.539 -30.848 1.00 35.66  ? 254 SER A CA  1 
ATOM   2527 C  C   . SER A 1 254 ? -16.772 -18.502 -30.128 1.00 38.45  ? 254 SER A C   1 
ATOM   2528 O  O   . SER A 1 254 ? -17.920 -18.122 -29.869 1.00 34.21  ? 254 SER A O   1 
ATOM   2529 C  CB  . SER A 1 254 ? -15.432 -18.084 -32.183 1.00 35.93  ? 254 SER A CB  1 
ATOM   2530 O  OG  . SER A 1 254 ? -16.522 -18.048 -33.073 1.00 41.99  ? 254 SER A OG  1 
ATOM   2531 N  N   . ALA A 1 255 ? -16.294 -19.710 -29.819 1.00 39.96  ? 255 ALA A N   1 
ATOM   2532 C  CA  . ALA A 1 255 ? -17.078 -20.799 -29.188 1.00 40.10  ? 255 ALA A CA  1 
ATOM   2533 C  C   . ALA A 1 255 ? -17.522 -20.352 -27.795 1.00 40.20  ? 255 ALA A C   1 
ATOM   2534 O  O   . ALA A 1 255 ? -18.710 -20.477 -27.492 1.00 46.80  ? 255 ALA A O   1 
ATOM   2535 C  CB  . ALA A 1 255 ? -16.278 -22.076 -29.135 1.00 39.26  ? 255 ALA A CB  1 
ATOM   2536 N  N   . GLN A 1 256 ? -16.619 -19.794 -27.000 1.00 40.82  ? 256 GLN A N   1 
ATOM   2537 C  CA  . GLN A 1 256 ? -16.950 -19.279 -25.652 1.00 43.01  ? 256 GLN A CA  1 
ATOM   2538 C  C   . GLN A 1 256 ? -18.152 -18.331 -25.765 1.00 44.63  ? 256 GLN A C   1 
ATOM   2539 O  O   . GLN A 1 256 ? -19.105 -18.517 -25.005 1.00 39.72  ? 256 GLN A O   1 
ATOM   2540 C  CB  . GLN A 1 256 ? -15.726 -18.634 -25.004 1.00 50.09  ? 256 GLN A CB  1 
ATOM   2541 C  CG  . GLN A 1 256 ? -16.019 -18.085 -23.616 1.00 54.93  ? 256 GLN A CG  1 
ATOM   2542 C  CD  . GLN A 1 256 ? -14.823 -17.966 -22.704 1.00 61.54  ? 256 GLN A CD  1 
ATOM   2543 O  OE1 . GLN A 1 256 ? -13.657 -18.095 -23.098 1.00 65.23  ? 256 GLN A OE1 1 
ATOM   2544 N  NE2 . GLN A 1 256 ? -15.130 -17.702 -21.446 1.00 68.61  ? 256 GLN A NE2 1 
ATOM   2545 N  N   . THR A 1 257 ? -18.140 -17.371 -26.697 1.00 44.41  ? 257 THR A N   1 
ATOM   2546 C  CA  . THR A 1 257 ? -19.118 -16.248 -26.719 1.00 43.03  ? 257 THR A CA  1 
ATOM   2547 C  C   . THR A 1 257 ? -20.291 -16.562 -27.658 1.00 44.65  ? 257 THR A C   1 
ATOM   2548 O  O   . THR A 1 257 ? -21.284 -15.826 -27.579 1.00 48.00  ? 257 THR A O   1 
ATOM   2549 C  CB  . THR A 1 257 ? -18.488 -14.914 -27.141 1.00 42.59  ? 257 THR A CB  1 
ATOM   2550 O  OG1 . THR A 1 257 ? -18.063 -15.089 -28.494 1.00 36.97  ? 257 THR A OG1 1 
ATOM   2551 C  CG2 . THR A 1 257 ? -17.376 -14.455 -26.220 1.00 41.06  ? 257 THR A CG2 1 
ATOM   2552 N  N   . GLY A 1 258 ? -20.165 -17.565 -28.537 1.00 42.18  ? 258 GLY A N   1 
ATOM   2553 C  CA  . GLY A 1 258 ? -21.192 -17.904 -29.539 1.00 40.42  ? 258 GLY A CA  1 
ATOM   2554 C  C   . GLY A 1 258 ? -21.259 -16.903 -30.688 1.00 40.97  ? 258 GLY A C   1 
ATOM   2555 O  O   . GLY A 1 258 ? -22.209 -16.989 -31.476 1.00 39.48  ? 258 GLY A O   1 
ATOM   2556 N  N   . ILE A 1 259 ? -20.267 -16.019 -30.843 1.00 38.02  ? 259 ILE A N   1 
ATOM   2557 C  CA  . ILE A 1 259 ? -20.182 -15.062 -31.989 1.00 34.74  ? 259 ILE A CA  1 
ATOM   2558 C  C   . ILE A 1 259 ? -19.076 -15.501 -32.960 1.00 34.23  ? 259 ILE A C   1 
ATOM   2559 O  O   . ILE A 1 259 ? -17.889 -15.531 -32.546 1.00 34.18  ? 259 ILE A O   1 
ATOM   2560 C  CB  . ILE A 1 259 ? -19.923 -13.650 -31.447 1.00 35.10  ? 259 ILE A CB  1 
ATOM   2561 C  CG1 . ILE A 1 259 ? -20.938 -13.299 -30.351 1.00 35.04  ? 259 ILE A CG1 1 
ATOM   2562 C  CG2 . ILE A 1 259 ? -19.874 -12.640 -32.583 1.00 35.41  ? 259 ILE A CG2 1 
ATOM   2563 C  CD1 . ILE A 1 259 ? -20.703 -11.956 -29.696 1.00 37.44  ? 259 ILE A CD1 1 
ATOM   2564 N  N   . ALA A 1 260 ? -19.450 -15.818 -34.202 1.00 30.80  ? 260 ALA A N   1 
ATOM   2565 C  CA  . ALA A 1 260 ? -18.546 -16.248 -35.292 1.00 32.03  ? 260 ALA A CA  1 
ATOM   2566 C  C   . ALA A 1 260 ? -17.478 -15.170 -35.539 1.00 35.62  ? 260 ALA A C   1 
ATOM   2567 O  O   . ALA A 1 260 ? -17.767 -13.942 -35.390 1.00 31.37  ? 260 ALA A O   1 
ATOM   2568 C  CB  . ALA A 1 260 ? -19.327 -16.520 -36.551 1.00 31.47  ? 260 ALA A CB  1 
ATOM   2569 N  N   . VAL A 1 261 ? -16.277 -15.607 -35.920 1.00 31.40  ? 261 VAL A N   1 
ATOM   2570 C  CA  . VAL A 1 261 ? -15.114 -14.699 -36.108 1.00 31.12  ? 261 VAL A CA  1 
ATOM   2571 C  C   . VAL A 1 261 ? -15.512 -13.645 -37.138 1.00 28.72  ? 261 VAL A C   1 
ATOM   2572 O  O   . VAL A 1 261 ? -15.255 -12.461 -36.901 1.00 28.10  ? 261 VAL A O   1 
ATOM   2573 C  CB  . VAL A 1 261 ? -13.836 -15.460 -36.504 1.00 32.36  ? 261 VAL A CB  1 
ATOM   2574 C  CG1 . VAL A 1 261 ? -12.742 -14.495 -36.953 1.00 30.15  ? 261 VAL A CG1 1 
ATOM   2575 C  CG2 . VAL A 1 261 ? -13.358 -16.351 -35.361 1.00 34.19  ? 261 VAL A CG2 1 
ATOM   2576 N  N   . LEU A 1 262 ? -16.157 -14.059 -38.221 1.00 28.04  ? 262 LEU A N   1 
ATOM   2577 C  CA  . LEU A 1 262 ? -16.594 -13.129 -39.288 1.00 28.40  ? 262 LEU A CA  1 
ATOM   2578 C  C   . LEU A 1 262 ? -17.785 -12.255 -38.848 1.00 27.23  ? 262 LEU A C   1 
ATOM   2579 O  O   . LEU A 1 262 ? -17.879 -11.160 -39.391 1.00 27.71  ? 262 LEU A O   1 
ATOM   2580 C  CB  . LEU A 1 262 ? -16.858 -13.930 -40.555 1.00 29.77  ? 262 LEU A CB  1 
ATOM   2581 C  CG  . LEU A 1 262 ? -15.608 -14.572 -41.148 1.00 32.18  ? 262 LEU A CG  1 
ATOM   2582 C  CD1 . LEU A 1 262 ? -15.971 -15.510 -42.292 1.00 32.97  ? 262 LEU A CD1 1 
ATOM   2583 C  CD2 . LEU A 1 262 ? -14.608 -13.514 -41.614 1.00 33.00  ? 262 LEU A CD2 1 
ATOM   2584 N  N   . ASP A 1 263 ? -18.597 -12.629 -37.854 1.00 29.15  ? 263 ASP A N   1 
ATOM   2585 C  CA  . ASP A 1 263 ? -19.594 -11.671 -37.280 1.00 32.70  ? 263 ASP A CA  1 
ATOM   2586 C  C   . ASP A 1 263 ? -18.835 -10.581 -36.519 1.00 28.97  ? 263 ASP A C   1 
ATOM   2587 O  O   . ASP A 1 263 ? -19.111 -9.371  -36.715 1.00 28.73  ? 263 ASP A O   1 
ATOM   2588 C  CB  . ASP A 1 263 ? -20.634 -12.288 -36.334 1.00 38.90  ? 263 ASP A CB  1 
ATOM   2589 C  CG  . ASP A 1 263 ? -21.607 -13.259 -36.976 1.00 46.99  ? 263 ASP A CG  1 
ATOM   2590 O  OD1 . ASP A 1 263 ? -21.561 -13.398 -38.228 1.00 56.93  ? 263 ASP A OD1 1 
ATOM   2591 O  OD2 . ASP A 1 263 ? -22.399 -13.883 -36.217 1.00 49.48  ? 263 ASP A OD2 1 
ATOM   2592 N  N   . MET A 1 264 ? -17.890 -10.985 -35.684 1.00 29.60  ? 264 MET A N   1 
ATOM   2593 C  CA  . MET A 1 264 ? -17.082 -10.012 -34.913 1.00 28.45  ? 264 MET A CA  1 
ATOM   2594 C  C   . MET A 1 264 ? -16.333 -9.117  -35.900 1.00 26.70  ? 264 MET A C   1 
ATOM   2595 O  O   . MET A 1 264 ? -16.247 -7.923  -35.604 1.00 28.62  ? 264 MET A O   1 
ATOM   2596 C  CB  . MET A 1 264 ? -16.126 -10.685 -33.927 1.00 29.07  ? 264 MET A CB  1 
ATOM   2597 C  CG  . MET A 1 264 ? -15.583 -9.710  -32.895 1.00 27.76  ? 264 MET A CG  1 
ATOM   2598 S  SD  . MET A 1 264 ? -16.867 -8.903  -31.886 1.00 28.50  ? 264 MET A SD  1 
ATOM   2599 C  CE  . MET A 1 264 ? -17.193 -10.228 -30.726 1.00 29.57  ? 264 MET A CE  1 
ATOM   2600 N  N   . CYS A 1 265 ? -15.933 -9.631  -37.071 1.00 26.10  ? 265 CYS A N   1 
ATOM   2601 C  CA  . CYS A 1 265 ? -15.225 -8.834  -38.103 1.00 26.69  ? 265 CYS A CA  1 
ATOM   2602 C  C   . CYS A 1 265 ? -16.176 -7.755  -38.639 1.00 27.42  ? 265 CYS A C   1 
ATOM   2603 O  O   . CYS A 1 265 ? -15.699 -6.621  -38.837 1.00 27.19  ? 265 CYS A O   1 
ATOM   2604 C  CB  . CYS A 1 265 ? -14.619 -9.697  -39.203 1.00 28.00  ? 265 CYS A CB  1 
ATOM   2605 S  SG  . CYS A 1 265 ? -13.146 -10.620 -38.664 1.00 28.48  ? 265 CYS A SG  1 
ATOM   2606 N  N   . ALA A 1 266 ? -17.471 -8.060  -38.798 1.00 25.37  ? 266 ALA A N   1 
ATOM   2607 C  CA  . ALA A 1 266 ? -18.500 -7.090  -39.243 1.00 28.27  ? 266 ALA A CA  1 
ATOM   2608 C  C   . ALA A 1 266 ? -18.638 -5.963  -38.196 1.00 27.59  ? 266 ALA A C   1 
ATOM   2609 O  O   . ALA A 1 266 ? -18.657 -4.780  -38.564 1.00 29.51  ? 266 ALA A O   1 
ATOM   2610 C  CB  . ALA A 1 266 ? -19.815 -7.794  -39.520 1.00 30.89  ? 266 ALA A CB  1 
ATOM   2611 N  N   . SER A 1 267 ? -18.687 -6.316  -36.919 1.00 29.77  ? 267 SER A N   1 
ATOM   2612 C  CA  . SER A 1 267 ? -18.708 -5.375  -35.773 1.00 29.54  ? 267 SER A CA  1 
ATOM   2613 C  C   . SER A 1 267 ? -17.483 -4.441  -35.842 1.00 27.73  ? 267 SER A C   1 
ATOM   2614 O  O   . SER A 1 267 ? -17.644 -3.213  -35.792 1.00 24.38  ? 267 SER A O   1 
ATOM   2615 C  CB  . SER A 1 267 ? -18.802 -6.203  -34.505 1.00 35.35  ? 267 SER A CB  1 
ATOM   2616 O  OG  . SER A 1 267 ? -18.785 -5.400  -33.348 1.00 46.72  ? 267 SER A OG  1 
ATOM   2617 N  N   . LEU A 1 268 ? -16.275 -4.978  -36.030 1.00 27.09  ? 268 LEU A N   1 
ATOM   2618 C  CA  . LEU A 1 268 ? -15.051 -4.133  -36.132 1.00 23.91  ? 268 LEU A CA  1 
ATOM   2619 C  C   . LEU A 1 268 ? -15.194 -3.190  -37.335 1.00 23.43  ? 268 LEU A C   1 
ATOM   2620 O  O   . LEU A 1 268 ? -14.902 -2.011  -37.158 1.00 23.34  ? 268 LEU A O   1 
ATOM   2621 C  CB  . LEU A 1 268 ? -13.806 -5.020  -36.219 1.00 21.67  ? 268 LEU A CB  1 
ATOM   2622 C  CG  . LEU A 1 268 ? -12.464 -4.293  -36.346 1.00 22.51  ? 268 LEU A CG  1 
ATOM   2623 C  CD1 . LEU A 1 268 ? -12.324 -3.169  -35.318 1.00 20.31  ? 268 LEU A CD1 1 
ATOM   2624 C  CD2 . LEU A 1 268 ? -11.316 -5.287  -36.205 1.00 23.49  ? 268 LEU A CD2 1 
ATOM   2625 N  N   . LYS A 1 269 ? -15.652 -3.659  -38.508 1.00 26.21  ? 269 LYS A N   1 
ATOM   2626 C  CA  . LYS A 1 269 ? -15.782 -2.791  -39.719 1.00 28.07  ? 269 LYS A CA  1 
ATOM   2627 C  C   . LYS A 1 269 ? -16.667 -1.589  -39.378 1.00 27.46  ? 269 LYS A C   1 
ATOM   2628 O  O   . LYS A 1 269 ? -16.336 -0.456  -39.795 1.00 24.13  ? 269 LYS A O   1 
ATOM   2629 C  CB  . LYS A 1 269 ? -16.394 -3.521  -40.920 1.00 33.36  ? 269 LYS A CB  1 
ATOM   2630 C  CG  . LYS A 1 269 ? -15.581 -4.689  -41.451 1.00 37.97  ? 269 LYS A CG  1 
ATOM   2631 C  CD  . LYS A 1 269 ? -16.351 -5.640  -42.353 1.00 39.58  ? 269 LYS A CD  1 
ATOM   2632 C  CE  . LYS A 1 269 ? -16.640 -5.065  -43.718 1.00 40.01  ? 269 LYS A CE  1 
ATOM   2633 N  NZ  . LYS A 1 269 ? -17.499 -5.979  -44.512 1.00 42.27  ? 269 LYS A NZ  1 
ATOM   2634 N  N   . GLU A 1 270 ? -17.747 -1.839  -38.625 1.00 27.58  ? 270 GLU A N   1 
ATOM   2635 C  CA  . GLU A 1 270 ? -18.742 -0.804  -38.233 1.00 28.74  ? 270 GLU A CA  1 
ATOM   2636 C  C   . GLU A 1 270 ? -18.112 0.171   -37.238 1.00 26.60  ? 270 GLU A C   1 
ATOM   2637 O  O   . GLU A 1 270 ? -18.303 1.368   -37.414 1.00 25.84  ? 270 GLU A O   1 
ATOM   2638 C  CB  . GLU A 1 270 ? -20.001 -1.440  -37.649 1.00 27.59  ? 270 GLU A CB  1 
ATOM   2639 C  CG  . GLU A 1 270 ? -21.095 -0.440  -37.345 1.00 29.55  ? 270 GLU A CG  1 
ATOM   2640 C  CD  . GLU A 1 270 ? -22.436 -1.113  -37.081 1.00 30.44  ? 270 GLU A CD  1 
ATOM   2641 O  OE1 . GLU A 1 270 ? -23.080 -1.562  -38.049 1.00 29.67  ? 270 GLU A OE1 1 
ATOM   2642 O  OE2 . GLU A 1 270 ? -22.806 -1.240  -35.916 1.00 31.58  ? 270 GLU A OE2 1 
ATOM   2643 N  N   . LEU A 1 271 ? -17.366 -0.325  -36.251 1.00 25.82  ? 271 LEU A N   1 
ATOM   2644 C  CA  . LEU A 1 271 ? -16.692 0.544   -35.254 1.00 26.37  ? 271 LEU A CA  1 
ATOM   2645 C  C   . LEU A 1 271 ? -15.701 1.472   -35.969 1.00 26.95  ? 271 LEU A C   1 
ATOM   2646 O  O   . LEU A 1 271 ? -15.619 2.622   -35.557 1.00 25.73  ? 271 LEU A O   1 
ATOM   2647 C  CB  . LEU A 1 271 ? -15.978 -0.331  -34.226 1.00 27.50  ? 271 LEU A CB  1 
ATOM   2648 C  CG  . LEU A 1 271 ? -16.846 -0.882  -33.106 1.00 28.17  ? 271 LEU A CG  1 
ATOM   2649 C  CD1 . LEU A 1 271 ? -16.140 -2.038  -32.399 1.00 27.87  ? 271 LEU A CD1 1 
ATOM   2650 C  CD2 . LEU A 1 271 ? -17.200 0.232   -32.130 1.00 29.16  ? 271 LEU A CD2 1 
ATOM   2651 N  N   . LEU A 1 272 ? -14.990 0.985   -37.002 1.00 24.51  ? 272 LEU A N   1 
ATOM   2652 C  CA  . LEU A 1 272 ? -14.003 1.799   -37.778 1.00 25.79  ? 272 LEU A CA  1 
ATOM   2653 C  C   . LEU A 1 272 ? -14.752 2.898   -38.525 1.00 27.05  ? 272 LEU A C   1 
ATOM   2654 O  O   . LEU A 1 272 ? -14.258 4.030   -38.596 1.00 27.58  ? 272 LEU A O   1 
ATOM   2655 C  CB  . LEU A 1 272 ? -13.213 0.911   -38.749 1.00 24.01  ? 272 LEU A CB  1 
ATOM   2656 C  CG  . LEU A 1 272 ? -12.234 -0.037  -38.071 1.00 25.45  ? 272 LEU A CG  1 
ATOM   2657 C  CD1 . LEU A 1 272 ? -11.638 -1.043  -39.045 1.00 27.16  ? 272 LEU A CD1 1 
ATOM   2658 C  CD2 . LEU A 1 272 ? -11.130 0.742   -37.378 1.00 26.64  ? 272 LEU A CD2 1 
ATOM   2659 N  N   . GLN A 1 273 ? -15.917 2.563   -39.062 1.00 26.39  ? 273 GLN A N   1 
ATOM   2660 C  CA  . GLN A 1 273 ? -16.812 3.501   -39.786 1.00 24.57  ? 273 GLN A CA  1 
ATOM   2661 C  C   . GLN A 1 273 ? -17.432 4.552   -38.845 1.00 24.84  ? 273 GLN A C   1 
ATOM   2662 O  O   . GLN A 1 273 ? -17.611 5.700   -39.284 1.00 27.49  ? 273 GLN A O   1 
ATOM   2663 C  CB  . GLN A 1 273 ? -17.871 2.647   -40.471 1.00 22.53  ? 273 GLN A CB  1 
ATOM   2664 C  CG  . GLN A 1 273 ? -19.052 3.434   -41.008 1.00 24.40  ? 273 GLN A CG  1 
ATOM   2665 C  CD  . GLN A 1 273 ? -20.138 2.491   -41.465 1.00 24.41  ? 273 GLN A CD  1 
ATOM   2666 O  OE1 . GLN A 1 273 ? -21.068 2.186   -40.725 1.00 28.68  ? 273 GLN A OE1 1 
ATOM   2667 N  NE2 . GLN A 1 273 ? -19.987 1.985   -42.676 1.00 23.51  ? 273 GLN A NE2 1 
ATOM   2668 N  N   . ASN A 1 274 ? -17.802 4.190   -37.619 1.00 26.41  ? 274 ASN A N   1 
ATOM   2669 C  CA  . ASN A 1 274 ? -18.670 5.020   -36.745 1.00 28.25  ? 274 ASN A CA  1 
ATOM   2670 C  C   . ASN A 1 274 ? -17.869 5.672   -35.609 1.00 32.93  ? 274 ASN A C   1 
ATOM   2671 O  O   . ASN A 1 274 ? -18.345 6.709   -35.093 1.00 30.13  ? 274 ASN A O   1 
ATOM   2672 C  CB  . ASN A 1 274 ? -19.818 4.206   -36.139 1.00 28.55  ? 274 ASN A CB  1 
ATOM   2673 C  CG  . ASN A 1 274 ? -20.821 3.709   -37.163 1.00 26.68  ? 274 ASN A CG  1 
ATOM   2674 O  OD1 . ASN A 1 274 ? -20.763 4.070   -38.336 1.00 26.78  ? 274 ASN A OD1 1 
ATOM   2675 N  ND2 . ASN A 1 274 ? -21.757 2.886   -36.724 1.00 24.37  ? 274 ASN A ND2 1 
ATOM   2676 N  N   . GLY A 1 275 ? -16.739 5.096   -35.184 1.00 31.23  ? 275 GLY A N   1 
ATOM   2677 C  CA  . GLY A 1 275 ? -16.156 5.483   -33.890 1.00 31.75  ? 275 GLY A CA  1 
ATOM   2678 C  C   . GLY A 1 275 ? -17.040 4.952   -32.776 1.00 33.87  ? 275 GLY A C   1 
ATOM   2679 O  O   . GLY A 1 275 ? -17.787 4.016   -33.040 1.00 30.84  ? 275 GLY A O   1 
ATOM   2680 N  N   . MET A 1 276 ? -16.952 5.492   -31.566 1.00 35.38  ? 276 MET A N   1 
ATOM   2681 C  CA  . MET A 1 276 ? -17.639 4.898   -30.387 1.00 40.36  ? 276 MET A CA  1 
ATOM   2682 C  C   . MET A 1 276 ? -18.775 5.790   -29.896 1.00 37.69  ? 276 MET A C   1 
ATOM   2683 O  O   . MET A 1 276 ? -19.446 5.382   -28.924 1.00 39.48  ? 276 MET A O   1 
ATOM   2684 C  CB  . MET A 1 276 ? -16.645 4.691   -29.247 1.00 45.51  ? 276 MET A CB  1 
ATOM   2685 C  CG  . MET A 1 276 ? -15.475 3.880   -29.690 1.00 48.75  ? 276 MET A CG  1 
ATOM   2686 S  SD  . MET A 1 276 ? -14.773 3.023   -28.333 1.00 53.58  ? 276 MET A SD  1 
ATOM   2687 C  CE  . MET A 1 276 ? -13.994 1.676   -29.218 1.00 55.19  ? 276 MET A CE  1 
ATOM   2688 N  N   . ASN A 1 277 ? -18.968 6.950   -30.519 1.00 39.12  ? 277 ASN A N   1 
ATOM   2689 C  CA  . ASN A 1 277 ? -20.134 7.830   -30.245 1.00 43.32  ? 277 ASN A CA  1 
ATOM   2690 C  C   . ASN A 1 277 ? -20.165 8.073   -28.727 1.00 41.36  ? 277 ASN A C   1 
ATOM   2691 O  O   . ASN A 1 277 ? -21.192 7.771   -28.098 1.00 37.34  ? 277 ASN A O   1 
ATOM   2692 C  CB  . ASN A 1 277 ? -21.397 7.192   -30.838 1.00 48.52  ? 277 ASN A CB  1 
ATOM   2693 C  CG  . ASN A 1 277 ? -22.621 8.090   -30.866 1.00 58.59  ? 277 ASN A CG  1 
ATOM   2694 O  OD1 . ASN A 1 277 ? -22.534 9.302   -30.657 1.00 62.29  ? 277 ASN A OD1 1 
ATOM   2695 N  ND2 . ASN A 1 277 ? -23.781 7.498   -31.122 1.00 59.06  ? 277 ASN A ND2 1 
ATOM   2696 N  N   . GLY A 1 278 ? -19.041 8.531   -28.156 1.00 41.42  ? 278 GLY A N   1 
ATOM   2697 C  CA  . GLY A 1 278 ? -18.904 8.923   -26.737 1.00 39.86  ? 278 GLY A CA  1 
ATOM   2698 C  C   . GLY A 1 278 ? -18.943 7.739   -25.781 1.00 44.33  ? 278 GLY A C   1 
ATOM   2699 O  O   . GLY A 1 278 ? -19.054 7.962   -24.577 1.00 47.70  ? 278 GLY A O   1 
ATOM   2700 N  N   . ARG A 1 279 ? -18.851 6.506   -26.271 1.00 43.71  ? 279 ARG A N   1 
ATOM   2701 C  CA  . ARG A 1 279 ? -18.876 5.296   -25.406 1.00 44.24  ? 279 ARG A CA  1 
ATOM   2702 C  C   . ARG A 1 279 ? -17.440 4.775   -25.266 1.00 41.10  ? 279 ARG A C   1 
ATOM   2703 O  O   . ARG A 1 279 ? -16.506 5.361   -25.855 1.00 42.69  ? 279 ARG A O   1 
ATOM   2704 C  CB  . ARG A 1 279 ? -19.837 4.234   -25.960 1.00 47.85  ? 279 ARG A CB  1 
ATOM   2705 C  CG  . ARG A 1 279 ? -21.312 4.518   -25.697 1.00 51.65  ? 279 ARG A CG  1 
ATOM   2706 C  CD  . ARG A 1 279 ? -22.258 3.641   -26.496 1.00 50.96  ? 279 ARG A CD  1 
ATOM   2707 N  NE  . ARG A 1 279 ? -22.097 3.987   -27.899 1.00 59.61  ? 279 ARG A NE  1 
ATOM   2708 C  CZ  . ARG A 1 279 ? -22.887 3.596   -28.895 1.00 63.04  ? 279 ARG A CZ  1 
ATOM   2709 N  NH1 . ARG A 1 279 ? -23.935 2.820   -28.668 1.00 65.96  ? 279 ARG A NH1 1 
ATOM   2710 N  NH2 . ARG A 1 279 ? -22.620 3.995   -30.126 1.00 58.04  ? 279 ARG A NH2 1 
ATOM   2711 N  N   . THR A 1 280 ? -17.269 3.757   -24.434 1.00 42.47  ? 280 THR A N   1 
ATOM   2712 C  CA  . THR A 1 280 ? -15.968 3.109   -24.152 1.00 41.52  ? 280 THR A CA  1 
ATOM   2713 C  C   . THR A 1 280 ? -16.173 1.616   -24.286 1.00 40.48  ? 280 THR A C   1 
ATOM   2714 O  O   . THR A 1 280 ? -17.331 1.165   -24.183 1.00 42.21  ? 280 THR A O   1 
ATOM   2715 C  CB  . THR A 1 280 ? -15.446 3.434   -22.750 1.00 39.16  ? 280 THR A CB  1 
ATOM   2716 O  OG1 . THR A 1 280 ? -16.443 3.011   -21.823 1.00 39.94  ? 280 THR A OG1 1 
ATOM   2717 C  CG2 . THR A 1 280 ? -15.139 4.902   -22.563 1.00 37.31  ? 280 THR A CG2 1 
ATOM   2718 N  N   . ILE A 1 281 ? -15.092 0.903   -24.554 1.00 42.85  ? 281 ILE A N   1 
ATOM   2719 C  CA  . ILE A 1 281 ? -15.060 -0.582  -24.491 1.00 39.94  ? 281 ILE A CA  1 
ATOM   2720 C  C   . ILE A 1 281 ? -13.942 -0.938  -23.510 1.00 37.13  ? 281 ILE A C   1 
ATOM   2721 O  O   . ILE A 1 281 ? -12.878 -0.329  -23.610 1.00 35.12  ? 281 ILE A O   1 
ATOM   2722 C  CB  . ILE A 1 281 ? -14.889 -1.211  -25.887 1.00 37.46  ? 281 ILE A CB  1 
ATOM   2723 C  CG1 . ILE A 1 281 ? -15.996 -0.767  -26.840 1.00 36.42  ? 281 ILE A CG1 1 
ATOM   2724 C  CG2 . ILE A 1 281 ? -14.834 -2.725  -25.775 1.00 38.22  ? 281 ILE A CG2 1 
ATOM   2725 C  CD1 . ILE A 1 281 ? -15.881 -1.362  -28.235 1.00 37.86  ? 281 ILE A CD1 1 
ATOM   2726 N  N   . LEU A 1 282 ? -14.249 -1.802  -22.539 1.00 42.91  ? 282 LEU A N   1 
ATOM   2727 C  CA  . LEU A 1 282 ? -13.371 -2.181  -21.404 1.00 40.24  ? 282 LEU A CA  1 
ATOM   2728 C  C   . LEU A 1 282 ? -12.588 -0.947  -20.939 1.00 39.14  ? 282 LEU A C   1 
ATOM   2729 O  O   . LEU A 1 282 ? -11.409 -1.083  -20.678 1.00 37.70  ? 282 LEU A O   1 
ATOM   2730 C  CB  . LEU A 1 282 ? -12.444 -3.310  -21.869 1.00 38.55  ? 282 LEU A CB  1 
ATOM   2731 C  CG  . LEU A 1 282 ? -13.148 -4.618  -22.213 1.00 39.75  ? 282 LEU A CG  1 
ATOM   2732 C  CD1 . LEU A 1 282 ? -12.241 -5.543  -22.995 1.00 38.71  ? 282 LEU A CD1 1 
ATOM   2733 C  CD2 . LEU A 1 282 ? -13.677 -5.314  -20.957 1.00 39.08  ? 282 LEU A CD2 1 
ATOM   2734 N  N   . GLY A 1 283 ? -13.230 0.220   -20.855 1.00 41.92  ? 283 GLY A N   1 
ATOM   2735 C  CA  . GLY A 1 283 ? -12.627 1.426   -20.260 1.00 40.47  ? 283 GLY A CA  1 
ATOM   2736 C  C   . GLY A 1 283 ? -11.748 2.185   -21.235 1.00 41.96  ? 283 GLY A C   1 
ATOM   2737 O  O   . GLY A 1 283 ? -11.034 3.097   -20.785 1.00 43.38  ? 283 GLY A O   1 
ATOM   2738 N  N   . SER A 1 284 ? -11.782 1.849   -22.529 1.00 38.98  ? 284 SER A N   1 
ATOM   2739 C  CA  . SER A 1 284 ? -10.987 2.555   -23.568 1.00 35.90  ? 284 SER A CA  1 
ATOM   2740 C  C   . SER A 1 284 ? -11.917 3.221   -24.592 1.00 33.07  ? 284 SER A C   1 
ATOM   2741 O  O   . SER A 1 284 ? -12.925 2.616   -24.958 1.00 33.77  ? 284 SER A O   1 
ATOM   2742 C  CB  . SER A 1 284 ? -10.001 1.624   -24.210 1.00 31.07  ? 284 SER A CB  1 
ATOM   2743 O  OG  . SER A 1 284 ? -9.105  2.373   -25.006 1.00 34.66  ? 284 SER A OG  1 
ATOM   2744 N  N   . ALA A 1 285 ? -11.580 4.429   -25.037 1.00 34.66  ? 285 ALA A N   1 
ATOM   2745 C  CA  . ALA A 1 285 ? -12.297 5.142   -26.119 1.00 33.96  ? 285 ALA A CA  1 
ATOM   2746 C  C   . ALA A 1 285 ? -11.567 4.930   -27.448 1.00 35.70  ? 285 ALA A C   1 
ATOM   2747 O  O   . ALA A 1 285 ? -11.907 5.639   -28.399 1.00 35.16  ? 285 ALA A O   1 
ATOM   2748 C  CB  . ALA A 1 285 ? -12.414 6.606   -25.802 1.00 34.92  ? 285 ALA A CB  1 
ATOM   2749 N  N   . LEU A 1 286 ? -10.551 4.053   -27.478 1.00 36.27  ? 286 LEU A N   1 
ATOM   2750 C  CA  . LEU A 1 286 ? -9.871  3.601   -28.719 1.00 35.20  ? 286 LEU A CA  1 
ATOM   2751 C  C   . LEU A 1 286 ? -9.946  2.074   -28.784 1.00 31.77  ? 286 LEU A C   1 
ATOM   2752 O  O   . LEU A 1 286 ? -10.256 1.445   -27.772 1.00 30.54  ? 286 LEU A O   1 
ATOM   2753 C  CB  . LEU A 1 286 ? -8.414  4.062   -28.731 1.00 40.87  ? 286 LEU A CB  1 
ATOM   2754 C  CG  . LEU A 1 286 ? -8.155  5.513   -29.144 1.00 45.27  ? 286 LEU A CG  1 
ATOM   2755 C  CD1 . LEU A 1 286 ? -6.662  5.741   -29.315 1.00 43.09  ? 286 LEU A CD1 1 
ATOM   2756 C  CD2 . LEU A 1 286 ? -8.905  5.915   -30.417 1.00 48.00  ? 286 LEU A CD2 1 
ATOM   2757 N  N   . LEU A 1 287 ? -9.688  1.510   -29.956 1.00 28.70  ? 287 LEU A N   1 
ATOM   2758 C  CA  . LEU A 1 287 ? -9.636  0.038   -30.144 1.00 29.51  ? 287 LEU A CA  1 
ATOM   2759 C  C   . LEU A 1 287 ? -8.230  -0.477  -29.772 1.00 25.98  ? 287 LEU A C   1 
ATOM   2760 O  O   . LEU A 1 287 ? -7.296  -0.132  -30.449 1.00 24.50  ? 287 LEU A O   1 
ATOM   2761 C  CB  . LEU A 1 287 ? -10.033 -0.257  -31.590 1.00 28.84  ? 287 LEU A CB  1 
ATOM   2762 C  CG  . LEU A 1 287 ? -11.429 0.244   -31.975 1.00 29.49  ? 287 LEU A CG  1 
ATOM   2763 C  CD1 . LEU A 1 287 ? -11.688 0.068   -33.468 1.00 30.01  ? 287 LEU A CD1 1 
ATOM   2764 C  CD2 . LEU A 1 287 ? -12.487 -0.475  -31.163 1.00 32.34  ? 287 LEU A CD2 1 
ATOM   2765 N  N   . GLU A 1 288 ? -8.143  -1.272  -28.709 1.00 26.12  ? 288 GLU A N   1 
ATOM   2766 C  CA  . GLU A 1 288 ? -6.897  -1.782  -28.089 1.00 28.75  ? 288 GLU A CA  1 
ATOM   2767 C  C   . GLU A 1 288 ? -6.322  -2.943  -28.903 1.00 27.01  ? 288 GLU A C   1 
ATOM   2768 O  O   . GLU A 1 288 ? -7.050  -3.966  -29.100 1.00 25.54  ? 288 GLU A O   1 
ATOM   2769 C  CB  . GLU A 1 288 ? -7.196  -2.241  -26.660 1.00 33.69  ? 288 GLU A CB  1 
ATOM   2770 C  CG  . GLU A 1 288 ? -7.598  -1.095  -25.747 1.00 42.01  ? 288 GLU A CG  1 
ATOM   2771 C  CD  . GLU A 1 288 ? -6.497  -0.061  -25.540 1.00 47.72  ? 288 GLU A CD  1 
ATOM   2772 O  OE1 . GLU A 1 288 ? -5.301  -0.431  -25.691 1.00 44.32  ? 288 GLU A OE1 1 
ATOM   2773 O  OE2 . GLU A 1 288 ? -6.831  1.118   -25.263 1.00 54.37  ? 288 GLU A OE2 1 
ATOM   2774 N  N   . ASP A 1 289 ? -5.036  -2.871  -29.257 1.00 24.27  ? 289 ASP A N   1 
ATOM   2775 C  CA  . ASP A 1 289 ? -4.417  -3.960  -30.068 1.00 23.87  ? 289 ASP A CA  1 
ATOM   2776 C  C   . ASP A 1 289 ? -3.212  -4.598  -29.387 1.00 24.69  ? 289 ASP A C   1 
ATOM   2777 O  O   . ASP A 1 289 ? -2.523  -5.351  -30.115 1.00 25.40  ? 289 ASP A O   1 
ATOM   2778 C  CB  . ASP A 1 289 ? -4.081  -3.510  -31.488 1.00 22.43  ? 289 ASP A CB  1 
ATOM   2779 C  CG  . ASP A 1 289 ? -2.840  -2.654  -31.600 1.00 22.72  ? 289 ASP A CG  1 
ATOM   2780 O  OD1 . ASP A 1 289 ? -2.364  -2.175  -30.551 1.00 21.32  ? 289 ASP A OD1 1 
ATOM   2781 O  OD2 . ASP A 1 289 ? -2.376  -2.474  -32.739 1.00 21.32  ? 289 ASP A OD2 1 
ATOM   2782 N  N   . GLU A 1 290 ? -3.000  -4.390  -28.078 1.00 24.79  ? 290 GLU A N   1 
ATOM   2783 C  CA  . GLU A 1 290 ? -1.846  -4.993  -27.340 1.00 24.58  ? 290 GLU A CA  1 
ATOM   2784 C  C   . GLU A 1 290 ? -2.325  -6.063  -26.339 1.00 22.61  ? 290 GLU A C   1 
ATOM   2785 O  O   . GLU A 1 290 ? -1.591  -6.364  -25.386 1.00 25.01  ? 290 GLU A O   1 
ATOM   2786 C  CB  . GLU A 1 290 ? -0.954  -3.878  -26.768 1.00 24.91  ? 290 GLU A CB  1 
ATOM   2787 C  CG  . GLU A 1 290 ? -0.262  -3.063  -27.860 1.00 27.12  ? 290 GLU A CG  1 
ATOM   2788 C  CD  . GLU A 1 290 ? 1.030   -2.316  -27.536 1.00 27.31  ? 290 GLU A CD  1 
ATOM   2789 O  OE1 . GLU A 1 290 ? 1.388   -2.270  -26.349 1.00 25.41  ? 290 GLU A OE1 1 
ATOM   2790 O  OE2 . GLU A 1 290 ? 1.654   -1.726  -28.491 1.00 29.69  ? 290 GLU A OE2 1 
ATOM   2791 N  N   . PHE A 1 291 ? -3.459  -6.721  -26.595 1.00 25.39  ? 291 PHE A N   1 
ATOM   2792 C  CA  . PHE A 1 291 ? -3.869  -7.991  -25.919 1.00 24.85  ? 291 PHE A CA  1 
ATOM   2793 C  C   . PHE A 1 291 ? -4.016  -9.126  -26.942 1.00 25.70  ? 291 PHE A C   1 
ATOM   2794 O  O   . PHE A 1 291 ? -4.876  -9.006  -27.821 1.00 27.49  ? 291 PHE A O   1 
ATOM   2795 C  CB  . PHE A 1 291 ? -5.214  -7.854  -25.213 1.00 27.15  ? 291 PHE A CB  1 
ATOM   2796 C  CG  . PHE A 1 291 ? -5.271  -6.811  -24.139 1.00 27.24  ? 291 PHE A CG  1 
ATOM   2797 C  CD1 . PHE A 1 291 ? -4.862  -7.120  -22.853 1.00 28.06  ? 291 PHE A CD1 1 
ATOM   2798 C  CD2 . PHE A 1 291 ? -5.757  -5.539  -24.408 1.00 30.26  ? 291 PHE A CD2 1 
ATOM   2799 C  CE1 . PHE A 1 291 ? -4.928  -6.155  -21.855 1.00 29.99  ? 291 PHE A CE1 1 
ATOM   2800 C  CE2 . PHE A 1 291 ? -5.818  -4.578  -23.408 1.00 31.74  ? 291 PHE A CE2 1 
ATOM   2801 C  CZ  . PHE A 1 291 ? -5.403  -4.890  -22.132 1.00 29.94  ? 291 PHE A CZ  1 
ATOM   2802 N  N   . THR A 1 292 ? -3.223  -10.192 -26.828 1.00 24.49  ? 292 THR A N   1 
ATOM   2803 C  CA  . THR A 1 292 ? -3.295  -11.364 -27.729 1.00 23.85  ? 292 THR A CA  1 
ATOM   2804 C  C   . THR A 1 292 ? -4.494  -12.228 -27.345 1.00 24.91  ? 292 THR A C   1 
ATOM   2805 O  O   . THR A 1 292 ? -4.995  -12.134 -26.213 1.00 22.31  ? 292 THR A O   1 
ATOM   2806 C  CB  . THR A 1 292 ? -2.041  -12.236 -27.650 1.00 24.89  ? 292 THR A CB  1 
ATOM   2807 O  OG1 . THR A 1 292 ? -1.956  -12.750 -26.323 1.00 25.64  ? 292 THR A OG1 1 
ATOM   2808 C  CG2 . THR A 1 292 ? -0.774  -11.494 -27.999 1.00 26.59  ? 292 THR A CG2 1 
ATOM   2809 N  N   . PRO A 1 293 ? -4.987  -13.083 -28.281 1.00 24.35  ? 293 PRO A N   1 
ATOM   2810 C  CA  . PRO A 1 293 ? -5.982  -14.109 -27.962 1.00 25.54  ? 293 PRO A CA  1 
ATOM   2811 C  C   . PRO A 1 293 ? -5.632  -14.944 -26.727 1.00 27.68  ? 293 PRO A C   1 
ATOM   2812 O  O   . PRO A 1 293 ? -6.505  -15.172 -25.926 1.00 28.76  ? 293 PRO A O   1 
ATOM   2813 C  CB  . PRO A 1 293 ? -5.994  -14.979 -29.228 1.00 24.93  ? 293 PRO A CB  1 
ATOM   2814 C  CG  . PRO A 1 293 ? -5.707  -13.970 -30.333 1.00 25.14  ? 293 PRO A CG  1 
ATOM   2815 C  CD  . PRO A 1 293 ? -4.645  -13.077 -29.719 1.00 25.00  ? 293 PRO A CD  1 
ATOM   2816 N  N   . PHE A 1 294 ? -4.375  -15.359 -26.590 1.00 30.56  ? 294 PHE A N   1 
ATOM   2817 C  CA  . PHE A 1 294 ? -3.883  -16.105 -25.410 1.00 32.09  ? 294 PHE A CA  1 
ATOM   2818 C  C   . PHE A 1 294 ? -4.049  -15.224 -24.168 1.00 32.13  ? 294 PHE A C   1 
ATOM   2819 O  O   . PHE A 1 294 ? -4.595  -15.729 -23.186 1.00 36.40  ? 294 PHE A O   1 
ATOM   2820 C  CB  . PHE A 1 294 ? -2.446  -16.582 -25.629 1.00 34.57  ? 294 PHE A CB  1 
ATOM   2821 C  CG  . PHE A 1 294 ? -1.893  -17.496 -24.555 1.00 40.91  ? 294 PHE A CG  1 
ATOM   2822 C  CD1 . PHE A 1 294 ? -1.489  -16.992 -23.321 1.00 43.42  ? 294 PHE A CD1 1 
ATOM   2823 C  CD2 . PHE A 1 294 ? -1.716  -18.857 -24.794 1.00 42.87  ? 294 PHE A CD2 1 
ATOM   2824 C  CE1 . PHE A 1 294 ? -0.963  -17.827 -22.343 1.00 44.17  ? 294 PHE A CE1 1 
ATOM   2825 C  CE2 . PHE A 1 294 ? -1.183  -19.691 -23.817 1.00 42.18  ? 294 PHE A CE2 1 
ATOM   2826 C  CZ  . PHE A 1 294 ? -0.813  -19.178 -22.593 1.00 44.42  ? 294 PHE A CZ  1 
ATOM   2827 N  N   . ASP A 1 295 ? -3.611  -13.959 -24.217 1.00 32.15  ? 295 ASP A N   1 
ATOM   2828 C  CA  . ASP A 1 295 ? -3.662  -13.012 -23.072 1.00 31.12  ? 295 ASP A CA  1 
ATOM   2829 C  C   . ASP A 1 295 ? -5.108  -12.880 -22.589 1.00 39.47  ? 295 ASP A C   1 
ATOM   2830 O  O   . ASP A 1 295 ? -5.298  -12.802 -21.364 1.00 43.61  ? 295 ASP A O   1 
ATOM   2831 C  CB  . ASP A 1 295 ? -3.210  -11.594 -23.422 1.00 30.85  ? 295 ASP A CB  1 
ATOM   2832 C  CG  . ASP A 1 295 ? -1.729  -11.409 -23.704 1.00 28.37  ? 295 ASP A CG  1 
ATOM   2833 O  OD1 . ASP A 1 295 ? -0.945  -12.307 -23.346 1.00 31.60  ? 295 ASP A OD1 1 
ATOM   2834 O  OD2 . ASP A 1 295 ? -1.377  -10.352 -24.252 1.00 23.55  ? 295 ASP A OD2 1 
ATOM   2835 N  N   . VAL A 1 296 ? -6.071  -12.799 -23.519 1.00 37.30  ? 296 VAL A N   1 
ATOM   2836 C  CA  . VAL A 1 296 ? -7.515  -12.585 -23.201 1.00 38.71  ? 296 VAL A CA  1 
ATOM   2837 C  C   . VAL A 1 296 ? -8.035  -13.826 -22.460 1.00 44.99  ? 296 VAL A C   1 
ATOM   2838 O  O   . VAL A 1 296 ? -8.753  -13.654 -21.472 1.00 44.82  ? 296 VAL A O   1 
ATOM   2839 C  CB  . VAL A 1 296 ? -8.354  -12.236 -24.449 1.00 34.90  ? 296 VAL A CB  1 
ATOM   2840 C  CG1 . VAL A 1 296 ? -9.824  -12.583 -24.284 1.00 35.22  ? 296 VAL A CG1 1 
ATOM   2841 C  CG2 . VAL A 1 296 ? -8.217  -10.769 -24.817 1.00 32.17  ? 296 VAL A CG2 1 
ATOM   2842 N  N   . VAL A 1 297 ? -7.654  -15.032 -22.874 1.00 48.84  ? 297 VAL A N   1 
ATOM   2843 C  CA  . VAL A 1 297 ? -8.081  -16.280 -22.171 1.00 52.35  ? 297 VAL A CA  1 
ATOM   2844 C  C   . VAL A 1 297 ? -7.397  -16.346 -20.795 1.00 55.94  ? 297 VAL A C   1 
ATOM   2845 O  O   . VAL A 1 297 ? -8.099  -16.635 -19.816 1.00 51.35  ? 297 VAL A O   1 
ATOM   2846 C  CB  . VAL A 1 297 ? -7.816  -17.533 -23.019 1.00 50.87  ? 297 VAL A CB  1 
ATOM   2847 C  CG1 . VAL A 1 297 ? -8.203  -18.802 -22.282 1.00 51.54  ? 297 VAL A CG1 1 
ATOM   2848 C  CG2 . VAL A 1 297 ? -8.536  -17.451 -24.356 1.00 48.54  ? 297 VAL A CG2 1 
ATOM   2849 N  N   . ARG A 1 298 ? -6.095  -16.053 -20.697 1.00 64.55  ? 298 ARG A N   1 
ATOM   2850 C  CA  . ARG A 1 298 ? -5.386  -16.052 -19.386 1.00 68.97  ? 298 ARG A CA  1 
ATOM   2851 C  C   . ARG A 1 298 ? -6.132  -15.090 -18.446 1.00 68.42  ? 298 ARG A C   1 
ATOM   2852 O  O   . ARG A 1 298 ? -6.702  -15.584 -17.465 1.00 72.47  ? 298 ARG A O   1 
ATOM   2853 C  CB  . ARG A 1 298 ? -3.888  -15.734 -19.521 1.00 76.79  ? 298 ARG A CB  1 
ATOM   2854 C  CG  . ARG A 1 298 ? -3.052  -16.092 -18.294 1.00 88.36  ? 298 ARG A CG  1 
ATOM   2855 C  CD  . ARG A 1 298 ? -2.940  -14.990 -17.238 1.00 99.12  ? 298 ARG A CD  1 
ATOM   2856 N  NE  . ARG A 1 298 ? -3.875  -15.058 -16.116 1.00 106.12 ? 298 ARG A NE  1 
ATOM   2857 C  CZ  . ARG A 1 298 ? -4.085  -14.088 -15.220 1.00 99.45  ? 298 ARG A CZ  1 
ATOM   2858 N  NH1 . ARG A 1 298 ? -3.426  -12.939 -15.280 1.00 92.25  ? 298 ARG A NH1 1 
ATOM   2859 N  NH2 . ARG A 1 298 ? -4.972  -14.278 -14.262 1.00 97.64  ? 298 ARG A NH2 1 
ATOM   2860 N  N   . GLN A 1 299 ? -6.202  -13.792 -18.761 1.00 64.95  ? 299 GLN A N   1 
ATOM   2861 C  CA  . GLN A 1 299 ? -6.685  -12.738 -17.818 1.00 65.57  ? 299 GLN A CA  1 
ATOM   2862 C  C   . GLN A 1 299 ? -8.165  -12.956 -17.447 1.00 68.28  ? 299 GLN A C   1 
ATOM   2863 O  O   . GLN A 1 299 ? -8.519  -12.512 -16.330 1.00 79.24  ? 299 GLN A O   1 
ATOM   2864 C  CB  . GLN A 1 299 ? -6.425  -11.326 -18.367 1.00 60.04  ? 299 GLN A CB  1 
ATOM   2865 C  CG  . GLN A 1 299 ? -7.127  -10.220 -17.582 1.00 56.91  ? 299 GLN A CG  1 
ATOM   2866 C  CD  . GLN A 1 299 ? -6.469  -8.861  -17.679 1.00 60.93  ? 299 GLN A CD  1 
ATOM   2867 O  OE1 . GLN A 1 299 ? -6.816  -7.931  -16.952 1.00 55.34  ? 299 GLN A OE1 1 
ATOM   2868 N  NE2 . GLN A 1 299 ? -5.506  -8.724  -18.580 1.00 70.25  ? 299 GLN A NE2 1 
ATOM   2869 N  N   . CYS A 1 300 ? -8.981  -13.628 -18.288 1.00 68.66  ? 300 CYS A N   1 
ATOM   2870 C  CA  . CYS A 1 300 ? -10.479 -13.692 -18.177 1.00 68.15  ? 300 CYS A CA  1 
ATOM   2871 C  C   . CYS A 1 300 ? -10.973 -14.925 -17.398 1.00 65.23  ? 300 CYS A C   1 
ATOM   2872 O  O   . CYS A 1 300 ? -10.675 -16.101 -17.640 1.00 64.55  ? 300 CYS A O   1 
ATOM   2873 C  CB  . CYS A 1 300 ? -11.162 -13.644 -19.540 1.00 64.86  ? 300 CYS A CB  1 
ATOM   2874 S  SG  . CYS A 1 300 ? -11.296 -11.949 -20.169 1.00 69.57  ? 300 CYS A SG  1 
ATOM   2875 N  N   . SER B 1 1   ? 12.676  8.200   -24.523 1.00 31.03  ? 1   SER B N   1 
ATOM   2876 C  CA  . SER B 1 1   ? 11.303  8.708   -24.303 1.00 31.51  ? 1   SER B CA  1 
ATOM   2877 C  C   . SER B 1 1   ? 10.263  7.574   -24.355 1.00 33.27  ? 1   SER B C   1 
ATOM   2878 O  O   . SER B 1 1   ? 10.640  6.368   -24.393 1.00 32.54  ? 1   SER B O   1 
ATOM   2879 C  CB  . SER B 1 1   ? 11.011  9.768   -25.319 1.00 32.44  ? 1   SER B CB  1 
ATOM   2880 O  OG  . SER B 1 1   ? 11.272  9.246   -26.596 1.00 32.23  ? 1   SER B OG  1 
ATOM   2881 N  N   . GLY B 1 2   ? 8.989   7.959   -24.388 1.00 29.89  ? 2   GLY B N   1 
ATOM   2882 C  CA  . GLY B 1 2   ? 7.836   7.046   -24.332 1.00 30.58  ? 2   GLY B CA  1 
ATOM   2883 C  C   . GLY B 1 2   ? 7.201   7.169   -22.965 1.00 29.12  ? 2   GLY B C   1 
ATOM   2884 O  O   . GLY B 1 2   ? 7.876   7.616   -22.024 1.00 29.34  ? 2   GLY B O   1 
ATOM   2885 N  N   . PHE B 1 3   ? 5.941   6.801   -22.843 1.00 30.98  ? 3   PHE B N   1 
ATOM   2886 C  CA  . PHE B 1 3   ? 5.190   6.939   -21.573 1.00 30.86  ? 3   PHE B CA  1 
ATOM   2887 C  C   . PHE B 1 3   ? 4.265   5.752   -21.461 1.00 28.92  ? 3   PHE B C   1 
ATOM   2888 O  O   . PHE B 1 3   ? 3.514   5.501   -22.389 1.00 30.42  ? 3   PHE B O   1 
ATOM   2889 C  CB  . PHE B 1 3   ? 4.394   8.247   -21.469 1.00 31.99  ? 3   PHE B CB  1 
ATOM   2890 C  CG  . PHE B 1 3   ? 4.227   8.651   -20.031 1.00 31.68  ? 3   PHE B CG  1 
ATOM   2891 C  CD1 . PHE B 1 3   ? 5.346   8.950   -19.268 1.00 31.79  ? 3   PHE B CD1 1 
ATOM   2892 C  CD2 . PHE B 1 3   ? 2.989   8.598   -19.408 1.00 31.58  ? 3   PHE B CD2 1 
ATOM   2893 C  CE1 . PHE B 1 3   ? 5.225   9.258   -17.923 1.00 32.81  ? 3   PHE B CE1 1 
ATOM   2894 C  CE2 . PHE B 1 3   ? 2.871   8.910   -18.063 1.00 33.11  ? 3   PHE B CE2 1 
ATOM   2895 C  CZ  . PHE B 1 3   ? 3.988   9.244   -17.323 1.00 31.27  ? 3   PHE B CZ  1 
ATOM   2896 N  N   . ARG B 1 4   ? 4.407   5.012   -20.376 1.00 29.17  ? 4   ARG B N   1 
ATOM   2897 C  CA  . ARG B 1 4   ? 3.633   3.774   -20.153 1.00 28.58  ? 4   ARG B CA  1 
ATOM   2898 C  C   . ARG B 1 4   ? 3.146   3.769   -18.701 1.00 24.34  ? 4   ARG B C   1 
ATOM   2899 O  O   . ARG B 1 4   ? 3.846   4.301   -17.817 1.00 23.70  ? 4   ARG B O   1 
ATOM   2900 C  CB  . ARG B 1 4   ? 4.487   2.558   -20.540 1.00 31.44  ? 4   ARG B CB  1 
ATOM   2901 C  CG  . ARG B 1 4   ? 4.506   2.279   -22.038 1.00 33.25  ? 4   ARG B CG  1 
ATOM   2902 C  CD  . ARG B 1 4   ? 3.588   1.121   -22.431 1.00 33.01  ? 4   ARG B CD  1 
ATOM   2903 N  NE  . ARG B 1 4   ? 3.776   0.761   -23.831 1.00 34.70  ? 4   ARG B NE  1 
ATOM   2904 C  CZ  . ARG B 1 4   ? 2.889   0.106   -24.581 1.00 34.86  ? 4   ARG B CZ  1 
ATOM   2905 N  NH1 . ARG B 1 4   ? 1.735   -0.265  -24.059 1.00 36.97  ? 4   ARG B NH1 1 
ATOM   2906 N  NH2 . ARG B 1 4   ? 3.146   -0.156  -25.854 1.00 33.10  ? 4   ARG B NH2 1 
ATOM   2907 N  N   . LYS B 1 5   ? 1.977   3.190   -18.487 1.00 24.75  ? 5   LYS B N   1 
ATOM   2908 C  CA  . LYS B 1 5   ? 1.509   2.782   -17.152 1.00 27.17  ? 5   LYS B CA  1 
ATOM   2909 C  C   . LYS B 1 5   ? 2.482   1.708   -16.664 1.00 27.04  ? 5   LYS B C   1 
ATOM   2910 O  O   . LYS B 1 5   ? 2.523   0.606   -17.240 1.00 29.35  ? 5   LYS B O   1 
ATOM   2911 C  CB  . LYS B 1 5   ? 0.070   2.279   -17.175 1.00 30.00  ? 5   LYS B CB  1 
ATOM   2912 C  CG  . LYS B 1 5   ? -0.535  2.230   -15.786 1.00 35.85  ? 5   LYS B CG  1 
ATOM   2913 C  CD  . LYS B 1 5   ? -1.995  2.496   -15.764 1.00 42.18  ? 5   LYS B CD  1 
ATOM   2914 C  CE  . LYS B 1 5   ? -2.348  3.917   -16.133 1.00 43.94  ? 5   LYS B CE  1 
ATOM   2915 N  NZ  . LYS B 1 5   ? -3.711  3.952   -16.708 1.00 48.40  ? 5   LYS B NZ  1 
ATOM   2916 N  N   . MET B 1 6   ? 3.255   2.074   -15.663 1.00 24.29  ? 6   MET B N   1 
ATOM   2917 C  CA  . MET B 1 6   ? 4.446   1.342   -15.193 1.00 27.48  ? 6   MET B CA  1 
ATOM   2918 C  C   . MET B 1 6   ? 4.232   0.966   -13.735 1.00 21.95  ? 6   MET B C   1 
ATOM   2919 O  O   . MET B 1 6   ? 3.970   1.873   -12.938 1.00 22.09  ? 6   MET B O   1 
ATOM   2920 C  CB  . MET B 1 6   ? 5.646   2.289   -15.320 1.00 30.34  ? 6   MET B CB  1 
ATOM   2921 C  CG  . MET B 1 6   ? 6.966   1.644   -15.162 1.00 34.67  ? 6   MET B CG  1 
ATOM   2922 S  SD  . MET B 1 6   ? 8.264   2.823   -15.619 1.00 37.52  ? 6   MET B SD  1 
ATOM   2923 C  CE  . MET B 1 6   ? 8.222   2.625   -17.398 1.00 35.75  ? 6   MET B CE  1 
ATOM   2924 N  N   . ALA B 1 7   ? 4.377   -0.305  -13.392 1.00 20.80  ? 7   ALA B N   1 
ATOM   2925 C  CA  . ALA B 1 7   ? 4.344   -0.787  -11.997 1.00 20.50  ? 7   ALA B CA  1 
ATOM   2926 C  C   . ALA B 1 7   ? 5.756   -0.781  -11.418 1.00 21.39  ? 7   ALA B C   1 
ATOM   2927 O  O   . ALA B 1 7   ? 6.718   -0.899  -12.194 1.00 23.66  ? 7   ALA B O   1 
ATOM   2928 C  CB  . ALA B 1 7   ? 3.725   -2.165  -11.941 1.00 20.97  ? 7   ALA B CB  1 
ATOM   2929 N  N   . PHE B 1 8   ? 5.879   -0.724  -10.096 1.00 20.18  ? 8   PHE B N   1 
ATOM   2930 C  CA  . PHE B 1 8   ? 7.151   -1.040  -9.403  1.00 22.05  ? 8   PHE B CA  1 
ATOM   2931 C  C   . PHE B 1 8   ? 7.556   -2.485  -9.704  1.00 21.93  ? 8   PHE B C   1 
ATOM   2932 O  O   . PHE B 1 8   ? 6.719   -3.353  -9.931  1.00 23.03  ? 8   PHE B O   1 
ATOM   2933 C  CB  . PHE B 1 8   ? 7.036   -0.764  -7.911  1.00 21.38  ? 8   PHE B CB  1 
ATOM   2934 C  CG  . PHE B 1 8   ? 7.027   0.704   -7.588  1.00 21.37  ? 8   PHE B CG  1 
ATOM   2935 C  CD1 . PHE B 1 8   ? 8.197   1.449   -7.658  1.00 23.09  ? 8   PHE B CD1 1 
ATOM   2936 C  CD2 . PHE B 1 8   ? 5.856   1.343   -7.245  1.00 23.65  ? 8   PHE B CD2 1 
ATOM   2937 C  CE1 . PHE B 1 8   ? 8.200   2.806   -7.370  1.00 25.00  ? 8   PHE B CE1 1 
ATOM   2938 C  CE2 . PHE B 1 8   ? 5.857   2.703   -6.957  1.00 25.90  ? 8   PHE B CE2 1 
ATOM   2939 C  CZ  . PHE B 1 8   ? 7.030   3.432   -7.013  1.00 25.92  ? 8   PHE B CZ  1 
ATOM   2940 N  N   . PRO B 1 9   ? 8.871   -2.790  -9.718  1.00 22.38  ? 9   PRO B N   1 
ATOM   2941 C  CA  . PRO B 1 9   ? 9.324   -4.184  -9.782  1.00 22.01  ? 9   PRO B CA  1 
ATOM   2942 C  C   . PRO B 1 9   ? 8.712   -4.946  -8.593  1.00 22.64  ? 9   PRO B C   1 
ATOM   2943 O  O   . PRO B 1 9   ? 8.814   -4.439  -7.485  1.00 26.44  ? 9   PRO B O   1 
ATOM   2944 C  CB  . PRO B 1 9   ? 10.846  -4.070  -9.676  1.00 23.52  ? 9   PRO B CB  1 
ATOM   2945 C  CG  . PRO B 1 9   ? 11.160  -2.624  -10.099 1.00 23.66  ? 9   PRO B CG  1 
ATOM   2946 C  CD  . PRO B 1 9   ? 9.967   -1.815  -9.643  1.00 22.90  ? 9   PRO B CD  1 
ATOM   2947 N  N   . SER B 1 10  ? 8.053   -6.078  -8.839  1.00 22.06  ? 10  SER B N   1 
ATOM   2948 C  CA  . SER B 1 10  ? 7.246   -6.833  -7.837  1.00 23.01  ? 10  SER B CA  1 
ATOM   2949 C  C   . SER B 1 10  ? 8.066   -7.815  -6.976  1.00 23.42  ? 10  SER B C   1 
ATOM   2950 O  O   . SER B 1 10  ? 7.487   -8.361  -6.041  1.00 23.59  ? 10  SER B O   1 
ATOM   2951 C  CB  . SER B 1 10  ? 6.083   -7.551  -8.485  1.00 23.39  ? 10  SER B CB  1 
ATOM   2952 O  OG  . SER B 1 10  ? 6.472   -8.440  -9.521  1.00 24.91  ? 10  SER B OG  1 
ATOM   2953 N  N   . GLY B 1 11  ? 9.349   -8.050  -7.257  1.00 24.93  ? 11  GLY B N   1 
ATOM   2954 C  CA  . GLY B 1 11  ? 10.107  -9.175  -6.669  1.00 26.18  ? 11  GLY B CA  1 
ATOM   2955 C  C   . GLY B 1 11  ? 10.121  -9.147  -5.145  1.00 27.34  ? 11  GLY B C   1 
ATOM   2956 O  O   . GLY B 1 11  ? 9.948   -10.209 -4.514  1.00 26.77  ? 11  GLY B O   1 
ATOM   2957 N  N   . LYS B 1 12  ? 10.331  -7.982  -4.540  1.00 24.79  ? 12  LYS B N   1 
ATOM   2958 C  CA  . LYS B 1 12  ? 10.354  -7.876  -3.056  1.00 25.24  ? 12  LYS B CA  1 
ATOM   2959 C  C   . LYS B 1 12  ? 9.018   -8.301  -2.440  1.00 25.21  ? 12  LYS B C   1 
ATOM   2960 O  O   . LYS B 1 12  ? 9.037   -8.713  -1.284  1.00 26.91  ? 12  LYS B O   1 
ATOM   2961 C  CB  . LYS B 1 12  ? 10.693  -6.454  -2.631  1.00 28.49  ? 12  LYS B CB  1 
ATOM   2962 C  CG  . LYS B 1 12  ? 12.151  -6.073  -2.819  1.00 28.14  ? 12  LYS B CG  1 
ATOM   2963 C  CD  . LYS B 1 12  ? 12.385  -4.665  -2.322  1.00 32.89  ? 12  LYS B CD  1 
ATOM   2964 C  CE  . LYS B 1 12  ? 13.850  -4.301  -2.170  1.00 35.52  ? 12  LYS B CE  1 
ATOM   2965 N  NZ  . LYS B 1 12  ? 14.589  -4.582  -3.421  1.00 36.34  ? 12  LYS B NZ  1 
ATOM   2966 N  N   . VAL B 1 13  ? 7.916   -8.227  -3.195  1.00 24.48  ? 13  VAL B N   1 
ATOM   2967 C  CA  . VAL B 1 13  ? 6.558   -8.619  -2.736  1.00 24.51  ? 13  VAL B CA  1 
ATOM   2968 C  C   . VAL B 1 13  ? 6.259   -10.083 -3.101  1.00 24.63  ? 13  VAL B C   1 
ATOM   2969 O  O   . VAL B 1 13  ? 5.699   -10.806 -2.238  1.00 25.53  ? 13  VAL B O   1 
ATOM   2970 C  CB  . VAL B 1 13  ? 5.533   -7.623  -3.296  1.00 24.39  ? 13  VAL B CB  1 
ATOM   2971 C  CG1 . VAL B 1 13  ? 4.147   -7.966  -2.818  1.00 23.74  ? 13  VAL B CG1 1 
ATOM   2972 C  CG2 . VAL B 1 13  ? 5.900   -6.188  -2.947  1.00 22.86  ? 13  VAL B CG2 1 
ATOM   2973 N  N   . GLU B 1 14  ? 6.646   -10.546 -4.294  1.00 25.58  ? 14  GLU B N   1 
ATOM   2974 C  CA  . GLU B 1 14  ? 6.538   -11.979 -4.693  1.00 23.87  ? 14  GLU B CA  1 
ATOM   2975 C  C   . GLU B 1 14  ? 7.115   -12.875 -3.577  1.00 24.29  ? 14  GLU B C   1 
ATOM   2976 O  O   . GLU B 1 14  ? 6.473   -13.866 -3.254  1.00 24.28  ? 14  GLU B O   1 
ATOM   2977 C  CB  . GLU B 1 14  ? 7.274   -12.254 -6.003  1.00 25.04  ? 14  GLU B CB  1 
ATOM   2978 C  CG  . GLU B 1 14  ? 6.653   -11.614 -7.226  1.00 24.38  ? 14  GLU B CG  1 
ATOM   2979 C  CD  . GLU B 1 14  ? 7.560   -11.619 -8.447  1.00 25.16  ? 14  GLU B CD  1 
ATOM   2980 O  OE1 . GLU B 1 14  ? 7.999   -12.700 -8.846  1.00 25.31  ? 14  GLU B OE1 1 
ATOM   2981 O  OE2 . GLU B 1 14  ? 7.843   -10.535 -8.997  1.00 24.04  ? 14  GLU B OE2 1 
ATOM   2982 N  N   . GLY B 1 15  ? 8.239   -12.492 -2.966  1.00 25.56  ? 15  GLY B N   1 
ATOM   2983 C  CA  . GLY B 1 15  ? 8.884   -13.182 -1.828  1.00 26.67  ? 15  GLY B CA  1 
ATOM   2984 C  C   . GLY B 1 15  ? 8.023   -13.232 -0.564  1.00 27.25  ? 15  GLY B C   1 
ATOM   2985 O  O   . GLY B 1 15  ? 8.424   -13.932 0.367   1.00 22.38  ? 15  GLY B O   1 
ATOM   2986 N  N   . CYS B 1 16  ? 6.881   -12.530 -0.509  1.00 26.51  ? 16  CYS B N   1 
ATOM   2987 C  CA  . CYS B 1 16  ? 6.019   -12.483 0.705   1.00 26.54  ? 16  CYS B CA  1 
ATOM   2988 C  C   . CYS B 1 16  ? 4.646   -13.131 0.555   1.00 25.50  ? 16  CYS B C   1 
ATOM   2989 O  O   . CYS B 1 16  ? 3.894   -13.145 1.534   1.00 27.06  ? 16  CYS B O   1 
ATOM   2990 C  CB  . CYS B 1 16  ? 5.801   -11.035 1.111   1.00 26.95  ? 16  CYS B CB  1 
ATOM   2991 S  SG  . CYS B 1 16  ? 7.372   -10.275 1.555   1.00 28.18  ? 16  CYS B SG  1 
ATOM   2992 N  N   A MET B 1 17  ? 4.316   -13.627 -0.642  0.25 25.80  ? 17  MET B N   1 
ATOM   2993 N  N   B MET B 1 17  ? 4.316   -13.627 -0.642  0.25 25.80  ? 17  MET B N   1 
ATOM   2994 N  N   C MET B 1 17  ? 4.349   -13.695 -0.621  0.25 26.75  ? 17  MET B N   1 
ATOM   2995 N  N   D MET B 1 17  ? 4.349   -13.695 -0.621  0.25 26.75  ? 17  MET B N   1 
ATOM   2996 C  CA  A MET B 1 17  ? 2.961   -14.144 -0.967  0.25 24.86  ? 17  MET B CA  1 
ATOM   2997 C  CA  B MET B 1 17  ? 2.961   -14.144 -0.967  0.25 24.86  ? 17  MET B CA  1 
ATOM   2998 C  CA  C MET B 1 17  ? 2.995   -14.174 -1.006  0.25 26.44  ? 17  MET B CA  1 
ATOM   2999 C  CA  D MET B 1 17  ? 2.995   -14.174 -1.006  0.25 26.44  ? 17  MET B CA  1 
ATOM   3000 C  C   A MET B 1 17  ? 2.876   -15.623 -0.573  0.25 26.40  ? 17  MET B C   1 
ATOM   3001 C  C   B MET B 1 17  ? 2.876   -15.623 -0.573  0.25 26.40  ? 17  MET B C   1 
ATOM   3002 C  C   C MET B 1 17  ? 2.830   -15.655 -0.649  0.25 27.43  ? 17  MET B C   1 
ATOM   3003 C  C   D MET B 1 17  ? 2.830   -15.655 -0.649  0.25 27.43  ? 17  MET B C   1 
ATOM   3004 O  O   A MET B 1 17  ? 3.762   -16.398 -0.968  0.25 26.55  ? 17  MET B O   1 
ATOM   3005 O  O   B MET B 1 17  ? 3.762   -16.398 -0.968  0.25 26.55  ? 17  MET B O   1 
ATOM   3006 O  O   C MET B 1 17  ? 3.582   -16.480 -1.198  0.25 27.60  ? 17  MET B O   1 
ATOM   3007 O  O   D MET B 1 17  ? 3.582   -16.480 -1.198  0.25 27.60  ? 17  MET B O   1 
ATOM   3008 C  CB  A MET B 1 17  ? 2.643   -13.981 -2.456  0.25 23.78  ? 17  MET B CB  1 
ATOM   3009 C  CB  B MET B 1 17  ? 2.643   -13.981 -2.456  0.25 23.78  ? 17  MET B CB  1 
ATOM   3010 C  CB  C MET B 1 17  ? 2.784   -13.984 -2.509  0.25 26.52  ? 17  MET B CB  1 
ATOM   3011 C  CB  D MET B 1 17  ? 2.784   -13.984 -2.509  0.25 26.52  ? 17  MET B CB  1 
ATOM   3012 C  CG  A MET B 1 17  ? 2.641   -12.534 -2.919  0.25 23.11  ? 17  MET B CG  1 
ATOM   3013 C  CG  B MET B 1 17  ? 2.641   -12.534 -2.919  0.25 23.11  ? 17  MET B CG  1 
ATOM   3014 C  CG  C MET B 1 17  ? 2.887   -12.537 -2.928  0.25 26.59  ? 17  MET B CG  1 
ATOM   3015 C  CG  D MET B 1 17  ? 2.887   -12.537 -2.928  0.25 26.59  ? 17  MET B CG  1 
ATOM   3016 S  SD  A MET B 1 17  ? 1.714   -11.437 -1.819  0.25 21.79  ? 17  MET B SD  1 
ATOM   3017 S  SD  B MET B 1 17  ? 1.714   -11.437 -1.819  0.25 21.79  ? 17  MET B SD  1 
ATOM   3018 S  SD  C MET B 1 17  ? 1.398   -11.640 -2.468  0.25 26.32  ? 17  MET B SD  1 
ATOM   3019 S  SD  D MET B 1 17  ? 1.398   -11.640 -2.468  0.25 26.32  ? 17  MET B SD  1 
ATOM   3020 C  CE  A MET B 1 17  ? 0.166   -12.327 -1.661  0.25 22.54  ? 17  MET B CE  1 
ATOM   3021 C  CE  B MET B 1 17  ? 0.166   -12.327 -1.661  0.25 22.54  ? 17  MET B CE  1 
ATOM   3022 C  CE  C MET B 1 17  ? 2.081   -10.066 -1.971  0.25 27.55  ? 17  MET B CE  1 
ATOM   3023 C  CE  D MET B 1 17  ? 2.081   -10.066 -1.971  0.25 27.55  ? 17  MET B CE  1 
ATOM   3024 N  N   . VAL B 1 18  ? 1.849   -15.974 0.204   1.00 27.84  ? 18  VAL B N   1 
ATOM   3025 C  CA  . VAL B 1 18  ? 1.546   -17.369 0.617   1.00 29.17  ? 18  VAL B CA  1 
ATOM   3026 C  C   . VAL B 1 18  ? 0.062   -17.646 0.336   1.00 30.52  ? 18  VAL B C   1 
ATOM   3027 O  O   . VAL B 1 18  ? -0.718  -16.700 0.071   1.00 29.81  ? 18  VAL B O   1 
ATOM   3028 C  CB  . VAL B 1 18  ? 1.945   -17.592 2.089   1.00 29.76  ? 18  VAL B CB  1 
ATOM   3029 C  CG1 . VAL B 1 18  ? 3.385   -17.173 2.337   1.00 30.59  ? 18  VAL B CG1 1 
ATOM   3030 C  CG2 . VAL B 1 18  ? 1.016   -16.887 3.062   1.00 31.39  ? 18  VAL B CG2 1 
ATOM   3031 N  N   . GLN B 1 19  ? -0.298  -18.924 0.336   1.00 33.40  ? 19  GLN B N   1 
ATOM   3032 C  CA  . GLN B 1 19  ? -1.690  -19.429 0.222   1.00 34.00  ? 19  GLN B CA  1 
ATOM   3033 C  C   . GLN B 1 19  ? -2.211  -19.660 1.644   1.00 32.66  ? 19  GLN B C   1 
ATOM   3034 O  O   . GLN B 1 19  ? -1.482  -20.228 2.471   1.00 37.34  ? 19  GLN B O   1 
ATOM   3035 C  CB  . GLN B 1 19  ? -1.686  -20.691 -0.637  1.00 39.64  ? 19  GLN B CB  1 
ATOM   3036 C  CG  . GLN B 1 19  ? -3.058  -21.329 -0.841  1.00 47.22  ? 19  GLN B CG  1 
ATOM   3037 C  CD  . GLN B 1 19  ? -2.979  -22.755 -1.359  1.00 53.24  ? 19  GLN B CD  1 
ATOM   3038 O  OE1 . GLN B 1 19  ? -2.373  -23.645 -0.744  1.00 53.45  ? 19  GLN B OE1 1 
ATOM   3039 N  NE2 . GLN B 1 19  ? -3.614  -22.990 -2.500  1.00 48.90  ? 19  GLN B NE2 1 
ATOM   3040 N  N   . VAL B 1 20  ? -3.396  -19.161 1.950   1.00 34.08  ? 20  VAL B N   1 
ATOM   3041 C  CA  . VAL B 1 20  ? -4.061  -19.393 3.263   1.00 34.34  ? 20  VAL B CA  1 
ATOM   3042 C  C   . VAL B 1 20  ? -5.399  -20.094 3.027   1.00 36.30  ? 20  VAL B C   1 
ATOM   3043 O  O   . VAL B 1 20  ? -6.228  -19.567 2.247   1.00 35.72  ? 20  VAL B O   1 
ATOM   3044 C  CB  . VAL B 1 20  ? -4.270  -18.076 4.019   1.00 33.08  ? 20  VAL B CB  1 
ATOM   3045 C  CG1 . VAL B 1 20  ? -5.020  -18.328 5.314   1.00 31.79  ? 20  VAL B CG1 1 
ATOM   3046 C  CG2 . VAL B 1 20  ? -2.949  -17.353 4.258   1.00 32.92  ? 20  VAL B CG2 1 
ATOM   3047 N  N   . THR B 1 21  ? -5.621  -21.212 3.715   1.00 37.75  ? 21  THR B N   1 
ATOM   3048 C  CA  . THR B 1 21  ? -6.870  -22.016 3.616   1.00 37.53  ? 21  THR B CA  1 
ATOM   3049 C  C   . THR B 1 21  ? -7.508  -22.110 5.005   1.00 39.46  ? 21  THR B C   1 
ATOM   3050 O  O   . THR B 1 21  ? -6.799  -22.349 6.004   1.00 43.58  ? 21  THR B O   1 
ATOM   3051 C  CB  . THR B 1 21  ? -6.601  -23.401 3.012   1.00 41.05  ? 21  THR B CB  1 
ATOM   3052 O  OG1 . THR B 1 21  ? -5.895  -23.255 1.777   1.00 33.42  ? 21  THR B OG1 1 
ATOM   3053 C  CG2 . THR B 1 21  ? -7.877  -24.189 2.786   1.00 40.73  ? 21  THR B CG2 1 
ATOM   3054 N  N   . CYS B 1 22  ? -8.799  -21.836 5.072   1.00 40.51  ? 22  CYS B N   1 
ATOM   3055 C  CA  . CYS B 1 22  ? -9.642  -22.084 6.259   1.00 42.41  ? 22  CYS B CA  1 
ATOM   3056 C  C   . CYS B 1 22  ? -10.913 -22.763 5.743   1.00 44.19  ? 22  CYS B C   1 
ATOM   3057 O  O   . CYS B 1 22  ? -11.575 -22.178 4.866   1.00 41.74  ? 22  CYS B O   1 
ATOM   3058 C  CB  . CYS B 1 22  ? -9.905  -20.778 6.989   1.00 42.06  ? 22  CYS B CB  1 
ATOM   3059 S  SG  . CYS B 1 22  ? -10.925 -20.960 8.466   1.00 42.24  ? 22  CYS B SG  1 
ATOM   3060 N  N   . GLY B 1 23  ? -11.172 -23.997 6.190   1.00 47.38  ? 23  GLY B N   1 
ATOM   3061 C  CA  . GLY B 1 23  ? -12.240 -24.854 5.646   1.00 45.10  ? 23  GLY B CA  1 
ATOM   3062 C  C   . GLY B 1 23  ? -12.069 -25.057 4.153   1.00 43.35  ? 23  GLY B C   1 
ATOM   3063 O  O   . GLY B 1 23  ? -11.058 -25.613 3.760   1.00 44.52  ? 23  GLY B O   1 
ATOM   3064 N  N   . THR B 1 24  ? -13.026 -24.598 3.350   1.00 48.26  ? 24  THR B N   1 
ATOM   3065 C  CA  . THR B 1 24  ? -13.026 -24.751 1.873   1.00 53.48  ? 24  THR B CA  1 
ATOM   3066 C  C   . THR B 1 24  ? -12.445 -23.497 1.216   1.00 54.30  ? 24  THR B C   1 
ATOM   3067 O  O   . THR B 1 24  ? -12.079 -23.596 0.034   1.00 59.91  ? 24  THR B O   1 
ATOM   3068 C  CB  . THR B 1 24  ? -14.432 -25.009 1.309   1.00 56.82  ? 24  THR B CB  1 
ATOM   3069 O  OG1 . THR B 1 24  ? -15.374 -24.144 1.940   1.00 58.90  ? 24  THR B OG1 1 
ATOM   3070 C  CG2 . THR B 1 24  ? -14.889 -26.435 1.500   1.00 58.36  ? 24  THR B CG2 1 
ATOM   3071 N  N   . THR B 1 25  ? -12.390 -22.366 1.928   1.00 55.01  ? 25  THR B N   1 
ATOM   3072 C  CA  . THR B 1 25  ? -11.914 -21.073 1.372   1.00 49.58  ? 25  THR B CA  1 
ATOM   3073 C  C   . THR B 1 25  ? -10.390 -21.081 1.315   1.00 47.42  ? 25  THR B C   1 
ATOM   3074 O  O   . THR B 1 25  ? -9.725  -21.429 2.328   1.00 54.31  ? 25  THR B O   1 
ATOM   3075 C  CB  . THR B 1 25  ? -12.321 -19.854 2.205   1.00 51.61  ? 25  THR B CB  1 
ATOM   3076 O  OG1 . THR B 1 25  ? -13.678 -19.987 2.621   1.00 54.67  ? 25  THR B OG1 1 
ATOM   3077 C  CG2 . THR B 1 25  ? -12.148 -18.555 1.447   1.00 55.09  ? 25  THR B CG2 1 
ATOM   3078 N  N   A THR B 1 26  ? -9.847  -20.831 0.125   0.25 44.77  ? 26  THR B N   1 
ATOM   3079 N  N   B THR B 1 26  ? -9.847  -20.831 0.125   0.25 44.77  ? 26  THR B N   1 
ATOM   3080 N  N   C THR B 1 26  ? -9.842  -20.583 0.200   0.25 49.50  ? 26  THR B N   1 
ATOM   3081 N  N   D THR B 1 26  ? -9.842  -20.583 0.200   0.25 49.50  ? 26  THR B N   1 
ATOM   3082 C  CA  A THR B 1 26  ? -8.402  -20.591 -0.105  0.25 41.21  ? 26  THR B CA  1 
ATOM   3083 C  CA  B THR B 1 26  ? -8.402  -20.591 -0.105  0.25 41.21  ? 26  THR B CA  1 
ATOM   3084 C  CA  C THR B 1 26  ? -8.384  -20.423 -0.051  0.25 47.72  ? 26  THR B CA  1 
ATOM   3085 C  CA  D THR B 1 26  ? -8.384  -20.423 -0.051  0.25 47.72  ? 26  THR B CA  1 
ATOM   3086 C  C   A THR B 1 26  ? -8.253  -19.196 -0.713  0.25 37.60  ? 26  THR B C   1 
ATOM   3087 C  C   B THR B 1 26  ? -8.253  -19.196 -0.713  0.25 37.60  ? 26  THR B C   1 
ATOM   3088 C  C   C THR B 1 26  ? -8.104  -19.060 -0.702  0.25 45.44  ? 26  THR B C   1 
ATOM   3089 C  C   D THR B 1 26  ? -8.104  -19.060 -0.702  0.25 45.44  ? 26  THR B C   1 
ATOM   3090 O  O   A THR B 1 26  ? -9.121  -18.806 -1.516  0.25 36.97  ? 26  THR B O   1 
ATOM   3091 O  O   B THR B 1 26  ? -9.121  -18.806 -1.516  0.25 36.97  ? 26  THR B O   1 
ATOM   3092 O  O   C THR B 1 26  ? -8.478  -18.891 -1.878  0.25 47.09  ? 26  THR B O   1 
ATOM   3093 O  O   D THR B 1 26  ? -8.478  -18.891 -1.878  0.25 47.09  ? 26  THR B O   1 
ATOM   3094 C  CB  A THR B 1 26  ? -7.786  -21.704 -0.959  0.25 40.92  ? 26  THR B CB  1 
ATOM   3095 C  CB  B THR B 1 26  ? -7.786  -21.704 -0.959  0.25 40.92  ? 26  THR B CB  1 
ATOM   3096 C  CB  C THR B 1 26  ? -7.875  -21.584 -0.914  0.25 47.79  ? 26  THR B CB  1 
ATOM   3097 C  CB  D THR B 1 26  ? -7.875  -21.584 -0.914  0.25 47.79  ? 26  THR B CB  1 
ATOM   3098 O  OG1 A THR B 1 26  ? -7.711  -22.867 -0.133  0.25 40.85  ? 26  THR B OG1 1 
ATOM   3099 O  OG1 B THR B 1 26  ? -7.711  -22.867 -0.133  0.25 40.85  ? 26  THR B OG1 1 
ATOM   3100 O  OG1 C THR B 1 26  ? -7.317  -22.557 -0.031  0.25 47.93  ? 26  THR B OG1 1 
ATOM   3101 O  OG1 D THR B 1 26  ? -7.317  -22.557 -0.031  0.25 47.93  ? 26  THR B OG1 1 
ATOM   3102 C  CG2 A THR B 1 26  ? -6.413  -21.350 -1.484  0.25 40.54  ? 26  THR B CG2 1 
ATOM   3103 C  CG2 B THR B 1 26  ? -6.413  -21.350 -1.484  0.25 40.54  ? 26  THR B CG2 1 
ATOM   3104 C  CG2 C THR B 1 26  ? -6.846  -21.157 -1.937  0.25 47.75  ? 26  THR B CG2 1 
ATOM   3105 C  CG2 D THR B 1 26  ? -6.846  -21.157 -1.937  0.25 47.75  ? 26  THR B CG2 1 
ATOM   3106 N  N   A LEU B 1 27  ? -7.227  -18.460 -0.289  0.25 34.38  ? 27  LEU B N   1 
ATOM   3107 N  N   B LEU B 1 27  ? -7.227  -18.460 -0.289  0.25 34.38  ? 27  LEU B N   1 
ATOM   3108 N  N   C LEU B 1 27  ? -7.469  -18.134 0.030   0.25 43.07  ? 27  LEU B N   1 
ATOM   3109 N  N   D LEU B 1 27  ? -7.469  -18.134 0.030   0.25 43.07  ? 27  LEU B N   1 
ATOM   3110 C  CA  A LEU B 1 27  ? -6.875  -17.131 -0.848  0.25 32.07  ? 27  LEU B CA  1 
ATOM   3111 C  CA  B LEU B 1 27  ? -6.875  -17.131 -0.848  0.25 32.07  ? 27  LEU B CA  1 
ATOM   3112 C  CA  C LEU B 1 27  ? -6.995  -16.822 -0.497  0.25 40.45  ? 27  LEU B CA  1 
ATOM   3113 C  CA  D LEU B 1 27  ? -6.995  -16.822 -0.497  0.25 40.45  ? 27  LEU B CA  1 
ATOM   3114 C  C   A LEU B 1 27  ? -5.441  -16.788 -0.439  0.25 29.49  ? 27  LEU B C   1 
ATOM   3115 C  C   B LEU B 1 27  ? -5.441  -16.788 -0.439  0.25 29.49  ? 27  LEU B C   1 
ATOM   3116 C  C   C LEU B 1 27  ? -5.486  -16.683 -0.271  0.25 38.10  ? 27  LEU B C   1 
ATOM   3117 C  C   D LEU B 1 27  ? -5.486  -16.683 -0.271  0.25 38.10  ? 27  LEU B C   1 
ATOM   3118 O  O   A LEU B 1 27  ? -4.731  -17.683 0.065   0.25 28.39  ? 27  LEU B O   1 
ATOM   3119 O  O   B LEU B 1 27  ? -4.731  -17.683 0.065   0.25 28.39  ? 27  LEU B O   1 
ATOM   3120 O  O   C LEU B 1 27  ? -4.898  -17.562 0.389   0.25 37.29  ? 27  LEU B O   1 
ATOM   3121 O  O   D LEU B 1 27  ? -4.898  -17.562 0.389   0.25 37.29  ? 27  LEU B O   1 
ATOM   3122 C  CB  A LEU B 1 27  ? -7.886  -16.081 -0.374  0.25 32.47  ? 27  LEU B CB  1 
ATOM   3123 C  CB  B LEU B 1 27  ? -7.886  -16.081 -0.374  0.25 32.47  ? 27  LEU B CB  1 
ATOM   3124 C  CB  C LEU B 1 27  ? -7.750  -15.671 0.178   0.25 41.00  ? 27  LEU B CB  1 
ATOM   3125 C  CB  D LEU B 1 27  ? -7.750  -15.671 0.178   0.25 41.00  ? 27  LEU B CB  1 
ATOM   3126 C  CG  A LEU B 1 27  ? -8.302  -16.147 1.095   0.25 32.90  ? 27  LEU B CG  1 
ATOM   3127 C  CG  B LEU B 1 27  ? -8.302  -16.147 1.095   0.25 32.90  ? 27  LEU B CG  1 
ATOM   3128 C  CG  C LEU B 1 27  ? -8.353  -15.957 1.551   0.25 41.05  ? 27  LEU B CG  1 
ATOM   3129 C  CG  D LEU B 1 27  ? -8.353  -15.957 1.551   0.25 41.05  ? 27  LEU B CG  1 
ATOM   3130 C  CD1 A LEU B 1 27  ? -7.138  -15.800 2.012   0.25 32.69  ? 27  LEU B CD1 1 
ATOM   3131 C  CD1 B LEU B 1 27  ? -7.138  -15.800 2.012   0.25 32.69  ? 27  LEU B CD1 1 
ATOM   3132 C  CD1 C LEU B 1 27  ? -7.321  -15.735 2.648   0.25 40.51  ? 27  LEU B CD1 1 
ATOM   3133 C  CD1 D LEU B 1 27  ? -7.321  -15.735 2.648   0.25 40.51  ? 27  LEU B CD1 1 
ATOM   3134 C  CD2 A LEU B 1 27  ? -9.478  -15.218 1.353   0.25 33.03  ? 27  LEU B CD2 1 
ATOM   3135 C  CD2 B LEU B 1 27  ? -9.478  -15.218 1.353   0.25 33.03  ? 27  LEU B CD2 1 
ATOM   3136 C  CD2 C LEU B 1 27  ? -9.578  -15.083 1.774   0.25 41.46  ? 27  LEU B CD2 1 
ATOM   3137 C  CD2 D LEU B 1 27  ? -9.578  -15.083 1.774   0.25 41.46  ? 27  LEU B CD2 1 
ATOM   3138 N  N   A ASN B 1 28  ? -5.027  -15.543 -0.676  0.25 27.24  ? 28  ASN B N   1 
ATOM   3139 N  N   B ASN B 1 28  ? -5.027  -15.543 -0.676  0.25 27.24  ? 28  ASN B N   1 
ATOM   3140 N  N   C ASN B 1 28  ? -4.880  -15.615 -0.799  0.25 35.90  ? 28  ASN B N   1 
ATOM   3141 N  N   D ASN B 1 28  ? -4.880  -15.615 -0.799  0.25 35.90  ? 28  ASN B N   1 
ATOM   3142 C  CA  A ASN B 1 28  ? -3.605  -15.118 -0.598  0.25 24.93  ? 28  ASN B CA  1 
ATOM   3143 C  CA  B ASN B 1 28  ? -3.605  -15.118 -0.598  0.25 24.93  ? 28  ASN B CA  1 
ATOM   3144 C  CA  C ASN B 1 28  ? -3.427  -15.358 -0.623  0.25 33.12  ? 28  ASN B CA  1 
ATOM   3145 C  CA  D ASN B 1 28  ? -3.427  -15.358 -0.623  0.25 33.12  ? 28  ASN B CA  1 
ATOM   3146 C  C   A ASN B 1 28  ? -3.339  -14.464 0.756   0.25 24.60  ? 28  ASN B C   1 
ATOM   3147 C  C   B ASN B 1 28  ? -3.339  -14.464 0.756   0.25 24.60  ? 28  ASN B C   1 
ATOM   3148 C  C   C ASN B 1 28  ? -3.252  -14.453 0.604   0.25 29.10  ? 28  ASN B C   1 
ATOM   3149 C  C   D ASN B 1 28  ? -3.252  -14.453 0.604   0.25 29.10  ? 28  ASN B C   1 
ATOM   3150 O  O   A ASN B 1 28  ? -4.254  -13.796 1.279   0.25 23.77  ? 28  ASN B O   1 
ATOM   3151 O  O   B ASN B 1 28  ? -4.254  -13.796 1.279   0.25 23.77  ? 28  ASN B O   1 
ATOM   3152 O  O   C ASN B 1 28  ? -4.162  -13.658 0.911   0.25 28.41  ? 28  ASN B O   1 
ATOM   3153 O  O   D ASN B 1 28  ? -4.162  -13.658 0.911   0.25 28.41  ? 28  ASN B O   1 
ATOM   3154 C  CB  A ASN B 1 28  ? -3.256  -14.186 -1.758  0.25 23.83  ? 28  ASN B CB  1 
ATOM   3155 C  CB  B ASN B 1 28  ? -3.256  -14.186 -1.758  0.25 23.83  ? 28  ASN B CB  1 
ATOM   3156 C  CB  C ASN B 1 28  ? -2.758  -14.898 -1.929  0.25 35.09  ? 28  ASN B CB  1 
ATOM   3157 C  CB  D ASN B 1 28  ? -2.758  -14.898 -1.929  0.25 35.09  ? 28  ASN B CB  1 
ATOM   3158 C  CG  A ASN B 1 28  ? -3.617  -14.782 -3.100  0.25 23.36  ? 28  ASN B CG  1 
ATOM   3159 C  CG  B ASN B 1 28  ? -3.617  -14.782 -3.100  0.25 23.36  ? 28  ASN B CG  1 
ATOM   3160 C  CG  C ASN B 1 28  ? -2.288  -13.459 -1.936  0.25 36.66  ? 28  ASN B CG  1 
ATOM   3161 C  CG  D ASN B 1 28  ? -2.288  -13.459 -1.936  0.25 36.66  ? 28  ASN B CG  1 
ATOM   3162 O  OD1 A ASN B 1 28  ? -2.917  -15.658 -3.600  0.25 22.61  ? 28  ASN B OD1 1 
ATOM   3163 O  OD1 B ASN B 1 28  ? -2.917  -15.658 -3.600  0.25 22.61  ? 28  ASN B OD1 1 
ATOM   3164 O  OD1 C ASN B 1 28  ? -1.086  -13.195 -1.946  0.25 36.50  ? 28  ASN B OD1 1 
ATOM   3165 O  OD1 D ASN B 1 28  ? -1.086  -13.195 -1.946  0.25 36.50  ? 28  ASN B OD1 1 
ATOM   3166 N  ND2 A ASN B 1 28  ? -4.701  -14.309 -3.690  0.25 23.18  ? 28  ASN B ND2 1 
ATOM   3167 N  ND2 B ASN B 1 28  ? -4.701  -14.309 -3.690  0.25 23.18  ? 28  ASN B ND2 1 
ATOM   3168 N  ND2 C ASN B 1 28  ? -3.225  -12.523 -1.962  0.25 39.51  ? 28  ASN B ND2 1 
ATOM   3169 N  ND2 D ASN B 1 28  ? -3.225  -12.523 -1.962  0.25 39.51  ? 28  ASN B ND2 1 
ATOM   3170 N  N   . GLY B 1 29  ? -2.139  -14.654 1.309   1.00 25.06  ? 29  GLY B N   1 
ATOM   3171 C  CA  . GLY B 1 29  ? -1.747  -13.925 2.507   1.00 25.38  ? 29  GLY B CA  1 
ATOM   3172 C  C   . GLY B 1 29  ? -0.429  -13.251 2.256   1.00 22.35  ? 29  GLY B C   1 
ATOM   3173 O  O   . GLY B 1 29  ? 0.283   -13.674 1.334   1.00 20.50  ? 29  GLY B O   1 
ATOM   3174 N  N   . LEU B 1 30  ? -0.107  -12.276 3.091   1.00 22.55  ? 30  LEU B N   1 
ATOM   3175 C  CA  . LEU B 1 30  ? 1.185   -11.569 3.031   1.00 23.76  ? 30  LEU B CA  1 
ATOM   3176 C  C   . LEU B 1 30  ? 2.018   -12.041 4.227   1.00 23.87  ? 30  LEU B C   1 
ATOM   3177 O  O   . LEU B 1 30  ? 1.620   -11.831 5.364   1.00 24.03  ? 30  LEU B O   1 
ATOM   3178 C  CB  . LEU B 1 30  ? 0.933   -10.059 3.035   1.00 22.60  ? 30  LEU B CB  1 
ATOM   3179 C  CG  . LEU B 1 30  ? 2.159   -9.198  2.720   1.00 21.89  ? 30  LEU B CG  1 
ATOM   3180 C  CD1 . LEU B 1 30  ? 2.632   -9.389  1.287   1.00 21.53  ? 30  LEU B CD1 1 
ATOM   3181 C  CD2 . LEU B 1 30  ? 1.856   -7.735  3.001   1.00 22.02  ? 30  LEU B CD2 1 
ATOM   3182 N  N   . TRP B 1 31  ? 3.141   -12.687 3.967   1.00 24.56  ? 31  TRP B N   1 
ATOM   3183 C  CA  . TRP B 1 31  ? 4.015   -13.236 5.030   1.00 24.15  ? 31  TRP B CA  1 
ATOM   3184 C  C   . TRP B 1 31  ? 5.176   -12.270 5.302   1.00 23.98  ? 31  TRP B C   1 
ATOM   3185 O  O   . TRP B 1 31  ? 6.081   -12.186 4.508   1.00 24.63  ? 31  TRP B O   1 
ATOM   3186 C  CB  . TRP B 1 31  ? 4.460   -14.625 4.582   1.00 25.67  ? 31  TRP B CB  1 
ATOM   3187 C  CG  . TRP B 1 31  ? 5.332   -15.343 5.561   1.00 28.91  ? 31  TRP B CG  1 
ATOM   3188 C  CD1 . TRP B 1 31  ? 5.446   -15.116 6.903   1.00 32.88  ? 31  TRP B CD1 1 
ATOM   3189 C  CD2 . TRP B 1 31  ? 6.245   -16.404 5.257   1.00 29.52  ? 31  TRP B CD2 1 
ATOM   3190 N  NE1 . TRP B 1 31  ? 6.380   -15.956 7.453   1.00 32.06  ? 31  TRP B NE1 1 
ATOM   3191 C  CE2 . TRP B 1 31  ? 6.874   -16.766 6.467   1.00 32.62  ? 31  TRP B CE2 1 
ATOM   3192 C  CE3 . TRP B 1 31  ? 6.582   -17.081 4.085   1.00 29.08  ? 31  TRP B CE3 1 
ATOM   3193 C  CZ2 . TRP B 1 31  ? 7.825   -17.782 6.535   1.00 33.01  ? 31  TRP B CZ2 1 
ATOM   3194 C  CZ3 . TRP B 1 31  ? 7.523   -18.082 4.158   1.00 33.92  ? 31  TRP B CZ3 1 
ATOM   3195 C  CH2 . TRP B 1 31  ? 8.126   -18.435 5.367   1.00 32.07  ? 31  TRP B CH2 1 
ATOM   3196 N  N   . LEU B 1 32  ? 5.162   -11.588 6.436   1.00 26.63  ? 32  LEU B N   1 
ATOM   3197 C  CA  . LEU B 1 32  ? 6.208   -10.621 6.849   1.00 26.98  ? 32  LEU B CA  1 
ATOM   3198 C  C   . LEU B 1 32  ? 6.607   -10.956 8.278   1.00 27.09  ? 32  LEU B C   1 
ATOM   3199 O  O   . LEU B 1 32  ? 5.697   -11.238 9.076   1.00 28.73  ? 32  LEU B O   1 
ATOM   3200 C  CB  . LEU B 1 32  ? 5.658   -9.193  6.758   1.00 25.92  ? 32  LEU B CB  1 
ATOM   3201 C  CG  . LEU B 1 32  ? 5.215   -8.755  5.365   1.00 25.80  ? 32  LEU B CG  1 
ATOM   3202 C  CD1 . LEU B 1 32  ? 4.465   -7.445  5.436   1.00 25.81  ? 32  LEU B CD1 1 
ATOM   3203 C  CD2 . LEU B 1 32  ? 6.416   -8.652  4.446   1.00 26.28  ? 32  LEU B CD2 1 
ATOM   3204 N  N   . ASP B 1 33  ? 7.916   -10.964 8.550   1.00 30.11  ? 33  ASP B N   1 
ATOM   3205 C  CA  . ASP B 1 33  ? 8.496   -11.535 9.789   1.00 28.32  ? 33  ASP B CA  1 
ATOM   3206 C  C   . ASP B 1 33  ? 7.762   -12.863 10.061  1.00 28.72  ? 33  ASP B C   1 
ATOM   3207 O  O   . ASP B 1 33  ? 7.638   -13.699 9.115   1.00 28.40  ? 33  ASP B O   1 
ATOM   3208 C  CB  . ASP B 1 33  ? 8.426   -10.453 10.867  1.00 29.18  ? 33  ASP B CB  1 
ATOM   3209 C  CG  . ASP B 1 33  ? 9.031   -9.137  10.396  1.00 32.87  ? 33  ASP B CG  1 
ATOM   3210 O  OD1 . ASP B 1 33  ? 10.268  -9.106  10.210  1.00 34.32  ? 33  ASP B OD1 1 
ATOM   3211 O  OD2 . ASP B 1 33  ? 8.262   -8.138  10.245  1.00 35.87  ? 33  ASP B OD2 1 
ATOM   3212 N  N   . ASP B 1 34  ? 7.212   -13.062 11.259  1.00 31.19  ? 34  ASP B N   1 
ATOM   3213 C  CA  . ASP B 1 34  ? 6.517   -14.331 11.615  1.00 30.58  ? 34  ASP B CA  1 
ATOM   3214 C  C   . ASP B 1 34  ? 4.988   -14.141 11.617  1.00 31.70  ? 34  ASP B C   1 
ATOM   3215 O  O   . ASP B 1 34  ? 4.305   -14.867 12.383  1.00 40.56  ? 34  ASP B O   1 
ATOM   3216 C  CB  . ASP B 1 34  ? 7.084   -14.868 12.929  1.00 31.87  ? 34  ASP B CB  1 
ATOM   3217 C  CG  . ASP B 1 34  ? 6.892   -13.940 14.113  1.00 32.21  ? 34  ASP B CG  1 
ATOM   3218 O  OD1 . ASP B 1 34  ? 6.522   -12.784 13.895  1.00 32.62  ? 34  ASP B OD1 1 
ATOM   3219 O  OD2 . ASP B 1 34  ? 7.093   -14.394 15.235  1.00 34.66  ? 34  ASP B OD2 1 
ATOM   3220 N  N   . VAL B 1 35  ? 4.430   -13.250 10.789  1.00 25.51  ? 35  VAL B N   1 
ATOM   3221 C  CA  . VAL B 1 35  ? 2.945   -13.070 10.715  1.00 25.66  ? 35  VAL B CA  1 
ATOM   3222 C  C   . VAL B 1 35  ? 2.491   -13.158 9.259   1.00 26.03  ? 35  VAL B C   1 
ATOM   3223 O  O   . VAL B 1 35  ? 3.145   -12.560 8.374   1.00 24.60  ? 35  VAL B O   1 
ATOM   3224 C  CB  . VAL B 1 35  ? 2.480   -11.740 11.337  1.00 26.77  ? 35  VAL B CB  1 
ATOM   3225 C  CG1 . VAL B 1 35  ? 0.961   -11.589 11.261  1.00 24.73  ? 35  VAL B CG1 1 
ATOM   3226 C  CG2 . VAL B 1 35  ? 2.964   -11.582 12.764  1.00 25.71  ? 35  VAL B CG2 1 
ATOM   3227 N  N   . VAL B 1 36  ? 1.380   -13.856 9.035   1.00 25.68  ? 36  VAL B N   1 
ATOM   3228 C  CA  . VAL B 1 36  ? 0.669   -13.882 7.738   1.00 27.35  ? 36  VAL B CA  1 
ATOM   3229 C  C   . VAL B 1 36  ? -0.584  -13.034 7.894   1.00 28.20  ? 36  VAL B C   1 
ATOM   3230 O  O   . VAL B 1 36  ? -1.327  -13.317 8.837   1.00 25.13  ? 36  VAL B O   1 
ATOM   3231 C  CB  . VAL B 1 36  ? 0.316   -15.302 7.296   1.00 27.64  ? 36  VAL B CB  1 
ATOM   3232 C  CG1 . VAL B 1 36  ? -0.392  -15.255 5.945   1.00 25.56  ? 36  VAL B CG1 1 
ATOM   3233 C  CG2 . VAL B 1 36  ? 1.571   -16.177 7.270   1.00 28.16  ? 36  VAL B CG2 1 
ATOM   3234 N  N   . TYR B 1 37  ? -0.746  -12.037 7.011   1.00 27.58  ? 37  TYR B N   1 
ATOM   3235 C  CA  . TYR B 1 37  ? -1.894  -11.104 6.923   1.00 25.61  ? 37  TYR B CA  1 
ATOM   3236 C  C   . TYR B 1 37  ? -2.792  -11.534 5.767   1.00 24.61  ? 37  TYR B C   1 
ATOM   3237 O  O   . TYR B 1 37  ? -2.261  -11.767 4.667   1.00 25.08  ? 37  TYR B O   1 
ATOM   3238 C  CB  . TYR B 1 37  ? -1.399  -9.672  6.712   1.00 26.44  ? 37  TYR B CB  1 
ATOM   3239 C  CG  . TYR B 1 37  ? -0.442  -9.196  7.768   1.00 24.44  ? 37  TYR B CG  1 
ATOM   3240 C  CD1 . TYR B 1 37  ? 0.908   -9.489  7.682   1.00 28.14  ? 37  TYR B CD1 1 
ATOM   3241 C  CD2 . TYR B 1 37  ? -0.873  -8.478  8.869   1.00 24.27  ? 37  TYR B CD2 1 
ATOM   3242 C  CE1 . TYR B 1 37  ? 1.805   -9.067  8.657   1.00 27.35  ? 37  TYR B CE1 1 
ATOM   3243 C  CE2 . TYR B 1 37  ? 0.007   -8.020  9.846   1.00 24.74  ? 37  TYR B CE2 1 
ATOM   3244 C  CZ  . TYR B 1 37  ? 1.355   -8.317  9.739   1.00 28.38  ? 37  TYR B CZ  1 
ATOM   3245 O  OH  . TYR B 1 37  ? 2.217   -7.902  10.709  1.00 28.82  ? 37  TYR B OH  1 
ATOM   3246 N  N   . CYS B 1 38  ? -4.100  -11.668 6.012   1.00 23.47  ? 38  CYS B N   1 
ATOM   3247 C  CA  . CYS B 1 38  ? -5.103  -12.011 4.964   1.00 24.13  ? 38  CYS B CA  1 
ATOM   3248 C  C   . CYS B 1 38  ? -6.448  -11.420 5.359   1.00 23.10  ? 38  CYS B C   1 
ATOM   3249 O  O   . CYS B 1 38  ? -6.604  -10.947 6.482   1.00 24.22  ? 38  CYS B O   1 
ATOM   3250 C  CB  . CYS B 1 38  ? -5.177  -13.517 4.737   1.00 25.53  ? 38  CYS B CB  1 
ATOM   3251 S  SG  . CYS B 1 38  ? -6.009  -14.447 6.061   1.00 27.24  ? 38  CYS B SG  1 
ATOM   3252 N  N   . PRO B 1 39  ? -7.451  -11.382 4.457   1.00 24.50  ? 39  PRO B N   1 
ATOM   3253 C  CA  . PRO B 1 39  ? -8.783  -10.899 4.825   1.00 24.96  ? 39  PRO B CA  1 
ATOM   3254 C  C   . PRO B 1 39  ? -9.442  -11.811 5.875   1.00 25.28  ? 39  PRO B C   1 
ATOM   3255 O  O   . PRO B 1 39  ? -9.350  -13.016 5.771   1.00 23.32  ? 39  PRO B O   1 
ATOM   3256 C  CB  . PRO B 1 39  ? -9.517  -10.870 3.473   1.00 23.29  ? 39  PRO B CB  1 
ATOM   3257 C  CG  . PRO B 1 39  ? -8.407  -10.766 2.474   1.00 23.70  ? 39  PRO B CG  1 
ATOM   3258 C  CD  . PRO B 1 39  ? -7.373  -11.724 3.031   1.00 24.43  ? 39  PRO B CD  1 
ATOM   3259 N  N   . ARG B 1 40  ? -10.056 -11.202 6.885   1.00 26.26  ? 40  ARG B N   1 
ATOM   3260 C  CA  . ARG B 1 40  ? -10.709 -11.958 7.975   1.00 28.18  ? 40  ARG B CA  1 
ATOM   3261 C  C   . ARG B 1 40  ? -11.838 -12.791 7.365   1.00 28.44  ? 40  ARG B C   1 
ATOM   3262 O  O   . ARG B 1 40  ? -12.146 -13.825 7.944   1.00 32.71  ? 40  ARG B O   1 
ATOM   3263 C  CB  . ARG B 1 40  ? -11.188 -11.038 9.099   1.00 30.26  ? 40  ARG B CB  1 
ATOM   3264 C  CG  . ARG B 1 40  ? -12.367 -10.136 8.761   1.00 31.34  ? 40  ARG B CG  1 
ATOM   3265 C  CD  . ARG B 1 40  ? -12.843 -9.408  10.011  1.00 28.85  ? 40  ARG B CD  1 
ATOM   3266 N  NE  . ARG B 1 40  ? -13.892 -8.481  9.654   1.00 29.30  ? 40  ARG B NE  1 
ATOM   3267 C  CZ  . ARG B 1 40  ? -14.604 -7.754  10.503  1.00 29.49  ? 40  ARG B CZ  1 
ATOM   3268 N  NH1 . ARG B 1 40  ? -14.371 -7.830  11.798  1.00 30.84  ? 40  ARG B NH1 1 
ATOM   3269 N  NH2 . ARG B 1 40  ? -15.571 -6.969  10.056  1.00 29.70  ? 40  ARG B NH2 1 
ATOM   3270 N  N   . HIS B 1 41  ? -12.415 -12.404 6.229   1.00 27.21  ? 41  HIS B N   1 
ATOM   3271 C  CA  . HIS B 1 41  ? -13.548 -13.164 5.645   1.00 29.50  ? 41  HIS B CA  1 
ATOM   3272 C  C   . HIS B 1 41  ? -13.106 -14.558 5.186   1.00 30.10  ? 41  HIS B C   1 
ATOM   3273 O  O   . HIS B 1 41  ? -13.985 -15.318 4.815   1.00 32.83  ? 41  HIS B O   1 
ATOM   3274 C  CB  . HIS B 1 41  ? -14.287 -12.380 4.553   1.00 32.54  ? 41  HIS B CB  1 
ATOM   3275 C  CG  . HIS B 1 41  ? -13.545 -12.217 3.272   1.00 32.69  ? 41  HIS B CG  1 
ATOM   3276 N  ND1 . HIS B 1 41  ? -13.275 -13.275 2.429   1.00 33.92  ? 41  HIS B ND1 1 
ATOM   3277 C  CD2 . HIS B 1 41  ? -13.057 -11.113 2.667   1.00 34.78  ? 41  HIS B CD2 1 
ATOM   3278 C  CE1 . HIS B 1 41  ? -12.619 -12.837 1.375   1.00 35.86  ? 41  HIS B CE1 1 
ATOM   3279 N  NE2 . HIS B 1 41  ? -12.481 -11.513 1.493   1.00 34.83  ? 41  HIS B NE2 1 
ATOM   3280 N  N   . VAL B 1 42  ? -11.833 -14.930 5.289   1.00 32.67  ? 42  VAL B N   1 
ATOM   3281 C  CA  . VAL B 1 42  ? -11.380 -16.326 5.007   1.00 32.37  ? 42  VAL B CA  1 
ATOM   3282 C  C   . VAL B 1 42  ? -12.016 -17.295 6.010   1.00 37.84  ? 42  VAL B C   1 
ATOM   3283 O  O   . VAL B 1 42  ? -12.038 -18.506 5.688   1.00 37.02  ? 42  VAL B O   1 
ATOM   3284 C  CB  . VAL B 1 42  ? -9.852  -16.481 5.029   1.00 29.32  ? 42  VAL B CB  1 
ATOM   3285 C  CG1 . VAL B 1 42  ? -9.269  -16.388 6.419   1.00 28.36  ? 42  VAL B CG1 1 
ATOM   3286 C  CG2 . VAL B 1 42  ? -9.405  -17.773 4.358   1.00 29.88  ? 42  VAL B CG2 1 
ATOM   3287 N  N   . ILE B 1 43  ? -12.467 -16.814 7.179   1.00 41.00  ? 43  ILE B N   1 
ATOM   3288 C  CA  . ILE B 1 43  ? -13.056 -17.701 8.234   1.00 44.78  ? 43  ILE B CA  1 
ATOM   3289 C  C   . ILE B 1 43  ? -14.542 -17.930 7.948   1.00 46.55  ? 43  ILE B C   1 
ATOM   3290 O  O   . ILE B 1 43  ? -15.158 -18.691 8.712   1.00 51.35  ? 43  ILE B O   1 
ATOM   3291 C  CB  . ILE B 1 43  ? -12.842 -17.159 9.663   1.00 38.22  ? 43  ILE B CB  1 
ATOM   3292 C  CG1 . ILE B 1 43  ? -13.751 -15.961 9.953   1.00 34.32  ? 43  ILE B CG1 1 
ATOM   3293 C  CG2 . ILE B 1 43  ? -11.367 -16.884 9.890   1.00 40.57  ? 43  ILE B CG2 1 
ATOM   3294 C  CD1 . ILE B 1 43  ? -13.520 -15.314 11.299  1.00 35.08  ? 43  ILE B CD1 1 
ATOM   3295 N  N   . CYS B 1 44  ? -15.092 -17.302 6.910   1.00 47.04  ? 44  CYS B N   1 
ATOM   3296 C  CA  . CYS B 1 44  ? -16.528 -17.397 6.553   1.00 50.21  ? 44  CYS B CA  1 
ATOM   3297 C  C   . CYS B 1 44  ? -16.790 -18.541 5.572   1.00 56.23  ? 44  CYS B C   1 
ATOM   3298 O  O   . CYS B 1 44  ? -15.967 -18.765 4.670   1.00 58.16  ? 44  CYS B O   1 
ATOM   3299 C  CB  . CYS B 1 44  ? -17.045 -16.085 5.986   1.00 49.31  ? 44  CYS B CB  1 
ATOM   3300 S  SG  . CYS B 1 44  ? -17.250 -14.844 7.289   1.00 56.19  ? 44  CYS B SG  1 
ATOM   3301 N  N   . THR B 1 45  ? -17.896 -19.253 5.815   1.00 63.18  ? 45  THR B N   1 
ATOM   3302 C  CA  . THR B 1 45  ? -18.636 -20.098 4.846   1.00 63.74  ? 45  THR B CA  1 
ATOM   3303 C  C   . THR B 1 45  ? -19.591 -19.159 4.103   1.00 70.16  ? 45  THR B C   1 
ATOM   3304 O  O   . THR B 1 45  ? -19.786 -18.044 4.617   1.00 62.98  ? 45  THR B O   1 
ATOM   3305 C  CB  . THR B 1 45  ? -19.400 -21.213 5.573   1.00 61.53  ? 45  THR B CB  1 
ATOM   3306 O  OG1 . THR B 1 45  ? -20.503 -20.580 6.222   1.00 59.24  ? 45  THR B OG1 1 
ATOM   3307 C  CG2 . THR B 1 45  ? -18.574 -21.966 6.594   1.00 55.23  ? 45  THR B CG2 1 
ATOM   3308 N  N   . SER B 1 46  ? -20.175 -19.584 2.974   1.00 81.05  ? 46  SER B N   1 
ATOM   3309 C  CA  . SER B 1 46  ? -21.120 -18.769 2.154   1.00 84.53  ? 46  SER B CA  1 
ATOM   3310 C  C   . SER B 1 46  ? -22.365 -18.405 2.976   1.00 83.45  ? 46  SER B C   1 
ATOM   3311 O  O   . SER B 1 46  ? -22.927 -17.305 2.749   1.00 91.16  ? 46  SER B O   1 
ATOM   3312 C  CB  . SER B 1 46  ? -21.496 -19.462 0.869   1.00 84.54  ? 46  SER B CB  1 
ATOM   3313 O  OG  . SER B 1 46  ? -20.444 -19.352 -0.078  1.00 89.99  ? 46  SER B OG  1 
ATOM   3314 N  N   . GLU B 1 47  ? -22.764 -19.286 3.898   1.00 75.50  ? 47  GLU B N   1 
ATOM   3315 C  CA  . GLU B 1 47  ? -23.866 -19.051 4.870   1.00 71.45  ? 47  GLU B CA  1 
ATOM   3316 C  C   . GLU B 1 47  ? -23.511 -17.860 5.763   1.00 64.86  ? 47  GLU B C   1 
ATOM   3317 O  O   . GLU B 1 47  ? -24.349 -16.949 5.934   1.00 61.24  ? 47  GLU B O   1 
ATOM   3318 C  CB  . GLU B 1 47  ? -24.058 -20.274 5.763   1.00 78.82  ? 47  GLU B CB  1 
ATOM   3319 C  CG  . GLU B 1 47  ? -24.449 -21.530 5.011   1.00 88.97  ? 47  GLU B CG  1 
ATOM   3320 C  CD  . GLU B 1 47  ? -24.704 -22.725 5.912   1.00 95.59  ? 47  GLU B CD  1 
ATOM   3321 O  OE1 . GLU B 1 47  ? -24.273 -22.679 7.084   1.00 95.86  ? 47  GLU B OE1 1 
ATOM   3322 O  OE2 . GLU B 1 47  ? -25.337 -23.694 5.441   1.00 109.64 ? 47  GLU B OE2 1 
ATOM   3323 N  N   . ASP B 1 48  ? -22.302 -17.901 6.320   1.00 61.77  ? 48  ASP B N   1 
ATOM   3324 C  CA  . ASP B 1 48  ? -21.751 -16.891 7.261   1.00 57.94  ? 48  ASP B CA  1 
ATOM   3325 C  C   . ASP B 1 48  ? -21.749 -15.496 6.620   1.00 55.52  ? 48  ASP B C   1 
ATOM   3326 O  O   . ASP B 1 48  ? -22.061 -14.522 7.353   1.00 47.08  ? 48  ASP B O   1 
ATOM   3327 C  CB  . ASP B 1 48  ? -20.342 -17.294 7.707   1.00 58.44  ? 48  ASP B CB  1 
ATOM   3328 C  CG  . ASP B 1 48  ? -20.327 -18.315 8.832   1.00 60.80  ? 48  ASP B CG  1 
ATOM   3329 O  OD1 . ASP B 1 48  ? -21.109 -18.123 9.797   1.00 57.69  ? 48  ASP B OD1 1 
ATOM   3330 O  OD2 . ASP B 1 48  ? -19.542 -19.296 8.735   1.00 56.81  ? 48  ASP B OD2 1 
ATOM   3331 N  N   . MET B 1 49  ? -21.408 -15.395 5.321   1.00 58.70  ? 49  MET B N   1 
ATOM   3332 C  CA  . MET B 1 49  ? -21.041 -14.106 4.656   1.00 54.10  ? 49  MET B CA  1 
ATOM   3333 C  C   . MET B 1 49  ? -22.258 -13.156 4.605   1.00 52.02  ? 49  MET B C   1 
ATOM   3334 O  O   . MET B 1 49  ? -22.023 -11.932 4.492   1.00 43.09  ? 49  MET B O   1 
ATOM   3335 C  CB  . MET B 1 49  ? -20.434 -14.297 3.255   1.00 53.38  ? 49  MET B CB  1 
ATOM   3336 C  CG  . MET B 1 49  ? -18.872 -14.250 3.204   1.00 56.72  ? 49  MET B CG  1 
ATOM   3337 S  SD  . MET B 1 49  ? -18.071 -12.652 3.670   1.00 55.39  ? 49  MET B SD  1 
ATOM   3338 C  CE  . MET B 1 49  ? -17.452 -12.030 2.102   1.00 56.54  ? 49  MET B CE  1 
ATOM   3339 N  N   . LEU B 1 50  ? -23.496 -13.652 4.765   1.00 48.91  ? 50  LEU B N   1 
ATOM   3340 C  CA  . LEU B 1 50  ? -24.715 -12.790 4.723   1.00 51.79  ? 50  LEU B CA  1 
ATOM   3341 C  C   . LEU B 1 50  ? -24.781 -11.887 5.960   1.00 46.30  ? 50  LEU B C   1 
ATOM   3342 O  O   . LEU B 1 50  ? -25.107 -10.705 5.803   1.00 48.27  ? 50  LEU B O   1 
ATOM   3343 C  CB  . LEU B 1 50  ? -25.980 -13.645 4.560   1.00 57.42  ? 50  LEU B CB  1 
ATOM   3344 C  CG  . LEU B 1 50  ? -26.341 -13.977 3.109   1.00 66.06  ? 50  LEU B CG  1 
ATOM   3345 C  CD1 . LEU B 1 50  ? -25.284 -14.878 2.469   1.00 68.75  ? 50  LEU B CD1 1 
ATOM   3346 C  CD2 . LEU B 1 50  ? -27.730 -14.607 3.007   1.00 66.61  ? 50  LEU B CD2 1 
ATOM   3347 N  N   . ASN B 1 51  ? -24.465 -12.401 7.143   1.00 49.93  ? 51  ASN B N   1 
ATOM   3348 C  CA  . ASN B 1 51  ? -24.353 -11.564 8.365   1.00 52.71  ? 51  ASN B CA  1 
ATOM   3349 C  C   . ASN B 1 51  ? -23.353 -12.208 9.319   1.00 48.65  ? 51  ASN B C   1 
ATOM   3350 O  O   . ASN B 1 51  ? -23.734 -12.840 10.299  1.00 49.30  ? 51  ASN B O   1 
ATOM   3351 C  CB  . ASN B 1 51  ? -25.717 -11.287 9.003   1.00 60.00  ? 51  ASN B CB  1 
ATOM   3352 C  CG  . ASN B 1 51  ? -25.691 -10.059 9.887   1.00 61.77  ? 51  ASN B CG  1 
ATOM   3353 O  OD1 . ASN B 1 51  ? -25.368 -10.157 11.067  1.00 79.53  ? 51  ASN B OD1 1 
ATOM   3354 N  ND2 . ASN B 1 51  ? -26.010 -8.905  9.324   1.00 58.44  ? 51  ASN B ND2 1 
ATOM   3355 N  N   . PRO B 1 52  ? -22.035 -12.048 9.060   1.00 47.37  ? 52  PRO B N   1 
ATOM   3356 C  CA  . PRO B 1 52  ? -21.004 -12.674 9.881   1.00 42.48  ? 52  PRO B CA  1 
ATOM   3357 C  C   . PRO B 1 52  ? -20.838 -11.964 11.221  1.00 38.80  ? 52  PRO B C   1 
ATOM   3358 O  O   . PRO B 1 52  ? -20.886 -10.759 11.254  1.00 40.50  ? 52  PRO B O   1 
ATOM   3359 C  CB  . PRO B 1 52  ? -19.726 -12.493 9.055   1.00 47.72  ? 52  PRO B CB  1 
ATOM   3360 C  CG  . PRO B 1 52  ? -19.981 -11.216 8.268   1.00 46.83  ? 52  PRO B CG  1 
ATOM   3361 C  CD  . PRO B 1 52  ? -21.465 -11.238 7.967   1.00 48.45  ? 52  PRO B CD  1 
ATOM   3362 N  N   . ASN B 1 53  ? -20.657 -12.741 12.281  1.00 39.49  ? 53  ASN B N   1 
ATOM   3363 C  CA  . ASN B 1 53  ? -20.197 -12.256 13.602  1.00 40.94  ? 53  ASN B CA  1 
ATOM   3364 C  C   . ASN B 1 53  ? -18.760 -12.750 13.735  1.00 43.34  ? 53  ASN B C   1 
ATOM   3365 O  O   . ASN B 1 53  ? -18.540 -13.953 14.049  1.00 38.47  ? 53  ASN B O   1 
ATOM   3366 C  CB  . ASN B 1 53  ? -21.124 -12.702 14.735  1.00 45.87  ? 53  ASN B CB  1 
ATOM   3367 C  CG  . ASN B 1 53  ? -20.664 -12.245 16.105  1.00 48.67  ? 53  ASN B CG  1 
ATOM   3368 O  OD1 . ASN B 1 53  ? -19.589 -11.669 16.252  1.00 50.23  ? 53  ASN B OD1 1 
ATOM   3369 N  ND2 . ASN B 1 53  ? -21.463 -12.523 17.123  1.00 55.29  ? 53  ASN B ND2 1 
ATOM   3370 N  N   . TYR B 1 54  ? -17.820 -11.881 13.371  1.00 43.96  ? 54  TYR B N   1 
ATOM   3371 C  CA  . TYR B 1 54  ? -16.396 -12.252 13.193  1.00 41.94  ? 54  TYR B CA  1 
ATOM   3372 C  C   . TYR B 1 54  ? -15.836 -12.609 14.567  1.00 41.55  ? 54  TYR B C   1 
ATOM   3373 O  O   . TYR B 1 54  ? -15.135 -13.644 14.642  1.00 42.67  ? 54  TYR B O   1 
ATOM   3374 C  CB  . TYR B 1 54  ? -15.628 -11.143 12.465  1.00 39.04  ? 54  TYR B CB  1 
ATOM   3375 C  CG  . TYR B 1 54  ? -15.866 -11.108 10.978  1.00 31.99  ? 54  TYR B CG  1 
ATOM   3376 C  CD1 . TYR B 1 54  ? -15.287 -12.056 10.155  1.00 29.91  ? 54  TYR B CD1 1 
ATOM   3377 C  CD2 . TYR B 1 54  ? -16.697 -10.162 10.402  1.00 31.06  ? 54  TYR B CD2 1 
ATOM   3378 C  CE1 . TYR B 1 54  ? -15.523 -12.062 8.789   1.00 31.19  ? 54  TYR B CE1 1 
ATOM   3379 C  CE2 . TYR B 1 54  ? -16.931 -10.139 9.035   1.00 30.06  ? 54  TYR B CE2 1 
ATOM   3380 C  CZ  . TYR B 1 54  ? -16.337 -11.093 8.218   1.00 31.16  ? 54  TYR B CZ  1 
ATOM   3381 O  OH  . TYR B 1 54  ? -16.532 -11.095 6.857   1.00 29.25  ? 54  TYR B OH  1 
ATOM   3382 N  N   . GLU B 1 55  ? -16.180 -11.806 15.588  1.00 47.53  ? 55  GLU B N   1 
ATOM   3383 C  CA  . GLU B 1 55  ? -15.863 -12.054 17.025  1.00 51.14  ? 55  GLU B CA  1 
ATOM   3384 C  C   . GLU B 1 55  ? -16.114 -13.532 17.318  1.00 50.87  ? 55  GLU B C   1 
ATOM   3385 O  O   . GLU B 1 55  ? -15.123 -14.264 17.576  1.00 43.76  ? 55  GLU B O   1 
ATOM   3386 C  CB  . GLU B 1 55  ? -16.754 -11.239 17.972  1.00 55.80  ? 55  GLU B CB  1 
ATOM   3387 C  CG  . GLU B 1 55  ? -16.626 -9.737  17.818  1.00 58.46  ? 55  GLU B CG  1 
ATOM   3388 C  CD  . GLU B 1 55  ? -16.947 -8.978  19.090  1.00 57.51  ? 55  GLU B CD  1 
ATOM   3389 O  OE1 . GLU B 1 55  ? -18.088 -9.094  19.592  1.00 57.51  ? 55  GLU B OE1 1 
ATOM   3390 O  OE2 . GLU B 1 55  ? -16.043 -8.288  19.586  1.00 61.87  ? 55  GLU B OE2 1 
ATOM   3391 N  N   . ASP B 1 56  ? -17.390 -13.933 17.181  1.00 51.47  ? 56  ASP B N   1 
ATOM   3392 C  CA  . ASP B 1 56  ? -17.916 -15.288 17.485  1.00 49.58  ? 56  ASP B CA  1 
ATOM   3393 C  C   . ASP B 1 56  ? -17.253 -16.319 16.570  1.00 46.40  ? 56  ASP B C   1 
ATOM   3394 O  O   . ASP B 1 56  ? -16.636 -17.262 17.098  1.00 49.44  ? 56  ASP B O   1 
ATOM   3395 C  CB  . ASP B 1 56  ? -19.441 -15.357 17.364  1.00 51.92  ? 56  ASP B CB  1 
ATOM   3396 C  CG  . ASP B 1 56  ? -19.996 -16.596 18.046  1.00 51.19  ? 56  ASP B CG  1 
ATOM   3397 O  OD1 . ASP B 1 56  ? -19.616 -16.822 19.214  1.00 54.17  ? 56  ASP B OD1 1 
ATOM   3398 O  OD2 . ASP B 1 56  ? -20.747 -17.358 17.393  1.00 49.64  ? 56  ASP B OD2 1 
ATOM   3399 N  N   . LEU B 1 57  ? -17.354 -16.152 15.253  1.00 45.61  ? 57  LEU B N   1 
ATOM   3400 C  CA  . LEU B 1 57  ? -16.746 -17.095 14.276  1.00 47.92  ? 57  LEU B CA  1 
ATOM   3401 C  C   . LEU B 1 57  ? -15.275 -17.379 14.634  1.00 50.85  ? 57  LEU B C   1 
ATOM   3402 O  O   . LEU B 1 57  ? -14.828 -18.503 14.347  1.00 52.50  ? 57  LEU B O   1 
ATOM   3403 C  CB  . LEU B 1 57  ? -16.847 -16.513 12.862  1.00 52.29  ? 57  LEU B CB  1 
ATOM   3404 C  CG  . LEU B 1 57  ? -18.190 -16.688 12.161  1.00 52.89  ? 57  LEU B CG  1 
ATOM   3405 C  CD1 . LEU B 1 57  ? -18.352 -15.664 11.051  1.00 53.39  ? 57  LEU B CD1 1 
ATOM   3406 C  CD2 . LEU B 1 57  ? -18.324 -18.104 11.613  1.00 53.47  ? 57  LEU B CD2 1 
ATOM   3407 N  N   . LEU B 1 58  ? -14.526 -16.413 15.194  1.00 52.08  ? 58  LEU B N   1 
ATOM   3408 C  CA  . LEU B 1 58  ? -13.049 -16.553 15.366  1.00 55.09  ? 58  LEU B CA  1 
ATOM   3409 C  C   . LEU B 1 58  ? -12.703 -17.207 16.718  1.00 56.11  ? 58  LEU B C   1 
ATOM   3410 O  O   . LEU B 1 58  ? -11.736 -18.016 16.750  1.00 50.21  ? 58  LEU B O   1 
ATOM   3411 C  CB  . LEU B 1 58  ? -12.360 -15.193 15.210  1.00 53.95  ? 58  LEU B CB  1 
ATOM   3412 C  CG  . LEU B 1 58  ? -10.832 -15.224 15.351  1.00 55.21  ? 58  LEU B CG  1 
ATOM   3413 C  CD1 . LEU B 1 58  ? -10.177 -16.037 14.235  1.00 56.66  ? 58  LEU B CD1 1 
ATOM   3414 C  CD2 . LEU B 1 58  ? -10.258 -13.821 15.400  1.00 54.55  ? 58  LEU B CD2 1 
ATOM   3415 N  N   . ILE B 1 59  ? -13.425 -16.878 17.801  1.00 60.84  ? 59  ILE B N   1 
ATOM   3416 C  CA  . ILE B 1 59  ? -13.234 -17.562 19.122  1.00 64.48  ? 59  ILE B CA  1 
ATOM   3417 C  C   . ILE B 1 59  ? -13.588 -19.044 18.948  1.00 58.99  ? 59  ILE B C   1 
ATOM   3418 O  O   . ILE B 1 59  ? -12.992 -19.853 19.643  1.00 58.79  ? 59  ILE B O   1 
ATOM   3419 C  CB  . ILE B 1 59  ? -14.023 -16.923 20.290  1.00 67.79  ? 59  ILE B CB  1 
ATOM   3420 C  CG1 . ILE B 1 59  ? -15.538 -16.950 20.067  1.00 70.79  ? 59  ILE B CG1 1 
ATOM   3421 C  CG2 . ILE B 1 59  ? -13.527 -15.517 20.597  1.00 65.56  ? 59  ILE B CG2 1 
ATOM   3422 C  CD1 . ILE B 1 59  ? -16.338 -17.187 21.333  1.00 74.55  ? 59  ILE B CD1 1 
ATOM   3423 N  N   . ARG B 1 60  ? -14.507 -19.372 18.034  1.00 62.51  ? 60  ARG B N   1 
ATOM   3424 C  CA  . ARG B 1 60  ? -14.880 -20.769 17.676  1.00 64.43  ? 60  ARG B CA  1 
ATOM   3425 C  C   . ARG B 1 60  ? -13.742 -21.428 16.892  1.00 57.22  ? 60  ARG B C   1 
ATOM   3426 O  O   . ARG B 1 60  ? -13.755 -22.649 16.751  1.00 50.62  ? 60  ARG B O   1 
ATOM   3427 C  CB  . ARG B 1 60  ? -16.140 -20.805 16.803  1.00 68.55  ? 60  ARG B CB  1 
ATOM   3428 C  CG  . ARG B 1 60  ? -17.439 -20.487 17.526  1.00 71.32  ? 60  ARG B CG  1 
ATOM   3429 C  CD  . ARG B 1 60  ? -18.566 -20.467 16.514  1.00 74.92  ? 60  ARG B CD  1 
ATOM   3430 N  NE  . ARG B 1 60  ? -19.877 -20.461 17.141  1.00 80.99  ? 60  ARG B NE  1 
ATOM   3431 C  CZ  . ARG B 1 60  ? -21.025 -20.672 16.495  1.00 88.30  ? 60  ARG B CZ  1 
ATOM   3432 N  NH1 . ARG B 1 60  ? -21.033 -20.902 15.189  1.00 88.87  ? 60  ARG B NH1 1 
ATOM   3433 N  NH2 . ARG B 1 60  ? -22.168 -20.640 17.160  1.00 84.13  ? 60  ARG B NH2 1 
ATOM   3434 N  N   . LYS B 1 61  ? -12.847 -20.625 16.320  1.00 60.64  ? 61  LYS B N   1 
ATOM   3435 C  CA  . LYS B 1 61  ? -11.724 -21.105 15.480  1.00 58.30  ? 61  LYS B CA  1 
ATOM   3436 C  C   . LYS B 1 61  ? -10.502 -21.292 16.371  1.00 55.14  ? 61  LYS B C   1 
ATOM   3437 O  O   . LYS B 1 61  ? -10.376 -20.572 17.391  1.00 55.40  ? 61  LYS B O   1 
ATOM   3438 C  CB  . LYS B 1 61  ? -11.385 -20.115 14.357  1.00 58.91  ? 61  LYS B CB  1 
ATOM   3439 C  CG  . LYS B 1 61  ? -12.384 -20.056 13.211  1.00 57.16  ? 61  LYS B CG  1 
ATOM   3440 C  CD  . LYS B 1 61  ? -12.209 -21.153 12.197  1.00 54.93  ? 61  LYS B CD  1 
ATOM   3441 C  CE  . LYS B 1 61  ? -13.445 -21.334 11.338  1.00 56.69  ? 61  LYS B CE  1 
ATOM   3442 N  NZ  . LYS B 1 61  ? -13.298 -22.494 10.428  1.00 57.65  ? 61  LYS B NZ  1 
ATOM   3443 N  N   . SER B 1 62  ? -9.610  -22.180 15.949  1.00 51.33  ? 62  SER B N   1 
ATOM   3444 C  CA  . SER B 1 62  ? -8.285  -22.359 16.576  1.00 55.73  ? 62  SER B CA  1 
ATOM   3445 C  C   . SER B 1 62  ? -7.195  -22.411 15.491  1.00 49.01  ? 62  SER B C   1 
ATOM   3446 O  O   . SER B 1 62  ? -7.531  -22.630 14.318  1.00 44.32  ? 62  SER B O   1 
ATOM   3447 C  CB  . SER B 1 62  ? -8.304  -23.584 17.442  1.00 60.37  ? 62  SER B CB  1 
ATOM   3448 O  OG  . SER B 1 62  ? -8.002  -24.718 16.653  1.00 71.44  ? 62  SER B OG  1 
ATOM   3449 N  N   . ASN B 1 63  ? -5.939  -22.210 15.902  1.00 49.37  ? 63  ASN B N   1 
ATOM   3450 C  CA  . ASN B 1 63  ? -4.699  -22.291 15.078  1.00 47.55  ? 63  ASN B CA  1 
ATOM   3451 C  C   . ASN B 1 63  ? -4.820  -23.357 13.981  1.00 50.34  ? 63  ASN B C   1 
ATOM   3452 O  O   . ASN B 1 63  ? -4.554  -23.030 12.811  1.00 51.20  ? 63  ASN B O   1 
ATOM   3453 C  CB  . ASN B 1 63  ? -3.474  -22.580 15.945  1.00 40.58  ? 63  ASN B CB  1 
ATOM   3454 C  CG  . ASN B 1 63  ? -3.074  -21.400 16.800  1.00 42.91  ? 63  ASN B CG  1 
ATOM   3455 O  OD1 . ASN B 1 63  ? -3.355  -20.248 16.460  1.00 42.31  ? 63  ASN B OD1 1 
ATOM   3456 N  ND2 . ASN B 1 63  ? -2.392  -21.667 17.901  1.00 39.61  ? 63  ASN B ND2 1 
ATOM   3457 N  N   . HIS B 1 64  ? -5.198  -24.581 14.343  1.00 55.60  ? 64  HIS B N   1 
ATOM   3458 C  CA  . HIS B 1 64  ? -5.178  -25.775 13.447  1.00 58.27  ? 64  HIS B CA  1 
ATOM   3459 C  C   . HIS B 1 64  ? -6.207  -25.634 12.313  1.00 54.25  ? 64  HIS B C   1 
ATOM   3460 O  O   . HIS B 1 64  ? -6.051  -26.336 11.301  1.00 52.66  ? 64  HIS B O   1 
ATOM   3461 C  CB  . HIS B 1 64  ? -5.371  -27.061 14.267  1.00 67.46  ? 64  HIS B CB  1 
ATOM   3462 C  CG  . HIS B 1 64  ? -6.496  -27.011 15.257  1.00 74.07  ? 64  HIS B CG  1 
ATOM   3463 N  ND1 . HIS B 1 64  ? -6.272  -26.883 16.624  1.00 75.27  ? 64  HIS B ND1 1 
ATOM   3464 C  CD2 . HIS B 1 64  ? -7.842  -27.073 15.095  1.00 74.77  ? 64  HIS B CD2 1 
ATOM   3465 C  CE1 . HIS B 1 64  ? -7.432  -26.878 17.260  1.00 73.76  ? 64  HIS B CE1 1 
ATOM   3466 N  NE2 . HIS B 1 64  ? -8.413  -26.988 16.342  1.00 71.82  ? 64  HIS B NE2 1 
ATOM   3467 N  N   . ASN B 1 65  ? -7.198  -24.745 12.453  1.00 50.55  ? 65  ASN B N   1 
ATOM   3468 C  CA  . ASN B 1 65  ? -8.210  -24.452 11.396  1.00 51.02  ? 65  ASN B CA  1 
ATOM   3469 C  C   . ASN B 1 65  ? -7.604  -23.657 10.235  1.00 48.05  ? 65  ASN B C   1 
ATOM   3470 O  O   . ASN B 1 65  ? -8.383  -23.327 9.314   1.00 45.58  ? 65  ASN B O   1 
ATOM   3471 C  CB  . ASN B 1 65  ? -9.379  -23.616 11.925  1.00 54.74  ? 65  ASN B CB  1 
ATOM   3472 C  CG  . ASN B 1 65  ? -10.209 -24.358 12.947  1.00 59.11  ? 65  ASN B CG  1 
ATOM   3473 O  OD1 . ASN B 1 65  ? -10.374 -23.916 14.089  1.00 56.81  ? 65  ASN B OD1 1 
ATOM   3474 N  ND2 . ASN B 1 65  ? -10.703 -25.510 12.540  1.00 56.44  ? 65  ASN B ND2 1 
ATOM   3475 N  N   . PHE B 1 66  ? -6.318  -23.289 10.307  1.00 43.89  ? 66  PHE B N   1 
ATOM   3476 C  CA  . PHE B 1 66  ? -5.623  -22.441 9.298   1.00 45.32  ? 66  PHE B CA  1 
ATOM   3477 C  C   . PHE B 1 66  ? -4.450  -23.216 8.687   1.00 41.66  ? 66  PHE B C   1 
ATOM   3478 O  O   . PHE B 1 66  ? -3.562  -23.640 9.429   1.00 48.13  ? 66  PHE B O   1 
ATOM   3479 C  CB  . PHE B 1 66  ? -5.172  -21.122 9.929   1.00 42.82  ? 66  PHE B CB  1 
ATOM   3480 C  CG  . PHE B 1 66  ? -6.303  -20.244 10.402  1.00 40.02  ? 66  PHE B CG  1 
ATOM   3481 C  CD1 . PHE B 1 66  ? -7.130  -19.600 9.500   1.00 36.69  ? 66  PHE B CD1 1 
ATOM   3482 C  CD2 . PHE B 1 66  ? -6.567  -20.105 11.755  1.00 39.44  ? 66  PHE B CD2 1 
ATOM   3483 C  CE1 . PHE B 1 66  ? -8.173  -18.809 9.949   1.00 39.18  ? 66  PHE B CE1 1 
ATOM   3484 C  CE2 . PHE B 1 66  ? -7.614  -19.316 12.203  1.00 38.42  ? 66  PHE B CE2 1 
ATOM   3485 C  CZ  . PHE B 1 66  ? -8.418  -18.672 11.300  1.00 39.23  ? 66  PHE B CZ  1 
ATOM   3486 N  N   . LEU B 1 67  ? -4.489  -23.381 7.365   1.00 44.44  ? 67  LEU B N   1 
ATOM   3487 C  CA  . LEU B 1 67  ? -3.467  -24.041 6.514   1.00 49.79  ? 67  LEU B CA  1 
ATOM   3488 C  C   . LEU B 1 67  ? -2.708  -22.969 5.718   1.00 50.35  ? 67  LEU B C   1 
ATOM   3489 O  O   . LEU B 1 67  ? -3.212  -22.493 4.670   1.00 49.01  ? 67  LEU B O   1 
ATOM   3490 C  CB  . LEU B 1 67  ? -4.170  -25.015 5.564   1.00 54.11  ? 67  LEU B CB  1 
ATOM   3491 C  CG  . LEU B 1 67  ? -4.687  -26.303 6.198   1.00 60.15  ? 67  LEU B CG  1 
ATOM   3492 C  CD1 . LEU B 1 67  ? -5.727  -26.980 5.305   1.00 57.71  ? 67  LEU B CD1 1 
ATOM   3493 C  CD2 . LEU B 1 67  ? -3.525  -27.243 6.506   1.00 59.98  ? 67  LEU B CD2 1 
ATOM   3494 N  N   . VAL B 1 68  ? -1.529  -22.602 6.191   1.00 46.85  ? 68  VAL B N   1 
ATOM   3495 C  CA  . VAL B 1 68  ? -0.662  -21.622 5.491   1.00 45.34  ? 68  VAL B CA  1 
ATOM   3496 C  C   . VAL B 1 68  ? 0.403   -22.391 4.715   1.00 45.70  ? 68  VAL B C   1 
ATOM   3497 O  O   . VAL B 1 68  ? 1.106   -23.205 5.320   1.00 41.76  ? 68  VAL B O   1 
ATOM   3498 C  CB  . VAL B 1 68  ? -0.059  -20.616 6.477   1.00 42.99  ? 68  VAL B CB  1 
ATOM   3499 C  CG1 . VAL B 1 68  ? 0.734   -19.544 5.746   1.00 43.92  ? 68  VAL B CG1 1 
ATOM   3500 C  CG2 . VAL B 1 68  ? -1.147  -20.007 7.341   1.00 43.10  ? 68  VAL B CG2 1 
ATOM   3501 N  N   . GLN B 1 69  ? 0.513   -22.096 3.419   1.00 49.52  ? 69  GLN B N   1 
ATOM   3502 C  CA  . GLN B 1 69  ? 1.451   -22.754 2.478   1.00 50.84  ? 69  GLN B CA  1 
ATOM   3503 C  C   . GLN B 1 69  ? 2.285   -21.689 1.745   1.00 43.96  ? 69  GLN B C   1 
ATOM   3504 O  O   . GLN B 1 69  ? 1.695   -20.816 1.094   1.00 38.38  ? 69  GLN B O   1 
ATOM   3505 C  CB  . GLN B 1 69  ? 0.645   -23.646 1.536   1.00 56.12  ? 69  GLN B CB  1 
ATOM   3506 C  CG  . GLN B 1 69  ? 1.478   -24.791 0.984   1.00 66.83  ? 69  GLN B CG  1 
ATOM   3507 C  CD  . GLN B 1 69  ? 0.670   -25.866 0.294   1.00 75.93  ? 69  GLN B CD  1 
ATOM   3508 O  OE1 . GLN B 1 69  ? -0.496  -26.108 0.607   1.00 72.47  ? 69  GLN B OE1 1 
ATOM   3509 N  NE2 . GLN B 1 69  ? 1.303   -26.539 -0.657  1.00 83.18  ? 69  GLN B NE2 1 
ATOM   3510 N  N   . ALA B 1 70  ? 3.606   -21.741 1.914   1.00 38.34  ? 70  ALA B N   1 
ATOM   3511 C  CA  . ALA B 1 70  ? 4.619   -20.966 1.168   1.00 40.27  ? 70  ALA B CA  1 
ATOM   3512 C  C   . ALA B 1 70  ? 5.242   -21.876 0.100   1.00 49.45  ? 70  ALA B C   1 
ATOM   3513 O  O   . ALA B 1 70  ? 6.152   -22.686 0.443   1.00 51.46  ? 70  ALA B O   1 
ATOM   3514 C  CB  . ALA B 1 70  ? 5.653   -20.425 2.118   1.00 37.30  ? 70  ALA B CB  1 
ATOM   3515 N  N   . GLY B 1 71  ? 4.772   -21.750 -1.148  1.00 56.81  ? 71  GLY B N   1 
ATOM   3516 C  CA  . GLY B 1 71  ? 5.044   -22.691 -2.255  1.00 57.13  ? 71  GLY B CA  1 
ATOM   3517 C  C   . GLY B 1 71  ? 4.690   -24.125 -1.874  1.00 64.62  ? 71  GLY B C   1 
ATOM   3518 O  O   . GLY B 1 71  ? 3.480   -24.479 -1.892  1.00 58.40  ? 71  GLY B O   1 
ATOM   3519 N  N   . ASN B 1 72  ? 5.703   -24.921 -1.514  1.00 72.39  ? 72  ASN B N   1 
ATOM   3520 C  CA  . ASN B 1 72  ? 5.578   -26.384 -1.269  1.00 81.47  ? 72  ASN B CA  1 
ATOM   3521 C  C   . ASN B 1 72  ? 5.902   -26.707 0.199   1.00 79.82  ? 72  ASN B C   1 
ATOM   3522 O  O   . ASN B 1 72  ? 6.163   -27.888 0.489   1.00 91.64  ? 72  ASN B O   1 
ATOM   3523 C  CB  . ASN B 1 72  ? 6.475   -27.166 -2.236  1.00 89.97  ? 72  ASN B CB  1 
ATOM   3524 C  CG  . ASN B 1 72  ? 5.764   -28.332 -2.892  1.00 95.77  ? 72  ASN B CG  1 
ATOM   3525 O  OD1 . ASN B 1 72  ? 4.621   -28.203 -3.329  1.00 98.88  ? 72  ASN B OD1 1 
ATOM   3526 N  ND2 . ASN B 1 72  ? 6.440   -29.467 -2.983  1.00 96.03  ? 72  ASN B ND2 1 
ATOM   3527 N  N   . VAL B 1 73  ? 5.865   -25.705 1.083   1.00 68.34  ? 73  VAL B N   1 
ATOM   3528 C  CA  . VAL B 1 73  ? 6.247   -25.798 2.525   1.00 62.81  ? 73  VAL B CA  1 
ATOM   3529 C  C   . VAL B 1 73  ? 5.031   -25.383 3.355   1.00 58.59  ? 73  VAL B C   1 
ATOM   3530 O  O   . VAL B 1 73  ? 4.526   -24.264 3.138   1.00 51.94  ? 73  VAL B O   1 
ATOM   3531 C  CB  . VAL B 1 73  ? 7.462   -24.899 2.833   1.00 62.12  ? 73  VAL B CB  1 
ATOM   3532 C  CG1 . VAL B 1 73  ? 7.725   -24.770 4.329   1.00 59.70  ? 73  VAL B CG1 1 
ATOM   3533 C  CG2 . VAL B 1 73  ? 8.707   -25.372 2.093   1.00 58.98  ? 73  VAL B CG2 1 
ATOM   3534 N  N   . GLN B 1 74  ? 4.560   -26.252 4.248   1.00 53.30  ? 74  GLN B N   1 
ATOM   3535 C  CA  . GLN B 1 74  ? 3.500   -25.898 5.221   1.00 54.49  ? 74  GLN B CA  1 
ATOM   3536 C  C   . GLN B 1 74  ? 4.152   -24.998 6.267   1.00 50.62  ? 74  GLN B C   1 
ATOM   3537 O  O   . GLN B 1 74  ? 5.252   -25.331 6.703   1.00 55.64  ? 74  GLN B O   1 
ATOM   3538 C  CB  . GLN B 1 74  ? 2.858   -27.143 5.830   1.00 61.70  ? 74  GLN B CB  1 
ATOM   3539 C  CG  . GLN B 1 74  ? 1.945   -27.892 4.866   1.00 71.89  ? 74  GLN B CG  1 
ATOM   3540 C  CD  . GLN B 1 74  ? 0.712   -27.097 4.502   1.00 86.59  ? 74  GLN B CD  1 
ATOM   3541 O  OE1 . GLN B 1 74  ? 0.511   -26.728 3.346   1.00 102.25 ? 74  GLN B OE1 1 
ATOM   3542 N  NE2 . GLN B 1 74  ? -0.124  -26.810 5.491   1.00 92.06  ? 74  GLN B NE2 1 
ATOM   3543 N  N   . LEU B 1 75  ? 3.564   -23.837 6.546   1.00 51.80  ? 75  LEU B N   1 
ATOM   3544 C  CA  . LEU B 1 75  ? 3.876   -23.031 7.755   1.00 50.62  ? 75  LEU B CA  1 
ATOM   3545 C  C   . LEU B 1 75  ? 2.919   -23.506 8.852   1.00 50.40  ? 75  LEU B C   1 
ATOM   3546 O  O   . LEU B 1 75  ? 1.725   -23.758 8.517   1.00 49.58  ? 75  LEU B O   1 
ATOM   3547 C  CB  . LEU B 1 75  ? 3.689   -21.535 7.469   1.00 50.69  ? 75  LEU B CB  1 
ATOM   3548 C  CG  . LEU B 1 75  ? 4.561   -20.936 6.372   1.00 50.08  ? 75  LEU B CG  1 
ATOM   3549 C  CD1 . LEU B 1 75  ? 4.384   -19.424 6.307   1.00 48.28  ? 75  LEU B CD1 1 
ATOM   3550 C  CD2 . LEU B 1 75  ? 6.023   -21.270 6.600   1.00 52.38  ? 75  LEU B CD2 1 
ATOM   3551 N  N   . ARG B 1 76  ? 3.433   -23.655 10.079  1.00 47.03  ? 76  ARG B N   1 
ATOM   3552 C  CA  . ARG B 1 76  ? 2.650   -24.001 11.293  1.00 48.02  ? 76  ARG B CA  1 
ATOM   3553 C  C   . ARG B 1 76  ? 2.140   -22.693 11.916  1.00 41.61  ? 76  ARG B C   1 
ATOM   3554 O  O   . ARG B 1 76  ? 2.982   -21.817 12.276  1.00 36.22  ? 76  ARG B O   1 
ATOM   3555 C  CB  . ARG B 1 76  ? 3.520   -24.813 12.265  1.00 56.90  ? 76  ARG B CB  1 
ATOM   3556 C  CG  . ARG B 1 76  ? 2.842   -25.193 13.577  1.00 65.26  ? 76  ARG B CG  1 
ATOM   3557 C  CD  . ARG B 1 76  ? 3.680   -26.062 14.505  1.00 71.55  ? 76  ARG B CD  1 
ATOM   3558 N  NE  . ARG B 1 76  ? 4.145   -27.301 13.873  1.00 82.95  ? 76  ARG B NE  1 
ATOM   3559 C  CZ  . ARG B 1 76  ? 3.565   -28.507 13.969  1.00 86.52  ? 76  ARG B CZ  1 
ATOM   3560 N  NH1 . ARG B 1 76  ? 2.461   -28.685 14.680  1.00 90.81  ? 76  ARG B NH1 1 
ATOM   3561 N  NH2 . ARG B 1 76  ? 4.103   -29.545 13.350  1.00 81.86  ? 76  ARG B NH2 1 
ATOM   3562 N  N   . VAL B 1 77  ? 0.819   -22.560 12.043  1.00 37.04  ? 77  VAL B N   1 
ATOM   3563 C  CA  . VAL B 1 77  ? 0.161   -21.403 12.716  1.00 37.16  ? 77  VAL B CA  1 
ATOM   3564 C  C   . VAL B 1 77  ? 0.177   -21.671 14.221  1.00 37.08  ? 77  VAL B C   1 
ATOM   3565 O  O   . VAL B 1 77  ? -0.388  -22.687 14.617  1.00 39.90  ? 77  VAL B O   1 
ATOM   3566 C  CB  . VAL B 1 77  ? -1.267  -21.169 12.192  1.00 38.03  ? 77  VAL B CB  1 
ATOM   3567 C  CG1 . VAL B 1 77  ? -1.977  -20.028 12.912  1.00 42.77  ? 77  VAL B CG1 1 
ATOM   3568 C  CG2 . VAL B 1 77  ? -1.273  -20.923 10.700  1.00 41.69  ? 77  VAL B CG2 1 
ATOM   3569 N  N   . ILE B 1 78  ? 0.773   -20.761 15.000  1.00 36.62  ? 78  ILE B N   1 
ATOM   3570 C  CA  . ILE B 1 78  ? 0.958   -20.858 16.478  1.00 35.75  ? 78  ILE B CA  1 
ATOM   3571 C  C   . ILE B 1 78  ? 0.192   -19.728 17.181  1.00 37.02  ? 78  ILE B C   1 
ATOM   3572 O  O   . ILE B 1 78  ? 0.323   -19.588 18.406  1.00 42.13  ? 78  ILE B O   1 
ATOM   3573 C  CB  . ILE B 1 78  ? 2.462   -20.851 16.815  1.00 35.95  ? 78  ILE B CB  1 
ATOM   3574 C  CG1 . ILE B 1 78  ? 3.166   -19.607 16.269  1.00 37.94  ? 78  ILE B CG1 1 
ATOM   3575 C  CG2 . ILE B 1 78  ? 3.138   -22.115 16.307  1.00 38.47  ? 78  ILE B CG2 1 
ATOM   3576 C  CD1 . ILE B 1 78  ? 4.430   -19.234 17.015  1.00 34.61  ? 78  ILE B CD1 1 
ATOM   3577 N  N   . GLY B 1 79  ? -0.598  -18.941 16.447  1.00 37.43  ? 79  GLY B N   1 
ATOM   3578 C  CA  . GLY B 1 79  ? -1.381  -17.832 17.022  1.00 35.59  ? 79  GLY B CA  1 
ATOM   3579 C  C   . GLY B 1 79  ? -2.268  -17.207 15.966  1.00 36.17  ? 79  GLY B C   1 
ATOM   3580 O  O   . GLY B 1 79  ? -1.996  -17.404 14.758  1.00 34.73  ? 79  GLY B O   1 
ATOM   3581 N  N   . HIS B 1 80  ? -3.336  -16.547 16.398  1.00 36.04  ? 80  HIS B N   1 
ATOM   3582 C  CA  . HIS B 1 80  ? -4.320  -15.909 15.495  1.00 37.77  ? 80  HIS B CA  1 
ATOM   3583 C  C   . HIS B 1 80  ? -4.940  -14.737 16.226  1.00 37.25  ? 80  HIS B C   1 
ATOM   3584 O  O   . HIS B 1 80  ? -5.239  -14.840 17.421  1.00 34.88  ? 80  HIS B O   1 
ATOM   3585 C  CB  . HIS B 1 80  ? -5.363  -16.882 14.921  1.00 39.65  ? 80  HIS B CB  1 
ATOM   3586 C  CG  . HIS B 1 80  ? -6.210  -17.591 15.919  1.00 43.23  ? 80  HIS B CG  1 
ATOM   3587 N  ND1 . HIS B 1 80  ? -5.852  -18.819 16.449  1.00 45.07  ? 80  HIS B ND1 1 
ATOM   3588 C  CD2 . HIS B 1 80  ? -7.425  -17.291 16.433  1.00 49.39  ? 80  HIS B CD2 1 
ATOM   3589 C  CE1 . HIS B 1 80  ? -6.795  -19.229 17.277  1.00 48.18  ? 80  HIS B CE1 1 
ATOM   3590 N  NE2 . HIS B 1 80  ? -7.776  -18.303 17.292  1.00 49.60  ? 80  HIS B NE2 1 
ATOM   3591 N  N   . SER B 1 81  ? -5.060  -13.629 15.530  1.00 35.00  ? 81  SER B N   1 
ATOM   3592 C  CA  . SER B 1 81  ? -5.841  -12.487 16.028  1.00 32.32  ? 81  SER B CA  1 
ATOM   3593 C  C   . SER B 1 81  ? -6.334  -11.685 14.840  1.00 33.23  ? 81  SER B C   1 
ATOM   3594 O  O   . SER B 1 81  ? -6.003  -12.020 13.685  1.00 30.92  ? 81  SER B O   1 
ATOM   3595 C  CB  . SER B 1 81  ? -5.065  -11.654 16.999  1.00 34.35  ? 81  SER B CB  1 
ATOM   3596 O  OG  . SER B 1 81  ? -3.975  -11.014 16.370  1.00 36.96  ? 81  SER B OG  1 
ATOM   3597 N  N   . MET B 1 82  ? -7.206  -10.743 15.159  1.00 34.03  ? 82  MET B N   1 
ATOM   3598 C  CA  . MET B 1 82  ? -7.931  -9.894  14.204  1.00 35.03  ? 82  MET B CA  1 
ATOM   3599 C  C   . MET B 1 82  ? -7.574  -8.439  14.511  1.00 32.73  ? 82  MET B C   1 
ATOM   3600 O  O   . MET B 1 82  ? -7.569  -8.041  15.684  1.00 29.76  ? 82  MET B O   1 
ATOM   3601 C  CB  . MET B 1 82  ? -9.421  -10.144 14.384  1.00 36.54  ? 82  MET B CB  1 
ATOM   3602 C  CG  . MET B 1 82  ? -10.294 -9.521  13.344  1.00 39.16  ? 82  MET B CG  1 
ATOM   3603 S  SD  . MET B 1 82  ? -11.918 -10.299 13.446  1.00 44.41  ? 82  MET B SD  1 
ATOM   3604 C  CE  . MET B 1 82  ? -11.501 -11.858 12.665  1.00 46.44  ? 82  MET B CE  1 
ATOM   3605 N  N   . GLN B 1 83  ? -7.196  -7.699  13.485  1.00 31.42  ? 83  GLN B N   1 
ATOM   3606 C  CA  . GLN B 1 83  ? -7.107  -6.234  13.562  1.00 29.44  ? 83  GLN B CA  1 
ATOM   3607 C  C   . GLN B 1 83  ? -8.088  -5.715  12.519  1.00 26.91  ? 83  GLN B C   1 
ATOM   3608 O  O   . GLN B 1 83  ? -7.887  -5.978  11.316  1.00 26.59  ? 83  GLN B O   1 
ATOM   3609 C  CB  . GLN B 1 83  ? -5.677  -5.757  13.344  1.00 32.27  ? 83  GLN B CB  1 
ATOM   3610 C  CG  . GLN B 1 83  ? -5.591  -4.247  13.365  1.00 30.02  ? 83  GLN B CG  1 
ATOM   3611 C  CD  . GLN B 1 83  ? -4.160  -3.804  13.357  1.00 34.66  ? 83  GLN B CD  1 
ATOM   3612 O  OE1 . GLN B 1 83  ? -3.247  -4.587  13.087  1.00 37.74  ? 83  GLN B OE1 1 
ATOM   3613 N  NE2 . GLN B 1 83  ? -3.965  -2.540  13.674  1.00 33.41  ? 83  GLN B NE2 1 
ATOM   3614 N  N   . ASN B 1 84  ? -9.182  -5.125  12.977  1.00 24.96  ? 84  ASN B N   1 
ATOM   3615 C  CA  . ASN B 1 84  ? -10.206 -4.608  12.050  1.00 25.40  ? 84  ASN B CA  1 
ATOM   3616 C  C   . ASN B 1 84  ? -10.591 -5.773  11.126  1.00 25.90  ? 84  ASN B C   1 
ATOM   3617 O  O   . ASN B 1 84  ? -10.923 -6.873  11.658  1.00 27.07  ? 84  ASN B O   1 
ATOM   3618 C  CB  . ASN B 1 84  ? -9.634  -3.351  11.408  1.00 24.01  ? 84  ASN B CB  1 
ATOM   3619 C  CG  . ASN B 1 84  ? -9.308  -2.294  12.441  1.00 25.55  ? 84  ASN B CG  1 
ATOM   3620 O  OD1 . ASN B 1 84  ? -10.141 -1.948  13.277  1.00 26.52  ? 84  ASN B OD1 1 
ATOM   3621 N  ND2 . ASN B 1 84  ? -8.098  -1.763  12.393  1.00 25.72  ? 84  ASN B ND2 1 
ATOM   3622 N  N   . CYS B 1 85  ? -10.492 -5.595  9.809   1.00 25.69  ? 85  CYS B N   1 
ATOM   3623 C  CA  . CYS B 1 85  ? -10.988 -6.587  8.817   1.00 24.30  ? 85  CYS B CA  1 
ATOM   3624 C  C   . CYS B 1 85  ? -9.851  -7.491  8.333   1.00 24.04  ? 85  CYS B C   1 
ATOM   3625 O  O   . CYS B 1 85  ? -10.072 -8.241  7.389   1.00 24.58  ? 85  CYS B O   1 
ATOM   3626 C  CB  . CYS B 1 85  ? -11.676 -5.910  7.642   1.00 23.66  ? 85  CYS B CB  1 
ATOM   3627 S  SG  . CYS B 1 85  ? -13.115 -4.920  8.141   1.00 24.87  ? 85  CYS B SG  1 
ATOM   3628 N  N   . VAL B 1 86  ? -8.691  -7.437  8.981   1.00 25.44  ? 86  VAL B N   1 
ATOM   3629 C  CA  . VAL B 1 86  ? -7.515  -8.272  8.623   1.00 24.90  ? 86  VAL B CA  1 
ATOM   3630 C  C   . VAL B 1 86  ? -7.277  -9.317  9.719   1.00 25.02  ? 86  VAL B C   1 
ATOM   3631 O  O   . VAL B 1 86  ? -7.294  -8.965  10.914  1.00 22.50  ? 86  VAL B O   1 
ATOM   3632 C  CB  . VAL B 1 86  ? -6.302  -7.365  8.382   1.00 25.77  ? 86  VAL B CB  1 
ATOM   3633 C  CG1 . VAL B 1 86  ? -4.983  -8.047  8.663   1.00 27.95  ? 86  VAL B CG1 1 
ATOM   3634 C  CG2 . VAL B 1 86  ? -6.359  -6.837  6.968   1.00 27.84  ? 86  VAL B CG2 1 
ATOM   3635 N  N   . LEU B 1 87  ? -7.047  -10.553 9.291   1.00 26.10  ? 87  LEU B N   1 
ATOM   3636 C  CA  . LEU B 1 87  ? -6.622  -11.701 10.136  1.00 27.61  ? 87  LEU B CA  1 
ATOM   3637 C  C   . LEU B 1 87  ? -5.087  -11.760 10.166  1.00 28.27  ? 87  LEU B C   1 
ATOM   3638 O  O   . LEU B 1 87  ? -4.477  -11.753 9.081   1.00 26.41  ? 87  LEU B O   1 
ATOM   3639 C  CB  . LEU B 1 87  ? -7.219  -12.966 9.514   1.00 30.51  ? 87  LEU B CB  1 
ATOM   3640 C  CG  . LEU B 1 87  ? -7.139  -14.225 10.365  1.00 34.81  ? 87  LEU B CG  1 
ATOM   3641 C  CD1 . LEU B 1 87  ? -8.153  -14.145 11.490  1.00 40.59  ? 87  LEU B CD1 1 
ATOM   3642 C  CD2 . LEU B 1 87  ? -7.381  -15.469 9.527   1.00 36.24  ? 87  LEU B CD2 1 
ATOM   3643 N  N   . LYS B 1 88  ? -4.494  -11.776 11.364  1.00 27.13  ? 88  LYS B N   1 
ATOM   3644 C  CA  . LYS B 1 88  ? -3.041  -11.951 11.590  1.00 29.46  ? 88  LYS B CA  1 
ATOM   3645 C  C   . LYS B 1 88  ? -2.796  -13.380 12.097  1.00 31.97  ? 88  LYS B C   1 
ATOM   3646 O  O   . LYS B 1 88  ? -3.286  -13.732 13.186  1.00 33.83  ? 88  LYS B O   1 
ATOM   3647 C  CB  . LYS B 1 88  ? -2.539  -10.913 12.591  1.00 30.49  ? 88  LYS B CB  1 
ATOM   3648 C  CG  . LYS B 1 88  ? -2.818  -9.476  12.186  1.00 34.10  ? 88  LYS B CG  1 
ATOM   3649 C  CD  . LYS B 1 88  ? -1.911  -8.488  12.853  1.00 33.92  ? 88  LYS B CD  1 
ATOM   3650 C  CE  . LYS B 1 88  ? -2.162  -8.415  14.327  1.00 36.89  ? 88  LYS B CE  1 
ATOM   3651 N  NZ  . LYS B 1 88  ? -1.629  -7.150  14.873  1.00 39.50  ? 88  LYS B NZ  1 
ATOM   3652 N  N   . LEU B 1 89  ? -2.109  -14.202 11.314  1.00 30.45  ? 89  LEU B N   1 
ATOM   3653 C  CA  . LEU B 1 89  ? -1.757  -15.583 11.717  1.00 31.32  ? 89  LEU B CA  1 
ATOM   3654 C  C   . LEU B 1 89  ? -0.298  -15.566 12.110  1.00 31.83  ? 89  LEU B C   1 
ATOM   3655 O  O   . LEU B 1 89  ? 0.531   -15.328 11.235  1.00 31.09  ? 89  LEU B O   1 
ATOM   3656 C  CB  . LEU B 1 89  ? -1.993  -16.535 10.551  1.00 31.30  ? 89  LEU B CB  1 
ATOM   3657 C  CG  . LEU B 1 89  ? -3.437  -16.625 10.069  1.00 31.97  ? 89  LEU B CG  1 
ATOM   3658 C  CD1 . LEU B 1 89  ? -3.586  -17.653 8.962   1.00 33.88  ? 89  LEU B CD1 1 
ATOM   3659 C  CD2 . LEU B 1 89  ? -4.370  -16.944 11.211  1.00 32.70  ? 89  LEU B CD2 1 
ATOM   3660 N  N   . LYS B 1 90  ? -0.000  -15.743 13.392  1.00 36.78  ? 90  LYS B N   1 
ATOM   3661 C  CA  . LYS B 1 90  ? 1.405   -15.895 13.828  1.00 37.25  ? 90  LYS B CA  1 
ATOM   3662 C  C   . LYS B 1 90  ? 1.856   -17.285 13.368  1.00 36.85  ? 90  LYS B C   1 
ATOM   3663 O  O   . LYS B 1 90  ? 1.056   -18.249 13.547  1.00 32.25  ? 90  LYS B O   1 
ATOM   3664 C  CB  . LYS B 1 90  ? 1.582   -15.681 15.330  1.00 40.12  ? 90  LYS B CB  1 
ATOM   3665 C  CG  . LYS B 1 90  ? 3.023   -15.847 15.789  1.00 46.92  ? 90  LYS B CG  1 
ATOM   3666 C  CD  . LYS B 1 90  ? 3.389   -15.047 17.001  1.00 52.09  ? 90  LYS B CD  1 
ATOM   3667 C  CE  . LYS B 1 90  ? 4.716   -15.467 17.591  1.00 56.86  ? 90  LYS B CE  1 
ATOM   3668 N  NZ  . LYS B 1 90  ? 5.199   -14.477 18.580  1.00 58.90  ? 90  LYS B NZ  1 
ATOM   3669 N  N   . VAL B 1 91  ? 3.047   -17.354 12.761  1.00 33.50  ? 91  VAL B N   1 
ATOM   3670 C  CA  . VAL B 1 91  ? 3.671   -18.622 12.286  1.00 36.03  ? 91  VAL B CA  1 
ATOM   3671 C  C   . VAL B 1 91  ? 4.972   -18.875 13.064  1.00 37.62  ? 91  VAL B C   1 
ATOM   3672 O  O   . VAL B 1 91  ? 5.528   -17.919 13.686  1.00 36.68  ? 91  VAL B O   1 
ATOM   3673 C  CB  . VAL B 1 91  ? 3.871   -18.616 10.754  1.00 37.09  ? 91  VAL B CB  1 
ATOM   3674 C  CG1 . VAL B 1 91  ? 2.532   -18.710 10.038  1.00 35.55  ? 91  VAL B CG1 1 
ATOM   3675 C  CG2 . VAL B 1 91  ? 4.663   -17.420 10.241  1.00 36.18  ? 91  VAL B CG2 1 
ATOM   3676 N  N   . ASP B 1 92  ? 5.449   -20.123 13.029  1.00 41.98  ? 92  ASP B N   1 
ATOM   3677 C  CA  . ASP B 1 92  ? 6.668   -20.577 13.760  1.00 45.29  ? 92  ASP B CA  1 
ATOM   3678 C  C   . ASP B 1 92  ? 7.946   -20.004 13.122  1.00 47.48  ? 92  ASP B C   1 
ATOM   3679 O  O   . ASP B 1 92  ? 8.994   -20.086 13.771  1.00 49.01  ? 92  ASP B O   1 
ATOM   3680 C  CB  . ASP B 1 92  ? 6.758   -22.108 13.823  1.00 47.09  ? 92  ASP B CB  1 
ATOM   3681 C  CG  . ASP B 1 92  ? 6.586   -22.801 12.479  1.00 51.84  ? 92  ASP B CG  1 
ATOM   3682 O  OD1 . ASP B 1 92  ? 6.791   -22.144 11.435  1.00 56.28  ? 92  ASP B OD1 1 
ATOM   3683 O  OD2 . ASP B 1 92  ? 6.225   -23.990 12.479  1.00 56.49  ? 92  ASP B OD2 1 
ATOM   3684 N  N   . THR B 1 93  ? 7.879   -19.461 11.898  1.00 47.59  ? 93  THR B N   1 
ATOM   3685 C  CA  . THR B 1 93  ? 9.066   -19.110 11.072  1.00 42.37  ? 93  THR B CA  1 
ATOM   3686 C  C   . THR B 1 93  ? 8.943   -17.708 10.473  1.00 37.00  ? 93  THR B C   1 
ATOM   3687 O  O   . THR B 1 93  ? 7.941   -17.435 9.825   1.00 34.36  ? 93  THR B O   1 
ATOM   3688 C  CB  . THR B 1 93  ? 9.253   -20.110 9.932   1.00 43.86  ? 93  THR B CB  1 
ATOM   3689 O  OG1 . THR B 1 93  ? 9.081   -21.387 10.545  1.00 45.07  ? 93  THR B OG1 1 
ATOM   3690 C  CG2 . THR B 1 93  ? 10.605  -19.970 9.260   1.00 46.91  ? 93  THR B CG2 1 
ATOM   3691 N  N   . ALA B 1 94  ? 9.956   -16.874 10.683  1.00 34.95  ? 94  ALA B N   1 
ATOM   3692 C  CA  . ALA B 1 94  ? 10.069  -15.546 10.059  1.00 37.05  ? 94  ALA B CA  1 
ATOM   3693 C  C   . ALA B 1 94  ? 10.376  -15.765 8.575   1.00 40.11  ? 94  ALA B C   1 
ATOM   3694 O  O   . ALA B 1 94  ? 11.067  -16.741 8.250   1.00 37.71  ? 94  ALA B O   1 
ATOM   3695 C  CB  . ALA B 1 94  ? 11.111  -14.735 10.779  1.00 36.61  ? 94  ALA B CB  1 
ATOM   3696 N  N   . ASN B 1 95  ? 9.781   -14.957 7.695   1.00 38.32  ? 95  ASN B N   1 
ATOM   3697 C  CA  . ASN B 1 95  ? 10.022  -15.032 6.235   1.00 32.60  ? 95  ASN B CA  1 
ATOM   3698 C  C   . ASN B 1 95  ? 11.463  -14.597 5.993   1.00 33.02  ? 95  ASN B C   1 
ATOM   3699 O  O   . ASN B 1 95  ? 11.773  -13.422 6.198   1.00 33.87  ? 95  ASN B O   1 
ATOM   3700 C  CB  . ASN B 1 95  ? 9.027   -14.147 5.471   1.00 35.10  ? 95  ASN B CB  1 
ATOM   3701 C  CG  . ASN B 1 95  ? 9.163   -14.290 3.973   1.00 33.88  ? 95  ASN B CG  1 
ATOM   3702 O  OD1 . ASN B 1 95  ? 10.071  -14.974 3.508   1.00 31.23  ? 95  ASN B OD1 1 
ATOM   3703 N  ND2 . ASN B 1 95  ? 8.287   -13.647 3.219   1.00 30.97  ? 95  ASN B ND2 1 
ATOM   3704 N  N   . PRO B 1 96  ? 12.396  -15.486 5.557   1.00 31.09  ? 96  PRO B N   1 
ATOM   3705 C  CA  . PRO B 1 96  ? 13.770  -15.064 5.312   1.00 34.33  ? 96  PRO B CA  1 
ATOM   3706 C  C   . PRO B 1 96  ? 13.817  -14.067 4.139   1.00 34.97  ? 96  PRO B C   1 
ATOM   3707 O  O   . PRO B 1 96  ? 14.837  -13.436 3.967   1.00 36.09  ? 96  PRO B O   1 
ATOM   3708 C  CB  . PRO B 1 96  ? 14.518  -16.373 4.994   1.00 34.55  ? 96  PRO B CB  1 
ATOM   3709 C  CG  . PRO B 1 96  ? 13.440  -17.309 4.498   1.00 33.40  ? 96  PRO B CG  1 
ATOM   3710 C  CD  . PRO B 1 96  ? 12.198  -16.910 5.261   1.00 33.33  ? 96  PRO B CD  1 
ATOM   3711 N  N   . LYS B 1 97  ? 12.730  -13.938 3.370   1.00 33.26  ? 97  LYS B N   1 
ATOM   3712 C  CA  . LYS B 1 97  ? 12.639  -12.968 2.246   1.00 33.81  ? 97  LYS B CA  1 
ATOM   3713 C  C   . LYS B 1 97  ? 11.896  -11.700 2.680   1.00 29.69  ? 97  LYS B C   1 
ATOM   3714 O  O   . LYS B 1 97  ? 11.616  -10.882 1.822   1.00 30.35  ? 97  LYS B O   1 
ATOM   3715 C  CB  . LYS B 1 97  ? 11.960  -13.612 1.035   1.00 35.22  ? 97  LYS B CB  1 
ATOM   3716 C  CG  . LYS B 1 97  ? 12.674  -14.833 0.475   1.00 39.54  ? 97  LYS B CG  1 
ATOM   3717 C  CD  . LYS B 1 97  ? 12.152  -15.218 -0.886  1.00 45.63  ? 97  LYS B CD  1 
ATOM   3718 C  CE  . LYS B 1 97  ? 12.837  -16.428 -1.485  1.00 52.88  ? 97  LYS B CE  1 
ATOM   3719 N  NZ  . LYS B 1 97  ? 12.165  -17.682 -1.074  1.00 60.59  ? 97  LYS B NZ  1 
ATOM   3720 N  N   . THR B 1 98  ? 11.656  -11.476 3.968   1.00 30.01  ? 98  THR B N   1 
ATOM   3721 C  CA  . THR B 1 98  ? 11.027  -10.209 4.442   1.00 30.47  ? 98  THR B CA  1 
ATOM   3722 C  C   . THR B 1 98  ? 11.849  -9.009  3.956   1.00 30.42  ? 98  THR B C   1 
ATOM   3723 O  O   . THR B 1 98  ? 12.995  -8.833  4.347   1.00 27.79  ? 98  THR B O   1 
ATOM   3724 C  CB  . THR B 1 98  ? 10.885  -10.152 5.970   1.00 30.76  ? 98  THR B CB  1 
ATOM   3725 O  OG1 . THR B 1 98  ? 10.102  -11.281 6.362   1.00 31.51  ? 98  THR B OG1 1 
ATOM   3726 C  CG2 . THR B 1 98  ? 10.249  -8.863  6.457   1.00 31.67  ? 98  THR B CG2 1 
ATOM   3727 N  N   . PRO B 1 99  ? 11.300  -8.103  3.119   1.00 27.38  ? 99  PRO B N   1 
ATOM   3728 C  CA  . PRO B 1 99  ? 12.009  -6.858  2.818   1.00 26.82  ? 99  PRO B CA  1 
ATOM   3729 C  C   . PRO B 1 99  ? 11.912  -5.830  3.950   1.00 27.76  ? 99  PRO B C   1 
ATOM   3730 O  O   . PRO B 1 99  ? 11.132  -6.023  4.866   1.00 30.08  ? 99  PRO B O   1 
ATOM   3731 C  CB  . PRO B 1 99  ? 11.260  -6.339  1.602   1.00 27.96  ? 99  PRO B CB  1 
ATOM   3732 C  CG  . PRO B 1 99  ? 9.839   -6.855  1.791   1.00 28.68  ? 99  PRO B CG  1 
ATOM   3733 C  CD  . PRO B 1 99  ? 9.994   -8.206  2.458   1.00 27.94  ? 99  PRO B CD  1 
ATOM   3734 N  N   . LYS B 1 100 ? 12.699  -4.763  3.859   1.00 25.01  ? 100 LYS B N   1 
ATOM   3735 C  CA  . LYS B 1 100 ? 12.445  -3.492  4.577   1.00 28.18  ? 100 LYS B CA  1 
ATOM   3736 C  C   . LYS B 1 100 ? 11.044  -3.016  4.157   1.00 26.85  ? 100 LYS B C   1 
ATOM   3737 O  O   . LYS B 1 100 ? 10.809  -2.904  2.937   1.00 24.42  ? 100 LYS B O   1 
ATOM   3738 C  CB  . LYS B 1 100 ? 13.574  -2.518  4.245   1.00 32.04  ? 100 LYS B CB  1 
ATOM   3739 C  CG  . LYS B 1 100 ? 13.534  -1.167  4.935   1.00 40.76  ? 100 LYS B CG  1 
ATOM   3740 C  CD  . LYS B 1 100 ? 14.565  -0.216  4.321   1.00 50.30  ? 100 LYS B CD  1 
ATOM   3741 C  CE  . LYS B 1 100 ? 14.655  1.152   4.966   1.00 54.01  ? 100 LYS B CE  1 
ATOM   3742 N  NZ  . LYS B 1 100 ? 15.402  1.098   6.244   1.00 57.62  ? 100 LYS B NZ  1 
ATOM   3743 N  N   . TYR B 1 101 ? 10.115  -2.845  5.105   1.00 24.92  ? 101 TYR B N   1 
ATOM   3744 C  CA  . TYR B 1 101 ? 8.707   -2.508  4.788   1.00 24.30  ? 101 TYR B CA  1 
ATOM   3745 C  C   . TYR B 1 101 ? 8.092   -1.690  5.912   1.00 27.73  ? 101 TYR B C   1 
ATOM   3746 O  O   . TYR B 1 101 ? 8.591   -1.721  7.053   1.00 26.22  ? 101 TYR B O   1 
ATOM   3747 C  CB  . TYR B 1 101 ? 7.849   -3.748  4.532   1.00 23.17  ? 101 TYR B CB  1 
ATOM   3748 C  CG  . TYR B 1 101 ? 7.439   -4.468  5.784   1.00 23.22  ? 101 TYR B CG  1 
ATOM   3749 C  CD1 . TYR B 1 101 ? 8.250   -5.438  6.355   1.00 23.43  ? 101 TYR B CD1 1 
ATOM   3750 C  CD2 . TYR B 1 101 ? 6.279   -4.114  6.444   1.00 21.53  ? 101 TYR B CD2 1 
ATOM   3751 C  CE1 . TYR B 1 101 ? 7.894   -6.063  7.538   1.00 24.36  ? 101 TYR B CE1 1 
ATOM   3752 C  CE2 . TYR B 1 101 ? 5.904   -4.743  7.612   1.00 22.60  ? 101 TYR B CE2 1 
ATOM   3753 C  CZ  . TYR B 1 101 ? 6.722   -5.694  8.180   1.00 24.49  ? 101 TYR B CZ  1 
ATOM   3754 O  OH  . TYR B 1 101 ? 6.338   -6.258  9.363   1.00 25.65  ? 101 TYR B OH  1 
ATOM   3755 N  N   . LYS B 1 102 ? 7.037   -0.954  5.557   1.00 27.56  ? 102 LYS B N   1 
ATOM   3756 C  CA  . LYS B 1 102 ? 6.069   -0.413  6.531   1.00 31.78  ? 102 LYS B CA  1 
ATOM   3757 C  C   . LYS B 1 102 ? 4.666   -0.546  5.940   1.00 29.09  ? 102 LYS B C   1 
ATOM   3758 O  O   . LYS B 1 102 ? 4.529   -0.759  4.711   1.00 29.66  ? 102 LYS B O   1 
ATOM   3759 C  CB  . LYS B 1 102 ? 6.450   1.022   6.904   1.00 35.13  ? 102 LYS B CB  1 
ATOM   3760 C  CG  . LYS B 1 102 ? 6.441   2.002   5.751   1.00 40.28  ? 102 LYS B CG  1 
ATOM   3761 C  CD  . LYS B 1 102 ? 6.686   3.434   6.170   1.00 45.46  ? 102 LYS B CD  1 
ATOM   3762 C  CE  . LYS B 1 102 ? 8.152   3.785   6.290   1.00 51.37  ? 102 LYS B CE  1 
ATOM   3763 N  NZ  . LYS B 1 102 ? 8.414   5.145   5.754   1.00 58.86  ? 102 LYS B NZ  1 
ATOM   3764 N  N   . PHE B 1 103 ? 3.670   -0.429  6.811   1.00 27.81  ? 103 PHE B N   1 
ATOM   3765 C  CA  . PHE B 1 103 ? 2.241   -0.292  6.467   1.00 24.87  ? 103 PHE B CA  1 
ATOM   3766 C  C   . PHE B 1 103 ? 1.957   1.196   6.359   1.00 25.51  ? 103 PHE B C   1 
ATOM   3767 O  O   . PHE B 1 103 ? 2.354   1.939   7.260   1.00 26.42  ? 103 PHE B O   1 
ATOM   3768 C  CB  . PHE B 1 103 ? 1.376   -0.994  7.510   1.00 25.84  ? 103 PHE B CB  1 
ATOM   3769 C  CG  . PHE B 1 103 ? 1.573   -2.487  7.575   1.00 25.72  ? 103 PHE B CG  1 
ATOM   3770 C  CD1 . PHE B 1 103 ? 2.200   -3.173  6.542   1.00 24.34  ? 103 PHE B CD1 1 
ATOM   3771 C  CD2 . PHE B 1 103 ? 1.067   -3.213  8.642   1.00 24.66  ? 103 PHE B CD2 1 
ATOM   3772 C  CE1 . PHE B 1 103 ? 2.371   -4.548  6.597   1.00 23.97  ? 103 PHE B CE1 1 
ATOM   3773 C  CE2 . PHE B 1 103 ? 1.213   -4.592  8.675   1.00 24.17  ? 103 PHE B CE2 1 
ATOM   3774 C  CZ  . PHE B 1 103 ? 1.859   -5.256  7.665   1.00 23.85  ? 103 PHE B CZ  1 
ATOM   3775 N  N   . VAL B 1 104 ? 1.343   1.607   5.257   1.00 25.31  ? 104 VAL B N   1 
ATOM   3776 C  CA  . VAL B 1 104 ? 0.989   3.026   5.001   1.00 29.08  ? 104 VAL B CA  1 
ATOM   3777 C  C   . VAL B 1 104 ? -0.455  3.046   4.501   1.00 28.31  ? 104 VAL B C   1 
ATOM   3778 O  O   . VAL B 1 104 ? -0.834  2.128   3.780   1.00 33.77  ? 104 VAL B O   1 
ATOM   3779 C  CB  . VAL B 1 104 ? 1.990   3.658   4.013   1.00 33.26  ? 104 VAL B CB  1 
ATOM   3780 C  CG1 . VAL B 1 104 ? 1.595   5.061   3.587   1.00 36.28  ? 104 VAL B CG1 1 
ATOM   3781 C  CG2 . VAL B 1 104 ? 3.393   3.671   4.607   1.00 32.54  ? 104 VAL B CG2 1 
ATOM   3782 N  N   . ARG B 1 105 ? -1.239  4.036   4.909   1.00 25.78  ? 105 ARG B N   1 
ATOM   3783 C  CA  . ARG B 1 105 ? -2.571  4.288   4.322   1.00 26.22  ? 105 ARG B CA  1 
ATOM   3784 C  C   . ARG B 1 105 ? -2.440  5.364   3.237   1.00 25.41  ? 105 ARG B C   1 
ATOM   3785 O  O   . ARG B 1 105 ? -1.904  6.437   3.534   1.00 28.05  ? 105 ARG B O   1 
ATOM   3786 C  CB  . ARG B 1 105 ? -3.567  4.681   5.413   1.00 26.32  ? 105 ARG B CB  1 
ATOM   3787 C  CG  . ARG B 1 105 ? -4.981  4.841   4.875   1.00 25.81  ? 105 ARG B CG  1 
ATOM   3788 C  CD  . ARG B 1 105 ? -5.997  4.876   5.977   1.00 25.89  ? 105 ARG B CD  1 
ATOM   3789 N  NE  . ARG B 1 105 ? -7.314  5.028   5.395   1.00 25.69  ? 105 ARG B NE  1 
ATOM   3790 C  CZ  . ARG B 1 105 ? -8.182  4.045   5.164   1.00 23.52  ? 105 ARG B CZ  1 
ATOM   3791 N  NH1 . ARG B 1 105 ? -7.878  2.794   5.430   1.00 24.62  ? 105 ARG B NH1 1 
ATOM   3792 N  NH2 . ARG B 1 105 ? -9.353  4.309   4.614   1.00 24.67  ? 105 ARG B NH2 1 
ATOM   3793 N  N   . ILE B 1 106 ? -2.901  5.098   2.017   1.00 25.14  ? 106 ILE B N   1 
ATOM   3794 C  CA  . ILE B 1 106 ? -2.811  6.093   0.903   1.00 27.79  ? 106 ILE B CA  1 
ATOM   3795 C  C   . ILE B 1 106 ? -4.062  6.980   0.890   1.00 27.06  ? 106 ILE B C   1 
ATOM   3796 O  O   . ILE B 1 106 ? -5.067  6.622   1.508   1.00 26.32  ? 106 ILE B O   1 
ATOM   3797 C  CB  . ILE B 1 106 ? -2.593  5.445   -0.477  1.00 29.99  ? 106 ILE B CB  1 
ATOM   3798 C  CG1 . ILE B 1 106 ? -3.581  4.303   -0.713  1.00 30.40  ? 106 ILE B CG1 1 
ATOM   3799 C  CG2 . ILE B 1 106 ? -1.141  5.027   -0.676  1.00 30.92  ? 106 ILE B CG2 1 
ATOM   3800 C  CD1 . ILE B 1 106 ? -3.696  3.884   -2.154  1.00 32.54  ? 106 ILE B CD1 1 
ATOM   3801 N  N   . GLN B 1 107 ? -3.959  8.112   0.202   1.00 31.06  ? 107 GLN B N   1 
ATOM   3802 C  CA  . GLN B 1 107 ? -5.043  9.104   -0.027  1.00 33.81  ? 107 GLN B CA  1 
ATOM   3803 C  C   . GLN B 1 107 ? -5.646  8.832   -1.392  1.00 31.14  ? 107 GLN B C   1 
ATOM   3804 O  O   . GLN B 1 107 ? -4.961  8.317   -2.267  1.00 27.30  ? 107 GLN B O   1 
ATOM   3805 C  CB  . GLN B 1 107 ? -4.481  10.527  -0.051  1.00 36.85  ? 107 GLN B CB  1 
ATOM   3806 C  CG  . GLN B 1 107 ? -3.801  10.943  1.242   1.00 43.77  ? 107 GLN B CG  1 
ATOM   3807 C  CD  . GLN B 1 107 ? -4.817  11.007  2.350   1.00 49.86  ? 107 GLN B CD  1 
ATOM   3808 O  OE1 . GLN B 1 107 ? -5.920  11.512  2.170   1.00 59.96  ? 107 GLN B OE1 1 
ATOM   3809 N  NE2 . GLN B 1 107 ? -4.470  10.441  3.490   1.00 56.47  ? 107 GLN B NE2 1 
ATOM   3810 N  N   . PRO B 1 108 ? -6.924  9.189   -1.623  1.00 33.46  ? 108 PRO B N   1 
ATOM   3811 C  CA  . PRO B 1 108 ? -7.509  9.068   -2.954  1.00 32.93  ? 108 PRO B CA  1 
ATOM   3812 C  C   . PRO B 1 108 ? -6.666  9.956   -3.882  1.00 28.62  ? 108 PRO B C   1 
ATOM   3813 O  O   . PRO B 1 108 ? -6.121  10.936  -3.406  1.00 24.74  ? 108 PRO B O   1 
ATOM   3814 C  CB  . PRO B 1 108 ? -8.963  9.551   -2.821  1.00 35.60  ? 108 PRO B CB  1 
ATOM   3815 C  CG  . PRO B 1 108 ? -9.214  9.667   -1.322  1.00 35.70  ? 108 PRO B CG  1 
ATOM   3816 C  CD  . PRO B 1 108 ? -7.861  9.769   -0.645  1.00 35.04  ? 108 PRO B CD  1 
ATOM   3817 N  N   . GLY B 1 109 ? -6.479  9.512   -5.131  1.00 26.96  ? 109 GLY B N   1 
ATOM   3818 C  CA  . GLY B 1 109 ? -5.629  10.177  -6.130  1.00 26.76  ? 109 GLY B CA  1 
ATOM   3819 C  C   . GLY B 1 109 ? -4.218  9.610   -6.176  1.00 29.86  ? 109 GLY B C   1 
ATOM   3820 O  O   . GLY B 1 109 ? -3.533  9.828   -7.193  1.00 28.07  ? 109 GLY B O   1 
ATOM   3821 N  N   . GLN B 1 110 ? -3.778  8.934   -5.108  1.00 30.95  ? 110 GLN B N   1 
ATOM   3822 C  CA  . GLN B 1 110 ? -2.424  8.330   -5.016  1.00 28.69  ? 110 GLN B CA  1 
ATOM   3823 C  C   . GLN B 1 110 ? -2.437  6.993   -5.762  1.00 26.76  ? 110 GLN B C   1 
ATOM   3824 O  O   . GLN B 1 110 ? -3.496  6.330   -5.807  1.00 27.87  ? 110 GLN B O   1 
ATOM   3825 C  CB  . GLN B 1 110 ? -1.968  8.205   -3.557  1.00 31.27  ? 110 GLN B CB  1 
ATOM   3826 C  CG  . GLN B 1 110 ? -1.701  9.564   -2.918  1.00 36.97  ? 110 GLN B CG  1 
ATOM   3827 C  CD  . GLN B 1 110 ? -0.985  9.557   -1.578  1.00 45.19  ? 110 GLN B CD  1 
ATOM   3828 O  OE1 . GLN B 1 110 ? -1.439  9.002   -0.566  1.00 42.96  ? 110 GLN B OE1 1 
ATOM   3829 N  NE2 . GLN B 1 110 ? 0.138   10.257  -1.533  1.00 54.14  ? 110 GLN B NE2 1 
ATOM   3830 N  N   . THR B 1 111 ? -1.306  6.636   -6.370  1.00 23.96  ? 111 THR B N   1 
ATOM   3831 C  CA  . THR B 1 111 ? -1.170  5.406   -7.185  1.00 22.14  ? 111 THR B CA  1 
ATOM   3832 C  C   . THR B 1 111 ? -0.377  4.360   -6.392  1.00 21.59  ? 111 THR B C   1 
ATOM   3833 O  O   . THR B 1 111 ? 0.354   4.704   -5.438  1.00 21.03  ? 111 THR B O   1 
ATOM   3834 C  CB  . THR B 1 111 ? -0.540  5.700   -8.545  1.00 21.29  ? 111 THR B CB  1 
ATOM   3835 O  OG1 . THR B 1 111 ? 0.775   6.205   -8.316  1.00 21.23  ? 111 THR B OG1 1 
ATOM   3836 C  CG2 . THR B 1 111 ? -1.351  6.679   -9.358  1.00 21.40  ? 111 THR B CG2 1 
ATOM   3837 N  N   . PHE B 1 112 ? -0.475  3.124   -6.836  1.00 21.03  ? 112 PHE B N   1 
ATOM   3838 C  CA  . PHE B 1 112 ? 0.278   1.994   -6.268  1.00 21.74  ? 112 PHE B CA  1 
ATOM   3839 C  C   . PHE B 1 112 ? 0.199   0.840   -7.248  1.00 20.87  ? 112 PHE B C   1 
ATOM   3840 O  O   . PHE B 1 112 ? -0.692  0.827   -8.107  1.00 18.24  ? 112 PHE B O   1 
ATOM   3841 C  CB  . PHE B 1 112 ? -0.279  1.574   -4.909  1.00 22.21  ? 112 PHE B CB  1 
ATOM   3842 C  CG  . PHE B 1 112 ? -1.742  1.188   -4.867  1.00 22.12  ? 112 PHE B CG  1 
ATOM   3843 C  CD1 . PHE B 1 112 ? -2.738  2.146   -4.700  1.00 22.63  ? 112 PHE B CD1 1 
ATOM   3844 C  CD2 . PHE B 1 112 ? -2.123  -0.143  -4.910  1.00 21.12  ? 112 PHE B CD2 1 
ATOM   3845 C  CE1 . PHE B 1 112 ? -4.075  1.785   -4.619  1.00 22.54  ? 112 PHE B CE1 1 
ATOM   3846 C  CE2 . PHE B 1 112 ? -3.456  -0.507  -4.796  1.00 23.16  ? 112 PHE B CE2 1 
ATOM   3847 C  CZ  . PHE B 1 112 ? -4.433  0.455   -4.645  1.00 23.32  ? 112 PHE B CZ  1 
ATOM   3848 N  N   . SER B 1 113 ? 1.172   -0.054  -7.108  1.00 21.08  ? 113 SER B N   1 
ATOM   3849 C  CA  . SER B 1 113 ? 1.291   -1.299  -7.878  1.00 20.96  ? 113 SER B CA  1 
ATOM   3850 C  C   . SER B 1 113 ? 0.552   -2.377  -7.102  1.00 21.11  ? 113 SER B C   1 
ATOM   3851 O  O   . SER B 1 113 ? 0.600   -2.399  -5.870  1.00 20.16  ? 113 SER B O   1 
ATOM   3852 C  CB  . SER B 1 113 ? 2.732   -1.666  -8.066  1.00 22.43  ? 113 SER B CB  1 
ATOM   3853 O  OG  . SER B 1 113 ? 3.395   -0.655  -8.807  1.00 22.96  ? 113 SER B OG  1 
ATOM   3854 N  N   A VAL B 1 114 ? -0.120  -3.257  -7.841  0.25 21.07  ? 114 VAL B N   1 
ATOM   3855 N  N   B VAL B 1 114 ? -0.127  -3.252  -7.839  0.25 21.07  ? 114 VAL B N   1 
ATOM   3856 N  N   C VAL B 1 114 ? -0.131  -3.257  -7.824  0.25 21.74  ? 114 VAL B N   1 
ATOM   3857 N  N   D VAL B 1 114 ? -0.131  -3.257  -7.824  0.25 21.74  ? 114 VAL B N   1 
ATOM   3858 C  CA  A VAL B 1 114 ? -0.899  -4.410  -7.313  0.25 21.86  ? 114 VAL B CA  1 
ATOM   3859 C  CA  B VAL B 1 114 ? -0.899  -4.412  -7.315  0.25 21.86  ? 114 VAL B CA  1 
ATOM   3860 C  CA  C VAL B 1 114 ? -0.866  -4.409  -7.240  0.25 23.02  ? 114 VAL B CA  1 
ATOM   3861 C  CA  D VAL B 1 114 ? -0.866  -4.409  -7.240  0.25 23.02  ? 114 VAL B CA  1 
ATOM   3862 C  C   A VAL B 1 114 ? -0.252  -5.680  -7.860  0.25 21.92  ? 114 VAL B C   1 
ATOM   3863 C  C   B VAL B 1 114 ? -0.248  -5.680  -7.862  0.25 21.92  ? 114 VAL B C   1 
ATOM   3864 C  C   C VAL B 1 114 ? -0.289  -5.685  -7.843  0.25 22.58  ? 114 VAL B C   1 
ATOM   3865 C  C   D VAL B 1 114 ? -0.289  -5.685  -7.843  0.25 22.58  ? 114 VAL B C   1 
ATOM   3866 O  O   A VAL B 1 114 ? -0.126  -5.773  -9.092  0.25 21.42  ? 114 VAL B O   1 
ATOM   3867 O  O   B VAL B 1 114 ? -0.118  -5.772  -9.093  0.25 21.42  ? 114 VAL B O   1 
ATOM   3868 O  O   C VAL B 1 114 ? -0.263  -5.788  -9.081  0.25 21.85  ? 114 VAL B O   1 
ATOM   3869 O  O   D VAL B 1 114 ? -0.263  -5.788  -9.081  0.25 21.85  ? 114 VAL B O   1 
ATOM   3870 C  CB  A VAL B 1 114 ? -2.375  -4.326  -7.741  0.25 21.81  ? 114 VAL B CB  1 
ATOM   3871 C  CB  B VAL B 1 114 ? -2.376  -4.334  -7.739  0.25 21.82  ? 114 VAL B CB  1 
ATOM   3872 C  CB  C VAL B 1 114 ? -2.378  -4.315  -7.495  0.25 23.98  ? 114 VAL B CB  1 
ATOM   3873 C  CB  D VAL B 1 114 ? -2.378  -4.315  -7.495  0.25 23.98  ? 114 VAL B CB  1 
ATOM   3874 C  CG1 A VAL B 1 114 ? -3.126  -5.614  -7.426  0.25 21.94  ? 114 VAL B CG1 1 
ATOM   3875 C  CG1 B VAL B 1 114 ? -3.129  -5.618  -7.414  0.25 21.94  ? 114 VAL B CG1 1 
ATOM   3876 C  CG1 C VAL B 1 114 ? -3.142  -5.258  -6.574  0.25 24.95  ? 114 VAL B CG1 1 
ATOM   3877 C  CG1 D VAL B 1 114 ? -3.142  -5.258  -6.574  0.25 24.95  ? 114 VAL B CG1 1 
ATOM   3878 C  CG2 A VAL B 1 114 ? -3.067  -3.130  -7.097  0.25 22.41  ? 114 VAL B CG2 1 
ATOM   3879 C  CG2 B VAL B 1 114 ? -3.065  -3.127  -7.117  0.25 22.41  ? 114 VAL B CG2 1 
ATOM   3880 C  CG2 C VAL B 1 114 ? -2.875  -2.884  -7.347  0.25 24.82  ? 114 VAL B CG2 1 
ATOM   3881 C  CG2 D VAL B 1 114 ? -2.875  -2.884  -7.347  0.25 24.82  ? 114 VAL B CG2 1 
ATOM   3882 N  N   . LEU B 1 115 ? 0.155   -6.598  -6.981  1.00 21.92  ? 115 LEU B N   1 
ATOM   3883 C  CA  . LEU B 1 115 ? 0.557   -7.954  -7.397  1.00 24.32  ? 115 LEU B CA  1 
ATOM   3884 C  C   . LEU B 1 115 ? -0.683  -8.847  -7.285  1.00 25.32  ? 115 LEU B C   1 
ATOM   3885 O  O   . LEU B 1 115 ? -1.039  -9.237  -6.186  1.00 24.93  ? 115 LEU B O   1 
ATOM   3886 C  CB  . LEU B 1 115 ? 1.688   -8.427  -6.491  1.00 22.89  ? 115 LEU B CB  1 
ATOM   3887 C  CG  . LEU B 1 115 ? 2.284   -9.750  -6.928  1.00 21.82  ? 115 LEU B CG  1 
ATOM   3888 C  CD1 . LEU B 1 115 ? 2.718   -9.660  -8.379  1.00 21.41  ? 115 LEU B CD1 1 
ATOM   3889 C  CD2 . LEU B 1 115 ? 3.434   -10.112 -6.009  1.00 21.52  ? 115 LEU B CD2 1 
ATOM   3890 N  N   A ALA B 1 116 ? -1.347  -9.123  -8.410  0.25 24.88  ? 116 ALA B N   1 
ATOM   3891 N  N   B ALA B 1 116 ? -1.347  -9.123  -8.410  0.25 24.88  ? 116 ALA B N   1 
ATOM   3892 N  N   C ALA B 1 116 ? -1.307  -9.162  -8.423  0.25 28.12  ? 116 ALA B N   1 
ATOM   3893 N  N   D ALA B 1 116 ? -1.307  -9.162  -8.423  0.25 28.12  ? 116 ALA B N   1 
ATOM   3894 C  CA  A ALA B 1 116 ? -2.516  -10.030 -8.477  0.25 25.21  ? 116 ALA B CA  1 
ATOM   3895 C  CA  B ALA B 1 116 ? -2.516  -10.030 -8.477  0.25 25.21  ? 116 ALA B CA  1 
ATOM   3896 C  CA  C ALA B 1 116 ? -2.547  -9.969  -8.504  0.25 31.16  ? 116 ALA B CA  1 
ATOM   3897 C  CA  D ALA B 1 116 ? -2.547  -9.969  -8.504  0.25 31.16  ? 116 ALA B CA  1 
ATOM   3898 C  C   A ALA B 1 116 ? -2.027  -11.465 -8.254  0.25 26.15  ? 116 ALA B C   1 
ATOM   3899 C  C   B ALA B 1 116 ? -2.027  -11.465 -8.254  0.25 26.15  ? 116 ALA B C   1 
ATOM   3900 C  C   C ALA B 1 116 ? -2.199  -11.460 -8.475  0.25 35.32  ? 116 ALA B C   1 
ATOM   3901 C  C   D ALA B 1 116 ? -2.199  -11.460 -8.475  0.25 35.32  ? 116 ALA B C   1 
ATOM   3902 O  O   A ALA B 1 116 ? -1.075  -11.873 -8.942  0.25 24.86  ? 116 ALA B O   1 
ATOM   3903 O  O   B ALA B 1 116 ? -1.075  -11.873 -8.942  0.25 24.86  ? 116 ALA B O   1 
ATOM   3904 O  O   C ALA B 1 116 ? -1.361  -11.896 -9.286  0.25 34.36  ? 116 ALA B O   1 
ATOM   3905 O  O   D ALA B 1 116 ? -1.361  -11.896 -9.286  0.25 34.36  ? 116 ALA B O   1 
ATOM   3906 C  CB  A ALA B 1 116 ? -3.220  -9.880  -9.801  0.25 25.12  ? 116 ALA B CB  1 
ATOM   3907 C  CB  B ALA B 1 116 ? -3.220  -9.880  -9.801  0.25 25.12  ? 116 ALA B CB  1 
ATOM   3908 C  CB  C ALA B 1 116 ? -3.322  -9.618  -9.745  0.25 31.18  ? 116 ALA B CB  1 
ATOM   3909 C  CB  D ALA B 1 116 ? -3.322  -9.618  -9.745  0.25 31.18  ? 116 ALA B CB  1 
ATOM   3910 N  N   A CYS B 1 117 ? -2.627  -12.188 -7.304  0.25 27.78  ? 117 CYS B N   1 
ATOM   3911 N  N   B CYS B 1 117 ? -2.627  -12.188 -7.304  0.25 27.78  ? 117 CYS B N   1 
ATOM   3912 N  N   C CYS B 1 117 ? -2.832  -12.197 -7.563  0.25 41.47  ? 117 CYS B N   1 
ATOM   3913 N  N   D CYS B 1 117 ? -2.832  -12.197 -7.563  0.25 41.47  ? 117 CYS B N   1 
ATOM   3914 C  CA  A CYS B 1 117 ? -2.233  -13.580 -6.955  0.25 29.24  ? 117 CYS B CA  1 
ATOM   3915 C  CA  B CYS B 1 117 ? -2.233  -13.580 -6.955  0.25 29.24  ? 117 CYS B CA  1 
ATOM   3916 C  CA  C CYS B 1 117 ? -2.737  -13.673 -7.436  0.25 46.89  ? 117 CYS B CA  1 
ATOM   3917 C  CA  D CYS B 1 117 ? -2.737  -13.673 -7.436  0.25 46.89  ? 117 CYS B CA  1 
ATOM   3918 C  C   A CYS B 1 117 ? -3.450  -14.503 -7.006  0.25 29.48  ? 117 CYS B C   1 
ATOM   3919 C  C   B CYS B 1 117 ? -3.450  -14.503 -7.006  0.25 29.48  ? 117 CYS B C   1 
ATOM   3920 C  C   C CYS B 1 117 ? -3.879  -14.297 -8.247  0.25 48.80  ? 117 CYS B C   1 
ATOM   3921 C  C   D CYS B 1 117 ? -3.879  -14.297 -8.247  0.25 48.80  ? 117 CYS B C   1 
ATOM   3922 O  O   A CYS B 1 117 ? -4.582  -14.009 -6.853  0.25 29.16  ? 117 CYS B O   1 
ATOM   3923 O  O   B CYS B 1 117 ? -4.582  -14.009 -6.853  0.25 29.16  ? 117 CYS B O   1 
ATOM   3924 O  O   C CYS B 1 117 ? -4.971  -13.696 -8.283  0.25 45.60  ? 117 CYS B O   1 
ATOM   3925 O  O   D CYS B 1 117 ? -4.971  -13.696 -8.283  0.25 45.60  ? 117 CYS B O   1 
ATOM   3926 C  CB  A CYS B 1 117 ? -1.615  -13.678 -5.566  0.25 29.59  ? 117 CYS B CB  1 
ATOM   3927 C  CB  B CYS B 1 117 ? -1.615  -13.678 -5.566  0.25 29.59  ? 117 CYS B CB  1 
ATOM   3928 C  CB  C CYS B 1 117 ? -2.783  -14.067 -5.965  0.25 50.47  ? 117 CYS B CB  1 
ATOM   3929 C  CB  D CYS B 1 117 ? -2.783  -14.067 -5.965  0.25 50.47  ? 117 CYS B CB  1 
ATOM   3930 S  SG  A CYS B 1 117 ? -0.239  -12.538 -5.277  0.25 30.79  ? 117 CYS B SG  1 
ATOM   3931 S  SG  B CYS B 1 117 ? -0.239  -12.538 -5.277  0.25 30.79  ? 117 CYS B SG  1 
ATOM   3932 S  SG  C CYS B 1 117 ? -2.620  -15.845 -5.668  0.25 54.73  ? 117 CYS B SG  1 
ATOM   3933 S  SG  D CYS B 1 117 ? -2.620  -15.845 -5.668  0.25 54.73  ? 117 CYS B SG  1 
ATOM   3934 N  N   A TYR B 1 118 ? -3.186  -15.796 -7.206  0.25 31.06  ? 118 TYR B N   1 
ATOM   3935 N  N   B TYR B 1 118 ? -3.186  -15.796 -7.206  0.25 31.06  ? 118 TYR B N   1 
ATOM   3936 N  N   C TYR B 1 118 ? -3.611  -15.423 -8.918  0.25 53.71  ? 118 TYR B N   1 
ATOM   3937 N  N   D TYR B 1 118 ? -3.611  -15.423 -8.918  0.25 53.71  ? 118 TYR B N   1 
ATOM   3938 C  CA  A TYR B 1 118 ? -4.167  -16.910 -7.228  0.25 30.74  ? 118 TYR B CA  1 
ATOM   3939 C  CA  B TYR B 1 118 ? -4.167  -16.910 -7.228  0.25 30.74  ? 118 TYR B CA  1 
ATOM   3940 C  CA  C TYR B 1 118 ? -4.588  -16.164 -9.759  0.25 55.07  ? 118 TYR B CA  1 
ATOM   3941 C  CA  D TYR B 1 118 ? -4.588  -16.164 -9.759  0.25 55.07  ? 118 TYR B CA  1 
ATOM   3942 C  C   A TYR B 1 118 ? -3.497  -18.107 -6.549  0.25 31.43  ? 118 TYR B C   1 
ATOM   3943 C  C   B TYR B 1 118 ? -3.497  -18.107 -6.549  0.25 31.43  ? 118 TYR B C   1 
ATOM   3944 C  C   C TYR B 1 118 ? -4.288  -17.667 -9.669  0.25 54.81  ? 118 TYR B C   1 
ATOM   3945 C  C   D TYR B 1 118 ? -4.288  -17.667 -9.669  0.25 54.81  ? 118 TYR B C   1 
ATOM   3946 O  O   A TYR B 1 118 ? -2.439  -18.555 -7.037  0.25 30.20  ? 118 TYR B O   1 
ATOM   3947 O  O   B TYR B 1 118 ? -2.439  -18.555 -7.037  0.25 30.20  ? 118 TYR B O   1 
ATOM   3948 O  O   C TYR B 1 118 ? -3.105  -18.067 -9.733  0.25 52.00  ? 118 TYR B O   1 
ATOM   3949 O  O   D TYR B 1 118 ? -3.105  -18.067 -9.733  0.25 52.00  ? 118 TYR B O   1 
ATOM   3950 C  CB  A TYR B 1 118 ? -4.620  -17.168 -8.668  0.25 32.13  ? 118 TYR B CB  1 
ATOM   3951 C  CB  B TYR B 1 118 ? -4.620  -17.168 -8.668  0.25 32.13  ? 118 TYR B CB  1 
ATOM   3952 C  CB  C TYR B 1 118 ? -4.585  -15.605 -11.183 0.25 57.99  ? 118 TYR B CB  1 
ATOM   3953 C  CB  D TYR B 1 118 ? -4.585  -15.605 -11.183 0.25 57.99  ? 118 TYR B CB  1 
ATOM   3954 C  CG  A TYR B 1 118 ? -5.374  -16.002 -9.255  0.25 32.96  ? 118 TYR B CG  1 
ATOM   3955 C  CG  B TYR B 1 118 ? -5.374  -16.002 -9.255  0.25 32.96  ? 118 TYR B CG  1 
ATOM   3956 C  CG  C TYR B 1 118 ? -5.299  -14.283 -11.338 0.25 61.50  ? 118 TYR B CG  1 
ATOM   3957 C  CG  D TYR B 1 118 ? -5.299  -14.283 -11.338 0.25 61.50  ? 118 TYR B CG  1 
ATOM   3958 C  CD1 A TYR B 1 118 ? -6.712  -15.802 -8.956  0.25 33.34  ? 118 TYR B CD1 1 
ATOM   3959 C  CD1 B TYR B 1 118 ? -6.712  -15.802 -8.956  0.25 33.34  ? 118 TYR B CD1 1 
ATOM   3960 C  CD1 C TYR B 1 118 ? -6.683  -14.219 -11.367 0.25 63.80  ? 118 TYR B CD1 1 
ATOM   3961 C  CD1 D TYR B 1 118 ? -6.683  -14.219 -11.367 0.25 63.80  ? 118 TYR B CD1 1 
ATOM   3962 C  CD2 A TYR B 1 118 ? -4.741  -15.059 -10.050 0.25 32.82  ? 118 TYR B CD2 1 
ATOM   3963 C  CD2 B TYR B 1 118 ? -4.741  -15.059 -10.050 0.25 32.82  ? 118 TYR B CD2 1 
ATOM   3964 C  CD2 C TYR B 1 118 ? -4.597  -13.094 -11.483 0.25 62.94  ? 118 TYR B CD2 1 
ATOM   3965 C  CD2 D TYR B 1 118 ? -4.597  -13.094 -11.483 0.25 62.94  ? 118 TYR B CD2 1 
ATOM   3966 C  CE1 A TYR B 1 118 ? -7.410  -14.717 -9.457  0.25 33.70  ? 118 TYR B CE1 1 
ATOM   3967 C  CE1 B TYR B 1 118 ? -7.410  -14.717 -9.457  0.25 33.70  ? 118 TYR B CE1 1 
ATOM   3968 C  CE1 C TYR B 1 118 ? -7.350  -13.015 -11.525 0.25 65.19  ? 118 TYR B CE1 1 
ATOM   3969 C  CE1 D TYR B 1 118 ? -7.350  -13.015 -11.525 0.25 65.19  ? 118 TYR B CE1 1 
ATOM   3970 C  CE2 A TYR B 1 118 ? -5.425  -13.965 -10.555 0.25 32.72  ? 118 TYR B CE2 1 
ATOM   3971 C  CE2 B TYR B 1 118 ? -5.425  -13.965 -10.555 0.25 32.72  ? 118 TYR B CE2 1 
ATOM   3972 C  CE2 C TYR B 1 118 ? -5.248  -11.882 -11.650 0.25 63.04  ? 118 TYR B CE2 1 
ATOM   3973 C  CE2 D TYR B 1 118 ? -5.248  -11.882 -11.650 0.25 63.04  ? 118 TYR B CE2 1 
ATOM   3974 C  CZ  A TYR B 1 118 ? -6.764  -13.794 -10.257 0.25 32.71  ? 118 TYR B CZ  1 
ATOM   3975 C  CZ  B TYR B 1 118 ? -6.764  -13.794 -10.257 0.25 32.71  ? 118 TYR B CZ  1 
ATOM   3976 C  CZ  C TYR B 1 118 ? -6.629  -11.841 -11.669 0.25 64.82  ? 118 TYR B CZ  1 
ATOM   3977 C  CZ  D TYR B 1 118 ? -6.629  -11.841 -11.669 0.25 64.82  ? 118 TYR B CZ  1 
ATOM   3978 O  OH  A TYR B 1 118 ? -7.457  -12.728 -10.750 0.25 32.82  ? 118 TYR B OH  1 
ATOM   3979 O  OH  B TYR B 1 118 ? -7.457  -12.728 -10.750 0.25 32.82  ? 118 TYR B OH  1 
ATOM   3980 O  OH  C TYR B 1 118 ? -7.264  -10.644 -11.829 0.25 67.12  ? 118 TYR B OH  1 
ATOM   3981 O  OH  D TYR B 1 118 ? -7.264  -10.644 -11.829 0.25 67.12  ? 118 TYR B OH  1 
ATOM   3982 N  N   A ASN B 1 119 ? -4.053  -18.536 -5.411  0.25 32.12  ? 119 ASN B N   1 
ATOM   3983 N  N   B ASN B 1 119 ? -4.053  -18.536 -5.411  0.25 32.12  ? 119 ASN B N   1 
ATOM   3984 N  N   C ASN B 1 119 ? -5.354  -18.464 -9.534  0.25 54.46  ? 119 ASN B N   1 
ATOM   3985 N  N   D ASN B 1 119 ? -5.354  -18.464 -9.534  0.25 54.46  ? 119 ASN B N   1 
ATOM   3986 C  CA  A ASN B 1 119 ? -3.556  -19.679 -4.599  0.25 33.04  ? 119 ASN B CA  1 
ATOM   3987 C  CA  B ASN B 1 119 ? -3.556  -19.679 -4.599  0.25 33.04  ? 119 ASN B CA  1 
ATOM   3988 C  CA  C ASN B 1 119 ? -5.343  -19.848 -8.987  0.25 53.25  ? 119 ASN B CA  1 
ATOM   3989 C  CA  D ASN B 1 119 ? -5.343  -19.848 -8.987  0.25 53.25  ? 119 ASN B CA  1 
ATOM   3990 C  C   A ASN B 1 119 ? -2.168  -19.340 -4.037  0.25 32.12  ? 119 ASN B C   1 
ATOM   3991 C  C   B ASN B 1 119 ? -2.168  -19.340 -4.037  0.25 32.12  ? 119 ASN B C   1 
ATOM   3992 C  C   C ASN B 1 119 ? -3.964  -20.167 -8.394  0.25 52.07  ? 119 ASN B C   1 
ATOM   3993 C  C   D ASN B 1 119 ? -3.964  -20.167 -8.394  0.25 52.07  ? 119 ASN B C   1 
ATOM   3994 O  O   A ASN B 1 119 ? -1.293  -20.226 -4.061  0.25 32.00  ? 119 ASN B O   1 
ATOM   3995 O  O   B ASN B 1 119 ? -1.293  -20.226 -4.061  0.25 32.00  ? 119 ASN B O   1 
ATOM   3996 O  O   C ASN B 1 119 ? -3.174  -20.863 -9.065  0.25 51.38  ? 119 ASN B O   1 
ATOM   3997 O  O   D ASN B 1 119 ? -3.174  -20.863 -9.065  0.25 51.38  ? 119 ASN B O   1 
ATOM   3998 C  CB  A ASN B 1 119 ? -3.539  -20.974 -5.420  0.25 34.79  ? 119 ASN B CB  1 
ATOM   3999 C  CB  B ASN B 1 119 ? -3.539  -20.974 -5.420  0.25 34.79  ? 119 ASN B CB  1 
ATOM   4000 C  CB  C ASN B 1 119 ? -5.769  -20.892 -10.022 0.25 53.56  ? 119 ASN B CB  1 
ATOM   4001 C  CB  D ASN B 1 119 ? -5.769  -20.892 -10.022 0.25 53.56  ? 119 ASN B CB  1 
ATOM   4002 C  CG  A ASN B 1 119 ? -4.926  -21.422 -5.836  0.25 35.55  ? 119 ASN B CG  1 
ATOM   4003 C  CG  B ASN B 1 119 ? -4.926  -21.422 -5.836  0.25 35.55  ? 119 ASN B CG  1 
ATOM   4004 C  CG  C ASN B 1 119 ? -5.913  -22.278 -9.424  0.25 53.67  ? 119 ASN B CG  1 
ATOM   4005 C  CG  D ASN B 1 119 ? -5.913  -22.278 -9.424  0.25 53.67  ? 119 ASN B CG  1 
ATOM   4006 O  OD1 A ASN B 1 119 ? -5.099  -22.057 -6.879  0.25 38.03  ? 119 ASN B OD1 1 
ATOM   4007 O  OD1 B ASN B 1 119 ? -5.099  -22.057 -6.879  0.25 38.03  ? 119 ASN B OD1 1 
ATOM   4008 O  OD1 C ASN B 1 119 ? -5.982  -23.270 -10.146 0.25 52.39  ? 119 ASN B OD1 1 
ATOM   4009 O  OD1 D ASN B 1 119 ? -5.982  -23.270 -10.146 0.25 52.39  ? 119 ASN B OD1 1 
ATOM   4010 N  ND2 A ASN B 1 119 ? -5.924  -21.087 -5.030  0.25 35.98  ? 119 ASN B ND2 1 
ATOM   4011 N  ND2 B ASN B 1 119 ? -5.924  -21.087 -5.030  0.25 35.98  ? 119 ASN B ND2 1 
ATOM   4012 N  ND2 C ASN B 1 119 ? -5.959  -22.357 -8.103  0.25 54.11  ? 119 ASN B ND2 1 
ATOM   4013 N  ND2 D ASN B 1 119 ? -5.959  -22.357 -8.103  0.25 54.11  ? 119 ASN B ND2 1 
ATOM   4014 N  N   A GLY B 1 120 ? -1.980  -18.106 -3.552  0.25 30.19  ? 120 GLY B N   1 
ATOM   4015 N  N   B GLY B 1 120 ? -1.980  -18.106 -3.552  0.25 30.19  ? 120 GLY B N   1 
ATOM   4016 N  N   C GLY B 1 120 ? -3.696  -19.663 -7.183  0.25 50.25  ? 120 GLY B N   1 
ATOM   4017 N  N   D GLY B 1 120 ? -3.696  -19.663 -7.183  0.25 50.25  ? 120 GLY B N   1 
ATOM   4018 C  CA  A GLY B 1 120 ? -0.706  -17.620 -2.984  0.25 29.44  ? 120 GLY B CA  1 
ATOM   4019 C  CA  B GLY B 1 120 ? -0.706  -17.620 -2.984  0.25 29.44  ? 120 GLY B CA  1 
ATOM   4020 C  CA  C GLY B 1 120 ? -2.691  -20.218 -6.253  0.25 49.39  ? 120 GLY B CA  1 
ATOM   4021 C  CA  D GLY B 1 120 ? -2.691  -20.218 -6.253  0.25 49.39  ? 120 GLY B CA  1 
ATOM   4022 C  C   A GLY B 1 120 ? 0.405   -17.554 -4.021  0.25 29.34  ? 120 GLY B C   1 
ATOM   4023 C  C   B GLY B 1 120 ? 0.405   -17.554 -4.021  0.25 29.34  ? 120 GLY B C   1 
ATOM   4024 C  C   C GLY B 1 120 ? -1.428  -19.378 -6.138  0.25 47.32  ? 120 GLY B C   1 
ATOM   4025 C  C   D GLY B 1 120 ? -1.428  -19.378 -6.138  0.25 47.32  ? 120 GLY B C   1 
ATOM   4026 O  O   A GLY B 1 120 ? 1.578   -17.464 -3.624  0.25 27.83  ? 120 GLY B O   1 
ATOM   4027 O  O   B GLY B 1 120 ? 1.578   -17.464 -3.624  0.25 27.83  ? 120 GLY B O   1 
ATOM   4028 O  O   C GLY B 1 120 ? -0.873  -19.308 -5.019  0.25 47.03  ? 120 GLY B O   1 
ATOM   4029 O  O   D GLY B 1 120 ? -0.873  -19.308 -5.019  0.25 47.03  ? 120 GLY B O   1 
ATOM   4030 N  N   A SER B 1 121 ? 0.052   -17.581 -5.310  0.25 29.61  ? 121 SER B N   1 
ATOM   4031 N  N   B SER B 1 121 ? 0.052   -17.581 -5.310  0.25 29.61  ? 121 SER B N   1 
ATOM   4032 N  N   C SER B 1 121 ? -0.965  -18.784 -7.242  0.25 44.29  ? 121 SER B N   1 
ATOM   4033 N  N   D SER B 1 121 ? -0.965  -18.784 -7.242  0.25 44.29  ? 121 SER B N   1 
ATOM   4034 C  CA  A SER B 1 121 ? 1.003   -17.599 -6.453  0.25 30.03  ? 121 SER B CA  1 
ATOM   4035 C  CA  B SER B 1 121 ? 1.003   -17.599 -6.453  0.25 30.03  ? 121 SER B CA  1 
ATOM   4036 C  CA  C SER B 1 121 ? 0.369   -18.133 -7.340  0.25 43.91  ? 121 SER B CA  1 
ATOM   4037 C  CA  D SER B 1 121 ? 0.369   -18.133 -7.340  0.25 43.91  ? 121 SER B CA  1 
ATOM   4038 C  C   A SER B 1 121 ? 0.867   -16.324 -7.285  0.25 29.47  ? 121 SER B C   1 
ATOM   4039 C  C   B SER B 1 121 ? 0.867   -16.324 -7.285  0.25 29.47  ? 121 SER B C   1 
ATOM   4040 C  C   C SER B 1 121 ? 0.215   -16.679 -7.772  0.25 41.66  ? 121 SER B C   1 
ATOM   4041 C  C   D SER B 1 121 ? 0.215   -16.679 -7.772  0.25 41.66  ? 121 SER B C   1 
ATOM   4042 O  O   A SER B 1 121 ? -0.132  -16.115 -7.969  0.25 27.15  ? 121 SER B O   1 
ATOM   4043 O  O   B SER B 1 121 ? -0.132  -16.115 -7.969  0.25 27.15  ? 121 SER B O   1 
ATOM   4044 O  O   C SER B 1 121 ? -0.690  -16.339 -8.529  0.25 40.38  ? 121 SER B O   1 
ATOM   4045 O  O   D SER B 1 121 ? -0.690  -16.339 -8.529  0.25 40.38  ? 121 SER B O   1 
ATOM   4046 C  CB  A SER B 1 121 ? 0.797   -18.824 -7.302  0.25 30.68  ? 121 SER B CB  1 
ATOM   4047 C  CB  B SER B 1 121 ? 0.797   -18.824 -7.302  0.25 30.68  ? 121 SER B CB  1 
ATOM   4048 C  CB  C SER B 1 121 ? 1.275   -18.890 -8.282  0.25 43.97  ? 121 SER B CB  1 
ATOM   4049 C  CB  D SER B 1 121 ? 1.275   -18.890 -8.282  0.25 43.97  ? 121 SER B CB  1 
ATOM   4050 O  OG  A SER B 1 121 ? 1.983   -19.141 -8.016  0.25 31.05  ? 121 SER B OG  1 
ATOM   4051 O  OG  B SER B 1 121 ? 1.983   -19.141 -8.016  0.25 31.05  ? 121 SER B OG  1 
ATOM   4052 O  OG  C SER B 1 121 ? 1.283   -18.292 -9.572  0.25 43.83  ? 121 SER B OG  1 
ATOM   4053 O  OG  D SER B 1 121 ? 1.283   -18.292 -9.572  0.25 43.83  ? 121 SER B OG  1 
ATOM   4054 N  N   A PRO B 1 122 ? 1.881   -15.432 -7.257  0.25 31.02  ? 122 PRO B N   1 
ATOM   4055 N  N   B PRO B 1 122 ? 1.881   -15.432 -7.257  0.25 31.02  ? 122 PRO B N   1 
ATOM   4056 N  N   C PRO B 1 122 ? 1.093   -15.771 -7.294  0.25 40.37  ? 122 PRO B N   1 
ATOM   4057 N  N   D PRO B 1 122 ? 1.093   -15.771 -7.294  0.25 40.37  ? 122 PRO B N   1 
ATOM   4058 C  CA  A PRO B 1 122 ? 1.812   -14.168 -7.991  0.25 31.27  ? 122 PRO B CA  1 
ATOM   4059 C  CA  B PRO B 1 122 ? 1.812   -14.168 -7.991  0.25 31.27  ? 122 PRO B CA  1 
ATOM   4060 C  CA  C PRO B 1 122 ? 1.158   -14.418 -7.839  0.25 38.83  ? 122 PRO B CA  1 
ATOM   4061 C  CA  D PRO B 1 122 ? 1.158   -14.418 -7.839  0.25 38.83  ? 122 PRO B CA  1 
ATOM   4062 C  C   A PRO B 1 122 ? 1.555   -14.413 -9.486  0.25 31.72  ? 122 PRO B C   1 
ATOM   4063 C  C   B PRO B 1 122 ? 1.555   -14.413 -9.486  0.25 31.72  ? 122 PRO B C   1 
ATOM   4064 C  C   C PRO B 1 122 ? 1.377   -14.495 -9.359  0.25 36.35  ? 122 PRO B C   1 
ATOM   4065 C  C   D PRO B 1 122 ? 1.377   -14.495 -9.359  0.25 36.35  ? 122 PRO B C   1 
ATOM   4066 O  O   A PRO B 1 122 ? 2.248   -15.238 -10.058 0.25 29.62  ? 122 PRO B O   1 
ATOM   4067 O  O   B PRO B 1 122 ? 2.248   -15.238 -10.058 0.25 29.62  ? 122 PRO B O   1 
ATOM   4068 O  O   C PRO B 1 122 ? 2.223   -15.248 -9.813  0.25 35.09  ? 122 PRO B O   1 
ATOM   4069 O  O   D PRO B 1 122 ? 2.223   -15.248 -9.813  0.25 35.09  ? 122 PRO B O   1 
ATOM   4070 C  CB  A PRO B 1 122 ? 3.198   -13.542 -7.763  0.25 30.63  ? 122 PRO B CB  1 
ATOM   4071 C  CB  B PRO B 1 122 ? 3.198   -13.542 -7.763  0.25 30.63  ? 122 PRO B CB  1 
ATOM   4072 C  CB  C PRO B 1 122 ? 2.315   -13.729 -7.095  0.25 39.47  ? 122 PRO B CB  1 
ATOM   4073 C  CB  D PRO B 1 122 ? 2.315   -13.729 -7.095  0.25 39.47  ? 122 PRO B CB  1 
ATOM   4074 C  CG  A PRO B 1 122 ? 3.708   -14.195 -6.492  0.25 30.71  ? 122 PRO B CG  1 
ATOM   4075 C  CG  B PRO B 1 122 ? 3.708   -14.195 -6.492  0.25 30.71  ? 122 PRO B CG  1 
ATOM   4076 C  CG  C PRO B 1 122 ? 3.025   -14.834 -6.319  0.25 39.44  ? 122 PRO B CG  1 
ATOM   4077 C  CG  D PRO B 1 122 ? 3.025   -14.834 -6.319  0.25 39.44  ? 122 PRO B CG  1 
ATOM   4078 C  CD  A PRO B 1 122 ? 3.141   -15.596 -6.517  0.25 30.19  ? 122 PRO B CD  1 
ATOM   4079 C  CD  B PRO B 1 122 ? 3.141   -15.596 -6.517  0.25 30.19  ? 122 PRO B CD  1 
ATOM   4080 C  CD  C PRO B 1 122 ? 2.051   -15.990 -6.202  0.25 40.94  ? 122 PRO B CD  1 
ATOM   4081 C  CD  D PRO B 1 122 ? 2.051   -15.990 -6.202  0.25 40.94  ? 122 PRO B CD  1 
ATOM   4082 N  N   . SER B 1 123 ? 0.600   -13.701 -10.095 1.00 32.37  ? 123 SER B N   1 
ATOM   4083 C  CA  . SER B 1 123 ? 0.235   -13.956 -11.510 1.00 33.39  ? 123 SER B CA  1 
ATOM   4084 C  C   . SER B 1 123 ? 0.386   -12.730 -12.423 1.00 29.52  ? 123 SER B C   1 
ATOM   4085 O  O   . SER B 1 123 ? 0.621   -12.922 -13.604 1.00 30.31  ? 123 SER B O   1 
ATOM   4086 C  CB  . SER B 1 123 ? -1.162  -14.470 -11.511 1.00 37.06  ? 123 SER B CB  1 
ATOM   4087 O  OG  . SER B 1 123 ? -1.420  -15.184 -12.700 1.00 52.24  ? 123 SER B OG  1 
ATOM   4088 N  N   . GLY B 1 124 ? 0.194   -11.518 -11.915 1.00 27.51  ? 124 GLY B N   1 
ATOM   4089 C  CA  . GLY B 1 124 ? 0.263   -10.295 -12.720 1.00 24.93  ? 124 GLY B CA  1 
ATOM   4090 C  C   . GLY B 1 124 ? 0.552   -9.107  -11.835 1.00 23.31  ? 124 GLY B C   1 
ATOM   4091 O  O   . GLY B 1 124 ? 0.316   -9.185  -10.641 1.00 24.61  ? 124 GLY B O   1 
ATOM   4092 N  N   A VAL B 1 125 ? 1.125   -8.057  -12.424 0.26 23.42  ? 125 VAL B N   1 
ATOM   4093 N  N   B VAL B 1 125 ? 1.073   -8.025  -12.417 0.24 22.66  ? 125 VAL B N   1 
ATOM   4094 N  N   C VAL B 1 125 ? 1.127   -8.059  -12.427 0.26 23.49  ? 125 VAL B N   1 
ATOM   4095 N  N   D VAL B 1 125 ? 1.070   -8.024  -12.419 0.24 22.73  ? 125 VAL B N   1 
ATOM   4096 C  CA  A VAL B 1 125 ? 1.349   -6.735  -11.778 0.26 23.68  ? 125 VAL B CA  1 
ATOM   4097 C  CA  B VAL B 1 125 ? 1.338   -6.742  -11.706 0.24 22.45  ? 125 VAL B CA  1 
ATOM   4098 C  CA  C VAL B 1 125 ? 1.352   -6.734  -11.789 0.26 23.87  ? 125 VAL B CA  1 
ATOM   4099 C  CA  D VAL B 1 125 ? 1.335   -6.738  -11.712 0.24 22.63  ? 125 VAL B CA  1 
ATOM   4100 C  C   A VAL B 1 125 ? 0.664   -5.687  -12.654 0.26 23.69  ? 125 VAL B C   1 
ATOM   4101 C  C   B VAL B 1 125 ? 0.867   -5.595  -12.603 0.24 23.00  ? 125 VAL B C   1 
ATOM   4102 C  C   C VAL B 1 125 ? 0.687   -5.685  -12.680 0.26 24.17  ? 125 VAL B C   1 
ATOM   4103 C  C   D VAL B 1 125 ? 0.867   -5.591  -12.613 0.24 23.48  ? 125 VAL B C   1 
ATOM   4104 O  O   A VAL B 1 125 ? 0.714   -5.813  -13.897 0.26 22.83  ? 125 VAL B O   1 
ATOM   4105 O  O   B VAL B 1 125 ? 1.254   -5.552  -13.791 0.24 22.43  ? 125 VAL B O   1 
ATOM   4106 O  O   C VAL B 1 125 ? 0.780   -5.790  -13.917 0.26 23.16  ? 125 VAL B O   1 
ATOM   4107 O  O   D VAL B 1 125 ? 1.277   -5.537  -13.791 0.24 22.75  ? 125 VAL B O   1 
ATOM   4108 C  CB  A VAL B 1 125 ? 2.846   -6.418  -11.595 0.26 24.78  ? 125 VAL B CB  1 
ATOM   4109 C  CB  B VAL B 1 125 ? 2.821   -6.592  -11.311 0.24 22.46  ? 125 VAL B CB  1 
ATOM   4110 C  CB  C VAL B 1 125 ? 2.848   -6.419  -11.597 0.26 24.85  ? 125 VAL B CB  1 
ATOM   4111 C  CB  D VAL B 1 125 ? 2.817   -6.592  -11.314 0.24 22.52  ? 125 VAL B CB  1 
ATOM   4112 C  CG1 A VAL B 1 125 ? 3.057   -5.292  -10.597 0.26 24.82  ? 125 VAL B CG1 1 
ATOM   4113 C  CG1 B VAL B 1 125 ? 3.732   -6.453  -12.522 0.24 22.15  ? 125 VAL B CG1 1 
ATOM   4114 C  CG1 C VAL B 1 125 ? 3.056   -5.295  -10.596 0.26 24.86  ? 125 VAL B CG1 1 
ATOM   4115 C  CG1 D VAL B 1 125 ? 3.733   -6.456  -12.521 0.24 22.18  ? 125 VAL B CG1 1 
ATOM   4116 C  CG2 A VAL B 1 125 ? 3.645   -7.642  -11.184 0.26 25.73  ? 125 VAL B CG2 1 
ATOM   4117 C  CG2 B VAL B 1 125 ? 3.030   -5.430  -10.354 0.24 22.34  ? 125 VAL B CG2 1 
ATOM   4118 C  CG2 C VAL B 1 125 ? 3.646   -7.645  -11.185 0.26 25.77  ? 125 VAL B CG2 1 
ATOM   4119 C  CG2 D VAL B 1 125 ? 3.029   -5.432  -10.356 0.24 22.37  ? 125 VAL B CG2 1 
ATOM   4120 N  N   A TYR B 1 126 ? 0.032   -4.694  -12.031 0.25 23.83  ? 126 TYR B N   1 
ATOM   4121 N  N   B TYR B 1 126 ? 0.055   -4.698  -12.043 0.25 23.58  ? 126 TYR B N   1 
ATOM   4122 N  N   C TYR B 1 126 ? 0.009   -4.719  -12.076 0.25 25.29  ? 126 TYR B N   1 
ATOM   4123 N  N   D TYR B 1 126 ? 0.021   -4.712  -12.083 0.25 25.04  ? 126 TYR B N   1 
ATOM   4124 C  CA  A TYR B 1 126 ? -0.526  -3.528  -12.753 0.25 23.26  ? 126 TYR B CA  1 
ATOM   4125 C  CA  B TYR B 1 126 ? -0.514  -3.532  -12.762 0.25 23.16  ? 126 TYR B CA  1 
ATOM   4126 C  CA  C TYR B 1 126 ? -0.479  -3.515  -12.789 0.25 25.23  ? 126 TYR B CA  1 
ATOM   4127 C  CA  D TYR B 1 126 ? -0.473  -3.514  -12.799 0.25 25.13  ? 126 TYR B CA  1 
ATOM   4128 C  C   A TYR B 1 126 ? -0.552  -2.335  -11.803 0.25 23.34  ? 126 TYR B C   1 
ATOM   4129 C  C   B TYR B 1 126 ? -0.546  -2.339  -11.808 0.25 23.30  ? 126 TYR B C   1 
ATOM   4130 C  C   C TYR B 1 126 ? -0.425  -2.342  -11.817 0.25 24.42  ? 126 TYR B C   1 
ATOM   4131 C  C   D TYR B 1 126 ? -0.426  -2.344  -11.822 0.25 24.38  ? 126 TYR B C   1 
ATOM   4132 O  O   A TYR B 1 126 ? -0.612  -2.553  -10.580 0.25 22.68  ? 126 TYR B O   1 
ATOM   4133 O  O   B TYR B 1 126 ? -0.610  -2.561  -10.586 0.25 22.66  ? 126 TYR B O   1 
ATOM   4134 O  O   C TYR B 1 126 ? -0.309  -2.586  -10.600 0.25 23.32  ? 126 TYR B O   1 
ATOM   4135 O  O   D TYR B 1 126 ? -0.315  -2.592  -10.606 0.25 23.30  ? 126 TYR B O   1 
ATOM   4136 C  CB  A TYR B 1 126 ? -1.889  -3.877  -13.360 0.25 23.76  ? 126 TYR B CB  1 
ATOM   4137 C  CB  B TYR B 1 126 ? -1.881  -3.882  -13.363 0.25 23.72  ? 126 TYR B CB  1 
ATOM   4138 C  CB  C TYR B 1 126 ? -1.893  -3.740  -13.328 0.25 27.30  ? 126 TYR B CB  1 
ATOM   4139 C  CB  D TYR B 1 126 ? -1.888  -3.742  -13.333 0.25 27.25  ? 126 TYR B CB  1 
ATOM   4140 C  CG  A TYR B 1 126 ? -2.942  -4.374  -12.399 0.25 23.90  ? 126 TYR B CG  1 
ATOM   4141 C  CG  B TYR B 1 126 ? -2.934  -4.375  -12.400 0.25 23.88  ? 126 TYR B CG  1 
ATOM   4142 C  CG  C TYR B 1 126 ? -2.910  -3.919  -12.233 0.25 29.03  ? 126 TYR B CG  1 
ATOM   4143 C  CG  D TYR B 1 126 ? -2.905  -3.920  -12.237 0.25 29.01  ? 126 TYR B CG  1 
ATOM   4144 C  CD1 A TYR B 1 126 ? -3.782  -3.487  -11.747 0.25 23.71  ? 126 TYR B CD1 1 
ATOM   4145 C  CD1 B TYR B 1 126 ? -3.776  -3.487  -11.749 0.25 23.70  ? 126 TYR B CD1 1 
ATOM   4146 C  CD1 C TYR B 1 126 ? -3.184  -5.172  -11.711 0.25 29.89  ? 126 TYR B CD1 1 
ATOM   4147 C  CD1 D TYR B 1 126 ? -3.181  -5.172  -11.715 0.25 29.88  ? 126 TYR B CD1 1 
ATOM   4148 C  CD2 A TYR B 1 126 ? -3.134  -5.729  -12.179 0.25 23.83  ? 126 TYR B CD2 1 
ATOM   4149 C  CD2 B TYR B 1 126 ? -3.129  -5.731  -12.178 0.25 23.82  ? 126 TYR B CD2 1 
ATOM   4150 C  CD2 C TYR B 1 126 ? -3.552  -2.827  -11.676 0.25 30.00  ? 126 TYR B CD2 1 
ATOM   4151 C  CD2 D TYR B 1 126 ? -3.547  -2.827  -11.680 0.25 29.99  ? 126 TYR B CD2 1 
ATOM   4152 C  CE1 A TYR B 1 126 ? -4.764  -3.928  -10.877 0.25 23.91  ? 126 TYR B CE1 1 
ATOM   4153 C  CE1 B TYR B 1 126 ? -4.759  -3.927  -10.880 0.25 23.91  ? 126 TYR B CE1 1 
ATOM   4154 C  CE1 C TYR B 1 126 ? -4.096  -5.338  -10.683 0.25 30.02  ? 126 TYR B CE1 1 
ATOM   4155 C  CE1 D TYR B 1 126 ? -4.093  -5.338  -10.687 0.25 30.01  ? 126 TYR B CE1 1 
ATOM   4156 C  CE2 A TYR B 1 126 ? -4.114  -6.188  -11.312 0.25 23.50  ? 126 TYR B CE2 1 
ATOM   4157 C  CE2 B TYR B 1 126 ? -4.109  -6.188  -11.311 0.25 23.50  ? 126 TYR B CE2 1 
ATOM   4158 C  CE2 C TYR B 1 126 ? -4.463  -2.973  -10.646 0.25 30.15  ? 126 TYR B CE2 1 
ATOM   4159 C  CE2 D TYR B 1 126 ? -4.458  -2.973  -10.649 0.25 30.14  ? 126 TYR B CE2 1 
ATOM   4160 C  CZ  A TYR B 1 126 ? -4.930  -5.284  -10.658 0.25 23.77  ? 126 TYR B CZ  1 
ATOM   4161 C  CZ  B TYR B 1 126 ? -4.925  -5.283  -10.659 0.25 23.77  ? 126 TYR B CZ  1 
ATOM   4162 C  CZ  C TYR B 1 126 ? -4.738  -4.235  -10.150 0.25 30.98  ? 126 TYR B CZ  1 
ATOM   4163 C  CZ  D TYR B 1 126 ? -4.735  -4.234  -10.154 0.25 30.98  ? 126 TYR B CZ  1 
ATOM   4164 O  OH  A TYR B 1 126 ? -5.900  -5.735  -9.811  0.25 24.42  ? 126 TYR B OH  1 
ATOM   4165 O  OH  B TYR B 1 126 ? -5.896  -5.732  -9.813  0.25 24.42  ? 126 TYR B OH  1 
ATOM   4166 O  OH  C TYR B 1 126 ? -5.641  -4.386  -9.138  0.25 31.45  ? 126 TYR B OH  1 
ATOM   4167 O  OH  D TYR B 1 126 ? -5.637  -4.385  -9.141  0.25 31.45  ? 126 TYR B OH  1 
ATOM   4168 N  N   . GLN B 1 127 ? -0.456  -1.128  -12.368 1.00 22.54  ? 127 GLN B N   1 
ATOM   4169 C  CA  . GLN B 1 127 ? -0.474  0.138   -11.611 1.00 25.49  ? 127 GLN B CA  1 
ATOM   4170 C  C   . GLN B 1 127 ? -1.950  0.544   -11.535 1.00 27.11  ? 127 GLN B C   1 
ATOM   4171 O  O   . GLN B 1 127 ? -2.698  0.339   -12.505 1.00 27.31  ? 127 GLN B O   1 
ATOM   4172 C  CB  . GLN B 1 127 ? 0.395   1.139   -12.384 1.00 27.11  ? 127 GLN B CB  1 
ATOM   4173 C  CG  . GLN B 1 127 ? 0.722   2.432   -11.664 1.00 28.96  ? 127 GLN B CG  1 
ATOM   4174 C  CD  . GLN B 1 127 ? 1.640   2.321   -10.482 1.00 27.22  ? 127 GLN B CD  1 
ATOM   4175 O  OE1 . GLN B 1 127 ? 2.070   1.236   -10.060 1.00 26.44  ? 127 GLN B OE1 1 
ATOM   4176 N  NE2 . GLN B 1 127 ? 1.911   3.480   -9.909  1.00 29.63  ? 127 GLN B NE2 1 
ATOM   4177 N  N   A CYS B 1 128 ? -2.367  1.038   -10.359 0.27 26.94  ? 128 CYS B N   1 
ATOM   4178 N  N   B CYS B 1 128 ? -2.362  1.146   -10.428 0.23 26.41  ? 128 CYS B N   1 
ATOM   4179 N  N   C CYS B 1 128 ? -2.368  1.034   -10.359 0.27 26.94  ? 128 CYS B N   1 
ATOM   4180 N  N   D CYS B 1 128 ? -2.362  1.146   -10.428 0.23 26.41  ? 128 CYS B N   1 
ATOM   4181 C  CA  A CYS B 1 128 ? -3.740  1.527   -10.041 0.27 26.96  ? 128 CYS B CA  1 
ATOM   4182 C  CA  B CYS B 1 128 ? -3.732  1.686   -10.306 0.23 25.95  ? 128 CYS B CA  1 
ATOM   4183 C  CA  C CYS B 1 128 ? -3.735  1.535   -10.044 0.27 26.96  ? 128 CYS B CA  1 
ATOM   4184 C  CA  D CYS B 1 128 ? -3.732  1.686   -10.306 0.23 25.95  ? 128 CYS B CA  1 
ATOM   4185 C  C   A CYS B 1 128 ? -3.641  2.927   -9.426  0.27 26.19  ? 128 CYS B C   1 
ATOM   4186 C  C   B CYS B 1 128 ? -3.749  2.822   -9.293  0.23 25.81  ? 128 CYS B C   1 
ATOM   4187 C  C   C CYS B 1 128 ? -3.637  2.935   -9.430  0.27 26.19  ? 128 CYS B C   1 
ATOM   4188 C  C   D CYS B 1 128 ? -3.749  2.822   -9.293  0.23 25.81  ? 128 CYS B C   1 
ATOM   4189 O  O   A CYS B 1 128 ? -2.538  3.282   -8.983  0.27 25.86  ? 128 CYS B O   1 
ATOM   4190 O  O   B CYS B 1 128 ? -2.882  2.856   -8.406  0.23 25.62  ? 128 CYS B O   1 
ATOM   4191 O  O   C CYS B 1 128 ? -2.534  3.292   -8.990  0.27 25.86  ? 128 CYS B O   1 
ATOM   4192 O  O   D CYS B 1 128 ? -2.882  2.856   -8.406  0.23 25.62  ? 128 CYS B O   1 
ATOM   4193 C  CB  A CYS B 1 128 ? -4.439  0.625   -9.026  0.27 27.27  ? 128 CYS B CB  1 
ATOM   4194 C  CB  B CYS B 1 128 ? -4.713  0.604   -9.885  0.23 25.81  ? 128 CYS B CB  1 
ATOM   4195 C  CB  C CYS B 1 128 ? -4.446  0.644   -9.030  0.27 27.27  ? 128 CYS B CB  1 
ATOM   4196 C  CB  D CYS B 1 128 ? -4.713  0.604   -9.885  0.23 25.81  ? 128 CYS B CB  1 
ATOM   4197 S  SG  A CYS B 1 128 ? -5.418  -0.718  -9.755  0.27 30.18  ? 128 CYS B SG  1 
ATOM   4198 S  SG  B CYS B 1 128 ? -4.499  0.119   -8.158  0.23 25.17  ? 128 CYS B SG  1 
ATOM   4199 S  SG  C CYS B 1 128 ? -5.401  -0.718  -9.753  0.27 30.18  ? 128 CYS B SG  1 
ATOM   4200 S  SG  D CYS B 1 128 ? -4.499  0.119   -8.158  0.23 25.17  ? 128 CYS B SG  1 
ATOM   4201 N  N   . ALA B 1 129 ? -4.742  3.692   -9.431  1.00 26.49  ? 129 ALA B N   1 
ATOM   4202 C  CA  . ALA B 1 129 ? -4.967  4.817   -8.511  1.00 26.12  ? 129 ALA B CA  1 
ATOM   4203 C  C   . ALA B 1 129 ? -6.125  4.389   -7.587  1.00 25.27  ? 129 ALA B C   1 
ATOM   4204 O  O   . ALA B 1 129 ? -7.052  3.709   -8.047  1.00 28.76  ? 129 ALA B O   1 
ATOM   4205 C  CB  . ALA B 1 129 ? -5.260  6.058   -9.304  1.00 28.00  ? 129 ALA B CB  1 
ATOM   4206 N  N   . MET B 1 130 ? -6.030  4.757   -6.315  1.00 26.13  ? 130 MET B N   1 
ATOM   4207 C  CA  . MET B 1 130 ? -7.150  4.827   -5.346  1.00 26.88  ? 130 MET B CA  1 
ATOM   4208 C  C   . MET B 1 130 ? -8.088  5.941   -5.845  1.00 25.76  ? 130 MET B C   1 
ATOM   4209 O  O   . MET B 1 130 ? -7.634  7.110   -5.884  1.00 24.61  ? 130 MET B O   1 
ATOM   4210 C  CB  . MET B 1 130 ? -6.590  5.148   -3.953  1.00 26.55  ? 130 MET B CB  1 
ATOM   4211 C  CG  . MET B 1 130 ? -7.612  5.282   -2.814  1.00 26.12  ? 130 MET B CG  1 
ATOM   4212 S  SD  . MET B 1 130 ? -8.584  3.790   -2.612  1.00 31.67  ? 130 MET B SD  1 
ATOM   4213 C  CE  . MET B 1 130 ? -7.297  2.690   -2.020  1.00 31.00  ? 130 MET B CE  1 
ATOM   4214 N  N   . ARG B 1 131 ? -9.291  5.578   -6.292  1.00 25.48  ? 131 ARG B N   1 
ATOM   4215 C  CA  . ARG B 1 131 ? -10.271 6.523   -6.890  1.00 26.22  ? 131 ARG B CA  1 
ATOM   4216 C  C   . ARG B 1 131 ? -10.737 7.483   -5.798  1.00 25.42  ? 131 ARG B C   1 
ATOM   4217 O  O   . ARG B 1 131 ? -10.681 7.151   -4.620  1.00 21.43  ? 131 ARG B O   1 
ATOM   4218 C  CB  . ARG B 1 131 ? -11.468 5.793   -7.503  1.00 27.80  ? 131 ARG B CB  1 
ATOM   4219 C  CG  . ARG B 1 131 ? -11.151 4.874   -8.680  1.00 29.72  ? 131 ARG B CG  1 
ATOM   4220 C  CD  . ARG B 1 131 ? -10.358 5.473   -9.827  1.00 28.21  ? 131 ARG B CD  1 
ATOM   4221 N  NE  . ARG B 1 131 ? -10.959 6.689   -10.361 1.00 27.31  ? 131 ARG B NE  1 
ATOM   4222 C  CZ  . ARG B 1 131 ? -10.339 7.551   -11.163 1.00 28.52  ? 131 ARG B CZ  1 
ATOM   4223 N  NH1 . ARG B 1 131 ? -9.100  7.317   -11.567 1.00 27.13  ? 131 ARG B NH1 1 
ATOM   4224 N  NH2 . ARG B 1 131 ? -10.944 8.666   -11.538 1.00 27.52  ? 131 ARG B NH2 1 
ATOM   4225 N  N   . PRO B 1 132 ? -11.198 8.713   -6.146  1.00 28.61  ? 132 PRO B N   1 
ATOM   4226 C  CA  . PRO B 1 132 ? -11.918 9.571   -5.200  1.00 26.97  ? 132 PRO B CA  1 
ATOM   4227 C  C   . PRO B 1 132 ? -13.063 8.878   -4.457  1.00 24.41  ? 132 PRO B C   1 
ATOM   4228 O  O   . PRO B 1 132 ? -13.185 9.168   -3.316  1.00 25.37  ? 132 PRO B O   1 
ATOM   4229 C  CB  . PRO B 1 132 ? -12.424 10.726  -6.076  1.00 29.08  ? 132 PRO B CB  1 
ATOM   4230 C  CG  . PRO B 1 132 ? -11.343 10.813  -7.154  1.00 28.19  ? 132 PRO B CG  1 
ATOM   4231 C  CD  . PRO B 1 132 ? -11.012 9.367   -7.454  1.00 27.34  ? 132 PRO B CD  1 
ATOM   4232 N  N   . ASN B 1 133 ? -13.775 7.932   -5.071  1.00 24.04  ? 133 ASN B N   1 
ATOM   4233 C  CA  . ASN B 1 133 ? -14.840 7.140   -4.399  1.00 24.64  ? 133 ASN B CA  1 
ATOM   4234 C  C   . ASN B 1 133 ? -14.272 5.910   -3.667  1.00 27.08  ? 133 ASN B C   1 
ATOM   4235 O  O   . ASN B 1 133 ? -15.079 5.010   -3.346  1.00 27.88  ? 133 ASN B O   1 
ATOM   4236 C  CB  . ASN B 1 133 ? -15.921 6.695   -5.378  1.00 24.07  ? 133 ASN B CB  1 
ATOM   4237 C  CG  . ASN B 1 133 ? -15.486 5.606   -6.331  1.00 26.83  ? 133 ASN B CG  1 
ATOM   4238 O  OD1 . ASN B 1 133 ? -14.352 5.136   -6.290  1.00 29.37  ? 133 ASN B OD1 1 
ATOM   4239 N  ND2 . ASN B 1 133 ? -16.384 5.207   -7.214  1.00 28.11  ? 133 ASN B ND2 1 
ATOM   4240 N  N   . PHE B 1 134 ? -12.950 5.827   -3.464  1.00 25.46  ? 134 PHE B N   1 
ATOM   4241 C  CA  . PHE B 1 134 ? -12.261 4.805   -2.628  1.00 27.32  ? 134 PHE B CA  1 
ATOM   4242 C  C   . PHE B 1 134 ? -12.358 3.389   -3.214  1.00 27.27  ? 134 PHE B C   1 
ATOM   4243 O  O   . PHE B 1 134 ? -12.077 2.426   -2.512  1.00 30.04  ? 134 PHE B O   1 
ATOM   4244 C  CB  . PHE B 1 134 ? -12.803 4.796   -1.197  1.00 27.10  ? 134 PHE B CB  1 
ATOM   4245 C  CG  . PHE B 1 134 ? -12.450 6.032   -0.408  1.00 28.49  ? 134 PHE B CG  1 
ATOM   4246 C  CD1 . PHE B 1 134 ? -11.138 6.279   -0.016  1.00 28.55  ? 134 PHE B CD1 1 
ATOM   4247 C  CD2 . PHE B 1 134 ? -13.415 6.984   -0.123  1.00 27.63  ? 134 PHE B CD2 1 
ATOM   4248 C  CE1 . PHE B 1 134 ? -10.817 7.432   0.691   1.00 29.84  ? 134 PHE B CE1 1 
ATOM   4249 C  CE2 . PHE B 1 134 ? -13.091 8.139   0.574   1.00 30.04  ? 134 PHE B CE2 1 
ATOM   4250 C  CZ  . PHE B 1 134 ? -11.794 8.362   0.983   1.00 28.55  ? 134 PHE B CZ  1 
ATOM   4251 N  N   . THR B 1 135 ? -12.704 3.234   -4.475  1.00 29.63  ? 135 THR B N   1 
ATOM   4252 C  CA  . THR B 1 135 ? -12.584 1.915   -5.156  1.00 29.74  ? 135 THR B CA  1 
ATOM   4253 C  C   . THR B 1 135 ? -11.303 1.954   -5.976  1.00 31.52  ? 135 THR B C   1 
ATOM   4254 O  O   . THR B 1 135 ? -10.668 3.036   -6.074  1.00 30.94  ? 135 THR B O   1 
ATOM   4255 C  CB  . THR B 1 135 ? -13.805 1.655   -6.036  1.00 29.19  ? 135 THR B CB  1 
ATOM   4256 O  OG1 . THR B 1 135 ? -13.785 2.626   -7.086  1.00 27.42  ? 135 THR B OG1 1 
ATOM   4257 C  CG2 . THR B 1 135 ? -15.099 1.761   -5.258  1.00 29.35  ? 135 THR B CG2 1 
ATOM   4258 N  N   A ILE B 1 136 ? -10.930 0.816   -6.561  0.25 31.84  ? 136 ILE B N   1 
ATOM   4259 N  N   B ILE B 1 136 ? -10.930 0.816   -6.561  0.25 31.84  ? 136 ILE B N   1 
ATOM   4260 N  N   C ILE B 1 136 ? -10.905 0.809   -6.532  0.25 31.89  ? 136 ILE B N   1 
ATOM   4261 N  N   D ILE B 1 136 ? -10.905 0.809   -6.532  0.25 31.89  ? 136 ILE B N   1 
ATOM   4262 C  CA  A ILE B 1 136 ? -9.860  0.734   -7.597  0.25 34.44  ? 136 ILE B CA  1 
ATOM   4263 C  CA  B ILE B 1 136 ? -9.860  0.734   -7.597  0.25 34.44  ? 136 ILE B CA  1 
ATOM   4264 C  CA  C ILE B 1 136 ? -9.875  0.745   -7.609  0.25 34.49  ? 136 ILE B CA  1 
ATOM   4265 C  CA  D ILE B 1 136 ? -9.875  0.745   -7.609  0.25 34.49  ? 136 ILE B CA  1 
ATOM   4266 C  C   A ILE B 1 136 ? -10.383 -0.085  -8.784  0.25 35.83  ? 136 ILE B C   1 
ATOM   4267 C  C   B ILE B 1 136 ? -10.383 -0.085  -8.784  0.25 35.83  ? 136 ILE B C   1 
ATOM   4268 C  C   C ILE B 1 136 ? -10.440 -0.047  -8.793  0.25 35.79  ? 136 ILE B C   1 
ATOM   4269 C  C   D ILE B 1 136 ? -10.440 -0.047  -8.793  0.25 35.79  ? 136 ILE B C   1 
ATOM   4270 O  O   A ILE B 1 136 ? -11.147 -1.056  -8.559  0.25 35.50  ? 136 ILE B O   1 
ATOM   4271 O  O   B ILE B 1 136 ? -11.147 -1.056  -8.559  0.25 35.50  ? 136 ILE B O   1 
ATOM   4272 O  O   C ILE B 1 136 ? -11.296 -0.940  -8.581  0.25 35.13  ? 136 ILE B O   1 
ATOM   4273 O  O   D ILE B 1 136 ? -11.296 -0.940  -8.581  0.25 35.13  ? 136 ILE B O   1 
ATOM   4274 C  CB  A ILE B 1 136 ? -8.543  0.171   -7.019  0.25 35.18  ? 136 ILE B CB  1 
ATOM   4275 C  CB  B ILE B 1 136 ? -8.543  0.171   -7.019  0.25 35.18  ? 136 ILE B CB  1 
ATOM   4276 C  CB  C ILE B 1 136 ? -8.520  0.191   -7.113  0.25 35.37  ? 136 ILE B CB  1 
ATOM   4277 C  CB  D ILE B 1 136 ? -8.520  0.191   -7.113  0.25 35.37  ? 136 ILE B CB  1 
ATOM   4278 C  CG1 A ILE B 1 136 ? -8.624  -1.326  -6.727  0.25 35.39  ? 136 ILE B CG1 1 
ATOM   4279 C  CG1 B ILE B 1 136 ? -8.624  -1.326  -6.727  0.25 35.39  ? 136 ILE B CG1 1 
ATOM   4280 C  CG1 C ILE B 1 136 ? -8.633  -1.159  -6.404  0.25 35.40  ? 136 ILE B CG1 1 
ATOM   4281 C  CG1 D ILE B 1 136 ? -8.633  -1.159  -6.404  0.25 35.40  ? 136 ILE B CG1 1 
ATOM   4282 C  CG2 A ILE B 1 136 ? -8.102  0.957   -5.791  0.25 34.43  ? 136 ILE B CG2 1 
ATOM   4283 C  CG2 B ILE B 1 136 ? -8.102  0.957   -5.791  0.25 34.43  ? 136 ILE B CG2 1 
ATOM   4284 C  CG2 C ILE B 1 136 ? -7.811  1.214   -6.236  0.25 34.77  ? 136 ILE B CG2 1 
ATOM   4285 C  CG2 D ILE B 1 136 ? -7.811  1.214   -6.236  0.25 34.77  ? 136 ILE B CG2 1 
ATOM   4286 C  CD1 A ILE B 1 136 ? -7.277  -1.951  -6.442  0.25 36.26  ? 136 ILE B CD1 1 
ATOM   4287 C  CD1 B ILE B 1 136 ? -7.277  -1.951  -6.442  0.25 36.26  ? 136 ILE B CD1 1 
ATOM   4288 C  CD1 C ILE B 1 136 ? -7.318  -1.909  -6.362  0.25 36.33  ? 136 ILE B CD1 1 
ATOM   4289 C  CD1 D ILE B 1 136 ? -7.318  -1.909  -6.362  0.25 36.33  ? 136 ILE B CD1 1 
ATOM   4290 N  N   . LYS B 1 137 ? -10.006 0.323   -9.999  1.00 35.80  ? 137 LYS B N   1 
ATOM   4291 C  CA  . LYS B 1 137 ? -10.358 -0.377  -11.255 1.00 40.57  ? 137 LYS B CA  1 
ATOM   4292 C  C   . LYS B 1 137 ? -9.230  -1.384  -11.456 1.00 39.04  ? 137 LYS B C   1 
ATOM   4293 O  O   . LYS B 1 137 ? -8.326  -1.135  -12.248 1.00 39.23  ? 137 LYS B O   1 
ATOM   4294 C  CB  . LYS B 1 137 ? -10.525 0.664   -12.367 1.00 46.41  ? 137 LYS B CB  1 
ATOM   4295 C  CG  . LYS B 1 137 ? -11.668 1.640   -12.114 1.00 54.12  ? 137 LYS B CG  1 
ATOM   4296 C  CD  . LYS B 1 137 ? -11.656 2.869   -12.986 1.00 59.83  ? 137 LYS B CD  1 
ATOM   4297 C  CE  . LYS B 1 137 ? -12.793 3.806   -12.649 1.00 65.85  ? 137 LYS B CE  1 
ATOM   4298 N  NZ  . LYS B 1 137 ? -13.034 4.773   -13.744 1.00 69.30  ? 137 LYS B NZ  1 
ATOM   4299 N  N   A GLY B 1 138 ? -9.330  -2.530  -10.780 0.25 37.21  ? 138 GLY B N   1 
ATOM   4300 N  N   B GLY B 1 138 ? -9.330  -2.530  -10.780 0.25 37.21  ? 138 GLY B N   1 
ATOM   4301 N  N   C GLY B 1 138 ? -9.234  -2.446  -10.645 0.25 43.54  ? 138 GLY B N   1 
ATOM   4302 N  N   D GLY B 1 138 ? -9.234  -2.446  -10.645 0.25 43.54  ? 138 GLY B N   1 
ATOM   4303 C  CA  A GLY B 1 138 ? -8.351  -3.628  -10.875 0.25 36.93  ? 138 GLY B CA  1 
ATOM   4304 C  CA  B GLY B 1 138 ? -8.351  -3.628  -10.875 0.25 36.93  ? 138 GLY B CA  1 
ATOM   4305 C  CA  C GLY B 1 138 ? -8.116  -3.403  -10.533 0.25 47.97  ? 138 GLY B CA  1 
ATOM   4306 C  CA  D GLY B 1 138 ? -8.116  -3.403  -10.533 0.25 47.97  ? 138 GLY B CA  1 
ATOM   4307 C  C   A GLY B 1 138 ? -8.790  -4.686  -11.869 0.25 35.29  ? 138 GLY B C   1 
ATOM   4308 C  C   B GLY B 1 138 ? -8.790  -4.686  -11.869 0.25 35.29  ? 138 GLY B C   1 
ATOM   4309 C  C   C GLY B 1 138 ? -8.033  -4.302  -11.750 0.25 50.60  ? 138 GLY B C   1 
ATOM   4310 C  C   D GLY B 1 138 ? -8.033  -4.302  -11.750 0.25 50.60  ? 138 GLY B C   1 
ATOM   4311 O  O   A GLY B 1 138 ? -9.803  -4.467  -12.569 0.25 35.88  ? 138 GLY B O   1 
ATOM   4312 O  O   B GLY B 1 138 ? -9.803  -4.467  -12.569 0.25 35.88  ? 138 GLY B O   1 
ATOM   4313 O  O   C GLY B 1 138 ? -7.223  -4.012  -12.637 0.25 54.48  ? 138 GLY B O   1 
ATOM   4314 O  O   D GLY B 1 138 ? -7.223  -4.012  -12.637 0.25 54.48  ? 138 GLY B O   1 
ATOM   4315 N  N   A SER B 1 139 ? -8.031  -5.780  -11.941 0.25 33.10  ? 139 SER B N   1 
ATOM   4316 N  N   B SER B 1 139 ? -8.031  -5.780  -11.941 0.25 33.10  ? 139 SER B N   1 
ATOM   4317 N  N   C SER B 1 139 ? -8.845  -5.360  -11.768 0.25 54.10  ? 139 SER B N   1 
ATOM   4318 N  N   D SER B 1 139 ? -8.845  -5.360  -11.768 0.25 54.10  ? 139 SER B N   1 
ATOM   4319 C  CA  A SER B 1 139 ? -8.412  -7.048  -12.610 0.25 33.65  ? 139 SER B CA  1 
ATOM   4320 C  CA  B SER B 1 139 ? -8.412  -7.048  -12.610 0.25 33.65  ? 139 SER B CA  1 
ATOM   4321 C  CA  C SER B 1 139 ? -9.013  -6.331  -12.881 0.25 58.21  ? 139 SER B CA  1 
ATOM   4322 C  CA  D SER B 1 139 ? -9.013  -6.331  -12.881 0.25 58.21  ? 139 SER B CA  1 
ATOM   4323 C  C   A SER B 1 139 ? -8.225  -8.180  -11.600 0.25 35.47  ? 139 SER B C   1 
ATOM   4324 C  C   B SER B 1 139 ? -8.225  -8.180  -11.600 0.25 35.47  ? 139 SER B C   1 
ATOM   4325 C  C   C SER B 1 139 ? -8.828  -7.743  -12.327 0.25 62.81  ? 139 SER B C   1 
ATOM   4326 C  C   D SER B 1 139 ? -8.828  -7.743  -12.327 0.25 62.81  ? 139 SER B C   1 
ATOM   4327 O  O   A SER B 1 139 ? -7.059  -8.470  -11.243 0.25 32.87  ? 139 SER B O   1 
ATOM   4328 O  O   B SER B 1 139 ? -7.059  -8.470  -11.243 0.25 32.87  ? 139 SER B O   1 
ATOM   4329 O  O   C SER B 1 139 ? -7.698  -8.270  -12.428 0.25 62.51  ? 139 SER B O   1 
ATOM   4330 O  O   D SER B 1 139 ? -7.698  -8.270  -12.428 0.25 62.51  ? 139 SER B O   1 
ATOM   4331 C  CB  A SER B 1 139 ? -7.625  -7.292  -13.864 0.25 32.98  ? 139 SER B CB  1 
ATOM   4332 C  CB  B SER B 1 139 ? -7.625  -7.292  -13.864 0.25 32.98  ? 139 SER B CB  1 
ATOM   4333 C  CB  C SER B 1 139 ? -8.064  -6.084  -14.022 0.25 58.72  ? 139 SER B CB  1 
ATOM   4334 C  CB  D SER B 1 139 ? -8.064  -6.084  -14.022 0.25 58.72  ? 139 SER B CB  1 
ATOM   4335 O  OG  A SER B 1 139 ? -7.914  -8.578  -14.388 0.25 32.44  ? 139 SER B OG  1 
ATOM   4336 O  OG  B SER B 1 139 ? -7.914  -8.578  -14.388 0.25 32.44  ? 139 SER B OG  1 
ATOM   4337 O  OG  C SER B 1 139 ? -8.021  -7.222  -14.872 0.25 57.42  ? 139 SER B OG  1 
ATOM   4338 O  OG  D SER B 1 139 ? -8.021  -7.222  -14.872 0.25 57.42  ? 139 SER B OG  1 
ATOM   4339 N  N   A PHE B 1 140 ? -9.344  -8.748  -11.133 0.25 36.29  ? 140 PHE B N   1 
ATOM   4340 N  N   B PHE B 1 140 ? -9.344  -8.748  -11.133 0.25 36.29  ? 140 PHE B N   1 
ATOM   4341 N  N   C PHE B 1 140 ? -9.893  -8.312  -11.753 0.25 67.07  ? 140 PHE B N   1 
ATOM   4342 N  N   D PHE B 1 140 ? -9.893  -8.312  -11.753 0.25 67.07  ? 140 PHE B N   1 
ATOM   4343 C  CA  A PHE B 1 140 ? -9.409  -9.758  -10.045 0.25 37.51  ? 140 PHE B CA  1 
ATOM   4344 C  CA  B PHE B 1 140 ? -9.409  -9.758  -10.045 0.25 37.51  ? 140 PHE B CA  1 
ATOM   4345 C  CA  C PHE B 1 140 ? -9.889  -9.654  -11.114 0.25 72.25  ? 140 PHE B CA  1 
ATOM   4346 C  CA  D PHE B 1 140 ? -9.889  -9.654  -11.114 0.25 72.25  ? 140 PHE B CA  1 
ATOM   4347 C  C   A PHE B 1 140 ? -10.486 -10.802 -10.350 0.25 38.81  ? 140 PHE B C   1 
ATOM   4348 C  C   B PHE B 1 140 ? -10.486 -10.802 -10.350 0.25 38.81  ? 140 PHE B C   1 
ATOM   4349 C  C   C PHE B 1 140 ? -11.170 -10.424 -11.439 0.25 75.18  ? 140 PHE B C   1 
ATOM   4350 C  C   D PHE B 1 140 ? -11.170 -10.424 -11.439 0.25 75.18  ? 140 PHE B C   1 
ATOM   4351 O  O   A PHE B 1 140 ? -11.674 -10.430 -10.419 0.25 38.39  ? 140 PHE B O   1 
ATOM   4352 O  O   B PHE B 1 140 ? -11.674 -10.430 -10.419 0.25 38.39  ? 140 PHE B O   1 
ATOM   4353 O  O   C PHE B 1 140 ? -12.274 -9.917  -11.160 0.25 75.01  ? 140 PHE B O   1 
ATOM   4354 O  O   D PHE B 1 140 ? -12.274 -9.917  -11.160 0.25 75.01  ? 140 PHE B O   1 
ATOM   4355 C  CB  A PHE B 1 140 ? -9.767  -9.107  -8.706  0.25 37.59  ? 140 PHE B CB  1 
ATOM   4356 C  CB  B PHE B 1 140 ? -9.767  -9.107  -8.706  0.25 37.59  ? 140 PHE B CB  1 
ATOM   4357 C  CB  C PHE B 1 140 ? -9.779  -9.546  -9.593  0.25 73.60  ? 140 PHE B CB  1 
ATOM   4358 C  CB  D PHE B 1 140 ? -9.779  -9.546  -9.593  0.25 73.60  ? 140 PHE B CB  1 
ATOM   4359 C  CG  A PHE B 1 140 ? -8.720  -8.188  -8.128  0.25 36.15  ? 140 PHE B CG  1 
ATOM   4360 C  CG  B PHE B 1 140 ? -8.720  -8.188  -8.128  0.25 36.15  ? 140 PHE B CG  1 
ATOM   4361 C  CG  C PHE B 1 140 ? -8.606  -8.738  -9.104  0.25 74.01  ? 140 PHE B CG  1 
ATOM   4362 C  CG  D PHE B 1 140 ? -8.606  -8.738  -9.104  0.25 74.01  ? 140 PHE B CG  1 
ATOM   4363 C  CD1 A PHE B 1 140 ? -7.464  -8.668  -7.792  0.25 35.63  ? 140 PHE B CD1 1 
ATOM   4364 C  CD1 B PHE B 1 140 ? -7.464  -8.668  -7.792  0.25 35.63  ? 140 PHE B CD1 1 
ATOM   4365 C  CD1 C PHE B 1 140 ? -8.759  -7.405  -8.762  0.25 73.34  ? 140 PHE B CD1 1 
ATOM   4366 C  CD1 D PHE B 1 140 ? -8.759  -7.405  -8.762  0.25 73.34  ? 140 PHE B CD1 1 
ATOM   4367 C  CD2 A PHE B 1 140 ? -9.004  -6.852  -7.892  0.25 35.62  ? 140 PHE B CD2 1 
ATOM   4368 C  CD2 B PHE B 1 140 ? -9.004  -6.852  -7.892  0.25 35.62  ? 140 PHE B CD2 1 
ATOM   4369 C  CD2 C PHE B 1 140 ? -7.352  -9.314  -8.988  0.25 72.93  ? 140 PHE B CD2 1 
ATOM   4370 C  CD2 D PHE B 1 140 ? -7.352  -9.314  -8.988  0.25 72.93  ? 140 PHE B CD2 1 
ATOM   4371 C  CE1 A PHE B 1 140 ? -6.506  -7.823  -7.255  0.25 35.69  ? 140 PHE B CE1 1 
ATOM   4372 C  CE1 B PHE B 1 140 ? -6.506  -7.823  -7.255  0.25 35.69  ? 140 PHE B CE1 1 
ATOM   4373 C  CE1 C PHE B 1 140 ? -7.678  -6.663  -8.314  0.25 73.15  ? 140 PHE B CE1 1 
ATOM   4374 C  CE1 D PHE B 1 140 ? -7.678  -6.663  -8.314  0.25 73.15  ? 140 PHE B CE1 1 
ATOM   4375 C  CE2 A PHE B 1 140 ? -8.045  -6.009  -7.351  0.25 35.88  ? 140 PHE B CE2 1 
ATOM   4376 C  CE2 B PHE B 1 140 ? -8.045  -6.009  -7.351  0.25 35.88  ? 140 PHE B CE2 1 
ATOM   4377 C  CE2 C PHE B 1 140 ? -6.273  -8.570  -8.539  0.25 71.52  ? 140 PHE B CE2 1 
ATOM   4378 C  CE2 D PHE B 1 140 ? -6.273  -8.570  -8.539  0.25 71.52  ? 140 PHE B CE2 1 
ATOM   4379 C  CZ  A PHE B 1 140 ? -6.799  -6.496  -7.035  0.25 35.65  ? 140 PHE B CZ  1 
ATOM   4380 C  CZ  B PHE B 1 140 ? -6.799  -6.496  -7.035  0.25 35.65  ? 140 PHE B CZ  1 
ATOM   4381 C  CZ  C PHE B 1 140 ? -6.439  -7.247  -8.204  0.25 71.77  ? 140 PHE B CZ  1 
ATOM   4382 C  CZ  D PHE B 1 140 ? -6.439  -7.247  -8.204  0.25 71.77  ? 140 PHE B CZ  1 
ATOM   4383 N  N   A LEU B 1 141 ? -10.079 -12.065 -10.503 0.25 39.17  ? 141 LEU B N   1 
ATOM   4384 N  N   B LEU B 1 141 ? -10.079 -12.065 -10.503 0.25 39.17  ? 141 LEU B N   1 
ATOM   4385 N  N   C LEU B 1 141 ? -10.999 -11.642 -11.960 0.25 78.84  ? 141 LEU B N   1 
ATOM   4386 N  N   D LEU B 1 141 ? -10.999 -11.642 -11.960 0.25 78.84  ? 141 LEU B N   1 
ATOM   4387 C  CA  A LEU B 1 141 ? -10.996 -13.233 -10.533 0.25 40.80  ? 141 LEU B CA  1 
ATOM   4388 C  CA  B LEU B 1 141 ? -10.996 -13.233 -10.533 0.25 40.80  ? 141 LEU B CA  1 
ATOM   4389 C  CA  C LEU B 1 141 ? -12.078 -12.613 -12.285 0.25 80.42  ? 141 LEU B CA  1 
ATOM   4390 C  CA  D LEU B 1 141 ? -12.078 -12.613 -12.285 0.25 80.42  ? 141 LEU B CA  1 
ATOM   4391 C  C   A LEU B 1 141 ? -10.970 -13.898 -9.150  0.25 40.84  ? 141 LEU B C   1 
ATOM   4392 C  C   B LEU B 1 141 ? -10.970 -13.898 -9.150  0.25 40.84  ? 141 LEU B C   1 
ATOM   4393 C  C   C LEU B 1 141 ? -12.168 -13.660 -11.163 0.25 83.10  ? 141 LEU B C   1 
ATOM   4394 C  C   D LEU B 1 141 ? -12.168 -13.660 -11.163 0.25 83.10  ? 141 LEU B C   1 
ATOM   4395 O  O   A LEU B 1 141 ? -10.214 -13.425 -8.285  0.25 40.00  ? 141 LEU B O   1 
ATOM   4396 O  O   B LEU B 1 141 ? -10.214 -13.425 -8.285  0.25 40.00  ? 141 LEU B O   1 
ATOM   4397 O  O   C LEU B 1 141 ? -11.466 -13.489 -10.141 0.25 84.45  ? 141 LEU B O   1 
ATOM   4398 O  O   D LEU B 1 141 ? -11.466 -13.489 -10.141 0.25 84.45  ? 141 LEU B O   1 
ATOM   4399 C  CB  A LEU B 1 141 ? -10.565 -14.199 -11.644 0.25 41.20  ? 141 LEU B CB  1 
ATOM   4400 C  CB  B LEU B 1 141 ? -10.565 -14.199 -11.644 0.25 41.20  ? 141 LEU B CB  1 
ATOM   4401 C  CB  C LEU B 1 141 ? -11.739 -13.247 -13.637 0.25 78.94  ? 141 LEU B CB  1 
ATOM   4402 C  CB  D LEU B 1 141 ? -11.739 -13.247 -13.637 0.25 78.94  ? 141 LEU B CB  1 
ATOM   4403 C  CG  A LEU B 1 141 ? -10.328 -13.572 -13.019 0.25 41.32  ? 141 LEU B CG  1 
ATOM   4404 C  CG  B LEU B 1 141 ? -10.328 -13.572 -13.019 0.25 41.32  ? 141 LEU B CG  1 
ATOM   4405 C  CG  C LEU B 1 141 ? -11.793 -12.308 -14.846 0.25 78.07  ? 141 LEU B CG  1 
ATOM   4406 C  CG  D LEU B 1 141 ? -11.793 -12.308 -14.846 0.25 78.07  ? 141 LEU B CG  1 
ATOM   4407 C  CD1 A LEU B 1 141 ? -9.933  -14.634 -14.032 0.25 41.73  ? 141 LEU B CD1 1 
ATOM   4408 C  CD1 B LEU B 1 141 ? -9.933  -14.634 -14.032 0.25 41.73  ? 141 LEU B CD1 1 
ATOM   4409 C  CD1 C LEU B 1 141 ? -13.226 -11.920 -15.177 0.25 78.34  ? 141 LEU B CD1 1 
ATOM   4410 C  CD1 D LEU B 1 141 ? -13.226 -11.920 -15.177 0.25 78.34  ? 141 LEU B CD1 1 
ATOM   4411 C  CD2 A LEU B 1 141 ? -11.554 -12.811 -13.500 0.25 41.39  ? 141 LEU B CD2 1 
ATOM   4412 C  CD2 B LEU B 1 141 ? -11.554 -12.811 -13.500 0.25 41.39  ? 141 LEU B CD2 1 
ATOM   4413 C  CD2 C LEU B 1 141 ? -10.933 -11.065 -14.638 0.25 75.64  ? 141 LEU B CD2 1 
ATOM   4414 C  CD2 D LEU B 1 141 ? -10.933 -11.065 -14.638 0.25 75.64  ? 141 LEU B CD2 1 
ATOM   4415 N  N   A ASN B 1 142 ? -11.771 -14.947 -8.952  0.25 41.63  ? 142 ASN B N   1 
ATOM   4416 N  N   B ASN B 1 142 ? -11.771 -14.947 -8.952  0.25 41.63  ? 142 ASN B N   1 
ATOM   4417 N  N   C ASN B 1 142 ? -13.011 -14.687 -11.333 0.25 83.26  ? 142 ASN B N   1 
ATOM   4418 N  N   D ASN B 1 142 ? -13.011 -14.687 -11.333 0.25 83.26  ? 142 ASN B N   1 
ATOM   4419 C  CA  A ASN B 1 142 ? -11.886 -15.690 -7.668  0.25 42.53  ? 142 ASN B CA  1 
ATOM   4420 C  CA  B ASN B 1 142 ? -11.886 -15.690 -7.668  0.25 42.53  ? 142 ASN B CA  1 
ATOM   4421 C  CA  C ASN B 1 142 ? -13.111 -15.849 -10.405 0.25 82.20  ? 142 ASN B CA  1 
ATOM   4422 C  CA  D ASN B 1 142 ? -13.111 -15.849 -10.405 0.25 82.20  ? 142 ASN B CA  1 
ATOM   4423 C  C   A ASN B 1 142 ? -10.510 -16.173 -7.211  0.25 40.96  ? 142 ASN B C   1 
ATOM   4424 C  C   B ASN B 1 142 ? -10.510 -16.173 -7.211  0.25 40.96  ? 142 ASN B C   1 
ATOM   4425 C  C   C ASN B 1 142 ? -11.970 -16.822 -10.727 0.25 79.04  ? 142 ASN B C   1 
ATOM   4426 C  C   D ASN B 1 142 ? -11.970 -16.822 -10.727 0.25 79.04  ? 142 ASN B C   1 
ATOM   4427 O  O   A ASN B 1 142 ? -9.753  -16.695 -8.055  0.25 42.55  ? 142 ASN B O   1 
ATOM   4428 O  O   B ASN B 1 142 ? -9.753  -16.695 -8.055  0.25 42.55  ? 142 ASN B O   1 
ATOM   4429 O  O   C ASN B 1 142 ? -11.765 -17.116 -11.922 0.25 76.93  ? 142 ASN B O   1 
ATOM   4430 O  O   D ASN B 1 142 ? -11.765 -17.116 -11.922 0.25 76.93  ? 142 ASN B O   1 
ATOM   4431 C  CB  A ASN B 1 142 ? -12.824 -16.891 -7.790  0.25 44.80  ? 142 ASN B CB  1 
ATOM   4432 C  CB  B ASN B 1 142 ? -12.824 -16.891 -7.790  0.25 44.80  ? 142 ASN B CB  1 
ATOM   4433 C  CB  C ASN B 1 142 ? -14.479 -16.533 -10.469 0.25 83.40  ? 142 ASN B CB  1 
ATOM   4434 C  CB  D ASN B 1 142 ? -14.479 -16.533 -10.469 0.25 83.40  ? 142 ASN B CB  1 
ATOM   4435 C  CG  A ASN B 1 142 ? -14.271 -16.472 -7.937  0.25 47.24  ? 142 ASN B CG  1 
ATOM   4436 C  CG  B ASN B 1 142 ? -14.271 -16.472 -7.937  0.25 47.24  ? 142 ASN B CG  1 
ATOM   4437 C  CG  C ASN B 1 142 ? -14.647 -17.616 -9.421  0.25 85.60  ? 142 ASN B CG  1 
ATOM   4438 C  CG  D ASN B 1 142 ? -14.647 -17.616 -9.421  0.25 85.60  ? 142 ASN B CG  1 
ATOM   4439 O  OD1 A ASN B 1 142 ? -14.673 -15.440 -7.399  0.25 47.73  ? 142 ASN B OD1 1 
ATOM   4440 O  OD1 B ASN B 1 142 ? -14.673 -15.440 -7.399  0.25 47.73  ? 142 ASN B OD1 1 
ATOM   4441 O  OD1 C ASN B 1 142 ? -13.721 -18.386 -9.161  0.25 85.83  ? 142 ASN B OD1 1 
ATOM   4442 O  OD1 D ASN B 1 142 ? -13.721 -18.386 -9.161  0.25 85.83  ? 142 ASN B OD1 1 
ATOM   4443 N  ND2 A ASN B 1 142 ? -15.059 -17.262 -8.653  0.25 49.38  ? 142 ASN B ND2 1 
ATOM   4444 N  ND2 B ASN B 1 142 ? -15.059 -17.262 -8.653  0.25 49.38  ? 142 ASN B ND2 1 
ATOM   4445 N  ND2 C ASN B 1 142 ? -15.826 -17.693 -8.824  0.25 84.01  ? 142 ASN B ND2 1 
ATOM   4446 N  ND2 D ASN B 1 142 ? -15.826 -17.693 -8.824  0.25 84.01  ? 142 ASN B ND2 1 
ATOM   4447 N  N   A GLY B 1 143 ? -10.231 -16.043 -5.910  0.25 38.40  ? 143 GLY B N   1 
ATOM   4448 N  N   B GLY B 1 143 ? -10.231 -16.043 -5.910  0.25 38.40  ? 143 GLY B N   1 
ATOM   4449 N  N   C GLY B 1 143 ? -11.282 -17.310 -9.689  0.25 75.93  ? 143 GLY B N   1 
ATOM   4450 N  N   D GLY B 1 143 ? -11.282 -17.310 -9.689  0.25 75.93  ? 143 GLY B N   1 
ATOM   4451 C  CA  A GLY B 1 143 ? -8.954  -16.443 -5.293  0.25 35.30  ? 143 GLY B CA  1 
ATOM   4452 C  CA  B GLY B 1 143 ? -8.954  -16.443 -5.293  0.25 35.30  ? 143 GLY B CA  1 
ATOM   4453 C  CA  C GLY B 1 143 ? -9.930  -17.894 -9.780  0.25 72.44  ? 143 GLY B CA  1 
ATOM   4454 C  CA  D GLY B 1 143 ? -9.930  -17.894 -9.780  0.25 72.44  ? 143 GLY B CA  1 
ATOM   4455 C  C   A GLY B 1 143 ? -7.957  -15.299 -5.289  0.25 32.66  ? 143 GLY B C   1 
ATOM   4456 C  C   B GLY B 1 143 ? -7.957  -15.299 -5.289  0.25 32.66  ? 143 GLY B C   1 
ATOM   4457 C  C   C GLY B 1 143 ? -8.896  -16.861 -9.363  0.25 70.22  ? 143 GLY B C   1 
ATOM   4458 C  C   D GLY B 1 143 ? -8.896  -16.861 -9.363  0.25 70.22  ? 143 GLY B C   1 
ATOM   4459 O  O   A GLY B 1 143 ? -6.852  -15.499 -4.766  0.25 33.22  ? 143 GLY B O   1 
ATOM   4460 O  O   B GLY B 1 143 ? -6.852  -15.499 -4.766  0.25 33.22  ? 143 GLY B O   1 
ATOM   4461 O  O   C GLY B 1 143 ? -7.697  -17.206 -9.302  0.25 68.64  ? 143 GLY B O   1 
ATOM   4462 O  O   D GLY B 1 143 ? -7.697  -17.206 -9.302  0.25 68.64  ? 143 GLY B O   1 
ATOM   4463 N  N   A SER B 1 144 ? -8.337  -14.148 -5.858  0.25 30.44  ? 144 SER B N   1 
ATOM   4464 N  N   B SER B 1 144 ? -8.337  -14.148 -5.858  0.25 30.44  ? 144 SER B N   1 
ATOM   4465 N  N   C SER B 1 144 ? -9.365  -15.634 -9.098  0.25 66.67  ? 144 SER B N   1 
ATOM   4466 N  N   D SER B 1 144 ? -9.365  -15.634 -9.098  0.25 66.67  ? 144 SER B N   1 
ATOM   4467 C  CA  A SER B 1 144 ? -7.518  -12.905 -5.910  0.25 28.91  ? 144 SER B CA  1 
ATOM   4468 C  CA  B SER B 1 144 ? -7.518  -12.905 -5.910  0.25 28.91  ? 144 SER B CA  1 
ATOM   4469 C  CA  C SER B 1 144 ? -8.585  -14.487 -8.558  0.25 63.91  ? 144 SER B CA  1 
ATOM   4470 C  CA  D SER B 1 144 ? -8.585  -14.487 -8.558  0.25 63.91  ? 144 SER B CA  1 
ATOM   4471 C  C   A SER B 1 144 ? -7.476  -12.255 -4.524  0.25 27.62  ? 144 SER B C   1 
ATOM   4472 C  C   B SER B 1 144 ? -7.476  -12.255 -4.524  0.25 27.62  ? 144 SER B C   1 
ATOM   4473 C  C   C SER B 1 144 ? -8.348  -14.691 -7.058  0.25 61.08  ? 144 SER B C   1 
ATOM   4474 C  C   D SER B 1 144 ? -8.348  -14.691 -7.058  0.25 61.08  ? 144 SER B C   1 
ATOM   4475 O  O   A SER B 1 144 ? -6.469  -11.604 -4.214  0.25 27.96  ? 144 SER B O   1 
ATOM   4476 O  O   B SER B 1 144 ? -6.469  -11.604 -4.214  0.25 27.96  ? 144 SER B O   1 
ATOM   4477 O  O   C SER B 1 144 ? -9.311  -14.538 -6.279  0.25 59.77  ? 144 SER B O   1 
ATOM   4478 O  O   D SER B 1 144 ? -9.311  -14.538 -6.279  0.25 59.77  ? 144 SER B O   1 
ATOM   4479 C  CB  A SER B 1 144 ? -8.029  -11.945 -6.952  0.25 27.46  ? 144 SER B CB  1 
ATOM   4480 C  CB  B SER B 1 144 ? -8.029  -11.945 -6.952  0.25 27.46  ? 144 SER B CB  1 
ATOM   4481 C  CB  C SER B 1 144 ? -9.285  -13.181 -8.817  0.25 64.29  ? 144 SER B CB  1 
ATOM   4482 C  CB  D SER B 1 144 ? -9.285  -13.181 -8.817  0.25 64.29  ? 144 SER B CB  1 
ATOM   4483 O  OG  A SER B 1 144 ? -9.262  -11.371 -6.559  0.25 26.83  ? 144 SER B OG  1 
ATOM   4484 O  OG  B SER B 1 144 ? -9.262  -11.371 -6.559  0.25 26.83  ? 144 SER B OG  1 
ATOM   4485 O  OG  C SER B 1 144 ? -8.948  -12.227 -7.817  0.25 64.75  ? 144 SER B OG  1 
ATOM   4486 O  OG  D SER B 1 144 ? -8.948  -12.227 -7.817  0.25 64.75  ? 144 SER B OG  1 
ATOM   4487 N  N   A CYS B 1 145 ? -8.525  -12.437 -3.718  0.25 26.75  ? 145 CYS B N   1 
ATOM   4488 N  N   B CYS B 1 145 ? -8.525  -12.437 -3.718  0.25 26.75  ? 145 CYS B N   1 
ATOM   4489 N  N   C CYS B 1 145 ? -7.103  -14.999 -6.685  0.25 57.50  ? 145 CYS B N   1 
ATOM   4490 N  N   D CYS B 1 145 ? -7.103  -14.999 -6.685  0.25 57.50  ? 145 CYS B N   1 
ATOM   4491 C  CA  A CYS B 1 145 ? -8.644  -11.840 -2.362  0.25 25.95  ? 145 CYS B CA  1 
ATOM   4492 C  CA  B CYS B 1 145 ? -8.644  -11.840 -2.362  0.25 25.95  ? 145 CYS B CA  1 
ATOM   4493 C  CA  C CYS B 1 145 ? -6.698  -15.520 -5.352  0.25 55.62  ? 145 CYS B CA  1 
ATOM   4494 C  CA  D CYS B 1 145 ? -6.698  -15.520 -5.352  0.25 55.62  ? 145 CYS B CA  1 
ATOM   4495 C  C   A CYS B 1 145 ? -7.333  -12.050 -1.596  0.25 23.94  ? 145 CYS B C   1 
ATOM   4496 C  C   B CYS B 1 145 ? -7.333  -12.050 -1.596  0.25 23.94  ? 145 CYS B C   1 
ATOM   4497 C  C   C CYS B 1 145 ? -6.393  -14.356 -4.396  0.25 52.73  ? 145 CYS B C   1 
ATOM   4498 C  C   D CYS B 1 145 ? -6.393  -14.356 -4.396  0.25 52.73  ? 145 CYS B C   1 
ATOM   4499 O  O   A CYS B 1 145 ? -6.788  -13.172 -1.642  0.25 24.49  ? 145 CYS B O   1 
ATOM   4500 O  O   B CYS B 1 145 ? -6.788  -13.172 -1.642  0.25 24.49  ? 145 CYS B O   1 
ATOM   4501 O  O   C CYS B 1 145 ? -6.026  -14.620 -3.228  0.25 51.38  ? 145 CYS B O   1 
ATOM   4502 O  O   D CYS B 1 145 ? -6.026  -14.620 -3.228  0.25 51.38  ? 145 CYS B O   1 
ATOM   4503 C  CB  A CYS B 1 145 ? -9.819  -12.439 -1.604  0.25 27.00  ? 145 CYS B CB  1 
ATOM   4504 C  CB  B CYS B 1 145 ? -9.819  -12.439 -1.604  0.25 27.00  ? 145 CYS B CB  1 
ATOM   4505 C  CB  C CYS B 1 145 ? -5.528  -16.483 -5.533  0.25 56.03  ? 145 CYS B CB  1 
ATOM   4506 C  CB  D CYS B 1 145 ? -5.528  -16.483 -5.533  0.25 56.03  ? 145 CYS B CB  1 
ATOM   4507 S  SG  A CYS B 1 145 ? -11.389 -12.252 -2.484  0.25 30.45  ? 145 CYS B SG  1 
ATOM   4508 S  SG  B CYS B 1 145 ? -11.389 -12.252 -2.484  0.25 30.45  ? 145 CYS B SG  1 
ATOM   4509 S  SG  C CYS B 1 145 ? -4.148  -16.217 -4.392  0.25 61.54  ? 145 CYS B SG  1 
ATOM   4510 S  SG  D CYS B 1 145 ? -4.148  -16.217 -4.392  0.25 61.54  ? 145 CYS B SG  1 
ATOM   4511 N  N   A GLY B 1 146 ? -6.835  -11.001 -0.940  0.25 22.13  ? 146 GLY B N   1 
ATOM   4512 N  N   B GLY B 1 146 ? -6.835  -11.001 -0.940  0.25 22.13  ? 146 GLY B N   1 
ATOM   4513 N  N   C GLY B 1 146 ? -6.581  -13.116 -4.863  0.25 48.46  ? 146 GLY B N   1 
ATOM   4514 N  N   D GLY B 1 146 ? -6.581  -13.116 -4.863  0.25 48.46  ? 146 GLY B N   1 
ATOM   4515 C  CA  A GLY B 1 146 ? -5.585  -11.048 -0.168  0.25 20.91  ? 146 GLY B CA  1 
ATOM   4516 C  CA  B GLY B 1 146 ? -5.585  -11.048 -0.168  0.25 20.91  ? 146 GLY B CA  1 
ATOM   4517 C  CA  C GLY B 1 146 ? -6.369  -11.886 -4.075  0.25 44.91  ? 146 GLY B CA  1 
ATOM   4518 C  CA  D GLY B 1 146 ? -6.369  -11.886 -4.075  0.25 44.91  ? 146 GLY B CA  1 
ATOM   4519 C  C   A GLY B 1 146 ? -4.392  -10.565 -0.972  0.25 20.20  ? 146 GLY B C   1 
ATOM   4520 C  C   B GLY B 1 146 ? -4.392  -10.565 -0.972  0.25 20.20  ? 146 GLY B C   1 
ATOM   4521 C  C   C GLY B 1 146 ? -5.359  -10.952 -4.725  0.25 42.13  ? 146 GLY B C   1 
ATOM   4522 C  C   D GLY B 1 146 ? -5.359  -10.952 -4.725  0.25 42.13  ? 146 GLY B C   1 
ATOM   4523 O  O   A GLY B 1 146 ? -3.319  -10.410 -0.360  0.25 18.18  ? 146 GLY B O   1 
ATOM   4524 O  O   B GLY B 1 146 ? -3.319  -10.410 -0.360  0.25 18.18  ? 146 GLY B O   1 
ATOM   4525 O  O   C GLY B 1 146 ? -4.952  -11.216 -5.879  0.25 39.00  ? 146 GLY B O   1 
ATOM   4526 O  O   D GLY B 1 146 ? -4.952  -11.216 -5.879  0.25 39.00  ? 146 GLY B O   1 
ATOM   4527 N  N   A SER B 1 147 ? -4.562  -10.386 -2.292  0.25 20.49  ? 147 SER B N   1 
ATOM   4528 N  N   B SER B 1 147 ? -4.562  -10.386 -2.292  0.25 20.49  ? 147 SER B N   1 
ATOM   4529 N  N   C SER B 1 147 ? -4.967  -9.895  -4.008  0.25 39.03  ? 147 SER B N   1 
ATOM   4530 N  N   D SER B 1 147 ? -4.967  -9.895  -4.008  0.25 39.03  ? 147 SER B N   1 
ATOM   4531 C  CA  A SER B 1 147 ? -3.614  -9.678  -3.197  0.25 20.42  ? 147 SER B CA  1 
ATOM   4532 C  CA  B SER B 1 147 ? -3.614  -9.678  -3.197  0.25 20.42  ? 147 SER B CA  1 
ATOM   4533 C  CA  C SER B 1 147 ? -4.050  -8.831  -4.490  0.25 37.42  ? 147 SER B CA  1 
ATOM   4534 C  CA  D SER B 1 147 ? -4.050  -8.831  -4.490  0.25 37.42  ? 147 SER B CA  1 
ATOM   4535 C  C   A SER B 1 147 ? -3.337  -8.289  -2.611  0.25 20.58  ? 147 SER B C   1 
ATOM   4536 C  C   B SER B 1 147 ? -3.337  -8.289  -2.611  0.25 20.58  ? 147 SER B C   1 
ATOM   4537 C  C   C SER B 1 147 ? -3.565  -7.989  -3.307  0.25 35.93  ? 147 SER B C   1 
ATOM   4538 C  C   D SER B 1 147 ? -3.565  -7.989  -3.307  0.25 35.93  ? 147 SER B C   1 
ATOM   4539 O  O   A SER B 1 147 ? -4.260  -7.703  -2.029  0.25 19.52  ? 147 SER B O   1 
ATOM   4540 O  O   B SER B 1 147 ? -4.260  -7.703  -2.029  0.25 19.52  ? 147 SER B O   1 
ATOM   4541 O  O   C SER B 1 147 ? -4.342  -7.782  -2.359  0.25 34.63  ? 147 SER B O   1 
ATOM   4542 O  O   D SER B 1 147 ? -4.342  -7.782  -2.359  0.25 34.63  ? 147 SER B O   1 
ATOM   4543 C  CB  A SER B 1 147 ? -4.152  -9.582  -4.607  0.25 20.38  ? 147 SER B CB  1 
ATOM   4544 C  CB  B SER B 1 147 ? -4.152  -9.582  -4.607  0.25 20.38  ? 147 SER B CB  1 
ATOM   4545 C  CB  C SER B 1 147 ? -4.728  -7.965  -5.511  0.25 38.42  ? 147 SER B CB  1 
ATOM   4546 C  CB  D SER B 1 147 ? -4.728  -7.965  -5.511  0.25 38.42  ? 147 SER B CB  1 
ATOM   4547 O  OG  A SER B 1 147 ? -4.044  -10.825 -5.294  0.25 19.87  ? 147 SER B OG  1 
ATOM   4548 O  OG  B SER B 1 147 ? -4.044  -10.825 -5.294  0.25 19.87  ? 147 SER B OG  1 
ATOM   4549 O  OG  C SER B 1 147 ? -5.261  -6.800  -4.898  0.25 40.66  ? 147 SER B OG  1 
ATOM   4550 O  OG  D SER B 1 147 ? -5.261  -6.800  -4.898  0.25 40.66  ? 147 SER B OG  1 
ATOM   4551 N  N   A VAL B 1 148 ? -2.124  -7.758  -2.755  0.25 21.69  ? 148 VAL B N   1 
ATOM   4552 N  N   B VAL B 1 148 ? -2.124  -7.758  -2.755  0.25 21.69  ? 148 VAL B N   1 
ATOM   4553 N  N   C VAL B 1 148 ? -2.327  -7.499  -3.374  0.25 33.76  ? 148 VAL B N   1 
ATOM   4554 N  N   D VAL B 1 148 ? -2.327  -7.499  -3.374  0.25 33.76  ? 148 VAL B N   1 
ATOM   4555 C  CA  A VAL B 1 148 ? -1.763  -6.479  -2.079  0.25 22.44  ? 148 VAL B CA  1 
ATOM   4556 C  CA  B VAL B 1 148 ? -1.763  -6.479  -2.079  0.25 22.44  ? 148 VAL B CA  1 
ATOM   4557 C  CA  C VAL B 1 148 ? -1.750  -6.576  -2.356  0.25 30.96  ? 148 VAL B CA  1 
ATOM   4558 C  CA  D VAL B 1 148 ? -1.750  -6.576  -2.356  0.25 30.96  ? 148 VAL B CA  1 
ATOM   4559 C  C   A VAL B 1 148 ? -1.256  -5.438  -3.085  0.25 23.74  ? 148 VAL B C   1 
ATOM   4560 C  C   B VAL B 1 148 ? -1.256  -5.438  -3.085  0.25 23.74  ? 148 VAL B C   1 
ATOM   4561 C  C   C VAL B 1 148 ? -1.086  -5.413  -3.096  0.25 28.56  ? 148 VAL B C   1 
ATOM   4562 C  C   D VAL B 1 148 ? -1.086  -5.413  -3.096  0.25 28.56  ? 148 VAL B C   1 
ATOM   4563 O  O   A VAL B 1 148 ? -0.852  -5.806  -4.213  0.25 23.93  ? 148 VAL B O   1 
ATOM   4564 O  O   B VAL B 1 148 ? -0.852  -5.806  -4.213  0.25 23.93  ? 148 VAL B O   1 
ATOM   4565 O  O   C VAL B 1 148 ? -0.354  -5.677  -4.077  0.25 28.20  ? 148 VAL B O   1 
ATOM   4566 O  O   D VAL B 1 148 ? -0.354  -5.677  -4.077  0.25 28.20  ? 148 VAL B O   1 
ATOM   4567 C  CB  A VAL B 1 148 ? -0.752  -6.711  -0.942  0.25 22.91  ? 148 VAL B CB  1 
ATOM   4568 C  CB  B VAL B 1 148 ? -0.752  -6.711  -0.942  0.25 22.91  ? 148 VAL B CB  1 
ATOM   4569 C  CB  C VAL B 1 148 ? -0.761  -7.319  -1.441  0.25 32.22  ? 148 VAL B CB  1 
ATOM   4570 C  CB  D VAL B 1 148 ? -0.761  -7.319  -1.441  0.25 32.22  ? 148 VAL B CB  1 
ATOM   4571 C  CG1 A VAL B 1 148 ? -1.321  -7.642  0.124   0.25 23.01  ? 148 VAL B CG1 1 
ATOM   4572 C  CG1 B VAL B 1 148 ? -1.321  -7.642  0.124   0.25 23.01  ? 148 VAL B CG1 1 
ATOM   4573 C  CG1 C VAL B 1 148 ? -1.325  -8.663  -0.995  0.25 32.79  ? 148 VAL B CG1 1 
ATOM   4574 C  CG1 D VAL B 1 148 ? -1.325  -8.663  -0.995  0.25 32.79  ? 148 VAL B CG1 1 
ATOM   4575 C  CG2 A VAL B 1 148 ? 0.573   -7.230  -1.467  0.25 22.49  ? 148 VAL B CG2 1 
ATOM   4576 C  CG2 B VAL B 1 148 ? 0.573   -7.230  -1.467  0.25 22.49  ? 148 VAL B CG2 1 
ATOM   4577 C  CG2 C VAL B 1 148 ? 0.590   -7.496  -2.108  0.25 32.61  ? 148 VAL B CG2 1 
ATOM   4578 C  CG2 D VAL B 1 148 ? 0.590   -7.496  -2.108  0.25 32.61  ? 148 VAL B CG2 1 
ATOM   4579 N  N   . GLY B 1 149 ? -1.336  -4.179  -2.653  1.00 24.62  ? 149 GLY B N   1 
ATOM   4580 C  CA  . GLY B 1 149 ? -0.853  -2.990  -3.352  1.00 22.89  ? 149 GLY B CA  1 
ATOM   4581 C  C   . GLY B 1 149 ? 0.236   -2.337  -2.530  1.00 22.09  ? 149 GLY B C   1 
ATOM   4582 O  O   . GLY B 1 149 ? 0.206   -2.411  -1.280  1.00 21.11  ? 149 GLY B O   1 
ATOM   4583 N  N   . PHE B 1 150 ? 1.191   -1.741  -3.213  1.00 20.15  ? 150 PHE B N   1 
ATOM   4584 C  CA  . PHE B 1 150 ? 2.459   -1.304  -2.607  1.00 20.82  ? 150 PHE B CA  1 
ATOM   4585 C  C   . PHE B 1 150 ? 3.092   -0.239  -3.491  1.00 21.65  ? 150 PHE B C   1 
ATOM   4586 O  O   . PHE B 1 150 ? 2.767   -0.153  -4.673  1.00 18.17  ? 150 PHE B O   1 
ATOM   4587 C  CB  . PHE B 1 150 ? 3.414   -2.480  -2.433  1.00 20.84  ? 150 PHE B CB  1 
ATOM   4588 C  CG  . PHE B 1 150 ? 3.835   -3.125  -3.721  1.00 19.56  ? 150 PHE B CG  1 
ATOM   4589 C  CD1 . PHE B 1 150 ? 3.048   -4.079  -4.336  1.00 22.12  ? 150 PHE B CD1 1 
ATOM   4590 C  CD2 . PHE B 1 150 ? 5.031   -2.782  -4.320  1.00 22.00  ? 150 PHE B CD2 1 
ATOM   4591 C  CE1 . PHE B 1 150 ? 3.438   -4.660  -5.535  1.00 21.34  ? 150 PHE B CE1 1 
ATOM   4592 C  CE2 . PHE B 1 150 ? 5.426   -3.364  -5.517  1.00 20.16  ? 150 PHE B CE2 1 
ATOM   4593 C  CZ  . PHE B 1 150 ? 4.622   -4.293  -6.128  1.00 20.63  ? 150 PHE B CZ  1 
ATOM   4594 N  N   . ASN B 1 151 ? 3.931   0.561   -2.844  1.00 22.94  ? 151 ASN B N   1 
ATOM   4595 C  CA  . ASN B 1 151 ? 4.906   1.488   -3.449  1.00 24.85  ? 151 ASN B CA  1 
ATOM   4596 C  C   . ASN B 1 151 ? 6.282   1.006   -3.007  1.00 26.18  ? 151 ASN B C   1 
ATOM   4597 O  O   . ASN B 1 151 ? 6.369   0.273   -2.005  1.00 26.52  ? 151 ASN B O   1 
ATOM   4598 C  CB  . ASN B 1 151 ? 4.571   2.929   -3.057  1.00 24.73  ? 151 ASN B CB  1 
ATOM   4599 C  CG  . ASN B 1 151 ? 3.376   3.410   -3.853  1.00 26.61  ? 151 ASN B CG  1 
ATOM   4600 O  OD1 . ASN B 1 151 ? 3.507   3.654   -5.038  1.00 27.52  ? 151 ASN B OD1 1 
ATOM   4601 N  ND2 . ASN B 1 151 ? 2.188   3.431   -3.267  1.00 24.73  ? 151 ASN B ND2 1 
ATOM   4602 N  N   . ILE B 1 152 ? 7.318   1.378   -3.742  1.00 28.21  ? 152 ILE B N   1 
ATOM   4603 C  CA  . ILE B 1 152 ? 8.723   1.202   -3.290  1.00 31.62  ? 152 ILE B CA  1 
ATOM   4604 C  C   . ILE B 1 152 ? 9.373   2.586   -3.265  1.00 36.41  ? 152 ILE B C   1 
ATOM   4605 O  O   . ILE B 1 152 ? 9.189   3.350   -4.240  1.00 35.67  ? 152 ILE B O   1 
ATOM   4606 C  CB  . ILE B 1 152 ? 9.471   0.202   -4.187  1.00 32.90  ? 152 ILE B CB  1 
ATOM   4607 C  CG1 . ILE B 1 152 ? 8.756   -1.152  -4.241  1.00 34.82  ? 152 ILE B CG1 1 
ATOM   4608 C  CG2 . ILE B 1 152 ? 10.911  0.077   -3.726  1.00 32.79  ? 152 ILE B CG2 1 
ATOM   4609 C  CD1 . ILE B 1 152 ? 9.437   -2.200  -5.120  1.00 36.20  ? 152 ILE B CD1 1 
ATOM   4610 N  N   . ASP B 1 153 ? 10.054  2.894   -2.165  1.00 41.24  ? 153 ASP B N   1 
ATOM   4611 C  CA  . ASP B 1 153 ? 10.785  4.166   -1.918  1.00 50.29  ? 153 ASP B CA  1 
ATOM   4612 C  C   . ASP B 1 153 ? 12.212  3.771   -1.528  1.00 56.81  ? 153 ASP B C   1 
ATOM   4613 O  O   . ASP B 1 153 ? 12.448  3.508   -0.331  1.00 68.26  ? 153 ASP B O   1 
ATOM   4614 C  CB  . ASP B 1 153 ? 10.059  5.004   -0.860  1.00 53.55  ? 153 ASP B CB  1 
ATOM   4615 C  CG  . ASP B 1 153 ? 8.604   4.591   -0.649  1.00 62.66  ? 153 ASP B CG  1 
ATOM   4616 O  OD1 . ASP B 1 153 ? 7.751   5.061   -1.418  1.00 62.46  ? 153 ASP B OD1 1 
ATOM   4617 O  OD2 . ASP B 1 153 ? 8.337   3.757   0.266   1.00 69.27  ? 153 ASP B OD2 1 
ATOM   4618 N  N   . TYR B 1 154 ? 13.098  3.652   -2.524  1.00 59.01  ? 154 TYR B N   1 
ATOM   4619 C  CA  . TYR B 1 154 ? 14.490  3.131   -2.431  1.00 59.48  ? 154 TYR B CA  1 
ATOM   4620 C  C   . TYR B 1 154 ? 14.422  1.619   -2.193  1.00 61.71  ? 154 TYR B C   1 
ATOM   4621 O  O   . TYR B 1 154 ? 14.102  0.876   -3.150  1.00 65.41  ? 154 TYR B O   1 
ATOM   4622 C  CB  . TYR B 1 154 ? 15.313  3.921   -1.404  1.00 68.74  ? 154 TYR B CB  1 
ATOM   4623 C  CG  . TYR B 1 154 ? 15.175  5.415   -1.559  1.00 79.22  ? 154 TYR B CG  1 
ATOM   4624 C  CD1 . TYR B 1 154 ? 15.789  6.087   -2.610  1.00 78.62  ? 154 TYR B CD1 1 
ATOM   4625 C  CD2 . TYR B 1 154 ? 14.366  6.148   -0.700  1.00 80.12  ? 154 TYR B CD2 1 
ATOM   4626 C  CE1 . TYR B 1 154 ? 15.623  7.451   -2.790  1.00 77.80  ? 154 TYR B CE1 1 
ATOM   4627 C  CE2 . TYR B 1 154 ? 14.199  7.516   -0.859  1.00 83.19  ? 154 TYR B CE2 1 
ATOM   4628 C  CZ  . TYR B 1 154 ? 14.832  8.168   -1.907  1.00 81.33  ? 154 TYR B CZ  1 
ATOM   4629 O  OH  . TYR B 1 154 ? 14.687  9.512   -2.079  1.00 80.61  ? 154 TYR B OH  1 
ATOM   4630 N  N   . ASP B 1 155 ? 14.698  1.165   -0.972  1.00 54.56  ? 155 ASP B N   1 
ATOM   4631 C  CA  . ASP B 1 155 ? 14.757  -0.287  -0.640  1.00 57.24  ? 155 ASP B CA  1 
ATOM   4632 C  C   . ASP B 1 155 ? 13.494  -0.685  0.141   1.00 48.08  ? 155 ASP B C   1 
ATOM   4633 O  O   . ASP B 1 155 ? 13.289  -1.915  0.347   1.00 46.77  ? 155 ASP B O   1 
ATOM   4634 C  CB  . ASP B 1 155 ? 16.042  -0.604  0.136   1.00 57.75  ? 155 ASP B CB  1 
ATOM   4635 C  CG  . ASP B 1 155 ? 16.255  0.293   1.354   1.00 61.04  ? 155 ASP B CG  1 
ATOM   4636 O  OD1 . ASP B 1 155 ? 15.664  1.419   1.402   1.00 59.00  ? 155 ASP B OD1 1 
ATOM   4637 O  OD2 . ASP B 1 155 ? 16.996  -0.131  2.257   1.00 62.84  ? 155 ASP B OD2 1 
ATOM   4638 N  N   . CYS B 1 156 ? 12.679  0.304   0.539   1.00 38.67  ? 156 CYS B N   1 
ATOM   4639 C  CA  . CYS B 1 156 ? 11.571  0.135   1.509   1.00 34.20  ? 156 CYS B CA  1 
ATOM   4640 C  C   . CYS B 1 156 ? 10.247  -0.073  0.756   1.00 31.54  ? 156 CYS B C   1 
ATOM   4641 O  O   . CYS B 1 156 ? 9.830   0.821   -0.027  1.00 29.01  ? 156 CYS B O   1 
ATOM   4642 C  CB  . CYS B 1 156 ? 11.507  1.319   2.464   1.00 35.47  ? 156 CYS B CB  1 
ATOM   4643 S  SG  . CYS B 1 156 ? 10.106  1.255   3.616   1.00 40.83  ? 156 CYS B SG  1 
ATOM   4644 N  N   . VAL B 1 157 ? 9.615   -1.226  0.964   1.00 26.17  ? 157 VAL B N   1 
ATOM   4645 C  CA  . VAL B 1 157 ? 8.240   -1.495  0.463   1.00 26.26  ? 157 VAL B CA  1 
ATOM   4646 C  C   . VAL B 1 157 ? 7.214   -0.891  1.423   1.00 25.04  ? 157 VAL B C   1 
ATOM   4647 O  O   . VAL B 1 157 ? 7.169   -1.280  2.613   1.00 24.20  ? 157 VAL B O   1 
ATOM   4648 C  CB  . VAL B 1 157 ? 7.949   -2.981  0.230   1.00 26.96  ? 157 VAL B CB  1 
ATOM   4649 C  CG1 . VAL B 1 157 ? 6.524   -3.156  -0.278  1.00 27.16  ? 157 VAL B CG1 1 
ATOM   4650 C  CG2 . VAL B 1 157 ? 8.954   -3.581  -0.738  1.00 28.94  ? 157 VAL B CG2 1 
ATOM   4651 N  N   . SER B 1 158 ? 6.389   -0.001  0.893   1.00 21.25  ? 158 SER B N   1 
ATOM   4652 C  CA  . SER B 1 158 ? 5.230   0.567   1.590   1.00 21.50  ? 158 SER B CA  1 
ATOM   4653 C  C   . SER B 1 158 ? 3.971   -0.167  1.135   1.00 20.22  ? 158 SER B C   1 
ATOM   4654 O  O   . SER B 1 158 ? 3.472   0.136   0.050   1.00 19.78  ? 158 SER B O   1 
ATOM   4655 C  CB  . SER B 1 158 ? 5.170   2.040   1.380   1.00 22.88  ? 158 SER B CB  1 
ATOM   4656 O  OG  . SER B 1 158 ? 6.152   2.637   2.208   1.00 25.15  ? 158 SER B OG  1 
ATOM   4657 N  N   . PHE B 1 159 ? 3.468   -1.076  1.971   1.00 19.69  ? 159 PHE B N   1 
ATOM   4658 C  CA  . PHE B 1 159 ? 2.204   -1.819  1.743   1.00 20.75  ? 159 PHE B CA  1 
ATOM   4659 C  C   . PHE B 1 159 ? 0.997   -0.941  2.105   1.00 22.03  ? 159 PHE B C   1 
ATOM   4660 O  O   . PHE B 1 159 ? 0.925   -0.408  3.234   1.00 22.65  ? 159 PHE B O   1 
ATOM   4661 C  CB  . PHE B 1 159 ? 2.197   -3.093  2.579   1.00 21.45  ? 159 PHE B CB  1 
ATOM   4662 C  CG  . PHE B 1 159 ? 3.203   -4.123  2.139   1.00 20.29  ? 159 PHE B CG  1 
ATOM   4663 C  CD1 . PHE B 1 159 ? 3.007   -4.821  0.969   1.00 22.07  ? 159 PHE B CD1 1 
ATOM   4664 C  CD2 . PHE B 1 159 ? 4.311   -4.434  2.914   1.00 22.87  ? 159 PHE B CD2 1 
ATOM   4665 C  CE1 . PHE B 1 159 ? 3.887   -5.818  0.576   1.00 23.22  ? 159 PHE B CE1 1 
ATOM   4666 C  CE2 . PHE B 1 159 ? 5.204   -5.417  2.515   1.00 21.20  ? 159 PHE B CE2 1 
ATOM   4667 C  CZ  . PHE B 1 159 ? 4.993   -6.099  1.339   1.00 22.02  ? 159 PHE B CZ  1 
ATOM   4668 N  N   . CYS B 1 160 ? 0.087   -0.747  1.148   1.00 22.25  ? 160 CYS B N   1 
ATOM   4669 C  CA  . CYS B 1 160 ? -1.038  0.209   1.309   1.00 24.03  ? 160 CYS B CA  1 
ATOM   4670 C  C   . CYS B 1 160 ? -2.391  -0.457  1.034   1.00 22.41  ? 160 CYS B C   1 
ATOM   4671 O  O   . CYS B 1 160 ? -3.381  0.138   1.416   1.00 22.90  ? 160 CYS B O   1 
ATOM   4672 C  CB  . CYS B 1 160 ? -0.853  1.435   0.424   1.00 23.25  ? 160 CYS B CB  1 
ATOM   4673 S  SG  . CYS B 1 160 ? -0.814  1.015   -1.338  1.00 22.67  ? 160 CYS B SG  1 
ATOM   4674 N  N   . TYR B 1 161 ? -2.455  -1.660  0.455   1.00 22.29  ? 161 TYR B N   1 
ATOM   4675 C  CA  . TYR B 1 161 ? -3.752  -2.230  -0.000  1.00 22.24  ? 161 TYR B CA  1 
ATOM   4676 C  C   . TYR B 1 161 ? -3.792  -3.739  0.138   1.00 21.56  ? 161 TYR B C   1 
ATOM   4677 O  O   . TYR B 1 161 ? -2.821  -4.374  -0.194  1.00 20.36  ? 161 TYR B O   1 
ATOM   4678 C  CB  . TYR B 1 161 ? -4.038  -1.871  -1.460  1.00 22.19  ? 161 TYR B CB  1 
ATOM   4679 C  CG  . TYR B 1 161 ? -5.381  -2.319  -1.975  1.00 22.87  ? 161 TYR B CG  1 
ATOM   4680 C  CD1 . TYR B 1 161 ? -6.551  -1.625  -1.669  1.00 24.88  ? 161 TYR B CD1 1 
ATOM   4681 C  CD2 . TYR B 1 161 ? -5.487  -3.421  -2.813  1.00 23.20  ? 161 TYR B CD2 1 
ATOM   4682 C  CE1 . TYR B 1 161 ? -7.790  -2.047  -2.156  1.00 23.75  ? 161 TYR B CE1 1 
ATOM   4683 C  CE2 . TYR B 1 161 ? -6.707  -3.853  -3.301  1.00 22.08  ? 161 TYR B CE2 1 
ATOM   4684 C  CZ  . TYR B 1 161 ? -7.862  -3.158  -2.979  1.00 22.29  ? 161 TYR B CZ  1 
ATOM   4685 O  OH  . TYR B 1 161 ? -9.060  -3.598  -3.456  1.00 23.23  ? 161 TYR B OH  1 
ATOM   4686 N  N   . MET B 1 162 ? -4.948  -4.265  0.536   1.00 21.50  ? 162 MET B N   1 
ATOM   4687 C  CA  . MET B 1 162 ? -5.267  -5.705  0.446   1.00 23.42  ? 162 MET B CA  1 
ATOM   4688 C  C   . MET B 1 162 ? -6.686  -5.839  -0.101  1.00 24.49  ? 162 MET B C   1 
ATOM   4689 O  O   . MET B 1 162 ? -7.631  -5.218  0.462   1.00 23.37  ? 162 MET B O   1 
ATOM   4690 C  CB  . MET B 1 162 ? -5.158  -6.374  1.815   1.00 24.51  ? 162 MET B CB  1 
ATOM   4691 C  CG  . MET B 1 162 ? -5.545  -7.838  1.805   1.00 25.68  ? 162 MET B CG  1 
ATOM   4692 S  SD  . MET B 1 162 ? -5.128  -8.626  3.383   1.00 31.04  ? 162 MET B SD  1 
ATOM   4693 C  CE  . MET B 1 162 ? -3.364  -8.851  3.194   1.00 29.96  ? 162 MET B CE  1 
ATOM   4694 N  N   A HIS B 1 163 ? -6.843  -6.640  -1.158  0.25 23.61  ? 163 HIS B N   1 
ATOM   4695 N  N   B HIS B 1 163 ? -6.843  -6.640  -1.158  0.25 23.61  ? 163 HIS B N   1 
ATOM   4696 N  N   C HIS B 1 163 ? -6.830  -6.604  -1.187  0.25 25.55  ? 163 HIS B N   1 
ATOM   4697 N  N   D HIS B 1 163 ? -6.830  -6.604  -1.187  0.25 25.55  ? 163 HIS B N   1 
ATOM   4698 C  CA  A HIS B 1 163 ? -8.117  -6.850  -1.896  0.25 24.12  ? 163 HIS B CA  1 
ATOM   4699 C  CA  B HIS B 1 163 ? -8.117  -6.850  -1.896  0.25 24.12  ? 163 HIS B CA  1 
ATOM   4700 C  CA  C HIS B 1 163 ? -8.120  -6.867  -1.876  0.25 27.36  ? 163 HIS B CA  1 
ATOM   4701 C  CA  D HIS B 1 163 ? -8.120  -6.867  -1.876  0.25 27.36  ? 163 HIS B CA  1 
ATOM   4702 C  C   A HIS B 1 163 ? -9.068  -7.733  -1.074  0.25 24.97  ? 163 HIS B C   1 
ATOM   4703 C  C   B HIS B 1 163 ? -9.068  -7.733  -1.074  0.25 24.97  ? 163 HIS B C   1 
ATOM   4704 C  C   C HIS B 1 163 ? -9.036  -7.681  -0.955  0.25 26.92  ? 163 HIS B C   1 
ATOM   4705 C  C   D HIS B 1 163 ? -9.036  -7.681  -0.955  0.25 26.92  ? 163 HIS B C   1 
ATOM   4706 O  O   A HIS B 1 163 ? -8.659  -8.862  -0.719  0.25 25.00  ? 163 HIS B O   1 
ATOM   4707 O  O   B HIS B 1 163 ? -8.659  -8.862  -0.719  0.25 25.00  ? 163 HIS B O   1 
ATOM   4708 O  O   C HIS B 1 163 ? -8.563  -8.684  -0.376  0.25 27.26  ? 163 HIS B O   1 
ATOM   4709 O  O   D HIS B 1 163 ? -8.563  -8.684  -0.376  0.25 27.26  ? 163 HIS B O   1 
ATOM   4710 C  CB  A HIS B 1 163 ? -7.825  -7.452  -3.278  0.25 23.25  ? 163 HIS B CB  1 
ATOM   4711 C  CB  B HIS B 1 163 ? -7.825  -7.452  -3.278  0.25 23.25  ? 163 HIS B CB  1 
ATOM   4712 C  CB  C HIS B 1 163 ? -7.895  -7.579  -3.218  0.25 28.87  ? 163 HIS B CB  1 
ATOM   4713 C  CB  D HIS B 1 163 ? -7.895  -7.579  -3.218  0.25 28.87  ? 163 HIS B CB  1 
ATOM   4714 C  CG  A HIS B 1 163 ? -9.042  -7.636  -4.122  0.25 22.78  ? 163 HIS B CG  1 
ATOM   4715 C  CG  B HIS B 1 163 ? -9.042  -7.636  -4.122  0.25 22.78  ? 163 HIS B CG  1 
ATOM   4716 C  CG  C HIS B 1 163 ? -9.103  -8.311  -3.702  0.25 31.42  ? 163 HIS B CG  1 
ATOM   4717 C  CG  D HIS B 1 163 ? -9.103  -8.311  -3.702  0.25 31.42  ? 163 HIS B CG  1 
ATOM   4718 N  ND1 A HIS B 1 163 ? -9.934  -6.608  -4.363  0.25 22.54  ? 163 HIS B ND1 1 
ATOM   4719 N  ND1 B HIS B 1 163 ? -9.934  -6.608  -4.363  0.25 22.54  ? 163 HIS B ND1 1 
ATOM   4720 N  ND1 C HIS B 1 163 ? -10.116 -7.687  -4.410  0.25 31.43  ? 163 HIS B ND1 1 
ATOM   4721 N  ND1 D HIS B 1 163 ? -10.116 -7.687  -4.410  0.25 31.43  ? 163 HIS B ND1 1 
ATOM   4722 C  CD2 A HIS B 1 163 ? -9.527  -8.722  -4.764  0.25 22.43  ? 163 HIS B CD2 1 
ATOM   4723 C  CD2 B HIS B 1 163 ? -9.527  -8.722  -4.764  0.25 22.43  ? 163 HIS B CD2 1 
ATOM   4724 C  CD2 C HIS B 1 163 ? -9.480  -9.601  -3.550  0.25 32.66  ? 163 HIS B CD2 1 
ATOM   4725 C  CD2 D HIS B 1 163 ? -9.480  -9.601  -3.550  0.25 32.66  ? 163 HIS B CD2 1 
ATOM   4726 C  CE1 A HIS B 1 163 ? -10.917 -7.055  -5.115  0.25 22.25  ? 163 HIS B CE1 1 
ATOM   4727 C  CE1 B HIS B 1 163 ? -10.917 -7.055  -5.115  0.25 22.25  ? 163 HIS B CE1 1 
ATOM   4728 C  CE1 C HIS B 1 163 ? -11.061 -8.565  -4.680  0.25 31.81  ? 163 HIS B CE1 1 
ATOM   4729 C  CE1 D HIS B 1 163 ? -11.061 -8.565  -4.680  0.25 31.81  ? 163 HIS B CE1 1 
ATOM   4730 N  NE2 A HIS B 1 163 ? -10.691 -8.347  -5.376  0.25 22.40  ? 163 HIS B NE2 1 
ATOM   4731 N  NE2 B HIS B 1 163 ? -10.691 -8.347  -5.376  0.25 22.40  ? 163 HIS B NE2 1 
ATOM   4732 N  NE2 C HIS B 1 163 ? -10.696 -9.746  -4.159  0.25 32.61  ? 163 HIS B NE2 1 
ATOM   4733 N  NE2 D HIS B 1 163 ? -10.696 -9.746  -4.159  0.25 32.61  ? 163 HIS B NE2 1 
ATOM   4734 N  N   . HIS B 1 164 ? -10.294 -7.255  -0.821  1.00 26.08  ? 164 HIS B N   1 
ATOM   4735 C  CA  . HIS B 1 164 ? -11.333 -8.014  -0.078  1.00 28.42  ? 164 HIS B CA  1 
ATOM   4736 C  C   . HIS B 1 164 ? -12.424 -8.518  -1.030  1.00 31.93  ? 164 HIS B C   1 
ATOM   4737 O  O   . HIS B 1 164 ? -12.818 -9.674  -0.890  1.00 33.41  ? 164 HIS B O   1 
ATOM   4738 C  CB  . HIS B 1 164 ? -11.863 -7.178  1.091   1.00 27.84  ? 164 HIS B CB  1 
ATOM   4739 C  CG  . HIS B 1 164 ? -10.880 -7.092  2.213   1.00 26.81  ? 164 HIS B CG  1 
ATOM   4740 N  ND1 . HIS B 1 164 ? -11.095 -7.675  3.450   1.00 26.14  ? 164 HIS B ND1 1 
ATOM   4741 C  CD2 . HIS B 1 164 ? -9.651  -6.528  2.260   1.00 26.54  ? 164 HIS B CD2 1 
ATOM   4742 C  CE1 . HIS B 1 164 ? -10.060 -7.413  4.228   1.00 28.11  ? 164 HIS B CE1 1 
ATOM   4743 N  NE2 . HIS B 1 164 ? -9.151  -6.711  3.511   1.00 25.52  ? 164 HIS B NE2 1 
ATOM   4744 N  N   . MET B 1 165 ? -12.911 -7.693  -1.947  1.00 32.24  ? 165 MET B N   1 
ATOM   4745 C  CA  . MET B 1 165 ? -14.164 -7.996  -2.674  1.00 37.59  ? 165 MET B CA  1 
ATOM   4746 C  C   . MET B 1 165 ? -14.254 -7.157  -3.943  1.00 39.47  ? 165 MET B C   1 
ATOM   4747 O  O   . MET B 1 165 ? -13.620 -6.104  -4.023  1.00 37.10  ? 165 MET B O   1 
ATOM   4748 C  CB  . MET B 1 165 ? -15.371 -7.645  -1.793  1.00 37.67  ? 165 MET B CB  1 
ATOM   4749 C  CG  . MET B 1 165 ? -15.359 -6.198  -1.298  1.00 41.92  ? 165 MET B CG  1 
ATOM   4750 S  SD  . MET B 1 165 ? -16.519 -5.791  0.046   1.00 49.72  ? 165 MET B SD  1 
ATOM   4751 C  CE  . MET B 1 165 ? -16.748 -7.425  0.758   1.00 55.19  ? 165 MET B CE  1 
ATOM   4752 N  N   A GLU B 1 166 ? -15.067 -7.616  -4.897  0.25 39.86  ? 166 GLU B N   1 
ATOM   4753 N  N   B GLU B 1 166 ? -15.067 -7.616  -4.897  0.25 39.86  ? 166 GLU B N   1 
ATOM   4754 N  N   C GLU B 1 166 ? -15.018 -7.638  -4.926  0.25 42.22  ? 166 GLU B N   1 
ATOM   4755 N  N   D GLU B 1 166 ? -15.018 -7.638  -4.926  0.25 42.22  ? 166 GLU B N   1 
ATOM   4756 C  CA  A GLU B 1 166 ? -15.459 -6.854  -6.112  0.25 41.45  ? 166 GLU B CA  1 
ATOM   4757 C  CA  B GLU B 1 166 ? -15.459 -6.854  -6.112  0.25 41.45  ? 166 GLU B CA  1 
ATOM   4758 C  CA  C GLU B 1 166 ? -15.456 -6.832  -6.096  0.25 45.43  ? 166 GLU B CA  1 
ATOM   4759 C  CA  D GLU B 1 166 ? -15.456 -6.832  -6.096  0.25 45.43  ? 166 GLU B CA  1 
ATOM   4760 C  C   A GLU B 1 166 ? -16.882 -6.312  -5.923  0.25 42.45  ? 166 GLU B C   1 
ATOM   4761 C  C   B GLU B 1 166 ? -16.882 -6.312  -5.923  0.25 42.45  ? 166 GLU B C   1 
ATOM   4762 C  C   C GLU B 1 166 ? -16.833 -6.242  -5.776  0.25 44.58  ? 166 GLU B C   1 
ATOM   4763 C  C   D GLU B 1 166 ? -16.833 -6.242  -5.776  0.25 44.58  ? 166 GLU B C   1 
ATOM   4764 O  O   A GLU B 1 166 ? -17.738 -7.073  -5.435  0.25 42.24  ? 166 GLU B O   1 
ATOM   4765 O  O   B GLU B 1 166 ? -17.738 -7.073  -5.435  0.25 42.24  ? 166 GLU B O   1 
ATOM   4766 O  O   C GLU B 1 166 ? -17.585 -6.877  -5.015  0.25 43.99  ? 166 GLU B O   1 
ATOM   4767 O  O   D GLU B 1 166 ? -17.585 -6.877  -5.015  0.25 43.99  ? 166 GLU B O   1 
ATOM   4768 C  CB  A GLU B 1 166 ? -15.370 -7.749  -7.347  0.25 40.39  ? 166 GLU B CB  1 
ATOM   4769 C  CB  B GLU B 1 166 ? -15.370 -7.749  -7.347  0.25 40.39  ? 166 GLU B CB  1 
ATOM   4770 C  CB  C GLU B 1 166 ? -15.525 -7.675  -7.371  0.25 47.56  ? 166 GLU B CB  1 
ATOM   4771 C  CB  D GLU B 1 166 ? -15.525 -7.675  -7.371  0.25 47.56  ? 166 GLU B CB  1 
ATOM   4772 C  CG  A GLU B 1 166 ? -15.679 -7.017  -8.637  0.25 39.96  ? 166 GLU B CG  1 
ATOM   4773 C  CG  B GLU B 1 166 ? -15.679 -7.017  -8.637  0.25 39.96  ? 166 GLU B CG  1 
ATOM   4774 C  CG  C GLU B 1 166 ? -16.929 -8.148  -7.701  0.25 50.41  ? 166 GLU B CG  1 
ATOM   4775 C  CG  D GLU B 1 166 ? -16.929 -8.148  -7.701  0.25 50.41  ? 166 GLU B CG  1 
ATOM   4776 C  CD  A GLU B 1 166 ? -15.584 -7.890  -9.873  0.25 40.14  ? 166 GLU B CD  1 
ATOM   4777 C  CD  B GLU B 1 166 ? -15.584 -7.890  -9.873  0.25 40.14  ? 166 GLU B CD  1 
ATOM   4778 C  CD  C GLU B 1 166 ? -17.152 -8.496  -9.164  0.25 52.91  ? 166 GLU B CD  1 
ATOM   4779 C  CD  D GLU B 1 166 ? -17.152 -8.496  -9.164  0.25 52.91  ? 166 GLU B CD  1 
ATOM   4780 O  OE1 A GLU B 1 166 ? -14.456 -8.253  -10.250 0.25 39.23  ? 166 GLU B OE1 1 
ATOM   4781 O  OE1 B GLU B 1 166 ? -14.456 -8.253  -10.250 0.25 39.23  ? 166 GLU B OE1 1 
ATOM   4782 O  OE1 C GLU B 1 166 ? -16.205 -8.312  -9.964  0.25 53.76  ? 166 GLU B OE1 1 
ATOM   4783 O  OE1 D GLU B 1 166 ? -16.205 -8.312  -9.964  0.25 53.76  ? 166 GLU B OE1 1 
ATOM   4784 O  OE2 A GLU B 1 166 ? -16.641 -8.220  -10.442 0.25 42.30  ? 166 GLU B OE2 1 
ATOM   4785 O  OE2 B GLU B 1 166 ? -16.641 -8.220  -10.442 0.25 42.30  ? 166 GLU B OE2 1 
ATOM   4786 O  OE2 C GLU B 1 166 ? -18.273 -8.947  -9.500  0.25 52.77  ? 166 GLU B OE2 1 
ATOM   4787 O  OE2 D GLU B 1 166 ? -18.273 -8.947  -9.500  0.25 52.77  ? 166 GLU B OE2 1 
ATOM   4788 N  N   . LEU B 1 167 ? -17.124 -5.056  -6.311  1.00 43.74  ? 167 LEU B N   1 
ATOM   4789 C  CA  . LEU B 1 167 ? -18.470 -4.434  -6.238  1.00 45.16  ? 167 LEU B CA  1 
ATOM   4790 C  C   . LEU B 1 167 ? -19.225 -4.788  -7.518  1.00 50.12  ? 167 LEU B C   1 
ATOM   4791 O  O   . LEU B 1 167 ? -18.621 -5.189  -8.519  1.00 46.21  ? 167 LEU B O   1 
ATOM   4792 C  CB  . LEU B 1 167 ? -18.323 -2.921  -6.055  1.00 44.30  ? 167 LEU B CB  1 
ATOM   4793 C  CG  . LEU B 1 167 ? -17.639 -2.493  -4.756  1.00 45.87  ? 167 LEU B CG  1 
ATOM   4794 C  CD1 . LEU B 1 167 ? -17.381 -0.996  -4.742  1.00 46.28  ? 167 LEU B CD1 1 
ATOM   4795 C  CD2 . LEU B 1 167 ? -18.451 -2.903  -3.544  1.00 42.38  ? 167 LEU B CD2 1 
ATOM   4796 N  N   . PRO B 1 168 ? -20.570 -4.650  -7.512  1.00 54.72  ? 168 PRO B N   1 
ATOM   4797 C  CA  . PRO B 1 168 ? -21.408 -5.071  -8.635  1.00 55.20  ? 168 PRO B CA  1 
ATOM   4798 C  C   . PRO B 1 168 ? -20.987 -4.470  -9.981  1.00 57.32  ? 168 PRO B C   1 
ATOM   4799 O  O   . PRO B 1 168 ? -21.223 -5.105  -10.984 1.00 65.52  ? 168 PRO B O   1 
ATOM   4800 C  CB  . PRO B 1 168 ? -22.799 -4.537  -8.272  1.00 53.89  ? 168 PRO B CB  1 
ATOM   4801 C  CG  . PRO B 1 168 ? -22.783 -4.472  -6.770  1.00 60.42  ? 168 PRO B CG  1 
ATOM   4802 C  CD  . PRO B 1 168 ? -21.364 -4.080  -6.412  1.00 56.82  ? 168 PRO B CD  1 
ATOM   4803 N  N   . THR B 1 169 ? -20.379 -3.282  -9.963  1.00 52.77  ? 169 THR B N   1 
ATOM   4804 C  CA  . THR B 1 169 ? -19.964 -2.525  -11.174 1.00 52.59  ? 169 THR B CA  1 
ATOM   4805 C  C   . THR B 1 169 ? -18.638 -3.034  -11.765 1.00 48.05  ? 169 THR B C   1 
ATOM   4806 O  O   . THR B 1 169 ? -18.197 -2.421  -12.719 1.00 46.89  ? 169 THR B O   1 
ATOM   4807 C  CB  . THR B 1 169 ? -19.813 -1.036  -10.846 1.00 54.42  ? 169 THR B CB  1 
ATOM   4808 O  OG1 . THR B 1 169 ? -19.237 -0.983  -9.538  1.00 62.67  ? 169 THR B OG1 1 
ATOM   4809 C  CG2 . THR B 1 169 ? -21.122 -0.282  -10.897 1.00 53.92  ? 169 THR B CG2 1 
ATOM   4810 N  N   . GLY B 1 170 ? -17.991 -4.063  -11.211 1.00 47.92  ? 170 GLY B N   1 
ATOM   4811 C  CA  . GLY B 1 170 ? -16.694 -4.567  -11.714 1.00 46.91  ? 170 GLY B CA  1 
ATOM   4812 C  C   . GLY B 1 170 ? -15.483 -3.974  -10.993 1.00 48.57  ? 170 GLY B C   1 
ATOM   4813 O  O   . GLY B 1 170 ? -14.366 -4.514  -11.189 1.00 48.63  ? 170 GLY B O   1 
ATOM   4814 N  N   . VAL B 1 171 ? -15.665 -2.910  -10.195 1.00 44.43  ? 171 VAL B N   1 
ATOM   4815 C  CA  . VAL B 1 171 ? -14.568 -2.240  -9.422  1.00 40.55  ? 171 VAL B CA  1 
ATOM   4816 C  C   . VAL B 1 171 ? -14.324 -3.027  -8.117  1.00 36.28  ? 171 VAL B C   1 
ATOM   4817 O  O   . VAL B 1 171 ? -15.140 -3.907  -7.764  1.00 34.92  ? 171 VAL B O   1 
ATOM   4818 C  CB  . VAL B 1 171 ? -14.861 -0.738  -9.215  1.00 45.14  ? 171 VAL B CB  1 
ATOM   4819 C  CG1 . VAL B 1 171 ? -15.093 -0.038  -10.560 1.00 45.02  ? 171 VAL B CG1 1 
ATOM   4820 C  CG2 . VAL B 1 171 ? -16.018 -0.484  -8.249  1.00 42.82  ? 171 VAL B CG2 1 
ATOM   4821 N  N   A HIS B 1 172 ? -13.233 -2.711  -7.412  0.25 33.37  ? 172 HIS B N   1 
ATOM   4822 N  N   B HIS B 1 172 ? -13.233 -2.711  -7.412  0.25 33.37  ? 172 HIS B N   1 
ATOM   4823 N  N   C HIS B 1 172 ? -13.203 -2.742  -7.440  0.25 36.21  ? 172 HIS B N   1 
ATOM   4824 N  N   D HIS B 1 172 ? -13.203 -2.742  -7.440  0.25 36.21  ? 172 HIS B N   1 
ATOM   4825 C  CA  A HIS B 1 172 ? -12.709 -3.521  -6.280  0.25 31.01  ? 172 HIS B CA  1 
ATOM   4826 C  CA  B HIS B 1 172 ? -12.709 -3.521  -6.280  0.25 31.01  ? 172 HIS B CA  1 
ATOM   4827 C  CA  C HIS B 1 172 ? -12.696 -3.520  -6.276  0.25 35.36  ? 172 HIS B CA  1 
ATOM   4828 C  CA  D HIS B 1 172 ? -12.696 -3.520  -6.276  0.25 35.36  ? 172 HIS B CA  1 
ATOM   4829 C  C   A HIS B 1 172 ? -12.573 -2.662  -5.019  0.25 29.46  ? 172 HIS B C   1 
ATOM   4830 C  C   B HIS B 1 172 ? -12.573 -2.662  -5.019  0.25 29.46  ? 172 HIS B C   1 
ATOM   4831 C  C   C HIS B 1 172 ? -12.618 -2.649  -5.019  0.25 31.79  ? 172 HIS B C   1 
ATOM   4832 C  C   D HIS B 1 172 ? -12.618 -2.649  -5.019  0.25 31.79  ? 172 HIS B C   1 
ATOM   4833 O  O   A HIS B 1 172 ? -12.282 -1.457  -5.148  0.25 28.66  ? 172 HIS B O   1 
ATOM   4834 O  O   B HIS B 1 172 ? -12.282 -1.457  -5.148  0.25 28.66  ? 172 HIS B O   1 
ATOM   4835 O  O   C HIS B 1 172 ? -12.409 -1.428  -5.150  0.25 30.85  ? 172 HIS B O   1 
ATOM   4836 O  O   D HIS B 1 172 ? -12.409 -1.428  -5.150  0.25 30.85  ? 172 HIS B O   1 
ATOM   4837 C  CB  A HIS B 1 172 ? -11.416 -4.202  -6.728  0.25 30.93  ? 172 HIS B CB  1 
ATOM   4838 C  CB  B HIS B 1 172 ? -11.416 -4.202  -6.728  0.25 30.93  ? 172 HIS B CB  1 
ATOM   4839 C  CB  C HIS B 1 172 ? -11.363 -4.183  -6.626  0.25 38.96  ? 172 HIS B CB  1 
ATOM   4840 C  CB  D HIS B 1 172 ? -11.363 -4.183  -6.626  0.25 38.96  ? 172 HIS B CB  1 
ATOM   4841 C  CG  A HIS B 1 172 ? -11.587 -4.900  -8.038  0.25 32.28  ? 172 HIS B CG  1 
ATOM   4842 C  CG  B HIS B 1 172 ? -11.587 -4.900  -8.038  0.25 32.28  ? 172 HIS B CG  1 
ATOM   4843 C  CG  C HIS B 1 172 ? -11.562 -5.456  -7.373  0.25 45.14  ? 172 HIS B CG  1 
ATOM   4844 C  CG  D HIS B 1 172 ? -11.562 -5.456  -7.373  0.25 45.14  ? 172 HIS B CG  1 
ATOM   4845 N  ND1 A HIS B 1 172 ? -11.137 -4.365  -9.234  0.25 30.77  ? 172 HIS B ND1 1 
ATOM   4846 N  ND1 B HIS B 1 172 ? -11.137 -4.365  -9.234  0.25 30.77  ? 172 HIS B ND1 1 
ATOM   4847 N  ND1 C HIS B 1 172 ? -11.260 -6.691  -6.829  0.25 47.72  ? 172 HIS B ND1 1 
ATOM   4848 N  ND1 D HIS B 1 172 ? -11.260 -6.691  -6.829  0.25 47.72  ? 172 HIS B ND1 1 
ATOM   4849 C  CD2 A HIS B 1 172 ? -12.215 -6.056  -8.352  0.25 31.94  ? 172 HIS B CD2 1 
ATOM   4850 C  CD2 B HIS B 1 172 ? -12.215 -6.056  -8.352  0.25 31.94  ? 172 HIS B CD2 1 
ATOM   4851 C  CD2 C HIS B 1 172 ? -12.092 -5.696  -8.594  0.25 47.11  ? 172 HIS B CD2 1 
ATOM   4852 C  CD2 D HIS B 1 172 ? -12.092 -5.696  -8.594  0.25 47.11  ? 172 HIS B CD2 1 
ATOM   4853 C  CE1 A HIS B 1 172 ? -11.440 -5.185  -10.219 0.25 31.11  ? 172 HIS B CE1 1 
ATOM   4854 C  CE1 B HIS B 1 172 ? -11.440 -5.185  -10.219 0.25 31.11  ? 172 HIS B CE1 1 
ATOM   4855 C  CE1 C HIS B 1 172 ? -11.570 -7.637  -7.696  0.25 47.96  ? 172 HIS B CE1 1 
ATOM   4856 C  CE1 D HIS B 1 172 ? -11.570 -7.637  -7.696  0.25 47.96  ? 172 HIS B CE1 1 
ATOM   4857 N  NE2 A HIS B 1 172 ? -12.109 -6.226  -9.707  0.25 31.28  ? 172 HIS B NE2 1 
ATOM   4858 N  NE2 B HIS B 1 172 ? -12.109 -6.226  -9.707  0.25 31.28  ? 172 HIS B NE2 1 
ATOM   4859 N  NE2 C HIS B 1 172 ? -12.084 -7.051  -8.786  0.25 48.04  ? 172 HIS B NE2 1 
ATOM   4860 N  NE2 D HIS B 1 172 ? -12.084 -7.051  -8.786  0.25 48.04  ? 172 HIS B NE2 1 
ATOM   4861 N  N   . ALA B 1 173 ? -12.792 -3.283  -3.855  1.00 27.72  ? 173 ALA B N   1 
ATOM   4862 C  CA  . ALA B 1 173 ? -12.745 -2.647  -2.529  1.00 27.04  ? 173 ALA B CA  1 
ATOM   4863 C  C   . ALA B 1 173 ? -11.865 -3.495  -1.615  1.00 24.92  ? 173 ALA B C   1 
ATOM   4864 O  O   . ALA B 1 173 ? -11.875 -4.733  -1.712  1.00 23.90  ? 173 ALA B O   1 
ATOM   4865 C  CB  . ALA B 1 173 ? -14.136 -2.545  -1.974  1.00 31.17  ? 173 ALA B CB  1 
ATOM   4866 N  N   . GLY B 1 174 ? -11.081 -2.825  -0.787  1.00 22.20  ? 174 GLY B N   1 
ATOM   4867 C  CA  . GLY B 1 174 ? -10.129 -3.479  0.110   1.00 21.23  ? 174 GLY B CA  1 
ATOM   4868 C  C   . GLY B 1 174 ? -9.761  -2.564  1.248   1.00 19.97  ? 174 GLY B C   1 
ATOM   4869 O  O   . GLY B 1 174 ? -10.376 -1.477  1.441   1.00 17.02  ? 174 GLY B O   1 
ATOM   4870 N  N   . THR B 1 175 ? -8.759  -2.984  1.991   1.00 20.34  ? 175 THR B N   1 
ATOM   4871 C  CA  . THR B 1 175 ? -8.379  -2.324  3.253   1.00 21.64  ? 175 THR B CA  1 
ATOM   4872 C  C   . THR B 1 175 ? -6.936  -1.901  3.121   1.00 21.21  ? 175 THR B C   1 
ATOM   4873 O  O   . THR B 1 175 ? -6.292  -2.388  2.207   1.00 23.12  ? 175 THR B O   1 
ATOM   4874 C  CB  . THR B 1 175 ? -8.513  -3.283  4.438   1.00 20.66  ? 175 THR B CB  1 
ATOM   4875 O  OG1 . THR B 1 175 ? -7.650  -4.401  4.206   1.00 17.93  ? 175 THR B OG1 1 
ATOM   4876 C  CG2 . THR B 1 175 ? -9.954  -3.688  4.627   1.00 21.57  ? 175 THR B CG2 1 
ATOM   4877 N  N   . ASP B 1 176 ? -6.462  -1.101  4.063   1.00 22.65  ? 176 ASP B N   1 
ATOM   4878 C  CA  . ASP B 1 176 ? -5.016  -0.985  4.325   1.00 22.81  ? 176 ASP B CA  1 
ATOM   4879 C  C   . ASP B 1 176 ? -4.620  -2.238  5.106   1.00 24.40  ? 176 ASP B C   1 
ATOM   4880 O  O   . ASP B 1 176 ? -5.491  -3.121  5.357   1.00 23.90  ? 176 ASP B O   1 
ATOM   4881 C  CB  . ASP B 1 176 ? -4.684  0.313   5.041   1.00 24.11  ? 176 ASP B CB  1 
ATOM   4882 C  CG  . ASP B 1 176 ? -5.258  0.386   6.438   1.00 24.06  ? 176 ASP B CG  1 
ATOM   4883 O  OD1 . ASP B 1 176 ? -5.447  -0.679  7.041   1.00 22.49  ? 176 ASP B OD1 1 
ATOM   4884 O  OD2 . ASP B 1 176 ? -5.518  1.499   6.883   1.00 23.21  ? 176 ASP B OD2 1 
ATOM   4885 N  N   . LEU B 1 177 ? -3.346  -2.345  5.448   1.00 24.72  ? 177 LEU B N   1 
ATOM   4886 C  CA  . LEU B 1 177 ? -2.792  -3.588  6.033   1.00 25.24  ? 177 LEU B CA  1 
ATOM   4887 C  C   . LEU B 1 177 ? -3.091  -3.614  7.533   1.00 26.95  ? 177 LEU B C   1 
ATOM   4888 O  O   . LEU B 1 177 ? -2.705  -4.585  8.165   1.00 24.31  ? 177 LEU B O   1 
ATOM   4889 C  CB  . LEU B 1 177 ? -1.290  -3.666  5.730   1.00 25.09  ? 177 LEU B CB  1 
ATOM   4890 C  CG  . LEU B 1 177 ? -0.942  -4.482  4.490   1.00 26.42  ? 177 LEU B CG  1 
ATOM   4891 C  CD1 . LEU B 1 177 ? -1.192  -5.964  4.733   1.00 28.79  ? 177 LEU B CD1 1 
ATOM   4892 C  CD2 . LEU B 1 177 ? -1.716  -3.997  3.265   1.00 27.23  ? 177 LEU B CD2 1 
ATOM   4893 N  N   . GLU B 1 178 ? -3.770  -2.592  8.064   1.00 25.81  ? 178 GLU B N   1 
ATOM   4894 C  CA  . GLU B 1 178 ? -4.285  -2.593  9.457   1.00 25.80  ? 178 GLU B CA  1 
ATOM   4895 C  C   . GLU B 1 178 ? -5.778  -2.918  9.417   1.00 22.80  ? 178 GLU B C   1 
ATOM   4896 O  O   . GLU B 1 178 ? -6.436  -2.729  10.455  1.00 22.45  ? 178 GLU B O   1 
ATOM   4897 C  CB  . GLU B 1 178 ? -4.024  -1.248  10.141  1.00 26.36  ? 178 GLU B CB  1 
ATOM   4898 C  CG  . GLU B 1 178 ? -2.553  -0.949  10.318  1.00 29.81  ? 178 GLU B CG  1 
ATOM   4899 C  CD  . GLU B 1 178 ? -2.216  0.472   10.744  1.00 36.82  ? 178 GLU B CD  1 
ATOM   4900 O  OE1 . GLU B 1 178 ? -1.449  1.128   10.015  1.00 51.84  ? 178 GLU B OE1 1 
ATOM   4901 O  OE2 . GLU B 1 178 ? -2.700  0.926   11.785  1.00 36.31  ? 178 GLU B OE2 1 
ATOM   4902 N  N   . GLY B 1 179 ? -6.287  -3.325  8.249   1.00 22.00  ? 179 GLY B N   1 
ATOM   4903 C  CA  . GLY B 1 179 ? -7.657  -3.854  8.065   1.00 22.82  ? 179 GLY B CA  1 
ATOM   4904 C  C   . GLY B 1 179 ? -8.733  -2.771  8.080   1.00 23.60  ? 179 GLY B C   1 
ATOM   4905 O  O   . GLY B 1 179 ? -9.930  -3.130  8.168   1.00 23.16  ? 179 GLY B O   1 
ATOM   4906 N  N   . ASN B 1 180 ? -8.352  -1.494  7.990   1.00 23.32  ? 180 ASN B N   1 
ATOM   4907 C  CA  . ASN B 1 180 ? -9.332  -0.393  7.807   1.00 24.71  ? 180 ASN B CA  1 
ATOM   4908 C  C   . ASN B 1 180 ? -9.724  -0.343  6.335   1.00 25.72  ? 180 ASN B C   1 
ATOM   4909 O  O   . ASN B 1 180 ? -8.817  -0.163  5.478   1.00 23.11  ? 180 ASN B O   1 
ATOM   4910 C  CB  . ASN B 1 180 ? -8.798  0.972   8.222   1.00 27.26  ? 180 ASN B CB  1 
ATOM   4911 C  CG  . ASN B 1 180 ? -8.140  0.957   9.577   1.00 27.57  ? 180 ASN B CG  1 
ATOM   4912 O  OD1 . ASN B 1 180 ? -6.922  1.107   9.682   1.00 30.02  ? 180 ASN B OD1 1 
ATOM   4913 N  ND2 . ASN B 1 180 ? -8.939  0.745   10.597  1.00 25.68  ? 180 ASN B ND2 1 
ATOM   4914 N  N   . PHE B 1 181 ? -11.023 -0.449  6.040   1.00 25.64  ? 181 PHE B N   1 
ATOM   4915 C  CA  . PHE B 1 181 ? -11.526 -0.231  4.659   1.00 23.70  ? 181 PHE B CA  1 
ATOM   4916 C  C   . PHE B 1 181 ? -11.115 1.142   4.135   1.00 21.21  ? 181 PHE B C   1 
ATOM   4917 O  O   . PHE B 1 181 ? -11.033 2.160   4.883   1.00 19.75  ? 181 PHE B O   1 
ATOM   4918 C  CB  . PHE B 1 181 ? -13.034 -0.421  4.523   1.00 24.16  ? 181 PHE B CB  1 
ATOM   4919 C  CG  . PHE B 1 181 ? -13.386 -1.805  4.035   1.00 25.93  ? 181 PHE B CG  1 
ATOM   4920 C  CD1 . PHE B 1 181 ? -13.337 -2.106  2.688   1.00 26.15  ? 181 PHE B CD1 1 
ATOM   4921 C  CD2 . PHE B 1 181 ? -13.679 -2.827  4.938   1.00 25.80  ? 181 PHE B CD2 1 
ATOM   4922 C  CE1 . PHE B 1 181 ? -13.629 -3.388  2.250   1.00 27.50  ? 181 PHE B CE1 1 
ATOM   4923 C  CE2 . PHE B 1 181 ? -13.957 -4.109  4.500   1.00 26.12  ? 181 PHE B CE2 1 
ATOM   4924 C  CZ  . PHE B 1 181 ? -13.912 -4.391  3.159   1.00 26.90  ? 181 PHE B CZ  1 
ATOM   4925 N  N   . TYR B 1 182 ? -10.841 1.150   2.837   1.00 21.96  ? 182 TYR B N   1 
ATOM   4926 C  CA  . TYR B 1 182 ? -10.916 2.361   1.986   1.00 24.44  ? 182 TYR B CA  1 
ATOM   4927 C  C   . TYR B 1 182 ? -12.348 2.453   1.485   1.00 23.86  ? 182 TYR B C   1 
ATOM   4928 O  O   . TYR B 1 182 ? -12.773 1.551   0.740   1.00 24.21  ? 182 TYR B O   1 
ATOM   4929 C  CB  . TYR B 1 182 ? -9.960  2.305   0.796   1.00 24.57  ? 182 TYR B CB  1 
ATOM   4930 C  CG  . TYR B 1 182 ? -8.498  2.359   1.139   1.00 24.43  ? 182 TYR B CG  1 
ATOM   4931 C  CD1 . TYR B 1 182 ? -7.869  3.555   1.441   1.00 25.22  ? 182 TYR B CD1 1 
ATOM   4932 C  CD2 . TYR B 1 182 ? -7.737  1.196   1.145   1.00 25.90  ? 182 TYR B CD2 1 
ATOM   4933 C  CE1 . TYR B 1 182 ? -6.515  3.599   1.732   1.00 25.45  ? 182 TYR B CE1 1 
ATOM   4934 C  CE2 . TYR B 1 182 ? -6.390  1.221   1.450   1.00 22.61  ? 182 TYR B CE2 1 
ATOM   4935 C  CZ  . TYR B 1 182 ? -5.771  2.426   1.736   1.00 25.78  ? 182 TYR B CZ  1 
ATOM   4936 O  OH  . TYR B 1 182 ? -4.433  2.451   2.033   1.00 22.07  ? 182 TYR B OH  1 
ATOM   4937 N  N   . GLY B 1 183 ? -13.062 3.482   1.934   1.00 24.75  ? 183 GLY B N   1 
ATOM   4938 C  CA  . GLY B 1 183 ? -14.426 3.784   1.467   1.00 27.17  ? 183 GLY B CA  1 
ATOM   4939 C  C   . GLY B 1 183 ? -15.484 3.142   2.358   1.00 26.49  ? 183 GLY B C   1 
ATOM   4940 O  O   . GLY B 1 183 ? -15.169 2.371   3.262   1.00 26.13  ? 183 GLY B O   1 
ATOM   4941 N  N   . PRO B 1 184 ? -16.768 3.473   2.107   1.00 29.13  ? 184 PRO B N   1 
ATOM   4942 C  CA  . PRO B 1 184 ? -17.871 3.106   2.999   1.00 28.38  ? 184 PRO B CA  1 
ATOM   4943 C  C   . PRO B 1 184 ? -18.362 1.668   2.813   1.00 28.70  ? 184 PRO B C   1 
ATOM   4944 O  O   . PRO B 1 184 ? -19.553 1.466   2.578   1.00 27.36  ? 184 PRO B O   1 
ATOM   4945 C  CB  . PRO B 1 184 ? -18.933 4.150   2.621   1.00 27.45  ? 184 PRO B CB  1 
ATOM   4946 C  CG  . PRO B 1 184 ? -18.708 4.400   1.145   1.00 29.08  ? 184 PRO B CG  1 
ATOM   4947 C  CD  . PRO B 1 184 ? -17.206 4.286   0.960   1.00 29.37  ? 184 PRO B CD  1 
ATOM   4948 N  N   . PHE B 1 185 ? -17.444 0.703   2.905   1.00 28.41  ? 185 PHE B N   1 
ATOM   4949 C  CA  . PHE B 1 185 ? -17.712 -0.721  2.565   1.00 27.18  ? 185 PHE B CA  1 
ATOM   4950 C  C   . PHE B 1 185 ? -17.591 -1.577  3.821   1.00 26.74  ? 185 PHE B C   1 
ATOM   4951 O  O   . PHE B 1 185 ? -16.908 -1.193  4.749   1.00 25.26  ? 185 PHE B O   1 
ATOM   4952 C  CB  . PHE B 1 185 ? -16.807 -1.184  1.420   1.00 27.67  ? 185 PHE B CB  1 
ATOM   4953 C  CG  . PHE B 1 185 ? -16.943 -0.307  0.197   1.00 27.12  ? 185 PHE B CG  1 
ATOM   4954 C  CD1 . PHE B 1 185 ? -18.138 -0.254  -0.508  1.00 27.49  ? 185 PHE B CD1 1 
ATOM   4955 C  CD2 . PHE B 1 185 ? -15.915 0.522   -0.199  1.00 25.58  ? 185 PHE B CD2 1 
ATOM   4956 C  CE1 . PHE B 1 185 ? -18.292 0.598   -1.592  1.00 28.11  ? 185 PHE B CE1 1 
ATOM   4957 C  CE2 . PHE B 1 185 ? -16.064 1.365   -1.288  1.00 27.56  ? 185 PHE B CE2 1 
ATOM   4958 C  CZ  . PHE B 1 185 ? -17.253 1.410   -1.978  1.00 28.68  ? 185 PHE B CZ  1 
ATOM   4959 N  N   . VAL B 1 186 ? -18.278 -2.706  3.820   1.00 27.26  ? 186 VAL B N   1 
ATOM   4960 C  CA  . VAL B 1 186 ? -18.246 -3.698  4.918   1.00 27.77  ? 186 VAL B CA  1 
ATOM   4961 C  C   . VAL B 1 186 ? -17.949 -5.054  4.288   1.00 28.89  ? 186 VAL B C   1 
ATOM   4962 O  O   . VAL B 1 186 ? -18.335 -5.264  3.116   1.00 31.14  ? 186 VAL B O   1 
ATOM   4963 C  CB  . VAL B 1 186 ? -19.553 -3.657  5.717   1.00 30.59  ? 186 VAL B CB  1 
ATOM   4964 C  CG1 . VAL B 1 186 ? -19.669 -2.357  6.503   1.00 29.58  ? 186 VAL B CG1 1 
ATOM   4965 C  CG2 . VAL B 1 186 ? -20.779 -3.882  4.848   1.00 31.30  ? 186 VAL B CG2 1 
ATOM   4966 N  N   . ASP B 1 187 ? -17.252 -5.927  5.006   1.00 27.32  ? 187 ASP B N   1 
ATOM   4967 C  CA  . ASP B 1 187 ? -16.912 -7.278  4.479   1.00 32.32  ? 187 ASP B CA  1 
ATOM   4968 C  C   . ASP B 1 187 ? -18.061 -8.251  4.823   1.00 33.20  ? 187 ASP B C   1 
ATOM   4969 O  O   . ASP B 1 187 ? -17.826 -9.209  5.580   1.00 35.71  ? 187 ASP B O   1 
ATOM   4970 C  CB  . ASP B 1 187 ? -15.536 -7.735  4.973   1.00 30.64  ? 187 ASP B CB  1 
ATOM   4971 C  CG  . ASP B 1 187 ? -15.305 -7.648  6.479   1.00 29.15  ? 187 ASP B CG  1 
ATOM   4972 O  OD1 . ASP B 1 187 ? -16.100 -6.999  7.176   1.00 30.09  ? 187 ASP B OD1 1 
ATOM   4973 O  OD2 . ASP B 1 187 ? -14.289 -8.175  6.935   1.00 27.06  ? 187 ASP B OD2 1 
ATOM   4974 N  N   . ARG B 1 188 ? -19.259 -8.000  4.300   1.00 38.85  ? 188 ARG B N   1 
ATOM   4975 C  CA  . ARG B 1 188 ? -20.408 -8.950  4.356   1.00 46.31  ? 188 ARG B CA  1 
ATOM   4976 C  C   . ARG B 1 188 ? -21.075 -9.021  2.972   1.00 47.40  ? 188 ARG B C   1 
ATOM   4977 O  O   . ARG B 1 188 ? -20.948 -8.062  2.180   1.00 40.42  ? 188 ARG B O   1 
ATOM   4978 C  CB  . ARG B 1 188 ? -21.371 -8.582  5.496   1.00 50.22  ? 188 ARG B CB  1 
ATOM   4979 C  CG  . ARG B 1 188 ? -22.488 -7.598  5.167   1.00 57.38  ? 188 ARG B CG  1 
ATOM   4980 C  CD  . ARG B 1 188 ? -23.200 -7.051  6.407   1.00 65.21  ? 188 ARG B CD  1 
ATOM   4981 N  NE  . ARG B 1 188 ? -22.191 -6.539  7.333   1.00 71.47  ? 188 ARG B NE  1 
ATOM   4982 C  CZ  . ARG B 1 188 ? -21.881 -7.056  8.522   1.00 74.56  ? 188 ARG B CZ  1 
ATOM   4983 N  NH1 . ARG B 1 188 ? -22.545 -8.091  9.014   1.00 80.92  ? 188 ARG B NH1 1 
ATOM   4984 N  NH2 . ARG B 1 188 ? -20.893 -6.522  9.221   1.00 75.30  ? 188 ARG B NH2 1 
ATOM   4985 N  N   . GLN B 1 189 ? -21.723 -10.143 2.659   1.00 51.11  ? 189 GLN B N   1 
ATOM   4986 C  CA  . GLN B 1 189 ? -22.532 -10.266 1.423   1.00 57.84  ? 189 GLN B CA  1 
ATOM   4987 C  C   . GLN B 1 189 ? -23.792 -9.425  1.635   1.00 57.13  ? 189 GLN B C   1 
ATOM   4988 O  O   . GLN B 1 189 ? -24.622 -9.796  2.490   1.00 59.89  ? 189 GLN B O   1 
ATOM   4989 C  CB  . GLN B 1 189 ? -22.863 -11.721 1.086   1.00 65.30  ? 189 GLN B CB  1 
ATOM   4990 C  CG  . GLN B 1 189 ? -23.512 -11.877 -0.284  1.00 69.89  ? 189 GLN B CG  1 
ATOM   4991 C  CD  . GLN B 1 189 ? -22.729 -11.143 -1.349  1.00 77.10  ? 189 GLN B CD  1 
ATOM   4992 O  OE1 . GLN B 1 189 ? -23.254 -10.289 -2.064  1.00 80.95  ? 189 GLN B OE1 1 
ATOM   4993 N  NE2 . GLN B 1 189 ? -21.440 -11.440 -1.428  1.00 71.66  ? 189 GLN B NE2 1 
ATOM   4994 N  N   . THR B 1 190 ? -23.885 -8.304  0.925   1.00 51.66  ? 190 THR B N   1 
ATOM   4995 C  CA  . THR B 1 190 ? -24.935 -7.273  1.106   1.00 51.11  ? 190 THR B CA  1 
ATOM   4996 C  C   . THR B 1 190 ? -24.887 -6.348  -0.112  1.00 53.34  ? 190 THR B C   1 
ATOM   4997 O  O   . THR B 1 190 ? -23.935 -6.470  -0.901  1.00 57.28  ? 190 THR B O   1 
ATOM   4998 C  CB  . THR B 1 190 ? -24.753 -6.557  2.448   1.00 51.08  ? 190 THR B CB  1 
ATOM   4999 O  OG1 . THR B 1 190 ? -25.964 -5.891  2.795   1.00 50.28  ? 190 THR B OG1 1 
ATOM   5000 C  CG2 . THR B 1 190 ? -23.628 -5.546  2.433   1.00 53.97  ? 190 THR B CG2 1 
ATOM   5001 N  N   . ALA B 1 191 ? -25.903 -5.496  -0.267  1.00 57.96  ? 191 ALA B N   1 
ATOM   5002 C  CA  . ALA B 1 191 ? -26.050 -4.537  -1.385  1.00 56.35  ? 191 ALA B CA  1 
ATOM   5003 C  C   . ALA B 1 191 ? -25.086 -3.375  -1.141  1.00 49.10  ? 191 ALA B C   1 
ATOM   5004 O  O   . ALA B 1 191 ? -25.357 -2.572  -0.237  1.00 52.77  ? 191 ALA B O   1 
ATOM   5005 C  CB  . ALA B 1 191 ? -27.487 -4.065  -1.473  1.00 53.17  ? 191 ALA B CB  1 
ATOM   5006 N  N   . GLN B 1 192 ? -23.988 -3.308  -1.891  1.00 45.82  ? 192 GLN B N   1 
ATOM   5007 C  CA  . GLN B 1 192 ? -22.984 -2.211  -1.777  1.00 41.12  ? 192 GLN B CA  1 
ATOM   5008 C  C   . GLN B 1 192 ? -22.675 -1.704  -3.182  1.00 41.26  ? 192 GLN B C   1 
ATOM   5009 O  O   . GLN B 1 192 ? -22.426 -2.537  -4.071  1.00 45.94  ? 192 GLN B O   1 
ATOM   5010 C  CB  . GLN B 1 192 ? -21.705 -2.690  -1.084  1.00 38.42  ? 192 GLN B CB  1 
ATOM   5011 C  CG  . GLN B 1 192 ? -21.967 -3.428  0.214   1.00 34.66  ? 192 GLN B CG  1 
ATOM   5012 C  CD  . GLN B 1 192 ? -20.721 -3.626  1.029   1.00 31.83  ? 192 GLN B CD  1 
ATOM   5013 O  OE1 . GLN B 1 192 ? -20.133 -2.676  1.550   1.00 26.59  ? 192 GLN B OE1 1 
ATOM   5014 N  NE2 . GLN B 1 192 ? -20.333 -4.878  1.164   1.00 29.79  ? 192 GLN B NE2 1 
ATOM   5015 N  N   . ALA B 1 193 ? -22.736 -0.390  -3.366  1.00 39.25  ? 193 ALA B N   1 
ATOM   5016 C  CA  . ALA B 1 193 ? -22.414 0.307   -4.629  1.00 39.10  ? 193 ALA B CA  1 
ATOM   5017 C  C   . ALA B 1 193 ? -21.355 1.369   -4.333  1.00 41.46  ? 193 ALA B C   1 
ATOM   5018 O  O   . ALA B 1 193 ? -21.439 2.029   -3.278  1.00 38.05  ? 193 ALA B O   1 
ATOM   5019 C  CB  . ALA B 1 193 ? -23.649 0.944   -5.223  1.00 37.05  ? 193 ALA B CB  1 
ATOM   5020 N  N   . ALA B 1 194 ? -20.411 1.529   -5.253  1.00 42.62  ? 194 ALA B N   1 
ATOM   5021 C  CA  . ALA B 1 194 ? -19.472 2.669   -5.289  1.00 46.80  ? 194 ALA B CA  1 
ATOM   5022 C  C   . ALA B 1 194 ? -20.267 3.965   -5.469  1.00 45.35  ? 194 ALA B C   1 
ATOM   5023 O  O   . ALA B 1 194 ? -21.227 3.950   -6.283  1.00 45.80  ? 194 ALA B O   1 
ATOM   5024 C  CB  . ALA B 1 194 ? -18.495 2.458   -6.417  1.00 49.57  ? 194 ALA B CB  1 
ATOM   5025 N  N   . GLY B 1 195 ? -19.903 5.016   -4.722  1.00 41.92  ? 195 GLY B N   1 
ATOM   5026 C  CA  . GLY B 1 195 ? -20.290 6.411   -5.000  1.00 40.24  ? 195 GLY B CA  1 
ATOM   5027 C  C   . GLY B 1 195 ? -20.037 6.767   -6.457  1.00 42.58  ? 195 GLY B C   1 
ATOM   5028 O  O   . GLY B 1 195 ? -19.266 6.053   -7.144  1.00 40.66  ? 195 GLY B O   1 
ATOM   5029 N  N   . THR B 1 196 ? -20.699 7.794   -6.978  1.00 42.16  ? 196 THR B N   1 
ATOM   5030 C  CA  . THR B 1 196 ? -20.366 8.313   -8.328  1.00 43.87  ? 196 THR B CA  1 
ATOM   5031 C  C   . THR B 1 196 ? -18.926 8.833   -8.217  1.00 41.68  ? 196 THR B C   1 
ATOM   5032 O  O   . THR B 1 196 ? -18.598 9.588   -7.268  1.00 40.79  ? 196 THR B O   1 
ATOM   5033 C  CB  . THR B 1 196 ? -21.412 9.307   -8.865  1.00 47.33  ? 196 THR B CB  1 
ATOM   5034 O  OG1 . THR B 1 196 ? -21.544 10.376  -7.931  1.00 47.02  ? 196 THR B OG1 1 
ATOM   5035 C  CG2 . THR B 1 196 ? -22.767 8.671   -9.116  1.00 44.19  ? 196 THR B CG2 1 
ATOM   5036 N  N   . ASP B 1 197 ? -18.079 8.379   -9.119  1.00 37.50  ? 197 ASP B N   1 
ATOM   5037 C  CA  . ASP B 1 197 ? -16.627 8.652   -9.084  1.00 37.54  ? 197 ASP B CA  1 
ATOM   5038 C  C   . ASP B 1 197 ? -16.341 10.012  -9.721  1.00 36.60  ? 197 ASP B C   1 
ATOM   5039 O  O   . ASP B 1 197 ? -17.209 10.557  -10.406 1.00 39.06  ? 197 ASP B O   1 
ATOM   5040 C  CB  . ASP B 1 197 ? -15.885 7.501   -9.754  1.00 37.28  ? 197 ASP B CB  1 
ATOM   5041 C  CG  . ASP B 1 197 ? -14.424 7.441   -9.361  1.00 36.01  ? 197 ASP B CG  1 
ATOM   5042 O  OD1 . ASP B 1 197 ? -14.028 8.071   -8.333  1.00 34.84  ? 197 ASP B OD1 1 
ATOM   5043 O  OD2 . ASP B 1 197 ? -13.711 6.773   -10.079 1.00 36.82  ? 197 ASP B OD2 1 
ATOM   5044 N  N   . THR B 1 198 ? -15.174 10.573  -9.434  1.00 38.60  ? 198 THR B N   1 
ATOM   5045 C  CA  . THR B 1 198 ? -14.716 11.857  -10.004 1.00 37.57  ? 198 THR B CA  1 
ATOM   5046 C  C   . THR B 1 198 ? -13.340 11.666  -10.642 1.00 37.70  ? 198 THR B C   1 
ATOM   5047 O  O   . THR B 1 198 ? -12.661 10.651  -10.348 1.00 34.78  ? 198 THR B O   1 
ATOM   5048 C  CB  . THR B 1 198 ? -14.693 12.973  -8.957  1.00 38.46  ? 198 THR B CB  1 
ATOM   5049 O  OG1 . THR B 1 198 ? -14.221 12.477  -7.707  1.00 34.63  ? 198 THR B OG1 1 
ATOM   5050 C  CG2 . THR B 1 198 ? -16.059 13.594  -8.786  1.00 43.21  ? 198 THR B CG2 1 
ATOM   5051 N  N   . THR B 1 199 ? -12.941 12.638  -11.455 1.00 34.05  ? 199 THR B N   1 
ATOM   5052 C  CA  . THR B 1 199 ? -11.654 12.613  -12.185 1.00 33.71  ? 199 THR B CA  1 
ATOM   5053 C  C   . THR B 1 199 ? -10.608 13.296  -11.318 1.00 31.45  ? 199 THR B C   1 
ATOM   5054 O  O   . THR B 1 199 ? -10.916 14.369  -10.723 1.00 29.81  ? 199 THR B O   1 
ATOM   5055 C  CB  . THR B 1 199 ? -11.768 13.262  -13.567 1.00 33.06  ? 199 THR B CB  1 
ATOM   5056 O  OG1 . THR B 1 199 ? -12.715 12.486  -14.282 1.00 33.84  ? 199 THR B OG1 1 
ATOM   5057 C  CG2 . THR B 1 199 ? -10.456 13.272  -14.313 1.00 35.32  ? 199 THR B CG2 1 
ATOM   5058 N  N   . ILE B 1 200 ? -9.413  12.709  -11.273 1.00 27.46  ? 200 ILE B N   1 
ATOM   5059 C  CA  . ILE B 1 200 ? -8.324  13.221  -10.413 1.00 27.69  ? 200 ILE B CA  1 
ATOM   5060 C  C   . ILE B 1 200 ? -7.594  14.286  -11.232 1.00 29.88  ? 200 ILE B C   1 
ATOM   5061 O  O   . ILE B 1 200 ? -6.720  13.938  -12.026 1.00 30.69  ? 200 ILE B O   1 
ATOM   5062 C  CB  . ILE B 1 200 ? -7.431  12.081  -9.881  1.00 25.86  ? 200 ILE B CB  1 
ATOM   5063 C  CG1 . ILE B 1 200 ? -8.260  10.916  -9.319  1.00 25.59  ? 200 ILE B CG1 1 
ATOM   5064 C  CG2 . ILE B 1 200 ? -6.475  12.630  -8.844  1.00 24.54  ? 200 ILE B CG2 1 
ATOM   5065 C  CD1 . ILE B 1 200 ? -7.582  9.570   -9.465  1.00 27.15  ? 200 ILE B CD1 1 
ATOM   5066 N  N   . THR B 1 201 ? -7.932  15.552  -10.982 1.00 32.70  ? 201 THR B N   1 
ATOM   5067 C  CA  . THR B 1 201 ? -7.568  16.707  -11.836 1.00 30.64  ? 201 THR B CA  1 
ATOM   5068 C  C   . THR B 1 201 ? -6.053  16.857  -11.874 1.00 28.27  ? 201 THR B C   1 
ATOM   5069 O  O   . THR B 1 201 ? -5.506  17.148  -12.955 1.00 27.48  ? 201 THR B O   1 
ATOM   5070 C  CB  . THR B 1 201 ? -8.220  18.008  -11.335 1.00 29.93  ? 201 THR B CB  1 
ATOM   5071 O  OG1 . THR B 1 201 ? -9.606  17.710  -11.236 1.00 27.65  ? 201 THR B OG1 1 
ATOM   5072 C  CG2 . THR B 1 201 ? -7.979  19.185  -12.259 1.00 29.65  ? 201 THR B CG2 1 
ATOM   5073 N  N   . VAL B 1 202 ? -5.429  16.786  -10.707 1.00 24.95  ? 202 VAL B N   1 
ATOM   5074 C  CA  . VAL B 1 202 ? -3.972  17.027  -10.580 1.00 26.03  ? 202 VAL B CA  1 
ATOM   5075 C  C   . VAL B 1 202 ? -3.231  15.973  -11.427 1.00 24.83  ? 202 VAL B C   1 
ATOM   5076 O  O   . VAL B 1 202 ? -2.181  16.304  -11.991 1.00 25.47  ? 202 VAL B O   1 
ATOM   5077 C  CB  . VAL B 1 202 ? -3.527  17.064  -9.112  1.00 24.68  ? 202 VAL B CB  1 
ATOM   5078 C  CG1 . VAL B 1 202 ? -3.723  15.732  -8.403  1.00 26.52  ? 202 VAL B CG1 1 
ATOM   5079 C  CG2 . VAL B 1 202 ? -2.105  17.552  -9.007  1.00 23.86  ? 202 VAL B CG2 1 
ATOM   5080 N  N   . ASN B 1 203 ? -3.801  14.782  -11.542 1.00 23.97  ? 203 ASN B N   1 
ATOM   5081 C  CA  . ASN B 1 203 ? -3.179  13.637  -12.243 1.00 25.04  ? 203 ASN B CA  1 
ATOM   5082 C  C   . ASN B 1 203 ? -3.316  13.836  -13.746 1.00 23.02  ? 203 ASN B C   1 
ATOM   5083 O  O   . ASN B 1 203 ? -2.361  13.574  -14.444 1.00 25.02  ? 203 ASN B O   1 
ATOM   5084 C  CB  . ASN B 1 203 ? -3.788  12.316  -11.794 1.00 23.58  ? 203 ASN B CB  1 
ATOM   5085 C  CG  . ASN B 1 203 ? -3.347  11.903  -10.408 1.00 23.31  ? 203 ASN B CG  1 
ATOM   5086 O  OD1 . ASN B 1 203 ? -2.592  12.622  -9.753  1.00 21.88  ? 203 ASN B OD1 1 
ATOM   5087 N  ND2 . ASN B 1 203 ? -3.829  10.743  -9.971  1.00 22.35  ? 203 ASN B ND2 1 
ATOM   5088 N  N   . VAL B 1 204 ? -4.476  14.297  -14.201 1.00 27.10  ? 204 VAL B N   1 
ATOM   5089 C  CA  . VAL B 1 204 ? -4.732  14.640  -15.627 1.00 27.65  ? 204 VAL B CA  1 
ATOM   5090 C  C   . VAL B 1 204 ? -3.682  15.666  -16.042 1.00 27.71  ? 204 VAL B C   1 
ATOM   5091 O  O   . VAL B 1 204 ? -3.084  15.518  -17.127 1.00 27.31  ? 204 VAL B O   1 
ATOM   5092 C  CB  . VAL B 1 204 ? -6.155  15.190  -15.854 1.00 28.01  ? 204 VAL B CB  1 
ATOM   5093 C  CG1 . VAL B 1 204 ? -6.305  15.703  -17.277 1.00 28.59  ? 204 VAL B CG1 1 
ATOM   5094 C  CG2 . VAL B 1 204 ? -7.233  14.159  -15.561 1.00 27.37  ? 204 VAL B CG2 1 
ATOM   5095 N  N   . LEU B 1 205 ? -3.482  16.683  -15.208 1.00 26.33  ? 205 LEU B N   1 
ATOM   5096 C  CA  . LEU B 1 205 ? -2.534  17.786  -15.498 1.00 26.43  ? 205 LEU B CA  1 
ATOM   5097 C  C   . LEU B 1 205 ? -1.133  17.204  -15.601 1.00 27.53  ? 205 LEU B C   1 
ATOM   5098 O  O   . LEU B 1 205 ? -0.444  17.536  -16.574 1.00 27.93  ? 205 LEU B O   1 
ATOM   5099 C  CB  . LEU B 1 205 ? -2.612  18.865  -14.411 1.00 27.71  ? 205 LEU B CB  1 
ATOM   5100 C  CG  . LEU B 1 205 ? -3.852  19.752  -14.507 1.00 31.54  ? 205 LEU B CG  1 
ATOM   5101 C  CD1 . LEU B 1 205 ? -3.949  20.701  -13.309 1.00 33.56  ? 205 LEU B CD1 1 
ATOM   5102 C  CD2 . LEU B 1 205 ? -3.841  20.544  -15.808 1.00 31.12  ? 205 LEU B CD2 1 
ATOM   5103 N  N   . ALA B 1 206 ? -0.747  16.348  -14.649 1.00 25.65  ? 206 ALA B N   1 
ATOM   5104 C  CA  . ALA B 1 206 ? 0.580   15.693  -14.623 1.00 25.21  ? 206 ALA B CA  1 
ATOM   5105 C  C   . ALA B 1 206 ? 0.799   14.966  -15.956 1.00 24.93  ? 206 ALA B C   1 
ATOM   5106 O  O   . ALA B 1 206 ? 1.920   15.002  -16.483 1.00 25.24  ? 206 ALA B O   1 
ATOM   5107 C  CB  . ALA B 1 206 ? 0.658   14.743  -13.440 1.00 26.16  ? 206 ALA B CB  1 
ATOM   5108 N  N   . TRP B 1 207 ? -0.244  14.291  -16.437 1.00 24.35  ? 207 TRP B N   1 
ATOM   5109 C  CA  . TRP B 1 207 ? -0.234  13.454  -17.670 1.00 24.76  ? 207 TRP B CA  1 
ATOM   5110 C  C   . TRP B 1 207 ? -0.123  14.343  -18.924 1.00 25.92  ? 207 TRP B C   1 
ATOM   5111 O  O   . TRP B 1 207 ? 0.579   13.947  -19.887 1.00 22.47  ? 207 TRP B O   1 
ATOM   5112 C  CB  . TRP B 1 207 ? -1.486  12.577  -17.687 1.00 24.31  ? 207 TRP B CB  1 
ATOM   5113 C  CG  . TRP B 1 207 ? -1.718  11.780  -18.930 1.00 25.35  ? 207 TRP B CG  1 
ATOM   5114 C  CD1 . TRP B 1 207 ? -1.104  10.623  -19.327 1.00 26.69  ? 207 TRP B CD1 1 
ATOM   5115 C  CD2 . TRP B 1 207 ? -2.706  12.064  -19.925 1.00 25.46  ? 207 TRP B CD2 1 
ATOM   5116 N  NE1 . TRP B 1 207 ? -1.613  10.202  -20.533 1.00 24.51  ? 207 TRP B NE1 1 
ATOM   5117 C  CE2 . TRP B 1 207 ? -2.606  11.057  -20.910 1.00 25.39  ? 207 TRP B CE2 1 
ATOM   5118 C  CE3 . TRP B 1 207 ? -3.623  13.106  -20.096 1.00 26.96  ? 207 TRP B CE3 1 
ATOM   5119 C  CZ2 . TRP B 1 207 ? -3.402  11.061  -22.048 1.00 26.73  ? 207 TRP B CZ2 1 
ATOM   5120 C  CZ3 . TRP B 1 207 ? -4.446  13.078  -21.199 1.00 28.27  ? 207 TRP B CZ3 1 
ATOM   5121 C  CH2 . TRP B 1 207 ? -4.339  12.064  -22.156 1.00 27.07  ? 207 TRP B CH2 1 
ATOM   5122 N  N   . LEU B 1 208 ? -0.742  15.520  -18.902 1.00 25.62  ? 208 LEU B N   1 
ATOM   5123 C  CA  . LEU B 1 208 ? -0.583  16.532  -19.986 1.00 28.51  ? 208 LEU B CA  1 
ATOM   5124 C  C   . LEU B 1 208 ? 0.880   16.997  -20.029 1.00 29.41  ? 208 LEU B C   1 
ATOM   5125 O  O   . LEU B 1 208 ? 1.408   17.147  -21.148 1.00 32.12  ? 208 LEU B O   1 
ATOM   5126 C  CB  . LEU B 1 208 ? -1.550  17.707  -19.789 1.00 29.50  ? 208 LEU B CB  1 
ATOM   5127 C  CG  . LEU B 1 208 ? -3.018  17.380  -20.007 1.00 30.71  ? 208 LEU B CG  1 
ATOM   5128 C  CD1 . LEU B 1 208 ? -3.898  18.591  -19.728 1.00 33.50  ? 208 LEU B CD1 1 
ATOM   5129 C  CD2 . LEU B 1 208 ? -3.253  16.881  -21.419 1.00 32.72  ? 208 LEU B CD2 1 
ATOM   5130 N  N   . TYR B 1 209 ? 1.544   17.139  -18.882 1.00 28.24  ? 209 TYR B N   1 
ATOM   5131 C  CA  . TYR B 1 209 ? 2.990   17.441  -18.822 1.00 30.19  ? 209 TYR B CA  1 
ATOM   5132 C  C   . TYR B 1 209 ? 3.807   16.298  -19.454 1.00 32.36  ? 209 TYR B C   1 
ATOM   5133 O  O   . TYR B 1 209 ? 4.755   16.603  -20.224 1.00 30.74  ? 209 TYR B O   1 
ATOM   5134 C  CB  . TYR B 1 209 ? 3.437   17.723  -17.393 1.00 34.98  ? 209 TYR B CB  1 
ATOM   5135 C  CG  . TYR B 1 209 ? 3.135   19.128  -16.938 1.00 40.34  ? 209 TYR B CG  1 
ATOM   5136 C  CD1 . TYR B 1 209 ? 3.801   20.226  -17.470 1.00 40.49  ? 209 TYR B CD1 1 
ATOM   5137 C  CD2 . TYR B 1 209 ? 2.166   19.358  -15.980 1.00 42.63  ? 209 TYR B CD2 1 
ATOM   5138 C  CE1 . TYR B 1 209 ? 3.509   21.517  -17.050 1.00 42.14  ? 209 TYR B CE1 1 
ATOM   5139 C  CE2 . TYR B 1 209 ? 1.859   20.641  -15.557 1.00 45.88  ? 209 TYR B CE2 1 
ATOM   5140 C  CZ  . TYR B 1 209 ? 2.535   21.727  -16.088 1.00 45.08  ? 209 TYR B CZ  1 
ATOM   5141 O  OH  . TYR B 1 209 ? 2.209   22.978  -15.643 1.00 40.74  ? 209 TYR B OH  1 
ATOM   5142 N  N   . ALA B 1 210 ? 3.489   15.045  -19.124 1.00 26.62  ? 210 ALA B N   1 
ATOM   5143 C  CA  . ALA B 1 210 ? 4.111   13.841  -19.722 1.00 25.99  ? 210 ALA B CA  1 
ATOM   5144 C  C   . ALA B 1 210 ? 3.973   13.911  -21.247 1.00 24.58  ? 210 ALA B C   1 
ATOM   5145 O  O   . ALA B 1 210 ? 4.942   13.605  -21.950 1.00 23.96  ? 210 ALA B O   1 
ATOM   5146 C  CB  . ALA B 1 210 ? 3.459   12.600  -19.176 1.00 26.07  ? 210 ALA B CB  1 
ATOM   5147 N  N   . ALA B 1 211 ? 2.809   14.323  -21.735 1.00 24.20  ? 211 ALA B N   1 
ATOM   5148 C  CA  . ALA B 1 211 ? 2.507   14.354  -23.179 1.00 27.42  ? 211 ALA B CA  1 
ATOM   5149 C  C   . ALA B 1 211 ? 3.419   15.407  -23.814 1.00 30.68  ? 211 ALA B C   1 
ATOM   5150 O  O   . ALA B 1 211 ? 4.102   15.088  -24.789 1.00 28.18  ? 211 ALA B O   1 
ATOM   5151 C  CB  . ALA B 1 211 ? 1.051   14.633  -23.413 1.00 27.05  ? 211 ALA B CB  1 
ATOM   5152 N  N   . VAL B 1 212 ? 3.488   16.596  -23.212 1.00 30.67  ? 212 VAL B N   1 
ATOM   5153 C  CA  . VAL B 1 212 ? 4.350   17.711  -23.705 1.00 30.73  ? 212 VAL B CA  1 
ATOM   5154 C  C   . VAL B 1 212 ? 5.807   17.238  -23.700 1.00 28.39  ? 212 VAL B C   1 
ATOM   5155 O  O   . VAL B 1 212 ? 6.440   17.277  -24.743 1.00 29.46  ? 212 VAL B O   1 
ATOM   5156 C  CB  . VAL B 1 212 ? 4.160   18.988  -22.866 1.00 29.33  ? 212 VAL B CB  1 
ATOM   5157 C  CG1 . VAL B 1 212 ? 5.205   20.042  -23.214 1.00 29.55  ? 212 VAL B CG1 1 
ATOM   5158 C  CG2 . VAL B 1 212 ? 2.746   19.521  -23.004 1.00 28.80  ? 212 VAL B CG2 1 
ATOM   5159 N  N   . ILE B 1 213 ? 6.298   16.722  -22.585 1.00 28.96  ? 213 ILE B N   1 
ATOM   5160 C  CA  . ILE B 1 213 ? 7.681   16.167  -22.484 1.00 30.70  ? 213 ILE B CA  1 
ATOM   5161 C  C   . ILE B 1 213 ? 7.966   15.179  -23.629 1.00 30.79  ? 213 ILE B C   1 
ATOM   5162 O  O   . ILE B 1 213 ? 9.112   15.161  -24.093 1.00 28.15  ? 213 ILE B O   1 
ATOM   5163 C  CB  . ILE B 1 213 ? 7.920   15.546  -21.097 1.00 35.29  ? 213 ILE B CB  1 
ATOM   5164 C  CG1 . ILE B 1 213 ? 7.893   16.627  -20.013 1.00 36.02  ? 213 ILE B CG1 1 
ATOM   5165 C  CG2 . ILE B 1 213 ? 9.213   14.740  -21.081 1.00 38.20  ? 213 ILE B CG2 1 
ATOM   5166 C  CD1 . ILE B 1 213 ? 7.874   16.115  -18.598 1.00 36.94  ? 213 ILE B CD1 1 
ATOM   5167 N  N   . ASN B 1 214 ? 6.975   14.418  -24.091 1.00 31.31  ? 214 ASN B N   1 
ATOM   5168 C  CA  . ASN B 1 214 ? 7.123   13.398  -25.165 1.00 32.39  ? 214 ASN B CA  1 
ATOM   5169 C  C   . ASN B 1 214 ? 6.733   13.949  -26.549 1.00 34.99  ? 214 ASN B C   1 
ATOM   5170 O  O   . ASN B 1 214 ? 6.474   13.128  -27.456 1.00 35.96  ? 214 ASN B O   1 
ATOM   5171 C  CB  . ASN B 1 214 ? 6.297   12.166  -24.811 1.00 31.90  ? 214 ASN B CB  1 
ATOM   5172 C  CG  . ASN B 1 214 ? 6.992   11.388  -23.723 1.00 31.34  ? 214 ASN B CG  1 
ATOM   5173 O  OD1 . ASN B 1 214 ? 7.901   10.618  -24.009 1.00 32.45  ? 214 ASN B OD1 1 
ATOM   5174 N  ND2 . ASN B 1 214 ? 6.632   11.647  -22.479 1.00 31.18  ? 214 ASN B ND2 1 
ATOM   5175 N  N   . GLY B 1 215 ? 6.646   15.274  -26.707 1.00 34.30  ? 215 GLY B N   1 
ATOM   5176 C  CA  . GLY B 1 215 ? 6.468   15.926  -28.018 1.00 34.40  ? 215 GLY B CA  1 
ATOM   5177 C  C   . GLY B 1 215 ? 5.023   16.090  -28.442 1.00 34.85  ? 215 GLY B C   1 
ATOM   5178 O  O   . GLY B 1 215 ? 4.816   16.586  -29.534 1.00 34.43  ? 215 GLY B O   1 
ATOM   5179 N  N   . ASP B 1 216 ? 4.049   15.700  -27.624 1.00 38.23  ? 216 ASP B N   1 
ATOM   5180 C  CA  . ASP B 1 216 ? 2.605   15.793  -27.965 1.00 39.34  ? 216 ASP B CA  1 
ATOM   5181 C  C   . ASP B 1 216 ? 2.100   17.146  -27.434 1.00 42.10  ? 216 ASP B C   1 
ATOM   5182 O  O   . ASP B 1 216 ? 1.719   17.199  -26.257 1.00 44.04  ? 216 ASP B O   1 
ATOM   5183 C  CB  . ASP B 1 216 ? 1.880   14.576  -27.383 1.00 40.83  ? 216 ASP B CB  1 
ATOM   5184 C  CG  . ASP B 1 216 ? 0.900   13.902  -28.312 1.00 41.98  ? 216 ASP B CG  1 
ATOM   5185 O  OD1 . ASP B 1 216 ? 0.613   14.470  -29.376 1.00 45.46  ? 216 ASP B OD1 1 
ATOM   5186 O  OD2 . ASP B 1 216 ? 0.422   12.809  -27.954 1.00 40.46  ? 216 ASP B OD2 1 
ATOM   5187 N  N   . ARG B 1 217 ? 2.136   18.207  -28.246 1.00 41.05  ? 217 ARG B N   1 
ATOM   5188 C  CA  . ARG B 1 217 ? 2.052   19.613  -27.770 1.00 43.60  ? 217 ARG B CA  1 
ATOM   5189 C  C   . ARG B 1 217 ? 0.790   20.310  -28.279 1.00 40.92  ? 217 ARG B C   1 
ATOM   5190 O  O   . ARG B 1 217 ? 0.575   21.452  -27.889 1.00 43.77  ? 217 ARG B O   1 
ATOM   5191 C  CB  . ARG B 1 217 ? 3.264   20.427  -28.240 1.00 47.36  ? 217 ARG B CB  1 
ATOM   5192 C  CG  . ARG B 1 217 ? 4.601   19.918  -27.726 1.00 55.43  ? 217 ARG B CG  1 
ATOM   5193 C  CD  . ARG B 1 217 ? 5.745   20.819  -28.162 1.00 61.39  ? 217 ARG B CD  1 
ATOM   5194 N  NE  . ARG B 1 217 ? 5.523   22.201  -27.747 1.00 62.69  ? 217 ARG B NE  1 
ATOM   5195 C  CZ  . ARG B 1 217 ? 6.003   22.772  -26.634 1.00 64.69  ? 217 ARG B CZ  1 
ATOM   5196 N  NH1 . ARG B 1 217 ? 6.764   22.098  -25.783 1.00 65.62  ? 217 ARG B NH1 1 
ATOM   5197 N  NH2 . ARG B 1 217 ? 5.703   24.032  -26.369 1.00 65.30  ? 217 ARG B NH2 1 
ATOM   5198 N  N   . TRP B 1 218 ? -0.033  19.653  -29.090 1.00 41.72  ? 218 TRP B N   1 
ATOM   5199 C  CA  . TRP B 1 218 ? -1.083  20.317  -29.903 1.00 38.62  ? 218 TRP B CA  1 
ATOM   5200 C  C   . TRP B 1 218 ? -2.061  21.138  -29.052 1.00 41.44  ? 218 TRP B C   1 
ATOM   5201 O  O   . TRP B 1 218 ? -2.527  22.168  -29.557 1.00 42.27  ? 218 TRP B O   1 
ATOM   5202 C  CB  . TRP B 1 218 ? -1.815  19.312  -30.791 1.00 36.94  ? 218 TRP B CB  1 
ATOM   5203 C  CG  . TRP B 1 218 ? -2.520  18.183  -30.117 1.00 40.28  ? 218 TRP B CG  1 
ATOM   5204 C  CD1 . TRP B 1 218 ? -2.089  16.890  -30.034 1.00 42.30  ? 218 TRP B CD1 1 
ATOM   5205 C  CD2 . TRP B 1 218 ? -3.847  18.199  -29.554 1.00 44.31  ? 218 TRP B CD2 1 
ATOM   5206 N  NE1 . TRP B 1 218 ? -3.040  16.108  -29.430 1.00 44.16  ? 218 TRP B NE1 1 
ATOM   5207 C  CE2 . TRP B 1 218 ? -4.129  16.883  -29.125 1.00 42.58  ? 218 TRP B CE2 1 
ATOM   5208 C  CE3 . TRP B 1 218 ? -4.819  19.194  -29.367 1.00 48.47  ? 218 TRP B CE3 1 
ATOM   5209 C  CZ2 . TRP B 1 218 ? -5.334  16.544  -28.509 1.00 47.32  ? 218 TRP B CZ2 1 
ATOM   5210 C  CZ3 . TRP B 1 218 ? -6.008  18.857  -28.755 1.00 48.75  ? 218 TRP B CZ3 1 
ATOM   5211 C  CH2 . TRP B 1 218 ? -6.257  17.552  -28.323 1.00 49.20  ? 218 TRP B CH2 1 
ATOM   5212 N  N   . PHE B 1 219 ? -2.377  20.681  -27.838 1.00 41.88  ? 219 PHE B N   1 
ATOM   5213 C  CA  . PHE B 1 219 ? -3.489  21.166  -26.975 1.00 38.59  ? 219 PHE B CA  1 
ATOM   5214 C  C   . PHE B 1 219 ? -3.025  22.385  -26.187 1.00 35.44  ? 219 PHE B C   1 
ATOM   5215 O  O   . PHE B 1 219 ? -3.836  22.987  -25.468 1.00 41.47  ? 219 PHE B O   1 
ATOM   5216 C  CB  . PHE B 1 219 ? -3.953  20.067  -26.009 1.00 37.53  ? 219 PHE B CB  1 
ATOM   5217 C  CG  . PHE B 1 219 ? -2.812  19.388  -25.292 1.00 36.55  ? 219 PHE B CG  1 
ATOM   5218 C  CD1 . PHE B 1 219 ? -2.235  19.961  -24.170 1.00 35.26  ? 219 PHE B CD1 1 
ATOM   5219 C  CD2 . PHE B 1 219 ? -2.275  18.197  -25.770 1.00 35.38  ? 219 PHE B CD2 1 
ATOM   5220 C  CE1 . PHE B 1 219 ? -1.170  19.349  -23.531 1.00 35.22  ? 219 PHE B CE1 1 
ATOM   5221 C  CE2 . PHE B 1 219 ? -1.215  17.582  -25.121 1.00 31.47  ? 219 PHE B CE2 1 
ATOM   5222 C  CZ  . PHE B 1 219 ? -0.661  18.161  -24.008 1.00 31.91  ? 219 PHE B CZ  1 
ATOM   5223 N  N   . LEU B 1 220 ? -1.746  22.724  -26.256 1.00 33.92  ? 220 LEU B N   1 
ATOM   5224 C  CA  . LEU B 1 220 ? -1.261  23.937  -25.571 1.00 38.94  ? 220 LEU B CA  1 
ATOM   5225 C  C   . LEU B 1 220 ? -1.894  25.142  -26.262 1.00 42.24  ? 220 LEU B C   1 
ATOM   5226 O  O   . LEU B 1 220 ? -2.312  25.002  -27.427 1.00 40.39  ? 220 LEU B O   1 
ATOM   5227 C  CB  . LEU B 1 220 ? 0.259   24.021  -25.620 1.00 41.39  ? 220 LEU B CB  1 
ATOM   5228 C  CG  . LEU B 1 220 ? 0.979   22.865  -24.947 1.00 44.69  ? 220 LEU B CG  1 
ATOM   5229 C  CD1 . LEU B 1 220 ? 2.475   23.068  -25.053 1.00 44.34  ? 220 LEU B CD1 1 
ATOM   5230 C  CD2 . LEU B 1 220 ? 0.535   22.703  -23.494 1.00 46.54  ? 220 LEU B CD2 1 
ATOM   5231 N  N   . ASN B 1 221 ? -1.990  26.261  -25.544 1.00 42.04  ? 221 ASN B N   1 
ATOM   5232 C  CA  . ASN B 1 221 ? -2.588  27.512  -26.075 1.00 38.08  ? 221 ASN B CA  1 
ATOM   5233 C  C   . ASN B 1 221 ? -1.956  28.709  -25.371 1.00 38.22  ? 221 ASN B C   1 
ATOM   5234 O  O   . ASN B 1 221 ? -1.176  28.514  -24.431 1.00 32.94  ? 221 ASN B O   1 
ATOM   5235 C  CB  . ASN B 1 221 ? -4.115  27.472  -26.052 1.00 35.79  ? 221 ASN B CB  1 
ATOM   5236 C  CG  . ASN B 1 221 ? -4.728  27.306  -24.678 1.00 39.14  ? 221 ASN B CG  1 
ATOM   5237 O  OD1 . ASN B 1 221 ? -4.195  27.774  -23.663 1.00 36.66  ? 221 ASN B OD1 1 
ATOM   5238 N  ND2 . ASN B 1 221 ? -5.880  26.659  -24.660 1.00 33.78  ? 221 ASN B ND2 1 
ATOM   5239 N  N   . ARG B 1 222 ? -2.265  29.910  -25.857 1.00 39.28  ? 222 ARG B N   1 
ATOM   5240 C  CA  . ARG B 1 222 ? -1.632  31.173  -25.386 1.00 41.01  ? 222 ARG B CA  1 
ATOM   5241 C  C   . ARG B 1 222 ? -2.234  31.593  -24.038 1.00 34.29  ? 222 ARG B C   1 
ATOM   5242 O  O   . ARG B 1 222 ? -1.729  32.572  -23.466 1.00 34.45  ? 222 ARG B O   1 
ATOM   5243 C  CB  . ARG B 1 222 ? -1.782  32.284  -26.439 1.00 43.07  ? 222 ARG B CB  1 
ATOM   5244 C  CG  . ARG B 1 222 ? -3.196  32.504  -26.962 1.00 46.36  ? 222 ARG B CG  1 
ATOM   5245 C  CD  . ARG B 1 222 ? -3.409  33.780  -27.779 1.00 49.59  ? 222 ARG B CD  1 
ATOM   5246 N  NE  . ARG B 1 222 ? -2.440  34.055  -28.846 1.00 53.00  ? 222 ARG B NE  1 
ATOM   5247 C  CZ  . ARG B 1 222 ? -1.523  35.031  -28.813 1.00 52.58  ? 222 ARG B CZ  1 
ATOM   5248 N  NH1 . ARG B 1 222 ? -1.422  35.829  -27.759 1.00 56.95  ? 222 ARG B NH1 1 
ATOM   5249 N  NH2 . ARG B 1 222 ? -0.700  35.211  -29.834 1.00 55.04  ? 222 ARG B NH2 1 
ATOM   5250 N  N   . PHE B 1 223 ? -3.275  30.917  -23.563 1.00 33.46  ? 223 PHE B N   1 
ATOM   5251 C  CA  . PHE B 1 223 ? -4.148  31.419  -22.464 1.00 40.25  ? 223 PHE B CA  1 
ATOM   5252 C  C   . PHE B 1 223 ? -3.662  30.912  -21.102 1.00 45.43  ? 223 PHE B C   1 
ATOM   5253 O  O   . PHE B 1 223 ? -2.913  29.908  -21.002 1.00 46.01  ? 223 PHE B O   1 
ATOM   5254 C  CB  . PHE B 1 223 ? -5.611  31.037  -22.706 1.00 37.73  ? 223 PHE B CB  1 
ATOM   5255 C  CG  . PHE B 1 223 ? -6.126  31.523  -24.036 1.00 39.01  ? 223 PHE B CG  1 
ATOM   5256 C  CD1 . PHE B 1 223 ? -6.283  32.887  -24.291 1.00 40.79  ? 223 PHE B CD1 1 
ATOM   5257 C  CD2 . PHE B 1 223 ? -6.397  30.623  -25.057 1.00 39.04  ? 223 PHE B CD2 1 
ATOM   5258 C  CE1 . PHE B 1 223 ? -6.720  33.334  -25.534 1.00 37.80  ? 223 PHE B CE1 1 
ATOM   5259 C  CE2 . PHE B 1 223 ? -6.851  31.073  -26.289 1.00 39.59  ? 223 PHE B CE2 1 
ATOM   5260 C  CZ  . PHE B 1 223 ? -6.992  32.427  -26.533 1.00 41.24  ? 223 PHE B CZ  1 
ATOM   5261 N  N   . THR B 1 224 ? -4.088  31.615  -20.058 1.00 46.79  ? 224 THR B N   1 
ATOM   5262 C  CA  . THR B 1 224 ? -3.950  31.187  -18.647 1.00 48.48  ? 224 THR B CA  1 
ATOM   5263 C  C   . THR B 1 224 ? -5.302  31.399  -17.957 1.00 50.57  ? 224 THR B C   1 
ATOM   5264 O  O   . THR B 1 224 ? -6.280  31.800  -18.627 1.00 56.07  ? 224 THR B O   1 
ATOM   5265 C  CB  . THR B 1 224 ? -2.738  31.873  -18.011 1.00 51.76  ? 224 THR B CB  1 
ATOM   5266 O  OG1 . THR B 1 224 ? -2.527  31.195  -16.776 1.00 56.31  ? 224 THR B OG1 1 
ATOM   5267 C  CG2 . THR B 1 224 ? -2.920  33.362  -17.798 1.00 51.47  ? 224 THR B CG2 1 
ATOM   5268 N  N   . THR B 1 225 ? -5.401  31.070  -16.682 1.00 49.27  ? 225 THR B N   1 
ATOM   5269 C  CA  . THR B 1 225 ? -6.691  31.150  -15.964 1.00 49.01  ? 225 THR B CA  1 
ATOM   5270 C  C   . THR B 1 225 ? -6.418  31.291  -14.477 1.00 49.65  ? 225 THR B C   1 
ATOM   5271 O  O   . THR B 1 225 ? -5.272  31.628  -14.124 1.00 48.30  ? 225 THR B O   1 
ATOM   5272 C  CB  . THR B 1 225 ? -7.585  29.942  -16.242 1.00 49.93  ? 225 THR B CB  1 
ATOM   5273 O  OG1 . THR B 1 225 ? -8.857  30.224  -15.659 1.00 49.63  ? 225 THR B OG1 1 
ATOM   5274 C  CG2 . THR B 1 225 ? -7.043  28.656  -15.659 1.00 55.57  ? 225 THR B CG2 1 
ATOM   5275 N  N   . THR B 1 226 ? -7.453  31.063  -13.664 1.00 55.06  ? 226 THR B N   1 
ATOM   5276 C  CA  . THR B 1 226 ? -7.379  31.082  -12.177 1.00 57.23  ? 226 THR B CA  1 
ATOM   5277 C  C   . THR B 1 226 ? -8.048  29.829  -11.609 1.00 49.48  ? 226 THR B C   1 
ATOM   5278 O  O   . THR B 1 226 ? -8.986  29.271  -12.261 1.00 41.37  ? 226 THR B O   1 
ATOM   5279 C  CB  . THR B 1 226 ? -8.006  32.357  -11.593 1.00 53.65  ? 226 THR B CB  1 
ATOM   5280 O  OG1 . THR B 1 226 ? -9.390  32.388  -11.961 1.00 48.24  ? 226 THR B OG1 1 
ATOM   5281 C  CG2 . THR B 1 226 ? -7.278  33.602  -12.058 1.00 53.18  ? 226 THR B CG2 1 
ATOM   5282 N  N   . LEU B 1 227 ? -7.575  29.438  -10.427 1.00 53.15  ? 227 LEU B N   1 
ATOM   5283 C  CA  . LEU B 1 227 ? -8.104  28.307  -9.627  1.00 52.49  ? 227 LEU B CA  1 
ATOM   5284 C  C   . LEU B 1 227 ? -9.635  28.418  -9.550  1.00 55.66  ? 227 LEU B C   1 
ATOM   5285 O  O   . LEU B 1 227 ? -10.321 27.436  -9.935  1.00 54.05  ? 227 LEU B O   1 
ATOM   5286 C  CB  . LEU B 1 227 ? -7.424  28.353  -8.256  1.00 53.38  ? 227 LEU B CB  1 
ATOM   5287 C  CG  . LEU B 1 227 ? -6.991  27.008  -7.674  1.00 57.55  ? 227 LEU B CG  1 
ATOM   5288 C  CD1 . LEU B 1 227 ? -6.124  26.221  -8.646  1.00 60.52  ? 227 LEU B CD1 1 
ATOM   5289 C  CD2 . LEU B 1 227 ? -6.241  27.212  -6.364  1.00 57.86  ? 227 LEU B CD2 1 
ATOM   5290 N  N   . ASN B 1 228 ? -10.155 29.593  -9.165  1.00 54.74  ? 228 ASN B N   1 
ATOM   5291 C  CA  . ASN B 1 228 ? -11.609 29.817  -8.943  1.00 57.62  ? 228 ASN B CA  1 
ATOM   5292 C  C   . ASN B 1 228 ? -12.361 29.588  -10.254 1.00 52.80  ? 228 ASN B C   1 
ATOM   5293 O  O   . ASN B 1 228 ? -13.379 28.883  -10.253 1.00 56.74  ? 228 ASN B O   1 
ATOM   5294 C  CB  . ASN B 1 228 ? -11.915 31.226  -8.429  1.00 63.51  ? 228 ASN B CB  1 
ATOM   5295 C  CG  . ASN B 1 228 ? -11.335 31.505  -7.062  1.00 67.42  ? 228 ASN B CG  1 
ATOM   5296 O  OD1 . ASN B 1 228 ? -10.147 31.281  -6.823  1.00 66.77  ? 228 ASN B OD1 1 
ATOM   5297 N  ND2 . ASN B 1 228 ? -12.168 32.018  -6.173  1.00 72.98  ? 228 ASN B ND2 1 
ATOM   5298 N  N   . ASP B 1 229 ? -11.875 30.196  -11.332 1.00 55.88  ? 229 ASP B N   1 
ATOM   5299 C  CA  . ASP B 1 229 ? -12.453 30.056  -12.692 1.00 55.47  ? 229 ASP B CA  1 
ATOM   5300 C  C   . ASP B 1 229 ? -12.398 28.581  -13.093 1.00 52.25  ? 229 ASP B C   1 
ATOM   5301 O  O   . ASP B 1 229 ? -13.462 28.016  -13.491 1.00 45.48  ? 229 ASP B O   1 
ATOM   5302 C  CB  . ASP B 1 229 ? -11.704 30.945  -13.690 1.00 63.58  ? 229 ASP B CB  1 
ATOM   5303 C  CG  . ASP B 1 229 ? -12.148 32.396  -13.642 1.00 68.35  ? 229 ASP B CG  1 
ATOM   5304 O  OD1 . ASP B 1 229 ? -13.296 32.655  -14.051 1.00 66.04  ? 229 ASP B OD1 1 
ATOM   5305 O  OD2 . ASP B 1 229 ? -11.358 33.245  -13.164 1.00 68.76  ? 229 ASP B OD2 1 
ATOM   5306 N  N   . PHE B 1 230 ? -11.209 27.973  -12.995 1.00 48.95  ? 230 PHE B N   1 
ATOM   5307 C  CA  . PHE B 1 230 ? -11.010 26.561  -13.421 1.00 46.86  ? 230 PHE B CA  1 
ATOM   5308 C  C   . PHE B 1 230 ? -11.961 25.653  -12.627 1.00 45.90  ? 230 PHE B C   1 
ATOM   5309 O  O   . PHE B 1 230 ? -12.660 24.794  -13.240 1.00 47.33  ? 230 PHE B O   1 
ATOM   5310 C  CB  . PHE B 1 230 ? -9.555  26.119  -13.278 1.00 47.35  ? 230 PHE B CB  1 
ATOM   5311 C  CG  . PHE B 1 230 ? -9.362  24.691  -13.719 1.00 49.55  ? 230 PHE B CG  1 
ATOM   5312 C  CD1 . PHE B 1 230 ? -9.382  24.358  -15.067 1.00 45.94  ? 230 PHE B CD1 1 
ATOM   5313 C  CD2 . PHE B 1 230 ? -9.237  23.672  -12.785 1.00 44.21  ? 230 PHE B CD2 1 
ATOM   5314 C  CE1 . PHE B 1 230 ? -9.242  23.039  -15.469 1.00 46.42  ? 230 PHE B CE1 1 
ATOM   5315 C  CE2 . PHE B 1 230 ? -9.100  22.361  -13.194 1.00 39.28  ? 230 PHE B CE2 1 
ATOM   5316 C  CZ  . PHE B 1 230 ? -9.107  22.048  -14.530 1.00 41.67  ? 230 PHE B CZ  1 
ATOM   5317 N  N   . ASN B 1 231 ? -12.041 25.872  -11.309 1.00 44.28  ? 231 ASN B N   1 
ATOM   5318 C  CA  . ASN B 1 231 ? -12.698 24.940  -10.353 1.00 42.66  ? 231 ASN B CA  1 
ATOM   5319 C  C   . ASN B 1 231 ? -14.209 24.949  -10.569 1.00 47.96  ? 231 ASN B C   1 
ATOM   5320 O  O   . ASN B 1 231 ? -14.843 23.888  -10.388 1.00 54.16  ? 231 ASN B O   1 
ATOM   5321 C  CB  . ASN B 1 231 ? -12.235 25.225  -8.923  1.00 44.12  ? 231 ASN B CB  1 
ATOM   5322 C  CG  . ASN B 1 231 ? -10.995 24.421  -8.589  1.00 43.46  ? 231 ASN B CG  1 
ATOM   5323 O  OD1 . ASN B 1 231 ? -10.941 23.241  -8.945  1.00 45.71  ? 231 ASN B OD1 1 
ATOM   5324 N  ND2 . ASN B 1 231 ? -9.996  25.033  -7.961  1.00 36.24  ? 231 ASN B ND2 1 
ATOM   5325 N  N   . LEU B 1 232 ? -14.760 26.076  -11.020 1.00 56.04  ? 232 LEU B N   1 
ATOM   5326 C  CA  . LEU B 1 232 ? -16.174 26.166  -11.469 1.00 57.60  ? 232 LEU B CA  1 
ATOM   5327 C  C   . LEU B 1 232 ? -16.374 25.310  -12.726 1.00 53.21  ? 232 LEU B C   1 
ATOM   5328 O  O   . LEU B 1 232 ? -17.453 24.721  -12.863 1.00 51.59  ? 232 LEU B O   1 
ATOM   5329 C  CB  . LEU B 1 232 ? -16.517 27.638  -11.708 1.00 68.58  ? 232 LEU B CB  1 
ATOM   5330 C  CG  . LEU B 1 232 ? -16.598 28.494  -10.439 1.00 72.92  ? 232 LEU B CG  1 
ATOM   5331 C  CD1 . LEU B 1 232 ? -16.378 29.973  -10.749 1.00 66.50  ? 232 LEU B CD1 1 
ATOM   5332 C  CD2 . LEU B 1 232 ? -17.928 28.263  -9.719  1.00 70.30  ? 232 LEU B CD2 1 
ATOM   5333 N  N   . VAL B 1 233 ? -15.368 25.231  -13.602 1.00 58.69  ? 233 VAL B N   1 
ATOM   5334 C  CA  . VAL B 1 233 ? -15.377 24.313  -14.785 1.00 62.03  ? 233 VAL B CA  1 
ATOM   5335 C  C   . VAL B 1 233 ? -15.192 22.868  -14.292 1.00 58.20  ? 233 VAL B C   1 
ATOM   5336 O  O   . VAL B 1 233 ? -15.983 22.002  -14.719 1.00 58.76  ? 233 VAL B O   1 
ATOM   5337 C  CB  . VAL B 1 233 ? -14.325 24.710  -15.845 1.00 64.21  ? 233 VAL B CB  1 
ATOM   5338 C  CG1 . VAL B 1 233 ? -14.346 23.775  -17.048 1.00 63.09  ? 233 VAL B CG1 1 
ATOM   5339 C  CG2 . VAL B 1 233 ? -14.503 26.152  -16.301 1.00 61.33  ? 233 VAL B CG2 1 
ATOM   5340 N  N   . ALA B 1 234 ? -14.213 22.607  -13.416 1.00 56.97  ? 234 ALA B N   1 
ATOM   5341 C  CA  . ALA B 1 234 ? -13.931 21.248  -12.878 1.00 57.14  ? 234 ALA B CA  1 
ATOM   5342 C  C   . ALA B 1 234 ? -15.204 20.657  -12.254 1.00 56.26  ? 234 ALA B C   1 
ATOM   5343 O  O   . ALA B 1 234 ? -15.697 19.601  -12.745 1.00 52.21  ? 234 ALA B O   1 
ATOM   5344 C  CB  . ALA B 1 234 ? -12.805 21.297  -11.874 1.00 59.11  ? 234 ALA B CB  1 
ATOM   5345 N  N   . MET B 1 235 ? -15.740 21.331  -11.228 1.00 58.04  ? 235 MET B N   1 
ATOM   5346 C  CA  . MET B 1 235 ? -16.977 20.911  -10.522 1.00 58.06  ? 235 MET B CA  1 
ATOM   5347 C  C   . MET B 1 235 ? -18.046 20.561  -11.559 1.00 54.61  ? 235 MET B C   1 
ATOM   5348 O  O   . MET B 1 235 ? -18.771 19.570  -11.338 1.00 47.01  ? 235 MET B O   1 
ATOM   5349 C  CB  . MET B 1 235 ? -17.508 22.005  -9.588  1.00 66.95  ? 235 MET B CB  1 
ATOM   5350 C  CG  . MET B 1 235 ? -18.804 21.605  -8.876  1.00 72.60  ? 235 MET B CG  1 
ATOM   5351 S  SD  . MET B 1 235 ? -19.414 22.823  -7.670  1.00 80.05  ? 235 MET B SD  1 
ATOM   5352 C  CE  . MET B 1 235 ? -18.355 22.487  -6.263  1.00 75.56  ? 235 MET B CE  1 
ATOM   5353 N  N   . LYS B 1 236 ? -18.121 21.322  -12.660 1.00 56.06  ? 236 LYS B N   1 
ATOM   5354 C  CA  . LYS B 1 236 ? -19.152 21.134  -13.717 1.00 57.27  ? 236 LYS B CA  1 
ATOM   5355 C  C   . LYS B 1 236 ? -18.957 19.775  -14.392 1.00 52.30  ? 236 LYS B C   1 
ATOM   5356 O  O   . LYS B 1 236 ? -19.973 19.155  -14.728 1.00 45.43  ? 236 LYS B O   1 
ATOM   5357 C  CB  . LYS B 1 236 ? -19.142 22.267  -14.757 1.00 64.67  ? 236 LYS B CB  1 
ATOM   5358 C  CG  . LYS B 1 236 ? -20.195 22.129  -15.859 1.00 72.92  ? 236 LYS B CG  1 
ATOM   5359 C  CD  . LYS B 1 236 ? -20.291 23.297  -16.855 1.00 79.31  ? 236 LYS B CD  1 
ATOM   5360 C  CE  . LYS B 1 236 ? -20.546 24.659  -16.233 1.00 79.48  ? 236 LYS B CE  1 
ATOM   5361 N  NZ  . LYS B 1 236 ? -21.740 24.661  -15.350 1.00 84.33  ? 236 LYS B NZ  1 
ATOM   5362 N  N   . TYR B 1 237 ? -17.710 19.328  -14.597 1.00 53.81  ? 237 TYR B N   1 
ATOM   5363 C  CA  . TYR B 1 237 ? -17.411 18.096  -15.382 1.00 52.16  ? 237 TYR B CA  1 
ATOM   5364 C  C   . TYR B 1 237 ? -17.097 16.905  -14.466 1.00 52.76  ? 237 TYR B C   1 
ATOM   5365 O  O   . TYR B 1 237 ? -16.645 15.877  -15.007 1.00 46.27  ? 237 TYR B O   1 
ATOM   5366 C  CB  . TYR B 1 237 ? -16.299 18.386  -16.388 1.00 53.60  ? 237 TYR B CB  1 
ATOM   5367 C  CG  . TYR B 1 237 ? -16.729 19.328  -17.485 1.00 54.53  ? 237 TYR B CG  1 
ATOM   5368 C  CD1 . TYR B 1 237 ? -16.623 20.703  -17.330 1.00 57.70  ? 237 TYR B CD1 1 
ATOM   5369 C  CD2 . TYR B 1 237 ? -17.274 18.845  -18.663 1.00 53.37  ? 237 TYR B CD2 1 
ATOM   5370 C  CE1 . TYR B 1 237 ? -17.029 21.575  -18.328 1.00 61.00  ? 237 TYR B CE1 1 
ATOM   5371 C  CE2 . TYR B 1 237 ? -17.689 19.700  -19.669 1.00 56.23  ? 237 TYR B CE2 1 
ATOM   5372 C  CZ  . TYR B 1 237 ? -17.567 21.068  -19.501 1.00 59.07  ? 237 TYR B CZ  1 
ATOM   5373 O  OH  . TYR B 1 237 ? -17.976 21.898  -20.503 1.00 65.44  ? 237 TYR B OH  1 
ATOM   5374 N  N   . ASN B 1 238 ? -17.378 17.015  -13.157 1.00 51.21  ? 238 ASN B N   1 
ATOM   5375 C  CA  . ASN B 1 238 ? -17.132 15.955  -12.137 1.00 50.28  ? 238 ASN B CA  1 
ATOM   5376 C  C   . ASN B 1 238 ? -15.626 15.713  -12.020 1.00 48.02  ? 238 ASN B C   1 
ATOM   5377 O  O   . ASN B 1 238 ? -15.179 14.556  -12.023 1.00 44.62  ? 238 ASN B O   1 
ATOM   5378 C  CB  . ASN B 1 238 ? -17.869 14.656  -12.452 1.00 52.84  ? 238 ASN B CB  1 
ATOM   5379 C  CG  . ASN B 1 238 ? -19.322 14.758  -12.080 1.00 55.95  ? 238 ASN B CG  1 
ATOM   5380 O  OD1 . ASN B 1 238 ? -19.644 15.252  -11.008 1.00 58.35  ? 238 ASN B OD1 1 
ATOM   5381 N  ND2 . ASN B 1 238 ? -20.193 14.313  -12.965 1.00 61.33  ? 238 ASN B ND2 1 
ATOM   5382 N  N   . TYR B 1 239 ? -14.891 16.806  -11.971 1.00 44.28  ? 239 TYR B N   1 
ATOM   5383 C  CA  . TYR B 1 239 ? -13.450 16.848  -11.689 1.00 44.58  ? 239 TYR B CA  1 
ATOM   5384 C  C   . TYR B 1 239 ? -13.332 17.286  -10.239 1.00 45.28  ? 239 TYR B C   1 
ATOM   5385 O  O   . TYR B 1 239 ? -14.158 18.095  -9.805  1.00 50.04  ? 239 TYR B O   1 
ATOM   5386 C  CB  . TYR B 1 239 ? -12.745 17.791  -12.670 1.00 42.67  ? 239 TYR B CB  1 
ATOM   5387 C  CG  . TYR B 1 239 ? -12.246 17.111  -13.921 1.00 39.10  ? 239 TYR B CG  1 
ATOM   5388 C  CD1 . TYR B 1 239 ? -13.106 16.402  -14.747 1.00 38.57  ? 239 TYR B CD1 1 
ATOM   5389 C  CD2 . TYR B 1 239 ? -10.898 17.150  -14.257 1.00 37.24  ? 239 TYR B CD2 1 
ATOM   5390 C  CE1 . TYR B 1 239 ? -12.641 15.775  -15.896 1.00 40.66  ? 239 TYR B CE1 1 
ATOM   5391 C  CE2 . TYR B 1 239 ? -10.418 16.522  -15.397 1.00 36.33  ? 239 TYR B CE2 1 
ATOM   5392 C  CZ  . TYR B 1 239 ? -11.291 15.841  -16.224 1.00 38.49  ? 239 TYR B CZ  1 
ATOM   5393 O  OH  . TYR B 1 239 ? -10.798 15.237  -17.350 1.00 41.10  ? 239 TYR B OH  1 
ATOM   5394 N  N   . GLU B 1 240 ? -12.364 16.725  -9.528  1.00 41.72  ? 240 GLU B N   1 
ATOM   5395 C  CA  . GLU B 1 240 ? -11.979 17.146  -8.167  1.00 41.50  ? 240 GLU B CA  1 
ATOM   5396 C  C   . GLU B 1 240 ? -11.526 18.596  -8.254  1.00 41.70  ? 240 GLU B C   1 
ATOM   5397 O  O   . GLU B 1 240 ? -10.977 19.022  -9.261  1.00 40.90  ? 240 GLU B O   1 
ATOM   5398 C  CB  . GLU B 1 240 ? -10.858 16.261  -7.623  1.00 40.76  ? 240 GLU B CB  1 
ATOM   5399 C  CG  . GLU B 1 240 ? -11.293 14.839  -7.367  1.00 44.74  ? 240 GLU B CG  1 
ATOM   5400 C  CD  . GLU B 1 240 ? -12.068 14.690  -6.072  1.00 46.65  ? 240 GLU B CD  1 
ATOM   5401 O  OE1 . GLU B 1 240 ? -11.458 14.918  -5.012  1.00 49.88  ? 240 GLU B OE1 1 
ATOM   5402 O  OE2 . GLU B 1 240 ? -13.271 14.364  -6.131  1.00 41.28  ? 240 GLU B OE2 1 
ATOM   5403 N  N   . PRO B 1 241 ? -11.746 19.401  -7.199  1.00 42.78  ? 241 PRO B N   1 
ATOM   5404 C  CA  . PRO B 1 241 ? -11.108 20.707  -7.107  1.00 44.08  ? 241 PRO B CA  1 
ATOM   5405 C  C   . PRO B 1 241 ? -9.579  20.593  -7.149  1.00 47.62  ? 241 PRO B C   1 
ATOM   5406 O  O   . PRO B 1 241 ? -9.021  19.649  -6.574  1.00 48.60  ? 241 PRO B O   1 
ATOM   5407 C  CB  . PRO B 1 241 ? -11.593 21.243  -5.757  1.00 42.60  ? 241 PRO B CB  1 
ATOM   5408 C  CG  . PRO B 1 241 ? -12.903 20.531  -5.566  1.00 45.73  ? 241 PRO B CG  1 
ATOM   5409 C  CD  . PRO B 1 241 ? -12.636 19.126  -6.066  1.00 44.50  ? 241 PRO B CD  1 
ATOM   5410 N  N   . LEU B 1 242 ? -8.957  21.548  -7.847  1.00 45.07  ? 242 LEU B N   1 
ATOM   5411 C  CA  . LEU B 1 242 ? -7.508  21.823  -7.790  1.00 42.25  ? 242 LEU B CA  1 
ATOM   5412 C  C   . LEU B 1 242 ? -7.259  22.798  -6.644  1.00 43.08  ? 242 LEU B C   1 
ATOM   5413 O  O   . LEU B 1 242 ? -7.807  23.912  -6.682  1.00 42.60  ? 242 LEU B O   1 
ATOM   5414 C  CB  . LEU B 1 242 ? -7.023  22.396  -9.125  1.00 43.82  ? 242 LEU B CB  1 
ATOM   5415 C  CG  . LEU B 1 242 ? -5.526  22.208  -9.369  1.00 43.93  ? 242 LEU B CG  1 
ATOM   5416 C  CD1 . LEU B 1 242 ? -5.213  20.764  -9.756  1.00 43.90  ? 242 LEU B CD1 1 
ATOM   5417 C  CD2 . LEU B 1 242 ? -5.004  23.166  -10.423 1.00 44.80  ? 242 LEU B CD2 1 
ATOM   5418 N  N   . THR B 1 243 ? -6.455  22.370  -5.669  1.00 47.37  ? 243 THR B N   1 
ATOM   5419 C  CA  . THR B 1 243 ? -5.993  23.182  -4.515  1.00 47.42  ? 243 THR B CA  1 
ATOM   5420 C  C   . THR B 1 243 ? -4.677  23.849  -4.905  1.00 45.62  ? 243 THR B C   1 
ATOM   5421 O  O   . THR B 1 243 ? -4.109  23.459  -5.919  1.00 42.10  ? 243 THR B O   1 
ATOM   5422 C  CB  . THR B 1 243 ? -5.857  22.307  -3.263  1.00 46.33  ? 243 THR B CB  1 
ATOM   5423 O  OG1 . THR B 1 243 ? -4.792  21.383  -3.467  1.00 48.75  ? 243 THR B OG1 1 
ATOM   5424 C  CG2 . THR B 1 243 ? -7.103  21.512  -2.952  1.00 48.54  ? 243 THR B CG2 1 
ATOM   5425 N  N   . GLN B 1 244 ? -4.228  24.823  -4.120  1.00 52.57  ? 244 GLN B N   1 
ATOM   5426 C  CA  . GLN B 1 244 ? -2.886  25.446  -4.248  1.00 49.17  ? 244 GLN B CA  1 
ATOM   5427 C  C   . GLN B 1 244 ? -1.790  24.397  -4.044  1.00 50.73  ? 244 GLN B C   1 
ATOM   5428 O  O   . GLN B 1 244 ? -0.654  24.617  -4.521  1.00 49.90  ? 244 GLN B O   1 
ATOM   5429 C  CB  . GLN B 1 244 ? -2.679  26.533  -3.190  1.00 47.90  ? 244 GLN B CB  1 
ATOM   5430 C  CG  . GLN B 1 244 ? -1.343  27.243  -3.343  1.00 45.79  ? 244 GLN B CG  1 
ATOM   5431 C  CD  . GLN B 1 244 ? -1.148  27.652  -4.779  1.00 47.60  ? 244 GLN B CD  1 
ATOM   5432 O  OE1 . GLN B 1 244 ? -2.094  28.079  -5.445  1.00 54.10  ? 244 GLN B OE1 1 
ATOM   5433 N  NE2 . GLN B 1 244 ? 0.069   27.486  -5.272  1.00 48.72  ? 244 GLN B NE2 1 
ATOM   5434 N  N   . ASP B 1 245 ? -2.085  23.325  -3.306  1.00 49.07  ? 245 ASP B N   1 
ATOM   5435 C  CA  . ASP B 1 245 ? -1.071  22.285  -2.987  1.00 51.08  ? 245 ASP B CA  1 
ATOM   5436 C  C   . ASP B 1 245 ? -0.797  21.476  -4.265  1.00 42.98  ? 245 ASP B C   1 
ATOM   5437 O  O   . ASP B 1 245 ? 0.384   21.250  -4.592  1.00 39.94  ? 245 ASP B O   1 
ATOM   5438 C  CB  . ASP B 1 245 ? -1.513  21.423  -1.800  1.00 55.37  ? 245 ASP B CB  1 
ATOM   5439 C  CG  . ASP B 1 245 ? -0.489  20.359  -1.454  1.00 66.53  ? 245 ASP B CG  1 
ATOM   5440 O  OD1 . ASP B 1 245 ? 0.717   20.698  -1.415  1.00 74.63  ? 245 ASP B OD1 1 
ATOM   5441 O  OD2 . ASP B 1 245 ? -0.896  19.190  -1.266  1.00 77.06  ? 245 ASP B OD2 1 
ATOM   5442 N  N   . HIS B 1 246 ? -1.859  21.101  -4.977  1.00 39.98  ? 246 HIS B N   1 
ATOM   5443 C  CA  . HIS B 1 246 ? -1.796  20.488  -6.331  1.00 39.46  ? 246 HIS B CA  1 
ATOM   5444 C  C   . HIS B 1 246 ? -0.899  21.331  -7.241  1.00 41.42  ? 246 HIS B C   1 
ATOM   5445 O  O   . HIS B 1 246 ? 0.014   20.761  -7.872  1.00 40.00  ? 246 HIS B O   1 
ATOM   5446 C  CB  . HIS B 1 246 ? -3.194  20.369  -6.911  1.00 35.39  ? 246 HIS B CB  1 
ATOM   5447 C  CG  . HIS B 1 246 ? -4.042  19.362  -6.213  1.00 38.53  ? 246 HIS B CG  1 
ATOM   5448 N  ND1 . HIS B 1 246 ? -5.421  19.469  -6.163  1.00 41.33  ? 246 HIS B ND1 1 
ATOM   5449 C  CD2 . HIS B 1 246 ? -3.726  18.215  -5.570  1.00 37.87  ? 246 HIS B CD2 1 
ATOM   5450 C  CE1 . HIS B 1 246 ? -5.917  18.436  -5.510  1.00 40.58  ? 246 HIS B CE1 1 
ATOM   5451 N  NE2 . HIS B 1 246 ? -4.896  17.647  -5.146  1.00 36.82  ? 246 HIS B NE2 1 
ATOM   5452 N  N   . VAL B 1 247 ? -1.138  22.647  -7.287  1.00 44.87  ? 247 VAL B N   1 
ATOM   5453 C  CA  . VAL B 1 247 ? -0.350  23.580  -8.150  1.00 46.04  ? 247 VAL B CA  1 
ATOM   5454 C  C   . VAL B 1 247 ? 1.130   23.436  -7.794  1.00 43.48  ? 247 VAL B C   1 
ATOM   5455 O  O   . VAL B 1 247 ? 1.939   23.364  -8.727  1.00 55.59  ? 247 VAL B O   1 
ATOM   5456 C  CB  . VAL B 1 247 ? -0.826  25.047  -8.055  1.00 45.75  ? 247 VAL B CB  1 
ATOM   5457 C  CG1 . VAL B 1 247 ? 0.255   26.033  -8.468  1.00 40.14  ? 247 VAL B CG1 1 
ATOM   5458 C  CG2 . VAL B 1 247 ? -2.095  25.286  -8.856  1.00 45.43  ? 247 VAL B CG2 1 
ATOM   5459 N  N   . ASP B 1 248 ? 1.476   23.390  -6.507  1.00 48.62  ? 248 ASP B N   1 
ATOM   5460 C  CA  . ASP B 1 248 ? 2.892   23.403  -6.032  1.00 48.22  ? 248 ASP B CA  1 
ATOM   5461 C  C   . ASP B 1 248 ? 3.569   22.052  -6.339  1.00 48.06  ? 248 ASP B C   1 
ATOM   5462 O  O   . ASP B 1 248 ? 4.809   22.029  -6.590  1.00 44.43  ? 248 ASP B O   1 
ATOM   5463 C  CB  . ASP B 1 248 ? 2.970   23.752  -4.536  1.00 55.27  ? 248 ASP B CB  1 
ATOM   5464 C  CG  . ASP B 1 248 ? 2.291   25.062  -4.128  1.00 54.92  ? 248 ASP B CG  1 
ATOM   5465 O  OD1 . ASP B 1 248 ? 2.375   26.041  -4.882  1.00 51.82  ? 248 ASP B OD1 1 
ATOM   5466 O  OD2 . ASP B 1 248 ? 1.663   25.087  -3.060  1.00 53.80  ? 248 ASP B OD2 1 
ATOM   5467 N  N   . ILE B 1 249 ? 2.803   20.955  -6.307  1.00 44.85  ? 249 ILE B N   1 
ATOM   5468 C  CA  . ILE B 1 249 ? 3.314   19.573  -6.564  1.00 43.71  ? 249 ILE B CA  1 
ATOM   5469 C  C   . ILE B 1 249 ? 3.683   19.447  -8.049  1.00 40.20  ? 249 ILE B C   1 
ATOM   5470 O  O   . ILE B 1 249 ? 4.711   18.822  -8.341  1.00 40.14  ? 249 ILE B O   1 
ATOM   5471 C  CB  . ILE B 1 249 ? 2.287   18.526  -6.098  1.00 44.93  ? 249 ILE B CB  1 
ATOM   5472 C  CG1 . ILE B 1 249 ? 2.051   18.623  -4.587  1.00 50.79  ? 249 ILE B CG1 1 
ATOM   5473 C  CG2 . ILE B 1 249 ? 2.744   17.139  -6.479  1.00 48.17  ? 249 ILE B CG2 1 
ATOM   5474 C  CD1 . ILE B 1 249 ? 0.763   17.969  -4.101  1.00 49.49  ? 249 ILE B CD1 1 
ATOM   5475 N  N   . LEU B 1 250 ? 2.907   20.062  -8.949  1.00 38.64  ? 250 LEU B N   1 
ATOM   5476 C  CA  . LEU B 1 250 ? 3.198   20.114  -10.410 1.00 37.89  ? 250 LEU B CA  1 
ATOM   5477 C  C   . LEU B 1 250 ? 4.383   21.050  -10.697 1.00 40.62  ? 250 LEU B C   1 
ATOM   5478 O  O   . LEU B 1 250 ? 4.895   21.011  -11.828 1.00 45.42  ? 250 LEU B O   1 
ATOM   5479 C  CB  . LEU B 1 250 ? 1.943   20.587  -11.150 1.00 36.78  ? 250 LEU B CB  1 
ATOM   5480 C  CG  . LEU B 1 250 ? 0.760   19.624  -11.119 1.00 37.93  ? 250 LEU B CG  1 
ATOM   5481 C  CD1 . LEU B 1 250 ? -0.533  20.336  -11.473 1.00 37.59  ? 250 LEU B CD1 1 
ATOM   5482 C  CD2 . LEU B 1 250 ? 0.991   18.447  -12.060 1.00 39.00  ? 250 LEU B CD2 1 
ATOM   5483 N  N   . GLY B 1 251 ? 4.785   21.877  -9.725  1.00 42.87  ? 251 GLY B N   1 
ATOM   5484 C  CA  . GLY B 1 251 ? 5.912   22.831  -9.811  1.00 40.58  ? 251 GLY B CA  1 
ATOM   5485 C  C   . GLY B 1 251 ? 7.034   22.370  -10.732 1.00 40.61  ? 251 GLY B C   1 
ATOM   5486 O  O   . GLY B 1 251 ? 7.298   23.029  -11.739 1.00 44.81  ? 251 GLY B O   1 
ATOM   5487 N  N   . PRO B 1 252 ? 7.726   21.245  -10.422 1.00 39.98  ? 252 PRO B N   1 
ATOM   5488 C  CA  . PRO B 1 252 ? 8.851   20.761  -11.229 1.00 40.36  ? 252 PRO B CA  1 
ATOM   5489 C  C   . PRO B 1 252 ? 8.535   20.612  -12.723 1.00 46.54  ? 252 PRO B C   1 
ATOM   5490 O  O   . PRO B 1 252 ? 9.301   21.093  -13.535 1.00 53.25  ? 252 PRO B O   1 
ATOM   5491 C  CB  . PRO B 1 252 ? 9.159   19.369  -10.653 1.00 40.75  ? 252 PRO B CB  1 
ATOM   5492 C  CG  . PRO B 1 252 ? 8.669   19.452  -9.236  1.00 38.08  ? 252 PRO B CG  1 
ATOM   5493 C  CD  . PRO B 1 252 ? 7.468   20.378  -9.264  1.00 39.52  ? 252 PRO B CD  1 
ATOM   5494 N  N   . LEU B 1 253 ? 7.410   19.969  -13.044 1.00 47.33  ? 253 LEU B N   1 
ATOM   5495 C  CA  . LEU B 1 253 ? 6.922   19.791  -14.438 1.00 42.94  ? 253 LEU B CA  1 
ATOM   5496 C  C   . LEU B 1 253 ? 6.655   21.163  -15.070 1.00 44.11  ? 253 LEU B C   1 
ATOM   5497 O  O   . LEU B 1 253 ? 6.883   21.295  -16.281 1.00 38.54  ? 253 LEU B O   1 
ATOM   5498 C  CB  . LEU B 1 253 ? 5.659   18.923  -14.420 1.00 42.09  ? 253 LEU B CB  1 
ATOM   5499 C  CG  . LEU B 1 253 ? 5.846   17.497  -13.893 1.00 42.09  ? 253 LEU B CG  1 
ATOM   5500 C  CD1 . LEU B 1 253 ? 4.515   16.793  -13.711 1.00 40.65  ? 253 LEU B CD1 1 
ATOM   5501 C  CD2 . LEU B 1 253 ? 6.741   16.685  -14.809 1.00 41.96  ? 253 LEU B CD2 1 
ATOM   5502 N  N   . SER B 1 254 ? 6.171   22.137  -14.285 1.00 47.59  ? 254 SER B N   1 
ATOM   5503 C  CA  . SER B 1 254 ? 5.846   23.514  -14.751 1.00 49.87  ? 254 SER B CA  1 
ATOM   5504 C  C   . SER B 1 254 ? 7.138   24.187  -15.206 1.00 47.82  ? 254 SER B C   1 
ATOM   5505 O  O   . SER B 1 254 ? 7.111   24.859  -16.242 1.00 49.13  ? 254 SER B O   1 
ATOM   5506 C  CB  . SER B 1 254 ? 5.144   24.346  -13.699 1.00 51.49  ? 254 SER B CB  1 
ATOM   5507 O  OG  . SER B 1 254 ? 4.929   25.680  -14.161 1.00 52.55  ? 254 SER B OG  1 
ATOM   5508 N  N   . ALA B 1 255 ? 8.224   23.949  -14.471 1.00 51.41  ? 255 ALA B N   1 
ATOM   5509 C  CA  . ALA B 1 255 ? 9.599   24.369  -14.820 1.00 56.18  ? 255 ALA B CA  1 
ATOM   5510 C  C   . ALA B 1 255 ? 10.032  23.670  -16.112 1.00 57.78  ? 255 ALA B C   1 
ATOM   5511 O  O   . ALA B 1 255 ? 10.151  24.370  -17.134 1.00 53.32  ? 255 ALA B O   1 
ATOM   5512 C  CB  . ALA B 1 255 ? 10.549  24.081  -13.687 1.00 57.36  ? 255 ALA B CB  1 
ATOM   5513 N  N   . GLN B 1 256 ? 10.209  22.343  -16.092 1.00 57.84  ? 256 GLN B N   1 
ATOM   5514 C  CA  . GLN B 1 256 ? 10.889  21.594  -17.186 1.00 54.62  ? 256 GLN B CA  1 
ATOM   5515 C  C   . GLN B 1 256 ? 10.215  21.868  -18.545 1.00 51.52  ? 256 GLN B C   1 
ATOM   5516 O  O   . GLN B 1 256 ? 10.841  21.558  -19.575 1.00 55.45  ? 256 GLN B O   1 
ATOM   5517 C  CB  . GLN B 1 256 ? 10.971  20.096  -16.879 1.00 60.42  ? 256 GLN B CB  1 
ATOM   5518 C  CG  . GLN B 1 256 ? 12.055  19.368  -17.670 1.00 65.43  ? 256 GLN B CG  1 
ATOM   5519 C  CD  . GLN B 1 256 ? 11.900  17.863  -17.642 1.00 79.06  ? 256 GLN B CD  1 
ATOM   5520 O  OE1 . GLN B 1 256 ? 11.849  17.222  -16.585 1.00 84.08  ? 256 GLN B OE1 1 
ATOM   5521 N  NE2 . GLN B 1 256 ? 11.831  17.279  -18.827 1.00 80.75  ? 256 GLN B NE2 1 
ATOM   5522 N  N   . THR B 1 257 ? 9.015   22.452  -18.584 1.00 45.86  ? 257 THR B N   1 
ATOM   5523 C  CA  . THR B 1 257 ? 8.239   22.622  -19.842 1.00 46.58  ? 257 THR B CA  1 
ATOM   5524 C  C   . THR B 1 257 ? 7.893   24.094  -20.147 1.00 46.53  ? 257 THR B C   1 
ATOM   5525 O  O   . THR B 1 257 ? 7.563   24.367  -21.304 1.00 48.85  ? 257 THR B O   1 
ATOM   5526 C  CB  . THR B 1 257 ? 6.944   21.798  -19.803 1.00 46.48  ? 257 THR B CB  1 
ATOM   5527 O  OG1 . THR B 1 257 ? 6.231   22.136  -18.610 1.00 46.78  ? 257 THR B OG1 1 
ATOM   5528 C  CG2 . THR B 1 257 ? 7.193   20.307  -19.880 1.00 45.83  ? 257 THR B CG2 1 
ATOM   5529 N  N   . GLY B 1 258 ? 7.875   24.994  -19.163 1.00 43.27  ? 258 GLY B N   1 
ATOM   5530 C  CA  . GLY B 1 258 ? 7.536   26.411  -19.379 1.00 45.91  ? 258 GLY B CA  1 
ATOM   5531 C  C   . GLY B 1 258 ? 6.031   26.625  -19.421 1.00 53.22  ? 258 GLY B C   1 
ATOM   5532 O  O   . GLY B 1 258 ? 5.575   27.758  -19.743 1.00 56.52  ? 258 GLY B O   1 
ATOM   5533 N  N   . ILE B 1 259 ? 5.265   25.602  -19.048 1.00 45.07  ? 259 ILE B N   1 
ATOM   5534 C  CA  . ILE B 1 259 ? 3.784   25.678  -19.045 1.00 50.58  ? 259 ILE B CA  1 
ATOM   5535 C  C   . ILE B 1 259 ? 3.327   25.655  -17.581 1.00 52.37  ? 259 ILE B C   1 
ATOM   5536 O  O   . ILE B 1 259 ? 3.481   24.608  -16.922 1.00 49.35  ? 259 ILE B O   1 
ATOM   5537 C  CB  . ILE B 1 259 ? 3.194   24.558  -19.918 1.00 48.19  ? 259 ILE B CB  1 
ATOM   5538 C  CG1 . ILE B 1 259 ? 3.999   24.394  -21.209 1.00 50.75  ? 259 ILE B CG1 1 
ATOM   5539 C  CG2 . ILE B 1 259 ? 1.715   24.803  -20.183 1.00 44.32  ? 259 ILE B CG2 1 
ATOM   5540 C  CD1 . ILE B 1 259 ? 3.704   23.109  -21.934 1.00 53.16  ? 259 ILE B CD1 1 
ATOM   5541 N  N   . ALA B 1 260 ? 2.884   26.811  -17.078 1.00 51.47  ? 260 ALA B N   1 
ATOM   5542 C  CA  . ALA B 1 260 ? 2.442   27.023  -15.684 1.00 48.13  ? 260 ALA B CA  1 
ATOM   5543 C  C   . ALA B 1 260 ? 1.104   26.327  -15.508 1.00 47.42  ? 260 ALA B C   1 
ATOM   5544 O  O   . ALA B 1 260 ? 0.349   26.238  -16.484 1.00 54.97  ? 260 ALA B O   1 
ATOM   5545 C  CB  . ALA B 1 260 ? 2.321   28.498  -15.382 1.00 50.71  ? 260 ALA B CB  1 
ATOM   5546 N  N   . VAL B 1 261 ? 0.813   25.875  -14.300 1.00 46.71  ? 261 VAL B N   1 
ATOM   5547 C  CA  . VAL B 1 261 ? -0.341  24.970  -14.045 1.00 46.01  ? 261 VAL B CA  1 
ATOM   5548 C  C   . VAL B 1 261 ? -1.627  25.629  -14.568 1.00 49.91  ? 261 VAL B C   1 
ATOM   5549 O  O   . VAL B 1 261 ? -2.447  24.922  -15.215 1.00 52.52  ? 261 VAL B O   1 
ATOM   5550 C  CB  . VAL B 1 261 ? -0.422  24.599  -12.554 1.00 43.73  ? 261 VAL B CB  1 
ATOM   5551 C  CG1 . VAL B 1 261 ? -1.677  23.789  -12.255 1.00 47.41  ? 261 VAL B CG1 1 
ATOM   5552 C  CG2 . VAL B 1 261 ? 0.833   23.874  -12.089 1.00 40.77  ? 261 VAL B CG2 1 
ATOM   5553 N  N   . LEU B 1 262 ? -1.828  26.932  -14.334 1.00 52.19  ? 262 LEU B N   1 
ATOM   5554 C  CA  . LEU B 1 262 ? -3.070  27.610  -14.813 1.00 46.48  ? 262 LEU B CA  1 
ATOM   5555 C  C   . LEU B 1 262 ? -2.988  27.808  -16.337 1.00 42.55  ? 262 LEU B C   1 
ATOM   5556 O  O   . LEU B 1 262 ? -4.072  27.769  -16.992 1.00 42.14  ? 262 LEU B O   1 
ATOM   5557 C  CB  . LEU B 1 262 ? -3.296  28.919  -14.045 1.00 50.07  ? 262 LEU B CB  1 
ATOM   5558 C  CG  . LEU B 1 262 ? -3.536  28.748  -12.543 1.00 51.62  ? 262 LEU B CG  1 
ATOM   5559 C  CD1 . LEU B 1 262 ? -3.451  30.077  -11.804 1.00 55.69  ? 262 LEU B CD1 1 
ATOM   5560 C  CD2 . LEU B 1 262 ? -4.885  28.097  -12.291 1.00 56.43  ? 262 LEU B CD2 1 
ATOM   5561 N  N   . ASP B 1 263 ? -1.770  27.983  -16.880 1.00 39.14  ? 263 ASP B N   1 
ATOM   5562 C  CA  . ASP B 1 263 ? -1.473  27.865  -18.340 1.00 44.31  ? 263 ASP B CA  1 
ATOM   5563 C  C   . ASP B 1 263 ? -1.990  26.491  -18.806 1.00 41.32  ? 263 ASP B C   1 
ATOM   5564 O  O   . ASP B 1 263 ? -2.896  26.456  -19.651 1.00 38.53  ? 263 ASP B O   1 
ATOM   5565 C  CB  . ASP B 1 263 ? 0.019   28.096  -18.642 1.00 43.51  ? 263 ASP B CB  1 
ATOM   5566 C  CG  . ASP B 1 263 ? 0.393   28.186  -20.119 1.00 43.05  ? 263 ASP B CG  1 
ATOM   5567 O  OD1 . ASP B 1 263 ? -0.501  28.016  -20.974 1.00 38.99  ? 263 ASP B OD1 1 
ATOM   5568 O  OD2 . ASP B 1 263 ? 1.592   28.408  -20.408 1.00 41.74  ? 263 ASP B OD2 1 
ATOM   5569 N  N   . MET B 1 264 ? -1.496  25.396  -18.212 1.00 42.29  ? 264 MET B N   1 
ATOM   5570 C  CA  . MET B 1 264 ? -1.959  24.034  -18.576 1.00 38.14  ? 264 MET B CA  1 
ATOM   5571 C  C   . MET B 1 264 ? -3.432  23.889  -18.201 1.00 39.55  ? 264 MET B C   1 
ATOM   5572 O  O   . MET B 1 264 ? -4.133  23.208  -18.930 1.00 39.55  ? 264 MET B O   1 
ATOM   5573 C  CB  . MET B 1 264 ? -1.149  22.939  -17.881 1.00 38.92  ? 264 MET B CB  1 
ATOM   5574 C  CG  . MET B 1 264 ? -1.459  21.567  -18.439 1.00 35.94  ? 264 MET B CG  1 
ATOM   5575 S  SD  . MET B 1 264 ? -0.786  21.400  -20.093 1.00 33.70  ? 264 MET B SD  1 
ATOM   5576 C  CE  . MET B 1 264 ? 0.867   20.859  -19.674 1.00 31.12  ? 264 MET B CE  1 
ATOM   5577 N  N   . CYS B 1 265 ? -3.915  24.518  -17.121 1.00 39.76  ? 265 CYS B N   1 
ATOM   5578 C  CA  . CYS B 1 265 ? -5.356  24.406  -16.752 1.00 44.44  ? 265 CYS B CA  1 
ATOM   5579 C  C   . CYS B 1 265 ? -6.217  24.934  -17.899 1.00 43.02  ? 265 CYS B C   1 
ATOM   5580 O  O   . CYS B 1 265 ? -7.279  24.332  -18.182 1.00 40.51  ? 265 CYS B O   1 
ATOM   5581 C  CB  . CYS B 1 265 ? -5.710  25.142  -15.465 1.00 50.89  ? 265 CYS B CB  1 
ATOM   5582 S  SG  . CYS B 1 265 ? -5.209  24.253  -13.969 1.00 52.73  ? 265 CYS B SG  1 
ATOM   5583 N  N   . ALA B 1 266 ? -5.756  25.995  -18.572 1.00 47.79  ? 266 ALA B N   1 
ATOM   5584 C  CA  . ALA B 1 266 ? -6.501  26.611  -19.699 1.00 48.03  ? 266 ALA B CA  1 
ATOM   5585 C  C   . ALA B 1 266 ? -6.584  25.602  -20.856 1.00 41.59  ? 266 ALA B C   1 
ATOM   5586 O  O   . ALA B 1 266 ? -7.662  25.470  -21.454 1.00 34.92  ? 266 ALA B O   1 
ATOM   5587 C  CB  . ALA B 1 266 ? -5.865  27.926  -20.105 1.00 51.39  ? 266 ALA B CB  1 
ATOM   5588 N  N   . SER B 1 267 ? -5.496  24.871  -21.137 1.00 44.21  ? 267 SER B N   1 
ATOM   5589 C  CA  . SER B 1 267 ? -5.512  23.741  -22.108 1.00 38.03  ? 267 SER B CA  1 
ATOM   5590 C  C   . SER B 1 267 ? -6.595  22.755  -21.673 1.00 34.30  ? 267 SER B C   1 
ATOM   5591 O  O   . SER B 1 267 ? -7.458  22.423  -22.492 1.00 34.47  ? 267 SER B O   1 
ATOM   5592 C  CB  . SER B 1 267 ? -4.169  23.069  -22.218 1.00 38.01  ? 267 SER B CB  1 
ATOM   5593 O  OG  . SER B 1 267 ? -3.241  23.861  -22.942 1.00 39.28  ? 267 SER B OG  1 
ATOM   5594 N  N   . LEU B 1 268 ? -6.583  22.345  -20.397 1.00 36.29  ? 268 LEU B N   1 
ATOM   5595 C  CA  . LEU B 1 268 ? -7.527  21.322  -19.864 1.00 33.88  ? 268 LEU B CA  1 
ATOM   5596 C  C   . LEU B 1 268 ? -8.963  21.862  -19.867 1.00 35.50  ? 268 LEU B C   1 
ATOM   5597 O  O   . LEU B 1 268 ? -9.882  21.132  -20.291 1.00 31.89  ? 268 LEU B O   1 
ATOM   5598 C  CB  . LEU B 1 268 ? -7.088  20.937  -18.447 1.00 34.70  ? 268 LEU B CB  1 
ATOM   5599 C  CG  . LEU B 1 268 ? -7.957  19.896  -17.740 1.00 33.66  ? 268 LEU B CG  1 
ATOM   5600 C  CD1 . LEU B 1 268 ? -8.166  18.642  -18.594 1.00 34.21  ? 268 LEU B CD1 1 
ATOM   5601 C  CD2 . LEU B 1 268 ? -7.345  19.548  -16.401 1.00 33.02  ? 268 LEU B CD2 1 
ATOM   5602 N  N   . LYS B 1 269 ? -9.162  23.095  -19.390 1.00 42.70  ? 269 LYS B N   1 
ATOM   5603 C  CA  . LYS B 1 269 ? -10.489 23.772  -19.467 1.00 49.16  ? 269 LYS B CA  1 
ATOM   5604 C  C   . LYS B 1 269 ? -11.060 23.526  -20.869 1.00 45.73  ? 269 LYS B C   1 
ATOM   5605 O  O   . LYS B 1 269 ? -12.179 22.997  -20.989 1.00 46.51  ? 269 LYS B O   1 
ATOM   5606 C  CB  . LYS B 1 269 ? -10.304 25.253  -19.118 1.00 57.19  ? 269 LYS B CB  1 
ATOM   5607 C  CG  . LYS B 1 269 ? -11.529 26.155  -19.251 1.00 65.59  ? 269 LYS B CG  1 
ATOM   5608 C  CD  . LYS B 1 269 ? -11.253 27.617  -18.874 1.00 67.59  ? 269 LYS B CD  1 
ATOM   5609 C  CE  . LYS B 1 269 ? -10.646 27.751  -17.487 1.00 71.35  ? 269 LYS B CE  1 
ATOM   5610 N  NZ  . LYS B 1 269 ? -10.622 29.146  -16.990 1.00 74.47  ? 269 LYS B NZ  1 
ATOM   5611 N  N   . GLU B 1 270 ? -10.252 23.805  -21.898 1.00 53.41  ? 270 GLU B N   1 
ATOM   5612 C  CA  . GLU B 1 270 ? -10.671 23.777  -23.329 1.00 55.16  ? 270 GLU B CA  1 
ATOM   5613 C  C   . GLU B 1 270 ? -10.908 22.336  -23.797 1.00 49.37  ? 270 GLU B C   1 
ATOM   5614 O  O   . GLU B 1 270 ? -11.774 22.158  -24.647 1.00 41.56  ? 270 GLU B O   1 
ATOM   5615 C  CB  . GLU B 1 270 ? -9.632  24.454  -24.232 1.00 61.70  ? 270 GLU B CB  1 
ATOM   5616 C  CG  . GLU B 1 270 ? -9.344  25.908  -23.882 1.00 66.96  ? 270 GLU B CG  1 
ATOM   5617 C  CD  . GLU B 1 270 ? -10.478 26.889  -24.135 1.00 68.44  ? 270 GLU B CD  1 
ATOM   5618 O  OE1 . GLU B 1 270 ? -10.947 26.971  -25.291 1.00 73.78  ? 270 GLU B OE1 1 
ATOM   5619 O  OE2 . GLU B 1 270 ? -10.891 27.566  -23.169 1.00 71.89  ? 270 GLU B OE2 1 
ATOM   5620 N  N   . LEU B 1 271 ? -10.132 21.358  -23.314 1.00 43.23  ? 271 LEU B N   1 
ATOM   5621 C  CA  . LEU B 1 271 ? -10.357 19.926  -23.652 1.00 41.62  ? 271 LEU B CA  1 
ATOM   5622 C  C   . LEU B 1 271 ? -11.681 19.460  -23.042 1.00 39.94  ? 271 LEU B C   1 
ATOM   5623 O  O   . LEU B 1 271 ? -12.367 18.658  -23.684 1.00 40.90  ? 271 LEU B O   1 
ATOM   5624 C  CB  . LEU B 1 271 ? -9.177  19.086  -23.148 1.00 41.75  ? 271 LEU B CB  1 
ATOM   5625 C  CG  . LEU B 1 271 ? -7.875  19.287  -23.919 1.00 40.22  ? 271 LEU B CG  1 
ATOM   5626 C  CD1 . LEU B 1 271 ? -6.681  18.726  -23.167 1.00 43.76  ? 271 LEU B CD1 1 
ATOM   5627 C  CD2 . LEU B 1 271 ? -7.981  18.652  -25.288 1.00 41.64  ? 271 LEU B CD2 1 
ATOM   5628 N  N   . LEU B 1 272 ? -12.043 19.935  -21.848 1.00 42.63  ? 272 LEU B N   1 
ATOM   5629 C  CA  . LEU B 1 272 ? -13.318 19.531  -21.192 1.00 48.95  ? 272 LEU B CA  1 
ATOM   5630 C  C   . LEU B 1 272 ? -14.531 20.058  -21.975 1.00 53.87  ? 272 LEU B C   1 
ATOM   5631 O  O   . LEU B 1 272 ? -15.501 19.277  -22.188 1.00 48.85  ? 272 LEU B O   1 
ATOM   5632 C  CB  . LEU B 1 272 ? -13.315 20.055  -19.755 1.00 50.09  ? 272 LEU B CB  1 
ATOM   5633 C  CG  . LEU B 1 272 ? -12.306 19.387  -18.821 1.00 50.00  ? 272 LEU B CG  1 
ATOM   5634 C  CD1 . LEU B 1 272 ? -12.430 19.923  -17.402 1.00 46.80  ? 272 LEU B CD1 1 
ATOM   5635 C  CD2 . LEU B 1 272 ? -12.477 17.873  -18.839 1.00 51.11  ? 272 LEU B CD2 1 
ATOM   5636 N  N   . GLN B 1 273 ? -14.486 21.333  -22.381 1.00 64.90  ? 273 GLN B N   1 
ATOM   5637 C  CA  . GLN B 1 273 ? -15.585 22.022  -23.122 1.00 66.48  ? 273 GLN B CA  1 
ATOM   5638 C  C   . GLN B 1 273 ? -15.680 21.449  -24.542 1.00 65.74  ? 273 GLN B C   1 
ATOM   5639 O  O   . GLN B 1 273 ? -16.689 20.762  -24.824 1.00 68.84  ? 273 GLN B O   1 
ATOM   5640 C  CB  . GLN B 1 273 ? -15.352 23.538  -23.129 1.00 64.75  ? 273 GLN B CB  1 
ATOM   5641 C  CG  . GLN B 1 273 ? -15.593 24.202  -21.775 1.00 63.31  ? 273 GLN B CG  1 
ATOM   5642 C  CD  . GLN B 1 273 ? -14.827 25.491  -21.560 1.00 63.61  ? 273 GLN B CD  1 
ATOM   5643 O  OE1 . GLN B 1 273 ? -14.049 25.931  -22.403 1.00 65.87  ? 273 GLN B OE1 1 
ATOM   5644 N  NE2 . GLN B 1 273 ? -15.031 26.119  -20.412 1.00 58.26  ? 273 GLN B NE2 1 
ATOM   5645 N  N   . ASN B 1 274 ? -14.632 21.665  -25.353 1.00 68.43  ? 274 ASN B N   1 
ATOM   5646 C  CA  . ASN B 1 274 ? -14.600 21.475  -26.836 1.00 67.57  ? 274 ASN B CA  1 
ATOM   5647 C  C   . ASN B 1 274 ? -14.304 20.019  -27.208 1.00 62.43  ? 274 ASN B C   1 
ATOM   5648 O  O   . ASN B 1 274 ? -14.639 19.661  -28.339 1.00 56.61  ? 274 ASN B O   1 
ATOM   5649 C  CB  . ASN B 1 274 ? -13.539 22.342  -27.529 1.00 62.13  ? 274 ASN B CB  1 
ATOM   5650 C  CG  . ASN B 1 274 ? -13.641 23.816  -27.194 1.00 64.49  ? 274 ASN B CG  1 
ATOM   5651 O  OD1 . ASN B 1 274 ? -14.634 24.458  -27.508 1.00 76.26  ? 274 ASN B OD1 1 
ATOM   5652 N  ND2 . ASN B 1 274 ? -12.613 24.375  -26.576 1.00 66.26  ? 274 ASN B ND2 1 
ATOM   5653 N  N   . GLY B 1 275 ? -13.668 19.245  -26.313 1.00 66.23  ? 275 GLY B N   1 
ATOM   5654 C  CA  . GLY B 1 275 ? -13.175 17.873  -26.577 1.00 61.52  ? 275 GLY B CA  1 
ATOM   5655 C  C   . GLY B 1 275 ? -11.790 17.874  -27.212 1.00 57.78  ? 275 GLY B C   1 
ATOM   5656 O  O   . GLY B 1 275 ? -11.143 18.952  -27.262 1.00 45.12  ? 275 GLY B O   1 
ATOM   5657 N  N   . MET B 1 276 ? -11.354 16.712  -27.715 1.00 62.19  ? 276 MET B N   1 
ATOM   5658 C  CA  . MET B 1 276 ? -9.995  16.505  -28.298 1.00 63.18  ? 276 MET B CA  1 
ATOM   5659 C  C   . MET B 1 276 ? -10.002 16.766  -29.811 1.00 63.46  ? 276 MET B C   1 
ATOM   5660 O  O   . MET B 1 276 ? -8.981  16.459  -30.474 1.00 57.51  ? 276 MET B O   1 
ATOM   5661 C  CB  . MET B 1 276 ? -9.497  15.079  -28.041 1.00 63.40  ? 276 MET B CB  1 
ATOM   5662 C  CG  . MET B 1 276 ? -9.263  14.786  -26.572 1.00 61.52  ? 276 MET B CG  1 
ATOM   5663 S  SD  . MET B 1 276 ? -7.885  13.661  -26.306 1.00 59.07  ? 276 MET B SD  1 
ATOM   5664 C  CE  . MET B 1 276 ? -8.356  13.099  -24.677 1.00 60.22  ? 276 MET B CE  1 
ATOM   5665 N  N   . ASN B 1 277 ? -11.092 17.325  -30.343 1.00 62.35  ? 277 ASN B N   1 
ATOM   5666 C  CA  . ASN B 1 277 ? -11.244 17.578  -31.798 1.00 69.78  ? 277 ASN B CA  1 
ATOM   5667 C  C   . ASN B 1 277 ? -10.721 16.333  -32.535 1.00 67.88  ? 277 ASN B C   1 
ATOM   5668 O  O   . ASN B 1 277 ? -9.959  16.483  -33.505 1.00 62.96  ? 277 ASN B O   1 
ATOM   5669 C  CB  . ASN B 1 277 ? -10.570 18.901  -32.194 1.00 73.35  ? 277 ASN B CB  1 
ATOM   5670 C  CG  . ASN B 1 277 ? -11.262 20.131  -31.618 1.00 80.29  ? 277 ASN B CG  1 
ATOM   5671 O  OD1 . ASN B 1 277 ? -10.616 21.132  -31.300 1.00 80.86  ? 277 ASN B OD1 1 
ATOM   5672 N  ND2 . ASN B 1 277 ? -12.583 20.082  -31.492 1.00 75.63  ? 277 ASN B ND2 1 
ATOM   5673 N  N   . GLY B 1 278 ? -11.091 15.143  -32.046 1.00 67.03  ? 278 GLY B N   1 
ATOM   5674 C  CA  . GLY B 1 278 ? -10.764 13.842  -32.662 1.00 68.99  ? 278 GLY B CA  1 
ATOM   5675 C  C   . GLY B 1 278 ? -9.452  13.278  -32.149 1.00 64.12  ? 278 GLY B C   1 
ATOM   5676 O  O   . GLY B 1 278 ? -9.449  12.106  -31.718 1.00 65.86  ? 278 GLY B O   1 
ATOM   5677 N  N   . ARG B 1 279 ? -8.404  14.106  -32.137 1.00 59.26  ? 279 ARG B N   1 
ATOM   5678 C  CA  . ARG B 1 279 ? -6.986  13.725  -31.885 1.00 61.07  ? 279 ARG B CA  1 
ATOM   5679 C  C   . ARG B 1 279 ? -6.839  12.857  -30.618 1.00 52.86  ? 279 ARG B C   1 
ATOM   5680 O  O   . ARG B 1 279 ? -7.853  12.569  -29.939 1.00 53.54  ? 279 ARG B O   1 
ATOM   5681 C  CB  . ARG B 1 279 ? -6.100  14.979  -31.805 1.00 67.39  ? 279 ARG B CB  1 
ATOM   5682 C  CG  . ARG B 1 279 ? -5.876  15.682  -33.139 1.00 68.95  ? 279 ARG B CG  1 
ATOM   5683 C  CD  . ARG B 1 279 ? -5.377  17.113  -33.031 1.00 76.27  ? 279 ARG B CD  1 
ATOM   5684 N  NE  . ARG B 1 279 ? -6.356  18.047  -32.476 1.00 87.20  ? 279 ARG B NE  1 
ATOM   5685 C  CZ  . ARG B 1 279 ? -6.388  19.365  -32.702 1.00 90.31  ? 279 ARG B CZ  1 
ATOM   5686 N  NH1 . ARG B 1 279 ? -5.522  19.934  -33.528 1.00 91.20  ? 279 ARG B NH1 1 
ATOM   5687 N  NH2 . ARG B 1 279 ? -7.251  20.125  -32.048 1.00 87.10  ? 279 ARG B NH2 1 
ATOM   5688 N  N   . THR B 1 280 ? -5.606  12.398  -30.364 1.00 46.59  ? 280 THR B N   1 
ATOM   5689 C  CA  . THR B 1 280 ? -5.185  11.611  -29.175 1.00 39.92  ? 280 THR B CA  1 
ATOM   5690 C  C   . THR B 1 280 ? -4.070  12.362  -28.442 1.00 36.13  ? 280 THR B C   1 
ATOM   5691 O  O   . THR B 1 280 ? -3.450  13.278  -29.014 1.00 38.87  ? 280 THR B O   1 
ATOM   5692 C  CB  . THR B 1 280 ? -4.684  10.204  -29.540 1.00 36.72  ? 280 THR B CB  1 
ATOM   5693 O  OG1 . THR B 1 280 ? -3.640  10.380  -30.488 1.00 38.27  ? 280 THR B OG1 1 
ATOM   5694 C  CG2 . THR B 1 280 ? -5.742  9.288   -30.113 1.00 36.63  ? 280 THR B CG2 1 
ATOM   5695 N  N   . ILE B 1 281 ? -3.837  11.974  -27.195 1.00 34.85  ? 281 ILE B N   1 
ATOM   5696 C  CA  . ILE B 1 281 ? -2.688  12.418  -26.361 1.00 30.91  ? 281 ILE B CA  1 
ATOM   5697 C  C   . ILE B 1 281 ? -2.054  11.162  -25.759 1.00 26.39  ? 281 ILE B C   1 
ATOM   5698 O  O   . ILE B 1 281 ? -2.770  10.419  -25.083 1.00 30.30  ? 281 ILE B O   1 
ATOM   5699 C  CB  . ILE B 1 281 ? -3.163  13.396  -25.272 1.00 28.46  ? 281 ILE B CB  1 
ATOM   5700 C  CG1 . ILE B 1 281 ? -3.957  14.565  -25.857 1.00 31.01  ? 281 ILE B CG1 1 
ATOM   5701 C  CG2 . ILE B 1 281 ? -1.978  13.851  -24.469 1.00 28.81  ? 281 ILE B CG2 1 
ATOM   5702 C  CD1 . ILE B 1 281 ? -4.501  15.548  -24.831 1.00 32.37  ? 281 ILE B CD1 1 
ATOM   5703 N  N   . LEU B 1 282 ? -0.760  10.953  -25.978 1.00 28.44  ? 282 LEU B N   1 
ATOM   5704 C  CA  . LEU B 1 282 ? -0.038  9.730   -25.544 1.00 27.91  ? 282 LEU B CA  1 
ATOM   5705 C  C   . LEU B 1 282 ? -0.872  8.496   -25.873 1.00 25.97  ? 282 LEU B C   1 
ATOM   5706 O  O   . LEU B 1 282 ? -1.022  7.655   -24.991 1.00 25.89  ? 282 LEU B O   1 
ATOM   5707 C  CB  . LEU B 1 282 ? 0.238   9.832   -24.037 1.00 28.16  ? 282 LEU B CB  1 
ATOM   5708 C  CG  . LEU B 1 282 ? 1.279   10.888  -23.678 1.00 30.23  ? 282 LEU B CG  1 
ATOM   5709 C  CD1 . LEU B 1 282 ? 1.448   11.039  -22.168 1.00 28.50  ? 282 LEU B CD1 1 
ATOM   5710 C  CD2 . LEU B 1 282 ? 2.606   10.566  -24.366 1.00 27.70  ? 282 LEU B CD2 1 
ATOM   5711 N  N   . GLY B 1 283 ? -1.430  8.428   -27.077 1.00 29.20  ? 283 GLY B N   1 
ATOM   5712 C  CA  . GLY B 1 283 ? -2.191  7.263   -27.594 1.00 32.77  ? 283 GLY B CA  1 
ATOM   5713 C  C   . GLY B 1 283 ? -3.430  6.932   -26.769 1.00 37.30  ? 283 GLY B C   1 
ATOM   5714 O  O   . GLY B 1 283 ? -3.789  5.741   -26.663 1.00 40.01  ? 283 GLY B O   1 
ATOM   5715 N  N   . SER B 1 284 ? -4.055  7.940   -26.162 1.00 36.14  ? 284 SER B N   1 
ATOM   5716 C  CA  . SER B 1 284 ? -5.338  7.799   -25.448 1.00 33.15  ? 284 SER B CA  1 
ATOM   5717 C  C   . SER B 1 284 ? -6.337  8.780   -26.055 1.00 32.67  ? 284 SER B C   1 
ATOM   5718 O  O   . SER B 1 284 ? -5.929  9.903   -26.408 1.00 33.75  ? 284 SER B O   1 
ATOM   5719 C  CB  . SER B 1 284 ? -5.151  8.025   -23.984 1.00 34.28  ? 284 SER B CB  1 
ATOM   5720 O  OG  . SER B 1 284 ? -6.357  7.753   -23.304 1.00 34.92  ? 284 SER B OG  1 
ATOM   5721 N  N   . ALA B 1 285 ? -7.591  8.352   -26.186 1.00 36.39  ? 285 ALA B N   1 
ATOM   5722 C  CA  . ALA B 1 285 ? -8.722  9.224   -26.572 1.00 40.39  ? 285 ALA B CA  1 
ATOM   5723 C  C   . ALA B 1 285 ? -9.419  9.754   -25.313 1.00 40.20  ? 285 ALA B C   1 
ATOM   5724 O  O   . ALA B 1 285 ? -10.318 10.589  -25.473 1.00 43.03  ? 285 ALA B O   1 
ATOM   5725 C  CB  . ALA B 1 285 ? -9.685  8.490   -27.481 1.00 42.37  ? 285 ALA B CB  1 
ATOM   5726 N  N   . LEU B 1 286 ? -9.002  9.319   -24.117 1.00 36.98  ? 286 LEU B N   1 
ATOM   5727 C  CA  . LEU B 1 286 ? -9.543  9.795   -22.813 1.00 35.38  ? 286 LEU B CA  1 
ATOM   5728 C  C   . LEU B 1 286 ? -8.469  10.611  -22.088 1.00 33.45  ? 286 LEU B C   1 
ATOM   5729 O  O   . LEU B 1 286 ? -7.273  10.481  -22.422 1.00 34.38  ? 286 LEU B O   1 
ATOM   5730 C  CB  . LEU B 1 286 ? -9.973  8.595   -21.959 1.00 36.94  ? 286 LEU B CB  1 
ATOM   5731 C  CG  . LEU B 1 286 ? -11.222 7.865   -22.441 1.00 39.61  ? 286 LEU B CG  1 
ATOM   5732 C  CD1 . LEU B 1 286 ? -11.486 6.601   -21.627 1.00 38.32  ? 286 LEU B CD1 1 
ATOM   5733 C  CD2 . LEU B 1 286 ? -12.436 8.798   -22.417 1.00 40.43  ? 286 LEU B CD2 1 
ATOM   5734 N  N   . LEU B 1 287 ? -8.891  11.440  -21.136 1.00 30.73  ? 287 LEU B N   1 
ATOM   5735 C  CA  . LEU B 1 287 ? -7.982  12.197  -20.247 1.00 31.58  ? 287 LEU B CA  1 
ATOM   5736 C  C   . LEU B 1 287 ? -7.562  11.281  -19.091 1.00 31.23  ? 287 LEU B C   1 
ATOM   5737 O  O   . LEU B 1 287 ? -8.331  11.145  -18.155 1.00 36.19  ? 287 LEU B O   1 
ATOM   5738 C  CB  . LEU B 1 287 ? -8.691  13.483  -19.800 1.00 31.75  ? 287 LEU B CB  1 
ATOM   5739 C  CG  . LEU B 1 287 ? -8.918  14.483  -20.939 1.00 35.15  ? 287 LEU B CG  1 
ATOM   5740 C  CD1 . LEU B 1 287 ? -9.728  15.688  -20.495 1.00 37.73  ? 287 LEU B CD1 1 
ATOM   5741 C  CD2 . LEU B 1 287 ? -7.599  14.948  -21.521 1.00 35.85  ? 287 LEU B CD2 1 
ATOM   5742 N  N   . GLU B 1 288 ? -6.357  10.717  -19.154 1.00 32.89  ? 288 GLU B N   1 
ATOM   5743 C  CA  . GLU B 1 288 ? -5.828  9.725   -18.175 1.00 32.76  ? 288 GLU B CA  1 
ATOM   5744 C  C   . GLU B 1 288 ? -5.554  10.396  -16.834 1.00 29.64  ? 288 GLU B C   1 
ATOM   5745 O  O   . GLU B 1 288 ? -4.808  11.387  -16.819 1.00 29.04  ? 288 GLU B O   1 
ATOM   5746 C  CB  . GLU B 1 288 ? -4.531  9.098   -18.685 1.00 35.19  ? 288 GLU B CB  1 
ATOM   5747 C  CG  . GLU B 1 288 ? -4.758  8.163   -19.863 1.00 41.93  ? 288 GLU B CG  1 
ATOM   5748 C  CD  . GLU B 1 288 ? -5.510  6.872   -19.549 1.00 45.18  ? 288 GLU B CD  1 
ATOM   5749 O  OE1 . GLU B 1 288 ? -5.091  6.123   -18.622 1.00 49.21  ? 288 GLU B OE1 1 
ATOM   5750 O  OE2 . GLU B 1 288 ? -6.512  6.630   -20.214 1.00 44.96  ? 288 GLU B OE2 1 
ATOM   5751 N  N   . ASP B 1 289 ? -6.077  9.835   -15.741 1.00 28.50  ? 289 ASP B N   1 
ATOM   5752 C  CA  . ASP B 1 289 ? -5.943  10.449  -14.391 1.00 29.14  ? 289 ASP B CA  1 
ATOM   5753 C  C   . ASP B 1 289 ? -5.325  9.462   -13.400 1.00 26.55  ? 289 ASP B C   1 
ATOM   5754 O  O   . ASP B 1 289 ? -5.459  9.702   -12.215 1.00 24.47  ? 289 ASP B O   1 
ATOM   5755 C  CB  . ASP B 1 289 ? -7.284  10.995  -13.889 1.00 31.98  ? 289 ASP B CB  1 
ATOM   5756 C  CG  . ASP B 1 289 ? -8.287  9.926   -13.496 1.00 35.71  ? 289 ASP B CG  1 
ATOM   5757 O  OD1 . ASP B 1 289 ? -8.117  8.771   -13.940 1.00 32.54  ? 289 ASP B OD1 1 
ATOM   5758 O  OD2 . ASP B 1 289 ? -9.236  10.257  -12.721 1.00 36.68  ? 289 ASP B OD2 1 
ATOM   5759 N  N   . GLU B 1 290 ? -4.592  8.444   -13.848 1.00 26.48  ? 290 GLU B N   1 
ATOM   5760 C  CA  . GLU B 1 290 ? -3.947  7.495   -12.900 1.00 26.88  ? 290 GLU B CA  1 
ATOM   5761 C  C   . GLU B 1 290 ? -2.419  7.638   -12.939 1.00 25.18  ? 290 GLU B C   1 
ATOM   5762 O  O   . GLU B 1 290 ? -1.732  6.700   -12.544 1.00 30.20  ? 290 GLU B O   1 
ATOM   5763 C  CB  . GLU B 1 290 ? -4.466  6.079   -13.155 1.00 28.33  ? 290 GLU B CB  1 
ATOM   5764 C  CG  . GLU B 1 290 ? -5.975  5.972   -13.023 1.00 31.86  ? 290 GLU B CG  1 
ATOM   5765 C  CD  . GLU B 1 290 ? -6.517  4.670   -12.420 1.00 35.21  ? 290 GLU B CD  1 
ATOM   5766 O  OE1 . GLU B 1 290 ? -5.750  3.690   -12.347 1.00 35.52  ? 290 GLU B OE1 1 
ATOM   5767 O  OE2 . GLU B 1 290 ? -7.719  4.630   -12.046 1.00 32.87  ? 290 GLU B OE2 1 
ATOM   5768 N  N   . PHE B 1 291 ? -1.875  8.777   -13.375 1.00 23.27  ? 291 PHE B N   1 
ATOM   5769 C  CA  . PHE B 1 291 ? -0.463  9.150   -13.120 1.00 21.63  ? 291 PHE B CA  1 
ATOM   5770 C  C   . PHE B 1 291 ? -0.433  10.376  -12.206 1.00 23.38  ? 291 PHE B C   1 
ATOM   5771 O  O   . PHE B 1 291 ? -1.072  11.385  -12.532 1.00 21.14  ? 291 PHE B O   1 
ATOM   5772 C  CB  . PHE B 1 291 ? 0.299   9.435   -14.414 1.00 22.21  ? 291 PHE B CB  1 
ATOM   5773 C  CG  . PHE B 1 291 ? 0.295   8.323   -15.429 1.00 23.76  ? 291 PHE B CG  1 
ATOM   5774 C  CD1 . PHE B 1 291 ? -0.728  8.206   -16.360 1.00 23.81  ? 291 PHE B CD1 1 
ATOM   5775 C  CD2 . PHE B 1 291 ? 1.339   7.408   -15.468 1.00 24.07  ? 291 PHE B CD2 1 
ATOM   5776 C  CE1 . PHE B 1 291 ? -0.696  7.200   -17.321 1.00 27.72  ? 291 PHE B CE1 1 
ATOM   5777 C  CE2 . PHE B 1 291 ? 1.384   6.413   -16.440 1.00 26.11  ? 291 PHE B CE2 1 
ATOM   5778 C  CZ  . PHE B 1 291 ? 0.348   6.289   -17.344 1.00 28.48  ? 291 PHE B CZ  1 
ATOM   5779 N  N   . THR B 1 292 ? 0.315   10.294  -11.109 1.00 23.51  ? 292 THR B N   1 
ATOM   5780 C  CA  . THR B 1 292 ? 0.548   11.435  -10.195 1.00 24.64  ? 292 THR B CA  1 
ATOM   5781 C  C   . THR B 1 292 ? 1.689   12.255  -10.764 1.00 26.12  ? 292 THR B C   1 
ATOM   5782 O  O   . THR B 1 292 ? 2.433   11.785  -11.630 1.00 28.85  ? 292 THR B O   1 
ATOM   5783 C  CB  . THR B 1 292 ? 0.837   10.973  -8.764  1.00 24.34  ? 292 THR B CB  1 
ATOM   5784 O  OG1 . THR B 1 292 ? 2.087   10.300  -8.774  1.00 25.87  ? 292 THR B OG1 1 
ATOM   5785 C  CG2 . THR B 1 292 ? -0.234  10.067  -8.189  1.00 24.19  ? 292 THR B CG2 1 
ATOM   5786 N  N   . PRO B 1 293 ? 1.852   13.506  -10.302 1.00 27.20  ? 293 PRO B N   1 
ATOM   5787 C  CA  . PRO B 1 293 ? 3.070   14.272  -10.574 1.00 27.42  ? 293 PRO B CA  1 
ATOM   5788 C  C   . PRO B 1 293 ? 4.351   13.498  -10.291 1.00 28.52  ? 293 PRO B C   1 
ATOM   5789 O  O   . PRO B 1 293 ? 5.192   13.487  -11.141 1.00 29.75  ? 293 PRO B O   1 
ATOM   5790 C  CB  . PRO B 1 293 ? 2.936   15.468  -9.647  1.00 26.68  ? 293 PRO B CB  1 
ATOM   5791 C  CG  . PRO B 1 293 ? 1.438   15.682  -9.578  1.00 28.60  ? 293 PRO B CG  1 
ATOM   5792 C  CD  . PRO B 1 293 ? 0.861   14.277  -9.537  1.00 26.76  ? 293 PRO B CD  1 
ATOM   5793 N  N   . PHE B 1 294 ? 4.442   12.851  -9.129  1.00 32.83  ? 294 PHE B N   1 
ATOM   5794 C  CA  . PHE B 1 294 ? 5.610   12.025  -8.751  1.00 32.63  ? 294 PHE B CA  1 
ATOM   5795 C  C   . PHE B 1 294 ? 5.828   10.978  -9.849  1.00 30.23  ? 294 PHE B C   1 
ATOM   5796 O  O   . PHE B 1 294 ? 6.963   10.793  -10.321 1.00 28.66  ? 294 PHE B O   1 
ATOM   5797 C  CB  . PHE B 1 294 ? 5.444   11.364  -7.382  1.00 38.31  ? 294 PHE B CB  1 
ATOM   5798 C  CG  . PHE B 1 294 ? 6.617   10.464  -7.051  1.00 53.20  ? 294 PHE B CG  1 
ATOM   5799 C  CD1 . PHE B 1 294 ? 7.672   10.918  -6.261  1.00 55.35  ? 294 PHE B CD1 1 
ATOM   5800 C  CD2 . PHE B 1 294 ? 6.720   9.183   -7.610  1.00 61.29  ? 294 PHE B CD2 1 
ATOM   5801 C  CE1 . PHE B 1 294 ? 8.777   10.111  -6.014  1.00 52.95  ? 294 PHE B CE1 1 
ATOM   5802 C  CE2 . PHE B 1 294 ? 7.821   8.369   -7.353  1.00 60.24  ? 294 PHE B CE2 1 
ATOM   5803 C  CZ  . PHE B 1 294 ? 8.847   8.840   -6.553  1.00 57.06  ? 294 PHE B CZ  1 
ATOM   5804 N  N   . ASP B 1 295 ? 4.763   10.287  -10.250 1.00 27.97  ? 295 ASP B N   1 
ATOM   5805 C  CA  . ASP B 1 295 ? 4.861   9.211   -11.273 1.00 27.99  ? 295 ASP B CA  1 
ATOM   5806 C  C   . ASP B 1 295 ? 5.502   9.784   -12.544 1.00 28.07  ? 295 ASP B C   1 
ATOM   5807 O  O   . ASP B 1 295 ? 6.354   9.093   -13.155 1.00 27.81  ? 295 ASP B O   1 
ATOM   5808 C  CB  . ASP B 1 295 ? 3.503   8.585   -11.585 1.00 25.47  ? 295 ASP B CB  1 
ATOM   5809 C  CG  . ASP B 1 295 ? 2.863   7.811   -10.444 1.00 24.58  ? 295 ASP B CG  1 
ATOM   5810 O  OD1 . ASP B 1 295 ? 3.587   7.465   -9.464  1.00 25.29  ? 295 ASP B OD1 1 
ATOM   5811 O  OD2 . ASP B 1 295 ? 1.657   7.561   -10.550 1.00 20.20  ? 295 ASP B OD2 1 
ATOM   5812 N  N   . VAL B 1 296 ? 5.100   10.989  -12.937 1.00 27.66  ? 296 VAL B N   1 
ATOM   5813 C  CA  . VAL B 1 296 ? 5.546   11.600  -14.219 1.00 30.08  ? 296 VAL B CA  1 
ATOM   5814 C  C   . VAL B 1 296 ? 7.012   11.994  -14.079 1.00 32.52  ? 296 VAL B C   1 
ATOM   5815 O  O   . VAL B 1 296 ? 7.809   11.629  -14.962 1.00 35.51  ? 296 VAL B O   1 
ATOM   5816 C  CB  . VAL B 1 296 ? 4.659   12.779  -14.651 1.00 26.71  ? 296 VAL B CB  1 
ATOM   5817 C  CG1 . VAL B 1 296 ? 5.197   13.435  -15.907 1.00 26.16  ? 296 VAL B CG1 1 
ATOM   5818 C  CG2 . VAL B 1 296 ? 3.238   12.314  -14.863 1.00 26.56  ? 296 VAL B CG2 1 
ATOM   5819 N  N   . VAL B 1 297 ? 7.366   12.658  -12.983 1.00 35.86  ? 297 VAL B N   1 
ATOM   5820 C  CA  . VAL B 1 297 ? 8.787   13.004  -12.703 1.00 36.33  ? 297 VAL B CA  1 
ATOM   5821 C  C   . VAL B 1 297 ? 9.585   11.690  -12.681 1.00 37.07  ? 297 VAL B C   1 
ATOM   5822 O  O   . VAL B 1 297 ? 10.540  11.585  -13.428 1.00 36.80  ? 297 VAL B O   1 
ATOM   5823 C  CB  . VAL B 1 297 ? 8.930   13.842  -11.414 1.00 38.51  ? 297 VAL B CB  1 
ATOM   5824 C  CG1 . VAL B 1 297 ? 10.384  14.104  -11.052 1.00 39.80  ? 297 VAL B CG1 1 
ATOM   5825 C  CG2 . VAL B 1 297 ? 8.172   15.162  -11.508 1.00 37.90  ? 297 VAL B CG2 1 
ATOM   5826 N  N   . ARG B 1 298 ? 9.195   10.712  -11.865 1.00 39.50  ? 298 ARG B N   1 
ATOM   5827 C  CA  . ARG B 1 298 ? 9.902   9.404   -11.704 1.00 40.52  ? 298 ARG B CA  1 
ATOM   5828 C  C   . ARG B 1 298 ? 10.222  8.790   -13.080 1.00 37.19  ? 298 ARG B C   1 
ATOM   5829 O  O   . ARG B 1 298 ? 11.368  8.388   -13.265 1.00 37.56  ? 298 ARG B O   1 
ATOM   5830 C  CB  . ARG B 1 298 ? 9.063   8.496   -10.789 1.00 48.75  ? 298 ARG B CB  1 
ATOM   5831 C  CG  . ARG B 1 298 ? 9.124   6.997   -11.052 1.00 56.71  ? 298 ARG B CG  1 
ATOM   5832 C  CD  . ARG B 1 298 ? 7.739   6.324   -11.195 1.00 60.46  ? 298 ARG B CD  1 
ATOM   5833 N  NE  . ARG B 1 298 ? 7.878   4.865   -11.159 1.00 58.16  ? 298 ARG B NE  1 
ATOM   5834 C  CZ  . ARG B 1 298 ? 6.921   3.963   -11.314 1.00 41.30  ? 298 ARG B CZ  1 
ATOM   5835 N  NH1 . ARG B 1 298 ? 5.679   4.327   -11.516 1.00 39.05  ? 298 ARG B NH1 1 
ATOM   5836 N  NH2 . ARG B 1 298 ? 7.234   2.683   -11.231 1.00 45.29  ? 298 ARG B NH2 1 
ATOM   5837 N  N   . GLN B 1 299 ? 9.252   8.704   -13.994 1.00 32.13  ? 299 GLN B N   1 
ATOM   5838 C  CA  . GLN B 1 299 ? 9.327   7.905   -15.253 1.00 34.07  ? 299 GLN B CA  1 
ATOM   5839 C  C   . GLN B 1 299 ? 10.088  8.704   -16.319 1.00 38.07  ? 299 GLN B C   1 
ATOM   5840 O  O   . GLN B 1 299 ? 10.768  8.054   -17.152 1.00 34.58  ? 299 GLN B O   1 
ATOM   5841 C  CB  . GLN B 1 299 ? 7.923   7.515   -15.757 1.00 30.32  ? 299 GLN B CB  1 
ATOM   5842 C  CG  . GLN B 1 299 ? 7.923   6.899   -17.144 1.00 27.87  ? 299 GLN B CG  1 
ATOM   5843 C  CD  . GLN B 1 299 ? 6.668   6.175   -17.558 1.00 27.17  ? 299 GLN B CD  1 
ATOM   5844 O  OE1 . GLN B 1 299 ? 6.558   5.716   -18.688 1.00 29.19  ? 299 GLN B OE1 1 
ATOM   5845 N  NE2 . GLN B 1 299 ? 5.700   6.057   -16.670 1.00 24.45  ? 299 GLN B NE2 1 
ATOM   5846 N  N   . CYS B 1 300 ? 9.968   10.043  -16.302 1.00 36.82  ? 300 CYS B N   1 
ATOM   5847 C  CA  . CYS B 1 300 ? 10.484  10.955  -17.368 1.00 42.55  ? 300 CYS B CA  1 
ATOM   5848 C  C   . CYS B 1 300 ? 11.853  11.564  -17.019 1.00 48.94  ? 300 CYS B C   1 
ATOM   5849 O  O   . CYS B 1 300 ? 12.502  12.031  -17.954 1.00 52.60  ? 300 CYS B O   1 
ATOM   5850 C  CB  . CYS B 1 300 ? 9.519   12.097  -17.648 1.00 38.50  ? 300 CYS B CB  1 
ATOM   5851 S  SG  . CYS B 1 300 ? 8.001   11.543  -18.452 1.00 41.45  ? 300 CYS B SG  1 
ATOM   5852 N  N   . SER B 1 301 ? 12.261  11.569  -15.743 1.00 61.31  ? 301 SER B N   1 
ATOM   5853 C  CA  . SER B 1 301 ? 13.462  12.265  -15.196 1.00 63.21  ? 301 SER B CA  1 
ATOM   5854 C  C   . SER B 1 301 ? 14.169  11.337  -14.199 1.00 63.08  ? 301 SER B C   1 
ATOM   5855 O  O   . SER B 1 301 ? 14.482  10.182  -14.517 1.00 60.68  ? 301 SER B O   1 
ATOM   5856 C  CB  . SER B 1 301 ? 13.099  13.596  -14.544 1.00 67.74  ? 301 SER B CB  1 
ATOM   5857 O  OG  . SER B 1 301 ? 12.462  14.492  -15.461 1.00 74.32  ? 301 SER B OG  1 
HETATM 5858 CL CL  . CL  C 2 .   ? 5.282   -15.202 -31.038 1.00 35.98  ? 401 CL  A CL  1 
HETATM 5859 C  C4  C RB7 D 3 .   ? 24.950  3.760   -28.732 0.30 42.88  ? 402 RB7 A C4  1 
HETATM 5860 C  C4  D RB7 D 3 .   ? 24.950  3.760   -28.731 0.30 42.88  ? 402 RB7 A C4  1 
HETATM 5861 C  C5  C RB7 D 3 .   ? 23.948  3.159   -29.536 0.30 40.56  ? 402 RB7 A C5  1 
HETATM 5862 C  C5  D RB7 D 3 .   ? 23.948  3.159   -29.536 0.30 40.56  ? 402 RB7 A C5  1 
HETATM 5863 C  C6  C RB7 D 3 .   ? 24.325  2.634   -30.791 0.30 40.41  ? 402 RB7 A C6  1 
HETATM 5864 C  C6  D RB7 D 3 .   ? 24.325  2.634   -30.791 0.30 40.41  ? 402 RB7 A C6  1 
HETATM 5865 C  C7  C RB7 D 3 .   ? 27.444  4.523   -28.304 0.30 48.47  ? 402 RB7 A C7  1 
HETATM 5866 C  C7  D RB7 D 3 .   ? 27.444  4.523   -28.304 0.30 48.47  ? 402 RB7 A C7  1 
HETATM 5867 C  C8  C RB7 D 3 .   ? 26.224  6.292   -26.825 0.30 59.33  ? 402 RB7 A C8  1 
HETATM 5868 C  C8  D RB7 D 3 .   ? 26.224  6.292   -26.825 0.30 59.33  ? 402 RB7 A C8  1 
HETATM 5869 C  C9  C RB7 D 3 .   ? 26.979  7.472   -26.110 0.30 62.64  ? 402 RB7 A C9  1 
HETATM 5870 C  C9  D RB7 D 3 .   ? 26.979  7.472   -26.110 0.30 62.64  ? 402 RB7 A C9  1 
HETATM 5871 C  C10 C RB7 D 3 .   ? 29.897  7.976   -26.096 0.30 65.51  ? 402 RB7 A C10 1 
HETATM 5872 C  C10 D RB7 D 3 .   ? 29.897  7.976   -26.096 0.30 65.51  ? 402 RB7 A C10 1 
HETATM 5873 O  O1  C RB7 D 3 .   ? 28.836  5.570   -25.696 0.30 69.09  ? 402 RB7 A O1  1 
HETATM 5874 O  O1  D RB7 D 3 .   ? 28.836  5.570   -25.696 0.30 69.09  ? 402 RB7 A O1  1 
HETATM 5875 S  S   C RB7 D 3 .   ? 28.594  6.960   -25.415 0.30 68.82  ? 402 RB7 A S   1 
HETATM 5876 S  S   D RB7 D 3 .   ? 28.594  6.960   -25.415 0.30 68.82  ? 402 RB7 A S   1 
HETATM 5877 O  O   C RB7 D 3 .   ? 28.564  7.041   -23.975 0.30 70.42  ? 402 RB7 A O   1 
HETATM 5878 O  O   D RB7 D 3 .   ? 28.564  7.041   -23.975 0.30 70.42  ? 402 RB7 A O   1 
HETATM 5879 N  N   C RB7 D 3 .   ? 27.005  4.957   -26.900 0.30 54.67  ? 402 RB7 A N   1 
HETATM 5880 N  N   D RB7 D 3 .   ? 27.005  4.957   -26.900 0.30 54.67  ? 402 RB7 A N   1 
HETATM 5881 C  C3  C RB7 D 3 .   ? 26.314  3.850   -29.186 0.30 44.93  ? 402 RB7 A C3  1 
HETATM 5882 C  C3  D RB7 D 3 .   ? 26.314  3.850   -29.186 0.30 44.93  ? 402 RB7 A C3  1 
HETATM 5883 C  C2  C RB7 D 3 .   ? 26.627  3.302   -30.473 0.30 41.85  ? 402 RB7 A C2  1 
HETATM 5884 C  C2  D RB7 D 3 .   ? 26.627  3.302   -30.473 0.30 41.85  ? 402 RB7 A C2  1 
HETATM 5885 BR BR  C RB7 D 3 .   ? 22.924  1.803   -31.855 0.30 42.66  ? 402 RB7 A BR  1 
HETATM 5886 BR BR  D RB7 D 3 .   ? 22.924  1.803   -31.855 0.30 42.66  ? 402 RB7 A BR  1 
HETATM 5887 C  C1  C RB7 D 3 .   ? 25.653  2.690   -31.292 0.30 37.48  ? 402 RB7 A C1  1 
HETATM 5888 C  C1  D RB7 D 3 .   ? 25.653  2.690   -31.292 0.30 37.48  ? 402 RB7 A C1  1 
HETATM 5889 C  C   C RB7 D 3 .   ? 26.033  2.138   -32.601 0.30 34.35  ? 402 RB7 A C   1 
HETATM 5890 C  C   D RB7 D 3 .   ? 26.033  2.138   -32.601 0.30 34.35  ? 402 RB7 A C   1 
HETATM 5891 S  S   . DMS E 4 .   ? -0.632  -11.569 -18.191 1.00 44.04  ? 403 DMS A S   1 
HETATM 5892 O  O   . DMS E 4 .   ? 0.263   -11.185 -19.384 1.00 44.33  ? 403 DMS A O   1 
HETATM 5893 C  C1  . DMS E 4 .   ? 0.375   -11.353 -16.732 1.00 37.90  ? 403 DMS A C1  1 
HETATM 5894 C  C2  . DMS E 4 .   ? -0.642  -13.335 -18.149 1.00 42.71  ? 403 DMS A C2  1 
HETATM 5895 NA NA  . NA  F 5 .   ? -2.389  27.872  -22.152 1.00 44.26  ? 401 NA  B NA  1 
HETATM 5896 O  O   . HOH G 6 .   ? -3.632  -2.156  -26.280 1.00 35.97  ? 501 HOH A O   1 
HETATM 5897 O  O   . HOH G 6 .   ? 23.396  -18.199 -20.164 1.00 44.16  ? 502 HOH A O   1 
HETATM 5898 O  O   . HOH G 6 .   ? -1.408  -11.549 -31.653 1.00 25.39  ? 503 HOH A O   1 
HETATM 5899 O  O   . HOH G 6 .   ? -15.734 -11.797 -50.609 1.00 29.81  ? 504 HOH A O   1 
HETATM 5900 O  O   . HOH G 6 .   ? -17.838 -5.048  -46.865 1.00 27.81  ? 505 HOH A O   1 
HETATM 5901 O  O   . HOH G 6 .   ? 26.095  -2.430  -37.007 1.00 28.89  ? 506 HOH A O   1 
HETATM 5902 O  O   . HOH G 6 .   ? -1.074  -15.104 -40.086 1.00 31.86  ? 507 HOH A O   1 
HETATM 5903 O  O   . HOH G 6 .   ? -8.624  1.680   -34.682 1.00 30.06  ? 508 HOH A O   1 
HETATM 5904 O  O   . HOH G 6 .   ? 28.586  -1.259  -38.171 1.00 35.75  ? 509 HOH A O   1 
HETATM 5905 O  O   . HOH G 6 .   ? -18.865 -9.520  -47.254 1.00 27.35  ? 510 HOH A O   1 
HETATM 5906 O  O   . HOH G 6 .   ? 4.537   -1.788  -28.230 1.00 17.57  ? 511 HOH A O   1 
HETATM 5907 O  O   . HOH G 6 .   ? -21.059 0.058   -44.087 1.00 32.92  ? 512 HOH A O   1 
HETATM 5908 O  O   . HOH G 6 .   ? -15.647 0.457   -42.167 1.00 32.45  ? 513 HOH A O   1 
HETATM 5909 O  O   . HOH G 6 .   ? 8.789   -13.227 -11.409 1.00 21.92  ? 514 HOH A O   1 
HETATM 5910 O  O   . HOH G 6 .   ? -0.946  -8.055  -22.913 1.00 28.21  ? 515 HOH A O   1 
HETATM 5911 O  O   . HOH G 6 .   ? 15.434  -5.840  -17.603 1.00 26.49  ? 516 HOH A O   1 
HETATM 5912 O  O   . HOH G 6 .   ? 16.036  -14.238 -10.426 1.00 30.38  ? 517 HOH A O   1 
HETATM 5913 O  O   . HOH G 6 .   ? 22.503  -16.064 -27.028 1.00 32.07  ? 518 HOH A O   1 
HETATM 5914 O  O   . HOH G 6 .   ? -6.066  -6.247  -27.990 1.00 23.29  ? 519 HOH A O   1 
HETATM 5915 O  O   . HOH G 6 .   ? 0.589   0.783   -28.673 1.00 40.27  ? 520 HOH A O   1 
HETATM 5916 O  O   . HOH G 6 .   ? 29.494  0.425   -42.172 1.00 27.78  ? 521 HOH A O   1 
HETATM 5917 O  O   . HOH G 6 .   ? -13.404 -14.206 -48.095 1.00 30.01  ? 522 HOH A O   1 
HETATM 5918 O  O   . HOH G 6 .   ? 13.421  -3.833  -33.090 1.00 28.01  ? 523 HOH A O   1 
HETATM 5919 O  O   . HOH G 6 .   ? 15.512  -14.520 -27.618 1.00 22.75  ? 524 HOH A O   1 
HETATM 5920 O  O   . HOH G 6 .   ? -20.396 -4.462  -40.746 1.00 30.01  ? 525 HOH A O   1 
HETATM 5921 O  O   . HOH G 6 .   ? 2.340   -11.136 -22.595 1.00 29.75  ? 526 HOH A O   1 
HETATM 5922 O  O   A HOH G 6 .   ? 18.991  5.398   -28.855 0.20 8.93   ? 527 HOH A O   1 
HETATM 5923 O  O   B HOH G 6 .   ? 18.991  5.398   -28.855 0.20 8.93   ? 527 HOH A O   1 
HETATM 5924 O  O   C HOH G 6 .   ? 19.083  5.213   -29.368 0.30 16.87  ? 527 HOH A O   1 
HETATM 5925 O  O   D HOH G 6 .   ? 19.083  5.213   -29.368 0.30 16.87  ? 527 HOH A O   1 
HETATM 5926 O  O   . HOH G 6 .   ? -3.940  -9.261  -37.388 1.00 19.67  ? 528 HOH A O   1 
HETATM 5927 O  O   . HOH G 6 .   ? 20.586  -8.307  -36.439 1.00 23.73  ? 529 HOH A O   1 
HETATM 5928 O  O   . HOH G 6 .   ? 24.385  -3.355  -29.977 1.00 22.90  ? 530 HOH A O   1 
HETATM 5929 O  O   . HOH G 6 .   ? -1.815  -7.936  -20.334 1.00 26.09  ? 531 HOH A O   1 
HETATM 5930 O  O   . HOH G 6 .   ? 30.991  -4.817  -37.528 1.00 24.67  ? 532 HOH A O   1 
HETATM 5931 O  O   . HOH G 6 .   ? 32.353  -7.221  -37.136 1.00 35.72  ? 533 HOH A O   1 
HETATM 5932 O  O   . HOH G 6 .   ? -8.138  -11.470 -47.706 1.00 29.96  ? 534 HOH A O   1 
HETATM 5933 O  O   . HOH G 6 .   ? -19.877 -7.592  -45.517 1.00 27.73  ? 535 HOH A O   1 
HETATM 5934 O  O   . HOH G 6 .   ? -24.619 -9.898  -43.373 1.00 32.31  ? 536 HOH A O   1 
HETATM 5935 O  O   . HOH G 6 .   ? 15.837  -16.391 -29.510 1.00 30.79  ? 537 HOH A O   1 
HETATM 5936 O  O   . HOH G 6 .   ? -21.025 -10.852 -47.538 1.00 32.08  ? 538 HOH A O   1 
HETATM 5937 O  O   . HOH H 6 .   ? -0.114  -9.787  -4.027  1.00 49.79  ? 501 HOH B O   1 
HETATM 5938 O  O   . HOH H 6 .   ? 7.097   -16.960 15.393  1.00 39.92  ? 502 HOH B O   1 
HETATM 5939 O  O   . HOH H 6 .   ? -3.407  -22.970 2.100   1.00 36.78  ? 503 HOH B O   1 
HETATM 5940 O  O   . HOH H 6 .   ? -11.786 0.151   -1.150  1.00 17.21  ? 504 HOH B O   1 
HETATM 5941 O  O   . HOH H 6 .   ? 1.100   5.520   -12.095 1.00 23.81  ? 505 HOH B O   1 
HETATM 5942 O  O   . HOH H 6 .   ? -8.024  2.484   -10.154 1.00 23.05  ? 506 HOH B O   1 
HETATM 5943 O  O   . HOH H 6 .   ? -2.877  11.022  -15.020 1.00 25.78  ? 507 HOH B O   1 
HETATM 5944 O  O   . HOH H 6 .   ? 2.967   8.669   -6.854  1.00 31.01  ? 508 HOH B O   1 
HETATM 5945 O  O   . HOH H 6 .   ? -3.314  29.701  -28.352 1.00 32.01  ? 509 HOH B O   1 
HETATM 5946 O  O   . HOH H 6 .   ? -12.302 -6.853  14.005  1.00 33.65  ? 510 HOH B O   1 
HETATM 5947 O  O   . HOH H 6 .   ? 2.995   4.581   -7.665  1.00 25.27  ? 511 HOH B O   1 
HETATM 5948 O  O   . HOH H 6 .   ? 10.890  -5.727  -6.020  1.00 23.81  ? 512 HOH B O   1 
HETATM 5949 O  O   . HOH H 6 .   ? -8.592  5.953   -25.101 1.00 27.70  ? 513 HOH B O   1 
HETATM 5950 O  O   . HOH H 6 .   ? -1.457  -0.245  5.263   1.00 21.70  ? 514 HOH B O   1 
HETATM 5951 O  O   . HOH H 6 .   ? -12.193 13.712  -29.853 1.00 42.67  ? 515 HOH B O   1 
HETATM 5952 O  O   . HOH H 6 .   ? -12.571 -9.638  5.153   1.00 20.03  ? 516 HOH B O   1 
HETATM 5953 O  O   . HOH H 6 .   ? 1.277   7.411   -4.880  1.00 34.13  ? 517 HOH B O   1 
HETATM 5954 O  O   . HOH H 6 .   ? -16.375 -4.138  7.656   1.00 33.47  ? 518 HOH B O   1 
HETATM 5955 O  O   . HOH H 6 .   ? 3.026   4.540   -13.772 1.00 18.27  ? 519 HOH B O   1 
HETATM 5956 O  O   A HOH H 6 .   ? -10.780 -14.329 -3.416  0.25 19.75  ? 520 HOH B O   1 
HETATM 5957 O  O   B HOH H 6 .   ? -10.780 -14.329 -3.416  0.25 19.75  ? 520 HOH B O   1 
HETATM 5958 O  O   C HOH H 6 .   ? -9.852  -12.528 -2.312  0.25 34.17  ? 520 HOH B O   1 
HETATM 5959 O  O   D HOH H 6 .   ? -9.852  -12.528 -2.312  0.25 34.17  ? 520 HOH B O   1 
HETATM 5960 O  O   . HOH H 6 .   ? 5.222   6.407   -13.768 1.00 26.93  ? 521 HOH B O   1 
HETATM 5961 O  O   . HOH H 6 .   ? -15.886 2.978   -9.242  1.00 33.43  ? 522 HOH B O   1 
HETATM 5962 O  O   . HOH H 6 .   ? -7.166  17.126  -8.158  1.00 35.69  ? 523 HOH B O   1 
# 
