data_8W1U
# 
_entry.id   8W1U 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8W1U         pdb_00008w1u 10.2210/pdb8w1u/pdb 
WWPDB D_1000281698 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8W1U 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8W1T 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              sacchett@tamu.edu 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_last          Sacchettini 
_pdbx_contact_author.name_mi            C. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5767-2367 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bian, X.'          1 ? 
'Tang, S.'          2 ? 
'Sacchettini, J.C.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Cell Rep' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2211-1247 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            43 
_citation.language                  ? 
_citation.page_first                114929 
_citation.page_last                 114929 
_citation.title                     
'An oral non-covalent non-peptidic inhibitor of SARS-CoV-2 Mpro ameliorates viral replication and pathogenesis in vivo.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.celrep.2024.114929 
_citation.pdbx_database_id_PubMed   39504242 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhou, N.E.'         1  ? 
primary 'Tang, S.'           2  ? 
primary 'Bian, X.'           3  ? 
primary 'Parai, M.K.'        4  ? 
primary 'Krieger, I.V.'      5  ? 
primary 'Flores, A.'         6  ? 
primary 'Jaiswal, P.K.'      7  ? 
primary 'Bam, R.'            8  ? 
primary 'Wood, J.L.'         9  ? 
primary 'Shi, Z.'            10 ? 
primary 'Stevens, L.J.'      11 ? 
primary 'Scobey, T.'         12 ? 
primary 'Diefenbacher, M.V.' 13 ? 
primary 'Moreira, F.R.'      14 ? 
primary 'Baric, T.J.'        15 ? 
primary 'Acharya, A.'        16 ? 
primary 'Shin, J.'           17 ? 
primary 'Rathi, M.M.'        18 ? 
primary 'Wolff, K.C.'        19 ? 
primary 'Riva, L.'           20 ? 
primary 'Bakowski, M.A.'     21 ? 
primary 'McNamara, C.W.'     22 ? 
primary 'Catanzaro, N.J.'    23 ? 
primary 'Graham, R.L.'       24 ? 
primary 'Schultz, D.C.'      25 ? 
primary 'Cherry, S.'         26 ? 
primary 'Kawaoka, Y.'        27 ? 
primary 'Halfmann, P.J.'     28 ? 
primary 'Baric, R.S.'        29 ? 
primary 'Denison, M.R.'      30 ? 
primary 'Sheahan, T.P.'      31 ? 
primary 'Sacchettini, J.C.'  32 ? 
# 
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 ? 'UNP residues 3264-3569' ? 
2 non-polymer syn 
'11-[1-(1H-pyrrolo[3,2-c]pyridine-7-carbonyl)piperidin-4-ylidene]-6,11-dihydro-5H-5lambda~6~-dibenzo[b,e]thiepine-5,5-dione' 
469.555   2   ?         ? ?                        ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    2   ?         ? ?                        ? 
4 water       nat water 18.015    113 ?         ? ?                        ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;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 '11-[1-(1H-pyrrolo[3,2-c]pyridine-7-carbonyl)piperidin-4-ylidene]-6,11-dihydro-5H-5lambda~6~-dibenzo[b,e]thiepine-5,5-dione' 
A1AFE 
3 'DIMETHYL SULFOXIDE'                                                                                                         DMS 
4 water                                                                                                                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   306 
_entity_src_gen.gene_src_common_name               'SARS-CoV-2, 2019-nCoV, COVID-19 virus' 
_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          ? 
_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 
A1AFE non-polymer         . 
'11-[1-(1H-pyrrolo[3,2-c]pyridine-7-carbonyl)piperidin-4-ylidene]-6,11-dihydro-5H-5lambda~6~-dibenzo[b,e]thiepine-5,5-dione' 
NZ-804 'C27 H23 N3 O3 S' 469.555 
ALA   'L-peptide linking' y ALANINE ?      'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ?      'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ?      'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?      'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE ?      'C3 H7 N O2 S'    121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ?      'C2 H6 O S'       78.133  
GLN   'L-peptide linking' y GLUTAMINE ?      'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?      'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE ?      'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE ?      'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER ?      'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?      'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE ?      'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE ?      'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE ?      'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?      'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ?      'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE ?      'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE ?      'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?      'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE ?      'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE ?      'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 ?   ?   ?   A . n 
A 1 303 VAL 303 303 ?   ?   ?   A . n 
A 1 304 THR 304 304 ?   ?   ?   A . n 
A 1 305 PHE 305 305 ?   ?   ?   A . n 
A 1 306 GLN 306 306 ?   ?   ?   A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   GLY 2   2   2   GLY GLY B . n 
B 1 3   PHE 3   3   3   PHE PHE B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   MET 6   6   6   MET MET B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  CYS 16  16  16  CYS CYS B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  TRP 31  31  31  TRP TRP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  CYS 38  38  38  CYS CYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  HIS 41  41  41  HIS HIS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  CYS 44  44  44  CYS CYS B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  MET 49  49  49  MET MET B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  ASN 51  51  51  ASN ASN B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 CYS 117 117 117 CYS CYS B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 GLN 127 127 127 GLN GLN B . n 
B 1 128 CYS 128 128 128 CYS CYS B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 MET 130 130 130 MET MET B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 CYS 145 145 145 CYS CYS B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 CYS 160 160 160 CYS CYS B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 MET 162 162 162 MET MET B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 MET 165 165 165 MET MET B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 HIS 172 172 172 HIS HIS B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 TRP 207 207 207 TRP TRP B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 TYR 209 209 209 TYR TYR B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 ASP 216 216 216 ASP ASP B . n 
B 1 217 ARG 217 217 217 ARG ARG B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 ASN 221 221 221 ASN ASN B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 ASN 228 228 228 ASN ASN B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 MET 235 235 235 MET MET B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 GLU 240 240 240 GLU GLU B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 HIS 246 246 246 HIS HIS B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 MET 264 264 264 MET MET B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 GLN 273 273 273 GLN GLN B . n 
B 1 274 ASN 274 274 274 ASN ASN B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 MET 276 276 276 MET MET B . n 
B 1 277 ASN 277 277 277 ASN ASN B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 PHE 291 291 291 PHE PHE B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 PRO 293 293 293 PRO PRO B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLN 299 299 299 GLN GLN B . n 
B 1 300 CYS 300 300 300 CYS CYS B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 GLY 302 302 ?   ?   ?   B . n 
B 1 303 VAL 303 303 ?   ?   ?   B . n 
B 1 304 THR 304 304 ?   ?   ?   B . n 
B 1 305 PHE 305 305 ?   ?   ?   B . n 
B 1 306 GLN 306 306 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AFE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AFE 
_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 A1AFE 1  401 401 A1AFE Z0N A . 
D 3 DMS   1  402 402 DMS   DMS A . 
E 2 A1AFE 1  401 401 A1AFE Z0N B . 
F 3 DMS   1  402 402 DMS   DMS B . 
G 4 HOH   1  501 21  HOH   HOH A . 
G 4 HOH   2  502 38  HOH   HOH A . 
G 4 HOH   3  503 100 HOH   HOH A . 
G 4 HOH   4  504 14  HOH   HOH A . 
G 4 HOH   5  505 16  HOH   HOH A . 
G 4 HOH   6  506 76  HOH   HOH A . 
G 4 HOH   7  507 107 HOH   HOH A . 
G 4 HOH   8  508 70  HOH   HOH A . 
G 4 HOH   9  509 84  HOH   HOH A . 
G 4 HOH   10 510 103 HOH   HOH A . 
G 4 HOH   11 511 40  HOH   HOH A . 
G 4 HOH   12 512 33  HOH   HOH A . 
G 4 HOH   13 513 51  HOH   HOH A . 
G 4 HOH   14 514 6   HOH   HOH A . 
G 4 HOH   15 515 18  HOH   HOH A . 
G 4 HOH   16 516 7   HOH   HOH A . 
G 4 HOH   17 517 2   HOH   HOH A . 
G 4 HOH   18 518 15  HOH   HOH A . 
G 4 HOH   19 519 17  HOH   HOH A . 
G 4 HOH   20 520 47  HOH   HOH A . 
G 4 HOH   21 521 56  HOH   HOH A . 
G 4 HOH   22 522 68  HOH   HOH A . 
G 4 HOH   23 523 105 HOH   HOH A . 
G 4 HOH   24 524 49  HOH   HOH A . 
G 4 HOH   25 525 3   HOH   HOH A . 
G 4 HOH   26 526 75  HOH   HOH A . 
G 4 HOH   27 527 99  HOH   HOH A . 
G 4 HOH   28 528 53  HOH   HOH A . 
G 4 HOH   29 529 59  HOH   HOH A . 
G 4 HOH   30 530 23  HOH   HOH A . 
G 4 HOH   31 531 42  HOH   HOH A . 
G 4 HOH   32 532 10  HOH   HOH A . 
G 4 HOH   33 533 112 HOH   HOH A . 
G 4 HOH   34 534 30  HOH   HOH A . 
G 4 HOH   35 535 82  HOH   HOH A . 
G 4 HOH   36 536 45  HOH   HOH A . 
G 4 HOH   37 537 48  HOH   HOH A . 
G 4 HOH   38 538 91  HOH   HOH A . 
G 4 HOH   39 539 35  HOH   HOH A . 
G 4 HOH   40 540 4   HOH   HOH A . 
G 4 HOH   41 541 58  HOH   HOH A . 
G 4 HOH   42 542 52  HOH   HOH A . 
G 4 HOH   43 543 26  HOH   HOH A . 
G 4 HOH   44 544 90  HOH   HOH A . 
G 4 HOH   45 545 111 HOH   HOH A . 
G 4 HOH   46 546 89  HOH   HOH A . 
G 4 HOH   47 547 73  HOH   HOH A . 
G 4 HOH   48 548 95  HOH   HOH A . 
H 4 HOH   1  501 62  HOH   HOH B . 
H 4 HOH   2  502 98  HOH   HOH B . 
H 4 HOH   3  503 34  HOH   HOH B . 
H 4 HOH   4  504 55  HOH   HOH B . 
H 4 HOH   5  505 66  HOH   HOH B . 
H 4 HOH   6  506 28  HOH   HOH B . 
H 4 HOH   7  507 96  HOH   HOH B . 
H 4 HOH   8  508 27  HOH   HOH B . 
H 4 HOH   9  509 97  HOH   HOH B . 
H 4 HOH   10 510 19  HOH   HOH B . 
H 4 HOH   11 511 94  HOH   HOH B . 
H 4 HOH   12 512 57  HOH   HOH B . 
H 4 HOH   13 513 44  HOH   HOH B . 
H 4 HOH   14 514 93  HOH   HOH B . 
H 4 HOH   15 515 46  HOH   HOH B . 
H 4 HOH   16 516 79  HOH   HOH B . 
H 4 HOH   17 517 25  HOH   HOH B . 
H 4 HOH   18 518 9   HOH   HOH B . 
H 4 HOH   19 519 102 HOH   HOH B . 
H 4 HOH   20 520 60  HOH   HOH B . 
H 4 HOH   21 521 50  HOH   HOH B . 
H 4 HOH   22 522 24  HOH   HOH B . 
H 4 HOH   23 523 32  HOH   HOH B . 
H 4 HOH   24 524 64  HOH   HOH B . 
H 4 HOH   25 525 61  HOH   HOH B . 
H 4 HOH   26 526 11  HOH   HOH B . 
H 4 HOH   27 527 39  HOH   HOH B . 
H 4 HOH   28 528 20  HOH   HOH B . 
H 4 HOH   29 529 8   HOH   HOH B . 
H 4 HOH   30 530 5   HOH   HOH B . 
H 4 HOH   31 531 88  HOH   HOH B . 
H 4 HOH   32 532 87  HOH   HOH B . 
H 4 HOH   33 533 81  HOH   HOH B . 
H 4 HOH   34 534 12  HOH   HOH B . 
H 4 HOH   35 535 71  HOH   HOH B . 
H 4 HOH   36 536 86  HOH   HOH B . 
H 4 HOH   37 537 65  HOH   HOH B . 
H 4 HOH   38 538 1   HOH   HOH B . 
H 4 HOH   39 539 109 HOH   HOH B . 
H 4 HOH   40 540 92  HOH   HOH B . 
H 4 HOH   41 541 36  HOH   HOH B . 
H 4 HOH   42 542 74  HOH   HOH B . 
H 4 HOH   43 543 67  HOH   HOH B . 
H 4 HOH   44 544 43  HOH   HOH B . 
H 4 HOH   45 545 22  HOH   HOH B . 
H 4 HOH   46 546 37  HOH   HOH B . 
H 4 HOH   47 547 54  HOH   HOH B . 
H 4 HOH   48 548 31  HOH   HOH B . 
H 4 HOH   49 549 72  HOH   HOH B . 
H 4 HOH   50 550 13  HOH   HOH B . 
H 4 HOH   51 551 29  HOH   HOH B . 
H 4 HOH   52 552 101 HOH   HOH B . 
H 4 HOH   53 553 77  HOH   HOH B . 
H 4 HOH   54 554 78  HOH   HOH B . 
H 4 HOH   55 555 110 HOH   HOH B . 
H 4 HOH   56 556 83  HOH   HOH B . 
H 4 HOH   57 557 80  HOH   HOH B . 
H 4 HOH   58 558 41  HOH   HOH B . 
H 4 HOH   59 559 69  HOH   HOH B . 
H 4 HOH   60 560 104 HOH   HOH B . 
H 4 HOH   61 561 108 HOH   HOH B . 
H 4 HOH   62 562 63  HOH   HOH B . 
H 4 HOH   63 563 106 HOH   HOH B . 
H 4 HOH   64 564 85  HOH   HOH B . 
H 4 HOH   65 565 113 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 47  ? CG  ? A GLU 47  CG  
2  1 Y 1 A GLU 47  ? CD  ? A GLU 47  CD  
3  1 Y 1 A GLU 47  ? OE1 ? A GLU 47  OE1 
4  1 Y 1 A GLU 47  ? OE2 ? A GLU 47  OE2 
5  1 Y 1 A ASN 72  ? CG  ? A ASN 72  CG  
6  1 Y 1 A ASN 72  ? OD1 ? A ASN 72  OD1 
7  1 Y 1 A ASN 72  ? ND2 ? A ASN 72  ND2 
8  1 Y 1 A LEU 75  ? CG  ? A LEU 75  CG  
9  1 Y 1 A LEU 75  ? CD1 ? A LEU 75  CD1 
10 1 Y 1 A LEU 75  ? CD2 ? A LEU 75  CD2 
11 1 Y 1 A TYR 154 ? CG  ? A TYR 154 CG  
12 1 Y 1 A TYR 154 ? CD1 ? A TYR 154 CD1 
13 1 Y 1 A TYR 154 ? CD2 ? A TYR 154 CD2 
14 1 Y 1 A TYR 154 ? CE1 ? A TYR 154 CE1 
15 1 Y 1 A TYR 154 ? CE2 ? A TYR 154 CE2 
16 1 Y 1 A TYR 154 ? CZ  ? A TYR 154 CZ  
17 1 Y 1 A TYR 154 ? OH  ? A TYR 154 OH  
18 1 Y 1 A ARG 222 ? CG  ? A ARG 222 CG  
19 1 Y 1 A ARG 222 ? CD  ? A ARG 222 CD  
20 1 Y 1 A ARG 222 ? NE  ? A ARG 222 NE  
21 1 Y 1 A ARG 222 ? CZ  ? A ARG 222 CZ  
22 1 Y 1 A ARG 222 ? NH1 ? A ARG 222 NH1 
23 1 Y 1 A ARG 222 ? NH2 ? A ARG 222 NH2 
24 1 Y 1 A ASP 229 ? CG  ? A ASP 229 CG  
25 1 Y 1 A ASP 229 ? OD1 ? A ASP 229 OD1 
26 1 Y 1 A ASP 229 ? OD2 ? A ASP 229 OD2 
27 1 Y 1 A LEU 232 ? CG  ? A LEU 232 CG  
28 1 Y 1 A LEU 232 ? CD1 ? A LEU 232 CD1 
29 1 Y 1 A LEU 232 ? CD2 ? A LEU 232 CD2 
30 1 Y 1 A MET 235 ? CG  ? A MET 235 CG  
31 1 Y 1 A MET 235 ? SD  ? A MET 235 SD  
32 1 Y 1 A MET 235 ? CE  ? A MET 235 CE  
33 1 Y 1 A LYS 236 ? CG  ? A LYS 236 CG  
34 1 Y 1 A LYS 236 ? CD  ? A LYS 236 CD  
35 1 Y 1 A LYS 236 ? CE  ? A LYS 236 CE  
36 1 Y 1 A LYS 236 ? NZ  ? A LYS 236 NZ  
37 1 Y 1 A LEU 271 ? CG  ? A LEU 271 CG  
38 1 Y 1 A LEU 271 ? CD1 ? A LEU 271 CD1 
39 1 Y 1 A LEU 271 ? CD2 ? A LEU 271 CD2 
40 1 Y 1 A ASN 277 ? CG  ? A ASN 277 CG  
41 1 Y 1 A ASN 277 ? OD1 ? A ASN 277 OD1 
42 1 Y 1 A ASN 277 ? ND2 ? A ASN 277 ND2 
43 1 Y 1 A ARG 279 ? CG  ? A ARG 279 CG  
44 1 Y 1 A ARG 279 ? CD  ? A ARG 279 CD  
45 1 Y 1 A ARG 279 ? NE  ? A ARG 279 NE  
46 1 Y 1 A ARG 279 ? CZ  ? A ARG 279 CZ  
47 1 Y 1 A ARG 279 ? NH1 ? A ARG 279 NH1 
48 1 Y 1 A ARG 279 ? NH2 ? A ARG 279 NH2 
49 1 Y 1 B GLU 47  ? CG  ? B GLU 47  CG  
50 1 Y 1 B GLU 47  ? CD  ? B GLU 47  CD  
51 1 Y 1 B GLU 47  ? OE1 ? B GLU 47  OE1 
52 1 Y 1 B GLU 47  ? OE2 ? B GLU 47  OE2 
53 1 Y 1 B ASP 153 ? CG  ? B ASP 153 CG  
54 1 Y 1 B ASP 153 ? OD1 ? B ASP 153 OD1 
55 1 Y 1 B ASP 153 ? OD2 ? B ASP 153 OD2 
56 1 Y 1 B TYR 154 ? CG  ? B TYR 154 CG  
57 1 Y 1 B TYR 154 ? CD1 ? B TYR 154 CD1 
58 1 Y 1 B TYR 154 ? CD2 ? B TYR 154 CD2 
59 1 Y 1 B TYR 154 ? CE1 ? B TYR 154 CE1 
60 1 Y 1 B TYR 154 ? CE2 ? B TYR 154 CE2 
61 1 Y 1 B TYR 154 ? CZ  ? B TYR 154 CZ  
62 1 Y 1 B TYR 154 ? OH  ? B TYR 154 OH  
63 1 Y 1 B ARG 222 ? CG  ? B ARG 222 CG  
64 1 Y 1 B ARG 222 ? CD  ? B ARG 222 CD  
65 1 Y 1 B ARG 222 ? NE  ? B ARG 222 NE  
66 1 Y 1 B ARG 222 ? CZ  ? B ARG 222 CZ  
67 1 Y 1 B ARG 222 ? NH1 ? B ARG 222 NH1 
68 1 Y 1 B ARG 222 ? NH2 ? B ARG 222 NH2 
69 1 Y 1 B ASP 229 ? CG  ? B ASP 229 CG  
70 1 Y 1 B ASP 229 ? OD1 ? B ASP 229 OD1 
71 1 Y 1 B ASP 229 ? OD2 ? B ASP 229 OD2 
72 1 Y 1 B MET 235 ? CG  ? B MET 235 CG  
73 1 Y 1 B MET 235 ? SD  ? B MET 235 SD  
74 1 Y 1 B MET 235 ? CE  ? B MET 235 CE  
75 1 Y 1 B LYS 236 ? CG  ? B LYS 236 CG  
76 1 Y 1 B LYS 236 ? CD  ? B LYS 236 CD  
77 1 Y 1 B LYS 236 ? CE  ? B LYS 236 CE  
78 1 Y 1 B LYS 236 ? NZ  ? B LYS 236 NZ  
79 1 Y 1 B ASN 238 ? CG  ? B ASN 238 CG  
80 1 Y 1 B ASN 238 ? OD1 ? B ASN 238 OD1 
81 1 Y 1 B ASN 238 ? ND2 ? B ASN 238 ND2 
82 1 Y 1 B ARG 279 ? CG  ? B ARG 279 CG  
83 1 Y 1 B ARG 279 ? CD  ? B ARG 279 CD  
84 1 Y 1 B ARG 279 ? NE  ? B ARG 279 NE  
85 1 Y 1 B ARG 279 ? CZ  ? B ARG 279 CZ  
86 1 Y 1 B ARG 279 ? NH1 ? B ARG 279 NH1 
87 1 Y 1 B ARG 279 ? NH2 ? B ARG 279 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   101.53 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8W1U 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.956 
_cell.length_a_esd                 ? 
_cell.length_b                     54.066 
_cell.length_b_esd                 ? 
_cell.length_c                     112.877 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8W1U 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8W1U 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.03 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.44 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.8 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M MES pH 6.8, 0.2 M lithium sulfate, 24% PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            290 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-04-12 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0332 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 23-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0332 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8W1U 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.05 
_reflns.d_resolution_low                               45.03 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     34252 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.05 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.098 
_reflns.pdbx_Rpim_I_all                                0.038 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       220460 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.090 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.05 
_reflns_shell.d_res_low                                     2.11 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           17609 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2661 
_reflns_shell.percent_possible_obs                          99.9 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.6 
_reflns_shell.pdbx_chi_squared                              1.18 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.4 
_reflns_shell.pdbx_Rrim_I_all                               1.624 
_reflns_shell.pdbx_Rpim_I_all                               0.624 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.589 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.496 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8W1U 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.05 
_refine.ls_d_res_low                             45.03 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     34123 
_refine.ls_number_reflns_R_free                  1648 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.34 
_refine.ls_percent_reflns_R_free                 4.83 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2451 
_refine.ls_R_factor_R_free                       0.2882 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2429 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            'Radom selection' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 37.90 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.33 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4571 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         76 
_refine_hist.number_atoms_solvent             113 
_refine_hist.number_atoms_total               4760 
_refine_hist.d_res_high                       2.05 
_refine_hist.d_res_low                        45.03 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.607  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.614 ? 1658 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041  ? 727  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 838  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.05 2.11  . . 140 2681 100.00 . . . . 0.3608 . . . . . . . . . . . 0.3810 
'X-RAY DIFFRACTION' 2.11 2.18  . . 123 2719 100.00 . . . . 0.3542 . . . . . . . . . . . 0.3825 
'X-RAY DIFFRACTION' 2.18 2.26  . . 115 2720 100.00 . . . . 0.3357 . . . . . . . . . . . 0.3292 
'X-RAY DIFFRACTION' 2.26 2.35  . . 136 2702 100.00 . . . . 0.3186 . . . . . . . . . . . 0.3541 
'X-RAY DIFFRACTION' 2.35 2.45  . . 126 2715 100.00 . . . . 0.3209 . . . . . . . . . . . 0.4090 
'X-RAY DIFFRACTION' 2.45 2.58  . . 115 2689 99.00  . . . . 0.3061 . . . . . . . . . . . 0.3890 
'X-RAY DIFFRACTION' 2.58 2.74  . . 140 2731 100.00 . . . . 0.2965 . . . . . . . . . . . 0.3962 
'X-RAY DIFFRACTION' 2.74 2.96  . . 141 2711 100.00 . . . . 0.2966 . . . . . . . . . . . 0.3369 
'X-RAY DIFFRACTION' 2.96 3.25  . . 172 2665 99.00  . . . . 0.2617 . . . . . . . . . . . 0.2975 
'X-RAY DIFFRACTION' 3.25 3.72  . . 167 2667 99.00  . . . . 0.2350 . . . . . . . . . . . 0.2658 
'X-RAY DIFFRACTION' 3.72 4.69  . . 128 2746 99.00  . . . . 0.1877 . . . . . . . . . . . 0.2376 
'X-RAY DIFFRACTION' 4.69 45.03 . . 145 2729 97.00  . . . . 0.1844 . . . . . . . . . . . 0.2350 
# 
_struct.entry_id                     8W1U 
_struct.title                        'SARS-CoV-2 Main protease bound to non-covalent lead molecule NZ-804' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8W1U 
_struct_keywords.text            'Protease, Inhibitor, Complex, HYDROLASE, HYDROLASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   HYDROLASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8W1U A 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
2 1 8W1U B 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3280  ? 
1 MORE         -6    ? 
1 'SSA (A^2)'  24550 ? 
# 
_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 THR A 45  ? LEU A 50  ? THR A 45  LEU A 50  1 ? 6  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? SER A 301 ? THR A 292 SER A 301 1 ? 10 
HELX_P HELX_P12 AB3 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P13 AB4 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P14 AB5 GLU B 47  ? ASN B 51  ? GLU B 47  ASN B 51  5 ? 5  
HELX_P HELX_P15 AB6 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P16 AB7 SER B 62  ? HIS B 64  ? SER B 62  HIS B 64  5 ? 3  
HELX_P HELX_P17 AB8 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P18 AB9 THR B 226 ? TYR B 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P19 AC1 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P20 AC2 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P21 AC3 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P22 AC4 THR B 292 ? SER B 301 ? THR B 292 SER B 301 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 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 PHE B 66  ? ALA B 70  ? PHE B 66  ALA B 70  
AA4 3 MET B 17  ? CYS B 22  ? MET B 17  CYS B 22  
AA4 4 THR B 25  ? LEU B 32  ? THR B 25  LEU B 32  
AA4 5 VAL B 35  ? PRO B 39  ? VAL B 35  PRO B 39  
AA4 6 VAL B 86  ? VAL B 91  ? VAL B 86  VAL B 91  
AA4 7 VAL B 77  ? GLN B 83  ? VAL B 77  GLN B 83  
AA5 1 TYR B 101 ? PHE B 103 ? TYR B 101 PHE B 103 
AA5 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA5 3 VAL B 148 ? ASP B 153 ? VAL B 148 ASP B 153 
AA5 4 THR B 111 ? TYR B 118 ? THR B 111 TYR B 118 
AA5 5 SER B 121 ? ALA B 129 ? SER B 121 ALA B 129 
AA6 1 TYR B 101 ? PHE B 103 ? TYR B 101 PHE B 103 
AA6 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA6 3 HIS B 172 ? THR B 175 ? HIS B 172 THR B 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 18  ? N VAL A 18  O GLY A 29  ? O GLY A 29  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N VAL A 36  ? N VAL A 36  O LEU A 89  ? O LEU A 89  
AA1 6 7 O LYS A 90  ? O LYS A 90  N ILE A 78  ? N ILE A 78  
AA2 1 2 N LYS A 102 ? N LYS A 102 O VAL A 157 ? O VAL A 157 
AA2 2 3 O TYR A 161 ? O TYR A 161 N GLY A 149 ? N GLY A 149 
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 VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
AA4 1 2 O VAL B 73  ? O VAL B 73  N ALA B 70  ? N ALA B 70  
AA4 2 3 O LEU B 67  ? O LEU B 67  N THR B 21  ? N THR B 21  
AA4 3 4 N VAL B 20  ? N VAL B 20  O LEU B 27  ? O LEU B 27  
AA4 4 5 N LEU B 30  ? N LEU B 30  O TYR B 37  ? O TYR B 37  
AA4 5 6 N CYS B 38  ? N CYS B 38  O LEU B 87  ? O LEU B 87  
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 VAL B 157 ? O VAL B 157 
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 VAL B 157 ? O VAL B 157 
AA6 2 3 N MET B 165 ? N MET B 165 O ALA B 173 ? O ALA B 173 
# 
_pdbx_entry_details.entry_id                   8W1U 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    290 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    501 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.16 
# 
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  ? ? 53.54   -125.20 
2  1 HIS A 41  ? ? -66.68  1.04    
3  1 ASN A 51  ? ? -157.17 82.04   
4  1 ASN A 84  ? ? 55.20   -121.36 
5  1 TYR A 154 ? ? 59.33   -120.14 
6  1 ALA A 191 ? ? -93.44  54.52   
7  1 ASP B 33  ? ? 58.47   -128.43 
8  1 ASN B 51  ? ? -152.84 80.74   
9  1 ASN B 84  ? ? 53.29   -120.06 
10 1 TYR B 154 ? ? 61.14   -124.29 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 302 ? A GLY 302 
2  1 Y 1 A VAL 303 ? A VAL 303 
3  1 Y 1 A THR 304 ? A THR 304 
4  1 Y 1 A PHE 305 ? A PHE 305 
5  1 Y 1 A GLN 306 ? A GLN 306 
6  1 Y 1 B GLY 302 ? B GLY 302 
7  1 Y 1 B VAL 303 ? B VAL 303 
8  1 Y 1 B THR 304 ? B THR 304 
9  1 Y 1 B PHE 305 ? B PHE 305 
10 1 Y 1 B GLN 306 ? B GLN 306 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AFE C02  C N N 1   
A1AFE C04  C N N 2   
A1AFE C05  C N N 3   
A1AFE C06  C N N 4   
A1AFE C07  C N N 5   
A1AFE C08  C N N 6   
A1AFE C09  C N N 7   
A1AFE C10  C Y N 8   
A1AFE C11  C Y N 9   
A1AFE C12  C Y N 10  
A1AFE C13  C Y N 11  
A1AFE C14  C Y N 12  
A1AFE C15  C Y N 13  
A1AFE C16  C N N 14  
A1AFE C20  C Y N 15  
A1AFE C21  C Y N 16  
A1AFE C22  C Y N 17  
A1AFE C23  C Y N 18  
A1AFE C24  C Y N 19  
A1AFE C25  C Y N 20  
A1AFE C26  C Y N 21  
A1AFE C27  C Y N 22  
A1AFE C29  C Y N 23  
A1AFE C30  C Y N 24  
A1AFE C31  C Y N 25  
A1AFE C32  C Y N 26  
A1AFE C34  C Y N 27  
A1AFE N03  N N N 28  
A1AFE N28  N Y N 29  
A1AFE N33  N Y N 30  
A1AFE O01  O N N 31  
A1AFE O18  O N N 32  
A1AFE O19  O N N 33  
A1AFE S17  S N N 34  
A1AFE H1   H N N 35  
A1AFE H2   H N N 36  
A1AFE H3   H N N 37  
A1AFE H4   H N N 38  
A1AFE H5   H N N 39  
A1AFE H6   H N N 40  
A1AFE H7   H N N 41  
A1AFE H8   H N N 42  
A1AFE H9   H N N 43  
A1AFE H10  H N N 44  
A1AFE H11  H N N 45  
A1AFE H12  H N N 46  
A1AFE H13  H N N 47  
A1AFE H14  H N N 48  
A1AFE H15  H N N 49  
A1AFE H16  H N N 50  
A1AFE H17  H N N 51  
A1AFE H18  H N N 52  
A1AFE H19  H N N 53  
A1AFE H20  H N N 54  
A1AFE H21  H N N 55  
A1AFE H22  H N N 56  
A1AFE H23  H N N 57  
ALA   N    N N N 58  
ALA   CA   C N S 59  
ALA   C    C N N 60  
ALA   O    O N N 61  
ALA   CB   C N N 62  
ALA   OXT  O N N 63  
ALA   H    H N N 64  
ALA   H2   H N N 65  
ALA   HA   H N N 66  
ALA   HB1  H N N 67  
ALA   HB2  H N N 68  
ALA   HB3  H N N 69  
ALA   HXT  H N N 70  
ARG   N    N N N 71  
ARG   CA   C N S 72  
ARG   C    C N N 73  
ARG   O    O N N 74  
ARG   CB   C N N 75  
ARG   CG   C N N 76  
ARG   CD   C N N 77  
ARG   NE   N N N 78  
ARG   CZ   C N N 79  
ARG   NH1  N N N 80  
ARG   NH2  N N N 81  
ARG   OXT  O N N 82  
ARG   H    H N N 83  
ARG   H2   H N N 84  
ARG   HA   H N N 85  
ARG   HB2  H N N 86  
ARG   HB3  H N N 87  
ARG   HG2  H N N 88  
ARG   HG3  H N N 89  
ARG   HD2  H N N 90  
ARG   HD3  H N N 91  
ARG   HE   H N N 92  
ARG   HH11 H N N 93  
ARG   HH12 H N N 94  
ARG   HH21 H N N 95  
ARG   HH22 H N N 96  
ARG   HXT  H N N 97  
ASN   N    N N N 98  
ASN   CA   C N S 99  
ASN   C    C N N 100 
ASN   O    O N N 101 
ASN   CB   C N N 102 
ASN   CG   C N N 103 
ASN   OD1  O N N 104 
ASN   ND2  N N N 105 
ASN   OXT  O N N 106 
ASN   H    H N N 107 
ASN   H2   H N N 108 
ASN   HA   H N N 109 
ASN   HB2  H N N 110 
ASN   HB3  H N N 111 
ASN   HD21 H N N 112 
ASN   HD22 H N N 113 
ASN   HXT  H N N 114 
ASP   N    N N N 115 
ASP   CA   C N S 116 
ASP   C    C N N 117 
ASP   O    O N N 118 
ASP   CB   C N N 119 
ASP   CG   C N N 120 
ASP   OD1  O N N 121 
ASP   OD2  O N N 122 
ASP   OXT  O N N 123 
ASP   H    H N N 124 
ASP   H2   H N N 125 
ASP   HA   H N N 126 
ASP   HB2  H N N 127 
ASP   HB3  H N N 128 
ASP   HD2  H N N 129 
ASP   HXT  H N N 130 
CYS   N    N N N 131 
CYS   CA   C N R 132 
CYS   C    C N N 133 
CYS   O    O N N 134 
CYS   CB   C N N 135 
CYS   SG   S N N 136 
CYS   OXT  O N N 137 
CYS   H    H N N 138 
CYS   H2   H N N 139 
CYS   HA   H N N 140 
CYS   HB2  H N N 141 
CYS   HB3  H N N 142 
CYS   HG   H N N 143 
CYS   HXT  H N N 144 
DMS   S    S N N 145 
DMS   O    O N N 146 
DMS   C1   C N N 147 
DMS   C2   C N N 148 
DMS   H11  H N N 149 
DMS   H12  H N N 150 
DMS   H13  H N N 151 
DMS   H21  H N N 152 
DMS   H22  H N N 153 
DMS   H23  H N N 154 
GLN   N    N N N 155 
GLN   CA   C N S 156 
GLN   C    C N N 157 
GLN   O    O N N 158 
GLN   CB   C N N 159 
GLN   CG   C N N 160 
GLN   CD   C N N 161 
GLN   OE1  O N N 162 
GLN   NE2  N N N 163 
GLN   OXT  O N N 164 
GLN   H    H N N 165 
GLN   H2   H N N 166 
GLN   HA   H N N 167 
GLN   HB2  H N N 168 
GLN   HB3  H N N 169 
GLN   HG2  H N N 170 
GLN   HG3  H N N 171 
GLN   HE21 H N N 172 
GLN   HE22 H N N 173 
GLN   HXT  H N N 174 
GLU   N    N N N 175 
GLU   CA   C N S 176 
GLU   C    C N N 177 
GLU   O    O N N 178 
GLU   CB   C N N 179 
GLU   CG   C N N 180 
GLU   CD   C N N 181 
GLU   OE1  O N N 182 
GLU   OE2  O N N 183 
GLU   OXT  O N N 184 
GLU   H    H N N 185 
GLU   H2   H N N 186 
GLU   HA   H N N 187 
GLU   HB2  H N N 188 
GLU   HB3  H N N 189 
GLU   HG2  H N N 190 
GLU   HG3  H N N 191 
GLU   HE2  H N N 192 
GLU   HXT  H N N 193 
GLY   N    N N N 194 
GLY   CA   C N N 195 
GLY   C    C N N 196 
GLY   O    O N N 197 
GLY   OXT  O N N 198 
GLY   H    H N N 199 
GLY   H2   H N N 200 
GLY   HA2  H N N 201 
GLY   HA3  H N N 202 
GLY   HXT  H N N 203 
HIS   N    N N N 204 
HIS   CA   C N S 205 
HIS   C    C N N 206 
HIS   O    O N N 207 
HIS   CB   C N N 208 
HIS   CG   C Y N 209 
HIS   ND1  N Y N 210 
HIS   CD2  C Y N 211 
HIS   CE1  C Y N 212 
HIS   NE2  N Y N 213 
HIS   OXT  O N N 214 
HIS   H    H N N 215 
HIS   H2   H N N 216 
HIS   HA   H N N 217 
HIS   HB2  H N N 218 
HIS   HB3  H N N 219 
HIS   HD1  H N N 220 
HIS   HD2  H N N 221 
HIS   HE1  H N N 222 
HIS   HE2  H N N 223 
HIS   HXT  H N N 224 
HOH   O    O N N 225 
HOH   H1   H N N 226 
HOH   H2   H N N 227 
ILE   N    N N N 228 
ILE   CA   C N S 229 
ILE   C    C N N 230 
ILE   O    O N N 231 
ILE   CB   C N S 232 
ILE   CG1  C N N 233 
ILE   CG2  C N N 234 
ILE   CD1  C N N 235 
ILE   OXT  O N N 236 
ILE   H    H N N 237 
ILE   H2   H N N 238 
ILE   HA   H N N 239 
ILE   HB   H N N 240 
ILE   HG12 H N N 241 
ILE   HG13 H N N 242 
ILE   HG21 H N N 243 
ILE   HG22 H N N 244 
ILE   HG23 H N N 245 
ILE   HD11 H N N 246 
ILE   HD12 H N N 247 
ILE   HD13 H N N 248 
ILE   HXT  H N N 249 
LEU   N    N N N 250 
LEU   CA   C N S 251 
LEU   C    C N N 252 
LEU   O    O N N 253 
LEU   CB   C N N 254 
LEU   CG   C N N 255 
LEU   CD1  C N N 256 
LEU   CD2  C N N 257 
LEU   OXT  O N N 258 
LEU   H    H N N 259 
LEU   H2   H N N 260 
LEU   HA   H N N 261 
LEU   HB2  H N N 262 
LEU   HB3  H N N 263 
LEU   HG   H N N 264 
LEU   HD11 H N N 265 
LEU   HD12 H N N 266 
LEU   HD13 H N N 267 
LEU   HD21 H N N 268 
LEU   HD22 H N N 269 
LEU   HD23 H N N 270 
LEU   HXT  H N N 271 
LYS   N    N N N 272 
LYS   CA   C N S 273 
LYS   C    C N N 274 
LYS   O    O N N 275 
LYS   CB   C N N 276 
LYS   CG   C N N 277 
LYS   CD   C N N 278 
LYS   CE   C N N 279 
LYS   NZ   N N N 280 
LYS   OXT  O N N 281 
LYS   H    H N N 282 
LYS   H2   H N N 283 
LYS   HA   H N N 284 
LYS   HB2  H N N 285 
LYS   HB3  H N N 286 
LYS   HG2  H N N 287 
LYS   HG3  H N N 288 
LYS   HD2  H N N 289 
LYS   HD3  H N N 290 
LYS   HE2  H N N 291 
LYS   HE3  H N N 292 
LYS   HZ1  H N N 293 
LYS   HZ2  H N N 294 
LYS   HZ3  H N N 295 
LYS   HXT  H N N 296 
MET   N    N N N 297 
MET   CA   C N S 298 
MET   C    C N N 299 
MET   O    O N N 300 
MET   CB   C N N 301 
MET   CG   C N N 302 
MET   SD   S N N 303 
MET   CE   C N N 304 
MET   OXT  O N N 305 
MET   H    H N N 306 
MET   H2   H N N 307 
MET   HA   H N N 308 
MET   HB2  H N N 309 
MET   HB3  H N N 310 
MET   HG2  H N N 311 
MET   HG3  H N N 312 
MET   HE1  H N N 313 
MET   HE2  H N N 314 
MET   HE3  H N N 315 
MET   HXT  H N N 316 
PHE   N    N N N 317 
PHE   CA   C N S 318 
PHE   C    C N N 319 
PHE   O    O N N 320 
PHE   CB   C N N 321 
PHE   CG   C Y N 322 
PHE   CD1  C Y N 323 
PHE   CD2  C Y N 324 
PHE   CE1  C Y N 325 
PHE   CE2  C Y N 326 
PHE   CZ   C Y N 327 
PHE   OXT  O N N 328 
PHE   H    H N N 329 
PHE   H2   H N N 330 
PHE   HA   H N N 331 
PHE   HB2  H N N 332 
PHE   HB3  H N N 333 
PHE   HD1  H N N 334 
PHE   HD2  H N N 335 
PHE   HE1  H N N 336 
PHE   HE2  H N N 337 
PHE   HZ   H N N 338 
PHE   HXT  H N N 339 
PRO   N    N N N 340 
PRO   CA   C N S 341 
PRO   C    C N N 342 
PRO   O    O N N 343 
PRO   CB   C N N 344 
PRO   CG   C N N 345 
PRO   CD   C N N 346 
PRO   OXT  O N N 347 
PRO   H    H N N 348 
PRO   HA   H N N 349 
PRO   HB2  H N N 350 
PRO   HB3  H N N 351 
PRO   HG2  H N N 352 
PRO   HG3  H N N 353 
PRO   HD2  H N N 354 
PRO   HD3  H N N 355 
PRO   HXT  H N N 356 
SER   N    N N N 357 
SER   CA   C N S 358 
SER   C    C N N 359 
SER   O    O N N 360 
SER   CB   C N N 361 
SER   OG   O N N 362 
SER   OXT  O N N 363 
SER   H    H N N 364 
SER   H2   H N N 365 
SER   HA   H N N 366 
SER   HB2  H N N 367 
SER   HB3  H N N 368 
SER   HG   H N N 369 
SER   HXT  H N N 370 
THR   N    N N N 371 
THR   CA   C N S 372 
THR   C    C N N 373 
THR   O    O N N 374 
THR   CB   C N R 375 
THR   OG1  O N N 376 
THR   CG2  C N N 377 
THR   OXT  O N N 378 
THR   H    H N N 379 
THR   H2   H N N 380 
THR   HA   H N N 381 
THR   HB   H N N 382 
THR   HG1  H N N 383 
THR   HG21 H N N 384 
THR   HG22 H N N 385 
THR   HG23 H N N 386 
THR   HXT  H N N 387 
TRP   N    N N N 388 
TRP   CA   C N S 389 
TRP   C    C N N 390 
TRP   O    O N N 391 
TRP   CB   C N N 392 
TRP   CG   C Y N 393 
TRP   CD1  C Y N 394 
TRP   CD2  C Y N 395 
TRP   NE1  N Y N 396 
TRP   CE2  C Y N 397 
TRP   CE3  C Y N 398 
TRP   CZ2  C Y N 399 
TRP   CZ3  C Y N 400 
TRP   CH2  C Y N 401 
TRP   OXT  O N N 402 
TRP   H    H N N 403 
TRP   H2   H N N 404 
TRP   HA   H N N 405 
TRP   HB2  H N N 406 
TRP   HB3  H N N 407 
TRP   HD1  H N N 408 
TRP   HE1  H N N 409 
TRP   HE3  H N N 410 
TRP   HZ2  H N N 411 
TRP   HZ3  H N N 412 
TRP   HH2  H N N 413 
TRP   HXT  H N N 414 
TYR   N    N N N 415 
TYR   CA   C N S 416 
TYR   C    C N N 417 
TYR   O    O N N 418 
TYR   CB   C N N 419 
TYR   CG   C Y N 420 
TYR   CD1  C Y N 421 
TYR   CD2  C Y N 422 
TYR   CE1  C Y N 423 
TYR   CE2  C Y N 424 
TYR   CZ   C Y N 425 
TYR   OH   O N N 426 
TYR   OXT  O N N 427 
TYR   H    H N N 428 
TYR   H2   H N N 429 
TYR   HA   H N N 430 
TYR   HB2  H N N 431 
TYR   HB3  H N N 432 
TYR   HD1  H N N 433 
TYR   HD2  H N N 434 
TYR   HE1  H N N 435 
TYR   HE2  H N N 436 
TYR   HH   H N N 437 
TYR   HXT  H N N 438 
VAL   N    N N N 439 
VAL   CA   C N S 440 
VAL   C    C N N 441 
VAL   O    O N N 442 
VAL   CB   C N N 443 
VAL   CG1  C N N 444 
VAL   CG2  C N N 445 
VAL   OXT  O N N 446 
VAL   H    H N N 447 
VAL   H2   H N N 448 
VAL   HA   H N N 449 
VAL   HB   H N N 450 
VAL   HG11 H N N 451 
VAL   HG12 H N N 452 
VAL   HG13 H N N 453 
VAL   HG21 H N N 454 
VAL   HG22 H N N 455 
VAL   HG23 H N N 456 
VAL   HXT  H N N 457 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1AFE C22 C23  doub Y N 1   
A1AFE C22 C21  sing Y N 2   
A1AFE C23 C24  sing Y N 3   
A1AFE C21 C20  doub Y N 4   
A1AFE C24 C25  doub Y N 5   
A1AFE O19 S17  doub N N 6   
A1AFE C20 C25  sing Y N 7   
A1AFE C20 S17  sing N N 8   
A1AFE C25 C09  sing N N 9   
A1AFE C12 C11  doub Y N 10  
A1AFE C12 C13  sing Y N 11  
A1AFE C11 C10  sing Y N 12  
A1AFE C13 C14  doub Y N 13  
A1AFE S17 O18  doub N N 14  
A1AFE S17 C16  sing N N 15  
A1AFE C10 C09  sing N N 16  
A1AFE C10 C15  doub Y N 17  
A1AFE C14 C15  sing Y N 18  
A1AFE C09 C06  doub N N 19  
A1AFE C15 C16  sing N N 20  
A1AFE C06 C07  sing N N 21  
A1AFE C06 C05  sing N N 22  
A1AFE C07 C08  sing N N 23  
A1AFE C05 C04  sing N N 24  
A1AFE C08 N03  sing N N 25  
A1AFE C04 N03  sing N N 26  
A1AFE N03 C02  sing N N 27  
A1AFE C34 N33  doub Y N 28  
A1AFE C34 C26  sing Y N 29  
A1AFE C02 C26  sing N N 30  
A1AFE C02 O01  doub N N 31  
A1AFE N33 C32  sing Y N 32  
A1AFE C26 C27  doub Y N 33  
A1AFE C32 C31  doub Y N 34  
A1AFE C27 C31  sing Y N 35  
A1AFE C27 N28  sing Y N 36  
A1AFE C31 C30  sing Y N 37  
A1AFE N28 C29  sing Y N 38  
A1AFE C30 C29  doub Y N 39  
A1AFE C04 H1   sing N N 40  
A1AFE C04 H2   sing N N 41  
A1AFE C05 H3   sing N N 42  
A1AFE C05 H4   sing N N 43  
A1AFE C07 H5   sing N N 44  
A1AFE C07 H6   sing N N 45  
A1AFE C08 H7   sing N N 46  
A1AFE C08 H8   sing N N 47  
A1AFE C11 H9   sing N N 48  
A1AFE C12 H10  sing N N 49  
A1AFE C13 H11  sing N N 50  
A1AFE C14 H12  sing N N 51  
A1AFE C16 H13  sing N N 52  
A1AFE C16 H14  sing N N 53  
A1AFE C21 H15  sing N N 54  
A1AFE C22 H16  sing N N 55  
A1AFE C23 H17  sing N N 56  
A1AFE C24 H18  sing N N 57  
A1AFE C29 H19  sing N N 58  
A1AFE C30 H20  sing N N 59  
A1AFE C32 H21  sing N N 60  
A1AFE C34 H22  sing N N 61  
A1AFE N28 H23  sing N N 62  
ALA   N   CA   sing N N 63  
ALA   N   H    sing N N 64  
ALA   N   H2   sing N N 65  
ALA   CA  C    sing N N 66  
ALA   CA  CB   sing N N 67  
ALA   CA  HA   sing N N 68  
ALA   C   O    doub N N 69  
ALA   C   OXT  sing N N 70  
ALA   CB  HB1  sing N N 71  
ALA   CB  HB2  sing N N 72  
ALA   CB  HB3  sing N N 73  
ALA   OXT HXT  sing N N 74  
ARG   N   CA   sing N N 75  
ARG   N   H    sing N N 76  
ARG   N   H2   sing N N 77  
ARG   CA  C    sing N N 78  
ARG   CA  CB   sing N N 79  
ARG   CA  HA   sing N N 80  
ARG   C   O    doub N N 81  
ARG   C   OXT  sing N N 82  
ARG   CB  CG   sing N N 83  
ARG   CB  HB2  sing N N 84  
ARG   CB  HB3  sing N N 85  
ARG   CG  CD   sing N N 86  
ARG   CG  HG2  sing N N 87  
ARG   CG  HG3  sing N N 88  
ARG   CD  NE   sing N N 89  
ARG   CD  HD2  sing N N 90  
ARG   CD  HD3  sing N N 91  
ARG   NE  CZ   sing N N 92  
ARG   NE  HE   sing N N 93  
ARG   CZ  NH1  sing N N 94  
ARG   CZ  NH2  doub N N 95  
ARG   NH1 HH11 sing N N 96  
ARG   NH1 HH12 sing N N 97  
ARG   NH2 HH21 sing N N 98  
ARG   NH2 HH22 sing N N 99  
ARG   OXT HXT  sing N N 100 
ASN   N   CA   sing N N 101 
ASN   N   H    sing N N 102 
ASN   N   H2   sing N N 103 
ASN   CA  C    sing N N 104 
ASN   CA  CB   sing N N 105 
ASN   CA  HA   sing N N 106 
ASN   C   O    doub N N 107 
ASN   C   OXT  sing N N 108 
ASN   CB  CG   sing N N 109 
ASN   CB  HB2  sing N N 110 
ASN   CB  HB3  sing N N 111 
ASN   CG  OD1  doub N N 112 
ASN   CG  ND2  sing N N 113 
ASN   ND2 HD21 sing N N 114 
ASN   ND2 HD22 sing N N 115 
ASN   OXT HXT  sing N N 116 
ASP   N   CA   sing N N 117 
ASP   N   H    sing N N 118 
ASP   N   H2   sing N N 119 
ASP   CA  C    sing N N 120 
ASP   CA  CB   sing N N 121 
ASP   CA  HA   sing N N 122 
ASP   C   O    doub N N 123 
ASP   C   OXT  sing N N 124 
ASP   CB  CG   sing N N 125 
ASP   CB  HB2  sing N N 126 
ASP   CB  HB3  sing N N 127 
ASP   CG  OD1  doub N N 128 
ASP   CG  OD2  sing N N 129 
ASP   OD2 HD2  sing N N 130 
ASP   OXT HXT  sing N N 131 
CYS   N   CA   sing N N 132 
CYS   N   H    sing N N 133 
CYS   N   H2   sing N N 134 
CYS   CA  C    sing N N 135 
CYS   CA  CB   sing N N 136 
CYS   CA  HA   sing N N 137 
CYS   C   O    doub N N 138 
CYS   C   OXT  sing N N 139 
CYS   CB  SG   sing N N 140 
CYS   CB  HB2  sing N N 141 
CYS   CB  HB3  sing N N 142 
CYS   SG  HG   sing N N 143 
CYS   OXT HXT  sing N N 144 
DMS   S   O    doub N N 145 
DMS   S   C1   sing N N 146 
DMS   S   C2   sing N N 147 
DMS   C1  H11  sing N N 148 
DMS   C1  H12  sing N N 149 
DMS   C1  H13  sing N N 150 
DMS   C2  H21  sing N N 151 
DMS   C2  H22  sing N N 152 
DMS   C2  H23  sing N N 153 
GLN   N   CA   sing N N 154 
GLN   N   H    sing N N 155 
GLN   N   H2   sing N N 156 
GLN   CA  C    sing N N 157 
GLN   CA  CB   sing N N 158 
GLN   CA  HA   sing N N 159 
GLN   C   O    doub N N 160 
GLN   C   OXT  sing N N 161 
GLN   CB  CG   sing N N 162 
GLN   CB  HB2  sing N N 163 
GLN   CB  HB3  sing N N 164 
GLN   CG  CD   sing N N 165 
GLN   CG  HG2  sing N N 166 
GLN   CG  HG3  sing N N 167 
GLN   CD  OE1  doub N N 168 
GLN   CD  NE2  sing N N 169 
GLN   NE2 HE21 sing N N 170 
GLN   NE2 HE22 sing N N 171 
GLN   OXT HXT  sing N N 172 
GLU   N   CA   sing N N 173 
GLU   N   H    sing N N 174 
GLU   N   H2   sing N N 175 
GLU   CA  C    sing N N 176 
GLU   CA  CB   sing N N 177 
GLU   CA  HA   sing N N 178 
GLU   C   O    doub N N 179 
GLU   C   OXT  sing N N 180 
GLU   CB  CG   sing N N 181 
GLU   CB  HB2  sing N N 182 
GLU   CB  HB3  sing N N 183 
GLU   CG  CD   sing N N 184 
GLU   CG  HG2  sing N N 185 
GLU   CG  HG3  sing N N 186 
GLU   CD  OE1  doub N N 187 
GLU   CD  OE2  sing N N 188 
GLU   OE2 HE2  sing N N 189 
GLU   OXT HXT  sing N N 190 
GLY   N   CA   sing N N 191 
GLY   N   H    sing N N 192 
GLY   N   H2   sing N N 193 
GLY   CA  C    sing N N 194 
GLY   CA  HA2  sing N N 195 
GLY   CA  HA3  sing N N 196 
GLY   C   O    doub N N 197 
GLY   C   OXT  sing N N 198 
GLY   OXT HXT  sing N N 199 
HIS   N   CA   sing N N 200 
HIS   N   H    sing N N 201 
HIS   N   H2   sing N N 202 
HIS   CA  C    sing N N 203 
HIS   CA  CB   sing N N 204 
HIS   CA  HA   sing N N 205 
HIS   C   O    doub N N 206 
HIS   C   OXT  sing N N 207 
HIS   CB  CG   sing N N 208 
HIS   CB  HB2  sing N N 209 
HIS   CB  HB3  sing N N 210 
HIS   CG  ND1  sing Y N 211 
HIS   CG  CD2  doub Y N 212 
HIS   ND1 CE1  doub Y N 213 
HIS   ND1 HD1  sing N N 214 
HIS   CD2 NE2  sing Y N 215 
HIS   CD2 HD2  sing N N 216 
HIS   CE1 NE2  sing Y N 217 
HIS   CE1 HE1  sing N N 218 
HIS   NE2 HE2  sing N N 219 
HIS   OXT HXT  sing N N 220 
HOH   O   H1   sing N N 221 
HOH   O   H2   sing N N 222 
ILE   N   CA   sing N N 223 
ILE   N   H    sing N N 224 
ILE   N   H2   sing N N 225 
ILE   CA  C    sing N N 226 
ILE   CA  CB   sing N N 227 
ILE   CA  HA   sing N N 228 
ILE   C   O    doub N N 229 
ILE   C   OXT  sing N N 230 
ILE   CB  CG1  sing N N 231 
ILE   CB  CG2  sing N N 232 
ILE   CB  HB   sing N N 233 
ILE   CG1 CD1  sing N N 234 
ILE   CG1 HG12 sing N N 235 
ILE   CG1 HG13 sing N N 236 
ILE   CG2 HG21 sing N N 237 
ILE   CG2 HG22 sing N N 238 
ILE   CG2 HG23 sing N N 239 
ILE   CD1 HD11 sing N N 240 
ILE   CD1 HD12 sing N N 241 
ILE   CD1 HD13 sing N N 242 
ILE   OXT HXT  sing N N 243 
LEU   N   CA   sing N N 244 
LEU   N   H    sing N N 245 
LEU   N   H2   sing N N 246 
LEU   CA  C    sing N N 247 
LEU   CA  CB   sing N N 248 
LEU   CA  HA   sing N N 249 
LEU   C   O    doub N N 250 
LEU   C   OXT  sing N N 251 
LEU   CB  CG   sing N N 252 
LEU   CB  HB2  sing N N 253 
LEU   CB  HB3  sing N N 254 
LEU   CG  CD1  sing N N 255 
LEU   CG  CD2  sing N N 256 
LEU   CG  HG   sing N N 257 
LEU   CD1 HD11 sing N N 258 
LEU   CD1 HD12 sing N N 259 
LEU   CD1 HD13 sing N N 260 
LEU   CD2 HD21 sing N N 261 
LEU   CD2 HD22 sing N N 262 
LEU   CD2 HD23 sing N N 263 
LEU   OXT HXT  sing N N 264 
LYS   N   CA   sing N N 265 
LYS   N   H    sing N N 266 
LYS   N   H2   sing N N 267 
LYS   CA  C    sing N N 268 
LYS   CA  CB   sing N N 269 
LYS   CA  HA   sing N N 270 
LYS   C   O    doub N N 271 
LYS   C   OXT  sing N N 272 
LYS   CB  CG   sing N N 273 
LYS   CB  HB2  sing N N 274 
LYS   CB  HB3  sing N N 275 
LYS   CG  CD   sing N N 276 
LYS   CG  HG2  sing N N 277 
LYS   CG  HG3  sing N N 278 
LYS   CD  CE   sing N N 279 
LYS   CD  HD2  sing N N 280 
LYS   CD  HD3  sing N N 281 
LYS   CE  NZ   sing N N 282 
LYS   CE  HE2  sing N N 283 
LYS   CE  HE3  sing N N 284 
LYS   NZ  HZ1  sing N N 285 
LYS   NZ  HZ2  sing N N 286 
LYS   NZ  HZ3  sing N N 287 
LYS   OXT HXT  sing N N 288 
MET   N   CA   sing N N 289 
MET   N   H    sing N N 290 
MET   N   H2   sing N N 291 
MET   CA  C    sing N N 292 
MET   CA  CB   sing N N 293 
MET   CA  HA   sing N N 294 
MET   C   O    doub N N 295 
MET   C   OXT  sing N N 296 
MET   CB  CG   sing N N 297 
MET   CB  HB2  sing N N 298 
MET   CB  HB3  sing N N 299 
MET   CG  SD   sing N N 300 
MET   CG  HG2  sing N N 301 
MET   CG  HG3  sing N N 302 
MET   SD  CE   sing N N 303 
MET   CE  HE1  sing N N 304 
MET   CE  HE2  sing N N 305 
MET   CE  HE3  sing N N 306 
MET   OXT HXT  sing N N 307 
PHE   N   CA   sing N N 308 
PHE   N   H    sing N N 309 
PHE   N   H2   sing N N 310 
PHE   CA  C    sing N N 311 
PHE   CA  CB   sing N N 312 
PHE   CA  HA   sing N N 313 
PHE   C   O    doub N N 314 
PHE   C   OXT  sing N N 315 
PHE   CB  CG   sing N N 316 
PHE   CB  HB2  sing N N 317 
PHE   CB  HB3  sing N N 318 
PHE   CG  CD1  doub Y N 319 
PHE   CG  CD2  sing Y N 320 
PHE   CD1 CE1  sing Y N 321 
PHE   CD1 HD1  sing N N 322 
PHE   CD2 CE2  doub Y N 323 
PHE   CD2 HD2  sing N N 324 
PHE   CE1 CZ   doub Y N 325 
PHE   CE1 HE1  sing N N 326 
PHE   CE2 CZ   sing Y N 327 
PHE   CE2 HE2  sing N N 328 
PHE   CZ  HZ   sing N N 329 
PHE   OXT HXT  sing N N 330 
PRO   N   CA   sing N N 331 
PRO   N   CD   sing N N 332 
PRO   N   H    sing N N 333 
PRO   CA  C    sing N N 334 
PRO   CA  CB   sing N N 335 
PRO   CA  HA   sing N N 336 
PRO   C   O    doub N N 337 
PRO   C   OXT  sing N N 338 
PRO   CB  CG   sing N N 339 
PRO   CB  HB2  sing N N 340 
PRO   CB  HB3  sing N N 341 
PRO   CG  CD   sing N N 342 
PRO   CG  HG2  sing N N 343 
PRO   CG  HG3  sing N N 344 
PRO   CD  HD2  sing N N 345 
PRO   CD  HD3  sing N N 346 
PRO   OXT HXT  sing N N 347 
SER   N   CA   sing N N 348 
SER   N   H    sing N N 349 
SER   N   H2   sing N N 350 
SER   CA  C    sing N N 351 
SER   CA  CB   sing N N 352 
SER   CA  HA   sing N N 353 
SER   C   O    doub N N 354 
SER   C   OXT  sing N N 355 
SER   CB  OG   sing N N 356 
SER   CB  HB2  sing N N 357 
SER   CB  HB3  sing N N 358 
SER   OG  HG   sing N N 359 
SER   OXT HXT  sing N N 360 
THR   N   CA   sing N N 361 
THR   N   H    sing N N 362 
THR   N   H2   sing N N 363 
THR   CA  C    sing N N 364 
THR   CA  CB   sing N N 365 
THR   CA  HA   sing N N 366 
THR   C   O    doub N N 367 
THR   C   OXT  sing N N 368 
THR   CB  OG1  sing N N 369 
THR   CB  CG2  sing N N 370 
THR   CB  HB   sing N N 371 
THR   OG1 HG1  sing N N 372 
THR   CG2 HG21 sing N N 373 
THR   CG2 HG22 sing N N 374 
THR   CG2 HG23 sing N N 375 
THR   OXT HXT  sing N N 376 
TRP   N   CA   sing N N 377 
TRP   N   H    sing N N 378 
TRP   N   H2   sing N N 379 
TRP   CA  C    sing N N 380 
TRP   CA  CB   sing N N 381 
TRP   CA  HA   sing N N 382 
TRP   C   O    doub N N 383 
TRP   C   OXT  sing N N 384 
TRP   CB  CG   sing N N 385 
TRP   CB  HB2  sing N N 386 
TRP   CB  HB3  sing N N 387 
TRP   CG  CD1  doub Y N 388 
TRP   CG  CD2  sing Y N 389 
TRP   CD1 NE1  sing Y N 390 
TRP   CD1 HD1  sing N N 391 
TRP   CD2 CE2  doub Y N 392 
TRP   CD2 CE3  sing Y N 393 
TRP   NE1 CE2  sing Y N 394 
TRP   NE1 HE1  sing N N 395 
TRP   CE2 CZ2  sing Y N 396 
TRP   CE3 CZ3  doub Y N 397 
TRP   CE3 HE3  sing N N 398 
TRP   CZ2 CH2  doub Y N 399 
TRP   CZ2 HZ2  sing N N 400 
TRP   CZ3 CH2  sing Y N 401 
TRP   CZ3 HZ3  sing N N 402 
TRP   CH2 HH2  sing N N 403 
TRP   OXT HXT  sing N N 404 
TYR   N   CA   sing N N 405 
TYR   N   H    sing N N 406 
TYR   N   H2   sing N N 407 
TYR   CA  C    sing N N 408 
TYR   CA  CB   sing N N 409 
TYR   CA  HA   sing N N 410 
TYR   C   O    doub N N 411 
TYR   C   OXT  sing N N 412 
TYR   CB  CG   sing N N 413 
TYR   CB  HB2  sing N N 414 
TYR   CB  HB3  sing N N 415 
TYR   CG  CD1  doub Y N 416 
TYR   CG  CD2  sing Y N 417 
TYR   CD1 CE1  sing Y N 418 
TYR   CD1 HD1  sing N N 419 
TYR   CD2 CE2  doub Y N 420 
TYR   CD2 HD2  sing N N 421 
TYR   CE1 CZ   doub Y N 422 
TYR   CE1 HE1  sing N N 423 
TYR   CE2 CZ   sing Y N 424 
TYR   CE2 HE2  sing N N 425 
TYR   CZ  OH   sing N N 426 
TYR   OH  HH   sing N N 427 
TYR   OXT HXT  sing N N 428 
VAL   N   CA   sing N N 429 
VAL   N   H    sing N N 430 
VAL   N   H2   sing N N 431 
VAL   CA  C    sing N N 432 
VAL   CA  CB   sing N N 433 
VAL   CA  HA   sing N N 434 
VAL   C   O    doub N N 435 
VAL   C   OXT  sing N N 436 
VAL   CB  CG1  sing N N 437 
VAL   CB  CG2  sing N N 438 
VAL   CB  HB   sing N N 439 
VAL   CG1 HG11 sing N N 440 
VAL   CG1 HG12 sing N N 441 
VAL   CG1 HG13 sing N N 442 
VAL   CG2 HG21 sing N N 443 
VAL   CG2 HG22 sing N N 444 
VAL   CG2 HG23 sing N N 445 
VAL   OXT HXT  sing N N 446 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6LU7 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8W1U 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.021760 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004439 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018496 
_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]   0.009042 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER   A 1 1   ? 33.223  -4.446  33.413 1.00 38.67  ? 1   SER   A N   1 
ATOM   2    C CA  . SER   A 1 1   ? 32.782  -5.464  32.469 1.00 41.66  ? 1   SER   A CA  1 
ATOM   3    C C   . SER   A 1 1   ? 31.269  -5.663  32.557 1.00 49.33  ? 1   SER   A C   1 
ATOM   4    O O   . SER   A 1 1   ? 30.566  -4.850  33.160 1.00 41.56  ? 1   SER   A O   1 
ATOM   5    C CB  . SER   A 1 1   ? 33.519  -6.784  32.717 1.00 49.75  ? 1   SER   A CB  1 
ATOM   6    O OG  . SER   A 1 1   ? 33.355  -7.234  34.048 1.00 55.00  ? 1   SER   A OG  1 
ATOM   7    N N   . GLY   A 1 2   ? 30.773  -6.736  31.951 1.00 39.04  ? 2   GLY   A N   1 
ATOM   8    C CA  . GLY   A 1 2   ? 29.350  -6.968  31.838 1.00 41.48  ? 2   GLY   A CA  1 
ATOM   9    C C   . GLY   A 1 2   ? 28.819  -6.559  30.473 1.00 37.94  ? 2   GLY   A C   1 
ATOM   10   O O   . GLY   A 1 2   ? 29.379  -5.707  29.779 1.00 46.40  ? 2   GLY   A O   1 
ATOM   11   N N   . PHE   A 1 3   ? 27.713  -7.183  30.074 1.00 38.11  ? 3   PHE   A N   1 
ATOM   12   C CA  . PHE   A 1 3   ? 27.154  -6.921  28.753 1.00 36.47  ? 3   PHE   A CA  1 
ATOM   13   C C   . PHE   A 1 3   ? 25.642  -6.852  28.848 1.00 38.03  ? 3   PHE   A C   1 
ATOM   14   O O   . PHE   A 1 3   ? 24.997  -7.820  29.261 1.00 46.42  ? 3   PHE   A O   1 
ATOM   15   C CB  . PHE   A 1 3   ? 27.589  -7.986  27.742 1.00 42.66  ? 3   PHE   A CB  1 
ATOM   16   C CG  . PHE   A 1 3   ? 27.599  -7.496  26.320 1.00 44.72  ? 3   PHE   A CG  1 
ATOM   17   C CD1 . PHE   A 1 3   ? 28.576  -6.613  25.883 1.00 43.43  ? 3   PHE   A CD1 1 
ATOM   18   C CD2 . PHE   A 1 3   ? 26.633  -7.916  25.423 1.00 43.79  ? 3   PHE   A CD2 1 
ATOM   19   C CE1 . PHE   A 1 3   ? 28.588  -6.159  24.577 1.00 40.82  ? 3   PHE   A CE1 1 
ATOM   20   C CE2 . PHE   A 1 3   ? 26.641  -7.467  24.118 1.00 43.02  ? 3   PHE   A CE2 1 
ATOM   21   C CZ  . PHE   A 1 3   ? 27.619  -6.585  23.696 1.00 43.26  ? 3   PHE   A CZ  1 
ATOM   22   N N   . ARG   A 1 4   ? 25.086  -5.713  28.449 1.00 36.31  ? 4   ARG   A N   1 
ATOM   23   C CA  . ARG   A 1 4   ? 23.665  -5.446  28.568 1.00 40.12  ? 4   ARG   A CA  1 
ATOM   24   C C   . ARG   A 1 4   ? 23.136  -4.876  27.263 1.00 43.31  ? 4   ARG   A C   1 
ATOM   25   O O   . ARG   A 1 4   ? 23.868  -4.236  26.502 1.00 43.70  ? 4   ARG   A O   1 
ATOM   26   C CB  . ARG   A 1 4   ? 23.379  -4.458  29.709 1.00 38.84  ? 4   ARG   A CB  1 
ATOM   27   C CG  . ARG   A 1 4   ? 23.871  -4.923  31.070 1.00 41.98  ? 4   ARG   A CG  1 
ATOM   28   C CD  . ARG   A 1 4   ? 23.100  -6.140  31.534 1.00 46.96  ? 4   ARG   A CD  1 
ATOM   29   N NE  . ARG   A 1 4   ? 21.672  -5.949  31.318 1.00 54.90  ? 4   ARG   A NE  1 
ATOM   30   C CZ  . ARG   A 1 4   ? 20.863  -5.336  32.170 1.00 55.17  ? 4   ARG   A CZ  1 
ATOM   31   N NH1 . ARG   A 1 4   ? 21.299  -4.887  33.336 1.00 54.15  ? 4   ARG   A NH1 1 
ATOM   32   N NH2 . ARG   A 1 4   ? 19.585  -5.163  31.841 1.00 56.71  ? 4   ARG   A NH2 1 
ATOM   33   N N   . LYS   A 1 5   ? 21.851  -5.111  27.011 1.00 42.04  ? 5   LYS   A N   1 
ATOM   34   C CA  . LYS   A 1 5   ? 21.157  -4.419  25.929 1.00 48.35  ? 5   LYS   A CA  1 
ATOM   35   C C   . LYS   A 1 5   ? 21.014  -2.958  26.335 1.00 43.69  ? 5   LYS   A C   1 
ATOM   36   O O   . LYS   A 1 5   ? 20.203  -2.612  27.195 1.00 45.25  ? 5   LYS   A O   1 
ATOM   37   C CB  . LYS   A 1 5   ? 19.808  -5.071  25.648 1.00 45.68  ? 5   LYS   A CB  1 
ATOM   38   C CG  . LYS   A 1 5   ? 19.637  -5.467  24.190 1.00 49.08  ? 5   LYS   A CG  1 
ATOM   39   C CD  . LYS   A 1 5   ? 18.328  -6.193  23.939 1.00 57.89  ? 5   LYS   A CD  1 
ATOM   40   C CE  . LYS   A 1 5   ? 18.311  -7.564  24.591 1.00 63.92  ? 5   LYS   A CE  1 
ATOM   41   N NZ  . LYS   A 1 5   ? 17.122  -8.346  24.158 1.00 59.75  ? 5   LYS   A NZ  1 
ATOM   42   N N   . MET   A 1 6   ? 21.817  -2.096  25.717 1.00 39.29  ? 6   MET   A N   1 
ATOM   43   C CA  . MET   A 1 6   ? 22.014  -0.723  26.166 1.00 46.05  ? 6   MET   A CA  1 
ATOM   44   C C   . MET   A 1 6   ? 21.537  0.230   25.082 1.00 48.28  ? 6   MET   A C   1 
ATOM   45   O O   . MET   A 1 6   ? 22.019  0.166   23.946 1.00 45.41  ? 6   MET   A O   1 
ATOM   46   C CB  . MET   A 1 6   ? 23.490  -0.480  26.488 1.00 38.05  ? 6   MET   A CB  1 
ATOM   47   C CG  . MET   A 1 6   ? 23.789  0.812   27.215 1.00 48.23  ? 6   MET   A CG  1 
ATOM   48   S SD  . MET   A 1 6   ? 25.554  0.949   27.562 1.00 62.87  ? 6   MET   A SD  1 
ATOM   49   C CE  . MET   A 1 6   ? 25.852  -0.619  28.368 1.00 43.53  ? 6   MET   A CE  1 
ATOM   50   N N   . ALA   A 1 7   ? 20.605  1.113   25.434 1.00 36.14  ? 7   ALA   A N   1 
ATOM   51   C CA  . ALA   A 1 7   ? 20.105  2.125   24.515 1.00 40.67  ? 7   ALA   A CA  1 
ATOM   52   C C   . ALA   A 1 7   ? 20.930  3.406   24.619 1.00 39.57  ? 7   ALA   A C   1 
ATOM   53   O O   . ALA   A 1 7   ? 21.635  3.638   25.601 1.00 43.61  ? 7   ALA   A O   1 
ATOM   54   C CB  . ALA   A 1 7   ? 18.635  2.432   24.802 1.00 38.72  ? 7   ALA   A CB  1 
ATOM   55   N N   . PHE   A 1 8   ? 20.828  4.241   23.585 1.00 37.85  ? 8   PHE   A N   1 
ATOM   56   C CA  . PHE   A 1 8   ? 21.429  5.565   23.640 1.00 35.35  ? 8   PHE   A CA  1 
ATOM   57   C C   . PHE   A 1 8   ? 20.665  6.449   24.621 1.00 36.82  ? 8   PHE   A C   1 
ATOM   58   O O   . PHE   A 1 8   ? 19.461  6.268   24.822 1.00 40.41  ? 8   PHE   A O   1 
ATOM   59   C CB  . PHE   A 1 8   ? 21.421  6.225   22.265 1.00 38.75  ? 8   PHE   A CB  1 
ATOM   60   C CG  . PHE   A 1 8   ? 22.389  5.626   21.306 1.00 39.91  ? 8   PHE   A CG  1 
ATOM   61   C CD1 . PHE   A 1 8   ? 23.736  5.924   21.391 1.00 44.24  ? 8   PHE   A CD1 1 
ATOM   62   C CD2 . PHE   A 1 8   ? 21.956  4.764   20.318 1.00 36.90  ? 8   PHE   A CD2 1 
ATOM   63   C CE1 . PHE   A 1 8   ? 24.635  5.374   20.507 1.00 50.05  ? 8   PHE   A CE1 1 
ATOM   64   C CE2 . PHE   A 1 8   ? 22.849  4.207   19.432 1.00 44.30  ? 8   PHE   A CE2 1 
ATOM   65   C CZ  . PHE   A 1 8   ? 24.193  4.513   19.524 1.00 41.10  ? 8   PHE   A CZ  1 
ATOM   66   N N   . PRO   A 1 9   ? 21.338  7.418   25.239 1.00 35.67  ? 9   PRO   A N   1 
ATOM   67   C CA  . PRO   A 1 9   ? 20.618  8.382   26.077 1.00 40.49  ? 9   PRO   A CA  1 
ATOM   68   C C   . PRO   A 1 9   ? 19.581  9.124   25.245 1.00 40.10  ? 9   PRO   A C   1 
ATOM   69   O O   . PRO   A 1 9   ? 19.852  9.554   24.123 1.00 41.71  ? 9   PRO   A O   1 
ATOM   70   C CB  . PRO   A 1 9   ? 21.726  9.313   26.583 1.00 40.19  ? 9   PRO   A CB  1 
ATOM   71   C CG  . PRO   A 1 9   ? 22.995  8.531   26.414 1.00 46.88  ? 9   PRO   A CG  1 
ATOM   72   C CD  . PRO   A 1 9   ? 22.779  7.711   25.180 1.00 34.33  ? 9   PRO   A CD  1 
ATOM   73   N N   . SER   A 1 10  ? 18.379  9.255   25.799 1.00 43.08  ? 10  SER   A N   1 
ATOM   74   C CA  . SER   A 1 10  ? 17.224  9.712   25.041 1.00 44.39  ? 10  SER   A CA  1 
ATOM   75   C C   . SER   A 1 10  ? 16.936  11.197  25.214 1.00 43.35  ? 10  SER   A C   1 
ATOM   76   O O   . SER   A 1 10  ? 15.919  11.675  24.702 1.00 39.40  ? 10  SER   A O   1 
ATOM   77   C CB  . SER   A 1 10  ? 15.990  8.901   25.434 1.00 39.18  ? 10  SER   A CB  1 
ATOM   78   O OG  . SER   A 1 10  ? 15.589  9.202   26.759 1.00 42.34  ? 10  SER   A OG  1 
ATOM   79   N N   . GLY   A 1 11  ? 17.807  11.935  25.902 1.00 41.59  ? 11  GLY   A N   1 
ATOM   80   C CA  . GLY   A 1 11  ? 17.493  13.319  26.231 1.00 44.77  ? 11  GLY   A CA  1 
ATOM   81   C C   . GLY   A 1 11  ? 17.243  14.183  25.010 1.00 46.57  ? 11  GLY   A C   1 
ATOM   82   O O   . GLY   A 1 11  ? 16.257  14.925  24.948 1.00 43.82  ? 11  GLY   A O   1 
ATOM   83   N N   . LYS   A 1 12  ? 18.137  14.104  24.024 1.00 41.00  ? 12  LYS   A N   1 
ATOM   84   C CA  . LYS   A 1 12  ? 18.008  14.947  22.845 1.00 46.01  ? 12  LYS   A CA  1 
ATOM   85   C C   . LYS   A 1 12  ? 16.763  14.610  22.032 1.00 48.60  ? 12  LYS   A C   1 
ATOM   86   O O   . LYS   A 1 12  ? 16.270  15.466  21.290 1.00 47.87  ? 12  LYS   A O   1 
ATOM   87   C CB  . LYS   A 1 12  ? 19.271  14.828  21.987 1.00 48.29  ? 12  LYS   A CB  1 
ATOM   88   C CG  . LYS   A 1 12  ? 20.539  15.230  22.729 1.00 56.62  ? 12  LYS   A CG  1 
ATOM   89   C CD  . LYS   A 1 12  ? 21.545  15.891  21.802 1.00 59.75  ? 12  LYS   A CD  1 
ATOM   90   C CE  . LYS   A 1 12  ? 22.059  14.914  20.764 1.00 57.64  ? 12  LYS   A CE  1 
ATOM   91   N NZ  . LYS   A 1 12  ? 22.985  15.584  19.808 1.00 67.12  ? 12  LYS   A NZ  1 
ATOM   92   N N   . VAL   A 1 13  ? 16.238  13.394  22.164 1.00 47.29  ? 13  VAL   A N   1 
ATOM   93   C CA  . VAL   A 1 13  ? 15.029  13.021  21.441 1.00 44.08  ? 13  VAL   A CA  1 
ATOM   94   C C   . VAL   A 1 13  ? 13.775  13.372  22.235 1.00 39.03  ? 13  VAL   A C   1 
ATOM   95   O O   . VAL   A 1 13  ? 12.753  13.733  21.643 1.00 41.59  ? 13  VAL   A O   1 
ATOM   96   C CB  . VAL   A 1 13  ? 15.056  11.524  21.084 1.00 37.70  ? 13  VAL   A CB  1 
ATOM   97   C CG1 . VAL   A 1 13  ? 13.824  11.149  20.267 1.00 41.49  ? 13  VAL   A CG1 1 
ATOM   98   C CG2 . VAL   A 1 13  ? 16.328  11.182  20.328 1.00 35.16  ? 13  VAL   A CG2 1 
ATOM   99   N N   . GLU   A 1 14  ? 13.833  13.279  23.568 1.00 45.54  ? 14  GLU   A N   1 
ATOM   100  C CA  . GLU   A 1 14  ? 12.684  13.650  24.387 1.00 44.28  ? 14  GLU   A CA  1 
ATOM   101  C C   . GLU   A 1 14  ? 12.210  15.059  24.058 1.00 47.63  ? 14  GLU   A C   1 
ATOM   102  O O   . GLU   A 1 14  ? 11.003  15.316  23.995 1.00 44.41  ? 14  GLU   A O   1 
ATOM   103  C CB  . GLU   A 1 14  ? 13.032  13.535  25.871 1.00 40.86  ? 14  GLU   A CB  1 
ATOM   104  C CG  . GLU   A 1 14  ? 13.318  12.116  26.333 1.00 42.31  ? 14  GLU   A CG  1 
ATOM   105  C CD  . GLU   A 1 14  ? 13.995  12.063  27.690 1.00 47.66  ? 14  GLU   A CD  1 
ATOM   106  O OE1 . GLU   A 1 14  ? 13.449  12.639  28.655 1.00 45.22  ? 14  GLU   A OE1 1 
ATOM   107  O OE2 . GLU   A 1 14  ? 15.081  11.451  27.788 1.00 43.04  ? 14  GLU   A OE2 1 
ATOM   108  N N   . GLY   A 1 15  ? 13.146  15.976  23.809 1.00 46.53  ? 15  GLY   A N   1 
ATOM   109  C CA  . GLY   A 1 15  ? 12.814  17.351  23.491 1.00 48.24  ? 15  GLY   A CA  1 
ATOM   110  C C   . GLY   A 1 15  ? 12.199  17.567  22.128 1.00 54.74  ? 15  GLY   A C   1 
ATOM   111  O O   . GLY   A 1 15  ? 11.940  18.715  21.759 1.00 53.60  ? 15  GLY   A O   1 
ATOM   112  N N   . CYS   A 1 16  ? 11.960  16.501  21.366 1.00 46.73  ? 16  CYS   A N   1 
ATOM   113  C CA  . CYS   A 1 16  ? 11.354  16.607  20.050 1.00 42.00  ? 16  CYS   A CA  1 
ATOM   114  C C   . CYS   A 1 16  ? 10.016  15.889  19.960 1.00 34.31  ? 16  CYS   A C   1 
ATOM   115  O O   . CYS   A 1 16  ? 9.377   15.931  18.904 1.00 44.83  ? 16  CYS   A O   1 
ATOM   116  C CB  . CYS   A 1 16  ? 12.312  16.060  18.985 1.00 36.55  ? 16  CYS   A CB  1 
ATOM   117  S SG  . CYS   A 1 16  ? 13.936  16.835  19.025 1.00 52.53  ? 16  CYS   A SG  1 
ATOM   118  N N   . MET   A 1 17  ? 9.570   15.247  21.034 1.00 41.19  ? 17  MET   A N   1 
ATOM   119  C CA  . MET   A 1 17  ? 8.315   14.508  21.032 1.00 42.27  ? 17  MET   A CA  1 
ATOM   120  C C   . MET   A 1 17  ? 7.154   15.437  21.355 1.00 47.64  ? 17  MET   A C   1 
ATOM   121  O O   . MET   A 1 17  ? 7.148   16.103  22.395 1.00 51.74  ? 17  MET   A O   1 
ATOM   122  C CB  . MET   A 1 17  ? 8.358   13.359  22.039 1.00 44.09  ? 17  MET   A CB  1 
ATOM   123  C CG  . MET   A 1 17  ? 9.405   12.309  21.724 1.00 49.21  ? 17  MET   A CG  1 
ATOM   124  S SD  . MET   A 1 17  ? 9.427   11.832  19.984 1.00 45.99  ? 17  MET   A SD  1 
ATOM   125  C CE  . MET   A 1 17  ? 7.790   11.125  19.786 1.00 43.85  ? 17  MET   A CE  1 
ATOM   126  N N   . VAL   A 1 18  ? 6.166   15.466  20.464 1.00 49.16  ? 18  VAL   A N   1 
ATOM   127  C CA  . VAL   A 1 18  ? 4.960   16.258  20.647 1.00 55.84  ? 18  VAL   A CA  1 
ATOM   128  C C   . VAL   A 1 18  ? 3.751   15.344  20.503 1.00 52.66  ? 18  VAL   A C   1 
ATOM   129  O O   . VAL   A 1 18  ? 3.855   14.191  20.082 1.00 47.67  ? 18  VAL   A O   1 
ATOM   130  C CB  . VAL   A 1 18  ? 4.868   17.425  19.646 1.00 51.38  ? 18  VAL   A CB  1 
ATOM   131  C CG1 . VAL   A 1 18  ? 6.051   18.360  19.816 1.00 51.16  ? 18  VAL   A CG1 1 
ATOM   132  C CG2 . VAL   A 1 18  ? 4.799   16.890  18.222 1.00 47.90  ? 18  VAL   A CG2 1 
ATOM   133  N N   . GLN   A 1 19  ? 2.592   15.887  20.854 1.00 53.55  ? 19  GLN   A N   1 
ATOM   134  C CA  . GLN   A 1 19  ? 1.320   15.193  20.721 1.00 51.74  ? 19  GLN   A CA  1 
ATOM   135  C C   . GLN   A 1 19  ? 0.610   15.691  19.469 1.00 58.61  ? 19  GLN   A C   1 
ATOM   136  O O   . GLN   A 1 19  ? 0.530   16.902  19.238 1.00 56.32  ? 19  GLN   A O   1 
ATOM   137  C CB  . GLN   A 1 19  ? 0.451   15.428  21.954 1.00 49.74  ? 19  GLN   A CB  1 
ATOM   138  C CG  . GLN   A 1 19  ? -0.852  14.671  21.948 1.00 52.28  ? 19  GLN   A CG  1 
ATOM   139  C CD  . GLN   A 1 19  ? -1.772  15.123  23.056 1.00 57.99  ? 19  GLN   A CD  1 
ATOM   140  O OE1 . GLN   A 1 19  ? -2.100  14.355  23.959 1.00 58.86  ? 19  GLN   A OE1 1 
ATOM   141  N NE2 . GLN   A 1 19  ? -2.191  16.381  22.996 1.00 65.51  ? 19  GLN   A NE2 1 
ATOM   142  N N   . VAL   A 1 20  ? 0.108   14.763  18.659 1.00 49.78  ? 20  VAL   A N   1 
ATOM   143  C CA  . VAL   A 1 20  ? -0.641  15.100  17.453 1.00 53.43  ? 20  VAL   A CA  1 
ATOM   144  C C   . VAL   A 1 20  ? -2.031  14.499  17.576 1.00 51.58  ? 20  VAL   A C   1 
ATOM   145  O O   . VAL   A 1 20  ? -2.176  13.284  17.760 1.00 51.45  ? 20  VAL   A O   1 
ATOM   146  C CB  . VAL   A 1 20  ? 0.054   14.605  16.178 1.00 50.88  ? 20  VAL   A CB  1 
ATOM   147  C CG1 . VAL   A 1 20  ? -0.796  14.942  14.962 1.00 51.20  ? 20  VAL   A CG1 1 
ATOM   148  C CG2 . VAL   A 1 20  ? 1.433   15.224  16.057 1.00 52.44  ? 20  VAL   A CG2 1 
ATOM   149  N N   . THR   A 1 21  ? -3.049  15.345  17.469 1.00 54.00  ? 21  THR   A N   1 
ATOM   150  C CA  . THR   A 1 21  ? -4.435  14.921  17.570 1.00 58.37  ? 21  THR   A CA  1 
ATOM   151  C C   . THR   A 1 21  ? -5.163  15.288  16.288 1.00 60.33  ? 21  THR   A C   1 
ATOM   152  O O   . THR   A 1 21  ? -5.049  16.419  15.806 1.00 55.46  ? 21  THR   A O   1 
ATOM   153  C CB  . THR   A 1 21  ? -5.125  15.567  18.771 1.00 60.75  ? 21  THR   A CB  1 
ATOM   154  O OG1 . THR   A 1 21  ? -4.327  15.367  19.945 1.00 61.33  ? 21  THR   A OG1 1 
ATOM   155  C CG2 . THR   A 1 21  ? -6.495  14.941  18.988 1.00 56.80  ? 21  THR   A CG2 1 
ATOM   156  N N   . CYS   A 1 22  ? -5.900  14.329  15.735 1.00 55.24  ? 22  CYS   A N   1 
ATOM   157  C CA  . CYS   A 1 22  ? -6.741  14.566  14.564 1.00 61.27  ? 22  CYS   A CA  1 
ATOM   158  C C   . CYS   A 1 22  ? -8.126  14.017  14.878 1.00 58.14  ? 22  CYS   A C   1 
ATOM   159  O O   . CYS   A 1 22  ? -8.358  12.808  14.790 1.00 61.43  ? 22  CYS   A O   1 
ATOM   160  C CB  . CYS   A 1 22  ? -6.159  13.923  13.312 1.00 56.39  ? 22  CYS   A CB  1 
ATOM   161  S SG  . CYS   A 1 22  ? -7.040  14.396  11.815 1.00 64.97  ? 22  CYS   A SG  1 
ATOM   162  N N   . GLY   A 1 23  ? -9.041  14.907  15.245 1.00 62.03  ? 23  GLY   A N   1 
ATOM   163  C CA  . GLY   A 1 23  ? -10.358 14.478  15.657 1.00 50.43  ? 23  GLY   A CA  1 
ATOM   164  C C   . GLY   A 1 23  ? -10.311 13.741  16.977 1.00 65.38  ? 23  GLY   A C   1 
ATOM   165  O O   . GLY   A 1 23  ? -10.035 14.339  18.021 1.00 72.58  ? 23  GLY   A O   1 
ATOM   166  N N   . THR   A 1 24  ? -10.561 12.432  16.938 1.00 57.16  ? 24  THR   A N   1 
ATOM   167  C CA  . THR   A 1 24  ? -10.589 11.602  18.133 1.00 62.59  ? 24  THR   A CA  1 
ATOM   168  C C   . THR   A 1 24  ? -9.306  10.810  18.358 1.00 64.50  ? 24  THR   A C   1 
ATOM   169  O O   . THR   A 1 24  ? -9.174  10.162  19.402 1.00 66.69  ? 24  THR   A O   1 
ATOM   170  C CB  . THR   A 1 24  ? -11.768 10.624  18.063 1.00 66.58  ? 24  THR   A CB  1 
ATOM   171  O OG1 . THR   A 1 24  ? -11.721 9.737   19.186 1.00 63.06  ? 24  THR   A OG1 1 
ATOM   172  C CG2 . THR   A 1 24  ? -11.702 9.809   16.779 1.00 68.79  ? 24  THR   A CG2 1 
ATOM   173  N N   . THR   A 1 25  ? -8.369  10.837  17.415 1.00 63.74  ? 25  THR   A N   1 
ATOM   174  C CA  . THR   A 1 25  ? -7.150  10.042  17.496 1.00 62.97  ? 25  THR   A CA  1 
ATOM   175  C C   . THR   A 1 25  ? -5.991  10.904  17.971 1.00 55.80  ? 25  THR   A C   1 
ATOM   176  O O   . THR   A 1 25  ? -5.751  11.989  17.430 1.00 58.81  ? 25  THR   A O   1 
ATOM   177  C CB  . THR   A 1 25  ? -6.805  9.422   16.141 1.00 56.16  ? 25  THR   A CB  1 
ATOM   178  O OG1 . THR   A 1 25  ? -7.891  8.600   15.698 1.00 60.75  ? 25  THR   A OG1 1 
ATOM   179  C CG2 . THR   A 1 25  ? -5.542  8.575   16.255 1.00 49.33  ? 25  THR   A CG2 1 
ATOM   180  N N   . THR   A 1 26  ? -5.269  10.411  18.971 1.00 48.71  ? 26  THR   A N   1 
ATOM   181  C CA  . THR   A 1 26  ? -4.068  11.057  19.475 1.00 54.21  ? 26  THR   A CA  1 
ATOM   182  C C   . THR   A 1 26  ? -2.897  10.092  19.341 1.00 47.70  ? 26  THR   A C   1 
ATOM   183  O O   . THR   A 1 26  ? -3.004  8.921   19.724 1.00 48.34  ? 26  THR   A O   1 
ATOM   184  C CB  . THR   A 1 26  ? -4.262  11.497  20.934 1.00 57.42  ? 26  THR   A CB  1 
ATOM   185  O OG1 . THR   A 1 26  ? -3.009  11.907  21.496 1.00 58.95  ? 26  THR   A OG1 1 
ATOM   186  C CG2 . THR   A 1 26  ? -4.857  10.366  21.768 1.00 57.37  ? 26  THR   A CG2 1 
ATOM   187  N N   . LEU   A 1 27  ? -1.797  10.570  18.766 1.00 44.96  ? 27  LEU   A N   1 
ATOM   188  C CA  . LEU   A 1 27  ? -0.561  9.798   18.698 1.00 46.50  ? 27  LEU   A CA  1 
ATOM   189  C C   . LEU   A 1 27  ? 0.609   10.755  18.895 1.00 43.83  ? 27  LEU   A C   1 
ATOM   190  O O   . LEU   A 1 27  ? 0.438   11.894  19.340 1.00 50.26  ? 27  LEU   A O   1 
ATOM   191  C CB  . LEU   A 1 27  ? -0.469  9.006   17.384 1.00 42.55  ? 27  LEU   A CB  1 
ATOM   192  C CG  . LEU   A 1 27  ? -0.836  9.650   16.047 1.00 40.59  ? 27  LEU   A CG  1 
ATOM   193  C CD1 . LEU   A 1 27  ? 0.229   10.624  15.551 1.00 40.24  ? 27  LEU   A CD1 1 
ATOM   194  C CD2 . LEU   A 1 27  ? -1.081  8.560   15.021 1.00 42.57  ? 27  LEU   A CD2 1 
ATOM   195  N N   . ASN   A 1 28  ? 1.807   10.290  18.559 1.00 41.55  ? 28  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 28  ? 3.028   11.039  18.809 1.00 42.74  ? 28  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 28  ? 3.578   11.633  17.520 1.00 39.58  ? 28  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 28  ? 3.453   11.050  16.440 1.00 42.21  ? 28  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 28  ? 4.084   10.146  19.463 1.00 40.74  ? 28  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 28  ? 3.589   9.503   20.741 1.00 37.22  ? 28  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 28  ? 3.429   10.172  21.759 1.00 40.26  ? 28  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 28  ? 3.354   8.195   20.698 1.00 32.82  ? 28  ASN   A ND2 1 
ATOM   203  N N   . GLY   A 1 29  ? 4.195   12.810  17.649 1.00 38.03  ? 29  GLY   A N   1 
ATOM   204  C CA  . GLY   A 1 29  ? 4.850   13.450  16.533 1.00 38.24  ? 29  GLY   A CA  1 
ATOM   205  C C   . GLY   A 1 29  ? 6.277   13.827  16.887 1.00 44.08  ? 29  GLY   A C   1 
ATOM   206  O O   . GLY   A 1 29  ? 6.648   13.921  18.057 1.00 42.95  ? 29  GLY   A O   1 
ATOM   207  N N   . LEU   A 1 30  ? 7.077   14.043  15.842 1.00 39.56  ? 30  LEU   A N   1 
ATOM   208  C CA  . LEU   A 1 30  ? 8.489   14.396  15.971 1.00 41.00  ? 30  LEU   A CA  1 
ATOM   209  C C   . LEU   A 1 30  ? 8.681   15.825  15.476 1.00 44.67  ? 30  LEU   A C   1 
ATOM   210  O O   . LEU   A 1 30  ? 8.577   16.091  14.274 1.00 37.40  ? 30  LEU   A O   1 
ATOM   211  C CB  . LEU   A 1 30  ? 9.368   13.427  15.184 1.00 43.37  ? 30  LEU   A CB  1 
ATOM   212  C CG  . LEU   A 1 30  ? 10.877  13.632  15.331 1.00 47.54  ? 30  LEU   A CG  1 
ATOM   213  C CD1 . LEU   A 1 30  ? 11.310  13.328  16.758 1.00 40.56  ? 30  LEU   A CD1 1 
ATOM   214  C CD2 . LEU   A 1 30  ? 11.648  12.777  14.338 1.00 39.04  ? 30  LEU   A CD2 1 
ATOM   215  N N   . TRP   A 1 31  ? 8.986   16.736  16.397 1.00 44.11  ? 31  TRP   A N   1 
ATOM   216  C CA  . TRP   A 1 31  ? 9.072   18.165  16.096 1.00 42.03  ? 31  TRP   A CA  1 
ATOM   217  C C   . TRP   A 1 31  ? 10.528  18.536  15.836 1.00 44.58  ? 31  TRP   A C   1 
ATOM   218  O O   . TRP   A 1 31  ? 11.330  18.649  16.767 1.00 40.12  ? 31  TRP   A O   1 
ATOM   219  C CB  . TRP   A 1 31  ? 8.492   18.989  17.237 1.00 47.07  ? 31  TRP   A CB  1 
ATOM   220  C CG  . TRP   A 1 31  ? 8.455   20.455  16.960 1.00 46.60  ? 31  TRP   A CG  1 
ATOM   221  C CD1 . TRP   A 1 31  ? 8.520   21.067  15.741 1.00 47.15  ? 31  TRP   A CD1 1 
ATOM   222  C CD2 . TRP   A 1 31  ? 8.347   21.501  17.929 1.00 50.89  ? 31  TRP   A CD2 1 
ATOM   223  N NE1 . TRP   A 1 31  ? 8.455   22.432  15.892 1.00 52.12  ? 31  TRP   A NE1 1 
ATOM   224  C CE2 . TRP   A 1 31  ? 8.347   22.724  17.227 1.00 51.76  ? 31  TRP   A CE2 1 
ATOM   225  C CE3 . TRP   A 1 31  ? 8.249   21.523  19.323 1.00 46.36  ? 31  TRP   A CE3 1 
ATOM   226  C CZ2 . TRP   A 1 31  ? 8.252   23.953  17.872 1.00 52.48  ? 31  TRP   A CZ2 1 
ATOM   227  C CZ3 . TRP   A 1 31  ? 8.155   22.745  19.962 1.00 57.52  ? 31  TRP   A CZ3 1 
ATOM   228  C CH2 . TRP   A 1 31  ? 8.159   23.944  19.236 1.00 45.67  ? 31  TRP   A CH2 1 
ATOM   229  N N   . LEU   A 1 32  ? 10.858  18.743  14.564 1.00 39.82  ? 32  LEU   A N   1 
ATOM   230  C CA  . LEU   A 1 32  ? 12.197  19.124  14.135 1.00 44.29  ? 32  LEU   A CA  1 
ATOM   231  C C   . LEU   A 1 32  ? 12.090  20.400  13.316 1.00 49.20  ? 32  LEU   A C   1 
ATOM   232  O O   . LEU   A 1 32  ? 11.371  20.435  12.312 1.00 47.40  ? 32  LEU   A O   1 
ATOM   233  C CB  . LEU   A 1 32  ? 12.854  18.010  13.318 1.00 41.42  ? 32  LEU   A CB  1 
ATOM   234  C CG  . LEU   A 1 32  ? 13.198  16.714  14.057 1.00 47.02  ? 32  LEU   A CG  1 
ATOM   235  C CD1 . LEU   A 1 32  ? 13.726  15.675  13.085 1.00 41.05  ? 32  LEU   A CD1 1 
ATOM   236  C CD2 . LEU   A 1 32  ? 14.214  16.977  15.162 1.00 47.31  ? 32  LEU   A CD2 1 
ATOM   237  N N   . ASP   A 1 33  ? 12.813  21.438  13.740 1.00 54.50  ? 33  ASP   A N   1 
ATOM   238  C CA  . ASP   A 1 33  ? 12.692  22.763  13.141 1.00 47.37  ? 33  ASP   A CA  1 
ATOM   239  C C   . ASP   A 1 33  ? 11.230  23.195  13.151 1.00 49.56  ? 33  ASP   A C   1 
ATOM   240  O O   . ASP   A 1 33  ? 10.586  23.177  14.204 1.00 48.91  ? 33  ASP   A O   1 
ATOM   241  C CB  . ASP   A 1 33  ? 13.272  22.767  11.726 1.00 57.95  ? 33  ASP   A CB  1 
ATOM   242  C CG  . ASP   A 1 33  ? 14.753  22.442  11.707 1.00 55.49  ? 33  ASP   A CG  1 
ATOM   243  O OD1 . ASP   A 1 33  ? 15.500  23.034  12.515 1.00 53.40  ? 33  ASP   A OD1 1 
ATOM   244  O OD2 . ASP   A 1 33  ? 15.171  21.589  10.892 1.00 56.96  ? 33  ASP   A OD2 1 
ATOM   245  N N   . ASP   A 1 34  ? 10.683  23.554  11.991 1.00 55.30  ? 34  ASP   A N   1 
ATOM   246  C CA  . ASP   A 1 34  ? 9.297   23.997  11.893 1.00 62.17  ? 34  ASP   A CA  1 
ATOM   247  C C   . ASP   A 1 34  ? 8.389   22.935  11.274 1.00 65.86  ? 34  ASP   A C   1 
ATOM   248  O O   . ASP   A 1 34  ? 7.400   23.266  10.615 1.00 69.89  ? 34  ASP   A O   1 
ATOM   249  C CB  . ASP   A 1 34  ? 9.210   25.302  11.101 1.00 61.14  ? 34  ASP   A CB  1 
ATOM   250  C CG  . ASP   A 1 34  ? 9.717   25.160  9.677  1.00 69.98  ? 34  ASP   A CG  1 
ATOM   251  O OD1 . ASP   A 1 34  ? 10.518  24.239  9.416  1.00 67.73  ? 34  ASP   A OD1 1 
ATOM   252  O OD2 . ASP   A 1 34  ? 9.318   25.976  8.818  1.00 76.16  ? 34  ASP   A OD2 1 
ATOM   253  N N   . VAL   A 1 35  ? 8.702   21.657  11.483 1.00 58.23  ? 35  VAL   A N   1 
ATOM   254  C CA  . VAL   A 1 35  ? 7.934   20.552  10.920 1.00 50.65  ? 35  VAL   A CA  1 
ATOM   255  C C   . VAL   A 1 35  ? 7.625   19.548  12.024 1.00 53.51  ? 35  VAL   A C   1 
ATOM   256  O O   . VAL   A 1 35  ? 8.459   19.299  12.903 1.00 45.74  ? 35  VAL   A O   1 
ATOM   257  C CB  . VAL   A 1 35  ? 8.690   19.867  9.760  1.00 52.26  ? 35  VAL   A CB  1 
ATOM   258  C CG1 . VAL   A 1 35  ? 7.848   18.753  9.151  1.00 52.16  ? 35  VAL   A CG1 1 
ATOM   259  C CG2 . VAL   A 1 35  ? 9.078   20.885  8.697  1.00 56.47  ? 35  VAL   A CG2 1 
ATOM   260  N N   . VAL   A 1 36  ? 6.423   18.979  11.984 1.00 43.66  ? 36  VAL   A N   1 
ATOM   261  C CA  . VAL   A 1 36  ? 6.031   17.885  12.865 1.00 45.53  ? 36  VAL   A CA  1 
ATOM   262  C C   . VAL   A 1 36  ? 5.760   16.662  11.997 1.00 48.61  ? 36  VAL   A C   1 
ATOM   263  O O   . VAL   A 1 36  ? 4.896   16.702  11.111 1.00 46.31  ? 36  VAL   A O   1 
ATOM   264  C CB  . VAL   A 1 36  ? 4.803   18.246  13.716 1.00 46.82  ? 36  VAL   A CB  1 
ATOM   265  C CG1 . VAL   A 1 36  ? 4.345   17.043  14.527 1.00 41.70  ? 36  VAL   A CG1 1 
ATOM   266  C CG2 . VAL   A 1 36  ? 5.123   19.415  14.635 1.00 50.83  ? 36  VAL   A CG2 1 
ATOM   267  N N   . TYR   A 1 37  ? 6.499   15.582  12.246 1.00 47.87  ? 37  TYR   A N   1 
ATOM   268  C CA  . TYR   A 1 37  ? 6.363   14.333  11.507 1.00 40.09  ? 37  TYR   A CA  1 
ATOM   269  C C   . TYR   A 1 37  ? 5.579   13.324  12.337 1.00 40.54  ? 37  TYR   A C   1 
ATOM   270  O O   . TYR   A 1 37  ? 5.818   13.181  13.541 1.00 42.98  ? 37  TYR   A O   1 
ATOM   271  C CB  . TYR   A 1 37  ? 7.734   13.748  11.155 1.00 39.98  ? 37  TYR   A CB  1 
ATOM   272  C CG  . TYR   A 1 37  ? 8.663   14.684  10.411 1.00 42.08  ? 37  TYR   A CG  1 
ATOM   273  C CD1 . TYR   A 1 37  ? 9.442   15.611  11.093 1.00 45.58  ? 37  TYR   A CD1 1 
ATOM   274  C CD2 . TYR   A 1 37  ? 8.779   14.627  9.027  1.00 45.34  ? 37  TYR   A CD2 1 
ATOM   275  C CE1 . TYR   A 1 37  ? 10.295  16.463  10.418 1.00 44.28  ? 37  TYR   A CE1 1 
ATOM   276  C CE2 . TYR   A 1 37  ? 9.632   15.474  8.344  1.00 43.19  ? 37  TYR   A CE2 1 
ATOM   277  C CZ  . TYR   A 1 37  ? 10.387  16.389  9.045  1.00 43.97  ? 37  TYR   A CZ  1 
ATOM   278  O OH  . TYR   A 1 37  ? 11.237  17.237  8.373  1.00 47.05  ? 37  TYR   A OH  1 
ATOM   279  N N   . CYS   A 1 38  ? 4.646   12.625  11.693 1.00 39.23  ? 38  CYS   A N   1 
ATOM   280  C CA  . CYS   A 1 38  ? 3.845   11.607  12.361 1.00 41.59  ? 38  CYS   A CA  1 
ATOM   281  C C   . CYS   A 1 38  ? 3.283   10.663  11.302 1.00 38.70  ? 38  CYS   A C   1 
ATOM   282  O O   . CYS   A 1 38  ? 3.361   10.955  10.103 1.00 37.78  ? 38  CYS   A O   1 
ATOM   283  C CB  . CYS   A 1 38  ? 2.715   12.242  13.193 1.00 41.54  ? 38  CYS   A CB  1 
ATOM   284  S SG  . CYS   A 1 38  ? 1.303   12.859  12.251 1.00 48.01  ? 38  CYS   A SG  1 
ATOM   285  N N   . PRO   A 1 39  ? 2.747   9.508   11.706 1.00 41.55  ? 39  PRO   A N   1 
ATOM   286  C CA  . PRO   A 1 39  ? 2.174   8.585   10.715 1.00 40.30  ? 39  PRO   A CA  1 
ATOM   287  C C   . PRO   A 1 39  ? 0.895   9.146   10.112 1.00 41.49  ? 39  PRO   A C   1 
ATOM   288  O O   . PRO   A 1 39  ? 0.048   9.698   10.816 1.00 39.84  ? 39  PRO   A O   1 
ATOM   289  C CB  . PRO   A 1 39  ? 1.896   7.313   11.529 1.00 33.87  ? 39  PRO   A CB  1 
ATOM   290  C CG  . PRO   A 1 39  ? 2.753   7.431   12.745 1.00 41.01  ? 39  PRO   A CG  1 
ATOM   291  C CD  . PRO   A 1 39  ? 2.816   8.895   13.045 1.00 38.24  ? 39  PRO   A CD  1 
ATOM   292  N N   . ARG   A 1 40  ? 0.745   8.978   8.797  1.00 34.52  ? 40  ARG   A N   1 
ATOM   293  C CA  . ARG   A 1 40  ? -0.406  9.558   8.113  1.00 38.33  ? 40  ARG   A CA  1 
ATOM   294  C C   . ARG   A 1 40  ? -1.725  8.899   8.507  1.00 36.80  ? 40  ARG   A C   1 
ATOM   295  O O   . ARG   A 1 40  ? -2.780  9.526   8.360  1.00 32.18  ? 40  ARG   A O   1 
ATOM   296  C CB  . ARG   A 1 40  ? -0.222  9.475   6.596  1.00 40.32  ? 40  ARG   A CB  1 
ATOM   297  C CG  . ARG   A 1 40  ? -0.261  8.077   6.008  1.00 32.94  ? 40  ARG   A CG  1 
ATOM   298  C CD  . ARG   A 1 40  ? -0.151  8.137   4.487  1.00 33.08  ? 40  ARG   A CD  1 
ATOM   299  N NE  . ARG   A 1 40  ? -0.062  6.817   3.870  1.00 30.73  ? 40  ARG   A NE  1 
ATOM   300  C CZ  . ARG   A 1 40  ? -0.069  6.610   2.560  1.00 36.72  ? 40  ARG   A CZ  1 
ATOM   301  N NH1 . ARG   A 1 40  ? -0.166  7.614   1.702  1.00 36.74  ? 40  ARG   A NH1 1 
ATOM   302  N NH2 . ARG   A 1 40  ? 0.021   5.365   2.098  1.00 33.27  ? 40  ARG   A NH2 1 
ATOM   303  N N   . HIS   A 1 41  ? -1.698  7.663   9.017  1.00 38.35  ? 41  HIS   A N   1 
ATOM   304  C CA  . HIS   A 1 41  ? -2.950  7.005   9.388  1.00 38.30  ? 41  HIS   A CA  1 
ATOM   305  C C   . HIS   A 1 41  ? -3.654  7.677   10.565 1.00 37.98  ? 41  HIS   A C   1 
ATOM   306  O O   . HIS   A 1 41  ? -4.727  7.214   10.965 1.00 41.08  ? 41  HIS   A O   1 
ATOM   307  C CB  . HIS   A 1 41  ? -2.723  5.504   9.667  1.00 39.11  ? 41  HIS   A CB  1 
ATOM   308  C CG  . HIS   A 1 41  ? -1.870  5.199   10.863 1.00 42.46  ? 41  HIS   A CG  1 
ATOM   309  N ND1 . HIS   A 1 41  ? -2.178  5.631   12.136 1.00 37.74  ? 41  HIS   A ND1 1 
ATOM   310  C CD2 . HIS   A 1 41  ? -0.749  4.448   10.983 1.00 42.98  ? 41  HIS   A CD2 1 
ATOM   311  C CE1 . HIS   A 1 41  ? -1.268  5.184   12.983 1.00 35.20  ? 41  HIS   A CE1 1 
ATOM   312  N NE2 . HIS   A 1 41  ? -0.390  4.462   12.310 1.00 42.19  ? 41  HIS   A NE2 1 
ATOM   313  N N   . VAL   A 1 42  ? -3.104  8.765   11.111 1.00 37.63  ? 42  VAL   A N   1 
ATOM   314  C CA  . VAL   A 1 42  ? -3.814  9.539   12.122 1.00 44.49  ? 42  VAL   A CA  1 
ATOM   315  C C   . VAL   A 1 42  ? -5.121  10.110  11.575 1.00 44.14  ? 42  VAL   A C   1 
ATOM   316  O O   . VAL   A 1 42  ? -6.064  10.340  12.339 1.00 43.32  ? 42  VAL   A O   1 
ATOM   317  C CB  . VAL   A 1 42  ? -2.885  10.652  12.671 1.00 37.42  ? 42  VAL   A CB  1 
ATOM   318  C CG1 . VAL   A 1 42  ? -2.519  11.666  11.586 1.00 36.27  ? 42  VAL   A CG1 1 
ATOM   319  C CG2 . VAL   A 1 42  ? -3.498  11.333  13.884 1.00 45.15  ? 42  VAL   A CG2 1 
ATOM   320  N N   . ILE   A 1 43  ? -5.217  10.315  10.255 1.00 49.17  ? 43  ILE   A N   1 
ATOM   321  C CA  . ILE   A 1 43  ? -6.405  10.932  9.671  1.00 53.22  ? 43  ILE   A CA  1 
ATOM   322  C C   . ILE   A 1 43  ? -7.483  9.922   9.300  1.00 44.85  ? 43  ILE   A C   1 
ATOM   323  O O   . ILE   A 1 43  ? -8.512  10.313  8.734  1.00 49.01  ? 43  ILE   A O   1 
ATOM   324  C CB  . ILE   A 1 43  ? -6.030  11.761  8.426  1.00 46.38  ? 43  ILE   A CB  1 
ATOM   325  C CG1 . ILE   A 1 43  ? -5.613  10.838  7.279  1.00 41.98  ? 43  ILE   A CG1 1 
ATOM   326  C CG2 . ILE   A 1 43  ? -4.919  12.739  8.765  1.00 50.48  ? 43  ILE   A CG2 1 
ATOM   327  C CD1 . ILE   A 1 43  ? -5.235  11.579  6.007  1.00 41.87  ? 43  ILE   A CD1 1 
ATOM   328  N N   . CYS   A 1 44  ? -7.295  8.644   9.616  1.00 37.77  ? 44  CYS   A N   1 
ATOM   329  C CA  . CYS   A 1 44  ? -8.202  7.588   9.189  1.00 40.17  ? 44  CYS   A CA  1 
ATOM   330  C C   . CYS   A 1 44  ? -9.100  7.129   10.327 1.00 48.28  ? 44  CYS   A C   1 
ATOM   331  O O   . CYS   A 1 44  ? -8.669  7.035   11.480 1.00 45.33  ? 44  CYS   A O   1 
ATOM   332  C CB  . CYS   A 1 44  ? -7.431  6.382   8.659  1.00 39.37  ? 44  CYS   A CB  1 
ATOM   333  S SG  . CYS   A 1 44  ? -6.457  6.708   7.203  1.00 43.82  ? 44  CYS   A SG  1 
ATOM   334  N N   . THR   A 1 45  ? -10.345 6.827   9.989  1.00 46.73  ? 45  THR   A N   1 
ATOM   335  C CA  . THR   A 1 45  ? -11.232 6.111   10.887 1.00 49.59  ? 45  THR   A CA  1 
ATOM   336  C C   . THR   A 1 45  ? -11.031 4.609   10.703 1.00 51.42  ? 45  THR   A C   1 
ATOM   337  O O   . THR   A 1 45  ? -10.348 4.157   9.781  1.00 48.90  ? 45  THR   A O   1 
ATOM   338  C CB  . THR   A 1 45  ? -12.682 6.500   10.620 1.00 54.11  ? 45  THR   A CB  1 
ATOM   339  O OG1 . THR   A 1 45  ? -13.050 6.072   9.302  1.00 54.48  ? 45  THR   A OG1 1 
ATOM   340  C CG2 . THR   A 1 45  ? -12.838 8.006   10.708 1.00 48.97  ? 45  THR   A CG2 1 
ATOM   341  N N   . SER   A 1 46  ? -11.629 3.827   11.605 1.00 54.56  ? 46  SER   A N   1 
ATOM   342  C CA  . SER   A 1 46  ? -11.595 2.378   11.438 1.00 48.40  ? 46  SER   A CA  1 
ATOM   343  C C   . SER   A 1 46  ? -12.190 1.968   10.096 1.00 51.95  ? 46  SER   A C   1 
ATOM   344  O O   . SER   A 1 46  ? -11.678 1.051   9.441  1.00 52.95  ? 46  SER   A O   1 
ATOM   345  C CB  . SER   A 1 46  ? -12.330 1.698   12.594 1.00 50.56  ? 46  SER   A CB  1 
ATOM   346  O OG  . SER   A 1 46  ? -11.627 1.873   13.812 1.00 56.18  ? 46  SER   A OG  1 
ATOM   347  N N   . GLU   A 1 47  ? -13.246 2.658   9.655  1.00 48.65  ? 47  GLU   A N   1 
ATOM   348  C CA  . GLU   A 1 47  ? -13.845 2.355   8.361  1.00 52.14  ? 47  GLU   A CA  1 
ATOM   349  C C   . GLU   A 1 47  ? -12.910 2.719   7.214  1.00 51.74  ? 47  GLU   A C   1 
ATOM   350  O O   . GLU   A 1 47  ? -12.857 1.999   6.209  1.00 51.87  ? 47  GLU   A O   1 
ATOM   351  C CB  . GLU   A 1 47  ? -15.181 3.089   8.216  1.00 50.53  ? 47  GLU   A CB  1 
ATOM   352  N N   . ASP   A 1 48  ? -12.167 3.823   7.344  1.00 46.33  ? 48  ASP   A N   1 
ATOM   353  C CA  . ASP   A 1 48  ? -11.240 4.214   6.285  1.00 52.38  ? 48  ASP   A CA  1 
ATOM   354  C C   . ASP   A 1 48  ? -10.141 3.182   6.084  1.00 49.48  ? 48  ASP   A C   1 
ATOM   355  O O   . ASP   A 1 48  ? -9.669  2.992   4.957  1.00 49.89  ? 48  ASP   A O   1 
ATOM   356  C CB  . ASP   A 1 48  ? -10.607 5.568   6.595  1.00 49.63  ? 48  ASP   A CB  1 
ATOM   357  C CG  . ASP   A 1 48  ? -11.586 6.708   6.491  1.00 56.01  ? 48  ASP   A CG  1 
ATOM   358  O OD1 . ASP   A 1 48  ? -12.505 6.627   5.649  1.00 60.01  ? 48  ASP   A OD1 1 
ATOM   359  O OD2 . ASP   A 1 48  ? -11.427 7.687   7.253  1.00 56.06  ? 48  ASP   A OD2 1 
ATOM   360  N N   . MET   A 1 49  ? -9.721  2.503   7.151  1.00 44.86  ? 49  MET   A N   1 
ATOM   361  C CA  . MET   A 1 49  ? -8.543  1.652   7.042  1.00 45.44  ? 49  MET   A CA  1 
ATOM   362  C C   . MET   A 1 49  ? -8.799  0.388   6.235  1.00 47.59  ? 49  MET   A C   1 
ATOM   363  O O   . MET   A 1 49  ? -7.835  -0.240  5.786  1.00 44.93  ? 49  MET   A O   1 
ATOM   364  C CB  . MET   A 1 49  ? -8.011  1.303   8.430  1.00 46.13  ? 49  MET   A CB  1 
ATOM   365  C CG  . MET   A 1 49  ? -7.352  2.479   9.136  1.00 46.30  ? 49  MET   A CG  1 
ATOM   366  S SD  . MET   A 1 49  ? -5.909  3.155   8.278  1.00 44.87  ? 49  MET   A SD  1 
ATOM   367  C CE  . MET   A 1 49  ? -4.650  1.956   8.705  1.00 39.74  ? 49  MET   A CE  1 
ATOM   368  N N   . LEU   A 1 50  ? -10.063 0.011   6.014  1.00 48.53  ? 50  LEU   A N   1 
ATOM   369  C CA  . LEU   A 1 50  ? -10.337 -1.136  5.151  1.00 53.14  ? 50  LEU   A CA  1 
ATOM   370  C C   . LEU   A 1 50  ? -9.794  -0.912  3.745  1.00 47.86  ? 50  LEU   A C   1 
ATOM   371  O O   . LEU   A 1 50  ? -9.237  -1.831  3.132  1.00 51.67  ? 50  LEU   A O   1 
ATOM   372  C CB  . LEU   A 1 50  ? -11.837 -1.427  5.103  1.00 57.99  ? 50  LEU   A CB  1 
ATOM   373  C CG  . LEU   A 1 50  ? -12.396 -2.304  6.224  1.00 61.30  ? 50  LEU   A CG  1 
ATOM   374  C CD1 . LEU   A 1 50  ? -13.740 -2.874  5.805  1.00 63.04  ? 50  LEU   A CD1 1 
ATOM   375  C CD2 . LEU   A 1 50  ? -11.423 -3.418  6.587  1.00 60.02  ? 50  LEU   A CD2 1 
ATOM   376  N N   . ASN   A 1 51  ? -9.941  0.306   3.219  1.00 50.21  ? 51  ASN   A N   1 
ATOM   377  C CA  . ASN   A 1 51  ? -9.391  0.659   1.914  1.00 51.52  ? 51  ASN   A CA  1 
ATOM   378  C C   . ASN   A 1 51  ? -9.209  2.169   1.826  1.00 49.49  ? 51  ASN   A C   1 
ATOM   379  O O   . ASN   A 1 51  ? -10.061 2.866   1.261  1.00 53.46  ? 51  ASN   A O   1 
ATOM   380  C CB  . ASN   A 1 51  ? -10.294 0.169   0.782  1.00 55.06  ? 51  ASN   A CB  1 
ATOM   381  C CG  . ASN   A 1 51  ? -9.685  0.401   -0.584 1.00 58.97  ? 51  ASN   A CG  1 
ATOM   382  O OD1 . ASN   A 1 51  ? -8.464  0.354   -0.750 1.00 57.58  ? 51  ASN   A OD1 1 
ATOM   383  N ND2 . ASN   A 1 51  ? -10.531 0.666   -1.571 1.00 72.72  ? 51  ASN   A ND2 1 
ATOM   384  N N   . PRO   A 1 52  ? -8.116  2.708   2.365  1.00 46.83  ? 52  PRO   A N   1 
ATOM   385  C CA  . PRO   A 1 52  ? -7.975  4.165   2.444  1.00 48.74  ? 52  PRO   A CA  1 
ATOM   386  C C   . PRO   A 1 52  ? -7.331  4.770   1.209  1.00 40.92  ? 52  PRO   A C   1 
ATOM   387  O O   . PRO   A 1 52  ? -6.245  4.356   0.793  1.00 45.93  ? 52  PRO   A O   1 
ATOM   388  C CB  . PRO   A 1 52  ? -7.087  4.351   3.676  1.00 43.84  ? 52  PRO   A CB  1 
ATOM   389  C CG  . PRO   A 1 52  ? -6.194  3.143   3.640  1.00 42.68  ? 52  PRO   A CG  1 
ATOM   390  C CD  . PRO   A 1 52  ? -6.998  2.012   3.026  1.00 43.77  ? 52  PRO   A CD  1 
ATOM   391  N N   . ASN   A 1 53  ? -8.000  5.752   0.614  1.00 45.91  ? 53  ASN   A N   1 
ATOM   392  C CA  . ASN   A 1 53  ? -7.382  6.588   -0.411 1.00 42.49  ? 53  ASN   A CA  1 
ATOM   393  C C   . ASN   A 1 53  ? -6.809  7.790   0.323  1.00 40.33  ? 53  ASN   A C   1 
ATOM   394  O O   . ASN   A 1 53  ? -7.503  8.775   0.587  1.00 42.75  ? 53  ASN   A O   1 
ATOM   395  C CB  . ASN   A 1 53  ? -8.391  6.983   -1.480 1.00 44.42  ? 53  ASN   A CB  1 
ATOM   396  C CG  . ASN   A 1 53  ? -7.740  7.644   -2.679 1.00 48.78  ? 53  ASN   A CG  1 
ATOM   397  O OD1 . ASN   A 1 53  ? -6.863  8.498   -2.536 1.00 42.63  ? 53  ASN   A OD1 1 
ATOM   398  N ND2 . ASN   A 1 53  ? -8.165  7.247   -3.874 1.00 44.35  ? 53  ASN   A ND2 1 
ATOM   399  N N   . TYR   A 1 54  ? -5.523  7.699   0.670  1.00 38.63  ? 54  TYR   A N   1 
ATOM   400  C CA  . TYR   A 1 54  ? -4.926  8.690   1.558  1.00 44.93  ? 54  TYR   A CA  1 
ATOM   401  C C   . TYR   A 1 54  ? -4.892  10.069  0.913  1.00 44.78  ? 54  TYR   A C   1 
ATOM   402  O O   . TYR   A 1 54  ? -5.144  11.079  1.582  1.00 46.21  ? 54  TYR   A O   1 
ATOM   403  C CB  . TYR   A 1 54  ? -3.524  8.247   1.972  1.00 39.57  ? 54  TYR   A CB  1 
ATOM   404  C CG  . TYR   A 1 54  ? -3.521  7.292   3.145  1.00 37.81  ? 54  TYR   A CG  1 
ATOM   405  C CD1 . TYR   A 1 54  ? -3.664  7.764   4.443  1.00 39.77  ? 54  TYR   A CD1 1 
ATOM   406  C CD2 . TYR   A 1 54  ? -3.377  5.921   2.957  1.00 34.21  ? 54  TYR   A CD2 1 
ATOM   407  C CE1 . TYR   A 1 54  ? -3.655  6.904   5.523  1.00 36.57  ? 54  TYR   A CE1 1 
ATOM   408  C CE2 . TYR   A 1 54  ? -3.369  5.049   4.039  1.00 36.65  ? 54  TYR   A CE2 1 
ATOM   409  C CZ  . TYR   A 1 54  ? -3.512  5.552   5.321  1.00 32.22  ? 54  TYR   A CZ  1 
ATOM   410  O OH  . TYR   A 1 54  ? -3.509  4.706   6.407  1.00 37.40  ? 54  TYR   A OH  1 
ATOM   411  N N   . GLU   A 1 55  ? -4.594  10.131  -0.385 1.00 43.65  ? 55  GLU   A N   1 
ATOM   412  C CA  . GLU   A 1 55  ? -4.634  11.409  -1.086 1.00 49.18  ? 55  GLU   A CA  1 
ATOM   413  C C   . GLU   A 1 55  ? -6.007  12.062  -0.958 1.00 47.90  ? 55  GLU   A C   1 
ATOM   414  O O   . GLU   A 1 55  ? -6.108  13.259  -0.664 1.00 51.20  ? 55  GLU   A O   1 
ATOM   415  C CB  . GLU   A 1 55  ? -4.254  11.204  -2.551 1.00 47.69  ? 55  GLU   A CB  1 
ATOM   416  C CG  . GLU   A 1 55  ? -3.065  12.029  -2.995 1.00 62.28  ? 55  GLU   A CG  1 
ATOM   417  C CD  . GLU   A 1 55  ? -3.483  13.267  -3.760 1.00 76.76  ? 55  GLU   A CD  1 
ATOM   418  O OE1 . GLU   A 1 55  ? -4.325  13.138  -4.676 1.00 78.93  ? 55  GLU   A OE1 1 
ATOM   419  O OE2 . GLU   A 1 55  ? -2.978  14.367  -3.441 1.00 74.61  ? 55  GLU   A OE2 1 
ATOM   420  N N   . ASP   A 1 56  ? -7.077  11.283  -1.134 1.00 48.11  ? 56  ASP   A N   1 
ATOM   421  C CA  . ASP   A 1 56  ? -8.422  11.838  -1.012 1.00 42.14  ? 56  ASP   A CA  1 
ATOM   422  C C   . ASP   A 1 56  ? -8.749  12.216  0.428  1.00 44.83  ? 56  ASP   A C   1 
ATOM   423  O O   . ASP   A 1 56  ? -9.382  13.250  0.672  1.00 49.18  ? 56  ASP   A O   1 
ATOM   424  C CB  . ASP   A 1 56  ? -9.456  10.845  -1.543 1.00 45.06  ? 56  ASP   A CB  1 
ATOM   425  C CG  . ASP   A 1 56  ? -9.441  10.737  -3.056 1.00 54.98  ? 56  ASP   A CG  1 
ATOM   426  O OD1 . ASP   A 1 56  ? -8.646  11.458  -3.699 1.00 48.31  ? 56  ASP   A OD1 1 
ATOM   427  O OD2 . ASP   A 1 56  ? -10.225 9.927   -3.597 1.00 49.57  ? 56  ASP   A OD2 1 
ATOM   428  N N   . LEU   A 1 57  ? -8.347  11.388  1.396  1.00 46.95  ? 57  LEU   A N   1 
ATOM   429  C CA  . LEU   A 1 57  ? -8.681  11.683  2.786  1.00 48.41  ? 57  LEU   A CA  1 
ATOM   430  C C   . LEU   A 1 57  ? -7.947  12.925  3.276  1.00 50.93  ? 57  LEU   A C   1 
ATOM   431  O O   . LEU   A 1 57  ? -8.531  13.764  3.972  1.00 52.03  ? 57  LEU   A O   1 
ATOM   432  C CB  . LEU   A 1 57  ? -8.366  10.480  3.676  1.00 47.03  ? 57  LEU   A CB  1 
ATOM   433  C CG  . LEU   A 1 57  ? -9.225  9.236   3.436  1.00 52.84  ? 57  LEU   A CG  1 
ATOM   434  C CD1 . LEU   A 1 57  ? -8.767  8.079   4.308  1.00 50.49  ? 57  LEU   A CD1 1 
ATOM   435  C CD2 . LEU   A 1 57  ? -10.700 9.539   3.674  1.00 40.05  ? 57  LEU   A CD2 1 
ATOM   436  N N   . LEU   A 1 58  ? -6.671  13.065  2.911  1.00 47.30  ? 58  LEU   A N   1 
ATOM   437  C CA  . LEU   A 1 58  ? -5.913  14.245  3.311  1.00 53.72  ? 58  LEU   A CA  1 
ATOM   438  C C   . LEU   A 1 58  ? -6.453  15.509  2.656  1.00 53.03  ? 58  LEU   A C   1 
ATOM   439  O O   . LEU   A 1 58  ? -6.332  16.600  3.222  1.00 51.70  ? 58  LEU   A O   1 
ATOM   440  C CB  . LEU   A 1 58  ? -4.437  14.062  2.963  1.00 57.93  ? 58  LEU   A CB  1 
ATOM   441  C CG  . LEU   A 1 58  ? -3.500  15.142  3.497  1.00 53.03  ? 58  LEU   A CG  1 
ATOM   442  C CD1 . LEU   A 1 58  ? -3.558  15.164  5.016  1.00 55.83  ? 58  LEU   A CD1 1 
ATOM   443  C CD2 . LEU   A 1 58  ? -2.082  14.910  3.012  1.00 53.95  ? 58  LEU   A CD2 1 
ATOM   444  N N   . ILE   A 1 59  ? -7.040  15.384  1.466  1.00 53.81  ? 59  ILE   A N   1 
ATOM   445  C CA  . ILE   A 1 59  ? -7.623  16.547  0.806  1.00 56.51  ? 59  ILE   A CA  1 
ATOM   446  C C   . ILE   A 1 59  ? -8.835  17.043  1.584  1.00 50.14  ? 59  ILE   A C   1 
ATOM   447  O O   . ILE   A 1 59  ? -9.055  18.253  1.713  1.00 59.42  ? 59  ILE   A O   1 
ATOM   448  C CB  . ILE   A 1 59  ? -7.958  16.208  -0.659 1.00 55.48  ? 59  ILE   A CB  1 
ATOM   449  C CG1 . ILE   A 1 59  ? -6.827  16.689  -1.573 1.00 49.62  ? 59  ILE   A CG1 1 
ATOM   450  C CG2 . ILE   A 1 59  ? -9.309  16.791  -1.074 1.00 48.88  ? 59  ILE   A CG2 1 
ATOM   451  C CD1 . ILE   A 1 59  ? -6.494  15.744  -2.713 1.00 59.50  ? 59  ILE   A CD1 1 
ATOM   452  N N   . ARG   A 1 60  ? -9.619  16.126  2.149  1.00 52.11  ? 60  ARG   A N   1 
ATOM   453  C CA  . ARG   A 1 60  ? -10.734 16.526  2.997  1.00 60.02  ? 60  ARG   A CA  1 
ATOM   454  C C   . ARG   A 1 60  ? -10.287 17.124  4.328  1.00 61.88  ? 60  ARG   A C   1 
ATOM   455  O O   . ARG   A 1 60  ? -11.139 17.606  5.085  1.00 54.31  ? 60  ARG   A O   1 
ATOM   456  C CB  . ARG   A 1 60  ? -11.658 15.331  3.246  1.00 61.76  ? 60  ARG   A CB  1 
ATOM   457  C CG  . ARG   A 1 60  ? -12.563 14.981  2.070  1.00 68.39  ? 60  ARG   A CG  1 
ATOM   458  C CD  . ARG   A 1 60  ? -13.493 13.825  2.414  1.00 70.50  ? 60  ARG   A CD  1 
ATOM   459  N NE  . ARG   A 1 60  ? -13.848 13.840  3.828  1.00 76.37  ? 60  ARG   A NE  1 
ATOM   460  C CZ  . ARG   A 1 60  ? -14.826 14.566  4.353  1.00 75.79  ? 60  ARG   A CZ  1 
ATOM   461  N NH1 . ARG   A 1 60  ? -15.610 15.319  3.598  1.00 66.94  ? 60  ARG   A NH1 1 
ATOM   462  N NH2 . ARG   A 1 60  ? -15.015 14.544  5.670  1.00 78.08  ? 60  ARG   A NH2 1 
ATOM   463  N N   . LYS   A 1 61  ? -8.994  17.115  4.637  1.00 60.60  ? 61  LYS   A N   1 
ATOM   464  C CA  . LYS   A 1 61  ? -8.494  17.673  5.885  1.00 61.60  ? 61  LYS   A CA  1 
ATOM   465  C C   . LYS   A 1 61  ? -7.977  19.089  5.671  1.00 62.48  ? 61  LYS   A C   1 
ATOM   466  O O   . LYS   A 1 61  ? -7.365  19.393  4.642  1.00 59.53  ? 61  LYS   A O   1 
ATOM   467  C CB  . LYS   A 1 61  ? -7.391  16.792  6.467  1.00 56.24  ? 61  LYS   A CB  1 
ATOM   468  C CG  . LYS   A 1 61  ? -7.900  15.463  6.977  1.00 51.93  ? 61  LYS   A CG  1 
ATOM   469  C CD  . LYS   A 1 61  ? -8.840  15.678  8.141  1.00 50.57  ? 61  LYS   A CD  1 
ATOM   470  C CE  . LYS   A 1 61  ? -9.346  14.363  8.691  1.00 56.88  ? 61  LYS   A CE  1 
ATOM   471  N NZ  . LYS   A 1 61  ? -10.276 14.587  9.830  1.00 66.79  ? 61  LYS   A NZ  1 
ATOM   472  N N   . SER   A 1 62  ? -8.236  19.950  6.646  1.00 57.22  ? 62  SER   A N   1 
ATOM   473  C CA  . SER   A 1 62  ? -7.754  21.321  6.646  1.00 67.39  ? 62  SER   A CA  1 
ATOM   474  C C   . SER   A 1 62  ? -6.638  21.468  7.672  1.00 65.96  ? 62  SER   A C   1 
ATOM   475  O O   . SER   A 1 62  ? -6.412  20.590  8.508  1.00 69.63  ? 62  SER   A O   1 
ATOM   476  C CB  . SER   A 1 62  ? -8.895  22.299  6.947  1.00 69.49  ? 62  SER   A CB  1 
ATOM   477  O OG  . SER   A 1 62  ? -9.977  22.121  6.044  1.00 72.10  ? 62  SER   A OG  1 
ATOM   478  N N   . ASN   A 1 63  ? -5.929  22.598  7.591  1.00 71.39  ? 63  ASN   A N   1 
ATOM   479  C CA  . ASN   A 1 63  ? -4.865  22.872  8.554  1.00 69.70  ? 63  ASN   A CA  1 
ATOM   480  C C   . ASN   A 1 63  ? -5.401  22.879  9.980  1.00 71.05  ? 63  ASN   A C   1 
ATOM   481  O O   . ASN   A 1 63  ? -4.742  22.387  10.903 1.00 68.81  ? 63  ASN   A O   1 
ATOM   482  C CB  . ASN   A 1 63  ? -4.191  24.206  8.235  1.00 69.22  ? 63  ASN   A CB  1 
ATOM   483  C CG  . ASN   A 1 63  ? -3.284  24.130  7.026  1.00 70.91  ? 63  ASN   A CG  1 
ATOM   484  O OD1 . ASN   A 1 63  ? -2.604  23.128  6.807  1.00 71.56  ? 63  ASN   A OD1 1 
ATOM   485  N ND2 . ASN   A 1 63  ? -3.263  25.196  6.235  1.00 77.70  ? 63  ASN   A ND2 1 
ATOM   486  N N   . HIS   A 1 64  ? -6.602  23.420  10.176 1.00 74.52  ? 64  HIS   A N   1 
ATOM   487  C CA  . HIS   A 1 64  ? -7.190  23.520  11.505 1.00 71.03  ? 64  HIS   A CA  1 
ATOM   488  C C   . HIS   A 1 64  ? -7.704  22.189  12.040 1.00 68.01  ? 64  HIS   A C   1 
ATOM   489  O O   . HIS   A 1 64  ? -8.146  22.139  13.192 1.00 68.70  ? 64  HIS   A O   1 
ATOM   490  C CB  . HIS   A 1 64  ? -8.326  24.547  11.500 1.00 77.00  ? 64  HIS   A CB  1 
ATOM   491  C CG  . HIS   A 1 64  ? -9.447  24.207  10.568 1.00 77.67  ? 64  HIS   A CG  1 
ATOM   492  N ND1 . HIS   A 1 64  ? -10.379 23.230  10.850 1.00 74.90  ? 64  HIS   A ND1 1 
ATOM   493  C CD2 . HIS   A 1 64  ? -9.787  24.715  9.360  1.00 68.55  ? 64  HIS   A CD2 1 
ATOM   494  C CE1 . HIS   A 1 64  ? -11.243 23.150  9.855  1.00 73.34  ? 64  HIS   A CE1 1 
ATOM   495  N NE2 . HIS   A 1 64  ? -10.907 24.040  8.938  1.00 75.14  ? 64  HIS   A NE2 1 
ATOM   496  N N   . ASN   A 1 65  ? -7.671  21.118  11.248 1.00 71.50  ? 65  ASN   A N   1 
ATOM   497  C CA  . ASN   A 1 65  ? -8.082  19.811  11.742 1.00 70.46  ? 65  ASN   A CA  1 
ATOM   498  C C   . ASN   A 1 65  ? -6.971  19.080  12.485 1.00 68.01  ? 65  ASN   A C   1 
ATOM   499  O O   . ASN   A 1 65  ? -7.227  18.013  13.056 1.00 63.01  ? 65  ASN   A O   1 
ATOM   500  C CB  . ASN   A 1 65  ? -8.582  18.927  10.591 1.00 72.35  ? 65  ASN   A CB  1 
ATOM   501  C CG  . ASN   A 1 65  ? -9.912  19.392  10.028 1.00 73.19  ? 65  ASN   A CG  1 
ATOM   502  O OD1 . ASN   A 1 65  ? -10.042 19.617  8.824  1.00 69.66  ? 65  ASN   A OD1 1 
ATOM   503  N ND2 . ASN   A 1 65  ? -10.909 19.536  10.896 1.00 75.33  ? 65  ASN   A ND2 1 
ATOM   504  N N   . PHE   A 1 66  ? -5.756  19.624  12.501 1.00 63.85  ? 66  PHE   A N   1 
ATOM   505  C CA  . PHE   A 1 66  ? -4.612  18.996  13.153 1.00 64.08  ? 66  PHE   A CA  1 
ATOM   506  C C   . PHE   A 1 66  ? -4.254  19.782  14.409 1.00 63.57  ? 66  PHE   A C   1 
ATOM   507  O O   . PHE   A 1 66  ? -3.989  20.987  14.336 1.00 63.11  ? 66  PHE   A O   1 
ATOM   508  C CB  . PHE   A 1 66  ? -3.415  18.923  12.204 1.00 61.98  ? 66  PHE   A CB  1 
ATOM   509  C CG  . PHE   A 1 66  ? -3.660  18.094  10.969 1.00 62.83  ? 66  PHE   A CG  1 
ATOM   510  C CD1 . PHE   A 1 66  ? -3.841  16.721  11.061 1.00 62.01  ? 66  PHE   A CD1 1 
ATOM   511  C CD2 . PHE   A 1 66  ? -3.684  18.684  9.712  1.00 55.09  ? 66  PHE   A CD2 1 
ATOM   512  C CE1 . PHE   A 1 66  ? -4.057  15.955  9.926  1.00 55.99  ? 66  PHE   A CE1 1 
ATOM   513  C CE2 . PHE   A 1 66  ? -3.895  17.923  8.574  1.00 60.17  ? 66  PHE   A CE2 1 
ATOM   514  C CZ  . PHE   A 1 66  ? -4.082  16.556  8.681  1.00 63.20  ? 66  PHE   A CZ  1 
ATOM   515  N N   . LEU   A 1 67  ? -4.241  19.099  15.554 1.00 66.09  ? 67  LEU   A N   1 
ATOM   516  C CA  . LEU   A 1 67  ? -3.915  19.705  16.842 1.00 65.33  ? 67  LEU   A CA  1 
ATOM   517  C C   . LEU   A 1 67  ? -2.563  19.178  17.304 1.00 61.25  ? 67  LEU   A C   1 
ATOM   518  O O   . LEU   A 1 67  ? -2.447  18.010  17.688 1.00 59.63  ? 67  LEU   A O   1 
ATOM   519  C CB  . LEU   A 1 67  ? -4.997  19.404  17.876 1.00 69.65  ? 67  LEU   A CB  1 
ATOM   520  C CG  . LEU   A 1 67  ? -6.403  19.865  17.495 1.00 76.02  ? 67  LEU   A CG  1 
ATOM   521  C CD1 . LEU   A 1 67  ? -7.376  19.687  18.651 1.00 71.57  ? 67  LEU   A CD1 1 
ATOM   522  C CD2 . LEU   A 1 67  ? -6.359  21.309  17.031 1.00 72.91  ? 67  LEU   A CD2 1 
ATOM   523  N N   . VAL   A 1 68  ? -1.549  20.040  17.270 1.00 62.07  ? 68  VAL   A N   1 
ATOM   524  C CA  . VAL   A 1 68  ? -0.209  19.716  17.746 1.00 62.29  ? 68  VAL   A CA  1 
ATOM   525  C C   . VAL   A 1 68  ? 0.009   20.416  19.079 1.00 68.25  ? 68  VAL   A C   1 
ATOM   526  O O   . VAL   A 1 68  ? -0.169  21.636  19.185 1.00 65.92  ? 68  VAL   A O   1 
ATOM   527  C CB  . VAL   A 1 68  ? 0.869   20.129  16.731 1.00 63.28  ? 68  VAL   A CB  1 
ATOM   528  C CG1 . VAL   A 1 68  ? 2.254   19.822  17.283 1.00 56.42  ? 68  VAL   A CG1 1 
ATOM   529  C CG2 . VAL   A 1 68  ? 0.646   19.418  15.405 1.00 62.32  ? 68  VAL   A CG2 1 
ATOM   530  N N   . GLN   A 1 69  ? 0.402   19.647  20.091 1.00 62.52  ? 69  GLN   A N   1 
ATOM   531  C CA  . GLN   A 1 69  ? 0.584   20.158  21.446 1.00 64.15  ? 69  GLN   A CA  1 
ATOM   532  C C   . GLN   A 1 69  ? 1.962   19.746  21.946 1.00 64.64  ? 69  GLN   A C   1 
ATOM   533  O O   . GLN   A 1 69  ? 2.225   18.555  22.139 1.00 59.00  ? 69  GLN   A O   1 
ATOM   534  C CB  . GLN   A 1 69  ? -0.515  19.638  22.372 1.00 64.54  ? 69  GLN   A CB  1 
ATOM   535  C CG  . GLN   A 1 69  ? -0.569  20.302  23.729 1.00 70.41  ? 69  GLN   A CG  1 
ATOM   536  C CD  . GLN   A 1 69  ? -1.885  20.043  24.432 1.00 75.42  ? 69  GLN   A CD  1 
ATOM   537  O OE1 . GLN   A 1 69  ? -2.882  19.699  23.795 1.00 70.18  ? 69  GLN   A OE1 1 
ATOM   538  N NE2 . GLN   A 1 69  ? -1.896  20.201  25.750 1.00 80.91  ? 69  GLN   A NE2 1 
ATOM   539  N N   . ALA   A 1 70  ? 2.841   20.724  22.146 1.00 66.82  ? 70  ALA   A N   1 
ATOM   540  C CA  . ALA   A 1 70  ? 4.162   20.495  22.726 1.00 62.46  ? 70  ALA   A CA  1 
ATOM   541  C C   . ALA   A 1 70  ? 4.069   20.816  24.212 1.00 64.05  ? 70  ALA   A C   1 
ATOM   542  O O   . ALA   A 1 70  ? 4.151   21.979  24.614 1.00 64.76  ? 70  ALA   A O   1 
ATOM   543  C CB  . ALA   A 1 70  ? 5.222   21.344  22.032 1.00 60.26  ? 70  ALA   A CB  1 
ATOM   544  N N   . GLY   A 1 71  ? 3.899   19.783  25.031 1.00 58.53  ? 71  GLY   A N   1 
ATOM   545  C CA  . GLY   A 1 71  ? 3.705   19.998  26.450 1.00 71.62  ? 71  GLY   A CA  1 
ATOM   546  C C   . GLY   A 1 71  ? 2.422   20.752  26.732 1.00 74.99  ? 71  GLY   A C   1 
ATOM   547  O O   . GLY   A 1 71  ? 1.337   20.164  26.717 1.00 76.18  ? 71  GLY   A O   1 
ATOM   548  N N   . ASN   A 1 72  ? 2.526   22.056  26.983 1.00 73.80  ? 72  ASN   A N   1 
ATOM   549  C CA  . ASN   A 1 72  ? 1.353   22.887  27.210 1.00 74.72  ? 72  ASN   A CA  1 
ATOM   550  C C   . ASN   A 1 72  ? 1.221   24.016  26.200 1.00 80.60  ? 72  ASN   A C   1 
ATOM   551  O O   . ASN   A 1 72  ? 0.245   24.774  26.264 1.00 85.72  ? 72  ASN   A O   1 
ATOM   552  C CB  . ASN   A 1 72  ? 1.376   23.470  28.630 1.00 72.88  ? 72  ASN   A CB  1 
ATOM   553  N N   . VAL   A 1 73  ? 2.163   24.149  25.274 1.00 73.76  ? 73  VAL   A N   1 
ATOM   554  C CA  . VAL   A 1 73  ? 2.143   25.208  24.276 1.00 75.26  ? 73  VAL   A CA  1 
ATOM   555  C C   . VAL   A 1 73  ? 1.587   24.618  22.986 1.00 80.18  ? 73  VAL   A C   1 
ATOM   556  O O   . VAL   A 1 73  ? 2.137   23.648  22.449 1.00 78.95  ? 73  VAL   A O   1 
ATOM   557  C CB  . VAL   A 1 73  ? 3.544   25.809  24.074 1.00 71.85  ? 73  VAL   A CB  1 
ATOM   558  C CG1 . VAL   A 1 73  ? 3.486   27.016  23.150 1.00 68.61  ? 73  VAL   A CG1 1 
ATOM   559  C CG2 . VAL   A 1 73  ? 4.141   26.191  25.420 1.00 69.93  ? 73  VAL   A CG2 1 
ATOM   560  N N   . GLN   A 1 74  ? 0.483   25.185  22.503 1.00 78.77  ? 74  GLN   A N   1 
ATOM   561  C CA  . GLN   A 1 74  ? -0.118  24.745  21.252 1.00 75.66  ? 74  GLN   A CA  1 
ATOM   562  C C   . GLN   A 1 74  ? 0.681   25.295  20.082 1.00 76.20  ? 74  GLN   A C   1 
ATOM   563  O O   . GLN   A 1 74  ? 0.911   26.505  19.994 1.00 79.01  ? 74  GLN   A O   1 
ATOM   564  C CB  . GLN   A 1 74  ? -1.568  25.218  21.154 1.00 75.64  ? 74  GLN   A CB  1 
ATOM   565  C CG  . GLN   A 1 74  ? -2.367  25.052  22.427 1.00 83.72  ? 74  GLN   A CG  1 
ATOM   566  C CD  . GLN   A 1 74  ? -2.309  23.638  22.957 1.00 84.92  ? 74  GLN   A CD  1 
ATOM   567  O OE1 . GLN   A 1 74  ? -1.535  23.336  23.866 1.00 86.24  ? 74  GLN   A OE1 1 
ATOM   568  N NE2 . GLN   A 1 74  ? -3.124  22.758  22.386 1.00 80.73  ? 74  GLN   A NE2 1 
ATOM   569  N N   . LEU   A 1 75  ? 1.100   24.416  19.180 1.00 71.48  ? 75  LEU   A N   1 
ATOM   570  C CA  . LEU   A 1 75  ? 1.771   24.833  17.958 1.00 67.74  ? 75  LEU   A CA  1 
ATOM   571  C C   . LEU   A 1 75  ? 0.744   24.918  16.837 1.00 76.22  ? 75  LEU   A C   1 
ATOM   572  O O   . LEU   A 1 75  ? -0.020  23.971  16.615 1.00 71.66  ? 75  LEU   A O   1 
ATOM   573  C CB  . LEU   A 1 75  ? 2.899   23.869  17.587 1.00 67.27  ? 75  LEU   A CB  1 
ATOM   574  N N   . ARG   A 1 76  ? 0.715   26.057  16.148 1.00 74.90  ? 76  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 76  ? -0.274  26.286  15.103 1.00 73.18  ? 76  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 76  ? 0.201   25.691  13.784 1.00 70.68  ? 76  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 76  ? 1.317   25.966  13.335 1.00 72.40  ? 76  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 76  ? -0.550  27.782  14.942 1.00 66.87  ? 76  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 76  ? -1.952  28.178  15.382 1.00 73.52  ? 76  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 76  ? -2.611  29.161  14.423 1.00 74.34  ? 76  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 76  ? -2.295  30.539  14.776 1.00 83.86  ? 76  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 76  ? -2.559  31.593  14.015 1.00 81.72  ? 76  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 76  ? -3.172  31.470  12.848 1.00 76.51  ? 76  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 76  ? -2.190  32.801  14.432 1.00 79.56  ? 76  ARG   A NH2 1 
ATOM   585  N N   . VAL   A 1 77  ? -0.649  24.878  13.163 1.00 71.48  ? 77  VAL   A N   1 
ATOM   586  C CA  . VAL   A 1 77  ? -0.319  24.263  11.881 1.00 69.38  ? 77  VAL   A CA  1 
ATOM   587  C C   . VAL   A 1 77  ? -0.579  25.267  10.768 1.00 69.45  ? 77  VAL   A C   1 
ATOM   588  O O   . VAL   A 1 77  ? -1.673  25.834  10.669 1.00 73.15  ? 77  VAL   A O   1 
ATOM   589  C CB  . VAL   A 1 77  ? -1.130  22.978  11.664 1.00 63.43  ? 77  VAL   A CB  1 
ATOM   590  C CG1 . VAL   A 1 77  ? -0.783  22.367  10.316 1.00 64.92  ? 77  VAL   A CG1 1 
ATOM   591  C CG2 . VAL   A 1 77  ? -0.865  21.988  12.783 1.00 66.09  ? 77  VAL   A CG2 1 
ATOM   592  N N   . ILE   A 1 78  ? 0.428   25.486  9.923  1.00 71.69  ? 78  ILE   A N   1 
ATOM   593  C CA  . ILE   A 1 78  ? 0.340   26.426  8.815  1.00 70.27  ? 78  ILE   A CA  1 
ATOM   594  C C   . ILE   A 1 78  ? 0.526   25.742  7.467  1.00 72.16  ? 78  ILE   A C   1 
ATOM   595  O O   . ILE   A 1 78  ? 0.621   26.420  6.441  1.00 74.01  ? 78  ILE   A O   1 
ATOM   596  C CB  . ILE   A 1 78  ? 1.349   27.579  8.982  1.00 71.95  ? 78  ILE   A CB  1 
ATOM   597  C CG1 . ILE   A 1 78  ? 2.787   27.059  8.875  1.00 70.25  ? 78  ILE   A CG1 1 
ATOM   598  C CG2 . ILE   A 1 78  ? 1.133   28.283  10.313 1.00 65.71  ? 78  ILE   A CG2 1 
ATOM   599  C CD1 . ILE   A 1 78  ? 3.843   28.148  8.999  1.00 64.74  ? 78  ILE   A CD1 1 
ATOM   600  N N   . GLY   A 1 79  ? 0.580   24.414  7.446  1.00 70.45  ? 79  GLY   A N   1 
ATOM   601  C CA  . GLY   A 1 79  ? 0.787   23.675  6.217  1.00 73.88  ? 79  GLY   A CA  1 
ATOM   602  C C   . GLY   A 1 79  ? 0.843   22.180  6.452  1.00 72.45  ? 79  GLY   A C   1 
ATOM   603  O O   . GLY   A 1 79  ? 1.335   21.725  7.490  1.00 75.11  ? 79  GLY   A O   1 
ATOM   604  N N   . HIS   A 1 80  ? 0.336   21.404  5.499  1.00 70.77  ? 80  HIS   A N   1 
ATOM   605  C CA  . HIS   A 1 80  ? 0.305   19.955  5.633  1.00 63.08  ? 80  HIS   A CA  1 
ATOM   606  C C   . HIS   A 1 80  ? 0.434   19.331  4.255  1.00 68.66  ? 80  HIS   A C   1 
ATOM   607  O O   . HIS   A 1 80  ? -0.286  19.713  3.327  1.00 67.12  ? 80  HIS   A O   1 
ATOM   608  C CB  . HIS   A 1 80  ? -0.991  19.484  6.303  1.00 63.26  ? 80  HIS   A CB  1 
ATOM   609  C CG  . HIS   A 1 80  ? -2.218  19.719  5.475  1.00 73.12  ? 80  HIS   A CG  1 
ATOM   610  N ND1 . HIS   A 1 80  ? -2.878  20.928  5.448  1.00 75.19  ? 80  HIS   A ND1 1 
ATOM   611  C CD2 . HIS   A 1 80  ? -2.896  18.902  4.633  1.00 72.10  ? 80  HIS   A CD2 1 
ATOM   612  C CE1 . HIS   A 1 80  ? -3.913  20.846  4.630  1.00 74.21  ? 80  HIS   A CE1 1 
ATOM   613  N NE2 . HIS   A 1 80  ? -3.946  19.627  4.122  1.00 76.31  ? 80  HIS   A NE2 1 
ATOM   614  N N   . SER   A 1 81  ? 1.355   18.384  4.124  1.00 61.98  ? 81  SER   A N   1 
ATOM   615  C CA  . SER   A 1 81  ? 1.433   17.576  2.920  1.00 57.77  ? 81  SER   A CA  1 
ATOM   616  C C   . SER   A 1 81  ? 1.841   16.169  3.323  1.00 57.63  ? 81  SER   A C   1 
ATOM   617  O O   . SER   A 1 81  ? 2.068   15.877  4.501  1.00 51.87  ? 81  SER   A O   1 
ATOM   618  C CB  . SER   A 1 81  ? 2.400   18.173  1.893  1.00 65.68  ? 81  SER   A CB  1 
ATOM   619  O OG  . SER   A 1 81  ? 3.750   18.040  2.308  1.00 72.84  ? 81  SER   A OG  1 
ATOM   620  N N   . MET   A 1 82  ? 1.911   15.291  2.330  1.00 50.87  ? 82  MET   A N   1 
ATOM   621  C CA  . MET   A 1 82  ? 2.138   13.873  2.554  1.00 47.09  ? 82  MET   A CA  1 
ATOM   622  C C   . MET   A 1 82  ? 3.384   13.451  1.794  1.00 48.18  ? 82  MET   A C   1 
ATOM   623  O O   . MET   A 1 82  ? 3.450   13.603  0.571  1.00 50.78  ? 82  MET   A O   1 
ATOM   624  C CB  . MET   A 1 82  ? 0.928   13.057  2.103  1.00 46.12  ? 82  MET   A CB  1 
ATOM   625  C CG  . MET   A 1 82  ? 0.870   11.651  2.647  1.00 46.54  ? 82  MET   A CG  1 
ATOM   626  S SD  . MET   A 1 82  ? -0.762  10.965  2.322  1.00 59.90  ? 82  MET   A SD  1 
ATOM   627  C CE  . MET   A 1 82  ? -0.837  11.161  0.544  1.00 50.99  ? 82  MET   A CE  1 
ATOM   628  N N   . GLN   A 1 83  ? 4.365   12.932  2.518  1.00 44.06  ? 83  GLN   A N   1 
ATOM   629  C CA  . GLN   A 1 83  ? 5.553   12.336  1.922  1.00 46.45  ? 83  GLN   A CA  1 
ATOM   630  C C   . GLN   A 1 83  ? 5.484   10.846  2.225  1.00 42.64  ? 83  GLN   A C   1 
ATOM   631  O O   . GLN   A 1 83  ? 5.752   10.423  3.354  1.00 41.31  ? 83  GLN   A O   1 
ATOM   632  C CB  . GLN   A 1 83  ? 6.825   12.969  2.469  1.00 44.13  ? 83  GLN   A CB  1 
ATOM   633  C CG  . GLN   A 1 83  ? 8.091   12.466  1.800  1.00 51.79  ? 83  GLN   A CG  1 
ATOM   634  C CD  . GLN   A 1 83  ? 9.335   13.090  2.392  1.00 56.81  ? 83  GLN   A CD  1 
ATOM   635  O OE1 . GLN   A 1 83  ? 9.256   13.869  3.343  1.00 65.10  ? 83  GLN   A OE1 1 
ATOM   636  N NE2 . GLN   A 1 83  ? 10.492  12.755  1.833  1.00 54.64  ? 83  GLN   A NE2 1 
ATOM   637  N N   . ASN   A 1 84  ? 5.106   10.057  1.220  1.00 35.48  ? 84  ASN   A N   1 
ATOM   638  C CA  . ASN   A 1 84  ? 4.937   8.610   1.366  1.00 36.72  ? 84  ASN   A CA  1 
ATOM   639  C C   . ASN   A 1 84  ? 3.959   8.382   2.512  1.00 37.10  ? 84  ASN   A C   1 
ATOM   640  O O   . ASN   A 1 84  ? 2.833   8.908   2.444  1.00 37.87  ? 84  ASN   A O   1 
ATOM   641  C CB  . ASN   A 1 84  ? 6.321   7.975   1.508  1.00 36.08  ? 84  ASN   A CB  1 
ATOM   642  C CG  . ASN   A 1 84  ? 7.190   8.193   0.274  1.00 47.46  ? 84  ASN   A CG  1 
ATOM   643  O OD1 . ASN   A 1 84  ? 6.763   7.932   -0.854 1.00 40.67  ? 84  ASN   A OD1 1 
ATOM   644  N ND2 . ASN   A 1 84  ? 8.407   8.689   0.484  1.00 40.19  ? 84  ASN   A ND2 1 
ATOM   645  N N   . CYS   A 1 85  ? 4.323   7.666   3.576  1.00 36.21  ? 85  CYS   A N   1 
ATOM   646  C CA  . CYS   A 1 85  ? 3.382   7.338   4.639  1.00 38.54  ? 85  CYS   A CA  1 
ATOM   647  C C   . CYS   A 1 85  ? 3.533   8.215   5.875  1.00 41.78  ? 85  CYS   A C   1 
ATOM   648  O O   . CYS   A 1 85  ? 2.943   7.901   6.914  1.00 40.46  ? 85  CYS   A O   1 
ATOM   649  C CB  . CYS   A 1 85  ? 3.514   5.867   5.035  1.00 38.65  ? 85  CYS   A CB  1 
ATOM   650  S SG  . CYS   A 1 85  ? 3.164   4.709   3.689  1.00 41.10  ? 85  CYS   A SG  1 
ATOM   651  N N   . VAL   A 1 86  ? 4.298   9.302   5.800  1.00 34.08  ? 86  VAL   A N   1 
ATOM   652  C CA  . VAL   A 1 86  ? 4.389   10.238  6.913  1.00 40.79  ? 86  VAL   A CA  1 
ATOM   653  C C   . VAL   A 1 86  ? 3.672   11.520  6.537  1.00 39.67  ? 86  VAL   A C   1 
ATOM   654  O O   . VAL   A 1 86  ? 3.671   11.958  5.381  1.00 41.35  ? 86  VAL   A O   1 
ATOM   655  C CB  . VAL   A 1 86  ? 5.835   10.554  7.357  1.00 37.68  ? 86  VAL   A CB  1 
ATOM   656  C CG1 . VAL   A 1 86  ? 6.539   9.295   7.796  1.00 49.29  ? 86  VAL   A CG1 1 
ATOM   657  C CG2 . VAL   A 1 86  ? 6.609   11.251  6.259  1.00 49.75  ? 86  VAL   A CG2 1 
ATOM   658  N N   . LEU   A 1 87  ? 3.047   12.114  7.538  1.00 39.13  ? 87  LEU   A N   1 
ATOM   659  C CA  . LEU   A 1 87  ? 2.428   13.421  7.424  1.00 50.09  ? 87  LEU   A CA  1 
ATOM   660  C C   . LEU   A 1 87  ? 3.362   14.449  8.048  1.00 53.98  ? 87  LEU   A C   1 
ATOM   661  O O   . LEU   A 1 87  ? 3.758   14.303  9.211  1.00 45.12  ? 87  LEU   A O   1 
ATOM   662  C CB  . LEU   A 1 87  ? 1.070   13.420  8.124  1.00 43.95  ? 87  LEU   A CB  1 
ATOM   663  C CG  . LEU   A 1 87  ? 0.264   14.714  8.147  1.00 50.86  ? 87  LEU   A CG  1 
ATOM   664  C CD1 . LEU   A 1 87  ? -0.164  15.083  6.739  1.00 52.78  ? 87  LEU   A CD1 1 
ATOM   665  C CD2 . LEU   A 1 87  ? -0.934  14.534  9.055  1.00 49.99  ? 87  LEU   A CD2 1 
ATOM   666  N N   . LYS   A 1 88  ? 3.736   15.467  7.270  1.00 48.41  ? 88  LYS   A N   1 
ATOM   667  C CA  . LYS   A 1 88  ? 4.576   16.563  7.746  1.00 43.61  ? 88  LYS   A CA  1 
ATOM   668  C C   . LYS   A 1 88  ? 3.691   17.787  7.957  1.00 53.88  ? 88  LYS   A C   1 
ATOM   669  O O   . LYS   A 1 88  ? 3.212   18.385  6.988  1.00 56.11  ? 88  LYS   A O   1 
ATOM   670  C CB  . LYS   A 1 88  ? 5.702   16.870  6.760  1.00 48.77  ? 88  LYS   A CB  1 
ATOM   671  C CG  . LYS   A 1 88  ? 6.432   15.638  6.240  1.00 53.19  ? 88  LYS   A CG  1 
ATOM   672  C CD  . LYS   A 1 88  ? 7.672   16.006  5.432  1.00 54.88  ? 88  LYS   A CD  1 
ATOM   673  C CE  . LYS   A 1 88  ? 7.324   16.778  4.169  1.00 51.18  ? 88  LYS   A CE  1 
ATOM   674  N NZ  . LYS   A 1 88  ? 8.540   17.158  3.394  1.00 56.98  ? 88  LYS   A NZ  1 
ATOM   675  N N   . LEU   A 1 89  ? 3.486   18.164  9.221  1.00 48.97  ? 89  LEU   A N   1 
ATOM   676  C CA  . LEU   A 1 89  ? 2.683   19.326  9.590  1.00 49.49  ? 89  LEU   A CA  1 
ATOM   677  C C   . LEU   A 1 89  ? 3.608   20.512  9.844  1.00 59.40  ? 89  LEU   A C   1 
ATOM   678  O O   . LEU   A 1 89  ? 4.296   20.560  10.869 1.00 45.24  ? 89  LEU   A O   1 
ATOM   679  C CB  . LEU   A 1 89  ? 1.847   19.029  10.830 1.00 45.45  ? 89  LEU   A CB  1 
ATOM   680  C CG  . LEU   A 1 89  ? 0.884   17.857  10.731 1.00 49.59  ? 89  LEU   A CG  1 
ATOM   681  C CD1 . LEU   A 1 89  ? 0.226   17.589  12.073 1.00 52.52  ? 89  LEU   A CD1 1 
ATOM   682  C CD2 . LEU   A 1 89  ? -0.145  18.180  9.677  1.00 50.68  ? 89  LEU   A CD2 1 
ATOM   683  N N   . LYS   A 1 90  ? 3.611   21.479  8.929  1.00 56.64  ? 90  LYS   A N   1 
ATOM   684  C CA  . LYS   A 1 90  ? 4.436   22.668  9.117  1.00 52.98  ? 90  LYS   A CA  1 
ATOM   685  C C   . LYS   A 1 90  ? 3.817   23.567  10.182 1.00 64.88  ? 90  LYS   A C   1 
ATOM   686  O O   . LYS   A 1 90  ? 2.627   23.891  10.118 1.00 70.30  ? 90  LYS   A O   1 
ATOM   687  C CB  . LYS   A 1 90  ? 4.594   23.425  7.796  1.00 59.85  ? 90  LYS   A CB  1 
ATOM   688  C CG  . LYS   A 1 90  ? 5.661   24.519  7.806  1.00 65.53  ? 90  LYS   A CG  1 
ATOM   689  C CD  . LYS   A 1 90  ? 6.013   24.941  6.383  1.00 70.13  ? 90  LYS   A CD  1 
ATOM   690  C CE  . LYS   A 1 90  ? 7.194   25.903  6.334  1.00 76.60  ? 90  LYS   A CE  1 
ATOM   691  N NZ  . LYS   A 1 90  ? 7.678   26.098  4.932  1.00 70.60  ? 90  LYS   A NZ  1 
ATOM   692  N N   . VAL   A 1 91  ? 4.621   23.961  11.170 1.00 60.54  ? 91  VAL   A N   1 
ATOM   693  C CA  . VAL   A 1 91  ? 4.135   24.739  12.301 1.00 61.58  ? 91  VAL   A CA  1 
ATOM   694  C C   . VAL   A 1 91  ? 4.802   26.109  12.306 1.00 58.57  ? 91  VAL   A C   1 
ATOM   695  O O   . VAL   A 1 91  ? 5.848   26.328  11.691 1.00 58.07  ? 91  VAL   A O   1 
ATOM   696  C CB  . VAL   A 1 91  ? 4.364   24.021  13.649 1.00 61.61  ? 91  VAL   A CB  1 
ATOM   697  C CG1 . VAL   A 1 91  ? 3.416   22.842  13.794 1.00 59.55  ? 91  VAL   A CG1 1 
ATOM   698  C CG2 . VAL   A 1 91  ? 5.814   23.574  13.779 1.00 55.36  ? 91  VAL   A CG2 1 
ATOM   699  N N   . ASP   A 1 92  ? 4.177   27.034  13.035 1.00 67.39  ? 92  ASP   A N   1 
ATOM   700  C CA  . ASP   A 1 92  ? 4.586   28.433  13.073 1.00 70.24  ? 92  ASP   A CA  1 
ATOM   701  C C   . ASP   A 1 92  ? 5.793   28.687  13.968 1.00 74.48  ? 92  ASP   A C   1 
ATOM   702  O O   . ASP   A 1 92  ? 6.242   29.834  14.061 1.00 73.32  ? 92  ASP   A O   1 
ATOM   703  C CB  . ASP   A 1 92  ? 3.418   29.300  13.547 1.00 70.32  ? 92  ASP   A CB  1 
ATOM   704  C CG  . ASP   A 1 92  ? 3.020   29.005  14.982 1.00 75.64  ? 92  ASP   A CG  1 
ATOM   705  O OD1 . ASP   A 1 92  ? 3.231   27.861  15.437 1.00 80.31  ? 92  ASP   A OD1 1 
ATOM   706  O OD2 . ASP   A 1 92  ? 2.500   29.919  15.657 1.00 77.97  ? 92  ASP   A OD2 1 
ATOM   707  N N   . THR   A 1 93  ? 6.326   27.660  14.625 1.00 71.46  ? 93  THR   A N   1 
ATOM   708  C CA  . THR   A 1 93  ? 7.418   27.817  15.574 1.00 63.34  ? 93  THR   A CA  1 
ATOM   709  C C   . THR   A 1 93  ? 8.475   26.760  15.301 1.00 60.38  ? 93  THR   A C   1 
ATOM   710  O O   . THR   A 1 93  ? 8.161   25.566  15.244 1.00 55.47  ? 93  THR   A O   1 
ATOM   711  C CB  . THR   A 1 93  ? 6.919   27.692  17.020 1.00 64.20  ? 93  THR   A CB  1 
ATOM   712  O OG1 . THR   A 1 93  ? 5.922   28.690  17.276 1.00 73.95  ? 93  THR   A OG1 1 
ATOM   713  C CG2 . THR   A 1 93  ? 8.070   27.859  18.006 1.00 57.84  ? 93  THR   A CG2 1 
ATOM   714  N N   . ALA   A 1 94  ? 9.718   27.196  15.121 1.00 60.75  ? 94  ALA   A N   1 
ATOM   715  C CA  . ALA   A 1 94  ? 10.828  26.258  15.067 1.00 49.83  ? 94  ALA   A CA  1 
ATOM   716  C C   . ALA   A 1 94  ? 11.121  25.733  16.467 1.00 52.71  ? 94  ALA   A C   1 
ATOM   717  O O   . ALA   A 1 94  ? 11.089  26.483  17.446 1.00 52.32  ? 94  ALA   A O   1 
ATOM   718  C CB  . ALA   A 1 94  ? 12.070  26.922  14.475 1.00 49.11  ? 94  ALA   A CB  1 
ATOM   719  N N   . ASN   A 1 95  ? 11.380  24.437  16.564 1.00 48.78  ? 95  ASN   A N   1 
ATOM   720  C CA  . ASN   A 1 95  ? 11.683  23.826  17.852 1.00 43.48  ? 95  ASN   A CA  1 
ATOM   721  C C   . ASN   A 1 95  ? 13.020  24.356  18.352 1.00 44.87  ? 95  ASN   A C   1 
ATOM   722  O O   . ASN   A 1 95  ? 14.045  24.132  17.694 1.00 45.32  ? 95  ASN   A O   1 
ATOM   723  C CB  . ASN   A 1 95  ? 11.700  22.299  17.715 1.00 52.83  ? 95  ASN   A CB  1 
ATOM   724  C CG  . ASN   A 1 95  ? 11.925  21.580  19.041 1.00 52.68  ? 95  ASN   A CG  1 
ATOM   725  O OD1 . ASN   A 1 95  ? 11.953  22.196  20.107 1.00 53.95  ? 95  ASN   A OD1 1 
ATOM   726  N ND2 . ASN   A 1 95  ? 12.079  20.260  18.974 1.00 52.15  ? 95  ASN   A ND2 1 
ATOM   727  N N   . PRO   A 1 96  ? 13.062  25.082  19.473 1.00 53.45  ? 96  PRO   A N   1 
ATOM   728  C CA  . PRO   A 1 96  ? 14.355  25.581  19.966 1.00 50.15  ? 96  PRO   A CA  1 
ATOM   729  C C   . PRO   A 1 96  ? 15.263  24.472  20.455 1.00 51.83  ? 96  PRO   A C   1 
ATOM   730  O O   . PRO   A 1 96  ? 16.480  24.677  20.544 1.00 48.03  ? 96  PRO   A O   1 
ATOM   731  C CB  . PRO   A 1 96  ? 13.956  26.522  21.108 1.00 54.52  ? 96  PRO   A CB  1 
ATOM   732  C CG  . PRO   A 1 96  ? 12.650  25.983  21.596 1.00 52.78  ? 96  PRO   A CG  1 
ATOM   733  C CD  . PRO   A 1 96  ? 11.954  25.393  20.395 1.00 46.85  ? 96  PRO   A CD  1 
ATOM   734  N N   . LYS   A 1 97  ? 14.698  23.303  20.758 1.00 54.99  ? 97  LYS   A N   1 
ATOM   735  C CA  . LYS   A 1 97  ? 15.424  22.135  21.233 1.00 51.80  ? 97  LYS   A CA  1 
ATOM   736  C C   . LYS   A 1 97  ? 15.836  21.205  20.102 1.00 51.28  ? 97  LYS   A C   1 
ATOM   737  O O   . LYS   A 1 97  ? 16.197  20.055  20.363 1.00 55.97  ? 97  LYS   A O   1 
ATOM   738  C CB  . LYS   A 1 97  ? 14.565  21.372  22.247 1.00 54.73  ? 97  LYS   A CB  1 
ATOM   739  C CG  . LYS   A 1 97  ? 14.135  22.205  23.449 1.00 55.58  ? 97  LYS   A CG  1 
ATOM   740  C CD  . LYS   A 1 97  ? 13.167  21.460  24.364 1.00 63.23  ? 97  LYS   A CD  1 
ATOM   741  C CE  . LYS   A 1 97  ? 11.815  21.193  23.696 1.00 75.35  ? 97  LYS   A CE  1 
ATOM   742  N NZ  . LYS   A 1 97  ? 11.038  22.426  23.370 1.00 61.28  ? 97  LYS   A NZ  1 
ATOM   743  N N   . THR   A 1 98  ? 15.775  21.666  18.859 1.00 48.94  ? 98  THR   A N   1 
ATOM   744  C CA  . THR   A 1 98  ? 16.136  20.825  17.721 1.00 49.46  ? 98  THR   A CA  1 
ATOM   745  C C   . THR   A 1 98  ? 17.622  20.497  17.762 1.00 51.68  ? 98  THR   A C   1 
ATOM   746  O O   . THR   A 1 98  ? 18.450  21.415  17.686 1.00 48.96  ? 98  THR   A O   1 
ATOM   747  C CB  . THR   A 1 98  ? 15.797  21.517  16.403 1.00 50.21  ? 98  THR   A CB  1 
ATOM   748  O OG1 . THR   A 1 98  ? 14.389  21.748  16.323 1.00 49.47  ? 98  THR   A OG1 1 
ATOM   749  C CG2 . THR   A 1 98  ? 16.235  20.653  15.225 1.00 44.02  ? 98  THR   A CG2 1 
ATOM   750  N N   . PRO   A 1 99  ? 18.007  19.231  17.872 1.00 52.53  ? 99  PRO   A N   1 
ATOM   751  C CA  . PRO   A 1 99  ? 19.425  18.881  17.807 1.00 48.57  ? 99  PRO   A CA  1 
ATOM   752  C C   . PRO   A 1 99  ? 19.875  18.731  16.362 1.00 47.83  ? 99  PRO   A C   1 
ATOM   753  O O   . PRO   A 1 99  ? 19.070  18.672  15.431 1.00 51.29  ? 99  PRO   A O   1 
ATOM   754  C CB  . PRO   A 1 99  ? 19.482  17.543  18.541 1.00 52.24  ? 99  PRO   A CB  1 
ATOM   755  C CG  . PRO   A 1 99  ? 18.175  16.913  18.197 1.00 51.02  ? 99  PRO   A CG  1 
ATOM   756  C CD  . PRO   A 1 99  ? 17.168  18.046  18.113 1.00 47.10  ? 99  PRO   A CD  1 
ATOM   757  N N   . LYS   A 1 100 ? 21.195  18.678  16.188 1.00 53.70  ? 100 LYS   A N   1 
ATOM   758  C CA  . LYS   A 1 100 ? 21.756  18.252  14.914 1.00 52.41  ? 100 LYS   A CA  1 
ATOM   759  C C   . LYS   A 1 100 ? 21.258  16.846  14.611 1.00 51.13  ? 100 LYS   A C   1 
ATOM   760  O O   . LYS   A 1 100 ? 21.501  15.913  15.383 1.00 51.93  ? 100 LYS   A O   1 
ATOM   761  C CB  . LYS   A 1 100 ? 23.285  18.289  14.963 1.00 50.77  ? 100 LYS   A CB  1 
ATOM   762  C CG  . LYS   A 1 100 ? 23.962  18.106  13.607 1.00 66.95  ? 100 LYS   A CG  1 
ATOM   763  C CD  . LYS   A 1 100 ? 25.482  18.079  13.739 1.00 68.76  ? 100 LYS   A CD  1 
ATOM   764  C CE  . LYS   A 1 100 ? 26.166  18.093  12.378 1.00 70.32  ? 100 LYS   A CE  1 
ATOM   765  N NZ  . LYS   A 1 100 ? 25.832  19.317  11.593 1.00 71.32  ? 100 LYS   A NZ  1 
ATOM   766  N N   . TYR   A 1 101 ? 20.531  16.697  13.510 1.00 48.83  ? 101 TYR   A N   1 
ATOM   767  C CA  . TYR   A 1 101 ? 19.876  15.439  13.196 1.00 48.30  ? 101 TYR   A CA  1 
ATOM   768  C C   . TYR   A 1 101 ? 20.076  15.091  11.729 1.00 44.28  ? 101 TYR   A C   1 
ATOM   769  O O   . TYR   A 1 101 ? 20.475  15.923  10.911 1.00 48.54  ? 101 TYR   A O   1 
ATOM   770  C CB  . TYR   A 1 101 ? 18.375  15.487  13.516 1.00 44.59  ? 101 TYR   A CB  1 
ATOM   771  C CG  . TYR   A 1 101 ? 17.575  16.334  12.553 1.00 48.11  ? 101 TYR   A CG  1 
ATOM   772  C CD1 . TYR   A 1 101 ? 17.407  17.696  12.773 1.00 47.89  ? 101 TYR   A CD1 1 
ATOM   773  C CD2 . TYR   A 1 101 ? 16.991  15.775  11.420 1.00 46.02  ? 101 TYR   A CD2 1 
ATOM   774  C CE1 . TYR   A 1 101 ? 16.679  18.476  11.896 1.00 48.14  ? 101 TYR   A CE1 1 
ATOM   775  C CE2 . TYR   A 1 101 ? 16.265  16.547  10.536 1.00 47.28  ? 101 TYR   A CE2 1 
ATOM   776  C CZ  . TYR   A 1 101 ? 16.110  17.897  10.779 1.00 47.49  ? 101 TYR   A CZ  1 
ATOM   777  O OH  . TYR   A 1 101 ? 15.384  18.669  9.903  1.00 52.97  ? 101 TYR   A OH  1 
ATOM   778  N N   . LYS   A 1 102 ? 19.768  13.836  11.413 1.00 45.25  ? 102 LYS   A N   1 
ATOM   779  C CA  . LYS   A 1 102 ? 19.803  13.314  10.056 1.00 44.73  ? 102 LYS   A CA  1 
ATOM   780  C C   . LYS   A 1 102 ? 18.768  12.202  9.957  1.00 48.20  ? 102 LYS   A C   1 
ATOM   781  O O   . LYS   A 1 102 ? 18.531  11.478  10.929 1.00 46.05  ? 102 LYS   A O   1 
ATOM   782  C CB  . LYS   A 1 102 ? 21.202  12.798  9.692  1.00 46.01  ? 102 LYS   A CB  1 
ATOM   783  C CG  . LYS   A 1 102 ? 21.304  12.101  8.334  1.00 63.43  ? 102 LYS   A CG  1 
ATOM   784  C CD  . LYS   A 1 102 ? 20.811  12.991  7.195  1.00 60.45  ? 102 LYS   A CD  1 
ATOM   785  C CE  . LYS   A 1 102 ? 20.973  12.314  5.834  1.00 68.36  ? 102 LYS   A CE  1 
ATOM   786  N NZ  . LYS   A 1 102 ? 22.403  12.155  5.438  1.00 69.65  ? 102 LYS   A NZ  1 
ATOM   787  N N   . PHE   A 1 103 ? 18.135  12.093  8.792  1.00 44.54  ? 103 PHE   A N   1 
ATOM   788  C CA  . PHE   A 1 103 ? 17.225  10.994  8.498  1.00 46.23  ? 103 PHE   A CA  1 
ATOM   789  C C   . PHE   A 1 103 ? 17.996  9.911   7.758  1.00 46.66  ? 103 PHE   A C   1 
ATOM   790  O O   . PHE   A 1 103 ? 18.554  10.168  6.686  1.00 47.50  ? 103 PHE   A O   1 
ATOM   791  C CB  . PHE   A 1 103 ? 16.042  11.464  7.655  1.00 43.43  ? 103 PHE   A CB  1 
ATOM   792  C CG  . PHE   A 1 103 ? 15.103  12.381  8.378  1.00 39.79  ? 103 PHE   A CG  1 
ATOM   793  C CD1 . PHE   A 1 103 ? 15.163  12.520  9.755  1.00 38.99  ? 103 PHE   A CD1 1 
ATOM   794  C CD2 . PHE   A 1 103 ? 14.150  13.099  7.677  1.00 40.55  ? 103 PHE   A CD2 1 
ATOM   795  C CE1 . PHE   A 1 103 ? 14.292  13.363  10.416 1.00 40.71  ? 103 PHE   A CE1 1 
ATOM   796  C CE2 . PHE   A 1 103 ? 13.277  13.943  8.331  1.00 39.74  ? 103 PHE   A CE2 1 
ATOM   797  C CZ  . PHE   A 1 103 ? 13.347  14.075  9.704  1.00 45.86  ? 103 PHE   A CZ  1 
ATOM   798  N N   . VAL   A 1 104 ? 18.030  8.709   8.325  1.00 39.09  ? 104 VAL   A N   1 
ATOM   799  C CA  . VAL   A 1 104 ? 18.738  7.596   7.708  1.00 41.79  ? 104 VAL   A CA  1 
ATOM   800  C C   . VAL   A 1 104 ? 17.783  6.422   7.560  1.00 41.39  ? 104 VAL   A C   1 
ATOM   801  O O   . VAL   A 1 104 ? 16.830  6.265   8.330  1.00 41.55  ? 104 VAL   A O   1 
ATOM   802  C CB  . VAL   A 1 104 ? 19.989  7.181   8.515  1.00 41.73  ? 104 VAL   A CB  1 
ATOM   803  C CG1 . VAL   A 1 104 ? 20.996  8.320   8.558  1.00 47.26  ? 104 VAL   A CG1 1 
ATOM   804  C CG2 . VAL   A 1 104 ? 19.601  6.749   9.917  1.00 45.23  ? 104 VAL   A CG2 1 
ATOM   805  N N   . ARG   A 1 105 ? 18.041  5.603   6.548  1.00 37.62  ? 105 ARG   A N   1 
ATOM   806  C CA  . ARG   A 1 105 ? 17.346  4.337   6.351  1.00 39.02  ? 105 ARG   A CA  1 
ATOM   807  C C   . ARG   A 1 105 ? 18.344  3.222   6.632  1.00 39.95  ? 105 ARG   A C   1 
ATOM   808  O O   . ARG   A 1 105 ? 19.319  3.057   5.893  1.00 41.98  ? 105 ARG   A O   1 
ATOM   809  C CB  . ARG   A 1 105 ? 16.781  4.231   4.937  1.00 40.52  ? 105 ARG   A CB  1 
ATOM   810  C CG  . ARG   A 1 105 ? 16.119  2.899   4.651  1.00 39.50  ? 105 ARG   A CG  1 
ATOM   811  C CD  . ARG   A 1 105 ? 15.357  2.928   3.341  1.00 46.70  ? 105 ARG   A CD  1 
ATOM   812  N NE  . ARG   A 1 105 ? 14.566  1.718   3.153  1.00 43.45  ? 105 ARG   A NE  1 
ATOM   813  C CZ  . ARG   A 1 105 ? 13.287  1.601   3.482  1.00 44.78  ? 105 ARG   A CZ  1 
ATOM   814  N NH1 . ARG   A 1 105 ? 12.612  2.612   4.005  1.00 41.89  ? 105 ARG   A NH1 1 
ATOM   815  N NH2 . ARG   A 1 105 ? 12.671  0.441   3.282  1.00 37.84  ? 105 ARG   A NH2 1 
ATOM   816  N N   . ILE   A 1 106 ? 18.106  2.465   7.705  1.00 35.04  ? 106 ILE   A N   1 
ATOM   817  C CA  . ILE   A 1 106 ? 19.021  1.404   8.112  1.00 44.45  ? 106 ILE   A CA  1 
ATOM   818  C C   . ILE   A 1 106 ? 18.735  0.136   7.324  1.00 41.83  ? 106 ILE   A C   1 
ATOM   819  O O   . ILE   A 1 106 ? 17.664  -0.012  6.727  1.00 45.30  ? 106 ILE   A O   1 
ATOM   820  C CB  . ILE   A 1 106 ? 18.924  1.110   9.619  1.00 44.77  ? 106 ILE   A CB  1 
ATOM   821  C CG1 . ILE   A 1 106 ? 17.498  0.677   9.970  1.00 44.12  ? 106 ILE   A CG1 1 
ATOM   822  C CG2 . ILE   A 1 106 ? 19.396  2.306   10.438 1.00 50.15  ? 106 ILE   A CG2 1 
ATOM   823  C CD1 . ILE   A 1 106 ? 17.377  0.022   11.312 1.00 44.87  ? 106 ILE   A CD1 1 
ATOM   824  N N   . GLN   A 1 107 ? 19.689  -0.791  7.342  1.00 45.97  ? 107 GLN   A N   1 
ATOM   825  C CA  . GLN   A 1 107 ? 19.632  -2.106  6.727  1.00 42.58  ? 107 GLN   A CA  1 
ATOM   826  C C   . GLN   A 1 107 ? 19.295  -3.163  7.761  1.00 37.53  ? 107 GLN   A C   1 
ATOM   827  O O   . GLN   A 1 107 ? 19.593  -3.001  8.949  1.00 40.10  ? 107 GLN   A O   1 
ATOM   828  C CB  . GLN   A 1 107 ? 20.976  -2.451  6.073  1.00 52.14  ? 107 GLN   A CB  1 
ATOM   829  C CG  . GLN   A 1 107 ? 21.164  -1.864  4.688  1.00 56.51  ? 107 GLN   A CG  1 
ATOM   830  C CD  . GLN   A 1 107 ? 21.311  -0.360  4.719  1.00 64.25  ? 107 GLN   A CD  1 
ATOM   831  O OE1 . GLN   A 1 107 ? 20.669  0.354   3.949  1.00 71.64  ? 107 GLN   A OE1 1 
ATOM   832  N NE2 . GLN   A 1 107 ? 22.163  0.132   5.612  1.00 65.33  ? 107 GLN   A NE2 1 
ATOM   833  N N   . PRO   A 1 108 ? 18.673  -4.266  7.343  1.00 40.63  ? 108 PRO   A N   1 
ATOM   834  C CA  . PRO   A 1 108 ? 18.415  -5.362  8.283  1.00 40.09  ? 108 PRO   A CA  1 
ATOM   835  C C   . PRO   A 1 108 ? 19.701  -5.808  8.958  1.00 41.69  ? 108 PRO   A C   1 
ATOM   836  O O   . PRO   A 1 108 ? 20.758  -5.893  8.330  1.00 44.17  ? 108 PRO   A O   1 
ATOM   837  C CB  . PRO   A 1 108 ? 17.824  -6.467  7.397  1.00 37.18  ? 108 PRO   A CB  1 
ATOM   838  C CG  . PRO   A 1 108 ? 18.170  -6.083  5.989  1.00 46.65  ? 108 PRO   A CG  1 
ATOM   839  C CD  . PRO   A 1 108 ? 18.206  -4.586  5.983  1.00 45.42  ? 108 PRO   A CD  1 
ATOM   840  N N   . GLY   A 1 109 ? 19.607  -6.064  10.264 1.00 34.52  ? 109 GLY   A N   1 
ATOM   841  C CA  . GLY   A 1 109 ? 20.744  -6.403  11.088 1.00 37.01  ? 109 GLY   A CA  1 
ATOM   842  C C   . GLY   A 1 109 ? 21.224  -5.265  11.968 1.00 39.32  ? 109 GLY   A C   1 
ATOM   843  O O   . GLY   A 1 109 ? 21.733  -5.519  13.065 1.00 41.31  ? 109 GLY   A O   1 
ATOM   844  N N   . GLN   A 1 110 ? 21.082  -4.023  11.511 1.00 35.04  ? 110 GLN   A N   1 
ATOM   845  C CA  . GLN   A 1 110 ? 21.503  -2.882  12.311 1.00 42.57  ? 110 GLN   A CA  1 
ATOM   846  C C   . GLN   A 1 110 ? 20.495  -2.607  13.427 1.00 38.22  ? 110 GLN   A C   1 
ATOM   847  O O   . GLN   A 1 110 ? 19.316  -2.961  13.336 1.00 37.08  ? 110 GLN   A O   1 
ATOM   848  C CB  . GLN   A 1 110 ? 21.687  -1.642  11.426 1.00 44.95  ? 110 GLN   A CB  1 
ATOM   849  C CG  . GLN   A 1 110 ? 22.959  -1.682  10.567 1.00 48.79  ? 110 GLN   A CG  1 
ATOM   850  C CD  . GLN   A 1 110 ? 23.073  -0.514  9.592  1.00 56.98  ? 110 GLN   A CD  1 
ATOM   851  O OE1 . GLN   A 1 110 ? 22.085  0.146   9.264  1.00 47.89  ? 110 GLN   A OE1 1 
ATOM   852  N NE2 . GLN   A 1 110 ? 24.289  -0.260  9.120  1.00 68.31  ? 110 GLN   A NE2 1 
ATOM   853  N N   . THR   A 1 111 ? 20.980  -1.984  14.495 1.00 37.94  ? 111 THR   A N   1 
ATOM   854  C CA  . THR   A 1 111 ? 20.197  -1.740  15.695 1.00 41.08  ? 111 THR   A CA  1 
ATOM   855  C C   . THR   A 1 111 ? 19.921  -0.251  15.862 1.00 35.90  ? 111 THR   A C   1 
ATOM   856  O O   . THR   A 1 111 ? 20.527  0.603   15.206 1.00 33.29  ? 111 THR   A O   1 
ATOM   857  C CB  . THR   A 1 111 ? 20.920  -2.284  16.935 1.00 41.95  ? 111 THR   A CB  1 
ATOM   858  O OG1 . THR   A 1 111 ? 22.208  -1.667  17.047 1.00 39.41  ? 111 THR   A OG1 1 
ATOM   859  C CG2 . THR   A 1 111 ? 21.093  -3.793  16.836 1.00 43.61  ? 111 THR   A CG2 1 
ATOM   860  N N   . PHE   A 1 112 ? 18.987  0.051   16.760 1.00 33.84  ? 112 PHE   A N   1 
ATOM   861  C CA  . PHE   A 1 112 ? 18.672  1.431   17.109 1.00 37.90  ? 112 PHE   A CA  1 
ATOM   862  C C   . PHE   A 1 112 ? 17.964  1.446   18.455 1.00 33.50  ? 112 PHE   A C   1 
ATOM   863  O O   . PHE   A 1 112 ? 17.504  0.413   18.946 1.00 32.66  ? 112 PHE   A O   1 
ATOM   864  C CB  . PHE   A 1 112 ? 17.815  2.109   16.033 1.00 31.65  ? 112 PHE   A CB  1 
ATOM   865  C CG  . PHE   A 1 112 ? 16.577  1.339   15.663 1.00 39.38  ? 112 PHE   A CG  1 
ATOM   866  C CD1 . PHE   A 1 112 ? 16.619  0.364   14.680 1.00 38.56  ? 112 PHE   A CD1 1 
ATOM   867  C CD2 . PHE   A 1 112 ? 15.368  1.595   16.294 1.00 36.23  ? 112 PHE   A CD2 1 
ATOM   868  C CE1 . PHE   A 1 112 ? 15.484  -0.347  14.335 1.00 41.84  ? 112 PHE   A CE1 1 
ATOM   869  C CE2 . PHE   A 1 112 ? 14.228  0.887   15.955 1.00 38.25  ? 112 PHE   A CE2 1 
ATOM   870  C CZ  . PHE   A 1 112 ? 14.286  -0.085  14.972 1.00 40.56  ? 112 PHE   A CZ  1 
ATOM   871  N N   . SER   A 1 113 ? 17.902  2.635   19.052 1.00 34.41  ? 113 SER   A N   1 
ATOM   872  C CA  . SER   A 1 113 ? 17.170  2.849   20.292 1.00 35.47  ? 113 SER   A CA  1 
ATOM   873  C C   . SER   A 1 113 ? 15.757  3.315   19.975 1.00 34.77  ? 113 SER   A C   1 
ATOM   874  O O   . SER   A 1 113 ? 15.548  4.115   19.061 1.00 35.04  ? 113 SER   A O   1 
ATOM   875  C CB  . SER   A 1 113 ? 17.867  3.891   21.173 1.00 36.88  ? 113 SER   A CB  1 
ATOM   876  O OG  . SER   A 1 113 ? 19.148  3.459   21.583 1.00 38.42  ? 113 SER   A OG  1 
ATOM   877  N N   . VAL   A 1 114 ? 14.792  2.817   20.741 1.00 34.43  ? 114 VAL   A N   1 
ATOM   878  C CA  . VAL   A 1 114 ? 13.388  3.177   20.589 1.00 26.54  ? 114 VAL   A CA  1 
ATOM   879  C C   . VAL   A 1 114 ? 12.977  4.001   21.798 1.00 34.91  ? 114 VAL   A C   1 
ATOM   880  O O   . VAL   A 1 114 ? 13.202  3.590   22.944 1.00 28.71  ? 114 VAL   A O   1 
ATOM   881  C CB  . VAL   A 1 114 ? 12.494  1.932   20.452 1.00 35.32  ? 114 VAL   A CB  1 
ATOM   882  C CG1 . VAL   A 1 114 ? 11.023  2.313   20.592 1.00 37.40  ? 114 VAL   A CG1 1 
ATOM   883  C CG2 . VAL   A 1 114 ? 12.744  1.247   19.124 1.00 31.54  ? 114 VAL   A CG2 1 
ATOM   884  N N   . LEU   A 1 115 ? 12.381  5.161   21.546 1.00 31.98  ? 115 LEU   A N   1 
ATOM   885  C CA  . LEU   A 1 115 ? 11.770  5.958   22.605 1.00 33.18  ? 115 LEU   A CA  1 
ATOM   886  C C   . LEU   A 1 115 ? 10.264  5.760   22.486 1.00 29.85  ? 115 LEU   A C   1 
ATOM   887  O O   . LEU   A 1 115 ? 9.595   6.399   21.675 1.00 34.99  ? 115 LEU   A O   1 
ATOM   888  C CB  . LEU   A 1 115 ? 12.173  7.422   22.501 1.00 32.66  ? 115 LEU   A CB  1 
ATOM   889  C CG  . LEU   A 1 115 ? 11.614  8.319   23.608 1.00 41.73  ? 115 LEU   A CG  1 
ATOM   890  C CD1 . LEU   A 1 115 ? 12.075  7.851   24.989 1.00 39.14  ? 115 LEU   A CD1 1 
ATOM   891  C CD2 . LEU   A 1 115 ? 12.010  9.765   23.364 1.00 37.27  ? 115 LEU   A CD2 1 
ATOM   892  N N   . ALA   A 1 116 ? 9.737   4.838   23.287 1.00 30.02  ? 116 ALA   A N   1 
ATOM   893  C CA  . ALA   A 1 116 ? 8.305   4.564   23.294 1.00 39.85  ? 116 ALA   A CA  1 
ATOM   894  C C   . ALA   A 1 116 ? 7.565   5.722   23.954 1.00 38.60  ? 116 ALA   A C   1 
ATOM   895  O O   . ALA   A 1 116 ? 7.835   6.060   25.111 1.00 41.44  ? 116 ALA   A O   1 
ATOM   896  C CB  . ALA   A 1 116 ? 8.020   3.254   24.024 1.00 31.68  ? 116 ALA   A CB  1 
ATOM   897  N N   . CYS   A 1 117 ? 6.635   6.331   23.220 1.00 38.57  ? 117 CYS   A N   1 
ATOM   898  C CA  . CYS   A 1 117 ? 5.907   7.498   23.696 1.00 41.38  ? 117 CYS   A CA  1 
ATOM   899  C C   . CYS   A 1 117 ? 4.404   7.270   23.608 1.00 41.09  ? 117 CYS   A C   1 
ATOM   900  O O   . CYS   A 1 117 ? 3.915   6.524   22.753 1.00 39.41  ? 117 CYS   A O   1 
ATOM   901  C CB  . CYS   A 1 117 ? 6.274   8.755   22.897 1.00 37.64  ? 117 CYS   A CB  1 
ATOM   902  S SG  . CYS   A 1 117 ? 7.999   9.256   23.030 1.00 48.66  ? 117 CYS   A SG  1 
ATOM   903  N N   . TYR   A 1 118 ? 3.680   7.931   24.510 1.00 40.15  ? 118 TYR   A N   1 
ATOM   904  C CA  . TYR   A 1 118 ? 2.223   7.935   24.529 1.00 37.98  ? 118 TYR   A CA  1 
ATOM   905  C C   . TYR   A 1 118 ? 1.752   9.342   24.873 1.00 46.24  ? 118 TYR   A C   1 
ATOM   906  O O   . TYR   A 1 118 ? 2.218   9.930   25.853 1.00 42.28  ? 118 TYR   A O   1 
ATOM   907  C CB  . TYR   A 1 118 ? 1.680   6.913   25.534 1.00 38.98  ? 118 TYR   A CB  1 
ATOM   908  C CG  . TYR   A 1 118 ? 2.102   5.502   25.205 1.00 42.03  ? 118 TYR   A CG  1 
ATOM   909  C CD1 . TYR   A 1 118 ? 1.335   4.708   24.361 1.00 35.83  ? 118 TYR   A CD1 1 
ATOM   910  C CD2 . TYR   A 1 118 ? 3.283   4.970   25.716 1.00 41.86  ? 118 TYR   A CD2 1 
ATOM   911  C CE1 . TYR   A 1 118 ? 1.720   3.420   24.049 1.00 37.05  ? 118 TYR   A CE1 1 
ATOM   912  C CE2 . TYR   A 1 118 ? 3.679   3.684   25.402 1.00 41.35  ? 118 TYR   A CE2 1 
ATOM   913  C CZ  . TYR   A 1 118 ? 2.896   2.913   24.567 1.00 36.67  ? 118 TYR   A CZ  1 
ATOM   914  O OH  . TYR   A 1 118 ? 3.289   1.629   24.255 1.00 32.35  ? 118 TYR   A OH  1 
ATOM   915  N N   . ASN   A 1 119 ? 0.846   9.881   24.051 1.00 44.21  ? 119 ASN   A N   1 
ATOM   916  C CA  . ASN   A 1 119 ? 0.325   11.244  24.201 1.00 45.92  ? 119 ASN   A CA  1 
ATOM   917  C C   . ASN   A 1 119 ? 1.433   12.291  24.146 1.00 48.71  ? 119 ASN   A C   1 
ATOM   918  O O   . ASN   A 1 119 ? 1.370   13.312  24.835 1.00 45.48  ? 119 ASN   A O   1 
ATOM   919  C CB  . ASN   A 1 119 ? -0.481  11.413  25.494 1.00 50.92  ? 119 ASN   A CB  1 
ATOM   920  C CG  . ASN   A 1 119 ? -1.654  10.461  25.585 1.00 52.16  ? 119 ASN   A CG  1 
ATOM   921  O OD1 . ASN   A 1 119 ? -1.737  9.653   26.511 1.00 58.47  ? 119 ASN   A OD1 1 
ATOM   922  N ND2 . ASN   A 1 119 ? -2.573  10.551  24.627 1.00 51.99  ? 119 ASN   A ND2 1 
ATOM   923  N N   . GLY   A 1 120 ? 2.455   12.056  23.328 1.00 45.41  ? 120 GLY   A N   1 
ATOM   924  C CA  . GLY   A 1 120 ? 3.542   13.003  23.196 1.00 39.54  ? 120 GLY   A CA  1 
ATOM   925  C C   . GLY   A 1 120 ? 4.582   12.962  24.295 1.00 37.44  ? 120 GLY   A C   1 
ATOM   926  O O   . GLY   A 1 120 ? 5.540   13.742  24.241 1.00 41.90  ? 120 GLY   A O   1 
ATOM   927  N N   . SER   A 1 121 ? 4.437   12.075  25.279 1.00 36.01  ? 121 SER   A N   1 
ATOM   928  C CA  . SER   A 1 121 ? 5.333   12.011  26.427 1.00 42.20  ? 121 SER   A CA  1 
ATOM   929  C C   . SER   A 1 121 ? 6.090   10.692  26.443 1.00 48.00  ? 121 SER   A C   1 
ATOM   930  O O   . SER   A 1 121 ? 5.473   9.629   26.296 1.00 38.75  ? 121 SER   A O   1 
ATOM   931  C CB  . SER   A 1 121 ? 4.549   12.174  27.731 1.00 37.85  ? 121 SER   A CB  1 
ATOM   932  O OG  . SER   A 1 121 ? 3.990   13.470  27.827 1.00 54.14  ? 121 SER   A OG  1 
ATOM   933  N N   . PRO   A 1 122 ? 7.410   10.715  26.624 1.00 51.55  ? 122 PRO   A N   1 
ATOM   934  C CA  . PRO   A 1 122 ? 8.179   9.464   26.581 1.00 43.59  ? 122 PRO   A CA  1 
ATOM   935  C C   . PRO   A 1 122 ? 7.861   8.560   27.761 1.00 44.03  ? 122 PRO   A C   1 
ATOM   936  O O   . PRO   A 1 122 ? 7.754   9.009   28.903 1.00 47.63  ? 122 PRO   A O   1 
ATOM   937  C CB  . PRO   A 1 122 ? 9.636   9.941   26.618 1.00 46.92  ? 122 PRO   A CB  1 
ATOM   938  C CG  . PRO   A 1 122 ? 9.581   11.367  26.155 1.00 51.17  ? 122 PRO   A CG  1 
ATOM   939  C CD  . PRO   A 1 122 ? 8.287   11.895  26.693 1.00 50.99  ? 122 PRO   A CD  1 
ATOM   940  N N   . SER   A 1 123 ? 7.704   7.270   27.466 1.00 38.69  ? 123 SER   A N   1 
ATOM   941  C CA  . SER   A 1 123 ? 7.419   6.244   28.462 1.00 43.76  ? 123 SER   A CA  1 
ATOM   942  C C   . SER   A 1 123 ? 8.639   5.412   28.829 1.00 44.39  ? 123 SER   A C   1 
ATOM   943  O O   . SER   A 1 123 ? 8.773   4.997   29.983 1.00 40.44  ? 123 SER   A O   1 
ATOM   944  C CB  . SER   A 1 123 ? 6.314   5.311   27.955 1.00 43.52  ? 123 SER   A CB  1 
ATOM   945  O OG  . SER   A 1 123 ? 6.219   4.149   28.762 1.00 43.60  ? 123 SER   A OG  1 
ATOM   946  N N   . GLY   A 1 124 ? 9.521   5.146   27.874 1.00 35.40  ? 124 GLY   A N   1 
ATOM   947  C CA  . GLY   A 1 124 ? 10.681  4.319   28.145 1.00 34.47  ? 124 GLY   A CA  1 
ATOM   948  C C   . GLY   A 1 124 ? 11.541  4.219   26.906 1.00 39.02  ? 124 GLY   A C   1 
ATOM   949  O O   . GLY   A 1 124 ? 11.157  4.652   25.815 1.00 36.33  ? 124 GLY   A O   1 
ATOM   950  N N   . VAL   A 1 125 ? 12.723  3.637   27.091 1.00 36.52  ? 125 VAL   A N   1 
ATOM   951  C CA  . VAL   A 1 125 ? 13.694  3.504   26.014 1.00 33.18  ? 125 VAL   A CA  1 
ATOM   952  C C   . VAL   A 1 125 ? 14.275  2.097   26.041 1.00 34.71  ? 125 VAL   A C   1 
ATOM   953  O O   . VAL   A 1 125 ? 14.496  1.524   27.114 1.00 36.41  ? 125 VAL   A O   1 
ATOM   954  C CB  . VAL   A 1 125 ? 14.803  4.575   26.116 1.00 34.51  ? 125 VAL   A CB  1 
ATOM   955  C CG1 . VAL   A 1 125 ? 15.633  4.377   27.371 1.00 36.53  ? 125 VAL   A CG1 1 
ATOM   956  C CG2 . VAL   A 1 125 ? 15.671  4.572   24.863 1.00 41.33  ? 125 VAL   A CG2 1 
ATOM   957  N N   . TYR   A 1 126 ? 14.493  1.529   24.856 1.00 33.07  ? 126 TYR   A N   1 
ATOM   958  C CA  . TYR   A 1 126 ? 15.039  0.183   24.753 1.00 31.12  ? 126 TYR   A CA  1 
ATOM   959  C C   . TYR   A 1 126 ? 15.681  0.008   23.383 1.00 35.51  ? 126 TYR   A C   1 
ATOM   960  O O   . TYR   A 1 126 ? 15.447  0.793   22.461 1.00 30.10  ? 126 TYR   A O   1 
ATOM   961  C CB  . TYR   A 1 126 ? 13.960  -0.881  24.998 1.00 35.53  ? 126 TYR   A CB  1 
ATOM   962  C CG  . TYR   A 1 126 ? 12.733  -0.762  24.114 1.00 39.76  ? 126 TYR   A CG  1 
ATOM   963  C CD1 . TYR   A 1 126 ? 12.675  -1.406  22.887 1.00 39.95  ? 126 TYR   A CD1 1 
ATOM   964  C CD2 . TYR   A 1 126 ? 11.629  -0.019  24.513 1.00 39.84  ? 126 TYR   A CD2 1 
ATOM   965  C CE1 . TYR   A 1 126 ? 11.561  -1.309  22.076 1.00 40.65  ? 126 TYR   A CE1 1 
ATOM   966  C CE2 . TYR   A 1 126 ? 10.505  0.084   23.703 1.00 41.40  ? 126 TYR   A CE2 1 
ATOM   967  C CZ  . TYR   A 1 126 ? 10.480  -0.566  22.488 1.00 36.70  ? 126 TYR   A CZ  1 
ATOM   968  O OH  . TYR   A 1 126 ? 9.374   -0.474  21.674 1.00 41.67  ? 126 TYR   A OH  1 
ATOM   969  N N   . GLN   A 1 127 ? 16.501  -1.036  23.268 1.00 37.39  ? 127 GLN   A N   1 
ATOM   970  C CA  . GLN   A 1 127 ? 17.202  -1.352  22.029 1.00 42.44  ? 127 GLN   A CA  1 
ATOM   971  C C   . GLN   A 1 127 ? 16.383  -2.292  21.160 1.00 42.19  ? 127 GLN   A C   1 
ATOM   972  O O   . GLN   A 1 127 ? 15.720  -3.204  21.663 1.00 38.04  ? 127 GLN   A O   1 
ATOM   973  C CB  . GLN   A 1 127 ? 18.553  -2.002  22.320 1.00 42.97  ? 127 GLN   A CB  1 
ATOM   974  C CG  . GLN   A 1 127 ? 19.655  -1.027  22.593 1.00 46.79  ? 127 GLN   A CG  1 
ATOM   975  C CD  . GLN   A 1 127 ? 20.026  -0.199  21.377 1.00 43.64  ? 127 GLN   A CD  1 
ATOM   976  O OE1 . GLN   A 1 127 ? 19.619  0.956   21.251 1.00 44.57  ? 127 GLN   A OE1 1 
ATOM   977  N NE2 . GLN   A 1 127 ? 20.812  -0.783  20.481 1.00 44.43  ? 127 GLN   A NE2 1 
ATOM   978  N N   . CYS   A 1 128 ? 16.453  -2.076  19.847 1.00 39.26  ? 128 CYS   A N   1 
ATOM   979  C CA  . CYS   A 1 128 ? 15.810  -2.941  18.871 1.00 33.59  ? 128 CYS   A CA  1 
ATOM   980  C C   . CYS   A 1 128 ? 16.746  -3.160  17.691 1.00 48.00  ? 128 CYS   A C   1 
ATOM   981  O O   . CYS   A 1 128 ? 17.664  -2.378  17.438 1.00 39.90  ? 128 CYS   A O   1 
ATOM   982  C CB  . CYS   A 1 128 ? 14.487  -2.360  18.352 1.00 37.54  ? 128 CYS   A CB  1 
ATOM   983  S SG  . CYS   A 1 128 ? 13.029  -2.820  19.301 1.00 66.49  ? 128 CYS   A SG  1 
ATOM   984  N N   . ALA   A 1 129 ? 16.484  -4.233  16.958 1.00 42.19  ? 129 ALA   A N   1 
ATOM   985  C CA  . ALA   A 1 129 ? 17.195  -4.526  15.726 1.00 43.98  ? 129 ALA   A CA  1 
ATOM   986  C C   . ALA   A 1 129 ? 16.188  -4.697  14.602 1.00 39.56  ? 129 ALA   A C   1 
ATOM   987  O O   . ALA   A 1 129 ? 15.136  -5.318  14.787 1.00 42.21  ? 129 ALA   A O   1 
ATOM   988  C CB  . ALA   A 1 129 ? 18.056  -5.788  15.859 1.00 35.56  ? 129 ALA   A CB  1 
ATOM   989  N N   . MET   A 1 130 ? 16.502  -4.124  13.447 1.00 40.25  ? 130 MET   A N   1 
ATOM   990  C CA  . MET   A 1 130 ? 15.746  -4.409  12.234 1.00 35.40  ? 130 MET   A CA  1 
ATOM   991  C C   . MET   A 1 130 ? 15.964  -5.872  11.865 1.00 37.07  ? 130 MET   A C   1 
ATOM   992  O O   . MET   A 1 130 ? 17.088  -6.282  11.554 1.00 40.71  ? 130 MET   A O   1 
ATOM   993  C CB  . MET   A 1 130 ? 16.186  -3.478  11.109 1.00 36.23  ? 130 MET   A CB  1 
ATOM   994  C CG  . MET   A 1 130 ? 15.386  -3.614  9.823  1.00 39.63  ? 130 MET   A CG  1 
ATOM   995  S SD  . MET   A 1 130 ? 13.624  -3.328  10.062 1.00 44.26  ? 130 MET   A SD  1 
ATOM   996  C CE  . MET   A 1 130 ? 13.623  -1.639  10.668 1.00 35.86  ? 130 MET   A CE  1 
ATOM   997  N N   . ARG   A 1 131 ? 14.903  -6.669  11.930 1.00 38.70  ? 131 ARG   A N   1 
ATOM   998  C CA  . ARG   A 1 131 ? 15.011  -8.076  11.598 1.00 34.91  ? 131 ARG   A CA  1 
ATOM   999  C C   . ARG   A 1 131 ? 15.210  -8.240  10.094 1.00 37.57  ? 131 ARG   A C   1 
ATOM   1000 O O   . ARG   A 1 131 ? 14.884  -7.343  9.313  1.00 37.41  ? 131 ARG   A O   1 
ATOM   1001 C CB  . ARG   A 1 131 ? 13.762  -8.836  12.041 1.00 32.27  ? 131 ARG   A CB  1 
ATOM   1002 C CG  . ARG   A 1 131 ? 13.407  -8.702  13.513 1.00 40.78  ? 131 ARG   A CG  1 
ATOM   1003 C CD  . ARG   A 1 131 ? 14.509  -9.218  14.411 1.00 43.81  ? 131 ARG   A CD  1 
ATOM   1004 N NE  . ARG   A 1 131 ? 14.952  -10.548 14.013 1.00 42.50  ? 131 ARG   A NE  1 
ATOM   1005 C CZ  . ARG   A 1 131 ? 16.032  -11.146 14.495 1.00 45.07  ? 131 ARG   A CZ  1 
ATOM   1006 N NH1 . ARG   A 1 131 ? 16.782  -10.573 15.422 1.00 40.07  ? 131 ARG   A NH1 1 
ATOM   1007 N NH2 . ARG   A 1 131 ? 16.372  -12.344 14.028 1.00 42.01  ? 131 ARG   A NH2 1 
ATOM   1008 N N   . PRO   A 1 132 ? 15.759  -9.378  9.666  1.00 39.49  ? 132 PRO   A N   1 
ATOM   1009 C CA  . PRO   A 1 132 ? 15.877  -9.633  8.221  1.00 42.06  ? 132 PRO   A CA  1 
ATOM   1010 C C   . PRO   A 1 132 ? 14.568  -9.490  7.460  1.00 40.01  ? 132 PRO   A C   1 
ATOM   1011 O O   . PRO   A 1 132 ? 14.589  -9.057  6.300  1.00 39.48  ? 132 PRO   A O   1 
ATOM   1012 C CB  . PRO   A 1 132 ? 16.415  -11.068 8.178  1.00 40.69  ? 132 PRO   A CB  1 
ATOM   1013 C CG  . PRO   A 1 132 ? 17.257  -11.159 9.411  1.00 43.42  ? 132 PRO   A CG  1 
ATOM   1014 C CD  . PRO   A 1 132 ? 16.514  -10.365 10.461 1.00 42.75  ? 132 PRO   A CD  1 
ATOM   1015 N N   . ASN   A 1 133 ? 13.429  -9.816  8.073  1.00 37.23  ? 133 ASN   A N   1 
ATOM   1016 C CA  . ASN   A 1 133 ? 12.132  -9.636  7.430  1.00 37.20  ? 133 ASN   A CA  1 
ATOM   1017 C C   . ASN   A 1 133 ? 11.572  -8.229  7.604  1.00 32.08  ? 133 ASN   A C   1 
ATOM   1018 O O   . ASN   A 1 133 ? 10.385  -8.013  7.338  1.00 39.55  ? 133 ASN   A O   1 
ATOM   1019 C CB  . ASN   A 1 133 ? 11.127  -10.664 7.955  1.00 42.40  ? 133 ASN   A CB  1 
ATOM   1020 C CG  . ASN   A 1 133 ? 10.938  -10.585 9.457  1.00 43.14  ? 133 ASN   A CG  1 
ATOM   1021 O OD1 . ASN   A 1 133 ? 11.457  -9.685  10.116 1.00 33.50  ? 133 ASN   A OD1 1 
ATOM   1022 N ND2 . ASN   A 1 133 ? 10.187  -11.532 10.006 1.00 39.61  ? 133 ASN   A ND2 1 
ATOM   1023 N N   . PHE   A 1 134 ? 12.392  -7.283  8.063  1.00 31.55  ? 134 PHE   A N   1 
ATOM   1024 C CA  . PHE   A 1 134 ? 12.018  -5.869  8.172  1.00 37.33  ? 134 PHE   A CA  1 
ATOM   1025 C C   . PHE   A 1 134 ? 10.907  -5.625  9.193  1.00 38.98  ? 134 PHE   A C   1 
ATOM   1026 O O   . PHE   A 1 134 ? 10.115  -4.690  9.052  1.00 36.83  ? 134 PHE   A O   1 
ATOM   1027 C CB  . PHE   A 1 134 ? 11.627  -5.293  6.811  1.00 33.76  ? 134 PHE   A CB  1 
ATOM   1028 C CG  . PHE   A 1 134 ? 12.772  -5.194  5.853  1.00 36.99  ? 134 PHE   A CG  1 
ATOM   1029 C CD1 . PHE   A 1 134 ? 13.694  -4.165  5.965  1.00 42.84  ? 134 PHE   A CD1 1 
ATOM   1030 C CD2 . PHE   A 1 134 ? 12.937  -6.132  4.849  1.00 44.11  ? 134 PHE   A CD2 1 
ATOM   1031 C CE1 . PHE   A 1 134 ? 14.758  -4.066  5.088  1.00 44.12  ? 134 PHE   A CE1 1 
ATOM   1032 C CE2 . PHE   A 1 134 ? 14.000  -6.042  3.969  1.00 44.04  ? 134 PHE   A CE2 1 
ATOM   1033 C CZ  . PHE   A 1 134 ? 14.911  -5.006  4.087  1.00 47.24  ? 134 PHE   A CZ  1 
ATOM   1034 N N   . THR   A 1 135 ? 10.837  -6.453  10.227 1.00 35.48  ? 135 THR   A N   1 
ATOM   1035 C CA  . THR   A 1 135 ? 10.042  -6.162  11.410 1.00 34.38  ? 135 THR   A CA  1 
ATOM   1036 C C   . THR   A 1 135 ? 10.978  -5.866  12.569 1.00 33.25  ? 135 THR   A C   1 
ATOM   1037 O O   . THR   A 1 135 ? 12.199  -6.017  12.466 1.00 34.00  ? 135 THR   A O   1 
ATOM   1038 C CB  . THR   A 1 135 ? 9.114   -7.329  11.771 1.00 34.76  ? 135 THR   A CB  1 
ATOM   1039 O OG1 . THR   A 1 135 ? 9.900   -8.471  12.135 1.00 35.07  ? 135 THR   A OG1 1 
ATOM   1040 C CG2 . THR   A 1 135 ? 8.220   -7.679  10.597 1.00 37.13  ? 135 THR   A CG2 1 
ATOM   1041 N N   . ILE   A 1 136 ? 10.398  -5.424  13.681 1.00 34.41  ? 136 ILE   A N   1 
ATOM   1042 C CA  . ILE   A 1 136 ? 11.131  -5.280  14.931 1.00 38.58  ? 136 ILE   A CA  1 
ATOM   1043 C C   . ILE   A 1 136 ? 10.296  -5.893  16.046 1.00 33.86  ? 136 ILE   A C   1 
ATOM   1044 O O   . ILE   A 1 136 ? 9.063   -5.808  16.035 1.00 37.67  ? 136 ILE   A O   1 
ATOM   1045 C CB  . ILE   A 1 136 ? 11.489  -3.808  15.239 1.00 40.57  ? 136 ILE   A CB  1 
ATOM   1046 C CG1 . ILE   A 1 136 ? 10.245  -2.971  15.514 1.00 33.98  ? 136 ILE   A CG1 1 
ATOM   1047 C CG2 . ILE   A 1 136 ? 12.273  -3.188  14.083 1.00 38.85  ? 136 ILE   A CG2 1 
ATOM   1048 C CD1 . ILE   A 1 136 ? 10.571  -1.582  15.993 1.00 35.94  ? 136 ILE   A CD1 1 
ATOM   1049 N N   . LYS   A 1 137 ? 10.970  -6.557  16.985 1.00 39.44  ? 137 LYS   A N   1 
ATOM   1050 C CA  . LYS   A 1 137 ? 10.310  -7.131  18.156 1.00 40.72  ? 137 LYS   A CA  1 
ATOM   1051 C C   . LYS   A 1 137 ? 10.402  -6.110  19.284 1.00 32.77  ? 137 LYS   A C   1 
ATOM   1052 O O   . LYS   A 1 137 ? 11.286  -6.149  20.141 1.00 39.16  ? 137 LYS   A O   1 
ATOM   1053 C CB  . LYS   A 1 137 ? 10.947  -8.460  18.546 1.00 43.00  ? 137 LYS   A CB  1 
ATOM   1054 C CG  . LYS   A 1 137 ? 10.781  -9.585  17.531 1.00 50.92  ? 137 LYS   A CG  1 
ATOM   1055 C CD  . LYS   A 1 137 ? 11.483  -10.857 18.011 1.00 58.50  ? 137 LYS   A CD  1 
ATOM   1056 C CE  . LYS   A 1 137 ? 11.341  -12.001 17.012 1.00 60.19  ? 137 LYS   A CE  1 
ATOM   1057 N NZ  . LYS   A 1 137 ? 9.923   -12.427 16.827 1.00 64.28  ? 137 LYS   A NZ  1 
ATOM   1058 N N   . GLY   A 1 138 ? 9.460   -5.169  19.274 1.00 38.56  ? 138 GLY   A N   1 
ATOM   1059 C CA  . GLY   A 1 138 ? 9.429   -4.100  20.244 1.00 37.85  ? 138 GLY   A CA  1 
ATOM   1060 C C   . GLY   A 1 138 ? 8.365   -4.300  21.309 1.00 39.02  ? 138 GLY   A C   1 
ATOM   1061 O O   . GLY   A 1 138 ? 7.778   -5.372  21.464 1.00 40.46  ? 138 GLY   A O   1 
ATOM   1062 N N   . SER   A 1 139 ? 8.125   -3.227  22.060 1.00 37.96  ? 139 SER   A N   1 
ATOM   1063 C CA  . SER   A 1 139 ? 7.137   -3.197  23.138 1.00 40.86  ? 139 SER   A CA  1 
ATOM   1064 C C   . SER   A 1 139 ? 6.309   -1.935  22.917 1.00 32.71  ? 139 SER   A C   1 
ATOM   1065 O O   . SER   A 1 139 ? 6.705   -0.837  23.317 1.00 38.56  ? 139 SER   A O   1 
ATOM   1066 C CB  . SER   A 1 139 ? 7.808   -3.225  24.513 1.00 37.70  ? 139 SER   A CB  1 
ATOM   1067 O OG  . SER   A 1 139 ? 6.853   -3.142  25.558 1.00 45.52  ? 139 SER   A OG  1 
ATOM   1068 N N   . PHE   A 1 140 ? 5.164   -2.101  22.261 1.00 33.71  ? 140 PHE   A N   1 
ATOM   1069 C CA  . PHE   A 1 140 ? 4.307   -0.998  21.849 1.00 35.40  ? 140 PHE   A CA  1 
ATOM   1070 C C   . PHE   A 1 140 ? 2.865   -1.323  22.214 1.00 38.22  ? 140 PHE   A C   1 
ATOM   1071 O O   . PHE   A 1 140 ? 2.368   -2.408  21.892 1.00 35.00  ? 140 PHE   A O   1 
ATOM   1072 C CB  . PHE   A 1 140 ? 4.398   -0.747  20.336 1.00 33.07  ? 140 PHE   A CB  1 
ATOM   1073 C CG  . PHE   A 1 140 ? 5.734   -0.229  19.862 1.00 35.03  ? 140 PHE   A CG  1 
ATOM   1074 C CD1 . PHE   A 1 140 ? 6.140   1.066   20.150 1.00 39.58  ? 140 PHE   A CD1 1 
ATOM   1075 C CD2 . PHE   A 1 140 ? 6.560   -1.023  19.083 1.00 34.53  ? 140 PHE   A CD2 1 
ATOM   1076 C CE1 . PHE   A 1 140 ? 7.363   1.548   19.693 1.00 36.05  ? 140 PHE   A CE1 1 
ATOM   1077 C CE2 . PHE   A 1 140 ? 7.782   -0.546  18.623 1.00 37.93  ? 140 PHE   A CE2 1 
ATOM   1078 C CZ  . PHE   A 1 140 ? 8.182   0.736   18.929 1.00 34.05  ? 140 PHE   A CZ  1 
ATOM   1079 N N   . LEU   A 1 141 ? 2.199   -0.385  22.875 1.00 39.63  ? 141 LEU   A N   1 
ATOM   1080 C CA  . LEU   A 1 141 ? 0.775   -0.469  23.156 1.00 41.89  ? 141 LEU   A CA  1 
ATOM   1081 C C   . LEU   A 1 141 ? 0.025   0.494   22.248 1.00 36.78  ? 141 LEU   A C   1 
ATOM   1082 O O   . LEU   A 1 141 ? 0.623   1.286   21.518 1.00 35.92  ? 141 LEU   A O   1 
ATOM   1083 C CB  . LEU   A 1 141 ? 0.484   -0.145  24.620 1.00 34.28  ? 141 LEU   A CB  1 
ATOM   1084 C CG  . LEU   A 1 141 ? 1.220   -0.976  25.662 1.00 41.78  ? 141 LEU   A CG  1 
ATOM   1085 C CD1 . LEU   A 1 141 ? 0.935   -0.403  27.033 1.00 49.31  ? 141 LEU   A CD1 1 
ATOM   1086 C CD2 . LEU   A 1 141 ? 0.788   -2.425  25.573 1.00 37.59  ? 141 LEU   A CD2 1 
ATOM   1087 N N   . ASN   A 1 142 ? -1.303  0.429   22.317 1.00 43.81  ? 142 ASN   A N   1 
ATOM   1088 C CA  . ASN   A 1 142 ? -2.126  1.414   21.633 1.00 38.99  ? 142 ASN   A CA  1 
ATOM   1089 C C   . ASN   A 1 142 ? -1.737  2.817   22.078 1.00 42.20  ? 142 ASN   A C   1 
ATOM   1090 O O   . ASN   A 1 142 ? -1.515  3.069   23.266 1.00 47.67  ? 142 ASN   A O   1 
ATOM   1091 C CB  . ASN   A 1 142 ? -3.606  1.163   21.906 1.00 44.87  ? 142 ASN   A CB  1 
ATOM   1092 C CG  . ASN   A 1 142 ? -4.502  2.151   21.182 1.00 45.49  ? 142 ASN   A CG  1 
ATOM   1093 O OD1 . ASN   A 1 142 ? -4.867  3.193   21.726 1.00 61.43  ? 142 ASN   A OD1 1 
ATOM   1094 N ND2 . ASN   A 1 142 ? -4.856  1.831   19.945 1.00 49.52  ? 142 ASN   A ND2 1 
ATOM   1095 N N   . GLY   A 1 143 ? -1.640  3.726   21.114 1.00 37.04  ? 143 GLY   A N   1 
ATOM   1096 C CA  . GLY   A 1 143 ? -1.202  5.080   21.356 1.00 31.36  ? 143 GLY   A CA  1 
ATOM   1097 C C   . GLY   A 1 143 ? 0.263   5.335   21.063 1.00 34.88  ? 143 GLY   A C   1 
ATOM   1098 O O   . GLY   A 1 143 ? 0.680   6.499   21.057 1.00 37.49  ? 143 GLY   A O   1 
ATOM   1099 N N   . SER   A 1 144 ? 1.051   4.288   20.817 1.00 38.39  ? 144 SER   A N   1 
ATOM   1100 C CA  . SER   A 1 144 ? 2.494   4.411   20.641 1.00 37.75  ? 144 SER   A CA  1 
ATOM   1101 C C   . SER   A 1 144 ? 2.910   4.745   19.215 1.00 31.79  ? 144 SER   A C   1 
ATOM   1102 O O   . SER   A 1 144 ? 4.111   4.860   18.955 1.00 27.53  ? 144 SER   A O   1 
ATOM   1103 C CB  . SER   A 1 144 ? 3.194   3.117   21.064 1.00 27.12  ? 144 SER   A CB  1 
ATOM   1104 O OG  . SER   A 1 144 ? 2.890   2.067   20.166 1.00 32.55  ? 144 SER   A OG  1 
ATOM   1105 N N   . CYS   A 1 145 ? 1.967   4.875   18.283 1.00 35.43  ? 145 CYS   A N   1 
ATOM   1106 C CA  . CYS   A 1 145 ? 2.335   5.231   16.918 1.00 36.28  ? 145 CYS   A CA  1 
ATOM   1107 C C   . CYS   A 1 145 ? 2.990   6.606   16.895 1.00 36.10  ? 145 CYS   A C   1 
ATOM   1108 O O   . CYS   A 1 145 ? 2.585   7.520   17.617 1.00 38.15  ? 145 CYS   A O   1 
ATOM   1109 C CB  . CYS   A 1 145 ? 1.107   5.212   16.003 1.00 36.84  ? 145 CYS   A CB  1 
ATOM   1110 S SG  . CYS   A 1 145 ? 0.328   3.589   15.827 1.00 42.66  ? 145 CYS   A SG  1 
ATOM   1111 N N   . GLY   A 1 146 ? 4.019   6.747   16.066 1.00 33.43  ? 146 GLY   A N   1 
ATOM   1112 C CA  . GLY   A 1 146 ? 4.800   7.961   16.014 1.00 36.11  ? 146 GLY   A CA  1 
ATOM   1113 C C   . GLY   A 1 146 ? 6.045   7.941   16.871 1.00 30.49  ? 146 GLY   A C   1 
ATOM   1114 O O   . GLY   A 1 146 ? 6.903   8.818   16.704 1.00 31.82  ? 146 GLY   A O   1 
ATOM   1115 N N   . SER   A 1 147 ? 6.163   6.983   17.788 1.00 29.71  ? 147 SER   A N   1 
ATOM   1116 C CA  . SER   A 1 147 ? 7.421   6.781   18.490 1.00 25.98  ? 147 SER   A CA  1 
ATOM   1117 C C   . SER   A 1 147 ? 8.523   6.492   17.479 1.00 29.26  ? 147 SER   A C   1 
ATOM   1118 O O   . SER   A 1 147 ? 8.289   5.854   16.449 1.00 29.89  ? 147 SER   A O   1 
ATOM   1119 C CB  . SER   A 1 147 ? 7.301   5.627   19.482 1.00 35.61  ? 147 SER   A CB  1 
ATOM   1120 O OG  . SER   A 1 147 ? 6.258   5.858   20.413 1.00 36.83  ? 147 SER   A OG  1 
ATOM   1121 N N   . VAL   A 1 148 ? 9.730   6.969   17.771 1.00 28.42  ? 148 VAL   A N   1 
ATOM   1122 C CA  . VAL   A 1 148 ? 10.802  6.957   16.786 1.00 36.42  ? 148 VAL   A CA  1 
ATOM   1123 C C   . VAL   A 1 148 ? 11.974  6.145   17.308 1.00 35.38  ? 148 VAL   A C   1 
ATOM   1124 O O   . VAL   A 1 148 ? 12.195  6.025   18.518 1.00 30.65  ? 148 VAL   A O   1 
ATOM   1125 C CB  . VAL   A 1 148 ? 11.269  8.376   16.403 1.00 31.58  ? 148 VAL   A CB  1 
ATOM   1126 C CG1 . VAL   A 1 148 ? 10.117  9.171   15.820 1.00 39.34  ? 148 VAL   A CG1 1 
ATOM   1127 C CG2 . VAL   A 1 148 ? 11.872  9.076   17.608 1.00 37.12  ? 148 VAL   A CG2 1 
ATOM   1128 N N   . GLY   A 1 149 ? 12.711  5.565   16.366 1.00 34.45  ? 149 GLY   A N   1 
ATOM   1129 C CA  . GLY   A 1 149 ? 13.962  4.890   16.646 1.00 35.49  ? 149 GLY   A CA  1 
ATOM   1130 C C   . GLY   A 1 149 ? 15.111  5.746   16.149 1.00 36.71  ? 149 GLY   A C   1 
ATOM   1131 O O   . GLY   A 1 149 ? 14.965  6.497   15.183 1.00 32.29  ? 149 GLY   A O   1 
ATOM   1132 N N   . PHE   A 1 150 ? 16.256  5.641   16.817 1.00 34.54  ? 150 PHE   A N   1 
ATOM   1133 C CA  . PHE   A 1 150 ? 17.341  6.564   16.529 1.00 39.11  ? 150 PHE   A CA  1 
ATOM   1134 C C   . PHE   A 1 150 ? 18.662  5.965   16.978 1.00 33.53  ? 150 PHE   A C   1 
ATOM   1135 O O   . PHE   A 1 150 ? 18.711  5.051   17.807 1.00 30.69  ? 150 PHE   A O   1 
ATOM   1136 C CB  . PHE   A 1 150 ? 17.112  7.920   17.214 1.00 34.87  ? 150 PHE   A CB  1 
ATOM   1137 C CG  . PHE   A 1 150 ? 17.115  7.845   18.716 1.00 37.71  ? 150 PHE   A CG  1 
ATOM   1138 C CD1 . PHE   A 1 150 ? 15.960  7.523   19.414 1.00 34.54  ? 150 PHE   A CD1 1 
ATOM   1139 C CD2 . PHE   A 1 150 ? 18.274  8.100   19.429 1.00 35.53  ? 150 PHE   A CD2 1 
ATOM   1140 C CE1 . PHE   A 1 150 ? 15.966  7.453   20.799 1.00 35.61  ? 150 PHE   A CE1 1 
ATOM   1141 C CE2 . PHE   A 1 150 ? 18.290  8.028   20.807 1.00 37.01  ? 150 PHE   A CE2 1 
ATOM   1142 C CZ  . PHE   A 1 150 ? 17.135  7.708   21.498 1.00 33.83  ? 150 PHE   A CZ  1 
ATOM   1143 N N   . ASN   A 1 151 ? 19.734  6.495   16.397 1.00 40.08  ? 151 ASN   A N   1 
ATOM   1144 C CA  . ASN   A 1 151 ? 21.090  6.290   16.875 1.00 42.37  ? 151 ASN   A CA  1 
ATOM   1145 C C   . ASN   A 1 151 ? 21.708  7.657   17.118 1.00 48.77  ? 151 ASN   A C   1 
ATOM   1146 O O   . ASN   A 1 151 ? 21.259  8.662   16.561 1.00 39.97  ? 151 ASN   A O   1 
ATOM   1147 C CB  . ASN   A 1 151 ? 21.941  5.495   15.877 1.00 39.67  ? 151 ASN   A CB  1 
ATOM   1148 C CG  . ASN   A 1 151 ? 21.550  4.029   15.809 1.00 38.34  ? 151 ASN   A CG  1 
ATOM   1149 O OD1 . ASN   A 1 151 ? 21.987  3.225   16.630 1.00 42.21  ? 151 ASN   A OD1 1 
ATOM   1150 N ND2 . ASN   A 1 151 ? 20.738  3.672   14.818 1.00 35.44  ? 151 ASN   A ND2 1 
ATOM   1151 N N   . ILE   A 1 152 ? 22.728  7.695   17.963 1.00 48.00  ? 152 ILE   A N   1 
ATOM   1152 C CA  . ILE   A 1 152 ? 23.454  8.925   18.251 1.00 53.56  ? 152 ILE   A CA  1 
ATOM   1153 C C   . ILE   A 1 152 ? 24.886  8.712   17.777 1.00 64.02  ? 152 ILE   A C   1 
ATOM   1154 O O   . ILE   A 1 152 ? 25.712  8.131   18.491 1.00 65.96  ? 152 ILE   A O   1 
ATOM   1155 C CB  . ILE   A 1 152 ? 23.385  9.300   19.735 1.00 51.93  ? 152 ILE   A CB  1 
ATOM   1156 C CG1 . ILE   A 1 152 ? 21.925  9.482   20.161 1.00 42.59  ? 152 ILE   A CG1 1 
ATOM   1157 C CG2 . ILE   A 1 152 ? 24.175  10.570  20.003 1.00 61.55  ? 152 ILE   A CG2 1 
ATOM   1158 C CD1 . ILE   A 1 152 ? 21.759  10.006  21.564 1.00 51.45  ? 152 ILE   A CD1 1 
ATOM   1159 N N   . ASP   A 1 153 ? 25.179  9.166   16.558 1.00 69.33  ? 153 ASP   A N   1 
ATOM   1160 C CA  . ASP   A 1 153 ? 26.499  9.029   15.953 1.00 73.76  ? 153 ASP   A CA  1 
ATOM   1161 C C   . ASP   A 1 153 ? 27.216  10.371  16.034 1.00 74.05  ? 153 ASP   A C   1 
ATOM   1162 O O   . ASP   A 1 153 ? 26.741  11.365  15.472 1.00 68.73  ? 153 ASP   A O   1 
ATOM   1163 C CB  . ASP   A 1 153 ? 26.397  8.573   14.497 1.00 67.76  ? 153 ASP   A CB  1 
ATOM   1164 C CG  . ASP   A 1 153 ? 25.277  7.576   14.273 1.00 73.22  ? 153 ASP   A CG  1 
ATOM   1165 O OD1 . ASP   A 1 153 ? 24.098  7.973   14.391 1.00 72.31  ? 153 ASP   A OD1 1 
ATOM   1166 O OD2 . ASP   A 1 153 ? 25.575  6.400   13.971 1.00 83.18  ? 153 ASP   A OD2 1 
ATOM   1167 N N   . TYR   A 1 154 ? 28.365  10.388  16.711 1.00 76.40  ? 154 TYR   A N   1 
ATOM   1168 C CA  . TYR   A 1 154 ? 29.096  11.619  17.032 1.00 78.50  ? 154 TYR   A CA  1 
ATOM   1169 C C   . TYR   A 1 154 ? 28.160  12.489  17.860 1.00 75.42  ? 154 TYR   A C   1 
ATOM   1170 O O   . TYR   A 1 154 ? 27.729  12.044  18.940 1.00 72.62  ? 154 TYR   A O   1 
ATOM   1171 C CB  . TYR   A 1 154 ? 29.636  12.253  15.746 1.00 70.56  ? 154 TYR   A CB  1 
ATOM   1172 N N   . ASP   A 1 155 ? 27.816  13.698  17.424 1.00 77.22  ? 155 ASP   A N   1 
ATOM   1173 C CA  . ASP   A 1 155 ? 26.885  14.558  18.141 1.00 77.70  ? 155 ASP   A CA  1 
ATOM   1174 C C   . ASP   A 1 155 ? 25.531  14.648  17.446 1.00 76.17  ? 155 ASP   A C   1 
ATOM   1175 O O   . ASP   A 1 155 ? 24.654  15.392  17.901 1.00 71.02  ? 155 ASP   A O   1 
ATOM   1176 C CB  . ASP   A 1 155 ? 27.487  15.956  18.313 1.00 77.55  ? 155 ASP   A CB  1 
ATOM   1177 C CG  . ASP   A 1 155 ? 27.880  16.592  16.987 1.00 80.40  ? 155 ASP   A CG  1 
ATOM   1178 O OD1 . ASP   A 1 155 ? 28.360  15.866  16.087 1.00 81.47  ? 155 ASP   A OD1 1 
ATOM   1179 O OD2 . ASP   A 1 155 ? 27.709  17.822  16.847 1.00 85.46  ? 155 ASP   A OD2 1 
ATOM   1180 N N   . CYS   A 1 156 ? 25.339  13.894  16.367 1.00 68.47  ? 156 CYS   A N   1 
ATOM   1181 C CA  . CYS   A 1 156 ? 24.166  13.993  15.511 1.00 58.73  ? 156 CYS   A CA  1 
ATOM   1182 C C   . CYS   A 1 156 ? 23.227  12.821  15.766 1.00 60.91  ? 156 CYS   A C   1 
ATOM   1183 O O   . CYS   A 1 156 ? 23.665  11.665  15.807 1.00 61.11  ? 156 CYS   A O   1 
ATOM   1184 C CB  . CYS   A 1 156 ? 24.586  14.026  14.042 1.00 56.72  ? 156 CYS   A CB  1 
ATOM   1185 S SG  . CYS   A 1 156 ? 23.235  13.856  12.870 1.00 56.50  ? 156 CYS   A SG  1 
ATOM   1186 N N   . VAL   A 1 157 ? 21.941  13.121  15.930 1.00 50.64  ? 157 VAL   A N   1 
ATOM   1187 C CA  . VAL   A 1 157 ? 20.917  12.097  16.115 1.00 49.54  ? 157 VAL   A CA  1 
ATOM   1188 C C   . VAL   A 1 157 ? 20.433  11.636  14.745 1.00 51.35  ? 157 VAL   A C   1 
ATOM   1189 O O   . VAL   A 1 157 ? 19.889  12.432  13.973 1.00 46.46  ? 157 VAL   A O   1 
ATOM   1190 C CB  . VAL   A 1 157 ? 19.744  12.626  16.954 1.00 43.58  ? 157 VAL   A CB  1 
ATOM   1191 C CG1 . VAL   A 1 157 ? 18.640  11.573  17.036 1.00 42.14  ? 157 VAL   A CG1 1 
ATOM   1192 C CG2 . VAL   A 1 157 ? 20.213  13.023  18.341 1.00 56.66  ? 157 VAL   A CG2 1 
ATOM   1193 N N   . SER   A 1 158 ? 20.610  10.346  14.447 1.00 44.82  ? 158 SER   A N   1 
ATOM   1194 C CA  . SER   A 1 158 ? 20.158  9.762   13.182 1.00 45.62  ? 158 SER   A CA  1 
ATOM   1195 C C   . SER   A 1 158 ? 18.832  9.044   13.418 1.00 43.18  ? 158 SER   A C   1 
ATOM   1196 O O   . SER   A 1 158 ? 18.807  7.917   13.918 1.00 43.95  ? 158 SER   A O   1 
ATOM   1197 C CB  . SER   A 1 158 ? 21.202  8.806   12.614 1.00 42.83  ? 158 SER   A CB  1 
ATOM   1198 O OG  . SER   A 1 158 ? 22.361  9.501   12.192 1.00 55.01  ? 158 SER   A OG  1 
ATOM   1199 N N   . PHE   A 1 159 ? 17.730  9.695   13.049 1.00 39.66  ? 159 PHE   A N   1 
ATOM   1200 C CA  . PHE   A 1 159 ? 16.420  9.057   13.112 1.00 38.25  ? 159 PHE   A CA  1 
ATOM   1201 C C   . PHE   A 1 159 ? 16.278  8.038   11.985 1.00 41.64  ? 159 PHE   A C   1 
ATOM   1202 O O   . PHE   A 1 159 ? 16.526  8.353   10.818 1.00 37.15  ? 159 PHE   A O   1 
ATOM   1203 C CB  . PHE   A 1 159 ? 15.313  10.106  13.014 1.00 36.71  ? 159 PHE   A CB  1 
ATOM   1204 C CG  . PHE   A 1 159 ? 15.322  11.112  14.129 1.00 34.92  ? 159 PHE   A CG  1 
ATOM   1205 C CD1 . PHE   A 1 159 ? 14.790  10.796  15.368 1.00 37.12  ? 159 PHE   A CD1 1 
ATOM   1206 C CD2 . PHE   A 1 159 ? 15.847  12.380  13.935 1.00 38.85  ? 159 PHE   A CD2 1 
ATOM   1207 C CE1 . PHE   A 1 159 ? 14.785  11.722  16.394 1.00 37.09  ? 159 PHE   A CE1 1 
ATOM   1208 C CE2 . PHE   A 1 159 ? 15.845  13.312  14.958 1.00 36.39  ? 159 PHE   A CE2 1 
ATOM   1209 C CZ  . PHE   A 1 159 ? 15.314  12.983  16.187 1.00 42.33  ? 159 PHE   A CZ  1 
ATOM   1210 N N   . CYS   A 1 160 ? 15.868  6.813   12.327 1.00 31.60  ? 160 CYS   A N   1 
ATOM   1211 C CA  . CYS   A 1 160 ? 15.746  5.748   11.334 1.00 34.31  ? 160 CYS   A CA  1 
ATOM   1212 C C   . CYS   A 1 160 ? 14.396  5.041   11.310 1.00 38.64  ? 160 CYS   A C   1 
ATOM   1213 O O   . CYS   A 1 160 ? 14.108  4.353   10.323 1.00 32.37  ? 160 CYS   A O   1 
ATOM   1214 C CB  . CYS   A 1 160 ? 16.842  4.692   11.545 1.00 35.74  ? 160 CYS   A CB  1 
ATOM   1215 S SG  . CYS   A 1 160 ? 16.868  3.950   13.191 1.00 38.09  ? 160 CYS   A SG  1 
ATOM   1216 N N   . TYR   A 1 161 ? 13.560  5.180   12.337 1.00 31.55  ? 161 TYR   A N   1 
ATOM   1217 C CA  . TYR   A 1 161 ? 12.338  4.395   12.430 1.00 31.84  ? 161 TYR   A CA  1 
ATOM   1218 C C   . TYR   A 1 161 ? 11.245  5.220   13.084 1.00 27.26  ? 161 TYR   A C   1 
ATOM   1219 O O   . TYR   A 1 161 ? 11.500  5.944   14.046 1.00 32.91  ? 161 TYR   A O   1 
ATOM   1220 C CB  . TYR   A 1 161 ? 12.574  3.103   13.228 1.00 29.20  ? 161 TYR   A CB  1 
ATOM   1221 C CG  . TYR   A 1 161 ? 11.330  2.278   13.480 1.00 32.68  ? 161 TYR   A CG  1 
ATOM   1222 C CD1 . TYR   A 1 161 ? 10.842  1.420   12.508 1.00 37.21  ? 161 TYR   A CD1 1 
ATOM   1223 C CD2 . TYR   A 1 161 ? 10.655  2.343   14.697 1.00 31.28  ? 161 TYR   A CD2 1 
ATOM   1224 C CE1 . TYR   A 1 161 ? 9.717   0.659   12.726 1.00 34.71  ? 161 TYR   A CE1 1 
ATOM   1225 C CE2 . TYR   A 1 161 ? 9.519   1.580   14.925 1.00 28.68  ? 161 TYR   A CE2 1 
ATOM   1226 C CZ  . TYR   A 1 161 ? 9.056   0.741   13.930 1.00 33.51  ? 161 TYR   A CZ  1 
ATOM   1227 O OH  . TYR   A 1 161 ? 7.933   -0.030  14.126 1.00 32.56  ? 161 TYR   A OH  1 
ATOM   1228 N N   . MET   A 1 162 ? 10.035  5.124   12.540 1.00 33.27  ? 162 MET   A N   1 
ATOM   1229 C CA  . MET   A 1 162 ? 8.843   5.670   13.173 1.00 34.33  ? 162 MET   A CA  1 
ATOM   1230 C C   . MET   A 1 162 ? 7.782   4.582   13.208 1.00 35.43  ? 162 MET   A C   1 
ATOM   1231 O O   . MET   A 1 162 ? 7.496   3.959   12.181 1.00 33.05  ? 162 MET   A O   1 
ATOM   1232 C CB  . MET   A 1 162 ? 8.311   6.906   12.445 1.00 37.94  ? 162 MET   A CB  1 
ATOM   1233 C CG  . MET   A 1 162 ? 7.184   7.588   13.212 1.00 39.78  ? 162 MET   A CG  1 
ATOM   1234 S SD  . MET   A 1 162 ? 6.612   9.125   12.477 1.00 42.36  ? 162 MET   A SD  1 
ATOM   1235 C CE  . MET   A 1 162 ? 5.865   8.468   11.003 1.00 40.70  ? 162 MET   A CE  1 
ATOM   1236 N N   . HIS   A 1 163 ? 7.203   4.359   14.383 1.00 28.90  ? 163 HIS   A N   1 
ATOM   1237 C CA  . HIS   A 1 163 ? 6.318   3.220   14.574 1.00 33.58  ? 163 HIS   A CA  1 
ATOM   1238 C C   . HIS   A 1 163 ? 4.963   3.478   13.926 1.00 36.72  ? 163 HIS   A C   1 
ATOM   1239 O O   . HIS   A 1 163 ? 4.385   4.560   14.071 1.00 36.98  ? 163 HIS   A O   1 
ATOM   1240 C CB  . HIS   A 1 163 ? 6.150   2.929   16.065 1.00 33.61  ? 163 HIS   A CB  1 
ATOM   1241 C CG  . HIS   A 1 163 ? 5.317   1.721   16.350 1.00 35.92  ? 163 HIS   A CG  1 
ATOM   1242 N ND1 . HIS   A 1 163 ? 5.584   0.486   15.797 1.00 31.25  ? 163 HIS   A ND1 1 
ATOM   1243 C CD2 . HIS   A 1 163 ? 4.222   1.556   17.128 1.00 34.76  ? 163 HIS   A CD2 1 
ATOM   1244 C CE1 . HIS   A 1 163 ? 4.689   -0.387  16.221 1.00 36.12  ? 163 HIS   A CE1 1 
ATOM   1245 N NE2 . HIS   A 1 163 ? 3.854   0.236   17.031 1.00 32.93  ? 163 HIS   A NE2 1 
ATOM   1246 N N   . HIS   A 1 164 ? 4.462   2.477   13.203 1.00 33.01  ? 164 HIS   A N   1 
ATOM   1247 C CA  . HIS   A 1 164 ? 3.187   2.583   12.502 1.00 38.52  ? 164 HIS   A CA  1 
ATOM   1248 C C   . HIS   A 1 164 ? 2.152   1.565   12.948 1.00 29.97  ? 164 HIS   A C   1 
ATOM   1249 O O   . HIS   A 1 164 ? 0.973   1.912   13.053 1.00 36.27  ? 164 HIS   A O   1 
ATOM   1250 C CB  . HIS   A 1 164 ? 3.387   2.448   10.982 1.00 34.03  ? 164 HIS   A CB  1 
ATOM   1251 C CG  . HIS   A 1 164 ? 3.731   3.733   10.295 1.00 35.53  ? 164 HIS   A CG  1 
ATOM   1252 N ND1 . HIS   A 1 164 ? 4.944   4.366   10.464 1.00 40.59  ? 164 HIS   A ND1 1 
ATOM   1253 C CD2 . HIS   A 1 164 ? 3.025   4.498   9.430  1.00 32.23  ? 164 HIS   A CD2 1 
ATOM   1254 C CE1 . HIS   A 1 164 ? 4.967   5.469   9.738  1.00 34.92  ? 164 HIS   A CE1 1 
ATOM   1255 N NE2 . HIS   A 1 164 ? 3.816   5.571   9.098  1.00 36.59  ? 164 HIS   A NE2 1 
ATOM   1256 N N   . MET   A 1 165 ? 2.539   0.316   13.204 1.00 39.38  ? 165 MET   A N   1 
ATOM   1257 C CA  . MET   A 1 165 ? 1.521   -0.708  13.401 1.00 36.05  ? 165 MET   A CA  1 
ATOM   1258 C C   . MET   A 1 165 ? 2.121   -1.965  14.012 1.00 43.48  ? 165 MET   A C   1 
ATOM   1259 O O   . MET   A 1 165 ? 3.338   -2.174  14.002 1.00 33.25  ? 165 MET   A O   1 
ATOM   1260 C CB  . MET   A 1 165 ? 0.834   -1.053  12.078 1.00 41.67  ? 165 MET   A CB  1 
ATOM   1261 C CG  . MET   A 1 165 ? 1.755   -1.727  11.087 1.00 44.88  ? 165 MET   A CG  1 
ATOM   1262 S SD  . MET   A 1 165 ? 1.039   -1.821  9.440  1.00 59.24  ? 165 MET   A SD  1 
ATOM   1263 C CE  . MET   A 1 165 ? 1.893   -3.254  8.800  1.00 52.19  ? 165 MET   A CE  1 
ATOM   1264 N N   . GLU   A 1 166 ? 1.231   -2.803  14.540 1.00 40.02  ? 166 GLU   A N   1 
ATOM   1265 C CA  . GLU   A 1 166 ? 1.566   -4.124  15.046 1.00 44.95  ? 166 GLU   A CA  1 
ATOM   1266 C C   . GLU   A 1 166 ? 0.968   -5.176  14.125 1.00 43.25  ? 166 GLU   A C   1 
ATOM   1267 O O   . GLU   A 1 166 ? -0.173  -5.044  13.673 1.00 46.51  ? 166 GLU   A O   1 
ATOM   1268 C CB  . GLU   A 1 166 ? 1.046   -4.322  16.475 1.00 40.74  ? 166 GLU   A CB  1 
ATOM   1269 C CG  . GLU   A 1 166 ? 1.286   -5.719  17.032 1.00 42.26  ? 166 GLU   A CG  1 
ATOM   1270 C CD  . GLU   A 1 166 ? 1.019   -5.809  18.524 1.00 50.20  ? 166 GLU   A CD  1 
ATOM   1271 O OE1 . GLU   A 1 166 ? 1.501   -4.935  19.278 1.00 49.33  ? 166 GLU   A OE1 1 
ATOM   1272 O OE2 . GLU   A 1 166 ? 0.323   -6.755  18.944 1.00 55.58  ? 166 GLU   A OE2 1 
ATOM   1273 N N   . LEU   A 1 167 ? 1.742   -6.200  13.843 1.00 42.50  ? 167 LEU   A N   1 
ATOM   1274 C CA  . LEU   A 1 167 ? 1.302   -7.279  12.977 1.00 51.77  ? 167 LEU   A CA  1 
ATOM   1275 C C   . LEU   A 1 167 ? 0.668   -8.394  13.801 1.00 60.45  ? 167 LEU   A C   1 
ATOM   1276 O O   . LEU   A 1 167 ? 0.856   -8.462  15.021 1.00 50.83  ? 167 LEU   A O   1 
ATOM   1277 C CB  . LEU   A 1 167 ? 2.485   -7.801  12.165 1.00 50.13  ? 167 LEU   A CB  1 
ATOM   1278 C CG  . LEU   A 1 167 ? 2.991   -6.781  11.142 1.00 46.08  ? 167 LEU   A CG  1 
ATOM   1279 C CD1 . LEU   A 1 167 ? 4.353   -7.182  10.604 1.00 45.65  ? 167 LEU   A CD1 1 
ATOM   1280 C CD2 . LEU   A 1 167 ? 1.988   -6.632  10.009 1.00 49.04  ? 167 LEU   A CD2 1 
ATOM   1281 N N   . PRO   A 1 168 ? -0.114  -9.273  13.163 1.00 63.34  ? 168 PRO   A N   1 
ATOM   1282 C CA  . PRO   A 1 168 ? -0.829  -10.310 13.928 1.00 54.28  ? 168 PRO   A CA  1 
ATOM   1283 C C   . PRO   A 1 168 ? 0.068   -11.196 14.774 1.00 55.23  ? 168 PRO   A C   1 
ATOM   1284 O O   . PRO   A 1 168 ? -0.382  -11.702 15.809 1.00 64.89  ? 168 PRO   A O   1 
ATOM   1285 C CB  . PRO   A 1 168 ? -1.539  -11.112 12.830 1.00 65.08  ? 168 PRO   A CB  1 
ATOM   1286 C CG  . PRO   A 1 168 ? -1.767  -10.111 11.743 1.00 64.60  ? 168 PRO   A CG  1 
ATOM   1287 C CD  . PRO   A 1 168 ? -0.551  -9.231  11.755 1.00 58.78  ? 168 PRO   A CD  1 
ATOM   1288 N N   . THR   A 1 169 ? 1.320   -11.400 14.376 1.00 53.26  ? 169 THR   A N   1 
ATOM   1289 C CA  . THR   A 1 169 ? 2.238   -12.243 15.129 1.00 59.48  ? 169 THR   A CA  1 
ATOM   1290 C C   . THR   A 1 169 ? 2.896   -11.506 16.296 1.00 55.80  ? 169 THR   A C   1 
ATOM   1291 O O   . THR   A 1 169 ? 3.798   -12.060 16.935 1.00 55.57  ? 169 THR   A O   1 
ATOM   1292 C CB  . THR   A 1 169 ? 3.308   -12.818 14.194 1.00 65.66  ? 169 THR   A CB  1 
ATOM   1293 O OG1 . THR   A 1 169 ? 4.347   -13.437 14.964 1.00 67.57  ? 169 THR   A OG1 1 
ATOM   1294 C CG2 . THR   A 1 169 ? 3.898   -11.725 13.312 1.00 58.19  ? 169 THR   A CG2 1 
ATOM   1295 N N   . GLY   A 1 170 ? 2.465   -10.280 16.590 1.00 54.31  ? 170 GLY   A N   1 
ATOM   1296 C CA  . GLY   A 1 170 ? 2.981   -9.537  17.719 1.00 51.20  ? 170 GLY   A CA  1 
ATOM   1297 C C   . GLY   A 1 170 ? 4.244   -8.748  17.449 1.00 43.53  ? 170 GLY   A C   1 
ATOM   1298 O O   . GLY   A 1 170 ? 4.784   -8.142  18.380 1.00 43.42  ? 170 GLY   A O   1 
ATOM   1299 N N   . VAL   A 1 171 ? 4.734   -8.731  16.216 1.00 47.35  ? 171 VAL   A N   1 
ATOM   1300 C CA  . VAL   A 1 171 ? 5.877   -7.926  15.860 1.00 43.29  ? 171 VAL   A CA  1 
ATOM   1301 C C   . VAL   A 1 171 ? 5.389   -6.605  15.277 1.00 39.93  ? 171 VAL   A C   1 
ATOM   1302 O O   . VAL   A 1 171 ? 4.200   -6.406  15.030 1.00 36.79  ? 171 VAL   A O   1 
ATOM   1303 C CB  . VAL   A 1 171 ? 6.826   -8.664  14.889 1.00 45.59  ? 171 VAL   A CB  1 
ATOM   1304 C CG1 . VAL   A 1 171 ? 7.365   -9.927  15.551 1.00 53.70  ? 171 VAL   A CG1 1 
ATOM   1305 C CG2 . VAL   A 1 171 ? 6.107   -8.981  13.589 1.00 41.27  ? 171 VAL   A CG2 1 
ATOM   1306 N N   . HIS   A 1 172 ? 6.324   -5.691  15.038 1.00 35.70  ? 172 HIS   A N   1 
ATOM   1307 C CA  . HIS   A 1 172 ? 5.987   -4.312  14.731 1.00 33.89  ? 172 HIS   A CA  1 
ATOM   1308 C C   . HIS   A 1 172 ? 6.647   -3.883  13.428 1.00 37.19  ? 172 HIS   A C   1 
ATOM   1309 O O   . HIS   A 1 172 ? 7.725   -4.366  13.063 1.00 34.26  ? 172 HIS   A O   1 
ATOM   1310 C CB  . HIS   A 1 172 ? 6.400   -3.406  15.897 1.00 34.26  ? 172 HIS   A CB  1 
ATOM   1311 C CG  . HIS   A 1 172 ? 5.818   -3.829  17.211 1.00 36.18  ? 172 HIS   A CG  1 
ATOM   1312 N ND1 . HIS   A 1 172 ? 6.563   -4.445  18.194 1.00 32.57  ? 172 HIS   A ND1 1 
ATOM   1313 C CD2 . HIS   A 1 172 ? 4.550   -3.766  17.683 1.00 35.01  ? 172 HIS   A CD2 1 
ATOM   1314 C CE1 . HIS   A 1 172 ? 5.784   -4.720  19.225 1.00 36.45  ? 172 HIS   A CE1 1 
ATOM   1315 N NE2 . HIS   A 1 172 ? 4.558   -4.319  18.940 1.00 32.97  ? 172 HIS   A NE2 1 
ATOM   1316 N N   . ALA   A 1 173 ? 5.970   -2.984  12.721 1.00 32.70  ? 173 ALA   A N   1 
ATOM   1317 C CA  . ALA   A 1 173 ? 6.434   -2.475  11.441 1.00 32.94  ? 173 ALA   A CA  1 
ATOM   1318 C C   . ALA   A 1 173 ? 6.263   -0.965  11.419 1.00 34.17  ? 173 ALA   A C   1 
ATOM   1319 O O   . ALA   A 1 173 ? 5.383   -0.416  12.088 1.00 28.81  ? 173 ALA   A O   1 
ATOM   1320 C CB  . ALA   A 1 173 ? 5.677   -3.114  10.267 1.00 32.74  ? 173 ALA   A CB  1 
ATOM   1321 N N   . GLY   A 1 174 ? 7.115   -0.303  10.648 1.00 30.02  ? 174 GLY   A N   1 
ATOM   1322 C CA  . GLY   A 1 174 ? 7.058   1.140   10.539 1.00 36.68  ? 174 GLY   A CA  1 
ATOM   1323 C C   . GLY   A 1 174 ? 7.883   1.617   9.364  1.00 34.11  ? 174 GLY   A C   1 
ATOM   1324 O O   . GLY   A 1 174 ? 8.319   0.826   8.530  1.00 31.95  ? 174 GLY   A O   1 
ATOM   1325 N N   . THR   A 1 175 ? 8.105   2.927   9.312  1.00 36.11  ? 175 THR   A N   1 
ATOM   1326 C CA  . THR   A 1 175 ? 8.779   3.539   8.176  1.00 35.79  ? 175 THR   A CA  1 
ATOM   1327 C C   . THR   A 1 175 ? 10.079  4.203   8.612  1.00 35.73  ? 175 THR   A C   1 
ATOM   1328 O O   . THR   A 1 175 ? 10.416  4.261   9.799  1.00 37.54  ? 175 THR   A O   1 
ATOM   1329 C CB  . THR   A 1 175 ? 7.879   4.577   7.489  1.00 36.71  ? 175 THR   A CB  1 
ATOM   1330 O OG1 . THR   A 1 175 ? 7.705   5.712   8.350  1.00 37.63  ? 175 THR   A OG1 1 
ATOM   1331 C CG2 . THR   A 1 175 ? 6.522   3.977   7.162  1.00 35.51  ? 175 THR   A CG2 1 
ATOM   1332 N N   . ASP   A 1 176 ? 10.818  4.691   7.618  1.00 29.81  ? 176 ASP   A N   1 
ATOM   1333 C CA  . ASP   A 1 176 ? 11.872  5.655   7.868  1.00 35.98  ? 176 ASP   A CA  1 
ATOM   1334 C C   . ASP   A 1 176 ? 11.243  7.040   7.991  1.00 33.77  ? 176 ASP   A C   1 
ATOM   1335 O O   . ASP   A 1 176 ? 10.029  7.209   7.848  1.00 34.61  ? 176 ASP   A O   1 
ATOM   1336 C CB  . ASP   A 1 176 ? 12.933  5.600   6.766  1.00 37.61  ? 176 ASP   A CB  1 
ATOM   1337 C CG  . ASP   A 1 176 ? 12.355  5.771   5.363  1.00 39.69  ? 176 ASP   A CG  1 
ATOM   1338 O OD1 . ASP   A 1 176 ? 11.437  6.601   5.171  1.00 36.71  ? 176 ASP   A OD1 1 
ATOM   1339 O OD2 . ASP   A 1 176 ? 12.849  5.093   4.434  1.00 40.24  ? 176 ASP   A OD2 1 
ATOM   1340 N N   . LEU   A 1 177 ? 12.066  8.052   8.242  1.00 34.19  ? 177 LEU   A N   1 
ATOM   1341 C CA  . LEU   A 1 177 ? 11.505  9.378   8.462  1.00 38.00  ? 177 LEU   A CA  1 
ATOM   1342 C C   . LEU   A 1 177 ? 11.109  10.074  7.168  1.00 41.32  ? 177 LEU   A C   1 
ATOM   1343 O O   . LEU   A 1 177 ? 10.603  11.200  7.220  1.00 45.77  ? 177 LEU   A O   1 
ATOM   1344 C CB  . LEU   A 1 177 ? 12.482  10.239  9.266  1.00 36.80  ? 177 LEU   A CB  1 
ATOM   1345 C CG  . LEU   A 1 177 ? 12.276  10.195  10.785 1.00 41.17  ? 177 LEU   A CG  1 
ATOM   1346 C CD1 . LEU   A 1 177 ? 10.975  10.875  11.178 1.00 41.56  ? 177 LEU   A CD1 1 
ATOM   1347 C CD2 . LEU   A 1 177 ? 12.302  8.760   11.326 1.00 35.28  ? 177 LEU   A CD2 1 
ATOM   1348 N N   . GLU   A 1 178 ? 11.298  9.430   6.018  1.00 39.57  ? 178 GLU   A N   1 
ATOM   1349 C CA  . GLU   A 1 178 ? 10.758  9.922   4.760  1.00 41.05  ? 178 GLU   A CA  1 
ATOM   1350 C C   . GLU   A 1 178 ? 9.465   9.220   4.362  1.00 41.66  ? 178 GLU   A C   1 
ATOM   1351 O O   . GLU   A 1 178 ? 8.955   9.461   3.264  1.00 46.58  ? 178 GLU   A O   1 
ATOM   1352 C CB  . GLU   A 1 178 ? 11.799  9.776   3.647  1.00 44.43  ? 178 GLU   A CB  1 
ATOM   1353 C CG  . GLU   A 1 178 ? 13.040  10.631  3.855  1.00 45.53  ? 178 GLU   A CG  1 
ATOM   1354 C CD  . GLU   A 1 178 ? 14.045  10.485  2.727  1.00 70.12  ? 178 GLU   A CD  1 
ATOM   1355 O OE1 . GLU   A 1 178 ? 13.873  9.572   1.888  1.00 65.17  ? 178 GLU   A OE1 1 
ATOM   1356 O OE2 . GLU   A 1 178 ? 15.004  11.288  2.679  1.00 64.99  ? 178 GLU   A OE2 1 
ATOM   1357 N N   . GLY   A 1 179 ? 8.929   8.352   5.220  1.00 42.35  ? 179 GLY   A N   1 
ATOM   1358 C CA  . GLY   A 1 179 ? 7.641   7.733   4.991  1.00 40.63  ? 179 GLY   A CA  1 
ATOM   1359 C C   . GLY   A 1 179 ? 7.658   6.394   4.290  1.00 38.45  ? 179 GLY   A C   1 
ATOM   1360 O O   . GLY   A 1 179 ? 6.583   5.854   4.009  1.00 33.29  ? 179 GLY   A O   1 
ATOM   1361 N N   . ASN   A 1 180 ? 8.827   5.840   3.997  1.00 37.77  ? 180 ASN   A N   1 
ATOM   1362 C CA  . ASN   A 1 180 ? 8.915   4.575   3.281  1.00 36.97  ? 180 ASN   A CA  1 
ATOM   1363 C C   . ASN   A 1 180 ? 8.967   3.431   4.283  1.00 34.84  ? 180 ASN   A C   1 
ATOM   1364 O O   . ASN   A 1 180 ? 9.867   3.383   5.129  1.00 38.15  ? 180 ASN   A O   1 
ATOM   1365 C CB  . ASN   A 1 180 ? 10.142  4.553   2.373  1.00 43.61  ? 180 ASN   A CB  1 
ATOM   1366 C CG  . ASN   A 1 180 ? 10.191  5.745   1.439  1.00 41.84  ? 180 ASN   A CG  1 
ATOM   1367 O OD1 . ASN   A 1 180 ? 9.419   5.830   0.486  1.00 47.49  ? 180 ASN   A OD1 1 
ATOM   1368 N ND2 . ASN   A 1 180 ? 11.102  6.675   1.710  1.00 45.00  ? 180 ASN   A ND2 1 
ATOM   1369 N N   . PHE   A 1 181 ? 8.001   2.521   4.191  1.00 34.46  ? 181 PHE   A N   1 
ATOM   1370 C CA  . PHE   A 1 181 ? 7.966   1.387   5.103  1.00 39.05  ? 181 PHE   A CA  1 
ATOM   1371 C C   . PHE   A 1 181 ? 9.218   0.539   4.941  1.00 42.72  ? 181 PHE   A C   1 
ATOM   1372 O O   . PHE   A 1 181 ? 9.734   0.367   3.833  1.00 38.94  ? 181 PHE   A O   1 
ATOM   1373 C CB  . PHE   A 1 181 ? 6.724   0.527   4.847  1.00 37.87  ? 181 PHE   A CB  1 
ATOM   1374 C CG  . PHE   A 1 181 ? 5.576   0.816   5.781  1.00 32.23  ? 181 PHE   A CG  1 
ATOM   1375 C CD1 . PHE   A 1 181 ? 5.521   0.233   7.038  1.00 32.96  ? 181 PHE   A CD1 1 
ATOM   1376 C CD2 . PHE   A 1 181 ? 4.542   1.653   5.392  1.00 35.83  ? 181 PHE   A CD2 1 
ATOM   1377 C CE1 . PHE   A 1 181 ? 4.457   0.495   7.902  1.00 35.79  ? 181 PHE   A CE1 1 
ATOM   1378 C CE2 . PHE   A 1 181 ? 3.480   1.921   6.245  1.00 36.20  ? 181 PHE   A CE2 1 
ATOM   1379 C CZ  . PHE   A 1 181 ? 3.436   1.339   7.502  1.00 33.82  ? 181 PHE   A CZ  1 
ATOM   1380 N N   . TYR   A 1 182 ? 9.724   0.034   6.061  1.00 34.04  ? 182 TYR   A N   1 
ATOM   1381 C CA  . TYR   A 1 182 ? 10.639  -1.095  6.021  1.00 36.88  ? 182 TYR   A CA  1 
ATOM   1382 C C   . TYR   A 1 182 ? 9.819   -2.339  5.701  1.00 35.13  ? 182 TYR   A C   1 
ATOM   1383 O O   . TYR   A 1 182 ? 8.857   -2.653  6.410  1.00 35.86  ? 182 TYR   A O   1 
ATOM   1384 C CB  . TYR   A 1 182 ? 11.382  -1.247  7.348  1.00 30.16  ? 182 TYR   A CB  1 
ATOM   1385 C CG  . TYR   A 1 182 ? 12.359  -0.132  7.657  1.00 37.69  ? 182 TYR   A CG  1 
ATOM   1386 C CD1 . TYR   A 1 182 ? 13.658  -0.152  7.148  1.00 32.08  ? 182 TYR   A CD1 1 
ATOM   1387 C CD2 . TYR   A 1 182 ? 11.991  0.933   8.473  1.00 32.13  ? 182 TYR   A CD2 1 
ATOM   1388 C CE1 . TYR   A 1 182 ? 14.558  0.862   7.436  1.00 33.74  ? 182 TYR   A CE1 1 
ATOM   1389 C CE2 . TYR   A 1 182 ? 12.883  1.950   8.767  1.00 35.14  ? 182 TYR   A CE2 1 
ATOM   1390 C CZ  . TYR   A 1 182 ? 14.167  1.909   8.245  1.00 38.10  ? 182 TYR   A CZ  1 
ATOM   1391 O OH  . TYR   A 1 182 ? 15.055  2.919   8.535  1.00 31.97  ? 182 TYR   A OH  1 
ATOM   1392 N N   . GLY   A 1 183 ? 10.162  -3.017  4.612  1.00 36.24  ? 183 GLY   A N   1 
ATOM   1393 C CA  . GLY   A 1 183 ? 9.473   -4.224  4.222  1.00 34.50  ? 183 GLY   A CA  1 
ATOM   1394 C C   . GLY   A 1 183 ? 8.303   -3.985  3.291  1.00 40.01  ? 183 GLY   A C   1 
ATOM   1395 O O   . GLY   A 1 183 ? 8.088   -2.883  2.775  1.00 40.13  ? 183 GLY   A O   1 
ATOM   1396 N N   . PRO   A 1 184 ? 7.518   -5.039  3.058  1.00 36.49  ? 184 PRO   A N   1 
ATOM   1397 C CA  . PRO   A 1 184 ? 6.387   -4.968  2.125  1.00 39.21  ? 184 PRO   A CA  1 
ATOM   1398 C C   . PRO   A 1 184 ? 5.089   -4.463  2.737  1.00 45.26  ? 184 PRO   A C   1 
ATOM   1399 O O   . PRO   A 1 184 ? 4.041   -4.579  2.093  1.00 46.97  ? 184 PRO   A O   1 
ATOM   1400 C CB  . PRO   A 1 184 ? 6.231   -6.436  1.717  1.00 36.04  ? 184 PRO   A CB  1 
ATOM   1401 C CG  . PRO   A 1 184 ? 6.541   -7.162  2.992  1.00 38.39  ? 184 PRO   A CG  1 
ATOM   1402 C CD  . PRO   A 1 184 ? 7.645   -6.375  3.664  1.00 40.02  ? 184 PRO   A CD  1 
ATOM   1403 N N   . PHE   A 1 185 ? 5.133   -3.924  3.947  1.00 40.35  ? 185 PHE   A N   1 
ATOM   1404 C CA  . PHE   A 1 185 ? 3.923   -3.637  4.694  1.00 43.79  ? 185 PHE   A CA  1 
ATOM   1405 C C   . PHE   A 1 185 ? 3.300   -2.321  4.243  1.00 39.16  ? 185 PHE   A C   1 
ATOM   1406 O O   . PHE   A 1 185 ? 3.965   -1.433  3.704  1.00 38.04  ? 185 PHE   A O   1 
ATOM   1407 C CB  . PHE   A 1 185 ? 4.231   -3.610  6.188  1.00 40.42  ? 185 PHE   A CB  1 
ATOM   1408 C CG  . PHE   A 1 185 ? 5.016   -4.799  6.653  1.00 40.24  ? 185 PHE   A CG  1 
ATOM   1409 C CD1 . PHE   A 1 185 ? 4.441   -6.059  6.663  1.00 39.09  ? 185 PHE   A CD1 1 
ATOM   1410 C CD2 . PHE   A 1 185 ? 6.330   -4.663  7.066  1.00 32.02  ? 185 PHE   A CD2 1 
ATOM   1411 C CE1 . PHE   A 1 185 ? 5.160   -7.159  7.079  1.00 45.80  ? 185 PHE   A CE1 1 
ATOM   1412 C CE2 . PHE   A 1 185 ? 7.055   -5.760  7.487  1.00 41.46  ? 185 PHE   A CE2 1 
ATOM   1413 C CZ  . PHE   A 1 185 ? 6.470   -7.011  7.493  1.00 41.71  ? 185 PHE   A CZ  1 
ATOM   1414 N N   . VAL   A 1 186 ? 1.994   -2.212  4.467  1.00 44.88  ? 186 VAL   A N   1 
ATOM   1415 C CA  . VAL   A 1 186 ? 1.219   -1.044  4.081  1.00 36.31  ? 186 VAL   A CA  1 
ATOM   1416 C C   . VAL   A 1 186 ? 0.378   -0.607  5.269  1.00 39.64  ? 186 VAL   A C   1 
ATOM   1417 O O   . VAL   A 1 186 ? 0.034   -1.412  6.141  1.00 36.02  ? 186 VAL   A O   1 
ATOM   1418 C CB  . VAL   A 1 186 ? 0.323   -1.330  2.858  1.00 45.69  ? 186 VAL   A CB  1 
ATOM   1419 C CG1 . VAL   A 1 186 ? 1.160   -1.392  1.590  1.00 46.74  ? 186 VAL   A CG1 1 
ATOM   1420 C CG2 . VAL   A 1 186 ? -0.437  -2.633  3.061  1.00 41.89  ? 186 VAL   A CG2 1 
ATOM   1421 N N   . ASP   A 1 187 ? 0.045   0.683   5.302  1.00 35.76  ? 187 ASP   A N   1 
ATOM   1422 C CA  . ASP   A 1 187 ? -0.778  1.225   6.382  1.00 33.21  ? 187 ASP   A CA  1 
ATOM   1423 C C   . ASP   A 1 187 ? -2.252  1.169   5.976  1.00 35.56  ? 187 ASP   A C   1 
ATOM   1424 O O   . ASP   A 1 187 ? -2.919  2.178   5.739  1.00 35.81  ? 187 ASP   A O   1 
ATOM   1425 C CB  . ASP   A 1 187 ? -0.331  2.636   6.752  1.00 35.03  ? 187 ASP   A CB  1 
ATOM   1426 C CG  . ASP   A 1 187 ? -0.146  3.543   5.542  1.00 38.15  ? 187 ASP   A CG  1 
ATOM   1427 O OD1 . ASP   A 1 187 ? -0.245  3.062   4.398  1.00 34.72  ? 187 ASP   A OD1 1 
ATOM   1428 O OD2 . ASP   A 1 187 ? 0.098   4.752   5.747  1.00 35.72  ? 187 ASP   A OD2 1 
ATOM   1429 N N   . ARG   A 1 188 ? -2.744  -0.066  5.886  1.00 33.55  ? 188 ARG   A N   1 
ATOM   1430 C CA  . ARG   A 1 188 ? -4.164  -0.351  5.741  1.00 44.00  ? 188 ARG   A CA  1 
ATOM   1431 C C   . ARG   A 1 188 ? -4.455  -1.691  6.403  1.00 43.84  ? 188 ARG   A C   1 
ATOM   1432 O O   . ARG   A 1 188 ? -3.547  -2.473  6.693  1.00 40.37  ? 188 ARG   A O   1 
ATOM   1433 C CB  . ARG   A 1 188 ? -4.614  -0.362  4.270  1.00 49.03  ? 188 ARG   A CB  1 
ATOM   1434 C CG  . ARG   A 1 188 ? -3.808  -1.255  3.336  1.00 48.71  ? 188 ARG   A CG  1 
ATOM   1435 C CD  . ARG   A 1 188 ? -4.317  -1.139  1.895  1.00 57.04  ? 188 ARG   A CD  1 
ATOM   1436 N NE  . ARG   A 1 188 ? -3.281  -1.460  0.919  1.00 58.08  ? 188 ARG   A NE  1 
ATOM   1437 C CZ  . ARG   A 1 188 ? -2.514  -0.560  0.316  1.00 62.02  ? 188 ARG   A CZ  1 
ATOM   1438 N NH1 . ARG   A 1 188 ? -2.657  0.736   0.546  1.00 65.70  ? 188 ARG   A NH1 1 
ATOM   1439 N NH2 . ARG   A 1 188 ? -1.582  -0.969  -0.542 1.00 59.34  ? 188 ARG   A NH2 1 
ATOM   1440 N N   . GLN   A 1 189 ? -5.740  -1.945  6.645  1.00 50.31  ? 189 GLN   A N   1 
ATOM   1441 C CA  . GLN   A 1 189 ? -6.188  -3.177  7.294  1.00 45.80  ? 189 GLN   A CA  1 
ATOM   1442 C C   . GLN   A 1 189 ? -6.373  -4.249  6.226  1.00 55.35  ? 189 GLN   A C   1 
ATOM   1443 O O   . GLN   A 1 189 ? -7.458  -4.422  5.667  1.00 56.15  ? 189 GLN   A O   1 
ATOM   1444 C CB  . GLN   A 1 189 ? -7.471  -2.934  8.077  1.00 48.61  ? 189 GLN   A CB  1 
ATOM   1445 C CG  . GLN   A 1 189 ? -7.937  -4.136  8.869  1.00 60.00  ? 189 GLN   A CG  1 
ATOM   1446 C CD  . GLN   A 1 189 ? -6.850  -4.694  9.771  1.00 65.56  ? 189 GLN   A CD  1 
ATOM   1447 O OE1 . GLN   A 1 189 ? -6.366  -5.811  9.566  1.00 55.17  ? 189 GLN   A OE1 1 
ATOM   1448 N NE2 . GLN   A 1 189 ? -6.459  -3.915  10.775 1.00 60.50  ? 189 GLN   A NE2 1 
ATOM   1449 N N   . THR   A 1 190 ? -5.295  -4.976  5.938  1.00 55.52  ? 190 THR   A N   1 
ATOM   1450 C CA  . THR   A 1 190 ? -5.309  -6.085  4.995  1.00 57.77  ? 190 THR   A CA  1 
ATOM   1451 C C   . THR   A 1 190 ? -4.633  -7.281  5.654  1.00 60.10  ? 190 THR   A C   1 
ATOM   1452 O O   . THR   A 1 190 ? -4.199  -7.215  6.807  1.00 63.08  ? 190 THR   A O   1 
ATOM   1453 C CB  . THR   A 1 190 ? -4.615  -5.714  3.678  1.00 57.33  ? 190 THR   A CB  1 
ATOM   1454 O OG1 . THR   A 1 190 ? -4.687  -4.297  3.486  1.00 67.35  ? 190 THR   A OG1 1 
ATOM   1455 C CG2 . THR   A 1 190 ? -5.296  -6.405  2.502  1.00 56.27  ? 190 THR   A CG2 1 
ATOM   1456 N N   . ALA   A 1 191 ? -4.536  -8.382  4.911  1.00 64.69  ? 191 ALA   A N   1 
ATOM   1457 C CA  . ALA   A 1 191 ? -3.991  -9.629  5.446  1.00 61.55  ? 191 ALA   A CA  1 
ATOM   1458 C C   . ALA   A 1 191 ? -2.491  -9.740  5.157  1.00 67.88  ? 191 ALA   A C   1 
ATOM   1459 O O   . ALA   A 1 191 ? -2.003  -10.714 4.585  1.00 75.90  ? 191 ALA   A O   1 
ATOM   1460 C CB  . ALA   A 1 191 ? -4.756  -10.820 4.881  1.00 61.73  ? 191 ALA   A CB  1 
ATOM   1461 N N   . GLN   A 1 192 ? -1.756  -8.713  5.574  1.00 67.15  ? 192 GLN   A N   1 
ATOM   1462 C CA  . GLN   A 1 192 ? -0.305  -8.721  5.457  1.00 64.12  ? 192 GLN   A CA  1 
ATOM   1463 C C   . GLN   A 1 192 ? 0.320   -9.530  6.589  1.00 64.47  ? 192 GLN   A C   1 
ATOM   1464 O O   . GLN   A 1 192 ? -0.217  -9.608  7.700  1.00 56.25  ? 192 GLN   A O   1 
ATOM   1465 C CB  . GLN   A 1 192 ? 0.235   -7.292  5.463  1.00 57.49  ? 192 GLN   A CB  1 
ATOM   1466 C CG  . GLN   A 1 192 ? -0.538  -6.350  6.370  1.00 60.28  ? 192 GLN   A CG  1 
ATOM   1467 C CD  . GLN   A 1 192 ? -0.138  -4.903  6.178  1.00 48.57  ? 192 GLN   A CD  1 
ATOM   1468 O OE1 . GLN   A 1 192 ? 0.880   -4.609  5.554  1.00 43.34  ? 192 GLN   A OE1 1 
ATOM   1469 N NE2 . GLN   A 1 192 ? -0.943  -3.990  6.706  1.00 41.24  ? 192 GLN   A NE2 1 
ATOM   1470 N N   . ALA   A 1 193 ? 1.470   -10.134 6.295  1.00 58.18  ? 193 ALA   A N   1 
ATOM   1471 C CA  . ALA   A 1 193 ? 2.136   -11.002 7.255  1.00 66.45  ? 193 ALA   A CA  1 
ATOM   1472 C C   . ALA   A 1 193 ? 3.646   -10.872 7.113  1.00 61.92  ? 193 ALA   A C   1 
ATOM   1473 O O   . ALA   A 1 193 ? 4.171   -10.685 6.011  1.00 49.73  ? 193 ALA   A O   1 
ATOM   1474 C CB  . ALA   A 1 193 ? 1.717   -12.467 7.078  1.00 60.49  ? 193 ALA   A CB  1 
ATOM   1475 N N   . ALA   A 1 194 ? 4.334   -10.968 8.249  1.00 68.37  ? 194 ALA   A N   1 
ATOM   1476 C CA  . ALA   A 1 194 ? 5.790   -10.976 8.253  1.00 62.82  ? 194 ALA   A CA  1 
ATOM   1477 C C   . ALA   A 1 194 ? 6.309   -12.295 7.691  1.00 68.45  ? 194 ALA   A C   1 
ATOM   1478 O O   . ALA   A 1 194 ? 5.892   -13.375 8.123  1.00 68.41  ? 194 ALA   A O   1 
ATOM   1479 C CB  . ALA   A 1 194 ? 6.322   -10.751 9.670  1.00 58.04  ? 194 ALA   A CB  1 
ATOM   1480 N N   . GLY   A 1 195 ? 7.220   -12.207 6.725  1.00 58.40  ? 195 GLY   A N   1 
ATOM   1481 C CA  . GLY   A 1 195 ? 7.823   -13.392 6.144  1.00 60.16  ? 195 GLY   A CA  1 
ATOM   1482 C C   . GLY   A 1 195 ? 8.674   -14.165 7.136  1.00 59.78  ? 195 GLY   A C   1 
ATOM   1483 O O   . GLY   A 1 195 ? 8.786   -13.766 8.301  1.00 55.81  ? 195 GLY   A O   1 
ATOM   1484 N N   . THR   A 1 196 ? 9.282   -15.272 6.703  1.00 54.26  ? 196 THR   A N   1 
ATOM   1485 C CA  . THR   A 1 196 ? 10.063  -16.087 7.632  1.00 56.57  ? 196 THR   A CA  1 
ATOM   1486 C C   . THR   A 1 196 ? 11.299  -15.328 8.093  1.00 52.47  ? 196 THR   A C   1 
ATOM   1487 O O   . THR   A 1 196 ? 12.122  -14.911 7.274  1.00 54.52  ? 196 THR   A O   1 
ATOM   1488 C CB  . THR   A 1 196 ? 10.473  -17.417 6.994  1.00 49.23  ? 196 THR   A CB  1 
ATOM   1489 O OG1 . THR   A 1 196 ? 11.126  -17.173 5.747  1.00 62.10  ? 196 THR   A OG1 1 
ATOM   1490 C CG2 . THR   A 1 196 ? 9.254   -18.314 6.768  1.00 46.86  ? 196 THR   A CG2 1 
ATOM   1491 N N   . ASP   A 1 197 ? 11.420  -15.120 9.402  1.00 57.91  ? 197 ASP   A N   1 
ATOM   1492 C CA  . ASP   A 1 197 ? 12.589  -14.427 9.921  1.00 58.08  ? 197 ASP   A CA  1 
ATOM   1493 C C   . ASP   A 1 197 ? 13.804  -15.353 9.938  1.00 60.68  ? 197 ASP   A C   1 
ATOM   1494 O O   . ASP   A 1 197 ? 13.691  -16.582 9.983  1.00 61.13  ? 197 ASP   A O   1 
ATOM   1495 C CB  . ASP   A 1 197 ? 12.329  -13.886 11.329 1.00 54.89  ? 197 ASP   A CB  1 
ATOM   1496 C CG  . ASP   A 1 197 ? 13.317  -12.794 11.733 1.00 53.82  ? 197 ASP   A CG  1 
ATOM   1497 O OD1 . ASP   A 1 197 ? 13.961  -12.201 10.841 1.00 51.03  ? 197 ASP   A OD1 1 
ATOM   1498 O OD2 . ASP   A 1 197 ? 13.459  -12.534 12.947 1.00 45.31  ? 197 ASP   A OD2 1 
ATOM   1499 N N   . THR   A 1 198 ? 14.981  -14.742 9.894  1.00 54.21  ? 198 THR   A N   1 
ATOM   1500 C CA  . THR   A 1 198 ? 16.233  -15.471 9.986  1.00 54.33  ? 198 THR   A CA  1 
ATOM   1501 C C   . THR   A 1 198 ? 17.108  -14.825 11.051 1.00 51.00  ? 198 THR   A C   1 
ATOM   1502 O O   . THR   A 1 198 ? 16.890  -13.678 11.449 1.00 50.72  ? 198 THR   A O   1 
ATOM   1503 C CB  . THR   A 1 198 ? 16.959  -15.514 8.630  1.00 51.86  ? 198 THR   A CB  1 
ATOM   1504 O OG1 . THR   A 1 198 ? 17.036  -14.193 8.086  1.00 58.72  ? 198 THR   A OG1 1 
ATOM   1505 C CG2 . THR   A 1 198 ? 16.204  -16.402 7.655  1.00 45.73  ? 198 THR   A CG2 1 
ATOM   1506 N N   . THR   A 1 199 ? 18.096  -15.583 11.522 1.00 47.37  ? 199 THR   A N   1 
ATOM   1507 C CA  . THR   A 1 199 ? 19.012  -15.123 12.558 1.00 47.24  ? 199 THR   A CA  1 
ATOM   1508 C C   . THR   A 1 199 ? 20.186  -14.373 11.934 1.00 45.55  ? 199 THR   A C   1 
ATOM   1509 O O   . THR   A 1 199 ? 20.783  -14.839 10.958 1.00 48.21  ? 199 THR   A O   1 
ATOM   1510 C CB  . THR   A 1 199 ? 19.523  -16.307 13.379 1.00 44.25  ? 199 THR   A CB  1 
ATOM   1511 O OG1 . THR   A 1 199 ? 18.414  -17.068 13.868 1.00 41.22  ? 199 THR   A OG1 1 
ATOM   1512 C CG2 . THR   A 1 199 ? 20.360  -15.820 14.551 1.00 40.33  ? 199 THR   A CG2 1 
ATOM   1513 N N   . ILE   A 1 200 ? 20.517  -13.217 12.504 1.00 33.54  ? 200 ILE   A N   1 
ATOM   1514 C CA  . ILE   A 1 200 ? 21.588  -12.369 11.987 1.00 33.01  ? 200 ILE   A CA  1 
ATOM   1515 C C   . ILE   A 1 200 ? 22.924  -12.962 12.424 1.00 41.72  ? 200 ILE   A C   1 
ATOM   1516 O O   . ILE   A 1 200 ? 23.343  -12.793 13.571 1.00 39.35  ? 200 ILE   A O   1 
ATOM   1517 C CB  . ILE   A 1 200 ? 21.437  -10.923 12.470 1.00 40.31  ? 200 ILE   A CB  1 
ATOM   1518 C CG1 . ILE   A 1 200 ? 20.008  -10.434 12.236 1.00 39.47  ? 200 ILE   A CG1 1 
ATOM   1519 C CG2 . ILE   A 1 200 ? 22.443  -10.016 11.771 1.00 38.65  ? 200 ILE   A CG2 1 
ATOM   1520 C CD1 . ILE   A 1 200 ? 19.624  -9.234  13.089 1.00 44.51  ? 200 ILE   A CD1 1 
ATOM   1521 N N   . THR   A 1 201 ? 23.612  -13.626 11.490 1.00 40.14  ? 201 THR   A N   1 
ATOM   1522 C CA  . THR   A 1 201 ? 24.793  -14.416 11.831 1.00 36.05  ? 201 THR   A CA  1 
ATOM   1523 C C   . THR   A 1 201 ? 25.941  -13.542 12.316 1.00 28.39  ? 201 THR   A C   1 
ATOM   1524 O O   . THR   A 1 201 ? 26.611  -13.873 13.301 1.00 36.29  ? 201 THR   A O   1 
ATOM   1525 C CB  . THR   A 1 201 ? 25.236  -15.237 10.620 1.00 40.42  ? 201 THR   A CB  1 
ATOM   1526 O OG1 . THR   A 1 201 ? 24.153  -16.064 10.180 1.00 43.37  ? 201 THR   A OG1 1 
ATOM   1527 C CG2 . THR   A 1 201 ? 26.431  -16.110 10.984 1.00 42.68  ? 201 THR   A CG2 1 
ATOM   1528 N N   . VAL   A 1 202 ? 26.202  -12.432 11.626 1.00 34.94  ? 202 VAL   A N   1 
ATOM   1529 C CA  . VAL   A 1 202 ? 27.324  -11.588 12.023 1.00 39.02  ? 202 VAL   A CA  1 
ATOM   1530 C C   . VAL   A 1 202 ? 27.088  -11.006 13.412 1.00 35.37  ? 202 VAL   A C   1 
ATOM   1531 O O   . VAL   A 1 202 ? 28.041  -10.766 14.163 1.00 37.08  ? 202 VAL   A O   1 
ATOM   1532 C CB  . VAL   A 1 202 ? 27.572  -10.496 10.957 1.00 40.15  ? 202 VAL   A CB  1 
ATOM   1533 C CG1 . VAL   A 1 202 ? 26.386  -9.548  10.848 1.00 36.32  ? 202 VAL   A CG1 1 
ATOM   1534 C CG2 . VAL   A 1 202 ? 28.873  -9.743  11.234 1.00 36.75  ? 202 VAL   A CG2 1 
ATOM   1535 N N   . ASN   A 1 203 ? 25.821  -10.814 13.795 1.00 30.75  ? 203 ASN   A N   1 
ATOM   1536 C CA  . ASN   A 1 203 ? 25.513  -10.314 15.133 1.00 32.20  ? 203 ASN   A CA  1 
ATOM   1537 C C   . ASN   A 1 203 ? 25.768  -11.376 16.201 1.00 35.23  ? 203 ASN   A C   1 
ATOM   1538 O O   . ASN   A 1 203 ? 26.336  -11.074 17.257 1.00 35.33  ? 203 ASN   A O   1 
ATOM   1539 C CB  . ASN   A 1 203 ? 24.064  -9.828  15.190 1.00 27.37  ? 203 ASN   A CB  1 
ATOM   1540 C CG  . ASN   A 1 203 ? 23.875  -8.476  14.518 1.00 43.20  ? 203 ASN   A CG  1 
ATOM   1541 O OD1 . ASN   A 1 203 ? 24.784  -7.961  13.866 1.00 36.03  ? 203 ASN   A OD1 1 
ATOM   1542 N ND2 . ASN   A 1 203 ? 22.687  -7.897  14.672 1.00 36.93  ? 203 ASN   A ND2 1 
ATOM   1543 N N   . VAL   A 1 204 ? 25.350  -12.622 15.954 1.00 36.99  ? 204 VAL   A N   1 
ATOM   1544 C CA  . VAL   A 1 204 ? 25.623  -13.695 16.911 1.00 35.67  ? 204 VAL   A CA  1 
ATOM   1545 C C   . VAL   A 1 204 ? 27.123  -13.823 17.146 1.00 33.87  ? 204 VAL   A C   1 
ATOM   1546 O O   . VAL   A 1 204 ? 27.579  -13.978 18.286 1.00 36.84  ? 204 VAL   A O   1 
ATOM   1547 C CB  . VAL   A 1 204 ? 25.015  -15.026 16.424 1.00 33.38  ? 204 VAL   A CB  1 
ATOM   1548 C CG1 . VAL   A 1 204 ? 25.403  -16.169 17.354 1.00 38.91  ? 204 VAL   A CG1 1 
ATOM   1549 C CG2 . VAL   A 1 204 ? 23.510  -14.923 16.320 1.00 30.08  ? 204 VAL   A CG2 1 
ATOM   1550 N N   . LEU   A 1 205 ? 27.913  -13.740 16.073 1.00 36.71  ? 205 LEU   A N   1 
ATOM   1551 C CA  . LEU   A 1 205 ? 29.362  -13.844 16.201 1.00 40.50  ? 205 LEU   A CA  1 
ATOM   1552 C C   . LEU   A 1 205 ? 29.938  -12.698 17.022 1.00 38.66  ? 205 LEU   A C   1 
ATOM   1553 O O   . LEU   A 1 205 ? 30.865  -12.898 17.814 1.00 36.19  ? 205 LEU   A O   1 
ATOM   1554 C CB  . LEU   A 1 205 ? 30.003  -13.878 14.815 1.00 42.58  ? 205 LEU   A CB  1 
ATOM   1555 C CG  . LEU   A 1 205 ? 29.619  -15.112 14.007 1.00 37.02  ? 205 LEU   A CG  1 
ATOM   1556 C CD1 . LEU   A 1 205 ? 30.174  -15.016 12.601 1.00 40.31  ? 205 LEU   A CD1 1 
ATOM   1557 C CD2 . LEU   A 1 205 ? 30.144  -16.341 14.716 1.00 35.50  ? 205 LEU   A CD2 1 
ATOM   1558 N N   . ALA   A 1 206 ? 29.423  -11.482 16.829 1.00 35.70  ? 206 ALA   A N   1 
ATOM   1559 C CA  . ALA   A 1 206 ? 29.893  -10.363 17.640 1.00 46.00  ? 206 ALA   A CA  1 
ATOM   1560 C C   . ALA   A 1 206 ? 29.535  -10.571 19.106 1.00 31.46  ? 206 ALA   A C   1 
ATOM   1561 O O   . ALA   A 1 206 ? 30.323  -10.243 20.000 1.00 40.85  ? 206 ALA   A O   1 
ATOM   1562 C CB  . ALA   A 1 206 ? 29.311  -9.049  17.121 1.00 40.94  ? 206 ALA   A CB  1 
ATOM   1563 N N   . TRP   A 1 207 ? 28.355  -11.141 19.364 1.00 38.33  ? 207 TRP   A N   1 
ATOM   1564 C CA  . TRP   A 1 207 ? 27.922  -11.420 20.731 1.00 40.65  ? 207 TRP   A CA  1 
ATOM   1565 C C   . TRP   A 1 207 ? 28.802  -12.480 21.383 1.00 42.28  ? 207 TRP   A C   1 
ATOM   1566 O O   . TRP   A 1 207 ? 29.119  -12.386 22.576 1.00 43.85  ? 207 TRP   A O   1 
ATOM   1567 C CB  . TRP   A 1 207 ? 26.452  -11.848 20.719 1.00 40.71  ? 207 TRP   A CB  1 
ATOM   1568 C CG  . TRP   A 1 207 ? 25.878  -12.294 22.034 1.00 45.93  ? 207 TRP   A CG  1 
ATOM   1569 C CD1 . TRP   A 1 207 ? 25.548  -11.505 23.103 1.00 46.59  ? 207 TRP   A CD1 1 
ATOM   1570 C CD2 . TRP   A 1 207 ? 25.522  -13.633 22.399 1.00 44.25  ? 207 TRP   A CD2 1 
ATOM   1571 N NE1 . TRP   A 1 207 ? 25.028  -12.277 24.117 1.00 45.95  ? 207 TRP   A NE1 1 
ATOM   1572 C CE2 . TRP   A 1 207 ? 25.002  -13.585 23.710 1.00 49.29  ? 207 TRP   A CE2 1 
ATOM   1573 C CE3 . TRP   A 1 207 ? 25.602  -14.868 21.750 1.00 43.30  ? 207 TRP   A CE3 1 
ATOM   1574 C CZ2 . TRP   A 1 207 ? 24.563  -14.725 24.378 1.00 48.32  ? 207 TRP   A CZ2 1 
ATOM   1575 C CZ3 . TRP   A 1 207 ? 25.167  -15.999 22.420 1.00 46.84  ? 207 TRP   A CZ3 1 
ATOM   1576 C CH2 . TRP   A 1 207 ? 24.655  -15.919 23.717 1.00 46.68  ? 207 TRP   A CH2 1 
ATOM   1577 N N   . LEU   A 1 208 ? 29.219  -13.489 20.615 1.00 45.99  ? 208 LEU   A N   1 
ATOM   1578 C CA  . LEU   A 1 208 ? 30.172  -14.463 21.139 1.00 44.74  ? 208 LEU   A CA  1 
ATOM   1579 C C   . LEU   A 1 208 ? 31.500  -13.803 21.482 1.00 40.50  ? 208 LEU   A C   1 
ATOM   1580 O O   . LEU   A 1 208 ? 32.121  -14.134 22.498 1.00 41.74  ? 208 LEU   A O   1 
ATOM   1581 C CB  . LEU   A 1 208 ? 30.381  -15.590 20.132 1.00 40.64  ? 208 LEU   A CB  1 
ATOM   1582 C CG  . LEU   A 1 208 ? 29.118  -16.402 19.869 1.00 41.21  ? 208 LEU   A CG  1 
ATOM   1583 C CD1 . LEU   A 1 208 ? 29.351  -17.400 18.751 1.00 42.10  ? 208 LEU   A CD1 1 
ATOM   1584 C CD2 . LEU   A 1 208 ? 28.674  -17.101 21.144 1.00 39.16  ? 208 LEU   A CD2 1 
ATOM   1585 N N   . TYR   A 1 209 ? 31.956  -12.869 20.644 1.00 34.45  ? 209 TYR   A N   1 
ATOM   1586 C CA  . TYR   A 1 209 ? 33.156  -12.112 20.982 1.00 41.07  ? 209 TYR   A CA  1 
ATOM   1587 C C   . TYR   A 1 209 ? 32.950  -11.307 22.258 1.00 46.39  ? 209 TYR   A C   1 
ATOM   1588 O O   . TYR   A 1 209 ? 33.844  -11.243 23.109 1.00 50.43  ? 209 TYR   A O   1 
ATOM   1589 C CB  . TYR   A 1 209 ? 33.553  -11.199 19.825 1.00 46.23  ? 209 TYR   A CB  1 
ATOM   1590 C CG  . TYR   A 1 209 ? 34.354  -11.893 18.751 1.00 50.56  ? 209 TYR   A CG  1 
ATOM   1591 C CD1 . TYR   A 1 209 ? 35.665  -12.293 18.989 1.00 59.35  ? 209 TYR   A CD1 1 
ATOM   1592 C CD2 . TYR   A 1 209 ? 33.811  -12.139 17.500 1.00 44.91  ? 209 TYR   A CD2 1 
ATOM   1593 C CE1 . TYR   A 1 209 ? 36.408  -12.926 18.015 1.00 56.68  ? 209 TYR   A CE1 1 
ATOM   1594 C CE2 . TYR   A 1 209 ? 34.548  -12.772 16.517 1.00 54.76  ? 209 TYR   A CE2 1 
ATOM   1595 C CZ  . TYR   A 1 209 ? 35.847  -13.162 16.780 1.00 57.27  ? 209 TYR   A CZ  1 
ATOM   1596 O OH  . TYR   A 1 209 ? 36.586  -13.793 15.805 1.00 56.34  ? 209 TYR   A OH  1 
ATOM   1597 N N   . ALA   A 1 210 ? 31.776  -10.686 22.409 1.00 40.59  ? 210 ALA   A N   1 
ATOM   1598 C CA  . ALA   A 1 210 ? 31.454  -10.028 23.671 1.00 48.13  ? 210 ALA   A CA  1 
ATOM   1599 C C   . ALA   A 1 210 ? 31.518  -11.015 24.827 1.00 47.89  ? 210 ALA   A C   1 
ATOM   1600 O O   . ALA   A 1 210 ? 32.014  -10.685 25.910 1.00 52.43  ? 210 ALA   A O   1 
ATOM   1601 C CB  . ALA   A 1 210 ? 30.072  -9.378  23.594 1.00 38.62  ? 210 ALA   A CB  1 
ATOM   1602 N N   . ALA   A 1 211 ? 31.037  -12.242 24.605 1.00 42.59  ? 211 ALA   A N   1 
ATOM   1603 C CA  . ALA   A 1 211 ? 31.089  -13.263 25.643 1.00 43.55  ? 211 ALA   A CA  1 
ATOM   1604 C C   . ALA   A 1 211 ? 32.525  -13.615 26.004 1.00 50.73  ? 211 ALA   A C   1 
ATOM   1605 O O   . ALA   A 1 211 ? 32.852  -13.784 27.184 1.00 53.64  ? 211 ALA   A O   1 
ATOM   1606 C CB  . ALA   A 1 211 ? 30.332  -14.508 25.189 1.00 45.28  ? 211 ALA   A CB  1 
ATOM   1607 N N   . VAL   A 1 212 ? 33.397  -13.736 25.002 1.00 47.85  ? 212 VAL   A N   1 
ATOM   1608 C CA  . VAL   A 1 212 ? 34.800  -14.033 25.276 1.00 54.08  ? 212 VAL   A CA  1 
ATOM   1609 C C   . VAL   A 1 212 ? 35.446  -12.889 26.046 1.00 51.25  ? 212 VAL   A C   1 
ATOM   1610 O O   . VAL   A 1 212 ? 36.181  -13.111 27.016 1.00 51.79  ? 212 VAL   A O   1 
ATOM   1611 C CB  . VAL   A 1 212 ? 35.548  -14.327 23.963 1.00 48.02  ? 212 VAL   A CB  1 
ATOM   1612 C CG1 . VAL   A 1 212 ? 37.039  -14.465 24.219 1.00 55.27  ? 212 VAL   A CG1 1 
ATOM   1613 C CG2 . VAL   A 1 212 ? 34.994  -15.583 23.306 1.00 48.02  ? 212 VAL   A CG2 1 
ATOM   1614 N N   . ILE   A 1 213 ? 35.177  -11.648 25.631 1.00 58.05  ? 213 ILE   A N   1 
ATOM   1615 C CA  . ILE   A 1 213 ? 35.744  -10.480 26.300 1.00 53.65  ? 213 ILE   A CA  1 
ATOM   1616 C C   . ILE   A 1 213 ? 35.339  -10.440 27.768 1.00 54.23  ? 213 ILE   A C   1 
ATOM   1617 O O   . ILE   A 1 213 ? 36.122  -10.012 28.624 1.00 58.53  ? 213 ILE   A O   1 
ATOM   1618 C CB  . ILE   A 1 213 ? 35.321  -9.198  25.554 1.00 57.61  ? 213 ILE   A CB  1 
ATOM   1619 C CG1 . ILE   A 1 213 ? 35.943  -9.163  24.155 1.00 57.33  ? 213 ILE   A CG1 1 
ATOM   1620 C CG2 . ILE   A 1 213 ? 35.724  -7.953  26.331 1.00 64.35  ? 213 ILE   A CG2 1 
ATOM   1621 C CD1 . ILE   A 1 213 ? 35.415  -8.048  23.284 1.00 57.22  ? 213 ILE   A CD1 1 
ATOM   1622 N N   . ASN   A 1 214 ? 34.134  -10.904 28.092 1.00 56.31  ? 214 ASN   A N   1 
ATOM   1623 C CA  . ASN   A 1 214 ? 33.621  -10.822 29.454 1.00 62.08  ? 214 ASN   A CA  1 
ATOM   1624 C C   . ASN   A 1 214 ? 33.841  -12.089 30.270 1.00 61.38  ? 214 ASN   A C   1 
ATOM   1625 O O   . ASN   A 1 214 ? 33.198  -12.254 31.313 1.00 59.14  ? 214 ASN   A O   1 
ATOM   1626 C CB  . ASN   A 1 214 ? 32.129  -10.485 29.444 1.00 55.47  ? 214 ASN   A CB  1 
ATOM   1627 C CG  . ASN   A 1 214 ? 31.868  -9.018  29.201 1.00 56.49  ? 214 ASN   A CG  1 
ATOM   1628 O OD1 . ASN   A 1 214 ? 31.954  -8.200  30.118 1.00 60.41  ? 214 ASN   A OD1 1 
ATOM   1629 N ND2 . ASN   A 1 214 ? 31.546  -8.673  27.962 1.00 59.79  ? 214 ASN   A ND2 1 
ATOM   1630 N N   . GLY   A 1 215 ? 34.721  -12.988 29.831 1.00 61.94  ? 215 GLY   A N   1 
ATOM   1631 C CA  . GLY   A 1 215 ? 35.086  -14.149 30.605 1.00 65.14  ? 215 GLY   A CA  1 
ATOM   1632 C C   . GLY   A 1 215 ? 34.395  -15.438 30.201 1.00 67.95  ? 215 GLY   A C   1 
ATOM   1633 O O   . GLY   A 1 215 ? 34.938  -16.517 30.461 1.00 76.35  ? 215 GLY   A O   1 
ATOM   1634 N N   . ASP   A 1 216 ? 33.214  -15.362 29.588 1.00 62.40  ? 216 ASP   A N   1 
ATOM   1635 C CA  . ASP   A 1 216 ? 32.522  -16.569 29.138 1.00 57.94  ? 216 ASP   A CA  1 
ATOM   1636 C C   . ASP   A 1 216 ? 33.278  -17.168 27.960 1.00 63.54  ? 216 ASP   A C   1 
ATOM   1637 O O   . ASP   A 1 216 ? 33.315  -16.585 26.870 1.00 56.96  ? 216 ASP   A O   1 
ATOM   1638 C CB  . ASP   A 1 216 ? 31.080  -16.259 28.754 1.00 60.03  ? 216 ASP   A CB  1 
ATOM   1639 C CG  . ASP   A 1 216 ? 30.182  -16.066 29.957 1.00 67.01  ? 216 ASP   A CG  1 
ATOM   1640 O OD1 . ASP   A 1 216 ? 30.678  -16.170 31.098 1.00 72.08  ? 216 ASP   A OD1 1 
ATOM   1641 O OD2 . ASP   A 1 216 ? 28.974  -15.808 29.754 1.00 62.14  ? 216 ASP   A OD2 1 
ATOM   1642 N N   . ARG   A 1 217 ? 33.869  -18.345 28.173 1.00 66.45  ? 217 ARG   A N   1 
ATOM   1643 C CA  . ARG   A 1 217 ? 34.797  -18.909 27.201 1.00 67.19  ? 217 ARG   A CA  1 
ATOM   1644 C C   . ARG   A 1 217 ? 34.612  -20.411 27.005 1.00 61.73  ? 217 ARG   A C   1 
ATOM   1645 O O   . ARG   A 1 217 ? 35.426  -21.034 26.312 1.00 69.24  ? 217 ARG   A O   1 
ATOM   1646 C CB  . ARG   A 1 217 ? 36.242  -18.598 27.643 1.00 68.13  ? 217 ARG   A CB  1 
ATOM   1647 C CG  . ARG   A 1 217 ? 37.309  -18.689 26.569 1.00 74.01  ? 217 ARG   A CG  1 
ATOM   1648 C CD  . ARG   A 1 217 ? 38.644  -18.135 27.047 1.00 70.27  ? 217 ARG   A CD  1 
ATOM   1649 N NE  . ARG   A 1 217 ? 38.667  -16.676 27.063 1.00 76.04  ? 217 ARG   A NE  1 
ATOM   1650 C CZ  . ARG   A 1 217 ? 38.472  -15.925 28.141 1.00 79.08  ? 217 ARG   A CZ  1 
ATOM   1651 N NH1 . ARG   A 1 217 ? 38.249  -16.463 29.330 1.00 81.77  ? 217 ARG   A NH1 1 
ATOM   1652 N NH2 . ARG   A 1 217 ? 38.505  -14.600 28.023 1.00 67.44  ? 217 ARG   A NH2 1 
ATOM   1653 N N   . TRP   A 1 218 ? 33.563  -21.009 27.575 1.00 61.30  ? 218 TRP   A N   1 
ATOM   1654 C CA  . TRP   A 1 218 ? 33.421  -22.462 27.522 1.00 66.52  ? 218 TRP   A CA  1 
ATOM   1655 C C   . TRP   A 1 218 ? 33.132  -22.964 26.112 1.00 67.99  ? 218 TRP   A C   1 
ATOM   1656 O O   . TRP   A 1 218 ? 33.529  -24.082 25.757 1.00 69.99  ? 218 TRP   A O   1 
ATOM   1657 C CB  . TRP   A 1 218 ? 32.315  -22.923 28.475 1.00 54.99  ? 218 TRP   A CB  1 
ATOM   1658 C CG  . TRP   A 1 218 ? 30.938  -22.426 28.111 1.00 61.33  ? 218 TRP   A CG  1 
ATOM   1659 C CD1 . TRP   A 1 218 ? 30.306  -21.322 28.609 1.00 66.56  ? 218 TRP   A CD1 1 
ATOM   1660 C CD2 . TRP   A 1 218 ? 30.021  -23.026 27.185 1.00 65.58  ? 218 TRP   A CD2 1 
ATOM   1661 N NE1 . TRP   A 1 218 ? 29.058  -21.196 28.049 1.00 60.93  ? 218 TRP   A NE1 1 
ATOM   1662 C CE2 . TRP   A 1 218 ? 28.859  -22.227 27.170 1.00 63.12  ? 218 TRP   A CE2 1 
ATOM   1663 C CE3 . TRP   A 1 218 ? 30.071  -24.158 26.365 1.00 67.79  ? 218 TRP   A CE3 1 
ATOM   1664 C CZ2 . TRP   A 1 218 ? 27.760  -22.525 26.369 1.00 62.91  ? 218 TRP   A CZ2 1 
ATOM   1665 C CZ3 . TRP   A 1 218 ? 28.979  -24.449 25.568 1.00 66.06  ? 218 TRP   A CZ3 1 
ATOM   1666 C CH2 . TRP   A 1 218 ? 27.838  -23.636 25.578 1.00 62.53  ? 218 TRP   A CH2 1 
ATOM   1667 N N   . PHE   A 1 219 ? 32.443  -22.167 25.299 1.00 68.14  ? 219 PHE   A N   1 
ATOM   1668 C CA  . PHE   A 1 219 ? 32.070  -22.594 23.957 1.00 65.93  ? 219 PHE   A CA  1 
ATOM   1669 C C   . PHE   A 1 219 ? 33.235  -22.560 22.975 1.00 63.10  ? 219 PHE   A C   1 
ATOM   1670 O O   . PHE   A 1 219 ? 33.091  -23.055 21.852 1.00 56.70  ? 219 PHE   A O   1 
ATOM   1671 C CB  . PHE   A 1 219 ? 30.927  -21.720 23.436 1.00 56.29  ? 219 PHE   A CB  1 
ATOM   1672 C CG  . PHE   A 1 219 ? 31.214  -20.248 23.510 1.00 62.97  ? 219 PHE   A CG  1 
ATOM   1673 C CD1 . PHE   A 1 219 ? 31.859  -19.604 22.467 1.00 57.70  ? 219 PHE   A CD1 1 
ATOM   1674 C CD2 . PHE   A 1 219 ? 30.847  -19.510 24.625 1.00 54.19  ? 219 PHE   A CD2 1 
ATOM   1675 C CE1 . PHE   A 1 219 ? 32.132  -18.255 22.531 1.00 59.69  ? 219 PHE   A CE1 1 
ATOM   1676 C CE2 . PHE   A 1 219 ? 31.117  -18.161 24.694 1.00 52.61  ? 219 PHE   A CE2 1 
ATOM   1677 C CZ  . PHE   A 1 219 ? 31.761  -17.531 23.647 1.00 57.36  ? 219 PHE   A CZ  1 
ATOM   1678 N N   . LEU   A 1 220 ? 34.375  -21.991 23.358 1.00 62.93  ? 220 LEU   A N   1 
ATOM   1679 C CA  . LEU   A 1 220 ? 35.507  -21.925 22.445 1.00 69.57  ? 220 LEU   A CA  1 
ATOM   1680 C C   . LEU   A 1 220 ? 36.156  -23.296 22.303 1.00 72.40  ? 220 LEU   A C   1 
ATOM   1681 O O   . LEU   A 1 220 ? 36.249  -24.063 23.266 1.00 72.96  ? 220 LEU   A O   1 
ATOM   1682 C CB  . LEU   A 1 220 ? 36.534  -20.902 22.931 1.00 66.09  ? 220 LEU   A CB  1 
ATOM   1683 C CG  . LEU   A 1 220 ? 36.202  -19.425 22.714 1.00 62.30  ? 220 LEU   A CG  1 
ATOM   1684 C CD1 . LEU   A 1 220 ? 37.384  -18.570 23.115 1.00 61.42  ? 220 LEU   A CD1 1 
ATOM   1685 C CD2 . LEU   A 1 220 ? 35.818  -19.155 21.264 1.00 54.26  ? 220 LEU   A CD2 1 
ATOM   1686 N N   . ASN   A 1 221 ? 36.595  -23.608 21.085 1.00 71.14  ? 221 ASN   A N   1 
ATOM   1687 C CA  . ASN   A 1 221 ? 37.307  -24.855 20.845 1.00 73.73  ? 221 ASN   A CA  1 
ATOM   1688 C C   . ASN   A 1 221 ? 38.567  -24.589 20.035 1.00 72.25  ? 221 ASN   A C   1 
ATOM   1689 O O   . ASN   A 1 221 ? 38.887  -23.434 19.733 1.00 73.83  ? 221 ASN   A O   1 
ATOM   1690 C CB  . ASN   A 1 221 ? 36.406  -25.873 20.137 1.00 63.27  ? 221 ASN   A CB  1 
ATOM   1691 C CG  . ASN   A 1 221 ? 35.849  -25.359 18.813 1.00 69.16  ? 221 ASN   A CG  1 
ATOM   1692 O OD1 . ASN   A 1 221 ? 36.544  -24.707 18.031 1.00 66.12  ? 221 ASN   A OD1 1 
ATOM   1693 N ND2 . ASN   A 1 221 ? 34.580  -25.658 18.557 1.00 66.65  ? 221 ASN   A ND2 1 
ATOM   1694 N N   . ARG   A 1 222 ? 39.283  -25.650 19.673 1.00 75.25  ? 222 ARG   A N   1 
ATOM   1695 C CA  . ARG   A 1 222 ? 40.456  -25.538 18.821 1.00 76.83  ? 222 ARG   A CA  1 
ATOM   1696 C C   . ARG   A 1 222 ? 40.154  -25.884 17.368 1.00 78.40  ? 222 ARG   A C   1 
ATOM   1697 O O   . ARG   A 1 222 ? 41.081  -25.966 16.558 1.00 81.43  ? 222 ARG   A O   1 
ATOM   1698 C CB  . ARG   A 1 222 ? 41.584  -26.426 19.356 1.00 73.30  ? 222 ARG   A CB  1 
ATOM   1699 N N   . PHE   A 1 223 ? 38.882  -26.071 17.017 1.00 78.57  ? 223 PHE   A N   1 
ATOM   1700 C CA  . PHE   A 1 223 ? 38.528  -26.464 15.662 1.00 63.88  ? 223 PHE   A CA  1 
ATOM   1701 C C   . PHE   A 1 223 ? 38.545  -25.254 14.735 1.00 71.89  ? 223 PHE   A C   1 
ATOM   1702 O O   . PHE   A 1 223 ? 38.728  -24.110 15.156 1.00 75.04  ? 223 PHE   A O   1 
ATOM   1703 C CB  . PHE   A 1 223 ? 37.143  -27.110 15.600 1.00 59.97  ? 223 PHE   A CB  1 
ATOM   1704 C CG  . PHE   A 1 223 ? 37.025  -28.403 16.353 1.00 67.18  ? 223 PHE   A CG  1 
ATOM   1705 C CD1 . PHE   A 1 223 ? 37.997  -28.799 17.253 1.00 73.43  ? 223 PHE   A CD1 1 
ATOM   1706 C CD2 . PHE   A 1 223 ? 35.931  -29.227 16.155 1.00 73.07  ? 223 PHE   A CD2 1 
ATOM   1707 C CE1 . PHE   A 1 223 ? 37.879  -29.975 17.949 1.00 78.08  ? 223 PHE   A CE1 1 
ATOM   1708 C CE2 . PHE   A 1 223 ? 35.809  -30.417 16.845 1.00 80.15  ? 223 PHE   A CE2 1 
ATOM   1709 C CZ  . PHE   A 1 223 ? 36.787  -30.791 17.744 1.00 80.69  ? 223 PHE   A CZ  1 
ATOM   1710 N N   . THR   A 1 224 ? 38.334  -25.523 13.451 1.00 74.82  ? 224 THR   A N   1 
ATOM   1711 C CA  . THR   A 1 224 ? 38.172  -24.471 12.461 1.00 70.89  ? 224 THR   A CA  1 
ATOM   1712 C C   . THR   A 1 224 ? 37.291  -25.011 11.341 1.00 70.54  ? 224 THR   A C   1 
ATOM   1713 O O   . THR   A 1 224 ? 36.949  -26.198 11.314 1.00 70.48  ? 224 THR   A O   1 
ATOM   1714 C CB  . THR   A 1 224 ? 39.528  -23.982 11.941 1.00 77.91  ? 224 THR   A CB  1 
ATOM   1715 O OG1 . THR   A 1 224 ? 39.344  -22.799 11.153 1.00 75.30  ? 224 THR   A OG1 1 
ATOM   1716 C CG2 . THR   A 1 224 ? 40.194  -25.058 11.094 1.00 76.15  ? 224 THR   A CG2 1 
ATOM   1717 N N   . THR   A 1 225 ? 36.913  -24.127 10.421 1.00 71.35  ? 225 THR   A N   1 
ATOM   1718 C CA  . THR   A 1 225 ? 36.059  -24.483 9.293  1.00 73.32  ? 225 THR   A CA  1 
ATOM   1719 C C   . THR   A 1 225 ? 36.087  -23.336 8.288  1.00 74.05  ? 225 THR   A C   1 
ATOM   1720 O O   . THR   A 1 225 ? 36.197  -22.170 8.675  1.00 78.77  ? 225 THR   A O   1 
ATOM   1721 C CB  . THR   A 1 225 ? 34.623  -24.783 9.759  1.00 73.46  ? 225 THR   A CB  1 
ATOM   1722 O OG1 . THR   A 1 225 ? 34.626  -25.956 10.585 1.00 75.81  ? 225 THR   A OG1 1 
ATOM   1723 C CG2 . THR   A 1 225 ? 33.696  -25.022 8.585  1.00 69.23  ? 225 THR   A CG2 1 
ATOM   1724 N N   . THR   A 1 226 ? 36.022  -23.674 6.998  1.00 79.00  ? 226 THR   A N   1 
ATOM   1725 C CA  . THR   A 1 226 ? 35.971  -22.644 5.968  1.00 76.67  ? 226 THR   A CA  1 
ATOM   1726 C C   . THR   A 1 226 ? 34.654  -21.877 6.052  1.00 66.83  ? 226 THR   A C   1 
ATOM   1727 O O   . THR   A 1 226 ? 33.682  -22.315 6.674  1.00 63.27  ? 226 THR   A O   1 
ATOM   1728 C CB  . THR   A 1 226 ? 36.118  -23.245 4.566  1.00 70.90  ? 226 THR   A CB  1 
ATOM   1729 O OG1 . THR   A 1 226 ? 34.934  -23.981 4.232  1.00 70.38  ? 226 THR   A OG1 1 
ATOM   1730 C CG2 . THR   A 1 226 ? 37.332  -24.163 4.485  1.00 75.03  ? 226 THR   A CG2 1 
ATOM   1731 N N   . LEU   A 1 227 ? 34.631  -20.708 5.407  1.00 68.40  ? 227 LEU   A N   1 
ATOM   1732 C CA  . LEU   A 1 227 ? 33.397  -19.933 5.353  1.00 66.63  ? 227 LEU   A CA  1 
ATOM   1733 C C   . LEU   A 1 227 ? 32.303  -20.692 4.614  1.00 70.05  ? 227 LEU   A C   1 
ATOM   1734 O O   . LEU   A 1 227 ? 31.120  -20.577 4.959  1.00 69.88  ? 227 LEU   A O   1 
ATOM   1735 C CB  . LEU   A 1 227 ? 33.656  -18.577 4.691  1.00 62.05  ? 227 LEU   A CB  1 
ATOM   1736 C CG  . LEU   A 1 227 ? 32.472  -17.613 4.559  1.00 67.69  ? 227 LEU   A CG  1 
ATOM   1737 C CD1 . LEU   A 1 227 ? 32.871  -16.219 5.016  1.00 66.50  ? 227 LEU   A CD1 1 
ATOM   1738 C CD2 . LEU   A 1 227 ? 31.964  -17.579 3.124  1.00 68.50  ? 227 LEU   A CD2 1 
ATOM   1739 N N   . ASN   A 1 228 ? 32.685  -21.493 3.616  1.00 69.54  ? 228 ASN   A N   1 
ATOM   1740 C CA  . ASN   A 1 228 ? 31.700  -22.202 2.808  1.00 65.61  ? 228 ASN   A CA  1 
ATOM   1741 C C   . ASN   A 1 228 ? 31.032  -23.322 3.595  1.00 60.27  ? 228 ASN   A C   1 
ATOM   1742 O O   . ASN   A 1 228 ? 29.812  -23.508 3.508  1.00 65.87  ? 228 ASN   A O   1 
ATOM   1743 C CB  . ASN   A 1 228 ? 32.363  -22.755 1.547  1.00 66.04  ? 228 ASN   A CB  1 
ATOM   1744 C CG  . ASN   A 1 228 ? 31.367  -23.024 0.443  1.00 59.36  ? 228 ASN   A CG  1 
ATOM   1745 O OD1 . ASN   A 1 228 ? 31.141  -22.173 -0.414 1.00 61.48  ? 228 ASN   A OD1 1 
ATOM   1746 N ND2 . ASN   A 1 228 ? 30.756  -24.207 0.461  1.00 69.79  ? 228 ASN   A ND2 1 
ATOM   1747 N N   . ASP   A 1 229 ? 31.811  -24.083 4.364  1.00 64.69  ? 229 ASP   A N   1 
ATOM   1748 C CA  . ASP   A 1 229 ? 31.240  -25.197 5.110  1.00 64.09  ? 229 ASP   A CA  1 
ATOM   1749 C C   . ASP   A 1 229 ? 30.474  -24.735 6.342  1.00 69.98  ? 229 ASP   A C   1 
ATOM   1750 O O   . ASP   A 1 229 ? 29.600  -25.465 6.825  1.00 68.11  ? 229 ASP   A O   1 
ATOM   1751 C CB  . ASP   A 1 229 ? 32.337  -26.182 5.511  1.00 70.36  ? 229 ASP   A CB  1 
ATOM   1752 N N   . PHE   A 1 230 ? 30.775  -23.544 6.862  1.00 70.30  ? 230 PHE   A N   1 
ATOM   1753 C CA  . PHE   A 1 230 ? 29.964  -22.993 7.943  1.00 66.64  ? 230 PHE   A CA  1 
ATOM   1754 C C   . PHE   A 1 230 ? 28.592  -22.568 7.435  1.00 61.24  ? 230 PHE   A C   1 
ATOM   1755 O O   . PHE   A 1 230 ? 27.580  -22.775 8.115  1.00 60.06  ? 230 PHE   A O   1 
ATOM   1756 C CB  . PHE   A 1 230 ? 30.686  -21.814 8.600  1.00 66.57  ? 230 PHE   A CB  1 
ATOM   1757 C CG  . PHE   A 1 230 ? 29.821  -21.026 9.544  1.00 67.08  ? 230 PHE   A CG  1 
ATOM   1758 C CD1 . PHE   A 1 230 ? 29.565  -21.495 10.823 1.00 65.07  ? 230 PHE   A CD1 1 
ATOM   1759 C CD2 . PHE   A 1 230 ? 29.258  -19.822 9.150  1.00 63.47  ? 230 PHE   A CD2 1 
ATOM   1760 C CE1 . PHE   A 1 230 ? 28.764  -20.777 11.689 1.00 61.48  ? 230 PHE   A CE1 1 
ATOM   1761 C CE2 . PHE   A 1 230 ? 28.457  -19.101 10.012 1.00 56.67  ? 230 PHE   A CE2 1 
ATOM   1762 C CZ  . PHE   A 1 230 ? 28.211  -19.579 11.282 1.00 56.73  ? 230 PHE   A CZ  1 
ATOM   1763 N N   . ASN   A 1 231 ? 28.538  -21.974 6.239  1.00 63.64  ? 231 ASN   A N   1 
ATOM   1764 C CA  . ASN   A 1 231 ? 27.262  -21.521 5.695  1.00 61.60  ? 231 ASN   A CA  1 
ATOM   1765 C C   . ASN   A 1 231 ? 26.333  -22.689 5.381  1.00 66.01  ? 231 ASN   A C   1 
ATOM   1766 O O   . ASN   A 1 231 ? 25.107  -22.526 5.410  1.00 64.82  ? 231 ASN   A O   1 
ATOM   1767 C CB  . ASN   A 1 231 ? 27.498  -20.665 4.451  1.00 57.61  ? 231 ASN   A CB  1 
ATOM   1768 C CG  . ASN   A 1 231 ? 28.002  -19.270 4.791  1.00 63.36  ? 231 ASN   A CG  1 
ATOM   1769 O OD1 . ASN   A 1 231 ? 27.533  -18.642 5.741  1.00 66.60  ? 231 ASN   A OD1 1 
ATOM   1770 N ND2 . ASN   A 1 231 ? 28.962  -18.782 4.016  1.00 53.75  ? 231 ASN   A ND2 1 
ATOM   1771 N N   . LEU   A 1 232 ? 26.891  -23.867 5.083  1.00 71.84  ? 232 LEU   A N   1 
ATOM   1772 C CA  . LEU   A 1 232 ? 26.059  -25.054 4.905  1.00 66.05  ? 232 LEU   A CA  1 
ATOM   1773 C C   . LEU   A 1 232 ? 25.372  -25.442 6.207  1.00 62.25  ? 232 LEU   A C   1 
ATOM   1774 O O   . LEU   A 1 232 ? 24.196  -25.825 6.208  1.00 66.48  ? 232 LEU   A O   1 
ATOM   1775 C CB  . LEU   A 1 232 ? 26.900  -26.218 4.381  1.00 62.81  ? 232 LEU   A CB  1 
ATOM   1776 N N   . VAL   A 1 233 ? 26.092  -25.352 7.326  1.00 63.96  ? 233 VAL   A N   1 
ATOM   1777 C CA  . VAL   A 1 233 ? 25.480  -25.610 8.623  1.00 63.05  ? 233 VAL   A CA  1 
ATOM   1778 C C   . VAL   A 1 233 ? 24.499  -24.498 8.977  1.00 65.61  ? 233 VAL   A C   1 
ATOM   1779 O O   . VAL   A 1 233 ? 23.462  -24.748 9.608  1.00 64.93  ? 233 VAL   A O   1 
ATOM   1780 C CB  . VAL   A 1 233 ? 26.581  -25.784 9.688  1.00 67.29  ? 233 VAL   A CB  1 
ATOM   1781 C CG1 . VAL   A 1 233 ? 25.994  -25.807 11.088 1.00 66.41  ? 233 VAL   A CG1 1 
ATOM   1782 C CG2 . VAL   A 1 233 ? 27.371  -27.061 9.422  1.00 65.42  ? 233 VAL   A CG2 1 
ATOM   1783 N N   . ALA   A 1 234 ? 24.781  -23.266 8.538  1.00 65.16  ? 234 ALA   A N   1 
ATOM   1784 C CA  . ALA   A 1 234 ? 23.942  -22.124 8.891  1.00 61.88  ? 234 ALA   A CA  1 
ATOM   1785 C C   . ALA   A 1 234 ? 22.594  -22.156 8.179  1.00 59.09  ? 234 ALA   A C   1 
ATOM   1786 O O   . ALA   A 1 234 ? 21.601  -21.657 8.719  1.00 61.80  ? 234 ALA   A O   1 
ATOM   1787 C CB  . ALA   A 1 234 ? 24.673  -20.819 8.572  1.00 59.43  ? 234 ALA   A CB  1 
ATOM   1788 N N   . MET   A 1 235 ? 22.534  -22.727 6.975  1.00 61.46  ? 235 MET   A N   1 
ATOM   1789 C CA  . MET   A 1 235 ? 21.268  -22.773 6.247  1.00 63.66  ? 235 MET   A CA  1 
ATOM   1790 C C   . MET   A 1 235 ? 20.275  -23.730 6.899  1.00 64.70  ? 235 MET   A C   1 
ATOM   1791 O O   . MET   A 1 235 ? 19.066  -23.473 6.893  1.00 65.16  ? 235 MET   A O   1 
ATOM   1792 C CB  . MET   A 1 235 ? 21.512  -23.165 4.790  1.00 61.50  ? 235 MET   A CB  1 
ATOM   1793 N N   . LYS   A 1 236 ? 20.754  -24.844 7.456  1.00 62.81  ? 236 LYS   A N   1 
ATOM   1794 C CA  . LYS   A 1 236 ? 19.820  -25.807 8.030  1.00 64.49  ? 236 LYS   A CA  1 
ATOM   1795 C C   . LYS   A 1 236 ? 19.191  -25.300 9.319  1.00 61.37  ? 236 LYS   A C   1 
ATOM   1796 O O   . LYS   A 1 236 ? 18.084  -25.727 9.666  1.00 74.89  ? 236 LYS   A O   1 
ATOM   1797 C CB  . LYS   A 1 236 ? 20.513  -27.148 8.277  1.00 63.78  ? 236 LYS   A CB  1 
ATOM   1798 N N   . TYR   A 1 237 ? 19.857  -24.383 10.018 1.00 67.94  ? 237 TYR   A N   1 
ATOM   1799 C CA  . TYR   A 1 237 ? 19.368  -23.821 11.268 1.00 64.84  ? 237 TYR   A CA  1 
ATOM   1800 C C   . TYR   A 1 237 ? 18.811  -22.409 11.097 1.00 60.91  ? 237 TYR   A C   1 
ATOM   1801 O O   . TYR   A 1 237 ? 18.635  -21.694 12.089 1.00 58.42  ? 237 TYR   A O   1 
ATOM   1802 C CB  . TYR   A 1 237 ? 20.483  -23.842 12.316 1.00 61.95  ? 237 TYR   A CB  1 
ATOM   1803 C CG  . TYR   A 1 237 ? 20.777  -25.225 12.867 1.00 61.80  ? 237 TYR   A CG  1 
ATOM   1804 C CD1 . TYR   A 1 237 ? 21.723  -26.056 12.271 1.00 63.83  ? 237 TYR   A CD1 1 
ATOM   1805 C CD2 . TYR   A 1 237 ? 20.105  -25.698 13.985 1.00 72.00  ? 237 TYR   A CD2 1 
ATOM   1806 C CE1 . TYR   A 1 237 ? 21.987  -27.322 12.782 1.00 67.61  ? 237 TYR   A CE1 1 
ATOM   1807 C CE2 . TYR   A 1 237 ? 20.360  -26.955 14.499 1.00 71.86  ? 237 TYR   A CE2 1 
ATOM   1808 C CZ  . TYR   A 1 237 ? 21.301  -27.764 13.897 1.00 71.26  ? 237 TYR   A CZ  1 
ATOM   1809 O OH  . TYR   A 1 237 ? 21.547  -29.016 14.421 1.00 75.83  ? 237 TYR   A OH  1 
ATOM   1810 N N   . ASN   A 1 238 ? 18.541  -21.994 9.854  1.00 60.82  ? 238 ASN   A N   1 
ATOM   1811 C CA  . ASN   A 1 238 ? 17.869  -20.723 9.558  1.00 58.02  ? 238 ASN   A CA  1 
ATOM   1812 C C   . ASN   A 1 238 ? 18.721  -19.521 9.984  1.00 60.35  ? 238 ASN   A C   1 
ATOM   1813 O O   . ASN   A 1 238 ? 18.258  -18.622 10.689 1.00 55.36  ? 238 ASN   A O   1 
ATOM   1814 C CB  . ASN   A 1 238 ? 16.481  -20.675 10.204 1.00 65.38  ? 238 ASN   A CB  1 
ATOM   1815 C CG  . ASN   A 1 238 ? 15.585  -19.619 9.592  1.00 72.40  ? 238 ASN   A CG  1 
ATOM   1816 O OD1 . ASN   A 1 238 ? 15.545  -19.452 8.372  1.00 74.94  ? 238 ASN   A OD1 1 
ATOM   1817 N ND2 . ASN   A 1 238 ? 14.858  -18.897 10.441 1.00 75.11  ? 238 ASN   A ND2 1 
ATOM   1818 N N   . TYR   A 1 239 ? 19.972  -19.508 9.535  1.00 52.23  ? 239 TYR   A N   1 
ATOM   1819 C CA  . TYR   A 1 239 ? 20.902  -18.418 9.788  1.00 48.72  ? 239 TYR   A CA  1 
ATOM   1820 C C   . TYR   A 1 239 ? 21.247  -17.716 8.480  1.00 56.81  ? 239 TYR   A C   1 
ATOM   1821 O O   . TYR   A 1 239 ? 21.250  -18.331 7.409  1.00 56.75  ? 239 TYR   A O   1 
ATOM   1822 C CB  . TYR   A 1 239 ? 22.181  -18.931 10.462 1.00 50.01  ? 239 TYR   A CB  1 
ATOM   1823 C CG  . TYR   A 1 239 ? 22.114  -18.954 11.975 1.00 50.40  ? 239 TYR   A CG  1 
ATOM   1824 C CD1 . TYR   A 1 239 ? 21.099  -19.635 12.637 1.00 50.79  ? 239 TYR   A CD1 1 
ATOM   1825 C CD2 . TYR   A 1 239 ? 23.070  -18.298 12.741 1.00 48.65  ? 239 TYR   A CD2 1 
ATOM   1826 C CE1 . TYR   A 1 239 ? 21.032  -19.656 14.018 1.00 46.92  ? 239 TYR   A CE1 1 
ATOM   1827 C CE2 . TYR   A 1 239 ? 23.012  -18.314 14.121 1.00 52.38  ? 239 TYR   A CE2 1 
ATOM   1828 C CZ  . TYR   A 1 239 ? 21.992  -18.995 14.755 1.00 49.59  ? 239 TYR   A CZ  1 
ATOM   1829 O OH  . TYR   A 1 239 ? 21.933  -19.010 16.129 1.00 47.57  ? 239 TYR   A OH  1 
ATOM   1830 N N   . GLU   A 1 240 ? 21.529  -16.417 8.575  1.00 54.88  ? 240 GLU   A N   1 
ATOM   1831 C CA  . GLU   A 1 240 ? 21.936  -15.654 7.404  1.00 52.34  ? 240 GLU   A CA  1 
ATOM   1832 C C   . GLU   A 1 240 ? 23.288  -16.149 6.896  1.00 48.05  ? 240 GLU   A C   1 
ATOM   1833 O O   . GLU   A 1 240 ? 24.138  -16.569 7.685  1.00 46.43  ? 240 GLU   A O   1 
ATOM   1834 C CB  . GLU   A 1 240 ? 22.039  -14.164 7.728  1.00 50.91  ? 240 GLU   A CB  1 
ATOM   1835 C CG  . GLU   A 1 240 ? 20.722  -13.475 8.035  1.00 57.50  ? 240 GLU   A CG  1 
ATOM   1836 C CD  . GLU   A 1 240 ? 19.825  -13.353 6.820  1.00 67.59  ? 240 GLU   A CD  1 
ATOM   1837 O OE1 . GLU   A 1 240 ? 20.320  -13.526 5.686  1.00 67.22  ? 240 GLU   A OE1 1 
ATOM   1838 O OE2 . GLU   A 1 240 ? 18.620  -13.083 7.002  1.00 67.62  ? 240 GLU   A OE2 1 
ATOM   1839 N N   . PRO   A 1 241 ? 23.514  -16.107 5.583  1.00 54.81  ? 241 PRO   A N   1 
ATOM   1840 C CA  . PRO   A 1 241 ? 24.841  -16.450 5.062  1.00 49.46  ? 241 PRO   A CA  1 
ATOM   1841 C C   . PRO   A 1 241 ? 25.889  -15.472 5.568  1.00 54.71  ? 241 PRO   A C   1 
ATOM   1842 O O   . PRO   A 1 241 ? 25.625  -14.281 5.751  1.00 57.73  ? 241 PRO   A O   1 
ATOM   1843 C CB  . PRO   A 1 241 ? 24.670  -16.348 3.541  1.00 61.48  ? 241 PRO   A CB  1 
ATOM   1844 C CG  . PRO   A 1 241 ? 23.199  -16.435 3.305  1.00 62.21  ? 241 PRO   A CG  1 
ATOM   1845 C CD  . PRO   A 1 241 ? 22.560  -15.802 4.505  1.00 56.79  ? 241 PRO   A CD  1 
ATOM   1846 N N   . LEU   A 1 242 ? 27.089  -15.988 5.805  1.00 51.28  ? 242 LEU   A N   1 
ATOM   1847 C CA  . LEU   A 1 242 ? 28.206  -15.177 6.265  1.00 58.48  ? 242 LEU   A CA  1 
ATOM   1848 C C   . LEU   A 1 242 ? 29.086  -14.837 5.069  1.00 59.78  ? 242 LEU   A C   1 
ATOM   1849 O O   . LEU   A 1 242 ? 29.615  -15.737 4.408  1.00 58.18  ? 242 LEU   A O   1 
ATOM   1850 C CB  . LEU   A 1 242 ? 29.008  -15.906 7.341  1.00 55.05  ? 242 LEU   A CB  1 
ATOM   1851 C CG  . LEU   A 1 242 ? 29.928  -15.005 8.166  1.00 54.67  ? 242 LEU   A CG  1 
ATOM   1852 C CD1 . LEU   A 1 242 ? 29.120  -14.018 8.999  1.00 54.42  ? 242 LEU   A CD1 1 
ATOM   1853 C CD2 . LEU   A 1 242 ? 30.821  -15.842 9.047  1.00 59.32  ? 242 LEU   A CD2 1 
ATOM   1854 N N   . THR   A 1 243 ? 29.234  -13.545 4.791  1.00 54.61  ? 243 THR   A N   1 
ATOM   1855 C CA  . THR   A 1 243 ? 30.022  -13.075 3.666  1.00 58.05  ? 243 THR   A CA  1 
ATOM   1856 C C   . THR   A 1 243 ? 31.402  -12.635 4.142  1.00 61.65  ? 243 THR   A C   1 
ATOM   1857 O O   . THR   A 1 243 ? 31.728  -12.683 5.332  1.00 60.85  ? 243 THR   A O   1 
ATOM   1858 C CB  . THR   A 1 243 ? 29.313  -11.926 2.947  1.00 56.28  ? 243 THR   A CB  1 
ATOM   1859 O OG1 . THR   A 1 243 ? 29.314  -10.764 3.786  1.00 57.22  ? 243 THR   A OG1 1 
ATOM   1860 C CG2 . THR   A 1 243 ? 27.878  -12.306 2.613  1.00 55.86  ? 243 THR   A CG2 1 
ATOM   1861 N N   . GLN   A 1 244 ? 32.223  -12.193 3.188  1.00 56.81  ? 244 GLN   A N   1 
ATOM   1862 C CA  . GLN   A 1 244 ? 33.542  -11.676 3.527  1.00 56.58  ? 244 GLN   A CA  1 
ATOM   1863 C C   . GLN   A 1 244 ? 33.469  -10.268 4.094  1.00 54.54  ? 244 GLN   A C   1 
ATOM   1864 O O   . GLN   A 1 244 ? 34.294  -9.906  4.940  1.00 55.92  ? 244 GLN   A O   1 
ATOM   1865 C CB  . GLN   A 1 244 ? 34.456  -11.690 2.305  1.00 54.84  ? 244 GLN   A CB  1 
ATOM   1866 C CG  . GLN   A 1 244 ? 35.903  -11.392 2.644  1.00 53.12  ? 244 GLN   A CG  1 
ATOM   1867 C CD  . GLN   A 1 244 ? 36.532  -12.486 3.484  1.00 50.52  ? 244 GLN   A CD  1 
ATOM   1868 O OE1 . GLN   A 1 244 ? 36.130  -13.647 3.411  1.00 57.75  ? 244 GLN   A OE1 1 
ATOM   1869 N NE2 . GLN   A 1 244 ? 37.523  -12.120 4.289  1.00 53.75  ? 244 GLN   A NE2 1 
ATOM   1870 N N   . ASP   A 1 245 ? 32.515  -9.459  3.628  1.00 52.94  ? 245 ASP   A N   1 
ATOM   1871 C CA  . ASP   A 1 245 ? 32.252  -8.186  4.289  1.00 60.29  ? 245 ASP   A CA  1 
ATOM   1872 C C   . ASP   A 1 245 ? 31.968  -8.398  5.768  1.00 57.45  ? 245 ASP   A C   1 
ATOM   1873 O O   . ASP   A 1 245 ? 32.501  -7.677  6.619  1.00 61.03  ? 245 ASP   A O   1 
ATOM   1874 C CB  . ASP   A 1 245 ? 31.083  -7.465  3.616  1.00 55.68  ? 245 ASP   A CB  1 
ATOM   1875 C CG  . ASP   A 1 245 ? 31.531  -6.546  2.499  1.00 74.57  ? 245 ASP   A CG  1 
ATOM   1876 O OD1 . ASP   A 1 245 ? 32.751  -6.291  2.395  1.00 77.54  ? 245 ASP   A OD1 1 
ATOM   1877 O OD2 . ASP   A 1 245 ? 30.667  -6.081  1.726  1.00 76.12  ? 245 ASP   A OD2 1 
ATOM   1878 N N   . HIS   A 1 246 ? 31.150  -9.402  6.092  1.00 57.95  ? 246 HIS   A N   1 
ATOM   1879 C CA  . HIS   A 1 246 ? 30.874  -9.713  7.490  1.00 50.65  ? 246 HIS   A CA  1 
ATOM   1880 C C   . HIS   A 1 246 ? 32.152  -10.079 8.236  1.00 54.28  ? 246 HIS   A C   1 
ATOM   1881 O O   . HIS   A 1 246 ? 32.376  -9.618  9.362  1.00 55.11  ? 246 HIS   A O   1 
ATOM   1882 C CB  . HIS   A 1 246 ? 29.851  -10.845 7.581  1.00 52.26  ? 246 HIS   A CB  1 
ATOM   1883 C CG  . HIS   A 1 246 ? 28.469  -10.448 7.163  1.00 51.38  ? 246 HIS   A CG  1 
ATOM   1884 N ND1 . HIS   A 1 246 ? 27.516  -11.368 6.783  1.00 51.89  ? 246 HIS   A ND1 1 
ATOM   1885 C CD2 . HIS   A 1 246 ? 27.876  -9.234  7.077  1.00 47.85  ? 246 HIS   A CD2 1 
ATOM   1886 C CE1 . HIS   A 1 246 ? 26.397  -10.737 6.473  1.00 54.85  ? 246 HIS   A CE1 1 
ATOM   1887 N NE2 . HIS   A 1 246 ? 26.589  -9.441  6.645  1.00 52.07  ? 246 HIS   A NE2 1 
ATOM   1888 N N   . VAL   A 1 247 ? 33.008  -10.899 7.622  1.00 56.46  ? 247 VAL   A N   1 
ATOM   1889 C CA  . VAL   A 1 247 ? 34.257  -11.285 8.271  1.00 51.51  ? 247 VAL   A CA  1 
ATOM   1890 C C   . VAL   A 1 247 ? 35.166  -10.072 8.447  1.00 53.59  ? 247 VAL   A C   1 
ATOM   1891 O O   . VAL   A 1 247 ? 35.863  -9.944  9.462  1.00 54.09  ? 247 VAL   A O   1 
ATOM   1892 C CB  . VAL   A 1 247 ? 34.941  -12.411 7.474  1.00 58.49  ? 247 VAL   A CB  1 
ATOM   1893 C CG1 . VAL   A 1 247 ? 36.287  -12.767 8.083  1.00 54.90  ? 247 VAL   A CG1 1 
ATOM   1894 C CG2 . VAL   A 1 247 ? 34.041  -13.639 7.423  1.00 59.03  ? 247 VAL   A CG2 1 
ATOM   1895 N N   . ASP   A 1 248 ? 35.163  -9.156  7.473  1.00 56.35  ? 248 ASP   A N   1 
ATOM   1896 C CA  . ASP   A 1 248 ? 35.929  -7.919  7.613  1.00 54.92  ? 248 ASP   A CA  1 
ATOM   1897 C C   . ASP   A 1 248 ? 35.392  -7.063  8.758  1.00 52.27  ? 248 ASP   A C   1 
ATOM   1898 O O   . ASP   A 1 248 ? 36.169  -6.486  9.528  1.00 46.94  ? 248 ASP   A O   1 
ATOM   1899 C CB  . ASP   A 1 248 ? 35.909  -7.130  6.298  1.00 62.33  ? 248 ASP   A CB  1 
ATOM   1900 C CG  . ASP   A 1 248 ? 36.872  -7.690  5.249  1.00 66.66  ? 248 ASP   A CG  1 
ATOM   1901 O OD1 . ASP   A 1 248 ? 37.952  -8.199  5.624  1.00 59.64  ? 248 ASP   A OD1 1 
ATOM   1902 O OD2 . ASP   A 1 248 ? 36.548  -7.612  4.044  1.00 68.01  ? 248 ASP   A OD2 1 
ATOM   1903 N N   . ILE   A 1 249 ? 34.064  -6.980  8.893  1.00 56.31  ? 249 ILE   A N   1 
ATOM   1904 C CA  . ILE   A 1 249 ? 33.455  -6.179  9.957  1.00 56.15  ? 249 ILE   A CA  1 
ATOM   1905 C C   . ILE   A 1 249 ? 33.856  -6.710  11.331 1.00 51.88  ? 249 ILE   A C   1 
ATOM   1906 O O   . ILE   A 1 249 ? 34.092  -5.938  12.269 1.00 51.41  ? 249 ILE   A O   1 
ATOM   1907 C CB  . ILE   A 1 249 ? 31.923  -6.146  9.784  1.00 54.65  ? 249 ILE   A CB  1 
ATOM   1908 C CG1 . ILE   A 1 249 ? 31.546  -5.416  8.493  1.00 54.95  ? 249 ILE   A CG1 1 
ATOM   1909 C CG2 . ILE   A 1 249 ? 31.252  -5.484  10.977 1.00 51.30  ? 249 ILE   A CG2 1 
ATOM   1910 C CD1 . ILE   A 1 249 ? 30.066  -5.459  8.176  1.00 66.61  ? 249 ILE   A CD1 1 
ATOM   1911 N N   . LEU   A 1 250 ? 33.953  -8.029  11.470 1.00 50.19  ? 250 LEU   A N   1 
ATOM   1912 C CA  . LEU   A 1 250 ? 34.352  -8.636  12.732 1.00 46.47  ? 250 LEU   A CA  1 
ATOM   1913 C C   . LEU   A 1 250 ? 35.854  -8.551  12.985 1.00 56.32  ? 250 LEU   A C   1 
ATOM   1914 O O   . LEU   A 1 250 ? 36.327  -9.089  13.993 1.00 56.77  ? 250 LEU   A O   1 
ATOM   1915 C CB  . LEU   A 1 250 ? 33.895  -10.099 12.768 1.00 54.77  ? 250 LEU   A CB  1 
ATOM   1916 C CG  . LEU   A 1 250 ? 32.383  -10.337 12.677 1.00 50.36  ? 250 LEU   A CG  1 
ATOM   1917 C CD1 . LEU   A 1 250 ? 32.083  -11.778 12.298 1.00 46.84  ? 250 LEU   A CD1 1 
ATOM   1918 C CD2 . LEU   A 1 250 ? 31.694  -9.977  13.989 1.00 47.01  ? 250 LEU   A CD2 1 
ATOM   1919 N N   . GLY   A 1 251 ? 36.604  -7.891  12.104 1.00 59.16  ? 251 GLY   A N   1 
ATOM   1920 C CA  . GLY   A 1 251 ? 38.038  -7.757  12.236 1.00 56.32  ? 251 GLY   A CA  1 
ATOM   1921 C C   . GLY   A 1 251 ? 38.515  -7.218  13.574 1.00 61.51  ? 251 GLY   A C   1 
ATOM   1922 O O   . GLY   A 1 251 ? 39.325  -7.853  14.258 1.00 62.39  ? 251 GLY   A O   1 
ATOM   1923 N N   . PRO   A 1 252 ? 38.049  -6.024  13.964 1.00 58.59  ? 252 PRO   A N   1 
ATOM   1924 C CA  . PRO   A 1 252 ? 38.489  -5.464  15.255 1.00 57.56  ? 252 PRO   A CA  1 
ATOM   1925 C C   . PRO   A 1 252 ? 38.191  -6.359  16.446 1.00 59.44  ? 252 PRO   A C   1 
ATOM   1926 O O   . PRO   A 1 252 ? 39.019  -6.458  17.362 1.00 61.45  ? 252 PRO   A O   1 
ATOM   1927 C CB  . PRO   A 1 252 ? 37.725  -4.137  15.333 1.00 59.43  ? 252 PRO   A CB  1 
ATOM   1928 C CG  . PRO   A 1 252 ? 37.507  -3.757  13.915 1.00 56.04  ? 252 PRO   A CG  1 
ATOM   1929 C CD  . PRO   A 1 252 ? 37.288  -5.042  13.170 1.00 58.24  ? 252 PRO   A CD  1 
ATOM   1930 N N   . LEU   A 1 253 ? 37.029  -7.017  16.463 1.00 57.58  ? 253 LEU   A N   1 
ATOM   1931 C CA  . LEU   A 1 253 ? 36.730  -7.951  17.545 1.00 57.92  ? 253 LEU   A CA  1 
ATOM   1932 C C   . LEU   A 1 253 ? 37.658  -9.156  17.508 1.00 62.19  ? 253 LEU   A C   1 
ATOM   1933 O O   . LEU   A 1 253 ? 38.170  -9.583  18.549 1.00 62.25  ? 253 LEU   A O   1 
ATOM   1934 C CB  . LEU   A 1 253 ? 35.276  -8.408  17.466 1.00 55.64  ? 253 LEU   A CB  1 
ATOM   1935 C CG  . LEU   A 1 253 ? 34.248  -7.375  17.910 1.00 52.75  ? 253 LEU   A CG  1 
ATOM   1936 C CD1 . LEU   A 1 253 ? 32.853  -7.915  17.684 1.00 51.86  ? 253 LEU   A CD1 1 
ATOM   1937 C CD2 . LEU   A 1 253 ? 34.473  -7.023  19.370 1.00 52.74  ? 253 LEU   A CD2 1 
ATOM   1938 N N   . SER   A 1 254 ? 37.875  -9.728  16.323 1.00 62.41  ? 254 SER   A N   1 
ATOM   1939 C CA  . SER   A 1 254 ? 38.790  -10.858 16.221 1.00 64.55  ? 254 SER   A CA  1 
ATOM   1940 C C   . SER   A 1 254 ? 40.202  -10.455 16.619 1.00 62.13  ? 254 SER   A C   1 
ATOM   1941 O O   . SER   A 1 254 ? 40.851  -11.145 17.415 1.00 59.88  ? 254 SER   A O   1 
ATOM   1942 C CB  . SER   A 1 254 ? 38.774  -11.426 14.803 1.00 64.95  ? 254 SER   A CB  1 
ATOM   1943 O OG  . SER   A 1 254 ? 39.547  -12.610 14.736 1.00 68.44  ? 254 SER   A OG  1 
ATOM   1944 N N   . ALA   A 1 255 ? 40.684  -9.328  16.094 1.00 63.42  ? 255 ALA   A N   1 
ATOM   1945 C CA  . ALA   A 1 255 ? 42.031  -8.857  16.385 1.00 64.77  ? 255 ALA   A CA  1 
ATOM   1946 C C   . ALA   A 1 255 ? 42.222  -8.457  17.841 1.00 70.12  ? 255 ALA   A C   1 
ATOM   1947 O O   . ALA   A 1 255 ? 43.369  -8.316  18.281 1.00 70.69  ? 255 ALA   A O   1 
ATOM   1948 C CB  . ALA   A 1 255 ? 42.380  -7.675  15.479 1.00 65.18  ? 255 ALA   A CB  1 
ATOM   1949 N N   . GLN   A 1 256 ? 41.142  -8.269  18.596 1.00 68.35  ? 256 GLN   A N   1 
ATOM   1950 C CA  . GLN   A 1 256 ? 41.262  -7.887  19.996 1.00 67.26  ? 256 GLN   A CA  1 
ATOM   1951 C C   . GLN   A 1 256 ? 41.418  -9.096  20.912 1.00 67.18  ? 256 GLN   A C   1 
ATOM   1952 O O   . GLN   A 1 256 ? 42.243  -9.081  21.830 1.00 69.73  ? 256 GLN   A O   1 
ATOM   1953 C CB  . GLN   A 1 256 ? 40.046  -7.067  20.417 1.00 68.31  ? 256 GLN   A CB  1 
ATOM   1954 C CG  . GLN   A 1 256 ? 40.023  -6.740  21.889 1.00 71.23  ? 256 GLN   A CG  1 
ATOM   1955 C CD  . GLN   A 1 256 ? 38.701  -6.149  22.319 1.00 81.22  ? 256 GLN   A CD  1 
ATOM   1956 O OE1 . GLN   A 1 256 ? 37.688  -6.305  21.635 1.00 81.47  ? 256 GLN   A OE1 1 
ATOM   1957 N NE2 . GLN   A 1 256 ? 38.701  -5.460  23.453 1.00 84.17  ? 256 GLN   A NE2 1 
ATOM   1958 N N   . THR   A 1 257 ? 40.629  -10.146 20.675 1.00 61.91  ? 257 THR   A N   1 
ATOM   1959 C CA  . THR   A 1 257 ? 40.665  -11.353 21.491 1.00 56.72  ? 257 THR   A CA  1 
ATOM   1960 C C   . THR   A 1 257 ? 41.712  -12.358 21.035 1.00 70.19  ? 257 THR   A C   1 
ATOM   1961 O O   . THR   A 1 257 ? 41.943  -13.347 21.741 1.00 65.33  ? 257 THR   A O   1 
ATOM   1962 C CB  . THR   A 1 257 ? 39.295  -12.037 21.482 1.00 60.87  ? 257 THR   A CB  1 
ATOM   1963 O OG1 . THR   A 1 257 ? 38.912  -12.318 20.130 1.00 59.73  ? 257 THR   A OG1 1 
ATOM   1964 C CG2 . THR   A 1 257 ? 38.247  -11.147 22.124 1.00 56.38  ? 257 THR   A CG2 1 
ATOM   1965 N N   . GLY   A 1 258 ? 42.338  -12.143 19.879 1.00 73.76  ? 258 GLY   A N   1 
ATOM   1966 C CA  . GLY   A 1 258 ? 43.260  -13.111 19.325 1.00 72.75  ? 258 GLY   A CA  1 
ATOM   1967 C C   . GLY   A 1 258 ? 42.619  -14.342 18.726 1.00 67.37  ? 258 GLY   A C   1 
ATOM   1968 O O   . GLY   A 1 258 ? 43.341  -15.270 18.345 1.00 74.15  ? 258 GLY   A O   1 
ATOM   1969 N N   . ILE   A 1 259 ? 41.293  -14.387 18.632 1.00 66.40  ? 259 ILE   A N   1 
ATOM   1970 C CA  . ILE   A 1 259 ? 40.575  -15.519 18.058 1.00 61.47  ? 259 ILE   A CA  1 
ATOM   1971 C C   . ILE   A 1 259 ? 40.172  -15.152 16.639 1.00 64.61  ? 259 ILE   A C   1 
ATOM   1972 O O   . ILE   A 1 259 ? 39.520  -14.125 16.416 1.00 58.65  ? 259 ILE   A O   1 
ATOM   1973 C CB  . ILE   A 1 259 ? 39.345  -15.885 18.899 1.00 62.57  ? 259 ILE   A CB  1 
ATOM   1974 C CG1 . ILE   A 1 259 ? 39.764  -16.181 20.337 1.00 62.52  ? 259 ILE   A CG1 1 
ATOM   1975 C CG2 . ILE   A 1 259 ? 38.612  -17.067 18.282 1.00 52.88  ? 259 ILE   A CG2 1 
ATOM   1976 C CD1 . ILE   A 1 259 ? 38.725  -15.792 21.348 1.00 62.81  ? 259 ILE   A CD1 1 
ATOM   1977 N N   . ALA   A 1 260 ? 40.557  -15.989 15.680 1.00 63.93  ? 260 ALA   A N   1 
ATOM   1978 C CA  . ALA   A 1 260 ? 40.216  -15.734 14.290 1.00 61.87  ? 260 ALA   A CA  1 
ATOM   1979 C C   . ALA   A 1 260 ? 38.712  -15.856 14.076 1.00 53.21  ? 260 ALA   A C   1 
ATOM   1980 O O   . ALA   A 1 260 ? 38.017  -16.595 14.780 1.00 56.63  ? 260 ALA   A O   1 
ATOM   1981 C CB  . ALA   A 1 260 ? 40.959  -16.697 13.364 1.00 61.67  ? 260 ALA   A CB  1 
ATOM   1982 N N   . VAL   A 1 261 ? 38.216  -15.110 13.086 1.00 54.77  ? 261 VAL   A N   1 
ATOM   1983 C CA  . VAL   A 1 261 ? 36.790  -15.124 12.769 1.00 52.13  ? 261 VAL   A CA  1 
ATOM   1984 C C   . VAL   A 1 261 ? 36.337  -16.533 12.411 1.00 51.68  ? 261 VAL   A C   1 
ATOM   1985 O O   . VAL   A 1 261 ? 35.282  -16.998 12.856 1.00 53.41  ? 261 VAL   A O   1 
ATOM   1986 C CB  . VAL   A 1 261 ? 36.485  -14.131 11.631 1.00 54.08  ? 261 VAL   A CB  1 
ATOM   1987 C CG1 . VAL   A 1 261 ? 34.999  -14.136 11.297 1.00 50.22  ? 261 VAL   A CG1 1 
ATOM   1988 C CG2 . VAL   A 1 261 ? 36.945  -12.736 12.007 1.00 58.93  ? 261 VAL   A CG2 1 
ATOM   1989 N N   . LEU   A 1 262 ? 37.127  -17.234 11.592 1.00 65.46  ? 262 LEU   A N   1 
ATOM   1990 C CA  . LEU   A 1 262 ? 36.741  -18.580 11.181 1.00 60.72  ? 262 LEU   A CA  1 
ATOM   1991 C C   . LEU   A 1 262 ? 36.772  -19.556 12.351 1.00 49.92  ? 262 LEU   A C   1 
ATOM   1992 O O   . LEU   A 1 262 ? 35.986  -20.510 12.380 1.00 53.62  ? 262 LEU   A O   1 
ATOM   1993 C CB  . LEU   A 1 262 ? 37.645  -19.067 10.046 1.00 58.49  ? 262 LEU   A CB  1 
ATOM   1994 C CG  . LEU   A 1 262 ? 37.386  -18.468 8.658  1.00 64.35  ? 262 LEU   A CG  1 
ATOM   1995 C CD1 . LEU   A 1 262 ? 35.890  -18.447 8.344  1.00 60.66  ? 262 LEU   A CD1 1 
ATOM   1996 C CD2 . LEU   A 1 262 ? 38.001  -17.077 8.512  1.00 51.71  ? 262 LEU   A CD2 1 
ATOM   1997 N N   . ASP   A 1 263 ? 37.658  -19.330 13.325 1.00 55.69  ? 263 ASP   A N   1 
ATOM   1998 C CA  . ASP   A 1 263 ? 37.664  -20.166 14.523 1.00 52.90  ? 263 ASP   A CA  1 
ATOM   1999 C C   . ASP   A 1 263 ? 36.417  -19.933 15.364 1.00 55.70  ? 263 ASP   A C   1 
ATOM   2000 O O   . ASP   A 1 263 ? 35.897  -20.866 15.989 1.00 55.56  ? 263 ASP   A O   1 
ATOM   2001 C CB  . ASP   A 1 263 ? 38.918  -19.897 15.351 1.00 61.88  ? 263 ASP   A CB  1 
ATOM   2002 C CG  . ASP   A 1 263 ? 40.111  -20.684 14.861 1.00 74.98  ? 263 ASP   A CG  1 
ATOM   2003 O OD1 . ASP   A 1 263 ? 40.027  -21.252 13.752 1.00 77.96  ? 263 ASP   A OD1 1 
ATOM   2004 O OD2 . ASP   A 1 263 ? 41.125  -20.747 15.589 1.00 79.19  ? 263 ASP   A OD2 1 
ATOM   2005 N N   . MET   A 1 264 ? 35.929  -18.692 15.401 1.00 61.54  ? 264 MET   A N   1 
ATOM   2006 C CA  . MET   A 1 264 ? 34.674  -18.425 16.091 1.00 53.85  ? 264 MET   A CA  1 
ATOM   2007 C C   . MET   A 1 264 ? 33.501  -19.088 15.381 1.00 53.97  ? 264 MET   A C   1 
ATOM   2008 O O   . MET   A 1 264 ? 32.548  -19.523 16.036 1.00 56.78  ? 264 MET   A O   1 
ATOM   2009 C CB  . MET   A 1 264 ? 34.450  -16.917 16.209 1.00 54.25  ? 264 MET   A CB  1 
ATOM   2010 C CG  . MET   A 1 264 ? 33.316  -16.532 17.148 1.00 53.38  ? 264 MET   A CG  1 
ATOM   2011 S SD  . MET   A 1 264 ? 33.627  -17.049 18.847 1.00 56.27  ? 264 MET   A SD  1 
ATOM   2012 C CE  . MET   A 1 264 ? 34.814  -15.818 19.380 1.00 52.28  ? 264 MET   A CE  1 
ATOM   2013 N N   . CYS   A 1 265 ? 33.556  -19.187 14.048 1.00 56.27  ? 265 CYS   A N   1 
ATOM   2014 C CA  . CYS   A 1 265 ? 32.478  -19.843 13.312 1.00 58.42  ? 265 CYS   A CA  1 
ATOM   2015 C C   . CYS   A 1 265 ? 32.423  -21.334 13.618 1.00 58.76  ? 265 CYS   A C   1 
ATOM   2016 O O   . CYS   A 1 265 ? 31.339  -21.928 13.648 1.00 62.57  ? 265 CYS   A O   1 
ATOM   2017 C CB  . CYS   A 1 265 ? 32.643  -19.615 11.810 1.00 50.11  ? 265 CYS   A CB  1 
ATOM   2018 S SG  . CYS   A 1 265 ? 32.517  -17.892 11.297 1.00 60.40  ? 265 CYS   A SG  1 
ATOM   2019 N N   . ALA   A 1 266 ? 33.581  -21.961 13.844 1.00 67.20  ? 266 ALA   A N   1 
ATOM   2020 C CA  . ALA   A 1 266 ? 33.589  -23.368 14.236 1.00 63.30  ? 266 ALA   A CA  1 
ATOM   2021 C C   . ALA   A 1 266 ? 32.934  -23.564 15.596 1.00 61.97  ? 266 ALA   A C   1 
ATOM   2022 O O   . ALA   A 1 266 ? 32.230  -24.558 15.815 1.00 65.84  ? 266 ALA   A O   1 
ATOM   2023 C CB  . ALA   A 1 266 ? 35.016  -23.906 14.246 1.00 67.53  ? 266 ALA   A CB  1 
ATOM   2024 N N   . SER   A 1 267 ? 33.150  -22.624 16.522 1.00 66.22  ? 267 SER   A N   1 
ATOM   2025 C CA  . SER   A 1 267 ? 32.471  -22.683 17.814 1.00 61.84  ? 267 SER   A CA  1 
ATOM   2026 C C   . SER   A 1 267 ? 30.966  -22.523 17.652 1.00 52.48  ? 267 SER   A C   1 
ATOM   2027 O O   . SER   A 1 267 ? 30.186  -23.231 18.301 1.00 58.58  ? 267 SER   A O   1 
ATOM   2028 C CB  . SER   A 1 267 ? 33.022  -21.608 18.750 1.00 61.66  ? 267 SER   A CB  1 
ATOM   2029 O OG  . SER   A 1 267 ? 34.397  -21.818 19.014 1.00 67.61  ? 267 SER   A OG  1 
ATOM   2030 N N   . LEU   A 1 268 ? 30.538  -21.597 16.791 1.00 60.42  ? 268 LEU   A N   1 
ATOM   2031 C CA  . LEU   A 1 268 ? 29.111  -21.442 16.528 1.00 57.46  ? 268 LEU   A CA  1 
ATOM   2032 C C   . LEU   A 1 268 ? 28.540  -22.669 15.832 1.00 54.57  ? 268 LEU   A C   1 
ATOM   2033 O O   . LEU   A 1 268 ? 27.370  -23.012 16.037 1.00 58.85  ? 268 LEU   A O   1 
ATOM   2034 C CB  . LEU   A 1 268 ? 28.865  -20.188 15.690 1.00 54.24  ? 268 LEU   A CB  1 
ATOM   2035 C CG  . LEU   A 1 268 ? 27.414  -19.906 15.297 1.00 50.09  ? 268 LEU   A CG  1 
ATOM   2036 C CD1 . LEU   A 1 268 ? 26.520  -19.892 16.526 1.00 47.34  ? 268 LEU   A CD1 1 
ATOM   2037 C CD2 . LEU   A 1 268 ? 27.317  -18.589 14.549 1.00 51.08  ? 268 LEU   A CD2 1 
ATOM   2038 N N   . LYS   A 1 269 ? 29.346  -23.341 15.009 1.00 65.74  ? 269 LYS   A N   1 
ATOM   2039 C CA  . LYS   A 1 269 ? 28.907  -24.593 14.404 1.00 64.24  ? 269 LYS   A CA  1 
ATOM   2040 C C   . LYS   A 1 269 ? 28.565  -25.626 15.469 1.00 60.83  ? 269 LYS   A C   1 
ATOM   2041 O O   . LYS   A 1 269 ? 27.534  -26.304 15.383 1.00 62.17  ? 269 LYS   A O   1 
ATOM   2042 C CB  . LYS   A 1 269 ? 29.992  -25.131 13.477 1.00 64.90  ? 269 LYS   A CB  1 
ATOM   2043 C CG  . LYS   A 1 269 ? 29.709  -26.521 12.946 1.00 69.66  ? 269 LYS   A CG  1 
ATOM   2044 C CD  . LYS   A 1 269 ? 30.925  -27.091 12.248 1.00 66.90  ? 269 LYS   A CD  1 
ATOM   2045 C CE  . LYS   A 1 269 ? 31.476  -26.101 11.240 1.00 70.83  ? 269 LYS   A CE  1 
ATOM   2046 N NZ  . LYS   A 1 269 ? 30.454  -25.709 10.230 1.00 79.64  ? 269 LYS   A NZ  1 
ATOM   2047 N N   . GLU   A 1 270 ? 29.416  -25.750 16.490 1.00 65.25  ? 270 GLU   A N   1 
ATOM   2048 C CA  . GLU   A 1 270 ? 29.200  -26.757 17.523 1.00 61.95  ? 270 GLU   A CA  1 
ATOM   2049 C C   . GLU   A 1 270 ? 28.009  -26.406 18.408 1.00 68.85  ? 270 GLU   A C   1 
ATOM   2050 O O   . GLU   A 1 270 ? 27.295  -27.299 18.878 1.00 69.62  ? 270 GLU   A O   1 
ATOM   2051 C CB  . GLU   A 1 270 ? 30.471  -26.923 18.359 1.00 67.94  ? 270 GLU   A CB  1 
ATOM   2052 C CG  . GLU   A 1 270 ? 30.431  -28.086 19.341 1.00 76.25  ? 270 GLU   A CG  1 
ATOM   2053 C CD  . GLU   A 1 270 ? 31.816  -28.545 19.768 1.00 82.33  ? 270 GLU   A CD  1 
ATOM   2054 O OE1 . GLU   A 1 270 ? 32.778  -27.759 19.625 1.00 81.19  ? 270 GLU   A OE1 1 
ATOM   2055 O OE2 . GLU   A 1 270 ? 31.943  -29.697 20.238 1.00 80.23  ? 270 GLU   A OE2 1 
ATOM   2056 N N   . LEU   A 1 271 ? 27.772  -25.113 18.644 1.00 60.57  ? 271 LEU   A N   1 
ATOM   2057 C CA  . LEU   A 1 271 ? 26.633  -24.720 19.467 1.00 62.31  ? 271 LEU   A CA  1 
ATOM   2058 C C   . LEU   A 1 271 ? 25.312  -24.953 18.744 1.00 59.46  ? 271 LEU   A C   1 
ATOM   2059 O O   . LEU   A 1 271 ? 24.296  -25.242 19.388 1.00 54.29  ? 271 LEU   A O   1 
ATOM   2060 C CB  . LEU   A 1 271 ? 26.765  -23.254 19.882 1.00 63.08  ? 271 LEU   A CB  1 
ATOM   2061 N N   . LEU   A 1 272 ? 25.305  -24.832 17.414 1.00 56.93  ? 272 LEU   A N   1 
ATOM   2062 C CA  . LEU   A 1 272 ? 24.082  -25.071 16.654 1.00 63.50  ? 272 LEU   A CA  1 
ATOM   2063 C C   . LEU   A 1 272 ? 23.763  -26.558 16.579 1.00 64.23  ? 272 LEU   A C   1 
ATOM   2064 O O   . LEU   A 1 272 ? 22.606  -26.959 16.746 1.00 67.46  ? 272 LEU   A O   1 
ATOM   2065 C CB  . LEU   A 1 272 ? 24.209  -24.481 15.246 1.00 61.64  ? 272 LEU   A CB  1 
ATOM   2066 C CG  . LEU   A 1 272 ? 24.343  -22.962 15.093 1.00 61.58  ? 272 LEU   A CG  1 
ATOM   2067 C CD1 . LEU   A 1 272 ? 24.522  -22.585 13.629 1.00 60.58  ? 272 LEU   A CD1 1 
ATOM   2068 C CD2 . LEU   A 1 272 ? 23.141  -22.247 15.692 1.00 52.00  ? 272 LEU   A CD2 1 
ATOM   2069 N N   . GLN   A 1 273 ? 24.780  -27.392 16.335 1.00 66.72  ? 273 GLN   A N   1 
ATOM   2070 C CA  . GLN   A 1 273 ? 24.550  -28.824 16.167 1.00 67.79  ? 273 GLN   A CA  1 
ATOM   2071 C C   . GLN   A 1 273 ? 24.199  -29.509 17.482 1.00 69.16  ? 273 GLN   A C   1 
ATOM   2072 O O   . GLN   A 1 273 ? 23.436  -30.481 17.485 1.00 65.31  ? 273 GLN   A O   1 
ATOM   2073 C CB  . GLN   A 1 273 ? 25.784  -29.491 15.556 1.00 67.41  ? 273 GLN   A CB  1 
ATOM   2074 C CG  . GLN   A 1 273 ? 26.156  -29.013 14.160 1.00 67.11  ? 273 GLN   A CG  1 
ATOM   2075 C CD  . GLN   A 1 273 ? 27.434  -29.660 13.643 1.00 67.76  ? 273 GLN   A CD  1 
ATOM   2076 O OE1 . GLN   A 1 273 ? 27.996  -30.552 14.282 1.00 70.75  ? 273 GLN   A OE1 1 
ATOM   2077 N NE2 . GLN   A 1 273 ? 27.900  -29.209 12.482 1.00 63.23  ? 273 GLN   A NE2 1 
ATOM   2078 N N   . ASN   A 1 274 ? 24.747  -29.039 18.600 1.00 68.33  ? 274 ASN   A N   1 
ATOM   2079 C CA  . ASN   A 1 274 ? 24.563  -29.717 19.875 1.00 70.04  ? 274 ASN   A CA  1 
ATOM   2080 C C   . ASN   A 1 274 ? 23.677  -28.963 20.854 1.00 74.44  ? 274 ASN   A C   1 
ATOM   2081 O O   . ASN   A 1 274 ? 22.978  -29.599 21.645 1.00 68.95  ? 274 ASN   A O   1 
ATOM   2082 C CB  . ASN   A 1 274 ? 25.923  -29.978 20.537 1.00 71.73  ? 274 ASN   A CB  1 
ATOM   2083 C CG  . ASN   A 1 274 ? 26.908  -30.658 19.599 1.00 73.48  ? 274 ASN   A CG  1 
ATOM   2084 O OD1 . ASN   A 1 274 ? 27.995  -30.143 19.340 1.00 67.02  ? 274 ASN   A OD1 1 
ATOM   2085 N ND2 . ASN   A 1 274 ? 26.527  -31.821 19.083 1.00 80.14  ? 274 ASN   A ND2 1 
ATOM   2086 N N   . GLY   A 1 275 ? 23.676  -27.635 20.813 1.00 68.47  ? 275 GLY   A N   1 
ATOM   2087 C CA  . GLY   A 1 275 ? 22.986  -26.850 21.813 1.00 68.01  ? 275 GLY   A CA  1 
ATOM   2088 C C   . GLY   A 1 275 ? 23.919  -26.437 22.929 1.00 68.50  ? 275 GLY   A C   1 
ATOM   2089 O O   . GLY   A 1 275 ? 25.128  -26.685 22.908 1.00 73.18  ? 275 GLY   A O   1 
ATOM   2090 N N   . MET   A 1 276 ? 23.338  -25.786 23.932 1.00 69.74  ? 276 MET   A N   1 
ATOM   2091 C CA  . MET   A 1 276 ? 24.111  -25.324 25.075 1.00 71.42  ? 276 MET   A CA  1 
ATOM   2092 C C   . MET   A 1 276 ? 24.164  -26.340 26.207 1.00 83.26  ? 276 MET   A C   1 
ATOM   2093 O O   . MET   A 1 276 ? 24.972  -26.170 27.129 1.00 79.68  ? 276 MET   A O   1 
ATOM   2094 C CB  . MET   A 1 276 ? 23.546  -24.005 25.601 1.00 76.32  ? 276 MET   A CB  1 
ATOM   2095 C CG  . MET   A 1 276 ? 23.635  -22.861 24.610 1.00 69.38  ? 276 MET   A CG  1 
ATOM   2096 S SD  . MET   A 1 276 ? 23.349  -21.284 25.426 1.00 72.48  ? 276 MET   A SD  1 
ATOM   2097 C CE  . MET   A 1 276 ? 23.377  -20.168 24.029 1.00 59.00  ? 276 MET   A CE  1 
ATOM   2098 N N   . ASN   A 1 277 ? 23.331  -27.383 26.157 1.00 78.93  ? 277 ASN   A N   1 
ATOM   2099 C CA  . ASN   A 1 277 ? 23.340  -28.453 27.154 1.00 77.64  ? 277 ASN   A CA  1 
ATOM   2100 C C   . ASN   A 1 277 ? 23.139  -27.895 28.560 1.00 74.23  ? 277 ASN   A C   1 
ATOM   2101 O O   . ASN   A 1 277 ? 23.832  -28.277 29.506 1.00 82.32  ? 277 ASN   A O   1 
ATOM   2102 C CB  . ASN   A 1 277 ? 24.629  -29.276 27.068 1.00 75.37  ? 277 ASN   A CB  1 
ATOM   2103 N N   . GLY   A 1 278 ? 22.193  -26.967 28.693 1.00 68.49  ? 278 GLY   A N   1 
ATOM   2104 C CA  . GLY   A 1 278 ? 21.875  -26.377 29.975 1.00 76.95  ? 278 GLY   A CA  1 
ATOM   2105 C C   . GLY   A 1 278 ? 22.829  -25.306 30.455 1.00 71.07  ? 278 GLY   A C   1 
ATOM   2106 O O   . GLY   A 1 278 ? 22.642  -24.790 31.563 1.00 72.21  ? 278 GLY   A O   1 
ATOM   2107 N N   . ARG   A 1 279 ? 23.845  -24.960 29.674 1.00 78.00  ? 279 ARG   A N   1 
ATOM   2108 C CA  . ARG   A 1 279 ? 24.757  -23.890 30.041 1.00 75.49  ? 279 ARG   A CA  1 
ATOM   2109 C C   . ARG   A 1 279 ? 24.210  -22.546 29.564 1.00 70.42  ? 279 ARG   A C   1 
ATOM   2110 O O   . ARG   A 1 279 ? 23.234  -22.471 28.814 1.00 67.37  ? 279 ARG   A O   1 
ATOM   2111 C CB  . ARG   A 1 279 ? 26.149  -24.147 29.459 1.00 72.21  ? 279 ARG   A CB  1 
ATOM   2112 N N   . THR   A 1 280 ? 24.848  -21.472 30.019 1.00 65.15  ? 280 THR   A N   1 
ATOM   2113 C CA  . THR   A 1 280 ? 24.454  -20.126 29.640 1.00 59.21  ? 280 THR   A CA  1 
ATOM   2114 C C   . THR   A 1 280 ? 25.648  -19.387 29.056 1.00 58.92  ? 280 THR   A C   1 
ATOM   2115 O O   . THR   A 1 280 ? 26.803  -19.698 29.358 1.00 57.91  ? 280 THR   A O   1 
ATOM   2116 C CB  . THR   A 1 280 ? 23.892  -19.330 30.831 1.00 58.88  ? 280 THR   A CB  1 
ATOM   2117 O OG1 . THR   A 1 280 ? 24.924  -19.127 31.803 1.00 57.83  ? 280 THR   A OG1 1 
ATOM   2118 C CG2 . THR   A 1 280 ? 22.728  -20.072 31.473 1.00 56.01  ? 280 THR   A CG2 1 
ATOM   2119 N N   . ILE   A 1 281 ? 25.352  -18.409 28.205 1.00 53.14  ? 281 ILE   A N   1 
ATOM   2120 C CA  . ILE   A 1 281 ? 26.353  -17.505 27.654 1.00 54.82  ? 281 ILE   A CA  1 
ATOM   2121 C C   . ILE   A 1 281 ? 25.864  -16.088 27.894 1.00 51.46  ? 281 ILE   A C   1 
ATOM   2122 O O   . ILE   A 1 281 ? 24.798  -15.707 27.395 1.00 46.18  ? 281 ILE   A O   1 
ATOM   2123 C CB  . ILE   A 1 281 ? 26.594  -17.740 26.156 1.00 53.18  ? 281 ILE   A CB  1 
ATOM   2124 C CG1 . ILE   A 1 281 ? 26.967  -19.196 25.892 1.00 55.34  ? 281 ILE   A CG1 1 
ATOM   2125 C CG2 . ILE   A 1 281 ? 27.683  -16.818 25.657 1.00 49.45  ? 281 ILE   A CG2 1 
ATOM   2126 C CD1 . ILE   A 1 281 ? 27.145  -19.512 24.428 1.00 50.57  ? 281 ILE   A CD1 1 
ATOM   2127 N N   . LEU   A 1 282 ? 26.640  -15.308 28.648 1.00 50.54  ? 282 LEU   A N   1 
ATOM   2128 C CA  . LEU   A 1 282 ? 26.251  -13.947 29.012 1.00 48.96  ? 282 LEU   A CA  1 
ATOM   2129 C C   . LEU   A 1 282 ? 24.842  -13.925 29.601 1.00 46.78  ? 282 LEU   A C   1 
ATOM   2130 O O   . LEU   A 1 282 ? 24.008  -13.089 29.246 1.00 47.93  ? 282 LEU   A O   1 
ATOM   2131 C CB  . LEU   A 1 282 ? 26.358  -13.005 27.812 1.00 45.56  ? 282 LEU   A CB  1 
ATOM   2132 C CG  . LEU   A 1 282 ? 27.761  -12.572 27.391 1.00 43.74  ? 282 LEU   A CG  1 
ATOM   2133 C CD1 . LEU   A 1 282 ? 27.690  -11.678 26.167 1.00 46.46  ? 282 LEU   A CD1 1 
ATOM   2134 C CD2 . LEU   A 1 282 ? 28.454  -11.855 28.533 1.00 45.07  ? 282 LEU   A CD2 1 
ATOM   2135 N N   . GLY   A 1 283 ? 24.567  -14.877 30.491 1.00 53.75  ? 283 GLY   A N   1 
ATOM   2136 C CA  . GLY   A 1 283 ? 23.283  -14.946 31.159 1.00 51.97  ? 283 GLY   A CA  1 
ATOM   2137 C C   . GLY   A 1 283 ? 22.117  -15.393 30.307 1.00 53.39  ? 283 GLY   A C   1 
ATOM   2138 O O   . GLY   A 1 283 ? 20.975  -15.335 30.772 1.00 49.13  ? 283 GLY   A O   1 
ATOM   2139 N N   . SER   A 1 284 ? 22.358  -15.842 29.078 1.00 57.17  ? 284 SER   A N   1 
ATOM   2140 C CA  . SER   A 1 284 ? 21.290  -16.238 28.171 1.00 47.02  ? 284 SER   A CA  1 
ATOM   2141 C C   . SER   A 1 284 ? 21.409  -17.717 27.832 1.00 51.44  ? 284 SER   A C   1 
ATOM   2142 O O   . SER   A 1 284 ? 22.516  -18.238 27.659 1.00 52.34  ? 284 SER   A O   1 
ATOM   2143 C CB  . SER   A 1 284 ? 21.324  -15.407 26.884 1.00 53.06  ? 284 SER   A CB  1 
ATOM   2144 O OG  . SER   A 1 284 ? 20.351  -15.863 25.958 1.00 54.65  ? 284 SER   A OG  1 
ATOM   2145 N N   . ALA   A 1 285 ? 20.264  -18.389 27.732 1.00 49.83  ? 285 ALA   A N   1 
ATOM   2146 C CA  . ALA   A 1 285 ? 20.223  -19.774 27.282 1.00 53.52  ? 285 ALA   A CA  1 
ATOM   2147 C C   . ALA   A 1 285 ? 19.999  -19.904 25.780 1.00 45.80  ? 285 ALA   A C   1 
ATOM   2148 O O   . ALA   A 1 285 ? 19.953  -21.028 25.272 1.00 52.03  ? 285 ALA   A O   1 
ATOM   2149 C CB  . ALA   A 1 285 ? 19.135  -20.547 28.033 1.00 48.55  ? 285 ALA   A CB  1 
ATOM   2150 N N   . LEU   A 1 286 ? 19.858  -18.790 25.064 1.00 46.86  ? 286 LEU   A N   1 
ATOM   2151 C CA  . LEU   A 1 286 ? 19.701  -18.783 23.617 1.00 44.01  ? 286 LEU   A CA  1 
ATOM   2152 C C   . LEU   A 1 286 ? 20.779  -17.911 22.984 1.00 48.12  ? 286 LEU   A C   1 
ATOM   2153 O O   . LEU   A 1 286 ? 21.378  -17.053 23.636 1.00 46.33  ? 286 LEU   A O   1 
ATOM   2154 C CB  . LEU   A 1 286 ? 18.313  -18.266 23.206 1.00 50.80  ? 286 LEU   A CB  1 
ATOM   2155 C CG  . LEU   A 1 286 ? 17.084  -19.030 23.703 1.00 47.00  ? 286 LEU   A CG  1 
ATOM   2156 C CD1 . LEU   A 1 286 ? 15.800  -18.288 23.348 1.00 49.25  ? 286 LEU   A CD1 1 
ATOM   2157 C CD2 . LEU   A 1 286 ? 17.066  -20.435 23.123 1.00 51.24  ? 286 LEU   A CD2 1 
ATOM   2158 N N   . LEU   A 1 287 ? 21.016  -18.134 21.695 1.00 50.07  ? 287 LEU   A N   1 
ATOM   2159 C CA  . LEU   A 1 287 ? 21.969  -17.322 20.950 1.00 43.52  ? 287 LEU   A CA  1 
ATOM   2160 C C   . LEU   A 1 287 ? 21.321  -15.992 20.581 1.00 42.33  ? 287 LEU   A C   1 
ATOM   2161 O O   . LEU   A 1 287 ? 20.224  -15.966 20.013 1.00 46.46  ? 287 LEU   A O   1 
ATOM   2162 C CB  . LEU   A 1 287 ? 22.437  -18.075 19.709 1.00 49.68  ? 287 LEU   A CB  1 
ATOM   2163 C CG  . LEU   A 1 287 ? 23.159  -19.381 20.047 1.00 50.96  ? 287 LEU   A CG  1 
ATOM   2164 C CD1 . LEU   A 1 287 ? 23.418  -20.209 18.802 1.00 51.17  ? 287 LEU   A CD1 1 
ATOM   2165 C CD2 . LEU   A 1 287 ? 24.463  -19.098 20.781 1.00 47.36  ? 287 LEU   A CD2 1 
ATOM   2166 N N   . GLU   A 1 288 ? 21.998  -14.891 20.901 1.00 39.44  ? 288 GLU   A N   1 
ATOM   2167 C CA  . GLU   A 1 288 ? 21.448  -13.548 20.756 1.00 42.41  ? 288 GLU   A CA  1 
ATOM   2168 C C   . GLU   A 1 288 ? 21.979  -12.888 19.490 1.00 37.45  ? 288 GLU   A C   1 
ATOM   2169 O O   . GLU   A 1 288 ? 23.194  -12.821 19.284 1.00 37.51  ? 288 GLU   A O   1 
ATOM   2170 C CB  . GLU   A 1 288 ? 21.793  -12.692 21.975 1.00 40.03  ? 288 GLU   A CB  1 
ATOM   2171 C CG  . GLU   A 1 288 ? 20.761  -12.764 23.084 1.00 56.80  ? 288 GLU   A CG  1 
ATOM   2172 C CD  . GLU   A 1 288 ? 19.408  -12.227 22.646 1.00 65.98  ? 288 GLU   A CD  1 
ATOM   2173 O OE1 . GLU   A 1 288 ? 19.379  -11.199 21.928 1.00 60.55  ? 288 GLU   A OE1 1 
ATOM   2174 O OE2 . GLU   A 1 288 ? 18.380  -12.844 23.008 1.00 62.54  ? 288 GLU   A OE2 1 
ATOM   2175 N N   . ASP   A 1 289 ? 21.072  -12.378 18.654 1.00 36.68  ? 289 ASP   A N   1 
ATOM   2176 C CA  . ASP   A 1 289 ? 21.465  -11.784 17.380 1.00 43.89  ? 289 ASP   A CA  1 
ATOM   2177 C C   . ASP   A 1 289 ? 21.070  -10.315 17.259 1.00 46.81  ? 289 ASP   A C   1 
ATOM   2178 O O   . ASP   A 1 289 ? 20.945  -9.805  16.142 1.00 39.23  ? 289 ASP   A O   1 
ATOM   2179 C CB  . ASP   A 1 289 ? 20.881  -12.584 16.213 1.00 36.77  ? 289 ASP   A CB  1 
ATOM   2180 C CG  . ASP   A 1 289 ? 19.389  -12.357 16.025 1.00 46.84  ? 289 ASP   A CG  1 
ATOM   2181 O OD1 . ASP   A 1 289 ? 18.696  -12.020 17.009 1.00 42.74  ? 289 ASP   A OD1 1 
ATOM   2182 O OD2 . ASP   A 1 289 ? 18.907  -12.519 14.881 1.00 45.06  ? 289 ASP   A OD2 1 
ATOM   2183 N N   . GLU   A 1 290 ? 20.879  -9.613  18.376 1.00 41.37  ? 290 GLU   A N   1 
ATOM   2184 C CA  . GLU   A 1 290 ? 20.473  -8.214  18.330 1.00 46.48  ? 290 GLU   A CA  1 
ATOM   2185 C C   . GLU   A 1 290 ? 21.586  -7.271  18.782 1.00 46.31  ? 290 GLU   A C   1 
ATOM   2186 O O   . GLU   A 1 290 ? 21.321  -6.141  19.198 1.00 40.64  ? 290 GLU   A O   1 
ATOM   2187 C CB  . GLU   A 1 290 ? 19.202  -8.008  19.151 1.00 45.19  ? 290 GLU   A CB  1 
ATOM   2188 C CG  . GLU   A 1 290 ? 18.030  -8.826  18.621 1.00 46.54  ? 290 GLU   A CG  1 
ATOM   2189 C CD  . GLU   A 1 290 ? 16.802  -7.984  18.320 1.00 51.35  ? 290 GLU   A CD  1 
ATOM   2190 O OE1 . GLU   A 1 290 ? 16.684  -6.873  18.880 1.00 50.81  ? 290 GLU   A OE1 1 
ATOM   2191 O OE2 . GLU   A 1 290 ? 15.952  -8.436  17.522 1.00 43.71  ? 290 GLU   A OE2 1 
ATOM   2192 N N   . PHE   A 1 291 ? 22.837  -7.714  18.684 1.00 39.01  ? 291 PHE   A N   1 
ATOM   2193 C CA  . PHE   A 1 291 ? 24.003  -6.874  18.936 1.00 40.90  ? 291 PHE   A CA  1 
ATOM   2194 C C   . PHE   A 1 291 ? 24.855  -6.836  17.675 1.00 44.43  ? 291 PHE   A C   1 
ATOM   2195 O O   . PHE   A 1 291 ? 25.378  -7.871  17.249 1.00 41.56  ? 291 PHE   A O   1 
ATOM   2196 C CB  . PHE   A 1 291 ? 24.831  -7.409  20.110 1.00 38.84  ? 291 PHE   A CB  1 
ATOM   2197 C CG  . PHE   A 1 291 ? 24.151  -7.303  21.447 1.00 47.12  ? 291 PHE   A CG  1 
ATOM   2198 C CD1 . PHE   A 1 291 ? 24.129  -6.098  22.136 1.00 50.74  ? 291 PHE   A CD1 1 
ATOM   2199 C CD2 . PHE   A 1 291 ? 23.553  -8.411  22.027 1.00 41.77  ? 291 PHE   A CD2 1 
ATOM   2200 C CE1 . PHE   A 1 291 ? 23.511  -5.996  23.375 1.00 43.06  ? 291 PHE   A CE1 1 
ATOM   2201 C CE2 . PHE   A 1 291 ? 22.933  -8.316  23.264 1.00 49.33  ? 291 PHE   A CE2 1 
ATOM   2202 C CZ  . PHE   A 1 291 ? 22.912  -7.106  23.938 1.00 44.76  ? 291 PHE   A CZ  1 
ATOM   2203 N N   . THR   A 1 292 ? 25.003  -5.650  17.082 1.00 46.97  ? 292 THR   A N   1 
ATOM   2204 C CA  . THR   A 1 292 ? 25.900  -5.497  15.944 1.00 39.32  ? 292 THR   A CA  1 
ATOM   2205 C C   . THR   A 1 292 ? 27.351  -5.485  16.420 1.00 42.68  ? 292 THR   A C   1 
ATOM   2206 O O   . THR   A 1 292 ? 27.623  -5.286  17.606 1.00 42.05  ? 292 THR   A O   1 
ATOM   2207 C CB  . THR   A 1 292 ? 25.610  -4.207  15.180 1.00 41.54  ? 292 THR   A CB  1 
ATOM   2208 O OG1 . THR   A 1 292 ? 25.950  -3.080  15.998 1.00 46.36  ? 292 THR   A OG1 1 
ATOM   2209 C CG2 . THR   A 1 292 ? 24.150  -4.130  14.776 1.00 45.37  ? 292 THR   A CG2 1 
ATOM   2210 N N   . PRO   A 1 293 ? 28.306  -5.699  15.509 1.00 40.21  ? 293 PRO   A N   1 
ATOM   2211 C CA  . PRO   A 1 293 ? 29.714  -5.533  15.898 1.00 37.06  ? 293 PRO   A CA  1 
ATOM   2212 C C   . PRO   A 1 293 ? 30.022  -4.152  16.447 1.00 42.14  ? 293 PRO   A C   1 
ATOM   2213 O O   . PRO   A 1 293 ? 30.818  -4.036  17.386 1.00 37.82  ? 293 PRO   A O   1 
ATOM   2214 C CB  . PRO   A 1 293 ? 30.467  -5.819  14.593 1.00 45.38  ? 293 PRO   A CB  1 
ATOM   2215 C CG  . PRO   A 1 293 ? 29.570  -6.773  13.870 1.00 45.85  ? 293 PRO   A CG  1 
ATOM   2216 C CD  . PRO   A 1 293 ? 28.176  -6.283  14.162 1.00 40.21  ? 293 PRO   A CD  1 
ATOM   2217 N N   . PHE   A 1 294 ? 29.404  -3.099  15.905 1.00 45.80  ? 294 PHE   A N   1 
ATOM   2218 C CA  . PHE   A 1 294 ? 29.567  -1.777  16.502 1.00 49.07  ? 294 PHE   A CA  1 
ATOM   2219 C C   . PHE   A 1 294 ? 29.090  -1.766  17.950 1.00 47.94  ? 294 PHE   A C   1 
ATOM   2220 O O   . PHE   A 1 294 ? 29.765  -1.215  18.829 1.00 47.43  ? 294 PHE   A O   1 
ATOM   2221 C CB  . PHE   A 1 294 ? 28.818  -0.720  15.688 1.00 55.32  ? 294 PHE   A CB  1 
ATOM   2222 C CG  . PHE   A 1 294 ? 29.038  0.686   16.179 1.00 62.10  ? 294 PHE   A CG  1 
ATOM   2223 C CD1 . PHE   A 1 294 ? 30.093  1.445   15.695 1.00 65.96  ? 294 PHE   A CD1 1 
ATOM   2224 C CD2 . PHE   A 1 294 ? 28.201  1.243   17.135 1.00 60.44  ? 294 PHE   A CD2 1 
ATOM   2225 C CE1 . PHE   A 1 294 ? 30.305  2.732   16.148 1.00 69.22  ? 294 PHE   A CE1 1 
ATOM   2226 C CE2 . PHE   A 1 294 ? 28.408  2.529   17.594 1.00 67.10  ? 294 PHE   A CE2 1 
ATOM   2227 C CZ  . PHE   A 1 294 ? 29.461  3.275   17.101 1.00 69.64  ? 294 PHE   A CZ  1 
ATOM   2228 N N   . ASP   A 1 295 ? 27.931  -2.377  18.219 1.00 48.26  ? 295 ASP   A N   1 
ATOM   2229 C CA  . ASP   A 1 295 ? 27.373  -2.356  19.570 1.00 39.78  ? 295 ASP   A CA  1 
ATOM   2230 C C   . ASP   A 1 295 ? 28.314  -3.007  20.576 1.00 47.82  ? 295 ASP   A C   1 
ATOM   2231 O O   . ASP   A 1 295 ? 28.400  -2.568  21.729 1.00 46.46  ? 295 ASP   A O   1 
ATOM   2232 C CB  . ASP   A 1 295 ? 26.012  -3.055  19.595 1.00 46.34  ? 295 ASP   A CB  1 
ATOM   2233 C CG  . ASP   A 1 295 ? 24.967  -2.334  18.765 1.00 54.83  ? 295 ASP   A CG  1 
ATOM   2234 O OD1 . ASP   A 1 295 ? 25.139  -1.123  18.504 1.00 49.45  ? 295 ASP   A OD1 1 
ATOM   2235 O OD2 . ASP   A 1 295 ? 23.971  -2.983  18.375 1.00 51.97  ? 295 ASP   A OD2 1 
ATOM   2236 N N   . VAL   A 1 296 ? 29.028  -4.055  20.161 1.00 44.72  ? 296 VAL   A N   1 
ATOM   2237 C CA  . VAL   A 1 296 ? 29.926  -4.750  21.080 1.00 43.76  ? 296 VAL   A CA  1 
ATOM   2238 C C   . VAL   A 1 296 ? 31.164  -3.909  21.366 1.00 45.90  ? 296 VAL   A C   1 
ATOM   2239 O O   . VAL   A 1 296 ? 31.597  -3.794  22.519 1.00 51.85  ? 296 VAL   A O   1 
ATOM   2240 C CB  . VAL   A 1 296 ? 30.300  -6.134  20.518 1.00 41.86  ? 296 VAL   A CB  1 
ATOM   2241 C CG1 . VAL   A 1 296 ? 31.385  -6.772  21.364 1.00 41.66  ? 296 VAL   A CG1 1 
ATOM   2242 C CG2 . VAL   A 1 296 ? 29.076  -7.033  20.454 1.00 36.02  ? 296 VAL   A CG2 1 
ATOM   2243 N N   . VAL   A 1 297 ? 31.751  -3.307  20.329 1.00 44.19  ? 297 VAL   A N   1 
ATOM   2244 C CA  . VAL   A 1 297 ? 32.938  -2.477  20.518 1.00 54.15  ? 297 VAL   A CA  1 
ATOM   2245 C C   . VAL   A 1 297 ? 32.612  -1.253  21.367 1.00 54.21  ? 297 VAL   A C   1 
ATOM   2246 O O   . VAL   A 1 297 ? 33.403  -0.852  22.231 1.00 54.66  ? 297 VAL   A O   1 
ATOM   2247 C CB  . VAL   A 1 297 ? 33.533  -2.076  19.155 1.00 49.21  ? 297 VAL   A CB  1 
ATOM   2248 C CG1 . VAL   A 1 297 ? 34.618  -1.023  19.344 1.00 47.07  ? 297 VAL   A CG1 1 
ATOM   2249 C CG2 . VAL   A 1 297 ? 34.088  -3.294  18.434 1.00 44.17  ? 297 VAL   A CG2 1 
ATOM   2250 N N   . ARG   A 1 298 ? 31.445  -0.637  21.133 1.00 49.91  ? 298 ARG   A N   1 
ATOM   2251 C CA  . ARG   A 1 298 ? 31.062  0.554   21.887 1.00 56.05  ? 298 ARG   A CA  1 
ATOM   2252 C C   . ARG   A 1 298 ? 30.864  0.242   23.364 1.00 54.38  ? 298 ARG   A C   1 
ATOM   2253 O O   . ARG   A 1 298 ? 31.114  1.103   24.215 1.00 61.19  ? 298 ARG   A O   1 
ATOM   2254 C CB  . ARG   A 1 298 ? 29.789  1.175   21.298 1.00 61.02  ? 298 ARG   A CB  1 
ATOM   2255 C CG  . ARG   A 1 298 ? 28.587  1.209   22.255 1.00 64.36  ? 298 ARG   A CG  1 
ATOM   2256 C CD  . ARG   A 1 298 ? 27.443  2.033   21.662 1.00 63.68  ? 298 ARG   A CD  1 
ATOM   2257 N NE  . ARG   A 1 298 ? 26.607  2.671   22.675 1.00 63.08  ? 298 ARG   A NE  1 
ATOM   2258 C CZ  . ARG   A 1 298 ? 25.336  2.365   22.907 1.00 62.18  ? 298 ARG   A CZ  1 
ATOM   2259 N NH1 . ARG   A 1 298 ? 24.736  1.370   22.274 1.00 62.81  ? 298 ARG   A NH1 1 
ATOM   2260 N NH2 . ARG   A 1 298 ? 24.646  3.082   23.791 1.00 49.02  ? 298 ARG   A NH2 1 
ATOM   2261 N N   . GLN   A 1 299 ? 30.460  -0.987  23.689 1.00 50.50  ? 299 GLN   A N   1 
ATOM   2262 C CA  . GLN   A 1 299 ? 30.172  -1.366  25.065 1.00 49.65  ? 299 GLN   A CA  1 
ATOM   2263 C C   . GLN   A 1 299 ? 31.311  -2.115  25.740 1.00 56.92  ? 299 GLN   A C   1 
ATOM   2264 O O   . GLN   A 1 299 ? 31.419  -2.075  26.970 1.00 61.12  ? 299 GLN   A O   1 
ATOM   2265 C CB  . GLN   A 1 299 ? 28.901  -2.226  25.125 1.00 47.24  ? 299 GLN   A CB  1 
ATOM   2266 C CG  . GLN   A 1 299 ? 28.359  -2.423  26.537 1.00 40.08  ? 299 GLN   A CG  1 
ATOM   2267 C CD  . GLN   A 1 299 ? 27.073  -3.226  26.588 1.00 43.63  ? 299 GLN   A CD  1 
ATOM   2268 O OE1 . GLN   A 1 299 ? 26.752  -3.828  27.611 1.00 42.78  ? 299 GLN   A OE1 1 
ATOM   2269 N NE2 . GLN   A 1 299 ? 26.324  -3.229  25.493 1.00 41.94  ? 299 GLN   A NE2 1 
ATOM   2270 N N   . CYS   A 1 300 ? 32.168  -2.794  24.980 1.00 57.55  ? 300 CYS   A N   1 
ATOM   2271 C CA  . CYS   A 1 300 ? 33.228  -3.601  25.565 1.00 57.85  ? 300 CYS   A CA  1 
ATOM   2272 C C   . CYS   A 1 300 ? 34.566  -2.878  25.626 1.00 58.75  ? 300 CYS   A C   1 
ATOM   2273 O O   . CYS   A 1 300 ? 35.572  -3.493  25.997 1.00 66.27  ? 300 CYS   A O   1 
ATOM   2274 C CB  . CYS   A 1 300 ? 33.371  -4.918  24.803 1.00 53.04  ? 300 CYS   A CB  1 
ATOM   2275 S SG  . CYS   A 1 300 ? 32.091  -6.113  25.226 1.00 67.57  ? 300 CYS   A SG  1 
ATOM   2276 N N   . SER   A 1 301 ? 34.600  -1.592  25.292 1.00 55.20  ? 301 SER   A N   1 
ATOM   2277 C CA  . SER   A 1 301 ? 35.830  -0.817  25.389 1.00 61.62  ? 301 SER   A CA  1 
ATOM   2278 C C   . SER   A 1 301 ? 35.523  0.676   25.465 1.00 59.08  ? 301 SER   A C   1 
ATOM   2279 O O   . SER   A 1 301 ? 34.511  1.138   24.936 1.00 55.64  ? 301 SER   A O   1 
ATOM   2280 C CB  . SER   A 1 301 ? 36.748  -1.105  24.201 1.00 70.98  ? 301 SER   A CB  1 
ATOM   2281 O OG  . SER   A 1 301 ? 38.035  -0.551  24.420 1.00 77.85  ? 301 SER   A OG  1 
ATOM   2282 N N   . SER   B 1 1   ? 1.593   -4.792  21.760 1.00 38.99  ? 1   SER   B N   1 
ATOM   2283 C CA  . SER   B 1 1   ? 2.058   -5.860  22.638 1.00 40.69  ? 1   SER   B CA  1 
ATOM   2284 C C   . SER   B 1 1   ? 3.578   -6.007  22.545 1.00 41.47  ? 1   SER   B C   1 
ATOM   2285 O O   . SER   B 1 1   ? 4.252   -5.161  21.961 1.00 43.02  ? 1   SER   B O   1 
ATOM   2286 C CB  . SER   B 1 1   ? 1.363   -7.182  22.297 1.00 49.33  ? 1   SER   B CB  1 
ATOM   2287 O OG  . SER   B 1 1   ? 1.680   -7.618  20.988 1.00 61.34  ? 1   SER   B OG  1 
ATOM   2288 N N   . GLY   B 1 2   ? 4.109   -7.073  23.121 1.00 43.83  ? 2   GLY   B N   1 
ATOM   2289 C CA  . GLY   B 1 2   ? 5.544   -7.238  23.238 1.00 43.66  ? 2   GLY   B CA  1 
ATOM   2290 C C   . GLY   B 1 2   ? 6.034   -6.849  24.621 1.00 44.45  ? 2   GLY   B C   1 
ATOM   2291 O O   . GLY   B 1 2   ? 5.419   -6.041  25.327 1.00 45.25  ? 2   GLY   B O   1 
ATOM   2292 N N   . PHE   B 1 3   ? 7.161   -7.433  25.024 1.00 41.52  ? 3   PHE   B N   1 
ATOM   2293 C CA  . PHE   B 1 3   ? 7.708   -7.180  26.352 1.00 36.89  ? 3   PHE   B CA  1 
ATOM   2294 C C   . PHE   B 1 3   ? 9.220   -7.083  26.263 1.00 40.00  ? 3   PHE   B C   1 
ATOM   2295 O O   . PHE   B 1 3   ? 9.888   -8.043  25.869 1.00 41.76  ? 3   PHE   B O   1 
ATOM   2296 C CB  . PHE   B 1 3   ? 7.293   -8.268  27.347 1.00 39.37  ? 3   PHE   B CB  1 
ATOM   2297 C CG  . PHE   B 1 3   ? 7.259   -7.795  28.773 1.00 42.65  ? 3   PHE   B CG  1 
ATOM   2298 C CD1 . PHE   B 1 3   ? 6.249   -6.950  29.211 1.00 44.39  ? 3   PHE   B CD1 1 
ATOM   2299 C CD2 . PHE   B 1 3   ? 8.236   -8.188  29.672 1.00 44.91  ? 3   PHE   B CD2 1 
ATOM   2300 C CE1 . PHE   B 1 3   ? 6.213   -6.508  30.521 1.00 43.36  ? 3   PHE   B CE1 1 
ATOM   2301 C CE2 . PHE   B 1 3   ? 8.202   -7.753  30.981 1.00 43.29  ? 3   PHE   B CE2 1 
ATOM   2302 C CZ  . PHE   B 1 3   ? 7.192   -6.908  31.405 1.00 45.97  ? 3   PHE   B CZ  1 
ATOM   2303 N N   . ARG   B 1 4   ? 9.752   -5.928  26.649 1.00 42.96  ? 4   ARG   B N   1 
ATOM   2304 C CA  . ARG   B 1 4   ? 11.169  -5.629  26.542 1.00 41.26  ? 4   ARG   B CA  1 
ATOM   2305 C C   . ARG   B 1 4   ? 11.666  -5.043  27.856 1.00 44.99  ? 4   ARG   B C   1 
ATOM   2306 O O   . ARG   B 1 4   ? 10.905  -4.423  28.604 1.00 44.60  ? 4   ARG   B O   1 
ATOM   2307 C CB  . ARG   B 1 4   ? 11.436  -4.639  25.399 1.00 39.57  ? 4   ARG   B CB  1 
ATOM   2308 C CG  . ARG   B 1 4   ? 10.948  -5.109  24.037 1.00 39.21  ? 4   ARG   B CG  1 
ATOM   2309 C CD  . ARG   B 1 4   ? 11.770  -6.286  23.552 1.00 50.45  ? 4   ARG   B CD  1 
ATOM   2310 N NE  . ARG   B 1 4   ? 13.186  -6.059  23.807 1.00 51.57  ? 4   ARG   B NE  1 
ATOM   2311 C CZ  . ARG   B 1 4   ? 13.959  -5.269  23.075 1.00 51.99  ? 4   ARG   B CZ  1 
ATOM   2312 N NH1 . ARG   B 1 4   ? 13.494  -4.651  22.002 1.00 51.86  ? 4   ARG   B NH1 1 
ATOM   2313 N NH2 . ARG   B 1 4   ? 15.227  -5.088  23.433 1.00 55.20  ? 4   ARG   B NH2 1 
ATOM   2314 N N   . LYS   B 1 5   ? 12.950  -5.252  28.135 1.00 43.31  ? 5   LYS   B N   1 
ATOM   2315 C CA  . LYS   B 1 5   ? 13.608  -4.532  29.220 1.00 51.10  ? 5   LYS   B CA  1 
ATOM   2316 C C   . LYS   B 1 5   ? 13.671  -3.059  28.844 1.00 44.93  ? 5   LYS   B C   1 
ATOM   2317 O O   . LYS   B 1 5   ? 14.391  -2.677  27.916 1.00 44.79  ? 5   LYS   B O   1 
ATOM   2318 C CB  . LYS   B 1 5   ? 15.001  -5.095  29.478 1.00 50.19  ? 5   LYS   B CB  1 
ATOM   2319 C CG  . LYS   B 1 5   ? 15.145  -5.785  30.820 1.00 47.52  ? 5   LYS   B CG  1 
ATOM   2320 C CD  . LYS   B 1 5   ? 16.420  -6.598  30.867 1.00 58.04  ? 5   LYS   B CD  1 
ATOM   2321 C CE  . LYS   B 1 5   ? 16.261  -7.815  31.757 1.00 61.98  ? 5   LYS   B CE  1 
ATOM   2322 N NZ  . LYS   B 1 5   ? 17.496  -8.640  31.734 1.00 67.34  ? 5   LYS   B NZ  1 
ATOM   2323 N N   . MET   B 1 6   ? 12.910  -2.234  29.555 1.00 39.31  ? 6   MET   B N   1 
ATOM   2324 C CA  . MET   B 1 6   ? 12.662  -0.853  29.166 1.00 45.61  ? 6   MET   B CA  1 
ATOM   2325 C C   . MET   B 1 6   ? 13.152  0.069   30.271 1.00 44.69  ? 6   MET   B C   1 
ATOM   2326 O O   . MET   B 1 6   ? 12.652  0.007   31.399 1.00 45.04  ? 6   MET   B O   1 
ATOM   2327 C CB  . MET   B 1 6   ? 11.171  -0.637  28.902 1.00 44.54  ? 6   MET   B CB  1 
ATOM   2328 C CG  . MET   B 1 6   ? 10.848  0.552   28.025 1.00 48.09  ? 6   MET   B CG  1 
ATOM   2329 S SD  . MET   B 1 6   ? 9.147   0.458   27.436 1.00 61.21  ? 6   MET   B SD  1 
ATOM   2330 C CE  . MET   B 1 6   ? 8.263   0.325   28.990 1.00 56.53  ? 6   MET   B CE  1 
ATOM   2331 N N   . ALA   B 1 7   ? 14.123  0.916   29.949 1.00 35.69  ? 7   ALA   B N   1 
ATOM   2332 C CA  . ALA   B 1 7   ? 14.614  1.901   30.897 1.00 37.63  ? 7   ALA   B CA  1 
ATOM   2333 C C   . ALA   B 1 7   ? 13.787  3.179   30.812 1.00 39.42  ? 7   ALA   B C   1 
ATOM   2334 O O   . ALA   B 1 7   ? 13.138  3.462   29.803 1.00 41.55  ? 7   ALA   B O   1 
ATOM   2335 C CB  . ALA   B 1 7   ? 16.088  2.213   30.638 1.00 37.16  ? 7   ALA   B CB  1 
ATOM   2336 N N   . PHE   B 1 8   ? 13.819  3.955   31.895 1.00 41.52  ? 8   PHE   B N   1 
ATOM   2337 C CA  . PHE   B 1 8   ? 13.181  5.262   31.890 1.00 40.85  ? 8   PHE   B CA  1 
ATOM   2338 C C   . PHE   B 1 8   ? 13.916  6.204   30.941 1.00 37.41  ? 8   PHE   B C   1 
ATOM   2339 O O   . PHE   B 1 8   ? 15.115  6.045   30.704 1.00 41.40  ? 8   PHE   B O   1 
ATOM   2340 C CB  . PHE   B 1 8   ? 13.179  5.867   33.289 1.00 38.96  ? 8   PHE   B CB  1 
ATOM   2341 C CG  . PHE   B 1 8   ? 12.230  5.210   34.226 1.00 38.25  ? 8   PHE   B CG  1 
ATOM   2342 C CD1 . PHE   B 1 8   ? 10.881  5.505   34.178 1.00 45.46  ? 8   PHE   B CD1 1 
ATOM   2343 C CD2 . PHE   B 1 8   ? 12.683  4.300   35.162 1.00 37.52  ? 8   PHE   B CD2 1 
ATOM   2344 C CE1 . PHE   B 1 8   ? 9.999   4.902   35.048 1.00 47.20  ? 8   PHE   B CE1 1 
ATOM   2345 C CE2 . PHE   B 1 8   ? 11.807  3.693   36.032 1.00 46.95  ? 8   PHE   B CE2 1 
ATOM   2346 C CZ  . PHE   B 1 8   ? 10.463  3.994   35.977 1.00 45.25  ? 8   PHE   B CZ  1 
ATOM   2347 N N   . PRO   B 1 9   ? 13.222  7.199   30.390 1.00 44.15  ? 9   PRO   B N   1 
ATOM   2348 C CA  . PRO   B 1 9   ? 13.925  8.240   29.632 1.00 39.81  ? 9   PRO   B CA  1 
ATOM   2349 C C   . PRO   B 1 9   ? 14.934  8.941   30.528 1.00 40.02  ? 9   PRO   B C   1 
ATOM   2350 O O   . PRO   B 1 9   ? 14.658  9.237   31.693 1.00 47.41  ? 9   PRO   B O   1 
ATOM   2351 C CB  . PRO   B 1 9   ? 12.800  9.182   29.189 1.00 48.30  ? 9   PRO   B CB  1 
ATOM   2352 C CG  . PRO   B 1 9   ? 11.555  8.359   29.278 1.00 51.96  ? 9   PRO   B CG  1 
ATOM   2353 C CD  . PRO   B 1 9   ? 11.771  7.436   30.432 1.00 40.59  ? 9   PRO   B CD  1 
ATOM   2354 N N   . SER   B 1 10  ? 16.117  9.195   29.977 1.00 42.62  ? 10  SER   B N   1 
ATOM   2355 C CA  . SER   B 1 10  ? 17.262  9.633   30.760 1.00 45.57  ? 10  SER   B CA  1 
ATOM   2356 C C   . SER   B 1 10  ? 17.519  11.131  30.665 1.00 44.05  ? 10  SER   B C   1 
ATOM   2357 O O   . SER   B 1 10  ? 18.510  11.610  31.224 1.00 43.02  ? 10  SER   B O   1 
ATOM   2358 C CB  . SER   B 1 10  ? 18.512  8.866   30.325 1.00 38.15  ? 10  SER   B CB  1 
ATOM   2359 O OG  . SER   B 1 10  ? 18.944  9.279   29.039 1.00 40.79  ? 10  SER   B OG  1 
ATOM   2360 N N   . GLY   B 1 11  ? 16.649  11.879  29.982 1.00 44.76  ? 11  GLY   B N   1 
ATOM   2361 C CA  . GLY   B 1 11  ? 16.935  13.283  29.720 1.00 42.55  ? 11  GLY   B CA  1 
ATOM   2362 C C   . GLY   B 1 11  ? 17.127  14.102  30.982 1.00 40.55  ? 11  GLY   B C   1 
ATOM   2363 O O   . GLY   B 1 11  ? 18.062  14.901  31.084 1.00 49.26  ? 11  GLY   B O   1 
ATOM   2364 N N   . LYS   B 1 12  ? 16.243  13.917  31.963 1.00 44.72  ? 12  LYS   B N   1 
ATOM   2365 C CA  . LYS   B 1 12  ? 16.349  14.683  33.202 1.00 49.44  ? 12  LYS   B CA  1 
ATOM   2366 C C   . LYS   B 1 12  ? 17.655  14.394  33.934 1.00 48.72  ? 12  LYS   B C   1 
ATOM   2367 O O   . LYS   B 1 12  ? 18.201  15.276  34.608 1.00 46.41  ? 12  LYS   B O   1 
ATOM   2368 C CB  . LYS   B 1 12  ? 15.153  14.381  34.105 1.00 50.41  ? 12  LYS   B CB  1 
ATOM   2369 C CG  . LYS   B 1 12  ? 13.812  14.525  33.396 1.00 60.98  ? 12  LYS   B CG  1 
ATOM   2370 C CD  . LYS   B 1 12  ? 12.645  14.179  34.306 1.00 53.28  ? 12  LYS   B CD  1 
ATOM   2371 C CE  . LYS   B 1 12  ? 12.384  15.277  35.321 1.00 58.19  ? 12  LYS   B CE  1 
ATOM   2372 N NZ  . LYS   B 1 12  ? 11.130  15.022  36.086 1.00 74.66  ? 12  LYS   B NZ  1 
ATOM   2373 N N   . VAL   B 1 13  ? 18.181  13.176  33.799 1.00 44.24  ? 13  VAL   B N   1 
ATOM   2374 C CA  . VAL   B 1 13  ? 19.399  12.812  34.515 1.00 45.04  ? 13  VAL   B CA  1 
ATOM   2375 C C   . VAL   B 1 13  ? 20.639  13.274  33.760 1.00 43.02  ? 13  VAL   B C   1 
ATOM   2376 O O   . VAL   B 1 13  ? 21.640  13.650  34.383 1.00 42.43  ? 13  VAL   B O   1 
ATOM   2377 C CB  . VAL   B 1 13  ? 19.421  11.296  34.771 1.00 40.99  ? 13  VAL   B CB  1 
ATOM   2378 C CG1 . VAL   B 1 13  ? 20.667  10.896  35.544 1.00 40.42  ? 13  VAL   B CG1 1 
ATOM   2379 C CG2 . VAL   B 1 13  ? 18.166  10.876  35.516 1.00 40.40  ? 13  VAL   B CG2 1 
ATOM   2380 N N   . GLU   B 1 14  ? 20.590  13.268  32.422 1.00 42.32  ? 14  GLU   B N   1 
ATOM   2381 C CA  . GLU   B 1 14  ? 21.728  13.717  31.622 1.00 40.95  ? 14  GLU   B CA  1 
ATOM   2382 C C   . GLU   B 1 14  ? 22.162  15.127  32.010 1.00 41.31  ? 14  GLU   B C   1 
ATOM   2383 O O   . GLU   B 1 14  ? 23.362  15.409  32.116 1.00 41.75  ? 14  GLU   B O   1 
ATOM   2384 C CB  . GLU   B 1 14  ? 21.382  13.661  30.129 1.00 40.30  ? 14  GLU   B CB  1 
ATOM   2385 C CG  . GLU   B 1 14  ? 21.083  12.260  29.593 1.00 45.40  ? 14  GLU   B CG  1 
ATOM   2386 C CD  . GLU   B 1 14  ? 20.606  12.265  28.145 1.00 49.66  ? 14  GLU   B CD  1 
ATOM   2387 O OE1 . GLU   B 1 14  ? 21.208  12.984  27.319 1.00 50.84  ? 14  GLU   B OE1 1 
ATOM   2388 O OE2 . GLU   B 1 14  ? 19.625  11.553  27.836 1.00 44.14  ? 14  GLU   B OE2 1 
ATOM   2389 N N   . GLY   B 1 15  ? 21.203  16.023  32.239 1.00 41.99  ? 15  GLY   B N   1 
ATOM   2390 C CA  . GLY   B 1 15  ? 21.526  17.387  32.611 1.00 47.28  ? 15  GLY   B CA  1 
ATOM   2391 C C   . GLY   B 1 15  ? 22.155  17.552  33.979 1.00 48.83  ? 15  GLY   B C   1 
ATOM   2392 O O   . GLY   B 1 15  ? 22.466  18.683  34.365 1.00 49.25  ? 15  GLY   B O   1 
ATOM   2393 N N   . CYS   B 1 16  ? 22.351  16.460  34.721 1.00 45.52  ? 16  CYS   B N   1 
ATOM   2394 C CA  . CYS   B 1 16  ? 22.968  16.504  36.038 1.00 43.70  ? 16  CYS   B CA  1 
ATOM   2395 C C   . CYS   B 1 16  ? 24.332  15.835  36.095 1.00 41.11  ? 16  CYS   B C   1 
ATOM   2396 O O   . CYS   B 1 16  ? 24.959  15.839  37.162 1.00 43.50  ? 16  CYS   B O   1 
ATOM   2397 C CB  . CYS   B 1 16  ? 22.055  15.839  37.077 1.00 42.20  ? 16  CYS   B CB  1 
ATOM   2398 S SG  . CYS   B 1 16  ? 20.393  16.525  37.159 1.00 51.98  ? 16  CYS   B SG  1 
ATOM   2399 N N   . MET   B 1 17  ? 24.801  15.249  35.000 1.00 36.11  ? 17  MET   B N   1 
ATOM   2400 C CA  . MET   B 1 17  ? 26.078  14.553  35.017 1.00 41.57  ? 17  MET   B CA  1 
ATOM   2401 C C   . MET   B 1 17  ? 27.206  15.530  34.722 1.00 39.85  ? 17  MET   B C   1 
ATOM   2402 O O   . MET   B 1 17  ? 27.153  16.275  33.740 1.00 44.27  ? 17  MET   B O   1 
ATOM   2403 C CB  . MET   B 1 17  ? 26.081  13.407  34.008 1.00 39.83  ? 17  MET   B CB  1 
ATOM   2404 C CG  . MET   B 1 17  ? 25.048  12.331  34.308 1.00 37.06  ? 17  MET   B CG  1 
ATOM   2405 S SD  . MET   B 1 17  ? 25.032  11.796  36.029 1.00 46.56  ? 17  MET   B SD  1 
ATOM   2406 C CE  . MET   B 1 17  ? 26.691  11.144  36.218 1.00 33.97  ? 17  MET   B CE  1 
ATOM   2407 N N   . VAL   B 1 18  ? 28.218  15.535  35.587 1.00 38.26  ? 18  VAL   B N   1 
ATOM   2408 C CA  . VAL   B 1 18  ? 29.370  16.411  35.454 1.00 37.35  ? 18  VAL   B CA  1 
ATOM   2409 C C   . VAL   B 1 18  ? 30.634  15.579  35.578 1.00 34.82  ? 18  VAL   B C   1 
ATOM   2410 O O   . VAL   B 1 18  ? 30.617  14.430  36.021 1.00 36.35  ? 18  VAL   B O   1 
ATOM   2411 C CB  . VAL   B 1 18  ? 29.383  17.540  36.505 1.00 44.49  ? 18  VAL   B CB  1 
ATOM   2412 C CG1 . VAL   B 1 18  ? 28.152  18.412  36.368 1.00 42.65  ? 18  VAL   B CG1 1 
ATOM   2413 C CG2 . VAL   B 1 18  ? 29.500  16.950  37.903 1.00 38.63  ? 18  VAL   B CG2 1 
ATOM   2414 N N   . GLN   B 1 19  ? 31.744  16.195  35.197 1.00 40.01  ? 19  GLN   B N   1 
ATOM   2415 C CA  . GLN   B 1 19  ? 33.057  15.578  35.285 1.00 46.60  ? 19  GLN   B CA  1 
ATOM   2416 C C   . GLN   B 1 19  ? 33.774  16.097  36.523 1.00 42.23  ? 19  GLN   B C   1 
ATOM   2417 O O   . GLN   B 1 19  ? 33.882  17.311  36.719 1.00 41.57  ? 19  GLN   B O   1 
ATOM   2418 C CB  . GLN   B 1 19  ? 33.872  15.883  34.032 1.00 39.96  ? 19  GLN   B CB  1 
ATOM   2419 C CG  . GLN   B 1 19  ? 35.301  15.424  34.115 1.00 47.54  ? 19  GLN   B CG  1 
ATOM   2420 C CD  . GLN   B 1 19  ? 36.136  15.965  32.980 1.00 56.42  ? 19  GLN   B CD  1 
ATOM   2421 O OE1 . GLN   B 1 19  ? 36.378  15.277  31.987 1.00 57.16  ? 19  GLN   B OE1 1 
ATOM   2422 N NE2 . GLN   B 1 19  ? 36.579  17.210  33.115 1.00 54.09  ? 19  GLN   B NE2 1 
ATOM   2423 N N   . VAL   B 1 20  ? 34.250  15.180  37.359 1.00 40.06  ? 20  VAL   B N   1 
ATOM   2424 C CA  . VAL   B 1 20  ? 35.002  15.523  38.560 1.00 41.50  ? 20  VAL   B CA  1 
ATOM   2425 C C   . VAL   B 1 20  ? 36.426  15.025  38.383 1.00 41.63  ? 20  VAL   B C   1 
ATOM   2426 O O   . VAL   B 1 20  ? 36.644  13.871  37.994 1.00 40.71  ? 20  VAL   B O   1 
ATOM   2427 C CB  . VAL   B 1 20  ? 34.363  14.928  39.827 1.00 44.82  ? 20  VAL   B CB  1 
ATOM   2428 C CG1 . VAL   B 1 20  ? 35.238  15.212  41.042 1.00 44.64  ? 20  VAL   B CG1 1 
ATOM   2429 C CG2 . VAL   B 1 20  ? 32.970  15.497  40.030 1.00 39.91  ? 20  VAL   B CG2 1 
ATOM   2430 N N   . THR   B 1 21  ? 37.390  15.897  38.658 1.00 42.83  ? 21  THR   B N   1 
ATOM   2431 C CA  . THR   B 1 21  ? 38.803  15.571  38.550 1.00 47.47  ? 21  THR   B CA  1 
ATOM   2432 C C   . THR   B 1 21  ? 39.487  15.884  39.871 1.00 43.08  ? 21  THR   B C   1 
ATOM   2433 O O   . THR   B 1 21  ? 39.331  16.983  40.412 1.00 48.07  ? 21  THR   B O   1 
ATOM   2434 C CB  . THR   B 1 21  ? 39.470  16.356  37.419 1.00 41.94  ? 21  THR   B CB  1 
ATOM   2435 O OG1 . THR   B 1 21  ? 38.745  16.147  36.202 1.00 47.92  ? 21  THR   B OG1 1 
ATOM   2436 C CG2 . THR   B 1 21  ? 40.905  15.893  37.236 1.00 49.13  ? 21  THR   B CG2 1 
ATOM   2437 N N   . CYS   B 1 22  ? 40.235  14.914  40.385 1.00 51.44  ? 22  CYS   B N   1 
ATOM   2438 C CA  . CYS   B 1 22  ? 41.059  15.098  41.576 1.00 50.45  ? 22  CYS   B CA  1 
ATOM   2439 C C   . CYS   B 1 22  ? 42.439  14.547  41.246 1.00 51.45  ? 22  CYS   B C   1 
ATOM   2440 O O   . CYS   B 1 22  ? 42.626  13.328  41.178 1.00 53.22  ? 22  CYS   B O   1 
ATOM   2441 C CB  . CYS   B 1 22  ? 40.454  14.405  42.790 1.00 53.69  ? 22  CYS   B CB  1 
ATOM   2442 S SG  . CYS   B 1 22  ? 41.333  14.764  44.321 1.00 53.34  ? 22  CYS   B SG  1 
ATOM   2443 N N   . GLY   B 1 23  ? 43.396  15.445  41.033 1.00 54.78  ? 23  GLY   B N   1 
ATOM   2444 C CA  . GLY   B 1 23  ? 44.706  15.038  40.570 1.00 59.04  ? 23  GLY   B CA  1 
ATOM   2445 C C   . GLY   B 1 23  ? 44.652  14.469  39.168 1.00 52.26  ? 23  GLY   B C   1 
ATOM   2446 O O   . GLY   B 1 23  ? 44.249  15.161  38.228 1.00 53.81  ? 23  GLY   B O   1 
ATOM   2447 N N   . THR   B 1 24  ? 45.043  13.206  39.015 1.00 52.48  ? 24  THR   B N   1 
ATOM   2448 C CA  . THR   B 1 24  ? 45.017  12.528  37.727 1.00 56.82  ? 24  THR   B CA  1 
ATOM   2449 C C   . THR   B 1 24  ? 43.774  11.669  37.526 1.00 60.75  ? 24  THR   B C   1 
ATOM   2450 O O   . THR   B 1 24  ? 43.620  11.073  36.455 1.00 57.81  ? 24  THR   B O   1 
ATOM   2451 C CB  . THR   B 1 24  ? 46.266  11.653  37.563 1.00 64.57  ? 24  THR   B CB  1 
ATOM   2452 O OG1 . THR   B 1 24  ? 46.323  10.701  38.633 1.00 65.88  ? 24  THR   B OG1 1 
ATOM   2453 C CG2 . THR   B 1 24  ? 47.530  12.505  37.575 1.00 65.11  ? 24  THR   B CG2 1 
ATOM   2454 N N   . THR   B 1 25  ? 42.893  11.583  38.524 1.00 46.24  ? 25  THR   B N   1 
ATOM   2455 C CA  . THR   B 1 25  ? 41.684  10.772  38.426 1.00 56.93  ? 25  THR   B CA  1 
ATOM   2456 C C   . THR   B 1 25  ? 40.518  11.628  37.950 1.00 52.59  ? 25  THR   B C   1 
ATOM   2457 O O   . THR   B 1 25  ? 40.294  12.729  38.466 1.00 46.05  ? 25  THR   B O   1 
ATOM   2458 C CB  . THR   B 1 25  ? 41.328  10.130  39.771 1.00 47.59  ? 25  THR   B CB  1 
ATOM   2459 O OG1 . THR   B 1 25  ? 42.425  9.336   40.236 1.00 55.70  ? 25  THR   B OG1 1 
ATOM   2460 C CG2 . THR   B 1 25  ? 40.097  9.235   39.626 1.00 45.12  ? 25  THR   B CG2 1 
ATOM   2461 N N   . THR   B 1 26  ? 39.775  11.112  36.973 1.00 42.87  ? 26  THR   B N   1 
ATOM   2462 C CA  . THR   B 1 26  ? 38.544  11.736  36.508 1.00 42.89  ? 26  THR   B CA  1 
ATOM   2463 C C   . THR   B 1 26  ? 37.425  10.703  36.546 1.00 43.48  ? 26  THR   B C   1 
ATOM   2464 O O   . THR   B 1 26  ? 37.565  9.613   35.983 1.00 41.86  ? 26  THR   B O   1 
ATOM   2465 C CB  . THR   B 1 26  ? 38.718  12.306  35.097 1.00 46.09  ? 26  THR   B CB  1 
ATOM   2466 O OG1 . THR   B 1 26  ? 39.468  13.526  35.169 1.00 46.16  ? 26  THR   B OG1 1 
ATOM   2467 C CG2 . THR   B 1 26  ? 37.371  12.577  34.460 1.00 47.16  ? 26  THR   B CG2 1 
ATOM   2468 N N   . LEU   B 1 27  ? 36.329  11.037  37.224 1.00 42.55  ? 27  LEU   B N   1 
ATOM   2469 C CA  . LEU   B 1 27  ? 35.143  10.187  37.252 1.00 35.80  ? 27  LEU   B CA  1 
ATOM   2470 C C   . LEU   B 1 27  ? 33.914  11.085  37.135 1.00 35.83  ? 27  LEU   B C   1 
ATOM   2471 O O   . LEU   B 1 27  ? 34.024  12.299  36.934 1.00 37.51  ? 27  LEU   B O   1 
ATOM   2472 C CB  . LEU   B 1 27  ? 35.127  9.301   38.508 1.00 34.56  ? 27  LEU   B CB  1 
ATOM   2473 C CG  . LEU   B 1 27  ? 35.390  9.906   39.893 1.00 40.10  ? 27  LEU   B CG  1 
ATOM   2474 C CD1 . LEU   B 1 27  ? 34.244  10.790  40.357 1.00 33.21  ? 27  LEU   B CD1 1 
ATOM   2475 C CD2 . LEU   B 1 27  ? 35.657  8.805   40.907 1.00 34.94  ? 27  LEU   B CD2 1 
ATOM   2476 N N   . ASN   B 1 28  ? 32.734  10.489  37.274 1.00 33.94  ? 28  ASN   B N   1 
ATOM   2477 C CA  . ASN   B 1 28  ? 31.484  11.204  37.079 1.00 32.08  ? 28  ASN   B CA  1 
ATOM   2478 C C   . ASN   B 1 28  ? 30.927  11.707  38.405 1.00 35.78  ? 28  ASN   B C   1 
ATOM   2479 O O   . ASN   B 1 28  ? 31.100  11.083  39.456 1.00 35.44  ? 28  ASN   B O   1 
ATOM   2480 C CB  . ASN   B 1 28  ? 30.449  10.315  36.387 1.00 36.15  ? 28  ASN   B CB  1 
ATOM   2481 C CG  . ASN   B 1 28  ? 30.969  9.716   35.096 1.00 32.96  ? 28  ASN   B CG  1 
ATOM   2482 O OD1 . ASN   B 1 28  ? 31.082  10.401  34.080 1.00 38.36  ? 28  ASN   B OD1 1 
ATOM   2483 N ND2 . ASN   B 1 28  ? 31.285  8.428   35.126 1.00 33.11  ? 28  ASN   B ND2 1 
ATOM   2484 N N   . GLY   B 1 29  ? 30.257  12.856  38.338 1.00 33.25  ? 29  GLY   B N   1 
ATOM   2485 C CA  . GLY   B 1 29  ? 29.591  13.414  39.490 1.00 36.38  ? 29  GLY   B CA  1 
ATOM   2486 C C   . GLY   B 1 29  ? 28.150  13.749  39.162 1.00 34.70  ? 29  GLY   B C   1 
ATOM   2487 O O   . GLY   B 1 29  ? 27.759  13.855  38.000 1.00 32.13  ? 29  GLY   B O   1 
ATOM   2488 N N   . LEU   B 1 30  ? 27.357  13.906  40.217 1.00 38.61  ? 30  LEU   B N   1 
ATOM   2489 C CA  . LEU   B 1 30  ? 25.942  14.238  40.101 1.00 41.88  ? 30  LEU   B CA  1 
ATOM   2490 C C   . LEU   B 1 30  ? 25.751  15.657  40.625 1.00 40.06  ? 30  LEU   B C   1 
ATOM   2491 O O   . LEU   B 1 30  ? 25.982  15.920  41.809 1.00 42.64  ? 30  LEU   B O   1 
ATOM   2492 C CB  . LEU   B 1 30  ? 25.085  13.236  40.874 1.00 34.00  ? 30  LEU   B CB  1 
ATOM   2493 C CG  . LEU   B 1 30  ? 23.572  13.385  40.718 1.00 43.91  ? 30  LEU   B CG  1 
ATOM   2494 C CD1 . LEU   B 1 30  ? 23.144  13.054  39.293 1.00 34.50  ? 30  LEU   B CD1 1 
ATOM   2495 C CD2 . LEU   B 1 30  ? 22.838  12.511  41.718 1.00 35.84  ? 30  LEU   B CD2 1 
ATOM   2496 N N   . TRP   B 1 31  ? 25.326  16.564  39.747 1.00 43.23  ? 31  TRP   B N   1 
ATOM   2497 C CA  . TRP   B 1 31  ? 25.222  17.990  40.059 1.00 39.27  ? 31  TRP   B CA  1 
ATOM   2498 C C   . TRP   B 1 31  ? 23.755  18.336  40.283 1.00 41.66  ? 31  TRP   B C   1 
ATOM   2499 O O   . TRP   B 1 31  ? 22.988  18.489  39.330 1.00 44.12  ? 31  TRP   B O   1 
ATOM   2500 C CB  . TRP   B 1 31  ? 25.825  18.828  38.936 1.00 43.71  ? 31  TRP   B CB  1 
ATOM   2501 C CG  . TRP   B 1 31  ? 25.846  20.318  39.184 1.00 46.06  ? 31  TRP   B CG  1 
ATOM   2502 C CD1 . TRP   B 1 31  ? 25.786  20.955  40.392 1.00 50.14  ? 31  TRP   B CD1 1 
ATOM   2503 C CD2 . TRP   B 1 31  ? 25.930  21.352  38.191 1.00 44.05  ? 31  TRP   B CD2 1 
ATOM   2504 N NE1 . TRP   B 1 31  ? 25.830  22.320  40.212 1.00 47.02  ? 31  TRP   B NE1 1 
ATOM   2505 C CE2 . TRP   B 1 31  ? 25.918  22.589  38.871 1.00 45.95  ? 31  TRP   B CE2 1 
ATOM   2506 C CE3 . TRP   B 1 31  ? 26.013  21.351  36.795 1.00 44.72  ? 31  TRP   B CE3 1 
ATOM   2507 C CZ2 . TRP   B 1 31  ? 25.985  23.810  38.201 1.00 49.42  ? 31  TRP   B CZ2 1 
ATOM   2508 C CZ3 . TRP   B 1 31  ? 26.082  22.566  36.132 1.00 50.41  ? 31  TRP   B CZ3 1 
ATOM   2509 C CH2 . TRP   B 1 31  ? 26.068  23.778  36.835 1.00 49.71  ? 31  TRP   B CH2 1 
ATOM   2510 N N   . LEU   B 1 32  ? 23.367  18.464  41.550 1.00 41.61  ? 32  LEU   B N   1 
ATOM   2511 C CA  . LEU   B 1 32  ? 22.012  18.835  41.935 1.00 43.45  ? 32  LEU   B CA  1 
ATOM   2512 C C   . LEU   B 1 32  ? 22.090  20.076  42.813 1.00 49.32  ? 32  LEU   B C   1 
ATOM   2513 O O   . LEU   B 1 32  ? 22.723  20.047  43.875 1.00 43.93  ? 32  LEU   B O   1 
ATOM   2514 C CB  . LEU   B 1 32  ? 21.314  17.689  42.670 1.00 46.48  ? 32  LEU   B CB  1 
ATOM   2515 C CG  . LEU   B 1 32  ? 21.145  16.369  41.910 1.00 45.96  ? 32  LEU   B CG  1 
ATOM   2516 C CD1 . LEU   B 1 32  ? 20.662  15.278  42.847 1.00 42.41  ? 32  LEU   B CD1 1 
ATOM   2517 C CD2 . LEU   B 1 32  ? 20.187  16.530  40.735 1.00 50.40  ? 32  LEU   B CD2 1 
ATOM   2518 N N   . ASP   B 1 33  ? 21.450  21.155  42.367 1.00 51.22  ? 33  ASP   B N   1 
ATOM   2519 C CA  . ASP   B 1 33  ? 21.517  22.469  43.026 1.00 48.98  ? 33  ASP   B CA  1 
ATOM   2520 C C   . ASP   B 1 33  ? 22.990  22.877  43.064 1.00 51.57  ? 33  ASP   B C   1 
ATOM   2521 O O   . ASP   B 1 33  ? 23.653  22.829  42.017 1.00 47.33  ? 33  ASP   B O   1 
ATOM   2522 C CB  . ASP   B 1 33  ? 20.804  22.395  44.370 1.00 49.20  ? 33  ASP   B CB  1 
ATOM   2523 C CG  . ASP   B 1 33  ? 19.318  22.111  44.218 1.00 55.10  ? 33  ASP   B CG  1 
ATOM   2524 O OD1 . ASP   B 1 33  ? 18.697  22.717  43.312 1.00 57.58  ? 33  ASP   B OD1 1 
ATOM   2525 O OD2 . ASP   B 1 33  ? 18.779  21.284  44.989 1.00 51.90  ? 33  ASP   B OD2 1 
ATOM   2526 N N   . ASP   B 1 34  ? 23.543  23.259  44.217 1.00 47.41  ? 34  ASP   B N   1 
ATOM   2527 C CA  . ASP   B 1 34  ? 24.935  23.689  44.301 1.00 53.63  ? 34  ASP   B CA  1 
ATOM   2528 C C   . ASP   B 1 34  ? 25.825  22.648  44.976 1.00 51.94  ? 34  ASP   B C   1 
ATOM   2529 O O   . ASP   B 1 34  ? 26.790  22.999  45.658 1.00 55.16  ? 34  ASP   B O   1 
ATOM   2530 C CB  . ASP   B 1 34  ? 25.038  25.027  45.032 1.00 52.06  ? 34  ASP   B CB  1 
ATOM   2531 C CG  . ASP   B 1 34  ? 24.557  24.947  46.470 1.00 57.69  ? 34  ASP   B CG  1 
ATOM   2532 O OD1 . ASP   B 1 34  ? 23.787  24.017  46.793 1.00 59.75  ? 34  ASP   B OD1 1 
ATOM   2533 O OD2 . ASP   B 1 34  ? 24.943  25.819  47.278 1.00 61.03  ? 34  ASP   B OD2 1 
ATOM   2534 N N   . VAL   B 1 35  ? 25.514  21.366  44.802 1.00 45.52  ? 35  VAL   B N   1 
ATOM   2535 C CA  . VAL   B 1 35  ? 26.314  20.279  45.356 1.00 44.33  ? 35  VAL   B CA  1 
ATOM   2536 C C   . VAL   B 1 35  ? 26.582  19.260  44.256 1.00 40.84  ? 35  VAL   B C   1 
ATOM   2537 O O   . VAL   B 1 35  ? 25.680  18.912  43.487 1.00 42.83  ? 35  VAL   B O   1 
ATOM   2538 C CB  . VAL   B 1 35  ? 25.616  19.609  46.560 1.00 45.44  ? 35  VAL   B CB  1 
ATOM   2539 C CG1 . VAL   B 1 35  ? 26.467  18.468  47.108 1.00 41.04  ? 35  VAL   B CG1 1 
ATOM   2540 C CG2 . VAL   B 1 35  ? 25.327  20.630  47.658 1.00 43.92  ? 35  VAL   B CG2 1 
ATOM   2541 N N   . VAL   B 1 36  ? 27.823  18.788  44.177 1.00 40.34  ? 36  VAL   B N   1 
ATOM   2542 C CA  . VAL   B 1 36  ? 28.212  17.730  43.248 1.00 39.72  ? 36  VAL   B CA  1 
ATOM   2543 C C   . VAL   B 1 36  ? 28.544  16.484  44.060 1.00 46.16  ? 36  VAL   B C   1 
ATOM   2544 O O   . VAL   B 1 36  ? 29.393  16.527  44.959 1.00 43.35  ? 36  VAL   B O   1 
ATOM   2545 C CB  . VAL   B 1 36  ? 29.398  18.148  42.369 1.00 40.28  ? 36  VAL   B CB  1 
ATOM   2546 C CG1 . VAL   B 1 36  ? 29.916  16.952  41.580 1.00 35.67  ? 36  VAL   B CG1 1 
ATOM   2547 C CG2 . VAL   B 1 36  ? 28.993  19.271  41.427 1.00 37.65  ? 36  VAL   B CG2 1 
ATOM   2548 N N   . TYR   B 1 37  ? 27.877  15.376  43.738 1.00 39.83  ? 37  TYR   B N   1 
ATOM   2549 C CA  . TYR   B 1 37  ? 28.038  14.108  44.441 1.00 41.80  ? 37  TYR   B CA  1 
ATOM   2550 C C   . TYR   B 1 37  ? 28.862  13.149  43.593 1.00 37.89  ? 37  TYR   B C   1 
ATOM   2551 O O   . TYR   B 1 37  ? 28.606  12.999  42.395 1.00 40.95  ? 37  TYR   B O   1 
ATOM   2552 C CB  . TYR   B 1 37  ? 26.678  13.479  44.753 1.00 32.92  ? 37  TYR   B CB  1 
ATOM   2553 C CG  . TYR   B 1 37  ? 25.734  14.378  45.517 1.00 36.38  ? 37  TYR   B CG  1 
ATOM   2554 C CD1 . TYR   B 1 37  ? 24.984  15.344  44.860 1.00 39.54  ? 37  TYR   B CD1 1 
ATOM   2555 C CD2 . TYR   B 1 37  ? 25.583  14.256  46.891 1.00 41.25  ? 37  TYR   B CD2 1 
ATOM   2556 C CE1 . TYR   B 1 37  ? 24.120  16.169  45.545 1.00 42.52  ? 37  TYR   B CE1 1 
ATOM   2557 C CE2 . TYR   B 1 37  ? 24.715  15.078  47.590 1.00 45.43  ? 37  TYR   B CE2 1 
ATOM   2558 C CZ  . TYR   B 1 37  ? 23.986  16.032  46.909 1.00 47.37  ? 37  TYR   B CZ  1 
ATOM   2559 O OH  . TYR   B 1 37  ? 23.122  16.856  47.594 1.00 46.93  ? 37  TYR   B OH  1 
ATOM   2560 N N   . CYS   B 1 38  ? 29.834  12.489  44.218 1.00 36.85  ? 38  CYS   B N   1 
ATOM   2561 C CA  . CYS   B 1 38  ? 30.697  11.540  43.527 1.00 35.31  ? 38  CYS   B CA  1 
ATOM   2562 C C   . CYS   B 1 38  ? 31.280  10.585  44.560 1.00 34.04  ? 38  CYS   B C   1 
ATOM   2563 O O   . CYS   B 1 38  ? 31.225  10.864  45.764 1.00 38.52  ? 38  CYS   B O   1 
ATOM   2564 C CB  . CYS   B 1 38  ? 31.816  12.264  42.760 1.00 41.09  ? 38  CYS   B CB  1 
ATOM   2565 S SG  . CYS   B 1 38  ? 33.153  12.884  43.802 1.00 42.80  ? 38  CYS   B SG  1 
ATOM   2566 N N   . PRO   B 1 39  ? 31.832  9.449   44.129 1.00 32.03  ? 39  PRO   B N   1 
ATOM   2567 C CA  . PRO   B 1 39  ? 32.421  8.513   45.097 1.00 33.88  ? 39  PRO   B CA  1 
ATOM   2568 C C   . PRO   B 1 39  ? 33.647  9.114   45.763 1.00 36.30  ? 39  PRO   B C   1 
ATOM   2569 O O   . PRO   B 1 39  ? 34.422  9.842   45.137 1.00 33.56  ? 39  PRO   B O   1 
ATOM   2570 C CB  . PRO   B 1 39  ? 32.795  7.294   44.242 1.00 31.75  ? 39  PRO   B CB  1 
ATOM   2571 C CG  . PRO   B 1 39  ? 31.975  7.420   43.002 1.00 31.07  ? 39  PRO   B CG  1 
ATOM   2572 C CD  . PRO   B 1 39  ? 31.840  8.893   42.763 1.00 33.84  ? 39  PRO   B CD  1 
ATOM   2573 N N   . ARG   B 1 40  ? 33.821  8.800   47.049 1.00 35.26  ? 40  ARG   B N   1 
ATOM   2574 C CA  . ARG   B 1 40  ? 34.956  9.344   47.783 1.00 34.69  ? 40  ARG   B CA  1 
ATOM   2575 C C   . ARG   B 1 40  ? 36.279  8.725   47.355 1.00 36.07  ? 40  ARG   B C   1 
ATOM   2576 O O   . ARG   B 1 40  ? 37.330  9.336   47.582 1.00 34.14  ? 40  ARG   B O   1 
ATOM   2577 C CB  . ARG   B 1 40  ? 34.764  9.159   49.291 1.00 37.57  ? 40  ARG   B CB  1 
ATOM   2578 C CG  . ARG   B 1 40  ? 34.858  7.729   49.782 1.00 33.51  ? 40  ARG   B CG  1 
ATOM   2579 C CD  . ARG   B 1 40  ? 34.747  7.691   51.301 1.00 40.20  ? 40  ARG   B CD  1 
ATOM   2580 N NE  . ARG   B 1 40  ? 34.746  6.333   51.832 1.00 31.60  ? 40  ARG   B NE  1 
ATOM   2581 C CZ  . ARG   B 1 40  ? 34.718  6.038   53.124 1.00 37.73  ? 40  ARG   B CZ  1 
ATOM   2582 N NH1 . ARG   B 1 40  ? 34.669  6.983   54.048 1.00 36.19  ? 40  ARG   B NH1 1 
ATOM   2583 N NH2 . ARG   B 1 40  ? 34.743  4.763   53.498 1.00 35.95  ? 40  ARG   B NH2 1 
ATOM   2584 N N   . HIS   B 1 41  ? 36.259  7.540   46.717 1.00 36.39  ? 41  HIS   B N   1 
ATOM   2585 C CA  . HIS   B 1 41  ? 37.551  6.992   46.303 1.00 38.74  ? 41  HIS   B CA  1 
ATOM   2586 C C   . HIS   B 1 41  ? 38.187  7.782   45.157 1.00 38.93  ? 41  HIS   B C   1 
ATOM   2587 O O   . HIS   B 1 41  ? 39.215  7.354   44.630 1.00 38.07  ? 41  HIS   B O   1 
ATOM   2588 C CB  . HIS   B 1 41  ? 37.440  5.499   45.949 1.00 38.53  ? 41  HIS   B CB  1 
ATOM   2589 C CG  . HIS   B 1 41  ? 36.633  5.188   44.720 1.00 45.19  ? 41  HIS   B CG  1 
ATOM   2590 N ND1 . HIS   B 1 41  ? 36.911  5.718   43.478 1.00 43.45  ? 41  HIS   B ND1 1 
ATOM   2591 C CD2 . HIS   B 1 41  ? 35.590  4.341   44.539 1.00 40.05  ? 41  HIS   B CD2 1 
ATOM   2592 C CE1 . HIS   B 1 41  ? 36.055  5.238   42.592 1.00 35.82  ? 41  HIS   B CE1 1 
ATOM   2593 N NE2 . HIS   B 1 41  ? 35.244  4.399   43.210 1.00 40.47  ? 41  HIS   B NE2 1 
ATOM   2594 N N   . VAL   B 1 42  ? 37.617  8.930   44.783 1.00 40.28  ? 42  VAL   B N   1 
ATOM   2595 C CA  . VAL   B 1 42  ? 38.267  9.792   43.802 1.00 47.48  ? 42  VAL   B CA  1 
ATOM   2596 C C   . VAL   B 1 42  ? 39.572  10.356  44.360 1.00 45.89  ? 42  VAL   B C   1 
ATOM   2597 O O   . VAL   B 1 42  ? 40.507  10.644  43.599 1.00 40.90  ? 42  VAL   B O   1 
ATOM   2598 C CB  . VAL   B 1 42  ? 37.305  10.911  43.349 1.00 41.06  ? 42  VAL   B CB  1 
ATOM   2599 C CG1 . VAL   B 1 42  ? 36.948  11.840  44.509 1.00 34.73  ? 42  VAL   B CG1 1 
ATOM   2600 C CG2 . VAL   B 1 42  ? 37.895  11.692  42.183 1.00 35.12  ? 42  VAL   B CG2 1 
ATOM   2601 N N   . ILE   B 1 43  ? 39.678  10.497  45.688 1.00 42.26  ? 43  ILE   B N   1 
ATOM   2602 C CA  . ILE   B 1 43  ? 40.870  11.094  46.290 1.00 38.95  ? 43  ILE   B CA  1 
ATOM   2603 C C   . ILE   B 1 43  ? 42.008  10.106  46.478 1.00 43.32  ? 43  ILE   B C   1 
ATOM   2604 O O   . ILE   B 1 43  ? 43.081  10.499  46.953 1.00 53.59  ? 43  ILE   B O   1 
ATOM   2605 C CB  . ILE   B 1 43  ? 40.564  11.729  47.663 1.00 46.57  ? 43  ILE   B CB  1 
ATOM   2606 C CG1 . ILE   B 1 43  ? 40.145  10.658  48.670 1.00 45.10  ? 43  ILE   B CG1 1 
ATOM   2607 C CG2 . ILE   B 1 43  ? 39.488  12.796  47.543 1.00 41.90  ? 43  ILE   B CG2 1 
ATOM   2608 C CD1 . ILE   B 1 43  ? 39.783  11.219  50.030 1.00 44.36  ? 43  ILE   B CD1 1 
ATOM   2609 N N   . CYS   B 1 44  ? 41.826  8.844   46.106 1.00 42.01  ? 44  CYS   B N   1 
ATOM   2610 C CA  . CYS   B 1 44  ? 42.773  7.796   46.455 1.00 44.92  ? 44  CYS   B CA  1 
ATOM   2611 C C   . CYS   B 1 44  ? 43.678  7.440   45.287 1.00 52.43  ? 44  CYS   B C   1 
ATOM   2612 O O   . CYS   B 1 44  ? 43.233  7.354   44.139 1.00 48.11  ? 44  CYS   B O   1 
ATOM   2613 C CB  . CYS   B 1 44  ? 42.041  6.540   46.922 1.00 42.92  ? 44  CYS   B CB  1 
ATOM   2614 S SG  . CYS   B 1 44  ? 41.122  6.768   48.442 1.00 47.48  ? 44  CYS   B SG  1 
ATOM   2615 N N   . THR   B 1 45  ? 44.953  7.231   45.595 1.00 49.95  ? 45  THR   B N   1 
ATOM   2616 C CA  . THR   B 1 45  ? 45.858  6.577   44.671 1.00 58.06  ? 45  THR   B CA  1 
ATOM   2617 C C   . THR   B 1 45  ? 45.655  5.068   44.746 1.00 55.63  ? 45  THR   B C   1 
ATOM   2618 O O   . THR   B 1 45  ? 44.966  4.550   45.630 1.00 51.83  ? 45  THR   B O   1 
ATOM   2619 C CB  . THR   B 1 45  ? 47.308  6.926   44.994 1.00 54.14  ? 45  THR   B CB  1 
ATOM   2620 O OG1 . THR   B 1 45  ? 47.691  6.272   46.210 1.00 52.84  ? 45  THR   B OG1 1 
ATOM   2621 C CG2 . THR   B 1 45  ? 47.463  8.427   45.169 1.00 53.71  ? 45  THR   B CG2 1 
ATOM   2622 N N   . SER   B 1 46  ? 46.273  4.357   43.801 1.00 53.62  ? 46  SER   B N   1 
ATOM   2623 C CA  . SER   B 1 46  ? 46.197  2.900   43.815 1.00 57.51  ? 46  SER   B CA  1 
ATOM   2624 C C   . SER   B 1 46  ? 46.756  2.334   45.117 1.00 54.14  ? 46  SER   B C   1 
ATOM   2625 O O   . SER   B 1 46  ? 46.235  1.347   45.648 1.00 58.57  ? 46  SER   B O   1 
ATOM   2626 C CB  . SER   B 1 46  ? 46.939  2.327   42.608 1.00 57.64  ? 46  SER   B CB  1 
ATOM   2627 O OG  . SER   B 1 46  ? 46.714  0.935   42.488 1.00 61.43  ? 46  SER   B OG  1 
ATOM   2628 N N   . GLU   B 1 47  ? 47.802  2.962   45.662 1.00 52.93  ? 47  GLU   B N   1 
ATOM   2629 C CA  . GLU   B 1 47  ? 48.378  2.476   46.912 1.00 52.17  ? 47  GLU   B CA  1 
ATOM   2630 C C   . GLU   B 1 47  ? 47.478  2.781   48.103 1.00 54.76  ? 47  GLU   B C   1 
ATOM   2631 O O   . GLU   B 1 47  ? 47.466  2.021   49.079 1.00 51.12  ? 47  GLU   B O   1 
ATOM   2632 C CB  . GLU   B 1 47  ? 49.765  3.082   47.127 1.00 48.66  ? 47  GLU   B CB  1 
ATOM   2633 N N   . ASP   B 1 48  ? 46.723  3.882   48.044 1.00 52.55  ? 48  ASP   B N   1 
ATOM   2634 C CA  . ASP   B 1 48  ? 45.807  4.205   49.134 1.00 52.30  ? 48  ASP   B CA  1 
ATOM   2635 C C   . ASP   B 1 48  ? 44.738  3.134   49.309 1.00 51.68  ? 48  ASP   B C   1 
ATOM   2636 O O   . ASP   B 1 48  ? 44.294  2.879   50.435 1.00 52.19  ? 48  ASP   B O   1 
ATOM   2637 C CB  . ASP   B 1 48  ? 45.142  5.561   48.889 1.00 54.03  ? 48  ASP   B CB  1 
ATOM   2638 C CG  . ASP   B 1 48  ? 46.115  6.715   48.986 1.00 55.95  ? 48  ASP   B CG  1 
ATOM   2639 O OD1 . ASP   B 1 48  ? 47.138  6.570   49.688 1.00 58.62  ? 48  ASP   B OD1 1 
ATOM   2640 O OD2 . ASP   B 1 48  ? 45.850  7.768   48.367 1.00 55.13  ? 48  ASP   B OD2 1 
ATOM   2641 N N   . MET   B 1 49  ? 44.318  2.493   48.216 1.00 51.22  ? 49  MET   B N   1 
ATOM   2642 C CA  . MET   B 1 49  ? 43.163  1.605   48.284 1.00 49.12  ? 49  MET   B CA  1 
ATOM   2643 C C   . MET   B 1 49  ? 43.447  0.301   49.015 1.00 51.50  ? 49  MET   B C   1 
ATOM   2644 O O   . MET   B 1 49  ? 42.496  -0.398  49.379 1.00 51.62  ? 49  MET   B O   1 
ATOM   2645 C CB  . MET   B 1 49  ? 42.638  1.302   46.880 1.00 48.65  ? 49  MET   B CB  1 
ATOM   2646 C CG  . MET   B 1 49  ? 41.986  2.495   46.201 1.00 49.80  ? 49  MET   B CG  1 
ATOM   2647 S SD  . MET   B 1 49  ? 40.587  3.196   47.108 1.00 48.77  ? 49  MET   B SD  1 
ATOM   2648 C CE  . MET   B 1 49  ? 39.322  1.961   46.825 1.00 37.79  ? 49  MET   B CE  1 
ATOM   2649 N N   . LEU   B 1 50  ? 44.715  -0.046  49.244 1.00 51.91  ? 50  LEU   B N   1 
ATOM   2650 C CA  . LEU   B 1 50  ? 44.997  -1.256  50.010 1.00 53.62  ? 50  LEU   B CA  1 
ATOM   2651 C C   . LEU   B 1 50  ? 44.515  -1.116  51.448 1.00 52.98  ? 50  LEU   B C   1 
ATOM   2652 O O   . LEU   B 1 50  ? 43.963  -2.066  52.017 1.00 52.96  ? 50  LEU   B O   1 
ATOM   2653 C CB  . LEU   B 1 50  ? 46.489  -1.579  49.956 1.00 60.34  ? 50  LEU   B CB  1 
ATOM   2654 C CG  . LEU   B 1 50  ? 46.950  -2.132  48.606 1.00 61.23  ? 50  LEU   B CG  1 
ATOM   2655 C CD1 . LEU   B 1 50  ? 48.450  -2.357  48.605 1.00 65.51  ? 50  LEU   B CD1 1 
ATOM   2656 C CD2 . LEU   B 1 50  ? 46.208  -3.423  48.274 1.00 61.10  ? 50  LEU   B CD2 1 
ATOM   2657 N N   . ASN   B 1 51  ? 44.695  0.062   52.043 1.00 45.68  ? 51  ASN   B N   1 
ATOM   2658 C CA  . ASN   B 1 51  ? 44.194  0.346   53.389 1.00 54.89  ? 51  ASN   B CA  1 
ATOM   2659 C C   . ASN   B 1 51  ? 43.944  1.842   53.514 1.00 49.25  ? 51  ASN   B C   1 
ATOM   2660 O O   . ASN   B 1 51  ? 44.767  2.585   54.061 1.00 50.87  ? 51  ASN   B O   1 
ATOM   2661 C CB  . ASN   B 1 51  ? 45.174  -0.133  54.462 1.00 56.31  ? 51  ASN   B CB  1 
ATOM   2662 C CG  . ASN   B 1 51  ? 44.618  0.013   55.860 1.00 57.07  ? 51  ASN   B CG  1 
ATOM   2663 O OD1 . ASN   B 1 51  ? 43.408  -0.079  56.070 1.00 58.86  ? 51  ASN   B OD1 1 
ATOM   2664 N ND2 . ASN   B 1 51  ? 45.496  0.254   56.824 1.00 67.71  ? 51  ASN   B ND2 1 
ATOM   2665 N N   . PRO   B 1 52  ? 42.799  2.327   53.007 1.00 44.06  ? 52  PRO   B N   1 
ATOM   2666 C CA  . PRO   B 1 52  ? 42.558  3.777   52.985 1.00 48.37  ? 52  PRO   B CA  1 
ATOM   2667 C C   . PRO   B 1 52  ? 41.928  4.323   54.257 1.00 44.73  ? 52  PRO   B C   1 
ATOM   2668 O O   . PRO   B 1 52  ? 40.901  3.822   54.725 1.00 50.58  ? 52  PRO   B O   1 
ATOM   2669 C CB  . PRO   B 1 52  ? 41.612  3.945   51.791 1.00 46.07  ? 52  PRO   B CB  1 
ATOM   2670 C CG  . PRO   B 1 52  ? 40.829  2.672   51.780 1.00 44.27  ? 52  PRO   B CG  1 
ATOM   2671 C CD  . PRO   B 1 52  ? 41.761  1.585   52.270 1.00 46.42  ? 52  PRO   B CD  1 
ATOM   2672 N N   . ASN   B 1 53  ? 42.540  5.363   54.816 1.00 43.88  ? 53  ASN   B N   1 
ATOM   2673 C CA  . ASN   B 1 53  ? 41.950  6.150   55.899 1.00 45.31  ? 53  ASN   B CA  1 
ATOM   2674 C C   . ASN   B 1 53  ? 41.377  7.405   55.249 1.00 46.21  ? 53  ASN   B C   1 
ATOM   2675 O O   . ASN   B 1 53  ? 42.074  8.403   55.067 1.00 44.10  ? 53  ASN   B O   1 
ATOM   2676 C CB  . ASN   B 1 53  ? 42.989  6.478   56.964 1.00 39.88  ? 53  ASN   B CB  1 
ATOM   2677 C CG  . ASN   B 1 53  ? 42.393  7.178   58.174 1.00 50.05  ? 53  ASN   B CG  1 
ATOM   2678 O OD1 . ASN   B 1 53  ? 41.614  8.127   58.048 1.00 44.34  ? 53  ASN   B OD1 1 
ATOM   2679 N ND2 . ASN   B 1 53  ? 42.759  6.709   59.361 1.00 50.65  ? 53  ASN   B ND2 1 
ATOM   2680 N N   . TYR   B 1 54  ? 40.089  7.347   54.896 1.00 43.49  ? 54  TYR   B N   1 
ATOM   2681 C CA  . TYR   B 1 54  ? 39.510  8.390   54.054 1.00 47.81  ? 54  TYR   B CA  1 
ATOM   2682 C C   . TYR   B 1 54  ? 39.472  9.744   54.754 1.00 46.61  ? 54  TYR   B C   1 
ATOM   2683 O O   . TYR   B 1 54  ? 39.674  10.775  54.101 1.00 48.65  ? 54  TYR   B O   1 
ATOM   2684 C CB  . TYR   B 1 54  ? 38.113  7.979   53.589 1.00 44.38  ? 54  TYR   B CB  1 
ATOM   2685 C CG  . TYR   B 1 54  ? 38.126  7.027   52.406 1.00 40.20  ? 54  TYR   B CG  1 
ATOM   2686 C CD1 . TYR   B 1 54  ? 38.251  7.504   51.106 1.00 40.07  ? 54  TYR   B CD1 1 
ATOM   2687 C CD2 . TYR   B 1 54  ? 38.016  5.654   52.588 1.00 37.13  ? 54  TYR   B CD2 1 
ATOM   2688 C CE1 . TYR   B 1 54  ? 38.256  6.639   50.022 1.00 33.94  ? 54  TYR   B CE1 1 
ATOM   2689 C CE2 . TYR   B 1 54  ? 38.024  4.785   51.509 1.00 36.56  ? 54  TYR   B CE2 1 
ATOM   2690 C CZ  . TYR   B 1 54  ? 38.149  5.285   50.227 1.00 42.24  ? 54  TYR   B CZ  1 
ATOM   2691 O OH  . TYR   B 1 54  ? 38.159  4.429   49.146 1.00 36.72  ? 54  TYR   B OH  1 
ATOM   2692 N N   . GLU   B 1 55  ? 39.225  9.774   56.067 1.00 44.82  ? 55  GLU   B N   1 
ATOM   2693 C CA  . GLU   B 1 55  ? 39.292  11.044  56.785 1.00 47.05  ? 55  GLU   B CA  1 
ATOM   2694 C C   . GLU   B 1 55  ? 40.669  11.682  56.644 1.00 48.90  ? 55  GLU   B C   1 
ATOM   2695 O O   . GLU   B 1 55  ? 40.780  12.885  56.383 1.00 54.23  ? 55  GLU   B O   1 
ATOM   2696 C CB  . GLU   B 1 55  ? 38.941  10.851  58.261 1.00 48.36  ? 55  GLU   B CB  1 
ATOM   2697 C CG  . GLU   B 1 55  ? 37.484  11.130  58.599 1.00 55.23  ? 55  GLU   B CG  1 
ATOM   2698 C CD  . GLU   B 1 55  ? 36.653  9.863   58.710 1.00 73.05  ? 55  GLU   B CD  1 
ATOM   2699 O OE1 . GLU   B 1 55  ? 37.153  8.784   58.321 1.00 67.25  ? 55  GLU   B OE1 1 
ATOM   2700 O OE2 . GLU   B 1 55  ? 35.501  9.944   59.192 1.00 70.96  ? 55  GLU   B OE2 1 
ATOM   2701 N N   . ASP   B 1 56  ? 41.731  10.886  56.786 1.00 46.48  ? 56  ASP   B N   1 
ATOM   2702 C CA  . ASP   B 1 56  ? 43.079  11.436  56.665 1.00 50.33  ? 56  ASP   B CA  1 
ATOM   2703 C C   . ASP   B 1 56  ? 43.386  11.855  55.230 1.00 49.14  ? 56  ASP   B C   1 
ATOM   2704 O O   . ASP   B 1 56  ? 43.954  12.929  55.002 1.00 48.76  ? 56  ASP   B O   1 
ATOM   2705 C CB  . ASP   B 1 56  ? 44.109  10.422  57.164 1.00 49.01  ? 56  ASP   B CB  1 
ATOM   2706 C CG  . ASP   B 1 56  ? 44.164  10.340  58.682 1.00 53.00  ? 56  ASP   B CG  1 
ATOM   2707 O OD1 . ASP   B 1 56  ? 43.333  10.992  59.353 1.00 53.41  ? 56  ASP   B OD1 1 
ATOM   2708 O OD2 . ASP   B 1 56  ? 45.046  9.628   59.207 1.00 48.58  ? 56  ASP   B OD2 1 
ATOM   2709 N N   . LEU   B 1 57  ? 43.021  11.023  54.249 1.00 47.85  ? 57  LEU   B N   1 
ATOM   2710 C CA  . LEU   B 1 57  ? 43.309  11.357  52.854 1.00 49.36  ? 57  LEU   B CA  1 
ATOM   2711 C C   . LEU   B 1 57  ? 42.548  12.600  52.411 1.00 51.88  ? 57  LEU   B C   1 
ATOM   2712 O O   . LEU   B 1 57  ? 43.093  13.443  51.689 1.00 54.39  ? 57  LEU   B O   1 
ATOM   2713 C CB  . LEU   B 1 57  ? 42.971  10.176  51.944 1.00 46.20  ? 57  LEU   B CB  1 
ATOM   2714 C CG  . LEU   B 1 57  ? 43.845  8.935   52.131 1.00 51.23  ? 57  LEU   B CG  1 
ATOM   2715 C CD1 . LEU   B 1 57  ? 43.269  7.750   51.375 1.00 50.59  ? 57  LEU   B CD1 1 
ATOM   2716 C CD2 . LEU   B 1 57  ? 45.270  9.223   51.683 1.00 43.29  ? 57  LEU   B CD2 1 
ATOM   2717 N N   . LEU   B 1 58  ? 41.287  12.731  52.825 1.00 50.06  ? 58  LEU   B N   1 
ATOM   2718 C CA  . LEU   B 1 58  ? 40.535  13.938  52.503 1.00 57.26  ? 58  LEU   B CA  1 
ATOM   2719 C C   . LEU   B 1 58  ? 41.100  15.157  53.218 1.00 57.99  ? 58  LEU   B C   1 
ATOM   2720 O O   . LEU   B 1 58  ? 40.999  16.278  52.704 1.00 49.59  ? 58  LEU   B O   1 
ATOM   2721 C CB  . LEU   B 1 58  ? 39.063  13.759  52.863 1.00 52.86  ? 58  LEU   B CB  1 
ATOM   2722 C CG  . LEU   B 1 58  ? 38.103  14.835  52.364 1.00 46.69  ? 58  LEU   B CG  1 
ATOM   2723 C CD1 . LEU   B 1 58  ? 38.138  14.931  50.840 1.00 46.43  ? 58  LEU   B CD1 1 
ATOM   2724 C CD2 . LEU   B 1 58  ? 36.700  14.541  52.850 1.00 42.76  ? 58  LEU   B CD2 1 
ATOM   2725 N N   . ILE   B 1 59  ? 41.718  14.954  54.385 1.00 54.74  ? 59  ILE   B N   1 
ATOM   2726 C CA  . ILE   B 1 59  ? 42.223  16.070  55.181 1.00 57.05  ? 59  ILE   B CA  1 
ATOM   2727 C C   . ILE   B 1 59  ? 43.312  16.832  54.430 1.00 58.84  ? 59  ILE   B C   1 
ATOM   2728 O O   . ILE   B 1 59  ? 43.433  18.054  54.574 1.00 66.10  ? 59  ILE   B O   1 
ATOM   2729 C CB  . ILE   B 1 59  ? 42.711  15.551  56.552 1.00 60.81  ? 59  ILE   B CB  1 
ATOM   2730 C CG1 . ILE   B 1 59  ? 41.798  16.040  57.680 1.00 52.61  ? 59  ILE   B CG1 1 
ATOM   2731 C CG2 . ILE   B 1 59  ? 44.152  15.959  56.836 1.00 55.34  ? 59  ILE   B CG2 1 
ATOM   2732 C CD1 . ILE   B 1 59  ? 40.311  15.895  57.401 1.00 56.98  ? 59  ILE   B CD1 1 
ATOM   2733 N N   . ARG   B 1 60  ? 44.103  16.144  53.607 1.00 53.74  ? 60  ARG   B N   1 
ATOM   2734 C CA  . ARG   B 1 60  ? 45.176  16.782  52.853 1.00 65.00  ? 60  ARG   B CA  1 
ATOM   2735 C C   . ARG   B 1 60  ? 44.707  17.398  51.538 1.00 63.08  ? 60  ARG   B C   1 
ATOM   2736 O O   . ARG   B 1 60  ? 45.504  18.060  50.863 1.00 65.69  ? 60  ARG   B O   1 
ATOM   2737 C CB  . ARG   B 1 60  ? 46.302  15.775  52.570 1.00 69.11  ? 60  ARG   B CB  1 
ATOM   2738 C CG  . ARG   B 1 60  ? 46.829  15.081  53.825 1.00 73.60  ? 60  ARG   B CG  1 
ATOM   2739 C CD  . ARG   B 1 60  ? 48.231  14.499  53.635 1.00 73.93  ? 60  ARG   B CD  1 
ATOM   2740 N NE  . ARG   B 1 60  ? 49.284  15.483  53.869 1.00 77.49  ? 60  ARG   B NE  1 
ATOM   2741 C CZ  . ARG   B 1 60  ? 50.135  15.909  52.945 1.00 84.47  ? 60  ARG   B CZ  1 
ATOM   2742 N NH1 . ARG   B 1 60  ? 50.097  15.445  51.705 1.00 81.72  ? 60  ARG   B NH1 1 
ATOM   2743 N NH2 . ARG   B 1 60  ? 51.052  16.816  53.275 1.00 75.84  ? 60  ARG   B NH2 1 
ATOM   2744 N N   . LYS   B 1 61  ? 43.449  17.202  51.154 1.00 64.57  ? 61  LYS   B N   1 
ATOM   2745 C CA  . LYS   B 1 61  ? 42.912  17.814  49.947 1.00 56.11  ? 61  LYS   B CA  1 
ATOM   2746 C C   . LYS   B 1 61  ? 42.218  19.126  50.286 1.00 54.63  ? 61  LYS   B C   1 
ATOM   2747 O O   . LYS   B 1 61  ? 41.495  19.222  51.281 1.00 55.23  ? 61  LYS   B O   1 
ATOM   2748 C CB  . LYS   B 1 61  ? 41.930  16.870  49.250 1.00 49.96  ? 61  LYS   B CB  1 
ATOM   2749 C CG  . LYS   B 1 61  ? 42.573  15.622  48.675 1.00 53.50  ? 61  LYS   B CG  1 
ATOM   2750 C CD  . LYS   B 1 61  ? 43.418  15.949  47.458 1.00 53.37  ? 61  LYS   B CD  1 
ATOM   2751 C CE  . LYS   B 1 61  ? 43.974  14.686  46.831 1.00 54.17  ? 61  LYS   B CE  1 
ATOM   2752 N NZ  . LYS   B 1 61  ? 44.840  13.948  47.787 1.00 65.68  ? 61  LYS   B NZ  1 
ATOM   2753 N N   . SER   B 1 62  ? 42.450  20.137  49.455 1.00 52.74  ? 62  SER   B N   1 
ATOM   2754 C CA  . SER   B 1 62  ? 41.792  21.430  49.573 1.00 56.19  ? 62  SER   B CA  1 
ATOM   2755 C C   . SER   B 1 62  ? 40.756  21.581  48.465 1.00 52.62  ? 62  SER   B C   1 
ATOM   2756 O O   . SER   B 1 62  ? 40.646  20.741  47.567 1.00 47.91  ? 62  SER   B O   1 
ATOM   2757 C CB  . SER   B 1 62  ? 42.813  22.574  49.517 1.00 56.16  ? 62  SER   B CB  1 
ATOM   2758 O OG  . SER   B 1 62  ? 43.716  22.508  50.608 1.00 58.12  ? 62  SER   B OG  1 
ATOM   2759 N N   . ASN   B 1 63  ? 39.986  22.672  48.545 1.00 51.22  ? 63  ASN   B N   1 
ATOM   2760 C CA  . ASN   B 1 63  ? 38.966  22.936  47.533 1.00 56.56  ? 63  ASN   B CA  1 
ATOM   2761 C C   . ASN   B 1 63  ? 39.573  23.008  46.137 1.00 52.94  ? 63  ASN   B C   1 
ATOM   2762 O O   . ASN   B 1 63  ? 39.014  22.457  45.181 1.00 51.88  ? 63  ASN   B O   1 
ATOM   2763 C CB  . ASN   B 1 63  ? 38.222  24.235  47.846 1.00 45.96  ? 63  ASN   B CB  1 
ATOM   2764 C CG  . ASN   B 1 63  ? 37.298  24.111  49.039 1.00 57.46  ? 63  ASN   B CG  1 
ATOM   2765 O OD1 . ASN   B 1 63  ? 36.754  23.041  49.318 1.00 52.53  ? 63  ASN   B OD1 1 
ATOM   2766 N ND2 . ASN   B 1 63  ? 37.107  25.216  49.749 1.00 53.18  ? 63  ASN   B ND2 1 
ATOM   2767 N N   . HIS   B 1 64  ? 40.721  23.677  45.999 1.00 55.14  ? 64  HIS   B N   1 
ATOM   2768 C CA  . HIS   B 1 64  ? 41.322  23.856  44.682 1.00 56.74  ? 64  HIS   B CA  1 
ATOM   2769 C C   . HIS   B 1 64  ? 41.890  22.565  44.103 1.00 51.70  ? 64  HIS   B C   1 
ATOM   2770 O O   . HIS   B 1 64  ? 42.251  22.548  42.922 1.00 48.84  ? 64  HIS   B O   1 
ATOM   2771 C CB  . HIS   B 1 64  ? 42.418  24.923  44.737 1.00 54.12  ? 64  HIS   B CB  1 
ATOM   2772 C CG  . HIS   B 1 64  ? 43.604  24.533  45.563 1.00 56.43  ? 64  HIS   B CG  1 
ATOM   2773 N ND1 . HIS   B 1 64  ? 44.523  23.591  45.150 1.00 64.70  ? 64  HIS   B ND1 1 
ATOM   2774 C CD2 . HIS   B 1 64  ? 44.023  24.961  46.776 1.00 57.71  ? 64  HIS   B CD2 1 
ATOM   2775 C CE1 . HIS   B 1 64  ? 45.456  23.455  46.075 1.00 60.37  ? 64  HIS   B CE1 1 
ATOM   2776 N NE2 . HIS   B 1 64  ? 45.177  24.276  47.071 1.00 62.16  ? 64  HIS   B NE2 1 
ATOM   2777 N N   . ASN   B 1 65  ? 41.987  21.494  44.893 1.00 50.13  ? 65  ASN   B N   1 
ATOM   2778 C CA  . ASN   B 1 65  ? 42.401  20.206  44.352 1.00 49.09  ? 65  ASN   B CA  1 
ATOM   2779 C C   . ASN   B 1 65  ? 41.291  19.505  43.584 1.00 47.75  ? 65  ASN   B C   1 
ATOM   2780 O O   . ASN   B 1 65  ? 41.546  18.454  42.985 1.00 43.85  ? 65  ASN   B O   1 
ATOM   2781 C CB  . ASN   B 1 65  ? 42.886  19.278  45.468 1.00 55.86  ? 65  ASN   B CB  1 
ATOM   2782 C CG  . ASN   B 1 65  ? 44.168  19.755  46.113 1.00 57.73  ? 65  ASN   B CG  1 
ATOM   2783 O OD1 . ASN   B 1 65  ? 44.244  19.887  47.333 1.00 56.21  ? 65  ASN   B OD1 1 
ATOM   2784 N ND2 . ASN   B 1 65  ? 45.185  20.012  45.299 1.00 58.18  ? 65  ASN   B ND2 1 
ATOM   2785 N N   . PHE   B 1 66  ? 40.076  20.041  43.598 1.00 40.53  ? 66  PHE   B N   1 
ATOM   2786 C CA  . PHE   B 1 66  ? 38.938  19.428  42.928 1.00 50.91  ? 66  PHE   B CA  1 
ATOM   2787 C C   . PHE   B 1 66  ? 38.516  20.299  41.753 1.00 45.07  ? 66  PHE   B C   1 
ATOM   2788 O O   . PHE   B 1 66  ? 38.224  21.488  41.924 1.00 50.21  ? 66  PHE   B O   1 
ATOM   2789 C CB  . PHE   B 1 66  ? 37.756  19.233  43.886 1.00 40.71  ? 66  PHE   B CB  1 
ATOM   2790 C CG  . PHE   B 1 66  ? 38.026  18.274  45.022 1.00 41.81  ? 66  PHE   B CG  1 
ATOM   2791 C CD1 . PHE   B 1 66  ? 38.092  16.903  44.800 1.00 47.11  ? 66  PHE   B CD1 1 
ATOM   2792 C CD2 . PHE   B 1 66  ? 38.166  18.743  46.320 1.00 45.83  ? 66  PHE   B CD2 1 
ATOM   2793 C CE1 . PHE   B 1 66  ? 38.325  16.023  45.848 1.00 46.33  ? 66  PHE   B CE1 1 
ATOM   2794 C CE2 . PHE   B 1 66  ? 38.392  17.868  47.372 1.00 44.13  ? 66  PHE   B CE2 1 
ATOM   2795 C CZ  . PHE   B 1 66  ? 38.472  16.508  47.135 1.00 44.67  ? 66  PHE   B CZ  1 
ATOM   2796 N N   . LEU   B 1 67  ? 38.484  19.703  40.566 1.00 42.36  ? 67  LEU   B N   1 
ATOM   2797 C CA  . LEU   B 1 67  ? 38.061  20.376  39.344 1.00 41.64  ? 67  LEU   B CA  1 
ATOM   2798 C C   . LEU   B 1 67  ? 36.750  19.756  38.884 1.00 43.83  ? 67  LEU   B C   1 
ATOM   2799 O O   . LEU   B 1 67  ? 36.697  18.555  38.596 1.00 40.43  ? 67  LEU   B O   1 
ATOM   2800 C CB  . LEU   B 1 67  ? 39.124  20.242  38.253 1.00 50.90  ? 67  LEU   B CB  1 
ATOM   2801 C CG  . LEU   B 1 67  ? 40.362  21.143  38.207 1.00 62.05  ? 67  LEU   B CG  1 
ATOM   2802 C CD1 . LEU   B 1 67  ? 40.831  21.616  39.580 1.00 58.40  ? 67  LEU   B CD1 1 
ATOM   2803 C CD2 . LEU   B 1 67  ? 41.462  20.366  37.510 1.00 56.98  ? 67  LEU   B CD2 1 
ATOM   2804 N N   . VAL   B 1 68  ? 35.697  20.565  38.817 1.00 35.90  ? 68  VAL   B N   1 
ATOM   2805 C CA  . VAL   B 1 68  ? 34.396  20.117  38.333 1.00 47.42  ? 68  VAL   B CA  1 
ATOM   2806 C C   . VAL   B 1 68  ? 34.116  20.807  37.008 1.00 51.61  ? 68  VAL   B C   1 
ATOM   2807 O O   . VAL   B 1 68  ? 34.226  22.035  36.902 1.00 53.62  ? 68  VAL   B O   1 
ATOM   2808 C CB  . VAL   B 1 68  ? 33.274  20.397  39.346 1.00 42.34  ? 68  VAL   B CB  1 
ATOM   2809 C CG1 . VAL   B 1 68  ? 31.944  19.890  38.801 1.00 37.20  ? 68  VAL   B CG1 1 
ATOM   2810 C CG2 . VAL   B 1 68  ? 33.590  19.736  40.677 1.00 41.35  ? 68  VAL   B CG2 1 
ATOM   2811 N N   . GLN   B 1 69  ? 33.753  20.016  36.000 1.00 50.02  ? 69  GLN   B N   1 
ATOM   2812 C CA  . GLN   B 1 69  ? 33.489  20.524  34.658 1.00 47.58  ? 69  GLN   B CA  1 
ATOM   2813 C C   . GLN   B 1 69  ? 32.137  19.998  34.194 1.00 47.03  ? 69  GLN   B C   1 
ATOM   2814 O O   . GLN   B 1 69  ? 31.964  18.789  34.010 1.00 47.88  ? 69  GLN   B O   1 
ATOM   2815 C CB  . GLN   B 1 69  ? 34.601  20.116  33.691 1.00 50.55  ? 69  GLN   B CB  1 
ATOM   2816 C CG  . GLN   B 1 69  ? 34.624  20.924  32.407 1.00 62.19  ? 69  GLN   B CG  1 
ATOM   2817 C CD  . GLN   B 1 69  ? 35.918  20.756  31.630 1.00 67.93  ? 69  GLN   B CD  1 
ATOM   2818 O OE1 . GLN   B 1 69  ? 36.837  20.065  32.071 1.00 63.20  ? 69  GLN   B OE1 1 
ATOM   2819 N NE2 . GLN   B 1 69  ? 35.995  21.395  30.467 1.00 68.91  ? 69  GLN   B NE2 1 
ATOM   2820 N N   . ALA   B 1 70  ? 31.180  20.906  34.015 1.00 52.39  ? 70  ALA   B N   1 
ATOM   2821 C CA  . ALA   B 1 70  ? 29.864  20.585  33.462 1.00 52.03  ? 70  ALA   B CA  1 
ATOM   2822 C C   . ALA   B 1 70  ? 29.931  20.849  31.960 1.00 57.93  ? 70  ALA   B C   1 
ATOM   2823 O O   . ALA   B 1 70  ? 29.658  21.955  31.491 1.00 58.84  ? 70  ALA   B O   1 
ATOM   2824 C CB  . ALA   B 1 70  ? 28.773  21.409  34.133 1.00 44.98  ? 70  ALA   B CB  1 
ATOM   2825 N N   . GLY   B 1 71  ? 30.300  19.821  31.201 1.00 53.27  ? 71  GLY   B N   1 
ATOM   2826 C CA  . GLY   B 1 71  ? 30.567  20.011  29.790 1.00 55.93  ? 71  GLY   B CA  1 
ATOM   2827 C C   . GLY   B 1 71  ? 31.843  20.803  29.596 1.00 60.26  ? 71  GLY   B C   1 
ATOM   2828 O O   . GLY   B 1 71  ? 32.941  20.269  29.778 1.00 62.30  ? 71  GLY   B O   1 
ATOM   2829 N N   . ASN   B 1 72  ? 31.718  22.082  29.245 1.00 56.94  ? 72  ASN   B N   1 
ATOM   2830 C CA  . ASN   B 1 72  ? 32.871  22.969  29.150 1.00 69.67  ? 72  ASN   B CA  1 
ATOM   2831 C C   . ASN   B 1 72  ? 32.795  24.124  30.142 1.00 69.28  ? 72  ASN   B C   1 
ATOM   2832 O O   . ASN   B 1 72  ? 33.580  25.075  30.035 1.00 69.60  ? 72  ASN   B O   1 
ATOM   2833 C CB  . ASN   B 1 72  ? 33.019  23.500  27.721 1.00 71.60  ? 72  ASN   B CB  1 
ATOM   2834 C CG  . ASN   B 1 72  ? 33.152  22.385  26.699 1.00 74.05  ? 72  ASN   B CG  1 
ATOM   2835 O OD1 . ASN   B 1 72  ? 34.245  21.865  26.467 1.00 73.89  ? 72  ASN   B OD1 1 
ATOM   2836 N ND2 . ASN   B 1 72  ? 32.035  22.009  26.087 1.00 77.20  ? 72  ASN   B ND2 1 
ATOM   2837 N N   . VAL   B 1 73  ? 31.881  24.061  31.107 1.00 65.20  ? 73  VAL   B N   1 
ATOM   2838 C CA  . VAL   B 1 73  ? 31.717  25.093  32.124 1.00 65.37  ? 73  VAL   B CA  1 
ATOM   2839 C C   . VAL   B 1 73  ? 32.422  24.631  33.393 1.00 67.01  ? 73  VAL   B C   1 
ATOM   2840 O O   . VAL   B 1 73  ? 32.051  23.607  33.980 1.00 57.61  ? 73  VAL   B O   1 
ATOM   2841 C CB  . VAL   B 1 73  ? 30.231  25.378  32.394 1.00 63.91  ? 73  VAL   B CB  1 
ATOM   2842 C CG1 . VAL   B 1 73  ? 30.072  26.337  33.567 1.00 64.38  ? 73  VAL   B CG1 1 
ATOM   2843 C CG2 . VAL   B 1 73  ? 29.559  25.932  31.143 1.00 58.89  ? 73  VAL   B CG2 1 
ATOM   2844 N N   . GLN   B 1 74  ? 33.439  25.380  33.818 1.00 65.98  ? 74  GLN   B N   1 
ATOM   2845 C CA  . GLN   B 1 74  ? 34.175  25.056  35.035 1.00 61.73  ? 74  GLN   B CA  1 
ATOM   2846 C C   . GLN   B 1 74  ? 33.421  25.595  36.246 1.00 65.94  ? 74  GLN   B C   1 
ATOM   2847 O O   . GLN   B 1 74  ? 33.139  26.797  36.324 1.00 66.40  ? 74  GLN   B O   1 
ATOM   2848 C CB  . GLN   B 1 74  ? 35.586  25.641  34.984 1.00 63.31  ? 74  GLN   B CB  1 
ATOM   2849 C CG  . GLN   B 1 74  ? 36.233  25.629  33.607 1.00 73.41  ? 74  GLN   B CG  1 
ATOM   2850 C CD  . GLN   B 1 74  ? 36.469  24.229  33.079 1.00 70.45  ? 74  GLN   B CD  1 
ATOM   2851 O OE1 . GLN   B 1 74  ? 35.873  23.823  32.083 1.00 68.14  ? 74  GLN   B OE1 1 
ATOM   2852 N NE2 . GLN   B 1 74  ? 37.352  23.485  33.738 1.00 68.29  ? 74  GLN   B NE2 1 
ATOM   2853 N N   . LEU   B 1 75  ? 33.100  24.710  37.186 1.00 54.60  ? 75  LEU   B N   1 
ATOM   2854 C CA  . LEU   B 1 75  ? 32.412  25.073  38.419 1.00 58.96  ? 75  LEU   B CA  1 
ATOM   2855 C C   . LEU   B 1 75  ? 33.424  25.066  39.556 1.00 61.11  ? 75  LEU   B C   1 
ATOM   2856 O O   . LEU   B 1 75  ? 33.950  24.005  39.912 1.00 62.61  ? 75  LEU   B O   1 
ATOM   2857 C CB  . LEU   B 1 75  ? 31.273  24.098  38.719 1.00 48.15  ? 75  LEU   B CB  1 
ATOM   2858 C CG  . LEU   B 1 75  ? 30.245  23.847  37.615 1.00 54.95  ? 75  LEU   B CG  1 
ATOM   2859 C CD1 . LEU   B 1 75  ? 29.307  22.729  38.031 1.00 50.71  ? 75  LEU   B CD1 1 
ATOM   2860 C CD2 . LEU   B 1 75  ? 29.475  25.118  37.322 1.00 60.66  ? 75  LEU   B CD2 1 
ATOM   2861 N N   . ARG   B 1 76  ? 33.690  26.235  40.131 1.00 59.39  ? 76  ARG   B N   1 
ATOM   2862 C CA  . ARG   B 1 76  ? 34.712  26.332  41.162 1.00 59.23  ? 76  ARG   B CA  1 
ATOM   2863 C C   . ARG   B 1 76  ? 34.187  25.785  42.485 1.00 55.79  ? 76  ARG   B C   1 
ATOM   2864 O O   . ARG   B 1 76  ? 33.050  26.064  42.884 1.00 47.60  ? 76  ARG   B O   1 
ATOM   2865 C CB  . ARG   B 1 76  ? 35.193  27.775  41.309 1.00 56.68  ? 76  ARG   B CB  1 
ATOM   2866 C CG  . ARG   B 1 76  ? 36.097  28.206  40.159 1.00 72.88  ? 76  ARG   B CG  1 
ATOM   2867 C CD  . ARG   B 1 76  ? 37.051  29.315  40.565 1.00 71.36  ? 76  ARG   B CD  1 
ATOM   2868 N NE  . ARG   B 1 76  ? 36.361  30.575  40.815 1.00 82.53  ? 76  ARG   B NE  1 
ATOM   2869 C CZ  . ARG   B 1 76  ? 36.947  31.661  41.300 1.00 77.42  ? 76  ARG   B CZ  1 
ATOM   2870 N NH1 . ARG   B 1 76  ? 38.232  31.671  41.614 1.00 77.84  ? 76  ARG   B NH1 1 
ATOM   2871 N NH2 . ARG   B 1 76  ? 36.225  32.764  41.477 1.00 78.89  ? 76  ARG   B NH2 1 
ATOM   2872 N N   . VAL   B 1 77  ? 35.017  24.984  43.146 1.00 52.55  ? 77  VAL   B N   1 
ATOM   2873 C CA  . VAL   B 1 77  ? 34.634  24.314  44.382 1.00 46.28  ? 77  VAL   B CA  1 
ATOM   2874 C C   . VAL   B 1 77  ? 34.887  25.247  45.556 1.00 48.98  ? 77  VAL   B C   1 
ATOM   2875 O O   . VAL   B 1 77  ? 36.005  25.741  45.743 1.00 52.92  ? 77  VAL   B O   1 
ATOM   2876 C CB  . VAL   B 1 77  ? 35.409  22.999  44.548 1.00 46.52  ? 77  VAL   B CB  1 
ATOM   2877 C CG1 . VAL   B 1 77  ? 35.019  22.319  45.851 1.00 50.25  ? 77  VAL   B CG1 1 
ATOM   2878 C CG2 . VAL   B 1 77  ? 35.163  22.079  43.359 1.00 42.16  ? 77  VAL   B CG2 1 
ATOM   2879 N N   . ILE   B 1 78  ? 33.848  25.485  46.353 1.00 45.51  ? 78  ILE   B N   1 
ATOM   2880 C CA  . ILE   B 1 78  ? 33.935  26.344  47.525 1.00 55.12  ? 78  ILE   B CA  1 
ATOM   2881 C C   . ILE   B 1 78  ? 33.729  25.572  48.822 1.00 55.85  ? 78  ILE   B C   1 
ATOM   2882 O O   . ILE   B 1 78  ? 33.623  26.179  49.888 1.00 55.40  ? 78  ILE   B O   1 
ATOM   2883 C CB  . ILE   B 1 78  ? 32.937  27.513  47.426 1.00 50.79  ? 78  ILE   B CB  1 
ATOM   2884 C CG1 . ILE   B 1 78  ? 31.500  26.988  47.469 1.00 54.79  ? 78  ILE   B CG1 1 
ATOM   2885 C CG2 . ILE   B 1 78  ? 33.170  28.298  46.146 1.00 48.11  ? 78  ILE   B CG2 1 
ATOM   2886 C CD1 . ILE   B 1 78  ? 30.453  28.075  47.362 1.00 51.91  ? 78  ILE   B CD1 1 
ATOM   2887 N N   . GLY   B 1 79  ? 33.667  24.244  48.755 1.00 55.97  ? 79  GLY   B N   1 
ATOM   2888 C CA  . GLY   B 1 79  ? 33.479  23.431  49.941 1.00 54.50  ? 79  GLY   B CA  1 
ATOM   2889 C C   . GLY   B 1 79  ? 33.473  21.950  49.625 1.00 56.99  ? 79  GLY   B C   1 
ATOM   2890 O O   . GLY   B 1 79  ? 33.030  21.544  48.547 1.00 48.38  ? 79  GLY   B O   1 
ATOM   2891 N N   . HIS   B 1 80  ? 33.968  21.134  50.554 1.00 54.01  ? 80  HIS   B N   1 
ATOM   2892 C CA  . HIS   B 1 80  ? 34.035  19.694  50.349 1.00 48.81  ? 80  HIS   B CA  1 
ATOM   2893 C C   . HIS   B 1 80  ? 33.840  18.995  51.683 1.00 59.68  ? 80  HIS   B C   1 
ATOM   2894 O O   . HIS   B 1 80  ? 34.454  19.375  52.685 1.00 57.41  ? 80  HIS   B O   1 
ATOM   2895 C CB  . HIS   B 1 80  ? 35.371  19.281  49.721 1.00 53.43  ? 80  HIS   B CB  1 
ATOM   2896 C CG  . HIS   B 1 80  ? 36.561  19.530  50.598 1.00 54.36  ? 80  HIS   B CG  1 
ATOM   2897 N ND1 . HIS   B 1 80  ? 37.106  20.784  50.778 1.00 59.32  ? 80  HIS   B ND1 1 
ATOM   2898 C CD2 . HIS   B 1 80  ? 37.318  18.683  51.335 1.00 53.74  ? 80  HIS   B CD2 1 
ATOM   2899 C CE1 . HIS   B 1 80  ? 38.143  20.699  51.591 1.00 53.41  ? 80  HIS   B CE1 1 
ATOM   2900 N NE2 . HIS   B 1 80  ? 38.294  19.435  51.943 1.00 54.43  ? 80  HIS   B NE2 1 
ATOM   2901 N N   . SER   B 1 81  ? 32.980  17.982  51.697 1.00 43.90  ? 81  SER   B N   1 
ATOM   2902 C CA  . SER   B 1 81  ? 32.785  17.179  52.892 1.00 47.31  ? 81  SER   B CA  1 
ATOM   2903 C C   . SER   B 1 81  ? 32.532  15.745  52.465 1.00 51.46  ? 81  SER   B C   1 
ATOM   2904 O O   . SER   B 1 81  ? 32.278  15.458  51.293 1.00 40.19  ? 81  SER   B O   1 
ATOM   2905 C CB  . SER   B 1 81  ? 31.630  17.701  53.753 1.00 45.01  ? 81  SER   B CB  1 
ATOM   2906 O OG  . SER   B 1 81  ? 30.374  17.391  53.176 1.00 49.82  ? 81  SER   B OG  1 
ATOM   2907 N N   . MET   B 1 82  ? 32.594  14.844  53.435 1.00 40.22  ? 82  MET   B N   1 
ATOM   2908 C CA  . MET   B 1 82  ? 32.426  13.423  53.183 1.00 44.01  ? 82  MET   B CA  1 
ATOM   2909 C C   . MET   B 1 82  ? 31.225  12.924  53.966 1.00 44.97  ? 82  MET   B C   1 
ATOM   2910 O O   . MET   B 1 82  ? 31.182  13.057  55.195 1.00 47.55  ? 82  MET   B O   1 
ATOM   2911 C CB  . MET   B 1 82  ? 33.684  12.657  53.574 1.00 38.99  ? 82  MET   B CB  1 
ATOM   2912 C CG  . MET   B 1 82  ? 33.625  11.185  53.282 1.00 46.42  ? 82  MET   B CG  1 
ATOM   2913 S SD  . MET   B 1 82  ? 35.239  10.473  53.604 1.00 49.44  ? 82  MET   B SD  1 
ATOM   2914 C CE  . MET   B 1 82  ? 35.370  10.786  55.362 1.00 54.08  ? 82  MET   B CE  1 
ATOM   2915 N N   . GLN   B 1 83  ? 30.246  12.368  53.255 1.00 40.15  ? 83  GLN   B N   1 
ATOM   2916 C CA  . GLN   B 1 83  ? 29.094  11.720  53.872 1.00 46.00  ? 83  GLN   B CA  1 
ATOM   2917 C C   . GLN   B 1 83  ? 29.193  10.236  53.563 1.00 44.96  ? 83  GLN   B C   1 
ATOM   2918 O O   . GLN   B 1 83  ? 28.950  9.819   52.424 1.00 39.55  ? 83  GLN   B O   1 
ATOM   2919 C CB  . GLN   B 1 83  ? 27.773  12.295  53.366 1.00 47.04  ? 83  GLN   B CB  1 
ATOM   2920 C CG  . GLN   B 1 83  ? 26.562  11.597  53.969 1.00 51.95  ? 83  GLN   B CG  1 
ATOM   2921 C CD  . GLN   B 1 83  ? 25.243  12.237  53.581 1.00 58.64  ? 83  GLN   B CD  1 
ATOM   2922 O OE1 . GLN   B 1 83  ? 25.208  13.249  52.880 1.00 64.40  ? 83  GLN   B OE1 1 
ATOM   2923 N NE2 . GLN   B 1 83  ? 24.145  11.646  54.041 1.00 54.30  ? 83  GLN   B NE2 1 
ATOM   2924 N N   . ASN   B 1 84  ? 29.548  9.445   54.575 1.00 36.19  ? 84  ASN   B N   1 
ATOM   2925 C CA  . ASN   B 1 84  ? 29.752  8.018   54.380 1.00 36.43  ? 84  ASN   B CA  1 
ATOM   2926 C C   . ASN   B 1 84  ? 30.742  7.817   53.236 1.00 33.95  ? 84  ASN   B C   1 
ATOM   2927 O O   . ASN   B 1 84  ? 31.867  8.322   53.300 1.00 34.40  ? 84  ASN   B O   1 
ATOM   2928 C CB  . ASN   B 1 84  ? 28.408  7.325   54.133 1.00 40.38  ? 84  ASN   B CB  1 
ATOM   2929 C CG  . ASN   B 1 84  ? 27.468  7.440   55.330 1.00 44.80  ? 84  ASN   B CG  1 
ATOM   2930 O OD1 . ASN   B 1 84  ? 27.839  7.104   56.455 1.00 37.13  ? 84  ASN   B OD1 1 
ATOM   2931 N ND2 . ASN   B 1 84  ? 26.256  7.932   55.093 1.00 40.00  ? 84  ASN   B ND2 1 
ATOM   2932 N N   . CYS   B 1 85  ? 30.338  7.132   52.168 1.00 37.10  ? 85  CYS   B N   1 
ATOM   2933 C CA  . CYS   B 1 85  ? 31.259  6.828   51.078 1.00 36.27  ? 85  CYS   B CA  1 
ATOM   2934 C C   . CYS   B 1 85  ? 31.122  7.761   49.876 1.00 37.73  ? 85  CYS   B C   1 
ATOM   2935 O O   . CYS   B 1 85  ? 31.702  7.476   48.822 1.00 39.20  ? 85  CYS   B O   1 
ATOM   2936 C CB  . CYS   B 1 85  ? 31.084  5.379   50.633 1.00 38.63  ? 85  CYS   B CB  1 
ATOM   2937 S SG  . CYS   B 1 85  ? 31.481  4.190   51.922 1.00 42.70  ? 85  CYS   B SG  1 
ATOM   2938 N N   . VAL   B 1 86  ? 30.389  8.866   50.001 1.00 34.07  ? 86  VAL   B N   1 
ATOM   2939 C CA  . VAL   B 1 86  ? 30.274  9.822   48.905 1.00 34.44  ? 86  VAL   B CA  1 
ATOM   2940 C C   . VAL   B 1 86  ? 30.885  11.151  49.319 1.00 41.01  ? 86  VAL   B C   1 
ATOM   2941 O O   . VAL   B 1 86  ? 30.823  11.566  50.482 1.00 34.90  ? 86  VAL   B O   1 
ATOM   2942 C CB  . VAL   B 1 86  ? 28.818  10.038  48.432 1.00 39.83  ? 86  VAL   B CB  1 
ATOM   2943 C CG1 . VAL   B 1 86  ? 28.231  8.746   47.918 1.00 39.52  ? 86  VAL   B CG1 1 
ATOM   2944 C CG2 . VAL   B 1 86  ? 27.960  10.626  49.540 1.00 48.70  ? 86  VAL   B CG2 1 
ATOM   2945 N N   . LEU   B 1 87  ? 31.469  11.824  48.336 1.00 32.37  ? 87  LEU   B N   1 
ATOM   2946 C CA  . LEU   B 1 87  ? 32.032  13.155  48.502 1.00 39.15  ? 87  LEU   B CA  1 
ATOM   2947 C C   . LEU   B 1 87  ? 31.021  14.183  48.018 1.00 44.15  ? 87  LEU   B C   1 
ATOM   2948 O O   . LEU   B 1 87  ? 30.481  14.053  46.914 1.00 40.76  ? 87  LEU   B O   1 
ATOM   2949 C CB  . LEU   B 1 87  ? 33.337  13.281  47.713 1.00 45.29  ? 87  LEU   B CB  1 
ATOM   2950 C CG  . LEU   B 1 87  ? 34.152  14.561  47.853 1.00 51.67  ? 87  LEU   B CG  1 
ATOM   2951 C CD1 . LEU   B 1 87  ? 34.620  14.729  49.284 1.00 48.91  ? 87  LEU   B CD1 1 
ATOM   2952 C CD2 . LEU   B 1 87  ? 35.336  14.527  46.902 1.00 43.29  ? 87  LEU   B CD2 1 
ATOM   2953 N N   . LYS   B 1 88  ? 30.762  15.197  48.842 1.00 43.85  ? 88  LYS   B N   1 
ATOM   2954 C CA  . LYS   B 1 88  ? 29.862  16.292  48.492 1.00 43.12  ? 88  LYS   B CA  1 
ATOM   2955 C C   . LYS   B 1 88  ? 30.692  17.549  48.253 1.00 47.71  ? 88  LYS   B C   1 
ATOM   2956 O O   . LYS   B 1 88  ? 31.196  18.158  49.203 1.00 51.80  ? 88  LYS   B O   1 
ATOM   2957 C CB  . LYS   B 1 88  ? 28.815  16.521  49.581 1.00 41.18  ? 88  LYS   B CB  1 
ATOM   2958 C CG  . LYS   B 1 88  ? 27.803  15.394  49.710 1.00 45.57  ? 88  LYS   B CG  1 
ATOM   2959 C CD  . LYS   B 1 88  ? 26.602  15.806  50.549 1.00 44.79  ? 88  LYS   B CD  1 
ATOM   2960 C CE  . LYS   B 1 88  ? 26.971  16.036  52.002 1.00 57.07  ? 88  LYS   B CE  1 
ATOM   2961 N NZ  . LYS   B 1 88  ? 25.761  16.394  52.795 1.00 54.67  ? 88  LYS   B NZ  1 
ATOM   2962 N N   . LEU   B 1 89  ? 30.830  17.932  46.983 1.00 47.30  ? 89  LEU   B N   1 
ATOM   2963 C CA  . LEU   B 1 89  ? 31.529  19.149  46.584 1.00 45.03  ? 89  LEU   B CA  1 
ATOM   2964 C C   . LEU   B 1 89  ? 30.510  20.274  46.443 1.00 51.09  ? 89  LEU   B C   1 
ATOM   2965 O O   . LEU   B 1 89  ? 29.657  20.237  45.550 1.00 45.27  ? 89  LEU   B O   1 
ATOM   2966 C CB  . LEU   B 1 89  ? 32.276  18.940  45.268 1.00 38.70  ? 89  LEU   B CB  1 
ATOM   2967 C CG  . LEU   B 1 89  ? 33.278  17.793  45.206 1.00 44.48  ? 89  LEU   B CG  1 
ATOM   2968 C CD1 . LEU   B 1 89  ? 33.912  17.700  43.823 1.00 41.95  ? 89  LEU   B CD1 1 
ATOM   2969 C CD2 . LEU   B 1 89  ? 34.337  17.981  46.272 1.00 48.72  ? 89  LEU   B CD2 1 
ATOM   2970 N N   . LYS   B 1 90  ? 30.598  21.278  47.314 1.00 49.85  ? 90  LYS   B N   1 
ATOM   2971 C CA  . LYS   B 1 90  ? 29.758  22.458  47.167 1.00 47.16  ? 90  LYS   B CA  1 
ATOM   2972 C C   . LYS   B 1 90  ? 30.365  23.371  46.111 1.00 43.30  ? 90  LYS   B C   1 
ATOM   2973 O O   . LYS   B 1 90  ? 31.555  23.695  46.168 1.00 50.09  ? 90  LYS   B O   1 
ATOM   2974 C CB  . LYS   B 1 90  ? 29.605  23.197  48.497 1.00 47.99  ? 90  LYS   B CB  1 
ATOM   2975 C CG  . LYS   B 1 90  ? 28.524  24.276  48.478 1.00 52.28  ? 90  LYS   B CG  1 
ATOM   2976 C CD  . LYS   B 1 90  ? 28.202  24.774  49.882 1.00 66.41  ? 90  LYS   B CD  1 
ATOM   2977 C CE  . LYS   B 1 90  ? 27.082  25.807  49.877 1.00 66.73  ? 90  LYS   B CE  1 
ATOM   2978 N NZ  . LYS   B 1 90  ? 26.791  26.306  51.251 1.00 70.39  ? 90  LYS   B NZ  1 
ATOM   2979 N N   . VAL   B 1 91  ? 29.555  23.772  45.140 1.00 46.39  ? 91  VAL   B N   1 
ATOM   2980 C CA  . VAL   B 1 91  ? 30.046  24.531  44.000 1.00 50.47  ? 91  VAL   B CA  1 
ATOM   2981 C C   . VAL   B 1 91  ? 29.401  25.908  43.998 1.00 49.53  ? 91  VAL   B C   1 
ATOM   2982 O O   . VAL   B 1 91  ? 28.396  26.162  44.670 1.00 47.65  ? 91  VAL   B O   1 
ATOM   2983 C CB  . VAL   B 1 91  ? 29.798  23.797  42.665 1.00 52.28  ? 91  VAL   B CB  1 
ATOM   2984 C CG1 . VAL   B 1 91  ? 30.676  22.560  42.579 1.00 44.60  ? 91  VAL   B CG1 1 
ATOM   2985 C CG2 . VAL   B 1 91  ? 28.328  23.425  42.521 1.00 46.65  ? 91  VAL   B CG2 1 
ATOM   2986 N N   . ASP   B 1 92  ? 30.003  26.812  43.226 1.00 52.91  ? 92  ASP   B N   1 
ATOM   2987 C CA  . ASP   B 1 92  ? 29.590  28.207  43.218 1.00 58.68  ? 92  ASP   B CA  1 
ATOM   2988 C C   . ASP   B 1 92  ? 28.331  28.452  42.398 1.00 64.95  ? 92  ASP   B C   1 
ATOM   2989 O O   . ASP   B 1 92  ? 27.759  29.545  42.483 1.00 59.04  ? 92  ASP   B O   1 
ATOM   2990 C CB  . ASP   B 1 92  ? 30.730  29.082  42.686 1.00 53.99  ? 92  ASP   B CB  1 
ATOM   2991 C CG  . ASP   B 1 92  ? 31.108  28.742  41.257 1.00 67.15  ? 92  ASP   B CG  1 
ATOM   2992 O OD1 . ASP   B 1 92  ? 30.864  27.594  40.825 1.00 66.00  ? 92  ASP   B OD1 1 
ATOM   2993 O OD2 . ASP   B 1 92  ? 31.650  29.625  40.563 1.00 74.70  ? 92  ASP   B OD2 1 
ATOM   2994 N N   . THR   B 1 93  ? 27.881  27.468  41.625 1.00 59.16  ? 93  THR   B N   1 
ATOM   2995 C CA  . THR   B 1 93  ? 26.753  27.639  40.723 1.00 58.35  ? 93  THR   B CA  1 
ATOM   2996 C C   . THR   B 1 93  ? 25.735  26.539  40.974 1.00 54.68  ? 93  THR   B C   1 
ATOM   2997 O O   . THR   B 1 93  ? 26.081  25.355  40.942 1.00 55.89  ? 93  THR   B O   1 
ATOM   2998 C CB  . THR   B 1 93  ? 27.212  27.608  39.261 1.00 59.09  ? 93  THR   B CB  1 
ATOM   2999 O OG1 . THR   B 1 93  ? 28.224  28.603  39.055 1.00 63.12  ? 93  THR   B OG1 1 
ATOM   3000 C CG2 . THR   B 1 93  ? 26.045  27.873  38.324 1.00 59.92  ? 93  THR   B CG2 1 
ATOM   3001 N N   . ALA   B 1 94  ? 24.492  26.931  41.237 1.00 52.97  ? 94  ALA   B N   1 
ATOM   3002 C CA  . ALA   B 1 94  ? 23.405  25.964  41.260 1.00 51.59  ? 94  ALA   B CA  1 
ATOM   3003 C C   . ALA   B 1 94  ? 23.147  25.460  39.845 1.00 54.83  ? 94  ALA   B C   1 
ATOM   3004 O O   . ALA   B 1 94  ? 23.311  26.195  38.868 1.00 55.40  ? 94  ALA   B O   1 
ATOM   3005 C CB  . ALA   B 1 94  ? 22.141  26.589  41.846 1.00 51.66  ? 94  ALA   B CB  1 
ATOM   3006 N N   . ASN   B 1 95  ? 22.764  24.197  39.737 1.00 55.56  ? 95  ASN   B N   1 
ATOM   3007 C CA  . ASN   B 1 95  ? 22.516  23.590  38.434 1.00 50.03  ? 95  ASN   B CA  1 
ATOM   3008 C C   . ASN   B 1 95  ? 21.181  24.080  37.887 1.00 44.96  ? 95  ASN   B C   1 
ATOM   3009 O O   . ASN   B 1 95  ? 20.136  23.760  38.468 1.00 50.25  ? 95  ASN   B O   1 
ATOM   3010 C CB  . ASN   B 1 95  ? 22.541  22.062  38.560 1.00 45.65  ? 95  ASN   B CB  1 
ATOM   3011 C CG  . ASN   B 1 95  ? 22.368  21.348  37.223 1.00 52.05  ? 95  ASN   B CG  1 
ATOM   3012 O OD1 . ASN   B 1 95  ? 22.354  21.970  36.159 1.00 48.49  ? 95  ASN   B OD1 1 
ATOM   3013 N ND2 . ASN   B 1 95  ? 22.246  20.026  37.279 1.00 44.57  ? 95  ASN   B ND2 1 
ATOM   3014 N N   . PRO   B 1 96  ? 21.158  24.856  36.799 1.00 45.31  ? 96  PRO   B N   1 
ATOM   3015 C CA  . PRO   B 1 96  ? 19.879  25.373  36.287 1.00 49.33  ? 96  PRO   B CA  1 
ATOM   3016 C C   . PRO   B 1 96  ? 18.979  24.294  35.718 1.00 56.26  ? 96  PRO   B C   1 
ATOM   3017 O O   . PRO   B 1 96  ? 17.781  24.545  35.527 1.00 62.12  ? 96  PRO   B O   1 
ATOM   3018 C CB  . PRO   B 1 96  ? 20.314  26.362  35.199 1.00 44.94  ? 96  PRO   B CB  1 
ATOM   3019 C CG  . PRO   B 1 96  ? 21.637  25.840  34.732 1.00 53.55  ? 96  PRO   B CG  1 
ATOM   3020 C CD  . PRO   B 1 96  ? 22.298  25.242  35.948 1.00 51.01  ? 96  PRO   B CD  1 
ATOM   3021 N N   . LYS   B 1 97  ? 19.522  23.107  35.448 1.00 56.24  ? 97  LYS   B N   1 
ATOM   3022 C CA  . LYS   B 1 97  ? 18.781  21.971  34.924 1.00 51.41  ? 97  LYS   B CA  1 
ATOM   3023 C C   . LYS   B 1 97  ? 18.426  20.966  36.014 1.00 55.15  ? 97  LYS   B C   1 
ATOM   3024 O O   . LYS   B 1 97  ? 18.155  19.800  35.711 1.00 58.55  ? 97  LYS   B O   1 
ATOM   3025 C CB  . LYS   B 1 97  ? 19.595  21.298  33.816 1.00 48.11  ? 97  LYS   B CB  1 
ATOM   3026 C CG  . LYS   B 1 97  ? 20.072  22.272  32.741 1.00 43.87  ? 97  LYS   B CG  1 
ATOM   3027 C CD  . LYS   B 1 97  ? 21.273  21.747  31.958 1.00 61.17  ? 97  LYS   B CD  1 
ATOM   3028 C CE  . LYS   B 1 97  ? 20.881  20.696  30.927 1.00 65.14  ? 97  LYS   B CE  1 
ATOM   3029 N NZ  . LYS   B 1 97  ? 20.056  21.252  29.816 1.00 68.87  ? 97  LYS   B NZ  1 
ATOM   3030 N N   . THR   B 1 98  ? 18.432  21.389  37.274 1.00 53.48  ? 98  THR   B N   1 
ATOM   3031 C CA  . THR   B 1 98  ? 18.101  20.474  38.360 1.00 53.31  ? 98  THR   B CA  1 
ATOM   3032 C C   . THR   B 1 98  ? 16.636  20.069  38.258 1.00 53.72  ? 98  THR   B C   1 
ATOM   3033 O O   . THR   B 1 98  ? 15.761  20.939  38.167 1.00 52.27  ? 98  THR   B O   1 
ATOM   3034 C CB  . THR   B 1 98  ? 18.373  21.106  39.725 1.00 50.77  ? 98  THR   B CB  1 
ATOM   3035 O OG1 . THR   B 1 98  ? 19.774  21.360  39.870 1.00 52.62  ? 98  THR   B OG1 1 
ATOM   3036 C CG2 . THR   B 1 98  ? 17.928  20.175  40.836 1.00 47.92  ? 98  THR   B CG2 1 
ATOM   3037 N N   . PRO   B 1 99  ? 16.331  18.779  38.246 1.00 56.43  ? 99  PRO   B N   1 
ATOM   3038 C CA  . PRO   B 1 99  ? 14.940  18.335  38.233 1.00 50.74  ? 99  PRO   B CA  1 
ATOM   3039 C C   . PRO   B 1 99  ? 14.432  18.124  39.652 1.00 54.48  ? 99  PRO   B C   1 
ATOM   3040 O O   . PRO   B 1 99  ? 15.200  18.047  40.613 1.00 57.00  ? 99  PRO   B O   1 
ATOM   3041 C CB  . PRO   B 1 99  ? 15.024  17.001  37.483 1.00 58.37  ? 99  PRO   B CB  1 
ATOM   3042 C CG  . PRO   B 1 99  ? 16.344  16.451  37.932 1.00 57.78  ? 99  PRO   B CG  1 
ATOM   3043 C CD  . PRO   B 1 99  ? 17.265  17.651  38.086 1.00 55.22  ? 99  PRO   B CD  1 
ATOM   3044 N N   . LYS   B 1 100 ? 13.111  18.035  39.765 1.00 54.18  ? 100 LYS   B N   1 
ATOM   3045 C CA  . LYS   B 1 100 ? 12.510  17.582  41.009 1.00 55.32  ? 100 LYS   B CA  1 
ATOM   3046 C C   . LYS   B 1 100 ? 13.051  16.196  41.331 1.00 54.65  ? 100 LYS   B C   1 
ATOM   3047 O O   . LYS   B 1 100 ? 12.824  15.245  40.578 1.00 54.06  ? 100 LYS   B O   1 
ATOM   3048 C CB  . LYS   B 1 100 ? 10.987  17.562  40.875 1.00 62.10  ? 100 LYS   B CB  1 
ATOM   3049 C CG  . LYS   B 1 100 ? 10.235  17.590  42.199 1.00 66.65  ? 100 LYS   B CG  1 
ATOM   3050 C CD  . LYS   B 1 100 ? 8.757   17.893  41.983 1.00 71.98  ? 100 LYS   B CD  1 
ATOM   3051 C CE  . LYS   B 1 100 ? 8.025   18.103  43.303 1.00 73.26  ? 100 LYS   B CE  1 
ATOM   3052 N NZ  . LYS   B 1 100 ? 7.930   16.854  44.112 1.00 76.55  ? 100 LYS   B NZ  1 
ATOM   3053 N N   . TYR   B 1 101 ? 13.800  16.081  42.425 1.00 53.41  ? 101 TYR   B N   1 
ATOM   3054 C CA  . TYR   B 1 101 ? 14.513  14.846  42.711 1.00 51.69  ? 101 TYR   B CA  1 
ATOM   3055 C C   . TYR   B 1 101 ? 14.332  14.441  44.167 1.00 54.98  ? 101 TYR   B C   1 
ATOM   3056 O O   . TYR   B 1 101 ? 13.903  15.228  45.014 1.00 54.60  ? 101 TYR   B O   1 
ATOM   3057 C CB  . TYR   B 1 101 ? 16.008  14.973  42.384 1.00 52.11  ? 101 TYR   B CB  1 
ATOM   3058 C CG  . TYR   B 1 101 ? 16.775  15.853  43.344 1.00 47.87  ? 101 TYR   B CG  1 
ATOM   3059 C CD1 . TYR   B 1 101 ? 16.843  17.225  43.152 1.00 48.21  ? 101 TYR   B CD1 1 
ATOM   3060 C CD2 . TYR   B 1 101 ? 17.435  15.310  44.438 1.00 47.34  ? 101 TYR   B CD2 1 
ATOM   3061 C CE1 . TYR   B 1 101 ? 17.544  18.034  44.024 1.00 50.32  ? 101 TYR   B CE1 1 
ATOM   3062 C CE2 . TYR   B 1 101 ? 18.136  16.111  45.318 1.00 49.15  ? 101 TYR   B CE2 1 
ATOM   3063 C CZ  . TYR   B 1 101 ? 18.187  17.472  45.106 1.00 50.77  ? 101 TYR   B CZ  1 
ATOM   3064 O OH  . TYR   B 1 101 ? 18.887  18.273  45.978 1.00 52.74  ? 101 TYR   B OH  1 
ATOM   3065 N N   . LYS   B 1 102 ? 14.674  13.183  44.441 1.00 47.26  ? 102 LYS   B N   1 
ATOM   3066 C CA  . LYS   B 1 102 ? 14.701  12.654  45.794 1.00 51.54  ? 102 LYS   B CA  1 
ATOM   3067 C C   . LYS   B 1 102 ? 15.728  11.533  45.861 1.00 49.14  ? 102 LYS   B C   1 
ATOM   3068 O O   . LYS   B 1 102 ? 15.959  10.824  44.878 1.00 49.95  ? 102 LYS   B O   1 
ATOM   3069 C CB  . LYS   B 1 102 ? 13.325  12.143  46.240 1.00 53.27  ? 102 LYS   B CB  1 
ATOM   3070 C CG  . LYS   B 1 102 ? 13.275  11.748  47.710 1.00 66.21  ? 102 LYS   B CG  1 
ATOM   3071 C CD  . LYS   B 1 102 ? 13.890  12.839  48.591 1.00 67.65  ? 102 LYS   B CD  1 
ATOM   3072 C CE  . LYS   B 1 102 ? 14.451  12.263  49.890 1.00 73.61  ? 102 LYS   B CE  1 
ATOM   3073 N NZ  . LYS   B 1 102 ? 15.326  13.221  50.633 1.00 68.29  ? 102 LYS   B NZ  1 
ATOM   3074 N N   . PHE   B 1 103 ? 16.351  11.393  47.027 1.00 45.55  ? 103 PHE   B N   1 
ATOM   3075 C CA  . PHE   B 1 103 ? 17.290  10.313  47.288 1.00 43.46  ? 103 PHE   B CA  1 
ATOM   3076 C C   . PHE   B 1 103 ? 16.551  9.193   48.006 1.00 50.60  ? 103 PHE   B C   1 
ATOM   3077 O O   . PHE   B 1 103 ? 16.004  9.403   49.094 1.00 53.49  ? 103 PHE   B O   1 
ATOM   3078 C CB  . PHE   B 1 103 ? 18.471  10.801  48.128 1.00 44.52  ? 103 PHE   B CB  1 
ATOM   3079 C CG  . PHE   B 1 103 ? 19.375  11.769  47.413 1.00 47.24  ? 103 PHE   B CG  1 
ATOM   3080 C CD1 . PHE   B 1 103 ? 19.251  11.985  46.048 1.00 41.94  ? 103 PHE   B CD1 1 
ATOM   3081 C CD2 . PHE   B 1 103 ? 20.360  12.452  48.107 1.00 43.51  ? 103 PHE   B CD2 1 
ATOM   3082 C CE1 . PHE   B 1 103 ? 20.084  12.868  45.396 1.00 38.92  ? 103 PHE   B CE1 1 
ATOM   3083 C CE2 . PHE   B 1 103 ? 21.200  13.333  47.457 1.00 44.10  ? 103 PHE   B CE2 1 
ATOM   3084 C CZ  . PHE   B 1 103 ? 21.061  13.544  46.102 1.00 42.54  ? 103 PHE   B CZ  1 
ATOM   3085 N N   . VAL   B 1 104 ? 16.529  8.012   47.400 1.00 45.30  ? 104 VAL   B N   1 
ATOM   3086 C CA  . VAL   B 1 104 ? 15.819  6.869   47.957 1.00 47.82  ? 104 VAL   B CA  1 
ATOM   3087 C C   . VAL   B 1 104 ? 16.775  5.691   48.052 1.00 46.30  ? 104 VAL   B C   1 
ATOM   3088 O O   . VAL   B 1 104 ? 17.730  5.569   47.277 1.00 44.32  ? 104 VAL   B O   1 
ATOM   3089 C CB  . VAL   B 1 104 ? 14.576  6.493   47.120 1.00 44.18  ? 104 VAL   B CB  1 
ATOM   3090 C CG1 . VAL   B 1 104 ? 13.623  7.677   47.013 1.00 49.00  ? 104 VAL   B CG1 1 
ATOM   3091 C CG2 . VAL   B 1 104 ? 14.989  6.010   45.741 1.00 47.24  ? 104 VAL   B CG2 1 
ATOM   3092 N N   . ARG   B 1 105 ? 16.513  4.822   49.019 1.00 44.19  ? 105 ARG   B N   1 
ATOM   3093 C CA  . ARG   B 1 105 ? 17.246  3.573   49.169 1.00 46.08  ? 105 ARG   B CA  1 
ATOM   3094 C C   . ARG   B 1 105 ? 16.293  2.444   48.801 1.00 46.32  ? 105 ARG   B C   1 
ATOM   3095 O O   . ARG   B 1 105 ? 15.330  2.175   49.528 1.00 48.56  ? 105 ARG   B O   1 
ATOM   3096 C CB  . ARG   B 1 105 ? 17.791  3.410   50.583 1.00 42.51  ? 105 ARG   B CB  1 
ATOM   3097 C CG  . ARG   B 1 105 ? 18.670  2.191   50.737 1.00 45.50  ? 105 ARG   B CG  1 
ATOM   3098 C CD  . ARG   B 1 105 ? 19.310  2.162   52.101 1.00 47.96  ? 105 ARG   B CD  1 
ATOM   3099 N NE  . ARG   B 1 105 ? 20.187  1.011   52.262 1.00 47.18  ? 105 ARG   B NE  1 
ATOM   3100 C CZ  . ARG   B 1 105 ? 21.452  0.974   51.869 1.00 44.04  ? 105 ARG   B CZ  1 
ATOM   3101 N NH1 . ARG   B 1 105 ? 22.015  2.004   51.258 1.00 41.14  ? 105 ARG   B NH1 1 
ATOM   3102 N NH2 . ARG   B 1 105 ? 22.169  -0.122  52.094 1.00 40.38  ? 105 ARG   B NH2 1 
ATOM   3103 N N   . ILE   B 1 106 ? 16.556  1.795   47.668 1.00 47.08  ? 106 ILE   B N   1 
ATOM   3104 C CA  . ILE   B 1 106 ? 15.690  0.721   47.207 1.00 48.39  ? 106 ILE   B CA  1 
ATOM   3105 C C   . ILE   B 1 106 ? 15.990  -0.560  47.976 1.00 45.34  ? 106 ILE   B C   1 
ATOM   3106 O O   . ILE   B 1 106 ? 17.043  -0.723  48.599 1.00 49.07  ? 106 ILE   B O   1 
ATOM   3107 C CB  . ILE   B 1 106 ? 15.835  0.499   45.693 1.00 43.92  ? 106 ILE   B CB  1 
ATOM   3108 C CG1 . ILE   B 1 106 ? 17.285  0.137   45.367 1.00 43.54  ? 106 ILE   B CG1 1 
ATOM   3109 C CG2 . ILE   B 1 106 ? 15.365  1.719   44.919 1.00 46.94  ? 106 ILE   B CG2 1 
ATOM   3110 C CD1 . ILE   B 1 106 ? 17.456  -0.501  44.031 1.00 47.40  ? 106 ILE   B CD1 1 
ATOM   3111 N N   . GLN   B 1 107 ? 15.044  -1.490  47.907 1.00 44.16  ? 107 GLN   B N   1 
ATOM   3112 C CA  . GLN   B 1 107 ? 15.125  -2.801  48.522 1.00 49.64  ? 107 GLN   B CA  1 
ATOM   3113 C C   . GLN   B 1 107 ? 15.505  -3.848  47.485 1.00 48.69  ? 107 GLN   B C   1 
ATOM   3114 O O   . GLN   B 1 107 ? 15.219  -3.682  46.295 1.00 42.72  ? 107 GLN   B O   1 
ATOM   3115 C CB  . GLN   B 1 107 ? 13.788  -3.190  49.162 1.00 56.08  ? 107 GLN   B CB  1 
ATOM   3116 C CG  . GLN   B 1 107 ? 13.512  -2.511  50.491 1.00 55.76  ? 107 GLN   B CG  1 
ATOM   3117 C CD  . GLN   B 1 107 ? 13.178  -1.044  50.327 1.00 60.75  ? 107 GLN   B CD  1 
ATOM   3118 O OE1 . GLN   B 1 107 ? 13.675  -0.194  51.067 1.00 67.46  ? 107 GLN   B OE1 1 
ATOM   3119 N NE2 . GLN   B 1 107 ? 12.329  -0.737  49.351 1.00 56.98  ? 107 GLN   B NE2 1 
ATOM   3120 N N   . PRO   B 1 108 ? 16.149  -4.935  47.913 1.00 49.85  ? 108 PRO   B N   1 
ATOM   3121 C CA  . PRO   B 1 108 ? 16.463  -6.016  46.972 1.00 41.89  ? 108 PRO   B CA  1 
ATOM   3122 C C   . PRO   B 1 108 ? 15.206  -6.499  46.264 1.00 47.42  ? 108 PRO   B C   1 
ATOM   3123 O O   . PRO   B 1 108 ? 14.152  -6.677  46.877 1.00 46.77  ? 108 PRO   B O   1 
ATOM   3124 C CB  . PRO   B 1 108 ? 17.071  -7.106  47.865 1.00 49.20  ? 108 PRO   B CB  1 
ATOM   3125 C CG  . PRO   B 1 108 ? 16.680  -6.741  49.268 1.00 47.10  ? 108 PRO   B CG  1 
ATOM   3126 C CD  . PRO   B 1 108 ? 16.583  -5.249  49.285 1.00 46.60  ? 108 PRO   B CD  1 
ATOM   3127 N N   . GLY   B 1 109 ? 15.321  -6.684  44.950 1.00 44.96  ? 109 GLY   B N   1 
ATOM   3128 C CA  . GLY   B 1 109 ? 14.215  -7.062  44.113 1.00 45.98  ? 109 GLY   B CA  1 
ATOM   3129 C C   . GLY   B 1 109 ? 13.652  -5.924  43.284 1.00 42.73  ? 109 GLY   B C   1 
ATOM   3130 O O   . GLY   B 1 109 ? 13.044  -6.177  42.241 1.00 51.68  ? 109 GLY   B O   1 
ATOM   3131 N N   . GLN   B 1 110 ? 13.831  -4.683  43.727 1.00 42.42  ? 110 GLN   B N   1 
ATOM   3132 C CA  . GLN   B 1 110 ? 13.393  -3.547  42.934 1.00 40.54  ? 110 GLN   B CA  1 
ATOM   3133 C C   . GLN   B 1 110 ? 14.348  -3.311  41.767 1.00 43.68  ? 110 GLN   B C   1 
ATOM   3134 O O   . GLN   B 1 110 ? 15.510  -3.725  41.784 1.00 40.41  ? 110 GLN   B O   1 
ATOM   3135 C CB  . GLN   B 1 110 ? 13.300  -2.284  43.789 1.00 51.99  ? 110 GLN   B CB  1 
ATOM   3136 C CG  . GLN   B 1 110 ? 12.158  -2.275  44.794 1.00 58.18  ? 110 GLN   B CG  1 
ATOM   3137 C CD  . GLN   B 1 110 ? 11.817  -0.871  45.256 1.00 59.85  ? 110 GLN   B CD  1 
ATOM   3138 O OE1 . GLN   B 1 110 ? 12.177  -0.462  46.362 1.00 53.67  ? 110 GLN   B OE1 1 
ATOM   3139 N NE2 . GLN   B 1 110 ? 11.127  -0.118  44.402 1.00 48.96  ? 110 GLN   B NE2 1 
ATOM   3140 N N   . THR   B 1 111 ? 13.836  -2.636  40.743 1.00 38.03  ? 111 THR   B N   1 
ATOM   3141 C CA  . THR   B 1 111 ? 14.592  -2.325  39.543 1.00 40.93  ? 111 THR   B CA  1 
ATOM   3142 C C   . THR   B 1 111 ? 14.805  -0.822  39.425 1.00 44.10  ? 111 THR   B C   1 
ATOM   3143 O O   . THR   B 1 111 ? 14.134  -0.017  40.080 1.00 38.42  ? 111 THR   B O   1 
ATOM   3144 C CB  . THR   B 1 111 ? 13.877  -2.840  38.290 1.00 45.23  ? 111 THR   B CB  1 
ATOM   3145 O OG1 . THR   B 1 111 ? 12.612  -2.179  38.156 1.00 43.91  ? 111 THR   B OG1 1 
ATOM   3146 C CG2 . THR   B 1 111 ? 13.654  -4.341  38.379 1.00 48.19  ? 111 THR   B CG2 1 
ATOM   3147 N N   . PHE   B 1 112 ? 15.750  -0.451  38.567 1.00 35.48  ? 112 PHE   B N   1 
ATOM   3148 C CA  . PHE   B 1 112 ? 16.030  0.951   38.298 1.00 37.26  ? 112 PHE   B CA  1 
ATOM   3149 C C   . PHE   B 1 112 ? 16.771  1.051   36.974 1.00 36.32  ? 112 PHE   B C   1 
ATOM   3150 O O   . PHE   B 1 112 ? 17.332  0.069   36.479 1.00 38.40  ? 112 PHE   B O   1 
ATOM   3151 C CB  . PHE   B 1 112 ? 16.840  1.589   39.434 1.00 35.60  ? 112 PHE   B CB  1 
ATOM   3152 C CG  . PHE   B 1 112 ? 18.095  0.839   39.782 1.00 37.37  ? 112 PHE   B CG  1 
ATOM   3153 C CD1 . PHE   B 1 112 ? 18.063  -0.220  40.672 1.00 43.71  ? 112 PHE   B CD1 1 
ATOM   3154 C CD2 . PHE   B 1 112 ? 19.308  1.194   39.218 1.00 37.50  ? 112 PHE   B CD2 1 
ATOM   3155 C CE1 . PHE   B 1 112 ? 19.217  -0.914  40.993 1.00 38.47  ? 112 PHE   B CE1 1 
ATOM   3156 C CE2 . PHE   B 1 112 ? 20.464  0.508   39.538 1.00 38.91  ? 112 PHE   B CE2 1 
ATOM   3157 C CZ  . PHE   B 1 112 ? 20.419  -0.547  40.426 1.00 41.56  ? 112 PHE   B CZ  1 
ATOM   3158 N N   . SER   B 1 113 ? 16.744  2.247   36.399 1.00 33.11  ? 113 SER   B N   1 
ATOM   3159 C CA  . SER   B 1 113 ? 17.503  2.547   35.195 1.00 36.84  ? 113 SER   B CA  1 
ATOM   3160 C C   . SER   B 1 113 ? 18.889  3.046   35.579 1.00 40.10  ? 113 SER   B C   1 
ATOM   3161 O O   . SER   B 1 113 ? 19.050  3.753   36.576 1.00 40.19  ? 113 SER   B O   1 
ATOM   3162 C CB  . SER   B 1 113 ? 16.792  3.604   34.346 1.00 37.49  ? 113 SER   B CB  1 
ATOM   3163 O OG  . SER   B 1 113 ? 15.557  3.130   33.848 1.00 37.54  ? 113 SER   B OG  1 
ATOM   3164 N N   . VAL   B 1 114 ? 19.885  2.679   34.778 1.00 36.91  ? 114 VAL   B N   1 
ATOM   3165 C CA  . VAL   B 1 114 ? 21.267  3.094   34.982 1.00 29.75  ? 114 VAL   B CA  1 
ATOM   3166 C C   . VAL   B 1 114 ? 21.694  3.913   33.777 1.00 37.47  ? 114 VAL   B C   1 
ATOM   3167 O O   . VAL   B 1 114 ? 21.515  3.479   32.632 1.00 30.99  ? 114 VAL   B O   1 
ATOM   3168 C CB  . VAL   B 1 114 ? 22.203  1.887   35.180 1.00 36.38  ? 114 VAL   B CB  1 
ATOM   3169 C CG1 . VAL   B 1 114 ? 23.660  2.304   35.029 1.00 32.70  ? 114 VAL   B CG1 1 
ATOM   3170 C CG2 . VAL   B 1 114 ? 21.971  1.258   36.538 1.00 37.13  ? 114 VAL   B CG2 1 
ATOM   3171 N N   . LEU   B 1 115 ? 22.243  5.098   34.031 1.00 33.47  ? 115 LEU   B N   1 
ATOM   3172 C CA  . LEU   B 1 115 ? 22.821  5.934   32.986 1.00 28.10  ? 115 LEU   B CA  1 
ATOM   3173 C C   . LEU   B 1 115 ? 24.337  5.813   33.091 1.00 33.12  ? 115 LEU   B C   1 
ATOM   3174 O O   . LEU   B 1 115 ? 24.973  6.504   33.891 1.00 27.06  ? 115 LEU   B O   1 
ATOM   3175 C CB  . LEU   B 1 115 ? 22.359  7.380   33.117 1.00 39.23  ? 115 LEU   B CB  1 
ATOM   3176 C CG  . LEU   B 1 115 ? 22.890  8.329   32.041 1.00 37.94  ? 115 LEU   B CG  1 
ATOM   3177 C CD1 . LEU   B 1 115 ? 22.479  7.853   30.654 1.00 43.65  ? 115 LEU   B CD1 1 
ATOM   3178 C CD2 . LEU   B 1 115 ? 22.413  9.753   32.287 1.00 37.27  ? 115 LEU   B CD2 1 
ATOM   3179 N N   . ALA   B 1 116 ? 24.912  4.919   32.288 1.00 31.97  ? 116 ALA   B N   1 
ATOM   3180 C CA  . ALA   B 1 116 ? 26.357  4.734   32.281 1.00 41.05  ? 116 ALA   B CA  1 
ATOM   3181 C C   . ALA   B 1 116 ? 27.040  5.964   31.692 1.00 35.73  ? 116 ALA   B C   1 
ATOM   3182 O O   . ALA   B 1 116 ? 26.725  6.385   30.574 1.00 40.26  ? 116 ALA   B O   1 
ATOM   3183 C CB  . ALA   B 1 116 ? 26.726  3.483   31.486 1.00 34.21  ? 116 ALA   B CB  1 
ATOM   3184 N N   . CYS   B 1 117 ? 27.975  6.542   32.448 1.00 33.41  ? 117 CYS   B N   1 
ATOM   3185 C CA  . CYS   B 1 117 ? 28.665  7.758   32.043 1.00 35.13  ? 117 CYS   B CA  1 
ATOM   3186 C C   . CYS   B 1 117 ? 30.174  7.569   32.083 1.00 39.75  ? 117 CYS   B C   1 
ATOM   3187 O O   . CYS   B 1 117 ? 30.702  6.748   32.841 1.00 38.44  ? 117 CYS   B O   1 
ATOM   3188 C CB  . CYS   B 1 117 ? 28.290  8.948   32.933 1.00 37.91  ? 117 CYS   B CB  1 
ATOM   3189 S SG  . CYS   B 1 117 ? 26.600  9.532   32.742 1.00 45.94  ? 117 CYS   B SG  1 
ATOM   3190 N N   . TYR   B 1 118 ? 30.858  8.357   31.253 1.00 36.53  ? 118 TYR   B N   1 
ATOM   3191 C CA  . TYR   B 1 118 ? 32.310  8.415   31.197 1.00 35.66  ? 118 TYR   B CA  1 
ATOM   3192 C C   . TYR   B 1 118 ? 32.715  9.862   30.967 1.00 39.52  ? 118 TYR   B C   1 
ATOM   3193 O O   . TYR   B 1 118 ? 32.206  10.511  30.048 1.00 38.20  ? 118 TYR   B O   1 
ATOM   3194 C CB  . TYR   B 1 118 ? 32.854  7.506   30.087 1.00 37.91  ? 118 TYR   B CB  1 
ATOM   3195 C CG  . TYR   B 1 118 ? 32.487  6.061   30.309 1.00 37.50  ? 118 TYR   B CG  1 
ATOM   3196 C CD1 . TYR   B 1 118 ? 33.274  5.246   31.110 1.00 32.82  ? 118 TYR   B CD1 1 
ATOM   3197 C CD2 . TYR   B 1 118 ? 31.333  5.519   29.752 1.00 37.73  ? 118 TYR   B CD2 1 
ATOM   3198 C CE1 . TYR   B 1 118 ? 32.938  3.928   31.336 1.00 33.30  ? 118 TYR   B CE1 1 
ATOM   3199 C CE2 . TYR   B 1 118 ? 30.985  4.196   29.975 1.00 39.28  ? 118 TYR   B CE2 1 
ATOM   3200 C CZ  . TYR   B 1 118 ? 31.792  3.406   30.769 1.00 36.03  ? 118 TYR   B CZ  1 
ATOM   3201 O OH  . TYR   B 1 118 ? 31.459  2.089   30.999 1.00 33.45  ? 118 TYR   B OH  1 
ATOM   3202 N N   . ASN   B 1 119 ? 33.595  10.373  31.829 1.00 41.21  ? 119 ASN   B N   1 
ATOM   3203 C CA  . ASN   B 1 119 ? 34.086  11.751  31.746 1.00 37.17  ? 119 ASN   B CA  1 
ATOM   3204 C C   . ASN   B 1 119 ? 32.944  12.760  31.790 1.00 42.54  ? 119 ASN   B C   1 
ATOM   3205 O O   . ASN   B 1 119 ? 32.998  13.821  31.164 1.00 36.39  ? 119 ASN   B O   1 
ATOM   3206 C CB  . ASN   B 1 119 ? 34.948  11.953  30.502 1.00 42.90  ? 119 ASN   B CB  1 
ATOM   3207 C CG  . ASN   B 1 119 ? 36.201  11.113  30.535 1.00 53.00  ? 119 ASN   B CG  1 
ATOM   3208 O OD1 . ASN   B 1 119 ? 37.176  11.459  31.203 1.00 58.17  ? 119 ASN   B OD1 1 
ATOM   3209 N ND2 . ASN   B 1 119 ? 36.177  9.992   29.828 1.00 55.22  ? 119 ASN   B ND2 1 
ATOM   3210 N N   . GLY   B 1 120 ? 31.905  12.435  32.555 1.00 37.67  ? 120 GLY   B N   1 
ATOM   3211 C CA  . GLY   B 1 120 ? 30.764  13.308  32.688 1.00 42.46  ? 120 GLY   B CA  1 
ATOM   3212 C C   . GLY   B 1 120 ? 29.812  13.301  31.514 1.00 39.65  ? 120 GLY   B C   1 
ATOM   3213 O O   . GLY   B 1 120 ? 28.857  14.090  31.512 1.00 40.40  ? 120 GLY   B O   1 
ATOM   3214 N N   . SER   B 1 121 ? 30.033  12.441  30.520 1.00 37.65  ? 121 SER   B N   1 
ATOM   3215 C CA  . SER   B 1 121 ? 29.167  12.374  29.355 1.00 40.34  ? 121 SER   B CA  1 
ATOM   3216 C C   . SER   B 1 121 ? 28.450  11.035  29.308 1.00 43.62  ? 121 SER   B C   1 
ATOM   3217 O O   . SER   B 1 121 ? 29.098  9.985   29.405 1.00 40.40  ? 121 SER   B O   1 
ATOM   3218 C CB  . SER   B 1 121 ? 29.970  12.582  28.065 1.00 41.15  ? 121 SER   B CB  1 
ATOM   3219 O OG  . SER   B 1 121 ? 30.639  13.835  28.083 1.00 48.70  ? 121 SER   B OG  1 
ATOM   3220 N N   . PRO   B 1 122 ? 27.127  11.036  29.157 1.00 49.25  ? 122 PRO   B N   1 
ATOM   3221 C CA  . PRO   B 1 122 ? 26.382  9.770   29.128 1.00 45.82  ? 122 PRO   B CA  1 
ATOM   3222 C C   . PRO   B 1 122 ? 26.726  8.927   27.909 1.00 44.75  ? 122 PRO   B C   1 
ATOM   3223 O O   . PRO   B 1 122 ? 26.873  9.437   26.796 1.00 45.02  ? 122 PRO   B O   1 
ATOM   3224 C CB  . PRO   B 1 122 ? 24.918  10.225  29.092 1.00 49.02  ? 122 PRO   B CB  1 
ATOM   3225 C CG  . PRO   B 1 122 ? 24.940  11.621  29.662 1.00 50.46  ? 122 PRO   B CG  1 
ATOM   3226 C CD  . PRO   B 1 122 ? 26.237  12.208  29.195 1.00 45.86  ? 122 PRO   B CD  1 
ATOM   3227 N N   . SER   B 1 123 ? 26.846  7.619   28.135 1.00 41.73  ? 123 SER   B N   1 
ATOM   3228 C CA  . SER   B 1 123 ? 27.109  6.644   27.083 1.00 37.58  ? 123 SER   B CA  1 
ATOM   3229 C C   . SER   B 1 123 ? 25.897  5.807   26.714 1.00 40.41  ? 123 SER   B C   1 
ATOM   3230 O O   . SER   B 1 123 ? 25.734  5.457   25.543 1.00 42.62  ? 123 SER   B O   1 
ATOM   3231 C CB  . SER   B 1 123 ? 28.244  5.701   27.499 1.00 38.27  ? 123 SER   B CB  1 
ATOM   3232 O OG  . SER   B 1 123 ? 28.331  4.592   26.614 1.00 46.57  ? 123 SER   B OG  1 
ATOM   3233 N N   . GLY   B 1 124 ? 25.053  5.460   27.678 1.00 37.62  ? 124 GLY   B N   1 
ATOM   3234 C CA  . GLY   B 1 124 ? 23.941  4.569   27.400 1.00 38.39  ? 124 GLY   B CA  1 
ATOM   3235 C C   . GLY   B 1 124 ? 23.096  4.379   28.639 1.00 39.35  ? 124 GLY   B C   1 
ATOM   3236 O O   . GLY   B 1 124 ? 23.479  4.763   29.749 1.00 35.25  ? 124 GLY   B O   1 
ATOM   3237 N N   . VAL   B 1 125 ? 21.931  3.771   28.434 1.00 36.01  ? 125 VAL   B N   1 
ATOM   3238 C CA  . VAL   B 1 125 ? 20.976  3.557   29.514 1.00 38.23  ? 125 VAL   B CA  1 
ATOM   3239 C C   . VAL   B 1 125 ? 20.424  2.140   29.416 1.00 40.21  ? 125 VAL   B C   1 
ATOM   3240 O O   . VAL   B 1 125 ? 20.224  1.611   28.317 1.00 37.72  ? 125 VAL   B O   1 
ATOM   3241 C CB  . VAL   B 1 125 ? 19.852  4.617   29.484 1.00 36.30  ? 125 VAL   B CB  1 
ATOM   3242 C CG1 . VAL   B 1 125 ? 19.047  4.521   28.198 1.00 39.08  ? 125 VAL   B CG1 1 
ATOM   3243 C CG2 . VAL   B 1 125 ? 18.962  4.502   30.716 1.00 41.19  ? 125 VAL   B CG2 1 
ATOM   3244 N N   . TYR   B 1 126 ? 20.205  1.515   30.575 1.00 36.45  ? 126 TYR   B N   1 
ATOM   3245 C CA  . TYR   B 1 126 ? 19.680  0.157   30.634 1.00 34.93  ? 126 TYR   B CA  1 
ATOM   3246 C C   . TYR   B 1 126 ? 19.062  -0.082  32.004 1.00 40.93  ? 126 TYR   B C   1 
ATOM   3247 O O   . TYR   B 1 126 ? 19.313  0.660   32.957 1.00 35.10  ? 126 TYR   B O   1 
ATOM   3248 C CB  . TYR   B 1 126 ? 20.773  -0.882  30.344 1.00 39.71  ? 126 TYR   B CB  1 
ATOM   3249 C CG  . TYR   B 1 126 ? 21.997  -0.780  31.234 1.00 39.86  ? 126 TYR   B CG  1 
ATOM   3250 C CD1 . TYR   B 1 126 ? 22.064  -1.463  32.439 1.00 37.15  ? 126 TYR   B CD1 1 
ATOM   3251 C CD2 . TYR   B 1 126 ? 23.090  -0.008  30.860 1.00 40.23  ? 126 TYR   B CD2 1 
ATOM   3252 C CE1 . TYR   B 1 126 ? 23.178  -1.376  33.250 1.00 40.50  ? 126 TYR   B CE1 1 
ATOM   3253 C CE2 . TYR   B 1 126 ? 24.211  0.083   31.666 1.00 39.37  ? 126 TYR   B CE2 1 
ATOM   3254 C CZ  . TYR   B 1 126 ? 24.249  -0.603  32.857 1.00 30.92  ? 126 TYR   B CZ  1 
ATOM   3255 O OH  . TYR   B 1 126 ? 25.359  -0.518  33.664 1.00 40.33  ? 126 TYR   B OH  1 
ATOM   3256 N N   . GLN   B 1 127 ? 18.255  -1.141  32.091 1.00 36.66  ? 127 GLN   B N   1 
ATOM   3257 C CA  . GLN   B 1 127 ? 17.560  -1.499  33.322 1.00 41.10  ? 127 GLN   B CA  1 
ATOM   3258 C C   . GLN   B 1 127 ? 18.390  -2.463  34.154 1.00 42.88  ? 127 GLN   B C   1 
ATOM   3259 O O   . GLN   B 1 127 ? 19.037  -3.369  33.621 1.00 38.91  ? 127 GLN   B O   1 
ATOM   3260 C CB  . GLN   B 1 127 ? 16.204  -2.140  33.022 1.00 40.76  ? 127 GLN   B CB  1 
ATOM   3261 C CG  . GLN   B 1 127 ? 15.085  -1.158  32.802 1.00 48.95  ? 127 GLN   B CG  1 
ATOM   3262 C CD  . GLN   B 1 127 ? 14.645  -0.462  34.077 1.00 46.26  ? 127 GLN   B CD  1 
ATOM   3263 O OE1 . GLN   B 1 127 ? 14.885  0.731   34.260 1.00 44.02  ? 127 GLN   B OE1 1 
ATOM   3264 N NE2 . GLN   B 1 127 ? 13.982  -1.201  34.959 1.00 45.42  ? 127 GLN   B NE2 1 
ATOM   3265 N N   . CYS   B 1 128 ? 18.356  -2.266  35.469 1.00 36.44  ? 128 CYS   B N   1 
ATOM   3266 C CA  . CYS   B 1 128 ? 19.033  -3.139  36.414 1.00 39.02  ? 128 CYS   B CA  1 
ATOM   3267 C C   . CYS   B 1 128 ? 18.097  -3.427  37.575 1.00 42.48  ? 128 CYS   B C   1 
ATOM   3268 O O   . CYS   B 1 128 ? 17.202  -2.640  37.886 1.00 40.27  ? 128 CYS   B O   1 
ATOM   3269 C CB  . CYS   B 1 128 ? 20.329  -2.514  36.942 1.00 38.87  ? 128 CYS   B CB  1 
ATOM   3270 S SG  . CYS   B 1 128 ? 21.829  -3.181  36.205 1.00 54.72  ? 128 CYS   B SG  1 
ATOM   3271 N N   . ALA   B 1 129 ? 18.308  -4.570  38.214 1.00 41.37  ? 129 ALA   B N   1 
ATOM   3272 C CA  . ALA   B 1 129 ? 17.596  -4.910  39.435 1.00 42.57  ? 129 ALA   B CA  1 
ATOM   3273 C C   . ALA   B 1 129 ? 18.596  -5.100  40.563 1.00 45.01  ? 129 ALA   B C   1 
ATOM   3274 O O   . ALA   B 1 129 ? 19.658  -5.705  40.372 1.00 40.10  ? 129 ALA   B O   1 
ATOM   3275 C CB  . ALA   B 1 129 ? 16.748  -6.176  39.266 1.00 40.30  ? 129 ALA   B CB  1 
ATOM   3276 N N   . MET   B 1 130 ? 18.260  -4.561  41.731 1.00 40.32  ? 130 MET   B N   1 
ATOM   3277 C CA  . MET   B 1 130 ? 19.020  -4.849  42.938 1.00 39.96  ? 130 MET   B CA  1 
ATOM   3278 C C   . MET   B 1 130 ? 18.850  -6.326  43.269 1.00 39.54  ? 130 MET   B C   1 
ATOM   3279 O O   . MET   B 1 130 ? 17.743  -6.777  43.578 1.00 43.09  ? 130 MET   B O   1 
ATOM   3280 C CB  . MET   B 1 130 ? 18.546  -3.964  44.086 1.00 42.06  ? 130 MET   B CB  1 
ATOM   3281 C CG  . MET   B 1 130 ? 19.296  -4.181  45.379 1.00 40.56  ? 130 MET   B CG  1 
ATOM   3282 S SD  . MET   B 1 130 ? 21.055  -3.849  45.197 1.00 45.54  ? 130 MET   B SD  1 
ATOM   3283 C CE  . MET   B 1 130 ? 21.022  -2.132  44.691 1.00 40.87  ? 130 MET   B CE  1 
ATOM   3284 N N   . ARG   B 1 131 ? 19.933  -7.091  43.169 1.00 44.80  ? 131 ARG   B N   1 
ATOM   3285 C CA  . ARG   B 1 131 ? 19.863  -8.506  43.462 1.00 37.83  ? 131 ARG   B CA  1 
ATOM   3286 C C   . ARG   B 1 131 ? 19.662  -8.720  44.960 1.00 42.44  ? 131 ARG   B C   1 
ATOM   3287 O O   . ARG   B 1 131 ? 19.976  -7.846  45.772 1.00 39.93  ? 131 ARG   B O   1 
ATOM   3288 C CB  . ARG   B 1 131 ? 21.134  -9.221  43.004 1.00 38.70  ? 131 ARG   B CB  1 
ATOM   3289 C CG  . ARG   B 1 131 ? 21.454  -9.109  41.520 1.00 37.61  ? 131 ARG   B CG  1 
ATOM   3290 C CD  . ARG   B 1 131 ? 20.328  -9.631  40.645 1.00 45.26  ? 131 ARG   B CD  1 
ATOM   3291 N NE  . ARG   B 1 131 ? 19.952  -10.999 40.981 1.00 43.52  ? 131 ARG   B NE  1 
ATOM   3292 C CZ  . ARG   B 1 131 ? 18.852  -11.596 40.545 1.00 47.48  ? 131 ARG   B CZ  1 
ATOM   3293 N NH1 . ARG   B 1 131 ? 18.011  -10.981 39.729 1.00 45.09  ? 131 ARG   B NH1 1 
ATOM   3294 N NH2 . ARG   B 1 131 ? 18.585  -12.839 40.944 1.00 49.20  ? 131 ARG   B NH2 1 
ATOM   3295 N N   . PRO   B 1 132 ? 19.125  -9.878  45.348 1.00 45.52  ? 132 PRO   B N   1 
ATOM   3296 C CA  . PRO   B 1 132 ? 19.019  -10.185 46.783 1.00 47.99  ? 132 PRO   B CA  1 
ATOM   3297 C C   . PRO   B 1 132 ? 20.342  -10.108 47.532 1.00 48.61  ? 132 PRO   B C   1 
ATOM   3298 O O   . PRO   B 1 132 ? 20.337  -9.779  48.725 1.00 46.26  ? 132 PRO   B O   1 
ATOM   3299 C CB  . PRO   B 1 132 ? 18.439  -11.604 46.781 1.00 49.13  ? 132 PRO   B CB  1 
ATOM   3300 C CG  . PRO   B 1 132 ? 17.603  -11.641 45.530 1.00 50.42  ? 132 PRO   B CG  1 
ATOM   3301 C CD  . PRO   B 1 132 ? 18.388  -10.848 44.515 1.00 47.41  ? 132 PRO   B CD  1 
ATOM   3302 N N   . ASN   B 1 133 ? 21.475  -10.381 46.877 1.00 46.09  ? 133 ASN   B N   1 
ATOM   3303 C CA  . ASN   B 1 133 ? 22.781  -10.234 47.514 1.00 44.27  ? 133 ASN   B CA  1 
ATOM   3304 C C   . ASN   B 1 133 ? 23.348  -8.819  47.386 1.00 39.54  ? 133 ASN   B C   1 
ATOM   3305 O O   . ASN   B 1 133 ? 24.545  -8.620  47.629 1.00 39.94  ? 133 ASN   B O   1 
ATOM   3306 C CB  . ASN   B 1 133 ? 23.775  -11.261 46.954 1.00 43.71  ? 133 ASN   B CB  1 
ATOM   3307 C CG  . ASN   B 1 133 ? 24.053  -11.076 45.467 1.00 45.76  ? 133 ASN   B CG  1 
ATOM   3308 O OD1 . ASN   B 1 133 ? 23.543  -10.153 44.832 1.00 38.57  ? 133 ASN   B OD1 1 
ATOM   3309 N ND2 . ASN   B 1 133 ? 24.879  -11.958 44.910 1.00 38.51  ? 133 ASN   B ND2 1 
ATOM   3310 N N   . PHE   B 1 134 ? 22.514  -7.849  46.995 1.00 36.71  ? 134 PHE   B N   1 
ATOM   3311 C CA  . PHE   B 1 134 ? 22.848  -6.421  46.962 1.00 43.73  ? 134 PHE   B CA  1 
ATOM   3312 C C   . PHE   B 1 134 ? 23.908  -6.079  45.919 1.00 43.81  ? 134 PHE   B C   1 
ATOM   3313 O O   . PHE   B 1 134 ? 24.626  -5.084  46.055 1.00 37.46  ? 134 PHE   B O   1 
ATOM   3314 C CB  . PHE   B 1 134 ? 23.274  -5.911  48.341 1.00 43.56  ? 134 PHE   B CB  1 
ATOM   3315 C CG  . PHE   B 1 134 ? 22.173  -5.947  49.350 1.00 42.08  ? 134 PHE   B CG  1 
ATOM   3316 C CD1 . PHE   B 1 134 ? 21.229  -4.935  49.398 1.00 49.28  ? 134 PHE   B CD1 1 
ATOM   3317 C CD2 . PHE   B 1 134 ? 22.065  -7.008  50.233 1.00 46.04  ? 134 PHE   B CD2 1 
ATOM   3318 C CE1 . PHE   B 1 134 ? 20.201  -4.973  50.321 1.00 53.46  ? 134 PHE   B CE1 1 
ATOM   3319 C CE2 . PHE   B 1 134 ? 21.042  -7.054  51.158 1.00 42.73  ? 134 PHE   B CE2 1 
ATOM   3320 C CZ  . PHE   B 1 134 ? 20.108  -6.033  51.202 1.00 48.31  ? 134 PHE   B CZ  1 
ATOM   3321 N N   . THR   B 1 135 ? 24.004  -6.882  44.867 1.00 44.47  ? 135 THR   B N   1 
ATOM   3322 C CA  . THR   B 1 135 ? 24.778  -6.538  43.685 1.00 39.51  ? 135 THR   B CA  1 
ATOM   3323 C C   . THR   B 1 135 ? 23.830  -6.190  42.548 1.00 38.38  ? 135 THR   B C   1 
ATOM   3324 O O   . THR   B 1 135 ? 22.609  -6.336  42.654 1.00 40.79  ? 135 THR   B O   1 
ATOM   3325 C CB  . THR   B 1 135 ? 25.694  -7.691  43.263 1.00 38.97  ? 135 THR   B CB  1 
ATOM   3326 O OG1 . THR   B 1 135 ? 24.906  -8.865  43.027 1.00 37.71  ? 135 THR   B OG1 1 
ATOM   3327 C CG2 . THR   B 1 135 ? 26.728  -7.975  44.336 1.00 40.87  ? 135 THR   B CG2 1 
ATOM   3328 N N   . ILE   B 1 136 ? 24.405  -5.720  41.448 1.00 35.91  ? 136 ILE   B N   1 
ATOM   3329 C CA  . ILE   B 1 136 ? 23.668  -5.556  40.204 1.00 35.58  ? 136 ILE   B CA  1 
ATOM   3330 C C   . ILE   B 1 136 ? 24.493  -6.165  39.078 1.00 36.37  ? 136 ILE   B C   1 
ATOM   3331 O O   . ILE   B 1 136 ? 25.728  -6.179  39.137 1.00 38.51  ? 136 ILE   B O   1 
ATOM   3332 C CB  . ILE   B 1 136 ? 23.320  -4.076  39.921 1.00 37.38  ? 136 ILE   B CB  1 
ATOM   3333 C CG1 . ILE   B 1 136 ? 24.572  -3.227  39.719 1.00 36.62  ? 136 ILE   B CG1 1 
ATOM   3334 C CG2 . ILE   B 1 136 ? 22.493  -3.488  41.063 1.00 40.27  ? 136 ILE   B CG2 1 
ATOM   3335 C CD1 . ILE   B 1 136 ? 24.251  -1.802  39.306 1.00 32.75  ? 136 ILE   B CD1 1 
ATOM   3336 N N   . LYS   B 1 137 ? 23.805  -6.719  38.078 1.00 40.18  ? 137 LYS   B N   1 
ATOM   3337 C CA  . LYS   B 1 137 ? 24.452  -7.269  36.886 1.00 45.11  ? 137 LYS   B CA  1 
ATOM   3338 C C   . LYS   B 1 137 ? 24.399  -6.197  35.803 1.00 31.62  ? 137 LYS   B C   1 
ATOM   3339 O O   . LYS   B 1 137 ? 23.535  -6.192  34.925 1.00 38.57  ? 137 LYS   B O   1 
ATOM   3340 C CB  . LYS   B 1 137 ? 23.769  -8.554  36.430 1.00 43.89  ? 137 LYS   B CB  1 
ATOM   3341 C CG  . LYS   B 1 137 ? 23.932  -9.753  37.349 1.00 46.42  ? 137 LYS   B CG  1 
ATOM   3342 C CD  . LYS   B 1 137 ? 23.143  -10.945 36.808 1.00 55.16  ? 137 LYS   B CD  1 
ATOM   3343 C CE  . LYS   B 1 137 ? 23.155  -12.123 37.772 1.00 60.93  ? 137 LYS   B CE  1 
ATOM   3344 N NZ  . LYS   B 1 137 ? 24.501  -12.754 37.864 1.00 70.24  ? 137 LYS   B NZ  1 
ATOM   3345 N N   . GLY   B 1 138 ? 25.346  -5.263  35.881 1.00 36.31  ? 138 GLY   B N   1 
ATOM   3346 C CA  . GLY   B 1 138 ? 25.372  -4.116  35.003 1.00 38.67  ? 138 GLY   B CA  1 
ATOM   3347 C C   . GLY   B 1 138 ? 26.429  -4.223  33.917 1.00 37.12  ? 138 GLY   B C   1 
ATOM   3348 O O   . GLY   B 1 138 ? 27.014  -5.278  33.666 1.00 36.42  ? 138 GLY   B O   1 
ATOM   3349 N N   . SER   B 1 139 ? 26.663  -3.092  33.258 1.00 39.07  ? 139 SER   B N   1 
ATOM   3350 C CA  . SER   B 1 139 ? 27.677  -2.973  32.212 1.00 35.49  ? 139 SER   B CA  1 
ATOM   3351 C C   . SER   B 1 139 ? 28.464  -1.698  32.492 1.00 32.39  ? 139 SER   B C   1 
ATOM   3352 O O   . SER   B 1 139 ? 28.021  -0.595  32.157 1.00 35.02  ? 139 SER   B O   1 
ATOM   3353 C CB  . SER   B 1 139 ? 27.043  -2.953  30.825 1.00 39.39  ? 139 SER   B CB  1 
ATOM   3354 O OG  . SER   B 1 139 ? 28.029  -2.819  29.818 1.00 40.45  ? 139 SER   B OG  1 
ATOM   3355 N N   . PHE   B 1 140 ? 29.621  -1.849  33.123 1.00 32.37  ? 140 PHE   B N   1 
ATOM   3356 C CA  . PHE   B 1 140 ? 30.465  -0.729  33.510 1.00 39.22  ? 140 PHE   B CA  1 
ATOM   3357 C C   . PHE   B 1 140 ? 31.908  -1.021  33.119 1.00 41.02  ? 140 PHE   B C   1 
ATOM   3358 O O   . PHE   B 1 140 ? 32.393  -2.146  33.291 1.00 36.79  ? 140 PHE   B O   1 
ATOM   3359 C CB  . PHE   B 1 140 ? 30.389  -0.464  35.023 1.00 36.57  ? 140 PHE   B CB  1 
ATOM   3360 C CG  . PHE   B 1 140 ? 29.024  -0.039  35.512 1.00 35.45  ? 140 PHE   B CG  1 
ATOM   3361 C CD1 . PHE   B 1 140 ? 28.576  1.259   35.323 1.00 38.30  ? 140 PHE   B CD1 1 
ATOM   3362 C CD2 . PHE   B 1 140 ? 28.206  -0.930  36.188 1.00 31.95  ? 140 PHE   B CD2 1 
ATOM   3363 C CE1 . PHE   B 1 140 ? 27.329  1.655   35.787 1.00 35.66  ? 140 PHE   B CE1 1 
ATOM   3364 C CE2 . PHE   B 1 140 ? 26.956  -0.537  36.654 1.00 35.33  ? 140 PHE   B CE2 1 
ATOM   3365 C CZ  . PHE   B 1 140 ? 26.521  0.751   36.454 1.00 32.06  ? 140 PHE   B CZ  1 
ATOM   3366 N N   . LEU   B 1 141 ? 32.588  -0.009  32.591 1.00 38.32  ? 141 LEU   B N   1 
ATOM   3367 C CA  . LEU   B 1 141 ? 34.012  -0.073  32.303 1.00 37.47  ? 141 LEU   B CA  1 
ATOM   3368 C C   . LEU   B 1 141 ? 34.761  0.878   33.227 1.00 41.72  ? 141 LEU   B C   1 
ATOM   3369 O O   . LEU   B 1 141 ? 34.166  1.587   34.046 1.00 38.62  ? 141 LEU   B O   1 
ATOM   3370 C CB  . LEU   B 1 141 ? 34.290  0.276   30.841 1.00 30.28  ? 141 LEU   B CB  1 
ATOM   3371 C CG  . LEU   B 1 141 ? 33.502  -0.514  29.801 1.00 32.22  ? 141 LEU   B CG  1 
ATOM   3372 C CD1 . LEU   B 1 141 ? 33.705  0.098   28.430 1.00 47.78  ? 141 LEU   B CD1 1 
ATOM   3373 C CD2 . LEU   B 1 141 ? 33.934  -1.969  29.812 1.00 40.99  ? 141 LEU   B CD2 1 
ATOM   3374 N N   . ASN   B 1 142 ? 36.084  0.894   33.077 1.00 42.76  ? 142 ASN   B N   1 
ATOM   3375 C CA  . ASN   B 1 142 ? 36.899  1.892   33.756 1.00 43.70  ? 142 ASN   B CA  1 
ATOM   3376 C C   . ASN   B 1 142 ? 36.400  3.295   33.428 1.00 37.40  ? 142 ASN   B C   1 
ATOM   3377 O O   . ASN   B 1 142 ? 36.101  3.611   32.272 1.00 39.16  ? 142 ASN   B O   1 
ATOM   3378 C CB  . ASN   B 1 142 ? 38.368  1.745   33.356 1.00 41.36  ? 142 ASN   B CB  1 
ATOM   3379 C CG  . ASN   B 1 142 ? 39.256  2.784   34.019 1.00 44.12  ? 142 ASN   B CG  1 
ATOM   3380 O OD1 . ASN   B 1 142 ? 39.688  3.747   33.384 1.00 55.63  ? 142 ASN   B OD1 1 
ATOM   3381 N ND2 . ASN   B 1 142 ? 39.520  2.598   35.309 1.00 43.57  ? 142 ASN   B ND2 1 
ATOM   3382 N N   . GLY   B 1 143 ? 36.295  4.130   34.460 1.00 38.02  ? 143 GLY   B N   1 
ATOM   3383 C CA  . GLY   B 1 143 ? 35.822  5.490   34.323 1.00 33.14  ? 143 GLY   B CA  1 
ATOM   3384 C C   . GLY   B 1 143 ? 34.340  5.686   34.566 1.00 30.54  ? 143 GLY   B C   1 
ATOM   3385 O O   . GLY   B 1 143 ? 33.883  6.835   34.604 1.00 30.46  ? 143 GLY   B O   1 
ATOM   3386 N N   . SER   B 1 144 ? 33.577  4.610   34.733 1.00 32.50  ? 144 SER   B N   1 
ATOM   3387 C CA  . SER   B 1 144 ? 32.130  4.688   34.892 1.00 33.22  ? 144 SER   B CA  1 
ATOM   3388 C C   . SER   B 1 144 ? 31.694  4.980   36.322 1.00 32.56  ? 144 SER   B C   1 
ATOM   3389 O O   . SER   B 1 144 ? 30.494  5.146   36.557 1.00 27.45  ? 144 SER   B O   1 
ATOM   3390 C CB  . SER   B 1 144 ? 31.477  3.386   34.420 1.00 26.85  ? 144 SER   B CB  1 
ATOM   3391 O OG  . SER   B 1 144 ? 31.919  2.287   35.192 1.00 31.90  ? 144 SER   B OG  1 
ATOM   3392 N N   . CYS   B 1 145 ? 32.625  5.029   37.275 1.00 31.37  ? 145 CYS   B N   1 
ATOM   3393 C CA  . CYS   B 1 145 ? 32.274  5.347   38.654 1.00 33.13  ? 145 CYS   B CA  1 
ATOM   3394 C C   . CYS   B 1 145 ? 31.577  6.699   38.732 1.00 36.05  ? 145 CYS   B C   1 
ATOM   3395 O O   . CYS   B 1 145 ? 31.943  7.650   38.036 1.00 33.64  ? 145 CYS   B O   1 
ATOM   3396 C CB  . CYS   B 1 145 ? 33.522  5.357   39.539 1.00 29.23  ? 145 CYS   B CB  1 
ATOM   3397 S SG  . CYS   B 1 145 ? 34.317  3.747   39.715 1.00 41.27  ? 145 CYS   B SG  1 
ATOM   3398 N N   . GLY   B 1 146 ? 30.570  6.782   39.596 1.00 32.72  ? 146 GLY   B N   1 
ATOM   3399 C CA  . GLY   B 1 146 ? 29.754  7.965   39.685 1.00 32.42  ? 146 GLY   B CA  1 
ATOM   3400 C C   . GLY   B 1 146 ? 28.544  7.960   38.783 1.00 31.66  ? 146 GLY   B C   1 
ATOM   3401 O O   . GLY   B 1 146 ? 27.706  8.862   38.899 1.00 33.10  ? 146 GLY   B O   1 
ATOM   3402 N N   . SER   B 1 147 ? 28.437  6.993   37.873 1.00 27.01  ? 147 SER   B N   1 
ATOM   3403 C CA  . SER   B 1 147 ? 27.186  6.802   37.153 1.00 33.00  ? 147 SER   B CA  1 
ATOM   3404 C C   . SER   B 1 147 ? 26.096  6.447   38.153 1.00 29.54  ? 147 SER   B C   1 
ATOM   3405 O O   . SER   B 1 147 ? 26.357  5.783   39.159 1.00 35.80  ? 147 SER   B O   1 
ATOM   3406 C CB  . SER   B 1 147 ? 27.326  5.693   36.111 1.00 34.05  ? 147 SER   B CB  1 
ATOM   3407 O OG  . SER   B 1 147 ? 28.423  5.936   35.250 1.00 34.83  ? 147 SER   B OG  1 
ATOM   3408 N N   . VAL   B 1 148 ? 24.873  6.900   37.889 1.00 33.36  ? 148 VAL   B N   1 
ATOM   3409 C CA  . VAL   B 1 148 ? 23.812  6.787   38.880 1.00 34.21  ? 148 VAL   B CA  1 
ATOM   3410 C C   . VAL   B 1 148 ? 22.671  5.942   38.340 1.00 38.10  ? 148 VAL   B C   1 
ATOM   3411 O O   . VAL   B 1 148 ? 22.463  5.828   37.127 1.00 33.94  ? 148 VAL   B O   1 
ATOM   3412 C CB  . VAL   B 1 148 ? 23.290  8.166   39.337 1.00 36.21  ? 148 VAL   B CB  1 
ATOM   3413 C CG1 . VAL   B 1 148 ? 24.390  8.931   40.047 1.00 34.10  ? 148 VAL   B CG1 1 
ATOM   3414 C CG2 . VAL   B 1 148 ? 22.748  8.946   38.156 1.00 33.25  ? 148 VAL   B CG2 1 
ATOM   3415 N N   . GLY   B 1 149 ? 21.947  5.324   39.270 1.00 35.85  ? 149 GLY   B N   1 
ATOM   3416 C CA  . GLY   B 1 149 ? 20.730  4.595   38.974 1.00 38.62  ? 149 GLY   B CA  1 
ATOM   3417 C C   . GLY   B 1 149 ? 19.535  5.345   39.534 1.00 41.77  ? 149 GLY   B C   1 
ATOM   3418 O O   . GLY   B 1 149 ? 19.632  6.006   40.572 1.00 35.78  ? 149 GLY   B O   1 
ATOM   3419 N N   . PHE   B 1 150 ? 18.403  5.238   38.845 1.00 36.85  ? 150 PHE   B N   1 
ATOM   3420 C CA  . PHE   B 1 150 ? 17.272  6.093   39.164 1.00 41.86  ? 150 PHE   B CA  1 
ATOM   3421 C C   . PHE   B 1 150 ? 15.982  5.466   38.660 1.00 44.09  ? 150 PHE   B C   1 
ATOM   3422 O O   . PHE   B 1 150 ? 15.977  4.699   37.691 1.00 37.18  ? 150 PHE   B O   1 
ATOM   3423 C CB  . PHE   B 1 150 ? 17.447  7.487   38.545 1.00 38.72  ? 150 PHE   B CB  1 
ATOM   3424 C CG  . PHE   B 1 150 ? 17.476  7.475   37.044 1.00 39.29  ? 150 PHE   B CG  1 
ATOM   3425 C CD1 . PHE   B 1 150 ? 18.645  7.162   36.361 1.00 36.99  ? 150 PHE   B CD1 1 
ATOM   3426 C CD2 . PHE   B 1 150 ? 16.335  7.767   36.312 1.00 38.96  ? 150 PHE   B CD2 1 
ATOM   3427 C CE1 . PHE   B 1 150 ? 18.675  7.142   34.980 1.00 40.28  ? 150 PHE   B CE1 1 
ATOM   3428 C CE2 . PHE   B 1 150 ? 16.358  7.748   34.929 1.00 38.09  ? 150 PHE   B CE2 1 
ATOM   3429 C CZ  . PHE   B 1 150 ? 17.530  7.438   34.262 1.00 39.06  ? 150 PHE   B CZ  1 
ATOM   3430 N N   . ASN   B 1 151 ? 14.889  5.814   39.331 1.00 44.97  ? 151 ASN   B N   1 
ATOM   3431 C CA  . ASN   B 1 151 ? 13.544  5.615   38.821 1.00 47.33  ? 151 ASN   B CA  1 
ATOM   3432 C C   . ASN   B 1 151 ? 12.878  6.976   38.675 1.00 47.01  ? 151 ASN   B C   1 
ATOM   3433 O O   . ASN   B 1 151 ? 13.253  7.941   39.350 1.00 48.88  ? 151 ASN   B O   1 
ATOM   3434 C CB  . ASN   B 1 151 ? 12.721  4.712   39.738 1.00 44.90  ? 151 ASN   B CB  1 
ATOM   3435 C CG  . ASN   B 1 151 ? 13.166  3.267   39.681 1.00 45.37  ? 151 ASN   B CG  1 
ATOM   3436 O OD1 . ASN   B 1 151 ? 12.863  2.553   38.725 1.00 52.28  ? 151 ASN   B OD1 1 
ATOM   3437 N ND2 . ASN   B 1 151 ? 13.881  2.823   40.710 1.00 42.93  ? 151 ASN   B ND2 1 
ATOM   3438 N N   . ILE   B 1 152 ? 11.904  7.061   37.772 1.00 46.25  ? 152 ILE   B N   1 
ATOM   3439 C CA  . ILE   B 1 152 ? 11.208  8.323   37.540 1.00 51.49  ? 152 ILE   B CA  1 
ATOM   3440 C C   . ILE   B 1 152 ? 9.766   8.194   38.010 1.00 62.28  ? 152 ILE   B C   1 
ATOM   3441 O O   . ILE   B 1 152 ? 8.876   7.820   37.236 1.00 67.19  ? 152 ILE   B O   1 
ATOM   3442 C CB  . ILE   B 1 152 ? 11.283  8.746   36.062 1.00 53.34  ? 152 ILE   B CB  1 
ATOM   3443 C CG1 . ILE   B 1 152 ? 12.746  8.820   35.614 1.00 49.57  ? 152 ILE   B CG1 1 
ATOM   3444 C CG2 . ILE   B 1 152 ? 10.582  10.083  35.857 1.00 59.29  ? 152 ILE   B CG2 1 
ATOM   3445 C CD1 . ILE   B 1 152 ? 13.015  9.846   34.538 1.00 46.57  ? 152 ILE   B CD1 1 
ATOM   3446 N N   . ASP   B 1 153 ? 9.528   8.495   39.284 1.00 65.55  ? 153 ASP   B N   1 
ATOM   3447 C CA  . ASP   B 1 153 ? 8.194   8.425   39.871 1.00 71.49  ? 153 ASP   B CA  1 
ATOM   3448 C C   . ASP   B 1 153 ? 7.486   9.753   39.627 1.00 73.33  ? 153 ASP   B C   1 
ATOM   3449 O O   . ASP   B 1 153 ? 7.869   10.782  40.197 1.00 69.67  ? 153 ASP   B O   1 
ATOM   3450 C CB  . ASP   B 1 153 ? 8.278   8.103   41.362 1.00 61.64  ? 153 ASP   B CB  1 
ATOM   3451 N N   . TYR   B 1 154 ? 6.455   9.728   38.779 1.00 75.83  ? 154 TYR   B N   1 
ATOM   3452 C CA  . TYR   B 1 154 ? 5.708   10.922  38.365 1.00 77.66  ? 154 TYR   B CA  1 
ATOM   3453 C C   . TYR   B 1 154 ? 6.686   11.854  37.663 1.00 71.60  ? 154 TYR   B C   1 
ATOM   3454 O O   . TYR   B 1 154 ? 7.325   11.422  36.687 1.00 72.69  ? 154 TYR   B O   1 
ATOM   3455 C CB  . TYR   B 1 154 ? 4.975   11.513  39.574 1.00 73.02  ? 154 TYR   B CB  1 
ATOM   3456 N N   . ASP   B 1 155 ? 6.836   13.105  38.093 1.00 71.66  ? 155 ASP   B N   1 
ATOM   3457 C CA  . ASP   B 1 155 ? 7.819   14.022  37.534 1.00 79.76  ? 155 ASP   B CA  1 
ATOM   3458 C C   . ASP   B 1 155 ? 9.075   14.118  38.393 1.00 77.46  ? 155 ASP   B C   1 
ATOM   3459 O O   . ASP   B 1 155 ? 9.917   14.990  38.150 1.00 67.88  ? 155 ASP   B O   1 
ATOM   3460 C CB  . ASP   B 1 155 ? 7.199   15.411  37.349 1.00 75.25  ? 155 ASP   B CB  1 
ATOM   3461 C CG  . ASP   B 1 155 ? 6.688   16.009  38.655 1.00 83.99  ? 155 ASP   B CG  1 
ATOM   3462 O OD1 . ASP   B 1 155 ? 6.222   15.242  39.528 1.00 76.23  ? 155 ASP   B OD1 1 
ATOM   3463 O OD2 . ASP   B 1 155 ? 6.751   17.250  38.804 1.00 83.20  ? 155 ASP   B OD2 1 
ATOM   3464 N N   . CYS   B 1 156 ? 9.223   13.235  39.379 1.00 70.45  ? 156 CYS   B N   1 
ATOM   3465 C CA  . CYS   B 1 156 ? 10.310  13.285  40.348 1.00 63.77  ? 156 CYS   B CA  1 
ATOM   3466 C C   . CYS   B 1 156 ? 11.284  12.140  40.097 1.00 59.90  ? 156 CYS   B C   1 
ATOM   3467 O O   . CYS   B 1 156 ? 10.873  10.977  40.015 1.00 54.57  ? 156 CYS   B O   1 
ATOM   3468 C CB  . CYS   B 1 156 ? 9.757   13.212  41.775 1.00 63.24  ? 156 CYS   B CB  1 
ATOM   3469 S SG  . CYS   B 1 156 ? 10.996  13.264  43.085 1.00 61.99  ? 156 CYS   B SG  1 
ATOM   3470 N N   . VAL   B 1 157 ? 12.568  12.470  39.977 1.00 54.16  ? 157 VAL   B N   1 
ATOM   3471 C CA  . VAL   B 1 157 ? 13.615  11.470  39.802 1.00 44.94  ? 157 VAL   B CA  1 
ATOM   3472 C C   . VAL   B 1 157 ? 14.033  10.962  41.175 1.00 50.62  ? 157 VAL   B C   1 
ATOM   3473 O O   . VAL   B 1 157 ? 14.447  11.744  42.037 1.00 47.35  ? 157 VAL   B O   1 
ATOM   3474 C CB  . VAL   B 1 157 ? 14.820  12.048  39.046 1.00 50.07  ? 157 VAL   B CB  1 
ATOM   3475 C CG1 . VAL   B 1 157 ? 15.864  10.959  38.806 1.00 46.36  ? 157 VAL   B CG1 1 
ATOM   3476 C CG2 . VAL   B 1 157 ? 14.377  12.680  37.738 1.00 45.94  ? 157 VAL   B CG2 1 
ATOM   3477 N N   . SER   B 1 158 ? 13.934  9.652   41.380 1.00 42.64  ? 158 SER   B N   1 
ATOM   3478 C CA  . SER   B 1 158 ? 14.338  9.027   42.638 1.00 45.19  ? 158 SER   B CA  1 
ATOM   3479 C C   . SER   B 1 158 ? 15.700  8.375   42.421 1.00 49.22  ? 158 SER   B C   1 
ATOM   3480 O O   . SER   B 1 158 ? 15.799  7.237   41.959 1.00 50.78  ? 158 SER   B O   1 
ATOM   3481 C CB  . SER   B 1 158 ? 13.291  8.023   43.104 1.00 43.29  ? 158 SER   B CB  1 
ATOM   3482 O OG  . SER   B 1 158 ? 12.076  8.675   43.437 1.00 54.38  ? 158 SER   B OG  1 
ATOM   3483 N N   . PHE   B 1 159 ? 16.760  9.114   42.751 1.00 42.27  ? 159 PHE   B N   1 
ATOM   3484 C CA  . PHE   B 1 159 ? 18.109  8.569   42.678 1.00 39.80  ? 159 PHE   B CA  1 
ATOM   3485 C C   . PHE   B 1 159 ? 18.294  7.502   43.746 1.00 42.99  ? 159 PHE   B C   1 
ATOM   3486 O O   . PHE   B 1 159 ? 18.016  7.736   44.926 1.00 43.79  ? 159 PHE   B O   1 
ATOM   3487 C CB  . PHE   B 1 159 ? 19.142  9.678   42.855 1.00 41.90  ? 159 PHE   B CB  1 
ATOM   3488 C CG  . PHE   B 1 159 ? 19.165  10.675  41.731 1.00 43.94  ? 159 PHE   B CG  1 
ATOM   3489 C CD1 . PHE   B 1 159 ? 19.724  10.347  40.511 1.00 36.17  ? 159 PHE   B CD1 1 
ATOM   3490 C CD2 . PHE   B 1 159 ? 18.635  11.941  41.901 1.00 43.11  ? 159 PHE   B CD2 1 
ATOM   3491 C CE1 . PHE   B 1 159 ? 19.749  11.263  39.475 1.00 34.59  ? 159 PHE   B CE1 1 
ATOM   3492 C CE2 . PHE   B 1 159 ? 18.661  12.861  40.871 1.00 41.11  ? 159 PHE   B CE2 1 
ATOM   3493 C CZ  . PHE   B 1 159 ? 19.218  12.522  39.658 1.00 39.84  ? 159 PHE   B CZ  1 
ATOM   3494 N N   . CYS   B 1 160 ? 18.764  6.324   43.335 1.00 35.40  ? 160 CYS   B N   1 
ATOM   3495 C CA  . CYS   B 1 160 ? 18.891  5.195   44.249 1.00 40.31  ? 160 CYS   B CA  1 
ATOM   3496 C C   . CYS   B 1 160 ? 20.248  4.506   44.229 1.00 35.07  ? 160 CYS   B C   1 
ATOM   3497 O O   . CYS   B 1 160 ? 20.543  3.752   45.164 1.00 36.22  ? 160 CYS   B O   1 
ATOM   3498 C CB  . CYS   B 1 160 ? 17.809  4.145   43.953 1.00 40.98  ? 160 CYS   B CB  1 
ATOM   3499 S SG  . CYS   B 1 160 ? 17.869  3.452   42.283 1.00 43.65  ? 160 CYS   B SG  1 
ATOM   3500 N N   . TYR   B 1 161 ? 21.082  4.736   43.220 1.00 33.88  ? 161 TYR   B N   1 
ATOM   3501 C CA  . TYR   B 1 161 ? 22.333  4.007   43.071 1.00 30.40  ? 161 TYR   B CA  1 
ATOM   3502 C C   . TYR   B 1 161 ? 23.397  4.943   42.529 1.00 32.40  ? 161 TYR   B C   1 
ATOM   3503 O O   . TYR   B 1 161 ? 23.119  5.754   41.647 1.00 32.02  ? 161 TYR   B O   1 
ATOM   3504 C CB  . TYR   B 1 161 ? 22.165  2.808   42.123 1.00 33.94  ? 161 TYR   B CB  1 
ATOM   3505 C CG  . TYR   B 1 161 ? 23.423  1.987   41.913 1.00 34.58  ? 161 TYR   B CG  1 
ATOM   3506 C CD1 . TYR   B 1 161 ? 23.814  1.042   42.849 1.00 33.56  ? 161 TYR   B CD1 1 
ATOM   3507 C CD2 . TYR   B 1 161 ? 24.204  2.144   40.773 1.00 33.36  ? 161 TYR   B CD2 1 
ATOM   3508 C CE1 . TYR   B 1 161 ? 24.952  0.282   42.669 1.00 34.97  ? 161 TYR   B CE1 1 
ATOM   3509 C CE2 . TYR   B 1 161 ? 25.351  1.386   40.580 1.00 31.96  ? 161 TYR   B CE2 1 
ATOM   3510 C CZ  . TYR   B 1 161 ? 25.719  0.457   41.537 1.00 37.02  ? 161 TYR   B CZ  1 
ATOM   3511 O OH  . TYR   B 1 161 ? 26.850  -0.308  41.371 1.00 29.52  ? 161 TYR   B OH  1 
ATOM   3512 N N   . MET   B 1 162 ? 24.604  4.844   43.075 1.00 30.49  ? 162 MET   B N   1 
ATOM   3513 C CA  . MET   B 1 162 ? 25.779  5.441   42.462 1.00 33.93  ? 162 MET   B CA  1 
ATOM   3514 C C   . MET   B 1 162 ? 26.853  4.371   42.387 1.00 32.16  ? 162 MET   B C   1 
ATOM   3515 O O   . MET   B 1 162 ? 27.110  3.670   43.373 1.00 33.93  ? 162 MET   B O   1 
ATOM   3516 C CB  . MET   B 1 162 ? 26.291  6.662   43.229 1.00 33.84  ? 162 MET   B CB  1 
ATOM   3517 C CG  . MET   B 1 162 ? 27.307  7.459   42.418 1.00 39.19  ? 162 MET   B CG  1 
ATOM   3518 S SD  . MET   B 1 162 ? 27.991  8.882   43.280 1.00 41.99  ? 162 MET   B SD  1 
ATOM   3519 C CE  . MET   B 1 162 ? 28.828  8.033   44.599 1.00 33.33  ? 162 MET   B CE  1 
ATOM   3520 N N   . HIS   B 1 163 ? 27.470  4.242   41.221 1.00 28.87  ? 163 HIS   B N   1 
ATOM   3521 C CA  . HIS   B 1 163 ? 28.360  3.125   40.964 1.00 26.20  ? 163 HIS   B CA  1 
ATOM   3522 C C   . HIS   B 1 163 ? 29.715  3.364   41.615 1.00 30.52  ? 163 HIS   B C   1 
ATOM   3523 O O   . HIS   B 1 163 ? 30.246  4.478   41.593 1.00 32.39  ? 163 HIS   B O   1 
ATOM   3524 C CB  . HIS   B 1 163 ? 28.508  2.917   39.459 1.00 30.78  ? 163 HIS   B CB  1 
ATOM   3525 C CG  . HIS   B 1 163 ? 29.384  1.764   39.099 1.00 31.29  ? 163 HIS   B CG  1 
ATOM   3526 N ND1 . HIS   B 1 163 ? 29.233  0.514   39.659 1.00 28.63  ? 163 HIS   B ND1 1 
ATOM   3527 C CD2 . HIS   B 1 163 ? 30.427  1.671   38.242 1.00 32.27  ? 163 HIS   B CD2 1 
ATOM   3528 C CE1 . HIS   B 1 163 ? 30.146  -0.301  39.161 1.00 34.32  ? 163 HIS   B CE1 1 
ATOM   3529 N NE2 . HIS   B 1 163 ? 30.881  0.376   38.298 1.00 35.62  ? 163 HIS   B NE2 1 
ATOM   3530 N N   . HIS   B 1 164 ? 30.264  2.322   42.210 1.00 30.84  ? 164 HIS   B N   1 
ATOM   3531 C CA  . HIS   B 1 164 ? 31.540  2.482   42.900 1.00 33.36  ? 164 HIS   B CA  1 
ATOM   3532 C C   . HIS   B 1 164 ? 32.620  1.528   42.419 1.00 29.11  ? 164 HIS   B C   1 
ATOM   3533 O O   . HIS   B 1 164 ? 33.781  1.933   42.329 1.00 40.33  ? 164 HIS   B O   1 
ATOM   3534 C CB  . HIS   B 1 164 ? 31.366  2.308   44.420 1.00 29.49  ? 164 HIS   B CB  1 
ATOM   3535 C CG  . HIS   B 1 164 ? 30.873  3.536   45.120 1.00 31.32  ? 164 HIS   B CG  1 
ATOM   3536 N ND1 . HIS   B 1 164 ? 31.672  4.285   45.957 1.00 33.87  ? 164 HIS   B ND1 1 
ATOM   3537 C CD2 . HIS   B 1 164 ? 29.661  4.140   45.116 1.00 28.34  ? 164 HIS   B CD2 1 
ATOM   3538 C CE1 . HIS   B 1 164 ? 30.974  5.298   46.438 1.00 34.02  ? 164 HIS   B CE1 1 
ATOM   3539 N NE2 . HIS   B 1 164 ? 29.751  5.235   45.940 1.00 34.96  ? 164 HIS   B NE2 1 
ATOM   3540 N N   . MET   B 1 165 ? 32.278  0.278   42.122 1.00 34.43  ? 165 MET   B N   1 
ATOM   3541 C CA  . MET   B 1 165 ? 33.307  -0.738  41.960 1.00 37.22  ? 165 MET   B CA  1 
ATOM   3542 C C   . MET   B 1 165 ? 32.724  -1.963  41.274 1.00 39.04  ? 165 MET   B C   1 
ATOM   3543 O O   . MET   B 1 165 ? 31.508  -2.162  41.233 1.00 37.16  ? 165 MET   B O   1 
ATOM   3544 C CB  . MET   B 1 165 ? 33.897  -1.141  43.315 1.00 38.61  ? 165 MET   B CB  1 
ATOM   3545 C CG  . MET   B 1 165 ? 32.920  -1.947  44.144 1.00 44.91  ? 165 MET   B CG  1 
ATOM   3546 S SD  . MET   B 1 165 ? 33.474  -2.208  45.830 1.00 54.91  ? 165 MET   B SD  1 
ATOM   3547 C CE  . MET   B 1 165 ? 33.719  -0.513  46.319 1.00 52.23  ? 165 MET   B CE  1 
ATOM   3548 N N   . GLU   B 1 166 ? 33.620  -2.792  40.750 1.00 41.72  ? 166 GLU   B N   1 
ATOM   3549 C CA  . GLU   B 1 166 ? 33.271  -4.081  40.178 1.00 38.61  ? 166 GLU   B CA  1 
ATOM   3550 C C   . GLU   B 1 166 ? 33.871  -5.177  41.043 1.00 38.60  ? 166 GLU   B C   1 
ATOM   3551 O O   . GLU   B 1 166 ? 35.020  -5.077  41.483 1.00 44.67  ? 166 GLU   B O   1 
ATOM   3552 C CB  . GLU   B 1 166 ? 33.774  -4.218  38.735 1.00 38.62  ? 166 GLU   B CB  1 
ATOM   3553 C CG  . GLU   B 1 166 ? 33.452  -5.565  38.094 1.00 39.78  ? 166 GLU   B CG  1 
ATOM   3554 C CD  . GLU   B 1 166 ? 33.758  -5.590  36.603 1.00 45.23  ? 166 GLU   B CD  1 
ATOM   3555 O OE1 . GLU   B 1 166 ? 33.226  -4.733  35.864 1.00 42.85  ? 166 GLU   B OE1 1 
ATOM   3556 O OE2 . GLU   B 1 166 ? 34.544  -6.462  36.178 1.00 48.58  ? 166 GLU   B OE2 1 
ATOM   3557 N N   . LEU   B 1 167 ? 33.093  -6.203  41.289 1.00 38.68  ? 167 LEU   B N   1 
ATOM   3558 C CA  . LEU   B 1 167 ? 33.529  -7.314  42.113 1.00 45.09  ? 167 LEU   B CA  1 
ATOM   3559 C C   . LEU   B 1 167 ? 34.167  -8.395  41.255 1.00 55.78  ? 167 LEU   B C   1 
ATOM   3560 O O   . LEU   B 1 167 ? 33.960  -8.438  40.038 1.00 50.73  ? 167 LEU   B O   1 
ATOM   3561 C CB  . LEU   B 1 167 ? 32.343  -7.875  42.886 1.00 45.91  ? 167 LEU   B CB  1 
ATOM   3562 C CG  . LEU   B 1 167 ? 31.786  -6.893  43.913 1.00 44.04  ? 167 LEU   B CG  1 
ATOM   3563 C CD1 . LEU   B 1 167 ? 30.481  -7.429  44.457 1.00 43.90  ? 167 LEU   B CD1 1 
ATOM   3564 C CD2 . LEU   B 1 167 ? 32.794  -6.660  45.029 1.00 47.77  ? 167 LEU   B CD2 1 
ATOM   3565 N N   . PRO   B 1 168 ? 34.957  -9.286  41.867 1.00 60.66  ? 168 PRO   B N   1 
ATOM   3566 C CA  . PRO   B 1 168 ? 35.672  -10.303 41.076 1.00 57.06  ? 168 PRO   B CA  1 
ATOM   3567 C C   . PRO   B 1 168 ? 34.778  -11.155 40.190 1.00 60.03  ? 168 PRO   B C   1 
ATOM   3568 O O   . PRO   B 1 168 ? 35.222  -11.587 39.118 1.00 67.69  ? 168 PRO   B O   1 
ATOM   3569 C CB  . PRO   B 1 168 ? 36.363  -11.146 42.154 1.00 64.23  ? 168 PRO   B CB  1 
ATOM   3570 C CG  . PRO   B 1 168 ? 36.575  -10.188 43.282 1.00 61.70  ? 168 PRO   B CG  1 
ATOM   3571 C CD  . PRO   B 1 168 ? 35.366  -9.304  43.284 1.00 55.68  ? 168 PRO   B CD  1 
ATOM   3572 N N   . THR   B 1 169 ? 33.535  -11.406 40.594 1.00 57.43  ? 169 THR   B N   1 
ATOM   3573 C CA  . THR   B 1 169 ? 32.624  -12.231 39.808 1.00 65.20  ? 169 THR   B CA  1 
ATOM   3574 C C   . THR   B 1 169 ? 31.999  -11.484 38.632 1.00 57.90  ? 169 THR   B C   1 
ATOM   3575 O O   . THR   B 1 169 ? 31.135  -12.047 37.949 1.00 56.20  ? 169 THR   B O   1 
ATOM   3576 C CB  . THR   B 1 169 ? 31.532  -12.811 40.715 1.00 63.02  ? 169 THR   B CB  1 
ATOM   3577 O OG1 . THR   B 1 169 ? 30.457  -13.326 39.916 1.00 65.73  ? 169 THR   B OG1 1 
ATOM   3578 C CG2 . THR   B 1 169 ? 31.007  -11.748 41.668 1.00 64.80  ? 169 THR   B CG2 1 
ATOM   3579 N N   . GLY   B 1 170 ? 32.428  -10.250 38.368 1.00 55.32  ? 170 GLY   B N   1 
ATOM   3580 C CA  . GLY   B 1 170 ? 31.907  -9.473  37.265 1.00 51.83  ? 170 GLY   B CA  1 
ATOM   3581 C C   . GLY   B 1 170 ? 30.659  -8.682  37.569 1.00 51.24  ? 170 GLY   B C   1 
ATOM   3582 O O   . GLY   B 1 170 ? 30.158  -7.982  36.679 1.00 52.14  ? 170 GLY   B O   1 
ATOM   3583 N N   . VAL   B 1 171 ? 30.139  -8.767  38.792 1.00 48.15  ? 171 VAL   B N   1 
ATOM   3584 C CA  . VAL   B 1 171 ? 28.980  -7.972  39.182 1.00 44.41  ? 171 VAL   B CA  1 
ATOM   3585 C C   . VAL   B 1 171 ? 29.454  -6.670  39.825 1.00 42.60  ? 171 VAL   B C   1 
ATOM   3586 O O   . VAL   B 1 171 ? 30.650  -6.486  40.093 1.00 36.32  ? 171 VAL   B O   1 
ATOM   3587 C CB  . VAL   B 1 171 ? 28.051  -8.762  40.123 1.00 50.35  ? 171 VAL   B CB  1 
ATOM   3588 C CG1 . VAL   B 1 171 ? 27.586  -10.050 39.457 1.00 52.93  ? 171 VAL   B CG1 1 
ATOM   3589 C CG2 . VAL   B 1 171 ? 28.747  -9.042  41.437 1.00 41.50  ? 171 VAL   B CG2 1 
ATOM   3590 N N   . HIS   B 1 172 ? 28.519  -5.764  40.089 1.00 38.31  ? 172 HIS   B N   1 
ATOM   3591 C CA  . HIS   B 1 172 ? 28.860  -4.400  40.454 1.00 35.54  ? 172 HIS   B CA  1 
ATOM   3592 C C   . HIS   B 1 172 ? 28.193  -4.012  41.766 1.00 39.16  ? 172 HIS   B C   1 
ATOM   3593 O O   . HIS   B 1 172 ? 27.098  -4.478  42.093 1.00 34.39  ? 172 HIS   B O   1 
ATOM   3594 C CB  . HIS   B 1 172 ? 28.461  -3.444  39.337 1.00 29.93  ? 172 HIS   B CB  1 
ATOM   3595 C CG  . HIS   B 1 172 ? 28.994  -3.852  37.999 1.00 39.65  ? 172 HIS   B CG  1 
ATOM   3596 N ND1 . HIS   B 1 172 ? 28.233  -4.522  37.064 1.00 33.98  ? 172 HIS   B ND1 1 
ATOM   3597 C CD2 . HIS   B 1 172 ? 30.228  -3.722  37.454 1.00 36.43  ? 172 HIS   B CD2 1 
ATOM   3598 C CE1 . HIS   B 1 172 ? 28.967  -4.763  35.992 1.00 36.79  ? 172 HIS   B CE1 1 
ATOM   3599 N NE2 . HIS   B 1 172 ? 30.182  -4.289  36.203 1.00 37.06  ? 172 HIS   B NE2 1 
ATOM   3600 N N   . ALA   B 1 173 ? 28.888  -3.168  42.529 1.00 32.78  ? 173 ALA   B N   1 
ATOM   3601 C CA  . ALA   B 1 173 ? 28.411  -2.693  43.818 1.00 34.68  ? 173 ALA   B CA  1 
ATOM   3602 C C   . ALA   B 1 173 ? 28.520  -1.176  43.882 1.00 35.13  ? 173 ALA   B C   1 
ATOM   3603 O O   . ALA   B 1 173 ? 29.417  -0.570  43.286 1.00 29.28  ? 173 ALA   B O   1 
ATOM   3604 C CB  . ALA   B 1 173 ? 29.197  -3.324  44.971 1.00 39.81  ? 173 ALA   B CB  1 
ATOM   3605 N N   . GLY   B 1 174 ? 27.591  -0.572  44.613 1.00 27.54  ? 174 GLY   B N   1 
ATOM   3606 C CA  . GLY   B 1 174 ? 27.590  0.858   44.799 1.00 32.30  ? 174 GLY   B CA  1 
ATOM   3607 C C   . GLY   B 1 174 ? 26.807  1.246   46.035 1.00 30.86  ? 174 GLY   B C   1 
ATOM   3608 O O   . GLY   B 1 174 ? 26.437  0.400   46.851 1.00 30.29  ? 174 GLY   B O   1 
ATOM   3609 N N   . THR   B 1 175 ? 26.547  2.543   46.151 1.00 28.52  ? 175 THR   B N   1 
ATOM   3610 C CA  . THR   B 1 175 ? 25.915  3.135   47.322 1.00 32.55  ? 175 THR   B CA  1 
ATOM   3611 C C   . THR   B 1 175 ? 24.594  3.787   46.934 1.00 36.48  ? 175 THR   B C   1 
ATOM   3612 O O   . THR   B 1 175 ? 24.257  3.913   45.753 1.00 32.97  ? 175 THR   B O   1 
ATOM   3613 C CB  . THR   B 1 175 ? 26.826  4.188   47.965 1.00 30.80  ? 175 THR   B CB  1 
ATOM   3614 O OG1 . THR   B 1 175 ? 27.024  5.268   47.042 1.00 34.06  ? 175 THR   B OG1 1 
ATOM   3615 C CG2 . THR   B 1 175 ? 28.173  3.588   48.320 1.00 30.96  ? 175 THR   B CG2 1 
ATOM   3616 N N   . ASP   B 1 176 ? 23.844  4.218   47.948 1.00 32.63  ? 176 ASP   B N   1 
ATOM   3617 C CA  . ASP   B 1 176 ? 22.772  5.164   47.695 1.00 32.68  ? 176 ASP   B CA  1 
ATOM   3618 C C   . ASP   B 1 176 ? 23.369  6.568   47.621 1.00 35.53  ? 176 ASP   B C   1 
ATOM   3619 O O   . ASP   B 1 176 ? 24.577  6.761   47.782 1.00 33.55  ? 176 ASP   B O   1 
ATOM   3620 C CB  . ASP   B 1 176 ? 21.668  5.040   48.752 1.00 41.15  ? 176 ASP   B CB  1 
ATOM   3621 C CG  . ASP   B 1 176 ? 22.170  5.223   50.183 1.00 41.17  ? 176 ASP   B CG  1 
ATOM   3622 O OD1 . ASP   B 1 176 ? 23.208  5.884   50.402 1.00 40.13  ? 176 ASP   B OD1 1 
ATOM   3623 O OD2 . ASP   B 1 176 ? 21.506  4.700   51.103 1.00 43.20  ? 176 ASP   B OD2 1 
ATOM   3624 N N   . LEU   B 1 177 ? 22.527  7.568   47.370 1.00 34.68  ? 177 LEU   B N   1 
ATOM   3625 C CA  . LEU   B 1 177 ? 23.082  8.911   47.240 1.00 37.77  ? 177 LEU   B CA  1 
ATOM   3626 C C   . LEU   B 1 177 ? 23.464  9.531   48.580 1.00 44.74  ? 177 LEU   B C   1 
ATOM   3627 O O   . LEU   B 1 177 ? 24.001  10.645  48.590 1.00 42.77  ? 177 LEU   B O   1 
ATOM   3628 C CB  . LEU   B 1 177 ? 22.105  9.815   46.486 1.00 37.85  ? 177 LEU   B CB  1 
ATOM   3629 C CG  . LEU   B 1 177 ? 22.325  9.888   44.968 1.00 38.16  ? 177 LEU   B CG  1 
ATOM   3630 C CD1 . LEU   B 1 177 ? 23.644  10.564  44.645 1.00 39.92  ? 177 LEU   B CD1 1 
ATOM   3631 C CD2 . LEU   B 1 177 ? 22.271  8.502   44.328 1.00 34.84  ? 177 LEU   B CD2 1 
ATOM   3632 N N   . GLU   B 1 178 ? 23.222  8.844   49.698 1.00 44.81  ? 178 GLU   B N   1 
ATOM   3633 C CA  . GLU   B 1 178 ? 23.741  9.261   50.993 1.00 43.07  ? 178 GLU   B CA  1 
ATOM   3634 C C   . GLU   B 1 178 ? 25.057  8.580   51.344 1.00 44.23  ? 178 GLU   B C   1 
ATOM   3635 O O   . GLU   B 1 178 ? 25.582  8.797   52.442 1.00 41.03  ? 178 GLU   B O   1 
ATOM   3636 C CB  . GLU   B 1 178 ? 22.712  8.989   52.094 1.00 54.64  ? 178 GLU   B CB  1 
ATOM   3637 C CG  . GLU   B 1 178 ? 21.449  9.825   51.994 1.00 54.08  ? 178 GLU   B CG  1 
ATOM   3638 C CD  . GLU   B 1 178 ? 20.467  9.522   53.107 1.00 68.26  ? 178 GLU   B CD  1 
ATOM   3639 O OE1 . GLU   B 1 178 ? 20.774  8.652   53.949 1.00 74.23  ? 178 GLU   B OE1 1 
ATOM   3640 O OE2 . GLU   B 1 178 ? 19.389  10.152  53.142 1.00 77.01  ? 178 GLU   B OE2 1 
ATOM   3641 N N   . GLY   B 1 179 ? 25.594  7.749   50.452 1.00 35.03  ? 179 GLY   B N   1 
ATOM   3642 C CA  . GLY   B 1 179 ? 26.908  7.178   50.640 1.00 34.28  ? 179 GLY   B CA  1 
ATOM   3643 C C   . GLY   B 1 179 ? 26.947  5.820   51.299 1.00 34.60  ? 179 GLY   B C   1 
ATOM   3644 O O   . GLY   B 1 179 ? 28.041  5.326   51.593 1.00 33.00  ? 179 GLY   B O   1 
ATOM   3645 N N   . ASN   B 1 180 ? 25.801  5.200   51.540 1.00 35.52  ? 180 ASN   B N   1 
ATOM   3646 C CA  . ASN   B 1 180 ? 25.742  3.907   52.203 1.00 34.80  ? 180 ASN   B CA  1 
ATOM   3647 C C   . ASN   B 1 180 ? 25.709  2.808   51.150 1.00 30.39  ? 180 ASN   B C   1 
ATOM   3648 O O   . ASN   B 1 180 ? 24.808  2.779   50.305 1.00 36.88  ? 180 ASN   B O   1 
ATOM   3649 C CB  . ASN   B 1 180 ? 24.522  3.832   53.119 1.00 43.93  ? 180 ASN   B CB  1 
ATOM   3650 C CG  . ASN   B 1 180 ? 24.576  4.861   54.234 1.00 45.42  ? 180 ASN   B CG  1 
ATOM   3651 O OD1 . ASN   B 1 180 ? 25.572  4.961   54.954 1.00 43.68  ? 180 ASN   B OD1 1 
ATOM   3652 N ND2 . ASN   B 1 180 ? 23.512  5.642   54.370 1.00 47.00  ? 180 ASN   B ND2 1 
ATOM   3653 N N   . PHE   B 1 181 ? 26.696  1.920   51.196 1.00 31.87  ? 181 PHE   B N   1 
ATOM   3654 C CA  . PHE   B 1 181 ? 26.729  0.793   50.276 1.00 42.23  ? 181 PHE   B CA  1 
ATOM   3655 C C   . PHE   B 1 181 ? 25.501  -0.084  50.456 1.00 42.31  ? 181 PHE   B C   1 
ATOM   3656 O O   . PHE   B 1 181 ? 25.046  -0.333  51.577 1.00 42.27  ? 181 PHE   B O   1 
ATOM   3657 C CB  . PHE   B 1 181 ? 27.984  -0.053  50.499 1.00 32.47  ? 181 PHE   B CB  1 
ATOM   3658 C CG  . PHE   B 1 181 ? 29.135  0.324   49.621 1.00 36.08  ? 181 PHE   B CG  1 
ATOM   3659 C CD1 . PHE   B 1 181 ? 29.266  -0.216  48.347 1.00 36.22  ? 181 PHE   B CD1 1 
ATOM   3660 C CD2 . PHE   B 1 181 ? 30.098  1.208   50.075 1.00 37.29  ? 181 PHE   B CD2 1 
ATOM   3661 C CE1 . PHE   B 1 181 ? 30.336  0.131   47.541 1.00 38.11  ? 181 PHE   B CE1 1 
ATOM   3662 C CE2 . PHE   B 1 181 ? 31.165  1.560   49.282 1.00 37.58  ? 181 PHE   B CE2 1 
ATOM   3663 C CZ  . PHE   B 1 181 ? 31.286  1.024   48.011 1.00 38.84  ? 181 PHE   B CZ  1 
ATOM   3664 N N   . TYR   B 1 182 ? 24.952  -0.534  49.335 1.00 35.21  ? 182 TYR   B N   1 
ATOM   3665 C CA  . TYR   B 1 182 ? 24.086  -1.700  49.352 1.00 37.41  ? 182 TYR   B CA  1 
ATOM   3666 C C   . TYR   B 1 182 ? 24.943  -2.923  49.659 1.00 39.13  ? 182 TYR   B C   1 
ATOM   3667 O O   . TYR   B 1 182 ? 25.949  -3.168  48.986 1.00 35.09  ? 182 TYR   B O   1 
ATOM   3668 C CB  . TYR   B 1 182 ? 23.365  -1.848  48.013 1.00 32.80  ? 182 TYR   B CB  1 
ATOM   3669 C CG  . TYR   B 1 182 ? 22.404  -0.715  47.719 1.00 36.02  ? 182 TYR   B CG  1 
ATOM   3670 C CD1 . TYR   B 1 182 ? 21.095  -0.752  48.189 1.00 37.16  ? 182 TYR   B CD1 1 
ATOM   3671 C CD2 . TYR   B 1 182 ? 22.805  0.394   46.980 1.00 33.47  ? 182 TYR   B CD2 1 
ATOM   3672 C CE1 . TYR   B 1 182 ? 20.211  0.274   47.930 1.00 31.57  ? 182 TYR   B CE1 1 
ATOM   3673 C CE2 . TYR   B 1 182 ? 21.927  1.428   46.711 1.00 31.60  ? 182 TYR   B CE2 1 
ATOM   3674 C CZ  . TYR   B 1 182 ? 20.627  1.362   47.196 1.00 38.99  ? 182 TYR   B CZ  1 
ATOM   3675 O OH  . TYR   B 1 182 ? 19.738  2.380   46.943 1.00 32.97  ? 182 TYR   B OH  1 
ATOM   3676 N N   . GLY   B 1 183 ? 24.579  -3.660  50.704 1.00 34.68  ? 183 GLY   B N   1 
ATOM   3677 C CA  . GLY   B 1 183 ? 25.295  -4.860  51.069 1.00 37.89  ? 183 GLY   B CA  1 
ATOM   3678 C C   . GLY   B 1 183 ? 26.490  -4.602  51.966 1.00 36.89  ? 183 GLY   B C   1 
ATOM   3679 O O   . GLY   B 1 183 ? 26.650  -3.519  52.539 1.00 39.63  ? 183 GLY   B O   1 
ATOM   3680 N N   . PRO   B 1 184 ? 27.355  -5.604  52.103 1.00 34.31  ? 184 PRO   B N   1 
ATOM   3681 C CA  . PRO   B 1 184 ? 28.503  -5.504  53.013 1.00 35.23  ? 184 PRO   B CA  1 
ATOM   3682 C C   . PRO   B 1 184 ? 29.767  -4.939  52.386 1.00 42.07  ? 184 PRO   B C   1 
ATOM   3683 O O   . PRO   B 1 184 ? 30.817  -4.953  53.040 1.00 38.39  ? 184 PRO   B O   1 
ATOM   3684 C CB  . PRO   B 1 184 ? 28.717  -6.968  53.409 1.00 36.87  ? 184 PRO   B CB  1 
ATOM   3685 C CG  . PRO   B 1 184 ? 28.366  -7.715  52.160 1.00 41.82  ? 184 PRO   B CG  1 
ATOM   3686 C CD  . PRO   B 1 184 ? 27.268  -6.934  51.475 1.00 42.71  ? 184 PRO   B CD  1 
ATOM   3687 N N   . PHE   B 1 185 ? 29.698  -4.451  51.152 1.00 35.83  ? 185 PHE   B N   1 
ATOM   3688 C CA  . PHE   B 1 185 ? 30.907  -4.097  50.427 1.00 40.05  ? 185 PHE   B CA  1 
ATOM   3689 C C   . PHE   B 1 185 ? 31.491  -2.788  50.946 1.00 37.90  ? 185 PHE   B C   1 
ATOM   3690 O O   . PHE   B 1 185 ? 30.792  -1.946  51.513 1.00 34.16  ? 185 PHE   B O   1 
ATOM   3691 C CB  . PHE   B 1 185 ? 30.607  -4.010  48.931 1.00 39.27  ? 185 PHE   B CB  1 
ATOM   3692 C CG  . PHE   B 1 185 ? 29.820  -5.183  48.419 1.00 38.05  ? 185 PHE   B CG  1 
ATOM   3693 C CD1 . PHE   B 1 185 ? 30.413  -6.429  48.297 1.00 33.18  ? 185 PHE   B CD1 1 
ATOM   3694 C CD2 . PHE   B 1 185 ? 28.483  -5.048  48.091 1.00 34.41  ? 185 PHE   B CD2 1 
ATOM   3695 C CE1 . PHE   B 1 185 ? 29.686  -7.519  47.845 1.00 48.94  ? 185 PHE   B CE1 1 
ATOM   3696 C CE2 . PHE   B 1 185 ? 27.752  -6.129  47.633 1.00 39.83  ? 185 PHE   B CE2 1 
ATOM   3697 C CZ  . PHE   B 1 185 ? 28.352  -7.366  47.511 1.00 40.40  ? 185 PHE   B CZ  1 
ATOM   3698 N N   . VAL   B 1 186 ? 32.796  -2.636  50.764 1.00 42.25  ? 186 VAL   B N   1 
ATOM   3699 C CA  . VAL   B 1 186 ? 33.515  -1.453  51.209 1.00 36.16  ? 186 VAL   B CA  1 
ATOM   3700 C C   . VAL   B 1 186 ? 34.374  -0.960  50.057 1.00 38.84  ? 186 VAL   B C   1 
ATOM   3701 O O   . VAL   B 1 186 ? 34.743  -1.728  49.162 1.00 34.61  ? 186 VAL   B O   1 
ATOM   3702 C CB  . VAL   B 1 186 ? 34.375  -1.740  52.459 1.00 38.38  ? 186 VAL   B CB  1 
ATOM   3703 C CG1 . VAL   B 1 186 ? 33.483  -1.993  53.666 1.00 51.89  ? 186 VAL   B CG1 1 
ATOM   3704 C CG2 . VAL   B 1 186 ? 35.286  -2.933  52.217 1.00 37.50  ? 186 VAL   B CG2 1 
ATOM   3705 N N   . ASP   B 1 187 ? 34.683  0.336   50.077 1.00 35.74  ? 187 ASP   B N   1 
ATOM   3706 C CA  . ASP   B 1 187 ? 35.498  0.940   49.024 1.00 38.51  ? 187 ASP   B CA  1 
ATOM   3707 C C   . ASP   B 1 187 ? 36.974  0.870   49.418 1.00 40.83  ? 187 ASP   B C   1 
ATOM   3708 O O   . ASP   B 1 187 ? 37.617  1.854   49.786 1.00 37.22  ? 187 ASP   B O   1 
ATOM   3709 C CB  . ASP   B 1 187 ? 35.039  2.364   48.729 1.00 34.75  ? 187 ASP   B CB  1 
ATOM   3710 C CG  . ASP   B 1 187 ? 34.822  3.199   49.982 1.00 38.52  ? 187 ASP   B CG  1 
ATOM   3711 O OD1 . ASP   B 1 187 ? 34.870  2.650   51.102 1.00 43.95  ? 187 ASP   B OD1 1 
ATOM   3712 O OD2 . ASP   B 1 187 ? 34.602  4.420   49.841 1.00 35.09  ? 187 ASP   B OD2 1 
ATOM   3713 N N   . ARG   B 1 188 ? 37.498  -0.352  49.338 1.00 42.56  ? 188 ARG   B N   1 
ATOM   3714 C CA  . ARG   B 1 188 ? 38.914  -0.625  49.539 1.00 44.50  ? 188 ARG   B CA  1 
ATOM   3715 C C   . ARG   B 1 188 ? 39.238  -1.942  48.847 1.00 49.28  ? 188 ARG   B C   1 
ATOM   3716 O O   . ARG   B 1 188 ? 38.350  -2.751  48.563 1.00 41.29  ? 188 ARG   B O   1 
ATOM   3717 C CB  . ARG   B 1 188 ? 39.283  -0.669  51.031 1.00 50.82  ? 188 ARG   B CB  1 
ATOM   3718 C CG  . ARG   B 1 188 ? 38.717  -1.850  51.804 1.00 50.45  ? 188 ARG   B CG  1 
ATOM   3719 C CD  . ARG   B 1 188 ? 39.138  -1.832  53.277 1.00 65.14  ? 188 ARG   B CD  1 
ATOM   3720 N NE  . ARG   B 1 188 ? 38.097  -1.292  54.146 1.00 57.51  ? 188 ARG   B NE  1 
ATOM   3721 C CZ  . ARG   B 1 188 ? 38.124  -0.086  54.696 1.00 70.22  ? 188 ARG   B CZ  1 
ATOM   3722 N NH1 . ARG   B 1 188 ? 39.162  0.721   54.540 1.00 64.53  ? 188 ARG   B NH1 1 
ATOM   3723 N NH2 . ARG   B 1 188 ? 37.092  0.312   55.438 1.00 64.21  ? 188 ARG   B NH2 1 
ATOM   3724 N N   . GLN   B 1 189 ? 40.524  -2.143  48.568 1.00 53.06  ? 189 GLN   B N   1 
ATOM   3725 C CA  . GLN   B 1 189 ? 40.990  -3.331  47.854 1.00 53.32  ? 189 GLN   B CA  1 
ATOM   3726 C C   . GLN   B 1 189 ? 41.184  -4.456  48.862 1.00 55.02  ? 189 GLN   B C   1 
ATOM   3727 O O   . GLN   B 1 189 ? 42.253  -4.610  49.458 1.00 58.82  ? 189 GLN   B O   1 
ATOM   3728 C CB  . GLN   B 1 189 ? 42.275  -3.030  47.092 1.00 54.60  ? 189 GLN   B CB  1 
ATOM   3729 C CG  . GLN   B 1 189 ? 42.741  -4.173  46.214 1.00 60.67  ? 189 GLN   B CG  1 
ATOM   3730 C CD  . GLN   B 1 189 ? 41.657  -4.638  45.265 1.00 66.52  ? 189 GLN   B CD  1 
ATOM   3731 O OE1 . GLN   B 1 189 ? 41.102  -5.728  45.421 1.00 62.51  ? 189 GLN   B OE1 1 
ATOM   3732 N NE2 . GLN   B 1 189 ? 41.344  -3.810  44.274 1.00 65.34  ? 189 GLN   B NE2 1 
ATOM   3733 N N   . THR   B 1 190 ? 40.127  -5.244  49.066 1.00 55.56  ? 190 THR   B N   1 
ATOM   3734 C CA  . THR   B 1 190 ? 40.174  -6.408  49.940 1.00 59.95  ? 190 THR   B CA  1 
ATOM   3735 C C   . THR   B 1 190 ? 39.499  -7.573  49.234 1.00 65.05  ? 190 THR   B C   1 
ATOM   3736 O O   . THR   B 1 190 ? 38.907  -7.419  48.162 1.00 60.78  ? 190 THR   B O   1 
ATOM   3737 C CB  . THR   B 1 190 ? 39.503  -6.138  51.294 1.00 61.74  ? 190 THR   B CB  1 
ATOM   3738 O OG1 . THR   B 1 190 ? 39.691  -4.766  51.648 1.00 66.38  ? 190 THR   B OG1 1 
ATOM   3739 C CG2 . THR   B 1 190 ? 40.115  -7.008  52.387 1.00 66.86  ? 190 THR   B CG2 1 
ATOM   3740 N N   . ALA   B 1 191 ? 39.596  -8.753  49.847 1.00 71.46  ? 191 ALA   B N   1 
ATOM   3741 C CA  . ALA   B 1 191 ? 38.964  -9.962  49.323 1.00 63.82  ? 191 ALA   B CA  1 
ATOM   3742 C C   . ALA   B 1 191 ? 37.465  -9.877  49.596 1.00 67.81  ? 191 ALA   B C   1 
ATOM   3743 O O   . ALA   B 1 191 ? 36.929  -10.468 50.536 1.00 74.00  ? 191 ALA   B O   1 
ATOM   3744 C CB  . ALA   B 1 191 ? 39.584  -11.206 49.946 1.00 64.03  ? 191 ALA   B CB  1 
ATOM   3745 N N   . GLN   B 1 192 ? 36.778  -9.111  48.755 1.00 69.56  ? 192 GLN   B N   1 
ATOM   3746 C CA  . GLN   B 1 192 ? 35.335  -8.960  48.864 1.00 64.54  ? 192 GLN   B CA  1 
ATOM   3747 C C   . GLN   B 1 192 ? 34.642  -9.970  47.965 1.00 58.47  ? 192 GLN   B C   1 
ATOM   3748 O O   . GLN   B 1 192 ? 35.124  -10.281 46.871 1.00 68.03  ? 192 GLN   B O   1 
ATOM   3749 C CB  . GLN   B 1 192 ? 34.902  -7.544  48.486 1.00 53.74  ? 192 GLN   B CB  1 
ATOM   3750 C CG  . GLN   B 1 192 ? 35.734  -6.454  49.122 1.00 52.82  ? 192 GLN   B CG  1 
ATOM   3751 C CD  . GLN   B 1 192 ? 35.106  -5.097  48.948 1.00 44.70  ? 192 GLN   B CD  1 
ATOM   3752 O OE1 . GLN   B 1 192 ? 33.923  -4.915  49.224 1.00 49.17  ? 192 GLN   B OE1 1 
ATOM   3753 N NE2 . GLN   B 1 192 ? 35.889  -4.135  48.478 1.00 42.07  ? 192 GLN   B NE2 1 
ATOM   3754 N N   . ALA   B 1 193 ? 33.505  -10.478 48.429 1.00 57.44  ? 193 ALA   B N   1 
ATOM   3755 C CA  . ALA   B 1 193 ? 32.776  -11.492 47.684 1.00 61.44  ? 193 ALA   B CA  1 
ATOM   3756 C C   . ALA   B 1 193 ? 31.284  -11.296 47.898 1.00 61.86  ? 193 ALA   B C   1 
ATOM   3757 O O   . ALA   B 1 193 ? 30.836  -11.089 49.030 1.00 58.04  ? 193 ALA   B O   1 
ATOM   3758 C CB  . ALA   B 1 193 ? 33.197  -12.899 48.116 1.00 60.31  ? 193 ALA   B CB  1 
ATOM   3759 N N   . ALA   B 1 194 ? 30.524  -11.359 46.811 1.00 63.55  ? 194 ALA   B N   1 
ATOM   3760 C CA  . ALA   B 1 194 ? 29.076  -11.302 46.925 1.00 59.23  ? 194 ALA   B CA  1 
ATOM   3761 C C   . ALA   B 1 194 ? 28.549  -12.619 47.477 1.00 57.83  ? 194 ALA   B C   1 
ATOM   3762 O O   . ALA   B 1 194 ? 29.031  -13.698 47.117 1.00 61.80  ? 194 ALA   B O   1 
ATOM   3763 C CB  . ALA   B 1 194 ? 28.444  -11.005 45.566 1.00 53.94  ? 194 ALA   B CB  1 
ATOM   3764 N N   . GLY   B 1 195 ? 27.562  -12.527 48.363 1.00 49.90  ? 195 GLY   B N   1 
ATOM   3765 C CA  . GLY   B 1 195 ? 26.945  -13.705 48.929 1.00 54.13  ? 195 GLY   B CA  1 
ATOM   3766 C C   . GLY   B 1 195 ? 26.170  -14.490 47.886 1.00 55.69  ? 195 GLY   B C   1 
ATOM   3767 O O   . GLY   B 1 195 ? 26.072  -14.121 46.714 1.00 56.97  ? 195 GLY   B O   1 
ATOM   3768 N N   . THR   B 1 196 ? 25.605  -15.609 48.333 1.00 51.06  ? 196 THR   B N   1 
ATOM   3769 C CA  . THR   B 1 196 ? 24.835  -16.457 47.434 1.00 56.47  ? 196 THR   B CA  1 
ATOM   3770 C C   . THR   B 1 196 ? 23.603  -15.701 46.950 1.00 52.16  ? 196 THR   B C   1 
ATOM   3771 O O   . THR   B 1 196 ? 22.822  -15.184 47.756 1.00 51.64  ? 196 THR   B O   1 
ATOM   3772 C CB  . THR   B 1 196 ? 24.434  -17.760 48.123 1.00 52.87  ? 196 THR   B CB  1 
ATOM   3773 O OG1 . THR   B 1 196 ? 23.617  -17.477 49.264 1.00 63.30  ? 196 THR   B OG1 1 
ATOM   3774 C CG2 . THR   B 1 196 ? 25.668  -18.533 48.559 1.00 52.19  ? 196 THR   B CG2 1 
ATOM   3775 N N   . ASP   B 1 197 ? 23.441  -15.620 45.637 1.00 55.61  ? 197 ASP   B N   1 
ATOM   3776 C CA  . ASP   B 1 197 ? 22.295  -14.940 45.062 1.00 58.19  ? 197 ASP   B CA  1 
ATOM   3777 C C   . ASP   B 1 197 ? 21.121  -15.901 44.951 1.00 56.16  ? 197 ASP   B C   1 
ATOM   3778 O O   . ASP   B 1 197 ? 21.292  -17.116 44.811 1.00 70.16  ? 197 ASP   B O   1 
ATOM   3779 C CB  . ASP   B 1 197 ? 22.623  -14.364 43.685 1.00 52.32  ? 197 ASP   B CB  1 
ATOM   3780 C CG  . ASP   B 1 197 ? 21.638  -13.292 43.262 1.00 56.72  ? 197 ASP   B CG  1 
ATOM   3781 O OD1 . ASP   B 1 197 ? 20.912  -12.777 44.144 1.00 57.36  ? 197 ASP   B OD1 1 
ATOM   3782 O OD2 . ASP   B 1 197 ? 21.585  -12.970 42.056 1.00 54.69  ? 197 ASP   B OD2 1 
ATOM   3783 N N   . THR   B 1 198 ? 19.921  -15.344 45.018 1.00 58.64  ? 198 THR   B N   1 
ATOM   3784 C CA  . THR   B 1 198 ? 18.700  -16.120 44.905 1.00 56.34  ? 198 THR   B CA  1 
ATOM   3785 C C   . THR   B 1 198 ? 17.793  -15.462 43.875 1.00 51.76  ? 198 THR   B C   1 
ATOM   3786 O O   . THR   B 1 198 ? 18.008  -14.318 43.472 1.00 50.93  ? 198 THR   B O   1 
ATOM   3787 C CB  . THR   B 1 198 ? 18.004  -16.249 46.268 1.00 58.45  ? 198 THR   B CB  1 
ATOM   3788 O OG1 . THR   B 1 198 ? 17.890  -14.955 46.871 1.00 59.24  ? 198 THR   B OG1 1 
ATOM   3789 C CG2 . THR   B 1 198 ? 18.821  -17.148 47.188 1.00 48.30  ? 198 THR   B CG2 1 
ATOM   3790 N N   . THR   B 1 199 ? 16.781  -16.206 43.436 1.00 46.17  ? 199 THR   B N   1 
ATOM   3791 C CA  . THR   B 1 199 ? 15.865  -15.735 42.406 1.00 43.91  ? 199 THR   B CA  1 
ATOM   3792 C C   . THR   B 1 199 ? 14.663  -15.041 43.042 1.00 55.11  ? 199 THR   B C   1 
ATOM   3793 O O   . THR   B 1 199 ? 14.067  -15.555 43.995 1.00 51.57  ? 199 THR   B O   1 
ATOM   3794 C CB  . THR   B 1 199 ? 15.411  -16.899 41.523 1.00 50.91  ? 199 THR   B CB  1 
ATOM   3795 O OG1 . THR   B 1 199 ? 16.560  -17.550 40.960 1.00 40.40  ? 199 THR   B OG1 1 
ATOM   3796 C CG2 . THR   B 1 199 ? 14.525  -16.397 40.398 1.00 43.42  ? 199 THR   B CG2 1 
ATOM   3797 N N   . ILE   B 1 200 ? 14.311  -13.873 42.503 1.00 43.46  ? 200 ILE   B N   1 
ATOM   3798 C CA  . ILE   B 1 200 ? 13.243  -13.023 43.029 1.00 43.91  ? 200 ILE   B CA  1 
ATOM   3799 C C   . ILE   B 1 200 ? 11.910  -13.608 42.567 1.00 45.51  ? 200 ILE   B C   1 
ATOM   3800 O O   . ILE   B 1 200 ? 11.457  -13.338 41.454 1.00 38.16  ? 200 ILE   B O   1 
ATOM   3801 C CB  . ILE   B 1 200 ? 13.403  -11.571 42.575 1.00 42.68  ? 200 ILE   B CB  1 
ATOM   3802 C CG1 . ILE   B 1 200 ? 14.807  -11.056 42.890 1.00 47.60  ? 200 ILE   B CG1 1 
ATOM   3803 C CG2 . ILE   B 1 200 ? 12.336  -10.692 43.204 1.00 37.67  ? 200 ILE   B CG2 1 
ATOM   3804 C CD1 . ILE   B 1 200 ? 15.244  -9.919  41.978 1.00 43.79  ? 200 ILE   B CD1 1 
ATOM   3805 N N   . THR   B 1 201 ? 11.254  -14.371 43.445 1.00 48.53  ? 201 THR   B N   1 
ATOM   3806 C CA  . THR   B 1 201 ? 10.094  -15.163 43.043 1.00 41.13  ? 201 THR   B CA  1 
ATOM   3807 C C   . THR   B 1 201 ? 8.939   -14.288 42.566 1.00 35.95  ? 201 THR   B C   1 
ATOM   3808 O O   . THR   B 1 201 ? 8.301   -14.598 41.553 1.00 45.74  ? 201 THR   B O   1 
ATOM   3809 C CB  . THR   B 1 201 ? 9.645   -16.051 44.205 1.00 45.66  ? 201 THR   B CB  1 
ATOM   3810 O OG1 . THR   B 1 201 ? 10.726  -16.902 44.604 1.00 39.68  ? 201 THR   B OG1 1 
ATOM   3811 C CG2 . THR   B 1 201 ? 8.459   -16.910 43.790 1.00 45.01  ? 201 THR   B CG2 1 
ATOM   3812 N N   . VAL   B 1 202 ? 8.647   -13.199 43.279 1.00 37.60  ? 202 VAL   B N   1 
ATOM   3813 C CA  . VAL   B 1 202 ? 7.517   -12.357 42.898 1.00 43.76  ? 202 VAL   B CA  1 
ATOM   3814 C C   . VAL   B 1 202 ? 7.737   -11.755 41.515 1.00 40.27  ? 202 VAL   B C   1 
ATOM   3815 O O   . VAL   B 1 202 ? 6.778   -11.536 40.763 1.00 39.76  ? 202 VAL   B O   1 
ATOM   3816 C CB  . VAL   B 1 202 ? 7.270   -11.276 43.973 1.00 46.33  ? 202 VAL   B CB  1 
ATOM   3817 C CG1 . VAL   B 1 202 ? 8.510   -10.420 44.181 1.00 47.01  ? 202 VAL   B CG1 1 
ATOM   3818 C CG2 . VAL   B 1 202 ? 6.059   -10.418 43.612 1.00 49.63  ? 202 VAL   B CG2 1 
ATOM   3819 N N   . ASN   B 1 203 ? 8.996   -11.511 41.143 1.00 44.83  ? 203 ASN   B N   1 
ATOM   3820 C CA  . ASN   B 1 203 ? 9.294   -10.970 39.820 1.00 44.85  ? 203 ASN   B CA  1 
ATOM   3821 C C   . ASN   B 1 203 ? 9.091   -12.017 38.727 1.00 44.53  ? 203 ASN   B C   1 
ATOM   3822 O O   . ASN   B 1 203 ? 8.568   -11.698 37.653 1.00 41.70  ? 203 ASN   B O   1 
ATOM   3823 C CB  . ASN   B 1 203 ? 10.722  -10.423 39.791 1.00 44.06  ? 203 ASN   B CB  1 
ATOM   3824 C CG  . ASN   B 1 203 ? 10.855  -9.093  40.519 1.00 42.17  ? 203 ASN   B CG  1 
ATOM   3825 O OD1 . ASN   B 1 203 ? 9.929   -8.646  41.195 1.00 43.46  ? 203 ASN   B OD1 1 
ATOM   3826 N ND2 . ASN   B 1 203 ? 12.015  -8.455  40.382 1.00 47.17  ? 203 ASN   B ND2 1 
ATOM   3827 N N   . VAL   B 1 204 ? 9.502   -13.267 38.971 1.00 46.18  ? 204 VAL   B N   1 
ATOM   3828 C CA  . VAL   B 1 204 ? 9.261   -14.329 37.992 1.00 46.01  ? 204 VAL   B CA  1 
ATOM   3829 C C   . VAL   B 1 204 ? 7.767   -14.502 37.756 1.00 48.42  ? 204 VAL   B C   1 
ATOM   3830 O O   . VAL   B 1 204 ? 7.318   -14.670 36.614 1.00 45.27  ? 204 VAL   B O   1 
ATOM   3831 C CB  . VAL   B 1 204 ? 9.906   -15.654 38.444 1.00 39.61  ? 204 VAL   B CB  1 
ATOM   3832 C CG1 . VAL   B 1 204 ? 9.505   -16.785 37.501 1.00 46.23  ? 204 VAL   B CG1 1 
ATOM   3833 C CG2 . VAL   B 1 204 ? 11.413  -15.536 38.501 1.00 39.59  ? 204 VAL   B CG2 1 
ATOM   3834 N N   . LEU   B 1 205 ? 6.976   -14.468 38.832 1.00 45.67  ? 205 LEU   B N   1 
ATOM   3835 C CA  . LEU   B 1 205 ? 5.528   -14.595 38.702 1.00 51.70  ? 205 LEU   B CA  1 
ATOM   3836 C C   . LEU   B 1 205 ? 4.940   -13.442 37.901 1.00 48.58  ? 205 LEU   B C   1 
ATOM   3837 O O   . LEU   B 1 205 ? 4.070   -13.650 37.046 1.00 45.82  ? 205 LEU   B O   1 
ATOM   3838 C CB  . LEU   B 1 205 ? 4.880   -14.660 40.085 1.00 46.13  ? 205 LEU   B CB  1 
ATOM   3839 C CG  . LEU   B 1 205 ? 5.226   -15.878 40.934 1.00 46.79  ? 205 LEU   B CG  1 
ATOM   3840 C CD1 . LEU   B 1 205 ? 4.599   -15.749 42.310 1.00 50.08  ? 205 LEU   B CD1 1 
ATOM   3841 C CD2 . LEU   B 1 205 ? 4.751   -17.139 40.240 1.00 52.49  ? 205 LEU   B CD2 1 
ATOM   3842 N N   . ALA   B 1 206 ? 5.385   -12.214 38.179 1.00 44.34  ? 206 ALA   B N   1 
ATOM   3843 C CA  . ALA   B 1 206 ? 4.943   -11.081 37.373 1.00 43.50  ? 206 ALA   B CA  1 
ATOM   3844 C C   . ALA   B 1 206 ? 5.334   -11.266 35.916 1.00 39.39  ? 206 ALA   B C   1 
ATOM   3845 O O   . ALA   B 1 206 ? 4.565   -10.919 35.013 1.00 45.03  ? 206 ALA   B O   1 
ATOM   3846 C CB  . ALA   B 1 206 ? 5.530   -9.781  37.921 1.00 42.56  ? 206 ALA   B CB  1 
ATOM   3847 N N   . TRP   B 1 207 ? 6.513   -11.837 35.673 1.00 40.58  ? 207 TRP   B N   1 
ATOM   3848 C CA  . TRP   B 1 207 ? 6.978   -12.052 34.309 1.00 46.66  ? 207 TRP   B CA  1 
ATOM   3849 C C   . TRP   B 1 207 ? 6.131   -13.102 33.596 1.00 49.44  ? 207 TRP   B C   1 
ATOM   3850 O O   . TRP   B 1 207 ? 5.777   -12.931 32.422 1.00 45.33  ? 207 TRP   B O   1 
ATOM   3851 C CB  . TRP   B 1 207 ? 8.454   -12.445 34.343 1.00 41.06  ? 207 TRP   B CB  1 
ATOM   3852 C CG  . TRP   B 1 207 ? 9.053   -12.770 33.026 1.00 52.52  ? 207 TRP   B CG  1 
ATOM   3853 C CD1 . TRP   B 1 207 ? 9.376   -11.895 32.027 1.00 52.67  ? 207 TRP   B CD1 1 
ATOM   3854 C CD2 . TRP   B 1 207 ? 9.436   -14.068 32.566 1.00 46.57  ? 207 TRP   B CD2 1 
ATOM   3855 N NE1 . TRP   B 1 207 ? 9.926   -12.575 30.966 1.00 46.46  ? 207 TRP   B NE1 1 
ATOM   3856 C CE2 . TRP   B 1 207 ? 9.973   -13.910 31.274 1.00 53.13  ? 207 TRP   B CE2 1 
ATOM   3857 C CE3 . TRP   B 1 207 ? 9.369   -15.349 33.118 1.00 50.22  ? 207 TRP   B CE3 1 
ATOM   3858 C CZ2 . TRP   B 1 207 ? 10.441  -14.988 30.526 1.00 54.39  ? 207 TRP   B CZ2 1 
ATOM   3859 C CZ3 . TRP   B 1 207 ? 9.834   -16.417 32.375 1.00 49.87  ? 207 TRP   B CZ3 1 
ATOM   3860 C CH2 . TRP   B 1 207 ? 10.363  -16.230 31.095 1.00 48.75  ? 207 TRP   B CH2 1 
ATOM   3861 N N   . LEU   B 1 208 ? 5.777   -14.186 34.293 1.00 46.52  ? 208 LEU   B N   1 
ATOM   3862 C CA  . LEU   B 1 208 ? 4.882   -15.182 33.708 1.00 46.07  ? 208 LEU   B CA  1 
ATOM   3863 C C   . LEU   B 1 208 ? 3.513   -14.583 33.409 1.00 42.18  ? 208 LEU   B C   1 
ATOM   3864 O O   . LEU   B 1 208 ? 2.883   -14.932 32.403 1.00 46.74  ? 208 LEU   B O   1 
ATOM   3865 C CB  . LEU   B 1 208 ? 4.751   -16.387 34.640 1.00 47.12  ? 208 LEU   B CB  1 
ATOM   3866 C CG  . LEU   B 1 208 ? 6.044   -17.152 34.922 1.00 48.24  ? 208 LEU   B CG  1 
ATOM   3867 C CD1 . LEU   B 1 208 ? 5.814   -18.219 35.981 1.00 48.67  ? 208 LEU   B CD1 1 
ATOM   3868 C CD2 . LEU   B 1 208 ? 6.602   -17.770 33.647 1.00 50.72  ? 208 LEU   B CD2 1 
ATOM   3869 N N   . TYR   B 1 209 ? 3.035   -13.683 34.274 1.00 45.11  ? 209 TYR   B N   1 
ATOM   3870 C CA  . TYR   B 1 209 ? 1.820   -12.930 33.974 1.00 40.05  ? 209 TYR   B CA  1 
ATOM   3871 C C   . TYR   B 1 209 ? 1.992   -12.104 32.706 1.00 49.33  ? 209 TYR   B C   1 
ATOM   3872 O O   . TYR   B 1 209 ? 1.129   -12.112 31.820 1.00 46.36  ? 209 TYR   B O   1 
ATOM   3873 C CB  . TYR   B 1 209 ? 1.457   -12.026 35.153 1.00 49.96  ? 209 TYR   B CB  1 
ATOM   3874 C CG  . TYR   B 1 209 ? 0.662   -12.711 36.238 1.00 50.90  ? 209 TYR   B CG  1 
ATOM   3875 C CD1 . TYR   B 1 209 ? -0.443  -13.493 35.927 1.00 57.00  ? 209 TYR   B CD1 1 
ATOM   3876 C CD2 . TYR   B 1 209 ? 1.014   -12.575 37.573 1.00 48.98  ? 209 TYR   B CD2 1 
ATOM   3877 C CE1 . TYR   B 1 209 ? -1.177  -14.122 36.914 1.00 59.45  ? 209 TYR   B CE1 1 
ATOM   3878 C CE2 . TYR   B 1 209 ? 0.287   -13.200 38.568 1.00 61.06  ? 209 TYR   B CE2 1 
ATOM   3879 C CZ  . TYR   B 1 209 ? -0.807  -13.972 38.233 1.00 63.37  ? 209 TYR   B CZ  1 
ATOM   3880 O OH  . TYR   B 1 209 ? -1.536  -14.597 39.218 1.00 63.88  ? 209 TYR   B OH  1 
ATOM   3881 N N   . ALA   B 1 210 ? 3.105   -11.371 32.611 1.00 49.11  ? 210 ALA   B N   1 
ATOM   3882 C CA  . ALA   B 1 210 ? 3.410   -10.636 31.387 1.00 51.00  ? 210 ALA   B CA  1 
ATOM   3883 C C   . ALA   B 1 210 ? 3.379   -11.558 30.177 1.00 47.18  ? 210 ALA   B C   1 
ATOM   3884 O O   . ALA   B 1 210 ? 2.861   -11.188 29.117 1.00 49.00  ? 210 ALA   B O   1 
ATOM   3885 C CB  . ALA   B 1 210 ? 4.776   -9.960  31.508 1.00 48.20  ? 210 ALA   B CB  1 
ATOM   3886 N N   . ALA   B 1 211 ? 3.917   -12.771 30.325 1.00 44.05  ? 211 ALA   B N   1 
ATOM   3887 C CA  . ALA   B 1 211 ? 3.904   -13.738 29.233 1.00 42.18  ? 211 ALA   B CA  1 
ATOM   3888 C C   . ALA   B 1 211 ? 2.483   -14.122 28.846 1.00 49.14  ? 211 ALA   B C   1 
ATOM   3889 O O   . ALA   B 1 211 ? 2.156   -14.208 27.656 1.00 48.40  ? 211 ALA   B O   1 
ATOM   3890 C CB  . ALA   B 1 211 ? 4.695   -14.980 29.632 1.00 48.11  ? 211 ALA   B CB  1 
ATOM   3891 N N   . VAL   B 1 212 ? 1.630   -14.373 29.838 1.00 45.12  ? 212 VAL   B N   1 
ATOM   3892 C CA  . VAL   B 1 212 ? 0.234   -14.692 29.556 1.00 53.35  ? 212 VAL   B CA  1 
ATOM   3893 C C   . VAL   B 1 212 ? -0.447  -13.520 28.862 1.00 49.35  ? 212 VAL   B C   1 
ATOM   3894 O O   . VAL   B 1 212 ? -1.225  -13.704 27.916 1.00 47.11  ? 212 VAL   B O   1 
ATOM   3895 C CB  . VAL   B 1 212 ? -0.482  -15.091 30.860 1.00 46.44  ? 212 VAL   B CB  1 
ATOM   3896 C CG1 . VAL   B 1 212 ? -1.988  -15.118 30.674 1.00 53.20  ? 212 VAL   B CG1 1 
ATOM   3897 C CG2 . VAL   B 1 212 ? 0.026   -16.446 31.333 1.00 54.66  ? 212 VAL   B CG2 1 
ATOM   3898 N N   . ILE   B 1 213 ? -0.151  -12.295 29.307 1.00 51.97  ? 213 ILE   B N   1 
ATOM   3899 C CA  . ILE   B 1 213 ? -0.691  -11.102 28.656 1.00 50.57  ? 213 ILE   B CA  1 
ATOM   3900 C C   . ILE   B 1 213 ? -0.269  -11.050 27.193 1.00 49.38  ? 213 ILE   B C   1 
ATOM   3901 O O   . ILE   B 1 213 ? -1.027  -10.583 26.334 1.00 51.92  ? 213 ILE   B O   1 
ATOM   3902 C CB  . ILE   B 1 213 ? -0.255  -9.835  29.425 1.00 53.71  ? 213 ILE   B CB  1 
ATOM   3903 C CG1 . ILE   B 1 213 ? -0.834  -9.848  30.839 1.00 49.28  ? 213 ILE   B CG1 1 
ATOM   3904 C CG2 . ILE   B 1 213 ? -0.720  -8.575  28.718 1.00 54.55  ? 213 ILE   B CG2 1 
ATOM   3905 C CD1 . ILE   B 1 213 ? -0.251  -8.795  31.767 1.00 46.10  ? 213 ILE   B CD1 1 
ATOM   3906 N N   . ASN   B 1 214 ? 0.930   -11.549 26.878 1.00 46.61  ? 214 ASN   B N   1 
ATOM   3907 C CA  . ASN   B 1 214 ? 1.452   -11.510 25.515 1.00 53.81  ? 214 ASN   B CA  1 
ATOM   3908 C C   . ASN   B 1 214 ? 1.017   -12.694 24.666 1.00 56.43  ? 214 ASN   B C   1 
ATOM   3909 O O   . ASN   B 1 214 ? 1.349   -12.736 23.477 1.00 59.48  ? 214 ASN   B O   1 
ATOM   3910 C CB  . ASN   B 1 214 ? 2.980   -11.460 25.510 1.00 51.94  ? 214 ASN   B CB  1 
ATOM   3911 C CG  . ASN   B 1 214 ? 3.521   -10.048 25.637 1.00 60.17  ? 214 ASN   B CG  1 
ATOM   3912 O OD1 . ASN   B 1 214 ? 3.594   -9.300  24.661 1.00 52.53  ? 214 ASN   B OD1 1 
ATOM   3913 N ND2 . ASN   B 1 214 ? 3.940   -9.690  26.838 1.00 59.87  ? 214 ASN   B ND2 1 
ATOM   3914 N N   . GLY   B 1 215 ? 0.291   -13.654 25.231 1.00 59.09  ? 215 GLY   B N   1 
ATOM   3915 C CA  . GLY   B 1 215 ? -0.171  -14.794 24.471 1.00 59.62  ? 215 GLY   B CA  1 
ATOM   3916 C C   . GLY   B 1 215 ? 0.604   -16.074 24.685 1.00 61.04  ? 215 GLY   B C   1 
ATOM   3917 O O   . GLY   B 1 215 ? 0.276   -17.082 24.053 1.00 63.73  ? 215 GLY   B O   1 
ATOM   3918 N N   . ASP   B 1 216 ? 1.621   -16.072 25.547 1.00 53.52  ? 216 ASP   B N   1 
ATOM   3919 C CA  . ASP   B 1 216 ? 2.363   -17.289 25.881 1.00 57.63  ? 216 ASP   B CA  1 
ATOM   3920 C C   . ASP   B 1 216 ? 1.647   -17.984 27.033 1.00 60.66  ? 216 ASP   B C   1 
ATOM   3921 O O   . ASP   B 1 216 ? 1.736   -17.553 28.185 1.00 53.75  ? 216 ASP   B O   1 
ATOM   3922 C CB  . ASP   B 1 216 ? 3.808   -16.965 26.237 1.00 56.93  ? 216 ASP   B CB  1 
ATOM   3923 C CG  . ASP   B 1 216 ? 4.588   -16.416 25.060 1.00 66.54  ? 216 ASP   B CG  1 
ATOM   3924 O OD1 . ASP   B 1 216 ? 3.957   -16.068 24.035 1.00 63.55  ? 216 ASP   B OD1 1 
ATOM   3925 O OD2 . ASP   B 1 216 ? 5.834   -16.340 25.165 1.00 62.73  ? 216 ASP   B OD2 1 
ATOM   3926 N N   . ARG   B 1 217 ? 0.925   -19.065 26.722 1.00 61.13  ? 217 ARG   B N   1 
ATOM   3927 C CA  . ARG   B 1 217 ? 0.133   -19.772 27.720 1.00 62.03  ? 217 ARG   B CA  1 
ATOM   3928 C C   . ARG   B 1 217 ? 0.476   -21.257 27.802 1.00 62.50  ? 217 ARG   B C   1 
ATOM   3929 O O   . ARG   B 1 217 ? -0.211  -21.996 28.516 1.00 58.03  ? 217 ARG   B O   1 
ATOM   3930 C CB  . ARG   B 1 217 ? -1.367  -19.610 27.437 1.00 59.51  ? 217 ARG   B CB  1 
ATOM   3931 C CG  . ARG   B 1 217 ? -1.753  -18.325 26.710 1.00 61.72  ? 217 ARG   B CG  1 
ATOM   3932 C CD  . ARG   B 1 217 ? -2.748  -17.502 27.516 1.00 67.48  ? 217 ARG   B CD  1 
ATOM   3933 N NE  . ARG   B 1 217 ? -3.737  -18.352 28.166 1.00 71.48  ? 217 ARG   B NE  1 
ATOM   3934 C CZ  . ARG   B 1 217 ? -4.609  -17.936 29.075 1.00 75.19  ? 217 ARG   B CZ  1 
ATOM   3935 N NH1 . ARG   B 1 217 ? -4.671  -16.666 29.443 1.00 70.14  ? 217 ARG   B NH1 1 
ATOM   3936 N NH2 . ARG   B 1 217 ? -5.437  -18.817 29.631 1.00 75.01  ? 217 ARG   B NH2 1 
ATOM   3937 N N   . TRP   B 1 218 ? 1.524   -21.710 27.104 1.00 65.14  ? 218 TRP   B N   1 
ATOM   3938 C CA  . TRP   B 1 218 ? 1.830   -23.137 27.037 1.00 58.35  ? 218 TRP   B CA  1 
ATOM   3939 C C   . TRP   B 1 218 ? 2.193   -23.725 28.391 1.00 62.00  ? 218 TRP   B C   1 
ATOM   3940 O O   . TRP   B 1 218 ? 2.047   -24.935 28.586 1.00 65.81  ? 218 TRP   B O   1 
ATOM   3941 C CB  . TRP   B 1 218 ? 2.971   -23.393 26.049 1.00 60.75  ? 218 TRP   B CB  1 
ATOM   3942 C CG  . TRP   B 1 218 ? 4.302   -22.864 26.504 1.00 63.24  ? 218 TRP   B CG  1 
ATOM   3943 C CD1 . TRP   B 1 218 ? 4.793   -21.606 26.306 1.00 66.29  ? 218 TRP   B CD1 1 
ATOM   3944 C CD2 . TRP   B 1 218 ? 5.316   -23.581 27.222 1.00 62.60  ? 218 TRP   B CD2 1 
ATOM   3945 N NE1 . TRP   B 1 218 ? 6.045   -21.493 26.859 1.00 65.04  ? 218 TRP   B NE1 1 
ATOM   3946 C CE2 . TRP   B 1 218 ? 6.390   -22.691 27.427 1.00 64.13  ? 218 TRP   B CE2 1 
ATOM   3947 C CE3 . TRP   B 1 218 ? 5.419   -24.887 27.712 1.00 65.35  ? 218 TRP   B CE3 1 
ATOM   3948 C CZ2 . TRP   B 1 218 ? 7.551   -23.063 28.102 1.00 62.15  ? 218 TRP   B CZ2 1 
ATOM   3949 C CZ3 . TRP   B 1 218 ? 6.575   -25.255 28.382 1.00 67.07  ? 218 TRP   B CZ3 1 
ATOM   3950 C CH2 . TRP   B 1 218 ? 7.625   -24.346 28.571 1.00 66.69  ? 218 TRP   B CH2 1 
ATOM   3951 N N   . PHE   B 1 219 ? 2.671   -22.905 29.321 1.00 63.60  ? 219 PHE   B N   1 
ATOM   3952 C CA  . PHE   B 1 219 ? 3.044   -23.366 30.649 1.00 59.31  ? 219 PHE   B CA  1 
ATOM   3953 C C   . PHE   B 1 219 ? 1.872   -23.394 31.620 1.00 58.04  ? 219 PHE   B C   1 
ATOM   3954 O O   . PHE   B 1 219 ? 1.997   -23.988 32.696 1.00 63.40  ? 219 PHE   B O   1 
ATOM   3955 C CB  . PHE   B 1 219 ? 4.159   -22.477 31.214 1.00 56.54  ? 219 PHE   B CB  1 
ATOM   3956 C CG  . PHE   B 1 219 ? 3.840   -21.009 31.173 1.00 55.44  ? 219 PHE   B CG  1 
ATOM   3957 C CD1 . PHE   B 1 219 ? 4.162   -20.245 30.062 1.00 58.13  ? 219 PHE   B CD1 1 
ATOM   3958 C CD2 . PHE   B 1 219 ? 3.217   -20.393 32.245 1.00 59.10  ? 219 PHE   B CD2 1 
ATOM   3959 C CE1 . PHE   B 1 219 ? 3.867   -18.895 30.023 1.00 56.17  ? 219 PHE   B CE1 1 
ATOM   3960 C CE2 . PHE   B 1 219 ? 2.919   -19.044 32.211 1.00 55.48  ? 219 PHE   B CE2 1 
ATOM   3961 C CZ  . PHE   B 1 219 ? 3.244   -18.294 31.098 1.00 50.92  ? 219 PHE   B CZ  1 
ATOM   3962 N N   . LEU   B 1 220 ? 0.747   -22.770 31.274 1.00 58.41  ? 220 LEU   B N   1 
ATOM   3963 C CA  . LEU   B 1 220 ? -0.403  -22.747 32.169 1.00 61.94  ? 220 LEU   B CA  1 
ATOM   3964 C C   . LEU   B 1 220 ? -0.989  -24.148 32.313 1.00 66.93  ? 220 LEU   B C   1 
ATOM   3965 O O   . LEU   B 1 220 ? -1.178  -24.862 31.322 1.00 61.87  ? 220 LEU   B O   1 
ATOM   3966 C CB  . LEU   B 1 220 ? -1.459  -21.770 31.653 1.00 59.39  ? 220 LEU   B CB  1 
ATOM   3967 C CG  . LEU   B 1 220 ? -1.107  -20.282 31.753 1.00 59.24  ? 220 LEU   B CG  1 
ATOM   3968 C CD1 . LEU   B 1 220 ? -2.234  -19.409 31.218 1.00 55.94  ? 220 LEU   B CD1 1 
ATOM   3969 C CD2 . LEU   B 1 220 ? -0.772  -19.906 33.191 1.00 56.63  ? 220 LEU   B CD2 1 
ATOM   3970 N N   . ASN   B 1 221 ? -1.274  -24.541 33.549 1.00 62.63  ? 221 ASN   B N   1 
ATOM   3971 C CA  . ASN   B 1 221 ? -1.726  -25.887 33.871 1.00 69.06  ? 221 ASN   B CA  1 
ATOM   3972 C C   . ASN   B 1 221 ? -3.161  -25.862 34.391 1.00 70.66  ? 221 ASN   B C   1 
ATOM   3973 O O   . ASN   B 1 221 ? -3.798  -24.809 34.497 1.00 69.91  ? 221 ASN   B O   1 
ATOM   3974 C CB  . ASN   B 1 221 ? -0.787  -26.536 34.892 1.00 70.66  ? 221 ASN   B CB  1 
ATOM   3975 C CG  . ASN   B 1 221 ? -0.694  -25.749 36.197 1.00 71.01  ? 221 ASN   B CG  1 
ATOM   3976 O OD1 . ASN   B 1 221 ? -1.406  -24.763 36.403 1.00 69.30  ? 221 ASN   B OD1 1 
ATOM   3977 N ND2 . ASN   B 1 221 ? 0.188   -26.191 37.085 1.00 70.92  ? 221 ASN   B ND2 1 
ATOM   3978 N N   . ARG   B 1 222 ? -3.667  -27.053 34.719 1.00 78.31  ? 222 ARG   B N   1 
ATOM   3979 C CA  . ARG   B 1 222 ? -4.941  -27.200 35.408 1.00 79.27  ? 222 ARG   B CA  1 
ATOM   3980 C C   . ARG   B 1 222 ? -4.781  -27.390 36.909 1.00 75.18  ? 222 ARG   B C   1 
ATOM   3981 O O   . ARG   B 1 222 ? -5.767  -27.258 37.643 1.00 78.73  ? 222 ARG   B O   1 
ATOM   3982 C CB  . ARG   B 1 222 ? -5.727  -28.384 34.830 1.00 75.49  ? 222 ARG   B CB  1 
ATOM   3983 N N   . PHE   B 1 223 ? -3.573  -27.690 37.380 1.00 72.84  ? 223 PHE   B N   1 
ATOM   3984 C CA  . PHE   B 1 223 ? -3.355  -27.921 38.798 1.00 62.29  ? 223 PHE   B CA  1 
ATOM   3985 C C   . PHE   B 1 223 ? -3.140  -26.601 39.526 1.00 62.97  ? 223 PHE   B C   1 
ATOM   3986 O O   . PHE   B 1 223 ? -2.774  -25.586 38.928 1.00 61.76  ? 223 PHE   B O   1 
ATOM   3987 C CB  . PHE   B 1 223 ? -2.155  -28.844 39.005 1.00 62.25  ? 223 PHE   B CB  1 
ATOM   3988 C CG  . PHE   B 1 223 ? -1.822  -29.668 37.796 1.00 76.67  ? 223 PHE   B CG  1 
ATOM   3989 C CD1 . PHE   B 1 223 ? -2.552  -30.801 37.484 1.00 79.02  ? 223 PHE   B CD1 1 
ATOM   3990 C CD2 . PHE   B 1 223 ? -0.788  -29.297 36.957 1.00 81.05  ? 223 PHE   B CD2 1 
ATOM   3991 C CE1 . PHE   B 1 223 ? -2.246  -31.549 36.358 1.00 82.74  ? 223 PHE   B CE1 1 
ATOM   3992 C CE2 . PHE   B 1 223 ? -0.483  -30.040 35.834 1.00 87.01  ? 223 PHE   B CE2 1 
ATOM   3993 C CZ  . PHE   B 1 223 ? -1.212  -31.169 35.536 1.00 85.24  ? 223 PHE   B CZ  1 
ATOM   3994 N N   . THR   B 1 224 ? -3.404  -26.620 40.825 1.00 53.15  ? 224 THR   B N   1 
ATOM   3995 C CA  . THR   B 1 224 ? -3.115  -25.511 41.720 1.00 59.14  ? 224 THR   B CA  1 
ATOM   3996 C C   . THR   B 1 224 ? -2.212  -26.030 42.838 1.00 59.91  ? 224 THR   B C   1 
ATOM   3997 O O   . THR   B 1 224 ? -1.712  -27.158 42.784 1.00 55.29  ? 224 THR   B O   1 
ATOM   3998 C CB  . THR   B 1 224 ? -4.407  -24.889 42.259 1.00 62.57  ? 224 THR   B CB  1 
ATOM   3999 O OG1 . THR   B 1 224 ? -4.093  -23.714 43.015 1.00 61.19  ? 224 THR   B OG1 1 
ATOM   4000 C CG2 . THR   B 1 224 ? -5.157  -25.876 43.147 1.00 60.73  ? 224 THR   B CG2 1 
ATOM   4001 N N   . THR   B 1 225 ? -1.995  -25.199 43.852 1.00 56.52  ? 225 THR   B N   1 
ATOM   4002 C CA  . THR   B 1 225 ? -1.177  -25.587 44.996 1.00 60.41  ? 225 THR   B CA  1 
ATOM   4003 C C   . THR   B 1 225 ? -1.422  -24.593 46.123 1.00 58.77  ? 225 THR   B C   1 
ATOM   4004 O O   . THR   B 1 225 ? -2.305  -23.732 46.037 1.00 61.31  ? 225 THR   B O   1 
ATOM   4005 C CB  . THR   B 1 225 ? 0.309   -25.651 44.628 1.00 64.79  ? 225 THR   B CB  1 
ATOM   4006 O OG1 . THR   B 1 225 ? 1.057   -26.100 45.765 1.00 70.01  ? 225 THR   B OG1 1 
ATOM   4007 C CG2 . THR   B 1 225 ? 0.817   -24.277 44.208 1.00 62.87  ? 225 THR   B CG2 1 
ATOM   4008 N N   . THR   B 1 226 ? -0.630  -24.710 47.182 1.00 64.96  ? 226 THR   B N   1 
ATOM   4009 C CA  . THR   B 1 226 ? -0.722  -23.843 48.345 1.00 63.80  ? 226 THR   B CA  1 
ATOM   4010 C C   . THR   B 1 226 ? 0.569   -23.047 48.482 1.00 57.37  ? 226 THR   B C   1 
ATOM   4011 O O   . THR   B 1 226 ? 1.566   -23.323 47.810 1.00 63.01  ? 226 THR   B O   1 
ATOM   4012 C CB  . THR   B 1 226 ? -0.970  -24.650 49.626 1.00 62.55  ? 226 THR   B CB  1 
ATOM   4013 O OG1 . THR   B 1 226 ? 0.276   -25.171 50.108 1.00 56.32  ? 226 THR   B OG1 1 
ATOM   4014 C CG2 . THR   B 1 226 ? -1.934  -25.802 49.367 1.00 63.49  ? 226 THR   B CG2 1 
ATOM   4015 N N   . LEU   B 1 227 ? 0.553   -22.068 49.390 1.00 56.25  ? 227 LEU   B N   1 
ATOM   4016 C CA  . LEU   B 1 227 ? 1.730   -21.227 49.586 1.00 61.98  ? 227 LEU   B CA  1 
ATOM   4017 C C   . LEU   B 1 227 ? 2.904   -22.026 50.141 1.00 60.62  ? 227 LEU   B C   1 
ATOM   4018 O O   . LEU   B 1 227 ? 4.009   -21.984 49.581 1.00 56.83  ? 227 LEU   B O   1 
ATOM   4019 C CB  . LEU   B 1 227 ? 1.398   -20.048 50.501 1.00 62.69  ? 227 LEU   B CB  1 
ATOM   4020 C CG  . LEU   B 1 227 ? 1.301   -18.685 49.812 1.00 61.73  ? 227 LEU   B CG  1 
ATOM   4021 C CD1 . LEU   B 1 227 ? -0.145  -18.249 49.663 1.00 59.89  ? 227 LEU   B CD1 1 
ATOM   4022 C CD2 . LEU   B 1 227 ? 2.104   -17.632 50.561 1.00 59.35  ? 227 LEU   B CD2 1 
ATOM   4023 N N   . ASN   B 1 228 ? 2.697   -22.751 51.248 1.00 60.48  ? 228 ASN   B N   1 
ATOM   4024 C CA  . ASN   B 1 228 ? 3.811   -23.502 51.819 1.00 57.63  ? 228 ASN   B CA  1 
ATOM   4025 C C   . ASN   B 1 228 ? 4.280   -24.604 50.869 1.00 62.47  ? 228 ASN   B C   1 
ATOM   4026 O O   . ASN   B 1 228 ? 5.481   -24.884 50.771 1.00 67.72  ? 228 ASN   B O   1 
ATOM   4027 C CB  . ASN   B 1 228 ? 3.427   -24.096 53.175 1.00 70.10  ? 228 ASN   B CB  1 
ATOM   4028 C CG  . ASN   B 1 228 ? 3.176   -23.036 54.246 1.00 67.95  ? 228 ASN   B CG  1 
ATOM   4029 O OD1 . ASN   B 1 228 ? 2.549   -22.009 53.990 1.00 65.92  ? 228 ASN   B OD1 1 
ATOM   4030 N ND2 . ASN   B 1 228 ? 3.660   -23.295 55.457 1.00 67.98  ? 228 ASN   B ND2 1 
ATOM   4031 N N   . ASP   B 1 229 ? 3.349   -25.237 50.153 1.00 55.68  ? 229 ASP   B N   1 
ATOM   4032 C CA  . ASP   B 1 229 ? 3.743   -26.263 49.192 1.00 62.86  ? 229 ASP   B CA  1 
ATOM   4033 C C   . ASP   B 1 229 ? 4.538   -25.660 48.039 1.00 62.86  ? 229 ASP   B C   1 
ATOM   4034 O O   . ASP   B 1 229 ? 5.472   -26.287 47.523 1.00 53.52  ? 229 ASP   B O   1 
ATOM   4035 C CB  . ASP   B 1 229 ? 2.510   -27.002 48.672 1.00 57.90  ? 229 ASP   B CB  1 
ATOM   4036 N N   . PHE   B 1 230 ? 4.194   -24.437 47.629 1.00 60.73  ? 230 PHE   B N   1 
ATOM   4037 C CA  . PHE   B 1 230 ? 4.975   -23.758 46.600 1.00 62.07  ? 230 PHE   B CA  1 
ATOM   4038 C C   . PHE   B 1 230 ? 6.331   -23.313 47.143 1.00 61.51  ? 230 PHE   B C   1 
ATOM   4039 O O   . PHE   B 1 230 ? 7.370   -23.550 46.515 1.00 62.81  ? 230 PHE   B O   1 
ATOM   4040 C CB  . PHE   B 1 230 ? 4.191   -22.568 46.045 1.00 60.46  ? 230 PHE   B CB  1 
ATOM   4041 C CG  . PHE   B 1 230 ? 4.997   -21.689 45.136 1.00 65.39  ? 230 PHE   B CG  1 
ATOM   4042 C CD1 . PHE   B 1 230 ? 5.263   -22.078 43.834 1.00 64.09  ? 230 PHE   B CD1 1 
ATOM   4043 C CD2 . PHE   B 1 230 ? 5.495   -20.479 45.589 1.00 59.15  ? 230 PHE   B CD2 1 
ATOM   4044 C CE1 . PHE   B 1 230 ? 6.007   -21.275 43.003 1.00 59.27  ? 230 PHE   B CE1 1 
ATOM   4045 C CE2 . PHE   B 1 230 ? 6.239   -19.675 44.762 1.00 58.59  ? 230 PHE   B CE2 1 
ATOM   4046 C CZ  . PHE   B 1 230 ? 6.495   -20.073 43.468 1.00 60.38  ? 230 PHE   B CZ  1 
ATOM   4047 N N   . ASN   B 1 231 ? 6.341   -22.673 48.319 1.00 57.77  ? 231 ASN   B N   1 
ATOM   4048 C CA  . ASN   B 1 231 ? 7.599   -22.219 48.906 1.00 60.88  ? 231 ASN   B CA  1 
ATOM   4049 C C   . ASN   B 1 231 ? 8.546   -23.379 49.186 1.00 63.51  ? 231 ASN   B C   1 
ATOM   4050 O O   . ASN   B 1 231 ? 9.769   -23.202 49.156 1.00 61.13  ? 231 ASN   B O   1 
ATOM   4051 C CB  . ASN   B 1 231 ? 7.328   -21.429 50.188 1.00 58.54  ? 231 ASN   B CB  1 
ATOM   4052 C CG  . ASN   B 1 231 ? 6.718   -20.072 49.912 1.00 69.25  ? 231 ASN   B CG  1 
ATOM   4053 O OD1 . ASN   B 1 231 ? 6.927   -19.496 48.843 1.00 73.50  ? 231 ASN   B OD1 1 
ATOM   4054 N ND2 . ASN   B 1 231 ? 5.960   -19.553 50.870 1.00 57.84  ? 231 ASN   B ND2 1 
ATOM   4055 N N   . LEU   B 1 232 ? 8.003   -24.568 49.462 1.00 63.65  ? 232 LEU   B N   1 
ATOM   4056 C CA  . LEU   B 1 232 ? 8.843   -25.750 49.619 1.00 62.61  ? 232 LEU   B CA  1 
ATOM   4057 C C   . LEU   B 1 232 ? 9.633   -26.026 48.348 1.00 63.30  ? 232 LEU   B C   1 
ATOM   4058 O O   . LEU   B 1 232 ? 10.832  -26.326 48.398 1.00 64.69  ? 232 LEU   B O   1 
ATOM   4059 C CB  . LEU   B 1 232 ? 7.981   -26.958 49.989 1.00 62.53  ? 232 LEU   B CB  1 
ATOM   4060 C CG  . LEU   B 1 232 ? 8.164   -27.533 51.393 1.00 66.33  ? 232 LEU   B CG  1 
ATOM   4061 C CD1 . LEU   B 1 232 ? 9.591   -28.041 51.575 1.00 63.20  ? 232 LEU   B CD1 1 
ATOM   4062 C CD2 . LEU   B 1 232 ? 7.799   -26.499 52.459 1.00 73.24  ? 232 LEU   B CD2 1 
ATOM   4063 N N   . VAL   B 1 233 ? 8.973   -25.927 47.192 1.00 62.66  ? 233 VAL   B N   1 
ATOM   4064 C CA  . VAL   B 1 233 ? 9.666   -26.096 45.920 1.00 65.59  ? 233 VAL   B CA  1 
ATOM   4065 C C   . VAL   B 1 233 ? 10.579  -24.906 45.649 1.00 63.77  ? 233 VAL   B C   1 
ATOM   4066 O O   . VAL   B 1 233 ? 11.659  -25.059 45.065 1.00 65.05  ? 233 VAL   B O   1 
ATOM   4067 C CB  . VAL   B 1 233 ? 8.641   -26.303 44.788 1.00 66.41  ? 233 VAL   B CB  1 
ATOM   4068 C CG1 . VAL   B 1 233 ? 9.340   -26.676 43.488 1.00 69.84  ? 233 VAL   B CG1 1 
ATOM   4069 C CG2 . VAL   B 1 233 ? 7.626   -27.370 45.179 1.00 62.72  ? 233 VAL   B CG2 1 
ATOM   4070 N N   . ALA   B 1 234 ? 10.175  -23.709 46.083 1.00 65.74  ? 234 ALA   B N   1 
ATOM   4071 C CA  . ALA   B 1 234 ? 10.988  -22.520 45.852 1.00 63.85  ? 234 ALA   B CA  1 
ATOM   4072 C C   . ALA   B 1 234 ? 12.305  -22.589 46.615 1.00 67.44  ? 234 ALA   B C   1 
ATOM   4073 O O   . ALA   B 1 234 ? 13.357  -22.214 46.082 1.00 62.88  ? 234 ALA   B O   1 
ATOM   4074 C CB  . ALA   B 1 234 ? 10.204  -21.269 46.244 1.00 64.76  ? 234 ALA   B CB  1 
ATOM   4075 N N   . MET   B 1 235 ? 12.269  -23.070 47.861 1.00 65.10  ? 235 MET   B N   1 
ATOM   4076 C CA  . MET   B 1 235 ? 13.486  -23.146 48.663 1.00 66.88  ? 235 MET   B CA  1 
ATOM   4077 C C   . MET   B 1 235 ? 14.493  -24.130 48.077 1.00 57.99  ? 235 MET   B C   1 
ATOM   4078 O O   . MET   B 1 235 ? 15.702  -23.960 48.263 1.00 61.67  ? 235 MET   B O   1 
ATOM   4079 C CB  . MET   B 1 235 ? 13.142  -23.531 50.102 1.00 60.37  ? 235 MET   B CB  1 
ATOM   4080 N N   . LYS   B 1 236 ? 14.023  -25.156 47.365 1.00 63.69  ? 236 LYS   B N   1 
ATOM   4081 C CA  . LYS   B 1 236 ? 14.933  -26.142 46.796 1.00 53.63  ? 236 LYS   B CA  1 
ATOM   4082 C C   . LYS   B 1 236 ? 15.651  -25.637 45.553 1.00 62.68  ? 236 LYS   B C   1 
ATOM   4083 O O   . LYS   B 1 236 ? 16.688  -26.199 45.180 1.00 63.85  ? 236 LYS   B O   1 
ATOM   4084 C CB  . LYS   B 1 236 ? 14.174  -27.426 46.456 1.00 64.59  ? 236 LYS   B CB  1 
ATOM   4085 N N   . TYR   B 1 237 ? 15.130  -24.595 44.904 1.00 61.88  ? 237 TYR   B N   1 
ATOM   4086 C CA  . TYR   B 1 237 ? 15.690  -24.096 43.655 1.00 64.04  ? 237 TYR   B CA  1 
ATOM   4087 C C   . TYR   B 1 237 ? 16.265  -22.689 43.798 1.00 58.37  ? 237 TYR   B C   1 
ATOM   4088 O O   . TYR   B 1 237 ? 16.377  -21.966 42.803 1.00 64.78  ? 237 TYR   B O   1 
ATOM   4089 C CB  . TYR   B 1 237 ? 14.629  -24.144 42.554 1.00 62.45  ? 237 TYR   B CB  1 
ATOM   4090 C CG  . TYR   B 1 237 ? 14.282  -25.547 42.085 1.00 66.08  ? 237 TYR   B CG  1 
ATOM   4091 C CD1 . TYR   B 1 237 ? 15.085  -26.209 41.161 1.00 67.61  ? 237 TYR   B CD1 1 
ATOM   4092 C CD2 . TYR   B 1 237 ? 13.151  -26.205 42.558 1.00 62.54  ? 237 TYR   B CD2 1 
ATOM   4093 C CE1 . TYR   B 1 237 ? 14.774  -27.486 40.725 1.00 65.65  ? 237 TYR   B CE1 1 
ATOM   4094 C CE2 . TYR   B 1 237 ? 12.831  -27.485 42.125 1.00 57.75  ? 237 TYR   B CE2 1 
ATOM   4095 C CZ  . TYR   B 1 237 ? 13.647  -28.119 41.210 1.00 60.92  ? 237 TYR   B CZ  1 
ATOM   4096 O OH  . TYR   B 1 237 ? 13.341  -29.389 40.774 1.00 62.71  ? 237 TYR   B OH  1 
ATOM   4097 N N   . ASN   B 1 238 ? 16.637  -22.297 45.018 1.00 59.25  ? 238 ASN   B N   1 
ATOM   4098 C CA  . ASN   B 1 238 ? 17.232  -20.986 45.298 1.00 55.48  ? 238 ASN   B CA  1 
ATOM   4099 C C   . ASN   B 1 238 ? 16.296  -19.841 44.913 1.00 56.97  ? 238 ASN   B C   1 
ATOM   4100 O O   . ASN   B 1 238 ? 16.720  -18.843 44.329 1.00 52.57  ? 238 ASN   B O   1 
ATOM   4101 C CB  . ASN   B 1 238 ? 18.588  -20.829 44.606 1.00 56.94  ? 238 ASN   B CB  1 
ATOM   4102 N N   . TYR   B 1 239 ? 15.016  -19.975 45.250 1.00 54.83  ? 239 TYR   B N   1 
ATOM   4103 C CA  . TYR   B 1 239 ? 14.028  -18.928 45.024 1.00 54.72  ? 239 TYR   B CA  1 
ATOM   4104 C C   . TYR   B 1 239 ? 13.643  -18.287 46.350 1.00 58.15  ? 239 TYR   B C   1 
ATOM   4105 O O   . TYR   B 1 239 ? 13.506  -18.975 47.367 1.00 53.35  ? 239 TYR   B O   1 
ATOM   4106 C CB  . TYR   B 1 239 ? 12.776  -19.481 44.334 1.00 52.24  ? 239 TYR   B CB  1 
ATOM   4107 C CG  . TYR   B 1 239 ? 12.825  -19.478 42.818 1.00 53.81  ? 239 TYR   B CG  1 
ATOM   4108 C CD1 . TYR   B 1 239 ? 13.813  -20.171 42.133 1.00 52.92  ? 239 TYR   B CD1 1 
ATOM   4109 C CD2 . TYR   B 1 239 ? 11.865  -18.800 42.074 1.00 52.45  ? 239 TYR   B CD2 1 
ATOM   4110 C CE1 . TYR   B 1 239 ? 13.855  -20.178 40.748 1.00 56.71  ? 239 TYR   B CE1 1 
ATOM   4111 C CE2 . TYR   B 1 239 ? 11.897  -18.804 40.690 1.00 58.09  ? 239 TYR   B CE2 1 
ATOM   4112 C CZ  . TYR   B 1 239 ? 12.896  -19.493 40.034 1.00 48.94  ? 239 TYR   B CZ  1 
ATOM   4113 O OH  . TYR   B 1 239 ? 12.933  -19.499 38.659 1.00 54.00  ? 239 TYR   B OH  1 
ATOM   4114 N N   . GLU   B 1 240 ? 13.465  -16.969 46.333 1.00 55.21  ? 240 GLU   B N   1 
ATOM   4115 C CA  . GLU   B 1 240 ? 13.095  -16.257 47.543 1.00 57.37  ? 240 GLU   B CA  1 
ATOM   4116 C C   . GLU   B 1 240 ? 11.674  -16.630 47.965 1.00 55.48  ? 240 GLU   B C   1 
ATOM   4117 O O   . GLU   B 1 240 ? 10.845  -17.004 47.131 1.00 51.38  ? 240 GLU   B O   1 
ATOM   4118 C CB  . GLU   B 1 240 ? 13.207  -14.748 47.331 1.00 56.74  ? 240 GLU   B CB  1 
ATOM   4119 C CG  . GLU   B 1 240 ? 14.610  -14.302 46.932 1.00 65.14  ? 240 GLU   B CG  1 
ATOM   4120 C CD  . GLU   B 1 240 ? 15.253  -13.381 47.954 1.00 73.75  ? 240 GLU   B CD  1 
ATOM   4121 O OE1 . GLU   B 1 240 ? 14.815  -12.215 48.063 1.00 79.90  ? 240 GLU   B OE1 1 
ATOM   4122 O OE2 . GLU   B 1 240 ? 16.196  -13.824 48.648 1.00 69.39  ? 240 GLU   B OE2 1 
ATOM   4123 N N   . PRO   B 1 241 ? 11.374  -16.557 49.261 1.00 58.87  ? 241 PRO   B N   1 
ATOM   4124 C CA  . PRO   B 1 241 ? 10.042  -16.948 49.730 1.00 56.15  ? 241 PRO   B CA  1 
ATOM   4125 C C   . PRO   B 1 241 ? 8.965   -16.020 49.194 1.00 58.60  ? 241 PRO   B C   1 
ATOM   4126 O O   . PRO   B 1 241 ? 9.209   -14.848 48.893 1.00 58.97  ? 241 PRO   B O   1 
ATOM   4127 C CB  . PRO   B 1 241 ? 10.154  -16.848 51.257 1.00 60.71  ? 241 PRO   B CB  1 
ATOM   4128 C CG  . PRO   B 1 241 ? 11.623  -16.878 51.543 1.00 65.31  ? 241 PRO   B CG  1 
ATOM   4129 C CD  . PRO   B 1 241 ? 12.268  -16.203 50.375 1.00 61.76  ? 241 PRO   B CD  1 
ATOM   4130 N N   . LEU   B 1 242 ? 7.759   -16.564 49.081 1.00 54.34  ? 242 LEU   B N   1 
ATOM   4131 C CA  . LEU   B 1 242 ? 6.600   -15.827 48.602 1.00 64.01  ? 242 LEU   B CA  1 
ATOM   4132 C C   . LEU   B 1 242 ? 5.713   -15.494 49.792 1.00 64.50  ? 242 LEU   B C   1 
ATOM   4133 O O   . LEU   B 1 242 ? 5.214   -16.397 50.472 1.00 66.22  ? 242 LEU   B O   1 
ATOM   4134 C CB  . LEU   B 1 242 ? 5.828   -16.637 47.561 1.00 56.76  ? 242 LEU   B CB  1 
ATOM   4135 C CG  . LEU   B 1 242 ? 4.788   -15.848 46.771 1.00 56.39  ? 242 LEU   B CG  1 
ATOM   4136 C CD1 . LEU   B 1 242 ? 5.480   -14.879 45.825 1.00 59.28  ? 242 LEU   B CD1 1 
ATOM   4137 C CD2 . LEU   B 1 242 ? 3.874   -16.790 46.012 1.00 61.00  ? 242 LEU   B CD2 1 
ATOM   4138 N N   . THR   B 1 243 ? 5.526   -14.204 50.045 1.00 65.70  ? 243 THR   B N   1 
ATOM   4139 C CA  . THR   B 1 243 ? 4.735   -13.739 51.169 1.00 62.17  ? 243 THR   B CA  1 
ATOM   4140 C C   . THR   B 1 243 ? 3.317   -13.414 50.712 1.00 68.75  ? 243 THR   B C   1 
ATOM   4141 O O   . THR   B 1 243 ? 2.985   -13.468 49.525 1.00 62.59  ? 243 THR   B O   1 
ATOM   4142 C CB  . THR   B 1 243 ? 5.386   -12.513 51.808 1.00 63.80  ? 243 THR   B CB  1 
ATOM   4143 O OG1 . THR   B 1 243 ? 5.288   -11.401 50.909 1.00 71.16  ? 243 THR   B OG1 1 
ATOM   4144 C CG2 . THR   B 1 243 ? 6.849   -12.785 52.110 1.00 63.08  ? 243 THR   B CG2 1 
ATOM   4145 N N   . GLN   B 1 244 ? 2.465   -13.065 51.677 1.00 64.86  ? 244 GLN   B N   1 
ATOM   4146 C CA  . GLN   B 1 244 ? 1.148   -12.546 51.329 1.00 67.90  ? 244 GLN   B CA  1 
ATOM   4147 C C   . GLN   B 1 244 ? 1.243   -11.124 50.792 1.00 67.53  ? 244 GLN   B C   1 
ATOM   4148 O O   . GLN   B 1 244 ? 0.430   -10.726 49.950 1.00 66.04  ? 244 GLN   B O   1 
ATOM   4149 C CB  . GLN   B 1 244 ? 0.219   -12.604 52.540 1.00 70.74  ? 244 GLN   B CB  1 
ATOM   4150 C CG  . GLN   B 1 244 ? -1.240  -12.322 52.214 1.00 66.16  ? 244 GLN   B CG  1 
ATOM   4151 C CD  . GLN   B 1 244 ? -1.872  -13.393 51.341 1.00 67.68  ? 244 GLN   B CD  1 
ATOM   4152 O OE1 . GLN   B 1 244 ? -1.456  -14.553 51.354 1.00 71.92  ? 244 GLN   B OE1 1 
ATOM   4153 N NE2 . GLN   B 1 244 ? -2.886  -13.006 50.573 1.00 62.88  ? 244 GLN   B NE2 1 
ATOM   4154 N N   . ASP   B 1 245 ? 2.228   -10.351 51.264 1.00 59.22  ? 245 ASP   B N   1 
ATOM   4155 C CA  . ASP   B 1 245 ? 2.523   -9.067  50.638 1.00 67.07  ? 245 ASP   B CA  1 
ATOM   4156 C C   . ASP   B 1 245 ? 2.812   -9.240  49.153 1.00 68.22  ? 245 ASP   B C   1 
ATOM   4157 O O   . ASP   B 1 245 ? 2.331   -8.459  48.325 1.00 73.35  ? 245 ASP   B O   1 
ATOM   4158 C CB  . ASP   B 1 245 ? 3.706   -8.397  51.338 1.00 69.26  ? 245 ASP   B CB  1 
ATOM   4159 C CG  . ASP   B 1 245 ? 3.475   -8.210  52.822 1.00 77.62  ? 245 ASP   B CG  1 
ATOM   4160 O OD1 . ASP   B 1 245 ? 3.399   -9.229  53.542 1.00 75.82  ? 245 ASP   B OD1 1 
ATOM   4161 O OD2 . ASP   B 1 245 ? 3.373   -7.048  53.270 1.00 84.09  ? 245 ASP   B OD2 1 
ATOM   4162 N N   . HIS   B 1 246 ? 3.584   -10.270 48.796 1.00 56.33  ? 246 HIS   B N   1 
ATOM   4163 C CA  . HIS   B 1 246 ? 3.854   -10.534 47.387 1.00 66.90  ? 246 HIS   B CA  1 
ATOM   4164 C C   . HIS   B 1 246 ? 2.571   -10.863 46.634 1.00 66.51  ? 246 HIS   B C   1 
ATOM   4165 O O   . HIS   B 1 246 ? 2.359   -10.386 45.513 1.00 67.34  ? 246 HIS   B O   1 
ATOM   4166 C CB  . HIS   B 1 246 ? 4.867   -11.672 47.246 1.00 62.16  ? 246 HIS   B CB  1 
ATOM   4167 C CG  . HIS   B 1 246 ? 6.253   -11.305 47.677 1.00 62.31  ? 246 HIS   B CG  1 
ATOM   4168 N ND1 . HIS   B 1 246 ? 7.180   -12.243 48.077 1.00 59.62  ? 246 HIS   B ND1 1 
ATOM   4169 C CD2 . HIS   B 1 246 ? 6.873   -10.104 47.763 1.00 58.25  ? 246 HIS   B CD2 1 
ATOM   4170 C CE1 . HIS   B 1 246 ? 8.309   -11.636 48.397 1.00 57.78  ? 246 HIS   B CE1 1 
ATOM   4171 N NE2 . HIS   B 1 246 ? 8.150   -10.337 48.213 1.00 56.58  ? 246 HIS   B NE2 1 
ATOM   4172 N N   . VAL   B 1 247 ? 1.698   -11.672 47.239 1.00 66.68  ? 247 VAL   B N   1 
ATOM   4173 C CA  . VAL   B 1 247 ? 0.424   -11.989 46.607 1.00 59.64  ? 247 VAL   B CA  1 
ATOM   4174 C C   . VAL   B 1 247 ? -0.456  -10.743 46.514 1.00 65.94  ? 247 VAL   B C   1 
ATOM   4175 O O   . VAL   B 1 247 ? -1.211  -10.579 45.548 1.00 64.81  ? 247 VAL   B O   1 
ATOM   4176 C CB  . VAL   B 1 247 ? -0.267  -13.137 47.368 1.00 64.16  ? 247 VAL   B CB  1 
ATOM   4177 C CG1 . VAL   B 1 247 ? -1.618  -13.461 46.752 1.00 60.20  ? 247 VAL   B CG1 1 
ATOM   4178 C CG2 . VAL   B 1 247 ? 0.622   -14.376 47.378 1.00 56.72  ? 247 VAL   B CG2 1 
ATOM   4179 N N   . ASP   B 1 248 ? -0.370  -9.840  47.496 1.00 65.57  ? 248 ASP   B N   1 
ATOM   4180 C CA  . ASP   B 1 248 ? -1.101  -8.579  47.392 1.00 68.38  ? 248 ASP   B CA  1 
ATOM   4181 C C   . ASP   B 1 248 ? -0.599  -7.752  46.213 1.00 66.51  ? 248 ASP   B C   1 
ATOM   4182 O O   . ASP   B 1 248 ? -1.398  -7.192  45.453 1.00 58.80  ? 248 ASP   B O   1 
ATOM   4183 C CB  . ASP   B 1 248 ? -0.979  -7.778  48.693 1.00 70.61  ? 248 ASP   B CB  1 
ATOM   4184 C CG  . ASP   B 1 248 ? -2.011  -8.176  49.742 1.00 77.17  ? 248 ASP   B CG  1 
ATOM   4185 O OD1 . ASP   B 1 248 ? -3.192  -8.379  49.388 1.00 72.00  ? 248 ASP   B OD1 1 
ATOM   4186 O OD2 . ASP   B 1 248 ? -1.633  -8.279  50.930 1.00 74.08  ? 248 ASP   B OD2 1 
ATOM   4187 N N   . ILE   B 1 249 ? 0.724   -7.669  46.046 1.00 68.34  ? 249 ILE   B N   1 
ATOM   4188 C CA  . ILE   B 1 249 ? 1.302   -6.894  44.950 1.00 66.09  ? 249 ILE   B CA  1 
ATOM   4189 C C   . ILE   B 1 249 ? 0.882   -7.476  43.606 1.00 65.29  ? 249 ILE   B C   1 
ATOM   4190 O O   . ILE   B 1 249 ? 0.592   -6.739  42.656 1.00 66.28  ? 249 ILE   B O   1 
ATOM   4191 C CB  . ILE   B 1 249 ? 2.836   -6.834  45.095 1.00 70.26  ? 249 ILE   B CB  1 
ATOM   4192 C CG1 . ILE   B 1 249 ? 3.221   -6.176  46.423 1.00 73.41  ? 249 ILE   B CG1 1 
ATOM   4193 C CG2 . ILE   B 1 249 ? 3.456   -6.064  43.943 1.00 63.12  ? 249 ILE   B CG2 1 
ATOM   4194 C CD1 . ILE   B 1 249 ? 4.703   -6.253  46.735 1.00 77.41  ? 249 ILE   B CD1 1 
ATOM   4195 N N   . LEU   B 1 250 ? 0.825   -8.801  43.509 1.00 61.60  ? 250 LEU   B N   1 
ATOM   4196 C CA  . LEU   B 1 250 ? 0.376   -9.464  42.285 1.00 70.99  ? 250 LEU   B CA  1 
ATOM   4197 C C   . LEU   B 1 250 ? -1.131  -9.394  42.092 1.00 71.18  ? 250 LEU   B C   1 
ATOM   4198 O O   . LEU   B 1 250 ? -1.643  -10.047 41.172 1.00 72.37  ? 250 LEU   B O   1 
ATOM   4199 C CB  . LEU   B 1 250 ? 0.837   -10.921 42.281 1.00 62.94  ? 250 LEU   B CB  1 
ATOM   4200 C CG  . LEU   B 1 250 ? 2.351   -11.141 42.221 1.00 62.17  ? 250 LEU   B CG  1 
ATOM   4201 C CD1 . LEU   B 1 250 ? 2.700   -12.589 42.533 1.00 52.22  ? 250 LEU   B CD1 1 
ATOM   4202 C CD2 . LEU   B 1 250 ? 2.899   -10.739 40.856 1.00 54.72  ? 250 LEU   B CD2 1 
ATOM   4203 N N   . GLY   B 1 251 ? -1.827  -8.623  42.925 1.00 69.60  ? 251 GLY   B N   1 
ATOM   4204 C CA  . GLY   B 1 251 ? -3.255  -8.444  42.811 1.00 66.38  ? 251 GLY   B CA  1 
ATOM   4205 C C   . GLY   B 1 251 ? -3.706  -7.966  41.445 1.00 68.13  ? 251 GLY   B C   1 
ATOM   4206 O O   . GLY   B 1 251 ? -4.460  -8.654  40.749 1.00 65.85  ? 251 GLY   B O   1 
ATOM   4207 N N   . PRO   B 1 252 ? -3.272  -6.767  41.037 1.00 62.76  ? 252 PRO   B N   1 
ATOM   4208 C CA  . PRO   B 1 252 ? -3.702  -6.255  39.724 1.00 56.08  ? 252 PRO   B CA  1 
ATOM   4209 C C   . PRO   B 1 252 ? -3.360  -7.179  38.566 1.00 64.69  ? 252 PRO   B C   1 
ATOM   4210 O O   . PRO   B 1 252 ? -4.133  -7.262  37.603 1.00 60.21  ? 252 PRO   B O   1 
ATOM   4211 C CB  . PRO   B 1 252 ? -2.970  -4.909  39.626 1.00 60.98  ? 252 PRO   B CB  1 
ATOM   4212 C CG  . PRO   B 1 252 ? -2.807  -4.480  41.048 1.00 62.41  ? 252 PRO   B CG  1 
ATOM   4213 C CD  . PRO   B 1 252 ? -2.517  -5.754  41.798 1.00 64.85  ? 252 PRO   B CD  1 
ATOM   4214 N N   . LEU   B 1 253 ? -2.230  -7.889  38.638 1.00 57.57  ? 253 LEU   B N   1 
ATOM   4215 C CA  . LEU   B 1 253 ? -1.861  -8.813  37.567 1.00 66.35  ? 253 LEU   B CA  1 
ATOM   4216 C C   . LEU   B 1 253 ? -2.718  -10.072 37.594 1.00 68.70  ? 253 LEU   B C   1 
ATOM   4217 O O   . LEU   B 1 253 ? -3.158  -10.552 36.542 1.00 64.74  ? 253 LEU   B O   1 
ATOM   4218 C CB  . LEU   B 1 253 ? -0.385  -9.184  37.673 1.00 58.93  ? 253 LEU   B CB  1 
ATOM   4219 C CG  . LEU   B 1 253 ? 0.612   -8.150  37.168 1.00 49.47  ? 253 LEU   B CG  1 
ATOM   4220 C CD1 . LEU   B 1 253 ? 2.018   -8.694  37.321 1.00 49.07  ? 253 LEU   B CD1 1 
ATOM   4221 C CD2 . LEU   B 1 253 ? 0.316   -7.806  35.719 1.00 51.86  ? 253 LEU   B CD2 1 
ATOM   4222 N N   . SER   B 1 254 ? -2.941  -10.638 38.781 1.00 71.11  ? 254 SER   B N   1 
ATOM   4223 C CA  . SER   B 1 254 ? -3.819  -11.799 38.879 1.00 69.32  ? 254 SER   B CA  1 
ATOM   4224 C C   . SER   B 1 254 ? -5.252  -11.425 38.533 1.00 65.89  ? 254 SER   B C   1 
ATOM   4225 O O   . SER   B 1 254 ? -5.944  -12.173 37.832 1.00 68.16  ? 254 SER   B O   1 
ATOM   4226 C CB  . SER   B 1 254 ? -3.741  -12.404 40.280 1.00 70.77  ? 254 SER   B CB  1 
ATOM   4227 O OG  . SER   B 1 254 ? -4.471  -13.617 40.351 1.00 66.96  ? 254 SER   B OG  1 
ATOM   4228 N N   . ALA   B 1 255 ? -5.705  -10.258 38.996 1.00 70.35  ? 255 ALA   B N   1 
ATOM   4229 C CA  . ALA   B 1 255 ? -7.054  -9.787  38.711 1.00 71.10  ? 255 ALA   B CA  1 
ATOM   4230 C C   . ALA   B 1 255 ? -7.265  -9.427  37.246 1.00 69.73  ? 255 ALA   B C   1 
ATOM   4231 O O   . ALA   B 1 255 ? -8.417  -9.257  36.831 1.00 66.83  ? 255 ALA   B O   1 
ATOM   4232 C CB  . ALA   B 1 255 ? -7.382  -8.574  39.586 1.00 66.33  ? 255 ALA   B CB  1 
ATOM   4233 N N   . GLN   B 1 256 ? -6.197  -9.311  36.456 1.00 70.15  ? 256 GLN   B N   1 
ATOM   4234 C CA  . GLN   B 1 256 ? -6.310  -8.924  35.054 1.00 65.24  ? 256 GLN   B CA  1 
ATOM   4235 C C   . GLN   B 1 256 ? -6.266  -10.108 34.097 1.00 57.75  ? 256 GLN   B C   1 
ATOM   4236 O O   . GLN   B 1 256 ? -6.975  -10.103 33.087 1.00 58.94  ? 256 GLN   B O   1 
ATOM   4237 C CB  . GLN   B 1 256 ? -5.196  -7.943  34.683 1.00 64.44  ? 256 GLN   B CB  1 
ATOM   4238 C CG  . GLN   B 1 256 ? -5.602  -6.950  33.617 1.00 68.44  ? 256 GLN   B CG  1 
ATOM   4239 C CD  . GLN   B 1 256 ? -6.627  -5.960  34.131 1.00 84.68  ? 256 GLN   B CD  1 
ATOM   4240 O OE1 . GLN   B 1 256 ? -6.335  -5.150  35.013 1.00 81.56  ? 256 GLN   B OE1 1 
ATOM   4241 N NE2 . GLN   B 1 256 ? -7.842  -6.031  33.596 1.00 79.55  ? 256 GLN   B NE2 1 
ATOM   4242 N N   . THR   B 1 257 ? -5.446  -11.122 34.388 1.00 63.27  ? 257 THR   B N   1 
ATOM   4243 C CA  . THR   B 1 257 ? -5.321  -12.275 33.499 1.00 65.48  ? 257 THR   B CA  1 
ATOM   4244 C C   . THR   B 1 257 ? -6.422  -13.306 33.713 1.00 71.93  ? 257 THR   B C   1 
ATOM   4245 O O   . THR   B 1 257 ? -6.733  -14.070 32.793 1.00 68.73  ? 257 THR   B O   1 
ATOM   4246 C CB  . THR   B 1 257 ? -3.968  -12.962 33.695 1.00 63.75  ? 257 THR   B CB  1 
ATOM   4247 O OG1 . THR   B 1 257 ? -3.715  -13.141 35.096 1.00 64.47  ? 257 THR   B OG1 1 
ATOM   4248 C CG2 . THR   B 1 257 ? -2.839  -12.159 33.060 1.00 58.94  ? 257 THR   B CG2 1 
ATOM   4249 N N   . GLY   B 1 258 ? -7.006  -13.358 34.909 1.00 70.10  ? 258 GLY   B N   1 
ATOM   4250 C CA  . GLY   B 1 258 ? -7.924  -14.410 35.272 1.00 62.95  ? 258 GLY   B CA  1 
ATOM   4251 C C   . GLY   B 1 258 ? -7.276  -15.595 35.953 1.00 66.52  ? 258 GLY   B C   1 
ATOM   4252 O O   . GLY   B 1 258 ? -7.986  -16.434 36.518 1.00 76.59  ? 258 GLY   B O   1 
ATOM   4253 N N   . ILE   B 1 259 ? -5.954  -15.690 35.907 1.00 63.68  ? 259 ILE   B N   1 
ATOM   4254 C CA  . ILE   B 1 259 ? -5.227  -16.723 36.630 1.00 61.19  ? 259 ILE   B CA  1 
ATOM   4255 C C   . ILE   B 1 259 ? -5.000  -16.246 38.055 1.00 66.23  ? 259 ILE   B C   1 
ATOM   4256 O O   . ILE   B 1 259 ? -4.651  -15.083 38.289 1.00 66.95  ? 259 ILE   B O   1 
ATOM   4257 C CB  . ILE   B 1 259 ? -3.897  -17.045 35.921 1.00 61.95  ? 259 ILE   B CB  1 
ATOM   4258 C CG1 . ILE   B 1 259 ? -4.151  -17.596 34.515 1.00 65.75  ? 259 ILE   B CG1 1 
ATOM   4259 C CG2 . ILE   B 1 259 ? -3.059  -18.023 36.735 1.00 61.66  ? 259 ILE   B CG2 1 
ATOM   4260 C CD1 . ILE   B 1 259 ? -4.065  -16.555 33.419 1.00 60.20  ? 259 ILE   B CD1 1 
ATOM   4261 N N   . ALA   B 1 260 ? -5.227  -17.132 39.019 1.00 63.80  ? 260 ALA   B N   1 
ATOM   4262 C CA  . ALA   B 1 260 ? -4.948  -16.802 40.405 1.00 62.29  ? 260 ALA   B CA  1 
ATOM   4263 C C   . ALA   B 1 260 ? -3.472  -17.016 40.702 1.00 59.30  ? 260 ALA   B C   1 
ATOM   4264 O O   . ALA   B 1 260 ? -2.809  -17.855 40.084 1.00 63.54  ? 260 ALA   B O   1 
ATOM   4265 C CB  . ALA   B 1 260 ? -5.801  -17.643 41.355 1.00 61.93  ? 260 ALA   B CB  1 
ATOM   4266 N N   . VAL   B 1 261 ? -2.963  -16.235 41.656 1.00 54.74  ? 261 VAL   B N   1 
ATOM   4267 C CA  . VAL   B 1 261 ? -1.554  -16.329 42.030 1.00 58.64  ? 261 VAL   B CA  1 
ATOM   4268 C C   . VAL   B 1 261 ? -1.177  -17.775 42.340 1.00 60.03  ? 261 VAL   B C   1 
ATOM   4269 O O   . VAL   B 1 261 ? -0.191  -18.304 41.813 1.00 52.21  ? 261 VAL   B O   1 
ATOM   4270 C CB  . VAL   B 1 261 ? -1.252  -15.395 43.216 1.00 57.02  ? 261 VAL   B CB  1 
ATOM   4271 C CG1 . VAL   B 1 261 ? 0.229   -15.428 43.551 1.00 58.65  ? 261 VAL   B CG1 1 
ATOM   4272 C CG2 . VAL   B 1 261 ? -1.696  -13.980 42.895 1.00 59.53  ? 261 VAL   B CG2 1 
ATOM   4273 N N   . LEU   B 1 262 ? -1.964  -18.442 43.189 1.00 53.41  ? 262 LEU   B N   1 
ATOM   4274 C CA  . LEU   B 1 262 ? -1.655  -19.829 43.528 1.00 54.80  ? 262 LEU   B CA  1 
ATOM   4275 C C   . LEU   B 1 262 ? -1.755  -20.745 42.314 1.00 59.53  ? 262 LEU   B C   1 
ATOM   4276 O O   . LEU   B 1 262 ? -1.042  -21.753 42.236 1.00 54.46  ? 262 LEU   B O   1 
ATOM   4277 C CB  . LEU   B 1 262 ? -2.577  -20.319 44.642 1.00 62.15  ? 262 LEU   B CB  1 
ATOM   4278 C CG  . LEU   B 1 262 ? -2.329  -19.692 46.009 1.00 59.38  ? 262 LEU   B CG  1 
ATOM   4279 C CD1 . LEU   B 1 262 ? -3.380  -20.157 46.997 1.00 61.28  ? 262 LEU   B CD1 1 
ATOM   4280 C CD2 . LEU   B 1 262 ? -0.927  -20.021 46.521 1.00 54.11  ? 262 LEU   B CD2 1 
ATOM   4281 N N   . ASP   B 1 263 ? -2.629  -20.415 41.362 1.00 51.76  ? 263 ASP   B N   1 
ATOM   4282 C CA  . ASP   B 1 263 ? -2.682  -21.148 40.104 1.00 61.69  ? 263 ASP   B CA  1 
ATOM   4283 C C   . ASP   B 1 263 ? -1.473  -20.855 39.229 1.00 62.02  ? 263 ASP   B C   1 
ATOM   4284 O O   . ASP   B 1 263 ? -0.985  -21.755 38.538 1.00 59.33  ? 263 ASP   B O   1 
ATOM   4285 C CB  . ASP   B 1 263 ? -3.986  -20.822 39.375 1.00 63.03  ? 263 ASP   B CB  1 
ATOM   4286 C CG  . ASP   B 1 263 ? -5.156  -21.602 39.934 1.00 64.86  ? 263 ASP   B CG  1 
ATOM   4287 O OD1 . ASP   B 1 263 ? -5.124  -22.842 39.824 1.00 69.44  ? 263 ASP   B OD1 1 
ATOM   4288 O OD2 . ASP   B 1 263 ? -6.081  -20.992 40.515 1.00 70.36  ? 263 ASP   B OD2 1 
ATOM   4289 N N   . MET   B 1 264 ? -0.965  -19.619 39.250 1.00 61.08  ? 264 MET   B N   1 
ATOM   4290 C CA  . MET   B 1 264 ? 0.283   -19.344 38.545 1.00 56.70  ? 264 MET   B CA  1 
ATOM   4291 C C   . MET   B 1 264 ? 1.479   -19.968 39.258 1.00 57.65  ? 264 MET   B C   1 
ATOM   4292 O O   . MET   B 1 264 ? 2.452   -20.361 38.603 1.00 50.04  ? 264 MET   B O   1 
ATOM   4293 C CB  . MET   B 1 264 ? 0.484   -17.837 38.381 1.00 60.67  ? 264 MET   B CB  1 
ATOM   4294 C CG  . MET   B 1 264 ? 1.685   -17.468 37.519 1.00 52.68  ? 264 MET   B CG  1 
ATOM   4295 S SD  . MET   B 1 264 ? 1.550   -18.054 35.814 1.00 57.51  ? 264 MET   B SD  1 
ATOM   4296 C CE  . MET   B 1 264 ? 0.376   -16.879 35.142 1.00 53.13  ? 264 MET   B CE  1 
ATOM   4297 N N   . CYS   B 1 265 ? 1.422   -20.078 40.590 1.00 52.55  ? 265 CYS   B N   1 
ATOM   4298 C CA  . CYS   B 1 265 ? 2.506   -20.711 41.338 1.00 58.11  ? 265 CYS   B CA  1 
ATOM   4299 C C   . CYS   B 1 265 ? 2.643   -22.186 40.983 1.00 60.09  ? 265 CYS   B C   1 
ATOM   4300 O O   . CYS   B 1 265 ? 3.761   -22.695 40.835 1.00 53.77  ? 265 CYS   B O   1 
ATOM   4301 C CB  . CYS   B 1 265 ? 2.274   -20.560 42.840 1.00 62.10  ? 265 CYS   B CB  1 
ATOM   4302 S SG  . CYS   B 1 265 ? 2.439   -18.888 43.467 1.00 51.92  ? 265 CYS   B SG  1 
ATOM   4303 N N   . ALA   B 1 266 ? 1.518   -22.895 40.870 1.00 62.25  ? 266 ALA   B N   1 
ATOM   4304 C CA  . ALA   B 1 266 ? 1.577   -24.290 40.452 1.00 58.32  ? 266 ALA   B CA  1 
ATOM   4305 C C   . ALA   B 1 266 ? 2.175   -24.418 39.061 1.00 62.14  ? 266 ALA   B C   1 
ATOM   4306 O O   . ALA   B 1 266 ? 2.921   -25.366 38.788 1.00 58.51  ? 266 ALA   B O   1 
ATOM   4307 C CB  . ALA   B 1 266 ? 0.184   -24.914 40.496 1.00 60.30  ? 266 ALA   B CB  1 
ATOM   4308 N N   . SER   B 1 267 ? 1.874   -23.467 38.176 1.00 59.36  ? 267 SER   B N   1 
ATOM   4309 C CA  . SER   B 1 267 ? 2.498   -23.462 36.859 1.00 65.58  ? 267 SER   B CA  1 
ATOM   4310 C C   . SER   B 1 267 ? 4.003   -23.240 36.969 1.00 59.99  ? 267 SER   B C   1 
ATOM   4311 O O   . SER   B 1 267 ? 4.786   -23.905 36.280 1.00 57.55  ? 267 SER   B O   1 
ATOM   4312 C CB  . SER   B 1 267 ? 1.850   -22.393 35.981 1.00 61.05  ? 267 SER   B CB  1 
ATOM   4313 O OG  . SER   B 1 267 ? 2.044   -22.679 34.609 1.00 67.37  ? 267 SER   B OG  1 
ATOM   4314 N N   . LEU   B 1 268 ? 4.425   -22.320 37.841 1.00 54.17  ? 268 LEU   B N   1 
ATOM   4315 C CA  . LEU   B 1 268 ? 5.853   -22.119 38.072 1.00 57.97  ? 268 LEU   B CA  1 
ATOM   4316 C C   . LEU   B 1 268 ? 6.469   -23.321 38.775 1.00 56.27  ? 268 LEU   B C   1 
ATOM   4317 O O   . LEU   B 1 268 ? 7.595   -23.725 38.458 1.00 54.50  ? 268 LEU   B O   1 
ATOM   4318 C CB  . LEU   B 1 268 ? 6.086   -20.849 38.890 1.00 57.64  ? 268 LEU   B CB  1 
ATOM   4319 C CG  . LEU   B 1 268 ? 7.523   -20.633 39.374 1.00 57.37  ? 268 LEU   B CG  1 
ATOM   4320 C CD1 . LEU   B 1 268 ? 8.483   -20.571 38.195 1.00 50.49  ? 268 LEU   B CD1 1 
ATOM   4321 C CD2 . LEU   B 1 268 ? 7.633   -19.377 40.219 1.00 56.99  ? 268 LEU   B CD2 1 
ATOM   4322 N N   . LYS   B 1 269 ? 5.748   -23.894 39.741 1.00 59.73  ? 269 LYS   B N   1 
ATOM   4323 C CA  . LYS   B 1 269 ? 6.208   -25.118 40.386 1.00 61.69  ? 269 LYS   B CA  1 
ATOM   4324 C C   . LYS   B 1 269 ? 6.539   -26.189 39.355 1.00 59.23  ? 269 LYS   B C   1 
ATOM   4325 O O   . LYS   B 1 269 ? 7.589   -26.839 39.435 1.00 58.82  ? 269 LYS   B O   1 
ATOM   4326 C CB  . LYS   B 1 269 ? 5.144   -25.622 41.358 1.00 53.16  ? 269 LYS   B CB  1 
ATOM   4327 C CG  . LYS   B 1 269 ? 5.425   -27.003 41.907 1.00 66.81  ? 269 LYS   B CG  1 
ATOM   4328 C CD  . LYS   B 1 269 ? 4.260   -27.525 42.721 1.00 59.99  ? 269 LYS   B CD  1 
ATOM   4329 C CE  . LYS   B 1 269 ? 3.963   -26.620 43.898 1.00 66.09  ? 269 LYS   B CE  1 
ATOM   4330 N NZ  . LYS   B 1 269 ? 3.101   -27.315 44.891 1.00 69.12  ? 269 LYS   B NZ  1 
ATOM   4331 N N   . GLU   B 1 270 ? 5.662   -26.369 38.364 1.00 56.12  ? 270 GLU   B N   1 
ATOM   4332 C CA  . GLU   B 1 270 ? 5.897   -27.381 37.342 1.00 58.15  ? 270 GLU   B CA  1 
ATOM   4333 C C   . GLU   B 1 270 ? 7.069   -27.004 36.442 1.00 62.75  ? 270 GLU   B C   1 
ATOM   4334 O O   . GLU   B 1 270 ? 7.811   -27.885 35.992 1.00 58.94  ? 270 GLU   B O   1 
ATOM   4335 C CB  . GLU   B 1 270 ? 4.622   -27.593 36.521 1.00 64.87  ? 270 GLU   B CB  1 
ATOM   4336 C CG  . GLU   B 1 270 ? 4.378   -29.040 36.120 1.00 78.97  ? 270 GLU   B CG  1 
ATOM   4337 C CD  . GLU   B 1 270 ? 2.932   -29.310 35.742 1.00 83.23  ? 270 GLU   B CD  1 
ATOM   4338 O OE1 . GLU   B 1 270 ? 2.200   -28.338 35.457 1.00 82.62  ? 270 GLU   B OE1 1 
ATOM   4339 O OE2 . GLU   B 1 270 ? 2.528   -30.493 35.737 1.00 90.43  ? 270 GLU   B OE2 1 
ATOM   4340 N N   . LEU   B 1 271 ? 7.260   -25.707 36.178 1.00 56.98  ? 271 LEU   B N   1 
ATOM   4341 C CA  . LEU   B 1 271 ? 8.395   -25.285 35.363 1.00 59.29  ? 271 LEU   B CA  1 
ATOM   4342 C C   . LEU   B 1 271 ? 9.714   -25.526 36.084 1.00 60.65  ? 271 LEU   B C   1 
ATOM   4343 O O   . LEU   B 1 271 ? 10.708  -25.908 35.457 1.00 54.09  ? 271 LEU   B O   1 
ATOM   4344 C CB  . LEU   B 1 271 ? 8.253   -23.812 34.980 1.00 53.45  ? 271 LEU   B CB  1 
ATOM   4345 C CG  . LEU   B 1 271 ? 7.251   -23.507 33.868 1.00 52.28  ? 271 LEU   B CG  1 
ATOM   4346 C CD1 . LEU   B 1 271 ? 6.997   -22.012 33.769 1.00 54.66  ? 271 LEU   B CD1 1 
ATOM   4347 C CD2 . LEU   B 1 271 ? 7.751   -24.055 32.542 1.00 61.17  ? 271 LEU   B CD2 1 
ATOM   4348 N N   . LEU   B 1 272 ? 9.747   -25.307 37.401 1.00 52.87  ? 272 LEU   B N   1 
ATOM   4349 C CA  . LEU   B 1 272 ? 10.967  -25.571 38.158 1.00 55.69  ? 272 LEU   B CA  1 
ATOM   4350 C C   . LEU   B 1 272 ? 11.248  -27.065 38.239 1.00 64.65  ? 272 LEU   B C   1 
ATOM   4351 O O   . LEU   B 1 272 ? 12.379  -27.508 38.003 1.00 60.12  ? 272 LEU   B O   1 
ATOM   4352 C CB  . LEU   B 1 272 ? 10.861  -24.974 39.561 1.00 53.81  ? 272 LEU   B CB  1 
ATOM   4353 C CG  . LEU   B 1 272 ? 10.840  -23.448 39.666 1.00 62.43  ? 272 LEU   B CG  1 
ATOM   4354 C CD1 . LEU   B 1 272 ? 10.800  -23.015 41.122 1.00 56.67  ? 272 LEU   B CD1 1 
ATOM   4355 C CD2 . LEU   B 1 272 ? 12.045  -22.849 38.957 1.00 54.29  ? 272 LEU   B CD2 1 
ATOM   4356 N N   . GLN   B 1 273 ? 10.226  -27.861 38.567 1.00 59.91  ? 273 GLN   B N   1 
ATOM   4357 C CA  . GLN   B 1 273 ? 10.441  -29.290 38.770 1.00 65.90  ? 273 GLN   B CA  1 
ATOM   4358 C C   . GLN   B 1 273 ? 10.818  -30.003 37.477 1.00 63.96  ? 273 GLN   B C   1 
ATOM   4359 O O   . GLN   B 1 273 ? 11.638  -30.926 37.500 1.00 63.03  ? 273 GLN   B O   1 
ATOM   4360 C CB  . GLN   B 1 273 ? 9.193   -29.930 39.379 1.00 65.03  ? 273 GLN   B CB  1 
ATOM   4361 C CG  . GLN   B 1 273 ? 8.916   -29.533 40.819 1.00 58.82  ? 273 GLN   B CG  1 
ATOM   4362 C CD  . GLN   B 1 273 ? 7.606   -30.099 41.326 1.00 61.11  ? 273 GLN   B CD  1 
ATOM   4363 O OE1 . GLN   B 1 273 ? 6.970   -30.914 40.659 1.00 67.97  ? 273 GLN   B OE1 1 
ATOM   4364 N NE2 . GLN   B 1 273 ? 7.192   -29.666 42.510 1.00 65.89  ? 273 GLN   B NE2 1 
ATOM   4365 N N   . ASN   B 1 274 ? 10.244  -29.590 36.347 1.00 60.28  ? 274 ASN   B N   1 
ATOM   4366 C CA  . ASN   B 1 274 ? 10.433  -30.295 35.086 1.00 66.22  ? 274 ASN   B CA  1 
ATOM   4367 C C   . ASN   B 1 274 ? 11.331  -29.568 34.098 1.00 65.53  ? 274 ASN   B C   1 
ATOM   4368 O O   . ASN   B 1 274 ? 11.971  -30.223 33.273 1.00 61.21  ? 274 ASN   B O   1 
ATOM   4369 C CB  . ASN   B 1 274 ? 9.076   -30.558 34.417 1.00 65.64  ? 274 ASN   B CB  1 
ATOM   4370 C CG  . ASN   B 1 274 ? 8.081   -31.218 35.357 1.00 70.12  ? 274 ASN   B CG  1 
ATOM   4371 O OD1 . ASN   B 1 274 ? 6.986   -30.703 35.587 1.00 66.80  ? 274 ASN   B OD1 1 
ATOM   4372 N ND2 . ASN   B 1 274 ? 8.462   -32.363 35.910 1.00 68.07  ? 274 ASN   B ND2 1 
ATOM   4373 N N   . GLY   B 1 275 ? 11.401  -28.246 34.159 1.00 68.90  ? 275 GLY   B N   1 
ATOM   4374 C CA  . GLY   B 1 275 ? 12.115  -27.476 33.160 1.00 67.12  ? 275 GLY   B CA  1 
ATOM   4375 C C   . GLY   B 1 275 ? 11.178  -26.945 32.094 1.00 58.41  ? 275 GLY   B C   1 
ATOM   4376 O O   . GLY   B 1 275 ? 9.951   -27.040 32.187 1.00 63.51  ? 275 GLY   B O   1 
ATOM   4377 N N   . MET   B 1 276 ? 11.781  -26.381 31.050 1.00 70.12  ? 276 MET   B N   1 
ATOM   4378 C CA  . MET   B 1 276 ? 11.028  -25.777 29.959 1.00 66.25  ? 276 MET   B CA  1 
ATOM   4379 C C   . MET   B 1 276 ? 11.050  -26.607 28.680 1.00 69.12  ? 276 MET   B C   1 
ATOM   4380 O O   . MET   B 1 276 ? 10.418  -26.212 27.695 1.00 66.00  ? 276 MET   B O   1 
ATOM   4381 C CB  . MET   B 1 276 ? 11.553  -24.368 29.676 1.00 68.02  ? 276 MET   B CB  1 
ATOM   4382 C CG  . MET   B 1 276 ? 11.274  -23.381 30.799 1.00 70.13  ? 276 MET   B CG  1 
ATOM   4383 S SD  . MET   B 1 276 ? 11.962  -21.752 30.464 1.00 72.67  ? 276 MET   B SD  1 
ATOM   4384 C CE  . MET   B 1 276 ? 11.143  -21.364 28.922 1.00 51.90  ? 276 MET   B CE  1 
ATOM   4385 N N   . ASN   B 1 277 ? 11.760  -27.738 28.674 1.00 62.71  ? 277 ASN   B N   1 
ATOM   4386 C CA  . ASN   B 1 277 ? 11.729  -28.695 27.565 1.00 65.48  ? 277 ASN   B CA  1 
ATOM   4387 C C   . ASN   B 1 277 ? 12.117  -28.041 26.242 1.00 66.43  ? 277 ASN   B C   1 
ATOM   4388 O O   . ASN   B 1 277 ? 11.536  -28.326 25.193 1.00 69.96  ? 277 ASN   B O   1 
ATOM   4389 C CB  . ASN   B 1 277 ? 10.360  -29.368 27.453 1.00 70.84  ? 277 ASN   B CB  1 
ATOM   4390 C CG  . ASN   B 1 277 ? 10.054  -30.262 28.636 1.00 68.05  ? 277 ASN   B CG  1 
ATOM   4391 O OD1 . ASN   B 1 277 ? 10.657  -31.324 28.792 1.00 78.14  ? 277 ASN   B OD1 1 
ATOM   4392 N ND2 . ASN   B 1 277 ? 9.110   -29.842 29.473 1.00 76.53  ? 277 ASN   B ND2 1 
ATOM   4393 N N   . GLY   B 1 278 ? 13.108  -27.155 26.289 1.00 63.26  ? 278 GLY   B N   1 
ATOM   4394 C CA  . GLY   B 1 278 ? 13.549  -26.460 25.101 1.00 68.58  ? 278 GLY   B CA  1 
ATOM   4395 C C   . GLY   B 1 278 ? 12.593  -25.419 24.568 1.00 58.41  ? 278 GLY   B C   1 
ATOM   4396 O O   . GLY   B 1 278 ? 12.930  -24.741 23.589 1.00 60.77  ? 278 GLY   B O   1 
ATOM   4397 N N   . ARG   B 1 279 ? 11.412  -25.273 25.162 1.00 51.38  ? 279 ARG   B N   1 
ATOM   4398 C CA  . ARG   B 1 279 ? 10.488  -24.226 24.763 1.00 59.71  ? 279 ARG   B CA  1 
ATOM   4399 C C   . ARG   B 1 279 ? 10.954  -22.877 25.310 1.00 64.45  ? 279 ARG   B C   1 
ATOM   4400 O O   . ARG   B 1 279 ? 11.865  -22.791 26.137 1.00 60.86  ? 279 ARG   B O   1 
ATOM   4401 C CB  . ARG   B 1 279 ? 9.075   -24.550 25.244 1.00 61.35  ? 279 ARG   B CB  1 
ATOM   4402 N N   . THR   B 1 280 ? 10.326  -21.808 24.828 1.00 57.57  ? 280 THR   B N   1 
ATOM   4403 C CA  . THR   B 1 280 ? 10.677  -20.468 25.269 1.00 55.27  ? 280 THR   B CA  1 
ATOM   4404 C C   . THR   B 1 280 ? 9.452   -19.759 25.824 1.00 56.89  ? 280 THR   B C   1 
ATOM   4405 O O   . THR   B 1 280 ? 8.308   -20.112 25.525 1.00 54.14  ? 280 THR   B O   1 
ATOM   4406 C CB  . THR   B 1 280 ? 11.291  -19.621 24.140 1.00 53.18  ? 280 THR   B CB  1 
ATOM   4407 O OG1 . THR   B 1 280 ? 10.304  -19.357 23.135 1.00 51.96  ? 280 THR   B OG1 1 
ATOM   4408 C CG2 . THR   B 1 280 ? 12.479  -20.341 23.518 1.00 45.19  ? 280 THR   B CG2 1 
ATOM   4409 N N   . ILE   B 1 281 ? 9.718   -18.752 26.651 1.00 49.65  ? 281 ILE   B N   1 
ATOM   4410 C CA  . ILE   B 1 281 ? 8.695   -17.873 27.197 1.00 54.16  ? 281 ILE   B CA  1 
ATOM   4411 C C   . ILE   B 1 281 ? 9.175   -16.446 26.983 1.00 51.99  ? 281 ILE   B C   1 
ATOM   4412 O O   . ILE   B 1 281 ? 10.246  -16.072 27.478 1.00 43.16  ? 281 ILE   B O   1 
ATOM   4413 C CB  . ILE   B 1 281 ? 8.432   -18.138 28.689 1.00 47.52  ? 281 ILE   B CB  1 
ATOM   4414 C CG1 . ILE   B 1 281 ? 7.955   -19.572 28.913 1.00 55.77  ? 281 ILE   B CG1 1 
ATOM   4415 C CG2 . ILE   B 1 281 ? 7.408   -17.164 29.224 1.00 48.45  ? 281 ILE   B CG2 1 
ATOM   4416 C CD1 . ILE   B 1 281 ? 7.828   -19.941 30.371 1.00 48.25  ? 281 ILE   B CD1 1 
ATOM   4417 N N   . LEU   B 1 282 ? 8.398   -15.660 26.239 1.00 45.94  ? 282 LEU   B N   1 
ATOM   4418 C CA  . LEU   B 1 282 ? 8.749   -14.273 25.939 1.00 45.09  ? 282 LEU   B CA  1 
ATOM   4419 C C   . LEU   B 1 282 ? 10.155  -14.179 25.348 1.00 49.74  ? 282 LEU   B C   1 
ATOM   4420 O O   . LEU   B 1 282 ? 10.974  -13.354 25.757 1.00 48.78  ? 282 LEU   B O   1 
ATOM   4421 C CB  . LEU   B 1 282 ? 8.623   -13.394 27.186 1.00 49.27  ? 282 LEU   B CB  1 
ATOM   4422 C CG  . LEU   B 1 282 ? 7.214   -13.001 27.628 1.00 46.42  ? 282 LEU   B CG  1 
ATOM   4423 C CD1 . LEU   B 1 282 ? 7.280   -12.182 28.903 1.00 45.82  ? 282 LEU   B CD1 1 
ATOM   4424 C CD2 . LEU   B 1 282 ? 6.511   -12.219 26.530 1.00 42.16  ? 282 LEU   B CD2 1 
ATOM   4425 N N   . GLY   B 1 283 ? 10.437  -15.057 24.384 1.00 50.05  ? 283 GLY   B N   1 
ATOM   4426 C CA  . GLY   B 1 283 ? 11.726  -15.073 23.720 1.00 46.88  ? 283 GLY   B CA  1 
ATOM   4427 C C   . GLY   B 1 283 ? 12.904  -15.464 24.582 1.00 53.41  ? 283 GLY   B C   1 
ATOM   4428 O O   . GLY   B 1 283 ? 14.048  -15.259 24.166 1.00 52.41  ? 283 GLY   B O   1 
ATOM   4429 N N   . SER   B 1 284 ? 12.669  -16.017 25.768 1.00 45.87  ? 284 SER   B N   1 
ATOM   4430 C CA  . SER   B 1 284 ? 13.734  -16.421 26.672 1.00 42.13  ? 284 SER   B CA  1 
ATOM   4431 C C   . SER   B 1 284 ? 13.601  -17.903 26.994 1.00 43.92  ? 284 SER   B C   1 
ATOM   4432 O O   . SER   B 1 284 ? 12.489  -18.408 27.182 1.00 50.93  ? 284 SER   B O   1 
ATOM   4433 C CB  . SER   B 1 284 ? 13.700  -15.599 27.967 1.00 43.64  ? 284 SER   B CB  1 
ATOM   4434 O OG  . SER   B 1 284 ? 14.721  -16.009 28.861 1.00 41.05  ? 284 SER   B OG  1 
ATOM   4435 N N   . ALA   B 1 285 ? 14.736  -18.597 27.049 1.00 44.80  ? 285 ALA   B N   1 
ATOM   4436 C CA  . ALA   B 1 285 ? 14.771  -19.984 27.492 1.00 50.44  ? 285 ALA   B CA  1 
ATOM   4437 C C   . ALA   B 1 285 ? 15.042  -20.117 28.984 1.00 49.52  ? 285 ALA   B C   1 
ATOM   4438 O O   . ALA   B 1 285 ? 15.075  -21.241 29.496 1.00 54.48  ? 285 ALA   B O   1 
ATOM   4439 C CB  . ALA   B 1 285 ? 15.823  -20.768 26.704 1.00 45.00  ? 285 ALA   B CB  1 
ATOM   4440 N N   . LEU   B 1 286 ? 15.238  -19.004 29.685 1.00 50.81  ? 286 LEU   B N   1 
ATOM   4441 C CA  . LEU   B 1 286 ? 15.416  -18.969 31.128 1.00 45.88  ? 286 LEU   B CA  1 
ATOM   4442 C C   . LEU   B 1 286 ? 14.285  -18.172 31.766 1.00 45.97  ? 286 LEU   B C   1 
ATOM   4443 O O   . LEU   B 1 286 ? 13.658  -17.322 31.128 1.00 41.36  ? 286 LEU   B O   1 
ATOM   4444 C CB  . LEU   B 1 286 ? 16.766  -18.344 31.505 1.00 49.60  ? 286 LEU   B CB  1 
ATOM   4445 C CG  . LEU   B 1 286 ? 18.052  -19.053 31.079 1.00 52.27  ? 286 LEU   B CG  1 
ATOM   4446 C CD1 . LEU   B 1 286 ? 19.279  -18.195 31.378 1.00 50.35  ? 286 LEU   B CD1 1 
ATOM   4447 C CD2 . LEU   B 1 286 ? 18.170  -20.408 31.760 1.00 48.73  ? 286 LEU   B CD2 1 
ATOM   4448 N N   . LEU   B 1 287 ? 14.031  -18.453 33.041 1.00 49.83  ? 287 LEU   B N   1 
ATOM   4449 C CA  . LEU   B 1 287 ? 13.045  -17.692 33.796 1.00 46.93  ? 287 LEU   B CA  1 
ATOM   4450 C C   . LEU   B 1 287 ? 13.648  -16.362 34.232 1.00 44.97  ? 287 LEU   B C   1 
ATOM   4451 O O   . LEU   B 1 287 ? 14.739  -16.325 34.808 1.00 47.90  ? 287 LEU   B O   1 
ATOM   4452 C CB  . LEU   B 1 287 ? 12.571  -18.495 35.005 1.00 45.45  ? 287 LEU   B CB  1 
ATOM   4453 C CG  . LEU   B 1 287 ? 11.917  -19.827 34.634 1.00 45.52  ? 287 LEU   B CG  1 
ATOM   4454 C CD1 . LEU   B 1 287 ? 11.517  -20.609 35.873 1.00 43.76  ? 287 LEU   B CD1 1 
ATOM   4455 C CD2 . LEU   B 1 287 ? 10.716  -19.589 33.736 1.00 50.06  ? 287 LEU   B CD2 1 
ATOM   4456 N N   . GLU   B 1 288 ? 12.937  -15.273 33.958 1.00 44.48  ? 288 GLU   B N   1 
ATOM   4457 C CA  . GLU   B 1 288 ? 13.441  -13.923 34.181 1.00 49.83  ? 288 GLU   B CA  1 
ATOM   4458 C C   . GLU   B 1 288 ? 12.900  -13.353 35.487 1.00 44.87  ? 288 GLU   B C   1 
ATOM   4459 O O   . GLU   B 1 288 ? 11.694  -13.394 35.740 1.00 46.79  ? 288 GLU   B O   1 
ATOM   4460 C CB  . GLU   B 1 288 ? 13.053  -13.005 33.020 1.00 41.93  ? 288 GLU   B CB  1 
ATOM   4461 C CG  . GLU   B 1 288 ? 14.040  -13.009 31.865 1.00 58.08  ? 288 GLU   B CG  1 
ATOM   4462 C CD  . GLU   B 1 288 ? 15.373  -12.386 32.242 1.00 65.62  ? 288 GLU   B CD  1 
ATOM   4463 O OE1 . GLU   B 1 288 ? 15.379  -11.425 33.046 1.00 61.95  ? 288 GLU   B OE1 1 
ATOM   4464 O OE2 . GLU   B 1 288 ? 16.413  -12.868 31.743 1.00 63.21  ? 288 GLU   B OE2 1 
ATOM   4465 N N   . ASP   B 1 289 ? 13.796  -12.794 36.308 1.00 46.10  ? 289 ASP   B N   1 
ATOM   4466 C CA  . ASP   B 1 289 ? 13.379  -12.227 37.587 1.00 48.52  ? 289 ASP   B CA  1 
ATOM   4467 C C   . ASP   B 1 289 ? 13.777  -10.762 37.742 1.00 51.99  ? 289 ASP   B C   1 
ATOM   4468 O O   . ASP   B 1 289 ? 13.885  -10.276 38.873 1.00 43.59  ? 289 ASP   B O   1 
ATOM   4469 C CB  . ASP   B 1 289 ? 13.929  -13.053 38.759 1.00 46.93  ? 289 ASP   B CB  1 
ATOM   4470 C CG  . ASP   B 1 289 ? 15.407  -12.806 39.025 1.00 50.65  ? 289 ASP   B CG  1 
ATOM   4471 O OD1 . ASP   B 1 289 ? 16.142  -12.433 38.084 1.00 48.90  ? 289 ASP   B OD1 1 
ATOM   4472 O OD2 . ASP   B 1 289 ? 15.832  -12.997 40.188 1.00 45.06  ? 289 ASP   B OD2 1 
ATOM   4473 N N   . GLU   B 1 290 ? 13.985  -10.036 36.643 1.00 43.19  ? 290 GLU   B N   1 
ATOM   4474 C CA  . GLU   B 1 290 ? 14.364  -8.630  36.726 1.00 43.68  ? 290 GLU   B CA  1 
ATOM   4475 C C   . GLU   B 1 290 ? 13.238  -7.700  36.280 1.00 49.64  ? 290 GLU   B C   1 
ATOM   4476 O O   . GLU   B 1 290 ? 13.488  -6.566  35.867 1.00 41.44  ? 290 GLU   B O   1 
ATOM   4477 C CB  . GLU   B 1 290 ? 15.643  -8.375  35.931 1.00 49.23  ? 290 GLU   B CB  1 
ATOM   4478 C CG  . GLU   B 1 290 ? 16.823  -9.205  36.426 1.00 48.89  ? 290 GLU   B CG  1 
ATOM   4479 C CD  . GLU   B 1 290 ? 18.070  -8.375  36.682 1.00 56.36  ? 290 GLU   B CD  1 
ATOM   4480 O OE1 . GLU   B 1 290 ? 18.139  -7.230  36.188 1.00 52.09  ? 290 GLU   B OE1 1 
ATOM   4481 O OE2 . GLU   B 1 290 ? 18.983  -8.867  37.382 1.00 48.31  ? 290 GLU   B OE2 1 
ATOM   4482 N N   . PHE   B 1 291 ? 11.991  -8.162  36.381 1.00 41.30  ? 291 PHE   B N   1 
ATOM   4483 C CA  . PHE   B 1 291 ? 10.812  -7.334  36.142 1.00 43.63  ? 291 PHE   B CA  1 
ATOM   4484 C C   . PHE   B 1 291 ? 9.938   -7.374  37.391 1.00 50.18  ? 291 PHE   B C   1 
ATOM   4485 O O   . PHE   B 1 291 ? 9.405   -8.432  37.742 1.00 44.13  ? 291 PHE   B O   1 
ATOM   4486 C CB  . PHE   B 1 291 ? 10.023  -7.823  34.924 1.00 40.94  ? 291 PHE   B CB  1 
ATOM   4487 C CG  . PHE   B 1 291 ? 10.734  -7.638  33.611 1.00 43.27  ? 291 PHE   B CG  1 
ATOM   4488 C CD1 . PHE   B 1 291 ? 10.628  -6.443  32.915 1.00 49.43  ? 291 PHE   B CD1 1 
ATOM   4489 C CD2 . PHE   B 1 291 ? 11.490  -8.663  33.064 1.00 44.18  ? 291 PHE   B CD2 1 
ATOM   4490 C CE1 . PHE   B 1 291 ? 11.273  -6.268  31.701 1.00 46.08  ? 291 PHE   B CE1 1 
ATOM   4491 C CE2 . PHE   B 1 291 ? 12.138  -8.494  31.849 1.00 55.45  ? 291 PHE   B CE2 1 
ATOM   4492 C CZ  . PHE   B 1 291 ? 12.027  -7.296  31.168 1.00 49.95  ? 291 PHE   B CZ  1 
ATOM   4493 N N   . THR   B 1 292 ? 9.785   -6.232  38.063 1.00 48.80  ? 292 THR   B N   1 
ATOM   4494 C CA  . THR   B 1 292 ? 8.876   -6.152  39.197 1.00 50.99  ? 292 THR   B CA  1 
ATOM   4495 C C   . THR   B 1 292 ? 7.429   -6.143  38.704 1.00 47.69  ? 292 THR   B C   1 
ATOM   4496 O O   . THR   B 1 292 ? 7.170   -5.892  37.524 1.00 49.16  ? 292 THR   B O   1 
ATOM   4497 C CB  . THR   B 1 292 ? 9.148   -4.897  40.028 1.00 46.49  ? 292 THR   B CB  1 
ATOM   4498 O OG1 . THR   B 1 292 ? 8.789   -3.734  39.273 1.00 48.51  ? 292 THR   B OG1 1 
ATOM   4499 C CG2 . THR   B 1 292 ? 10.612  -4.820  40.430 1.00 52.00  ? 292 THR   B CG2 1 
ATOM   4500 N N   . PRO   B 1 293 ? 6.464   -6.429  39.585 1.00 49.44  ? 293 PRO   B N   1 
ATOM   4501 C CA  . PRO   B 1 293 ? 5.059   -6.305  39.165 1.00 46.12  ? 293 PRO   B CA  1 
ATOM   4502 C C   . PRO   B 1 293 ? 4.702   -4.905  38.704 1.00 51.96  ? 293 PRO   B C   1 
ATOM   4503 O O   . PRO   B 1 293 ? 3.872   -4.758  37.799 1.00 47.73  ? 293 PRO   B O   1 
ATOM   4504 C CB  . PRO   B 1 293 ? 4.280   -6.714  40.420 1.00 47.26  ? 293 PRO   B CB  1 
ATOM   4505 C CG  . PRO   B 1 293 ? 5.208   -7.637  41.138 1.00 58.13  ? 293 PRO   B CG  1 
ATOM   4506 C CD  . PRO   B 1 293 ? 6.584   -7.068  40.909 1.00 53.52  ? 293 PRO   B CD  1 
ATOM   4507 N N   . PHE   B 1 294 ? 5.313   -3.869  39.286 1.00 53.19  ? 294 PHE   B N   1 
ATOM   4508 C CA  . PHE   B 1 294 ? 5.105   -2.520  38.771 1.00 53.94  ? 294 PHE   B CA  1 
ATOM   4509 C C   . PHE   B 1 294 ? 5.606   -2.390  37.336 1.00 54.80  ? 294 PHE   B C   1 
ATOM   4510 O O   . PHE   B 1 294 ? 4.936   -1.775  36.501 1.00 53.38  ? 294 PHE   B O   1 
ATOM   4511 C CB  . PHE   B 1 294 ? 5.785   -1.482  39.671 1.00 58.81  ? 294 PHE   B CB  1 
ATOM   4512 C CG  . PHE   B 1 294 ? 5.971   -0.134  39.010 1.00 67.10  ? 294 PHE   B CG  1 
ATOM   4513 C CD1 . PHE   B 1 294 ? 4.920   0.768   38.922 1.00 64.42  ? 294 PHE   B CD1 1 
ATOM   4514 C CD2 . PHE   B 1 294 ? 7.198   0.224   38.471 1.00 68.42  ? 294 PHE   B CD2 1 
ATOM   4515 C CE1 . PHE   B 1 294 ? 5.093   2.001   38.310 1.00 63.36  ? 294 PHE   B CE1 1 
ATOM   4516 C CE2 . PHE   B 1 294 ? 7.376   1.453   37.858 1.00 61.45  ? 294 PHE   B CE2 1 
ATOM   4517 C CZ  . PHE   B 1 294 ? 6.323   2.342   37.778 1.00 61.67  ? 294 PHE   B CZ  1 
ATOM   4518 N N   . ASP   B 1 295 ? 6.780   -2.953  37.025 1.00 51.01  ? 295 ASP   B N   1 
ATOM   4519 C CA  . ASP   B 1 295 ? 7.312   -2.810  35.671 1.00 50.66  ? 295 ASP   B CA  1 
ATOM   4520 C C   . ASP   B 1 295 ? 6.389   -3.459  34.648 1.00 53.12  ? 295 ASP   B C   1 
ATOM   4521 O O   . ASP   B 1 295 ? 6.224   -2.948  33.535 1.00 51.85  ? 295 ASP   B O   1 
ATOM   4522 C CB  . ASP   B 1 295 ? 8.712   -3.421  35.562 1.00 56.29  ? 295 ASP   B CB  1 
ATOM   4523 C CG  . ASP   B 1 295 ? 9.716   -2.795  36.514 1.00 56.47  ? 295 ASP   B CG  1 
ATOM   4524 O OD1 . ASP   B 1 295 ? 9.535   -1.624  36.916 1.00 61.03  ? 295 ASP   B OD1 1 
ATOM   4525 O OD2 . ASP   B 1 295 ? 10.698  -3.495  36.854 1.00 46.59  ? 295 ASP   B OD2 1 
ATOM   4526 N N   . VAL   B 1 296 ? 5.778   -4.588  35.010 1.00 47.84  ? 296 VAL   B N   1 
ATOM   4527 C CA  . VAL   B 1 296 ? 4.912   -5.298  34.074 1.00 47.52  ? 296 VAL   B CA  1 
ATOM   4528 C C   . VAL   B 1 296 ? 3.663   -4.479  33.778 1.00 49.61  ? 296 VAL   B C   1 
ATOM   4529 O O   . VAL   B 1 296 ? 3.251   -4.346  32.620 1.00 54.55  ? 296 VAL   B O   1 
ATOM   4530 C CB  . VAL   B 1 296 ? 4.571   -6.695  34.628 1.00 43.81  ? 296 VAL   B CB  1 
ATOM   4531 C CG1 . VAL   B 1 296 ? 3.523   -7.382  33.767 1.00 50.68  ? 296 VAL   B CG1 1 
ATOM   4532 C CG2 . VAL   B 1 296 ? 5.826   -7.553  34.718 1.00 46.50  ? 296 VAL   B CG2 1 
ATOM   4533 N N   . VAL   B 1 297 ? 3.057   -3.896  34.815 1.00 46.73  ? 297 VAL   B N   1 
ATOM   4534 C CA  . VAL   B 1 297 ? 1.856   -3.081  34.638 1.00 53.21  ? 297 VAL   B CA  1 
ATOM   4535 C C   . VAL   B 1 297 ? 2.172   -1.821  33.839 1.00 61.47  ? 297 VAL   B C   1 
ATOM   4536 O O   . VAL   B 1 297 ? 1.426   -1.441  32.928 1.00 57.87  ? 297 VAL   B O   1 
ATOM   4537 C CB  . VAL   B 1 297 ? 1.243   -2.734  36.007 1.00 51.38  ? 297 VAL   B CB  1 
ATOM   4538 C CG1 . VAL   B 1 297 ? 0.112   -1.728  35.847 1.00 48.88  ? 297 VAL   B CG1 1 
ATOM   4539 C CG2 . VAL   B 1 297 ? 0.752   -3.992  36.710 1.00 48.80  ? 297 VAL   B CG2 1 
ATOM   4540 N N   . ARG   B 1 298 ? 3.270   -1.143  34.187 1.00 58.75  ? 298 ARG   B N   1 
ATOM   4541 C CA  . ARG   B 1 298 ? 3.681   0.055   33.461 1.00 54.27  ? 298 ARG   B CA  1 
ATOM   4542 C C   . ARG   B 1 298 ? 3.853   -0.235  31.976 1.00 57.81  ? 298 ARG   B C   1 
ATOM   4543 O O   . ARG   B 1 298 ? 3.413   0.548   31.126 1.00 56.06  ? 298 ARG   B O   1 
ATOM   4544 C CB  . ARG   B 1 298 ? 4.980   0.600   34.064 1.00 63.11  ? 298 ARG   B CB  1 
ATOM   4545 C CG  . ARG   B 1 298 ? 5.825   1.463   33.124 1.00 67.68  ? 298 ARG   B CG  1 
ATOM   4546 C CD  . ARG   B 1 298 ? 7.312   1.367   33.482 1.00 66.60  ? 298 ARG   B CD  1 
ATOM   4547 N NE  . ARG   B 1 298 ? 8.164   2.111   32.559 1.00 65.87  ? 298 ARG   B NE  1 
ATOM   4548 C CZ  . ARG   B 1 298 ? 9.487   2.008   32.503 1.00 65.27  ? 298 ARG   B CZ  1 
ATOM   4549 N NH1 . ARG   B 1 298 ? 10.151  1.187   33.301 1.00 62.27  ? 298 ARG   B NH1 1 
ATOM   4550 N NH2 . ARG   B 1 298 ? 10.160  2.743   31.619 1.00 50.36  ? 298 ARG   B NH2 1 
ATOM   4551 N N   . GLN   B 1 299 ? 4.466   -1.373  31.647 1.00 55.64  ? 299 GLN   B N   1 
ATOM   4552 C CA  . GLN   B 1 299 ? 4.726   -1.735  30.260 1.00 56.74  ? 299 GLN   B CA  1 
ATOM   4553 C C   . GLN   B 1 299 ? 3.516   -2.362  29.578 1.00 62.69  ? 299 GLN   B C   1 
ATOM   4554 O O   . GLN   B 1 299 ? 3.250   -2.067  28.409 1.00 62.29  ? 299 GLN   B O   1 
ATOM   4555 C CB  . GLN   B 1 299 ? 5.919   -2.693  30.178 1.00 50.77  ? 299 GLN   B CB  1 
ATOM   4556 C CG  . GLN   B 1 299 ? 6.418   -2.914  28.755 1.00 43.04  ? 299 GLN   B CG  1 
ATOM   4557 C CD  . GLN   B 1 299 ? 7.765   -3.608  28.692 1.00 43.33  ? 299 GLN   B CD  1 
ATOM   4558 O OE1 . GLN   B 1 299 ? 8.172   -4.095  27.638 1.00 44.21  ? 299 GLN   B OE1 1 
ATOM   4559 N NE2 . GLN   B 1 299 ? 8.467   -3.650  29.817 1.00 46.53  ? 299 GLN   B NE2 1 
ATOM   4560 N N   . CYS   B 1 300 ? 2.778   -3.231  30.273 1.00 52.41  ? 300 CYS   B N   1 
ATOM   4561 C CA  . CYS   B 1 300 ? 1.637   -3.887  29.648 1.00 55.54  ? 300 CYS   B CA  1 
ATOM   4562 C C   . CYS   B 1 300 ? 0.379   -3.027  29.655 1.00 56.84  ? 300 CYS   B C   1 
ATOM   4563 O O   . CYS   B 1 300 ? -0.612  -3.413  29.025 1.00 59.00  ? 300 CYS   B O   1 
ATOM   4564 C CB  . CYS   B 1 300 ? 1.364   -5.231  30.326 1.00 51.60  ? 300 CYS   B CB  1 
ATOM   4565 S SG  . CYS   B 1 300 ? 2.631   -6.479  29.979 1.00 59.83  ? 300 CYS   B SG  1 
ATOM   4566 N N   . SER   B 1 301 ? 0.404   -1.881  30.335 1.00 62.22  ? 301 SER   B N   1 
ATOM   4567 C CA  . SER   B 1 301 ? -0.691  -0.910  30.319 1.00 56.22  ? 301 SER   B CA  1 
ATOM   4568 C C   . SER   B 1 301 ? -0.294  0.354   31.080 1.00 58.41  ? 301 SER   B C   1 
ATOM   4569 O O   . SER   B 1 301 ? -0.158  1.429   30.494 1.00 58.69  ? 301 SER   B O   1 
ATOM   4570 C CB  . SER   B 1 301 ? -1.970  -1.501  30.919 1.00 70.57  ? 301 SER   B CB  1 
ATOM   4571 O OG  . SER   B 1 301 ? -2.658  -2.292  29.964 1.00 70.06  ? 301 SER   B OG  1 
HETATM 4572 C C02 . A1AFE C 2 .   ? -1.802  1.309   17.942 0.97 37.34  ? 401 A1AFE A C02 1 
HETATM 4573 C C04 . A1AFE C 2 .   ? -3.684  2.111   16.423 0.97 33.27  ? 401 A1AFE A C04 1 
HETATM 4574 C C05 . A1AFE C 2 .   ? -3.625  2.618   15.000 0.97 34.59  ? 401 A1AFE A C05 1 
HETATM 4575 C C06 . A1AFE C 2 .   ? -3.318  1.579   13.963 0.97 39.91  ? 401 A1AFE A C06 1 
HETATM 4576 C C07 . A1AFE C 2 .   ? -2.151  0.733   14.399 0.97 40.36  ? 401 A1AFE A C07 1 
HETATM 4577 C C08 . A1AFE C 2 .   ? -2.484  0.078   15.744 0.97 39.72  ? 401 A1AFE A C08 1 
HETATM 4578 C C09 . A1AFE C 2 .   ? -4.011  1.474   12.848 0.97 38.96  ? 401 A1AFE A C09 1 
HETATM 4579 C C10 . A1AFE C 2 .   ? -5.210  2.436   12.618 0.97 42.89  ? 401 A1AFE A C10 1 
HETATM 4580 C C11 . A1AFE C 2 .   ? -4.963  3.746   12.142 0.97 38.49  ? 401 A1AFE A C11 1 
HETATM 4581 C C12 . A1AFE C 2 .   ? -6.049  4.599   11.950 0.97 42.36  ? 401 A1AFE A C12 1 
HETATM 4582 C C13 . A1AFE C 2 .   ? -7.354  4.170   12.220 0.97 41.10  ? 401 A1AFE A C13 1 
HETATM 4583 C C14 . A1AFE C 2 .   ? -7.587  2.883   12.691 0.97 45.25  ? 401 A1AFE A C14 1 
HETATM 4584 C C15 . A1AFE C 2 .   ? -6.488  2.012   12.891 0.97 44.02  ? 401 A1AFE A C15 1 
HETATM 4585 C C16 . A1AFE C 2 .   ? -6.757  0.587   13.408 0.97 41.81  ? 401 A1AFE A C16 1 
HETATM 4586 C C20 . A1AFE C 2 .   ? -4.579  -0.577  11.445 0.97 39.11  ? 401 A1AFE A C20 1 
HETATM 4587 C C21 . A1AFE C 2 .   ? -4.265  -1.518  10.449 0.97 44.44  ? 401 A1AFE A C21 1 
HETATM 4588 C C22 . A1AFE C 2 .   ? -3.039  -1.438  9.780  0.97 42.02  ? 401 A1AFE A C22 1 
HETATM 4589 C C23 . A1AFE C 2 .   ? -2.133  -0.424  10.101 0.97 44.59  ? 401 A1AFE A C23 1 
HETATM 4590 C C24 . A1AFE C 2 .   ? -2.445  0.507   11.081 0.97 44.76  ? 401 A1AFE A C24 1 
HETATM 4591 C C25 . A1AFE C 2 .   ? -3.682  0.415   11.769 0.97 36.79  ? 401 A1AFE A C25 1 
HETATM 4592 C C26 . A1AFE C 2 .   ? -0.729  0.270   18.271 0.97 38.35  ? 401 A1AFE A C26 1 
HETATM 4593 C C27 . A1AFE C 2 .   ? -1.158  -0.900  18.953 0.97 43.28  ? 401 A1AFE A C27 1 
HETATM 4594 C C29 . A1AFE C 2 .   ? -2.259  -2.514  19.989 0.97 39.23  ? 401 A1AFE A C29 1 
HETATM 4595 C C30 . A1AFE C 2 .   ? -0.921  -2.878  19.925 0.97 46.31  ? 401 A1AFE A C30 1 
HETATM 4596 C C31 . A1AFE C 2 .   ? -0.225  -1.846  19.265 0.97 44.31  ? 401 A1AFE A C31 1 
HETATM 4597 C C32 . A1AFE C 2 .   ? 1.120   -1.612  18.891 0.97 38.58  ? 401 A1AFE A C32 1 
HETATM 4598 C C34 . A1AFE C 2 .   ? 0.601   0.443   17.934 0.97 37.20  ? 401 A1AFE A C34 1 
HETATM 4599 N N03 . A1AFE C 2 .   ? -2.625  1.151   16.749 0.97 36.55  ? 401 A1AFE A N03 1 
HETATM 4600 N N28 . A1AFE C 2 .   ? -2.389  -1.320  19.400 0.97 36.59  ? 401 A1AFE A N28 1 
HETATM 4601 N N33 . A1AFE C 2 .   ? 1.469   -0.505  18.258 0.97 38.94  ? 401 A1AFE A N33 1 
HETATM 4602 O O01 . A1AFE C 2 .   ? -2.002  2.222   18.662 0.97 42.95  ? 401 A1AFE A O01 1 
HETATM 4603 O O18 . A1AFE C 2 .   ? -6.111  -1.954  13.074 0.97 56.19  ? 401 A1AFE A O18 1 
HETATM 4604 O O19 . A1AFE C 2 .   ? -7.182  -0.839  11.219 0.97 52.90  ? 401 A1AFE A O19 1 
HETATM 4605 S S17 . A1AFE C 2 .   ? -6.189  -0.721  12.289 0.97 50.19  ? 401 A1AFE A S17 1 
HETATM 4606 S S   . DMS   D 3 .   ? 19.699  -8.327  28.743 1.00 104.38 ? 402 DMS   A S   1 
HETATM 4607 O O   . DMS   D 3 .   ? 19.599  -6.837  28.806 1.00 61.85  ? 402 DMS   A O   1 
HETATM 4608 C C1  . DMS   D 3 .   ? 20.741  -8.930  30.099 1.00 65.52  ? 402 DMS   A C1  1 
HETATM 4609 C C2  . DMS   D 3 .   ? 20.748  -8.802  27.342 1.00 73.83  ? 402 DMS   A C2  1 
HETATM 4610 C C02 . A1AFE E 2 .   ? 36.486  1.624   37.470 0.98 40.07  ? 401 A1AFE B C02 1 
HETATM 4611 C C04 . A1AFE E 2 .   ? 38.368  2.456   39.001 0.98 36.91  ? 401 A1AFE B C04 1 
HETATM 4612 C C05 . A1AFE E 2 .   ? 38.351  2.866   40.461 0.98 41.07  ? 401 A1AFE B C05 1 
HETATM 4613 C C06 . A1AFE E 2 .   ? 38.082  1.771   41.454 0.98 38.82  ? 401 A1AFE B C06 1 
HETATM 4614 C C07 . A1AFE E 2 .   ? 36.950  0.900   40.977 0.98 43.15  ? 401 A1AFE B C07 1 
HETATM 4615 C C08 . A1AFE E 2 .   ? 37.294  0.336   39.595 0.98 40.68  ? 401 A1AFE B C08 1 
HETATM 4616 C C09 . A1AFE E 2 .   ? 38.772  1.645   42.572 0.98 41.91  ? 401 A1AFE B C09 1 
HETATM 4617 C C10 . A1AFE E 2 .   ? 39.929  2.646   42.843 0.98 38.34  ? 401 A1AFE B C10 1 
HETATM 4618 C C11 . A1AFE E 2 .   ? 39.626  3.931   43.357 0.98 46.26  ? 401 A1AFE B C11 1 
HETATM 4619 C C12 . A1AFE E 2 .   ? 40.671  4.827   43.583 0.98 48.77  ? 401 A1AFE B C12 1 
HETATM 4620 C C13 . A1AFE E 2 .   ? 41.994  4.458   43.310 0.98 46.79  ? 401 A1AFE B C13 1 
HETATM 4621 C C14 . A1AFE E 2 .   ? 42.281  3.194   42.805 0.98 41.87  ? 401 A1AFE B C14 1 
HETATM 4622 C C15 . A1AFE E 2 .   ? 41.223  2.282   42.570 0.98 45.71  ? 401 A1AFE B C15 1 
HETATM 4623 C C16 . A1AFE E 2 .   ? 41.552  0.883   42.007 0.98 43.98  ? 401 A1AFE B C16 1 
HETATM 4624 C C20 . A1AFE E 2 .   ? 39.419  -0.443  43.901 0.98 45.11  ? 401 A1AFE B C20 1 
HETATM 4625 C C21 . A1AFE E 2 .   ? 39.137  -1.440  44.850 0.98 46.97  ? 401 A1AFE B C21 1 
HETATM 4626 C C22 . A1AFE E 2 .   ? 37.906  -1.447  45.509 0.98 45.31  ? 401 A1AFE B C22 1 
HETATM 4627 C C23 . A1AFE E 2 .   ? 36.960  -0.462  45.220 0.98 46.82  ? 401 A1AFE B C23 1 
HETATM 4628 C C24 . A1AFE E 2 .   ? 37.237  0.524   44.284 0.98 48.54  ? 401 A1AFE B C24 1 
HETATM 4629 C C25 . A1AFE E 2 .   ? 38.483  0.524   43.605 0.98 41.46  ? 401 A1AFE B C25 1 
HETATM 4630 C C26 . A1AFE E 2 .   ? 35.458  0.546   37.097 0.98 39.74  ? 401 A1AFE B C26 1 
HETATM 4631 C C27 . A1AFE E 2 .   ? 35.939  -0.578  36.371 0.98 43.94  ? 401 A1AFE B C27 1 
HETATM 4632 C C29 . A1AFE E 2 .   ? 37.122  -2.098  35.285 0.98 42.14  ? 401 A1AFE B C29 1 
HETATM 4633 C C30 . A1AFE E 2 .   ? 35.804  -2.528  35.323 0.98 45.24  ? 401 A1AFE B C30 1 
HETATM 4634 C C31 . A1AFE E 2 .   ? 35.054  -1.556  36.014 0.98 41.39  ? 401 A1AFE B C31 1 
HETATM 4635 C C32 . A1AFE E 2 .   ? 33.696  -1.403  36.381 0.98 37.55  ? 401 A1AFE B C32 1 
HETATM 4636 C C34 . A1AFE E 2 .   ? 34.113  0.635   37.422 0.98 38.58  ? 401 A1AFE B C34 1 
HETATM 4637 N N03 . A1AFE E 2 .   ? 37.349  1.460   38.641 0.98 40.46  ? 401 A1AFE B N03 1 
HETATM 4638 N N28 . A1AFE E 2 .   ? 37.189  -0.924  35.919 0.98 39.46  ? 401 A1AFE B N28 1 
HETATM 4639 N N33 . A1AFE E 2 .   ? 33.291  -0.340  37.054 0.98 36.70  ? 401 A1AFE B N33 1 
HETATM 4640 O O01 . A1AFE E 2 .   ? 36.622  2.581   36.790 0.98 41.74  ? 401 A1AFE B O01 1 
HETATM 4641 O O18 . A1AFE E 2 .   ? 41.041  -1.712  42.264 0.98 56.90  ? 401 A1AFE B O18 1 
HETATM 4642 O O19 . A1AFE E 2 .   ? 42.035  -0.602  44.146 0.98 62.49  ? 401 A1AFE B O19 1 
HETATM 4643 S S17 . A1AFE E 2 .   ? 41.043  -0.493  43.075 0.98 57.35  ? 401 A1AFE B S17 1 
HETATM 4644 S S   . DMS   F 3 .   ? 14.670  -7.762  26.658 1.00 77.97  ? 402 DMS   B S   1 
HETATM 4645 O O   . DMS   F 3 .   ? 15.313  -6.660  25.880 1.00 65.42  ? 402 DMS   B O   1 
HETATM 4646 C C1  . DMS   F 3 .   ? 14.186  -9.117  25.550 1.00 53.76  ? 402 DMS   B C1  1 
HETATM 4647 C C2  . DMS   F 3 .   ? 15.920  -8.595  27.675 1.00 73.17  ? 402 DMS   B C2  1 
HETATM 4648 O O   . HOH   G 4 .   ? 17.208  -6.007  20.792 1.00 44.10  ? 501 HOH   A O   1 
HETATM 4649 O O   . HOH   G 4 .   ? 27.711  4.439   23.468 1.00 53.93  ? 502 HOH   A O   1 
HETATM 4650 O O   . HOH   G 4 .   ? -1.899  1.646   2.545  1.00 50.76  ? 503 HOH   A O   1 
HETATM 4651 O O   . HOH   G 4 .   ? 9.748   8.325   20.326 1.00 43.35  ? 504 HOH   A O   1 
HETATM 4652 O O   . HOH   G 4 .   ? 14.958  7.825   8.226  1.00 41.85  ? 505 HOH   A O   1 
HETATM 4653 O O   . HOH   G 4 .   ? 35.388  1.423   22.664 1.00 55.82  ? 506 HOH   A O   1 
HETATM 4654 O O   . HOH   G 4 .   ? 9.011   0.084   1.507  1.00 55.94  ? 507 HOH   A O   1 
HETATM 4655 O O   . HOH   G 4 .   ? 6.276   -1.599  1.680  1.00 45.78  ? 508 HOH   A O   1 
HETATM 4656 O O   . HOH   G 4 .   ? 18.809  -23.200 25.644 1.00 51.94  ? 509 HOH   A O   1 
HETATM 4657 O O   . HOH   G 4 .   ? 19.104  -4.087  28.897 1.00 49.77  ? 510 HOH   A O   1 
HETATM 4658 O O   . HOH   G 4 .   ? 19.941  -19.918 17.349 1.00 47.93  ? 511 HOH   A O   1 
HETATM 4659 O O   . HOH   G 4 .   ? -0.529  8.388   22.190 1.00 46.66  ? 512 HOH   A O   1 
HETATM 4660 O O   . HOH   G 4 .   ? -10.337 6.558   1.377  1.00 49.89  ? 513 HOH   A O   1 
HETATM 4661 O O   . HOH   G 4 .   ? 5.599   0.991   25.283 1.00 39.15  ? 514 HOH   A O   1 
HETATM 4662 O O   . HOH   G 4 .   ? 8.606   -2.549  9.045  1.00 32.68  ? 515 HOH   A O   1 
HETATM 4663 O O   . HOH   G 4 .   ? 23.999  -10.344 18.872 1.00 34.61  ? 516 HOH   A O   1 
HETATM 4664 O O   . HOH   G 4 .   ? 0.428   5.589   8.243  1.00 32.50  ? 517 HOH   A O   1 
HETATM 4665 O O   . HOH   G 4 .   ? 19.929  5.313   12.833 1.00 43.31  ? 518 HOH   A O   1 
HETATM 4666 O O   . HOH   G 4 .   ? 1.310   1.872   2.538  1.00 39.07  ? 519 HOH   A O   1 
HETATM 4667 O O   . HOH   G 4 .   ? -2.028  -3.120  14.067 1.00 46.97  ? 520 HOH   A O   1 
HETATM 4668 O O   . HOH   G 4 .   ? -6.782  7.844   13.323 1.00 42.86  ? 521 HOH   A O   1 
HETATM 4669 O O   . HOH   G 4 .   ? -1.885  31.036  10.471 1.00 58.73  ? 522 HOH   A O   1 
HETATM 4670 O O   . HOH   G 4 .   ? 12.329  -2.502  3.019  1.00 44.38  ? 523 HOH   A O   1 
HETATM 4671 O O   . HOH   G 4 .   ? 10.697  13.541  5.682  1.00 41.68  ? 524 HOH   A O   1 
HETATM 4672 O O   . HOH   G 4 .   ? 13.820  -6.696  16.805 1.00 33.61  ? 525 HOH   A O   1 
HETATM 4673 O O   . HOH   G 4 .   ? 0.738   16.041  -0.072 1.00 54.00  ? 526 HOH   A O   1 
HETATM 4674 O O   . HOH   G 4 .   ? -4.165  6.591   13.825 1.00 43.53  ? 527 HOH   A O   1 
HETATM 4675 O O   . HOH   G 4 .   ? 23.004  0.283   13.885 1.00 45.39  ? 528 HOH   A O   1 
HETATM 4676 O O   . HOH   G 4 .   ? 14.741  -1.326  2.420  1.00 54.60  ? 529 HOH   A O   1 
HETATM 4677 O O   . HOH   G 4 .   ? 28.432  -2.767  13.227 1.00 45.09  ? 530 HOH   A O   1 
HETATM 4678 O O   . HOH   G 4 .   ? 23.167  -11.997 26.650 1.00 44.69  ? 531 HOH   A O   1 
HETATM 4679 O O   . HOH   G 4 .   ? -1.177  4.990   18.110 1.00 36.34  ? 532 HOH   A O   1 
HETATM 4680 O O   . HOH   G 4 .   ? -5.249  18.737  1.495  1.00 54.37  ? 533 HOH   A O   1 
HETATM 4681 O O   . HOH   G 4 .   ? 22.586  18.906  18.787 1.00 43.50  ? 534 HOH   A O   1 
HETATM 4682 O O   . HOH   G 4 .   ? 19.906  -20.398 20.074 1.00 46.59  ? 535 HOH   A O   1 
HETATM 4683 O O   . HOH   G 4 .   ? 17.509  -2.010  25.992 1.00 45.77  ? 536 HOH   A O   1 
HETATM 4684 O O   . HOH   G 4 .   ? -12.969 5.313   2.954  1.00 54.30  ? 537 HOH   A O   1 
HETATM 4685 O O   . HOH   G 4 .   ? 10.678  11.560  -0.992 1.00 57.15  ? 538 HOH   A O   1 
HETATM 4686 O O   . HOH   G 4 .   ? -3.641  5.809   -0.858 1.00 47.85  ? 539 HOH   A O   1 
HETATM 4687 O O   . HOH   G 4 .   ? 17.519  -16.971 27.447 1.00 33.77  ? 540 HOH   A O   1 
HETATM 4688 O O   . HOH   G 4 .   ? 8.798   -11.539 12.839 1.00 45.51  ? 541 HOH   A O   1 
HETATM 4689 O O   . HOH   G 4 .   ? 11.688  8.985   -0.437 1.00 56.00  ? 542 HOH   A O   1 
HETATM 4690 O O   . HOH   G 4 .   ? -14.145 19.916  10.392 1.00 66.45  ? 543 HOH   A O   1 
HETATM 4691 O O   . HOH   G 4 .   ? -2.512  -2.447  23.443 1.00 44.79  ? 544 HOH   A O   1 
HETATM 4692 O O   . HOH   G 4 .   ? 4.901   1.135   27.622 1.00 50.84  ? 545 HOH   A O   1 
HETATM 4693 O O   . HOH   G 4 .   ? 30.630  -31.333 10.713 1.00 62.61  ? 546 HOH   A O   1 
HETATM 4694 O O   . HOH   G 4 .   ? 8.105   7.941   32.963 1.00 52.91  ? 547 HOH   A O   1 
HETATM 4695 O O   . HOH   G 4 .   ? 6.443   -2.742  -1.216 1.00 50.00  ? 548 HOH   A O   1 
HETATM 4696 O O   . HOH   H 4 .   ? 12.118  -0.026  37.865 1.00 43.87  ? 501 HOH   B O   1 
HETATM 4697 O O   . HOH   H 4 .   ? 17.522  -6.031  34.300 1.00 47.79  ? 502 HOH   B O   1 
HETATM 4698 O O   . HOH   H 4 .   ? 39.784  0.532   36.359 1.00 42.53  ? 503 HOH   B O   1 
HETATM 4699 O O   . HOH   H 4 .   ? 9.896   0.372   35.498 1.00 49.75  ? 504 HOH   B O   1 
HETATM 4700 O O   . HOH   H 4 .   ? 18.362  24.416  41.697 1.00 58.49  ? 505 HOH   B O   1 
HETATM 4701 O O   . HOH   H 4 .   ? 40.943  8.582   42.518 1.00 50.73  ? 506 HOH   B O   1 
HETATM 4702 O O   . HOH   H 4 .   ? 14.963  -20.374 37.708 1.00 55.04  ? 507 HOH   B O   1 
HETATM 4703 O O   . HOH   H 4 .   ? 21.815  18.609  46.576 1.00 44.81  ? 508 HOH   B O   1 
HETATM 4704 O O   . HOH   H 4 .   ? 24.933  8.478   35.296 1.00 46.12  ? 509 HOH   B O   1 
HETATM 4705 O O   . HOH   H 4 .   ? 28.437  -2.187  53.566 1.00 38.88  ? 510 HOH   B O   1 
HETATM 4706 O O   . HOH   H 4 .   ? -3.357  -22.453 35.221 1.00 63.26  ? 511 HOH   B O   1 
HETATM 4707 O O   . HOH   H 4 .   ? 15.831  -3.845  26.229 1.00 46.71  ? 512 HOH   B O   1 
HETATM 4708 O O   . HOH   H 4 .   ? 14.831  5.011   42.631 1.00 45.74  ? 513 HOH   B O   1 
HETATM 4709 O O   . HOH   H 4 .   ? 16.090  -23.318 30.498 1.00 55.35  ? 514 HOH   B O   1 
HETATM 4710 O O   . HOH   H 4 .   ? 43.856  17.670  37.715 1.00 57.82  ? 515 HOH   B O   1 
HETATM 4711 O O   . HOH   H 4 .   ? 36.293  23.581  38.874 1.00 51.13  ? 516 HOH   B O   1 
HETATM 4712 O O   . HOH   H 4 .   ? 35.028  8.994   33.595 1.00 42.33  ? 517 HOH   B O   1 
HETATM 4713 O O   . HOH   H 4 .   ? 19.696  7.355   47.270 1.00 43.06  ? 518 HOH   B O   1 
HETATM 4714 O O   . HOH   H 4 .   ? 44.967  6.397   54.375 1.00 50.62  ? 519 HOH   B O   1 
HETATM 4715 O O   . HOH   H 4 .   ? 35.855  5.109   37.305 1.00 42.20  ? 520 HOH   B O   1 
HETATM 4716 O O   . HOH   H 4 .   ? 4.557   -1.697  26.073 1.00 47.65  ? 521 HOH   B O   1 
HETATM 4717 O O   . HOH   H 4 .   ? 20.601  12.421  24.746 1.00 48.92  ? 522 HOH   B O   1 
HETATM 4718 O O   . HOH   H 4 .   ? 29.577  17.243  31.609 1.00 52.31  ? 523 HOH   B O   1 
HETATM 4719 O O   . HOH   H 4 .   ? 45.353  17.380  44.669 1.00 46.43  ? 524 HOH   B O   1 
HETATM 4720 O O   . HOH   H 4 .   ? 39.728  18.227  54.107 1.00 46.87  ? 525 HOH   B O   1 
HETATM 4721 O O   . HOH   H 4 .   ? 10.853  -10.856 36.243 1.00 39.22  ? 526 HOH   B O   1 
HETATM 4722 O O   . HOH   H 4 .   ? 29.142  1.050   30.016 1.00 37.47  ? 527 HOH   B O   1 
HETATM 4723 O O   . HOH   H 4 .   ? 33.368  1.462   53.041 1.00 43.13  ? 528 HOH   B O   1 
HETATM 4724 O O   . HOH   H 4 .   ? 38.753  6.871   41.831 1.00 36.73  ? 529 HOH   B O   1 
HETATM 4725 O O   . HOH   H 4 .   ? 26.202  -2.854  46.267 1.00 32.62  ? 530 HOH   B O   1 
HETATM 4726 O O   . HOH   H 4 .   ? 40.654  8.950   35.517 1.00 47.62  ? 531 HOH   B O   1 
HETATM 4727 O O   . HOH   H 4 .   ? 32.310  11.868  57.423 1.00 50.07  ? 532 HOH   B O   1 
HETATM 4728 O O   . HOH   H 4 .   ? 38.040  7.048   36.938 1.00 41.68  ? 533 HOH   B O   1 
HETATM 4729 O O   . HOH   H 4 .   ? 21.024  -6.698  38.091 1.00 35.44  ? 534 HOH   B O   1 
HETATM 4730 O O   . HOH   H 4 .   ? 8.553   -1.973  32.348 1.00 52.81  ? 535 HOH   B O   1 
HETATM 4731 O O   . HOH   H 4 .   ? 25.885  -0.236  54.264 1.00 52.16  ? 536 HOH   B O   1 
HETATM 4732 O O   . HOH   H 4 .   ? 33.778  15.813  55.840 1.00 45.71  ? 537 HOH   B O   1 
HETATM 4733 O O   . HOH   H 4 .   ? 34.083  5.403   47.215 1.00 30.18  ? 538 HOH   B O   1 
HETATM 4734 O O   . HOH   H 4 .   ? 47.786  5.661   41.724 1.00 51.49  ? 539 HOH   B O   1 
HETATM 4735 O O   . HOH   H 4 .   ? 9.920   -7.371  43.789 1.00 51.05  ? 540 HOH   B O   1 
HETATM 4736 O O   . HOH   H 4 .   ? 11.584  -0.391  41.537 1.00 43.19  ? 541 HOH   B O   1 
HETATM 4737 O O   . HOH   H 4 .   ? 6.824   -23.435 52.950 1.00 50.98  ? 542 HOH   B O   1 
HETATM 4738 O O   . HOH   H 4 .   ? 6.551   14.321  43.492 1.00 59.74  ? 543 HOH   B O   1 
HETATM 4739 O O   . HOH   H 4 .   ? 22.092  -3.494  52.302 1.00 48.05  ? 544 HOH   B O   1 
HETATM 4740 O O   . HOH   H 4 .   ? 41.079  26.012  47.799 1.00 51.02  ? 545 HOH   B O   1 
HETATM 4741 O O   . HOH   H 4 .   ? 36.821  -2.763  40.937 1.00 45.09  ? 546 HOH   B O   1 
HETATM 4742 O O   . HOH   H 4 .   ? 25.849  -11.661 42.099 1.00 43.36  ? 547 HOH   B O   1 
HETATM 4743 O O   . HOH   H 4 .   ? 44.226  20.569  55.991 1.00 47.83  ? 548 HOH   B O   1 
HETATM 4744 O O   . HOH   H 4 .   ? -1.271  -5.059  22.626 1.00 49.56  ? 549 HOH   B O   1 
HETATM 4745 O O   . HOH   H 4 .   ? 17.205  -2.072  29.426 1.00 41.46  ? 550 HOH   B O   1 
HETATM 4746 O O   . HOH   H 4 .   ? 28.778  1.813   53.380 1.00 45.76  ? 551 HOH   B O   1 
HETATM 4747 O O   . HOH   H 4 .   ? 11.601  -12.171 28.486 1.00 42.07  ? 552 HOH   B O   1 
HETATM 4748 O O   . HOH   H 4 .   ? 30.233  10.934  57.146 1.00 52.12  ? 553 HOH   B O   1 
HETATM 4749 O O   . HOH   H 4 .   ? 38.287  5.415   56.408 1.00 48.25  ? 554 HOH   B O   1 
HETATM 4750 O O   . HOH   H 4 .   ? 6.460   -3.731  42.115 1.00 47.15  ? 555 HOH   B O   1 
HETATM 4751 O O   . HOH   H 4 .   ? 37.176  28.065  48.613 1.00 54.53  ? 556 HOH   B O   1 
HETATM 4752 O O   . HOH   H 4 .   ? 15.909  26.808  36.445 1.00 55.90  ? 557 HOH   B O   1 
HETATM 4753 O O   . HOH   H 4 .   ? 39.772  24.463  51.167 1.00 48.60  ? 558 HOH   B O   1 
HETATM 4754 O O   . HOH   H 4 .   ? 19.540  -1.571  53.995 1.00 55.61  ? 559 HOH   B O   1 
HETATM 4755 O O   . HOH   H 4 .   ? 7.902   10.048  33.598 1.00 58.59  ? 560 HOH   B O   1 
HETATM 4756 O O   . HOH   H 4 .   ? 10.447  -4.871  44.487 1.00 50.11  ? 561 HOH   B O   1 
HETATM 4757 O O   . HOH   H 4 .   ? 19.159  7.530   50.340 1.00 51.50  ? 562 HOH   B O   1 
HETATM 4758 O O   . HOH   H 4 .   ? 39.654  27.872  46.958 1.00 56.34  ? 563 HOH   B O   1 
HETATM 4759 O O   . HOH   H 4 .   ? 37.415  17.288  56.044 1.00 60.55  ? 564 HOH   B O   1 
HETATM 4760 O O   . HOH   H 4 .   ? 7.852   -5.514  44.231 1.00 52.37  ? 565 HOH   B O   1 
# 
