data_9NWA
# 
_entry.id   9NWA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9NWA         pdb_00009nwa 10.2210/pdb9nwa/pdb 
WWPDB D_1000281842 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-04 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9NWA 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-21 
_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_contact_author.id                 2 
_pdbx_contact_author.email              hiroaki.mitsuya2@nih.gov 
_pdbx_contact_author.name_first         Hiroaki 
_pdbx_contact_author.name_last          Mitsuya 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9274-3853 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bulut, H.'    1  0000-0003-0262-6296 
'Kuwata, N.'   2  ?                   
'Hayashi, H.'  3  ?                   
'Aoki, H.'     4  ?                   
'Das, D.'      5  ?                   
'Li, M.'       6  ?                   
'Wlodawer, A.' 7  ?                   
'Misumi, S.'   8  ?                   
'Tamamura, H.' 9  ?                   
'Mitsuya, H.'  10 0000-0001-9274-3853 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Impact of Single Halogen Atom Substitutions on Potency of Inhibitors Targeting SARS-CoV-2 Main Protease' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Bulut, H.'    1  ? 
primary 'Kuwata, N.'   2  ? 
primary 'Hayashi, H.'  3  ? 
primary 'Aoki, H.'     4  ? 
primary 'Das, D.'      5  ? 
primary 'Mi, L.'       6  ? 
primary 'Wlodawer, A.' 7  ? 
primary 'Misumi, S.'   8  ? 
primary 'Tamamura, H.' 9  ? 
primary 'Mitsuya, H.'  10 ? 
# 
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 1   3.4.22.69 ? ? ? 
2 non-polymer syn 
;(1R,2S,5S)-N-{(1S,2S)-1-(5-chloro-1,3-benzothiazol-2-yl)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-6,6-dimethyl-3-[3-methyl-N-(trifluoroacetyl)-L-valyl]-3-azabicyclo[3.1.0]hexane-2-carboxamide
;
672.158   1   ?         ? ? ? 
3 water       nat water 18.015    211 ?         ? ? ? 
# 
_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 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(1R,2S,5S)-N-{(1S,2S)-1-(5-chloro-1,3-benzothiazol-2-yl)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-6,6-dimethyl-3-[3-methyl-N-(trifluoroacetyl)-L-valyl]-3-azabicyclo[3.1.0]hexane-2-carboxamide
;
A1B7C 
3 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
A1B7C non-polymer         . 
;(1R,2S,5S)-N-{(1S,2S)-1-(5-chloro-1,3-benzothiazol-2-yl)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-6,6-dimethyl-3-[3-methyl-N-(trifluoroacetyl)-L-valyl]-3-azabicyclo[3.1.0]hexane-2-carboxamide
;
TKB-277-5Cl 'C30 H37 Cl F3 N5 O5 S' 672.158 
ALA   'L-peptide linking' y ALANINE ?           'C3 H7 N O2'            89.093  
ARG   'L-peptide linking' y ARGININE ?           'C6 H15 N4 O2 1'        175.209 
ASN   'L-peptide linking' y ASPARAGINE ?           'C4 H8 N2 O3'           132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?           'C4 H7 N O4'            133.103 
CYS   'L-peptide linking' y CYSTEINE ?           'C3 H7 N O2 S'          121.158 
GLN   'L-peptide linking' y GLUTAMINE ?           'C5 H10 N2 O3'          146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?           'C5 H9 N O4'            147.129 
GLY   'peptide linking'   y GLYCINE ?           'C2 H5 N O2'            75.067  
HIS   'L-peptide linking' y HISTIDINE ?           'C6 H10 N3 O2 1'        156.162 
HOH   non-polymer         . WATER ?           'H2 O'                  18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?           'C6 H13 N O2'           131.173 
LEU   'L-peptide linking' y LEUCINE ?           'C6 H13 N O2'           131.173 
LYS   'L-peptide linking' y LYSINE ?           'C6 H15 N2 O2 1'        147.195 
MET   'L-peptide linking' y METHIONINE ?           'C5 H11 N O2 S'         149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?           'C9 H11 N O2'           165.189 
PRO   'L-peptide linking' y PROLINE ?           'C5 H9 N O2'            115.130 
SER   'L-peptide linking' y SERINE ?           'C3 H7 N O3'            105.093 
THR   'L-peptide linking' y THREONINE ?           'C4 H9 N O3'            119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?           'C11 H12 N2 O2'         204.225 
TYR   'L-peptide linking' y TYROSINE ?           'C9 H11 N O3'           181.189 
VAL   'L-peptide linking' y VALINE ?           'C5 H11 N O2'           117.146 
# 
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 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 GLN 306 306 306 GLN GLN A . n 
# 
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 
B 2 A1B7C 1   401 1   A1B7C DRG A . 
C 3 HOH   1   501 102 HOH   HOH A . 
C 3 HOH   2   502 215 HOH   HOH A . 
C 3 HOH   3   503 173 HOH   HOH A . 
C 3 HOH   4   504 72  HOH   HOH A . 
C 3 HOH   5   505 105 HOH   HOH A . 
C 3 HOH   6   506 138 HOH   HOH A . 
C 3 HOH   7   507 129 HOH   HOH A . 
C 3 HOH   8   508 171 HOH   HOH A . 
C 3 HOH   9   509 150 HOH   HOH A . 
C 3 HOH   10  510 210 HOH   HOH A . 
C 3 HOH   11  511 1   HOH   HOH A . 
C 3 HOH   12  512 135 HOH   HOH A . 
C 3 HOH   13  513 229 HOH   HOH A . 
C 3 HOH   14  514 182 HOH   HOH A . 
C 3 HOH   15  515 119 HOH   HOH A . 
C 3 HOH   16  516 181 HOH   HOH A . 
C 3 HOH   17  517 106 HOH   HOH A . 
C 3 HOH   18  518 56  HOH   HOH A . 
C 3 HOH   19  519 143 HOH   HOH A . 
C 3 HOH   20  520 21  HOH   HOH A . 
C 3 HOH   21  521 96  HOH   HOH A . 
C 3 HOH   22  522 205 HOH   HOH A . 
C 3 HOH   23  523 111 HOH   HOH A . 
C 3 HOH   24  524 235 HOH   HOH A . 
C 3 HOH   25  525 11  HOH   HOH A . 
C 3 HOH   26  526 57  HOH   HOH A . 
C 3 HOH   27  527 15  HOH   HOH A . 
C 3 HOH   28  528 186 HOH   HOH A . 
C 3 HOH   29  529 165 HOH   HOH A . 
C 3 HOH   30  530 75  HOH   HOH A . 
C 3 HOH   31  531 28  HOH   HOH A . 
C 3 HOH   32  532 159 HOH   HOH A . 
C 3 HOH   33  533 216 HOH   HOH A . 
C 3 HOH   34  534 86  HOH   HOH A . 
C 3 HOH   35  535 85  HOH   HOH A . 
C 3 HOH   36  536 191 HOH   HOH A . 
C 3 HOH   37  537 70  HOH   HOH A . 
C 3 HOH   38  538 156 HOH   HOH A . 
C 3 HOH   39  539 188 HOH   HOH A . 
C 3 HOH   40  540 4   HOH   HOH A . 
C 3 HOH   41  541 217 HOH   HOH A . 
C 3 HOH   42  542 12  HOH   HOH A . 
C 3 HOH   43  543 27  HOH   HOH A . 
C 3 HOH   44  544 233 HOH   HOH A . 
C 3 HOH   45  545 41  HOH   HOH A . 
C 3 HOH   46  546 83  HOH   HOH A . 
C 3 HOH   47  547 160 HOH   HOH A . 
C 3 HOH   48  548 48  HOH   HOH A . 
C 3 HOH   49  549 81  HOH   HOH A . 
C 3 HOH   50  550 38  HOH   HOH A . 
C 3 HOH   51  551 26  HOH   HOH A . 
C 3 HOH   52  552 68  HOH   HOH A . 
C 3 HOH   53  553 46  HOH   HOH A . 
C 3 HOH   54  554 190 HOH   HOH A . 
C 3 HOH   55  555 2   HOH   HOH A . 
C 3 HOH   56  556 114 HOH   HOH A . 
C 3 HOH   57  557 107 HOH   HOH A . 
C 3 HOH   58  558 179 HOH   HOH A . 
C 3 HOH   59  559 115 HOH   HOH A . 
C 3 HOH   60  560 43  HOH   HOH A . 
C 3 HOH   61  561 92  HOH   HOH A . 
C 3 HOH   62  562 40  HOH   HOH A . 
C 3 HOH   63  563 97  HOH   HOH A . 
C 3 HOH   64  564 195 HOH   HOH A . 
C 3 HOH   65  565 241 HOH   HOH A . 
C 3 HOH   66  566 49  HOH   HOH A . 
C 3 HOH   67  567 214 HOH   HOH A . 
C 3 HOH   68  568 5   HOH   HOH A . 
C 3 HOH   69  569 55  HOH   HOH A . 
C 3 HOH   70  570 45  HOH   HOH A . 
C 3 HOH   71  571 223 HOH   HOH A . 
C 3 HOH   72  572 66  HOH   HOH A . 
C 3 HOH   73  573 89  HOH   HOH A . 
C 3 HOH   74  574 22  HOH   HOH A . 
C 3 HOH   75  575 44  HOH   HOH A . 
C 3 HOH   76  576 33  HOH   HOH A . 
C 3 HOH   77  577 228 HOH   HOH A . 
C 3 HOH   78  578 74  HOH   HOH A . 
C 3 HOH   79  579 125 HOH   HOH A . 
C 3 HOH   80  580 82  HOH   HOH A . 
C 3 HOH   81  581 32  HOH   HOH A . 
C 3 HOH   82  582 193 HOH   HOH A . 
C 3 HOH   83  583 8   HOH   HOH A . 
C 3 HOH   84  584 99  HOH   HOH A . 
C 3 HOH   85  585 34  HOH   HOH A . 
C 3 HOH   86  586 137 HOH   HOH A . 
C 3 HOH   87  587 110 HOH   HOH A . 
C 3 HOH   88  588 172 HOH   HOH A . 
C 3 HOH   89  589 220 HOH   HOH A . 
C 3 HOH   90  590 64  HOH   HOH A . 
C 3 HOH   91  591 37  HOH   HOH A . 
C 3 HOH   92  592 142 HOH   HOH A . 
C 3 HOH   93  593 206 HOH   HOH A . 
C 3 HOH   94  594 14  HOH   HOH A . 
C 3 HOH   95  595 19  HOH   HOH A . 
C 3 HOH   96  596 78  HOH   HOH A . 
C 3 HOH   97  597 198 HOH   HOH A . 
C 3 HOH   98  598 62  HOH   HOH A . 
C 3 HOH   99  599 152 HOH   HOH A . 
C 3 HOH   100 600 10  HOH   HOH A . 
C 3 HOH   101 601 155 HOH   HOH A . 
C 3 HOH   102 602 117 HOH   HOH A . 
C 3 HOH   103 603 178 HOH   HOH A . 
C 3 HOH   104 604 90  HOH   HOH A . 
C 3 HOH   105 605 30  HOH   HOH A . 
C 3 HOH   106 606 166 HOH   HOH A . 
C 3 HOH   107 607 47  HOH   HOH A . 
C 3 HOH   108 608 120 HOH   HOH A . 
C 3 HOH   109 609 212 HOH   HOH A . 
C 3 HOH   110 610 207 HOH   HOH A . 
C 3 HOH   111 611 58  HOH   HOH A . 
C 3 HOH   112 612 73  HOH   HOH A . 
C 3 HOH   113 613 153 HOH   HOH A . 
C 3 HOH   114 614 103 HOH   HOH A . 
C 3 HOH   115 615 7   HOH   HOH A . 
C 3 HOH   116 616 24  HOH   HOH A . 
C 3 HOH   117 617 112 HOH   HOH A . 
C 3 HOH   118 618 77  HOH   HOH A . 
C 3 HOH   119 619 84  HOH   HOH A . 
C 3 HOH   120 620 20  HOH   HOH A . 
C 3 HOH   121 621 31  HOH   HOH A . 
C 3 HOH   122 622 6   HOH   HOH A . 
C 3 HOH   123 623 116 HOH   HOH A . 
C 3 HOH   124 624 203 HOH   HOH A . 
C 3 HOH   125 625 36  HOH   HOH A . 
C 3 HOH   126 626 69  HOH   HOH A . 
C 3 HOH   127 627 243 HOH   HOH A . 
C 3 HOH   128 628 189 HOH   HOH A . 
C 3 HOH   129 629 87  HOH   HOH A . 
C 3 HOH   130 630 9   HOH   HOH A . 
C 3 HOH   131 631 51  HOH   HOH A . 
C 3 HOH   132 632 168 HOH   HOH A . 
C 3 HOH   133 633 201 HOH   HOH A . 
C 3 HOH   134 634 53  HOH   HOH A . 
C 3 HOH   135 635 147 HOH   HOH A . 
C 3 HOH   136 636 29  HOH   HOH A . 
C 3 HOH   137 637 239 HOH   HOH A . 
C 3 HOH   138 638 67  HOH   HOH A . 
C 3 HOH   139 639 185 HOH   HOH A . 
C 3 HOH   140 640 25  HOH   HOH A . 
C 3 HOH   141 641 169 HOH   HOH A . 
C 3 HOH   142 642 226 HOH   HOH A . 
C 3 HOH   143 643 146 HOH   HOH A . 
C 3 HOH   144 644 177 HOH   HOH A . 
C 3 HOH   145 645 130 HOH   HOH A . 
C 3 HOH   146 646 60  HOH   HOH A . 
C 3 HOH   147 647 52  HOH   HOH A . 
C 3 HOH   148 648 221 HOH   HOH A . 
C 3 HOH   149 649 126 HOH   HOH A . 
C 3 HOH   150 650 23  HOH   HOH A . 
C 3 HOH   151 651 3   HOH   HOH A . 
C 3 HOH   152 652 139 HOH   HOH A . 
C 3 HOH   153 653 88  HOH   HOH A . 
C 3 HOH   154 654 158 HOH   HOH A . 
C 3 HOH   155 655 244 HOH   HOH A . 
C 3 HOH   156 656 76  HOH   HOH A . 
C 3 HOH   157 657 42  HOH   HOH A . 
C 3 HOH   158 658 128 HOH   HOH A . 
C 3 HOH   159 659 136 HOH   HOH A . 
C 3 HOH   160 660 118 HOH   HOH A . 
C 3 HOH   161 661 164 HOH   HOH A . 
C 3 HOH   162 662 91  HOH   HOH A . 
C 3 HOH   163 663 236 HOH   HOH A . 
C 3 HOH   164 664 59  HOH   HOH A . 
C 3 HOH   165 665 109 HOH   HOH A . 
C 3 HOH   166 666 170 HOH   HOH A . 
C 3 HOH   167 667 18  HOH   HOH A . 
C 3 HOH   168 668 13  HOH   HOH A . 
C 3 HOH   169 669 127 HOH   HOH A . 
C 3 HOH   170 670 174 HOH   HOH A . 
C 3 HOH   171 671 232 HOH   HOH A . 
C 3 HOH   172 672 134 HOH   HOH A . 
C 3 HOH   173 673 63  HOH   HOH A . 
C 3 HOH   174 674 100 HOH   HOH A . 
C 3 HOH   175 675 121 HOH   HOH A . 
C 3 HOH   176 676 208 HOH   HOH A . 
C 3 HOH   177 677 167 HOH   HOH A . 
C 3 HOH   178 678 16  HOH   HOH A . 
C 3 HOH   179 679 209 HOH   HOH A . 
C 3 HOH   180 680 39  HOH   HOH A . 
C 3 HOH   181 681 227 HOH   HOH A . 
C 3 HOH   182 682 213 HOH   HOH A . 
C 3 HOH   183 683 211 HOH   HOH A . 
C 3 HOH   184 684 202 HOH   HOH A . 
C 3 HOH   185 685 123 HOH   HOH A . 
C 3 HOH   186 686 80  HOH   HOH A . 
C 3 HOH   187 687 180 HOH   HOH A . 
C 3 HOH   188 688 230 HOH   HOH A . 
C 3 HOH   189 689 101 HOH   HOH A . 
C 3 HOH   190 690 93  HOH   HOH A . 
C 3 HOH   191 691 240 HOH   HOH A . 
C 3 HOH   192 692 194 HOH   HOH A . 
C 3 HOH   193 693 61  HOH   HOH A . 
C 3 HOH   194 694 175 HOH   HOH A . 
C 3 HOH   195 695 204 HOH   HOH A . 
C 3 HOH   196 696 238 HOH   HOH A . 
C 3 HOH   197 697 140 HOH   HOH A . 
C 3 HOH   198 698 94  HOH   HOH A . 
C 3 HOH   199 699 196 HOH   HOH A . 
C 3 HOH   200 700 163 HOH   HOH A . 
C 3 HOH   201 701 65  HOH   HOH A . 
C 3 HOH   202 702 141 HOH   HOH A . 
C 3 HOH   203 703 71  HOH   HOH A . 
C 3 HOH   204 704 145 HOH   HOH A . 
C 3 HOH   205 705 95  HOH   HOH A . 
C 3 HOH   206 706 176 HOH   HOH A . 
C 3 HOH   207 707 144 HOH   HOH A . 
C 3 HOH   208 708 184 HOH   HOH A . 
C 3 HOH   209 709 79  HOH   HOH A . 
C 3 HOH   210 710 237 HOH   HOH A . 
C 3 HOH   211 711 157 HOH   HOH A . 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0425 ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .        ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .        ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        ? 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NWA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.531 
_cell.length_a_esd                 ? 
_cell.length_b                     64.238 
_cell.length_b_esd                 ? 
_cell.length_c                     105.383 
_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                         9NWA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_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                   9NWA 
_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             2.28 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.01 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES pH 7.5, 16 % w/v Polyethylene glycol 3,350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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 EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979497 
_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                        'NSLS-II BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979497 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9NWA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               50.00 
_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                                     29303 
_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                           94.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.88 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.092 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.8 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             27006 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          66.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.393 
_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]                            -0.18 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.28 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.10 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.448 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9NWA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             32.14 
_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                     25644 
_refine.ls_number_reflns_R_free                  1362 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.99 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16615 
_refine.ls_R_factor_R_free                       0.19999 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16442 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.130 
_refine.pdbx_overall_ESU_R_Free                  0.121 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_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                 ? 
_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                             2.715 
_refine.overall_SU_ML                            0.082 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        32.14 
_refine_hist.number_atoms_solvent             211 
_refine_hist.number_atoms_total               2623 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2367 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         45 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  0.012  2494 ? r_bond_refined_d             ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  2295 ? r_bond_other_d               ? ? ? 
'X-RAY DIFFRACTION' ? 1.819  1.815  3403 ? r_angle_refined_deg          ? ? ? 
'X-RAY DIFFRACTION' ? 0.604  1.734  5271 ? r_angle_other_deg            ? ? ? 
'X-RAY DIFFRACTION' ? 7.010  5.000  309  ? r_dihedral_angle_1_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 22.482 6.467  15   ? r_dihedral_angle_2_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 12.238 10.000 391  ? r_dihedral_angle_3_deg       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 0.086  0.200  382  ? r_chiral_restr               ? ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  2966 ? r_gen_planes_refined         ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  592  ? r_gen_planes_other           ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? ? 
'X-RAY DIFFRACTION' ? 2.017  1.994  1233 ? r_mcbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 2.017  1.994  1233 ? r_mcbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? 3.105  3.570  1543 ? r_mcangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 3.104  3.574  1544 ? r_mcangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 3.075  2.343  1261 ? r_scbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 3.074  2.343  1262 ? r_scbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 4.731  4.139  1858 ? r_scangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 6.441  21.36  2793 ? r_long_range_B_refined       ? ? ? 
'X-RAY DIFFRACTION' ? 6.440  21.36  2794 ? r_long_range_B_other         ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? ? 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          1.802 
_refine_ls_shell.d_res_low                           1.848 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                58 
_refine_ls_shell.number_reflns_R_work                1259 
_refine_ls_shell.percent_reflns_obs                  61.95 
_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                     0.283 
_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.correlation_coeff_Fo_to_Fc          ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free     ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free   ? 
_refine_ls_shell.pdbx_total_number_of_bins_used      20 
_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                     0.315 
# 
_struct.entry_id                     9NWA 
_struct.title                        'Crystal structure of SARS-CoV-2 main protease in complex with an inhibitor TKB-277-5Cl' 
_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        9NWA 
_struct_keywords.text            'SARS-CoV-2 main protease, 3C-like proteinase, VIRAL PROTEIN, SARS-CoV-2' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_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 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9NWA 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 306 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0DTD1 
_struct_ref_seq.db_align_beg                  3264 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  3569 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       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)' 3140  ? 
1 MORE         -14   ? 
1 'SSA (A^2)'  24780 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0           0.0          0.0          0.0          0.0          1.0           0.0 
0.0          0.0          0.0          1.0          0.0          
2 'crystal symmetry operation' 2_555 -x,-y,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 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 GLU A 47  ? ASN A 51  ? GLU A 47  ASN A 51  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? 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 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        one 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            145 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           A1B7C 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C20 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             145 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            A1B7C 
_struct_conn.ptnr2_auth_seq_id             401 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.913 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1B7C 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      145 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1B7C 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       145 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C20 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1B7C 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 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 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? LEU A 167 ? CYS A 156 LEU A 167 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? LEU A 167 ? CYS A 156 LEU A 167 
AA3 3 VAL A 171 ? THR A 175 ? VAL A 171 THR A 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 32  ? N LEU A 32  O VAL A 35  ? O VAL A 35  
AA1 5 6 N VAL A 36  ? N VAL A 36  O LEU A 89  ? O LEU A 89  
AA1 6 7 O VAL A 86  ? O VAL A 86  N GLN A 83  ? N GLN A 83  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N LEU A 167 ? N LEU A 167 O VAL A 171 ? O VAL A 171 
# 
_pdbx_entry_details.entry_id                   9NWA 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 76  ? ? CZ A ARG 76  ? ? NH1 A ARG 76  ? ? 123.64 120.30 3.34   0.50 N 
2 1 NE A ARG 76  ? ? CZ A ARG 76  ? ? NH2 A ARG 76  ? ? 116.33 120.30 -3.97  0.50 N 
3 1 CG A MET 276 ? ? SD A MET 276 ? ? CE  A MET 276 ? ? 87.56  100.20 -12.64 1.60 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 33  ? ? 52.22   -126.42 
2 1 SER A 46  ? ? -77.07  43.75   
3 1 GLU A 47  ? ? -145.14 -38.89  
4 1 ASN A 51  ? ? -151.98 74.33   
5 1 ASN A 84  ? ? 53.86   -122.11 
6 1 TYR A 154 ? A 49.84   -106.92 
7 1 TYR A 154 ? B 59.05   -104.31 
8 1 THR A 169 ? ? 83.49   8.68    
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 4   ? ? 0.103 'SIDE CHAIN' 
2 1 ARG A 76  ? ? 0.201 'SIDE CHAIN' 
3 1 ARG A 217 ? ? 0.096 'SIDE CHAIN' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 685 ? C HOH . 
2 1 A HOH 690 ? C HOH . 
# 
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 
A1B7C C4   C  N N 1   
A1B7C C14  C  N S 2   
A1B7C C5   C  N S 3   
A1B7C C6   C  N N 4   
A1B7C C11  C  N R 5   
A1B7C C7   C  N N 6   
A1B7C C8   C  N N 7   
A1B7C C9   C  N N 8   
A1B7C C10  C  N S 9   
A1B7C C12  C  N S 10  
A1B7C C13  C  N N 11  
A1B7C N1   N  N N 12  
A1B7C N2   N  N N 13  
A1B7C C3   C  N N 14  
A1B7C N3   N  N N 15  
A1B7C C1   C  N N 16  
A1B7C C2   C  N N 17  
A1B7C O1   O  N N 18  
A1B7C F1   F  N N 19  
A1B7C F2   F  N N 20  
A1B7C F3   F  N N 21  
A1B7C O2   O  N N 22  
A1B7C O3   O  N N 23  
A1B7C C15  C  N N 24  
A1B7C C16  C  N S 25  
A1B7C C17  C  N N 26  
A1B7C C18  C  N N 27  
A1B7C N4   N  N N 28  
A1B7C C19  C  N N 29  
A1B7C O4   O  N N 30  
A1B7C C20  C  N S 31  
A1B7C O5   O  N N 32  
A1B7C C21  C  Y N 33  
A1B7C N5   N  Y N 34  
A1B7C C22  C  Y N 35  
A1B7C C23  C  Y N 36  
A1B7C C24  C  Y N 37  
A1B7C CL1  CL N N 38  
A1B7C C25  C  Y N 39  
A1B7C C26  C  Y N 40  
A1B7C C27  C  Y N 41  
A1B7C S1   S  Y N 42  
A1B7C C28  C  N N 43  
A1B7C C29  C  N N 44  
A1B7C C30  C  N N 45  
A1B7C H1   H  N N 46  
A1B7C H2   H  N N 47  
A1B7C H3   H  N N 48  
A1B7C H4   H  N N 49  
A1B7C H5   H  N N 50  
A1B7C H6   H  N N 51  
A1B7C H7   H  N N 52  
A1B7C H8   H  N N 53  
A1B7C H9   H  N N 54  
A1B7C H10  H  N N 55  
A1B7C H11  H  N N 56  
A1B7C H12  H  N N 57  
A1B7C H13  H  N N 58  
A1B7C H14  H  N N 59  
A1B7C H15  H  N N 60  
A1B7C H16  H  N N 61  
A1B7C H17  H  N N 62  
A1B7C H18  H  N N 63  
A1B7C H19  H  N N 64  
A1B7C H20  H  N N 65  
A1B7C H21  H  N N 66  
A1B7C H22  H  N N 67  
A1B7C H23  H  N N 68  
A1B7C H24  H  N N 69  
A1B7C H25  H  N N 70  
A1B7C H26  H  N N 71  
A1B7C H27  H  N N 72  
A1B7C H28  H  N N 73  
A1B7C H29  H  N N 74  
A1B7C H30  H  N N 75  
A1B7C H31  H  N N 76  
A1B7C H32  H  N N 77  
A1B7C H33  H  N N 78  
A1B7C H34  H  N N 79  
A1B7C H35  H  N N 80  
A1B7C H36  H  N N 81  
A1B7C H37  H  N N 82  
ALA   N    N  N N 83  
ALA   CA   C  N S 84  
ALA   C    C  N N 85  
ALA   O    O  N N 86  
ALA   CB   C  N N 87  
ALA   OXT  O  N N 88  
ALA   H    H  N N 89  
ALA   H2   H  N N 90  
ALA   HA   H  N N 91  
ALA   HB1  H  N N 92  
ALA   HB2  H  N N 93  
ALA   HB3  H  N N 94  
ALA   HXT  H  N N 95  
ARG   N    N  N N 96  
ARG   CA   C  N S 97  
ARG   C    C  N N 98  
ARG   O    O  N N 99  
ARG   CB   C  N N 100 
ARG   CG   C  N N 101 
ARG   CD   C  N N 102 
ARG   NE   N  N N 103 
ARG   CZ   C  N N 104 
ARG   NH1  N  N N 105 
ARG   NH2  N  N N 106 
ARG   OXT  O  N N 107 
ARG   H    H  N N 108 
ARG   H2   H  N N 109 
ARG   HA   H  N N 110 
ARG   HB2  H  N N 111 
ARG   HB3  H  N N 112 
ARG   HG2  H  N N 113 
ARG   HG3  H  N N 114 
ARG   HD2  H  N N 115 
ARG   HD3  H  N N 116 
ARG   HE   H  N N 117 
ARG   HH11 H  N N 118 
ARG   HH12 H  N N 119 
ARG   HH21 H  N N 120 
ARG   HH22 H  N N 121 
ARG   HXT  H  N N 122 
ASN   N    N  N N 123 
ASN   CA   C  N S 124 
ASN   C    C  N N 125 
ASN   O    O  N N 126 
ASN   CB   C  N N 127 
ASN   CG   C  N N 128 
ASN   OD1  O  N N 129 
ASN   ND2  N  N N 130 
ASN   OXT  O  N N 131 
ASN   H    H  N N 132 
ASN   H2   H  N N 133 
ASN   HA   H  N N 134 
ASN   HB2  H  N N 135 
ASN   HB3  H  N N 136 
ASN   HD21 H  N N 137 
ASN   HD22 H  N N 138 
ASN   HXT  H  N N 139 
ASP   N    N  N N 140 
ASP   CA   C  N S 141 
ASP   C    C  N N 142 
ASP   O    O  N N 143 
ASP   CB   C  N N 144 
ASP   CG   C  N N 145 
ASP   OD1  O  N N 146 
ASP   OD2  O  N N 147 
ASP   OXT  O  N N 148 
ASP   H    H  N N 149 
ASP   H2   H  N N 150 
ASP   HA   H  N N 151 
ASP   HB2  H  N N 152 
ASP   HB3  H  N N 153 
ASP   HD2  H  N N 154 
ASP   HXT  H  N N 155 
CYS   N    N  N N 156 
CYS   CA   C  N R 157 
CYS   C    C  N N 158 
CYS   O    O  N N 159 
CYS   CB   C  N N 160 
CYS   SG   S  N N 161 
CYS   OXT  O  N N 162 
CYS   H    H  N N 163 
CYS   H2   H  N N 164 
CYS   HA   H  N N 165 
CYS   HB2  H  N N 166 
CYS   HB3  H  N N 167 
CYS   HG   H  N N 168 
CYS   HXT  H  N N 169 
GLN   N    N  N N 170 
GLN   CA   C  N S 171 
GLN   C    C  N N 172 
GLN   O    O  N N 173 
GLN   CB   C  N N 174 
GLN   CG   C  N N 175 
GLN   CD   C  N N 176 
GLN   OE1  O  N N 177 
GLN   NE2  N  N N 178 
GLN   OXT  O  N N 179 
GLN   H    H  N N 180 
GLN   H2   H  N N 181 
GLN   HA   H  N N 182 
GLN   HB2  H  N N 183 
GLN   HB3  H  N N 184 
GLN   HG2  H  N N 185 
GLN   HG3  H  N N 186 
GLN   HE21 H  N N 187 
GLN   HE22 H  N N 188 
GLN   HXT  H  N N 189 
GLU   N    N  N N 190 
GLU   CA   C  N S 191 
GLU   C    C  N N 192 
GLU   O    O  N N 193 
GLU   CB   C  N N 194 
GLU   CG   C  N N 195 
GLU   CD   C  N N 196 
GLU   OE1  O  N N 197 
GLU   OE2  O  N N 198 
GLU   OXT  O  N N 199 
GLU   H    H  N N 200 
GLU   H2   H  N N 201 
GLU   HA   H  N N 202 
GLU   HB2  H  N N 203 
GLU   HB3  H  N N 204 
GLU   HG2  H  N N 205 
GLU   HG3  H  N N 206 
GLU   HE2  H  N N 207 
GLU   HXT  H  N N 208 
GLY   N    N  N N 209 
GLY   CA   C  N N 210 
GLY   C    C  N N 211 
GLY   O    O  N N 212 
GLY   OXT  O  N N 213 
GLY   H    H  N N 214 
GLY   H2   H  N N 215 
GLY   HA2  H  N N 216 
GLY   HA3  H  N N 217 
GLY   HXT  H  N N 218 
HIS   N    N  N N 219 
HIS   CA   C  N S 220 
HIS   C    C  N N 221 
HIS   O    O  N N 222 
HIS   CB   C  N N 223 
HIS   CG   C  Y N 224 
HIS   ND1  N  Y N 225 
HIS   CD2  C  Y N 226 
HIS   CE1  C  Y N 227 
HIS   NE2  N  Y N 228 
HIS   OXT  O  N N 229 
HIS   H    H  N N 230 
HIS   H2   H  N N 231 
HIS   HA   H  N N 232 
HIS   HB2  H  N N 233 
HIS   HB3  H  N N 234 
HIS   HD1  H  N N 235 
HIS   HD2  H  N N 236 
HIS   HE1  H  N N 237 
HIS   HE2  H  N N 238 
HIS   HXT  H  N N 239 
HOH   O    O  N N 240 
HOH   H1   H  N N 241 
HOH   H2   H  N N 242 
ILE   N    N  N N 243 
ILE   CA   C  N S 244 
ILE   C    C  N N 245 
ILE   O    O  N N 246 
ILE   CB   C  N S 247 
ILE   CG1  C  N N 248 
ILE   CG2  C  N N 249 
ILE   CD1  C  N N 250 
ILE   OXT  O  N N 251 
ILE   H    H  N N 252 
ILE   H2   H  N N 253 
ILE   HA   H  N N 254 
ILE   HB   H  N N 255 
ILE   HG12 H  N N 256 
ILE   HG13 H  N N 257 
ILE   HG21 H  N N 258 
ILE   HG22 H  N N 259 
ILE   HG23 H  N N 260 
ILE   HD11 H  N N 261 
ILE   HD12 H  N N 262 
ILE   HD13 H  N N 263 
ILE   HXT  H  N N 264 
LEU   N    N  N N 265 
LEU   CA   C  N S 266 
LEU   C    C  N N 267 
LEU   O    O  N N 268 
LEU   CB   C  N N 269 
LEU   CG   C  N N 270 
LEU   CD1  C  N N 271 
LEU   CD2  C  N N 272 
LEU   OXT  O  N N 273 
LEU   H    H  N N 274 
LEU   H2   H  N N 275 
LEU   HA   H  N N 276 
LEU   HB2  H  N N 277 
LEU   HB3  H  N N 278 
LEU   HG   H  N N 279 
LEU   HD11 H  N N 280 
LEU   HD12 H  N N 281 
LEU   HD13 H  N N 282 
LEU   HD21 H  N N 283 
LEU   HD22 H  N N 284 
LEU   HD23 H  N N 285 
LEU   HXT  H  N N 286 
LYS   N    N  N N 287 
LYS   CA   C  N S 288 
LYS   C    C  N N 289 
LYS   O    O  N N 290 
LYS   CB   C  N N 291 
LYS   CG   C  N N 292 
LYS   CD   C  N N 293 
LYS   CE   C  N N 294 
LYS   NZ   N  N N 295 
LYS   OXT  O  N N 296 
LYS   H    H  N N 297 
LYS   H2   H  N N 298 
LYS   HA   H  N N 299 
LYS   HB2  H  N N 300 
LYS   HB3  H  N N 301 
LYS   HG2  H  N N 302 
LYS   HG3  H  N N 303 
LYS   HD2  H  N N 304 
LYS   HD3  H  N N 305 
LYS   HE2  H  N N 306 
LYS   HE3  H  N N 307 
LYS   HZ1  H  N N 308 
LYS   HZ2  H  N N 309 
LYS   HZ3  H  N N 310 
LYS   HXT  H  N N 311 
MET   N    N  N N 312 
MET   CA   C  N S 313 
MET   C    C  N N 314 
MET   O    O  N N 315 
MET   CB   C  N N 316 
MET   CG   C  N N 317 
MET   SD   S  N N 318 
MET   CE   C  N N 319 
MET   OXT  O  N N 320 
MET   H    H  N N 321 
MET   H2   H  N N 322 
MET   HA   H  N N 323 
MET   HB2  H  N N 324 
MET   HB3  H  N N 325 
MET   HG2  H  N N 326 
MET   HG3  H  N N 327 
MET   HE1  H  N N 328 
MET   HE2  H  N N 329 
MET   HE3  H  N N 330 
MET   HXT  H  N N 331 
PHE   N    N  N N 332 
PHE   CA   C  N S 333 
PHE   C    C  N N 334 
PHE   O    O  N N 335 
PHE   CB   C  N N 336 
PHE   CG   C  Y N 337 
PHE   CD1  C  Y N 338 
PHE   CD2  C  Y N 339 
PHE   CE1  C  Y N 340 
PHE   CE2  C  Y N 341 
PHE   CZ   C  Y N 342 
PHE   OXT  O  N N 343 
PHE   H    H  N N 344 
PHE   H2   H  N N 345 
PHE   HA   H  N N 346 
PHE   HB2  H  N N 347 
PHE   HB3  H  N N 348 
PHE   HD1  H  N N 349 
PHE   HD2  H  N N 350 
PHE   HE1  H  N N 351 
PHE   HE2  H  N N 352 
PHE   HZ   H  N N 353 
PHE   HXT  H  N N 354 
PRO   N    N  N N 355 
PRO   CA   C  N S 356 
PRO   C    C  N N 357 
PRO   O    O  N N 358 
PRO   CB   C  N N 359 
PRO   CG   C  N N 360 
PRO   CD   C  N N 361 
PRO   OXT  O  N N 362 
PRO   H    H  N N 363 
PRO   HA   H  N N 364 
PRO   HB2  H  N N 365 
PRO   HB3  H  N N 366 
PRO   HG2  H  N N 367 
PRO   HG3  H  N N 368 
PRO   HD2  H  N N 369 
PRO   HD3  H  N N 370 
PRO   HXT  H  N N 371 
SER   N    N  N N 372 
SER   CA   C  N S 373 
SER   C    C  N N 374 
SER   O    O  N N 375 
SER   CB   C  N N 376 
SER   OG   O  N N 377 
SER   OXT  O  N N 378 
SER   H    H  N N 379 
SER   H2   H  N N 380 
SER   HA   H  N N 381 
SER   HB2  H  N N 382 
SER   HB3  H  N N 383 
SER   HG   H  N N 384 
SER   HXT  H  N N 385 
THR   N    N  N N 386 
THR   CA   C  N S 387 
THR   C    C  N N 388 
THR   O    O  N N 389 
THR   CB   C  N R 390 
THR   OG1  O  N N 391 
THR   CG2  C  N N 392 
THR   OXT  O  N N 393 
THR   H    H  N N 394 
THR   H2   H  N N 395 
THR   HA   H  N N 396 
THR   HB   H  N N 397 
THR   HG1  H  N N 398 
THR   HG21 H  N N 399 
THR   HG22 H  N N 400 
THR   HG23 H  N N 401 
THR   HXT  H  N N 402 
TRP   N    N  N N 403 
TRP   CA   C  N S 404 
TRP   C    C  N N 405 
TRP   O    O  N N 406 
TRP   CB   C  N N 407 
TRP   CG   C  Y N 408 
TRP   CD1  C  Y N 409 
TRP   CD2  C  Y N 410 
TRP   NE1  N  Y N 411 
TRP   CE2  C  Y N 412 
TRP   CE3  C  Y N 413 
TRP   CZ2  C  Y N 414 
TRP   CZ3  C  Y N 415 
TRP   CH2  C  Y N 416 
TRP   OXT  O  N N 417 
TRP   H    H  N N 418 
TRP   H2   H  N N 419 
TRP   HA   H  N N 420 
TRP   HB2  H  N N 421 
TRP   HB3  H  N N 422 
TRP   HD1  H  N N 423 
TRP   HE1  H  N N 424 
TRP   HE3  H  N N 425 
TRP   HZ2  H  N N 426 
TRP   HZ3  H  N N 427 
TRP   HH2  H  N N 428 
TRP   HXT  H  N N 429 
TYR   N    N  N N 430 
TYR   CA   C  N S 431 
TYR   C    C  N N 432 
TYR   O    O  N N 433 
TYR   CB   C  N N 434 
TYR   CG   C  Y N 435 
TYR   CD1  C  Y N 436 
TYR   CD2  C  Y N 437 
TYR   CE1  C  Y N 438 
TYR   CE2  C  Y N 439 
TYR   CZ   C  Y N 440 
TYR   OH   O  N N 441 
TYR   OXT  O  N N 442 
TYR   H    H  N N 443 
TYR   H2   H  N N 444 
TYR   HA   H  N N 445 
TYR   HB2  H  N N 446 
TYR   HB3  H  N N 447 
TYR   HD1  H  N N 448 
TYR   HD2  H  N N 449 
TYR   HE1  H  N N 450 
TYR   HE2  H  N N 451 
TYR   HH   H  N N 452 
TYR   HXT  H  N N 453 
VAL   N    N  N N 454 
VAL   CA   C  N S 455 
VAL   C    C  N N 456 
VAL   O    O  N N 457 
VAL   CB   C  N N 458 
VAL   CG1  C  N N 459 
VAL   CG2  C  N N 460 
VAL   OXT  O  N N 461 
VAL   H    H  N N 462 
VAL   H2   H  N N 463 
VAL   HA   H  N N 464 
VAL   HB   H  N N 465 
VAL   HG11 H  N N 466 
VAL   HG12 H  N N 467 
VAL   HG13 H  N N 468 
VAL   HG21 H  N N 469 
VAL   HG22 H  N N 470 
VAL   HG23 H  N N 471 
VAL   HXT  H  N N 472 
# 
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 
A1B7C C25 C26  doub Y N 1   
A1B7C C25 C24  sing Y N 2   
A1B7C CL1 C24  sing N N 3   
A1B7C C26 C27  sing Y N 4   
A1B7C C24 C23  doub Y N 5   
A1B7C C27 S1   sing Y N 6   
A1B7C C27 C22  doub Y N 7   
A1B7C C23 C22  sing Y N 8   
A1B7C S1  C21  sing Y N 9   
A1B7C C22 N5   sing Y N 10  
A1B7C N5  C21  doub Y N 11  
A1B7C C21 C20  sing N N 12  
A1B7C O5  C20  sing N N 13  
A1B7C C20 C14  sing N N 14  
A1B7C C29 C28  sing N N 15  
A1B7C C14 N3   sing N N 16  
A1B7C C14 C15  sing N N 17  
A1B7C C11 C28  sing N N 18  
A1B7C C11 C10  sing N N 19  
A1B7C C11 C12  sing N N 20  
A1B7C N3  C13  sing N N 21  
A1B7C C28 C10  sing N N 22  
A1B7C C28 C30  sing N N 23  
A1B7C C15 C16  sing N N 24  
A1B7C C13 O3   doub N N 25  
A1B7C C13 C12  sing N N 26  
A1B7C C10 C9   sing N N 27  
A1B7C C12 N2   sing N N 28  
A1B7C C16 C17  sing N N 29  
A1B7C C16 C19  sing N N 30  
A1B7C C9  N2   sing N N 31  
A1B7C C17 C18  sing N N 32  
A1B7C N2  C8   sing N N 33  
A1B7C O4  C19  doub N N 34  
A1B7C C19 N4   sing N N 35  
A1B7C C18 N4   sing N N 36  
A1B7C C8  O2   doub N N 37  
A1B7C C8  C5   sing N N 38  
A1B7C C1  C2   sing N N 39  
A1B7C C5  C2   sing N N 40  
A1B7C C5  N1   sing N N 41  
A1B7C C2  C3   sing N N 42  
A1B7C C2  C4   sing N N 43  
A1B7C N1  C6   sing N N 44  
A1B7C O1  C6   doub N N 45  
A1B7C C6  C7   sing N N 46  
A1B7C F2  C7   sing N N 47  
A1B7C C7  F3   sing N N 48  
A1B7C C7  F1   sing N N 49  
A1B7C C4  H1   sing N N 50  
A1B7C C4  H2   sing N N 51  
A1B7C C4  H3   sing N N 52  
A1B7C C14 H4   sing N N 53  
A1B7C C5  H5   sing N N 54  
A1B7C C11 H6   sing N N 55  
A1B7C C9  H7   sing N N 56  
A1B7C C9  H8   sing N N 57  
A1B7C C10 H9   sing N N 58  
A1B7C C12 H10  sing N N 59  
A1B7C N1  H11  sing N N 60  
A1B7C C3  H12  sing N N 61  
A1B7C C3  H13  sing N N 62  
A1B7C C3  H14  sing N N 63  
A1B7C N3  H15  sing N N 64  
A1B7C C1  H16  sing N N 65  
A1B7C C1  H17  sing N N 66  
A1B7C C1  H18  sing N N 67  
A1B7C C15 H19  sing N N 68  
A1B7C C15 H20  sing N N 69  
A1B7C C16 H21  sing N N 70  
A1B7C C17 H22  sing N N 71  
A1B7C C17 H23  sing N N 72  
A1B7C C18 H24  sing N N 73  
A1B7C C18 H25  sing N N 74  
A1B7C N4  H26  sing N N 75  
A1B7C C23 H27  sing N N 76  
A1B7C C25 H28  sing N N 77  
A1B7C C26 H29  sing N N 78  
A1B7C C29 H30  sing N N 79  
A1B7C C29 H31  sing N N 80  
A1B7C C29 H32  sing N N 81  
A1B7C C30 H33  sing N N 82  
A1B7C C30 H34  sing N N 83  
A1B7C C30 H35  sing N N 84  
A1B7C C20 H36  sing N N 85  
A1B7C O5  H37  sing N N 86  
ALA   N   CA   sing N N 87  
ALA   N   H    sing N N 88  
ALA   N   H2   sing N N 89  
ALA   CA  C    sing N N 90  
ALA   CA  CB   sing N N 91  
ALA   CA  HA   sing N N 92  
ALA   C   O    doub N N 93  
ALA   C   OXT  sing N N 94  
ALA   CB  HB1  sing N N 95  
ALA   CB  HB2  sing N N 96  
ALA   CB  HB3  sing N N 97  
ALA   OXT HXT  sing N N 98  
ARG   N   CA   sing N N 99  
ARG   N   H    sing N N 100 
ARG   N   H2   sing N N 101 
ARG   CA  C    sing N N 102 
ARG   CA  CB   sing N N 103 
ARG   CA  HA   sing N N 104 
ARG   C   O    doub N N 105 
ARG   C   OXT  sing N N 106 
ARG   CB  CG   sing N N 107 
ARG   CB  HB2  sing N N 108 
ARG   CB  HB3  sing N N 109 
ARG   CG  CD   sing N N 110 
ARG   CG  HG2  sing N N 111 
ARG   CG  HG3  sing N N 112 
ARG   CD  NE   sing N N 113 
ARG   CD  HD2  sing N N 114 
ARG   CD  HD3  sing N N 115 
ARG   NE  CZ   sing N N 116 
ARG   NE  HE   sing N N 117 
ARG   CZ  NH1  sing N N 118 
ARG   CZ  NH2  doub N N 119 
ARG   NH1 HH11 sing N N 120 
ARG   NH1 HH12 sing N N 121 
ARG   NH2 HH21 sing N N 122 
ARG   NH2 HH22 sing N N 123 
ARG   OXT HXT  sing N N 124 
ASN   N   CA   sing N N 125 
ASN   N   H    sing N N 126 
ASN   N   H2   sing N N 127 
ASN   CA  C    sing N N 128 
ASN   CA  CB   sing N N 129 
ASN   CA  HA   sing N N 130 
ASN   C   O    doub N N 131 
ASN   C   OXT  sing N N 132 
ASN   CB  CG   sing N N 133 
ASN   CB  HB2  sing N N 134 
ASN   CB  HB3  sing N N 135 
ASN   CG  OD1  doub N N 136 
ASN   CG  ND2  sing N N 137 
ASN   ND2 HD21 sing N N 138 
ASN   ND2 HD22 sing N N 139 
ASN   OXT HXT  sing N N 140 
ASP   N   CA   sing N N 141 
ASP   N   H    sing N N 142 
ASP   N   H2   sing N N 143 
ASP   CA  C    sing N N 144 
ASP   CA  CB   sing N N 145 
ASP   CA  HA   sing N N 146 
ASP   C   O    doub N N 147 
ASP   C   OXT  sing N N 148 
ASP   CB  CG   sing N N 149 
ASP   CB  HB2  sing N N 150 
ASP   CB  HB3  sing N N 151 
ASP   CG  OD1  doub N N 152 
ASP   CG  OD2  sing N N 153 
ASP   OD2 HD2  sing N N 154 
ASP   OXT HXT  sing N N 155 
CYS   N   CA   sing N N 156 
CYS   N   H    sing N N 157 
CYS   N   H2   sing N N 158 
CYS   CA  C    sing N N 159 
CYS   CA  CB   sing N N 160 
CYS   CA  HA   sing N N 161 
CYS   C   O    doub N N 162 
CYS   C   OXT  sing N N 163 
CYS   CB  SG   sing N N 164 
CYS   CB  HB2  sing N N 165 
CYS   CB  HB3  sing N N 166 
CYS   SG  HG   sing N N 167 
CYS   OXT HXT  sing N N 168 
GLN   N   CA   sing N N 169 
GLN   N   H    sing N N 170 
GLN   N   H2   sing N N 171 
GLN   CA  C    sing N N 172 
GLN   CA  CB   sing N N 173 
GLN   CA  HA   sing N N 174 
GLN   C   O    doub N N 175 
GLN   C   OXT  sing N N 176 
GLN   CB  CG   sing N N 177 
GLN   CB  HB2  sing N N 178 
GLN   CB  HB3  sing N N 179 
GLN   CG  CD   sing N N 180 
GLN   CG  HG2  sing N N 181 
GLN   CG  HG3  sing N N 182 
GLN   CD  OE1  doub N N 183 
GLN   CD  NE2  sing N N 184 
GLN   NE2 HE21 sing N N 185 
GLN   NE2 HE22 sing N N 186 
GLN   OXT HXT  sing N N 187 
GLU   N   CA   sing N N 188 
GLU   N   H    sing N N 189 
GLU   N   H2   sing N N 190 
GLU   CA  C    sing N N 191 
GLU   CA  CB   sing N N 192 
GLU   CA  HA   sing N N 193 
GLU   C   O    doub N N 194 
GLU   C   OXT  sing N N 195 
GLU   CB  CG   sing N N 196 
GLU   CB  HB2  sing N N 197 
GLU   CB  HB3  sing N N 198 
GLU   CG  CD   sing N N 199 
GLU   CG  HG2  sing N N 200 
GLU   CG  HG3  sing N N 201 
GLU   CD  OE1  doub N N 202 
GLU   CD  OE2  sing N N 203 
GLU   OE2 HE2  sing N N 204 
GLU   OXT HXT  sing N N 205 
GLY   N   CA   sing N N 206 
GLY   N   H    sing N N 207 
GLY   N   H2   sing N N 208 
GLY   CA  C    sing N N 209 
GLY   CA  HA2  sing N N 210 
GLY   CA  HA3  sing N N 211 
GLY   C   O    doub N N 212 
GLY   C   OXT  sing N N 213 
GLY   OXT HXT  sing N N 214 
HIS   N   CA   sing N N 215 
HIS   N   H    sing N N 216 
HIS   N   H2   sing N N 217 
HIS   CA  C    sing N N 218 
HIS   CA  CB   sing N N 219 
HIS   CA  HA   sing N N 220 
HIS   C   O    doub N N 221 
HIS   C   OXT  sing N N 222 
HIS   CB  CG   sing N N 223 
HIS   CB  HB2  sing N N 224 
HIS   CB  HB3  sing N N 225 
HIS   CG  ND1  sing Y N 226 
HIS   CG  CD2  doub Y N 227 
HIS   ND1 CE1  doub Y N 228 
HIS   ND1 HD1  sing N N 229 
HIS   CD2 NE2  sing Y N 230 
HIS   CD2 HD2  sing N N 231 
HIS   CE1 NE2  sing Y N 232 
HIS   CE1 HE1  sing N N 233 
HIS   NE2 HE2  sing N N 234 
HIS   OXT HXT  sing N N 235 
HOH   O   H1   sing N N 236 
HOH   O   H2   sing N N 237 
ILE   N   CA   sing N N 238 
ILE   N   H    sing N N 239 
ILE   N   H2   sing N N 240 
ILE   CA  C    sing N N 241 
ILE   CA  CB   sing N N 242 
ILE   CA  HA   sing N N 243 
ILE   C   O    doub N N 244 
ILE   C   OXT  sing N N 245 
ILE   CB  CG1  sing N N 246 
ILE   CB  CG2  sing N N 247 
ILE   CB  HB   sing N N 248 
ILE   CG1 CD1  sing N N 249 
ILE   CG1 HG12 sing N N 250 
ILE   CG1 HG13 sing N N 251 
ILE   CG2 HG21 sing N N 252 
ILE   CG2 HG22 sing N N 253 
ILE   CG2 HG23 sing N N 254 
ILE   CD1 HD11 sing N N 255 
ILE   CD1 HD12 sing N N 256 
ILE   CD1 HD13 sing N N 257 
ILE   OXT HXT  sing N N 258 
LEU   N   CA   sing N N 259 
LEU   N   H    sing N N 260 
LEU   N   H2   sing N N 261 
LEU   CA  C    sing N N 262 
LEU   CA  CB   sing N N 263 
LEU   CA  HA   sing N N 264 
LEU   C   O    doub N N 265 
LEU   C   OXT  sing N N 266 
LEU   CB  CG   sing N N 267 
LEU   CB  HB2  sing N N 268 
LEU   CB  HB3  sing N N 269 
LEU   CG  CD1  sing N N 270 
LEU   CG  CD2  sing N N 271 
LEU   CG  HG   sing N N 272 
LEU   CD1 HD11 sing N N 273 
LEU   CD1 HD12 sing N N 274 
LEU   CD1 HD13 sing N N 275 
LEU   CD2 HD21 sing N N 276 
LEU   CD2 HD22 sing N N 277 
LEU   CD2 HD23 sing N N 278 
LEU   OXT HXT  sing N N 279 
LYS   N   CA   sing N N 280 
LYS   N   H    sing N N 281 
LYS   N   H2   sing N N 282 
LYS   CA  C    sing N N 283 
LYS   CA  CB   sing N N 284 
LYS   CA  HA   sing N N 285 
LYS   C   O    doub N N 286 
LYS   C   OXT  sing N N 287 
LYS   CB  CG   sing N N 288 
LYS   CB  HB2  sing N N 289 
LYS   CB  HB3  sing N N 290 
LYS   CG  CD   sing N N 291 
LYS   CG  HG2  sing N N 292 
LYS   CG  HG3  sing N N 293 
LYS   CD  CE   sing N N 294 
LYS   CD  HD2  sing N N 295 
LYS   CD  HD3  sing N N 296 
LYS   CE  NZ   sing N N 297 
LYS   CE  HE2  sing N N 298 
LYS   CE  HE3  sing N N 299 
LYS   NZ  HZ1  sing N N 300 
LYS   NZ  HZ2  sing N N 301 
LYS   NZ  HZ3  sing N N 302 
LYS   OXT HXT  sing N N 303 
MET   N   CA   sing N N 304 
MET   N   H    sing N N 305 
MET   N   H2   sing N N 306 
MET   CA  C    sing N N 307 
MET   CA  CB   sing N N 308 
MET   CA  HA   sing N N 309 
MET   C   O    doub N N 310 
MET   C   OXT  sing N N 311 
MET   CB  CG   sing N N 312 
MET   CB  HB2  sing N N 313 
MET   CB  HB3  sing N N 314 
MET   CG  SD   sing N N 315 
MET   CG  HG2  sing N N 316 
MET   CG  HG3  sing N N 317 
MET   SD  CE   sing N N 318 
MET   CE  HE1  sing N N 319 
MET   CE  HE2  sing N N 320 
MET   CE  HE3  sing N N 321 
MET   OXT HXT  sing N N 322 
PHE   N   CA   sing N N 323 
PHE   N   H    sing N N 324 
PHE   N   H2   sing N N 325 
PHE   CA  C    sing N N 326 
PHE   CA  CB   sing N N 327 
PHE   CA  HA   sing N N 328 
PHE   C   O    doub N N 329 
PHE   C   OXT  sing N N 330 
PHE   CB  CG   sing N N 331 
PHE   CB  HB2  sing N N 332 
PHE   CB  HB3  sing N N 333 
PHE   CG  CD1  doub Y N 334 
PHE   CG  CD2  sing Y N 335 
PHE   CD1 CE1  sing Y N 336 
PHE   CD1 HD1  sing N N 337 
PHE   CD2 CE2  doub Y N 338 
PHE   CD2 HD2  sing N N 339 
PHE   CE1 CZ   doub Y N 340 
PHE   CE1 HE1  sing N N 341 
PHE   CE2 CZ   sing Y N 342 
PHE   CE2 HE2  sing N N 343 
PHE   CZ  HZ   sing N N 344 
PHE   OXT HXT  sing N N 345 
PRO   N   CA   sing N N 346 
PRO   N   CD   sing N N 347 
PRO   N   H    sing N N 348 
PRO   CA  C    sing N N 349 
PRO   CA  CB   sing N N 350 
PRO   CA  HA   sing N N 351 
PRO   C   O    doub N N 352 
PRO   C   OXT  sing N N 353 
PRO   CB  CG   sing N N 354 
PRO   CB  HB2  sing N N 355 
PRO   CB  HB3  sing N N 356 
PRO   CG  CD   sing N N 357 
PRO   CG  HG2  sing N N 358 
PRO   CG  HG3  sing N N 359 
PRO   CD  HD2  sing N N 360 
PRO   CD  HD3  sing N N 361 
PRO   OXT HXT  sing N N 362 
SER   N   CA   sing N N 363 
SER   N   H    sing N N 364 
SER   N   H2   sing N N 365 
SER   CA  C    sing N N 366 
SER   CA  CB   sing N N 367 
SER   CA  HA   sing N N 368 
SER   C   O    doub N N 369 
SER   C   OXT  sing N N 370 
SER   CB  OG   sing N N 371 
SER   CB  HB2  sing N N 372 
SER   CB  HB3  sing N N 373 
SER   OG  HG   sing N N 374 
SER   OXT HXT  sing N N 375 
THR   N   CA   sing N N 376 
THR   N   H    sing N N 377 
THR   N   H2   sing N N 378 
THR   CA  C    sing N N 379 
THR   CA  CB   sing N N 380 
THR   CA  HA   sing N N 381 
THR   C   O    doub N N 382 
THR   C   OXT  sing N N 383 
THR   CB  OG1  sing N N 384 
THR   CB  CG2  sing N N 385 
THR   CB  HB   sing N N 386 
THR   OG1 HG1  sing N N 387 
THR   CG2 HG21 sing N N 388 
THR   CG2 HG22 sing N N 389 
THR   CG2 HG23 sing N N 390 
THR   OXT HXT  sing N N 391 
TRP   N   CA   sing N N 392 
TRP   N   H    sing N N 393 
TRP   N   H2   sing N N 394 
TRP   CA  C    sing N N 395 
TRP   CA  CB   sing N N 396 
TRP   CA  HA   sing N N 397 
TRP   C   O    doub N N 398 
TRP   C   OXT  sing N N 399 
TRP   CB  CG   sing N N 400 
TRP   CB  HB2  sing N N 401 
TRP   CB  HB3  sing N N 402 
TRP   CG  CD1  doub Y N 403 
TRP   CG  CD2  sing Y N 404 
TRP   CD1 NE1  sing Y N 405 
TRP   CD1 HD1  sing N N 406 
TRP   CD2 CE2  doub Y N 407 
TRP   CD2 CE3  sing Y N 408 
TRP   NE1 CE2  sing Y N 409 
TRP   NE1 HE1  sing N N 410 
TRP   CE2 CZ2  sing Y N 411 
TRP   CE3 CZ3  doub Y N 412 
TRP   CE3 HE3  sing N N 413 
TRP   CZ2 CH2  doub Y N 414 
TRP   CZ2 HZ2  sing N N 415 
TRP   CZ3 CH2  sing Y N 416 
TRP   CZ3 HZ3  sing N N 417 
TRP   CH2 HH2  sing N N 418 
TRP   OXT HXT  sing N N 419 
TYR   N   CA   sing N N 420 
TYR   N   H    sing N N 421 
TYR   N   H2   sing N N 422 
TYR   CA  C    sing N N 423 
TYR   CA  CB   sing N N 424 
TYR   CA  HA   sing N N 425 
TYR   C   O    doub N N 426 
TYR   C   OXT  sing N N 427 
TYR   CB  CG   sing N N 428 
TYR   CB  HB2  sing N N 429 
TYR   CB  HB3  sing N N 430 
TYR   CG  CD1  doub Y N 431 
TYR   CG  CD2  sing Y N 432 
TYR   CD1 CE1  sing Y N 433 
TYR   CD1 HD1  sing N N 434 
TYR   CD2 CE2  doub Y N 435 
TYR   CD2 HD2  sing N N 436 
TYR   CE1 CZ   doub Y N 437 
TYR   CE1 HE1  sing N N 438 
TYR   CE2 CZ   sing Y N 439 
TYR   CE2 HE2  sing N N 440 
TYR   CZ  OH   sing N N 441 
TYR   OH  HH   sing N N 442 
TYR   OXT HXT  sing N N 443 
VAL   N   CA   sing N N 444 
VAL   N   H    sing N N 445 
VAL   N   H2   sing N N 446 
VAL   CA  C    sing N N 447 
VAL   CA  CB   sing N N 448 
VAL   CA  HA   sing N N 449 
VAL   C   O    doub N N 450 
VAL   C   OXT  sing N N 451 
VAL   CB  CG1  sing N N 452 
VAL   CB  CG2  sing N N 453 
VAL   CB  HB   sing N N 454 
VAL   CG1 HG11 sing N N 455 
VAL   CG1 HG12 sing N N 456 
VAL   CG1 HG13 sing N N 457 
VAL   CG2 HG21 sing N N 458 
VAL   CG2 HG22 sing N N 459 
VAL   CG2 HG23 sing N N 460 
VAL   OXT HXT  sing N N 461 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Cancer Institute (NIH/NCI)' 
_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   8UH5 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9NWA 
_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]   0.021963 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015567 
_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]   0.009489 
_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  
CL 
F  
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   ? -15.765 -6.271 31.204 1.00 18.57 ? 1   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? -15.166 -5.778 32.474 1.00 20.00 ? 1   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? -13.651 -5.819 32.417 1.00 18.76 ? 1   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? -13.062 -6.329 31.463 1.00 17.13 ? 1   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? -15.654 -6.613 33.673 1.00 21.35 ? 1   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? -17.064 -6.491 33.776 1.00 29.61 ? 1   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? -13.068 -5.287 33.497 1.00 19.20 ? 2   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? -11.633 -5.150 33.642 1.00 19.71 ? 2   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? -11.254 -3.728 33.274 1.00 18.85 ? 2   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? -11.986 -3.045 32.584 1.00 20.84 ? 2   GLY   A O   1 
ATOM   11   N  N   . PHE   A 1 3   ? -10.129 -3.262 33.787 1.00 19.51 ? 3   PHE   A N   1 
ATOM   12   C  CA  . PHE   A 1 3   ? -9.708  -1.913 33.502 1.00 18.71 ? 3   PHE   A CA  1 
ATOM   13   C  C   . PHE   A 1 3   ? -8.196  -1.910 33.468 1.00 18.81 ? 3   PHE   A C   1 
ATOM   14   O  O   . PHE   A 1 3   ? -7.542  -2.367 34.403 1.00 17.95 ? 3   PHE   A O   1 
ATOM   15   C  CB  . PHE   A 1 3   ? -10.295 -0.958 34.550 1.00 19.40 ? 3   PHE   A CB  1 
ATOM   16   C  CG  . PHE   A 1 3   ? -10.270 0.483  34.080 1.00 17.52 ? 3   PHE   A CG  1 
ATOM   17   C  CD1 . PHE   A 1 3   ? -11.218 0.933  33.172 1.00 19.96 ? 3   PHE   A CD1 1 
ATOM   18   C  CD2 . PHE   A 1 3   ? -9.310  1.376  34.548 1.00 21.85 ? 3   PHE   A CD2 1 
ATOM   19   C  CE1 . PHE   A 1 3   ? -11.209 2.249  32.745 1.00 22.15 ? 3   PHE   A CE1 1 
ATOM   20   C  CE2 . PHE   A 1 3   ? -9.313  2.687  34.138 1.00 20.37 ? 3   PHE   A CE2 1 
ATOM   21   C  CZ  . PHE   A 1 3   ? -10.245 3.115  33.211 1.00 21.09 ? 3   PHE   A CZ  1 
ATOM   22   N  N   . ARG   A 1 4   ? -7.671  -1.467 32.329 1.00 17.35 ? 4   ARG   A N   1 
ATOM   23   C  CA  . ARG   A 1 4   ? -6.256  -1.523 32.063 1.00 17.78 ? 4   ARG   A CA  1 
ATOM   24   C  C   . ARG   A 1 4   ? -5.783  -0.166 31.577 1.00 15.61 ? 4   ARG   A C   1 
ATOM   25   O  O   . ARG   A 1 4   ? -6.521  0.581  30.957 1.00 16.73 ? 4   ARG   A O   1 
ATOM   26   C  CB  . ARG   A 1 4   ? -5.990  -2.579 30.991 1.00 20.27 ? 4   ARG   A CB  1 
ATOM   27   C  CG  . ARG   A 1 4   ? -5.949  -3.991 31.533 1.00 25.72 ? 4   ARG   A CG  1 
ATOM   28   C  CD  . ARG   A 1 4   ? -4.576  -4.206 32.173 1.00 31.23 ? 4   ARG   A CD  1 
ATOM   29   N  NE  . ARG   A 1 4   ? -4.193  -5.613 32.042 1.00 37.03 ? 4   ARG   A NE  1 
ATOM   30   C  CZ  . ARG   A 1 4   ? -3.203  -6.142 32.738 1.00 42.03 ? 4   ARG   A CZ  1 
ATOM   31   N  NH1 . ARG   A 1 4   ? -2.275  -5.339 33.237 1.00 47.01 ? 4   ARG   A NH1 1 
ATOM   32   N  NH2 . ARG   A 1 4   ? -3.131  -7.456 32.899 1.00 36.25 ? 4   ARG   A NH2 1 
ATOM   33   N  N   . LYS   A 1 5   ? -4.505  0.113  31.801 1.00 16.51 ? 5   LYS   A N   1 
ATOM   34   C  CA  . LYS   A 1 5   ? -3.893  1.265  31.166 1.00 18.93 ? 5   LYS   A CA  1 
ATOM   35   C  C   . LYS   A 1 5   ? -3.737  0.958  29.677 1.00 18.29 ? 5   LYS   A C   1 
ATOM   36   O  O   . LYS   A 1 5   ? -2.831  0.268  29.271 1.00 22.09 ? 5   LYS   A O   1 
ATOM   37   C  CB  . LYS   A 1 5   ? -2.547  1.642  31.789 1.00 24.47 ? 5   LYS   A CB  1 
ATOM   38   C  CG  . LYS   A 1 5   ? -2.131  3.080  31.480 1.00 30.34 ? 5   LYS   A CG  1 
ATOM   39   C  CD  . LYS   A 1 5   ? -1.034  3.593  32.403 1.00 38.68 ? 5   LYS   A CD  1 
ATOM   40   C  CE  . LYS   A 1 5   ? -1.494  3.998  33.783 1.00 44.67 ? 5   LYS   A CE  1 
ATOM   41   N  NZ  . LYS   A 1 5   ? -2.474  5.083  33.721 1.00 48.18 ? 5   LYS   A NZ  1 
ATOM   42   N  N   . MET   A 1 6   ? -4.586  1.546  28.852 1.00 18.16 ? 6   MET   A N   1 
ATOM   43   C  CA  . MET   A 1 6   ? -4.697  1.178  27.463 1.00 20.28 ? 6   MET   A CA  1 
ATOM   44   C  C   . MET   A 1 6   ? -4.176  2.335  26.614 1.00 18.86 ? 6   MET   A C   1 
ATOM   45   O  O   . MET   A 1 6   ? -4.529  3.496  26.842 1.00 18.80 ? 6   MET   A O   1 
ATOM   46   C  CB  . MET   A 1 6   ? -6.185  0.928  27.214 1.00 23.11 ? 6   MET   A CB  1 
ATOM   47   C  CG  . MET   A 1 6   ? -6.554  0.436  25.878 1.00 30.94 ? 6   MET   A CG  1 
ATOM   48   S  SD  . MET   A 1 6   ? -8.331  0.157  25.925 1.00 35.59 ? 6   MET   A SD  1 
ATOM   49   C  CE  . MET   A 1 6   ? -8.467  -1.309 26.948 1.00 29.98 ? 6   MET   A CE  1 
ATOM   50   N  N   . ALA   A 1 7   ? -3.325  1.999  25.646 1.00 16.41 ? 7   ALA   A N   1 
ATOM   51   C  CA  . ALA   A 1 7   ? -2.790  2.949  24.689 1.00 16.39 ? 7   ALA   A CA  1 
ATOM   52   C  C   . ALA   A 1 7   ? -3.629  2.895  23.416 1.00 16.06 ? 7   ALA   A C   1 
ATOM   53   O  O   . ALA   A 1 7   ? -4.356  1.929  23.206 1.00 15.46 ? 7   ALA   A O   1 
ATOM   54   C  CB  . ALA   A 1 7   ? -1.355  2.613  24.434 1.00 16.25 ? 7   ALA   A CB  1 
ATOM   55   N  N   . PHE   A 1 8   ? -3.601  3.964  22.627 1.00 14.18 ? 8   PHE   A N   1 
ATOM   56   C  CA  . PHE   A 1 8   ? -4.188  3.942  21.303 1.00 15.44 ? 8   PHE   A CA  1 
ATOM   57   C  C   . PHE   A 1 8   ? -3.446  2.951  20.413 1.00 14.71 ? 8   PHE   A C   1 
ATOM   58   O  O   . PHE   A 1 8   ? -2.248  2.762  20.524 1.00 14.15 ? 8   PHE   A O   1 
ATOM   59   C  CB  . PHE   A 1 8   ? -4.155  5.311  20.636 1.00 16.00 ? 8   PHE   A CB  1 
ATOM   60   C  CG  . PHE   A 1 8   ? -5.101  6.286  21.294 1.00 16.71 ? 8   PHE   A CG  1 
ATOM   61   C  CD1 . PHE   A 1 8   ? -6.450  6.274  20.987 1.00 19.05 ? 8   PHE   A CD1 1 
ATOM   62   C  CD2 . PHE   A 1 8   ? -4.629  7.236  22.187 1.00 19.61 ? 8   PHE   A CD2 1 
ATOM   63   C  CE1 . PHE   A 1 8   ? -7.311  7.166  21.606 1.00 19.25 ? 8   PHE   A CE1 1 
ATOM   64   C  CE2 . PHE   A 1 8   ? -5.498  8.101  22.818 1.00 22.11 ? 8   PHE   A CE2 1 
ATOM   65   C  CZ  . PHE   A 1 8   ? -6.828  8.078  22.515 1.00 20.90 ? 8   PHE   A CZ  1 
ATOM   66   N  N   . PRO   A 1 9   ? -4.121  2.380  19.404 1.00 16.94 ? 9   PRO   A N   1 
ATOM   67   C  CA  . PRO   A 1 9   ? -3.426  1.568  18.407 1.00 17.56 ? 9   PRO   A CA  1 
ATOM   68   C  C   . PRO   A 1 9   ? -2.423  2.473  17.685 1.00 15.84 ? 9   PRO   A C   1 
ATOM   69   O  O   . PRO   A 1 9   ? -2.780  3.595  17.340 1.00 17.24 ? 9   PRO   A O   1 
ATOM   70   C  CB  . PRO   A 1 9   ? -4.526  1.097  17.439 1.00 18.45 ? 9   PRO   A CB  1 
ATOM   71   C  CG  . PRO   A 1 9   ? -5.842  1.508  18.088 1.00 21.61 ? 9   PRO   A CG  1 
ATOM   72   C  CD  . PRO   A 1 9   ? -5.561  2.545  19.148 1.00 18.31 ? 9   PRO   A CD  1 
ATOM   73   N  N   . SER   A 1 10  ? -1.223  1.966  17.456 1.00 15.66 ? 10  SER   A N   1 
ATOM   74   C  CA  . SER   A 1 10  ? -0.107  2.810  17.052 1.00 16.12 ? 10  SER   A CA  1 
ATOM   75   C  C   . SER   A 1 10  ? 0.122   2.810  15.536 1.00 15.50 ? 10  SER   A C   1 
ATOM   76   O  O   . SER   A 1 10  ? 1.007   3.529  15.059 1.00 15.04 ? 10  SER   A O   1 
ATOM   77   C  CB  . SER   A 1 10  ? 1.164   2.400  17.770 1.00 15.78 ? 10  SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 10  ? 1.515   1.032  17.556 1.00 14.25 ? 10  SER   A OG  1 
ATOM   79   N  N   . GLY   A 1 11  ? -0.635  2.022  14.760 1.00 16.00 ? 11  GLY   A N   1 
ATOM   80   C  CA  . GLY   A 1 11  ? -0.249  1.749  13.377 1.00 14.52 ? 11  GLY   A CA  1 
ATOM   81   C  C   . GLY   A 1 11  ? -0.158  3.031  12.534 1.00 16.13 ? 11  GLY   A C   1 
ATOM   82   O  O   . GLY   A 1 11  ? 0.763   3.189  11.738 1.00 19.78 ? 11  GLY   A O   1 
ATOM   83   N  N   . LYS   A 1 12  ? -1.125  3.940  12.697 1.00 16.57 ? 12  LYS   A N   1 
ATOM   84   C  CA  . LYS   A 1 12  ? -1.148  5.187  11.930 1.00 17.69 ? 12  LYS   A CA  1 
ATOM   85   C  C   . LYS   A 1 12  ? 0.125   6.011  12.157 1.00 17.54 ? 12  LYS   A C   1 
ATOM   86   O  O   . LYS   A 1 12  ? 0.591   6.696  11.247 1.00 14.34 ? 12  LYS   A O   1 
ATOM   87   C  CB  . LYS   A 1 12  ? -2.407  6.004  12.219 1.00 20.07 ? 12  LYS   A CB  1 
ATOM   88   C  CG  . LYS   A 1 12  ? -3.654  5.446  11.537 1.00 25.06 ? 12  LYS   A CG  1 
ATOM   89   C  CD  . LYS   A 1 12  ? -4.937  5.927  12.180 1.00 31.64 ? 12  LYS   A CD  1 
ATOM   90   C  CE  . LYS   A 1 12  ? -6.146  5.304  11.552 1.00 35.89 ? 12  LYS   A CE  1 
ATOM   91   N  NZ  . LYS   A 1 12  ? -6.753  6.293  10.667 1.00 39.68 ? 12  LYS   A NZ  1 
ATOM   92   N  N   . VAL   A 1 13  ? 0.659   5.977  13.389 1.00 15.14 ? 13  VAL   A N   1 
ATOM   93   C  CA  . VAL   A 1 13  ? 1.901   6.665  13.707 1.00 14.57 ? 13  VAL   A CA  1 
ATOM   94   C  C   . VAL   A 1 13  ? 3.131   5.883  13.276 1.00 13.63 ? 13  VAL   A C   1 
ATOM   95   O  O   . VAL   A 1 13  ? 4.109   6.493  12.828 1.00 14.64 ? 13  VAL   A O   1 
ATOM   96   C  CB  . VAL   A 1 13  ? 1.930   6.989  15.216 1.00 14.40 ? 13  VAL   A CB  1 
ATOM   97   C  CG1 . VAL   A 1 13  ? 3.219   7.721  15.585 1.00 15.07 ? 13  VAL   A CG1 1 
ATOM   98   C  CG2 . VAL   A 1 13  ? 0.722   7.823  15.603 1.00 14.87 ? 13  VAL   A CG2 1 
ATOM   99   N  N   . GLU   A 1 14  ? 3.128   4.546  13.400 1.00 13.02 ? 14  GLU   A N   1 
ATOM   100  C  CA  . GLU   A 1 14  ? 4.234   3.723  12.954 1.00 13.24 ? 14  GLU   A CA  1 
ATOM   101  C  C   . GLU   A 1 14  ? 4.577   4.010  11.492 1.00 14.13 ? 14  GLU   A C   1 
ATOM   102  O  O   . GLU   A 1 14  ? 5.757   4.125  11.147 1.00 13.69 ? 14  GLU   A O   1 
ATOM   103  C  CB  . GLU   A 1 14  ? 4.011   2.221  13.085 1.00 14.89 ? 14  GLU   A CB  1 
ATOM   104  C  CG  . GLU   A 1 14  ? 3.860   1.736  14.518 1.00 15.40 ? 14  GLU   A CG  1 
ATOM   105  C  CD  . GLU   A 1 14  ? 3.257   0.338  14.620 1.00 17.12 ? 14  GLU   A CD  1 
ATOM   106  O  OE1 . GLU   A 1 14  ? 3.806   -0.584 13.941 1.00 18.48 ? 14  GLU   A OE1 1 
ATOM   107  O  OE2 . GLU   A 1 14  ? 2.212   0.205  15.335 1.00 19.11 ? 14  GLU   A OE2 1 
ATOM   108  N  N   . GLY   A 1 15  ? 3.561   4.273  10.679 1.00 14.00 ? 15  GLY   A N   1 
ATOM   109  C  CA  . GLY   A 1 15  ? 3.795   4.498  9.253  1.00 16.34 ? 15  GLY   A CA  1 
ATOM   110  C  C   . GLY   A 1 15  ? 4.452   5.857  8.956  1.00 16.90 ? 15  GLY   A C   1 
ATOM   111  O  O   . GLY   A 1 15  ? 4.766   6.172  7.807  1.00 16.94 ? 15  GLY   A O   1 
ATOM   112  N  N   . CYS   A 1 16  ? 4.619   6.695  9.989  1.00 15.72 ? 16  CYS   A N   1 
ATOM   113  C  CA  . CYS   A 1 16  ? 5.177   8.023  9.823  1.00 14.52 ? 16  CYS   A CA  1 
ATOM   114  C  C   . CYS   A 1 16  ? 6.573   8.147  10.429 1.00 14.11 ? 16  CYS   A C   1 
ATOM   115  O  O   . CYS   A 1 16  ? 7.178   9.186  10.285 1.00 13.89 ? 16  CYS   A O   1 
ATOM   116  C  CB  . CYS   A 1 16  ? 4.324   9.069  10.512 1.00 15.83 ? 16  CYS   A CB  1 
ATOM   117  S  SG  . CYS   A 1 16  ? 2.625   9.127  9.875  1.00 18.50 ? 16  CYS   A SG  1 
ATOM   118  N  N   . MET   A 1 17  ? 7.084   7.125  11.117 1.00 13.10 ? 17  MET   A N   1 
ATOM   119  C  CA  . MET   A 1 17  ? 8.386   7.267  11.771 1.00 13.90 ? 17  MET   A CA  1 
ATOM   120  C  C   . MET   A 1 17  ? 9.539   7.070  10.791 1.00 14.49 ? 17  MET   A C   1 
ATOM   121  O  O   . MET   A 1 17  ? 9.512   6.168  9.956  1.00 16.30 ? 17  MET   A O   1 
ATOM   122  C  CB  . MET   A 1 17  ? 8.521   6.260  12.907 1.00 14.79 ? 17  MET   A CB  1 
ATOM   123  C  CG  . MET   A 1 17  ? 7.478   6.464  13.974 1.00 14.89 ? 17  MET   A CG  1 
ATOM   124  S  SD  . MET   A 1 17  ? 7.300   8.141  14.640 1.00 15.14 ? 17  MET   A SD  1 
ATOM   125  C  CE  . MET   A 1 17  ? 9.000   8.516  15.108 1.00 17.35 ? 17  MET   A CE  1 
ATOM   126  N  N   . VAL   A 1 18  ? 10.558  7.932  10.899 1.00 13.76 ? 18  VAL   A N   1 
ATOM   127  C  CA  . VAL   A 1 18  ? 11.774  7.850  10.108 1.00 13.81 ? 18  VAL   A CA  1 
ATOM   128  C  C   . VAL   A 1 18  ? 12.963  8.148  11.011 1.00 14.08 ? 18  VAL   A C   1 
ATOM   129  O  O   . VAL   A 1 18  ? 12.779  8.539  12.147 1.00 14.18 ? 18  VAL   A O   1 
ATOM   130  C  CB  . VAL   A 1 18  ? 11.751  8.831  8.908  1.00 14.25 ? 18  VAL   A CB  1 
ATOM   131  C  CG1 . VAL   A 1 18  ? 10.590  8.492  7.974  1.00 14.53 ? 18  VAL   A CG1 1 
ATOM   132  C  CG2 . VAL   A 1 18  ? 11.679  10.286 9.356  1.00 14.61 ? 18  VAL   A CG2 1 
ATOM   133  N  N   . GLN   A 1 19  ? 14.164  7.967  10.458 1.00 14.80 ? 19  GLN   A N   1 
ATOM   134  C  CA  . GLN   A 1 19  ? 15.450  8.230  11.103 1.00 17.08 ? 19  GLN   A CA  1 
ATOM   135  C  C   . GLN   A 1 19  ? 16.032  9.456  10.425 1.00 16.57 ? 19  GLN   A C   1 
ATOM   136  O  O   . GLN   A 1 19  ? 15.960  9.563  9.194  1.00 16.72 ? 19  GLN   A O   1 
ATOM   137  C  CB  . GLN   A 1 19  ? 16.295  6.974  10.825 1.00 21.39 ? 19  GLN   A CB  1 
ATOM   138  C  CG  . GLN   A 1 19  ? 17.562  6.817  11.638 1.00 28.93 ? 19  GLN   A CG  1 
ATOM   139  C  CD  . GLN   A 1 19  ? 18.241  5.486  11.409 1.00 25.97 ? 19  GLN   A CD  1 
ATOM   140  O  OE1 . GLN   A 1 19  ? 17.977  4.750  10.442 1.00 31.42 ? 19  GLN   A OE1 1 
ATOM   141  N  NE2 . GLN   A 1 19  ? 19.109  5.175  12.342 1.00 31.91 ? 19  GLN   A NE2 1 
ATOM   142  N  N   . VAL   A 1 20  ? 16.539  10.402 11.220 1.00 16.83 ? 20  VAL   A N   1 
ATOM   143  C  CA  . VAL   A 1 20  ? 17.232  11.565 10.683 1.00 15.66 ? 20  VAL   A CA  1 
ATOM   144  C  C   . VAL   A 1 20  ? 18.657  11.569 11.233 1.00 16.76 ? 20  VAL   A C   1 
ATOM   145  O  O   . VAL   A 1 20  ? 18.836  11.547 12.453 1.00 14.84 ? 20  VAL   A O   1 
ATOM   146  C  CB  . VAL   A 1 20  ? 16.537  12.867 11.092 1.00 15.69 ? 20  VAL   A CB  1 
ATOM   147  C  CG1 . VAL   A 1 20  ? 17.245  14.089 10.509 1.00 16.19 ? 20  VAL   A CG1 1 
ATOM   148  C  CG2 . VAL   A 1 20  ? 15.054  12.847 10.739 1.00 16.69 ? 20  VAL   A CG2 1 
ATOM   149  N  N   . THR   A 1 21  ? 19.627  11.647 10.335 1.00 16.33 ? 21  THR   A N   1 
ATOM   150  C  CA  . THR   A 1 21  ? 21.039  11.681 10.712 1.00 18.66 ? 21  THR   A CA  1 
ATOM   151  C  C   . THR   A 1 21  ? 21.658  12.958 10.160 1.00 19.83 ? 21  THR   A C   1 
ATOM   152  O  O   . THR   A 1 21  ? 21.510  13.291 8.975  1.00 19.92 ? 21  THR   A O   1 
ATOM   153  C  CB  . THR   A 1 21  ? 21.789  10.440 10.213 1.00 17.84 ? 21  THR   A CB  1 
ATOM   154  O  OG1 . THR   A 1 21  ? 21.192  9.285  10.785 1.00 19.80 ? 21  THR   A OG1 1 
ATOM   155  C  CG2 . THR   A 1 21  ? 23.243  10.398 10.664 1.00 18.28 ? 21  THR   A CG2 1 
ATOM   156  N  N   . CYS   A 1 22  ? 22.372  13.651 11.049 1.00 20.30 ? 22  CYS   A N   1 
ATOM   157  C  CA  . CYS   A 1 22  ? 23.141  14.822 10.683 1.00 21.54 ? 22  CYS   A CA  1 
ATOM   158  C  C   . CYS   A 1 22  ? 24.515  14.645 11.312 1.00 23.95 ? 22  CYS   A C   1 
ATOM   159  O  O   . CYS   A 1 22  ? 24.639  14.527 12.539 1.00 23.28 ? 22  CYS   A O   1 
ATOM   160  C  CB  . CYS   A 1 22  ? 22.439  16.093 11.141 1.00 22.86 ? 22  CYS   A CB  1 
ATOM   161  S  SG  . CYS   A 1 22  ? 23.262  17.572 10.515 1.00 29.20 ? 22  CYS   A SG  1 
ATOM   162  N  N   . GLY   A 1 23  ? 25.545  14.515 10.469 1.00 29.30 ? 23  GLY   A N   1 
ATOM   163  C  CA  . GLY   A 1 23  ? 26.869  14.200 11.001 1.00 29.58 ? 23  GLY   A CA  1 
ATOM   164  C  C   . GLY   A 1 23  ? 26.863  12.818 11.641 1.00 27.43 ? 23  GLY   A C   1 
ATOM   165  O  O   . GLY   A 1 23  ? 26.486  11.853 10.987 1.00 29.17 ? 23  GLY   A O   1 
ATOM   166  N  N   . THR   A 1 24  ? 27.175  12.747 12.941 1.00 24.70 ? 24  THR   A N   1 
ATOM   167  C  CA  . THR   A 1 24  ? 27.200  11.476 13.654 1.00 25.42 ? 24  THR   A CA  1 
ATOM   168  C  C   . THR   A 1 24  ? 25.960  11.301 14.532 1.00 24.73 ? 24  THR   A C   1 
ATOM   169  O  O   . THR   A 1 24  ? 25.836  10.278 15.190 1.00 27.90 ? 24  THR   A O   1 
ATOM   170  C  CB  . THR   A 1 24  ? 28.501  11.416 14.462 1.00 28.52 ? 24  THR   A CB  1 
ATOM   171  O  OG1 . THR   A 1 24  ? 28.599  12.578 15.289 1.00 27.64 ? 24  THR   A OG1 1 
ATOM   172  C  CG2 . THR   A 1 24  ? 29.714  11.504 13.553 1.00 30.27 ? 24  THR   A CG2 1 
ATOM   173  N  N   . THR   A 1 25  ? 25.063  12.304 14.556 1.00 22.36 ? 25  THR   A N   1 
ATOM   174  C  CA  . THR   A 1 25  ? 23.899  12.343 15.431 1.00 19.11 ? 25  THR   A CA  1 
ATOM   175  C  C   . THR   A 1 25  ? 22.686  11.782 14.693 1.00 19.98 ? 25  THR   A C   1 
ATOM   176  O  O   . THR   A 1 25  ? 22.422  12.232 13.588 1.00 17.62 ? 25  THR   A O   1 
ATOM   177  C  CB  . THR   A 1 25  ? 23.638  13.776 15.894 1.00 19.47 ? 25  THR   A CB  1 
ATOM   178  O  OG1 . THR   A 1 25  ? 24.742  14.238 16.666 1.00 20.25 ? 25  THR   A OG1 1 
ATOM   179  C  CG2 . THR   A 1 25  ? 22.393  13.894 16.761 1.00 19.66 ? 25  THR   A CG2 1 
ATOM   180  N  N   . THR   A 1 26  ? 21.990  10.794 15.294 1.00 19.68 ? 26  THR   A N   1 
ATOM   181  C  CA  . THR   A 1 26  ? 20.801  10.201 14.697 1.00 20.72 ? 26  THR   A CA  1 
ATOM   182  C  C   . THR   A 1 26  ? 19.673  10.252 15.714 1.00 20.48 ? 26  THR   A C   1 
ATOM   183  O  O   . THR   A 1 26  ? 19.836  9.896  16.878 1.00 21.34 ? 26  THR   A O   1 
ATOM   184  C  CB  . THR   A 1 26  ? 21.014  8.756  14.248 1.00 22.64 ? 26  THR   A CB  1 
ATOM   185  O  OG1 . THR   A 1 26  ? 21.908  8.731  13.137 1.00 25.34 ? 26  THR   A OG1 1 
ATOM   186  C  CG2 . THR   A 1 26  ? 19.723  8.104  13.782 1.00 21.89 ? 26  THR   A CG2 1 
ATOM   187  N  N   . LEU   A 1 27  ? 18.508  10.727 15.274 1.00 18.17 ? 27  LEU   A N   1 
ATOM   188  C  CA  . LEU   A 1 27  ? 17.345  10.589 16.121 1.00 17.22 ? 27  LEU   A CA  1 
ATOM   189  C  C   . LEU   A 1 27  ? 16.131  10.302 15.234 1.00 14.08 ? 27  LEU   A C   1 
ATOM   190  O  O   . LEU   A 1 27  ? 16.251  10.140 14.020 1.00 13.57 ? 27  LEU   A O   1 
ATOM   191  C  CB  . LEU   A 1 27  ? 17.187  11.791 17.042 1.00 20.39 ? 27  LEU   A CB  1 
ATOM   192  C  CG  . LEU   A 1 27  ? 17.517  13.158 16.467 1.00 21.65 ? 27  LEU   A CG  1 
ATOM   193  C  CD1 . LEU   A 1 27  ? 16.514  13.447 15.363 1.00 24.15 ? 27  LEU   A CD1 1 
ATOM   194  C  CD2 . LEU   A 1 27  ? 17.467  14.198 17.575 1.00 20.18 ? 27  LEU   A CD2 1 
ATOM   195  N  N   . ASN   A 1 28  ? 14.975  10.215 15.862 1.00 11.75 ? 28  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 28  ? 13.758  9.892  15.149 1.00 12.25 ? 28  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 28  ? 13.069  11.153 14.606 1.00 12.94 ? 28  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 28  ? 13.117  12.228 15.194 1.00 13.83 ? 28  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 28  ? 12.790  9.177  16.071 1.00 12.82 ? 28  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 28  ? 13.389  7.951  16.725 1.00 13.09 ? 28  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 28  ? 13.530  6.908  16.074 1.00 14.24 ? 28  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 28  ? 13.686  8.048  18.022 1.00 13.23 ? 28  ASN   A ND2 1 
ATOM   203  N  N   . GLY   A 1 29  ? 12.411  11.001 13.449 1.00 13.85 ? 29  GLY   A N   1 
ATOM   204  C  CA  . GLY   A 1 29  ? 11.582  12.053 12.913 1.00 12.63 ? 29  GLY   A CA  1 
ATOM   205  C  C   . GLY   A 1 29  ? 10.205  11.513 12.537 1.00 13.46 ? 29  GLY   A C   1 
ATOM   206  O  O   . GLY   A 1 29  ? 10.002  10.311 12.450 1.00 13.67 ? 29  GLY   A O   1 
ATOM   207  N  N   . LEU   A 1 30  ? 9.305   12.452 12.253 1.00 12.75 ? 30  LEU   A N   1 
ATOM   208  C  CA  . LEU   A 1 30  ? 7.914   12.200 11.910 1.00 12.73 ? 30  LEU   A CA  1 
ATOM   209  C  C   . LEU   A 1 30  ? 7.671   12.774 10.521 1.00 13.15 ? 30  LEU   A C   1 
ATOM   210  O  O   . LEU   A 1 30  ? 7.764   13.992 10.322 1.00 14.15 ? 30  LEU   A O   1 
ATOM   211  C  CB  . LEU   A 1 30  ? 7.021   12.853 12.952 1.00 12.09 ? 30  LEU   A CB  1 
ATOM   212  C  CG  . LEU   A 1 30  ? 5.505   12.629 12.855 1.00 12.28 ? 30  LEU   A CG  1 
ATOM   213  C  CD1 . LEU   A 1 30  ? 5.126   11.224 13.357 1.00 12.92 ? 30  LEU   A CD1 1 
ATOM   214  C  CD2 . LEU   A 1 30  ? 4.745   13.652 13.604 1.00 12.91 ? 30  LEU   A CD2 1 
ATOM   215  N  N   . TRP   A 1 31  ? 7.330   11.877 9.594  1.00 13.06 ? 31  TRP   A N   1 
ATOM   216  C  CA  . TRP   A 1 31  ? 7.143   12.221 8.195  1.00 12.79 ? 31  TRP   A CA  1 
ATOM   217  C  C   . TRP   A 1 31  ? 5.646   12.321 7.897  1.00 12.84 ? 31  TRP   A C   1 
ATOM   218  O  O   . TRP   A 1 31  ? 4.958   11.316 7.918  1.00 14.60 ? 31  TRP   A O   1 
ATOM   219  C  CB  . TRP   A 1 31  ? 7.825   11.115 7.399  1.00 12.98 ? 31  TRP   A CB  1 
ATOM   220  C  CG  . TRP   A 1 31  ? 7.809   11.253 5.910  1.00 12.67 ? 31  TRP   A CG  1 
ATOM   221  C  CD1 . TRP   A 1 31  ? 7.655   12.375 5.158  1.00 13.12 ? 31  TRP   A CD1 1 
ATOM   222  C  CD2 . TRP   A 1 31  ? 7.956   10.165 4.992  1.00 12.96 ? 31  TRP   A CD2 1 
ATOM   223  N  NE1 . TRP   A 1 31  ? 7.760   12.072 3.822  1.00 13.00 ? 31  TRP   A NE1 1 
ATOM   224  C  CE2 . TRP   A 1 31  ? 7.893   10.718 3.691  1.00 13.47 ? 31  TRP   A CE2 1 
ATOM   225  C  CE3 . TRP   A 1 31  ? 8.060   8.780  5.145  1.00 14.07 ? 31  TRP   A CE3 1 
ATOM   226  C  CZ2 . TRP   A 1 31  ? 7.982   9.929  2.551  1.00 14.82 ? 31  TRP   A CZ2 1 
ATOM   227  C  CZ3 . TRP   A 1 31  ? 8.155   8.001  4.015  1.00 14.87 ? 31  TRP   A CZ3 1 
ATOM   228  C  CH2 . TRP   A 1 31  ? 8.084   8.569  2.745  1.00 14.64 ? 31  TRP   A CH2 1 
ATOM   229  N  N   . LEU   A 1 32  ? 5.150   13.542 7.687  1.00 13.86 ? 32  LEU   A N   1 
ATOM   230  C  CA  . LEU   A 1 32  ? 3.765   13.779 7.304  1.00 13.15 ? 32  LEU   A CA  1 
ATOM   231  C  C   . LEU   A 1 32  ? 3.758   14.569 6.000  1.00 13.60 ? 32  LEU   A C   1 
ATOM   232  O  O   . LEU   A 1 32  ? 4.464   15.568 5.913  1.00 14.22 ? 32  LEU   A O   1 
ATOM   233  C  CB  . LEU   A 1 32  ? 3.076   14.568 8.396  1.00 13.46 ? 32  LEU   A CB  1 
ATOM   234  C  CG  . LEU   A 1 32  ? 3.102   13.933 9.791  1.00 14.25 ? 32  LEU   A CG  1 
ATOM   235  C  CD1 . LEU   A 1 32  ? 2.644   14.933 10.801 1.00 13.37 ? 32  LEU   A CD1 1 
ATOM   236  C  CD2 . LEU   A 1 32  ? 2.249   12.694 9.878  1.00 16.22 ? 32  LEU   A CD2 1 
ATOM   237  N  N   . ASP   A 1 33  ? 3.052   14.027 4.994  1.00 14.60 ? 33  ASP   A N   1 
ATOM   238  C  CA  . ASP   A 1 33  ? 3.076   14.586 3.653  1.00 14.39 ? 33  ASP   A CA  1 
ATOM   239  C  C   . ASP   A 1 33  ? 4.546   14.719 3.255  1.00 14.96 ? 33  ASP   A C   1 
ATOM   240  O  O   . ASP   A 1 33  ? 5.274   13.758 3.414  1.00 12.57 ? 33  ASP   A O   1 
ATOM   241  C  CB  . ASP   A 1 33  ? 2.225   15.838 3.633  1.00 15.81 ? 33  ASP   A CB  1 
ATOM   242  C  CG  . ASP   A 1 33  ? 0.745   15.535 3.845  1.00 18.19 ? 33  ASP   A CG  1 
ATOM   243  O  OD1 . ASP   A 1 33  ? 0.303   14.396 3.449  1.00 17.82 ? 33  ASP   A OD1 1 
ATOM   244  O  OD2 . ASP   A 1 33  ? 0.066   16.399 4.451  1.00 20.04 ? 33  ASP   A OD2 1 
ATOM   245  N  N   . ASP   A 1 34  ? 4.991   15.911 2.834  1.00 14.63 ? 34  ASP   A N   1 
ATOM   246  C  CA  . ASP   A 1 34  ? 6.367   16.054 2.370  1.00 16.67 ? 34  ASP   A CA  1 
ATOM   247  C  C   . ASP   A 1 34  ? 7.237   16.793 3.383  1.00 15.67 ? 34  ASP   A C   1 
ATOM   248  O  O   . ASP   A 1 34  ? 8.236   17.412 2.996  1.00 15.17 ? 34  ASP   A O   1 
ATOM   249  C  CB  . ASP   A 1 34  ? 6.437   16.733 1.005  1.00 18.00 ? 34  ASP   A CB  1 
ATOM   250  C  CG  . ASP   A 1 34  ? 5.828   18.128 0.950  1.00 20.69 ? 34  ASP   A CG  1 
ATOM   251  O  OD1 . ASP   A 1 34  ? 5.199   18.523 1.939  1.00 19.40 ? 34  ASP   A OD1 1 
ATOM   252  O  OD2 . ASP   A 1 34  ? 6.011   18.825 -0.090 1.00 25.83 ? 34  ASP   A OD2 1 
ATOM   253  N  N   . VAL   A 1 35  ? 6.962   16.623 4.686  1.00 16.45 ? 35  VAL   A N   1 
ATOM   254  C  CA  . VAL   A 1 35  ? 7.760   17.277 5.696  1.00 15.43 ? 35  VAL   A CA  1 
ATOM   255  C  C   . VAL   A 1 35  ? 8.157   16.230 6.737  1.00 15.91 ? 35  VAL   A C   1 
ATOM   256  O  O   . VAL   A 1 35  ? 7.338   15.411 7.129  1.00 14.15 ? 35  VAL   A O   1 
ATOM   257  C  CB  . VAL   A 1 35  ? 7.062   18.483 6.359  1.00 15.10 ? 35  VAL   A CB  1 
ATOM   258  C  CG1 . VAL   A 1 35  ? 7.920   19.123 7.432  1.00 14.56 ? 35  VAL   A CG1 1 
ATOM   259  C  CG2 . VAL   A 1 35  ? 6.641   19.562 5.351  1.00 17.16 ? 35  VAL   A CG2 1 
ATOM   260  N  N   . VAL   A 1 36  ? 9.402   16.339 7.214  1.00 13.91 ? 36  VAL   A N   1 
ATOM   261  C  CA  . VAL   A 1 36  ? 9.898   15.537 8.325  1.00 14.75 ? 36  VAL   A CA  1 
ATOM   262  C  C   . VAL   A 1 36  ? 10.151  16.476 9.507  1.00 14.52 ? 36  VAL   A C   1 
ATOM   263  O  O   . VAL   A 1 36  ? 10.786  17.505 9.366  1.00 15.42 ? 36  VAL   A O   1 
ATOM   264  C  CB  . VAL   A 1 36  ? 11.144  14.699 7.981  1.00 15.01 ? 36  VAL   A CB  1 
ATOM   265  C  CG1 . VAL   A 1 36  ? 11.710  14.016 9.237  1.00 16.00 ? 36  VAL   A CG1 1 
ATOM   266  C  CG2 . VAL   A 1 36  ? 10.862  13.672 6.885  1.00 14.93 ? 36  VAL   A CG2 1 
ATOM   267  N  N   . TYR   A 1 37  ? 9.571   16.157 10.672 1.00 13.81 ? 37  TYR   A N   1 
ATOM   268  C  CA  . TYR   A 1 37  ? 9.670   17.010 11.845 1.00 13.40 ? 37  TYR   A CA  1 
ATOM   269  C  C   . TYR   A 1 37  ? 10.587  16.284 12.817 1.00 14.64 ? 37  TYR   A C   1 
ATOM   270  O  O   . TYR   A 1 37  ? 10.380  15.100 13.019 1.00 12.74 ? 37  TYR   A O   1 
ATOM   271  C  CB  . TYR   A 1 37  ? 8.336   17.264 12.552 1.00 14.70 ? 37  TYR   A CB  1 
ATOM   272  C  CG  . TYR   A 1 37  ? 7.269   17.879 11.648 1.00 15.74 ? 37  TYR   A CG  1 
ATOM   273  C  CD1 . TYR   A 1 37  ? 6.626   17.113 10.691 1.00 17.82 ? 37  TYR   A CD1 1 
ATOM   274  C  CD2 . TYR   A 1 37  ? 7.006   19.251 11.673 1.00 18.09 ? 37  TYR   A CD2 1 
ATOM   275  C  CE1 . TYR   A 1 37  ? 5.719   17.687 9.804  1.00 18.76 ? 37  TYR   A CE1 1 
ATOM   276  C  CE2 . TYR   A 1 37  ? 6.074   19.828 10.818 1.00 19.53 ? 37  TYR   A CE2 1 
ATOM   277  C  CZ  . TYR   A 1 37  ? 5.436   19.040 9.880  1.00 18.00 ? 37  TYR   A CZ  1 
ATOM   278  O  OH  . TYR   A 1 37  ? 4.549   19.568 8.983  1.00 19.83 ? 37  TYR   A OH  1 
ATOM   279  N  N   . CYS   A 1 38  ? 11.599  16.964 13.396 1.00 15.57 ? 38  CYS   A N   1 
ATOM   280  C  CA  . CYS   A 1 38  ? 12.430  16.282 14.384 1.00 15.74 ? 38  CYS   A CA  1 
ATOM   281  C  C   . CYS   A 1 38  ? 12.987  17.311 15.355 1.00 15.99 ? 38  CYS   A C   1 
ATOM   282  O  O   . CYS   A 1 38  ? 12.913  18.489 15.064 1.00 15.45 ? 38  CYS   A O   1 
ATOM   283  C  CB  . CYS   A 1 38  ? 13.549  15.458 13.745 1.00 16.59 ? 38  CYS   A CB  1 
ATOM   284  S  SG  . CYS   A 1 38  ? 14.813  16.447 12.892 1.00 18.94 ? 38  CYS   A SG  1 
ATOM   285  N  N   . PRO   A 1 39  ? 13.541  16.908 16.525 1.00 15.57 ? 39  PRO   A N   1 
ATOM   286  C  CA  . PRO   A 1 39  ? 14.176  17.846 17.441 1.00 15.21 ? 39  PRO   A CA  1 
ATOM   287  C  C   . PRO   A 1 39  ? 15.346  18.556 16.770 1.00 15.28 ? 39  PRO   A C   1 
ATOM   288  O  O   . PRO   A 1 39  ? 16.107  17.926 16.060 1.00 14.36 ? 39  PRO   A O   1 
ATOM   289  C  CB  . PRO   A 1 39  ? 14.695  16.948 18.586 1.00 15.36 ? 39  PRO   A CB  1 
ATOM   290  C  CG  . PRO   A 1 39  ? 13.752  15.754 18.540 1.00 15.91 ? 39  PRO   A CG  1 
ATOM   291  C  CD  . PRO   A 1 39  ? 13.579  15.530 17.041 1.00 16.26 ? 39  PRO   A CD  1 
ATOM   292  N  N   . ARG   A 1 40  ? 15.504  19.848 17.052 1.00 15.32 ? 40  ARG   A N   1 
ATOM   293  C  CA  . ARG   A 1 40  ? 16.511  20.625 16.345 1.00 16.47 ? 40  ARG   A CA  1 
ATOM   294  C  C   . ARG   A 1 40  ? 17.918  20.177 16.723 1.00 16.22 ? 40  ARG   A C   1 
ATOM   295  O  O   . ARG   A 1 40  ? 18.863  20.400 15.966 1.00 17.69 ? 40  ARG   A O   1 
ATOM   296  C  CB  . ARG   A 1 40  ? 16.281  22.115 16.585 1.00 16.62 ? 40  ARG   A CB  1 
ATOM   297  C  CG  . ARG   A 1 40  ? 16.469  22.587 18.007 1.00 16.34 ? 40  ARG   A CG  1 
ATOM   298  C  CD  . ARG   A 1 40  ? 16.337  24.072 18.077 1.00 16.11 ? 40  ARG   A CD  1 
ATOM   299  N  NE  . ARG   A 1 40  ? 16.248  24.525 19.466 1.00 16.37 ? 40  ARG   A NE  1 
ATOM   300  C  CZ  . ARG   A 1 40  ? 16.323  25.799 19.788 1.00 16.84 ? 40  ARG   A CZ  1 
ATOM   301  N  NH1 . ARG   A 1 40  ? 16.394  26.691 18.804 1.00 16.44 ? 40  ARG   A NH1 1 
ATOM   302  N  NH2 . ARG   A 1 40  ? 16.318  26.165 21.062 1.00 16.72 ? 40  ARG   A NH2 1 
ATOM   303  N  N   . HIS   A 1 41  ? 18.063  19.509 17.865 1.00 15.31 ? 41  HIS   A N   1 
ATOM   304  C  CA  . HIS   A 1 41  ? 19.374  19.136 18.349 1.00 15.97 ? 41  HIS   A CA  1 
ATOM   305  C  C   . HIS   A 1 41  ? 19.967  17.932 17.614 1.00 15.80 ? 41  HIS   A C   1 
ATOM   306  O  O   . HIS   A 1 41  ? 21.059  17.474 17.993 1.00 18.42 ? 41  HIS   A O   1 
ATOM   307  C  CB  . HIS   A 1 41  ? 19.416  19.099 19.878 1.00 16.16 ? 41  HIS   A CB  1 
ATOM   308  C  CG  . HIS   A 1 41  ? 18.207  18.584 20.542 1.00 17.91 ? 41  HIS   A CG  1 
ATOM   309  N  ND1 . HIS   A 1 41  ? 18.042  17.253 20.846 1.00 19.66 ? 41  HIS   A ND1 1 
ATOM   310  C  CD2 . HIS   A 1 41  ? 17.080  19.238 20.948 1.00 21.26 ? 41  HIS   A CD2 1 
ATOM   311  C  CE1 . HIS   A 1 41  ? 16.855  17.115 21.459 1.00 20.71 ? 41  HIS   A CE1 1 
ATOM   312  N  NE2 . HIS   A 1 41  ? 16.266  18.327 21.545 1.00 21.72 ? 41  HIS   A NE2 1 
ATOM   313  N  N   . VAL   A 1 42  ? 19.318  17.478 16.529 1.00 14.50 ? 42  VAL   A N   1 
ATOM   314  C  CA  . VAL   A 1 42  ? 19.954  16.565 15.584 1.00 14.94 ? 42  VAL   A CA  1 
ATOM   315  C  C   . VAL   A 1 42  ? 21.215  17.223 15.002 1.00 15.62 ? 42  VAL   A C   1 
ATOM   316  O  O   . VAL   A 1 42  ? 22.154  16.522 14.612 1.00 19.93 ? 42  VAL   A O   1 
ATOM   317  C  CB  . VAL   A 1 42  ? 18.983  16.076 14.484 1.00 14.66 ? 42  VAL   A CB  1 
ATOM   318  C  CG1 . VAL   A 1 42  ? 18.544  17.224 13.599 1.00 16.02 ? 42  VAL   A CG1 1 
ATOM   319  C  CG2 . VAL   A 1 42  ? 19.564  14.920 13.681 1.00 15.57 ? 42  VAL   A CG2 1 
ATOM   320  N  N   . ILE   A 1 43  ? 21.283  18.557 15.018 1.00 18.00 ? 43  ILE   A N   1 
ATOM   321  C  CA  . ILE   A 1 43  ? 22.427  19.257 14.444 1.00 19.83 ? 43  ILE   A CA  1 
ATOM   322  C  C   . ILE   A 1 43  ? 23.566  19.435 15.451 1.00 22.20 ? 43  ILE   A C   1 
ATOM   323  O  O   . ILE   A 1 43  ? 24.539  20.100 15.102 1.00 21.50 ? 43  ILE   A O   1 
ATOM   324  C  CB  . ILE   A 1 43  ? 22.040  20.613 13.817 1.00 19.11 ? 43  ILE   A CB  1 
ATOM   325  C  CG1 . ILE   A 1 43  ? 21.677  21.665 14.872 1.00 20.27 ? 43  ILE   A CG1 1 
ATOM   326  C  CG2 . ILE   A 1 43  ? 20.971  20.468 12.728 1.00 20.01 ? 43  ILE   A CG2 1 
ATOM   327  C  CD1 . ILE   A 1 43  ? 21.275  23.016 14.308 1.00 19.57 ? 43  ILE   A CD1 1 
ATOM   328  N  N   . CYS   A 1 44  ? 23.407  18.864 16.638 1.00 21.71 ? 44  CYS   A N   1 
ATOM   329  C  CA  . CYS   A 1 44  ? 24.433  19.013 17.694 1.00 24.26 ? 44  CYS   A CA  1 
ATOM   330  C  C   . CYS   A 1 44  ? 25.264  17.742 17.910 1.00 24.85 ? 44  CYS   A C   1 
ATOM   331  O  O   . CYS   A 1 44  ? 24.750  16.643 17.667 1.00 25.38 ? 44  CYS   A O   1 
ATOM   332  C  CB  . CYS   A 1 44  ? 23.811  19.334 19.048 1.00 23.36 ? 44  CYS   A CB  1 
ATOM   333  S  SG  . CYS   A 1 44  ? 22.940  20.913 19.124 1.00 28.21 ? 44  CYS   A SG  1 
ATOM   334  N  N   . THR   A 1 45  ? 26.519  17.926 18.310 1.00 27.46 ? 45  THR   A N   1 
ATOM   335  C  CA  . THR   A 1 45  ? 27.352  16.796 18.733 1.00 30.47 ? 45  THR   A CA  1 
ATOM   336  C  C   . THR   A 1 45  ? 27.205  16.749 20.239 1.00 31.39 ? 45  THR   A C   1 
ATOM   337  O  O   . THR   A 1 45  ? 26.661  17.702 20.800 1.00 27.70 ? 45  THR   A O   1 
ATOM   338  C  CB  . THR   A 1 45  ? 28.813  17.053 18.368 1.00 30.91 ? 45  THR   A CB  1 
ATOM   339  O  OG1 . THR   A 1 45  ? 29.162  18.218 19.104 1.00 32.29 ? 45  THR   A OG1 1 
ATOM   340  C  CG2 . THR   A 1 45  ? 29.014  17.306 16.887 1.00 35.66 ? 45  THR   A CG2 1 
ATOM   341  N  N   . SER   A 1 46  ? 27.766  15.731 20.882 1.00 36.98 ? 46  SER   A N   1 
ATOM   342  C  CA  . SER   A 1 46  ? 27.727  15.658 22.366 1.00 49.52 ? 46  SER   A CA  1 
ATOM   343  C  C   . SER   A 1 46  ? 28.757  16.616 22.968 1.00 55.97 ? 46  SER   A C   1 
ATOM   344  O  O   . SER   A 1 46  ? 29.474  16.169 23.878 1.00 70.32 ? 46  SER   A O   1 
ATOM   345  C  CB  . SER   A 1 46  ? 27.983  14.280 22.882 1.00 51.38 ? 46  SER   A CB  1 
ATOM   346  O  OG  . SER   A 1 46  ? 27.893  14.282 24.298 1.00 62.05 ? 46  SER   A OG  1 
ATOM   347  N  N   . GLU   A 1 47  ? 28.861  17.840 22.455 1.00 52.27 ? 47  GLU   A N   1 
ATOM   348  C  CA  . GLU   A 1 47  ? 29.746  18.881 23.020 1.00 49.53 ? 47  GLU   A CA  1 
ATOM   349  C  C   . GLU   A 1 47  ? 28.987  20.190 22.806 1.00 43.83 ? 47  GLU   A C   1 
ATOM   350  O  O   . GLU   A 1 47  ? 28.978  21.033 23.707 1.00 48.06 ? 47  GLU   A O   1 
ATOM   351  C  CB  . GLU   A 1 47  ? 31.104  18.918 22.324 1.00 54.24 ? 47  GLU   A CB  1 
ATOM   352  C  CG  . GLU   A 1 47  ? 31.408  17.681 21.487 1.00 65.96 ? 47  GLU   A CG  1 
ATOM   353  C  CD  . GLU   A 1 47  ? 32.242  17.973 20.255 1.00 74.48 ? 47  GLU   A CD  1 
ATOM   354  O  OE1 . GLU   A 1 47  ? 31.767  18.738 19.384 1.00 79.88 ? 47  GLU   A OE1 1 
ATOM   355  O  OE2 . GLU   A 1 47  ? 33.369  17.441 20.170 1.00 68.91 ? 47  GLU   A OE2 1 
ATOM   356  N  N   . ASP   A 1 48  ? 28.333  20.307 21.661 1.00 38.21 ? 48  ASP   A N   1 
ATOM   357  C  CA  . ASP   A 1 48  ? 27.496  21.497 21.378 1.00 38.12 ? 48  ASP   A CA  1 
ATOM   358  C  C   . ASP   A 1 48  ? 26.349  21.591 22.385 1.00 35.30 ? 48  ASP   A C   1 
ATOM   359  O  O   . ASP   A 1 48  ? 25.912  22.708 22.624 1.00 33.51 ? 48  ASP   A O   1 
ATOM   360  C  CB  . ASP   A 1 48  ? 26.938  21.428 19.967 1.00 35.93 ? 48  ASP   A CB  1 
ATOM   361  C  CG  . ASP   A 1 48  ? 27.957  21.350 18.840 1.00 41.27 ? 48  ASP   A CG  1 
ATOM   362  O  OD1 . ASP   A 1 48  ? 28.865  22.204 18.814 1.00 37.49 ? 48  ASP   A OD1 1 
ATOM   363  O  OD2 . ASP   A 1 48  ? 27.816  20.457 17.981 1.00 33.88 ? 48  ASP   A OD2 1 
ATOM   364  N  N   . MET   A 1 49  ? 25.940  20.479 22.993 1.00 39.94 ? 49  MET   A N   1 
ATOM   365  C  CA  . MET   A 1 49  ? 24.706  20.434 23.840 1.00 38.58 ? 49  MET   A CA  1 
ATOM   366  C  C   . MET   A 1 49  ? 24.807  21.142 25.208 1.00 31.17 ? 49  MET   A C   1 
ATOM   367  O  O   . MET   A 1 49  ? 23.755  21.411 25.774 1.00 26.08 ? 49  MET   A O   1 
ATOM   368  C  CB  . MET   A 1 49  ? 24.232  18.983 24.015 1.00 37.65 ? 49  MET   A CB  1 
ATOM   369  C  CG  . MET   A 1 49  ? 23.783  18.360 22.714 1.00 40.54 ? 49  MET   A CG  1 
ATOM   370  S  SD  . MET   A 1 49  ? 23.149  16.689 22.927 1.00 47.19 ? 49  MET   A SD  1 
ATOM   371  C  CE  . MET   A 1 49  ? 24.380  15.974 24.023 1.00 46.75 ? 49  MET   A CE  1 
ATOM   372  N  N   . LEU   A 1 50  ? 26.003  21.459 25.688 1.00 30.42 ? 50  LEU   A N   1 
ATOM   373  C  CA  . LEU   A 1 50  ? 26.127  22.220 26.959 1.00 32.62 ? 50  LEU   A CA  1 
ATOM   374  C  C   . LEU   A 1 50  ? 25.529  23.631 26.822 1.00 32.29 ? 50  LEU   A C   1 
ATOM   375  O  O   . LEU   A 1 50  ? 24.795  24.044 27.727 1.00 33.40 ? 50  LEU   A O   1 
ATOM   376  C  CB  . LEU   A 1 50  ? 27.596  22.250 27.380 1.00 40.97 ? 50  LEU   A CB  1 
ATOM   377  C  CG  . LEU   A 1 50  ? 28.177  20.884 27.759 1.00 45.04 ? 50  LEU   A CG  1 
ATOM   378  C  CD1 . LEU   A 1 50  ? 29.692  20.905 27.886 1.00 48.58 ? 50  LEU   A CD1 1 
ATOM   379  C  CD2 . LEU   A 1 50  ? 27.530  20.364 29.032 1.00 43.58 ? 50  LEU   A CD2 1 
ATOM   380  N  N   . ASN   A 1 51  ? 25.846  24.342 25.741 1.00 32.62 ? 51  ASN   A N   1 
ATOM   381  C  CA  . ASN   A 1 51  ? 25.214  25.664 25.488 1.00 34.59 ? 51  ASN   A CA  1 
ATOM   382  C  C   . ASN   A 1 51  ? 25.187  25.906 23.979 1.00 31.19 ? 51  ASN   A C   1 
ATOM   383  O  O   . ASN   A 1 51  ? 25.993  26.695 23.466 1.00 29.10 ? 51  ASN   A O   1 
ATOM   384  C  CB  . ASN   A 1 51  ? 25.874  26.837 26.195 1.00 39.67 ? 51  ASN   A CB  1 
ATOM   385  C  CG  . ASN   A 1 51  ? 24.931  28.014 26.260 1.00 45.06 ? 51  ASN   A CG  1 
ATOM   386  O  OD1 . ASN   A 1 51  ? 23.748  27.876 25.929 1.00 50.27 ? 51  ASN   A OD1 1 
ATOM   387  N  ND2 . ASN   A 1 51  ? 25.416  29.163 26.702 1.00 51.96 ? 51  ASN   A ND2 1 
ATOM   388  N  N   . PRO   A 1 52  ? 24.294  25.220 23.255 1.00 25.84 ? 52  PRO   A N   1 
ATOM   389  C  CA  . PRO   A 1 52  ? 24.271  25.380 21.817 1.00 24.29 ? 52  PRO   A CA  1 
ATOM   390  C  C   . PRO   A 1 52  ? 23.644  26.636 21.272 1.00 21.22 ? 52  PRO   A C   1 
ATOM   391  O  O   . PRO   A 1 52  ? 22.687  27.138 21.865 1.00 22.43 ? 52  PRO   A O   1 
ATOM   392  C  CB  . PRO   A 1 52  ? 23.464  24.156 21.393 1.00 25.60 ? 52  PRO   A CB  1 
ATOM   393  C  CG  . PRO   A 1 52  ? 22.526  23.907 22.551 1.00 27.93 ? 52  PRO   A CG  1 
ATOM   394  C  CD  . PRO   A 1 52  ? 23.301  24.309 23.787 1.00 26.53 ? 52  PRO   A CD  1 
ATOM   395  N  N   . ASN   A 1 53  ? 24.231  27.166 20.210 1.00 19.60 ? 53  ASN   A N   1 
ATOM   396  C  CA  . ASN   A 1 53  ? 23.605  28.215 19.441 1.00 19.71 ? 53  ASN   A CA  1 
ATOM   397  C  C   . ASN   A 1 53  ? 23.034  27.557 18.193 1.00 18.22 ? 53  ASN   A C   1 
ATOM   398  O  O   . ASN   A 1 53  ? 23.744  27.346 17.205 1.00 19.92 ? 53  ASN   A O   1 
ATOM   399  C  CB  . ASN   A 1 53  ? 24.592  29.355 19.148 1.00 21.37 ? 53  ASN   A CB  1 
ATOM   400  C  CG  . ASN   A 1 53  ? 23.937  30.503 18.423 1.00 21.79 ? 53  ASN   A CG  1 
ATOM   401  O  OD1 . ASN   A 1 53  ? 22.921  30.332 17.726 1.00 21.97 ? 53  ASN   A OD1 1 
ATOM   402  N  ND2 . ASN   A 1 53  ? 24.482  31.704 18.570 1.00 22.50 ? 53  ASN   A ND2 1 
ATOM   403  N  N   . TYR   A 1 54  ? 21.744  27.229 18.235 1.00 17.95 ? 54  TYR   A N   1 
ATOM   404  C  CA  . TYR   A 1 54  ? 21.137  26.457 17.167 1.00 18.45 ? 54  TYR   A CA  1 
ATOM   405  C  C   . TYR   A 1 54  ? 21.129  27.219 15.850 1.00 19.00 ? 54  TYR   A C   1 
ATOM   406  O  O   . TYR   A 1 54  ? 21.307  26.650 14.785 1.00 20.34 ? 54  TYR   A O   1 
ATOM   407  C  CB  . TYR   A 1 54  ? 19.719  26.124 17.630 1.00 17.78 ? 54  TYR   A CB  1 
ATOM   408  C  CG  . TYR   A 1 54  ? 19.747  25.021 18.676 1.00 16.51 ? 54  TYR   A CG  1 
ATOM   409  C  CD1 . TYR   A 1 54  ? 20.095  23.731 18.327 1.00 18.94 ? 54  TYR   A CD1 1 
ATOM   410  C  CD2 . TYR   A 1 54  ? 19.491  25.291 20.013 1.00 18.28 ? 54  TYR   A CD2 1 
ATOM   411  C  CE1 . TYR   A 1 54  ? 20.136  22.717 19.269 1.00 18.48 ? 54  TYR   A CE1 1 
ATOM   412  C  CE2 . TYR   A 1 54  ? 19.497  24.282 20.966 1.00 18.64 ? 54  TYR   A CE2 1 
ATOM   413  C  CZ  . TYR   A 1 54  ? 19.799  22.986 20.585 1.00 18.99 ? 54  TYR   A CZ  1 
ATOM   414  O  OH  . TYR   A 1 54  ? 19.850  21.973 21.521 1.00 19.02 ? 54  TYR   A OH  1 
ATOM   415  N  N   . GLU   A 1 55  ? 20.830  28.506 15.925 1.00 20.59 ? 55  GLU   A N   1 
ATOM   416  C  CA  . GLU   A 1 55  ? 20.768  29.318 14.727 1.00 21.72 ? 55  GLU   A CA  1 
ATOM   417  C  C   . GLU   A 1 55  ? 22.117  29.307 14.018 1.00 22.26 ? 55  GLU   A C   1 
ATOM   418  O  O   . GLU   A 1 55  ? 22.178  29.222 12.780 1.00 22.20 ? 55  GLU   A O   1 
ATOM   419  C  CB  . GLU   A 1 55  ? 20.354  30.736 15.089 1.00 23.90 ? 55  GLU   A CB  1 
ATOM   420  C  CG  . GLU   A 1 55  ? 18.904  30.831 15.543 1.00 25.26 ? 55  GLU   A CG  1 
ATOM   421  C  CD  . GLU   A 1 55  ? 18.647  30.585 17.015 1.00 23.71 ? 55  GLU   A CD  1 
ATOM   422  O  OE1 . GLU   A 1 55  ? 19.526  30.168 17.792 1.00 23.10 ? 55  GLU   A OE1 1 
ATOM   423  O  OE2 . GLU   A 1 55  ? 17.492  30.878 17.379 1.00 26.23 ? 55  GLU   A OE2 1 
ATOM   424  N  N   . ASP   A 1 56  ? 23.178  29.462 14.815 1.00 20.53 ? 56  ASP   A N   1 
ATOM   425  C  CA  . ASP   A 1 56  ? 24.533  29.398 14.309 1.00 21.78 ? 56  ASP   A CA  1 
ATOM   426  C  C   . ASP   A 1 56  ? 24.879  28.031 13.724 1.00 22.79 ? 56  ASP   A C   1 
ATOM   427  O  O   . ASP   A 1 56  ? 25.471  27.964 12.648 1.00 22.63 ? 56  ASP   A O   1 
ATOM   428  C  CB  . ASP   A 1 56  ? 25.571  29.787 15.348 1.00 21.56 ? 56  ASP   A CB  1 
ATOM   429  C  CG  . ASP   A 1 56  ? 26.976  29.816 14.772 1.00 24.61 ? 56  ASP   A CG  1 
ATOM   430  O  OD1 . ASP   A 1 56  ? 27.149  30.480 13.731 1.00 24.13 ? 56  ASP   A OD1 1 
ATOM   431  O  OD2 . ASP   A 1 56  ? 27.860  29.139 15.318 1.00 26.88 ? 56  ASP   A OD2 1 
ATOM   432  N  N   . LEU   A 1 57  ? 24.554  26.932 14.430 1.00 21.31 ? 57  LEU   A N   1 
ATOM   433  C  CA  . LEU   A 1 57  ? 24.851  25.601 13.911 1.00 20.19 ? 57  LEU   A CA  1 
ATOM   434  C  C   . LEU   A 1 57  ? 24.120  25.324 12.595 1.00 19.61 ? 57  LEU   A C   1 
ATOM   435  O  O   . LEU   A 1 57  ? 24.665  24.672 11.709 1.00 23.45 ? 57  LEU   A O   1 
ATOM   436  C  CB  . LEU   A 1 57  ? 24.498  24.574 14.985 1.00 21.77 ? 57  LEU   A CB  1 
ATOM   437  C  CG  . LEU   A 1 57  ? 25.381  24.575 16.240 1.00 23.62 ? 57  LEU   A CG  1 
ATOM   438  C  CD1 . LEU   A 1 57  ? 24.828  23.624 17.268 1.00 23.06 ? 57  LEU   A CD1 1 
ATOM   439  C  CD2 . LEU   A 1 57  ? 26.834  24.223 15.963 1.00 25.46 ? 57  LEU   A CD2 1 
ATOM   440  N  N   . LEU   A 1 58  ? 22.887  25.809 12.471 1.00 19.48 ? 58  LEU   A N   1 
ATOM   441  C  CA  . LEU   A 1 58  ? 22.032  25.490 11.341 1.00 21.30 ? 58  LEU   A CA  1 
ATOM   442  C  C   . LEU   A 1 58  ? 22.474  26.218 10.082 1.00 22.44 ? 58  LEU   A C   1 
ATOM   443  O  O   . LEU   A 1 58  ? 22.365  25.674 8.985  1.00 19.83 ? 58  LEU   A O   1 
ATOM   444  C  CB  . LEU   A 1 58  ? 20.588  25.832 11.673 1.00 21.05 ? 58  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A 1 58  ? 19.575  25.410 10.619 1.00 22.18 ? 58  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A 1 58  ? 19.641  23.913 10.412 1.00 20.84 ? 58  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A 1 58  ? 18.216  25.909 11.039 1.00 24.84 ? 58  LEU   A CD2 1 
ATOM   448  N  N   . ILE   A 1 59  ? 22.968  27.456 10.234 1.00 24.79 ? 59  ILE   A N   1 
ATOM   449  C  CA  . ILE   A 1 59  ? 23.325  28.215 9.049  1.00 26.57 ? 59  ILE   A CA  1 
ATOM   450  C  C   . ILE   A 1 59  ? 24.495  27.523 8.355  1.00 25.10 ? 59  ILE   A C   1 
ATOM   451  O  O   . ILE   A 1 59  ? 24.655  27.642 7.138  1.00 24.43 ? 59  ILE   A O   1 
ATOM   452  C  CB  . ILE   A 1 59  ? 23.619  29.691 9.377  1.00 31.46 ? 59  ILE   A CB  1 
ATOM   453  C  CG1 . ILE   A 1 59  ? 23.519  30.577 8.126  1.00 37.51 ? 59  ILE   A CG1 1 
ATOM   454  C  CG2 . ILE   A 1 59  ? 24.987  29.844 10.011 1.00 32.74 ? 59  ILE   A CG2 1 
ATOM   455  C  CD1 . ILE   A 1 59  ? 22.232  30.469 7.315  1.00 36.89 ? 59  ILE   A CD1 1 
ATOM   456  N  N   . ARG   A 1 60  ? 25.284  26.756 9.108  1.00 23.29 ? 60  ARG   A N   1 
ATOM   457  C  CA  . ARG   A 1 60  ? 26.397  26.042 8.508  1.00 28.97 ? 60  ARG   A CA  1 
ATOM   458  C  C   . ARG   A 1 60  ? 25.977  24.707 7.906  1.00 28.28 ? 60  ARG   A C   1 
ATOM   459  O  O   . ARG   A 1 60  ? 26.813  24.015 7.346  1.00 29.47 ? 60  ARG   A O   1 
ATOM   460  C  CB  . ARG   A 1 60  ? 27.528  25.839 9.516  1.00 35.93 ? 60  ARG   A CB  1 
ATOM   461  C  CG  . ARG   A 1 60  ? 28.490  27.022 9.530  1.00 45.27 ? 60  ARG   A CG  1 
ATOM   462  C  CD  . ARG   A 1 60  ? 29.782  26.663 10.272 1.00 48.03 ? 60  ARG   A CD  1 
ATOM   463  N  NE  . ARG   A 1 60  ? 29.509  26.357 11.679 1.00 46.53 ? 60  ARG   A NE  1 
ATOM   464  C  CZ  . ARG   A 1 60  ? 29.092  27.268 12.543 1.00 44.07 ? 60  ARG   A CZ  1 
ATOM   465  N  NH1 . ARG   A 1 60  ? 29.033  26.974 13.827 1.00 43.84 ? 60  ARG   A NH1 1 
ATOM   466  N  NH2 . ARG   A 1 60  ? 28.805  28.490 12.125 1.00 41.17 ? 60  ARG   A NH2 1 
ATOM   467  N  N   . LYS   A 1 61  ? 24.701  24.323 8.022  1.00 26.31 ? 61  LYS   A N   1 
ATOM   468  C  CA  . LYS   A 1 61  ? 24.221  23.126 7.359  1.00 24.55 ? 61  LYS   A CA  1 
ATOM   469  C  C   . LYS   A 1 61  ? 23.483  23.483 6.070  1.00 23.27 ? 61  LYS   A C   1 
ATOM   470  O  O   . LYS   A 1 61  ? 22.890  24.551 5.950  1.00 24.98 ? 61  LYS   A O   1 
ATOM   471  C  CB  . LYS   A 1 61  ? 23.208  22.392 8.254  1.00 26.98 ? 61  LYS   A CB  1 
ATOM   472  C  CG  . LYS   A 1 61  ? 23.697  22.016 9.649  1.00 28.57 ? 61  LYS   A CG  1 
ATOM   473  C  CD  . LYS   A 1 61  ? 24.844  21.025 9.609  1.00 28.70 ? 61  LYS   A CD  1 
ATOM   474  C  CE  . LYS   A 1 61  ? 25.321  20.696 10.974 1.00 30.01 ? 61  LYS   A CE  1 
ATOM   475  N  NZ  . LYS   A 1 61  ? 26.222  19.546 10.886 1.00 29.21 ? 61  LYS   A NZ  1 
ATOM   476  N  N   . SER   A 1 62  ? 23.452  22.530 5.145  1.00 21.70 ? 62  SER   A N   1 
ATOM   477  C  CA  . SER   A 1 62  ? 22.621  22.592 3.952  1.00 22.62 ? 62  SER   A CA  1 
ATOM   478  C  C   . SER   A 1 62  ? 21.784  21.313 3.852  1.00 20.61 ? 62  SER   A C   1 
ATOM   479  O  O   . SER   A 1 62  ? 21.985  20.347 4.597  1.00 19.62 ? 62  SER   A O   1 
ATOM   480  C  CB  . SER   A 1 62  ? 23.480  22.809 2.708  1.00 24.22 ? 62  SER   A CB  1 
ATOM   481  O  OG  . SER   A 1 62  ? 24.297  21.676 2.457  1.00 23.44 ? 62  SER   A OG  1 
ATOM   482  N  N   . ASN   A 1 63  ? 20.807  21.326 2.947  1.00 21.14 ? 63  ASN   A N   1 
ATOM   483  C  CA  . ASN   A 1 63  ? 19.862  20.221 2.795  1.00 20.08 ? 63  ASN   A CA  1 
ATOM   484  C  C   . ASN   A 1 63  ? 20.526  18.844 2.800  1.00 20.10 ? 63  ASN   A C   1 
ATOM   485  O  O   . ASN   A 1 63  ? 20.049  17.949 3.487  1.00 20.63 ? 63  ASN   A O   1 
ATOM   486  C  CB  . ASN   A 1 63  ? 19.067  20.377 1.505  1.00 18.64 ? 63  ASN   A CB  1 
ATOM   487  C  CG  . ASN   A 1 63  ? 18.157  21.581 1.500  1.00 20.26 ? 63  ASN   A CG  1 
ATOM   488  O  OD1 . ASN   A 1 63  ? 17.706  22.085 2.545  1.00 19.56 ? 63  ASN   A OD1 1 
ATOM   489  N  ND2 . ASN   A 1 63  ? 17.852  22.049 0.298  1.00 20.59 ? 63  ASN   A ND2 1 
ATOM   490  N  N   . HIS   A 1 64  ? 21.610  18.648 2.012  1.00 17.66 ? 64  HIS   A N   1 
ATOM   491  C  CA  . HIS   A 1 64  ? 22.199  17.337 1.774  1.00 18.53 ? 64  HIS   A CA  1 
ATOM   492  C  C   . HIS   A 1 64  ? 22.833  16.757 3.042  1.00 17.94 ? 64  HIS   A C   1 
ATOM   493  O  O   . HIS   A 1 64  ? 23.083  15.557 3.122  1.00 18.87 ? 64  HIS   A O   1 
ATOM   494  C  CB  . HIS   A 1 64  ? 23.206  17.398 0.596  1.00 18.28 ? 64  HIS   A CB  1 
ATOM   495  C  CG  . HIS   A 1 64  ? 23.680  16.059 0.148  1.00 17.41 ? 64  HIS   A CG  1 
ATOM   496  N  ND1 . HIS   A 1 64  ? 24.878  15.542 0.592  1.00 19.37 ? 64  HIS   A ND1 1 
ATOM   497  C  CD2 . HIS   A 1 64  ? 23.138  15.112 -0.658 1.00 18.35 ? 64  HIS   A CD2 1 
ATOM   498  C  CE1 . HIS   A 1 64  ? 25.058  14.333 0.042  1.00 18.61 ? 64  HIS   A CE1 1 
ATOM   499  N  NE2 . HIS   A 1 64  ? 24.019  14.054 -0.714 1.00 18.10 ? 64  HIS   A NE2 1 
ATOM   500  N  N   . ASN   A 1 65  ? 23.119  17.608 4.013  1.00 18.34 ? 65  ASN   A N   1 
ATOM   501  C  CA  . ASN   A 1 65  ? 23.700  17.163 5.268  1.00 18.14 ? 65  ASN   A CA  1 
ATOM   502  C  C   . ASN   A 1 65  ? 22.696  16.370 6.114  1.00 19.51 ? 65  ASN   A C   1 
ATOM   503  O  O   . ASN   A 1 65  ? 23.066  15.827 7.159  1.00 18.70 ? 65  ASN   A O   1 
ATOM   504  C  CB  . ASN   A 1 65  ? 24.157  18.359 6.090  1.00 19.22 ? 65  ASN   A CB  1 
ATOM   505  C  CG  . ASN   A 1 65  ? 25.233  19.188 5.414  1.00 20.78 ? 65  ASN   A CG  1 
ATOM   506  O  OD1 . ASN   A 1 65  ? 25.901  18.726 4.479  1.00 24.41 ? 65  ASN   A OD1 1 
ATOM   507  N  ND2 . ASN   A 1 65  ? 25.370  20.430 5.836  1.00 18.93 ? 65  ASN   A ND2 1 
ATOM   508  N  N   . PHE   A 1 66  ? 21.408  16.439 5.769  1.00 17.15 ? 66  PHE   A N   1 
ATOM   509  C  CA  . PHE   A 1 66  ? 20.416  15.712 6.546  1.00 17.10 ? 66  PHE   A CA  1 
ATOM   510  C  C   . PHE   A 1 66  ? 20.114  14.428 5.815  1.00 18.39 ? 66  PHE   A C   1 
ATOM   511  O  O   . PHE   A 1 66  ? 19.564  14.469 4.717  1.00 17.56 ? 66  PHE   A O   1 
ATOM   512  C  CB  . PHE   A 1 66  ? 19.096  16.456 6.713  1.00 16.59 ? 66  PHE   A CB  1 
ATOM   513  C  CG  . PHE   A 1 66  ? 19.330  17.718 7.511  1.00 16.67 ? 66  PHE   A CG  1 
ATOM   514  C  CD1 . PHE   A 1 66  ? 19.362  17.669 8.890  1.00 17.90 ? 66  PHE   A CD1 1 
ATOM   515  C  CD2 . PHE   A 1 66  ? 19.599  18.915 6.875  1.00 18.00 ? 66  PHE   A CD2 1 
ATOM   516  C  CE1 . PHE   A 1 66  ? 19.588  18.825 9.635  1.00 18.34 ? 66  PHE   A CE1 1 
ATOM   517  C  CE2 . PHE   A 1 66  ? 19.831  20.068 7.612  1.00 19.23 ? 66  PHE   A CE2 1 
ATOM   518  C  CZ  . PHE   A 1 66  ? 19.867  20.008 8.996  1.00 20.58 ? 66  PHE   A CZ  1 
ATOM   519  N  N   . LEU   A 1 67  ? 20.488  13.316 6.425  1.00 18.74 ? 67  LEU   A N   1 
ATOM   520  C  CA  . LEU   A 1 67  ? 20.209  12.008 5.854  1.00 19.27 ? 67  LEU   A CA  1 
ATOM   521  C  C   . LEU   A 1 67  ? 18.924  11.469 6.477  1.00 18.81 ? 67  LEU   A C   1 
ATOM   522  O  O   . LEU   A 1 67  ? 18.909  11.161 7.666  1.00 21.14 ? 67  LEU   A O   1 
ATOM   523  C  CB  . LEU   A 1 67  ? 21.398  11.089 6.125  1.00 20.52 ? 67  LEU   A CB  1 
ATOM   524  C  CG  . LEU   A 1 67  ? 21.176  9.598  5.825  1.00 23.32 ? 67  LEU   A CG  1 
ATOM   525  C  CD1 . LEU   A 1 67  ? 20.770  9.388  4.393  1.00 26.23 ? 67  LEU   A CD1 1 
ATOM   526  C  CD2 . LEU   A 1 67  ? 22.390  8.698  6.178  1.00 25.16 ? 67  LEU   A CD2 1 
ATOM   527  N  N   . VAL   A 1 68  ? 17.842  11.441 5.710  1.00 18.50 ? 68  VAL   A N   1 
ATOM   528  C  CA  . VAL   A 1 68  ? 16.544  10.969 6.194  1.00 18.16 ? 68  VAL   A CA  1 
ATOM   529  C  C   . VAL   A 1 68  ? 16.267  9.586  5.620  1.00 18.09 ? 68  VAL   A C   1 
ATOM   530  O  O   . VAL   A 1 68  ? 16.323  9.412  4.394  1.00 18.01 ? 68  VAL   A O   1 
ATOM   531  C  CB  . VAL   A 1 68  ? 15.413  11.936 5.807  1.00 18.62 ? 68  VAL   A CB  1 
ATOM   532  C  CG1 . VAL   A 1 68  ? 14.070  11.420 6.314  1.00 19.65 ? 68  VAL   A CG1 1 
ATOM   533  C  CG2 . VAL   A 1 68  ? 15.696  13.354 6.301  1.00 18.53 ? 68  VAL   A CG2 1 
ATOM   534  N  N   . GLN   A 1 69  ? 16.011  8.590  6.496  1.00 17.69 ? 69  GLN   A N   1 
ATOM   535  C  CA  . GLN   A 1 69  ? 15.724  7.247  5.997  1.00 19.58 ? 69  GLN   A CA  1 
ATOM   536  C  C   . GLN   A 1 69  ? 14.389  6.722  6.504  1.00 19.01 ? 69  GLN   A C   1 
ATOM   537  O  O   . GLN   A 1 69  ? 14.123  6.756  7.694  1.00 17.61 ? 69  GLN   A O   1 
ATOM   538  C  CB  . GLN   A 1 69  ? 16.811  6.239  6.347  1.00 23.43 ? 69  GLN   A CB  1 
ATOM   539  C  CG  . GLN   A 1 69  ? 18.158  6.690  5.804  1.00 28.90 ? 69  GLN   A CG  1 
ATOM   540  C  CD  . GLN   A 1 69  ? 19.322  6.005  6.472  1.00 36.04 ? 69  GLN   A CD  1 
ATOM   541  O  OE1 . GLN   A 1 69  ? 19.729  6.339  7.601  1.00 33.18 ? 69  GLN   A OE1 1 
ATOM   542  N  NE2 . GLN   A 1 69  ? 19.863  5.045  5.738  1.00 42.25 ? 69  GLN   A NE2 1 
ATOM   543  N  N   . ALA   A 1 70  ? 13.560  6.267  5.558  1.00 18.76 ? 70  ALA   A N   1 
ATOM   544  C  CA  . ALA   A 1 70  ? 12.290  5.633  5.871  1.00 19.26 ? 70  ALA   A CA  1 
ATOM   545  C  C   . ALA   A 1 70  ? 12.422  4.149  5.544  1.00 23.90 ? 70  ALA   A C   1 
ATOM   546  O  O   . ALA   A 1 70  ? 12.436  3.772  4.378  1.00 22.92 ? 70  ALA   A O   1 
ATOM   547  C  CB  . ALA   A 1 70  ? 11.198  6.273  5.079  1.00 19.63 ? 70  ALA   A CB  1 
ATOM   548  N  N   . GLY   A 1 71  ? 12.626  3.328  6.586  1.00 24.69 ? 71  GLY   A N   1 
ATOM   549  C  CA  . GLY   A 1 71  ? 13.071  1.969  6.367  1.00 30.81 ? 71  GLY   A CA  1 
ATOM   550  C  C   . GLY   A 1 71  ? 14.428  1.977  5.676  1.00 35.24 ? 71  GLY   A C   1 
ATOM   551  O  O   . GLY   A 1 71  ? 15.354  2.660  6.117  1.00 31.50 ? 71  GLY   A O   1 
ATOM   552  N  N   . ASN   A 1 72  ? 14.529  1.208  4.590  1.00 42.14 ? 72  ASN   A N   1 
ATOM   553  C  CA  . ASN   A 1 72  ? 15.714  1.249  3.745  1.00 54.09 ? 72  ASN   A CA  1 
ATOM   554  C  C   . ASN   A 1 72  ? 15.893  2.658  3.187  1.00 50.47 ? 72  ASN   A C   1 
ATOM   555  O  O   . ASN   A 1 72  ? 16.921  3.289  3.434  1.00 58.71 ? 72  ASN   A O   1 
ATOM   556  C  CB  . ASN   A 1 72  ? 15.627  0.239  2.604  1.00 59.72 ? 72  ASN   A CB  1 
ATOM   557  C  CG  . ASN   A 1 72  ? 15.783  -1.184 3.091  1.00 68.04 ? 72  ASN   A CG  1 
ATOM   558  O  OD1 . ASN   A 1 72  ? 15.855  -1.431 4.302  1.00 75.21 ? 72  ASN   A OD1 1 
ATOM   559  N  ND2 . ASN   A 1 72  ? 15.841  -2.135 2.170  1.00 70.46 ? 72  ASN   A ND2 1 
ATOM   560  N  N   . VAL   A 1 73  ? 14.817  3.146  2.555  1.00 38.30 ? 73  VAL   A N   1 
ATOM   561  C  CA  . VAL   A 1 73  ? 14.851  4.161  1.513  1.00 34.27 ? 73  VAL   A CA  1 
ATOM   562  C  C   . VAL   A 1 73  ? 15.280  5.515  2.058  1.00 29.96 ? 73  VAL   A C   1 
ATOM   563  O  O   . VAL   A 1 73  ? 14.712  6.003  3.028  1.00 24.62 ? 73  VAL   A O   1 
ATOM   564  C  CB  . VAL   A 1 73  ? 13.433  4.265  0.937  1.00 34.65 ? 73  VAL   A CB  1 
ATOM   565  C  CG1 . VAL   A 1 73  ? 13.373  5.194  -0.264 1.00 35.04 ? 73  VAL   A CG1 1 
ATOM   566  C  CG2 . VAL   A 1 73  ? 12.872  2.883  0.621  1.00 37.88 ? 73  VAL   A CG2 1 
ATOM   567  N  N   . GLN   A 1 74  ? 16.177  6.183  1.331  1.00 25.66 ? 74  GLN   A N   1 
ATOM   568  C  CA  . GLN   A 1 74  ? 16.575  7.535  1.677  1.00 25.24 ? 74  GLN   A CA  1 
ATOM   569  C  C   . GLN   A 1 74  ? 15.622  8.529  1.009  1.00 24.88 ? 74  GLN   A C   1 
ATOM   570  O  O   . GLN   A 1 74  ? 15.349  8.463  -0.188 1.00 27.11 ? 74  GLN   A O   1 
ATOM   571  C  CB  . GLN   A 1 74  ? 18.039  7.793  1.317  1.00 27.44 ? 74  GLN   A CB  1 
ATOM   572  C  CG  . GLN   A 1 74  ? 18.452  9.253  1.492  1.00 30.68 ? 74  GLN   A CG  1 
ATOM   573  C  CD  . GLN   A 1 74  ? 19.888  9.539  1.107  1.00 37.33 ? 74  GLN   A CD  1 
ATOM   574  O  OE1 . GLN   A 1 74  ? 20.592  8.669  0.578  1.00 37.78 ? 74  GLN   A OE1 1 
ATOM   575  N  NE2 . GLN   A 1 74  ? 20.344  10.757 1.385  1.00 36.61 ? 74  GLN   A NE2 1 
ATOM   576  N  N   . LEU   A 1 75  ? 15.105  9.464  1.794  1.00 22.62 ? 75  LEU   A N   1 
ATOM   577  C  CA  . LEU   A 1 75  ? 14.311  10.569 1.274  1.00 21.62 ? 75  LEU   A CA  1 
ATOM   578  C  C   . LEU   A 1 75  ? 15.235  11.761 1.043  1.00 22.64 ? 75  LEU   A C   1 
ATOM   579  O  O   . LEU   A 1 75  ? 15.940  12.176 1.958  1.00 26.89 ? 75  LEU   A O   1 
ATOM   580  C  CB  . LEU   A 1 75  ? 13.263  10.905 2.336  1.00 20.69 ? 75  LEU   A CB  1 
ATOM   581  C  CG  . LEU   A 1 75  ? 12.378  9.746  2.791  1.00 22.45 ? 75  LEU   A CG  1 
ATOM   582  C  CD1 . LEU   A 1 75  ? 11.302  10.260 3.734  1.00 21.29 ? 75  LEU   A CD1 1 
ATOM   583  C  CD2 . LEU   A 1 75  ? 11.775  8.991  1.606  1.00 24.43 ? 75  LEU   A CD2 1 
ATOM   584  N  N   . ARG   A 1 76  ? 15.165  12.367 -0.139 1.00 19.64 ? 76  ARG   A N   1 
ATOM   585  C  CA  . ARG   A 1 76  ? 16.019  13.486 -0.498 1.00 19.98 ? 76  ARG   A CA  1 
ATOM   586  C  C   . ARG   A 1 76  ? 15.460  14.776 0.108  1.00 16.78 ? 76  ARG   A C   1 
ATOM   587  O  O   . ARG   A 1 76  ? 14.297  15.135 -0.052 1.00 17.74 ? 76  ARG   A O   1 
ATOM   588  C  CB  . ARG   A 1 76  ? 16.204  13.571 -2.035 1.00 22.42 ? 76  ARG   A CB  1 
ATOM   589  C  CG  . ARG   A 1 76  ? 16.923  14.870 -2.394 1.00 25.49 ? 76  ARG   A CG  1 
ATOM   590  C  CD  . ARG   A 1 76  ? 17.043  15.310 -3.857 1.00 31.58 ? 76  ARG   A CD  1 
ATOM   591  N  NE  . ARG   A 1 76  ? 18.297  14.835 -4.437 1.00 35.05 ? 76  ARG   A NE  1 
ATOM   592  C  CZ  . ARG   A 1 76  ? 19.519  15.304 -4.213 1.00 35.04 ? 76  ARG   A CZ  1 
ATOM   593  N  NH1 . ARG   A 1 76  ? 19.868  16.565 -4.411 1.00 39.86 ? 76  ARG   A NH1 1 
ATOM   594  N  NH2 . ARG   A 1 76  ? 20.439  14.420 -3.963 1.00 36.02 ? 76  ARG   A NH2 1 
ATOM   595  N  N   . VAL   A 1 77  ? 16.286  15.481 0.865  1.00 17.45 ? 77  VAL   A N   1 
ATOM   596  C  CA  . VAL   A 1 77  ? 15.866  16.729 1.494  1.00 16.93 ? 77  VAL   A CA  1 
ATOM   597  C  C   . VAL   A 1 77  ? 16.034  17.894 0.521  1.00 16.03 ? 77  VAL   A C   1 
ATOM   598  O  O   . VAL   A 1 77  ? 17.109  18.087 -0.049 1.00 16.30 ? 77  VAL   A O   1 
ATOM   599  C  CB  . VAL   A 1 77  ? 16.670  16.949 2.782  1.00 15.40 ? 77  VAL   A CB  1 
ATOM   600  C  CG1 . VAL   A 1 77  ? 16.418  18.306 3.401  1.00 17.71 ? 77  VAL   A CG1 1 
ATOM   601  C  CG2 . VAL   A 1 77  ? 16.384  15.872 3.797  1.00 16.02 ? 77  VAL   A CG2 1 
ATOM   602  N  N   . ILE   A 1 78  ? 14.981  18.694 0.368  1.00 17.12 ? 78  ILE   A N   1 
ATOM   603  C  CA  . ILE   A 1 78  ? 14.981  19.782 -0.597 1.00 19.33 ? 78  ILE   A CA  1 
ATOM   604  C  C   . ILE   A 1 78  ? 14.728  21.132 0.074  1.00 18.76 ? 78  ILE   A C   1 
ATOM   605  O  O   . ILE   A 1 78  ? 14.626  22.132 -0.602 1.00 20.37 ? 78  ILE   A O   1 
ATOM   606  C  CB  . ILE   A 1 78  ? 13.978  19.502 -1.737 1.00 18.70 ? 78  ILE   A CB  1 
ATOM   607  C  CG1 . ILE   A 1 78  ? 12.530  19.523 -1.258 1.00 19.71 ? 78  ILE   A CG1 1 
ATOM   608  C  CG2 . ILE   A 1 78  ? 14.338  18.201 -2.438 1.00 20.57 ? 78  ILE   A CG2 1 
ATOM   609  C  CD1 . ILE   A 1 78  ? 11.494  19.375 -2.359 1.00 19.88 ? 78  ILE   A CD1 1 
ATOM   610  N  N   . GLY   A 1 79  ? 14.642  21.193 1.401  1.00 15.90 ? 79  GLY   A N   1 
ATOM   611  C  CA  . GLY   A 1 79  ? 14.551  22.441 2.129  1.00 15.61 ? 79  GLY   A CA  1 
ATOM   612  C  C   . GLY   A 1 79  ? 14.584  22.128 3.621  1.00 17.93 ? 79  GLY   A C   1 
ATOM   613  O  O   . GLY   A 1 79  ? 14.343  20.981 3.997  1.00 18.45 ? 79  GLY   A O   1 
ATOM   614  N  N   . HIS   A 1 80  ? 14.821  23.140 4.452  1.00 18.71 ? 80  HIS   A N   1 
ATOM   615  C  CA  . HIS   A 1 80  ? 14.900  22.978 5.905  1.00 20.68 ? 80  HIS   A CA  1 
ATOM   616  C  C   . HIS   A 1 80  ? 14.619  24.328 6.548  1.00 22.69 ? 80  HIS   A C   1 
ATOM   617  O  O   . HIS   A 1 80  ? 14.892  25.359 5.949  1.00 22.66 ? 80  HIS   A O   1 
ATOM   618  C  CB  . HIS   A 1 80  ? 16.257  22.428 6.369  1.00 21.60 ? 80  HIS   A CB  1 
ATOM   619  C  CG  . HIS   A 1 80  ? 17.432  23.306 6.130  1.00 23.22 ? 80  HIS   A CG  1 
ATOM   620  N  ND1 . HIS   A 1 80  ? 18.157  23.271 4.954  1.00 24.43 ? 80  HIS   A ND1 1 
ATOM   621  C  CD2 . HIS   A 1 80  ? 18.002  24.261 6.896  1.00 27.12 ? 80  HIS   A CD2 1 
ATOM   622  C  CE1 . HIS   A 1 80  ? 19.125  24.190 5.011  1.00 26.30 ? 80  HIS   A CE1 1 
ATOM   623  N  NE2 . HIS   A 1 80  ? 19.080  24.779 6.202  1.00 25.95 ? 80  HIS   A NE2 1 
ATOM   624  N  N   . SER   A 1 81  ? 14.030  24.311 7.743  1.00 22.15 ? 81  SER   A N   1 
ATOM   625  C  CA  . SER   A 1 81  ? 13.799  25.499 8.530  1.00 22.96 ? 81  SER   A CA  1 
ATOM   626  C  C   . SER   A 1 81  ? 13.606  25.073 9.981  1.00 23.01 ? 81  SER   A C   1 
ATOM   627  O  O   . SER   A 1 81  ? 13.167  23.965 10.259 1.00 20.90 ? 81  SER   A O   1 
ATOM   628  C  CB  . SER   A 1 81  ? 12.606  26.278 8.050  1.00 25.06 ? 81  SER   A CB  1 
ATOM   629  O  OG  . SER   A 1 81  ? 11.397  25.562 8.237  1.00 25.01 ? 81  SER   A OG  1 
ATOM   630  N  N   . MET   A 1 82  ? 13.857  26.010 10.881 1.00 21.32 ? 82  MET   A N   1 
ATOM   631  C  CA  . MET   A 1 82  ? 13.735  25.758 12.292 1.00 21.87 ? 82  MET   A CA  1 
ATOM   632  C  C   . MET   A 1 82  ? 12.479  26.458 12.787 1.00 23.27 ? 82  MET   A C   1 
ATOM   633  O  O   . MET   A 1 82  ? 12.283  27.620 12.450 1.00 19.75 ? 82  MET   A O   1 
ATOM   634  C  CB  . MET   A 1 82  ? 14.976  26.290 13.003 1.00 22.14 ? 82  MET   A CB  1 
ATOM   635  C  CG  . MET   A 1 82  ? 15.026  25.853 14.449 1.00 25.33 ? 82  MET   A CG  1 
ATOM   636  S  SD  . MET   A 1 82  ? 16.690  26.038 15.115 1.00 27.78 ? 82  MET   A SD  1 
ATOM   637  C  CE  . MET   A 1 82  ? 16.935  27.817 15.062 1.00 32.88 ? 82  MET   A CE  1 
ATOM   638  N  N   . GLN   A 1 83  ? 11.652  25.758 13.580 1.00 17.91 ? 83  GLN   A N   1 
ATOM   639  C  CA  . GLN   A 1 83  ? 10.510  26.387 14.226 1.00 19.81 ? 83  GLN   A CA  1 
ATOM   640  C  C   . GLN   A 1 83  ? 10.601  26.093 15.718 1.00 19.12 ? 83  GLN   A C   1 
ATOM   641  O  O   . GLN   A 1 83  ? 10.448  24.949 16.109 1.00 19.87 ? 83  GLN   A O   1 
ATOM   642  C  CB  . GLN   A 1 83  ? 9.216   25.865 13.609 1.00 19.35 ? 83  GLN   A CB  1 
ATOM   643  C  CG  . GLN   A 1 83  ? 7.956   26.479 14.209 1.00 20.30 ? 83  GLN   A CG  1 
ATOM   644  C  CD  . GLN   A 1 83  ? 6.681   25.942 13.607 1.00 21.29 ? 83  GLN   A CD  1 
ATOM   645  O  OE1 . GLN   A 1 83  ? 6.634   24.957 12.845 1.00 21.58 ? 83  GLN   A OE1 1 
ATOM   646  N  NE2 . GLN   A 1 83  ? 5.608   26.615 13.961 1.00 23.03 ? 83  GLN   A NE2 1 
ATOM   647  N  N   . ASN   A 1 84  ? 10.929  27.097 16.522 1.00 19.01 ? 84  ASN   A N   1 
ATOM   648  C  CA  . ASN   A 1 84  ? 11.165  26.882 17.943 1.00 18.41 ? 84  ASN   A CA  1 
ATOM   649  C  C   . ASN   A 1 84  ? 12.215  25.780 18.093 1.00 18.59 ? 84  ASN   A C   1 
ATOM   650  O  O   . ASN   A 1 84  ? 13.299  25.910 17.560 1.00 16.65 ? 84  ASN   A O   1 
ATOM   651  C  CB  . ASN   A 1 84  ? 9.828   26.678 18.639 1.00 20.97 ? 84  ASN   A CB  1 
ATOM   652  C  CG  . ASN   A 1 84  ? 8.919   27.873 18.417 1.00 22.54 ? 84  ASN   A CG  1 
ATOM   653  O  OD1 . ASN   A 1 84  ? 9.318   29.002 18.710 1.00 22.34 ? 84  ASN   A OD1 1 
ATOM   654  N  ND2 . ASN   A 1 84  ? 7.721   27.652 17.899 1.00 20.51 ? 84  ASN   A ND2 1 
ATOM   655  N  N   . CYS   A 1 85  ? 11.899  24.679 18.796 1.00 16.46 ? 85  CYS   A N   1 
ATOM   656  C  CA  . CYS   A 1 85  ? 12.875  23.637 19.049 1.00 15.54 ? 85  CYS   A CA  1 
ATOM   657  C  C   . CYS   A 1 85  ? 12.712  22.444 18.104 1.00 16.54 ? 85  CYS   A C   1 
ATOM   658  O  O   . CYS   A 1 85  ? 13.277  21.383 18.395 1.00 15.20 ? 85  CYS   A O   1 
ATOM   659  C  CB  . CYS   A 1 85  ? 12.792  23.157 20.498 1.00 16.07 ? 85  CYS   A CB  1 
ATOM   660  S  SG  . CYS   A 1 85  ? 13.064  24.448 21.733 1.00 18.36 ? 85  CYS   A SG  1 
ATOM   661  N  N   . VAL   A 1 86  ? 11.960  22.596 16.991 1.00 16.90 ? 86  VAL   A N   1 
ATOM   662  C  CA  . VAL   A 1 86  ? 11.906  21.556 15.985 1.00 18.39 ? 86  VAL   A CA  1 
ATOM   663  C  C   . VAL   A 1 86  ? 12.481  22.053 14.655 1.00 19.10 ? 86  VAL   A C   1 
ATOM   664  O  O   . VAL   A 1 86  ? 12.431  23.228 14.311 1.00 18.41 ? 86  VAL   A O   1 
ATOM   665  C  CB  . VAL   A 1 86  ? 10.520  20.913 15.760 1.00 21.83 ? 86  VAL   A CB  1 
ATOM   666  C  CG1 . VAL   A 1 86  ? 10.026  20.198 17.016 1.00 20.67 ? 86  VAL   A CG1 1 
ATOM   667  C  CG2 . VAL   A 1 86  ? 9.508   21.914 15.251 1.00 26.45 ? 86  VAL   A CG2 1 
ATOM   668  N  N   . LEU   A 1 87  ? 13.055  21.103 13.935 1.00 18.46 ? 87  LEU   A N   1 
ATOM   669  C  CA  . LEU   A 1 87  ? 13.477  21.283 12.562 1.00 21.84 ? 87  LEU   A CA  1 
ATOM   670  C  C   . LEU   A 1 87  ? 12.428  20.659 11.655 1.00 19.32 ? 87  LEU   A C   1 
ATOM   671  O  O   . LEU   A 1 87  ? 11.891  19.602 11.971 1.00 18.29 ? 87  LEU   A O   1 
ATOM   672  C  CB  . LEU   A 1 87  ? 14.804  20.529 12.535 1.00 25.06 ? 87  LEU   A CB  1 
ATOM   673  C  CG  . LEU   A 1 87  ? 15.778  20.840 11.411 1.00 35.01 ? 87  LEU   A CG  1 
ATOM   674  C  CD1 . LEU   A 1 87  ? 16.113  22.322 11.370 1.00 39.67 ? 87  LEU   A CD1 1 
ATOM   675  C  CD2 . LEU   A 1 87  ? 17.031  20.014 11.614 1.00 34.97 ? 87  LEU   A CD2 1 
ATOM   676  N  N   . LYS   A 1 88  ? 12.168  21.309 10.525 1.00 16.97 ? 88  LYS   A N   1 
ATOM   677  C  CA  . LYS   A 1 88  ? 11.253  20.814 9.523  1.00 17.14 ? 88  LYS   A CA  1 
ATOM   678  C  C   . LYS   A 1 88  ? 12.059  20.635 8.258  1.00 16.82 ? 88  LYS   A C   1 
ATOM   679  O  O   . LYS   A 1 88  ? 12.627  21.597 7.731  1.00 18.91 ? 88  LYS   A O   1 
ATOM   680  C  CB  . LYS   A 1 88  ? 10.090  21.791 9.304  1.00 18.60 ? 88  LYS   A CB  1 
ATOM   681  C  CG  . LYS   A 1 88  ? 9.269   22.043 10.556 1.00 22.81 ? 88  LYS   A CG  1 
ATOM   682  C  CD  . LYS   A 1 88  ? 8.020   22.901 10.375 1.00 23.89 ? 88  LYS   A CD  1 
ATOM   683  C  CE  . LYS   A 1 88  ? 8.396   24.293 10.065 1.00 25.44 ? 88  LYS   A CE  1 
ATOM   684  N  NZ  . LYS   A 1 88  ? 7.210   25.136 10.205 1.00 26.39 ? 88  LYS   A NZ  1 
ATOM   685  N  N   . LEU   A 1 89  ? 12.140  19.400 7.819  1.00 14.71 ? 89  LEU   A N   1 
ATOM   686  C  CA  . LEU   A 1 89  ? 12.846  19.054 6.597  1.00 16.54 ? 89  LEU   A CA  1 
ATOM   687  C  C   . LEU   A 1 89  ? 11.840  18.759 5.504  1.00 16.39 ? 89  LEU   A C   1 
ATOM   688  O  O   . LEU   A 1 89  ? 11.107  17.778 5.582  1.00 15.60 ? 89  LEU   A O   1 
ATOM   689  C  CB  . LEU   A 1 89  ? 13.730  17.843 6.827  1.00 16.62 ? 89  LEU   A CB  1 
ATOM   690  C  CG  . LEU   A 1 89  ? 14.654  17.943 8.041  1.00 19.05 ? 89  LEU   A CG  1 
ATOM   691  C  CD1 . LEU   A 1 89  ? 15.382  16.640 8.269  1.00 18.50 ? 89  LEU   A CD1 1 
ATOM   692  C  CD2 . LEU   A 1 89  ? 15.636  19.081 7.812  1.00 20.28 ? 89  LEU   A CD2 1 
ATOM   693  N  N   . LYS   A 1 90  ? 11.867  19.589 4.466  1.00 16.56 ? 90  LYS   A N   1 
ATOM   694  C  CA  . LYS   A 1 90  ? 11.037  19.360 3.307  1.00 17.24 ? 90  LYS   A CA  1 
ATOM   695  C  C   . LYS   A 1 90  ? 11.766  18.326 2.468  1.00 15.71 ? 90  LYS   A C   1 
ATOM   696  O  O   . LYS   A 1 90  ? 12.976  18.442 2.232  1.00 16.22 ? 90  LYS   A O   1 
ATOM   697  C  CB  . LYS   A 1 90  ? 10.810  20.629 2.479  1.00 20.15 ? 90  LYS   A CB  1 
ATOM   698  C  CG  . LYS   A 1 90  ? 9.999   20.311 1.231  1.00 29.02 ? 90  LYS   A CG  1 
ATOM   699  C  CD  . LYS   A 1 90  ? 9.227   21.449 0.588  1.00 39.62 ? 90  LYS   A CD  1 
ATOM   700  C  CE  . LYS   A 1 90  ? 7.960   21.620 1.369  1.00 50.95 ? 90  LYS   A CE  1 
ATOM   701  N  NZ  . LYS   A 1 90  ? 7.033   22.504 0.660  1.00 56.27 ? 90  LYS   A NZ  1 
ATOM   702  N  N   . VAL   A 1 91  ? 11.033  17.288 2.103  1.00 15.45 ? 91  VAL   A N   1 
ATOM   703  C  CA  . VAL   A 1 91  ? 11.568  16.170 1.345  1.00 16.27 ? 91  VAL   A CA  1 
ATOM   704  C  C   . VAL   A 1 91  ? 10.836  16.101 0.006  1.00 17.04 ? 91  VAL   A C   1 
ATOM   705  O  O   . VAL   A 1 91  ? 9.725   16.628 -0.164 1.00 17.04 ? 91  VAL   A O   1 
ATOM   706  C  CB  . VAL   A 1 91  ? 11.517  14.839 2.108  1.00 16.33 ? 91  VAL   A CB  1 
ATOM   707  C  CG1 . VAL   A 1 91  ? 12.508  14.852 3.255  1.00 17.29 ? 91  VAL   A CG1 1 
ATOM   708  C  CG2 . VAL   A 1 91  ? 10.125  14.473 2.616  1.00 17.02 ? 91  VAL   A CG2 1 
ATOM   709  N  N   . ASP   A 1 92  ? 11.404  15.358 -0.937 1.00 18.04 ? 92  ASP   A N   1 
ATOM   710  C  CA  . ASP   A 1 92  ? 10.853  15.371 -2.285 1.00 19.87 ? 92  ASP   A CA  1 
ATOM   711  C  C   . ASP   A 1 92  ? 9.805   14.298 -2.504 1.00 22.53 ? 92  ASP   A C   1 
ATOM   712  O  O   . ASP   A 1 92  ? 9.315   14.175 -3.626 1.00 20.83 ? 92  ASP   A O   1 
ATOM   713  C  CB  . ASP   A 1 92  ? 11.940  15.267 -3.341 1.00 22.44 ? 92  ASP   A CB  1 
ATOM   714  C  CG  . ASP   A 1 92  ? 12.600  13.908 -3.466 1.00 27.82 ? 92  ASP   A CG  1 
ATOM   715  O  OD1 . ASP   A 1 92  ? 12.252  12.999 -2.669 1.00 28.59 ? 92  ASP   A OD1 1 
ATOM   716  O  OD2 . ASP   A 1 92  ? 13.451  13.774 -4.378 1.00 31.06 ? 92  ASP   A OD2 1 
ATOM   717  N  N   . THR   A 1 93  ? 9.446   13.550 -1.452 1.00 21.24 ? 93  THR   A N   1 
ATOM   718  C  CA  . THR   A 1 93  ? 8.457   12.484 -1.544 1.00 21.42 ? 93  THR   A CA  1 
ATOM   719  C  C   . THR   A 1 93  ? 7.418   12.711 -0.447 1.00 18.06 ? 93  THR   A C   1 
ATOM   720  O  O   . THR   A 1 93  ? 7.780   12.838 0.718  1.00 16.78 ? 93  THR   A O   1 
ATOM   721  C  CB  . THR   A 1 93  ? 9.156   11.137 -1.353 1.00 22.91 ? 93  THR   A CB  1 
ATOM   722  O  OG1 . THR   A 1 93  ? 9.990   10.938 -2.487 1.00 27.12 ? 93  THR   A OG1 1 
ATOM   723  C  CG2 . THR   A 1 93  ? 8.208   9.945  -1.366 1.00 25.30 ? 93  THR   A CG2 1 
ATOM   724  N  N   . ALA   A 1 94  ? 6.139   12.648 -0.797 1.00 16.66 ? 94  ALA   A N   1 
ATOM   725  C  CA  . ALA   A 1 94  ? 5.084   12.743 0.212  1.00 16.05 ? 94  ALA   A CA  1 
ATOM   726  C  C   . ALA   A 1 94  ? 4.879   11.374 0.832  1.00 16.35 ? 94  ALA   A C   1 
ATOM   727  O  O   . ALA   A 1 94  ? 4.908   10.391 0.111  1.00 17.15 ? 94  ALA   A O   1 
ATOM   728  C  CB  . ALA   A 1 94  ? 3.806   13.232 -0.398 1.00 15.66 ? 94  ALA   A CB  1 
ATOM   729  N  N   . ASN   A 1 95  ? 4.703   11.293 2.166  1.00 17.94 ? 95  ASN   A N   1 
ATOM   730  C  CA  . ASN   A 1 95  ? 4.522   9.989  2.807  1.00 15.86 ? 95  ASN   A CA  1 
ATOM   731  C  C   . ASN   A 1 95  ? 3.146   9.445  2.425  1.00 16.04 ? 95  ASN   A C   1 
ATOM   732  O  O   . ASN   A 1 95  ? 2.133   10.017 2.836  1.00 15.67 ? 95  ASN   A O   1 
ATOM   733  C  CB  . ASN   A 1 95  ? 4.670   10.080 4.328  1.00 15.73 ? 95  ASN   A CB  1 
ATOM   734  C  CG  . ASN   A 1 95  ? 4.450   8.754  5.023  1.00 14.77 ? 95  ASN   A CG  1 
ATOM   735  O  OD1 . ASN   A 1 95  ? 4.269   7.711  4.384  1.00 13.87 ? 95  ASN   A OD1 1 
ATOM   736  N  ND2 . ASN   A 1 95  ? 4.500   8.771  6.341  1.00 16.07 ? 95  ASN   A ND2 1 
ATOM   737  N  N   . PRO   A 1 96  ? 3.044   8.321  1.671  1.00 16.95 ? 96  PRO   A N   1 
ATOM   738  C  CA  . PRO   A 1 96  ? 1.731   7.814  1.239  1.00 18.92 ? 96  PRO   A CA  1 
ATOM   739  C  C   . PRO   A 1 96  ? 0.879   7.238  2.376  1.00 21.59 ? 96  PRO   A C   1 
ATOM   740  O  O   . PRO   A 1 96  ? -0.337  7.146  2.225  1.00 18.81 ? 96  PRO   A O   1 
ATOM   741  C  CB  . PRO   A 1 96  ? 2.081   6.739  0.198  1.00 20.44 ? 96  PRO   A CB  1 
ATOM   742  C  CG  . PRO   A 1 96  ? 3.428   6.249  0.641  1.00 21.33 ? 96  PRO   A CG  1 
ATOM   743  C  CD  . PRO   A 1 96  ? 4.147   7.499  1.156  1.00 17.83 ? 96  PRO   A CD  1 
ATOM   744  N  N   . LYS   A 1 97  ? 1.505   6.965  3.535  1.00 20.79 ? 97  LYS   A N   1 
ATOM   745  C  CA  . LYS   A 1 97  ? 0.804   6.474  4.719  1.00 22.35 ? 97  LYS   A CA  1 
ATOM   746  C  C   . LYS   A 1 97  ? 0.416   7.566  5.721  1.00 19.16 ? 97  LYS   A C   1 
ATOM   747  O  O   . LYS   A 1 97  ? 0.010   7.250  6.831  1.00 17.90 ? 97  LYS   A O   1 
ATOM   748  C  CB  . LYS   A 1 97  ? 1.747   5.506  5.441  1.00 24.66 ? 97  LYS   A CB  1 
ATOM   749  C  CG  . LYS   A 1 97  ? 2.074   4.221  4.693  1.00 27.67 ? 97  LYS   A CG  1 
ATOM   750  C  CD  . LYS   A 1 97  ? 2.897   3.332  5.618  1.00 30.95 ? 97  LYS   A CD  1 
ATOM   751  C  CE  . LYS   A 1 97  ? 4.002   2.558  5.018  1.00 39.58 ? 97  LYS   A CE  1 
ATOM   752  N  NZ  . LYS   A 1 97  ? 3.439   1.327  4.475  1.00 46.96 ? 97  LYS   A NZ  1 
ATOM   753  N  N   . THR   A 1 98  ? 0.505   8.834  5.330  1.00 16.76 ? 98  THR   A N   1 
ATOM   754  C  CA  . THR   A 1 98  ? 0.152   9.950  6.186  1.00 16.40 ? 98  THR   A CA  1 
ATOM   755  C  C   . THR   A 1 98  ? -1.316  9.801  6.576  1.00 15.92 ? 98  THR   A C   1 
ATOM   756  O  O   . THR   A 1 98  ? -2.184  9.791  5.713  1.00 14.41 ? 98  THR   A O   1 
ATOM   757  C  CB  . THR   A 1 98  ? 0.370   11.278 5.464  1.00 17.16 ? 98  THR   A CB  1 
ATOM   758  O  OG1 . THR   A 1 98  ? 1.757   11.365 5.135  1.00 17.18 ? 98  THR   A OG1 1 
ATOM   759  C  CG2 . THR   A 1 98  ? 0.033   12.486 6.303  1.00 17.64 ? 98  THR   A CG2 1 
ATOM   760  N  N   . PRO   A 1 99  ? -1.641  9.758  7.872  1.00 14.73 ? 99  PRO   A N   1 
ATOM   761  C  CA  . PRO   A 1 99  ? -3.044  9.758  8.300  1.00 15.58 ? 99  PRO   A CA  1 
ATOM   762  C  C   . PRO   A 1 99  ? -3.638  11.153 8.228  1.00 14.81 ? 99  PRO   A C   1 
ATOM   763  O  O   . PRO   A 1 99  ? -2.907  12.135 8.144  1.00 14.20 ? 99  PRO   A O   1 
ATOM   764  C  CB  . PRO   A 1 99  ? -2.929  9.281  9.744  1.00 15.09 ? 99  PRO   A CB  1 
ATOM   765  C  CG  . PRO   A 1 99  ? -1.598  9.844  10.222 1.00 14.91 ? 99  PRO   A CG  1 
ATOM   766  C  CD  . PRO   A 1 99  ? -0.680  9.745  9.008  1.00 14.88 ? 99  PRO   A CD  1 
ATOM   767  N  N   . LYS   A 1 100 ? -4.972  11.261 8.346  1.00 15.13 ? 100 LYS   A N   1 
ATOM   768  C  CA  . LYS   A 1 100 ? -5.537  12.544 8.712  1.00 16.11 ? 100 LYS   A CA  1 
ATOM   769  C  C   . LYS   A 1 100 ? -4.960  12.920 10.071 1.00 15.90 ? 100 LYS   A C   1 
ATOM   770  O  O   . LYS   A 1 100 ? -4.909  12.066 10.970 1.00 16.02 ? 100 LYS   A O   1 
ATOM   771  C  CB  . LYS   A 1 100 ? -7.055  12.487 8.835  1.00 18.30 ? 100 LYS   A CB  1 
ATOM   772  C  CG  . LYS   A 1 100 ? -7.731  13.811 9.118  1.00 19.72 ? 100 LYS   A CG  1 
ATOM   773  C  CD  . LYS   A 1 100 ? -9.247  13.636 9.215  1.00 22.63 ? 100 LYS   A CD  1 
ATOM   774  C  CE  . LYS   A 1 100 ? -9.967  14.937 9.415  1.00 24.98 ? 100 LYS   A CE  1 
ATOM   775  N  NZ  . LYS   A 1 100 ? -11.406 14.615 9.424  1.00 26.67 ? 100 LYS   A NZ  1 
ATOM   776  N  N   . TYR   A 1 101 ? -4.510  14.160 10.235 1.00 15.10 ? 101 TYR   A N   1 
ATOM   777  C  CA  . TYR   A 1 101 ? -3.842  14.512 11.466 1.00 17.47 ? 101 TYR   A CA  1 
ATOM   778  C  C   . TYR   A 1 101 ? -4.043  15.983 11.790 1.00 19.62 ? 101 TYR   A C   1 
ATOM   779  O  O   . TYR   A 1 101 ? -4.443  16.758 10.923 1.00 19.42 ? 101 TYR   A O   1 
ATOM   780  C  CB  . TYR   A 1 101 ? -2.356  14.166 11.371 1.00 16.52 ? 101 TYR   A CB  1 
ATOM   781  C  CG  . TYR   A 1 101 ? -1.578  15.158 10.518 1.00 18.59 ? 101 TYR   A CG  1 
ATOM   782  C  CD1 . TYR   A 1 101 ? -1.458  14.991 9.144  1.00 18.95 ? 101 TYR   A CD1 1 
ATOM   783  C  CD2 . TYR   A 1 101 ? -0.977  16.266 11.096 1.00 20.64 ? 101 TYR   A CD2 1 
ATOM   784  C  CE1 . TYR   A 1 101 ? -0.758  15.900 8.373  1.00 20.36 ? 101 TYR   A CE1 1 
ATOM   785  C  CE2 . TYR   A 1 101 ? -0.266  17.174 10.341 1.00 21.04 ? 101 TYR   A CE2 1 
ATOM   786  C  CZ  . TYR   A 1 101 ? -0.190  17.005 8.970  1.00 22.20 ? 101 TYR   A CZ  1 
ATOM   787  O  OH  . TYR   A 1 101 ? 0.530   17.871 8.228  1.00 24.92 ? 101 TYR   A OH  1 
ATOM   788  N  N   . LYS   A 1 102 ? -3.771  16.319 13.056 1.00 18.73 ? 102 LYS   A N   1 
ATOM   789  C  CA  . LYS   A 1 102 ? -3.712  17.680 13.556 1.00 22.17 ? 102 LYS   A CA  1 
ATOM   790  C  C   . LYS   A 1 102 ? -2.559  17.789 14.553 1.00 19.63 ? 102 LYS   A C   1 
ATOM   791  O  O   . LYS   A 1 102 ? -2.184  16.801 15.140 1.00 17.43 ? 102 LYS   A O   1 
ATOM   792  C  CB  . LYS   A 1 102 ? -4.941  18.032 14.410 1.00 24.69 ? 102 LYS   A CB  1 
ATOM   793  C  CG  . LYS   A 1 102 ? -6.207  18.357 13.628 1.00 34.41 ? 102 LYS   A CG  1 
ATOM   794  C  CD  . LYS   A 1 102 ? -7.513  17.986 14.334 1.00 40.91 ? 102 LYS   A CD  1 
ATOM   795  C  CE  . LYS   A 1 102 ? -7.567  18.196 15.815 1.00 46.74 ? 102 LYS   A CE  1 
ATOM   796  N  NZ  . LYS   A 1 102 ? -7.517  19.627 16.140 1.00 53.87 ? 102 LYS   A NZ  1 
ATOM   797  N  N   . PHE   A 1 103 ? -2.059  19.000 14.751 1.00 20.22 ? 103 PHE   A N   1 
ATOM   798  C  CA  . PHE   A 1 103 ? -1.108  19.285 15.804 1.00 19.16 ? 103 PHE   A CA  1 
ATOM   799  C  C   . PHE   A 1 103 ? -1.869  20.006 16.895 1.00 21.66 ? 103 PHE   A C   1 
ATOM   800  O  O   . PHE   A 1 103 ? -2.552  20.987 16.596 1.00 21.93 ? 103 PHE   A O   1 
ATOM   801  C  CB  . PHE   A 1 103 ? 0.019   20.155 15.264 1.00 16.93 ? 103 PHE   A CB  1 
ATOM   802  C  CG  . PHE   A 1 103 ? 1.020   19.509 14.328 1.00 16.85 ? 103 PHE   A CG  1 
ATOM   803  C  CD1 . PHE   A 1 103 ? 1.072   18.134 14.133 1.00 16.09 ? 103 PHE   A CD1 1 
ATOM   804  C  CD2 . PHE   A 1 103 ? 1.932   20.308 13.653 1.00 18.50 ? 103 PHE   A CD2 1 
ATOM   805  C  CE1 . PHE   A 1 103 ? 2.022   17.571 13.278 1.00 17.87 ? 103 PHE   A CE1 1 
ATOM   806  C  CE2 . PHE   A 1 103 ? 2.858   19.751 12.785 1.00 17.32 ? 103 PHE   A CE2 1 
ATOM   807  C  CZ  . PHE   A 1 103 ? 2.921   18.378 12.622 1.00 16.79 ? 103 PHE   A CZ  1 
ATOM   808  N  N   . VAL   A 1 104 ? -1.806  19.489 18.127 1.00 19.44 ? 104 VAL   A N   1 
ATOM   809  C  CA  . VAL   A 1 104 ? -2.512  20.129 19.225 1.00 18.83 ? 104 VAL   A CA  1 
ATOM   810  C  C   . VAL   A 1 104 ? -1.552  20.311 20.385 1.00 18.43 ? 104 VAL   A C   1 
ATOM   811  O  O   . VAL   A 1 104 ? -0.633  19.522 20.567 1.00 18.16 ? 104 VAL   A O   1 
ATOM   812  C  CB  . VAL   A 1 104 ? -3.755  19.367 19.710 1.00 21.82 ? 104 VAL   A CB  1 
ATOM   813  C  CG1 . VAL   A 1 104 ? -4.729  19.079 18.570 1.00 24.53 ? 104 VAL   A CG1 1 
ATOM   814  C  CG2 . VAL   A 1 104 ? -3.363  18.089 20.425 1.00 26.48 ? 104 VAL   A CG2 1 
ATOM   815  N  N   . ARG   A 1 105 ? -1.758  21.386 21.150 1.00 19.11 ? 105 ARG   A N   1 
ATOM   816  C  CA  . ARG   A 1 105 ? -1.064  21.565 22.405 1.00 20.36 ? 105 ARG   A CA  1 
ATOM   817  C  C   . ARG   A 1 105 ? -1.995  21.073 23.499 1.00 23.69 ? 105 ARG   A C   1 
ATOM   818  O  O   . ARG   A 1 105 ? -3.077  21.623 23.654 1.00 23.17 ? 105 ARG   A O   1 
ATOM   819  C  CB  . ARG   A 1 105 ? -0.705  23.036 22.612 1.00 23.74 ? 105 ARG   A CB  1 
ATOM   820  C  CG  . ARG   A 1 105 ? 0.217   23.273 23.794 1.00 23.46 ? 105 ARG   A CG  1 
ATOM   821  C  CD  . ARG   A 1 105 ? 0.969   24.570 23.653 1.00 24.46 ? 105 ARG   A CD  1 
ATOM   822  N  NE  . ARG   A 1 105 ? 1.740   24.767 24.884 1.00 21.86 ? 105 ARG   A NE  1 
ATOM   823  C  CZ  . ARG   A 1 105 ? 3.012   24.493 25.036 1.00 19.51 ? 105 ARG   A CZ  1 
ATOM   824  N  NH1 . ARG   A 1 105 ? 3.658   23.957 24.042 1.00 19.58 ? 105 ARG   A NH1 1 
ATOM   825  N  NH2 . ARG   A 1 105 ? 3.592   24.644 26.211 1.00 18.88 ? 105 ARG   A NH2 1 
ATOM   826  N  N   . ILE   A 1 106 ? -1.608  20.032 24.233 1.00 19.80 ? 106 ILE   A N   1 
ATOM   827  C  CA  . ILE   A 1 106 ? -2.483  19.572 25.300 1.00 22.56 ? 106 ILE   A CA  1 
ATOM   828  C  C   . ILE   A 1 106 ? -2.253  20.363 26.581 1.00 21.23 ? 106 ILE   A C   1 
ATOM   829  O  O   . ILE   A 1 106 ? -1.301  21.105 26.722 1.00 20.06 ? 106 ILE   A O   1 
ATOM   830  C  CB  . ILE   A 1 106 ? -2.324  18.075 25.563 1.00 23.25 ? 106 ILE   A CB  1 
ATOM   831  C  CG1 . ILE   A 1 106 ? -0.881  17.727 25.904 1.00 22.21 ? 106 ILE   A CG1 1 
ATOM   832  C  CG2 . ILE   A 1 106 ? -2.900  17.296 24.387 1.00 27.12 ? 106 ILE   A CG2 1 
ATOM   833  C  CD1 . ILE   A 1 106 ? -0.742  16.337 26.477 1.00 25.72 ? 106 ILE   A CD1 1 
ATOM   834  N  N   . GLN   A 1 107 ? -3.184  20.160 27.508 1.00 23.05 ? 107 GLN   A N   1 
ATOM   835  C  CA  . GLN   A 1 107 ? -3.242  20.842 28.781 1.00 25.06 ? 107 GLN   A CA  1 
ATOM   836  C  C   . GLN   A 1 107 ? -2.761  19.867 29.847 1.00 23.09 ? 107 GLN   A C   1 
ATOM   837  O  O   . GLN   A 1 107 ? -2.918  18.660 29.715 1.00 17.29 ? 107 GLN   A O   1 
ATOM   838  C  CB  . GLN   A 1 107 ? -4.698  21.170 29.110 1.00 28.73 ? 107 GLN   A CB  1 
ATOM   839  C  CG  . GLN   A 1 107 ? -5.358  22.132 28.128 1.00 35.57 ? 107 GLN   A CG  1 
ATOM   840  C  CD  . GLN   A 1 107 ? -4.595  23.432 28.036 1.00 42.45 ? 107 GLN   A CD  1 
ATOM   841  O  OE1 . GLN   A 1 107 ? -4.248  23.899 26.944 1.00 52.43 ? 107 GLN   A OE1 1 
ATOM   842  N  NE2 . GLN   A 1 107 ? -4.287  24.010 29.189 1.00 41.10 ? 107 GLN   A NE2 1 
ATOM   843  N  N   . PRO   A 1 108 ? -2.186  20.351 30.959 1.00 23.32 ? 108 PRO   A N   1 
ATOM   844  C  CA  . PRO   A 1 108 ? -1.812  19.456 32.047 1.00 24.05 ? 108 PRO   A CA  1 
ATOM   845  C  C   . PRO   A 1 108 ? -3.040  18.693 32.512 1.00 21.87 ? 108 PRO   A C   1 
ATOM   846  O  O   . PRO   A 1 108 ? -4.139  19.233 32.514 1.00 20.41 ? 108 PRO   A O   1 
ATOM   847  C  CB  . PRO   A 1 108 ? -1.201  20.388 33.130 1.00 27.49 ? 108 PRO   A CB  1 
ATOM   848  C  CG  . PRO   A 1 108 ? -1.583  21.794 32.688 1.00 26.90 ? 108 PRO   A CG  1 
ATOM   849  C  CD  . PRO   A 1 108 ? -1.851  21.759 31.206 1.00 27.10 ? 108 PRO   A CD  1 
ATOM   850  N  N   . GLY   A 1 109 ? -2.865  17.415 32.853 1.00 19.92 ? 109 GLY   A N   1 
ATOM   851  C  CA  . GLY   A 1 109 ? -3.965  16.540 33.211 1.00 19.30 ? 109 GLY   A CA  1 
ATOM   852  C  C   . GLY   A 1 109 ? -4.443  15.644 32.067 1.00 20.88 ? 109 GLY   A C   1 
ATOM   853  O  O   . GLY   A 1 109 ? -5.039  14.615 32.319 1.00 22.03 ? 109 GLY   A O   1 
ATOM   854  N  N   . GLN   A 1 110 ? -4.171  16.015 30.813 1.00 18.59 ? 110 GLN   A N   1 
ATOM   855  C  CA  . GLN   A 1 110 ? -4.581  15.212 29.676 1.00 19.38 ? 110 GLN   A CA  1 
ATOM   856  C  C   . GLN   A 1 110 ? -3.566  14.103 29.429 1.00 17.27 ? 110 GLN   A C   1 
ATOM   857  O  O   . GLN   A 1 110 ? -2.393  14.217 29.772 1.00 16.91 ? 110 GLN   A O   1 
ATOM   858  C  CB  . GLN   A 1 110 ? -4.766  16.148 28.475 1.00 22.99 ? 110 GLN   A CB  1 
ATOM   859  C  CG  . GLN   A 1 110 ? -5.901  17.134 28.742 1.00 28.08 ? 110 GLN   A CG  1 
ATOM   860  C  CD  . GLN   A 1 110 ? -6.202  18.128 27.635 1.00 36.00 ? 110 GLN   A CD  1 
ATOM   861  O  OE1 . GLN   A 1 110 ? -5.365  18.534 26.814 1.00 31.75 ? 110 GLN   A OE1 1 
ATOM   862  N  NE2 . GLN   A 1 110 ? -7.444  18.586 27.647 1.00 45.20 ? 110 GLN   A NE2 1 
ATOM   863  N  N   . THR   A 1 111 ? -4.065  13.019 28.838 1.00 16.95 ? 111 THR   A N   1 
ATOM   864  C  CA  . THR   A 1 111 ? -3.292  11.824 28.570 1.00 16.65 ? 111 THR   A CA  1 
ATOM   865  C  C   . THR   A 1 111 ? -3.073  11.694 27.066 1.00 15.26 ? 111 THR   A C   1 
ATOM   866  O  O   . THR   A 1 111 ? -3.769  12.333 26.271 1.00 15.49 ? 111 THR   A O   1 
ATOM   867  C  CB  . THR   A 1 111 ? -4.006  10.585 29.110 1.00 17.16 ? 111 THR   A CB  1 
ATOM   868  O  OG1 . THR   A 1 111 ? -5.301  10.603 28.509 1.00 15.87 ? 111 THR   A OG1 1 
ATOM   869  C  CG2 . THR   A 1 111 ? -4.140  10.619 30.624 1.00 16.78 ? 111 THR   A CG2 1 
ATOM   870  N  N   . PHE   A 1 112 ? -2.146  10.815 26.721 1.00 13.97 ? 112 PHE   A N   1 
ATOM   871  C  CA  . PHE   A 1 112 ? -1.812  10.535 25.333 1.00 14.16 ? 112 PHE   A CA  1 
ATOM   872  C  C   . PHE   A 1 112 ? -0.971  9.262  25.315 1.00 14.58 ? 112 PHE   A C   1 
ATOM   873  O  O   . PHE   A 1 112 ? -0.448  8.856  26.354 1.00 17.74 ? 112 PHE   A O   1 
ATOM   874  C  CB  . PHE   A 1 112 ? -1.089  11.724 24.703 1.00 12.70 ? 112 PHE   A CB  1 
ATOM   875  C  CG  . PHE   A 1 112 ? 0.197   12.181 25.371 1.00 13.12 ? 112 PHE   A CG  1 
ATOM   876  C  CD1 . PHE   A 1 112 ? 1.415   11.628 25.000 1.00 14.76 ? 112 PHE   A CD1 1 
ATOM   877  C  CD2 . PHE   A 1 112 ? 0.193   13.158 26.349 1.00 14.10 ? 112 PHE   A CD2 1 
ATOM   878  C  CE1 . PHE   A 1 112 ? 2.588   12.080 25.568 1.00 17.17 ? 112 PHE   A CE1 1 
ATOM   879  C  CE2 . PHE   A 1 112 ? 1.370   13.578 26.937 1.00 15.82 ? 112 PHE   A CE2 1 
ATOM   880  C  CZ  . PHE   A 1 112 ? 2.569   13.063 26.523 1.00 16.93 ? 112 PHE   A CZ  1 
ATOM   881  N  N   . SER   A 1 113 ? -0.872  8.638  24.125 1.00 13.69 ? 113 SER   A N   1 
ATOM   882  C  CA  . SER   A 1 113 ? -0.017  7.487  23.933 1.00 12.90 ? 113 SER   A CA  1 
ATOM   883  C  C   . SER   A 1 113 ? 1.335   7.954  23.411 1.00 12.93 ? 113 SER   A C   1 
ATOM   884  O  O   . SER   A 1 113 ? 1.388   8.840  22.577 1.00 12.19 ? 113 SER   A O   1 
ATOM   885  C  CB  . SER   A 1 113 ? -0.638  6.502  22.980 1.00 13.94 ? 113 SER   A CB  1 
ATOM   886  O  OG  . SER   A 1 113 ? -1.871  5.995  23.500 1.00 13.07 ? 113 SER   A OG  1 
ATOM   887  N  N   . VAL   A 1 114 ? 2.395   7.288  23.862 1.00 13.54 ? 114 VAL   A N   1 
ATOM   888  C  CA  . VAL   A 1 114 ? 3.727   7.443  23.317 1.00 13.22 ? 114 VAL   A CA  1 
ATOM   889  C  C   . VAL   A 1 114 ? 4.107   6.199  22.534 1.00 13.22 ? 114 VAL   A C   1 
ATOM   890  O  O   . VAL   A 1 114 ? 3.959   5.069  23.008 1.00 13.54 ? 114 VAL   A O   1 
ATOM   891  C  CB  . VAL   A 1 114 ? 4.694   7.697  24.471 1.00 14.07 ? 114 VAL   A CB  1 
ATOM   892  C  CG1 . VAL   A 1 114 ? 6.172   7.653  24.048 1.00 14.86 ? 114 VAL   A CG1 1 
ATOM   893  C  CG2 . VAL   A 1 114 ? 4.348   9.013  25.139 1.00 16.88 ? 114 VAL   A CG2 1 
ATOM   894  N  N   . LEU   A 1 115 ? 4.626   6.428  21.318 1.00 12.60 ? 115 LEU   A N   1 
ATOM   895  C  CA  . LEU   A 1 115 ? 5.275   5.389  20.552 1.00 12.73 ? 115 LEU   A CA  1 
ATOM   896  C  C   . LEU   A 1 115 ? 6.776   5.584  20.668 1.00 12.58 ? 115 LEU   A C   1 
ATOM   897  O  O   . LEU   A 1 115 ? 7.314   6.484  20.029 1.00 13.02 ? 115 LEU   A O   1 
ATOM   898  C  CB  . LEU   A 1 115 ? 4.812   5.426  19.094 1.00 12.87 ? 115 LEU   A CB  1 
ATOM   899  C  CG  . LEU   A 1 115 ? 5.412   4.328  18.205 1.00 13.21 ? 115 LEU   A CG  1 
ATOM   900  C  CD1 . LEU   A 1 115 ? 4.909   2.948  18.596 1.00 14.37 ? 115 LEU   A CD1 1 
ATOM   901  C  CD2 . LEU   A 1 115 ? 5.103   4.612  16.739 1.00 13.61 ? 115 LEU   A CD2 1 
ATOM   902  N  N   . ALA   A 1 116 ? 7.418   4.824  21.571 1.00 12.45 ? 116 ALA   A N   1 
ATOM   903  C  CA  . ALA   A 1 116 ? 8.846   4.954  21.803 1.00 14.42 ? 116 ALA   A CA  1 
ATOM   904  C  C   . ALA   A 1 116 ? 9.580   4.311  20.637 1.00 15.08 ? 116 ALA   A C   1 
ATOM   905  O  O   . ALA   A 1 116 ? 9.297   3.165  20.284 1.00 17.10 ? 116 ALA   A O   1 
ATOM   906  C  CB  . ALA   A 1 116 ? 9.240   4.314  23.133 1.00 16.22 ? 116 ALA   A CB  1 
ATOM   907  N  N   . CYS   A 1 117 ? 10.488  5.074  20.035 1.00 13.88 ? 117 CYS   A N   1 
ATOM   908  C  CA  . CYS   A 1 117 ? 11.201  4.660  18.848 1.00 14.38 ? 117 CYS   A CA  1 
ATOM   909  C  C   . CYS   A 1 117 ? 12.707  4.848  19.012 1.00 13.75 ? 117 CYS   A C   1 
ATOM   910  O  O   . CYS   A 1 117 ? 13.134  5.732  19.742 1.00 13.35 ? 117 CYS   A O   1 
ATOM   911  C  CB  . CYS   A 1 117 ? 10.780  5.496  17.654 1.00 15.48 ? 117 CYS   A CB  1 
ATOM   912  S  SG  . CYS   A 1 117 ? 9.072   5.193  17.178 1.00 20.25 ? 117 CYS   A SG  1 
ATOM   913  N  N   . TYR   A 1 118 ? 13.492  3.994  18.349 1.00 14.64 ? 118 TYR   A N   1 
ATOM   914  C  CA  . TYR   A 1 118 ? 14.952  4.096  18.252 1.00 16.28 ? 118 TYR   A CA  1 
ATOM   915  C  C   . TYR   A 1 118 ? 15.360  3.836  16.797 1.00 17.72 ? 118 TYR   A C   1 
ATOM   916  O  O   . TYR   A 1 118 ? 14.871  2.908  16.163 1.00 16.11 ? 118 TYR   A O   1 
ATOM   917  C  CB  . TYR   A 1 118 ? 15.679  3.120  19.196 1.00 16.38 ? 118 TYR   A CB  1 
ATOM   918  C  CG  . TYR   A 1 118 ? 15.246  3.337  20.636 1.00 15.44 ? 118 TYR   A CG  1 
ATOM   919  C  CD1 . TYR   A 1 118 ? 14.096  2.766  21.151 1.00 16.42 ? 118 TYR   A CD1 1 
ATOM   920  C  CD2 . TYR   A 1 118 ? 15.945  4.226  21.442 1.00 14.69 ? 118 TYR   A CD2 1 
ATOM   921  C  CE1 . TYR   A 1 118 ? 13.655  3.071  22.441 1.00 15.33 ? 118 TYR   A CE1 1 
ATOM   922  C  CE2 . TYR   A 1 118 ? 15.507  4.550  22.712 1.00 14.39 ? 118 TYR   A CE2 1 
ATOM   923  C  CZ  . TYR   A 1 118 ? 14.377  3.951  23.224 1.00 15.53 ? 118 TYR   A CZ  1 
ATOM   924  O  OH  . TYR   A 1 118 ? 13.941  4.336  24.471 1.00 13.78 ? 118 TYR   A OH  1 
ATOM   925  N  N   . ASN   A 1 119 ? 16.192  4.730  16.253 1.00 19.74 ? 119 ASN   A N   1 
ATOM   926  C  CA  . ASN   A 1 119 ? 16.694  4.580  14.903 1.00 20.04 ? 119 ASN   A CA  1 
ATOM   927  C  C   . ASN   A 1 119 ? 15.522  4.492  13.938 1.00 17.44 ? 119 ASN   A C   1 
ATOM   928  O  O   . ASN   A 1 119 ? 15.583  3.758  12.959 1.00 17.25 ? 119 ASN   A O   1 
ATOM   929  C  CB  . ASN   A 1 119 ? 17.632  3.385  14.795 1.00 22.47 ? 119 ASN   A CB  1 
ATOM   930  C  CG  . ASN   A 1 119 ? 18.857  3.619  15.637 1.00 27.02 ? 119 ASN   A CG  1 
ATOM   931  O  OD1 . ASN   A 1 119 ? 19.559  4.615  15.446 1.00 30.60 ? 119 ASN   A OD1 1 
ATOM   932  N  ND2 . ASN   A 1 119 ? 19.104  2.732  16.573 1.00 31.86 ? 119 ASN   A ND2 1 
ATOM   933  N  N   . GLY   A 1 120 ? 14.450  5.230  14.204 1.00 15.78 ? 120 GLY   A N   1 
ATOM   934  C  CA  . GLY   A 1 120 ? 13.347  5.283  13.261 1.00 17.97 ? 120 GLY   A CA  1 
ATOM   935  C  C   . GLY   A 1 120 ? 12.380  4.100  13.362 1.00 18.87 ? 120 GLY   A C   1 
ATOM   936  O  O   . GLY   A 1 120 ? 11.442  4.038  12.578 1.00 20.31 ? 120 GLY   A O   1 
ATOM   937  N  N   . SER   A 1 121 ? 12.624  3.153  14.290 1.00 19.04 ? 121 SER   A N   1 
ATOM   938  C  CA  . SER   A 1 121 ? 11.826  1.939  14.425 1.00 19.81 ? 121 SER   A CA  1 
ATOM   939  C  C   . SER   A 1 121 ? 11.136  1.929  15.777 1.00 19.46 ? 121 SER   A C   1 
ATOM   940  O  O   . SER   A 1 121 ? 11.756  2.244  16.796 1.00 17.88 ? 121 SER   A O   1 
ATOM   941  C  CB  . SER   A 1 121 ? 12.660  0.682  14.321 1.00 21.78 ? 121 SER   A CB  1 
ATOM   942  O  OG  . SER   A 1 121 ? 13.176  0.569  13.005 1.00 26.92 ? 121 SER   A OG  1 
ATOM   943  N  N   . PRO   A 1 122 ? 9.853   1.536  15.820 1.00 23.30 ? 122 PRO   A N   1 
ATOM   944  C  CA  . PRO   A 1 122 ? 9.124   1.483  17.090 1.00 24.38 ? 122 PRO   A CA  1 
ATOM   945  C  C   . PRO   A 1 122 ? 9.508   0.316  17.993 1.00 23.52 ? 122 PRO   A C   1 
ATOM   946  O  O   . PRO   A 1 122 ? 9.711   -0.796 17.524 1.00 25.24 ? 122 PRO   A O   1 
ATOM   947  C  CB  . PRO   A 1 122 ? 7.696   1.395  16.585 1.00 26.10 ? 122 PRO   A CB  1 
ATOM   948  C  CG  . PRO   A 1 122 ? 7.828   0.566  15.325 1.00 30.38 ? 122 PRO   A CG  1 
ATOM   949  C  CD  . PRO   A 1 122 ? 9.027   1.183  14.644 1.00 27.07 ? 122 PRO   A CD  1 
ATOM   950  N  N   . SER   A 1 123 ? 9.631   0.606  19.291 1.00 21.18 ? 123 SER   A N   1 
ATOM   951  C  CA  . SER   A 1 123 ? 9.995   -0.336 20.340 1.00 20.61 ? 123 SER   A CA  1 
ATOM   952  C  C   . SER   A 1 123 ? 8.722   -0.763 21.108 1.00 20.36 ? 123 SER   A C   1 
ATOM   953  O  O   . SER   A 1 123 ? 8.563   -1.923 21.487 1.00 17.94 ? 123 SER   A O   1 
ATOM   954  C  CB  . SER   A 1 123 ? 11.004  0.324  21.271 1.00 23.23 ? 123 SER   A CB  1 
ATOM   955  O  OG  . SER   A 1 123 ? 11.425  -0.480 22.384 1.00 29.30 ? 123 SER   A OG  1 
ATOM   956  N  N   . GLY   A 1 124 ? 7.837   0.202  21.394 1.00 16.06 ? 124 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 124 ? 6.644   -0.077 22.176 1.00 16.07 ? 124 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 124 ? 5.747   1.143  22.318 1.00 14.71 ? 124 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 124 ? 6.123   2.248  21.908 1.00 15.64 ? 124 GLY   A O   1 
ATOM   960  N  N   . VAL   A 1 125 ? 4.567   0.923  22.932 1.00 13.74 ? 125 VAL   A N   1 
ATOM   961  C  CA  . VAL   A 1 125 ? 3.564   1.957  23.085 1.00 14.29 ? 125 VAL   A CA  1 
ATOM   962  C  C   . VAL   A 1 125 ? 3.060   1.915  24.524 1.00 15.63 ? 125 VAL   A C   1 
ATOM   963  O  O   . VAL   A 1 125 ? 2.857   0.840  25.099 1.00 16.30 ? 125 VAL   A O   1 
ATOM   964  C  CB  . VAL   A 1 125 ? 2.441   1.865  22.020 1.00 17.68 ? 125 VAL   A CB  1 
ATOM   965  C  CG1 . VAL   A 1 125 ? 1.656   0.585  22.093 1.00 21.60 ? 125 VAL   A CG1 1 
ATOM   966  C  CG2 . VAL   A 1 125 ? 1.490   3.046  22.038 1.00 18.83 ? 125 VAL   A CG2 1 
ATOM   967  N  N   . TYR   A 1 126 ? 2.891   3.098  25.112 1.00 15.20 ? 126 TYR   A N   1 
ATOM   968  C  CA  . TYR   A 1 126 ? 2.297   3.195  26.435 1.00 15.37 ? 126 TYR   A CA  1 
ATOM   969  C  C   . TYR   A 1 126 ? 1.573   4.525  26.589 1.00 15.61 ? 126 TYR   A C   1 
ATOM   970  O  O   . TYR   A 1 126 ? 1.756   5.458  25.813 1.00 14.16 ? 126 TYR   A O   1 
ATOM   971  C  CB  . TYR   A 1 126 ? 3.417   2.961  27.466 1.00 15.50 ? 126 TYR   A CB  1 
ATOM   972  C  CG  . TYR   A 1 126 ? 4.583   3.916  27.330 1.00 16.50 ? 126 TYR   A CG  1 
ATOM   973  C  CD1 . TYR   A 1 126 ? 4.545   5.162  27.937 1.00 17.59 ? 126 TYR   A CD1 1 
ATOM   974  C  CD2 . TYR   A 1 126 ? 5.728   3.566  26.641 1.00 19.00 ? 126 TYR   A CD2 1 
ATOM   975  C  CE1 . TYR   A 1 126 ? 5.603   6.048  27.823 1.00 18.64 ? 126 TYR   A CE1 1 
ATOM   976  C  CE2 . TYR   A 1 126 ? 6.800   4.437  26.541 1.00 18.62 ? 126 TYR   A CE2 1 
ATOM   977  C  CZ  . TYR   A 1 126 ? 6.730   5.694  27.121 1.00 19.26 ? 126 TYR   A CZ  1 
ATOM   978  O  OH  . TYR   A 1 126 ? 7.796   6.555  27.004 1.00 19.84 ? 126 TYR   A OH  1 
ATOM   979  N  N   . GLN   A 1 127 ? 0.725   4.595  27.614 1.00 15.91 ? 127 GLN   A N   1 
ATOM   980  C  CA  . GLN   A 1 127 ? -0.063  5.771  27.903 1.00 18.67 ? 127 GLN   A CA  1 
ATOM   981  C  C   . GLN   A 1 127 ? 0.636   6.587  28.983 1.00 18.29 ? 127 GLN   A C   1 
ATOM   982  O  O   . GLN   A 1 127 ? 1.138   5.997  29.945 1.00 18.94 ? 127 GLN   A O   1 
ATOM   983  C  CB  . GLN   A 1 127 ? -1.382  5.475  28.614 1.00 24.00 ? 127 GLN   A CB  1 
ATOM   984  C  CG  . GLN   A 1 127 ? -2.609  5.278  27.766 1.00 29.18 ? 127 GLN   A CG  1 
ATOM   985  C  CD  . GLN   A 1 127 ? -3.054  6.464  26.937 1.00 31.06 ? 127 GLN   A CD  1 
ATOM   986  O  OE1 . GLN   A 1 127 ? -2.603  6.639  25.808 1.00 28.39 ? 127 GLN   A OE1 1 
ATOM   987  N  NE2 . GLN   A 1 127 ? -4.059  7.188  27.412 1.00 30.26 ? 127 GLN   A NE2 1 
ATOM   988  N  N   . CYS   A 1 128 ? 0.567   7.911  28.828 1.00 18.40 ? 128 CYS   A N   1 
ATOM   989  C  CA  . CYS   A 1 128 ? 1.194   8.911  29.701 1.00 21.56 ? 128 CYS   A CA  1 
ATOM   990  C  C   . CYS   A 1 128 ? 0.204   10.036 30.005 1.00 18.96 ? 128 CYS   A C   1 
ATOM   991  O  O   . CYS   A 1 128 ? -0.700  10.268 29.229 1.00 19.27 ? 128 CYS   A O   1 
ATOM   992  C  CB  . CYS   A 1 128 ? 2.329   9.642  28.976 1.00 24.35 ? 128 CYS   A CB  1 
ATOM   993  S  SG  . CYS   A 1 128 ? 3.866   8.744  29.157 1.00 40.66 ? 128 CYS   A SG  1 
ATOM   994  N  N   . ALA   A 1 129 ? 0.373   10.736 31.134 1.00 17.24 ? 129 ALA   A N   1 
ATOM   995  C  CA  . ALA   A 1 129 ? -0.319  11.991 31.387 1.00 17.88 ? 129 ALA   A CA  1 
ATOM   996  C  C   . ALA   A 1 129 ? 0.692   13.131 31.342 1.00 16.97 ? 129 ALA   A C   1 
ATOM   997  O  O   . ALA   A 1 129 ? 1.802   12.972 31.796 1.00 18.85 ? 129 ALA   A O   1 
ATOM   998  C  CB  . ALA   A 1 129 ? -1.014  11.965 32.722 1.00 18.78 ? 129 ALA   A CB  1 
ATOM   999  N  N   . MET   A 1 130 ? 0.304   14.260 30.740 1.00 17.36 ? 130 MET   A N   1 
ATOM   1000 C  CA  . MET   A 1 130 ? 0.994   15.515 30.958 1.00 15.38 ? 130 MET   A CA  1 
ATOM   1001 C  C   . MET   A 1 130 ? 0.760   15.913 32.417 1.00 16.17 ? 130 MET   A C   1 
ATOM   1002 O  O   . MET   A 1 130 ? -0.362  16.213 32.805 1.00 16.63 ? 130 MET   A O   1 
ATOM   1003 C  CB  . MET   A 1 130 ? 0.465   16.600 30.025 1.00 15.10 ? 130 MET   A CB  1 
ATOM   1004 C  CG  . MET   A 1 130 ? 1.185   17.933 30.133 1.00 16.73 ? 130 MET   A CG  1 
ATOM   1005 S  SD  . MET   A 1 130 ? 2.960   17.870 29.912 1.00 21.44 ? 130 MET   A SD  1 
ATOM   1006 C  CE  . MET   A 1 130 ? 3.082   17.325 28.201 1.00 20.53 ? 130 MET   A CE  1 
ATOM   1007 N  N   . ARG   A 1 131 ? 1.825   15.922 33.213 1.00 17.71 ? 131 ARG   A N   1 
ATOM   1008 C  CA  . ARG   A 1 131 ? 1.705   16.188 34.640 1.00 15.89 ? 131 ARG   A CA  1 
ATOM   1009 C  C   . ARG   A 1 131 ? 1.476   17.683 34.852 1.00 16.98 ? 131 ARG   A C   1 
ATOM   1010 O  O   . ARG   A 1 131 ? 1.843   18.492 33.985 1.00 14.87 ? 131 ARG   A O   1 
ATOM   1011 C  CB  . ARG   A 1 131 ? 2.976   15.738 35.362 1.00 17.50 ? 131 ARG   A CB  1 
ATOM   1012 C  CG  . ARG   A 1 131 ? 3.432   14.281 35.291 1.00 18.93 ? 131 ARG   A CG  1 
ATOM   1013 C  CD  . ARG   A 1 131 ? 2.387   13.251 35.734 1.00 20.54 ? 131 ARG   A CD  1 
ATOM   1014 N  NE  . ARG   A 1 131 ? 1.861   13.601 37.056 1.00 19.77 ? 131 ARG   A NE  1 
ATOM   1015 C  CZ  . ARG   A 1 131 ? 0.776   13.089 37.599 1.00 19.83 ? 131 ARG   A CZ  1 
ATOM   1016 N  NH1 . ARG   A 1 131 ? 0.314   13.572 38.755 1.00 19.73 ? 131 ARG   A NH1 1 
ATOM   1017 N  NH2 . ARG   A 1 131 ? 0.170   12.092 37.003 1.00 18.75 ? 131 ARG   A NH2 1 
ATOM   1018 N  N   . PRO   A 1 132 ? 0.848   18.108 35.988 1.00 17.55 ? 132 PRO   A N   1 
ATOM   1019 C  CA  . PRO   A 1 132 ? 0.732   19.527 36.326 1.00 19.29 ? 132 PRO   A CA  1 
ATOM   1020 C  C   . PRO   A 1 132 ? 2.040   20.316 36.267 1.00 18.82 ? 132 PRO   A C   1 
ATOM   1021 O  O   . PRO   A 1 132 ? 2.008   21.525 36.034 1.00 18.53 ? 132 PRO   A O   1 
ATOM   1022 C  CB  . PRO   A 1 132 ? 0.159   19.514 37.760 1.00 20.00 ? 132 PRO   A CB  1 
ATOM   1023 C  CG  . PRO   A 1 132 ? -0.695  18.244 37.798 1.00 19.15 ? 132 PRO   A CG  1 
ATOM   1024 C  CD  . PRO   A 1 132 ? 0.072   17.256 36.908 1.00 19.16 ? 132 PRO   A CD  1 
ATOM   1025 N  N   . ASN   A 1 133 ? 3.177   19.628 36.433 1.00 17.46 ? 133 ASN   A N   1 
ATOM   1026 C  CA  . ASN   A 1 133 ? 4.466   20.313 36.386 1.00 18.12 ? 133 ASN   A CA  1 
ATOM   1027 C  C   . ASN   A 1 133 ? 5.086   20.224 34.991 1.00 20.64 ? 133 ASN   A C   1 
ATOM   1028 O  O   . ASN   A 1 133 ? 6.267   20.529 34.823 1.00 17.43 ? 133 ASN   A O   1 
ATOM   1029 C  CB  . ASN   A 1 133 ? 5.415   19.818 37.465 1.00 21.00 ? 133 ASN   A CB  1 
ATOM   1030 C  CG  . ASN   A 1 133 ? 5.887   18.405 37.219 1.00 21.33 ? 133 ASN   A CG  1 
ATOM   1031 O  OD1 . ASN   A 1 133 ? 5.475   17.757 36.249 1.00 19.86 ? 133 ASN   A OD1 1 
ATOM   1032 N  ND2 . ASN   A 1 133 ? 6.725   17.907 38.101 1.00 20.89 ? 133 ASN   A ND2 1 
ATOM   1033 N  N   . PHE   A 1 134 ? 4.285   19.813 33.996 1.00 21.28 ? 134 PHE   A N   1 
ATOM   1034 C  CA  . PHE   A 1 134 ? 4.706   19.813 32.603 1.00 21.37 ? 134 PHE   A CA  1 
ATOM   1035 C  C   . PHE   A 1 134 ? 5.807   18.791 32.306 1.00 20.52 ? 134 PHE   A C   1 
ATOM   1036 O  O   . PHE   A 1 134 ? 6.518   18.941 31.310 1.00 21.99 ? 134 PHE   A O   1 
ATOM   1037 C  CB  . PHE   A 1 134 ? 5.114   21.218 32.145 1.00 21.42 ? 134 PHE   A CB  1 
ATOM   1038 C  CG  . PHE   A 1 134 ? 3.914   22.151 32.160 1.00 25.24 ? 134 PHE   A CG  1 
ATOM   1039 C  CD1 . PHE   A 1 134 ? 2.926   22.043 31.185 1.00 24.88 ? 134 PHE   A CD1 1 
ATOM   1040 C  CD2 . PHE   A 1 134 ? 3.761   23.113 33.155 1.00 29.64 ? 134 PHE   A CD2 1 
ATOM   1041 C  CE1 . PHE   A 1 134 ? 1.816   22.881 31.205 1.00 30.80 ? 134 PHE   A CE1 1 
ATOM   1042 C  CE2 . PHE   A 1 134 ? 2.655   23.952 33.170 1.00 28.08 ? 134 PHE   A CE2 1 
ATOM   1043 C  CZ  . PHE   A 1 134 ? 1.679   23.834 32.197 1.00 28.52 ? 134 PHE   A CZ  1 
ATOM   1044 N  N   . THR   A 1 135 ? 5.894   17.717 33.091 1.00 18.14 ? 135 THR   A N   1 
ATOM   1045 C  CA  . THR   A 1 135 ? 6.725   16.570 32.732 1.00 19.34 ? 135 THR   A CA  1 
ATOM   1046 C  C   . THR   A 1 135 ? 5.811   15.400 32.396 1.00 17.19 ? 135 THR   A C   1 
ATOM   1047 O  O   . THR   A 1 135 ? 4.613   15.483 32.626 1.00 21.01 ? 135 THR   A O   1 
ATOM   1048 C  CB  . THR   A 1 135 ? 7.658   16.237 33.884 1.00 19.08 ? 135 THR   A CB  1 
ATOM   1049 O  OG1 . THR   A 1 135 ? 6.845   15.785 34.965 1.00 19.45 ? 135 THR   A OG1 1 
ATOM   1050 C  CG2 . THR   A 1 135 ? 8.519   17.441 34.215 1.00 20.27 ? 135 THR   A CG2 1 
ATOM   1051 N  N   . ILE   A 1 136 ? 6.367   14.341 31.823 1.00 15.95 ? 136 ILE   A N   1 
ATOM   1052 C  CA  . ILE   A 1 136 ? 5.682   13.068 31.728 1.00 15.64 ? 136 ILE   A CA  1 
ATOM   1053 C  C   . ILE   A 1 136 ? 6.552   12.003 32.376 1.00 16.28 ? 136 ILE   A C   1 
ATOM   1054 O  O   . ILE   A 1 136 ? 7.767   12.100 32.372 1.00 15.51 ? 136 ILE   A O   1 
ATOM   1055 C  CB  . ILE   A 1 136 ? 5.319   12.718 30.276 1.00 16.71 ? 136 ILE   A CB  1 
ATOM   1056 C  CG1 . ILE   A 1 136 ? 6.557   12.388 29.462 1.00 16.94 ? 136 ILE   A CG1 1 
ATOM   1057 C  CG2 . ILE   A 1 136 ? 4.534   13.863 29.634 1.00 17.10 ? 136 ILE   A CG2 1 
ATOM   1058 C  CD1 . ILE   A 1 136 ? 6.260   11.937 28.047 1.00 18.65 ? 136 ILE   A CD1 1 
ATOM   1059 N  N   . LYS   A 1 137 ? 5.894   11.008 32.953 1.00 17.78 ? 137 LYS   A N   1 
ATOM   1060 C  CA  . LYS   A 1 137 ? 6.569   9.862  33.524 1.00 20.60 ? 137 LYS   A CA  1 
ATOM   1061 C  C   . LYS   A 1 137 ? 6.631   8.805  32.431 1.00 19.20 ? 137 LYS   A C   1 
ATOM   1062 O  O   . LYS   A 1 137 ? 5.780   7.906  32.359 1.00 19.13 ? 137 LYS   A O   1 
ATOM   1063 C  CB  . LYS   A 1 137 ? 5.837   9.349  34.766 1.00 24.25 ? 137 LYS   A CB  1 
ATOM   1064 C  CG  . LYS   A 1 137 ? 5.684   10.442 35.808 1.00 30.88 ? 137 LYS   A CG  1 
ATOM   1065 C  CD  . LYS   A 1 137 ? 4.881   10.005 37.030 1.00 41.21 ? 137 LYS   A CD  1 
ATOM   1066 C  CE  . LYS   A 1 137 ? 5.013   11.002 38.147 1.00 45.53 ? 137 LYS   A CE  1 
ATOM   1067 N  NZ  . LYS   A 1 137 ? 4.272   10.525 39.312 1.00 50.81 ? 137 LYS   A NZ  1 
ATOM   1068 N  N   . GLY   A 1 138 ? 7.685   8.936  31.608 1.00 17.25 ? 138 GLY   A N   1 
ATOM   1069 C  CA  . GLY   A 1 138 ? 7.881   8.093  30.448 1.00 15.99 ? 138 GLY   A CA  1 
ATOM   1070 C  C   . GLY   A 1 138 ? 8.866   6.959  30.706 1.00 16.22 ? 138 GLY   A C   1 
ATOM   1071 O  O   . GLY   A 1 138 ? 9.342   6.739  31.825 1.00 16.86 ? 138 GLY   A O   1 
ATOM   1072 N  N   . SER   A 1 139 ? 9.233   6.293  29.604 1.00 14.33 ? 139 SER   A N   1 
ATOM   1073 C  CA  . SER   A 1 139 ? 10.256  5.266  29.590 1.00 14.80 ? 139 SER   A CA  1 
ATOM   1074 C  C   . SER   A 1 139 ? 11.059  5.455  28.309 1.00 15.31 ? 139 SER   A C   1 
ATOM   1075 O  O   . SER   A 1 139 ? 10.598  5.066  27.231 1.00 15.72 ? 139 SER   A O   1 
ATOM   1076 C  CB  . SER   A 1 139 ? 9.663   3.870  29.651 1.00 15.36 ? 139 SER   A CB  1 
ATOM   1077 O  OG  . SER   A 1 139 ? 10.671  2.885  29.506 1.00 15.86 ? 139 SER   A OG  1 
ATOM   1078 N  N   . PHE   A 1 140 ? 12.198  6.124  28.444 1.00 14.24 ? 140 PHE   A N   1 
ATOM   1079 C  CA  . PHE   A 1 140 ? 12.967  6.570  27.295 1.00 13.95 ? 140 PHE   A CA  1 
ATOM   1080 C  C   . PHE   A 1 140 ? 14.464  6.445  27.595 1.00 15.86 ? 140 PHE   A C   1 
ATOM   1081 O  O   . PHE   A 1 140 ? 14.910  6.798  28.690 1.00 16.98 ? 140 PHE   A O   1 
ATOM   1082 C  CB  . PHE   A 1 140 ? 12.672  8.040  27.033 1.00 13.85 ? 140 PHE   A CB  1 
ATOM   1083 C  CG  . PHE   A 1 140 ? 11.289  8.475  26.554 1.00 15.00 ? 140 PHE   A CG  1 
ATOM   1084 C  CD1 . PHE   A 1 140 ? 10.920  8.294  25.226 1.00 17.12 ? 140 PHE   A CD1 1 
ATOM   1085 C  CD2 . PHE   A 1 140 ? 10.427  9.165  27.381 1.00 16.81 ? 140 PHE   A CD2 1 
ATOM   1086 C  CE1 . PHE   A 1 140 ? 9.703   8.773  24.757 1.00 17.32 ? 140 PHE   A CE1 1 
ATOM   1087 C  CE2 . PHE   A 1 140 ? 9.213   9.635  26.906 1.00 17.65 ? 140 PHE   A CE2 1 
ATOM   1088 C  CZ  . PHE   A 1 140 ? 8.873   9.460  25.603 1.00 15.81 ? 140 PHE   A CZ  1 
ATOM   1089 N  N   . LEU   A 1 141 ? 15.187  5.975  26.583 1.00 15.36 ? 141 LEU   A N   1 
ATOM   1090 C  CA  . LEU   A 1 141 ? 16.629  5.745  26.616 1.00 15.92 ? 141 LEU   A CA  1 
ATOM   1091 C  C   . LEU   A 1 141 ? 17.314  6.691  25.630 1.00 16.58 ? 141 LEU   A C   1 
ATOM   1092 O  O   . LEU   A 1 141 ? 16.665  7.413  24.870 1.00 15.51 ? 141 LEU   A O   1 
ATOM   1093 C  CB  . LEU   A 1 141 ? 16.914  4.294  26.215 1.00 16.73 ? 141 LEU   A CB  1 
ATOM   1094 C  CG  . LEU   A 1 141 ? 16.210  3.199  27.017 1.00 17.82 ? 141 LEU   A CG  1 
ATOM   1095 C  CD1 . LEU   A 1 141 ? 16.444  1.894  26.420 1.00 19.66 ? 141 LEU   A CD1 1 
ATOM   1096 C  CD2 . LEU   A 1 141 ? 16.696  3.156  28.446 1.00 21.24 ? 141 LEU   A CD2 1 
ATOM   1097 N  N   . ASN   A 1 142 ? 18.659  6.667  25.640 1.00 16.35 ? 142 ASN   A N   1 
ATOM   1098 C  CA  . ASN   A 1 142 ? 19.442  7.219  24.545 1.00 18.32 ? 142 ASN   A CA  1 
ATOM   1099 C  C   . ASN   A 1 142 ? 18.907  6.752  23.191 1.00 17.63 ? 142 ASN   A C   1 
ATOM   1100 O  O   . ASN   A 1 142 ? 18.699  5.567  22.958 1.00 20.06 ? 142 ASN   A O   1 
ATOM   1101 C  CB  . ASN   A 1 142 ? 20.914  6.822  24.631 1.00 21.63 ? 142 ASN   A CB  1 
ATOM   1102 C  CG  . ASN   A 1 142 ? 21.596  7.470  25.809 1.00 29.14 ? 142 ASN   A CG  1 
ATOM   1103 O  OD1 . ASN   A 1 142 ? 21.135  8.494  26.340 1.00 30.69 ? 142 ASN   A OD1 1 
ATOM   1104 N  ND2 . ASN   A 1 142 ? 22.698  6.871  26.240 1.00 32.94 ? 142 ASN   A ND2 1 
ATOM   1105 N  N   . GLY   A 1 143 ? 18.653  7.720  22.314 1.00 17.72 ? 143 GLY   A N   1 
ATOM   1106 C  CA  . GLY   A 1 143 ? 18.223  7.462  20.949 1.00 17.33 ? 143 GLY   A CA  1 
ATOM   1107 C  C   . GLY   A 1 143 ? 16.706  7.602  20.782 1.00 16.52 ? 143 GLY   A C   1 
ATOM   1108 O  O   . GLY   A 1 143 ? 16.197  7.459  19.670 1.00 16.09 ? 143 GLY   A O   1 
ATOM   1109 N  N   . SER   A 1 144 ? 15.976  7.868  21.879 1.00 13.68 ? 144 SER   A N   1 
ATOM   1110 C  CA  . SER   A 1 144 ? 14.519  7.950  21.836 1.00 13.91 ? 144 SER   A CA  1 
ATOM   1111 C  C   . SER   A 1 144 ? 14.013  9.314  21.358 1.00 12.54 ? 144 SER   A C   1 
ATOM   1112 O  O   . SER   A 1 144 ? 12.844  9.442  21.034 1.00 12.30 ? 144 SER   A O   1 
ATOM   1113 C  CB  . SER   A 1 144 ? 13.917  7.599  23.206 1.00 13.53 ? 144 SER   A CB  1 
ATOM   1114 O  OG  . SER   A 1 144 ? 14.289  8.566  24.176 1.00 14.94 ? 144 SER   A OG  1 
ATOM   1115 N  N   . CYS   A 1 145 ? 14.862  10.361 21.362 1.00 12.37 ? 145 CYS   A N   1 
ATOM   1116 C  CA  . CYS   A 1 145 ? 14.440  11.698 20.981 1.00 12.79 ? 145 CYS   A CA  1 
ATOM   1117 C  C   . CYS   A 1 145 ? 13.777  11.697 19.602 1.00 12.59 ? 145 CYS   A C   1 
ATOM   1118 O  O   . CYS   A 1 145 ? 14.240  11.015 18.699 1.00 13.48 ? 145 CYS   A O   1 
ATOM   1119 C  CB  . CYS   A 1 145 ? 15.599  12.686 20.983 1.00 15.32 ? 145 CYS   A CB  1 
ATOM   1120 S  SG  . CYS   A 1 145 ? 16.169  13.060 22.656 1.00 17.52 ? 145 CYS   A SG  1 
ATOM   1121 N  N   . GLY   A 1 146 ? 12.699  12.488 19.483 1.00 13.33 ? 146 GLY   A N   1 
ATOM   1122 C  CA  . GLY   A 1 146 ? 11.869  12.536 18.285 1.00 13.19 ? 146 GLY   A CA  1 
ATOM   1123 C  C   . GLY   A 1 146 ? 10.720  11.517 18.289 1.00 12.60 ? 146 GLY   A C   1 
ATOM   1124 O  O   . GLY   A 1 146 ? 9.842   11.611 17.445 1.00 12.77 ? 146 GLY   A O   1 
ATOM   1125 N  N   . SER   A 1 147 ? 10.664  10.604 19.264 1.00 11.68 ? 147 SER   A N   1 
ATOM   1126 C  CA  . SER   A 1 147 ? 9.462   9.818  19.525 1.00 11.60 ? 147 SER   A CA  1 
ATOM   1127 C  C   . SER   A 1 147 ? 8.303   10.766 19.817 1.00 11.68 ? 147 SER   A C   1 
ATOM   1128 O  O   . SER   A 1 147 ? 8.506   11.838 20.392 1.00 12.00 ? 147 SER   A O   1 
ATOM   1129 C  CB  . SER   A 1 147 ? 9.677   8.853  20.678 1.00 11.34 ? 147 SER   A CB  1 
ATOM   1130 O  OG  . SER   A 1 147 ? 10.724  7.926  20.413 1.00 12.37 ? 147 SER   A OG  1 
ATOM   1131 N  N   . VAL   A 1 148 ? 7.090   10.389 19.405 1.00 11.98 ? 148 VAL   A N   1 
ATOM   1132 C  CA  . VAL   A 1 148 ? 5.953   11.278 19.532 1.00 12.94 ? 148 VAL   A CA  1 
ATOM   1133 C  C   . VAL   A 1 148 ? 4.865   10.680 20.420 1.00 13.24 ? 148 VAL   A C   1 
ATOM   1134 O  O   . VAL   A 1 148 ? 4.701   9.465  20.579 1.00 12.64 ? 148 VAL   A O   1 
ATOM   1135 C  CB  . VAL   A 1 148 ? 5.381   11.724 18.169 1.00 12.84 ? 148 VAL   A CB  1 
ATOM   1136 C  CG1 . VAL   A 1 148 ? 6.432   12.503 17.380 1.00 12.47 ? 148 VAL   A CG1 1 
ATOM   1137 C  CG2 . VAL   A 1 148 ? 4.871   10.555 17.359 1.00 12.56 ? 148 VAL   A CG2 1 
ATOM   1138 N  N   . GLY   A 1 149 ? 4.077   11.598 20.945 1.00 14.00 ? 149 GLY   A N   1 
ATOM   1139 C  CA  . GLY   A 1 149 ? 2.848   11.266 21.649 1.00 13.20 ? 149 GLY   A CA  1 
ATOM   1140 C  C   . GLY   A 1 149 ? 1.629   11.772 20.893 1.00 13.00 ? 149 GLY   A C   1 
ATOM   1141 O  O   . GLY   A 1 149 ? 1.710   12.802 20.228 1.00 11.81 ? 149 GLY   A O   1 
ATOM   1142 N  N   . PHE   A 1 150 ? 0.503   11.075 21.066 1.00 12.77 ? 150 PHE   A N   1 
ATOM   1143 C  CA  . PHE   A 1 150 ? -0.656  11.308 20.216 1.00 13.15 ? 150 PHE   A CA  1 
ATOM   1144 C  C   . PHE   A 1 150 ? -1.926  10.775 20.856 1.00 13.10 ? 150 PHE   A C   1 
ATOM   1145 O  O   . PHE   A 1 150 ? -1.892  9.922  21.742 1.00 12.35 ? 150 PHE   A O   1 
ATOM   1146 C  CB  . PHE   A 1 150 ? -0.461  10.630 18.865 1.00 13.37 ? 150 PHE   A CB  1 
ATOM   1147 C  CG  . PHE   A 1 150 ? -0.283  9.124  18.968 1.00 13.61 ? 150 PHE   A CG  1 
ATOM   1148 C  CD1 . PHE   A 1 150 ? 0.964   8.578  19.238 1.00 16.05 ? 150 PHE   A CD1 1 
ATOM   1149 C  CD2 . PHE   A 1 150 ? -1.349  8.256  18.763 1.00 14.51 ? 150 PHE   A CD2 1 
ATOM   1150 C  CE1 . PHE   A 1 150 ? 1.126   7.210  19.369 1.00 15.61 ? 150 PHE   A CE1 1 
ATOM   1151 C  CE2 . PHE   A 1 150 ? -1.175  6.887  18.867 1.00 15.44 ? 150 PHE   A CE2 1 
ATOM   1152 C  CZ  . PHE   A 1 150 ? 0.051   6.366  19.184 1.00 16.71 ? 150 PHE   A CZ  1 
ATOM   1153 N  N   . ASN   A 1 151 ? -3.046  11.349 20.409 1.00 14.85 ? 151 ASN   A N   1 
ATOM   1154 C  CA  . ASN   A 1 151 ? -4.382  10.838 20.639 1.00 15.37 ? 151 ASN   A CA  1 
ATOM   1155 C  C   . ASN   A 1 151 ? -4.972  10.508 19.277 1.00 15.91 ? 151 ASN   A C   1 
ATOM   1156 O  O   . ASN   A 1 151 ? -4.565  11.076 18.269 1.00 17.55 ? 151 ASN   A O   1 
ATOM   1157 C  CB  . ASN   A 1 151 ? -5.277  11.832 21.376 1.00 17.12 ? 151 ASN   A CB  1 
ATOM   1158 C  CG  . ASN   A 1 151 ? -4.932  11.904 22.849 1.00 20.01 ? 151 ASN   A CG  1 
ATOM   1159 O  OD1 . ASN   A 1 151 ? -5.375  11.091 23.678 1.00 24.38 ? 151 ASN   A OD1 1 
ATOM   1160 N  ND2 . ASN   A 1 151 ? -4.116  12.872 23.175 1.00 19.57 ? 151 ASN   A ND2 1 
ATOM   1161 N  N   . ILE   A 1 152 ? -5.942  9.605  19.247 1.00 18.17 ? 152 ILE   A N   1 
ATOM   1162 C  CA  . ILE   A 1 152 ? -6.675  9.326  18.020 1.00 18.37 ? 152 ILE   A CA  1 
ATOM   1163 C  C   . ILE   A 1 152 ? -8.155  9.572  18.316 1.00 23.35 ? 152 ILE   A C   1 
ATOM   1164 O  O   . ILE   A 1 152 ? -8.643  9.178  19.365 1.00 23.74 ? 152 ILE   A O   1 
ATOM   1165 C  CB  . ILE   A 1 152 ? -6.400  7.905  17.519 1.00 19.71 ? 152 ILE   A CB  1 
ATOM   1166 C  CG1 . ILE   A 1 152 ? -4.915  7.628  17.398 1.00 21.68 ? 152 ILE   A CG1 1 
ATOM   1167 C  CG2 . ILE   A 1 152 ? -7.122  7.635  16.179 1.00 25.51 ? 152 ILE   A CG2 1 
ATOM   1168 C  CD1 . ILE   A 1 152 ? -4.583  6.285  16.754 1.00 24.71 ? 152 ILE   A CD1 1 
ATOM   1169 N  N   . ASP   A 1 153 ? -8.846  10.258 17.403 1.00 25.65 ? 153 ASP   A N   1 
ATOM   1170 C  CA  . ASP   A 1 153 ? -10.293 10.438 17.440 1.00 27.28 ? 153 ASP   A CA  1 
ATOM   1171 C  C   . ASP   A 1 153 ? -10.829 9.968  16.078 1.00 25.69 ? 153 ASP   A C   1 
ATOM   1172 O  O   . ASP   A 1 153 ? -10.601 10.632 15.085 1.00 22.34 ? 153 ASP   A O   1 
ATOM   1173 C  CB  . ASP   A 1 153 ? -10.634 11.887 17.750 1.00 33.14 ? 153 ASP   A CB  1 
ATOM   1174 C  CG  . ASP   A 1 153 ? -12.118 12.232 17.833 1.00 47.91 ? 153 ASP   A CG  1 
ATOM   1175 O  OD1 . ASP   A 1 153 ? -12.875 11.845 16.906 1.00 53.26 ? 153 ASP   A OD1 1 
ATOM   1176 O  OD2 . ASP   A 1 153 ? -12.504 12.916 18.812 1.00 58.66 ? 153 ASP   A OD2 1 
ATOM   1177 N  N   A TYR   A 1 154 ? -11.542 8.828  16.059 0.50 25.36 ? 154 TYR   A N   1 
ATOM   1178 N  N   B TYR   A 1 154 ? -11.483 8.796  16.068 0.50 24.69 ? 154 TYR   A N   1 
ATOM   1179 C  CA  A TYR   A 1 154 ? -11.937 8.128  14.840 0.50 25.22 ? 154 TYR   A CA  1 
ATOM   1180 C  CA  B TYR   A 1 154 ? -11.982 8.164  14.856 0.50 24.04 ? 154 TYR   A CA  1 
ATOM   1181 C  C   A TYR   A 1 154 ? -10.723 7.948  13.937 0.50 24.03 ? 154 TYR   A C   1 
ATOM   1182 C  C   B TYR   A 1 154 ? -10.810 7.911  13.903 0.50 23.20 ? 154 TYR   A C   1 
ATOM   1183 O  O   A TYR   A 1 154 ? -9.857  7.126  14.211 0.50 25.65 ? 154 TYR   A O   1 
ATOM   1184 O  O   B TYR   A 1 154 ? -10.035 6.989  14.117 0.50 24.53 ? 154 TYR   A O   1 
ATOM   1185 C  CB  A TYR   A 1 154 ? -13.074 8.747  14.014 0.50 26.67 ? 154 TYR   A CB  1 
ATOM   1186 C  CB  B TYR   A 1 154 ? -13.188 8.993  14.388 0.50 24.62 ? 154 TYR   A CB  1 
ATOM   1187 C  CG  A TYR   A 1 154 ? -13.543 7.858  12.860 0.50 30.09 ? 154 TYR   A CG  1 
ATOM   1188 C  CG  B TYR   A 1 154 ? -14.466 8.824  15.220 0.50 26.23 ? 154 TYR   A CG  1 
ATOM   1189 C  CD1 A TYR   A 1 154 ? -13.503 6.470  12.969 0.50 33.02 ? 154 TYR   A CD1 1 
ATOM   1190 C  CD1 B TYR   A 1 154 ? -14.674 9.533  16.401 0.50 28.24 ? 154 TYR   A CD1 1 
ATOM   1191 C  CD2 A TYR   A 1 154 ? -13.991 8.395  11.652 0.50 29.99 ? 154 TYR   A CD2 1 
ATOM   1192 C  CD2 B TYR   A 1 154 ? -15.480 7.963  14.810 0.50 27.72 ? 154 TYR   A CD2 1 
ATOM   1193 C  CE1 A TYR   A 1 154 ? -13.913 5.649  11.928 0.50 32.91 ? 154 TYR   A CE1 1 
ATOM   1194 C  CE1 B TYR   A 1 154 ? -15.828 9.382  17.153 0.50 28.43 ? 154 TYR   A CE1 1 
ATOM   1195 C  CE2 A TYR   A 1 154 ? -14.406 7.584  10.610 0.50 31.48 ? 154 TYR   A CE2 1 
ATOM   1196 C  CE2 B TYR   A 1 154 ? -16.644 7.805  15.546 0.50 28.33 ? 154 TYR   A CE2 1 
ATOM   1197 C  CZ  A TYR   A 1 154 ? -14.366 6.208  10.748 0.50 34.73 ? 154 TYR   A CZ  1 
ATOM   1198 C  CZ  B TYR   A 1 154 ? -16.819 8.519  16.718 0.50 30.19 ? 154 TYR   A CZ  1 
ATOM   1199 O  OH  A TYR   A 1 154 ? -14.769 5.383  9.730  0.50 38.21 ? 154 TYR   A OH  1 
ATOM   1200 O  OH  B TYR   A 1 154 ? -17.985 8.383  17.416 0.50 30.34 ? 154 TYR   A OH  1 
ATOM   1201 N  N   . ASP   A 1 155 ? -10.666 8.712  12.848 1.00 22.57 ? 155 ASP   A N   1 
ATOM   1202 C  CA  . ASP   A 1 155 ? -9.626  8.490  11.852 1.00 27.29 ? 155 ASP   A CA  1 
ATOM   1203 C  C   . ASP   A 1 155 ? -8.474  9.499  12.007 1.00 25.33 ? 155 ASP   A C   1 
ATOM   1204 O  O   . ASP   A 1 155 ? -7.499  9.454  11.249 1.00 27.13 ? 155 ASP   A O   1 
ATOM   1205 C  CB  . ASP   A 1 155 ? -10.214 8.568  10.448 1.00 30.39 ? 155 ASP   A CB  1 
ATOM   1206 C  CG  . ASP   A 1 155 ? -10.846 9.921  10.120 1.00 34.69 ? 155 ASP   A CG  1 
ATOM   1207 O  OD1 . ASP   A 1 155 ? -11.311 10.613 11.066 1.00 35.28 ? 155 ASP   A OD1 1 
ATOM   1208 O  OD2 . ASP   A 1 155 ? -10.853 10.292 8.930  1.00 37.55 ? 155 ASP   A OD2 1 
ATOM   1209 N  N   . CYS   A 1 156 ? -8.579  10.426 12.972 1.00 21.32 ? 156 CYS   A N   1 
ATOM   1210 C  CA  . CYS   A 1 156 ? -7.721  11.589 12.989 1.00 20.08 ? 156 CYS   A CA  1 
ATOM   1211 C  C   . CYS   A 1 156 ? -6.712  11.494 14.145 1.00 20.16 ? 156 CYS   A C   1 
ATOM   1212 O  O   . CYS   A 1 156 ? -7.124  11.368 15.313 1.00 17.40 ? 156 CYS   A O   1 
ATOM   1213 C  CB  . CYS   A 1 156 ? -8.555  12.855 13.125 1.00 21.36 ? 156 CYS   A CB  1 
ATOM   1214 S  SG  . CYS   A 1 156 ? -7.541  14.351 13.152 1.00 26.08 ? 156 CYS   A SG  1 
ATOM   1215 N  N   . VAL   A 1 157 ? -5.417  11.592 13.806 1.00 17.54 ? 157 VAL   A N   1 
ATOM   1216 C  CA  . VAL   A 1 157 ? -4.335  11.530 14.787 1.00 17.80 ? 157 VAL   A CA  1 
ATOM   1217 C  C   . VAL   A 1 157 ? -4.000  12.953 15.209 1.00 16.51 ? 157 VAL   A C   1 
ATOM   1218 O  O   . VAL   A 1 157 ? -3.585  13.735 14.365 1.00 15.59 ? 157 VAL   A O   1 
ATOM   1219 C  CB  . VAL   A 1 157 ? -3.048  10.841 14.277 1.00 18.99 ? 157 VAL   A CB  1 
ATOM   1220 C  CG1 . VAL   A 1 157 ? -1.953  10.782 15.349 1.00 18.57 ? 157 VAL   A CG1 1 
ATOM   1221 C  CG2 . VAL   A 1 157 ? -3.326  9.449  13.703 1.00 18.27 ? 157 VAL   A CG2 1 
ATOM   1222 N  N   . SER   A 1 158 ? -4.192  13.282 16.500 1.00 15.02 ? 158 SER   A N   1 
ATOM   1223 C  CA  . SER   A 1 158 ? -3.768  14.546 17.076 1.00 15.19 ? 158 SER   A CA  1 
ATOM   1224 C  C   . SER   A 1 158 ? -2.404  14.347 17.737 1.00 14.81 ? 158 SER   A C   1 
ATOM   1225 O  O   . SER   A 1 158 ? -2.318  13.704 18.780 1.00 15.24 ? 158 SER   A O   1 
ATOM   1226 C  CB  . SER   A 1 158 ? -4.775  15.057 18.087 1.00 18.08 ? 158 SER   A CB  1 
ATOM   1227 O  OG  . SER   A 1 158 ? -5.918  15.512 17.380 1.00 19.36 ? 158 SER   A OG  1 
ATOM   1228 N  N   . PHE   A 1 159 ? -1.353  14.844 17.097 1.00 15.10 ? 159 PHE   A N   1 
ATOM   1229 C  CA  . PHE   A 1 159 ? -0.008  14.738 17.645 1.00 15.13 ? 159 PHE   A CA  1 
ATOM   1230 C  C   . PHE   A 1 159 ? 0.166   15.844 18.656 1.00 15.40 ? 159 PHE   A C   1 
ATOM   1231 O  O   . PHE   A 1 159 ? -0.075  16.993 18.341 1.00 16.42 ? 159 PHE   A O   1 
ATOM   1232 C  CB  . PHE   A 1 159 ? 1.071   14.872 16.566 1.00 14.53 ? 159 PHE   A CB  1 
ATOM   1233 C  CG  . PHE   A 1 159 ? 1.097   13.726 15.580 1.00 13.15 ? 159 PHE   A CG  1 
ATOM   1234 C  CD1 . PHE   A 1 159 ? 1.727   12.534 15.885 1.00 13.18 ? 159 PHE   A CD1 1 
ATOM   1235 C  CD2 . PHE   A 1 159 ? 0.536   13.877 14.317 1.00 13.82 ? 159 PHE   A CD2 1 
ATOM   1236 C  CE1 . PHE   A 1 159 ? 1.789   11.505 14.964 1.00 13.21 ? 159 PHE   A CE1 1 
ATOM   1237 C  CE2 . PHE   A 1 159 ? 0.555   12.836 13.408 1.00 13.35 ? 159 PHE   A CE2 1 
ATOM   1238 C  CZ  . PHE   A 1 159 ? 1.221   11.664 13.712 1.00 14.13 ? 159 PHE   A CZ  1 
ATOM   1239 N  N   . CYS   A 1 160 ? 0.609   15.489 19.875 1.00 16.60 ? 160 CYS   A N   1 
ATOM   1240 C  CA  . CYS   A 1 160 ? 0.692   16.486 20.913 1.00 15.12 ? 160 CYS   A CA  1 
ATOM   1241 C  C   . CYS   A 1 160 ? 2.063   16.569 21.575 1.00 13.13 ? 160 CYS   A C   1 
ATOM   1242 O  O   . CYS   A 1 160 ? 2.278   17.482 22.366 1.00 15.89 ? 160 CYS   A O   1 
ATOM   1243 C  CB  . CYS   A 1 160 ? -0.362  16.269 21.970 1.00 15.83 ? 160 CYS   A CB  1 
ATOM   1244 S  SG  . CYS   A 1 160 ? -0.235  14.681 22.827 1.00 18.45 ? 160 CYS   A SG  1 
ATOM   1245 N  N   . TYR   A 1 161 ? 2.994   15.658 21.278 1.00 11.61 ? 161 TYR   A N   1 
ATOM   1246 C  CA  . TYR   A 1 161 ? 4.240   15.612 22.053 1.00 12.39 ? 161 TYR   A CA  1 
ATOM   1247 C  C   . TYR   A 1 161 ? 5.357   15.084 21.166 1.00 12.97 ? 161 TYR   A C   1 
ATOM   1248 O  O   . TYR   A 1 161 ? 5.138   14.146 20.410 1.00 12.41 ? 161 TYR   A O   1 
ATOM   1249 C  CB  . TYR   A 1 161 ? 4.134   14.766 23.331 1.00 12.14 ? 161 TYR   A CB  1 
ATOM   1250 C  CG  . TYR   A 1 161 ? 5.415   14.594 24.148 1.00 11.80 ? 161 TYR   A CG  1 
ATOM   1251 C  CD1 . TYR   A 1 161 ? 5.742   15.495 25.146 1.00 14.08 ? 161 TYR   A CD1 1 
ATOM   1252 C  CD2 . TYR   A 1 161 ? 6.230   13.486 24.008 1.00 12.57 ? 161 TYR   A CD2 1 
ATOM   1253 C  CE1 . TYR   A 1 161 ? 6.909   15.372 25.879 1.00 12.75 ? 161 TYR   A CE1 1 
ATOM   1254 C  CE2 . TYR   A 1 161 ? 7.398   13.319 24.757 1.00 12.01 ? 161 TYR   A CE2 1 
ATOM   1255 C  CZ  . TYR   A 1 161 ? 7.721   14.267 25.705 1.00 13.39 ? 161 TYR   A CZ  1 
ATOM   1256 O  OH  . TYR   A 1 161 ? 8.839   14.149 26.474 1.00 14.19 ? 161 TYR   A OH  1 
ATOM   1257 N  N   . MET   A 1 162 ? 6.530   15.738 21.241 1.00 13.15 ? 162 MET   A N   1 
ATOM   1258 C  CA  . MET   A 1 162 ? 7.761   15.197 20.690 1.00 12.94 ? 162 MET   A CA  1 
ATOM   1259 C  C   . MET   A 1 162 ? 8.806   15.189 21.814 1.00 13.40 ? 162 MET   A C   1 
ATOM   1260 O  O   . MET   A 1 162 ? 8.935   16.168 22.562 1.00 12.94 ? 162 MET   A O   1 
ATOM   1261 C  CB  . MET   A 1 162 ? 8.260   15.988 19.473 1.00 13.77 ? 162 MET   A CB  1 
ATOM   1262 C  CG  . MET   A 1 162 ? 9.561   15.490 18.907 1.00 15.65 ? 162 MET   A CG  1 
ATOM   1263 S  SD  . MET   A 1 162 ? 10.041  16.192 17.313 1.00 20.56 ? 162 MET   A SD  1 
ATOM   1264 C  CE  . MET   A 1 162 ? 9.135   14.986 16.320 1.00 21.64 ? 162 MET   A CE  1 
ATOM   1265 N  N   . HIS   A 1 163 ? 9.484   14.037 21.957 1.00 13.07 ? 163 HIS   A N   1 
ATOM   1266 C  CA  . HIS   A 1 163 ? 10.386  13.814 23.080 1.00 12.40 ? 163 HIS   A CA  1 
ATOM   1267 C  C   . HIS   A 1 163 ? 11.758  14.458 22.829 1.00 11.84 ? 163 HIS   A C   1 
ATOM   1268 O  O   . HIS   A 1 163 ? 12.362  14.305 21.760 1.00 12.40 ? 163 HIS   A O   1 
ATOM   1269 C  CB  . HIS   A 1 163 ? 10.536  12.318 23.357 1.00 12.40 ? 163 HIS   A CB  1 
ATOM   1270 C  CG  . HIS   A 1 163 ? 11.412  12.076 24.507 1.00 11.67 ? 163 HIS   A CG  1 
ATOM   1271 N  ND1 . HIS   A 1 163 ? 11.079  12.590 25.729 1.00 11.61 ? 163 HIS   A ND1 1 
ATOM   1272 C  CD2 . HIS   A 1 163 ? 12.609  11.494 24.645 1.00 11.72 ? 163 HIS   A CD2 1 
ATOM   1273 C  CE1 . HIS   A 1 163 ? 12.051  12.297 26.579 1.00 12.47 ? 163 HIS   A CE1 1 
ATOM   1274 N  NE2 . HIS   A 1 163 ? 12.978  11.627 25.956 1.00 11.41 ? 163 HIS   A NE2 1 
ATOM   1275 N  N   . HIS   A 1 164 ? 12.276  15.131 23.873 1.00 12.75 ? 164 HIS   A N   1 
ATOM   1276 C  CA  . HIS   A 1 164 ? 13.561  15.813 23.816 1.00 12.82 ? 164 HIS   A CA  1 
ATOM   1277 C  C   . HIS   A 1 164 ? 14.529  15.422 24.940 1.00 13.39 ? 164 HIS   A C   1 
ATOM   1278 O  O   . HIS   A 1 164 ? 15.731  15.421 24.682 1.00 14.15 ? 164 HIS   A O   1 
ATOM   1279 C  CB  . HIS   A 1 164 ? 13.397  17.328 23.928 1.00 12.77 ? 164 HIS   A CB  1 
ATOM   1280 C  CG  . HIS   A 1 164 ? 12.887  17.999 22.677 1.00 13.95 ? 164 HIS   A CG  1 
ATOM   1281 N  ND1 . HIS   A 1 164 ? 11.590  17.874 22.202 1.00 15.05 ? 164 HIS   A ND1 1 
ATOM   1282 C  CD2 . HIS   A 1 164 ? 13.499  18.830 21.825 1.00 14.71 ? 164 HIS   A CD2 1 
ATOM   1283 C  CE1 . HIS   A 1 164 ? 11.469  18.591 21.074 1.00 12.96 ? 164 HIS   A CE1 1 
ATOM   1284 N  NE2 . HIS   A 1 164 ? 12.631  19.177 20.841 1.00 16.68 ? 164 HIS   A NE2 1 
ATOM   1285 N  N   . MET   A 1 165 ? 14.050  15.223 26.182 1.00 13.60 ? 165 MET   A N   1 
ATOM   1286 C  CA  . MET   A 1 165 ? 14.998  15.131 27.274 1.00 15.43 ? 165 MET   A CA  1 
ATOM   1287 C  C   . MET   A 1 165 ? 14.465  14.440 28.519 1.00 15.69 ? 165 MET   A C   1 
ATOM   1288 O  O   . MET   A 1 165 ? 13.253  14.296 28.704 1.00 16.01 ? 165 MET   A O   1 
ATOM   1289 C  CB  . MET   A 1 165 ? 15.476  16.524 27.667 1.00 17.72 ? 165 MET   A CB  1 
ATOM   1290 C  CG  . MET   A 1 165 ? 14.394  17.423 28.212 1.00 21.37 ? 165 MET   A CG  1 
ATOM   1291 S  SD  . MET   A 1 165 ? 14.941  19.148 28.334 1.00 28.99 ? 165 MET   A SD  1 
ATOM   1292 C  CE  . MET   A 1 165 ? 16.343  18.983 29.438 1.00 32.94 ? 165 MET   A CE  1 
ATOM   1293 N  N   . GLU   A 1 166 ? 15.436  14.063 29.368 1.00 15.13 ? 166 GLU   A N   1 
ATOM   1294 C  CA  . GLU   A 1 166 ? 15.187  13.405 30.640 1.00 15.56 ? 166 GLU   A CA  1 
ATOM   1295 C  C   . GLU   A 1 166 ? 15.698  14.280 31.776 1.00 16.89 ? 166 GLU   A C   1 
ATOM   1296 O  O   . GLU   A 1 166 ? 16.817  14.753 31.735 1.00 17.08 ? 166 GLU   A O   1 
ATOM   1297 C  CB  . GLU   A 1 166 ? 15.843  12.033 30.666 1.00 15.15 ? 166 GLU   A CB  1 
ATOM   1298 C  CG  . GLU   A 1 166 ? 15.513  11.263 31.941 1.00 17.41 ? 166 GLU   A CG  1 
ATOM   1299 C  CD  . GLU   A 1 166 ? 15.969  9.822  31.984 1.00 19.86 ? 166 GLU   A CD  1 
ATOM   1300 O  OE1 . GLU   A 1 166 ? 16.816  9.568  32.873 1.00 24.58 ? 166 GLU   A OE1 1 
ATOM   1301 O  OE2 . GLU   A 1 166 ? 15.509  8.970  31.177 1.00 18.70 ? 166 GLU   A OE2 1 
ATOM   1302 N  N   . LEU   A 1 167 ? 14.848  14.499 32.778 1.00 19.43 ? 167 LEU   A N   1 
ATOM   1303 C  CA  . LEU   A 1 167 ? 15.184  15.334 33.927 1.00 20.26 ? 167 LEU   A CA  1 
ATOM   1304 C  C   . LEU   A 1 167 ? 15.505  14.444 35.129 1.00 26.91 ? 167 LEU   A C   1 
ATOM   1305 O  O   . LEU   A 1 167 ? 15.204  13.241 35.120 1.00 25.11 ? 167 LEU   A O   1 
ATOM   1306 C  CB  . LEU   A 1 167 ? 13.950  16.174 34.238 1.00 21.54 ? 167 LEU   A CB  1 
ATOM   1307 C  CG  . LEU   A 1 167 ? 13.588  17.236 33.193 1.00 22.07 ? 167 LEU   A CG  1 
ATOM   1308 C  CD1 . LEU   A 1 167 ? 12.146  17.645 33.280 1.00 23.51 ? 167 LEU   A CD1 1 
ATOM   1309 C  CD2 . LEU   A 1 167 ? 14.493  18.419 33.386 1.00 23.91 ? 167 LEU   A CD2 1 
ATOM   1310 N  N   . PRO   A 1 168 ? 16.048  15.032 36.227 1.00 30.07 ? 168 PRO   A N   1 
ATOM   1311 C  CA  . PRO   A 1 168 ? 16.241  14.297 37.476 1.00 32.13 ? 168 PRO   A CA  1 
ATOM   1312 C  C   . PRO   A 1 168 ? 14.974  13.603 37.965 1.00 33.48 ? 168 PRO   A C   1 
ATOM   1313 O  O   . PRO   A 1 168 ? 13.860  14.115 37.821 1.00 34.06 ? 168 PRO   A O   1 
ATOM   1314 C  CB  . PRO   A 1 168 ? 16.710  15.404 38.457 1.00 33.25 ? 168 PRO   A CB  1 
ATOM   1315 C  CG  . PRO   A 1 168 ? 17.382  16.433 37.582 1.00 32.66 ? 168 PRO   A CG  1 
ATOM   1316 C  CD  . PRO   A 1 168 ? 16.542  16.422 36.309 1.00 30.26 ? 168 PRO   A CD  1 
ATOM   1317 N  N   . THR   A 1 169 ? 15.177  12.421 38.544 1.00 36.98 ? 169 THR   A N   1 
ATOM   1318 C  CA  . THR   A 1 169 ? 14.121  11.577 39.075 1.00 39.67 ? 169 THR   A CA  1 
ATOM   1319 C  C   . THR   A 1 169 ? 13.529  10.757 37.930 1.00 35.12 ? 169 THR   A C   1 
ATOM   1320 O  O   . THR   A 1 169 ? 12.513  10.085 38.114 1.00 34.38 ? 169 THR   A O   1 
ATOM   1321 C  CB  . THR   A 1 169 ? 13.028  12.357 39.819 1.00 46.31 ? 169 THR   A CB  1 
ATOM   1322 O  OG1 . THR   A 1 169 ? 12.276  13.070 38.842 1.00 46.28 ? 169 THR   A OG1 1 
ATOM   1323 C  CG2 . THR   A 1 169 ? 13.544  13.299 40.899 1.00 48.98 ? 169 THR   A CG2 1 
ATOM   1324 N  N   . GLY   A 1 170 ? 14.158  10.804 36.748 1.00 30.13 ? 170 GLY   A N   1 
ATOM   1325 C  CA  . GLY   A 1 170 ? 13.746  9.936  35.657 1.00 26.00 ? 170 GLY   A CA  1 
ATOM   1326 C  C   . GLY   A 1 170 ? 12.374  10.315 35.101 1.00 23.47 ? 170 GLY   A C   1 
ATOM   1327 O  O   . GLY   A 1 170 ? 11.541  9.445  34.833 1.00 29.78 ? 170 GLY   A O   1 
ATOM   1328 N  N   . VAL   A 1 171 ? 12.120  11.610 34.954 1.00 19.41 ? 171 VAL   A N   1 
ATOM   1329 C  CA  . VAL   A 1 171 ? 10.914  12.054 34.265 1.00 19.34 ? 171 VAL   A CA  1 
ATOM   1330 C  C   . VAL   A 1 171 ? 11.350  12.771 32.996 1.00 16.23 ? 171 VAL   A C   1 
ATOM   1331 O  O   . VAL   A 1 171 ? 12.528  13.007 32.840 1.00 16.39 ? 171 VAL   A O   1 
ATOM   1332 C  CB  . VAL   A 1 171 ? 10.000  12.948 35.116 1.00 21.65 ? 171 VAL   A CB  1 
ATOM   1333 C  CG1 . VAL   A 1 171 ? 9.565   12.220 36.386 1.00 25.59 ? 171 VAL   A CG1 1 
ATOM   1334 C  CG2 . VAL   A 1 171 ? 10.633  14.294 35.428 1.00 20.70 ? 171 VAL   A CG2 1 
ATOM   1335 N  N   . HIS   A 1 172 ? 10.399  13.094 32.119 1.00 14.02 ? 172 HIS   A N   1 
ATOM   1336 C  CA  . HIS   A 1 172 ? 10.713  13.453 30.748 1.00 13.85 ? 172 HIS   A CA  1 
ATOM   1337 C  C   . HIS   A 1 172 ? 10.073  14.776 30.370 1.00 13.96 ? 172 HIS   A C   1 
ATOM   1338 O  O   . HIS   A 1 172 ? 9.024   15.163 30.894 1.00 15.26 ? 172 HIS   A O   1 
ATOM   1339 C  CB  . HIS   A 1 172 ? 10.312  12.303 29.816 1.00 13.06 ? 172 HIS   A CB  1 
ATOM   1340 C  CG  . HIS   A 1 172 ? 11.087  11.087 30.196 1.00 14.13 ? 172 HIS   A CG  1 
ATOM   1341 N  ND1 . HIS   A 1 172 ? 10.555  10.032 30.925 1.00 15.03 ? 172 HIS   A ND1 1 
ATOM   1342 C  CD2 . HIS   A 1 172 ? 12.383  10.806 30.001 1.00 14.31 ? 172 HIS   A CD2 1 
ATOM   1343 C  CE1 . HIS   A 1 172 ? 11.513  9.132  31.132 1.00 15.30 ? 172 HIS   A CE1 1 
ATOM   1344 N  NE2 . HIS   A 1 172 ? 12.627  9.549  30.551 1.00 15.36 ? 172 HIS   A NE2 1 
ATOM   1345 N  N   . ALA   A 1 173 ? 10.693  15.425 29.401 1.00 13.47 ? 173 ALA   A N   1 
ATOM   1346 C  CA  . ALA   A 1 173 ? 10.215  16.708 28.915 1.00 13.71 ? 173 ALA   A CA  1 
ATOM   1347 C  C   . ALA   A 1 173 ? 10.391  16.811 27.401 1.00 12.38 ? 173 ALA   A C   1 
ATOM   1348 O  O   . ALA   A 1 173 ? 11.278  16.219 26.798 1.00 11.74 ? 173 ALA   A O   1 
ATOM   1349 C  CB  . ALA   A 1 173 ? 10.946  17.832 29.609 1.00 14.52 ? 173 ALA   A CB  1 
ATOM   1350 N  N   . GLY   A 1 174 ? 9.496   17.562 26.783 1.00 11.82 ? 174 GLY   A N   1 
ATOM   1351 C  CA  . GLY   A 1 174 ? 9.498   17.698 25.332 1.00 12.70 ? 174 GLY   A CA  1 
ATOM   1352 C  C   . GLY   A 1 174 ? 8.570   18.828 24.901 1.00 13.16 ? 174 GLY   A C   1 
ATOM   1353 O  O   . GLY   A 1 174 ? 8.160   19.615 25.736 1.00 11.96 ? 174 GLY   A O   1 
ATOM   1354 N  N   . THR   A 1 175 ? 8.267   18.873 23.585 1.00 13.13 ? 175 THR   A N   1 
ATOM   1355 C  CA  . THR   A 1 175 ? 7.627   20.001 22.951 1.00 13.27 ? 175 THR   A CA  1 
ATOM   1356 C  C   . THR   A 1 175 ? 6.319   19.532 22.343 1.00 14.20 ? 175 THR   A C   1 
ATOM   1357 O  O   . THR   A 1 175 ? 6.065   18.343 22.202 1.00 14.60 ? 175 THR   A O   1 
ATOM   1358 C  CB  . THR   A 1 175 ? 8.545   20.612 21.887 1.00 13.08 ? 175 THR   A CB  1 
ATOM   1359 O  OG1 . THR   A 1 175 ? 8.733   19.681 20.811 1.00 13.15 ? 175 THR   A OG1 1 
ATOM   1360 C  CG2 . THR   A 1 175 ? 9.883   21.057 22.466 1.00 14.03 ? 175 THR   A CG2 1 
ATOM   1361 N  N   . ASP   A 1 176 ? 5.487   20.492 21.955 1.00 16.57 ? 176 ASP   A N   1 
ATOM   1362 C  CA  . ASP   A 1 176 ? 4.452   20.227 20.983 1.00 15.87 ? 176 ASP   A CA  1 
ATOM   1363 C  C   . ASP   A 1 176 ? 5.096   20.131 19.594 1.00 16.38 ? 176 ASP   A C   1 
ATOM   1364 O  O   . ASP   A 1 176 ? 6.301   20.283 19.460 1.00 16.46 ? 176 ASP   A O   1 
ATOM   1365 C  CB  . ASP   A 1 176 ? 3.363   21.280 21.075 1.00 18.05 ? 176 ASP   A CB  1 
ATOM   1366 C  CG  . ASP   A 1 176 ? 3.768   22.713 20.756 1.00 20.95 ? 176 ASP   A CG  1 
ATOM   1367 O  OD1 . ASP   A 1 176 ? 4.735   22.894 20.003 1.00 19.09 ? 176 ASP   A OD1 1 
ATOM   1368 O  OD2 . ASP   A 1 176 ? 3.117   23.646 21.290 1.00 22.12 ? 176 ASP   A OD2 1 
ATOM   1369 N  N   . LEU   A 1 177 ? 4.273   19.911 18.561 1.00 15.17 ? 177 LEU   A N   1 
ATOM   1370 C  CA  . LEU   A 1 177 ? 4.802   19.688 17.237 1.00 17.51 ? 177 LEU   A CA  1 
ATOM   1371 C  C   . LEU   A 1 177 ? 5.139   21.015 16.556 1.00 18.79 ? 177 LEU   A C   1 
ATOM   1372 O  O   . LEU   A 1 177 ? 5.690   20.999 15.463 1.00 18.86 ? 177 LEU   A O   1 
ATOM   1373 C  CB  . LEU   A 1 177 ? 3.910   18.797 16.382 1.00 18.42 ? 177 LEU   A CB  1 
ATOM   1374 C  CG  . LEU   A 1 177 ? 4.188   17.293 16.480 1.00 19.24 ? 177 LEU   A CG  1 
ATOM   1375 C  CD1 . LEU   A 1 177 ? 5.499   16.906 15.882 1.00 20.09 ? 177 LEU   A CD1 1 
ATOM   1376 C  CD2 . LEU   A 1 177 ? 4.168   16.819 17.930 1.00 18.77 ? 177 LEU   A CD2 1 
ATOM   1377 N  N   . GLU   A 1 178 ? 4.878   22.158 17.201 1.00 19.47 ? 178 GLU   A N   1 
ATOM   1378 C  CA  . GLU   A 1 178 ? 5.435   23.416 16.729 1.00 21.55 ? 178 GLU   A CA  1 
ATOM   1379 C  C   . GLU   A 1 178 ? 6.744   23.757 17.444 1.00 19.75 ? 178 GLU   A C   1 
ATOM   1380 O  O   . GLU   A 1 178 ? 7.243   24.859 17.263 1.00 17.84 ? 178 GLU   A O   1 
ATOM   1381 C  CB  . GLU   A 1 178 ? 4.452   24.568 16.915 1.00 25.15 ? 178 GLU   A CB  1 
ATOM   1382 C  CG  . GLU   A 1 178 ? 3.087   24.291 16.298 1.00 29.15 ? 178 GLU   A CG  1 
ATOM   1383 C  CD  . GLU   A 1 178 ? 2.142   25.473 16.444 1.00 36.13 ? 178 GLU   A CD  1 
ATOM   1384 O  OE1 . GLU   A 1 178 ? 2.058   26.115 17.530 1.00 37.92 ? 178 GLU   A OE1 1 
ATOM   1385 O  OE2 . GLU   A 1 178 ? 1.489   25.736 15.420 1.00 34.32 ? 178 GLU   A OE2 1 
ATOM   1386 N  N   . GLY   A 1 179 ? 7.274   22.832 18.273 1.00 17.47 ? 179 GLY   A N   1 
ATOM   1387 C  CA  . GLY   A 1 179 ? 8.600   22.973 18.882 1.00 15.90 ? 179 GLY   A CA  1 
ATOM   1388 C  C   . GLY   A 1 179 ? 8.632   23.837 20.146 1.00 15.19 ? 179 GLY   A C   1 
ATOM   1389 O  O   . GLY   A 1 179 ? 9.715   24.179 20.648 1.00 16.42 ? 179 GLY   A O   1 
ATOM   1390 N  N   . ASN   A 1 180 ? 7.469   24.156 20.709 1.00 15.53 ? 180 ASN   A N   1 
ATOM   1391 C  CA  . ASN   A 1 180 ? 7.405   24.882 21.958 1.00 16.55 ? 180 ASN   A CA  1 
ATOM   1392 C  C   . ASN   A 1 180 ? 7.376   23.891 23.130 1.00 15.54 ? 180 ASN   A C   1 
ATOM   1393 O  O   . ASN   A 1 180 ? 6.479   23.072 23.224 1.00 13.96 ? 180 ASN   A O   1 
ATOM   1394 C  CB  . ASN   A 1 180 ? 6.183   25.786 22.038 1.00 18.94 ? 180 ASN   A CB  1 
ATOM   1395 C  CG  . ASN   A 1 180 ? 6.277   26.923 21.051 1.00 22.73 ? 180 ASN   A CG  1 
ATOM   1396 O  OD1 . ASN   A 1 180 ? 7.334   27.567 20.961 1.00 24.50 ? 180 ASN   A OD1 1 
ATOM   1397 N  ND2 . ASN   A 1 180 ? 5.249   27.094 20.234 1.00 25.15 ? 180 ASN   A ND2 1 
ATOM   1398 N  N   . PHE   A 1 181 ? 8.311   24.007 24.066 1.00 15.62 ? 181 PHE   A N   1 
ATOM   1399 C  CA  . PHE   A 1 181 ? 8.345   23.113 25.222 1.00 16.10 ? 181 PHE   A CA  1 
ATOM   1400 C  C   . PHE   A 1 181 ? 7.071   23.191 26.057 1.00 16.49 ? 181 PHE   A C   1 
ATOM   1401 O  O   . PHE   A 1 181 ? 6.466   24.239 26.183 1.00 15.85 ? 181 PHE   A O   1 
ATOM   1402 C  CB  . PHE   A 1 181 ? 9.527   23.408 26.147 1.00 15.26 ? 181 PHE   A CB  1 
ATOM   1403 C  CG  . PHE   A 1 181 ? 10.722  22.530 25.843 1.00 15.41 ? 181 PHE   A CG  1 
ATOM   1404 C  CD1 . PHE   A 1 181 ? 10.865  21.297 26.470 1.00 15.92 ? 181 PHE   A CD1 1 
ATOM   1405 C  CD2 . PHE   A 1 181 ? 11.693  22.936 24.935 1.00 15.46 ? 181 PHE   A CD2 1 
ATOM   1406 C  CE1 . PHE   A 1 181 ? 11.942  20.475 26.181 1.00 15.31 ? 181 PHE   A CE1 1 
ATOM   1407 C  CE2 . PHE   A 1 181 ? 12.766  22.105 24.651 1.00 16.23 ? 181 PHE   A CE2 1 
ATOM   1408 C  CZ  . PHE   A 1 181 ? 12.896  20.878 25.288 1.00 16.33 ? 181 PHE   A CZ  1 
ATOM   1409 N  N   . TYR   A 1 182 ? 6.658   22.045 26.609 1.00 15.17 ? 182 TYR   A N   1 
ATOM   1410 C  CA  . TYR   A 1 182 ? 5.783   22.012 27.766 1.00 16.97 ? 182 TYR   A CA  1 
ATOM   1411 C  C   . TYR   A 1 182 ? 6.620   22.353 29.000 1.00 17.86 ? 182 TYR   A C   1 
ATOM   1412 O  O   . TYR   A 1 182 ? 7.655   21.737 29.217 1.00 17.11 ? 182 TYR   A O   1 
ATOM   1413 C  CB  . TYR   A 1 182 ? 5.141   20.622 27.830 1.00 15.17 ? 182 TYR   A CB  1 
ATOM   1414 C  CG  . TYR   A 1 182 ? 4.113   20.339 26.740 1.00 15.46 ? 182 TYR   A CG  1 
ATOM   1415 C  CD1 . TYR   A 1 182 ? 2.853   20.921 26.788 1.00 15.87 ? 182 TYR   A CD1 1 
ATOM   1416 C  CD2 . TYR   A 1 182 ? 4.424   19.565 25.624 1.00 15.45 ? 182 TYR   A CD2 1 
ATOM   1417 C  CE1 . TYR   A 1 182 ? 1.907   20.676 25.803 1.00 16.08 ? 182 TYR   A CE1 1 
ATOM   1418 C  CE2 . TYR   A 1 182 ? 3.496   19.327 24.631 1.00 16.20 ? 182 TYR   A CE2 1 
ATOM   1419 C  CZ  . TYR   A 1 182 ? 2.237   19.883 24.721 1.00 15.23 ? 182 TYR   A CZ  1 
ATOM   1420 O  OH  . TYR   A 1 182 ? 1.313   19.599 23.777 1.00 15.76 ? 182 TYR   A OH  1 
ATOM   1421 N  N   . GLY   A 1 183 ? 6.167   23.344 29.786 1.00 19.87 ? 183 GLY   A N   1 
ATOM   1422 C  CA  . GLY   A 1 183 ? 6.877   23.746 30.982 1.00 20.02 ? 183 GLY   A CA  1 
ATOM   1423 C  C   . GLY   A 1 183 ? 8.076   24.656 30.707 1.00 21.14 ? 183 GLY   A C   1 
ATOM   1424 O  O   . GLY   A 1 183 ? 8.409   25.025 29.578 1.00 18.06 ? 183 GLY   A O   1 
ATOM   1425 N  N   . PRO   A 1 184 ? 8.829   24.999 31.766 1.00 22.26 ? 184 PRO   A N   1 
ATOM   1426 C  CA  . PRO   A 1 184 ? 9.911   25.977 31.632 1.00 24.91 ? 184 PRO   A CA  1 
ATOM   1427 C  C   . PRO   A 1 184 ? 11.249  25.485 31.068 1.00 25.48 ? 184 PRO   A C   1 
ATOM   1428 O  O   . PRO   A 1 184 ? 12.267  26.144 31.215 1.00 30.92 ? 184 PRO   A O   1 
ATOM   1429 C  CB  . PRO   A 1 184 ? 10.038  26.441 33.107 1.00 25.00 ? 184 PRO   A CB  1 
ATOM   1430 C  CG  . PRO   A 1 184 ? 9.722   25.200 33.926 1.00 24.60 ? 184 PRO   A CG  1 
ATOM   1431 C  CD  . PRO   A 1 184 ? 8.616   24.508 33.137 1.00 23.06 ? 184 PRO   A CD  1 
ATOM   1432 N  N   . PHE   A 1 185 ? 11.250  24.353 30.379 1.00 22.23 ? 185 PHE   A N   1 
ATOM   1433 C  CA  . PHE   A 1 185 ? 12.479  23.660 30.047 1.00 20.14 ? 185 PHE   A CA  1 
ATOM   1434 C  C   . PHE   A 1 185 ? 13.039  24.214 28.736 1.00 20.72 ? 185 PHE   A C   1 
ATOM   1435 O  O   . PHE   A 1 185 ? 12.327  24.884 27.972 1.00 21.33 ? 185 PHE   A O   1 
ATOM   1436 C  CB  . PHE   A 1 185 ? 12.277  22.146 29.986 1.00 19.78 ? 185 PHE   A CB  1 
ATOM   1437 C  CG  . PHE   A 1 185 ? 11.572  21.672 31.247 1.00 19.92 ? 185 PHE   A CG  1 
ATOM   1438 C  CD1 . PHE   A 1 185 ? 12.194  21.773 32.483 1.00 18.57 ? 185 PHE   A CD1 1 
ATOM   1439 C  CD2 . PHE   A 1 185 ? 10.264  21.186 31.191 1.00 18.32 ? 185 PHE   A CD2 1 
ATOM   1440 C  CE1 . PHE   A 1 185 ? 11.526  21.366 33.641 1.00 21.17 ? 185 PHE   A CE1 1 
ATOM   1441 C  CE2 . PHE   A 1 185 ? 9.599   20.804 32.353 1.00 18.70 ? 185 PHE   A CE2 1 
ATOM   1442 C  CZ  . PHE   A 1 185 ? 10.225  20.907 33.582 1.00 19.47 ? 185 PHE   A CZ  1 
ATOM   1443 N  N   . VAL   A 1 186 ? 14.351  23.969 28.573 1.00 19.33 ? 186 VAL   A N   1 
ATOM   1444 C  CA  . VAL   A 1 186 ? 15.140  24.363 27.411 1.00 18.28 ? 186 VAL   A CA  1 
ATOM   1445 C  C   . VAL   A 1 186 ? 15.929  23.139 26.956 1.00 17.54 ? 186 VAL   A C   1 
ATOM   1446 O  O   . VAL   A 1 186 ? 16.286  22.248 27.757 1.00 15.47 ? 186 VAL   A O   1 
ATOM   1447 C  CB  . VAL   A 1 186 ? 16.058  25.572 27.708 1.00 21.24 ? 186 VAL   A CB  1 
ATOM   1448 C  CG1 . VAL   A 1 186 ? 15.279  26.849 27.997 1.00 21.94 ? 186 VAL   A CG1 1 
ATOM   1449 C  CG2 . VAL   A 1 186 ? 17.002  25.302 28.863 1.00 22.10 ? 186 VAL   A CG2 1 
ATOM   1450 N  N   . ASP   A 1 187 ? 16.172  23.081 25.634 1.00 17.37 ? 187 ASP   A N   1 
ATOM   1451 C  CA  . ASP   A 1 187 ? 16.930  22.015 25.001 1.00 17.33 ? 187 ASP   A CA  1 
ATOM   1452 C  C   . ASP   A 1 187 ? 18.431  22.298 25.104 1.00 18.47 ? 187 ASP   A C   1 
ATOM   1453 O  O   . ASP   A 1 187 ? 19.135  22.585 24.123 1.00 20.14 ? 187 ASP   A O   1 
ATOM   1454 C  CB  . ASP   A 1 187 ? 16.433  21.728 23.593 1.00 18.16 ? 187 ASP   A CB  1 
ATOM   1455 C  CG  . ASP   A 1 187 ? 16.402  22.891 22.610 1.00 20.11 ? 187 ASP   A CG  1 
ATOM   1456 O  OD1 . ASP   A 1 187 ? 16.471  24.064 23.057 1.00 20.12 ? 187 ASP   A OD1 1 
ATOM   1457 O  OD2 . ASP   A 1 187 ? 16.261  22.614 21.389 1.00 19.76 ? 187 ASP   A OD2 1 
ATOM   1458 N  N   . ARG   A 1 188 ? 18.938  22.143 26.312 1.00 17.05 ? 188 ARG   A N   1 
ATOM   1459 C  CA  . ARG   A 1 188 ? 20.354  22.255 26.544 1.00 20.79 ? 188 ARG   A CA  1 
ATOM   1460 C  C   . ARG   A 1 188 ? 20.685  21.423 27.754 1.00 20.55 ? 188 ARG   A C   1 
ATOM   1461 O  O   . ARG   A 1 188 ? 19.888  21.328 28.675 1.00 18.81 ? 188 ARG   A O   1 
ATOM   1462 C  CB  . ARG   A 1 188 ? 20.912  23.679 26.720 1.00 26.33 ? 188 ARG   A CB  1 
ATOM   1463 C  CG  . ARG   A 1 188 ? 20.249  24.611 27.710 1.00 36.03 ? 188 ARG   A CG  1 
ATOM   1464 C  CD  . ARG   A 1 188 ? 20.883  26.027 27.707 1.00 42.93 ? 188 ARG   A CD  1 
ATOM   1465 N  NE  . ARG   A 1 188 ? 22.283  25.974 28.152 1.00 52.91 ? 188 ARG   A NE  1 
ATOM   1466 C  CZ  . ARG   A 1 188 ? 22.870  26.735 29.077 1.00 50.41 ? 188 ARG   A CZ  1 
ATOM   1467 N  NH1 . ARG   A 1 188 ? 24.141  26.534 29.371 1.00 48.96 ? 188 ARG   A NH1 1 
ATOM   1468 N  NH2 . ARG   A 1 188 ? 22.191  27.689 29.691 1.00 52.72 ? 188 ARG   A NH2 1 
ATOM   1469 N  N   . GLN   A 1 189 ? 21.895  20.877 27.741 1.00 21.68 ? 189 GLN   A N   1 
ATOM   1470 C  CA  . GLN   A 1 189 ? 22.352  20.061 28.842 1.00 21.75 ? 189 GLN   A CA  1 
ATOM   1471 C  C   . GLN   A 1 189 ? 22.897  20.953 29.948 1.00 24.60 ? 189 GLN   A C   1 
ATOM   1472 O  O   . GLN   A 1 189 ? 24.096  21.210 30.008 1.00 29.19 ? 189 GLN   A O   1 
ATOM   1473 C  CB  . GLN   A 1 189 ? 23.354  19.034 28.357 1.00 22.48 ? 189 GLN   A CB  1 
ATOM   1474 C  CG  . GLN   A 1 189 ? 23.737  18.051 29.455 1.00 20.81 ? 189 GLN   A CG  1 
ATOM   1475 C  CD  . GLN   A 1 189 ? 24.647  16.972 28.949 1.00 22.07 ? 189 GLN   A CD  1 
ATOM   1476 O  OE1 . GLN   A 1 189 ? 24.425  16.358 27.900 1.00 26.35 ? 189 GLN   A OE1 1 
ATOM   1477 N  NE2 . GLN   A 1 189 ? 25.682  16.716 29.728 1.00 22.39 ? 189 GLN   A NE2 1 
ATOM   1478 N  N   . THR   A 1 190 ? 21.985  21.363 30.819 1.00 27.15 ? 190 THR   A N   1 
ATOM   1479 C  CA  . THR   A 1 190 ? 22.215  22.315 31.901 1.00 32.56 ? 190 THR   A CA  1 
ATOM   1480 C  C   . THR   A 1 190 ? 21.293  21.896 33.042 1.00 32.07 ? 190 THR   A C   1 
ATOM   1481 O  O   . THR   A 1 190 ? 20.337  21.174 32.798 1.00 28.54 ? 190 THR   A O   1 
ATOM   1482 C  CB  . THR   A 1 190 ? 21.910  23.749 31.452 1.00 31.08 ? 190 THR   A CB  1 
ATOM   1483 O  OG1 . THR   A 1 190 ? 22.343  24.550 32.541 1.00 39.99 ? 190 THR   A OG1 1 
ATOM   1484 C  CG2 . THR   A 1 190 ? 20.437  24.054 31.280 1.00 30.79 ? 190 THR   A CG2 1 
ATOM   1485 N  N   . ALA   A 1 191 ? 21.543  22.416 34.249 1.00 35.57 ? 191 ALA   A N   1 
ATOM   1486 C  CA  . ALA   A 1 191 ? 20.816  21.997 35.438 1.00 33.86 ? 191 ALA   A CA  1 
ATOM   1487 C  C   . ALA   A 1 191 ? 19.384  22.483 35.331 1.00 29.67 ? 191 ALA   A C   1 
ATOM   1488 O  O   . ALA   A 1 191 ? 19.132  23.674 35.220 1.00 30.80 ? 191 ALA   A O   1 
ATOM   1489 C  CB  . ALA   A 1 191 ? 21.485  22.514 36.704 1.00 33.75 ? 191 ALA   A CB  1 
ATOM   1490 N  N   . GLN   A 1 192 ? 18.447  21.533 35.285 1.00 30.85 ? 192 GLN   A N   1 
ATOM   1491 C  CA  . GLN   A 1 192 ? 17.038  21.850 35.203 1.00 25.88 ? 192 GLN   A CA  1 
ATOM   1492 C  C   . GLN   A 1 192 ? 16.302  20.863 36.092 1.00 27.08 ? 192 GLN   A C   1 
ATOM   1493 O  O   . GLN   A 1 192 ? 16.637  19.684 36.116 1.00 27.28 ? 192 GLN   A O   1 
ATOM   1494 C  CB  . GLN   A 1 192 ? 16.510  21.728 33.769 1.00 25.56 ? 192 GLN   A CB  1 
ATOM   1495 C  CG  . GLN   A 1 192 ? 17.186  22.652 32.769 1.00 24.50 ? 192 GLN   A CG  1 
ATOM   1496 C  CD  . GLN   A 1 192 ? 16.645  22.514 31.360 1.00 23.79 ? 192 GLN   A CD  1 
ATOM   1497 O  OE1 . GLN   A 1 192 ? 15.542  22.988 31.063 1.00 22.70 ? 192 GLN   A OE1 1 
ATOM   1498 N  NE2 . GLN   A 1 192 ? 17.457  21.965 30.456 1.00 23.83 ? 192 GLN   A NE2 1 
ATOM   1499 N  N   . ALA   A 1 193 ? 15.316  21.354 36.838 1.00 28.96 ? 193 ALA   A N   1 
ATOM   1500 C  CA  . ALA   A 1 193 ? 14.486  20.468 37.631 1.00 29.45 ? 193 ALA   A CA  1 
ATOM   1501 C  C   . ALA   A 1 193 ? 13.016  20.798 37.419 1.00 28.21 ? 193 ALA   A C   1 
ATOM   1502 O  O   . ALA   A 1 193 ? 12.651  21.949 37.223 1.00 27.44 ? 193 ALA   A O   1 
ATOM   1503 C  CB  . ALA   A 1 193 ? 14.857  20.534 39.086 1.00 32.12 ? 193 ALA   A CB  1 
ATOM   1504 N  N   . ALA   A 1 194 ? 12.186  19.752 37.433 1.00 30.50 ? 194 ALA   A N   1 
ATOM   1505 C  CA  . ALA   A 1 194 ? 10.740  19.929 37.422 1.00 30.57 ? 194 ALA   A CA  1 
ATOM   1506 C  C   . ALA   A 1 194 ? 10.296  20.607 38.719 1.00 33.78 ? 194 ALA   A C   1 
ATOM   1507 O  O   . ALA   A 1 194 ? 10.913  20.380 39.751 1.00 31.26 ? 194 ALA   A O   1 
ATOM   1508 C  CB  . ALA   A 1 194 ? 10.104  18.585 37.275 1.00 32.47 ? 194 ALA   A CB  1 
ATOM   1509 N  N   . GLY   A 1 195 ? 9.264   21.460 38.647 1.00 33.61 ? 195 GLY   A N   1 
ATOM   1510 C  CA  . GLY   A 1 195 ? 8.528   21.911 39.819 1.00 34.11 ? 195 GLY   A CA  1 
ATOM   1511 C  C   . GLY   A 1 195 ? 7.910   20.729 40.571 1.00 31.34 ? 195 GLY   A C   1 
ATOM   1512 O  O   . GLY   A 1 195 ? 7.910   19.602 40.084 1.00 25.09 ? 195 GLY   A O   1 
ATOM   1513 N  N   . THR   A 1 196 ? 7.453   20.978 41.806 1.00 32.00 ? 196 THR   A N   1 
ATOM   1514 C  CA  . THR   A 1 196 ? 6.788   19.956 42.592 1.00 32.14 ? 196 THR   A CA  1 
ATOM   1515 C  C   . THR   A 1 196 ? 5.546   19.583 41.803 1.00 28.23 ? 196 THR   A C   1 
ATOM   1516 O  O   . THR   A 1 196 ? 4.929   20.462 41.214 1.00 27.10 ? 196 THR   A O   1 
ATOM   1517 C  CB  . THR   A 1 196 ? 6.401   20.439 43.987 1.00 39.89 ? 196 THR   A CB  1 
ATOM   1518 O  OG1 . THR   A 1 196 ? 7.594   20.958 44.579 1.00 42.73 ? 196 THR   A OG1 1 
ATOM   1519 C  CG2 . THR   A 1 196 ? 5.833   19.303 44.825 1.00 38.29 ? 196 THR   A CG2 1 
ATOM   1520 N  N   . ASP   A 1 197 ? 5.237   18.285 41.767 1.00 27.82 ? 197 ASP   A N   1 
ATOM   1521 C  CA  . ASP   A 1 197 ? 4.074   17.814 41.035 1.00 28.50 ? 197 ASP   A CA  1 
ATOM   1522 C  C   . ASP   A 1 197 ? 2.849   17.854 41.955 1.00 29.89 ? 197 ASP   A C   1 
ATOM   1523 O  O   . ASP   A 1 197 ? 2.980   18.117 43.160 1.00 28.06 ? 197 ASP   A O   1 
ATOM   1524 C  CB  . ASP   A 1 197 ? 4.304   16.423 40.461 1.00 26.71 ? 197 ASP   A CB  1 
ATOM   1525 C  CG  . ASP   A 1 197 ? 3.463   16.113 39.224 1.00 27.30 ? 197 ASP   A CG  1 
ATOM   1526 O  OD1 . ASP   A 1 197 ? 2.939   17.089 38.600 1.00 24.41 ? 197 ASP   A OD1 1 
ATOM   1527 O  OD2 . ASP   A 1 197 ? 3.349   14.911 38.881 1.00 25.33 ? 197 ASP   A OD2 1 
ATOM   1528 N  N   . THR   A 1 198 ? 1.663   17.720 41.336 1.00 23.92 ? 198 THR   A N   1 
ATOM   1529 C  CA  . THR   A 1 198 ? 0.369   17.696 42.005 1.00 23.73 ? 198 THR   A CA  1 
ATOM   1530 C  C   . THR   A 1 198 ? -0.423  16.495 41.492 1.00 21.11 ? 198 THR   A C   1 
ATOM   1531 O  O   . THR   A 1 198 ? -0.165  16.066 40.383 1.00 18.97 ? 198 THR   A O   1 
ATOM   1532 C  CB  . THR   A 1 198 ? -0.370  18.989 41.654 1.00 28.31 ? 198 THR   A CB  1 
ATOM   1533 O  OG1 . THR   A 1 198 ? 0.518   20.006 42.093 1.00 36.25 ? 198 THR   A OG1 1 
ATOM   1534 C  CG2 . THR   A 1 198 ? -1.653  19.181 42.439 1.00 29.90 ? 198 THR   A CG2 1 
ATOM   1535 N  N   . THR   A 1 199 ? -1.406  15.997 42.255 1.00 16.86 ? 199 THR   A N   1 
ATOM   1536 C  CA  . THR   A 1 199 ? -2.278  14.922 41.789 1.00 17.84 ? 199 THR   A CA  1 
ATOM   1537 C  C   . THR   A 1 199 ? -3.433  15.515 40.987 1.00 16.65 ? 199 THR   A C   1 
ATOM   1538 O  O   . THR   A 1 199 ? -4.052  16.504 41.386 1.00 16.45 ? 199 THR   A O   1 
ATOM   1539 C  CB  . THR   A 1 199 ? -2.787  14.087 42.964 1.00 18.97 ? 199 THR   A CB  1 
ATOM   1540 O  OG1 . THR   A 1 199 ? -1.623  13.574 43.609 1.00 16.38 ? 199 THR   A OG1 1 
ATOM   1541 C  CG2 . THR   A 1 199 ? -3.716  12.961 42.530 1.00 19.47 ? 199 THR   A CG2 1 
ATOM   1542 N  N   . ILE   A 1 200 ? -3.737  14.888 39.849 1.00 15.87 ? 200 ILE   A N   1 
ATOM   1543 C  CA  . ILE   A 1 200 ? -4.788  15.370 38.961 1.00 15.62 ? 200 ILE   A CA  1 
ATOM   1544 C  C   . ILE   A 1 200 ? -6.134  14.850 39.482 1.00 14.83 ? 200 ILE   A C   1 
ATOM   1545 O  O   . ILE   A 1 200 ? -6.582  13.751 39.152 1.00 13.87 ? 200 ILE   A O   1 
ATOM   1546 C  CB  . ILE   A 1 200 ? -4.531  14.946 37.495 1.00 15.28 ? 200 ILE   A CB  1 
ATOM   1547 C  CG1 . ILE   A 1 200 ? -3.128  15.253 37.004 1.00 15.45 ? 200 ILE   A CG1 1 
ATOM   1548 C  CG2 . ILE   A 1 200 ? -5.590  15.528 36.569 1.00 15.97 ? 200 ILE   A CG2 1 
ATOM   1549 C  CD1 . ILE   A 1 200 ? -2.619  14.225 35.996 1.00 14.98 ? 200 ILE   A CD1 1 
ATOM   1550 N  N   . THR   A 1 201 ? -6.793  15.669 40.297 1.00 13.56 ? 201 THR   A N   1 
ATOM   1551 C  CA  . THR   A 1 201 ? -8.013  15.323 40.994 1.00 13.61 ? 201 THR   A CA  1 
ATOM   1552 C  C   . THR   A 1 201 ? -9.113  14.790 40.075 1.00 13.37 ? 201 THR   A C   1 
ATOM   1553 O  O   . THR   A 1 201 ? -9.785  13.825 40.412 1.00 13.09 ? 201 THR   A O   1 
ATOM   1554 C  CB  . THR   A 1 201 ? -8.495  16.597 41.708 1.00 15.48 ? 201 THR   A CB  1 
ATOM   1555 O  OG1 . THR   A 1 201 ? -7.372  17.030 42.479 1.00 15.04 ? 201 THR   A OG1 1 
ATOM   1556 C  CG2 . THR   A 1 201 ? -9.692  16.337 42.601 1.00 15.37 ? 201 THR   A CG2 1 
ATOM   1557 N  N   . VAL   A 1 202 ? -9.388  15.481 38.974 1.00 12.21 ? 202 VAL   A N   1 
ATOM   1558 C  CA  . VAL   A 1 202 ? -10.482 15.081 38.101 1.00 13.64 ? 202 VAL   A CA  1 
ATOM   1559 C  C   . VAL   A 1 202 ? -10.259 13.652 37.579 1.00 12.35 ? 202 VAL   A C   1 
ATOM   1560 O  O   . VAL   A 1 202 ? -11.198 12.893 37.404 1.00 12.64 ? 202 VAL   A O   1 
ATOM   1561 C  CB  . VAL   A 1 202 ? -10.741 16.110 36.980 1.00 14.10 ? 202 VAL   A CB  1 
ATOM   1562 C  CG1 . VAL   A 1 202 ? -9.604  16.233 35.977 1.00 14.97 ? 202 VAL   A CG1 1 
ATOM   1563 C  CG2 . VAL   A 1 202 ? -12.053 15.778 36.249 1.00 15.58 ? 202 VAL   A CG2 1 
ATOM   1564 N  N   . ASN   A 1 203 ? -9.019  13.285 37.293 1.00 12.72 ? 203 ASN   A N   1 
ATOM   1565 C  CA  . ASN   A 1 203 ? -8.684  11.949 36.809 1.00 13.34 ? 203 ASN   A CA  1 
ATOM   1566 C  C   . ASN   A 1 203 ? -8.859  10.904 37.905 1.00 13.62 ? 203 ASN   A C   1 
ATOM   1567 O  O   . ASN   A 1 203 ? -9.264  9.776  37.638 1.00 13.40 ? 203 ASN   A O   1 
ATOM   1568 C  CB  . ASN   A 1 203 ? -7.253  11.858 36.276 1.00 14.76 ? 203 ASN   A CB  1 
ATOM   1569 C  CG  . ASN   A 1 203 ? -6.997  12.665 35.019 1.00 13.93 ? 203 ASN   A CG  1 
ATOM   1570 O  OD1 . ASN   A 1 203 ? -5.876  12.586 34.476 1.00 15.91 ? 203 ASN   A OD1 1 
ATOM   1571 N  ND2 . ASN   A 1 203 ? -7.998  13.353 34.487 1.00 11.31 ? 203 ASN   A ND2 1 
ATOM   1572 N  N   . VAL   A 1 204 ? -8.502  11.242 39.149 1.00 13.14 ? 204 VAL   A N   1 
ATOM   1573 C  CA  . VAL   A 1 204 ? -8.746  10.323 40.253 1.00 11.94 ? 204 VAL   A CA  1 
ATOM   1574 C  C   . VAL   A 1 204 ? -10.239 10.018 40.339 1.00 11.39 ? 204 VAL   A C   1 
ATOM   1575 O  O   . VAL   A 1 204 ? -10.591 8.863  40.525 1.00 11.47 ? 204 VAL   A O   1 
ATOM   1576 C  CB  . VAL   A 1 204 ? -8.225  10.838 41.605 1.00 12.29 ? 204 VAL   A CB  1 
ATOM   1577 C  CG1 . VAL   A 1 204 ? -8.563  9.876  42.736 1.00 12.39 ? 204 VAL   A CG1 1 
ATOM   1578 C  CG2 . VAL   A 1 204 ? -6.730  11.094 41.559 1.00 13.00 ? 204 VAL   A CG2 1 
ATOM   1579 N  N   . LEU   A 1 205 ? -11.102 11.049 40.268 1.00 10.81 ? 205 LEU   A N   1 
ATOM   1580 C  CA  . LEU   A 1 205 ? -12.545 10.865 40.345 1.00 11.52 ? 205 LEU   A CA  1 
ATOM   1581 C  C   . LEU   A 1 205 ? -13.038 9.995  39.175 1.00 12.04 ? 205 LEU   A C   1 
ATOM   1582 O  O   . LEU   A 1 205 ? -13.844 9.076  39.376 1.00 13.00 ? 205 LEU   A O   1 
ATOM   1583 C  CB  . LEU   A 1 205 ? -13.148 12.264 40.370 1.00 12.27 ? 205 LEU   A CB  1 
ATOM   1584 C  CG  . LEU   A 1 205 ? -13.009 13.036 41.696 1.00 13.50 ? 205 LEU   A CG  1 
ATOM   1585 C  CD1 . LEU   A 1 205 ? -13.385 14.494 41.495 1.00 14.14 ? 205 LEU   A CD1 1 
ATOM   1586 C  CD2 . LEU   A 1 205 ? -13.832 12.417 42.811 1.00 14.07 ? 205 LEU   A CD2 1 
ATOM   1587 N  N   . ALA   A 1 206 ? -12.510 10.274 37.968 1.00 11.79 ? 206 ALA   A N   1 
ATOM   1588 C  CA  . ALA   A 1 206 ? -12.819 9.462  36.793 1.00 12.30 ? 206 ALA   A CA  1 
ATOM   1589 C  C   . ALA   A 1 206 ? -12.563 7.967  37.071 1.00 13.54 ? 206 ALA   A C   1 
ATOM   1590 O  O   . ALA   A 1 206 ? -13.387 7.117  36.773 1.00 12.59 ? 206 ALA   A O   1 
ATOM   1591 C  CB  . ALA   A 1 206 ? -12.035 9.934  35.596 1.00 12.60 ? 206 ALA   A CB  1 
ATOM   1592 N  N   . TRP   A 1 207 ? -11.383 7.670  37.632 1.00 13.39 ? 207 TRP   A N   1 
ATOM   1593 C  CA  . TRP   A 1 207 ? -10.970 6.322  37.932 1.00 13.42 ? 207 TRP   A CA  1 
ATOM   1594 C  C   . TRP   A 1 207 ? -11.828 5.690  39.032 1.00 12.95 ? 207 TRP   A C   1 
ATOM   1595 O  O   . TRP   A 1 207 ? -12.067 4.486  39.006 1.00 12.38 ? 207 TRP   A O   1 
ATOM   1596 C  CB  . TRP   A 1 207 ? -9.468  6.351  38.272 1.00 14.26 ? 207 TRP   A CB  1 
ATOM   1597 C  CG  . TRP   A 1 207 ? -8.855  5.070  38.761 1.00 15.44 ? 207 TRP   A CG  1 
ATOM   1598 C  CD1 . TRP   A 1 207 ? -8.373  4.018  38.027 1.00 16.52 ? 207 TRP   A CD1 1 
ATOM   1599 C  CD2 . TRP   A 1 207 ? -8.512  4.786  40.137 1.00 15.38 ? 207 TRP   A CD2 1 
ATOM   1600 N  NE1 . TRP   A 1 207 ? -7.828  3.069  38.864 1.00 17.47 ? 207 TRP   A NE1 1 
ATOM   1601 C  CE2 . TRP   A 1 207 ? -7.871  3.524  40.156 1.00 17.50 ? 207 TRP   A CE2 1 
ATOM   1602 C  CE3 . TRP   A 1 207 ? -8.713  5.456  41.339 1.00 17.79 ? 207 TRP   A CE3 1 
ATOM   1603 C  CZ2 . TRP   A 1 207 ? -7.401  2.941  41.339 1.00 17.31 ? 207 TRP   A CZ2 1 
ATOM   1604 C  CZ3 . TRP   A 1 207 ? -8.241  4.884  42.506 1.00 18.88 ? 207 TRP   A CZ3 1 
ATOM   1605 C  CH2 . TRP   A 1 207 ? -7.621  3.635  42.503 1.00 18.00 ? 207 TRP   A CH2 1 
ATOM   1606 N  N   . LEU   A 1 208 ? -12.262 6.465  40.028 1.00 12.11 ? 208 LEU   A N   1 
ATOM   1607 C  CA  . LEU   A 1 208 ? -13.212 5.956  41.000 1.00 11.91 ? 208 LEU   A CA  1 
ATOM   1608 C  C   . LEU   A 1 208 ? -14.537 5.572  40.337 1.00 12.20 ? 208 LEU   A C   1 
ATOM   1609 O  O   . LEU   A 1 208 ? -15.125 4.570  40.712 1.00 12.81 ? 208 LEU   A O   1 
ATOM   1610 C  CB  . LEU   A 1 208 ? -13.403 6.974  42.120 1.00 12.27 ? 208 LEU   A CB  1 
ATOM   1611 C  CG  . LEU   A 1 208 ? -12.194 7.201  43.023 1.00 12.43 ? 208 LEU   A CG  1 
ATOM   1612 C  CD1 . LEU   A 1 208 ? -12.585 8.254  44.059 1.00 12.82 ? 208 LEU   A CD1 1 
ATOM   1613 C  CD2 . LEU   A 1 208 ? -11.702 5.948  43.718 1.00 13.53 ? 208 LEU   A CD2 1 
ATOM   1614 N  N   . TYR   A 1 209 ? -14.999 6.334  39.344 1.00 12.47 ? 209 TYR   A N   1 
ATOM   1615 C  CA  . TYR   A 1 209 ? -16.180 5.954  38.564 1.00 12.35 ? 209 TYR   A CA  1 
ATOM   1616 C  C   . TYR   A 1 209 ? -15.918 4.638  37.830 1.00 13.04 ? 209 TYR   A C   1 
ATOM   1617 O  O   . TYR   A 1 209 ? -16.777 3.758  37.814 1.00 13.14 ? 209 TYR   A O   1 
ATOM   1618 C  CB  . TYR   A 1 209 ? -16.648 7.043  37.587 1.00 11.95 ? 209 TYR   A CB  1 
ATOM   1619 C  CG  . TYR   A 1 209 ? -17.426 8.158  38.273 1.00 12.34 ? 209 TYR   A CG  1 
ATOM   1620 C  CD1 . TYR   A 1 209 ? -18.751 7.977  38.676 1.00 13.78 ? 209 TYR   A CD1 1 
ATOM   1621 C  CD2 . TYR   A 1 209 ? -16.855 9.388  38.541 1.00 13.41 ? 209 TYR   A CD2 1 
ATOM   1622 C  CE1 . TYR   A 1 209 ? -19.466 8.987  39.309 1.00 12.41 ? 209 TYR   A CE1 1 
ATOM   1623 C  CE2 . TYR   A 1 209 ? -17.583 10.423 39.122 1.00 14.42 ? 209 TYR   A CE2 1 
ATOM   1624 C  CZ  . TYR   A 1 209 ? -18.900 10.231 39.497 1.00 13.18 ? 209 TYR   A CZ  1 
ATOM   1625 O  OH  . TYR   A 1 209 ? -19.591 11.215 40.171 1.00 14.35 ? 209 TYR   A OH  1 
ATOM   1626 N  N   . ALA   A 1 210 ? -14.755 4.521  37.203 1.00 13.77 ? 210 ALA   A N   1 
ATOM   1627 C  CA  . ALA   A 1 210 ? -14.346 3.273  36.560 1.00 14.62 ? 210 ALA   A CA  1 
ATOM   1628 C  C   . ALA   A 1 210 ? -14.429 2.088  37.521 1.00 13.97 ? 210 ALA   A C   1 
ATOM   1629 O  O   . ALA   A 1 210 ? -14.862 1.018  37.147 1.00 15.19 ? 210 ALA   A O   1 
ATOM   1630 C  CB  . ALA   A 1 210 ? -12.961 3.435  35.980 1.00 15.63 ? 210 ALA   A CB  1 
ATOM   1631 N  N   . ALA   A 1 211 ? -14.019 2.271  38.774 1.00 14.56 ? 211 ALA   A N   1 
ATOM   1632 C  CA  . ALA   A 1 211 ? -14.083 1.227  39.787 1.00 13.89 ? 211 ALA   A CA  1 
ATOM   1633 C  C   . ALA   A 1 211 ? -15.525 0.791  40.073 1.00 15.74 ? 211 ALA   A C   1 
ATOM   1634 O  O   . ALA   A 1 211 ? -15.819 -0.418 40.101 1.00 13.56 ? 211 ALA   A O   1 
ATOM   1635 C  CB  . ALA   A 1 211 ? -13.418 1.737  41.053 1.00 14.33 ? 211 ALA   A CB  1 
ATOM   1636 N  N   . VAL   A 1 212 ? -16.420 1.777  40.267 1.00 15.85 ? 212 VAL   A N   1 
ATOM   1637 C  CA  . VAL   A 1 212 ? -17.840 1.512  40.469 1.00 15.11 ? 212 VAL   A CA  1 
ATOM   1638 C  C   . VAL   A 1 212 ? -18.417 0.718  39.286 1.00 15.40 ? 212 VAL   A C   1 
ATOM   1639 O  O   . VAL   A 1 212 ? -19.117 -0.276 39.503 1.00 16.54 ? 212 VAL   A O   1 
ATOM   1640 C  CB  . VAL   A 1 212 ? -18.648 2.796  40.720 1.00 15.95 ? 212 VAL   A CB  1 
ATOM   1641 C  CG1 . VAL   A 1 212 ? -20.131 2.503  40.846 1.00 17.70 ? 212 VAL   A CG1 1 
ATOM   1642 C  CG2 . VAL   A 1 212 ? -18.154 3.496  41.993 1.00 16.55 ? 212 VAL   A CG2 1 
ATOM   1643 N  N   . ILE   A 1 213 ? -18.078 1.114  38.062 1.00 15.93 ? 213 ILE   A N   1 
ATOM   1644 C  CA  . ILE   A 1 213 ? -18.607 0.456  36.874 1.00 17.75 ? 213 ILE   A CA  1 
ATOM   1645 C  C   . ILE   A 1 213 ? -18.137 -0.997 36.853 1.00 19.58 ? 213 ILE   A C   1 
ATOM   1646 O  O   . ILE   A 1 213 ? -18.873 -1.862 36.425 1.00 18.40 ? 213 ILE   A O   1 
ATOM   1647 C  CB  . ILE   A 1 213 ? -18.204 1.207  35.596 1.00 19.17 ? 213 ILE   A CB  1 
ATOM   1648 C  CG1 . ILE   A 1 213 ? -18.887 2.560  35.521 1.00 18.10 ? 213 ILE   A CG1 1 
ATOM   1649 C  CG2 . ILE   A 1 213 ? -18.455 0.376  34.327 1.00 19.60 ? 213 ILE   A CG2 1 
ATOM   1650 C  CD1 . ILE   A 1 213 ? -18.336 3.456  34.436 1.00 19.16 ? 213 ILE   A CD1 1 
ATOM   1651 N  N   . ASN   A 1 214 ? -16.927 -1.256 37.352 1.00 19.82 ? 214 ASN   A N   1 
ATOM   1652 C  CA  . ASN   A 1 214 ? -16.397 -2.611 37.447 1.00 21.73 ? 214 ASN   A CA  1 
ATOM   1653 C  C   . ASN   A 1 214 ? -16.847 -3.373 38.693 1.00 22.35 ? 214 ASN   A C   1 
ATOM   1654 O  O   . ASN   A 1 214 ? -16.427 -4.517 38.877 1.00 25.24 ? 214 ASN   A O   1 
ATOM   1655 C  CB  . ASN   A 1 214 ? -14.878 -2.594 37.425 1.00 23.58 ? 214 ASN   A CB  1 
ATOM   1656 C  CG  . ASN   A 1 214 ? -14.433 -2.534 35.992 1.00 27.35 ? 214 ASN   A CG  1 
ATOM   1657 O  OD1 . ASN   A 1 214 ? -14.227 -3.603 35.413 1.00 28.43 ? 214 ASN   A OD1 1 
ATOM   1658 N  ND2 . ASN   A 1 214 ? -14.455 -1.350 35.383 1.00 27.10 ? 214 ASN   A ND2 1 
ATOM   1659 N  N   . GLY   A 1 215 ? -17.664 -2.755 39.553 1.00 20.20 ? 215 GLY   A N   1 
ATOM   1660 C  CA  . GLY   A 1 215 ? -18.192 -3.433 40.726 1.00 20.48 ? 215 GLY   A CA  1 
ATOM   1661 C  C   . GLY   A 1 215 ? -17.257 -3.374 41.931 1.00 20.62 ? 215 GLY   A C   1 
ATOM   1662 O  O   . GLY   A 1 215 ? -17.480 -4.080 42.924 1.00 21.97 ? 215 GLY   A O   1 
ATOM   1663 N  N   . ASP   A 1 216 ? -16.278 -2.464 41.913 1.00 19.23 ? 216 ASP   A N   1 
ATOM   1664 C  CA  . ASP   A 1 216 ? -15.417 -2.263 43.077 1.00 21.03 ? 216 ASP   A CA  1 
ATOM   1665 C  C   . ASP   A 1 216 ? -15.965 -1.054 43.842 1.00 21.42 ? 216 ASP   A C   1 
ATOM   1666 O  O   . ASP   A 1 216 ? -15.648 0.077  43.463 1.00 23.60 ? 216 ASP   A O   1 
ATOM   1667 C  CB  . ASP   A 1 216 ? -13.970 -2.066 42.621 1.00 23.40 ? 216 ASP   A CB  1 
ATOM   1668 C  CG  . ASP   A 1 216 ? -12.874 -2.623 43.525 1.00 28.32 ? 216 ASP   A CG  1 
ATOM   1669 O  OD1 . ASP   A 1 216 ? -13.201 -3.101 44.643 1.00 29.01 ? 216 ASP   A OD1 1 
ATOM   1670 O  OD2 . ASP   A 1 216 ? -11.697 -2.596 43.095 1.00 27.74 ? 216 ASP   A OD2 1 
ATOM   1671 N  N   . ARG   A 1 217 ? -16.815 -1.270 44.864 1.00 19.21 ? 217 ARG   A N   1 
ATOM   1672 C  CA  . ARG   A 1 217 ? -17.659 -0.211 45.404 1.00 20.67 ? 217 ARG   A CA  1 
ATOM   1673 C  C   . ARG   A 1 217 ? -17.460 0.053  46.901 1.00 20.84 ? 217 ARG   A C   1 
ATOM   1674 O  O   . ARG   A 1 217 ? -18.139 0.924  47.446 1.00 17.39 ? 217 ARG   A O   1 
ATOM   1675 C  CB  . ARG   A 1 217 ? -19.147 -0.515 45.173 1.00 24.95 ? 217 ARG   A CB  1 
ATOM   1676 C  CG  . ARG   A 1 217 ? -19.556 -0.522 43.706 1.00 30.87 ? 217 ARG   A CG  1 
ATOM   1677 C  CD  . ARG   A 1 217 ? -21.054 -0.716 43.494 1.00 32.98 ? 217 ARG   A CD  1 
ATOM   1678 N  NE  . ARG   A 1 217 ? -21.553 -1.718 44.436 1.00 35.94 ? 217 ARG   A NE  1 
ATOM   1679 C  CZ  . ARG   A 1 217 ? -21.356 -3.025 44.352 1.00 33.75 ? 217 ARG   A CZ  1 
ATOM   1680 N  NH1 . ARG   A 1 217 ? -21.062 -3.575 43.192 1.00 36.91 ? 217 ARG   A NH1 1 
ATOM   1681 N  NH2 . ARG   A 1 217 ? -21.512 -3.779 45.424 1.00 33.51 ? 217 ARG   A NH2 1 
ATOM   1682 N  N   . TRP   A 1 218 ? -16.481 -0.623 47.536 1.00 21.86 ? 218 TRP   A N   1 
ATOM   1683 C  CA  . TRP   A 1 218 ? -16.305 -0.599 48.982 1.00 21.23 ? 218 TRP   A CA  1 
ATOM   1684 C  C   . TRP   A 1 218 ? -16.082 0.808  49.537 1.00 20.16 ? 218 TRP   A C   1 
ATOM   1685 O  O   . TRP   A 1 218 ? -16.446 1.090  50.677 1.00 20.83 ? 218 TRP   A O   1 
ATOM   1686 C  CB  . TRP   A 1 218 ? -15.147 -1.531 49.395 1.00 19.93 ? 218 TRP   A CB  1 
ATOM   1687 C  CG  . TRP   A 1 218 ? -13.767 -1.098 48.953 1.00 19.39 ? 218 TRP   A CG  1 
ATOM   1688 C  CD1 . TRP   A 1 218 ? -13.083 -1.524 47.853 1.00 20.15 ? 218 TRP   A CD1 1 
ATOM   1689 C  CD2 . TRP   A 1 218 ? -12.906 -0.144 49.600 1.00 17.56 ? 218 TRP   A CD2 1 
ATOM   1690 N  NE1 . TRP   A 1 218 ? -11.842 -0.954 47.798 1.00 18.98 ? 218 TRP   A NE1 1 
ATOM   1691 C  CE2 . TRP   A 1 218 ? -11.713 -0.084 48.852 1.00 18.95 ? 218 TRP   A CE2 1 
ATOM   1692 C  CE3 . TRP   A 1 218 ? -13.013 0.646  50.750 1.00 19.69 ? 218 TRP   A CE3 1 
ATOM   1693 C  CZ2 . TRP   A 1 218 ? -10.647 0.740  49.217 1.00 18.44 ? 218 TRP   A CZ2 1 
ATOM   1694 C  CZ3 . TRP   A 1 218 ? -11.957 1.454  51.117 1.00 19.77 ? 218 TRP   A CZ3 1 
ATOM   1695 C  CH2 . TRP   A 1 218 ? -10.786 1.496  50.363 1.00 20.45 ? 218 TRP   A CH2 1 
ATOM   1696 N  N   . PHE   A 1 219 ? -15.498 1.704  48.751 1.00 17.90 ? 219 PHE   A N   1 
ATOM   1697 C  CA  . PHE   A 1 219 ? -15.094 3.022  49.238 1.00 16.83 ? 219 PHE   A CA  1 
ATOM   1698 C  C   . PHE   A 1 219 ? -16.225 4.056  49.173 1.00 17.70 ? 219 PHE   A C   1 
ATOM   1699 O  O   . PHE   A 1 219 ? -16.037 5.177  49.614 1.00 18.76 ? 219 PHE   A O   1 
ATOM   1700 C  CB  . PHE   A 1 219 ? -13.891 3.526  48.427 1.00 16.81 ? 219 PHE   A CB  1 
ATOM   1701 C  CG  . PHE   A 1 219 ? -14.208 3.583  46.933 1.00 15.63 ? 219 PHE   A CG  1 
ATOM   1702 C  CD1 . PHE   A 1 219 ? -14.859 4.679  46.372 1.00 16.32 ? 219 PHE   A CD1 1 
ATOM   1703 C  CD2 . PHE   A 1 219 ? -13.908 2.511  46.094 1.00 16.69 ? 219 PHE   A CD2 1 
ATOM   1704 C  CE1 . PHE   A 1 219 ? -15.164 4.705  45.025 1.00 15.54 ? 219 PHE   A CE1 1 
ATOM   1705 C  CE2 . PHE   A 1 219 ? -14.260 2.523  44.743 1.00 16.61 ? 219 PHE   A CE2 1 
ATOM   1706 C  CZ  . PHE   A 1 219 ? -14.850 3.624  44.208 1.00 16.06 ? 219 PHE   A CZ  1 
ATOM   1707 N  N   . LEU   A 1 220 ? -17.398 3.726  48.618 1.00 19.23 ? 220 LEU   A N   1 
ATOM   1708 C  CA  . LEU   A 1 220 ? -18.468 4.720  48.517 1.00 17.56 ? 220 LEU   A CA  1 
ATOM   1709 C  C   . LEU   A 1 220 ? -19.030 4.951  49.910 1.00 20.78 ? 220 LEU   A C   1 
ATOM   1710 O  O   . LEU   A 1 220 ? -19.456 4.000  50.552 1.00 18.60 ? 220 LEU   A O   1 
ATOM   1711 C  CB  . LEU   A 1 220 ? -19.587 4.244  47.592 1.00 17.67 ? 220 LEU   A CB  1 
ATOM   1712 C  CG  . LEU   A 1 220 ? -19.195 4.030  46.134 1.00 18.77 ? 220 LEU   A CG  1 
ATOM   1713 C  CD1 . LEU   A 1 220 ? -20.362 3.443  45.379 1.00 20.02 ? 220 LEU   A CD1 1 
ATOM   1714 C  CD2 . LEU   A 1 220 ? -18.774 5.354  45.545 1.00 18.53 ? 220 LEU   A CD2 1 
ATOM   1715 N  N   . ASN   A 1 221 ? -19.072 6.207  50.357 1.00 21.30 ? 221 ASN   A N   1 
ATOM   1716 C  CA  . ASN   A 1 221 ? -19.653 6.490  51.663 1.00 21.88 ? 221 ASN   A CA  1 
ATOM   1717 C  C   . ASN   A 1 221 ? -21.045 7.091  51.463 1.00 23.87 ? 221 ASN   A C   1 
ATOM   1718 O  O   . ASN   A 1 221 ? -21.502 7.247  50.337 1.00 21.34 ? 221 ASN   A O   1 
ATOM   1719 C  CB  . ASN   A 1 221 ? -18.663 7.285  52.507 1.00 22.18 ? 221 ASN   A CB  1 
ATOM   1720 C  CG  . ASN   A 1 221 ? -18.481 8.704  52.023 1.00 23.41 ? 221 ASN   A CG  1 
ATOM   1721 O  OD1 . ASN   A 1 221 ? -19.346 9.250  51.349 1.00 23.11 ? 221 ASN   A OD1 1 
ATOM   1722 N  ND2 . ASN   A 1 221 ? -17.396 9.361  52.421 1.00 30.09 ? 221 ASN   A ND2 1 
ATOM   1723 N  N   . ARG   A 1 222 ? -21.737 7.417  52.565 1.00 24.52 ? 222 ARG   A N   1 
ATOM   1724 C  CA  . ARG   A 1 222 ? -23.142 7.794  52.492 1.00 28.87 ? 222 ARG   A CA  1 
ATOM   1725 C  C   . ARG   A 1 222 ? -23.289 9.322  52.482 1.00 27.25 ? 222 ARG   A C   1 
ATOM   1726 O  O   . ARG   A 1 222 ? -24.404 9.830  52.532 1.00 24.74 ? 222 ARG   A O   1 
ATOM   1727 C  CB  . ARG   A 1 222 ? -23.865 7.139  53.677 1.00 34.87 ? 222 ARG   A CB  1 
ATOM   1728 C  CG  . ARG   A 1 222 ? -23.559 7.836  54.992 1.00 42.39 ? 222 ARG   A CG  1 
ATOM   1729 C  CD  . ARG   A 1 222 ? -24.096 7.069  56.196 1.00 50.47 ? 222 ARG   A CD  1 
ATOM   1730 N  NE  . ARG   A 1 222 ? -23.633 7.716  57.431 1.00 54.89 ? 222 ARG   A NE  1 
ATOM   1731 C  CZ  . ARG   A 1 222 ? -22.680 7.227  58.212 1.00 59.75 ? 222 ARG   A CZ  1 
ATOM   1732 N  NH1 . ARG   A 1 222 ? -22.028 6.137  57.846 1.00 60.35 ? 222 ARG   A NH1 1 
ATOM   1733 N  NH2 . ARG   A 1 222 ? -22.381 7.827  59.349 1.00 58.13 ? 222 ARG   A NH2 1 
ATOM   1734 N  N   . PHE   A 1 223 ? -22.173 10.053 52.330 1.00 23.20 ? 223 PHE   A N   1 
ATOM   1735 C  CA  . PHE   A 1 223 ? -22.166 11.497 52.490 1.00 23.28 ? 223 PHE   A CA  1 
ATOM   1736 C  C   . PHE   A 1 223 ? -22.018 12.230 51.163 1.00 24.51 ? 223 PHE   A C   1 
ATOM   1737 O  O   . PHE   A 1 223 ? -21.755 11.617 50.127 1.00 23.77 ? 223 PHE   A O   1 
ATOM   1738 C  CB  . PHE   A 1 223 ? -20.981 11.902 53.376 1.00 25.55 ? 223 PHE   A CB  1 
ATOM   1739 C  CG  . PHE   A 1 223 ? -20.994 11.275 54.762 1.00 28.87 ? 223 PHE   A CG  1 
ATOM   1740 C  CD1 . PHE   A 1 223 ? -22.027 11.561 55.649 1.00 30.35 ? 223 PHE   A CD1 1 
ATOM   1741 C  CD2 . PHE   A 1 223 ? -19.964 10.429 55.188 1.00 30.00 ? 223 PHE   A CD2 1 
ATOM   1742 C  CE1 . PHE   A 1 223 ? -22.032 11.011 56.932 1.00 30.85 ? 223 PHE   A CE1 1 
ATOM   1743 C  CE2 . PHE   A 1 223 ? -19.972 9.888  56.467 1.00 30.42 ? 223 PHE   A CE2 1 
ATOM   1744 C  CZ  . PHE   A 1 223 ? -20.996 10.201 57.343 1.00 30.78 ? 223 PHE   A CZ  1 
ATOM   1745 N  N   . THR   A 1 224 ? -22.214 13.554 51.241 1.00 23.46 ? 224 THR   A N   1 
ATOM   1746 C  CA  . THR   A 1 224 ? -21.918 14.502 50.171 1.00 24.12 ? 224 THR   A CA  1 
ATOM   1747 C  C   . THR   A 1 224 ? -21.002 15.565 50.758 1.00 24.31 ? 224 THR   A C   1 
ATOM   1748 O  O   . THR   A 1 224 ? -20.771 15.544 51.962 1.00 26.82 ? 224 THR   A O   1 
ATOM   1749 C  CB  . THR   A 1 224 ? -23.182 15.132 49.579 1.00 26.27 ? 224 THR   A CB  1 
ATOM   1750 O  OG1 . THR   A 1 224 ? -22.826 15.689 48.313 1.00 24.77 ? 224 THR   A OG1 1 
ATOM   1751 C  CG2 . THR   A 1 224 ? -23.764 16.241 50.448 1.00 28.35 ? 224 THR   A CG2 1 
ATOM   1752 N  N   . THR   A 1 225 ? -20.545 16.507 49.918 1.00 22.98 ? 225 THR   A N   1 
ATOM   1753 C  CA  . THR   A 1 225 ? -19.743 17.633 50.362 1.00 23.68 ? 225 THR   A CA  1 
ATOM   1754 C  C   . THR   A 1 225 ? -20.001 18.770 49.395 1.00 23.85 ? 225 THR   A C   1 
ATOM   1755 O  O   . THR   A 1 225 ? -20.612 18.575 48.339 1.00 25.89 ? 225 THR   A O   1 
ATOM   1756 C  CB  . THR   A 1 225 ? -18.245 17.303 50.448 1.00 28.53 ? 225 THR   A CB  1 
ATOM   1757 O  OG1 . THR   A 1 225 ? -17.571 18.456 50.960 1.00 32.47 ? 225 THR   A OG1 1 
ATOM   1758 C  CG2 . THR   A 1 225 ? -17.611 16.956 49.111 1.00 25.49 ? 225 THR   A CG2 1 
ATOM   1759 N  N   . THR   A 1 226 ? -19.525 19.962 49.770 1.00 23.10 ? 226 THR   A N   1 
ATOM   1760 C  CA  . THR   A 1 226 ? -19.552 21.100 48.873 1.00 22.10 ? 226 THR   A CA  1 
ATOM   1761 C  C   . THR   A 1 226 ? -18.236 21.086 48.122 1.00 21.20 ? 226 THR   A C   1 
ATOM   1762 O  O   . THR   A 1 226 ? -17.240 20.557 48.615 1.00 22.07 ? 226 THR   A O   1 
ATOM   1763 C  CB  . THR   A 1 226 ? -19.716 22.422 49.633 1.00 23.23 ? 226 THR   A CB  1 
ATOM   1764 O  OG1 . THR   A 1 226 ? -18.519 22.598 50.381 1.00 22.38 ? 226 THR   A OG1 1 
ATOM   1765 C  CG2 . THR   A 1 226 ? -20.944 22.405 50.522 1.00 26.37 ? 226 THR   A CG2 1 
ATOM   1766 N  N   . LEU   A 1 227 ? -18.229 21.738 46.968 1.00 22.44 ? 227 LEU   A N   1 
ATOM   1767 C  CA  . LEU   A 1 227 ? -17.015 21.865 46.187 1.00 22.91 ? 227 LEU   A CA  1 
ATOM   1768 C  C   . LEU   A 1 227 ? -15.951 22.585 47.020 1.00 26.03 ? 227 LEU   A C   1 
ATOM   1769 O  O   . LEU   A 1 227 ? -14.769 22.210 47.028 1.00 23.31 ? 227 LEU   A O   1 
ATOM   1770 C  CB  . LEU   A 1 227 ? -17.413 22.641 44.938 1.00 23.91 ? 227 LEU   A CB  1 
ATOM   1771 C  CG  . LEU   A 1 227 ? -16.298 22.860 43.922 1.00 23.33 ? 227 LEU   A CG  1 
ATOM   1772 C  CD1 . LEU   A 1 227 ? -15.659 21.494 43.610 1.00 23.80 ? 227 LEU   A CD1 1 
ATOM   1773 C  CD2 . LEU   A 1 227 ? -16.809 23.530 42.668 1.00 25.13 ? 227 LEU   A CD2 1 
ATOM   1774 N  N   . ASN   A 1 228 ? -16.387 23.612 47.769 1.00 26.47 ? 228 ASN   A N   1 
ATOM   1775 C  CA  . ASN   A 1 228 ? -15.454 24.438 48.515 1.00 29.86 ? 228 ASN   A CA  1 
ATOM   1776 C  C   . ASN   A 1 228 ? -14.730 23.630 49.576 1.00 24.69 ? 228 ASN   A C   1 
ATOM   1777 O  O   . ASN   A 1 228 ? -13.503 23.702 49.657 1.00 27.55 ? 228 ASN   A O   1 
ATOM   1778 C  CB  . ASN   A 1 228 ? -16.123 25.643 49.165 1.00 33.62 ? 228 ASN   A CB  1 
ATOM   1779 C  CG  . ASN   A 1 228 ? -16.254 26.780 48.189 1.00 37.85 ? 228 ASN   A CG  1 
ATOM   1780 O  OD1 . ASN   A 1 228 ? -15.717 26.731 47.070 1.00 44.19 ? 228 ASN   A OD1 1 
ATOM   1781 N  ND2 . ASN   A 1 228 ? -16.966 27.813 48.600 1.00 46.19 ? 228 ASN   A ND2 1 
ATOM   1782 N  N   . ASP   A 1 229 ? -15.489 22.863 50.359 1.00 23.71 ? 229 ASP   A N   1 
ATOM   1783 C  CA  . ASP   A 1 229 ? -14.937 22.082 51.458 1.00 26.24 ? 229 ASP   A CA  1 
ATOM   1784 C  C   . ASP   A 1 229 ? -14.082 20.943 50.918 1.00 23.33 ? 229 ASP   A C   1 
ATOM   1785 O  O   . ASP   A 1 229 ? -13.033 20.603 51.480 1.00 22.73 ? 229 ASP   A O   1 
ATOM   1786 C  CB  . ASP   A 1 229 ? -16.038 21.488 52.308 1.00 30.50 ? 229 ASP   A CB  1 
ATOM   1787 C  CG  . ASP   A 1 229 ? -16.769 22.511 53.169 1.00 42.54 ? 229 ASP   A CG  1 
ATOM   1788 O  OD1 . ASP   A 1 229 ? -16.256 23.653 53.288 1.00 44.48 ? 229 ASP   A OD1 1 
ATOM   1789 O  OD2 . ASP   A 1 229 ? -17.850 22.163 53.702 1.00 54.42 ? 229 ASP   A OD2 1 
ATOM   1790 N  N   . PHE   A 1 230 ? -14.517 20.393 49.782 1.00 19.96 ? 230 PHE   A N   1 
ATOM   1791 C  CA  . PHE   A 1 230 ? -13.688 19.385 49.135 1.00 20.42 ? 230 PHE   A CA  1 
ATOM   1792 C  C   . PHE   A 1 230 ? -12.329 19.990 48.768 1.00 19.10 ? 230 PHE   A C   1 
ATOM   1793 O  O   . PHE   A 1 230 ? -11.296 19.410 49.116 1.00 22.08 ? 230 PHE   A O   1 
ATOM   1794 C  CB  . PHE   A 1 230 ? -14.370 18.753 47.921 1.00 18.24 ? 230 PHE   A CB  1 
ATOM   1795 C  CG  . PHE   A 1 230 ? -13.357 17.841 47.229 1.00 18.78 ? 230 PHE   A CG  1 
ATOM   1796 C  CD1 . PHE   A 1 230 ? -13.124 16.560 47.695 1.00 18.61 ? 230 PHE   A CD1 1 
ATOM   1797 C  CD2 . PHE   A 1 230 ? -12.625 18.304 46.152 1.00 20.69 ? 230 PHE   A CD2 1 
ATOM   1798 C  CE1 . PHE   A 1 230 ? -12.173 15.749 47.093 1.00 21.40 ? 230 PHE   A CE1 1 
ATOM   1799 C  CE2 . PHE   A 1 230 ? -11.665 17.490 45.549 1.00 23.46 ? 230 PHE   A CE2 1 
ATOM   1800 C  CZ  . PHE   A 1 230 ? -11.448 16.210 46.021 1.00 22.23 ? 230 PHE   A CZ  1 
ATOM   1801 N  N   . ASN   A 1 231 ? -12.312 21.175 48.146 1.00 19.85 ? 231 ASN   A N   1 
ATOM   1802 C  CA  . ASN   A 1 231 ? -11.047 21.776 47.718 1.00 20.99 ? 231 ASN   A CA  1 
ATOM   1803 C  C   . ASN   A 1 231 ? -10.091 22.135 48.871 1.00 24.05 ? 231 ASN   A C   1 
ATOM   1804 O  O   . ASN   A 1 231 ? -8.868  22.096 48.689 1.00 24.13 ? 231 ASN   A O   1 
ATOM   1805 C  CB  . ASN   A 1 231 ? -11.270 22.944 46.787 1.00 20.83 ? 231 ASN   A CB  1 
ATOM   1806 C  CG  . ASN   A 1 231 ? -11.591 22.420 45.414 1.00 22.66 ? 231 ASN   A CG  1 
ATOM   1807 O  OD1 . ASN   A 1 231 ? -11.083 21.362 44.995 1.00 21.13 ? 231 ASN   A OD1 1 
ATOM   1808 N  ND2 . ASN   A 1 231 ? -12.463 23.134 44.736 1.00 21.80 ? 231 ASN   A ND2 1 
ATOM   1809 N  N   . LEU   A 1 232 ? -10.618 22.467 50.038 1.00 26.48 ? 232 LEU   A N   1 
ATOM   1810 C  CA  . LEU   A 1 232 ? -9.780  22.736 51.209 1.00 28.12 ? 232 LEU   A CA  1 
ATOM   1811 C  C   . LEU   A 1 232 ? -9.058  21.468 51.641 1.00 28.65 ? 232 LEU   A C   1 
ATOM   1812 O  O   . LEU   A 1 232 ? -7.859  21.513 51.894 1.00 32.20 ? 232 LEU   A O   1 
ATOM   1813 C  CB  . LEU   A 1 232 ? -10.605 23.339 52.343 1.00 29.28 ? 232 LEU   A CB  1 
ATOM   1814 C  CG  . LEU   A 1 232 ? -11.216 24.712 52.047 1.00 33.60 ? 232 LEU   A CG  1 
ATOM   1815 C  CD1 . LEU   A 1 232 ? -12.097 25.174 53.185 1.00 35.94 ? 232 LEU   A CD1 1 
ATOM   1816 C  CD2 . LEU   A 1 232 ? -10.174 25.778 51.727 1.00 35.35 ? 232 LEU   A CD2 1 
ATOM   1817 N  N   . VAL   A 1 233 ? -9.738  20.313 51.605 1.00 30.03 ? 233 VAL   A N   1 
ATOM   1818 C  CA  . VAL   A 1 233 ? -9.087  19.045 51.917 1.00 31.31 ? 233 VAL   A CA  1 
ATOM   1819 C  C   . VAL   A 1 233 ? -8.100  18.631 50.826 1.00 35.23 ? 233 VAL   A C   1 
ATOM   1820 O  O   . VAL   A 1 233 ? -6.939  18.339 51.097 1.00 37.26 ? 233 VAL   A O   1 
ATOM   1821 C  CB  . VAL   A 1 233 ? -10.121 17.932 52.155 1.00 37.55 ? 233 VAL   A CB  1 
ATOM   1822 C  CG1 . VAL   A 1 233 ? -9.459  16.557 52.256 1.00 40.99 ? 233 VAL   A CG1 1 
ATOM   1823 C  CG2 . VAL   A 1 233 ? -10.962 18.225 53.382 1.00 36.17 ? 233 VAL   A CG2 1 
ATOM   1824 N  N   . ALA   A 1 234 ? -8.546  18.589 49.580 1.00 31.40 ? 234 ALA   A N   1 
ATOM   1825 C  CA  . ALA   A 1 234 ? -7.657  18.228 48.498 1.00 34.28 ? 234 ALA   A CA  1 
ATOM   1826 C  C   . ALA   A 1 234 ? -6.350  19.004 48.622 1.00 32.52 ? 234 ALA   A C   1 
ATOM   1827 O  O   . ALA   A 1 234 ? -5.287  18.442 48.398 1.00 28.32 ? 234 ALA   A O   1 
ATOM   1828 C  CB  . ALA   A 1 234 ? -8.303  18.482 47.157 1.00 39.76 ? 234 ALA   A CB  1 
ATOM   1829 N  N   . MET   A 1 235 ? -6.445  20.305 48.918 1.00 32.22 ? 235 MET   A N   1 
ATOM   1830 C  CA  . MET   A 1 235 ? -5.287  21.184 48.925 1.00 31.61 ? 235 MET   A CA  1 
ATOM   1831 C  C   . MET   A 1 235 ? -4.158  20.636 49.815 1.00 25.72 ? 235 MET   A C   1 
ATOM   1832 O  O   . MET   A 1 235 ? -2.982  20.658 49.434 1.00 21.76 ? 235 MET   A O   1 
ATOM   1833 C  CB  . MET   A 1 235 ? -5.686  22.591 49.374 1.00 34.72 ? 235 MET   A CB  1 
ATOM   1834 C  CG  . MET   A 1 235 ? -4.499  23.545 49.477 1.00 41.07 ? 235 MET   A CG  1 
ATOM   1835 S  SD  . MET   A 1 235 ? -4.944  25.263 49.813 1.00 53.05 ? 235 MET   A SD  1 
ATOM   1836 C  CE  . MET   A 1 235 ? -6.046  25.294 51.236 1.00 50.00 ? 235 MET   A CE  1 
ATOM   1837 N  N   . LYS   A 1 236 ? -4.528  20.118 50.984 1.00 23.90 ? 236 LYS   A N   1 
ATOM   1838 C  CA  . LYS   A 1 236 ? -3.594  19.625 51.984 1.00 25.74 ? 236 LYS   A CA  1 
ATOM   1839 C  C   . LYS   A 1 236 ? -2.849  18.384 51.487 1.00 23.27 ? 236 LYS   A C   1 
ATOM   1840 O  O   . LYS   A 1 236 ? -1.712  18.098 51.885 1.00 21.70 ? 236 LYS   A O   1 
ATOM   1841 C  CB  . LYS   A 1 236 ? -4.462  19.397 53.231 1.00 31.38 ? 236 LYS   A CB  1 
ATOM   1842 C  CG  . LYS   A 1 236 ? -3.718  19.016 54.470 1.00 40.90 ? 236 LYS   A CG  1 
ATOM   1843 C  CD  . LYS   A 1 236 ? -4.557  18.611 55.686 1.00 47.86 ? 236 LYS   A CD  1 
ATOM   1844 C  CE  . LYS   A 1 236 ? -3.627  17.985 56.710 1.00 57.67 ? 236 LYS   A CE  1 
ATOM   1845 N  NZ  . LYS   A 1 236 ? -4.060  17.827 58.106 1.00 60.66 ? 236 LYS   A NZ  1 
ATOM   1846 N  N   . TYR   A 1 237 ? -3.490  17.604 50.603 1.00 22.12 ? 237 TYR   A N   1 
ATOM   1847 C  CA  . TYR   A 1 237 ? -2.891  16.360 50.139 1.00 19.86 ? 237 TYR   A CA  1 
ATOM   1848 C  C   . TYR   A 1 237 ? -2.271  16.521 48.756 1.00 20.15 ? 237 TYR   A C   1 
ATOM   1849 O  O   . TYR   A 1 237 ? -1.954  15.524 48.098 1.00 21.79 ? 237 TYR   A O   1 
ATOM   1850 C  CB  . TYR   A 1 237 ? -3.991  15.295 50.127 1.00 20.02 ? 237 TYR   A CB  1 
ATOM   1851 C  CG  . TYR   A 1 237 ? -4.401  14.948 51.543 1.00 20.50 ? 237 TYR   A CG  1 
ATOM   1852 C  CD1 . TYR   A 1 237 ? -3.646  14.081 52.309 1.00 23.59 ? 237 TYR   A CD1 1 
ATOM   1853 C  CD2 . TYR   A 1 237 ? -5.528  15.513 52.114 1.00 22.89 ? 237 TYR   A CD2 1 
ATOM   1854 C  CE1 . TYR   A 1 237 ? -4.002  13.779 53.615 1.00 24.57 ? 237 TYR   A CE1 1 
ATOM   1855 C  CE2 . TYR   A 1 237 ? -5.888  15.239 53.421 1.00 23.96 ? 237 TYR   A CE2 1 
ATOM   1856 C  CZ  . TYR   A 1 237 ? -5.133  14.353 54.165 1.00 24.38 ? 237 TYR   A CZ  1 
ATOM   1857 O  OH  . TYR   A 1 237 ? -5.508  14.082 55.449 1.00 29.00 ? 237 TYR   A OH  1 
ATOM   1858 N  N   . ASN   A 1 238 ? -2.088  17.776 48.356 1.00 18.17 ? 238 ASN   A N   1 
ATOM   1859 C  CA  . ASN   A 1 238 ? -1.400  18.155 47.141 1.00 17.69 ? 238 ASN   A CA  1 
ATOM   1860 C  C   . ASN   A 1 238 ? -2.172  17.640 45.922 1.00 16.36 ? 238 ASN   A C   1 
ATOM   1861 O  O   . ASN   A 1 238 ? -1.580  17.130 44.971 1.00 17.54 ? 238 ASN   A O   1 
ATOM   1862 C  CB  . ASN   A 1 238 ? 0.058   17.698 47.165 1.00 21.02 ? 238 ASN   A CB  1 
ATOM   1863 C  CG  . ASN   A 1 238 ? 0.880   18.299 46.057 1.00 22.68 ? 238 ASN   A CG  1 
ATOM   1864 O  OD1 . ASN   A 1 238 ? 0.642   19.438 45.648 1.00 27.11 ? 238 ASN   A OD1 1 
ATOM   1865 N  ND2 . ASN   A 1 238 ? 1.855   17.560 45.558 1.00 24.34 ? 238 ASN   A ND2 1 
ATOM   1866 N  N   . TYR   A 1 239 ? -3.485  17.791 45.973 1.00 15.90 ? 239 TYR   A N   1 
ATOM   1867 C  CA  . TYR   A 1 239 ? -4.379  17.572 44.838 1.00 17.29 ? 239 TYR   A CA  1 
ATOM   1868 C  C   . TYR   A 1 239 ? -4.675  18.939 44.223 1.00 20.02 ? 239 TYR   A C   1 
ATOM   1869 O  O   . TYR   A 1 239 ? -4.856  19.905 44.959 1.00 21.75 ? 239 TYR   A O   1 
ATOM   1870 C  CB  . TYR   A 1 239 ? -5.661  16.882 45.335 1.00 18.33 ? 239 TYR   A CB  1 
ATOM   1871 C  CG  . TYR   A 1 239 ? -5.630  15.360 45.385 1.00 17.45 ? 239 TYR   A CG  1 
ATOM   1872 C  CD1 . TYR   A 1 239 ? -4.649  14.681 46.090 1.00 18.05 ? 239 TYR   A CD1 1 
ATOM   1873 C  CD2 . TYR   A 1 239 ? -6.548  14.598 44.663 1.00 19.04 ? 239 TYR   A CD2 1 
ATOM   1874 C  CE1 . TYR   A 1 239 ? -4.585  13.295 46.113 1.00 18.03 ? 239 TYR   A CE1 1 
ATOM   1875 C  CE2 . TYR   A 1 239 ? -6.510  13.209 44.691 1.00 17.70 ? 239 TYR   A CE2 1 
ATOM   1876 C  CZ  . TYR   A 1 239 ? -5.498  12.563 45.380 1.00 18.10 ? 239 TYR   A CZ  1 
ATOM   1877 O  OH  . TYR   A 1 239 ? -5.398  11.223 45.421 1.00 21.83 ? 239 TYR   A OH  1 
ATOM   1878 N  N   . GLU   A 1 240 ? -4.778  18.992 42.883 1.00 18.86 ? 240 GLU   A N   1 
ATOM   1879 C  CA  . GLU   A 1 240 ? -5.231  20.162 42.140 1.00 21.10 ? 240 GLU   A CA  1 
ATOM   1880 C  C   . GLU   A 1 240 ? -6.640  20.570 42.565 1.00 19.17 ? 240 GLU   A C   1 
ATOM   1881 O  O   . GLU   A 1 240 ? -7.463  19.719 42.903 1.00 19.12 ? 240 GLU   A O   1 
ATOM   1882 C  CB  . GLU   A 1 240 ? -5.477  19.844 40.657 1.00 26.29 ? 240 GLU   A CB  1 
ATOM   1883 C  CG  . GLU   A 1 240 ? -4.262  19.839 39.743 1.00 34.94 ? 240 GLU   A CG  1 
ATOM   1884 C  CD  . GLU   A 1 240 ? -4.682  19.674 38.274 1.00 39.21 ? 240 GLU   A CD  1 
ATOM   1885 O  OE1 . GLU   A 1 240 ? -5.874  19.345 37.919 1.00 45.89 ? 240 GLU   A OE1 1 
ATOM   1886 O  OE2 . GLU   A 1 240 ? -3.784  19.920 37.434 1.00 52.17 ? 240 GLU   A OE2 1 
ATOM   1887 N  N   . PRO   A 1 241 ? -7.000  21.873 42.508 1.00 19.91 ? 241 PRO   A N   1 
ATOM   1888 C  CA  . PRO   A 1 241 ? -8.378  22.283 42.731 1.00 22.11 ? 241 PRO   A CA  1 
ATOM   1889 C  C   . PRO   A 1 241 ? -9.291  21.618 41.703 1.00 22.06 ? 241 PRO   A C   1 
ATOM   1890 O  O   . PRO   A 1 241 ? -8.954  21.527 40.519 1.00 21.51 ? 241 PRO   A O   1 
ATOM   1891 C  CB  . PRO   A 1 241 ? -8.349  23.854 42.566 1.00 21.34 ? 241 PRO   A CB  1 
ATOM   1892 C  CG  . PRO   A 1 241 ? -6.914  24.221 42.823 1.00 20.71 ? 241 PRO   A CG  1 
ATOM   1893 C  CD  . PRO   A 1 241 ? -6.110  23.031 42.271 1.00 20.53 ? 241 PRO   A CD  1 
ATOM   1894 N  N   . LEU   A 1 242 ? -10.467 21.197 42.161 1.00 20.86 ? 242 LEU   A N   1 
ATOM   1895 C  CA  . LEU   A 1 242 ? -11.514 20.755 41.251 1.00 19.95 ? 242 LEU   A CA  1 
ATOM   1896 C  C   . LEU   A 1 242 ? -12.368 21.967 40.884 1.00 19.37 ? 242 LEU   A C   1 
ATOM   1897 O  O   . LEU   A 1 242 ? -12.812 22.696 41.774 1.00 19.65 ? 242 LEU   A O   1 
ATOM   1898 C  CB  . LEU   A 1 242 ? -12.334 19.667 41.946 1.00 19.35 ? 242 LEU   A CB  1 
ATOM   1899 C  CG  . LEU   A 1 242 ? -13.289 18.874 41.052 1.00 18.51 ? 242 LEU   A CG  1 
ATOM   1900 C  CD1 . LEU   A 1 242 ? -12.442 17.988 40.154 1.00 17.85 ? 242 LEU   A CD1 1 
ATOM   1901 C  CD2 . LEU   A 1 242 ? -14.291 18.086 41.893 1.00 19.26 ? 242 LEU   A CD2 1 
ATOM   1902 N  N   . THR   A 1 243 ? -12.510 22.225 39.587 1.00 18.74 ? 243 THR   A N   1 
ATOM   1903 C  CA  . THR   A 1 243 ? -13.285 23.361 39.107 1.00 18.89 ? 243 THR   A CA  1 
ATOM   1904 C  C   . THR   A 1 243 ? -14.649 22.878 38.634 1.00 21.24 ? 243 THR   A C   1 
ATOM   1905 O  O   . THR   A 1 243 ? -14.880 21.674 38.451 1.00 17.20 ? 243 THR   A O   1 
ATOM   1906 C  CB  . THR   A 1 243 ? -12.540 24.054 37.972 1.00 20.20 ? 243 THR   A CB  1 
ATOM   1907 O  OG1 . THR   A 1 243 ? -12.501 23.134 36.877 1.00 22.33 ? 243 THR   A OG1 1 
ATOM   1908 C  CG2 . THR   A 1 243 ? -11.145 24.474 38.395 1.00 22.11 ? 243 THR   A CG2 1 
ATOM   1909 N  N   . GLN   A 1 244 ? -15.536 23.852 38.380 1.00 21.67 ? 244 GLN   A N   1 
ATOM   1910 C  CA  . GLN   A 1 244 ? -16.857 23.543 37.837 1.00 22.47 ? 244 GLN   A CA  1 
ATOM   1911 C  C   . GLN   A 1 244 ? -16.724 22.906 36.456 1.00 19.18 ? 244 GLN   A C   1 
ATOM   1912 O  O   . GLN   A 1 244 ? -17.500 22.022 36.082 1.00 19.60 ? 244 GLN   A O   1 
ATOM   1913 C  CB  . GLN   A 1 244 ? -17.740 24.796 37.793 1.00 23.75 ? 244 GLN   A CB  1 
ATOM   1914 C  CG  . GLN   A 1 244 ? -19.193 24.496 37.429 1.00 24.79 ? 244 GLN   A CG  1 
ATOM   1915 C  CD  . GLN   A 1 244 ? -19.857 23.499 38.359 1.00 23.47 ? 244 GLN   A CD  1 
ATOM   1916 O  OE1 . GLN   A 1 244 ? -19.751 23.575 39.587 1.00 25.55 ? 244 GLN   A OE1 1 
ATOM   1917 N  NE2 . GLN   A 1 244 ? -20.550 22.533 37.785 1.00 21.87 ? 244 GLN   A NE2 1 
ATOM   1918 N  N   . ASP   A 1 245 ? -15.734 23.326 35.678 1.00 19.69 ? 245 ASP   A N   1 
ATOM   1919 C  CA  . ASP   A 1 245 ? -15.516 22.695 34.385 1.00 21.05 ? 245 ASP   A CA  1 
ATOM   1920 C  C   . ASP   A 1 245 ? -15.204 21.210 34.536 1.00 19.80 ? 245 ASP   A C   1 
ATOM   1921 O  O   . ASP   A 1 245 ? -15.667 20.411 33.728 1.00 19.79 ? 245 ASP   A O   1 
ATOM   1922 C  CB  . ASP   A 1 245 ? -14.412 23.345 33.581 1.00 25.00 ? 245 ASP   A CB  1 
ATOM   1923 C  CG  . ASP   A 1 245 ? -14.826 24.655 32.920 1.00 29.34 ? 245 ASP   A CG  1 
ATOM   1924 O  OD1 . ASP   A 1 245 ? -15.983 25.081 33.125 1.00 32.39 ? 245 ASP   A OD1 1 
ATOM   1925 O  OD2 . ASP   A 1 245 ? -13.981 25.237 32.237 1.00 32.79 ? 245 ASP   A OD2 1 
ATOM   1926 N  N   . HIS   A 1 246 ? -14.391 20.863 35.546 1.00 19.18 ? 246 HIS   A N   1 
ATOM   1927 C  CA  . HIS   A 1 246 ? -14.089 19.476 35.869 1.00 17.77 ? 246 HIS   A CA  1 
ATOM   1928 C  C   . HIS   A 1 246 ? -15.344 18.711 36.259 1.00 16.72 ? 246 HIS   A C   1 
ATOM   1929 O  O   . HIS   A 1 246 ? -15.547 17.584 35.808 1.00 15.93 ? 246 HIS   A O   1 
ATOM   1930 C  CB  . HIS   A 1 246 ? -13.101 19.385 37.037 1.00 17.65 ? 246 HIS   A CB  1 
ATOM   1931 C  CG  . HIS   A 1 246 ? -11.738 19.819 36.653 1.00 19.39 ? 246 HIS   A CG  1 
ATOM   1932 N  ND1 . HIS   A 1 246 ? -10.905 20.426 37.560 1.00 19.65 ? 246 HIS   A ND1 1 
ATOM   1933 C  CD2 . HIS   A 1 246 ? -11.076 19.783 35.486 1.00 21.23 ? 246 HIS   A CD2 1 
ATOM   1934 C  CE1 . HIS   A 1 246 ? -9.769  20.729 36.951 1.00 21.67 ? 246 HIS   A CE1 1 
ATOM   1935 N  NE2 . HIS   A 1 246 ? -9.853  20.337 35.691 1.00 21.46 ? 246 HIS   A NE2 1 
ATOM   1936 N  N   . VAL   A 1 247 ? -16.168 19.334 37.107 1.00 16.80 ? 247 VAL   A N   1 
ATOM   1937 C  CA  . VAL   A 1 247 ? -17.432 18.722 37.481 1.00 17.90 ? 247 VAL   A CA  1 
ATOM   1938 C  C   . VAL   A 1 247 ? -18.259 18.448 36.230 1.00 18.04 ? 247 VAL   A C   1 
ATOM   1939 O  O   . VAL   A 1 247 ? -18.878 17.409 36.109 1.00 19.05 ? 247 VAL   A O   1 
ATOM   1940 C  CB  . VAL   A 1 247 ? -18.182 19.583 38.507 1.00 17.62 ? 247 VAL   A CB  1 
ATOM   1941 C  CG1 . VAL   A 1 247 ? -19.599 19.073 38.773 1.00 18.23 ? 247 VAL   A CG1 1 
ATOM   1942 C  CG2 . VAL   A 1 247 ? -17.405 19.666 39.815 1.00 18.25 ? 247 VAL   A CG2 1 
ATOM   1943 N  N   . ASP   A 1 248 ? -18.323 19.411 35.305 1.00 19.90 ? 248 ASP   A N   1 
ATOM   1944 C  CA  . ASP   A 1 248 ? -19.151 19.264 34.121 1.00 19.55 ? 248 ASP   A CA  1 
ATOM   1945 C  C   . ASP   A 1 248 ? -18.647 18.120 33.252 1.00 17.99 ? 248 ASP   A C   1 
ATOM   1946 O  O   . ASP   A 1 248 ? -19.451 17.379 32.714 1.00 18.91 ? 248 ASP   A O   1 
ATOM   1947 C  CB  . ASP   A 1 248 ? -19.168 20.542 33.308 1.00 21.47 ? 248 ASP   A CB  1 
ATOM   1948 C  CG  . ASP   A 1 248 ? -19.955 21.662 33.980 1.00 23.82 ? 248 ASP   A CG  1 
ATOM   1949 O  OD1 . ASP   A 1 248 ? -20.734 21.347 34.906 1.00 23.99 ? 248 ASP   A OD1 1 
ATOM   1950 O  OD2 . ASP   A 1 248 ? -19.774 22.842 33.568 1.00 25.82 ? 248 ASP   A OD2 1 
ATOM   1951 N  N   . ILE   A 1 249 ? -17.322 17.959 33.144 1.00 16.59 ? 249 ILE   A N   1 
ATOM   1952 C  CA  . ILE   A 1 249 ? -16.716 16.910 32.354 1.00 16.76 ? 249 ILE   A CA  1 
ATOM   1953 C  C   . ILE   A 1 249 ? -16.981 15.513 32.943 1.00 15.13 ? 249 ILE   A C   1 
ATOM   1954 O  O   . ILE   A 1 249 ? -17.002 14.540 32.186 1.00 15.85 ? 249 ILE   A O   1 
ATOM   1955 C  CB  . ILE   A 1 249 ? -15.237 17.264 32.167 1.00 21.26 ? 249 ILE   A CB  1 
ATOM   1956 C  CG1 . ILE   A 1 249 ? -15.076 18.375 31.089 1.00 23.76 ? 249 ILE   A CG1 1 
ATOM   1957 C  CG2 . ILE   A 1 249 ? -14.386 16.054 31.859 1.00 25.80 ? 249 ILE   A CG2 1 
ATOM   1958 C  CD1 . ILE   A 1 249 ? -13.846 19.255 31.320 1.00 29.53 ? 249 ILE   A CD1 1 
ATOM   1959 N  N   . LEU   A 1 250 ? -17.174 15.416 34.261 1.00 13.33 ? 250 LEU   A N   1 
ATOM   1960 C  CA  . LEU   A 1 250 ? -17.501 14.165 34.938 1.00 13.62 ? 250 LEU   A CA  1 
ATOM   1961 C  C   . LEU   A 1 250 ? -18.985 13.817 34.818 1.00 13.40 ? 250 LEU   A C   1 
ATOM   1962 O  O   . LEU   A 1 250 ? -19.382 12.747 35.269 1.00 13.38 ? 250 LEU   A O   1 
ATOM   1963 C  CB  . LEU   A 1 250 ? -17.084 14.209 36.409 1.00 13.80 ? 250 LEU   A CB  1 
ATOM   1964 C  CG  . LEU   A 1 250 ? -15.584 14.107 36.718 1.00 14.43 ? 250 LEU   A CG  1 
ATOM   1965 C  CD1 . LEU   A 1 250 ? -15.299 14.521 38.156 1.00 14.16 ? 250 LEU   A CD1 1 
ATOM   1966 C  CD2 . LEU   A 1 250 ? -15.073 12.682 36.509 1.00 13.37 ? 250 LEU   A CD2 1 
ATOM   1967 N  N   . GLY   A 1 251 ? -19.791 14.687 34.185 1.00 14.54 ? 251 GLY   A N   1 
ATOM   1968 C  CA  . GLY   A 1 251 ? -21.240 14.546 34.115 1.00 14.03 ? 251 GLY   A CA  1 
ATOM   1969 C  C   . GLY   A 1 251 ? -21.660 13.217 33.485 1.00 14.69 ? 251 GLY   A C   1 
ATOM   1970 O  O   . GLY   A 1 251 ? -22.495 12.515 34.033 1.00 14.58 ? 251 GLY   A O   1 
ATOM   1971 N  N   . PRO   A 1 252 ? -21.102 12.813 32.326 1.00 16.82 ? 252 PRO   A N   1 
ATOM   1972 C  CA  . PRO   A 1 252 ? -21.417 11.515 31.728 1.00 15.91 ? 252 PRO   A CA  1 
ATOM   1973 C  C   . PRO   A 1 252 ? -21.235 10.330 32.677 1.00 17.01 ? 252 PRO   A C   1 
ATOM   1974 O  O   . PRO   A 1 252 ? -22.087 9.428  32.709 1.00 14.59 ? 252 PRO   A O   1 
ATOM   1975 C  CB  . PRO   A 1 252 ? -20.515 11.442 30.479 1.00 18.28 ? 252 PRO   A CB  1 
ATOM   1976 C  CG  . PRO   A 1 252 ? -20.304 12.904 30.107 1.00 18.01 ? 252 PRO   A CG  1 
ATOM   1977 C  CD  . PRO   A 1 252 ? -20.249 13.633 31.440 1.00 18.73 ? 252 PRO   A CD  1 
ATOM   1978 N  N   . LEU   A 1 253 ? -20.102 10.282 33.389 1.00 14.33 ? 253 LEU   A N   1 
ATOM   1979 C  CA  . LEU   A 1 253 ? -19.856 9.165  34.302 1.00 14.68 ? 253 LEU   A CA  1 
ATOM   1980 C  C   . LEU   A 1 253 ? -20.819 9.233  35.482 1.00 13.13 ? 253 LEU   A C   1 
ATOM   1981 O  O   . LEU   A 1 253 ? -21.320 8.213  35.966 1.00 14.58 ? 253 LEU   A O   1 
ATOM   1982 C  CB  . LEU   A 1 253 ? -18.391 9.121  34.750 1.00 13.95 ? 253 LEU   A CB  1 
ATOM   1983 C  CG  . LEU   A 1 253 ? -17.386 8.742  33.659 1.00 13.93 ? 253 LEU   A CG  1 
ATOM   1984 C  CD1 . LEU   A 1 253 ? -15.953 9.012  34.057 1.00 15.04 ? 253 LEU   A CD1 1 
ATOM   1985 C  CD2 . LEU   A 1 253 ? -17.567 7.256  33.391 1.00 15.42 ? 253 LEU   A CD2 1 
ATOM   1986 N  N   . SER   A 1 254 ? -21.066 10.439 35.981 1.00 14.00 ? 254 SER   A N   1 
ATOM   1987 C  CA  . SER   A 1 254 ? -22.005 10.624 37.071 1.00 14.17 ? 254 SER   A CA  1 
ATOM   1988 C  C   . SER   A 1 254 ? -23.401 10.144 36.674 1.00 14.51 ? 254 SER   A C   1 
ATOM   1989 O  O   . SER   A 1 254 ? -24.079 9.483  37.460 1.00 15.74 ? 254 SER   A O   1 
ATOM   1990 C  CB  . SER   A 1 254 ? -22.004 12.068 37.502 1.00 14.29 ? 254 SER   A CB  1 
ATOM   1991 O  OG  . SER   A 1 254 ? -22.983 12.272 38.492 1.00 15.71 ? 254 SER   A OG  1 
ATOM   1992 N  N   . ALA   A 1 255 ? -23.804 10.422 35.439 1.00 15.28 ? 255 ALA   A N   1 
ATOM   1993 C  CA  . ALA   A 1 255 ? -25.139 10.064 34.975 1.00 15.65 ? 255 ALA   A CA  1 
ATOM   1994 C  C   . ALA   A 1 255 ? -25.238 8.543  34.800 1.00 16.45 ? 255 ALA   A C   1 
ATOM   1995 O  O   . ALA   A 1 255 ? -26.227 7.914  35.185 1.00 16.76 ? 255 ALA   A O   1 
ATOM   1996 C  CB  . ALA   A 1 255 ? -25.439 10.823 33.678 1.00 16.97 ? 255 ALA   A CB  1 
ATOM   1997 N  N   . GLN   A 1 256 ? -24.168 7.936  34.272 1.00 15.21 ? 256 GLN   A N   1 
ATOM   1998 C  CA  . GLN   A 1 256 ? -24.158 6.508  34.030 1.00 17.84 ? 256 GLN   A CA  1 
ATOM   1999 C  C   . GLN   A 1 256 ? -24.305 5.720  35.334 1.00 17.75 ? 256 GLN   A C   1 
ATOM   2000 O  O   . GLN   A 1 256 ? -25.069 4.756  35.420 1.00 18.76 ? 256 GLN   A O   1 
ATOM   2001 C  CB  . GLN   A 1 256 ? -22.863 6.124  33.303 1.00 20.31 ? 256 GLN   A CB  1 
ATOM   2002 C  CG  . GLN   A 1 256 ? -22.761 4.622  33.073 1.00 24.35 ? 256 GLN   A CG  1 
ATOM   2003 C  CD  . GLN   A 1 256 ? -21.504 4.178  32.363 1.00 26.82 ? 256 GLN   A CD  1 
ATOM   2004 O  OE1 . GLN   A 1 256 ? -20.775 4.970  31.763 1.00 30.11 ? 256 GLN   A OE1 1 
ATOM   2005 N  NE2 . GLN   A 1 256 ? -21.244 2.882  32.433 1.00 26.05 ? 256 GLN   A NE2 1 
ATOM   2006 N  N   . THR   A 1 257 ? -23.619 6.170  36.386 1.00 16.72 ? 257 THR   A N   1 
ATOM   2007 C  CA  . THR   A 1 257 ? -23.545 5.400  37.618 1.00 16.43 ? 257 THR   A CA  1 
ATOM   2008 C  C   . THR   A 1 257 ? -24.609 5.834  38.599 1.00 16.49 ? 257 THR   A C   1 
ATOM   2009 O  O   . THR   A 1 257 ? -24.802 5.176  39.609 1.00 16.36 ? 257 THR   A O   1 
ATOM   2010 C  CB  . THR   A 1 257 ? -22.162 5.564  38.235 1.00 15.61 ? 257 THR   A CB  1 
ATOM   2011 O  OG1 . THR   A 1 257 ? -21.975 6.950  38.571 1.00 14.27 ? 257 THR   A OG1 1 
ATOM   2012 C  CG2 . THR   A 1 257 ? -21.111 4.952  37.322 1.00 16.01 ? 257 THR   A CG2 1 
ATOM   2013 N  N   . GLY   A 1 258 ? -25.173 7.022  38.372 1.00 16.32 ? 258 GLY   A N   1 
ATOM   2014 C  CA  . GLY   A 1 258 ? -26.124 7.595  39.302 1.00 18.05 ? 258 GLY   A CA  1 
ATOM   2015 C  C   . GLY   A 1 258 ? -25.489 8.088  40.601 1.00 19.24 ? 258 GLY   A C   1 
ATOM   2016 O  O   . GLY   A 1 258 ? -26.194 8.189  41.594 1.00 23.61 ? 258 GLY   A O   1 
ATOM   2017 N  N   . ILE   A 1 259 ? -24.192 8.433  40.583 1.00 16.11 ? 259 ILE   A N   1 
ATOM   2018 C  CA  . ILE   A 1 259 ? -23.495 8.987  41.730 1.00 16.79 ? 259 ILE   A CA  1 
ATOM   2019 C  C   . ILE   A 1 259 ? -23.124 10.418 41.403 1.00 16.19 ? 259 ILE   A C   1 
ATOM   2020 O  O   . ILE   A 1 259 ? -22.276 10.657 40.533 1.00 15.36 ? 259 ILE   A O   1 
ATOM   2021 C  CB  . ILE   A 1 259 ? -22.237 8.169  42.076 1.00 16.86 ? 259 ILE   A CB  1 
ATOM   2022 C  CG1 . ILE   A 1 259 ? -22.600 6.704  42.338 1.00 17.33 ? 259 ILE   A CG1 1 
ATOM   2023 C  CG2 . ILE   A 1 259 ? -21.463 8.828  43.229 1.00 17.30 ? 259 ILE   A CG2 1 
ATOM   2024 C  CD1 . ILE   A 1 259 ? -21.398 5.783  42.445 1.00 18.58 ? 259 ILE   A CD1 1 
ATOM   2025 N  N   . ALA   A 1 260 ? -23.737 11.367 42.133 1.00 16.66 ? 260 ALA   A N   1 
ATOM   2026 C  CA  . ALA   A 1 260 ? -23.367 12.764 41.968 1.00 16.12 ? 260 ALA   A CA  1 
ATOM   2027 C  C   . ALA   A 1 260 ? -21.857 12.966 42.166 1.00 16.76 ? 260 ALA   A C   1 
ATOM   2028 O  O   . ALA   A 1 260 ? -21.220 12.353 43.020 1.00 14.96 ? 260 ALA   A O   1 
ATOM   2029 C  CB  . ALA   A 1 260 ? -24.177 13.652 42.923 1.00 16.36 ? 260 ALA   A CB  1 
ATOM   2030 N  N   . VAL   A 1 261 ? -21.295 13.913 41.420 1.00 15.87 ? 261 VAL   A N   1 
ATOM   2031 C  CA  . VAL   A 1 261 ? -19.882 14.209 41.496 1.00 16.85 ? 261 VAL   A CA  1 
ATOM   2032 C  C   . VAL   A 1 261 ? -19.489 14.604 42.925 1.00 16.63 ? 261 VAL   A C   1 
ATOM   2033 O  O   . VAL   A 1 261 ? -18.514 14.079 43.470 1.00 14.91 ? 261 VAL   A O   1 
ATOM   2034 C  CB  . VAL   A 1 261 ? -19.490 15.278 40.453 1.00 18.43 ? 261 VAL   A CB  1 
ATOM   2035 C  CG1 . VAL   A 1 261 ? -18.092 15.817 40.734 1.00 19.29 ? 261 VAL   A CG1 1 
ATOM   2036 C  CG2 . VAL   A 1 261 ? -19.580 14.709 39.030 1.00 18.76 ? 261 VAL   A CG2 1 
ATOM   2037 N  N   . LEU   A 1 262 ? -20.262 15.479 43.575 1.00 16.52 ? 262 LEU   A N   1 
ATOM   2038 C  CA  . LEU   A 1 262 ? -19.899 15.884 44.923 1.00 16.97 ? 262 LEU   A CA  1 
ATOM   2039 C  C   . LEU   A 1 262 ? -20.052 14.733 45.919 1.00 16.87 ? 262 LEU   A C   1 
ATOM   2040 O  O   . LEU   A 1 262 ? -19.375 14.731 46.939 1.00 18.05 ? 262 LEU   A O   1 
ATOM   2041 C  CB  . LEU   A 1 262 ? -20.736 17.102 45.328 1.00 19.08 ? 262 LEU   A CB  1 
ATOM   2042 C  CG  . LEU   A 1 262 ? -20.428 18.369 44.542 1.00 20.14 ? 262 LEU   A CG  1 
ATOM   2043 C  CD1 . LEU   A 1 262 ? -21.412 19.405 45.047 1.00 23.50 ? 262 LEU   A CD1 1 
ATOM   2044 C  CD2 . LEU   A 1 262 ? -18.986 18.818 44.705 1.00 20.86 ? 262 LEU   A CD2 1 
ATOM   2045 N  N   . ASP   A 1 263 ? -20.921 13.756 45.660 1.00 17.22 ? 263 ASP   A N   1 
ATOM   2046 C  CA  . ASP   A 1 263 ? -20.932 12.540 46.470 1.00 17.36 ? 263 ASP   A CA  1 
ATOM   2047 C  C   . ASP   A 1 263 ? -19.649 11.729 46.268 1.00 17.08 ? 263 ASP   A C   1 
ATOM   2048 O  O   . ASP   A 1 263 ? -19.035 11.220 47.210 1.00 16.53 ? 263 ASP   A O   1 
ATOM   2049 C  CB  . ASP   A 1 263 ? -22.180 11.716 46.222 1.00 19.95 ? 263 ASP   A CB  1 
ATOM   2050 C  CG  . ASP   A 1 263 ? -23.518 12.357 46.588 1.00 24.52 ? 263 ASP   A CG  1 
ATOM   2051 O  OD1 . ASP   A 1 263 ? -23.550 13.551 46.982 1.00 22.40 ? 263 ASP   A OD1 1 
ATOM   2052 O  OD2 . ASP   A 1 263 ? -24.544 11.668 46.416 1.00 28.53 ? 263 ASP   A OD2 1 
ATOM   2053 N  N   . MET   A 1 264 ? -19.182 11.602 45.027 1.00 16.96 ? 264 MET   A N   1 
ATOM   2054 C  CA  . MET   A 1 264 ? -17.903 10.938 44.811 1.00 16.71 ? 264 MET   A CA  1 
ATOM   2055 C  C   . MET   A 1 264 ? -16.774 11.734 45.469 1.00 15.17 ? 264 MET   A C   1 
ATOM   2056 O  O   . MET   A 1 264 ? -15.833 11.145 45.989 1.00 18.21 ? 264 MET   A O   1 
ATOM   2057 C  CB  . MET   A 1 264 ? -17.611 10.717 43.319 1.00 15.74 ? 264 MET   A CB  1 
ATOM   2058 C  CG  . MET   A 1 264 ? -16.456 9.762  43.075 1.00 16.18 ? 264 MET   A CG  1 
ATOM   2059 S  SD  . MET   A 1 264 ? -16.820 8.076  43.603 1.00 15.72 ? 264 MET   A SD  1 
ATOM   2060 C  CE  . MET   A 1 264 ? -17.611 7.385  42.141 1.00 16.54 ? 264 MET   A CE  1 
ATOM   2061 N  N   . CYS   A 1 265 ? -16.872 13.067 45.500 1.00 16.00 ? 265 CYS   A N   1 
ATOM   2062 C  CA  . CYS   A 1 265 ? -15.875 13.892 46.164 1.00 16.39 ? 265 CYS   A CA  1 
ATOM   2063 C  C   . CYS   A 1 265 ? -15.857 13.561 47.654 1.00 15.74 ? 265 CYS   A C   1 
ATOM   2064 O  O   . CYS   A 1 265 ? -14.800 13.498 48.256 1.00 16.19 ? 265 CYS   A O   1 
ATOM   2065 C  CB  . CYS   A 1 265 ? -16.112 15.382 45.950 1.00 18.12 ? 265 CYS   A CB  1 
ATOM   2066 S  SG  . CYS   A 1 265 ? -15.728 15.957 44.273 1.00 19.05 ? 265 CYS   A SG  1 
ATOM   2067 N  N   . ALA   A 1 266 ? -17.027 13.328 48.252 1.00 15.59 ? 266 ALA   A N   1 
ATOM   2068 C  CA  . ALA   A 1 266 ? -17.031 12.984 49.664 1.00 16.26 ? 266 ALA   A CA  1 
ATOM   2069 C  C   . ALA   A 1 266 ? -16.319 11.661 49.909 1.00 15.42 ? 266 ALA   A C   1 
ATOM   2070 O  O   . ALA   A 1 266 ? -15.710 11.464 50.964 1.00 16.08 ? 266 ALA   A O   1 
ATOM   2071 C  CB  . ALA   A 1 266 ? -18.455 12.934 50.147 1.00 17.02 ? 266 ALA   A CB  1 
ATOM   2072 N  N   . SER   A 1 267 ? -16.477 10.705 48.984 1.00 14.30 ? 267 SER   A N   1 
ATOM   2073 C  CA  . SER   A 1 267 ? -15.808 9.422  49.127 1.00 14.33 ? 267 SER   A CA  1 
ATOM   2074 C  C   . SER   A 1 267 ? -14.295 9.611  48.991 1.00 14.43 ? 267 SER   A C   1 
ATOM   2075 O  O   . SER   A 1 267 ? -13.523 9.002  49.747 1.00 15.18 ? 267 SER   A O   1 
ATOM   2076 C  CB  . SER   A 1 267 ? -16.331 8.358  48.178 1.00 14.79 ? 267 SER   A CB  1 
ATOM   2077 O  OG  . SER   A 1 267 ? -17.683 8.033  48.457 1.00 16.69 ? 267 SER   A OG  1 
ATOM   2078 N  N   . LEU   A 1 268 ? -13.865 10.431 48.027 1.00 13.65 ? 268 LEU   A N   1 
ATOM   2079 C  CA  . LEU   A 1 268 ? -12.461 10.704 47.835 1.00 13.87 ? 268 LEU   A CA  1 
ATOM   2080 C  C   . LEU   A 1 268 ? -11.871 11.382 49.085 1.00 16.07 ? 268 LEU   A C   1 
ATOM   2081 O  O   . LEU   A 1 268 ? -10.757 11.071 49.526 1.00 16.64 ? 268 LEU   A O   1 
ATOM   2082 C  CB  . LEU   A 1 268 ? -12.231 11.536 46.588 1.00 13.70 ? 268 LEU   A CB  1 
ATOM   2083 C  CG  . LEU   A 1 268 ? -10.795 11.953 46.292 1.00 13.45 ? 268 LEU   A CG  1 
ATOM   2084 C  CD1 . LEU   A 1 268 ? -9.850  10.772 46.345 1.00 13.95 ? 268 LEU   A CD1 1 
ATOM   2085 C  CD2 . LEU   A 1 268 ? -10.681 12.658 44.955 1.00 14.21 ? 268 LEU   A CD2 1 
ATOM   2086 N  N   . LYS   A 1 269 ? -12.604 12.332 49.650 1.00 17.23 ? 269 LYS   A N   1 
ATOM   2087 C  CA  . LYS   A 1 269 ? -12.114 13.031 50.832 1.00 19.46 ? 269 LYS   A CA  1 
ATOM   2088 C  C   . LYS   A 1 269 ? -11.798 12.014 51.938 1.00 17.67 ? 269 LYS   A C   1 
ATOM   2089 O  O   . LYS   A 1 269 ? -10.799 12.146 52.633 1.00 20.46 ? 269 LYS   A O   1 
ATOM   2090 C  CB  . LYS   A 1 269 ? -13.176 14.076 51.220 1.00 23.73 ? 269 LYS   A CB  1 
ATOM   2091 C  CG  . LYS   A 1 269 ? -12.937 14.844 52.533 1.00 29.16 ? 269 LYS   A CG  1 
ATOM   2092 C  CD  . LYS   A 1 269 ? -14.107 15.693 53.015 1.00 33.89 ? 269 LYS   A CD  1 
ATOM   2093 C  CE  . LYS   A 1 269 ? -14.594 16.697 51.991 1.00 38.01 ? 269 LYS   A CE  1 
ATOM   2094 N  NZ  . LYS   A 1 269 ? -15.555 17.697 52.498 1.00 40.08 ? 269 LYS   A NZ  1 
ATOM   2095 N  N   . GLU   A 1 270 ? -12.678 11.026 52.131 1.00 16.72 ? 270 GLU   A N   1 
ATOM   2096 C  CA  . GLU   A 1 270 ? -12.494 10.033 53.173 1.00 20.15 ? 270 GLU   A CA  1 
ATOM   2097 C  C   . GLU   A 1 270 ? -11.284 9.139  52.868 1.00 18.57 ? 270 GLU   A C   1 
ATOM   2098 O  O   . GLU   A 1 270 ? -10.527 8.795  53.767 1.00 21.01 ? 270 GLU   A O   1 
ATOM   2099 C  CB  . GLU   A 1 270 ? -13.793 9.259  53.392 1.00 22.81 ? 270 GLU   A CB  1 
ATOM   2100 C  CG  . GLU   A 1 270 ? -13.575 8.076  54.326 1.00 27.68 ? 270 GLU   A CG  1 
ATOM   2101 C  CD  . GLU   A 1 270 ? -14.832 7.382  54.824 1.00 30.82 ? 270 GLU   A CD  1 
ATOM   2102 O  OE1 . GLU   A 1 270 ? -15.929 7.976  54.714 1.00 32.22 ? 270 GLU   A OE1 1 
ATOM   2103 O  OE2 . GLU   A 1 270 ? -14.715 6.221  55.265 1.00 32.52 ? 270 GLU   A OE2 1 
ATOM   2104 N  N   . LEU   A 1 271 ? -11.057 8.786  51.599 1.00 16.21 ? 271 LEU   A N   1 
ATOM   2105 C  CA  . LEU   A 1 271 ? -9.867  8.033  51.221 1.00 16.78 ? 271 LEU   A CA  1 
ATOM   2106 C  C   . LEU   A 1 271 ? -8.607  8.846  51.518 1.00 17.29 ? 271 LEU   A C   1 
ATOM   2107 O  O   . LEU   A 1 271 ? -7.597  8.274  51.924 1.00 18.09 ? 271 LEU   A O   1 
ATOM   2108 C  CB  . LEU   A 1 271 ? -9.878  7.609  49.748 1.00 17.21 ? 271 LEU   A CB  1 
ATOM   2109 C  CG  . LEU   A 1 271 ? -10.876 6.517  49.368 1.00 19.15 ? 271 LEU   A CG  1 
ATOM   2110 C  CD1 . LEU   A 1 271 ? -11.120 6.440  47.879 1.00 18.82 ? 271 LEU   A CD1 1 
ATOM   2111 C  CD2 . LEU   A 1 271 ? -10.494 5.133  49.893 1.00 21.75 ? 271 LEU   A CD2 1 
ATOM   2112 N  N   . LEU   A 1 272 ? -8.647  10.165 51.269 1.00 16.18 ? 272 LEU   A N   1 
ATOM   2113 C  CA  . LEU   A 1 272 ? -7.480  11.010 51.486 1.00 18.55 ? 272 LEU   A CA  1 
ATOM   2114 C  C   . LEU   A 1 272 ? -7.225  11.127 52.981 1.00 19.92 ? 272 LEU   A C   1 
ATOM   2115 O  O   . LEU   A 1 272 ? -6.084  11.145 53.405 1.00 21.44 ? 272 LEU   A O   1 
ATOM   2116 C  CB  . LEU   A 1 272 ? -7.703  12.385 50.861 1.00 18.52 ? 272 LEU   A CB  1 
ATOM   2117 C  CG  . LEU   A 1 272 ? -7.731  12.412 49.329 1.00 19.94 ? 272 LEU   A CG  1 
ATOM   2118 C  CD1 . LEU   A 1 272 ? -7.929  13.827 48.866 1.00 20.89 ? 272 LEU   A CD1 1 
ATOM   2119 C  CD2 . LEU   A 1 272 ? -6.461  11.841 48.754 1.00 22.20 ? 272 LEU   A CD2 1 
ATOM   2120 N  N   . GLN   A 1 273 ? -8.299  11.196 53.757 1.00 22.36 ? 273 GLN   A N   1 
ATOM   2121 C  CA  . GLN   A 1 273 ? -8.149  11.457 55.186 1.00 25.66 ? 273 GLN   A CA  1 
ATOM   2122 C  C   . GLN   A 1 273 ? -7.816  10.183 55.946 1.00 27.17 ? 273 GLN   A C   1 
ATOM   2123 O  O   . GLN   A 1 273 ? -7.084  10.266 56.931 1.00 28.62 ? 273 GLN   A O   1 
ATOM   2124 C  CB  . GLN   A 1 273 ? -9.384  12.143 55.745 1.00 25.87 ? 273 GLN   A CB  1 
ATOM   2125 C  CG  . GLN   A 1 273 ? -9.411  13.623 55.377 1.00 29.46 ? 273 GLN   A CG  1 
ATOM   2126 C  CD  . GLN   A 1 273 ? -10.699 14.312 55.763 1.00 29.59 ? 273 GLN   A CD  1 
ATOM   2127 O  OE1 . GLN   A 1 273 ? -11.756 13.695 55.834 1.00 35.50 ? 273 GLN   A OE1 1 
ATOM   2128 N  NE2 . GLN   A 1 273 ? -10.648 15.620 55.914 1.00 32.13 ? 273 GLN   A NE2 1 
ATOM   2129 N  N   . ASN   A 1 274 ? -8.344  9.027  55.516 1.00 25.96 ? 274 ASN   A N   1 
ATOM   2130 C  CA  . ASN   A 1 274 ? -8.202  7.794  56.278 1.00 27.62 ? 274 ASN   A CA  1 
ATOM   2131 C  C   . ASN   A 1 274 ? -7.284  6.769  55.621 1.00 30.11 ? 274 ASN   A C   1 
ATOM   2132 O  O   . ASN   A 1 274 ? -6.969  5.773  56.259 1.00 28.91 ? 274 ASN   A O   1 
ATOM   2133 C  CB  . ASN   A 1 274 ? -9.543  7.113  56.465 1.00 28.72 ? 274 ASN   A CB  1 
ATOM   2134 C  CG  . ASN   A 1 274 ? -10.498 7.988  57.223 1.00 32.83 ? 274 ASN   A CG  1 
ATOM   2135 O  OD1 . ASN   A 1 274 ? -10.080 8.910  57.922 1.00 39.10 ? 274 ASN   A OD1 1 
ATOM   2136 N  ND2 . ASN   A 1 274 ? -11.781 7.696  57.123 1.00 42.49 ? 274 ASN   A ND2 1 
ATOM   2137 N  N   . GLY   A 1 275 ? -6.913  6.963  54.342 1.00 27.71 ? 275 GLY   A N   1 
ATOM   2138 C  CA  . GLY   A 1 275 ? -6.166  5.968  53.589 1.00 25.50 ? 275 GLY   A CA  1 
ATOM   2139 C  C   . GLY   A 1 275 ? -7.043  4.807  53.120 1.00 23.98 ? 275 GLY   A C   1 
ATOM   2140 O  O   . GLY   A 1 275 ? -8.241  4.746  53.403 1.00 26.52 ? 275 GLY   A O   1 
ATOM   2141 N  N   . MET   A 1 276 ? -6.421  3.866  52.407 1.00 27.04 ? 276 MET   A N   1 
ATOM   2142 C  CA  . MET   A 1 276 ? -7.107  2.718  51.839 1.00 29.09 ? 276 MET   A CA  1 
ATOM   2143 C  C   . MET   A 1 276 ? -7.103  1.524  52.803 1.00 32.16 ? 276 MET   A C   1 
ATOM   2144 O  O   . MET   A 1 276 ? -7.747  0.518  52.532 1.00 29.99 ? 276 MET   A O   1 
ATOM   2145 C  CB  . MET   A 1 276 ? -6.505  2.356  50.472 1.00 31.53 ? 276 MET   A CB  1 
ATOM   2146 C  CG  . MET   A 1 276 ? -7.084  3.167  49.301 1.00 35.03 ? 276 MET   A CG  1 
ATOM   2147 S  SD  . MET   A 1 276 ? -6.479  2.655  47.673 1.00 45.60 ? 276 MET   A SD  1 
ATOM   2148 C  CE  . MET   A 1 276 ? -5.241  3.939  47.814 1.00 36.25 ? 276 MET   A CE  1 
ATOM   2149 N  N   . ASN   A 1 277 ? -6.380  1.624  53.933 1.00 40.21 ? 277 ASN   A N   1 
ATOM   2150 C  CA  . ASN   A 1 277 ? -6.355  0.589  54.968 1.00 43.87 ? 277 ASN   A CA  1 
ATOM   2151 C  C   . ASN   A 1 277 ? -6.018  -0.792 54.394 1.00 40.27 ? 277 ASN   A C   1 
ATOM   2152 O  O   . ASN   A 1 277 ? -6.643  -1.778 54.766 1.00 43.97 ? 277 ASN   A O   1 
ATOM   2153 C  CB  . ASN   A 1 277 ? -7.661  0.578  55.756 1.00 49.12 ? 277 ASN   A CB  1 
ATOM   2154 C  CG  . ASN   A 1 277 ? -7.897  1.907  56.439 1.00 62.27 ? 277 ASN   A CG  1 
ATOM   2155 O  OD1 . ASN   A 1 277 ? -7.897  2.961  55.788 1.00 68.93 ? 277 ASN   A OD1 1 
ATOM   2156 N  ND2 . ASN   A 1 277 ? -8.073  1.892  57.750 1.00 68.02 ? 277 ASN   A ND2 1 
ATOM   2157 N  N   . GLY   A 1 278 ? -5.040  -0.858 53.484 1.00 40.53 ? 278 GLY   A N   1 
ATOM   2158 C  CA  . GLY   A 1 278 ? -4.564  -2.126 52.944 1.00 41.23 ? 278 GLY   A CA  1 
ATOM   2159 C  C   . GLY   A 1 278 ? -5.451  -2.711 51.834 1.00 41.66 ? 278 GLY   A C   1 
ATOM   2160 O  O   . GLY   A 1 278 ? -5.134  -3.773 51.296 1.00 41.46 ? 278 GLY   A O   1 
ATOM   2161 N  N   . ARG   A 1 279 ? -6.556  -2.044 51.472 1.00 36.39 ? 279 ARG   A N   1 
ATOM   2162 C  CA  . ARG   A 1 279 ? -7.394  -2.513 50.373 1.00 31.29 ? 279 ARG   A CA  1 
ATOM   2163 C  C   . ARG   A 1 279 ? -6.935  -1.914 49.048 1.00 26.21 ? 279 ARG   A C   1 
ATOM   2164 O  O   . ARG   A 1 279 ? -6.180  -0.957 49.045 1.00 27.26 ? 279 ARG   A O   1 
ATOM   2165 C  CB  . ARG   A 1 279 ? -8.836  -2.051 50.561 1.00 31.69 ? 279 ARG   A CB  1 
ATOM   2166 C  CG  . ARG   A 1 279 ? -9.359  -2.467 51.922 1.00 33.07 ? 279 ARG   A CG  1 
ATOM   2167 C  CD  . ARG   A 1 279 ? -10.837 -2.388 51.943 1.00 31.66 ? 279 ARG   A CD  1 
ATOM   2168 N  NE  . ARG   A 1 279 ? -11.431 -3.320 50.982 1.00 32.01 ? 279 ARG   A NE  1 
ATOM   2169 C  CZ  . ARG   A 1 279 ? -12.717 -3.611 51.030 1.00 30.19 ? 279 ARG   A CZ  1 
ATOM   2170 N  NH1 . ARG   A 1 279 ? -13.236 -4.447 50.161 1.00 29.18 ? 279 ARG   A NH1 1 
ATOM   2171 N  NH2 . ARG   A 1 279 ? -13.454 -3.050 51.958 1.00 30.28 ? 279 ARG   A NH2 1 
ATOM   2172 N  N   . THR   A 1 280 ? -7.409  -2.494 47.940 1.00 23.77 ? 280 THR   A N   1 
ATOM   2173 C  CA  . THR   A 1 280 ? -7.058  -2.051 46.598 1.00 19.97 ? 280 THR   A CA  1 
ATOM   2174 C  C   . THR   A 1 280 ? -8.328  -1.544 45.932 1.00 22.25 ? 280 THR   A C   1 
ATOM   2175 O  O   . THR   A 1 280 ? -9.430  -1.896 46.355 1.00 21.57 ? 280 THR   A O   1 
ATOM   2176 C  CB  . THR   A 1 280 ? -6.406  -3.179 45.786 1.00 21.73 ? 280 THR   A CB  1 
ATOM   2177 O  OG1 . THR   A 1 280 ? -7.329  -4.262 45.664 1.00 21.02 ? 280 THR   A OG1 1 
ATOM   2178 C  CG2 . THR   A 1 280 ? -5.095  -3.653 46.385 1.00 22.10 ? 280 THR   A CG2 1 
ATOM   2179 N  N   . ILE   A 1 281 ? -8.147  -0.683 44.930 1.00 20.09 ? 281 ILE   A N   1 
ATOM   2180 C  CA  . ILE   A 1 281 ? -9.213  -0.266 44.031 1.00 18.99 ? 281 ILE   A CA  1 
ATOM   2181 C  C   . ILE   A 1 281 ? -8.720  -0.566 42.622 1.00 19.60 ? 281 ILE   A C   1 
ATOM   2182 O  O   . ILE   A 1 281 ? -7.654  -0.096 42.232 1.00 17.89 ? 281 ILE   A O   1 
ATOM   2183 C  CB  . ILE   A 1 281 ? -9.578  1.222  44.212 1.00 17.95 ? 281 ILE   A CB  1 
ATOM   2184 C  CG1 . ILE   A 1 281 ? -10.054 1.512  45.612 1.00 16.27 ? 281 ILE   A CG1 1 
ATOM   2185 C  CG2 . ILE   A 1 281 ? -10.629 1.671  43.184 1.00 17.46 ? 281 ILE   A CG2 1 
ATOM   2186 C  CD1 . ILE   A 1 281 ? -10.181 2.996  45.928 1.00 17.88 ? 281 ILE   A CD1 1 
ATOM   2187 N  N   . LEU   A 1 282 ? -9.451  -1.424 41.892 1.00 19.54 ? 282 LEU   A N   1 
ATOM   2188 C  CA  . LEU   A 1 282 ? -9.071  -1.821 40.544 1.00 20.56 ? 282 LEU   A CA  1 
ATOM   2189 C  C   . LEU   A 1 282 ? -7.655  -2.374 40.546 1.00 23.11 ? 282 LEU   A C   1 
ATOM   2190 O  O   . LEU   A 1 282 ? -6.870  -2.099 39.639 1.00 21.75 ? 282 LEU   A O   1 
ATOM   2191 C  CB  . LEU   A 1 282 ? -9.232  -0.658 39.570 1.00 20.49 ? 282 LEU   A CB  1 
ATOM   2192 C  CG  . LEU   A 1 282 ? -10.673 -0.337 39.145 1.00 21.04 ? 282 LEU   A CG  1 
ATOM   2193 C  CD1 . LEU   A 1 282 ? -10.730 0.942  38.352 1.00 22.45 ? 282 LEU   A CD1 1 
ATOM   2194 C  CD2 . LEU   A 1 282 ? -11.306 -1.470 38.369 1.00 21.00 ? 282 LEU   A CD2 1 
ATOM   2195 N  N   . GLY   A 1 283 ? -7.337  -3.140 41.601 1.00 23.85 ? 283 GLY   A N   1 
ATOM   2196 C  CA  . GLY   A 1 283 ? -6.059  -3.835 41.674 1.00 27.25 ? 283 GLY   A CA  1 
ATOM   2197 C  C   . GLY   A 1 283 ? -4.936  -2.952 42.213 1.00 27.77 ? 283 GLY   A C   1 
ATOM   2198 O  O   . GLY   A 1 283 ? -3.862  -3.469 42.519 1.00 31.39 ? 283 GLY   A O   1 
ATOM   2199 N  N   . SER   A 1 284 ? -5.199  -1.636 42.375 1.00 24.75 ? 284 SER   A N   1 
ATOM   2200 C  CA  . SER   A 1 284 ? -4.180  -0.670 42.752 1.00 23.13 ? 284 SER   A CA  1 
ATOM   2201 C  C   . SER   A 1 284 ? -4.248  -0.310 44.238 1.00 20.60 ? 284 SER   A C   1 
ATOM   2202 O  O   . SER   A 1 284 ? -5.308  -0.121 44.839 1.00 17.37 ? 284 SER   A O   1 
ATOM   2203 C  CB  . SER   A 1 284 ? -4.229  0.565  41.865 1.00 25.03 ? 284 SER   A CB  1 
ATOM   2204 O  OG  . SER   A 1 284 ? -3.403  1.577  42.425 1.00 29.40 ? 284 SER   A OG  1 
ATOM   2205 N  N   . ALA   A 1 285 ? -3.069  -0.186 44.846 1.00 20.95 ? 285 ALA   A N   1 
ATOM   2206 C  CA  . ALA   A 1 285 ? -3.000  0.141  46.255 1.00 22.56 ? 285 ALA   A CA  1 
ATOM   2207 C  C   . ALA   A 1 285 ? -2.828  1.646  46.455 1.00 21.99 ? 285 ALA   A C   1 
ATOM   2208 O  O   . ALA   A 1 285 ? -2.821  2.119  47.579 1.00 23.17 ? 285 ALA   A O   1 
ATOM   2209 C  CB  . ALA   A 1 285 ? -1.887  -0.664 46.900 1.00 24.39 ? 285 ALA   A CB  1 
ATOM   2210 N  N   . LEU   A 1 286 ? -2.702  2.405  45.363 1.00 20.39 ? 286 LEU   A N   1 
ATOM   2211 C  CA  . LEU   A 1 286 ? -2.644  3.863  45.404 1.00 21.13 ? 286 LEU   A CA  1 
ATOM   2212 C  C   . LEU   A 1 286 ? -3.751  4.407  44.513 1.00 19.67 ? 286 LEU   A C   1 
ATOM   2213 O  O   . LEU   A 1 286 ? -4.136  3.719  43.582 1.00 20.60 ? 286 LEU   A O   1 
ATOM   2214 C  CB  . LEU   A 1 286 ? -1.331  4.330  44.811 1.00 23.79 ? 286 LEU   A CB  1 
ATOM   2215 C  CG  . LEU   A 1 286 ? -0.068  3.699  45.389 1.00 27.98 ? 286 LEU   A CG  1 
ATOM   2216 C  CD1 . LEU   A 1 286 ? 1.095   4.054  44.454 1.00 28.91 ? 286 LEU   A CD1 1 
ATOM   2217 C  CD2 . LEU   A 1 286 ? 0.107   4.193  46.806 1.00 27.97 ? 286 LEU   A CD2 1 
ATOM   2218 N  N   . LEU   A 1 287 ? -4.156  5.659  44.738 1.00 18.73 ? 287 LEU   A N   1 
ATOM   2219 C  CA  . LEU   A 1 287 ? -5.155  6.299  43.899 1.00 18.00 ? 287 LEU   A CA  1 
ATOM   2220 C  C   . LEU   A 1 287 ? -4.476  6.690  42.600 1.00 18.42 ? 287 LEU   A C   1 
ATOM   2221 O  O   . LEU   A 1 287 ? -3.374  7.240  42.628 1.00 19.71 ? 287 LEU   A O   1 
ATOM   2222 C  CB  . LEU   A 1 287 ? -5.732  7.499  44.631 1.00 18.36 ? 287 LEU   A CB  1 
ATOM   2223 C  CG  . LEU   A 1 287 ? -6.349  7.197  46.000 1.00 19.21 ? 287 LEU   A CG  1 
ATOM   2224 C  CD1 . LEU   A 1 287 ? -6.816  8.449  46.728 1.00 20.73 ? 287 LEU   A CD1 1 
ATOM   2225 C  CD2 . LEU   A 1 287 ? -7.488  6.256  45.823 1.00 20.63 ? 287 LEU   A CD2 1 
ATOM   2226 N  N   A GLU   A 1 288 ? -5.112  6.368  41.471 0.50 17.98 ? 288 GLU   A N   1 
ATOM   2227 N  N   B GLU   A 1 288 ? -5.118  6.368  41.479 0.50 16.87 ? 288 GLU   A N   1 
ATOM   2228 C  CA  A GLU   A 1 288 ? -4.508  6.575  40.167 0.50 18.36 ? 288 GLU   A CA  1 
ATOM   2229 C  CA  B GLU   A 1 288 ? -4.531  6.583  40.172 0.50 16.42 ? 288 GLU   A CA  1 
ATOM   2230 C  C   A GLU   A 1 288 ? -5.065  7.841  39.516 0.50 16.79 ? 288 GLU   A C   1 
ATOM   2231 C  C   B GLU   A 1 288 ? -5.067  7.865  39.540 0.50 15.79 ? 288 GLU   A C   1 
ATOM   2232 O  O   A GLU   A 1 288 ? -6.278  8.075  39.535 0.50 15.62 ? 288 GLU   A O   1 
ATOM   2233 O  O   B GLU   A 1 288 ? -6.274  8.118  39.574 0.50 14.79 ? 288 GLU   A O   1 
ATOM   2234 C  CB  A GLU   A 1 288 ? -4.741  5.335  39.305 0.50 21.11 ? 288 GLU   A CB  1 
ATOM   2235 C  CB  B GLU   A 1 288 ? -4.901  5.393  39.296 0.50 17.29 ? 288 GLU   A CB  1 
ATOM   2236 C  CG  A GLU   A 1 288 ? -4.273  4.042  39.966 0.50 22.49 ? 288 GLU   A CG  1 
ATOM   2237 C  CG  B GLU   A 1 288 ? -4.603  5.651  37.826 0.50 17.13 ? 288 GLU   A CG  1 
ATOM   2238 C  CD  A GLU   A 1 288 ? -3.416  3.222  39.039 0.50 27.29 ? 288 GLU   A CD  1 
ATOM   2239 C  CD  B GLU   A 1 288 ? -3.132  5.492  37.480 0.50 17.63 ? 288 GLU   A CD  1 
ATOM   2240 O  OE1 A GLU   A 1 288 ? -3.916  2.313  38.329 0.50 29.34 ? 288 GLU   A OE1 1 
ATOM   2241 O  OE1 B GLU   A 1 288 ? -2.514  4.518  37.974 0.50 19.04 ? 288 GLU   A OE1 1 
ATOM   2242 O  OE2 A GLU   A 1 288 ? -2.216  3.552  39.036 0.50 31.54 ? 288 GLU   A OE2 1 
ATOM   2243 O  OE2 B GLU   A 1 288 ? -2.621  6.291  36.694 0.50 14.89 ? 288 GLU   A OE2 1 
ATOM   2244 N  N   . ASP   A 1 289 ? -4.178  8.635  38.906 1.00 15.83 ? 289 ASP   A N   1 
ATOM   2245 C  CA  . ASP   A 1 289 ? -4.588  9.889  38.310 1.00 15.64 ? 289 ASP   A CA  1 
ATOM   2246 C  C   . ASP   A 1 289 ? -4.221  10.047 36.836 1.00 16.06 ? 289 ASP   A C   1 
ATOM   2247 O  O   . ASP   A 1 289 ? -4.210  11.186 36.353 1.00 15.42 ? 289 ASP   A O   1 
ATOM   2248 C  CB  . ASP   A 1 289 ? -4.064  11.068 39.098 1.00 16.09 ? 289 ASP   A CB  1 
ATOM   2249 C  CG  . ASP   A 1 289 ? -2.586  11.367 38.951 1.00 16.19 ? 289 ASP   A CG  1 
ATOM   2250 O  OD1 . ASP   A 1 289 ? -1.854  10.518 38.407 1.00 16.11 ? 289 ASP   A OD1 1 
ATOM   2251 O  OD2 . ASP   A 1 289 ? -2.206  12.481 39.343 1.00 14.97 ? 289 ASP   A OD2 1 
ATOM   2252 N  N   . GLU   A 1 290 ? -3.943  8.953  36.131 1.00 16.16 ? 290 GLU   A N   1 
ATOM   2253 C  CA  . GLU   A 1 290 ? -3.564  9.067  34.728 1.00 17.24 ? 290 GLU   A CA  1 
ATOM   2254 C  C   . GLU   A 1 290 ? -4.630  8.462  33.816 1.00 16.61 ? 290 GLU   A C   1 
ATOM   2255 O  O   . GLU   A 1 290 ? -4.334  8.046  32.685 1.00 17.48 ? 290 GLU   A O   1 
ATOM   2256 C  CB  . GLU   A 1 290 ? -2.150  8.529  34.482 1.00 20.25 ? 290 GLU   A CB  1 
ATOM   2257 C  CG  . GLU   A 1 290 ? -1.078  9.431  35.103 1.00 22.94 ? 290 GLU   A CG  1 
ATOM   2258 C  CD  . GLU   A 1 290 ? 0.333   9.366  34.533 1.00 24.48 ? 290 GLU   A CD  1 
ATOM   2259 O  OE1 . GLU   A 1 290 ? 0.494   8.541  33.587 1.00 20.38 ? 290 GLU   A OE1 1 
ATOM   2260 O  OE2 . GLU   A 1 290 ? 1.243   10.129 35.035 1.00 22.47 ? 290 GLU   A OE2 1 
ATOM   2261 N  N   . PHE   A 1 291 ? -5.891  8.474  34.264 1.00 15.54 ? 291 PHE   A N   1 
ATOM   2262 C  CA  . PHE   A 1 291 ? -7.021  8.214  33.384 1.00 16.34 ? 291 PHE   A CA  1 
ATOM   2263 C  C   . PHE   A 1 291 ? -7.961  9.419  33.375 1.00 15.99 ? 291 PHE   A C   1 
ATOM   2264 O  O   . PHE   A 1 291 ? -8.483  9.782  34.419 1.00 14.36 ? 291 PHE   A O   1 
ATOM   2265 C  CB  . PHE   A 1 291 ? -7.863  7.010  33.819 1.00 17.23 ? 291 PHE   A CB  1 
ATOM   2266 C  CG  . PHE   A 1 291 ? -7.120  5.698  33.844 1.00 17.88 ? 291 PHE   A CG  1 
ATOM   2267 C  CD1 . PHE   A 1 291 ? -6.983  4.943  32.681 1.00 21.17 ? 291 PHE   A CD1 1 
ATOM   2268 C  CD2 . PHE   A 1 291 ? -6.472  5.282  34.991 1.00 20.23 ? 291 PHE   A CD2 1 
ATOM   2269 C  CE1 . PHE   A 1 291 ? -6.243  3.775  32.696 1.00 23.75 ? 291 PHE   A CE1 1 
ATOM   2270 C  CE2 . PHE   A 1 291 ? -5.772  4.074  35.011 1.00 26.50 ? 291 PHE   A CE2 1 
ATOM   2271 C  CZ  . PHE   A 1 291 ? -5.663  3.327  33.866 1.00 25.25 ? 291 PHE   A CZ  1 
ATOM   2272 N  N   . THR   A 1 292 ? -8.237  9.982  32.191 1.00 15.24 ? 292 THR   A N   1 
ATOM   2273 C  CA  . THR   A 1 292 ? -9.129  11.118 32.095 1.00 14.77 ? 292 THR   A CA  1 
ATOM   2274 C  C   . THR   A 1 292 ? -10.551 10.583 32.108 1.00 14.31 ? 292 THR   A C   1 
ATOM   2275 O  O   . THR   A 1 292 ? -10.763 9.388  31.937 1.00 14.78 ? 292 THR   A O   1 
ATOM   2276 C  CB  . THR   A 1 292 ? -8.929  11.966 30.831 1.00 17.66 ? 292 THR   A CB  1 
ATOM   2277 O  OG1 . THR   A 1 292 ? -9.286  11.158 29.710 1.00 17.74 ? 292 THR   A OG1 1 
ATOM   2278 C  CG2 . THR   A 1 292 ? -7.505  12.462 30.662 1.00 18.24 ? 292 THR   A CG2 1 
ATOM   2279 N  N   . PRO   A 1 293 ? -11.563 11.455 32.302 1.00 14.17 ? 293 PRO   A N   1 
ATOM   2280 C  CA  . PRO   A 1 293 ? -12.955 11.030 32.161 1.00 15.47 ? 293 PRO   A CA  1 
ATOM   2281 C  C   . PRO   A 1 293 ? -13.179 10.389 30.786 1.00 16.73 ? 293 PRO   A C   1 
ATOM   2282 O  O   . PRO   A 1 293 ? -13.888 9.402  30.646 1.00 16.87 ? 293 PRO   A O   1 
ATOM   2283 C  CB  . PRO   A 1 293 ? -13.697 12.318 32.351 1.00 15.42 ? 293 PRO   A CB  1 
ATOM   2284 C  CG  . PRO   A 1 293 ? -12.843 13.099 33.309 1.00 15.46 ? 293 PRO   A CG  1 
ATOM   2285 C  CD  . PRO   A 1 293 ? -11.433 12.842 32.788 1.00 15.14 ? 293 PRO   A CD  1 
ATOM   2286 N  N   . PHE   A 1 294 ? -12.538 10.933 29.762 1.00 18.50 ? 294 PHE   A N   1 
ATOM   2287 C  CA  . PHE   A 1 294 ? -12.760 10.436 28.395 1.00 20.93 ? 294 PHE   A CA  1 
ATOM   2288 C  C   . PHE   A 1 294 ? -12.150 9.043  28.258 1.00 19.86 ? 294 PHE   A C   1 
ATOM   2289 O  O   . PHE   A 1 294 ? -12.764 8.168  27.657 1.00 18.89 ? 294 PHE   A O   1 
ATOM   2290 C  CB  . PHE   A 1 294 ? -12.215 11.446 27.384 1.00 27.61 ? 294 PHE   A CB  1 
ATOM   2291 C  CG  . PHE   A 1 294 ? -12.668 12.860 27.723 1.00 43.42 ? 294 PHE   A CG  1 
ATOM   2292 C  CD1 . PHE   A 1 294 ? -11.960 13.641 28.655 1.00 47.84 ? 294 PHE   A CD1 1 
ATOM   2293 C  CD2 . PHE   A 1 294 ? -13.860 13.373 27.190 1.00 52.88 ? 294 PHE   A CD2 1 
ATOM   2294 C  CE1 . PHE   A 1 294 ? -12.414 14.912 28.986 1.00 53.14 ? 294 PHE   A CE1 1 
ATOM   2295 C  CE2 . PHE   A 1 294 ? -14.306 14.647 27.527 1.00 52.30 ? 294 PHE   A CE2 1 
ATOM   2296 C  CZ  . PHE   A 1 294 ? -13.579 15.417 28.413 1.00 54.87 ? 294 PHE   A CZ  1 
ATOM   2297 N  N   . ASP   A 1 295 ? -10.952 8.832  28.825 1.00 17.51 ? 295 ASP   A N   1 
ATOM   2298 C  CA  . ASP   A 1 295 ? -10.295 7.526  28.834 1.00 18.11 ? 295 ASP   A CA  1 
ATOM   2299 C  C   . ASP   A 1 295 ? -11.182 6.490  29.499 1.00 16.76 ? 295 ASP   A C   1 
ATOM   2300 O  O   . ASP   A 1 295 ? -11.291 5.370  29.021 1.00 17.61 ? 295 ASP   A O   1 
ATOM   2301 C  CB  . ASP   A 1 295 ? -8.974  7.540  29.579 1.00 18.21 ? 295 ASP   A CB  1 
ATOM   2302 C  CG  . ASP   A 1 295 ? -7.874  8.439  29.023 1.00 21.41 ? 295 ASP   A CG  1 
ATOM   2303 O  OD1 . ASP   A 1 295 ? -7.945  8.825  27.833 1.00 23.36 ? 295 ASP   A OD1 1 
ATOM   2304 O  OD2 . ASP   A 1 295 ? -6.974  8.800  29.811 1.00 19.57 ? 295 ASP   A OD2 1 
ATOM   2305 N  N   . VAL   A 1 296 ? -11.847 6.876  30.591 1.00 15.38 ? 296 VAL   A N   1 
ATOM   2306 C  CA  . VAL   A 1 296 ? -12.706 5.939  31.271 1.00 16.83 ? 296 VAL   A CA  1 
ATOM   2307 C  C   . VAL   A 1 296 ? -13.866 5.552  30.356 1.00 18.98 ? 296 VAL   A C   1 
ATOM   2308 O  O   . VAL   A 1 296 ? -14.188 4.362  30.204 1.00 18.97 ? 296 VAL   A O   1 
ATOM   2309 C  CB  . VAL   A 1 296 ? -13.222 6.454  32.619 1.00 16.80 ? 296 VAL   A CB  1 
ATOM   2310 C  CG1 . VAL   A 1 296 ? -14.218 5.467  33.204 1.00 17.19 ? 296 VAL   A CG1 1 
ATOM   2311 C  CG2 . VAL   A 1 296 ? -12.058 6.688  33.535 1.00 17.25 ? 296 VAL   A CG2 1 
ATOM   2312 N  N   . VAL   A 1 297 ? -14.497 6.551  29.771 1.00 20.06 ? 297 VAL   A N   1 
ATOM   2313 C  CA  . VAL   A 1 297 ? -15.655 6.276  28.935 1.00 23.55 ? 297 VAL   A CA  1 
ATOM   2314 C  C   . VAL   A 1 297 ? -15.226 5.461  27.705 1.00 23.83 ? 297 VAL   A C   1 
ATOM   2315 O  O   . VAL   A 1 297 ? -15.875 4.472  27.386 1.00 27.16 ? 297 VAL   A O   1 
ATOM   2316 C  CB  . VAL   A 1 297 ? -16.410 7.563  28.559 1.00 23.74 ? 297 VAL   A CB  1 
ATOM   2317 C  CG1 . VAL   A 1 297 ? -17.319 7.364  27.348 1.00 26.10 ? 297 VAL   A CG1 1 
ATOM   2318 C  CG2 . VAL   A 1 297 ? -17.220 8.056  29.745 1.00 21.70 ? 297 VAL   A CG2 1 
ATOM   2319 N  N   . ARG   A 1 298 ? -14.132 5.848  27.059 1.00 24.70 ? 298 ARG   A N   1 
ATOM   2320 C  CA  . ARG   A 1 298 ? -13.627 5.168  25.862 1.00 29.09 ? 298 ARG   A CA  1 
ATOM   2321 C  C   . ARG   A 1 298 ? -13.434 3.680  26.169 1.00 30.63 ? 298 ARG   A C   1 
ATOM   2322 O  O   . ARG   A 1 298 ? -13.848 2.805  25.408 1.00 33.96 ? 298 ARG   A O   1 
ATOM   2323 C  CB  . ARG   A 1 298 ? -12.334 5.835  25.359 1.00 34.12 ? 298 ARG   A CB  1 
ATOM   2324 C  CG  . ARG   A 1 298 ? -11.473 5.053  24.372 1.00 42.56 ? 298 ARG   A CG  1 
ATOM   2325 C  CD  . ARG   A 1 298 ? -10.105 5.657  23.964 1.00 47.35 ? 298 ARG   A CD  1 
ATOM   2326 N  NE  . ARG   A 1 298 ? -8.949  5.573  24.875 1.00 48.87 ? 298 ARG   A NE  1 
ATOM   2327 C  CZ  . ARG   A 1 298 ? -7.851  4.802  24.744 1.00 51.91 ? 298 ARG   A CZ  1 
ATOM   2328 N  NH1 . ARG   A 1 298 ? -7.797  3.763  23.898 1.00 47.49 ? 298 ARG   A NH1 1 
ATOM   2329 N  NH2 . ARG   A 1 298 ? -6.795  5.060  25.505 1.00 51.24 ? 298 ARG   A NH2 1 
ATOM   2330 N  N   . GLN   A 1 299 ? -12.814 3.399  27.314 1.00 25.39 ? 299 GLN   A N   1 
ATOM   2331 C  CA  . GLN   A 1 299 ? -12.467 2.041  27.673 1.00 26.51 ? 299 GLN   A CA  1 
ATOM   2332 C  C   . GLN   A 1 299 ? -13.709 1.262  28.108 1.00 26.54 ? 299 GLN   A C   1 
ATOM   2333 O  O   . GLN   A 1 299 ? -13.897 0.123  27.691 1.00 31.24 ? 299 GLN   A O   1 
ATOM   2334 C  CB  . GLN   A 1 299 ? -11.358 1.953  28.728 1.00 24.10 ? 299 GLN   A CB  1 
ATOM   2335 C  CG  . GLN   A 1 299 ? -11.060 0.510  29.100 1.00 21.78 ? 299 GLN   A CG  1 
ATOM   2336 C  CD  . GLN   A 1 299 ? -9.773  0.292  29.869 1.00 19.13 ? 299 GLN   A CD  1 
ATOM   2337 O  OE1 . GLN   A 1 299 ? -9.553  -0.801 30.379 1.00 19.84 ? 299 GLN   A OE1 1 
ATOM   2338 N  NE2 . GLN   A 1 299 ? -8.939  1.308  30.015 1.00 18.27 ? 299 GLN   A NE2 1 
ATOM   2339 N  N   . CYS   A 1 300 ? -14.548 1.857  28.948 1.00 26.77 ? 300 CYS   A N   1 
ATOM   2340 C  CA  . CYS   A 1 300 ? -15.750 1.195  29.431 1.00 29.49 ? 300 CYS   A CA  1 
ATOM   2341 C  C   . CYS   A 1 300 ? -16.880 1.147  28.368 1.00 32.21 ? 300 CYS   A C   1 
ATOM   2342 O  O   . CYS   A 1 300 ? -17.823 0.386  28.556 1.00 31.37 ? 300 CYS   A O   1 
ATOM   2343 C  CB  . CYS   A 1 300 ? -16.175 1.812  30.767 1.00 29.89 ? 300 CYS   A CB  1 
ATOM   2344 S  SG  . CYS   A 1 300 ? -14.957 1.627  32.103 1.00 34.38 ? 300 CYS   A SG  1 
ATOM   2345 N  N   . SER   A 1 301 ? -16.831 1.900  27.239 1.00 30.18 ? 301 SER   A N   1 
ATOM   2346 C  CA  . SER   A 1 301 ? -17.874 1.861  26.200 1.00 28.06 ? 301 SER   A CA  1 
ATOM   2347 C  C   . SER   A 1 301 ? -17.402 1.264  24.863 1.00 30.29 ? 301 SER   A C   1 
ATOM   2348 O  O   . SER   A 1 301 ? -18.208 1.055  23.949 1.00 28.28 ? 301 SER   A O   1 
ATOM   2349 C  CB  . SER   A 1 301 ? -18.429 3.245  25.905 1.00 29.13 ? 301 SER   A CB  1 
ATOM   2350 O  OG  . SER   A 1 301 ? -17.546 3.936  25.019 1.00 29.54 ? 301 SER   A OG  1 
ATOM   2351 N  N   . GLY   A 1 302 ? -16.094 1.049  24.689 1.00 25.81 ? 302 GLY   A N   1 
ATOM   2352 C  CA  . GLY   A 1 302 ? -15.595 0.294  23.548 1.00 29.58 ? 302 GLY   A CA  1 
ATOM   2353 C  C   . GLY   A 1 302 ? -15.502 1.180  22.309 1.00 28.75 ? 302 GLY   A C   1 
ATOM   2354 O  O   . GLY   A 1 302 ? -15.816 0.732  21.197 1.00 27.89 ? 302 GLY   A O   1 
ATOM   2355 N  N   . VAL   A 1 303 ? -15.039 2.425  22.517 1.00 27.91 ? 303 VAL   A N   1 
ATOM   2356 C  CA  . VAL   A 1 303 ? -14.855 3.350  21.406 1.00 30.10 ? 303 VAL   A CA  1 
ATOM   2357 C  C   . VAL   A 1 303 ? -13.693 2.834  20.537 1.00 28.20 ? 303 VAL   A C   1 
ATOM   2358 O  O   . VAL   A 1 303 ? -12.622 2.549  21.065 1.00 28.15 ? 303 VAL   A O   1 
ATOM   2359 C  CB  . VAL   A 1 303 ? -14.640 4.815  21.853 1.00 29.29 ? 303 VAL   A CB  1 
ATOM   2360 C  CG1 . VAL   A 1 303 ? -14.258 5.732  20.690 1.00 28.30 ? 303 VAL   A CG1 1 
ATOM   2361 C  CG2 . VAL   A 1 303 ? -15.862 5.374  22.587 1.00 31.00 ? 303 VAL   A CG2 1 
ATOM   2362 N  N   . THR   A 1 304 ? -13.912 2.752  19.204 1.00 26.66 ? 304 THR   A N   1 
ATOM   2363 C  CA  . THR   A 1 304 ? -12.908 2.282  18.240 1.00 27.41 ? 304 THR   A CA  1 
ATOM   2364 C  C   . THR   A 1 304 ? -12.471 3.411  17.295 1.00 29.50 ? 304 THR   A C   1 
ATOM   2365 O  O   . THR   A 1 304 ? -13.101 4.474  17.214 1.00 25.57 ? 304 THR   A O   1 
ATOM   2366 C  CB  . THR   A 1 304 ? -13.444 1.111  17.403 1.00 26.08 ? 304 THR   A CB  1 
ATOM   2367 O  OG1 . THR   A 1 304 ? -14.562 1.617  16.671 1.00 26.04 ? 304 THR   A OG1 1 
ATOM   2368 C  CG2 . THR   A 1 304 ? -13.881 -0.058 18.252 1.00 25.73 ? 304 THR   A CG2 1 
ATOM   2369 N  N   . PHE   A 1 305 ? -11.387 3.127  16.551 1.00 33.21 ? 305 PHE   A N   1 
ATOM   2370 C  CA  . PHE   A 1 305 ? -10.738 4.071  15.654 1.00 38.14 ? 305 PHE   A CA  1 
ATOM   2371 C  C   . PHE   A 1 305 ? -10.631 3.399  14.284 1.00 44.95 ? 305 PHE   A C   1 
ATOM   2372 O  O   . PHE   A 1 305 ? -10.627 2.175  14.196 1.00 44.96 ? 305 PHE   A O   1 
ATOM   2373 C  CB  . PHE   A 1 305 ? -9.401  4.472  16.304 1.00 38.98 ? 305 PHE   A CB  1 
ATOM   2374 C  CG  . PHE   A 1 305 ? -9.591  4.939  17.740 1.00 36.87 ? 305 PHE   A CG  1 
ATOM   2375 C  CD1 . PHE   A 1 305 ? -10.104 6.204  17.996 1.00 38.70 ? 305 PHE   A CD1 1 
ATOM   2376 C  CD2 . PHE   A 1 305 ? -9.334  4.094  18.823 1.00 42.12 ? 305 PHE   A CD2 1 
ATOM   2377 C  CE1 . PHE   A 1 305 ? -10.346 6.630  19.296 1.00 42.67 ? 305 PHE   A CE1 1 
ATOM   2378 C  CE2 . PHE   A 1 305 ? -9.582  4.515  20.128 1.00 40.67 ? 305 PHE   A CE2 1 
ATOM   2379 C  CZ  . PHE   A 1 305 ? -10.088 5.784  20.360 1.00 43.67 ? 305 PHE   A CZ  1 
ATOM   2380 N  N   . GLN   A 1 306 ? -10.501 4.201  13.224 1.00 53.99 ? 306 GLN   A N   1 
ATOM   2381 C  CA  . GLN   A 1 306 ? -10.546 3.690  11.861 1.00 59.64 ? 306 GLN   A CA  1 
ATOM   2382 C  C   . GLN   A 1 306 ? -9.387  2.706  11.597 1.00 61.75 ? 306 GLN   A C   1 
ATOM   2383 O  O   . GLN   A 1 306 ? -8.399  2.718  12.376 1.00 60.78 ? 306 GLN   A O   1 
ATOM   2384 C  CB  . GLN   A 1 306 ? -10.486 4.844  10.864 1.00 62.00 ? 306 GLN   A CB  1 
ATOM   2385 C  CG  . GLN   A 1 306 ? -11.170 4.532  9.537  1.00 68.75 ? 306 GLN   A CG  1 
ATOM   2386 C  CD  . GLN   A 1 306 ? -10.684 5.426  8.416  1.00 70.05 ? 306 GLN   A CD  1 
ATOM   2387 O  OE1 . GLN   A 1 306 ? -9.480  5.489  8.143  1.00 68.84 ? 306 GLN   A OE1 1 
ATOM   2388 N  NE2 . GLN   A 1 306 ? -11.600 6.137  7.769  1.00 69.43 ? 306 GLN   A NE2 1 
HETATM 2389 C  C4  . A1B7C B 2 .   ? 21.387  14.483 31.351 1.00 21.98 ? 401 A1B7C A C4  1 
HETATM 2390 C  C14 . A1B7C B 2 .   ? 17.900  12.095 24.451 1.00 17.21 ? 401 A1B7C A C14 1 
HETATM 2391 C  C5  . A1B7C B 2 .   ? 19.967  15.374 29.516 1.00 18.96 ? 401 A1B7C A C5  1 
HETATM 2392 C  C6  . A1B7C B 2 .   ? 19.385  17.285 30.903 1.00 28.35 ? 401 A1B7C A C6  1 
HETATM 2393 C  C11 . A1B7C B 2 .   ? 19.532  16.441 24.873 1.00 18.64 ? 401 A1B7C A C11 1 
HETATM 2394 C  C7  . A1B7C B 2 .   ? 18.289  17.930 31.763 1.00 33.91 ? 401 A1B7C A C7  1 
HETATM 2395 C  C8  . A1B7C B 2 .   ? 19.152  15.174 28.243 1.00 17.32 ? 401 A1B7C A C8  1 
HETATM 2396 C  C9  . A1B7C B 2 .   ? 20.753  16.651 26.964 1.00 17.82 ? 401 A1B7C A C9  1 
HETATM 2397 C  C10 . A1B7C B 2 .   ? 20.676  17.155 25.542 1.00 19.54 ? 401 A1B7C A C10 1 
HETATM 2398 C  C12 . A1B7C B 2 .   ? 18.880  15.502 25.887 1.00 17.35 ? 401 A1B7C A C12 1 
HETATM 2399 C  C13 . A1B7C B 2 .   ? 19.025  14.050 25.472 1.00 17.39 ? 401 A1B7C A C13 1 
HETATM 2400 N  N1  . A1B7C B 2 .   ? 19.104  16.070 30.458 1.00 19.89 ? 401 A1B7C A N1  1 
HETATM 2401 N  N2  . A1B7C B 2 .   ? 19.597  15.756 27.132 1.00 16.63 ? 401 A1B7C A N2  1 
HETATM 2402 C  C3  . A1B7C B 2 .   ? 19.564  13.018 30.453 1.00 19.21 ? 401 A1B7C A C3  1 
HETATM 2403 N  N3  . A1B7C B 2 .   ? 17.943  13.482 24.900 1.00 16.26 ? 401 A1B7C A N3  1 
HETATM 2404 C  C1  . A1B7C B 2 .   ? 21.595  13.538 29.070 1.00 19.30 ? 401 A1B7C A C1  1 
HETATM 2405 C  C2  . A1B7C B 2 .   ? 20.602  14.085 30.092 1.00 19.46 ? 401 A1B7C A C2  1 
HETATM 2406 O  O1  . A1B7C B 2 .   ? 20.411  17.904 30.706 1.00 30.94 ? 401 A1B7C A O1  1 
HETATM 2407 F  F1  . A1B7C B 2 .   ? 18.180  17.401 32.943 1.00 37.53 ? 401 A1B7C A F1  1 
HETATM 2408 F  F2  . A1B7C B 2 .   ? 17.078  17.585 31.391 1.00 33.81 ? 401 A1B7C A F2  1 
HETATM 2409 F  F3  . A1B7C B 2 .   ? 18.327  19.267 31.785 1.00 34.18 ? 401 A1B7C A F3  1 
HETATM 2410 O  O2  . A1B7C B 2 .   ? 18.134  14.522 28.263 1.00 15.15 ? 401 A1B7C A O2  1 
HETATM 2411 O  O3  . A1B7C B 2 .   ? 20.106  13.481 25.654 1.00 14.48 ? 401 A1B7C A O3  1 
HETATM 2412 C  C15 . A1B7C B 2 .   ? 16.845  11.254 25.200 1.00 16.86 ? 401 A1B7C A C15 1 
HETATM 2413 C  C16 . A1B7C B 2 .   ? 17.285  11.087 26.657 1.00 17.66 ? 401 A1B7C A C16 1 
HETATM 2414 C  C17 . A1B7C B 2 .   ? 18.591  10.352 26.968 1.00 17.86 ? 401 A1B7C A C17 1 
HETATM 2415 C  C18 . A1B7C B 2 .   ? 18.309  9.556  28.222 1.00 19.83 ? 401 A1B7C A C18 1 
HETATM 2416 N  N4  . A1B7C B 2 .   ? 16.851  9.496  28.273 1.00 20.67 ? 401 A1B7C A N4  1 
HETATM 2417 C  C19 . A1B7C B 2 .   ? 16.241  10.382 27.496 1.00 19.31 ? 401 A1B7C A C19 1 
HETATM 2418 O  O4  . A1B7C B 2 .   ? 15.050  10.636 27.458 1.00 18.98 ? 401 A1B7C A O4  1 
HETATM 2419 C  C20 . A1B7C B 2 .   ? 17.749  12.017 22.932 1.00 19.00 ? 401 A1B7C A C20 1 
HETATM 2420 O  O5  . A1B7C B 2 .   ? 17.445  10.901 22.460 1.00 18.19 ? 401 A1B7C A O5  1 
HETATM 2421 C  C21 . A1B7C B 2 .   ? 18.684  12.866 22.290 1.00 21.14 ? 401 A1B7C A C21 1 
HETATM 2422 N  N5  . A1B7C B 2 .   ? 19.933  12.342 22.259 1.00 21.37 ? 401 A1B7C A N5  1 
HETATM 2423 C  C22 . A1B7C B 2 .   ? 20.900  13.125 21.595 1.00 23.81 ? 401 A1B7C A C22 1 
HETATM 2424 C  C23 . A1B7C B 2 .   ? 22.257  12.912 21.371 1.00 24.60 ? 401 A1B7C A C23 1 
HETATM 2425 C  C24 . A1B7C B 2 .   ? 22.929  13.906 20.669 1.00 29.51 ? 401 A1B7C A C24 1 
HETATM 2426 CL CL1 . A1B7C B 2 .   ? 24.625  13.733 20.348 1.00 32.81 ? 401 A1B7C A CL1 1 
HETATM 2427 C  C25 . A1B7C B 2 .   ? 22.338  15.072 20.216 1.00 25.59 ? 401 A1B7C A C25 1 
HETATM 2428 C  C26 . A1B7C B 2 .   ? 20.990  15.281 20.422 1.00 25.74 ? 401 A1B7C A C26 1 
HETATM 2429 C  C27 . A1B7C B 2 .   ? 20.268  14.317 21.102 1.00 25.68 ? 401 A1B7C A C27 1 
HETATM 2430 S  S1  . A1B7C B 2 .   ? 18.572  14.415 21.507 1.00 23.94 ? 401 A1B7C A S1  1 
HETATM 2431 C  C28 . A1B7C B 2 .   ? 19.451  17.930 25.132 1.00 20.53 ? 401 A1B7C A C28 1 
HETATM 2432 C  C29 . A1B7C B 2 .   ? 19.485  18.795 23.881 1.00 22.37 ? 401 A1B7C A C29 1 
HETATM 2433 C  C30 . A1B7C B 2 .   ? 18.578  18.519 26.221 1.00 21.57 ? 401 A1B7C A C30 1 
HETATM 2434 O  O   . HOH   C 3 .   ? 13.625  11.163 -2.245 1.00 32.43 ? 501 HOH   A O   1 
HETATM 2435 O  O   . HOH   C 3 .   ? 24.689  8.388  14.272 1.00 38.02 ? 502 HOH   A O   1 
HETATM 2436 O  O   . HOH   C 3 .   ? -12.316 12.050 8.115  1.00 33.85 ? 503 HOH   A O   1 
HETATM 2437 O  O   . HOH   C 3 .   ? 2.936   25.822 20.221 1.00 28.02 ? 504 HOH   A O   1 
HETATM 2438 O  O   . HOH   C 3 .   ? -3.405  10.222 46.427 1.00 23.90 ? 505 HOH   A O   1 
HETATM 2439 O  O   . HOH   C 3 .   ? 15.184  23.790 36.436 1.00 36.76 ? 506 HOH   A O   1 
HETATM 2440 O  O   . HOH   C 3 .   ? -0.378  6.563  32.370 1.00 26.05 ? 507 HOH   A O   1 
HETATM 2441 O  O   . HOH   C 3 .   ? 15.418  31.319 16.063 1.00 37.05 ? 508 HOH   A O   1 
HETATM 2442 O  O   . HOH   C 3 .   ? -21.872 -3.155 40.867 1.00 24.51 ? 509 HOH   A O   1 
HETATM 2443 O  O   . HOH   C 3 .   ? -11.457 -4.032 46.185 1.00 30.45 ? 510 HOH   A O   1 
HETATM 2444 O  O   . HOH   C 3 .   ? 11.846  3.346  25.442 1.00 21.24 ? 511 HOH   A O   1 
HETATM 2445 O  O   . HOH   C 3 .   ? 16.991  10.932 34.979 1.00 31.62 ? 512 HOH   A O   1 
HETATM 2446 O  O   . HOH   C 3 .   ? -20.428 0.511  48.446 1.00 32.64 ? 513 HOH   A O   1 
HETATM 2447 O  O   . HOH   C 3 .   ? 19.023  18.418 -5.939 1.00 36.31 ? 514 HOH   A O   1 
HETATM 2448 O  O   . HOH   C 3 .   ? 28.660  24.443 20.013 1.00 39.09 ? 515 HOH   A O   1 
HETATM 2449 O  O   . HOH   C 3 .   ? -1.199  14.044 46.079 1.00 36.61 ? 516 HOH   A O   1 
HETATM 2450 O  O   . HOH   C 3 .   ? -19.353 25.826 40.717 1.00 38.06 ? 517 HOH   A O   1 
HETATM 2451 O  O   . HOH   C 3 .   ? -19.910 9.459  48.835 1.00 30.98 ? 518 HOH   A O   1 
HETATM 2452 O  O   . HOH   C 3 .   ? -19.677 -5.687 42.823 1.00 28.93 ? 519 HOH   A O   1 
HETATM 2453 O  O   . HOH   C 3 .   ? -12.161 25.754 48.946 1.00 31.25 ? 520 HOH   A O   1 
HETATM 2454 O  O   . HOH   C 3 .   ? -5.254  22.323 45.719 1.00 27.17 ? 521 HOH   A O   1 
HETATM 2455 O  O   . HOH   C 3 .   ? 18.787  10.802 20.271 1.00 27.12 ? 522 HOH   A O   1 
HETATM 2456 O  O   . HOH   C 3 .   ? -10.768 23.633 35.036 1.00 28.48 ? 523 HOH   A O   1 
HETATM 2457 O  O   . HOH   C 3 .   ? -23.118 19.191 48.280 1.00 36.02 ? 524 HOH   A O   1 
HETATM 2458 O  O   . HOH   C 3 .   ? 18.295  12.254 3.032  1.00 20.29 ? 525 HOH   A O   1 
HETATM 2459 O  O   . HOH   C 3 .   ? -12.077 12.966 11.889 1.00 31.86 ? 526 HOH   A O   1 
HETATM 2460 O  O   . HOH   C 3 .   ? 17.419  7.101  17.391 1.00 23.04 ? 527 HOH   A O   1 
HETATM 2461 O  O   . HOH   C 3 .   ? 26.797  23.246 12.206 1.00 31.53 ? 528 HOH   A O   1 
HETATM 2462 O  O   . HOH   C 3 .   ? -18.174 -0.883 30.817 1.00 31.75 ? 529 HOH   A O   1 
HETATM 2463 O  O   . HOH   C 3 .   ? -18.392 24.989 34.159 1.00 34.45 ? 530 HOH   A O   1 
HETATM 2464 O  O   . HOH   C 3 .   ? 0.547   5.633  8.825  1.00 22.88 ? 531 HOH   A O   1 
HETATM 2465 O  O   . HOH   C 3 .   ? -17.933 -0.754 20.741 1.00 44.11 ? 532 HOH   A O   1 
HETATM 2466 O  O   . HOH   C 3 .   ? 21.954  11.611 25.631 1.00 35.39 ? 533 HOH   A O   1 
HETATM 2467 O  O   . HOH   C 3 .   ? 22.209  9.933  28.261 1.00 26.43 ? 534 HOH   A O   1 
HETATM 2468 O  O   . HOH   C 3 .   ? -16.538 12.327 53.307 1.00 28.96 ? 535 HOH   A O   1 
HETATM 2469 O  O   . HOH   C 3 .   ? 9.920   2.355  11.231 1.00 32.21 ? 536 HOH   A O   1 
HETATM 2470 O  O   . HOH   C 3 .   ? 13.023  2.395  28.413 1.00 20.70 ? 537 HOH   A O   1 
HETATM 2471 O  O   . HOH   C 3 .   ? -10.772 4.203  53.926 1.00 33.25 ? 538 HOH   A O   1 
HETATM 2472 O  O   . HOH   C 3 .   ? -16.421 -0.160 16.062 1.00 42.17 ? 539 HOH   A O   1 
HETATM 2473 O  O   . HOH   C 3 .   ? 19.200  8.596  8.881  1.00 19.86 ? 540 HOH   A O   1 
HETATM 2474 O  O   . HOH   C 3 .   ? 15.725  22.410 -2.997 1.00 33.40 ? 541 HOH   A O   1 
HETATM 2475 O  O   . HOH   C 3 .   ? 8.085   17.783 -1.897 1.00 21.15 ? 542 HOH   A O   1 
HETATM 2476 O  O   . HOH   C 3 .   ? 1.208   12.504 1.825  1.00 20.39 ? 543 HOH   A O   1 
HETATM 2477 O  O   . HOH   C 3 .   ? -21.709 24.163 34.814 1.00 38.51 ? 544 HOH   A O   1 
HETATM 2478 O  O   . HOH   C 3 .   ? -8.391  11.828 27.300 1.00 24.34 ? 545 HOH   A O   1 
HETATM 2479 O  O   . HOH   C 3 .   ? 26.885  22.277 2.403  1.00 23.23 ? 546 HOH   A O   1 
HETATM 2480 O  O   . HOH   C 3 .   ? -1.131  13.326 49.348 1.00 38.87 ? 547 HOH   A O   1 
HETATM 2481 O  O   . HOH   C 3 .   ? 7.874   22.149 36.193 1.00 26.53 ? 548 HOH   A O   1 
HETATM 2482 O  O   . HOH   C 3 .   ? -7.651  13.467 16.863 1.00 25.29 ? 549 HOH   A O   1 
HETATM 2483 O  O   . HOH   C 3 .   ? -7.481  22.896 38.772 1.00 26.71 ? 550 HOH   A O   1 
HETATM 2484 O  O   . HOH   C 3 .   ? 12.280  26.231 25.673 1.00 24.75 ? 551 HOH   A O   1 
HETATM 2485 O  O   . HOH   C 3 .   ? 3.469   17.848 6.885  1.00 20.91 ? 552 HOH   A O   1 
HETATM 2486 O  O   . HOH   C 3 .   ? 6.989   7.978  17.837 1.00 16.50 ? 553 HOH   A O   1 
HETATM 2487 O  O   . HOH   C 3 .   ? 26.840  21.099 14.170 1.00 31.27 ? 554 HOH   A O   1 
HETATM 2488 O  O   . HOH   C 3 .   ? -8.010  15.504 32.894 1.00 17.02 ? 555 HOH   A O   1 
HETATM 2489 O  O   . HOH   C 3 .   ? -25.353 13.171 37.626 1.00 30.69 ? 556 HOH   A O   1 
HETATM 2490 O  O   . HOH   C 3 .   ? 29.005  21.170 15.683 1.00 37.81 ? 557 HOH   A O   1 
HETATM 2491 O  O   . HOH   C 3 .   ? 25.873  23.194 30.349 1.00 38.86 ? 558 HOH   A O   1 
HETATM 2492 O  O   . HOH   C 3 .   ? 20.680  26.759 7.191  1.00 26.15 ? 559 HOH   A O   1 
HETATM 2493 O  O   . HOH   C 3 .   ? 4.925   22.019 7.916  1.00 39.41 ? 560 HOH   A O   1 
HETATM 2494 O  O   . HOH   C 3 .   ? -5.564  9.577  25.907 1.00 23.05 ? 561 HOH   A O   1 
HETATM 2495 O  O   . HOH   C 3 .   ? -14.341 6.697  51.067 1.00 22.59 ? 562 HOH   A O   1 
HETATM 2496 O  O   . HOH   C 3 .   ? 7.381   14.889 37.461 1.00 32.17 ? 563 HOH   A O   1 
HETATM 2497 O  O   . HOH   C 3 .   ? -28.143 8.890  36.829 1.00 24.51 ? 564 HOH   A O   1 
HETATM 2498 O  O   . HOH   C 3 .   ? -7.793  22.598 46.255 1.00 31.88 ? 565 HOH   A O   1 
HETATM 2499 O  O   . HOH   C 3 .   ? -6.542  8.751  8.810  1.00 22.74 ? 566 HOH   A O   1 
HETATM 2500 O  O   . HOH   C 3 .   ? -12.720 25.402 41.971 1.00 40.15 ? 567 HOH   A O   1 
HETATM 2501 O  O   . HOH   C 3 .   ? -7.067  8.396  36.832 1.00 14.89 ? 568 HOH   A O   1 
HETATM 2502 O  O   . HOH   C 3 .   ? 5.613   5.365  4.084  1.00 27.23 ? 569 HOH   A O   1 
HETATM 2503 O  O   . HOH   C 3 .   ? 19.917  29.456 11.284 1.00 25.62 ? 570 HOH   A O   1 
HETATM 2504 O  O   . HOH   C 3 .   ? 3.012   10.861 33.018 1.00 16.85 ? 571 HOH   A O   1 
HETATM 2505 O  O   . HOH   C 3 .   ? -23.870 9.253  30.658 1.00 19.46 ? 572 HOH   A O   1 
HETATM 2506 O  O   . HOH   C 3 .   ? -9.152  -4.002 43.657 1.00 21.75 ? 573 HOH   A O   1 
HETATM 2507 O  O   . HOH   C 3 .   ? 26.776  12.687 17.610 1.00 29.79 ? 574 HOH   A O   1 
HETATM 2508 O  O   . HOH   C 3 .   ? -17.421 14.774 29.502 1.00 29.27 ? 575 HOH   A O   1 
HETATM 2509 O  O   . HOH   C 3 .   ? 14.112  28.438 16.940 1.00 23.10 ? 576 HOH   A O   1 
HETATM 2510 O  O   . HOH   C 3 .   ? 20.484  18.604 -2.703 1.00 33.79 ? 577 HOH   A O   1 
HETATM 2511 O  O   . HOH   C 3 .   ? -25.523 10.478 44.161 1.00 24.78 ? 578 HOH   A O   1 
HETATM 2512 O  O   . HOH   C 3 .   ? -15.014 26.383 39.265 1.00 33.96 ? 579 HOH   A O   1 
HETATM 2513 O  O   . HOH   C 3 .   ? 26.668  26.417 19.228 1.00 24.94 ? 580 HOH   A O   1 
HETATM 2514 O  O   . HOH   C 3 .   ? -0.219  23.066 35.665 1.00 28.54 ? 581 HOH   A O   1 
HETATM 2515 O  O   . HOH   C 3 .   ? -5.007  8.231  51.044 1.00 42.26 ? 582 HOH   A O   1 
HETATM 2516 O  O   . HOH   C 3 .   ? 7.745   18.933 28.864 1.00 14.59 ? 583 HOH   A O   1 
HETATM 2517 O  O   . HOH   C 3 .   ? -0.368  23.282 28.095 1.00 36.99 ? 584 HOH   A O   1 
HETATM 2518 O  O   . HOH   C 3 .   ? 5.349   22.543 13.070 1.00 21.59 ? 585 HOH   A O   1 
HETATM 2519 O  O   . HOH   C 3 .   ? 20.767  9.956  23.330 1.00 27.46 ? 586 HOH   A O   1 
HETATM 2520 O  O   . HOH   C 3 .   ? 9.143   7.973  34.270 1.00 36.42 ? 587 HOH   A O   1 
HETATM 2521 O  O   . HOH   C 3 .   ? -3.836  0.245  49.829 1.00 34.99 ? 588 HOH   A O   1 
HETATM 2522 O  O   . HOH   C 3 .   ? 19.552  16.920 -0.561 1.00 26.89 ? 589 HOH   A O   1 
HETATM 2523 O  O   . HOH   C 3 .   ? 19.978  28.860 20.175 1.00 26.90 ? 590 HOH   A O   1 
HETATM 2524 O  O   . HOH   C 3 .   ? -21.636 -1.958 36.548 1.00 25.93 ? 591 HOH   A O   1 
HETATM 2525 O  O   . HOH   C 3 .   ? 25.725  15.365 7.788  1.00 30.31 ? 592 HOH   A O   1 
HETATM 2526 O  O   . HOH   C 3 .   ? -18.718 25.052 47.319 1.00 32.18 ? 593 HOH   A O   1 
HETATM 2527 O  O   . HOH   C 3 .   ? 3.359   -3.263 14.535 1.00 20.32 ? 594 HOH   A O   1 
HETATM 2528 O  O   . HOH   C 3 .   ? -17.570 11.828 32.425 1.00 18.17 ? 595 HOH   A O   1 
HETATM 2529 O  O   . HOH   C 3 .   ? 2.540   21.102 39.942 1.00 40.53 ? 596 HOH   A O   1 
HETATM 2530 O  O   . HOH   C 3 .   ? -15.945 -6.876 37.484 1.00 27.94 ? 597 HOH   A O   1 
HETATM 2531 O  O   . HOH   C 3 .   ? 4.183   25.249 29.355 1.00 26.45 ? 598 HOH   A O   1 
HETATM 2532 O  O   . HOH   C 3 .   ? -5.016  6.836  30.085 1.00 23.39 ? 599 HOH   A O   1 
HETATM 2533 O  O   . HOH   C 3 .   ? 1.482   19.887 18.689 1.00 20.15 ? 600 HOH   A O   1 
HETATM 2534 O  O   . HOH   C 3 .   ? 26.657  18.065 13.222 1.00 30.37 ? 601 HOH   A O   1 
HETATM 2535 O  O   . HOH   C 3 .   ? 0.482   16.663 50.900 1.00 32.73 ? 602 HOH   A O   1 
HETATM 2536 O  O   . HOH   C 3 .   ? -18.101 6.645  55.882 1.00 38.79 ? 603 HOH   A O   1 
HETATM 2537 O  O   . HOH   C 3 .   ? 14.731  25.855 24.341 1.00 23.86 ? 604 HOH   A O   1 
HETATM 2538 O  O   . HOH   C 3 .   ? -18.491 -5.807 30.701 1.00 19.23 ? 605 HOH   A O   1 
HETATM 2539 O  O   . HOH   C 3 .   ? -12.155 13.101 14.492 1.00 34.33 ? 606 HOH   A O   1 
HETATM 2540 O  O   . HOH   C 3 .   ? -3.098  20.904 12.956 1.00 30.02 ? 607 HOH   A O   1 
HETATM 2541 O  O   . HOH   C 3 .   ? -6.322  0.782  38.208 1.00 30.29 ? 608 HOH   A O   1 
HETATM 2542 O  O   . HOH   C 3 .   ? 21.079  13.821 2.171  1.00 37.40 ? 609 HOH   A O   1 
HETATM 2543 O  O   . HOH   C 3 .   ? 14.060  16.081 -5.884 1.00 33.35 ? 610 HOH   A O   1 
HETATM 2544 O  O   . HOH   C 3 .   ? 5.468   11.917 -3.443 1.00 22.26 ? 611 HOH   A O   1 
HETATM 2545 O  O   . HOH   C 3 .   ? 15.060  28.372 9.879  1.00 24.41 ? 612 HOH   A O   1 
HETATM 2546 O  O   . HOH   C 3 .   ? -21.511 16.569 36.739 1.00 29.07 ? 613 HOH   A O   1 
HETATM 2547 O  O   . HOH   C 3 .   ? -21.856 -0.977 39.272 1.00 33.09 ? 614 HOH   A O   1 
HETATM 2548 O  O   . HOH   C 3 .   ? -3.349  14.918 21.365 1.00 21.17 ? 615 HOH   A O   1 
HETATM 2549 O  O   . HOH   C 3 .   ? -6.045  4.350  29.087 1.00 18.60 ? 616 HOH   A O   1 
HETATM 2550 O  O   . HOH   C 3 .   ? -20.122 21.801 41.778 1.00 29.93 ? 617 HOH   A O   1 
HETATM 2551 O  O   . HOH   C 3 .   ? 23.194  9.598  17.583 1.00 27.37 ? 618 HOH   A O   1 
HETATM 2552 O  O   . HOH   C 3 .   ? -19.485 20.010 52.800 1.00 34.40 ? 619 HOH   A O   1 
HETATM 2553 O  O   . HOH   C 3 .   ? 10.126  26.197 23.882 1.00 19.87 ? 620 HOH   A O   1 
HETATM 2554 O  O   . HOH   C 3 .   ? -2.833  7.195  46.744 1.00 26.83 ? 621 HOH   A O   1 
HETATM 2555 O  O   . HOH   C 3 .   ? -20.641 23.054 46.201 1.00 22.80 ? 622 HOH   A O   1 
HETATM 2556 O  O   . HOH   C 3 .   ? 10.931  29.757 15.484 1.00 27.46 ? 623 HOH   A O   1 
HETATM 2557 O  O   . HOH   C 3 .   ? -14.054 -3.442 30.644 1.00 24.15 ? 624 HOH   A O   1 
HETATM 2558 O  O   . HOH   C 3 .   ? 22.672  20.798 0.267  1.00 19.58 ? 625 HOH   A O   1 
HETATM 2559 O  O   . HOH   C 3 .   ? 25.004  16.709 14.380 1.00 29.27 ? 626 HOH   A O   1 
HETATM 2560 O  O   . HOH   C 3 .   ? -6.374  23.513 53.315 1.00 40.01 ? 627 HOH   A O   1 
HETATM 2561 O  O   . HOH   C 3 .   ? -8.186  11.641 23.505 1.00 37.09 ? 628 HOH   A O   1 
HETATM 2562 O  O   . HOH   C 3 .   ? -22.949 15.424 39.617 1.00 27.21 ? 629 HOH   A O   1 
HETATM 2563 O  O   . HOH   C 3 .   ? -1.330  7.639  38.883 1.00 34.07 ? 630 HOH   A O   1 
HETATM 2564 O  O   . HOH   C 3 .   ? -3.799  10.417 51.802 1.00 24.91 ? 631 HOH   A O   1 
HETATM 2565 O  O   . HOH   C 3 .   ? -3.822  23.205 20.275 1.00 26.01 ? 632 HOH   A O   1 
HETATM 2566 O  O   . HOH   C 3 .   ? 26.306  16.145 3.032  1.00 22.09 ? 633 HOH   A O   1 
HETATM 2567 O  O   . HOH   C 3 .   ? 19.941  5.611  28.013 1.00 24.70 ? 634 HOH   A O   1 
HETATM 2568 O  O   . HOH   C 3 .   ? 18.473  14.774 34.123 1.00 31.57 ? 635 HOH   A O   1 
HETATM 2569 O  O   . HOH   C 3 .   ? -8.763  3.949  28.767 1.00 27.88 ? 636 HOH   A O   1 
HETATM 2570 O  O   . HOH   C 3 .   ? 10.797  -0.028 11.417 1.00 44.45 ? 637 HOH   A O   1 
HETATM 2571 O  O   . HOH   C 3 .   ? -6.359  13.483 26.986 1.00 27.85 ? 638 HOH   A O   1 
HETATM 2572 O  O   . HOH   C 3 .   ? 3.297   24.022 36.857 1.00 38.33 ? 639 HOH   A O   1 
HETATM 2573 O  O   . HOH   C 3 .   ? 11.016  23.399 6.075  1.00 30.38 ? 640 HOH   A O   1 
HETATM 2574 O  O   . HOH   C 3 .   ? -13.105 25.993 45.963 1.00 47.63 ? 641 HOH   A O   1 
HETATM 2575 O  O   . HOH   C 3 .   ? 23.227  11.300 1.387  1.00 32.73 ? 642 HOH   A O   1 
HETATM 2576 O  O   . HOH   C 3 .   ? -24.733 13.978 35.241 1.00 26.71 ? 643 HOH   A O   1 
HETATM 2577 O  O   . HOH   C 3 .   ? -13.230 7.321  17.931 1.00 35.88 ? 644 HOH   A O   1 
HETATM 2578 O  O   . HOH   C 3 .   ? -16.618 3.685  18.521 1.00 32.07 ? 645 HOH   A O   1 
HETATM 2579 O  O   . HOH   C 3 .   ? -22.369 17.766 32.750 1.00 26.41 ? 646 HOH   A O   1 
HETATM 2580 O  O   . HOH   C 3 .   ? -7.318  17.263 10.518 1.00 29.82 ? 647 HOH   A O   1 
HETATM 2581 O  O   . HOH   C 3 .   ? 19.918  12.746 -1.591 1.00 29.63 ? 648 HOH   A O   1 
HETATM 2582 O  O   . HOH   C 3 .   ? -8.904  -4.954 48.609 1.00 38.53 ? 649 HOH   A O   1 
HETATM 2583 O  O   . HOH   C 3 .   ? 19.079  8.113  31.640 1.00 18.98 ? 650 HOH   A O   1 
HETATM 2584 O  O   . HOH   C 3 .   ? -8.577  18.317 38.691 1.00 18.62 ? 651 HOH   A O   1 
HETATM 2585 O  O   . HOH   C 3 .   ? 19.025  2.689  23.590 1.00 33.18 ? 652 HOH   A O   1 
HETATM 2586 O  O   . HOH   C 3 .   ? -22.399 17.008 42.199 1.00 24.72 ? 653 HOH   A O   1 
HETATM 2587 O  O   . HOH   C 3 .   ? 13.416  17.038 38.067 1.00 33.06 ? 654 HOH   A O   1 
HETATM 2588 O  O   . HOH   C 3 .   ? -0.199  1.878  28.385 1.00 33.37 ? 655 HOH   A O   1 
HETATM 2589 O  O   . HOH   C 3 .   ? 9.579   27.386 9.731  1.00 41.44 ? 656 HOH   A O   1 
HETATM 2590 O  O   . HOH   C 3 .   ? -1.583  9.404  0.732  1.00 28.17 ? 657 HOH   A O   1 
HETATM 2591 O  O   . HOH   C 3 .   ? 20.454  24.042 1.765  1.00 27.91 ? 658 HOH   A O   1 
HETATM 2592 O  O   . HOH   C 3 .   ? 2.956   25.895 12.799 1.00 36.22 ? 659 HOH   A O   1 
HETATM 2593 O  O   . HOH   C 3 .   ? -9.137  -4.865 36.109 1.00 36.12 ? 660 HOH   A O   1 
HETATM 2594 O  O   . HOH   C 3 .   ? 1.504   24.744 28.353 1.00 38.34 ? 661 HOH   A O   1 
HETATM 2595 O  O   . HOH   C 3 .   ? -18.076 26.408 45.256 1.00 35.83 ? 662 HOH   A O   1 
HETATM 2596 O  O   . HOH   C 3 .   ? -20.656 6.235  55.102 1.00 35.51 ? 663 HOH   A O   1 
HETATM 2597 O  O   . HOH   C 3 .   ? -14.619 26.114 35.760 1.00 29.08 ? 664 HOH   A O   1 
HETATM 2598 O  O   . HOH   C 3 .   ? -23.091 1.164  34.065 1.00 33.70 ? 665 HOH   A O   1 
HETATM 2599 O  O   . HOH   C 3 .   ? -23.076 5.352  48.614 1.00 40.66 ? 666 HOH   A O   1 
HETATM 2600 O  O   . HOH   C 3 .   ? 18.601  25.590 24.543 1.00 26.68 ? 667 HOH   A O   1 
HETATM 2601 O  O   . HOH   C 3 .   ? -15.711 -3.501 46.565 1.00 31.52 ? 668 HOH   A O   1 
HETATM 2602 O  O   . HOH   C 3 .   ? 15.271  3.954  8.846  1.00 33.74 ? 669 HOH   A O   1 
HETATM 2603 O  O   . HOH   C 3 .   ? 24.102  12.978 7.308  1.00 36.13 ? 670 HOH   A O   1 
HETATM 2604 O  O   . HOH   C 3 .   ? 22.309  12.106 -2.323 1.00 37.35 ? 671 HOH   A O   1 
HETATM 2605 O  O   . HOH   C 3 .   ? 18.197  28.433 21.865 1.00 38.63 ? 672 HOH   A O   1 
HETATM 2606 O  O   . HOH   C 3 .   ? 11.892  4.275  9.476  1.00 26.21 ? 673 HOH   A O   1 
HETATM 2607 O  O   . HOH   C 3 .   ? -22.572 20.969 39.517 1.00 23.73 ? 674 HOH   A O   1 
HETATM 2608 O  O   . HOH   C 3 .   ? 4.917   29.223 18.001 1.00 39.84 ? 675 HOH   A O   1 
HETATM 2609 O  O   . HOH   C 3 .   ? 1.007   20.707 9.397  1.00 38.83 ? 676 HOH   A O   1 
HETATM 2610 O  O   . HOH   C 3 .   ? -19.053 3.291  28.924 1.00 45.16 ? 677 HOH   A O   1 
HETATM 2611 O  O   . HOH   C 3 .   ? -4.527  15.971 7.696  1.00 23.27 ? 678 HOH   A O   1 
HETATM 2612 O  O   . HOH   C 3 .   ? -3.515  18.964 8.913  1.00 42.08 ? 679 HOH   A O   1 
HETATM 2613 O  O   . HOH   C 3 .   ? -6.186  3.712  14.370 1.00 32.54 ? 680 HOH   A O   1 
HETATM 2614 O  O   . HOH   C 3 .   ? 18.730  20.583 -2.345 1.00 31.68 ? 681 HOH   A O   1 
HETATM 2615 O  O   . HOH   C 3 .   ? -11.429 -4.790 40.846 1.00 37.53 ? 682 HOH   A O   1 
HETATM 2616 O  O   . HOH   C 3 .   ? -16.451 11.157 30.096 1.00 27.39 ? 683 HOH   A O   1 
HETATM 2617 O  O   . HOH   C 3 .   ? 12.243  0.789  25.159 1.00 26.41 ? 684 HOH   A O   1 
HETATM 2618 O  O   . HOH   C 3 .   ? -22.766 0.000  46.824 0.50 20.28 ? 685 HOH   A O   1 
HETATM 2619 O  O   . HOH   C 3 .   ? 7.008   4.450  6.341  1.00 40.78 ? 686 HOH   A O   1 
HETATM 2620 O  O   . HOH   C 3 .   ? 0.150   3.068  8.603  1.00 32.60 ? 687 HOH   A O   1 
HETATM 2621 O  O   . HOH   C 3 .   ? 19.342  14.421 0.355  1.00 33.02 ? 688 HOH   A O   1 
HETATM 2622 O  O   . HOH   C 3 .   ? 24.677  8.783  28.016 1.00 30.07 ? 689 HOH   A O   1 
HETATM 2623 O  O   . HOH   C 3 .   ? 0.000   0.000  43.706 0.50 30.97 ? 690 HOH   A O   1 
HETATM 2624 O  O   . HOH   C 3 .   ? -2.288  -2.045 32.962 1.00 31.70 ? 691 HOH   A O   1 
HETATM 2625 O  O   . HOH   C 3 .   ? -2.988  6.242  7.808  1.00 49.35 ? 692 HOH   A O   1 
HETATM 2626 O  O   . HOH   C 3 .   ? -13.014 4.842  52.720 1.00 27.21 ? 693 HOH   A O   1 
HETATM 2627 O  O   . HOH   C 3 .   ? -17.655 14.978 53.233 1.00 39.73 ? 694 HOH   A O   1 
HETATM 2628 O  O   . HOH   C 3 .   ? -15.560 -1.794 32.168 1.00 32.49 ? 695 HOH   A O   1 
HETATM 2629 O  O   . HOH   C 3 .   ? -15.737 3.362  53.230 1.00 38.22 ? 696 HOH   A O   1 
HETATM 2630 O  O   . HOH   C 3 .   ? 21.683  30.479 21.710 1.00 34.12 ? 697 HOH   A O   1 
HETATM 2631 O  O   . HOH   C 3 .   ? 3.439   23.408 11.946 1.00 35.73 ? 698 HOH   A O   1 
HETATM 2632 O  O   . HOH   C 3 .   ? 16.360  17.745 -5.577 1.00 35.98 ? 699 HOH   A O   1 
HETATM 2633 O  O   . HOH   C 3 .   ? -9.307  25.800 48.680 1.00 32.94 ? 700 HOH   A O   1 
HETATM 2634 O  O   . HOH   C 3 .   ? -5.907  15.769 21.570 1.00 33.53 ? 701 HOH   A O   1 
HETATM 2635 O  O   . HOH   C 3 .   ? -8.321  23.751 36.173 1.00 33.39 ? 702 HOH   A O   1 
HETATM 2636 O  O   . HOH   C 3 .   ? 0.671   22.661 18.529 1.00 29.11 ? 703 HOH   A O   1 
HETATM 2637 O  O   . HOH   C 3 .   ? 19.635  28.555 8.594  1.00 29.85 ? 704 HOH   A O   1 
HETATM 2638 O  O   . HOH   C 3 .   ? -9.526  -4.573 54.540 1.00 39.36 ? 705 HOH   A O   1 
HETATM 2639 O  O   . HOH   C 3 .   ? -8.645  25.298 46.025 1.00 34.47 ? 706 HOH   A O   1 
HETATM 2640 O  O   . HOH   C 3 .   ? -20.904 23.313 43.692 1.00 33.44 ? 707 HOH   A O   1 
HETATM 2641 O  O   . HOH   C 3 .   ? -9.729  15.517 30.400 1.00 37.66 ? 708 HOH   A O   1 
HETATM 2642 O  O   . HOH   C 3 .   ? 7.722   23.107 6.161  1.00 40.72 ? 709 HOH   A O   1 
HETATM 2643 O  O   . HOH   C 3 .   ? -24.723 17.174 43.488 1.00 34.21 ? 710 HOH   A O   1 
HETATM 2644 O  O   . HOH   C 3 .   ? -22.039 19.715 41.593 1.00 30.43 ? 711 HOH   A O   1 
# 
