data_9DU3
# 
_entry.id   9DU3 
# 
_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   9DU3         pdb_00009du3 10.2210/pdb9du3/pdb 
WWPDB D_1000288835 ?            ?                   
# 
_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       2025-04-30 
_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                        9DU3 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-02 
_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              david.degoey@abbvie.com 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          DeGoey 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7415-1811 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bigelow, L.'  1 0009-0004-0889-4982 
'Tang, H.'     2 0000-0001-7600-6263 
'Boguslaw, N.' 3 0000-0001-8257-0792 
'Duda, D.M.'   4 0000-0003-0356-7515 
# 
_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                     
;Inhibition of Dimeric SARS-CoV-2 Mpro by Aldehyde and Nitrilebased
Inhibitors Displays Positive Cooperativity and a Mixture of
Covalent and Non-covalent Binding.
;
_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 'Padmanabha Das, K.M.' 1  0000-0002-0116-4256 
primary 'Chen, J.'             2  ?                   
primary 'Charifson, P.S.'      3  ?                   
primary 'Green, J.'            4  ?                   
primary 'Tang, H.'             5  0000-0001-7600-6263 
primary 'Panchal, S.'          6  ?                   
primary 'Pu, F.'               7  ?                   
primary 'Korepanova, A.'       8  ?                   
primary 'Afanador, G.'         9  ?                   
primary 'Stojkovic, V.'        10 ?                   
primary 'Nocek, B.'            11 0000-0001-8257-0792 
primary 'Bigelow, L.'          12 0009-0004-0889-4982 
primary 'Stubbs, S.'           13 ?                   
primary 'Davey, R.A.'          14 ?                   
primary 'DeGoey, D.A.'         15 0000-0001-7415-1811 
primary 'Arthanari, H.'        16 ?                   
primary 'Namchuk, M.N.'        17 ?                   
# 
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' 35027.883 1   3.4.22.69 ? ? ? 
2 non-polymer syn 
;N-[(2S)-3-cyclopropyl-1-({(2R)-1-hydroxy-3-[(3R)-2-oxopyrrolidin-3-yl]propan-2-yl}amino)-1-oxopropan-2-yl]-4-methoxy-1H-indole-2-carboxamide
;
442.508   1   ?         ? ? ? 
3 water       nat water 18.015    109 ?         ? ? ? 
# 
_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       
;MSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIG
HSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSF
CYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNY
EPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIG
HSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSF
CYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNY
EPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQLEHHHHHH
;
_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 
;N-[(2S)-3-cyclopropyl-1-({(2R)-1-hydroxy-3-[(3R)-2-oxopyrrolidin-3-yl]propan-2-yl}amino)-1-oxopropan-2-yl]-4-methoxy-1H-indole-2-carboxamide
;
A1BCX 
3 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   GLY n 
1 4   PHE n 
1 5   ARG n 
1 6   LYS n 
1 7   MET n 
1 8   ALA n 
1 9   PHE n 
1 10  PRO n 
1 11  SER n 
1 12  GLY n 
1 13  LYS n 
1 14  VAL n 
1 15  GLU n 
1 16  GLY n 
1 17  CYS n 
1 18  MET n 
1 19  VAL n 
1 20  GLN n 
1 21  VAL n 
1 22  THR n 
1 23  CYS n 
1 24  GLY n 
1 25  THR n 
1 26  THR n 
1 27  THR n 
1 28  LEU n 
1 29  ASN n 
1 30  GLY n 
1 31  LEU n 
1 32  TRP n 
1 33  LEU n 
1 34  ASP n 
1 35  ASP n 
1 36  VAL n 
1 37  VAL n 
1 38  TYR n 
1 39  CYS n 
1 40  PRO n 
1 41  ARG n 
1 42  HIS n 
1 43  VAL n 
1 44  ILE n 
1 45  CYS n 
1 46  THR n 
1 47  SER n 
1 48  GLU n 
1 49  ASP n 
1 50  MET n 
1 51  LEU n 
1 52  ASN n 
1 53  PRO n 
1 54  ASN n 
1 55  TYR n 
1 56  GLU n 
1 57  ASP n 
1 58  LEU n 
1 59  LEU n 
1 60  ILE n 
1 61  ARG n 
1 62  LYS n 
1 63  SER n 
1 64  ASN n 
1 65  HIS n 
1 66  ASN n 
1 67  PHE n 
1 68  LEU n 
1 69  VAL n 
1 70  GLN n 
1 71  ALA n 
1 72  GLY n 
1 73  ASN n 
1 74  VAL n 
1 75  GLN n 
1 76  LEU n 
1 77  ARG n 
1 78  VAL n 
1 79  ILE n 
1 80  GLY n 
1 81  HIS n 
1 82  SER n 
1 83  MET n 
1 84  GLN n 
1 85  ASN n 
1 86  CYS n 
1 87  VAL n 
1 88  LEU n 
1 89  LYS n 
1 90  LEU n 
1 91  LYS n 
1 92  VAL n 
1 93  ASP n 
1 94  THR n 
1 95  ALA n 
1 96  ASN n 
1 97  PRO n 
1 98  LYS n 
1 99  THR n 
1 100 PRO n 
1 101 LYS n 
1 102 TYR n 
1 103 LYS n 
1 104 PHE n 
1 105 VAL n 
1 106 ARG n 
1 107 ILE n 
1 108 GLN n 
1 109 PRO n 
1 110 GLY n 
1 111 GLN n 
1 112 THR n 
1 113 PHE n 
1 114 SER n 
1 115 VAL n 
1 116 LEU n 
1 117 ALA n 
1 118 CYS n 
1 119 TYR n 
1 120 ASN n 
1 121 GLY n 
1 122 SER n 
1 123 PRO n 
1 124 SER n 
1 125 GLY n 
1 126 VAL n 
1 127 TYR n 
1 128 GLN n 
1 129 CYS n 
1 130 ALA n 
1 131 MET n 
1 132 ARG n 
1 133 PRO n 
1 134 ASN n 
1 135 PHE n 
1 136 THR n 
1 137 ILE n 
1 138 LYS n 
1 139 GLY n 
1 140 SER n 
1 141 PHE n 
1 142 LEU n 
1 143 ASN n 
1 144 GLY n 
1 145 SER n 
1 146 CYS n 
1 147 GLY n 
1 148 SER n 
1 149 VAL n 
1 150 GLY n 
1 151 PHE n 
1 152 ASN n 
1 153 ILE n 
1 154 ASP n 
1 155 TYR n 
1 156 ASP n 
1 157 CYS n 
1 158 VAL n 
1 159 SER n 
1 160 PHE n 
1 161 CYS n 
1 162 TYR n 
1 163 MET n 
1 164 HIS n 
1 165 HIS n 
1 166 MET n 
1 167 GLU n 
1 168 LEU n 
1 169 PRO n 
1 170 THR n 
1 171 GLY n 
1 172 VAL n 
1 173 HIS n 
1 174 ALA n 
1 175 GLY n 
1 176 THR n 
1 177 ASP n 
1 178 LEU n 
1 179 GLU n 
1 180 GLY n 
1 181 ASN n 
1 182 PHE n 
1 183 TYR n 
1 184 GLY n 
1 185 PRO n 
1 186 PHE n 
1 187 VAL n 
1 188 ASP n 
1 189 ARG n 
1 190 GLN n 
1 191 THR n 
1 192 ALA n 
1 193 GLN n 
1 194 ALA n 
1 195 ALA n 
1 196 GLY n 
1 197 THR n 
1 198 ASP n 
1 199 THR n 
1 200 THR n 
1 201 ILE n 
1 202 THR n 
1 203 VAL n 
1 204 ASN n 
1 205 VAL n 
1 206 LEU n 
1 207 ALA n 
1 208 TRP n 
1 209 LEU n 
1 210 TYR n 
1 211 ALA n 
1 212 ALA n 
1 213 VAL n 
1 214 ILE n 
1 215 ASN n 
1 216 GLY n 
1 217 ASP n 
1 218 ARG n 
1 219 TRP n 
1 220 PHE n 
1 221 LEU n 
1 222 ASN n 
1 223 ARG n 
1 224 PHE n 
1 225 THR n 
1 226 THR n 
1 227 THR n 
1 228 LEU n 
1 229 ASN n 
1 230 ASP n 
1 231 PHE n 
1 232 ASN n 
1 233 LEU n 
1 234 VAL n 
1 235 ALA n 
1 236 MET n 
1 237 LYS n 
1 238 TYR n 
1 239 ASN n 
1 240 TYR n 
1 241 GLU n 
1 242 PRO n 
1 243 LEU n 
1 244 THR n 
1 245 GLN n 
1 246 ASP n 
1 247 HIS n 
1 248 VAL n 
1 249 ASP n 
1 250 ILE n 
1 251 LEU n 
1 252 GLY n 
1 253 PRO n 
1 254 LEU n 
1 255 SER n 
1 256 ALA n 
1 257 GLN n 
1 258 THR n 
1 259 GLY n 
1 260 ILE n 
1 261 ALA n 
1 262 VAL n 
1 263 LEU n 
1 264 ASP n 
1 265 MET n 
1 266 CYS n 
1 267 ALA n 
1 268 SER n 
1 269 LEU n 
1 270 LYS n 
1 271 GLU n 
1 272 LEU n 
1 273 LEU n 
1 274 GLN n 
1 275 ASN n 
1 276 GLY n 
1 277 MET n 
1 278 ASN n 
1 279 GLY n 
1 280 ARG n 
1 281 THR n 
1 282 ILE n 
1 283 LEU n 
1 284 GLY n 
1 285 SER n 
1 286 ALA n 
1 287 LEU n 
1 288 LEU n 
1 289 GLU n 
1 290 ASP n 
1 291 GLU n 
1 292 PHE n 
1 293 THR n 
1 294 PRO n 
1 295 PHE n 
1 296 ASP n 
1 297 VAL n 
1 298 VAL n 
1 299 ARG n 
1 300 GLN n 
1 301 CYS n 
1 302 SER n 
1 303 GLY n 
1 304 VAL n 
1 305 THR n 
1 306 PHE n 
1 307 GLN n 
1 308 LEU n 
1 309 GLU n 
1 310 HIS n 
1 311 HIS n 
1 312 HIS n 
1 313 HIS n 
1 314 HIS n 
1 315 HIS 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                   315 
_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 
A1BCX non-polymer         . 
;N-[(2S)-3-cyclopropyl-1-({(2R)-1-hydroxy-3-[(3R)-2-oxopyrrolidin-3-yl]propan-2-yl}amino)-1-oxopropan-2-yl]-4-methoxy-1H-indole-2-carboxamide
;
? 'C23 H30 N4 O5'  442.508 
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   MET 1   0   ?   ?   ?   A . n 
A 1 2   SER 2   1   1   SER SER A . n 
A 1 3   GLY 3   2   2   GLY GLY A . n 
A 1 4   PHE 4   3   3   PHE PHE A . n 
A 1 5   ARG 5   4   4   ARG ARG A . n 
A 1 6   LYS 6   5   5   LYS LYS A . n 
A 1 7   MET 7   6   6   MET MET A . n 
A 1 8   ALA 8   7   7   ALA ALA A . n 
A 1 9   PHE 9   8   8   PHE PHE A . n 
A 1 10  PRO 10  9   9   PRO PRO A . n 
A 1 11  SER 11  10  10  SER SER A . n 
A 1 12  GLY 12  11  11  GLY GLY A . n 
A 1 13  LYS 13  12  12  LYS LYS A . n 
A 1 14  VAL 14  13  13  VAL VAL A . n 
A 1 15  GLU 15  14  14  GLU GLU A . n 
A 1 16  GLY 16  15  15  GLY GLY A . n 
A 1 17  CYS 17  16  16  CYS CYS A . n 
A 1 18  MET 18  17  17  MET MET A . n 
A 1 19  VAL 19  18  18  VAL VAL A . n 
A 1 20  GLN 20  19  19  GLN GLN A . n 
A 1 21  VAL 21  20  20  VAL VAL A . n 
A 1 22  THR 22  21  21  THR THR A . n 
A 1 23  CYS 23  22  22  CYS CYS A . n 
A 1 24  GLY 24  23  23  GLY GLY A . n 
A 1 25  THR 25  24  24  THR THR A . n 
A 1 26  THR 26  25  25  THR THR A . n 
A 1 27  THR 27  26  26  THR THR A . n 
A 1 28  LEU 28  27  27  LEU LEU A . n 
A 1 29  ASN 29  28  28  ASN ASN A . n 
A 1 30  GLY 30  29  29  GLY GLY A . n 
A 1 31  LEU 31  30  30  LEU LEU A . n 
A 1 32  TRP 32  31  31  TRP TRP A . n 
A 1 33  LEU 33  32  32  LEU LEU A . n 
A 1 34  ASP 34  33  33  ASP ASP A . n 
A 1 35  ASP 35  34  34  ASP ASP A . n 
A 1 36  VAL 36  35  35  VAL VAL A . n 
A 1 37  VAL 37  36  36  VAL VAL A . n 
A 1 38  TYR 38  37  37  TYR TYR A . n 
A 1 39  CYS 39  38  38  CYS CYS A . n 
A 1 40  PRO 40  39  39  PRO PRO A . n 
A 1 41  ARG 41  40  40  ARG ARG A . n 
A 1 42  HIS 42  41  41  HIS HIS A . n 
A 1 43  VAL 43  42  42  VAL VAL A . n 
A 1 44  ILE 44  43  43  ILE ILE A . n 
A 1 45  CYS 45  44  44  CYS CYS A . n 
A 1 46  THR 46  45  45  THR THR A . n 
A 1 47  SER 47  46  46  SER SER A . n 
A 1 48  GLU 48  47  47  GLU GLU A . n 
A 1 49  ASP 49  48  48  ASP ASP A . n 
A 1 50  MET 50  49  49  MET MET A . n 
A 1 51  LEU 51  50  50  LEU LEU A . n 
A 1 52  ASN 52  51  51  ASN ASN A . n 
A 1 53  PRO 53  52  52  PRO PRO A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  TYR 55  54  54  TYR TYR A . n 
A 1 56  GLU 56  55  55  GLU GLU A . n 
A 1 57  ASP 57  56  56  ASP ASP A . n 
A 1 58  LEU 58  57  57  LEU LEU A . n 
A 1 59  LEU 59  58  58  LEU LEU A . n 
A 1 60  ILE 60  59  59  ILE ILE A . n 
A 1 61  ARG 61  60  60  ARG ARG A . n 
A 1 62  LYS 62  61  61  LYS LYS A . n 
A 1 63  SER 63  62  62  SER SER A . n 
A 1 64  ASN 64  63  63  ASN ASN A . n 
A 1 65  HIS 65  64  64  HIS HIS A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  PHE 67  66  66  PHE PHE A . n 
A 1 68  LEU 68  67  67  LEU LEU A . n 
A 1 69  VAL 69  68  68  VAL VAL A . n 
A 1 70  GLN 70  69  69  GLN GLN A . n 
A 1 71  ALA 71  70  70  ALA ALA A . n 
A 1 72  GLY 72  71  71  GLY GLY A . n 
A 1 73  ASN 73  72  72  ASN ASN A . n 
A 1 74  VAL 74  73  73  VAL VAL A . n 
A 1 75  GLN 75  74  74  GLN GLN A . n 
A 1 76  LEU 76  75  75  LEU LEU A . n 
A 1 77  ARG 77  76  76  ARG ARG A . n 
A 1 78  VAL 78  77  77  VAL VAL A . n 
A 1 79  ILE 79  78  78  ILE ILE A . n 
A 1 80  GLY 80  79  79  GLY GLY A . n 
A 1 81  HIS 81  80  80  HIS HIS A . n 
A 1 82  SER 82  81  81  SER SER A . n 
A 1 83  MET 83  82  82  MET MET A . n 
A 1 84  GLN 84  83  83  GLN GLN A . n 
A 1 85  ASN 85  84  84  ASN ASN A . n 
A 1 86  CYS 86  85  85  CYS CYS A . n 
A 1 87  VAL 87  86  86  VAL VAL A . n 
A 1 88  LEU 88  87  87  LEU LEU A . n 
A 1 89  LYS 89  88  88  LYS LYS A . n 
A 1 90  LEU 90  89  89  LEU LEU A . n 
A 1 91  LYS 91  90  90  LYS LYS A . n 
A 1 92  VAL 92  91  91  VAL VAL A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  THR 94  93  93  THR THR A . n 
A 1 95  ALA 95  94  94  ALA ALA A . n 
A 1 96  ASN 96  95  95  ASN ASN A . n 
A 1 97  PRO 97  96  96  PRO PRO A . n 
A 1 98  LYS 98  97  97  LYS LYS A . n 
A 1 99  THR 99  98  98  THR THR A . n 
A 1 100 PRO 100 99  99  PRO PRO A . n 
A 1 101 LYS 101 100 100 LYS LYS A . n 
A 1 102 TYR 102 101 101 TYR TYR A . n 
A 1 103 LYS 103 102 102 LYS LYS A . n 
A 1 104 PHE 104 103 103 PHE PHE A . n 
A 1 105 VAL 105 104 104 VAL VAL A . n 
A 1 106 ARG 106 105 105 ARG ARG A . n 
A 1 107 ILE 107 106 106 ILE ILE A . n 
A 1 108 GLN 108 107 107 GLN GLN A . n 
A 1 109 PRO 109 108 108 PRO PRO A . n 
A 1 110 GLY 110 109 109 GLY GLY A . n 
A 1 111 GLN 111 110 110 GLN GLN A . n 
A 1 112 THR 112 111 111 THR THR A . n 
A 1 113 PHE 113 112 112 PHE PHE A . n 
A 1 114 SER 114 113 113 SER SER A . n 
A 1 115 VAL 115 114 114 VAL VAL A . n 
A 1 116 LEU 116 115 115 LEU LEU A . n 
A 1 117 ALA 117 116 116 ALA ALA A . n 
A 1 118 CYS 118 117 117 CYS CYS A . n 
A 1 119 TYR 119 118 118 TYR TYR A . n 
A 1 120 ASN 120 119 119 ASN ASN A . n 
A 1 121 GLY 121 120 120 GLY GLY A . n 
A 1 122 SER 122 121 121 SER SER A . n 
A 1 123 PRO 123 122 122 PRO PRO A . n 
A 1 124 SER 124 123 123 SER SER A . n 
A 1 125 GLY 125 124 124 GLY GLY A . n 
A 1 126 VAL 126 125 125 VAL VAL A . n 
A 1 127 TYR 127 126 126 TYR TYR A . n 
A 1 128 GLN 128 127 127 GLN GLN A . n 
A 1 129 CYS 129 128 128 CYS CYS A . n 
A 1 130 ALA 130 129 129 ALA ALA A . n 
A 1 131 MET 131 130 130 MET MET A . n 
A 1 132 ARG 132 131 131 ARG ARG A . n 
A 1 133 PRO 133 132 132 PRO PRO A . n 
A 1 134 ASN 134 133 133 ASN ASN A . n 
A 1 135 PHE 135 134 134 PHE PHE A . n 
A 1 136 THR 136 135 135 THR THR A . n 
A 1 137 ILE 137 136 136 ILE ILE A . n 
A 1 138 LYS 138 137 137 LYS LYS A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 SER 140 139 139 SER SER A . n 
A 1 141 PHE 141 140 140 PHE PHE A . n 
A 1 142 LEU 142 141 141 LEU LEU A . n 
A 1 143 ASN 143 142 142 ASN ASN A . n 
A 1 144 GLY 144 143 143 GLY GLY A . n 
A 1 145 SER 145 144 144 SER SER A . n 
A 1 146 CYS 146 145 145 CYS CYS A . n 
A 1 147 GLY 147 146 146 GLY GLY A . n 
A 1 148 SER 148 147 147 SER SER A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 GLY 150 149 149 GLY GLY A . n 
A 1 151 PHE 151 150 150 PHE PHE A . n 
A 1 152 ASN 152 151 151 ASN ASN A . n 
A 1 153 ILE 153 152 152 ILE ILE A . n 
A 1 154 ASP 154 153 153 ASP ASP A . n 
A 1 155 TYR 155 154 154 TYR TYR A . n 
A 1 156 ASP 156 155 155 ASP ASP A . n 
A 1 157 CYS 157 156 156 CYS CYS A . n 
A 1 158 VAL 158 157 157 VAL VAL A . n 
A 1 159 SER 159 158 158 SER SER A . n 
A 1 160 PHE 160 159 159 PHE PHE A . n 
A 1 161 CYS 161 160 160 CYS CYS A . n 
A 1 162 TYR 162 161 161 TYR TYR A . n 
A 1 163 MET 163 162 162 MET MET A . n 
A 1 164 HIS 164 163 163 HIS HIS A . n 
A 1 165 HIS 165 164 164 HIS HIS A . n 
A 1 166 MET 166 165 165 MET MET A . n 
A 1 167 GLU 167 166 166 GLU GLU A . n 
A 1 168 LEU 168 167 167 LEU LEU A . n 
A 1 169 PRO 169 168 168 PRO PRO A . n 
A 1 170 THR 170 169 169 THR THR A . n 
A 1 171 GLY 171 170 170 GLY GLY A . n 
A 1 172 VAL 172 171 171 VAL VAL A . n 
A 1 173 HIS 173 172 172 HIS HIS A . n 
A 1 174 ALA 174 173 173 ALA ALA A . n 
A 1 175 GLY 175 174 174 GLY GLY A . n 
A 1 176 THR 176 175 175 THR THR A . n 
A 1 177 ASP 177 176 176 ASP ASP A . n 
A 1 178 LEU 178 177 177 LEU LEU A . n 
A 1 179 GLU 179 178 178 GLU GLU A . n 
A 1 180 GLY 180 179 179 GLY GLY A . n 
A 1 181 ASN 181 180 180 ASN ASN A . n 
A 1 182 PHE 182 181 181 PHE PHE A . n 
A 1 183 TYR 183 182 182 TYR TYR A . n 
A 1 184 GLY 184 183 183 GLY GLY A . n 
A 1 185 PRO 185 184 184 PRO PRO A . n 
A 1 186 PHE 186 185 185 PHE PHE A . n 
A 1 187 VAL 187 186 186 VAL VAL A . n 
A 1 188 ASP 188 187 187 ASP ASP A . n 
A 1 189 ARG 189 188 188 ARG ARG A . n 
A 1 190 GLN 190 189 189 GLN GLN A . n 
A 1 191 THR 191 190 190 THR THR A . n 
A 1 192 ALA 192 191 191 ALA ALA A . n 
A 1 193 GLN 193 192 192 GLN GLN A . n 
A 1 194 ALA 194 193 193 ALA ALA A . n 
A 1 195 ALA 195 194 194 ALA ALA A . n 
A 1 196 GLY 196 195 195 GLY GLY A . n 
A 1 197 THR 197 196 196 THR THR A . n 
A 1 198 ASP 198 197 197 ASP ASP A . n 
A 1 199 THR 199 198 198 THR THR A . n 
A 1 200 THR 200 199 199 THR THR A . n 
A 1 201 ILE 201 200 200 ILE ILE A . n 
A 1 202 THR 202 201 201 THR THR A . n 
A 1 203 VAL 203 202 202 VAL VAL A . n 
A 1 204 ASN 204 203 203 ASN ASN A . n 
A 1 205 VAL 205 204 204 VAL VAL A . n 
A 1 206 LEU 206 205 205 LEU LEU A . n 
A 1 207 ALA 207 206 206 ALA ALA A . n 
A 1 208 TRP 208 207 207 TRP TRP A . n 
A 1 209 LEU 209 208 208 LEU LEU A . n 
A 1 210 TYR 210 209 209 TYR TYR A . n 
A 1 211 ALA 211 210 210 ALA ALA A . n 
A 1 212 ALA 212 211 211 ALA ALA A . n 
A 1 213 VAL 213 212 212 VAL VAL A . n 
A 1 214 ILE 214 213 213 ILE ILE A . n 
A 1 215 ASN 215 214 214 ASN ASN A . n 
A 1 216 GLY 216 215 215 GLY GLY A . n 
A 1 217 ASP 217 216 216 ASP ASP A . n 
A 1 218 ARG 218 217 217 ARG ARG A . n 
A 1 219 TRP 219 218 218 TRP TRP A . n 
A 1 220 PHE 220 219 219 PHE PHE A . n 
A 1 221 LEU 221 220 220 LEU LEU A . n 
A 1 222 ASN 222 221 221 ASN ASN A . n 
A 1 223 ARG 223 222 222 ARG ARG A . n 
A 1 224 PHE 224 223 223 PHE PHE A . n 
A 1 225 THR 225 224 224 THR THR A . n 
A 1 226 THR 226 225 225 THR THR A . n 
A 1 227 THR 227 226 226 THR THR A . n 
A 1 228 LEU 228 227 227 LEU LEU A . n 
A 1 229 ASN 229 228 228 ASN ASN A . n 
A 1 230 ASP 230 229 229 ASP ASP A . n 
A 1 231 PHE 231 230 230 PHE PHE A . n 
A 1 232 ASN 232 231 231 ASN ASN A . n 
A 1 233 LEU 233 232 232 LEU LEU A . n 
A 1 234 VAL 234 233 233 VAL VAL A . n 
A 1 235 ALA 235 234 234 ALA ALA A . n 
A 1 236 MET 236 235 235 MET MET A . n 
A 1 237 LYS 237 236 236 LYS LYS A . n 
A 1 238 TYR 238 237 237 TYR TYR A . n 
A 1 239 ASN 239 238 238 ASN ASN A . n 
A 1 240 TYR 240 239 239 TYR TYR A . n 
A 1 241 GLU 241 240 240 GLU GLU A . n 
A 1 242 PRO 242 241 241 PRO PRO A . n 
A 1 243 LEU 243 242 242 LEU LEU A . n 
A 1 244 THR 244 243 243 THR THR A . n 
A 1 245 GLN 245 244 244 GLN GLN A . n 
A 1 246 ASP 246 245 245 ASP ASP A . n 
A 1 247 HIS 247 246 246 HIS HIS A . n 
A 1 248 VAL 248 247 247 VAL VAL A . n 
A 1 249 ASP 249 248 248 ASP ASP A . n 
A 1 250 ILE 250 249 249 ILE ILE A . n 
A 1 251 LEU 251 250 250 LEU LEU A . n 
A 1 252 GLY 252 251 251 GLY GLY A . n 
A 1 253 PRO 253 252 252 PRO PRO A . n 
A 1 254 LEU 254 253 253 LEU LEU A . n 
A 1 255 SER 255 254 254 SER SER A . n 
A 1 256 ALA 256 255 255 ALA ALA A . n 
A 1 257 GLN 257 256 256 GLN GLN A . n 
A 1 258 THR 258 257 257 THR THR A . n 
A 1 259 GLY 259 258 258 GLY GLY A . n 
A 1 260 ILE 260 259 259 ILE ILE A . n 
A 1 261 ALA 261 260 260 ALA ALA A . n 
A 1 262 VAL 262 261 261 VAL VAL A . n 
A 1 263 LEU 263 262 262 LEU LEU A . n 
A 1 264 ASP 264 263 263 ASP ASP A . n 
A 1 265 MET 265 264 264 MET MET A . n 
A 1 266 CYS 266 265 265 CYS CYS A . n 
A 1 267 ALA 267 266 266 ALA ALA A . n 
A 1 268 SER 268 267 267 SER SER A . n 
A 1 269 LEU 269 268 268 LEU LEU A . n 
A 1 270 LYS 270 269 269 LYS LYS A . n 
A 1 271 GLU 271 270 270 GLU GLU A . n 
A 1 272 LEU 272 271 271 LEU LEU A . n 
A 1 273 LEU 273 272 272 LEU LEU A . n 
A 1 274 GLN 274 273 273 GLN GLN A . n 
A 1 275 ASN 275 274 274 ASN ASN A . n 
A 1 276 GLY 276 275 275 GLY GLY A . n 
A 1 277 MET 277 276 276 MET MET A . n 
A 1 278 ASN 278 277 277 ASN ASN A . n 
A 1 279 GLY 279 278 278 GLY GLY A . n 
A 1 280 ARG 280 279 279 ARG ARG A . n 
A 1 281 THR 281 280 280 THR THR A . n 
A 1 282 ILE 282 281 281 ILE ILE A . n 
A 1 283 LEU 283 282 282 LEU LEU A . n 
A 1 284 GLY 284 283 283 GLY GLY A . n 
A 1 285 SER 285 284 284 SER SER A . n 
A 1 286 ALA 286 285 285 ALA ALA A . n 
A 1 287 LEU 287 286 286 LEU LEU A . n 
A 1 288 LEU 288 287 287 LEU LEU A . n 
A 1 289 GLU 289 288 288 GLU GLU A . n 
A 1 290 ASP 290 289 289 ASP ASP A . n 
A 1 291 GLU 291 290 290 GLU GLU A . n 
A 1 292 PHE 292 291 291 PHE PHE A . n 
A 1 293 THR 293 292 292 THR THR A . n 
A 1 294 PRO 294 293 293 PRO PRO A . n 
A 1 295 PHE 295 294 294 PHE PHE A . n 
A 1 296 ASP 296 295 295 ASP ASP A . n 
A 1 297 VAL 297 296 296 VAL VAL A . n 
A 1 298 VAL 298 297 297 VAL VAL A . n 
A 1 299 ARG 299 298 298 ARG ARG A . n 
A 1 300 GLN 300 299 299 GLN GLN A . n 
A 1 301 CYS 301 300 300 CYS CYS A . n 
A 1 302 SER 302 301 301 SER SER A . n 
A 1 303 GLY 303 302 302 GLY GLY A . n 
A 1 304 VAL 304 303 303 VAL VAL A . n 
A 1 305 THR 305 304 ?   ?   ?   A . n 
A 1 306 PHE 306 305 ?   ?   ?   A . n 
A 1 307 GLN 307 306 ?   ?   ?   A . n 
A 1 308 LEU 308 307 ?   ?   ?   A . n 
A 1 309 GLU 309 308 ?   ?   ?   A . n 
A 1 310 HIS 310 309 ?   ?   ?   A . n 
A 1 311 HIS 311 310 ?   ?   ?   A . n 
A 1 312 HIS 312 311 ?   ?   ?   A . n 
A 1 313 HIS 313 312 ?   ?   ?   A . n 
A 1 314 HIS 314 313 ?   ?   ?   A . n 
A 1 315 HIS 315 314 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BCX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BCX 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1BCX 1   401 401 A1BCX LIG A . 
C 3 HOH   1   501 193 HOH   HOH A . 
C 3 HOH   2   502 420 HOH   HOH A . 
C 3 HOH   3   503 247 HOH   HOH A . 
C 3 HOH   4   504 26  HOH   HOH A . 
C 3 HOH   5   505 397 HOH   HOH A . 
C 3 HOH   6   506 136 HOH   HOH A . 
C 3 HOH   7   507 30  HOH   HOH A . 
C 3 HOH   8   508 302 HOH   HOH A . 
C 3 HOH   9   509 164 HOH   HOH A . 
C 3 HOH   10  510 227 HOH   HOH A . 
C 3 HOH   11  511 314 HOH   HOH A . 
C 3 HOH   12  512 16  HOH   HOH A . 
C 3 HOH   13  513 9   HOH   HOH A . 
C 3 HOH   14  514 281 HOH   HOH A . 
C 3 HOH   15  515 131 HOH   HOH A . 
C 3 HOH   16  516 28  HOH   HOH A . 
C 3 HOH   17  517 73  HOH   HOH A . 
C 3 HOH   18  518 12  HOH   HOH A . 
C 3 HOH   19  519 126 HOH   HOH A . 
C 3 HOH   20  520 451 HOH   HOH A . 
C 3 HOH   21  521 225 HOH   HOH A . 
C 3 HOH   22  522 32  HOH   HOH A . 
C 3 HOH   23  523 54  HOH   HOH A . 
C 3 HOH   24  524 287 HOH   HOH A . 
C 3 HOH   25  525 37  HOH   HOH A . 
C 3 HOH   26  526 36  HOH   HOH A . 
C 3 HOH   27  527 10  HOH   HOH A . 
C 3 HOH   28  528 179 HOH   HOH A . 
C 3 HOH   29  529 234 HOH   HOH A . 
C 3 HOH   30  530 51  HOH   HOH A . 
C 3 HOH   31  531 138 HOH   HOH A . 
C 3 HOH   32  532 96  HOH   HOH A . 
C 3 HOH   33  533 8   HOH   HOH A . 
C 3 HOH   34  534 14  HOH   HOH A . 
C 3 HOH   35  535 161 HOH   HOH A . 
C 3 HOH   36  536 283 HOH   HOH A . 
C 3 HOH   37  537 130 HOH   HOH A . 
C 3 HOH   38  538 334 HOH   HOH A . 
C 3 HOH   39  539 1   HOH   HOH A . 
C 3 HOH   40  540 55  HOH   HOH A . 
C 3 HOH   41  541 217 HOH   HOH A . 
C 3 HOH   42  542 23  HOH   HOH A . 
C 3 HOH   43  543 104 HOH   HOH A . 
C 3 HOH   44  544 485 HOH   HOH A . 
C 3 HOH   45  545 34  HOH   HOH A . 
C 3 HOH   46  546 21  HOH   HOH A . 
C 3 HOH   47  547 160 HOH   HOH A . 
C 3 HOH   48  548 416 HOH   HOH A . 
C 3 HOH   49  549 209 HOH   HOH A . 
C 3 HOH   50  550 3   HOH   HOH A . 
C 3 HOH   51  551 329 HOH   HOH A . 
C 3 HOH   52  552 5   HOH   HOH A . 
C 3 HOH   53  553 95  HOH   HOH A . 
C 3 HOH   54  554 445 HOH   HOH A . 
C 3 HOH   55  555 25  HOH   HOH A . 
C 3 HOH   56  556 120 HOH   HOH A . 
C 3 HOH   57  557 4   HOH   HOH A . 
C 3 HOH   58  558 98  HOH   HOH A . 
C 3 HOH   59  559 77  HOH   HOH A . 
C 3 HOH   60  560 38  HOH   HOH A . 
C 3 HOH   61  561 278 HOH   HOH A . 
C 3 HOH   62  562 20  HOH   HOH A . 
C 3 HOH   63  563 52  HOH   HOH A . 
C 3 HOH   64  564 18  HOH   HOH A . 
C 3 HOH   65  565 417 HOH   HOH A . 
C 3 HOH   66  566 124 HOH   HOH A . 
C 3 HOH   67  567 24  HOH   HOH A . 
C 3 HOH   68  568 74  HOH   HOH A . 
C 3 HOH   69  569 218 HOH   HOH A . 
C 3 HOH   70  570 189 HOH   HOH A . 
C 3 HOH   71  571 11  HOH   HOH A . 
C 3 HOH   72  572 427 HOH   HOH A . 
C 3 HOH   73  573 35  HOH   HOH A . 
C 3 HOH   74  574 13  HOH   HOH A . 
C 3 HOH   75  575 299 HOH   HOH A . 
C 3 HOH   76  576 282 HOH   HOH A . 
C 3 HOH   77  577 448 HOH   HOH A . 
C 3 HOH   78  578 170 HOH   HOH A . 
C 3 HOH   79  579 212 HOH   HOH A . 
C 3 HOH   80  580 210 HOH   HOH A . 
C 3 HOH   81  581 468 HOH   HOH A . 
C 3 HOH   82  582 63  HOH   HOH A . 
C 3 HOH   83  583 461 HOH   HOH A . 
C 3 HOH   84  584 266 HOH   HOH A . 
C 3 HOH   85  585 159 HOH   HOH A . 
C 3 HOH   86  586 239 HOH   HOH A . 
C 3 HOH   87  587 93  HOH   HOH A . 
C 3 HOH   88  588 343 HOH   HOH A . 
C 3 HOH   89  589 216 HOH   HOH A . 
C 3 HOH   90  590 277 HOH   HOH A . 
C 3 HOH   91  591 249 HOH   HOH A . 
C 3 HOH   92  592 339 HOH   HOH A . 
C 3 HOH   93  593 186 HOH   HOH A . 
C 3 HOH   94  594 490 HOH   HOH A . 
C 3 HOH   95  595 431 HOH   HOH A . 
C 3 HOH   96  596 279 HOH   HOH A . 
C 3 HOH   97  597 45  HOH   HOH A . 
C 3 HOH   98  598 507 HOH   HOH A . 
C 3 HOH   99  599 178 HOH   HOH A . 
C 3 HOH   100 600 487 HOH   HOH A . 
C 3 HOH   101 601 129 HOH   HOH A . 
C 3 HOH   102 602 477 HOH   HOH A . 
C 3 HOH   103 603 251 HOH   HOH A . 
C 3 HOH   104 604 215 HOH   HOH A . 
C 3 HOH   105 605 263 HOH   HOH A . 
C 3 HOH   106 606 200 HOH   HOH A . 
C 3 HOH   107 607 112 HOH   HOH A . 
C 3 HOH   108 608 49  HOH   HOH A . 
C 3 HOH   109 609 233 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_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21.1_5286 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   102.614 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DU3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     113.950 
_cell.length_a_esd                 ? 
_cell.length_b                     53.640 
_cell.length_b_esd                 ? 
_cell.length_c                     45.440 
_cell.length_c_esd                 ? 
_cell.volume                       271038.175 
_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                         9DU3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DU3 
_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             1.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.42 
_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    '20% PEG 3350, 0.2M Ammonium Tartrate Dibasic' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          38.91 
_reflns.entry_id                                       9DU3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.07 
_reflns.d_resolution_low                               34.33 
_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                                     15953 
_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                           95.81 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.26 
_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                                   0.98 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.07 
_reflns_shell.d_res_low                                     2.144 
_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                             1488 
_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                                  0.837 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               50.16 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DU3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.07 
_refine.ls_d_res_low                             34.33 
_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                     15814 
_refine.ls_number_reflns_R_free                  723 
_refine.ls_number_reflns_R_work                  15091 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.84 
_refine.ls_percent_reflns_R_free                 4.57 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2194 
_refine.ls_R_factor_R_free                       0.2444 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2182 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 32.5057 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3351 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.07 
_refine_hist.d_res_low                        34.33 
_refine_hist.number_atoms_solvent             109 
_refine_hist.number_atoms_total               2481 
_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        2340 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_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_restraint_function 
'X-RAY DIFFRACTION' ? 0.0023  ? 2427 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5419  ? 3300 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0415  ? 370  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0049  ? 435  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.7811 ? 885  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.07 2.23  . . 140 2883 92.67 . . . . 0.3633 . . . . . . . . . . . 0.4061 
'X-RAY DIFFRACTION' 2.23 2.45  . . 150 2924 94.24 . . . . 0.3118 . . . . . . . . . . . 0.3369 
'X-RAY DIFFRACTION' 2.45 2.81  . . 138 3016 95.60 . . . . 0.2742 . . . . . . . . . . . 0.3099 
'X-RAY DIFFRACTION' 2.81 3.53  . . 141 3103 97.95 . . . . 0.2236 . . . . . . . . . . . 0.2688 
'X-RAY DIFFRACTION' 3.53 34.33 . . 154 3165 98.63 . . . . 0.1698 . . . . . . . . . . . 0.1842 
# 
_struct.entry_id                     9DU3 
_struct.title                        'SARS-CoV-2 Mpro in complex with compound 1' 
_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        9DU3 
_struct_keywords.text            
;SARS-CoV-2 Mpro Hydrolase, Compound 5, Corona Virus, Aldehyde and Nitrile based inhibitors, VIRAL PROTEIN, HYDROLASE-INHIBITOR complex
;
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, HYDROLASE/INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 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              9DU3 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 307 
_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 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9DU3 MET A 1   ? UNP P0DTD1 ? ? 'initiating methionine' 0   1 
1 9DU3 LEU A 308 ? UNP P0DTD1 ? ? 'expression tag'        307 2 
1 9DU3 GLU A 309 ? UNP P0DTD1 ? ? 'expression tag'        308 3 
1 9DU3 HIS A 310 ? UNP P0DTD1 ? ? 'expression tag'        309 4 
1 9DU3 HIS A 311 ? UNP P0DTD1 ? ? 'expression tag'        310 5 
1 9DU3 HIS A 312 ? UNP P0DTD1 ? ? 'expression tag'        311 6 
1 9DU3 HIS A 313 ? UNP P0DTD1 ? ? 'expression tag'        312 7 
1 9DU3 HIS A 314 ? UNP P0DTD1 ? ? 'expression tag'        313 8 
1 9DU3 HIS A 315 ? UNP P0DTD1 ? ? 'expression tag'        314 9 
# 
_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)' 2770  ? 
1 MORE         -13   ? 
1 'SSA (A^2)'  25410 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
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   1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
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 11  ? GLY A 16  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 42  ? CYS A 45  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 ASN A 54  ? ARG A 61  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P4  AA4 LYS A 62  ? PHE A 67  ? LYS A 61  PHE A 66  5 ? 6  
HELX_P HELX_P5  AA5 ILE A 201 ? ASN A 215 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P6  AA6 THR A 227 ? MET A 236 ? THR A 226 MET A 235 1 ? 10 
HELX_P HELX_P7  AA7 THR A 244 ? LEU A 251 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P8  AA8 LEU A 251 ? GLY A 259 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P9  AA9 ALA A 261 ? GLY A 276 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P10 AB1 THR A 293 ? GLY A 303 ? 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        none 
_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            146 
_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           A1BCX 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C34 
_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            A1BCX 
_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               1.766 
_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                      A1BCX 
_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      146 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1BCX 
_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               C34 
_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                        A1BCX 
_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 74  ? LEU A 76  ? VAL A 73  LEU A 75  
AA1 2 LEU A 68  ? ALA A 71  ? LEU A 67  ALA A 70  
AA1 3 MET A 18  ? CYS A 23  ? MET A 17  CYS A 22  
AA1 4 THR A 26  ? LEU A 33  ? THR A 25  LEU A 32  
AA1 5 VAL A 36  ? PRO A 40  ? VAL A 35  PRO A 39  
AA1 6 VAL A 87  ? VAL A 92  ? VAL A 86  VAL A 91  
AA1 7 VAL A 78  ? GLN A 84  ? VAL A 77  GLN A 83  
AA2 1 TYR A 102 ? PHE A 104 ? TYR A 101 PHE A 103 
AA2 2 CYS A 157 ? GLU A 167 ? CYS A 156 GLU A 166 
AA2 3 VAL A 149 ? ASP A 154 ? VAL A 148 ASP A 153 
AA2 4 THR A 112 ? TYR A 119 ? THR A 111 TYR A 118 
AA2 5 SER A 122 ? ALA A 130 ? SER A 121 ALA A 129 
AA3 1 TYR A 102 ? PHE A 104 ? TYR A 101 PHE A 103 
AA3 2 CYS A 157 ? GLU A 167 ? CYS A 156 GLU A 166 
AA3 3 HIS A 173 ? THR A 176 ? HIS A 172 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 74  ? O VAL A 73  N ALA A 71  ? N ALA A 70  
AA1 2 3 O GLN A 70  ? O GLN A 69  N GLN A 20  ? N GLN A 19  
AA1 3 4 N VAL A 21  ? N VAL A 20  O LEU A 28  ? O LEU A 27  
AA1 4 5 N LEU A 31  ? N LEU A 30  O TYR A 38  ? O TYR A 37  
AA1 5 6 N VAL A 37  ? N VAL A 36  O LEU A 90  ? O LEU A 89  
AA1 6 7 O LYS A 91  ? O LYS A 90  N ILE A 79  ? N ILE A 78  
AA2 1 2 N LYS A 103 ? N LYS A 102 O VAL A 158 ? O VAL A 157 
AA2 2 3 O CYS A 157 ? O CYS A 156 N ASP A 154 ? N ASP A 153 
AA2 3 4 O PHE A 151 ? O PHE A 150 N SER A 114 ? N SER A 113 
AA2 4 5 N VAL A 115 ? N VAL A 114 O TYR A 127 ? O TYR A 126 
AA3 1 2 N LYS A 103 ? N LYS A 102 O VAL A 158 ? O VAL A 157 
AA3 2 3 N MET A 166 ? N MET A 165 O ALA A 174 ? O ALA A 173 
# 
_pdbx_entry_details.entry_id                   9DU3 
_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_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  ? ? 52.54   -131.04 
2 1 HIS A 41  ? ? -66.04  5.19    
3 1 ASN A 84  ? ? 49.83   -122.88 
4 1 TYR A 154 ? ? 56.64   -87.51  
5 1 ARG A 217 ? ? -142.01 13.00   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     608 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 12.1596577162 -21.2836186977 14.8470537518 0.340749120928 ? -0.0536732329153  ? 0.0317536070808  ? 
0.383162202446 ? 0.0219174174028  ? 0.297982718122 ? 3.50446964545 ? -0.355310588945 ? 1.74792639464   ? 2.89926794269 ? 
-0.489375483101  ? 1.37644550191 ? 0.192601317209   ? -0.308570597539  ? -0.328908238489 ? 0.186220557563     ? -0.0802025567314 ? 
-0.10437980811   ? 0.247560347201  ? -0.142934717367  ? -0.13112701545   ? 
2 'X-RAY DIFFRACTION' ? refined 11.5506687961 -6.90795674751 7.24955508598 0.30109352198  ? -0.00492387301324 ? 0.0383713325564  ? 
0.392186266512 ? -0.0345132520372 ? 0.288241962716 ? 2.0507048292  ? -0.313169032276 ? 1.13072574476   ? 1.93829525764 ? 
-1.04709609886   ? 1.74725245042 ? -0.0829048976111 ? -0.0338131332907 ? 0.167798929463  ? -5.61864352364e-05 ? -0.0519140202283 ? 
-0.106659333292  ? 0.100548395162  ? 0.00990745061932 ? 0.122223033633   ? 
3 'X-RAY DIFFRACTION' ? refined 12.7454879178 8.44563406382  -9.9611225707 0.394211393825 ? -0.136564330656   ? -0.0390729591943 ? 
0.590871781386 ? 0.122215582638   ? 0.444414745583 ? 2.04090569075 ? 0.228623648425  ? -0.845844358135 ? 1.78923664112 ? 
-0.0512579721925 ? 2.62880342861 ? -0.0502869007038 ? 0.380319668455   ? 0.402436939263  ? 0.0967698134217    ? 0.0250420760607  ? 
-0.0214877858183 ? -0.227644766105 ? 0.4104383501     ? 0.00432240214996 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 1   ? A 110 A 110 ? ? 
;chain 'A' and (resid    1  through  110 )
;
2 'X-RAY DIFFRACTION' 2 A 111 A 111 ? A 213 A 213 ? ? 
;chain 'A' and (resid  111  through  213 )
;
3 'X-RAY DIFFRACTION' 3 A 214 A 214 ? A 303 A 303 ? ? 
;chain 'A' and (resid  214  through  303 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 0   ? A MET 1   
2  1 Y 1 A THR 304 ? A THR 305 
3  1 Y 1 A PHE 305 ? A PHE 306 
4  1 Y 1 A GLN 306 ? A GLN 307 
5  1 Y 1 A LEU 307 ? A LEU 308 
6  1 Y 1 A GLU 308 ? A GLU 309 
7  1 Y 1 A HIS 309 ? A HIS 310 
8  1 Y 1 A HIS 310 ? A HIS 311 
9  1 Y 1 A HIS 311 ? A HIS 312 
10 1 Y 1 A HIS 312 ? A HIS 313 
11 1 Y 1 A HIS 313 ? A HIS 314 
12 1 Y 1 A HIS 314 ? A HIS 315 
# 
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 
A1BCX C4   C Y N 1   
A1BCX C5   C Y N 2   
A1BCX C6   C Y N 3   
A1BCX C7   C Y N 4   
A1BCX C10  C Y N 5   
A1BCX C15  C N S 6   
A1BCX C17  C N N 7   
A1BCX C21  C N N 8   
A1BCX C24  C N S 9   
A1BCX C26  C N N 10  
A1BCX C1   C N N 11  
A1BCX C11  C Y N 12  
A1BCX C12  C N N 13  
A1BCX C27  C N R 14  
A1BCX C29  C N N 15  
A1BCX C3   C Y N 16  
A1BCX C30  C N N 17  
A1BCX C32  C N N 18  
A1BCX C34  C N N 19  
A1BCX C38  C N N 20  
A1BCX C39  C N N 21  
A1BCX C40  C N N 22  
A1BCX C9   C Y N 23  
A1BCX N14  N N N 24  
A1BCX N23  N N N 25  
A1BCX N31  N N N 26  
A1BCX N8   N Y N 27  
A1BCX O13  O N N 28  
A1BCX O2   O N N 29  
A1BCX O22  O N N 30  
A1BCX O33  O N N 31  
A1BCX O36  O N N 32  
A1BCX H4   H N N 33  
A1BCX H5   H N N 34  
A1BCX H6   H N N 35  
A1BCX H8   H N N 36  
A1BCX H10  H N N 37  
A1BCX H17  H N N 38  
A1BCX H170 H N N 39  
A1BCX H21  H N N 40  
A1BCX H22  H N N 41  
A1BCX H23  H N N 42  
A1BCX H3   H N N 43  
A1BCX H2   H N N 44  
A1BCX H1   H N N 45  
A1BCX H24  H N N 46  
A1BCX H26  H N N 47  
A1BCX H25  H N N 48  
A1BCX H28  H N N 49  
A1BCX H27  H N N 50  
A1BCX H34  H N N 51  
A1BCX H340 H N N 52  
A1BCX H38  H N N 53  
A1BCX H39A H N N 54  
A1BCX H39B H N N 55  
A1BCX H40B H N N 56  
A1BCX H40A H N N 57  
A1BCX H9   H N N 58  
A1BCX H20  H N N 59  
A1BCX H29  H N N 60  
A1BCX H7   H N N 61  
A1BCX H36  H N N 62  
ALA   N    N N N 63  
ALA   CA   C N S 64  
ALA   C    C N N 65  
ALA   O    O N N 66  
ALA   CB   C N N 67  
ALA   OXT  O N N 68  
ALA   H    H N N 69  
ALA   H2   H N N 70  
ALA   HA   H N N 71  
ALA   HB1  H N N 72  
ALA   HB2  H N N 73  
ALA   HB3  H N N 74  
ALA   HXT  H N N 75  
ARG   N    N N N 76  
ARG   CA   C N S 77  
ARG   C    C N N 78  
ARG   O    O N N 79  
ARG   CB   C N N 80  
ARG   CG   C N N 81  
ARG   CD   C N N 82  
ARG   NE   N N N 83  
ARG   CZ   C N N 84  
ARG   NH1  N N N 85  
ARG   NH2  N N N 86  
ARG   OXT  O N N 87  
ARG   H    H N N 88  
ARG   H2   H N N 89  
ARG   HA   H N N 90  
ARG   HB2  H N N 91  
ARG   HB3  H N N 92  
ARG   HG2  H N N 93  
ARG   HG3  H N N 94  
ARG   HD2  H N N 95  
ARG   HD3  H N N 96  
ARG   HE   H N N 97  
ARG   HH11 H N N 98  
ARG   HH12 H N N 99  
ARG   HH21 H N N 100 
ARG   HH22 H N N 101 
ARG   HXT  H N N 102 
ASN   N    N N N 103 
ASN   CA   C N S 104 
ASN   C    C N N 105 
ASN   O    O N N 106 
ASN   CB   C N N 107 
ASN   CG   C N N 108 
ASN   OD1  O N N 109 
ASN   ND2  N N N 110 
ASN   OXT  O N N 111 
ASN   H    H N N 112 
ASN   H2   H N N 113 
ASN   HA   H N N 114 
ASN   HB2  H N N 115 
ASN   HB3  H N N 116 
ASN   HD21 H N N 117 
ASN   HD22 H N N 118 
ASN   HXT  H N N 119 
ASP   N    N N N 120 
ASP   CA   C N S 121 
ASP   C    C N N 122 
ASP   O    O N N 123 
ASP   CB   C N N 124 
ASP   CG   C N N 125 
ASP   OD1  O N N 126 
ASP   OD2  O N N 127 
ASP   OXT  O N N 128 
ASP   H    H N N 129 
ASP   H2   H N N 130 
ASP   HA   H N N 131 
ASP   HB2  H N N 132 
ASP   HB3  H N N 133 
ASP   HD2  H N N 134 
ASP   HXT  H N N 135 
CYS   N    N N N 136 
CYS   CA   C N R 137 
CYS   C    C N N 138 
CYS   O    O N N 139 
CYS   CB   C N N 140 
CYS   SG   S N N 141 
CYS   OXT  O N N 142 
CYS   H    H N N 143 
CYS   H2   H N N 144 
CYS   HA   H N N 145 
CYS   HB2  H N N 146 
CYS   HB3  H N N 147 
CYS   HG   H N N 148 
CYS   HXT  H N N 149 
GLN   N    N N N 150 
GLN   CA   C N S 151 
GLN   C    C N N 152 
GLN   O    O N N 153 
GLN   CB   C N N 154 
GLN   CG   C N N 155 
GLN   CD   C N N 156 
GLN   OE1  O N N 157 
GLN   NE2  N N N 158 
GLN   OXT  O N N 159 
GLN   H    H N N 160 
GLN   H2   H N N 161 
GLN   HA   H N N 162 
GLN   HB2  H N N 163 
GLN   HB3  H N N 164 
GLN   HG2  H N N 165 
GLN   HG3  H N N 166 
GLN   HE21 H N N 167 
GLN   HE22 H N N 168 
GLN   HXT  H N N 169 
GLU   N    N N N 170 
GLU   CA   C N S 171 
GLU   C    C N N 172 
GLU   O    O N N 173 
GLU   CB   C N N 174 
GLU   CG   C N N 175 
GLU   CD   C N N 176 
GLU   OE1  O N N 177 
GLU   OE2  O N N 178 
GLU   OXT  O N N 179 
GLU   H    H N N 180 
GLU   H2   H N N 181 
GLU   HA   H N N 182 
GLU   HB2  H N N 183 
GLU   HB3  H N N 184 
GLU   HG2  H N N 185 
GLU   HG3  H N N 186 
GLU   HE2  H N N 187 
GLU   HXT  H N N 188 
GLY   N    N N N 189 
GLY   CA   C N N 190 
GLY   C    C N N 191 
GLY   O    O N N 192 
GLY   OXT  O N N 193 
GLY   H    H N N 194 
GLY   H2   H N N 195 
GLY   HA2  H N N 196 
GLY   HA3  H N N 197 
GLY   HXT  H N N 198 
HIS   N    N N N 199 
HIS   CA   C N S 200 
HIS   C    C N N 201 
HIS   O    O N N 202 
HIS   CB   C N N 203 
HIS   CG   C Y N 204 
HIS   ND1  N Y N 205 
HIS   CD2  C Y N 206 
HIS   CE1  C Y N 207 
HIS   NE2  N Y N 208 
HIS   OXT  O N N 209 
HIS   H    H N N 210 
HIS   H2   H N N 211 
HIS   HA   H N N 212 
HIS   HB2  H N N 213 
HIS   HB3  H N N 214 
HIS   HD1  H N N 215 
HIS   HD2  H N N 216 
HIS   HE1  H N N 217 
HIS   HE2  H N N 218 
HIS   HXT  H N N 219 
HOH   O    O N N 220 
HOH   H1   H N N 221 
HOH   H2   H N N 222 
ILE   N    N N N 223 
ILE   CA   C N S 224 
ILE   C    C N N 225 
ILE   O    O N N 226 
ILE   CB   C N S 227 
ILE   CG1  C N N 228 
ILE   CG2  C N N 229 
ILE   CD1  C N N 230 
ILE   OXT  O N N 231 
ILE   H    H N N 232 
ILE   H2   H N N 233 
ILE   HA   H N N 234 
ILE   HB   H N N 235 
ILE   HG12 H N N 236 
ILE   HG13 H N N 237 
ILE   HG21 H N N 238 
ILE   HG22 H N N 239 
ILE   HG23 H N N 240 
ILE   HD11 H N N 241 
ILE   HD12 H N N 242 
ILE   HD13 H N N 243 
ILE   HXT  H N N 244 
LEU   N    N N N 245 
LEU   CA   C N S 246 
LEU   C    C N N 247 
LEU   O    O N N 248 
LEU   CB   C N N 249 
LEU   CG   C N N 250 
LEU   CD1  C N N 251 
LEU   CD2  C N N 252 
LEU   OXT  O N N 253 
LEU   H    H N N 254 
LEU   H2   H N N 255 
LEU   HA   H N N 256 
LEU   HB2  H N N 257 
LEU   HB3  H N N 258 
LEU   HG   H N N 259 
LEU   HD11 H N N 260 
LEU   HD12 H N N 261 
LEU   HD13 H N N 262 
LEU   HD21 H N N 263 
LEU   HD22 H N N 264 
LEU   HD23 H N N 265 
LEU   HXT  H N N 266 
LYS   N    N N N 267 
LYS   CA   C N S 268 
LYS   C    C N N 269 
LYS   O    O N N 270 
LYS   CB   C N N 271 
LYS   CG   C N N 272 
LYS   CD   C N N 273 
LYS   CE   C N N 274 
LYS   NZ   N N N 275 
LYS   OXT  O N N 276 
LYS   H    H N N 277 
LYS   H2   H N N 278 
LYS   HA   H N N 279 
LYS   HB2  H N N 280 
LYS   HB3  H N N 281 
LYS   HG2  H N N 282 
LYS   HG3  H N N 283 
LYS   HD2  H N N 284 
LYS   HD3  H N N 285 
LYS   HE2  H N N 286 
LYS   HE3  H N N 287 
LYS   HZ1  H N N 288 
LYS   HZ2  H N N 289 
LYS   HZ3  H N N 290 
LYS   HXT  H N N 291 
MET   N    N N N 292 
MET   CA   C N S 293 
MET   C    C N N 294 
MET   O    O N N 295 
MET   CB   C N N 296 
MET   CG   C N N 297 
MET   SD   S N N 298 
MET   CE   C N N 299 
MET   OXT  O N N 300 
MET   H    H N N 301 
MET   H2   H N N 302 
MET   HA   H N N 303 
MET   HB2  H N N 304 
MET   HB3  H N N 305 
MET   HG2  H N N 306 
MET   HG3  H N N 307 
MET   HE1  H N N 308 
MET   HE2  H N N 309 
MET   HE3  H N N 310 
MET   HXT  H N N 311 
PHE   N    N N N 312 
PHE   CA   C N S 313 
PHE   C    C N N 314 
PHE   O    O N N 315 
PHE   CB   C N N 316 
PHE   CG   C Y N 317 
PHE   CD1  C Y N 318 
PHE   CD2  C Y N 319 
PHE   CE1  C Y N 320 
PHE   CE2  C Y N 321 
PHE   CZ   C Y N 322 
PHE   OXT  O N N 323 
PHE   H    H N N 324 
PHE   H2   H N N 325 
PHE   HA   H N N 326 
PHE   HB2  H N N 327 
PHE   HB3  H N N 328 
PHE   HD1  H N N 329 
PHE   HD2  H N N 330 
PHE   HE1  H N N 331 
PHE   HE2  H N N 332 
PHE   HZ   H N N 333 
PHE   HXT  H N N 334 
PRO   N    N N N 335 
PRO   CA   C N S 336 
PRO   C    C N N 337 
PRO   O    O N N 338 
PRO   CB   C N N 339 
PRO   CG   C N N 340 
PRO   CD   C N N 341 
PRO   OXT  O N N 342 
PRO   H    H N N 343 
PRO   HA   H N N 344 
PRO   HB2  H N N 345 
PRO   HB3  H N N 346 
PRO   HG2  H N N 347 
PRO   HG3  H N N 348 
PRO   HD2  H N N 349 
PRO   HD3  H N N 350 
PRO   HXT  H N N 351 
SER   N    N N N 352 
SER   CA   C N S 353 
SER   C    C N N 354 
SER   O    O N N 355 
SER   CB   C N N 356 
SER   OG   O N N 357 
SER   OXT  O N N 358 
SER   H    H N N 359 
SER   H2   H N N 360 
SER   HA   H N N 361 
SER   HB2  H N N 362 
SER   HB3  H N N 363 
SER   HG   H N N 364 
SER   HXT  H N N 365 
THR   N    N N N 366 
THR   CA   C N S 367 
THR   C    C N N 368 
THR   O    O N N 369 
THR   CB   C N R 370 
THR   OG1  O N N 371 
THR   CG2  C N N 372 
THR   OXT  O N N 373 
THR   H    H N N 374 
THR   H2   H N N 375 
THR   HA   H N N 376 
THR   HB   H N N 377 
THR   HG1  H N N 378 
THR   HG21 H N N 379 
THR   HG22 H N N 380 
THR   HG23 H N N 381 
THR   HXT  H N N 382 
TRP   N    N N N 383 
TRP   CA   C N S 384 
TRP   C    C N N 385 
TRP   O    O N N 386 
TRP   CB   C N N 387 
TRP   CG   C Y N 388 
TRP   CD1  C Y N 389 
TRP   CD2  C Y N 390 
TRP   NE1  N Y N 391 
TRP   CE2  C Y N 392 
TRP   CE3  C Y N 393 
TRP   CZ2  C Y N 394 
TRP   CZ3  C Y N 395 
TRP   CH2  C Y N 396 
TRP   OXT  O N N 397 
TRP   H    H N N 398 
TRP   H2   H N N 399 
TRP   HA   H N N 400 
TRP   HB2  H N N 401 
TRP   HB3  H N N 402 
TRP   HD1  H N N 403 
TRP   HE1  H N N 404 
TRP   HE3  H N N 405 
TRP   HZ2  H N N 406 
TRP   HZ3  H N N 407 
TRP   HH2  H N N 408 
TRP   HXT  H N N 409 
TYR   N    N N N 410 
TYR   CA   C N S 411 
TYR   C    C N N 412 
TYR   O    O N N 413 
TYR   CB   C N N 414 
TYR   CG   C Y N 415 
TYR   CD1  C Y N 416 
TYR   CD2  C Y N 417 
TYR   CE1  C Y N 418 
TYR   CE2  C Y N 419 
TYR   CZ   C Y N 420 
TYR   OH   O N N 421 
TYR   OXT  O N N 422 
TYR   H    H N N 423 
TYR   H2   H N N 424 
TYR   HA   H N N 425 
TYR   HB2  H N N 426 
TYR   HB3  H N N 427 
TYR   HD1  H N N 428 
TYR   HD2  H N N 429 
TYR   HE1  H N N 430 
TYR   HE2  H N N 431 
TYR   HH   H N N 432 
TYR   HXT  H N N 433 
VAL   N    N N N 434 
VAL   CA   C N S 435 
VAL   C    C N N 436 
VAL   O    O N N 437 
VAL   CB   C N N 438 
VAL   CG1  C N N 439 
VAL   CG2  C N N 440 
VAL   OXT  O N N 441 
VAL   H    H N N 442 
VAL   H2   H N N 443 
VAL   HA   H N N 444 
VAL   HB   H N N 445 
VAL   HG11 H N N 446 
VAL   HG12 H N N 447 
VAL   HG13 H N N 448 
VAL   HG21 H N N 449 
VAL   HG22 H N N 450 
VAL   HG23 H N N 451 
VAL   HXT  H N N 452 
# 
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 
A1BCX C1  O2   sing N N 1   
A1BCX O2  C3   sing N N 2   
A1BCX C3  C11  doub Y N 3   
A1BCX C11 C10  sing Y N 4   
A1BCX C10 C9   doub Y N 5   
A1BCX C9  C12  sing N N 6   
A1BCX C12 N14  sing N N 7   
A1BCX N14 C15  sing N N 8   
A1BCX C15 C21  sing N N 9   
A1BCX C21 N23  sing N N 10  
A1BCX N23 C24  sing N N 11  
A1BCX C24 C34  sing N N 12  
A1BCX C34 O36  sing N N 13  
A1BCX C24 C26  sing N N 14  
A1BCX C26 C27  sing N N 15  
A1BCX C27 C29  sing N N 16  
A1BCX C29 C30  sing N N 17  
A1BCX C30 N31  sing N N 18  
A1BCX N31 C32  sing N N 19  
A1BCX C32 O33  doub N N 20  
A1BCX C21 O22  doub N N 21  
A1BCX C15 C17  sing N N 22  
A1BCX C17 C38  sing N N 23  
A1BCX C38 C39  sing N N 24  
A1BCX C39 C40  sing N N 25  
A1BCX C12 O13  doub N N 26  
A1BCX C9  N8   sing Y N 27  
A1BCX N8  C7   sing Y N 28  
A1BCX C7  C6   doub Y N 29  
A1BCX C6  C5   sing Y N 30  
A1BCX C5  C4   doub Y N 31  
A1BCX C4  C3   sing Y N 32  
A1BCX C7  C11  sing Y N 33  
A1BCX C32 C27  sing N N 34  
A1BCX C40 C38  sing N N 35  
A1BCX C4  H4   sing N N 36  
A1BCX C5  H5   sing N N 37  
A1BCX C6  H6   sing N N 38  
A1BCX C10 H8   sing N N 39  
A1BCX C15 H10  sing N N 40  
A1BCX C17 H17  sing N N 41  
A1BCX C17 H170 sing N N 42  
A1BCX C24 H21  sing N N 43  
A1BCX C26 H22  sing N N 44  
A1BCX C26 H23  sing N N 45  
A1BCX C1  H3   sing N N 46  
A1BCX C1  H2   sing N N 47  
A1BCX C1  H1   sing N N 48  
A1BCX C27 H24  sing N N 49  
A1BCX C29 H26  sing N N 50  
A1BCX C29 H25  sing N N 51  
A1BCX C30 H28  sing N N 52  
A1BCX C30 H27  sing N N 53  
A1BCX C34 H34  sing N N 54  
A1BCX C34 H340 sing N N 55  
A1BCX C38 H38  sing N N 56  
A1BCX C39 H39A sing N N 57  
A1BCX C39 H39B sing N N 58  
A1BCX C40 H40B sing N N 59  
A1BCX C40 H40A sing N N 60  
A1BCX N14 H9   sing N N 61  
A1BCX N23 H20  sing N N 62  
A1BCX N31 H29  sing N N 63  
A1BCX N8  H7   sing N N 64  
A1BCX O36 H36  sing N N 65  
ALA   N   CA   sing N N 66  
ALA   N   H    sing N N 67  
ALA   N   H2   sing N N 68  
ALA   CA  C    sing N N 69  
ALA   CA  CB   sing N N 70  
ALA   CA  HA   sing N N 71  
ALA   C   O    doub N N 72  
ALA   C   OXT  sing N N 73  
ALA   CB  HB1  sing N N 74  
ALA   CB  HB2  sing N N 75  
ALA   CB  HB3  sing N N 76  
ALA   OXT HXT  sing N N 77  
ARG   N   CA   sing N N 78  
ARG   N   H    sing N N 79  
ARG   N   H2   sing N N 80  
ARG   CA  C    sing N N 81  
ARG   CA  CB   sing N N 82  
ARG   CA  HA   sing N N 83  
ARG   C   O    doub N N 84  
ARG   C   OXT  sing N N 85  
ARG   CB  CG   sing N N 86  
ARG   CB  HB2  sing N N 87  
ARG   CB  HB3  sing N N 88  
ARG   CG  CD   sing N N 89  
ARG   CG  HG2  sing N N 90  
ARG   CG  HG3  sing N N 91  
ARG   CD  NE   sing N N 92  
ARG   CD  HD2  sing N N 93  
ARG   CD  HD3  sing N N 94  
ARG   NE  CZ   sing N N 95  
ARG   NE  HE   sing N N 96  
ARG   CZ  NH1  sing N N 97  
ARG   CZ  NH2  doub N N 98  
ARG   NH1 HH11 sing N N 99  
ARG   NH1 HH12 sing N N 100 
ARG   NH2 HH21 sing N N 101 
ARG   NH2 HH22 sing N N 102 
ARG   OXT HXT  sing N N 103 
ASN   N   CA   sing N N 104 
ASN   N   H    sing N N 105 
ASN   N   H2   sing N N 106 
ASN   CA  C    sing N N 107 
ASN   CA  CB   sing N N 108 
ASN   CA  HA   sing N N 109 
ASN   C   O    doub N N 110 
ASN   C   OXT  sing N N 111 
ASN   CB  CG   sing N N 112 
ASN   CB  HB2  sing N N 113 
ASN   CB  HB3  sing N N 114 
ASN   CG  OD1  doub N N 115 
ASN   CG  ND2  sing N N 116 
ASN   ND2 HD21 sing N N 117 
ASN   ND2 HD22 sing N N 118 
ASN   OXT HXT  sing N N 119 
ASP   N   CA   sing N N 120 
ASP   N   H    sing N N 121 
ASP   N   H2   sing N N 122 
ASP   CA  C    sing N N 123 
ASP   CA  CB   sing N N 124 
ASP   CA  HA   sing N N 125 
ASP   C   O    doub N N 126 
ASP   C   OXT  sing N N 127 
ASP   CB  CG   sing N N 128 
ASP   CB  HB2  sing N N 129 
ASP   CB  HB3  sing N N 130 
ASP   CG  OD1  doub N N 131 
ASP   CG  OD2  sing N N 132 
ASP   OD2 HD2  sing N N 133 
ASP   OXT HXT  sing N N 134 
CYS   N   CA   sing N N 135 
CYS   N   H    sing N N 136 
CYS   N   H2   sing N N 137 
CYS   CA  C    sing N N 138 
CYS   CA  CB   sing N N 139 
CYS   CA  HA   sing N N 140 
CYS   C   O    doub N N 141 
CYS   C   OXT  sing N N 142 
CYS   CB  SG   sing N N 143 
CYS   CB  HB2  sing N N 144 
CYS   CB  HB3  sing N N 145 
CYS   SG  HG   sing N N 146 
CYS   OXT HXT  sing N N 147 
GLN   N   CA   sing N N 148 
GLN   N   H    sing N N 149 
GLN   N   H2   sing N N 150 
GLN   CA  C    sing N N 151 
GLN   CA  CB   sing N N 152 
GLN   CA  HA   sing N N 153 
GLN   C   O    doub N N 154 
GLN   C   OXT  sing N N 155 
GLN   CB  CG   sing N N 156 
GLN   CB  HB2  sing N N 157 
GLN   CB  HB3  sing N N 158 
GLN   CG  CD   sing N N 159 
GLN   CG  HG2  sing N N 160 
GLN   CG  HG3  sing N N 161 
GLN   CD  OE1  doub N N 162 
GLN   CD  NE2  sing N N 163 
GLN   NE2 HE21 sing N N 164 
GLN   NE2 HE22 sing N N 165 
GLN   OXT HXT  sing N N 166 
GLU   N   CA   sing N N 167 
GLU   N   H    sing N N 168 
GLU   N   H2   sing N N 169 
GLU   CA  C    sing N N 170 
GLU   CA  CB   sing N N 171 
GLU   CA  HA   sing N N 172 
GLU   C   O    doub N N 173 
GLU   C   OXT  sing N N 174 
GLU   CB  CG   sing N N 175 
GLU   CB  HB2  sing N N 176 
GLU   CB  HB3  sing N N 177 
GLU   CG  CD   sing N N 178 
GLU   CG  HG2  sing N N 179 
GLU   CG  HG3  sing N N 180 
GLU   CD  OE1  doub N N 181 
GLU   CD  OE2  sing N N 182 
GLU   OE2 HE2  sing N N 183 
GLU   OXT HXT  sing N N 184 
GLY   N   CA   sing N N 185 
GLY   N   H    sing N N 186 
GLY   N   H2   sing N N 187 
GLY   CA  C    sing N N 188 
GLY   CA  HA2  sing N N 189 
GLY   CA  HA3  sing N N 190 
GLY   C   O    doub N N 191 
GLY   C   OXT  sing N N 192 
GLY   OXT HXT  sing N N 193 
HIS   N   CA   sing N N 194 
HIS   N   H    sing N N 195 
HIS   N   H2   sing N N 196 
HIS   CA  C    sing N N 197 
HIS   CA  CB   sing N N 198 
HIS   CA  HA   sing N N 199 
HIS   C   O    doub N N 200 
HIS   C   OXT  sing N N 201 
HIS   CB  CG   sing N N 202 
HIS   CB  HB2  sing N N 203 
HIS   CB  HB3  sing N N 204 
HIS   CG  ND1  sing Y N 205 
HIS   CG  CD2  doub Y N 206 
HIS   ND1 CE1  doub Y N 207 
HIS   ND1 HD1  sing N N 208 
HIS   CD2 NE2  sing Y N 209 
HIS   CD2 HD2  sing N N 210 
HIS   CE1 NE2  sing Y N 211 
HIS   CE1 HE1  sing N N 212 
HIS   NE2 HE2  sing N N 213 
HIS   OXT HXT  sing N N 214 
HOH   O   H1   sing N N 215 
HOH   O   H2   sing N N 216 
ILE   N   CA   sing N N 217 
ILE   N   H    sing N N 218 
ILE   N   H2   sing N N 219 
ILE   CA  C    sing N N 220 
ILE   CA  CB   sing N N 221 
ILE   CA  HA   sing N N 222 
ILE   C   O    doub N N 223 
ILE   C   OXT  sing N N 224 
ILE   CB  CG1  sing N N 225 
ILE   CB  CG2  sing N N 226 
ILE   CB  HB   sing N N 227 
ILE   CG1 CD1  sing N N 228 
ILE   CG1 HG12 sing N N 229 
ILE   CG1 HG13 sing N N 230 
ILE   CG2 HG21 sing N N 231 
ILE   CG2 HG22 sing N N 232 
ILE   CG2 HG23 sing N N 233 
ILE   CD1 HD11 sing N N 234 
ILE   CD1 HD12 sing N N 235 
ILE   CD1 HD13 sing N N 236 
ILE   OXT HXT  sing N N 237 
LEU   N   CA   sing N N 238 
LEU   N   H    sing N N 239 
LEU   N   H2   sing N N 240 
LEU   CA  C    sing N N 241 
LEU   CA  CB   sing N N 242 
LEU   CA  HA   sing N N 243 
LEU   C   O    doub N N 244 
LEU   C   OXT  sing N N 245 
LEU   CB  CG   sing N N 246 
LEU   CB  HB2  sing N N 247 
LEU   CB  HB3  sing N N 248 
LEU   CG  CD1  sing N N 249 
LEU   CG  CD2  sing N N 250 
LEU   CG  HG   sing N N 251 
LEU   CD1 HD11 sing N N 252 
LEU   CD1 HD12 sing N N 253 
LEU   CD1 HD13 sing N N 254 
LEU   CD2 HD21 sing N N 255 
LEU   CD2 HD22 sing N N 256 
LEU   CD2 HD23 sing N N 257 
LEU   OXT HXT  sing N N 258 
LYS   N   CA   sing N N 259 
LYS   N   H    sing N N 260 
LYS   N   H2   sing N N 261 
LYS   CA  C    sing N N 262 
LYS   CA  CB   sing N N 263 
LYS   CA  HA   sing N N 264 
LYS   C   O    doub N N 265 
LYS   C   OXT  sing N N 266 
LYS   CB  CG   sing N N 267 
LYS   CB  HB2  sing N N 268 
LYS   CB  HB3  sing N N 269 
LYS   CG  CD   sing N N 270 
LYS   CG  HG2  sing N N 271 
LYS   CG  HG3  sing N N 272 
LYS   CD  CE   sing N N 273 
LYS   CD  HD2  sing N N 274 
LYS   CD  HD3  sing N N 275 
LYS   CE  NZ   sing N N 276 
LYS   CE  HE2  sing N N 277 
LYS   CE  HE3  sing N N 278 
LYS   NZ  HZ1  sing N N 279 
LYS   NZ  HZ2  sing N N 280 
LYS   NZ  HZ3  sing N N 281 
LYS   OXT HXT  sing N N 282 
MET   N   CA   sing N N 283 
MET   N   H    sing N N 284 
MET   N   H2   sing N N 285 
MET   CA  C    sing N N 286 
MET   CA  CB   sing N N 287 
MET   CA  HA   sing N N 288 
MET   C   O    doub N N 289 
MET   C   OXT  sing N N 290 
MET   CB  CG   sing N N 291 
MET   CB  HB2  sing N N 292 
MET   CB  HB3  sing N N 293 
MET   CG  SD   sing N N 294 
MET   CG  HG2  sing N N 295 
MET   CG  HG3  sing N N 296 
MET   SD  CE   sing N N 297 
MET   CE  HE1  sing N N 298 
MET   CE  HE2  sing N N 299 
MET   CE  HE3  sing N N 300 
MET   OXT HXT  sing N N 301 
PHE   N   CA   sing N N 302 
PHE   N   H    sing N N 303 
PHE   N   H2   sing N N 304 
PHE   CA  C    sing N N 305 
PHE   CA  CB   sing N N 306 
PHE   CA  HA   sing N N 307 
PHE   C   O    doub N N 308 
PHE   C   OXT  sing N N 309 
PHE   CB  CG   sing N N 310 
PHE   CB  HB2  sing N N 311 
PHE   CB  HB3  sing N N 312 
PHE   CG  CD1  doub Y N 313 
PHE   CG  CD2  sing Y N 314 
PHE   CD1 CE1  sing Y N 315 
PHE   CD1 HD1  sing N N 316 
PHE   CD2 CE2  doub Y N 317 
PHE   CD2 HD2  sing N N 318 
PHE   CE1 CZ   doub Y N 319 
PHE   CE1 HE1  sing N N 320 
PHE   CE2 CZ   sing Y N 321 
PHE   CE2 HE2  sing N N 322 
PHE   CZ  HZ   sing N N 323 
PHE   OXT HXT  sing N N 324 
PRO   N   CA   sing N N 325 
PRO   N   CD   sing N N 326 
PRO   N   H    sing N N 327 
PRO   CA  C    sing N N 328 
PRO   CA  CB   sing N N 329 
PRO   CA  HA   sing N N 330 
PRO   C   O    doub N N 331 
PRO   C   OXT  sing N N 332 
PRO   CB  CG   sing N N 333 
PRO   CB  HB2  sing N N 334 
PRO   CB  HB3  sing N N 335 
PRO   CG  CD   sing N N 336 
PRO   CG  HG2  sing N N 337 
PRO   CG  HG3  sing N N 338 
PRO   CD  HD2  sing N N 339 
PRO   CD  HD3  sing N N 340 
PRO   OXT HXT  sing N N 341 
SER   N   CA   sing N N 342 
SER   N   H    sing N N 343 
SER   N   H2   sing N N 344 
SER   CA  C    sing N N 345 
SER   CA  CB   sing N N 346 
SER   CA  HA   sing N N 347 
SER   C   O    doub N N 348 
SER   C   OXT  sing N N 349 
SER   CB  OG   sing N N 350 
SER   CB  HB2  sing N N 351 
SER   CB  HB3  sing N N 352 
SER   OG  HG   sing N N 353 
SER   OXT HXT  sing N N 354 
THR   N   CA   sing N N 355 
THR   N   H    sing N N 356 
THR   N   H2   sing N N 357 
THR   CA  C    sing N N 358 
THR   CA  CB   sing N N 359 
THR   CA  HA   sing N N 360 
THR   C   O    doub N N 361 
THR   C   OXT  sing N N 362 
THR   CB  OG1  sing N N 363 
THR   CB  CG2  sing N N 364 
THR   CB  HB   sing N N 365 
THR   OG1 HG1  sing N N 366 
THR   CG2 HG21 sing N N 367 
THR   CG2 HG22 sing N N 368 
THR   CG2 HG23 sing N N 369 
THR   OXT HXT  sing N N 370 
TRP   N   CA   sing N N 371 
TRP   N   H    sing N N 372 
TRP   N   H2   sing N N 373 
TRP   CA  C    sing N N 374 
TRP   CA  CB   sing N N 375 
TRP   CA  HA   sing N N 376 
TRP   C   O    doub N N 377 
TRP   C   OXT  sing N N 378 
TRP   CB  CG   sing N N 379 
TRP   CB  HB2  sing N N 380 
TRP   CB  HB3  sing N N 381 
TRP   CG  CD1  doub Y N 382 
TRP   CG  CD2  sing Y N 383 
TRP   CD1 NE1  sing Y N 384 
TRP   CD1 HD1  sing N N 385 
TRP   CD2 CE2  doub Y N 386 
TRP   CD2 CE3  sing Y N 387 
TRP   NE1 CE2  sing Y N 388 
TRP   NE1 HE1  sing N N 389 
TRP   CE2 CZ2  sing Y N 390 
TRP   CE3 CZ3  doub Y N 391 
TRP   CE3 HE3  sing N N 392 
TRP   CZ2 CH2  doub Y N 393 
TRP   CZ2 HZ2  sing N N 394 
TRP   CZ3 CH2  sing Y N 395 
TRP   CZ3 HZ3  sing N N 396 
TRP   CH2 HH2  sing N N 397 
TRP   OXT HXT  sing N N 398 
TYR   N   CA   sing N N 399 
TYR   N   H    sing N N 400 
TYR   N   H2   sing N N 401 
TYR   CA  C    sing N N 402 
TYR   CA  CB   sing N N 403 
TYR   CA  HA   sing N N 404 
TYR   C   O    doub N N 405 
TYR   C   OXT  sing N N 406 
TYR   CB  CG   sing N N 407 
TYR   CB  HB2  sing N N 408 
TYR   CB  HB3  sing N N 409 
TYR   CG  CD1  doub Y N 410 
TYR   CG  CD2  sing Y N 411 
TYR   CD1 CE1  sing Y N 412 
TYR   CD1 HD1  sing N N 413 
TYR   CD2 CE2  doub Y N 414 
TYR   CD2 HD2  sing N N 415 
TYR   CE1 CZ   doub Y N 416 
TYR   CE1 HE1  sing N N 417 
TYR   CE2 CZ   sing Y N 418 
TYR   CE2 HE2  sing N N 419 
TYR   CZ  OH   sing N N 420 
TYR   OH  HH   sing N N 421 
TYR   OXT HXT  sing N N 422 
VAL   N   CA   sing N N 423 
VAL   N   H    sing N N 424 
VAL   N   H2   sing N N 425 
VAL   CA  C    sing N N 426 
VAL   CA  CB   sing N N 427 
VAL   CA  HA   sing N N 428 
VAL   C   O    doub N N 429 
VAL   C   OXT  sing N N 430 
VAL   CB  CG1  sing N N 431 
VAL   CB  CG2  sing N N 432 
VAL   CB  HB   sing N N 433 
VAL   CG1 HG11 sing N N 434 
VAL   CG1 HG12 sing N N 435 
VAL   CG1 HG13 sing N N 436 
VAL   CG2 HG21 sing N N 437 
VAL   CG2 HG22 sing N N 438 
VAL   CG2 HG23 sing N N 439 
VAL   OXT HXT  sing N N 440 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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   6XHM 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9DU3 
_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]   0.008776 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001964 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018643 
_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]   0.022551 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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 2   ? -3.08229 -3.51199  -16.82688 1.000 55.96331 ? 1   SER   A N   1 
ATOM   2    C CA  . SER   A 1 2   ? -2.16121 -2.57751  -16.19455 1.000 55.03675 ? 1   SER   A CA  1 
ATOM   3    C C   . SER   A 1 2   ? -2.45830 -2.44693  -14.70497 1.000 52.00552 ? 1   SER   A C   1 
ATOM   4    O O   . SER   A 1 2   ? -3.16639 -3.27363  -14.12989 1.000 50.46632 ? 1   SER   A O   1 
ATOM   5    C CB  . SER   A 1 2   ? -2.23488 -1.20845  -16.86995 1.000 57.43703 ? 1   SER   A CB  1 
ATOM   6    O OG  . SER   A 1 2   ? -3.53255 -0.65318  -16.75856 1.000 57.67748 ? 1   SER   A OG  1 
ATOM   7    N N   . GLY   A 1 3   ? -1.91318 -1.41170  -14.08825 1.000 57.41228 ? 2   GLY   A N   1 
ATOM   8    C CA  . GLY   A 1 3   ? -2.05180 -1.21902  -12.65939 1.000 50.49313 ? 2   GLY   A CA  1 
ATOM   9    C C   . GLY   A 1 3   ? -0.82564 -1.69444  -11.90387 1.000 50.03297 ? 2   GLY   A C   1 
ATOM   10   O O   . GLY   A 1 3   ? -0.16877 -2.67376  -12.27530 1.000 51.96517 ? 2   GLY   A O   1 
ATOM   11   N N   . PHE   A 1 4   ? -0.50702 -0.99252  -10.81954 1.000 47.04808 ? 3   PHE   A N   1 
ATOM   12   C CA  . PHE   A 1 4   ? 0.68955  -1.27867  -10.03896 1.000 46.72201 ? 3   PHE   A CA  1 
ATOM   13   C C   . PHE   A 1 4   ? 0.31725  -1.34685  -8.56704  1.000 45.31163 ? 3   PHE   A C   1 
ATOM   14   O O   . PHE   A 1 4   ? -0.22729 -0.38414  -8.01754  1.000 45.81198 ? 3   PHE   A O   1 
ATOM   15   C CB  . PHE   A 1 4   ? 1.77124  -0.22377  -10.27779 1.000 46.80008 ? 3   PHE   A CB  1 
ATOM   16   C CG  . PHE   A 1 4   ? 3.15579  -0.71182  -9.98279  1.000 47.25614 ? 3   PHE   A CG  1 
ATOM   17   C CD1 . PHE   A 1 4   ? 3.76167  -1.64331  -10.80965 1.000 48.31501 ? 3   PHE   A CD1 1 
ATOM   18   C CD2 . PHE   A 1 4   ? 3.85030  -0.24934  -8.87898  1.000 45.33974 ? 3   PHE   A CD2 1 
ATOM   19   C CE1 . PHE   A 1 4   ? 5.03744  -2.10321  -10.54434 1.000 47.51255 ? 3   PHE   A CE1 1 
ATOM   20   C CE2 . PHE   A 1 4   ? 5.12745  -0.70296  -8.61017  1.000 47.52284 ? 3   PHE   A CE2 1 
ATOM   21   C CZ  . PHE   A 1 4   ? 5.72132  -1.63239  -9.44433  1.000 47.66867 ? 3   PHE   A CZ  1 
ATOM   22   N N   . ARG   A 1 5   ? 0.62605  -2.47673  -7.93255  1.000 45.53101 ? 4   ARG   A N   1 
ATOM   23   C CA  . ARG   A 1 5   ? 0.20591  -2.76758  -6.57153  1.000 43.68514 ? 4   ARG   A CA  1 
ATOM   24   C C   . ARG   A 1 5   ? 1.38604  -3.27012  -5.75281  1.000 43.46143 ? 4   ARG   A C   1 
ATOM   25   O O   . ARG   A 1 5   ? 2.31661  -3.87752  -6.28691  1.000 43.36456 ? 4   ARG   A O   1 
ATOM   26   C CB  . ARG   A 1 5   ? -0.90514 -3.82723  -6.55324  1.000 43.20713 ? 4   ARG   A CB  1 
ATOM   27   C CG  . ARG   A 1 5   ? -2.15718 -3.43961  -7.31474  1.000 43.79246 ? 4   ARG   A CG  1 
ATOM   28   C CD  . ARG   A 1 5   ? -2.87253 -2.31029  -6.60347  1.000 48.07074 ? 4   ARG   A CD  1 
ATOM   29   N NE  . ARG   A 1 5   ? -2.79919 -2.48459  -5.15878  1.000 47.83382 ? 4   ARG   A NE  1 
ATOM   30   C CZ  . ARG   A 1 5   ? -3.65826 -3.19728  -4.44445  1.000 47.10661 ? 4   ARG   A CZ  1 
ATOM   31   N NH1 . ARG   A 1 5   ? -4.70498 -3.78271  -5.00530  1.000 43.15117 ? 4   ARG   A NH1 1 
ATOM   32   N NH2 . ARG   A 1 5   ? -3.45907 -3.32989  -3.13521  1.000 46.17415 ? 4   ARG   A NH2 1 
ATOM   33   N N   . LYS   A 1 6   ? 1.33741  -3.01589  -4.44455  1.000 44.49762 ? 5   LYS   A N   1 
ATOM   34   C CA  . LYS   A 1 6   ? 2.26206  -3.65538  -3.51500  1.000 42.56089 ? 5   LYS   A CA  1 
ATOM   35   C C   . LYS   A 1 6   ? 1.89913  -5.13224  -3.42116  1.000 42.58007 ? 5   LYS   A C   1 
ATOM   36   O O   . LYS   A 1 6   ? 0.89745  -5.49722  -2.79764  1.000 40.81378 ? 5   LYS   A O   1 
ATOM   37   C CB  . LYS   A 1 6   ? 2.20527  -2.97736  -2.14783  1.000 43.72462 ? 5   LYS   A CB  1 
ATOM   38   C CG  . LYS   A 1 6   ? 3.56846  -2.61319  -1.57368  1.000 44.61467 ? 5   LYS   A CG  1 
ATOM   39   C CD  . LYS   A 1 6   ? 3.42980  -1.60976  -0.43580  1.000 50.22004 ? 5   LYS   A CD  1 
ATOM   40   C CE  . LYS   A 1 6   ? 4.74939  -0.90778  -0.12512  1.000 52.06274 ? 5   LYS   A CE  1 
ATOM   41   N NZ  . LYS   A 1 6   ? 5.60814  -1.66581  0.83365   1.000 54.57360 ? 5   LYS   A NZ  1 
ATOM   42   N N   . MET   A 1 7   ? 2.70325  -5.98082  -4.05120  1.000 41.68941 ? 6   MET   A N   1 
ATOM   43   C CA  . MET   A 1 7   ? 2.35995  -7.37616  -4.28383  1.000 40.17938 ? 6   MET   A CA  1 
ATOM   44   C C   . MET   A 1 7   ? 3.31326  -8.27557  -3.51002  1.000 39.49241 ? 6   MET   A C   1 
ATOM   45   O O   . MET   A 1 7   ? 4.53033  -8.06012  -3.53076  1.000 41.01984 ? 6   MET   A O   1 
ATOM   46   C CB  . MET   A 1 7   ? 2.42397  -7.68923  -5.78048  1.000 41.09743 ? 6   MET   A CB  1 
ATOM   47   C CG  . MET   A 1 7   ? 1.84526  -9.02577  -6.18599  1.000 41.14444 ? 6   MET   A CG  1 
ATOM   48   S SD  . MET   A 1 7   ? 1.77244  -9.18185  -7.98003  1.000 48.55826 ? 6   MET   A SD  1 
ATOM   49   C CE  . MET   A 1 7   ? 0.84652  -7.70676  -8.39876  1.000 39.71679 ? 6   MET   A CE  1 
ATOM   50   N N   . ALA   A 1 8   ? 2.76362  -9.28154  -2.83589  1.000 37.06497 ? 7   ALA   A N   1 
ATOM   51   C CA  . ALA   A 1 8   ? 3.55750  -10.24586 -2.09146  1.000 39.46968 ? 7   ALA   A CA  1 
ATOM   52   C C   . ALA   A 1 8   ? 3.58639  -11.58031 -2.82521  1.000 39.69693 ? 7   ALA   A C   1 
ATOM   53   O O   . ALA   A 1 8   ? 2.69709  -11.90198 -3.61713  1.000 39.29050 ? 7   ALA   A O   1 
ATOM   54   C CB  . ALA   A 1 8   ? 3.00881  -10.43852 -0.67254  1.000 39.27553 ? 7   ALA   A CB  1 
ATOM   55   N N   . PHE   A 1 9   ? 4.63204  -12.35554 -2.55146  1.000 41.74809 ? 8   PHE   A N   1 
ATOM   56   C CA  . PHE   A 1 9   ? 4.76262  -13.66985 -3.15318  1.000 40.59190 ? 8   PHE   A CA  1 
ATOM   57   C C   . PHE   A 1 9   ? 3.66463  -14.60362 -2.64818  1.000 40.08870 ? 8   PHE   A C   1 
ATOM   58   O O   . PHE   A 1 9   ? 3.18911  -14.46235 -1.51749  1.000 39.62311 ? 8   PHE   A O   1 
ATOM   59   C CB  . PHE   A 1 9   ? 6.12526  -14.27727 -2.83272  1.000 39.77581 ? 8   PHE   A CB  1 
ATOM   60   C CG  . PHE   A 1 9   ? 7.26475  -13.63143 -3.55759  1.000 43.05365 ? 8   PHE   A CG  1 
ATOM   61   C CD1 . PHE   A 1 9   ? 7.54755  -13.97097 -4.87030  1.000 44.61310 ? 8   PHE   A CD1 1 
ATOM   62   C CD2 . PHE   A 1 9   ? 8.06404  -12.69471 -2.92530  1.000 42.76785 ? 8   PHE   A CD2 1 
ATOM   63   C CE1 . PHE   A 1 9   ? 8.60352  -13.38249 -5.54391  1.000 45.38063 ? 8   PHE   A CE1 1 
ATOM   64   C CE2 . PHE   A 1 9   ? 9.12208  -12.10153 -3.59377  1.000 43.39462 ? 8   PHE   A CE2 1 
ATOM   65   C CZ  . PHE   A 1 9   ? 9.39177  -12.44738 -4.90600  1.000 44.69907 ? 8   PHE   A CZ  1 
ATOM   66   N N   . PRO   A 1 10  ? 3.24291  -15.56249 -3.47231  1.000 40.82516 ? 9   PRO   A N   1 
ATOM   67   C CA  . PRO   A 1 10  ? 2.36328  -16.62848 -2.97552  1.000 40.87100 ? 9   PRO   A CA  1 
ATOM   68   C C   . PRO   A 1 10  ? 3.03911  -17.36467 -1.82708  1.000 40.86415 ? 9   PRO   A C   1 
ATOM   69   O O   . PRO   A 1 10  ? 4.21657  -17.72263 -1.90643  1.000 40.71710 ? 9   PRO   A O   1 
ATOM   70   C CB  . PRO   A 1 10  ? 2.16905  -17.52849 -4.20193  1.000 40.74365 ? 9   PRO   A CB  1 
ATOM   71   C CG  . PRO   A 1 10  ? 2.49101  -16.65186 -5.38165  1.000 41.67996 ? 9   PRO   A CG  1 
ATOM   72   C CD  . PRO   A 1 10  ? 3.56417  -15.72424 -4.90038  1.000 40.75031 ? 9   PRO   A CD  1 
ATOM   73   N N   . SER   A 1 11  ? 2.28597  -17.58724 -0.75126  1.000 40.56197 ? 10  SER   A N   1 
ATOM   74   C CA  . SER   A 1 11  ? 2.86367  -17.97616 0.52815   1.000 39.45011 ? 10  SER   A CA  1 
ATOM   75   C C   . SER   A 1 11  ? 2.66011  -19.44737 0.87756   1.000 40.36925 ? 10  SER   A C   1 
ATOM   76   O O   . SER   A 1 11  ? 3.02607  -19.85754 1.98312   1.000 39.32830 ? 10  SER   A O   1 
ATOM   77   C CB  . SER   A 1 11  ? 2.29138  -17.09615 1.64227   1.000 39.75350 ? 10  SER   A CB  1 
ATOM   78   O OG  . SER   A 1 11  ? 0.87706  -17.19150 1.69649   1.000 39.03156 ? 10  SER   A OG  1 
ATOM   79   N N   . GLY   A 1 12  ? 2.10712  -20.25290 -0.03329  1.000 40.42473 ? 11  GLY   A N   1 
ATOM   80   C CA  . GLY   A 1 12  ? 1.79546  -21.63595 0.30970   1.000 39.96336 ? 11  GLY   A CA  1 
ATOM   81   C C   . GLY   A 1 12  ? 3.01460  -22.44491 0.71525   1.000 40.55402 ? 11  GLY   A C   1 
ATOM   82   O O   . GLY   A 1 12  ? 2.97479  -23.20368 1.69297   1.000 40.57655 ? 11  GLY   A O   1 
ATOM   83   N N   . LYS   A 1 13  ? 4.11666  -22.29041 -0.02572  1.000 38.65610 ? 12  LYS   A N   1 
ATOM   84   C CA  . LYS   A 1 13  ? 5.33267  -23.03308 0.28617   1.000 40.76354 ? 12  LYS   A CA  1 
ATOM   85   C C   . LYS   A 1 13  ? 5.84957  -22.70653 1.68033   1.000 41.22979 ? 12  LYS   A C   1 
ATOM   86   O O   . LYS   A 1 13  ? 6.43594  -23.57150 2.34004   1.000 41.14685 ? 12  LYS   A O   1 
ATOM   87   C CB  . LYS   A 1 13  ? 6.41737  -22.74276 -0.75383  1.000 41.95284 ? 12  LYS   A CB  1 
ATOM   88   C CG  . LYS   A 1 13  ? 6.10114  -23.24873 -2.15383  1.000 43.71999 ? 12  LYS   A CG  1 
ATOM   89   C CD  . LYS   A 1 13  ? 7.32191  -23.15508 -3.05924  1.000 48.55582 ? 12  LYS   A CD  1 
ATOM   90   C CE  . LYS   A 1 13  ? 7.01855  -23.65596 -4.46266  1.000 52.65802 ? 12  LYS   A CE  1 
ATOM   91   N NZ  . LYS   A 1 13  ? 6.03125  -22.78647 -5.15538  1.000 51.31892 ? 12  LYS   A NZ  1 
ATOM   92   N N   . VAL   A 1 14  ? 5.64627  -21.47171 2.14352   1.000 39.90361 ? 13  VAL   A N   1 
ATOM   93   C CA  . VAL   A 1 14  ? 6.09109  -21.09458 3.48104   1.000 39.09997 ? 13  VAL   A CA  1 
ATOM   94   C C   . VAL   A 1 14  ? 5.04916  -21.47899 4.52376   1.000 39.39329 ? 13  VAL   A C   1 
ATOM   95   O O   . VAL   A 1 14  ? 5.39538  -21.86245 5.64722   1.000 39.34571 ? 13  VAL   A O   1 
ATOM   96   C CB  . VAL   A 1 14  ? 6.41107  -19.59140 3.52754   1.000 38.28926 ? 13  VAL   A CB  1 
ATOM   97   C CG1 . VAL   A 1 14  ? 6.97893  -19.21220 4.88429   1.000 38.40712 ? 13  VAL   A CG1 1 
ATOM   98   C CG2 . VAL   A 1 14  ? 7.38233  -19.22533 2.41516   1.000 37.96784 ? 13  VAL   A CG2 1 
ATOM   99   N N   . GLU   A 1 15  ? 3.76005  -21.37364 4.17723   1.000 38.48350 ? 14  GLU   A N   1 
ATOM   100  C CA  . GLU   A 1 15  ? 2.71025  -21.86612 5.06469   1.000 40.58532 ? 14  GLU   A CA  1 
ATOM   101  C C   . GLU   A 1 15  ? 2.96575  -23.31269 5.45763   1.000 41.02128 ? 14  GLU   A C   1 
ATOM   102  O O   . GLU   A 1 15  ? 2.77461  -23.69448 6.61903   1.000 40.87295 ? 14  GLU   A O   1 
ATOM   103  C CB  . GLU   A 1 15  ? 1.34296  -21.73559 4.39256   1.000 38.44024 ? 14  GLU   A CB  1 
ATOM   104  C CG  . GLU   A 1 15  ? 0.88626  -20.30739 4.17201   1.000 38.82650 ? 14  GLU   A CG  1 
ATOM   105  C CD  . GLU   A 1 15  ? -0.33765 -20.22451 3.28768   1.000 42.05152 ? 14  GLU   A CD  1 
ATOM   106  O OE1 . GLU   A 1 15  ? -1.28328 -21.01012 3.50629   1.000 41.23266 ? 14  GLU   A OE1 1 
ATOM   107  O OE2 . GLU   A 1 15  ? -0.34886 -19.38228 2.36445   1.000 42.28186 ? 14  GLU   A OE2 1 
ATOM   108  N N   . GLY   A 1 16  ? 3.42289  -24.12753 4.50757   1.000 39.59562 ? 15  GLY   A N   1 
ATOM   109  C CA  . GLY   A 1 16  ? 3.74379  -25.51096 4.81244   1.000 40.91972 ? 15  GLY   A CA  1 
ATOM   110  C C   . GLY   A 1 16  ? 4.88201  -25.71338 5.80320   1.000 41.72192 ? 15  GLY   A C   1 
ATOM   111  O O   . GLY   A 1 16  ? 5.16976  -26.85182 6.18803   1.000 41.51495 ? 15  GLY   A O   1 
ATOM   112  N N   . CYS   A 1 17  ? 5.53146  -24.62851 6.23527   1.000 39.45220 ? 16  CYS   A N   1 
ATOM   113  C CA  . CYS   A 1 17  ? 6.70608  -24.72312 7.08999   1.000 40.19819 ? 16  CYS   A CA  1 
ATOM   114  C C   . CYS   A 1 17  ? 6.56013  -24.03983 8.44463   1.000 39.23450 ? 16  CYS   A C   1 
ATOM   115  O O   . CYS   A 1 17  ? 7.53757  -24.00009 9.20171   1.000 39.87415 ? 16  CYS   A O   1 
ATOM   116  C CB  . CYS   A 1 17  ? 7.92992  -24.13418 6.37500   1.000 39.88611 ? 16  CYS   A CB  1 
ATOM   117  S SG  . CYS   A 1 17  ? 8.33098  -24.91824 4.80419   1.000 43.91860 ? 16  CYS   A SG  1 
ATOM   118  N N   . MET   A 1 18  ? 5.39161  -23.49990 8.77947   1.000 38.70098 ? 17  MET   A N   1 
ATOM   119  C CA  . MET   A 1 18  ? 5.22400  -22.78223 10.03596  1.000 39.08231 ? 17  MET   A CA  1 
ATOM   120  C C   . MET   A 1 18  ? 4.69798  -23.71975 11.11440  1.000 42.39256 ? 17  MET   A C   1 
ATOM   121  O O   . MET   A 1 18  ? 3.68061  -24.39353 10.92192  1.000 42.71946 ? 17  MET   A O   1 
ATOM   122  C CB  . MET   A 1 18  ? 4.28501  -21.58849 9.86457   1.000 40.81233 ? 17  MET   A CB  1 
ATOM   123  C CG  . MET   A 1 18  ? 4.76502  -20.57521 8.84103   1.000 40.13083 ? 17  MET   A CG  1 
ATOM   124  S SD  . MET   A 1 18  ? 6.54161  -20.27104 8.92193   1.000 39.26457 ? 17  MET   A SD  1 
ATOM   125  C CE  . MET   A 1 18  ? 6.69943  -19.41939 10.48470  1.000 39.04234 ? 17  MET   A CE  1 
ATOM   126  N N   . VAL   A 1 19  ? 5.39789  -23.75690 12.24921  1.000 42.95223 ? 18  VAL   A N   1 
ATOM   127  C CA  . VAL   A 1 19  ? 5.01899  -24.56734 13.39738  1.000 43.17049 ? 18  VAL   A CA  1 
ATOM   128  C C   . VAL   A 1 19  ? 4.97974  -23.67131 14.62905  1.000 43.16367 ? 18  VAL   A C   1 
ATOM   129  O O   . VAL   A 1 19  ? 5.39554  -22.51364 14.60004  1.000 41.70613 ? 18  VAL   A O   1 
ATOM   130  C CB  . VAL   A 1 19  ? 5.98102  -25.75189 13.62690  1.000 42.99904 ? 18  VAL   A CB  1 
ATOM   131  C CG1 . VAL   A 1 19  ? 6.04678  -26.63586 12.39153  1.000 43.01214 ? 18  VAL   A CG1 1 
ATOM   132  C CG2 . VAL   A 1 19  ? 7.36283  -25.24413 14.00317  1.000 40.58842 ? 18  VAL   A CG2 1 
ATOM   133  N N   . GLN   A 1 20  ? 4.48828  -24.23487 15.72589  1.000 44.00667 ? 19  GLN   A N   1 
ATOM   134  C CA  . GLN   A 1 20  ? 4.36347  -23.53899 16.99615  1.000 45.83964 ? 19  GLN   A CA  1 
ATOM   135  C C   . GLN   A 1 20  ? 5.42520  -24.06187 17.95308  1.000 44.38063 ? 19  GLN   A C   1 
ATOM   136  O O   . GLN   A 1 20  ? 5.55254  -25.27742 18.13714  1.000 45.74492 ? 19  GLN   A O   1 
ATOM   137  C CB  . GLN   A 1 20  ? 2.96205  -23.74485 17.57430  1.000 45.88139 ? 19  GLN   A CB  1 
ATOM   138  C CG  . GLN   A 1 20  ? 2.79751  -23.32578 19.01385  1.000 46.95924 ? 19  GLN   A CG  1 
ATOM   139  C CD  . GLN   A 1 20  ? 1.43038  -23.68225 19.55371  1.000 47.35439 ? 19  GLN   A CD  1 
ATOM   140  O OE1 . GLN   A 1 20  ? 0.41866  -23.13470 19.11800  1.000 49.87468 ? 19  GLN   A OE1 1 
ATOM   141  N NE2 . GLN   A 1 20  ? 1.39047  -24.61485 20.49883  1.000 51.05211 ? 19  GLN   A NE2 1 
ATOM   142  N N   . VAL   A 1 21  ? 6.19410  -23.15128 18.54459  1.000 42.40644 ? 20  VAL   A N   1 
ATOM   143  C CA  . VAL   A 1 21  ? 7.23479  -23.50013 19.50165  1.000 45.48404 ? 20  VAL   A CA  1 
ATOM   144  C C   . VAL   A 1 21  ? 6.87027  -22.87225 20.83733  1.000 45.83623 ? 20  VAL   A C   1 
ATOM   145  O O   . VAL   A 1 21  ? 6.70575  -21.64885 20.93346  1.000 45.54922 ? 20  VAL   A O   1 
ATOM   146  C CB  . VAL   A 1 21  ? 8.62296  -23.03247 19.04167  1.000 43.29684 ? 20  VAL   A CB  1 
ATOM   147  C CG1 . VAL   A 1 21  ? 9.69666  -23.57108 19.98007  1.000 44.71776 ? 20  VAL   A CG1 1 
ATOM   148  C CG2 . VAL   A 1 21  ? 8.88241  -23.46097 17.60277  1.000 42.10980 ? 20  VAL   A CG2 1 
ATOM   149  N N   . THR   A 1 22  ? 6.75207  -23.70481 21.86481  1.000 46.13264 ? 21  THR   A N   1 
ATOM   150  C CA  . THR   A 1 22  ? 6.44412  -23.25827 23.21303  1.000 49.82086 ? 21  THR   A CA  1 
ATOM   151  C C   . THR   A 1 22  ? 7.55898  -23.68917 24.15268  1.000 49.64870 ? 21  THR   A C   1 
ATOM   152  O O   . THR   A 1 22  ? 8.03206  -24.83023 24.09227  1.000 48.91533 ? 21  THR   A O   1 
ATOM   153  C CB  . THR   A 1 22  ? 5.10173  -23.82170 23.69768  1.000 48.91385 ? 21  THR   A CB  1 
ATOM   154  O OG1 . THR   A 1 22  ? 4.04904  -23.33250 22.85994  1.000 47.82889 ? 21  THR   A OG1 1 
ATOM   155  C CG2 . THR   A 1 22  ? 4.82549  -23.40453 25.13843  1.000 51.16659 ? 21  THR   A CG2 1 
ATOM   156  N N   . CYS   A 1 23  ? 7.98477  -22.75401 24.99922  1.000 50.58248 ? 22  CYS   A N   1 
ATOM   157  C CA  . CYS   A 1 23  ? 8.93624  -23.01912 26.06957  1.000 50.58240 ? 22  CYS   A CA  1 
ATOM   158  C C   . CYS   A 1 23  ? 8.46016  -22.26611 27.30129  1.000 52.84953 ? 22  CYS   A C   1 
ATOM   159  O O   . CYS   A 1 23  ? 8.31241  -21.03945 27.25934  1.000 53.68098 ? 22  CYS   A O   1 
ATOM   160  C CB  . CYS   A 1 23  ? 10.35257 -22.58817 25.67562  1.000 49.80747 ? 22  CYS   A CB  1 
ATOM   161  S SG  . CYS   A 1 23  ? 11.65855 -23.31198 26.69142  1.000 58.40627 ? 22  CYS   A SG  1 
ATOM   162  N N   . GLY   A 1 24  ? 8.20724  -22.99654 28.38249  1.000 55.13305 ? 23  GLY   A N   1 
ATOM   163  C CA  . GLY   A 1 24  ? 7.64053  -22.37956 29.57172  1.000 56.68961 ? 23  GLY   A CA  1 
ATOM   164  C C   . GLY   A 1 24  ? 6.30349  -21.74445 29.24552  1.000 57.63649 ? 23  GLY   A C   1 
ATOM   165  O O   . GLY   A 1 24  ? 5.39727  -22.38722 28.70119  1.000 56.61037 ? 23  GLY   A O   1 
ATOM   166  N N   . THR   A 1 25  ? 6.17245  -20.45740 29.56980  1.000 58.38263 ? 24  THR   A N   1 
ATOM   167  C CA  . THR   A 1 25  ? 4.97601  -19.70406 29.21750  1.000 60.98554 ? 24  THR   A CA  1 
ATOM   168  C C   . THR   A 1 25  ? 5.00893  -19.18413 27.78786  1.000 58.40997 ? 24  THR   A C   1 
ATOM   169  O O   . THR   A 1 25  ? 3.94599  -18.94455 27.20521  1.000 58.56290 ? 24  THR   A O   1 
ATOM   170  C CB  . THR   A 1 25  ? 4.79291  -18.52102 30.17110  1.000 64.22857 ? 24  THR   A CB  1 
ATOM   171  O OG1 . THR   A 1 25  ? 6.07227  -17.94126 30.46297  1.000 65.15415 ? 24  THR   A OG1 1 
ATOM   172  C CG2 . THR   A 1 25  ? 4.12613  -18.96276 31.46526  1.000 68.81522 ? 24  THR   A CG2 1 
ATOM   173  N N   . THR   A 1 26  ? 6.19413  -19.01372 27.21124  1.000 56.40775 ? 25  THR   A N   1 
ATOM   174  C CA  . THR   A 1 26  ? 6.32308  -18.34684 25.92337  1.000 55.45750 ? 25  THR   A CA  1 
ATOM   175  C C   . THR   A 1 26  ? 5.91751  -19.26903 24.77913  1.000 53.98239 ? 25  THR   A C   1 
ATOM   176  O O   . THR   A 1 26  ? 6.27037  -20.45045 24.75653  1.000 55.27489 ? 25  THR   A O   1 
ATOM   177  C CB  . THR   A 1 26  ? 7.76089  -17.86049 25.72556  1.000 54.11463 ? 25  THR   A CB  1 
ATOM   178  O OG1 . THR   A 1 26  ? 8.04178  -16.81191 26.66242  1.000 55.42126 ? 25  THR   A OG1 1 
ATOM   179  C CG2 . THR   A 1 26  ? 7.97352  -17.34214 24.30964  1.000 52.19468 ? 25  THR   A CG2 1 
ATOM   180  N N   . THR   A 1 27  ? 5.16024  -18.72011 23.83042  1.000 54.07022 ? 26  THR   A N   1 
ATOM   181  C CA  . THR   A 1 27  ? 4.81805  -19.40612 22.59167  1.000 49.72274 ? 26  THR   A CA  1 
ATOM   182  C C   . THR   A 1 27  ? 5.06333  -18.45764 21.43063  1.000 45.29170 ? 26  THR   A C   1 
ATOM   183  O O   . THR   A 1 27  ? 4.55130  -17.33365 21.42457  1.000 45.90244 ? 26  THR   A O   1 
ATOM   184  C CB  . THR   A 1 27  ? 3.35858  -19.87989 22.58154  1.000 47.80584 ? 26  THR   A CB  1 
ATOM   185  O OG1 . THR   A 1 27  ? 3.19631  -20.95162 23.51609  1.000 53.84851 ? 26  THR   A OG1 1 
ATOM   186  C CG2 . THR   A 1 27  ? 2.96554  -20.36963 21.19644  1.000 46.57454 ? 26  THR   A CG2 1 
ATOM   187  N N   . LEU   A 1 28  ? 5.85474  -18.90255 20.46015  1.000 45.55664 ? 27  LEU   A N   1 
ATOM   188  C CA  . LEU   A 1 28  ? 6.07146  -18.13631 19.24178  1.000 40.18633 ? 27  LEU   A CA  1 
ATOM   189  C C   . LEU   A 1 28  ? 6.09690  -19.10673 18.06548  1.000 41.05644 ? 27  LEU   A C   1 
ATOM   190  O O   . LEU   A 1 28  ? 5.77285  -20.29187 18.20041  1.000 40.44521 ? 27  LEU   A O   1 
ATOM   191  C CB  . LEU   A 1 28  ? 7.34335  -17.28266 19.34665  1.000 40.12871 ? 27  LEU   A CB  1 
ATOM   192  C CG  . LEU   A 1 28  ? 8.61336  -17.84647 19.98725  1.000 42.02485 ? 27  LEU   A CG  1 
ATOM   193  C CD1 . LEU   A 1 28  ? 9.19970  -18.99737 19.18088  1.000 40.78111 ? 27  LEU   A CD1 1 
ATOM   194  C CD2 . LEU   A 1 28  ? 9.64140  -16.73259 20.15921  1.000 40.09600 ? 27  LEU   A CD2 1 
ATOM   195  N N   . ASN   A 1 29  ? 6.48249  -18.59783 16.90117  1.000 37.13871 ? 28  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 29  ? 6.46135  -19.37135 15.67137  1.000 38.70197 ? 28  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 29  ? 7.84368  -19.93203 15.37046  1.000 38.91348 ? 28  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 29  ? 8.86461  -19.39176 15.80420  1.000 38.25807 ? 28  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 29  ? 5.98248  -18.51640 14.49596  1.000 36.68054 ? 28  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 29  ? 4.68647  -17.79249 14.79429  1.000 38.68810 ? 28  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 29  ? 3.60607  -18.37948 14.73806  1.000 41.62714 ? 28  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 29  ? 4.78780  -16.50800 15.11394  1.000 36.91774 ? 28  ASN   A ND2 1 
ATOM   203  N N   . GLY   A 1 30  ? 7.86018  -21.03382 14.62443  1.000 36.48150 ? 29  GLY   A N   1 
ATOM   204  C CA  . GLY   A 1 30  ? 9.09998  -21.62523 14.17383  1.000 37.44062 ? 29  GLY   A CA  1 
ATOM   205  C C   . GLY   A 1 30  ? 8.97602  -22.05997 12.72748  1.000 37.90166 ? 29  GLY   A C   1 
ATOM   206  O O   . GLY   A 1 30  ? 7.87807  -22.28122 12.21057  1.000 38.63715 ? 29  GLY   A O   1 
ATOM   207  N N   . LEU   A 1 31  ? 10.13007 -22.17853 12.08184  1.000 35.99040 ? 30  LEU   A N   1 
ATOM   208  C CA  . LEU   A 1 31  ? 10.22977 -22.55229 10.67654  1.000 36.89646 ? 30  LEU   A CA  1 
ATOM   209  C C   . LEU   A 1 31  ? 10.77700 -23.97098 10.58924  1.000 37.99654 ? 30  LEU   A C   1 
ATOM   210  O O   . LEU   A 1 31  ? 11.89925 -24.23236 11.03386  1.000 38.88852 ? 30  LEU   A O   1 
ATOM   211  C CB  . LEU   A 1 31  ? 11.12817 -21.57389 9.92154   1.000 36.29145 ? 30  LEU   A CB  1 
ATOM   212  C CG  . LEU   A 1 31  ? 11.27129 -21.78312 8.41506   1.000 37.63881 ? 30  LEU   A CG  1 
ATOM   213  C CD1 . LEU   A 1 31  ? 9.96780  -21.45626 7.70163   1.000 36.45863 ? 30  LEU   A CD1 1 
ATOM   214  C CD2 . LEU   A 1 31  ? 12.41734 -20.94603 7.87065   1.000 35.99458 ? 30  LEU   A CD2 1 
ATOM   215  N N   . TRP   A 1 32  ? 9.98507  -24.88017 10.02351  1.000 38.98226 ? 31  TRP   A N   1 
ATOM   216  C CA  . TRP   A 1 32  ? 10.30111 -26.30591 9.99909   1.000 39.22651 ? 31  TRP   A CA  1 
ATOM   217  C C   . TRP   A 1 32  ? 10.79649 -26.68418 8.60608   1.000 42.92274 ? 31  TRP   A C   1 
ATOM   218  O O   . TRP   A 1 32  ? 10.00272 -26.79804 7.66629   1.000 39.78717 ? 31  TRP   A O   1 
ATOM   219  C CB  . TRP   A 1 32  ? 9.07417  -27.12822 10.39081  1.000 39.67681 ? 31  TRP   A CB  1 
ATOM   220  C CG  . TRP   A 1 32  ? 9.30474  -28.61404 10.48050  1.000 42.47864 ? 31  TRP   A CG  1 
ATOM   221  C CD1 . TRP   A 1 32  ? 10.50352 -29.25748 10.59190  1.000 43.53382 ? 31  TRP   A CD1 1 
ATOM   222  C CD2 . TRP   A 1 32  ? 8.30092  -29.63908 10.46435  1.000 43.40773 ? 31  TRP   A CD2 1 
ATOM   223  N NE1 . TRP   A 1 32  ? 10.30810 -30.61705 10.64650  1.000 44.29277 ? 31  TRP   A NE1 1 
ATOM   224  C CE2 . TRP   A 1 32  ? 8.96531  -30.87682 10.57085  1.000 43.48460 ? 31  TRP   A CE2 1 
ATOM   225  C CE3 . TRP   A 1 32  ? 6.90547  -29.62897 10.36879  1.000 43.68479 ? 31  TRP   A CE3 1 
ATOM   226  C CZ2 . TRP   A 1 32  ? 8.28349  -32.09151 10.58660  1.000 46.45724 ? 31  TRP   A CZ2 1 
ATOM   227  C CZ3 . TRP   A 1 32  ? 6.23003  -30.83719 10.38393  1.000 44.09861 ? 31  TRP   A CZ3 1 
ATOM   228  C CH2 . TRP   A 1 32  ? 6.92006  -32.05119 10.49127  1.000 45.82337 ? 31  TRP   A CH2 1 
ATOM   229  N N   . LEU   A 1 33  ? 12.10653 -26.88660 8.47857   1.000 41.58702 ? 32  LEU   A N   1 
ATOM   230  C CA  . LEU   A 1 33  ? 12.72125 -27.31762 7.23025   1.000 42.16515 ? 32  LEU   A CA  1 
ATOM   231  C C   . LEU   A 1 33  ? 13.53391 -28.57376 7.50262   1.000 43.79697 ? 32  LEU   A C   1 
ATOM   232  O O   . LEU   A 1 33  ? 14.31935 -28.61225 8.45678   1.000 42.49566 ? 32  LEU   A O   1 
ATOM   233  C CB  . LEU   A 1 33  ? 13.60821 -26.21817 6.63466   1.000 41.68294 ? 32  LEU   A CB  1 
ATOM   234  C CG  . LEU   A 1 33  ? 12.90610 -24.92461 6.21080   1.000 40.68378 ? 32  LEU   A CG  1 
ATOM   235  C CD1 . LEU   A 1 33  ? 13.91992 -23.83059 5.93562   1.000 39.09005 ? 32  LEU   A CD1 1 
ATOM   236  C CD2 . LEU   A 1 33  ? 12.03005 -25.15261 4.98872   1.000 40.77672 ? 32  LEU   A CD2 1 
ATOM   237  N N   . ASP   A 1 34  ? 13.33834 -29.59565 6.66753   1.000 44.42366 ? 33  ASP   A N   1 
ATOM   238  C CA  . ASP   A 1 34  ? 13.94272 -30.92089 6.85446   1.000 44.77962 ? 33  ASP   A CA  1 
ATOM   239  C C   . ASP   A 1 34  ? 13.60360 -31.37145 8.27649   1.000 45.59062 ? 33  ASP   A C   1 
ATOM   240  O O   . ASP   A 1 34  ? 12.43542 -31.27820 8.67812   1.000 45.27840 ? 33  ASP   A O   1 
ATOM   241  C CB  . ASP   A 1 34  ? 15.42600 -30.85765 6.51253   1.000 46.31376 ? 33  ASP   A CB  1 
ATOM   242  C CG  . ASP   A 1 34  ? 15.67538 -30.40207 5.08559   1.000 48.66192 ? 33  ASP   A CG  1 
ATOM   243  O OD1 . ASP   A 1 34  ? 14.90732 -30.80564 4.18604   1.000 49.30233 ? 33  ASP   A OD1 1 
ATOM   244  O OD2 . ASP   A 1 34  ? 16.63616 -29.63457 4.86406   1.000 48.14764 ? 33  ASP   A OD2 1 
ATOM   245  N N   . ASP   A 1 35  ? 14.56818 -31.83974 9.06835   1.000 46.04596 ? 34  ASP   A N   1 
ATOM   246  C CA  . ASP   A 1 35  ? 14.31353 -32.23047 10.44902  1.000 45.50414 ? 34  ASP   A CA  1 
ATOM   247  C C   . ASP   A 1 35  ? 14.76313 -31.16530 11.44629  1.000 44.98232 ? 34  ASP   A C   1 
ATOM   248  O O   . ASP   A 1 35  ? 15.18410 -31.49720 12.55981  1.000 45.82311 ? 34  ASP   A O   1 
ATOM   249  C CB  . ASP   A 1 35  ? 14.98121 -33.57284 10.75441  1.000 45.97908 ? 34  ASP   A CB  1 
ATOM   250  C CG  . ASP   A 1 35  ? 16.49295 -33.53506 10.58475  1.000 48.85744 ? 34  ASP   A CG  1 
ATOM   251  O OD1 . ASP   A 1 35  ? 17.01265 -32.54496 10.02865  1.000 46.84188 ? 34  ASP   A OD1 1 
ATOM   252  O OD2 . ASP   A 1 35  ? 17.16397 -34.49847 11.01573  1.000 52.30980 ? 34  ASP   A OD2 1 
ATOM   253  N N   . VAL   A 1 36  ? 14.68067 -29.88732 11.07268  1.000 43.41002 ? 35  VAL   A N   1 
ATOM   254  C CA  . VAL   A 1 36  ? 15.13320 -28.79356 11.92484  1.000 42.55291 ? 35  VAL   A CA  1 
ATOM   255  C C   . VAL   A 1 36  ? 14.03020 -27.74824 12.03474  1.000 41.68035 ? 35  VAL   A C   1 
ATOM   256  O O   . VAL   A 1 36  ? 13.35977 -27.42523 11.04719  1.000 40.63046 ? 35  VAL   A O   1 
ATOM   257  C CB  . VAL   A 1 36  ? 16.43424 -28.15176 11.39318  1.000 41.41037 ? 35  VAL   A CB  1 
ATOM   258  C CG1 . VAL   A 1 36  ? 16.91816 -27.06646 12.34426  1.000 40.01737 ? 35  VAL   A CG1 1 
ATOM   259  C CG2 . VAL   A 1 36  ? 17.51491 -29.20809 11.19417  1.000 41.52463 ? 35  VAL   A CG2 1 
ATOM   260  N N   . VAL   A 1 37  ? 13.84047 -27.22426 13.24350  1.000 38.89319 ? 36  VAL   A N   1 
ATOM   261  C CA  . VAL   A 1 37  ? 12.92651 -26.11873 13.50675  1.000 37.72031 ? 36  VAL   A CA  1 
ATOM   262  C C   . VAL   A 1 37  ? 13.75701 -24.93985 13.99283  1.000 38.84364 ? 36  VAL   A C   1 
ATOM   263  O O   . VAL   A 1 37  ? 14.46920 -25.04913 14.99805  1.000 39.04893 ? 36  VAL   A O   1 
ATOM   264  C CB  . VAL   A 1 37  ? 11.85199 -26.49336 14.53952  1.000 37.82166 ? 36  VAL   A CB  1 
ATOM   265  C CG1 . VAL   A 1 37  ? 11.02491 -25.27227 14.90874  1.000 35.44987 ? 36  VAL   A CG1 1 
ATOM   266  C CG2 . VAL   A 1 37  ? 10.96256 -27.60207 14.00156  1.000 40.19177 ? 36  VAL   A CG2 1 
ATOM   267  N N   . TYR   A 1 38  ? 13.67467 -23.82340 13.27681  1.000 36.52207 ? 37  TYR   A N   1 
ATOM   268  C CA  . TYR   A 1 38  ? 14.38280 -22.59842 13.62678  1.000 35.18889 ? 37  TYR   A CA  1 
ATOM   269  C C   . TYR   A 1 38  ? 13.41078 -21.64256 14.30272  1.000 38.03367 ? 37  TYR   A C   1 
ATOM   270  O O   . TYR   A 1 38  ? 12.30075 -21.43718 13.80526  1.000 35.03272 ? 37  TYR   A O   1 
ATOM   271  C CB  . TYR   A 1 38  ? 14.98012 -21.93232 12.38477  1.000 35.61205 ? 37  TYR   A CB  1 
ATOM   272  C CG  . TYR   A 1 38  ? 15.83897 -22.83303 11.52538  1.000 37.53554 ? 37  TYR   A CG  1 
ATOM   273  C CD1 . TYR   A 1 38  ? 15.26589 -23.74805 10.64681  1.000 37.97510 ? 37  TYR   A CD1 1 
ATOM   274  C CD2 . TYR   A 1 38  ? 17.22363 -22.75255 11.57433  1.000 38.42389 ? 37  TYR   A CD2 1 
ATOM   275  C CE1 . TYR   A 1 38  ? 16.05098 -24.56883 9.85595   1.000 38.22709 ? 37  TYR   A CE1 1 
ATOM   276  C CE2 . TYR   A 1 38  ? 18.01464 -23.56370 10.78396  1.000 38.54770 ? 37  TYR   A CE2 1 
ATOM   277  C CZ  . TYR   A 1 38  ? 17.42667 -24.47001 9.92943   1.000 39.11776 ? 37  TYR   A CZ  1 
ATOM   278  O OH  . TYR   A 1 38  ? 18.21821 -25.27869 9.14589   1.000 41.24677 ? 37  TYR   A OH  1 
ATOM   279  N N   . CYS   A 1 39  ? 13.82233 -21.05513 15.42193  1.000 35.80311 ? 38  CYS   A N   1 
ATOM   280  C CA  . CYS   A 1 39  ? 12.95589 -20.10635 16.10838  1.000 35.14196 ? 38  CYS   A CA  1 
ATOM   281  C C   . CYS   A 1 39  ? 13.81688 -19.06805 16.80857  1.000 35.99552 ? 38  CYS   A C   1 
ATOM   282  O O   . CYS   A 1 39  ? 15.02721 -19.26075 16.96055  1.000 36.15320 ? 38  CYS   A O   1 
ATOM   283  C CB  . CYS   A 1 39  ? 12.02605 -20.81193 17.10770  1.000 36.96164 ? 38  CYS   A CB  1 
ATOM   284  S SG  . CYS   A 1 39  ? 12.82569 -21.50566 18.56325  1.000 44.63320 ? 38  CYS   A SG  1 
ATOM   285  N N   . PRO   A 1 40  ? 13.23626 -17.93458 17.20324  1.000 35.49543 ? 39  PRO   A N   1 
ATOM   286  C CA  . PRO   A 1 40  ? 13.99908 -16.96885 18.00325  1.000 37.42683 ? 39  PRO   A CA  1 
ATOM   287  C C   . PRO   A 1 40  ? 14.39299 -17.56868 19.34461  1.000 38.11282 ? 39  PRO   A C   1 
ATOM   288  O O   . PRO   A 1 40  ? 13.66312 -18.37131 19.93024  1.000 36.30872 ? 39  PRO   A O   1 
ATOM   289  C CB  . PRO   A 1 40  ? 13.02428 -15.79759 18.17662  1.000 37.44087 ? 39  PRO   A CB  1 
ATOM   290  C CG  . PRO   A 1 40  ? 12.08361 -15.91871 17.02363  1.000 36.44541 ? 39  PRO   A CG  1 
ATOM   291  C CD  . PRO   A 1 40  ? 11.93597 -17.38872 16.77409  1.000 35.56168 ? 39  PRO   A CD  1 
ATOM   292  N N   . ARG   A 1 41  ? 15.56750 -17.17169 19.83525  1.000 38.32410 ? 40  ARG   A N   1 
ATOM   293  C CA  . ARG   A 1 41  ? 16.06005 -17.76184 21.07492  1.000 39.02929 ? 40  ARG   A CA  1 
ATOM   294  C C   . ARG   A 1 41  ? 15.36165 -17.19631 22.30700  1.000 39.50159 ? 40  ARG   A C   1 
ATOM   295  O O   . ARG   A 1 41  ? 15.24360 -17.89926 23.31960  1.000 40.81188 ? 40  ARG   A O   1 
ATOM   296  C CB  . ARG   A 1 41  ? 17.57686 -17.58541 21.18346  1.000 37.96314 ? 40  ARG   A CB  1 
ATOM   297  C CG  . ARG   A 1 41  ? 18.07713 -16.16188 21.32205  1.000 36.51646 ? 40  ARG   A CG  1 
ATOM   298  C CD  . ARG   A 1 41  ? 19.58985 -16.17262 21.47043  1.000 36.90095 ? 40  ARG   A CD  1 
ATOM   299  N NE  . ARG   A 1 41  ? 20.15915 -14.83966 21.61996  1.000 38.15455 ? 40  ARG   A NE  1 
ATOM   300  C CZ  . ARG   A 1 41  ? 21.45129 -14.60025 21.79711  1.000 38.17073 ? 40  ARG   A CZ  1 
ATOM   301  N NH1 . ARG   A 1 41  ? 22.33360 -15.58431 21.85414  1.000 38.73200 ? 40  ARG   A NH1 1 
ATOM   302  N NH2 . ARG   A 1 41  ? 21.86728 -13.34361 21.92862  1.000 37.56095 ? 40  ARG   A NH2 1 
ATOM   303  N N   . HIS   A 1 42  ? 14.85350 -15.95537 22.23912  1.000 38.67469 ? 41  HIS   A N   1 
ATOM   304  C CA  . HIS   A 1 42  ? 14.17330 -15.43056 23.42642  1.000 41.39631 ? 41  HIS   A CA  1 
ATOM   305  C C   . HIS   A 1 42  ? 12.88473 -16.18854 23.75851  1.000 42.67351 ? 41  HIS   A C   1 
ATOM   306  O O   . HIS   A 1 42  ? 12.17908 -15.78023 24.68844  1.000 44.02872 ? 41  HIS   A O   1 
ATOM   307  C CB  . HIS   A 1 42  ? 13.89078 -13.93198 23.27910  1.000 40.45691 ? 41  HIS   A CB  1 
ATOM   308  C CG  . HIS   A 1 42  ? 12.87725 -13.59369 22.23029  1.000 40.14922 ? 41  HIS   A CG  1 
ATOM   309  N ND1 . HIS   A 1 42  ? 13.22512 -13.20541 20.95398  1.000 38.91993 ? 41  HIS   A ND1 1 
ATOM   310  C CD2 . HIS   A 1 42  ? 11.52547 -13.55083 22.27835  1.000 39.09525 ? 41  HIS   A CD2 1 
ATOM   311  C CE1 . HIS   A 1 42  ? 12.13191 -12.95600 20.25457  1.000 39.56411 ? 41  HIS   A CE1 1 
ATOM   312  N NE2 . HIS   A 1 42  ? 11.08653 -13.15867 21.03557  1.000 39.34369 ? 41  HIS   A NE2 1 
ATOM   313  N N   . VAL   A 1 43  ? 12.57377 -17.27097 23.03860  1.000 42.75653 ? 42  VAL   A N   1 
ATOM   314  C CA  . VAL   A 1 43  ? 11.51784 -18.18052 23.46055  1.000 44.31402 ? 42  VAL   A CA  1 
ATOM   315  C C   . VAL   A 1 43  ? 11.85566 -18.81693 24.80214  1.000 45.57496 ? 42  VAL   A C   1 
ATOM   316  O O   . VAL   A 1 43  ? 10.95276 -19.25710 25.52356  1.000 47.93075 ? 42  VAL   A O   1 
ATOM   317  C CB  . VAL   A 1 43  ? 11.27218 -19.25748 22.37670  1.000 42.01343 ? 42  VAL   A CB  1 
ATOM   318  C CG1 . VAL   A 1 43  ? 12.46771 -20.19101 22.25673  1.000 41.28131 ? 42  VAL   A CG1 1 
ATOM   319  C CG2 . VAL   A 1 43  ? 10.00125 -20.04394 22.66851  1.000 45.15183 ? 42  VAL   A CG2 1 
ATOM   320  N N   . ILE   A 1 44  ? 13.14382 -18.86293 25.16975  1.000 46.29791 ? 43  ILE   A N   1 
ATOM   321  C CA  . ILE   A 1 44  ? 13.54051 -19.45542 26.44420  1.000 45.78501 ? 43  ILE   A CA  1 
ATOM   322  C C   . ILE   A 1 44  ? 13.53687 -18.44956 27.58508  1.000 46.91809 ? 43  ILE   A C   1 
ATOM   323  O O   . ILE   A 1 44  ? 13.86241 -18.81587 28.72265  1.000 51.12621 ? 43  ILE   A O   1 
ATOM   324  C CB  . ILE   A 1 44  ? 14.93744 -20.10407 26.35655  1.000 47.06081 ? 43  ILE   A CB  1 
ATOM   325  C CG1 . ILE   A 1 44  ? 16.02748 -19.03081 26.32883  1.000 46.52033 ? 43  ILE   A CG1 1 
ATOM   326  C CG2 . ILE   A 1 44  ? 15.03257 -21.00152 25.13378  1.000 46.33208 ? 43  ILE   A CG2 1 
ATOM   327  C CD1 . ILE   A 1 44  ? 17.43211 -19.58899 26.29464  1.000 45.48944 ? 43  ILE   A CD1 1 
ATOM   328  N N   . CYS   A 1 45  ? 13.17772 -17.19835 27.32548  1.000 47.85524 ? 44  CYS   A N   1 
ATOM   329  C CA  . CYS   A 1 45  ? 13.20401 -16.16748 28.35104  1.000 52.33436 ? 44  CYS   A CA  1 
ATOM   330  C C   . CYS   A 1 45  ? 11.85059 -16.03662 29.03686  1.000 56.52637 ? 44  CYS   A C   1 
ATOM   331  O O   . CYS   A 1 45  ? 10.79972 -16.28457 28.43942  1.000 56.50996 ? 44  CYS   A O   1 
ATOM   332  C CB  . CYS   A 1 45  ? 13.59778 -14.81736 27.75069  1.000 52.98327 ? 44  CYS   A CB  1 
ATOM   333  S SG  . CYS   A 1 45  ? 15.27590 -14.73885 27.11250  1.000 45.85874 ? 44  CYS   A SG  1 
ATOM   334  N N   . THR   A 1 46  ? 11.88934 -15.64518 30.30552  1.000 60.99943 ? 45  THR   A N   1 
ATOM   335  C CA  . THR   A 1 46  ? 10.69831 -15.18556 30.99759  1.000 65.26379 ? 45  THR   A CA  1 
ATOM   336  C C   . THR   A 1 46  ? 10.59449 -13.67013 30.86921  1.000 70.55341 ? 45  THR   A C   1 
ATOM   337  O O   . THR   A 1 46  ? 11.49428 -13.00378 30.35434  1.000 69.03586 ? 45  THR   A O   1 
ATOM   338  C CB  . THR   A 1 46  ? 10.72667 -15.59658 32.46985  1.000 66.96489 ? 45  THR   A CB  1 
ATOM   339  O OG1 . THR   A 1 46  ? 11.79616 -14.91369 33.13775  1.000 69.71409 ? 45  THR   A OG1 1 
ATOM   340  C CG2 . THR   A 1 46  ? 10.92969 -17.09751 32.59853  1.000 62.81615 ? 45  THR   A CG2 1 
ATOM   341  N N   . SER   A 1 47  ? 9.47367  -13.12387 31.34604  1.000 78.14054 ? 46  SER   A N   1 
ATOM   342  C CA  . SER   A 1 47  ? 9.30706  -11.67432 31.34989  1.000 77.90318 ? 46  SER   A CA  1 
ATOM   343  C C   . SER   A 1 47  ? 10.41281 -10.97784 32.13360  1.000 80.89953 ? 46  SER   A C   1 
ATOM   344  O O   . SER   A 1 47  ? 10.70647 -9.80575  31.87372  1.000 82.26381 ? 46  SER   A O   1 
ATOM   345  C CB  . SER   A 1 47  ? 7.93958  -11.30563 31.92737  1.000 83.54616 ? 46  SER   A CB  1 
ATOM   346  O OG  . SER   A 1 47  ? 7.76777  -9.90116  31.97126  1.000 92.17125 ? 46  SER   A OG  1 
ATOM   347  N N   . GLU   A 1 48  ? 11.03910 -11.68476 33.07447  1.000 75.55630 ? 47  GLU   A N   1 
ATOM   348  C CA  . GLU   A 1 48  ? 12.11586 -11.12397 33.88084  1.000 77.40631 ? 47  GLU   A CA  1 
ATOM   349  C C   . GLU   A 1 48  ? 13.45457 -11.17117 33.15083  1.000 74.60917 ? 47  GLU   A C   1 
ATOM   350  O O   . GLU   A 1 48  ? 14.25588 -10.23625 33.25916  1.000 72.86641 ? 47  GLU   A O   1 
ATOM   351  C CB  . GLU   A 1 48  ? 12.19202 -11.87958 35.20850  1.000 79.43779 ? 47  GLU   A CB  1 
ATOM   352  C CG  . GLU   A 1 48  ? 13.55705 -11.90638 35.86577  1.000 84.86297 ? 47  GLU   A CG  1 
ATOM   353  C CD  . GLU   A 1 48  ? 13.63668 -12.93855 36.97625  1.000 89.94177 ? 47  GLU   A CD  1 
ATOM   354  O OE1 . GLU   A 1 48  ? 12.93767 -13.96972 36.87985  1.000 95.86192 ? 47  GLU   A OE1 1 
ATOM   355  O OE2 . GLU   A 1 48  ? 14.39090 -12.71818 37.94713  1.000 90.97421 ? 47  GLU   A OE2 1 
ATOM   356  N N   . ASP   A 1 49  ? 13.71072 -12.24443 32.39778  1.000 72.74085 ? 48  ASP   A N   1 
ATOM   357  C CA  . ASP   A 1 49  ? 14.99100 -12.39781 31.71419  1.000 69.67977 ? 48  ASP   A CA  1 
ATOM   358  C C   . ASP   A 1 49  ? 15.16644 -11.42004 30.55895  1.000 68.04270 ? 48  ASP   A C   1 
ATOM   359  O O   . ASP   A 1 49  ? 16.30056 -11.20160 30.12017  1.000 68.46860 ? 48  ASP   A O   1 
ATOM   360  C CB  . ASP   A 1 49  ? 15.14255 -13.82785 31.19031  1.000 65.23480 ? 48  ASP   A CB  1 
ATOM   361  C CG  . ASP   A 1 49  ? 15.16127 -14.85795 32.29981  1.000 67.03239 ? 48  ASP   A CG  1 
ATOM   362  O OD1 . ASP   A 1 49  ? 15.67693 -14.54591 33.39345  1.000 72.09005 ? 48  ASP   A OD1 1 
ATOM   363  O OD2 . ASP   A 1 49  ? 14.66266 -15.98142 32.07536  1.000 64.63931 ? 48  ASP   A OD2 1 
ATOM   364  N N   . MET   A 1 50  ? 14.07763 -10.82699 30.06180  1.000 66.55332 ? 49  MET   A N   1 
ATOM   365  C CA  . MET   A 1 50  ? 14.14235 -10.01340 28.85206  1.000 62.80350 ? 49  MET   A CA  1 
ATOM   366  C C   . MET   A 1 50  ? 14.98448 -8.75402  29.02021  1.000 59.77853 ? 49  MET   A C   1 
ATOM   367  O O   . MET   A 1 50  ? 15.49846 -8.23411  28.02359  1.000 57.51635 ? 49  MET   A O   1 
ATOM   368  C CB  . MET   A 1 50  ? 12.73175 -9.62906  28.40595  1.000 62.98503 ? 49  MET   A CB  1 
ATOM   369  C CG  . MET   A 1 50  ? 11.87824 -10.79565 27.93355  1.000 62.18979 ? 49  MET   A CG  1 
ATOM   370  S SD  . MET   A 1 50  ? 12.36172 -11.41041 26.31127  1.000 64.78733 ? 49  MET   A SD  1 
ATOM   371  C CE  . MET   A 1 50  ? 10.76722 -11.93277 25.67086  1.000 52.14830 ? 49  MET   A CE  1 
ATOM   372  N N   . LEU   A 1 51  ? 15.13661 -8.24830  30.24503  1.000 62.15163 ? 50  LEU   A N   1 
ATOM   373  C CA  . LEU   A 1 51  ? 15.92394 -7.03571  30.44559  1.000 62.13730 ? 50  LEU   A CA  1 
ATOM   374  C C   . LEU   A 1 51  ? 17.40770 -7.29996  30.21743  1.000 62.70378 ? 50  LEU   A C   1 
ATOM   375  O O   . LEU   A 1 51  ? 18.08247 -6.54443  29.50683  1.000 61.93974 ? 50  LEU   A O   1 
ATOM   376  C CB  . LEU   A 1 51  ? 15.67477 -6.48000  31.85113  1.000 60.70926 ? 50  LEU   A CB  1 
ATOM   377  C CG  . LEU   A 1 51  ? 16.30829 -5.14255  32.26077  1.000 64.67256 ? 50  LEU   A CG  1 
ATOM   378  C CD1 . LEU   A 1 51  ? 17.67870 -5.33188  32.91010  1.000 67.03987 ? 50  LEU   A CD1 1 
ATOM   379  C CD2 . LEU   A 1 51  ? 16.39643 -4.18356  31.07684  1.000 63.40347 ? 50  LEU   A CD2 1 
ATOM   380  N N   . ASN   A 1 52  ? 17.93177 -8.36968  30.80920  1.000 62.17892 ? 51  ASN   A N   1 
ATOM   381  C CA  . ASN   A 1 52  ? 19.36223 -8.67698  30.77275  1.000 65.13495 ? 51  ASN   A CA  1 
ATOM   382  C C   . ASN   A 1 52  ? 19.54037 -10.18506 30.65563  1.000 63.97067 ? 51  ASN   A C   1 
ATOM   383  O O   . ASN   A 1 52  ? 19.92285 -10.86339 31.61700  1.000 68.95652 ? 51  ASN   A O   1 
ATOM   384  C CB  . ASN   A 1 52  ? 20.05821 -8.12784  32.02117  1.000 71.36670 ? 51  ASN   A CB  1 
ATOM   385  C CG  . ASN   A 1 52  ? 21.54092 -8.44112  32.05358  1.000 76.95602 ? 51  ASN   A CG  1 
ATOM   386  O OD1 . ASN   A 1 52  ? 22.24313 -8.28723  31.05452  1.000 82.56202 ? 51  ASN   A OD1 1 
ATOM   387  N ND2 . ASN   A 1 52  ? 22.02233 -8.89663  33.20502  1.000 79.22459 ? 51  ASN   A ND2 1 
ATOM   388  N N   . PRO   A 1 53  ? 19.26823 -10.74813 29.48005  1.000 60.66972 ? 52  PRO   A N   1 
ATOM   389  C CA  . PRO   A 1 53  ? 19.36862 -12.20239 29.32371  1.000 56.51730 ? 52  PRO   A CA  1 
ATOM   390  C C   . PRO   A 1 53  ? 20.80242 -12.65327 29.09407  1.000 52.93026 ? 52  PRO   A C   1 
ATOM   391  O O   . PRO   A 1 53  ? 21.56229 -12.03479 28.34468  1.000 55.43404 ? 52  PRO   A O   1 
ATOM   392  C CB  . PRO   A 1 53  ? 18.49758 -12.47995 28.09345  1.000 54.53360 ? 52  PRO   A CB  1 
ATOM   393  C CG  . PRO   A 1 53  ? 18.62250 -11.23880 27.28007  1.000 54.85691 ? 52  PRO   A CG  1 
ATOM   394  C CD  . PRO   A 1 53  ? 18.80012 -10.09159 28.24626  1.000 60.23963 ? 52  PRO   A CD  1 
ATOM   395  N N   . ASN   A 1 54  ? 21.16944 -13.73836 29.76579  1.000 50.44720 ? 53  ASN   A N   1 
ATOM   396  C CA  . ASN   A 1 54  ? 22.42141 -14.45121 29.52370  1.000 49.33948 ? 53  ASN   A CA  1 
ATOM   397  C C   . ASN   A 1 54  ? 22.01224 -15.75450 28.84474  1.000 49.55604 ? 53  ASN   A C   1 
ATOM   398  O O   . ASN   A 1 54  ? 21.71491 -16.74958 29.50710  1.000 47.92335 ? 53  ASN   A O   1 
ATOM   399  C CB  . ASN   A 1 54  ? 23.19907 -14.68971 30.82105  1.000 49.02712 ? 53  ASN   A CB  1 
ATOM   400  C CG  . ASN   A 1 54  ? 24.59498 -15.23829 30.57524  1.000 49.73305 ? 53  ASN   A CG  1 
ATOM   401  O OD1 . ASN   A 1 54  ? 24.80036 -16.08411 29.70378  1.000 52.36456 ? 53  ASN   A OD1 1 
ATOM   402  N ND2 . ASN   A 1 54  ? 25.56407 -14.75103 31.34013  1.000 51.35824 ? 53  ASN   A ND2 1 
ATOM   403  N N   . TYR   A 1 55  ? 21.99475 -15.73703 27.50892  1.000 48.33280 ? 54  TYR   A N   1 
ATOM   404  C CA  . TYR   A 1 55  ? 21.34340 -16.81072 26.76705  1.000 46.80790 ? 54  TYR   A CA  1 
ATOM   405  C C   . TYR   A 1 55  ? 22.04297 -18.15101 26.94803  1.000 47.68818 ? 54  TYR   A C   1 
ATOM   406  O O   . TYR   A 1 55  ? 21.38368 -19.19325 26.92231  1.000 46.94795 ? 54  TYR   A O   1 
ATOM   407  C CB  . TYR   A 1 55  ? 21.25074 -16.44459 25.28657  1.000 43.84308 ? 54  TYR   A CB  1 
ATOM   408  C CG  . TYR   A 1 55  ? 20.13899 -15.46381 24.99198  1.000 42.18573 ? 54  TYR   A CG  1 
ATOM   409  C CD1 . TYR   A 1 55  ? 18.81919 -15.89135 24.89192  1.000 41.18719 ? 54  TYR   A CD1 1 
ATOM   410  C CD2 . TYR   A 1 55  ? 20.40391 -14.11022 24.82683  1.000 41.57369 ? 54  TYR   A CD2 1 
ATOM   411  C CE1 . TYR   A 1 55  ? 17.79456 -14.99868 24.62376  1.000 40.86564 ? 54  TYR   A CE1 1 
ATOM   412  C CE2 . TYR   A 1 55  ? 19.38719 -13.21151 24.55384  1.000 42.68606 ? 54  TYR   A CE2 1 
ATOM   413  C CZ  . TYR   A 1 55  ? 18.08512 -13.66113 24.45548  1.000 40.55724 ? 54  TYR   A CZ  1 
ATOM   414  O OH  . TYR   A 1 55  ? 17.07006 -12.77042 24.18818  1.000 37.33168 ? 54  TYR   A OH  1 
ATOM   415  N N   . GLU   A 1 56  ? 23.36275 -18.15804 27.13760  1.000 48.43033 ? 55  GLU   A N   1 
ATOM   416  C CA  . GLU   A 1 56  ? 24.04008 -19.41980 27.42199  1.000 50.85802 ? 55  GLU   A CA  1 
ATOM   417  C C   . GLU   A 1 56  ? 23.55404 -20.01204 28.74039  0.950 50.46645 ? 55  GLU   A C   1 
ATOM   418  O O   . GLU   A 1 56  ? 23.16249 -21.18446 28.80222  1.000 51.00867 ? 55  GLU   A O   1 
ATOM   419  C CB  . GLU   A 1 56  ? 25.55613 -19.21840 27.44178  0.980 53.86741 ? 55  GLU   A CB  1 
ATOM   420  C CG  . GLU   A 1 56  ? 26.22443 -19.39928 26.08634  1.000 59.43556 ? 55  GLU   A CG  1 
ATOM   421  C CD  . GLU   A 1 56  ? 27.73735 -19.27498 26.15352  0.730 66.80773 ? 55  GLU   A CD  1 
ATOM   422  O OE1 . GLU   A 1 56  ? 28.30995 -19.45946 27.24950  0.860 68.79922 ? 55  GLU   A OE1 1 
ATOM   423  O OE2 . GLU   A 1 56  ? 28.35522 -18.98938 25.10606  0.910 69.36340 ? 55  GLU   A OE2 1 
ATOM   424  N N   . ASP   A 1 57  ? 23.55892 -19.20539 29.80617  1.000 50.68960 ? 56  ASP   A N   1 
ATOM   425  C CA  . ASP   A 1 57  ? 23.12746 -19.69471 31.11267  1.000 51.81256 ? 56  ASP   A CA  1 
ATOM   426  C C   . ASP   A 1 57  ? 21.65734 -20.09782 31.09783  1.000 51.22767 ? 56  ASP   A C   1 
ATOM   427  O O   . ASP   A 1 57  ? 21.27866 -21.11362 31.69341  1.000 53.44558 ? 56  ASP   A O   1 
ATOM   428  C CB  . ASP   A 1 57  ? 23.37878 -18.63040 32.18259  1.000 51.26322 ? 56  ASP   A CB  1 
ATOM   429  C CG  . ASP   A 1 57  ? 24.84964 -18.29804 32.34314  1.000 51.82113 ? 56  ASP   A CG  1 
ATOM   430  O OD1 . ASP   A 1 57  ? 25.68206 -18.93107 31.66003  1.000 51.82059 ? 56  ASP   A OD1 1 
ATOM   431  O OD2 . ASP   A 1 57  ? 25.17301 -17.40113 33.15218  1.000 51.56669 ? 56  ASP   A OD2 1 
ATOM   432  N N   . LEU   A 1 58  ? 20.81269 -19.31372 30.42391  1.000 51.34907 ? 57  LEU   A N   1 
ATOM   433  C CA  . LEU   A 1 58  ? 19.39192 -19.64420 30.36066  1.000 53.74248 ? 57  LEU   A CA  1 
ATOM   434  C C   . LEU   A 1 58  ? 19.15667 -20.92203 29.56587  1.000 53.05179 ? 57  LEU   A C   1 
ATOM   435  O O   . LEU   A 1 58  ? 18.37441 -21.78434 29.98274  1.000 54.81884 ? 57  LEU   A O   1 
ATOM   436  C CB  . LEU   A 1 58  ? 18.60885 -18.48060 29.75216  1.000 51.68855 ? 57  LEU   A CB  1 
ATOM   437  C CG  . LEU   A 1 58  ? 18.57834 -17.19483 30.57966  1.000 54.37734 ? 57  LEU   A CG  1 
ATOM   438  C CD1 . LEU   A 1 58  ? 17.90410 -16.07023 29.80928  1.000 53.26387 ? 57  LEU   A CD1 1 
ATOM   439  C CD2 . LEU   A 1 58  ? 17.87684 -17.43838 31.90603  1.000 57.80531 ? 57  LEU   A CD2 1 
ATOM   440  N N   . LEU   A 1 59  ? 19.83627 -21.06482 28.42576  1.000 50.79081 ? 58  LEU   A N   1 
ATOM   441  C CA  . LEU   A 1 59  ? 19.66193 -22.23924 27.57945  1.000 51.68340 ? 58  LEU   A CA  1 
ATOM   442  C C   . LEU   A 1 59  ? 20.18135 -23.50165 28.25088  1.000 53.08987 ? 58  LEU   A C   1 
ATOM   443  O O   . LEU   A 1 59  ? 19.62595 -24.58674 28.04191  1.000 52.69354 ? 58  LEU   A O   1 
ATOM   444  C CB  . LEU   A 1 59  ? 20.37214 -22.02224 26.24275  1.000 47.93090 ? 58  LEU   A CB  1 
ATOM   445  C CG  . LEU   A 1 59  ? 20.28494 -23.16358 25.23176  1.000 46.74911 ? 58  LEU   A CG  1 
ATOM   446  C CD1 . LEU   A 1 59  ? 18.85258 -23.33012 24.75076  1.000 48.24606 ? 58  LEU   A CD1 1 
ATOM   447  C CD2 . LEU   A 1 59  ? 21.22641 -22.92327 24.06529  1.000 43.02874 ? 58  LEU   A CD2 1 
ATOM   448  N N   . ILE   A 1 60  ? 21.23669 -23.38136 29.06068  1.000 51.98821 ? 59  ILE   A N   1 
ATOM   449  C CA  . ILE   A 1 60  ? 21.82021 -24.54452 29.71732  1.000 52.72122 ? 59  ILE   A CA  1 
ATOM   450  C C   . ILE   A 1 60  ? 20.83907 -25.21502 30.67203  1.000 55.69062 ? 59  ILE   A C   1 
ATOM   451  O O   . ILE   A 1 60  ? 20.93481 -26.42493 30.90767  1.000 58.52362 ? 59  ILE   A O   1 
ATOM   452  C CB  . ILE   A 1 60  ? 23.13621 -24.10930 30.40222  1.000 53.00951 ? 59  ILE   A CB  1 
ATOM   453  C CG1 . ILE   A 1 60  ? 24.25954 -24.06763 29.36456  1.000 51.60918 ? 59  ILE   A CG1 1 
ATOM   454  C CG2 . ILE   A 1 60  ? 23.49339 -25.00475 31.58359  1.000 51.40788 ? 59  ILE   A CG2 1 
ATOM   455  C CD1 . ILE   A 1 60  ? 25.57525 -23.60770 29.89743  1.000 51.95939 ? 59  ILE   A CD1 1 
ATOM   456  N N   . ARG   A 1 61  ? 19.86692 -24.47268 31.19448  1.000 57.32783 ? 60  ARG   A N   1 
ATOM   457  C CA  . ARG   A 1 61  ? 18.84060 -25.05364 32.05110  1.000 58.34433 ? 60  ARG   A CA  1 
ATOM   458  C C   . ARG   A 1 61  ? 17.68591 -25.67550 31.26710  1.000 57.99925 ? 60  ARG   A C   1 
ATOM   459  O O   . ARG   A 1 61  ? 16.65290 -25.99167 31.86782  1.000 64.38524 ? 60  ARG   A O   1 
ATOM   460  C CB  . ARG   A 1 61  ? 18.29090 -23.99601 33.01350  1.000 64.48602 ? 60  ARG   A CB  1 
ATOM   461  C CG  . ARG   A 1 61  ? 19.34727 -23.25773 33.82357  1.000 68.13687 ? 60  ARG   A CG  1 
ATOM   462  C CD  . ARG   A 1 61  ? 18.70338 -22.50982 34.98182  1.000 76.45769 ? 60  ARG   A CD  1 
ATOM   463  N NE  . ARG   A 1 61  ? 17.49602 -21.80355 34.56701  1.000 78.48732 ? 60  ARG   A NE  1 
ATOM   464  C CZ  . ARG   A 1 61  ? 17.38113 -20.48434 34.49490  1.000 75.09477 ? 60  ARG   A CZ  1 
ATOM   465  N NH1 . ARG   A 1 61  ? 18.37598 -19.68364 34.84107  1.000 78.53738 ? 60  ARG   A NH1 1 
ATOM   466  N NH2 . ARG   A 1 61  ? 16.23649 -19.95512 34.07091  1.000 73.55427 ? 60  ARG   A NH2 1 
ATOM   467  N N   . LYS   A 1 62  ? 17.82723 -25.86153 29.95635  1.000 56.00458 ? 61  LYS   A N   1 
ATOM   468  C CA  . LYS   A 1 62  ? 16.75067 -26.36538 29.11287  1.000 56.37589 ? 61  LYS   A CA  1 
ATOM   469  C C   . LYS   A 1 62  ? 17.16421 -27.68044 28.46807  1.000 54.23765 ? 61  LYS   A C   1 
ATOM   470  O O   . LYS   A 1 62  ? 18.26898 -27.79167 27.92610  1.000 53.44536 ? 61  LYS   A O   1 
ATOM   471  C CB  . LYS   A 1 62  ? 16.37190 -25.34587 28.03272  1.000 53.21634 ? 61  LYS   A CB  1 
ATOM   472  C CG  . LYS   A 1 62  ? 15.62041 -24.13266 28.55792  1.000 52.86843 ? 61  LYS   A CG  1 
ATOM   473  C CD  . LYS   A 1 62  ? 14.37126 -24.55355 29.31849  1.000 55.44070 ? 61  LYS   A CD  1 
ATOM   474  C CE  . LYS   A 1 62  ? 13.50147 -23.36031 29.68607  1.000 54.40004 ? 61  LYS   A CE  1 
ATOM   475  N NZ  . LYS   A 1 62  ? 14.17867 -22.41482 30.61238  1.000 60.24210 ? 61  LYS   A NZ  1 
ATOM   476  N N   . SER   A 1 63  ? 16.27610 -28.66736 28.52817  1.000 53.49098 ? 62  SER   A N   1 
ATOM   477  C CA  . SER   A 1 63  ? 16.46006 -29.95933 27.88571  1.000 53.38183 ? 62  SER   A CA  1 
ATOM   478  C C   . SER   A 1 63  ? 15.54631 -30.05908 26.67063  1.000 51.33017 ? 62  SER   A C   1 
ATOM   479  O O   . SER   A 1 63  ? 14.68103 -29.20992 26.44610  1.000 52.25873 ? 62  SER   A O   1 
ATOM   480  C CB  . SER   A 1 63  ? 16.17536 -31.10291 28.86730  1.000 55.64572 ? 62  SER   A CB  1 
ATOM   481  O OG  . SER   A 1 63  ? 17.01822 -31.02604 30.00574  1.000 60.46885 ? 62  SER   A OG  1 
ATOM   482  N N   . ASN   A 1 64  ? 15.74974 -31.12296 25.88616  1.000 50.91505 ? 63  ASN   A N   1 
ATOM   483  C CA  . ASN   A 1 64  ? 14.97159 -31.31134 24.66301  1.000 51.73970 ? 63  ASN   A CA  1 
ATOM   484  C C   . ASN   A 1 64  ? 13.47497 -31.32306 24.94678  1.000 53.41252 ? 63  ASN   A C   1 
ATOM   485  O O   . ASN   A 1 64  ? 12.69369 -30.68694 24.22788  1.000 51.09873 ? 63  ASN   A O   1 
ATOM   486  C CB  . ASN   A 1 64  ? 15.38203 -32.61045 23.96765  1.000 50.32777 ? 63  ASN   A CB  1 
ATOM   487  C CG  . ASN   A 1 64  ? 16.78453 -32.55343 23.39724  1.000 50.47647 ? 63  ASN   A CG  1 
ATOM   488  O OD1 . ASN   A 1 64  ? 17.28137 -31.48562 23.04041  1.000 48.93093 ? 63  ASN   A OD1 1 
ATOM   489  N ND2 . ASN   A 1 64  ? 17.42779 -33.71152 23.29838  1.000 50.77870 ? 63  ASN   A ND2 1 
ATOM   490  N N   . HIS   A 1 65  ? 13.05583 -32.03818 25.99258  1.000 53.29291 ? 64  HIS   A N   1 
ATOM   491  C CA  . HIS   A 1 65  ? 11.63538 -32.16771 26.29091  1.000 54.14661 ? 64  HIS   A CA  1 
ATOM   492  C C   . HIS   A 1 65  ? 11.01467 -30.87031 26.78924  1.000 53.72081 ? 64  HIS   A C   1 
ATOM   493  O O   . HIS   A 1 65  ? 9.78702  -30.80250 26.91365  1.000 56.50241 ? 64  HIS   A O   1 
ATOM   494  C CB  . HIS   A 1 65  ? 11.41254 -33.27724 27.31937  1.000 57.05762 ? 64  HIS   A CB  1 
ATOM   495  C CG  . HIS   A 1 65  ? 11.94279 -32.95597 28.68135  1.000 57.95267 ? 64  HIS   A CG  1 
ATOM   496  N ND1 . HIS   A 1 65  ? 13.24106 -33.22463 29.05717  1.000 59.54086 ? 64  HIS   A ND1 1 
ATOM   497  C CD2 . HIS   A 1 65  ? 11.34834 -32.39004 29.75843  1.000 59.94521 ? 64  HIS   A CD2 1 
ATOM   498  C CE1 . HIS   A 1 65  ? 13.42420 -32.83557 30.30632  1.000 63.02454 ? 64  HIS   A CE1 1 
ATOM   499  N NE2 . HIS   A 1 65  ? 12.29123 -32.32622 30.75525  1.000 62.16468 ? 64  HIS   A NE2 1 
ATOM   500  N N   . ASN   A 1 66  ? 11.82240 -29.84901 27.08104  1.000 53.47561 ? 65  ASN   A N   1 
ATOM   501  C CA  . ASN   A 1 66  ? 11.29309 -28.54486 27.45693  1.000 52.86758 ? 65  ASN   A CA  1 
ATOM   502  C C   . ASN   A 1 66  ? 10.81018 -27.74217 26.26028  1.000 52.67369 ? 65  ASN   A C   1 
ATOM   503  O O   . ASN   A 1 66  ? 10.19992 -26.68415 26.44907  1.000 51.32574 ? 65  ASN   A O   1 
ATOM   504  C CB  . ASN   A 1 66  ? 12.35136 -27.73667 28.21195  1.000 52.29360 ? 65  ASN   A CB  1 
ATOM   505  C CG  . ASN   A 1 66  ? 12.72801 -28.36448 29.53563  1.000 56.59361 ? 65  ASN   A CG  1 
ATOM   506  O OD1 . ASN   A 1 66  ? 13.90051 -28.63638 29.79500  1.000 56.16869 ? 65  ASN   A OD1 1 
ATOM   507  N ND2 . ASN   A 1 66  ? 11.73183 -28.60349 30.38205  1.000 55.91384 ? 65  ASN   A ND2 1 
ATOM   508  N N   . PHE   A 1 67  ? 11.07358 -28.21052 25.04577  1.000 50.05576 ? 66  PHE   A N   1 
ATOM   509  C CA  . PHE   A 1 67  ? 10.67528 -27.52154 23.82597  1.000 51.08816 ? 66  PHE   A CA  1 
ATOM   510  C C   . PHE   A 1 67  ? 9.48627  -28.26265 23.23285  1.000 50.82967 ? 66  PHE   A C   1 
ATOM   511  O O   . PHE   A 1 67  ? 9.62565  -29.39759 22.76383  1.000 51.49484 ? 66  PHE   A O   1 
ATOM   512  C CB  . PHE   A 1 67  ? 11.83646 -27.44463 22.83731  1.000 51.32187 ? 66  PHE   A CB  1 
ATOM   513  C CG  . PHE   A 1 67  ? 12.97558 -26.59304 23.31436  1.000 51.08319 ? 66  PHE   A CG  1 
ATOM   514  C CD1 . PHE   A 1 67  ? 12.85594 -25.21292 23.34290  1.000 50.72874 ? 66  PHE   A CD1 1 
ATOM   515  C CD2 . PHE   A 1 67  ? 14.16228 -27.16873 23.74061  1.000 50.51967 ? 66  PHE   A CD2 1 
ATOM   516  C CE1 . PHE   A 1 67  ? 13.89644 -24.42131 23.78600  1.000 50.63289 ? 66  PHE   A CE1 1 
ATOM   517  C CE2 . PHE   A 1 67  ? 15.20961 -26.38105 24.18275  1.000 49.33222 ? 66  PHE   A CE2 1 
ATOM   518  C CZ  . PHE   A 1 67  ? 15.07673 -25.00539 24.20503  1.000 49.29407 ? 66  PHE   A CZ  1 
ATOM   519  N N   . LEU   A 1 68  ? 8.32068  -27.62357 23.26106  1.000 49.02496 ? 67  LEU   A N   1 
ATOM   520  C CA  . LEU   A 1 68  ? 7.09503  -28.20116 22.72313  1.000 51.97603 ? 67  LEU   A CA  1 
ATOM   521  C C   . LEU   A 1 68  ? 6.89561  -27.66803 21.30891  1.000 51.56011 ? 67  LEU   A C   1 
ATOM   522  O O   . LEU   A 1 68  ? 6.63562  -26.47627 21.11845  1.000 48.17492 ? 67  LEU   A O   1 
ATOM   523  C CB  . LEU   A 1 68  ? 5.90493  -27.86778 23.61872  1.000 51.34178 ? 67  LEU   A CB  1 
ATOM   524  C CG  . LEU   A 1 68  ? 6.03390  -28.34623 25.06459  1.000 54.06591 ? 67  LEU   A CG  1 
ATOM   525  C CD1 . LEU   A 1 68  ? 4.93525  -27.74679 25.92680  1.000 55.51383 ? 67  LEU   A CD1 1 
ATOM   526  C CD2 . LEU   A 1 68  ? 6.00642  -29.86730 25.12664  1.000 57.72976 ? 67  LEU   A CD2 1 
ATOM   527  N N   . VAL   A 1 69  ? 7.03024  -28.54554 20.31914  1.000 52.54056 ? 68  VAL   A N   1 
ATOM   528  C CA  . VAL   A 1 69  ? 6.87902  -28.18427 18.91440  1.000 51.68245 ? 68  VAL   A CA  1 
ATOM   529  C C   . VAL   A 1 69  ? 5.61695  -28.84719 18.38564  1.000 53.81643 ? 68  VAL   A C   1 
ATOM   530  O O   . VAL   A 1 69  ? 5.43548  -30.06170 18.53718  1.000 55.81512 ? 68  VAL   A O   1 
ATOM   531  C CB  . VAL   A 1 69  ? 8.10751  -28.59767 18.08588  1.000 51.93967 ? 68  VAL   A CB  1 
ATOM   532  C CG1 . VAL   A 1 69  ? 7.93153  -28.17909 16.62843  1.000 47.36216 ? 68  VAL   A CG1 1 
ATOM   533  C CG2 . VAL   A 1 69  ? 9.37251  -27.99305 18.67907  1.000 48.67363 ? 68  VAL   A CG2 1 
ATOM   534  N N   . GLN   A 1 70  ? 4.74732  -28.05298 17.76435  1.000 52.97169 ? 69  GLN   A N   1 
ATOM   535  C CA  . GLN   A 1 70  ? 3.48097  -28.55246 17.24183  1.000 56.62438 ? 69  GLN   A CA  1 
ATOM   536  C C   . GLN   A 1 70  ? 3.28405  -28.05238 15.81765  1.000 55.21395 ? 69  GLN   A C   1 
ATOM   537  O O   . GLN   A 1 70  ? 3.27626  -26.84172 15.57553  1.000 50.55567 ? 69  GLN   A O   1 
ATOM   538  C CB  . GLN   A 1 70  ? 2.31344  -28.12596 18.13720  1.000 56.74803 ? 69  GLN   A CB  1 
ATOM   539  C CG  . GLN   A 1 70  ? 1.09208  -29.01898 18.01537  1.000 64.36991 ? 69  GLN   A CG  1 
ATOM   540  C CD  . GLN   A 1 70  ? 0.13805  -28.86499 19.18404  1.000 67.65284 ? 69  GLN   A CD  1 
ATOM   541  O OE1 . GLN   A 1 70  ? -0.10955 -27.75556 19.65645  1.000 64.38849 ? 69  GLN   A OE1 1 
ATOM   542  N NE2 . GLN   A 1 70  ? -0.39590 -29.98354 19.66378  1.000 72.27104 ? 69  GLN   A NE2 1 
ATOM   543  N N   . ALA   A 1 71  ? 3.13956  -28.98467 14.88003  1.000 59.74794 ? 70  ALA   A N   1 
ATOM   544  C CA  . ALA   A 1 71  ? 2.80442  -28.67634 13.49306  1.000 59.57984 ? 70  ALA   A CA  1 
ATOM   545  C C   . ALA   A 1 71  ? 1.33207  -29.02366 13.30791  1.000 64.84502 ? 70  ALA   A C   1 
ATOM   546  O O   . ALA   A 1 71  ? 0.96839  -30.19833 13.19938  1.000 66.08149 ? 70  ALA   A O   1 
ATOM   547  C CB  . ALA   A 1 71  ? 3.69353  -29.44828 12.52564  1.000 53.67220 ? 70  ALA   A CB  1 
ATOM   548  N N   . GLY   A 1 72  ? 0.48746  -28.00225 13.27454  1.000 61.15792 ? 71  GLY   A N   1 
ATOM   549  C CA  . GLY   A 1 72  ? -0.94204 -28.25328 13.29496  1.000 68.39339 ? 71  GLY   A CA  1 
ATOM   550  C C   . GLY   A 1 72  ? -1.31301 -28.87017 14.62926  1.000 74.76540 ? 71  GLY   A C   1 
ATOM   551  O O   . GLY   A 1 72  ? -1.14135 -28.26080 15.69220  1.000 75.41987 ? 71  GLY   A O   1 
ATOM   552  N N   . ASN   A 1 73  ? -1.81171 -30.10395 14.58854  1.000 76.82340 ? 72  ASN   A N   1 
ATOM   553  C CA  . ASN   A 1 73  ? -2.08858 -30.87678 15.79009  1.000 81.64679 ? 72  ASN   A CA  1 
ATOM   554  C C   . ASN   A 1 73  ? -1.02484 -31.92988 16.06883  1.000 84.33933 ? 72  ASN   A C   1 
ATOM   555  O O   . ASN   A 1 73  ? -1.10639 -32.62489 17.08844  1.000 86.61840 ? 72  ASN   A O   1 
ATOM   556  C CB  . ASN   A 1 73  ? -3.46160 -31.55104 15.68269  1.000 87.10748 ? 72  ASN   A CB  1 
ATOM   557  C CG  . ASN   A 1 73  ? -4.60480 -30.56121 15.76611  1.000 94.37266 ? 72  ASN   A CG  1 
ATOM   558  O OD1 . ASN   A 1 73  ? -4.83950 -29.78507 14.83992  1.000 98.99731 ? 72  ASN   A OD1 1 
ATOM   559  N ND2 . ASN   A 1 73  ? -5.32850 -30.58743 16.87924  1.000 91.57333 ? 72  ASN   A ND2 1 
ATOM   560  N N   . VAL   A 1 74  ? -0.03062 -32.05848 15.19731  1.000 74.04555 ? 73  VAL   A N   1 
ATOM   561  C CA  . VAL   A 1 74  ? 0.97592  -33.10611 15.32337  1.000 71.99540 ? 73  VAL   A CA  1 
ATOM   562  C C   . VAL   A 1 74  ? 2.07131  -32.62306 16.26371  1.000 68.12342 ? 73  VAL   A C   1 
ATOM   563  O O   . VAL   A 1 74  ? 2.67822  -31.57200 16.03923  1.000 64.50200 ? 73  VAL   A O   1 
ATOM   564  C CB  . VAL   A 1 74  ? 1.55489  -33.48131 13.95231  1.000 71.70426 ? 73  VAL   A CB  1 
ATOM   565  C CG1 . VAL   A 1 74  ? 2.20049  -34.85718 14.00631  1.000 71.36165 ? 73  VAL   A CG1 1 
ATOM   566  C CG2 . VAL   A 1 74  ? 0.47393  -33.42928 12.88702  1.000 76.63885 ? 73  VAL   A CG2 1 
ATOM   567  N N   . GLN   A 1 75  ? 2.33045  -33.39003 17.31608  1.000 66.77744 ? 74  GLN   A N   1 
ATOM   568  C CA  . GLN   A 1 75  ? 3.39519  -33.07067 18.25682  1.000 64.32585 ? 74  GLN   A CA  1 
ATOM   569  C C   . GLN   A 1 75  ? 4.71050  -33.62842 17.72739  1.000 63.20449 ? 74  GLN   A C   1 
ATOM   570  O O   . GLN   A 1 75  ? 4.83578  -34.83952 17.52131  1.000 68.39449 ? 74  GLN   A O   1 
ATOM   571  C CB  . GLN   A 1 75  ? 3.08610  -33.64481 19.63887  1.000 71.13435 ? 74  GLN   A CB  1 
ATOM   572  C CG  . GLN   A 1 75  ? 3.93087  -33.05593 20.75522  1.000 69.92729 ? 74  GLN   A CG  1 
ATOM   573  C CD  . GLN   A 1 75  ? 3.54236  -31.62599 21.07599  1.000 70.55555 ? 74  GLN   A CD  1 
ATOM   574  O OE1 . GLN   A 1 75  ? 2.43368  -31.18869 20.76391  1.000 72.13893 ? 74  GLN   A OE1 1 
ATOM   575  N NE2 . GLN   A 1 75  ? 4.45463  -30.88778 21.69818  1.000 69.41115 ? 74  GLN   A NE2 1 
ATOM   576  N N   . LEU   A 1 76  ? 5.68419  -32.75194 17.49958  1.000 60.91763 ? 75  LEU   A N   1 
ATOM   577  C CA  . LEU   A 1 76  ? 7.00572  -33.19657 17.08719  1.000 59.15778 ? 75  LEU   A CA  1 
ATOM   578  C C   . LEU   A 1 76  ? 7.84375  -33.55108 18.30704  1.000 59.73827 ? 75  LEU   A C   1 
ATOM   579  O O   . LEU   A 1 76  ? 7.74599  -32.90960 19.35767  1.000 59.93278 ? 75  LEU   A O   1 
ATOM   580  C CB  . LEU   A 1 76  ? 7.71336  -32.11954 16.26664  1.000 55.16675 ? 75  LEU   A CB  1 
ATOM   581  C CG  . LEU   A 1 76  ? 7.12240  -31.78379 14.89585  1.000 53.94665 ? 75  LEU   A CG  1 
ATOM   582  C CD1 . LEU   A 1 76  ? 8.09691  -30.93579 14.09558  1.000 49.03015 ? 75  LEU   A CD1 1 
ATOM   583  C CD2 . LEU   A 1 76  ? 6.75405  -33.04843 14.13563  1.000 53.79310 ? 75  LEU   A CD2 1 
ATOM   584  N N   . ARG   A 1 77  ? 8.66252  -34.58778 18.16426  1.000 57.69527 ? 76  ARG   A N   1 
ATOM   585  C CA  . ARG   A 1 77  ? 9.57736  -35.00984 19.21594  1.000 58.01040 ? 76  ARG   A CA  1 
ATOM   586  C C   . ARG   A 1 77  ? 10.92376 -34.33306 18.98914  1.000 55.30496 ? 76  ARG   A C   1 
ATOM   587  O O   . ARG   A 1 77  ? 11.50511 -34.44723 17.90535  1.000 52.41075 ? 76  ARG   A O   1 
ATOM   588  C CB  . ARG   A 1 77  ? 9.71777  -36.53191 19.22033  1.000 60.47649 ? 76  ARG   A CB  1 
ATOM   589  C CG  . ARG   A 1 77  ? 10.65694 -37.10228 20.27822  1.000 60.46544 ? 76  ARG   A CG  1 
ATOM   590  C CD  . ARG   A 1 77  ? 10.09465 -36.99497 21.69326  1.000 63.91040 ? 76  ARG   A CD  1 
ATOM   591  N NE  . ARG   A 1 77  ? 8.63886  -37.09442 21.74237  1.000 70.48746 ? 76  ARG   A NE  1 
ATOM   592  C CZ  . ARG   A 1 77  ? 7.84530  -36.15685 22.24361  1.000 66.34044 ? 76  ARG   A CZ  1 
ATOM   593  N NH1 . ARG   A 1 77  ? 8.33755  -35.05115 22.78150  1.000 66.49595 ? 76  ARG   A NH1 1 
ATOM   594  N NH2 . ARG   A 1 77  ? 6.52705  -36.33604 22.21148  1.000 66.21405 ? 76  ARG   A NH2 1 
ATOM   595  N N   . VAL   A 1 78  ? 11.40616 -33.61934 20.00085  1.000 54.36220 ? 77  VAL   A N   1 
ATOM   596  C CA  . VAL   A 1 78  ? 12.67906 -32.90942 19.92347  1.000 52.19347 ? 77  VAL   A CA  1 
ATOM   597  C C   . VAL   A 1 78  ? 13.78851 -33.84700 20.38604  1.000 51.23229 ? 77  VAL   A C   1 
ATOM   598  O O   . VAL   A 1 78  ? 13.73538 -34.38817 21.49628  1.000 50.98442 ? 77  VAL   A O   1 
ATOM   599  C CB  . VAL   A 1 78  ? 12.65106 -31.62472 20.76569  1.000 51.97735 ? 77  VAL   A CB  1 
ATOM   600  C CG1 . VAL   A 1 78  ? 14.03137 -30.98387 20.80826  1.000 49.94888 ? 77  VAL   A CG1 1 
ATOM   601  C CG2 . VAL   A 1 78  ? 11.62154 -30.64882 20.20797  1.000 50.86082 ? 77  VAL   A CG2 1 
ATOM   602  N N   . ILE   A 1 79  ? 14.79729 -34.03760 19.53725  1.000 50.69732 ? 78  ILE   A N   1 
ATOM   603  C CA  . ILE   A 1 79  ? 15.88192 -34.96908 19.81492  1.000 49.31154 ? 78  ILE   A CA  1 
ATOM   604  C C   . ILE   A 1 79  ? 17.23699 -34.26228 19.84538  1.000 49.26339 ? 78  ILE   A C   1 
ATOM   605  O O   . ILE   A 1 79  ? 18.27477 -34.90001 19.70328  1.000 49.68216 ? 78  ILE   A O   1 
ATOM   606  C CB  . ILE   A 1 79  ? 15.87855 -36.13509 18.80774  1.000 48.53060 ? 78  ILE   A CB  1 
ATOM   607  C CG1 . ILE   A 1 79  ? 16.13530 -35.62487 17.38835  1.000 49.76753 ? 78  ILE   A CG1 1 
ATOM   608  C CG2 . ILE   A 1 79  ? 14.55353 -36.88040 18.86553  1.000 50.43396 ? 78  ILE   A CG2 1 
ATOM   609  C CD1 . ILE   A 1 79  ? 16.05737 -36.70705 16.32836  1.000 49.02122 ? 78  ILE   A CD1 1 
ATOM   610  N N   . GLY   A 1 80  ? 17.23447 -32.95431 20.04128  1.000 49.46790 ? 79  GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 80  ? 18.45494 -32.17822 20.10236  1.000 46.60083 ? 79  GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 80  ? 18.16398 -30.71255 19.90682  1.000 45.91536 ? 79  GLY   A C   1 
ATOM   613  O O   . GLY   A 1 80  ? 17.14624 -30.32036 19.34135  1.000 44.79501 ? 79  GLY   A O   1 
ATOM   614  N N   . HIS   A 1 81  ? 19.08830 -29.88111 20.37874  1.000 44.25543 ? 80  HIS   A N   1 
ATOM   615  C CA  . HIS   A 1 81  ? 18.89733 -28.44306 20.26676  1.000 44.01532 ? 80  HIS   A CA  1 
ATOM   616  C C   . HIS   A 1 81  ? 20.24484 -27.74097 20.34252  1.000 44.98186 ? 80  HIS   A C   1 
ATOM   617  O O   . HIS   A 1 81  ? 21.13772 -28.17101 21.07796  1.000 44.39885 ? 80  HIS   A O   1 
ATOM   618  C CB  . HIS   A 1 81  ? 17.96884 -27.92021 21.36630  1.000 43.14044 ? 80  HIS   A CB  1 
ATOM   619  C CG  . HIS   A 1 81  ? 18.54908 -28.02603 22.74126  1.000 45.97236 ? 80  HIS   A CG  1 
ATOM   620  N ND1 . HIS   A 1 81  ? 18.41649 -29.15508 23.52140  1.000 47.32857 ? 80  HIS   A ND1 1 
ATOM   621  C CD2 . HIS   A 1 81  ? 19.27131 -27.14532 23.47313  1.000 46.23770 ? 80  HIS   A CD2 1 
ATOM   622  C CE1 . HIS   A 1 81  ? 19.02880 -28.96337 24.67626  1.000 47.91003 ? 80  HIS   A CE1 1 
ATOM   623  N NE2 . HIS   A 1 81  ? 19.55536 -27.75181 24.67264  1.000 47.43494 ? 80  HIS   A NE2 1 
ATOM   624  N N   . SER   A 1 82  ? 20.37687 -26.65850 19.57912  1.000 41.37650 ? 81  SER   A N   1 
ATOM   625  C CA  . SER   A 1 82  ? 21.57239 -25.83001 19.60578  1.000 42.81872 ? 81  SER   A CA  1 
ATOM   626  C C   . SER   A 1 82  ? 21.17417 -24.37422 19.40868  1.000 41.88937 ? 81  SER   A C   1 
ATOM   627  O O   . SER   A 1 82  ? 20.04055 -24.05824 19.03736  1.000 40.42709 ? 81  SER   A O   1 
ATOM   628  C CB  . SER   A 1 82  ? 22.58432 -26.26371 18.53818  1.000 41.05356 ? 81  SER   A CB  1 
ATOM   629  O OG  . SER   A 1 82  ? 22.09095 -26.00689 17.23567  1.000 47.71708 ? 81  SER   A OG  1 
ATOM   630  N N   . MET   A 1 83  ? 22.12451 -23.48085 19.66459  1.000 40.10294 ? 82  MET   A N   1 
ATOM   631  C CA  . MET   A 1 83  ? 21.92001 -22.04659 19.50755  1.000 39.25793 ? 82  MET   A CA  1 
ATOM   632  C C   . MET   A 1 83  ? 22.96072 -21.50403 18.54046  1.000 40.32868 ? 82  MET   A C   1 
ATOM   633  O O   . MET   A 1 83  ? 24.16491 -21.61186 18.79646  1.000 42.31216 ? 82  MET   A O   1 
ATOM   634  C CB  . MET   A 1 83  ? 22.00669 -21.32878 20.85677  1.000 40.00506 ? 82  MET   A CB  1 
ATOM   635  C CG  . MET   A 1 83  ? 21.85550 -19.82060 20.76837  1.000 39.59615 ? 82  MET   A CG  1 
ATOM   636  S SD  . MET   A 1 83  ? 21.73511 -19.02852 22.38566  1.000 42.47370 ? 82  MET   A SD  1 
ATOM   637  C CE  . MET   A 1 83  ? 23.33500 -19.41464 23.09616  1.000 40.20449 ? 82  MET   A CE  1 
ATOM   638  N N   . GLN   A 1 84  ? 22.49748 -20.93352 17.43149  1.000 38.22775 ? 83  GLN   A N   1 
ATOM   639  C CA  . GLN   A 1 84  ? 23.35180 -20.27154 16.45538  1.000 39.26092 ? 83  GLN   A CA  1 
ATOM   640  C C   . GLN   A 1 84  ? 22.97959 -18.79553 16.46803  1.000 38.50617 ? 83  GLN   A C   1 
ATOM   641  O O   . GLN   A 1 84  ? 21.87687 -18.42227 16.04642  1.000 38.76477 ? 83  GLN   A O   1 
ATOM   642  C CB  . GLN   A 1 84  ? 23.17430 -20.87199 15.06500  1.000 41.25477 ? 83  GLN   A CB  1 
ATOM   643  C CG  . GLN   A 1 84  ? 23.98086 -20.18186 13.97886  1.000 42.25495 ? 83  GLN   A CG  1 
ATOM   644  C CD  . GLN   A 1 84  ? 23.73469 -20.77981 12.60534  1.000 44.90201 ? 83  GLN   A CD  1 
ATOM   645  O OE1 . GLN   A 1 84  ? 22.85126 -21.61844 12.42806  1.000 45.80711 ? 83  GLN   A OE1 1 
ATOM   646  N NE2 . GLN   A 1 84  ? 24.52090 -20.34968 11.62414  1.000 44.99105 ? 83  GLN   A NE2 1 
ATOM   647  N N   . ASN   A 1 85  ? 23.89707 -17.96376 16.95976  1.000 35.90375 ? 84  ASN   A N   1 
ATOM   648  C CA  . ASN   A 1 85  ? 23.64635 -16.53849 17.12899  1.000 37.47034 ? 84  ASN   A CA  1 
ATOM   649  C C   . ASN   A 1 85  ? 22.32431 -16.33228 17.86821  1.000 37.77203 ? 84  ASN   A C   1 
ATOM   650  O O   . ASN   A 1 85  ? 22.14511 -16.85423 18.97406  1.000 39.84786 ? 84  ASN   A O   1 
ATOM   651  C CB  . ASN   A 1 85  ? 23.66908 -15.84056 15.76856  1.000 37.93484 ? 84  ASN   A CB  1 
ATOM   652  C CG  . ASN   A 1 85  ? 24.99804 -16.02153 15.04793  1.000 40.12370 ? 84  ASN   A CG  1 
ATOM   653  O OD1 . ASN   A 1 85  ? 26.06558 -15.81608 15.62934  1.000 38.72616 ? 84  ASN   A OD1 1 
ATOM   654  N ND2 . ASN   A 1 85  ? 24.93886 -16.41800 13.78244  1.000 42.04074 ? 84  ASN   A ND2 1 
ATOM   655  N N   . CYS   A 1 86  ? 21.38479 -15.59728 17.27550  1.000 36.56550 ? 85  CYS   A N   1 
ATOM   656  C CA  . CYS   A 1 86  ? 20.12448 -15.28727 17.93795  1.000 37.02192 ? 85  CYS   A CA  1 
ATOM   657  C C   . CYS   A 1 86  ? 19.00280 -16.26125 17.58720  1.000 36.04246 ? 85  CYS   A C   1 
ATOM   658  O O   . CYS   A 1 86  ? 17.82692 -15.92620 17.77634  1.000 35.66572 ? 85  CYS   A O   1 
ATOM   659  C CB  . CYS   A 1 86  ? 19.69017 -13.86035 17.60478  1.000 35.96480 ? 85  CYS   A CB  1 
ATOM   660  S SG  . CYS   A 1 86  ? 20.78362 -12.59418 18.25911  1.000 41.23916 ? 85  CYS   A SG  1 
ATOM   661  N N   . VAL   A 1 87  ? 19.32912 -17.45921 17.10555  1.000 36.21833 ? 86  VAL   A N   1 
ATOM   662  C CA  . VAL   A 1 87  ? 18.32443 -18.41093 16.64539  1.000 37.18958 ? 86  VAL   A CA  1 
ATOM   663  C C   . VAL   A 1 87  ? 18.56749 -19.76287 17.30270  1.000 38.58843 ? 86  VAL   A C   1 
ATOM   664  O O   . VAL   A 1 87  ? 19.70268 -20.24898 17.34207  1.000 38.62724 ? 86  VAL   A O   1 
ATOM   665  C CB  . VAL   A 1 87  ? 18.32912 -18.54021 15.10840  1.000 38.42677 ? 86  VAL   A CB  1 
ATOM   666  C CG1 . VAL   A 1 87  ? 17.76564 -19.88348 14.67322  1.000 38.52373 ? 86  VAL   A CG1 1 
ATOM   667  C CG2 . VAL   A 1 87  ? 17.52203 -17.41380 14.48866  1.000 37.03900 ? 86  VAL   A CG2 1 
ATOM   668  N N   . LEU   A 1 88  ? 17.50023 -20.36161 17.82336  1.000 36.47338 ? 87  LEU   A N   1 
ATOM   669  C CA  . LEU   A 1 88  ? 17.51282 -21.73891 18.28526  1.000 37.27005 ? 87  LEU   A CA  1 
ATOM   670  C C   . LEU   A 1 88  ? 17.20476 -22.67363 17.12496  1.000 40.25060 ? 87  LEU   A C   1 
ATOM   671  O O   . LEU   A 1 88  ? 16.32442 -22.39247 16.30257  1.000 37.90994 ? 87  LEU   A O   1 
ATOM   672  C CB  . LEU   A 1 88  ? 16.47880 -21.94339 19.39134  1.000 39.39917 ? 87  LEU   A CB  1 
ATOM   673  C CG  . LEU   A 1 88  ? 16.94812 -22.21718 20.81651  1.000 43.79800 ? 87  LEU   A CG  1 
ATOM   674  C CD1 . LEU   A 1 88  ? 17.90366 -21.13802 21.29830  1.000 41.62060 ? 87  LEU   A CD1 1 
ATOM   675  C CD2 . LEU   A 1 88  ? 15.73983 -22.31353 21.72905  1.000 45.65898 ? 87  LEU   A CD2 1 
ATOM   676  N N   . LYS   A 1 89  ? 17.93114 -23.79026 17.07158  1.000 40.33514 ? 88  LYS   A N   1 
ATOM   677  C CA  . LYS   A 1 89  ? 17.70355 -24.85426 16.10003  1.000 40.49936 ? 88  LYS   A CA  1 
ATOM   678  C C   . LYS   A 1 89  ? 17.39158 -26.12817 16.87363  1.000 41.54539 ? 88  LYS   A C   1 
ATOM   679  O O   . LYS   A 1 89  ? 18.25769 -26.66644 17.57385  1.000 42.66455 ? 88  LYS   A O   1 
ATOM   680  C CB  . LYS   A 1 89  ? 18.91369 -25.04014 15.18398  1.000 39.46905 ? 88  LYS   A CB  1 
ATOM   681  C CG  . LYS   A 1 89  ? 19.27228 -23.79368 14.38962  1.000 40.48876 ? 88  LYS   A CG  1 
ATOM   682  C CD  . LYS   A 1 89  ? 20.28143 -24.09286 13.29294  1.000 42.87966 ? 88  LYS   A CD  1 
ATOM   683  C CE  . LYS   A 1 89  ? 21.61626 -24.53503 13.85665  1.000 43.70918 ? 88  LYS   A CE  1 
ATOM   684  N NZ  . LYS   A 1 89  ? 22.60875 -24.76366 12.77168  1.000 45.71441 ? 88  LYS   A NZ  1 
ATOM   685  N N   . LEU   A 1 90  ? 16.15186 -26.59108 16.76120  1.000 40.47646 ? 89  LEU   A N   1 
ATOM   686  C CA  . LEU   A 1 90  ? 15.68866 -27.80324 17.41967  1.000 41.86024 ? 89  LEU   A CA  1 
ATOM   687  C C   . LEU   A 1 90  ? 15.62149 -28.92459 16.39056  1.000 43.37824 ? 89  LEU   A C   1 
ATOM   688  O O   . LEU   A 1 90  ? 14.89026 -28.81904 15.40061  1.000 42.66937 ? 89  LEU   A O   1 
ATOM   689  C CB  . LEU   A 1 90  ? 14.31607 -27.57759 18.05337  1.000 41.75381 ? 89  LEU   A CB  1 
ATOM   690  C CG  . LEU   A 1 90  ? 14.11273 -26.23811 18.76100  1.000 41.94694 ? 89  LEU   A CG  1 
ATOM   691  C CD1 . LEU   A 1 90  ? 12.63396 -25.97045 18.99111  1.000 41.37844 ? 89  LEU   A CD1 1 
ATOM   692  C CD2 . LEU   A 1 90  ? 14.87427 -26.21124 20.07649  1.000 44.59238 ? 89  LEU   A CD2 1 
ATOM   693  N N   . LYS   A 1 91  ? 16.38745 -29.98505 16.61498  1.000 42.36388 ? 90  LYS   A N   1 
ATOM   694  C CA  . LYS   A 1 91  ? 16.30887 -31.15918 15.76339  1.000 45.63027 ? 90  LYS   A CA  1 
ATOM   695  C C   . LYS   A 1 91  ? 15.11580 -32.00464 16.18392  1.000 48.81698 ? 90  LYS   A C   1 
ATOM   696  O O   . LYS   A 1 91  ? 14.96535 -32.33468 17.36450  1.000 47.05505 ? 90  LYS   A O   1 
ATOM   697  C CB  . LYS   A 1 91  ? 17.59525 -31.97914 15.84819  1.000 46.26335 ? 90  LYS   A CB  1 
ATOM   698  C CG  . LYS   A 1 91  ? 17.75343 -32.96618 14.70352  1.000 48.63953 ? 90  LYS   A CG  1 
ATOM   699  C CD  . LYS   A 1 91  ? 18.78748 -34.03738 15.00105  1.000 51.04667 ? 90  LYS   A CD  1 
ATOM   700  C CE  . LYS   A 1 91  ? 19.11500 -34.82644 13.74100  1.000 54.67372 ? 90  LYS   A CE  1 
ATOM   701  N NZ  . LYS   A 1 91  ? 19.72475 -36.15429 14.03464  1.000 58.85335 ? 90  LYS   A NZ  1 
ATOM   702  N N   . VAL   A 1 92  ? 14.26287 -32.34038 15.22155  1.000 48.75903 ? 91  VAL   A N   1 
ATOM   703  C CA  . VAL   A 1 92  ? 13.11228 -33.19642 15.46233  1.000 49.87156 ? 91  VAL   A CA  1 
ATOM   704  C C   . VAL   A 1 92  ? 13.35204 -34.53993 14.77886  1.000 51.58487 ? 91  VAL   A C   1 
ATOM   705  O O   . VAL   A 1 92  ? 14.26926 -34.70182 13.97469  1.000 52.02731 ? 91  VAL   A O   1 
ATOM   706  C CB  . VAL   A 1 92  ? 11.79586 -32.55083 14.98561  1.000 50.62659 ? 91  VAL   A CB  1 
ATOM   707  C CG1 . VAL   A 1 92  ? 11.48188 -31.31542 15.81323  1.000 48.36185 ? 91  VAL   A CG1 1 
ATOM   708  C CG2 . VAL   A 1 92  ? 11.88175 -32.19694 13.51089  1.000 49.83568 ? 91  VAL   A CG2 1 
ATOM   709  N N   . ASP   A 1 93  ? 12.51076 -35.51579 15.11265  1.000 52.24713 ? 92  ASP   A N   1 
ATOM   710  C CA  . ASP   A 1 93  ? 12.67453 -36.85802 14.57089  1.000 56.36530 ? 92  ASP   A CA  1 
ATOM   711  C C   . ASP   A 1 93  ? 12.02046 -37.03855 13.20694  1.000 56.44264 ? 92  ASP   A C   1 
ATOM   712  O O   . ASP   A 1 93  ? 12.16995 -38.10764 12.60564  1.000 59.23665 ? 92  ASP   A O   1 
ATOM   713  C CB  . ASP   A 1 93  ? 12.11089 -37.89458 15.54939  1.000 57.38769 ? 92  ASP   A CB  1 
ATOM   714  C CG  . ASP   A 1 93  ? 10.61942 -37.72877 15.78730  1.000 61.69945 ? 92  ASP   A CG  1 
ATOM   715  O OD1 . ASP   A 1 93  ? 10.05309 -36.68828 15.38593  1.000 62.98943 ? 92  ASP   A OD1 1 
ATOM   716  O OD2 . ASP   A 1 93  ? 10.01014 -38.64858 16.37501  1.000 63.72609 ? 92  ASP   A OD2 1 
ATOM   717  N N   . THR   A 1 94  ? 11.30935 -36.03302 12.70396  1.000 54.32577 ? 93  THR   A N   1 
ATOM   718  C CA  . THR   A 1 94  ? 10.55039 -36.15821 11.46792  1.000 53.15368 ? 93  THR   A CA  1 
ATOM   719  C C   . THR   A 1 94  ? 10.93737 -35.04276 10.51133  1.000 51.45917 ? 93  THR   A C   1 
ATOM   720  O O   . THR   A 1 94  ? 10.92761 -33.86588 10.88685  1.000 48.44597 ? 93  THR   A O   1 
ATOM   721  C CB  . THR   A 1 94  ? 9.04189  -36.11618 11.73933  1.000 54.51477 ? 93  THR   A CB  1 
ATOM   722  O OG1 . THR   A 1 94  ? 8.67173  -37.23388 12.55604  1.000 58.26081 ? 93  THR   A OG1 1 
ATOM   723  C CG2 . THR   A 1 94  ? 8.25869  -36.16378 10.43232  1.000 54.58122 ? 93  THR   A CG2 1 
ATOM   724  N N   . ALA   A 1 95  ? 11.28317 -35.41641 9.28251   1.000 52.02467 ? 94  ALA   A N   1 
ATOM   725  C CA  . ALA   A 1 95  ? 11.49293 -34.44010 8.22542   1.000 47.79973 ? 94  ALA   A CA  1 
ATOM   726  C C   . ALA   A 1 95  ? 10.14520 -33.92021 7.74335   1.000 47.06000 ? 94  ALA   A C   1 
ATOM   727  O O   . ALA   A 1 95  ? 9.22072  -34.70288 7.50057   1.000 47.43868 ? 94  ALA   A O   1 
ATOM   728  C CB  . ALA   A 1 95  ? 12.27164 -35.06176 7.06612   1.000 47.40323 ? 94  ALA   A CB  1 
ATOM   729  N N   . ASN   A 1 96  ? 10.03121 -32.60520 7.62013   1.000 46.32232 ? 95  ASN   A N   1 
ATOM   730  C CA  . ASN   A 1 96  ? 8.79926  -31.99402 7.13912   1.000 46.19717 ? 95  ASN   A CA  1 
ATOM   731  C C   . ASN   A 1 96  ? 8.49539  -32.49039 5.72987   1.000 45.74838 ? 95  ASN   A C   1 
ATOM   732  O O   . ASN   A 1 96  ? 9.30391  -32.26800 4.81584   1.000 44.74755 ? 95  ASN   A O   1 
ATOM   733  C CB  . ASN   A 1 96  ? 8.92321  -30.46972 7.16236   1.000 45.11134 ? 95  ASN   A CB  1 
ATOM   734  C CG  . ASN   A 1 96  ? 7.65266  -29.75845 6.70720   1.000 45.46344 ? 95  ASN   A CG  1 
ATOM   735  O OD1 . ASN   A 1 96  ? 6.63484  -30.38641 6.41031   1.000 44.79915 ? 95  ASN   A OD1 1 
ATOM   736  N ND2 . ASN   A 1 96  ? 7.70954  -28.43168 6.66530   1.000 44.15880 ? 95  ASN   A ND2 1 
ATOM   737  N N   . PRO   A 1 97  ? 7.36425  -33.16431 5.50840   1.000 47.54199 ? 96  PRO   A N   1 
ATOM   738  C CA  . PRO   A 1 97  ? 7.04929  -33.63649 4.15050   1.000 46.66624 ? 96  PRO   A CA  1 
ATOM   739  C C   . PRO   A 1 97  ? 6.82257  -32.51006 3.16284   1.000 47.58273 ? 96  PRO   A C   1 
ATOM   740  O O   . PRO   A 1 97  ? 6.86637  -32.74861 1.94931   1.000 47.48884 ? 96  PRO   A O   1 
ATOM   741  C CB  . PRO   A 1 97  ? 5.77220  -34.46749 4.35008   1.000 48.26704 ? 96  PRO   A CB  1 
ATOM   742  C CG  . PRO   A 1 97  ? 5.69753  -34.73952 5.82552   1.000 50.33684 ? 96  PRO   A CG  1 
ATOM   743  C CD  . PRO   A 1 97  ? 6.34019  -33.56530 6.48664   1.000 47.05687 ? 96  PRO   A CD  1 
ATOM   744  N N   . LYS   A 1 98  ? 6.58274  -31.29044 3.64235   1.000 46.99027 ? 97  LYS   A N   1 
ATOM   745  C CA  . LYS   A 1 98  ? 6.30803  -30.14378 2.79004   1.000 46.72573 ? 97  LYS   A CA  1 
ATOM   746  C C   . LYS   A 1 98  ? 7.50551  -29.21104 2.66189   1.000 46.15743 ? 97  LYS   A C   1 
ATOM   747  O O   . LYS   A 1 98  ? 7.33461  -28.04419 2.29265   1.000 45.45347 ? 97  LYS   A O   1 
ATOM   748  C CB  . LYS   A 1 98  ? 5.10112  -29.37201 3.32233   1.000 47.89350 ? 97  LYS   A CB  1 
ATOM   749  C CG  . LYS   A 1 98  ? 3.83078  -30.19220 3.44118   1.000 50.11525 ? 97  LYS   A CG  1 
ATOM   750  C CD  . LYS   A 1 98  ? 2.74444  -29.37473 4.11066   1.000 53.61832 ? 97  LYS   A CD  1 
ATOM   751  C CE  . LYS   A 1 98  ? 1.36578  -29.92073 3.80603   1.000 64.80823 ? 97  LYS   A CE  1 
ATOM   752  N NZ  . LYS   A 1 98  ? 0.32580  -28.89381 4.08351   1.000 69.45085 ? 97  LYS   A NZ  1 
ATOM   753  N N   . THR   A 1 99  ? 8.70347  -29.69265 2.96831   1.000 46.82452 ? 98  THR   A N   1 
ATOM   754  C CA  . THR   A 1 99  ? 9.89824  -28.86994 2.85095   1.000 45.49419 ? 98  THR   A CA  1 
ATOM   755  C C   . THR   A 1 99  ? 10.12219 -28.49552 1.39124   1.000 47.49363 ? 98  THR   A C   1 
ATOM   756  O O   . THR   A 1 99  ? 10.26502 -29.39129 0.54444   1.000 45.35850 ? 98  THR   A O   1 
ATOM   757  C CB  . THR   A 1 99  ? 11.12449 -29.60109 3.39318   1.000 45.64919 ? 98  THR   A CB  1 
ATOM   758  O OG1 . THR   A 1 99  ? 10.88290 -30.01463 4.74197   1.000 45.93512 ? 98  THR   A OG1 1 
ATOM   759  C CG2 . THR   A 1 99  ? 12.34088 -28.68913 3.36429   1.000 44.26033 ? 98  THR   A CG2 1 
ATOM   760  N N   . PRO   A 1 100 ? 10.15149 -27.21365 1.05132   1.000 45.96455 ? 99  PRO   A N   1 
ATOM   761  C CA  . PRO   A 1 100 ? 10.38647 -26.80950 -0.33289  1.000 45.93046 ? 99  PRO   A CA  1 
ATOM   762  C C   . PRO   A 1 100 ? 11.88005 -26.70133 -0.61127  1.000 48.43235 ? 99  PRO   A C   1 
ATOM   763  O O   . PRO   A 1 100 ? 12.71571 -26.77310 0.29283   1.000 45.51296 ? 99  PRO   A O   1 
ATOM   764  C CB  . PRO   A 1 100 ? 9.72168  -25.43118 -0.39574  1.000 46.29253 ? 99  PRO   A CB  1 
ATOM   765  C CG  . PRO   A 1 100 ? 9.98408  -24.87016 0.97213   1.000 44.90123 ? 99  PRO   A CG  1 
ATOM   766  C CD  . PRO   A 1 100 ? 9.95086  -26.04877 1.93156   1.000 45.20018 ? 99  PRO   A CD  1 
ATOM   767  N N   . LYS   A 1 101 ? 12.20052 -26.53456 -1.89112  1.000 48.68460 ? 100 LYS   A N   1 
ATOM   768  C CA  . LYS   A 1 101 ? 13.53495 -26.08311 -2.25116  1.000 50.02524 ? 100 LYS   A CA  1 
ATOM   769  C C   . LYS   A 1 101 ? 13.76706 -24.72233 -1.61114  1.000 48.05304 ? 100 LYS   A C   1 
ATOM   770  O O   . LYS   A 1 101 ? 12.99916 -23.78318 -1.84123  1.000 48.08881 ? 100 LYS   A O   1 
ATOM   771  C CB  . LYS   A 1 101 ? 13.67997 -26.00745 -3.77117  1.000 54.73399 ? 100 LYS   A CB  1 
ATOM   772  C CG  . LYS   A 1 101 ? 15.10954 -25.78026 -4.24425  1.000 58.13409 ? 100 LYS   A CG  1 
ATOM   773  C CD  . LYS   A 1 101 ? 15.47764 -26.70422 -5.40056  1.000 61.00437 ? 100 LYS   A CD  1 
ATOM   774  C CE  . LYS   A 1 101 ? 15.11176 -26.10363 -6.74871  1.000 64.69755 ? 100 LYS   A CE  1 
ATOM   775  N NZ  . LYS   A 1 101 ? 15.45503 -27.02191 -7.87351  1.000 64.81197 ? 100 LYS   A NZ  1 
ATOM   776  N N   . TYR   A 1 102 ? 14.79731 -24.61709 -0.77566  1.000 46.12035 ? 101 TYR   A N   1 
ATOM   777  C CA  . TYR   A 1 102 ? 14.97242 -23.40919 0.01380   1.000 45.04240 ? 101 TYR   A CA  1 
ATOM   778  C C   . TYR   A 1 102 ? 16.44204 -23.02906 0.10707   1.000 44.55583 ? 101 TYR   A C   1 
ATOM   779  O O   . TYR   A 1 102 ? 17.33996 -23.86161 -0.03552  1.000 44.20449 ? 101 TYR   A O   1 
ATOM   780  C CB  . TYR   A 1 102 ? 14.37590 -23.56225 1.42324   1.000 43.61841 ? 101 TYR   A CB  1 
ATOM   781  C CG  . TYR   A 1 102 ? 15.15267 -24.46920 2.35681   1.000 44.30418 ? 101 TYR   A CG  1 
ATOM   782  C CD1 . TYR   A 1 102 ? 14.89536 -25.83259 2.40543   1.000 43.58653 ? 101 TYR   A CD1 1 
ATOM   783  C CD2 . TYR   A 1 102 ? 16.13102 -23.95579 3.20547   1.000 43.89535 ? 101 TYR   A CD2 1 
ATOM   784  C CE1 . TYR   A 1 102 ? 15.59527 -26.66184 3.26294   1.000 44.09097 ? 101 TYR   A CE1 1 
ATOM   785  C CE2 . TYR   A 1 102 ? 16.83728 -24.77828 4.06640   1.000 42.43420 ? 101 TYR   A CE2 1 
ATOM   786  C CZ  . TYR   A 1 102 ? 16.56448 -26.12893 4.09081   1.000 43.85663 ? 101 TYR   A CZ  1 
ATOM   787  O OH  . TYR   A 1 102 ? 17.26377 -26.95069 4.94432   1.000 43.01074 ? 101 TYR   A OH  1 
ATOM   788  N N   . LYS   A 1 103 ? 16.66338 -21.73883 0.34857   1.000 45.53271 ? 102 LYS   A N   1 
ATOM   789  C CA  . LYS   A 1 103 ? 17.97325 -21.18084 0.63821   1.000 43.72978 ? 102 LYS   A CA  1 
ATOM   790  C C   . LYS   A 1 103 ? 17.87099 -20.30280 1.87537   1.000 41.88527 ? 102 LYS   A C   1 
ATOM   791  O O   . LYS   A 1 103 ? 16.78644 -19.85722 2.25937   1.000 40.27700 ? 102 LYS   A O   1 
ATOM   792  C CB  . LYS   A 1 103 ? 18.51710 -20.33402 -0.52309  1.000 46.07149 ? 102 LYS   A CB  1 
ATOM   793  C CG  . LYS   A 1 103 ? 19.01353 -21.09529 -1.73500  1.000 50.33529 ? 102 LYS   A CG  1 
ATOM   794  C CD  . LYS   A 1 103 ? 19.32194 -20.10779 -2.85345  1.000 53.59141 ? 102 LYS   A CD  1 
ATOM   795  C CE  . LYS   A 1 103 ? 20.25548 -20.68580 -3.90046  1.000 60.24912 ? 102 LYS   A CE  1 
ATOM   796  N NZ  . LYS   A 1 103 ? 20.72245 -19.62517 -4.83721  1.000 63.66560 ? 102 LYS   A NZ  1 
ATOM   797  N N   . PHE   A 1 104 ? 19.01926 -20.05732 2.49613   1.000 40.94589 ? 103 PHE   A N   1 
ATOM   798  C CA  . PHE   A 1 104 ? 19.16835 -19.01314 3.50072   1.000 40.60741 ? 103 PHE   A CA  1 
ATOM   799  C C   . PHE   A 1 104 ? 19.99954 -17.89874 2.88308   1.000 41.38180 ? 103 PHE   A C   1 
ATOM   800  O O   . PHE   A 1 104 ? 21.15739 -18.11848 2.50966   1.000 39.89695 ? 103 PHE   A O   1 
ATOM   801  C CB  . PHE   A 1 104 ? 19.83226 -19.54002 4.77388   1.000 39.70178 ? 103 PHE   A CB  1 
ATOM   802  C CG  . PHE   A 1 104 ? 18.94202 -20.41492 5.61262   1.000 38.46361 ? 103 PHE   A CG  1 
ATOM   803  C CD1 . PHE   A 1 104 ? 17.58434 -20.50545 5.34986   1.000 38.24449 ? 103 PHE   A CD1 1 
ATOM   804  C CD2 . PHE   A 1 104 ? 19.46603 -21.13993 6.67334   1.000 36.60099 ? 103 PHE   A CD2 1 
ATOM   805  C CE1 . PHE   A 1 104 ? 16.76666 -21.30730 6.12189   1.000 37.24411 ? 103 PHE   A CE1 1 
ATOM   806  C CE2 . PHE   A 1 104 ? 18.65409 -21.94261 7.45023   1.000 38.38382 ? 103 PHE   A CE2 1 
ATOM   807  C CZ  . PHE   A 1 104 ? 17.30083 -22.02644 7.17502   1.000 38.19854 ? 103 PHE   A CZ  1 
ATOM   808  N N   . VAL   A 1 105 ? 19.40657 -16.71527 2.76192   1.000 39.66226 ? 104 VAL   A N   1 
ATOM   809  C CA  . VAL   A 1 105 ? 20.05292 -15.57320 2.13027   1.000 40.85424 ? 104 VAL   A CA  1 
ATOM   810  C C   . VAL   A 1 105 ? 19.98548 -14.38841 3.07998   1.000 40.92367 ? 104 VAL   A C   1 
ATOM   811  O O   . VAL   A 1 105 ? 18.95533 -14.14995 3.71918   1.000 38.99623 ? 104 VAL   A O   1 
ATOM   812  C CB  . VAL   A 1 105 ? 19.39597 -15.21813 0.77768   1.000 41.83412 ? 104 VAL   A CB  1 
ATOM   813  C CG1 . VAL   A 1 105 ? 20.09483 -14.02344 0.13842   1.000 42.74018 ? 104 VAL   A CG1 1 
ATOM   814  C CG2 . VAL   A 1 105 ? 19.42038 -16.41509 -0.15739  1.000 43.68754 ? 104 VAL   A CG2 1 
ATOM   815  N N   . ARG   A 1 106 ? 21.08536 -13.65169 3.17815   1.000 40.12166 ? 105 ARG   A N   1 
ATOM   816  C CA  . ARG   A 1 106 ? 21.11588 -12.38392 3.89543   1.000 42.57823 ? 105 ARG   A CA  1 
ATOM   817  C C   . ARG   A 1 106 ? 21.00531 -11.27123 2.86133   1.000 43.35902 ? 105 ARG   A C   1 
ATOM   818  O O   . ARG   A 1 106 ? 21.95164 -11.02070 2.10805   1.000 42.92983 ? 105 ARG   A O   1 
ATOM   819  C CB  . ARG   A 1 106 ? 22.39077 -12.24547 4.72347   1.000 42.81781 ? 105 ARG   A CB  1 
ATOM   820  C CG  . ARG   A 1 106 ? 22.41993 -10.99677 5.58497   1.000 42.24426 ? 105 ARG   A CG  1 
ATOM   821  C CD  . ARG   A 1 106 ? 23.66828 -10.94491 6.44457   1.000 42.23443 ? 105 ARG   A CD  1 
ATOM   822  N NE  . ARG   A 1 106 ? 23.70587 -9.73601  7.25768   1.000 43.32262 ? 105 ARG   A NE  1 
ATOM   823  C CZ  . ARG   A 1 106 ? 23.09823 -9.60607  8.42842   1.000 39.05724 ? 105 ARG   A CZ  1 
ATOM   824  N NH1 . ARG   A 1 106 ? 22.39784 -10.59596 8.95548   1.000 37.63400 ? 105 ARG   A NH1 1 
ATOM   825  N NH2 . ARG   A 1 106 ? 23.19420 -8.45369  9.08495   1.000 38.52783 ? 105 ARG   A NH2 1 
ATOM   826  N N   . ILE   A 1 107 ? 19.84811 -10.61258 2.82017   1.000 42.44938 ? 106 ILE   A N   1 
ATOM   827  C CA  . ILE   A 1 107 ? 19.60112 -9.59678  1.80544   1.000 44.24267 ? 106 ILE   A CA  1 
ATOM   828  C C   . ILE   A 1 107 ? 20.31772 -8.30088  2.17123   1.000 45.93765 ? 106 ILE   A C   1 
ATOM   829  O O   . ILE   A 1 107 ? 20.64336 -8.03609  3.33117   1.000 45.60944 ? 106 ILE   A O   1 
ATOM   830  C CB  . ILE   A 1 107 ? 18.09355 -9.35717  1.61629   1.000 43.83806 ? 106 ILE   A CB  1 
ATOM   831  C CG1 . ILE   A 1 107 ? 17.46272 -8.92740  2.94104   1.000 41.25212 ? 106 ILE   A CG1 1 
ATOM   832  C CG2 . ILE   A 1 107 ? 17.42034 -10.60018 1.05830   1.000 41.83602 ? 106 ILE   A CG2 1 
ATOM   833  C CD1 . ILE   A 1 107 ? 16.10491 -8.30187  2.79184   1.000 41.53909 ? 106 ILE   A CD1 1 
ATOM   834  N N   . GLN   A 1 108 ? 20.55217 -7.47919  1.15516   1.000 47.36242 ? 107 GLN   A N   1 
ATOM   835  C CA  . GLN   A 1 108 ? 21.13298 -6.15345  1.28060   1.000 49.71135 ? 107 GLN   A CA  1 
ATOM   836  C C   . GLN   A 1 108 ? 20.04168 -5.11938  1.52144   1.000 47.00213 ? 107 GLN   A C   1 
ATOM   837  O O   . GLN   A 1 108 ? 18.87702 -5.33784  1.17241   1.000 45.39382 ? 107 GLN   A O   1 
ATOM   838  C CB  . GLN   A 1 108 ? 21.91392 -5.80616  0.01374   1.000 50.38958 ? 107 GLN   A CB  1 
ATOM   839  C CG  . GLN   A 1 108 ? 23.12584 -6.68837  -0.23531  1.000 56.17879 ? 107 GLN   A CG  1 
ATOM   840  C CD  . GLN   A 1 108 ? 24.31524 -6.31021  0.62871   1.000 58.26518 ? 107 GLN   A CD  1 
ATOM   841  O OE1 . GLN   A 1 108 ? 24.65519 -7.01362  1.58059   1.000 59.35780 ? 107 GLN   A OE1 1 
ATOM   842  N NE2 . GLN   A 1 108 ? 24.95926 -5.19709  0.29465   1.000 60.05041 ? 107 GLN   A NE2 1 
ATOM   843  N N   . PRO   A 1 109 ? 20.38206 -3.97997  2.12672   1.000 47.55179 ? 108 PRO   A N   1 
ATOM   844  C CA  . PRO   A 1 109 ? 19.38118 -2.92218  2.30784   1.000 46.30240 ? 108 PRO   A CA  1 
ATOM   845  C C   . PRO   A 1 109 ? 18.89574 -2.39173  0.96694   1.000 46.34712 ? 108 PRO   A C   1 
ATOM   846  O O   . PRO   A 1 109 ? 19.65808 -2.28589  0.00270   1.000 47.67106 ? 108 PRO   A O   1 
ATOM   847  C CB  . PRO   A 1 109 ? 20.13508 -1.84835  3.10063   1.000 45.79262 ? 108 PRO   A CB  1 
ATOM   848  C CG  . PRO   A 1 109 ? 21.57701 -2.12104  2.83533   1.000 47.76282 ? 108 PRO   A CG  1 
ATOM   849  C CD  . PRO   A 1 109 ? 21.68058 -3.61092  2.71418   1.000 48.41935 ? 108 PRO   A CD  1 
ATOM   850  N N   . GLY   A 1 110 ? 17.60968 -2.05263  0.91636   1.000 44.38857 ? 109 GLY   A N   1 
ATOM   851  C CA  . GLY   A 1 110 ? 16.95457 -1.65424  -0.30646  1.000 45.18019 ? 109 GLY   A CA  1 
ATOM   852  C C   . GLY   A 1 110 ? 16.23040 -2.77743  -1.01728  1.000 44.64699 ? 109 GLY   A C   1 
ATOM   853  O O   . GLY   A 1 110 ? 15.37589 -2.50468  -1.86784  1.000 46.02887 ? 109 GLY   A O   1 
ATOM   854  N N   . GLN   A 1 111 ? 16.54852 -4.02680  -0.69066  1.000 43.88643 ? 110 GLN   A N   1 
ATOM   855  C CA  . GLN   A 1 111 ? 15.86231 -5.16419  -1.27940  1.000 45.40520 ? 110 GLN   A CA  1 
ATOM   856  C C   . GLN   A 1 111 ? 14.54783 -5.42927  -0.55401  1.000 42.75466 ? 110 GLN   A C   1 
ATOM   857  O O   . GLN   A 1 111 ? 14.35558 -5.04845  0.60366   1.000 41.13245 ? 110 GLN   A O   1 
ATOM   858  C CB  . GLN   A 1 111 ? 16.75004 -6.40850  -1.24353  1.000 45.42872 ? 110 GLN   A CB  1 
ATOM   859  C CG  . GLN   A 1 111 ? 17.95286 -6.32747  -2.16819  1.000 49.66005 ? 110 GLN   A CG  1 
ATOM   860  C CD  . GLN   A 1 111 ? 17.56226 -6.03448  -3.60805  1.000 56.33066 ? 110 GLN   A CD  1 
ATOM   861  O OE1 . GLN   A 1 111 ? 17.17715 -6.93340  -4.35516  1.000 57.77022 ? 110 GLN   A OE1 1 
ATOM   862  N NE2 . GLN   A 1 111 ? 17.65955 -4.76813  -4.00247  1.000 59.59807 ? 110 GLN   A NE2 1 
ATOM   863  N N   . THR   A 1 112 ? 13.63738 -6.09137  -1.25552  1.000 42.13148 ? 111 THR   A N   1 
ATOM   864  C CA  . THR   A 1 112 ? 12.30143 -6.36716  -0.75255  1.000 41.18192 ? 111 THR   A CA  1 
ATOM   865  C C   . THR   A 1 112 ? 12.10897 -7.86537  -0.55876  1.000 38.67796 ? 111 THR   A C   1 
ATOM   866  O O   . THR   A 1 112 ? 12.88735 -8.68928  -1.04694  1.000 39.99160 ? 111 THR   A O   1 
ATOM   867  C CB  . THR   A 1 112 ? 11.23930 -5.81045  -1.70752  1.000 41.96405 ? 111 THR   A CB  1 
ATOM   868  O OG1 . THR   A 1 112 ? 11.49342 -6.29215  -3.03373  1.000 42.29202 ? 111 THR   A OG1 1 
ATOM   869  C CG2 . THR   A 1 112 ? 11.27163 -4.28642  -1.70794  1.000 41.30949 ? 111 THR   A CG2 1 
ATOM   870  N N   . PHE   A 1 113 ? 11.05179 -8.20282  0.17486   1.000 38.71524 ? 112 PHE   A N   1 
ATOM   871  C CA  . PHE   A 1 113 ? 10.68744 -9.58650  0.45217   1.000 37.50229 ? 112 PHE   A CA  1 
ATOM   872  C C   . PHE   A 1 113 ? 9.27912  -9.60477  1.02548   1.000 35.51510 ? 112 PHE   A C   1 
ATOM   873  O O   . PHE   A 1 113 ? 8.77265  -8.58473  1.49594   1.000 37.73286 ? 112 PHE   A O   1 
ATOM   874  C CB  . PHE   A 1 113 ? 11.67384 -10.25301 1.41924   1.000 37.39241 ? 112 PHE   A CB  1 
ATOM   875  C CG  . PHE   A 1 113 ? 11.78385 -9.56494  2.75306   1.000 36.94153 ? 112 PHE   A CG  1 
ATOM   876  C CD1 . PHE   A 1 113 ? 10.97734 -9.94375  3.81641   1.000 36.81368 ? 112 PHE   A CD1 1 
ATOM   877  C CD2 . PHE   A 1 113 ? 12.70288 -8.54647  2.94763   1.000 37.99509 ? 112 PHE   A CD2 1 
ATOM   878  C CE1 . PHE   A 1 113 ? 11.08509 -9.31566  5.05072   1.000 36.62916 ? 112 PHE   A CE1 1 
ATOM   879  C CE2 . PHE   A 1 113 ? 12.81551 -7.91361  4.17904   1.000 40.04785 ? 112 PHE   A CE2 1 
ATOM   880  C CZ  . PHE   A 1 113 ? 12.00185 -8.29832  5.23093   1.000 36.86672 ? 112 PHE   A CZ  1 
ATOM   881  N N   . SER   A 1 114 ? 8.65770  -10.77876 0.99697   1.000 35.60158 ? 113 SER   A N   1 
ATOM   882  C CA  . SER   A 1 114 ? 7.31714  -10.96166 1.53607   1.000 34.76313 ? 113 SER   A CA  1 
ATOM   883  C C   . SER   A 1 114 ? 7.40841  -11.51381 2.95213   1.000 37.75340 ? 113 SER   A C   1 
ATOM   884  O O   . SER   A 1 114 ? 8.16323  -12.45597 3.20740   1.000 37.53344 ? 113 SER   A O   1 
ATOM   885  C CB  . SER   A 1 114 ? 6.49553  -11.90318 0.65459   1.000 35.88714 ? 113 SER   A CB  1 
ATOM   886  O OG  . SER   A 1 114 ? 6.31300  -11.36458 -0.64281  1.000 38.88615 ? 113 SER   A OG  1 
ATOM   887  N N   . VAL   A 1 115 ? 6.64826  -10.91853 3.86485   1.000 36.15825 ? 114 VAL   A N   1 
ATOM   888  C CA  . VAL   A 1 115 ? 6.53854  -11.37026 5.24435   1.000 34.82742 ? 114 VAL   A CA  1 
ATOM   889  C C   . VAL   A 1 115 ? 5.23746  -12.14085 5.38628   1.000 35.74761 ? 114 VAL   A C   1 
ATOM   890  O O   . VAL   A 1 115 ? 4.17383  -11.67052 4.94634   1.000 34.24182 ? 114 VAL   A O   1 
ATOM   891  C CB  . VAL   A 1 115 ? 6.57704  -10.18814 6.22869   1.000 36.27741 ? 114 VAL   A CB  1 
ATOM   892  C CG1 . VAL   A 1 115 ? 6.07466  -10.62125 7.60178   1.000 35.79003 ? 114 VAL   A CG1 1 
ATOM   893  C CG2 . VAL   A 1 115 ? 7.97784  -9.63094  6.33354   1.000 35.12837 ? 114 VAL   A CG2 1 
ATOM   894  N N   . LEU   A 1 116 ? 5.32590  -13.32748 5.99055   1.000 35.06491 ? 115 LEU   A N   1 
ATOM   895  C CA  . LEU   A 1 116 ? 4.15397  -14.12734 6.34352   1.000 35.08449 ? 115 LEU   A CA  1 
ATOM   896  C C   . LEU   A 1 116 ? 3.96268  -14.00595 7.85352   1.000 37.48616 ? 115 LEU   A C   1 
ATOM   897  O O   . LEU   A 1 116 ? 4.58263  -14.72306 8.64007   1.000 37.25092 ? 115 LEU   A O   1 
ATOM   898  C CB  . LEU   A 1 116 ? 4.32952  -15.57613 5.90273   1.000 35.90245 ? 115 LEU   A CB  1 
ATOM   899  C CG  . LEU   A 1 116 ? 3.22585  -16.56196 6.29283   1.000 38.88188 ? 115 LEU   A CG  1 
ATOM   900  C CD1 . LEU   A 1 116 ? 1.88570  -16.15356 5.69837   1.000 37.80607 ? 115 LEU   A CD1 1 
ATOM   901  C CD2 . LEU   A 1 116 ? 3.59928  -17.97456 5.86977   1.000 38.99936 ? 115 LEU   A CD2 1 
ATOM   902  N N   . ALA   A 1 117 ? 3.10451  -13.06961 8.25514   1.000 36.46731 ? 116 ALA   A N   1 
ATOM   903  C CA  . ALA   A 1 117 ? 2.81360  -12.85700 9.66603   1.000 38.11368 ? 116 ALA   A CA  1 
ATOM   904  C C   . ALA   A 1 117 ? 1.97697  -14.00605 10.21109  1.000 39.69803 ? 116 ALA   A C   1 
ATOM   905  O O   . ALA   A 1 117 ? 0.89965  -14.31323 9.67742   1.000 40.59316 ? 116 ALA   A O   1 
ATOM   906  C CB  . ALA   A 1 117 ? 2.08479  -11.53031 9.86741   1.000 38.23731 ? 116 ALA   A CB  1 
ATOM   907  N N   . CYS   A 1 118 ? 2.47994  -14.61799 11.29084  1.000 37.05683 ? 117 CYS   A N   1 
ATOM   908  C CA  . CYS   A 1 118 ? 1.92034  -15.81252 11.90686  1.000 40.14376 ? 117 CYS   A CA  1 
ATOM   909  C C   . CYS   A 1 118 ? 1.74163  -15.60726 13.40688  1.000 41.62310 ? 117 CYS   A C   1 
ATOM   910  O O   . CYS   A 1 118 ? 2.42807  -14.79742 14.03610  1.000 38.54248 ? 117 CYS   A O   1 
ATOM   911  C CB  . CYS   A 1 118 ? 2.81948  -17.03994 11.68405  1.000 40.11618 ? 117 CYS   A CB  1 
ATOM   912  S SG  . CYS   A 1 118 ? 3.08581  -17.51425 9.96759   1.000 42.07383 ? 117 CYS   A SG  1 
ATOM   913  N N   . TYR   A 1 119 ? 0.81017  -16.37305 13.97521  1.000 44.27799 ? 118 TYR   A N   1 
ATOM   914  C CA  . TYR   A 1 119 ? 0.57641  -16.41524 15.41419  1.000 43.10116 ? 118 TYR   A CA  1 
ATOM   915  C C   . TYR   A 1 119 ? 0.21756  -17.84169 15.79926  1.000 44.67290 ? 118 TYR   A C   1 
ATOM   916  O O   . TYR   A 1 119 ? -0.64501 -18.45812 15.16593  1.000 44.93069 ? 118 TYR   A O   1 
ATOM   917  C CB  . TYR   A 1 119 ? -0.53486 -15.44083 15.83467  1.000 42.76226 ? 118 TYR   A CB  1 
ATOM   918  C CG  . TYR   A 1 119 ? -0.19339 -13.99883 15.53402  1.000 44.16666 ? 118 TYR   A CG  1 
ATOM   919  C CD1 . TYR   A 1 119 ? 0.47676  -13.21417 16.46707  1.000 41.51289 ? 118 TYR   A CD1 1 
ATOM   920  C CD2 . TYR   A 1 119 ? -0.51779 -13.42891 14.30655  1.000 42.88425 ? 118 TYR   A CD2 1 
ATOM   921  C CE1 . TYR   A 1 119 ? 0.80362  -11.90240 16.19222  1.000 39.98036 ? 118 TYR   A CE1 1 
ATOM   922  C CE2 . TYR   A 1 119 ? -0.19239 -12.11734 14.02108  1.000 42.68488 ? 118 TYR   A CE2 1 
ATOM   923  C CZ  . TYR   A 1 119 ? 0.46777  -11.35930 14.96723  1.000 42.01323 ? 118 TYR   A CZ  1 
ATOM   924  O OH  . TYR   A 1 119 ? 0.79130  -10.05262 14.68457  1.000 42.65437 ? 118 TYR   A OH  1 
ATOM   925  N N   . ASN   A 1 120 ? 0.89602  -18.36262 16.82431  1.000 43.43929 ? 119 ASN   A N   1 
ATOM   926  C CA  . ASN   A 1 120 ? 0.71623  -19.74192 17.28465  1.000 45.35390 ? 119 ASN   A CA  1 
ATOM   927  C C   . ASN   A 1 120 ? 0.97099  -20.74586 16.16180  1.000 46.25199 ? 119 ASN   A C   1 
ATOM   928  O O   . ASN   A 1 120 ? 0.29656  -21.77259 16.05768  1.000 49.13188 ? 119 ASN   A O   1 
ATOM   929  C CB  . ASN   A 1 120 ? -0.67145 -19.95435 17.89586  1.000 47.45101 ? 119 ASN   A CB  1 
ATOM   930  C CG  . ASN   A 1 120 ? -0.90379 -19.09978 19.12501  1.000 49.36251 ? 119 ASN   A CG  1 
ATOM   931  O OD1 . ASN   A 1 120 ? -0.30751 -19.32767 20.17909  1.000 46.59536 ? 119 ASN   A OD1 1 
ATOM   932  N ND2 . ASN   A 1 120 ? -1.77839 -18.10961 18.99693  1.000 48.59270 ? 119 ASN   A ND2 1 
ATOM   933  N N   . GLY   A 1 121 ? 1.95197  -20.44720 15.31186  1.000 43.61680 ? 120 GLY   A N   1 
ATOM   934  C CA  . GLY   A 1 121 ? 2.34563  -21.37142 14.26740  1.000 43.65744 ? 120 GLY   A CA  1 
ATOM   935  C C   . GLY   A 1 121 ? 1.39507  -21.49207 13.09838  1.000 45.68849 ? 120 GLY   A C   1 
ATOM   936  O O   . GLY   A 1 121 ? 1.60471  -22.35553 12.24051  1.000 46.52731 ? 120 GLY   A O   1 
ATOM   937  N N   . SER   A 1 122 ? 0.35221  -20.66368 13.03373  1.000 45.03525 ? 121 SER   A N   1 
ATOM   938  C CA  . SER   A 1 122 ? -0.55485 -20.68547 11.90038  1.000 46.25524 ? 121 SER   A CA  1 
ATOM   939  C C   . SER   A 1 122 ? -0.55910 -19.32980 11.20355  1.000 46.68857 ? 121 SER   A C   1 
ATOM   940  O O   . SER   A 1 122 ? -0.49412 -18.29118 11.87024  1.000 43.96892 ? 121 SER   A O   1 
ATOM   941  C CB  . SER   A 1 122 ? -1.98333 -21.04712 12.33433  1.000 47.91153 ? 121 SER   A CB  1 
ATOM   942  O OG  . SER   A 1 122 ? -2.52680 -20.05012 13.17832  1.000 50.57576 ? 121 SER   A OG  1 
ATOM   943  N N   . PRO   A 1 123 ? -0.62641 -19.30607 9.87336   1.000 48.49479 ? 122 PRO   A N   1 
ATOM   944  C CA  . PRO   A 1 123 ? -0.49575 -18.03634 9.14999   1.000 43.37868 ? 122 PRO   A CA  1 
ATOM   945  C C   . PRO   A 1 123 ? -1.67425 -17.10705 9.39201   1.000 43.01550 ? 122 PRO   A C   1 
ATOM   946  O O   . PRO   A 1 123 ? -2.82046 -17.53561 9.54802   1.000 46.01924 ? 122 PRO   A O   1 
ATOM   947  C CB  . PRO   A 1 123 ? -0.42924 -18.46928 7.67962   1.000 44.51514 ? 122 PRO   A CB  1 
ATOM   948  C CG  . PRO   A 1 123 ? -0.04477 -19.92054 7.71615   1.000 49.47734 ? 122 PRO   A CG  1 
ATOM   949  C CD  . PRO   A 1 123 ? -0.68047 -20.45858 8.96004   1.000 47.16085 ? 122 PRO   A CD  1 
ATOM   950  N N   . SER   A 1 124 ? -1.37145 -15.81184 9.41545   1.000 43.07110 ? 123 SER   A N   1 
ATOM   951  C CA  . SER   A 1 124 ? -2.36571 -14.76408 9.59671   1.000 43.69902 ? 123 SER   A CA  1 
ATOM   952  C C   . SER   A 1 124 ? -2.44464 -13.78668 8.43543   1.000 44.03393 ? 123 SER   A C   1 
ATOM   953  O O   . SER   A 1 124 ? -3.53620 -13.29567 8.13738   1.000 41.06592 ? 123 SER   A O   1 
ATOM   954  C CB  . SER   A 1 124 ? -2.08144 -13.97581 10.88417  1.000 44.84049 ? 123 SER   A CB  1 
ATOM   955  O OG  . SER   A 1 124 ? -2.73640 -12.71970 10.86491  1.000 47.72361 ? 123 SER   A OG  1 
ATOM   956  N N   . GLY   A 1 125 ? -1.32835 -13.48144 7.78243   1.000 39.57141 ? 124 GLY   A N   1 
ATOM   957  C CA  . GLY   A 1 125 ? -1.39805 -12.58420 6.63684   1.000 39.14543 ? 124 GLY   A CA  1 
ATOM   958  C C   . GLY   A 1 125 ? -0.07213 -12.50352 5.91670   1.000 39.64648 ? 124 GLY   A C   1 
ATOM   959  O O   . GLY   A 1 125 ? 0.95245  -12.97376 6.41131   1.000 40.14204 ? 124 GLY   A O   1 
ATOM   960  N N   . VAL   A 1 126 ? -0.10208 -11.90498 4.72399   1.000 37.16856 ? 125 VAL   A N   1 
ATOM   961  C CA  . VAL   A 1 126 ? 1.09396  -11.74259 3.90076   1.000 37.39928 ? 125 VAL   A CA  1 
ATOM   962  C C   . VAL   A 1 126 ? 1.18449  -10.30055 3.42058   1.000 36.21203 ? 125 VAL   A C   1 
ATOM   963  O O   . VAL   A 1 126 ? 0.18059  -9.71066  3.00578   1.000 36.04415 ? 125 VAL   A O   1 
ATOM   964  C CB  . VAL   A 1 126 ? 1.10995  -12.70058 2.68913   1.000 38.93465 ? 125 VAL   A CB  1 
ATOM   965  C CG1 . VAL   A 1 126 ? 2.53745  -12.88233 2.18810   1.000 36.20420 ? 125 VAL   A CG1 1 
ATOM   966  C CG2 . VAL   A 1 126 ? 0.48074  -14.04025 3.03601   1.000 40.62654 ? 125 VAL   A CG2 1 
ATOM   967  N N   . TYR   A 1 127 ? 2.39170  -9.73644  3.46335   1.000 36.29267 ? 126 TYR   A N   1 
ATOM   968  C CA  . TYR   A 1 127 ? 2.57966  -8.37927  2.95303   1.000 36.76185 ? 126 TYR   A CA  1 
ATOM   969  C C   . TYR   A 1 127 ? 4.03543  -8.17280  2.55938   1.000 36.86941 ? 126 TYR   A C   1 
ATOM   970  O O   . TYR   A 1 127 ? 4.92833  -8.86139  3.04662   1.000 33.29673 ? 126 TYR   A O   1 
ATOM   971  C CB  . TYR   A 1 127 ? 2.14367  -7.32099  3.97596   1.000 38.92342 ? 126 TYR   A CB  1 
ATOM   972  C CG  . TYR   A 1 127 ? 2.74722  -7.50561  5.34874   1.000 39.37589 ? 126 TYR   A CG  1 
ATOM   973  C CD1 . TYR   A 1 127 ? 4.00468  -6.99995  5.65232   1.000 38.92473 ? 126 TYR   A CD1 1 
ATOM   974  C CD2 . TYR   A 1 127 ? 2.05898  -8.18714  6.34153   1.000 38.89784 ? 126 TYR   A CD2 1 
ATOM   975  C CE1 . TYR   A 1 127 ? 4.55902  -7.17262  6.90522   1.000 40.32589 ? 126 TYR   A CE1 1 
ATOM   976  C CE2 . TYR   A 1 127 ? 2.60663  -8.36409  7.59632   1.000 39.81296 ? 126 TYR   A CE2 1 
ATOM   977  C CZ  . TYR   A 1 127 ? 3.85613  -7.85439  7.87239   1.000 38.53546 ? 126 TYR   A CZ  1 
ATOM   978  O OH  . TYR   A 1 127 ? 4.40333  -8.02776  9.12210   1.000 38.44864 ? 126 TYR   A OH  1 
ATOM   979  N N   . GLN   A 1 128 ? 4.26735  -7.18819  1.69418   1.000 37.13580 ? 127 GLN   A N   1 
ATOM   980  C CA  . GLN   A 1 128 ? 5.58975  -6.93000  1.13370   1.000 37.99050 ? 127 GLN   A CA  1 
ATOM   981  C C   . GLN   A 1 128 ? 6.30889  -5.84685  1.93328   1.000 40.12596 ? 127 GLN   A C   1 
ATOM   982  O O   . GLN   A 1 128 ? 5.71876  -4.81052  2.25628   1.000 42.99165 ? 127 GLN   A O   1 
ATOM   983  C CB  . GLN   A 1 128 ? 5.47675  -6.51977  -0.33651  1.000 40.28308 ? 127 GLN   A CB  1 
ATOM   984  C CG  . GLN   A 1 128 ? 6.79489  -6.52766  -1.10125  1.000 40.72721 ? 127 GLN   A CG  1 
ATOM   985  C CD  . GLN   A 1 128 ? 7.22145  -7.91921  -1.53647  1.000 39.90937 ? 127 GLN   A CD  1 
ATOM   986  O OE1 . GLN   A 1 128 ? 6.57446  -8.91408  -1.20749  1.000 36.04704 ? 127 GLN   A OE1 1 
ATOM   987  N NE2 . GLN   A 1 128 ? 8.31456  -7.99304  -2.28850  1.000 41.27660 ? 127 GLN   A NE2 1 
ATOM   988  N N   . CYS   A 1 129 ? 7.58380  -6.08802  2.24313   1.000 38.73219 ? 128 CYS   A N   1 
ATOM   989  C CA  . CYS   A 1 129 ? 8.41229  -5.17238  3.01451   1.000 40.48028 ? 128 CYS   A CA  1 
ATOM   990  C C   . CYS   A 1 129 ? 9.74256  -4.96169  2.30769   1.000 40.24678 ? 128 CYS   A C   1 
ATOM   991  O O   . CYS   A 1 129 ? 10.16391 -5.76598  1.47234   1.000 40.05181 ? 128 CYS   A O   1 
ATOM   992  C CB  . CYS   A 1 129 ? 8.68323  -5.69663  4.43366   1.000 38.33978 ? 128 CYS   A CB  1 
ATOM   993  S SG  . CYS   A 1 129 ? 7.28808  -5.59008  5.56226   1.000 46.58316 ? 128 CYS   A SG  1 
ATOM   994  N N   . ALA   A 1 130 ? 10.40473 -3.86479  2.66210   1.000 39.15390 ? 129 ALA   A N   1 
ATOM   995  C CA  . ALA   A 1 130 ? 11.75603 -3.57884  2.21072   1.000 41.50962 ? 129 ALA   A CA  1 
ATOM   996  C C   . ALA   A 1 130 ? 12.67504 -3.46270  3.41818   1.000 40.98600 ? 129 ALA   A C   1 
ATOM   997  O O   . ALA   A 1 130 ? 12.26694 -2.99397  4.48459   1.000 39.21607 ? 129 ALA   A O   1 
ATOM   998  C CB  . ALA   A 1 130 ? 11.81246 -2.28731  1.38359   1.000 39.88839 ? 129 ALA   A CB  1 
ATOM   999  N N   . MET   A 1 131 ? 13.91689 -3.90960  3.24884   1.000 38.74559 ? 130 MET   A N   1 
ATOM   1000 C CA  . MET   A 1 131 ? 14.94346 -3.72575  4.27183   1.000 40.52063 ? 130 MET   A CA  1 
ATOM   1001 C C   . MET   A 1 131 ? 15.44647 -2.29304  4.16490   1.000 41.04043 ? 130 MET   A C   1 
ATOM   1002 O O   . MET   A 1 131 ? 16.20845 -1.95756  3.25458   1.000 43.51344 ? 130 MET   A O   1 
ATOM   1003 C CB  . MET   A 1 131 ? 16.07365 -4.73272  4.09275   1.000 40.90061 ? 130 MET   A CB  1 
ATOM   1004 C CG  . MET   A 1 131 ? 17.17896 -4.62928  5.13195   1.000 42.66416 ? 130 MET   A CG  1 
ATOM   1005 S SD  . MET   A 1 131 ? 16.60887 -4.97549  6.81173   1.000 43.16575 ? 130 MET   A SD  1 
ATOM   1006 C CE  . MET   A 1 131 ? 15.76551 -6.53579  6.56133   1.000 38.79098 ? 130 MET   A CE  1 
ATOM   1007 N N   . ARG   A 1 132 ? 15.00461 -1.43640  5.09193   1.000 40.62843 ? 131 ARG   A N   1 
ATOM   1008 C CA  . ARG   A 1 132 ? 15.36081 -0.02681  5.04870   1.000 41.48801 ? 131 ARG   A CA  1 
ATOM   1009 C C   . ARG   A 1 132 ? 16.87824 0.14253   5.12339   1.000 42.80633 ? 131 ARG   A C   1 
ATOM   1010 O O   . ARG   A 1 132 ? 17.59070 -0.74598  5.59638   1.000 40.87181 ? 131 ARG   A O   1 
ATOM   1011 C CB  . ARG   A 1 132 ? 14.69657 0.73300   6.19851   1.000 42.95119 ? 131 ARG   A CB  1 
ATOM   1012 C CG  . ARG   A 1 132 ? 13.19506 0.50688   6.35803   1.000 44.85397 ? 131 ARG   A CG  1 
ATOM   1013 C CD  . ARG   A 1 132 ? 12.40910 1.02020   5.17343   1.000 44.75475 ? 131 ARG   A CD  1 
ATOM   1014 N NE  . ARG   A 1 132 ? 12.68370 2.42539   4.90621   1.000 46.64741 ? 131 ARG   A NE  1 
ATOM   1015 C CZ  . ARG   A 1 132 ? 12.29403 3.06151   3.81108   1.000 45.76074 ? 131 ARG   A CZ  1 
ATOM   1016 N NH1 . ARG   A 1 132 ? 11.59869 2.44764   2.86819   1.000 43.08063 ? 131 ARG   A NH1 1 
ATOM   1017 N NH2 . ARG   A 1 132 ? 12.61562 4.34235   3.65524   1.000 46.15905 ? 131 ARG   A NH2 1 
ATOM   1018 N N   . PRO   A 1 133 ? 17.39612 1.27315   4.63733   1.000 43.14384 ? 132 PRO   A N   1 
ATOM   1019 C CA  . PRO   A 1 133 ? 18.83244 1.54883   4.80614   1.000 44.63148 ? 132 PRO   A CA  1 
ATOM   1020 C C   . PRO   A 1 133 ? 19.30952 1.49243   6.25073   1.000 43.97604 ? 132 PRO   A C   1 
ATOM   1021 O O   . PRO   A 1 133 ? 20.49826 1.24052   6.48573   1.000 42.57396 ? 132 PRO   A O   1 
ATOM   1022 C CB  . PRO   A 1 133 ? 18.97852 2.95465   4.21227   1.000 49.71676 ? 132 PRO   A CB  1 
ATOM   1023 C CG  . PRO   A 1 133 ? 17.92278 3.00614   3.16294   1.000 48.35081 ? 132 PRO   A CG  1 
ATOM   1024 C CD  . PRO   A 1 133 ? 16.76178 2.20743   3.69026   1.000 44.74328 ? 132 PRO   A CD  1 
ATOM   1025 N N   . ASN   A 1 134 ? 18.42853 1.71529   7.22830   1.000 42.28578 ? 133 ASN   A N   1 
ATOM   1026 C CA  . ASN   A 1 134 ? 18.78980 1.58327   8.63415   1.000 42.24676 ? 133 ASN   A CA  1 
ATOM   1027 C C   . ASN   A 1 134 ? 18.50560 0.18671   9.18161   1.000 40.30953 ? 133 ASN   A C   1 
ATOM   1028 O O   . ASN   A 1 134 ? 18.46917 0.00373   10.40360  1.000 42.52937 ? 133 ASN   A O   1 
ATOM   1029 C CB  . ASN   A 1 134 ? 18.07694 2.65199   9.47123   1.000 42.59490 ? 133 ASN   A CB  1 
ATOM   1030 C CG  . ASN   A 1 134 ? 16.57720 2.41385   9.59651   1.000 44.78721 ? 133 ASN   A CG  1 
ATOM   1031 O OD1 . ASN   A 1 134 ? 16.01061 1.53746   8.94449   1.000 41.92206 ? 133 ASN   A OD1 1 
ATOM   1032 N ND2 . ASN   A 1 134 ? 15.92648 3.21218   10.43621  1.000 45.62971 ? 133 ASN   A ND2 1 
ATOM   1033 N N   . PHE   A 1 135 ? 18.28042 -0.78762  8.29797   1.000 40.45560 ? 134 PHE   A N   1 
ATOM   1034 C CA  . PHE   A 1 135 ? 18.14218 -2.20086  8.65784   1.000 40.16977 ? 134 PHE   A CA  1 
ATOM   1035 C C   . PHE   A 1 135 ? 16.93670 -2.46619  9.55654   1.000 39.00555 ? 134 PHE   A C   1 
ATOM   1036 O O   . PHE   A 1 135 ? 16.95854 -3.37634  10.38817  1.000 39.79707 ? 134 PHE   A O   1 
ATOM   1037 C CB  . PHE   A 1 135 ? 19.41941 -2.73581  9.30675   1.000 39.31550 ? 134 PHE   A CB  1 
ATOM   1038 C CG  . PHE   A 1 135 ? 20.57507 -2.84413  8.35614   1.000 41.05336 ? 134 PHE   A CG  1 
ATOM   1039 C CD1 . PHE   A 1 135 ? 21.56178 -1.87292  8.32883   1.000 40.71227 ? 134 PHE   A CD1 1 
ATOM   1040 C CD2 . PHE   A 1 135 ? 20.66657 -3.91238  7.47755   1.000 41.84627 ? 134 PHE   A CD2 1 
ATOM   1041 C CE1 . PHE   A 1 135 ? 22.62485 -1.96955  7.45003   1.000 42.96442 ? 134 PHE   A CE1 1 
ATOM   1042 C CE2 . PHE   A 1 135 ? 21.72665 -4.01593  6.59563   1.000 46.86755 ? 134 PHE   A CE2 1 
ATOM   1043 C CZ  . PHE   A 1 135 ? 22.70791 -3.04241  6.58205   1.000 43.85685 ? 134 PHE   A CZ  1 
ATOM   1044 N N   . THR   A 1 136 ? 15.87459 -1.68728  9.39294   1.000 40.28858 ? 135 THR   A N   1 
ATOM   1045 C CA  . THR   A 1 136 ? 14.58006 -1.97243  9.99535   1.000 39.00805 ? 135 THR   A CA  1 
ATOM   1046 C C   . THR   A 1 136 ? 13.57007 -2.26864  8.89293   1.000 41.04070 ? 135 THR   A C   1 
ATOM   1047 O O   . THR   A 1 136 ? 13.87390 -2.16787  7.70159   1.000 41.66252 ? 135 THR   A O   1 
ATOM   1048 C CB  . THR   A 1 136 ? 14.10921 -0.79934  10.86456  1.000 41.08776 ? 135 THR   A CB  1 
ATOM   1049 O OG1 . THR   A 1 136 ? 13.88131 0.35105   10.04031  1.000 39.99883 ? 135 THR   A OG1 1 
ATOM   1050 C CG2 . THR   A 1 136 ? 15.15984 -0.45938  11.90499  1.000 39.00793 ? 135 THR   A CG2 1 
ATOM   1051 N N   . ILE   A 1 137 ? 12.36121 -2.66408  9.29522   1.000 40.02773 ? 136 ILE   A N   1 
ATOM   1052 C CA  . ILE   A 1 137 ? 11.25600 -2.82922  8.35749   1.000 39.73991 ? 136 ILE   A CA  1 
ATOM   1053 C C   . ILE   A 1 137 ? 10.00093 -2.21580  8.96051   1.000 40.95474 ? 136 ILE   A C   1 
ATOM   1054 O O   . ILE   A 1 137 ? 9.81092  -2.20235  10.18108  1.000 38.44544 ? 136 ILE   A O   1 
ATOM   1055 C CB  . ILE   A 1 137 ? 10.99658 -4.30746  7.96677   1.000 38.87425 ? 136 ILE   A CB  1 
ATOM   1056 C CG1 . ILE   A 1 137 ? 10.44524 -5.10800  9.14759   1.000 38.29375 ? 136 ILE   A CG1 1 
ATOM   1057 C CG2 . ILE   A 1 137 ? 12.25651 -4.96083  7.40995   1.000 39.97917 ? 136 ILE   A CG2 1 
ATOM   1058 C CD1 . ILE   A 1 137 ? 10.05959 -6.53118  8.78080   1.000 36.10240 ? 136 ILE   A CD1 1 
ATOM   1059 N N   . LYS   A 1 138 ? 9.14700  -1.69140  8.08660   1.000 40.47974 ? 137 LYS   A N   1 
ATOM   1060 C CA  . LYS   A 1 138 ? 7.85675  -1.12536  8.47412   1.000 42.66688 ? 137 LYS   A CA  1 
ATOM   1061 C C   . LYS   A 1 138 ? 6.81252  -2.21649  8.26728   1.000 41.28271 ? 137 LYS   A C   1 
ATOM   1062 O O   . LYS   A 1 138 ? 6.21093  -2.33441  7.19994   1.000 42.92780 ? 137 LYS   A O   1 
ATOM   1063 C CB  . LYS   A 1 138 ? 7.54331  0.12205   7.65814   1.000 45.01061 ? 137 LYS   A CB  1 
ATOM   1064 C CG  . LYS   A 1 138 ? 8.48455  1.28548   7.91385   1.000 45.24620 ? 137 LYS   A CG  1 
ATOM   1065 C CD  . LYS   A 1 138 ? 8.18458  2.45144   6.98401   1.000 53.09890 ? 137 LYS   A CD  1 
ATOM   1066 C CE  . LYS   A 1 138 ? 8.82276  3.73304   7.49545   1.000 55.77978 ? 137 LYS   A CE  1 
ATOM   1067 N NZ  . LYS   A 1 138 ? 9.69896  4.37373   6.47763   1.000 53.65255 ? 137 LYS   A NZ  1 
ATOM   1068 N N   . GLY   A 1 139 ? 6.59965  -3.02750  9.30273   1.000 40.97759 ? 138 GLY   A N   1 
ATOM   1069 C CA  . GLY   A 1 139 ? 5.73230  -4.17036  9.22095   1.000 41.57437 ? 138 GLY   A CA  1 
ATOM   1070 C C   . GLY   A 1 139 ? 4.47856  -4.02517  10.05754  1.000 42.18878 ? 138 GLY   A C   1 
ATOM   1071 O O   . GLY   A 1 139 ? 4.07442  -2.92124  10.44566  1.000 43.90629 ? 138 GLY   A O   1 
ATOM   1072 N N   . SER   A 1 140 ? 3.84902  -5.16565  10.33682  1.000 41.75868 ? 139 SER   A N   1 
ATOM   1073 C CA  . SER   A 1 140 ? 2.64854  -5.23657  11.16747  1.000 42.36629 ? 139 SER   A CA  1 
ATOM   1074 C C   . SER   A 1 140 ? 2.79658  -6.47374  12.04698  1.000 41.38524 ? 139 SER   A C   1 
ATOM   1075 O O   . SER   A 1 140 ? 2.46281  -7.58620  11.62663  1.000 39.74719 ? 139 SER   A O   1 
ATOM   1076 C CB  . SER   A 1 140 ? 1.38580  -5.29618  10.31831  1.000 42.87441 ? 139 SER   A CB  1 
ATOM   1077 O OG  . SER   A 1 140 ? 0.23053  -5.43964  11.12518  1.000 45.57973 ? 139 SER   A OG  1 
ATOM   1078 N N   . PHE   A 1 141 ? 3.30946  -6.27745  13.25999  1.000 40.45104 ? 140 PHE   A N   1 
ATOM   1079 C CA  . PHE   A 1 141 ? 3.65514  -7.37407  14.15331  1.000 40.82000 ? 140 PHE   A CA  1 
ATOM   1080 C C   . PHE   A 1 141 ? 3.07973  -7.10819  15.53592  1.000 40.64333 ? 140 PHE   A C   1 
ATOM   1081 O O   . PHE   A 1 141 ? 3.27334  -6.02329  16.09362  1.000 40.02840 ? 140 PHE   A O   1 
ATOM   1082 C CB  . PHE   A 1 141 ? 5.17759  -7.55262  14.24923  1.000 38.52220 ? 140 PHE   A CB  1 
ATOM   1083 C CG  . PHE   A 1 141 ? 5.82325  -8.04323  12.97882  1.000 38.46672 ? 140 PHE   A CG  1 
ATOM   1084 C CD1 . PHE   A 1 141 ? 5.60290  -9.33310  12.52561  1.000 37.48956 ? 140 PHE   A CD1 1 
ATOM   1085 C CD2 . PHE   A 1 141 ? 6.67313  -7.22290  12.25498  1.000 38.58149 ? 140 PHE   A CD2 1 
ATOM   1086 C CE1 . PHE   A 1 141 ? 6.20435  -9.78958  11.36528  1.000 36.52670 ? 140 PHE   A CE1 1 
ATOM   1087 C CE2 . PHE   A 1 141 ? 7.27801  -7.67250  11.09416  1.000 37.37368 ? 140 PHE   A CE2 1 
ATOM   1088 C CZ  . PHE   A 1 141 ? 7.04331  -8.95686  10.64980  1.000 36.66660 ? 140 PHE   A CZ  1 
ATOM   1089 N N   . LEU   A 1 142 ? 2.38511  -8.09752  16.08747  1.000 40.98775 ? 141 LEU   A N   1 
ATOM   1090 C CA  . LEU   A 1 142 ? 1.87710  -8.05212  17.45091  1.000 41.31296 ? 141 LEU   A CA  1 
ATOM   1091 C C   . LEU   A 1 142 ? 2.63498  -9.06321  18.30637  1.000 41.35263 ? 141 LEU   A C   1 
ATOM   1092 O O   . LEU   A 1 142 ? 3.56783  -9.72680  17.84565  1.000 40.17699 ? 141 LEU   A O   1 
ATOM   1093 C CB  . LEU   A 1 142 ? 0.37122  -8.32521  17.47924  1.000 41.00716 ? 141 LEU   A CB  1 
ATOM   1094 C CG  . LEU   A 1 142 ? -0.55177 -7.37238  16.71403  1.000 44.20734 ? 141 LEU   A CG  1 
ATOM   1095 C CD1 . LEU   A 1 142 ? -1.96057 -7.93990  16.65965  1.000 47.72477 ? 141 LEU   A CD1 1 
ATOM   1096 C CD2 . LEU   A 1 142 ? -0.55992 -5.98425  17.33841  1.000 43.14525 ? 141 LEU   A CD2 1 
ATOM   1097 N N   . ASN   A 1 143 ? 2.22619  -9.17666  19.56921  1.000 42.66782 ? 142 ASN   A N   1 
ATOM   1098 C CA  . ASN   A 1 143 ? 2.82708  -10.16645 20.45331  1.000 42.98601 ? 142 ASN   A CA  1 
ATOM   1099 C C   . ASN   A 1 143 ? 2.54685  -11.57202 19.93920  1.000 40.96244 ? 142 ASN   A C   1 
ATOM   1100 O O   . ASN   A 1 143 ? 1.44138  -11.87771 19.48402  1.000 37.89729 ? 142 ASN   A O   1 
ATOM   1101 C CB  . ASN   A 1 143 ? 2.29781  -10.00724 21.88126  1.000 43.97182 ? 142 ASN   A CB  1 
ATOM   1102 C CG  . ASN   A 1 143 ? 3.23162  -9.19692  22.75925  1.000 51.25899 ? 142 ASN   A CG  1 
ATOM   1103 O OD1 . ASN   A 1 143 ? 2.92126  -8.06868  23.14209  1.000 59.49607 ? 142 ASN   A OD1 1 
ATOM   1104 N ND2 . ASN   A 1 143 ? 4.38689  -9.77080  23.08228  1.000 49.64628 ? 142 ASN   A ND2 1 
ATOM   1105 N N   . GLY   A 1 144 ? 3.56271  -12.42817 20.00781  1.000 40.61250 ? 143 GLY   A N   1 
ATOM   1106 C CA  . GLY   A 1 144 ? 3.46308  -13.76899 19.47786  1.000 40.56929 ? 143 GLY   A CA  1 
ATOM   1107 C C   . GLY   A 1 144 ? 3.78668  -13.89948 18.00642  1.000 38.39806 ? 143 GLY   A C   1 
ATOM   1108 O O   . GLY   A 1 144 ? 3.74326  -15.01714 17.47722  1.000 38.49099 ? 143 GLY   A O   1 
ATOM   1109 N N   . SER   A 1 145 ? 4.11005  -12.79893 17.32762  1.000 36.43189 ? 144 SER   A N   1 
ATOM   1110 C CA  . SER   A 1 145 ? 4.43989  -12.85344 15.91018  1.000 38.85101 ? 144 SER   A CA  1 
ATOM   1111 C C   . SER   A 1 145 ? 5.89268  -13.22598 15.65088  1.000 37.12102 ? 144 SER   A C   1 
ATOM   1112 O O   . SER   A 1 145 ? 6.24805  -13.48219 14.49580  1.000 34.79967 ? 144 SER   A O   1 
ATOM   1113 C CB  . SER   A 1 145 ? 4.13733  -11.51010 15.24207  1.000 38.02813 ? 144 SER   A CB  1 
ATOM   1114 O OG  . SER   A 1 145 ? 5.03977  -10.51139 15.68245  1.000 36.53449 ? 144 SER   A OG  1 
ATOM   1115 N N   . CYS   A 1 146 ? 6.73459  -13.26053 16.68139  1.000 33.87672 ? 145 CYS   A N   1 
ATOM   1116 C CA  . CYS   A 1 146 ? 8.13268  -13.61383 16.48102  1.000 34.62127 ? 145 CYS   A CA  1 
ATOM   1117 C C   . CYS   A 1 146 ? 8.24863  -15.02586 15.92049  1.000 34.55298 ? 145 CYS   A C   1 
ATOM   1118 O O   . CYS   A 1 146 ? 7.41633  -15.89655 16.18754  1.000 35.28944 ? 145 CYS   A O   1 
ATOM   1119 C CB  . CYS   A 1 146 ? 8.90647  -13.49271 17.79207  1.000 35.37912 ? 145 CYS   A CB  1 
ATOM   1120 S SG  . CYS   A 1 146 ? 9.13189  -11.78751 18.33224  1.000 38.71749 ? 145 CYS   A SG  1 
ATOM   1121 N N   . GLY   A 1 147 ? 9.29228  -15.24550 15.12380  1.000 34.67257 ? 146 GLY   A N   1 
ATOM   1122 C CA  . GLY   A 1 147 ? 9.42258  -16.45492 14.34833  1.000 35.55992 ? 146 GLY   A CA  1 
ATOM   1123 C C   . GLY   A 1 147 ? 8.79589  -16.38979 12.97120  1.000 35.46069 ? 146 GLY   A C   1 
ATOM   1124 O O   . GLY   A 1 147 ? 9.09776  -17.24207 12.12728  1.000 33.47369 ? 146 GLY   A O   1 
ATOM   1125 N N   . SER   A 1 148 ? 7.91587  -15.41943 12.72817  1.000 36.40084 ? 147 SER   A N   1 
ATOM   1126 C CA  . SER   A 1 148 ? 7.43035  -15.17398 11.37859  1.000 33.45524 ? 147 SER   A CA  1 
ATOM   1127 C C   . SER   A 1 148 ? 8.60578  -14.83979 10.47210  1.000 36.30370 ? 147 SER   A C   1 
ATOM   1128 O O   . SER   A 1 148 ? 9.60009  -14.25211 10.90702  1.000 36.53084 ? 147 SER   A O   1 
ATOM   1129 C CB  . SER   A 1 148 ? 6.42212  -14.02687 11.37049  1.000 33.64566 ? 147 SER   A CB  1 
ATOM   1130 O OG  . SER   A 1 148 ? 5.32377  -14.30817 12.21524  1.000 34.25303 ? 147 SER   A OG  1 
ATOM   1131 N N   . VAL   A 1 149 ? 8.49142  -15.21382 9.19794   1.000 33.68054 ? 148 VAL   A N   1 
ATOM   1132 C CA  . VAL   A 1 149 ? 9.62800  -15.12605 8.29572   1.000 35.07486 ? 148 VAL   A CA  1 
ATOM   1133 C C   . VAL   A 1 149 ? 9.31162  -14.24474 7.09340   1.000 36.27552 ? 148 VAL   A C   1 
ATOM   1134 O O   . VAL   A 1 149 ? 8.15677  -14.06775 6.67860   1.000 34.24944 ? 148 VAL   A O   1 
ATOM   1135 C CB  . VAL   A 1 149 ? 10.10563 -16.51611 7.82439   1.000 35.41034 ? 148 VAL   A CB  1 
ATOM   1136 C CG1 . VAL   A 1 149 ? 10.84991 -17.22309 8.94375   1.000 33.51815 ? 148 VAL   A CG1 1 
ATOM   1137 C CG2 . VAL   A 1 149 ? 8.93130  -17.35152 7.34515   1.000 34.96712 ? 148 VAL   A CG2 1 
ATOM   1138 N N   . GLY   A 1 150 ? 10.38714 -13.69364 6.53526   1.000 35.73443 ? 149 GLY   A N   1 
ATOM   1139 C CA  . GLY   A 1 150 ? 10.36145 -13.01492 5.25662   1.000 34.99831 ? 149 GLY   A CA  1 
ATOM   1140 C C   . GLY   A 1 150 ? 11.14148 -13.82915 4.24182   1.000 36.06185 ? 149 GLY   A C   1 
ATOM   1141 O O   . GLY   A 1 150 ? 12.13366 -14.48490 4.57588   1.000 33.47827 ? 149 GLY   A O   1 
ATOM   1142 N N   . PHE   A 1 151 ? 10.69446 -13.77297 2.99270   1.000 34.35548 ? 150 PHE   A N   1 
ATOM   1143 C CA  . PHE   A 1 151 ? 11.21282 -14.67331 1.97808   1.000 36.30869 ? 150 PHE   A CA  1 
ATOM   1144 C C   . PHE   A 1 151 ? 11.00861 -14.06785 0.59807   1.000 37.86538 ? 150 PHE   A C   1 
ATOM   1145 O O   . PHE   A 1 151 ? 10.20238 -13.15371 0.40445   1.000 34.74368 ? 150 PHE   A O   1 
ATOM   1146 C CB  . PHE   A 1 151 ? 10.53459 -16.04486 2.06698   1.000 35.44977 ? 150 PHE   A CB  1 
ATOM   1147 C CG  . PHE   A 1 151 ? 9.04727  -15.99902 1.84392   1.000 38.58076 ? 150 PHE   A CG  1 
ATOM   1148 C CD1 . PHE   A 1 151 ? 8.18803  -15.66084 2.87777   1.000 37.22639 ? 150 PHE   A CD1 1 
ATOM   1149 C CD2 . PHE   A 1 151 ? 8.50901  -16.28794 0.59852   1.000 37.34750 ? 150 PHE   A CD2 1 
ATOM   1150 C CE1 . PHE   A 1 151 ? 6.81861  -15.61045 2.67699   1.000 36.76677 ? 150 PHE   A CE1 1 
ATOM   1151 C CE2 . PHE   A 1 151 ? 7.13815  -16.24091 0.39008   1.000 41.16709 ? 150 PHE   A CE2 1 
ATOM   1152 C CZ  . PHE   A 1 151 ? 6.29299  -15.90160 1.43327   1.000 39.92586 ? 150 PHE   A CZ  1 
ATOM   1153 N N   . ASN   A 1 152 ? 11.77470 -14.58559 -0.35230  1.000 38.43393 ? 151 ASN   A N   1 
ATOM   1154 C CA  . ASN   A 1 152 ? 11.53007 -14.39658 -1.77221  1.000 40.48786 ? 151 ASN   A CA  1 
ATOM   1155 C C   . ASN   A 1 152 ? 11.37911 -15.76517 -2.41782  1.000 43.27204 ? 151 ASN   A C   1 
ATOM   1156 O O   . ASN   A 1 152 ? 11.68700 -16.79489 -1.81571  1.000 43.18633 ? 151 ASN   A O   1 
ATOM   1157 C CB  . ASN   A 1 152 ? 12.66132 -13.60223 -2.43735  1.000 40.72347 ? 151 ASN   A CB  1 
ATOM   1158 C CG  . ASN   A 1 152 ? 12.67403 -12.14851 -2.01623  1.000 41.48643 ? 151 ASN   A CG  1 
ATOM   1159 O OD1 . ASN   A 1 152 ? 12.01497 -11.30790 -2.62720  1.000 44.28666 ? 151 ASN   A OD1 1 
ATOM   1160 N ND2 . ASN   A 1 152 ? 13.42288 -11.84420 -0.96372  1.000 38.45862 ? 151 ASN   A ND2 1 
ATOM   1161 N N   . ILE   A 1 153 ? 10.89341 -15.77902 -3.65393  1.000 43.27687 ? 152 ILE   A N   1 
ATOM   1162 C CA  . ILE   A 1 153 ? 10.72499 -17.01910 -4.39975  1.000 49.03883 ? 152 ILE   A CA  1 
ATOM   1163 C C   . ILE   A 1 153 ? 11.33329 -16.83876 -5.78108  1.000 52.99590 ? 152 ILE   A C   1 
ATOM   1164 O O   . ILE   A 1 153 ? 11.03309 -15.85932 -6.47186  1.000 51.03411 ? 152 ILE   A O   1 
ATOM   1165 C CB  . ILE   A 1 153 ? 9.24473  -17.43403 -4.49918  1.000 48.75395 ? 152 ILE   A CB  1 
ATOM   1166 C CG1 . ILE   A 1 153 ? 8.72078  -17.82999 -3.11641  1.000 47.80974 ? 152 ILE   A CG1 1 
ATOM   1167 C CG2 . ILE   A 1 153 ? 9.07594  -18.57989 -5.48300  1.000 55.42311 ? 152 ILE   A CG2 1 
ATOM   1168 C CD1 . ILE   A 1 153 ? 7.21525  -17.92874 -3.03552  1.000 47.50340 ? 152 ILE   A CD1 1 
ATOM   1169 N N   . ASP   A 1 154 ? 12.20344 -17.76934 -6.16736  1.000 58.48030 ? 153 ASP   A N   1 
ATOM   1170 C CA  . ASP   A 1 154 ? 12.79948 -17.81720 -7.49995  1.000 63.95300 ? 153 ASP   A CA  1 
ATOM   1171 C C   . ASP   A 1 154 ? 12.33092 -19.11811 -8.14464  1.000 67.09769 ? 153 ASP   A C   1 
ATOM   1172 O O   . ASP   A 1 154 ? 12.86375 -20.19246 -7.84392  1.000 68.43980 ? 153 ASP   A O   1 
ATOM   1173 C CB  . ASP   A 1 154 ? 14.32102 -17.72623 -7.42389  1.000 66.32899 ? 153 ASP   A CB  1 
ATOM   1174 C CG  . ASP   A 1 154 ? 14.98045 -17.84825 -8.78122  1.000 77.32139 ? 153 ASP   A CG  1 
ATOM   1175 O OD1 . ASP   A 1 154 ? 16.08539 -18.42713 -8.85581  1.000 81.72591 ? 153 ASP   A OD1 1 
ATOM   1176 O OD2 . ASP   A 1 154 ? 14.38596 -17.38120 -9.77685  1.000 82.26887 ? 153 ASP   A OD2 1 
ATOM   1177 N N   . TYR   A 1 155 ? 11.33146 -19.00899 -9.02470  1.000 70.14651 ? 154 TYR   A N   1 
ATOM   1178 C CA  . TYR   A 1 155 ? 10.62938 -20.15735 -9.59108  1.000 74.01650 ? 154 TYR   A CA  1 
ATOM   1179 C C   . TYR   A 1 155 ? 10.04456 -21.01913 -8.47774  1.000 73.58722 ? 154 TYR   A C   1 
ATOM   1180 O O   . TYR   A 1 155 ? 8.87996  -20.84857 -8.09964  1.000 71.90882 ? 154 TYR   A O   1 
ATOM   1181 C CB  . TYR   A 1 155 ? 11.55819 -20.98411 -10.48897 1.000 76.48936 ? 154 TYR   A CB  1 
ATOM   1182 C CG  . TYR   A 1 155 ? 10.90956 -22.19165 -11.14629 1.000 80.57809 ? 154 TYR   A CG  1 
ATOM   1183 C CD1 . TYR   A 1 155 ? 9.52484  -22.32831 -11.20493 1.000 81.79479 ? 154 TYR   A CD1 1 
ATOM   1184 C CD2 . TYR   A 1 155 ? 11.68696 -23.19786 -11.70554 1.000 84.09753 ? 154 TYR   A CD2 1 
ATOM   1185 C CE1 . TYR   A 1 155 ? 8.93703  -23.42856 -11.79169 1.000 83.73776 ? 154 TYR   A CE1 1 
ATOM   1186 C CE2 . TYR   A 1 155 ? 11.10347 -24.30512 -12.30241 1.000 85.09846 ? 154 TYR   A CE2 1 
ATOM   1187 C CZ  . TYR   A 1 155 ? 9.72785  -24.41415 -12.34180 1.000 85.48076 ? 154 TYR   A CZ  1 
ATOM   1188 O OH  . TYR   A 1 155 ? 9.14242  -25.51007 -12.93205 1.000 90.15068 ? 154 TYR   A OH  1 
ATOM   1189 N N   . ASP   A 1 156 ? 10.83551 -21.95948 -7.96442  1.000 77.56135 ? 155 ASP   A N   1 
ATOM   1190 C CA  . ASP   A 1 156 ? 10.37694 -22.86740 -6.92465  1.000 74.08678 ? 155 ASP   A CA  1 
ATOM   1191 C C   . ASP   A 1 156 ? 11.24935 -22.84415 -5.67916  1.000 68.71469 ? 155 ASP   A C   1 
ATOM   1192 O O   . ASP   A 1 156 ? 10.93972 -23.55247 -4.71327  1.000 68.30617 ? 155 ASP   A O   1 
ATOM   1193 C CB  . ASP   A 1 156 ? 10.29915 -24.30260 -7.46672  1.000 82.42651 ? 155 ASP   A CB  1 
ATOM   1194 C CG  . ASP   A 1 156 ? 11.64938 -24.83188 -7.91314  1.000 86.94529 ? 155 ASP   A CG  1 
ATOM   1195 O OD1 . ASP   A 1 156 ? 12.50779 -24.01685 -8.31919  1.000 79.66819 ? 155 ASP   A OD1 1 
ATOM   1196 O OD2 . ASP   A 1 156 ? 11.85146 -26.06387 -7.86299  1.000 90.89419 ? 155 ASP   A OD2 1 
ATOM   1197 N N   . CYS   A 1 157 ? 12.32210 -22.05726 -5.66830  1.000 65.17429 ? 156 CYS   A N   1 
ATOM   1198 C CA  . CYS   A 1 157 ? 13.23359 -21.99018 -4.53404  1.000 57.50479 ? 156 CYS   A CA  1 
ATOM   1199 C C   . CYS   A 1 157 ? 12.84384 -20.82347 -3.63496  1.000 52.82292 ? 156 CYS   A C   1 
ATOM   1200 O O   . CYS   A 1 157 ? 12.84894 -19.66706 -4.07601  1.000 51.35491 ? 156 CYS   A O   1 
ATOM   1201 C CB  . CYS   A 1 157 ? 14.68015 -21.84060 -5.00068  1.000 56.59559 ? 156 CYS   A CB  1 
ATOM   1202 S SG  . CYS   A 1 157 ? 15.87465 -21.79326 -3.64245  1.000 52.61669 ? 156 CYS   A SG  1 
ATOM   1203 N N   . VAL   A 1 158 ? 12.51505 -21.12961 -2.38181  1.000 49.61120 ? 157 VAL   A N   1 
ATOM   1204 C CA  . VAL   A 1 158 ? 12.21013 -20.11261 -1.38400  1.000 46.94690 ? 157 VAL   A CA  1 
ATOM   1205 C C   . VAL   A 1 158 ? 13.51318 -19.67427 -0.73265  1.000 43.05823 ? 157 VAL   A C   1 
ATOM   1206 O O   . VAL   A 1 158 ? 14.19654 -20.47726 -0.09109  1.000 41.61099 ? 157 VAL   A O   1 
ATOM   1207 C CB  . VAL   A 1 158 ? 11.22188 -20.64064 -0.33251  1.000 44.11724 ? 157 VAL   A CB  1 
ATOM   1208 C CG1 . VAL   A 1 158 ? 10.94001 -19.56963 0.71452   1.000 40.41025 ? 157 VAL   A CG1 1 
ATOM   1209 C CG2 . VAL   A 1 158 ? 9.93601  -21.10633 -0.99340  1.000 46.28455 ? 157 VAL   A CG2 1 
ATOM   1210 N N   . SER   A 1 159 ? 13.86326 -18.40730 -0.90139  1.000 41.33931 ? 158 SER   A N   1 
ATOM   1211 C CA  . SER   A 1 159 ? 15.01509 -17.81656 -0.22830  1.000 41.81842 ? 158 SER   A CA  1 
ATOM   1212 C C   . SER   A 1 159 ? 14.49952 -17.13475 1.03236   1.000 38.30757 ? 158 SER   A C   1 
ATOM   1213 O O   . SER   A 1 159 ? 13.93758 -16.03773 0.97063   1.000 37.48827 ? 158 SER   A O   1 
ATOM   1214 C CB  . SER   A 1 159 ? 15.74552 -16.83684 -1.13847  1.000 40.14280 ? 158 SER   A CB  1 
ATOM   1215 O OG  . SER   A 1 159 ? 16.47635 -17.52055 -2.14162  1.000 45.02422 ? 158 SER   A OG  1 
ATOM   1216 N N   . PHE   A 1 160 ? 14.66438 -17.80691 2.16966   1.000 38.68869 ? 159 PHE   A N   1 
ATOM   1217 C CA  . PHE   A 1 160 ? 14.34124 -17.20674 3.45660   1.000 36.92229 ? 159 PHE   A CA  1 
ATOM   1218 C C   . PHE   A 1 160 ? 15.41102 -16.18952 3.82409   1.000 35.68794 ? 159 PHE   A C   1 
ATOM   1219 O O   . PHE   A 1 160 ? 16.60720 -16.49785 3.79915   1.000 37.35205 ? 159 PHE   A O   1 
ATOM   1220 C CB  . PHE   A 1 160 ? 14.24820 -18.27809 4.54267   1.000 36.34856 ? 159 PHE   A CB  1 
ATOM   1221 C CG  . PHE   A 1 160 ? 13.12187 -19.25253 4.35046   1.000 35.71642 ? 159 PHE   A CG  1 
ATOM   1222 C CD1 . PHE   A 1 160 ? 11.82223 -18.89770 4.66568   1.000 35.09330 ? 159 PHE   A CD1 1 
ATOM   1223 C CD2 . PHE   A 1 160 ? 13.36661 -20.52995 3.87814   1.000 37.29188 ? 159 PHE   A CD2 1 
ATOM   1224 C CE1 . PHE   A 1 160 ? 10.78613 -19.79216 4.49879   1.000 35.17921 ? 159 PHE   A CE1 1 
ATOM   1225 C CE2 . PHE   A 1 160 ? 12.33361 -21.43047 3.70904   1.000 36.84876 ? 159 PHE   A CE2 1 
ATOM   1226 C CZ  . PHE   A 1 160 ? 11.04232 -21.06062 4.02033   1.000 36.41381 ? 159 PHE   A CZ  1 
ATOM   1227 N N   . CYS   A 1 161 ? 14.98766 -14.97452 4.16963   1.000 34.48961 ? 160 CYS   A N   1 
ATOM   1228 C CA  . CYS   A 1 161 ? 15.93385 -13.91517 4.47217   1.000 34.27169 ? 160 CYS   A CA  1 
ATOM   1229 C C   . CYS   A 1 161 ? 15.70368 -13.22311 5.80684   1.000 36.09048 ? 160 CYS   A C   1 
ATOM   1230 O O   . CYS   A 1 161 ? 16.59496 -12.49391 6.25417   1.000 37.34150 ? 160 CYS   A O   1 
ATOM   1231 C CB  . CYS   A 1 161 ? 15.92162 -12.85385 3.36170   1.000 34.26994 ? 160 CYS   A CB  1 
ATOM   1232 S SG  . CYS   A 1 161 ? 14.32564 -12.04322 3.11717   1.000 37.02911 ? 160 CYS   A SG  1 
ATOM   1233 N N   . TYR   A 1 162 ? 14.56305 -13.42790 6.46170   1.000 34.25713 ? 161 TYR   A N   1 
ATOM   1234 C CA  . TYR   A 1 162 ? 14.23488 -12.64712 7.64469   1.000 34.65041 ? 161 TYR   A CA  1 
ATOM   1235 C C   . TYR   A 1 162 ? 13.46751 -13.49780 8.64602   1.000 35.55239 ? 161 TYR   A C   1 
ATOM   1236 O O   . TYR   A 1 162 ? 12.65175 -14.34054 8.26430   1.000 34.50794 ? 161 TYR   A O   1 
ATOM   1237 C CB  . TYR   A 1 162 ? 13.41596 -11.40508 7.26437   1.000 35.04983 ? 161 TYR   A CB  1 
ATOM   1238 C CG  . TYR   A 1 162 ? 12.98363 -10.54815 8.43501   1.000 36.04371 ? 161 TYR   A CG  1 
ATOM   1239 C CD1 . TYR   A 1 162 ? 13.84468 -9.61184  8.99354   1.000 36.13382 ? 161 TYR   A CD1 1 
ATOM   1240 C CD2 . TYR   A 1 162 ? 11.70702 -10.66273 8.97055   1.000 35.97257 ? 161 TYR   A CD2 1 
ATOM   1241 C CE1 . TYR   A 1 162 ? 13.44805 -8.82092  10.05990  1.000 33.90325 ? 161 TYR   A CE1 1 
ATOM   1242 C CE2 . TYR   A 1 162 ? 11.30378 -9.87824  10.03385  1.000 32.90057 ? 161 TYR   A CE2 1 
ATOM   1243 C CZ  . TYR   A 1 162 ? 12.17467 -8.96093  10.57600  1.000 34.93944 ? 161 TYR   A CZ  1 
ATOM   1244 O OH  . TYR   A 1 162 ? 11.77556 -8.17771  11.63706  1.000 31.57473 ? 161 TYR   A OH  1 
ATOM   1245 N N   . MET   A 1 163 ? 13.74998 -13.27307 9.92771   1.000 33.91946 ? 162 MET   A N   1 
ATOM   1246 C CA  . MET   A 1 163 ? 12.96099 -13.80523 11.02974  1.000 33.85055 ? 162 MET   A CA  1 
ATOM   1247 C C   . MET   A 1 163 ? 12.76387 -12.68364 12.03720  1.000 33.61317 ? 162 MET   A C   1 
ATOM   1248 O O   . MET   A 1 163 ? 13.73056 -12.01762 12.42332  1.000 32.95073 ? 162 MET   A O   1 
ATOM   1249 C CB  . MET   A 1 163 ? 13.63478 -15.01925 11.67994  1.000 33.84024 ? 162 MET   A CB  1 
ATOM   1250 C CG  . MET   A 1 163 ? 12.82224 -15.63949 12.81523  1.000 34.92482 ? 162 MET   A CG  1 
ATOM   1251 S SD  . MET   A 1 163 ? 13.42924 -17.25220 13.35722  1.000 37.80908 ? 162 MET   A SD  1 
ATOM   1252 C CE  . MET   A 1 163 ? 12.42994 -18.35840 12.35882  1.000 35.15823 ? 162 MET   A CE  1 
ATOM   1253 N N   . HIS   A 1 164 ? 11.51628 -12.47369 12.45240  1.000 33.63712 ? 163 HIS   A N   1 
ATOM   1254 C CA  . HIS   A 1 164 ? 11.15605 -11.30428 13.24426  1.000 34.11929 ? 163 HIS   A CA  1 
ATOM   1255 C C   . HIS   A 1 164 ? 11.48184 -11.51240 14.71712  1.000 34.23622 ? 163 HIS   A C   1 
ATOM   1256 O O   . HIS   A 1 164 ? 11.23113 -12.58648 15.27220  1.000 33.52425 ? 163 HIS   A O   1 
ATOM   1257 C CB  . HIS   A 1 164 ? 9.66747  -11.00139 13.08455  1.000 33.35529 ? 163 HIS   A CB  1 
ATOM   1258 C CG  . HIS   A 1 164 ? 9.19807  -9.86013  13.92623  1.000 35.22749 ? 163 HIS   A CG  1 
ATOM   1259 N ND1 . HIS   A 1 164 ? 9.65136  -8.57165  13.74556  1.000 35.46406 ? 163 HIS   A ND1 1 
ATOM   1260 C CD2 . HIS   A 1 164 ? 8.32896  -9.81283  14.96299  1.000 35.67485 ? 163 HIS   A CD2 1 
ATOM   1261 C CE1 . HIS   A 1 164 ? 9.07551  -7.77763  14.62997  1.000 38.01258 ? 163 HIS   A CE1 1 
ATOM   1262 N NE2 . HIS   A 1 164 ? 8.26798  -8.50549  15.37999  1.000 37.46279 ? 163 HIS   A NE2 1 
ATOM   1263 N N   . HIS   A 1 165 ? 12.02104 -10.47116 15.36437  1.000 33.94816 ? 164 HIS   A N   1 
ATOM   1264 C CA  . HIS   A 1 165 ? 12.41529 -10.61474 16.76025  1.000 34.93016 ? 164 HIS   A CA  1 
ATOM   1265 C C   . HIS   A 1 165 ? 11.84696 -9.51794  17.65094  1.000 36.20818 ? 164 HIS   A C   1 
ATOM   1266 O O   . HIS   A 1 165 ? 11.58322 -9.75650  18.83328  1.000 38.18713 ? 164 HIS   A O   1 
ATOM   1267 C CB  . HIS   A 1 165 ? 13.94259 -10.61920 16.89027  1.000 34.77286 ? 164 HIS   A CB  1 
ATOM   1268 C CG  . HIS   A 1 165 ? 14.58181 -11.92038 16.51970  1.000 34.85775 ? 164 HIS   A CG  1 
ATOM   1269 N ND1 . HIS   A 1 165 ? 15.19337 -12.73923 17.44524  1.000 35.10494 ? 164 HIS   A ND1 1 
ATOM   1270 C CD2 . HIS   A 1 165 ? 14.70976 -12.54300 15.32413  1.000 33.48620 ? 164 HIS   A CD2 1 
ATOM   1271 C CE1 . HIS   A 1 165 ? 15.66874 -13.81118 16.83627  1.000 36.77983 ? 164 HIS   A CE1 1 
ATOM   1272 N NE2 . HIS   A 1 165 ? 15.38800 -13.71707 15.54839  1.000 34.60395 ? 164 HIS   A NE2 1 
ATOM   1273 N N   . MET   A 1 166 ? 11.65522 -8.31623  17.11205  1.000 36.19172 ? 165 MET   A N   1 
ATOM   1274 C CA  . MET   A 1 166 ? 11.51919 -7.16718  17.99525  1.000 38.08074 ? 165 MET   A CA  1 
ATOM   1275 C C   . MET   A 1 166 ? 10.89393 -5.98802  17.26207  1.000 39.48494 ? 165 MET   A C   1 
ATOM   1276 O O   . MET   A 1 166 ? 11.08330 -5.81474  16.05550  1.000 36.93556 ? 165 MET   A O   1 
ATOM   1277 C CB  . MET   A 1 166 ? 12.89483 -6.79374  18.56431  1.000 38.93237 ? 165 MET   A CB  1 
ATOM   1278 C CG  . MET   A 1 166 ? 13.01845 -5.41913  19.18706  1.000 42.23902 ? 165 MET   A CG  1 
ATOM   1279 S SD  . MET   A 1 166 ? 14.71511 -5.11904  19.72764  1.000 57.62371 ? 165 MET   A SD  1 
ATOM   1280 C CE  . MET   A 1 166 ? 15.60587 -6.29560  18.71021  1.000 40.09437 ? 165 MET   A CE  1 
ATOM   1281 N N   . GLU   A 1 167 ? 10.14080 -5.18617  18.01315  1.000 39.06663 ? 166 GLU   A N   1 
ATOM   1282 C CA  . GLU   A 1 167 ? 9.64459  -3.89552  17.56003  1.000 41.50588 ? 166 GLU   A CA  1 
ATOM   1283 C C   . GLU   A 1 167 ? 10.38023 -2.78005  18.29076  1.000 43.99939 ? 166 GLU   A C   1 
ATOM   1284 O O   . GLU   A 1 167 ? 10.57096 -2.84407  19.50976  1.000 43.18310 ? 166 GLU   A O   1 
ATOM   1285 C CB  . GLU   A 1 167 ? 8.13836  -3.76557  17.79867  1.000 42.41492 ? 166 GLU   A CB  1 
ATOM   1286 C CG  . GLU   A 1 167 ? 7.61743  -2.34343  17.67013  1.000 44.77198 ? 166 GLU   A CG  1 
ATOM   1287 C CD  . GLU   A 1 167 ? 6.11024  -2.26228  17.78196  1.000 47.13012 ? 166 GLU   A CD  1 
ATOM   1288 O OE1 . GLU   A 1 167 ? 5.42936  -3.22172  17.36119  1.000 46.10996 ? 166 GLU   A OE1 1 
ATOM   1289 O OE2 . GLU   A 1 167 ? 5.60841  -1.24052  18.29552  1.000 49.53668 ? 166 GLU   A OE2 1 
ATOM   1290 N N   . LEU   A 1 168 ? 10.78926 -1.75991  17.54152  1.000 42.86166 ? 167 LEU   A N   1 
ATOM   1291 C CA  . LEU   A 1 168 ? 11.51088 -0.61974  18.08247  1.000 46.57864 ? 167 LEU   A CA  1 
ATOM   1292 C C   . LEU   A 1 168 ? 10.54060 0.44546   18.57742  1.000 49.45158 ? 167 LEU   A C   1 
ATOM   1293 O O   . LEU   A 1 168 ? 9.35635  0.42975   18.22891  1.000 49.60801 ? 167 LEU   A O   1 
ATOM   1294 C CB  . LEU   A 1 168 ? 12.44002 -0.04261  17.01571  1.000 46.65296 ? 167 LEU   A CB  1 
ATOM   1295 C CG  . LEU   A 1 168 ? 13.58886 -0.96663  16.60979  1.000 45.64648 ? 167 LEU   A CG  1 
ATOM   1296 C CD1 . LEU   A 1 168 ? 14.39817 -0.35619  15.48331  1.000 46.36044 ? 167 LEU   A CD1 1 
ATOM   1297 C CD2 . LEU   A 1 168 ? 14.47634 -1.26735  17.80832  1.000 45.70985 ? 167 LEU   A CD2 1 
ATOM   1298 N N   . PRO   A 1 169 ? 11.01132 1.37826   19.41743  1.000 50.68813 ? 168 PRO   A N   1 
ATOM   1299 C CA  . PRO   A 1 169 ? 10.11629 2.44016   19.91428  1.000 51.36314 ? 168 PRO   A CA  1 
ATOM   1300 C C   . PRO   A 1 169 ? 9.37498  3.20415   18.82781  1.000 54.47458 ? 168 PRO   A C   1 
ATOM   1301 O O   . PRO   A 1 169 ? 8.20731  3.56184   19.02699  1.000 56.58568 ? 168 PRO   A O   1 
ATOM   1302 C CB  . PRO   A 1 169 ? 11.07490 3.35023   20.69082  1.000 50.76325 ? 168 PRO   A CB  1 
ATOM   1303 C CG  . PRO   A 1 169 ? 12.11347 2.41949   21.20104  1.000 50.13926 ? 168 PRO   A CG  1 
ATOM   1304 C CD  . PRO   A 1 169 ? 12.30291 1.37673   20.12922  1.000 48.67949 ? 168 PRO   A CD  1 
ATOM   1305 N N   . THR   A 1 170 ? 10.00947 3.46310   17.68254  1.000 50.68266 ? 169 THR   A N   1 
ATOM   1306 C CA  . THR   A 1 170 ? 9.32550  4.17971   16.61041  1.000 51.84002 ? 169 THR   A CA  1 
ATOM   1307 C C   . THR   A 1 170 ? 8.28531  3.32910   15.89347  1.000 49.38943 ? 169 THR   A C   1 
ATOM   1308 O O   . THR   A 1 170 ? 7.69026  3.80570   14.92044  1.000 49.33242 ? 169 THR   A O   1 
ATOM   1309 C CB  . THR   A 1 170 ? 10.33502 4.71015   15.58892  1.000 52.99161 ? 169 THR   A CB  1 
ATOM   1310 O OG1 . THR   A 1 170 ? 11.13861 3.62969   15.10047  1.000 49.54380 ? 169 THR   A OG1 1 
ATOM   1311 C CG2 . THR   A 1 170 ? 11.23049 5.76705   16.21692  1.000 49.32330 ? 169 THR   A CG2 1 
ATOM   1312 N N   . GLY   A 1 171 ? 8.05190  2.09525   16.33290  1.000 49.16695 ? 170 GLY   A N   1 
ATOM   1313 C CA  . GLY   A 1 171 ? 7.05549  1.24832   15.71835  1.000 47.12737 ? 170 GLY   A CA  1 
ATOM   1314 C C   . GLY   A 1 171 ? 7.53374  0.43409   14.53819  1.000 45.20761 ? 170 GLY   A C   1 
ATOM   1315 O O   . GLY   A 1 171 ? 6.75103  -0.35916  14.00098  1.000 43.42569 ? 170 GLY   A O   1 
ATOM   1316 N N   . VAL   A 1 172 ? 8.78220  0.60679   14.10635  1.000 44.03011 ? 171 VAL   A N   1 
ATOM   1317 C CA  . VAL   A 1 172 ? 9.34177  -0.23544  13.05563  1.000 40.93867 ? 171 VAL   A CA  1 
ATOM   1318 C C   . VAL   A 1 172 ? 9.83024  -1.52695  13.69542  1.000 41.72864 ? 171 VAL   A C   1 
ATOM   1319 O O   . VAL   A 1 172 ? 9.78030  -1.68197  14.92108  1.000 41.57644 ? 171 VAL   A O   1 
ATOM   1320 C CB  . VAL   A 1 172 ? 10.46852 0.47815   12.28603  1.000 43.78512 ? 171 VAL   A CB  1 
ATOM   1321 C CG1 . VAL   A 1 172 ? 9.90019  1.62480   11.45787  1.000 43.47554 ? 171 VAL   A CG1 1 
ATOM   1322 C CG2 . VAL   A 1 172 ? 11.53630 0.97858   13.24450  1.000 43.47448 ? 171 VAL   A CG2 1 
ATOM   1323 N N   . HIS   A 1 173 ? 10.30791 -2.46136  12.87986  1.000 40.31642 ? 172 HIS   A N   1 
ATOM   1324 C CA  . HIS   A 1 173 ? 10.56477 -3.81245  13.34845  1.000 39.80425 ? 172 HIS   A CA  1 
ATOM   1325 C C   . HIS   A 1 173 ? 11.97521 -4.25343  12.98236  1.000 37.37727 ? 172 HIS   A C   1 
ATOM   1326 O O   . HIS   A 1 173 ? 12.59992 -3.72321  12.06014  1.000 37.11886 ? 172 HIS   A O   1 
ATOM   1327 C CB  . HIS   A 1 173 ? 9.52100  -4.77771  12.78388  1.000 37.46055 ? 172 HIS   A CB  1 
ATOM   1328 C CG  . HIS   A 1 173 ? 8.11601  -4.39100  13.12593  1.000 39.94092 ? 172 HIS   A CG  1 
ATOM   1329 N ND1 . HIS   A 1 173 ? 7.29242  -3.71732  12.24950  1.000 40.45645 ? 172 HIS   A ND1 1 
ATOM   1330 C CD2 . HIS   A 1 173 ? 7.39974  -4.55641  14.26318  1.000 40.10670 ? 172 HIS   A CD2 1 
ATOM   1331 C CE1 . HIS   A 1 173 ? 6.12351  -3.49952  12.82638  1.000 41.83860 ? 172 HIS   A CE1 1 
ATOM   1332 N NE2 . HIS   A 1 173 ? 6.16259  -3.99894  14.04875  1.000 41.41024 ? 172 HIS   A NE2 1 
ATOM   1333 N N   . ALA   A 1 174 ? 12.46981 -5.23742  13.73324  1.000 35.55462 ? 173 ALA   A N   1 
ATOM   1334 C CA  . ALA   A 1 174 ? 13.84163 -5.70463  13.61177  1.000 34.18341 ? 173 ALA   A CA  1 
ATOM   1335 C C   . ALA   A 1 174 ? 13.88855 -7.22214  13.73166  1.000 35.92525 ? 173 ALA   A C   1 
ATOM   1336 O O   . ALA   A 1 174 ? 13.01374 -7.85185  14.34050  1.000 34.15343 ? 173 ALA   A O   1 
ATOM   1337 C CB  . ALA   A 1 174 ? 14.75018 -5.06418  14.67155  1.000 37.34198 ? 173 ALA   A CB  1 
ATOM   1338 N N   . GLY   A 1 175 ? 14.92103 -7.80450  13.13788  1.000 34.17177 ? 174 GLY   A N   1 
ATOM   1339 C CA  . GLY   A 1 175 ? 15.04046 -9.24541  13.14520  1.000 35.21418 ? 174 GLY   A CA  1 
ATOM   1340 C C   . GLY   A 1 175 ? 16.37245 -9.69176  12.59266  1.000 34.68072 ? 174 GLY   A C   1 
ATOM   1341 O O   . GLY   A 1 175 ? 17.28275 -8.88898  12.37968  1.000 34.84676 ? 174 GLY   A O   1 
ATOM   1342 N N   . THR   A 1 176 ? 16.46868 -10.99507 12.35719  1.000 32.46039 ? 175 THR   A N   1 
ATOM   1343 C CA  . THR   A 1 176 ? 17.71527 -11.61984 11.94353  1.000 36.09773 ? 175 THR   A CA  1 
ATOM   1344 C C   . THR   A 1 176 ? 17.55289 -12.27175 10.57843  1.000 36.01066 ? 175 THR   A C   1 
ATOM   1345 O O   . THR   A 1 176 ? 16.45719 -12.34211 10.01953  1.000 34.00103 ? 175 THR   A O   1 
ATOM   1346 C CB  . THR   A 1 176 ? 18.17288 -12.67809 12.95626  1.000 35.48024 ? 175 THR   A CB  1 
ATOM   1347 O OG1 . THR   A 1 176 ? 17.31587 -13.82228 12.86470  1.000 33.65789 ? 175 THR   A OG1 1 
ATOM   1348 C CG2 . THR   A 1 176 ? 18.12934 -12.13078 14.37480  1.000 35.62555 ? 175 THR   A CG2 1 
ATOM   1349 N N   . ASP   A 1 177 ? 18.67229 -12.74486 10.04021  1.000 36.05009 ? 176 ASP   A N   1 
ATOM   1350 C CA  . ASP   A 1 177 ? 18.62020 -13.70755 8.95560   1.000 36.29926 ? 176 ASP   A CA  1 
ATOM   1351 C C   . ASP   A 1 177 ? 18.39548 -15.09162 9.55543   1.000 35.11402 ? 176 ASP   A C   1 
ATOM   1352 O O   . ASP   A 1 177 ? 18.32285 -15.25855 10.77510  1.000 35.73234 ? 176 ASP   A O   1 
ATOM   1353 C CB  . ASP   A 1 177 ? 19.89060 -13.63721 8.10551   1.000 37.11382 ? 176 ASP   A CB  1 
ATOM   1354 C CG  . ASP   A 1 177 ? 21.16377 -13.90840 8.89976   1.000 37.53973 ? 176 ASP   A CG  1 
ATOM   1355 O OD1 . ASP   A 1 177 ? 21.11299 -14.58226 9.95160   1.000 36.47913 ? 176 ASP   A OD1 1 
ATOM   1356 O OD2 . ASP   A 1 177 ? 22.23457 -13.43717 8.45814   1.000 39.79126 ? 176 ASP   A OD2 1 
ATOM   1357 N N   . LEU   A 1 178 ? 18.29972 -16.10571 8.70565   1.000 33.85536 ? 177 LEU   A N   1 
ATOM   1358 C CA  . LEU   A 1 178 ? 18.02736 -17.44149 9.21919   1.000 37.29299 ? 177 LEU   A CA  1 
ATOM   1359 C C   . LEU   A 1 178 ? 19.25128 -18.09995 9.84327   1.000 39.96278 ? 177 LEU   A C   1 
ATOM   1360 O O   . LEU   A 1 178 ? 19.14197 -19.22500 10.34291  1.000 39.63538 ? 177 LEU   A O   1 
ATOM   1361 C CB  . LEU   A 1 178 ? 17.44708 -18.32323 8.11333   1.000 36.67369 ? 177 LEU   A CB  1 
ATOM   1362 C CG  . LEU   A 1 178 ? 15.91485 -18.33779 8.09322   1.000 36.37884 ? 177 LEU   A CG  1 
ATOM   1363 C CD1 . LEU   A 1 178 ? 15.38249 -18.94010 9.38040   1.000 36.01685 ? 177 LEU   A CD1 1 
ATOM   1364 C CD2 . LEU   A 1 178 ? 15.34526 -16.94125 7.89616   1.000 35.81080 ? 177 LEU   A CD2 1 
ATOM   1365 N N   . GLU   A 1 179 ? 20.40159 -17.43134 9.83538   1.000 39.29739 ? 178 GLU   A N   1 
ATOM   1366 C CA  . GLU   A 1 179 ? 21.55291 -17.85908 10.61582  1.000 40.90928 ? 178 GLU   A CA  1 
ATOM   1367 C C   . GLU   A 1 179 ? 21.61094 -17.18773 11.98235  1.000 39.72346 ? 178 GLU   A C   1 
ATOM   1368 O O   . GLU   A 1 179 ? 22.53950 -17.45673 12.75167  1.000 39.08684 ? 178 GLU   A O   1 
ATOM   1369 C CB  . GLU   A 1 179 ? 22.84844 -17.58323 9.84807   1.000 41.34968 ? 178 GLU   A CB  1 
ATOM   1370 C CG  . GLU   A 1 179 ? 22.97820 -18.36875 8.55555   1.000 42.78178 ? 178 GLU   A CG  1 
ATOM   1371 C CD  . GLU   A 1 179 ? 24.34705 -18.22244 7.92639   1.000 49.13430 ? 178 GLU   A CD  1 
ATOM   1372 O OE1 . GLU   A 1 179 ? 25.19763 -17.51753 8.50960   1.000 50.00304 ? 178 GLU   A OE1 1 
ATOM   1373 O OE2 . GLU   A 1 179 ? 24.57401 -18.81342 6.84980   1.000 52.51218 ? 178 GLU   A OE2 1 
ATOM   1374 N N   . GLY   A 1 180 ? 20.65289 -16.31976 12.29551  1.000 37.97519 ? 179 GLY   A N   1 
ATOM   1375 C CA  . GLY   A 1 180 ? 20.56750 -15.71016 13.60472  1.000 37.70158 ? 179 GLY   A CA  1 
ATOM   1376 C C   . GLY   A 1 180 ? 21.28062 -14.38775 13.76559  1.000 38.59880 ? 179 GLY   A C   1 
ATOM   1377 O O   . GLY   A 1 180 ? 21.32488 -13.86245 14.88397  1.000 37.58526 ? 179 GLY   A O   1 
ATOM   1378 N N   . ASN   A 1 181 ? 21.84264 -13.83146 12.69698  1.000 38.58201 ? 180 ASN   A N   1 
ATOM   1379 C CA  . ASN   A 1 181 ? 22.54558 -12.55734 12.77309  1.000 38.38345 ? 180 ASN   A CA  1 
ATOM   1380 C C   . ASN   A 1 181 ? 21.56334 -11.42526 12.50396  1.000 37.31001 ? 180 ASN   A C   1 
ATOM   1381 O O   . ASN   A 1 181 ? 20.95371 -11.36639 11.42942  1.000 34.02898 ? 180 ASN   A O   1 
ATOM   1382 C CB  . ASN   A 1 181 ? 23.70578 -12.51363 11.78084  1.000 38.57946 ? 180 ASN   A CB  1 
ATOM   1383 C CG  . ASN   A 1 181 ? 24.75177 -13.57119 12.06488  1.000 40.93177 ? 180 ASN   A CG  1 
ATOM   1384 O OD1 . ASN   A 1 181 ? 24.97851 -14.46826 11.25412  1.000 44.71817 ? 180 ASN   A OD1 1 
ATOM   1385 N ND2 . ASN   A 1 181 ? 25.39579 -13.47206 13.22255  1.000 40.84271 ? 180 ASN   A ND2 1 
ATOM   1386 N N   . PHE   A 1 182 ? 21.41565 -10.53222 13.47955  1.000 35.39183 ? 181 PHE   A N   1 
ATOM   1387 C CA  . PHE   A 1 182 ? 20.50881 -9.40367  13.33324  1.000 36.07237 ? 181 PHE   A CA  1 
ATOM   1388 C C   . PHE   A 1 182 ? 20.89814 -8.54712  12.13889  1.000 37.88678 ? 181 PHE   A C   1 
ATOM   1389 O O   . PHE   A 1 182 ? 22.08210 -8.37567  11.83083  1.000 34.95982 ? 181 PHE   A O   1 
ATOM   1390 C CB  . PHE   A 1 182 ? 20.51605 -8.54312  14.59936  1.000 36.59390 ? 181 PHE   A CB  1 
ATOM   1391 C CG  . PHE   A 1 182 ? 19.39663 -8.84790  15.54769  1.000 38.25171 ? 181 PHE   A CG  1 
ATOM   1392 C CD1 . PHE   A 1 182 ? 18.16834 -8.21953  15.41301  1.000 37.36113 ? 181 PHE   A CD1 1 
ATOM   1393 C CD2 . PHE   A 1 182 ? 19.57063 -9.75686  16.57790  1.000 37.51389 ? 181 PHE   A CD2 1 
ATOM   1394 C CE1 . PHE   A 1 182 ? 17.13135 -8.49547  16.28477  1.000 37.15185 ? 181 PHE   A CE1 1 
ATOM   1395 C CE2 . PHE   A 1 182 ? 18.53610 -10.03802 17.45441  1.000 38.90113 ? 181 PHE   A CE2 1 
ATOM   1396 C CZ  . PHE   A 1 182 ? 17.31429 -9.40560  17.30649  1.000 38.94856 ? 181 PHE   A CZ  1 
ATOM   1397 N N   . TYR   A 1 183 ? 19.88756 -8.02094  11.45638  1.000 35.45929 ? 182 TYR   A N   1 
ATOM   1398 C CA  . TYR   A 1 183 ? 20.09869 -6.91649  10.53697  1.000 38.70795 ? 182 TYR   A CA  1 
ATOM   1399 C C   . TYR   A 1 183 ? 20.24409 -5.63664  11.35014  1.000 37.66272 ? 182 TYR   A C   1 
ATOM   1400 O O   . TYR   A 1 183 ? 19.38075 -5.31378  12.17091  1.000 36.22835 ? 182 TYR   A O   1 
ATOM   1401 C CB  . TYR   A 1 183 ? 18.93471 -6.79821  9.55342   1.000 36.13997 ? 182 TYR   A CB  1 
ATOM   1402 C CG  . TYR   A 1 183 ? 18.84758 -7.92176  8.54221   1.000 38.13045 ? 182 TYR   A CG  1 
ATOM   1403 C CD1 . TYR   A 1 183 ? 19.61014 -7.89785  7.38008   1.000 39.22312 ? 182 TYR   A CD1 1 
ATOM   1404 C CD2 . TYR   A 1 183 ? 17.99134 -8.99676  8.73993   1.000 37.14575 ? 182 TYR   A CD2 1 
ATOM   1405 C CE1 . TYR   A 1 183 ? 19.52929 -8.91839  6.44826   1.000 39.98815 ? 182 TYR   A CE1 1 
ATOM   1406 C CE2 . TYR   A 1 183 ? 17.90340 -10.02273 7.81284   1.000 35.93874 ? 182 TYR   A CE2 1 
ATOM   1407 C CZ  . TYR   A 1 183 ? 18.67520 -9.97800  6.67015   1.000 38.32985 ? 182 TYR   A CZ  1 
ATOM   1408 O OH  . TYR   A 1 183 ? 18.59243 -10.99384 5.74494   1.000 37.25323 ? 182 TYR   A OH  1 
ATOM   1409 N N   . GLY   A 1 184 ? 21.34344 -4.92078  11.14322  1.000 37.80849 ? 183 GLY   A N   1 
ATOM   1410 C CA  . GLY   A 1 184 ? 21.59419 -3.70556  11.87927  1.000 39.37969 ? 183 GLY   A CA  1 
ATOM   1411 C C   . GLY   A 1 184 ? 22.25217 -3.96556  13.21847  1.000 41.28991 ? 183 GLY   A C   1 
ATOM   1412 O O   . GLY   A 1 184 ? 22.68678 -5.08189  13.51869  1.000 39.71725 ? 183 GLY   A O   1 
ATOM   1413 N N   . PRO   A 1 185 ? 22.32799 -2.93055  14.05848  1.000 41.76953 ? 184 PRO   A N   1 
ATOM   1414 C CA  . PRO   A 1 185 ? 23.09637 -3.04120  15.30481  1.000 42.53880 ? 184 PRO   A CA  1 
ATOM   1415 C C   . PRO   A 1 185 ? 22.26934 -3.52678  16.48404  1.000 42.55095 ? 184 PRO   A C   1 
ATOM   1416 O O   . PRO   A 1 185 ? 22.66031 -3.33453  17.63887  1.000 46.36120 ? 184 PRO   A O   1 
ATOM   1417 C CB  . PRO   A 1 185 ? 23.57077 -1.60335  15.52864  1.000 43.18757 ? 184 PRO   A CB  1 
ATOM   1418 C CG  . PRO   A 1 185 ? 22.41070 -0.78884  15.01677  1.000 45.29717 ? 184 PRO   A CG  1 
ATOM   1419 C CD  . PRO   A 1 185 ? 21.81412 -1.56425  13.85326  1.000 42.92939 ? 184 PRO   A CD  1 
ATOM   1420 N N   . PHE   A 1 186 ? 21.13193 -4.15687  16.21377  1.000 43.59763 ? 185 PHE   A N   1 
ATOM   1421 C CA  . PHE   A 1 186 ? 20.19158 -4.45930  17.27829  1.000 41.94585 ? 185 PHE   A CA  1 
ATOM   1422 C C   . PHE   A 1 186 ? 20.55067 -5.76895  17.97759  1.000 42.27169 ? 185 PHE   A C   1 
ATOM   1423 O O   . PHE   A 1 186 ? 21.24734 -6.63185  17.43488  1.000 40.78370 ? 185 PHE   A O   1 
ATOM   1424 C CB  . PHE   A 1 186 ? 18.76901 -4.51089  16.72167  1.000 41.50433 ? 185 PHE   A CB  1 
ATOM   1425 C CG  . PHE   A 1 186 ? 18.41365 -3.31382  15.89025  1.000 41.27586 ? 185 PHE   A CG  1 
ATOM   1426 C CD1 . PHE   A 1 186 ? 18.26335 -2.06865  16.47640  1.000 42.14473 ? 185 PHE   A CD1 1 
ATOM   1427 C CD2 . PHE   A 1 186 ? 18.25163 -3.42703  14.52247  1.000 38.38354 ? 185 PHE   A CD2 1 
ATOM   1428 C CE1 . PHE   A 1 186 ? 17.94845 -0.96138  15.71329  1.000 44.20939 ? 185 PHE   A CE1 1 
ATOM   1429 C CE2 . PHE   A 1 186 ? 17.93565 -2.32424  13.75551  1.000 39.49296 ? 185 PHE   A CE2 1 
ATOM   1430 C CZ  . PHE   A 1 186 ? 17.78386 -1.09021  14.35095  1.000 42.12055 ? 185 PHE   A CZ  1 
ATOM   1431 N N   . VAL   A 1 187 ? 20.07176 -5.89488  19.21444  1.000 40.37308 ? 186 VAL   A N   1 
ATOM   1432 C CA  . VAL   A 1 187 ? 20.27246 -7.07686  20.04143  1.000 41.16280 ? 186 VAL   A CA  1 
ATOM   1433 C C   . VAL   A 1 187 ? 18.92476 -7.49045  20.61337  1.000 41.27896 ? 186 VAL   A C   1 
ATOM   1434 O O   . VAL   A 1 187 ? 18.02084 -6.66443  20.77471  1.000 39.66102 ? 186 VAL   A O   1 
ATOM   1435 C CB  . VAL   A 1 187 ? 21.29362 -6.82108  21.16960  1.000 43.65902 ? 186 VAL   A CB  1 
ATOM   1436 C CG1 . VAL   A 1 187 ? 22.70269 -6.75762  20.60161  1.000 40.67977 ? 186 VAL   A CG1 1 
ATOM   1437 C CG2 . VAL   A 1 187 ? 20.95743 -5.52916  21.89157  1.000 44.29586 ? 186 VAL   A CG2 1 
ATOM   1438 N N   . ASP   A 1 188 ? 18.78728 -8.78184  20.91622  1.000 40.00803 ? 187 ASP   A N   1 
ATOM   1439 C CA  . ASP   A 1 188 ? 17.50710 -9.32278  21.37808  1.000 38.71058 ? 187 ASP   A CA  1 
ATOM   1440 C C   . ASP   A 1 188 ? 17.42272 -9.24542  22.90482  1.000 43.37085 ? 187 ASP   A C   1 
ATOM   1441 O O   . ASP   A 1 188 ? 17.51475 -10.23778 23.63097  1.000 41.82775 ? 187 ASP   A O   1 
ATOM   1442 C CB  . ASP   A 1 188 ? 17.30820 -10.74444 20.86521  1.000 37.46475 ? 187 ASP   A CB  1 
ATOM   1443 C CG  . ASP   A 1 188 ? 18.51518 -11.62979 21.09681  1.000 37.80829 ? 187 ASP   A CG  1 
ATOM   1444 O OD1 . ASP   A 1 188 ? 19.62872 -11.09504 21.26913  1.000 40.50526 ? 187 ASP   A OD1 1 
ATOM   1445 O OD2 . ASP   A 1 188 ? 18.35006 -12.86756 21.09575  1.000 36.24161 ? 187 ASP   A OD2 1 
ATOM   1446 N N   . ARG   A 1 189 ? 17.23616 -8.01811  23.38473  1.000 41.96449 ? 188 ARG   A N   1 
ATOM   1447 C CA  . ARG   A 1 189 ? 16.92434 -7.77611  24.78509  1.000 48.53510 ? 188 ARG   A CA  1 
ATOM   1448 C C   . ARG   A 1 189 ? 16.08583 -6.50813  24.87957  1.000 49.35905 ? 188 ARG   A C   1 
ATOM   1449 O O   . ARG   A 1 189 ? 15.99037 -5.72522  23.93107  1.000 49.55378 ? 188 ARG   A O   1 
ATOM   1450 C CB  . ARG   A 1 189 ? 18.19082 -7.68104  25.64458  1.000 50.78833 ? 188 ARG   A CB  1 
ATOM   1451 C CG  . ARG   A 1 189 ? 19.03024 -6.44071  25.41852  1.000 52.55871 ? 188 ARG   A CG  1 
ATOM   1452 C CD  . ARG   A 1 189 ? 20.46719 -6.82211  25.11714  1.000 56.43488 ? 188 ARG   A CD  1 
ATOM   1453 N NE  . ARG   A 1 189 ? 20.97498 -7.83535  26.03407  1.000 63.05197 ? 188 ARG   A NE  1 
ATOM   1454 C CZ  . ARG   A 1 189 ? 22.07254 -8.54943  25.82386  1.000 68.57314 ? 188 ARG   A CZ  1 
ATOM   1455 N NH1 . ARG   A 1 189 ? 22.79903 -8.39409  24.72798  1.000 64.93628 ? 188 ARG   A NH1 1 
ATOM   1456 N NH2 . ARG   A 1 189 ? 22.44757 -9.44564  26.73264  1.000 62.99313 ? 188 ARG   A NH2 1 
ATOM   1457 N N   . GLN   A 1 190 ? 15.47379 -6.31507  26.04602  1.000 53.42206 ? 189 GLN   A N   1 
ATOM   1458 C CA  . GLN   A 1 190 ? 14.53404 -5.21488  26.26609  1.000 52.63109 ? 189 GLN   A CA  1 
ATOM   1459 C C   . GLN   A 1 190 ? 15.26860 -4.02370  26.88572  1.000 56.15537 ? 189 GLN   A C   1 
ATOM   1460 O O   . GLN   A 1 190 ? 15.13961 -3.70222  28.06885  1.000 56.76642 ? 189 GLN   A O   1 
ATOM   1461 C CB  . GLN   A 1 190 ? 13.37593 -5.68804  27.13504  1.000 52.69718 ? 189 GLN   A CB  1 
ATOM   1462 C CG  . GLN   A 1 190 ? 12.29654 -4.65495  27.39796  1.000 51.43069 ? 189 GLN   A CG  1 
ATOM   1463 C CD  . GLN   A 1 190 ? 11.13343 -5.22965  28.17537  1.000 52.01156 ? 189 GLN   A CD  1 
ATOM   1464 O OE1 . GLN   A 1 190 ? 10.81540 -6.41112  28.04445  1.000 51.93592 ? 189 GLN   A OE1 1 
ATOM   1465 N NE2 . GLN   A 1 190 ? 10.49539 -4.40023  28.99623  1.000 49.61374 ? 189 GLN   A NE2 1 
ATOM   1466 N N   . THR   A 1 191 ? 16.06208 -3.36576  26.05072  1.000 54.96043 ? 190 THR   A N   1 
ATOM   1467 C CA  . THR   A 1 191 ? 16.80459 -2.17373  26.43766  1.000 58.29461 ? 190 THR   A CA  1 
ATOM   1468 C C   . THR   A 1 191 ? 16.46700 -1.03493  25.48099  1.000 62.90167 ? 190 THR   A C   1 
ATOM   1469 O O   . THR   A 1 191 ? 15.67166 -1.18744  24.55079  1.000 55.88437 ? 190 THR   A O   1 
ATOM   1470 C CB  . THR   A 1 191 ? 18.31442 -2.43958  26.45488  1.000 56.95665 ? 190 THR   A CB  1 
ATOM   1471 O OG1 . THR   A 1 191 ? 18.72738 -2.95924  25.18520  1.000 59.75742 ? 190 THR   A OG1 1 
ATOM   1472 C CG2 . THR   A 1 191 ? 18.67528 -3.43072  27.54893  1.000 60.73107 ? 190 THR   A CG2 1 
ATOM   1473 N N   . ALA   A 1 192 ? 17.08294 0.11932   25.72555  1.000 60.28826 ? 191 ALA   A N   1 
ATOM   1474 C CA  . ALA   A 1 192 ? 16.89885 1.28136   24.86369  1.000 58.73221 ? 191 ALA   A CA  1 
ATOM   1475 C C   . ALA   A 1 192 ? 17.62831 1.04875   23.54695  1.000 57.50765 ? 191 ALA   A C   1 
ATOM   1476 O O   . ALA   A 1 192 ? 18.86263 1.06538   23.50169  1.000 55.65502 ? 191 ALA   A O   1 
ATOM   1477 C CB  . ALA   A 1 192 ? 17.40717 2.54056   25.55856  1.000 58.74250 ? 191 ALA   A CB  1 
ATOM   1478 N N   . GLN   A 1 193 ? 16.86940 0.81864   22.47655  1.000 56.70213 ? 192 GLN   A N   1 
ATOM   1479 C CA  . GLN   A 1 193 ? 17.42557 0.61171   21.14423  1.000 54.97459 ? 192 GLN   A CA  1 
ATOM   1480 C C   . GLN   A 1 193 ? 16.71777 1.54313   20.17626  1.000 55.90866 ? 192 GLN   A C   1 
ATOM   1481 O O   . GLN   A 1 193 ? 15.49307 1.47550   20.02946  1.000 54.61503 ? 192 GLN   A O   1 
ATOM   1482 C CB  . GLN   A 1 193 ? 17.27310 -0.84211  20.69029  1.000 52.39554 ? 192 GLN   A CB  1 
ATOM   1483 C CG  . GLN   A 1 193 ? 17.95637 -1.85300  21.58825  1.000 52.03659 ? 192 GLN   A CG  1 
ATOM   1484 C CD  . GLN   A 1 193 ? 17.94529 -3.24330  20.99397  1.000 47.96305 ? 192 GLN   A CD  1 
ATOM   1485 O OE1 . GLN   A 1 193 ? 18.59375 -3.50117  19.98039  1.000 44.14836 ? 192 GLN   A OE1 1 
ATOM   1486 N NE2 . GLN   A 1 193 ? 17.20008 -4.14817  21.61738  1.000 47.39174 ? 192 GLN   A NE2 1 
ATOM   1487 N N   . ALA   A 1 194 ? 17.48417 2.40588   19.51912  1.000 56.10052 ? 193 ALA   A N   1 
ATOM   1488 C CA  . ALA   A 1 194 ? 16.94784 3.35792   18.56023  1.000 58.52331 ? 193 ALA   A CA  1 
ATOM   1489 C C   . ALA   A 1 194 ? 17.55667 3.09017   17.19352  1.000 59.25113 ? 193 ALA   A C   1 
ATOM   1490 O O   . ALA   A 1 194 ? 18.77814 2.94839   17.06948  1.000 58.76196 ? 193 ALA   A O   1 
ATOM   1491 C CB  . ALA   A 1 194 ? 17.22976 4.79846   18.99253  1.000 60.21745 ? 193 ALA   A CB  1 
ATOM   1492 N N   . ALA   A 1 195 ? 16.70670 3.01118   16.17589  1.000 58.07971 ? 194 ALA   A N   1 
ATOM   1493 C CA  . ALA   A 1 195 ? 17.19174 2.95104   14.80881  1.000 54.41414 ? 194 ALA   A CA  1 
ATOM   1494 C C   . ALA   A 1 195 ? 17.67371 4.32727   14.36895  1.000 59.58342 ? 194 ALA   A C   1 
ATOM   1495 O O   . ALA   A 1 195 ? 17.19414 5.36110   14.84553  1.000 63.18305 ? 194 ALA   A O   1 
ATOM   1496 C CB  . ALA   A 1 195 ? 16.09891 2.45292   13.86483  1.000 50.29593 ? 194 ALA   A CB  1 
ATOM   1497 N N   . GLY   A 1 196 ? 18.63218 4.33414   13.45017  1.000 55.20112 ? 195 GLY   A N   1 
ATOM   1498 C CA  . GLY   A 1 196 ? 19.19733 5.56823   12.95519  1.000 53.10096 ? 195 GLY   A CA  1 
ATOM   1499 C C   . GLY   A 1 196 ? 18.25840 6.28928   12.00648  1.000 50.62237 ? 195 GLY   A C   1 
ATOM   1500 O O   . GLY   A 1 196 ? 17.06916 5.98559   11.89261  1.000 48.09263 ? 195 GLY   A O   1 
ATOM   1501 N N   . THR   A 1 197 ? 18.82376 7.26968   11.30696  1.000 49.96927 ? 196 THR   A N   1 
ATOM   1502 C CA  . THR   A 1 197 ? 18.05095 8.05313   10.35305  1.000 48.11660 ? 196 THR   A CA  1 
ATOM   1503 C C   . THR   A 1 197 ? 17.50674 7.15898   9.24620   1.000 48.60857 ? 196 THR   A C   1 
ATOM   1504 O O   . THR   A 1 197 ? 18.25140 6.40040   8.61828   1.000 49.25315 ? 196 THR   A O   1 
ATOM   1505 C CB  . THR   A 1 197 ? 18.91628 9.16482   9.75991   1.000 48.70689 ? 196 THR   A CB  1 
ATOM   1506 O OG1 . THR   A 1 197 ? 19.45070 9.96903   10.81839  1.000 49.81208 ? 196 THR   A OG1 1 
ATOM   1507 C CG2 . THR   A 1 197 ? 18.09312 10.04586  8.82790   1.000 51.06122 ? 196 THR   A CG2 1 
ATOM   1508 N N   . ASP   A 1 198 ? 16.19777 7.24510   9.01710   1.000 47.39215 ? 197 ASP   A N   1 
ATOM   1509 C CA  . ASP   A 1 198 ? 15.52280 6.44423   7.99756   1.000 49.45369 ? 197 ASP   A CA  1 
ATOM   1510 C C   . ASP   A 1 198 ? 15.61518 7.20030   6.67931   1.000 51.19490 ? 197 ASP   A C   1 
ATOM   1511 O O   . ASP   A 1 198 ? 14.80175 8.07684   6.38487   1.000 51.06197 ? 197 ASP   A O   1 
ATOM   1512 C CB  . ASP   A 1 198 ? 14.07244 6.18396   8.39061   1.000 49.00785 ? 197 ASP   A CB  1 
ATOM   1513 C CG  . ASP   A 1 198 ? 13.43014 5.07953   7.56914   1.000 51.50914 ? 197 ASP   A CG  1 
ATOM   1514 O OD1 . ASP   A 1 198 ? 12.20236 4.87762   7.70392   1.000 54.84269 ? 197 ASP   A OD1 1 
ATOM   1515 O OD2 . ASP   A 1 198 ? 14.15480 4.40037   6.80997   1.000 52.19617 ? 197 ASP   A OD2 1 
ATOM   1516 N N   . THR   A 1 199 ? 16.62085 6.86219   5.87744   1.000 51.25766 ? 198 THR   A N   1 
ATOM   1517 C CA  . THR   A 1 199 ? 16.80449 7.49393   4.58067   1.000 53.17201 ? 198 THR   A CA  1 
ATOM   1518 C C   . THR   A 1 199 ? 16.03417 6.73795   3.50052   1.000 51.77502 ? 198 THR   A C   1 
ATOM   1519 O O   . THR   A 1 199 ? 15.64973 5.57921   3.66956   1.000 50.13145 ? 198 THR   A O   1 
ATOM   1520 C CB  . THR   A 1 199 ? 18.28981 7.57028   4.21889   1.000 56.31541 ? 198 THR   A CB  1 
ATOM   1521 O OG1 . THR   A 1 199 ? 18.85836 6.25507   4.23112   1.000 58.76523 ? 198 THR   A OG1 1 
ATOM   1522 C CG2 . THR   A 1 199 ? 19.03735 8.45249   5.21465   1.000 57.75803 ? 198 THR   A CG2 1 
ATOM   1523 N N   . THR   A 1 200 ? 15.81088 7.41768   2.37823   1.000 51.73293 ? 199 THR   A N   1 
ATOM   1524 C CA  . THR   A 1 200 ? 14.98097 6.89120   1.30397   1.000 49.65821 ? 199 THR   A CA  1 
ATOM   1525 C C   . THR   A 1 200 ? 15.82602 6.14724   0.27668   1.000 49.69324 ? 199 THR   A C   1 
ATOM   1526 O O   . THR   A 1 200 ? 16.93309 6.57081   -0.06440  1.000 52.59659 ? 199 THR   A O   1 
ATOM   1527 C CB  . THR   A 1 200 ? 14.20963 8.02386   0.62524   1.000 49.54121 ? 199 THR   A CB  1 
ATOM   1528 O OG1 . THR   A 1 200 ? 13.58935 8.84176   1.62459   1.000 51.76452 ? 199 THR   A OG1 1 
ATOM   1529 C CG2 . THR   A 1 200 ? 13.13235 7.46593   -0.29094  1.000 46.47975 ? 199 THR   A CG2 1 
ATOM   1530 N N   . ILE   A 1 201 ? 15.28933 5.03343   -0.21775  1.000 46.94772 ? 200 ILE   A N   1 
ATOM   1531 C CA  . ILE   A 1 201 ? 15.96204 4.20709   -1.21827  1.000 46.87720 ? 200 ILE   A CA  1 
ATOM   1532 C C   . ILE   A 1 201 ? 15.73826 4.86765   -2.57700  1.000 45.78553 ? 200 ILE   A C   1 
ATOM   1533 O O   . ILE   A 1 201 ? 14.69755 4.67876   -3.20826  1.000 42.98341 ? 200 ILE   A O   1 
ATOM   1534 C CB  . ILE   A 1 201 ? 15.45273 2.76538   -1.19595  1.000 44.30584 ? 200 ILE   A CB  1 
ATOM   1535 C CG1 . ILE   A 1 201 ? 15.34063 2.27164   0.24768   1.000 44.97799 ? 200 ILE   A CG1 1 
ATOM   1536 C CG2 . ILE   A 1 201 ? 16.38284 1.86288   -1.99111  1.000 45.13281 ? 200 ILE   A CG2 1 
ATOM   1537 C CD1 . ILE   A 1 201 ? 14.50648 1.02019   0.40358   1.000 42.67131 ? 200 ILE   A CD1 1 
ATOM   1538 N N   . THR   A 1 202 ? 16.73061 5.63409   -3.03767  1.000 46.85373 ? 201 THR   A N   1 
ATOM   1539 C CA  . THR   A 1 202 ? 16.55196 6.47629   -4.21915  1.000 45.87953 ? 201 THR   A CA  1 
ATOM   1540 C C   . THR   A 1 202 ? 16.27696 5.64305   -5.46749  1.000 44.32106 ? 201 THR   A C   1 
ATOM   1541 O O   . THR   A 1 202 ? 15.37690 5.96144   -6.25866  1.000 43.06674 ? 201 THR   A O   1 
ATOM   1542 C CB  . THR   A 1 202 ? 17.79080 7.34992   -4.42249  1.000 49.83695 ? 201 THR   A CB  1 
ATOM   1543 O OG1 . THR   A 1 202 ? 18.17975 7.93404   -3.17272  1.000 50.23522 ? 201 THR   A OG1 1 
ATOM   1544 C CG2 . THR   A 1 202 ? 17.49839 8.45520   -5.41435  1.000 48.95550 ? 201 THR   A CG2 1 
ATOM   1545 N N   . VAL   A 1 203 ? 17.05243 4.57271   -5.66498  1.000 42.52814 ? 202 VAL   A N   1 
ATOM   1546 C CA  . VAL   A 1 203 ? 16.88016 3.73763   -6.84957  1.000 44.77111 ? 202 VAL   A CA  1 
ATOM   1547 C C   . VAL   A 1 203 ? 15.47942 3.14291   -6.88299  1.000 43.04794 ? 202 VAL   A C   1 
ATOM   1548 O O   . VAL   A 1 203 ? 14.89030 2.97779   -7.95860  1.000 42.13677 ? 202 VAL   A O   1 
ATOM   1549 C CB  . VAL   A 1 203 ? 17.97253 2.64721   -6.90348  1.000 46.02153 ? 202 VAL   A CB  1 
ATOM   1550 C CG1 . VAL   A 1 203 ? 17.73378 1.56608   -5.85391  1.000 45.46424 ? 202 VAL   A CG1 1 
ATOM   1551 C CG2 . VAL   A 1 203 ? 18.04978 2.04092   -8.29399  1.000 47.30686 ? 202 VAL   A CG2 1 
ATOM   1552 N N   . ASN   A 1 204 ? 14.90392 2.85817   -5.71264  1.000 42.25596 ? 203 ASN   A N   1 
ATOM   1553 C CA  . ASN   A 1 204 ? 13.55187 2.31511   -5.66623  1.000 41.50370 ? 203 ASN   A CA  1 
ATOM   1554 C C   . ASN   A 1 204 ? 12.51988 3.36288   -6.06238  1.000 42.04661 ? 203 ASN   A C   1 
ATOM   1555 O O   . ASN   A 1 204 ? 11.53891 3.04576   -6.74428  1.000 41.85236 ? 203 ASN   A O   1 
ATOM   1556 C CB  . ASN   A 1 204 ? 13.25786 1.76616   -4.27265  1.000 41.83177 ? 203 ASN   A CB  1 
ATOM   1557 C CG  . ASN   A 1 204 ? 13.96194 0.45086   -4.00585  1.000 41.30624 ? 203 ASN   A CG  1 
ATOM   1558 O OD1 . ASN   A 1 204 ? 14.80018 0.01013   -4.79229  1.000 41.08772 ? 203 ASN   A OD1 1 
ATOM   1559 N ND2 . ASN   A 1 204 ? 13.62762 -0.18087  -2.88774  1.000 41.53171 ? 203 ASN   A ND2 1 
ATOM   1560 N N   . VAL   A 1 205 ? 12.71942 4.61574   -5.64689  1.000 41.16404 ? 204 VAL   A N   1 
ATOM   1561 C CA  . VAL   A 1 205 ? 11.81576 5.68014   -6.07254  1.000 42.04312 ? 204 VAL   A CA  1 
ATOM   1562 C C   . VAL   A 1 205 ? 11.89651 5.87301   -7.58128  1.000 43.93851 ? 204 VAL   A C   1 
ATOM   1563 O O   . VAL   A 1 205 ? 10.87904 6.09804   -8.24756  1.000 41.91900 ? 204 VAL   A O   1 
ATOM   1564 C CB  . VAL   A 1 205 ? 12.12556 6.98642   -5.31922  1.000 42.58651 ? 204 VAL   A CB  1 
ATOM   1565 C CG1 . VAL   A 1 205 ? 11.19259 8.09850   -5.77792  1.000 43.10436 ? 204 VAL   A CG1 1 
ATOM   1566 C CG2 . VAL   A 1 205 ? 12.00839 6.77706   -3.82440  1.000 41.92172 ? 204 VAL   A CG2 1 
ATOM   1567 N N   . LEU   A 1 206 ? 13.10231 5.78195   -8.14711  1.000 41.10683 ? 205 LEU   A N   1 
ATOM   1568 C CA  . LEU   A 1 206 ? 13.23438 5.89359   -9.59737  1.000 43.81455 ? 205 LEU   A CA  1 
ATOM   1569 C C   . LEU   A 1 206 ? 12.53521 4.73900   -10.30898 1.000 42.22448 ? 205 LEU   A C   1 
ATOM   1570 O O   . LEU   A 1 206 ? 11.86268 4.94185   -11.32829 1.000 41.11130 ? 205 LEU   A O   1 
ATOM   1571 C CB  . LEU   A 1 206 ? 14.71125 5.95319   -9.98546  1.000 43.44855 ? 205 LEU   A CB  1 
ATOM   1572 C CG  . LEU   A 1 206 ? 15.41937 7.24210   -9.56971  1.000 43.16257 ? 205 LEU   A CG  1 
ATOM   1573 C CD1 . LEU   A 1 206 ? 16.90940 7.15737   -9.85024  1.000 45.64276 ? 205 LEU   A CD1 1 
ATOM   1574 C CD2 . LEU   A 1 206 ? 14.80238 8.42911   -10.28998 1.000 46.47094 ? 205 LEU   A CD2 1 
ATOM   1575 N N   . ALA   A 1 207 ? 12.68580 3.51782   -9.78838  1.000 39.99215 ? 206 ALA   A N   1 
ATOM   1576 C CA  . ALA   A 1 207 ? 11.98900 2.37268   -10.36815 1.000 42.30178 ? 206 ALA   A CA  1 
ATOM   1577 C C   . ALA   A 1 207 ? 10.47742 2.55165   -10.28861 1.000 45.14248 ? 206 ALA   A C   1 
ATOM   1578 O O   . ALA   A 1 207 ? 9.74771  2.20788   -11.22753 1.000 44.73690 ? 206 ALA   A O   1 
ATOM   1579 C CB  . ALA   A 1 207 ? 12.41706 1.08810   -9.65921  1.000 42.68686 ? 206 ALA   A CB  1 
ATOM   1580 N N   . TRP   A 1 208 ? 9.99251  3.10033   -9.17530  1.000 40.83165 ? 207 TRP   A N   1 
ATOM   1581 C CA  . TRP   A 1 208 ? 8.56438  3.34702   -9.01648  1.000 44.29816 ? 207 TRP   A CA  1 
ATOM   1582 C C   . TRP   A 1 208 ? 8.07591  4.41517   -9.98951  1.000 44.73871 ? 207 TRP   A C   1 
ATOM   1583 O O   . TRP   A 1 208 ? 6.96657  4.31680   -10.52481 1.000 45.15955 ? 207 TRP   A O   1 
ATOM   1584 C CB  . TRP   A 1 208 ? 8.28654  3.74172   -7.56691  1.000 43.06473 ? 207 TRP   A CB  1 
ATOM   1585 C CG  . TRP   A 1 208 ? 6.86738  4.07564   -7.25552  1.000 43.85246 ? 207 TRP   A CG  1 
ATOM   1586 C CD1 . TRP   A 1 208 ? 5.82107  3.20671   -7.14743  1.000 43.13146 ? 207 TRP   A CD1 1 
ATOM   1587 C CD2 . TRP   A 1 208 ? 6.34322  5.37455   -6.96992  1.000 42.94929 ? 207 TRP   A CD2 1 
ATOM   1588 N NE1 . TRP   A 1 208 ? 4.67205  3.88933   -6.82896  1.000 43.92457 ? 207 TRP   A NE1 1 
ATOM   1589 C CE2 . TRP   A 1 208 ? 4.96742  5.22232   -6.71403  1.000 44.26521 ? 207 TRP   A CE2 1 
ATOM   1590 C CE3 . TRP   A 1 208 ? 6.90365  6.65449   -6.91284  1.000 44.69381 ? 207 TRP   A CE3 1 
ATOM   1591 C CZ2 . TRP   A 1 208 ? 4.14447  6.30020   -6.40584  1.000 45.82243 ? 207 TRP   A CZ2 1 
ATOM   1592 C CZ3 . TRP   A 1 208 ? 6.08450  7.72386   -6.60754  1.000 45.42348 ? 207 TRP   A CZ3 1 
ATOM   1593 C CH2 . TRP   A 1 208 ? 4.72047  7.53994   -6.35584  1.000 46.94498 ? 207 TRP   A CH2 1 
ATOM   1594 N N   . LEU   A 1 209 ? 8.89819  5.43385   -10.24636 1.000 43.30143 ? 208 LEU   A N   1 
ATOM   1595 C CA  . LEU   A 1 209 ? 8.54045  6.43634   -11.24576 1.000 45.37673 ? 208 LEU   A CA  1 
ATOM   1596 C C   . LEU   A 1 209 ? 8.50953  5.83442   -12.64630 1.000 46.70192 ? 208 LEU   A C   1 
ATOM   1597 O O   . LEU   A 1 209 ? 7.67461  6.21480   -13.47687 1.000 45.13241 ? 208 LEU   A O   1 
ATOM   1598 C CB  . LEU   A 1 209 ? 9.51906  7.60752   -11.18738 1.000 45.69622 ? 208 LEU   A CB  1 
ATOM   1599 C CG  . LEU   A 1 209 ? 9.46473  8.44814   -9.91253  1.000 46.02051 ? 208 LEU   A CG  1 
ATOM   1600 C CD1 . LEU   A 1 209 ? 10.45802 9.59797   -9.98189  1.000 48.25029 ? 208 LEU   A CD1 1 
ATOM   1601 C CD2 . LEU   A 1 209 ? 8.05235  8.96201   -9.67351  1.000 46.32392 ? 208 LEU   A CD2 1 
ATOM   1602 N N   . TYR   A 1 210 ? 9.42200  4.90332   -12.93198 1.000 46.39450 ? 209 TYR   A N   1 
ATOM   1603 C CA  . TYR   A 1 210 ? 9.37554  4.20613   -14.21378 1.000 46.27644 ? 209 TYR   A CA  1 
ATOM   1604 C C   . TYR   A 1 210 ? 8.10696  3.36830   -14.33383 1.000 46.71240 ? 209 TYR   A C   1 
ATOM   1605 O O   . TYR   A 1 210 ? 7.48158  3.32127   -15.40049 1.000 45.50293 ? 209 TYR   A O   1 
ATOM   1606 C CB  . TYR   A 1 210 ? 10.62312 3.33979   -14.39224 1.000 45.33134 ? 209 TYR   A CB  1 
ATOM   1607 C CG  . TYR   A 1 210 ? 11.82304 4.11274   -14.89750 1.000 46.15738 ? 209 TYR   A CG  1 
ATOM   1608 C CD1 . TYR   A 1 210 ? 11.83084 4.65556   -16.17563 1.000 47.93501 ? 209 TYR   A CD1 1 
ATOM   1609 C CD2 . TYR   A 1 210 ? 12.94511 4.29889   -14.10076 1.000 46.67580 ? 209 TYR   A CD2 1 
ATOM   1610 C CE1 . TYR   A 1 210 ? 12.91695 5.36537   -16.64448 1.000 48.76175 ? 209 TYR   A CE1 1 
ATOM   1611 C CE2 . TYR   A 1 210 ? 14.04014 5.00946   -14.56297 1.000 46.70445 ? 209 TYR   A CE2 1 
ATOM   1612 C CZ  . TYR   A 1 210 ? 14.01894 5.53875   -15.83526 1.000 49.23005 ? 209 TYR   A CZ  1 
ATOM   1613 O OH  . TYR   A 1 210 ? 15.10086 6.24519   -16.30507 1.000 49.39665 ? 209 TYR   A OH  1 
ATOM   1614 N N   . ALA   A 1 211 ? 7.71064  2.70428   -13.24554 1.000 44.55506 ? 210 ALA   A N   1 
ATOM   1615 C CA  . ALA   A 1 211 ? 6.44166  1.98076   -13.23920 1.000 47.91429 ? 210 ALA   A CA  1 
ATOM   1616 C C   . ALA   A 1 211 ? 5.27062  2.92744   -13.46917 1.000 47.61286 ? 210 ALA   A C   1 
ATOM   1617 O O   . ALA   A 1 211 ? 4.29188  2.56977   -14.13507 1.000 47.95143 ? 210 ALA   A O   1 
ATOM   1618 C CB  . ALA   A 1 211 ? 6.26756  1.22915   -11.91902 1.000 46.51024 ? 210 ALA   A CB  1 
ATOM   1619 N N   . ALA   A 1 212 ? 5.35223  4.13769   -12.91348 1.000 47.90986 ? 211 ALA   A N   1 
ATOM   1620 C CA  . ALA   A 1 212 ? 4.31446  5.13880   -13.13915 1.000 48.86752 ? 211 ALA   A CA  1 
ATOM   1621 C C   . ALA   A 1 212 ? 4.22625  5.50990   -14.61222 1.000 51.85545 ? 211 ALA   A C   1 
ATOM   1622 O O   . ALA   A 1 212 ? 3.13705  5.52539   -15.19856 1.000 52.05098 ? 211 ALA   A O   1 
ATOM   1623 C CB  . ALA   A 1 212 ? 4.59214  6.37910   -12.29159 1.000 48.89739 ? 211 ALA   A CB  1 
ATOM   1624 N N   . VAL   A 1 213 ? 5.37258  5.82166   -15.22188 1.000 49.49979 ? 212 VAL   A N   1 
ATOM   1625 C CA  . VAL   A 1 213 ? 5.40540  6.14274   -16.64730 1.000 51.00902 ? 212 VAL   A CA  1 
ATOM   1626 C C   . VAL   A 1 213 ? 4.80658  5.00540   -17.46251 1.000 50.13596 ? 212 VAL   A C   1 
ATOM   1627 O O   . VAL   A 1 213 ? 4.00020  5.23100   -18.37351 1.000 49.60218 ? 212 VAL   A O   1 
ATOM   1628 C CB  . VAL   A 1 213 ? 6.84428  6.45881   -17.09624 1.000 48.58953 ? 212 VAL   A CB  1 
ATOM   1629 C CG1 . VAL   A 1 213 ? 6.92977  6.49009   -18.61597 1.000 49.64037 ? 212 VAL   A CG1 1 
ATOM   1630 C CG2 . VAL   A 1 213 ? 7.30404  7.78297   -16.50708 1.000 50.77952 ? 212 VAL   A CG2 1 
ATOM   1631 N N   . ILE   A 1 214 ? 5.17961  3.76530   -17.13767 1.000 49.64031 ? 213 ILE   A N   1 
ATOM   1632 C CA  . ILE   A 1 214 ? 4.66734  2.61335   -17.87500 1.000 49.66715 ? 213 ILE   A CA  1 
ATOM   1633 C C   . ILE   A 1 214 ? 3.14813  2.53773   -17.77020 1.000 50.10812 ? 213 ILE   A C   1 
ATOM   1634 O O   . ILE   A 1 214 ? 2.45820  2.24406   -18.75394 1.000 50.82099 ? 213 ILE   A O   1 
ATOM   1635 C CB  . ILE   A 1 214 ? 5.34047  1.32185   -17.37322 1.000 49.07958 ? 213 ILE   A CB  1 
ATOM   1636 C CG1 . ILE   A 1 214 ? 6.81614  1.30219   -17.77763 1.000 48.93121 ? 213 ILE   A CG1 1 
ATOM   1637 C CG2 . ILE   A 1 214 ? 4.61916  0.09166   -17.90331 1.000 50.04066 ? 213 ILE   A CG2 1 
ATOM   1638 C CD1 . ILE   A 1 214 ? 7.60962  0.17437   -17.15204 1.000 49.46417 ? 213 ILE   A CD1 1 
ATOM   1639 N N   . ASN   A 1 215 ? 2.60050  2.82555   -16.58881 1.000 49.84840 ? 214 ASN   A N   1 
ATOM   1640 C CA  . ASN   A 1 215 ? 1.17163  2.69219   -16.33772 1.000 52.10971 ? 214 ASN   A CA  1 
ATOM   1641 C C   . ASN   A 1 215 ? 0.38173  3.96558   -16.63720 1.000 54.08339 ? 214 ASN   A C   1 
ATOM   1642 O O   . ASN   A 1 215 ? -0.76847 4.08205   -16.19864 1.000 57.58952 ? 214 ASN   A O   1 
ATOM   1643 C CB  . ASN   A 1 215 ? 0.92864  2.25380   -14.89232 1.000 51.04073 ? 214 ASN   A CB  1 
ATOM   1644 C CG  . ASN   A 1 215 ? 1.16660  0.77023   -14.68765 1.000 51.28808 ? 214 ASN   A CG  1 
ATOM   1645 O OD1 . ASN   A 1 215 ? 0.24162  -0.03611  -14.78860 1.000 50.73310 ? 214 ASN   A OD1 1 
ATOM   1646 N ND2 . ASN   A 1 215 ? 2.41130  0.40136   -14.40263 1.000 51.14174 ? 214 ASN   A ND2 1 
ATOM   1647 N N   . GLY   A 1 216 ? 0.96403  4.91805   -17.36655 1.000 55.02495 ? 215 GLY   A N   1 
ATOM   1648 C CA  . GLY   A 1 216 ? 0.23829  6.06946   -17.85717 1.000 56.82924 ? 215 GLY   A CA  1 
ATOM   1649 C C   . GLY   A 1 216 ? 0.48547  7.36336   -17.10646 1.000 59.89909 ? 215 GLY   A C   1 
ATOM   1650 O O   . GLY   A 1 216 ? 0.29284  8.43966   -17.68463 1.000 60.52171 ? 215 GLY   A O   1 
ATOM   1651 N N   . ASP   A 1 217 ? 0.88956  7.29545   -15.84039 1.000 62.11816 ? 216 ASP   A N   1 
ATOM   1652 C CA  . ASP   A 1 217 ? 1.18590  8.50007   -15.06851 1.000 61.48973 ? 216 ASP   A CA  1 
ATOM   1653 C C   . ASP   A 1 217 ? 2.46706  9.13594   -15.59382 1.000 61.04876 ? 216 ASP   A C   1 
ATOM   1654 O O   . ASP   A 1 217 ? 3.54730  8.54840   -15.48356 1.000 61.98142 ? 216 ASP   A O   1 
ATOM   1655 C CB  . ASP   A 1 217 ? 1.32219  8.15998   -13.58701 1.000 65.55721 ? 216 ASP   A CB  1 
ATOM   1656 C CG  . ASP   A 1 217 ? -0.01379 7.91074   -12.91544 1.000 70.66188 ? 216 ASP   A CG  1 
ATOM   1657 O OD1 . ASP   A 1 217 ? -0.71523 6.95385   -13.30855 1.000 71.78639 ? 216 ASP   A OD1 1 
ATOM   1658 O OD2 . ASP   A 1 217 ? -0.35785 8.67045   -11.98390 1.000 72.43151 ? 216 ASP   A OD2 1 
ATOM   1659 N N   . ARG   A 1 218 ? 2.36209  10.34166  -16.16184 1.000 61.06413 ? 217 ARG   A N   1 
ATOM   1660 C CA  . ARG   A 1 218 ? 3.55139  11.00106  -16.68724 1.000 61.78855 ? 217 ARG   A CA  1 
ATOM   1661 C C   . ARG   A 1 218 ? 3.56507  12.50902  -16.45357 1.000 61.19219 ? 217 ARG   A C   1 
ATOM   1662 O O   . ARG   A 1 218 ? 4.40916  13.19941  -17.04058 1.000 62.19089 ? 217 ARG   A O   1 
ATOM   1663 C CB  . ARG   A 1 218 ? 3.71473  10.70434  -18.18821 1.000 65.30098 ? 217 ARG   A CB  1 
ATOM   1664 C CG  . ARG   A 1 218 ? 2.85635  11.54657  -19.12231 1.000 69.14543 ? 217 ARG   A CG  1 
ATOM   1665 C CD  . ARG   A 1 218 ? 3.72226  12.14573  -20.22366 1.000 75.09684 ? 217 ARG   A CD  1 
ATOM   1666 N NE  . ARG   A 1 218 ? 2.96999  12.99523  -21.13943 1.000 81.72694 ? 217 ARG   A NE  1 
ATOM   1667 C CZ  . ARG   A 1 218 ? 2.65273  14.26009  -20.89825 1.000 83.97574 ? 217 ARG   A CZ  1 
ATOM   1668 N NH1 . ARG   A 1 218 ? 2.96869  14.84621  -19.75468 1.000 81.74142 ? 217 ARG   A NH1 1 
ATOM   1669 N NH2 . ARG   A 1 218 ? 2.00021  14.95395  -21.82688 1.000 85.42220 ? 217 ARG   A NH2 1 
ATOM   1670 N N   . TRP   A 1 219 ? 2.68437  13.04223  -15.60088 1.000 61.26361 ? 218 TRP   A N   1 
ATOM   1671 C CA  . TRP   A 1 219 ? 2.65668  14.48565  -15.37783 1.000 60.30357 ? 218 TRP   A CA  1 
ATOM   1672 C C   . TRP   A 1 219 ? 3.96384  14.99371  -14.78247 1.000 59.77288 ? 218 TRP   A C   1 
ATOM   1673 O O   . TRP   A 1 219 ? 4.34562  16.14638  -15.01767 1.000 59.98480 ? 218 TRP   A O   1 
ATOM   1674 C CB  . TRP   A 1 219 ? 1.48071  14.86286  -14.47226 1.000 59.83473 ? 218 TRP   A CB  1 
ATOM   1675 C CG  . TRP   A 1 219 ? 1.52716  14.26174  -13.09242 1.000 58.27415 ? 218 TRP   A CG  1 
ATOM   1676 C CD1 . TRP   A 1 219 ? 0.90176  13.12350  -12.67453 1.000 57.86033 ? 218 TRP   A CD1 1 
ATOM   1677 C CD2 . TRP   A 1 219 ? 2.22476  14.77750  -11.94883 1.000 60.62171 ? 218 TRP   A CD2 1 
ATOM   1678 N NE1 . TRP   A 1 219 ? 1.17007  12.89511  -11.34662 1.000 57.08556 ? 218 TRP   A NE1 1 
ATOM   1679 C CE2 . TRP   A 1 219 ? 1.98060  13.89543  -10.87785 1.000 59.31039 ? 218 TRP   A CE2 1 
ATOM   1680 C CE3 . TRP   A 1 219 ? 3.03375  15.89640  -11.72825 1.000 62.68199 ? 218 TRP   A CE3 1 
ATOM   1681 C CZ2 . TRP   A 1 219 ? 2.51534  14.09874  -9.60560  1.000 60.63863 ? 218 TRP   A CZ2 1 
ATOM   1682 C CZ3 . TRP   A 1 219 ? 3.56777  16.09216  -10.46532 1.000 63.85301 ? 218 TRP   A CZ3 1 
ATOM   1683 C CH2 . TRP   A 1 219 ? 3.30453  15.19913  -9.42090  1.000 62.23783 ? 218 TRP   A CH2 1 
ATOM   1684 N N   . PHE   A 1 220 ? 4.66419  14.15412  -14.02186 1.000 58.60242 ? 219 PHE   A N   1 
ATOM   1685 C CA  . PHE   A 1 220 ? 5.90040  14.54655  -13.35696 1.000 58.23936 ? 219 PHE   A CA  1 
ATOM   1686 C C   . PHE   A 1 220 ? 7.09533  14.62325  -14.30078 1.000 59.01197 ? 219 PHE   A C   1 
ATOM   1687 O O   . PHE   A 1 220 ? 8.18497  15.00299  -13.85832 1.000 57.04950 ? 219 PHE   A O   1 
ATOM   1688 C CB  . PHE   A 1 220 ? 6.20447  13.57415  -12.21393 1.000 53.96173 ? 219 PHE   A CB  1 
ATOM   1689 C CG  . PHE   A 1 220 ? 6.20101  12.12972  -12.63124 1.000 54.68868 ? 219 PHE   A CG  1 
ATOM   1690 C CD1 . PHE   A 1 220 ? 5.02693  11.39175  -12.61715 1.000 55.38466 ? 219 PHE   A CD1 1 
ATOM   1691 C CD2 . PHE   A 1 220 ? 7.37071  11.50889  -13.03805 1.000 53.92127 ? 219 PHE   A CD2 1 
ATOM   1692 C CE1 . PHE   A 1 220 ? 5.01943  10.06272  -13.00248 1.000 54.03415 ? 219 PHE   A CE1 1 
ATOM   1693 C CE2 . PHE   A 1 220 ? 7.37042  10.17931  -13.42494 1.000 53.34529 ? 219 PHE   A CE2 1 
ATOM   1694 C CZ  . PHE   A 1 220 ? 6.19307  9.45562   -13.40721 1.000 52.82023 ? 219 PHE   A CZ  1 
ATOM   1695 N N   . LEU   A 1 221 ? 6.92647  14.27763  -15.57556 1.000 58.17266 ? 220 LEU   A N   1 
ATOM   1696 C CA  . LEU   A 1 221 ? 8.02178  14.34905  -16.53342 1.000 60.50353 ? 220 LEU   A CA  1 
ATOM   1697 C C   . LEU   A 1 221 ? 8.23192  15.79075  -16.98177 1.000 62.80050 ? 220 LEU   A C   1 
ATOM   1698 O O   . LEU   A 1 221 ? 7.27789  16.47898  -17.35856 1.000 63.10438 ? 220 LEU   A O   1 
ATOM   1699 C CB  . LEU   A 1 221 ? 7.73657  13.45368  -17.73867 1.000 61.01748 ? 220 LEU   A CB  1 
ATOM   1700 C CG  . LEU   A 1 221 ? 7.62117  11.94954  -17.48051 1.000 58.78506 ? 220 LEU   A CG  1 
ATOM   1701 C CD1 . LEU   A 1 221 ? 7.28588  11.21423  -18.76818 1.000 59.42291 ? 220 LEU   A CD1 1 
ATOM   1702 C CD2 . LEU   A 1 221 ? 8.90493  11.40846  -16.87348 1.000 57.25625 ? 220 LEU   A CD2 1 
ATOM   1703 N N   . ASN   A 1 222 ? 9.47985  16.24449  -16.94579 1.000 62.95969 ? 221 ASN   A N   1 
ATOM   1704 C CA  . ASN   A 1 222 ? 9.82361  17.62067  -17.27614 1.000 66.67775 ? 221 ASN   A CA  1 
ATOM   1705 C C   . ASN   A 1 222 ? 10.80328 17.65374  -18.44688 1.000 67.85354 ? 221 ASN   A C   1 
ATOM   1706 O O   . ASN   A 1 222 ? 11.25869 16.61936  -18.94131 1.000 67.77848 ? 221 ASN   A O   1 
ATOM   1707 C CB  . ASN   A 1 222 ? 10.39966 18.34724  -16.05555 1.000 65.80611 ? 221 ASN   A CB  1 
ATOM   1708 C CG  . ASN   A 1 222 ? 11.64412 17.67547  -15.49870 1.000 64.03711 ? 221 ASN   A CG  1 
ATOM   1709 O OD1 . ASN   A 1 222 ? 12.18064 16.73339  -16.08346 1.000 63.62491 ? 221 ASN   A OD1 1 
ATOM   1710 N ND2 . ASN   A 1 222 ? 12.11277 18.16771  -14.35870 1.000 64.00547 ? 221 ASN   A ND2 1 
ATOM   1711 N N   . ARG   A 1 223 ? 11.12888 18.86891  -18.88066 1.000 71.71527 ? 222 ARG   A N   1 
ATOM   1712 C CA  . ARG   A 1 223 ? 12.05557 19.09770  -19.98073 1.000 70.73796 ? 222 ARG   A CA  1 
ATOM   1713 C C   . ARG   A 1 223 ? 13.50384 19.21233  -19.52142 1.000 69.46946 ? 222 ARG   A C   1 
ATOM   1714 O O   . ARG   A 1 223 ? 14.38305 19.47192  -20.34994 1.000 73.64381 ? 222 ARG   A O   1 
ATOM   1715 C CB  . ARG   A 1 223 ? 11.66126 20.36774  -20.74961 1.000 74.82007 ? 222 ARG   A CB  1 
ATOM   1716 C CG  . ARG   A 1 223 ? 10.45081 20.21602  -21.66963 1.000 77.82125 ? 222 ARG   A CG  1 
ATOM   1717 C CD  . ARG   A 1 223 ? 9.13509  20.31901  -20.90894 1.000 82.96150 ? 222 ARG   A CD  1 
ATOM   1718 N NE  . ARG   A 1 223 ? 8.51865  21.63544  -21.03263 1.000 89.22092 ? 222 ARG   A NE  1 
ATOM   1719 C CZ  . ARG   A 1 223 ? 7.47293  22.04090  -20.32414 1.000 89.28959 ? 222 ARG   A CZ  1 
ATOM   1720 N NH1 . ARG   A 1 223 ? 6.91754  21.26581  -19.40636 1.000 84.31463 ? 222 ARG   A NH1 1 
ATOM   1721 N NH2 . ARG   A 1 223 ? 6.97414  23.25547  -20.53915 1.000 87.07637 ? 222 ARG   A NH2 1 
ATOM   1722 N N   . PHE   A 1 224 ? 13.77292 19.02008  -18.23449 1.000 67.64967 ? 223 PHE   A N   1 
ATOM   1723 C CA  . PHE   A 1 224 ? 15.09955 19.22853  -17.67895 1.000 64.99115 ? 223 PHE   A CA  1 
ATOM   1724 C C   . PHE   A 1 224 ? 15.90548 17.93273  -17.67349 1.000 63.78983 ? 223 PHE   A C   1 
ATOM   1725 O O   . PHE   A 1 224 ? 15.38482 16.83628  -17.88581 1.000 63.33001 ? 223 PHE   A O   1 
ATOM   1726 C CB  . PHE   A 1 224 ? 15.00912 19.77486  -16.25289 1.000 64.39846 ? 223 PHE   A CB  1 
ATOM   1727 C CG  . PHE   A 1 224 ? 14.25652 21.06807  -16.13610 1.000 65.56540 ? 223 PHE   A CG  1 
ATOM   1728 C CD1 . PHE   A 1 224 ? 12.87387 21.07558  -16.05439 1.000 68.15674 ? 223 PHE   A CD1 1 
ATOM   1729 C CD2 . PHE   A 1 224 ? 14.93220 22.27494  -16.08198 1.000 65.32222 ? 223 PHE   A CD2 1 
ATOM   1730 C CE1 . PHE   A 1 224 ? 12.17772 22.26216  -15.93823 1.000 67.68725 ? 223 PHE   A CE1 1 
ATOM   1731 C CE2 . PHE   A 1 224 ? 14.24161 23.46565  -15.96324 1.000 65.40434 ? 223 PHE   A CE2 1 
ATOM   1732 C CZ  . PHE   A 1 224 ? 12.86177 23.45880  -15.89201 1.000 65.46073 ? 223 PHE   A CZ  1 
ATOM   1733 N N   . THR   A 1 225 ? 17.20440 18.08020  -17.42249 1.000 62.87999 ? 224 THR   A N   1 
ATOM   1734 C CA  . THR   A 1 225 ? 18.09173 16.96827  -17.11933 1.000 61.70764 ? 224 THR   A CA  1 
ATOM   1735 C C   . THR   A 1 225 ? 19.03229 17.41706  -16.00838 1.000 62.97583 ? 224 THR   A C   1 
ATOM   1736 O O   . THR   A 1 225 ? 19.00067 18.57226  -15.57180 1.000 62.11028 ? 224 THR   A O   1 
ATOM   1737 C CB  . THR   A 1 225 ? 18.86835 16.50538  -18.35788 1.000 61.86800 ? 224 THR   A CB  1 
ATOM   1738 O OG1 . THR   A 1 225 ? 19.57121 15.29354  -18.05595 1.000 60.57280 ? 224 THR   A OG1 1 
ATOM   1739 C CG2 . THR   A 1 225 ? 19.86846 17.56580  -18.78449 1.000 61.32765 ? 224 THR   A CG2 1 
ATOM   1740 N N   . THR   A 1 226 ? 19.87516 16.49858  -15.54281 1.000 62.26856 ? 225 THR   A N   1 
ATOM   1741 C CA  . THR   A 1 226 ? 20.82384 16.80441  -14.48143 1.000 62.84343 ? 225 THR   A CA  1 
ATOM   1742 C C   . THR   A 1 226 ? 21.99975 15.84184  -14.58202 1.000 62.04683 ? 225 THR   A C   1 
ATOM   1743 O O   . THR   A 1 226 ? 22.01372 14.92893  -15.41290 1.000 61.46804 ? 225 THR   A O   1 
ATOM   1744 C CB  . THR   A 1 226 ? 20.15964 16.72256  -13.10226 1.000 63.83428 ? 225 THR   A CB  1 
ATOM   1745 O OG1 . THR   A 1 226 ? 21.08172 17.16113  -12.09636 1.000 66.68737 ? 225 THR   A OG1 1 
ATOM   1746 C CG2 . THR   A 1 226 ? 19.73614 15.29363  -12.79996 1.000 60.63928 ? 225 THR   A CG2 1 
ATOM   1747 N N   . THR   A 1 227 ? 22.99828 16.06177  -13.73339 1.000 66.23308 ? 226 THR   A N   1 
ATOM   1748 C CA  . THR   A 1 227 ? 24.11278 15.14179  -13.57973 1.000 65.18514 ? 226 THR   A CA  1 
ATOM   1749 C C   . THR   A 1 227 ? 23.97099 14.39505  -12.26027 1.000 63.41792 ? 226 THR   A C   1 
ATOM   1750 O O   . THR   A 1 227 ? 23.20166 14.78722  -11.37831 1.000 65.61509 ? 226 THR   A O   1 
ATOM   1751 C CB  . THR   A 1 227 ? 25.46141 15.87190  -13.62504 1.000 65.47654 ? 226 THR   A CB  1 
ATOM   1752 O OG1 . THR   A 1 227 ? 25.74331 16.43720  -12.34030 1.000 67.35223 ? 226 THR   A OG1 1 
ATOM   1753 C CG2 . THR   A 1 227 ? 25.43588 16.98320  -14.66216 1.000 64.21922 ? 226 THR   A CG2 1 
ATOM   1754 N N   . LEU   A 1 228 ? 24.72979 13.30460  -12.13509 1.000 60.68764 ? 227 LEU   A N   1 
ATOM   1755 C CA  . LEU   A 1 228 ? 24.61292 12.45947  -10.95156 1.000 62.44368 ? 227 LEU   A CA  1 
ATOM   1756 C C   . LEU   A 1 228 ? 25.00231 13.21834  -9.68718  1.000 64.18213 ? 227 LEU   A C   1 
ATOM   1757 O O   . LEU   A 1 228 ? 24.33015 13.10414  -8.65604  1.000 63.50362 ? 227 LEU   A O   1 
ATOM   1758 C CB  . LEU   A 1 228 ? 25.46621 11.20361  -11.12428 1.000 60.04554 ? 227 LEU   A CB  1 
ATOM   1759 C CG  . LEU   A 1 228 ? 25.06710 9.98931   -10.28567 1.000 59.85444 ? 227 LEU   A CG  1 
ATOM   1760 C CD1 . LEU   A 1 228 ? 23.55880 9.80645   -10.29866 1.000 58.02960 ? 227 LEU   A CD1 1 
ATOM   1761 C CD2 . LEU   A 1 228 ? 25.75786 8.74173   -10.81157 1.000 60.69631 ? 227 LEU   A CD2 1 
ATOM   1762 N N   . ASN   A 1 229 ? 26.07797 14.00902  -9.74842  1.000 64.52556 ? 228 ASN   A N   1 
ATOM   1763 C CA  . ASN   A 1 229 ? 26.44491 14.84397  -8.60681  1.000 66.18788 ? 228 ASN   A CA  1 
ATOM   1764 C C   . ASN   A 1 229 ? 25.42118 15.95209  -8.38150  1.000 70.15061 ? 228 ASN   A C   1 
ATOM   1765 O O   . ASN   A 1 229 ? 25.07387 16.26705  -7.23227  1.000 72.35355 ? 228 ASN   A O   1 
ATOM   1766 C CB  . ASN   A 1 229 ? 27.83904 15.43663  -8.81554  1.000 68.41790 ? 228 ASN   A CB  1 
ATOM   1767 C CG  . ASN   A 1 229 ? 28.92911 14.38189  -8.81952  1.000 63.01265 ? 228 ASN   A CG  1 
ATOM   1768 O OD1 . ASN   A 1 229 ? 28.65669 13.18928  -8.95679  1.000 63.53886 ? 228 ASN   A OD1 1 
ATOM   1769 N ND2 . ASN   A 1 229 ? 30.17335 14.81922  -8.66955  1.000 60.12664 ? 228 ASN   A ND2 1 
ATOM   1770 N N   . ASP   A 1 230 ? 24.93853 16.56536  -9.46636  1.000 76.39723 ? 229 ASP   A N   1 
ATOM   1771 C CA  . ASP   A 1 230 ? 23.90127 17.58387  -9.36596  1.000 78.00236 ? 229 ASP   A CA  1 
ATOM   1772 C C   . ASP   A 1 230 ? 22.54106 16.99859  -9.03231  1.000 79.86113 ? 229 ASP   A C   1 
ATOM   1773 O O   . ASP   A 1 230 ? 21.58488 17.76190  -8.85259  1.000 83.01015 ? 229 ASP   A O   1 
ATOM   1774 C CB  . ASP   A 1 230 ? 23.81202 18.39654  -10.65810 1.000 80.81015 ? 229 ASP   A CB  1 
ATOM   1775 C CG  . ASP   A 1 230 ? 25.03907 19.25469  -10.88983 1.000 85.53371 ? 229 ASP   A CG  1 
ATOM   1776 O OD1 . ASP   A 1 230 ? 25.26980 19.66412  -12.04595 1.000 85.82102 ? 229 ASP   A OD1 1 
ATOM   1777 O OD2 . ASP   A 1 230 ? 25.78361 19.50410  -9.91711  1.000 87.52666 ? 229 ASP   A OD2 1 
ATOM   1778 N N   . PHE   A 1 231 ? 22.43430 15.67754  -8.91450  1.000 70.41282 ? 230 PHE   A N   1 
ATOM   1779 C CA  . PHE   A 1 231 ? 21.27714 15.05956  -8.28532  1.000 68.06086 ? 230 PHE   A CA  1 
ATOM   1780 C C   . PHE   A 1 231 ? 21.53336 14.66839  -6.83817  1.000 68.14668 ? 230 PHE   A C   1 
ATOM   1781 O O   . PHE   A 1 231 ? 20.61552 14.73837  -6.01398  1.000 67.44856 ? 230 PHE   A O   1 
ATOM   1782 C CB  . PHE   A 1 231 ? 20.83402 13.82073  -9.06709  1.000 63.43482 ? 230 PHE   A CB  1 
ATOM   1783 C CG  . PHE   A 1 231 ? 19.79623 13.00762  -8.35521  1.000 61.41024 ? 230 PHE   A CG  1 
ATOM   1784 C CD1 . PHE   A 1 231 ? 18.48423 13.44678  -8.28409  1.000 58.26036 ? 230 PHE   A CD1 1 
ATOM   1785 C CD2 . PHE   A 1 231 ? 20.13282 11.80993  -7.74796  1.000 59.95564 ? 230 PHE   A CD2 1 
ATOM   1786 C CE1 . PHE   A 1 231 ? 17.52913 12.70704  -7.62596  1.000 56.96893 ? 230 PHE   A CE1 1 
ATOM   1787 C CE2 . PHE   A 1 231 ? 19.18180 11.06574  -7.08927  1.000 59.05562 ? 230 PHE   A CE2 1 
ATOM   1788 C CZ  . PHE   A 1 231 ? 17.87678 11.51504  -7.02803  1.000 56.82954 ? 230 PHE   A CZ  1 
ATOM   1789 N N   . ASN   A 1 232 ? 22.76525 14.27545  -6.51004  1.000 69.45498 ? 231 ASN   A N   1 
ATOM   1790 C CA  . ASN   A 1 232 ? 23.07492 13.85988  -5.14478  1.000 67.58192 ? 231 ASN   A CA  1 
ATOM   1791 C C   . ASN   A 1 232 ? 23.09782 15.04472  -4.18649  1.000 70.94163 ? 231 ASN   A C   1 
ATOM   1792 O O   . ASN   A 1 232 ? 22.64214 14.92741  -3.04088  1.000 72.55184 ? 231 ASN   A O   1 
ATOM   1793 C CB  . ASN   A 1 232 ? 24.40770 13.10491  -5.11006  1.000 65.20255 ? 231 ASN   A CB  1 
ATOM   1794 C CG  . ASN   A 1 232 ? 24.29433 11.68990  -5.65834  1.000 62.61489 ? 231 ASN   A CG  1 
ATOM   1795 O OD1 . ASN   A 1 232 ? 23.25736 11.04201  -5.53120  1.000 62.54608 ? 231 ASN   A OD1 1 
ATOM   1796 N ND2 . ASN   A 1 232 ? 25.37239 11.20401  -6.26868  1.000 61.30800 ? 231 ASN   A ND2 1 
ATOM   1797 N N   . LEU   A 1 233 ? 23.62332 16.19450  -4.62754  1.000 73.15251 ? 232 LEU   A N   1 
ATOM   1798 C CA  . LEU   A 1 233 ? 23.62465 17.37721  -3.75228  1.000 75.23451 ? 232 LEU   A CA  1 
ATOM   1799 C C   . LEU   A 1 233 ? 22.20965 17.87959  -3.45267  1.000 72.22168 ? 232 LEU   A C   1 
ATOM   1800 O O   . LEU   A 1 233 ? 22.04416 18.73462  -2.56840  1.000 72.32041 ? 232 LEU   A O   1 
ATOM   1801 C CB  . LEU   A 1 233 ? 24.47226 18.49678  -4.37187  1.000 75.75227 ? 232 LEU   A CB  1 
ATOM   1802 C CG  . LEU   A 1 233 ? 25.93891 18.58937  -3.94610  1.000 82.12748 ? 232 LEU   A CG  1 
ATOM   1803 C CD1 . LEU   A 1 233 ? 26.04497 18.79580  -2.43860  1.000 81.44118 ? 232 LEU   A CD1 1 
ATOM   1804 C CD2 . LEU   A 1 233 ? 26.71083 17.34896  -4.37410  1.000 78.24660 ? 232 LEU   A CD2 1 
ATOM   1805 N N   . VAL   A 1 234 ? 21.20382 17.38984  -4.17505  1.000 71.65488 ? 233 VAL   A N   1 
ATOM   1806 C CA  . VAL   A 1 234 ? 19.81895 17.60932  -3.79315  1.000 71.88639 ? 233 VAL   A CA  1 
ATOM   1807 C C   . VAL   A 1 234 ? 19.25719 16.41674  -3.00984  1.000 70.79034 ? 233 VAL   A C   1 
ATOM   1808 O O   . VAL   A 1 234 ? 18.41634 16.60122  -2.11679  1.000 68.46682 ? 233 VAL   A O   1 
ATOM   1809 C CB  . VAL   A 1 234 ? 18.90571 17.93763  -5.00532  1.000 70.42356 ? 233 VAL   A CB  1 
ATOM   1810 C CG1 . VAL   A 1 234 ? 17.65273 18.66756  -4.54203  1.000 69.72661 ? 233 VAL   A CG1 1 
ATOM   1811 C CG2 . VAL   A 1 234 ? 19.64221 18.74594  -6.05497  1.000 70.30573 ? 233 VAL   A CG2 1 
ATOM   1812 N N   . ALA   A 1 235 ? 19.72126 15.19673  -3.28869  1.000 70.86292 ? 234 ALA   A N   1 
ATOM   1813 C CA  . ALA   A 1 235 ? 19.19240 14.03113  -2.58004  1.000 65.97557 ? 234 ALA   A CA  1 
ATOM   1814 C C   . ALA   A 1 235 ? 19.61641 14.02392  -1.12376  1.000 65.95366 ? 234 ALA   A C   1 
ATOM   1815 O O   . ALA   A 1 235 ? 18.83217 13.63611  -0.25400  1.000 64.42227 ? 234 ALA   A O   1 
ATOM   1816 C CB  . ALA   A 1 235 ? 19.65125 12.73801  -3.24355  1.000 68.25054 ? 234 ALA   A CB  1 
ATOM   1817 N N   . MET   A 1 236 ? 20.85983 14.42884  -0.84160  1.000 68.55021 ? 235 MET   A N   1 
ATOM   1818 C CA  . MET   A 1 236 ? 21.34168 14.44001  0.53725   1.000 69.32569 ? 235 MET   A CA  1 
ATOM   1819 C C   . MET   A 1 236 ? 20.56551 15.42751  1.40443   1.000 68.47175 ? 235 MET   A C   1 
ATOM   1820 O O   . MET   A 1 236 ? 20.40869 15.20623  2.61252   1.000 67.55365 ? 235 MET   A O   1 
ATOM   1821 C CB  . MET   A 1 236 ? 22.83972 14.76140  0.56150   1.000 72.13656 ? 235 MET   A CB  1 
ATOM   1822 C CG  . MET   A 1 236 ? 23.73018 13.53737  0.42425   1.000 73.12002 ? 235 MET   A CG  1 
ATOM   1823 S SD  . MET   A 1 236 ? 25.44783 13.93281  0.03714   1.000 94.42899 ? 235 MET   A SD  1 
ATOM   1824 C CE  . MET   A 1 236 ? 25.95725 14.82840  1.50258   1.000 74.44927 ? 235 MET   A CE  1 
ATOM   1825 N N   . LYS   A 1 237 ? 20.07195 16.51699  0.81189   1.000 68.28682 ? 236 LYS   A N   1 
ATOM   1826 C CA  . LYS   A 1 237 ? 19.27683 17.47186  1.57670   1.000 68.00909 ? 236 LYS   A CA  1 
ATOM   1827 C C   . LYS   A 1 237 ? 17.99753 16.83095  2.09903   1.000 66.45595 ? 236 LYS   A C   1 
ATOM   1828 O O   . LYS   A 1 237 ? 17.56569 17.11523  3.22229   1.000 66.85196 ? 236 LYS   A O   1 
ATOM   1829 C CB  . LYS   A 1 237 ? 18.94473 18.69268  0.71821   1.000 69.41012 ? 236 LYS   A CB  1 
ATOM   1830 C CG  . LYS   A 1 237 ? 18.14555 19.76180  1.45485   1.000 70.02519 ? 236 LYS   A CG  1 
ATOM   1831 C CD  . LYS   A 1 237 ? 19.05818 20.81336  2.06667   1.000 75.48010 ? 236 LYS   A CD  1 
ATOM   1832 C CE  . LYS   A 1 237 ? 18.48203 21.37640  3.35793   1.000 72.41742 ? 236 LYS   A CE  1 
ATOM   1833 N NZ  . LYS   A 1 237 ? 18.60980 20.40671  4.48395   1.000 66.56833 ? 236 LYS   A NZ  1 
ATOM   1834 N N   . TYR   A 1 238 ? 17.38255 15.95539  1.30229   1.000 66.42268 ? 237 TYR   A N   1 
ATOM   1835 C CA  . TYR   A 1 238 ? 16.10394 15.34299  1.63649   1.000 63.55301 ? 237 TYR   A CA  1 
ATOM   1836 C C   . TYR   A 1 238 ? 16.25118 13.92656  2.18549   1.000 62.15904 ? 237 TYR   A C   1 
ATOM   1837 O O   . TYR   A 1 238 ? 15.27614 13.16665  2.18538   1.000 59.69145 ? 237 TYR   A O   1 
ATOM   1838 C CB  . TYR   A 1 238 ? 15.18861 15.34539  0.41134   1.000 61.32128 ? 237 TYR   A CB  1 
ATOM   1839 C CG  . TYR   A 1 238 ? 14.73246 16.72616  -0.00229  1.000 62.36684 ? 237 TYR   A CG  1 
ATOM   1840 C CD1 . TYR   A 1 238 ? 15.48546 17.49540  -0.87977  1.000 63.27448 ? 237 TYR   A CD1 1 
ATOM   1841 C CD2 . TYR   A 1 238 ? 13.54809 17.26130  0.48821   1.000 63.06526 ? 237 TYR   A CD2 1 
ATOM   1842 C CE1 . TYR   A 1 238 ? 15.07002 18.75924  -1.25779  1.000 63.70234 ? 237 TYR   A CE1 1 
ATOM   1843 C CE2 . TYR   A 1 238 ? 13.12476 18.52318  0.11703   1.000 61.39227 ? 237 TYR   A CE2 1 
ATOM   1844 C CZ  . TYR   A 1 238 ? 13.88814 19.26739  -0.75564  1.000 62.22704 ? 237 TYR   A CZ  1 
ATOM   1845 O OH  . TYR   A 1 238 ? 13.46622 20.52343  -1.12650  1.000 63.27684 ? 237 TYR   A OH  1 
ATOM   1846 N N   . ASN   A 1 239 ? 17.44235 13.56544  2.65948   1.000 63.33148 ? 238 ASN   A N   1 
ATOM   1847 C CA  . ASN   A 1 239 ? 17.72294 12.24539  3.22513   1.000 61.16531 ? 238 ASN   A CA  1 
ATOM   1848 C C   . ASN   A 1 239 ? 17.35267 11.13090  2.24523   1.000 58.15465 ? 238 ASN   A C   1 
ATOM   1849 O O   . ASN   A 1 239 ? 16.54582 10.24600  2.53243   1.000 57.65812 ? 238 ASN   A O   1 
ATOM   1850 C CB  . ASN   A 1 239 ? 17.01394 12.05856  4.56960   1.000 60.88817 ? 238 ASN   A CB  1 
ATOM   1851 C CG  . ASN   A 1 239 ? 17.72909 12.76352  5.70717   1.000 64.72396 ? 238 ASN   A CG  1 
ATOM   1852 O OD1 . ASN   A 1 239 ? 18.92265 13.05378  5.61914   1.000 63.46482 ? 238 ASN   A OD1 1 
ATOM   1853 N ND2 . ASN   A 1 239 ? 17.00377 13.03632  6.78539   1.000 64.74565 ? 238 ASN   A ND2 1 
ATOM   1854 N N   . TYR   A 1 240 ? 17.96237 11.19744  1.06661   1.000 59.59236 ? 239 TYR   A N   1 
ATOM   1855 C CA  . TYR   A 1 240 ? 17.86937 10.15093  0.06061   1.000 58.70831 ? 239 TYR   A CA  1 
ATOM   1856 C C   . TYR   A 1 240 ? 19.21500 9.44813   -0.05240  1.000 61.53620 ? 239 TYR   A C   1 
ATOM   1857 O O   . TYR   A 1 240 ? 20.26587 10.09404  0.01082   1.000 60.97467 ? 239 TYR   A O   1 
ATOM   1858 C CB  . TYR   A 1 240 ? 17.46472 10.72730  -1.29912  1.000 57.83764 ? 239 TYR   A CB  1 
ATOM   1859 C CG  . TYR   A 1 240 ? 15.97794 10.72159  -1.57316  1.000 54.58187 ? 239 TYR   A CG  1 
ATOM   1860 C CD1 . TYR   A 1 240 ? 15.09039 11.37395  -0.72734  1.000 53.90916 ? 239 TYR   A CD1 1 
ATOM   1861 C CD2 . TYR   A 1 240 ? 15.46508 10.07733  -2.69068  1.000 48.77778 ? 239 TYR   A CD2 1 
ATOM   1862 C CE1 . TYR   A 1 240 ? 13.72985 11.37113  -0.97949  1.000 52.02378 ? 239 TYR   A CE1 1 
ATOM   1863 C CE2 . TYR   A 1 240 ? 14.10741 10.07023  -2.95254  1.000 49.70928 ? 239 TYR   A CE2 1 
ATOM   1864 C CZ  . TYR   A 1 240 ? 13.24385 10.71900  -2.09434  1.000 49.69122 ? 239 TYR   A CZ  1 
ATOM   1865 O OH  . TYR   A 1 240 ? 11.89125 10.71398  -2.35206  1.000 50.68728 ? 239 TYR   A OH  1 
ATOM   1866 N N   . GLU   A 1 241 ? 19.17971 8.12743   -0.20895  1.000 62.87871 ? 240 GLU   A N   1 
ATOM   1867 C CA  . GLU   A 1 241 ? 20.41419 7.36877   -0.35449  1.000 65.35867 ? 240 GLU   A CA  1 
ATOM   1868 C C   . GLU   A 1 241 ? 21.15991 7.82698   -1.60595  1.000 66.83658 ? 240 GLU   A C   1 
ATOM   1869 O O   . GLU   A 1 241 ? 20.53434 8.08096   -2.64253  1.000 66.45387 ? 240 GLU   A O   1 
ATOM   1870 C CB  . GLU   A 1 241 ? 20.12562 5.86795   -0.43756  1.000 63.81980 ? 240 GLU   A CB  1 
ATOM   1871 C CG  . GLU   A 1 241 ? 19.73893 5.21643   0.88436   1.000 66.93191 ? 240 GLU   A CG  1 
ATOM   1872 C CD  . GLU   A 1 241 ? 20.87207 5.21364   1.89888   1.000 78.89932 ? 240 GLU   A CD  1 
ATOM   1873 O OE1 . GLU   A 1 241 ? 20.77833 5.94946   2.90418   1.000 85.16673 ? 240 GLU   A OE1 1 
ATOM   1874 O OE2 . GLU   A 1 241 ? 21.86023 4.47659   1.68977   1.000 79.95036 ? 240 GLU   A OE2 1 
ATOM   1875 N N   . PRO   A 1 242 ? 22.48444 7.96103   -1.54291  1.000 63.89495 ? 241 PRO   A N   1 
ATOM   1876 C CA  . PRO   A 1 242 ? 23.23420 8.42448   -2.71649  1.000 61.43113 ? 241 PRO   A CA  1 
ATOM   1877 C C   . PRO   A 1 242 ? 23.07052 7.47905   -3.89683  1.000 62.13496 ? 241 PRO   A C   1 
ATOM   1878 O O   . PRO   A 1 242 ? 23.14554 6.25647   -3.75609  1.000 62.26470 ? 241 PRO   A O   1 
ATOM   1879 C CB  . PRO   A 1 242 ? 24.68413 8.45780   -2.22016  1.000 62.62170 ? 241 PRO   A CB  1 
ATOM   1880 C CG  . PRO   A 1 242 ? 24.57299 8.59079   -0.73732  1.000 61.37770 ? 241 PRO   A CG  1 
ATOM   1881 C CD  . PRO   A 1 242 ? 23.34660 7.81273   -0.35861  1.000 63.99020 ? 241 PRO   A CD  1 
ATOM   1882 N N   . LEU   A 1 243 ? 22.83989 8.06347   -5.06937  1.000 60.89867 ? 242 LEU   A N   1 
ATOM   1883 C CA  . LEU   A 1 243 ? 22.67132 7.30377   -6.30069  1.000 58.97765 ? 242 LEU   A CA  1 
ATOM   1884 C C   . LEU   A 1 243 ? 24.04403 7.04293   -6.90699  1.000 57.85473 ? 242 LEU   A C   1 
ATOM   1885 O O   . LEU   A 1 243 ? 24.81169 7.98215   -7.14223  1.000 57.69298 ? 242 LEU   A O   1 
ATOM   1886 C CB  . LEU   A 1 243 ? 21.77936 8.06044   -7.28370  1.000 57.14997 ? 242 LEU   A CB  1 
ATOM   1887 C CG  . LEU   A 1 243 ? 21.17922 7.26594   -8.44465  1.000 57.00903 ? 242 LEU   A CG  1 
ATOM   1888 C CD1 . LEU   A 1 243 ? 20.24956 6.18878   -7.92295  1.000 52.66815 ? 242 LEU   A CD1 1 
ATOM   1889 C CD2 . LEU   A 1 243 ? 20.43007 8.19138   -9.37722  1.000 58.89502 ? 242 LEU   A CD2 1 
ATOM   1890 N N   . THR   A 1 244 ? 24.35409 5.77429   -7.14557  1.000 58.59095 ? 243 THR   A N   1 
ATOM   1891 C CA  . THR   A 1 244 ? 25.62394 5.36231   -7.72287  1.000 57.30254 ? 243 THR   A CA  1 
ATOM   1892 C C   . THR   A 1 244 ? 25.42352 4.94471   -9.17390  1.000 57.42055 ? 243 THR   A C   1 
ATOM   1893 O O   . THR   A 1 244 ? 24.29874 4.75251   -9.64229  1.000 54.85013 ? 243 THR   A O   1 
ATOM   1894 C CB  . THR   A 1 244 ? 26.23902 4.21215   -6.91753  1.000 57.49879 ? 243 THR   A CB  1 
ATOM   1895 O OG1 . THR   A 1 244 ? 25.40488 3.05258   -7.02897  1.000 57.98216 ? 243 THR   A OG1 1 
ATOM   1896 C CG2 . THR   A 1 244 ? 26.35934 4.59674   -5.45006  1.000 56.64595 ? 243 THR   A CG2 1 
ATOM   1897 N N   . GLN   A 1 245 ? 26.54218 4.81033   -9.89111  1.000 57.25761 ? 244 GLN   A N   1 
ATOM   1898 C CA  . GLN   A 1 245 ? 26.47596 4.34579   -11.27317 1.000 57.84748 ? 244 GLN   A CA  1 
ATOM   1899 C C   . GLN   A 1 245 ? 25.96941 2.90991   -11.35250 1.000 57.56558 ? 244 GLN   A C   1 
ATOM   1900 O O   . GLN   A 1 245 ? 25.37742 2.51675   -12.36550 1.000 56.31906 ? 244 GLN   A O   1 
ATOM   1901 C CB  . GLN   A 1 245 ? 27.84848 4.48139   -11.93808 1.000 59.52793 ? 244 GLN   A CB  1 
ATOM   1902 C CG  . GLN   A 1 245 ? 27.88218 4.10402   -13.41493 1.000 59.56536 ? 244 GLN   A CG  1 
ATOM   1903 C CD  . GLN   A 1 245 ? 26.85283 4.85681   -14.24075 1.000 61.07336 ? 244 GLN   A CD  1 
ATOM   1904 O OE1 . GLN   A 1 245 ? 26.82161 6.08736   -14.24701 1.000 60.99307 ? 244 GLN   A OE1 1 
ATOM   1905 N NE2 . GLN   A 1 245 ? 25.99910 4.11596   -14.93879 1.000 60.98665 ? 244 GLN   A NE2 1 
ATOM   1906 N N   . ASP   A 1 246 ? 26.17644 2.12127   -10.29305 1.000 56.57607 ? 245 ASP   A N   1 
ATOM   1907 C CA  . ASP   A 1 246 ? 25.58610 0.78785   -10.23834 1.000 56.66684 ? 245 ASP   A CA  1 
ATOM   1908 C C   . ASP   A 1 246 ? 24.06530 0.86245   -10.19464 1.000 54.82432 ? 245 ASP   A C   1 
ATOM   1909 O O   . ASP   A 1 246 ? 23.37916 0.07497   -10.85664 1.000 54.66334 ? 245 ASP   A O   1 
ATOM   1910 C CB  . ASP   A 1 246 ? 26.11854 0.02284   -9.02810  1.000 57.36214 ? 245 ASP   A CB  1 
ATOM   1911 C CG  . ASP   A 1 246 ? 27.59085 -0.29833  -9.14569  1.000 61.75881 ? 245 ASP   A CG  1 
ATOM   1912 O OD1 . ASP   A 1 246 ? 28.41733 0.62486   -8.97886  1.000 61.09062 ? 245 ASP   A OD1 1 
ATOM   1913 O OD2 . ASP   A 1 246 ? 27.92067 -1.47467  -9.40840  1.000 63.10471 ? 245 ASP   A OD2 1 
ATOM   1914 N N   . HIS   A 1 247 ? 23.52023 1.80181   -9.41608  1.000 54.66264 ? 246 HIS   A N   1 
ATOM   1915 C CA  . HIS   A 1 247 ? 22.07638 2.01917   -9.41896  1.000 54.70029 ? 246 HIS   A CA  1 
ATOM   1916 C C   . HIS   A 1 247 ? 21.59139 2.45658   -10.79460 1.000 53.80887 ? 246 HIS   A C   1 
ATOM   1917 O O   . HIS   A 1 247 ? 20.52091 2.03470   -11.24932 1.000 52.51353 ? 246 HIS   A O   1 
ATOM   1918 C CB  . HIS   A 1 247 ? 21.69654 3.06782   -8.37503  1.000 54.68450 ? 246 HIS   A CB  1 
ATOM   1919 C CG  . HIS   A 1 247 ? 21.95122 2.64757   -6.96154  1.000 53.62469 ? 246 HIS   A CG  1 
ATOM   1920 N ND1 . HIS   A 1 247 ? 22.48200 3.50158   -6.01883  1.000 56.03667 ? 246 HIS   A ND1 1 
ATOM   1921 C CD2 . HIS   A 1 247 ? 21.73000 1.47388   -6.32395  1.000 53.58736 ? 246 HIS   A CD2 1 
ATOM   1922 C CE1 . HIS   A 1 247 ? 22.58789 2.86891   -4.86409  1.000 56.51283 ? 246 HIS   A CE1 1 
ATOM   1923 N NE2 . HIS   A 1 247 ? 22.13782 1.63688   -5.02183  1.000 57.18658 ? 246 HIS   A NE2 1 
ATOM   1924 N N   . VAL   A 1 248 ? 22.36143 3.31724   -11.46423 1.000 55.78909 ? 247 VAL   A N   1 
ATOM   1925 C CA  . VAL   A 1 248 ? 22.00653 3.75029   -12.81310 1.000 54.60830 ? 247 VAL   A CA  1 
ATOM   1926 C C   . VAL   A 1 248 ? 21.92317 2.55011   -13.74713 1.000 55.68327 ? 247 VAL   A C   1 
ATOM   1927 O O   . VAL   A 1 248 ? 20.96293 2.39955   -14.51263 1.000 54.82751 ? 247 VAL   A O   1 
ATOM   1928 C CB  . VAL   A 1 248 ? 23.01808 4.79271   -13.32286 1.000 55.16184 ? 247 VAL   A CB  1 
ATOM   1929 C CG1 . VAL   A 1 248 ? 22.67768 5.21781   -14.73850 1.000 54.16977 ? 247 VAL   A CG1 1 
ATOM   1930 C CG2 . VAL   A 1 248 ? 23.05641 5.99550   -12.39351 1.000 55.75423 ? 247 VAL   A CG2 1 
ATOM   1931 N N   . ASP   A 1 249 ? 22.92416 1.66862   -13.68605 1.000 56.52075 ? 248 ASP   A N   1 
ATOM   1932 C CA  . ASP   A 1 249 ? 22.93921 0.50873   -14.57210 1.000 58.03421 ? 248 ASP   A CA  1 
ATOM   1933 C C   . ASP   A 1 249 ? 21.81621 -0.46700  -14.23804 1.000 56.04487 ? 248 ASP   A C   1 
ATOM   1934 O O   . ASP   A 1 249 ? 21.22812 -1.07178  -15.14277 1.000 58.29633 ? 248 ASP   A O   1 
ATOM   1935 C CB  . ASP   A 1 249 ? 24.29945 -0.18598  -14.50823 1.000 58.70200 ? 248 ASP   A CB  1 
ATOM   1936 C CG  . ASP   A 1 249 ? 25.34391 0.50378   -15.36276 1.000 61.07459 ? 248 ASP   A CG  1 
ATOM   1937 O OD1 . ASP   A 1 249 ? 24.96058 1.15351   -16.35947 1.000 63.76696 ? 248 ASP   A OD1 1 
ATOM   1938 O OD2 . ASP   A 1 249 ? 26.54629 0.39345   -15.04202 1.000 64.85423 ? 248 ASP   A OD2 1 
ATOM   1939 N N   . ILE   A 1 250 ? 21.50635 -0.63955  -12.94911 1.000 54.70705 ? 249 ILE   A N   1 
ATOM   1940 C CA  . ILE   A 1 250 ? 20.37255 -1.48023  -12.56655 1.000 51.38271 ? 249 ILE   A CA  1 
ATOM   1941 C C   . ILE   A 1 250 ? 19.08688 -0.94759  -13.18675 1.000 51.26330 ? 249 ILE   A C   1 
ATOM   1942 O O   . ILE   A 1 250 ? 18.22448 -1.71759  -13.62870 1.000 50.47107 ? 249 ILE   A O   1 
ATOM   1943 C CB  . ILE   A 1 250 ? 20.26338 -1.57520  -11.03216 1.000 51.64675 ? 249 ILE   A CB  1 
ATOM   1944 C CG1 . ILE   A 1 250 ? 21.44170 -2.35780  -10.44907 1.000 48.81597 ? 249 ILE   A CG1 1 
ATOM   1945 C CG2 . ILE   A 1 250 ? 18.95516 -2.23218  -10.62256 1.000 48.96511 ? 249 ILE   A CG2 1 
ATOM   1946 C CD1 . ILE   A 1 250 ? 21.42796 -2.43165  -8.93842  1.000 48.71374 ? 249 ILE   A CD1 1 
ATOM   1947 N N   . LEU   A 1 251 ? 18.94367 0.37544   -13.24147 1.000 49.99143 ? 250 LEU   A N   1 
ATOM   1948 C CA  . LEU   A 1 251 ? 17.78635 1.00621   -13.86110 1.000 50.71985 ? 250 LEU   A CA  1 
ATOM   1949 C C   . LEU   A 1 251 ? 17.87290 1.03568   -15.37997 1.000 52.72914 ? 250 LEU   A C   1 
ATOM   1950 O O   . LEU   A 1 251 ? 16.98063 1.59878   -16.02379 1.000 50.66557 ? 250 LEU   A O   1 
ATOM   1951 C CB  . LEU   A 1 251 ? 17.62132 2.42875   -13.32570 1.000 49.07529 ? 250 LEU   A CB  1 
ATOM   1952 C CG  . LEU   A 1 251 ? 17.22665 2.52166   -11.85275 1.000 49.04087 ? 250 LEU   A CG  1 
ATOM   1953 C CD1 . LEU   A 1 251 ? 17.50216 3.91510   -11.32205 1.000 46.16332 ? 250 LEU   A CD1 1 
ATOM   1954 C CD2 . LEU   A 1 251 ? 15.75996 2.15632   -11.68027 1.000 47.06897 ? 250 LEU   A CD2 1 
ATOM   1955 N N   . GLY   A 1 252 ? 18.91669 0.44587   -15.95665 1.000 51.24013 ? 251 GLY   A N   1 
ATOM   1956 C CA  . GLY   A 1 252 ? 19.12462 0.43715   -17.38455 1.000 50.60907 ? 251 GLY   A CA  1 
ATOM   1957 C C   . GLY   A 1 252 ? 17.96453 -0.11938  -18.18632 1.000 49.39339 ? 251 GLY   A C   1 
ATOM   1958 O O   . GLY   A 1 252 ? 17.41362 0.56080   -19.05585 1.000 52.49496 ? 251 GLY   A O   1 
ATOM   1959 N N   . PRO   A 1 253 ? 17.58904 -1.37871  -17.93421 1.000 49.96313 ? 252 PRO   A N   1 
ATOM   1960 C CA  . PRO   A 1 253 ? 16.45585 -1.96494  -18.67532 1.000 51.18552 ? 252 PRO   A CA  1 
ATOM   1961 C C   . PRO   A 1 253 ? 15.17370 -1.14539  -18.60620 1.000 52.05117 ? 252 PRO   A C   1 
ATOM   1962 O O   . PRO   A 1 253 ? 14.46983 -1.02421  -19.61653 1.000 48.83034 ? 252 PRO   A O   1 
ATOM   1963 C CB  . PRO   A 1 253 ? 16.29371 -3.33855  -18.01166 1.000 49.25696 ? 252 PRO   A CB  1 
ATOM   1964 C CG  . PRO   A 1 253 ? 17.66212 -3.68042  -17.54197 1.000 50.21692 ? 252 PRO   A CG  1 
ATOM   1965 C CD  . PRO   A 1 253 ? 18.28532 -2.38275  -17.10834 1.000 50.24428 ? 252 PRO   A CD  1 
ATOM   1966 N N   . LEU   A 1 254 ? 14.85146 -0.57153  -17.44434 1.000 51.25026 ? 253 LEU   A N   1 
ATOM   1967 C CA  . LEU   A 1 254 ? 13.65843 0.26458   -17.34594 1.000 51.17821 ? 253 LEU   A CA  1 
ATOM   1968 C C   . LEU   A 1 254 ? 13.78883 1.51800   -18.20320 1.000 52.78156 ? 253 LEU   A C   1 
ATOM   1969 O O   . LEU   A 1 254 ? 12.84183 1.90638   -18.90190 1.000 49.79280 ? 253 LEU   A O   1 
ATOM   1970 C CB  . LEU   A 1 254 ? 13.39567 0.63693   -15.88746 1.000 49.53793 ? 253 LEU   A CB  1 
ATOM   1971 C CG  . LEU   A 1 254 ? 12.71493 -0.43215  -15.03298 1.000 49.21911 ? 253 LEU   A CG  1 
ATOM   1972 C CD1 . LEU   A 1 254 ? 12.42425 0.09962   -13.63585 1.000 46.94434 ? 253 LEU   A CD1 1 
ATOM   1973 C CD2 . LEU   A 1 254 ? 11.43888 -0.91155  -15.70802 1.000 50.68140 ? 253 LEU   A CD2 1 
ATOM   1974 N N   . SER   A 1 255 ? 14.95508 2.16718   -18.15754 1.000 50.36257 ? 254 SER   A N   1 
ATOM   1975 C CA  . SER   A 1 255 ? 15.17844 3.35030   -18.98118 1.000 49.95245 ? 254 SER   A CA  1 
ATOM   1976 C C   . SER   A 1 255 ? 15.06434 3.01765   -20.46292 1.000 50.80853 ? 254 SER   A C   1 
ATOM   1977 O O   . SER   A 1 255 ? 14.51699 3.80498   -21.24393 1.000 53.30493 ? 254 SER   A O   1 
ATOM   1978 C CB  . SER   A 1 255 ? 16.54691 3.95426   -18.66673 1.000 50.88126 ? 254 SER   A CB  1 
ATOM   1979 O OG  . SER   A 1 255 ? 17.55662 2.96243   -18.68662 1.000 54.49858 ? 254 SER   A OG  1 
ATOM   1980 N N   . ALA   A 1 256 ? 15.56234 1.84597   -20.86551 1.000 51.62487 ? 255 ALA   A N   1 
ATOM   1981 C CA  . ALA   A 1 256 ? 15.48765 1.44975   -22.26723 1.000 52.79657 ? 255 ALA   A CA  1 
ATOM   1982 C C   . ALA   A 1 256 ? 14.06574 1.09062   -22.67585 1.000 53.28918 ? 255 ALA   A C   1 
ATOM   1983 O O   . ALA   A 1 256 ? 13.67998 1.31258   -23.82806 1.000 53.85461 ? 255 ALA   A O   1 
ATOM   1984 C CB  . ALA   A 1 256 ? 16.42786 0.27489   -22.53498 1.000 50.36111 ? 255 ALA   A CB  1 
ATOM   1985 N N   . GLN   A 1 257 ? 13.27660 0.53163   -21.75698 1.000 51.48030 ? 256 GLN   A N   1 
ATOM   1986 C CA  . GLN   A 1 257 ? 11.89299 0.20377   -22.08539 1.000 54.94790 ? 256 GLN   A CA  1 
ATOM   1987 C C   . GLN   A 1 257 ? 11.03846 1.45921   -22.20240 1.000 53.16252 ? 256 GLN   A C   1 
ATOM   1988 O O   . GLN   A 1 257 ? 10.19428 1.55933   -23.10057 1.000 53.97413 ? 256 GLN   A O   1 
ATOM   1989 C CB  . GLN   A 1 257 ? 11.30942 -0.74451  -21.03823 1.000 54.06755 ? 256 GLN   A CB  1 
ATOM   1990 C CG  . GLN   A 1 257 ? 9.84079  -1.07407  -21.26151 1.000 55.68099 ? 256 GLN   A CG  1 
ATOM   1991 C CD  . GLN   A 1 257 ? 9.25900  -1.94385  -20.16391 1.000 60.74513 ? 256 GLN   A CD  1 
ATOM   1992 O OE1 . GLN   A 1 257 ? 9.99024  -2.60504  -19.42724 1.000 57.69466 ? 256 GLN   A OE1 1 
ATOM   1993 N NE2 . GLN   A 1 257 ? 7.93490  -1.94434  -20.04705 1.000 60.41926 ? 256 GLN   A NE2 1 
ATOM   1994 N N   . THR   A 1 258 ? 11.23991 2.42798   -21.30930 1.000 53.39763 ? 257 THR   A N   1 
ATOM   1995 C CA  . THR   A 1 258 ? 10.43382 3.64254   -21.33379 1.000 52.55223 ? 257 THR   A CA  1 
ATOM   1996 C C   . THR   A 1 258 ? 10.96612 4.70143   -22.28804 1.000 53.89026 ? 257 THR   A C   1 
ATOM   1997 O O   . THR   A 1 258 ? 10.21035 5.60093   -22.67366 1.000 56.84269 ? 257 THR   A O   1 
ATOM   1998 C CB  . THR   A 1 258 ? 10.33218 4.24830   -19.93042 1.000 50.97468 ? 257 THR   A CB  1 
ATOM   1999 O OG1 . THR   A 1 258 ? 11.64412 4.57105   -19.45363 1.000 51.01826 ? 257 THR   A OG1 1 
ATOM   2000 C CG2 . THR   A 1 258 ? 9.67922  3.26765   -18.97289 1.000 48.71789 ? 257 THR   A CG2 1 
ATOM   2001 N N   . GLY   A 1 259 ? 12.23293 4.61394   -22.68495 1.000 53.04910 ? 258 GLY   A N   1 
ATOM   2002 C CA  . GLY   A 1 259 ? 12.82836 5.65629   -23.49285 1.000 51.81034 ? 258 GLY   A CA  1 
ATOM   2003 C C   . GLY   A 1 259 ? 13.20498 6.89953   -22.72411 1.000 53.24127 ? 258 GLY   A C   1 
ATOM   2004 O O   . GLY   A 1 259 ? 13.37238 7.96292   -23.32899 1.000 54.05332 ? 258 GLY   A O   1 
ATOM   2005 N N   . ILE   A 1 260 ? 13.34413 6.79995   -21.40432 1.000 53.91720 ? 259 ILE   A N   1 
ATOM   2006 C CA  . ILE   A 1 260 ? 13.65489 7.93531   -20.54310 1.000 51.98867 ? 259 ILE   A CA  1 
ATOM   2007 C C   . ILE   A 1 260 ? 15.00680 7.68033   -19.89685 1.000 52.07506 ? 259 ILE   A C   1 
ATOM   2008 O O   . ILE   A 1 260 ? 15.16655 6.71007   -19.14560 1.000 50.98073 ? 259 ILE   A O   1 
ATOM   2009 C CB  . ILE   A 1 260 ? 12.57885 8.15373   -19.46837 1.000 49.82572 ? 259 ILE   A CB  1 
ATOM   2010 C CG1 . ILE   A 1 260 ? 11.19193 8.25286   -20.10310 1.000 49.83256 ? 259 ILE   A CG1 1 
ATOM   2011 C CG2 . ILE   A 1 260 ? 12.88726 9.40420   -18.66017 1.000 51.19892 ? 259 ILE   A CG2 1 
ATOM   2012 C CD1 . ILE   A 1 260 ? 10.07172 8.36532   -19.09314 1.000 49.89032 ? 259 ILE   A CD1 1 
ATOM   2013 N N   . ALA   A 1 261 ? 15.97379 8.54973   -20.18232 1.000 53.82256 ? 260 ALA   A N   1 
ATOM   2014 C CA  . ALA   A 1 261 ? 17.28398 8.43464   -19.55896 1.000 52.62740 ? 260 ALA   A CA  1 
ATOM   2015 C C   . ALA   A 1 261 ? 17.16215 8.55332   -18.04422 1.000 52.13872 ? 260 ALA   A C   1 
ATOM   2016 O O   . ALA   A 1 261 ? 16.27951 9.23923   -17.52061 1.000 51.90306 ? 260 ALA   A O   1 
ATOM   2017 C CB  . ALA   A 1 261 ? 18.22996 9.50797   -20.09885 1.000 51.21627 ? 260 ALA   A CB  1 
ATOM   2018 N N   . VAL   A 1 262 ? 18.06245 7.86414   -17.33879 1.000 52.43314 ? 261 VAL   A N   1 
ATOM   2019 C CA  . VAL   A 1 262 ? 18.01810 7.85097   -15.87882 1.000 52.00249 ? 261 VAL   A CA  1 
ATOM   2020 C C   . VAL   A 1 262 ? 18.21937 9.25570   -15.32219 1.000 53.45494 ? 261 VAL   A C   1 
ATOM   2021 O O   . VAL   A 1 262 ? 17.59115 9.63884   -14.32873 1.000 52.76138 ? 261 VAL   A O   1 
ATOM   2022 C CB  . VAL   A 1 262 ? 19.05944 6.86003   -15.32228 1.000 53.75097 ? 261 VAL   A CB  1 
ATOM   2023 C CG1 . VAL   A 1 262 ? 19.08984 6.90205   -13.79806 1.000 51.53783 ? 261 VAL   A CG1 1 
ATOM   2024 C CG2 . VAL   A 1 262 ? 18.75895 5.45084   -15.81046 1.000 52.40653 ? 261 VAL   A CG2 1 
ATOM   2025 N N   . LEU   A 1 263 ? 19.08025 10.05354  -15.96198 1.000 54.46820 ? 262 LEU   A N   1 
ATOM   2026 C CA  . LEU   A 1 263 ? 19.34535 11.39980  -15.46092 1.000 55.29545 ? 262 LEU   A CA  1 
ATOM   2027 C C   . LEU   A 1 263 ? 18.15274 12.33072  -15.66622 1.000 54.75963 ? 262 LEU   A C   1 
ATOM   2028 O O   . LEU   A 1 263 ? 17.91473 13.22264  -14.84276 1.000 57.01671 ? 262 LEU   A O   1 
ATOM   2029 C CB  . LEU   A 1 263 ? 20.59877 11.97305  -16.12703 1.000 57.34217 ? 262 LEU   A CB  1 
ATOM   2030 C CG  . LEU   A 1 263 ? 21.92767 11.27583  -15.81353 1.000 55.44395 ? 262 LEU   A CG  1 
ATOM   2031 C CD1 . LEU   A 1 263 ? 23.09807 12.04284  -16.41188 1.000 57.22103 ? 262 LEU   A CD1 1 
ATOM   2032 C CD2 . LEU   A 1 263 ? 22.11434 11.09670  -14.31198 1.000 55.77500 ? 262 LEU   A CD2 1 
ATOM   2033 N N   . ASP   A 1 264 ? 17.37985 12.13529  -16.73670 1.000 54.21681 ? 263 ASP   A N   1 
ATOM   2034 C CA  . ASP   A 1 264 ? 16.18038 12.94793  -16.92505 1.000 55.78822 ? 263 ASP   A CA  1 
ATOM   2035 C C   . ASP   A 1 264 ? 15.11796 12.61330  -15.88039 1.000 53.95631 ? 263 ASP   A C   1 
ATOM   2036 O O   . ASP   A 1 264 ? 14.48082 13.51523  -15.31340 1.000 55.21837 ? 263 ASP   A O   1 
ATOM   2037 C CB  . ASP   A 1 264 ? 15.63720 12.75568  -18.34092 1.000 57.32260 ? 263 ASP   A CB  1 
ATOM   2038 C CG  . ASP   A 1 264 ? 16.64412 13.14804  -19.41055 1.000 57.53948 ? 263 ASP   A CG  1 
ATOM   2039 O OD1 . ASP   A 1 264 ? 17.80456 13.44543  -19.05905 1.000 59.41602 ? 263 ASP   A OD1 1 
ATOM   2040 O OD2 . ASP   A 1 264 ? 16.27496 13.16342  -20.60294 1.000 57.93590 ? 263 ASP   A OD2 1 
ATOM   2041 N N   . MET   A 1 265 ? 14.91548 11.32083  -15.60900 1.000 52.94590 ? 264 MET   A N   1 
ATOM   2042 C CA  . MET   A 1 265 ? 14.04048 10.93038  -14.50940 1.000 52.41285 ? 264 MET   A CA  1 
ATOM   2043 C C   . MET   A 1 265 ? 14.56210 11.45850  -13.17853 1.000 52.26970 ? 264 MET   A C   1 
ATOM   2044 O O   . MET   A 1 265 ? 13.77168 11.79355  -12.28971 1.000 53.19342 ? 264 MET   A O   1 
ATOM   2045 C CB  . MET   A 1 265 ? 13.89512 9.40739   -14.46685 1.000 49.66327 ? 264 MET   A CB  1 
ATOM   2046 C CG  . MET   A 1 265 ? 12.80373 8.91549   -13.53246 1.000 49.78386 ? 264 MET   A CG  1 
ATOM   2047 S SD  . MET   A 1 265 ? 11.14449 9.28134   -14.14355 1.000 52.21182 ? 264 MET   A SD  1 
ATOM   2048 C CE  . MET   A 1 265 ? 10.85905 7.89331   -15.23931 1.000 47.83571 ? 264 MET   A CE  1 
ATOM   2049 N N   . CYS   A 1 266 ? 15.88639 11.55670  -13.03059 1.000 52.62668 ? 265 CYS   A N   1 
ATOM   2050 C CA  . CYS   A 1 266 ? 16.46057 12.15749  -11.83078 1.000 52.66297 ? 265 CYS   A CA  1 
ATOM   2051 C C   . CYS   A 1 266 ? 16.09965 13.63154  -11.72641 1.000 53.28595 ? 265 CYS   A C   1 
ATOM   2052 O O   . CYS   A 1 266 ? 15.84407 14.13729  -10.63062 1.000 53.39927 ? 265 CYS   A O   1 
ATOM   2053 C CB  . CYS   A 1 266 ? 17.97893 11.98588  -11.82727 1.000 53.17904 ? 265 CYS   A CB  1 
ATOM   2054 S SG  . CYS   A 1 266 ? 18.54763 10.31423  -11.48213 1.000 51.04992 ? 265 CYS   A SG  1 
ATOM   2055 N N   . ALA   A 1 267 ? 16.09900 14.34260  -12.85513 1.000 54.48071 ? 266 ALA   A N   1 
ATOM   2056 C CA  . ALA   A 1 267 ? 15.66791 15.73877  -12.84436 1.000 54.30844 ? 266 ALA   A CA  1 
ATOM   2057 C C   . ALA   A 1 267 ? 14.20448 15.85400  -12.43316 1.000 56.00787 ? 266 ALA   A C   1 
ATOM   2058 O O   . ALA   A 1 267 ? 13.83191 16.74572  -11.65668 1.000 56.24759 ? 266 ALA   A O   1 
ATOM   2059 C CB  . ALA   A 1 267 ? 15.89078 16.37156  -14.21681 1.000 58.74473 ? 266 ALA   A CB  1 
ATOM   2060 N N   . SER   A 1 268 ? 13.36044 14.95360  -12.94532 1.000 54.29253 ? 267 SER   A N   1 
ATOM   2061 C CA  . SER   A 1 268 ? 11.95754 14.93783  -12.53084 1.000 56.04490 ? 267 SER   A CA  1 
ATOM   2062 C C   . SER   A 1 268 ? 11.82429 14.68866  -11.03015 1.000 54.00976 ? 267 SER   A C   1 
ATOM   2063 O O   . SER   A 1 268 ? 11.02505 15.34531  -10.34832 1.000 53.63321 ? 267 SER   A O   1 
ATOM   2064 C CB  . SER   A 1 268 ? 11.18434 13.87986  -13.31951 1.000 55.22875 ? 267 SER   A CB  1 
ATOM   2065 O OG  . SER   A 1 268 ? 11.04709 14.24986  -14.68105 1.000 59.15082 ? 267 SER   A OG  1 
ATOM   2066 N N   . LEU   A 1 269 ? 12.60319 13.74309  -10.49819 1.000 53.42424 ? 268 LEU   A N   1 
ATOM   2067 C CA  . LEU   A 1 269 ? 12.55441 13.45314  -9.06688  1.000 52.44931 ? 268 LEU   A CA  1 
ATOM   2068 C C   . LEU   A 1 269 ? 13.06222 14.63251  -8.24486  1.000 53.54638 ? 268 LEU   A C   1 
ATOM   2069 O O   . LEU   A 1 269 ? 12.53559 14.91297  -7.16218  1.000 54.51699 ? 268 LEU   A O   1 
ATOM   2070 C CB  . LEU   A 1 269 ? 13.36021 12.18877  -8.76136  1.000 50.73165 ? 268 LEU   A CB  1 
ATOM   2071 C CG  . LEU   A 1 269 ? 13.66084 11.82200  -7.30476  1.000 49.58839 ? 268 LEU   A CG  1 
ATOM   2072 C CD1 . LEU   A 1 269 ? 12.39626 11.79812  -6.46079  1.000 50.77470 ? 268 LEU   A CD1 1 
ATOM   2073 C CD2 . LEU   A 1 269 ? 14.35595 10.47361  -7.24889  1.000 48.90731 ? 268 LEU   A CD2 1 
ATOM   2074 N N   . LYS   A 1 270 ? 14.08726 15.33110  -8.73873  1.000 54.61823 ? 269 LYS   A N   1 
ATOM   2075 C CA  . LYS   A 1 270 ? 14.55413 16.53746  -8.06373  1.000 55.76404 ? 269 LYS   A CA  1 
ATOM   2076 C C   . LYS   A 1 270 ? 13.45240 17.58326  -8.00399  1.000 57.75517 ? 269 LYS   A C   1 
ATOM   2077 O O   . LYS   A 1 270 ? 13.25080 18.22806  -6.96773  1.000 57.90243 ? 269 LYS   A O   1 
ATOM   2078 C CB  . LYS   A 1 270 ? 15.78279 17.11000  -8.77210  1.000 55.59618 ? 269 LYS   A CB  1 
ATOM   2079 C CG  . LYS   A 1 270 ? 16.35236 18.34154  -8.07703  1.000 60.72297 ? 269 LYS   A CG  1 
ATOM   2080 C CD  . LYS   A 1 270 ? 16.81535 19.41144  -9.05898  1.000 61.94265 ? 269 LYS   A CD  1 
ATOM   2081 C CE  . LYS   A 1 270 ? 18.25196 19.19273  -9.50339  1.000 63.23535 ? 269 LYS   A CE  1 
ATOM   2082 N NZ  . LYS   A 1 270 ? 18.84462 20.43868  -10.07086 1.000 62.98777 ? 269 LYS   A NZ  1 
ATOM   2083 N N   . GLU   A 1 271 ? 12.73475 17.76909  -9.11394  1.000 56.07777 ? 270 GLU   A N   1 
ATOM   2084 C CA  . GLU   A 1 271 ? 11.61987 18.71033  -9.12414  1.000 57.23146 ? 270 GLU   A CA  1 
ATOM   2085 C C   . GLU   A 1 271 ? 10.54123 18.29774  -8.12904  1.000 57.81513 ? 270 GLU   A C   1 
ATOM   2086 O O   . GLU   A 1 271 ? 9.96316  19.14686  -7.43954  1.000 59.72134 ? 270 GLU   A O   1 
ATOM   2087 C CB  . GLU   A 1 271 ? 11.04032 18.81684  -10.53332 1.000 60.97460 ? 270 GLU   A CB  1 
ATOM   2088 C CG  . GLU   A 1 271 ? 9.95714  19.86512  -10.68006 1.000 65.77283 ? 270 GLU   A CG  1 
ATOM   2089 C CD  . GLU   A 1 271 ? 10.24789 20.82665  -11.80869 1.000 68.77029 ? 270 GLU   A CD  1 
ATOM   2090 O OE1 . GLU   A 1 271 ? 11.43539 20.96597  -12.17128 1.000 70.61407 ? 270 GLU   A OE1 1 
ATOM   2091 O OE2 . GLU   A 1 271 ? 9.29339  21.43562  -12.33599 1.000 70.63380 ? 270 GLU   A OE2 1 
ATOM   2092 N N   . LEU   A 1 272 ? 10.25756 16.99577  -8.04051  1.000 56.09881 ? 271 LEU   A N   1 
ATOM   2093 C CA  . LEU   A 1 272 ? 9.27194  16.52079  -7.07070  1.000 57.69528 ? 271 LEU   A CA  1 
ATOM   2094 C C   . LEU   A 1 272 ? 9.72547  16.78783  -5.63901  1.000 58.64283 ? 271 LEU   A C   1 
ATOM   2095 O O   . LEU   A 1 272 ? 8.92125  17.18434  -4.78708  1.000 57.78643 ? 271 LEU   A O   1 
ATOM   2096 C CB  . LEU   A 1 272 ? 9.00403  15.03003  -7.27460  1.000 53.85772 ? 271 LEU   A CB  1 
ATOM   2097 C CG  . LEU   A 1 272 ? 8.18629  14.63213  -8.50169  1.000 52.40579 ? 271 LEU   A CG  1 
ATOM   2098 C CD1 . LEU   A 1 272 ? 8.02663  13.12124  -8.56342  1.000 49.50041 ? 271 LEU   A CD1 1 
ATOM   2099 C CD2 . LEU   A 1 272 ? 6.83111  15.31793  -8.47594  1.000 52.99789 ? 271 LEU   A CD2 1 
ATOM   2100 N N   . LEU   A 1 273 ? 11.01161 16.57345  -5.35583  1.000 57.21118 ? 272 LEU   A N   1 
ATOM   2101 C CA  . LEU   A 1 273 ? 11.52177 16.79808  -4.00750  1.000 57.43685 ? 272 LEU   A CA  1 
ATOM   2102 C C   . LEU   A 1 273 ? 11.56137 18.27851  -3.65984  1.000 59.48229 ? 272 LEU   A C   1 
ATOM   2103 O O   . LEU   A 1 273 ? 11.40764 18.64309  -2.48882  1.000 60.44134 ? 272 LEU   A O   1 
ATOM   2104 C CB  . LEU   A 1 273 ? 12.91586 16.18919  -3.86195  1.000 55.43272 ? 272 LEU   A CB  1 
ATOM   2105 C CG  . LEU   A 1 273 ? 13.00110 14.66586  -3.94050  1.000 52.48057 ? 272 LEU   A CG  1 
ATOM   2106 C CD1 . LEU   A 1 273 ? 14.44825 14.20822  -3.92485  1.000 53.10500 ? 272 LEU   A CD1 1 
ATOM   2107 C CD2 . LEU   A 1 273 ? 12.22812 14.03776  -2.79635  1.000 54.88210 ? 272 LEU   A CD2 1 
ATOM   2108 N N   . GLN   A 1 274 ? 11.76487 19.14048  -4.65390  1.000 59.10746 ? 273 GLN   A N   1 
ATOM   2109 C CA  . GLN   A 1 274 ? 11.89874 20.56733  -4.40160  1.000 61.70927 ? 273 GLN   A CA  1 
ATOM   2110 C C   . GLN   A 1 274 ? 10.57196 21.31348  -4.41135  1.000 63.81809 ? 273 GLN   A C   1 
ATOM   2111 O O   . GLN   A 1 274 ? 10.48596 22.39562  -3.81903  1.000 65.51531 ? 273 GLN   A O   1 
ATOM   2112 C CB  . GLN   A 1 274 ? 12.84063 21.19815  -5.43185  1.000 62.94247 ? 273 GLN   A CB  1 
ATOM   2113 C CG  . GLN   A 1 274 ? 14.29233 20.76588  -5.29184  1.000 63.61034 ? 273 GLN   A CG  1 
ATOM   2114 C CD  . GLN   A 1 274 ? 15.20405 21.44637  -6.29553  1.000 64.15954 ? 273 GLN   A CD  1 
ATOM   2115 O OE1 . GLN   A 1 274 ? 14.74387 22.01811  -7.28328  1.000 65.71494 ? 273 GLN   A OE1 1 
ATOM   2116 N NE2 . GLN   A 1 274 ? 16.50516 21.39149  -6.04347  1.000 65.65290 ? 273 GLN   A NE2 1 
ATOM   2117 N N   . ASN   A 1 275 ? 9.53999  20.77176  -5.06175  1.000 62.70697 ? 274 ASN   A N   1 
ATOM   2118 C CA  . ASN   A 1 275 ? 8.25135  21.44306  -5.14657  1.000 65.50655 ? 274 ASN   A CA  1 
ATOM   2119 C C   . ASN   A 1 275 ? 7.08575  20.62420  -4.61117  1.000 65.70534 ? 274 ASN   A C   1 
ATOM   2120 O O   . ASN   A 1 275 ? 5.98195  21.16759  -4.48760  1.000 69.11565 ? 274 ASN   A O   1 
ATOM   2121 C CB  . ASN   A 1 275 ? 7.95033  21.84243  -6.60050  1.000 71.27852 ? 274 ASN   A CB  1 
ATOM   2122 C CG  . ASN   A 1 275 ? 8.96989  22.81538  -7.15943  1.000 75.69891 ? 274 ASN   A CG  1 
ATOM   2123 O OD1 . ASN   A 1 275 ? 9.54747  23.61701  -6.42499  1.000 78.56569 ? 274 ASN   A OD1 1 
ATOM   2124 N ND2 . ASN   A 1 275 ? 9.19746  22.74884  -8.46650  1.000 72.84190 ? 274 ASN   A ND2 1 
ATOM   2125 N N   . GLY   A 1 276 ? 7.28821  19.35046  -4.29102  1.000 65.38726 ? 275 GLY   A N   1 
ATOM   2126 C CA  . GLY   A 1 276 ? 6.21253  18.52759  -3.78468  1.000 65.22663 ? 275 GLY   A CA  1 
ATOM   2127 C C   . GLY   A 1 276 ? 5.31069  17.99944  -4.88521  1.000 67.57592 ? 275 GLY   A C   1 
ATOM   2128 O O   . GLY   A 1 276 ? 5.58823  18.10879  -6.08322  1.000 66.63753 ? 275 GLY   A O   1 
ATOM   2129 N N   . MET   A 1 277 ? 4.19887  17.40767  -4.45006  1.000 67.03240 ? 276 MET   A N   1 
ATOM   2130 C CA  . MET   A 1 277 ? 3.21116  16.85014  -5.36435  1.000 69.98940 ? 276 MET   A CA  1 
ATOM   2131 C C   . MET   A 1 277 ? 2.16686  17.86689  -5.80188  1.000 73.87466 ? 276 MET   A C   1 
ATOM   2132 O O   . MET   A 1 277 ? 1.47001  17.62801  -6.79568  1.000 72.53943 ? 276 MET   A O   1 
ATOM   2133 C CB  . MET   A 1 277 ? 2.50587  15.65507  -4.71292  1.000 69.37736 ? 276 MET   A CB  1 
ATOM   2134 C CG  . MET   A 1 277 ? 3.44832  14.59984  -4.15039  1.000 68.28877 ? 276 MET   A CG  1 
ATOM   2135 S SD  . MET   A 1 277 ? 3.92124  13.34228  -5.35143  1.000 67.56736 ? 276 MET   A SD  1 
ATOM   2136 C CE  . MET   A 1 277 ? 2.37018  12.47026  -5.55458  1.000 57.64326 ? 276 MET   A CE  1 
ATOM   2137 N N   . ASN   A 1 278 ? 2.04262  18.98413  -5.08119  1.000 81.21897 ? 277 ASN   A N   1 
ATOM   2138 C CA  . ASN   A 1 278 ? 1.07386  20.03797  -5.38908  1.000 81.85163 ? 277 ASN   A CA  1 
ATOM   2139 C C   . ASN   A 1 278 ? -0.35554 19.50230  -5.42521  1.000 80.01110 ? 277 ASN   A C   1 
ATOM   2140 O O   . ASN   A 1 278 ? -1.18796 19.96781  -6.20856  1.000 80.59830 ? 277 ASN   A O   1 
ATOM   2141 C CB  . ASN   A 1 278 ? 1.41932  20.74441  -6.70377  1.000 81.97166 ? 277 ASN   A CB  1 
ATOM   2142 C CG  . ASN   A 1 278 ? 1.47743  22.25200  -6.55628  1.000 85.30084 ? 277 ASN   A CG  1 
ATOM   2143 O OD1 . ASN   A 1 278 ? 1.75532  22.77010  -5.47442  1.000 87.49174 ? 277 ASN   A OD1 1 
ATOM   2144 N ND2 . ASN   A 1 278 ? 1.21175  22.96527  -7.64485  1.000 87.37930 ? 277 ASN   A ND2 1 
ATOM   2145 N N   . GLY   A 1 279 ? -0.65138 18.51946  -4.57663  1.000 75.14158 ? 278 GLY   A N   1 
ATOM   2146 C CA  . GLY   A 1 279 ? -1.98003 17.95349  -4.49138  1.000 71.78724 ? 278 GLY   A CA  1 
ATOM   2147 C C   . GLY   A 1 279 ? -2.28724 16.85473  -5.48502  1.000 70.16901 ? 278 GLY   A C   1 
ATOM   2148 O O   . GLY   A 1 279 ? -3.42966 16.38095  -5.52070  1.000 67.32294 ? 278 GLY   A O   1 
ATOM   2149 N N   . ARG   A 1 280 ? -1.31696 16.43610  -6.29246  1.000 69.77455 ? 279 ARG   A N   1 
ATOM   2150 C CA  . ARG   A 1 280 ? -1.52292 15.35357  -7.23983  1.000 68.04070 ? 279 ARG   A CA  1 
ATOM   2151 C C   . ARG   A 1 280 ? -1.14653 14.01428  -6.60859  1.000 67.62119 ? 279 ARG   A C   1 
ATOM   2152 O O   . ARG   A 1 280 ? -0.69323 13.93696  -5.46392  1.000 67.48893 ? 279 ARG   A O   1 
ATOM   2153 C CB  . ARG   A 1 280 ? -0.71588 15.58993  -8.51613  1.000 69.39106 ? 279 ARG   A CB  1 
ATOM   2154 C CG  . ARG   A 1 280 ? -1.42574 16.41750  -9.57446  1.000 73.78582 ? 279 ARG   A CG  1 
ATOM   2155 C CD  . ARG   A 1 280 ? -0.91317 17.84609  -9.59831  1.000 77.53027 ? 279 ARG   A CD  1 
ATOM   2156 N NE  . ARG   A 1 280 ? 0.53034  17.90697  -9.79769  1.000 79.97209 ? 279 ARG   A NE  1 
ATOM   2157 C CZ  . ARG   A 1 280 ? 1.22600  19.03274  -9.88599  1.000 85.45071 ? 279 ARG   A CZ  1 
ATOM   2158 N NH1 . ARG   A 1 280 ? 0.63773  20.21567  -9.81392  1.000 88.88728 ? 279 ARG   A NH1 1 
ATOM   2159 N NH2 . ARG   A 1 280 ? 2.54488  18.97083  -10.04977 1.000 80.57356 ? 279 ARG   A NH2 1 
ATOM   2160 N N   . THR   A 1 281 ? -1.34212 12.94080  -7.37106  1.000 60.68304 ? 280 THR   A N   1 
ATOM   2161 C CA  . THR   A 1 281 ? -0.94593 11.60123  -6.96806  1.000 55.53071 ? 280 THR   A CA  1 
ATOM   2162 C C   . THR   A 1 281 ? -0.16367 10.94501  -8.09711  1.000 54.68802 ? 280 THR   A C   1 
ATOM   2163 O O   . THR   A 1 281 ? -0.29852 11.30547  -9.26903  1.000 56.36797 ? 280 THR   A O   1 
ATOM   2164 C CB  . THR   A 1 281 ? -2.15582 10.72477  -6.60704  1.000 54.51750 ? 280 THR   A CB  1 
ATOM   2165 O OG1 . THR   A 1 281 ? -2.96383 10.51809  -7.77256  1.000 53.89637 ? 280 THR   A OG1 1 
ATOM   2166 C CG2 . THR   A 1 281 ? -2.99529 11.38312  -5.52186  1.000 54.00403 ? 280 THR   A CG2 1 
ATOM   2167 N N   . ILE   A 1 282 ? 0.66649  9.97507   -7.72644  1.000 52.85088 ? 281 ILE   A N   1 
ATOM   2168 C CA  . ILE   A 1 282 ? 1.38807  9.14121   -8.67953  1.000 52.35453 ? 281 ILE   A CA  1 
ATOM   2169 C C   . ILE   A 1 282 ? 1.08989  7.69244   -8.33265  1.000 51.28876 ? 281 ILE   A C   1 
ATOM   2170 O O   . ILE   A 1 282 ? 1.40235  7.24303   -7.22373  1.000 49.60056 ? 281 ILE   A O   1 
ATOM   2171 C CB  . ILE   A 1 282 ? 2.90245  9.39916   -8.65571  1.000 50.91877 ? 281 ILE   A CB  1 
ATOM   2172 C CG1 . ILE   A 1 282 ? 3.21438  10.82839  -9.08832  1.000 53.08619 ? 281 ILE   A CG1 1 
ATOM   2173 C CG2 . ILE   A 1 282 ? 3.61678  8.41095   -9.55169  1.000 50.13177 ? 281 ILE   A CG2 1 
ATOM   2174 C CD1 . ILE   A 1 282 ? 4.69282  11.15525  -9.08130  1.000 52.23106 ? 281 ILE   A CD1 1 
ATOM   2175 N N   . LEU   A 1 283 ? 0.48886  6.96651   -9.27344  1.000 51.82694 ? 282 LEU   A N   1 
ATOM   2176 C CA  . LEU   A 1 283 ? 0.05434  5.58982   -9.04924  1.000 49.71772 ? 282 LEU   A CA  1 
ATOM   2177 C C   . LEU   A 1 283 ? -0.77074 5.48066   -7.76797  1.000 48.70584 ? 282 LEU   A C   1 
ATOM   2178 O O   . LEU   A 1 283 ? -0.56565 4.59580   -6.93507  1.000 48.25237 ? 282 LEU   A O   1 
ATOM   2179 C CB  . LEU   A 1 283 ? 1.24620  4.63376   -9.02109  1.000 48.97670 ? 282 LEU   A CB  1 
ATOM   2180 C CG  . LEU   A 1 283 ? 1.87511  4.29577   -10.37624 1.000 49.41624 ? 282 LEU   A CG  1 
ATOM   2181 C CD1 . LEU   A 1 283 ? 3.04826  3.34132   -10.20773 1.000 45.44237 ? 282 LEU   A CD1 1 
ATOM   2182 C CD2 . LEU   A 1 283 ? 0.83261  3.70968   -11.31727 1.000 49.17998 ? 282 LEU   A CD2 1 
ATOM   2183 N N   . GLY   A 1 284 ? -1.70774 6.41519   -7.60816  1.000 48.44673 ? 283 GLY   A N   1 
ATOM   2184 C CA  . GLY   A 1 284 ? -2.60977 6.41733   -6.47436  1.000 49.08348 ? 283 GLY   A CA  1 
ATOM   2185 C C   . GLY   A 1 284 ? -1.99786 6.79762   -5.14511  1.000 49.23079 ? 283 GLY   A C   1 
ATOM   2186 O O   . GLY   A 1 284 ? -2.69241 6.72840   -4.12526  1.000 47.33003 ? 283 GLY   A O   1 
ATOM   2187 N N   . SER   A 1 285 ? -0.72968 7.19460   -5.11275  1.000 48.45379 ? 284 SER   A N   1 
ATOM   2188 C CA  . SER   A 1 285 ? -0.05573 7.57062   -3.87925  1.000 48.32615 ? 284 SER   A CA  1 
ATOM   2189 C C   . SER   A 1 285 ? 0.27588  9.05517   -3.90043  1.000 48.85241 ? 284 SER   A C   1 
ATOM   2190 O O   . SER   A 1 285 ? 0.65396  9.60055   -4.94129  1.000 50.08030 ? 284 SER   A O   1 
ATOM   2191 C CB  . SER   A 1 285 ? 1.22487  6.75320   -3.68063  1.000 48.56776 ? 284 SER   A CB  1 
ATOM   2192 O OG  . SER   A 1 285 ? 1.95701  7.21604   -2.55810  1.000 47.73909 ? 284 SER   A OG  1 
ATOM   2193 N N   . ALA   A 1 286 ? 0.12725  9.70664   -2.74965  1.000 48.32750 ? 285 ALA   A N   1 
ATOM   2194 C CA  . ALA   A 1 286 ? 0.55613  11.08944  -2.59226  1.000 50.13346 ? 285 ALA   A CA  1 
ATOM   2195 C C   . ALA   A 1 286 ? 1.96562  11.20442  -2.02718  1.000 48.83161 ? 285 ALA   A C   1 
ATOM   2196 O O   . ALA   A 1 286 ? 2.42601  12.32002  -1.76174  1.000 51.10846 ? 285 ALA   A O   1 
ATOM   2197 C CB  . ALA   A 1 286 ? -0.42372 11.85474  -1.70208  1.000 47.85902 ? 285 ALA   A CB  1 
ATOM   2198 N N   . LEU   A 1 287 ? 2.65713  10.08512  -1.84284  1.000 46.93889 ? 286 LEU   A N   1 
ATOM   2199 C CA  . LEU   A 1 287 ? 4.03858  10.07237  -1.39660  1.000 47.31694 ? 286 LEU   A CA  1 
ATOM   2200 C C   . LEU   A 1 287 ? 4.90179  9.36630   -2.43115  1.000 47.00012 ? 286 LEU   A C   1 
ATOM   2201 O O   . LEU   A 1 287 ? 4.41377  8.58048   -3.24840  1.000 47.12167 ? 286 LEU   A O   1 
ATOM   2202 C CB  . LEU   A 1 287 ? 4.18473  9.37515   -0.03807  1.000 46.54377 ? 286 LEU   A CB  1 
ATOM   2203 C CG  . LEU   A 1 287 ? 3.54128  10.08993  1.14674   1.000 46.73039 ? 286 LEU   A CG  1 
ATOM   2204 C CD1 . LEU   A 1 287 ? 3.95174  9.44060   2.45914   1.000 47.09309 ? 286 LEU   A CD1 1 
ATOM   2205 C CD2 . LEU   A 1 287 ? 3.91471  11.56376  1.12789   1.000 46.60704 ? 286 LEU   A CD2 1 
ATOM   2206 N N   . LEU   A 1 288 ? 6.19695  9.66136   -2.39040  1.000 45.82590 ? 287 LEU   A N   1 
ATOM   2207 C CA  . LEU   A 1 288 ? 7.16143  8.94559   -3.21198  1.000 44.76639 ? 287 LEU   A CA  1 
ATOM   2208 C C   . LEU   A 1 288 ? 7.42160  7.58167   -2.58270  1.000 44.24329 ? 287 LEU   A C   1 
ATOM   2209 O O   . LEU   A 1 288 ? 7.91481  7.49820   -1.45325  1.000 44.58683 ? 287 LEU   A O   1 
ATOM   2210 C CB  . LEU   A 1 288 ? 8.45522  9.74648   -3.34637  1.000 45.70504 ? 287 LEU   A CB  1 
ATOM   2211 C CG  . LEU   A 1 288 ? 8.42128  11.05209  -4.15526  1.000 49.24414 ? 287 LEU   A CG  1 
ATOM   2212 C CD1 . LEU   A 1 288 ? 7.62029  10.88480  -5.44207  1.000 48.45519 ? 287 LEU   A CD1 1 
ATOM   2213 C CD2 . LEU   A 1 288 ? 7.89767  12.22722  -3.33557  1.000 52.14750 ? 287 LEU   A CD2 1 
ATOM   2214 N N   . GLU   A 1 289 ? 7.07242  6.51796   -3.30186  1.000 43.96730 ? 288 GLU   A N   1 
ATOM   2215 C CA  . GLU   A 1 289 ? 7.21267  5.15642   -2.80315  1.000 43.05856 ? 288 GLU   A CA  1 
ATOM   2216 C C   . GLU   A 1 289 ? 8.61811  4.63337   -3.06797  1.000 42.51726 ? 288 GLU   A C   1 
ATOM   2217 O O   . GLU   A 1 289 ? 9.15347  4.79228   -4.16913  1.000 41.64014 ? 288 GLU   A O   1 
ATOM   2218 C CB  . GLU   A 1 289 ? 6.18772  4.23518   -3.46670  1.000 43.13203 ? 288 GLU   A CB  1 
ATOM   2219 C CG  . GLU   A 1 289 ? 4.73937  4.55581   -3.13650  1.000 45.33195 ? 288 GLU   A CG  1 
ATOM   2220 C CD  . GLU   A 1 289 ? 4.42211  4.38023   -1.66659  1.000 49.24732 ? 288 GLU   A CD  1 
ATOM   2221 O OE1 . GLU   A 1 289 ? 3.80690  5.29309   -1.07763  1.000 51.66355 ? 288 GLU   A OE1 1 
ATOM   2222 O OE2 . GLU   A 1 289 ? 4.79427  3.32847   -1.10035  1.000 50.54576 ? 288 GLU   A OE2 1 
ATOM   2223 N N   . ASP   A 1 290 ? 9.20997  3.98903   -2.05617  1.000 41.16233 ? 289 ASP   A N   1 
ATOM   2224 C CA  . ASP   A 1 290 ? 10.57652 3.49130   -2.17891  1.000 41.06700 ? 289 ASP   A CA  1 
ATOM   2225 C C   . ASP   A 1 290 ? 10.70510 2.02128   -1.79288  1.000 40.90820 ? 289 ASP   A C   1 
ATOM   2226 O O   . ASP   A 1 290 ? 11.81459 1.55929   -1.50796  1.000 41.42928 ? 289 ASP   A O   1 
ATOM   2227 C CB  . ASP   A 1 290 ? 11.54342 4.33567   -1.34268  1.000 42.09700 ? 289 ASP   A CB  1 
ATOM   2228 C CG  . ASP   A 1 290 ? 11.43745 4.05571   0.14522   1.000 43.46965 ? 289 ASP   A CG  1 
ATOM   2229 O OD1 . ASP   A 1 290 ? 10.33305 3.71949   0.62258   1.000 42.95633 ? 289 ASP   A OD1 1 
ATOM   2230 O OD2 . ASP   A 1 290 ? 12.46926 4.17638   0.83870   1.000 44.46127 ? 289 ASP   A OD2 1 
ATOM   2231 N N   . GLU   A 1 291 ? 9.60665  1.26927   -1.77900  1.000 39.90432 ? 290 GLU   A N   1 
ATOM   2232 C CA  . GLU   A 1 291 ? 9.65748  -0.14741  -1.43935  1.000 41.77450 ? 290 GLU   A CA  1 
ATOM   2233 C C   . GLU   A 1 291 ? 9.38400  -1.03808  -2.65085  1.000 41.93663 ? 290 GLU   A C   1 
ATOM   2234 O O   . GLU   A 1 291 ? 8.89679  -2.16146  -2.50646  1.000 42.21273 ? 290 GLU   A O   1 
ATOM   2235 C CB  . GLU   A 1 291 ? 8.69328  -0.46031  -0.29432  1.000 42.13697 ? 290 GLU   A CB  1 
ATOM   2236 C CG  . GLU   A 1 291 ? 8.91043  0.42480   0.93216   1.000 43.33914 ? 290 GLU   A CG  1 
ATOM   2237 C CD  . GLU   A 1 291 ? 8.91322  -0.34589  2.24407   1.000 44.96927 ? 290 GLU   A CD  1 
ATOM   2238 O OE1 . GLU   A 1 291 ? 8.37367  -1.47242  2.28867   1.000 44.63310 ? 290 GLU   A OE1 1 
ATOM   2239 O OE2 . GLU   A 1 291 ? 9.46213  0.18051   3.23561   1.000 44.21710 ? 290 GLU   A OE2 1 
ATOM   2240 N N   . PHE   A 1 292 ? 9.70073  -0.54676  -3.84963  1.000 40.89119 ? 291 PHE   A N   1 
ATOM   2241 C CA  . PHE   A 1 292 ? 9.71077  -1.34614  -5.07012  1.000 41.81746 ? 291 PHE   A CA  1 
ATOM   2242 C C   . PHE   A 1 292 ? 11.11218 -1.30717  -5.66294  1.000 40.33160 ? 291 PHE   A C   1 
ATOM   2243 O O   . PHE   A 1 292 ? 11.60095 -0.23365  -6.02660  1.000 41.21355 ? 291 PHE   A O   1 
ATOM   2244 C CB  . PHE   A 1 292 ? 8.70554  -0.82318  -6.09918  1.000 42.34738 ? 291 PHE   A CB  1 
ATOM   2245 C CG  . PHE   A 1 292 ? 7.27001  -0.98641  -5.69912  1.000 40.91162 ? 291 PHE   A CG  1 
ATOM   2246 C CD1 . PHE   A 1 292 ? 6.61030  -2.18725  -5.90500  1.000 41.89338 ? 291 PHE   A CD1 1 
ATOM   2247 C CD2 . PHE   A 1 292 ? 6.56941  0.07211   -5.14714  1.000 40.94690 ? 291 PHE   A CD2 1 
ATOM   2248 C CE1 . PHE   A 1 292 ? 5.28048  -2.33424  -5.54937  1.000 43.86492 ? 291 PHE   A CE1 1 
ATOM   2249 C CE2 . PHE   A 1 292 ? 5.24162  -0.06722  -4.79036  1.000 42.94674 ? 291 PHE   A CE2 1 
ATOM   2250 C CZ  . PHE   A 1 292 ? 4.59591  -1.27167  -4.99177  1.000 42.23494 ? 291 PHE   A CZ  1 
ATOM   2251 N N   . THR   A 1 293 ? 11.75167 -2.46601  -5.76787  1.000 39.73146 ? 292 THR   A N   1 
ATOM   2252 C CA  . THR   A 1 293 ? 13.01707 -2.54599  -6.47974  1.000 41.67200 ? 292 THR   A CA  1 
ATOM   2253 C C   . THR   A 1 293 ? 12.77197 -2.54498  -7.98687  1.000 46.30157 ? 292 THR   A C   1 
ATOM   2254 O O   . THR   A 1 293 ? 11.65016 -2.78565  -8.44169  1.000 42.31701 ? 292 THR   A O   1 
ATOM   2255 C CB  . THR   A 1 293 ? 13.77578 -3.80769  -6.07640  1.000 44.53870 ? 292 THR   A CB  1 
ATOM   2256 O OG1 . THR   A 1 293 ? 13.08439 -4.96201  -6.56846  1.000 43.51074 ? 292 THR   A OG1 1 
ATOM   2257 C CG2 . THR   A 1 293 ? 13.89319 -3.90081  -4.56553  1.000 43.66332 ? 292 THR   A CG2 1 
ATOM   2258 N N   . PRO   A 1 294 ? 13.80280 -2.25173  -8.78914  1.000 43.86472 ? 293 PRO   A N   1 
ATOM   2259 C CA  . PRO   A 1 294 ? 13.64097 -2.40323  -10.24587 1.000 47.09449 ? 293 PRO   A CA  1 
ATOM   2260 C C   . PRO   A 1 294 ? 13.20439 -3.80022  -10.65190 1.000 48.75082 ? 293 PRO   A C   1 
ATOM   2261 O O   . PRO   A 1 294 ? 12.41963 -3.95478  -11.59964 1.000 47.29861 ? 293 PRO   A O   1 
ATOM   2262 C CB  . PRO   A 1 294 ? 15.03450 -2.05469  -10.78471 1.000 46.03329 ? 293 PRO   A CB  1 
ATOM   2263 C CG  . PRO   A 1 294 ? 15.59152 -1.11537  -9.77022  1.000 44.93214 ? 293 PRO   A CG  1 
ATOM   2264 C CD  . PRO   A 1 294 ? 15.07900 -1.60069  -8.44124  1.000 44.17642 ? 293 PRO   A CD  1 
ATOM   2265 N N   . PHE   A 1 295 ? 13.68671 -4.82756  -9.94621  1.000 48.13837 ? 294 PHE   A N   1 
ATOM   2266 C CA  . PHE   A 1 295 ? 13.24465 -6.18844  -10.23042 1.000 50.62447 ? 294 PHE   A CA  1 
ATOM   2267 C C   . PHE   A 1 295 ? 11.76281 -6.36372  -9.92437  1.000 50.92072 ? 294 PHE   A C   1 
ATOM   2268 O O   . PHE   A 1 295 ? 11.04882 -7.03737  -10.67322 1.000 51.17983 ? 294 PHE   A O   1 
ATOM   2269 C CB  . PHE   A 1 295 ? 14.07650 -7.19747  -9.43811  1.000 53.76885 ? 294 PHE   A CB  1 
ATOM   2270 C CG  . PHE   A 1 295 ? 13.61726 -8.62151  -9.60206  1.000 57.74296 ? 294 PHE   A CG  1 
ATOM   2271 C CD1 . PHE   A 1 295 ? 14.03921 -9.37839  -10.68182 1.000 62.36202 ? 294 PHE   A CD1 1 
ATOM   2272 C CD2 . PHE   A 1 295 ? 12.76293 -9.20253  -8.67593  1.000 61.20599 ? 294 PHE   A CD2 1 
ATOM   2273 C CE1 . PHE   A 1 295 ? 13.61844 -10.68687 -10.83704 1.000 65.83448 ? 294 PHE   A CE1 1 
ATOM   2274 C CE2 . PHE   A 1 295 ? 12.33742 -10.51016 -8.82681  1.000 62.16950 ? 294 PHE   A CE2 1 
ATOM   2275 C CZ  . PHE   A 1 295 ? 12.76685 -11.25273 -9.90836  1.000 66.21878 ? 294 PHE   A CZ  1 
ATOM   2276 N N   . ASP   A 1 296 ? 11.28479 -5.78081  -8.81973  1.000 47.54373 ? 295 ASP   A N   1 
ATOM   2277 C CA  . ASP   A 1 296 ? 9.85610  -5.83382  -8.51801  1.000 47.55968 ? 295 ASP   A CA  1 
ATOM   2278 C C   . ASP   A 1 296 ? 9.03864  -5.21307  -9.64285  1.000 49.50469 ? 295 ASP   A C   1 
ATOM   2279 O O   . ASP   A 1 296 ? 8.00472  -5.75965  -10.04908 1.000 50.44508 ? 295 ASP   A O   1 
ATOM   2280 C CB  . ASP   A 1 296 ? 9.56193  -5.11861  -7.19845  1.000 44.19937 ? 295 ASP   A CB  1 
ATOM   2281 C CG  . ASP   A 1 296 ? 10.26071 -5.75878  -6.01110  1.000 45.61526 ? 295 ASP   A CG  1 
ATOM   2282 O OD1 . ASP   A 1 296 ? 10.41342 -6.99825  -5.99481  1.000 47.14055 ? 295 ASP   A OD1 1 
ATOM   2283 O OD2 . ASP   A 1 296 ? 10.65949 -5.01533  -5.08967  1.000 44.28925 ? 295 ASP   A OD2 1 
ATOM   2284 N N   . VAL   A 1 297 ? 9.50068  -4.07713  -10.16912 1.000 48.23865 ? 296 VAL   A N   1 
ATOM   2285 C CA  . VAL   A 1 297 ? 8.77575  -3.38882  -11.23368 1.000 50.48419 ? 296 VAL   A CA  1 
ATOM   2286 C C   . VAL   A 1 297 ? 8.74269  -4.24074  -12.49664 1.000 51.50349 ? 296 VAL   A C   1 
ATOM   2287 O O   . VAL   A 1 297 ? 7.68653  -4.42087  -13.11657 1.000 51.33983 ? 296 VAL   A O   1 
ATOM   2288 C CB  . VAL   A 1 297 ? 9.40465  -2.01048  -11.50088 1.000 49.29649 ? 296 VAL   A CB  1 
ATOM   2289 C CG1 . VAL   A 1 297 ? 8.68519  -1.31351  -12.64378 1.000 47.62856 ? 296 VAL   A CG1 1 
ATOM   2290 C CG2 . VAL   A 1 297 ? 9.37446  -1.16200  -10.23833 1.000 46.95787 ? 296 VAL   A CG2 1 
ATOM   2291 N N   . VAL   A 1 298 ? 9.90297  -4.76410  -12.90599 1.000 51.11760 ? 297 VAL   A N   1 
ATOM   2292 C CA  . VAL   A 1 298 ? 9.95426  -5.59463  -14.10843 1.000 51.51482 ? 297 VAL   A CA  1 
ATOM   2293 C C   . VAL   A 1 298 ? 9.08362  -6.83384  -13.94066 1.000 53.05794 ? 297 VAL   A C   1 
ATOM   2294 O O   . VAL   A 1 298 ? 8.33689  -7.21377  -14.85126 1.000 53.14834 ? 297 VAL   A O   1 
ATOM   2295 C CB  . VAL   A 1 298 ? 11.41159 -5.96380  -14.44378 1.000 52.56835 ? 297 VAL   A CB  1 
ATOM   2296 C CG1 . VAL   A 1 298 ? 11.45931 -7.17907  -15.35685 1.000 50.51737 ? 297 VAL   A CG1 1 
ATOM   2297 C CG2 . VAL   A 1 298 ? 12.11741 -4.78441  -15.09644 1.000 51.14984 ? 297 VAL   A CG2 1 
ATOM   2298 N N   . ARG   A 1 299 ? 9.14971  -7.47014  -12.76756 1.000 54.25717 ? 298 ARG   A N   1 
ATOM   2299 C CA  . ARG   A 1 299 ? 8.36839  -8.67522  -12.51688 1.000 51.98457 ? 298 ARG   A CA  1 
ATOM   2300 C C   . ARG   A 1 299 ? 6.87392  -8.39296  -12.58161 1.000 52.65712 ? 298 ARG   A C   1 
ATOM   2301 O O   . ARG   A 1 299 ? 6.11719  -9.16757  -13.17837 1.000 55.10751 ? 298 ARG   A O   1 
ATOM   2302 C CB  . ARG   A 1 299 ? 8.75332  -9.26491  -11.15748 1.000 52.49996 ? 298 ARG   A CB  1 
ATOM   2303 C CG  . ARG   A 1 299 ? 7.60657  -9.90684  -10.39148 1.000 59.18389 ? 298 ARG   A CG  1 
ATOM   2304 C CD  . ARG   A 1 299 ? 7.86023  -9.85384  -8.89097  1.000 59.79376 ? 298 ARG   A CD  1 
ATOM   2305 N NE  . ARG   A 1 299 ? 6.67233  -10.19024 -8.11410  1.000 56.25228 ? 298 ARG   A NE  1 
ATOM   2306 C CZ  . ARG   A 1 299 ? 6.54131  -9.97008  -6.81238  1.000 54.63261 ? 298 ARG   A CZ  1 
ATOM   2307 N NH1 . ARG   A 1 299 ? 7.50635  -9.40391  -6.10606  1.000 55.73236 ? 298 ARG   A NH1 1 
ATOM   2308 N NH2 . ARG   A 1 299 ? 5.41139  -10.32164 -6.20451  1.000 46.50423 ? 298 ARG   A NH2 1 
ATOM   2309 N N   . GLN   A 1 300 ? 6.42557  -7.28319  -11.98801 1.000 52.79329 ? 299 GLN   A N   1 
ATOM   2310 C CA  . GLN   A 1 300 ? 4.99212  -7.01691  -11.97109 1.000 52.64465 ? 299 GLN   A CA  1 
ATOM   2311 C C   . GLN   A 1 300 ? 4.48092  -6.53118  -13.31976 1.000 53.08965 ? 299 GLN   A C   1 
ATOM   2312 O O   . GLN   A 1 300 ? 3.34282  -6.84154  -13.68908 1.000 52.69813 ? 299 GLN   A O   1 
ATOM   2313 C CB  . GLN   A 1 300 ? 4.63696  -6.00076  -10.88368 1.000 50.11740 ? 299 GLN   A CB  1 
ATOM   2314 C CG  . GLN   A 1 300 ? 3.13153  -5.82676  -10.71969 1.000 47.23977 ? 299 GLN   A CG  1 
ATOM   2315 C CD  . GLN   A 1 300 ? 2.75280  -4.92355  -9.56812  1.000 47.51650 ? 299 GLN   A CD  1 
ATOM   2316 O OE1 . GLN   A 1 300 ? 1.68186  -4.31915  -9.57249  1.000 45.83923 ? 299 GLN   A OE1 1 
ATOM   2317 N NE2 . GLN   A 1 300 ? 3.62229  -4.83533  -8.56827  1.000 44.46858 ? 299 GLN   A NE2 1 
ATOM   2318 N N   . CYS   A 1 301 ? 5.29042  -5.78713  -14.07146 1.000 53.90444 ? 300 CYS   A N   1 
ATOM   2319 C CA  . CYS   A 1 301 ? 4.86966  -5.31418  -15.38325 1.000 54.11704 ? 300 CYS   A CA  1 
ATOM   2320 C C   . CYS   A 1 301 ? 5.11454  -6.32897  -16.49287 1.000 54.58433 ? 300 CYS   A C   1 
ATOM   2321 O O   . CYS   A 1 301 ? 4.67655  -6.10157  -17.62493 1.000 57.26301 ? 300 CYS   A O   1 
ATOM   2322 C CB  . CYS   A 1 301 ? 5.58055  -3.99885  -15.71953 1.000 54.24758 ? 300 CYS   A CB  1 
ATOM   2323 S SG  . CYS   A 1 301 ? 5.21881  -2.64910  -14.56191 1.000 55.49634 ? 300 CYS   A SG  1 
ATOM   2324 N N   . SER   A 1 302 ? 5.79388  -7.43856  -16.19785 1.000 54.79965 ? 301 SER   A N   1 
ATOM   2325 C CA  . SER   A 1 302 ? 6.05280  -8.48079  -17.17890 1.000 55.68159 ? 301 SER   A CA  1 
ATOM   2326 C C   . SER   A 1 302 ? 5.31963  -9.78379  -16.89108 1.000 56.47608 ? 301 SER   A C   1 
ATOM   2327 O O   . SER   A 1 302 ? 5.31370  -10.67177 -17.75144 1.000 56.69613 ? 301 SER   A O   1 
ATOM   2328 C CB  . SER   A 1 302 ? 7.56061  -8.76020  -17.26821 1.000 57.13660 ? 301 SER   A CB  1 
ATOM   2329 O OG  . SER   A 1 302 ? 7.82432  -9.84584  -18.13855 1.000 59.82956 ? 301 SER   A OG  1 
ATOM   2330 N N   . GLY   A 1 303 ? 4.72015  -9.93020  -15.71122 1.000 54.52167 ? 302 GLY   A N   1 
ATOM   2331 C CA  . GLY   A 1 303 ? 3.90249  -11.09294 -15.42153 1.000 53.29429 ? 302 GLY   A CA  1 
ATOM   2332 C C   . GLY   A 1 303 ? 4.65257  -12.33681 -15.00390 1.000 54.41457 ? 302 GLY   A C   1 
ATOM   2333 O O   . GLY   A 1 303 ? 4.21619  -13.44810 -15.32198 1.000 51.80261 ? 302 GLY   A O   1 
ATOM   2334 N N   . VAL   A 1 304 ? 5.76706  -12.18827 -14.29577 1.000 56.62877 ? 303 VAL   A N   1 
ATOM   2335 C CA  . VAL   A 1 304 ? 6.53387  -13.33995 -13.83650 1.000 55.70915 ? 303 VAL   A CA  1 
ATOM   2336 C C   . VAL   A 1 304 ? 5.78785  -14.05859 -12.71612 1.000 54.43178 ? 303 VAL   A C   1 
ATOM   2337 O O   . VAL   A 1 304 ? 5.51132  -15.25525 -12.80868 1.000 53.07180 ? 303 VAL   A O   1 
ATOM   2338 C CB  . VAL   A 1 304 ? 7.94121  -12.92570 -13.37426 1.000 54.91175 ? 303 VAL   A CB  1 
ATOM   2339 C CG1 . VAL   A 1 304 ? 8.72310  -14.14368 -12.90961 1.000 55.51784 ? 303 VAL   A CG1 1 
ATOM   2340 C CG2 . VAL   A 1 304 ? 8.67936  -12.20802 -14.49453 1.000 58.14288 ? 303 VAL   A CG2 1 
HETATM 2341 C C4  . A1BCX B 2 .   ? 11.20686 -0.46171  24.29631  1.000 48.55166 ? 401 A1BCX A C4  1 
HETATM 2342 C C5  . A1BCX B 2 .   ? 10.36283 -0.14116  23.24081  1.000 49.05749 ? 401 A1BCX A C5  1 
HETATM 2343 C C6  . A1BCX B 2 .   ? 9.85210  -1.12362  22.40008  1.000 48.74352 ? 401 A1BCX A C6  1 
HETATM 2344 C C7  . A1BCX B 2 .   ? 10.21455 -2.44115  22.64566  1.000 46.77426 ? 401 A1BCX A C7  1 
HETATM 2345 C C10 . A1BCX B 2 .   ? 11.26510 -4.22081  23.60141  1.000 47.07480 ? 401 A1BCX A C10 1 
HETATM 2346 C C15 . A1BCX B 2 .   ? 10.83550 -8.39787  22.09037  1.000 40.70328 ? 401 A1BCX A C15 1 
HETATM 2347 C C17 . A1BCX B 2 .   ? 11.46699 -9.38146  23.07823  1.000 42.25209 ? 401 A1BCX A C17 1 
HETATM 2348 C C21 . A1BCX B 2 .   ? 9.41137  -8.82699  21.73471  1.000 41.58889 ? 401 A1BCX A C21 1 
HETATM 2349 C C24 . A1BCX B 2 .   ? 7.97884  -9.93329  20.05691  1.000 40.03972 ? 401 A1BCX A C24 1 
HETATM 2350 C C26 . A1BCX B 2 .   ? 7.58889  -9.07508  18.85376  1.000 39.66564 ? 401 A1BCX A C26 1 
HETATM 2351 C C1  . A1BCX B 2 .   ? 12.95447 -1.18887  26.37527  1.000 54.70569 ? 401 A1BCX A C1  1 
HETATM 2352 C C11 . A1BCX B 2 .   ? 11.06398 -2.80552  23.70458  1.000 48.79156 ? 401 A1BCX A C11 1 
HETATM 2353 C C12 . A1BCX B 2 .   ? 10.41902 -6.00107  21.89265  1.000 42.75554 ? 401 A1BCX A C12 1 
HETATM 2354 C C27 . A1BCX B 2 .   ? 6.29214  -8.26375  19.01359  1.000 42.14515 ? 401 A1BCX A C27 1 
HETATM 2355 C C29 . A1BCX B 2 .   ? 6.04364  -7.72519  20.43749  1.000 44.02072 ? 401 A1BCX A C29 1 
HETATM 2356 C C3  . A1BCX B 2 .   ? 11.56115 -1.78180  24.53275  1.000 49.98537 ? 401 A1BCX A C3  1 
HETATM 2357 C C30 . A1BCX B 2 .   ? 5.28739  -6.41368  20.23908  1.000 45.11648 ? 401 A1BCX A C30 1 
HETATM 2358 C C32 . A1BCX B 2 .   ? 6.30946  -6.97846  18.20929  1.000 42.27466 ? 401 A1BCX A C32 1 
HETATM 2359 C C34 . A1BCX B 2 .   ? 8.07056  -11.40632 19.69170  1.000 37.63285 ? 401 A1BCX A C34 1 
HETATM 2360 C C38 . A1BCX B 2 .   ? 12.75991 -10.02258 22.58073  1.000 41.68793 ? 401 A1BCX A C38 1 
HETATM 2361 C C39 . A1BCX B 2 .   ? 14.02080 -9.82978  23.35003  1.000 43.43245 ? 401 A1BCX A C39 1 
HETATM 2362 C C40 . A1BCX B 2 .   ? 13.84505 -9.16230  22.03010  1.000 41.79321 ? 401 A1BCX A C40 1 
HETATM 2363 C C9  . A1BCX B 2 .   ? 10.55538 -4.66228  22.51602  1.000 44.55437 ? 401 A1BCX A C9  1 
HETATM 2364 N N14 . A1BCX B 2 .   ? 10.89055 -7.03747  22.60085  1.000 40.09420 ? 401 A1BCX A N14 1 
HETATM 2365 N N23 . A1BCX B 2 .   ? 9.26804  -9.48473  20.57833  1.000 37.89051 ? 401 A1BCX A N23 1 
HETATM 2366 N N31 . A1BCX B 2 .   ? 5.49974  -6.11929  18.82652  1.000 43.92965 ? 401 A1BCX A N31 1 
HETATM 2367 N N8  . A1BCX B 2 .   ? 9.91061  -3.59386  21.92788  1.000 44.22715 ? 401 A1BCX A N8  1 
HETATM 2368 O O13 . A1BCX B 2 .   ? 9.91733  -6.12935  20.77493  1.000 41.86498 ? 401 A1BCX A O13 1 
HETATM 2369 O O2  . A1BCX B 2 .   ? 12.40118 -2.19273  25.52828  1.000 53.36241 ? 401 A1BCX A O2  1 
HETATM 2370 O O22 . A1BCX B 2 .   ? 8.47353  -8.56824  22.48375  1.000 42.62510 ? 401 A1BCX A O22 1 
HETATM 2371 O O33 . A1BCX B 2 .   ? 6.96554  -6.76218  17.19470  1.000 40.23786 ? 401 A1BCX A O33 1 
HETATM 2372 O O36 . A1BCX B 2 .   ? 6.79797  -11.94003 19.35255  1.000 37.98680 ? 401 A1BCX A O36 1 
HETATM 2373 O O   . HOH   C 3 .   ? 13.36417 15.87464  -17.93806 1.000 64.93198 ? 501 HOH   A O   1 
HETATM 2374 O O   . HOH   C 3 .   ? 10.06609 -33.62056 22.61940  1.000 58.09536 ? 502 HOH   A O   1 
HETATM 2375 O O   . HOH   C 3 .   ? 18.34403 -16.73793 -3.19303  1.000 50.97900 ? 503 HOH   A O   1 
HETATM 2376 O O   . HOH   C 3 .   ? 21.51334 -10.14610 20.35649  1.000 39.74433 ? 504 HOH   A O   1 
HETATM 2377 O O   . HOH   C 3 .   ? 15.61517 18.27626  3.65164   1.000 63.41391 ? 505 HOH   A O   1 
HETATM 2378 O O   . HOH   C 3 .   ? 9.81627  -9.51657  -6.25011  1.000 52.01609 ? 506 HOH   A O   1 
HETATM 2379 O O   . HOH   C 3 .   ? 14.82686 -2.77996  23.07969  1.000 51.71690 ? 507 HOH   A O   1 
HETATM 2380 O O   . HOH   C 3 .   ? 21.02836 13.26459  3.73929   1.000 63.93174 ? 508 HOH   A O   1 
HETATM 2381 O O   . HOH   C 3 .   ? 10.11172 -31.71893 0.33539   1.000 50.70866 ? 509 HOH   A O   1 
HETATM 2382 O O   . HOH   C 3 .   ? 6.77941  2.10299   -0.83950  1.000 45.41874 ? 510 HOH   A O   1 
HETATM 2383 O O   . HOH   C 3 .   ? 23.06259 17.96649  -0.58656  1.000 73.16503 ? 511 HOH   A O   1 
HETATM 2384 O O   . HOH   C 3 .   ? 6.00254  -16.60445 8.60029   1.000 37.41508 ? 512 HOH   A O   1 
HETATM 2385 O O   . HOH   C 3 .   ? 13.22287 2.63063   10.34302  1.000 43.93073 ? 513 HOH   A O   1 
HETATM 2386 O O   . HOH   C 3 .   ? 0.17476  -3.95451  -14.28003 1.000 49.06467 ? 514 HOH   A O   1 
HETATM 2387 O O   . HOH   C 3 .   ? 16.43188 3.71755   6.40588   1.000 46.54049 ? 515 HOH   A O   1 
HETATM 2388 O O   . HOH   C 3 .   ? 24.18565 4.63502   -2.27993  1.000 56.21537 ? 516 HOH   A O   1 
HETATM 2389 O O   . HOH   C 3 .   ? 17.06810 -27.17390 8.10726   1.000 43.00230 ? 517 HOH   A O   1 
HETATM 2390 O O   . HOH   C 3 .   ? 10.47475 -7.15870  25.73484  1.000 45.31794 ? 518 HOH   A O   1 
HETATM 2391 O O   . HOH   C 3 .   ? 5.78177  3.21411   18.91015  1.000 53.38071 ? 519 HOH   A O   1 
HETATM 2392 O O   . HOH   C 3 .   ? 22.45981 17.48079  -6.41485  1.000 73.59713 ? 520 HOH   A O   1 
HETATM 2393 O O   . HOH   C 3 .   ? 17.95255 -13.53575 33.49424  1.000 62.67299 ? 521 HOH   A O   1 
HETATM 2394 O O   . HOH   C 3 .   ? -2.60023 7.93368   -9.39309  1.000 53.95195 ? 522 HOH   A O   1 
HETATM 2395 O O   . HOH   C 3 .   ? 4.23931  -25.72633 21.12876  1.000 47.32636 ? 523 HOH   A O   1 
HETATM 2396 O O   . HOH   C 3 .   ? -2.45567 6.07111   -11.72652 1.000 57.51838 ? 524 HOH   A O   1 
HETATM 2397 O O   . HOH   C 3 .   ? 2.95725  -16.95177 18.88946  1.000 42.56675 ? 525 HOH   A O   1 
HETATM 2398 O O   . HOH   C 3 .   ? 5.68115  -26.15371 1.90127   1.000 43.30954 ? 526 HOH   A O   1 
HETATM 2399 O O   . HOH   C 3 .   ? 14.86236 -13.75382 0.34492   1.000 38.46616 ? 527 HOH   A O   1 
HETATM 2400 O O   . HOH   C 3 .   ? 24.45827 -11.30758 1.69927   1.000 46.07792 ? 528 HOH   A O   1 
HETATM 2401 O O   . HOH   C 3 .   ? 11.34588 14.31723  -17.83103 1.000 61.36468 ? 529 HOH   A O   1 
HETATM 2402 O O   . HOH   C 3 .   ? 20.92891 -21.36105 10.75424  1.000 42.83584 ? 530 HOH   A O   1 
HETATM 2403 O O   . HOH   C 3 .   ? 14.90246 -34.12213 27.32569  1.000 53.72272 ? 531 HOH   A O   1 
HETATM 2404 O O   . HOH   C 3 .   ? 15.99239 -2.18362  -14.84206 1.000 50.25437 ? 532 HOH   A O   1 
HETATM 2405 O O   . HOH   C 3 .   ? 7.09615  -31.22567 21.20907  1.000 56.24248 ? 533 HOH   A O   1 
HETATM 2406 O O   . HOH   C 3 .   ? 16.70000 -5.51649  11.82667  1.000 34.79641 ? 534 HOH   A O   1 
HETATM 2407 O O   . HOH   C 3 .   ? 14.30129 0.47123   22.54996  1.000 54.95072 ? 535 HOH   A O   1 
HETATM 2408 O O   . HOH   C 3 .   ? -5.19824 6.15453   -3.78294  1.000 48.35406 ? 536 HOH   A O   1 
HETATM 2409 O O   . HOH   C 3 .   ? 4.23293  -17.46200 -13.42164 1.000 51.29635 ? 537 HOH   A O   1 
HETATM 2410 O O   . HOH   C 3 .   ? 19.25733 1.96919   12.47099  1.000 48.21596 ? 538 HOH   A O   1 
HETATM 2411 O O   . HOH   C 3 .   ? 15.63842 -13.74714 20.04326  1.000 33.75533 ? 539 HOH   A O   1 
HETATM 2412 O O   . HOH   C 3 .   ? 22.92263 -8.65949  17.65560  1.000 41.36352 ? 540 HOH   A O   1 
HETATM 2413 O O   . HOH   C 3 .   ? 12.75182 23.09033  -2.62765  1.000 58.03280 ? 541 HOH   A O   1 
HETATM 2414 O O   . HOH   C 3 .   ? 10.52404 -8.98339  -3.38381  1.000 42.40156 ? 542 HOH   A O   1 
HETATM 2415 O O   . HOH   C 3 .   ? -2.97965 8.33695   -13.09625 1.000 62.14239 ? 543 HOH   A O   1 
HETATM 2416 O O   . HOH   C 3 .   ? 19.56989 -31.79331 9.70333   1.000 53.95446 ? 544 HOH   A O   1 
HETATM 2417 O O   . HOH   C 3 .   ? 0.23126  -9.11168  12.22283  1.000 43.26275 ? 545 HOH   A O   1 
HETATM 2418 O O   . HOH   C 3 .   ? -0.98598 -3.83954  -1.78653  1.000 44.08482 ? 546 HOH   A O   1 
HETATM 2419 O O   . HOH   C 3 .   ? 24.59626 -8.40501  12.84461  1.000 41.18741 ? 547 HOH   A O   1 
HETATM 2420 O O   . HOH   C 3 .   ? 12.054   -30.815   33.005    1.000 62.56335 ? 548 HOH   A O   1 
HETATM 2421 O O   . HOH   C 3 .   ? 23.50696 -6.46696  15.71259  1.000 39.82620 ? 549 HOH   A O   1 
HETATM 2422 O O   . HOH   C 3 .   ? 18.93916 -16.07314 6.05859   1.000 37.46333 ? 550 HOH   A O   1 
HETATM 2423 O O   . HOH   C 3 .   ? 23.06305 -10.91166 15.61798  1.000 39.93127 ? 551 HOH   A O   1 
HETATM 2424 O O   . HOH   C 3 .   ? 9.87862  -1.81514  5.07067   1.000 37.89806 ? 552 HOH   A O   1 
HETATM 2425 O O   . HOH   C 3 .   ? 6.45200  -6.26273  -7.86306  1.000 47.30182 ? 553 HOH   A O   1 
HETATM 2426 O O   . HOH   C 3 .   ? 6.66780  -36.19405 16.01874  1.000 59.88528 ? 554 HOH   A O   1 
HETATM 2427 O O   . HOH   C 3 .   ? 20.93811 -26.64165 26.81022  1.000 46.06772 ? 555 HOH   A O   1 
HETATM 2428 O O   . HOH   C 3 .   ? 10.11965 11.67162  -0.50318  1.000 48.47383 ? 556 HOH   A O   1 
HETATM 2429 O O   . HOH   C 3 .   ? 9.69799  2.05042   -4.96180  1.000 41.90563 ? 557 HOH   A O   1 
HETATM 2430 O O   . HOH   C 3 .   ? 4.23111  -20.39624 -2.55101  1.000 44.60070 ? 558 HOH   A O   1 
HETATM 2431 O O   . HOH   C 3 .   ? 1.11712  17.97798  -2.53388  1.000 68.44085 ? 559 HOH   A O   1 
HETATM 2432 O O   . HOH   C 3 .   ? 18.12103 20.60622  -18.19183 1.000 58.70379 ? 560 HOH   A O   1 
HETATM 2433 O O   . HOH   C 3 .   ? 9.00817  21.86731  -15.09075 1.000 67.78869 ? 561 HOH   A O   1 
HETATM 2434 O O   . HOH   C 3 .   ? 14.35316 -8.07750  -3.36732  1.000 45.27633 ? 562 HOH   A O   1 
HETATM 2435 O O   . HOH   C 3 .   ? 23.13657 -14.57230 1.44960   1.000 44.81818 ? 563 HOH   A O   1 
HETATM 2436 O O   . HOH   C 3 .   ? 17.03297 -1.76189  -4.45853  1.000 44.36566 ? 564 HOH   A O   1 
HETATM 2437 O O   . HOH   C 3 .   ? 23.62407 -5.61460  9.16745   1.000 40.75283 ? 565 HOH   A O   1 
HETATM 2438 O O   . HOH   C 3 .   ? 3.92998  -29.85592 7.26055   1.000 47.16592 ? 566 HOH   A O   1 
HETATM 2439 O O   . HOH   C 3 .   ? 1.00136  -25.17045 13.07897  1.000 49.99691 ? 567 HOH   A O   1 
HETATM 2440 O O   . HOH   C 3 .   ? 24.01087 -24.27062 21.70035  1.000 40.91655 ? 568 HOH   A O   1 
HETATM 2441 O O   . HOH   C 3 .   ? -5.548   -12.248   9.928     1.000 51.71778 ? 569 HOH   A O   1 
HETATM 2442 O O   . HOH   C 3 .   ? 3.84720  -2.24726  20.36490  1.000 50.09538 ? 570 HOH   A O   1 
HETATM 2443 O O   . HOH   C 3 .   ? 5.45030  -5.62862  -4.90707  1.000 40.71747 ? 571 HOH   A O   1 
HETATM 2444 O O   . HOH   C 3 .   ? 7.54694  -6.49340  24.31783  1.000 46.29063 ? 572 HOH   A O   1 
HETATM 2445 O O   . HOH   C 3 .   ? 18.36785 -32.40481 26.13088  1.000 51.53174 ? 573 HOH   A O   1 
HETATM 2446 O O   . HOH   C 3 .   ? 8.01994  -4.73878  -3.59094  1.000 41.90845 ? 574 HOH   A O   1 
HETATM 2447 O O   . HOH   C 3 .   ? 22.90160 -15.94900 34.32102  1.000 47.60574 ? 575 HOH   A O   1 
HETATM 2448 O O   . HOH   C 3 .   ? 7.11346  -4.21912  22.68102  1.000 46.61720 ? 576 HOH   A O   1 
HETATM 2449 O O   . HOH   C 3 .   ? 16.16429 -4.96829  -8.31966  1.000 49.76231 ? 577 HOH   A O   1 
HETATM 2450 O O   . HOH   C 3 .   ? 12.18858 -38.19015 8.60413   1.000 50.85900 ? 578 HOH   A O   1 
HETATM 2451 O O   . HOH   C 3 .   ? 6.55140  -7.15862  32.19129  1.000 59.96299 ? 579 HOH   A O   1 
HETATM 2452 O O   . HOH   C 3 .   ? 9.98664  -26.52347 -3.93376  1.000 56.58980 ? 580 HOH   A O   1 
HETATM 2453 O O   . HOH   C 3 .   ? 8.89041  -11.13378 -20.65154 1.000 55.42015 ? 581 HOH   A O   1 
HETATM 2454 O O   . HOH   C 3 .   ? 1.75675  -6.29605  0.23342   1.000 40.34317 ? 582 HOH   A O   1 
HETATM 2455 O O   . HOH   C 3 .   ? 19.10698 23.46575  -9.79082  1.000 55.59276 ? 583 HOH   A O   1 
HETATM 2456 O O   . HOH   C 3 .   ? 23.61638 -13.63273 25.96821  1.000 46.39918 ? 584 HOH   A O   1 
HETATM 2457 O O   . HOH   C 3 .   ? 1.59072  -2.42176  -16.20434 1.000 49.77700 ? 585 HOH   A O   1 
HETATM 2458 O O   . HOH   C 3 .   ? 19.82978 -14.57122 32.42005  1.000 53.08180 ? 586 HOH   A O   1 
HETATM 2459 O O   . HOH   C 3 .   ? -2.45970 -9.98433  12.40961  1.000 48.68580 ? 587 HOH   A O   1 
HETATM 2460 O O   . HOH   C 3 .   ? 28.45536 -13.67812 12.47009  1.000 52.15672 ? 588 HOH   A O   1 
HETATM 2461 O O   . HOH   C 3 .   ? -1.225   -4.149    -19.301   1.000 49.08341 ? 589 HOH   A O   1 
HETATM 2462 O O   . HOH   C 3 .   ? 25.29442 -15.78212 26.24883  1.000 50.18801 ? 590 HOH   A O   1 
HETATM 2463 O O   . HOH   C 3 .   ? 14.777   -3.539    -21.707   1.000 46.06552 ? 591 HOH   A O   1 
HETATM 2464 O O   . HOH   C 3 .   ? 9.39579  21.11482  -17.20113 1.000 73.25739 ? 592 HOH   A O   1 
HETATM 2465 O O   . HOH   C 3 .   ? 1.17796  -6.27594  20.74870  1.000 47.11017 ? 593 HOH   A O   1 
HETATM 2466 O O   . HOH   C 3 .   ? 19.68527 1.54199   -2.81268  1.000 53.66676 ? 594 HOH   A O   1 
HETATM 2467 O O   . HOH   C 3 .   ? 25.28845 -6.77148  7.05239   1.000 46.52275 ? 595 HOH   A O   1 
HETATM 2468 O O   . HOH   C 3 .   ? 15.145   -5.454    -12.968   1.000 52.55728 ? 596 HOH   A O   1 
HETATM 2469 O O   . HOH   C 3 .   ? 8.33922  -28.77901 30.18205  1.000 50.98204 ? 597 HOH   A O   1 
HETATM 2470 O O   . HOH   C 3 .   ? 26.07143 -8.16477  5.27914   1.000 51.54849 ? 598 HOH   A O   1 
HETATM 2471 O O   . HOH   C 3 .   ? 13.51037 -1.76389  21.07492  1.000 48.13860 ? 599 HOH   A O   1 
HETATM 2472 O O   . HOH   C 3 .   ? 5.50595  -5.55219  23.71306  1.000 49.71712 ? 600 HOH   A O   1 
HETATM 2473 O O   . HOH   C 3 .   ? 21.67951 -16.08448 5.86378   1.000 42.88836 ? 601 HOH   A O   1 
HETATM 2474 O O   . HOH   C 3 .   ? 19.81505 1.83664   0.09621   1.000 52.02571 ? 602 HOH   A O   1 
HETATM 2475 O O   . HOH   C 3 .   ? 17.91692 -15.54241 -6.89509  1.000 55.94589 ? 603 HOH   A O   1 
HETATM 2476 O O   . HOH   C 3 .   ? 17.99803 -34.19275 27.60171  1.000 52.25461 ? 604 HOH   A O   1 
HETATM 2477 O O   . HOH   C 3 .   ? 21.53571 23.39436  -9.15289  1.000 57.24102 ? 605 HOH   A O   1 
HETATM 2478 O O   . HOH   C 3 .   ? 23.37205 -25.71085 26.23993  1.000 44.94055 ? 606 HOH   A O   1 
HETATM 2479 O O   . HOH   C 3 .   ? 8.61773  -27.72920 33.12136  1.000 56.12925 ? 607 HOH   A O   1 
HETATM 2480 O O   . HOH   C 3 .   ? 0.00000  17.91075  0.00000   0.50  55.94549 ? 608 HOH   A O   1 
HETATM 2481 O O   . HOH   C 3 .   ? 22.03459 23.00432  -6.46987  1.000 45.13660 ? 609 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 2   ? 0.83191 0.77233 0.52211 -0.07391 -0.25963 0.19201  1   SER A N   
2    C CA  . SER A 2   ? 0.80192 0.76150 0.52772 -0.07992 -0.24171 0.21072  1   SER A CA  
3    C C   . SER A 2   ? 0.73997 0.69965 0.53635 -0.07995 -0.23577 0.19178  1   SER A C   
4    O O   . SER A 2   ? 0.71873 0.66944 0.52933 -0.07446 -0.23706 0.16429  1   SER A O   
5    C CB  . SER A 2   ? 0.82868 0.78795 0.56572 -0.09181 -0.26262 0.24715  1   SER A CB  
6    O OG  . SER A 2   ? 0.82329 0.76249 0.60570 -0.09678 -0.29565 0.24492  1   SER A OG  
7    N N   . GLY A 3   ? 0.79035 0.76074 0.63032 -0.08612 -0.22998 0.20707  2   GLY A N   
8    C CA  . GLY A 3   ? 0.68147 0.65434 0.58270 -0.08474 -0.22249 0.18909  2   GLY A CA  
9    C C   . GLY A 3   ? 0.67191 0.66219 0.56693 -0.08023 -0.18950 0.18166  2   GLY A C   
10   O O   . GLY A 3   ? 0.71045 0.70789 0.55610 -0.07416 -0.17058 0.17606  2   GLY A O   
11   N N   . PHE A 4   ? 0.61480 0.61129 0.56153 -0.08227 -0.18397 0.18026  3   PHE A N   
12   C CA  . PHE A 4   ? 0.60506 0.61729 0.55288 -0.07922 -0.15623 0.17577  3   PHE A CA  
13   C C   . PHE A 4   ? 0.57188 0.58278 0.56697 -0.07518 -0.15177 0.15030  3   PHE A C   
14   O O   . PHE A 4   ? 0.56343 0.56904 0.60818 -0.07772 -0.16747 0.14957  3   PHE A O   
15   C CB  . PHE A 4   ? 0.59839 0.62280 0.55700 -0.08698 -0.15338 0.20631  3   PHE A CB  
16   C CG  . PHE A 4   ? 0.60366 0.64715 0.54471 -0.08394 -0.12412 0.20820  3   PHE A CG  
17   C CD1 . PHE A 4   ? 0.63272 0.68716 0.51587 -0.07882 -0.10621 0.21088  3   PHE A CD1 
18   C CD2 . PHE A 4   ? 0.56310 0.61347 0.54614 -0.08504 -0.11567 0.20576  3   PHE A CD2 
19   C CE1 . PHE A 4   ? 0.62004 0.69379 0.49142 -0.07491 -0.07926 0.21202  3   PHE A CE1 
20   C CE2 . PHE A 4   ? 0.58903 0.65705 0.55957 -0.08243 -0.09048 0.20819  3   PHE A CE2 
21   C CZ  . PHE A 4   ? 0.60465 0.68528 0.52126 -0.07738 -0.07167 0.21173  3   PHE A CZ  
22   N N   . ARG A 5   ? 0.57819 0.59446 0.55732 -0.06829 -0.13081 0.12959  4   ARG A N   
23   C CA  . ARG A 5   ? 0.54299 0.55991 0.55693 -0.06402 -0.12456 0.10507  4   ARG A CA  
24   C C   . ARG A 5   ? 0.53830 0.56730 0.54574 -0.06056 -0.09950 0.09879  4   ARG A C   
25   O O   . ARG A 5   ? 0.54749 0.58326 0.51690 -0.05885 -0.08478 0.10579  4   ARG A O   
26   C CB  . ARG A 5   ? 0.54259 0.55151 0.54758 -0.06008 -0.12862 0.08494  4   ARG A CB  
27   C CG  . ARG A 5   ? 0.55093 0.54733 0.56565 -0.06308 -0.15522 0.08899  4   ARG A CG  
28   C CD  . ARG A 5   ? 0.58531 0.58167 0.65949 -0.06454 -0.16920 0.08644  4   ARG A CD  
29   N NE  . ARG A 5   ? 0.56888 0.57581 0.67277 -0.05979 -0.15295 0.06696  4   ARG A NE  
30   C CZ  . ARG A 5   ? 0.55303 0.56370 0.67311 -0.05608 -0.14867 0.04707  4   ARG A CZ  
31   N NH1 . ARG A 5   ? 0.50650 0.51005 0.62299 -0.05685 -0.16127 0.04308  4   ARG A NH1 
32   N NH2 . ARG A 5   ? 0.53040 0.55300 0.67100 -0.05194 -0.13208 0.03208  4   ARG A NH2 
33   N N   . LYS A 6   ? 0.53787 0.57029 0.58255 -0.05860 -0.09514 0.08468  5   LYS A N   
34   C CA  . LYS A 6   ? 0.51204 0.55365 0.55143 -0.05483 -0.07371 0.07471  5   LYS A CA  
35   C C   . LYS A 6   ? 0.52195 0.56176 0.53413 -0.05017 -0.06344 0.05798  5   LYS A C   
36   O O   . LYS A 6   ? 0.49477 0.53196 0.52401 -0.04863 -0.06700 0.04203  5   LYS A O   
37   C CB  . LYS A 6   ? 0.51144 0.55602 0.59387 -0.05330 -0.07449 0.06292  5   LYS A CB  
38   C CG  . LYS A 6   ? 0.51788 0.57004 0.60723 -0.05386 -0.06412 0.06954  5   LYS A CG  
39   C CD  . LYS A 6   ? 0.57461 0.62561 0.70791 -0.05224 -0.07308 0.05958  5   LYS A CD  
40   C CE  . LYS A 6   ? 0.59198 0.64657 0.73960 -0.05498 -0.07194 0.07185  5   LYS A CE  
41   N NZ  . LYS A 6   ? 0.62497 0.68677 0.76181 -0.05124 -0.05408 0.06100  5   LYS A NZ  
42   N N   . MET A 7   ? 0.52313 0.56532 0.49556 -0.04767 -0.05127 0.06199  6   MET A N   
43   C CA  . MET A 7   ? 0.51578 0.55189 0.45896 -0.04309 -0.04696 0.04819  6   MET A CA  
44   C C   . MET A 7   ? 0.50762 0.55043 0.44248 -0.03867 -0.02732 0.03919  6   MET A C   
45   O O   . MET A 7   ? 0.52579 0.57855 0.45423 -0.03759 -0.01517 0.04870  6   MET A O   
46   C CB  . MET A 7   ? 0.54359 0.57441 0.44352 -0.04131 -0.05234 0.05704  6   MET A CB  
47   C CG  . MET A 7   ? 0.55753 0.57651 0.42925 -0.03624 -0.05600 0.04125  6   MET A CG  
48   S SD  . MET A 7   ? 0.67177 0.68286 0.49036 -0.03301 -0.06723 0.04993  6   MET A SD  
49   C CE  . MET A 7   ? 0.55247 0.55941 0.39717 -0.04236 -0.09020 0.06746  6   MET A CE  
50   N N   . ALA A 8   ? 0.47743 0.51552 0.41535 -0.03678 -0.02526 0.02274  7   ALA A N   
51   C CA  . ALA A 8   ? 0.50903 0.55082 0.43981 -0.03306 -0.00984 0.01436  7   ALA A CA  
52   C C   . ALA A 8   ? 0.52649 0.55876 0.42305 -0.02757 -0.00951 0.00635  7   ALA A C   
53   O O   . ALA A 8   ? 0.52944 0.55036 0.41305 -0.02740 -0.02310 0.00281  7   ALA A O   
54   C CB  . ALA A 8   ? 0.49583 0.54048 0.45598 -0.03537 -0.00754 0.00351  7   ALA A CB  
55   N N   . PHE A 9   ? 0.55558 0.59139 0.43927 -0.02237 0.00416  0.00250  8   PHE A N   
56   C CA  . PHE A 9   ? 0.55418 0.57986 0.40827 -0.01507 0.00389  -0.00820 8   PHE A CA  
57   C C   . PHE A 9   ? 0.54830 0.56066 0.41423 -0.01787 -0.00711 -0.02050 8   PHE A C   
58   O O   . PHE A 9   ? 0.53080 0.54758 0.42711 -0.02418 -0.00619 -0.02103 8   PHE A O   
59   C CB  . PHE A 9   ? 0.54404 0.57723 0.39002 -0.00839 0.02022  -0.01031 8   PHE A CB  
60   C CG  . PHE A 9   ? 0.58545 0.63380 0.41660 -0.00415 0.03201  0.00203  8   PHE A CG  
61   C CD1 . PHE A 9   ? 0.61758 0.66631 0.41120 0.00441  0.03344  0.00123  8   PHE A CD1 
62   C CD2 . PHE A 9   ? 0.56882 0.63232 0.42385 -0.00851 0.04137  0.01478  8   PHE A CD2 
63   C CE1 . PHE A 9   ? 0.62518 0.69313 0.40595 0.00795  0.04686  0.01538  8   PHE A CE1 
64   C CE2 . PHE A 9   ? 0.57391 0.65411 0.42078 -0.00610 0.05222  0.02953  8   PHE A CE2 
65   C CZ  . PHE A 9   ? 0.60131 0.68575 0.41130 0.00186  0.05645  0.03102  8   PHE A CZ  
66   N N   . PRO A 10  ? 0.57049 0.56737 0.41332 -0.01315 -0.01818 -0.03015 9   PRO A N   
67   C CA  . PRO A 10  ? 0.57056 0.55448 0.42787 -0.01623 -0.02912 -0.04026 9   PRO A CA  
68   C C   . PRO A 10  ? 0.56466 0.55246 0.43554 -0.01630 -0.01745 -0.04312 9   PRO A C   
69   O O   . PRO A 10  ? 0.56735 0.55757 0.42215 -0.00871 -0.00656 -0.04534 9   PRO A O   
70   C CB  . PRO A 10  ? 0.58640 0.55125 0.41042 -0.00823 -0.04333 -0.05138 9   PRO A CB  
71   C CG  . PRO A 10  ? 0.60680 0.57638 0.40046 -0.00356 -0.04265 -0.04477 9   PRO A CG  
72   C CD  . PRO A 10  ? 0.58522 0.57611 0.38699 -0.00443 -0.02210 -0.03216 9   PRO A CD  
73   N N   . SER A 11  ? 0.54982 0.54001 0.45134 -0.02487 -0.01968 -0.04200 10  SER A N   
74   C CA  . SER A 11  ? 0.52801 0.52605 0.44486 -0.02739 -0.00801 -0.04021 10  SER A CA  
75   C C   . SER A 11  ? 0.54249 0.52724 0.46411 -0.02863 -0.01577 -0.04564 10  SER A C   
76   O O   . SER A 11  ? 0.52297 0.51333 0.45800 -0.03224 -0.00846 -0.04211 10  SER A O   
77   C CB  . SER A 11  ? 0.51651 0.53129 0.46265 -0.03566 -0.00210 -0.03345 10  SER A CB  
78   O OG  . SER A 11  ? 0.50075 0.51493 0.46734 -0.04229 -0.01308 -0.03349 10  SER A OG  
79   N N   . GLY A 12  ? 0.55296 0.51891 0.46408 -0.02584 -0.03245 -0.05368 11  GLY A N   
80   C CA  . GLY A 12  ? 0.54831 0.49927 0.47084 -0.02851 -0.04418 -0.05763 11  GLY A CA  
81   C C   . GLY A 12  ? 0.55986 0.50631 0.47470 -0.02216 -0.03718 -0.06120 11  GLY A C   
82   O O   . GLY A 12  ? 0.55388 0.49888 0.48897 -0.02875 -0.03868 -0.05616 11  GLY A O   
83   N N   . LYS A 13  ? 0.54521 0.49116 0.43239 -0.00944 -0.02938 -0.06850 12  LYS A N   
84   C CA  . LYS A 13  ? 0.57430 0.51736 0.45717 -0.00152 -0.02280 -0.07306 12  LYS A CA  
85   C C   . LYS A 13  ? 0.56794 0.52706 0.47154 -0.00921 -0.00915 -0.06073 12  LYS A C   
86   O O   . LYS A 13  ? 0.56578 0.51918 0.47843 -0.00856 -0.01010 -0.06078 12  LYS A O   
87   C CB  . LYS A 13  ? 0.59804 0.54549 0.45049 0.01375  -0.01289 -0.08118 12  LYS A CB  
88   C CG  . LYS A 13  ? 0.63572 0.56619 0.45925 0.02492  -0.02646 -0.09669 12  LYS A CG  
89   C CD  . LYS A 13  ? 0.70424 0.64336 0.49729 0.04185  -0.01321 -0.10492 12  LYS A CD  
90   C CE  . LYS A 13  ? 0.77338 0.69657 0.53081 0.05497  -0.02644 -0.12248 12  LYS A CE  
91   N NZ  . LYS A 13  ? 0.76091 0.68455 0.50442 0.04851  -0.03398 -0.11623 12  LYS A NZ  
92   N N   . VAL A 14  ? 0.54243 0.52016 0.45356 -0.01591 0.00153  -0.05086 13  VAL A N   
93   C CA  . VAL A 14  ? 0.52203 0.51424 0.44935 -0.02227 0.01266  -0.04123 13  VAL A CA  
94   C C   . VAL A 14  ? 0.51778 0.51196 0.46703 -0.03465 0.00736  -0.03412 13  VAL A C   
95   O O   . VAL A 14  ? 0.51238 0.51104 0.47155 -0.03946 0.01112  -0.02749 13  VAL A O   
96   C CB  . VAL A 14  ? 0.50607 0.51613 0.43262 -0.02235 0.02460  -0.03579 13  VAL A CB  
97   C CG1 . VAL A 14  ? 0.49895 0.52150 0.43884 -0.02689 0.03373  -0.02879 13  VAL A CG1 
98   C CG2 . VAL A 14  ? 0.50810 0.51971 0.41480 -0.01162 0.03041  -0.03879 13  VAL A CG2 
99   N N   . GLU A 15  ? 0.50383 0.49665 0.46172 -0.04023 -0.00136 -0.03393 14  GLU A N   
100  C CA  . GLU A 15  ? 0.52080 0.51835 0.50291 -0.05207 -0.00607 -0.02564 14  GLU A CA  
101  C C   . GLU A 15  ? 0.52909 0.51210 0.51744 -0.05476 -0.01534 -0.02304 14  GLU A C   
102  O O   . GLU A 15  ? 0.51892 0.51102 0.52304 -0.06417 -0.01240 -0.01141 14  GLU A O   
103  C CB  . GLU A 15  ? 0.49060 0.48571 0.48425 -0.05632 -0.01767 -0.02682 14  GLU A CB  
104  C CG  . GLU A 15  ? 0.48972 0.50007 0.48544 -0.05566 -0.01098 -0.02710 14  GLU A CG  
105  C CD  . GLU A 15  ? 0.52949 0.53351 0.53476 -0.05803 -0.02581 -0.02945 14  GLU A CD  
106  O OE1 . GLU A 15  ? 0.51261 0.51405 0.53999 -0.06599 -0.03624 -0.02531 14  GLU A OE1 
107  O OE2 . GLU A 15  ? 0.53757 0.53913 0.52982 -0.05262 -0.02844 -0.03385 14  GLU A OE2 
108  N N   . GLY A 16  ? 0.52276 0.48339 0.49830 -0.04594 -0.02713 -0.03377 15  GLY A N   
109  C CA  . GLY A 16  ? 0.54250 0.48570 0.52656 -0.04683 -0.03911 -0.03311 15  GLY A CA  
110  C C   . GLY A 16  ? 0.55067 0.49952 0.53505 -0.04625 -0.02942 -0.02688 15  GLY A C   
111  O O   . GLY A 16  ? 0.54926 0.48392 0.54420 -0.04809 -0.04038 -0.02389 15  GLY A O   
112  N N   . CYS A 17  ? 0.51862 0.48644 0.49394 -0.04409 -0.01161 -0.02435 16  CYS A N   
113  C CA  . CYS A 17  ? 0.52684 0.49921 0.50129 -0.04234 -0.00404 -0.01966 16  CYS A CA  
114  C C   . CYS A 17  ? 0.50556 0.49883 0.48633 -0.05224 0.00703  -0.00667 16  CYS A C   
115  O O   . CYS A 17  ? 0.51310 0.51037 0.49156 -0.05108 0.01209  -0.00259 16  CYS A O   
116  C CB  . CYS A 17  ? 0.52758 0.50225 0.48566 -0.02849 0.00538  -0.02956 16  CYS A CB  
117  S SG  . CYS A 17  ? 0.59022 0.54481 0.53367 -0.01268 -0.00387 -0.04754 16  CYS A SG  
118  N N   . MET A 18  ? 0.49149 0.49880 0.48016 -0.06082 0.01043  -0.00116 17  MET A N   
119  C CA  . MET A 18  ? 0.48818 0.51751 0.47927 -0.06746 0.02209  0.00766  17  MET A CA  
120  C C   . MET A 18  ? 0.52462 0.55832 0.52778 -0.07964 0.01839  0.02306  17  MET A C   
121  O O   . MET A 18  ? 0.52443 0.55536 0.54335 -0.08723 0.01011  0.02902  17  MET A O   
122  C CB  . MET A 18  ? 0.50328 0.54937 0.49804 -0.06809 0.02958  0.00404  17  MET A CB  
123  C CG  . MET A 18  ? 0.49915 0.54227 0.48337 -0.05805 0.03225  -0.00712 17  MET A CG  
124  S SD  . MET A 18  ? 0.49396 0.53346 0.46445 -0.04918 0.03775  -0.00991 17  MET A SD  
125  C CE  . MET A 18  ? 0.48409 0.54284 0.45650 -0.05340 0.04688  -0.00497 17  MET A CE  
126  N N   . VAL A 19  ? 0.53149 0.57240 0.52809 -0.08217 0.02334  0.03108  18  VAL A N   
127  C CA  . VAL A 19  ? 0.52941 0.57768 0.53319 -0.09443 0.02123  0.04918  18  VAL A CA  
128  C C   . VAL A 19  ? 0.52464 0.59873 0.51665 -0.09675 0.03575  0.05365  18  VAL A C   
129  O O   . VAL A 19  ? 0.50758 0.58875 0.48831 -0.08836 0.04409  0.04167  18  VAL A O   
130  C CB  . VAL A 19  ? 0.53369 0.56136 0.53872 -0.09534 0.00828  0.05620  18  VAL A CB  
131  C CG1 . VAL A 19  ? 0.53923 0.54027 0.55476 -0.09005 -0.00721 0.04742  18  VAL A CG1 
132  C CG2 . VAL A 19  ? 0.50877 0.53518 0.49823 -0.08697 0.01268  0.05064  18  VAL A CG2 
133  N N   . GLN A 20  ? 0.52981 0.61787 0.52437 -0.10815 0.03760  0.07149  19  GLN A N   
134  C CA  . GLN A 20  ? 0.54927 0.66376 0.52868 -0.11017 0.05116  0.07619  19  GLN A CA  
135  C C   . GLN A 20  ? 0.53834 0.64602 0.50190 -0.11277 0.04570  0.08669  19  GLN A C   
136  O O   . GLN A 20  ? 0.55681 0.65240 0.52889 -0.12150 0.03417  0.10296  19  GLN A O   
137  C CB  . GLN A 20  ? 0.53654 0.67824 0.52850 -0.12106 0.05986  0.09054  19  GLN A CB  
138  C CG  . GLN A 20  ? 0.54646 0.71802 0.51975 -0.12391 0.07402  0.09865  19  GLN A CG  
139  C CD  . GLN A 20  ? 0.53591 0.73831 0.52504 -0.13530 0.08420  0.11626  19  GLN A CD  
140  O OE1 . GLN A 20  ? 0.55647 0.77519 0.56334 -0.13323 0.09236  0.10899  19  GLN A OE1 
141  N NE2 . GLN A 20  ? 0.58082 0.79261 0.56632 -0.14796 0.08326  0.14143  19  GLN A NE2 
142  N N   . VAL A 21  ? 0.51835 0.63170 0.46120 -0.10529 0.05117  0.07755  20  VAL A N   
143  C CA  . VAL A 21  ? 0.56488 0.67218 0.49112 -0.10695 0.04460  0.08626  20  VAL A CA  
144  C C   . VAL A 21  ? 0.56807 0.70259 0.47091 -0.10900 0.05599  0.09007  20  VAL A C   
145  O O   . VAL A 21  ? 0.56312 0.71084 0.45669 -0.10019 0.06564  0.07335  20  VAL A O   
146  C CB  . VAL A 21  ? 0.54466 0.63271 0.46772 -0.09567 0.03764  0.07200  20  VAL A CB  
147  C CG1 . VAL A 21  ? 0.56948 0.64851 0.48107 -0.09834 0.02704  0.08289  20  VAL A CG1 
148  C CG2 . VAL A 21  ? 0.53006 0.59710 0.47281 -0.09040 0.03083  0.06409  20  VAL A CG2 
149  N N   . THR A 22  ? 0.57240 0.71521 0.46522 -0.12004 0.05394  0.11186  21  THR A N   
150  C CA  . THR A 22  ? 0.61933 0.78974 0.48390 -0.12195 0.06484  0.11748  21  THR A CA  
151  C C   . THR A 22  ? 0.62853 0.78753 0.47037 -0.12466 0.05245  0.12846  21  THR A C   
152  O O   . THR A 22  ? 0.62195 0.76183 0.47478 -0.13303 0.03782  0.14588  21  THR A O   
153  C CB  . THR A 22  ? 0.59614 0.79548 0.46689 -0.13432 0.07656  0.13807  21  THR A CB  
154  O OG1 . THR A 22  ? 0.57070 0.78186 0.46472 -0.13105 0.08707  0.12672  21  THR A OG1 
155  C CG2 . THR A 22  ? 0.62533 0.85704 0.46173 -0.13508 0.08986  0.14431  21  THR A CG2 
156  N N   . CYS A 23  ? 0.64709 0.81597 0.45884 -0.11677 0.05598  0.11685  22  CYS A N   
157  C CA  . CYS A 23  ? 0.65848 0.82055 0.44287 -0.11906 0.04417  0.12673  22  CYS A CA  
158  C C   . CYS A 23  ? 0.69003 0.88224 0.43578 -0.11579 0.05682  0.12281  22  CYS A C   
159  O O   . CYS A 23  ? 0.70020 0.90146 0.43798 -0.10298 0.06490  0.09766  22  CYS A O   
160  C CB  . CYS A 23  ? 0.65654 0.79026 0.44565 -0.10920 0.02851  0.11106  22  CYS A CB  
161  S SG  . CYS A 23  ? 0.77764 0.89334 0.54819 -0.11444 0.00651  0.12798  22  CYS A SG  
162  N N   . GLY A 24  ? 0.72157 0.92968 0.44355 -0.12685 0.05801  0.14754  23  GLY A N   
163  C CA  . GLY A 24  ? 0.74350 0.98558 0.42487 -0.12332 0.07292  0.14500  23  GLY A CA  
164  C C   . GLY A 24  ? 0.74100 1.01442 0.43450 -0.11834 0.09677  0.13310  23  GLY A C   
165  O O   . GLY A 24  ? 0.71442 0.99858 0.43793 -0.12814 0.10525  0.14844  23  GLY A O   
166  N N   . THR A 25  ? 0.75256 1.03981 0.42590 -0.10243 0.10570  0.10461  24  THR A N   
167  C CA  . THR A 25  ? 0.77132 1.08334 0.46251 -0.09371 0.12545  0.08779  24  THR A CA  
168  C C   . THR A 25  ? 0.73235 1.02475 0.46221 -0.08827 0.12127  0.06956  24  THR A C   
169  O O   . THR A 25  ? 0.71977 1.02978 0.47557 -0.08706 0.13486  0.06483  24  THR A O   
170  C CB  . THR A 25  ? 0.81761 1.14403 0.47875 -0.07544 0.13284  0.06151  24  THR A CB  
171  O OG1 . THR A 25  ? 0.84585 1.15176 0.47796 -0.06824 0.11522  0.04578  24  THR A OG1 
172  C CG2 . THR A 25  ? 0.87599 1.22447 0.51420 -0.07692 0.14431  0.07668  24  THR A CG2 
173  N N   . THR A 26  ? 0.71679 0.97251 0.45393 -0.08449 0.10208  0.06014  25  THR A N   
174  C CA  . THR A 26  ? 0.70031 0.93696 0.46986 -0.07688 0.09772  0.04119  25  THR A CA  
175  C C   . THR A 26  ? 0.67313 0.89939 0.47857 -0.08706 0.09697  0.05605  25  THR A C   
176  O O   . THR A 26  ? 0.69234 0.90569 0.50216 -0.09844 0.08829  0.07769  25  THR A O   
177  C CB  . THR A 26  ? 0.69475 0.90003 0.46133 -0.06985 0.07869  0.02870  25  THR A CB  
178  O OG1 . THR A 26  ? 0.71851 0.93110 0.45615 -0.05835 0.07677  0.00956  25  THR A OG1 
179  C CG2 . THR A 26  ? 0.66531 0.85149 0.46637 -0.06461 0.07424  0.01566  25  THR A CG2 
180  N N   . THR A 27  ? 0.66408 0.89469 0.49565 -0.08240 0.10400  0.04359  26  THR A N   
181  C CA  . THR A 27  ? 0.60270 0.81943 0.46711 -0.08910 0.10032  0.05172  26  THR A CA  
182  C C   . THR A 27  ? 0.54617 0.74649 0.42821 -0.07866 0.09585  0.03050  26  THR A C   
183  O O   . THR A 27  ? 0.54864 0.76249 0.43296 -0.06943 0.10308  0.01299  26  THR A O   
184  C CB  . THR A 27  ? 0.56371 0.80713 0.44556 -0.09744 0.11348  0.06445  26  THR A CB  
185  O OG1 . THR A 27  ? 0.63972 0.89613 0.51015 -0.11035 0.11556  0.09066  26  THR A OG1 
186  C CG2 . THR A 27  ? 0.54248 0.76874 0.45839 -0.10167 0.10667  0.06686  26  THR A CG2 
187  N N   . LEU A 28  ? 0.55466 0.72688 0.44940 -0.07960 0.08372  0.03235  27  LEU A N   
188  C CA  . LEU A 28  ? 0.48582 0.64389 0.39719 -0.07157 0.08000  0.01707  27  LEU A CA  
189  C C   . LEU A 28  ? 0.49708 0.63632 0.42656 -0.07647 0.07310  0.02516  27  LEU A C   
190  O O   . LEU A 28  ? 0.48842 0.62617 0.42214 -0.08592 0.07066  0.04089  27  LEU A O   
191  C CB  . LEU A 28  ? 0.49250 0.63719 0.39502 -0.06284 0.07205  0.00523  27  LEU A CB  
192  C CG  . LEU A 28  ? 0.52566 0.65676 0.41433 -0.06480 0.06193  0.01340  27  LEU A CG  
193  C CD1 . LEU A 28  ? 0.51216 0.62326 0.41407 -0.06934 0.05413  0.02466  27  LEU A CD1 
194  C CD2 . LEU A 28  ? 0.50508 0.62829 0.39010 -0.05577 0.05437  -0.00020 27  LEU A CD2 
195  N N   . ASN A 29  ? 0.44877 0.57353 0.38881 -0.06976 0.06889  0.01449  28  ASN A N   
196  C CA  . ASN A 29  ? 0.46986 0.57748 0.42316 -0.07127 0.06261  0.01742  28  ASN A CA  
197  C C   . ASN A 29  ? 0.48040 0.56755 0.43059 -0.06825 0.05384  0.01923  28  ASN A C   
198  O O   . ASN A 29  ? 0.47515 0.56048 0.41800 -0.06360 0.05240  0.01578  28  ASN A O   
199  C CB  . ASN A 29  ? 0.44099 0.54742 0.40528 -0.06545 0.06386  0.00586  28  ASN A CB  
200  C CG  . ASN A 29  ? 0.45677 0.58436 0.42884 -0.06622 0.07179  0.00160  28  ASN A CG  
201  O OD1 . ASN A 29  ? 0.48745 0.62342 0.47077 -0.07276 0.07364  0.00838  28  ASN A OD1 
202  N ND2 . ASN A 29  ? 0.43212 0.56867 0.40191 -0.05914 0.07535  -0.00992 28  ASN A ND2 
203  N N   . GLY A 30  ? 0.45197 0.52378 0.41038 -0.07028 0.04675  0.02385  29  GLY A N   
204  C CA  . GLY A 30  ? 0.46983 0.52338 0.42936 -0.06511 0.03904  0.02310  29  GLY A CA  
205  C C   . GLY A 30  ? 0.47779 0.51748 0.44483 -0.05995 0.03500  0.01606  29  GLY A C   
206  O O   . GLY A 30  ? 0.48532 0.52496 0.45776 -0.06343 0.03374  0.01554  29  GLY A O   
207  N N   . LEU A 31  ? 0.45699 0.48607 0.42441 -0.05096 0.03270  0.01034  30  LEU A N   
208  C CA  . LEU A 31  ? 0.47195 0.48916 0.44079 -0.04285 0.02997  0.00123  30  LEU A CA  
209  C C   . LEU A 31  ? 0.48970 0.48904 0.46496 -0.04046 0.01886  0.00214  30  LEU A C   
210  O O   . LEU A 31  ? 0.50062 0.49722 0.47974 -0.03691 0.01701  0.00436  30  LEU A O   
211  C CB  . LEU A 31  ? 0.46344 0.48650 0.42896 -0.03290 0.03780  -0.00597 30  LEU A CB  
212  C CG  . LEU A 31  ? 0.48452 0.50039 0.44520 -0.02298 0.03811  -0.01551 30  LEU A CG  
213  C CD1 . LEU A 31  ? 0.47149 0.48720 0.42656 -0.02586 0.03694  -0.01903 30  LEU A CD1 
214  C CD2 . LEU A 31  ? 0.46046 0.48628 0.42089 -0.01426 0.04719  -0.01733 30  LEU A CD2 
215  N N   . TRP A 32  ? 0.50522 0.49130 0.48463 -0.04216 0.00927  0.00003  31  TRP A N   
216  C CA  . TRP A 32  ? 0.51162 0.47755 0.50126 -0.04090 -0.00552 0.00070  31  TRP A CA  
217  C C   . TRP A 32  ? 0.56416 0.51668 0.55003 -0.02551 -0.00898 -0.01676 31  TRP A C   
218  O O   . TRP A 32  ? 0.52857 0.47383 0.50933 -0.02319 -0.01344 -0.02531 31  TRP A O   
219  C CB  . TRP A 32  ? 0.51588 0.47507 0.51659 -0.05396 -0.01705 0.01128  31  TRP A CB  
220  C CG  . TRP A 32  ? 0.55385 0.49009 0.57006 -0.05503 -0.03624 0.01477  31  TRP A CG  
221  C CD1 . TRP A 32  ? 0.56946 0.49327 0.59136 -0.04702 -0.04328 0.01182  31  TRP A CD1 
222  C CD2 . TRP A 32  ? 0.56469 0.48702 0.59758 -0.06479 -0.05308 0.02239  31  TRP A CD2 
223  N NE1 . TRP A 32  ? 0.58047 0.48172 0.62073 -0.05058 -0.06433 0.01613  31  TRP A NE1 
224  C CE2 . TRP A 32  ? 0.56840 0.46787 0.61595 -0.06211 -0.07121 0.02340  31  TRP A CE2 
225  C CE3 . TRP A 32  ? 0.56383 0.49109 0.60490 -0.07569 -0.05588 0.02913  31  TRP A CE3 
226  C CZ2 . TRP A 32  ? 0.60528 0.48480 0.67508 -0.07064 -0.09343 0.03145  31  TRP A CZ2 
227  C CZ3 . TRP A 32  ? 0.56732 0.47695 0.63127 -0.08471 -0.07673 0.03810  31  TRP A CZ3 
228  C CH2 . TRP A 32  ? 0.59272 0.47773 0.67063 -0.08247 -0.09598 0.03944  31  TRP A CH2 
229  N N   . LEU A 33  ? 0.54714 0.49752 0.53545 -0.01434 -0.00722 -0.02241 32  LEU A N   
230  C CA  . LEU A 33  ? 0.55887 0.50022 0.54300 0.00278  -0.00839 -0.03998 32  LEU A CA  
231  C C   . LEU A 33  ? 0.57954 0.50397 0.58057 0.00910  -0.02183 -0.04287 32  LEU A C   
232  O O   . LEU A 33  ? 0.55766 0.48638 0.57060 0.00585  -0.02175 -0.03274 32  LEU A O   
233  C CB  . LEU A 33  ? 0.54942 0.51058 0.52377 0.01302  0.00996  -0.04493 32  LEU A CB  
234  C CG  . LEU A 33  ? 0.53662 0.51288 0.49630 0.00850  0.02132  -0.04270 32  LEU A CG  
235  C CD1 . LEU A 33  ? 0.51022 0.50694 0.46809 0.01491  0.03732  -0.04097 32  LEU A CD1 
236  C CD2 . LEU A 33  ? 0.54615 0.51258 0.49060 0.01348  0.01624  -0.05435 32  LEU A CD2 
237  N N   . ASP A 34  ? 0.59378 0.49750 0.59662 0.01862  -0.03559 -0.05748 33  ASP A N   
238  C CA  . ASP A 34  ? 0.59866 0.48114 0.62162 0.02530  -0.05342 -0.06243 33  ASP A CA  
239  C C   . ASP A 34  ? 0.60505 0.48153 0.64566 0.00617  -0.06548 -0.03946 33  ASP A C   
240  O O   . ASP A 34  ? 0.60150 0.47842 0.64045 -0.00969 -0.06906 -0.02692 33  ASP A O   
241  C CB  . ASP A 34  ? 0.61348 0.50532 0.64091 0.04341  -0.04338 -0.07350 33  ASP A CB  
242  C CG  . ASP A 34  ? 0.64669 0.54897 0.65326 0.06151  -0.02925 -0.09352 33  ASP A CG  
243  O OD1 . ASP A 34  ? 0.66421 0.55213 0.65693 0.06689  -0.03794 -0.10755 33  ASP A OD1 
244  O OD2 . ASP A 34  ? 0.63325 0.55880 0.63734 0.06988  -0.01018 -0.09401 33  ASP A OD2 
245  N N   . ASP A 35  ? 0.60627 0.47927 0.66399 0.00674  -0.07159 -0.03204 34  ASP A N   
246  C CA  . ASP A 35  ? 0.59656 0.46584 0.66655 -0.01171 -0.08264 -0.00782 34  ASP A CA  
247  C C   . ASP A 35  ? 0.58527 0.47822 0.64564 -0.01963 -0.06709 0.00655  34  ASP A C   
248  O O   . ASP A 35  ? 0.59359 0.48434 0.66314 -0.02821 -0.07564 0.02282  34  ASP A O   
249  C CB  . ASP A 35  ? 0.60176 0.44682 0.69841 -0.00780 -0.10587 -0.00669 34  ASP A CB  
250  C CG  . ASP A 35  ? 0.63365 0.48276 0.73995 0.00956  -0.10113 -0.01822 34  ASP A CG  
251  O OD1 . ASP A 35  ? 0.60569 0.47570 0.69839 0.01995  -0.07979 -0.02880 34  ASP A OD1 
252  O OD2 . ASP A 35  ? 0.67483 0.50703 0.80567 0.01236  -0.11955 -0.01517 34  ASP A OD2 
253  N N   . VAL A 36  ? 0.56443 0.47850 0.60645 -0.01693 -0.04666 0.00093  35  VAL A N   
254  C CA  . VAL A 36  ? 0.54948 0.48402 0.58332 -0.02238 -0.03397 0.01086  35  VAL A CA  
255  C C   . VAL A 36  ? 0.53901 0.48980 0.55485 -0.03194 -0.02139 0.01478  35  VAL A C   
256  O O   . VAL A 36  ? 0.52771 0.48018 0.53588 -0.02796 -0.01540 0.00438  35  VAL A O   
257  C CB  . VAL A 36  ? 0.53006 0.47577 0.56757 -0.00746 -0.02268 0.00004  35  VAL A CB  
258  C CG1 . VAL A 36  ? 0.50811 0.47112 0.54125 -0.01393 -0.01469 0.01058  35  VAL A CG1 
259  C CG2 . VAL A 36  ? 0.52878 0.46075 0.58821 0.00466  -0.03415 -0.00649 35  VAL A CG2 
260  N N   . VAL A 37  ? 0.50209 0.46483 0.51084 -0.04366 -0.01836 0.02899  36  VAL A N   
261  C CA  . VAL A 37  ? 0.48612 0.46714 0.47994 -0.05069 -0.00572 0.03114  36  VAL A CA  
262  C C   . VAL A 37  ? 0.49783 0.49315 0.48490 -0.04743 0.00327  0.02989  36  VAL A C   
263  O O   . VAL A 37  ? 0.50035 0.49544 0.48788 -0.05051 -0.00257 0.03850  36  VAL A O   
264  C CB  . VAL A 37  ? 0.48699 0.47270 0.47736 -0.06636 -0.00937 0.04753  36  VAL A CB  
265  C CG1 . VAL A 37  ? 0.45417 0.46206 0.43070 -0.07084 0.00504  0.04726  36  VAL A CG1 
266  C CG2 . VAL A 37  ? 0.51758 0.48908 0.52045 -0.07098 -0.02031 0.05019  36  VAL A CG2 
267  N N   . TYR A 38  ? 0.46641 0.47267 0.44859 -0.04163 0.01498  0.02002  37  TYR A N   
268  C CA  . TYR A 38  ? 0.44606 0.46484 0.42612 -0.03889 0.02149  0.01851  37  TYR A CA  
269  C C   . TYR A 38  ? 0.48188 0.51395 0.44928 -0.04615 0.02735  0.01988  37  TYR A C   
270  O O   . TYR A 38  ? 0.44362 0.47986 0.40760 -0.04825 0.03248  0.01652  37  TYR A O   
271  C CB  . TYR A 38  ? 0.44775 0.47117 0.43418 -0.02807 0.02963  0.00895  37  TYR A CB  
272  C CG  . TYR A 38  ? 0.47130 0.48596 0.46893 -0.01768 0.02741  0.00394  37  TYR A CG  
273  C CD1 . TYR A 38  ? 0.48155 0.48479 0.47654 -0.01383 0.02450  -0.00294 37  TYR A CD1 
274  C CD2 . TYR A 38  ? 0.47625 0.49476 0.48892 -0.01057 0.02751  0.00472  37  TYR A CD2 
275  C CE1 . TYR A 38  ? 0.48435 0.47985 0.48825 -0.00161 0.02225  -0.01118 37  TYR A CE1 
276  C CE2 . TYR A 38  ? 0.47527 0.48923 0.50014 0.00115  0.02722  -0.00173 37  TYR A CE2 
277  C CZ  . TYR A 38  ? 0.48837 0.49071 0.50722 0.00641  0.02491  -0.01084 37  TYR A CZ  
278  O OH  . TYR A 38  ? 0.51315 0.51115 0.54289 0.02063  0.02433  -0.02069 37  TYR A OH  
279  N N   . CYS A 39  ? 0.45351 0.49220 0.41464 -0.04885 0.02558  0.02342  38  CYS A N   
280  C CA  . CYS A 39  ? 0.44479 0.49725 0.39319 -0.05288 0.03121  0.02127  38  CYS A CA  
281  C C   . CYS A 39  ? 0.45500 0.51172 0.40094 -0.04962 0.02809  0.01769  38  CYS A C   
282  O O   . CYS A 39  ? 0.45669 0.50613 0.41084 -0.04688 0.02049  0.02064  38  CYS A O   
283  C CB  . CYS A 39  ? 0.47023 0.52790 0.40625 -0.06265 0.03062  0.03129  38  CYS A CB  
284  S SG  . CYS A 39  ? 0.57264 0.62600 0.49721 -0.06830 0.01954  0.04467  38  CYS A SG  
285  N N   . PRO A 40  ? 0.44757 0.51537 0.38572 -0.04897 0.03219  0.01020  39  PRO A N   
286  C CA  . PRO A 40  ? 0.47259 0.54179 0.40767 -0.04585 0.02530  0.00533  39  PRO A CA  
287  C C   . PRO A 40  ? 0.48776 0.55470 0.40565 -0.05006 0.01681  0.01271  39  PRO A C   
288  O O   . PRO A 40  ? 0.46852 0.53991 0.37113 -0.05641 0.01959  0.02061  39  PRO A O   
289  C CB  . PRO A 40  ? 0.47084 0.55179 0.39996 -0.04360 0.03083  -0.00617 39  PRO A CB  
290  C CG  . PRO A 40  ? 0.45411 0.53806 0.39259 -0.04406 0.04021  -0.00710 39  PRO A CG  
291  C CD  . PRO A 40  ? 0.44540 0.52338 0.38240 -0.04927 0.04132  0.00371  39  PRO A CD  
292  N N   . ARG A 41  ? 0.49135 0.55174 0.41305 -0.04724 0.00515  0.01195  40  ARG A N   
293  C CA  . ARG A 41  ? 0.50747 0.56338 0.41209 -0.05119 -0.00600 0.02005  40  ARG A CA  
294  C C   . ARG A 41  ? 0.52032 0.58696 0.39360 -0.05195 -0.00573 0.01429  40  ARG A C   
295  O O   . ARG A 41  ? 0.54408 0.61258 0.39400 -0.05748 -0.00952 0.02413  40  ARG A O   
296  C CB  . ARG A 41  ? 0.49188 0.53671 0.41383 -0.04791 -0.02083 0.02164  40  ARG A CB  
297  C CG  . ARG A 41  ? 0.47073 0.51626 0.40047 -0.04238 -0.02792 0.00999  40  ARG A CG  
298  C CD  . ARG A 41  ? 0.47156 0.50714 0.42337 -0.04084 -0.04395 0.01522  40  ARG A CD  
299  N NE  . ARG A 41  ? 0.48343 0.51771 0.44855 -0.03677 -0.05465 0.00613  40  ARG A NE  
300  C CZ  . ARG A 41  ? 0.47800 0.50525 0.46707 -0.03565 -0.07063 0.00996  40  ARG A CZ  
301  N NH1 . ARG A 41  ? 0.48249 0.50433 0.48482 -0.03722 -0.07696 0.02169  40  ARG A NH1 
302  N NH2 . ARG A 41  ? 0.46607 0.49126 0.46982 -0.03284 -0.08229 0.00198  40  ARG A NH2 
303  N N   . HIS A 42  ? 0.50761 0.58246 0.37939 -0.04604 -0.00121 -0.00133 41  HIS A N   
304  C CA  . HIS A 42  ? 0.54840 0.63552 0.38894 -0.04403 0.00005  -0.01008 41  HIS A CA  
305  C C   . HIS A 42  ? 0.56502 0.66946 0.38692 -0.05000 0.01529  -0.00190 41  HIS A C   
306  O O   . HIS A 42  ? 0.58550 0.70621 0.38118 -0.04747 0.02088  -0.00902 41  HIS A O   
307  C CB  . HIS A 42  ? 0.53306 0.62405 0.38007 -0.03481 -0.00037 -0.03078 41  HIS A CB  
308  C CG  . HIS A 42  ? 0.52028 0.62000 0.38521 -0.03352 0.01377  -0.03569 41  HIS A CG  
309  N ND1 . HIS A 42  ? 0.49715 0.58849 0.39315 -0.03227 0.01305  -0.03575 41  HIS A ND1 
310  C CD2 . HIS A 42  ? 0.50378 0.62108 0.36059 -0.03317 0.02828  -0.04010 41  HIS A CD2 
311  C CE1 . HIS A 42  ? 0.49954 0.60019 0.40353 -0.03150 0.02469  -0.04005 41  HIS A CE1 
312  N NE2 . HIS A 42  ? 0.49846 0.61482 0.38160 -0.03194 0.03379  -0.04314 41  HIS A NE2 
313  N N   . VAL A 43  ? 0.56209 0.66438 0.39808 -0.05731 0.02147  0.01255  42  VAL A N   
314  C CA  . VAL A 43  ? 0.58134 0.69828 0.40411 -0.06580 0.03183  0.02608  42  VAL A CA  
315  C C   . VAL A 43  ? 0.60626 0.72569 0.39969 -0.07167 0.02462  0.03968  42  VAL A C   
316  O O   . VAL A 43  ? 0.63615 0.77487 0.41013 -0.07786 0.03423  0.05018  42  VAL A O   
317  C CB  . VAL A 43  ? 0.54684 0.65498 0.39449 -0.07229 0.03404  0.03833  42  VAL A CB  
318  C CG1 . VAL A 43  ? 0.54154 0.62832 0.39865 -0.07512 0.01949  0.04970  42  VAL A CG1 
319  C CG2 . VAL A 43  ? 0.58266 0.70763 0.42528 -0.08172 0.04456  0.05210  42  VAL A CG2 
320  N N   . ILE A 44  ? 0.62227 0.72411 0.41273 -0.07021 0.00748  0.04122  43  ILE A N   
321  C CA  . ILE A 44  ? 0.62566 0.72733 0.38664 -0.07596 -0.00272 0.05513  43  ILE A CA  
322  C C   . ILE A 44  ? 0.64843 0.76076 0.37349 -0.06877 -0.00510 0.04093  43  ILE A C   
323  O O   . ILE A 44  ? 0.71196 0.82525 0.40536 -0.07244 -0.01436 0.05088  43  ILE A O   
324  C CB  . ILE A 44  ? 0.64488 0.72176 0.42146 -0.07810 -0.02290 0.06502  43  ILE A CB  
325  C CG1 . ILE A 44  ? 0.63932 0.70438 0.42386 -0.06824 -0.03576 0.04797  43  ILE A CG1 
326  C CG2 . ILE A 44  ? 0.62738 0.69243 0.44061 -0.08128 -0.02140 0.07320  43  ILE A CG2 
327  C CD1 . ILE A 44  ? 0.62672 0.67091 0.43076 -0.06940 -0.05548 0.05720  43  ILE A CD1 
328  N N   . CYS A 45  ? 0.65693 0.77628 0.38508 -0.05814 0.00122  0.01755  44  CYS A N   
329  C CA  . CYS A 45  ? 0.72191 0.84848 0.41808 -0.04851 -0.00367 -0.00097 44  CYS A CA  
330  C C   . CYS A 45  ? 0.77441 0.93240 0.44094 -0.04671 0.01624  -0.00457 44  CYS A C   
331  O O   . CYS A 45  ? 0.76341 0.93764 0.44607 -0.05001 0.03470  -0.00009 44  CYS A O   
332  C CB  . CYS A 45  ? 0.72608 0.84170 0.44534 -0.03698 -0.01108 -0.02546 44  CYS A CB  
333  S SG  . CYS A 45  ? 0.63439 0.71941 0.38862 -0.03751 -0.03417 -0.02220 44  CYS A SG  
334  N N   . THR A 46  ? 0.84230 1.01003 0.46537 -0.04084 0.01204  -0.01295 45  THR A N   
335  C CA  . THR A 46  ? 0.89508 1.09562 0.48903 -0.03375 0.03126  -0.02440 45  THR A CA  
336  C C   . THR A 46  ? 0.96068 1.15951 0.56052 -0.01626 0.02804  -0.05972 45  THR A C   
337  O O   . THR A 46  ? 0.94253 1.11452 0.56600 -0.01149 0.00928  -0.07210 45  THR A O   
338  C CB  . THR A 46  ? 0.93022 1.14576 0.46838 -0.03543 0.03003  -0.01503 45  THR A CB  
339  O OG1 . THR A 46  ? 0.97991 1.17436 0.49455 -0.02623 0.00552  -0.03206 45  THR A OG1 
340  C CG2 . THR A 46  ? 0.87904 1.09205 0.41564 -0.05398 0.02837  0.02249  45  THR A CG2 
341  N N   . SER A 47  ? 1.05286 1.28200 0.63413 -0.00654 0.04625  -0.07532 46  SER A N   
342  C CA  . SER A 47  ? 1.04882 1.27674 0.63441 0.01182  0.04145  -0.11107 46  SER A CA  
343  C C   . SER A 47  ? 1.10302 1.30791 0.66288 0.02143  0.01432  -0.12941 46  SER A C   
344  O O   . SER A 47  ? 1.11963 1.30837 0.69765 0.03373  -0.00040 -0.15585 46  SER A O   
345  C CB  . SER A 47  ? 1.11374 1.38002 0.68062 0.02226  0.06569  -0.12468 46  SER A CB  
346  O OG  . SER A 47  ? 1.22198 1.48250 0.79761 0.04122  0.05857  -0.15997 46  SER A OG  
347  N N   . GLU A 48  ? 1.04965 1.25117 0.56998 0.01532  0.00493  -0.11462 47  GLU A N   
348  C CA  . GLU A 48  ? 1.08964 1.26810 0.58334 0.02334  -0.02378 -0.13009 47  GLU A CA  
349  C C   . GLU A 48  ? 1.05345 1.19412 0.58724 0.01579  -0.04934 -0.12114 47  GLU A C   
350  O O   . GLU A 48  ? 1.03644 1.15392 0.57823 0.02481  -0.07433 -0.14139 47  GLU A O   
351  C CB  . GLU A 48  ? 1.13126 1.32330 0.56371 0.01958  -0.02382 -0.11618 47  GLU A CB  
352  C CG  . GLU A 48  ? 1.21704 1.37863 0.62873 0.01857  -0.05721 -0.11503 47  GLU A CG  
353  C CD  . GLU A 48  ? 1.29544 1.46406 0.65788 0.00905  -0.05621 -0.08944 47  GLU A CD  
354  O OE1 . GLU A 48  ? 1.36326 1.55139 0.72766 -0.00349 -0.03344 -0.06091 47  GLU A OE1 
355  O OE2 . GLU A 48  ? 1.32662 1.47605 0.65394 0.01337  -0.07943 -0.09618 47  GLU A OE2 
356  N N   . ASP A 49  ? 1.02230 1.15730 0.58422 -0.00011 -0.04395 -0.09136 48  ASP A N   
357  C CA  . ASP A 49  ? 0.98093 1.08521 0.58137 -0.00666 -0.06507 -0.08128 48  ASP A CA  
358  C C   . ASP A 49  ? 0.94743 1.03917 0.59872 -0.00113 -0.06886 -0.09611 48  ASP A C   
359  O O   . ASP A 49  ? 0.95017 1.01859 0.63273 -0.00305 -0.08873 -0.09347 48  ASP A O   
360  C CB  . ASP A 49  ? 0.91942 1.02260 0.53660 -0.02280 -0.05718 -0.04828 48  ASP A CB  
361  C CG  . ASP A 49  ? 0.95437 1.06527 0.52729 -0.03099 -0.05886 -0.02796 48  ASP A CG  
362  O OD1 . ASP A 49  ? 1.03305 1.13819 0.56785 -0.02587 -0.07644 -0.03588 48  ASP A OD1 
363  O OD2 . ASP A 49  ? 0.91924 1.04096 0.49580 -0.04289 -0.04446 -0.00333 48  ASP A OD2 
364  N N   . MET A 50  ? 0.91948 1.02753 0.58171 0.00526  -0.05073 -0.10990 49  MET A N   
365  C CA  . MET A 50  ? 0.85894 0.95659 0.57072 0.00809  -0.05278 -0.11852 49  MET A CA  
366  C C   . MET A 50  ? 0.82309 0.89919 0.54903 0.01779  -0.08000 -0.13966 49  MET A C   
367  O O   . MET A 50  ? 0.78388 0.84584 0.55563 0.01609  -0.08827 -0.13806 49  MET A O   
368  C CB  . MET A 50  ? 0.85162 0.97151 0.57001 0.01340  -0.03004 -0.12927 49  MET A CB  
369  C CG  . MET A 50  ? 0.83473 0.97355 0.55465 0.00237  -0.00507 -0.10696 49  MET A CG  
370  S SD  . MET A 50  ? 0.85651 0.97936 0.62576 -0.00944 -0.00373 -0.08557 49  MET A SD  
371  C CE  . MET A 50  ? 0.68540 0.83342 0.46258 -0.01362 0.02408  -0.07858 49  MET A CE  
372  N N   . LEU A 51  ? 0.86663 0.94012 0.55473 0.02782  -0.09505 -0.15881 50  LEU A N   
373  C CA  . LEU A 51  ? 0.86900 0.91927 0.57267 0.03729  -0.12505 -0.18033 50  LEU A CA  
374  C C   . LEU A 51  ? 0.87521 0.90106 0.60619 0.02792  -0.14843 -0.16310 50  LEU A C   
375  O O   . LEU A 51  ? 0.85536 0.86456 0.63351 0.02765  -0.16450 -0.16498 50  LEU A O   
376  C CB  . LEU A 51  ? 0.86735 0.92067 0.51865 0.05208  -0.13632 -0.20781 50  LEU A CB  
377  C CG  . LEU A 51  ? 0.92275 0.95147 0.58304 0.06524  -0.17046 -0.23703 50  LEU A CG  
378  C CD1 . LEU A 51  ? 0.96390 0.96793 0.61538 0.06092  -0.20202 -0.23037 50  LEU A CD1 
379  C CD2 . LEU A 51  ? 0.88962 0.90549 0.61394 0.06567  -0.17782 -0.24185 50  LEU A CD2 
380  N N   . ASN A 52  ? 0.87756 0.90238 0.58258 0.01983  -0.15093 -0.14461 51  ASN A N   
381  C CA  . ASN A 52  ? 0.91425 0.91754 0.64304 0.01225  -0.17475 -0.12926 51  ASN A CA  
382  C C   . ASN A 52  ? 0.89945 0.90917 0.62197 -0.00064 -0.16179 -0.09944 51  ASN A C   
383  O O   . ASN A 52  ? 0.97542 0.98162 0.66299 -0.00383 -0.17232 -0.09088 51  ASN A O   
384  C CB  . ASN A 52  ? 1.00882 0.99501 0.70777 0.01994  -0.20707 -0.14603 51  ASN A CB  
385  C CG  . ASN A 52  ? 1.07763 1.04225 0.80409 0.01210  -0.23397 -0.12984 51  ASN A CG  
386  O OD1 . ASN A 52  ? 1.13179 1.08882 0.91637 0.00642  -0.23796 -0.11832 51  ASN A OD1 
387  N ND2 . ASN A 52  ? 1.12284 1.07946 0.80788 0.01177  -0.25223 -0.12775 51  ASN A ND2 
388  N N   . PRO A 53  ? 0.84383 0.86170 0.59965 -0.00800 -0.14074 -0.08324 52  PRO A N   
389  C CA  . PRO A 53  ? 0.79076 0.81303 0.54361 -0.01912 -0.12978 -0.05697 52  PRO A CA  
390  C C   . PRO A 53  ? 0.74019 0.74464 0.52628 -0.02483 -0.14918 -0.04137 52  PRO A C   
391  O O   . PRO A 53  ? 0.75968 0.75517 0.59140 -0.02343 -0.15827 -0.04321 52  PRO A O   
392  C CB  . PRO A 53  ? 0.75293 0.78889 0.53021 -0.02222 -0.10247 -0.05090 52  PRO A CB  
393  C CG  . PRO A 53  ? 0.74644 0.77741 0.56047 -0.01586 -0.10631 -0.06566 52  PRO A CG  
394  C CD  . PRO A 53  ? 0.82350 0.84633 0.61900 -0.00600 -0.12725 -0.08875 52  PRO A CD  
395  N N   . ASN A 54  ? 0.71701 0.71789 0.48186 -0.03147 -0.15588 -0.02456 53  ASN A N   
396  C CA  . ASN A 54  ? 0.69653 0.68348 0.49466 -0.03731 -0.17114 -0.00671 53  ASN A CA  
397  C C   . ASN A 54  ? 0.69345 0.68834 0.50112 -0.04494 -0.15091 0.01289  53  ASN A C   
398  O O   . ASN A 54  ? 0.68215 0.67897 0.45974 -0.05127 -0.15019 0.02685  53  ASN A O   
399  C CB  . ASN A 54  ? 0.70661 0.67987 0.47632 -0.03869 -0.19927 -0.00270 53  ASN A CB  
400  C CG  . ASN A 54  ? 0.70617 0.66444 0.51902 -0.04303 -0.21883 0.01307  53  ASN A CG  
401  O OD1 . ASN A 54  ? 0.72723 0.68829 0.57409 -0.04736 -0.20713 0.02812  53  ASN A OD1 
402  N ND2 . ASN A 54  ? 0.73189 0.67435 0.54514 -0.04085 -0.24977 0.00835  53  ASN A ND2 
403  N N   . TYR A 55  ? 0.66258 0.66160 0.51224 -0.04432 -0.13585 0.01422  54  TYR A N   
404  C CA  . TYR A 55  ? 0.63872 0.64557 0.49420 -0.04936 -0.11523 0.02677  54  TYR A CA  
405  C C   . TYR A 55  ? 0.65017 0.64720 0.51456 -0.05555 -0.12531 0.04659  54  TYR A C   
406  O O   . TYR A 55  ? 0.64365 0.64426 0.49590 -0.06156 -0.11540 0.05874  54  TYR A O   
407  C CB  . TYR A 55  ? 0.58615 0.59840 0.48129 -0.04593 -0.09936 0.02222  54  TYR A CB  
408  C CG  . TYR A 55  ? 0.56514 0.58902 0.44871 -0.04194 -0.08452 0.00676  54  TYR A CG  
409  C CD1 . TYR A 55  ? 0.55573 0.59204 0.41715 -0.04454 -0.06526 0.00747  54  TYR A CD1 
410  C CD2 . TYR A 55  ? 0.55283 0.57504 0.45174 -0.03584 -0.09166 -0.00777 54  TYR A CD2 
411  C CE1 . TYR A 55  ? 0.55000 0.59776 0.40495 -0.04020 -0.05253 -0.00694 54  TYR A CE1 
412  C CE2 . TYR A 55  ? 0.56615 0.59760 0.45813 -0.03153 -0.08028 -0.02228 54  TYR A CE2 
413  C CZ  . TYR A 55  ? 0.54217 0.58684 0.41197 -0.03324 -0.06031 -0.02237 54  TYR A CZ  
414  O OH  . TYR A 55  ? 0.49901 0.55364 0.36579 -0.02827 -0.04984 -0.03707 54  TYR A OH  
415  N N   . GLU A 56  ? 0.65555 0.63986 0.54473 -0.05439 -0.14660 0.05079  55  GLU A N   
416  C CA  . GLU A 56  ? 0.68669 0.66044 0.58524 -0.05953 -0.15948 0.06903  55  GLU A CA  
417  C C   . GLU A 56  ? 0.69939 0.67078 0.54733 -0.06680 -0.16857 0.07950  55  GLU A C   
418  O O   . GLU A 56  ? 0.70877 0.67948 0.54985 -0.07386 -0.16483 0.09584  55  GLU A O   
419  C CB  . GLU A 56  ? 0.71551 0.67799 0.65322 -0.05634 -0.18196 0.07102  55  GLU A CB  
420  C CG  . GLU A 56  ? 0.76558 0.73219 0.76051 -0.05144 -0.17215 0.07227  55  GLU A CG  
421  C CD  . GLU A 56  ? 0.84665 0.80627 0.88547 -0.04864 -0.19360 0.07678  55  GLU A CD  
422  O OE1 . GLU A 56  ? 0.88021 0.82706 0.90679 -0.05191 -0.21913 0.08295  55  GLU A OE1 
423  O OE2 . GLU A 56  ? 0.86028 0.82875 0.94646 -0.04324 -0.18499 0.07513  55  GLU A OE2 
424  N N   . ASP A 57  ? 0.71470 0.68515 0.52612 -0.06504 -0.18128 0.07053  56  ASP A N   
425  C CA  . ASP A 57  ? 0.74668 0.71804 0.50392 -0.07127 -0.18936 0.08088  56  ASP A CA  
426  C C   . ASP A 57  ? 0.74302 0.73351 0.46989 -0.07594 -0.16323 0.08565  56  ASP A C   
427  O O   . ASP A 57  ? 0.77829 0.77135 0.48105 -0.08537 -0.16390 0.10612  56  ASP A O   
428  C CB  . ASP A 57  ? 0.75301 0.72081 0.47395 -0.06558 -0.20710 0.06530  56  ASP A CB  
429  C CG  . ASP A 57  ? 0.75653 0.70436 0.50807 -0.06274 -0.23760 0.06353  56  ASP A CG  
430  O OD1 . ASP A 57  ? 0.74275 0.68239 0.54381 -0.06500 -0.24306 0.07553  56  ASP A OD1 
431  O OD2 . ASP A 57  ? 0.76357 0.70438 0.49135 -0.05750 -0.25685 0.04927  56  ASP A OD2 
432  N N   . LEU A 58  ? 0.73854 0.74314 0.46935 -0.07018 -0.14123 0.06876  57  LEU A N   
433  C CA  . LEU A 58  ? 0.76955 0.79441 0.47800 -0.07431 -0.11633 0.07290  57  LEU A CA  
434  C C   . LEU A 58  ? 0.75204 0.77468 0.48901 -0.08275 -0.10786 0.09235  57  LEU A C   
435  O O   . LEU A 58  ? 0.77810 0.81023 0.49454 -0.09209 -0.10061 0.11002  57  LEU A O   
436  C CB  . LEU A 58  ? 0.73752 0.77592 0.45048 -0.06540 -0.09774 0.04958  57  LEU A CB  
437  C CG  . LEU A 58  ? 0.78071 0.82280 0.46258 -0.05566 -0.10496 0.02712  57  LEU A CG  
438  C CD1 . LEU A 58  ? 0.75793 0.80956 0.45630 -0.04669 -0.08971 0.00479  57  LEU A CD1 
439  C CD2 . LEU A 58  ? 0.83858 0.89629 0.46148 -0.05793 -0.10182 0.03192  57  LEU A CD2 
440  N N   . LEU A 59  ? 0.71133 0.72212 0.49637 -0.07932 -0.10943 0.08960  58  LEU A N   
441  C CA  . LEU A 59  ? 0.71463 0.72075 0.52835 -0.08443 -0.10337 0.10316  58  LEU A CA  
442  C C   . LEU A 59  ? 0.73744 0.73031 0.54943 -0.09332 -0.12225 0.12652  58  LEU A C   
443  O O   . LEU A 59  ? 0.73064 0.72259 0.54888 -0.10119 -0.11856 0.14230  58  LEU A O   
444  C CB  . LEU A 59  ? 0.65366 0.65223 0.51527 -0.07612 -0.10076 0.09238  58  LEU A CB  
445  C CG  . LEU A 59  ? 0.63056 0.62259 0.52310 -0.07760 -0.09559 0.10051  58  LEU A CG  
446  C CD1 . LEU A 59  ? 0.64905 0.65325 0.53083 -0.08133 -0.07547 0.09988  58  LEU A CD1 
447  C CD2 . LEU A 59  ? 0.57081 0.55769 0.50640 -0.06756 -0.09463 0.09000  58  LEU A CD2 
448  N N   . ILE A 60  ? 0.72945 0.71059 0.53528 -0.09262 -0.14503 0.12972  59  ILE A N   
449  C CA  . ILE A 60  ? 0.74334 0.70980 0.55003 -0.10096 -0.16668 0.15277  59  ILE A CA  
450  C C   . ILE A 60  ? 0.79201 0.76828 0.55570 -0.11352 -0.16393 0.17367  59  ILE A C   
451  O O   . ILE A 60  ? 0.82865 0.79474 0.60024 -0.12319 -0.17627 0.19722  59  ILE A O   
452  C CB  . ILE A 60  ? 0.75099 0.70371 0.55941 -0.09702 -0.19297 0.15015  59  ILE A CB  
453  C CG1 . ILE A 60  ? 0.71705 0.65901 0.58485 -0.08823 -0.19871 0.14147  59  ILE A CG1 
454  C CG2 . ILE A 60  ? 0.74235 0.68380 0.52712 -0.10711 -0.21725 0.17431  59  ILE A CG2 
455  C CD1 . ILE A 60  ? 0.72107 0.65112 0.60203 -0.08430 -0.22440 0.13901  59  ILE A CD1 
456  N N   . ARG A 61  ? 0.81978 0.81728 0.54114 -0.11347 -0.14744 0.16639  60  ARG A N   
457  C CA  . ARG A 61  ? 0.84034 0.85457 0.52191 -0.12520 -0.13967 0.18727  60  ARG A CA  
458  C C   . ARG A 61  ? 0.82556 0.85187 0.52627 -0.13150 -0.11849 0.19552  60  ARG A C   
459  O O   . ARG A 61  ? 0.90911 0.95614 0.58109 -0.14089 -0.10644 0.21147  60  ARG A O   
460  C CB  . ARG A 61  ? 0.92927 0.96484 0.55606 -0.12059 -0.13018 0.17466  60  ARG A CB  
461  C CG  . ARG A 61  ? 0.98738 1.01025 0.59126 -0.11325 -0.15305 0.16282  60  ARG A CG  
462  C CD  . ARG A 61  ? 1.10691 1.15118 0.64695 -0.10987 -0.14602 0.15464  60  ARG A CD  
463  N NE  . ARG A 61  ? 1.12594 1.19597 0.66025 -0.10370 -0.11584 0.13725  60  ARG A NE  
464  C CZ  . ARG A 61  ? 1.08388 1.15946 0.60993 -0.08957 -0.11002 0.10589  60  ARG A CZ  
465  N NH1 . ARG A 61  ? 1.13526 1.19281 0.65598 -0.08042 -0.13243 0.08804  60  ARG A NH1 
466  N NH2 . ARG A 61  ? 1.05648 1.15542 0.58283 -0.08463 -0.08317 0.09244  60  ARG A NH2 
467  N N   . LYS A 62  ? 0.78820 0.80351 0.53621 -0.12655 -0.11399 0.18567  61  LYS A N   
468  C CA  . LYS A 62  ? 0.78342 0.80734 0.55126 -0.13099 -0.09648 0.18962  61  LYS A CA  
469  C C   . LYS A 62  ? 0.75019 0.75147 0.55912 -0.13591 -0.11117 0.20407  61  LYS A C   
470  O O   . LYS A 62  ? 0.73678 0.71805 0.57585 -0.12783 -0.12455 0.19523  61  LYS A O   
471  C CB  . LYS A 62  ? 0.73550 0.76750 0.51898 -0.11920 -0.07707 0.16182  61  LYS A CB  
472  C CG  . LYS A 62  ? 0.73472 0.79119 0.48285 -0.11450 -0.06017 0.14712  61  LYS A CG  
473  C CD  . LYS A 62  ? 0.76867 0.84980 0.48802 -0.12545 -0.04696 0.16529  61  LYS A CD  
474  C CE  . LYS A 62  ? 0.75607 0.86475 0.44613 -0.11808 -0.02683 0.14706  61  LYS A CE  
475  N NZ  . LYS A 62  ? 0.84185 0.95016 0.49692 -0.10922 -0.03607 0.13236  61  LYS A NZ  
476  N N   . SER A 63  ? 0.73807 0.74347 0.55088 -0.14863 -0.10916 0.22599  62  SER A N   
477  C CA  . SER A 63  ? 0.73054 0.71377 0.58396 -0.15336 -0.12395 0.23865  62  SER A CA  
478  C C   . SER A 63  ? 0.69494 0.68171 0.57366 -0.15085 -0.10821 0.22746  62  SER A C   
479  O O   . SER A 63  ? 0.70440 0.71267 0.56853 -0.14815 -0.08612 0.21506  62  SER A O   
480  C CB  . SER A 63  ? 0.76299 0.74405 0.60725 -0.17146 -0.13939 0.27531  62  SER A CB  
481  O OG  . SER A 63  ? 0.83449 0.81128 0.65177 -0.17406 -0.15606 0.28667  62  SER A OG  
482  N N   . ASN A 64  ? 0.68424 0.64832 0.60199 -0.15101 -0.12193 0.23104  63  ASN A N   
483  C CA  . ASN A 64  ? 0.68696 0.64949 0.62942 -0.14755 -0.11171 0.21895  63  ASN A CA  
484  C C   . ASN A 64  ? 0.70494 0.69052 0.63397 -0.16051 -0.09682 0.23326  63  ASN A C   
485  O O   . ASN A 64  ? 0.67092 0.66971 0.60089 -0.15557 -0.07834 0.21710  63  ASN A O   
486  C CB  . ASN A 64  ? 0.66527 0.59807 0.64889 -0.14651 -0.13328 0.22268  63  ASN A CB  
487  C CG  . ASN A 64  ? 0.66633 0.58061 0.67094 -0.12995 -0.14320 0.20312  63  ASN A CG  
488  O OD1 . ASN A 64  ? 0.64631 0.56997 0.64287 -0.11759 -0.12977 0.18180  63  ASN A OD1 
489  N ND2 . ASN A 64  ? 0.66837 0.55714 0.70385 -0.12953 -0.16735 0.21099  63  ASN A ND2 
490  N N   . HIS A 65  ? 0.70474 0.69719 0.62295 -0.17752 -0.10471 0.26518  64  HIS A N   
491  C CA  . HIS A 65  ? 0.70926 0.72722 0.62084 -0.19122 -0.09048 0.28322  64  HIS A CA  
492  C C   . HIS A 65  ? 0.70464 0.75793 0.57858 -0.18748 -0.06342 0.27248  64  HIS A C   
493  O O   . HIS A 65  ? 0.73198 0.81145 0.60341 -0.19572 -0.04708 0.28236  64  HIS A O   
494  C CB  . HIS A 65  ? 0.74622 0.76510 0.65661 -0.21139 -0.10589 0.32408  64  HIS A CB  
495  C CG  . HIS A 65  ? 0.76767 0.79890 0.63536 -0.21548 -0.10767 0.33838  64  HIS A CG  
496  N ND1 . HIS A 65  ? 0.79666 0.80333 0.66229 -0.21182 -0.13042 0.33997  64  HIS A ND1 
497  C CD2 . HIS A 65  ? 0.79576 0.86174 0.62015 -0.22197 -0.09031 0.35079  64  HIS A CD2 
498  C CE1 . HIS A 65  ? 0.85002 0.87352 0.67110 -0.21664 -0.12883 0.35315  64  HIS A CE1 
499  N NE2 . HIS A 65  ? 0.83621 0.89617 0.62960 -0.22217 -0.10396 0.35902  64  HIS A NE2 
500  N N   . ASN A 66  ? 0.70961 0.76446 0.55776 -0.17494 -0.05954 0.25233  65  ASN A N   
501  C CA  . ASN A 66  ? 0.70288 0.78718 0.51867 -0.16812 -0.03651 0.23629  65  ASN A CA  
502  C C   . ASN A 66  ? 0.69323 0.78097 0.52716 -0.15647 -0.02096 0.20825  65  ASN A C   
503  O O   . ASN A 66  ? 0.67453 0.78669 0.48893 -0.15070 -0.00201 0.19426  65  ASN A O   
504  C CB  . ASN A 66  ? 0.70719 0.78843 0.49129 -0.15903 -0.04248 0.22442  65  ASN A CB  
505  C CG  . ASN A 66  ? 0.77062 0.85275 0.52693 -0.17040 -0.05676 0.25209  65  ASN A CG  
506  O OD1 . ASN A 66  ? 0.77253 0.83141 0.53021 -0.16852 -0.07824 0.25450  65  ASN A OD1 
507  N ND2 . ASN A 66  ? 0.76064 0.87137 0.49246 -0.18250 -0.04494 0.27457  65  ASN A ND2 
508  N N   . PHE A 67  ? 0.65611 0.72005 0.52573 -0.15207 -0.02941 0.19918  66  PHE A N   
509  C CA  . PHE A 67  ? 0.66355 0.72817 0.54939 -0.14139 -0.01725 0.17438  66  PHE A CA  
510  C C   . PHE A 67  ? 0.65104 0.71915 0.56110 -0.15059 -0.01457 0.18505  66  PHE A C   
511  O O   . PHE A 67  ? 0.65816 0.70407 0.59434 -0.15561 -0.03108 0.19514  66  PHE A O   
512  C CB  . PHE A 67  ? 0.66891 0.70715 0.57394 -0.12823 -0.02745 0.15506  66  PHE A CB  
513  C CG  . PHE A 67  ? 0.67211 0.70846 0.56036 -0.11910 -0.03019 0.14370  66  PHE A CG  
514  C CD1 . PHE A 67  ? 0.66792 0.71987 0.53967 -0.11062 -0.01633 0.12507  66  PHE A CD1 
515  C CD2 . PHE A 67  ? 0.66966 0.68758 0.56228 -0.11907 -0.04903 0.15181  66  PHE A CD2 
516  C CE1 . PHE A 67  ? 0.67176 0.72027 0.53179 -0.10287 -0.02198 0.11496  66  PHE A CE1 
517  C CE2 . PHE A 67  ? 0.65913 0.67509 0.54018 -0.11129 -0.05382 0.14208  66  PHE A CE2 
518  C CZ  . PHE A 67  ? 0.65909 0.68998 0.52388 -0.10349 -0.04068 0.12376  66  PHE A CZ  
519  N N   . LEU A 68  ? 0.62102 0.71641 0.52529 -0.15227 0.00442  0.18212  67  LEU A N   
520  C CA  . LEU A 68  ? 0.64751 0.74990 0.57745 -0.16135 0.00747  0.19219  67  LEU A CA  
521  C C   . LEU A 68  ? 0.63981 0.73166 0.58758 -0.14958 0.01090  0.16610  67  LEU A C   
522  O O   . LEU A 68  ? 0.59550 0.70273 0.53220 -0.14030 0.02613  0.14732  67  LEU A O   
523  C CB  . LEU A 68  ? 0.63052 0.77276 0.54747 -0.17040 0.02654  0.20660  67  LEU A CB  
524  C CG  . LEU A 68  ? 0.66791 0.82573 0.56062 -0.18234 0.02553  0.23449  67  LEU A CG  
525  C CD1 . LEU A 68  ? 0.67743 0.88095 0.55089 -0.18625 0.04989  0.24214  67  LEU A CD1 
526  C CD2 . LEU A 68  ? 0.71151 0.85247 0.62949 -0.19888 0.00564  0.26542  67  LEU A CD2 
527  N N   . VAL A 69  ? 0.65234 0.71714 0.62682 -0.14936 -0.00474 0.16454  68  VAL A N   
528  C CA  . VAL A 69  ? 0.64096 0.69348 0.62925 -0.13830 -0.00401 0.14124  68  VAL A CA  
529  C C   . VAL A 69  ? 0.65889 0.71260 0.67328 -0.14785 -0.00818 0.15045  68  VAL A C   
530  O O   . VAL A 69  ? 0.68188 0.72299 0.71585 -0.15902 -0.02425 0.16959  68  VAL A O   
531  C CB  . VAL A 69  ? 0.65240 0.67309 0.64798 -0.12680 -0.01866 0.12711  68  VAL A CB  
532  C CG1 . VAL A 69  ? 0.59486 0.60622 0.59847 -0.11492 -0.01614 0.10377  68  VAL A CG1 
533  C CG2 . VAL A 69  ? 0.61751 0.63835 0.59352 -0.11905 -0.01643 0.12133  68  VAL A CG2 
534  N N   . GLN A 70  ? 0.64236 0.71002 0.66030 -0.14389 0.00385  0.13762  69  GLN A N   
535  C CA  . GLN A 70  ? 0.67843 0.74937 0.72367 -0.15271 -0.00039 0.14534  69  GLN A CA  
536  C C   . GLN A 70  ? 0.66306 0.72054 0.71427 -0.14083 -0.00223 0.12061  69  GLN A C   
537  O O   . GLN A 70  ? 0.60456 0.67471 0.64162 -0.13123 0.01206  0.10410  69  GLN A O   
538  C CB  . GLN A 70  ? 0.66612 0.77681 0.71323 -0.16318 0.01741  0.16105  69  GLN A CB  
539  C CG  . GLN A 70  ? 0.74882 0.86591 0.83104 -0.17851 0.00978  0.18179  69  GLN A CG  
540  C CD  . GLN A 70  ? 0.77508 0.93577 0.85966 -0.19109 0.02798  0.20521  69  GLN A CD  
541  O OE1 . GLN A 70  ? 0.73017 0.92035 0.79595 -0.18430 0.04976  0.19561  69  GLN A OE1 
542  N NE2 . GLN A 70  ? 0.82372 0.98971 0.93254 -0.20915 0.01884  0.23642  69  GLN A NE2 
543  N N   . ALA A 71  ? 0.72269 0.75334 0.79412 -0.14123 -0.02163 0.11807  70  ALA A N   
544  C CA  . ALA A 71  ? 0.72355 0.74062 0.79959 -0.13145 -0.02641 0.09703  70  ALA A CA  
545  C C   . ALA A 71  ? 0.77768 0.80383 0.88231 -0.14346 -0.03185 0.10843  70  ALA A C   
546  O O   . ALA A 71  ? 0.79050 0.80036 0.91993 -0.15289 -0.05139 0.12087  70  ALA A O   
547  C CB  . ALA A 71  ? 0.66096 0.64166 0.73668 -0.12081 -0.04517 0.08245  70  ALA A CB  
548  N N   . GLY A 72  ? 0.72222 0.77405 0.82745 -0.14310 -0.01629 0.10443  71  GLY A N   
549  C CA  . GLY A 72  ? 0.79789 0.86598 0.93477 -0.15558 -0.01854 0.11837  71  GLY A CA  
550  C C   . GLY A 72  ? 0.86631 0.95782 1.01662 -0.17218 -0.01310 0.14850  71  GLY A C   
551  O O   . GLY A 72  ? 0.87126 0.99098 1.00337 -0.17287 0.00711  0.15512  71  GLY A O   
552  N N   . ASN A 73  ? 0.88587 0.96538 1.06769 -0.18580 -0.03255 0.16768  72  ASN A N   
553  C CA  . ASN A 73  ? 0.93566 1.03400 1.13254 -0.20369 -0.03125 0.20116  72  ASN A CA  
554  C C   . ASN A 73  ? 0.98167 1.04975 1.17309 -0.20623 -0.04993 0.20996  72  ASN A C   
555  O O   . ASN A 73  ? 1.00329 1.08348 1.20434 -0.22160 -0.05149 0.24002  72  ASN A O   
556  C CB  . ASN A 73  ? 0.98508 1.09498 1.22963 -0.22056 -0.04124 0.22314  72  ASN A CB  
557  C CG  . ASN A 73  ? 1.05969 1.21036 1.31568 -0.22099 -0.01931 0.22206  72  ASN A CG  
558  O OD1 . ASN A 73  ? 1.12140 1.26584 1.37421 -0.20888 -0.01838 0.19716  72  ASN A OD1 
559  N ND2 . ASN A 73  ? 1.00503 1.19916 1.27518 -0.23466 -0.00155 0.24977  72  ASN A ND2 
560  N N   . VAL A 74  ? 0.86845 0.89940 1.04554 -0.19132 -0.06384 0.18539  73  VAL A N   
561  C CA  . VAL A 74  ? 0.85268 0.85200 1.03081 -0.19137 -0.08452 0.19024  73  VAL A CA  
562  C C   . VAL A 74  ? 0.81132 0.82126 0.95580 -0.18647 -0.06956 0.19157  73  VAL A C   
563  O O   . VAL A 74  ? 0.77331 0.78848 0.88899 -0.17158 -0.05396 0.16916  73  VAL A O   
564  C CB  . VAL A 74  ? 0.86264 0.82030 1.04150 -0.17542 -0.10514 0.16139  73  VAL A CB  
565  C CG1 . VAL A 74  ? 0.86361 0.78698 1.06083 -0.17834 -0.13348 0.16946  73  VAL A CG1 
566  C CG2 . VAL A 74  ? 0.92052 0.87254 1.11887 -0.17496 -0.11386 0.15068  73  VAL A CG2 
567  N N   . GLN A 75  ? 0.79185 0.80417 0.94122 -0.19963 -0.07635 0.21911  74  GLN A N   
568  C CA  . GLN A 75  ? 0.76892 0.78767 0.88750 -0.19618 -0.06735 0.22249  74  GLN A CA  
569  C C   . GLN A 75  ? 0.76818 0.74773 0.88558 -0.18376 -0.08705 0.20664  74  GLN A C   
570  O O   . GLN A 75  ? 0.83430 0.78595 0.97843 -0.18910 -0.11290 0.21607  74  GLN A O   
571  C CB  . GLN A 75  ? 0.84709 0.88706 0.96863 -0.21613 -0.06655 0.26103  74  GLN A CB  
572  C CG  . GLN A 75  ? 0.83931 0.89551 0.92210 -0.21335 -0.05270 0.26504  74  GLN A CG  
573  C CD  . GLN A 75  ? 0.84483 0.93727 0.89869 -0.20583 -0.02250 0.25132  74  GLN A CD  
574  O OE1 . GLN A 75  ? 0.85353 0.96788 0.91954 -0.20781 -0.00957 0.24888  74  GLN A OE1 
575  N NE2 . GLN A 75  ? 0.84039 0.93822 0.85870 -0.19666 -0.01321 0.24151  74  GLN A NE2 
576  N N   . LEU A 76  ? 0.74879 0.72683 0.83897 -0.16690 -0.07572 0.18267  75  LEU A N   
577  C CA  . LEU A 76  ? 0.73672 0.68428 0.82672 -0.15402 -0.09062 0.16822  75  LEU A CA  
578  C C   . LEU A 76  ? 0.74673 0.69492 0.82813 -0.16068 -0.09606 0.18817  75  LEU A C   
579  O O   . LEU A 76  ? 0.74781 0.72312 0.80625 -0.16749 -0.08037 0.20127  75  LEU A O   
580  C CB  . LEU A 76  ? 0.69298 0.64074 0.76237 -0.13391 -0.07653 0.13663  75  LEU A CB  
581  C CG  . LEU A 76  ? 0.67801 0.61985 0.75187 -0.12428 -0.07418 0.11410  75  LEU A CG  
582  C CD1 . LEU A 76  ? 0.62293 0.56154 0.67845 -0.10470 -0.06399 0.08714  75  LEU A CD1 
583  C CD2 . LEU A 76  ? 0.67652 0.58892 0.77845 -0.12572 -0.09949 0.11310  75  LEU A CD2 
584  N N   . ARG A 77  ? 0.72496 0.64248 0.82472 -0.15785 -0.11990 0.18954  76  ARG A N   
585  C CA  . ARG A 77  ? 0.73215 0.64470 0.82727 -0.16292 -0.13003 0.20748  76  ARG A CA  
586  C C   . ARG A 77  ? 0.70494 0.61241 0.78399 -0.14421 -0.12394 0.18374  76  ARG A C   
587  O O   . ARG A 77  ? 0.67078 0.55915 0.76144 -0.12764 -0.12919 0.15858  76  ARG A O   
588  C CB  . ARG A 77  ? 0.76210 0.64339 0.89234 -0.17054 -0.16215 0.22357  76  ARG A CB  
589  C CG  . ARG A 77  ? 0.76498 0.63716 0.89527 -0.17679 -0.17774 0.24472  76  ARG A CG  
590  C CD  . ARG A 77  ? 0.80559 0.70583 0.91689 -0.19808 -0.16978 0.28126  76  ARG A CD  
591  N NE  . ARG A 77  ? 0.87929 0.79959 0.99932 -0.21378 -0.16169 0.29913  76  ARG A NE  
592  C CZ  . ARG A 77  ? 0.82261 0.78153 0.91649 -0.21944 -0.13413 0.30474  76  ARG A CZ  
593  N NH1 . ARG A 77  ? 0.83069 0.81021 0.88565 -0.21120 -0.11373 0.29385  76  ARG A NH1 
594  N NH2 . ARG A 77  ? 0.80948 0.78689 0.91946 -0.23314 -0.12813 0.32112  76  ARG A NH2 
595  N N   . VAL A 78  ? 0.69561 0.62162 0.74828 -0.14654 -0.11295 0.19168  77  VAL A N   
596  C CA  . VAL A 78  ? 0.67286 0.59688 0.71338 -0.13110 -0.10808 0.17292  77  VAL A CA  
597  C C   . VAL A 78  ? 0.66292 0.56403 0.71964 -0.13085 -0.13194 0.18327  77  VAL A C   
598  O O   . VAL A 78  ? 0.66084 0.56256 0.71378 -0.14573 -0.14342 0.21104  77  VAL A O   
599  C CB  . VAL A 78  ? 0.67216 0.62491 0.67782 -0.13263 -0.08780 0.17366  77  VAL A CB  
600  C CG1 . VAL A 78  ? 0.65011 0.59875 0.64897 -0.11916 -0.08782 0.15870  77  VAL A CG1 
601  C CG2 . VAL A 78  ? 0.65464 0.62839 0.64945 -0.13019 -0.06559 0.16007  77  VAL A CG2 
602  N N   . ILE A 79  ? 0.65616 0.53866 0.73145 -0.11363 -0.13930 0.16169  78  ILE A N   
603  C CA  . ILE A 79  ? 0.63865 0.49785 0.73711 -0.11031 -0.16335 0.16757  78  ILE A CA  
604  C C   . ILE A 79  ? 0.63778 0.50116 0.73285 -0.09590 -0.15820 0.15292  78  ILE A C   
605  O O   . ILE A 79  ? 0.64055 0.48591 0.76124 -0.08651 -0.17483 0.14831  78  ILE A O   
606  C CB  . ILE A 79  ? 0.62644 0.45694 0.76057 -0.10217 -0.18246 0.15640  78  ILE A CB  
607  C CG1 . ILE A 79  ? 0.64124 0.47243 0.77727 -0.08068 -0.16813 0.12132  78  ILE A CG1 
608  C CG2 . ILE A 79  ? 0.64946 0.47413 0.79267 -0.11877 -0.19204 0.17448  78  ILE A CG2 
609  C CD1 . ILE A 79  ? 0.63126 0.43497 0.79635 -0.06994 -0.18604 0.10532  78  ILE A CD1 
610  N N   . GLY A 80  ? 0.64163 0.52872 0.70920 -0.09405 -0.13674 0.14590  79  GLY A N   
611  C CA  . GLY A 80  ? 0.60361 0.49669 0.67032 -0.08234 -0.13227 0.13415  79  GLY A CA  
612  C C   . GLY A 80  ? 0.59524 0.51226 0.63707 -0.07877 -0.10774 0.12124  79  GLY A C   
613  O O   . GLY A 80  ? 0.58132 0.50811 0.61258 -0.07996 -0.09291 0.11423  79  GLY A O   
614  N N   . HIS A 81  ? 0.57356 0.49888 0.60907 -0.07427 -0.10579 0.11814  80  HIS A N   
615  C CA  . HIS A 81  ? 0.57043 0.51614 0.58581 -0.07093 -0.08628 0.10635  80  HIS A CA  
616  C C   . HIS A 81  ? 0.57798 0.52648 0.60465 -0.06137 -0.08873 0.09872  80  HIS A C   
617  O O   . HIS A 81  ? 0.57063 0.50963 0.60669 -0.06279 -0.10624 0.10858  80  HIS A O   
618  C CB  . HIS A 81  ? 0.56630 0.52631 0.54654 -0.08409 -0.08080 0.11841  80  HIS A CB  
619  C CG  . HIS A 81  ? 0.60789 0.56558 0.57327 -0.09152 -0.09585 0.13446  80  HIS A CG  
620  N ND1 . HIS A 81  ? 0.62907 0.57616 0.59305 -0.10323 -0.11248 0.15722  80  HIS A ND1 
621  C CD2 . HIS A 81  ? 0.61415 0.57753 0.56514 -0.08918 -0.09906 0.13169  80  HIS A CD2 
622  C CE1 . HIS A 81  ? 0.64243 0.58966 0.58827 -0.10763 -0.12436 0.16806  80  HIS A CE1 
623  N NE2 . HIS A 81  ? 0.63618 0.59252 0.57361 -0.09880 -0.11706 0.15166  80  HIS A NE2 
624  N N   . SER A 82  ? 0.52739 0.48906 0.55567 -0.05251 -0.07257 0.08290  81  SER A N   
625  C CA  . SER A 82  ? 0.53889 0.50679 0.58123 -0.04481 -0.07355 0.07710  81  SER A CA  
626  C C   . SER A 82  ? 0.52671 0.51123 0.55366 -0.04386 -0.05803 0.06756  81  SER A C   
627  O O   . SER A 82  ? 0.51168 0.50304 0.52133 -0.04654 -0.04501 0.06294  81  SER A O   
628  C CB  . SER A 82  ? 0.50497 0.47028 0.58460 -0.03091 -0.07282 0.06809  81  SER A CB  
629  O OG  . SER A 82  ? 0.58620 0.55960 0.66724 -0.02318 -0.05463 0.05469  81  SER A OG  
630  N N   . MET A 83  ? 0.49877 0.48898 0.53598 -0.04014 -0.06166 0.06506  82  MET A N   
631  C CA  . MET A 83  ? 0.48628 0.48963 0.51572 -0.03880 -0.05151 0.05640  82  MET A CA  
632  C C   . MET A 83  ? 0.48560 0.49716 0.54955 -0.02905 -0.04607 0.05091  82  MET A C   
633  O O   . MET A 83  ? 0.50287 0.51257 0.59222 -0.02584 -0.05741 0.05525  82  MET A O   
634  C CB  . MET A 83  ? 0.50306 0.50599 0.51096 -0.04472 -0.06361 0.05923  82  MET A CB  
635  C CG  . MET A 83  ? 0.49580 0.50903 0.49965 -0.04242 -0.05766 0.04869  82  MET A CG  
636  S SD  . MET A 83  ? 0.54408 0.55525 0.51448 -0.04718 -0.07262 0.04687  82  MET A SD  
637  C CE  . MET A 83  ? 0.51249 0.51120 0.50390 -0.04693 -0.09771 0.05623  82  MET A CE  
638  N N   . GLN A 84  ? 0.45471 0.47688 0.52089 -0.02473 -0.02899 0.04306  83  GLN A N   
639  C CA  . GLN A 84  ? 0.45366 0.48876 0.54932 -0.01673 -0.02047 0.04043  83  GLN A CA  
640  C C   . GLN A 84  ? 0.44345 0.48740 0.53221 -0.01990 -0.01636 0.03733  83  GLN A C   
641  O O   . GLN A 84  ? 0.45232 0.49909 0.52147 -0.02167 -0.00595 0.03189  83  GLN A O   
642  C CB  . GLN A 84  ? 0.47479 0.51496 0.57774 -0.00830 -0.00515 0.03491  83  GLN A CB  
643  C CG  . GLN A 84  ? 0.47245 0.53113 0.60191 -0.00007 0.00736  0.03426  83  GLN A CG  
644  C CD  . GLN A 84  ? 0.50449 0.56889 0.63269 0.00964  0.02293  0.02692  83  GLN A CD  
645  O OE1 . GLN A 84  ? 0.52688 0.57899 0.63459 0.00963  0.02286  0.02090  83  GLN A OE1 
646  N NE2 . GLN A 84  ? 0.49172 0.57570 0.64203 0.01803  0.03575  0.02789  83  GLN A NE2 
647  N N   . ASN A 85  ? 0.40303 0.45006 0.51109 -0.02055 -0.02691 0.04068  84  ASN A N   
648  C CA  . ASN A 85  ? 0.42209 0.47364 0.52797 -0.02350 -0.02891 0.03730  84  ASN A CA  
649  C C   . ASN A 85  ? 0.44138 0.48633 0.50746 -0.02851 -0.02973 0.02979  84  ASN A C   
650  O O   . ASN A 85  ? 0.47803 0.51391 0.52210 -0.03224 -0.04005 0.03058  84  ASN A O   
651  C CB  . ASN A 85  ? 0.41656 0.48300 0.54179 -0.01984 -0.01338 0.03803  84  ASN A CB  
652  C CG  . ASN A 85  ? 0.42661 0.50574 0.59216 -0.01417 -0.00953 0.04665  84  ASN A CG  
653  O OD1 . ASN A 85  ? 0.39997 0.47939 0.59206 -0.01483 -0.02308 0.05271  84  ASN A OD1 
654  N ND2 . ASN A 85  ? 0.44531 0.53625 0.61579 -0.00793 0.00876  0.04687  84  ASN A ND2 
655  N N   . CYS A 86  ? 0.42704 0.47818 0.48411 -0.02853 -0.01870 0.02350  85  CYS A N   
656  C CA  . CYS A 86  ? 0.44420 0.49343 0.46904 -0.03181 -0.01786 0.01533  85  CYS A CA  
657  C C   . CYS A 86  ? 0.43840 0.48814 0.44291 -0.03369 -0.00535 0.01531  85  CYS A C   
658  O O   . CYS A 86  ? 0.43887 0.49247 0.42379 -0.03569 0.00035  0.00910  85  CYS A O   
659  C CB  . CYS A 86  ? 0.42704 0.48166 0.45779 -0.03056 -0.01646 0.00765  85  CYS A CB  
660  S SG  . CYS A 86  ? 0.48761 0.53815 0.54114 -0.02974 -0.03681 0.00601  85  CYS A SG  
661  N N   . VAL A 87  ? 0.43957 0.48545 0.45112 -0.03267 -0.00241 0.02155  86  VAL A N   
662  C CA  . VAL A 87  ? 0.45698 0.50087 0.45518 -0.03441 0.00635  0.02169  86  VAL A CA  
663  C C   . VAL A 87  ? 0.47963 0.51319 0.47336 -0.03768 -0.00244 0.02984  86  VAL A C   
664  O O   . VAL A 87  ? 0.47587 0.50399 0.48780 -0.03441 -0.01043 0.03427  86  VAL A O   
665  C CB  . VAL A 87  ? 0.46686 0.51420 0.47897 -0.02836 0.01780  0.01892  86  VAL A CB  
666  C CG1 . VAL A 87  ? 0.47296 0.51223 0.47854 -0.02840 0.01998  0.01946  86  VAL A CG1 
667  C CG2 . VAL A 87  ? 0.44783 0.50366 0.45583 -0.02828 0.02636  0.01303  86  VAL A CG2 
668  N N   . LEU A 88  ? 0.46033 0.49227 0.43322 -0.04448 -0.00164 0.03326  87  LEU A N   
669  C CA  . LEU A 88  ? 0.47468 0.49611 0.44530 -0.04933 -0.01016 0.04375  87  LEU A CA  
670  C C   . LEU A 88  ? 0.51051 0.52499 0.49384 -0.04609 -0.00598 0.04184  87  LEU A C   
671  O O   . LEU A 88  ? 0.48038 0.49982 0.46020 -0.04497 0.00452  0.03510  87  LEU A O   
672  C CB  . LEU A 88  ? 0.50896 0.53497 0.45306 -0.05939 -0.01089 0.05147  87  LEU A CB  
673  C CG  . LEU A 88  ? 0.57086 0.59385 0.49942 -0.06523 -0.02409 0.06242  87  LEU A CG  
674  C CD1 . LEU A 88  ? 0.54299 0.56731 0.47110 -0.06008 -0.03086 0.05529  87  LEU A CD1 
675  C CD2 . LEU A 88  ? 0.60010 0.63468 0.50006 -0.07432 -0.01891 0.06981  87  LEU A CD2 
676  N N   . LYS A 89  ? 0.51076 0.51245 0.50933 -0.04386 -0.01632 0.04677  88  LYS A N   
677  C CA  . LYS A 89  ? 0.51243 0.50344 0.52292 -0.03954 -0.01704 0.04329  88  LYS A CA  
678  C C   . LYS A 89  ? 0.53044 0.50757 0.54052 -0.04854 -0.03175 0.05662  88  LYS A C   
679  O O   . LYS A 89  ? 0.54437 0.51297 0.56371 -0.04946 -0.04532 0.06507  88  LYS A O   
680  C CB  . LYS A 89  ? 0.49208 0.48095 0.52662 -0.02583 -0.01641 0.03468  88  LYS A CB  
681  C CG  . LYS A 89  ? 0.49859 0.50360 0.53621 -0.01842 -0.00184 0.02597  88  LYS A CG  
682  C CD  . LYS A 89  ? 0.52047 0.52838 0.58038 -0.00416 0.00311  0.01795  88  LYS A CD  
683  C CE  . LYS A 89  ? 0.52363 0.52879 0.60834 -0.00010 -0.00761 0.02296  88  LYS A CE  
684  N NZ  . LYS A 89  ? 0.53801 0.55179 0.64714 0.01547  0.00039  0.01443  88  LYS A NZ  
685  N N   . LEU A 90  ? 0.52024 0.49549 0.52219 -0.05605 -0.03045 0.06036  89  LEU A N   
686  C CA  . LEU A 90  ? 0.54083 0.50423 0.54544 -0.06686 -0.04451 0.07634  89  LEU A CA  
687  C C   . LEU A 90  ? 0.55934 0.50386 0.58497 -0.06085 -0.05357 0.06970  89  LEU A C   
688  O O   . LEU A 90  ? 0.55043 0.49548 0.57533 -0.05709 -0.04629 0.05859  89  LEU A O   
689  C CB  . LEU A 90  ? 0.54123 0.51808 0.52714 -0.08030 -0.03759 0.08727  89  LEU A CB  
690  C CG  . LEU A 90  ? 0.54434 0.54269 0.50676 -0.08198 -0.02438 0.08526  89  LEU A CG  
691  C CD1 . LEU A 90  ? 0.53576 0.55075 0.48568 -0.09089 -0.01328 0.09005  89  LEU A CD1 
692  C CD2 . LEU A 90  ? 0.58172 0.58086 0.53173 -0.08640 -0.03351 0.09690  89  LEU A CD2 
693  N N   . LYS A 91  ? 0.54614 0.47277 0.59072 -0.05907 -0.07129 0.07524  90  LYS A N   
694  C CA  . LYS A 91  ? 0.58746 0.49287 0.65341 -0.05286 -0.08417 0.06803  90  LYS A CA  
695  C C   . LYS A 91  ? 0.63014 0.52673 0.69796 -0.06875 -0.09577 0.08497  90  LYS A C   
696  O O   . LYS A 91  ? 0.60853 0.50624 0.67311 -0.08329 -0.10441 0.10791  90  LYS A O   
697  C CB  . LYS A 91  ? 0.59259 0.48174 0.68346 -0.04366 -0.10056 0.06650  90  LYS A CB  
698  C CG  . LYS A 91  ? 0.62191 0.49110 0.73507 -0.02955 -0.11076 0.04903  90  LYS A CG  
699  C CD  . LYS A 91  ? 0.64898 0.49849 0.79208 -0.02334 -0.13266 0.05129  90  LYS A CD  
700  C CE  . LYS A 91  ? 0.69339 0.52668 0.85729 -0.00339 -0.13937 0.02650  90  LYS A CE  
701  N NZ  . LYS A 91  ? 0.74382 0.55086 0.94148 0.00037  -0.16737 0.02949  90  LYS A NZ  
702  N N   . VAL A 92  ? 0.63018 0.51917 0.70327 -0.06651 -0.09650 0.07504  91  VAL A N   
703  C CA  . VAL A 92  ? 0.64411 0.52396 0.72683 -0.08140 -0.10947 0.09093  91  VAL A CA  
704  C C   . VAL A 92  ? 0.66683 0.51518 0.77797 -0.07415 -0.13380 0.08309  91  VAL A C   
705  O O   . VAL A 92  ? 0.67352 0.51071 0.79257 -0.05542 -0.13623 0.06128  91  VAL A O   
706  C CB  . VAL A 92  ? 0.65268 0.54748 0.72342 -0.08655 -0.09529 0.08747  91  VAL A CB  
707  C CG1 . VAL A 92  ? 0.62213 0.54712 0.66828 -0.09404 -0.07418 0.09598  91  VAL A CG1 
708  C CG2 . VAL A 92  ? 0.64539 0.53485 0.71329 -0.06911 -0.08878 0.05920  91  VAL A CG2 
709  N N   . ASP A 93  ? 0.67386 0.50883 0.80246 -0.08885 -0.15241 0.10128  92  ASP A N   
710  C CA  . ASP A 93  ? 0.72691 0.52828 0.88643 -0.08331 -0.18062 0.09511  92  ASP A CA  
711  C C   . ASP A 93  ? 0.73089 0.51933 0.89433 -0.07267 -0.18416 0.07099  92  ASP A C   
712  O O   . ASP A 93  ? 0.76830 0.52674 0.95568 -0.06423 -0.20850 0.05931  92  ASP A O   
713  C CB  . ASP A 93  ? 0.73623 0.52626 0.91798 -0.10516 -0.20354 0.12833  92  ASP A CB  
714  C CG  . ASP A 93  ? 0.78648 0.59240 0.96541 -0.12437 -0.19732 0.14725  92  ASP A CG  
715  O OD1 . ASP A 93  ? 0.80277 0.63098 0.95956 -0.12160 -0.17367 0.13608  92  ASP A OD1 
716  O OD2 . ASP A 93  ? 0.80737 0.60431 1.00962 -0.14259 -0.21683 0.17466  92  ASP A OD2 
717  N N   . THR A 94  ? 0.70489 0.51351 0.84573 -0.07214 -0.16282 0.06237  93  THR A N   
718  C CA  . THR A 94  ? 0.69369 0.49081 0.83509 -0.06449 -0.16766 0.04242  93  THR A CA  
719  C C   . THR A 94  ? 0.67650 0.48888 0.78983 -0.04668 -0.14406 0.01674  93  THR A C   
720  O O   . THR A 94  ? 0.63596 0.47598 0.72879 -0.05053 -0.12031 0.02240  93  THR A O   
721  C CB  . THR A 94  ? 0.70604 0.51211 0.85317 -0.08460 -0.16899 0.06153  93  THR A CB  
722  O OG1 . THR A 94  ? 0.74819 0.54038 0.92507 -0.10212 -0.19241 0.08819  93  THR A OG1 
723  C CG2 . THR A 94  ? 0.71116 0.50481 0.85787 -0.07645 -0.17560 0.04009  93  THR A CG2 
724  N N   . ALA A 95  ? 0.68993 0.48446 0.80231 -0.02692 -0.15151 -0.01119 94  ALA A N   
725  C CA  . ALA A 95  ? 0.64079 0.44958 0.72580 -0.01105 -0.13085 -0.03361 94  ALA A CA  
726  C C   . ALA A 95  ? 0.63329 0.44826 0.70652 -0.01963 -0.12720 -0.03289 94  ALA A C   
727  O O   . ALA A 95  ? 0.63960 0.43502 0.72783 -0.02629 -0.14824 -0.03162 94  ALA A O   
728  C CB  . ALA A 95  ? 0.64212 0.43222 0.72677 0.01390  -0.13946 -0.06378 94  ALA A CB  
729  N N   . ASN A 96  ? 0.62277 0.46411 0.67316 -0.01988 -0.10271 -0.03290 95  ASN A N   
730  C CA  . ASN A 96  ? 0.62188 0.47098 0.66243 -0.02678 -0.09855 -0.03285 95  ASN A CA  
731  C C   . ASN A 96  ? 0.62593 0.45311 0.65919 -0.01285 -0.11294 -0.05683 95  ASN A C   
732  O O   . ASN A 96  ? 0.61986 0.44678 0.63357 0.00648  -0.10531 -0.07771 95  ASN A O   
733  C CB  . ASN A 96  ? 0.60555 0.48427 0.62421 -0.02618 -0.07160 -0.03157 95  ASN A CB  
734  C CG  . ASN A 96  ? 0.60935 0.49723 0.62082 -0.03311 -0.06769 -0.03088 95  ASN A CG  
735  O OD1 . ASN A 96  ? 0.60155 0.47548 0.62514 -0.03952 -0.08447 -0.03009 95  ASN A OD1 
736  N ND2 . ASN A 96  ? 0.59049 0.50141 0.58593 -0.03216 -0.04736 -0.03054 95  ASN A ND2 
737  N N   . PRO A 97  ? 0.64953 0.45908 0.69777 -0.02162 -0.13410 -0.05454 96  PRO A N   
738  C CA  . PRO A 97  ? 0.64958 0.43552 0.68801 -0.00752 -0.15114 -0.07955 96  PRO A CA  
739  C C   . PRO A 97  ? 0.66709 0.46797 0.67286 0.00109  -0.13468 -0.09233 96  PRO A C   
740  O O   . PRO A 97  ? 0.67758 0.46276 0.66401 0.01738  -0.14391 -0.11616 96  PRO A O   
741  C CB  . PRO A 97  ? 0.66618 0.43358 0.73417 -0.02387 -0.17784 -0.06782 96  PRO A CB  
742  C CG  . PRO A 97  ? 0.67962 0.45779 0.77516 -0.04391 -0.17643 -0.03715 96  PRO A CG  
743  C CD  . PRO A 97  ? 0.63362 0.44464 0.70968 -0.04463 -0.14453 -0.02844 96  PRO A CD  
744  N N   . LYS A 98  ? 0.65232 0.48246 0.65064 -0.00881 -0.11194 -0.07748 97  LYS A N   
745  C CA  . LYS A 98  ? 0.65300 0.49781 0.62456 -0.00329 -0.09783 -0.08526 97  LYS A CA  
746  C C   . LYS A 98  ? 0.64595 0.51195 0.59587 0.00804  -0.07262 -0.08911 97  LYS A C   
747  O O   . LYS A 98  ? 0.63651 0.52080 0.56971 0.00793  -0.05756 -0.08735 97  LYS A O   
748  C CB  . LYS A 98  ? 0.65821 0.52025 0.64128 -0.02153 -0.09264 -0.06720 97  LYS A CB  
749  C CG  . LYS A 98  ? 0.68254 0.52915 0.69245 -0.03467 -0.11603 -0.05981 97  LYS A CG  
750  C CD  . LYS A 98  ? 0.71367 0.58471 0.73888 -0.05170 -0.10605 -0.04075 97  LYS A CD  
751  C CE  . LYS A 98  ? 0.85123 0.71041 0.90077 -0.06217 -0.12822 -0.03658 97  LYS A CE  
752  N NZ  . LYS A 98  ? 0.89790 0.78335 0.95757 -0.07314 -0.11631 -0.02464 97  LYS A NZ  
753  N N   . THR A 99  ? 0.65366 0.51779 0.60767 0.01713  -0.06919 -0.09286 98  THR A N   
754  C CA  . THR A 99  ? 0.63444 0.51987 0.57427 0.02754  -0.04644 -0.09501 98  THR A CA  
755  C C   . THR A 99  ? 0.66903 0.55700 0.57851 0.04462  -0.04010 -0.11346 98  THR A C   
756  O O   . THR A 99  ? 0.65143 0.52037 0.55162 0.05942  -0.05296 -0.13347 98  THR A O   
757  C CB  . THR A 99  ? 0.63272 0.51410 0.58764 0.03519  -0.04719 -0.09670 98  THR A CB  
758  O OG1 . THR A 99  ? 0.62927 0.50695 0.60911 0.01857  -0.05536 -0.07776 98  THR A OG1 
759  C CG2 . THR A 99  ? 0.60933 0.51599 0.55638 0.04373  -0.02370 -0.09548 98  THR A CG2 
760  N N   . PRO A 100 ? 0.64771 0.55812 0.54060 0.04358  -0.02197 -0.10760 99  PRO A N   
761  C CA  . PRO A 100 ? 0.65594 0.57195 0.51726 0.05864  -0.01481 -0.12124 99  PRO A CA  
762  C C   . PRO A 100 ? 0.68384 0.61702 0.53934 0.07438  0.00325  -0.12654 99  PRO A C   
763  O O   . PRO A 100 ? 0.63673 0.57812 0.51444 0.07229  0.01015  -0.11837 99  PRO A O   
764  C CB  . PRO A 100 ? 0.65727 0.59060 0.51103 0.04705  -0.00496 -0.10712 99  PRO A CB  
765  C CG  . PRO A 100 ? 0.62630 0.57442 0.50533 0.03360  0.00495  -0.08872 99  PRO A CG  
766  C CD  . PRO A 100 ? 0.62782 0.55946 0.53012 0.02855  -0.00842 -0.08778 99  PRO A CD  
767  N N   . LYS A 101 ? 0.69485 0.63481 0.52013 0.09041  0.01060  -0.13978 100 LYS A N   
768  C CA  . LYS A 101 ? 0.70485 0.67151 0.52438 0.10332  0.03349  -0.13945 100 LYS A CA  
769  C C   . LYS A 101 ? 0.66719 0.65893 0.49968 0.08877  0.04997  -0.11506 100 LYS A C   
770  O O   . LYS A 101 ? 0.66954 0.66639 0.49123 0.07850  0.05097  -0.10492 100 LYS A O   
771  C CB  . LYS A 101 ? 0.77530 0.74923 0.55511 0.12134  0.04025  -0.15468 100 LYS A CB  
772  C CG  . LYS A 101 ? 0.80984 0.81388 0.58512 0.13787  0.06467  -0.15643 100 LYS A CG  
773  C CD  . LYS A 101 ? 0.85741 0.85665 0.60383 0.16391  0.06349  -0.18482 100 LYS A CD  
774  C CE  . LYS A 101 ? 0.91629 0.92683 0.61509 0.17125  0.07063  -0.18825 100 LYS A CE  
775  N NZ  . LYS A 101 ? 0.93038 0.93651 0.59567 0.19881  0.06919  -0.21899 100 LYS A NZ  
776  N N   . TYR A 102 ? 0.62960 0.63493 0.48783 0.08777  0.06005  -0.10607 101 TYR A N   
777  C CA  . TYR A 102 ? 0.60430 0.62797 0.47914 0.07313  0.07024  -0.08451 101 TYR A CA  
778  C C   . TYR A 102 ? 0.58443 0.63345 0.47504 0.08042  0.08785  -0.07758 101 TYR A C   
779  O O   . TYR A 102 ? 0.57688 0.62757 0.47512 0.09463  0.09069  -0.08827 101 TYR A O   
780  C CB  . TYR A 102 ? 0.58331 0.59330 0.48069 0.05648  0.05783  -0.07551 101 TYR A CB  
781  C CG  . TYR A 102 ? 0.58646 0.58928 0.50762 0.05842  0.05255  -0.07648 101 TYR A CG  
782  C CD1 . TYR A 102 ? 0.58422 0.56291 0.50896 0.06322  0.03608  -0.08879 101 TYR A CD1 
783  C CD2 . TYR A 102 ? 0.56907 0.58742 0.51133 0.05482  0.06107  -0.06426 101 TYR A CD2 
784  C CE1 . TYR A 102 ? 0.58539 0.55607 0.53380 0.06429  0.02882  -0.08783 101 TYR A CE1 
785  C CE2 . TYR A 102 ? 0.54581 0.55659 0.50991 0.05616  0.05398  -0.06398 101 TYR A CE2 
786  C CZ  . TYR A 102 ? 0.57074 0.55790 0.53771 0.06077  0.03812  -0.07519 101 TYR A CZ  
787  O OH  . TYR A 102 ? 0.55513 0.53344 0.54565 0.06155  0.02882  -0.07323 101 TYR A OH  
788  N N   . LYS A 103 ? 0.58735 0.65617 0.48652 0.07054  0.09825  -0.05944 102 LYS A N   
789  C CA  . LYS A 103 ? 0.54851 0.64191 0.47111 0.07249  0.11231  -0.04761 102 LYS A CA  
790  C C   . LYS A 103 ? 0.51736 0.61133 0.46277 0.05535  0.10750  -0.03159 102 LYS A C   
791  O O   . LYS A 103 ? 0.50294 0.58554 0.44187 0.04331  0.09855  -0.02845 102 LYS A O   
792  C CB  . LYS A 103 ? 0.57260 0.69439 0.48351 0.07918  0.13064  -0.03961 102 LYS A CB  
793  C CG  . LYS A 103 ? 0.63061 0.76196 0.51995 0.09986  0.14119  -0.05481 102 LYS A CG  
794  C CD  . LYS A 103 ? 0.66750 0.82864 0.54008 0.10268  0.15921  -0.04198 102 LYS A CD  
795  C CE  . LYS A 103 ? 0.74866 0.93287 0.60766 0.12473  0.17712  -0.05273 102 LYS A CE  
796  N NZ  . LYS A 103 ? 0.78333 1.00353 0.63215 0.12491  0.19742  -0.03324 102 LYS A NZ  
797  N N   . PHE A 104 ? 0.49153 0.59952 0.46470 0.05538  0.11290  -0.02261 103 PHE A N   
798  C CA  . PHE A 104 ? 0.47851 0.59165 0.47274 0.04170  0.10963  -0.00748 103 PHE A CA  
799  C C   . PHE A 104 ? 0.47483 0.61559 0.48190 0.04240  0.12325  0.00728  103 PHE A C   
800  O O   . PHE A 104 ? 0.44449 0.60433 0.46709 0.05213  0.13452  0.00993  103 PHE A O   
801  C CB  . PHE A 104 ? 0.46149 0.56732 0.47968 0.03933  0.10099  -0.00660 103 PHE A CB  
802  C CG  . PHE A 104 ? 0.45735 0.53777 0.46632 0.03359  0.08606  -0.01425 103 PHE A CG  
803  C CD1 . PHE A 104 ? 0.46649 0.53378 0.45285 0.02866  0.08091  -0.01974 103 PHE A CD1 
804  C CD2 . PHE A 104 ? 0.43148 0.50241 0.45679 0.03224  0.07636  -0.01365 103 PHE A CD2 
805  C CE1 . PHE A 104 ? 0.46175 0.50938 0.44398 0.02210  0.06804  -0.02339 103 PHE A CE1 
806  C CE2 . PHE A 104 ? 0.46357 0.51359 0.48125 0.02544  0.06292  -0.01664 103 PHE A CE2 
807  C CZ  . PHE A 104 ? 0.47155 0.51113 0.46869 0.02010  0.05956  -0.02092 103 PHE A CZ  
808  N N   . VAL A 105 ? 0.45306 0.59710 0.45683 0.03216  0.12181  0.01774  104 VAL A N   
809  C CA  . VAL A 105 ? 0.45540 0.62428 0.47259 0.03013  0.13209  0.03540  104 VAL A CA  
810  C C   . VAL A 105 ? 0.44918 0.61540 0.49033 0.01626  0.12121  0.04728  104 VAL A C   
811  O O   . VAL A 105 ? 0.43379 0.58146 0.46643 0.00855  0.10897  0.04142  104 VAL A O   
812  C CB  . VAL A 105 ? 0.47531 0.65083 0.46336 0.03247  0.13917  0.03771  104 VAL A CB  
813  C CG1 . VAL A 105 ? 0.47224 0.67529 0.47640 0.02856  0.14939  0.06061  104 VAL A CG1 
814  C CG2 . VAL A 105 ? 0.50812 0.68376 0.46804 0.04818  0.14764  0.02194  104 VAL A CG2 
815  N N   . ARG A 106 ? 0.42193 0.60748 0.49503 0.01377  0.12508  0.06330  105 ARG A N   
816  C CA  . ARG A 106 ? 0.44517 0.62908 0.54353 0.00166  0.11309  0.07515  105 ARG A CA  
817  C C   . ARG A 106 ? 0.44893 0.64848 0.55004 -0.00309 0.11818  0.09263  105 ARG A C   
818  O O   . ARG A 106 ? 0.42953 0.65514 0.54647 -0.00070 0.13102  0.10888  105 ARG A O   
819  C CB  . ARG A 106 ? 0.43257 0.62491 0.56940 0.00032  0.10915  0.08310  105 ARG A CB  
820  C CG  . ARG A 106 ? 0.41889 0.60464 0.58156 -0.01111 0.09220  0.09147  105 ARG A CG  
821  C CD  . ARG A 106 ? 0.40455 0.59561 0.60455 -0.01223 0.08485  0.09784  105 ARG A CD  
822  N NE  . ARG A 106 ? 0.41323 0.59546 0.63738 -0.02211 0.06552  0.10358  105 ARG A NE  
823  C CZ  . ARG A 106 ? 0.37054 0.52958 0.58388 -0.02526 0.04853  0.08950  105 ARG A CZ  
824  N NH1 . ARG A 106 ? 0.36834 0.51233 0.54925 -0.02138 0.04906  0.07242  105 ARG A NH1 
825  N NH2 . ARG A 106 ? 0.35876 0.51029 0.59483 -0.03220 0.03009  0.09287  105 ARG A NH2 
826  N N   . ILE A 107 ? 0.44671 0.63205 0.53413 -0.00986 0.10817  0.09060  106 ILE A N   
827  C CA  . ILE A 107 ? 0.46564 0.66231 0.55307 -0.01501 0.11006  0.10770  106 ILE A CA  
828  C C   . ILE A 107 ? 0.46967 0.67547 0.60028 -0.02491 0.10105  0.12783  106 ILE A C   
829  O O   . ILE A 107 ? 0.46053 0.65648 0.61594 -0.02857 0.08828  0.12370  106 ILE A O   
830  C CB  . ILE A 107 ? 0.47539 0.65280 0.53745 -0.01833 0.10019  0.09828  106 ILE A CB  
831  C CG1 . ILE A 107 ? 0.44499 0.60188 0.52052 -0.02430 0.08261  0.08701  106 ILE A CG1 
832  C CG2 . ILE A 107 ? 0.46591 0.63547 0.48820 -0.00925 0.10750  0.08143  106 ILE A CG2 
833  C CD1 . ILE A 107 ? 0.45647 0.59986 0.52197 -0.02882 0.07157  0.08239  106 ILE A CD1 
834  N N   . GLN A 108 ? 0.47869 0.70296 0.61791 -0.02958 0.10611  0.15065  107 GLN A N   
835  C CA  . GLN A 108 ? 0.49104 0.72403 0.67374 -0.04071 0.09545  0.17410  107 GLN A CA  
836  C C   . GLN A 108 ? 0.46294 0.67410 0.64883 -0.04908 0.07442  0.17235  107 GLN A C   
837  O O   . GLN A 108 ? 0.45794 0.65584 0.61098 -0.04684 0.07309  0.16024  107 GLN A O   
838  C CB  . GLN A 108 ? 0.48551 0.75219 0.67688 -0.04245 0.11204  0.20324  107 GLN A CB  
839  C CG  . GLN A 108 ? 0.54762 0.84183 0.74508 -0.03311 0.13390  0.20661  107 GLN A CG  
840  C CD  . GLN A 108 ? 0.55302 0.85619 0.80461 -0.03813 0.12703  0.21774  107 GLN A CD  
841  O OE1 . GLN A 108 ? 0.56837 0.86060 0.82635 -0.03272 0.12316  0.20014  107 GLN A OE1 
842  N NE2 . GLN A 108 ? 0.55543 0.87822 0.84799 -0.04924 0.12366  0.24867  107 GLN A NE2 
843  N N   . PRO A 109 ? 0.45749 0.66372 0.68555 -0.05816 0.05588  0.18321  108 PRO A N   
844  C CA  . PRO A 109 ? 0.44574 0.63180 0.68174 -0.06463 0.03448  0.18095  108 PRO A CA  
845  C C   . PRO A 109 ? 0.44673 0.64215 0.67210 -0.06954 0.03766  0.20128  108 PRO A C   
846  O O   . PRO A 109 ? 0.45300 0.67426 0.68402 -0.07264 0.05098  0.22750  108 PRO A O   
847  C CB  . PRO A 109 ? 0.42323 0.60519 0.71149 -0.07245 0.01391  0.19120  108 PRO A CB  
848  C CG  . PRO A 109 ? 0.43144 0.64006 0.74327 -0.07373 0.02743  0.21174  108 PRO A CG  
849  C CD  . PRO A 109 ? 0.44977 0.66671 0.72324 -0.06224 0.05084  0.19625  108 PRO A CD  
850  N N   . GLY A 110 ? 0.43353 0.60933 0.64371 -0.07009 0.02530  0.18976  109 GLY A N   
851  C CA  . GLY A 110 ? 0.44765 0.62753 0.64146 -0.07399 0.02544  0.20546  109 GLY A CA  
852  C C   . GLY A 110 ? 0.45841 0.63873 0.59925 -0.06542 0.04117  0.19188  109 GLY A C   
853  O O   . GLY A 110 ? 0.48363 0.65970 0.60556 -0.06754 0.03640  0.19762  109 GLY A O   
854  N N   . GLN A 111 ? 0.45517 0.63874 0.57357 -0.05591 0.05705  0.17413  110 GLN A N   
855  C CA  . GLN A 111 ? 0.49131 0.67151 0.56237 -0.04706 0.06853  0.15824  110 GLN A CA  
856  C C   . GLN A 111 ? 0.46985 0.62427 0.53037 -0.04520 0.05588  0.13243  110 GLN A C   
857  O O   . GLN A 111 ? 0.44548 0.58756 0.52981 -0.04732 0.04398  0.12143  110 GLN A O   
858  C CB  . GLN A 111 ? 0.49237 0.68551 0.54821 -0.03716 0.08848  0.14986  110 GLN A CB  
859  C CG  . GLN A 111 ? 0.53407 0.75866 0.59413 -0.03611 0.10612  0.17391  110 GLN A CG  
860  C CD  . GLN A 111 ? 0.62442 0.86044 0.65545 -0.03708 0.11141  0.19025  110 GLN A CD  
861  O OE1 . GLN A 111 ? 0.65709 0.89341 0.64450 -0.02740 0.12135  0.17826  110 GLN A OE1 
862  N NE2 . GLN A 111 ? 0.65504 0.89926 0.71016 -0.04889 0.10261  0.21810  110 GLN A NE2 
863  N N   . THR A 112 ? 0.50928 0.61501 0.47651 0.00326  0.06147  0.00472  111 THR A N   
864  C CA  . THR A 112 ? 0.50377 0.59680 0.46416 -0.00171 0.05494  -0.00535 111 THR A CA  
865  C C   . THR A 112 ? 0.48375 0.56244 0.42339 0.00206  0.05826  -0.01360 111 THR A C   
866  O O   . THR A 112 ? 0.50598 0.58130 0.43222 0.00970  0.06539  -0.01323 111 THR A O   
867  C CB  . THR A 112 ? 0.51614 0.60690 0.47140 -0.00694 0.04986  -0.00416 111 THR A CB  
868  O OG1 . THR A 112 ? 0.52815 0.61628 0.46247 -0.00296 0.05531  -0.00106 111 THR A OG1 
869  C CG2 . THR A 112 ? 0.49626 0.59826 0.47506 -0.01155 0.04371  0.00347  111 THR A CG2 
870  N N   . PHE A 113 ? 0.48738 0.55807 0.42556 -0.00294 0.05272  -0.02041 112 PHE A N   
871  C CA  . PHE A 113 ? 0.48253 0.53839 0.40401 -0.00208 0.05279  -0.02674 112 PHE A CA  
872  C C   . PHE A 113 ? 0.45715 0.51039 0.38187 -0.01010 0.04580  -0.03018 112 PHE A C   
873  O O   . PHE A 113 ? 0.47619 0.54021 0.41728 -0.01372 0.04264  -0.02921 112 PHE A O   
874  C CB  . PHE A 113 ? 0.48008 0.53586 0.40480 0.00313  0.05678  -0.02731 112 PHE A CB  
875  C CG  . PHE A 113 ? 0.46430 0.53089 0.40842 0.00022  0.05408  -0.02658 112 PHE A CG  
876  C CD1 . PHE A 113 ? 0.46352 0.52737 0.40786 -0.00410 0.05041  -0.03053 112 PHE A CD1 
877  C CD2 . PHE A 113 ? 0.46761 0.54709 0.42894 0.00183  0.05454  -0.02135 112 PHE A CD2 
878  C CE1 . PHE A 113 ? 0.45375 0.52674 0.41125 -0.00515 0.04815  -0.03112 112 PHE A CE1 
879  C CE2 . PHE A 113 ? 0.48674 0.57246 0.46243 -0.00031 0.04997  -0.02229 112 PHE A CE2 
880  C CZ  . PHE A 113 ? 0.44898 0.53102 0.42077 -0.00300 0.04722  -0.02813 112 PHE A CZ  
881  N N   . SER A 114 ? 0.46787 0.50691 0.37792 -0.01238 0.04300  -0.03366 113 SER A N   
882  C CA  . SER A 114 ? 0.45566 0.49478 0.37039 -0.02050 0.03678  -0.03433 113 SER A CA  
883  C C   . SER A 114 ? 0.49056 0.53256 0.41134 -0.02097 0.03808  -0.03473 113 SER A C   
884  O O   . SER A 114 ? 0.49402 0.52624 0.40584 -0.01718 0.04015  -0.03562 113 SER A O   
885  C CB  . SER A 114 ? 0.48155 0.50340 0.37860 -0.02508 0.03015  -0.03564 113 SER A CB  
886  O OG  . SER A 114 ? 0.52293 0.54248 0.41209 -0.02517 0.02794  -0.03496 113 SER A OG  
887  N N   . VAL A 115 ? 0.46089 0.51674 0.39622 -0.02465 0.03700  -0.03384 114 VAL A N   
888  C CA  . VAL A 115 ? 0.44071 0.50232 0.38025 -0.02568 0.03828  -0.03317 114 VAL A CA  
889  C C   . VAL A 115 ? 0.45292 0.51369 0.39164 -0.03375 0.03387  -0.02966 114 VAL A C   
890  O O   . VAL A 115 ? 0.42923 0.49670 0.37510 -0.03813 0.03065  -0.02801 114 VAL A O   
891  C CB  . VAL A 115 ? 0.44867 0.52717 0.40254 -0.02269 0.04050  -0.03486 114 VAL A CB  
892  C CG1 . VAL A 115 ? 0.43896 0.52633 0.39456 -0.02435 0.04185  -0.03363 114 VAL A CG1 
893  C CG2 . VAL A 115 ? 0.43338 0.51163 0.38971 -0.01650 0.04259  -0.03632 114 VAL A CG2 
894  N N   . LEU A 116 ? 0.44905 0.50216 0.38110 -0.03625 0.03276  -0.02700 115 LEU A N   
895  C CA  . LEU A 116 ? 0.44789 0.50263 0.38253 -0.04537 0.02792  -0.02059 115 LEU A CA  
896  C C   . LEU A 116 ? 0.46881 0.54282 0.41267 -0.04533 0.03279  -0.01679 115 LEU A C   
897  O O   . LEU A 116 ? 0.46899 0.53889 0.40748 -0.04450 0.03382  -0.01473 115 LEU A O   
898  C CB  . LEU A 116 ? 0.47122 0.50147 0.39144 -0.04905 0.02111  -0.01902 115 LEU A CB  
899  C CG  . LEU A 116 ? 0.50801 0.53715 0.43217 -0.06043 0.01351  -0.00989 115 LEU A CG  
900  C CD1 . LEU A 116 ? 0.48802 0.52632 0.42212 -0.06830 0.00822  -0.00583 115 LEU A CD1 
901  C CD2 . LEU A 116 ? 0.52475 0.52385 0.43320 -0.06260 0.00480  -0.00997 115 LEU A CD2 
902  N N   . ALA A 117 ? 0.44445 0.53979 0.40135 -0.04516 0.03583  -0.01599 116 ALA A N   
903  C CA  . ALA A 117 ? 0.45650 0.57226 0.41938 -0.04325 0.04154  -0.01331 116 ALA A CA  
904  C C   . ALA A 117 ? 0.47392 0.59550 0.43892 -0.05242 0.03954  -0.00172 116 ALA A C   
905  O O   . ALA A 117 ? 0.48139 0.60636 0.45461 -0.06038 0.03492  0.00508  116 ALA A O   
906  C CB  . ALA A 117 ? 0.44710 0.58313 0.42261 -0.03822 0.04552  -0.01673 116 ALA A CB  
907  N N   . CYS A 118 ? 0.44189 0.56540 0.40070 -0.05203 0.04197  0.00193  117 CYS A N   
908  C CA  . CYS A 118 ? 0.47934 0.60661 0.43933 -0.06132 0.03930  0.01502  117 CYS A CA  
909  C C   . CYS A 118 ? 0.48934 0.64179 0.45036 -0.05829 0.04744  0.01992  117 CYS A C   
910  O O   . CYS A 118 ? 0.45058 0.60840 0.40546 -0.04851 0.05298  0.01122  117 CYS A O   
911  C CB  . CYS A 118 ? 0.49212 0.59182 0.44029 -0.06443 0.03218  0.01657  117 CYS A CB  
912  S SG  . CYS A 118 ? 0.53052 0.59743 0.47067 -0.06615 0.02256  0.01018  117 CYS A SG  
913  N N   . TYR A 119 ? 0.51547 0.68322 0.48367 -0.06718 0.04725  0.03484  118 TYR A N   
914  C CA  . TYR A 119 ? 0.49259 0.68569 0.45937 -0.06545 0.05519  0.04281  118 TYR A CA  
915  C C   . TYR A 119 ? 0.51176 0.70429 0.48132 -0.07857 0.04942  0.06125  118 TYR A C   
916  O O   . TYR A 119 ? 0.51147 0.70231 0.49339 -0.08974 0.04236  0.07166  118 TYR A O   
917  C CB  . TYR A 119 ? 0.47328 0.70011 0.45138 -0.06001 0.06508  0.04376  118 TYR A CB  
918  C CG  . TYR A 119 ? 0.49225 0.71769 0.46819 -0.04680 0.06905  0.02579  118 TYR A CG  
919  C CD1 . TYR A 119 ? 0.46122 0.69166 0.42441 -0.03481 0.07501  0.01534  118 TYR A CD1 
920  C CD2 . TYR A 119 ? 0.47546 0.69245 0.46150 -0.04698 0.06493  0.01977  118 TYR A CD2 
921  C CE1 . TYR A 119 ? 0.44354 0.66960 0.40593 -0.02375 0.07599  -0.00038 118 TYR A CE1 
922  C CE2 . TYR A 119 ? 0.47387 0.68842 0.45954 -0.03594 0.06701  0.00514  118 TYR A CE2 
923  C CZ  . TYR A 119 ? 0.46771 0.68618 0.44243 -0.02456 0.07213  -0.00482 118 TYR A CZ  
924  O OH  . TYR A 119 ? 0.47721 0.69060 0.45286 -0.01451 0.07173  -0.01868 118 TYR A OH  
925  N N   . ASN A 120 ? 0.49984 0.69233 0.45832 -0.07791 0.05064  0.06597  119 ASN A N   
926  C CA  . ASN A 120 ? 0.52446 0.71394 0.48484 -0.09037 0.04385  0.08452  119 ASN A CA  
927  C C   . ASN A 120 ? 0.54744 0.70084 0.50909 -0.09902 0.02914  0.08523  119 ASN A C   
928  O O   . ASN A 120 ? 0.58207 0.73179 0.55293 -0.11246 0.02000  0.10105  119 ASN A O   
929  C CB  . ASN A 120 ? 0.53424 0.75894 0.50974 -0.09875 0.04871  0.10392  119 ASN A CB  
930  C CG  . ASN A 120 ? 0.54833 0.80889 0.51832 -0.08831 0.06409  0.10364  119 ASN A CG  
931  O OD1 . ASN A 120 ? 0.51646 0.78168 0.47227 -0.08544 0.06723  0.10682  119 ASN A OD1 
932  N ND2 . ASN A 120 ? 0.52696 0.81232 0.50702 -0.08171 0.07322  0.09949  119 ASN A ND2 
933  N N   . GLY A 121 ? 0.52627 0.65270 0.47827 -0.09095 0.02632  0.06830  120 GLY A N   
934  C CA  . GLY A 121 ? 0.54026 0.63040 0.48812 -0.09530 0.01356  0.06592  120 GLY A CA  
935  C C   . GLY A 121 ? 0.56623 0.64773 0.52200 -0.10306 0.00560  0.06673  120 GLY A C   
936  O O   . GLY A 121 ? 0.58964 0.63885 0.53933 -0.10713 -0.00676 0.06494  120 GLY A O   
937  N N   . SER A 122 ? 0.54475 0.65309 0.51329 -0.10461 0.01139  0.06911  121 SER A N   
938  C CA  . SER A 122 ? 0.55968 0.66110 0.53671 -0.11209 0.00283  0.07013  121 SER A CA  
939  C C   . SER A 122 ? 0.56261 0.67137 0.53997 -0.10211 0.01003  0.05561  121 SER A C   
940  O O   . SER A 122 ? 0.51896 0.65227 0.49939 -0.09290 0.02253  0.05108  121 SER A O   
941  C CB  . SER A 122 ? 0.56477 0.69281 0.56284 -0.12568 0.00022  0.09064  121 SER A CB  
942  O OG  . SER A 122 ? 0.58124 0.75030 0.59011 -0.11948 0.01547  0.09357  121 SER A OG  
943  N N   . PRO A 123 ? 0.59436 0.68093 0.56729 -0.10344 0.00146  0.04810  122 PRO A N   
944  C CA  . PRO A 123 ? 0.52841 0.61924 0.50054 -0.09410 0.00723  0.03508  122 PRO A CA  
945  C C   . PRO A 123 ? 0.50586 0.63045 0.49808 -0.09505 0.01309  0.04073  122 PRO A C   
946  O O   . PRO A 123 ? 0.53352 0.67339 0.54161 -0.10573 0.00868  0.05508  122 PRO A O   
947  C CB  . PRO A 123 ? 0.55723 0.61608 0.51806 -0.09748 -0.00521 0.02909  122 PRO A CB  
948  C CG  . PRO A 123 ? 0.63308 0.66409 0.58274 -0.10342 -0.01574 0.03318  122 PRO A CG  
949  C CD  . PRO A 123 ? 0.59157 0.64409 0.55624 -0.11237 -0.01488 0.04989  122 PRO A CD  
950  N N   . SER A 124 ? 0.50237 0.63872 0.49541 -0.08340 0.02252  0.02989  123 SER A N   
951  C CA  . SER A 124 ? 0.49434 0.66050 0.50552 -0.08031 0.02876  0.03196  123 SER A CA  
952  C C   . SER A 124 ? 0.50015 0.65941 0.51353 -0.07627 0.02586  0.02277  123 SER A C   
953  O O   . SER A 124 ? 0.45089 0.62769 0.48174 -0.07871 0.02463  0.02810  123 SER A O   
954  C CB  . SER A 124 ? 0.50102 0.69018 0.51253 -0.06872 0.04222  0.02782  123 SER A CB  
955  O OG  . SER A 124 ? 0.52615 0.73628 0.55085 -0.06074 0.04810  0.02353  123 SER A OG  
956  N N   . GLY A 125 ? 0.45644 0.59289 0.45421 -0.07015 0.02485  0.01074  124 GLY A N   
957  C CA  . GLY A 125 ? 0.45254 0.58293 0.45187 -0.06741 0.02151  0.00430  124 GLY A CA  
958  C C   . GLY A 125 ? 0.47331 0.57904 0.45403 -0.06189 0.02072  -0.00583 124 GLY A C   
959  O O   . GLY A 125 ? 0.48667 0.58268 0.45587 -0.05816 0.02406  -0.00907 124 GLY A O   
960  N N   . VAL A 126 ? 0.44537 0.54278 0.42409 -0.06130 0.01630  -0.00947 125 VAL A N   
961  C CA  . VAL A 126 ? 0.46014 0.53838 0.42248 -0.05568 0.01657  -0.01710 125 VAL A CA  
962  C C   . VAL A 126 ? 0.43928 0.52629 0.41032 -0.05011 0.01852  -0.02059 125 VAL A C   
963  O O   . VAL A 126 ? 0.42977 0.52650 0.41324 -0.05322 0.01442  -0.01731 125 VAL A O   
964  C CB  . VAL A 126 ? 0.49416 0.54714 0.43804 -0.06101 0.00738  -0.01721 125 VAL A CB  
965  C CG1 . VAL A 126 ? 0.47181 0.50723 0.39655 -0.05280 0.01120  -0.02432 125 VAL A CG1 
966  C CG2 . VAL A 126 ? 0.51911 0.56382 0.46070 -0.07025 0.00019  -0.01098 125 VAL A CG2 
967  N N   . TYR A 127 ? 0.44294 0.52662 0.40940 -0.04235 0.02364  -0.02592 126 TYR A N   
968  C CA  . TYR A 127 ? 0.44401 0.53349 0.41928 -0.03812 0.02364  -0.02771 126 TYR A CA  
969  C C   . TYR A 127 ? 0.45154 0.53194 0.41739 -0.03259 0.02694  -0.03030 126 TYR A C   
970  O O   . TYR A 127 ? 0.41114 0.48562 0.36837 -0.02973 0.03095  -0.03197 126 TYR A O   
971  C CB  . TYR A 127 ? 0.45901 0.56683 0.45308 -0.03353 0.02642  -0.02956 126 TYR A CB  
972  C CG  . TYR A 127 ? 0.46359 0.57622 0.45630 -0.02870 0.03238  -0.03306 126 TYR A CG  
973  C CD1 . TYR A 127 ? 0.46012 0.56838 0.45046 -0.02293 0.03433  -0.03721 126 TYR A CD1 
974  C CD2 . TYR A 127 ? 0.45367 0.57635 0.44793 -0.03058 0.03528  -0.03066 126 TYR A CD2 
975  C CE1 . TYR A 127 ? 0.47762 0.58923 0.46535 -0.01904 0.03797  -0.04019 126 TYR A CE1 
976  C CE2 . TYR A 127 ? 0.46504 0.59225 0.45542 -0.02629 0.04025  -0.03321 126 TYR A CE2 
977  C CZ  . TYR A 127 ? 0.45246 0.57303 0.43868 -0.02044 0.04106  -0.03864 126 TYR A CZ  
978  O OH  . TYR A 127 ? 0.45188 0.57599 0.43301 -0.01664 0.04425  -0.04099 126 TYR A OH  
979  N N   . GLN A 128 ? 0.45323 0.53463 0.42313 -0.03117 0.02505  -0.02902 127 GLN A N   
980  C CA  . GLN A 128 ? 0.46773 0.54444 0.43130 -0.02677 0.02825  -0.02820 127 GLN A CA  
981  C C   . GLN A 128 ? 0.48625 0.57236 0.46599 -0.02236 0.02970  -0.02894 127 GLN A C   
982  O O   . GLN A 128 ? 0.51484 0.60861 0.51003 -0.02223 0.02588  -0.02973 127 GLN A O   
983  C CB  . GLN A 128 ? 0.50004 0.57309 0.45744 -0.02872 0.02479  -0.02392 127 GLN A CB  
984  C CG  . GLN A 128 ? 0.51022 0.58015 0.45708 -0.02400 0.02985  -0.02099 127 GLN A CG  
985  C CD  . GLN A 128 ? 0.51274 0.56860 0.43503 -0.02114 0.03351  -0.02399 127 GLN A CD  
986  O OE1 . GLN A 128 ? 0.46999 0.51599 0.38365 -0.02395 0.03070  -0.02806 127 GLN A OE1 
987  N NE2 . GLN A 128 ? 0.53389 0.58898 0.44545 -0.01505 0.03951  -0.02135 127 GLN A NE2 
988  N N   . CYS A 129 ? 0.47018 0.55468 0.44679 -0.01836 0.03404  -0.02869 128 CYS A N   
989  C CA  . CYS A 129 ? 0.48544 0.57632 0.47631 -0.01518 0.03321  -0.02877 128 CYS A CA  
990  C C   . CYS A 129 ? 0.48175 0.57374 0.47371 -0.01307 0.03563  -0.02210 128 CYS A C   
991  O O   . CYS A 129 ? 0.48524 0.57319 0.46336 -0.01148 0.04074  -0.01936 128 CYS A O   
992  C CB  . CYS A 129 ? 0.45853 0.55004 0.44817 -0.01283 0.03517  -0.03354 128 CYS A CB  
993  S SG  . CYS A 129 ? 0.55974 0.65730 0.55291 -0.01334 0.03366  -0.03968 128 CYS A SG  
994  N N   . ALA A 130 ? 0.46037 0.55810 0.46920 -0.01256 0.03150  -0.01917 129 ALA A N   
995  C CA  . ALA A 130 ? 0.48597 0.58927 0.50194 -0.01125 0.03328  -0.01023 129 ALA A CA  
996  C C   . ALA A 130 ? 0.47535 0.58064 0.50129 -0.00945 0.03089  -0.01127 129 ALA A C   
997  O O   . ALA A 130 ? 0.45215 0.55461 0.48327 -0.00970 0.02468  -0.01831 129 ALA A O   
998  C CB  . ALA A 130 ? 0.45877 0.56743 0.48938 -0.01464 0.02749  -0.00169 129 ALA A CB  
999  N N   . MET A 131 ? 0.44460 0.55522 0.47233 -0.00682 0.03580  -0.00423 130 MET A N   
1000 C CA  . MET A 131 ? 0.46182 0.57578 0.50200 -0.00607 0.03176  -0.00234 130 MET A CA  
1001 C C   . MET A 131 ? 0.45908 0.57850 0.52178 -0.01029 0.02196  0.00557  130 MET A C   
1002 O O   . MET A 131 ? 0.48332 0.61316 0.55684 -0.01139 0.02408  0.01844  130 MET A O   
1003 C CB  . MET A 131 ? 0.46577 0.58525 0.50301 -0.00117 0.04030  0.00375  130 MET A CB  
1004 C CG  . MET A 131 ? 0.48182 0.60589 0.53333 -0.00084 0.03528  0.00736  130 MET A CG  
1005 S SD  . MET A 131 ? 0.49516 0.60796 0.53698 -0.00139 0.02883  -0.00562 130 MET A SD  
1006 C CE  . MET A 131 ? 0.45076 0.55536 0.46777 0.00208  0.03943  -0.01234 130 MET A CE  
1007 N N   . ARG A 132 ? 0.45402 0.56620 0.52348 -0.01228 0.01079  -0.00177 131 ARG A N   
1008 C CA  . ARG A 132 ? 0.45791 0.57000 0.54845 -0.01665 -0.00195 0.00421  131 ARG A CA  
1009 C C   . ARG A 132 ? 0.46556 0.58689 0.57399 -0.01905 -0.00544 0.01735  131 ARG A C   
1010 O O   . ARG A 132 ? 0.44101 0.56654 0.54540 -0.01616 -0.00004 0.01815  131 ARG A O   
1011 C CB  . ARG A 132 ? 0.48061 0.58000 0.57134 -0.01569 -0.01376 -0.00892 131 ARG A CB  
1012 C CG  . ARG A 132 ? 0.51157 0.60563 0.58705 -0.01203 -0.00947 -0.02159 131 ARG A CG  
1013 C CD  . ARG A 132 ? 0.50827 0.60384 0.58837 -0.01422 -0.00909 -0.01728 131 ARG A CD  
1014 N NE  . ARG A 132 ? 0.52677 0.61853 0.62709 -0.01761 -0.02246 -0.01150 131 ARG A NE  
1015 C CZ  . ARG A 132 ? 0.51196 0.60567 0.62107 -0.02101 -0.02493 -0.00352 131 ARG A CZ  
1016 N NH1 . ARG A 132 ? 0.47993 0.57906 0.57788 -0.02129 -0.01528 -0.00127 131 ARG A NH1 
1017 N NH2 . ARG A 132 ? 0.51190 0.60071 0.64122 -0.02480 -0.03899 0.00296  131 ARG A NH2 
1018 N N   . PRO A 133 ? 0.46098 0.58667 0.59161 -0.02479 -0.01510 0.02954  132 PRO A N   
1019 C CA  . PRO A 133 ? 0.46893 0.60514 0.62173 -0.02858 -0.02101 0.04411  132 PRO A CA  
1020 C C   . PRO A 133 ? 0.46321 0.59049 0.61719 -0.02831 -0.03140 0.03637  132 PRO A C   
1021 O O   . PRO A 133 ? 0.43734 0.57520 0.60508 -0.02976 -0.03266 0.04726  132 PRO A O   
1022 C CB  . PRO A 133 ? 0.52513 0.66237 0.70151 -0.03647 -0.03414 0.05647  132 PRO A CB  
1023 C CG  . PRO A 133 ? 0.51179 0.64870 0.67662 -0.03535 -0.02645 0.05488  132 PRO A CG  
1024 C CD  . PRO A 133 ? 0.47910 0.60392 0.61702 -0.02861 -0.01936 0.03457  132 PRO A CD  
1025 N N   . ASN A 134 ? 0.45246 0.56199 0.59222 -0.02594 -0.03878 0.01852  133 ASN A N   
1026 C CA  . ASN A 134 ? 0.45688 0.55709 0.59122 -0.02462 -0.04795 0.00960  133 ASN A CA  
1027 C C   . ASN A 134 ? 0.43954 0.54131 0.55073 -0.01837 -0.03450 0.00089  133 ASN A C   
1028 O O   . ASN A 134 ? 0.47444 0.56737 0.57412 -0.01623 -0.04043 -0.00924 133 ASN A O   
1029 C CB  . ASN A 134 ? 0.46940 0.54958 0.59943 -0.02397 -0.06405 -0.00497 133 ASN A CB  
1030 C CG  . ASN A 134 ? 0.50674 0.58037 0.61461 -0.01709 -0.05534 -0.02110 133 ASN A CG  
1031 O OD1 . ASN A 134 ? 0.47087 0.55354 0.56844 -0.01489 -0.03928 -0.02027 133 ASN A OD1 
1032 N ND2 . ASN A 134 ? 0.52503 0.58277 0.62592 -0.01321 -0.06672 -0.03567 133 ASN A ND2 
1033 N N   . PHE A 135 ? 0.44096 0.55235 0.54382 -0.01546 -0.01765 0.00469  134 PHE A N   
1034 C CA  . PHE A 135 ? 0.44331 0.55564 0.52731 -0.01041 -0.00577 -0.00041 134 PHE A CA  
1035 C C   . PHE A 135 ? 0.43936 0.54066 0.50201 -0.00765 -0.00554 -0.01643 134 PHE A C   
1036 O O   . PHE A 135 ? 0.45433 0.55390 0.50388 -0.00517 -0.00235 -0.02080 134 PHE A O   
1037 C CB  . PHE A 135 ? 0.42791 0.54601 0.51989 -0.01000 -0.00815 0.00680  134 PHE A CB  
1038 C CG  . PHE A 135 ? 0.43779 0.57243 0.54962 -0.01023 -0.00283 0.02411  134 PHE A CG  
1039 C CD1 . PHE A 135 ? 0.42194 0.56443 0.56051 -0.01593 -0.01447 0.03689  134 PHE A CD1 
1040 C CD2 . PHE A 135 ? 0.44785 0.59047 0.55164 -0.00428 0.01348  0.02805  134 PHE A CD2 
1041 C CE1 . PHE A 135 ? 0.43692 0.59954 0.59600 -0.01571 -0.00801 0.05520  134 PHE A CE1 
1042 C CE2 . PHE A 135 ? 0.49990 0.66035 0.62050 -0.00207 0.02045  0.04384  134 PHE A CE2 
1043 C CZ  . PHE A 135 ? 0.44805 0.62087 0.59744 -0.00780 0.01068  0.05841  134 PHE A CZ  
1044 N N   . THR A 136 ? 0.45836 0.55389 0.51853 -0.00776 -0.00858 -0.02391 135 THR A N   
1045 C CA  . THR A 136 ? 0.44984 0.54035 0.49193 -0.00420 -0.00486 -0.03678 135 THR A CA  
1046 C C   . THR A 136 ? 0.47594 0.56962 0.51380 -0.00445 0.00460  -0.03603 135 THR A C   
1047 O O   . THR A 136 ? 0.47967 0.57757 0.52575 -0.00686 0.00744  -0.02699 135 THR A O   
1048 C CB  . THR A 136 ? 0.47915 0.56045 0.52154 -0.00195 -0.01697 -0.04757 135 THR A CB  
1049 O OG1 . THR A 136 ? 0.46126 0.53964 0.51887 -0.00394 -0.02372 -0.04509 135 THR A OG1 
1050 C CG2 . THR A 136 ? 0.45393 0.52923 0.49896 -0.00253 -0.02933 -0.04838 135 THR A CG2 
1051 N N   . ILE A 137 ? 0.46778 0.56069 0.49240 -0.00210 0.00933  -0.04455 136 ILE A N   
1052 C CA  . ILE A 137 ? 0.46424 0.55944 0.48626 -0.00313 0.01522  -0.04430 136 ILE A CA  
1053 C C   . ILE A 137 ? 0.48004 0.57546 0.50059 0.00023  0.01289  -0.05384 136 ILE A C   
1054 O O   . ILE A 137 ? 0.45076 0.54607 0.46392 0.00435  0.01171  -0.06153 136 ILE A O   
1055 C CB  . ILE A 137 ? 0.45734 0.55388 0.46582 -0.00437 0.02534  -0.04148 136 ILE A CB  
1056 C CG1 . ILE A 137 ? 0.45372 0.55131 0.44995 -0.00290 0.02843  -0.04697 136 ILE A CG1 
1057 C CG2 . ILE A 137 ? 0.47133 0.56766 0.48004 -0.00459 0.02883  -0.03341 136 ILE A CG2 
1058 C CD1 . ILE A 137 ? 0.43034 0.52645 0.41494 -0.00533 0.03551  -0.04371 136 ILE A CD1 
1059 N N   . LYS A 138 ? 0.47129 0.56807 0.49869 -0.00071 0.01239  -0.05289 137 LYS A N   
1060 C CA  . LYS A 138 ? 0.49741 0.59709 0.52665 0.00365  0.01141  -0.06055 137 LYS A CA  
1061 C C   . LYS A 138 ? 0.48001 0.58768 0.50086 0.00161  0.02055  -0.05872 137 LYS A C   
1062 O O   . LYS A 138 ? 0.49915 0.60840 0.52351 -0.00228 0.02153  -0.05367 137 LYS A O   
1063 C CB  . LYS A 138 ? 0.52299 0.61940 0.56781 0.00357  0.00355  -0.05914 137 LYS A CB  
1064 C CG  . LYS A 138 ? 0.52555 0.61234 0.58126 0.00458  -0.00843 -0.06015 137 LYS A CG  
1065 C CD  . LYS A 138 ? 0.62069 0.70353 0.69330 0.00304  -0.01712 -0.05600 137 LYS A CD  
1066 C CE  . LYS A 138 ? 0.65494 0.72522 0.73922 0.00515  -0.03212 -0.05960 137 LYS A CE  
1067 N NZ  . LYS A 138 ? 0.62327 0.69108 0.72421 -0.00282 -0.04025 -0.04574 137 LYS A NZ  
1068 N N   . GLY A 139 ? 0.47825 0.59077 0.48794 0.00344  0.02598  -0.06176 138 GLY A N   
1069 C CA  . GLY A 139 ? 0.48565 0.60529 0.48869 -0.00018 0.03305  -0.05783 138 GLY A CA  
1070 C C   . GLY A 139 ? 0.48850 0.62157 0.49292 0.00441  0.03678  -0.06172 138 GLY A C   
1071 O O   . GLY A 139 ? 0.50690 0.64315 0.51819 0.01184  0.03419  -0.06871 138 GLY A O   
1072 N N   . SER A 140 ? 0.48224 0.62367 0.48073 0.00042  0.04276  -0.05648 139 SER A N   
1073 C CA  . SER A 140 ? 0.48317 0.64275 0.48381 0.00405  0.04847  -0.05660 139 SER A CA  
1074 C C   . SER A 140 ? 0.47329 0.63762 0.46154 0.00057  0.05353  -0.05151 139 SER A C   
1075 O O   . SER A 140 ? 0.45276 0.61717 0.44029 -0.00818 0.05444  -0.04243 139 SER A O   
1076 C CB  . SER A 140 ? 0.48203 0.65116 0.49584 -0.00011 0.04880  -0.05038 139 SER A CB  
1077 O OG  . SER A 140 ? 0.50726 0.69834 0.52622 0.00329  0.05549  -0.04784 139 SER A OG  
1078 N N   . PHE A 141 ? 0.46424 0.63068 0.44203 0.00707  0.05518  -0.05712 140 PHE A N   
1079 C CA  . PHE A 141 ? 0.47232 0.64150 0.43716 0.00390  0.05853  -0.05183 140 PHE A CA  
1080 C C   . PHE A 141 ? 0.46670 0.65389 0.42366 0.01219  0.06475  -0.05507 140 PHE A C   
1081 O O   . PHE A 141 ? 0.46078 0.64674 0.41337 0.02258  0.06308  -0.06649 140 PHE A O   
1082 C CB  . PHE A 141 ? 0.45198 0.60356 0.40813 0.00295  0.05310  -0.05396 140 PHE A CB  
1083 C CG  . PHE A 141 ? 0.45477 0.59132 0.41547 -0.00378 0.04949  -0.04939 140 PHE A CG  
1084 C CD1 . PHE A 141 ? 0.44434 0.57754 0.40255 -0.01151 0.05088  -0.04068 140 PHE A CD1 
1085 C CD2 . PHE A 141 ? 0.45793 0.58344 0.42454 -0.00190 0.04429  -0.05345 140 PHE A CD2 
1086 C CE1 . PHE A 141 ? 0.43712 0.55521 0.39552 -0.01523 0.04800  -0.03836 140 PHE A CE1 
1087 C CE2 . PHE A 141 ? 0.44559 0.56017 0.41428 -0.00631 0.04285  -0.04890 140 PHE A CE2 
1088 C CZ  . PHE A 141 ? 0.43996 0.55030 0.40290 -0.01196 0.04515  -0.04248 140 PHE A CZ  
1089 N N   . LEU A 142 ? 0.46657 0.66991 0.42087 0.00784  0.07130  -0.04472 141 LEU A N   
1090 C CA  . LEU A 142 ? 0.46730 0.69119 0.41122 0.01531  0.07912  -0.04488 141 LEU A CA  
1091 C C   . LEU A 142 ? 0.47424 0.69489 0.40208 0.01045  0.07872  -0.03842 141 LEU A C   
1092 O O   . LEU A 142 ? 0.46609 0.66791 0.39255 0.00271  0.07223  -0.03509 141 LEU A O   
1093 C CB  . LEU A 142 ? 0.44998 0.70139 0.40671 0.01427  0.08786  -0.03478 141 LEU A CB  
1094 C CG  . LEU A 142 ? 0.48178 0.74087 0.45703 0.01961  0.08869  -0.03907 141 LEU A CG  
1095 C CD1 . LEU A 142 ? 0.51145 0.79878 0.50310 0.01487  0.09594  -0.02427 141 LEU A CD1 
1096 C CD2 . LEU A 142 ? 0.46957 0.73096 0.43880 0.03697  0.09059  -0.05531 141 LEU A CD2 
1097 N N   . ASN A 143 ? 0.48858 0.72875 0.40385 0.01600  0.08602  -0.03621 142 ASN A N   
1098 C CA  . ASN A 143 ? 0.49780 0.73766 0.39782 0.01089  0.08556  -0.02776 142 ASN A CA  
1099 C C   . ASN A 143 ? 0.46857 0.70872 0.37910 -0.00399 0.08468  -0.01007 142 ASN A C   
1100 O O   . ASN A 143 ? 0.41978 0.67476 0.34538 -0.00914 0.08877  -0.00067 142 ASN A O   
1101 C CB  . ASN A 143 ? 0.50777 0.77206 0.39090 0.02001  0.09471  -0.02726 142 ASN A CB  
1102 C CG  . ASN A 143 ? 0.61164 0.86397 0.47200 0.03100  0.08988  -0.04258 142 ASN A CG  
1103 O OD1 . ASN A 143 ? 0.71704 0.97367 0.56986 0.04488  0.09226  -0.05669 142 ASN A OD1 
1104 N ND2 . ASN A 143 ? 0.60030 0.83617 0.44987 0.02513  0.08170  -0.03997 142 ASN A ND2 
1105 N N   . GLY A 144 ? 0.47238 0.69487 0.37583 -0.01078 0.07792  -0.00540 143 GLY A N   
1106 C CA  . GLY A 144 ? 0.47155 0.68676 0.38314 -0.02394 0.07416  0.00919  143 GLY A CA  
1107 C C   . GLY A 144 ? 0.44798 0.64010 0.37087 -0.02864 0.06724  0.00568  143 GLY A C   
1108 O O   . GLY A 144 ? 0.45136 0.63233 0.37880 -0.03851 0.06235  0.01555  143 GLY A O   
1109 N N   . SER A 145 ? 0.42468 0.60844 0.35113 -0.02168 0.06599  -0.00780 144 SER A N   
1110 C CA  . SER A 145 ? 0.45916 0.62310 0.39391 -0.02513 0.06045  -0.01081 144 SER A CA  
1111 C C   . SER A 145 ? 0.44673 0.58844 0.37525 -0.02463 0.05471  -0.01361 144 SER A C   
1112 O O   . SER A 145 ? 0.42146 0.54683 0.35394 -0.02687 0.05108  -0.01474 144 SER A O   
1113 C CB  . SER A 145 ? 0.44517 0.61144 0.38829 -0.01865 0.06129  -0.02145 144 SER A CB  
1114 O OG  . SER A 145 ? 0.42980 0.59126 0.36708 -0.00982 0.05972  -0.03248 144 SER A OG  
1115 N N   . CYS A 146 ? 0.40892 0.55063 0.32761 -0.02112 0.05383  -0.01438 145 CYS A N   
1116 C CA  . CYS A 146 ? 0.42517 0.54889 0.34140 -0.02010 0.04840  -0.01543 145 CYS A CA  
1117 C C   . CYS A 146 ? 0.42874 0.53838 0.34573 -0.02683 0.04545  -0.00647 145 CYS A C   
1118 O O   . CYS A 146 ? 0.43677 0.55099 0.35308 -0.03383 0.04569  0.00310  145 CYS A O   
1119 C CB  . CYS A 146 ? 0.43700 0.56447 0.34277 -0.01641 0.04636  -0.01587 145 CYS A CB  
1120 S SG  . CYS A 146 ? 0.47830 0.61214 0.38064 -0.00697 0.04530  -0.02970 145 CYS A SG  
1121 N N   . GLY A 147 ? 0.43537 0.52770 0.35433 -0.02423 0.04221  -0.00919 146 GLY A N   
1122 C CA  . GLY A 147 ? 0.45278 0.52729 0.37105 -0.02770 0.03894  -0.00439 146 GLY A CA  
1123 C C   . GLY A 147 ? 0.45327 0.51967 0.37441 -0.02946 0.03893  -0.00784 146 GLY A C   
1124 O O   . GLY A 147 ? 0.43565 0.48296 0.35324 -0.02957 0.03556  -0.00741 146 GLY A O   
1125 N N   . SER A 148 ? 0.45911 0.53852 0.38544 -0.03018 0.04190  -0.01148 147 SER A N   
1126 C CA  . SER A 148 ? 0.42331 0.49559 0.35224 -0.03132 0.04099  -0.01507 147 SER A CA  
1127 C C   . SER A 148 ? 0.46385 0.52422 0.39131 -0.02420 0.04143  -0.02118 147 SER A C   
1128 O O   . SER A 148 ? 0.46430 0.52910 0.39461 -0.01842 0.04310  -0.02364 147 SER A O   
1129 C CB  . SER A 148 ? 0.41702 0.50710 0.35426 -0.03164 0.04392  -0.01779 147 SER A CB  
1130 O OG  . SER A 148 ? 0.41842 0.52433 0.35871 -0.03685 0.04544  -0.01084 147 SER A OG  
1131 N N   . VAL A 149 ? 0.43697 0.48298 0.35976 -0.02464 0.03950  -0.02287 148 VAL A N   
1132 C CA  . VAL A 149 ? 0.45921 0.49496 0.37851 -0.01694 0.04136  -0.02681 148 VAL A CA  
1133 C C   . VAL A 149 ? 0.47349 0.51092 0.39390 -0.01613 0.04244  -0.03052 148 VAL A C   
1134 O O   . VAL A 149 ? 0.44716 0.48619 0.36798 -0.02206 0.03970  -0.03037 148 VAL A O   
1135 C CB  . VAL A 149 ? 0.47476 0.48840 0.38227 -0.01448 0.03860  -0.02626 148 VAL A CB  
1136 C CG1 . VAL A 149 ? 0.45077 0.46312 0.35965 -0.01267 0.03783  -0.02199 148 VAL A CG1 
1137 C CG2 . VAL A 149 ? 0.47633 0.47638 0.37588 -0.02249 0.03183  -0.02491 148 VAL A CG2 
1138 N N   . GLY A 150 ? 0.46558 0.50417 0.38800 -0.00893 0.04615  -0.03216 149 GLY A N   
1139 C CA  . GLY A 150 ? 0.45672 0.49526 0.37780 -0.00708 0.04756  -0.03382 149 GLY A CA  
1140 C C   . GLY A 150 ? 0.47969 0.50357 0.38692 0.00006  0.05016  -0.03505 149 GLY A C   
1141 O O   . GLY A 150 ? 0.44887 0.46843 0.35473 0.00647  0.05276  -0.03423 149 GLY A O   
1142 N N   . PHE A 151 ? 0.46423 0.48067 0.36045 -0.00004 0.04933  -0.03713 150 PHE A N   
1143 C CA  . PHE A 151 ? 0.50125 0.50031 0.37801 0.00776  0.05113  -0.04039 150 PHE A CA  
1144 C C   . PHE A 151 ? 0.52403 0.52346 0.39123 0.00917  0.05239  -0.04124 150 PHE A C   
1145 O O   . PHE A 151 ? 0.47878 0.48758 0.35374 0.00186  0.04920  -0.03928 150 PHE A O   
1146 C CB  . PHE A 151 ? 0.50313 0.47887 0.36493 0.00432  0.04340  -0.04381 150 PHE A CB  
1147 C CG  . PHE A 151 ? 0.54485 0.51645 0.40459 -0.00738 0.03457  -0.04363 150 PHE A CG  
1148 C CD1 . PHE A 151 ? 0.51758 0.50297 0.39388 -0.01703 0.03166  -0.03907 150 PHE A CD1 
1149 C CD2 . PHE A 151 ? 0.54094 0.49608 0.38201 -0.00817 0.02909  -0.04754 150 PHE A CD2 
1150 C CE1 . PHE A 151 ? 0.51102 0.49657 0.38938 -0.02732 0.02416  -0.03700 150 PHE A CE1 
1151 C CE2 . PHE A 151 ? 0.58982 0.54245 0.43189 -0.01980 0.01949  -0.04578 150 PHE A CE2 
1152 C CZ  . PHE A 151 ? 0.56166 0.53088 0.42446 -0.02942 0.01738  -0.03980 150 PHE A CZ  
1153 N N   . ASN A 152 ? 0.54022 0.53003 0.39007 0.01976  0.05738  -0.04386 151 ASN A N   
1154 C CA  . ASN A 152 ? 0.57451 0.55836 0.40548 0.02235  0.05770  -0.04591 151 ASN A CA  
1155 C C   . ASN A 152 ? 0.62955 0.58376 0.43083 0.02815  0.05337  -0.05465 151 ASN A C   
1156 O O   . ASN A 152 ? 0.63419 0.57438 0.43231 0.03194  0.05176  -0.05801 151 ASN A O   
1157 C CB  . ASN A 152 ? 0.56983 0.57242 0.40506 0.03162  0.06895  -0.04022 151 ASN A CB  
1158 C CG  . ASN A 152 ? 0.56209 0.58941 0.42480 0.02431  0.06947  -0.03159 151 ASN A CG  
1159 O OD1 . ASN A 152 ? 0.59537 0.62809 0.45922 0.01813  0.06602  -0.02882 151 ASN A OD1 
1160 N ND2 . ASN A 152 ? 0.51196 0.55260 0.39669 0.02500  0.07219  -0.02737 151 ASN A ND2 
1161 N N   . ILE A 153 ? 0.64113 0.58374 0.41945 0.02883  0.04995  -0.05845 152 ILE A N   
1162 C CA  . ILE A 153 ? 0.73579 0.64616 0.48130 0.03508  0.04369  -0.06852 152 ILE A CA  
1163 C C   . ILE A 153 ? 0.79465 0.70426 0.51469 0.04808  0.05169  -0.07155 152 ILE A C   
1164 O O   . ILE A 153 ? 0.76494 0.68891 0.48521 0.04383  0.05294  -0.06646 152 ILE A O   
1165 C CB  . ILE A 153 ? 0.74146 0.63195 0.47902 0.02070  0.02654  -0.07119 152 ILE A CB  
1166 C CG1 . ILE A 153 ? 0.72158 0.61312 0.48185 0.00983  0.02010  -0.06726 152 ILE A CG1 
1167 C CG2 . ILE A 153 ? 0.85068 0.70469 0.55045 0.02709  0.01751  -0.08234 152 ILE A CG2 
1168 C CD1 . ILE A 153 ? 0.71859 0.60330 0.48302 -0.00671 0.00518  -0.06463 152 ILE A CD1 
1169 N N   . ASP A 154 ? 0.87654 0.77054 0.57490 0.06478  0.05752  -0.07919 153 ASP A N   
1170 C CA  . ASP A 154 ? 0.95711 0.84789 0.62492 0.08048  0.06616  -0.08376 153 ASP A CA  
1171 C C   . ASP A 154 ? 1.02450 0.87226 0.65264 0.08648  0.05428  -0.09904 153 ASP A C   
1172 O O   . ASP A 154 ? 1.05121 0.87882 0.67037 0.09792  0.05430  -0.10701 153 ASP A O   
1173 C CB  . ASP A 154 ? 0.97674 0.88938 0.65408 0.09801  0.08491  -0.07929 153 ASP A CB  
1174 C CG  . ASP A 154 ? 1.12698 1.03926 0.77162 0.11675  0.09627  -0.08341 153 ASP A CG  
1175 O OD1 . ASP A 154 ? 1.18394 1.09829 0.82298 0.13606  0.10851  -0.08613 153 ASP A OD1 
1176 O OD2 . ASP A 154 ? 1.19716 1.10766 0.82102 0.11293  0.09305  -0.08368 153 ASP A OD2 
1177 N N   . TYR A 155 ? 1.07596 0.90833 0.68097 0.07853  0.04247  -0.10286 154 TYR A N   
1178 C CA  . TYR A 155 ? 1.15179 0.93986 0.72064 0.07910  0.02526  -0.11677 154 TYR A CA  
1179 C C   . TYR A 155 ? 1.14741 0.91566 0.73292 0.06754  0.01075  -0.11789 154 TYR A C   
1180 O O   . TYR A 155 ? 1.12172 0.88850 0.72198 0.04778  -0.00351 -0.11252 154 TYR A O   
1181 C CB  . TYR A 155 ? 1.20363 0.97047 0.73214 0.10405  0.03293  -0.13023 154 TYR A CB  
1182 C CG  . TYR A 155 ? 1.28667 1.00215 0.77277 0.10679  0.01333  -0.14696 154 TYR A CG  
1183 C CD1 . TYR A 155 ? 1.31017 1.00462 0.79304 0.08616  -0.00977 -0.14723 154 TYR A CD1 
1184 C CD2 . TYR A 155 ? 1.35262 1.04006 0.80265 0.13052  0.01694  -0.16234 154 TYR A CD2 
1185 C CE1 . TYR A 155 ? 1.36358 1.00910 0.80897 0.08713  -0.03058 -0.16172 154 TYR A CE1 
1186 C CE2 . TYR A 155 ? 1.39605 1.03190 0.80541 0.13342  -0.00346 -0.17902 154 TYR A CE2 
1187 C CZ  . TYR A 155 ? 1.40877 1.02303 0.81608 0.11068  -0.02818 -0.17835 154 TYR A CZ  
1188 O OH  . TYR A 155 ? 1.49881 1.05981 0.86669 0.11197  -0.05136 -0.19415 154 TYR A OH  
1189 N N   . ASP A 156 ? 1.20296 0.95704 0.78698 0.07995  0.01415  -0.12362 155 ASP A N   
1190 C CA  . ASP A 156 ? 1.16084 0.89503 0.75909 0.06992  0.00029  -0.12341 155 ASP A CA  
1191 C C   . ASP A 156 ? 1.07452 0.83077 0.70556 0.07342  0.01203  -0.11562 155 ASP A C   
1192 O O   . ASP A 156 ? 1.06874 0.81265 0.71393 0.06490  0.00191  -0.11311 155 ASP A O   
1193 C CB  . ASP A 156 ? 1.29567 0.97910 0.85707 0.07930  -0.01459 -0.13890 155 ASP A CB  
1194 C CG  . ASP A 156 ? 1.36295 1.03779 0.90279 0.10711  -0.00043 -0.14944 155 ASP A CG  
1195 O OD1 . ASP A 156 ? 1.25962 0.96593 0.80148 0.11963  0.02016  -0.14602 155 ASP A OD1 
1196 O OD2 . ASP A 156 ? 1.43143 1.06855 0.95358 0.11676  -0.01019 -0.16033 155 ASP A OD2 
1197 N N   . CYS A 157 ? 1.01448 0.80330 0.65854 0.08479  0.03188  -0.11036 156 CYS A N   
1198 C CA  . CYS A 157 ? 0.90001 0.71029 0.57462 0.08856  0.04212  -0.10259 156 CYS A CA  
1199 C C   . CYS A 157 ? 0.81726 0.66204 0.52773 0.07140  0.04442  -0.08915 156 CYS A C   
1200 O O   . CYS A 157 ? 0.78796 0.65792 0.50537 0.06895  0.05205  -0.08362 156 CYS A O   
1201 C CB  . CYS A 157 ? 0.88421 0.71088 0.55529 0.11095  0.06121  -0.10321 156 CYS A CB  
1202 S SG  . CYS A 157 ? 0.81236 0.66492 0.52192 0.11579  0.07177  -0.09273 156 CYS A SG  
1203 N N   . VAL A 158 ? 0.76928 0.61445 0.50127 0.06031  0.03747  -0.08388 157 VAL A N   
1204 C CA  . VAL A 158 ? 0.71465 0.59059 0.47852 0.04668  0.03983  -0.07282 157 VAL A CA  
1205 C C   . VAL A 158 ? 0.65014 0.55094 0.43493 0.05592  0.05313  -0.06677 157 VAL A C   
1206 O O   . VAL A 158 ? 0.63303 0.52614 0.42186 0.06285  0.05360  -0.06689 157 VAL A O   
1207 C CB  . VAL A 158 ? 0.67789 0.54521 0.45315 0.03092  0.02687  -0.06897 157 VAL A CB  
1208 C CG1 . VAL A 158 ? 0.61037 0.50989 0.41515 0.01985  0.03071  -0.05918 157 VAL A CG1 
1209 C CG2 . VAL A 158 ? 0.71906 0.56260 0.47695 0.02059  0.01190  -0.07291 157 VAL A CG2 
1210 N N   . SER A 159 ? 0.61385 0.54368 0.41317 0.05550  0.06237  -0.06053 158 SER A N   
1211 C CA  . SER A 159 ? 0.60310 0.55904 0.42677 0.06081  0.07233  -0.05256 158 SER A CA  
1212 C C   . SER A 159 ? 0.54544 0.51666 0.39342 0.04614  0.06716  -0.04624 158 SER A C   
1213 O O   . SER A 159 ? 0.52686 0.51309 0.38443 0.03733  0.06638  -0.04303 158 SER A O   
1214 C CB  . SER A 159 ? 0.57347 0.55167 0.40010 0.06841  0.08388  -0.04782 158 SER A CB  
1215 O OG  . SER A 159 ? 0.64561 0.61433 0.45078 0.08579  0.09187  -0.05281 158 SER A OG  
1216 N N   . PHE A 160 ? 0.54912 0.51543 0.40544 0.04432  0.06321  -0.04473 159 PHE A N   
1217 C CA  . PHE A 160 ? 0.51478 0.49676 0.39134 0.03320  0.05973  -0.03904 159 PHE A CA  
1218 C C   . PHE A 160 ? 0.48386 0.49097 0.38115 0.03696  0.06655  -0.03261 159 PHE A C   
1219 O O   . PHE A 160 ? 0.50193 0.51301 0.40427 0.04765  0.07218  -0.02982 159 PHE A O   
1220 C CB  . PHE A 160 ? 0.51144 0.48107 0.38856 0.03027  0.05325  -0.03786 159 PHE A CB  
1221 C CG  . PHE A 160 ? 0.51666 0.46234 0.37807 0.02330  0.04365  -0.04143 159 PHE A CG  
1222 C CD1 . PHE A 160 ? 0.50600 0.45653 0.37085 0.00949  0.03773  -0.03937 159 PHE A CD1 
1223 C CD2 . PHE A 160 ? 0.55134 0.46957 0.39602 0.03082  0.03962  -0.04626 159 PHE A CD2 
1224 C CE1 . PHE A 160 ? 0.51734 0.44786 0.37145 0.00149  0.02751  -0.04011 159 PHE A CE1 
1225 C CE2 . PHE A 160 ? 0.55825 0.45207 0.38976 0.02289  0.02786  -0.04860 159 PHE A CE2 
1226 C CZ  . PHE A 160 ? 0.54837 0.44940 0.38578 0.00727  0.02155  -0.04451 159 PHE A CZ  
1227 N N   . CYS A 161 ? 0.45869 0.48244 0.36932 0.02843  0.06507  -0.02982 160 CYS A N   
1228 C CA  . CYS A 161 ? 0.44208 0.48714 0.37295 0.03015  0.06839  -0.02341 160 CYS A CA  
1229 C C   . CYS A 161 ? 0.45700 0.51200 0.40228 0.02188  0.06236  -0.02168 160 CYS A C   
1230 O O   . CYS A 161 ? 0.46262 0.53156 0.42463 0.02296  0.06213  -0.01645 160 CYS A O   
1231 C CB  . CYS A 161 ? 0.43750 0.49347 0.37114 0.03033  0.07215  -0.02105 160 CYS A CB  
1232 S SG  . CYS A 161 ? 0.47426 0.52841 0.40427 0.01878  0.06579  -0.02495 160 CYS A SG  
1233 N N   . TYR A 162 ? 0.43784 0.48674 0.37703 0.01410  0.05715  -0.02539 161 TYR A N   
1234 C CA  . TYR A 162 ? 0.43603 0.49540 0.38513 0.00809  0.05261  -0.02523 161 TYR A CA  
1235 C C   . TYR A 162 ? 0.45219 0.50540 0.39324 0.00322  0.04918  -0.02615 161 TYR A C   
1236 O O   . TYR A 162 ? 0.44638 0.48829 0.37647 0.00034  0.04837  -0.02734 161 TYR A O   
1237 C CB  . TYR A 162 ? 0.43677 0.50385 0.39111 0.00357  0.05113  -0.02756 161 TYR A CB  
1238 C CG  . TYR A 162 ? 0.44395 0.51984 0.40571 -0.00026 0.04651  -0.02977 161 TYR A CG  
1239 C CD1 . TYR A 162 ? 0.43834 0.52206 0.41252 0.00120  0.04295  -0.02844 161 TYR A CD1 
1240 C CD2 . TYR A 162 ? 0.44470 0.52125 0.40084 -0.00479 0.04522  -0.03301 161 TYR A CD2 
1241 C CE1 . TYR A 162 ? 0.40766 0.49601 0.38450 -0.00061 0.03767  -0.03268 161 TYR A CE1 
1242 C CE2 . TYR A 162 ? 0.40158 0.48681 0.36168 -0.00562 0.04240  -0.03622 161 TYR A CE2 
1243 C CZ  . TYR A 162 ? 0.42326 0.51257 0.39171 -0.00295 0.03836  -0.03726 161 TYR A CZ  
1244 O OH  . TYR A 162 ? 0.37889 0.47350 0.34731 -0.00218 0.03451  -0.04258 161 TYR A OH  
1245 N N   . MET A 163 ? 0.42725 0.48800 0.37354 0.00187  0.04623  -0.02462 162 MET A N   
1246 C CA  . MET A 163 ? 0.42848 0.48951 0.36819 -0.00335 0.04360  -0.02385 162 MET A CA  
1247 C C   . MET A 163 ? 0.41950 0.49385 0.36379 -0.00467 0.04136  -0.02640 162 MET A C   
1248 O O   . MET A 163 ? 0.40725 0.48592 0.35881 -0.00164 0.03858  -0.02643 162 MET A O   
1249 C CB  . MET A 163 ? 0.43232 0.48544 0.36802 -0.00192 0.04166  -0.01878 162 MET A CB  
1250 C CG  . MET A 163 ? 0.44778 0.50272 0.37648 -0.00830 0.03893  -0.01514 162 MET A CG  
1251 S SD  . MET A 163 ? 0.49050 0.53176 0.41431 -0.00805 0.03491  -0.00737 162 MET A SD  
1252 C CE  . MET A 163 ? 0.46571 0.48870 0.38144 -0.01237 0.03335  -0.00696 162 MET A CE  
1253 N N   . HIS A 164 ? 0.41901 0.49975 0.35930 -0.00864 0.04197  -0.02841 163 HIS A N   
1254 C CA  . HIS A 164 ? 0.42066 0.51274 0.36297 -0.00743 0.04062  -0.03343 163 HIS A CA  
1255 C C   . HIS A 164 ? 0.42312 0.51977 0.35793 -0.00674 0.03815  -0.03225 163 HIS A C   
1256 O O   . HIS A 164 ? 0.41669 0.51315 0.34392 -0.00986 0.03919  -0.02634 163 HIS A O   
1257 C CB  . HIS A 164 ? 0.40846 0.50838 0.35051 -0.00994 0.04360  -0.03557 163 HIS A CB  
1258 C CG  . HIS A 164 ? 0.42835 0.53939 0.37075 -0.00615 0.04310  -0.04202 163 HIS A CG  
1259 N ND1 . HIS A 164 ? 0.42948 0.53904 0.37895 -0.00190 0.03895  -0.04858 163 HIS A ND1 
1260 C CD2 . HIS A 164 ? 0.43209 0.55548 0.36791 -0.00500 0.04597  -0.04299 163 HIS A CD2 
1261 C CE1 . HIS A 164 ? 0.46039 0.57770 0.40622 0.00254  0.03839  -0.05523 163 HIS A CE1 
1262 N NE2 . HIS A 164 ? 0.45310 0.58038 0.38994 0.00154  0.04375  -0.05218 163 HIS A NE2 
1263 N N   . HIS A 165 ? 0.41800 0.51778 0.35409 -0.00310 0.03347  -0.03745 164 HIS A N   
1264 C CA  . HIS A 165 ? 0.43290 0.53554 0.35875 -0.00205 0.02955  -0.03699 164 HIS A CA  
1265 C C   . HIS A 165 ? 0.44943 0.55908 0.36723 0.00207  0.02760  -0.04604 164 HIS A C   
1266 O O   . HIS A 165 ? 0.47730 0.59317 0.38047 0.00326  0.02779  -0.04611 164 HIS A O   
1267 C CB  . HIS A 165 ? 0.43096 0.52708 0.36317 -0.00096 0.02241  -0.03384 164 HIS A CB  
1268 C CG  . HIS A 165 ? 0.43298 0.52323 0.36823 -0.00241 0.02420  -0.02478 164 HIS A CG  
1269 N ND1 . HIS A 165 ? 0.43848 0.52729 0.36806 -0.00311 0.02036  -0.01855 164 HIS A ND1 
1270 C CD2 . HIS A 165 ? 0.41539 0.49944 0.35749 -0.00215 0.02878  -0.02150 164 HIS A CD2 
1271 C CE1 . HIS A 165 ? 0.46041 0.54186 0.39519 -0.00281 0.02242  -0.01190 164 HIS A CE1 
1272 N NE2 . HIS A 165 ? 0.43193 0.50989 0.37298 -0.00167 0.02775  -0.01433 164 HIS A NE2 
1273 N N   . MET A 166 ? 0.44696 0.55524 0.37292 0.00508  0.02544  -0.05369 165 MET A N   
1274 C CA  . MET A 166 ? 0.47329 0.58209 0.39152 0.01104  0.01979  -0.06416 165 MET A CA  
1275 C C   . MET A 166 ? 0.48799 0.59578 0.41648 0.01434  0.01914  -0.07172 165 MET A C   
1276 O O   . MET A 166 ? 0.45183 0.55584 0.39571 0.01113  0.01909  -0.06820 165 MET A O   
1277 C CB  . MET A 166 ? 0.48732 0.58669 0.40525 0.01126  0.00772  -0.06497 165 MET A CB  
1278 C CG  . MET A 166 ? 0.53317 0.62555 0.44617 0.01682  -0.00301 -0.07690 165 MET A CG  
1279 S SD  . MET A 166 ? 0.73063 0.81136 0.64745 0.01400  -0.02000 -0.07437 165 MET A SD  
1280 C CE  . MET A 166 ? 0.50082 0.58557 0.43701 0.00709  -0.01432 -0.05794 165 MET A CE  
1281 N N   . GLU A 167 ? 0.48470 0.59615 0.40350 0.02169  0.01874  -0.08198 166 GLU A N   
1282 C CA  . GLU A 167 ? 0.51392 0.62159 0.44152 0.02695  0.01508  -0.09105 166 GLU A CA  
1283 C C   . GLU A 167 ? 0.55200 0.64589 0.47389 0.03230  0.00108  -0.10157 166 GLU A C   
1284 O O   . GLU A 167 ? 0.54850 0.64137 0.45089 0.03674  -0.00198 -0.10705 166 GLU A O   
1285 C CB  . GLU A 167 ? 0.52232 0.64414 0.44511 0.03347  0.02490  -0.09564 166 GLU A CB  
1286 C CG  . GLU A 167 ? 0.55195 0.66878 0.48041 0.04239  0.01984  -0.10760 166 GLU A CG  
1287 C CD  . GLU A 167 ? 0.57602 0.71032 0.50439 0.04959  0.03090  -0.11020 166 GLU A CD  
1288 O OE1 . GLU A 167 ? 0.55640 0.70534 0.49023 0.04351  0.04104  -0.09945 166 GLU A OE1 
1289 O OE2 . GLU A 167 ? 0.60849 0.74164 0.53204 0.06171  0.02873  -0.12276 166 GLU A OE2 
1290 N N   . LEU A 168 ? 0.53593 0.61843 0.47419 0.03136  -0.00866 -0.10369 167 LEU A N   
1291 C CA  . LEU A 168 ? 0.58907 0.65484 0.52586 0.03471  -0.02547 -0.11268 167 LEU A CA  
1292 C C   . LEU A 168 ? 0.63017 0.69102 0.55774 0.04669  -0.02811 -0.12850 167 LEU A C   
1293 O O   . LEU A 168 ? 0.62755 0.69986 0.55747 0.05140  -0.01682 -0.13019 167 LEU A O   
1294 C CB  . LEU A 168 ? 0.58467 0.64156 0.54636 0.02690  -0.03560 -0.10462 167 LEU A CB  
1295 C CG  . LEU A 168 ? 0.56720 0.62872 0.53843 0.01767  -0.03422 -0.08985 167 LEU A CG  
1296 C CD1 . LEU A 168 ? 0.56881 0.62685 0.56582 0.01103  -0.04158 -0.08014 167 LEU A CD1 
1297 C CD2 . LEU A 168 ? 0.57400 0.63055 0.53222 0.01746  -0.04286 -0.09097 167 LEU A CD2 
1298 N N   . PRO A 169 ? 0.65532 0.69857 0.57203 0.05260  -0.04374 -0.14060 168 PRO A N   
1299 C CA  . PRO A 169 ? 0.67007 0.70552 0.57598 0.06680  -0.04712 -0.15798 168 PRO A CA  
1300 C C   . PRO A 169 ? 0.70231 0.73718 0.63031 0.06863  -0.04611 -0.15828 168 PRO A C   
1301 O O   . PRO A 169 ? 0.72876 0.77019 0.65105 0.08066  -0.03845 -0.16784 168 PRO A O   
1302 C CB  . PRO A 169 ? 0.67447 0.68404 0.57026 0.06910  -0.06970 -0.16861 168 PRO A CB  
1303 C CG  . PRO A 169 ? 0.66817 0.68079 0.55610 0.06009  -0.07174 -0.15917 168 PRO A CG  
1304 C CD  . PRO A 169 ? 0.63660 0.66697 0.54603 0.04810  -0.05861 -0.13992 168 PRO A CD  
1305 N N   . THR A 170 ? 0.64768 0.67677 0.60126 0.05751  -0.05324 -0.14702 169 THR A N   
1306 C CA  . THR A 170 ? 0.65555 0.68420 0.62993 0.05820  -0.05327 -0.14549 169 THR A CA  
1307 C C   . THR A 170 ? 0.61502 0.66659 0.59496 0.05665  -0.03383 -0.13721 169 THR A C   
1308 O O   . THR A 170 ? 0.60789 0.66114 0.60538 0.05598  -0.03332 -0.13389 169 THR A O   
1309 C CB  . THR A 170 ? 0.66546 0.68327 0.66471 0.04620  -0.06655 -0.13370 169 THR A CB  
1310 O OG1 . THR A 170 ? 0.61599 0.64576 0.62069 0.03450  -0.05913 -0.11788 169 THR A OG1 
1311 C CG2 . THR A 170 ? 0.62746 0.62030 0.62631 0.04707  -0.08968 -0.14139 169 THR A CG2 
1312 N N   . GLY A 171 ? 0.61123 0.67937 0.57753 0.05523  -0.01966 -0.13283 170 GLY A N   
1313 C CA  . GLY A 171 ? 0.57699 0.66513 0.54850 0.05265  -0.00372 -0.12448 170 GLY A CA  
1314 C C   . GLY A 171 ? 0.54716 0.63900 0.53152 0.03924  -0.00008 -0.10893 170 GLY A C   
1315 O O   . GLY A 171 ? 0.51913 0.62464 0.50621 0.03582  0.01108  -0.10180 170 GLY A O   
1316 N N   . VAL A 172 ? 0.53337 0.61382 0.52576 0.03199  -0.00947 -0.10315 171 VAL A N   
1317 C CA  . VAL A 172 ? 0.48990 0.57468 0.49090 0.02168  -0.00455 -0.08915 171 VAL A CA  
1318 C C   . VAL A 172 ? 0.50274 0.59285 0.48990 0.01899  0.00214  -0.08503 171 VAL A C   
1319 O O   . VAL A 172 ? 0.50569 0.59652 0.47751 0.02389  0.00197  -0.09177 171 VAL A O   
1320 C CB  . VAL A 172 ? 0.52358 0.59866 0.54140 0.01585  -0.01564 -0.08225 171 VAL A CB  
1321 C CG1 . VAL A 172 ? 0.51601 0.58663 0.54923 0.01675  -0.02180 -0.08300 171 VAL A CG1 
1322 C CG2 . VAL A 172 ? 0.52421 0.58809 0.53954 0.01673  -0.02860 -0.08634 171 VAL A CG2 
1323 N N   . HIS A 173 ? 0.48250 0.57566 0.47368 0.01199  0.00769  -0.07406 172 HIS A N   
1324 C CA  . HIS A 173 ? 0.47847 0.57609 0.45783 0.00970  0.01468  -0.06938 172 HIS A CA  
1325 C C   . HIS A 173 ? 0.44709 0.54051 0.43256 0.00546  0.01194  -0.06078 172 HIS A C   
1326 O O   . HIS A 173 ? 0.43987 0.53092 0.43956 0.00306  0.00831  -0.05561 172 HIS A O   
1327 C CB  . HIS A 173 ? 0.44730 0.55275 0.42328 0.00701  0.02530  -0.06506 172 HIS A CB  
1328 C CG  . HIS A 173 ? 0.47643 0.59068 0.45046 0.01122  0.02895  -0.07093 172 HIS A CG  
1329 N ND1 . HIS A 173 ? 0.47851 0.59482 0.46382 0.01166  0.02881  -0.07175 172 HIS A ND1 
1330 C CD2 . HIS A 173 ? 0.47908 0.60273 0.44207 0.01603  0.03320  -0.07536 172 HIS A CD2 
1331 C CE1 . HIS A 173 ? 0.49310 0.62015 0.47643 0.01699  0.03299  -0.07651 172 HIS A CE1 
1332 N NE2 . HIS A 173 ? 0.49047 0.62310 0.45984 0.02005  0.03648  -0.07870 172 HIS A NE2 
1333 N N   . ALA A 174 ? 0.42701 0.52134 0.40256 0.00493  0.01395  -0.05803 173 ALA A N   
1334 C CA  . ALA A 174 ? 0.40825 0.50037 0.39019 0.00271  0.01124  -0.04994 173 ALA A CA  
1335 C C   . ALA A 174 ? 0.43296 0.52657 0.40547 0.00160  0.01895  -0.04438 173 ALA A C   
1336 O O   . ALA A 174 ? 0.41402 0.51020 0.37345 0.00156  0.02341  -0.04656 173 ALA A O   
1337 C CB  . ALA A 174 ? 0.44946 0.53734 0.43203 0.00364  -0.00083 -0.05243 173 ALA A CB  
1338 N N   . GLY A 175 ? 0.40846 0.50104 0.38887 0.00110  0.02029  -0.03626 174 GLY A N   
1339 C CA  . GLY A 175 ? 0.42496 0.51540 0.39762 0.00114  0.02617  -0.03131 174 GLY A CA  
1340 C C   . GLY A 175 ? 0.41463 0.50490 0.39818 0.00344  0.02683  -0.02318 174 GLY A C   
1341 O O   . GLY A 175 ? 0.41027 0.50499 0.40876 0.00393  0.02223  -0.01957 174 GLY A O   
1342 N N   . THR A 176 ? 0.39029 0.47567 0.36738 0.00516  0.03222  -0.01960 175 THR A N   
1343 C CA  . THR A 176 ? 0.43332 0.51889 0.41934 0.00996  0.03419  -0.01222 175 THR A CA  
1344 C C   . THR A 176 ? 0.43540 0.51555 0.41729 0.01401  0.04283  -0.01189 175 THR A C   
1345 O O   . THR A 176 ? 0.41528 0.48987 0.38673 0.01153  0.04561  -0.01683 175 THR A O   
1346 C CB  . THR A 176 ? 0.42843 0.51001 0.40965 0.01083  0.03123  -0.00845 175 THR A CB  
1347 O OG1 . THR A 176 ? 0.41372 0.48497 0.38016 0.00995  0.03504  -0.01005 175 THR A OG1 
1348 C CG2 . THR A 176 ? 0.43014 0.51531 0.40816 0.00674  0.02240  -0.01011 175 THR A CG2 
1349 N N   . ASP A 177 ? 0.43253 0.51473 0.42248 0.02101  0.04671  -0.00589 176 ASP A N   
1350 C CA  . ASP A 177 ? 0.44209 0.51496 0.42216 0.02760  0.05443  -0.00698 176 ASP A CA  
1351 C C   . ASP A 177 ? 0.43601 0.49411 0.40405 0.02854  0.05246  -0.00820 176 ASP A C   
1352 O O   . ASP A 177 ? 0.44366 0.50201 0.41199 0.02384  0.04628  -0.00658 176 ASP A O   
1353 C CB  . ASP A 177 ? 0.44471 0.52778 0.43766 0.03702  0.06100  -0.00010 176 ASP A CB  
1354 C CG  . ASP A 177 ? 0.44184 0.53327 0.45122 0.04109  0.05823  0.00812  176 ASP A CG  
1355 O OD1 . ASP A 177 ? 0.43239 0.51605 0.43761 0.03902  0.05236  0.00764  176 ASP A OD1 
1356 O OD2 . ASP A 177 ? 0.45879 0.56634 0.48676 0.04604  0.06164  0.01670  176 ASP A OD2 
1357 N N   . LEU A 178 ? 0.42871 0.47264 0.38500 0.03479  0.05676  -0.01078 177 LEU A N   
1358 C CA  . LEU A 178 ? 0.48162 0.50817 0.42717 0.03479  0.05273  -0.01133 177 LEU A CA  
1359 C C   . LEU A 178 ? 0.51177 0.53919 0.46745 0.04207  0.05140  -0.00495 177 LEU A C   
1360 O O   . LEU A 178 ? 0.51484 0.52737 0.46375 0.04227  0.04676  -0.00383 177 LEU A O   
1361 C CB  . LEU A 178 ? 0.48654 0.49259 0.41430 0.03874  0.05467  -0.01751 177 LEU A CB  
1362 C CG  . LEU A 178 ? 0.48954 0.48727 0.40541 0.02729  0.04990  -0.02145 177 LEU A CG  
1363 C CD1 . LEU A 178 ? 0.48616 0.48051 0.40180 0.01857  0.04260  -0.01712 177 LEU A CD1 
1364 C CD2 . LEU A 178 ? 0.47481 0.48931 0.39653 0.02111  0.05194  -0.02282 177 LEU A CD2 
1365 N N   . GLU A 179 ? 0.49154 0.53639 0.46520 0.04737  0.05420  0.00069  178 GLU A N   
1366 C CA  . GLU A 179 ? 0.50542 0.55564 0.49331 0.05229  0.05100  0.00869  178 GLU A CA  
1367 C C   . GLU A 179 ? 0.48422 0.54494 0.48015 0.04230  0.04175  0.01299  178 GLU A C   
1368 O O   . GLU A 179 ? 0.47047 0.53630 0.47835 0.04447  0.03671  0.02049  178 GLU A O   
1369 C CB  . GLU A 179 ? 0.49990 0.56549 0.50571 0.06407  0.05864  0.01470  178 GLU A CB  
1370 C CG  . GLU A 179 ? 0.52503 0.58031 0.52017 0.07777  0.06865  0.01014  178 GLU A CG  
1371 C CD  . GLU A 179 ? 0.59267 0.66723 0.60698 0.09156  0.07782  0.01820  178 GLU A CD  
1372 O OE1 . GLU A 179 ? 0.58832 0.68433 0.62723 0.08867  0.07489  0.02878  178 GLU A OE1 
1373 O OE2 . GLU A 179 ? 0.64062 0.70934 0.64526 0.10561  0.08762  0.01435  178 GLU A OE2 
1374 N N   . GLY A 180 ? 0.46344 0.52709 0.45235 0.03242  0.03898  0.00813  179 GLY A N   
1375 C CA  . GLY A 180 ? 0.45730 0.52775 0.44744 0.02441  0.03013  0.00953  179 GLY A CA  
1376 C C   . GLY A 180 ? 0.45822 0.54361 0.46475 0.02275  0.02583  0.01206  179 GLY A C   
1377 O O   . GLY A 180 ? 0.44454 0.53320 0.45032 0.01721  0.01662  0.01219  179 GLY A O   
1378 N N   . ASN A 181 ? 0.45043 0.54454 0.47097 0.02716  0.03126  0.01462  180 ASN A N   
1379 C CA  . ASN A 181 ? 0.43693 0.54500 0.47647 0.02419  0.02551  0.01934  180 ASN A CA  
1380 C C   . ASN A 181 ? 0.42565 0.53290 0.45906 0.01802  0.02436  0.01160  180 ASN A C   
1381 O O   . ASN A 181 ? 0.38647 0.49200 0.41448 0.01963  0.03264  0.00818  180 ASN A O   
1382 C CB  . ASN A 181 ? 0.42762 0.54948 0.48875 0.03173  0.03206  0.02941  180 ASN A CB  
1383 C CG  . ASN A 181 ? 0.45326 0.57782 0.52414 0.03970  0.03303  0.03761  180 ASN A CG  
1384 O OD1 . ASN A 181 ? 0.50274 0.62505 0.57130 0.05010  0.04349  0.03831  180 ASN A OD1 
1385 N ND2 . ASN A 181 ? 0.44753 0.57579 0.52852 0.03563  0.02127  0.04343  180 ASN A ND2 
1386 N N   . PHE A 182 ? 0.40137 0.50872 0.43465 0.01174  0.01330  0.00850  181 PHE A N   
1387 C CA  . PHE A 182 ? 0.41217 0.51760 0.44082 0.00734  0.01079  0.00052  181 PHE A CA  
1388 C C   . PHE A 182 ? 0.42638 0.54025 0.47290 0.00751  0.01325  0.00584  181 PHE A C   
1389 O O   . PHE A 182 ? 0.37880 0.50346 0.44605 0.00881  0.01177  0.01691  181 PHE A O   
1390 C CB  . PHE A 182 ? 0.42062 0.52325 0.44653 0.00287  -0.00309 -0.00404 181 PHE A CB  
1391 C CG  . PHE A 182 ? 0.45215 0.54749 0.45375 0.00203  -0.00304 -0.01386 181 PHE A CG  
1392 C CD1 . PHE A 182 ? 0.44516 0.53788 0.43652 0.00139  -0.00053 -0.02357 181 PHE A CD1 
1393 C CD2 . PHE A 182 ? 0.44729 0.54050 0.43757 0.00213  -0.00531 -0.01190 181 PHE A CD2 
1394 C CE1 . PHE A 182 ? 0.45002 0.54060 0.42098 0.00151  0.00114  -0.03082 181 PHE A CE1 
1395 C CE2 . PHE A 182 ? 0.47320 0.56338 0.44149 0.00123  -0.00417 -0.01860 181 PHE A CE2 
1396 C CZ  . PHE A 182 ? 0.47692 0.56705 0.43590 0.00123  -0.00024 -0.02791 181 PHE A CZ  
1397 N N   . TYR A 183 ? 0.39893 0.50974 0.43862 0.00600  0.01705  -0.00045 182 TYR A N   
1398 C CA  . TYR A 183 ? 0.43241 0.55024 0.48808 0.00395  0.01573  0.00434  182 TYR A CA  
1399 C C   . TYR A 183 ? 0.41683 0.53230 0.48189 -0.00152 0.00029  0.00232  182 TYR A C   
1400 O O   . TYR A 183 ? 0.40666 0.51243 0.45742 -0.00272 -0.00520 -0.00907 182 TYR A O   
1401 C CB  . TYR A 183 ? 0.40479 0.51886 0.44951 0.00400  0.02334  -0.00137 182 TYR A CB  
1402 C CG  . TYR A 183 ? 0.43341 0.54718 0.46820 0.00939  0.03639  0.00043  182 TYR A CG  
1403 C CD1 . TYR A 183 ? 0.44049 0.56445 0.48536 0.01333  0.04350  0.00991  182 TYR A CD1 
1404 C CD2 . TYR A 183 ? 0.43128 0.53424 0.44585 0.01078  0.04096  -0.00703 182 TYR A CD2 
1405 C CE1 . TYR A 183 ? 0.45563 0.57660 0.48714 0.02018  0.05486  0.00941  182 TYR A CE1 
1406 C CE2 . TYR A 183 ? 0.42133 0.51934 0.42484 0.01588  0.05019  -0.00681 182 TYR A CE2 
1407 C CZ  . TYR A 183 ? 0.44676 0.55258 0.45701 0.02140  0.05712  0.00015  182 TYR A CZ  
1408 O OH  . TYR A 183 ? 0.44064 0.53901 0.43580 0.02835  0.06580  -0.00167 182 TYR A OH  
1409 N N   . GLY A 184 ? 0.40773 0.53204 0.49677 -0.00438 -0.00724 0.01365  183 GLY A N   
1410 C CA  . GLY A 184 ? 0.42614 0.54489 0.52522 -0.01015 -0.02507 0.01233  183 GLY A CA  
1411 C C   . GLY A 184 ? 0.45251 0.56705 0.54926 -0.01111 -0.03633 0.01146  183 GLY A C   
1412 O O   . GLY A 184 ? 0.43250 0.55145 0.52513 -0.00770 -0.03017 0.01509  183 GLY A O   
1413 N N   . PRO A 185 ? 0.46165 0.56564 0.55976 -0.01549 -0.05444 0.00622  184 PRO A N   
1414 C CA  . PRO A 185 ? 0.47334 0.57280 0.57014 -0.01748 -0.06858 0.00681  184 PRO A CA  
1415 C C   . PRO A 185 ? 0.48833 0.57580 0.55261 -0.01367 -0.06858 -0.00844 184 PRO A C   
1416 O O   . PRO A 185 ? 0.54205 0.62120 0.59827 -0.01529 -0.08329 -0.01200 184 PRO A O   
1417 C CB  . PRO A 185 ? 0.47879 0.57015 0.59199 -0.02428 -0.09016 0.00840  184 PRO A CB  
1418 C CG  . PRO A 185 ? 0.51145 0.59344 0.61620 -0.02287 -0.08776 -0.00271 184 PRO A CG  
1419 C CD  . PRO A 185 ? 0.47810 0.57246 0.58056 -0.01876 -0.06493 0.00042  184 PRO A CD  
1420 N N   . PHE A 186 ? 0.50794 0.59528 0.55330 -0.00900 -0.05284 -0.01640 185 PHE A N   
1421 C CA  . PHE A 186 ? 0.49956 0.57872 0.51546 -0.00561 -0.05192 -0.02967 185 PHE A CA  
1422 C C   . PHE A 186 ? 0.50590 0.58884 0.51140 -0.00459 -0.04781 -0.02475 185 PHE A C   
1423 O O   . PHE A 186 ? 0.47986 0.57104 0.49870 -0.00451 -0.04109 -0.01317 185 PHE A O   
1424 C CB  . PHE A 186 ? 0.49799 0.57736 0.50163 -0.00219 -0.03840 -0.03827 185 PHE A CB  
1425 C CG  . PHE A 186 ? 0.49190 0.56829 0.50810 -0.00305 -0.04166 -0.04111 185 PHE A CG  
1426 C CD1 . PHE A 186 ? 0.50767 0.57226 0.52138 -0.00253 -0.05645 -0.05075 185 PHE A CD1 
1427 C CD2 . PHE A 186 ? 0.44841 0.53217 0.47782 -0.00403 -0.03119 -0.03414 185 PHE A CD2 
1428 C CE1 . PHE A 186 ? 0.53086 0.59105 0.55784 -0.00350 -0.06106 -0.05241 185 PHE A CE1 
1429 C CE2 . PHE A 186 ? 0.45923 0.54064 0.50068 -0.00551 -0.03510 -0.03497 185 PHE A CE2 
1430 C CZ  . PHE A 186 ? 0.49635 0.56596 0.53807 -0.00553 -0.05025 -0.04358 185 PHE A CZ  
1431 N N   . VAL A 187 ? 0.49216 0.56893 0.47290 -0.00296 -0.05220 -0.03355 186 VAL A N   
1432 C CA  . VAL A 187 ? 0.50577 0.58500 0.47323 -0.00261 -0.05000 -0.02899 186 VAL A CA  
1433 C C   . VAL A 187 ? 0.51635 0.59570 0.45636 0.00056  -0.04047 -0.03795 186 VAL A C   
1434 O O   . VAL A 187 ? 0.50072 0.57703 0.42918 0.00354  -0.04023 -0.04969 186 VAL A O   
1435 C CB  . VAL A 187 ? 0.53979 0.61397 0.50508 -0.00512 -0.06833 -0.02670 186 VAL A CB  
1436 C CG1 . VAL A 187 ? 0.48955 0.56924 0.48686 -0.00885 -0.07570 -0.01257 186 VAL A CG1 
1437 C CG2 . VAL A 187 ? 0.55678 0.61894 0.50733 -0.00416 -0.08216 -0.04061 186 VAL A CG2 
1438 N N   . ASP A 188 ? 0.50169 0.58547 0.43297 0.00016  -0.03278 -0.03125 187 ASP A N   
1439 C CA  . ASP A 188 ? 0.49122 0.57901 0.40060 0.00169  -0.02260 -0.03541 187 ASP A CA  
1440 C C   . ASP A 188 ? 0.55886 0.64614 0.44289 0.00301  -0.03017 -0.03948 187 ASP A C   
1441 O O   . ASP A 188 ? 0.54198 0.63253 0.41476 0.00120  -0.02943 -0.03183 187 ASP A O   
1442 C CB  . ASP A 188 ? 0.47301 0.56421 0.38627 -0.00035 -0.01172 -0.02524 187 ASP A CB  
1443 C CG  . ASP A 188 ? 0.47522 0.56431 0.39702 -0.00188 -0.01735 -0.01379 187 ASP A CG  
1444 O OD1 . ASP A 188 ? 0.50619 0.59352 0.43931 -0.00203 -0.02833 -0.01174 187 ASP A OD1 
1445 O OD2 . ASP A 188 ? 0.45637 0.54532 0.37533 -0.00307 -0.01177 -0.00603 187 ASP A OD2 
1446 N N   . ARG A 189 ? 0.54629 0.62822 0.41994 0.00674  -0.03831 -0.05201 188 ARG A N   
1447 C CA  . ARG A 189 ? 0.63991 0.72084 0.48335 0.01066  -0.04392 -0.05972 188 ARG A CA  
1448 C C   . ARG A 189 ? 0.65543 0.73226 0.48773 0.01811  -0.04448 -0.07645 188 ARG A C   
1449 O O   . ARG A 189 ? 0.65333 0.72550 0.50400 0.01861  -0.04494 -0.08089 188 ARG A O   
1450 C CB  . ARG A 189 ? 0.67286 0.74495 0.51192 0.00797  -0.06226 -0.05676 188 ARG A CB  
1451 C CG  . ARG A 189 ? 0.69515 0.75388 0.54795 0.00716  -0.07946 -0.06284 188 ARG A CG  
1452 C CD  . ARG A 189 ? 0.73578 0.79390 0.61458 0.00013  -0.08967 -0.04837 188 ARG A CD  
1453 N NE  . ARG A 189 ? 0.82237 0.88373 0.68958 -0.00222 -0.09344 -0.03895 188 ARG A NE  
1454 C CZ  . ARG A 189 ? 0.88379 0.94884 0.77284 -0.00686 -0.09786 -0.02388 188 ARG A CZ  
1455 N NH1 . ARG A 189 ? 0.82534 0.89354 0.74840 -0.00909 -0.09754 -0.01609 188 ARG A NH1 
1456 N NH2 . ARG A 189 ? 0.81652 0.88357 0.69336 -0.00864 -0.10228 -0.01558 188 ARG A NH2 
1457 N N   . GLN A 190 ? 0.71655 0.79550 0.51774 0.02481  -0.04433 -0.08541 189 GLN A N   
1458 C CA  . GLN A 190 ? 0.71221 0.78874 0.49879 0.03511  -0.04263 -0.10243 189 GLN A CA  
1459 C C   . GLN A 190 ? 0.76766 0.82309 0.54290 0.03902  -0.06393 -0.11585 189 GLN A C   
1460 O O   . GLN A 190 ? 0.78788 0.83826 0.53072 0.04646  -0.07026 -0.12643 189 GLN A O   
1461 C CB  . GLN A 190 ? 0.71657 0.81013 0.47556 0.04214  -0.02825 -0.10431 189 GLN A CB  
1462 C CG  . GLN A 190 ? 0.70511 0.80037 0.44865 0.05557  -0.02318 -0.12145 189 GLN A CG  
1463 C CD  . GLN A 190 ? 0.71226 0.83104 0.43290 0.06240  -0.00590 -0.11944 189 GLN A CD  
1464 O OE1 . GLN A 190 ? 0.70326 0.83934 0.43073 0.05483  0.00585  -0.10305 189 GLN A OE1 
1465 N NE2 . GLN A 190 ? 0.69064 0.81034 0.38411 0.07718  -0.00462 -0.13555 189 GLN A NE2 
1466 N N   . THR A 191 ? 0.74780 0.79046 0.54999 0.03365  -0.07594 -0.11466 190 THR A N   
1467 C CA  . THR A 191 ? 0.79863 0.81881 0.59749 0.03487  -0.09918 -0.12537 190 THR A CA  
1468 C C   . THR A 191 ? 0.85342 0.86422 0.67233 0.03718  -0.10211 -0.13313 190 THR A C   
1469 O O   . THR A 191 ? 0.75563 0.77830 0.58942 0.03803  -0.08590 -0.13022 190 THR A O   
1470 C CB  . THR A 191 ? 0.77794 0.79189 0.59427 0.02379  -0.11576 -0.11235 190 THR A CB  
1471 O OG1 . THR A 191 ? 0.79752 0.82244 0.65055 0.01563  -0.10718 -0.09631 190 THR A OG1 
1472 C CG2 . THR A 191 ? 0.83131 0.85111 0.62509 0.02226  -0.11682 -0.10596 190 THR A CG2 
1473 N N   . ALA A 192 ? 0.82781 0.81578 0.64709 0.03755  -0.12487 -0.14244 191 ALA A N   
1474 C CA  . ALA A 192 ? 0.80526 0.78100 0.64530 0.03850  -0.13198 -0.14839 191 ALA A CA  
1475 C C   . ALA A 192 ? 0.77295 0.75744 0.65463 0.02585  -0.13028 -0.12915 191 ALA A C   
1476 O O   . ALA A 192 ? 0.74521 0.72517 0.64425 0.01622  -0.14519 -0.11814 191 ALA A O   
1477 C CB  . ALA A 192 ? 0.81925 0.76517 0.64752 0.04153  -0.15982 -0.16292 191 ALA A CB  
1478 N N   . GLN A 193 ? 0.75284 0.75127 0.65031 0.02625  -0.11204 -0.12438 192 GLN A N   
1479 C CA  . GLN A 193 ? 0.71599 0.72393 0.64886 0.01646  -0.10780 -0.10733 192 GLN A CA  
1480 C C   . GLN A 193 ? 0.72411 0.72815 0.67202 0.01870  -0.10619 -0.11158 192 GLN A C   
1481 O O   . GLN A 193 ? 0.70905 0.71944 0.64663 0.02628  -0.09199 -0.11943 192 GLN A O   
1482 C CB  . GLN A 193 ? 0.67517 0.70446 0.61116 0.01365  -0.08663 -0.09467 192 GLN A CB  
1483 C CG  . GLN A 193 ? 0.67329 0.70706 0.59680 0.01125  -0.08780 -0.08841 192 GLN A CG  
1484 C CD  . GLN A 193 ? 0.61335 0.66418 0.54485 0.00796  -0.06993 -0.07482 192 GLN A CD  
1485 O OE1 . GLN A 193 ? 0.55456 0.61143 0.51144 0.00276  -0.06700 -0.06241 192 GLN A OE1 
1486 N NE2 . GLN A 193 ? 0.61092 0.66943 0.52032 0.01145  -0.05816 -0.07677 192 GLN A NE2 
1487 N N   . ALA A 194 ? 0.72083 0.71584 0.69490 0.01160  -0.12125 -0.10467 193 ALA A N   
1488 C CA  . ALA A 194 ? 0.74742 0.73745 0.73875 0.01213  -0.12278 -0.10609 193 ALA A CA  
1489 C C   . ALA A 194 ? 0.74102 0.74586 0.76439 0.00193  -0.11646 -0.08558 193 ALA A C   
1490 O O   . ALA A 194 ? 0.72766 0.73622 0.76880 -0.00665 -0.12468 -0.07157 193 ALA A O   
1491 C CB  . ALA A 194 ? 0.77713 0.74047 0.77038 0.01322  -0.14886 -0.11635 193 ALA A CB  
1492 N N   . ALA A 195 ? 0.72063 0.73520 0.75093 0.00343  -0.10176 -0.08331 194 ALA A N   
1493 C CA  . ALA A 195 ? 0.66102 0.68784 0.71863 -0.00472 -0.09667 -0.06540 194 ALA A CA  
1494 C C   . ALA A 195 ? 0.72274 0.73725 0.80391 -0.01040 -0.11636 -0.06051 194 ALA A C   
1495 O O   . ALA A 195 ? 0.77675 0.77166 0.85226 -0.00595 -0.13052 -0.07391 194 ALA A O   
1496 C CB  . ALA A 195 ? 0.60572 0.64470 0.66059 -0.00174 -0.07694 -0.06488 194 ALA A CB  
1497 N N   . GLY A 196 ? 0.65430 0.68065 0.76244 -0.01979 -0.11739 -0.04055 195 GLY A N   
1498 C CA  . GLY A 196 ? 0.62147 0.63967 0.75645 -0.02764 -0.13625 -0.03078 195 GLY A CA  
1499 C C   . GLY A 196 ? 0.58872 0.60407 0.73062 -0.02637 -0.13368 -0.03179 195 GLY A C   
1500 O O   . GLY A 196 ? 0.56215 0.57852 0.68663 -0.01832 -0.12006 -0.04335 195 GLY A O   
1501 N N   . THR A 197 ? 0.57187 0.58475 0.74198 -0.03533 -0.14809 -0.01742 196 THR A N   
1502 C CA  . THR A 197 ? 0.54605 0.55573 0.72643 -0.03571 -0.14871 -0.01520 196 THR A CA  
1503 C C   . THR A 197 ? 0.54613 0.57860 0.72217 -0.03416 -0.12338 -0.00776 196 THR A C   
1504 O O   . THR A 197 ? 0.54466 0.59815 0.72859 -0.03866 -0.11134 0.00825  196 THR A O   
1505 C CB  . THR A 197 ? 0.54344 0.54958 0.75761 -0.04783 -0.16888 0.00377  196 THR A CB  
1506 O OG1 . THR A 197 ? 0.56460 0.54609 0.78193 -0.05004 -0.19542 -0.00366 196 THR A OG1 
1507 C CG2 . THR A 197 ? 0.57163 0.57205 0.79641 -0.04840 -0.17202 0.00634  196 THR A CG2 
1508 N N   . ASP A 198 ? 0.53660 0.56444 0.69964 -0.02697 -0.11591 -0.01977 197 ASP A N   
1509 C CA  . ASP A 198 ? 0.55916 0.60448 0.71538 -0.02554 -0.09479 -0.01486 197 ASP A CA  
1510 C C   . ASP A 198 ? 0.57192 0.62286 0.75039 -0.03306 -0.09889 0.00234  197 ASP A C   
1511 O O   . ASP A 198 ? 0.57209 0.61222 0.75582 -0.03170 -0.10694 -0.00172 197 ASP A O   
1512 C CB  . ASP A 198 ? 0.56245 0.60240 0.69722 -0.01537 -0.08619 -0.03357 197 ASP A CB  
1513 C CG  . ASP A 198 ? 0.59226 0.64900 0.71586 -0.01438 -0.06518 -0.02996 197 ASP A CG  
1514 O OD1 . ASP A 198 ? 0.63896 0.69486 0.74995 -0.00789 -0.05824 -0.04127 197 ASP A OD1 
1515 O OD2 . ASP A 198 ? 0.59509 0.66577 0.72236 -0.01955 -0.05607 -0.01589 197 ASP A OD2 
1516 N N   . THR A 199 ? 0.56212 0.63134 0.75410 -0.04042 -0.09307 0.02262  198 THR A N   
1517 C CA  . THR A 199 ? 0.57648 0.65550 0.78831 -0.04800 -0.09501 0.04214  198 THR A CA  
1518 C C   . THR A 199 ? 0.55936 0.65175 0.75611 -0.04493 -0.07535 0.04407  198 THR A C   
1519 O O   . THR A 199 ? 0.54441 0.64153 0.71883 -0.03856 -0.05952 0.03428  198 THR A O   
1520 C CB  . THR A 199 ? 0.60296 0.69859 0.83818 -0.05689 -0.09808 0.06523  198 THR A CB  
1521 O OG1 . THR A 199 ? 0.63200 0.74530 0.85551 -0.05299 -0.07957 0.06746  198 THR A OG1 
1522 C CG2 . THR A 199 ? 0.62043 0.70045 0.87367 -0.06226 -0.12217 0.06525  198 THR A CG2 
1523 N N   . THR A 200 ? 0.55315 0.65029 0.76217 -0.05020 -0.07824 0.05757  199 THR A N   
1524 C CA  . THR A 200 ? 0.52879 0.63499 0.72301 -0.04808 -0.06381 0.05919  199 THR A CA  
1525 C C   . THR A 200 ? 0.52226 0.65170 0.71416 -0.05037 -0.04848 0.07690  199 THR A C   
1526 O O   . THR A 200 ? 0.54793 0.69010 0.76040 -0.05667 -0.05230 0.09606  199 THR A O   
1527 C CB  . THR A 200 ? 0.52582 0.62424 0.73228 -0.05182 -0.07566 0.06414  199 THR A CB  
1528 O OG1 . THR A 200 ? 0.55970 0.63581 0.77130 -0.04804 -0.09146 0.04813  199 THR A OG1 
1529 C CG2 . THR A 200 ? 0.49134 0.59519 0.67949 -0.04892 -0.06324 0.06172  199 THR A CG2 
1530 N N   . ILE A 201 ? 0.49398 0.62902 0.66080 -0.04472 -0.03147 0.07069  200 ILE A N   
1531 C CA  . ILE A 201 ? 0.48968 0.64413 0.64732 -0.04345 -0.01526 0.08356  200 ILE A CA  
1532 C C   . ILE A 201 ? 0.47133 0.63458 0.63373 -0.04869 -0.01623 0.09975  200 ILE A C   
1533 O O   . ILE A 201 ? 0.44328 0.60130 0.58860 -0.04727 -0.01307 0.09408  200 ILE A O   
1534 C CB  . ILE A 201 ? 0.46811 0.62008 0.59523 -0.03523 0.00032  0.06926  200 ILE A CB  
1535 C CG1 . ILE A 201 ? 0.48222 0.62232 0.60442 -0.03116 -0.00179 0.05217  200 ILE A CG1 
1536 C CG2 . ILE A 201 ? 0.47593 0.64543 0.59348 -0.03104 0.01633  0.08006  200 ILE A CG2 
1537 C CD1 . ILE A 201 ? 0.46444 0.59765 0.55923 -0.02505 0.00899  0.03718  200 ILE A CD1 
1538 N N   . THR A 202 ? 0.47193 0.64987 0.65843 -0.05549 -0.02127 0.12171  201 THR A N   
1539 C CA  . THR A 202 ? 0.45386 0.64001 0.64934 -0.06232 -0.02568 0.13987  201 THR A CA  
1540 C C   . THR A 202 ? 0.43925 0.63781 0.60694 -0.05763 -0.00811 0.14372  201 THR A C   
1541 O O   . THR A 202 ? 0.42797 0.62198 0.58639 -0.05993 -0.01103 0.14508  201 THR A O   
1542 C CB  . THR A 202 ? 0.48739 0.69041 0.71578 -0.07120 -0.03359 0.16556  201 THR A CB  
1543 O OG1 . THR A 202 ? 0.48965 0.67895 0.74011 -0.07474 -0.05033 0.15998  201 THR A OG1 
1544 C CG2 . THR A 202 ? 0.47018 0.67698 0.71292 -0.08032 -0.04384 0.18437  201 THR A CG2 
1545 N N   . VAL A 203 ? 0.41643 0.62965 0.56979 -0.05035 0.00934  0.14527  202 VAL A N   
1546 C CA  . VAL A 203 ? 0.45174 0.67449 0.57487 -0.04400 0.02572  0.14740  202 VAL A CA  
1547 C C   . VAL A 203 ? 0.44663 0.64780 0.54120 -0.04059 0.02543  0.12630  202 VAL A C   
1548 O O   . VAL A 203 ? 0.44196 0.64366 0.51538 -0.04009 0.02926  0.12877  202 VAL A O   
1549 C CB  . VAL A 203 ? 0.46545 0.70467 0.57849 -0.03410 0.04396  0.14966  202 VAL A CB  
1550 C CG1 . VAL A 203 ? 0.46904 0.69117 0.56722 -0.02654 0.04755  0.12635  202 VAL A CG1 
1551 C CG2 . VAL A 203 ? 0.48665 0.73948 0.57131 -0.02707 0.06009  0.15694  202 VAL A CG2 
1552 N N   . ASN A 204 ? 0.44277 0.62565 0.53711 -0.03888 0.01984  0.10670  203 ASN A N   
1553 C CA  . ASN A 204 ? 0.44650 0.61175 0.51871 -0.03669 0.01881  0.08891  203 ASN A CA  
1554 C C   . ASN A 204 ? 0.45253 0.61079 0.53426 -0.04357 0.00527  0.09194  203 ASN A C   
1555 O O   . ASN A 204 ? 0.45844 0.61064 0.52112 -0.04352 0.00570  0.08751  203 ASN A O   
1556 C CB  . ASN A 204 ? 0.45532 0.60718 0.52692 -0.03303 0.01737  0.07002  203 ASN A CB  
1557 C CG  . ASN A 204 ? 0.45332 0.60791 0.50822 -0.02528 0.03098  0.06426  203 ASN A CG  
1558 O OD1 . ASN A 204 ? 0.44906 0.61653 0.49556 -0.02128 0.04190  0.07414  203 ASN A OD1 
1559 N ND2 . ASN A 204 ? 0.46158 0.60475 0.51168 -0.02233 0.03057  0.04877  203 ASN A ND2 
1560 N N   . VAL A 205 ? 0.43158 0.58921 0.54326 -0.04952 -0.00837 0.09961  204 VAL A N   
1561 C CA  . VAL A 205 ? 0.44103 0.59184 0.56457 -0.05532 -0.02222 0.10421  204 VAL A CA  
1562 C C   . VAL A 205 ? 0.46354 0.62719 0.57874 -0.05957 -0.01915 0.12296  204 VAL A C   
1563 O O   . VAL A 205 ? 0.44242 0.60044 0.54987 -0.06192 -0.02460 0.12306  204 VAL A O   
1564 C CB  . VAL A 205 ? 0.43886 0.58327 0.59597 -0.06014 -0.03915 0.10861  204 VAL A CB  
1565 C CG1 . VAL A 205 ? 0.44376 0.57952 0.61449 -0.06497 -0.05436 0.11348  204 VAL A CG1 
1566 C CG2 . VAL A 205 ? 0.43397 0.56497 0.59389 -0.05469 -0.04207 0.08871  204 VAL A CG2 
1567 N N   . LEU A 206 ? 0.42087 0.60363 0.53737 -0.06027 -0.01019 0.14003  205 LEU A N   
1568 C CA  . LEU A 206 ? 0.45424 0.65205 0.55847 -0.06293 -0.00491 0.15851  205 LEU A CA  
1569 C C   . LEU A 206 ? 0.44931 0.64211 0.51292 -0.05632 0.00613  0.14690  205 LEU A C   
1570 O O   . LEU A 206 ? 0.43999 0.63238 0.48966 -0.05949 0.00280  0.15330  205 LEU A O   
1571 C CB  . LEU A 206 ? 0.43773 0.66106 0.55205 -0.06320 0.00496  0.17952  205 LEU A CB  
1572 C CG  . LEU A 206 ? 0.41780 0.64774 0.57445 -0.07305 -0.00939 0.19751  205 LEU A CG  
1573 C CD1 . LEU A 206 ? 0.43545 0.69410 0.60467 -0.07304 0.00163  0.21884  205 LEU A CD1 
1574 C CD2 . LEU A 206 ? 0.45605 0.68322 0.62641 -0.08302 -0.02485 0.21243  205 LEU A CD2 
1575 N N   . ALA A 207 ? 0.42940 0.61674 0.47338 -0.04757 0.01762  0.13023  206 ALA A N   
1576 C CA  . ALA A 207 ? 0.47473 0.65223 0.48031 -0.04170 0.02509  0.11737  206 ALA A CA  
1577 C C   . ALA A 207 ? 0.51756 0.67713 0.52052 -0.04633 0.01220  0.10648  206 ALA A C   
1578 O O   . ALA A 207 ? 0.52245 0.67677 0.50058 -0.04698 0.01114  0.10576  206 ALA A O   
1579 C CB  . ALA A 207 ? 0.48653 0.65850 0.47688 -0.03224 0.03678  0.10159  206 ALA A CB  
1580 N N   . TRP A 208 ? 0.45745 0.60816 0.48581 -0.04902 0.00196  0.09825  207 TRP A N   
1581 C CA  . TRP A 208 ? 0.50471 0.64232 0.53610 -0.05214 -0.00954 0.08920  207 TRP A CA  
1582 C C   . TRP A 208 ? 0.50607 0.64695 0.54684 -0.05935 -0.02093 0.10449  207 TRP A C   
1583 O O   . TRP A 208 ? 0.51724 0.65122 0.54740 -0.06171 -0.02726 0.10182  207 TRP A O   
1584 C CB  . TRP A 208 ? 0.48346 0.61345 0.53936 -0.05084 -0.01600 0.07734  207 TRP A CB  
1585 C CG  . TRP A 208 ? 0.49385 0.61423 0.55811 -0.05198 -0.02643 0.06854  207 TRP A CG  
1586 C CD1 . TRP A 208 ? 0.49206 0.60584 0.54089 -0.05037 -0.02484 0.05661  207 TRP A CD1 
1587 C CD2 . TRP A 208 ? 0.47408 0.59114 0.56665 -0.05432 -0.04046 0.07157  207 TRP A CD2 
1588 N NE1 . TRP A 208 ? 0.49722 0.60736 0.56435 -0.05129 -0.03560 0.05316  207 TRP A NE1 
1589 C CE2 . TRP A 208 ? 0.49257 0.60361 0.58569 -0.05269 -0.04506 0.06113  207 TRP A CE2 
1590 C CE3 . TRP A 208 ? 0.48716 0.60515 0.60585 -0.05756 -0.05059 0.08270  207 TRP A CE3 
1591 C CZ2 . TRP A 208 ? 0.50537 0.61223 0.62345 -0.05212 -0.05780 0.06037  207 TRP A CZ2 
1592 C CZ3 . TRP A 208 ? 0.49135 0.60122 0.63332 -0.05765 -0.06505 0.08103  207 TRP A CZ3 
1593 C CH2 . TRP A 208 ? 0.51258 0.61739 0.65373 -0.05393 -0.06775 0.06936  207 TRP A CH2 
1594 N N   . LEU A 209 ? 0.47722 0.62897 0.53907 -0.06373 -0.02479 0.12223  208 LEU A N   
1595 C CA  . LEU A 209 ? 0.49924 0.65511 0.56976 -0.07127 -0.03576 0.13989  208 LEU A CA  
1596 C C   . LEU A 209 ? 0.52496 0.68831 0.56119 -0.07146 -0.02812 0.14852  208 LEU A C   
1597 O O   . LEU A 209 ? 0.50792 0.66844 0.53847 -0.07646 -0.03749 0.15532  208 LEU A O   
1598 C CB  . LEU A 209 ? 0.48942 0.65558 0.59125 -0.07697 -0.04222 0.15906  208 LEU A CB  
1599 C CG  . LEU A 209 ? 0.48619 0.64052 0.62185 -0.07757 -0.05504 0.15146  208 LEU A CG  
1600 C CD1 . LEU A 209 ? 0.50151 0.66405 0.66774 -0.08506 -0.06435 0.17269  208 LEU A CD1 
1601 C CD2 . LEU A 209 ? 0.49227 0.63066 0.63716 -0.07748 -0.06881 0.14118  208 LEU A CD2 
1602 N N   . TYR A 210 ? 0.52603 0.69855 0.53820 -0.06519 -0.01160 0.14828  209 TYR A N   
1603 C CA  . TYR A 210 ? 0.53629 0.71283 0.50918 -0.06251 -0.00355 0.15244  209 TYR A CA  
1604 C C   . TYR A 210 ? 0.55702 0.71382 0.50402 -0.06125 -0.00832 0.13446  209 TYR A C   
1605 O O   . TYR A 210 ? 0.55031 0.70412 0.47448 -0.06419 -0.01342 0.13941  209 TYR A O   
1606 C CB  . TYR A 210 ? 0.52667 0.71607 0.47965 -0.05308 0.01588  0.15342  209 TYR A CB  
1607 C CG  . TYR A 210 ? 0.52292 0.73865 0.49221 -0.05528 0.02178  0.17883  209 TYR A CG  
1608 C CD1 . TYR A 210 ? 0.54465 0.77372 0.50294 -0.05969 0.02066  0.19916  209 TYR A CD1 
1609 C CD2 . TYR A 210 ? 0.51612 0.74473 0.51262 -0.05371 0.02769  0.18426  209 TYR A CD2 
1610 C CE1 . TYR A 210 ? 0.54034 0.79667 0.51571 -0.06263 0.02623  0.22535  209 TYR A CE1 
1611 C CE2 . TYR A 210 ? 0.50132 0.75655 0.51668 -0.05703 0.03217  0.21021  209 TYR A CE2 
1612 C CZ  . TYR A 210 ? 0.53176 0.80169 0.53707 -0.06154 0.03194  0.23124  209 TYR A CZ  
1613 O OH  . TYR A 210 ? 0.51714 0.81665 0.54306 -0.06567 0.03669  0.25990  209 TYR A OH  
1614 N N   . ALA A 211 ? 0.53280 0.67658 0.48351 -0.05765 -0.00773 0.11487  210 ALA A N   
1615 C CA  . ALA A 211 ? 0.58674 0.71332 0.52046 -0.05841 -0.01443 0.10006  210 ALA A CA  
1616 C C   . ALA A 211 ? 0.57757 0.70109 0.53041 -0.06672 -0.03144 0.10608  210 ALA A C   
1617 O O   . ALA A 211 ? 0.59089 0.70571 0.52533 -0.06995 -0.03916 0.10377  210 ALA A O   
1618 C CB  . ALA A 211 ? 0.56982 0.68692 0.51044 -0.05406 -0.01088 0.08147  210 ALA A CB  
1619 N N   . ALA A 212 ? 0.56688 0.69617 0.55731 -0.06997 -0.03881 0.11369  211 ALA A N   
1620 C CA  . ALA A 212 ? 0.57270 0.69938 0.58465 -0.07634 -0.05532 0.12054  211 ALA A CA  
1621 C C   . ALA A 212 ? 0.61418 0.74620 0.60990 -0.08233 -0.06088 0.13841  211 ALA A C   
1622 O O   . ALA A 212 ? 0.62098 0.74685 0.60987 -0.08661 -0.07187 0.13935  211 ALA A O   
1623 C CB  . ALA A 212 ? 0.55857 0.68763 0.61167 -0.07717 -0.06258 0.12502  211 ALA A CB  
1624 N N   . VAL A 213 ? 0.58177 0.72704 0.57195 -0.08290 -0.05359 0.15418  212 VAL A N   
1625 C CA  . VAL A 213 ? 0.60461 0.75792 0.57559 -0.08799 -0.05678 0.17297  212 VAL A CA  
1626 C C   . VAL A 213 ? 0.61185 0.75578 0.53731 -0.08573 -0.05448 0.16369  212 VAL A C   
1627 O O   . VAL A 213 ? 0.61035 0.75069 0.52361 -0.09156 -0.06614 0.17121  212 VAL A O   
1628 C CB  . VAL A 213 ? 0.56764 0.74089 0.53765 -0.08727 -0.04519 0.19131  212 VAL A CB  
1629 C CG1 . VAL A 213 ? 0.58795 0.77136 0.52679 -0.09005 -0.04399 0.20884  212 VAL A CG1 
1630 C CG2 . VAL A 213 ? 0.57736 0.75766 0.59437 -0.09311 -0.05395 0.20521  212 VAL A CG2 
1631 N N   . ILE A 214 ? 0.61615 0.75402 0.51593 -0.07742 -0.04125 0.14715  213 ILE A N   
1632 C CA  . ILE A 214 ? 0.63608 0.76056 0.49048 -0.07470 -0.04066 0.13649  213 ILE A CA  
1633 C C   . ILE A 214 ? 0.64481 0.75403 0.50504 -0.08133 -0.05795 0.12856  213 ILE A C   
1634 O O   . ILE A 214 ? 0.66597 0.76681 0.49819 -0.08512 -0.06721 0.13042  213 ILE A O   
1635 C CB  . ILE A 214 ? 0.63842 0.75631 0.47007 -0.06409 -0.02505 0.11920  213 ILE A CB  
1636 C CG1 . ILE A 214 ? 0.63462 0.77025 0.45429 -0.05632 -0.00742 0.12932  213 ILE A CG1 
1637 C CG2 . ILE A 214 ? 0.67172 0.76861 0.46098 -0.06198 -0.02896 0.10439  213 ILE A CG2 
1638 C CD1 . ILE A 214 ? 0.64726 0.77896 0.45319 -0.04480 0.00821  0.11405  213 ILE A CD1 
1639 N N   . ASN A 215 ? 0.51520 0.81553 0.56329 -0.12407 -0.03885 0.09987  214 ASN A N   
1640 C CA  . ASN A 215 ? 0.53799 0.84150 0.60044 -0.12451 -0.03973 0.09604  214 ASN A CA  
1641 C C   . ASN A 215 ? 0.55145 0.86911 0.63437 -0.12058 -0.04838 0.11459  214 ASN A C   
1642 O O   . ASN A 215 ? 0.58987 0.90803 0.69024 -0.11807 -0.04822 0.11362  214 ASN A O   
1643 C CB  . ASN A 215 ? 0.53450 0.80525 0.59957 -0.12080 -0.03000 0.08411  214 ASN A CB  
1644 C CG  . ASN A 215 ? 0.54726 0.80670 0.59475 -0.12472 -0.02114 0.06488  214 ASN A CG  
1645 O OD1 . ASN A 215 ? 0.53805 0.80257 0.58701 -0.13051 -0.01813 0.05364  214 ASN A OD1 
1646 N ND2 . ASN A 215 ? 0.55579 0.80003 0.58733 -0.12159 -0.01650 0.06121  214 ASN A ND2 
1647 N N   . GLY A 216 ? 0.56005 0.88881 0.64184 -0.11941 -0.05492 0.13207  215 GLY A N   
1648 C CA  . GLY A 216 ? 0.57235 0.91602 0.67088 -0.11475 -0.06338 0.15186  215 GLY A CA  
1649 C C   . GLY A 216 ? 0.61624 0.93308 0.72657 -0.10704 -0.06137 0.16540  215 GLY A C   
1650 O O   . GLY A 216 ? 0.61847 0.94370 0.73738 -0.10293 -0.06755 0.18545  215 GLY A O   
1651 N N   . ASP A 217 ? 0.65564 0.93935 0.76522 -0.10511 -0.05272 0.15517  216 ASP A N   
1652 C CA  . ASP A 217 ? 0.65447 0.90957 0.77229 -0.09990 -0.04989 0.16494  216 ASP A CA  
1653 C C   . ASP A 217 ? 0.65273 0.90706 0.75978 -0.10451 -0.05210 0.17625  216 ASP A C   
1654 O O   . ASP A 217 ? 0.67016 0.92247 0.76239 -0.11003 -0.04931 0.16711  216 ASP A O   
1655 C CB  . ASP A 217 ? 0.71763 0.94003 0.83322 -0.09834 -0.04058 0.14918  216 ASP A CB  
1656 C CG  . ASP A 217 ? 0.77902 0.99651 0.90929 -0.09299 -0.03618 0.14180  216 ASP A CG  
1657 O OD1 . ASP A 217 ? 0.78577 1.02441 0.91738 -0.09565 -0.03707 0.13347  216 ASP A OD1 
1658 O OD2 . ASP A 217 ? 0.80649 0.99875 0.94683 -0.08700 -0.03090 0.14344  216 ASP A OD2 
1659 N N   . ARG A 218 ? 0.64964 0.90568 0.76484 -0.10193 -0.05639 0.19687  217 ARG A N   
1660 C CA  . ARG A 218 ? 0.66234 0.91732 0.76802 -0.10806 -0.05724 0.20875  217 ARG A CA  
1661 C C   . ARG A 218 ? 0.65965 0.88966 0.77572 -0.10493 -0.05598 0.22624  217 ARG A C   
1662 O O   . ARG A 218 ? 0.67427 0.90448 0.78422 -0.11081 -0.05667 0.23979  217 ARG A O   
1663 C CB  . ARG A 218 ? 0.69815 0.98977 0.79322 -0.11243 -0.06387 0.21822  217 ARG A CB  
1664 C CG  . ARG A 218 ? 0.73868 1.04620 0.84233 -0.10691 -0.07142 0.24051  217 ARG A CG  
1665 C CD  . ARG A 218 ? 0.81407 1.13417 0.90510 -0.11297 -0.07393 0.25876  217 ARG A CD  
1666 N NE  . ARG A 218 ? 0.89159 1.22563 0.98803 -0.10670 -0.08144 0.28307  217 ARG A NE  
1667 C CZ  . ARG A 218 ? 0.92356 1.23410 1.03304 -0.09917 -0.08056 0.30153  217 ARG A CZ  
1668 N NH1 . ARG A 218 ? 0.90547 1.17669 1.02364 -0.09836 -0.07234 0.29671  217 ARG A NH1 
1669 N NH2 . ARG A 218 ? 0.93564 1.26169 1.04833 -0.09199 -0.08792 0.32543  217 ARG A NH2 
1670 N N   . TRP A 219 ? 0.66338 0.86992 0.79444 -0.09632 -0.05259 0.22587  218 TRP A N   
1671 C CA  . TRP A 219 ? 0.65765 0.83571 0.79790 -0.09254 -0.04968 0.24175  218 TRP A CA  
1672 C C   . TRP A 219 ? 0.66315 0.81426 0.79368 -0.10302 -0.04439 0.23811  218 TRP A C   
1673 O O   . TRP A 219 ? 0.67121 0.80463 0.80331 -0.10561 -0.04271 0.25375  218 TRP A O   
1674 C CB  . TRP A 219 ? 0.65298 0.80967 0.81079 -0.08057 -0.04479 0.23860  218 TRP A CB  
1675 C CG  . TRP A 219 ? 0.64149 0.77647 0.79619 -0.08206 -0.03730 0.21532  218 TRP A CG  
1676 C CD1 . TRP A 219 ? 0.63182 0.77913 0.78748 -0.07996 -0.03611 0.19888  218 TRP A CD1 
1677 C CD2 . TRP A 219 ? 0.68610 0.78282 0.83443 -0.08675 -0.02981 0.20634  218 TRP A CD2 
1678 N NE1 . TRP A 219 ? 0.63375 0.75233 0.78290 -0.08182 -0.02813 0.18175  218 TRP A NE1 
1679 C CE2 . TRP A 219 ? 0.67354 0.76225 0.81773 -0.08599 -0.02489 0.18551  218 TRP A CE2 
1680 C CE3 . TRP A 219 ? 0.72291 0.79122 0.86751 -0.09282 -0.02667 0.21355  218 TRP A CE3 
1681 C CZ2 . TRP A 219 ? 0.70446 0.76000 0.83953 -0.09011 -0.01812 0.17224  218 TRP A CZ2 
1682 C CZ3 . TRP A 219 ? 0.75110 0.78706 0.88797 -0.09844 -0.02009 0.19860  218 TRP A CZ3 
1683 C CH2 . TRP A 219 ? 0.73412 0.76499 0.86564 -0.09655 -0.01645 0.17841  218 TRP A CH2 
1684 N N   . PHE A 220 ? 0.65259 0.80084 0.77320 -0.10943 -0.04181 0.21820  219 PHE A N   
1685 C CA  . PHE A 220 ? 0.65738 0.78526 0.77019 -0.11992 -0.03815 0.21253  219 PHE A CA  
1686 C C   . PHE A 220 ? 0.66302 0.81183 0.76734 -0.13091 -0.04090 0.22155  219 PHE A C   
1687 O O   . PHE A 220 ? 0.64329 0.78076 0.74357 -0.14135 -0.03847 0.21825  219 PHE A O   
1688 C CB  . PHE A 220 ? 0.60799 0.72925 0.71306 -0.12102 -0.03548 0.18958  219 PHE A CB  
1689 C CG  . PHE A 220 ? 0.60969 0.76106 0.70717 -0.11939 -0.03821 0.17961  219 PHE A CG  
1690 C CD1 . PHE A 220 ? 0.61451 0.77351 0.71635 -0.11108 -0.03805 0.17348  219 PHE A CD1 
1691 C CD2 . PHE A 220 ? 0.59677 0.76848 0.68351 -0.12650 -0.03987 0.17585  219 PHE A CD2 
1692 C CE1 . PHE A 220 ? 0.59238 0.77483 0.68585 -0.11119 -0.03930 0.16313  219 PHE A CE1 
1693 C CE2 . PHE A 220 ? 0.58443 0.77942 0.66303 -0.12430 -0.04063 0.16592  219 PHE A CE2 
1694 C CZ  . PHE A 220 ? 0.57590 0.77426 0.65677 -0.11728 -0.04023 0.15921  219 PHE A CZ  
1695 N N   . LEU A 221 ? 0.64279 0.82339 0.74411 -0.12970 -0.04562 0.23225  220 LEU A N   
1696 C CA  . LEU A 221 ? 0.66817 0.87017 0.76052 -0.13989 -0.04662 0.24136  220 LEU A CA  
1697 C C   . LEU A 221 ? 0.70153 0.88691 0.79769 -0.14457 -0.04494 0.26339  220 LEU A C   
1698 O O   . LEU A 221 ? 0.70595 0.88279 0.80894 -0.13607 -0.04652 0.27902  220 LEU A O   
1699 C CB  . LEU A 221 ? 0.66454 0.90510 0.74874 -0.13746 -0.05139 0.24385  220 LEU A CB  
1700 C CG  . LEU A 221 ? 0.63299 0.88983 0.71075 -0.13456 -0.05161 0.22237  220 LEU A CG  
1701 C CD1 . LEU A 221 ? 0.63242 0.92475 0.70063 -0.13405 -0.05589 0.22530  220 LEU A CD1 
1702 C CD2 . LEU A 221 ? 0.61603 0.87201 0.68743 -0.14097 -0.04736 0.20816  220 LEU A CD2 
1703 N N   . ASN A 222 ? 0.70614 0.88739 0.79865 -0.15796 -0.04138 0.26521  221 ASN A N   
1704 C CA  . ASN A 222 ? 0.75939 0.91974 0.85433 -0.16560 -0.03770 0.28474  221 ASN A CA  
1705 C C   . ASN A 222 ? 0.76781 0.95636 0.85395 -0.17678 -0.03705 0.29733  221 ASN A C   
1706 O O   . ASN A 222 ? 0.75771 0.98129 0.83627 -0.17820 -0.03895 0.28927  221 ASN A O   
1707 C CB  . ASN A 222 ? 0.75890 0.88276 0.85866 -0.17485 -0.03225 0.27532  221 ASN A CB  
1708 C CG  . ASN A 222 ? 0.73247 0.87207 0.82857 -0.18651 -0.03208 0.25721  221 ASN A CG  
1709 O OD1 . ASN A 222 ? 0.71686 0.89302 0.80757 -0.18758 -0.03440 0.25323  221 ASN A OD1 
1710 N ND2 . ASN A 222 ? 0.74020 0.85266 0.83905 -0.19492 -0.02922 0.24600  221 ASN A ND2 
1711 N N   . ARG A 223 ? 0.82251 0.99325 0.90909 -0.18485 -0.03282 0.31723  222 ARG A N   
1712 C CA  . ARG A 223 ? 0.80550 0.99861 0.88361 -0.19702 -0.03004 0.33203  222 ARG A CA  
1713 C C   . ARG A 223 ? 0.78788 0.98318 0.86846 -0.21554 -0.02444 0.32223  222 ARG A C   
1714 O O   . ARG A 223 ? 0.83634 1.04973 0.91206 -0.22791 -0.02014 0.33380  222 ARG A O   
1715 C CB  . ARG A 223 ? 0.86485 1.03699 0.94099 -0.19664 -0.02742 0.36125  222 ARG A CB  
1716 C CG  . ARG A 223 ? 0.89947 1.08665 0.97073 -0.17999 -0.03445 0.37717  222 ARG A CG  
1717 C CD  . ARG A 223 ? 0.96820 1.13227 1.05169 -0.16281 -0.03812 0.37273  222 ARG A CD  
1718 N NE  . ARG A 223 ? 1.05741 1.18615 1.14642 -0.15581 -0.03515 0.39621  222 ARG A NE  
1719 C CZ  . ARG A 223 ? 1.06326 1.16397 1.16537 -0.14126 -0.03505 0.39553  222 ARG A CZ  
1720 N NH1 . ARG A 223 ? 0.99660 1.09976 1.10720 -0.13371 -0.03751 0.37253  222 ARG A NH1 
1721 N NH2 . ARG A 223 ? 1.04448 1.11290 1.15113 -0.13357 -0.03122 0.41899  222 ARG A NH2 
1722 N N   . PHE A 224 ? 0.76748 0.94752 0.85538 -0.21807 -0.02446 0.30154  223 PHE A N   
1723 C CA  . PHE A 224 ? 0.73146 0.91382 0.82409 -0.23606 -0.02070 0.29203  223 PHE A CA  
1724 C C   . PHE A 224 ? 0.70234 0.92753 0.79386 -0.23614 -0.02311 0.27559  223 PHE A C   
1725 O O   . PHE A 224 ? 0.69169 0.93678 0.77779 -0.22222 -0.02706 0.26787  223 PHE A O   
1726 C CB  . PHE A 224 ? 0.73486 0.87795 0.83403 -0.23969 -0.02000 0.27841  223 PHE A CB  
1727 C CG  . PHE A 224 ? 0.76488 0.86051 0.86579 -0.23881 -0.01554 0.29231  223 PHE A CG  
1728 C CD1 . PHE A 224 ? 0.80386 0.88060 0.90519 -0.21960 -0.01751 0.29622  223 PHE A CD1 
1729 C CD2 . PHE A 224 ? 0.76978 0.83911 0.87305 -0.25717 -0.00850 0.30099  223 PHE A CD2 
1730 C CE1 . PHE A 224 ? 0.81154 0.84427 0.91600 -0.21612 -0.01238 0.30951  223 PHE A CE1 
1731 C CE2 . PHE A 224 ? 0.78672 0.80751 0.89084 -0.25513 -0.00276 0.31375  223 PHE A CE2 
1732 C CZ  . PHE A 224 ? 0.79328 0.79572 0.89821 -0.23327 -0.00461 0.31839  223 PHE A CZ  
1733 N N   . THR A 225 ? 0.68410 0.92330 0.78176 -0.25234 -0.02013 0.27021  224 THR A N   
1734 C CA  . THR A 225 ? 0.65615 0.93172 0.75674 -0.25201 -0.02204 0.25305  224 THR A CA  
1735 C C   . THR A 225 ? 0.67114 0.93939 0.78226 -0.26690 -0.02245 0.24143  224 THR A C   
1736 O O   . THR A 225 ? 0.67032 0.90488 0.78471 -0.27907 -0.02028 0.24603  224 THR A O   
1737 C CB  . THR A 225 ? 0.64452 0.96372 0.74247 -0.25585 -0.01762 0.26108  224 THR A CB  
1738 O OG1 . THR A 225 ? 0.61589 0.96877 0.71684 -0.25023 -0.01899 0.24385  224 THR A OG1 
1739 C CG2 . THR A 225 ? 0.63403 0.95733 0.73882 -0.27752 -0.01075 0.27446  224 THR A CG2 
1740 N N   . THR A 226 ? 0.65001 0.94984 0.76607 -0.26586 -0.02527 0.22607  225 THR A N   
1741 C CA  . THR A 226 ? 0.65335 0.95484 0.77957 -0.27967 -0.02782 0.21405  225 THR A CA  
1742 C C   . THR A 226 ? 0.62332 0.97619 0.75798 -0.27921 -0.02877 0.20577  225 THR A C   
1743 O O   . THR A 226 ? 0.60779 0.98898 0.73874 -0.26729 -0.02626 0.20789  225 THR A O   
1744 C CB  . THR A 226 ? 0.67860 0.94675 0.80006 -0.27221 -0.03375 0.19883  225 THR A CB  
1745 O OG1 . THR A 226 ? 0.71192 0.98089 0.84101 -0.28835 -0.03700 0.18779  225 THR A OG1 
1746 C CG2 . THR A 226 ? 0.63572 0.91797 0.75032 -0.25070 -0.03804 0.18677  225 THR A CG2 
1747 N N   . THR A 227 ? 0.66821 1.03385 0.81449 -0.29233 -0.03221 0.19599  226 THR A N   
1748 C CA  . THR A 227 ? 0.63494 1.04964 0.79216 -0.28943 -0.03465 0.18673  226 THR A CA  
1749 C C   . THR A 227 ? 0.61591 1.02450 0.76918 -0.27673 -0.04382 0.16936  226 THR A C   
1750 O O   . THR A 227 ? 0.66046 1.02828 0.80433 -0.27609 -0.04778 0.16348  226 THR A O   
1751 C CB  . THR A 227 ? 0.62257 1.06661 0.79863 -0.31392 -0.03273 0.18915  226 THR A CB  
1752 O OG1 . THR A 227 ? 0.65014 1.07837 0.83057 -0.32677 -0.04030 0.17756  226 THR A OG1 
1753 C CG2 . THR A 227 ? 0.61059 1.04232 0.78713 -0.33135 -0.02319 0.20735  226 THR A CG2 
1754 N N   . LEU A 228 ? 0.56555 1.01487 0.72543 -0.26568 -0.04627 0.16177  227 LEU A N   
1755 C CA  . LEU A 228 ? 0.59117 1.03647 0.74494 -0.25078 -0.05450 0.14744  227 LEU A CA  
1756 C C   . LEU A 228 ? 0.61598 1.04951 0.77314 -0.26633 -0.06295 0.13871  227 LEU A C   
1757 O O   . LEU A 228 ? 0.62254 1.02424 0.76607 -0.25938 -0.06834 0.12948  227 LEU A O   
1758 C CB  . LEU A 228 ? 0.54240 1.03484 0.70422 -0.23552 -0.05450 0.14319  227 LEU A CB  
1759 C CG  . LEU A 228 ? 0.54688 1.03084 0.69647 -0.21205 -0.05934 0.13229  227 LEU A CG  
1760 C CD1 . LEU A 228 ? 0.54637 0.98306 0.67543 -0.20134 -0.05680 0.13172  227 LEU A CD1 
1761 C CD2 . LEU A 228 ? 0.54180 1.06658 0.69779 -0.19440 -0.05515 0.13124  227 LEU A CD2 
1762 N N   . ASN A 229 ? 0.60613 1.06504 0.78051 -0.28886 -0.06365 0.14082  228 ASN A N   
1763 C CA  . ASN A 229 ? 0.63065 1.07712 0.80707 -0.30789 -0.07148 0.13147  228 ASN A CA  
1764 C C   . ASN A 229 ? 0.70558 1.09157 0.86825 -0.31836 -0.06802 0.13301  228 ASN A C   
1765 O O   . ASN A 229 ? 0.74726 1.10291 0.89894 -0.32175 -0.07382 0.12161  228 ASN A O   
1766 C CB  . ASN A 229 ? 0.63639 1.12672 0.83645 -0.33203 -0.07213 0.13322  228 ASN A CB  
1767 C CG  . ASN A 229 ? 0.54136 1.09463 0.75820 -0.32094 -0.07668 0.13007  228 ASN A CG  
1768 O OD1 . ASN A 229 ? 0.54689 1.10997 0.75732 -0.29443 -0.07633 0.12936  228 ASN A OD1 
1769 N ND2 . ASN A 229 ? 0.48292 1.07927 0.72235 -0.34130 -0.08036 0.12808  228 ASN A ND2 
1770 N N   . ASP A 230 ? 0.79084 1.15868 0.95323 -0.32295 -0.05812 0.14742  229 ASP A N   
1771 C CA  . ASP A 230 ? 0.83436 1.14439 0.98499 -0.32873 -0.05350 0.15149  229 ASP A CA  
1772 C C   . ASP A 230 ? 0.87487 1.15121 1.00828 -0.30487 -0.05411 0.14811  229 ASP A C   
1773 O O   . ASP A 230 ? 0.93360 1.16230 1.05811 -0.30581 -0.05024 0.15056  229 ASP A O   
1774 C CB  . ASP A 230 ? 0.87081 1.17361 1.02601 -0.33904 -0.04311 0.17052  229 ASP A CB  
1775 C CG  . ASP A 230 ? 0.91809 1.24242 1.08939 -0.36776 -0.04018 0.17410  229 ASP A CG  
1776 O OD1 . ASP A 230 ? 0.91662 1.25073 1.09346 -0.37581 -0.03140 0.19034  229 ASP A OD1 
1777 O OD2 . ASP A 230 ? 0.93811 1.27144 1.11607 -0.38312 -0.04671 0.16060  229 ASP A OD2 
1778 N N   . PHE A 231 ? 0.74905 1.04799 0.87832 -0.28378 -0.05798 0.14232  230 PHE A N   
1779 C CA  . PHE A 231 ? 0.73456 1.00348 0.84796 -0.26410 -0.05946 0.13508  230 PHE A CA  
1780 C C   . PHE A 231 ? 0.73907 1.00529 0.84490 -0.26186 -0.06777 0.11856  230 PHE A C   
1781 O O   . PHE A 231 ? 0.74769 0.97568 0.83936 -0.25535 -0.06791 0.11122  230 PHE A O   
1782 C CB  . PHE A 231 ? 0.67084 0.95867 0.78073 -0.24225 -0.05700 0.13898  230 PHE A CB  
1783 C CG  . PHE A 231 ? 0.65818 0.92180 0.75333 -0.22315 -0.05840 0.12996  230 PHE A CG  
1784 C CD1 . PHE A 231 ? 0.63471 0.85718 0.72174 -0.21848 -0.05465 0.13223  230 PHE A CD1 
1785 C CD2 . PHE A 231 ? 0.63526 0.91737 0.72541 -0.20952 -0.06268 0.11999  230 PHE A CD2 
1786 C CE1 . PHE A 231 ? 0.62916 0.83125 0.70416 -0.20247 -0.05468 0.12381  230 PHE A CE1 
1787 C CE2 . PHE A 231 ? 0.63681 0.89464 0.71240 -0.19344 -0.06252 0.11237  230 PHE A CE2 
1788 C CZ  . PHE A 231 ? 0.62409 0.84271 0.69246 -0.19085 -0.05828 0.11381  230 PHE A CZ  
1789 N N   . ASN A 232 ? 0.73876 1.04645 0.85376 -0.26693 -0.07458 0.11313  231 ASN A N   
1790 C CA  . ASN A 232 ? 0.71715 1.02713 0.82352 -0.26395 -0.08408 0.09887  231 ASN A CA  
1791 C C   . ASN A 232 ? 0.77184 1.05133 0.87229 -0.28516 -0.08720 0.09004  231 ASN A C   
1792 O O   . ASN A 232 ? 0.80646 1.06051 0.88968 -0.28055 -0.09131 0.07855  231 ASN A O   
1793 C CB  . ASN A 232 ? 0.66318 1.03090 0.78332 -0.26176 -0.09125 0.09712  231 ASN A CB  
1794 C CG  . ASN A 232 ? 0.62341 1.01306 0.74260 -0.23570 -0.08845 0.10078  231 ASN A CG  
1795 O OD1 . ASN A 232 ? 0.63742 0.99850 0.74054 -0.21802 -0.08518 0.09916  231 ASN A OD1 
1796 N ND2 . ASN A 232 ? 0.58399 1.02448 0.72096 -0.23383 -0.08871 0.10507  231 ASN A ND2 
1797 N N   . LEU A 233 ? 0.79569 1.07526 0.90852 -0.30931 -0.08425 0.09470  232 LEU A N   
1798 C CA  . LEU A 233 ? 0.83589 1.08097 0.94172 -0.33145 -0.08547 0.08497  232 LEU A CA  
1799 C C   . LEU A 233 ? 0.82445 1.00688 0.91277 -0.32442 -0.07769 0.08367  232 LEU A C   
1800 O O   . LEU A 233 ? 0.84116 0.98787 0.91882 -0.33859 -0.07750 0.07282  232 LEU A O   
1801 C CB  . LEU A 233 ? 0.83326 1.08862 0.95637 -0.35987 -0.08185 0.09113  232 LEU A CB  
1802 C CG  . LEU A 233 ? 0.89299 1.19665 1.03084 -0.38039 -0.09157 0.08318  232 LEU A CG  
1803 C CD1 . LEU A 233 ? 0.89424 1.18323 1.01693 -0.38945 -0.10165 0.06399  232 LEU A CD1 
1804 C CD2 . LEU A 233 ? 0.81799 1.18469 0.97034 -0.36426 -0.09707 0.08764  232 LEU A CD2 
1805 N N   . VAL A 234 ? 0.82230 0.99211 0.90814 -0.30365 -0.07096 0.09383  233 VAL A N   
1806 C CA  . VAL A 234 ? 0.84705 0.96597 0.91834 -0.29200 -0.06463 0.09172  233 VAL A CA  
1807 C C   . VAL A 234 ? 0.83794 0.95716 0.89461 -0.27031 -0.06844 0.08232  233 VAL A C   
1808 O O   . VAL A 234 ? 0.82649 0.90709 0.86785 -0.26570 -0.06572 0.07318  233 VAL A O   
1809 C CB  . VAL A 234 ? 0.83229 0.93364 0.90984 -0.28365 -0.05491 0.10884  233 VAL A CB  
1810 C CG1 . VAL A 234 ? 0.84544 0.89077 0.91308 -0.27906 -0.04737 0.10689  233 VAL A CG1 
1811 C CG2 . VAL A 234 ? 0.82111 0.93660 0.91359 -0.30135 -0.05142 0.12248  233 VAL A CG2 
1812 N N   . ALA A 235 ? 0.82398 0.98428 0.88420 -0.25702 -0.07348 0.08405  234 ALA A N   
1813 C CA  . ALA A 235 ? 0.76803 0.92546 0.81328 -0.23648 -0.07568 0.07652  234 ALA A CA  
1814 C C   . ALA A 235 ? 0.77449 0.92671 0.80474 -0.24199 -0.08359 0.06164  234 ALA A C   
1815 O O   . ALA A 235 ? 0.77031 0.89546 0.78199 -0.23093 -0.08208 0.05374  234 ALA A O   
1816 C CB  . ALA A 235 ? 0.78058 0.98010 0.83253 -0.22095 -0.07791 0.08196  234 ALA A CB  
1817 N N   . MET A 236 ? 0.79552 0.97588 0.83319 -0.25956 -0.09215 0.05766  235 MET A N   
1818 C CA  . MET A 236 ? 0.81031 0.99105 0.83270 -0.26642 -0.10178 0.04333  235 MET A CA  
1819 C C   . MET A 236 ? 0.82337 0.95048 0.82776 -0.27726 -0.09696 0.03250  235 MET A C   
1820 O O   . MET A 236 ? 0.82378 0.93666 0.80629 -0.27481 -0.10127 0.02023  235 MET A O   
1821 C CB  . MET A 236 ? 0.82545 1.05211 0.86330 -0.28562 -0.11238 0.04151  235 MET A CB  
1822 C CG  . MET A 236 ? 0.81634 1.09823 0.86366 -0.27073 -0.12092 0.04565  235 MET A CG  
1823 S SD  . MET A 236 ? 1.05559 1.40062 1.13167 -0.29209 -0.13024 0.04775  235 MET A SD  
1824 C CE  . MET A 236 ? 0.80964 1.14694 0.87215 -0.31761 -0.14237 0.03017  235 MET A CE  
1825 N N   . LYS A 237 ? 0.82897 0.92472 0.84090 -0.28840 -0.08723 0.03719  236 LYS A N   
1826 C CA  . LYS A 237 ? 0.84904 0.89011 0.84488 -0.29649 -0.08008 0.02709  236 LYS A CA  
1827 C C   . LYS A 237 ? 0.84524 0.85609 0.82369 -0.27409 -0.07357 0.02381  236 LYS A C   
1828 O O   . LYS A 237 ? 0.86820 0.84640 0.82547 -0.27650 -0.07155 0.01015  236 LYS A O   
1829 C CB  . LYS A 237 ? 0.87197 0.88431 0.88099 -0.30860 -0.06946 0.03606  236 LYS A CB  
1830 C CG  . LYS A 237 ? 0.90467 0.85719 0.89879 -0.31633 -0.05995 0.02586  236 LYS A CG  
1831 C CD  . LYS A 237 ? 0.97822 0.92173 0.96795 -0.34654 -0.06338 0.01316  236 LYS A CD  
1832 C CE  . LYS A 237 ? 0.96440 0.85873 0.92840 -0.35180 -0.05853 -0.00583 236 LYS A CE  
1833 N NZ  . LYS A 237 ? 0.89133 0.80362 0.83434 -0.34310 -0.06853 -0.01888 236 LYS A NZ  
1834 N N   . TYR A 238 ? 0.83847 0.86037 0.82491 -0.25331 -0.06962 0.03538  237 TYR A N   
1835 C CA  . TYR A 238 ? 0.81495 0.81060 0.78918 -0.23321 -0.06195 0.03374  237 TYR A CA  
1836 C C   . TYR A 238 ? 0.79412 0.81213 0.75551 -0.21727 -0.06791 0.03011  237 TYR A C   
1837 O O   . TYR A 238 ? 0.76891 0.77467 0.72442 -0.19957 -0.06133 0.03176  237 TYR A O   
1838 C CB  . TYR A 238 ? 0.78317 0.77299 0.77377 -0.22189 -0.05301 0.04819  237 TYR A CB  
1839 C CG  . TYR A 238 ? 0.80439 0.76135 0.80392 -0.23232 -0.04471 0.05317  237 TYR A CG  
1840 C CD1 . TYR A 238 ? 0.80637 0.77615 0.82163 -0.24750 -0.04616 0.06288  237 TYR A CD1 
1841 C CD2 . TYR A 238 ? 0.83055 0.74274 0.82291 -0.22630 -0.03421 0.04884  237 TYR A CD2 
1842 C CE1 . TYR A 238 ? 0.82094 0.75658 0.84288 -0.25616 -0.03760 0.06906  237 TYR A CE1 
1843 C CE2 . TYR A 238 ? 0.81744 0.69699 0.81820 -0.23337 -0.02568 0.05446  237 TYR A CE2 
1844 C CZ  . TYR A 238 ? 0.81994 0.70975 0.83465 -0.24816 -0.02754 0.06503  237 TYR A CZ  
1845 O OH  . TYR A 238 ? 0.84305 0.69647 0.86472 -0.25433 -0.01812 0.07221  237 TYR A OH  
1846 N N   . ASN A 239 ? 0.79944 0.84995 0.75692 -0.22323 -0.07992 0.02568  238 ASN A N   
1847 C CA  . ASN A 239 ? 0.76914 0.84119 0.71367 -0.20741 -0.08629 0.02377  238 ASN A CA  
1848 C C   . ASN A 239 ? 0.72194 0.81059 0.67708 -0.18766 -0.08168 0.03500  238 ASN A C   
1849 O O   . ASN A 239 ? 0.72497 0.79841 0.66737 -0.17102 -0.07613 0.03421  238 ASN A O   
1850 C CB  . ASN A 239 ? 0.78687 0.82464 0.70196 -0.20185 -0.08352 0.01214  238 ASN A CB  
1851 C CG  . ASN A 239 ? 0.84195 0.87667 0.74060 -0.21968 -0.09244 -0.00094 238 ASN A CG  
1852 O OD1 . ASN A 239 ? 0.81133 0.87992 0.72013 -0.23334 -0.10385 -0.00128 238 ASN A OD1 
1853 N ND2 . ASN A 239 ? 0.86376 0.85955 0.73673 -0.22046 -0.08699 -0.01250 238 ASN A ND2 
1854 N N   . TYR A 240 ? 0.72223 0.84187 0.70014 -0.19119 -0.08316 0.04491  239 TYR A N   
1855 C CA  . TYR A 240 ? 0.70027 0.84221 0.68817 -0.17516 -0.07992 0.05427  239 TYR A CA  
1856 C C   . TYR A 240 ? 0.71772 0.90705 0.71333 -0.17201 -0.08913 0.05657  239 TYR A C   
1857 O O   . TYR A 240 ? 0.69885 0.91295 0.70496 -0.18740 -0.09691 0.05583  239 TYR A O   
1858 C CB  . TYR A 240 ? 0.68307 0.82482 0.68967 -0.17985 -0.07303 0.06467  239 TYR A CB  
1859 C CG  . TYR A 240 ? 0.65423 0.76242 0.65721 -0.17082 -0.06291 0.06671  239 TYR A CG  
1860 C CD1 . TYR A 240 ? 0.66296 0.73056 0.65479 -0.17346 -0.05817 0.05982  239 TYR A CD1 
1861 C CD2 . TYR A 240 ? 0.57423 0.69347 0.58563 -0.16010 -0.05788 0.07496  239 TYR A CD2 
1862 C CE1 . TYR A 240 ? 0.64754 0.68932 0.63980 -0.16446 -0.04879 0.06211  239 TYR A CE1 
1863 C CE2 . TYR A 240 ? 0.59464 0.68888 0.60520 -0.15267 -0.04991 0.07682  239 TYR A CE2 
1864 C CZ  . TYR A 240 ? 0.60947 0.66646 0.61211 -0.15437 -0.04544 0.07092  239 TYR A CZ  
1865 O OH  . TYR A 240 ? 0.62795 0.66464 0.63330 -0.14624 -0.03737 0.07315  239 TYR A OH  
1866 N N   . GLU A 241 ? 0.73204 0.93379 0.72327 -0.15219 -0.08754 0.05910  240 GLU A N   
1867 C CA  . GLU A 241 ? 0.74558 0.99221 0.74554 -0.14499 -0.09465 0.06223  240 GLU A CA  
1868 C C   . GLU A 241 ? 0.74416 1.02528 0.77004 -0.15504 -0.09410 0.07001  240 GLU A C   
1869 O O   . GLU A 241 ? 0.74007 1.01138 0.77350 -0.15693 -0.08567 0.07573  240 GLU A O   
1870 C CB  . GLU A 241 ? 0.72934 0.97585 0.71966 -0.12076 -0.08972 0.06415  240 GLU A CB  
1871 C CG  . GLU A 241 ? 0.78572 1.00763 0.74975 -0.10923 -0.09143 0.05827  240 GLU A CG  
1872 C CD  . GLU A 241 ? 0.93052 1.17795 0.88935 -0.11050 -0.10508 0.05583  240 GLU A CD  
1873 O OE1 . GLU A 241 ? 1.01994 1.25090 0.96512 -0.12249 -0.11082 0.04865  240 GLU A OE1 
1874 O OE2 . GLU A 241 ? 0.92803 1.21327 0.89645 -0.09926 -0.11008 0.06083  240 GLU A OE2 
1875 N N   . PRO A 242 ? 0.68812 1.01154 0.72805 -0.16210 -0.10287 0.07085  241 PRO A N   
1876 C CA  . PRO A 242 ? 0.63717 0.99490 0.70203 -0.17319 -0.10090 0.07839  241 PRO A CA  
1877 C C   . PRO A 242 ? 0.63955 1.01071 0.71058 -0.15673 -0.09165 0.08548  241 PRO A C   
1878 O O   . PRO A 242 ? 0.64075 1.01988 0.70514 -0.13600 -0.09061 0.08463  241 PRO A O   
1879 C CB  . PRO A 242 ? 0.63207 1.03711 0.71016 -0.17966 -0.11252 0.07653  241 PRO A CB  
1880 C CG  . PRO A 242 ? 0.62921 1.01526 0.68760 -0.18182 -0.12209 0.06694  241 PRO A CG  
1881 C CD  . PRO A 242 ? 0.68479 1.02784 0.71870 -0.16260 -0.11544 0.06496  241 PRO A CD  
1882 N N   . LEU A 243 ? 0.62007 0.99175 0.70206 -0.16637 -0.08440 0.09254  242 LEU A N   
1883 C CA  . LEU A 243 ? 0.58999 0.97471 0.67618 -0.15436 -0.07529 0.09855  242 LEU A CA  
1884 C C   . LEU A 243 ? 0.55128 0.98938 0.65756 -0.15478 -0.07580 0.10264  242 LEU A C   
1885 O O   . LEU A 243 ? 0.53617 0.99703 0.65887 -0.17375 -0.07839 0.10628  242 LEU A O   
1886 C CB  . LEU A 243 ? 0.57398 0.93682 0.66063 -0.16400 -0.06799 0.10538  242 LEU A CB  
1887 C CG  . LEU A 243 ? 0.57296 0.93724 0.65588 -0.15156 -0.05891 0.10944  242 LEU A CG  
1888 C CD1 . LEU A 243 ? 0.53281 0.87033 0.59801 -0.13331 -0.05662 0.10211  242 LEU A CD1 
1889 C CD2 . LEU A 243 ? 0.60147 0.95010 0.68618 -0.16300 -0.05434 0.11828  242 LEU A CD2 
1890 N N   . THR A 244 ? 0.55450 1.01169 0.66000 -0.13414 -0.07223 0.10180  243 THR A N   
1891 C CA  . THR A 244 ? 0.51433 1.02338 0.63953 -0.12993 -0.07072 0.10519  243 THR A CA  
1892 C C   . THR A 244 ? 0.51250 1.02968 0.63953 -0.12477 -0.05795 0.10985  243 THR A C   
1893 O O   . THR A 244 ? 0.49615 0.98027 0.60764 -0.12119 -0.05175 0.10957  243 THR A O   
1894 C CB  . THR A 244 ? 0.51149 1.03816 0.63504 -0.10807 -0.07519 0.10122  243 THR A CB  
1895 O OG1 . THR A 244 ? 0.53378 1.03116 0.63812 -0.08681 -0.06722 0.09838  243 THR A OG1 
1896 C CG2 . THR A 244 ? 0.50601 1.02347 0.62281 -0.11309 -0.08873 0.09650  243 THR A CG2 
1897 N N   . GLN A 245 ? 0.48821 1.05261 0.63471 -0.12503 -0.05396 0.11376  244 GLN A N   
1898 C CA  . GLN A 245 ? 0.49185 1.06784 0.63825 -0.11962 -0.04096 0.11711  244 GLN A CA  
1899 C C   . GLN A 245 ? 0.49942 1.05862 0.62919 -0.09449 -0.03398 0.11081  244 GLN A C   
1900 O O   . GLN A 245 ? 0.49066 1.03942 0.60979 -0.09107 -0.02392 0.11060  244 GLN A O   
1901 C CB  . GLN A 245 ? 0.48603 1.11824 0.65752 -0.12465 -0.03681 0.12188  244 GLN A CB  
1902 C CG  . GLN A 245 ? 0.48179 1.12922 0.65221 -0.12140 -0.02220 0.12526  244 GLN A CG  
1903 C CD  . GLN A 245 ? 0.51566 1.13309 0.67176 -0.13628 -0.01848 0.13090  244 GLN A CD  
1904 O OE1 . GLN A 245 ? 0.51422 1.12688 0.67636 -0.15759 -0.02259 0.13788  244 GLN A OE1 
1905 N NE2 . GLN A 245 ? 0.52792 1.12464 0.66466 -0.12505 -0.01070 0.12802  244 GLN A NE2 
1906 N N   . ASP A 246 ? 0.48967 1.04461 0.61535 -0.07752 -0.03909 0.10570  245 ASP A N   
1907 C CA  . ASP A 246 ? 0.50560 1.03488 0.61260 -0.05485 -0.03183 0.09972  245 ASP A CA  
1908 C C   . ASP A 246 ? 0.50677 0.98491 0.59140 -0.05920 -0.03039 0.09639  245 ASP A C   
1909 O O   . ASP A 246 ? 0.51541 0.97520 0.58635 -0.05059 -0.02051 0.09236  245 ASP A O   
1910 C CB  . ASP A 246 ? 0.51360 1.04639 0.61952 -0.03617 -0.03822 0.09737  245 ASP A CB  
1911 C CG  . ASP A 246 ? 0.54331 1.13033 0.67291 -0.02629 -0.03829 0.10066  245 ASP A CG  
1912 O OD1 . ASP A 246 ? 0.51587 1.13880 0.66649 -0.04170 -0.04685 0.10472  245 ASP A OD1 
1913 O OD2 . ASP A 246 ? 0.55861 1.15243 0.68666 -0.00326 -0.02908 0.09892  245 ASP A OD2 
1914 N N   . HIS A 247 ? 0.51340 0.96893 0.59460 -0.07292 -0.03968 0.09724  246 HIS A N   
1915 C CA  . HIS A 247 ? 0.53402 0.94579 0.59854 -0.07807 -0.03799 0.09511  246 HIS A CA  
1916 C C   . HIS A 247 ? 0.52114 0.93604 0.58732 -0.08870 -0.03137 0.09960  246 HIS A C   
1917 O O   . HIS A 247 ? 0.51732 0.90799 0.56997 -0.08540 -0.02587 0.09669  246 HIS A O   
1918 C CB  . HIS A 247 ? 0.54164 0.93164 0.60448 -0.09117 -0.04782 0.09536  246 HIS A CB  
1919 C CG  . HIS A 247 ? 0.53386 0.91493 0.58870 -0.08150 -0.05487 0.09050  246 HIS A CG  
1920 N ND1 . HIS A 247 ? 0.56042 0.94813 0.62058 -0.09276 -0.06571 0.09042  246 HIS A ND1 
1921 C CD2 . HIS A 247 ? 0.54393 0.90850 0.58365 -0.06228 -0.05250 0.08586  246 HIS A CD2 
1922 C CE1 . HIS A 247 ? 0.57359 0.95210 0.62154 -0.08033 -0.07071 0.08625  246 HIS A CE1 
1923 N NE2 . HIS A 247 ? 0.59132 0.95473 0.62678 -0.06116 -0.06250 0.08435  246 HIS A NE2 
1924 N N   . VAL A 248 ? 0.53059 0.97627 0.61287 -0.10244 -0.03203 0.10712  247 VAL A N   
1925 C CA  . VAL A 248 ? 0.51365 0.96542 0.59579 -0.11226 -0.02577 0.11349  247 VAL A CA  
1926 C C   . VAL A 248 ? 0.52764 0.98781 0.60026 -0.09865 -0.01509 0.10867  247 VAL A C   
1927 O O   . VAL A 248 ? 0.52628 0.97077 0.58615 -0.10005 -0.01078 0.10822  247 VAL A O   
1928 C CB  . VAL A 248 ? 0.50325 0.98861 0.60404 -0.12899 -0.02665 0.12289  247 VAL A CB  
1929 C CG1 . VAL A 248 ? 0.48968 0.98131 0.58722 -0.13833 -0.01968 0.13129  247 VAL A CG1 
1930 C CG2 . VAL A 248 ? 0.51273 0.98476 0.62091 -0.14450 -0.03632 0.12579  247 VAL A CG2 
1931 N N   . ASP A 249 ? 0.52789 1.01319 0.60646 -0.08500 -0.01060 0.10449  248 ASP A N   
1932 C CA  . ASP A 249 ? 0.54818 1.03978 0.61707 -0.07166 0.00156  0.09840  248 ASP A CA  
1933 C C   . ASP A 249 ? 0.54350 0.99466 0.59129 -0.06013 0.00449  0.08884  248 ASP A C   
1934 O O   . ASP A 249 ? 0.57929 1.02235 0.61335 -0.05814 0.01308  0.08367  248 ASP A O   
1935 C CB  . ASP A 249 ? 0.54033 1.06737 0.62271 -0.05749 0.00662  0.09662  248 ASP A CB  
1936 C CG  . ASP A 249 ? 0.54885 1.12150 0.65020 -0.06873 0.01004  0.10433  248 ASP A CG  
1937 O OD1 . ASP A 249 ? 0.58382 1.15829 0.68074 -0.08360 0.01325  0.10963  248 ASP A OD1 
1938 O OD2 . ASP A 249 ? 0.57837 1.18652 0.69928 -0.06265 0.00965  0.10579  248 ASP A OD2 
1939 N N   . ILE A 250 ? 0.53631 0.96215 0.58016 -0.05369 -0.00210 0.08593  249 ILE A N   
1940 C CA  . ILE A 250 ? 0.51423 0.89959 0.53849 -0.04539 0.00131  0.07761  249 ILE A CA  
1941 C C   . ILE A 250 ? 0.52157 0.88830 0.53791 -0.05922 0.00073  0.07826  249 ILE A C   
1942 O O   . ILE A 250 ? 0.52267 0.87051 0.52449 -0.05599 0.00748  0.07078  249 ILE A O   
1943 C CB  . ILE A 250 ? 0.52646 0.88875 0.54713 -0.03845 -0.00597 0.07631  249 ILE A CB  
1944 C CG1 . ILE A 250 ? 0.48308 0.86306 0.50864 -0.02044 -0.00512 0.07578  249 ILE A CG1 
1945 C CG2 . ILE A 250 ? 0.51346 0.83222 0.51478 -0.03431 -0.00209 0.06902  249 ILE A CG2 
1946 C CD1 . ILE A 250 ? 0.49003 0.85111 0.50976 -0.01352 -0.01344 0.07591  249 ILE A CD1 
1947 N N   . LEU A 251 ? 0.50028 0.87263 0.52653 -0.07489 -0.00719 0.08732  250 LEU A N   
1948 C CA  . LEU A 251 ? 0.51543 0.87453 0.53716 -0.08663 -0.00874 0.09090  250 LEU A CA  
1949 C C   . LEU A 251 ? 0.53360 0.91660 0.55327 -0.09251 -0.00325 0.09441  250 LEU A C   
1950 O O   . LEU A 251 ? 0.51035 0.88818 0.52653 -0.10195 -0.00551 0.09952  250 LEU A O   
1951 C CB  . LEU A 251 ? 0.49339 0.84558 0.52566 -0.09951 -0.01798 0.10013  250 LEU A CB  
1952 C CG  . LEU A 251 ? 0.50350 0.82647 0.53336 -0.09617 -0.02327 0.09579  250 LEU A CG  
1953 C CD1 . LEU A 251 ? 0.46368 0.78545 0.50486 -0.10916 -0.03104 0.10334  250 LEU A CD1 
1954 C CD2 . LEU A 251 ? 0.49289 0.78417 0.51135 -0.09348 -0.02116 0.09050  250 LEU A CD2 
1955 N N   . GLY A 252 ? 0.50520 0.91513 0.52656 -0.08641 0.00406  0.09217  251 GLY A N   
1956 C CA  . GLY A 252 ? 0.49043 0.92494 0.50755 -0.09181 0.01077  0.09476  251 GLY A CA  
1957 C C   . GLY A 252 ? 0.48594 0.90634 0.48444 -0.09316 0.01439  0.08831  251 GLY A C   
1958 O O   . GLY A 252 ? 0.52405 0.95160 0.51892 -0.10469 0.01158  0.09606  251 GLY A O   
1959 N N   . PRO A 253 ? 0.50386 0.90479 0.48972 -0.08182 0.02080  0.07426  252 PRO A N   
1960 C CA  . PRO A 253 ? 0.52948 0.91771 0.49763 -0.08541 0.02412  0.06585  252 PRO A CA  
1961 C C   . PRO A 253 ? 0.54444 0.91946 0.51381 -0.09646 0.01399  0.07237  252 PRO A C   
1962 O O   . PRO A 253 ? 0.50371 0.88741 0.46421 -0.10499 0.01292  0.07343  252 PRO A O   
1963 C CB  . PRO A 253 ? 0.51749 0.87887 0.47518 -0.07186 0.03210  0.05055  252 PRO A CB  
1964 C CG  . PRO A 253 ? 0.52263 0.89628 0.48910 -0.05856 0.03699  0.05098  252 PRO A CG  
1965 C CD  . PRO A 253 ? 0.50997 0.90285 0.49623 -0.06525 0.02664  0.06562  252 PRO A CD  
1966 N N   . LEU A 254 ? 0.53725 0.89286 0.51717 -0.09601 0.00660  0.07684  253 LEU A N   
1967 C CA  . LEU A 254 ? 0.53903 0.88266 0.52285 -0.10457 -0.00182 0.08369  253 LEU A CA  
1968 C C   . LEU A 254 ? 0.54978 0.91514 0.54054 -0.11544 -0.00747 0.09991  253 LEU A C   
1969 O O   . LEU A 254 ? 0.51192 0.88044 0.49954 -0.12197 -0.01169 0.10536  253 LEU A O   
1970 C CB  . LEU A 254 ? 0.52408 0.84157 0.51657 -0.10125 -0.00654 0.08429  253 LEU A CB  
1971 C CG  . LEU A 254 ? 0.53259 0.82136 0.51616 -0.09313 -0.00206 0.07086  253 LEU A CG  
1972 C CD1 . LEU A 254 ? 0.50959 0.77415 0.49993 -0.09134 -0.00675 0.07295  253 LEU A CD1 
1973 C CD2 . LEU A 254 ? 0.55542 0.83940 0.53084 -0.09796 -0.00035 0.06443  253 LEU A CD2 
1974 N N   . SER A 255 ? 0.51058 0.89184 0.51113 -0.11769 -0.00763 0.10851  254 SER A N   
1975 C CA  . SER A 255 ? 0.49746 0.89712 0.50339 -0.12883 -0.01104 0.12494  254 SER A CA  
1976 C C   . SER A 255 ? 0.50531 0.92806 0.49713 -0.13261 -0.00686 0.12615  254 SER A C   
1977 O O   . SER A 255 ? 0.53538 0.96528 0.52469 -0.14065 -0.01150 0.13889  254 SER A O   
1978 C CB  . SER A 255 ? 0.49978 0.91453 0.51895 -0.13210 -0.01008 0.13157  254 SER A CB  
1979 O OG  . SER A 255 ? 0.54044 0.97208 0.55818 -0.12372 -0.00233 0.12161  254 SER A OG  
1980 N N   . ALA A 256 ? 0.51567 0.94924 0.49661 -0.12627 0.00223  0.11304  255 ALA A N   
1981 C CA  . ALA A 256 ? 0.52909 0.98393 0.49301 -0.13036 0.00743  0.11141  255 ALA A CA  
1982 C C   . ALA A 256 ? 0.54308 0.98774 0.49393 -0.13315 0.00291  0.10593  255 ALA A C   
1983 O O   . ALA A 256 ? 0.54834 1.01093 0.48696 -0.14075 0.00112  0.11160  255 ALA A O   
1984 C CB  . ALA A 256 ? 0.49716 0.96335 0.45299 -0.12186 0.02026  0.09718  255 ALA A CB  
1985 N N   . GLN A 257 ? 0.52830 0.94649 0.48123 -0.12777 0.00101  0.09515  256 GLN A N   
1986 C CA  . GLN A 257 ? 0.57734 0.98885 0.52158 -0.13185 -0.00350 0.08946  256 GLN A CA  
1987 C C   . GLN A 257 ? 0.55034 0.96476 0.50483 -0.13818 -0.01543 0.10707  256 GLN A C   
1988 O O   . GLN A 257 ? 0.55862 0.98719 0.50496 -0.14430 -0.02078 0.11044  256 GLN A O   
1989 C CB  . GLN A 257 ? 0.57590 0.95794 0.52048 -0.12518 -0.00040 0.07346  256 GLN A CB  
1990 C CG  . GLN A 257 ? 0.59985 0.97626 0.53952 -0.13095 -0.00486 0.06680  256 GLN A CG  
1991 C CD  . GLN A 257 ? 0.67390 1.01938 0.61476 -0.12582 -0.00042 0.05234  256 GLN A CD  
1992 O OE1 . GLN A 257 ? 0.64185 0.96983 0.58046 -0.11688 0.00776  0.04440  256 GLN A OE1 
1993 N NE2 . GLN A 257 ? 0.67030 1.01018 0.61517 -0.13115 -0.00558 0.04979  256 GLN A NE2 
1994 N N   . THR A 258 ? 0.55192 0.95317 0.52377 -0.13648 -0.01971 0.11841  257 THR A N   
1995 C CA  . THR A 258 ? 0.53849 0.93715 0.52110 -0.14031 -0.02933 0.13530  257 THR A CA  
1996 C C   . THR A 258 ? 0.54896 0.96798 0.53065 -0.14703 -0.03174 0.15510  257 THR A C   
1997 O O   . THR A 258 ? 0.58428 1.00547 0.57001 -0.14968 -0.03935 0.17062  257 THR A O   
1998 C CB  . THR A 258 ? 0.52216 0.89289 0.52175 -0.13621 -0.03154 0.13751  257 THR A CB  
1999 O OG1 . THR A 258 ? 0.52123 0.89108 0.52615 -0.13625 -0.02788 0.13995  257 THR A OG1 
2000 C CG2 . THR A 258 ? 0.50096 0.84999 0.50011 -0.12996 -0.02884 0.12010  257 THR A CG2 
2001 N N   . GLY A 259 ? 0.53479 0.96915 0.51169 -0.14932 -0.02479 0.15579  258 GLY A N   
2002 C CA  . GLY A 259 ? 0.51351 0.96493 0.49013 -0.15698 -0.02521 0.17526  258 GLY A CA  
2003 C C   . GLY A 259 ? 0.53104 0.96623 0.52566 -0.15986 -0.02783 0.18911  258 GLY A C   
2004 O O   . GLY A 259 ? 0.53896 0.98037 0.53446 -0.16691 -0.02940 0.20840  258 GLY A O   
2005 N N   . ILE A 260 ? 0.54284 0.95577 0.55000 -0.15527 -0.02786 0.17974  259 ILE A N   
2006 C CA  . ILE A 260 ? 0.51955 0.91344 0.54234 -0.15910 -0.03027 0.18926  259 ILE A CA  
2007 C C   . ILE A 260 ? 0.51632 0.91630 0.54599 -0.16023 -0.02520 0.18116  259 ILE A C   
2008 O O   . ILE A 260 ? 0.50431 0.89919 0.53353 -0.15210 -0.02336 0.16493  259 ILE A O   
2009 C CB  . ILE A 260 ? 0.49985 0.86239 0.53091 -0.15338 -0.03549 0.18543  259 ILE A CB  
2010 C CG1 . ILE A 260 ? 0.50115 0.86384 0.52842 -0.15050 -0.04084 0.19201  259 ILE A CG1 
2011 C CG2 . ILE A 260 ? 0.52010 0.86075 0.56448 -0.15864 -0.03699 0.19474  259 ILE A CG2 
2012 C CD1 . ILE A 260 ? 0.50764 0.84338 0.54458 -0.14392 -0.04429 0.18712  259 ILE A CD1 
2013 N N   . ALA A 261 ? 0.53227 0.94395 0.56878 -0.17033 -0.02292 0.19315  260 ALA A N   
2014 C CA  . ALA A 261 ? 0.50997 0.93268 0.55695 -0.17286 -0.01937 0.18681  260 ALA A CA  
2015 C C   . ALA A 261 ? 0.50954 0.90549 0.56600 -0.16966 -0.02425 0.17796  260 ALA A C   
2016 O O   . ALA A 261 ? 0.51544 0.88262 0.57402 -0.17049 -0.02899 0.18193  260 ALA A O   
2017 C CB  . ALA A 261 ? 0.48429 0.92266 0.53903 -0.18747 -0.01618 0.20228  260 ALA A CB  
2018 N N   . VAL A 262 ? 0.50805 0.91457 0.56960 -0.16503 -0.02271 0.16603  261 VAL A N   
2019 C CA  . VAL A 262 ? 0.50835 0.89230 0.57520 -0.16138 -0.02758 0.15673  261 VAL A CA  
2020 C C   . VAL A 262 ? 0.52833 0.89695 0.60576 -0.17514 -0.03158 0.16525  261 VAL A C   
2021 O O   . VAL A 262 ? 0.52987 0.86759 0.60724 -0.17439 -0.03574 0.16147  261 VAL A O   
2022 C CB  . VAL A 262 ? 0.52292 0.92633 0.59304 -0.15299 -0.02579 0.14493  261 VAL A CB  
2023 C CG1 . VAL A 262 ? 0.50086 0.88331 0.57403 -0.15009 -0.03187 0.13672  261 VAL A CG1 
2024 C CG2 . VAL A 262 ? 0.50795 0.91770 0.56556 -0.13862 -0.02010 0.13531  261 VAL A CG2 
2025 N N   . LEU A 263 ? 0.53191 0.92002 0.61761 -0.18873 -0.02909 0.17641  262 LEU A N   
2026 C CA  . LEU A 263 ? 0.54480 0.91614 0.64004 -0.20415 -0.03146 0.18371  262 LEU A CA  
2027 C C   . LEU A 263 ? 0.55108 0.88796 0.64157 -0.20628 -0.03236 0.19477  262 LEU A C   
2028 O O   . LEU A 263 ? 0.58838 0.89512 0.68288 -0.21277 -0.03465 0.19503  262 LEU A O   
2029 C CB  . LEU A 263 ? 0.55697 0.95887 0.66290 -0.21961 -0.02702 0.19294  262 LEU A CB  
2030 C CG  . LEU A 263 ? 0.51667 0.95641 0.63354 -0.21910 -0.02632 0.18332  262 LEU A CG  
2031 C CD1 . LEU A 263 ? 0.52490 0.99368 0.65556 -0.23764 -0.02135 0.19329  262 LEU A CD1 
2032 C CD2 . LEU A 263 ? 0.52339 0.95114 0.64466 -0.21610 -0.03392 0.16971  262 LEU A CD2 
2033 N N   . ASP A 264 ? 0.54576 0.88675 0.62748 -0.20027 -0.03061 0.20360  263 ASP A N   
2034 C CA  . ASP A 264 ? 0.57636 0.88801 0.65533 -0.19893 -0.03236 0.21505  263 ASP A CA  
2035 C C   . ASP A 264 ? 0.56317 0.84610 0.64083 -0.18741 -0.03610 0.20336  263 ASP A C   
2036 O O   . ASP A 264 ? 0.58867 0.83913 0.67024 -0.18872 -0.03702 0.20747  263 ASP A O   
2037 C CB  . ASP A 264 ? 0.59314 0.92238 0.66247 -0.19513 -0.03121 0.22738  263 ASP A CB  
2038 C CG  . ASP A 264 ? 0.58726 0.94349 0.65549 -0.20704 -0.02592 0.24039  263 ASP A CG  
2039 O OD1 . ASP A 264 ? 0.60487 0.97032 0.68236 -0.21802 -0.02283 0.23828  263 ASP A OD1 
2040 O OD2 . ASP A 264 ? 0.59113 0.96114 0.64904 -0.20607 -0.02481 0.25279  263 ASP A OD2 
2041 N N   . MET A 265 ? 0.54906 0.84180 0.62085 -0.17605 -0.03683 0.18869  264 MET A N   
2042 C CA  . MET A 265 ? 0.55160 0.81812 0.62174 -0.16650 -0.03887 0.17647  264 MET A CA  
2043 C C   . MET A 265 ? 0.55511 0.80090 0.63000 -0.17211 -0.04014 0.16908  264 MET A C   
2044 O O   . MET A 265 ? 0.57721 0.79204 0.65185 -0.16877 -0.04075 0.16461  264 MET A O   
2045 C CB  . MET A 265 ? 0.51516 0.79503 0.57679 -0.15505 -0.03785 0.16232  264 MET A CB  
2046 C CG  . MET A 265 ? 0.52645 0.78043 0.58468 -0.14533 -0.03840 0.15144  264 MET A CG  
2047 S SD  . MET A 265 ? 0.56014 0.80327 0.62040 -0.14104 -0.03959 0.16016  264 MET A SD  
2048 C CE  . MET A 265 ? 0.49871 0.77041 0.54842 -0.13573 -0.03834 0.15428  264 MET A CE  
2049 N N   . CYS A 266 ? 0.55199 0.81625 0.63134 -0.18124 -0.04040 0.16734  265 CYS A N   
2050 C CA  . CYS A 266 ? 0.55637 0.80482 0.63977 -0.18976 -0.04290 0.16049  265 CYS A CA  
2051 C C   . CYS A 266 ? 0.57299 0.79084 0.66079 -0.20106 -0.04166 0.17002  265 CYS A C   
2052 O O   . CYS A 266 ? 0.58492 0.77273 0.67128 -0.20367 -0.04262 0.16254  265 CYS A O   
2053 C CB  . CYS A 266 ? 0.54940 0.83132 0.63984 -0.19840 -0.04408 0.15792  265 CYS A CB  
2054 S SG  . CYS A 266 ? 0.51446 0.82461 0.60059 -0.18298 -0.04542 0.14421  265 CYS A SG  
2055 N N   . ALA A 267 ? 0.58502 0.80839 0.67661 -0.20781 -0.03867 0.18671  266 ALA A N   
2056 C CA  . ALA A 267 ? 0.59292 0.78271 0.68784 -0.21631 -0.03604 0.19802  266 ALA A CA  
2057 C C   . ALA A 267 ? 0.62644 0.78324 0.71836 -0.20299 -0.03571 0.19714  266 ALA A C   
2058 O O   . ALA A 267 ? 0.64128 0.76128 0.73459 -0.20633 -0.03358 0.19554  266 ALA A O   
2059 C CB  . ALA A 267 ? 0.64404 0.84681 0.74119 -0.22376 -0.03249 0.21850  266 ALA A CB  
2060 N N   . SER A 268 ? 0.60147 0.77166 0.68974 -0.18834 -0.03707 0.19730  267 SER A N   
2061 C CA  . SER A 268 ? 0.63191 0.77730 0.72024 -0.17542 -0.03666 0.19520  267 SER A CA  
2062 C C   . SER A 268 ? 0.61504 0.73697 0.70012 -0.17280 -0.03622 0.17687  267 SER A C   
2063 O O   . SER A 268 ? 0.62081 0.70913 0.70787 -0.16949 -0.03322 0.17554  267 SER A O   
2064 C CB  . SER A 268 ? 0.61459 0.78408 0.69977 -0.16308 -0.03873 0.19581  267 SER A CB  
2065 O OG  . SER A 268 ? 0.65824 0.84507 0.74415 -0.16432 -0.03953 0.21406  267 SER A OG  
2066 N N   . LEU A 269 ? 0.60382 0.74298 0.68307 -0.17334 -0.03861 0.16312  268 LEU A N   
2067 C CA  . LEU A 269 ? 0.60038 0.71940 0.67306 -0.17094 -0.03881 0.14662  268 LEU A CA  
2068 C C   . LEU A 269 ? 0.62269 0.71575 0.69608 -0.18440 -0.03813 0.14416  268 LEU A C   
2069 O O   . LEU A 269 ? 0.64718 0.70910 0.71512 -0.18249 -0.03591 0.13454  268 LEU A O   
2070 C CB  . LEU A 269 ? 0.57216 0.71734 0.63807 -0.16735 -0.04201 0.13531  268 LEU A CB  
2071 C CG  . LEU A 269 ? 0.56533 0.69709 0.62171 -0.16621 -0.04388 0.11978  268 LEU A CG  
2072 C CD1 . LEU A 269 ? 0.59390 0.69166 0.64364 -0.15751 -0.03982 0.11280  268 LEU A CD1 
2073 C CD2 . LEU A 269 ? 0.54924 0.70911 0.59990 -0.15854 -0.04647 0.11272  268 LEU A CD2 
2074 N N   . LYS A 270 ? 0.63035 0.73533 0.70956 -0.19931 -0.03911 0.15187  269 LYS A N   
2075 C CA  . LYS A 270 ? 0.65342 0.73184 0.73352 -0.21520 -0.03767 0.14958  269 LYS A CA  
2076 C C   . LYS A 270 ? 0.69240 0.72798 0.77405 -0.21233 -0.03114 0.15645  269 LYS A C   
2077 O O   . LYS A 270 ? 0.70764 0.70808 0.78431 -0.21686 -0.02815 0.14676  269 LYS A O   
2078 C CB  . LYS A 270 ? 0.64127 0.74171 0.72942 -0.23302 -0.03839 0.15860  269 LYS A CB  
2079 C CG  . LYS A 270 ? 0.71490 0.78841 0.80389 -0.25305 -0.03665 0.15457  269 LYS A CG  
2080 C CD  . LYS A 270 ? 0.72816 0.79958 0.82580 -0.26850 -0.03177 0.17155  269 LYS A CD  
2081 C CE  . LYS A 270 ? 0.72716 0.84264 0.83285 -0.28354 -0.03491 0.17270  269 LYS A CE  
2082 N NZ  . LYS A 270 ? 0.72523 0.83011 0.83791 -0.30508 -0.02895 0.18512  269 LYS A NZ  
2083 N N   . GLU A 271 ? 0.66806 0.70656 0.75608 -0.20420 -0.02871 0.17327  270 GLU A N   
2084 C CA  . GLU A 271 ? 0.69387 0.69484 0.78582 -0.19752 -0.02258 0.18206  270 GLU A CA  
2085 C C   . GLU A 271 ? 0.70943 0.68949 0.79780 -0.18340 -0.02022 0.16890  270 GLU A C   
2086 O O   . GLU A 271 ? 0.74680 0.68710 0.83524 -0.18230 -0.01375 0.16606  270 GLU A O   
2087 C CB  . GLU A 271 ? 0.73386 0.75011 0.83279 -0.18918 -0.02261 0.20343  270 GLU A CB  
2088 C CG  . GLU A 271 ? 0.80416 0.78523 0.90967 -0.18069 -0.01672 0.21663  270 GLU A CG  
2089 C CD  . GLU A 271 ? 0.84163 0.82049 0.95085 -0.18742 -0.01461 0.23997  270 GLU A CD  
2090 O OE1 . GLU A 271 ? 0.86093 0.85472 0.96736 -0.20407 -0.01540 0.24250  270 GLU A OE1 
2091 O OE2 . GLU A 271 ? 0.86830 0.83187 0.98360 -0.17569 -0.01192 0.25660  270 GLU A OE2 
2092 N N   . LEU A 272 ? 0.68065 0.68546 0.76539 -0.17278 -0.02395 0.16051  271 LEU A N   
2093 C CA  . LEU A 272 ? 0.70825 0.69503 0.78888 -0.16079 -0.02060 0.14771  271 LEU A CA  
2094 C C   . LEU A 272 ? 0.73298 0.69326 0.80193 -0.16885 -0.01864 0.13053  271 LEU A C   
2095 O O   . LEU A 272 ? 0.73408 0.66134 0.80020 -0.16361 -0.01194 0.12322  271 LEU A O   
2096 C CB  . LEU A 272 ? 0.65058 0.66789 0.72788 -0.15051 -0.02418 0.14191  271 LEU A CB  
2097 C CG  . LEU A 272 ? 0.62143 0.66176 0.70799 -0.14063 -0.02552 0.15453  271 LEU A CG  
2098 C CD1 . LEU A 272 ? 0.57827 0.64376 0.65876 -0.13352 -0.02776 0.14493  271 LEU A CD1 
2099 C CD2 . LEU A 272 ? 0.63272 0.65081 0.73015 -0.13044 -0.02040 0.16144  271 LEU A CD2 
2100 N N   . LEU A 273 ? 0.71180 0.68819 0.77378 -0.18156 -0.02439 0.12366  272 LEU A N   
2101 C CA  . LEU A 273 ? 0.72566 0.68201 0.77467 -0.19069 -0.02468 0.10707  272 LEU A CA  
2102 C C   . LEU A 273 ? 0.76432 0.68190 0.81384 -0.20330 -0.01892 0.10720  272 LEU A C   
2103 O O   . LEU A 273 ? 0.79065 0.67758 0.82827 -0.20692 -0.01530 0.09289  272 LEU A O   
2104 C CB  . LEU A 273 ? 0.69065 0.68057 0.73497 -0.20053 -0.03370 0.10115  272 LEU A CB  
2105 C CG  . LEU A 273 ? 0.64398 0.66609 0.68395 -0.18769 -0.03825 0.09763  272 LEU A CG  
2106 C CD1 . LEU A 273 ? 0.64023 0.69771 0.67981 -0.19619 -0.04659 0.09468  272 LEU A CD1 
2107 C CD2 . LEU A 273 ? 0.68613 0.68757 0.71158 -0.17667 -0.03534 0.08459  272 LEU A CD2 
2108 N N   . GLN A 274 ? 0.75617 0.67230 0.81734 -0.21041 -0.01708 0.12299  273 GLN A N   
2109 C CA  . GLN A 274 ? 0.80233 0.67870 0.86364 -0.22395 -0.01043 0.12406  273 GLN A CA  
2110 C C   . GLN A 274 ? 0.84090 0.67685 0.90704 -0.21077 0.00020  0.13068  273 GLN A C   
2111 O O   . GLN A 274 ? 0.87828 0.67075 0.94025 -0.21869 0.00821  0.12563  273 GLN A O   
2112 C CB  . GLN A 274 ? 0.81000 0.70103 0.88051 -0.23963 -0.01207 0.13886  273 GLN A CB  
2113 C CG  . GLN A 274 ? 0.80708 0.73420 0.87563 -0.25654 -0.02080 0.13107  273 GLN A CG  
2114 C CD  . GLN A 274 ? 0.80594 0.74715 0.88469 -0.27359 -0.02028 0.14563  273 GLN A CD  
2115 O OE1 . GLN A 274 ? 0.82678 0.75748 0.91261 -0.26988 -0.01469 0.16436  273 GLN A OE1 
2116 N NE2 . GLN A 274 ? 0.81602 0.78273 0.89576 -0.29243 -0.02603 0.13782  273 GLN A NE2 
2117 N N   . ASN A 275 ? 0.81919 0.66881 0.89457 -0.19103 0.00078  0.14131  274 ASN A N   
2118 C CA  . ASN A 275 ? 0.86213 0.68051 0.94631 -0.17611 0.01017  0.14961  274 ASN A CA  
2119 C C   . ASN A 275 ? 0.86344 0.68458 0.94849 -0.15740 0.01276  0.14110  274 ASN A C   
2120 O O   . ASN A 275 ? 0.91227 0.70785 1.00596 -0.14418 0.02160  0.14521  274 ASN A O   
2121 C CB  . ASN A 275 ? 0.92603 0.75742 1.02480 -0.16976 0.00927  0.17532  274 ASN A CB  
2122 C CG  . ASN A 275 ? 0.98538 0.80706 1.08377 -0.18813 0.00993  0.18634  274 ASN A CG  
2123 O OD1 . ASN A 275 ? 1.03512 0.82385 1.12617 -0.20355 0.01496  0.17659  274 ASN A OD1 
2124 N ND2 . ASN A 275 ? 0.93739 0.78770 1.04256 -0.18791 0.00539  0.20626  274 ASN A ND2 
2125 N N   . GLY A 276 ? 0.85218 0.70279 0.92945 -0.15558 0.00638  0.12996  275 GLY A N   
2126 C CA  . GLY A 276 ? 0.84927 0.70233 0.92672 -0.14004 0.00990  0.12185  275 GLY A CA  
2127 C C   . GLY A 276 ? 0.86394 0.74581 0.95783 -0.12561 0.00756  0.13634  275 GLY A C   
2128 O O   . GLY A 276 ? 0.84170 0.74637 0.94385 -0.12714 0.00170  0.15249  275 GLY A O   
2129 N N   . MET A 277 ? 0.85572 0.73763 0.95358 -0.11233 0.01248  0.12985  276 MET A N   
2130 C CA  . MET A 277 ? 0.87812 0.78890 0.99226 -0.09942 0.01026  0.14068  276 MET A CA  
2131 C C   . MET A 277 ? 0.92531 0.82225 1.05934 -0.08736 0.01595  0.15550  276 MET A C   
2132 O O   . MET A 277 ? 0.89388 0.81908 1.04321 -0.07810 0.01150  0.16900  276 MET A O   
2133 C CB  . MET A 277 ? 0.86816 0.78900 0.97887 -0.09234 0.01322  0.12656  276 MET A CB  
2134 C CG  . MET A 277 ? 0.85814 0.78845 0.94807 -0.10098 0.00892  0.11232  276 MET A CG  
2135 S SD  . MET A 277 ? 0.83327 0.81094 0.92304 -0.10258 -0.00176 0.11779  276 MET A SD  
2136 C CE  . MET A 277 ? 0.69813 0.69138 0.80067 -0.09015 0.00247  0.11617  276 MET A CE  
2137 N N   . ASN A 278 ? 1.03263 0.88704 1.16629 -0.08689 0.02571  0.15310  277 ASN A N   
2138 C CA  . ASN A 278 ? 1.04072 0.87583 1.19344 -0.07315 0.03316  0.16733  277 ASN A CA  
2139 C C   . ASN A 278 ? 1.00466 0.85916 1.17623 -0.05518 0.03642  0.16839  277 ASN A C   
2140 O O   . ASN A 278 ? 1.00157 0.86649 1.19432 -0.04155 0.03609  0.18617  277 ASN A O   
2141 C CB  . ASN A 278 ? 1.03635 0.88091 1.19729 -0.07432 0.02667  0.19135  277 ASN A CB  
2142 C CG  . ASN A 278 ? 1.09337 0.89086 1.25681 -0.07396 0.03621  0.20007  277 ASN A CG  
2143 O OD1 . ASN A 278 ? 1.13829 0.89548 1.29052 -0.08074 0.04560  0.18480  277 ASN A OD1 
2144 N ND2 . ASN A 278 ? 1.11428 0.91504 1.29070 -0.06622 0.03423  0.22474  277 ASN A ND2 
2145 N N   . GLY A 279 ? 0.94328 0.80410 1.10766 -0.05522 0.03960  0.15005  278 GLY A N   
2146 C CA  . GLY A 279 ? 0.88862 0.76808 1.07088 -0.04109 0.04421  0.14838  278 GLY A CA  
2147 C C   . GLY A 279 ? 0.84834 0.77829 1.03947 -0.04001 0.03304  0.15455  278 GLY A C   
2148 O O   . GLY A 279 ? 0.79957 0.74997 1.00842 -0.02985 0.03595  0.15389  278 GLY A O   
2149 N N   . ARG A 280 ? 0.84000 0.79135 1.01976 -0.05081 0.02113  0.15966  279 ARG A N   
2150 C CA  . ARG A 280 ? 0.80148 0.79829 0.98546 -0.05161 0.01120  0.16309  279 ARG A CA  
2151 C C   . ARG A 280 ? 0.79988 0.80341 0.96601 -0.05977 0.01167  0.14368  279 ARG A C   
2152 O O   . ARG A 280 ? 0.81287 0.78857 0.96283 -0.06433 0.01828  0.12930  279 ARG A O   
2153 C CB  . ARG A 280 ? 0.81305 0.83007 0.99343 -0.05785 -0.00032 0.17928  279 ARG A CB  
2154 C CG  . ARG A 280 ? 0.85738 0.88824 1.05791 -0.04711 -0.00445 0.20231  279 ARG A CG  
2155 C CD  . ARG A 280 ? 0.91665 0.91286 1.11630 -0.04715 -0.00082 0.21555  279 ARG A CD  
2156 N NE  . ARG A 280 ? 0.95619 0.94666 1.13573 -0.06341 -0.00491 0.21483  279 ARG A NE  
2157 C CZ  . ARG A 280 ? 1.03645 0.99872 1.21156 -0.06907 -0.00229 0.22486  279 ARG A CZ  
2158 N NH1 . ARG A 280 ? 1.08577 1.01847 1.27308 -0.05888 0.00482  0.23707  279 ARG A NH1 
2159 N NH2 . ARG A 280 ? 0.97968 0.94315 1.13860 -0.08535 -0.00602 0.22260  279 ARG A NH2 
2160 N N   . THR A 281 ? 0.69932 0.73938 0.86698 -0.06158 0.00472  0.14345  280 THR A N   
2161 C CA  . THR A 281 ? 0.63754 0.68453 0.78784 -0.06866 0.00500  0.12742  280 THR A CA  
2162 C C   . THR A 281 ? 0.61976 0.69673 0.76140 -0.07596 -0.00571 0.13201  280 THR A C   
2163 O O   . THR A 281 ? 0.62983 0.73038 0.78151 -0.07485 -0.01332 0.14670  280 THR A O   
2164 C CB  . THR A 281 ? 0.61788 0.67560 0.77794 -0.06405 0.01147  0.11772  280 THR A CB  
2165 O OG1 . THR A 281 ? 0.59109 0.68645 0.77028 -0.06101 0.00458  0.12757  280 THR A OG1 
2166 C CG2 . THR A 281 ? 0.61711 0.64757 0.78722 -0.05584 0.02391  0.11329  280 THR A CG2 
2167 N N   . ILE A 282 ? 0.60358 0.67915 0.72536 -0.08260 -0.00569 0.11966  281 ILE A N   
2168 C CA  . ILE A 282 ? 0.59155 0.69413 0.70355 -0.08853 -0.01305 0.12027  281 ILE A CA  
2169 C C   . ILE A 282 ? 0.57958 0.68691 0.68225 -0.08932 -0.00874 0.10504  281 ILE A C   
2170 O O   . ILE A 282 ? 0.57028 0.65494 0.65937 -0.08940 -0.00250 0.09334  281 ILE A O   
2171 C CB  . ILE A 282 ? 0.58027 0.67692 0.67749 -0.09529 -0.01672 0.12160  281 ILE A CB  
2172 C CG1 . ILE A 282 ? 0.60689 0.69743 0.71271 -0.09689 -0.01995 0.13727  281 ILE A CG1 
2173 C CG2 . ILE A 282 ? 0.56453 0.68868 0.65157 -0.09971 -0.02173 0.12005  281 ILE A CG2 
2174 C CD1 . ILE A 282 ? 0.60092 0.68841 0.69521 -0.10591 -0.02311 0.13865  281 ILE A CD1 
2175 N N   . LEU A 283 ? 0.57505 0.71068 0.68345 -0.09052 -0.01188 0.10524  282 LEU A N   
2176 C CA  . LEU A 283 ? 0.54966 0.68863 0.65075 -0.09271 -0.00655 0.09080  282 LEU A CA  
2177 C C   . LEU A 283 ? 0.54381 0.65841 0.64838 -0.08903 0.00418  0.08159  282 LEU A C   
2178 O O   . LEU A 283 ? 0.54941 0.64589 0.63807 -0.09016 0.01151  0.06936  282 LEU A O   
2179 C CB  . LEU A 283 ? 0.54911 0.68452 0.62725 -0.09640 -0.00628 0.08252  282 LEU A CB  
2180 C CG  . LEU A 283 ? 0.54688 0.71081 0.61990 -0.10084 -0.01369 0.08701  282 LEU A CG  
2181 C CD1 . LEU A 283 ? 0.50544 0.66348 0.55768 -0.10180 -0.01115 0.07813  282 LEU A CD1 
2182 C CD2 . LEU A 283 ? 0.53241 0.72256 0.61364 -0.10430 -0.01566 0.08507  282 LEU A CD2 
2183 N N   . GLY A 284 ? 0.53400 0.64757 0.65919 -0.08362 0.00594  0.08846  283 GLY A N   
2184 C CA  . GLY A 284 ? 0.54653 0.64033 0.67809 -0.07957 0.01749  0.08053  283 GLY A CA  
2185 C C   . GLY A 284 ? 0.56662 0.62227 0.68165 -0.07777 0.02466  0.07452  283 GLY A C   
2186 O O   . GLY A 284 ? 0.54851 0.58544 0.66437 -0.07487 0.03583  0.06662  283 GLY A O   
2187 N N   . SER A 285 ? 0.56531 0.61059 0.66512 -0.08024 0.01884  0.07752  284 SER A N   
2188 C CA  . SER A 285 ? 0.58047 0.59289 0.66281 -0.08040 0.02351  0.07120  284 SER A CA  
2189 C C   . SER A 285 ? 0.58875 0.58896 0.67846 -0.07966 0.02057  0.08047  284 SER A C   
2190 O O   . SER A 285 ? 0.59566 0.61280 0.69436 -0.08131 0.01199  0.09263  284 SER A O   
2191 C CB  . SER A 285 ? 0.59229 0.60281 0.65025 -0.08490 0.01939  0.06545  284 SER A CB  
2192 O OG  . SER A 285 ? 0.59621 0.58011 0.63755 -0.08601 0.02107  0.06051  284 SER A OG  
2193 N N   . ALA A 286 ? 0.59442 0.56322 0.67858 -0.07778 0.02876  0.07448  285 ALA A N   
2194 C CA  . ALA A 286 ? 0.62319 0.57214 0.70951 -0.07898 0.02788  0.08022  285 ALA A CA  
2195 C C   . ALA A 286 ? 0.61897 0.55417 0.68224 -0.08794 0.02309  0.07468  285 ALA A C   
2196 O O   . ALA A 286 ? 0.65497 0.57026 0.71666 -0.09207 0.02299  0.07663  285 ALA A O   
2197 C CB  . ALA A 286 ? 0.60111 0.52234 0.69498 -0.07216 0.04051  0.07598  285 ALA A CB  
2198 N N   . LEU A 287 ? 0.59720 0.54288 0.64338 -0.09105 0.01928  0.06791  286 LEU A N   
2199 C CA  . LEU A 287 ? 0.60968 0.55139 0.63675 -0.09856 0.01279  0.06381  286 LEU A CA  
2200 C C   . LEU A 287 ? 0.59472 0.56857 0.62249 -0.10113 0.00314  0.06981  286 LEU A C   
2201 O O   . LEU A 287 ? 0.58677 0.58137 0.62227 -0.09720 0.00287  0.07285  286 LEU A O   
2202 C CB  . LEU A 287 ? 0.61424 0.53709 0.61712 -0.09770 0.01773  0.05020  286 LEU A CB  
2203 C CG  . LEU A 287 ? 0.63038 0.51900 0.62617 -0.09675 0.02807  0.04182  286 LEU A CG  
2204 C CD1 . LEU A 287 ? 0.65022 0.52243 0.61667 -0.09764 0.03059  0.02972  286 LEU A CD1 
2205 C CD2 . LEU A 287 ? 0.63199 0.50523 0.63363 -0.10313 0.02629  0.04499  286 LEU A CD2 
2206 N N   . LEU A 288 ? 0.58084 0.55966 0.60067 -0.10852 -0.00429 0.07063  287 LEU A N   
2207 C CA  . LEU A 288 ? 0.55774 0.56676 0.57642 -0.11030 -0.01195 0.07459  287 LEU A CA  
2208 C C   . LEU A 288 ? 0.55641 0.56701 0.55762 -0.10474 -0.01062 0.06512  287 LEU A C   
2209 O O   . LEU A 288 ? 0.57114 0.56703 0.55593 -0.10539 -0.01086 0.05749  287 LEU A O   
2210 C CB  . LEU A 288 ? 0.56702 0.58357 0.58599 -0.12049 -0.01943 0.07877  287 LEU A CB  
2211 C CG  . LEU A 288 ? 0.60670 0.62271 0.64165 -0.12725 -0.02072 0.09076  287 LEU A CG  
2212 C CD1 . LEU A 288 ? 0.58581 0.61996 0.63531 -0.12162 -0.02021 0.10181  287 LEU A CD1 
2213 C CD2 . LEU A 288 ? 0.65527 0.63548 0.69062 -0.13001 -0.01513 0.08804  287 LEU A CD2 
2214 N N   . GLU A 289 ? 0.54678 0.57371 0.55006 -0.09941 -0.00896 0.06566  288 GLU A N   
2215 C CA  . GLU A 289 ? 0.54159 0.56602 0.52842 -0.09307 -0.00563 0.05775  288 GLU A CA  
2216 C C   . GLU A 289 ? 0.53022 0.57505 0.51019 -0.09249 -0.01249 0.05905  288 GLU A C   
2217 O O   . GLU A 289 ? 0.50712 0.57705 0.49797 -0.09557 -0.01726 0.06580  288 GLU A O   
2218 C CB  . GLU A 289 ? 0.53883 0.56922 0.53077 -0.08915 0.00056  0.05622  288 GLU A CB  
2219 C CG  . GLU A 289 ? 0.56900 0.58367 0.56974 -0.08841 0.00836  0.05411  288 GLU A CG  
2220 C CD  . GLU A 289 ? 0.63394 0.61852 0.61872 -0.08559 0.01624  0.04546  288 GLU A CD  
2221 O OE1 . GLU A 289 ? 0.66843 0.63616 0.65839 -0.08639 0.02030  0.04473  288 GLU A OE1 
2222 O OE2 . GLU A 289 ? 0.65936 0.63599 0.62517 -0.08193 0.01913  0.03977  288 GLU A OE2 
2223 N N   . ASP A 290 ? 0.52228 0.55765 0.48404 -0.08766 -0.01254 0.05319  289 ASP A N   
2224 C CA  . ASP A 290 ? 0.51561 0.57222 0.47253 -0.08485 -0.01913 0.05476  289 ASP A CA  
2225 C C   . ASP A 290 ? 0.52107 0.57197 0.46128 -0.07306 -0.01436 0.05034  289 ASP A C   
2226 O O   . ASP A 290 ? 0.52600 0.58923 0.45889 -0.06741 -0.01924 0.05113  289 ASP A O   
2227 C CB  . ASP A 290 ? 0.52967 0.58734 0.48248 -0.09086 -0.02740 0.05444  289 ASP A CB  
2228 C CG  . ASP A 290 ? 0.56270 0.59554 0.49340 -0.08671 -0.02588 0.04729  289 ASP A CG  
2229 O OD1 . ASP A 290 ? 0.56769 0.57486 0.48960 -0.08285 -0.01673 0.04297  289 ASP A OD1 
2230 O OD2 . ASP A 290 ? 0.57543 0.61651 0.49738 -0.08783 -0.03394 0.04617  289 ASP A OD2 
2231 N N   . GLU A 291 ? 0.51619 0.54902 0.45097 -0.06910 -0.00455 0.04616  290 GLU A N   
2232 C CA  . GLU A 291 ? 0.54933 0.57092 0.46699 -0.05856 0.00213  0.04231  290 GLU A CA  
2233 C C   . GLU A 291 ? 0.54563 0.57837 0.46940 -0.05666 0.00761  0.04126  290 GLU A C   
2234 O O   . GLU A 291 ? 0.55889 0.57427 0.47073 -0.05123 0.01710  0.03631  290 GLU A O   
2235 C CB  . GLU A 291 ? 0.57056 0.55825 0.47221 -0.05657 0.01111  0.03694  290 GLU A CB  
2236 C CG  . GLU A 291 ? 0.59341 0.56801 0.48527 -0.05928 0.00667  0.03616  290 GLU A CG  
2237 C CD  . GLU A 291 ? 0.63188 0.58077 0.49597 -0.05129 0.01182  0.03312  290 GLU A CD  
2238 O OE1 . GLU A 291 ? 0.63633 0.56940 0.49013 -0.04507 0.02219  0.03125  290 GLU A OE1 
2239 O OE2 . GLU A 291 ? 0.62836 0.57224 0.47944 -0.05204 0.00562  0.03262  290 GLU A OE2 
2240 N N   . PHE A 292 ? 0.51759 0.57797 0.45812 -0.06209 0.00235  0.04555  291 PHE A N   
2241 C CA  . PHE A 292 ? 0.52308 0.59889 0.46691 -0.06082 0.00612  0.04408  291 PHE A CA  
2242 C C   . PHE A 292 ? 0.49326 0.59751 0.44165 -0.05769 0.00010  0.04879  291 PHE A C   
2243 O O   . PHE A 292 ? 0.49333 0.61770 0.45490 -0.06483 -0.00784 0.05534  291 PHE A O   
2244 C CB  . PHE A 292 ? 0.52118 0.60779 0.48004 -0.07060 0.00608  0.04532  291 PHE A CB  
2245 C CG  . PHE A 292 ? 0.51005 0.57563 0.46877 -0.07354 0.01305  0.04018  291 PHE A CG  
2246 C CD1 . PHE A 292 ? 0.52869 0.58379 0.47928 -0.07257 0.02246  0.03198  291 PHE A CD1 
2247 C CD2 . PHE A 292 ? 0.51042 0.56708 0.47830 -0.07789 0.01125  0.04306  291 PHE A CD2 
2248 C CE1 . PHE A 292 ? 0.55801 0.59748 0.51117 -0.07691 0.02941  0.02706  291 PHE A CE1 
2249 C CE2 . PHE A 292 ? 0.53994 0.58112 0.51073 -0.08004 0.01864  0.03845  291 PHE A CE2 
2250 C CZ  . PHE A 292 ? 0.53532 0.56978 0.49964 -0.08010 0.02744  0.03061  291 PHE A CZ  
2251 N N   . THR A 293 ? 0.48866 0.59403 0.42693 -0.04699 0.00501  0.04571  292 THR A N   
2252 C CA  . THR A 293 ? 0.50084 0.63668 0.44583 -0.04294 0.00165  0.04943  292 THR A CA  
2253 C C   . THR A 293 ? 0.55001 0.70578 0.50346 -0.04979 0.00422  0.04896  292 THR A C   
2254 O O   . THR A 293 ? 0.50393 0.64864 0.45528 -0.05535 0.00904  0.04433  292 THR A O   
2255 C CB  . THR A 293 ? 0.54368 0.67310 0.47548 -0.02651 0.00727  0.04674  292 THR A CB  
2256 O OG1 . THR A 293 ? 0.54059 0.65118 0.46143 -0.02287 0.01935  0.03892  292 THR A OG1 
2257 C CG2 . THR A 293 ? 0.54402 0.65186 0.46313 -0.01920 0.00472  0.04789  292 THR A CG2 
2258 N N   . PRO A 294 ? 0.50529 0.69298 0.46839 -0.05042 0.00092  0.05379  293 PRO A N   
2259 C CA  . PRO A 294 ? 0.53885 0.74546 0.50507 -0.05580 0.00465  0.05278  293 PRO A CA  
2260 C C   . PRO A 294 ? 0.56963 0.76137 0.52131 -0.04928 0.01604  0.04195  293 PRO A C   
2261 O O   . PRO A 294 ? 0.55094 0.74555 0.50064 -0.05726 0.01912  0.03778  293 PRO A O   
2262 C CB  . PRO A 294 ? 0.51043 0.75175 0.48688 -0.05452 0.00163  0.05908  293 PRO A CB  
2263 C CG  . PRO A 294 ? 0.49271 0.73657 0.47794 -0.05688 -0.00779 0.06573  293 PRO A CG  
2264 C CD  . PRO A 294 ? 0.49832 0.70896 0.47122 -0.04938 -0.00697 0.06073  293 PRO A CD  
2265 N N   . PHE A 295 ? 0.57116 0.74617 0.51171 -0.03515 0.02240  0.03737  294 PHE A N   
2266 C CA  . PHE A 295 ? 0.61519 0.76829 0.54002 -0.02924 0.03512  0.02640  294 PHE A CA  
2267 C C   . PHE A 295 ? 0.63058 0.75537 0.54880 -0.03804 0.03836  0.02025  294 PHE A C   
2268 O O   . PHE A 295 ? 0.63849 0.75639 0.54972 -0.04378 0.04594  0.01094  294 PHE A O   
2269 C CB  . PHE A 295 ? 0.66380 0.80123 0.57794 -0.01035 0.04153  0.02524  294 PHE A CB  
2270 C CG  . PHE A 295 ? 0.73050 0.83701 0.62646 -0.00382 0.05651  0.01409  294 PHE A CG  
2271 C CD1 . PHE A 295 ? 0.78771 0.90264 0.67912 0.00016  0.06613  0.00689  294 PHE A CD1 
2272 C CD2 . PHE A 295 ? 0.79203 0.85921 0.67430 -0.00255 0.06234  0.01022  294 PHE A CD2 
2273 C CE1 . PHE A 295 ? 0.84856 0.93097 0.72188 0.00489  0.08116  -0.00478 294 PHE A CE1 
2274 C CE2 . PHE A 295 ? 0.82055 0.85602 0.68559 0.00160  0.07740  -0.00023 294 PHE A CE2 
2275 C CZ  . PHE A 295 ? 0.87121 0.91314 0.73166 0.00513  0.08675  -0.00815 294 PHE A CZ  
2276 N N   . ASP A 296 ? 0.59234 0.70150 0.51261 -0.03987 0.03332  0.02442  295 ASP A N   
2277 C CA  . ASP A 296 ? 0.60082 0.68758 0.51865 -0.04871 0.03682  0.01931  295 ASP A CA  
2278 C C   . ASP A 296 ? 0.61430 0.72223 0.54442 -0.06299 0.03269  0.01909  295 ASP A C   
2279 O O   . ASP A 296 ? 0.63002 0.72969 0.55698 -0.07034 0.03849  0.01078  295 ASP A O   
2280 C CB  . ASP A 296 ? 0.56308 0.63391 0.48238 -0.04843 0.03207  0.02448  295 ASP A CB  
2281 C CG  . ASP A 296 ? 0.59329 0.64270 0.49718 -0.03449 0.03525  0.02538  295 ASP A CG  
2282 O OD1 . ASP A 296 ? 0.62337 0.65499 0.51277 -0.02546 0.04541  0.02008  295 ASP A OD1 
2283 O OD2 . ASP A 296 ? 0.57599 0.62562 0.48117 -0.03253 0.02759  0.03153  295 ASP A OD2 
2284 N N   . VAL A 297 ? 0.58421 0.72048 0.52816 -0.06746 0.02258  0.02866  296 VAL A N   
2285 C CA  . VAL A 297 ? 0.60183 0.75958 0.55676 -0.07938 0.01736  0.03172  296 VAL A CA  
2286 C C   . VAL A 297 ? 0.61306 0.78408 0.55975 -0.08267 0.02275  0.02368  296 VAL A C   
2287 O O   . VAL A 297 ? 0.60965 0.78427 0.55676 -0.09197 0.02338  0.01845  296 VAL A O   
2288 C CB  . VAL A 297 ? 0.57428 0.75553 0.54323 -0.08278 0.00687  0.04514  296 VAL A CB  
2289 C CG1 . VAL A 297 ? 0.54278 0.74577 0.52112 -0.09320 0.00146  0.05079  296 VAL A CG1 
2290 C CG2 . VAL A 297 ? 0.54808 0.71300 0.52310 -0.08135 0.00234  0.05062  296 VAL A CG2 
2291 N N   . VAL A 298 ? 0.60746 0.78791 0.54687 -0.07534 0.02677  0.02206  297 VAL A N   
2292 C CA  . VAL A 298 ? 0.61248 0.80363 0.54122 -0.07811 0.03363  0.01277  297 VAL A CA  
2293 C C   . VAL A 298 ? 0.64621 0.80870 0.56105 -0.07959 0.04432  -0.00226 297 VAL A C   
2294 O O   . VAL A 298 ? 0.64692 0.81604 0.55643 -0.09032 0.04654  -0.01099 297 VAL A O   
2295 C CB  . VAL A 298 ? 0.62277 0.82724 0.54734 -0.06746 0.03829  0.01338  297 VAL A CB  
2296 C CG1 . VAL A 298 ? 0.60339 0.80464 0.51140 -0.06657 0.05040  -0.00069 297 VAL A CG1 
2297 C CG2 . VAL A 298 ? 0.58862 0.82865 0.52619 -0.07209 0.02930  0.02632  297 VAL A CG2 
2298 N N   . ARG A 299 ? 0.67445 0.80472 0.58235 -0.07000 0.05102  -0.00534 298 ARG A N   
2299 C CA  . ARG A 299 ? 0.66114 0.75922 0.55482 -0.07180 0.06315  -0.01893 298 ARG A CA  
2300 C C   . ARG A 299 ? 0.66736 0.76498 0.56839 -0.08732 0.06022  -0.02247 298 ARG A C   
2301 O O   . ARG A 299 ? 0.70282 0.79483 0.59618 -0.09743 0.06698  -0.03526 298 ARG A O   
2302 C CB  . ARG A 299 ? 0.68224 0.74586 0.56666 -0.05766 0.07005  -0.01776 298 ARG A CB  
2303 C CG  . ARG A 299 ? 0.78131 0.80969 0.65773 -0.06285 0.07862  -0.02524 298 ARG A CG  
2304 C CD  . ARG A 299 ? 0.79894 0.80216 0.67079 -0.05120 0.07927  -0.01764 298 ARG A CD  
2305 N NE  . ARG A 299 ? 0.76544 0.73940 0.63250 -0.05833 0.08649  -0.02245 298 ARG A NE  
2306 C CZ  . ARG A 299 ? 0.75303 0.70645 0.61632 -0.05279 0.08671  -0.01631 298 ARG A CZ  
2307 N NH1 . ARG A 299 ? 0.76511 0.72408 0.62838 -0.04069 0.07871  -0.00566 298 ARG A NH1 
2308 N NH2 . ARG A 299 ? 0.65986 0.58813 0.51895 -0.06065 0.09535  -0.02148 298 ARG A NH2 
2309 N N   . GLN A 300 ? 0.66151 0.76616 0.57824 -0.08975 0.05053  -0.01189 299 GLN A N   
2310 C CA  . GLN A 300 ? 0.65579 0.76176 0.58270 -0.10217 0.04856  -0.01452 299 GLN A CA  
2311 C C   . GLN A 300 ? 0.64641 0.78828 0.58248 -0.11415 0.04012  -0.01380 299 GLN A C   
2312 O O   . GLN A 300 ? 0.63878 0.78530 0.57821 -0.12590 0.04119  -0.02175 299 GLN A O   
2313 C CB  . GLN A 300 ? 0.62140 0.72108 0.56176 -0.09949 0.04281  -0.00415 299 GLN A CB  
2314 C CG  . GLN A 300 ? 0.58099 0.68031 0.53359 -0.10995 0.04339  -0.00736 299 GLN A CG  
2315 C CD  . GLN A 300 ? 0.58451 0.67269 0.54821 -0.10615 0.04102  0.00081  299 GLN A CD  
2316 O OE1 . GLN A 300 ? 0.55414 0.65275 0.53479 -0.11241 0.03807  0.00302  299 GLN A OE1 
2317 N NE2 . GLN A 300 ? 0.55589 0.62377 0.50994 -0.09554 0.04251  0.00494  299 GLN A NE2 
2318 N N   . CYS A 301 ? 0.64644 0.81539 0.58630 -0.11209 0.03173  -0.00412 300 CYS A N   
2319 C CA  . CYS A 301 ? 0.63588 0.83933 0.58099 -0.12255 0.02341  -0.00143 300 CYS A CA  
2320 C C   . CYS A 301 ? 0.64520 0.85648 0.57227 -0.12789 0.02978  -0.01467 300 CYS A C   
2321 O O   . CYS A 301 ? 0.66962 0.90947 0.59665 -0.13815 0.02336  -0.01478 300 CYS A O   
2322 C CB  . CYS A 301 ? 0.62595 0.85340 0.58181 -0.11934 0.01261  0.01618  300 CYS A CB  
2323 S SG  . CYS A 301 ? 0.63795 0.85623 0.61443 -0.11527 0.00508  0.03091  300 CYS A SG  
2324 N N   . SER A 302 ? 0.66183 0.84786 0.57245 -0.12069 0.04250  -0.02571 301 SER A N   
2325 C CA  . SER A 302 ? 0.67908 0.86608 0.57049 -0.12479 0.05148  -0.04054 301 SER A CA  
2326 C C   . SER A 302 ? 0.70420 0.85904 0.58259 -0.13068 0.06436  -0.05911 301 SER A C   
2327 O O   . SER A 302 ? 0.71317 0.86641 0.57461 -0.13761 0.07237  -0.07429 301 SER A O   
2328 C CB  . SER A 302 ? 0.70126 0.88621 0.58346 -0.11046 0.05810  -0.03878 301 SER A CB  
2329 O OG  . SER A 302 ? 0.74358 0.92393 0.60574 -0.11264 0.06970  -0.05478 301 SER A OG  
2330 N N   . GLY A 303 ? 0.68655 0.81421 0.57081 -0.12894 0.06777  -0.05887 302 GLY A N   
2331 C CA  . GLY A 303 ? 0.68487 0.78179 0.55828 -0.13732 0.08044  -0.07542 302 GLY A CA  
2332 C C   . GLY A 303 ? 0.71974 0.77587 0.57190 -0.12626 0.09760  -0.08497 302 GLY A C   
2333 O O   . GLY A 303 ? 0.69908 0.73330 0.53588 -0.13538 0.11005  -0.10225 302 GLY A O   
2334 N N   . VAL A 304 ? 0.75186 0.79699 0.60278 -0.10686 0.09873  -0.07417 303 VAL A N   
2335 C CA  . VAL A 304 ? 0.75918 0.76626 0.59126 -0.09246 0.11453  -0.08027 303 VAL A CA  
2336 C C   . VAL A 304 ? 0.75998 0.72341 0.58477 -0.09352 0.12529  -0.08463 303 VAL A C   
2337 O O   . VAL A 304 ? 0.75973 0.68972 0.56704 -0.09736 0.14099  -0.09902 303 VAL A O   
2338 C CB  . VAL A 304 ? 0.74550 0.75980 0.58109 -0.07095 0.11072  -0.06599 303 VAL A CB  
2339 C CG1 . VAL A 304 ? 0.77182 0.74850 0.58911 -0.05335 0.12684  -0.07077 303 VAL A CG1 
2340 C CG2 . VAL A 304 ? 0.76937 0.82719 0.61261 -0.07151 0.10180  -0.06136 303 VAL A CG2 
# 
