data_9M10
# 
_entry.id   9M10 
# 
_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   9M10         pdb_00009m10 10.2210/pdb9m10/pdb 
WWPDB D_1300056695 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-11 
_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                        9M10 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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              ito.str@tmd.ac.jp 
_pdbx_contact_author.name_first         Nobutoshi 
_pdbx_contact_author.name_last          Ito 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0839-0384 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Thilakarathne, N.M.H.N.' 1 ? 
'Hanazono, Y.'            2 ? 
'Ito, N.'                 3 ? 
'Kagechika, H.'           4 ? 
'Fujii, S.'               5 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_id_ASTM           BMECEP 
_citation.journal_id_CSD            1200 
_citation.journal_id_ISSN           1464-3391 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                118261 
_citation.page_last                 ? 
_citation.title                     
;Structure-activity relationship and crystallographic analyses of non-secosteroidal vitamin D receptor ligands bearing diphenylsilane core as a hydrophobic pharmacophore
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2025.118261 
_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 'Mudiyanselage, H.N.T.N.' 1 ? 
primary 'Misawa, T.'              2 ? 
primary 'Ochiai, K.'              3 ? 
primary 'Demizu, Y.'              4 ? 
primary 'Hanazono, Y.'            5 ? 
primary 'Ito, N.'                 6 ? 
primary 'Fujii, S.'               7 ? 
# 
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 'Vitamin D3 receptor' 30595.037 1  ? ? ? ? 
2 polymer     syn 'Mediator of RNA polymerase II transcription subunit 1' 1570.898  1  ? ? ? ? 
3 non-polymer syn 
;(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)-3-(trifluoromethyl)phenyl]-dimethyl-silyl]-2-(trifluoromethyl)phenoxy]-4-oxidanyl-pentanoic acid
;
596.631   1  ? ? ? ? 
4 water       nat water 18.015    55 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'VDR,1,25-dihydroxyvitamin D3 receptor,Nuclear receptor subfamily 1 group I member 1' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GSHMGSPNSPLKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGSVTLDLSPLSMLPHLADLVSY
SIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLRSNQSFTMDDMSWDCGSQDYKYDVTDVSKAGHTLELIEPLIKF
QVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAKLVEAIQDRLSNTLQTYIRCRHPPPGSHQLYAKMIQKLADLRSLNEE
HSKQYRSLSFQPENSMKLTPLVLEVFGNEIS
;
;GSHMGSPNSPLKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGSVTLDLSPLSMLPHLADLVSY
SIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLRSNQSFTMDDMSWDCGSQDYKYDVTDVSKAGHTLELIEPLIKF
QVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAKLVEAIQDRLSNTLQTYIRCRHPPPGSHQLYAKMIQKLADLRSLNEE
HSKQYRSLSFQPENSMKLTPLVLEVFGNEIS
;
A ? 
2 'polypeptide(L)' no no KNHPMLMNLLKDN KNHPMLMNLLKDN C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 
;(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)-3-(trifluoromethyl)phenyl]-dimethyl-silyl]-2-(trifluoromethyl)phenoxy]-4-oxidanyl-pentanoic acid
;
A1L7X 
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   HIS n 
1 4   MET n 
1 5   GLY n 
1 6   SER n 
1 7   PRO n 
1 8   ASN n 
1 9   SER n 
1 10  PRO n 
1 11  LEU n 
1 12  LYS n 
1 13  ASP n 
1 14  SER n 
1 15  LEU n 
1 16  ARG n 
1 17  PRO n 
1 18  LYS n 
1 19  LEU n 
1 20  SER n 
1 21  GLU n 
1 22  GLU n 
1 23  GLN n 
1 24  GLN n 
1 25  HIS n 
1 26  ILE n 
1 27  ILE n 
1 28  ALA n 
1 29  ILE n 
1 30  LEU n 
1 31  LEU n 
1 32  ASP n 
1 33  ALA n 
1 34  HIS n 
1 35  HIS n 
1 36  LYS n 
1 37  THR n 
1 38  TYR n 
1 39  ASP n 
1 40  PRO n 
1 41  THR n 
1 42  TYR n 
1 43  ALA n 
1 44  ASP n 
1 45  PHE n 
1 46  ARG n 
1 47  ASP n 
1 48  PHE n 
1 49  ARG n 
1 50  PRO n 
1 51  PRO n 
1 52  VAL n 
1 53  ARG n 
1 54  MET n 
1 55  ASP n 
1 56  GLY n 
1 57  SER n 
1 58  THR n 
1 59  GLY n 
1 60  SER n 
1 61  VAL n 
1 62  THR n 
1 63  LEU n 
1 64  ASP n 
1 65  LEU n 
1 66  SER n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  MET n 
1 71  LEU n 
1 72  PRO n 
1 73  HIS n 
1 74  LEU n 
1 75  ALA n 
1 76  ASP n 
1 77  LEU n 
1 78  VAL n 
1 79  SER n 
1 80  TYR n 
1 81  SER n 
1 82  ILE n 
1 83  GLN n 
1 84  LYS n 
1 85  VAL n 
1 86  ILE n 
1 87  GLY n 
1 88  PHE n 
1 89  ALA n 
1 90  LYS n 
1 91  MET n 
1 92  ILE n 
1 93  PRO n 
1 94  GLY n 
1 95  PHE n 
1 96  ARG n 
1 97  ASP n 
1 98  LEU n 
1 99  THR n 
1 100 SER n 
1 101 ASP n 
1 102 ASP n 
1 103 GLN n 
1 104 ILE n 
1 105 VAL n 
1 106 LEU n 
1 107 LEU n 
1 108 LYS n 
1 109 SER n 
1 110 SER n 
1 111 ALA n 
1 112 ILE n 
1 113 GLU n 
1 114 VAL n 
1 115 ILE n 
1 116 MET n 
1 117 LEU n 
1 118 ARG n 
1 119 SER n 
1 120 ASN n 
1 121 GLN n 
1 122 SER n 
1 123 PHE n 
1 124 THR n 
1 125 MET n 
1 126 ASP n 
1 127 ASP n 
1 128 MET n 
1 129 SER n 
1 130 TRP n 
1 131 ASP n 
1 132 CYS n 
1 133 GLY n 
1 134 SER n 
1 135 GLN n 
1 136 ASP n 
1 137 TYR n 
1 138 LYS n 
1 139 TYR n 
1 140 ASP n 
1 141 VAL n 
1 142 THR n 
1 143 ASP n 
1 144 VAL n 
1 145 SER n 
1 146 LYS n 
1 147 ALA n 
1 148 GLY n 
1 149 HIS n 
1 150 THR n 
1 151 LEU n 
1 152 GLU n 
1 153 LEU n 
1 154 ILE n 
1 155 GLU n 
1 156 PRO n 
1 157 LEU n 
1 158 ILE n 
1 159 LYS n 
1 160 PHE n 
1 161 GLN n 
1 162 VAL n 
1 163 GLY n 
1 164 LEU n 
1 165 LYS n 
1 166 LYS n 
1 167 LEU n 
1 168 ASN n 
1 169 LEU n 
1 170 HIS n 
1 171 GLU n 
1 172 GLU n 
1 173 GLU n 
1 174 HIS n 
1 175 VAL n 
1 176 LEU n 
1 177 LEU n 
1 178 MET n 
1 179 ALA n 
1 180 ILE n 
1 181 CYS n 
1 182 ILE n 
1 183 VAL n 
1 184 SER n 
1 185 PRO n 
1 186 ASP n 
1 187 ARG n 
1 188 PRO n 
1 189 GLY n 
1 190 VAL n 
1 191 GLN n 
1 192 ASP n 
1 193 ALA n 
1 194 LYS n 
1 195 LEU n 
1 196 VAL n 
1 197 GLU n 
1 198 ALA n 
1 199 ILE n 
1 200 GLN n 
1 201 ASP n 
1 202 ARG n 
1 203 LEU n 
1 204 SER n 
1 205 ASN n 
1 206 THR n 
1 207 LEU n 
1 208 GLN n 
1 209 THR n 
1 210 TYR n 
1 211 ILE n 
1 212 ARG n 
1 213 CYS n 
1 214 ARG n 
1 215 HIS n 
1 216 PRO n 
1 217 PRO n 
1 218 PRO n 
1 219 GLY n 
1 220 SER n 
1 221 HIS n 
1 222 GLN n 
1 223 LEU n 
1 224 TYR n 
1 225 ALA n 
1 226 LYS n 
1 227 MET n 
1 228 ILE n 
1 229 GLN n 
1 230 LYS n 
1 231 LEU n 
1 232 ALA n 
1 233 ASP n 
1 234 LEU n 
1 235 ARG n 
1 236 SER n 
1 237 LEU n 
1 238 ASN n 
1 239 GLU n 
1 240 GLU n 
1 241 HIS n 
1 242 SER n 
1 243 LYS n 
1 244 GLN n 
1 245 TYR n 
1 246 ARG n 
1 247 SER n 
1 248 LEU n 
1 249 SER n 
1 250 PHE n 
1 251 GLN n 
1 252 PRO n 
1 253 GLU n 
1 254 ASN n 
1 255 SER n 
1 256 MET n 
1 257 LYS n 
1 258 LEU n 
1 259 THR n 
1 260 PRO n 
1 261 LEU n 
1 262 VAL n 
1 263 LEU n 
1 264 GLU n 
1 265 VAL n 
1 266 PHE n 
1 267 GLY n 
1 268 ASN n 
1 269 GLU n 
1 270 ILE n 
1 271 SER n 
2 1   LYS n 
2 2   ASN n 
2 3   HIS n 
2 4   PRO n 
2 5   MET n 
2 6   LEU n 
2 7   MET n 
2 8   ASN n 
2 9   LEU n 
2 10  LEU n 
2 11  LYS n 
2 12  ASP n 
2 13  ASN 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                   271 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Vdr, Nr1i1' 
_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      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_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                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       13 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
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 
A1L7X non-polymer         . 
;(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)-3-(trifluoromethyl)phenyl]-dimethyl-silyl]-2-(trifluoromethyl)phenoxy]-4-oxidanyl-pentanoic acid
;
? 'C27 H34 F6 O6 Si' 596.631 
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   GLY 1   106 ?   ?   ?   A . n 
A 1 2   SER 2   107 ?   ?   ?   A . n 
A 1 3   HIS 3   108 ?   ?   ?   A . n 
A 1 4   MET 4   109 ?   ?   ?   A . n 
A 1 5   GLY 5   110 ?   ?   ?   A . n 
A 1 6   SER 6   111 ?   ?   ?   A . n 
A 1 7   PRO 7   112 ?   ?   ?   A . n 
A 1 8   ASN 8   113 ?   ?   ?   A . n 
A 1 9   SER 9   114 ?   ?   ?   A . n 
A 1 10  PRO 10  115 ?   ?   ?   A . n 
A 1 11  LEU 11  116 ?   ?   ?   A . n 
A 1 12  LYS 12  117 ?   ?   ?   A . n 
A 1 13  ASP 13  118 ?   ?   ?   A . n 
A 1 14  SER 14  119 ?   ?   ?   A . n 
A 1 15  LEU 15  120 ?   ?   ?   A . n 
A 1 16  ARG 16  121 ?   ?   ?   A . n 
A 1 17  PRO 17  122 ?   ?   ?   A . n 
A 1 18  LYS 18  123 123 LYS LYS A . n 
A 1 19  LEU 19  124 124 LEU LEU A . n 
A 1 20  SER 20  125 125 SER SER A . n 
A 1 21  GLU 21  126 126 GLU GLU A . n 
A 1 22  GLU 22  127 127 GLU GLU A . n 
A 1 23  GLN 23  128 128 GLN GLN A . n 
A 1 24  GLN 24  129 129 GLN GLN A . n 
A 1 25  HIS 25  130 130 HIS HIS A . n 
A 1 26  ILE 26  131 131 ILE ILE A . n 
A 1 27  ILE 27  132 132 ILE ILE A . n 
A 1 28  ALA 28  133 133 ALA ALA A . n 
A 1 29  ILE 29  134 134 ILE ILE A . n 
A 1 30  LEU 30  135 135 LEU LEU A . n 
A 1 31  LEU 31  136 136 LEU LEU A . n 
A 1 32  ASP 32  137 137 ASP ASP A . n 
A 1 33  ALA 33  138 138 ALA ALA A . n 
A 1 34  HIS 34  139 139 HIS HIS A . n 
A 1 35  HIS 35  140 140 HIS HIS A . n 
A 1 36  LYS 36  141 141 LYS LYS A . n 
A 1 37  THR 37  142 142 THR THR A . n 
A 1 38  TYR 38  143 143 TYR TYR A . n 
A 1 39  ASP 39  144 144 ASP ASP A . n 
A 1 40  PRO 40  145 145 PRO PRO A . n 
A 1 41  THR 41  146 146 THR THR A . n 
A 1 42  TYR 42  147 147 TYR TYR A . n 
A 1 43  ALA 43  148 148 ALA ALA A . n 
A 1 44  ASP 44  149 149 ASP ASP A . n 
A 1 45  PHE 45  150 150 PHE PHE A . n 
A 1 46  ARG 46  151 151 ARG ARG A . n 
A 1 47  ASP 47  152 152 ASP ASP A . n 
A 1 48  PHE 48  153 153 PHE PHE A . n 
A 1 49  ARG 49  154 154 ARG ARG A . n 
A 1 50  PRO 50  155 155 PRO PRO A . n 
A 1 51  PRO 51  156 156 PRO PRO A . n 
A 1 52  VAL 52  157 157 VAL VAL A . n 
A 1 53  ARG 53  158 158 ARG ARG A . n 
A 1 54  MET 54  159 159 MET MET A . n 
A 1 55  ASP 55  207 ?   ?   ?   A . n 
A 1 56  GLY 56  208 ?   ?   ?   A . n 
A 1 57  SER 57  209 ?   ?   ?   A . n 
A 1 58  THR 58  210 ?   ?   ?   A . n 
A 1 59  GLY 59  211 ?   ?   ?   A . n 
A 1 60  SER 60  212 ?   ?   ?   A . n 
A 1 61  VAL 61  213 ?   ?   ?   A . n 
A 1 62  THR 62  214 ?   ?   ?   A . n 
A 1 63  LEU 63  215 ?   ?   ?   A . n 
A 1 64  ASP 64  216 ?   ?   ?   A . n 
A 1 65  LEU 65  217 ?   ?   ?   A . n 
A 1 66  SER 66  218 218 SER SER A . n 
A 1 67  PRO 67  219 219 PRO PRO A . n 
A 1 68  LEU 68  220 220 LEU LEU A . n 
A 1 69  SER 69  221 221 SER SER A . n 
A 1 70  MET 70  222 222 MET MET A . n 
A 1 71  LEU 71  223 223 LEU LEU A . n 
A 1 72  PRO 72  224 224 PRO PRO A . n 
A 1 73  HIS 73  225 225 HIS HIS A . n 
A 1 74  LEU 74  226 226 LEU LEU A . n 
A 1 75  ALA 75  227 227 ALA ALA A . n 
A 1 76  ASP 76  228 228 ASP ASP A . n 
A 1 77  LEU 77  229 229 LEU LEU A . n 
A 1 78  VAL 78  230 230 VAL VAL A . n 
A 1 79  SER 79  231 231 SER SER A . n 
A 1 80  TYR 80  232 232 TYR TYR A . n 
A 1 81  SER 81  233 233 SER SER A . n 
A 1 82  ILE 82  234 234 ILE ILE A . n 
A 1 83  GLN 83  235 235 GLN GLN A . n 
A 1 84  LYS 84  236 236 LYS LYS A . n 
A 1 85  VAL 85  237 237 VAL VAL A . n 
A 1 86  ILE 86  238 238 ILE ILE A . n 
A 1 87  GLY 87  239 239 GLY GLY A . n 
A 1 88  PHE 88  240 240 PHE PHE A . n 
A 1 89  ALA 89  241 241 ALA ALA A . n 
A 1 90  LYS 90  242 242 LYS LYS A . n 
A 1 91  MET 91  243 243 MET MET A . n 
A 1 92  ILE 92  244 244 ILE ILE A . n 
A 1 93  PRO 93  245 245 PRO PRO A . n 
A 1 94  GLY 94  246 246 GLY GLY A . n 
A 1 95  PHE 95  247 247 PHE PHE A . n 
A 1 96  ARG 96  248 248 ARG ARG A . n 
A 1 97  ASP 97  249 249 ASP ASP A . n 
A 1 98  LEU 98  250 250 LEU LEU A . n 
A 1 99  THR 99  251 251 THR THR A . n 
A 1 100 SER 100 252 252 SER SER A . n 
A 1 101 ASP 101 253 253 ASP ASP A . n 
A 1 102 ASP 102 254 254 ASP ASP A . n 
A 1 103 GLN 103 255 255 GLN GLN A . n 
A 1 104 ILE 104 256 256 ILE ILE A . n 
A 1 105 VAL 105 257 257 VAL VAL A . n 
A 1 106 LEU 106 258 258 LEU LEU A . n 
A 1 107 LEU 107 259 259 LEU LEU A . n 
A 1 108 LYS 108 260 260 LYS LYS A . n 
A 1 109 SER 109 261 261 SER SER A . n 
A 1 110 SER 110 262 262 SER SER A . n 
A 1 111 ALA 111 263 263 ALA ALA A . n 
A 1 112 ILE 112 264 264 ILE ILE A . n 
A 1 113 GLU 113 265 265 GLU GLU A . n 
A 1 114 VAL 114 266 266 VAL VAL A . n 
A 1 115 ILE 115 267 267 ILE ILE A . n 
A 1 116 MET 116 268 268 MET MET A . n 
A 1 117 LEU 117 269 269 LEU LEU A . n 
A 1 118 ARG 118 270 270 ARG ARG A . n 
A 1 119 SER 119 271 271 SER SER A . n 
A 1 120 ASN 120 272 272 ASN ASN A . n 
A 1 121 GLN 121 273 273 GLN GLN A . n 
A 1 122 SER 122 274 274 SER SER A . n 
A 1 123 PHE 123 275 275 PHE PHE A . n 
A 1 124 THR 124 276 276 THR THR A . n 
A 1 125 MET 125 277 277 MET MET A . n 
A 1 126 ASP 126 278 278 ASP ASP A . n 
A 1 127 ASP 127 279 279 ASP ASP A . n 
A 1 128 MET 128 280 280 MET MET A . n 
A 1 129 SER 129 281 281 SER SER A . n 
A 1 130 TRP 130 282 282 TRP TRP A . n 
A 1 131 ASP 131 283 283 ASP ASP A . n 
A 1 132 CYS 132 284 284 CYS CYS A . n 
A 1 133 GLY 133 285 285 GLY GLY A . n 
A 1 134 SER 134 286 286 SER SER A . n 
A 1 135 GLN 135 287 287 GLN GLN A . n 
A 1 136 ASP 136 288 288 ASP ASP A . n 
A 1 137 TYR 137 289 289 TYR TYR A . n 
A 1 138 LYS 138 290 290 LYS LYS A . n 
A 1 139 TYR 139 291 291 TYR TYR A . n 
A 1 140 ASP 140 292 292 ASP ASP A . n 
A 1 141 VAL 141 293 293 VAL VAL A . n 
A 1 142 THR 142 294 294 THR THR A . n 
A 1 143 ASP 143 295 295 ASP ASP A . n 
A 1 144 VAL 144 296 296 VAL VAL A . n 
A 1 145 SER 145 297 297 SER SER A . n 
A 1 146 LYS 146 298 298 LYS LYS A . n 
A 1 147 ALA 147 299 299 ALA ALA A . n 
A 1 148 GLY 148 300 300 GLY GLY A . n 
A 1 149 HIS 149 301 301 HIS HIS A . n 
A 1 150 THR 150 302 302 THR THR A . n 
A 1 151 LEU 151 303 303 LEU LEU A . n 
A 1 152 GLU 152 304 304 GLU GLU A . n 
A 1 153 LEU 153 305 305 LEU LEU A . n 
A 1 154 ILE 154 306 306 ILE ILE A . n 
A 1 155 GLU 155 307 307 GLU GLU A . n 
A 1 156 PRO 156 308 308 PRO PRO A . n 
A 1 157 LEU 157 309 309 LEU LEU A . n 
A 1 158 ILE 158 310 310 ILE ILE A . n 
A 1 159 LYS 159 311 311 LYS LYS A . n 
A 1 160 PHE 160 312 312 PHE PHE A . n 
A 1 161 GLN 161 313 313 GLN GLN A . n 
A 1 162 VAL 162 314 314 VAL VAL A . n 
A 1 163 GLY 163 315 315 GLY GLY A . n 
A 1 164 LEU 164 316 316 LEU LEU A . n 
A 1 165 LYS 165 317 317 LYS LYS A . n 
A 1 166 LYS 166 318 318 LYS LYS A . n 
A 1 167 LEU 167 319 319 LEU LEU A . n 
A 1 168 ASN 168 320 320 ASN ASN A . n 
A 1 169 LEU 169 321 321 LEU LEU A . n 
A 1 170 HIS 170 322 322 HIS HIS A . n 
A 1 171 GLU 171 323 323 GLU GLU A . n 
A 1 172 GLU 172 324 324 GLU GLU A . n 
A 1 173 GLU 173 325 325 GLU GLU A . n 
A 1 174 HIS 174 326 326 HIS HIS A . n 
A 1 175 VAL 175 327 327 VAL VAL A . n 
A 1 176 LEU 176 328 328 LEU LEU A . n 
A 1 177 LEU 177 329 329 LEU LEU A . n 
A 1 178 MET 178 330 330 MET MET A . n 
A 1 179 ALA 179 331 331 ALA ALA A . n 
A 1 180 ILE 180 332 332 ILE ILE A . n 
A 1 181 CYS 181 333 333 CYS CYS A . n 
A 1 182 ILE 182 334 334 ILE ILE A . n 
A 1 183 VAL 183 335 335 VAL VAL A . n 
A 1 184 SER 184 336 336 SER SER A . n 
A 1 185 PRO 185 337 337 PRO PRO A . n 
A 1 186 ASP 186 338 338 ASP ASP A . n 
A 1 187 ARG 187 339 339 ARG ARG A . n 
A 1 188 PRO 188 340 340 PRO PRO A . n 
A 1 189 GLY 189 341 341 GLY GLY A . n 
A 1 190 VAL 190 342 342 VAL VAL A . n 
A 1 191 GLN 191 343 343 GLN GLN A . n 
A 1 192 ASP 192 344 344 ASP ASP A . n 
A 1 193 ALA 193 345 345 ALA ALA A . n 
A 1 194 LYS 194 346 346 LYS LYS A . n 
A 1 195 LEU 195 347 347 LEU LEU A . n 
A 1 196 VAL 196 348 348 VAL VAL A . n 
A 1 197 GLU 197 349 349 GLU GLU A . n 
A 1 198 ALA 198 350 350 ALA ALA A . n 
A 1 199 ILE 199 351 351 ILE ILE A . n 
A 1 200 GLN 200 352 352 GLN GLN A . n 
A 1 201 ASP 201 353 353 ASP ASP A . n 
A 1 202 ARG 202 354 354 ARG ARG A . n 
A 1 203 LEU 203 355 355 LEU LEU A . n 
A 1 204 SER 204 356 356 SER SER A . n 
A 1 205 ASN 205 357 357 ASN ASN A . n 
A 1 206 THR 206 358 358 THR THR A . n 
A 1 207 LEU 207 359 359 LEU LEU A . n 
A 1 208 GLN 208 360 360 GLN GLN A . n 
A 1 209 THR 209 361 361 THR THR A . n 
A 1 210 TYR 210 362 362 TYR TYR A . n 
A 1 211 ILE 211 363 363 ILE ILE A . n 
A 1 212 ARG 212 364 364 ARG ARG A . n 
A 1 213 CYS 213 365 365 CYS CYS A . n 
A 1 214 ARG 214 366 366 ARG ARG A . n 
A 1 215 HIS 215 367 367 HIS HIS A . n 
A 1 216 PRO 216 368 368 PRO PRO A . n 
A 1 217 PRO 217 369 369 PRO PRO A . n 
A 1 218 PRO 218 370 370 PRO PRO A . n 
A 1 219 GLY 219 371 371 GLY GLY A . n 
A 1 220 SER 220 372 372 SER SER A . n 
A 1 221 HIS 221 373 373 HIS HIS A . n 
A 1 222 GLN 222 374 374 GLN GLN A . n 
A 1 223 LEU 223 375 375 LEU LEU A . n 
A 1 224 TYR 224 376 376 TYR TYR A . n 
A 1 225 ALA 225 377 377 ALA ALA A . n 
A 1 226 LYS 226 378 378 LYS LYS A . n 
A 1 227 MET 227 379 379 MET MET A . n 
A 1 228 ILE 228 380 380 ILE ILE A . n 
A 1 229 GLN 229 381 381 GLN GLN A . n 
A 1 230 LYS 230 382 382 LYS LYS A . n 
A 1 231 LEU 231 383 383 LEU LEU A . n 
A 1 232 ALA 232 384 384 ALA ALA A . n 
A 1 233 ASP 233 385 385 ASP ASP A . n 
A 1 234 LEU 234 386 386 LEU LEU A . n 
A 1 235 ARG 235 387 387 ARG ARG A . n 
A 1 236 SER 236 388 388 SER SER A . n 
A 1 237 LEU 237 389 389 LEU LEU A . n 
A 1 238 ASN 238 390 390 ASN ASN A . n 
A 1 239 GLU 239 391 391 GLU GLU A . n 
A 1 240 GLU 240 392 392 GLU GLU A . n 
A 1 241 HIS 241 393 393 HIS HIS A . n 
A 1 242 SER 242 394 394 SER SER A . n 
A 1 243 LYS 243 395 395 LYS LYS A . n 
A 1 244 GLN 244 396 396 GLN GLN A . n 
A 1 245 TYR 245 397 397 TYR TYR A . n 
A 1 246 ARG 246 398 398 ARG ARG A . n 
A 1 247 SER 247 399 399 SER SER A . n 
A 1 248 LEU 248 400 400 LEU LEU A . n 
A 1 249 SER 249 401 401 SER SER A . n 
A 1 250 PHE 250 402 402 PHE PHE A . n 
A 1 251 GLN 251 403 403 GLN GLN A . n 
A 1 252 PRO 252 404 404 PRO PRO A . n 
A 1 253 GLU 253 405 405 GLU GLU A . n 
A 1 254 ASN 254 406 406 ASN ASN A . n 
A 1 255 SER 255 407 407 SER SER A . n 
A 1 256 MET 256 408 408 MET MET A . n 
A 1 257 LYS 257 409 409 LYS LYS A . n 
A 1 258 LEU 258 410 410 LEU LEU A . n 
A 1 259 THR 259 411 411 THR THR A . n 
A 1 260 PRO 260 412 412 PRO PRO A . n 
A 1 261 LEU 261 413 413 LEU LEU A . n 
A 1 262 VAL 262 414 414 VAL VAL A . n 
A 1 263 LEU 263 415 415 LEU LEU A . n 
A 1 264 GLU 264 416 416 GLU GLU A . n 
A 1 265 VAL 265 417 417 VAL VAL A . n 
A 1 266 PHE 266 418 418 PHE PHE A . n 
A 1 267 GLY 267 419 419 GLY GLY A . n 
A 1 268 ASN 268 420 420 ASN ASN A . n 
A 1 269 GLU 269 421 ?   ?   ?   A . n 
A 1 270 ILE 270 422 ?   ?   ?   A . n 
A 1 271 SER 271 423 ?   ?   ?   A . n 
B 2 1   LYS 1   625 625 LYS LYS C . n 
B 2 2   ASN 2   626 626 ASN ASN C . n 
B 2 3   HIS 3   627 627 HIS HIS C . n 
B 2 4   PRO 4   628 628 PRO PRO C . n 
B 2 5   MET 5   629 629 MET MET C . n 
B 2 6   LEU 6   630 630 LEU LEU C . n 
B 2 7   MET 7   631 631 MET MET C . n 
B 2 8   ASN 8   632 632 ASN ASN C . n 
B 2 9   LEU 9   633 633 LEU LEU C . n 
B 2 10  LEU 10  634 634 LEU LEU C . n 
B 2 11  LYS 11  635 635 LYS LYS C . n 
B 2 12  ASP 12  636 ?   ?   ?   C . n 
B 2 13  ASN 13  637 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1L7X 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L7X 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1L7X 1  501 501 A1L7X LIG A . 
D 4 HOH   1  601 57  HOH   HOH A . 
D 4 HOH   2  602 32  HOH   HOH A . 
D 4 HOH   3  603 11  HOH   HOH A . 
D 4 HOH   4  604 20  HOH   HOH A . 
D 4 HOH   5  605 14  HOH   HOH A . 
D 4 HOH   6  606 34  HOH   HOH A . 
D 4 HOH   7  607 50  HOH   HOH A . 
D 4 HOH   8  608 28  HOH   HOH A . 
D 4 HOH   9  609 4   HOH   HOH A . 
D 4 HOH   10 610 13  HOH   HOH A . 
D 4 HOH   11 611 10  HOH   HOH A . 
D 4 HOH   12 612 1   HOH   HOH A . 
D 4 HOH   13 613 51  HOH   HOH A . 
D 4 HOH   14 614 35  HOH   HOH A . 
D 4 HOH   15 615 8   HOH   HOH A . 
D 4 HOH   16 616 3   HOH   HOH A . 
D 4 HOH   17 617 2   HOH   HOH A . 
D 4 HOH   18 618 47  HOH   HOH A . 
D 4 HOH   19 619 24  HOH   HOH A . 
D 4 HOH   20 620 26  HOH   HOH A . 
D 4 HOH   21 621 12  HOH   HOH A . 
D 4 HOH   22 622 16  HOH   HOH A . 
D 4 HOH   23 623 43  HOH   HOH A . 
D 4 HOH   24 624 41  HOH   HOH A . 
D 4 HOH   25 625 21  HOH   HOH A . 
D 4 HOH   26 626 9   HOH   HOH A . 
D 4 HOH   27 627 31  HOH   HOH A . 
D 4 HOH   28 628 53  HOH   HOH A . 
D 4 HOH   29 629 29  HOH   HOH A . 
D 4 HOH   30 630 19  HOH   HOH A . 
D 4 HOH   31 631 5   HOH   HOH A . 
D 4 HOH   32 632 7   HOH   HOH A . 
D 4 HOH   33 633 27  HOH   HOH A . 
D 4 HOH   34 634 17  HOH   HOH A . 
D 4 HOH   35 635 36  HOH   HOH A . 
D 4 HOH   36 636 6   HOH   HOH A . 
D 4 HOH   37 637 18  HOH   HOH A . 
D 4 HOH   38 638 39  HOH   HOH A . 
D 4 HOH   39 639 52  HOH   HOH A . 
D 4 HOH   40 640 49  HOH   HOH A . 
D 4 HOH   41 641 45  HOH   HOH A . 
D 4 HOH   42 642 23  HOH   HOH A . 
D 4 HOH   43 643 22  HOH   HOH A . 
D 4 HOH   44 644 56  HOH   HOH A . 
D 4 HOH   45 645 38  HOH   HOH A . 
D 4 HOH   46 646 46  HOH   HOH A . 
D 4 HOH   47 647 55  HOH   HOH A . 
D 4 HOH   48 648 54  HOH   HOH A . 
D 4 HOH   49 649 15  HOH   HOH A . 
D 4 HOH   50 650 40  HOH   HOH A . 
D 4 HOH   51 651 42  HOH   HOH A . 
D 4 HOH   52 652 44  HOH   HOH A . 
D 4 HOH   53 653 30  HOH   HOH A . 
D 4 HOH   54 654 48  HOH   HOH A . 
E 4 HOH   1  701 33  HOH   HOH C . 
# 
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 ? ? ? 1.14_3260 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.314 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9M10 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     127.160 
_cell.length_a_esd                 ? 
_cell.length_b                     43.010 
_cell.length_b_esd                 ? 
_cell.length_c                     45.590 
_cell.length_c_esd                 ? 
_cell.volume                       248921.658 
_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                         9M10 
_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                   9M10 
_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    '0.2 M magnesium acetate tetrahydrate, PEG 3350, pH 7.9.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-22 
_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   1.0 
_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                        'SPRING-8 BEAMLINE BL45XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL45XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9M10 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.02 
_reflns.d_resolution_low                               45.52 
_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                                     16309 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.62 
_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                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.154 
_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                                    2.02 
_reflns_shell.d_res_low                                     2.14 
_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                             2580 
_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                                  0.516 
_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                                  2.996 
_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                               54.97 
_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                                 9M10 
_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                            2.02 
_refine.ls_d_res_low                             45.51 
_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                     16262 
_refine.ls_number_reflns_R_free                  816 
_refine.ls_number_reflns_R_work                  15446 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.30 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1856 
_refine.ls_R_factor_R_free                       0.2215 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1838 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          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                      2ZLC 
_refine.pdbx_stereochemistry_target_values       '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             1.1100 
_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                 26.2258 
_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                            0.2561 
_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                       2.02 
_refine_hist.d_res_low                        45.51 
_refine_hist.number_atoms_solvent             55 
_refine_hist.number_atoms_total               2110 
_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        2015 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_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' ? 0.0048  ? 2148 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6372  ? 2918 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0374  ? 324  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0029  ? 372  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 24.3175 ? 825  ? 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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_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' 2.02 2.15  . . 135 2534 98.52 . . . . 0.2928 . . . . . . . . . . . . . . . 0.3698 
'X-RAY DIFFRACTION' 2.15 2.31  . . 139 2558 99.52 . . . . 0.2445 . . . . . . . . . . . . . . . 0.2668 
'X-RAY DIFFRACTION' 2.31 2.54  . . 133 2560 99.89 . . . . 0.2143 . . . . . . . . . . . . . . . 0.2894 
'X-RAY DIFFRACTION' 2.54 2.91  . . 134 2573 99.71 . . . . 0.1958 . . . . . . . . . . . . . . . 0.2400 
'X-RAY DIFFRACTION' 2.91 3.67  . . 138 2578 99.41 . . . . 0.1738 . . . . . . . . . . . . . . . 0.2363 
'X-RAY DIFFRACTION' 3.67 45.51 . . 137 2643 98.79 . . . . 0.1592 . . . . . . . . . . . . . . . 0.1727 
# 
_struct.entry_id                     9M10 
_struct.title                        'Vitamin D receptor complex with a dimethylbis((3-trifluoromethyl)phenyl)silane derivative' 
_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        9M10 
_struct_keywords.text            'Vitamin D receptor, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
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 ? 
D N N 4 ? 
E N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP VDR_RAT    P13053 ? 1 
;LKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGSYSPRPTLSFSGNSSSSSSDLYTTSLDMMEP
SGFSNLDLNGEDSDDPSVTLDLSPLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLRSNQSF
TMDDMSWDCGSQDYKYDVTDVSKAGHTLELIEPLIKFQVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAKLVEAIQDRL
SNTLQTYIRCRHPPPGSHQLYAKMIQKLADLRSLNEEHSKQYRSLSFQPENSMKLTPLVLEVFGNEIS
;
116 
2 UNP MED1_HUMAN Q15648 ? 2 KNHPMLMNLLKDN 640 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9M10 A 11 ? 271 ? P13053 116 ? 423 ? 116 423 
2 2 9M10 C 1  ? 13  ? Q15648 640 ? 652 ? 625 637 
# 
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 9M10 GLY A 1  ? UNP P13053 ?   ?   'expression tag' 106 1  
1 9M10 SER A 2  ? UNP P13053 ?   ?   'expression tag' 107 2  
1 9M10 HIS A 3  ? UNP P13053 ?   ?   'expression tag' 108 3  
1 9M10 MET A 4  ? UNP P13053 ?   ?   'expression tag' 109 4  
1 9M10 GLY A 5  ? UNP P13053 ?   ?   'expression tag' 110 5  
1 9M10 SER A 6  ? UNP P13053 ?   ?   'expression tag' 111 6  
1 9M10 PRO A 7  ? UNP P13053 ?   ?   'expression tag' 112 7  
1 9M10 ASN A 8  ? UNP P13053 ?   ?   'expression tag' 113 8  
1 9M10 SER A 9  ? UNP P13053 ?   ?   'expression tag' 114 9  
1 9M10 PRO A 10 ? UNP P13053 ?   ?   'expression tag' 115 10 
1 9M10 ?   A ?  ? UNP P13053 TYR 166 deletion         ?   11 
1 9M10 ?   A ?  ? UNP P13053 SER 167 deletion         ?   12 
1 9M10 ?   A ?  ? UNP P13053 PRO 168 deletion         ?   13 
1 9M10 ?   A ?  ? UNP P13053 ARG 169 deletion         ?   14 
1 9M10 ?   A ?  ? UNP P13053 PRO 170 deletion         ?   15 
1 9M10 ?   A ?  ? UNP P13053 THR 171 deletion         ?   16 
1 9M10 ?   A ?  ? UNP P13053 LEU 172 deletion         ?   17 
1 9M10 ?   A ?  ? UNP P13053 SER 173 deletion         ?   18 
1 9M10 ?   A ?  ? UNP P13053 PHE 174 deletion         ?   19 
1 9M10 ?   A ?  ? UNP P13053 SER 175 deletion         ?   20 
1 9M10 ?   A ?  ? UNP P13053 GLY 176 deletion         ?   21 
1 9M10 ?   A ?  ? UNP P13053 ASN 177 deletion         ?   22 
1 9M10 ?   A ?  ? UNP P13053 SER 178 deletion         ?   23 
1 9M10 ?   A ?  ? UNP P13053 SER 179 deletion         ?   24 
1 9M10 ?   A ?  ? UNP P13053 SER 180 deletion         ?   25 
1 9M10 ?   A ?  ? UNP P13053 SER 181 deletion         ?   26 
1 9M10 ?   A ?  ? UNP P13053 SER 182 deletion         ?   27 
1 9M10 ?   A ?  ? UNP P13053 SER 183 deletion         ?   28 
1 9M10 ?   A ?  ? UNP P13053 ASP 184 deletion         ?   29 
1 9M10 ?   A ?  ? UNP P13053 LEU 185 deletion         ?   30 
1 9M10 ?   A ?  ? UNP P13053 TYR 186 deletion         ?   31 
1 9M10 ?   A ?  ? UNP P13053 THR 187 deletion         ?   32 
1 9M10 ?   A ?  ? UNP P13053 THR 188 deletion         ?   33 
1 9M10 ?   A ?  ? UNP P13053 SER 189 deletion         ?   34 
1 9M10 ?   A ?  ? UNP P13053 LEU 190 deletion         ?   35 
1 9M10 ?   A ?  ? UNP P13053 ASP 191 deletion         ?   36 
1 9M10 ?   A ?  ? UNP P13053 MET 192 deletion         ?   37 
1 9M10 ?   A ?  ? UNP P13053 MET 193 deletion         ?   38 
1 9M10 ?   A ?  ? UNP P13053 GLU 194 deletion         ?   39 
1 9M10 ?   A ?  ? UNP P13053 PRO 195 deletion         ?   40 
1 9M10 ?   A ?  ? UNP P13053 SER 196 deletion         ?   41 
1 9M10 ?   A ?  ? UNP P13053 GLY 197 deletion         ?   42 
1 9M10 ?   A ?  ? UNP P13053 PHE 198 deletion         ?   43 
1 9M10 ?   A ?  ? UNP P13053 SER 199 deletion         ?   44 
1 9M10 ?   A ?  ? UNP P13053 ASN 200 deletion         ?   45 
1 9M10 ?   A ?  ? UNP P13053 LEU 201 deletion         ?   46 
1 9M10 ?   A ?  ? UNP P13053 ASP 202 deletion         ?   47 
1 9M10 ?   A ?  ? UNP P13053 LEU 203 deletion         ?   48 
1 9M10 ?   A ?  ? UNP P13053 ASN 204 deletion         ?   49 
1 9M10 ?   A ?  ? UNP P13053 GLY 205 deletion         ?   50 
1 9M10 ?   A ?  ? UNP P13053 GLU 206 deletion         ?   51 
1 9M10 ?   A ?  ? UNP P13053 ASP 207 deletion         ?   52 
1 9M10 ?   A ?  ? UNP P13053 SER 208 deletion         ?   53 
1 9M10 ?   A ?  ? UNP P13053 ASP 209 deletion         ?   54 
1 9M10 ?   A ?  ? UNP P13053 ASP 210 deletion         ?   55 
1 9M10 ?   A ?  ? UNP P13053 PRO 211 deletion         ?   56 
1 9M10 ?   A ?  ? UNP P13053 SER 212 deletion         ?   57 
# 
_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)' 1050  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  11990 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 20  ? TYR A 38  ? SER A 125 TYR A 143 1 ? 19 
HELX_P HELX_P2  AA2 TYR A 42  ? PHE A 48  ? TYR A 147 PHE A 153 5 ? 7  
HELX_P HELX_P3  AA3 MET A 70  ? LYS A 90  ? MET A 222 LYS A 242 1 ? 21 
HELX_P HELX_P4  AA4 GLY A 94  ? LEU A 98  ? GLY A 246 LEU A 250 5 ? 5  
HELX_P HELX_P5  AA5 THR A 99  ? SER A 119 ? THR A 251 SER A 271 1 ? 21 
HELX_P HELX_P6  AA6 ASP A 140 ? LYS A 146 ? ASP A 292 LYS A 298 1 ? 7  
HELX_P HELX_P7  AA7 THR A 150 ? LYS A 166 ? THR A 302 LYS A 318 1 ? 17 
HELX_P HELX_P8  AA8 HIS A 170 ? VAL A 183 ? HIS A 322 VAL A 335 1 ? 14 
HELX_P HELX_P9  AA9 ASP A 192 ? HIS A 215 ? ASP A 344 HIS A 367 1 ? 24 
HELX_P HELX_P10 AB1 GLN A 222 ? GLN A 251 ? GLN A 374 GLN A 403 1 ? 30 
HELX_P HELX_P11 AB2 GLN A 251 ? MET A 256 ? GLN A 403 MET A 408 1 ? 6  
HELX_P HELX_P12 AB3 THR A 259 ? GLY A 267 ? THR A 411 GLY A 419 1 ? 9  
HELX_P HELX_P13 AB4 HIS B 3   ? LEU B 10  ? HIS C 627 LEU C 634 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           217 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            369 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    218 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     370 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       5.83 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
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 
# 
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 PHE A 123 ? THR A 124 ? PHE A 275 THR A 276 
AA1 2 SER A 129 ? ASP A 131 ? SER A 281 ASP A 283 
AA1 3 LYS A 138 ? TYR A 139 ? LYS A 290 TYR A 291 
# 
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 N THR A 124 ? N THR A 276 O SER A 129 ? O SER A 281 
AA1 2 3 N TRP A 130 ? N TRP A 282 O TYR A 139 ? O TYR A 291 
# 
_pdbx_entry_details.entry_id                   9M10 
_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   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 289 ? ? -108.39 42.35 
2 1 VAL A 335 ? B -93.77  59.40 
# 
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 17.7115851187 0.106916333277 11.3422429316  0.275230662387 ? -0.040312253923 ? -0.003418098288 ? 
0.240308472847 ? 0.0155239107789 ? 0.230498487122 ? 3.57909254272 ? 0.457730186285 ? 1.00212786197 ? 2.24359759911 ? 
0.479687495144 ? 2.90481005341 ? -0.0474382693859 ? -0.284825472035 ? 0.258085167368 ? 0.0583329490809 ? -0.0680406394028 ? 
0.124583590356 ? -0.196284899983 ? -0.225091986141 ? 0.0865336366256 ? 
2 'X-RAY DIFFRACTION' ? refined 12.0163471181 -10.6574213045 -3.45877268454 0.683795996097 ? 0.0748140135306 ? -0.160727260135 ? 
0.723017504415 ? 0.0164401998356 ? 0.646526274022 ? 5.16139226589 ? -2.33900134001 ? 2.35290798442 ? 5.41394691143 ? 1.31481991923 
? 9.44144024162 ? 0.31145704374    ? 0.102752221496  ? -0.54920100583 ? -0.432935021328 ? 0.41552925339    ? 0.233039084542 ? 
0.749689827472  ? -0.376914115602 ? 0.0902069991587 ? 
# 
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 ? ? ? ? ? ? ? ? ? ? ? 'chain A' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 'chain C' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 106 ? A GLY 1   
2  1 Y 1 A SER 107 ? A SER 2   
3  1 Y 1 A HIS 108 ? A HIS 3   
4  1 Y 1 A MET 109 ? A MET 4   
5  1 Y 1 A GLY 110 ? A GLY 5   
6  1 Y 1 A SER 111 ? A SER 6   
7  1 Y 1 A PRO 112 ? A PRO 7   
8  1 Y 1 A ASN 113 ? A ASN 8   
9  1 Y 1 A SER 114 ? A SER 9   
10 1 Y 1 A PRO 115 ? A PRO 10  
11 1 Y 1 A LEU 116 ? A LEU 11  
12 1 Y 1 A LYS 117 ? A LYS 12  
13 1 Y 1 A ASP 118 ? A ASP 13  
14 1 Y 1 A SER 119 ? A SER 14  
15 1 Y 1 A LEU 120 ? A LEU 15  
16 1 Y 1 A ARG 121 ? A ARG 16  
17 1 Y 1 A PRO 122 ? A PRO 17  
18 1 Y 1 A ASP 207 ? A ASP 55  
19 1 Y 1 A GLY 208 ? A GLY 56  
20 1 Y 1 A SER 209 ? A SER 57  
21 1 Y 1 A THR 210 ? A THR 58  
22 1 Y 1 A GLY 211 ? A GLY 59  
23 1 Y 1 A SER 212 ? A SER 60  
24 1 Y 1 A VAL 213 ? A VAL 61  
25 1 Y 1 A THR 214 ? A THR 62  
26 1 Y 1 A LEU 215 ? A LEU 63  
27 1 Y 1 A ASP 216 ? A ASP 64  
28 1 Y 1 A LEU 217 ? A LEU 65  
29 1 Y 1 A GLU 421 ? A GLU 269 
30 1 Y 1 A ILE 422 ? A ILE 270 
31 1 Y 1 A SER 423 ? A SER 271 
32 1 Y 1 C ASP 636 ? B ASP 12  
33 1 Y 1 C ASN 637 ? B ASN 13  
# 
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 
A1L7X C10  C  Y N 1   
A1L7X C13  C  Y N 2   
A1L7X C15  C  N N 3   
A1L7X C20  C  N N 4   
A1L7X C21  C  N N 5   
A1L7X C22  C  N N 6   
A1L7X C24  C  N N 7   
A1L7X C26  C  N N 8   
A1L7X C28  C  N N 9   
A1L7X C01  C  Y N 10  
A1L7X C02  C  Y N 11  
A1L7X C03  C  Y N 12  
A1L7X C04  C  Y N 13  
A1L7X C05  C  Y N 14  
A1L7X C06  C  Y N 15  
A1L7X C08  C  Y N 16  
A1L7X C09  C  Y N 17  
A1L7X C11  C  Y N 18  
A1L7X C12  C  Y N 19  
A1L7X C14  C  N N 20  
A1L7X C18  C  N N 21  
A1L7X C19  C  N S 22  
A1L7X C23  C  N N 23  
A1L7X C25  C  N N 24  
A1L7X C27  C  N N 25  
A1L7X C33  C  N N 26  
A1L7X C37  C  N N 27  
A1L7X F34  F  N N 28  
A1L7X F35  F  N N 29  
A1L7X F36  F  N N 30  
A1L7X F38  F  N N 31  
A1L7X F39  F  N N 32  
A1L7X F40  F  N N 33  
A1L7X O16  O  N N 34  
A1L7X O17  O  N N 35  
A1L7X O29  O  N N 36  
A1L7X O30  O  N N 37  
A1L7X O31  O  N N 38  
A1L7X O32  O  N N 39  
A1L7X SI07 SI N N 40  
A1L7X H131 H  N N 41  
A1L7X H151 H  N N 42  
A1L7X H152 H  N N 43  
A1L7X H153 H  N N 44  
A1L7X H202 H  N N 45  
A1L7X H201 H  N N 46  
A1L7X H212 H  N N 47  
A1L7X H211 H  N N 48  
A1L7X H261 H  N N 49  
A1L7X H262 H  N N 50  
A1L7X H282 H  N N 51  
A1L7X H281 H  N N 52  
A1L7X H283 H  N N 53  
A1L7X H011 H  N N 54  
A1L7X H041 H  N N 55  
A1L7X H061 H  N N 56  
A1L7X H091 H  N N 57  
A1L7X H121 H  N N 58  
A1L7X H141 H  N N 59  
A1L7X H143 H  N N 60  
A1L7X H142 H  N N 61  
A1L7X H182 H  N N 62  
A1L7X H181 H  N N 63  
A1L7X H191 H  N N 64  
A1L7X H231 H  N N 65  
A1L7X H232 H  N N 66  
A1L7X H251 H  N N 67  
A1L7X H252 H  N N 68  
A1L7X H271 H  N N 69  
A1L7X H272 H  N N 70  
A1L7X H273 H  N N 71  
A1L7X H291 H  N N 72  
A1L7X H1   H  N N 73  
A1L7X H321 H  N N 74  
ALA   N    N  N N 75  
ALA   CA   C  N S 76  
ALA   C    C  N N 77  
ALA   O    O  N N 78  
ALA   CB   C  N N 79  
ALA   OXT  O  N N 80  
ALA   H    H  N N 81  
ALA   H2   H  N N 82  
ALA   HA   H  N N 83  
ALA   HB1  H  N N 84  
ALA   HB2  H  N N 85  
ALA   HB3  H  N N 86  
ALA   HXT  H  N N 87  
ARG   N    N  N N 88  
ARG   CA   C  N S 89  
ARG   C    C  N N 90  
ARG   O    O  N N 91  
ARG   CB   C  N N 92  
ARG   CG   C  N N 93  
ARG   CD   C  N N 94  
ARG   NE   N  N N 95  
ARG   CZ   C  N N 96  
ARG   NH1  N  N N 97  
ARG   NH2  N  N N 98  
ARG   OXT  O  N N 99  
ARG   H    H  N N 100 
ARG   H2   H  N N 101 
ARG   HA   H  N N 102 
ARG   HB2  H  N N 103 
ARG   HB3  H  N N 104 
ARG   HG2  H  N N 105 
ARG   HG3  H  N N 106 
ARG   HD2  H  N N 107 
ARG   HD3  H  N N 108 
ARG   HE   H  N N 109 
ARG   HH11 H  N N 110 
ARG   HH12 H  N N 111 
ARG   HH21 H  N N 112 
ARG   HH22 H  N N 113 
ARG   HXT  H  N N 114 
ASN   N    N  N N 115 
ASN   CA   C  N S 116 
ASN   C    C  N N 117 
ASN   O    O  N N 118 
ASN   CB   C  N N 119 
ASN   CG   C  N N 120 
ASN   OD1  O  N N 121 
ASN   ND2  N  N N 122 
ASN   OXT  O  N N 123 
ASN   H    H  N N 124 
ASN   H2   H  N N 125 
ASN   HA   H  N N 126 
ASN   HB2  H  N N 127 
ASN   HB3  H  N N 128 
ASN   HD21 H  N N 129 
ASN   HD22 H  N N 130 
ASN   HXT  H  N N 131 
ASP   N    N  N N 132 
ASP   CA   C  N S 133 
ASP   C    C  N N 134 
ASP   O    O  N N 135 
ASP   CB   C  N N 136 
ASP   CG   C  N N 137 
ASP   OD1  O  N N 138 
ASP   OD2  O  N N 139 
ASP   OXT  O  N N 140 
ASP   H    H  N N 141 
ASP   H2   H  N N 142 
ASP   HA   H  N N 143 
ASP   HB2  H  N N 144 
ASP   HB3  H  N N 145 
ASP   HD2  H  N N 146 
ASP   HXT  H  N N 147 
CYS   N    N  N N 148 
CYS   CA   C  N R 149 
CYS   C    C  N N 150 
CYS   O    O  N N 151 
CYS   CB   C  N N 152 
CYS   SG   S  N N 153 
CYS   OXT  O  N N 154 
CYS   H    H  N N 155 
CYS   H2   H  N N 156 
CYS   HA   H  N N 157 
CYS   HB2  H  N N 158 
CYS   HB3  H  N N 159 
CYS   HG   H  N N 160 
CYS   HXT  H  N N 161 
GLN   N    N  N N 162 
GLN   CA   C  N S 163 
GLN   C    C  N N 164 
GLN   O    O  N N 165 
GLN   CB   C  N N 166 
GLN   CG   C  N N 167 
GLN   CD   C  N N 168 
GLN   OE1  O  N N 169 
GLN   NE2  N  N N 170 
GLN   OXT  O  N N 171 
GLN   H    H  N N 172 
GLN   H2   H  N N 173 
GLN   HA   H  N N 174 
GLN   HB2  H  N N 175 
GLN   HB3  H  N N 176 
GLN   HG2  H  N N 177 
GLN   HG3  H  N N 178 
GLN   HE21 H  N N 179 
GLN   HE22 H  N N 180 
GLN   HXT  H  N N 181 
GLU   N    N  N N 182 
GLU   CA   C  N S 183 
GLU   C    C  N N 184 
GLU   O    O  N N 185 
GLU   CB   C  N N 186 
GLU   CG   C  N N 187 
GLU   CD   C  N N 188 
GLU   OE1  O  N N 189 
GLU   OE2  O  N N 190 
GLU   OXT  O  N N 191 
GLU   H    H  N N 192 
GLU   H2   H  N N 193 
GLU   HA   H  N N 194 
GLU   HB2  H  N N 195 
GLU   HB3  H  N N 196 
GLU   HG2  H  N N 197 
GLU   HG3  H  N N 198 
GLU   HE2  H  N N 199 
GLU   HXT  H  N N 200 
GLY   N    N  N N 201 
GLY   CA   C  N N 202 
GLY   C    C  N N 203 
GLY   O    O  N N 204 
GLY   OXT  O  N N 205 
GLY   H    H  N N 206 
GLY   H2   H  N N 207 
GLY   HA2  H  N N 208 
GLY   HA3  H  N N 209 
GLY   HXT  H  N N 210 
HIS   N    N  N N 211 
HIS   CA   C  N S 212 
HIS   C    C  N N 213 
HIS   O    O  N N 214 
HIS   CB   C  N N 215 
HIS   CG   C  Y N 216 
HIS   ND1  N  Y N 217 
HIS   CD2  C  Y N 218 
HIS   CE1  C  Y N 219 
HIS   NE2  N  Y N 220 
HIS   OXT  O  N N 221 
HIS   H    H  N N 222 
HIS   H2   H  N N 223 
HIS   HA   H  N N 224 
HIS   HB2  H  N N 225 
HIS   HB3  H  N N 226 
HIS   HD1  H  N N 227 
HIS   HD2  H  N N 228 
HIS   HE1  H  N N 229 
HIS   HE2  H  N N 230 
HIS   HXT  H  N N 231 
HOH   O    O  N N 232 
HOH   H1   H  N N 233 
HOH   H2   H  N N 234 
ILE   N    N  N N 235 
ILE   CA   C  N S 236 
ILE   C    C  N N 237 
ILE   O    O  N N 238 
ILE   CB   C  N S 239 
ILE   CG1  C  N N 240 
ILE   CG2  C  N N 241 
ILE   CD1  C  N N 242 
ILE   OXT  O  N N 243 
ILE   H    H  N N 244 
ILE   H2   H  N N 245 
ILE   HA   H  N N 246 
ILE   HB   H  N N 247 
ILE   HG12 H  N N 248 
ILE   HG13 H  N N 249 
ILE   HG21 H  N N 250 
ILE   HG22 H  N N 251 
ILE   HG23 H  N N 252 
ILE   HD11 H  N N 253 
ILE   HD12 H  N N 254 
ILE   HD13 H  N N 255 
ILE   HXT  H  N N 256 
LEU   N    N  N N 257 
LEU   CA   C  N S 258 
LEU   C    C  N N 259 
LEU   O    O  N N 260 
LEU   CB   C  N N 261 
LEU   CG   C  N N 262 
LEU   CD1  C  N N 263 
LEU   CD2  C  N N 264 
LEU   OXT  O  N N 265 
LEU   H    H  N N 266 
LEU   H2   H  N N 267 
LEU   HA   H  N N 268 
LEU   HB2  H  N N 269 
LEU   HB3  H  N N 270 
LEU   HG   H  N N 271 
LEU   HD11 H  N N 272 
LEU   HD12 H  N N 273 
LEU   HD13 H  N N 274 
LEU   HD21 H  N N 275 
LEU   HD22 H  N N 276 
LEU   HD23 H  N N 277 
LEU   HXT  H  N N 278 
LYS   N    N  N N 279 
LYS   CA   C  N S 280 
LYS   C    C  N N 281 
LYS   O    O  N N 282 
LYS   CB   C  N N 283 
LYS   CG   C  N N 284 
LYS   CD   C  N N 285 
LYS   CE   C  N N 286 
LYS   NZ   N  N N 287 
LYS   OXT  O  N N 288 
LYS   H    H  N N 289 
LYS   H2   H  N N 290 
LYS   HA   H  N N 291 
LYS   HB2  H  N N 292 
LYS   HB3  H  N N 293 
LYS   HG2  H  N N 294 
LYS   HG3  H  N N 295 
LYS   HD2  H  N N 296 
LYS   HD3  H  N N 297 
LYS   HE2  H  N N 298 
LYS   HE3  H  N N 299 
LYS   HZ1  H  N N 300 
LYS   HZ2  H  N N 301 
LYS   HZ3  H  N N 302 
LYS   HXT  H  N N 303 
MET   N    N  N N 304 
MET   CA   C  N S 305 
MET   C    C  N N 306 
MET   O    O  N N 307 
MET   CB   C  N N 308 
MET   CG   C  N N 309 
MET   SD   S  N N 310 
MET   CE   C  N N 311 
MET   OXT  O  N N 312 
MET   H    H  N N 313 
MET   H2   H  N N 314 
MET   HA   H  N N 315 
MET   HB2  H  N N 316 
MET   HB3  H  N N 317 
MET   HG2  H  N N 318 
MET   HG3  H  N N 319 
MET   HE1  H  N N 320 
MET   HE2  H  N N 321 
MET   HE3  H  N N 322 
MET   HXT  H  N N 323 
PHE   N    N  N N 324 
PHE   CA   C  N S 325 
PHE   C    C  N N 326 
PHE   O    O  N N 327 
PHE   CB   C  N N 328 
PHE   CG   C  Y N 329 
PHE   CD1  C  Y N 330 
PHE   CD2  C  Y N 331 
PHE   CE1  C  Y N 332 
PHE   CE2  C  Y N 333 
PHE   CZ   C  Y N 334 
PHE   OXT  O  N N 335 
PHE   H    H  N N 336 
PHE   H2   H  N N 337 
PHE   HA   H  N N 338 
PHE   HB2  H  N N 339 
PHE   HB3  H  N N 340 
PHE   HD1  H  N N 341 
PHE   HD2  H  N N 342 
PHE   HE1  H  N N 343 
PHE   HE2  H  N N 344 
PHE   HZ   H  N N 345 
PHE   HXT  H  N N 346 
PRO   N    N  N N 347 
PRO   CA   C  N S 348 
PRO   C    C  N N 349 
PRO   O    O  N N 350 
PRO   CB   C  N N 351 
PRO   CG   C  N N 352 
PRO   CD   C  N N 353 
PRO   OXT  O  N N 354 
PRO   H    H  N N 355 
PRO   HA   H  N N 356 
PRO   HB2  H  N N 357 
PRO   HB3  H  N N 358 
PRO   HG2  H  N N 359 
PRO   HG3  H  N N 360 
PRO   HD2  H  N N 361 
PRO   HD3  H  N N 362 
PRO   HXT  H  N N 363 
SER   N    N  N N 364 
SER   CA   C  N S 365 
SER   C    C  N N 366 
SER   O    O  N N 367 
SER   CB   C  N N 368 
SER   OG   O  N N 369 
SER   OXT  O  N N 370 
SER   H    H  N N 371 
SER   H2   H  N N 372 
SER   HA   H  N N 373 
SER   HB2  H  N N 374 
SER   HB3  H  N N 375 
SER   HG   H  N N 376 
SER   HXT  H  N N 377 
THR   N    N  N N 378 
THR   CA   C  N S 379 
THR   C    C  N N 380 
THR   O    O  N N 381 
THR   CB   C  N R 382 
THR   OG1  O  N N 383 
THR   CG2  C  N N 384 
THR   OXT  O  N N 385 
THR   H    H  N N 386 
THR   H2   H  N N 387 
THR   HA   H  N N 388 
THR   HB   H  N N 389 
THR   HG1  H  N N 390 
THR   HG21 H  N N 391 
THR   HG22 H  N N 392 
THR   HG23 H  N N 393 
THR   HXT  H  N N 394 
TRP   N    N  N N 395 
TRP   CA   C  N S 396 
TRP   C    C  N N 397 
TRP   O    O  N N 398 
TRP   CB   C  N N 399 
TRP   CG   C  Y N 400 
TRP   CD1  C  Y N 401 
TRP   CD2  C  Y N 402 
TRP   NE1  N  Y N 403 
TRP   CE2  C  Y N 404 
TRP   CE3  C  Y N 405 
TRP   CZ2  C  Y N 406 
TRP   CZ3  C  Y N 407 
TRP   CH2  C  Y N 408 
TRP   OXT  O  N N 409 
TRP   H    H  N N 410 
TRP   H2   H  N N 411 
TRP   HA   H  N N 412 
TRP   HB2  H  N N 413 
TRP   HB3  H  N N 414 
TRP   HD1  H  N N 415 
TRP   HE1  H  N N 416 
TRP   HE3  H  N N 417 
TRP   HZ2  H  N N 418 
TRP   HZ3  H  N N 419 
TRP   HH2  H  N N 420 
TRP   HXT  H  N N 421 
TYR   N    N  N N 422 
TYR   CA   C  N S 423 
TYR   C    C  N N 424 
TYR   O    O  N N 425 
TYR   CB   C  N N 426 
TYR   CG   C  Y N 427 
TYR   CD1  C  Y N 428 
TYR   CD2  C  Y N 429 
TYR   CE1  C  Y N 430 
TYR   CE2  C  Y N 431 
TYR   CZ   C  Y N 432 
TYR   OH   O  N N 433 
TYR   OXT  O  N N 434 
TYR   H    H  N N 435 
TYR   H2   H  N N 436 
TYR   HA   H  N N 437 
TYR   HB2  H  N N 438 
TYR   HB3  H  N N 439 
TYR   HD1  H  N N 440 
TYR   HD2  H  N N 441 
TYR   HE1  H  N N 442 
TYR   HE2  H  N N 443 
TYR   HH   H  N N 444 
TYR   HXT  H  N N 445 
VAL   N    N  N N 446 
VAL   CA   C  N S 447 
VAL   C    C  N N 448 
VAL   O    O  N N 449 
VAL   CB   C  N N 450 
VAL   CG1  C  N N 451 
VAL   CG2  C  N N 452 
VAL   OXT  O  N N 453 
VAL   H    H  N N 454 
VAL   H2   H  N N 455 
VAL   HA   H  N N 456 
VAL   HB   H  N N 457 
VAL   HG11 H  N N 458 
VAL   HG12 H  N N 459 
VAL   HG13 H  N N 460 
VAL   HG21 H  N N 461 
VAL   HG22 H  N N 462 
VAL   HG23 H  N N 463 
VAL   HXT  H  N N 464 
# 
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 
A1L7X C01  C02  doub Y N 1   
A1L7X C01  C06  sing Y N 2   
A1L7X C02  C03  sing Y N 3   
A1L7X C02  O17  sing N N 4   
A1L7X C03  C04  doub Y N 5   
A1L7X C03  C33  sing N N 6   
A1L7X C04  C05  sing Y N 7   
A1L7X C05  C06  doub Y N 8   
A1L7X C05  SI07 sing N N 9   
A1L7X SI07 C08  sing N N 10  
A1L7X SI07 C14  sing N N 11  
A1L7X SI07 C15  sing N N 12  
A1L7X C08  C09  doub Y N 13  
A1L7X C08  C13  sing Y N 14  
A1L7X C09  C10  sing Y N 15  
A1L7X C10  C11  doub Y N 16  
A1L7X C10  C37  sing N N 17  
A1L7X C11  C12  sing Y N 18  
A1L7X C11  O16  sing N N 19  
A1L7X C12  C13  doub Y N 20  
A1L7X O16  C23  sing N N 21  
A1L7X O17  C18  sing N N 22  
A1L7X C18  C19  sing N N 23  
A1L7X C19  C20  sing N N 24  
A1L7X C19  O32  sing N N 25  
A1L7X C20  C21  sing N N 26  
A1L7X C21  C22  sing N N 27  
A1L7X C22  O30  doub N N 28  
A1L7X C22  O31  sing N N 29  
A1L7X C23  C24  sing N N 30  
A1L7X C24  C25  sing N N 31  
A1L7X C24  C26  sing N N 32  
A1L7X C24  O29  sing N N 33  
A1L7X C25  C27  sing N N 34  
A1L7X C26  C28  sing N N 35  
A1L7X C33  F34  sing N N 36  
A1L7X C33  F35  sing N N 37  
A1L7X C33  F36  sing N N 38  
A1L7X C37  F38  sing N N 39  
A1L7X C37  F39  sing N N 40  
A1L7X C37  F40  sing N N 41  
A1L7X C13  H131 sing N N 42  
A1L7X C15  H151 sing N N 43  
A1L7X C15  H152 sing N N 44  
A1L7X C15  H153 sing N N 45  
A1L7X C20  H202 sing N N 46  
A1L7X C20  H201 sing N N 47  
A1L7X C21  H212 sing N N 48  
A1L7X C21  H211 sing N N 49  
A1L7X C26  H261 sing N N 50  
A1L7X C26  H262 sing N N 51  
A1L7X C28  H282 sing N N 52  
A1L7X C28  H281 sing N N 53  
A1L7X C28  H283 sing N N 54  
A1L7X C01  H011 sing N N 55  
A1L7X C04  H041 sing N N 56  
A1L7X C06  H061 sing N N 57  
A1L7X C09  H091 sing N N 58  
A1L7X C12  H121 sing N N 59  
A1L7X C14  H141 sing N N 60  
A1L7X C14  H143 sing N N 61  
A1L7X C14  H142 sing N N 62  
A1L7X C18  H182 sing N N 63  
A1L7X C18  H181 sing N N 64  
A1L7X C19  H191 sing N N 65  
A1L7X C23  H231 sing N N 66  
A1L7X C23  H232 sing N N 67  
A1L7X C25  H251 sing N N 68  
A1L7X C25  H252 sing N N 69  
A1L7X C27  H271 sing N N 70  
A1L7X C27  H272 sing N N 71  
A1L7X C27  H273 sing N N 72  
A1L7X O29  H291 sing N N 73  
A1L7X O31  H1   sing N N 74  
A1L7X O32  H321 sing N N 75  
ALA   N    CA   sing N N 76  
ALA   N    H    sing N N 77  
ALA   N    H2   sing N N 78  
ALA   CA   C    sing N N 79  
ALA   CA   CB   sing N N 80  
ALA   CA   HA   sing N N 81  
ALA   C    O    doub N N 82  
ALA   C    OXT  sing N N 83  
ALA   CB   HB1  sing N N 84  
ALA   CB   HB2  sing N N 85  
ALA   CB   HB3  sing N N 86  
ALA   OXT  HXT  sing N N 87  
ARG   N    CA   sing N N 88  
ARG   N    H    sing N N 89  
ARG   N    H2   sing N N 90  
ARG   CA   C    sing N N 91  
ARG   CA   CB   sing N N 92  
ARG   CA   HA   sing N N 93  
ARG   C    O    doub N N 94  
ARG   C    OXT  sing N N 95  
ARG   CB   CG   sing N N 96  
ARG   CB   HB2  sing N N 97  
ARG   CB   HB3  sing N N 98  
ARG   CG   CD   sing N N 99  
ARG   CG   HG2  sing N N 100 
ARG   CG   HG3  sing N N 101 
ARG   CD   NE   sing N N 102 
ARG   CD   HD2  sing N N 103 
ARG   CD   HD3  sing N N 104 
ARG   NE   CZ   sing N N 105 
ARG   NE   HE   sing N N 106 
ARG   CZ   NH1  sing N N 107 
ARG   CZ   NH2  doub N N 108 
ARG   NH1  HH11 sing N N 109 
ARG   NH1  HH12 sing N N 110 
ARG   NH2  HH21 sing N N 111 
ARG   NH2  HH22 sing N N 112 
ARG   OXT  HXT  sing N N 113 
ASN   N    CA   sing N N 114 
ASN   N    H    sing N N 115 
ASN   N    H2   sing N N 116 
ASN   CA   C    sing N N 117 
ASN   CA   CB   sing N N 118 
ASN   CA   HA   sing N N 119 
ASN   C    O    doub N N 120 
ASN   C    OXT  sing N N 121 
ASN   CB   CG   sing N N 122 
ASN   CB   HB2  sing N N 123 
ASN   CB   HB3  sing N N 124 
ASN   CG   OD1  doub N N 125 
ASN   CG   ND2  sing N N 126 
ASN   ND2  HD21 sing N N 127 
ASN   ND2  HD22 sing N N 128 
ASN   OXT  HXT  sing N N 129 
ASP   N    CA   sing N N 130 
ASP   N    H    sing N N 131 
ASP   N    H2   sing N N 132 
ASP   CA   C    sing N N 133 
ASP   CA   CB   sing N N 134 
ASP   CA   HA   sing N N 135 
ASP   C    O    doub N N 136 
ASP   C    OXT  sing N N 137 
ASP   CB   CG   sing N N 138 
ASP   CB   HB2  sing N N 139 
ASP   CB   HB3  sing N N 140 
ASP   CG   OD1  doub N N 141 
ASP   CG   OD2  sing N N 142 
ASP   OD2  HD2  sing N N 143 
ASP   OXT  HXT  sing N N 144 
CYS   N    CA   sing N N 145 
CYS   N    H    sing N N 146 
CYS   N    H2   sing N N 147 
CYS   CA   C    sing N N 148 
CYS   CA   CB   sing N N 149 
CYS   CA   HA   sing N N 150 
CYS   C    O    doub N N 151 
CYS   C    OXT  sing N N 152 
CYS   CB   SG   sing N N 153 
CYS   CB   HB2  sing N N 154 
CYS   CB   HB3  sing N N 155 
CYS   SG   HG   sing N N 156 
CYS   OXT  HXT  sing N N 157 
GLN   N    CA   sing N N 158 
GLN   N    H    sing N N 159 
GLN   N    H2   sing N N 160 
GLN   CA   C    sing N N 161 
GLN   CA   CB   sing N N 162 
GLN   CA   HA   sing N N 163 
GLN   C    O    doub N N 164 
GLN   C    OXT  sing N N 165 
GLN   CB   CG   sing N N 166 
GLN   CB   HB2  sing N N 167 
GLN   CB   HB3  sing N N 168 
GLN   CG   CD   sing N N 169 
GLN   CG   HG2  sing N N 170 
GLN   CG   HG3  sing N N 171 
GLN   CD   OE1  doub N N 172 
GLN   CD   NE2  sing N N 173 
GLN   NE2  HE21 sing N N 174 
GLN   NE2  HE22 sing N N 175 
GLN   OXT  HXT  sing N N 176 
GLU   N    CA   sing N N 177 
GLU   N    H    sing N N 178 
GLU   N    H2   sing N N 179 
GLU   CA   C    sing N N 180 
GLU   CA   CB   sing N N 181 
GLU   CA   HA   sing N N 182 
GLU   C    O    doub N N 183 
GLU   C    OXT  sing N N 184 
GLU   CB   CG   sing N N 185 
GLU   CB   HB2  sing N N 186 
GLU   CB   HB3  sing N N 187 
GLU   CG   CD   sing N N 188 
GLU   CG   HG2  sing N N 189 
GLU   CG   HG3  sing N N 190 
GLU   CD   OE1  doub N N 191 
GLU   CD   OE2  sing N N 192 
GLU   OE2  HE2  sing N N 193 
GLU   OXT  HXT  sing N N 194 
GLY   N    CA   sing N N 195 
GLY   N    H    sing N N 196 
GLY   N    H2   sing N N 197 
GLY   CA   C    sing N N 198 
GLY   CA   HA2  sing N N 199 
GLY   CA   HA3  sing N N 200 
GLY   C    O    doub N N 201 
GLY   C    OXT  sing N N 202 
GLY   OXT  HXT  sing N N 203 
HIS   N    CA   sing N N 204 
HIS   N    H    sing N N 205 
HIS   N    H2   sing N N 206 
HIS   CA   C    sing N N 207 
HIS   CA   CB   sing N N 208 
HIS   CA   HA   sing N N 209 
HIS   C    O    doub N N 210 
HIS   C    OXT  sing N N 211 
HIS   CB   CG   sing N N 212 
HIS   CB   HB2  sing N N 213 
HIS   CB   HB3  sing N N 214 
HIS   CG   ND1  sing Y N 215 
HIS   CG   CD2  doub Y N 216 
HIS   ND1  CE1  doub Y N 217 
HIS   ND1  HD1  sing N N 218 
HIS   CD2  NE2  sing Y N 219 
HIS   CD2  HD2  sing N N 220 
HIS   CE1  NE2  sing Y N 221 
HIS   CE1  HE1  sing N N 222 
HIS   NE2  HE2  sing N N 223 
HIS   OXT  HXT  sing N N 224 
HOH   O    H1   sing N N 225 
HOH   O    H2   sing N N 226 
ILE   N    CA   sing N N 227 
ILE   N    H    sing N N 228 
ILE   N    H2   sing N N 229 
ILE   CA   C    sing N N 230 
ILE   CA   CB   sing N N 231 
ILE   CA   HA   sing N N 232 
ILE   C    O    doub N N 233 
ILE   C    OXT  sing N N 234 
ILE   CB   CG1  sing N N 235 
ILE   CB   CG2  sing N N 236 
ILE   CB   HB   sing N N 237 
ILE   CG1  CD1  sing N N 238 
ILE   CG1  HG12 sing N N 239 
ILE   CG1  HG13 sing N N 240 
ILE   CG2  HG21 sing N N 241 
ILE   CG2  HG22 sing N N 242 
ILE   CG2  HG23 sing N N 243 
ILE   CD1  HD11 sing N N 244 
ILE   CD1  HD12 sing N N 245 
ILE   CD1  HD13 sing N N 246 
ILE   OXT  HXT  sing N N 247 
LEU   N    CA   sing N N 248 
LEU   N    H    sing N N 249 
LEU   N    H2   sing N N 250 
LEU   CA   C    sing N N 251 
LEU   CA   CB   sing N N 252 
LEU   CA   HA   sing N N 253 
LEU   C    O    doub N N 254 
LEU   C    OXT  sing N N 255 
LEU   CB   CG   sing N N 256 
LEU   CB   HB2  sing N N 257 
LEU   CB   HB3  sing N N 258 
LEU   CG   CD1  sing N N 259 
LEU   CG   CD2  sing N N 260 
LEU   CG   HG   sing N N 261 
LEU   CD1  HD11 sing N N 262 
LEU   CD1  HD12 sing N N 263 
LEU   CD1  HD13 sing N N 264 
LEU   CD2  HD21 sing N N 265 
LEU   CD2  HD22 sing N N 266 
LEU   CD2  HD23 sing N N 267 
LEU   OXT  HXT  sing N N 268 
LYS   N    CA   sing N N 269 
LYS   N    H    sing N N 270 
LYS   N    H2   sing N N 271 
LYS   CA   C    sing N N 272 
LYS   CA   CB   sing N N 273 
LYS   CA   HA   sing N N 274 
LYS   C    O    doub N N 275 
LYS   C    OXT  sing N N 276 
LYS   CB   CG   sing N N 277 
LYS   CB   HB2  sing N N 278 
LYS   CB   HB3  sing N N 279 
LYS   CG   CD   sing N N 280 
LYS   CG   HG2  sing N N 281 
LYS   CG   HG3  sing N N 282 
LYS   CD   CE   sing N N 283 
LYS   CD   HD2  sing N N 284 
LYS   CD   HD3  sing N N 285 
LYS   CE   NZ   sing N N 286 
LYS   CE   HE2  sing N N 287 
LYS   CE   HE3  sing N N 288 
LYS   NZ   HZ1  sing N N 289 
LYS   NZ   HZ2  sing N N 290 
LYS   NZ   HZ3  sing N N 291 
LYS   OXT  HXT  sing N N 292 
MET   N    CA   sing N N 293 
MET   N    H    sing N N 294 
MET   N    H2   sing N N 295 
MET   CA   C    sing N N 296 
MET   CA   CB   sing N N 297 
MET   CA   HA   sing N N 298 
MET   C    O    doub N N 299 
MET   C    OXT  sing N N 300 
MET   CB   CG   sing N N 301 
MET   CB   HB2  sing N N 302 
MET   CB   HB3  sing N N 303 
MET   CG   SD   sing N N 304 
MET   CG   HG2  sing N N 305 
MET   CG   HG3  sing N N 306 
MET   SD   CE   sing N N 307 
MET   CE   HE1  sing N N 308 
MET   CE   HE2  sing N N 309 
MET   CE   HE3  sing N N 310 
MET   OXT  HXT  sing N N 311 
PHE   N    CA   sing N N 312 
PHE   N    H    sing N N 313 
PHE   N    H2   sing N N 314 
PHE   CA   C    sing N N 315 
PHE   CA   CB   sing N N 316 
PHE   CA   HA   sing N N 317 
PHE   C    O    doub N N 318 
PHE   C    OXT  sing N N 319 
PHE   CB   CG   sing N N 320 
PHE   CB   HB2  sing N N 321 
PHE   CB   HB3  sing N N 322 
PHE   CG   CD1  doub Y N 323 
PHE   CG   CD2  sing Y N 324 
PHE   CD1  CE1  sing Y N 325 
PHE   CD1  HD1  sing N N 326 
PHE   CD2  CE2  doub Y N 327 
PHE   CD2  HD2  sing N N 328 
PHE   CE1  CZ   doub Y N 329 
PHE   CE1  HE1  sing N N 330 
PHE   CE2  CZ   sing Y N 331 
PHE   CE2  HE2  sing N N 332 
PHE   CZ   HZ   sing N N 333 
PHE   OXT  HXT  sing N N 334 
PRO   N    CA   sing N N 335 
PRO   N    CD   sing N N 336 
PRO   N    H    sing N N 337 
PRO   CA   C    sing N N 338 
PRO   CA   CB   sing N N 339 
PRO   CA   HA   sing N N 340 
PRO   C    O    doub N N 341 
PRO   C    OXT  sing N N 342 
PRO   CB   CG   sing N N 343 
PRO   CB   HB2  sing N N 344 
PRO   CB   HB3  sing N N 345 
PRO   CG   CD   sing N N 346 
PRO   CG   HG2  sing N N 347 
PRO   CG   HG3  sing N N 348 
PRO   CD   HD2  sing N N 349 
PRO   CD   HD3  sing N N 350 
PRO   OXT  HXT  sing N N 351 
SER   N    CA   sing N N 352 
SER   N    H    sing N N 353 
SER   N    H2   sing N N 354 
SER   CA   C    sing N N 355 
SER   CA   CB   sing N N 356 
SER   CA   HA   sing N N 357 
SER   C    O    doub N N 358 
SER   C    OXT  sing N N 359 
SER   CB   OG   sing N N 360 
SER   CB   HB2  sing N N 361 
SER   CB   HB3  sing N N 362 
SER   OG   HG   sing N N 363 
SER   OXT  HXT  sing N N 364 
THR   N    CA   sing N N 365 
THR   N    H    sing N N 366 
THR   N    H2   sing N N 367 
THR   CA   C    sing N N 368 
THR   CA   CB   sing N N 369 
THR   CA   HA   sing N N 370 
THR   C    O    doub N N 371 
THR   C    OXT  sing N N 372 
THR   CB   OG1  sing N N 373 
THR   CB   CG2  sing N N 374 
THR   CB   HB   sing N N 375 
THR   OG1  HG1  sing N N 376 
THR   CG2  HG21 sing N N 377 
THR   CG2  HG22 sing N N 378 
THR   CG2  HG23 sing N N 379 
THR   OXT  HXT  sing N N 380 
TRP   N    CA   sing N N 381 
TRP   N    H    sing N N 382 
TRP   N    H2   sing N N 383 
TRP   CA   C    sing N N 384 
TRP   CA   CB   sing N N 385 
TRP   CA   HA   sing N N 386 
TRP   C    O    doub N N 387 
TRP   C    OXT  sing N N 388 
TRP   CB   CG   sing N N 389 
TRP   CB   HB2  sing N N 390 
TRP   CB   HB3  sing N N 391 
TRP   CG   CD1  doub Y N 392 
TRP   CG   CD2  sing Y N 393 
TRP   CD1  NE1  sing Y N 394 
TRP   CD1  HD1  sing N N 395 
TRP   CD2  CE2  doub Y N 396 
TRP   CD2  CE3  sing Y N 397 
TRP   NE1  CE2  sing Y N 398 
TRP   NE1  HE1  sing N N 399 
TRP   CE2  CZ2  sing Y N 400 
TRP   CE3  CZ3  doub Y N 401 
TRP   CE3  HE3  sing N N 402 
TRP   CZ2  CH2  doub Y N 403 
TRP   CZ2  HZ2  sing N N 404 
TRP   CZ3  CH2  sing Y N 405 
TRP   CZ3  HZ3  sing N N 406 
TRP   CH2  HH2  sing N N 407 
TRP   OXT  HXT  sing N N 408 
TYR   N    CA   sing N N 409 
TYR   N    H    sing N N 410 
TYR   N    H2   sing N N 411 
TYR   CA   C    sing N N 412 
TYR   CA   CB   sing N N 413 
TYR   CA   HA   sing N N 414 
TYR   C    O    doub N N 415 
TYR   C    OXT  sing N N 416 
TYR   CB   CG   sing N N 417 
TYR   CB   HB2  sing N N 418 
TYR   CB   HB3  sing N N 419 
TYR   CG   CD1  doub Y N 420 
TYR   CG   CD2  sing Y N 421 
TYR   CD1  CE1  sing Y N 422 
TYR   CD1  HD1  sing N N 423 
TYR   CD2  CE2  doub Y N 424 
TYR   CD2  HD2  sing N N 425 
TYR   CE1  CZ   doub Y N 426 
TYR   CE1  HE1  sing N N 427 
TYR   CE2  CZ   sing Y N 428 
TYR   CE2  HE2  sing N N 429 
TYR   CZ   OH   sing N N 430 
TYR   OH   HH   sing N N 431 
TYR   OXT  HXT  sing N N 432 
VAL   N    CA   sing N N 433 
VAL   N    H    sing N N 434 
VAL   N    H2   sing N N 435 
VAL   CA   C    sing N N 436 
VAL   CA   CB   sing N N 437 
VAL   CA   HA   sing N N 438 
VAL   C    O    doub N N 439 
VAL   C    OXT  sing N N 440 
VAL   CB   CG1  sing N N 441 
VAL   CB   CG2  sing N N 442 
VAL   CB   HB   sing N N 443 
VAL   CG1  HG11 sing N N 444 
VAL   CG1  HG12 sing N N 445 
VAL   CG1  HG13 sing N N 446 
VAL   CG2  HG21 sing N N 447 
VAL   CG2  HG22 sing N N 448 
VAL   CG2  HG23 sing N N 449 
VAL   OXT  HXT  sing N N 450 
# 
_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   2ZLC 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9M10 
_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]   0.007864 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000455 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023250 
_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]   0.021971 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
SI 
# 
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    . LYS   A 1 18  ? 45.63300  0.30100   13.51500  1.000 98.36153  ?  123 LYS   A N    1 
ATOM   2    C  CA   . LYS   A 1 18  ? 46.17100  -0.66700  12.56600  1.000 100.39204 ?  123 LYS   A CA   1 
ATOM   3    C  C    . LYS   A 1 18  ? 45.09600  -1.13300  11.58700  1.000 91.60026  ?  123 LYS   A C    1 
ATOM   4    O  O    . LYS   A 1 18  ? 44.85900  -2.33100  11.42700  1.000 89.85166  ?  123 LYS   A O    1 
ATOM   5    C  CB   . LYS   A 1 18  ? 46.77300  -1.86300  13.30600  1.000 99.77168  ?  123 LYS   A CB   1 
ATOM   6    C  CG   . LYS   A 1 18  ? 46.00100  -2.27700  14.54700  1.000 94.49648  ?  123 LYS   A CG   1 
ATOM   7    C  CD   . LYS   A 1 18  ? 46.82300  -3.21200  15.41800  1.000 97.02889  ?  123 LYS   A CD   1 
ATOM   8    C  CE   . LYS   A 1 18  ? 46.97900  -4.58000  14.77200  1.000 96.74795  ?  123 LYS   A CE   1 
ATOM   9    N  NZ   . LYS   A 1 18  ? 47.69200  -5.53500  15.66400  1.000 96.98167  ?  123 LYS   A NZ   1 
ATOM   10   N  N    . LEU   A 1 19  ? 44.44800  -0.16900  10.93500  1.000 81.62742  ?  124 LEU   A N    1 
ATOM   11   C  CA   . LEU   A 1 19  ? 43.41000  -0.45200  9.95000   1.000 70.41886  ?  124 LEU   A CA   1 
ATOM   12   C  C    . LEU   A 1 19  ? 44.07300  -0.84800  8.63500   1.000 68.36948  ?  124 LEU   A C    1 
ATOM   13   O  O    . LEU   A 1 19  ? 44.68700  -0.01100  7.96400   1.000 67.36974  ?  124 LEU   A O    1 
ATOM   14   C  CB   . LEU   A 1 19  ? 42.51100  0.76800   9.76800   1.000 58.08535  ?  124 LEU   A CB   1 
ATOM   15   C  CG   . LEU   A 1 19  ? 40.99400  0.59100   9.65000   1.000 63.48186  ?  124 LEU   A CG   1 
ATOM   16   C  CD1  . LEU   A 1 19  ? 40.46100  -0.43600  10.63500  1.000 54.08768  ?  124 LEU   A CD1  1 
ATOM   17   C  CD2  . LEU   A 1 19  ? 40.30000  1.93000   9.84600   1.000 71.41763  ?  124 LEU   A CD2  1 
ATOM   18   N  N    . SER   A 1 20  ? 43.95400  -2.12200  8.26500   1.000 60.93610  ?  125 SER   A N    1 
ATOM   19   C  CA   . SER   A 1 20  ? 44.52000  -2.59700  7.01200   1.000 64.25580  ?  125 SER   A CA   1 
ATOM   20   C  C    . SER   A 1 20  ? 43.79100  -1.96800  5.82500   1.000 56.69772  ?  125 SER   A C    1 
ATOM   21   O  O    . SER   A 1 20  ? 42.72600  -1.35800  5.96400   1.000 50.49472  ?  125 SER   A O    1 
ATOM   22   C  CB   . SER   A 1 20  ? 44.43800  -4.12200  6.93100   1.000 66.53712  ?  125 SER   A CB   1 
ATOM   23   O  OG   . SER   A 1 20  ? 43.12000  -4.54900  6.62800   1.000 59.79010  ?  125 SER   A OG   1 
ATOM   24   N  N    . GLU   A 1 21  ? 44.38500  -2.11800  4.63800   1.000 58.02628  ?  126 GLU   A N    1 
ATOM   25   C  CA   . GLU   A 1 21  ? 43.71300  -1.66300  3.42500   1.000 59.47974  ?  126 GLU   A CA   1 
ATOM   26   C  C    . GLU   A 1 21  ? 42.39700  -2.40100  3.22200   1.000 52.33745  ?  126 GLU   A C    1 
ATOM   27   O  O    . GLU   A 1 21  ? 41.40200  -1.80400  2.79500   1.000 53.32338  ?  126 GLU   A O    1 
ATOM   28   C  CB   . GLU   A 1 21  ? 44.61900  -1.84700  2.20700   1.000 53.91456  ?  126 GLU   A CB   1 
ATOM   29   C  CG   . GLU   A 1 21  ? 44.03000  -1.27000  0.92500   1.000 57.90896  ?  126 GLU   A CG   1 
ATOM   30   C  CD   . GLU   A 1 21  ? 44.97500  -1.36100  -0.25700  1.000 67.83048  ?  126 GLU   A CD   1 
ATOM   31   O  OE1  . GLU   A 1 21  ? 44.55700  -1.00400  -1.37900  1.000 73.24823  ?  126 GLU   A OE1  1 
ATOM   32   O  OE2  . GLU   A 1 21  ? 46.13300  -1.79000  -0.06700  1.000 70.31956  ?  126 GLU   A OE2  1 
ATOM   33   N  N    . GLU   A 1 22  ? 42.37600  -3.70200  3.52300   1.000 51.46774  ?  127 GLU   A N    1 
ATOM   34   C  CA   . GLU   A 1 22  ? 41.13700  -4.47000  3.45200   1.000 54.25999  ?  127 GLU   A CA   1 
ATOM   35   C  C    . GLU   A 1 22  ? 40.07500  -3.87900  4.37000   1.000 49.94911  ?  127 GLU   A C    1 
ATOM   36   O  O    . GLU   A 1 22  ? 38.91200  -3.72700  3.97900   1.000 47.30824  ?  127 GLU   A O    1 
ATOM   37   C  CB   . GLU   A 1 22  ? 41.40700  -5.93100  3.81600   1.000 65.35829  ?  127 GLU   A CB   1 
ATOM   38   C  CG   . GLU   A 1 22  ? 40.35900  -6.91500  3.31300   1.000 80.71500  ?  127 GLU   A CG   1 
ATOM   39   C  CD   . GLU   A 1 22  ? 40.87100  -8.34400  3.28000   1.000 95.76075  ?  127 GLU   A CD   1 
ATOM   40   O  OE1  . GLU   A 1 22  ? 40.64900  -9.08000  4.26500   1.000 99.13053  ?  127 GLU   A OE1  1 
ATOM   41   O  OE2  . GLU   A 1 22  ? 41.49800  -8.73200  2.27000   1.000 100.77909 ?  127 GLU   A OE2  1 
ATOM   42   N  N    . GLN   A 1 23  ? 40.46100  -3.53900  5.60300   1.000 54.55912  ?  128 GLN   A N    1 
ATOM   43   C  CA   . GLN   A 1 23  ? 39.50500  -2.97500  6.54900   1.000 48.74343  ?  128 GLN   A CA   1 
ATOM   44   C  C    . GLN   A 1 23  ? 39.03900  -1.59400  6.10700   1.000 41.61634  ?  128 GLN   A C    1 
ATOM   45   O  O    . GLN   A 1 23  ? 37.85000  -1.27100  6.21900   1.000 46.45265  ?  128 GLN   A O    1 
ATOM   46   C  CB   . GLN   A 1 23  ? 40.12100  -2.92300  7.94700   1.000 50.10724  ?  128 GLN   A CB   1 
ATOM   47   C  CG   . GLN   A 1 23  ? 40.24000  -4.28700  8.61000   1.000 44.58919  ?  128 GLN   A CG   1 
ATOM   48   C  CD   . GLN   A 1 23  ? 41.09700  -4.26000  9.85900   1.000 54.90621  ?  128 GLN   A CD   1 
ATOM   49   O  OE1  . GLN   A 1 23  ? 41.91300  -3.36000  10.04600  1.000 63.69256  ?  128 GLN   A OE1  1 
ATOM   50   N  NE2  . GLN   A 1 23  ? 40.91500  -5.25200  10.72200  1.000 56.46012  ?  128 GLN   A NE2  1 
ATOM   51   N  N    . GLN   A 1 24  ? 39.95500  -0.76600  5.60000   1.000 40.52035  ?  129 GLN   A N    1 
ATOM   52   C  CA   . GLN   A 1 24  ? 39.54400  0.51400   5.03400   1.000 46.76172  ?  129 GLN   A CA   1 
ATOM   53   C  C    . GLN   A 1 24  ? 38.65400  0.30900   3.81800   1.000 44.36274  ?  129 GLN   A C    1 
ATOM   54   O  O    . GLN   A 1 24  ? 37.68900  1.05400   3.61300   1.000 41.36441  ?  129 GLN   A O    1 
ATOM   55   C  CB   . GLN   A 1 24  ? 40.76400  1.35200   4.65800   1.000 47.39263  ?  129 GLN   A CB   1 
ATOM   56   C  CG   . GLN   A 1 24  ? 41.71800  1.63500   5.79900   1.000 60.02220  ?  129 GLN   A CG   1 
ATOM   57   C  CD   . GLN   A 1 24  ? 42.98400  2.31400   5.32800   1.000 63.72143  ?  129 GLN   A CD   1 
ATOM   58   O  OE1  . GLN   A 1 24  ? 42.93400  3.27500   4.55900   1.000 62.94517  ?  129 GLN   A OE1  1 
ATOM   59   N  NE2  . GLN   A 1 24  ? 44.12900  1.81700   5.78100   1.000 63.80305  ?  129 GLN   A NE2  1 
ATOM   60   N  N    . HIS   A 1 25  ? 38.96800  -0.69800  2.99700   1.000 43.19175  ?  130 HIS   A N    1 
ATOM   61   C  CA   . HIS   A 1 25  ? 38.14200  -1.00200  1.83400   1.000 46.26844  ?  130 HIS   A CA   1 
ATOM   62   C  C    . HIS   A 1 25  ? 36.71900  -1.34700  2.24900   1.000 38.92402  ?  130 HIS   A C    1 
ATOM   63   O  O    . HIS   A 1 25  ? 35.75100  -0.86400  1.65200   1.000 44.66953  ?  130 HIS   A O    1 
ATOM   64   C  CB   . HIS   A 1 25  ? 38.76600  -2.14900  1.03900   1.000 58.89388  ?  130 HIS   A CB   1 
ATOM   65   C  CG   . HIS   A 1 25  ? 37.87900  -2.68900  -0.03900  1.000 65.15675  ?  130 HIS   A CG   1 
ATOM   66   N  ND1  . HIS   A 1 25  ? 37.74200  -2.07900  -1.26700  1.000 65.40581  ?  130 HIS   A ND1  1 
ATOM   67   C  CD2  . HIS   A 1 25  ? 37.07600  -3.78000  -0.07000  1.000 64.87819  ?  130 HIS   A CD2  1 
ATOM   68   C  CE1  . HIS   A 1 25  ? 36.89800  -2.77200  -2.01000  1.000 65.74874  ?  130 HIS   A CE1  1 
ATOM   69   N  NE2  . HIS   A 1 25  ? 36.47900  -3.80900  -1.30700  1.000 62.96174  ?  130 HIS   A NE2  1 
ATOM   70   N  N    . ILE   A 1 26  ? 36.57500  -2.18400  3.28000   1.000 38.23536  ?  131 ILE   A N    1 
ATOM   71   C  CA   . ILE   A 1 26  ? 35.24800  -2.53200  3.77800   1.000 38.04773  ?  131 ILE   A CA   1 
ATOM   72   C  C    . ILE   A 1 26  ? 34.51000  -1.28400  4.24100   1.000 42.10333  ?  131 ILE   A C    1 
ATOM   73   O  O    . ILE   A 1 26  ? 33.32000  -1.10200  3.95000   1.000 38.55169  ?  131 ILE   A O    1 
ATOM   74   C  CB   . ILE   A 1 26  ? 35.36100  -3.57400  4.90500   1.000 41.35467  ?  131 ILE   A CB   1 
ATOM   75   C  CG1  . ILE   A 1 26  ? 35.88400  -4.89800  4.35100   1.000 40.50878  ?  131 ILE   A CG1  1 
ATOM   76   C  CG2  . ILE   A 1 26  ? 34.02000  -3.77500  5.58300   1.000 38.32331  ?  131 ILE   A CG2  1 
ATOM   77   C  CD1  . ILE   A 1 26  ? 36.26600  -5.88400  5.42000   1.000 46.61763  ?  131 ILE   A CD1  1 
ATOM   78   N  N    . ILE   A 1 27  ? 35.20700  -0.39900  4.95800   1.000 36.97539  ?  132 ILE   A N    1 
ATOM   79   C  CA   . ILE   A 1 27  ? 34.59900  0.85000   5.40600   1.000 39.21519  ?  132 ILE   A CA   1 
ATOM   80   C  C    . ILE   A 1 27  ? 34.19500  1.70800   4.21400   1.000 41.39413  ?  132 ILE   A C    1 
ATOM   81   O  O    . ILE   A 1 27  ? 33.10400  2.29100   4.19000   1.000 38.43173  ?  132 ILE   A O    1 
ATOM   82   C  CB   . ILE   A 1 27  ? 35.56100  1.60300   6.34200   1.000 40.50020  ?  132 ILE   A CB   1 
ATOM   83   C  CG1  . ILE   A 1 27  ? 35.79400  0.80100   7.62500   1.000 37.52937  ?  132 ILE   A CG1  1 
ATOM   84   C  CG2  . ILE   A 1 27  ? 35.02300  2.98600   6.65000   1.000 40.08738  ?  132 ILE   A CG2  1 
ATOM   85   C  CD1  . ILE   A 1 27  ? 36.76800  1.44800   8.58500   1.000 35.10743  ?  132 ILE   A CD1  1 
ATOM   86   N  N    . ALA   A 1 28  ? 35.06800  1.80000   3.20700   1.000 38.63200  ?  133 ALA   A N    1 
ATOM   87   C  CA   . ALA   A 1 28  ? 34.75400  2.59000   2.02100   1.000 38.31246  ?  133 ALA   A CA   1 
ATOM   88   C  C    . ALA   A 1 28  ? 33.51500  2.05700   1.31200   1.000 38.25330  ?  133 ALA   A C    1 
ATOM   89   O  O    . ALA   A 1 28  ? 32.67900  2.83400   0.83600   1.000 38.32740  ?  133 ALA   A O    1 
ATOM   90   C  CB   . ALA   A 1 28  ? 35.94900  2.60400   1.06900   1.000 34.49562  ?  133 ALA   A CB   1 
ATOM   91   N  N    . ILE   A 1 29  ? 33.37800  0.73200   1.23500   1.000 34.01118  ?  134 ILE   A N    1 
ATOM   92   C  CA   . ILE   A 1 29  ? 32.20900  0.13900   0.59400   1.000 32.99479  ?  134 ILE   A CA   1 
ATOM   93   C  C    . ILE   A 1 29  ? 30.94700  0.46300   1.38300   1.000 37.53657  ?  134 ILE   A C    1 
ATOM   94   O  O    . ILE   A 1 29  ? 29.90400  0.79000   0.80300   1.000 37.08200  ?  134 ILE   A O    1 
ATOM   95   C  CB   . ILE   A 1 29  ? 32.39700  -1.38200  0.43900   1.000 38.21065  ?  134 ILE   A CB   1 
ATOM   96   C  CG1  . ILE   A 1 29  ? 33.56900  -1.69800  -0.48900  1.000 42.13084  ?  134 ILE   A CG1  1 
ATOM   97   C  CG2  . ILE   A 1 29  ? 31.13100  -2.01700  -0.10800  1.000 33.07210  ?  134 ILE   A CG2  1 
ATOM   98   C  CD1  . ILE   A 1 29  ? 33.31400  -1.35900  -1.93900  1.000 49.41472  ?  134 ILE   A CD1  1 
ATOM   99   N  N    . LEU   A 1 30  ? 31.01800  0.37800   2.71500   1.000 31.58488  ?  135 LEU   A N    1 
ATOM   100  C  CA   . LEU   A 1 30  ? 29.82500  0.59100   3.52900   1.000 30.31827  ?  135 LEU   A CA   1 
ATOM   101  C  C    . LEU   A 1 30  ? 29.45300  2.06700   3.60100   1.000 32.60542  ?  135 LEU   A C    1 
ATOM   102  O  O    . LEU   A 1 30  ? 28.26600  2.40900   3.64900   1.000 39.18701  ?  135 LEU   A O    1 
ATOM   103  C  CB   . LEU   A 1 30  ? 30.03700  0.02400   4.93200   1.000 32.50791  ?  135 LEU   A CB   1 
ATOM   104  C  CG   . LEU   A 1 30  ? 30.15600  -1.49800  5.04100   1.000 34.37720  ?  135 LEU   A CG   1 
ATOM   105  C  CD1  . LEU   A 1 30  ? 30.46000  -1.88700  6.47200   1.000 32.57658  ?  135 LEU   A CD1  1 
ATOM   106  C  CD2  . LEU   A 1 30  ? 28.88300  -2.17500  4.56300   1.000 29.08997  ?  135 LEU   A CD2  1 
ATOM   107  N  N    . LEU   A 1 31  ? 30.44900  2.95600   3.62200   1.000 38.24505  ?  136 LEU   A N    1 
ATOM   108  C  CA   . LEU   A 1 31  ? 30.15500  4.38400   3.56600   1.000 41.25134  ?  136 LEU   A CA   1 
ATOM   109  C  C    . LEU   A 1 31  ? 29.48500  4.74700   2.24800   1.000 42.54448  ?  136 LEU   A C    1 
ATOM   110  O  O    . LEU   A 1 31  ? 28.49700  5.49000   2.22900   1.000 42.09370  ?  136 LEU   A O    1 
ATOM   111  C  CB   . LEU   A 1 31  ? 31.43600  5.19700   3.76100   1.000 36.21397  ?  136 LEU   A CB   1 
ATOM   112  C  CG   . LEU   A 1 31  ? 31.99600  5.25100   5.18200   1.000 34.12962  ?  136 LEU   A CG   1 
ATOM   113  C  CD1  . LEU   A 1 31  ? 33.33400  5.97700   5.20100   1.000 40.78187  ?  136 LEU   A CD1  1 
ATOM   114  C  CD2  . LEU   A 1 31  ? 31.00100  5.91900   6.12200   1.000 42.55411  ?  136 LEU   A CD2  1 
ATOM   115  N  N    . ASP   A 1 32  ? 30.00300  4.22200   1.13600   1.000 44.05156  ?  137 ASP   A N    1 
ATOM   116  C  CA   . ASP   A 1 32  ? 29.39600  4.48800   -0.16300  1.000 40.08131  ?  137 ASP   A CA   1 
ATOM   117  C  C    . ASP   A 1 32  ? 28.01000  3.86200   -0.26400  1.000 41.24972  ?  137 ASP   A C    1 
ATOM   118  O  O    . ASP   A 1 32  ? 27.09500  4.45300   -0.85000  1.000 41.01638  ?  137 ASP   A O    1 
ATOM   119  C  CB   . ASP   A 1 32  ? 30.30600  3.97000   -1.27600  1.000 42.27024  ?  137 ASP   A CB   1 
ATOM   120  C  CG   . ASP   A 1 32  ? 29.65600  4.04400   -2.64200  1.000 49.68584  ?  137 ASP   A CG   1 
ATOM   121  O  OD1  . ASP   A 1 32  ? 29.25600  2.98200   -3.16700  1.000 48.32475  ?  137 ASP   A OD1  1 
ATOM   122  O  OD2  . ASP   A 1 32  ? 29.54900  5.16000   -3.19200  1.000 46.63421  ?  137 ASP   A OD2  1 
ATOM   123  N  N    . ALA   A 1 33  ? 27.83600  2.66400   0.30200   1.000 40.79970  ?  138 ALA   A N    1 
ATOM   124  C  CA   . ALA   A 1 33  ? 26.51700  2.04200   0.33200   1.000 34.07282  ?  138 ALA   A CA   1 
ATOM   125  C  C    . ALA   A 1 33  ? 25.52200  2.89800   1.10400   1.000 38.56408  ?  138 ALA   A C    1 
ATOM   126  O  O    . ALA   A 1 33  ? 24.36700  3.05300   0.69000   1.000 36.38510  ?  138 ALA   A O    1 
ATOM   127  C  CB   . ALA   A 1 33  ? 26.61000  0.64800   0.95100   1.000 28.78024  ?  138 ALA   A CB   1 
ATOM   128  N  N    . HIS   A 1 34  ? 25.95900  3.46900   2.22800   1.000 33.03243  ?  139 HIS   A N    1 
ATOM   129  C  CA   . HIS   A 1 34  ? 25.07700  4.29100   3.04800   1.000 35.14275  ?  139 HIS   A CA   1 
ATOM   130  C  C    . HIS   A 1 34  ? 24.68800  5.57500   2.32700   1.000 35.81554  ?  139 HIS   A C    1 
ATOM   131  O  O    . HIS   A 1 34  ? 23.51100  5.95200   2.29800   1.000 36.19944  ?  139 HIS   A O    1 
ATOM   132  C  CB   . HIS   A 1 34  ? 25.76100  4.61000   4.37600   1.000 31.51770  ?  139 HIS   A CB   1 
ATOM   133  C  CG   . HIS   A 1 34  ? 24.90800  5.39300   5.32200   1.000 36.47081  ?  139 HIS   A CG   1 
ATOM   134  N  ND1  . HIS   A 1 34  ? 23.66600  4.96000   5.73600   1.000 36.34996  ?  139 HIS   A ND1  1 
ATOM   135  C  CD2  . HIS   A 1 34  ? 25.11500  6.58200   5.93500   1.000 39.46895  ?  139 HIS   A CD2  1 
ATOM   136  C  CE1  . HIS   A 1 34  ? 23.14800  5.84600   6.56600   1.000 39.24068  ?  139 HIS   A CE1  1 
ATOM   137  N  NE2  . HIS   A 1 34  ? 24.00600  6.84100   6.70300   1.000 39.82423  ?  139 HIS   A NE2  1 
ATOM   138  N  N    . HIS   A 1 35  ? 25.67100  6.26700   1.74800   1.000 32.92159  ?  140 HIS   A N    1 
ATOM   139  C  CA   . HIS   A 1 35  ? 25.38400  7.51400   1.05000   1.000 35.79813  ?  140 HIS   A CA   1 
ATOM   140  C  C    . HIS   A 1 35  ? 24.51700  7.28000   -0.17700  1.000 43.22553  ?  140 HIS   A C    1 
ATOM   141  O  O    . HIS   A 1 35  ? 23.80100  8.18900   -0.61000  1.000 54.64826  ?  140 HIS   A O    1 
ATOM   142  C  CB   . HIS   A 1 35  ? 26.68800  8.20800   0.66000   1.000 36.34088  ?  140 HIS   A CB   1 
ATOM   143  C  CG   . HIS   A 1 35  ? 27.59200  8.48400   1.82000   1.000 47.21199  ?  140 HIS   A CG   1 
ATOM   144  N  ND1  . HIS   A 1 35  ? 28.96200  8.56600   1.69500   1.000 46.31063  ?  140 HIS   A ND1  1 
ATOM   145  C  CD2  . HIS   A 1 35  ? 27.32000  8.69200   3.13000   1.000 44.23857  ?  140 HIS   A CD2  1 
ATOM   146  C  CE1  . HIS   A 1 35  ? 29.49500  8.81800   2.87800   1.000 48.14183  ?  140 HIS   A CE1  1 
ATOM   147  N  NE2  . HIS   A 1 35  ? 28.52000  8.89800   3.76600   1.000 46.02635  ?  140 HIS   A NE2  1 
ATOM   148  N  N    . LYS   A 1 36  ? 24.56600  6.07400   -0.74700  1.000 42.46576  ?  141 LYS   A N    1 
ATOM   149  C  CA   . LYS   A 1 36  ? 23.69600  5.75100   -1.87100  1.000 42.20627  ?  141 LYS   A CA   1 
ATOM   150  C  C    . LYS   A 1 36  ? 22.26700  5.48700   -1.41700  1.000 42.95926  ?  141 LYS   A C    1 
ATOM   151  O  O    . LYS   A 1 36  ? 21.32900  5.65700   -2.20300  1.000 45.86212  ?  141 LYS   A O    1 
ATOM   152  C  CB   . LYS   A 1 36  ? 24.23200  4.52800   -2.61700  1.000 46.46398  ?  141 LYS   A CB   1 
ATOM   153  C  CG   . LYS   A 1 36  ? 25.38800  4.80400   -3.56100  1.000 53.15865  ?  141 LYS   A CG   1 
ATOM   154  C  CD   . LYS   A 1 36  ? 25.94000  3.50000   -4.13300  1.000 60.21704  ?  141 LYS   A CD   1 
ATOM   155  C  CE   . LYS   A 1 36  ? 26.99800  3.75600   -5.19900  1.000 69.45790  ?  141 LYS   A CE   1 
ATOM   156  N  NZ   . LYS   A 1 36  ? 27.96200  2.63600   -5.37700  1.000 69.27458  ?  141 LYS   A NZ   1 
ATOM   157  N  N    . THR   A 1 37  ? 22.07900  5.07100   -0.16300  1.000 40.73853  ?  142 THR   A N    1 
ATOM   158  C  CA   . THR   A 1 37  ? 20.77600  4.63100   0.31200   1.000 37.61154  ?  142 THR   A CA   1 
ATOM   159  C  C    . THR   A 1 37  ? 20.18800  5.49200   1.41800   1.000 40.65977  ?  142 THR   A C    1 
ATOM   160  O  O    . THR   A 1 37  ? 19.04600  5.24600   1.82100   1.000 44.56640  ?  142 THR   A O    1 
ATOM   161  C  CB   . THR   A 1 37  ? 20.85200  3.17800   0.80600   1.000 40.46162  ?  142 THR   A CB   1 
ATOM   162  O  OG1  . THR   A 1 37  ? 22.00600  3.01500   1.64300   1.000 38.97024  ?  142 THR   A OG1  1 
ATOM   163  C  CG2  . THR   A 1 37  ? 20.94400  2.22200   -0.37500  1.000 35.28632  ?  142 THR   A CG2  1 
ATOM   164  N  N    . TYR   A 1 38  ? 20.91800  6.47900   1.92700   1.000 39.27694  ?  143 TYR   A N    1 
ATOM   165  C  CA   . TYR   A 1 38  ? 20.38400  7.40400   2.92100   1.000 35.64563  ?  143 TYR   A CA   1 
ATOM   166  C  C    . TYR   A 1 38  ? 20.38200  8.80000   2.31800   1.000 39.82562  ?  143 TYR   A C    1 
ATOM   167  O  O    . TYR   A 1 38  ? 21.44600  9.36300   2.03900   1.000 45.18276  ?  143 TYR   A O    1 
ATOM   168  C  CB   . TYR   A 1 38  ? 21.18700  7.37200   4.22100   1.000 35.74141  ?  143 TYR   A CB   1 
ATOM   169  C  CG   . TYR   A 1 38  ? 20.47400  8.06400   5.36600   1.000 41.97176  ?  143 TYR   A CG   1 
ATOM   170  C  CD1  . TYR   A 1 38  ? 20.59000  9.43500   5.55700   1.000 48.60387  ?  143 TYR   A CD1  1 
ATOM   171  C  CD2  . TYR   A 1 38  ? 19.67000  7.34800   6.24400   1.000 43.51911  ?  143 TYR   A CD2  1 
ATOM   172  C  CE1  . TYR   A 1 38  ? 19.93200  10.07200  6.59400   1.000 50.63130  ?  143 TYR   A CE1  1 
ATOM   173  C  CE2  . TYR   A 1 38  ? 19.00900  7.97700   7.28500   1.000 34.74044  ?  143 TYR   A CE2  1 
ATOM   174  C  CZ   . TYR   A 1 38  ? 19.14400  9.33900   7.45400   1.000 43.52017  ?  143 TYR   A CZ   1 
ATOM   175  O  OH   . TYR   A 1 38  ? 18.49100  9.97200   8.48600   1.000 42.40117  ?  143 TYR   A OH   1 
ATOM   176  N  N    . ASP   A 1 39  ? 19.18600  9.35500   2.12100   1.000 42.54206  ?  144 ASP   A N    1 
ATOM   177  C  CA   . ASP   A 1 39  ? 19.02500  10.70400  1.60300   1.000 40.03699  ?  144 ASP   A CA   1 
ATOM   178  C  C    . ASP   A 1 39  ? 18.78200  11.64700  2.77300   1.000 52.57112  ?  144 ASP   A C    1 
ATOM   179  O  O    . ASP   A 1 39  ? 17.64600  11.73600  3.26500   1.000 54.27733  ?  144 ASP   A O    1 
ATOM   180  C  CB   . ASP   A 1 39  ? 17.86300  10.76300  0.60800   1.000 45.95662  ?  144 ASP   A CB   1 
ATOM   181  C  CG   . ASP   A 1 39  ? 17.53200  12.17700  0.18000   1.000 55.18435  ?  144 ASP   A CG   1 
ATOM   182  O  OD1  . ASP   A 1 39  ? 18.44300  13.03100  0.19300   1.000 55.30104  ?  144 ASP   A OD1  1 
ATOM   183  O  OD2  . ASP   A 1 39  ? 16.36100  12.43500  -0.17200  1.000 62.03655  ?  144 ASP   A OD2  1 
ATOM   184  N  N    . PRO   A 1 40  ? 19.79800  12.37400  3.25300   1.000 55.92355  ?  145 PRO   A N    1 
ATOM   185  C  CA   . PRO   A 1 40  ? 19.59400  13.24200  4.42500   1.000 54.58227  ?  145 PRO   A CA   1 
ATOM   186  C  C    . PRO   A 1 40  ? 18.69900  14.44100  4.15600   1.000 57.59289  ?  145 PRO   A C    1 
ATOM   187  O  O    . PRO   A 1 40  ? 18.35800  15.15700  5.10700   1.000 58.21889  ?  145 PRO   A O    1 
ATOM   188  C  CB   . PRO   A 1 40  ? 21.01700  13.68600  4.78800   1.000 54.39446  ?  145 PRO   A CB   1 
ATOM   189  C  CG   . PRO   A 1 40  ? 21.77800  13.59700  3.51100   1.000 55.91611  ?  145 PRO   A CG   1 
ATOM   190  C  CD   . PRO   A 1 40  ? 21.16700  12.47000  2.71700   1.000 55.61260  ?  145 PRO   A CD   1 
ATOM   191  N  N    . THR   A 1 41  ? 18.31500  14.69200  2.90400   1.000 54.91310  ?  146 THR   A N    1 
ATOM   192  C  CA   . THR   A 1 41  ? 17.35900  15.75300  2.62000   1.000 59.15110  ?  146 THR   A CA   1 
ATOM   193  C  C    . THR   A 1 41  ? 15.91700  15.29600  2.79300   1.000 58.56223  ?  146 THR   A C    1 
ATOM   194  O  O    . THR   A 1 41  ? 15.02200  16.14400  2.88000   1.000 63.25944  ?  146 THR   A O    1 
ATOM   195  C  CB   . THR   A 1 41  ? 17.55800  16.28700  1.19900   1.000 63.12860  ?  146 THR   A CB   1 
ATOM   196  O  OG1  . THR   A 1 41  ? 16.83900  15.46400  0.27200   1.000 60.47918  ?  146 THR   A OG1  1 
ATOM   197  C  CG2  . THR   A 1 41  ? 19.03600  16.29300  0.83300   1.000 62.02820  ?  146 THR   A CG2  1 
ATOM   198  N  N    . TYR   A 1 42  ? 15.68000  13.98200  2.84300   1.000 52.06715  ?  147 TYR   A N    1 
ATOM   199  C  CA   . TYR   A 1 42  ? 14.34000  13.42100  3.03100   1.000 52.67570  ?  147 TYR   A CA   1 
ATOM   200  C  C    . TYR   A 1 42  ? 13.37100  13.93900  1.96900   1.000 57.48885  ?  147 TYR   A C    1 
ATOM   201  O  O    . TYR   A 1 42  ? 12.20000  14.20800  2.24500   1.000 50.34948  ?  147 TYR   A O    1 
ATOM   202  C  CB   . TYR   A 1 42  ? 13.82300  13.70800  4.44200   1.000 53.44617  ?  147 TYR   A CB   1 
ATOM   203  C  CG   . TYR   A 1 42  ? 14.82700  13.35400  5.52000   1.000 52.64527  ?  147 TYR   A CG   1 
ATOM   204  C  CD1  . TYR   A 1 42  ? 15.46000  14.34400  6.26200   1.000 53.58444  ?  147 TYR   A CD1  1 
ATOM   205  C  CD2  . TYR   A 1 42  ? 15.15200  12.03000  5.78300   1.000 52.61124  ?  147 TYR   A CD2  1 
ATOM   206  C  CE1  . TYR   A 1 42  ? 16.38400  14.02200  7.24300   1.000 54.68246  ?  147 TYR   A CE1  1 
ATOM   207  C  CE2  . TYR   A 1 42  ? 16.07400  11.69800  6.75900   1.000 52.52883  ?  147 TYR   A CE2  1 
ATOM   208  C  CZ   . TYR   A 1 42  ? 16.68700  12.69700  7.48500   1.000 56.24896  ?  147 TYR   A CZ   1 
ATOM   209  O  OH   . TYR   A 1 42  ? 17.60400  12.36500  8.45700   1.000 62.28297  ?  147 TYR   A OH   1 
ATOM   210  N  N    . ALA   A 1 43  ? 13.86800  14.06900  0.73700   1.000 55.29644  ?  148 ALA   A N    1 
ATOM   211  C  CA   . ALA   A 1 43  ? 13.07800  14.66800  -0.33400  1.000 60.71670  ?  148 ALA   A CA   1 
ATOM   212  C  C    . ALA   A 1 43  ? 11.87200  13.81400  -0.70800  1.000 62.15486  ?  148 ALA   A C    1 
ATOM   213  O  O    . ALA   A 1 43  ? 10.82600  14.35600  -1.08500  1.000 69.14445  ?  148 ALA   A O    1 
ATOM   214  C  CB   . ALA   A 1 43  ? 13.95800  14.90400  -1.56000  1.000 62.26345  ?  148 ALA   A CB   1 
ATOM   215  N  N    . ASP   A 1 44  ? 11.98600  12.49000  -0.60600  1.000 57.83672  ?  149 ASP   A N    1 
ATOM   216  C  CA   . ASP   A 1 44  ? 10.92500  11.60400  -1.06800  1.000 60.50746  ?  149 ASP   A CA   1 
ATOM   217  C  C    . ASP   A 1 44  ? 9.73000   11.54500  -0.12700  1.000 58.62086  ?  149 ASP   A C    1 
ATOM   218  O  O    . ASP   A 1 44  ? 8.71600   10.93700  -0.48800  1.000 52.64579  ?  149 ASP   A O    1 
ATOM   219  C  CB   . ASP   A 1 44  ? 11.47400  10.19200  -1.27900  1.000 57.11040  ?  149 ASP   A CB   1 
ATOM   220  C  CG   . ASP   A 1 44  ? 12.51900  10.13400  -2.37200  1.000 62.03047  ?  149 ASP   A CG   1 
ATOM   221  O  OD1  . ASP   A 1 44  ? 12.34600  10.83100  -3.39600  1.000 64.22935  ?  149 ASP   A OD1  1 
ATOM   222  O  OD2  . ASP   A 1 44  ? 13.51400  9.39600   -2.20900  1.000 60.57731  ?  149 ASP   A OD2  1 
ATOM   223  N  N    . PHE   A 1 45  ? 9.81800   12.15800  1.05800   1.000 56.41698  ?  150 PHE   A N    1 
ATOM   224  C  CA   . PHE   A 1 45  ? 8.70900   12.12100  2.00700   1.000 57.34628  ?  150 PHE   A CA   1 
ATOM   225  C  C    . PHE   A 1 45  ? 7.45800   12.79600  1.45600   1.000 58.14824  ?  150 PHE   A C    1 
ATOM   226  O  O    . PHE   A 1 45  ? 6.36300   12.58400  1.99100   1.000 61.97344  ?  150 PHE   A O    1 
ATOM   227  C  CB   . PHE   A 1 45  ? 9.11500   12.78200  3.32900   1.000 58.75318  ?  150 PHE   A CB   1 
ATOM   228  C  CG   . PHE   A 1 45  ? 10.00500  11.92700  4.20200   1.000 60.92207  ?  150 PHE   A CG   1 
ATOM   229  C  CD1  . PHE   A 1 45  ? 11.06100  11.20700  3.66000   1.000 52.95147  ?  150 PHE   A CD1  1 
ATOM   230  C  CD2  . PHE   A 1 45  ? 9.79000   11.85700  5.57000   1.000 60.76712  ?  150 PHE   A CD2  1 
ATOM   231  C  CE1  . PHE   A 1 45  ? 11.87800  10.43000  4.46300   1.000 52.96776  ?  150 PHE   A CE1  1 
ATOM   232  C  CE2  . PHE   A 1 45  ? 10.60400  11.08200  6.37900   1.000 55.45869  ?  150 PHE   A CE2  1 
ATOM   233  C  CZ   . PHE   A 1 45  ? 11.65000  10.37000  5.82400   1.000 49.41384  ?  150 PHE   A CZ   1 
ATOM   234  N  N    . ARG   A 1 46  ? 7.59800   13.60800  0.40500   1.000 62.92331  ?  151 ARG   A N    1 
ATOM   235  C  CA   . ARG   A 1 46  ? 6.44600   14.21200  -0.25300  1.000 74.33214  ?  151 ARG   A CA   1 
ATOM   236  C  C    . ARG   A 1 46  ? 5.57700   13.17300  -0.95400  1.000 72.41360  ?  151 ARG   A C    1 
ATOM   237  O  O    . ARG   A 1 46  ? 4.37100   13.39300  -1.11100  1.000 77.42319  ?  151 ARG   A O    1 
ATOM   238  C  CB   . ARG   A 1 46  ? 6.93000   15.27600  -1.24400  1.000 76.85873  ?  151 ARG   A CB   1 
ATOM   239  C  CG   . ARG   A 1 46  ? 5.85300   15.93300  -2.09700  1.000 92.16096  ?  151 ARG   A CG   1 
ATOM   240  C  CD   . ARG   A 1 46  ? 6.34500   17.26500  -2.64900  1.000 99.25404  ?  151 ARG   A CD   1 
ATOM   241  N  NE   . ARG   A 1 46  ? 5.74000   17.60000  -3.93500  1.000 102.01685 ?  151 ARG   A NE   1 
ATOM   242  C  CZ   . ARG   A 1 46  ? 6.01600   18.70400  -4.62300  1.000 106.97850 ?  151 ARG   A CZ   1 
ATOM   243  N  NH1  . ARG   A 1 46  ? 6.89000   19.58200  -4.14900  1.000 106.44927 ?  151 ARG   A NH1  1 
ATOM   244  N  NH2  . ARG   A 1 46  ? 5.42000   18.93000  -5.78500  1.000 108.57732 ?  151 ARG   A NH2  1 
ATOM   245  N  N    . ASP   A 1 47  ? 6.15200   12.03500  -1.34800  1.000 65.60980  ?  152 ASP   A N    1 
ATOM   246  C  CA   . ASP   A 1 47  ? 5.41500   11.00300  -2.06500  1.000 70.19256  ?  152 ASP   A CA   1 
ATOM   247  C  C    . ASP   A 1 47  ? 4.64000   10.06600  -1.14800  1.000 65.61272  ?  152 ASP   A C    1 
ATOM   248  O  O    . ASP   A 1 47  ? 3.86600   9.24300   -1.65000  1.000 62.52701  ?  152 ASP   A O    1 
ATOM   249  C  CB   . ASP   A 1 47  ? 6.37400   10.18600  -2.93300  1.000 73.68689  ?  152 ASP   A CB   1 
ATOM   250  C  CG   . ASP   A 1 47  ? 7.33000   11.05800  -3.72000  1.000 76.21507  ?  152 ASP   A CG   1 
ATOM   251  O  OD1  . ASP   A 1 47  ? 7.06900   12.27500  -3.82100  1.000 83.03550  ?  152 ASP   A OD1  1 
ATOM   252  O  OD2  . ASP   A 1 47  ? 8.34200   10.53200  -4.22800  1.000 76.52985  ?  152 ASP   A OD2  1 
ATOM   253  N  N    . PHE   A 1 48  ? 4.82600   10.16000  0.16500   1.000 55.70267  ?  153 PHE   A N    1 
ATOM   254  C  CA   . PHE   A 1 48  ? 4.10200   9.29500   1.08300   1.000 50.44960  ?  153 PHE   A CA   1 
ATOM   255  C  C    . PHE   A 1 48  ? 2.66400   9.77700   1.24300   1.000 51.88166  ?  153 PHE   A C    1 
ATOM   256  O  O    . PHE   A 1 48  ? 2.31700   10.90700  0.88600   1.000 54.47558  ?  153 PHE   A O    1 
ATOM   257  C  CB   . PHE   A 1 48  ? 4.77300   9.25700   2.45900   1.000 47.58479  ?  153 PHE   A CB   1 
ATOM   258  C  CG   . PHE   A 1 48  ? 6.21500   8.82200   2.43900   1.000 45.29578  ?  153 PHE   A CG   1 
ATOM   259  C  CD1  . PHE   A 1 48  ? 7.02300   9.04700   3.54100   1.000 46.51478  ?  153 PHE   A CD1  1 
ATOM   260  C  CD2  . PHE   A 1 48  ? 6.76000   8.17900   1.33800   1.000 44.32285  ?  153 PHE   A CD2  1 
ATOM   261  C  CE1  . PHE   A 1 48  ? 8.34600   8.65300   3.54200   1.000 44.03197  ?  153 PHE   A CE1  1 
ATOM   262  C  CE2  . PHE   A 1 48  ? 8.08200   7.78300   1.33300   1.000 44.96688  ?  153 PHE   A CE2  1 
ATOM   263  C  CZ   . PHE   A 1 48  ? 8.87600   8.02200   2.43800   1.000 43.75268  ?  153 PHE   A CZ   1 
ATOM   264  N  N    . ARG   A 1 49  ? 1.82200   8.90300   1.78900   1.000 49.41387  ?  154 ARG   A N    1 
ATOM   265  C  CA   . ARG   A 1 49  ? 0.50000   9.33500   2.20800   1.000 57.74292  ?  154 ARG   A CA   1 
ATOM   266  C  C    . ARG   A 1 49  ? 0.64400   10.38200  3.31200   1.000 60.51664  ?  154 ARG   A C    1 
ATOM   267  O  O    . ARG   A 1 49  ? 1.57600   10.31700  4.12000   1.000 60.28005  ?  154 ARG   A O    1 
ATOM   268  C  CB   . ARG   A 1 49  ? -0.33300  8.15000   2.69500   1.000 65.46370  ?  154 ARG   A CB   1 
ATOM   269  C  CG   . ARG   A 1 49  ? -0.84700  7.25600   1.57400   1.000 59.90583  ?  154 ARG   A CG   1 
ATOM   270  C  CD   . ARG   A 1 49  ? -1.47500  5.98400   2.11400   1.000 57.82581  ?  154 ARG   A CD   1 
ATOM   271  N  NE   . ARG   A 1 49  ? -0.46600  5.00900   2.51600   1.000 53.67832  ?  154 ARG   A NE   1 
ATOM   272  C  CZ   . ARG   A 1 49  ? -0.73600  3.88000   3.16100   1.000 46.50462  ?  154 ARG   A CZ   1 
ATOM   273  N  NH1  . ARG   A 1 49  ? -1.98800  3.57900   3.47700   1.000 50.01035  ?  154 ARG   A NH1  1 
ATOM   274  N  NH2  . ARG   A 1 49  ? 0.24500   3.05100   3.49100   1.000 41.87891  ?  154 ARG   A NH2  1 
ATOM   275  N  N    . PRO   A 1 50  ? -0.25400  11.36000  3.36500   1.000 61.09985  ?  155 PRO   A N    1 
ATOM   276  C  CA   . PRO   A 1 50  ? -0.04800  12.51100  4.24800   1.000 71.91023  ?  155 PRO   A CA   1 
ATOM   277  C  C    . PRO   A 1 50  ? -0.10300  12.11000  5.71000   1.000 70.96764  ?  155 PRO   A C    1 
ATOM   278  O  O    . PRO   A 1 50  ? -0.92700  11.27200  6.10700   1.000 63.71367  ?  155 PRO   A O    1 
ATOM   279  C  CB   . PRO   A 1 50  ? -1.21400  13.44500  3.88700   1.000 67.30886  ?  155 PRO   A CB   1 
ATOM   280  C  CG   . PRO   A 1 50  ? -2.25800  12.53900  3.34100   1.000 68.93705  ?  155 PRO   A CG   1 
ATOM   281  C  CD   . PRO   A 1 50  ? -1.51100  11.46800  2.60400   1.000 63.19674  ?  155 PRO   A CD   1 
ATOM   282  N  N    . PRO   A 1 51  ? 0.76500   12.68300  6.54200   1.000 72.37359  ?  156 PRO   A N    1 
ATOM   283  C  CA   . PRO   A 1 51  ? 0.59800   12.53300  7.99000   1.000 70.12481  ?  156 PRO   A CA   1 
ATOM   284  C  C    . PRO   A 1 51  ? -0.59200  13.35300  8.46000   1.000 76.80927  ?  156 PRO   A C    1 
ATOM   285  O  O    . PRO   A 1 51  ? -0.68100  14.55400  8.19500   1.000 85.00570  ?  156 PRO   A O    1 
ATOM   286  C  CB   . PRO   A 1 51  ? 1.91600   13.06600  8.55900   1.000 68.03213  ?  156 PRO   A CB   1 
ATOM   287  C  CG   . PRO   A 1 51  ? 2.38900   14.04300  7.53600   1.000 69.21450  ?  156 PRO   A CG   1 
ATOM   288  C  CD   . PRO   A 1 51  ? 1.93200   13.51500  6.19900   1.000 72.14248  ?  156 PRO   A CD   1 
ATOM   289  N  N    . VAL   A 1 52  ? -1.52400  12.69300  9.13600   1.000 71.88966  ?  157 VAL   A N    1 
ATOM   290  C  CA   . VAL   A 1 52  ? -2.68200  13.35800  9.71500   1.000 86.88068  ?  157 VAL   A CA   1 
ATOM   291  C  C    . VAL   A 1 52  ? -2.64000  13.11400  11.21300  1.000 99.42785  ?  157 VAL   A C    1 
ATOM   292  O  O    . VAL   A 1 52  ? -2.72600  11.96400  11.66200  1.000 97.45375  ?  157 VAL   A O    1 
ATOM   293  C  CB   . VAL   A 1 52  ? -4.00300  12.86200  9.10500   1.000 87.81090  ?  157 VAL   A CB   1 
ATOM   294  C  CG1  . VAL   A 1 52  ? -5.11000  13.87600  9.35100   1.000 86.09820  ?  157 VAL   A CG1  1 
ATOM   295  C  CG2  . VAL   A 1 52  ? -3.83500  12.60700  7.61600   1.000 86.02244  ?  157 VAL   A CG2  1 
ATOM   296  N  N    . ARG   A 1 53  ? -2.48900  14.18800  11.98300  1.000 105.93839 ?  158 ARG   A N    1 
ATOM   297  C  CA   . ARG   A 1 53  ? -2.39500  14.08300  13.43100  1.000 109.38226 ?  158 ARG   A CA   1 
ATOM   298  C  C    . ARG   A 1 53  ? -3.67600  14.47800  14.15000  1.000 122.33636 ?  158 ARG   A C    1 
ATOM   299  O  O    . ARG   A 1 53  ? -3.91100  14.01700  15.27200  1.000 128.43071 ?  158 ARG   A O    1 
ATOM   300  C  CB   . ARG   A 1 53  ? -1.23800  14.94300  13.94900  1.000 101.90225 ?  158 ARG   A CB   1 
ATOM   301  C  CG   . ARG   A 1 53  ? 0.12300   14.28200  13.80400  1.000 90.80118  ?  158 ARG   A CG   1 
ATOM   302  C  CD   . ARG   A 1 53  ? 0.98700   15.01900  12.79500  1.000 87.66683  ?  158 ARG   A CD   1 
ATOM   303  N  NE   . ARG   A 1 53  ? 2.32000   14.43400  12.68400  1.000 83.92689  ?  158 ARG   A NE   1 
ATOM   304  C  CZ   . ARG   A 1 53  ? 3.26300   14.87900  11.86000  1.000 80.80057  ?  158 ARG   A CZ   1 
ATOM   305  N  NH1  . ARG   A 1 53  ? 3.02100   15.91800  11.07200  1.000 77.50627  ?  158 ARG   A NH1  1 
ATOM   306  N  NH2  . ARG   A 1 53  ? 4.44800   14.28600  11.82300  1.000 74.09570  ?  158 ARG   A NH2  1 
ATOM   307  N  N    . MET   A 1 54  ? -4.50600  15.31300  13.53400  1.000 126.80109 ?  159 MET   A N    1 
ATOM   308  C  CA   . MET   A 1 54  ? -5.76900  15.73400  14.13100  1.000 131.50103 ?  159 MET   A CA   1 
ATOM   309  C  C    . MET   A 1 54  ? -6.75300  14.57200  14.22400  1.000 131.29024 ?  159 MET   A C    1 
ATOM   310  O  O    . MET   A 1 54  ? -6.74200  13.81200  15.19300  1.000 129.76880 ?  159 MET   A O    1 
ATOM   311  C  CB   . MET   A 1 54  ? -6.38100  16.88000  13.32600  1.000 133.43157 ?  159 MET   A CB   1 
ATOM   312  C  CG   . MET   A 1 54  ? -5.76000  18.24000  13.60500  1.000 134.56017 ?  159 MET   A CG   1 
ATOM   313  S  SD   . MET   A 1 54  ? -4.13100  18.45300  12.86000  1.000 131.28421 ?  159 MET   A SD   1 
ATOM   314  C  CE   . MET   A 1 54  ? -3.40800  19.65600  13.97300  1.000 127.26085 ?  159 MET   A CE   1 
ATOM   315  N  N    . SER   A 1 66  ? -9.93200  1.69000   13.88400  1.000 146.60842 ?  218 SER   A N    1 
ATOM   316  C  CA   . SER   A 1 66  ? -9.54600  2.65000   14.91200  1.000 145.45219 ?  218 SER   A CA   1 
ATOM   317  C  C    . SER   A 1 66  ? -8.81300  3.83400   14.28700  1.000 134.67076 ?  218 SER   A C    1 
ATOM   318  O  O    . SER   A 1 66  ? -8.23300  3.70600   13.20900  1.000 135.88313 ?  218 SER   A O    1 
ATOM   319  C  CB   . SER   A 1 66  ? -8.67700  1.97100   15.97500  1.000 148.41624 ?  218 SER   A CB   1 
ATOM   320  O  OG   . SER   A 1 66  ? -9.24700  0.74000   16.38500  1.000 153.46609 ?  218 SER   A OG   1 
ATOM   321  N  N    . PRO   A 1 67  ? -8.84000  4.99500   14.95700  1.000 121.71513 ?  219 PRO   A N    1 
ATOM   322  C  CA   . PRO   A 1 67  ? -8.18800  6.18100   14.38600  1.000 111.43357 ?  219 PRO   A CA   1 
ATOM   323  C  C    . PRO   A 1 67  ? -6.66900  6.11800   14.43200  1.000 100.45260 ?  219 PRO   A C    1 
ATOM   324  O  O    . PRO   A 1 67  ? -6.02000  7.01900   14.97500  1.000 97.67057  ?  219 PRO   A O    1 
ATOM   325  C  CB   . PRO   A 1 67  ? -8.73000  7.32600   15.25000  1.000 113.58258 ?  219 PRO   A CB   1 
ATOM   326  C  CG   . PRO   A 1 67  ? -9.04700  6.68800   16.54800  1.000 119.41408 ?  219 PRO   A CG   1 
ATOM   327  C  CD   . PRO   A 1 67  ? -9.54400  5.30900   16.21300  1.000 122.34718 ?  219 PRO   A CD   1 
ATOM   328  N  N    . LEU   A 1 68  ? -6.09000  5.06000   13.86300  1.000 86.52212  ?  220 LEU   A N    1 
ATOM   329  C  CA   . LEU   A 1 68  ? -4.64800  5.00200   13.66400  1.000 73.36598  ?  220 LEU   A CA   1 
ATOM   330  C  C    . LEU   A 1 68  ? -4.27400  5.98600   12.56500  1.000 69.08855  ?  220 LEU   A C    1 
ATOM   331  O  O    . LEU   A 1 68  ? -3.95800  5.58700   11.44000  1.000 67.48277  ?  220 LEU   A O    1 
ATOM   332  C  CB   . LEU   A 1 68  ? -4.20200  3.58300   13.31100  1.000 70.86109  ?  220 LEU   A CB   1 
ATOM   333  C  CG   . LEU   A 1 68  ? -4.53400  2.52000   14.36000  1.000 72.05387  ?  220 LEU   A CG   1 
ATOM   334  C  CD1  . LEU   A 1 68  ? -3.88000  1.19000   14.01700  1.000 66.88243  ?  220 LEU   A CD1  1 
ATOM   335  C  CD2  . LEU   A 1 68  ? -4.11800  2.99000   15.74500  1.000 75.52171  ?  220 LEU   A CD2  1 
ATOM   336  N  N    . SER   A 1 69  ? -4.31300  7.27900   12.89300  1.000 74.03784  ?  221 SER   A N    1 
ATOM   337  C  CA   . SER   A 1 69  ? -4.26300  8.31500   11.86800  1.000 80.61873  ?  221 SER   A CA   1 
ATOM   338  C  C    . SER   A 1 69  ? -2.89800  8.40000   11.20200  1.000 74.62771  ?  221 SER   A C    1 
ATOM   339  O  O    . SER   A 1 69  ? -2.80900  8.75600   10.02100  1.000 76.74612  ?  221 SER   A O    1 
ATOM   340  C  CB   . SER   A 1 69  ? -4.64400  9.66100   12.48000  1.000 87.11891  ?  221 SER   A CB   1 
ATOM   341  O  OG   . SER   A 1 69  ? -3.53600  10.25000  13.14000  1.000 90.24763  ?  221 SER   A OG   1 
ATOM   342  N  N    . MET   A 1 70  ? -1.83000  8.08600   11.92900  1.000 67.85050  ?  222 MET   A N    1 
ATOM   343  C  CA   . MET   A 1 70  ? -0.48900  8.14000   11.36800  1.000 66.24847  ?  222 MET   A CA   1 
ATOM   344  C  C    . MET   A 1 70  ? -0.08700  6.85600   10.65800  1.000 56.17131  ?  222 MET   A C    1 
ATOM   345  O  O    . MET   A 1 70  ? 0.98700   6.81900   10.04700  1.000 56.83368  ?  222 MET   A O    1 
ATOM   346  C  CB   . MET   A 1 70  ? 0.53100   8.45500   12.46700  1.000 63.30487  ?  222 MET   A CB   1 
ATOM   347  C  CG   . MET   A 1 70  ? 0.50000   9.89900   12.93600  1.000 67.64760  ?  222 MET   A CG   1 
ATOM   348  S  SD   . MET   A 1 70  ? 0.78600   11.06000  11.58700  1.000 67.84622  ?  222 MET   A SD   1 
ATOM   349  C  CE   . MET   A 1 70  ? 2.57600   11.06900  11.53000  1.000 64.90412  ?  222 MET   A CE   1 
ATOM   350  N  N    . LEU   A 1 71  ? -0.91900  5.81400   10.71300  1.000 57.58824  ?  223 LEU   A N    1 
ATOM   351  C  CA   . LEU   A 1 71  ? -0.55800  4.54100   10.09200  1.000 61.17371  ?  223 LEU   A CA   1 
ATOM   352  C  C    . LEU   A 1 71  ? -0.30900  4.64900   8.59100   1.000 56.91069  ?  223 LEU   A C    1 
ATOM   353  O  O    . LEU   A 1 71  ? 0.68700   4.07700   8.11800   1.000 53.64358  ?  223 LEU   A O    1 
ATOM   354  C  CB   . LEU   A 1 71  ? -1.62800  3.49000   10.40900  1.000 63.08618  ?  223 LEU   A CB   1 
ATOM   355  C  CG   . LEU   A 1 71  ? -1.26600  2.05000   10.03300  1.000 55.34874  ?  223 LEU   A CG   1 
ATOM   356  C  CD1  . LEU   A 1 71  ? 0.14400   1.70800   10.49300  1.000 45.12675  ?  223 LEU   A CD1  1 
ATOM   357  C  CD2  . LEU   A 1 71  ? -2.27400  1.06400   10.60300  1.000 55.90543  ?  223 LEU   A CD2  1 
ATOM   358  N  N    . PRO   A 1 72  ? -1.13900  5.33800   7.79000   1.000 54.79360  ?  224 PRO   A N    1 
ATOM   359  C  CA   . PRO   A 1 72  ? -0.80300  5.46900   6.35700   1.000 55.88327  ?  224 PRO   A CA   1 
ATOM   360  C  C    . PRO   A 1 72  ? 0.54400   6.12000   6.11000   1.000 57.98464  ?  224 PRO   A C    1 
ATOM   361  O  O    . PRO   A 1 72  ? 1.33200   5.63200   5.28900   1.000 51.82838  ?  224 PRO   A O    1 
ATOM   362  C  CB   . PRO   A 1 72  ? -1.94700  6.33200   5.80900   1.000 50.64641  ?  224 PRO   A CB   1 
ATOM   363  C  CG   . PRO   A 1 72  ? -3.07100  6.09200   6.72100   1.000 58.60241  ?  224 PRO   A CG   1 
ATOM   364  C  CD   . PRO   A 1 72  ? -2.45300  5.94000   8.08400   1.000 56.32447  ?  224 PRO   A CD   1 
ATOM   365  N  N    . HIS   A 1 73  ? 0.81900   7.23600   6.78500   1.000 50.65353  ?  225 HIS   A N    1 
ATOM   366  C  CA   . HIS   A 1 73  ? 2.07400   7.93700   6.55200   1.000 52.26899  ?  225 HIS   A CA   1 
ATOM   367  C  C    . HIS   A 1 73  ? 3.26100   7.12000   7.04000   1.000 39.71718  ?  225 HIS   A C    1 
ATOM   368  O  O    . HIS   A 1 73  ? 4.27500   7.01300   6.34200   1.000 42.62223  ?  225 HIS   A O    1 
ATOM   369  C  CB   . HIS   A 1 73  ? 2.05800   9.30300   7.23400   1.000 60.93453  ?  225 HIS   A CB   1 
ATOM   370  C  CG   . HIS   A 1 73  ? 3.31900   10.08300  7.03500   1.000 63.88271  ?  225 HIS   A CG   1 
ATOM   371  N  ND1  . HIS   A 1 73  ? 3.66300   10.64500  5.82400   1.000 61.18263  ?  225 HIS   A ND1  1 
ATOM   372  C  CD2  . HIS   A 1 73  ? 4.33000   10.37700  7.88700   1.000 61.36514  ?  225 HIS   A CD2  1 
ATOM   373  C  CE1  . HIS   A 1 73  ? 4.82600   11.26100  5.94200   1.000 65.73974  ?  225 HIS   A CE1  1 
ATOM   374  N  NE2  . HIS   A 1 73  ? 5.25300   11.11200  7.18400   1.000 53.66913  ?  225 HIS   A NE2  1 
ATOM   375  N  N    . LEU   A 1 74  ? 3.15200   6.53000   8.23300   1.000 47.61223  ?  226 LEU   A N    1 
ATOM   376  C  CA   . LEU   A 1 74  ? 4.29200   5.81600   8.79600   1.000 42.12409  ?  226 LEU   A CA   1 
ATOM   377  C  C    . LEU   A 1 74  ? 4.51100   4.47100   8.11700   1.000 45.44915  ?  226 LEU   A C    1 
ATOM   378  O  O    . LEU   A 1 74  ? 5.65100   4.00100   8.04300   1.000 44.06291  ?  226 LEU   A O    1 
ATOM   379  C  CB   . LEU   A 1 74  ? 4.11200   5.64000   10.30200  1.000 49.32021  ?  226 LEU   A CB   1 
ATOM   380  C  CG   . LEU   A 1 74  ? 4.04400   6.96400   11.06700  1.000 52.75335  ?  226 LEU   A CG   1 
ATOM   381  C  CD1  . LEU   A 1 74  ? 3.76800   6.73200   12.53900  1.000 53.04742  ?  226 LEU   A CD1  1 
ATOM   382  C  CD2  . LEU   A 1 74  ? 5.33200   7.75000   10.87500  1.000 50.28024  ?  226 LEU   A CD2  1 
ATOM   383  N  N    . ALA   A 1 75  ? 3.44300   3.84000   7.61800   1.000 47.22695  ?  227 ALA   A N    1 
ATOM   384  C  CA   . ALA   A 1 75  ? 3.61700   2.63000   6.82100   1.000 44.82016  ?  227 ALA   A CA   1 
ATOM   385  C  C    . ALA   A 1 75  ? 4.42900   2.92000   5.56700   1.000 39.70345  ?  227 ALA   A C    1 
ATOM   386  O  O    . ALA   A 1 75  ? 5.33400   2.15600   5.21200   1.000 40.13266  ?  227 ALA   A O    1 
ATOM   387  C  CB   . ALA   A 1 75  ? 2.25800   2.03200   6.45300   1.000 42.00450  ?  227 ALA   A CB   1 
ATOM   388  N  N    . ASP   A 1 76  ? 4.12200   4.02700   4.88600   1.000 40.38065  ?  228 ASP   A N    1 
ATOM   389  C  CA   . ASP   A 1 76  ? 4.90500   4.42600   3.72100   1.000 37.32570  ?  228 ASP   A CA   1 
ATOM   390  C  C    . ASP   A 1 76  ? 6.33400   4.78400   4.11300   1.000 40.89165  ?  228 ASP   A C    1 
ATOM   391  O  O    . ASP   A 1 76  ? 7.28200   4.47100   3.38200   1.000 40.44749  ?  228 ASP   A O    1 
ATOM   392  C  CB   . ASP   A 1 76  ? 4.23100   5.60200   3.01600   1.000 35.03337  ?  228 ASP   A CB   1 
ATOM   393  C  CG   . ASP   A 1 76  ? 2.93000   5.20800   2.33600   1.000 43.28658  ?  228 ASP   A CG   1 
ATOM   394  O  OD1  . ASP   A 1 76  ? 2.15800   6.11300   1.95400   1.000 49.36133  ?  228 ASP   A OD1  1 
ATOM   395  O  OD2  . ASP   A 1 76  ? 2.67800   3.99500   2.18200   1.000 44.00280  ?  228 ASP   A OD2  1 
ATOM   396  N  N    . LEU   A 1 77  ? 6.50700   5.44200   5.26100   1.000 35.38144  ?  229 LEU   A N    1 
ATOM   397  C  CA   . LEU   A 1 77  ? 7.84700   5.76900   5.73800   1.000 38.28358  ?  229 LEU   A CA   1 
ATOM   398  C  C    . LEU   A 1 77  ? 8.64900   4.50300   6.01200   1.000 44.13061  ?  229 LEU   A C    1 
ATOM   399  O  O    . LEU   A 1 77  ? 9.77700   4.34900   5.53000   1.000 41.58604  ?  229 LEU   A O    1 
ATOM   400  C  CB   . LEU   A 1 77  ? 7.75700   6.63400   6.99700   1.000 45.39024  ?  229 LEU   A CB   1 
ATOM   401  C  CG   . LEU   A 1 77  ? 9.05300   6.84500   7.78900   1.000 49.51540  ?  229 LEU   A CG   1 
ATOM   402  C  CD1  . LEU   A 1 77  ? 10.13800  7.44000   6.90600   1.000 38.66466  ?  229 LEU   A CD1  1 
ATOM   403  C  CD2  . LEU   A 1 77  ? 8.81200   7.71600   9.01900   1.000 45.68663  ?  229 LEU   A CD2  1 
ATOM   404  N  N    . VAL   A 1 78  ? 8.07300   3.58100   6.78800   1.000 41.29435  ?  230 VAL   A N    1 
ATOM   405  C  CA   . VAL   A 1 78  ? 8.74800   2.32100   7.08800   1.000 37.61959  ?  230 VAL   A CA   1 
ATOM   406  C  C    . VAL   A 1 78  ? 9.00800   1.53700   5.80900   1.000 40.08737  ?  230 VAL   A C    1 
ATOM   407  O  O    . VAL   A 1 78  ? 10.09900  0.98700   5.61400   1.000 35.04275  ?  230 VAL   A O    1 
ATOM   408  C  CB   . VAL   A 1 78  ? 7.92000   1.50400   8.09800   1.000 41.00924  ?  230 VAL   A CB   1 
ATOM   409  C  CG1  . VAL   A 1 78  ? 8.45300   0.08200   8.20400   1.000 40.94538  ?  230 VAL   A CG1  1 
ATOM   410  C  CG2  . VAL   A 1 78  ? 7.92400   2.18400   9.45600   1.000 45.09680  ?  230 VAL   A CG2  1 
ATOM   411  N  N    . SER   A 1 79  ? 8.01300   1.47400   4.91800   1.000 40.67342  ?  231 SER   A N    1 
ATOM   412  C  CA   . SER   A 1 79  ? 8.19000   0.77500   3.64700   1.000 35.66870  ?  231 SER   A CA   1 
ATOM   413  C  C    . SER   A 1 79  ? 9.32500   1.38300   2.83700   1.000 43.74110  ?  231 SER   A C    1 
ATOM   414  O  O    . SER   A 1 79  ? 10.11900  0.66000   2.22300   1.000 41.94422  ?  231 SER   A O    1 
ATOM   415  C  CB   . SER   A 1 79  ? 6.89000   0.80700   2.84400   1.000 38.27755  ?  231 SER   A CB   1 
ATOM   416  O  OG   . SER   A 1 79  ? 6.94800   -0.07700  1.73800   1.000 38.17986  ?  231 SER   A OG   1 
ATOM   417  N  N    . TYR   A 1 80  ? 9.40600   2.71600   2.81400   1.000 36.61744  ?  232 TYR   A N    1 
ATOM   418  C  CA   . TYR   A 1 80  ? 10.51200  3.39300   2.14700   1.000 26.68222  ?  232 TYR   A CA   1 
ATOM   419  C  C    . TYR   A 1 80  ? 11.84600  3.02200   2.78600   1.000 32.99748  ?  232 TYR   A C    1 
ATOM   420  O  O    . TYR   A 1 80  ? 12.83000  2.75700   2.08500   1.000 29.56766  ?  232 TYR   A O    1 
ATOM   421  C  CB   . TYR   A 1 80  ? 10.27500  4.90300   2.19800   1.000 30.63007  ?  232 TYR   A CB   1 
ATOM   422  C  CG   . TYR   A 1 80  ? 11.35100  5.77100   1.58500   1.000 43.08122  ?  232 TYR   A CG   1 
ATOM   423  C  CD1  . TYR   A 1 80  ? 11.36300  6.03900   0.22300   1.000 44.70250  ?  232 TYR   A CD1  1 
ATOM   424  C  CD2  . TYR   A 1 80  ? 12.33100  6.36100   2.37800   1.000 47.77916  ?  232 TYR   A CD2  1 
ATOM   425  C  CE1  . TYR   A 1 80  ? 12.33400  6.84600   -0.33800  1.000 51.96063  ?  232 TYR   A CE1  1 
ATOM   426  C  CE2  . TYR   A 1 80  ? 13.30600  7.17000   1.82500   1.000 49.41414  ?  232 TYR   A CE2  1 
ATOM   427  C  CZ   . TYR   A 1 80  ? 13.30200  7.40900   0.46600   1.000 52.35513  ?  232 TYR   A CZ   1 
ATOM   428  O  OH   . TYR   A 1 80  ? 14.26700  8.21500   -0.09600  1.000 57.16187  ?  232 TYR   A OH   1 
ATOM   429  N  N    . SER   A 1 81  ? 11.89200  2.98400   4.12000   1.000 32.45894  ?  233 SER   A N    1 
ATOM   430  C  CA   . SER   A 1 81  ? 13.12600  2.63600   4.81800   1.000 40.79917  ?  233 SER   A CA   1 
ATOM   431  C  C    . SER   A 1 81  ? 13.56800  1.21500   4.49100   1.000 42.88783  ?  233 SER   A C    1 
ATOM   432  O  O    . SER   A 1 81  ? 14.76000  0.96100   4.27700   1.000 35.31580  ?  233 SER   A O    1 
ATOM   433  C  CB   . SER   A 1 81  ? 12.93700  2.80600   6.32500   1.000 37.13406  ?  233 SER   A CB   1 
ATOM   434  O  OG   . SER   A 1 81  ? 14.18400  2.86700   6.99600   1.000 49.25513  ?  233 SER   A OG   1 
ATOM   435  N  N    . ILE   A 1 82  ? 12.62000  0.27400   4.44900   1.000 40.04731  ?  234 ILE   A N    1 
ATOM   436  C  CA   . ILE   A 1 82  ? 12.95700  -1.11100  4.12600   1.000 32.21545  ?  234 ILE   A CA   1 
ATOM   437  C  C    . ILE   A 1 82  ? 13.62400  -1.19100  2.75800   1.000 32.64083  ?  234 ILE   A C    1 
ATOM   438  O  O    . ILE   A 1 82  ? 14.58900  -1.94200  2.56600   1.000 38.02452  ?  234 ILE   A O    1 
ATOM   439  C  CB   . ILE   A 1 82  ? 11.70100  -1.99800  4.20100   1.000 34.47681  ?  234 ILE   A CB   1 
ATOM   440  C  CG1  . ILE   A 1 82  ? 11.17800  -2.06100  5.63700   1.000 44.73125  ?  234 ILE   A CG1  1 
ATOM   441  C  CG2  . ILE   A 1 82  ? 11.99400  -3.39800  3.68900   1.000 33.53438  ?  234 ILE   A CG2  1 
ATOM   442  C  CD1  . ILE   A 1 82  ? 9.78400   -2.64300  5.75200   1.000 44.93611  ?  234 ILE   A CD1  1 
ATOM   443  N  N    . GLN   A 1 83  ? 13.13200  -0.41100  1.79200   1.000 30.34124  ?  235 GLN   A N    1 
ATOM   444  C  CA   . GLN   A 1 83  ? 13.77000  -0.36800  0.47900   1.000 39.49227  ?  235 GLN   A CA   1 
ATOM   445  C  C    . GLN   A 1 83  ? 15.21900  0.08400   0.58600   1.000 36.86904  ?  235 GLN   A C    1 
ATOM   446  O  O    . GLN   A 1 83  ? 16.10300  -0.48000  -0.06900  1.000 32.75906  ?  235 GLN   A O    1 
ATOM   447  C  CB   . GLN   A 1 83  ? 12.99400  0.55800   -0.45600  1.000 35.40703  ?  235 GLN   A CB   1 
ATOM   448  C  CG   . GLN   A 1 83  ? 11.56700  0.12500   -0.70000  1.000 38.71781  ?  235 GLN   A CG   1 
ATOM   449  C  CD   . GLN   A 1 83  ? 10.91200  0.88200   -1.83400  1.000 46.82974  ?  235 GLN   A CD   1 
ATOM   450  O  OE1  . GLN   A 1 83  ? 11.53900  1.16000   -2.85700  1.000 53.38367  ?  235 GLN   A OE1  1 
ATOM   451  N  NE2  . GLN   A 1 83  ? 9.64100   1.22400   -1.65700  1.000 55.03939  ?  235 GLN   A NE2  1 
ATOM   452  N  N    . LYS   A 1 84  ? 15.47900  1.10400   1.40600   1.000 31.34316  ?  236 LYS   A N    1 
ATOM   453  C  CA   . LYS   A 1 84  ? 16.84600  1.58300   1.58500   1.000 31.37634  ?  236 LYS   A CA   1 
ATOM   454  C  C    . LYS   A 1 84  ? 17.69800  0.55300   2.31300   1.000 30.37296  ?  236 LYS   A C    1 
ATOM   455  O  O    . LYS   A 1 84  ? 18.88200  0.38500   1.99600   1.000 35.18293  ?  236 LYS   A O    1 
ATOM   456  C  CB   . LYS   A 1 84  ? 16.84000  2.91100   2.34400   1.000 29.59978  ?  236 LYS   A CB   1 
ATOM   457  C  CG   . LYS   A 1 84  ? 16.09000  4.03700   1.64100   1.000 37.21458  ?  236 LYS   A CG   1 
ATOM   458  C  CD   . LYS   A 1 84  ? 16.35900  4.04600   0.14400   1.000 35.87337  ?  236 LYS   A CD   1 
ATOM   459  C  CE   . LYS   A 1 84  ? 16.00200  5.38900   -0.47800  1.000 43.84112  ?  236 LYS   A CE   1 
ATOM   460  N  NZ   . LYS   A 1 84  ? 16.63200  6.53600   0.24400   1.000 43.83585  ?  236 LYS   A NZ   1 
ATOM   461  N  N    . VAL   A 1 85  ? 17.11400  -0.14500  3.29100   1.000 28.29359  ?  237 VAL   A N    1 
ATOM   462  C  CA   . VAL   A 1 85  ? 17.85100  -1.17300  4.02200   1.000 29.98264  ?  237 VAL   A CA   1 
ATOM   463  C  C    . VAL   A 1 85  ? 18.28800  -2.28800  3.08100   1.000 34.96244  ?  237 VAL   A C    1 
ATOM   464  O  O    . VAL   A 1 85  ? 19.42500  -2.76900  3.14900   1.000 35.51417  ?  237 VAL   A O    1 
ATOM   465  C  CB   . VAL   A 1 85  ? 16.99800  -1.71400  5.18400   1.000 27.84413  ?  237 VAL   A CB   1 
ATOM   466  C  CG1  . VAL   A 1 85  ? 17.60100  -2.99800  5.73900   1.000 28.20494  ?  237 VAL   A CG1  1 
ATOM   467  C  CG2  . VAL   A 1 85  ? 16.86700  -0.66100  6.27400   1.000 35.03614  ?  237 VAL   A CG2  1 
ATOM   468  N  N    . ILE   A 1 86  ? 17.39400  -2.71400  2.18600   1.000 32.66566  ?  238 ILE   A N    1 
ATOM   469  C  CA   . ILE   A 1 86  ? 17.74700  -3.74000  1.20900   1.000 30.91251  ?  238 ILE   A CA   1 
ATOM   470  C  C    . ILE   A 1 86  ? 18.86200  -3.24800  0.29700   1.000 29.11523  ?  238 ILE   A C    1 
ATOM   471  O  O    . ILE   A 1 86  ? 19.82200  -3.97600  0.01700   1.000 36.19250  ?  238 ILE   A O    1 
ATOM   472  C  CB   . ILE   A 1 86  ? 16.50300  -4.16000  0.40600   1.000 37.63747  ?  238 ILE   A CB   1 
ATOM   473  C  CG1  . ILE   A 1 86  ? 15.45100  -4.77600  1.33100   1.000 34.23937  ?  238 ILE   A CG1  1 
ATOM   474  C  CG2  . ILE   A 1 86  ? 16.88200  -5.12700  -0.70200  1.000 37.60773  ?  238 ILE   A CG2  1 
ATOM   475  C  CD1  . ILE   A 1 86  ? 14.05400  -4.76800  0.74400   1.000 37.90898  ?  238 ILE   A CD1  1 
ATOM   476  N  N    . GLY   A 1 87  ? 18.75500  -2.00600  -0.18100  1.000 30.10795  ?  239 GLY   A N    1 
ATOM   477  C  CA   . GLY   A 1 87  ? 19.81200  -1.45200  -1.01200  1.000 32.40354  ?  239 GLY   A CA   1 
ATOM   478  C  C    . GLY   A 1 87  ? 21.14700  -1.38600  -0.29300  1.000 36.48743  ?  239 GLY   A C    1 
ATOM   479  O  O    . GLY   A 1 87  ? 22.19800  -1.63000  -0.88900  1.000 33.86211  ?  239 GLY   A O    1 
ATOM   480  N  N    . PHE   A 1 88  ? 21.12300  -1.06400  1.00100   1.000 30.37086  ?  240 PHE   A N    1 
ATOM   481  C  CA   . PHE   A 1 88  ? 22.36200  -1.02500  1.77400   1.000 30.69837  ?  240 PHE   A CA   1 
ATOM   482  C  C    . PHE   A 1 88  ? 22.92400  -2.42600  1.97600   1.000 27.44403  ?  240 PHE   A C    1 
ATOM   483  O  O    . PHE   A 1 88  ? 24.11800  -2.66500  1.75600   1.000 34.37748  ?  240 PHE   A O    1 
ATOM   484  C  CB   . PHE   A 1 88  ? 22.11600  -0.33900  3.12000   1.000 27.91553  ?  240 PHE   A CB   1 
ATOM   485  C  CG   . PHE   A 1 88  ? 23.28200  -0.42400  4.07500   1.000 33.00678  ?  240 PHE   A CG   1 
ATOM   486  C  CD1  . PHE   A 1 88  ? 24.36400  0.43100   3.94600   1.000 27.68391  ?  240 PHE   A CD1  1 
ATOM   487  C  CD2  . PHE   A 1 88  ? 23.28800  -1.35400  5.10600   1.000 31.99320  ?  240 PHE   A CD2  1 
ATOM   488  C  CE1  . PHE   A 1 88  ? 25.43300  0.36100   4.82400   1.000 32.36977  ?  240 PHE   A CE1  1 
ATOM   489  C  CE2  . PHE   A 1 88  ? 24.35600  -1.43000  5.98700   1.000 31.46534  ?  240 PHE   A CE2  1 
ATOM   490  C  CZ   . PHE   A 1 88  ? 25.42800  -0.57100  5.84600   1.000 35.85385  ?  240 PHE   A CZ   1 
ATOM   491  N  N    . ALA   A 1 89  ? 22.07100  -3.37000  2.38400   1.000 30.28026  ?  241 ALA   A N    1 
ATOM   492  C  CA   . ALA   A 1 89  ? 22.53400  -4.72300  2.68100   1.000 35.61505  ?  241 ALA   A CA   1 
ATOM   493  C  C    . ALA   A 1 89  ? 23.14400  -5.38600  1.45400   1.000 37.58590  ?  241 ALA   A C    1 
ATOM   494  O  O    . ALA   A 1 89  ? 24.11300  -6.14700  1.56900   1.000 34.38137  ?  241 ALA   A O    1 
ATOM   495  C  CB   . ALA   A 1 89  ? 21.37900  -5.56400  3.22200   1.000 28.24119  ?  241 ALA   A CB   1 
ATOM   496  N  N    . LYS   A 1 90  ? 22.59400  -5.10700  0.27000   1.000 31.45689  ?  242 LYS   A N    1 
ATOM   497  C  CA   . LYS   A 1 90  ? 23.11000  -5.69300  -0.96200  1.000 33.35722  ?  242 LYS   A CA   1 
ATOM   498  C  C    . LYS   A 1 90  ? 24.54500  -5.28700  -1.24700  1.000 28.01982  ?  242 LYS   A C    1 
ATOM   499  O  O    . LYS   A 1 90  ? 25.23800  -5.97800  -2.00100  1.000 36.03698  ?  242 LYS   A O    1 
ATOM   500  C  CB   . LYS   A 1 90  ? 22.24100  -5.28200  -2.14400  1.000 43.74545  ?  242 LYS   A CB   1 
ATOM   501  C  CG   . LYS   A 1 90  ? 20.92300  -5.99100  -2.20600  1.000 54.21753  ?  242 LYS   A CG   1 
ATOM   502  C  CD   . LYS   A 1 90  ? 20.06200  -5.39500  -3.29100  1.000 61.02509  ?  242 LYS   A CD   1 
ATOM   503  C  CE   . LYS   A 1 90  ? 20.81200  -5.31300  -4.60900  1.000 62.23155  ?  242 LYS   A CE   1 
ATOM   504  N  NZ   . LYS   A 1 90  ? 19.91500  -4.88100  -5.71300  1.000 70.60387  ?  242 LYS   A NZ   1 
ATOM   505  N  N    . MET   A 1 91  ? 25.00000  -4.17800  -0.68100  1.000 32.15077  ?  243 MET   A N    1 
ATOM   506  C  CA   . MET   A 1 91  ? 26.35000  -3.70200  -0.91300  1.000 34.53599  ?  243 MET   A CA   1 
ATOM   507  C  C    . MET   A 1 91  ? 27.30000  -4.05700  0.22000   1.000 38.53139  ?  243 MET   A C    1 
ATOM   508  O  O    . MET   A 1 91  ? 28.47100  -3.67600  0.16500   1.000 44.06898  ?  243 MET   A O    1 
ATOM   509  C  CB   . MET   A 1 91  ? 26.32900  -2.19100  -1.14100  1.000 38.26435  ?  243 MET   A CB   1 
ATOM   510  C  CG   . MET   A 1 91  ? 25.40300  -1.77500  -2.27500  1.000 47.74967  ?  243 MET   A CG   1 
ATOM   511  S  SD   . MET   A 1 91  ? 25.58700  -0.04400  -2.73200  1.000 58.81622  ?  243 MET   A SD   1 
ATOM   512  C  CE   . MET   A 1 91  ? 23.91700  0.55200   -2.48800  1.000 63.88546  ?  243 MET   A CE   1 
ATOM   513  N  N    . ILE   A 1 92  ? 26.83300  -4.77300  1.23600   1.000 33.02553  ?  244 ILE   A N    1 
ATOM   514  C  CA   . ILE   A 1 92  ? 27.74000  -5.24200  2.29000   1.000 30.67084  ?  244 ILE   A CA   1 
ATOM   515  C  C    . ILE   A 1 92  ? 28.70100  -6.26400  1.69400   1.000 35.11044  ?  244 ILE   A C    1 
ATOM   516  O  O    . ILE   A 1 92  ? 28.24800  -7.22400  1.04500   1.000 31.36672  ?  244 ILE   A O    1 
ATOM   517  C  CB   . ILE   A 1 92  ? 26.95000  -5.85500  3.44500   1.000 31.66045  ?  244 ILE   A CB   1 
ATOM   518  C  CG1  . ILE   A 1 92  ? 26.08300  -4.80100  4.13700   1.000 29.45328  ?  244 ILE   A CG1  1 
ATOM   519  C  CG2  . ILE   A 1 92  ? 27.90500  -6.52300  4.43800   1.000 30.88203  ?  244 ILE   A CG2  1 
ATOM   520  C  CD1  . ILE   A 1 92  ? 25.15600  -5.38300  5.18500   1.000 25.16379  ?  244 ILE   A CD1  1 
ATOM   521  N  N    . PRO   A 1 93  ? 30.01900  -6.11000  1.87700   1.000 34.33871  ?  245 PRO   A N    1 
ATOM   522  C  CA   . PRO   A 1 93  ? 30.95600  -7.11100  1.34900   1.000 37.03316  ?  245 PRO   A CA   1 
ATOM   523  C  C    . PRO   A 1 93  ? 30.61100  -8.52200  1.80200   1.000 42.03666  ?  245 PRO   A C    1 
ATOM   524  O  O    . PRO   A 1 93  ? 30.52800  -8.79700  3.00300   1.000 43.88455  ?  245 PRO   A O    1 
ATOM   525  C  CB   . PRO   A 1 93  ? 32.30900  -6.65000  1.90800   1.000 35.33336  ?  245 PRO   A CB   1 
ATOM   526  C  CG   . PRO   A 1 93  ? 32.14400  -5.17400  2.08800   1.000 42.04332  ?  245 PRO   A CG   1 
ATOM   527  C  CD   . PRO   A 1 93  ? 30.71800  -4.99500  2.54000   1.000 38.64158  ?  245 PRO   A CD   1 
ATOM   528  N  N    . GLY   A 1 94  ? 30.37600  -9.41600  0.83900   1.000 39.96704  ?  246 GLY   A N    1 
ATOM   529  C  CA   . GLY   A 1 94  ? 30.04400  -10.79400 1.09900   1.000 45.05326  ?  246 GLY   A CA   1 
ATOM   530  C  C    . GLY   A 1 94  ? 28.55600  -11.09900 1.09200   1.000 50.51542  ?  246 GLY   A C    1 
ATOM   531  O  O    . GLY   A 1 94  ? 28.17300  -12.23400 0.78200   1.000 43.75073  ?  246 GLY   A O    1 
ATOM   532  N  N    . PHE   A 1 95  ? 27.71200  -10.11700 1.42900   1.000 45.07778  ?  247 PHE   A N    1 
ATOM   533  C  CA   . PHE   A 1 95  ? 26.27800  -10.37200 1.54900   1.000 36.12194  ?  247 PHE   A CA   1 
ATOM   534  C  C    . PHE   A 1 95  ? 25.69500  -10.88000 0.23700   1.000 44.39956  ?  247 PHE   A C    1 
ATOM   535  O  O    . PHE   A 1 95  ? 24.95600  -11.87200 0.21500   1.000 38.09213  ?  247 PHE   A O    1 
ATOM   536  C  CB   . PHE   A 1 95  ? 25.55300  -9.10200  1.99800   1.000 39.66713  ?  247 PHE   A CB   1 
ATOM   537  C  CG   . PHE   A 1 95  ? 24.07600  -9.29300  2.23400   1.000 35.85151  ?  247 PHE   A CG   1 
ATOM   538  C  CD1  . PHE   A 1 95  ? 23.61000  -9.70800  3.46900   1.000 33.70151  ?  247 PHE   A CD1  1 
ATOM   539  C  CD2  . PHE   A 1 95  ? 23.15700  -9.05500  1.22300   1.000 39.01507  ?  247 PHE   A CD2  1 
ATOM   540  C  CE1  . PHE   A 1 95  ? 22.25900  -9.88500  3.69400   1.000 34.47698  ?  247 PHE   A CE1  1 
ATOM   541  C  CE2  . PHE   A 1 95  ? 21.80200  -9.23100  1.44100   1.000 38.25474  ?  247 PHE   A CE2  1 
ATOM   542  C  CZ   . PHE   A 1 95  ? 21.35300  -9.64700  2.67900   1.000 40.29210  ?  247 PHE   A CZ   1 
ATOM   543  N  N    . ARG   A 1 96  ? 26.01800  -10.20700 -0.87000  1.000 48.22441  ?  248 ARG   A N    1 
ATOM   544  C  CA   . ARG   A 1 96  ? 25.49700  -10.59600 -2.17500  1.000 53.97241  ?  248 ARG   A CA   1 
ATOM   545  C  C    . ARG   A 1 96  ? 26.00000  -11.96400 -2.61400  1.000 51.37310  ?  248 ARG   A C    1 
ATOM   546  O  O    . ARG   A 1 96  ? 25.41400  -12.56800 -3.51900  1.000 52.77342  ?  248 ARG   A O    1 
ATOM   547  C  CB   . ARG   A 1 96  ? 25.87200  -9.54000  -3.21700  1.000 63.71721  ?  248 ARG   A CB   1 
ATOM   548  C  CG   . ARG   A 1 96  ? 24.84100  -9.32100  -4.30600  1.000 75.55770  ?  248 ARG   A CG   1 
ATOM   549  C  CD   . ARG   A 1 96  ? 25.52000  -8.88100  -5.59300  1.000 95.04736  ?  248 ARG   A CD   1 
ATOM   550  N  NE   . ARG   A 1 96  ? 26.64100  -9.75500  -5.93300  1.000 108.52865 ?  248 ARG   A NE   1 
ATOM   551  C  CZ   . ARG   A 1 96  ? 26.51500  -11.00000 -6.38300  1.000 113.18381 ?  248 ARG   A CZ   1 
ATOM   552  N  NH1  . ARG   A 1 96  ? 27.59600  -11.71600 -6.65800  1.000 109.96223 ?  248 ARG   A NH1  1 
ATOM   553  N  NH2  . ARG   A 1 96  ? 25.31100  -11.52800 -6.56500  1.000 114.05530 ?  248 ARG   A NH2  1 
ATOM   554  N  N    . ASP   A 1 97  ? 27.07300  -12.46300 -1.99700  1.000 48.32363  ?  249 ASP   A N    1 
ATOM   555  C  CA   . ASP   A 1 97  ? 27.58000  -13.78900 -2.31800  1.000 43.87158  ?  249 ASP   A CA   1 
ATOM   556  C  C    . ASP   A 1 97  ? 26.79300  -14.89800 -1.63400  1.000 44.54501  ?  249 ASP   A C    1 
ATOM   557  O  O    . ASP   A 1 97  ? 26.84900  -16.04500 -2.08900  1.000 55.67985  ?  249 ASP   A O    1 
ATOM   558  C  CB   . ASP   A 1 97  ? 29.05800  -13.89200 -1.93800  1.000 45.72747  ?  249 ASP   A CB   1 
ATOM   559  C  CG   . ASP   A 1 97  ? 29.93800  -12.98700 -2.77700  1.000 55.56143  ?  249 ASP   A CG   1 
ATOM   560  O  OD1  . ASP   A 1 97  ? 29.46800  -12.50900 -3.83200  1.000 54.73136  ?  249 ASP   A OD1  1 
ATOM   561  O  OD2  . ASP   A 1 97  ? 31.09900  -12.75300 -2.38100  1.000 51.71134  ?  249 ASP   A OD2  1 
ATOM   562  N  N    . LEU   A 1 98  ? 26.07100  -14.58700 -0.56100  1.000 44.42633  ?  250 LEU   A N    1 
ATOM   563  C  CA   . LEU   A 1 98  ? 25.23100  -15.57600 0.09600   1.000 44.24498  ?  250 LEU   A CA   1 
ATOM   564  C  C    . LEU   A 1 98  ? 24.10800  -16.02100 -0.83600  1.000 47.96048  ?  250 LEU   A C    1 
ATOM   565  O  O    . LEU   A 1 98  ? 23.77800  -15.35000 -1.81900  1.000 49.83596  ?  250 LEU   A O    1 
ATOM   566  C  CB   . LEU   A 1 98  ? 24.63600  -15.00800 1.38600   1.000 33.07867  ?  250 LEU   A CB   1 
ATOM   567  C  CG   . LEU   A 1 98  ? 25.62100  -14.44800 2.41400   1.000 35.05582  ?  250 LEU   A CG   1 
ATOM   568  C  CD1  . LEU   A 1 98  ? 24.87900  -13.75600 3.54700   1.000 31.81475  ?  250 LEU   A CD1  1 
ATOM   569  C  CD2  . LEU   A 1 98  ? 26.51900  -15.55100 2.95100   1.000 39.42078  ?  250 LEU   A CD2  1 
ATOM   570  N  N    . THR   A 1 99  ? 23.52000  -17.17300 -0.51700  1.000 46.89259  ?  251 THR   A N    1 
ATOM   571  C  CA   . THR   A 1 99  ? 22.35100  -17.62900 -1.25500  1.000 46.85141  ?  251 THR   A CA   1 
ATOM   572  C  C    . THR   A 1 99  ? 21.19600  -16.65200 -1.06000  1.000 41.66216  ?  251 THR   A C    1 
ATOM   573  O  O    . THR   A 1 99  ? 21.14100  -15.90100 -0.08100  1.000 37.38289  ?  251 THR   A O    1 
ATOM   574  C  CB   . THR   A 1 99  ? 21.92500  -19.02700 -0.80200  1.000 44.36197  ?  251 THR   A CB   1 
ATOM   575  O  OG1  . THR   A 1 99  ? 21.34400  -18.95200 0.50700   1.000 39.40369  ?  251 THR   A OG1  1 
ATOM   576  C  CG2  . THR   A 1 99  ? 23.11600  -19.96700 -0.76700  1.000 39.97272  ?  251 THR   A CG2  1 
ATOM   577  N  N    . SER   A 1 100 ? 20.26400  -16.66700 -2.01700  1.000 42.02480  ?  252 SER   A N    1 
ATOM   578  C  CA   . SER   A 1 100 ? 19.09700  -15.79300 -1.93000  1.000 41.02781  ?  252 SER   A CA   1 
ATOM   579  C  C    . SER   A 1 100 ? 18.29000  -16.07300 -0.67100  1.000 38.98453  ?  252 SER   A C    1 
ATOM   580  O  O    . SER   A 1 100 ? 17.80300  -15.14300 -0.01800  1.000 37.57064  ?  252 SER   A O    1 
ATOM   581  C  CB   . SER   A 1 100 ? 18.21800  -15.96300 -3.17100  1.000 39.00470  ?  252 SER   A CB   1 
ATOM   582  O  OG   . SER   A 1 100 ? 18.96800  -15.77300 -4.35700  1.000 57.40339  ?  252 SER   A OG   1 
ATOM   583  N  N    . ASP   A 1 101 ? 18.13900  -17.35100 -0.31300  1.000 36.95040  ?  253 ASP   A N    1 
ATOM   584  C  CA   . ASP   A 1 101 ? 17.36500  -17.70900 0.87200   1.000 39.73529  ?  253 ASP   A CA   1 
ATOM   585  C  C    . ASP   A 1 101 ? 17.94800  -17.06600 2.12300   1.000 40.74067  ?  253 ASP   A C    1 
ATOM   586  O  O    . ASP   A 1 101 ? 17.21700  -16.49100 2.93800   1.000 37.02453  ?  253 ASP   A O    1 
ATOM   587  C  CB   . ASP   A 1 101 ? 17.31600  -19.22900 1.02700   1.000 40.46606  ?  253 ASP   A CB   1 
ATOM   588  C  CG   . ASP   A 1 101 ? 16.40400  -19.88900 0.01500   1.000 59.02946  ?  253 ASP   A CG   1 
ATOM   589  O  OD1  . ASP   A 1 101 ? 16.79200  -19.96800 -1.16900  1.000 65.72820  ?  253 ASP   A OD1  1 
ATOM   590  O  OD2  . ASP   A 1 101 ? 15.30400  -20.33500 0.40500   1.000 60.19520  ?  253 ASP   A OD2  1 
ATOM   591  N  N    . ASP   A 1 102 ? 19.27000  -17.15400 2.29000   1.000 37.46269  ?  254 ASP   A N    1 
ATOM   592  C  CA   . ASP   A 1 102 ? 19.90400  -16.56400 3.46300   1.000 33.26358  ?  254 ASP   A CA   1 
ATOM   593  C  C    . ASP   A 1 102 ? 19.80300  -15.04200 3.44200   1.000 34.07380  ?  254 ASP   A C    1 
ATOM   594  O  O    . ASP   A 1 102 ? 19.52600  -14.42200 4.47600   1.000 39.64191  ?  254 ASP   A O    1 
ATOM   595  C  CB   . ASP   A 1 102 ? 21.36200  -17.01500 3.55300   1.000 37.90285  ?  254 ASP   A CB   1 
ATOM   596  C  CG   . ASP   A 1 102 ? 21.50800  -18.39000 4.18900   1.000 48.21002  ?  254 ASP   A CG   1 
ATOM   597  O  OD1  . ASP   A 1 102 ? 22.57900  -19.01500 4.02600   1.000 44.90893  ?  254 ASP   A OD1  1 
ATOM   598  O  OD2  . ASP   A 1 102 ? 20.55100  -18.84500 4.85100   1.000 45.70068  ?  254 ASP   A OD2  1 
ATOM   599  N  N    . GLN   A 1 103 ? 20.01700  -14.42300 2.27700   1.000 33.14323  ?  255 GLN   A N    1 
ATOM   600  C  CA   . GLN   A 1 103 ? 19.83400  -12.97800 2.16300   1.000 36.51808  ?  255 GLN   A CA   1 
ATOM   601  C  C    . GLN   A 1 103 ? 18.43500  -12.56900 2.59600   1.000 31.39292  ?  255 GLN   A C    1 
ATOM   602  O  O    . GLN   A 1 103 ? 18.26000  -11.58600 3.32700   1.000 30.00576  ?  255 GLN   A O    1 
ATOM   603  C  CB   . GLN   A 1 103 ? 20.09300  -12.52200 0.72600   1.000 37.58176  ?  255 GLN   A CB   1 
ATOM   604  C  CG   . GLN   A 1 103 ? 21.49100  -12.80100 0.22000   1.000 40.99758  ?  255 GLN   A CG   1 
ATOM   605  C  CD   . GLN   A 1 103 ? 21.69000  -12.33700 -1.20700  1.000 42.39737  ?  255 GLN   A CD   1 
ATOM   606  O  OE1  . GLN   A 1 103 ? 21.08100  -11.36400 -1.64400  1.000 45.68894  ?  255 GLN   A OE1  1 
ATOM   607  N  NE2  . GLN   A 1 103 ? 22.54200  -13.03800 -1.94400  1.000 46.91742  ?  255 GLN   A NE2  1 
ATOM   608  N  N    . ILE   A 1 104 ? 17.42700  -13.33300 2.17000   1.000 30.74202  ?  256 ILE   A N    1 
ATOM   609  C  CA   . ILE   A 1 104 ? 16.04200  -13.02100 2.50900   1.000 39.10202  ?  256 ILE   A CA   1 
ATOM   610  C  C    . ILE   A 1 104 ? 15.81700  -13.15600 4.01000   1.000 34.28644  ?  256 ILE   A C    1 
ATOM   611  O  O    . ILE   A 1 104 ? 15.25000  -12.26500 4.65400   1.000 34.07008  ?  256 ILE   A O    1 
ATOM   612  C  CB   . ILE   A 1 104 ? 15.08300  -13.92300 1.71100   1.000 38.85999  ?  256 ILE   A CB   1 
ATOM   613  C  CG1  . ILE   A 1 104 ? 14.98900  -13.45400 0.25700   1.000 39.19278  ?  256 ILE   A CG1  1 
ATOM   614  C  CG2  . ILE   A 1 104 ? 13.70600  -13.95400 2.35800   1.000 36.47269  ?  256 ILE   A CG2  1 
ATOM   615  C  CD1  . ILE   A 1 104 ? 14.29500  -14.44500 -0.65100  1.000 41.72113  ?  256 ILE   A CD1  1 
ATOM   616  N  N    A VAL   A 1 105 ? 16.26600  -14.26700 4.60100   0.310 33.32905  ?  257 VAL   A N    1 
ATOM   617  N  N    B VAL   A 1 105 ? 16.24300  -14.28700 4.57800   0.690 31.42272  ?  257 VAL   A N    1 
ATOM   618  C  CA   A VAL   A 1 105 ? 16.01400  -14.46100 6.02700   0.310 35.35407  ?  257 VAL   A CA   1 
ATOM   619  C  CA   B VAL   A 1 105 ? 16.09300  -14.52700 6.01000   0.690 36.36047  ?  257 VAL   A CA   1 
ATOM   620  C  C    A VAL   A 1 105 ? 16.80500  -13.46100 6.86500   0.310 32.28142  ?  257 VAL   A C    1 
ATOM   621  C  C    B VAL   A 1 105 ? 16.77800  -13.42700 6.81200   0.690 31.16837  ?  257 VAL   A C    1 
ATOM   622  O  O    A VAL   A 1 105 ? 16.35000  -13.05200 7.94000   0.310 34.16208  ?  257 VAL   A O    1 
ATOM   623  O  O    B VAL   A 1 105 ? 16.22300  -12.91100 7.78900   0.690 30.39260  ?  257 VAL   A O    1 
ATOM   624  C  CB   A VAL   A 1 105 ? 16.30400  -15.91600 6.45400   0.310 37.88799  ?  257 VAL   A CB   1 
ATOM   625  C  CB   B VAL   A 1 105 ? 16.64400  -15.92100 6.36500   0.690 38.82362  ?  257 VAL   A CB   1 
ATOM   626  C  CG1  A VAL   A 1 105 ? 15.51600  -16.89400 5.59300   0.310 39.70563  ?  257 VAL   A CG1  1 
ATOM   627  C  CG1  B VAL   A 1 105 ? 17.11300  -15.96900 7.80800   0.690 40.52224  ?  257 VAL   A CG1  1 
ATOM   628  C  CG2  A VAL   A 1 105 ? 17.79300  -16.22300 6.40800   0.310 39.42677  ?  257 VAL   A CG2  1 
ATOM   629  C  CG2  B VAL   A 1 105 ? 15.59600  -16.99300 6.09400   0.690 40.99494  ?  257 VAL   A CG2  1 
ATOM   630  N  N    . LEU   A 1 106 ? 17.98200  -13.03500 6.39700   1.000 30.30995  ?  258 LEU   A N    1 
ATOM   631  C  CA   . LEU   A 1 106 ? 18.73300  -12.02900 7.14200   1.000 34.94228  ?  258 LEU   A CA   1 
ATOM   632  C  C    . LEU   A 1 106 ? 18.04400  -10.67200 7.08200   1.000 38.14225  ?  258 LEU   A C    1 
ATOM   633  O  O    . LEU   A 1 106 ? 17.98200  -9.95300  8.08700   1.000 31.99522  ?  258 LEU   A O    1 
ATOM   634  C  CB   . LEU   A 1 106 ? 20.16000  -11.93100 6.60600   1.000 35.94236  ?  258 LEU   A CB   1 
ATOM   635  C  CG   . LEU   A 1 106 ? 21.06100  -13.13300 6.89100   1.000 33.18996  ?  258 LEU   A CG   1 
ATOM   636  C  CD1  . LEU   A 1 106 ? 22.41300  -12.95500 6.21900   1.000 26.33993  ?  258 LEU   A CD1  1 
ATOM   637  C  CD2  . LEU   A 1 106 ? 21.21900  -13.33700 8.38500   1.000 31.13330  ?  258 LEU   A CD2  1 
ATOM   638  N  N    . LEU   A 1 107 ? 17.50800  -10.31300 5.91600   1.000 34.65080  ?  259 LEU   A N    1 
ATOM   639  C  CA   . LEU   A 1 107 ? 16.82400  -9.03300  5.78500   1.000 33.70913  ?  259 LEU   A CA   1 
ATOM   640  C  C    . LEU   A 1 107 ? 15.50300  -9.02700  6.54300   1.000 25.93334  ?  259 LEU   A C    1 
ATOM   641  O  O    . LEU   A 1 107 ? 15.16000  -8.03100  7.19000   1.000 33.30415  ?  259 LEU   A O    1 
ATOM   642  C  CB   . LEU   A 1 107 ? 16.60700  -8.71200  4.31000   1.000 33.56677  ?  259 LEU   A CB   1 
ATOM   643  C  CG   . LEU   A 1 107 ? 17.88300  -8.19000  3.65800   1.000 42.09535  ?  259 LEU   A CG   1 
ATOM   644  C  CD1  . LEU   A 1 107 ? 17.77000  -8.22600  2.15100   1.000 48.12671  ?  259 LEU   A CD1  1 
ATOM   645  C  CD2  . LEU   A 1 107 ? 18.16400  -6.78200  4.15300   1.000 38.80075  ?  259 LEU   A CD2  1 
ATOM   646  N  N    . LYS   A 1 108 ? 14.75300  -10.13100 6.48600   1.000 29.88539  ?  260 LYS   A N    1 
ATOM   647  C  CA   . LYS   A 1 108 ? 13.44900  -10.17300 7.14000   1.000 39.58072  ?  260 LYS   A CA   1 
ATOM   648  C  C    . LYS   A 1 108 ? 13.57200  -9.99000  8.64700   1.000 39.99950  ?  260 LYS   A C    1 
ATOM   649  O  O    . LYS   A 1 108 ? 12.75300  -9.30100  9.26600   1.000 43.50299  ?  260 LYS   A O    1 
ATOM   650  C  CB   . LYS   A 1 108 ? 12.74400  -11.49200 6.82700   1.000 35.06626  ?  260 LYS   A CB   1 
ATOM   651  C  CG   . LYS   A 1 108 ? 11.86900  -11.45500 5.59000   1.000 44.95980  ?  260 LYS   A CG   1 
ATOM   652  C  CD   . LYS   A 1 108 ? 11.09300  -12.75300 5.43200   1.000 52.54262  ?  260 LYS   A CD   1 
ATOM   653  C  CE   . LYS   A 1 108 ? 9.66900   -12.62300 5.95900   1.000 62.06117  ?  260 LYS   A CE   1 
ATOM   654  N  NZ   . LYS   A 1 108 ? 9.61200   -12.56200 7.44600   1.000 63.58557  ?  260 LYS   A NZ   1 
ATOM   655  N  N    . SER   A 1 109 ? 14.58600  -10.60500 9.25700   1.000 43.12541  ?  261 SER   A N    1 
ATOM   656  C  CA   . SER   A 1 109 ? 14.71300  -10.55300 10.70900  1.000 40.59348  ?  261 SER   A CA   1 
ATOM   657  C  C    . SER   A 1 109 ? 15.40800  -9.28500  11.18300  1.000 31.93342  ?  261 SER   A C    1 
ATOM   658  O  O    . SER   A 1 109 ? 15.16900  -8.84100  12.31200  1.000 39.61040  ?  261 SER   A O    1 
ATOM   659  C  CB   . SER   A 1 109 ? 15.46700  -11.78400 11.21400  1.000 42.42434  ?  261 SER   A CB   1 
ATOM   660  O  OG   . SER   A 1 109 ? 16.47500  -12.16900 10.29800  1.000 53.14247  ?  261 SER   A OG   1 
ATOM   661  N  N    . SER   A 1 110 ? 16.25500  -8.68300  10.34900  1.000 30.29577  ?  262 SER   A N    1 
ATOM   662  C  CA   . SER   A 1 110 ? 17.01900  -7.51300  10.76100  1.000 35.36565  ?  262 SER   A CA   1 
ATOM   663  C  C    . SER   A 1 110 ? 16.39900  -6.18800  10.34000  1.000 37.73480  ?  262 SER   A C    1 
ATOM   664  O  O    . SER   A 1 110 ? 16.79500  -5.15000  10.88000  1.000 36.25229  ?  262 SER   A O    1 
ATOM   665  C  CB   . SER   A 1 110 ? 18.44500  -7.58400  10.20300  1.000 36.48074  ?  262 SER   A CB   1 
ATOM   666  O  OG   . SER   A 1 110 ? 18.45400  -7.38200  8.80100   1.000 33.70598  ?  262 SER   A OG   1 
ATOM   667  N  N    . ALA   A 1 111 ? 15.44200  -6.19300  9.40600   1.000 28.91780  ?  263 ALA   A N    1 
ATOM   668  C  CA   . ALA   A 1 111 ? 14.94300  -4.94100  8.84000   1.000 25.61596  ?  263 ALA   A CA   1 
ATOM   669  C  C    . ALA   A 1 111 ? 14.44600  -3.99100  9.92300   1.000 26.09047  ?  263 ALA   A C    1 
ATOM   670  O  O    . ALA   A 1 111 ? 14.80600  -2.80900  9.94100   1.000 30.51862  ?  263 ALA   A O    1 
ATOM   671  C  CB   . ALA   A 1 111 ? 13.83400  -5.22400  7.82500   1.000 31.46280  ?  263 ALA   A CB   1 
ATOM   672  N  N    . ILE   A 1 112 ? 13.62300  -4.49800  10.84500  1.000 28.33855  ?  264 ILE   A N    1 
ATOM   673  C  CA   . ILE   A 1 112 ? 13.07300  -3.65000  11.90000  1.000 34.16838  ?  264 ILE   A CA   1 
ATOM   674  C  C    . ILE   A 1 112 ? 14.18900  -3.08700  12.77500  1.000 40.72611  ?  264 ILE   A C    1 
ATOM   675  O  O    . ILE   A 1 112 ? 14.11900  -1.94000  13.23700  1.000 41.43136  ?  264 ILE   A O    1 
ATOM   676  C  CB   . ILE   A 1 112 ? 12.03500  -4.43300  12.72700  1.000 35.76122  ?  264 ILE   A CB   1 
ATOM   677  C  CG1  . ILE   A 1 112 ? 11.38200  -3.52600  13.77200  1.000 40.65340  ?  264 ILE   A CG1  1 
ATOM   678  C  CG2  . ILE   A 1 112 ? 12.66700  -5.65700  13.38300  1.000 40.56618  ?  264 ILE   A CG2  1 
ATOM   679  C  CD1  . ILE   A 1 112 ? 10.65900  -2.33800  13.17600  1.000 41.30019  ?  264 ILE   A CD1  1 
ATOM   680  N  N    . GLU   A 1 113 ? 15.24200  -3.87600  13.00400  1.000 32.41307  ?  265 GLU   A N    1 
ATOM   681  C  CA   . GLU   A 1 113 ? 16.35900  -3.39900  13.81100  1.000 36.82542  ?  265 GLU   A CA   1 
ATOM   682  C  C    . GLU   A 1 113 ? 17.17000  -2.34700  13.06500  1.000 33.36483  ?  265 GLU   A C    1 
ATOM   683  O  O    . GLU   A 1 113 ? 17.56400  -1.33100  13.64800  1.000 31.27754  ?  265 GLU   A O    1 
ATOM   684  C  CB   . GLU   A 1 113 ? 17.24800  -4.57300  14.21600  1.000 34.51433  ?  265 GLU   A CB   1 
ATOM   685  C  CG   . GLU   A 1 113 ? 16.53500  -5.63900  15.02700  1.000 38.61061  ?  265 GLU   A CG   1 
ATOM   686  C  CD   . GLU   A 1 113 ? 17.41900  -6.83700  15.30800  1.000 40.98830  ?  265 GLU   A CD   1 
ATOM   687  O  OE1  . GLU   A 1 113 ? 18.65800  -6.68200  15.28700  1.000 39.88985  ?  265 GLU   A OE1  1 
ATOM   688  O  OE2  . GLU   A 1 113 ? 16.87400  -7.93500  15.54400  1.000 44.75536  ?  265 GLU   A OE2  1 
ATOM   689  N  N    . VAL   A 1 114 ? 17.43200  -2.57300  11.77600  1.000 32.17502  ?  266 VAL   A N    1 
ATOM   690  C  CA   . VAL   A 1 114 ? 18.20000  -1.60500  10.99900  1.000 29.94630  ?  266 VAL   A CA   1 
ATOM   691  C  C    . VAL   A 1 114 ? 17.42500  -0.30500  10.85300  1.000 34.05157  ?  266 VAL   A C    1 
ATOM   692  O  O    . VAL   A 1 114 ? 18.01100  0.78400   10.84200  1.000 36.19093  ?  266 VAL   A O    1 
ATOM   693  C  CB   . VAL   A 1 114 ? 18.57800  -2.19400  9.62900   1.000 31.30508  ?  266 VAL   A CB   1 
ATOM   694  C  CG1  . VAL   A 1 114 ? 19.49300  -1.23500  8.87500   1.000 28.03840  ?  266 VAL   A CG1  1 
ATOM   695  C  CG2  . VAL   A 1 114 ? 19.25100  -3.53400  9.81000   1.000 33.19243  ?  266 VAL   A CG2  1 
ATOM   696  N  N    . ILE   A 1 115 ? 16.09900  -0.39700  10.73200  1.000 29.60340  ?  267 ILE   A N    1 
ATOM   697  C  CA   . ILE   A 1 115 ? 15.26400  0.80000   10.69400  1.000 34.67015  ?  267 ILE   A CA   1 
ATOM   698  C  C    . ILE   A 1 115 ? 15.45300  1.61600   11.96700  1.000 42.35434  ?  267 ILE   A C    1 
ATOM   699  O  O    . ILE   A 1 115 ? 15.60100  2.84400   11.92600  1.000 38.70906  ?  267 ILE   A O    1 
ATOM   700  C  CB   . ILE   A 1 115 ? 13.78900  0.41400   10.48300  1.000 38.23446  ?  267 ILE   A CB   1 
ATOM   701  C  CG1  . ILE   A 1 115 ? 13.51000  0.15400   9.00200   1.000 36.38512  ?  267 ILE   A CG1  1 
ATOM   702  C  CG2  . ILE   A 1 115 ? 12.86300  1.48800   11.03000  1.000 39.96009  ?  267 ILE   A CG2  1 
ATOM   703  C  CD1  . ILE   A 1 115 ? 12.13400  -0.42000  8.74300   1.000 45.11508  ?  267 ILE   A CD1  1 
ATOM   704  N  N    . MET   A 1 116 ? 15.45800  0.94200   13.11900  1.000 35.99551  ?  268 MET   A N    1 
ATOM   705  C  CA   . MET   A 1 116 ? 15.66400  1.64800   14.37900  1.000 34.66326  ?  268 MET   A CA   1 
ATOM   706  C  C    . MET   A 1 116 ? 17.05400  2.26700   14.43800  1.000 32.46914  ?  268 MET   A C    1 
ATOM   707  O  O    . MET   A 1 116 ? 17.22100  3.38500   14.93700  1.000 36.24825  ?  268 MET   A O    1 
ATOM   708  C  CB   . MET   A 1 116 ? 15.43900  0.69900   15.55600  1.000 37.23407  ?  268 MET   A CB   1 
ATOM   709  C  CG   . MET   A 1 116 ? 13.97000  0.42800   15.85600  1.000 46.76137  ?  268 MET   A CG   1 
ATOM   710  S  SD   . MET   A 1 116 ? 13.68700  -1.10100  16.77300  1.000 46.76520  ?  268 MET   A SD   1 
ATOM   711  C  CE   . MET   A 1 116 ? 11.89600  -1.18000  16.76700  1.000 47.79805  ?  268 MET   A CE   1 
ATOM   712  N  N    . LEU   A 1 117 ? 18.06100  1.56100   13.91600  1.000 38.06788  ?  269 LEU   A N    1 
ATOM   713  C  CA   . LEU   A 1 117 ? 19.42100  2.09600   13.90200  1.000 35.81117  ?  269 LEU   A CA   1 
ATOM   714  C  C    . LEU   A 1 117 ? 19.53600  3.30000   12.97500  1.000 41.69508  ?  269 LEU   A C    1 
ATOM   715  O  O    . LEU   A 1 117 ? 20.06000  4.34900   13.36800  1.000 36.49767  ?  269 LEU   A O    1 
ATOM   716  C  CB   . LEU   A 1 117 ? 20.41400  1.01700   13.47300  1.000 28.74108  ?  269 LEU   A CB   1 
ATOM   717  C  CG   . LEU   A 1 117 ? 20.82300  -0.05800  14.47400  1.000 42.48965  ?  269 LEU   A CG   1 
ATOM   718  C  CD1  . LEU   A 1 117 ? 21.56700  -1.17900  13.75800  1.000 36.48334  ?  269 LEU   A CD1  1 
ATOM   719  C  CD2  . LEU   A 1 117 ? 21.67300  0.53800   15.58900  1.000 43.80143  ?  269 LEU   A CD2  1 
ATOM   720  N  N    . ARG   A 1 118 ? 19.07200  3.16300   11.73000  1.000 34.81635  ?  270 ARG   A N    1 
ATOM   721  C  CA   . ARG   A 1 118 ? 19.27400  4.23400   10.75900  1.000 37.74101  ?  270 ARG   A CA   1 
ATOM   722  C  C    . ARG   A 1 118 ? 18.44300  5.46600   11.09200  1.000 36.62739  ?  270 ARG   A C    1 
ATOM   723  O  O    . ARG   A 1 118 ? 18.83300  6.58500   10.73800  1.000 42.19148  ?  270 ARG   A O    1 
ATOM   724  C  CB   . ARG   A 1 118 ? 18.96100  3.73800   9.34600   1.000 35.70606  ?  270 ARG   A CB   1 
ATOM   725  C  CG   . ARG   A 1 118 ? 17.50500  3.39300   9.09800   1.000 38.03111  ?  270 ARG   A CG   1 
ATOM   726  C  CD   . ARG   A 1 118 ? 17.34300  2.59900   7.80700   1.000 36.15038  ?  270 ARG   A CD   1 
ATOM   727  N  NE   . ARG   A 1 118 ? 17.64400  3.39600   6.61900   1.000 35.33586  ?  270 ARG   A NE   1 
ATOM   728  C  CZ   . ARG   A 1 118 ? 18.78200  3.32600   5.93300   1.000 38.69868  ?  270 ARG   A CZ   1 
ATOM   729  N  NH1  . ARG   A 1 118 ? 19.74300  2.49100   6.31100   1.000 45.91887  ?  270 ARG   A NH1  1 
ATOM   730  N  NH2  . ARG   A 1 118 ? 18.96000  4.09300   4.86700   1.000 33.69618  ?  270 ARG   A NH2  1 
ATOM   731  N  N    . SER   A 1 119 ? 17.30900  5.29300   11.77400  1.000 36.06122  ?  271 SER   A N    1 
ATOM   732  C  CA   . SER   A 1 119 ? 16.51300  6.44600   12.17700  1.000 35.97829  ?  271 SER   A CA   1 
ATOM   733  C  C    . SER   A 1 119 ? 17.22000  7.29400   13.22600  1.000 36.25663  ?  271 SER   A C    1 
ATOM   734  O  O    . SER   A 1 119 ? 16.81300  8.43800   13.45700  1.000 38.57505  ?  271 SER   A O    1 
ATOM   735  C  CB   . SER   A 1 119 ? 15.15000  5.99200   12.70400  1.000 35.44943  ?  271 SER   A CB   1 
ATOM   736  O  OG   . SER   A 1 119 ? 15.26600  5.39000   13.98100  1.000 37.91692  ?  271 SER   A OG   1 
ATOM   737  N  N    . ASN   A 1 120 ? 18.26700  6.76200   13.86100  1.000 40.88093  ?  272 ASN   A N    1 
ATOM   738  C  CA   . ASN   A 1 120 ? 18.99600  7.52700   14.86700  1.000 37.57281  ?  272 ASN   A CA   1 
ATOM   739  C  C    . ASN   A 1 120 ? 19.68600  8.74200   14.26200  1.000 39.09722  ?  272 ASN   A C    1 
ATOM   740  O  O    . ASN   A 1 120 ? 19.90300  9.74100   14.95700  1.000 38.31082  ?  272 ASN   A O    1 
ATOM   741  C  CB   . ASN   A 1 120 ? 20.01300  6.62600   15.56400  1.000 32.29636  ?  272 ASN   A CB   1 
ATOM   742  C  CG   . ASN   A 1 120 ? 20.58100  7.25300   16.81500  1.000 41.23762  ?  272 ASN   A CG   1 
ATOM   743  O  OD1  . ASN   A 1 120 ? 21.75300  7.62400   16.85700  1.000 46.85468  ?  272 ASN   A OD1  1 
ATOM   744  N  ND2  . ASN   A 1 120 ? 19.75200  7.37200   17.84800  1.000 35.98807  ?  272 ASN   A ND2  1 
ATOM   745  N  N    . GLN   A 1 121 ? 20.04000  8.67600   12.97600  1.000 39.92427  ?  273 GLN   A N    1 
ATOM   746  C  CA   . GLN   A 1 121 ? 20.63200  9.83200   12.31000  1.000 44.87071  ?  273 GLN   A CA   1 
ATOM   747  C  C    . GLN   A 1 121 ? 19.70200  11.03700  12.35300  1.000 49.27651  ?  273 GLN   A C    1 
ATOM   748  O  O    . GLN   A 1 121 ? 20.16500  12.17600  12.47600  1.000 50.36177  ?  273 GLN   A O    1 
ATOM   749  C  CB   . GLN   A 1 121 ? 20.97900  9.47600   10.86600  1.000 56.03604  ?  273 GLN   A CB   1 
ATOM   750  C  CG   . GLN   A 1 121 ? 22.26600  10.09400  10.35400  1.000 64.87486  ?  273 GLN   A CG   1 
ATOM   751  C  CD   . GLN   A 1 121 ? 22.56500  9.69600   8.92300   1.000 68.53144  ?  273 GLN   A CD   1 
ATOM   752  O  OE1  . GLN   A 1 121 ? 22.64900  8.51000   8.60200   1.000 64.56958  ?  273 GLN   A OE1  1 
ATOM   753  N  NE2  . GLN   A 1 121 ? 22.72800  10.68700  8.05400   1.000 65.01818  ?  273 GLN   A NE2  1 
ATOM   754  N  N    . SER   A 1 122 ? 18.39400  10.80600  12.25900  1.000 49.27518  ?  274 SER   A N    1 
ATOM   755  C  CA   . SER   A 1 122 ? 17.39800  11.86600  12.33700  1.000 46.99049  ?  274 SER   A CA   1 
ATOM   756  C  C    . SER   A 1 122 ? 16.91200  12.12700  13.75600  1.000 42.52087  ?  274 SER   A C    1 
ATOM   757  O  O    . SER   A 1 122 ? 16.21300  13.12200  13.97900  1.000 44.39985  ?  274 SER   A O    1 
ATOM   758  C  CB   . SER   A 1 122 ? 16.19900  11.52400  11.44900  1.000 48.23498  ?  274 SER   A CB   1 
ATOM   759  O  OG   . SER   A 1 122 ? 15.18800  10.86300  12.19200  1.000 51.94269  ?  274 SER   A OG   1 
ATOM   760  N  N    . PHE   A 1 123 ? 17.25400  11.26800  14.71200  1.000 39.32721  ?  275 PHE   A N    1 
ATOM   761  C  CA   . PHE   A 1 123 ? 16.76400  11.43900  16.07200  1.000 45.62749  ?  275 PHE   A CA   1 
ATOM   762  C  C    . PHE   A 1 123 ? 17.43700  12.63100  16.74000  1.000 51.64876  ?  275 PHE   A C    1 
ATOM   763  O  O    . PHE   A 1 123 ? 18.64900  12.83100  16.62300  1.000 56.11019  ?  275 PHE   A O    1 
ATOM   764  C  CB   . PHE   A 1 123 ? 17.00500  10.17600  16.89600  1.000 45.48309  ?  275 PHE   A CB   1 
ATOM   765  C  CG   . PHE   A 1 123 ? 16.47700  10.26200  18.30400  1.000 54.79606  ?  275 PHE   A CG   1 
ATOM   766  C  CD1  . PHE   A 1 123 ? 15.11400  10.19200  18.55400  1.000 56.68427  ?  275 PHE   A CD1  1 
ATOM   767  C  CD2  . PHE   A 1 123 ? 17.34300  10.41300  19.37500  1.000 50.43348  ?  275 PHE   A CD2  1 
ATOM   768  C  CE1  . PHE   A 1 123 ? 14.62500  10.26900  19.84800  1.000 56.11898  ?  275 PHE   A CE1  1 
ATOM   769  C  CE2  . PHE   A 1 123 ? 16.86200  10.49100  20.67100  1.000 47.98402  ?  275 PHE   A CE2  1 
ATOM   770  C  CZ   . PHE   A 1 123 ? 15.50200  10.41900  20.90800  1.000 56.65538  ?  275 PHE   A CZ   1 
ATOM   771  N  N    . THR   A 1 124 ? 16.64100  13.42100  17.45000  1.000 54.83009  ?  276 THR   A N    1 
ATOM   772  C  CA   . THR   A 1 124 ? 17.10800  14.63400  18.09900  1.000 66.17276  ?  276 THR   A CA   1 
ATOM   773  C  C    . THR   A 1 124 ? 16.88100  14.51200  19.60000  1.000 66.03038  ?  276 THR   A C    1 
ATOM   774  O  O    . THR   A 1 124 ? 15.89800  13.91600  20.04500  1.000 72.76632  ?  276 THR   A O    1 
ATOM   775  C  CB   . THR   A 1 124 ? 16.37500  15.86500  17.53600  1.000 72.85178  ?  276 THR   A CB   1 
ATOM   776  O  OG1  . THR   A 1 124 ? 16.73000  16.04200  16.15800  1.000 86.51141  ?  276 THR   A OG1  1 
ATOM   777  C  CG2  . THR   A 1 124 ? 16.74200  17.12000  18.29800  1.000 71.42811  ?  276 THR   A CG2  1 
ATOM   778  N  N    . MET   A 1 125 ? 17.81300  15.05400  20.38300  1.000 73.61056  ?  277 MET   A N    1 
ATOM   779  C  CA   . MET   A 1 125 ? 17.65300  15.09300  21.82900  1.000 78.47695  ?  277 MET   A CA   1 
ATOM   780  C  C    . MET   A 1 125 ? 17.08700  16.41500  22.33500  1.000 82.56982  ?  277 MET   A C    1 
ATOM   781  O  O    . MET   A 1 125 ? 16.73000  16.50400  23.51300  1.000 87.38903  ?  277 MET   A O    1 
ATOM   782  C  CB   . MET   A 1 125 ? 18.98800  14.79600  22.52400  1.000 77.31201  ?  277 MET   A CB   1 
ATOM   783  C  CG   . MET   A 1 125 ? 19.48700  13.37600  22.28700  1.000 75.73642  ?  277 MET   A CG   1 
ATOM   784  S  SD   . MET   A 1 125 ? 20.14300  12.57700  23.76400  1.000 86.19643  ?  277 MET   A SD   1 
ATOM   785  C  CE   . MET   A 1 125 ? 21.90100  12.77700  23.49000  1.000 77.83119  ?  277 MET   A CE   1 
ATOM   786  N  N    . ASP   A 1 126 ? 16.99300  17.43500  21.47700  1.000 95.14796  ?  278 ASP   A N    1 
ATOM   787  C  CA   . ASP   A 1 126 ? 16.28500  18.66000  21.83300  1.000 112.24007 ?  278 ASP   A CA   1 
ATOM   788  C  C    . ASP   A 1 126 ? 14.87400  18.36100  22.31600  1.000 108.89471 ?  278 ASP   A C    1 
ATOM   789  O  O    . ASP   A 1 126 ? 14.35100  19.04900  23.20100  1.000 117.59935 ?  278 ASP   A O    1 
ATOM   790  C  CB   . ASP   A 1 126 ? 16.19300  19.58700  20.62200  1.000 129.16372 ?  278 ASP   A CB   1 
ATOM   791  C  CG   . ASP   A 1 126 ? 17.53900  19.86100  19.97200  1.000 137.92559 ?  278 ASP   A CG   1 
ATOM   792  O  OD1  . ASP   A 1 126 ? 18.58700  19.57300  20.58400  1.000 140.00359 ?  278 ASP   A OD1  1 
ATOM   793  O  OD2  . ASP   A 1 126 ? 17.54000  20.33700  18.81700  1.000 141.12849 ?  278 ASP   A OD2  1 
ATOM   794  N  N    . ASP   A 1 127 ? 14.25300  17.34000  21.74400  1.000 97.47879  ?  279 ASP   A N    1 
ATOM   795  C  CA   . ASP   A 1 127 ? 12.84700  17.05600  21.98800  1.000 94.63046  ?  279 ASP   A CA   1 
ATOM   796  C  C    . ASP   A 1 127 ? 12.52300  15.57200  21.92700  1.000 90.16528  ?  279 ASP   A C    1 
ATOM   797  O  O    . ASP   A 1 127 ? 11.34900  15.21900  22.05900  1.000 91.98953  ?  279 ASP   A O    1 
ATOM   798  C  CB   . ASP   A 1 127 ? 11.99500  17.82500  20.96700  1.000 97.64601  ?  279 ASP   A CB   1 
ATOM   799  C  CG   . ASP   A 1 127 ? 12.57400  17.76000  19.56700  1.000 98.33761  ?  279 ASP   A CG   1 
ATOM   800  O  OD1  . ASP   A 1 127 ? 13.02800  16.66900  19.16100  1.000 95.28778  ?  279 ASP   A OD1  1 
ATOM   801  O  OD2  . ASP   A 1 127 ? 12.58700  18.79900  18.87600  1.000 100.83420 ?  279 ASP   A OD2  1 
ATOM   802  N  N    . MET   A 1 128 ? 13.51200  14.69700  21.74300  1.000 86.94807  ?  280 MET   A N    1 
ATOM   803  C  CA   . MET   A 1 128 ? 13.29700  13.26100  21.56200  1.000 82.25141  ?  280 MET   A CA   1 
ATOM   804  C  C    . MET   A 1 128 ? 12.27800  13.00100  20.45400  1.000 69.65085  ?  280 MET   A C    1 
ATOM   805  O  O    . MET   A 1 128 ? 11.29100  12.28000  20.62400  1.000 68.62783  ?  280 MET   A O    1 
ATOM   806  C  CB   . MET   A 1 128 ? 12.89000  12.59800  22.87900  1.000 90.10080  ?  280 MET   A CB   1 
ATOM   807  C  CG   . MET   A 1 128 ? 13.81100  12.97800  24.03100  1.000 97.82903  ?  280 MET   A CG   1 
ATOM   808  S  SD   . MET   A 1 128 ? 15.54400  12.86500  23.54300  1.000 111.38057 ?  280 MET   A SD   1 
ATOM   809  C  CE   . MET   A 1 128 ? 16.39200  12.95100  25.11900  1.000 112.38246 ?  280 MET   A CE   1 
ATOM   810  N  N    . SER   A 1 129 ? 12.52900  13.61700  19.30300  1.000 62.77955  ?  281 SER   A N    1 
ATOM   811  C  CA   . SER   A 1 129 ? 11.73200  13.41100  18.10500  1.000 62.08195  ?  281 SER   A CA   1 
ATOM   812  C  C    . SER   A 1 129 ? 12.65900  13.05800  16.94900  1.000 60.72077  ?  281 SER   A C    1 
ATOM   813  O  O    . SER   A 1 129 ? 13.88000  13.21500  17.03100  1.000 52.10991  ?  281 SER   A O    1 
ATOM   814  C  CB   . SER   A 1 129 ? 10.90400  14.65500  17.76600  1.000 64.07350  ?  281 SER   A CB   1 
ATOM   815  O  OG   . SER   A 1 129 ? 11.75300  15.73800  17.43300  1.000 70.80775  ?  281 SER   A OG   1 
ATOM   816  N  N    . TRP   A 1 130 ? 12.06900  12.57500  15.86100  1.000 57.02555  ?  282 TRP   A N    1 
ATOM   817  C  CA   . TRP   A 1 130 ? 12.80700  12.28400  14.63800  1.000 50.12590  ?  282 TRP   A CA   1 
ATOM   818  C  C    . TRP   A 1 130 ? 12.62300  13.46100  13.68600  1.000 61.45027  ?  282 TRP   A C    1 
ATOM   819  O  O    . TRP   A 1 130 ? 11.53500  13.66200  13.13700  1.000 60.80947  ?  282 TRP   A O    1 
ATOM   820  C  CB   . TRP   A 1 130 ? 12.34000  10.97100  14.01300  1.000 48.96002  ?  282 TRP   A CB   1 
ATOM   821  C  CG   . TRP   A 1 130 ? 12.81500  9.76300   14.76600  1.000 49.45912  ?  282 TRP   A CG   1 
ATOM   822  C  CD1  . TRP   A 1 130 ? 13.90900  8.99900   14.48400  1.000 48.73004  ?  282 TRP   A CD1  1 
ATOM   823  C  CD2  . TRP   A 1 130 ? 12.21400  9.18700   15.93200  1.000 49.36807  ?  282 TRP   A CD2  1 
ATOM   824  N  NE1  . TRP   A 1 130 ? 14.02500  7.98100   15.39800  1.000 50.77664  ?  282 TRP   A NE1  1 
ATOM   825  C  CE2  . TRP   A 1 130 ? 12.99600  8.07300   16.29800  1.000 52.11485  ?  282 TRP   A CE2  1 
ATOM   826  C  CE3  . TRP   A 1 130 ? 11.08900  9.50200   16.70000  1.000 50.50468  ?  282 TRP   A CE3  1 
ATOM   827  C  CZ2  . TRP   A 1 130 ? 12.69200  7.27700   17.39900  1.000 56.68556  ?  282 TRP   A CZ2  1 
ATOM   828  C  CZ3  . TRP   A 1 130 ? 10.78700  8.70700   17.79300  1.000 53.01538  ?  282 TRP   A CZ3  1 
ATOM   829  C  CH2  . TRP   A 1 130 ? 11.58500  7.60800   18.13100  1.000 53.98642  ?  282 TRP   A CH2  1 
ATOM   830  N  N    . ASP   A 1 131 ? 13.68500  14.24200  13.50000  1.000 61.72206  ?  283 ASP   A N    1 
ATOM   831  C  CA   . ASP   A 1 131 ? 13.62400  15.47700  12.72100  1.000 61.66730  ?  283 ASP   A CA   1 
ATOM   832  C  C    . ASP   A 1 131 ? 14.01200  15.16600  11.28000  1.000 60.78687  ?  283 ASP   A C    1 
ATOM   833  O  O    . ASP   A 1 131 ? 15.19100  14.99500  10.96500  1.000 66.24415  ?  283 ASP   A O    1 
ATOM   834  C  CB   . ASP   A 1 131 ? 14.53800  16.53300  13.33200  1.000 70.60394  ?  283 ASP   A CB   1 
ATOM   835  C  CG   . ASP   A 1 131 ? 14.43300  17.87300  12.63200  1.000 78.66977  ?  283 ASP   A CG   1 
ATOM   836  O  OD1  . ASP   A 1 131 ? 13.43900  18.08800  11.90800  1.000 77.19512  ?  283 ASP   A OD1  1 
ATOM   837  O  OD2  . ASP   A 1 131 ? 15.33500  18.71800  12.82000  1.000 81.15231  ?  283 ASP   A OD2  1 
ATOM   838  N  N    . CYS   A 1 132 ? 13.01800  15.10200  10.39600  1.000 58.39674  ?  284 CYS   A N    1 
ATOM   839  C  CA   . CYS   A 1 132 ? 13.27800  14.75500  9.00600   1.000 62.85316  ?  284 CYS   A CA   1 
ATOM   840  C  C    . CYS   A 1 132 ? 12.97700  15.91800  8.06800   1.000 66.59400  ?  284 CYS   A C    1 
ATOM   841  O  O    . CYS   A 1 132 ? 12.30200  15.73800  7.05000   1.000 68.90184  ?  284 CYS   A O    1 
ATOM   842  C  CB   . CYS   A 1 132 ? 12.45900  13.52900  8.59500   1.000 52.68550  ?  284 CYS   A CB   1 
ATOM   843  S  SG   . CYS   A 1 132 ? 12.89800  12.00000  9.45700   1.000 50.22462  ?  284 CYS   A SG   1 
ATOM   844  N  N    . GLY   A 1 133 ? 13.45700  17.11300  8.39900   1.000 69.78912  ?  285 GLY   A N    1 
ATOM   845  C  CA   . GLY   A 1 133 ? 13.37500  18.22600  7.47300   1.000 76.46113  ?  285 GLY   A CA   1 
ATOM   846  C  C    . GLY   A 1 133 ? 12.37800  19.31300  7.82000   1.000 73.32839  ?  285 GLY   A C    1 
ATOM   847  O  O    . GLY   A 1 133 ? 12.73100  20.49600  7.82300   1.000 83.24367  ?  285 GLY   A O    1 
ATOM   848  N  N    . SER   A 1 134 ? 11.13300  18.93800  8.11300   1.000 71.65874  ?  286 SER   A N    1 
ATOM   849  C  CA   . SER   A 1 134 ? 10.07000  19.91400  8.30700   1.000 81.48012  ?  286 SER   A CA   1 
ATOM   850  C  C    . SER   A 1 134 ? 9.17700   19.49100  9.46500   1.000 79.23736  ?  286 SER   A C    1 
ATOM   851  O  O    . SER   A 1 134 ? 9.33300   18.41000  10.04100  1.000 73.53185  ?  286 SER   A O    1 
ATOM   852  C  CB   . SER   A 1 134 ? 9.23700   20.08700  7.03100   1.000 87.43406  ?  286 SER   A CB   1 
ATOM   853  O  OG   . SER   A 1 134 ? 10.05600  20.04500  5.87500   1.000 94.39899  ?  286 SER   A OG   1 
ATOM   854  N  N    . GLN   A 1 135 ? 8.23200   20.37200  9.80600   1.000 83.10716  ?  287 GLN   A N    1 
ATOM   855  C  CA   . GLN   A 1 135 ? 7.26100   20.05800  10.85200  1.000 90.25275  ?  287 GLN   A CA   1 
ATOM   856  C  C    . GLN   A 1 135 ? 6.36500   18.89800  10.44200  1.000 91.78872  ?  287 GLN   A C    1 
ATOM   857  O  O    . GLN   A 1 135 ? 5.97200   18.07900  11.28200  1.000 87.21316  ?  287 GLN   A O    1 
ATOM   858  C  CB   . GLN   A 1 135 ? 6.41700   21.29300  11.17500  1.000 97.06702  ?  287 GLN   A CB   1 
ATOM   859  C  CG   . GLN   A 1 135 ? 5.96700   21.38800  12.62400  1.000 101.14068 ?  287 GLN   A CG   1 
ATOM   860  C  CD   . GLN   A 1 135 ? 7.12600   21.54800  13.58100  1.000 102.77835 ?  287 GLN   A CD   1 
ATOM   861  O  OE1  . GLN   A 1 135 ? 7.99300   22.40000  13.38400  1.000 107.03995 ?  287 GLN   A OE1  1 
ATOM   862  N  NE2  . GLN   A 1 135 ? 7.14900   20.73200  14.62800  1.000 98.30511  ?  287 GLN   A NE2  1 
ATOM   863  N  N    . ASP   A 1 136 ? 6.02200   18.82300  9.15300   1.000 95.57868  ?  288 ASP   A N    1 
ATOM   864  C  CA   . ASP   A 1 136 ? 5.25100   17.69200  8.64900   1.000 97.71892  ?  288 ASP   A CA   1 
ATOM   865  C  C    . ASP   A 1 136 ? 5.95700   16.37400  8.93500   1.000 89.62925  ?  288 ASP   A C    1 
ATOM   866  O  O    . ASP   A 1 136 ? 5.31700   15.37600  9.28900   1.000 89.55138  ?  288 ASP   A O    1 
ATOM   867  C  CB   . ASP   A 1 136 ? 5.01800   17.84500  7.14700   1.000 100.57290 ?  288 ASP   A CB   1 
ATOM   868  C  CG   . ASP   A 1 136 ? 3.77800   18.65200  6.82600   1.000 109.20674 ?  288 ASP   A CG   1 
ATOM   869  O  OD1  . ASP   A 1 136 ? 2.88000   18.73200  7.69000   1.000 111.43156 ?  288 ASP   A OD1  1 
ATOM   870  O  OD2  . ASP   A 1 136 ? 3.69700   19.19600  5.70500   1.000 110.65351 ?  288 ASP   A OD2  1 
ATOM   871  N  N    . TYR   A 1 137 ? 7.27700   16.35300  8.78700   1.000 77.08393  ?  289 TYR   A N    1 
ATOM   872  C  CA   . TYR   A 1 137 ? 8.07800   15.14800  8.95200   1.000 73.15214  ?  289 TYR   A CA   1 
ATOM   873  C  C    . TYR   A 1 137 ? 8.89700   15.22200  10.23600  1.000 70.00086  ?  289 TYR   A C    1 
ATOM   874  O  O    . TYR   A 1 137 ? 10.07500  14.86500  10.27700  1.000 59.50304  ?  289 TYR   A O    1 
ATOM   875  C  CB   . TYR   A 1 137 ? 8.94400   14.93000  7.71600   1.000 68.45402  ?  289 TYR   A CB   1 
ATOM   876  C  CG   . TYR   A 1 137 ? 8.11600   15.07900  6.45900   1.000 63.71551  ?  289 TYR   A CG   1 
ATOM   877  C  CD1  . TYR   A 1 137 ? 8.54300   15.86700  5.39900   1.000 66.46416  ?  289 TYR   A CD1  1 
ATOM   878  C  CD2  . TYR   A 1 137 ? 6.88100   14.44900  6.35000   1.000 69.77829  ?  289 TYR   A CD2  1 
ATOM   879  C  CE1  . TYR   A 1 137 ? 7.76700   16.00900  4.25800   1.000 71.98236  ?  289 TYR   A CE1  1 
ATOM   880  C  CE2  . TYR   A 1 137 ? 6.10100   14.58600  5.22000   1.000 71.75388  ?  289 TYR   A CE2  1 
ATOM   881  C  CZ   . TYR   A 1 137 ? 6.54700   15.36500  4.17700   1.000 74.84890  ?  289 TYR   A CZ   1 
ATOM   882  O  OH   . TYR   A 1 137 ? 5.76600   15.49500  3.05100   1.000 77.95074  ?  289 TYR   A OH   1 
ATOM   883  N  N    . LYS   A 1 138 ? 8.25100   15.70300  11.29400  1.000 73.92334  ?  290 LYS   A N    1 
ATOM   884  C  CA   . LYS   A 1 138 ? 8.78300   15.73100  12.65100  1.000 77.88288  ?  290 LYS   A CA   1 
ATOM   885  C  C    . LYS   A 1 138 ? 7.96300   14.73800  13.46700  1.000 76.42876  ?  290 LYS   A C    1 
ATOM   886  O  O    . LYS   A 1 138 ? 6.78200   14.98000  13.73800  1.000 79.97697  ?  290 LYS   A O    1 
ATOM   887  C  CB   . LYS   A 1 138 ? 8.69100   17.13900  13.23300  1.000 79.63588  ?  290 LYS   A CB   1 
ATOM   888  C  CG   . LYS   A 1 138 ? 9.07700   17.24100  14.69400  1.000 88.10671  ?  290 LYS   A CG   1 
ATOM   889  C  CD   . LYS   A 1 138 ? 10.57500  17.14400  14.88100  1.000 86.90384  ?  290 LYS   A CD   1 
ATOM   890  C  CE   . LYS   A 1 138 ? 11.13700  18.47200  15.35400  1.000 85.86928  ?  290 LYS   A CE   1 
ATOM   891  N  NZ   . LYS   A 1 138 ? 12.50700  18.71500  14.84300  1.000 85.53790  ?  290 LYS   A NZ   1 
ATOM   892  N  N    . TYR   A 1 139 ? 8.57800   13.62300  13.85200  1.000 63.74958  ?  291 TYR   A N    1 
ATOM   893  C  CA   . TYR   A 1 139 ? 7.86200   12.50800  14.46100  1.000 57.16967  ?  291 TYR   A CA   1 
ATOM   894  C  C    . TYR   A 1 139 ? 8.21800   12.39300  15.93600  1.000 61.29742  ?  291 TYR   A C    1 
ATOM   895  O  O    . TYR   A 1 139 ? 9.38900   12.21300  16.28400  1.000 63.41007  ?  291 TYR   A O    1 
ATOM   896  C  CB   . TYR   A 1 139 ? 8.16900   11.20200  13.73200  1.000 50.52368  ?  291 TYR   A CB   1 
ATOM   897  C  CG   . TYR   A 1 139 ? 8.01200   11.30700  12.23700  1.000 54.17582  ?  291 TYR   A CG   1 
ATOM   898  C  CD1  . TYR   A 1 139 ? 9.12100   11.35600  11.40400  1.000 46.02895  ?  291 TYR   A CD1  1 
ATOM   899  C  CD2  . TYR   A 1 139 ? 6.75200   11.37400  11.65700  1.000 60.08020  ?  291 TYR   A CD2  1 
ATOM   900  C  CE1  . TYR   A 1 139 ? 8.98100   11.45800  10.03400  1.000 53.69760  ?  291 TYR   A CE1  1 
ATOM   901  C  CE2  . TYR   A 1 139 ? 6.60000   11.47800  10.28900  1.000 50.95750  ?  291 TYR   A CE2  1 
ATOM   902  C  CZ   . TYR   A 1 139 ? 7.71800   11.52000  9.48200   1.000 53.36364  ?  291 TYR   A CZ   1 
ATOM   903  O  OH   . TYR   A 1 139 ? 7.57700   11.62200  8.11900   1.000 55.44274  ?  291 TYR   A OH   1 
ATOM   904  N  N    . ASP   A 1 140 ? 7.20400   12.48300  16.79200  1.000 71.46857  ?  292 ASP   A N    1 
ATOM   905  C  CA   . ASP   A 1 140 ? 7.33000   12.29800  18.22700  1.000 78.40454  ?  292 ASP   A CA   1 
ATOM   906  C  C    . ASP   A 1 140 ? 6.71200   10.95700  18.61800  1.000 79.34908  ?  292 ASP   A C    1 
ATOM   907  O  O    . ASP   A 1 140 ? 6.33200   10.14900  17.76200  1.000 70.63600  ?  292 ASP   A O    1 
ATOM   908  C  CB   . ASP   A 1 140 ? 6.67900   13.47000  18.96900  1.000 82.97333  ?  292 ASP   A CB   1 
ATOM   909  C  CG   . ASP   A 1 140 ? 5.17600   13.53400  18.75800  1.000 91.69858  ?  292 ASP   A CG   1 
ATOM   910  O  OD1  . ASP   A 1 140 ? 4.46700   14.01200  19.66900  1.000 97.11885  ?  292 ASP   A OD1  1 
ATOM   911  O  OD2  . ASP   A 1 140 ? 4.70100   13.11100  17.68200  1.000 92.53403  ?  292 ASP   A OD2  1 
ATOM   912  N  N    . VAL   A 1 141 ? 6.60400   10.72000  19.92800  1.000 81.69371  ?  293 VAL   A N    1 
ATOM   913  C  CA   . VAL   A 1 141 ? 6.04100   9.46200   20.40200  1.000 77.25739  ?  293 VAL   A CA   1 
ATOM   914  C  C    . VAL   A 1 141 ? 4.53500   9.39800   20.18300  1.000 71.38082  ?  293 VAL   A C    1 
ATOM   915  O  O    . VAL   A 1 141 ? 3.95700   8.30500   20.20000  1.000 68.08270  ?  293 VAL   A O    1 
ATOM   916  C  CB   . VAL   A 1 141 ? 6.38800   9.24300   21.88600  1.000 79.51435  ?  293 VAL   A CB   1 
ATOM   917  C  CG1  . VAL   A 1 141 ? 7.84300   9.60500   22.14600  1.000 75.93842  ?  293 VAL   A CG1  1 
ATOM   918  C  CG2  . VAL   A 1 141 ? 5.46100   10.05300  22.78000  1.000 81.75974  ?  293 VAL   A CG2  1 
ATOM   919  N  N    . THR   A 1 142 ? 3.87900   10.54400  19.97700  1.000 68.26633  ?  294 THR   A N    1 
ATOM   920  C  CA   . THR   A 1 142 ? 2.45100   10.53400  19.67500  1.000 72.58773  ?  294 THR   A CA   1 
ATOM   921  C  C    . THR   A 1 142 ? 2.17200   9.88700   18.32800  1.000 71.07410  ?  294 THR   A C    1 
ATOM   922  O  O    . THR   A 1 142 ? 1.12300   9.25900   18.14600  1.000 74.21379  ?  294 THR   A O    1 
ATOM   923  C  CB   . THR   A 1 142 ? 1.89400   11.95800  19.69000  1.000 80.19160  ?  294 THR   A CB   1 
ATOM   924  O  OG1  . THR   A 1 142 ? 2.45200   12.68200  20.79400  1.000 85.77893  ?  294 THR   A OG1  1 
ATOM   925  C  CG2  . THR   A 1 142 ? 0.37600   11.93900  19.81100  1.000 84.20902  ?  294 THR   A CG2  1 
ATOM   926  N  N    . ASP   A 1 143 ? 3.09700   10.02400  17.37800  1.000 75.18770  ?  295 ASP   A N    1 
ATOM   927  C  CA   . ASP   A 1 143 ? 2.88700   9.44200   16.05900  1.000 74.97825  ?  295 ASP   A CA   1 
ATOM   928  C  C    . ASP   A 1 143 ? 3.03700   7.92600   16.09200  1.000 67.39769  ?  295 ASP   A C    1 
ATOM   929  O  O    . ASP   A 1 143 ? 2.31100   7.21100   15.39100  1.000 66.22978  ?  295 ASP   A O    1 
ATOM   930  C  CB   . ASP   A 1 143 ? 3.85500   10.07100  15.05900  1.000 75.31666  ?  295 ASP   A CB   1 
ATOM   931  C  CG   . ASP   A 1 143 ? 3.73600   11.58500  15.01300  1.000 77.74713  ?  295 ASP   A CG   1 
ATOM   932  O  OD1  . ASP   A 1 143 ? 4.77500   12.26300  14.88800  1.000 72.45861  ?  295 ASP   A OD1  1 
ATOM   933  O  OD2  . ASP   A 1 143 ? 2.60100   12.10000  15.10600  1.000 80.69812  ?  295 ASP   A OD2  1 
ATOM   934  N  N    . VAL   A 1 144 ? 3.96100   7.41100   16.90900  1.000 59.59359  ?  296 VAL   A N    1 
ATOM   935  C  CA   . VAL   A 1 144 ? 4.11800   5.96100   17.00500  1.000 60.96761  ?  296 VAL   A CA   1 
ATOM   936  C  C    . VAL   A 1 144 ? 2.90800   5.32700   17.68900  1.000 68.26752  ?  296 VAL   A C    1 
ATOM   937  O  O    . VAL   A 1 144 ? 2.57000   4.16800   17.41400  1.000 68.81389  ?  296 VAL   A O    1 
ATOM   938  C  CB   . VAL   A 1 144 ? 5.43200   5.60800   17.72800  1.000 56.95328  ?  296 VAL   A CB   1 
ATOM   939  C  CG1  . VAL   A 1 144 ? 5.75200   4.13800   17.55000  1.000 51.80340  ?  296 VAL   A CG1  1 
ATOM   940  C  CG2  . VAL   A 1 144 ? 6.58300   6.45700   17.19700  1.000 55.16774  ?  296 VAL   A CG2  1 
ATOM   941  N  N    . SER   A 1 145 ? 2.23500   6.06300   18.58100  1.000 68.24113  ?  297 SER   A N    1 
ATOM   942  C  CA   . SER   A 1 145 ? 1.00500   5.55500   19.18500  1.000 72.84151  ?  297 SER   A CA   1 
ATOM   943  C  C    . SER   A 1 145 ? -0.17000  5.66200   18.21900  1.000 75.94099  ?  297 SER   A C    1 
ATOM   944  O  O    . SER   A 1 145 ? -1.02700  4.77600   18.18100  1.000 73.40869  ?  297 SER   A O    1 
ATOM   945  C  CB   . SER   A 1 145 ? 0.70600   6.30600   20.49300  1.000 75.36686  ?  297 SER   A CB   1 
ATOM   946  O  OG   . SER   A 1 145 ? 0.31600   7.65500   20.24400  1.000 83.73832  ?  297 SER   A OG   1 
ATOM   947  N  N    . LYS   A 1 146 ? -0.21100  6.71600   17.41700  1.000 75.89919  ?  298 LYS   A N    1 
ATOM   948  C  CA   . LYS   A 1 146 ? -1.19000  6.82500   16.34700  1.000 77.39456  ?  298 LYS   A CA   1 
ATOM   949  C  C    . LYS   A 1 146 ? -0.85100  5.95500   15.14300  1.000 72.80599  ?  298 LYS   A C    1 
ATOM   950  O  O    . LYS   A 1 146 ? -1.54600  6.02000   14.12000  1.000 80.46303  ?  298 LYS   A O    1 
ATOM   951  C  CB   . LYS   A 1 146 ? -1.35700  8.28500   15.91800  1.000 80.59211  ?  298 LYS   A CB   1 
ATOM   952  C  CG   . LYS   A 1 146 ? -2.40900  8.99800   16.73400  1.000 95.11378  ?  298 LYS   A CG   1 
ATOM   953  C  CD   . LYS   A 1 146 ? -2.01400  10.42000  17.03600  1.000 101.58956 ?  298 LYS   A CD   1 
ATOM   954  C  CE   . LYS   A 1 146 ? -1.83700  11.22800  15.77400  1.000 103.27890 ?  298 LYS   A CE   1 
ATOM   955  N  NZ   . LYS   A 1 146 ? -1.83900  12.65700  16.15400  1.000 108.08043 ?  298 LYS   A NZ   1 
ATOM   956  N  N    . ALA   A 1 147 ? 0.20600   5.16200   15.23700  1.000 61.28035  ?  299 ALA   A N    1 
ATOM   957  C  CA   . ALA   A 1 147 ? 0.44300   4.06000   14.32100  1.000 61.41633  ?  299 ALA   A CA   1 
ATOM   958  C  C    . ALA   A 1 147 ? -0.00900  2.72700   14.89900  1.000 60.35717  ?  299 ALA   A C    1 
ATOM   959  O  O    . ALA   A 1 147 ? 0.07800   1.70800   14.20800  1.000 65.71227  ?  299 ALA   A O    1 
ATOM   960  C  CB   . ALA   A 1 147 ? 1.92700   3.98800   13.94600  1.000 62.32949  ?  299 ALA   A CB   1 
ATOM   961  N  N    . GLY   A 1 148 ? -0.48400  2.70900   16.14500  1.000 57.70031  ?  300 GLY   A N    1 
ATOM   962  C  CA   . GLY   A 1 148 ? -1.02300  1.51100   16.76000  1.000 60.60697  ?  300 GLY   A CA   1 
ATOM   963  C  C    . GLY   A 1 148 ? -0.18200  0.90900   17.86400  1.000 59.76054  ?  300 GLY   A C    1 
ATOM   964  O  O    . GLY   A 1 148 ? -0.60900  -0.08100  18.47200  1.000 65.67445  ?  300 GLY   A O    1 
ATOM   965  N  N    . HIS   A 1 149 ? 0.98500   1.46900   18.16000  1.000 60.36135  ?  301 HIS   A N    1 
ATOM   966  C  CA   . HIS   A 1 149 ? 1.90700   0.87300   19.11500  1.000 61.46795  ?  301 HIS   A CA   1 
ATOM   967  C  C    . HIS   A 1 149 ? 1.72300   1.46900   20.50400  1.000 67.82916  ?  301 HIS   A C    1 
ATOM   968  O  O    . HIS   A 1 149 ? 1.47700   2.66900   20.65400  1.000 65.34756  ?  301 HIS   A O    1 
ATOM   969  C  CB   . HIS   A 1 149 ? 3.35200   1.05300   18.65200  1.000 58.53033  ?  301 HIS   A CB   1 
ATOM   970  C  CG   . HIS   A 1 149 ? 3.70900   0.20300   17.47300  1.000 55.56668  ?  301 HIS   A CG   1 
ATOM   971  N  ND1  . HIS   A 1 149 ? 3.66000   -1.17400  17.50900  1.000 53.19000  ?  301 HIS   A ND1  1 
ATOM   972  C  CD2  . HIS   A 1 149 ? 4.11600   0.53200   16.22400  1.000 54.33791  ?  301 HIS   A CD2  1 
ATOM   973  C  CE1  . HIS   A 1 149 ? 4.02200   -1.65700  16.33400  1.000 52.23745  ?  301 HIS   A CE1  1 
ATOM   974  N  NE2  . HIS   A 1 149 ? 4.30500   -0.64300  15.53700  1.000 51.99707  ?  301 HIS   A NE2  1 
ATOM   975  N  N    . THR   A 1 150 ? 1.84700   0.61400   21.51600  1.000 76.62900  ?  302 THR   A N    1 
ATOM   976  C  CA   . THR   A 1 150 ? 1.74200   1.03000   22.90700  1.000 81.76429  ?  302 THR   A CA   1 
ATOM   977  C  C    . THR   A 1 150 ? 3.08300   1.59900   23.36000  1.000 85.95398  ?  302 THR   A C    1 
ATOM   978  O  O    . THR   A 1 150 ? 3.98300   1.85400   22.55700  1.000 90.29350  ?  302 THR   A O    1 
ATOM   979  C  CB   . THR   A 1 150 ? 1.31700   -0.14300  23.78500  1.000 82.14592  ?  302 THR   A CB   1 
ATOM   980  O  OG1  . THR   A 1 150 ? 2.47700   -0.88400  24.17900  1.000 76.58878  ?  302 THR   A OG1  1 
ATOM   981  C  CG2  . THR   A 1 150 ? 0.40400   -1.06900  23.01700  1.000 79.38217  ?  302 THR   A CG2  1 
ATOM   982  N  N    . LEU   A 1 151 ? 3.23800   1.78900   24.66800  1.000 84.98707  ?  303 LEU   A N    1 
ATOM   983  C  CA   . LEU   A 1 151 ? 4.50700   2.21800   25.23200  1.000 77.09788  ?  303 LEU   A CA   1 
ATOM   984  C  C    . LEU   A 1 151 ? 5.35900   1.05000   25.71000  1.000 71.84815  ?  303 LEU   A C    1 
ATOM   985  O  O    . LEU   A 1 151 ? 6.50300   1.26700   26.12600  1.000 70.33381  ?  303 LEU   A O    1 
ATOM   986  C  CB   . LEU   A 1 151 ? 4.26300   3.20700   26.37600  1.000 79.34145  ?  303 LEU   A CB   1 
ATOM   987  C  CG   . LEU   A 1 151 ? 3.56000   4.47000   25.86600  1.000 80.55155  ?  303 LEU   A CG   1 
ATOM   988  C  CD1  . LEU   A 1 151 ? 2.07700   4.45900   26.21600  1.000 86.75889  ?  303 LEU   A CD1  1 
ATOM   989  C  CD2  . LEU   A 1 151 ? 4.22800   5.73300   26.37700  1.000 74.70969  ?  303 LEU   A CD2  1 
ATOM   990  N  N    . GLU   A 1 152 ? 4.82900   -0.17700  25.65500  1.000 74.37139  ?  304 GLU   A N    1 
ATOM   991  C  CA   . GLU   A 1 152 ? 5.66400   -1.36500  25.79300  1.000 72.86176  ?  304 GLU   A CA   1 
ATOM   992  C  C    . GLU   A 1 152 ? 6.80500   -1.35400  24.78600  1.000 67.41679  ?  304 GLU   A C    1 
ATOM   993  O  O    . GLU   A 1 152 ? 7.85500   -1.96100  25.02300  1.000 60.17186  ?  304 GLU   A O    1 
ATOM   994  C  CB   . GLU   A 1 152 ? 4.81800   -2.62700  25.60200  1.000 79.97324  ?  304 GLU   A CB   1 
ATOM   995  C  CG   . GLU   A 1 152 ? 4.20200   -3.19800  26.86900  1.000 92.61676  ?  304 GLU   A CG   1 
ATOM   996  C  CD   . GLU   A 1 152 ? 4.10100   -4.71300  26.82600  1.000 100.68273 ?  304 GLU   A CD   1 
ATOM   997  O  OE1  . GLU   A 1 152 ? 2.99200   -5.23000  26.57200  1.000 102.79359 ?  304 GLU   A OE1  1 
ATOM   998  O  OE2  . GLU   A 1 152 ? 5.13000   -5.38900  27.04000  1.000 101.61961 ?  304 GLU   A OE2  1 
ATOM   999  N  N    . LEU   A 1 153 ? 6.61100   -0.68000  23.65400  1.000 58.70399  ?  305 LEU   A N    1 
ATOM   1000 C  CA   . LEU   A 1 153 ? 7.62500   -0.52400  22.62000  1.000 57.54599  ?  305 LEU   A CA   1 
ATOM   1001 C  C    . LEU   A 1 153 ? 8.19300   0.88300   22.54400  1.000 53.58796  ?  305 LEU   A C    1 
ATOM   1002 O  O    . LEU   A 1 153 ? 9.38900   1.04600   22.29600  1.000 52.36811  ?  305 LEU   A O    1 
ATOM   1003 C  CB   . LEU   A 1 153 ? 7.04100   -0.90600  21.25500  1.000 48.33001  ?  305 LEU   A CB   1 
ATOM   1004 C  CG   . LEU   A 1 153 ? 7.89000   -0.58900  20.02400  1.000 42.06888  ?  305 LEU   A CG   1 
ATOM   1005 C  CD1  . LEU   A 1 153 ? 9.03200   -1.58300  19.88900  1.000 36.23401  ?  305 LEU   A CD1  1 
ATOM   1006 C  CD2  . LEU   A 1 153 ? 7.02800   -0.57700  18.77200  1.000 45.66238  ?  305 LEU   A CD2  1 
ATOM   1007 N  N    . ILE   A 1 154 ? 7.36300   1.90600   22.76400  1.000 55.02977  ?  306 ILE   A N    1 
ATOM   1008 C  CA   . ILE   A 1 154 ? 7.81800   3.28500   22.61300  1.000 58.43407  ?  306 ILE   A CA   1 
ATOM   1009 C  C    . ILE   A 1 154 ? 8.84300   3.64100   23.68600  1.000 62.23241  ?  306 ILE   A C    1 
ATOM   1010 O  O    . ILE   A 1 154 ? 9.82100   4.34800   23.41300  1.000 57.86407  ?  306 ILE   A O    1 
ATOM   1011 C  CB   . ILE   A 1 154 ? 6.61400   4.24600   22.63000  1.000 60.60320  ?  306 ILE   A CB   1 
ATOM   1012 C  CG1  . ILE   A 1 154 ? 5.77300   4.07600   21.36200  1.000 57.99558  ?  306 ILE   A CG1  1 
ATOM   1013 C  CG2  . ILE   A 1 154 ? 7.07400   5.69000   22.75600  1.000 60.56587  ?  306 ILE   A CG2  1 
ATOM   1014 C  CD1  . ILE   A 1 154 ? 4.70400   5.13500   21.20100  1.000 64.07037  ?  306 ILE   A CD1  1 
ATOM   1015 N  N    . GLU   A 1 155 ? 8.64500   3.15700   24.92100  1.000 67.15676  ?  307 GLU   A N    1 
ATOM   1016 C  CA   . GLU   A 1 155 ? 9.60400   3.47800   25.97900  1.000 68.63808  ?  307 GLU   A CA   1 
ATOM   1017 C  C    . GLU   A 1 155 ? 10.97800  2.87600   25.70800  1.000 62.94800  ?  307 GLU   A C    1 
ATOM   1018 O  O    . GLU   A 1 155 ? 11.97000  3.62500   25.74200  1.000 62.55130  ?  307 GLU   A O    1 
ATOM   1019 C  CB   . GLU   A 1 155 ? 9.05400   3.05500   27.34500  1.000 76.03881  ?  307 GLU   A CB   1 
ATOM   1020 C  CG   . GLU   A 1 155 ? 9.97400   3.41500   28.50800  1.000 82.45812  ?  307 GLU   A CG   1 
ATOM   1021 C  CD   . GLU   A 1 155 ? 10.16900  2.26900   29.48400  1.000 91.03176  ?  307 GLU   A CD   1 
ATOM   1022 O  OE1  . GLU   A 1 155 ? 10.92400  2.44300   30.46400  1.000 95.48495  ?  307 GLU   A OE1  1 
ATOM   1023 O  OE2  . GLU   A 1 155 ? 9.56700   1.19500   29.27200  1.000 93.56447  ?  307 GLU   A OE2  1 
ATOM   1024 N  N    . PRO   A 1 156 ? 11.12600  1.57300   25.43500  1.000 62.21476  ?  308 PRO   A N    1 
ATOM   1025 C  CA   . PRO   A 1 156 ? 12.46800  1.07600   25.08900  1.000 59.31411  ?  308 PRO   A CA   1 
ATOM   1026 C  C    . PRO   A 1 156 ? 13.00900  1.67600   23.80500  1.000 52.93843  ?  308 PRO   A C    1 
ATOM   1027 O  O    . PRO   A 1 156 ? 14.23300  1.77900   23.65000  1.000 52.49324  ?  308 PRO   A O    1 
ATOM   1028 C  CB   . PRO   A 1 156 ? 12.26900  -0.44200  24.96700  1.000 62.61529  ?  308 PRO   A CB   1 
ATOM   1029 C  CG   . PRO   A 1 156 ? 10.82100  -0.62500  24.73300  1.000 63.17355  ?  308 PRO   A CG   1 
ATOM   1030 C  CD   . PRO   A 1 156 ? 10.14000  0.47600   25.47800  1.000 56.34440  ?  308 PRO   A CD   1 
ATOM   1031 N  N    . LEU   A 1 157 ? 12.13500  2.08900   22.88400  1.000 52.51937  ?  309 LEU   A N    1 
ATOM   1032 C  CA   . LEU   A 1 157 ? 12.60000  2.68400   21.63500  1.000 47.29540  ?  309 LEU   A CA   1 
ATOM   1033 C  C    . LEU   A 1 157 ? 13.28700  4.02200   21.88300  1.000 46.15466  ?  309 LEU   A C    1 
ATOM   1034 O  O    . LEU   A 1 157 ? 14.37800  4.27500   21.36000  1.000 44.12715  ?  309 LEU   A O    1 
ATOM   1035 C  CB   . LEU   A 1 157 ? 11.43600  2.85500   20.65900  1.000 48.33712  ?  309 LEU   A CB   1 
ATOM   1036 C  CG   . LEU   A 1 157 ? 11.84900  3.48700   19.32900  1.000 42.68320  ?  309 LEU   A CG   1 
ATOM   1037 C  CD1  . LEU   A 1 157 ? 12.92100  2.63700   18.66400  1.000 35.92630  ?  309 LEU   A CD1  1 
ATOM   1038 C  CD2  . LEU   A 1 157 ? 10.65500  3.68100   18.40000  1.000 41.87426  ?  309 LEU   A CD2  1 
ATOM   1039 N  N    . ILE   A 1 158 ? 12.66000  4.89500   22.67400  1.000 46.05922  ?  310 ILE   A N    1 
ATOM   1040 C  CA   . ILE   A 1 158 ? 13.26000  6.19600   22.95700  1.000 53.54537  ?  310 ILE   A CA   1 
ATOM   1041 C  C    . ILE   A 1 158 ? 14.54500  6.02800   23.75600  1.000 53.74682  ?  310 ILE   A C    1 
ATOM   1042 O  O    . ILE   A 1 158 ? 15.53900  6.72400   23.51200  1.000 60.43343  ?  310 ILE   A O    1 
ATOM   1043 C  CB   . ILE   A 1 158 ? 12.25400  7.10400   23.68600  1.000 56.09781  ?  310 ILE   A CB   1 
ATOM   1044 C  CG1  . ILE   A 1 158 ? 11.03900  7.37200   22.79900  1.000 57.36543  ?  310 ILE   A CG1  1 
ATOM   1045 C  CG2  . ILE   A 1 158 ? 12.91200  8.41500   24.09100  1.000 56.04681  ?  310 ILE   A CG2  1 
ATOM   1046 C  CD1  . ILE   A 1 158 ? 11.35500  8.20400   21.58000  1.000 58.28062  ?  310 ILE   A CD1  1 
ATOM   1047 N  N    . LYS   A 1 159 ? 14.55000  5.10200   24.71900  1.000 48.19059  ?  311 LYS   A N    1 
ATOM   1048 C  CA   . LYS   A 1 159 ? 15.76300  4.84200   25.48700  1.000 52.95933  ?  311 LYS   A CA   1 
ATOM   1049 C  C    . LYS   A 1 159 ? 16.88300  4.32600   24.59400  1.000 50.65253  ?  311 LYS   A C    1 
ATOM   1050 O  O    . LYS   A 1 159 ? 18.04600  4.71000   24.76200  1.000 43.08825  ?  311 LYS   A O    1 
ATOM   1051 C  CB   . LYS   A 1 159 ? 15.47600  3.84500   26.60900  1.000 60.55091  ?  311 LYS   A CB   1 
ATOM   1052 C  CG   . LYS   A 1 159 ? 14.74500  4.44000   27.79900  1.000 68.28668  ?  311 LYS   A CG   1 
ATOM   1053 C  CD   . LYS   A 1 159 ? 14.56100  3.41600   28.91400  1.000 79.01690  ?  311 LYS   A CD   1 
ATOM   1054 C  CE   . LYS   A 1 159 ? 15.70400  2.40800   28.95400  1.000 79.50804  ?  311 LYS   A CE   1 
ATOM   1055 N  NZ   . LYS   A 1 159 ? 16.07600  2.03200   30.34700  1.000 82.91862  ?  311 LYS   A NZ   1 
ATOM   1056 N  N    . PHE   A 1 160 ? 16.55300  3.45100   23.64200  1.000 43.96407  ?  312 PHE   A N    1 
ATOM   1057 C  CA   . PHE   A 1 160 ? 17.55600  2.99000   22.68800  1.000 39.94478  ?  312 PHE   A CA   1 
ATOM   1058 C  C    . PHE   A 1 160 ? 18.09500  4.15200   21.86600  1.000 42.31730  ?  312 PHE   A C    1 
ATOM   1059 O  O    . PHE   A 1 160 ? 19.31000  4.29300   21.69300  1.000 42.82438  ?  312 PHE   A O    1 
ATOM   1060 C  CB   . PHE   A 1 160 ? 16.96300  1.91300   21.77700  1.000 36.95740  ?  312 PHE   A CB   1 
ATOM   1061 C  CG   . PHE   A 1 160 ? 17.81900  1.58900   20.58300  1.000 42.47676  ?  312 PHE   A CG   1 
ATOM   1062 C  CD1  . PHE   A 1 160 ? 18.84300  0.66000   20.68200  1.000 42.86500  ?  312 PHE   A CD1  1 
ATOM   1063 C  CD2  . PHE   A 1 160 ? 17.59900  2.20900   19.36100  1.000 39.59506  ?  312 PHE   A CD2  1 
ATOM   1064 C  CE1  . PHE   A 1 160 ? 19.63500  0.35900   19.58800  1.000 43.15635  ?  312 PHE   A CE1  1 
ATOM   1065 C  CE2  . PHE   A 1 160 ? 18.39100  1.91300   18.26300  1.000 42.90523  ?  312 PHE   A CE2  1 
ATOM   1066 C  CZ   . PHE   A 1 160 ? 19.40900  0.98700   18.37800  1.000 42.01145  ?  312 PHE   A CZ   1 
ATOM   1067 N  N    . GLN   A 1 161 ? 17.19700  4.99200   21.34400  1.000 41.54120  ?  313 GLN   A N    1 
ATOM   1068 C  CA   . GLN   A 1 161 ? 17.61900  6.13100   20.53400  1.000 35.55813  ?  313 GLN   A CA   1 
ATOM   1069 C  C    . GLN   A 1 161 ? 18.52200  7.06400   21.32900  1.000 42.11961  ?  313 GLN   A C    1 
ATOM   1070 O  O    . GLN   A 1 161 ? 19.55800  7.51900   20.83200  1.000 42.08132  ?  313 GLN   A O    1 
ATOM   1071 C  CB   . GLN   A 1 161 ? 16.39300  6.88800   20.02100  1.000 41.19240  ?  313 GLN   A CB   1 
ATOM   1072 C  CG   . GLN   A 1 161 ? 15.52700  6.10500   19.05000  1.000 39.29068  ?  313 GLN   A CG   1 
ATOM   1073 C  CD   . GLN   A 1 161 ? 16.22900  5.82300   17.73900  1.000 41.71627  ?  313 GLN   A CD   1 
ATOM   1074 O  OE1  . GLN   A 1 161 ? 17.01100  6.63800   17.25400  1.000 47.34259  ?  313 GLN   A OE1  1 
ATOM   1075 N  NE2  . GLN   A 1 161 ? 15.94200  4.66800   17.15000  1.000 39.77301  ?  313 GLN   A NE2  1 
ATOM   1076 N  N    . VAL   A 1 162 ? 18.14300  7.35400   22.57500  1.000 45.14032  ?  314 VAL   A N    1 
ATOM   1077 C  CA   . VAL   A 1 162 ? 18.92300  8.26900   23.40200  1.000 48.59469  ?  314 VAL   A CA   1 
ATOM   1078 C  C    . VAL   A 1 162 ? 20.28700  7.67000   23.71200  1.000 45.30546  ?  314 VAL   A C    1 
ATOM   1079 O  O    . VAL   A 1 162 ? 21.32400  8.31800   23.52500  1.000 52.12796  ?  314 VAL   A O    1 
ATOM   1080 C  CB   . VAL   A 1 162 ? 18.15300  8.61200   24.68900  1.000 47.18049  ?  314 VAL   A CB   1 
ATOM   1081 C  CG1  . VAL   A 1 162 ? 19.08600  9.22800   25.72000  1.000 45.91066  ?  314 VAL   A CG1  1 
ATOM   1082 C  CG2  . VAL   A 1 162 ? 16.99300  9.53500   24.37800  1.000 49.67726  ?  314 VAL   A CG2  1 
ATOM   1083 N  N    . GLY   A 1 163 ? 20.30600  6.42300   24.19100  1.000 44.35724  ?  315 GLY   A N    1 
ATOM   1084 C  CA   . GLY   A 1 163 ? 21.56800  5.77100   24.49100  1.000 40.61023  ?  315 GLY   A CA   1 
ATOM   1085 C  C    . GLY   A 1 163 ? 22.44500  5.58200   23.27000  1.000 48.83023  ?  315 GLY   A C    1 
ATOM   1086 O  O    . GLY   A 1 163 ? 23.67500  5.60600   23.37300  1.000 47.38988  ?  315 GLY   A O    1 
ATOM   1087 N  N    . LEU   A 1 164 ? 21.83100  5.39600   22.09800  1.000 39.90946  ?  316 LEU   A N    1 
ATOM   1088 C  CA   . LEU   A 1 164 ? 22.61200  5.27800   20.87100  1.000 40.26410  ?  316 LEU   A CA   1 
ATOM   1089 C  C    . LEU   A 1 164 ? 23.16200  6.62900   20.43800  1.000 41.61801  ?  316 LEU   A C    1 
ATOM   1090 O  O    . LEU   A 1 164 ? 24.31600  6.72500   20.00400  1.000 49.86814  ?  316 LEU   A O    1 
ATOM   1091 C  CB   . LEU   A 1 164 ? 21.76000  4.66700   19.75900  1.000 39.43458  ?  316 LEU   A CB   1 
ATOM   1092 C  CG   . LEU   A 1 164 ? 22.44300  4.49300   18.40100  1.000 42.35402  ?  316 LEU   A CG   1 
ATOM   1093 C  CD1  . LEU   A 1 164 ? 23.69800  3.64700   18.53800  1.000 37.62645  ?  316 LEU   A CD1  1 
ATOM   1094 C  CD2  . LEU   A 1 164 ? 21.48600  3.87500   17.39100  1.000 37.95400  ?  316 LEU   A CD2  1 
ATOM   1095 N  N    . LYS   A 1 165 ? 22.34900  7.68500   20.53900  1.000 41.74074  ?  317 LYS   A N    1 
ATOM   1096 C  CA   . LYS   A 1 165 ? 22.82700  9.01500   20.17900  1.000 41.05041  ?  317 LYS   A CA   1 
ATOM   1097 C  C    . LYS   A 1 165 ? 23.94000  9.47300   21.10900  1.000 43.88323  ?  317 LYS   A C    1 
ATOM   1098 O  O    . LYS   A 1 165 ? 24.85400  10.18500  20.67800  1.000 51.10014  ?  317 LYS   A O    1 
ATOM   1099 C  CB   . LYS   A 1 165 ? 21.67200  10.01600  20.19900  1.000 47.13958  ?  317 LYS   A CB   1 
ATOM   1100 C  CG   . LYS   A 1 165 ? 21.93600  11.27300  19.38800  1.000 47.06005  ?  317 LYS   A CG   1 
ATOM   1101 C  CD   . LYS   A 1 165 ? 21.48700  11.09500  17.94900  1.000 54.15636  ?  317 LYS   A CD   1 
ATOM   1102 C  CE   . LYS   A 1 165 ? 21.80000  12.32400  17.11500  1.000 57.96463  ?  317 LYS   A CE   1 
ATOM   1103 N  NZ   . LYS   A 1 165 ? 21.23700  12.20300  15.74300  1.000 56.16281  ?  317 LYS   A NZ   1 
ATOM   1104 N  N    . LYS   A 1 166 ? 23.88900  9.06700   22.38100  1.000 39.81836  ?  318 LYS   A N    1 
ATOM   1105 C  CA   . LYS   A 1 166 ? 24.93300  9.44000   23.32600  1.000 44.72172  ?  318 LYS   A CA   1 
ATOM   1106 C  C    . LYS   A 1 166 ? 26.26600  8.77400   23.01100  1.000 46.04051  ?  318 LYS   A C    1 
ATOM   1107 O  O    . LYS   A 1 166 ? 27.30400  9.24200   23.48800  1.000 47.96842  ?  318 LYS   A O    1 
ATOM   1108 C  CB   . LYS   A 1 166 ? 24.49800  9.09600   24.75200  1.000 53.71501  ?  318 LYS   A CB   1 
ATOM   1109 C  CG   . LYS   A 1 166 ? 23.46400  10.05500  25.32500  1.000 57.27178  ?  318 LYS   A CG   1 
ATOM   1110 C  CD   . LYS   A 1 166 ? 22.82000  9.50800   26.58800  1.000 62.34074  ?  318 LYS   A CD   1 
ATOM   1111 C  CE   . LYS   A 1 166 ? 22.15900  10.61800  27.39100  1.000 66.97645  ?  318 LYS   A CE   1 
ATOM   1112 N  NZ   . LYS   A 1 166 ? 21.52700  10.10800  28.64000  1.000 72.09602  ?  318 LYS   A NZ   1 
ATOM   1113 N  N    . LEU   A 1 167 ? 26.26700  7.69900   22.21800  1.000 44.61199  ?  319 LEU   A N    1 
ATOM   1114 C  CA   . LEU   A 1 167 ? 27.52700  7.09100   21.80700  1.000 41.28136  ?  319 LEU   A CA   1 
ATOM   1115 C  C    . LEU   A 1 167 ? 28.28700  7.95700   20.81200  1.000 46.54700  ?  319 LEU   A C    1 
ATOM   1116 O  O    . LEU   A 1 167 ? 29.49400  7.75800   20.64100  1.000 44.55754  ?  319 LEU   A O    1 
ATOM   1117 C  CB   . LEU   A 1 167 ? 27.28100  5.70600   21.20300  1.000 33.04566  ?  319 LEU   A CB   1 
ATOM   1118 C  CG   . LEU   A 1 167 ? 26.73300  4.62000   22.13100  1.000 37.24389  ?  319 LEU   A CG   1 
ATOM   1119 C  CD1  . LEU   A 1 167 ? 26.73500  3.27300   21.42300  1.000 39.36407  ?  319 LEU   A CD1  1 
ATOM   1120 C  CD2  . LEU   A 1 167 ? 27.53800  4.55200   23.42300  1.000 40.02494  ?  319 LEU   A CD2  1 
ATOM   1121 N  N    . ASN   A 1 168 ? 27.61000  8.90700   20.16700  1.000 48.94134  ?  320 ASN   A N    1 
ATOM   1122 C  CA   . ASN   A 1 168 ? 28.19600  9.79900   19.16300  1.000 49.32580  ?  320 ASN   A CA   1 
ATOM   1123 C  C    . ASN   A 1 168 ? 29.09000  9.02600   18.19800  1.000 43.88765  ?  320 ASN   A C    1 
ATOM   1124 O  O    . ASN   A 1 168 ? 30.28100  9.29900   18.04400  1.000 46.02395  ?  320 ASN   A O    1 
ATOM   1125 C  CB   . ASN   A 1 168 ? 28.96300  10.94600  19.81900  1.000 56.07628  ?  320 ASN   A CB   1 
ATOM   1126 C  CG   . ASN   A 1 168 ? 28.17900  11.61000  20.92900  1.000 74.97001  ?  320 ASN   A CG   1 
ATOM   1127 O  OD1  . ASN   A 1 168 ? 27.21100  12.32600  20.67700  1.000 80.47647  ?  320 ASN   A OD1  1 
ATOM   1128 N  ND2  . ASN   A 1 168 ? 28.60000  11.38300  22.16900  1.000 76.79254  ?  320 ASN   A ND2  1 
ATOM   1129 N  N    . LEU   A 1 169 ? 28.48600  8.03300   17.55500  1.000 40.07715  ?  321 LEU   A N    1 
ATOM   1130 C  CA   . LEU   A 1 169 ? 29.23600  7.17300   16.65400  1.000 34.90863  ?  321 LEU   A CA   1 
ATOM   1131 C  C    . LEU   A 1 169 ? 29.74300  7.96100   15.45500  1.000 41.37439  ?  321 LEU   A C    1 
ATOM   1132 O  O    . LEU   A 1 169 ? 29.05700  8.84300   14.93200  1.000 42.12332  ?  321 LEU   A O    1 
ATOM   1133 C  CB   . LEU   A 1 169 ? 28.36200  6.01300   16.17500  1.000 34.76244  ?  321 LEU   A CB   1 
ATOM   1134 C  CG   . LEU   A 1 169 ? 27.89600  4.99000   17.21000  1.000 32.02317  ?  321 LEU   A CG   1 
ATOM   1135 C  CD1  . LEU   A 1 169 ? 27.15500  3.85000   16.52700  1.000 33.85709  ?  321 LEU   A CD1  1 
ATOM   1136 C  CD2  . LEU   A 1 169 ? 29.07300  4.46200   18.01000  1.000 32.87479  ?  321 LEU   A CD2  1 
ATOM   1137 N  N    . HIS   A 1 170 ? 30.96300  7.64700   15.03200  1.000 39.94679  ?  322 HIS   A N    1 
ATOM   1138 C  CA   . HIS   A 1 170 ? 31.39900  8.06400   13.71100  1.000 36.20883  ?  322 HIS   A CA   1 
ATOM   1139 C  C    . HIS   A 1 170 ? 30.50300  7.41500   12.66400  1.000 40.88388  ?  322 HIS   A C    1 
ATOM   1140 O  O    . HIS   A 1 170 ? 29.93800  6.34000   12.88300  1.000 35.31385  ?  322 HIS   A O    1 
ATOM   1141 C  CB   . HIS   A 1 170 ? 32.85800  7.66900   13.46900  1.000 35.83979  ?  322 HIS   A CB   1 
ATOM   1142 C  CG   . HIS   A 1 170 ? 33.82900  8.30800   14.41200  1.000 41.38912  ?  322 HIS   A CG   1 
ATOM   1143 N  ND1  . HIS   A 1 170 ? 35.18700  8.32300   14.18000  1.000 41.14037  ?  322 HIS   A ND1  1 
ATOM   1144 C  CD2  . HIS   A 1 170 ? 33.64200  8.95100   15.59000  1.000 40.80579  ?  322 HIS   A CD2  1 
ATOM   1145 C  CE1  . HIS   A 1 170 ? 35.79500  8.95000   15.17200  1.000 43.75040  ?  322 HIS   A CE1  1 
ATOM   1146 N  NE2  . HIS   A 1 170 ? 34.87900  9.34000   16.04100  1.000 42.31007  ?  322 HIS   A NE2  1 
ATOM   1147 N  N    . GLU   A 1 171 ? 30.36200  8.08700   11.52000  1.000 40.40884  ?  323 GLU   A N    1 
ATOM   1148 C  CA   . GLU   A 1 171 ? 29.62400  7.49600   10.41000  1.000 39.54240  ?  323 GLU   A CA   1 
ATOM   1149 C  C    . GLU   A 1 171 ? 30.17200  6.12100   10.05800  1.000 37.81070  ?  323 GLU   A C    1 
ATOM   1150 O  O    . GLU   A 1 171 ? 29.41300  5.22700   9.66600   1.000 36.53496  ?  323 GLU   A O    1 
ATOM   1151 C  CB   . GLU   A 1 171 ? 29.68500  8.42000   9.19600   1.000 42.68658  ?  323 GLU   A CB   1 
ATOM   1152 C  CG   . GLU   A 1 171 ? 28.62000  8.16000   8.15200   1.000 46.83733  ?  323 GLU   A CG   1 
ATOM   1153 C  CD   . GLU   A 1 171 ? 28.80700  9.03100   6.92600   1.000 47.58238  ?  323 GLU   A CD   1 
ATOM   1154 O  OE1  . GLU   A 1 171 ? 29.88100  9.65700   6.80500   1.000 48.96620  ?  323 GLU   A OE1  1 
ATOM   1155 O  OE2  . GLU   A 1 171 ? 27.88600  9.09200   6.08600   1.000 48.89974  ?  323 GLU   A OE2  1 
ATOM   1156 N  N    . GLU   A 1 172 ? 31.48400  5.92900   10.21300  1.000 36.50166  ?  324 GLU   A N    1 
ATOM   1157 C  CA   . GLU   A 1 172 ? 32.08000  4.62100   9.96900   1.000 36.88256  ?  324 GLU   A CA   1 
ATOM   1158 C  C    . GLU   A 1 172 ? 31.55900  3.58200   10.95600  1.000 37.18810  ?  324 GLU   A C    1 
ATOM   1159 O  O    . GLU   A 1 172 ? 31.25800  2.44700   10.57200  1.000 39.58317  ?  324 GLU   A O    1 
ATOM   1160 C  CB   . GLU   A 1 172 ? 33.60200  4.72400   10.04800  1.000 36.70518  ?  324 GLU   A CB   1 
ATOM   1161 C  CG   . GLU   A 1 172 ? 34.23100  5.53600   8.92600   1.000 40.45157  ?  324 GLU   A CG   1 
ATOM   1162 C  CD   . GLU   A 1 172 ? 34.34200  7.01800   9.24100   1.000 47.92889  ?  324 GLU   A CD   1 
ATOM   1163 O  OE1  . GLU   A 1 172 ? 35.20800  7.68100   8.63200   1.000 56.67418  ?  324 GLU   A OE1  1 
ATOM   1164 O  OE2  . GLU   A 1 172 ? 33.56900  7.52400   10.08300  1.000 44.29380  ?  324 GLU   A OE2  1 
ATOM   1165 N  N    . GLU   A 1 173 ? 31.45200  3.95100   12.23500  1.000 38.30640  ?  325 GLU   A N    1 
ATOM   1166 C  CA   . GLU   A 1 173 ? 30.90800  3.03000   13.22600  1.000 33.24312  ?  325 GLU   A CA   1 
ATOM   1167 C  C    . GLU   A 1 173 ? 29.41800  2.80000   13.01200  1.000 30.90071  ?  325 GLU   A C    1 
ATOM   1168 O  O    . GLU   A 1 173 ? 28.91900  1.69300   13.24700  1.000 32.43591  ?  325 GLU   A O    1 
ATOM   1169 C  CB   . GLU   A 1 173 ? 31.17500  3.56300   14.63500  1.000 33.10062  ?  325 GLU   A CB   1 
ATOM   1170 C  CG   . GLU   A 1 173 ? 32.65400  3.56800   15.01500  1.000 32.92226  ?  325 GLU   A CG   1 
ATOM   1171 C  CD   . GLU   A 1 173 ? 33.02400  4.68600   15.97600  1.000 39.45922  ?  325 GLU   A CD   1 
ATOM   1172 O  OE1  . GLU   A 1 173 ? 34.22800  4.82400   16.28600  1.000 42.84389  ?  325 GLU   A OE1  1 
ATOM   1173 O  OE2  . GLU   A 1 173 ? 32.12100  5.42200   16.42500  1.000 39.08164  ?  325 GLU   A OE2  1 
ATOM   1174 N  N    . HIS   A 1 174 ? 28.70400  3.82500   12.55000  1.000 32.57542  ?  326 HIS   A N    1 
ATOM   1175 C  CA   . HIS   A 1 174 ? 27.26700  3.70800   12.32800  1.000 32.55030  ?  326 HIS   A CA   1 
ATOM   1176 C  C    . HIS   A 1 174 ? 26.95600  2.70600   11.21900  1.000 36.04573  ?  326 HIS   A C    1 
ATOM   1177 O  O    . HIS   A 1 174 ? 26.06200  1.86300   11.36300  1.000 35.26575  ?  326 HIS   A O    1 
ATOM   1178 C  CB   . HIS   A 1 174 ? 26.69400  5.08900   12.00300  1.000 39.72581  ?  326 HIS   A CB   1 
ATOM   1179 C  CG   . HIS   A 1 174 ? 25.23100  5.08800   11.69200  1.000 48.13724  ?  326 HIS   A CG   1 
ATOM   1180 N  ND1  . HIS   A 1 174 ? 24.26400  4.90300   12.65700  1.000 46.21375  ?  326 HIS   A ND1  1 
ATOM   1181 C  CD2  . HIS   A 1 174 ? 24.56900  5.27200   10.52500  1.000 46.81262  ?  326 HIS   A CD2  1 
ATOM   1182 C  CE1  . HIS   A 1 174 ? 23.07000  4.96200   12.09500  1.000 50.95684  ?  326 HIS   A CE1  1 
ATOM   1183 N  NE2  . HIS   A 1 174 ? 23.22700  5.18500   10.80300  1.000 47.58577  ?  326 HIS   A NE2  1 
ATOM   1184 N  N    . VAL   A 1 175 ? 27.69000  2.77400   10.10700  1.000 35.25522  ?  327 VAL   A N    1 
ATOM   1185 C  CA   . VAL   A 1 175 ? 27.41000  1.87500   8.99000   1.000 30.53005  ?  327 VAL   A CA   1 
ATOM   1186 C  C    . VAL   A 1 175 ? 27.92300  0.46700   9.27200   1.000 39.04685  ?  327 VAL   A C    1 
ATOM   1187 O  O    . VAL   A 1 175 ? 27.34100  -0.51500  8.79400   1.000 30.50466  ?  327 VAL   A O    1 
ATOM   1188 C  CB   . VAL   A 1 175 ? 27.99900  2.43500   7.68300   1.000 31.48175  ?  327 VAL   A CB   1 
ATOM   1189 C  CG1  . VAL   A 1 175 ? 27.40100  3.79700   7.38200   1.000 35.41001  ?  327 VAL   A CG1  1 
ATOM   1190 C  CG2  . VAL   A 1 175 ? 29.51800  2.52300   7.76400   1.000 31.50829  ?  327 VAL   A CG2  1 
ATOM   1191 N  N    . LEU   A 1 176 ? 29.00800  0.33900   10.04100  1.000 35.29183  ?  328 LEU   A N    1 
ATOM   1192 C  CA   . LEU   A 1 176 ? 29.47800  -0.98600  10.43000  1.000 33.15096  ?  328 LEU   A CA   1 
ATOM   1193 C  C    . LEU   A 1 176 ? 28.48200  -1.66400  11.36000  1.000 32.09664  ?  328 LEU   A C    1 
ATOM   1194 O  O    . LEU   A 1 176 ? 28.23900  -2.87200  11.24600  1.000 35.92238  ?  328 LEU   A O    1 
ATOM   1195 C  CB   . LEU   A 1 176 ? 30.85100  -0.88400  11.09400  1.000 33.39604  ?  328 LEU   A CB   1 
ATOM   1196 C  CG   . LEU   A 1 176 ? 32.06200  -0.76000  10.16800  1.000 38.61874  ?  328 LEU   A CG   1 
ATOM   1197 C  CD1  . LEU   A 1 176 ? 33.24200  -0.15300  10.91400  1.000 33.95009  ?  328 LEU   A CD1  1 
ATOM   1198 C  CD2  . LEU   A 1 176 ? 32.43300  -2.11100  9.57500   1.000 33.18661  ?  328 LEU   A CD2  1 
ATOM   1199 N  N    . LEU   A 1 177 ? 27.88400  -0.90100  12.27800  1.000 30.24720  ?  329 LEU   A N    1 
ATOM   1200 C  CA   . LEU   A 1 177 ? 26.90500  -1.47900  13.19300  1.000 34.28544  ?  329 LEU   A CA   1 
ATOM   1201 C  C    . LEU   A 1 177 ? 25.66700  -1.95600  12.44500  1.000 29.47278  ?  329 LEU   A C    1 
ATOM   1202 O  O    . LEU   A 1 177 ? 25.13200  -3.03000  12.74100  1.000 27.34686  ?  329 LEU   A O    1 
ATOM   1203 C  CB   . LEU   A 1 177 ? 26.52500  -0.46400  14.27000  1.000 35.38023  ?  329 LEU   A CB   1 
ATOM   1204 C  CG   . LEU   A 1 177 ? 25.65300  -0.98900  15.41400  1.000 39.40927  ?  329 LEU   A CG   1 
ATOM   1205 C  CD1  . LEU   A 1 177 ? 26.31300  -2.18300  16.09200  1.000 38.48188  ?  329 LEU   A CD1  1 
ATOM   1206 C  CD2  . LEU   A 1 177 ? 25.36800  0.11600   16.41900  1.000 33.21917  ?  329 LEU   A CD2  1 
ATOM   1207 N  N    . MET   A 1 178 ? 25.19700  -1.17100  11.47200  1.000 32.77617  ?  330 MET   A N    1 
ATOM   1208 C  CA   . MET   A 1 178 ? 24.08500  -1.61500  10.63700  1.000 33.51553  ?  330 MET   A CA   1 
ATOM   1209 C  C    . MET   A 1 178 ? 24.44100  -2.89900  9.90100   1.000 31.66126  ?  330 MET   A C    1 
ATOM   1210 O  O    . MET   A 1 178 ? 23.65000  -3.85000  9.86100   1.000 33.67603  ?  330 MET   A O    1 
ATOM   1211 C  CB   . MET   A 1 178 ? 23.70200  -0.52100  9.64000   1.000 27.54513  ?  330 MET   A CB   1 
ATOM   1212 C  CG   . MET   A 1 178 ? 23.01100  0.68100   10.25300  1.000 37.86323  ?  330 MET   A CG   1 
ATOM   1213 S  SD   . MET   A 1 178 ? 22.21500  1.71800   9.00600   1.000 35.66153  ?  330 MET   A SD   1 
ATOM   1214 C  CE   . MET   A 1 178 ? 23.64100  2.33100   8.11400   1.000 34.92570  ?  330 MET   A CE   1 
ATOM   1215 N  N    . ALA   A 1 179 ? 25.63900  -2.94200  9.31200   1.000 33.25366  ?  331 ALA   A N    1 
ATOM   1216 C  CA   . ALA   A 1 179 ? 26.05800  -4.12100  8.56200   1.000 29.75280  ?  331 ALA   A CA   1 
ATOM   1217 C  C    . ALA   A 1 179 ? 26.18000  -5.33600  9.47300   1.000 31.19301  ?  331 ALA   A C    1 
ATOM   1218 O  O    . ALA   A 1 179 ? 25.68200  -6.41900  9.14800   1.000 28.69328  ?  331 ALA   A O    1 
ATOM   1219 C  CB   . ALA   A 1 179 ? 27.37900  -3.84300  7.84400   1.000 31.30203  ?  331 ALA   A CB   1 
ATOM   1220 N  N    . ILE   A 1 180 ? 26.83900  -5.17100  10.62400  1.000 32.09778  ?  332 ILE   A N    1 
ATOM   1221 C  CA   . ILE   A 1 180 ? 26.95700  -6.26600  11.58500  1.000 31.88953  ?  332 ILE   A CA   1 
ATOM   1222 C  C    . ILE   A 1 180 ? 25.57800  -6.75200  12.00600  1.000 36.38501  ?  332 ILE   A C    1 
ATOM   1223 O  O    . ILE   A 1 180 ? 25.33400  -7.96100  12.12000  1.000 32.99823  ?  332 ILE   A O    1 
ATOM   1224 C  CB   . ILE   A 1 180 ? 27.79200  -5.82200  12.80200  1.000 26.06011  ?  332 ILE   A CB   1 
ATOM   1225 C  CG1  . ILE   A 1 180 ? 29.25700  -5.62500  12.41100  1.000 33.92906  ?  332 ILE   A CG1  1 
ATOM   1226 C  CG2  . ILE   A 1 180 ? 27.67500  -6.83700  13.92900  1.000 29.49532  ?  332 ILE   A CG2  1 
ATOM   1227 C  CD1  . ILE   A 1 180 ? 30.04900  -4.78500  13.39800  1.000 34.68261  ?  332 ILE   A CD1  1 
ATOM   1228 N  N    . CYS   A 1 181 ? 24.65300  -5.81700  12.23700  1.000 33.46805  ?  333 CYS   A N    1 
ATOM   1229 C  CA   . CYS   A 1 181 ? 23.29300  -6.18400  12.61500  1.000 39.64939  ?  333 CYS   A CA   1 
ATOM   1230 C  C    . CYS   A 1 181 ? 22.64600  -7.07600  11.56300  1.000 33.96716  ?  333 CYS   A C    1 
ATOM   1231 O  O    . CYS   A 1 181 ? 21.94900  -8.04100  11.89900  1.000 33.43925  ?  333 CYS   A O    1 
ATOM   1232 C  CB   . CYS   A 1 181 ? 22.46000  -4.92100  12.83300  1.000 36.52696  ?  333 CYS   A CB   1 
ATOM   1233 S  SG   . CYS   A 1 181 ? 20.71300  -5.20500  13.17200  1.000 35.10133  ?  333 CYS   A SG   1 
ATOM   1234 N  N    . ILE   A 1 182 ? 22.88200  -6.78100  10.28300  1.000 33.61897  ?  334 ILE   A N    1 
ATOM   1235 C  CA   . ILE   A 1 182 ? 22.21400  -7.52300  9.21800   1.000 34.83147  ?  334 ILE   A CA   1 
ATOM   1236 C  C    . ILE   A 1 182 ? 22.78700  -8.93000  9.09200   1.000 35.75511  ?  334 ILE   A C    1 
ATOM   1237 O  O    . ILE   A 1 182 ? 22.04200  -9.90800  8.95800   1.000 33.27757  ?  334 ILE   A O    1 
ATOM   1238 C  CB   . ILE   A 1 182 ? 22.31000  -6.74700  7.89200   1.000 35.22741  ?  334 ILE   A CB   1 
ATOM   1239 C  CG1  . ILE   A 1 182 ? 21.49400  -5.45800  7.97700   1.000 34.79189  ?  334 ILE   A CG1  1 
ATOM   1240 C  CG2  . ILE   A 1 182 ? 21.82100  -7.60100  6.73200   1.000 34.71700  ?  334 ILE   A CG2  1 
ATOM   1241 C  CD1  . ILE   A 1 182 ? 21.76600  -4.47600  6.86100   1.000 34.76314  ?  334 ILE   A CD1  1 
ATOM   1242 N  N    A VAL   A 1 183 ? 24.11400  -9.06200  9.12200   0.720 35.17120  ?  335 VAL   A N    1 
ATOM   1243 N  N    B VAL   A 1 183 ? 24.11000  -9.06000  9.16300   0.280 34.70640  ?  335 VAL   A N    1 
ATOM   1244 C  CA   A VAL   A 1 183 ? 24.74300  -10.36300 8.91400   0.720 34.25996  ?  335 VAL   A CA   1 
ATOM   1245 C  CA   B VAL   A 1 183 ? 24.77600  -10.33400 8.91800   0.280 34.97266  ?  335 VAL   A CA   1 
ATOM   1246 C  C    A VAL   A 1 183 ? 24.96700  -11.05000 10.25700  0.720 33.89102  ?  335 VAL   A C    1 
ATOM   1247 C  C    B VAL   A 1 183 ? 24.98600  -11.06300 10.24600  0.280 35.30626  ?  335 VAL   A C    1 
ATOM   1248 O  O    A VAL   A 1 183 ? 26.10500  -11.32100 10.65600  0.720 40.43740  ?  335 VAL   A O    1 
ATOM   1249 O  O    B VAL   A 1 183 ? 26.11500  -11.38100 10.63900  0.280 39.50483  ?  335 VAL   A O    1 
ATOM   1250 C  CB   A VAL   A 1 183 ? 26.05200  -10.23100 8.10900   0.720 38.76939  ?  335 VAL   A CB   1 
ATOM   1251 C  CB   B VAL   A 1 183 ? 26.08500  -10.10100 8.13000   0.280 38.35209  ?  335 VAL   A CB   1 
ATOM   1252 C  CG1  A VAL   A 1 183 ? 25.74300  -9.80600  6.68300   0.720 37.21306  ?  335 VAL   A CG1  1 
ATOM   1253 C  CG1  B VAL   A 1 183 ? 27.07500  -9.23100  8.90700   0.280 41.26810  ?  335 VAL   A CG1  1 
ATOM   1254 C  CG2  A VAL   A 1 183 ? 26.99900  -9.23100  8.75200   0.720 43.84805  ?  335 VAL   A CG2  1 
ATOM   1255 C  CG2  B VAL   A 1 183 ? 26.71200  -11.40900 7.66300   0.280 36.20690  ?  335 VAL   A CG2  1 
ATOM   1256 N  N    . SER   A 1 184 ? 23.88300  -11.34500 10.95500  1.000 35.12668  ?  336 SER   A N    1 
ATOM   1257 C  CA   . SER   A 1 184 ? 23.99400  -12.09100 12.20400  1.000 38.01186  ?  336 SER   A CA   1 
ATOM   1258 C  C    . SER   A 1 184 ? 23.69800  -13.56000 11.95400  1.000 35.73539  ?  336 SER   A C    1 
ATOM   1259 O  O    . SER   A 1 184 ? 22.63200  -13.88500 11.41000  1.000 39.65568  ?  336 SER   A O    1 
ATOM   1260 C  CB   . SER   A 1 184 ? 23.03800  -11.53900 13.25700  1.000 39.00596  ?  336 SER   A CB   1 
ATOM   1261 O  OG   . SER   A 1 184 ? 23.08700  -10.12500 13.29500  1.000 44.64430  ?  336 SER   A OG   1 
ATOM   1262 N  N    . PRO   A 1 185 ? 24.60300  -14.47100 12.32800  1.000 37.75110  ?  337 PRO   A N    1 
ATOM   1263 C  CA   . PRO   A 1 185 ? 24.39800  -15.89100 12.00200  1.000 34.18933  ?  337 PRO   A CA   1 
ATOM   1264 C  C    . PRO   A 1 185 ? 23.31200  -16.56700 12.82000  1.000 39.24097  ?  337 PRO   A C    1 
ATOM   1265 O  O    . PRO   A 1 185 ? 22.87700  -17.66300 12.44300  1.000 43.33480  ?  337 PRO   A O    1 
ATOM   1266 C  CB   . PRO   A 1 185 ? 25.77000  -16.51700 12.28500  1.000 38.12705  ?  337 PRO   A CB   1 
ATOM   1267 C  CG   . PRO   A 1 185 ? 26.38800  -15.62100 13.30200  1.000 39.09651  ?  337 PRO   A CG   1 
ATOM   1268 C  CD   . PRO   A 1 185 ? 25.89600  -14.23300 12.99300  1.000 34.00788  ?  337 PRO   A CD   1 
ATOM   1269 N  N    . ASP   A 1 186 ? 22.86200  -15.96700 13.91600  1.000 43.07334  ?  338 ASP   A N    1 
ATOM   1270 C  CA   . ASP   A 1 186 ? 21.88600  -16.60300 14.79100  1.000 44.59627  ?  338 ASP   A CA   1 
ATOM   1271 C  C    . ASP   A 1 186 ? 20.44600  -16.32300 14.38500  1.000 41.29189  ?  338 ASP   A C    1 
ATOM   1272 O  O    . ASP   A 1 186 ? 19.52900  -16.72400 15.10800  1.000 48.80044  ?  338 ASP   A O    1 
ATOM   1273 C  CB   . ASP   A 1 186 ? 22.10100  -16.14700 16.23400  1.000 38.58290  ?  338 ASP   A CB   1 
ATOM   1274 C  CG   . ASP   A 1 186 ? 21.81700  -14.67800 16.41800  1.000 45.30716  ?  338 ASP   A CG   1 
ATOM   1275 O  OD1  . ASP   A 1 186 ? 21.19800  -14.31000 17.43700  1.000 62.25522  ?  338 ASP   A OD1  1 
ATOM   1276 O  OD2  . ASP   A 1 186 ? 22.20800  -13.89000 15.53100  1.000 50.41332  ?  338 ASP   A OD2  1 
ATOM   1277 N  N    . ARG   A 1 187 ? 20.22500  -15.64700 13.26200  1.000 37.35625  ?  339 ARG   A N    1 
ATOM   1278 C  CA   . ARG   A 1 187 ? 18.86400  -15.36700 12.82900  1.000 35.62361  ?  339 ARG   A CA   1 
ATOM   1279 C  C    . ARG   A 1 187 ? 18.15700  -16.66800 12.45900  1.000 40.09940  ?  339 ARG   A C    1 
ATOM   1280 O  O    . ARG   A 1 187 ? 18.77600  -17.57500 11.89400  1.000 45.45573  ?  339 ARG   A O    1 
ATOM   1281 C  CB   . ARG   A 1 187 ? 18.85900  -14.41400 11.63400  1.000 32.27495  ?  339 ARG   A CB   1 
ATOM   1282 C  CG   . ARG   A 1 187 ? 19.58800  -13.10600 11.87700  1.000 32.04883  ?  339 ARG   A CG   1 
ATOM   1283 C  CD   . ARG   A 1 187 ? 18.75300  -12.13800 12.69300  1.000 38.55285  ?  339 ARG   A CD   1 
ATOM   1284 N  NE   . ARG   A 1 187 ? 19.32800  -10.79500 12.68900  1.000 32.73894  ?  339 ARG   A NE   1 
ATOM   1285 C  CZ   . ARG   A 1 187 ? 18.91800  -9.80600  13.47500  1.000 35.78517  ?  339 ARG   A CZ   1 
ATOM   1286 N  NH1  . ARG   A 1 187 ? 17.92600  -10.00700 14.33100  1.000 33.20317  ?  339 ARG   A NH1  1 
ATOM   1287 N  NH2  . ARG   A 1 187 ? 19.50400  -8.61700  13.41100  1.000 32.33529  ?  339 ARG   A NH2  1 
ATOM   1288 N  N    . PRO   A 1 188 ? 16.86400  -16.79000 12.75900  1.000 54.58211  ?  340 PRO   A N    1 
ATOM   1289 C  CA   . PRO   A 1 188 ? 16.14700  -18.03600 12.45200  1.000 54.87242  ?  340 PRO   A CA   1 
ATOM   1290 C  C    . PRO   A 1 188 ? 16.03900  -18.25600 10.94900  1.000 45.05037  ?  340 PRO   A C    1 
ATOM   1291 O  O    . PRO   A 1 188 ? 15.69000  -17.34300 10.19800  1.000 49.59985  ?  340 PRO   A O    1 
ATOM   1292 C  CB   . PRO   A 1 188 ? 14.77100  -17.81600 13.09100  1.000 53.67197  ?  340 PRO   A CB   1 
ATOM   1293 C  CG   . PRO   A 1 188 ? 14.61300  -16.32300 13.11000  1.000 60.96175  ?  340 PRO   A CG   1 
ATOM   1294 C  CD   . PRO   A 1 188 ? 15.98800  -15.78800 13.38900  1.000 57.15910  ?  340 PRO   A CD   1 
ATOM   1295 N  N    . GLY   A 1 189 ? 16.34700  -19.47800 10.51600  1.000 43.40082  ?  341 GLY   A N    1 
ATOM   1296 C  CA   . GLY   A 1 189 ? 16.24200  -19.85700 9.12200   1.000 36.97227  ?  341 GLY   A CA   1 
ATOM   1297 C  C    . GLY   A 1 189 ? 17.52400  -19.76700 8.32200   1.000 45.90809  ?  341 GLY   A C    1 
ATOM   1298 O  O    . GLY   A 1 189 ? 17.51500  -20.11200 7.13400   1.000 42.45498  ?  341 GLY   A O    1 
ATOM   1299 N  N    . VAL   A 1 190 ? 18.62300  -19.31400 8.92500   1.000 48.49378  ?  342 VAL   A N    1 
ATOM   1300 C  CA   . VAL   A 1 190 ? 19.88300  -19.21000 8.20000   1.000 49.37764  ?  342 VAL   A CA   1 
ATOM   1301 C  C    . VAL   A 1 190 ? 20.40600  -20.60600 7.89000   1.000 44.11344  ?  342 VAL   A C    1 
ATOM   1302 O  O    . VAL   A 1 190 ? 20.41000  -21.49200 8.75400   1.000 49.32100  ?  342 VAL   A O    1 
ATOM   1303 C  CB   . VAL   A 1 190 ? 20.90400  -18.39400 9.00700   1.000 42.29334  ?  342 VAL   A CB   1 
ATOM   1304 C  CG1  . VAL   A 1 190 ? 22.27300  -18.44100 8.34400   1.000 39.29095  ?  342 VAL   A CG1  1 
ATOM   1305 C  CG2  . VAL   A 1 190 ? 20.43300  -16.95400 9.14800   1.000 39.00281  ?  342 VAL   A CG2  1 
ATOM   1306 N  N    . GLN   A 1 191 ? 20.83400  -20.81400 6.64600   1.000 47.42279  ?  343 GLN   A N    1 
ATOM   1307 C  CA   . GLN   A 1 191 ? 21.44800  -22.07500 6.24200   1.000 56.85351  ?  343 GLN   A CA   1 
ATOM   1308 C  C    . GLN   A 1 191 ? 22.95900  -22.04800 6.45400   1.000 43.11470  ?  343 GLN   A C    1 
ATOM   1309 O  O    . GLN   A 1 191 ? 23.51400  -22.91300 7.13900   1.000 53.55806  ?  343 GLN   A O    1 
ATOM   1310 C  CB   . GLN   A 1 191 ? 21.12100  -22.37700 4.77400   1.000 61.67033  ?  343 GLN   A CB   1 
ATOM   1311 C  CG   . GLN   A 1 191 ? 19.73400  -22.95000 4.53800   1.000 72.91907  ?  343 GLN   A CG   1 
ATOM   1312 C  CD   . GLN   A 1 191 ? 19.53900  -24.30900 5.18400   1.000 82.76964  ?  343 GLN   A CD   1 
ATOM   1313 O  OE1  . GLN   A 1 191 ? 20.49600  -25.06000 5.38200   1.000 88.41416  ?  343 GLN   A OE1  1 
ATOM   1314 N  NE2  . GLN   A 1 191 ? 18.29300  -24.63400 5.51100   1.000 87.06541  ?  343 GLN   A NE2  1 
ATOM   1315 N  N    . ASP   A 1 192 ? 23.63300  -21.05800 5.87300   1.000 38.74960  ?  344 ASP   A N    1 
ATOM   1316 C  CA   . ASP   A 1 192 ? 25.09000  -20.97100 5.93200   1.000 49.71186  ?  344 ASP   A CA   1 
ATOM   1317 C  C    . ASP   A 1 192 ? 25.51000  -20.03200 7.06200   1.000 41.81802  ?  344 ASP   A C    1 
ATOM   1318 O  O    . ASP   A 1 192 ? 26.07900  -18.96100 6.85000   1.000 39.46999  ?  344 ASP   A O    1 
ATOM   1319 C  CB   . ASP   A 1 192 ? 25.64200  -20.50800 4.58900   1.000 55.94163  ?  344 ASP   A CB   1 
ATOM   1320 C  CG   . ASP   A 1 192 ? 25.22900  -21.41200 3.45400   1.000 66.86949  ?  344 ASP   A CG   1 
ATOM   1321 O  OD1  . ASP   A 1 192 ? 24.71200  -22.51300 3.73500   1.000 79.39570  ?  344 ASP   A OD1  1 
ATOM   1322 O  OD2  . ASP   A 1 192 ? 25.41000  -21.02300 2.28200   1.000 67.82683  ?  344 ASP   A OD2  1 
ATOM   1323 N  N    . ALA   A 1 193 ? 25.22200  -20.47100 8.29100   1.000 44.95932  ?  345 ALA   A N    1 
ATOM   1324 C  CA   . ALA   A 1 193 ? 25.55600  -19.66700 9.46400   1.000 45.41944  ?  345 ALA   A CA   1 
ATOM   1325 C  C    . ALA   A 1 193 ? 27.05300  -19.39800 9.56000   1.000 44.64424  ?  345 ALA   A C    1 
ATOM   1326 O  O    . ALA   A 1 193 ? 27.46300  -18.31900 10.00400  1.000 41.94940  ?  345 ALA   A O    1 
ATOM   1327 C  CB   . ALA   A 1 193 ? 25.05600  -20.35700 10.73300  1.000 46.52566  ?  345 ALA   A CB   1 
ATOM   1328 N  N    . LYS   A 1 194 ? 27.88500  -20.35500 9.14400   1.000 43.68114  ?  346 LYS   A N    1 
ATOM   1329 C  CA   . LYS   A 1 194 ? 29.32700  -20.13700 9.20500   1.000 43.27126  ?  346 LYS   A CA   1 
ATOM   1330 C  C    . LYS   A 1 194 ? 29.77200  -19.10100 8.18100   1.000 46.85283  ?  346 LYS   A C    1 
ATOM   1331 O  O    . LYS   A 1 194 ? 30.66000  -18.28800 8.45900   1.000 47.11122  ?  346 LYS   A O    1 
ATOM   1332 C  CB   . LYS   A 1 194 ? 30.06800  -21.45700 9.00100   1.000 49.61000  ?  346 LYS   A CB   1 
ATOM   1333 C  CG   . LYS   A 1 194 ? 30.15000  -22.30300 10.25800  1.000 57.31333  ?  346 LYS   A CG   1 
ATOM   1334 C  CD   . LYS   A 1 194 ? 30.73200  -23.67400 9.97500   1.000 62.18820  ?  346 LYS   A CD   1 
ATOM   1335 C  CE   . LYS   A 1 194 ? 30.97700  -24.43400 11.26800  1.000 76.94581  ?  346 LYS   A CE   1 
ATOM   1336 N  NZ   . LYS   A 1 194 ? 29.80400  -25.26600 11.65800  1.000 83.61194  ?  346 LYS   A NZ   1 
ATOM   1337 N  N    . LEU   A 1 195 ? 29.16900  -19.11500 6.99000   1.000 49.18410  ?  347 LEU   A N    1 
ATOM   1338 C  CA   . LEU   A 1 195 ? 29.45000  -18.06900 6.01100   1.000 47.12573  ?  347 LEU   A CA   1 
ATOM   1339 C  C    . LEU   A 1 195 ? 28.98100  -16.71000 6.51000   1.000 42.33635  ?  347 LEU   A C    1 
ATOM   1340 O  O    . LEU   A 1 195 ? 29.67200  -15.70000 6.33100   1.000 42.65966  ?  347 LEU   A O    1 
ATOM   1341 C  CB   . LEU   A 1 195 ? 28.78400  -18.40000 4.67600   1.000 44.89264  ?  347 LEU   A CB   1 
ATOM   1342 C  CG   . LEU   A 1 195 ? 29.67700  -19.01300 3.60100   1.000 54.56672  ?  347 LEU   A CG   1 
ATOM   1343 C  CD1  . LEU   A 1 195 ? 30.58000  -20.08600 4.19200   1.000 64.17993  ?  347 LEU   A CD1  1 
ATOM   1344 C  CD2  . LEU   A 1 195 ? 28.82800  -19.56500 2.47100   1.000 61.15916  ?  347 LEU   A CD2  1 
ATOM   1345 N  N    . VAL   A 1 196 ? 27.79800  -16.66400 7.12500   1.000 34.48463  ?  348 VAL   A N    1 
ATOM   1346 C  CA   . VAL   A 1 196 ? 27.29700  -15.41800 7.69500   1.000 34.60804  ?  348 VAL   A CA   1 
ATOM   1347 C  C    . VAL   A 1 196 ? 28.21700  -14.93700 8.80900   1.000 38.57613  ?  348 VAL   A C    1 
ATOM   1348 O  O    . VAL   A 1 196 ? 28.56900  -13.75200 8.87700   1.000 36.75070  ?  348 VAL   A O    1 
ATOM   1349 C  CB   . VAL   A 1 196 ? 25.85200  -15.61100 8.19100   1.000 35.94837  ?  348 VAL   A CB   1 
ATOM   1350 C  CG1  . VAL   A 1 196 ? 25.34100  -14.35500 8.86600   1.000 28.61753  ?  348 VAL   A CG1  1 
ATOM   1351 C  CG2  . VAL   A 1 196 ? 24.94100  -15.99900 7.03400   1.000 34.76233  ?  348 VAL   A CG2  1 
ATOM   1352 N  N    . GLU   A 1 197 ? 28.63100  -15.84800 9.69500   1.000 35.97518  ?  349 GLU   A N    1 
ATOM   1353 C  CA   . GLU   A 1 197 ? 29.55700  -15.46900 10.75800  1.000 42.58311  ?  349 GLU   A CA   1 
ATOM   1354 C  C    . GLU   A 1 197 ? 30.91000  -15.05500 10.19900  1.000 47.66645  ?  349 GLU   A C    1 
ATOM   1355 O  O    . GLU   A 1 197 ? 31.57600  -14.18600 10.77400  1.000 48.72524  ?  349 GLU   A O    1 
ATOM   1356 C  CB   . GLU   A 1 197 ? 29.73200  -16.61600 11.75200  1.000 44.37588  ?  349 GLU   A CB   1 
ATOM   1357 C  CG   . GLU   A 1 197 ? 30.50000  -16.22600 13.00800  1.000 53.76843  ?  349 GLU   A CG   1 
ATOM   1358 C  CD   . GLU   A 1 197 ? 30.28800  -17.20100 14.14700  1.000 66.19578  ?  349 GLU   A CD   1 
ATOM   1359 O  OE1  . GLU   A 1 197 ? 30.61800  -18.39300 13.97500  1.000 68.06696  ?  349 GLU   A OE1  1 
ATOM   1360 O  OE2  . GLU   A 1 197 ? 29.78700  -16.77800 15.21000  1.000 71.27757  ?  349 GLU   A OE2  1 
ATOM   1361 N  N    . ALA   A 1 198 ? 31.33500  -15.65900 9.08900   1.000 53.51040  ?  350 ALA   A N    1 
ATOM   1362 C  CA   . ALA   A 1 198 ? 32.57000  -15.22200 8.44900   1.000 54.55008  ?  350 ALA   A CA   1 
ATOM   1363 C  C    . ALA   A 1 198 ? 32.49100  -13.74700 8.07500   1.000 53.49359  ?  350 ALA   A C    1 
ATOM   1364 O  O    . ALA   A 1 198 ? 33.38800  -12.96600 8.40200   1.000 52.60220  ?  350 ALA   A O    1 
ATOM   1365 C  CB   . ALA   A 1 198 ? 32.86100  -16.08000 7.22000   1.000 59.52506  ?  350 ALA   A CB   1 
ATOM   1366 N  N    . ILE   A 1 199 ? 31.40700  -13.34200 7.40700   1.000 45.62128  ?  351 ILE   A N    1 
ATOM   1367 C  CA   . ILE   A 1 199 ? 31.24900  -11.93600 7.03800   1.000 37.48017  ?  351 ILE   A CA   1 
ATOM   1368 C  C    . ILE   A 1 199 ? 31.21600  -11.06100 8.28400   1.000 38.76127  ?  351 ILE   A C    1 
ATOM   1369 O  O    . ILE   A 1 199 ? 31.92100  -10.04900 8.37100   1.000 36.53286  ?  351 ILE   A O    1 
ATOM   1370 C  CB   . ILE   A 1 199 ? 29.98700  -11.73600 6.18000   1.000 41.31860  ?  351 ILE   A CB   1 
ATOM   1371 C  CG1  . ILE   A 1 199 ? 30.08400  -12.55800 4.89500   1.000 41.29416  ?  351 ILE   A CG1  1 
ATOM   1372 C  CG2  . ILE   A 1 199 ? 29.79400  -10.25000 5.87400   1.000 40.56544  ?  351 ILE   A CG2  1 
ATOM   1373 C  CD1  . ILE   A 1 199 ? 28.79700  -12.62800 4.12300   1.000 43.01742  ?  351 ILE   A CD1  1 
ATOM   1374 N  N    . GLN   A 1 200 ? 30.40700  -11.44900 9.27500   1.000 40.17354  ?  352 GLN   A N    1 
ATOM   1375 C  CA   . GLN   A 1 200 ? 30.23900  -10.62200 10.46600  1.000 37.47671  ?  352 GLN   A CA   1 
ATOM   1376 C  C    . GLN   A 1 200 ? 31.54600  -10.45400 11.22500  1.000 35.68024  ?  352 GLN   A C    1 
ATOM   1377 O  O    . GLN   A 1 200 ? 31.83800  -9.36500  11.73400  1.000 46.02458  ?  352 GLN   A O    1 
ATOM   1378 C  CB   . GLN   A 1 200 ? 29.18100  -11.22200 11.38600  1.000 31.06188  ?  352 GLN   A CB   1 
ATOM   1379 C  CG   . GLN   A 1 200 ? 28.62000  -10.21800 12.37700  1.000 36.44681  ?  352 GLN   A CG   1 
ATOM   1380 C  CD   . GLN   A 1 200 ? 27.76100  -10.86200 13.43800  1.000 37.92878  ?  352 GLN   A CD   1 
ATOM   1381 O  OE1  . GLN   A 1 200 ? 28.13100  -11.88300 14.01600  1.000 38.42463  ?  352 GLN   A OE1  1 
ATOM   1382 N  NE2  . GLN   A 1 200 ? 26.60300  -10.26800 13.70100  1.000 39.89624  ?  352 GLN   A NE2  1 
ATOM   1383 N  N    . ASP   A 1 201 ? 32.33600  -11.52500 11.33500  1.000 38.98206  ?  353 ASP   A N    1 
ATOM   1384 C  CA   . ASP   A 1 201 ? 33.60800  -11.42900 12.04300  1.000 40.22831  ?  353 ASP   A CA   1 
ATOM   1385 C  C    . ASP   A 1 201 ? 34.54000  -10.42700 11.37300  1.000 45.26415  ?  353 ASP   A C    1 
ATOM   1386 O  O    . ASP   A 1 201 ? 35.29000  -9.71800  12.05300  1.000 42.02214  ?  353 ASP   A O    1 
ATOM   1387 C  CB   . ASP   A 1 201 ? 34.27100  -12.80400 12.12600  1.000 43.98575  ?  353 ASP   A CB   1 
ATOM   1388 C  CG   . ASP   A 1 201 ? 33.58800  -13.72100 13.11800  1.000 46.45626  ?  353 ASP   A CG   1 
ATOM   1389 O  OD1  . ASP   A 1 201 ? 32.68200  -13.24900 13.83600  1.000 55.51535  ?  353 ASP   A OD1  1 
ATOM   1390 O  OD2  . ASP   A 1 201 ? 33.95300  -14.91400 13.17500  1.000 56.87053  ?  353 ASP   A OD2  1 
ATOM   1391 N  N    . ARG   A 1 202 ? 34.51200  -10.35500 10.04000  1.000 43.07793  ?  354 ARG   A N    1 
ATOM   1392 C  CA   . ARG   A 1 202 ? 35.33200  -9.36700  9.34100   1.000 51.58026  ?  354 ARG   A CA   1 
ATOM   1393 C  C    . ARG   A 1 202 ? 34.83600  -7.95500  9.61700   1.000 49.01017  ?  354 ARG   A C    1 
ATOM   1394 O  O    . ARG   A 1 202 ? 35.63900  -7.03300  9.80400   1.000 46.13777  ?  354 ARG   A O    1 
ATOM   1395 C  CB   . ARG   A 1 202 ? 35.34400  -9.63500  7.83200   1.000 56.39186  ?  354 ARG   A CB   1 
ATOM   1396 C  CG   . ARG   A 1 202 ? 36.30100  -10.72400 7.33000   1.000 75.08088  ?  354 ARG   A CG   1 
ATOM   1397 C  CD   . ARG   A 1 202 ? 36.17300  -12.00700 8.13200   1.000 86.59529  ?  354 ARG   A CD   1 
ATOM   1398 N  NE   . ARG   A 1 202 ? 36.80000  -13.18000 7.53300   1.000 98.30043  ?  354 ARG   A NE   1 
ATOM   1399 C  CZ   . ARG   A 1 202 ? 36.44900  -13.71700 6.36700   1.000 105.13869 ?  354 ARG   A CZ   1 
ATOM   1400 N  NH1  . ARG   A 1 202 ? 35.47800  -13.19000 5.63400   1.000 100.68028 ?  354 ARG   A NH1  1 
ATOM   1401 N  NH2  . ARG   A 1 202 ? 37.08300  -14.79300 5.92900   1.000 109.12757 ?  354 ARG   A NH2  1 
ATOM   1402 N  N    . LEU   A 1 203 ? 33.51500  -7.76400  9.63500   1.000 45.02322  ?  355 LEU   A N    1 
ATOM   1403 C  CA   . LEU   A 1 203 ? 32.96300  -6.46500  10.00600  1.000 41.43146  ?  355 LEU   A CA   1 
ATOM   1404 C  C    . LEU   A 1 203 ? 33.22800  -6.15900  11.47500  1.000 39.93969  ?  355 LEU   A C    1 
ATOM   1405 O  O    . LEU   A 1 203 ? 33.52800  -5.01300  11.83000  1.000 39.84169  ?  355 LEU   A O    1 
ATOM   1406 C  CB   . LEU   A 1 203 ? 31.46400  -6.42500  9.70800   1.000 33.86617  ?  355 LEU   A CB   1 
ATOM   1407 C  CG   . LEU   A 1 203 ? 31.03100  -6.75900  8.28000   1.000 35.88816  ?  355 LEU   A CG   1 
ATOM   1408 C  CD1  . LEU   A 1 203 ? 29.52700  -6.82700  8.19600   1.000 35.50137  ?  355 LEU   A CD1  1 
ATOM   1409 C  CD2  . LEU   A 1 203 ? 31.56000  -5.73000  7.30500   1.000 32.73468  ?  355 LEU   A CD2  1 
ATOM   1410 N  N    . SER   A 1 204 ? 33.12500  -7.17200  12.34000  1.000 34.18754  ?  356 SER   A N    1 
ATOM   1411 C  CA   . SER   A 1 204 ? 33.40600  -6.97600  13.76000  1.000 45.14953  ?  356 SER   A CA   1 
ATOM   1412 C  C    . SER   A 1 204 ? 34.84300  -6.52300  13.97700  1.000 43.71355  ?  356 SER   A C    1 
ATOM   1413 O  O    . SER   A 1 204 ? 35.09800  -5.54900  14.69500  1.000 45.35342  ?  356 SER   A O    1 
ATOM   1414 C  CB   . SER   A 1 204 ? 33.13300  -8.26600  14.53400  1.000 50.30788  ?  356 SER   A CB   1 
ATOM   1415 O  OG   . SER   A 1 204 ? 31.82000  -8.28200  15.06300  1.000 69.75923  ?  356 SER   A OG   1 
ATOM   1416 N  N    A ASN   A 1 205 ? 35.80000  -7.22800  13.36500  0.530 40.95947  ?  357 ASN   A N    1 
ATOM   1417 N  N    B ASN   A 1 205 ? 35.80000  -7.22100  13.36100  0.470 41.22633  ?  357 ASN   A N    1 
ATOM   1418 C  CA   A ASN   A 1 205 ? 37.20400  -6.86200  13.51400  0.530 45.39523  ?  357 ASN   A CA   1 
ATOM   1419 C  CA   B ASN   A 1 205 ? 37.20300  -6.85300  13.52600  0.470 45.34894  ?  357 ASN   A CA   1 
ATOM   1420 C  C    A ASN   A 1 205 ? 37.48100  -5.48500  12.92400  0.530 44.22972  ?  357 ASN   A C    1 
ATOM   1421 C  C    B ASN   A 1 205 ? 37.49000  -5.48500  12.92000  0.470 44.12858  ?  357 ASN   A C    1 
ATOM   1422 O  O    A ASN   A 1 205 ? 38.26500  -4.70900  13.48200  0.530 42.97532  ?  357 ASN   A O    1 
ATOM   1423 O  O    B ASN   A 1 205 ? 38.29000  -4.71400  13.46200  0.470 43.41679  ?  357 ASN   A O    1 
ATOM   1424 C  CB   A ASN   A 1 205 ? 38.09200  -7.91500  12.85300  0.530 49.27143  ?  357 ASN   A CB   1 
ATOM   1425 C  CB   B ASN   A 1 205 ? 38.10100  -7.91900  12.90400  0.470 49.41198  ?  357 ASN   A CB   1 
ATOM   1426 C  CG   A ASN   A 1 205 ? 37.92300  -9.28700  13.47100  0.530 53.38569  ?  357 ASN   A CG   1 
ATOM   1427 C  CG   B ASN   A 1 205 ? 38.41000  -9.04800  13.86400  0.470 53.89322  ?  357 ASN   A CG   1 
ATOM   1428 O  OD1  A ASN   A 1 205 ? 37.62100  -9.41200  14.65800  0.530 52.88946  ?  357 ASN   A OD1  1 
ATOM   1429 O  OD1  B ASN   A 1 205 ? 37.58600  -9.93700  14.08300  0.470 56.17059  ?  357 ASN   A OD1  1 
ATOM   1430 N  ND2  A ASN   A 1 205 ? 38.11300  -10.32700 12.66600  0.530 56.10520  ?  357 ASN   A ND2  1 
ATOM   1431 N  ND2  B ASN   A 1 205 ? 39.60200  -9.01600  14.45200  0.470 54.64724  ?  357 ASN   A ND2  1 
ATOM   1432 N  N    . THR   A 1 206 ? 36.84800  -5.16800  11.79200  1.000 39.00764  ?  358 THR   A N    1 
ATOM   1433 C  CA   . THR   A 1 206 ? 36.99800  -3.84000  11.20600  1.000 39.48165  ?  358 THR   A CA   1 
ATOM   1434 C  C    . THR   A 1 206 ? 36.49800  -2.76400  12.16200  1.000 42.74322  ?  358 THR   A C    1 
ATOM   1435 O  O    . THR   A 1 206 ? 37.13500  -1.71400  12.31900  1.000 46.67479  ?  358 THR   A O    1 
ATOM   1436 C  CB   . THR   A 1 206 ? 36.24000  -3.76300  9.87800   1.000 37.83782  ?  358 THR   A CB   1 
ATOM   1437 O  OG1  . THR   A 1 206 ? 36.76500  -4.73400  8.96500   1.000 41.84344  ?  358 THR   A OG1  1 
ATOM   1438 C  CG2  . THR   A 1 206 ? 36.36700  -2.37900  9.26800   1.000 36.59751  ?  358 THR   A CG2  1 
ATOM   1439 N  N    . LEU   A 1 207 ? 35.36400  -3.01400  12.82000  1.000 33.50043  ?  359 LEU   A N    1 
ATOM   1440 C  CA   . LEU   A 1 207 ? 34.82900  -2.04400  13.76800  1.000 41.66664  ?  359 LEU   A CA   1 
ATOM   1441 C  C    . LEU   A 1 207 ? 35.74000  -1.90000  14.98100  1.000 46.77451  ?  359 LEU   A C    1 
ATOM   1442 O  O    . LEU   A 1 207 ? 36.05000  -0.78100  15.40500  1.000 42.39554  ?  359 LEU   A O    1 
ATOM   1443 C  CB   . LEU   A 1 207 ? 33.42100  -2.45200  14.19600  1.000 37.17100  ?  359 LEU   A CB   1 
ATOM   1444 C  CG   . LEU   A 1 207 ? 32.73500  -1.53900  15.21300  1.000 33.83632  ?  359 LEU   A CG   1 
ATOM   1445 C  CD1  . LEU   A 1 207 ? 32.69400  -0.10200  14.71300  1.000 29.15008  ?  359 LEU   A CD1  1 
ATOM   1446 C  CD2  . LEU   A 1 207 ? 31.33200  -2.04600  15.52800  1.000 31.63261  ?  359 LEU   A CD2  1 
ATOM   1447 N  N    . GLN   A 1 208 ? 36.17300  -3.02500  15.55700  1.000 44.85226  ?  360 GLN   A N    1 
ATOM   1448 C  CA   . GLN   A 1 208 ? 37.07500  -2.97300  16.70400  1.000 49.08195  ?  360 GLN   A CA   1 
ATOM   1449 C  C    . GLN   A 1 208 ? 38.34400  -2.20400  16.36500  1.000 48.09892  ?  360 GLN   A C    1 
ATOM   1450 O  O    . GLN   A 1 208 ? 38.75400  -1.30300  17.10400  1.000 48.70004  ?  360 GLN   A O    1 
ATOM   1451 C  CB   . GLN   A 1 208 ? 37.42000  -4.38600  17.17400  1.000 51.55306  ?  360 GLN   A CB   1 
ATOM   1452 C  CG   . GLN   A 1 208 ? 36.25400  -5.15400  17.76400  1.000 62.75059  ?  360 GLN   A CG   1 
ATOM   1453 C  CD   . GLN   A 1 208 ? 36.56900  -6.62400  17.95700  1.000 71.96261  ?  360 GLN   A CD   1 
ATOM   1454 O  OE1  . GLN   A 1 208 ? 35.68400  -7.47600  17.88100  1.000 75.16726  ?  360 GLN   A OE1  1 
ATOM   1455 N  NE2  . GLN   A 1 208 ? 37.83700  -6.93000  18.20700  1.000 76.05262  ?  360 GLN   A NE2  1 
ATOM   1456 N  N    . THR   A 1 209 ? 38.97100  -2.53800  15.23600  1.000 50.23166  ?  361 THR   A N    1 
ATOM   1457 C  CA   . THR   A 1 209 ? 40.20700  -1.86600  14.85300  1.000 46.46248  ?  361 THR   A CA   1 
ATOM   1458 C  C    . THR   A 1 209 ? 39.96500  -0.39600  14.53400  1.000 51.30039  ?  361 THR   A C    1 
ATOM   1459 O  O    . THR   A 1 209 ? 40.82100  0.45000   14.81500  1.000 46.87199  ?  361 THR   A O    1 
ATOM   1460 C  CB   . THR   A 1 209 ? 40.84500  -2.58200  13.66400  1.000 46.61808  ?  361 THR   A CB   1 
ATOM   1461 O  OG1  . THR   A 1 209 ? 40.99500  -3.97400  13.97200  1.000 52.28072  ?  361 THR   A OG1  1 
ATOM   1462 C  CG2  . THR   A 1 209 ? 42.21300  -1.99400  13.35900  1.000 43.76082  ?  361 THR   A CG2  1 
ATOM   1463 N  N    . TYR   A 1 210 ? 38.80400  -0.06700  13.95600  1.000 41.24998  ?  362 TYR   A N    1 
ATOM   1464 C  CA   . TYR   A 1 210 ? 38.49100  1.33800   13.71000  1.000 37.58227  ?  362 TYR   A CA   1 
ATOM   1465 C  C    . TYR   A 1 210 ? 38.39400  2.11500   15.01500  1.000 38.75051  ?  362 TYR   A C    1 
ATOM   1466 O  O    . TYR   A 1 210 ? 38.87300  3.25200   15.10700  1.000 46.58082  ?  362 TYR   A O    1 
ATOM   1467 C  CB   . TYR   A 1 210 ? 37.18600  1.48800   12.92300  1.000 39.46043  ?  362 TYR   A CB   1 
ATOM   1468 C  CG   . TYR   A 1 210 ? 36.84300  2.94500   12.67200  1.000 43.92086  ?  362 TYR   A CG   1 
ATOM   1469 C  CD1  . TYR   A 1 210 ? 36.04900  3.66000   13.56300  1.000 40.42264  ?  362 TYR   A CD1  1 
ATOM   1470 C  CD2  . TYR   A 1 210 ? 37.34600  3.61500   11.56300  1.000 43.99731  ?  362 TYR   A CD2  1 
ATOM   1471 C  CE1  . TYR   A 1 210 ? 35.75600  4.99500   13.34900  1.000 39.72996  ?  362 TYR   A CE1  1 
ATOM   1472 C  CE2  . TYR   A 1 210 ? 37.05100  4.94800   11.33800  1.000 43.83592  ?  362 TYR   A CE2  1 
ATOM   1473 C  CZ   . TYR   A 1 210 ? 36.25800  5.63200   12.23400  1.000 42.98636  ?  362 TYR   A CZ   1 
ATOM   1474 O  OH   . TYR   A 1 210 ? 35.96700  6.95900   12.01400  1.000 45.61306  ?  362 TYR   A OH   1 
ATOM   1475 N  N    . ILE   A 1 211 ? 37.75800  1.52900   16.03000  1.000 40.60251  ?  363 ILE   A N    1 
ATOM   1476 C  CA   . ILE   A 1 211 ? 37.60300  2.22600   17.30200  1.000 41.90663  ?  363 ILE   A CA   1 
ATOM   1477 C  C    . ILE   A 1 211 ? 38.96100  2.44700   17.95900  1.000 47.56974  ?  363 ILE   A C    1 
ATOM   1478 O  O    . ILE   A 1 211 ? 39.25200  3.54300   18.45600  1.000 47.67142  ?  363 ILE   A O    1 
ATOM   1479 C  CB   . ILE   A 1 211 ? 36.63800  1.45100   18.21700  1.000 42.49553  ?  363 ILE   A CB   1 
ATOM   1480 C  CG1  . ILE   A 1 211 ? 35.23300  1.42800   17.60200  1.000 44.69813  ?  363 ILE   A CG1  1 
ATOM   1481 C  CG2  . ILE   A 1 211 ? 36.60300  2.07100   19.60400  1.000 38.25886  ?  363 ILE   A CG2  1 
ATOM   1482 C  CD1  . ILE   A 1 211 ? 34.24600  0.55200   18.34400  1.000 39.45842  ?  363 ILE   A CD1  1 
ATOM   1483 N  N    . ARG   A 1 212 ? 39.82200  1.42400   17.95400  1.000 48.72681  ?  364 ARG   A N    1 
ATOM   1484 C  CA   . ARG   A 1 212 ? 41.14500  1.56700   18.55800  1.000 58.31382  ?  364 ARG   A CA   1 
ATOM   1485 C  C    . ARG   A 1 212 ? 41.97000  2.63500   17.85100  1.000 62.93107  ?  364 ARG   A C    1 
ATOM   1486 O  O    . ARG   A 1 212 ? 42.61400  3.46600   18.50200  1.000 63.96990  ?  364 ARG   A O    1 
ATOM   1487 C  CB   . ARG   A 1 212 ? 41.89700  0.23500   18.52700  1.000 66.42563  ?  364 ARG   A CB   1 
ATOM   1488 C  CG   . ARG   A 1 212 ? 41.12700  -0.96400  19.04300  1.000 68.33765  ?  364 ARG   A CG   1 
ATOM   1489 C  CD   . ARG   A 1 212 ? 42.03200  -2.18600  19.14300  1.000 76.81535  ?  364 ARG   A CD   1 
ATOM   1490 N  NE   . ARG   A 1 212 ? 41.35600  -3.31800  19.77100  1.000 86.36366  ?  364 ARG   A NE   1 
ATOM   1491 C  CZ   . ARG   A 1 212 ? 41.15400  -4.49100  19.17800  1.000 92.16982  ?  364 ARG   A CZ   1 
ATOM   1492 N  NH1  . ARG   A 1 212 ? 41.57800  -4.69400  17.93700  1.000 92.03686  ?  364 ARG   A NH1  1 
ATOM   1493 N  NH2  . ARG   A 1 212 ? 40.52700  -5.46300  19.82600  1.000 95.82592  ?  364 ARG   A NH2  1 
ATOM   1494 N  N    . CYS   A 1 213 ? 41.95700  2.62900   16.51900  1.000 62.10076  ?  365 CYS   A N    1 
ATOM   1495 C  CA   . CYS   A 1 213 ? 42.88100  3.43000   15.72800  1.000 71.51967  ?  365 CYS   A CA   1 
ATOM   1496 C  C    . CYS   A 1 213 ? 42.32400  4.79000   15.32300  1.000 69.66856  ?  365 CYS   A C    1 
ATOM   1497 O  O    . CYS   A 1 213 ? 43.10900  5.71800   15.09800  1.000 74.62513  ?  365 CYS   A O    1 
ATOM   1498 C  CB   . CYS   A 1 213 ? 43.30100  2.64100   14.47700  1.000 77.25039  ?  365 CYS   A CB   1 
ATOM   1499 S  SG   . CYS   A 1 213 ? 43.88100  3.59800   13.05500  1.000 90.21108  ?  365 CYS   A SG   1 
ATOM   1500 N  N    . ARG   A 1 214 ? 41.00200  4.95100   15.25200  1.000 62.62559  ?  366 ARG   A N    1 
ATOM   1501 C  CA   . ARG   A 1 214 ? 40.42300  6.18900   14.75200  1.000 56.75096  ?  366 ARG   A CA   1 
ATOM   1502 C  C    . ARG   A 1 214 ? 39.49400  6.90500   15.72200  1.000 51.15843  ?  366 ARG   A C    1 
ATOM   1503 O  O    . ARG   A 1 214 ? 39.27600  8.10800   15.55000  1.000 57.47335  ?  366 ARG   A O    1 
ATOM   1504 C  CB   . ARG   A 1 214 ? 39.65800  5.93400   13.44300  1.000 55.75260  ?  366 ARG   A CB   1 
ATOM   1505 C  CG   . ARG   A 1 214 ? 40.50900  5.32500   12.33800  1.000 61.10211  ?  366 ARG   A CG   1 
ATOM   1506 C  CD   . ARG   A 1 214 ? 41.23400  6.39600   11.53200  1.000 68.44748  ?  366 ARG   A CD   1 
ATOM   1507 N  NE   . ARG   A 1 214 ? 41.80800  5.85700   10.30100  1.000 80.93460  ?  366 ARG   A NE   1 
ATOM   1508 C  CZ   . ARG   A 1 214 ? 41.17300  5.81500   9.13300   1.000 84.18288  ?  366 ARG   A CZ   1 
ATOM   1509 N  NH1  . ARG   A 1 214 ? 39.93600  6.28500   9.03000   1.000 86.00824  ?  366 ARG   A NH1  1 
ATOM   1510 N  NH2  . ARG   A 1 214 ? 41.77400  5.30400   8.06700   1.000 86.37076  ?  366 ARG   A NH2  1 
ATOM   1511 N  N    . HIS   A 1 215 ? 38.93900  6.22200   16.72200  1.000 47.70595  ?  367 HIS   A N    1 
ATOM   1512 C  CA   . HIS   A 1 215 ? 38.06400  6.89200   17.67500  1.000 49.30605  ?  367 HIS   A CA   1 
ATOM   1513 C  C    . HIS   A 1 215 ? 38.88100  7.39000   18.85800  1.000 57.56981  ?  367 HIS   A C    1 
ATOM   1514 O  O    . HIS   A 1 215 ? 39.46400  6.57200   19.58100  1.000 62.42491  ?  367 HIS   A O    1 
ATOM   1515 C  CB   . HIS   A 1 215 ? 36.96000  5.96600   18.15600  1.000 45.29550  ?  367 HIS   A CB   1 
ATOM   1516 C  CG   . HIS   A 1 215 ? 35.74400  6.69400   18.64000  1.000 44.04937  ?  367 HIS   A CG   1 
ATOM   1517 N  ND1  . HIS   A 1 215 ? 34.53500  6.64800   17.98000  1.000 41.38390  ?  367 HIS   A ND1  1 
ATOM   1518 C  CD2  . HIS   A 1 215 ? 35.55900  7.50600   19.70800  1.000 44.07079  ?  367 HIS   A CD2  1 
ATOM   1519 C  CE1  . HIS   A 1 215 ? 33.65500  7.39200   18.62700  1.000 42.66278  ?  367 HIS   A CE1  1 
ATOM   1520 N  NE2  . HIS   A 1 215 ? 34.25100  7.92300   19.67900  1.000 45.23994  ?  367 HIS   A NE2  1 
ATOM   1521 N  N    . PRO   A 1 216 ? 38.94800  8.69600   19.09500  1.000 55.69595  ?  368 PRO   A N    1 
ATOM   1522 C  CA   . PRO   A 1 216 ? 39.80100  9.21700   20.16500  1.000 64.01015  ?  368 PRO   A CA   1 
ATOM   1523 C  C    . PRO   A 1 216 ? 39.13300  9.06700   21.52000  1.000 60.15593  ?  368 PRO   A C    1 
ATOM   1524 O  O    . PRO   A 1 216 ? 37.90400  9.18300   21.63500  1.000 54.17073  ?  368 PRO   A O    1 
ATOM   1525 C  CB   . PRO   A 1 216 ? 39.96600  10.69500  19.78700  1.000 68.04960  ?  368 PRO   A CB   1 
ATOM   1526 C  CG   . PRO   A 1 216 ? 38.68200  11.02500  19.08600  1.000 58.31626  ?  368 PRO   A CG   1 
ATOM   1527 C  CD   . PRO   A 1 216 ? 38.26900  9.77300   18.35000  1.000 47.75821  ?  368 PRO   A CD   1 
ATOM   1528 N  N    . PRO   A 1 217 ? 39.91100  8.79300   22.57200  1.000 61.88848  ?  369 PRO   A N    1 
ATOM   1529 C  CA   . PRO   A 1 217 ? 39.34000  8.83100   23.91700  1.000 50.90367  ?  369 PRO   A CA   1 
ATOM   1530 C  C    . PRO   A 1 217 ? 38.93100  10.24800  24.27000  1.000 56.20170  ?  369 PRO   A C    1 
ATOM   1531 O  O    . PRO   A 1 217 ? 39.47200  11.22000  23.71700  1.000 66.44420  ?  369 PRO   A O    1 
ATOM   1532 C  CB   . PRO   A 1 217 ? 40.50100  8.33700   24.80400  1.000 52.21092  ?  369 PRO   A CB   1 
ATOM   1533 C  CG   . PRO   A 1 217 ? 41.73000  8.63700   24.02200  1.000 59.72494  ?  369 PRO   A CG   1 
ATOM   1534 C  CD   . PRO   A 1 217 ? 41.34600  8.46800   22.57800  1.000 68.77538  ?  369 PRO   A CD   1 
ATOM   1535 N  N    . PRO   A 1 218 ? 37.97200  10.41900  25.19300  1.000 58.90222  ?  370 PRO   A N    1 
ATOM   1536 C  CA   . PRO   A 1 218 ? 37.31900  9.39900   26.01900  1.000 58.83603  ?  370 PRO   A CA   1 
ATOM   1537 C  C    . PRO   A 1 218 ? 36.09800  8.73100   25.38700  1.000 55.69003  ?  370 PRO   A C    1 
ATOM   1538 O  O    . PRO   A 1 218 ? 35.47200  7.89500   26.03700  1.000 57.50874  ?  370 PRO   A O    1 
ATOM   1539 C  CB   . PRO   A 1 218 ? 36.89700  10.19200  27.25200  1.000 67.20315  ?  370 PRO   A CB   1 
ATOM   1540 C  CG   . PRO   A 1 218 ? 36.57800  11.54700  26.70700  1.000 66.99143  ?  370 PRO   A CG   1 
ATOM   1541 C  CD   . PRO   A 1 218 ? 37.47600  11.77100  25.51000  1.000 65.54102  ?  370 PRO   A CD   1 
ATOM   1542 N  N    . GLY   A 1 219 ? 35.75800  9.09300   24.15000  1.000 49.91342  ?  371 GLY   A N    1 
ATOM   1543 C  CA   . GLY   A 1 219 ? 34.62300  8.46100   23.49900  1.000 54.31446  ?  371 GLY   A CA   1 
ATOM   1544 C  C    . GLY   A 1 219 ? 34.85600  7.00200   23.15800  1.000 52.65760  ?  371 GLY   A C    1 
ATOM   1545 O  O    . GLY   A 1 219 ? 33.90600  6.22400   23.04400  1.000 52.44652  ?  371 GLY   A O    1 
ATOM   1546 N  N    . SER   A 1 220 ? 36.10800  6.60900   22.98400  1.000 55.21375  ?  372 SER   A N    1 
ATOM   1547 C  CA   . SER   A 1 220 ? 36.42000  5.24200   22.60300  1.000 56.50114  ?  372 SER   A CA   1 
ATOM   1548 C  C    . SER   A 1 220 ? 36.14200  4.23400   23.70900  1.000 54.83064  ?  372 SER   A C    1 
ATOM   1549 O  O    . SER   A 1 220 ? 36.07500  3.03200   23.42800  1.000 50.86987  ?  372 SER   A O    1 
ATOM   1550 C  CB   . SER   A 1 220 ? 37.88200  5.13900   22.21200  1.000 70.82504  ?  372 SER   A CB   1 
ATOM   1551 O  OG   . SER   A 1 220 ? 38.32900  6.30100   21.54300  1.000 85.98371  ?  372 SER   A OG   1 
ATOM   1552 N  N    . HIS   A 1 221 ? 35.98000  4.69300   24.94900  1.000 54.77111  ?  373 HIS   A N    1 
ATOM   1553 C  CA   . HIS   A 1 221 ? 35.96500  3.80900   26.10800  1.000 50.54089  ?  373 HIS   A CA   1 
ATOM   1554 C  C    . HIS   A 1 221 ? 34.85400  2.77000   26.03100  1.000 48.54176  ?  373 HIS   A C    1 
ATOM   1555 O  O    . HIS   A 1 221 ? 33.66900  3.11400   26.09000  1.000 52.70607  ?  373 HIS   A O    1 
ATOM   1556 C  CB   . HIS   A 1 221 ? 35.82000  4.61500   27.39700  1.000 49.66326  ?  373 HIS   A CB   1 
ATOM   1557 C  CG   . HIS   A 1 221 ? 35.66500  3.76000   28.61900  1.000 58.66516  ?  373 HIS   A CG   1 
ATOM   1558 N  ND1  . HIS   A 1 221 ? 36.63400  2.87200   29.03500  1.000 57.23538  ?  373 HIS   A ND1  1 
ATOM   1559 C  CD2  . HIS   A 1 221 ? 34.64600  3.64500   29.50500  1.000 62.58249  ?  373 HIS   A CD2  1 
ATOM   1560 C  CE1  . HIS   A 1 221 ? 36.22400  2.25300   30.12800  1.000 62.92564  ?  373 HIS   A CE1  1 
ATOM   1561 N  NE2  . HIS   A 1 221 ? 35.02000  2.70400   30.43400  1.000 64.52080  ?  373 HIS   A NE2  1 
ATOM   1562 N  N    . GLN   A 1 222 ? 35.23700  1.49500   25.92300  1.000 54.22572  ?  374 GLN   A N    1 
ATOM   1563 C  CA   . GLN   A 1 222 ? 34.29100  0.38100   25.87000  1.000 46.25286  ?  374 GLN   A CA   1 
ATOM   1564 C  C    . GLN   A 1 222 ? 33.26800  0.56600   24.75400  1.000 40.21786  ?  374 GLN   A C    1 
ATOM   1565 O  O    . GLN   A 1 222 ? 32.13600  0.08700   24.85100  1.000 37.33557  ?  374 GLN   A O    1 
ATOM   1566 C  CB   . GLN   A 1 222 ? 33.58100  0.19200   27.21500  1.000 50.35810  ?  374 GLN   A CB   1 
ATOM   1567 C  CG   . GLN   A 1 222 ? 34.47800  -0.32700  28.32400  1.000 63.25350  ?  374 GLN   A CG   1 
ATOM   1568 C  CD   . GLN   A 1 222 ? 34.63400  -1.82900  28.27600  1.000 81.26420  ?  374 GLN   A CD   1 
ATOM   1569 O  OE1  . GLN   A 1 222 ? 35.67700  -2.34600  27.87400  1.000 88.20213  ?  374 GLN   A OE1  1 
ATOM   1570 N  NE2  . GLN   A 1 222 ? 33.58900  -2.54300  28.67600  1.000 84.19233  ?  374 GLN   A NE2  1 
ATOM   1571 N  N    . LEU   A 1 223 ? 33.66400  1.27000   23.69100  1.000 40.43946  ?  375 LEU   A N    1 
ATOM   1572 C  CA   . LEU   A 1 223 ? 32.71900  1.60100   22.63100  1.000 41.10266  ?  375 LEU   A CA   1 
ATOM   1573 C  C    . LEU   A 1 223 ? 32.19300  0.34700   21.94900  1.000 41.49601  ?  375 LEU   A C    1 
ATOM   1574 O  O    . LEU   A 1 223 ? 30.99000  0.23500   21.68700  1.000 41.30097  ?  375 LEU   A O    1 
ATOM   1575 C  CB   . LEU   A 1 223 ? 33.37100  2.53300   21.61300  1.000 38.68700  ?  375 LEU   A CB   1 
ATOM   1576 C  CG   . LEU   A 1 223 ? 32.41200  3.10500   20.56400  1.000 37.96960  ?  375 LEU   A CG   1 
ATOM   1577 C  CD1  . LEU   A 1 223 ? 31.10100  3.56900   21.19400  1.000 35.16874  ?  375 LEU   A CD1  1 
ATOM   1578 C  CD2  . LEU   A 1 223 ? 33.07300  4.23600   19.80200  1.000 46.99900  ?  375 LEU   A CD2  1 
ATOM   1579 N  N    . TYR   A 1 224 ? 33.07600  -0.61300  21.65900  1.000 46.28533  ?  376 TYR   A N    1 
ATOM   1580 C  CA   . TYR   A 1 224 ? 32.63000  -1.85500  21.03500  1.000 49.74531  ?  376 TYR   A CA   1 
ATOM   1581 C  C    . TYR   A 1 224 ? 31.63900  -2.58800  21.92800  1.000 42.55834  ?  376 TYR   A C    1 
ATOM   1582 O  O    . TYR   A 1 224 ? 30.59200  -3.05400  21.46300  1.000 46.84366  ?  376 TYR   A O    1 
ATOM   1583 C  CB   . TYR   A 1 224 ? 33.82100  -2.75700  20.71200  1.000 50.52894  ?  376 TYR   A CB   1 
ATOM   1584 C  CG   . TYR   A 1 224 ? 33.42000  -3.98700  19.92900  1.000 54.20963  ?  376 TYR   A CG   1 
ATOM   1585 C  CD1  . TYR   A 1 224 ? 32.92900  -3.87500  18.63400  1.000 41.37048  ?  376 TYR   A CD1  1 
ATOM   1586 C  CD2  . TYR   A 1 224 ? 33.50300  -5.25600  20.49000  1.000 53.85371  ?  376 TYR   A CD2  1 
ATOM   1587 C  CE1  . TYR   A 1 224 ? 32.55200  -4.98800  17.91400  1.000 44.03401  ?  376 TYR   A CE1  1 
ATOM   1588 C  CE2  . TYR   A 1 224 ? 33.12400  -6.38000  19.77500  1.000 49.92745  ?  376 TYR   A CE2  1 
ATOM   1589 C  CZ   . TYR   A 1 224 ? 32.64900  -6.23600  18.48600  1.000 50.39528  ?  376 TYR   A CZ   1 
ATOM   1590 O  OH   . TYR   A 1 224 ? 32.26600  -7.33900  17.75800  1.000 57.78709  ?  376 TYR   A OH   1 
ATOM   1591 N  N    . ALA   A 1 225 ? 31.95400  -2.69800  23.22000  1.000 38.54844  ?  377 ALA   A N    1 
ATOM   1592 C  CA   . ALA   A 1 225 ? 31.04200  -3.35400  24.15200  1.000 39.73504  ?  377 ALA   A CA   1 
ATOM   1593 C  C    . ALA   A 1 225 ? 29.68900  -2.65500  24.18500  1.000 40.30210  ?  377 ALA   A C    1 
ATOM   1594 O  O    . ALA   A 1 225 ? 28.64200  -3.31300  24.19700  1.000 50.70913  ?  377 ALA   A O    1 
ATOM   1595 C  CB   . ALA   A 1 225 ? 31.65900  -3.39400  25.55000  1.000 37.34899  ?  377 ALA   A CB   1 
ATOM   1596 N  N    . LYS   A 1 226 ? 29.69000  -1.32100  24.19700  1.000 39.76769  ?  378 LYS   A N    1 
ATOM   1597 C  CA   . LYS   A 1 226 ? 28.42900  -0.58700  24.20100  1.000 35.58046  ?  378 LYS   A CA   1 
ATOM   1598 C  C    . LYS   A 1 226 ? 27.67000  -0.78800  22.89400  1.000 39.46868  ?  378 LYS   A C    1 
ATOM   1599 O  O    . LYS   A 1 226 ? 26.43800  -0.90000  22.89700  1.000 40.42393  ?  378 LYS   A O    1 
ATOM   1600 C  CB   . LYS   A 1 226 ? 28.68400  0.90000   24.45100  1.000 34.14535  ?  378 LYS   A CB   1 
ATOM   1601 C  CG   . LYS   A 1 226 ? 29.21300  1.23500   25.84200  1.000 40.09265  ?  378 LYS   A CG   1 
ATOM   1602 C  CD   . LYS   A 1 226 ? 29.73400  2.66700   25.89000  1.000 47.65067  ?  378 LYS   A CD   1 
ATOM   1603 C  CE   . LYS   A 1 226 ? 29.98900  3.13300   27.31600  1.000 52.72655  ?  378 LYS   A CE   1 
ATOM   1604 N  NZ   . LYS   A 1 226 ? 30.94800  2.24500   28.02100  1.000 57.53750  ?  378 LYS   A NZ   1 
ATOM   1605 N  N    . MET   A 1 227 ? 28.38900  -0.84600  21.76900  1.000 38.69677  ?  379 MET   A N    1 
ATOM   1606 C  CA   . MET   A 1 227 ? 27.73300  -1.01700  20.47600  1.000 39.73799  ?  379 MET   A CA   1 
ATOM   1607 C  C    . MET   A 1 227 ? 27.11200  -2.40300  20.34800  1.000 38.11950  ?  379 MET   A C    1 
ATOM   1608 O  O    . MET   A 1 227 ? 26.01600  -2.54800  19.79600  1.000 38.55036  ?  379 MET   A O    1 
ATOM   1609 C  CB   . MET   A 1 227 ? 28.73000  -0.76800  19.34300  1.000 37.27812  ?  379 MET   A CB   1 
ATOM   1610 C  CG   . MET   A 1 227 ? 29.11600  0.69300   19.16300  1.000 36.38919  ?  379 MET   A CG   1 
ATOM   1611 S  SD   . MET   A 1 227 ? 30.32200  0.93600   17.84300  1.000 38.40834  ?  379 MET   A SD   1 
ATOM   1612 C  CE   . MET   A 1 227 ? 29.25800  0.82000   16.40900  1.000 33.60167  ?  379 MET   A CE   1 
ATOM   1613 N  N    . ILE   A 1 228 ? 27.80000  -3.43400  20.84200  1.000 33.50725  ?  380 ILE   A N    1 
ATOM   1614 C  CA   . ILE   A 1 228 ? 27.23900  -4.78100  20.80400  1.000 40.48085  ?  380 ILE   A CA   1 
ATOM   1615 C  C    . ILE   A 1 228 ? 26.04600  -4.88700  21.74700  1.000 46.65307  ?  380 ILE   A C    1 
ATOM   1616 O  O    . ILE   A 1 228 ? 25.07200  -5.59600  21.46200  1.000 44.61758  ?  380 ILE   A O    1 
ATOM   1617 C  CB   . ILE   A 1 228 ? 28.32500  -5.82000  21.13600  1.000 50.00114  ?  380 ILE   A CB   1 
ATOM   1618 C  CG1  . ILE   A 1 228 ? 29.47500  -5.72100  20.13400  1.000 42.38666  ?  380 ILE   A CG1  1 
ATOM   1619 C  CG2  . ILE   A 1 228 ? 27.74700  -7.22500  21.12700  1.000 58.03754  ?  380 ILE   A CG2  1 
ATOM   1620 C  CD1  . ILE   A 1 228 ? 29.06300  -5.97800  18.70500  1.000 51.57338  ?  380 ILE   A CD1  1 
ATOM   1621 N  N    . GLN   A 1 229 ? 26.09900  -4.18100  22.88100  1.000 43.94936  ?  381 GLN   A N    1 
ATOM   1622 C  CA   . GLN   A 1 229 ? 24.94000  -4.11600  23.76400  1.000 44.03908  ?  381 GLN   A CA   1 
ATOM   1623 C  C    . GLN   A 1 229 ? 23.73000  -3.54300  23.03700  1.000 45.00222  ?  381 GLN   A C    1 
ATOM   1624 O  O    . GLN   A 1 229 ? 22.59000  -3.95200  23.29300  1.000 41.51861  ?  381 GLN   A O    1 
ATOM   1625 C  CB   . GLN   A 1 229 ? 25.26700  -3.28200  25.00200  1.000 45.29526  ?  381 GLN   A CB   1 
ATOM   1626 C  CG   . GLN   A 1 229 ? 24.14300  -3.21100  26.02300  1.000 49.66849  ?  381 GLN   A CG   1 
ATOM   1627 C  CD   . GLN   A 1 229 ? 23.59700  -4.57700  26.39100  1.000 58.89615  ?  381 GLN   A CD   1 
ATOM   1628 O  OE1  . GLN   A 1 229 ? 24.35400  -5.50700  26.67000  1.000 65.66332  ?  381 GLN   A OE1  1 
ATOM   1629 N  NE2  . GLN   A 1 229 ? 22.27500  -4.70600  26.39100  1.000 52.48299  ?  381 GLN   A NE2  1 
ATOM   1630 N  N    A LYS   A 1 230 ? 23.95500  -2.59600  22.12400  0.680 39.66954  ?  382 LYS   A N    1 
ATOM   1631 N  N    B LYS   A 1 230 ? 23.96000  -2.59300  22.12700  0.320 40.17418  ?  382 LYS   A N    1 
ATOM   1632 C  CA   A LYS   A 1 230 ? 22.84600  -2.03800  21.35800  0.680 38.62542  ?  382 LYS   A CA   1 
ATOM   1633 C  CA   B LYS   A 1 230 ? 22.86400  -2.03500  21.34000  0.320 38.39768  ?  382 LYS   A CA   1 
ATOM   1634 C  C    A LYS   A 1 230 ? 22.22200  -3.07700  20.43500  0.680 36.05746  ?  382 LYS   A C    1 
ATOM   1635 C  C    B LYS   A 1 230 ? 22.21700  -3.10000  20.46600  0.320 36.79494  ?  382 LYS   A C    1 
ATOM   1636 O  O    A LYS   A 1 230 ? 21.01400  -3.02900  20.18000  0.680 37.28194  ?  382 LYS   A O    1 
ATOM   1637 O  O    B LYS   A 1 230 ? 20.99700  -3.09400  20.26600  0.320 37.47887  ?  382 LYS   A O    1 
ATOM   1638 C  CB   A LYS   A 1 230 ? 23.31700  -0.82200  20.56100  0.680 37.58303  ?  382 LYS   A CB   1 
ATOM   1639 C  CB   B LYS   A 1 230 ? 23.37100  -0.87500  20.48300  0.320 37.77031  ?  382 LYS   A CB   1 
ATOM   1640 C  CG   A LYS   A 1 230 ? 23.48300  0.43000   21.40700  0.680 41.88354  ?  382 LYS   A CG   1 
ATOM   1641 C  CG   B LYS   A 1 230 ? 23.74000  0.36600   21.27300  0.320 42.16301  ?  382 LYS   A CG   1 
ATOM   1642 C  CD   A LYS   A 1 230 ? 22.20700  0.74300   22.17700  0.680 49.18862  ?  382 LYS   A CD   1 
ATOM   1643 C  CD   B LYS   A 1 230 ? 22.58500  0.81300   22.14900  0.320 48.54132  ?  382 LYS   A CD   1 
ATOM   1644 C  CE   A LYS   A 1 230 ? 22.39900  1.92400   23.11500  0.680 54.36236  ?  382 LYS   A CE   1 
ATOM   1645 C  CE   B LYS   A 1 230 ? 23.06700  1.67000   23.30400  0.320 53.11441  ?  382 LYS   A CE   1 
ATOM   1646 N  NZ   A LYS   A 1 230 ? 23.25100  1.57300   24.28600  0.680 55.70035  ?  382 LYS   A NZ   1 
ATOM   1647 N  NZ   B LYS   A 1 230 ? 21.94800  2.04600   24.21100  0.320 55.33943  ?  382 LYS   A NZ   1 
ATOM   1648 N  N    . LEU   A 1 231 ? 23.02100  -4.02200  19.93200  1.000 38.28489  ?  383 LEU   A N    1 
ATOM   1649 C  CA   . LEU   A 1 231 ? 22.46600  -5.11200  19.13700  1.000 43.92319  ?  383 LEU   A CA   1 
ATOM   1650 C  C    . LEU   A 1 231 ? 21.60200  -6.03100  19.98800  1.000 40.18055  ?  383 LEU   A C    1 
ATOM   1651 O  O    . LEU   A 1 231 ? 20.60400  -6.57200  19.49900  1.000 37.42828  ?  383 LEU   A O    1 
ATOM   1652 C  CB   . LEU   A 1 231 ? 23.59000  -5.90400  18.47000  1.000 44.59207  ?  383 LEU   A CB   1 
ATOM   1653 C  CG   . LEU   A 1 231 ? 24.40400  -5.15000  17.41700  1.000 43.30527  ?  383 LEU   A CG   1 
ATOM   1654 C  CD1  . LEU   A 1 231 ? 25.57000  -5.99700  16.93000  1.000 43.61324  ?  383 LEU   A CD1  1 
ATOM   1655 C  CD2  . LEU   A 1 231 ? 23.51900  -4.72400  16.25400  1.000 35.13897  ?  383 LEU   A CD2  1 
ATOM   1656 N  N    . ALA   A 1 232 ? 21.96900  -6.22000  21.25700  1.000 36.21833  ?  384 ALA   A N    1 
ATOM   1657 C  CA   . ALA   A 1 232 ? 21.11300  -6.97000  22.16900  1.000 41.96437  ?  384 ALA   A CA   1 
ATOM   1658 C  C    . ALA   A 1 232 ? 19.81600  -6.21600  22.43700  1.000 42.99302  ?  384 ALA   A C    1 
ATOM   1659 O  O    . ALA   A 1 232 ? 18.72800  -6.80400  22.40700  1.000 41.95321  ?  384 ALA   A O    1 
ATOM   1660 C  CB   . ALA   A 1 232 ? 21.85600  -7.25300  23.47500  1.000 41.01212  ?  384 ALA   A CB   1 
ATOM   1661 N  N    . ASP   A 1 233 ? 19.91500  -4.90700  22.69500  1.000 36.97555  ?  385 ASP   A N    1 
ATOM   1662 C  CA   . ASP   A 1 233 ? 18.71600  -4.09400  22.88600  1.000 39.57260  ?  385 ASP   A CA   1 
ATOM   1663 C  C    . ASP   A 1 233 ? 17.80500  -4.16300  21.66700  1.000 36.06753  ?  385 ASP   A C    1 
ATOM   1664 O  O    . ASP   A 1 233 ? 16.57700  -4.21200  21.80100  1.000 38.99787  ?  385 ASP   A O    1 
ATOM   1665 C  CB   . ASP   A 1 233 ? 19.09600  -2.64100  23.17300  1.000 37.05049  ?  385 ASP   A CB   1 
ATOM   1666 C  CG   . ASP   A 1 233 ? 20.04300  -2.50300  24.34900  1.000 54.74757  ?  385 ASP   A CG   1 
ATOM   1667 O  OD1  . ASP   A 1 233 ? 20.64100  -1.41500  24.50100  1.000 51.02975  ?  385 ASP   A OD1  1 
ATOM   1668 O  OD2  . ASP   A 1 233 ? 20.18400  -3.47400  25.12300  1.000 47.36047  ?  385 ASP   A OD2  1 
ATOM   1669 N  N    . LEU   A 1 234 ? 18.39400  -4.16800  20.46800  1.000 34.51323  ?  386 LEU   A N    1 
ATOM   1670 C  CA   . LEU   A 1 234 ? 17.59800  -4.24100  19.24800  1.000 38.29354  ?  386 LEU   A CA   1 
ATOM   1671 C  C    . LEU   A 1 234 ? 16.84100  -5.55800  19.16000  1.000 39.05881  ?  386 LEU   A C    1 
ATOM   1672 O  O    . LEU   A 1 234 ? 15.71500  -5.59900  18.65400  1.000 39.82817  ?  386 LEU   A O    1 
ATOM   1673 C  CB   . LEU   A 1 234 ? 18.49700  -4.06300  18.02800  1.000 38.06786  ?  386 LEU   A CB   1 
ATOM   1674 C  CG   . LEU   A 1 234 ? 18.89600  -2.62400  17.72300  1.000 38.71960  ?  386 LEU   A CG   1 
ATOM   1675 C  CD1  . LEU   A 1 234 ? 20.10100  -2.61900  16.80400  1.000 36.70930  ?  386 LEU   A CD1  1 
ATOM   1676 C  CD2  . LEU   A 1 234 ? 17.73100  -1.86300  17.11100  1.000 34.40475  ?  386 LEU   A CD2  1 
ATOM   1677 N  N    . ARG   A 1 235 ? 17.45100  -6.64900  19.63100  1.000 36.03624  ?  387 ARG   A N    1 
ATOM   1678 C  CA   . ARG   A 1 235 ? 16.74000  -7.92300  19.68800  1.000 39.58198  ?  387 ARG   A CA   1 
ATOM   1679 C  C    . ARG   A 1 235 ? 15.48400  -7.80600  20.54100  1.000 39.95871  ?  387 ARG   A C    1 
ATOM   1680 O  O    . ARG   A 1 235 ? 14.41600  -8.30000  20.16100  1.000 42.88973  ?  387 ARG   A O    1 
ATOM   1681 C  CB   . ARG   A 1 235 ? 17.65700  -9.01700  20.23400  1.000 40.06240  ?  387 ARG   A CB   1 
ATOM   1682 C  CG   . ARG   A 1 235 ? 18.87300  -9.29300  19.37700  1.000 41.44896  ?  387 ARG   A CG   1 
ATOM   1683 C  CD   . ARG   A 1 235 ? 18.47400  -9.71800  17.97600  1.000 45.76301  ?  387 ARG   A CD   1 
ATOM   1684 N  NE   . ARG   A 1 235 ? 19.64400  -9.99400  17.14800  1.000 53.94843  ?  387 ARG   A NE   1 
ATOM   1685 C  CZ   . ARG   A 1 235 ? 20.09200  -11.21400 16.87300  1.000 47.52821  ?  387 ARG   A CZ   1 
ATOM   1686 N  NH1  . ARG   A 1 235 ? 19.46700  -12.27900 17.35700  1.000 41.91168  ?  387 ARG   A NH1  1 
ATOM   1687 N  NH2  . ARG   A 1 235 ? 21.16500  -11.37100 16.11100  1.000 50.41829  ?  387 ARG   A NH2  1 
ATOM   1688 N  N    A SER   A 1 236 ? 15.59300  -7.15300  21.70100  0.560 39.40782  ?  388 SER   A N    1 
ATOM   1689 N  N    B SER   A 1 236 ? 15.59600  -7.15500  21.70200  0.440 39.44418  ?  388 SER   A N    1 
ATOM   1690 C  CA   A SER   A 1 236 ? 14.42100  -6.95200  22.54700  0.560 41.17667  ?  388 SER   A CA   1 
ATOM   1691 C  CA   B SER   A 1 236 ? 14.42900  -6.94000  22.55200  0.440 41.25254  ?  388 SER   A CA   1 
ATOM   1692 C  C    A SER   A 1 236 ? 13.38800  -6.07000  21.85700  0.560 41.68569  ?  388 SER   A C    1 
ATOM   1693 C  C    B SER   A 1 236 ? 13.39200  -6.07800  21.84500  0.440 41.59950  ?  388 SER   A C    1 
ATOM   1694 O  O    A SER   A 1 236 ? 12.18500  -6.35600  21.90500  0.560 43.41261  ?  388 SER   A O    1 
ATOM   1695 O  O    B SER   A 1 236 ? 12.19300  -6.38200  21.86700  0.440 43.35845  ?  388 SER   A O    1 
ATOM   1696 C  CB   A SER   A 1 236 ? 14.83700  -6.34300  23.88500  0.560 42.19038  ?  388 SER   A CB   1 
ATOM   1697 C  CB   B SER   A 1 236 ? 14.85300  -6.29300  23.87100  0.440 42.42427  ?  388 SER   A CB   1 
ATOM   1698 O  OG   A SER   A 1 236 ? 13.70200  -5.94600  24.63400  0.560 45.40027  ?  388 SER   A OG   1 
ATOM   1699 O  OG   B SER   A 1 236 ? 15.51500  -7.22100  24.70800  0.440 43.85774  ?  388 SER   A OG   1 
ATOM   1700 N  N    . LEU   A 1 237 ? 13.83800  -4.99000  21.21400  1.000 38.93137  ?  389 LEU   A N    1 
ATOM   1701 C  CA   . LEU   A 1 237 ? 12.91900  -4.14000  20.46400  1.000 38.15287  ?  389 LEU   A CA   1 
ATOM   1702 C  C    . LEU   A 1 237 ? 12.31700  -4.89700  19.28900  1.000 41.64228  ?  389 LEU   A C    1 
ATOM   1703 O  O    . LEU   A 1 237 ? 11.14600  -4.69500  18.94300  1.000 44.21161  ?  389 LEU   A O    1 
ATOM   1704 C  CB   . LEU   A 1 237 ? 13.64500  -2.88600  19.97900  1.000 40.29294  ?  389 LEU   A CB   1 
ATOM   1705 C  CG   . LEU   A 1 237 ? 13.97200  -1.84200  21.04400  1.000 50.35933  ?  389 LEU   A CG   1 
ATOM   1706 C  CD1  . LEU   A 1 237 ? 15.06600  -0.90400  20.55900  1.000 43.19181  ?  389 LEU   A CD1  1 
ATOM   1707 C  CD2  . LEU   A 1 237 ? 12.71900  -1.06700  21.40800  1.000 58.27954  ?  389 LEU   A CD2  1 
ATOM   1708 N  N    . ASN   A 1 238 ? 13.10700  -5.77000  18.66100  1.000 47.12487  ?  390 ASN   A N    1 
ATOM   1709 C  CA   . ASN   A 1 238 ? 12.58500  -6.62800  17.60300  1.000 46.69528  ?  390 ASN   A CA   1 
ATOM   1710 C  C    . ASN   A 1 238 ? 11.44200  -7.49500  18.12200  1.000 47.97127  ?  390 ASN   A C    1 
ATOM   1711 O  O    . ASN   A 1 238 ? 10.37800  -7.57800  17.49800  1.000 45.04822  ?  390 ASN   A O    1 
ATOM   1712 C  CB   . ASN   A 1 238 ? 13.71400  -7.49500  17.03800  1.000 38.89489  ?  390 ASN   A CB   1 
ATOM   1713 C  CG   . ASN   A 1 238 ? 13.34200  -8.17300  15.73000  1.000 43.32799  ?  390 ASN   A CG   1 
ATOM   1714 O  OD1  . ASN   A 1 238 ? 12.22300  -8.65500  15.55800  1.000 48.98427  ?  390 ASN   A OD1  1 
ATOM   1715 N  ND2  . ASN   A 1 238 ? 14.29300  -8.22700  14.80500  1.000 41.00090  ?  390 ASN   A ND2  1 
ATOM   1716 N  N    . GLU   A 1 239 ? 11.64500  -8.14100  19.27400  1.000 53.25449  ?  391 GLU   A N    1 
ATOM   1717 C  CA   . GLU   A 1 239 ? 10.62000  -9.02300  19.82700  1.000 60.54592  ?  391 GLU   A CA   1 
ATOM   1718 C  C    . GLU   A 1 239 ? 9.35800   -8.24900  20.18400  1.000 55.61041  ?  391 GLU   A C    1 
ATOM   1719 O  O    . GLU   A 1 239 ? 8.24200   -8.68100  19.87200  1.000 54.08917  ?  391 GLU   A O    1 
ATOM   1720 C  CB   . GLU   A 1 239 ? 11.16000  -9.75300  21.05800  1.000 70.37443  ?  391 GLU   A CB   1 
ATOM   1721 C  CG   . GLU   A 1 239 ? 12.04700  -10.94700 20.75000  1.000 85.52866  ?  391 GLU   A CG   1 
ATOM   1722 C  CD   . GLU   A 1 239 ? 12.82800  -11.41900 21.96500  1.000 104.98167 ?  391 GLU   A CD   1 
ATOM   1723 O  OE1  . GLU   A 1 239 ? 13.96500  -11.90800 21.79000  1.000 109.79458 ?  391 GLU   A OE1  1 
ATOM   1724 O  OE2  . GLU   A 1 239 ? 12.30700  -11.30000 23.09400  1.000 109.91530 ?  391 GLU   A OE2  1 
ATOM   1725 N  N    . GLU   A 1 240 ? 9.51700   -7.09900  20.84500  1.000 44.49474  ?  392 GLU   A N    1 
ATOM   1726 C  CA   . GLU   A 1 240 ? 8.35100   -6.31700  21.24200  1.000 45.82265  ?  392 GLU   A CA   1 
ATOM   1727 C  C    . GLU   A 1 240 ? 7.60800   -5.76800  20.03000  1.000 55.16386  ?  392 GLU   A C    1 
ATOM   1728 O  O    . GLU   A 1 240 ? 6.37200   -5.78300  19.99900  1.000 56.21428  ?  392 GLU   A O    1 
ATOM   1729 C  CB   . GLU   A 1 240 ? 8.76900   -5.18400  22.17900  1.000 43.90816  ?  392 GLU   A CB   1 
ATOM   1730 C  CG   . GLU   A 1 240 ? 7.61200   -4.31600  22.65200  1.000 54.45185  ?  392 GLU   A CG   1 
ATOM   1731 C  CD   . GLU   A 1 240 ? 6.51100   -5.11600  23.32900  1.000 65.69489  ?  392 GLU   A CD   1 
ATOM   1732 O  OE1  . GLU   A 1 240 ? 5.32800   -4.74500  23.17400  1.000 68.59536  ?  392 GLU   A OE1  1 
ATOM   1733 O  OE2  . GLU   A 1 240 ? 6.82300   -6.10800  24.02300  1.000 67.51926  ?  392 GLU   A OE2  1 
ATOM   1734 N  N    . HIS   A 1 241 ? 8.33600   -5.28000  19.02000  1.000 48.49160  ?  393 HIS   A N    1 
ATOM   1735 C  CA   . HIS   A 1 241 ? 7.66800   -4.76400  17.82900  1.000 52.13661  ?  393 HIS   A CA   1 
ATOM   1736 C  C    . HIS   A 1 241 ? 6.90400   -5.86300  17.10500  1.000 52.10812  ?  393 HIS   A C    1 
ATOM   1737 O  O    . HIS   A 1 241 ? 5.79000   -5.63700  16.61700  1.000 55.11505  ?  393 HIS   A O    1 
ATOM   1738 C  CB   . HIS   A 1 241 ? 8.67100   -4.12100  16.87500  1.000 46.15409  ?  393 HIS   A CB   1 
ATOM   1739 C  CG   . HIS   A 1 241 ? 8.07200   -3.74000  15.55600  1.000 48.97613  ?  393 HIS   A CG   1 
ATOM   1740 N  ND1  . HIS   A 1 241 ? 8.10000   -4.57200  14.45700  1.000 45.23376  ?  393 HIS   A ND1  1 
ATOM   1741 C  CD2  . HIS   A 1 241 ? 7.40100   -2.62900  15.16900  1.000 44.80257  ?  393 HIS   A CD2  1 
ATOM   1742 C  CE1  . HIS   A 1 241 ? 7.48400   -3.98500  13.44700  1.000 45.62808  ?  393 HIS   A CE1  1 
ATOM   1743 N  NE2  . HIS   A 1 241 ? 7.05000   -2.80500  13.85200  1.000 45.31631  ?  393 HIS   A NE2  1 
ATOM   1744 N  N    . SER   A 1 242 ? 7.49100   -7.05900  17.02000  1.000 48.90261  ?  394 SER   A N    1 
ATOM   1745 C  CA   . SER   A 1 242 ? 6.84900   -8.15600  16.30200  1.000 52.25361  ?  394 SER   A CA   1 
ATOM   1746 C  C    . SER   A 1 242 ? 5.52900   -8.54600  16.95100  1.000 56.74060  ?  394 SER   A C    1 
ATOM   1747 O  O    . SER   A 1 242 ? 4.50300   -8.65700  16.27100  1.000 64.35578  ?  394 SER   A O    1 
ATOM   1748 C  CB   . SER   A 1 242 ? 7.78800   -9.36100  16.23000  1.000 48.27386  ?  394 SER   A CB   1 
ATOM   1749 O  OG   . SER   A 1 242 ? 8.88100   -9.10000  15.37000  1.000 61.61490  ?  394 SER   A OG   1 
ATOM   1750 N  N    . LYS   A 1 243 ? 5.53900   -8.77300  18.26900  1.000 51.70738  ?  395 LYS   A N    1 
ATOM   1751 C  CA   . LYS   A 1 243 ? 4.30300   -9.12800  18.95800  1.000 59.85578  ?  395 LYS   A CA   1 
ATOM   1752 C  C    . LYS   A 1 243 ? 3.24500   -8.04500  18.78900  1.000 65.06558  ?  395 LYS   A C    1 
ATOM   1753 O  O    . LYS   A 1 243 ? 2.05500   -8.34700  18.63800  1.000 67.70877  ?  395 LYS   A O    1 
ATOM   1754 C  CB   . LYS   A 1 243 ? 4.57500   -9.38300  20.43800  1.000 67.89051  ?  395 LYS   A CB   1 
ATOM   1755 C  CG   . LYS   A 1 243 ? 5.42400   -10.61100 20.70900  1.000 80.71668  ?  395 LYS   A CG   1 
ATOM   1756 C  CD   . LYS   A 1 243 ? 6.19500   -10.47800 22.01200  1.000 90.99212  ?  395 LYS   A CD   1 
ATOM   1757 C  CE   . LYS   A 1 243 ? 7.04900   -11.71200 22.26700  1.000 98.44200  ?  395 LYS   A CE   1 
ATOM   1758 N  NZ   . LYS   A 1 243 ? 7.58000   -11.75300 23.65800  1.000 99.88624  ?  395 LYS   A NZ   1 
ATOM   1759 N  N    . GLN   A 1 244 ? 3.65600   -6.77500  18.81300  1.000 58.67130  ?  396 GLN   A N    1 
ATOM   1760 C  CA   . GLN   A 1 244 ? 2.70600   -5.70400  18.54000  1.000 57.42886  ?  396 GLN   A CA   1 
ATOM   1761 C  C    . GLN   A 1 244 ? 2.33900   -5.64400  17.06300  1.000 61.37110  ?  396 GLN   A C    1 
ATOM   1762 O  O    . GLN   A 1 244 ? 1.21300   -5.26200  16.72400  1.000 61.96658  ?  396 GLN   A O    1 
ATOM   1763 C  CB   . GLN   A 1 244 ? 3.26900   -4.36300  19.00600  1.000 51.30970  ?  396 GLN   A CB   1 
ATOM   1764 C  CG   . GLN   A 1 244 ? 3.14900   -4.13900  20.50200  1.000 61.12569  ?  396 GLN   A CG   1 
ATOM   1765 C  CD   . GLN   A 1 244 ? 3.70200   -2.80000  20.93800  1.000 61.46093  ?  396 GLN   A CD   1 
ATOM   1766 O  OE1  . GLN   A 1 244 ? 3.53100   -1.79200  20.25300  1.000 62.00719  ?  396 GLN   A OE1  1 
ATOM   1767 N  NE2  . GLN   A 1 244 ? 4.36800   -2.78100  22.08600  1.000 67.83210  ?  396 GLN   A NE2  1 
ATOM   1768 N  N    . TYR   A 1 245 ? 3.26300   -6.01500  16.17100  1.000 54.33598  ?  397 TYR   A N    1 
ATOM   1769 C  CA   . TYR   A 1 245 ? 2.93800   -6.01300  14.74800  1.000 57.92665  ?  397 TYR   A CA   1 
ATOM   1770 C  C    . TYR   A 1 245 ? 1.91900   -7.09500  14.41300  1.000 54.68879  ?  397 TYR   A C    1 
ATOM   1771 O  O    . TYR   A 1 245 ? 0.98700   -6.85200  13.63700  1.000 53.96758  ?  397 TYR   A O    1 
ATOM   1772 C  CB   . TYR   A 1 245 ? 4.19900   -6.19300  13.90100  1.000 56.82307  ?  397 TYR   A CB   1 
ATOM   1773 C  CG   . TYR   A 1 245 ? 3.89400   -6.25100  12.42100  1.000 54.70668  ?  397 TYR   A CG   1 
ATOM   1774 C  CD1  . TYR   A 1 245 ? 3.69400   -5.08900  11.68900  1.000 49.89147  ?  397 TYR   A CD1  1 
ATOM   1775 C  CD2  . TYR   A 1 245 ? 3.77600   -7.46900  11.76400  1.000 56.57399  ?  397 TYR   A CD2  1 
ATOM   1776 C  CE1  . TYR   A 1 245 ? 3.40000   -5.13600  10.34000  1.000 45.26531  ?  397 TYR   A CE1  1 
ATOM   1777 C  CE2  . TYR   A 1 245 ? 3.48000   -7.52700  10.41700  1.000 53.50626  ?  397 TYR   A CE2  1 
ATOM   1778 C  CZ   . TYR   A 1 245 ? 3.29400   -6.35900  9.70900   1.000 54.00491  ?  397 TYR   A CZ   1 
ATOM   1779 O  OH   . TYR   A 1 245 ? 2.99900   -6.41800  8.36600   1.000 52.05761  ?  397 TYR   A OH   1 
ATOM   1780 N  N    . ARG   A 1 246 ? 2.08300   -8.29600  14.97800  1.000 50.77029  ?  398 ARG   A N    1 
ATOM   1781 C  CA   . ARG   A 1 246 ? 1.14100   -9.37600  14.69500  1.000 56.44491  ?  398 ARG   A CA   1 
ATOM   1782 C  C    . ARG   A 1 246 ? -0.25200  -9.04700  15.21200  1.000 62.64952  ?  398 ARG   A C    1 
ATOM   1783 O  O    . ARG   A 1 246 ? -1.25300  -9.41500  14.58700  1.000 67.15008  ?  398 ARG   A O    1 
ATOM   1784 C  CB   . ARG   A 1 246 ? 1.63000   -10.69800 15.29500  1.000 64.88636  ?  398 ARG   A CB   1 
ATOM   1785 C  CG   . ARG   A 1 246 ? 3.08100   -11.03700 15.01200  1.000 76.25284  ?  398 ARG   A CG   1 
ATOM   1786 C  CD   . ARG   A 1 246 ? 3.45800   -12.39200 15.59400  1.000 88.91401  ?  398 ARG   A CD   1 
ATOM   1787 N  NE   . ARG   A 1 246 ? 4.78300   -12.38300 16.21100  1.000 93.62828  ?  398 ARG   A NE   1 
ATOM   1788 C  CZ   . ARG   A 1 246 ? 4.99300   -12.49300 17.51800  1.000 90.00031  ?  398 ARG   A CZ   1 
ATOM   1789 N  NH1  . ARG   A 1 246 ? 3.96200   -12.62300 18.34200  1.000 93.06720  ?  398 ARG   A NH1  1 
ATOM   1790 N  NH2  . ARG   A 1 246 ? 6.22700   -12.47600 18.00400  1.000 79.11730  ?  398 ARG   A NH2  1 
ATOM   1791 N  N    . SER   A 1 247 ? -0.33900  -8.35500  16.35200  1.000 63.81564  ?  399 SER   A N    1 
ATOM   1792 C  CA   . SER   A 1 247 ? -1.64700  -7.97400  16.87600  1.000 67.17064  ?  399 SER   A CA   1 
ATOM   1793 C  C    . SER   A 1 247 ? -2.27800  -6.87300  16.03000  1.000 62.39398  ?  399 SER   A C    1 
ATOM   1794 O  O    . SER   A 1 247 ? -3.49700  -6.86200  15.82500  1.000 68.26451  ?  399 SER   A O    1 
ATOM   1795 C  CB   . SER   A 1 247 ? -1.52200  -7.53200  18.33500  1.000 68.75041  ?  399 SER   A CB   1 
ATOM   1796 O  OG   . SER   A 1 247 ? -1.47100  -6.12000  18.44100  1.000 76.49138  ?  399 SER   A OG   1 
ATOM   1797 N  N    . LEU   A 1 248 ? -1.46500  -5.93700  15.53500  1.000 62.32383  ?  400 LEU   A N    1 
ATOM   1798 C  CA   . LEU   A 1 248 ? -1.97700  -4.92400  14.61800  1.000 59.58231  ?  400 LEU   A CA   1 
ATOM   1799 C  C    . LEU   A 1 248 ? -2.36900  -5.54500  13.28400  1.000 66.17295  ?  400 LEU   A C    1 
ATOM   1800 O  O    . LEU   A 1 248 ? -3.45400  -5.27300  12.75400  1.000 69.63597  ?  400 LEU   A O    1 
ATOM   1801 C  CB   . LEU   A 1 248 ? -0.93400  -3.82400  14.41000  1.000 61.75110  ?  400 LEU   A CB   1 
ATOM   1802 C  CG   . LEU   A 1 248 ? -0.71700  -2.82700  15.54700  1.000 61.23153  ?  400 LEU   A CG   1 
ATOM   1803 C  CD1  . LEU   A 1 248 ? 0.57600   -2.05700  15.32800  1.000 56.92496  ?  400 LEU   A CD1  1 
ATOM   1804 C  CD2  . LEU   A 1 248 ? -1.90000  -1.87800  15.65100  1.000 63.63765  ?  400 LEU   A CD2  1 
ATOM   1805 N  N    . SER   A 1 249 ? -1.49800  -6.39400  12.73100  1.000 62.77922  ?  401 SER   A N    1 
ATOM   1806 C  CA   . SER   A 1 249 ? -1.74500  -6.99700  11.42500  1.000 71.12772  ?  401 SER   A CA   1 
ATOM   1807 C  C    . SER   A 1 249 ? -2.91000  -7.97300  11.43600  1.000 76.71735  ?  401 SER   A C    1 
ATOM   1808 O  O    . SER   A 1 249 ? -3.47600  -8.25100  10.37400  1.000 80.34883  ?  401 SER   A O    1 
ATOM   1809 C  CB   . SER   A 1 249 ? -0.48900  -7.71500  10.93000  1.000 59.72031  ?  401 SER   A CB   1 
ATOM   1810 O  OG   . SER   A 1 249 ? 0.44300   -6.79200  10.40700  1.000 71.86221  ?  401 SER   A OG   1 
ATOM   1811 N  N    . PHE   A 1 250 ? -3.27100  -8.51000  12.60300  1.000 85.82592  ?  402 PHE   A N    1 
ATOM   1812 C  CA   . PHE   A 1 250 ? -4.35800  -9.48100  12.65900  1.000 92.03886  ?  402 PHE   A CA   1 
ATOM   1813 C  C    . PHE   A 1 250 ? -5.69100  -8.86100  12.26500  1.000 92.10942  ?  402 PHE   A C    1 
ATOM   1814 O  O    . PHE   A 1 250 ? -6.56900  -9.56100  11.74800  1.000 100.91677 ?  402 PHE   A O    1 
ATOM   1815 C  CB   . PHE   A 1 250 ? -4.45300  -10.08700 14.05800  1.000 91.88761  ?  402 PHE   A CB   1 
ATOM   1816 C  CG   . PHE   A 1 250 ? -4.90800  -11.51400 14.06400  1.000 92.81178  ?  402 PHE   A CG   1 
ATOM   1817 C  CD1  . PHE   A 1 250 ? -4.08600  -12.51400 13.57700  1.000 89.20241  ?  402 PHE   A CD1  1 
ATOM   1818 C  CD2  . PHE   A 1 250 ? -6.16400  -11.85400 14.54100  1.000 93.27136  ?  402 PHE   A CD2  1 
ATOM   1819 C  CE1  . PHE   A 1 250 ? -4.50000  -13.83000 13.57400  1.000 91.98739  ?  402 PHE   A CE1  1 
ATOM   1820 C  CE2  . PHE   A 1 250 ? -6.58500  -13.17200 14.54000  1.000 94.31908  ?  402 PHE   A CE2  1 
ATOM   1821 C  CZ   . PHE   A 1 250 ? -5.75100  -14.16000 14.05500  1.000 96.23733  ?  402 PHE   A CZ   1 
ATOM   1822 N  N    . GLN   A 1 251 ? -5.86300  -7.56600  12.50500  1.000 88.29246  ?  403 GLN   A N    1 
ATOM   1823 C  CA   . GLN   A 1 251 ? -7.06900  -6.86200  12.09600  1.000 81.94230  ?  403 GLN   A CA   1 
ATOM   1824 C  C    . GLN   A 1 251 ? -6.92200  -6.40600  10.65000  1.000 75.88709  ?  403 GLN   A C    1 
ATOM   1825 O  O    . GLN   A 1 251 ? -6.06900  -5.56000  10.35200  1.000 68.38031  ?  403 GLN   A O    1 
ATOM   1826 C  CB   . GLN   A 1 251 ? -7.33300  -5.66800  13.01500  1.000 80.94124  ?  403 GLN   A CB   1 
ATOM   1827 C  CG   . GLN   A 1 251 ? -8.28900  -5.95600  14.16800  1.000 97.43167  ?  403 GLN   A CG   1 
ATOM   1828 C  CD   . GLN   A 1 251 ? -7.69800  -6.88200  15.21600  1.000 103.08869 ?  403 GLN   A CD   1 
ATOM   1829 O  OE1  . GLN   A 1 251 ? -8.16900  -8.00600  15.40500  1.000 103.61596 ?  403 GLN   A OE1  1 
ATOM   1830 N  NE2  . GLN   A 1 251 ? -6.66400  -6.41300  15.90500  1.000 99.76030  ?  403 GLN   A NE2  1 
ATOM   1831 N  N    . PRO   A 1 252 ? -7.72300  -6.94300  9.72600   1.000 79.08413  ?  404 PRO   A N    1 
ATOM   1832 C  CA   . PRO   A 1 252 ? -7.58300  -6.54700  8.31500   1.000 74.31677  ?  404 PRO   A CA   1 
ATOM   1833 C  C    . PRO   A 1 252 ? -7.79600  -5.06600  8.07000   1.000 70.74898  ?  404 PRO   A C    1 
ATOM   1834 O  O    . PRO   A 1 252 ? -7.31000  -4.55000  7.05700   1.000 73.89299  ?  404 PRO   A O    1 
ATOM   1835 C  CB   . PRO   A 1 252 ? -8.65200  -7.39300  7.61000   1.000 77.13428  ?  404 PRO   A CB   1 
ATOM   1836 C  CG   . PRO   A 1 252 ? -8.81600  -8.58600  8.50000   1.000 76.16848  ?  404 PRO   A CG   1 
ATOM   1837 C  CD   . PRO   A 1 252 ? -8.69700  -8.03400  9.89300   1.000 77.51485  ?  404 PRO   A CD   1 
ATOM   1838 N  N    . GLU   A 1 253 ? -8.50500  -4.36500  8.95800   1.000 77.66878  ?  405 GLU   A N    1 
ATOM   1839 C  CA   . GLU   A 1 253 ? -8.65100  -2.92000  8.81300   1.000 73.31244  ?  405 GLU   A CA   1 
ATOM   1840 C  C    . GLU   A 1 253 ? -7.29200  -2.22900  8.84100   1.000 65.61965  ?  405 GLU   A C    1 
ATOM   1841 O  O    . GLU   A 1 253 ? -7.05600  -1.27600  8.08900   1.000 66.01821  ?  405 GLU   A O    1 
ATOM   1842 C  CB   . GLU   A 1 253 ? -9.55600  -2.37000  9.91500   1.000 78.52205  ?  405 GLU   A CB   1 
ATOM   1843 C  CG   . GLU   A 1 253 ? -10.68000 -3.31100  10.32000  1.000 93.82005  ?  405 GLU   A CG   1 
ATOM   1844 C  CD   . GLU   A 1 253 ? -10.27800 -4.24000  11.44900  1.000 102.20401 ?  405 GLU   A CD   1 
ATOM   1845 O  OE1  . GLU   A 1 253 ? -10.48900 -5.46500  11.32300  1.000 105.29952 ?  405 GLU   A OE1  1 
ATOM   1846 O  OE2  . GLU   A 1 253 ? -9.75300  -3.73800  12.46400  1.000 106.81706 ?  405 GLU   A OE2  1 
ATOM   1847 N  N    . ASN   A 1 254 ? -6.38100  -2.70700  9.69300   1.000 55.29725  ?  406 ASN   A N    1 
ATOM   1848 C  CA   . ASN   A 1 254 ? -5.04900  -2.11700  9.78600   1.000 49.29410  ?  406 ASN   A CA   1 
ATOM   1849 C  C    . ASN   A 1 254 ? -4.14800  -2.59000  8.65100   1.000 54.20483  ?  406 ASN   A C    1 
ATOM   1850 O  O    . ASN   A 1 254 ? -3.42300  -1.78800  8.05100   1.000 52.52289  ?  406 ASN   A O    1 
ATOM   1851 C  CB   . ASN   A 1 254 ? -4.41500  -2.45800  11.13700  1.000 52.05554  ?  406 ASN   A CB   1 
ATOM   1852 C  CG   . ASN   A 1 254 ? -5.16400  -1.85000  12.30500  1.000 61.25010  ?  406 ASN   A CG   1 
ATOM   1853 O  OD1  . ASN   A 1 254 ? -5.78600  -0.79600  12.18000  1.000 67.70687  ?  406 ASN   A OD1  1 
ATOM   1854 N  ND2  . ASN   A 1 254 ? -5.11400  -2.52100  13.44900  1.000 69.46538  ?  406 ASN   A ND2  1 
ATOM   1855 N  N    . SER   A 1 255 ? -4.17600  -3.89300  8.35100   1.000 59.90528  ?  407 SER   A N    1 
ATOM   1856 C  CA   . SER   A 1 255 ? -3.34300  -4.43600  7.28100   1.000 60.58858  ?  407 SER   A CA   1 
ATOM   1857 C  C    . SER   A 1 255 ? -3.61600  -3.75400  5.94700   1.000 56.57649  ?  407 SER   A C    1 
ATOM   1858 O  O    . SER   A 1 255 ? -2.70900  -3.63700  5.11400   1.000 54.70806  ?  407 SER   A O    1 
ATOM   1859 C  CB   . SER   A 1 255 ? -3.56700  -5.94300  7.15900   1.000 61.56259  ?  407 SER   A CB   1 
ATOM   1860 O  OG   . SER   A 1 255 ? -4.53600  -6.22500  6.16300   1.000 73.95376  ?  407 SER   A OG   1 
ATOM   1861 N  N    . MET   A 1 256 ? -4.85400  -3.29900  5.72700   1.000 57.25771  ?  408 MET   A N    1 
ATOM   1862 C  CA   . MET   A 1 256 ? -5.18200  -2.57900  4.50100   1.000 55.37305  ?  408 MET   A CA   1 
ATOM   1863 C  C    . MET   A 1 256 ? -4.34300  -1.32200  4.34200   1.000 53.96352  ?  408 MET   A C    1 
ATOM   1864 O  O    . MET   A 1 256 ? -4.04600  -0.91100  3.21400   1.000 53.10719  ?  408 MET   A O    1 
ATOM   1865 C  CB   . MET   A 1 256 ? -6.66300  -2.20200  4.48500   1.000 50.66875  ?  408 MET   A CB   1 
ATOM   1866 C  CG   . MET   A 1 256 ? -7.61000  -3.33100  4.15900   1.000 61.74486  ?  408 MET   A CG   1 
ATOM   1867 S  SD   . MET   A 1 256 ? -9.23000  -2.69800  3.68500   1.000 71.72042  ?  408 MET   A SD   1 
ATOM   1868 C  CE   . MET   A 1 256 ? -9.35800  -1.25300  4.73600   1.000 72.39959  ?  408 MET   A CE   1 
ATOM   1869 N  N    . LYS   A 1 257 ? -3.96600  -0.69100  5.45100   1.000 54.72010  ?  409 LYS   A N    1 
ATOM   1870 C  CA   . LYS   A 1 257 ? -3.22200  0.55600   5.40200   1.000 49.16680  ?  409 LYS   A CA   1 
ATOM   1871 C  C    . LYS   A 1 257 ? -1.71900  0.34300   5.28500   1.000 44.68327  ?  409 LYS   A C    1 
ATOM   1872 O  O    . LYS   A 1 257 ? -0.98400  1.31400   5.07700   1.000 49.18103  ?  409 LYS   A O    1 
ATOM   1873 C  CB   . LYS   A 1 257 ? -3.53500  1.39900   6.64300   1.000 61.71016  ?  409 LYS   A CB   1 
ATOM   1874 C  CG   . LYS   A 1 257 ? -4.99700  1.83100   6.75100   1.000 69.74416  ?  409 LYS   A CG   1 
ATOM   1875 C  CD   . LYS   A 1 257 ? -5.10400  3.33200   6.89900   1.000 84.36012  ?  409 LYS   A CD   1 
ATOM   1876 C  CE   . LYS   A 1 257 ? -5.49900  3.74200   8.30700   1.000 93.37140  ?  409 LYS   A CE   1 
ATOM   1877 N  NZ   . LYS   A 1 257 ? -5.86600  5.18400   8.39100   1.000 97.97499  ?  409 LYS   A NZ   1 
ATOM   1878 N  N    . LEU   A 1 258 ? -1.24600  -0.89400  5.41500   1.000 46.36991  ?  410 LEU   A N    1 
ATOM   1879 C  CA   . LEU   A 1 258 ? 0.16500   -1.17900  5.23100   1.000 43.48378  ?  410 LEU   A CA   1 
ATOM   1880 C  C    . LEU   A 1 258 ? 0.49600   -1.24800  3.74100   1.000 45.89071  ?  410 LEU   A C    1 
ATOM   1881 O  O    . LEU   A 1 258 ? -0.37700  -1.14500  2.87600   1.000 47.82869  ?  410 LEU   A O    1 
ATOM   1882 C  CB   . LEU   A 1 258 ? 0.54400   -2.48300  5.93100   1.000 46.62108  ?  410 LEU   A CB   1 
ATOM   1883 C  CG   . LEU   A 1 258 ? 0.17200   -2.56400  7.41400   1.000 48.08189  ?  410 LEU   A CG   1 
ATOM   1884 C  CD1  . LEU   A 1 258 ? 0.68300   -3.85400  8.04000   1.000 38.85465  ?  410 LEU   A CD1  1 
ATOM   1885 C  CD2  . LEU   A 1 258 ? 0.70500   -1.35100  8.16800   1.000 44.54336  ?  410 LEU   A CD2  1 
ATOM   1886 N  N    . THR   A 1 259 ? 1.77200   -1.41300  3.44500   1.000 45.64153  ?  411 THR   A N    1 
ATOM   1887 C  CA   . THR   A 1 259 ? 2.20700   -1.56800  2.06900   1.000 45.74511  ?  411 THR   A CA   1 
ATOM   1888 C  C    . THR   A 1 259 ? 2.49300   -3.03100  1.77200   1.000 42.83216  ?  411 THR   A C    1 
ATOM   1889 O  O    . THR   A 1 259 ? 2.66400   -3.84000  2.68900   1.000 44.22349  ?  411 THR   A O    1 
ATOM   1890 C  CB   . THR   A 1 259 ? 3.46400   -0.73200  1.80400   1.000 42.42647  ?  411 THR   A CB   1 
ATOM   1891 O  OG1  . THR   A 1 259 ? 4.58600   -1.33700  2.45700   1.000 45.61458  ?  411 THR   A OG1  1 
ATOM   1892 C  CG2  . THR   A 1 259 ? 3.27800   0.69000   2.31500   1.000 37.99584  ?  411 THR   A CG2  1 
ATOM   1893 N  N    . PRO   A 1 260 ? 2.53400   -3.41600  0.49300   1.000 39.01614  ?  412 PRO   A N    1 
ATOM   1894 C  CA   . PRO   A 1 260 ? 2.88200   -4.81200  0.17600   1.000 42.91117  ?  412 PRO   A CA   1 
ATOM   1895 C  C    . PRO   A 1 260 ? 4.26200   -5.21600  0.67000   1.000 46.34763  ?  412 PRO   A C    1 
ATOM   1896 O  O    . PRO   A 1 260 ? 4.43100   -6.33800  1.16500   1.000 35.53057  ?  412 PRO   A O    1 
ATOM   1897 C  CB   . PRO   A 1 260 ? 2.78300   -4.85100  -1.35500  1.000 43.62254  ?  412 PRO   A CB   1 
ATOM   1898 C  CG   . PRO   A 1 260 ? 1.81000   -3.76500  -1.69300  1.000 42.64165  ?  412 PRO   A CG   1 
ATOM   1899 C  CD   . PRO   A 1 260 ? 2.08900   -2.67400  -0.70000  1.000 40.38972  ?  412 PRO   A CD   1 
ATOM   1900 N  N    . LEU   A 1 261 ? 5.25700   -4.33000  0.55800   1.000 39.69516  ?  413 LEU   A N    1 
ATOM   1901 C  CA   . LEU   A 1 261 ? 6.60000   -4.66900  1.02400   1.000 35.06969  ?  413 LEU   A CA   1 
ATOM   1902 C  C    . LEU   A 1 261 ? 6.62600   -4.87400  2.53300   1.000 35.00535  ?  413 LEU   A C    1 
ATOM   1903 O  O    . LEU   A 1 261 ? 7.26600   -5.81000  3.02800   1.000 42.79386  ?  413 LEU   A O    1 
ATOM   1904 C  CB   . LEU   A 1 261 ? 7.59700   -3.58300  0.61500   1.000 37.55206  ?  413 LEU   A CB   1 
ATOM   1905 C  CG   . LEU   A 1 261 ? 9.06600   -3.87600  0.95300   1.000 40.95091  ?  413 LEU   A CG   1 
ATOM   1906 C  CD1  . LEU   A 1 261 ? 9.57900   -5.10500  0.21000   1.000 33.82001  ?  413 LEU   A CD1  1 
ATOM   1907 C  CD2  . LEU   A 1 261 ? 9.94300   -2.67100  0.66400   1.000 32.43139  ?  413 LEU   A CD2  1 
ATOM   1908 N  N    . VAL   A 1 262 ? 5.94000   -4.00400  3.28000   1.000 39.43038  ?  414 VAL   A N    1 
ATOM   1909 C  CA   . VAL   A 1 262 ? 5.86100   -4.15900  4.73100   1.000 39.69674  ?  414 VAL   A CA   1 
ATOM   1910 C  C    . VAL   A 1 262 ? 5.24000   -5.50300  5.09100   1.000 43.27726  ?  414 VAL   A C    1 
ATOM   1911 O  O    . VAL   A 1 262 ? 5.73100   -6.21500  5.97700   1.000 40.62124  ?  414 VAL   A O    1 
ATOM   1912 C  CB   . VAL   A 1 262 ? 5.07500   -2.98700  5.34800   1.000 39.89637  ?  414 VAL   A CB   1 
ATOM   1913 C  CG1  . VAL   A 1 262 ? 4.60100   -3.33100  6.75500   1.000 36.83345  ?  414 VAL   A CG1  1 
ATOM   1914 C  CG2  . VAL   A 1 262 ? 5.92500   -1.72400  5.35900   1.000 36.61822  ?  414 VAL   A CG2  1 
ATOM   1915 N  N    . LEU   A 1 263 ? 4.15800   -5.87500  4.40500   1.000 39.41246  ?  415 LEU   A N    1 
ATOM   1916 C  CA   . LEU   A 1 263 ? 3.50800   -7.15300  4.67800   1.000 44.72221  ?  415 LEU   A CA   1 
ATOM   1917 C  C    . LEU   A 1 263 ? 4.42700   -8.32100  4.34700   1.000 46.06196  ?  415 LEU   A C    1 
ATOM   1918 O  O    . LEU   A 1 263 ? 4.45000   -9.32600  5.06700   1.000 50.10225  ?  415 LEU   A O    1 
ATOM   1919 C  CB   . LEU   A 1 263 ? 2.20500   -7.25700  3.88500   1.000 48.92859  ?  415 LEU   A CB   1 
ATOM   1920 C  CG   . LEU   A 1 263 ? 1.04300   -6.39700  4.38000   1.000 51.66070  ?  415 LEU   A CG   1 
ATOM   1921 C  CD1  . LEU   A 1 263 ? -0.14900  -6.51200  3.44200   1.000 50.00800  ?  415 LEU   A CD1  1 
ATOM   1922 C  CD2  . LEU   A 1 263 ? 0.65500   -6.79200  5.79800   1.000 52.54497  ?  415 LEU   A CD2  1 
ATOM   1923 N  N    . GLU   A 1 264 ? 5.19100   -8.20600  3.26100   1.000 41.69536  ?  416 GLU   A N    1 
ATOM   1924 C  CA   . GLU   A 1 264 ? 6.11100   -9.27300  2.88100   1.000 47.79120  ?  416 GLU   A CA   1 
ATOM   1925 C  C    . GLU   A 1 264 ? 7.23200   -9.42300  3.90400   1.000 49.65054  ?  416 GLU   A C    1 
ATOM   1926 O  O    . GLU   A 1 264 ? 7.54400   -10.53600 4.34200   1.000 49.47336  ?  416 GLU   A O    1 
ATOM   1927 C  CB   . GLU   A 1 264 ? 6.68400   -8.99100  1.49300   1.000 51.14781  ?  416 GLU   A CB   1 
ATOM   1928 C  CG   . GLU   A 1 264 ? 7.14400   -10.22000 0.73400   1.000 60.52546  ?  416 GLU   A CG   1 
ATOM   1929 C  CD   . GLU   A 1 264 ? 7.89100   -9.86200  -0.53600  1.000 68.09865  ?  416 GLU   A CD   1 
ATOM   1930 O  OE1  . GLU   A 1 264 ? 9.07800   -9.48600  -0.44100  1.000 65.22881  ?  416 GLU   A OE1  1 
ATOM   1931 O  OE2  . GLU   A 1 264 ? 7.29300   -9.95100  -1.62800  1.000 67.80715  ?  416 GLU   A OE2  1 
ATOM   1932 N  N    . VAL   A 1 265 ? 7.84100   -8.30800  4.30500   1.000 46.72503  ?  417 VAL   A N    1 
ATOM   1933 C  CA   . VAL   A 1 265 ? 8.99400   -8.36500  5.19800   1.000 45.59070  ?  417 VAL   A CA   1 
ATOM   1934 C  C    . VAL   A 1 265 ? 8.55900   -8.64300  6.63100   1.000 48.28820  ?  417 VAL   A C    1 
ATOM   1935 O  O    . VAL   A 1 265 ? 9.04100   -9.58700  7.26900   1.000 51.06535  ?  417 VAL   A O    1 
ATOM   1936 C  CB   . VAL   A 1 265 ? 9.80900   -7.06200  5.09500   1.000 37.90773  ?  417 VAL   A CB   1 
ATOM   1937 C  CG1  . VAL   A 1 265 ? 10.85600  -6.99600  6.20000   1.000 36.99037  ?  417 VAL   A CG1  1 
ATOM   1938 C  CG2  . VAL   A 1 265 ? 10.46300  -6.95700  3.72700   1.000 33.44955  ?  417 VAL   A CG2  1 
ATOM   1939 N  N    . PHE   A 1 266 ? 7.64100   -7.83300  7.15800   1.000 43.35167  ?  418 PHE   A N    1 
ATOM   1940 C  CA   . PHE   A 1 266 ? 7.23600   -7.95700  8.55200   1.000 44.89432  ?  418 PHE   A CA   1 
ATOM   1941 C  C    . PHE   A 1 266 ? 6.29500   -9.13100  8.80000   1.000 54.26737  ?  418 PHE   A C    1 
ATOM   1942 O  O    . PHE   A 1 266 ? 6.20400   -9.59900  9.94000   1.000 60.36560  ?  418 PHE   A O    1 
ATOM   1943 C  CB   . PHE   A 1 266 ? 6.57900   -6.65900  9.02300   1.000 46.86958  ?  418 PHE   A CB   1 
ATOM   1944 C  CG   . PHE   A 1 266 ? 7.54800   -5.53300  9.24300   1.000 46.33525  ?  418 PHE   A CG   1 
ATOM   1945 C  CD1  . PHE   A 1 266 ? 7.09300   -4.25200  9.50700   1.000 51.51237  ?  418 PHE   A CD1  1 
ATOM   1946 C  CD2  . PHE   A 1 266 ? 8.91500   -5.75700  9.18800   1.000 54.87164  ?  418 PHE   A CD2  1 
ATOM   1947 C  CE1  . PHE   A 1 266 ? 7.98200   -3.21300  9.71200   1.000 55.72571  ?  418 PHE   A CE1  1 
ATOM   1948 C  CE2  . PHE   A 1 266 ? 9.81100   -4.72400  9.39100   1.000 52.71099  ?  418 PHE   A CE2  1 
ATOM   1949 C  CZ   . PHE   A 1 266 ? 9.34500   -3.45000  9.65300   1.000 61.15705  ?  418 PHE   A CZ   1 
ATOM   1950 N  N    . GLY   A 1 267 ? 5.59600   -9.61000  7.78100   1.000 56.53525  ?  419 GLY   A N    1 
ATOM   1951 C  CA   . GLY   A 1 267 ? 4.74600   -10.77700 7.90300   1.000 63.08986  ?  419 GLY   A CA   1 
ATOM   1952 C  C    . GLY   A 1 267 ? 3.28000   -10.45200 7.67200   1.000 79.52871  ?  419 GLY   A C    1 
ATOM   1953 O  O    . GLY   A 1 267 ? 2.85900   -9.29600  7.63300   1.000 71.09232  ?  419 GLY   A O    1 
ATOM   1954 N  N    . ASN   A 1 268 ? 2.50300   -11.52200 7.51900   1.000 93.73964  ?  420 ASN   A N    1 
ATOM   1955 C  CA   . ASN   A 1 268 ? 1.06400   -11.41400 7.29200   1.000 100.67610 ?  420 ASN   A CA   1 
ATOM   1956 C  C    . ASN   A 1 268 ? 0.26700   -11.93400 8.48800   1.000 96.93770  ?  420 ASN   A C    1 
ATOM   1957 O  O    . ASN   A 1 268 ? -0.61000  -12.78800 8.34200   1.000 87.89939  ?  420 ASN   A O    1 
ATOM   1958 C  CB   . ASN   A 1 268 ? 0.66100   -12.17500 6.02600   1.000 100.01934 ?  420 ASN   A CB   1 
ATOM   1959 C  CG   . ASN   A 1 268 ? 0.93100   -11.38500 4.76000   1.000 98.35313  ?  420 ASN   A CG   1 
ATOM   1960 O  OD1  . ASN   A 1 268 ? 2.08300   -11.14600 4.39800   1.000 96.06978  ?  420 ASN   A OD1  1 
ATOM   1961 N  ND2  . ASN   A 1 268 ? -0.13400  -10.97900 4.07700   1.000 95.71339  ?  420 ASN   A ND2  1 
ATOM   1962 N  N    . LYS   B 2 1   ? 4.63600   -16.05400 2.23000   1.000 123.68620 ?  625 LYS   C N    1 
ATOM   1963 C  CA   . LYS   B 2 1   ? 5.75400   -16.82200 2.78700   1.000 126.95961 ?  625 LYS   C CA   1 
ATOM   1964 C  C    . LYS   B 2 1   ? 6.90400   -16.91900 1.79900   1.000 130.13986 ?  625 LYS   C C    1 
ATOM   1965 O  O    . LYS   B 2 1   ? 8.05600   -17.12100 2.19700   1.000 135.52576 ?  625 LYS   C O    1 
ATOM   1966 C  CB   . LYS   B 2 1   ? 5.30800   -18.21500 3.21900   1.000 128.81515 ?  625 LYS   C CB   1 
ATOM   1967 C  CG   . LYS   B 2 1   ? 4.27800   -18.29000 4.36300   1.000 129.96177 ?  625 LYS   C CG   1 
ATOM   1968 C  CD   . LYS   B 2 1   ? 4.32300   -17.09100 5.30300   1.000 128.48256 ?  625 LYS   C CD   1 
ATOM   1969 C  CE   . LYS   B 2 1   ? 5.67800   -16.84700 6.03200   1.000 123.29409 ?  625 LYS   C CE   1 
ATOM   1970 N  NZ   . LYS   B 2 1   ? 5.72000   -15.49500 6.67100   1.000 114.93018 ?  625 LYS   C NZ   1 
ATOM   1971 N  N    . ASN   B 2 2   ? 6.59700   -16.80100 0.51600   1.000 126.12405 ?  626 ASN   C N    1 
ATOM   1972 C  CA   . ASN   B 2 2   ? 7.60800   -16.52400 -0.48700  1.000 118.87352 ?  626 ASN   C CA   1 
ATOM   1973 C  C    . ASN   B 2 2   ? 7.58700   -15.03500 -0.79900  1.000 105.59209 ?  626 ASN   C C    1 
ATOM   1974 O  O    . ASN   B 2 2   ? 6.54600   -14.38000 -0.71900  1.000 108.33005 ?  626 ASN   C O    1 
ATOM   1975 C  CB   . ASN   B 2 2   ? 7.40100   -17.36900 -1.74600  1.000 123.74566 ?  626 ASN   C CB   1 
ATOM   1976 C  CG   . ASN   B 2 2   ? 8.14500   -18.68900 -1.66600  1.000 132.28686 ?  626 ASN   C CG   1 
ATOM   1977 O  OD1  . ASN   B 2 2   ? 8.65400   -19.05100 -0.60300  1.000 137.04516 ?  626 ASN   C OD1  1 
ATOM   1978 N  ND2  . ASN   B 2 2   ? 8.25900   -19.38800 -2.79300  1.000 131.93779 ?  626 ASN   C ND2  1 
ATOM   1979 N  N    . HIS   B 2 3   ? 8.75400   -14.50300 -1.15400  1.000 91.12149  ?  627 HIS   C N    1 
ATOM   1980 C  CA   . HIS   B 2 3   ? 9.03500   -13.07200 -1.05600  1.000 77.87031  ?  627 HIS   C CA   1 
ATOM   1981 C  C    . HIS   B 2 3   ? 9.53500   -12.57900 -2.40500  1.000 72.60414  ?  627 HIS   C C    1 
ATOM   1982 O  O    . HIS   B 2 3   ? 10.74300  -12.38500 -2.60100  1.000 64.92095  ?  627 HIS   C O    1 
ATOM   1983 C  CB   . HIS   B 2 3   ? 10.05000  -12.80500 0.05600   1.000 70.03087  ?  627 HIS   C CB   1 
ATOM   1984 C  CG   . HIS   B 2 3   ? 9.94100   -13.75800 1.20800   1.000 67.84986  ?  627 HIS   C CG   1 
ATOM   1985 N  ND1  . HIS   B 2 3   ? 9.23200   -13.45900 2.35200   1.000 73.21775  ?  627 HIS   C ND1  1 
ATOM   1986 C  CD2  . HIS   B 2 3   ? 10.43400  -15.00700 1.38600   1.000 73.40556  ?  627 HIS   C CD2  1 
ATOM   1987 C  CE1  . HIS   B 2 3   ? 9.29800   -14.48100 3.18700   1.000 79.36162  ?  627 HIS   C CE1  1 
ATOM   1988 N  NE2  . HIS   B 2 3   ? 10.02400  -15.43200 2.62600   1.000 77.94936  ?  627 HIS   C NE2  1 
ATOM   1989 N  N    . PRO   B 2 4   ? 8.62900   -12.37900 -3.36600  1.000 70.80767  ?  628 PRO   C N    1 
ATOM   1990 C  CA   . PRO   B 2 4   ? 9.06900   -11.92600 -4.69400  1.000 74.80874  ?  628 PRO   C CA   1 
ATOM   1991 C  C    . PRO   B 2 4   ? 9.52700   -10.47900 -4.72300  1.000 69.30530  ?  628 PRO   C C    1 
ATOM   1992 O  O    . PRO   B 2 4   ? 10.43600  -10.14800 -5.49400  1.000 65.00813  ?  628 PRO   C O    1 
ATOM   1993 C  CB   . PRO   B 2 4   ? 7.82300   -12.14100 -5.56300  1.000 72.22944  ?  628 PRO   C CB   1 
ATOM   1994 C  CG   . PRO   B 2 4   ? 6.68300   -12.02500 -4.60400  1.000 74.24091  ?  628 PRO   C CG   1 
ATOM   1995 C  CD   . PRO   B 2 4   ? 7.17500   -12.60900 -3.30900  1.000 73.60060  ?  628 PRO   C CD   1 
ATOM   1996 N  N    . MET   B 2 5   ? 8.91800   -9.59900  -3.92200  1.000 64.01554  ?  629 MET   C N    1 
ATOM   1997 C  CA   . MET   B 2 5   ? 9.33800   -8.20100  -3.92000  1.000 55.89024  ?  629 MET   C CA   1 
ATOM   1998 C  C    . MET   B 2 5   ? 10.70200  -8.03700  -3.26500  1.000 54.15629  ?  629 MET   C C    1 
ATOM   1999 O  O    . MET   B 2 5   ? 11.55600  -7.30100  -3.77300  1.000 51.76056  ?  629 MET   C O    1 
ATOM   2000 C  CB   . MET   B 2 5   ? 8.29500   -7.33700  -3.21400  1.000 54.54341  ?  629 MET   C CB   1 
ATOM   2001 C  CG   . MET   B 2 5   ? 6.99800   -7.18900  -3.98700  1.000 62.86111  ?  629 MET   C CG   1 
ATOM   2002 S  SD   . MET   B 2 5   ? 5.76300   -6.25000  -3.07400  1.000 74.97387  ?  629 MET   C SD   1 
ATOM   2003 C  CE   . MET   B 2 5   ? 5.23600   -7.47400  -1.87900  1.000 78.21580  ?  629 MET   C CE   1 
ATOM   2004 N  N    . LEU   B 2 6   ? 10.92500  -8.71300  -2.13600  1.000 52.33560  ?  630 LEU   C N    1 
ATOM   2005 C  CA   . LEU   B 2 6   ? 12.24000  -8.67700  -1.50700  1.000 61.57567  ?  630 LEU   C CA   1 
ATOM   2006 C  C    . LEU   B 2 6   ? 13.29300  -9.30200  -2.41400  1.000 59.56299  ?  630 LEU   C C    1 
ATOM   2007 O  O    . LEU   B 2 6   ? 14.42900  -8.81900  -2.48100  1.000 58.45985  ?  630 LEU   C O    1 
ATOM   2008 C  CB   . LEU   B 2 6   ? 12.18700  -9.38700  -0.15300  1.000 51.82057  ?  630 LEU   C CB   1 
ATOM   2009 C  CG   . LEU   B 2 6   ? 13.45400  -9.60800  0.67800   1.000 63.61524  ?  630 LEU   C CG   1 
ATOM   2010 C  CD1  . LEU   B 2 6   ? 14.33500  -8.36800  0.73400   1.000 58.41403  ?  630 LEU   C CD1  1 
ATOM   2011 C  CD2  . LEU   B 2 6   ? 13.07200  -10.05900 2.08000   1.000 62.10761  ?  630 LEU   C CD2  1 
ATOM   2012 N  N    . MET   B 2 7   ? 12.92500  -10.35900 -3.14500  1.000 55.10049  ?  631 MET   C N    1 
ATOM   2013 C  CA   . MET   B 2 7   ? 13.89500  -11.04400 -3.99400  1.000 55.67558  ?  631 MET   C CA   1 
ATOM   2014 C  C    . MET   B 2 7   ? 14.27300  -10.20300 -5.20900  1.000 63.86696  ?  631 MET   C C    1 
ATOM   2015 O  O    . MET   B 2 7   ? 15.45400  -10.11800 -5.56400  1.000 54.69164  ?  631 MET   C O    1 
ATOM   2016 C  CB   . MET   B 2 7   ? 13.34900  -12.40300 -4.43100  1.000 60.30890  ?  631 MET   C CB   1 
ATOM   2017 C  CG   . MET   B 2 7   ? 14.40400  -13.49800 -4.48500  1.000 78.98796  ?  631 MET   C CG   1 
ATOM   2018 S  SD   . MET   B 2 7   ? 13.71700  -15.12300 -4.85800  1.000 95.73990  ?  631 MET   C SD   1 
ATOM   2019 C  CE   . MET   B 2 7   ? 12.38100  -15.21800 -3.66800  1.000 90.70652  ?  631 MET   C CE   1 
ATOM   2020 N  N    A ASN   B 2 8   ? 13.28100  -9.58900  -5.86200  0.470 54.27419  ?  632 ASN   C N    1 
ATOM   2021 N  N    B ASN   B 2 8   ? 13.29500  -9.57100  -5.86400  0.530 54.25920  ?  632 ASN   C N    1 
ATOM   2022 C  CA   A ASN   B 2 8   ? 13.56000  -8.72600  -7.00600  0.470 57.34190  ?  632 ASN   C CA   1 
ATOM   2023 C  CA   B ASN   B 2 8   ? 13.63000  -8.74900  -7.02300  0.530 57.38415  ?  632 ASN   C CA   1 
ATOM   2024 C  C    A ASN   B 2 8   ? 14.37700  -7.51200  -6.59000  0.470 57.78012  ?  632 ASN   C C    1 
ATOM   2025 C  C    B ASN   B 2 8   ? 14.34600  -7.46800  -6.61600  0.530 58.07586  ?  632 ASN   C C    1 
ATOM   2026 O  O    A ASN   B 2 8   ? 15.22800  -7.03500  -7.35100  0.470 58.46843  ?  632 ASN   C O    1 
ATOM   2027 O  O    B ASN   B 2 8   ? 15.10200  -6.90300  -7.41600  0.530 59.20129  ?  632 ASN   C O    1 
ATOM   2028 C  CB   A ASN   B 2 8   ? 12.25100  -8.29000  -7.66400  0.470 57.85812  ?  632 ASN   C CB   1 
ATOM   2029 C  CB   B ASN   B 2 8   ? 12.37500  -8.43100  -7.83700  0.530 58.59000  ?  632 ASN   C CB   1 
ATOM   2030 C  CG   A ASN   B 2 8   ? 12.46500  -7.30100  -8.79500  0.470 62.93365  ?  632 ASN   C CG   1 
ATOM   2031 C  CG   B ASN   B 2 8   ? 12.46600  -8.93600  -9.26800  0.530 64.95673  ?  632 ASN   C CG   1 
ATOM   2032 O  OD1  A ASN   B 2 8   ? 12.44000  -6.08700  -8.58800  0.470 56.22117  ?  632 ASN   C OD1  1 
ATOM   2033 O  OD1  B ASN   B 2 8   ? 12.50200  -8.15200  -10.21800 0.530 65.59938  ?  632 ASN   C OD1  1 
ATOM   2034 N  ND2  A ASN   B 2 8   ? 12.66900  -7.81700  -10.00300 0.470 66.69330  ?  632 ASN   C ND2  1 
ATOM   2035 N  ND2  B ASN   B 2 8   ? 12.51000  -10.25400 -9.42800  0.530 59.45998  ?  632 ASN   C ND2  1 
ATOM   2036 N  N    . LEU   B 2 9   ? 14.13000  -6.99400  -5.38600  1.000 52.44544  ?  633 LEU   C N    1 
ATOM   2037 C  CA   . LEU   B 2 9   ? 14.93500  -5.89400  -4.87300  1.000 58.80627  ?  633 LEU   C CA   1 
ATOM   2038 C  C    . LEU   B 2 9   ? 16.37300  -6.32700  -4.61800  1.000 57.64653  ?  633 LEU   C C    1 
ATOM   2039 O  O    . LEU   B 2 9   ? 17.25900  -5.47200  -4.53500  1.000 56.28657  ?  633 LEU   C O    1 
ATOM   2040 C  CB   . LEU   B 2 9   ? 14.31100  -5.32800  -3.59600  1.000 57.83757  ?  633 LEU   C CB   1 
ATOM   2041 C  CG   . LEU   B 2 9   ? 13.02900  -4.51100  -3.78800  1.000 65.84358  ?  633 LEU   C CG   1 
ATOM   2042 C  CD1  . LEU   B 2 9   ? 12.44300  -4.09000  -2.44700  1.000 50.57463  ?  633 LEU   C CD1  1 
ATOM   2043 C  CD2  . LEU   B 2 9   ? 13.28100  -3.29700  -4.67200  1.000 61.96876  ?  633 LEU   C CD2  1 
ATOM   2044 N  N    . LEU   B 2 10  ? 16.61800  -7.63200  -4.49900  1.000 66.25361  ?  634 LEU   C N    1 
ATOM   2045 C  CA   . LEU   B 2 10  ? 17.95700  -8.20300  -4.44500  1.000 71.15606  ?  634 LEU   C CA   1 
ATOM   2046 C  C    . LEU   B 2 10  ? 18.46300  -8.64900  -5.81100  1.000 83.60450  ?  634 LEU   C C    1 
ATOM   2047 O  O    . LEU   B 2 10  ? 19.56000  -9.21300  -5.89300  1.000 90.56178  ?  634 LEU   C O    1 
ATOM   2048 C  CB   . LEU   B 2 10  ? 17.98300  -9.39800  -3.48500  1.000 62.28355  ?  634 LEU   C CB   1 
ATOM   2049 C  CG   . LEU   B 2 10  ? 17.51400  -9.15700  -2.05200  1.000 59.43686  ?  634 LEU   C CG   1 
ATOM   2050 C  CD1  . LEU   B 2 10  ? 17.28300  -10.47300 -1.33000  1.000 64.18417  ?  634 LEU   C CD1  1 
ATOM   2051 C  CD2  . LEU   B 2 10  ? 18.52700  -8.32200  -1.31400  1.000 61.60575  ?  634 LEU   C CD2  1 
ATOM   2052 N  N    . LYS   B 2 11  ? 17.69200  -8.41400  -6.87200  1.000 87.28033  ?  635 LYS   C N    1 
ATOM   2053 C  CA   . LYS   B 2 11  ? 18.01000  -8.87600  -8.22400  1.000 89.42900  ?  635 LYS   C CA   1 
ATOM   2054 C  C    . LYS   B 2 11  ? 18.18500  -10.39100 -8.26800  1.000 93.02804  ?  635 LYS   C C    1 
ATOM   2055 O  O    . LYS   B 2 11  ? 17.24000  -11.12700 -8.55600  1.000 93.76342  ?  635 LYS   C O    1 
ATOM   2056 C  CB   . LYS   B 2 11  ? 19.27000  -8.18800  -8.75800  1.000 92.36793  ?  635 LYS   C CB   1 
ATOM   2057 C  CG   . LYS   B 2 11  ? 19.23700  -6.67400  -8.68100  1.000 95.66151  ?  635 LYS   C CG   1 
ATOM   2058 C  CD   . LYS   B 2 11  ? 20.64300  -6.11100  -8.54800  1.000 102.66620 ?  635 LYS   C CD   1 
ATOM   2059 C  CE   . LYS   B 2 11  ? 20.78800  -4.78800  -9.27900  1.000 103.76211 ?  635 LYS   C CE   1 
ATOM   2060 N  NZ   . LYS   B 2 11  ? 21.96100  -4.79400  -10.19500 1.000 104.21393 ?  635 LYS   C NZ   1 
HETATM 2061 C  C10  . A1L7X C 3 .   ? 8.29600   2.13500   13.10500  1.000 52.58862  ?  501 A1L7X A C10  1 
HETATM 2062 C  C13  . A1L7X C 3 .   ? 7.07000   4.56200   13.04000  1.000 56.03919  ?  501 A1L7X A C13  1 
HETATM 2063 C  C15  . A1L7X C 3 .   ? 10.28800  5.98400   15.32900  1.000 62.56625  ?  501 A1L7X A C15  1 
HETATM 2064 C  C20  . A1L7X C 3 .   ? 14.59300  7.56900   6.96800   1.000 53.88326  ?  501 A1L7X A C20  1 
HETATM 2065 C  C21  . A1L7X C 3 .   ? 15.57000  7.56800   5.80600   1.000 51.18528  ?  501 A1L7X A C21  1 
HETATM 2066 C  C22  . A1L7X C 3 .   ? 16.01100  6.15100   5.51100   1.000 54.68759  ?  501 A1L7X A C22  1 
HETATM 2067 C  C24  . A1L7X C 3 .   ? 4.39100   -0.23100  12.15900  1.000 52.55982  ?  501 A1L7X A C24  1 
HETATM 2068 C  C26  . A1L7X C 3 .   ? 4.89800   -0.74800  10.84400  1.000 45.61485  ?  501 A1L7X A C26  1 
HETATM 2069 C  C28  . A1L7X C 3 .   ? 4.56600   0.26800   9.78000   1.000 50.78426  ?  501 A1L7X A C28  1 
HETATM 2070 C  C01  . A1L7X C 3 .   ? 12.16900  8.02100   11.30100  1.000 47.88886  ?  501 A1L7X A C01  1 
HETATM 2071 C  C02  . A1L7X C 3 .   ? 12.46500  7.06700   10.36400  1.000 47.98988  ?  501 A1L7X A C02  1 
HETATM 2072 C  C03  . A1L7X C 3 .   ? 11.84900  5.86300   10.42800  1.000 46.79347  ?  501 A1L7X A C03  1 
HETATM 2073 C  C04  . A1L7X C 3 .   ? 10.95200  5.59200   11.42000  1.000 50.99259  ?  501 A1L7X A C04  1 
HETATM 2074 C  C05  . A1L7X C 3 .   ? 10.64700  6.51200   12.36500  1.000 48.12721  ?  501 A1L7X A C05  1 
HETATM 2075 C  C06  . A1L7X C 3 .   ? 11.26900  7.73100   12.31500  1.000 48.16095  ?  501 A1L7X A C06  1 
HETATM 2076 C  C08  . A1L7X C 3 .   ? 8.41500   4.50700   13.34300  1.000 57.65310  ?  501 A1L7X A C08  1 
HETATM 2077 C  C09  . A1L7X C 3 .   ? 9.00700   3.27300   13.37400  1.000 51.57921  ?  501 A1L7X A C09  1 
HETATM 2078 C  C11  . A1L7X C 3 .   ? 6.96800   2.20400   12.81900  1.000 47.61119  ?  501 A1L7X A C11  1 
HETATM 2079 C  C12  . A1L7X C 3 .   ? 6.35500   3.42400   12.78500  1.000 50.73822  ?  501 A1L7X A C12  1 
HETATM 2080 C  C14  . A1L7X C 3 .   ? 8.19300   7.51700   13.75100  1.000 63.78770  ?  501 A1L7X A C14  1 
HETATM 2081 C  C18  . A1L7X C 3 .   ? 14.17000  8.33100   9.31000   1.000 47.40942  ?  501 A1L7X A C18  1 
HETATM 2082 C  C19  . A1L7X C 3 .   ? 15.23400  8.04600   8.26100   1.000 51.18198  ?  501 A1L7X A C19  1 
HETATM 2083 C  C23  . A1L7X C 3 .   ? 4.94800   1.12500   12.46300  1.000 50.71844  ?  501 A1L7X A C23  1 
HETATM 2084 C  C25  . A1L7X C 3 .   ? 2.89200   -0.06900  12.08700  1.000 52.48193  ?  501 A1L7X A C25  1 
HETATM 2085 C  C27  . A1L7X C 3 .   ? 2.26000   -1.40600  11.78000  1.000 51.04070  ?  501 A1L7X A C27  1 
HETATM 2086 C  C33  . A1L7X C 3 .   ? 12.15000  4.82000   9.40500   1.000 52.95509  ?  501 A1L7X A C33  1 
HETATM 2087 C  C37  . A1L7X C 3 .   ? 8.96600   0.79700   13.16100  1.000 51.52554  ?  501 A1L7X A C37  1 
HETATM 2088 F  F34  . A1L7X C 3 .   ? 13.33500  4.30400   9.60600   1.000 57.90625  ?  501 A1L7X A F34  1 
HETATM 2089 F  F35  . A1L7X C 3 .   ? 12.13300  5.28700   8.17500   1.000 55.76949  ?  501 A1L7X A F35  1 
HETATM 2090 F  F36  . A1L7X C 3 .   ? 11.28000  3.84100   9.49400   1.000 58.49834  ?  501 A1L7X A F36  1 
HETATM 2091 F  F38  . A1L7X C 3 .   ? 10.25900  0.95100   13.31300  1.000 47.82405  ?  501 A1L7X A F38  1 
HETATM 2092 F  F39  . A1L7X C 3 .   ? 8.77000   0.07100   12.08200  1.000 44.42367  ?  501 A1L7X A F39  1 
HETATM 2093 F  F40  . A1L7X C 3 .   ? 8.50300   0.16800   14.21300  1.000 48.09605  ?  501 A1L7X A F40  1 
HETATM 2094 O  O16  . A1L7X C 3 .   ? 6.30300   1.02600   12.56800  1.000 45.52158  ?  501 A1L7X A O16  1 
HETATM 2095 O  O17  . A1L7X C 3 .   ? 13.34200  7.25100   9.33300   1.000 46.29051  ?  501 A1L7X A O17  1 
HETATM 2096 O  O29  . A1L7X C 3 .   ? 4.74600   -1.12600  13.13100  1.000 48.99726  ?  501 A1L7X A O29  1 
HETATM 2097 O  O30  . A1L7X C 3 .   ? 15.70900  5.27500   6.31000   1.000 41.97822  ?  501 A1L7X A O30  1 
HETATM 2098 O  O31  . A1L7X C 3 .   ? 16.65700  5.88600   4.49100   1.000 48.32772  -1 501 A1L7X A O31  1 
HETATM 2099 O  O32  . A1L7X C 3 .   ? 16.07200  7.05500   8.72600   1.000 50.44256  ?  501 A1L7X A O32  1 
HETATM 2100 SI SI07 . A1L7X C 3 .   ? 9.40100   6.08000   13.68900  1.000 58.34756  ?  501 A1L7X A SI07 1 
HETATM 2101 O  O    . HOH   D 4 .   ? 24.25500  -13.41700 -7.14700  1.000 116.80000 ?  601 HOH   A O    1 
HETATM 2102 O  O    . HOH   D 4 .   ? 17.56700  19.86800  16.47300  1.000 60.79704  ?  602 HOH   A O    1 
HETATM 2103 O  O    . HOH   D 4 .   ? 27.39100  -7.80000  -1.11600  1.000 42.42303  ?  603 HOH   A O    1 
HETATM 2104 O  O    . HOH   D 4 .   ? 7.60900   0.51100   -0.49100  1.000 53.36007  ?  604 HOH   A O    1 
HETATM 2105 O  O    . HOH   D 4 .   ? 12.31300  -7.03600  10.19100  1.000 43.83077  ?  605 HOH   A O    1 
HETATM 2106 O  O    . HOH   D 4 .   ? 19.92400  -10.44700 10.15800  1.000 48.70379  ?  606 HOH   A O    1 
HETATM 2107 O  O    . HOH   D 4 .   ? 25.27100  0.26300   25.14300  1.000 60.45412  ?  607 HOH   A O    1 
HETATM 2108 O  O    . HOH   D 4 .   ? 1.51700   3.20900   0.03800   1.000 43.37374  ?  608 HOH   A O    1 
HETATM 2109 O  O    . HOH   D 4 .   ? 24.49500  -18.63400 1.95100   1.000 40.79138  ?  609 HOH   A O    1 
HETATM 2110 O  O    . HOH   D 4 .   ? 20.65200  -7.33200  16.81900  1.000 40.91655  ?  610 HOH   A O    1 
HETATM 2111 O  O    . HOH   D 4 .   ? 22.74100  -9.14100  15.68700  1.000 44.46284  ?  611 HOH   A O    1 
HETATM 2112 O  O    . HOH   D 4 .   ? 21.31800  6.31900   9.19300   1.000 42.87836  ?  612 HOH   A O    1 
HETATM 2113 O  O    . HOH   D 4 .   ? 24.73100  -13.04000 15.69400  1.000 69.45553  ?  613 HOH   A O    1 
HETATM 2114 O  O    . HOH   D 4 .   ? 14.25900  10.87500  0.39200   1.000 43.08985  ?  614 HOH   A O    1 
HETATM 2115 O  O    . HOH   D 4 .   ? 7.01400   4.14100   0.72400   1.000 41.99134  ?  615 HOH   A O    1 
HETATM 2116 O  O    . HOH   D 4 .   ? 16.64900  7.89600   2.69500   1.000 41.02077  ?  616 HOH   A O    1 
HETATM 2117 O  O    . HOH   D 4 .   ? 21.64800  3.23200   4.55100   1.000 37.49092  ?  617 HOH   A O    1 
HETATM 2118 O  O    A HOH   D 4 .   ? 33.92800  10.22200  9.94100   0.740 53.74493  ?  618 HOH   A O    1 
HETATM 2119 O  O    B HOH   D 4 .   ? 32.97200  10.08300  9.06200   0.260 50.25498  ?  618 HOH   A O    1 
HETATM 2120 O  O    . HOH   D 4 .   ? 25.69300  9.42900   7.68300   1.000 62.83836  ?  619 HOH   A O    1 
HETATM 2121 O  O    . HOH   D 4 .   ? -1.38600  0.59400   1.00700   1.000 54.06662  ?  620 HOH   A O    1 
HETATM 2122 O  O    . HOH   D 4 .   ? 15.93900  -0.08000  24.74600  1.000 51.02318  ?  621 HOH   A O    1 
HETATM 2123 O  O    . HOH   D 4 .   ? 29.18100  0.49200   -1.98200  1.000 48.19510  ?  622 HOH   A O    1 
HETATM 2124 O  O    . HOH   D 4 .   ? 3.07500   -8.59000  0.32600   1.000 54.91622  ?  623 HOH   A O    1 
HETATM 2125 O  O    . HOH   D 4 .   ? 42.71400  -7.11800  7.56000   1.000 53.90782  ?  624 HOH   A O    1 
HETATM 2126 O  O    . HOH   D 4 .   ? 31.28700  10.69300  11.26900  1.000 52.73724  ?  625 HOH   A O    1 
HETATM 2127 O  O    . HOH   D 4 .   ? -5.309    -1.871    0.923     1.000 34.86318  ?  626 HOH   A O    1 
HETATM 2128 O  O    . HOH   D 4 .   ? 24.71500  5.14900   25.92000  1.000 52.71689  ?  627 HOH   A O    1 
HETATM 2129 O  O    . HOH   D 4 .   ? 37.91800  0.88400   23.48400  1.000 56.81478  ?  628 HOH   A O    1 
HETATM 2130 O  O    . HOH   D 4 .   ? 18.77500  -9.47500  23.36300  1.000 45.24364  ?  629 HOH   A O    1 
HETATM 2131 O  O    . HOH   D 4 .   ? 3.71700   12.98800  2.93500   1.000 52.15636  ?  630 HOH   A O    1 
HETATM 2132 O  O    . HOH   D 4 .   ? 17.90200  -19.72700 4.33500   1.000 38.20447  ?  631 HOH   A O    1 
HETATM 2133 O  O    . HOH   D 4 .   ? 25.58300  7.77000   17.64900  1.000 36.25615  ?  632 HOH   A O    1 
HETATM 2134 O  O    . HOH   D 4 .   ? 24.19800  6.62600   15.72500  1.000 45.59184  ?  633 HOH   A O    1 
HETATM 2135 O  O    . HOH   D 4 .   ? 24.00500  9.83400   3.28400   1.000 45.99768  ?  634 HOH   A O    1 
HETATM 2136 O  O    . HOH   D 4 .   ? 18.99500  7.27000   -1.25400  1.000 48.32619  ?  635 HOH   A O    1 
HETATM 2137 O  O    . HOH   D 4 .   ? 15.33000  10.01500  2.77000   1.000 48.65455  ?  636 HOH   A O    1 
HETATM 2138 O  O    . HOH   D 4 .   ? 35.98800  -0.56300  22.01200  1.000 48.40743  ?  637 HOH   A O    1 
HETATM 2139 O  O    . HOH   D 4 .   ? 22.81500  -23.00500 1.54600   1.000 48.52200  ?  638 HOH   A O    1 
HETATM 2140 O  O    . HOH   D 4 .   ? -4.51300  4.73700   2.50300   1.000 60.34334  ?  639 HOH   A O    1 
HETATM 2141 O  O    A HOH   D 4 .   ? 25.86200  -17.21400 -4.65900  0.460 29.63474  ?  640 HOH   A O    1 
HETATM 2142 O  O    B HOH   D 4 .   ? 24.43700  -16.78300 -6.13300  0.280 26.27660  ?  640 HOH   A O    1 
HETATM 2143 O  O    C HOH   D 4 .   ? 26.18600  -15.20000 -6.85500  0.250 25.89389  ?  640 HOH   A O    1 
HETATM 2144 O  O    . HOH   D 4 .   ? 18.50200  0.66200   25.14400  1.000 59.05773  ?  641 HOH   A O    1 
HETATM 2145 O  O    . HOH   D 4 .   ? 33.21900  -10.27300 3.17300   1.000 53.45727  ?  642 HOH   A O    1 
HETATM 2146 O  O    . HOH   D 4 .   ? 34.98200  -2.22200  23.89600  1.000 37.35882  ?  643 HOH   A O    1 
HETATM 2147 O  O    . HOH   D 4 .   ? 47.03400  1.03800   16.29200  1.000 80.12562  ?  644 HOH   A O    1 
HETATM 2148 O  O    . HOH   D 4 .   ? 23.29400  -14.92000 -5.00500  1.000 69.31995  ?  645 HOH   A O    1 
HETATM 2149 O  O    . HOH   D 4 .   ? 24.74900  10.41800  5.47700   1.000 57.02432  ?  646 HOH   A O    1 
HETATM 2150 O  O    . HOH   D 4 .   ? 38.10000  -0.10900  25.69000  1.000 61.04178  ?  647 HOH   A O    1 
HETATM 2151 O  O    . HOH   D 4 .   ? 36.60800  -12.92600 15.18700  1.000 60.20979  ?  648 HOH   A O    1 
HETATM 2152 O  O    A HOH   D 4 .   ? 15.14900  -22.60500 2.87700   0.580 38.56770  ?  649 HOH   A O    1 
HETATM 2153 O  O    B HOH   D 4 .   ? 15.31200  -24.02200 4.29600   0.420 31.76054  ?  649 HOH   A O    1 
HETATM 2154 O  O    . HOH   D 4 .   ? 10.87900  -8.77200  12.07200  1.000 65.38350  ?  650 HOH   A O    1 
HETATM 2155 O  O    . HOH   D 4 .   ? 25.26900  10.26100  17.22100  1.000 62.68392  ?  651 HOH   A O    1 
HETATM 2156 O  O    A HOH   D 4 .   ? -3.38800  -10.69800 7.66200   0.500 47.73910  ?  652 HOH   A O    1 
HETATM 2157 O  O    B HOH   D 4 .   ? -1.72900  -9.67800  7.47400   0.500 46.11733  ?  652 HOH   A O    1 
HETATM 2158 O  O    . HOH   D 4 .   ? 34.26800  11.54600  12.27300  1.000 66.73420  ?  653 HOH   A O    1 
HETATM 2159 O  O    A HOH   D 4 .   ? 25.08100  9.10500   11.69900  0.500 36.35900  ?  654 HOH   A O    1 
HETATM 2160 O  O    B HOH   D 4 .   ? 26.73900  9.02300   12.67800  0.500 32.74029  ?  654 HOH   A O    1 
HETATM 2161 O  O    . HOH   E 4 .   ? 17.27500  -2.51900  -3.88900  1.000 52.61859  ?  701 HOH   C 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    . LYS   A 18  ? 0.98763 1.40398 1.34568 -0.13244 -0.06830 -0.01006 123 LYS   A N    
2    C  CA   . LYS   A 18  ? 0.99231 1.44397 1.37816 -0.11721 -0.05487 -0.01417 123 LYS   A CA   
3    C  C    . LYS   A 18  ? 0.90228 1.32066 1.25745 -0.10816 -0.03729 -0.01038 123 LYS   A C    
4    O  O    . LYS   A 18  ? 0.88144 1.29599 1.23652 -0.08409 -0.03703 -0.01313 123 LYS   A O    
5    C  CB   . LYS   A 18  ? 0.96826 1.44350 1.37910 -0.09104 -0.07223 -0.01915 123 LYS   A CB   
6    C  CG   . LYS   A 18  ? 0.92600 1.36018 1.30425 -0.07859 -0.09309 -0.01301 123 LYS   A CG   
7    C  CD   . LYS   A 18  ? 0.93951 1.40133 1.34582 -0.05816 -0.11521 -0.01513 123 LYS   A CD   
8    C  CE   . LYS   A 18  ? 0.92599 1.39765 1.35234 -0.03072 -0.11003 -0.01840 123 LYS   A CE   
9    N  NZ   . LYS   A 18  ? 0.91399 1.40486 1.36601 -0.00818 -0.13489 -0.01819 123 LYS   A NZ   
10   N  N    . LEU   A 19  ? 0.79294 1.18582 1.12271 -0.12790 -0.02438 -0.00398 124 LEU   A N    
11   C  CA   . LEU   A 19  ? 0.67107 1.03400 0.97053 -0.12260 -0.00865 0.00016  124 LEU   A CA   
12   C  C    . LEU   A 19  ? 0.62375 1.02825 0.94572 -0.12179 0.01175  -0.00510 124 LEU   A C    
13   O  O    . LEU   A 19  ? 0.59771 1.02921 0.93282 -0.14394 0.02398  -0.00271 124 LEU   A O    
14   C  CB   . LEU   A 19  ? 0.53983 0.86143 0.80572 -0.14298 -0.00517 0.00959  124 LEU   A CB   
15   C  CG   . LEU   A 19  ? 0.63949 0.90936 0.86317 -0.13394 -0.00379 0.01495  124 LEU   A CG   
16   C  CD1  . LEU   A 19  ? 0.52974 0.78202 0.74332 -0.11150 -0.01742 0.01222  124 LEU   A CD1  
17   C  CD2  . LEU   A 19  ? 0.76046 0.99303 0.96006 -0.15252 -0.00713 0.02183  124 LEU   A CD2  
18   N  N    . SER   A 20  ? 0.52640 0.93636 0.85253 -0.09713 0.01559  -0.01270 125 SER   A N    
19   C  CA   . SER   A 20  ? 0.54871 0.99883 0.89388 -0.09308 0.03571  -0.02176 125 SER   A CA   
20   C  C    . SER   A 20  ? 0.46998 0.90233 0.78194 -0.10972 0.05465  -0.01422 125 SER   A C    
21   O  O    . SER   A 20  ? 0.41981 0.80384 0.69492 -0.11869 0.05062  -0.00281 125 SER   A O    
22   C  CB   . SER   A 20  ? 0.57431 1.02507 0.92873 -0.06114 0.03301  -0.03363 125 SER   A CB   
23   O  OG   . SER   A 20  ? 0.51894 0.91966 0.83315 -0.05318 0.03472  -0.02979 125 SER   A OG   
24   N  N    . GLU   A 21  ? 0.46814 0.94287 0.79372 -0.11335 0.07529  -0.02106 126 GLU   A N    
25   C  CA   . GLU   A 21  ? 0.50254 0.96359 0.79383 -0.12732 0.09289  -0.01355 126 GLU   A CA   
26   C  C    . GLU   A 21  ? 0.44024 0.85315 0.69519 -0.10930 0.08979  -0.01446 126 GLU   A C    
27   O  O    . GLU   A 21  ? 0.47759 0.85355 0.69491 -0.12064 0.09225  -0.00246 126 GLU   A O    
28   C  CB   . GLU   A 21  ? 0.40537 0.92669 0.71645 -0.13247 0.11651  -0.02300 126 GLU   A CB   
29   C  CG   . GLU   A 21  ? 0.47167 0.98398 0.74463 -0.15089 0.13455  -0.01255 126 GLU   A CG   
30   C  CD   . GLU   A 21  ? 0.57538 1.14150 0.86037 -0.15632 0.15694  -0.02030 126 GLU   A CD   
31   O  OE1  . GLU   A 21  ? 0.66038 1.21402 0.90870 -0.16681 0.16928  -0.01198 126 GLU   A OE1  
32   O  OE2  . GLU   A 21  ? 0.57822 1.18919 0.90441 -0.14663 0.15879  -0.03391 126 GLU   A OE2  
33   N  N    . GLU   A 22  ? 0.42521 0.83755 0.69278 -0.08145 0.08310  -0.02825 127 GLU   A N    
34   C  CA   . GLU   A 22  ? 0.48635 0.85210 0.72318 -0.06550 0.07789  -0.02921 127 GLU   A CA   
35   C  C    . GLU   A 22  ? 0.45876 0.77188 0.66720 -0.07228 0.06255  -0.01395 127 GLU   A C    
36   O  O    . GLU   A 22  ? 0.44893 0.72579 0.62278 -0.07519 0.06415  -0.00738 127 GLU   A O    
37   C  CB   . GLU   A 22  ? 0.61753 0.98806 0.87773 -0.03599 0.06945  -0.04479 127 GLU   A CB   
38   C  CG   . GLU   A 22  ? 0.83190 1.16760 1.06731 -0.02023 0.06988  -0.05118 127 GLU   A CG   
39   C  CD   . GLU   A 22  ? 1.00847 1.35749 1.27251 0.00768  0.06621  -0.07041 127 GLU   A CD   
40   O  OE1  . GLU   A 22  ? 1.05825 1.37945 1.32881 0.02317  0.04742  -0.06818 127 GLU   A OE1  
41   O  OE2  . GLU   A 22  ? 1.05406 1.44126 1.33383 0.01425  0.08186  -0.08785 127 GLU   A OE2  
42   N  N    . GLN   A 23  ? 0.51278 0.82412 0.73610 -0.07440 0.04728  -0.00959 128 GLN   A N    
43   C  CA   . GLN   A 23  ? 0.46272 0.72908 0.66022 -0.07988 0.03347  0.00167  128 GLN   A CA   
44   C  C    . GLN   A 23  ? 0.38555 0.63517 0.56051 -0.10349 0.03969  0.01306  128 GLN   A C    
45   O  O    . GLN   A 23  ? 0.47057 0.67927 0.61515 -0.10490 0.03572  0.02014  128 GLN   A O    
46   C  CB   . GLN   A 23  ? 0.47106 0.74437 0.68841 -0.07727 0.01571  0.00173  128 GLN   A CB   
47   C  CG   . GLN   A 23  ? 0.39709 0.66979 0.62731 -0.05255 0.00358  -0.00422 128 GLN   A CG   
48   C  CD   . GLN   A 23  ? 0.51398 0.80451 0.76769 -0.05008 -0.01417 -0.00417 128 GLN   A CD   
49   O  OE1  . GLN   A 23  ? 0.61044 0.92765 0.88195 -0.06558 -0.01488 -0.00436 128 GLN   A OE1  
50   N  NE2  . GLN   A 23  ? 0.53881 0.81430 0.79212 -0.03175 -0.02979 -0.00298 128 GLN   A NE2  
51   N  N    . GLN   A 24  ? 0.35591 0.63678 0.54690 -0.12243 0.04885  0.01548  129 GLN   A N    
52   C  CA   . GLN   A 24  ? 0.44843 0.71045 0.61785 -0.14556 0.05450  0.02851  129 GLN   A CA   
53   C  C    . GLN   A 24  ? 0.43323 0.67973 0.57262 -0.14369 0.06641  0.03238  129 GLN   A C    
54   O  O    . GLN   A 24  ? 0.41716 0.62646 0.52803 -0.15212 0.06374  0.04353  129 GLN   A O    
55   C  CB   . GLN   A 24  ? 0.43520 0.73645 0.62905 -0.16867 0.06291  0.03198  129 GLN   A CB   
56   C  CG   . GLN   A 24  ? 0.57772 0.89903 0.80382 -0.17333 0.05016  0.02746  129 GLN   A CG   
57   C  CD   . GLN   A 24  ? 0.59903 0.96734 0.85475 -0.19672 0.06019  0.02957  129 GLN   A CD   
58   O  OE1  . GLN   A 24  ? 0.59536 0.95785 0.83842 -0.22052 0.06969  0.04213  129 GLN   A OE1  
59   N  NE2  . GLN   A 24  ? 0.57051 0.98677 0.86695 -0.19075 0.05752  0.01839  129 GLN   A NE2  
60   N  N    . HIS   A 25  ? 0.40650 0.68193 0.55266 -0.13174 0.07856  0.02190  130 HIS   A N    
61   C  CA   . HIS   A 25  ? 0.45926 0.72295 0.57578 -0.12897 0.08881  0.02282  130 HIS   A CA   
62   C  C    . HIS   A 25  ? 0.39130 0.60594 0.48169 -0.11617 0.07688  0.02485  130 HIS   A C    
63   O  O    . HIS   A 25  ? 0.48285 0.67102 0.54336 -0.12271 0.07784  0.03425  130 HIS   A O    
64   C  CB   . HIS   A 25  ? 0.60086 0.90467 0.73217 -0.11497 0.10216  0.00573  130 HIS   A CB   
65   C  CG   . HIS   A 25  ? 0.69466 0.98556 0.79544 -0.10829 0.10993  0.00194  130 HIS   A CG   
66   N  ND1  . HIS   A 25  ? 0.70283 1.00354 0.77875 -0.12490 0.12359  0.01009  130 HIS   A ND1  
67   C  CD2  . HIS   A 25  ? 0.70207 0.97071 0.79230 -0.08813 0.10471  -0.00867 130 HIS   A CD2  
68   C  CE1  . HIS   A 25  ? 0.72007 1.00712 0.77096 -0.11423 0.12604  0.00315  130 HIS   A CE1  
69   N  NE2  . HIS   A 25  ? 0.68826 0.95530 0.74870 -0.09229 0.11484  -0.00892 130 HIS   A NE2  
70   N  N    . ILE   A 26  ? 0.38235 0.58607 0.48435 -0.09844 0.06496  0.01712  131 ILE   A N    
71   C  CA   . ILE   A 26  ? 0.40136 0.56297 0.48131 -0.08835 0.05434  0.01956  131 ILE   A CA   
72   C  C    . ILE   A 26  ? 0.46906 0.59975 0.53093 -0.10154 0.04689  0.03246  131 ILE   A C    
73   O  O    . ILE   A 26  ? 0.44193 0.54377 0.47909 -0.10093 0.04495  0.03764  131 ILE   A O    
74   C  CB   . ILE   A 26  ? 0.43923 0.59675 0.53531 -0.07058 0.04241  0.01233  131 ILE   A CB   
75   C  CG1  . ILE   A 26  ? 0.41580 0.59484 0.52851 -0.05394 0.04788  -0.00178 131 ILE   A CG1  
76   C  CG2  . ILE   A 26  ? 0.42155 0.53893 0.49563 -0.06487 0.03195  0.01734  131 ILE   A CG2  
77   C  CD1  . ILE   A 26  ? 0.48646 0.66457 0.62023 -0.03704 0.03470  -0.00683 131 ILE   A CD1  
78   N  N    . ILE   A 27  ? 0.39735 0.53430 0.47325 -0.11313 0.04174  0.03631  132 ILE   A N    
79   C  CA   . ILE   A 27  ? 0.44062 0.54709 0.50228 -0.12512 0.03393  0.04565  132 ILE   A CA   
80   C  C    . ILE   A 27  ? 0.47833 0.57379 0.52068 -0.13902 0.04153  0.05688  132 ILE   A C    
81   O  O    . ILE   A 27  ? 0.45904 0.52055 0.48065 -0.13963 0.03567  0.06351  132 ILE   A O    
82   C  CB   . ILE   A 27  ? 0.44628 0.56374 0.52881 -0.13623 0.02646  0.04509  132 ILE   A CB   
83   C  CG1  . ILE   A 27  ? 0.40224 0.52590 0.49781 -0.12184 0.01538  0.03623  132 ILE   A CG1  
84   C  CG2  . ILE   A 27  ? 0.45636 0.54104 0.52574 -0.14979 0.01895  0.05262  132 ILE   A CG2  
85   C  CD1  . ILE   A 27  ? 0.35989 0.49808 0.47595 -0.13182 0.00595  0.03376  132 ILE   A CD1  
86   N  N    . ALA   A 28  ? 0.43097 0.55688 0.47999 -0.15026 0.05441  0.05963  133 ALA   A N    
87   C  CA   . ALA   A 28  ? 0.43694 0.55452 0.46425 -0.16543 0.06155  0.07332  133 ALA   A CA   
88   C  C    . ALA   A 28  ? 0.45201 0.54987 0.45158 -0.15361 0.06209  0.07377  133 ALA   A C    
89   O  O    . ALA   A 28  ? 0.46982 0.53973 0.44671 -0.16033 0.05792  0.08627  133 ALA   A O    
90   C  CB   . ALA   A 28  ? 0.37003 0.53209 0.40856 -0.17951 0.07780  0.07495  133 ALA   A CB   
91   N  N    . ILE   A 29  ? 0.39292 0.50393 0.39542 -0.13587 0.06553  0.06006  134 ILE   A N    
92   C  CA   . ILE   A 29  ? 0.39368 0.48766 0.37231 -0.12538 0.06487  0.05830  134 ILE   A CA   
93   C  C    . ILE   A 29  ? 0.46775 0.52234 0.43612 -0.11902 0.05068  0.06234  134 ILE   A C    
94   O  O    . ILE   A 29  ? 0.47616 0.51010 0.42269 -0.11944 0.04720  0.06941  134 ILE   A O    
95   C  CB   . ILE   A 29  ? 0.45019 0.56361 0.43803 -0.10822 0.06998  0.04086  134 ILE   A CB   
96   C  CG1  . ILE   A 29  ? 0.48218 0.63884 0.47976 -0.11256 0.08587  0.03366  134 ILE   A CG1  
97   C  CG2  . ILE   A 29  ? 0.39941 0.49268 0.36450 -0.09860 0.06692  0.03769  134 ILE   A CG2  
98   C  CD1  . ILE   A 29  ? 0.58097 0.74597 0.55060 -0.12344 0.09633  0.03994  134 ILE   A CD1  
99   N  N    . LEU   A 30  ? 0.38977 0.43652 0.37379 -0.11279 0.04214  0.05743  135 LEU   A N    
100  C  CA   . LEU   A 30  ? 0.38686 0.40282 0.36228 -0.10578 0.03083  0.05839  135 LEU   A CA   
101  C  C    . LEU   A 30  ? 0.42641 0.41863 0.39381 -0.11669 0.02442  0.06901  135 LEU   A C    
102  O  O    . LEU   A 30  ? 0.52207 0.48998 0.47689 -0.11168 0.01752  0.07167  135 LEU   A O    
103  C  CB   . LEU   A 30  ? 0.40893 0.42658 0.39965 -0.09677 0.02425  0.05018  135 LEU   A CB   
104  C  CG   . LEU   A 30  ? 0.42590 0.45611 0.42417 -0.08322 0.02607  0.04106  135 LEU   A CG   
105  C  CD1  . LEU   A 30  ? 0.39865 0.42941 0.40970 -0.07699 0.01754  0.03746  135 LEU   A CD1  
106  C  CD2  . LEU   A 30  ? 0.36951 0.38412 0.35166 -0.07531 0.02556  0.03974  135 LEU   A CD2  
107  N  N    . LEU   A 31  ? 0.49249 0.49116 0.46949 -0.13148 0.02569  0.07457  136 LEU   A N    
108  C  CA   . LEU   A 31  ? 0.54205 0.51335 0.51196 -0.14316 0.01853  0.08554  136 LEU   A CA   
109  C  C    . LEU   A 31  ? 0.56989 0.52906 0.51755 -0.14754 0.02033  0.09863  136 LEU   A C    
110  O  O    . LEU   A 31  ? 0.57817 0.50632 0.51487 -0.14513 0.01045  0.10487  136 LEU   A O    
111  C  CB   . LEU   A 31  ? 0.46938 0.45119 0.45540 -0.16142 0.01968  0.08970  136 LEU   A CB   
112  C  CG   . LEU   A 31  ? 0.43495 0.42088 0.44094 -0.15967 0.01240  0.07835  136 LEU   A CG   
113  C  CD1  . LEU   A 31  ? 0.50754 0.50995 0.53203 -0.17999 0.01406  0.08230  136 LEU   A CD1  
114  C  CD2  . LEU   A 31  ? 0.55570 0.50622 0.55495 -0.15267 -0.00067 0.07389  136 LEU   A CD2  
115  N  N    . ASP   A 32  ? 0.58271 0.56771 0.52334 -0.15302 0.03228  0.10207  137 ASP   A N    
116  C  CA   . ASP   A 32  ? 0.54350 0.52081 0.45861 -0.15778 0.03368  0.11488  137 ASP   A CA   
117  C  C    . ASP   A 32  ? 0.56740 0.53048 0.46942 -0.14044 0.02714  0.10928  137 ASP   A C    
118  O  O    . ASP   A 32  ? 0.57765 0.51886 0.46192 -0.14070 0.01915  0.12030  137 ASP   A O    
119  C  CB   . ASP   A 32  ? 0.56071 0.57530 0.47007 -0.16710 0.04971  0.11616  137 ASP   A CB   
120  C  CG   . ASP   A 32  ? 0.66602 0.67768 0.54414 -0.17083 0.05144  0.12745  137 ASP   A CG   
121  O  OD1  . ASP   A 32  ? 0.64719 0.67348 0.51546 -0.15928 0.05609  0.11635  137 ASP   A OD1  
122  O  OD2  . ASP   A 32  ? 0.63763 0.63110 0.50316 -0.18201 0.04609  0.14483  137 ASP   A OD2  
123  N  N    . ALA   A 33  ? 0.55438 0.52959 0.46624 -0.12583 0.02924  0.09309  138 ALA   A N    
124  C  CA   . ALA   A 33  ? 0.47598 0.43914 0.37948 -0.11157 0.02281  0.08729  138 ALA   A CA   
125  C  C    . ALA   A 33  ? 0.54201 0.47585 0.44740 -0.10674 0.00991  0.09053  138 ALA   A C    
126  O  O    . ALA   A 33  ? 0.52269 0.44286 0.41692 -0.10082 0.00256  0.09402  138 ALA   A O    
127  C  CB   . ALA   A 33  ? 0.39980 0.37764 0.31609 -0.09948 0.02641  0.07128  138 ALA   A CB   
128  N  N    . HIS   A 34  ? 0.46947 0.39557 0.39003 -0.10854 0.00651  0.08773  139 HIS   A N    
129  C  CA   . HIS   A 34  ? 0.50353 0.40414 0.42760 -0.10251 -0.00478 0.08648  139 HIS   A CA   
130  C  C    . HIS   A 34  ? 0.52391 0.39910 0.43781 -0.10881 -0.01311 0.10080  139 HIS   A C    
131  O  O    . HIS   A 34  ? 0.53594 0.39327 0.44621 -0.09917 -0.02261 0.10154  139 HIS   A O    
132  C  CB   . HIS   A 34  ? 0.45242 0.35252 0.39259 -0.10430 -0.00651 0.07828  139 HIS   A CB   
133  C  CG   . HIS   A 34  ? 0.52131 0.39902 0.46540 -0.09679 -0.01667 0.07211  139 HIS   A CG   
134  N  ND1  . HIS   A 34  ? 0.52061 0.39708 0.46345 -0.08276 -0.01942 0.06437  139 HIS   A ND1  
135  C  CD2  . HIS   A 34  ? 0.56393 0.42123 0.51447 -0.10133 -0.02444 0.07062  139 HIS   A CD2  
136  C  CE1  . HIS   A 34  ? 0.56105 0.42046 0.50945 -0.07762 -0.02723 0.05739  139 HIS   A CE1  
137  N  NE2  . HIS   A 34  ? 0.57178 0.41697 0.52438 -0.08806 -0.03111 0.06025  139 HIS   A NE2  
138  N  N    . HIS   A 35  ? 0.48880 0.36256 0.39951 -0.12535 -0.01037 0.11311  140 HIS   A N    
139  C  CA   . HIS   A 35  ? 0.53837 0.38361 0.43819 -0.13366 -0.01978 0.13049  140 HIS   A CA   
140  C  C    . HIS   A 35  ? 0.63982 0.48436 0.51820 -0.12968 -0.02231 0.14084  140 HIS   A C    
141  O  O    . HIS   A 35  ? 0.79665 0.61335 0.66638 -0.12871 -0.03506 0.15346  140 HIS   A O    
142  C  CB   . HIS   A 35  ? 0.54428 0.39177 0.44473 -0.15608 -0.01476 0.14352  140 HIS   A CB   
143  C  CG   . HIS   A 35  ? 0.67375 0.52382 0.59628 -0.16181 -0.01415 0.13327  140 HIS   A CG   
144  N  ND1  . HIS   A 35  ? 0.65203 0.52384 0.58372 -0.17952 -0.00499 0.13692  140 HIS   A ND1  
145  C  CD2  . HIS   A 35  ? 0.63543 0.47274 0.57269 -0.15200 -0.02182 0.11817  140 HIS   A CD2  
146  C  CE1  . HIS   A 35  ? 0.66923 0.53932 0.62062 -0.18131 -0.00887 0.12562  140 HIS   A CE1  
147  N  NE2  . HIS   A 35  ? 0.64891 0.49780 0.60209 -0.16446 -0.01892 0.11370  140 HIS   A NE2  
148  N  N    . LYS   A 36  ? 0.62324 0.49703 0.49324 -0.12670 -0.01197 0.13499  141 LYS   A N    
149  C  CA   . LYS   A 36  ? 0.62630 0.50223 0.47511 -0.12244 -0.01544 0.14151  141 LYS   A CA   
150  C  C    . LYS   A 36  ? 0.63710 0.50305 0.49211 -0.10403 -0.02620 0.13203  141 LYS   A C    
151  O  O    . LYS   A 36  ? 0.68090 0.53935 0.52230 -0.09949 -0.03580 0.13988  141 LYS   A O    
152  C  CB   . LYS   A 36  ? 0.67213 0.58246 0.51083 -0.12508 -0.00113 0.13449  141 LYS   A CB   
153  C  CG   . LYS   A 36  ? 0.75594 0.68306 0.58080 -0.14376 0.00997  0.14666  141 LYS   A CG   
154  C  CD   . LYS   A 36  ? 0.83448 0.79886 0.65463 -0.14234 0.02518  0.13284  141 LYS   A CD   
155  C  CE   . LYS   A 36  ? 0.94892 0.93723 0.75294 -0.16085 0.03824  0.14377  141 LYS   A CE   
156  N  NZ   . LYS   A 36  ? 0.93037 0.95870 0.74305 -0.15935 0.05567  0.12586  141 LYS   A NZ   
157  N  N    . THR   A 37  ? 0.60129 0.46999 0.47660 -0.09405 -0.02497 0.11575  142 THR   A N    
158  C  CA   . THR   A 37  ? 0.55911 0.42766 0.44230 -0.07847 -0.03147 0.10509  142 THR   A CA   
159  C  C    . THR   A 37  ? 0.59853 0.44801 0.49835 -0.06951 -0.04039 0.09940  142 THR   A C    
160  O  O    . THR   A 37  ? 0.64409 0.49674 0.55250 -0.05677 -0.04529 0.09055  142 THR   A O    
161  C  CB   . THR   A 37  ? 0.58489 0.47723 0.47524 -0.07394 -0.02163 0.08994  142 THR   A CB   
162  O  OG1  . THR   A 37  ? 0.56024 0.45927 0.46118 -0.07898 -0.01337 0.08457  142 THR   A OG1  
163  C  CG2  . THR   A 37  ? 0.51881 0.42838 0.39352 -0.07716 -0.01614 0.09044  142 THR   A CG2  
164  N  N    . TYR   A 38  ? 0.58488 0.41680 0.49067 -0.07604 -0.04242 0.10246  143 TYR   A N    
165  C  CA   . TYR   A 38  ? 0.54085 0.35219 0.46134 -0.06696 -0.05179 0.09451  143 TYR   A CA   
166  C  C    . TYR   A 38  ? 0.60651 0.38405 0.52263 -0.07143 -0.06462 0.10973  143 TYR   A C    
167  O  O    . TYR   A 38  ? 0.67969 0.44624 0.59080 -0.08741 -0.06313 0.12093  143 TYR   A O    
168  C  CB   . TYR   A 38  ? 0.53637 0.35267 0.46897 -0.06994 -0.04582 0.08151  143 TYR   A CB   
169  C  CG   . TYR   A 38  ? 0.61511 0.41815 0.56148 -0.05773 -0.05331 0.06687  143 TYR   A CG   
170  C  CD1  . TYR   A 38  ? 0.70784 0.47900 0.65989 -0.05878 -0.06423 0.06793  143 TYR   A CD1  
171  C  CD2  . TYR   A 38  ? 0.62575 0.44840 0.57938 -0.04564 -0.04934 0.05139  143 TYR   A CD2  
172  C  CE1  . TYR   A 38  ? 0.73284 0.49293 0.69798 -0.04577 -0.07081 0.05064  143 TYR   A CE1  
173  C  CE2  . TYR   A 38  ? 0.51284 0.32899 0.47815 -0.03423 -0.05421 0.03578  143 TYR   A CE2  
174  C  CZ   . TYR   A 38  ? 0.63234 0.41762 0.60361 -0.03313 -0.06487 0.03383  143 TYR   A CZ   
175  O  OH   . TYR   A 38  ? 0.61599 0.39564 0.59942 -0.02007 -0.06947 0.01451  143 TYR   A OH   
176  N  N    . ASP   A 39  ? 0.64506 0.40650 0.56485 -0.05766 -0.07798 0.11073  144 ASP   A N    
177  C  CA   . ASP   A 39  ? 0.62668 0.35023 0.54431 -0.05859 -0.09396 0.12566  144 ASP   A CA   
178  C  C    . ASP   A 39  ? 0.78643 0.48603 0.72500 -0.04826 -0.10232 0.11032  144 ASP   A C    
179  O  O    . ASP   A 39  ? 0.80270 0.50386 0.75574 -0.02852 -0.10883 0.09614  144 ASP   A O    
180  C  CB   . ASP   A 39  ? 0.70533 0.42532 0.61549 -0.04776 -0.10648 0.13636  144 ASP   A CB   
181  C  CG   . ASP   A 39  ? 0.83639 0.51314 0.74723 -0.04455 -0.12677 0.15173  144 ASP   A CG   
182  O  OD1  . ASP   A 39  ? 0.84763 0.49789 0.75567 -0.05866 -0.12873 0.16191  144 ASP   A OD1  
183  O  OD2  . ASP   A 39  ? 0.92354 0.59382 0.83974 -0.02793 -0.14138 0.15336  144 ASP   A OD2  
184  N  N    . PRO   A 40  ? 0.83446 0.51376 0.77662 -0.06089 -0.10251 0.11067  145 PRO   A N    
185  C  CA   . PRO   A 40  ? 0.81858 0.47551 0.77979 -0.05086 -0.11055 0.09169  145 PRO   A CA   
186  C  C    . PRO   A 40  ? 0.86721 0.48380 0.83726 -0.03700 -0.13097 0.09529  145 PRO   A C    
187  O  O    . PRO   A 40  ? 0.87532 0.47370 0.86304 -0.02442 -0.13848 0.07552  145 PRO   A O    
188  C  CB   . PRO   A 40  ? 0.82010 0.46555 0.78109 -0.07197 -0.10698 0.09425  145 PRO   A CB   
189  C  CG   . PRO   A 40  ? 0.84514 0.49105 0.78837 -0.09242 -0.10345 0.12183  145 PRO   A CG   
190  C  CD   . PRO   A 40  ? 0.83509 0.51274 0.76520 -0.08556 -0.09576 0.12738  145 PRO   A CD   
191  N  N    . THR   A 41  ? 0.84214 0.44403 0.80028 -0.03808 -0.14118 0.11907  146 THR   A N    
192  C  CA   . THR   A 41  ? 0.90175 0.47498 0.87074 -0.02103 -0.15995 0.12090  146 THR   A CA   
193  C  C    . THR   A 41  ? 0.88464 0.47328 0.86718 0.00511  -0.16637 0.10770  146 THR   A C    
194  O  O    . THR   A 41  ? 0.94539 0.51278 0.94539 0.02480  -0.18255 0.10137  146 THR   A O    
195  C  CB   . THR   A 41  ? 0.96077 0.52611 0.91172 -0.03252 -0.16485 0.14880  146 THR   A CB   
196  O  OG1  . THR   A 41  ? 0.92427 0.51201 0.86166 -0.02734 -0.16578 0.16007  146 THR   A OG1  
197  C  CG2  . THR   A 41  ? 0.94989 0.52166 0.88524 -0.06050 -0.15139 0.16219  146 THR   A CG2  
198  N  N    . TYR   A 42  ? 0.78804 0.42450 0.76577 0.00561  -0.15042 0.10010  147 TYR   A N    
199  C  CA   . TYR   A 42  ? 0.78074 0.44723 0.77346 0.02694  -0.15117 0.08516  147 TYR   A CA   
200  C  C    . TYR   A 42  ? 0.84652 0.49722 0.84058 0.03951  -0.17177 0.10103  147 TYR   A C    
201  O  O    . TYR   A 42  ? 0.74643 0.40278 0.76384 0.06264  -0.18189 0.08744  147 TYR   A O    
202  C  CB   . TYR   A 42  ? 0.77963 0.45277 0.79831 0.04436  -0.14876 0.05425  147 TYR   A CB   
203  C  CG   . TYR   A 42  ? 0.76711 0.45114 0.78203 0.03170  -0.13219 0.04021  147 TYR   A CG   
204  C  CD1  . TYR   A 42  ? 0.78734 0.43991 0.80872 0.02952  -0.13712 0.03035  147 TYR   A CD1  
205  C  CD2  . TYR   A 42  ? 0.75660 0.48066 0.76173 0.02184  -0.11363 0.03707  147 TYR   A CD2  
206  C  CE1  . TYR   A 42  ? 0.79849 0.46332 0.81587 0.01776  -0.12403 0.01761  147 TYR   A CE1  
207  C  CE2  . TYR   A 42  ? 0.75336 0.48758 0.75492 0.01123  -0.10100 0.02608  147 TYR   A CE2  
208  C  CZ   . TYR   A 42  ? 0.80782 0.51431 0.81507 0.00914  -0.10631 0.01644  147 TYR   A CZ   
209  O  OH   . TYR   A 42  ? 0.88139 0.60042 0.88466 -0.00149 -0.09564 0.00544  147 TYR   A OH   
210  N  N    . ALA   A 43  ? 0.83280 0.46675 0.80146 0.02408  -0.17812 0.13015  148 ALA   A N    
211  C  CA   . ALA   A 43  ? 0.90796 0.52585 0.87315 0.03324  -0.19857 0.14835  148 ALA   A CA   
212  C  C    . ALA   A 43  ? 0.91220 0.56573 0.88367 0.04832  -0.20282 0.14343  148 ALA   A C    
213  O  O    . ALA   A 43  ? 0.99829 0.64506 0.98382 0.06699  -0.22199 0.14574  148 ALA   A O    
214  C  CB   . ALA   A 43  ? 0.94011 0.55184 0.87378 0.00945  -0.19485 0.17510  148 ALA   A CB   
215  N  N    . ASP   A 44  ? 0.84544 0.54259 0.80951 0.03991  -0.18333 0.13386  149 ASP   A N    
216  C  CA   . ASP   A 44  ? 0.86530 0.60013 0.83358 0.04889  -0.18539 0.12929  149 ASP   A CA   
217  C  C    . ASP   A 44  ? 0.82102 0.57965 0.82665 0.07186  -0.18689 0.10337  149 ASP   A C    
218  O  O    . ASP   A 44  ? 0.73154 0.52190 0.74685 0.08044  -0.19141 0.09912  149 ASP   A O    
219  C  CB   . ASP   A 44  ? 0.81732 0.58649 0.76612 0.03131  -0.16498 0.12712  149 ASP   A CB   
220  C  CG   . ASP   A 44  ? 0.89604 0.65253 0.80831 0.01007  -0.16261 0.15084  149 ASP   A CG   
221  O  OD1  . ASP   A 44  ? 0.93638 0.67122 0.83282 0.00943  -0.18009 0.17299  149 ASP   A OD1  
222  O  OD2  . ASP   A 44  ? 0.87748 0.64719 0.77699 -0.00578 -0.14349 0.14764  149 ASP   A OD2  
223  N  N    . PHE   A 45  ? 0.78984 0.53694 0.81681 0.08123  -0.18301 0.08496  150 PHE   A N    
224  C  CA   . PHE   A 45  ? 0.78055 0.55560 0.84275 0.10268  -0.18165 0.05815  150 PHE   A CA   
225  C  C    . PHE   A 45  ? 0.78398 0.55629 0.86909 0.12624  -0.20549 0.05996  150 PHE   A C    
226  O  O    . PHE   A 45  ? 0.81026 0.61798 0.92646 0.14394  -0.20469 0.03923  150 PHE   A O    
227  C  CB   . PHE   A 45  ? 0.79856 0.55860 0.87520 0.10834  -0.17434 0.03735  150 PHE   A CB   
228  C  CG   . PHE   A 45  ? 0.82372 0.60332 0.88772 0.09086  -0.15004 0.02745  150 PHE   A CG   
229  C  CD1  . PHE   A 45  ? 0.73291 0.51146 0.76755 0.06737  -0.14012 0.04474  150 PHE   A CD1  
230  C  CD2  . PHE   A 45  ? 0.80903 0.60938 0.89046 0.09876  -0.13777 0.00048  150 PHE   A CD2  
231  C  CE1  . PHE   A 45  ? 0.73039 0.52600 0.75615 0.05357  -0.12045 0.03617  150 PHE   A CE1  
232  C  CE2  . PHE   A 45  ? 0.74059 0.55776 0.80882 0.08305  -0.11805 -0.00633 150 PHE   A CE2  
233  C  CZ   . PHE   A 45  ? 0.67409 0.48758 0.71583 0.06116  -0.11043 0.01200  150 PHE   A CZ   
234  N  N    . ARG   A 46  ? 0.86229 0.59505 0.93345 0.12654  -0.22708 0.08507  151 ARG   A N    
235  C  CA   . ARG   A 46  ? 1.00169 0.73037 1.09222 0.14888  -0.25330 0.09103  151 ARG   A CA   
236  C  C    . ARG   A 46  ? 0.96137 0.73775 1.05227 0.14898  -0.25461 0.09314  151 ARG   A C    
237  O  O    . ARG   A 46  ? 1.00882 0.80382 1.12909 0.17104  -0.27109 0.08628  151 ARG   A O    
238  C  CB   . ARG   A 46  ? 1.05689 0.74024 1.12316 0.13953  -0.26647 0.11788  151 ARG   A CB   
239  C  CG   . ARG   A 46  ? 1.24701 0.93071 1.32398 0.15507  -0.28692 0.12631  151 ARG   A CG   
240  C  CD   . ARG   A 46  ? 1.35810 0.99276 1.42034 0.14895  -0.29731 0.14541  151 ARG   A CD   
241  N  NE   . ARG   A 46  ? 1.39774 1.03025 1.44819 0.15144  -0.31502 0.16732  151 ARG   A NE   
242  C  CZ   . ARG   A 46  ? 1.47832 1.07167 1.51470 0.14664  -0.32713 0.18799  151 ARG   A CZ   
243  N  NH1  . ARG   A 46  ? 1.48562 1.03937 1.51960 0.13814  -0.32346 0.18894  151 ARG   A NH1  
244  N  NH2  . ARG   A 46  ? 1.50208 1.09650 1.52686 0.14977  -0.34362 0.20785  151 ARG   A NH2  
245  N  N    . ASP   A 47  ? 0.87772 0.67562 0.93953 0.12549  -0.23810 0.10023  152 ASP   A N    
246  C  CA   . ASP   A 47  ? 0.92278 0.76234 0.98188 0.12243  -0.23990 0.10163  152 ASP   A CA   
247  C  C    . ASP   A 47  ? 0.83727 0.72893 0.92678 0.12741  -0.22381 0.07408  152 ASP   A C    
248  O  O    . ASP   A 47  ? 0.78408 0.71256 0.87911 0.12613  -0.22700 0.07215  152 ASP   A O    
249  C  CB   . ASP   A 47  ? 0.98233 0.82046 0.99697 0.09569  -0.22996 0.11917  152 ASP   A CB   
250  C  CG   . ASP   A 47  ? 1.04132 0.83173 1.02277 0.08515  -0.23983 0.14686  152 ASP   A CG   
251  O  OD1  . ASP   A 47  ? 1.13589 0.89164 1.12744 0.09919  -0.26029 0.15683  152 ASP   A OD1  
252  O  OD2  . ASP   A 47  ? 1.05778 0.84558 1.00442 0.06274  -0.22717 0.15849  152 ASP   A OD2  
253  N  N    . PHE   A 48  ? 0.70398 0.60060 0.81187 0.13129  -0.20707 0.05341  153 PHE   A N    
254  C  CA   . PHE   A 48  ? 0.61174 0.55890 0.74622 0.13370  -0.19061 0.02947  153 PHE   A CA   
255  C  C    . PHE   A 48  ? 0.60595 0.58094 0.78437 0.15979  -0.20484 0.01490  153 PHE   A C    
256  O  O    . PHE   A 48  ? 0.64313 0.59219 0.83450 0.17954  -0.22685 0.01981  153 PHE   A O    
257  C  CB   . PHE   A 48  ? 0.57522 0.52126 0.71152 0.12889  -0.16832 0.01265  153 PHE   A CB   
258  C  CG   . PHE   A 48  ? 0.56656 0.48869 0.66578 0.10539  -0.15445 0.02445  153 PHE   A CG   
259  C  CD1  . PHE   A 48  ? 0.58710 0.49706 0.68319 0.10119  -0.13999 0.01379  153 PHE   A CD1  
260  C  CD2  . PHE   A 48  ? 0.56665 0.48208 0.63534 0.08814  -0.15592 0.04419  153 PHE   A CD2  
261  C  CE1  . PHE   A 48  ? 0.57147 0.46356 0.63799 0.08082  -0.12836 0.02379  153 PHE   A CE1  
262  C  CE2  . PHE   A 48  ? 0.59030 0.48868 0.62955 0.06850  -0.14258 0.05270  153 PHE   A CE2  
263  C  CZ   . PHE   A 48  ? 0.57847 0.46561 0.61831 0.06506  -0.12923 0.04304  153 PHE   A CZ   
264  N  N    . ARG   A 49  ? 0.54842 0.57738 0.75170 0.15959  -0.19253 -0.00284 154 ARG   A N    
265  C  CA   . ARG   A 49  ? 0.62593 0.69090 0.87714 0.18434  -0.20040 -0.02229 154 ARG   A CA   
266  C  C    . ARG   A 49  ? 0.66059 0.70867 0.93009 0.20244  -0.19575 -0.04108 154 ARG   A C    
267  O  O    . ARG   A 49  ? 0.66955 0.70101 0.91981 0.19069  -0.17755 -0.04607 154 ARG   A O    
268  C  CB   . ARG   A 49  ? 0.69489 0.82398 0.96845 0.17578  -0.18401 -0.03760 154 ARG   A CB   
269  C  CG   . ARG   A 49  ? 0.61855 0.77050 0.88710 0.16413  -0.19471 -0.02487 154 ARG   A CG   
270  C  CD   . ARG   A 49  ? 0.56746 0.77594 0.85372 0.14904  -0.17625 -0.03797 154 ARG   A CD   
271  N  NE   . ARG   A 49  ? 0.53007 0.72681 0.78266 0.12261  -0.15408 -0.03325 154 ARG   A NE   
272  C  CZ   . ARG   A 49  ? 0.42414 0.65823 0.68459 0.10554  -0.13512 -0.04175 154 ARG   A CZ   
273  N  NH1  . ARG   A 49  ? 0.43667 0.72587 0.73763 0.10984  -0.13371 -0.05561 154 ARG   A NH1  
274  N  NH2  . ARG   A 49  ? 0.38165 0.59860 0.61096 0.08380  -0.11818 -0.03565 154 ARG   A NH2  
275  N  N    . PRO   A 50  ? 0.65419 0.70596 0.96136 0.23187  -0.21313 -0.05305 155 PRO   A N    
276  C  CA   . PRO   A 50  ? 0.79525 0.81957 1.11744 0.25127  -0.21357 -0.07089 155 PRO   A CA   
277  C  C    . PRO   A 50  ? 0.76605 0.82956 1.10084 0.24871  -0.18488 -0.09979 155 PRO   A C    
278  O  O    . PRO   A 50  ? 0.64643 0.77165 1.00275 0.24602  -0.17087 -0.11305 155 PRO   A O    
279  C  CB   . PRO   A 50  ? 0.72166 0.75169 1.08408 0.28251  -0.23734 -0.07837 155 PRO   A CB   
280  C  CG   . PRO   A 50  ? 0.71632 0.80452 1.09845 0.28076  -0.23998 -0.07676 155 PRO   A CG   
281  C  CD   . PRO   A 50  ? 0.65995 0.74138 0.99986 0.25015  -0.23511 -0.05217 155 PRO   A CD   
282  N  N    . PRO   A 51  ? 0.79961 0.82997 1.12029 0.24770  -0.17580 -0.10951 156 PRO   A N    
283  C  CA   . PRO   A 51  ? 0.75399 0.82179 1.08864 0.25061  -0.15184 -0.14026 156 PRO   A CA   
284  C  C    . PRO   A 51  ? 0.81225 0.90880 1.19734 0.28490  -0.15908 -0.16995 156 PRO   A C    
285  O  O    . PRO   A 51  ? 0.92684 0.98166 1.32133 0.30384  -0.17849 -0.17152 156 PRO   A O    
286  C  CB   . PRO   A 51  ? 0.75491 0.77124 1.05875 0.24117  -0.14649 -0.14044 156 PRO   A CB   
287  C  CG   . PRO   A 51  ? 0.79502 0.74559 1.08923 0.24756  -0.17347 -0.11922 156 PRO   A CG   
288  C  CD   . PRO   A 51  ? 0.83036 0.78920 1.12152 0.24260  -0.18754 -0.09297 156 PRO   A CD   
289  N  N    . VAL   A 52  ? 0.71723 0.88496 1.12928 0.28709  -0.14103 -0.19050 157 VAL   A N    
290  C  CA   . VAL   A 52  ? 0.88270 1.08553 1.33284 0.30997  -0.13916 -0.21788 157 VAL   A CA   
291  C  C    . VAL   A 52  ? 1.02842 1.27097 1.47841 0.30554  -0.10982 -0.24659 157 VAL   A C    
292  O  O    . VAL   A 52  ? 0.98657 1.28142 1.43481 0.28832  -0.08841 -0.24856 157 VAL   A O    
293  C  CB   . VAL   A 52  ? 0.86630 1.12261 1.34750 0.31356  -0.14400 -0.21435 157 VAL   A CB   
294  C  CG1  . VAL   A 52  ? 0.82939 1.09851 1.34344 0.33804  -0.15051 -0.23428 157 VAL   A CG1  
295  C  CG2  . VAL   A 52  ? 0.85729 1.08450 1.32668 0.30766  -0.16836 -0.18149 157 VAL   A CG2  
296  N  N    . ARG   A 53  ? 1.11964 1.33692 1.56862 0.31868  -0.10915 -0.26750 158 ARG   A N    
297  C  CA   . ARG   A 53  ? 1.15439 1.40484 1.59680 0.31414  -0.08309 -0.29491 158 ARG   A CA   
298  C  C    . ARG   A 53  ? 1.29073 1.59296 1.76454 0.32925  -0.07390 -0.32231 158 ARG   A C    
299  O  O    . ARG   A 53  ? 1.35215 1.70486 1.82277 0.32059  -0.04858 -0.34105 158 ARG   A O    
300  C  CB   . ARG   A 53  ? 1.08882 1.27872 1.50428 0.31484  -0.08682 -0.30218 158 ARG   A CB   
301  C  CG   . ARG   A 53  ? 0.97059 1.12908 1.35037 0.29409  -0.08305 -0.28389 158 ARG   A CG   
302  C  CD   . ARG   A 53  ? 0.96272 1.04066 1.32755 0.29537  -0.10958 -0.26040 158 ARG   A CD   
303  N  NE   . ARG   A 53  ? 0.94103 0.98644 1.26136 0.26594  -0.10366 -0.23681 158 ARG   A NE   
304  C  CZ   . ARG   A 53  ? 0.93068 0.91071 1.22866 0.25710  -0.12121 -0.21156 158 ARG   A CZ   
305  N  NH1  . ARG   A 53  ? 0.89753 0.83369 1.21366 0.27702  -0.14757 -0.20614 158 ARG   A NH1  
306  N  NH2  . ARG   A 53  ? 0.86575 0.82544 1.12411 0.22819  -0.11273 -0.19105 158 ARG   A NH2  
307  N  N    . MET   A 54  ? 1.34126 1.63274 1.84387 0.35084  -0.09393 -0.32405 159 MET   A N    
308  C  CA   . MET   A 54  ? 1.37300 1.71361 1.90982 0.36790  -0.08726 -0.35063 159 MET   A CA   
309  C  C    . MET   A 54  ? 1.33753 1.75752 1.89339 0.35617  -0.06927 -0.35022 159 MET   A C    
310  O  O    . MET   A 54  ? 1.30640 1.77305 1.85117 0.33920  -0.04244 -0.36028 159 MET   A O    
311  C  CB   . MET   A 54  ? 1.39985 1.70648 1.96346 0.39399  -0.11557 -0.34945 159 MET   A CB   
312  C  CG   . MET   A 54  ? 1.43876 1.68049 1.99342 0.40851  -0.12951 -0.36060 159 MET   A CG   
313  S  SD   . MET   A 54  ? 1.44113 1.59377 1.95330 0.39349  -0.14654 -0.32951 159 MET   A SD   
314  C  CE   . MET   A 54  ? 1.40876 1.51839 1.90819 0.40068  -0.14507 -0.35640 159 MET   A CE   
315  N  N    . SER   A 66  ? 1.39645 2.22679 1.94721 0.08050  0.06105  -0.21103 218 SER   A N    
316  C  CA   . SER   A 66  ? 1.38884 2.21196 1.92572 0.09929  0.07246  -0.23073 218 SER   A CA   
317  C  C    . SER   A 66  ? 1.27013 2.04147 1.80528 0.13115  0.05089  -0.23818 218 SER   A C    
318  O  O    . SER   A 66  ? 1.29912 2.03436 1.82946 0.13175  0.03134  -0.22290 218 SER   A O    
319  C  CB   . SER   A 66  ? 1.44319 2.25959 1.93636 0.07359  0.09483  -0.22221 218 SER   A CB   
320  O  OG   . SER   A 66  ? 1.49626 2.34812 1.98663 0.04041  0.11053  -0.20798 218 SER   A OG   
321  N  N    . PRO   A 67  ? 1.10716 1.87230 1.64516 0.15702  0.05319  -0.26143 219 PRO   A N    
322  C  CA   . PRO   A 67  ? 0.99607 1.70523 1.53267 0.18696  0.03097  -0.26760 219 PRO   A CA   
323  C  C    . PRO   A 67  ? 0.88721 1.54536 1.38417 0.17997  0.03063  -0.25760 219 PRO   A C    
324  O  O    . PRO   A 67  ? 0.86798 1.49356 1.34949 0.19582  0.03067  -0.27168 219 PRO   A O    
325  C  CB   . PRO   A 67  ? 1.01466 1.73552 1.56544 0.21206  0.03621  -0.29684 219 PRO   A CB   
326  C  CG   . PRO   A 67  ? 1.07586 1.84664 1.61469 0.19095  0.06622  -0.30477 219 PRO   A CG   
327  C  CD   . PRO   A 67  ? 1.09877 1.90671 1.64316 0.16036  0.07394  -0.28341 219 PRO   A CD   
328  N  N    . LEU   A 68  ? 0.71862 1.36915 1.19967 0.15580  0.02965  -0.23411 220 LEU   A N    
329  C  CA   . LEU   A 68  ? 0.58950 1.17347 1.02460 0.14666  0.02423  -0.21698 220 LEU   A CA   
330  C  C    . LEU   A 68  ? 0.55532 1.07877 0.99096 0.17009  -0.00516 -0.21130 220 LEU   A C    
331  O  O    . LEU   A 68  ? 0.55120 1.04015 0.97269 0.16035  -0.02172 -0.18731 220 LEU   A O    
332  C  CB   . LEU   A 68  ? 0.57131 1.14445 0.97663 0.11036  0.02891  -0.18771 220 LEU   A CB   
333  C  CG   . LEU   A 68  ? 0.56988 1.19662 0.97123 0.08294  0.05620  -0.18732 220 LEU   A CG   
334  C  CD1  . LEU   A 68  ? 0.52496 1.12391 0.89235 0.04909  0.05740  -0.15754 220 LEU   A CD1  
335  C  CD2  . LEU   A 68  ? 0.61680 1.25303 0.99965 0.08703  0.07590  -0.20464 220 LEU   A CD2  
336  N  N    . SER   A 69  ? 0.61732 1.12736 1.06843 0.20060  -0.01191 -0.23365 221 SER   A N    
337  C  CA   . SER   A 69  ? 0.71290 1.17465 1.17560 0.22622  -0.04167 -0.22997 221 SER   A CA   
338  C  C    . SER   A 69  ? 0.67958 1.06155 1.09438 0.21422  -0.05443 -0.20365 221 SER   A C    
339  O  O    . SER   A 69  ? 0.71940 1.06323 1.13337 0.22172  -0.07889 -0.18672 221 SER   A O    
340  C  CB   . SER   A 69  ? 0.78989 1.24650 1.27373 0.25700  -0.04500 -0.25810 221 SER   A CB   
341  O  OG   . SER   A 69  ? 0.85359 1.26608 1.30933 0.26017  -0.04084 -0.26649 221 SER   A OG   
342  N  N    . MET   A 70  ? 0.61480 0.97346 0.98975 0.19545  -0.03866 -0.19948 222 MET   A N    
343  C  CA   . MET   A 70  ? 0.63178 0.92140 0.96396 0.18296  -0.04839 -0.17615 222 MET   A CA   
344  C  C    . MET   A 70  ? 0.51442 0.79910 0.82073 0.15402  -0.04640 -0.14818 222 MET   A C    
345  O  O    . MET   A 70  ? 0.55115 0.78396 0.82430 0.14343  -0.05447 -0.12822 222 MET   A O    
346  C  CB   . MET   A 70  ? 0.61178 0.87812 0.91540 0.17771  -0.03493 -0.18592 222 MET   A CB   
347  C  CG   . MET   A 70  ? 0.66829 0.91374 0.98827 0.20608  -0.04325 -0.21104 222 MET   A CG   
348  S  SD   . MET   A 70  ? 0.69245 0.86807 1.01732 0.22486  -0.07731 -0.19619 222 MET   A SD   
349  C  CE   . MET   A 70  ? 0.69484 0.80394 0.96728 0.20156  -0.07747 -0.17506 222 MET   A CE   
350  N  N    . LEU   A 71  ? 0.50944 0.84709 0.83156 0.14080  -0.03604 -0.14731 223 LEU   A N    
351  C  CA   . LEU   A 71  ? 0.56469 0.89606 0.86357 0.11325  -0.03437 -0.12368 223 LEU   A CA   
352  C  C    . LEU   A 71  ? 0.52703 0.81908 0.81624 0.11506  -0.05785 -0.10428 223 LEU   A C    
353  O  O    . LEU   A 71  ? 0.50960 0.76525 0.76336 0.09724  -0.05837 -0.08559 223 LEU   A O    
354  C  CB   . LEU   A 71  ? 0.55934 0.95505 0.88260 0.09901  -0.02121 -0.12770 223 LEU   A CB   
355  C  CG   . LEU   A 71  ? 0.47080 0.86145 0.77074 0.06805  -0.01635 -0.10667 223 LEU   A CG   
356  C  CD1  . LEU   A 71  ? 0.37078 0.71781 0.62603 0.05302  -0.00721 -0.09500 223 LEU   A CD1  
357  C  CD2  . LEU   A 71  ? 0.44905 0.90237 0.77273 0.05097  -0.00067 -0.11129 223 LEU   A CD2  
358  N  N    . PRO   A 72  ? 0.48864 0.78694 0.80632 0.13570  -0.07794 -0.10729 224 PRO   A N    
359  C  CA   . PRO   A 72  ? 0.52151 0.77973 0.82208 0.13568  -0.10075 -0.08636 224 PRO   A CA   
360  C  C    . PRO   A 72  ? 0.58219 0.77549 0.84548 0.13505  -0.10631 -0.07354 224 PRO   A C    
361  O  O    . PRO   A 72  ? 0.52513 0.68818 0.75593 0.11893  -0.11058 -0.05368 224 PRO   A O    
362  C  CB   . PRO   A 72  ? 0.43562 0.71241 0.77630 0.16288  -0.12199 -0.09457 224 PRO   A CB   
363  C  CG   . PRO   A 72  ? 0.50027 0.84356 0.88280 0.16874  -0.10793 -0.11752 224 PRO   A CG   
364  C  CD   . PRO   A 72  ? 0.47563 0.82176 0.84268 0.15925  -0.08169 -0.12882 224 PRO   A CD   
365  N  N    . HIS   A 73  ? 0.49448 0.66689 0.76323 0.15220  -0.10666 -0.08580 225 HIS   A N    
366  C  CA   . HIS   A 73  ? 0.54589 0.65708 0.78302 0.15038  -0.11321 -0.07368 225 HIS   A CA   
367  C  C    . HIS   A 73  ? 0.40297 0.50153 0.60458 0.12526  -0.09452 -0.06613 225 HIS   A C    
368  O  O    . HIS   A 73  ? 0.46279 0.52320 0.63345 0.11255  -0.09910 -0.04701 225 HIS   A O    
369  C  CB   . HIS   A 73  ? 0.65672 0.74785 0.91067 0.17381  -0.11863 -0.09142 225 HIS   A CB   
370  C  CG   . HIS   A 73  ? 0.72472 0.75285 0.94968 0.17014  -0.12622 -0.07937 225 HIS   A CG   
371  N  ND1  . HIS   A 73  ? 0.70970 0.69376 0.92120 0.17153  -0.14770 -0.05683 225 HIS   A ND1  
372  C  CD2  . HIS   A 73  ? 0.70706 0.71098 0.91356 0.16298  -0.11534 -0.08581 225 HIS   A CD2  
373  C  CE1  . HIS   A 73  ? 0.79135 0.72717 0.97929 0.16448  -0.14869 -0.04964 225 HIS   A CE1  
374  N  NE2  . HIS   A 73  ? 0.63554 0.58244 0.82120 0.15961  -0.12986 -0.06778 225 HIS   A NE2  
375  N  N    . LEU   A 74  ? 0.49029 0.62270 0.69605 0.11784  -0.07360 -0.08047 226 LEU   A N    
376  C  CA   . LEU   A 74  ? 0.43588 0.55518 0.60946 0.09645  -0.05805 -0.07346 226 LEU   A CA   
377  C  C    . LEU   A 74  ? 0.48183 0.60669 0.63834 0.07466  -0.05469 -0.05569 226 LEU   A C    
378  O  O    . LEU   A 74  ? 0.48273 0.58147 0.60999 0.05942  -0.04986 -0.04364 226 LEU   A O    
379  C  CB   . LEU   A 74  ? 0.51392 0.66640 0.69363 0.09513  -0.03838 -0.09260 226 LEU   A CB   
380  C  CG   . LEU   A 74  ? 0.55576 0.69994 0.74868 0.11644  -0.04048 -0.11442 226 LEU   A CG   
381  C  CD1  . LEU   A 74  ? 0.54461 0.72960 0.74136 0.11458  -0.01984 -0.13504 226 LEU   A CD1  
382  C  CD2  . LEU   A 74  ? 0.55208 0.63779 0.72055 0.11574  -0.04967 -0.10660 226 LEU   A CD2  
383  N  N    . ALA   A 75  ? 0.48634 0.64546 0.66261 0.07329  -0.05790 -0.05540 227 ALA   A N    
384  C  CA   . ALA   A 75  ? 0.46101 0.62003 0.62192 0.05396  -0.05836 -0.04036 227 ALA   A CA   
385  C  C    . ALA   A 75  ? 0.41900 0.53461 0.55494 0.05298  -0.07302 -0.02377 227 ALA   A C    
386  O  O    . ALA   A 75  ? 0.43954 0.53650 0.54882 0.03680  -0.06857 -0.01255 227 ALA   A O    
387  C  CB   . ALA   A 75  ? 0.40089 0.60443 0.59066 0.05311  -0.06222 -0.04470 227 ALA   A CB   
388  N  N    . ASP   A 76  ? 0.43007 0.52983 0.57438 0.07039  -0.09073 -0.02183 228 ASP   A N    
389  C  CA   . ASP   A 76  ? 0.41383 0.47272 0.53166 0.06833  -0.10430 -0.00399 228 ASP   A CA   
390  C  C    . ASP   A 76  ? 0.48010 0.50173 0.57186 0.06114  -0.09623 0.00157  228 ASP   A C    
391  O  O    . ASP   A 76  ? 0.49152 0.49005 0.55525 0.04839  -0.09657 0.01594  228 ASP   A O    
392  C  CB   . ASP   A 76  ? 0.38340 0.43130 0.51641 0.08877  -0.12656 -0.00110 228 ASP   A CB   
393  C  CG   . ASP   A 76  ? 0.46843 0.55210 0.62416 0.09444  -0.13881 -0.00291 228 ASP   A CG   
394  O  OD1  . ASP   A 76  ? 0.53806 0.62233 0.71511 0.11444  -0.15740 -0.00389 228 ASP   A OD1  
395  O  OD2  . ASP   A 76  ? 0.46924 0.57963 0.62303 0.07903  -0.13132 -0.00353 228 ASP   A OD2  
396  N  N    . LEU   A 77  ? 0.40818 0.42653 0.50963 0.06901  -0.08892 -0.01121 229 LEU   A N    
397  C  CA   . LEU   A 77  ? 0.46264 0.44961 0.54236 0.06118  -0.08182 -0.00794 229 LEU   A CA   
398  C  C    . LEU   A 77  ? 0.54066 0.53548 0.60062 0.04112  -0.06628 -0.00323 229 LEU   A C    
399  O  O    . LEU   A 77  ? 0.52431 0.49488 0.56089 0.02991  -0.06541 0.00904  229 LEU   A O    
400  C  CB   . LEU   A 77  ? 0.54752 0.53470 0.64240 0.07352  -0.07731 -0.02660 229 LEU   A CB   
401  C  CG   . LEU   A 77  ? 0.61370 0.57807 0.68960 0.06415  -0.06824 -0.02807 229 LEU   A CG   
402  C  CD1  . LEU   A 77  ? 0.49761 0.41803 0.55344 0.05741  -0.07823 -0.01039 229 LEU   A CD1  
403  C  CD2  . LEU   A 77  ? 0.55899 0.52674 0.65015 0.07770  -0.06521 -0.05043 229 LEU   A CD2  
404  N  N    . VAL   A 78  ? 0.48966 0.51920 0.56013 0.03632  -0.05417 -0.01253 230 VAL   A N    
405  C  CA   . VAL   A 78  ? 0.44686 0.48164 0.50087 0.01836  -0.04161 -0.00724 230 VAL   A CA   
406  C  C    . VAL   A 78  ? 0.48579 0.51167 0.52568 0.00848  -0.04711 0.00593  230 VAL   A C    
407  O  O    . VAL   A 78  ? 0.43413 0.44354 0.45380 -0.00253 -0.04235 0.01363  230 VAL   A O    
408  C  CB   . VAL   A 78  ? 0.47200 0.54547 0.54070 0.01378  -0.02941 -0.01698 230 VAL   A CB   
409  C  CG1  . VAL   A 78  ? 0.47558 0.55090 0.52926 -0.00487 -0.02056 -0.00836 230 VAL   A CG1  
410  C  CG2  . VAL   A 78  ? 0.51868 0.60150 0.59329 0.02105  -0.02091 -0.03101 230 VAL   A CG2  
411  N  N    . SER   A 79  ? 0.48515 0.52404 0.53622 0.01299  -0.05771 0.00707  231 SER   A N    
412  C  CA   . SER   A 79  ? 0.42915 0.46131 0.46479 0.00421  -0.06422 0.01700  231 SER   A CA   
413  C  C    . SER   A 79  ? 0.55096 0.54945 0.56155 0.00298  -0.06933 0.02886  231 SER   A C    
414  O  O    . SER   A 79  ? 0.53788 0.52755 0.52825 -0.00815 -0.06582 0.03498  231 SER   A O    
415  C  CB   . SER   A 79  ? 0.44976 0.50256 0.50205 0.01082  -0.07781 0.01555  231 SER   A CB   
416  O  OG   . SER   A 79  ? 0.45364 0.50603 0.49099 0.00032  -0.08295 0.02139  231 SER   A OG   
417  N  N    . TYR   A 80  ? 0.46622 0.44611 0.47897 0.01405  -0.07768 0.03181  232 TYR   A N    
418  C  CA   . TYR   A 80  ? 0.35863 0.30652 0.34865 0.01016  -0.08164 0.04493  232 TYR   A CA   
419  C  C    . TYR   A 80  ? 0.44608 0.38440 0.42327 -0.00105 -0.06721 0.04473  232 TYR   A C    
420  O  O    . TYR   A 80  ? 0.41324 0.34030 0.36990 -0.01124 -0.06445 0.05403  232 TYR   A O    
421  C  CB   . TYR   A 80  ? 0.41270 0.33932 0.41178 0.02374  -0.09419 0.04738  232 TYR   A CB   
422  C  CG   . TYR   A 80  ? 0.58920 0.48040 0.56728 0.01804  -0.09944 0.06294  232 TYR   A CG   
423  C  CD1  . TYR   A 80  ? 0.61994 0.49880 0.57976 0.01500  -0.11169 0.08016  232 TYR   A CD1  
424  C  CD2  . TYR   A 80  ? 0.65586 0.52736 0.63217 0.01442  -0.09285 0.06092  232 TYR   A CD2  
425  C  CE1  . TYR   A 80  ? 0.72866 0.57702 0.66859 0.00698  -0.11557 0.09670  232 TYR   A CE1  
426  C  CE2  . TYR   A 80  ? 0.69238 0.53307 0.65206 0.00646  -0.09751 0.07597  232 TYR   A CE2  
427  C  CZ   . TYR   A 80  ? 0.73946 0.56882 0.68097 0.00215  -0.10817 0.09470  232 TYR   A CZ   
428  O  OH   . TYR   A 80  ? 0.81581 0.61636 0.73972 -0.00863 -0.11185 0.11205  232 TYR   A OH   
429  N  N    . SER   A 81  ? 0.43263 0.37875 0.42191 0.00087  -0.05797 0.03357  233 SER   A N    
430  C  CA   . SER   A 81  ? 0.54395 0.48332 0.52291 -0.00866 -0.04652 0.03320  233 SER   A CA   
431  C  C    . SER   A 81  ? 0.57047 0.52000 0.53907 -0.01995 -0.03875 0.03593  233 SER   A C    
432  O  O    . SER   A 81  ? 0.48238 0.42182 0.43764 -0.02783 -0.03389 0.04109  233 SER   A O    
433  C  CB   . SER   A 81  ? 0.48984 0.43966 0.48142 -0.00429 -0.03951 0.02025  233 SER   A CB   
434  O  OG   . SER   A 81  ? 0.65036 0.58897 0.63214 -0.01126 -0.03302 0.02051  233 SER   A OG   
435  N  N    . ILE   A 82  ? 0.52491 0.49483 0.50187 -0.02083 -0.03798 0.03154  234 ILE   A N    
436  C  CA   . ILE   A 82  ? 0.42656 0.40179 0.39569 -0.03090 -0.03264 0.03252  234 ILE   A CA   
437  C  C    . ILE   A 82  ? 0.44199 0.40532 0.39289 -0.03476 -0.03640 0.03947  234 ILE   A C    
438  O  O    . ILE   A 82  ? 0.51502 0.47406 0.45568 -0.04142 -0.03006 0.03998  234 ILE   A O    
439  C  CB   . ILE   A 82  ? 0.44323 0.44048 0.42625 -0.03287 -0.03358 0.02708  234 ILE   A CB   
440  C  CG1  . ILE   A 82  ? 0.56251 0.57638 0.56069 -0.03224 -0.02612 0.02087  234 ILE   A CG1  
441  C  CG2  . ILE   A 82  ? 0.43413 0.43065 0.40937 -0.04306 -0.03126 0.02730  234 ILE   A CG2  
442  C  CD1  . ILE   A 82  ? 0.54984 0.59092 0.56660 -0.03443 -0.02695 0.01587  234 ILE   A CD1  
443  N  N    . GLN   A 83  ? 0.41574 0.37501 0.36209 -0.03014 -0.04699 0.04481  235 GLN   A N    
444  C  CA   . GLN   A 83  ? 0.54190 0.49223 0.46640 -0.03505 -0.05002 0.05284  235 GLN   A CA   
445  C  C    . GLN   A 83  ? 0.51721 0.45325 0.43040 -0.04018 -0.04248 0.05868  235 GLN   A C    
446  O  O    . GLN   A 83  ? 0.46956 0.40679 0.36834 -0.04727 -0.03650 0.05986  235 GLN   A O    
447  C  CB   . GLN   A 83  ? 0.49300 0.43938 0.41293 -0.02915 -0.06471 0.06098  235 GLN   A CB   
448  C  CG   . GLN   A 83  ? 0.52423 0.48942 0.45744 -0.02424 -0.07402 0.05500  235 GLN   A CG   
449  C  CD   . GLN   A 83  ? 0.63069 0.59304 0.55559 -0.01881 -0.09096 0.06451  235 GLN   A CD   
450  O  OE1  . GLN   A 83  ? 0.72605 0.67702 0.62526 -0.02404 -0.09428 0.07545  235 GLN   A OE1  
451  N  NE2  . GLN   A 83  ? 0.72314 0.69818 0.66993 -0.00829 -0.10207 0.06087  235 GLN   A NE2  
452  N  N    . LYS   A 84  ? 0.44840 0.37288 0.36962 -0.03675 -0.04276 0.06066  236 LYS   A N    
453  C  CA   . LYS   A 84  ? 0.45510 0.36783 0.36923 -0.04335 -0.03658 0.06574  236 LYS   A CA   
454  C  C    . LYS   A 84  ? 0.43791 0.36039 0.35573 -0.04784 -0.02501 0.05834  236 LYS   A C    
455  O  O    . LYS   A 84  ? 0.50130 0.42398 0.41151 -0.05473 -0.01859 0.06120  236 LYS   A O    
456  C  CB   . LYS   A 84  ? 0.43502 0.33108 0.35855 -0.03876 -0.04171 0.06707  236 LYS   A CB   
457  C  CG   . LYS   A 84  ? 0.53725 0.41764 0.45909 -0.03265 -0.05575 0.07592  236 LYS   A CG   
458  C  CD   . LYS   A 84  ? 0.52877 0.40571 0.42854 -0.04020 -0.05961 0.09036  236 LYS   A CD   
459  C  CE   . LYS   A 84  ? 0.63935 0.49238 0.53403 -0.03705 -0.07475 0.10474  236 LYS   A CE   
460  N  NZ   . LYS   A 84  ? 0.64493 0.47309 0.54755 -0.03843 -0.07650 0.10727  236 LYS   A NZ   
461  N  N    . VAL   A 85  ? 0.40422 0.33636 0.33445 -0.04421 -0.02260 0.04958  237 VAL   A N    
462  C  CA   . VAL   A 85  ? 0.42243 0.36103 0.35575 -0.04779 -0.01436 0.04489  237 VAL   A CA   
463  C  C    . VAL   A 85  ? 0.48658 0.42990 0.41193 -0.05168 -0.01110 0.04378  237 VAL   A C    
464  O  O    . VAL   A 85  ? 0.49347 0.43806 0.41785 -0.05439 -0.00517 0.04263  237 VAL   A O    
465  C  CB   . VAL   A 85  ? 0.38831 0.33632 0.33332 -0.04518 -0.01317 0.03874  237 VAL   A CB   
466  C  CG1  . VAL   A 85  ? 0.39127 0.34315 0.33725 -0.04940 -0.00755 0.03707  237 VAL   A CG1  
467  C  CG2  . VAL   A 85  ? 0.47787 0.42386 0.42948 -0.04096 -0.01386 0.03591  237 VAL   A CG2  
468  N  N    . ILE   A 86  ? 0.45760 0.40504 0.37851 -0.05119 -0.01567 0.04228  238 ILE   A N    
469  C  CA   . ILE   A 86  ? 0.43715 0.38849 0.34889 -0.05425 -0.01341 0.03781  238 ILE   A CA   
470  C  C    . ILE   A 86  ? 0.41928 0.37041 0.31655 -0.05760 -0.00922 0.04210  238 ILE   A C    
471  O  O    . ILE   A 86  ? 0.50789 0.46430 0.40296 -0.05915 -0.00215 0.03657  238 ILE   A O    
472  C  CB   . ILE   A 86  ? 0.52151 0.47826 0.43029 -0.05407 -0.02117 0.03445  238 ILE   A CB   
473  C  CG1  . ILE   A 86  ? 0.47103 0.43284 0.39708 -0.05366 -0.02332 0.03013  238 ILE   A CG1  
474  C  CG2  . ILE   A 86  ? 0.52424 0.48418 0.42051 -0.05707 -0.01965 0.02703  238 ILE   A CG2  
475  C  CD1  . ILE   A 86  ? 0.51313 0.48449 0.44275 -0.05313 -0.03282 0.02835  238 ILE   A CD1  
476  N  N    . GLY   A 87  ? 0.43665 0.38239 0.32493 -0.05893 -0.01360 0.05222  239 GLY   A N    
477  C  CA   . GLY   A 87  ? 0.47021 0.41710 0.34388 -0.06549 -0.00879 0.05939  239 GLY   A CA   
478  C  C    . GLY   A 87  ? 0.51790 0.46725 0.40121 -0.06864 0.00034  0.05856  239 GLY   A C    
479  O  O    . GLY   A 87  ? 0.48281 0.44355 0.36024 -0.07360 0.00876  0.05749  239 GLY   A O    
480  N  N    . PHE   A 88  ? 0.43766 0.37987 0.33643 -0.06572 -0.00125 0.05781  240 PHE   A N    
481  C  CA   . PHE   A 88  ? 0.43699 0.38322 0.34619 -0.06855 0.00502  0.05637  240 PHE   A CA   
482  C  C    . PHE   A 88  ? 0.38926 0.34748 0.30601 -0.06519 0.01090  0.04633  240 PHE   A C    
483  O  O    . PHE   A 88  ? 0.47186 0.44197 0.39235 -0.06766 0.01783  0.04405  240 PHE   A O    
484  C  CB   . PHE   A 88  ? 0.40129 0.33748 0.32189 -0.06606 0.00040  0.05640  240 PHE   A CB   
485  C  CG   . PHE   A 88  ? 0.46009 0.40211 0.39191 -0.06835 0.00430  0.05345  240 PHE   A CG   
486  C  CD1  . PHE   A 88  ? 0.39180 0.33458 0.32548 -0.07663 0.00638  0.05848  240 PHE   A CD1  
487  C  CD2  . PHE   A 88  ? 0.44256 0.38987 0.38317 -0.06343 0.00469  0.04693  240 PHE   A CD2  
488  C  CE1  . PHE   A 88  ? 0.44411 0.39548 0.39031 -0.07894 0.00826  0.05503  240 PHE   A CE1  
489  C  CE2  . PHE   A 88  ? 0.43048 0.38431 0.38075 -0.06484 0.00580  0.04507  240 PHE   A CE2  
490  C  CZ   . PHE   A 88  ? 0.48365 0.44085 0.43778 -0.07208 0.00730  0.04809  240 PHE   A CZ   
491  N  N    . ALA   A 89  ? 0.42466 0.38019 0.34566 -0.05966 0.00768  0.04032  241 ALA   A N    
492  C  CA   . ALA   A 89  ? 0.48786 0.44784 0.41751 -0.05588 0.01043  0.03205  241 ALA   A CA   
493  C  C    . ALA   A 89  ? 0.51157 0.48129 0.43524 -0.05544 0.01588  0.02464  241 ALA   A C    
494  O  O    . ALA   A 89  ? 0.46526 0.44219 0.39889 -0.05167 0.02009  0.01757  241 ALA   A O    
495  C  CB   . ALA   A 89  ? 0.39553 0.34836 0.32914 -0.05332 0.00523  0.02937  241 ALA   A CB   
496  N  N    . LYS   A 90  ? 0.43871 0.41040 0.34610 -0.05839 0.01534  0.02522  242 LYS   A N    
497  C  CA   . LYS   A 90  ? 0.46200 0.44614 0.35928 -0.05849 0.02133  0.01619  242 LYS   A CA   
498  C  C    . LYS   A 90  ? 0.38805 0.38928 0.28729 -0.06171 0.03158  0.01683  242 LYS   A C    
499  O  O    . LYS   A 90  ? 0.48485 0.50182 0.38257 -0.05939 0.03917  0.00520  242 LYS   A O    
500  C  CB   . LYS   A 90  ? 0.60074 0.58551 0.47588 -0.06265 0.01742  0.01937  242 LYS   A CB   
501  C  CG   . LYS   A 90  ? 0.73644 0.71256 0.61102 -0.05980 0.00823  0.01353  242 LYS   A CG   
502  C  CD   . LYS   A 90  ? 0.82885 0.80721 0.68261 -0.06358 0.00162  0.01899  242 LYS   A CD   
503  C  CE   . LYS   A 90  ? 0.84669 0.83991 0.67792 -0.06793 0.00858  0.01656  242 LYS   A CE   
504  N  NZ   . LYS   A 90  ? 0.95997 0.95549 0.76717 -0.07168 -0.00022 0.02215  242 LYS   A NZ   
505  N  N    . MET   A 91  ? 0.43916 0.43940 0.34302 -0.06739 0.03211  0.02865  243 MET   A N    
506  C  CA   . MET   A 91  ? 0.46155 0.48053 0.37014 -0.07351 0.04159  0.03073  243 MET   A CA   
507  C  C    . MET   A 91  ? 0.50165 0.52696 0.43540 -0.06889 0.04269  0.02605  243 MET   A C    
508  O  O    . MET   A 91  ? 0.56217 0.60663 0.50562 -0.07408 0.04985  0.02693  243 MET   A O    
509  C  CB   . MET   A 91  ? 0.51449 0.52740 0.41198 -0.08554 0.04021  0.04761  243 MET   A CB   
510  C  CG   . MET   A 91  ? 0.64562 0.65158 0.51706 -0.08969 0.03645  0.05525  243 MET   A CG   
511  S  SD   . MET   A 91  ? 0.79358 0.79027 0.65090 -0.10494 0.03426  0.07770  243 MET   A SD   
512  C  CE   . MET   A 91  ? 0.87022 0.83646 0.72068 -0.09838 0.01707  0.08545  243 MET   A CE   
513  N  N    . ILE   A 92  ? 0.43289 0.44462 0.37731 -0.06037 0.03530  0.02215  244 ILE   A N    
514  C  CA   . ILE   A 92  ? 0.39371 0.41166 0.35998 -0.05487 0.03412  0.01849  244 ILE   A CA   
515  C  C    . ILE   A 92  ? 0.43943 0.47705 0.41755 -0.04728 0.04094  0.00504  244 ILE   A C    
516  O  O    . ILE   A 92  ? 0.39531 0.42853 0.36795 -0.04075 0.04129  -0.00513 244 ILE   A O    
517  C  CB   . ILE   A 92  ? 0.41129 0.40994 0.38173 -0.04879 0.02449  0.01954  244 ILE   A CB   
518  C  CG1  . ILE   A 92  ? 0.39068 0.37562 0.35278 -0.05458 0.01915  0.02944  244 ILE   A CG1  
519  C  CG2  . ILE   A 92  ? 0.39279 0.39741 0.38318 -0.04195 0.02123  0.01670  244 ILE   A CG2  
520  C  CD1  . ILE   A 92  ? 0.34064 0.31181 0.30366 -0.05067 0.01209  0.03058  244 ILE   A CD1  
521  N  N    . PRO   A 93  ? 0.41587 0.47661 0.41224 -0.04734 0.04599  0.00260  245 PRO   A N    
522  C  CA   . PRO   A 93  ? 0.43716 0.52025 0.44968 -0.03710 0.05253  -0.01307 245 PRO   A CA   
523  C  C    . PRO   A 93  ? 0.50344 0.56843 0.52533 -0.02202 0.04383  -0.02249 245 PRO   A C    
524  O  O    . PRO   A 93  ? 0.52856 0.57845 0.56040 -0.01787 0.03324  -0.01629 245 PRO   A O    
525  C  CB   . PRO   A 93  ? 0.39887 0.50803 0.43561 -0.03927 0.05508  -0.01158 245 PRO   A CB   
526  C  CG   . PRO   A 93  ? 0.48914 0.59413 0.51418 -0.05627 0.05523  0.00408  245 PRO   A CG   
527  C  CD   . PRO   A 93  ? 0.46450 0.53395 0.46976 -0.05685 0.04557  0.01230  245 PRO   A CD   
528  N  N    . GLY   A 94  ? 0.47901 0.54379 0.49576 -0.01490 0.04748  -0.03711 246 GLY   A N    
529  C  CA   . GLY   A 94  ? 0.54744 0.59120 0.57318 -0.00175 0.03873  -0.04726 246 GLY   A CA   
530  C  C    . GLY   A 94  ? 0.63333 0.64607 0.63995 -0.00610 0.03101  -0.04287 246 GLY   A C    
531  O  O    . GLY   A 94  ? 0.55227 0.54919 0.56087 0.00149  0.02638  -0.05494 246 GLY   A O    
532  N  N    . PHE   A 95  ? 0.57258 0.57689 0.56328 -0.01795 0.02895  -0.02711 247 PHE   A N    
533  C  CA   . PHE   A 95  ? 0.47160 0.45174 0.44913 -0.02218 0.02137  -0.02254 247 PHE   A CA   
534  C  C    . PHE   A 95  ? 0.58132 0.56069 0.54497 -0.02212 0.02349  -0.03574 247 PHE   A C    
535  O  O    . PHE   A 95  ? 0.50754 0.46780 0.47199 -0.01975 0.01627  -0.04232 247 PHE   A O    
536  C  CB   . PHE   A 95  ? 0.52144 0.49890 0.48682 -0.03271 0.02010  -0.00655 247 PHE   A CB   
537  C  CG   . PHE   A 95  ? 0.48207 0.44136 0.43877 -0.03673 0.01287  -0.00194 247 PHE   A CG   
538  C  CD1  . PHE   A 95  ? 0.45689 0.40232 0.42129 -0.03686 0.00601  0.00519  247 PHE   A CD1  
539  C  CD2  . PHE   A 95  ? 0.52734 0.48676 0.46830 -0.04120 0.01276  -0.00423 247 PHE   A CD2  
540  C  CE1  . PHE   A 95  ? 0.47204 0.40670 0.43122 -0.04210 0.00104  0.00915  247 PHE   A CE1  
541  C  CE2  . PHE   A 95  ? 0.52269 0.47061 0.46020 -0.04502 0.00581  -0.00091 247 PHE   A CE2  
542  C  CZ   . PHE   A 95  ? 0.54871 0.48555 0.49665 -0.04584 0.00088  0.00539  247 PHE   A CZ   
543  N  N    . ARG   A 96  ? 0.62750 0.62777 0.57704 -0.02626 0.03280  -0.03929 248 ARG   A N    
544  C  CA   . ARG   A 96  ? 0.70525 0.70876 0.63669 -0.02713 0.03465  -0.05214 248 ARG   A CA   
545  C  C    . ARG   A 96  ? 0.66873 0.67200 0.61122 -0.01522 0.03557  -0.07543 248 ARG   A C    
546  O  O    . ARG   A 96  ? 0.69218 0.69122 0.62175 -0.01478 0.03365  -0.08965 248 ARG   A O    
547  C  CB   . ARG   A 96  ? 0.82708 0.85543 0.73845 -0.03531 0.04492  -0.04826 248 ARG   A CB   
548  C  CG   . ARG   A 96  ? 0.98682 1.01393 0.87011 -0.04208 0.04197  -0.04863 248 ARG   A CG   
549  C  CD   . ARG   A 96  ? 1.23096 1.28674 1.09367 -0.04703 0.05405  -0.05322 248 ARG   A CD   
550  N  NE   . ARG   A 96  ? 1.39087 1.46665 1.26607 -0.03766 0.06459  -0.07482 248 ARG   A NE   
551  C  CZ   . ARG   A 96  ? 1.45036 1.52226 1.32785 -0.02772 0.06281  -0.09879 248 ARG   A CZ   
552  N  NH1  . ARG   A 96  ? 1.39810 1.48961 1.29036 -0.01695 0.07252  -0.11974 248 ARG   A NH1  
553  N  NH2  . ARG   A 96  ? 1.47236 1.52161 1.33961 -0.02837 0.05080  -0.10319 248 ARG   A NH2  
554  N  N    . ASP   A 97  ? 0.62046 0.62801 0.58761 -0.00472 0.03708  -0.08086 249 ASP   A N    
555  C  CA   . ASP   A 97  ? 0.56019 0.56394 0.54279 0.00977  0.03596  -0.10410 249 ASP   A CA   
556  C  C    . ASP   A 97  ? 0.57840 0.54344 0.57066 0.01361  0.02083  -0.10471 249 ASP   A C    
557  O  O    . ASP   A 97  ? 0.72104 0.67355 0.72099 0.02349  0.01692  -0.12530 249 ASP   A O    
558  C  CB   . ASP   A 97  ? 0.56763 0.59307 0.57673 0.02129  0.04183  -0.10972 249 ASP   A CB   
559  C  CG   . ASP   A 97  ? 0.68016 0.74835 0.68257 0.01651  0.05869  -0.11297 249 ASP   A CG   
560  O  OD1  . ASP   A 97  ? 0.67515 0.75433 0.65007 0.00681  0.06585  -0.11481 249 ASP   A OD1  
561  O  OD2  . ASP   A 97  ? 0.61603 0.70815 0.64062 0.02134  0.06421  -0.11262 249 ASP   A OD2  
562  N  N    . LEU   A 98  ? 0.58322 0.52947 0.57531 0.00539  0.01250  -0.08331 250 LEU   A N    
563  C  CA   . LEU   A 98  ? 0.59025 0.50181 0.58904 0.00456  -0.00086 -0.08012 250 LEU   A CA   
564  C  C    . LEU   A 98  ? 0.64608 0.54646 0.62974 -0.00203 -0.00440 -0.09143 250 LEU   A C    
565  O  O    . LEU   A 98  ? 0.67022 0.58931 0.63401 -0.00783 0.00204  -0.09585 250 LEU   A O    
566  C  CB   . LEU   A 98  ? 0.45224 0.35443 0.45017 -0.00518 -0.00607 -0.05495 250 LEU   A CB   
567  C  CG   . LEU   A 98  ? 0.46965 0.38314 0.47917 -0.00128 -0.00461 -0.04238 250 LEU   A CG   
568  C  CD1  . LEU   A 98  ? 0.43282 0.34076 0.43523 -0.01225 -0.00818 -0.02094 250 LEU   A CD1  
569  C  CD2  . LEU   A 98  ? 0.52158 0.42226 0.55396 0.01254  -0.01227 -0.04762 250 LEU   A CD2  
570  N  N    . THR   A 99  ? 0.63994 0.50881 0.63296 -0.00214 -0.01615 -0.09515 251 THR   A N    
571  C  CA   . THR   A 99  ? 0.64726 0.50404 0.62884 -0.01101 -0.02206 -0.10471 251 THR   A CA   
572  C  C    . THR   A 99  ? 0.58316 0.44955 0.55026 -0.02627 -0.02203 -0.08637 251 THR   A C    
573  O  O    . THR   A 99  ? 0.52649 0.39809 0.49581 -0.03036 -0.02021 -0.06576 251 THR   A O    
574  C  CB   . THR   A 99  ? 0.62342 0.44138 0.62074 -0.01132 -0.03588 -0.10884 251 THR   A CB   
575  O  OG1  . THR   A 99  ? 0.56328 0.36714 0.56674 -0.02156 -0.04179 -0.08299 251 THR   A OG1  
576  C  CG2  . THR   A 99  ? 0.56584 0.37018 0.58276 0.00686  -0.03841 -0.12436 251 THR   A CG2  
577  N  N    . SER   A 100 ? 0.59128 0.46132 0.54416 -0.03373 -0.02497 -0.09583 252 SER   A N    
578  C  CA   . SER   A 100 ? 0.57849 0.45925 0.52112 -0.04609 -0.02688 -0.08086 252 SER   A CA   
579  C  C    . SER   A 100 ? 0.55311 0.41793 0.51020 -0.05506 -0.03355 -0.06387 252 SER   A C    
580  O  O    . SER   A 100 ? 0.53160 0.40862 0.48729 -0.06048 -0.03118 -0.04665 252 SER   A O    
581  C  CB   . SER   A 100 ? 0.55595 0.44246 0.48359 -0.05201 -0.03228 -0.09542 252 SER   A CB   
582  O  OG   . SER   A 100 ? 0.78913 0.69245 0.69949 -0.04485 -0.02533 -0.11167 252 SER   A OG   
583  N  N    . ASP   A 101 ? 0.53187 0.36930 0.50278 -0.05712 -0.04191 -0.06866 253 ASP   A N    
584  C  CA   . ASP   A 101 ? 0.56791 0.39114 0.55071 -0.06863 -0.04764 -0.05086 253 ASP   A CA   
585  C  C    . ASP   A 101 ? 0.57760 0.40687 0.56349 -0.06552 -0.04193 -0.03098 253 ASP   A C    
586  O  O    . ASP   A 101 ? 0.52714 0.36679 0.51283 -0.07472 -0.04028 -0.01473 253 ASP   A O    
587  C  CB   . ASP   A 101 ? 0.58447 0.37198 0.58108 -0.07133 -0.05846 -0.05773 253 ASP   A CB   
588  C  CG   . ASP   A 101 ? 0.82253 0.60240 0.81792 -0.08003 -0.06664 -0.07538 253 ASP   A CG   
589  O  OD1  . ASP   A 101 ? 0.90872 0.69386 0.89479 -0.07134 -0.06577 -0.09798 253 ASP   A OD1  
590  O  OD2  . ASP   A 101 ? 0.83757 0.60845 0.84113 -0.09657 -0.07382 -0.06721 253 ASP   A OD2  
591  N  N    . ASP   A 102 ? 0.53602 0.36167 0.52572 -0.05219 -0.03906 -0.03379 254 ASP   A N    
592  C  CA   . ASP   A 102 ? 0.47974 0.31205 0.47208 -0.04922 -0.03544 -0.01657 254 ASP   A CA   
593  C  C    . ASP   A 102 ? 0.48418 0.34542 0.46504 -0.05070 -0.02636 -0.00998 254 ASP   A C    
594  O  O    . ASP   A 102 ? 0.55272 0.42087 0.53263 -0.05575 -0.02475 0.00546  254 ASP   A O    
595  C  CB   . ASP   A 102 ? 0.53734 0.36287 0.53992 -0.03388 -0.03598 -0.02298 254 ASP   A CB   
596  C  CG   . ASP   A 102 ? 0.67448 0.46598 0.69130 -0.03199 -0.04794 -0.01973 254 ASP   A CG   
597  O  OD1  . ASP   A 102 ? 0.63174 0.41356 0.66104 -0.01708 -0.05128 -0.03024 254 ASP   A OD1  
598  O  OD2  . ASP   A 102 ? 0.64825 0.42321 0.66495 -0.04556 -0.05429 -0.00623 254 ASP   A OD2  
599  N  N    . GLN   A 103 ? 0.47028 0.34771 0.44130 -0.04670 -0.02085 -0.02155 255 GLN   A N    
600  C  CA   . GLN   A 103 ? 0.50942 0.40867 0.46943 -0.04904 -0.01459 -0.01409 255 GLN   A CA   
601  C  C    . GLN   A 103 ? 0.44380 0.34656 0.40242 -0.05908 -0.01774 -0.00438 255 GLN   A C    
602  O  O    . GLN   A 103 ? 0.42318 0.33619 0.38072 -0.06056 -0.01476 0.00672  255 GLN   A O    
603  C  CB   . GLN   A 103 ? 0.52272 0.43604 0.46918 -0.04614 -0.01013 -0.02595 255 GLN   A CB   
604  C  CG   . GLN   A 103 ? 0.56335 0.48239 0.51198 -0.03637 -0.00399 -0.03747 255 GLN   A CG   
605  C  CD   . GLN   A 103 ? 0.58092 0.51795 0.51203 -0.03609 0.00202  -0.04799 255 GLN   A CD   
606  O  OE1  . GLN   A 103 ? 0.62427 0.57127 0.54043 -0.04248 0.00239  -0.04013 255 GLN   A OE1  
607  N  NE2  . GLN   A 103 ? 0.63607 0.57801 0.56857 -0.02822 0.00634  -0.06596 255 GLN   A NE2  
608  N  N    . ILE   A 104 ? 0.43716 0.33294 0.39796 -0.06594 -0.02403 -0.01014 256 ILE   A N    
609  C  CA   . ILE   A 104 ? 0.53895 0.44385 0.50290 -0.07571 -0.02691 -0.00286 256 ILE   A CA   
610  C  C    . ILE   A 104 ? 0.47582 0.37802 0.44889 -0.08130 -0.02568 0.01147  256 ILE   A C    
611  O  O    . ILE   A 104 ? 0.46745 0.38601 0.44105 -0.08360 -0.02227 0.01976  256 ILE   A O    
612  C  CB   . ILE   A 104 ? 0.53669 0.43611 0.50370 -0.08358 -0.03495 -0.01331 256 ILE   A CB   
613  C  CG1  . ILE   A 104 ? 0.54172 0.45279 0.49464 -0.07978 -0.03660 -0.02535 256 ILE   A CG1  
614  C  CG2  . ILE   A 104 ? 0.49954 0.40844 0.47781 -0.09587 -0.03800 -0.00480 256 ILE   A CG2  
615  C  CD1  . ILE   A 104 ? 0.57583 0.48009 0.52929 -0.08625 -0.04569 -0.04015 256 ILE   A CD1  
616  N  N    A VAL   A 105 ? 0.46841 0.34992 0.44802 -0.08312 -0.02892 0.01447  257 VAL   A N    
617  N  N    B VAL   A 105 ? 0.44429 0.32564 0.42399 -0.08331 -0.02907 0.01421  257 VAL   A N    
618  C  CA   A VAL   A 105 ? 0.49323 0.37281 0.47726 -0.09068 -0.02837 0.03041  257 VAL   A CA   
619  C  CA   B VAL   A 105 ? 0.50652 0.38435 0.49066 -0.09018 -0.02868 0.03008  257 VAL   A CA   
620  C  C    A VAL   A 105 ? 0.45249 0.34352 0.43054 -0.08344 -0.02235 0.03821  257 VAL   A C    
621  C  C    B VAL   A 105 ? 0.43820 0.32991 0.41614 -0.08336 -0.02225 0.03769  257 VAL   A C    
622  O  O    A VAL   A 105 ? 0.47295 0.37537 0.44969 -0.08924 -0.01918 0.04894  257 VAL   A O    
623  O  O    B VAL   A 105 ? 0.42426 0.32957 0.40096 -0.08909 -0.01868 0.04737  257 VAL   A O    
624  C  CB   A VAL   A 105 ? 0.53272 0.38299 0.52386 -0.09505 -0.03591 0.03485  257 VAL   A CB   
625  C  CB   B VAL   A 105 ? 0.54557 0.39335 0.53620 -0.09130 -0.03601 0.03302  257 VAL   A CB   
626  C  CG1  A VAL   A 105 ? 0.55813 0.39431 0.55620 -0.10347 -0.04312 0.02479  257 VAL   A CG1  
627  C  CG1  B VAL   A 105 ? 0.56885 0.41287 0.55795 -0.09275 -0.03579 0.05068  257 VAL   A CG1  
628  C  CG2  A VAL   A 105 ? 0.55706 0.39212 0.54885 -0.08065 -0.03789 0.03088  257 VAL   A CG2  
629  C  CG2  B VAL   A 105 ? 0.57523 0.40847 0.57392 -0.10519 -0.04310 0.03149  257 VAL   A CG2  
630  N  N    . LEU   A 106 ? 0.42871 0.31961 0.40332 -0.07171 -0.02034 0.03186  258 LEU   A N    
631  C  CA   . LEU   A 106 ? 0.48497 0.38726 0.45543 -0.06654 -0.01581 0.03794  258 LEU   A CA   
632  C  C    . LEU   A 106 ? 0.52081 0.44241 0.48601 -0.06781 -0.01099 0.03799  258 LEU   A C    
633  O  O    . LEU   A 106 ? 0.44055 0.37163 0.40349 -0.06879 -0.00829 0.04440  258 LEU   A O    
634  C  CB   . LEU   A 106 ? 0.49771 0.39853 0.46941 -0.05563 -0.01465 0.03089  258 LEU   A CB   
635  C  CG   . LEU   A 106 ? 0.46555 0.34904 0.44648 -0.04991 -0.02044 0.03061  258 LEU   A CG   
636  C  CD1  . LEU   A 106 ? 0.37472 0.26538 0.36069 -0.03830 -0.01747 0.02030  258 LEU   A CD1  
637  C  CD2  . LEU   A 106 ? 0.44095 0.31967 0.42231 -0.05295 -0.02462 0.04593  258 LEU   A CD2  
638  N  N    . LEU   A 107 ? 0.47558 0.40254 0.43844 -0.06716 -0.01109 0.03026  259 LEU   A N    
639  C  CA   . LEU   A 107 ? 0.45966 0.40157 0.41956 -0.06644 -0.00921 0.03082  259 LEU   A CA   
640  C  C    . LEU   A 107 ? 0.35507 0.30835 0.32193 -0.07304 -0.00929 0.03460  259 LEU   A C    
641  O  O    . LEU   A 107 ? 0.44405 0.40969 0.41167 -0.07096 -0.00642 0.03653  259 LEU   A O    
642  C  CB   . LEU   A 107 ? 0.45909 0.40343 0.41287 -0.06409 -0.01149 0.02377  259 LEU   A CB   
643  C  CG   . LEU   A 107 ? 0.57064 0.51304 0.51575 -0.05844 -0.00814 0.02180  259 LEU   A CG   
644  C  CD1  . LEU   A 107 ? 0.64970 0.59439 0.58450 -0.05799 -0.00999 0.01481  259 LEU   A CD1  
645  C  CD2  . LEU   A 107 ? 0.52790 0.47546 0.47089 -0.05615 -0.00574 0.02817  259 LEU   A CD2  
646  N  N    . LYS   A 108 ? 0.40389 0.35432 0.37730 -0.08146 -0.01231 0.03458  260 LYS   A N    
647  C  CA   . LYS   A 108 ? 0.51801 0.48523 0.50065 -0.09002 -0.01106 0.03802  260 LYS   A CA   
648  C  C    . LYS   A 108 ? 0.52144 0.49596 0.50240 -0.09289 -0.00520 0.04674  260 LYS   A C    
649  O  O    . LYS   A 108 ? 0.55691 0.55360 0.54241 -0.09395 -0.00065 0.04655  260 LYS   A O    
650  C  CB   . LYS   A 108 ? 0.46031 0.42089 0.45116 -0.10180 -0.01587 0.03762  260 LYS   A CB   
651  C  CG   . LYS   A 108 ? 0.58101 0.55003 0.57723 -0.10282 -0.02173 0.02801  260 LYS   A CG   
652  C  CD   . LYS   A 108 ? 0.67536 0.63880 0.68222 -0.11730 -0.02715 0.02705  260 LYS   A CD   
653  C  CE   . LYS   A 108 ? 0.78099 0.77315 0.80390 -0.12822 -0.02528 0.03042  260 LYS   A CE   
654  N  NZ   . LYS   A 108 ? 0.79652 0.79860 0.82085 -0.13417 -0.01631 0.04243  260 LYS   A NZ   
655  N  N    . SER   A 109 ? 0.56871 0.52668 0.54317 -0.09340 -0.00579 0.05350  261 SER   A N    
656  C  CA   . SER   A 109 ? 0.53615 0.50120 0.50502 -0.09769 -0.00181 0.06311  261 SER   A CA   
657  C  C    . SER   A 109 ? 0.42624 0.39937 0.38772 -0.08790 0.00148  0.05980  261 SER   A C    
658  O  O    . SER   A 109 ? 0.52012 0.50838 0.47651 -0.09037 0.00608  0.06261  261 SER   A O    
659  C  CB   . SER   A 109 ? 0.56801 0.51080 0.53312 -0.10240 -0.00685 0.07381  261 SER   A CB   
660  O  OG   . SER   A 109 ? 0.71002 0.63208 0.67708 -0.09341 -0.01240 0.06791  261 SER   A OG   
661  N  N    . SER   A 110 ? 0.40878 0.37325 0.36907 -0.07809 -0.00059 0.05331  262 SER   A N    
662  C  CA   . SER   A 110 ? 0.47350 0.44186 0.42837 -0.07097 0.00108  0.05057  262 SER   A CA   
663  C  C    . SER   A 110 ? 0.49921 0.47772 0.45682 -0.06552 0.00273  0.04270  262 SER   A C    
664  O  O    . SER   A 110 ? 0.48054 0.46201 0.43487 -0.06115 0.00377  0.03956  262 SER   A O    
665  C  CB   . SER   A 110 ? 0.49260 0.44734 0.44617 -0.06527 -0.00186 0.04977  262 SER   A CB   
666  O  OG   . SER   A 110 ? 0.45812 0.40878 0.41377 -0.06181 -0.00240 0.04379  262 SER   A OG   
667  N  N    . ALA   A 111 ? 0.38398 0.36660 0.34816 -0.06540 0.00127  0.03922  263 ALA   A N    
668  C  CA   . ALA   A 111 ? 0.33930 0.32718 0.30680 -0.05813 -0.00040 0.03336  263 ALA   A CA   
669  C  C    . ALA   A 111 ? 0.33954 0.34140 0.31039 -0.05438 0.00295  0.02866  263 ALA   A C    
670  O  O    . ALA   A 111 ? 0.39794 0.39421 0.36742 -0.04724 0.00121  0.02449  263 ALA   A O    
671  C  CB   . ALA   A 111 ? 0.40856 0.40316 0.38372 -0.05901 -0.00432 0.03102  263 ALA   A CB   
672  N  N    . ILE   A 112 ? 0.36040 0.38078 0.33556 -0.05992 0.00796  0.02865  264 ILE   A N    
673  C  CA   . ILE   A 112 ? 0.42694 0.46625 0.40505 -0.05586 0.01291  0.02093  264 ILE   A CA   
674  C  C    . ILE   A 112 ? 0.51714 0.54764 0.48262 -0.05368 0.01371  0.01957  264 ILE   A C    
675  O  O    . ILE   A 112 ? 0.52435 0.55885 0.49101 -0.04591 0.01409  0.00930  264 ILE   A O    
676  C  CB   . ILE   A 112 ? 0.43658 0.50233 0.41985 -0.06534 0.02025  0.02259  264 ILE   A CB   
677  C  CG1  . ILE   A 112 ? 0.48856 0.58045 0.47563 -0.05989 0.02725  0.01101  264 ILE   A CG1  
678  C  CG2  . ILE   A 112 ? 0.50430 0.56230 0.47474 -0.07781 0.02205  0.03537  264 ILE   A CG2  
679  C  CD1  . ILE   A 112 ? 0.48902 0.58744 0.49276 -0.04540 0.02361  -0.00209 264 ILE   A CD1  
680  N  N    . GLU   A 113 ? 0.41956 0.43753 0.37446 -0.05981 0.01251  0.02868  265 GLU   A N    
681  C  CA   . GLU   A 113 ? 0.48097 0.49294 0.42529 -0.05852 0.01131  0.02765  265 GLU   A CA   
682  C  C    . GLU   A 113 ? 0.44195 0.43719 0.38857 -0.05173 0.00626  0.02307  265 GLU   A C    
683  O  O    . GLU   A 113 ? 0.41687 0.41078 0.36076 -0.04828 0.00500  0.01544  265 GLU   A O    
684  C  CB   . GLU   A 113 ? 0.45701 0.46157 0.39281 -0.06551 0.00928  0.03947  265 GLU   A CB   
685  C  CG   . GLU   A 113 ? 0.50645 0.52327 0.43731 -0.07515 0.01305  0.04806  265 GLU   A CG   
686  C  CD   . GLU   A 113 ? 0.54350 0.54628 0.46759 -0.08058 0.00778  0.06171  265 GLU   A CD   
687  O  OE1  . GLU   A 113 ? 0.53406 0.52564 0.45594 -0.07576 0.00221  0.06216  265 GLU   A OE1  
688  O  OE2  . GLU   A 113 ? 0.59157 0.59440 0.51452 -0.08980 0.00837  0.07219  265 GLU   A OE2  
689  N  N    . VAL   A 114 ? 0.42975 0.41234 0.38042 -0.05110 0.00327  0.02746  266 VAL   A N    
690  C  CA   . VAL   A 114 ? 0.40613 0.37433 0.35737 -0.04771 -0.00061 0.02619  266 VAL   A CA   
691  C  C    . VAL   A 114 ? 0.45698 0.42326 0.41356 -0.04083 -0.00312 0.01868  266 VAL   A C    
692  O  O    . VAL   A 114 ? 0.48831 0.44220 0.44458 -0.03884 -0.00679 0.01577  266 VAL   A O    
693  C  CB   . VAL   A 114 ? 0.42613 0.38586 0.37746 -0.04936 -0.00183 0.03223  266 VAL   A CB   
694  C  CG1  . VAL   A 114 ? 0.38919 0.33730 0.33885 -0.04916 -0.00421 0.03360  266 VAL   A CG1  
695  C  CG2  . VAL   A 114 ? 0.45039 0.41060 0.40016 -0.05335 -0.00044 0.03699  266 VAL   A CG2  
696  N  N    . ILE   A 115 ? 0.39428 0.37237 0.35815 -0.03708 -0.00226 0.01528  267 ILE   A N    
697  C  CA   . ILE   A 115 ? 0.45532 0.43370 0.42829 -0.02743 -0.00585 0.00648  267 ILE   A CA   
698  C  C    . ILE   A 115 ? 0.55202 0.53324 0.52401 -0.02383 -0.00415 -0.00504 267 ILE   A C    
699  O  O    . ILE   A 115 ? 0.50966 0.47585 0.48525 -0.01717 -0.00985 -0.01180 267 ILE   A O    
700  C  CB   . ILE   A 115 ? 0.48967 0.48837 0.47470 -0.02398 -0.00471 0.00345  267 ILE   A CB   
701  C  CG1  . ILE   A 115 ? 0.46821 0.45929 0.45497 -0.02408 -0.01113 0.01122  267 ILE   A CG1  
702  C  CG2  . ILE   A 115 ? 0.50362 0.51296 0.50172 -0.01216 -0.00574 -0.01026 267 ILE   A CG2  
703  C  CD1  . ILE   A 115 ? 0.56689 0.58043 0.56685 -0.02335 -0.01127 0.00887  267 ILE   A CD1  
704  N  N    . MET   A 116 ? 0.46762 0.46677 0.43328 -0.02886 0.00282  -0.00734 268 MET   A N    
705  C  CA   . MET   A 116 ? 0.45043 0.45557 0.41104 -0.02631 0.00460  -0.01992 268 MET   A CA   
706  C  C    . MET   A 116 ? 0.43229 0.41556 0.38583 -0.02902 -0.00147 -0.01934 268 MET   A C    
707  O  O    . MET   A 116 ? 0.48244 0.45781 0.43702 -0.02409 -0.00509 -0.03216 268 MET   A O    
708  C  CB   . MET   A 116 ? 0.47802 0.50827 0.42844 -0.03364 0.01296  -0.01890 268 MET   A CB   
709  C  CG   . MET   A 116 ? 0.58599 0.64527 0.54546 -0.03166 0.02083  -0.02474 268 MET   A CG   
710  S  SD   . MET   A 116 ? 0.58181 0.66619 0.52886 -0.04683 0.03021  -0.01260 268 MET   A SD   
711  C  CE   . MET   A 116 ? 0.57667 0.69681 0.54263 -0.04486 0.03913  -0.02059 268 MET   A CE   
712  N  N    . LEU   A 117 ? 0.50787 0.48207 0.45646 -0.03682 -0.00298 -0.00600 269 LEU   A N    
713  C  CA   . LEU   A 117 ? 0.48535 0.44417 0.43114 -0.04100 -0.00824 -0.00475 269 LEU   A CA   
714  C  C    . LEU   A 117 ? 0.56480 0.50128 0.51814 -0.03810 -0.01437 -0.00584 269 LEU   A C    
715  O  O    . LEU   A 117 ? 0.50282 0.42663 0.45730 -0.03849 -0.01956 -0.01364 269 LEU   A O    
716  C  CB   . LEU   A 117 ? 0.39662 0.35571 0.33970 -0.04814 -0.00768 0.00843  269 LEU   A CB   
717  C  CG   . LEU   A 117 ? 0.56885 0.54180 0.50376 -0.05239 -0.00612 0.01255  269 LEU   A CG   
718  C  CD1  . LEU   A 117 ? 0.49275 0.46291 0.43054 -0.05545 -0.00646 0.02438  269 LEU   A CD1  
719  C  CD2  . LEU   A 117 ? 0.58651 0.56241 0.51533 -0.05473 -0.01049 0.00552  269 LEU   A CD2  
720  N  N    . ARG   A 118 ? 0.47849 0.40846 0.43591 -0.03637 -0.01509 0.00272  270 ARG   A N    
721  C  CA   . ARG   A 118 ? 0.52200 0.42899 0.48300 -0.03586 -0.02198 0.00675  270 ARG   A CA   
722  C  C    . ARG   A 118 ? 0.50911 0.40455 0.47801 -0.02559 -0.02820 -0.00509 270 ARG   A C    
723  O  O    . ARG   A 118 ? 0.58698 0.45748 0.55863 -0.02626 -0.03613 -0.00416 270 ARG   A O    
724  C  CB   . ARG   A 118 ? 0.49731 0.40265 0.45671 -0.03676 -0.02202 0.01918  270 ARG   A CB   
725  C  CG   . ARG   A 118 ? 0.52127 0.43781 0.48593 -0.02817 -0.02217 0.01653  270 ARG   A CG   
726  C  CD   . ARG   A 118 ? 0.49810 0.41739 0.45806 -0.03142 -0.02196 0.02737  270 ARG   A CD   
727  N  NE   . ARG   A 118 ? 0.49577 0.39628 0.45055 -0.03307 -0.02869 0.03715  270 ARG   A NE   
728  C  CZ   . ARG   A 118 ? 0.54363 0.43767 0.48907 -0.04268 -0.02655 0.04638  270 ARG   A CZ   
729  N  NH1  . ARG   A 118 ? 0.63213 0.53679 0.57578 -0.04907 -0.01892 0.04537  270 ARG   A NH1  
730  N  NH2  . ARG   A 118 ? 0.48780 0.36633 0.42617 -0.04591 -0.03230 0.05718  270 ARG   A NH2  
731  N  N    . SER   A 119 ? 0.49426 0.40757 0.46833 -0.01623 -0.02490 -0.01662 271 SER   A N    
732  C  CA   . SER   A 119 ? 0.49210 0.39792 0.47698 -0.00351 -0.03036 -0.03203 271 SER   A CA   
733  C  C    . SER   A 119 ? 0.50005 0.39512 0.48242 -0.00444 -0.03302 -0.04627 271 SER   A C    
734  O  O    . SER   A 119 ? 0.53155 0.41075 0.52338 0.00584  -0.04012 -0.06017 271 SER   A O    
735  C  CB   . SER   A 119 ? 0.47256 0.40859 0.46577 0.00611  -0.02386 -0.04285 271 SER   A CB   
736  O  OG   . SER   A 119 ? 0.49854 0.45893 0.48320 0.00165  -0.01427 -0.05138 271 SER   A OG   
737  N  N    . ASN   A 120 ? 0.55988 0.46261 0.53080 -0.01581 -0.02903 -0.04412 272 ASN   A N    
738  C  CA   . ASN   A 120 ? 0.52182 0.41651 0.48926 -0.01835 -0.03302 -0.05834 272 ASN   A CA   
739  C  C    . ASN   A 120 ? 0.55104 0.40931 0.52517 -0.02194 -0.04433 -0.05628 272 ASN   A C    
740  O  O    . ASN   A 120 ? 0.54519 0.38839 0.52205 -0.01999 -0.05099 -0.07275 272 ASN   A O    
741  C  CB   . ASN   A 120 ? 0.45340 0.36555 0.40816 -0.03004 -0.02870 -0.05337 272 ASN   A CB   
742  C  CG   . ASN   A 120 ? 0.56849 0.48145 0.51691 -0.03212 -0.03263 -0.07085 272 ASN   A CG   
743  O  OD1  . ASN   A 120 ? 0.64374 0.54449 0.59204 -0.04182 -0.03918 -0.06894 272 ASN   A OD1  
744  N  ND2  . ASN   A 120 ? 0.49784 0.42845 0.44110 -0.02375 -0.02844 -0.08912 272 ASN   A ND2  
745  N  N    . GLN   A 121 ? 0.56583 0.40949 0.54162 -0.02841 -0.04675 -0.03641 273 GLN   A N    
746  C  CA   . GLN   A 121 ? 0.63848 0.44690 0.61950 -0.03443 -0.05728 -0.03027 273 GLN   A CA   
747  C  C    . GLN   A 121 ? 0.69923 0.48198 0.69107 -0.02028 -0.06745 -0.04269 273 GLN   A C    
748  O  O    . GLN   A 121 ? 0.72166 0.47299 0.71888 -0.02351 -0.07790 -0.04809 273 GLN   A O    
749  C  CB   . GLN   A 121 ? 0.78286 0.58582 0.76043 -0.04324 -0.05630 -0.00601 273 GLN   A CB   
750  C  CG   . GLN   A 121 ? 0.90136 0.68477 0.87881 -0.06038 -0.06070 0.00590  273 GLN   A CG   
751  C  CD   . GLN   A 121 ? 0.94951 0.73387 0.92051 -0.06919 -0.05736 0.02872  273 GLN   A CD   
752  O  OE1  . GLN   A 121 ? 0.89246 0.70318 0.85770 -0.06999 -0.04775 0.03423  273 GLN   A OE1  
753  N  NE2  . GLN   A 121 ? 0.91496 0.66966 0.88577 -0.07625 -0.06575 0.04196  273 GLN   A NE2  
754  N  N    . SER   A 122 ? 0.69301 0.48862 0.69061 -0.00444 -0.06548 -0.04805 274 SER   A N    
755  C  CA   . SER   A 122 ? 0.66554 0.44213 0.67776 0.01325  -0.07528 -0.06235 274 SER   A CA   
756  C  C    . SER   A 122 ? 0.60190 0.39474 0.61896 0.02505  -0.07168 -0.09259 274 SER   A C    
757  O  O    . SER   A 122 ? 0.62652 0.40241 0.65806 0.04119  -0.08024 -0.11010 274 SER   A O    
758  C  CB   . SER   A 122 ? 0.67541 0.46213 0.69517 0.02531  -0.07614 -0.05352 274 SER   A CB   
759  O  OG   . SER   A 122 ? 0.70751 0.53298 0.73309 0.03668  -0.06613 -0.06934 274 SER   A OG   
760  N  N    . PHE   A 123 ? 0.55468 0.38004 0.55954 0.01808  -0.05984 -0.09941 275 PHE   A N    
761  C  CA   . PHE   A 123 ? 0.62738 0.47432 0.63194 0.02784  -0.05462 -0.12762 275 PHE   A CA   
762  C  C    . PHE   A 123 ? 0.71299 0.53088 0.71855 0.02729  -0.06496 -0.14690 275 PHE   A C    
763  O  O    . PHE   A 123 ? 0.77839 0.57615 0.77739 0.01136  -0.07076 -0.13757 275 PHE   A O    
764  C  CB   . PHE   A 123 ? 0.61781 0.50537 0.60497 0.01816  -0.04076 -0.12557 275 PHE   A CB   
765  C  CG   . PHE   A 123 ? 0.72814 0.64410 0.70976 0.02597  -0.03348 -0.15260 275 PHE   A CG   
766  C  CD1  . PHE   A 123 ? 0.73945 0.68268 0.73161 0.04101  -0.02570 -0.16631 275 PHE   A CD1  
767  C  CD2  . PHE   A 123 ? 0.67706 0.59631 0.64287 0.01775  -0.03429 -0.16492 275 PHE   A CD2  
768  C  CE1  . PHE   A 123 ? 0.72399 0.69871 0.70957 0.04734  -0.01679 -0.19206 275 PHE   A CE1  
769  C  CE2  . PHE   A 123 ? 0.63958 0.58771 0.59588 0.02412  -0.02708 -0.19036 275 PHE   A CE2  
770  C  CZ   . PHE   A 123 ? 0.73686 0.71346 0.70233 0.03876  -0.01728 -0.20407 275 PHE   A CZ   
771  N  N    . THR   A 124 ? 0.75000 0.56765 0.76565 0.04474  -0.06729 -0.17569 276 THR   A N    
772  C  CA   . THR   A 124 ? 0.90274 0.68978 0.92174 0.04716  -0.07865 -0.19937 276 THR   A CA   
773  C  C    . THR   A 124 ? 0.89308 0.71496 0.90081 0.05254  -0.06940 -0.23034 276 THR   A C    
774  O  O    . THR   A 124 ? 0.96485 0.82811 0.97183 0.06300  -0.05624 -0.23948 276 THR   A O    
775  C  CB   . THR   A 124 ? 0.99252 0.74014 1.03538 0.06582  -0.09301 -0.20925 276 THR   A CB   
776  O  OG1  . THR   A 124 ? 1.17553 0.88812 1.22339 0.05726  -0.10313 -0.17777 276 THR   A OG1  
777  C  CG2  . THR   A 124 ? 0.98383 0.69805 1.03206 0.07034  -0.10534 -0.23862 276 THR   A CG2  
778  N  N    . MET   A 125 ? 0.99708 0.80493 0.99485 0.04346  -0.07613 -0.24592 277 MET   A N    
779  C  CA   . MET   A 125 ? 1.05335 0.89143 1.03699 0.04832  -0.06952 -0.27809 277 MET   A CA   
780  C  C    . MET   A 125 ? 1.10768 0.92360 1.10600 0.06783  -0.07824 -0.31664 277 MET   A C    
781  O  O    . MET   A 125 ? 1.16244 1.00793 1.15002 0.07585  -0.07102 -0.34825 277 MET   A O    
782  C  CB   . MET   A 125 ? 1.04421 0.88769 1.00560 0.02720  -0.07215 -0.27538 277 MET   A CB   
783  C  CG   . MET   A 125 ? 1.01946 0.89251 0.96567 0.01142  -0.06249 -0.24295 277 MET   A CG   
784  S  SD   . MET   A 125 ? 1.14849 1.06446 1.06213 -0.00076 -0.05642 -0.25091 277 MET   A SD   
785  C  CE   . MET   A 125 ? 1.05149 0.94031 0.96543 -0.02238 -0.07187 -0.23583 277 MET   A CE   
786  N  N    . ASP   A 126 ? 1.27633 1.04077 1.29809 0.07582  -0.09394 -0.31493 278 ASP   A N    
787  C  CA   . ASP   A 126 ? 1.49249 1.24013 1.53200 0.09581  -0.10005 -0.34033 278 ASP   A CA   
788  C  C    . ASP   A 126 ? 1.43162 1.22688 1.47900 0.11843  -0.08543 -0.36020 278 ASP   A C    
789  O  O    . ASP   A 126 ? 1.53598 1.34457 1.58768 0.13160  -0.08257 -0.38723 278 ASP   A O    
790  C  CB   . ASP   A 126 ? 1.71700 1.41035 1.78027 0.10056  -0.11667 -0.32142 278 ASP   A CB   
791  C  CG   . ASP   A 126 ? 1.84432 1.49431 1.90192 0.07554  -0.12907 -0.29583 278 ASP   A CG   
792  O  OD1  . ASP   A 126 ? 1.87397 1.53188 1.91365 0.05632  -0.12750 -0.29829 278 ASP   A OD1  
793  O  OD2  . ASP   A 126 ? 1.89312 1.50505 1.96408 0.07418  -0.14006 -0.27120 278 ASP   A OD2  
794  N  N    . ASP   A 127 ? 1.27673 1.09992 1.32710 0.12219  -0.07581 -0.34727 279 ASP   A N    
795  C  CA   . ASP   A 127 ? 1.22044 1.09038 1.28470 0.14242  -0.06216 -0.36135 279 ASP   A CA   
796  C  C    . ASP   A 127 ? 1.15078 1.07349 1.20159 0.13174  -0.04347 -0.34021 279 ASP   A C    
797  O  O    . ASP   A 127 ? 1.15519 1.12087 1.21913 0.14554  -0.03119 -0.34960 279 ASP   A O    
798  C  CB   . ASP   A 127 ? 1.25679 1.09807 1.35524 0.16231  -0.07479 -0.35507 279 ASP   A CB   
799  C  CG   . ASP   A 127 ? 1.28034 1.07322 1.38282 0.15265  -0.08976 -0.32147 279 ASP   A CG   
800  O  OD1  . ASP   A 127 ? 1.24135 1.05333 1.32582 0.13228  -0.08073 -0.29020 279 ASP   A OD1  
801  O  OD2  . ASP   A 127 ? 1.32234 1.06779 1.44111 0.15830  -0.10724 -0.31208 279 ASP   A OD2  
802  N  N    . MET   A 128 ? 1.11797 1.04058 1.14508 0.10673  -0.04094 -0.31012 280 MET   A N    
803  C  CA   . MET   A 128 ? 1.04876 1.01266 1.06376 0.09408  -0.02583 -0.28347 280 MET   A CA   
804  C  C    . MET   A 128 ? 0.87933 0.84814 0.91895 0.10473  -0.02551 -0.26772 280 MET   A C    
805  O  O    . MET   A 128 ? 0.84905 0.86436 0.89414 0.10910  -0.01149 -0.26874 280 MET   A O    
806  C  CB   . MET   A 128 ? 1.13551 1.15683 1.13108 0.09173  -0.00726 -0.30063 280 MET   A CB   
807  C  CG   . MET   A 128 ? 1.24287 1.26104 1.21315 0.08365  -0.00976 -0.32062 280 MET   A CG   
808  S  SD   . MET   A 128 ? 1.43433 1.40781 1.38981 0.06021  -0.02491 -0.29232 280 MET   A SD   
809  C  CE   . MET   A 128 ? 1.45187 1.44382 1.37433 0.04961  -0.02438 -0.31549 280 MET   A CE   
810  N  N    . SER   A 129 ? 0.80342 0.72426 0.85766 0.10758  -0.04200 -0.25240 281 SER   A N    
811  C  CA   . SER   A 129 ? 0.78855 0.70753 0.86276 0.11558  -0.04593 -0.23347 281 SER   A CA   
812  C  C    . SER   A 129 ? 0.78587 0.67172 0.84952 0.09741  -0.05419 -0.19712 281 SER   A C    
813  O  O    . SER   A 129 ? 0.69091 0.55048 0.73854 0.08177  -0.05892 -0.18935 281 SER   A O    
814  C  CB   . SER   A 129 ? 0.81175 0.70595 0.91680 0.14187  -0.06005 -0.25253 281 SER   A CB   
815  O  OG   . SER   A 129 ? 0.91725 0.75049 1.02264 0.14032  -0.07867 -0.25118 281 SER   A OG   
816  N  N    . TRP   A 130 ? 0.73424 0.62491 0.80756 0.09925  -0.05575 -0.17599 282 TRP   A N    
817  C  CA   . TRP   A 130 ? 0.65940 0.52174 0.72342 0.08437  -0.06323 -0.14332 282 TRP   A CA   
818  C  C    . TRP   A 130 ? 0.81295 0.62882 0.89305 0.09592  -0.08297 -0.13803 282 TRP   A C    
819  O  O    . TRP   A 130 ? 0.79647 0.61776 0.89626 0.11290  -0.08913 -0.13893 282 TRP   A O    
820  C  CB   . TRP   A 130 ? 0.63487 0.53006 0.69533 0.07721  -0.05374 -0.12338 282 TRP   A CB   
821  C  CG   . TRP   A 130 ? 0.63686 0.56470 0.67766 0.06101  -0.03775 -0.11990 282 TRP   A CG   
822  C  CD1  . TRP   A 130 ? 0.63626 0.55744 0.65782 0.04184  -0.03502 -0.09957 282 TRP   A CD1  
823  C  CD2  . TRP   A 130 ? 0.62159 0.59388 0.66030 0.06281  -0.02307 -0.13651 282 TRP   A CD2  
824  N  NE1  . TRP   A 130 ? 0.65552 0.61000 0.66376 0.03275  -0.02173 -0.10145 282 TRP   A NE1  
825  C  CE2  . TRP   A 130 ? 0.65925 0.64530 0.67558 0.04381  -0.01388 -0.12252 282 TRP   A CE2  
826  C  CE3  . TRP   A 130 ? 0.62037 0.62423 0.67435 0.07859  -0.01651 -0.16176 282 TRP   A CE3  
827  C  CZ2  . TRP   A 130 ? 0.70729 0.73355 0.71296 0.03842  0.00036  -0.12973 282 TRP   A CZ2  
828  C  CZ3  . TRP   A 130 ? 0.64075 0.68971 0.68389 0.07218  0.00019  -0.17036 282 TRP   A CZ3  
829  C  CH2  . TRP   A 130 ? 0.65854 0.71648 0.67622 0.05141  0.00789  -0.15280 282 TRP   A CH2  
830  N  N    . ASP   A 131 ? 0.83399 0.60458 0.90659 0.08599  -0.09394 -0.13157 283 ASP   A N    
831  C  CA   . ASP   A 131 ? 0.84613 0.56507 0.93188 0.09455  -0.11445 -0.12570 283 ASP   A CA   
832  C  C    . ASP   A 131 ? 0.84432 0.54583 0.91948 0.08059  -0.12026 -0.08886 283 ASP   A C    
833  O  O    . ASP   A 131 ? 0.92402 0.61123 0.98173 0.05856  -0.11859 -0.07099 283 ASP   A O    
834  C  CB   . ASP   A 131 ? 0.97337 0.65175 1.05751 0.08901  -0.12368 -0.13916 283 ASP   A CB   
835  C  CG   . ASP   A 131 ? 1.09013 0.70962 1.18934 0.09794  -0.14657 -0.13403 283 ASP   A CG   
836  O  OD1  . ASP   A 131 ? 1.06798 0.68255 1.18253 0.11545  -0.15582 -0.12764 283 ASP   A OD1  
837  O  OD2  . ASP   A 131 ? 1.13643 0.71393 1.23306 0.08713  -0.15667 -0.13607 283 ASP   A OD2  
838  N  N    . CYS   A 132 ? 0.80899 0.51476 0.89505 0.09349  -0.12727 -0.07841 284 CYS   A N    
839  C  CA   . CYS   A 132 ? 0.87361 0.56812 0.94640 0.08103  -0.13248 -0.04491 284 CYS   A CA   
840  C  C    . CYS   A 132 ? 0.93403 0.58049 1.01575 0.09041  -0.15574 -0.03102 284 CYS   A C    
841  O  O    . CYS   A 132 ? 0.96173 0.61168 1.04455 0.09634  -0.16385 -0.01388 284 CYS   A O    
842  C  CB   . CYS   A 132 ? 0.72947 0.47062 0.80171 0.08358  -0.12251 -0.03899 284 CYS   A CB   
843  S  SG   . CYS   A 132 ? 0.68651 0.47772 0.74408 0.06822  -0.09731 -0.04568 284 CYS   A SG   
844  N  N    . GLY   A 133 ? 0.98791 0.58799 1.07576 0.09150  -0.16824 -0.03780 285 GLY   A N    
845  C  CA   . GLY   A 133 ? 1.08820 0.63670 1.18028 0.09506  -0.19089 -0.01888 285 GLY   A CA   
846  C  C    . GLY   A 133 ? 1.04299 0.58201 1.16115 0.12072  -0.20273 -0.03886 285 GLY   A C    
847  O  O    . GLY   A 133 ? 1.17948 0.68351 1.29989 0.11742  -0.21241 -0.03729 285 GLY   A O    
848  N  N    . SER   A 134 ? 1.00373 0.57556 1.14342 0.14610  -0.20189 -0.05814 286 SER   A N    
849  C  CA   . SER   A 134 ? 1.12003 0.68907 1.28677 0.17167  -0.21321 -0.07563 286 SER   A CA   
850  C  C    . SER   A 134 ? 1.06836 0.68381 1.25849 0.19394  -0.20106 -0.11431 286 SER   A C    
851  O  O    . SER   A 134 ? 0.98659 0.63617 1.17112 0.18970  -0.18452 -0.12552 286 SER   A O    
852  C  CB   . SER   A 134 ? 1.19484 0.76063 1.36663 0.18044  -0.22872 -0.05147 286 SER   A CB   
853  O  OG   . SER   A 134 ? 1.30127 0.84087 1.44460 0.15629  -0.23393 -0.01353 286 SER   A OG   
854  N  N    . GLN   A 135 ? 1.10759 0.72613 1.32398 0.21733  -0.20873 -0.13501 287 GLN   A N    
855  C  CA   . GLN   A 135 ? 1.17286 0.84328 1.41306 0.23860  -0.19576 -0.17187 287 GLN   A CA   
856  C  C    . GLN   A 135 ? 1.17149 0.89346 1.42261 0.24645  -0.18876 -0.16764 287 GLN   A C    
857  O  O    . GLN   A 135 ? 1.09342 0.86770 1.35257 0.25154  -0.16992 -0.19080 287 GLN   A O    
858  C  CB   . GLN   A 135 ? 1.25294 0.91510 1.52007 0.26182  -0.20688 -0.19272 287 GLN   A CB   
859  C  CG   . GLN   A 135 ? 1.28675 0.98728 1.56885 0.27588  -0.19150 -0.23571 287 GLN   A CG   
860  C  CD   . GLN   A 135 ? 1.32067 1.00358 1.58086 0.25959  -0.18234 -0.24892 287 GLN   A CD   
861  O  OE1  . GLN   A 135 ? 1.39625 1.02575 1.64503 0.24811  -0.19461 -0.23782 287 GLN   A OE1  
862  N  NE2  . GLN   A 135 ? 1.25046 0.98061 1.50408 0.25706  -0.16064 -0.27211 287 GLN   A NE2  
863  N  N    . ASP   A 136 ? 1.22326 0.93424 1.47405 0.24617  -0.20351 -0.13793 288 ASP   A N    
864  C  CA   . ASP   A 136 ? 1.23148 0.99005 1.49134 0.25060  -0.19920 -0.13072 288 ASP   A CA   
865  C  C    . ASP   A 136 ? 1.12791 0.91661 1.36099 0.22530  -0.17646 -0.12407 288 ASP   A C    
866  O  O    . ASP   A 136 ? 1.10479 0.95306 1.34470 0.22390  -0.15927 -0.13332 288 ASP   A O    
867  C  CB   . ASP   A 136 ? 1.27743 1.01367 1.53020 0.24755  -0.21930 -0.09551 288 ASP   A CB   
868  C  CG   . ASP   A 136 ? 1.37458 1.11808 1.65670 0.27097  -0.23426 -0.10210 288 ASP   A CG   
869  O  OD1  . ASP   A 136 ? 1.37944 1.16265 1.69181 0.29038  -0.22613 -0.13381 288 ASP   A OD1  
870  O  OD2  . ASP   A 136 ? 1.40615 1.11798 1.68021 0.26929  -0.25346 -0.07541 288 ASP   A OD2  
871  N  N    . TYR   A 137 ? 0.99201 0.74461 1.19221 0.20049  -0.17390 -0.10583 289 TYR   A N    
872  C  CA   . TYR   A 137 ? 0.94352 0.72203 1.11389 0.17245  -0.15256 -0.09472 289 TYR   A CA   
873  C  C    . TYR   A 137 ? 0.90717 0.68545 1.06709 0.16371  -0.13803 -0.11530 289 TYR   A C    
874  O  O    . TYR   A 137 ? 0.78746 0.55278 0.92060 0.14017  -0.13063 -0.10215 289 TYR   A O    
875  C  CB   . TYR   A 137 ? 0.90380 0.65136 1.04577 0.15066  -0.15981 -0.05778 289 TYR   A CB   
876  C  CG   . TYR   A 137 ? 0.84272 0.58485 0.99333 0.16146  -0.17848 -0.03871 289 TYR   A CG   
877  C  CD1  . TYR   A 137 ? 0.89879 0.58927 1.03728 0.15745  -0.19906 -0.01209 289 TYR   A CD1  
878  C  CD2  . TYR   A 137 ? 0.89653 0.68695 1.06778 0.17495  -0.17645 -0.04693 289 TYR   A CD2  
879  C  CE1  . TYR   A 137 ? 0.96829 0.65477 1.11194 0.16761  -0.21807 0.00645  289 TYR   A CE1  
880  C  CE2  . TYR   A 137 ? 0.91930 0.70772 1.09931 0.18540  -0.19558 -0.03053 289 TYR   A CE2  
881  C  CZ   . TYR   A 137 ? 0.98104 0.71704 1.14584 0.18235  -0.21689 -0.00368 289 TYR   A CZ   
882  O  OH   . TYR   A 137 ? 1.01881 0.75371 1.18926 0.19264  -0.23766 0.01406  289 TYR   A OH   
883  N  N    . LYS   A 138 ? 0.94363 0.73927 1.12584 0.18378  -0.13447 -0.14933 290 LYS   A N    
884  C  CA   . LYS   A 138 ? 0.99295 0.79982 1.16642 0.17892  -0.11997 -0.17480 290 LYS   A CA   
885  C  C    . LYS   A 138 ? 0.94930 0.82576 1.12889 0.18184  -0.09817 -0.19221 290 LYS   A C    
886  O  O    . LYS   A 138 ? 0.97439 0.88108 1.18329 0.20479  -0.09779 -0.21379 290 LYS   A O    
887  C  CB   . LYS   A 138 ? 1.02087 0.79166 1.21327 0.19961  -0.13341 -0.20283 290 LYS   A CB   
888  C  CG   . LYS   A 138 ? 1.12528 0.91252 1.30985 0.19802  -0.11951 -0.23511 290 LYS   A CG   
889  C  CD   . LYS   A 138 ? 1.12998 0.88874 1.28323 0.17035  -0.11761 -0.22178 290 LYS   A CD   
890  C  CE   . LYS   A 138 ? 1.13257 0.83918 1.29090 0.17615  -0.13252 -0.24208 290 LYS   A CE   
891  N  NZ   . LYS   A 138 ? 1.15098 0.80986 1.28920 0.15057  -0.14174 -0.21650 290 LYS   A NZ   
892  N  N    . TYR   A 139 ? 0.78862 0.69134 0.94223 0.15854  -0.08050 -0.18228 291 TYR   A N    
893  C  CA   . TYR   A 139 ? 0.68371 0.64965 0.83882 0.15507  -0.06028 -0.18963 291 TYR   A CA   
894  C  C    . TYR   A 139 ? 0.73281 0.72250 0.87371 0.14995  -0.04415 -0.21304 291 TYR   A C    
895  O  O    . TYR   A 139 ? 0.77491 0.74564 0.88875 0.13198  -0.04163 -0.20541 291 TYR   A O    
896  C  CB   . TYR   A 139 ? 0.60146 0.58003 0.73818 0.13276  -0.05382 -0.15867 291 TYR   A CB   
897  C  CG   . TYR   A 139 ? 0.65449 0.60692 0.79702 0.13440  -0.07028 -0.13430 291 TYR   A CG   
898  C  CD1  . TYR   A 139 ? 0.57290 0.48275 0.69324 0.11893  -0.07881 -0.10931 291 TYR   A CD1  
899  C  CD2  . TYR   A 139 ? 0.71300 0.68661 0.88316 0.15121  -0.07756 -0.13660 291 TYR   A CD2  
900  C  CE1  . TYR   A 139 ? 0.67694 0.56532 0.79801 0.11925  -0.09334 -0.08658 291 TYR   A CE1  
901  C  CE2  . TYR   A 139 ? 0.60439 0.55518 0.77658 0.15251  -0.09433 -0.11377 291 TYR   A CE2  
902  C  CZ   . TYR   A 139 ? 0.65818 0.56584 0.80356 0.13611  -0.10184 -0.08851 291 TYR   A CZ   
903  O  OH   . TYR   A 139 ? 0.69216 0.57948 0.83493 0.13606  -0.11788 -0.06527 291 TYR   A OH   
904  N  N    . ASP   A 140 ? 0.84049 0.87534 0.99965 0.16550  -0.03328 -0.24155 292 ASP   A N    
905  C  CA   . ASP   A 140 ? 0.92195 0.99081 1.06626 0.16123  -0.01585 -0.26520 292 ASP   A CA   
906  C  C    . ASP   A 140 ? 0.91504 1.04608 1.05378 0.14801  0.00508  -0.25776 292 ASP   A C    
907  O  O    . ASP   A 140 ? 0.79891 0.94092 0.94402 0.14019  0.00501  -0.23404 292 ASP   A O    
908  C  CB   . ASP   A 140 ? 0.97001 1.04503 1.13757 0.18840  -0.01794 -0.30624 292 ASP   A CB   
909  C  CG   . ASP   A 140 ? 1.05322 1.17117 1.25974 0.21080  -0.01492 -0.32064 292 ASP   A CG   
910  O  OD1  . ASP   A 140 ? 1.10451 1.25773 1.32783 0.22922  -0.00578 -0.35699 292 ASP   A OD1  
911  O  OD2  . ASP   A 140 ? 1.05846 1.17774 1.27968 0.21029  -0.02184 -0.29712 292 ASP   A OD2  
912  N  N    . VAL   A 141 ? 0.93552 1.10738 1.06109 0.14426  0.02265  -0.27814 293 VAL   A N    
913  C  CA   . VAL   A 141 ? 0.86247 1.09256 0.98040 0.12875  0.04297  -0.26955 293 VAL   A CA   
914  C  C    . VAL   A 141 ? 0.75913 1.03815 0.91486 0.14363  0.04963  -0.28123 293 VAL   A C    
915  O  O    . VAL   A 141 ? 0.70249 1.02496 0.85937 0.12903  0.06293  -0.26741 293 VAL   A O    
916  C  CB   . VAL   A 141 ? 0.89065 1.15133 0.97920 0.11858  0.05949  -0.28564 293 VAL   A CB   
917  C  CG1  . VAL   A 141 ? 0.87177 1.08364 0.92989 0.10934  0.04905  -0.28155 293 VAL   A CG1  
918  C  CG2  . VAL   A 141 ? 0.89940 1.20029 1.00681 0.14044  0.06927  -0.32737 293 VAL   A CG2  
919  N  N    . THR   A 142 ? 0.71055 0.98358 0.89969 0.17238  0.03961  -0.30650 294 THR   A N    
920  C  CA   . THR   A 142 ? 0.73549 1.05605 0.96646 0.18900  0.04317  -0.31779 294 THR   A CA   
921  C  C    . THR   A 142 ? 0.71552 1.02605 0.95892 0.18150  0.03209  -0.28564 294 THR   A C    
922  O  O    . THR   A 142 ? 0.73017 1.09198 0.99764 0.18043  0.04031  -0.28393 294 THR   A O    
923  C  CB   . THR   A 142 ? 0.82466 1.13266 1.08960 0.22343  0.03059  -0.35029 294 THR   A CB   
924  O  OG1  . THR   A 142 ? 0.90821 1.20044 1.15056 0.22385  0.03359  -0.37113 294 THR   A OG1  
925  C  CG2  . THR   A 142 ? 0.84492 1.21008 1.14456 0.23356  0.03746  -0.36069 294 THR   A CG2  
926  N  N    . ASP   A 143 ? 0.79395 1.04177 1.02107 0.17509  0.01382  -0.26079 295 ASP   A N    
927  C  CA   . ASP   A 143 ? 0.79245 1.02930 1.02708 0.16803  0.00249  -0.23173 295 ASP   A CA   
928  C  C    . ASP   A 143 ? 0.69466 0.95805 0.90810 0.13851  0.01700  -0.20845 295 ASP   A C    
929  O  O    . ASP   A 143 ? 0.66639 0.95416 0.89588 0.13309  0.01610  -0.19546 295 ASP   A O    
930  C  CB   . ASP   A 143 ? 0.82525 0.99024 1.04620 0.16899  -0.01968 -0.21289 295 ASP   A CB   
931  C  CG   . ASP   A 143 ? 0.86056 0.99119 1.10228 0.19677  -0.03657 -0.23343 295 ASP   A CG   
932  O  OD1  . ASP   A 143 ? 0.81849 0.89300 1.04161 0.19434  -0.04783 -0.22816 295 ASP   A OD1  
933  O  OD2  . ASP   A 143 ? 0.87583 1.03567 1.15466 0.22107  -0.03918 -0.25528 295 ASP   A OD2  
934  N  N    . VAL   A 144 ? 0.60917 0.86757 0.78755 0.11926  0.02894  -0.20319 296 VAL   A N    
935  C  CA   . VAL   A 144 ? 0.62609 0.90555 0.78486 0.09203  0.04123  -0.18079 296 VAL   A CA   
936  C  C    . VAL   A 144 ? 0.68925 1.03829 0.86631 0.08777  0.05983  -0.19126 296 VAL   A C    
937  O  O    . VAL   A 144 ? 0.68901 1.05985 0.86576 0.06870  0.06590  -0.17249 296 VAL   A O    
938  C  CB   . VAL   A 144 ? 0.59673 0.85246 0.71477 0.07442  0.04671  -0.17181 296 VAL   A CB   
939  C  CG1  . VAL   A 144 ? 0.53615 0.79715 0.63499 0.04834  0.05302  -0.14404 296 VAL   A CG1  
940  C  CG2  . VAL   A 144 ? 0.59894 0.79273 0.70445 0.08023  0.02966  -0.16735 296 VAL   A CG2  
941  N  N    . SER   A 145 ? 0.67091 1.05688 0.86507 0.10455  0.06942  -0.22203 297 SER   A N    
942  C  CA   . SER   A 145 ? 0.69734 1.15658 0.91373 0.10136  0.08830  -0.23382 297 SER   A CA   
943  C  C    . SER   A 145 ? 0.71333 1.19632 0.97576 0.11529  0.07938  -0.23618 297 SER   A C    
944  O  O    . SER   A 145 ? 0.65922 1.19162 0.93835 0.10169  0.08985  -0.22921 297 SER   A O    
945  C  CB   . SER   A 145 ? 0.71642 1.21252 0.93466 0.11519  0.10329  -0.26896 297 SER   A CB   
946  O  OG   . SER   A 145 ? 0.81594 1.30012 1.06562 0.14875  0.09081  -0.29696 297 SER   A OG   
947  N  N    . LYS   A 146 ? 0.71774 1.16519 1.00089 0.14088  0.05861  -0.24415 298 LYS   A N    
948  C  CA   . LYS   A 146 ? 0.71874 1.17983 1.04207 0.15434  0.04461  -0.24177 298 LYS   A CA   
949  C  C    . LYS   A 146 ? 0.67501 1.10600 0.98529 0.13541  0.03213  -0.20768 298 LYS   A C    
950  O  O    . LYS   A 146 ? 0.76118 1.19683 1.09922 0.14477  0.01695  -0.20238 298 LYS   A O    
951  C  CB   . LYS   A 146 ? 0.76097 1.19131 1.10985 0.18924  0.02434  -0.26052 298 LYS   A CB   
952  C  CG   . LYS   A 146 ? 0.91451 1.39824 1.30114 0.21391  0.03386  -0.29773 298 LYS   A CG   
953  C  CD   . LYS   A 146 ? 1.01391 1.44896 1.39707 0.23754  0.02131  -0.31742 298 LYS   A CD   
954  C  CE   . LYS   A 146 ? 1.04968 1.42657 1.44788 0.25727  -0.00926 -0.30686 298 LYS   A CE   
955  N  NZ   . LYS   A 146 ? 1.12123 1.46104 1.52430 0.27951  -0.02074 -0.32775 298 LYS   A NZ   
956  N  N    . ALA   A 147 ? 0.55279 0.95367 0.82191 0.11035  0.03711  -0.18598 299 ALA   A N    
957  C  CA   . ALA   A 147 ? 0.56385 0.94958 0.82011 0.08855  0.03145  -0.15728 299 ALA   A CA   
958  C  C    . ALA   A 147 ? 0.53563 0.96825 0.78942 0.06236  0.05040  -0.14929 299 ALA   A C    
959  O  O    . ALA   A 147 ? 0.60895 1.03267 0.85516 0.04321  0.04648  -0.12793 299 ALA   A O    
960  C  CB   . ALA   A 147 ? 0.61048 0.93151 0.82624 0.07842  0.02323  -0.13791 299 ALA   A CB   
961  N  N    . GLY   A 148 ? 0.48394 0.96548 0.74293 0.06024  0.07063  -0.16597 300 GLY   A N    
962  C  CA   . GLY   A 148 ? 0.50461 1.03506 0.76312 0.03411  0.08943  -0.15763 300 GLY   A CA   
963  C  C    . GLY   A 148 ? 0.50971 1.03427 0.72666 0.01311  0.10489  -0.14829 300 GLY   A C    
964  O  O    . GLY   A 148 ? 0.57277 1.13646 0.78610 -0.01048 0.12085  -0.13908 300 GLY   A O    
965  N  N    . HIS   A 149 ? 0.54309 1.02133 0.72904 0.01974  0.09990  -0.14939 301 HIS   A N    
966  C  CA   . HIS   A 149 ? 0.57458 1.04186 0.71906 0.00020  0.11023  -0.13773 301 HIS   A CA   
967  C  C    . HIS   A 149 ? 0.64503 1.15062 0.78155 0.00649  0.12701  -0.16176 301 HIS   A C    
968  O  O    . HIS   A 149 ? 0.60635 1.11699 0.75957 0.03193  0.12463  -0.18945 301 HIS   A O    
969  C  CB   . HIS   A 149 ? 0.56997 0.96868 0.68524 0.00131  0.09485  -0.12455 301 HIS   A CB   
970  C  CG   . HIS   A 149 ? 0.54475 0.90903 0.65750 -0.01058 0.08245  -0.09909 301 HIS   A CG   
971  N  ND1  . HIS   A 149 ? 0.51521 0.88755 0.61822 -0.03573 0.08819  -0.07772 301 HIS   A ND1  
972  C  CD2  . HIS   A 149 ? 0.54171 0.86351 0.65937 -0.00110 0.06458  -0.09242 301 HIS   A CD2  
973  C  CE1  . HIS   A 149 ? 0.51501 0.85156 0.61822 -0.03965 0.07444  -0.06198 301 HIS   A CE1  
974  N  NE2  . HIS   A 149 ? 0.51907 0.82690 0.62968 -0.01937 0.06078  -0.07019 301 HIS   A NE2  
975  N  N    . THR   A 150 ? 0.75684 1.28816 0.86655 -0.01695 0.14319  -0.15100 302 THR   A N    
976  C  CA   . THR   A 150 ? 0.81412 1.38497 0.90758 -0.01547 0.16066  -0.17146 302 THR   A CA   
977  C  C    . THR   A 150 ? 0.89513 1.41865 0.95209 -0.00970 0.15215  -0.17488 302 THR   A C    
978  O  O    . THR   A 150 ? 0.97145 1.43605 1.02325 -0.00328 0.13350  -0.16534 302 THR   A O    
979  C  CB   . THR   A 150 ? 0.81558 1.41599 0.88960 -0.04471 0.17393  -0.15073 302 THR   A CB   
980  O  OG1  . THR   A 150 ? 0.77064 1.33798 0.80140 -0.06428 0.17158  -0.12625 302 THR   A OG1  
981  C  CG2  . THR   A 150 ? 0.76519 1.38366 0.86732 -0.05898 0.17408  -0.13328 302 THR   A CG2  
982  N  N    . LEU   A 151 ? 0.88360 1.43163 0.91390 -0.01352 0.16442  -0.18725 303 LEU   A N    
983  C  CA   . LEU   A 151 ? 0.80743 1.32098 0.80096 -0.01186 0.15823  -0.19136 303 LEU   A CA   
984  C  C    . LEU   A 151 ? 0.75935 1.25878 0.71177 -0.03971 0.15878  -0.15870 303 LEU   A C    
985  O  O    . LEU   A 151 ? 0.76113 1.22828 0.68295 -0.04062 0.15017  -0.15687 303 LEU   A O    
986  C  CB   . LEU   A 151 ? 0.83162 1.36365 0.81934 0.00181  0.16270  -0.22156 303 LEU   A CB   
987  C  CG   . LEU   A 151 ? 0.83233 1.36690 0.86136 0.03274  0.15768  -0.25443 303 LEU   A CG   
988  C  CD1  . LEU   A 151 ? 0.88367 1.47150 0.94128 0.03593  0.16928  -0.26503 303 LEU   A CD1  
989  C  CD2  . LEU   A 151 ? 0.77126 1.27771 0.78966 0.05146  0.14891  -0.28263 303 LEU   A CD2  
990  N  N    . GLU   A 152 ? 0.78566 1.30058 0.73953 -0.06170 0.16421  -0.13124 304 GLU   A N    
991  C  CA   . GLU   A 152 ? 0.78597 1.27402 0.70843 -0.08562 0.15916  -0.09632 304 GLU   A CA   
992  C  C    . GLU   A 152 ? 0.73786 1.16560 0.65807 -0.08024 0.14022  -0.08425 304 GLU   A C    
993  O  O    . GLU   A 152 ? 0.66593 1.06317 0.55716 -0.09206 0.13213  -0.06332 304 GLU   A O    
994  C  CB   . GLU   A 152 ? 0.86696 1.37024 0.80141 -0.10674 0.16369  -0.07082 304 GLU   A CB   
995  C  CG   . GLU   A 152 ? 1.02199 1.55640 0.94063 -0.12251 0.17374  -0.06320 304 GLU   A CG   
996  C  CD   . GLU   A 152 ? 1.13104 1.65268 1.04176 -0.14870 0.17120  -0.02748 304 GLU   A CD   
997  O  OE1  . GLU   A 152 ? 1.14129 1.68818 1.07622 -0.15785 0.17764  -0.02300 304 GLU   A OE1  
998  O  OE2  . GLU   A 152 ? 1.16476 1.64954 1.04678 -0.15932 0.16139  -0.00463 304 GLU   A OE2  
999  N  N    . LEU   A 153 ? 0.62415 1.02993 0.57640 -0.06159 0.13003  -0.09541 305 LEU   A N    
1000 C  CA   . LEU   A 153 ? 0.62875 0.97535 0.58239 -0.05445 0.11073  -0.08547 305 LEU   A CA   
1001 C  C    . LEU   A 153 ? 0.58608 0.90752 0.54250 -0.03257 0.10124  -0.10912 305 LEU   A C    
1002 O  O    . LEU   A 153 ? 0.58975 0.86837 0.53163 -0.03204 0.08853  -0.10158 305 LEU   A O    
1003 C  CB   . LEU   A 153 ? 0.50547 0.84116 0.48969 -0.05309 0.10404  -0.07541 305 LEU   A CB   
1004 C  CG   . LEU   A 153 ? 0.44241 0.72395 0.43206 -0.04338 0.08572  -0.06889 305 LEU   A CG   
1005 C  CD1  . LEU   A 153 ? 0.38786 0.63520 0.35366 -0.05870 0.07876  -0.04350 305 LEU   A CD1  
1006 C  CD2  . LEU   A 153 ? 0.47684 0.75930 0.49882 -0.03638 0.08002  -0.06874 305 LEU   A CD2  
1007 N  N    . ILE   A 154 ? 0.58886 0.93637 0.56565 -0.01461 0.10678  -0.13823 306 ILE   A N    
1008 C  CA   . ILE   A 154 ? 0.63953 0.95758 0.62312 0.00676  0.09565  -0.16123 306 ILE   A CA   
1009 C  C    . ILE   A 154 ? 0.70210 1.01035 0.65210 0.00332  0.09491  -0.16994 306 ILE   A C    
1010 O  O    . ILE   A 154 ? 0.66282 0.92783 0.60793 0.01005  0.08065  -0.17361 306 ILE   A O    
1011 C  CB   . ILE   A 154 ? 0.64572 0.99466 0.66227 0.02875  0.10084  -0.19186 306 ILE   A CB   
1012 C  CG1  . ILE   A 154 ? 0.60092 0.94950 0.65314 0.03517  0.09480  -0.18291 306 ILE   A CG1  
1013 C  CG2  . ILE   A 154 ? 0.65402 0.97296 0.67424 0.05006  0.09003  -0.21878 306 ILE   A CG2  
1014 C  CD1  . ILE   A 154 ? 0.65807 1.02851 0.74780 0.06117  0.09425  -0.21216 306 ILE   A CD1  
1015 N  N    . GLU   A 155 ? 0.75886 1.10841 0.68438 -0.00874 0.10970  -0.17262 307 GLU   A N    
1016 C  CA   . GLU   A 155 ? 0.79117 1.13471 0.68205 -0.01252 0.10760  -0.18142 307 GLU   A CA   
1017 C  C    . GLU   A 155 ? 0.74052 1.04108 0.61013 -0.02580 0.09339  -0.15369 307 GLU   A C    
1018 O  O    . GLU   A 155 ? 0.74886 1.01664 0.61116 -0.01965 0.08057  -0.16296 307 GLU   A O    
1019 C  CB   . GLU   A 155 ? 0.87431 1.27492 0.73990 -0.02379 0.12669  -0.18844 307 GLU   A CB   
1020 C  CG   . GLU   A 155 ? 0.96914 1.36688 0.79702 -0.02741 0.12317  -0.19889 307 GLU   A CG   
1021 C  CD   . GLU   A 155 ? 1.08277 1.49741 0.87860 -0.05066 0.12744  -0.17020 307 GLU   A CD   
1022 O  OE1  . GLU   A 155 ? 1.15040 1.56053 0.91706 -0.05472 0.12175  -0.17287 307 GLU   A OE1  
1023 O  OE2  . GLU   A 155 ? 1.10791 1.53815 0.90897 -0.06486 0.13494  -0.14481 307 GLU   A OE2  
1024 N  N    . PRO   A 156 ? 0.73475 1.03292 0.59620 -0.04346 0.09400  -0.12109 308 PRO   A N    
1025 C  CA   . PRO   A 156 ? 0.71659 0.97318 0.56390 -0.05180 0.07915  -0.09815 308 PRO   A CA   
1026 C  C    . PRO   A 156 ? 0.64286 0.85474 0.51382 -0.04024 0.06496  -0.09845 308 PRO   A C    
1027 O  O    . PRO   A 156 ? 0.65078 0.83105 0.51267 -0.04220 0.05256  -0.09132 308 PRO   A O    
1028 C  CB   . PRO   A 156 ? 0.75827 1.02214 0.59869 -0.07037 0.08329  -0.06615 308 PRO   A CB   
1029 C  CG   . PRO   A 156 ? 0.74671 1.04476 0.60884 -0.07034 0.09706  -0.07080 308 PRO   A CG   
1030 C  CD   . PRO   A 156 ? 0.64770 0.98027 0.51286 -0.05744 0.10740  -0.10408 308 PRO   A CD   
1031 N  N    . LEU   A 157 ? 0.62788 0.83866 0.52896 -0.02879 0.06608  -0.10601 309 LEU   A N    
1032 C  CA   . LEU   A 157 ? 0.56917 0.73834 0.48951 -0.01908 0.05254  -0.10412 309 LEU   A CA   
1033 C  C    . LEU   A 157 ? 0.56295 0.70880 0.48192 -0.00795 0.04329  -0.12523 309 LEU   A C    
1034 O  O    . LEU   A 157 ? 0.54994 0.65973 0.46695 -0.00995 0.03122  -0.11704 309 LEU   A O    
1035 C  CB   . LEU   A 157 ? 0.56992 0.74580 0.52087 -0.00894 0.05412  -0.10729 309 LEU   A CB   
1036 C  CG   . LEU   A 157 ? 0.50682 0.64068 0.47427 0.00022  0.03969  -0.10307 309 LEU   A CG   
1037 C  CD1  . LEU   A 157 ? 0.43423 0.54078 0.39003 -0.01281 0.03302  -0.07752 309 LEU   A CD1  
1038 C  CD2  . LEU   A 157 ? 0.48403 0.62666 0.48034 0.01116  0.03892  -0.10606 309 LEU   A CD2  
1039 N  N    . ILE   A 158 ? 0.55389 0.72078 0.47537 0.00343  0.04890  -0.15375 310 ILE   A N    
1040 C  CA   . ILE   A 158 ? 0.65706 0.79906 0.57836 0.01389  0.03897  -0.17681 310 ILE   A CA   
1041 C  C    . ILE   A 158 ? 0.67220 0.80575 0.56418 0.00113  0.03363  -0.17278 310 ILE   A C    
1042 O  O    . ILE   A 158 ? 0.76835 0.86674 0.66111 0.00154  0.02027  -0.17571 310 ILE   A O    
1043 C  CB   . ILE   A 158 ? 0.67711 0.84611 0.60824 0.03050  0.04664  -0.21191 310 ILE   A CB   
1044 C  CG1  . ILE   A 158 ? 0.67940 0.85479 0.64543 0.04580  0.04828  -0.21628 310 ILE   A CG1  
1045 C  CG2  . ILE   A 158 ? 0.68670 0.82710 0.61572 0.04020  0.03526  -0.23812 310 ILE   A CG2  
1046 C  CD1  . ILE   A 158 ? 0.70067 0.82549 0.68823 0.05632  0.03079  -0.21227 310 ILE   A CD1  
1047 N  N    . LYS   A 159 ? 0.59950 0.76587 0.46565 -0.01143 0.04298  -0.16472 311 LYS   A N    
1048 C  CA   . LYS   A 159 ? 0.67112 0.83221 0.50888 -0.02344 0.03584  -0.15821 311 LYS   A CA   
1049 C  C    . LYS   A 159 ? 0.65179 0.77858 0.49420 -0.03159 0.02360  -0.13145 311 LYS   A C    
1050 O  O    . LYS   A 159 ? 0.56494 0.67188 0.40033 -0.03516 0.01164  -0.13300 311 LYS   A O    
1051 C  CB   . LYS   A 159 ? 0.76352 0.96564 0.57149 -0.03613 0.04722  -0.14925 311 LYS   A CB   
1052 C  CG   . LYS   A 159 ? 0.85352 1.09433 0.64673 -0.03080 0.05876  -0.17941 311 LYS   A CG   
1053 C  CD   . LYS   A 159 ? 0.98749 1.26907 0.74573 -0.04700 0.06967  -0.16591 311 LYS   A CD   
1054 C  CE   . LYS   A 159 ? 1.00668 1.26950 0.74477 -0.06268 0.05790  -0.13279 311 LYS   A CE   
1055 N  NZ   . LYS   A 159 ? 1.05490 1.34558 0.75005 -0.07493 0.05885  -0.13046 311 LYS   A NZ   
1056 N  N    . PHE   A 160 ? 0.56432 0.68639 0.41972 -0.03482 0.02649  -0.10842 312 PHE   A N    
1057 C  CA   . PHE   A 160 ? 0.52110 0.61302 0.38360 -0.04036 0.01638  -0.08646 312 PHE   A CA   
1058 C  C    . PHE   A 160 ? 0.55632 0.61455 0.43699 -0.03275 0.00598  -0.09616 312 PHE   A C    
1059 O  O    . PHE   A 160 ? 0.56979 0.60836 0.44898 -0.03828 -0.00408 -0.09005 312 PHE   A O    
1060 C  CB   . PHE   A 160 ? 0.47908 0.57235 0.35278 -0.04378 0.02167  -0.06499 312 PHE   A CB   
1061 C  CG   . PHE   A 160 ? 0.55512 0.61845 0.44035 -0.04590 0.01294  -0.04787 312 PHE   A CG   
1062 C  CD1  . PHE   A 160 ? 0.56528 0.62293 0.44046 -0.05497 0.00766  -0.02983 312 PHE   A CD1  
1063 C  CD2  . PHE   A 160 ? 0.51860 0.56130 0.42453 -0.03829 0.00974  -0.04998 312 PHE   A CD2  
1064 C  CE1  . PHE   A 160 ? 0.57244 0.60767 0.45964 -0.05583 0.00134  -0.01716 312 PHE   A CE1  
1065 C  CE2  . PHE   A 160 ? 0.56555 0.58542 0.47923 -0.04129 0.00352  -0.03512 312 PHE   A CE2  
1066 C  CZ   . PHE   A 160 ? 0.55775 0.57560 0.46289 -0.04979 0.00033  -0.02016 312 PHE   A CZ   
1067 N  N    . GLN   A 161 ? 0.54235 0.59431 0.44172 -0.02052 0.00764  -0.11025 313 GLN   A N    
1068 C  CA   . GLN   A 161 ? 0.47296 0.48913 0.38896 -0.01414 -0.00332 -0.11678 313 GLN   A CA   
1069 C  C    . GLN   A 161 ? 0.56310 0.56679 0.47047 -0.01585 -0.01211 -0.13445 313 GLN   A C    
1070 O  O    . GLN   A 161 ? 0.57016 0.54587 0.48287 -0.02157 -0.02268 -0.12872 313 GLN   A O    
1071 C  CB   . GLN   A 161 ? 0.53835 0.55162 0.47516 0.00143  -0.00180 -0.13024 313 GLN   A CB   
1072 C  CG   . GLN   A 161 ? 0.50707 0.52950 0.45630 0.00293  0.00357  -0.11346 313 GLN   A CG   
1073 C  CD   . GLN   A 161 ? 0.54547 0.53976 0.49979 -0.00351 -0.00389 -0.09055 313 GLN   A CD   
1074 O  OE1  . GLN   A 161 ? 0.62579 0.58908 0.58393 -0.00402 -0.01390 -0.08996 313 GLN   A OE1  
1075 N  NE2  . GLN   A 161 ? 0.51704 0.52279 0.47137 -0.00940 0.00123  -0.07221 313 GLN   A NE2  
1076 N  N    . VAL   A 162 ? 0.59823 0.62492 0.49198 -0.01216 -0.00758 -0.15687 314 VAL   A N    
1077 C  CA   . VAL   A 162 ? 0.64856 0.66491 0.53291 -0.01358 -0.01679 -0.17797 314 VAL   A CA   
1078 C  C    . VAL   A 162 ? 0.61213 0.62834 0.48094 -0.02923 -0.02399 -0.16212 314 VAL   A C    
1079 O  O    . VAL   A 162 ? 0.70483 0.69621 0.57959 -0.03478 -0.03633 -0.16438 314 VAL   A O    
1080 C  CB   . VAL   A 162 ? 0.62523 0.67230 0.49512 -0.00586 -0.00876 -0.20728 314 VAL   A CB   
1081 C  CG1  . VAL   A 162 ? 0.61630 0.66017 0.46792 -0.01135 -0.01827 -0.22685 314 VAL   A CG1  
1082 C  CG2  . VAL   A 162 ? 0.65109 0.69285 0.54356 0.01295  -0.00574 -0.22981 314 VAL   A CG2  
1083 N  N    . GLY   A 163 ? 0.59688 0.64106 0.44744 -0.03688 -0.01733 -0.14525 315 GLY   A N    
1084 C  CA   . GLY   A 163 ? 0.55299 0.59882 0.39120 -0.04929 -0.02573 -0.12914 315 GLY   A CA   
1085 C  C    . GLY   A 163 ? 0.65885 0.67932 0.51715 -0.05389 -0.03271 -0.10895 315 GLY   A C    
1086 O  O    . GLY   A 163 ? 0.64244 0.65723 0.50093 -0.06198 -0.04321 -0.10422 315 GLY   A O    
1087 N  N    . LEU   A 164 ? 0.54409 0.55250 0.41978 -0.04908 -0.02697 -0.09770 316 LEU   A N    
1088 C  CA   . LEU   A 164 ? 0.55002 0.53692 0.44291 -0.05343 -0.03189 -0.08039 316 LEU   A CA   
1089 C  C    . LEU   A 164 ? 0.57180 0.53065 0.47884 -0.05427 -0.04114 -0.09167 316 LEU   A C    
1090 O  O    . LEU   A 164 ? 0.67699 0.62550 0.59227 -0.06333 -0.04821 -0.08279 316 LEU   A O    
1091 C  CB   . LEU   A 164 ? 0.53698 0.52088 0.44047 -0.04881 -0.02379 -0.06594 316 LEU   A CB   
1092 C  CG   . LEU   A 164 ? 0.57522 0.54059 0.49346 -0.05281 -0.02671 -0.04895 316 LEU   A CG   
1093 C  CD1  . LEU   A 164 ? 0.51356 0.48707 0.42900 -0.06140 -0.03055 -0.03585 316 LEU   A CD1  
1094 C  CD2  . LEU   A 164 ? 0.51733 0.48241 0.44234 -0.04801 -0.01950 -0.03777 316 LEU   A CD2  
1095 N  N    . LYS   A 165 ? 0.57587 0.52225 0.48784 -0.04512 -0.04152 -0.11117 317 LYS   A N    
1096 C  CA   . LYS   A 165 ? 0.57352 0.48734 0.49887 -0.04659 -0.05222 -0.12161 317 LYS   A CA   
1097 C  C    . LYS   A 165 ? 0.61159 0.52588 0.52989 -0.05647 -0.06223 -0.13419 317 LYS   A C    
1098 O  O    . LYS   A 165 ? 0.70661 0.59783 0.63713 -0.06593 -0.07199 -0.13251 317 LYS   A O    
1099 C  CB   . LYS   A 165 ? 0.65283 0.55206 0.58620 -0.03188 -0.05234 -0.14205 317 LYS   A CB   
1100 C  CG   . LYS   A 165 ? 0.66017 0.51646 0.61144 -0.03218 -0.06385 -0.14411 317 LYS   A CG   
1101 C  CD   . LYS   A 165 ? 0.75079 0.59267 0.71424 -0.02944 -0.06186 -0.12186 317 LYS   A CD   
1102 C  CE   . LYS   A 165 ? 0.80898 0.60635 0.78706 -0.03226 -0.07433 -0.11891 317 LYS   A CE   
1103 N  NZ   . LYS   A 165 ? 0.78770 0.57249 0.77375 -0.02837 -0.07345 -0.09781 317 LYS   A NZ   
1104 N  N    . LYS   A 166 ? 0.55764 0.49963 0.45565 -0.05605 -0.06042 -0.14596 318 LYS   A N    
1105 C  CA   . LYS   A 166 ? 0.62129 0.56777 0.51016 -0.06557 -0.07154 -0.15864 318 LYS   A CA   
1106 C  C    . LYS   A 166 ? 0.63401 0.58704 0.52828 -0.07890 -0.07762 -0.13713 318 LYS   A C    
1107 O  O    . LYS   A 166 ? 0.65828 0.61031 0.55400 -0.08887 -0.08957 -0.14529 318 LYS   A O    
1108 C  CB   . LYS   A 166 ? 0.73381 0.71207 0.59504 -0.06203 -0.06787 -0.17467 318 LYS   A CB   
1109 C  CG   . LYS   A 166 ? 0.78125 0.75631 0.63850 -0.04965 -0.06458 -0.20630 318 LYS   A CG   
1110 C  CD   . LYS   A 166 ? 0.84197 0.85681 0.66989 -0.04613 -0.05541 -0.21808 318 LYS   A CD   
1111 C  CE   . LYS   A 166 ? 0.90240 0.91764 0.72477 -0.03538 -0.05509 -0.25736 318 LYS   A CE   
1112 N  NZ   . LYS   A 166 ? 0.96289 1.02259 0.75384 -0.03334 -0.04407 -0.26978 318 LYS   A NZ   
1113 N  N    . LEU   A 167 ? 0.61156 0.57259 0.51090 -0.07887 -0.07025 -0.11172 319 LEU   A N    
1114 C  CA   . LEU   A 167 ? 0.56359 0.53172 0.47319 -0.08887 -0.07540 -0.09341 319 LEU   A CA   
1115 C  C    . LEU   A 167 ? 0.63023 0.57480 0.56354 -0.09774 -0.08068 -0.09037 319 LEU   A C    
1116 O  O    . LEU   A 167 ? 0.59807 0.55178 0.54313 -0.10806 -0.08661 -0.08171 319 LEU   A O    
1117 C  CB   . LEU   A 167 ? 0.45510 0.43596 0.36452 -0.08497 -0.06617 -0.07014 319 LEU   A CB   
1118 C  CG   . LEU   A 167 ? 0.50781 0.51253 0.39475 -0.08054 -0.06197 -0.06559 319 LEU   A CG   
1119 C  CD1  . LEU   A 167 ? 0.53107 0.54157 0.42302 -0.07883 -0.05629 -0.04201 319 LEU   A CD1  
1120 C  CD2  . LEU   A 167 ? 0.54198 0.56545 0.41333 -0.08612 -0.07309 -0.07229 319 LEU   A CD2  
1121 N  N    . ASN   A 168 ? 0.66742 0.58342 0.60871 -0.09429 -0.07911 -0.09648 320 ASN   A N    
1122 C  CA   . ASN   A 168 ? 0.67461 0.56385 0.63570 -0.10429 -0.08394 -0.09055 320 ASN   A CA   
1123 C  C    . ASN   A 168 ? 0.59730 0.49960 0.57063 -0.11301 -0.07970 -0.06698 320 ASN   A C    
1124 O  O    . ASN   A 168 ? 0.61843 0.52463 0.60564 -0.12705 -0.08567 -0.06333 320 ASN   A O    
1125 C  CB   . ASN   A 168 ? 0.76282 0.63816 0.72966 -0.11527 -0.09768 -0.10865 320 ASN   A CB   
1126 C  CG   . ASN   A 168 ? 1.00918 0.87721 0.96212 -0.10546 -0.10194 -0.13681 320 ASN   A CG   
1127 O  OD1  . ASN   A 168 ? 1.08659 0.92949 1.04165 -0.09529 -0.10085 -0.14658 320 ASN   A OD1  
1128 N  ND2  . ASN   A 168 ? 1.02915 0.92080 0.96782 -0.10770 -0.10744 -0.15093 320 ASN   A ND2  
1129 N  N    . LEU   A 169 ? 0.54729 0.45888 0.51659 -0.10445 -0.06900 -0.05260 321 LEU   A N    
1130 C  CA   . LEU   A 169 ? 0.47342 0.39994 0.45300 -0.10953 -0.06364 -0.03355 321 LEU   A CA   
1131 C  C    . LEU   A 169 ? 0.55618 0.46504 0.55082 -0.12104 -0.06339 -0.02413 321 LEU   A C    
1132 O  O    . LEU   A 169 ? 0.57543 0.45580 0.56926 -0.12012 -0.06428 -0.02480 321 LEU   A O    
1133 C  CB   . LEU   A 169 ? 0.47146 0.40652 0.44284 -0.09802 -0.05320 -0.02281 321 LEU   A CB   
1134 C  CG   . LEU   A 169 ? 0.43528 0.38985 0.39161 -0.08946 -0.05177 -0.02544 321 LEU   A CG   
1135 C  CD1  . LEU   A 169 ? 0.45799 0.41744 0.41098 -0.08177 -0.04227 -0.01276 321 LEU   A CD1  
1136 C  CD2  . LEU   A 169 ? 0.43818 0.41463 0.39628 -0.09457 -0.05916 -0.02462 321 LEU   A CD2  
1137 N  N    . HIS   A 170 ? 0.52713 0.45449 0.53618 -0.13209 -0.06262 -0.01481 322 HIS   A N    
1138 C  CA   . HIS   A 170 ? 0.47862 0.39810 0.49905 -0.14346 -0.05777 -0.00102 322 HIS   A CA   
1139 C  C    . HIS   A 170 ? 0.54222 0.45790 0.55329 -0.13344 -0.04720 0.01067  322 HIS   A C    
1140 O  O    . HIS   A 170 ? 0.47021 0.39886 0.47269 -0.12034 -0.04250 0.01034  322 HIS   A O    
1141 C  CB   . HIS   A 170 ? 0.45727 0.40762 0.49686 -0.15562 -0.05621 0.00527  322 HIS   A CB   
1142 C  CG   . HIS   A 170 ? 0.52091 0.47876 0.57293 -0.16777 -0.06799 -0.00560 322 HIS   A CG   
1143 N  ND1  . HIS   A 170 ? 0.50129 0.48551 0.57635 -0.18273 -0.06867 -0.00143 322 HIS   A ND1  
1144 C  CD2  . HIS   A 170 ? 0.51997 0.46521 0.56525 -0.16750 -0.07985 -0.02215 322 HIS   A CD2  
1145 C  CE1  . HIS   A 170 ? 0.53105 0.51748 0.61379 -0.19199 -0.08176 -0.01400 322 HIS   A CE1  
1146 N  NE2  . HIS   A 170 ? 0.52749 0.48933 0.59077 -0.18285 -0.08888 -0.02728 322 HIS   A NE2  
1147 N  N    . GLU   A 171 ? 0.54228 0.43900 0.55408 -0.14093 -0.04463 0.02177  323 GLU   A N    
1148 C  CA   . GLU   A 171 ? 0.53474 0.43060 0.53709 -0.13349 -0.03576 0.03324  323 GLU   A CA   
1149 C  C    . GLU   A 171 ? 0.50044 0.42982 0.50637 -0.13015 -0.02623 0.03770  323 GLU   A C    
1150 O  O    . GLU   A 171 ? 0.48604 0.41942 0.48271 -0.11857 -0.02057 0.04001  323 GLU   A O    
1151 C  CB   . GLU   A 171 ? 0.58174 0.45687 0.58329 -0.14582 -0.03539 0.04752  323 GLU   A CB   
1152 C  CG   . GLU   A 171 ? 0.64249 0.50724 0.62987 -0.13698 -0.03112 0.05739  323 GLU   A CG   
1153 C  CD   . GLU   A 171 ? 0.65933 0.50596 0.64262 -0.15120 -0.03154 0.07497  323 GLU   A CD   
1154 O  OE1  . GLU   A 171 ? 0.67319 0.52111 0.66619 -0.16986 -0.03199 0.08085  323 GLU   A OE1  
1155 O  OE2  . GLU   A 171 ? 0.68515 0.51741 0.65541 -0.14495 -0.03208 0.08394  323 GLU   A OE2  
1156 N  N    . GLU   A 172 ? 0.47041 0.42440 0.49209 -0.13962 -0.02537 0.03754  324 GLU   A N    
1157 C  CA   . GLU   A 172 ? 0.46197 0.44802 0.49138 -0.13374 -0.01799 0.03893  324 GLU   A CA   
1158 C  C    . GLU   A 172 ? 0.46623 0.45756 0.48918 -0.11775 -0.02142 0.03173  324 GLU   A C    
1159 O  O    . GLU   A 172 ? 0.49470 0.49484 0.51444 -0.10746 -0.01570 0.03412  324 GLU   A O    
1160 C  CB   . GLU   A 172 ? 0.44262 0.45703 0.49498 -0.14613 -0.01810 0.03845  324 GLU   A CB   
1161 C  CG   . GLU   A 172 ? 0.48664 0.50392 0.54642 -0.16472 -0.01137 0.04857  324 GLU   A CG   
1162 C  CD   . GLU   A 172 ? 0.58921 0.58101 0.65086 -0.18123 -0.02050 0.04953  324 GLU   A CD   
1163 O  OE1  . GLU   A 172 ? 0.69299 0.69332 0.76705 -0.20100 -0.01726 0.05761  324 GLU   A OE1  
1164 O  OE2  . GLU   A 172 ? 0.55597 0.51961 0.60738 -0.17511 -0.03065 0.04168  324 GLU   A OE2  
1165 N  N    . GLU   A 173 ? 0.48334 0.46900 0.50313 -0.11661 -0.03109 0.02291  325 GLU   A N    
1166 C  CA   . GLU   A 173 ? 0.42096 0.41162 0.43051 -0.10403 -0.03426 0.01857  325 GLU   A CA   
1167 C  C    . GLU   A 173 ? 0.40278 0.37599 0.39532 -0.09449 -0.02970 0.01953  325 GLU   A C    
1168 O  O    . GLU   A 173 ? 0.42236 0.40182 0.40824 -0.08535 -0.02754 0.02171  325 GLU   A O    
1169 C  CB   . GLU   A 173 ? 0.41960 0.41174 0.42634 -0.10677 -0.04535 0.00813  325 GLU   A CB   
1170 C  CG   . GLU   A 173 ? 0.40328 0.41894 0.42868 -0.11497 -0.05232 0.00659  325 GLU   A CG   
1171 C  CD   . GLU   A 173 ? 0.48769 0.49825 0.51333 -0.12464 -0.06364 -0.00516 325 GLU   A CD   
1172 O  OE1  . GLU   A 173 ? 0.51809 0.54876 0.56103 -0.13344 -0.07086 -0.00741 325 GLU   A OE1  
1173 O  OE2  . GLU   A 173 ? 0.49552 0.48357 0.50583 -0.12305 -0.06587 -0.01384 325 GLU   A OE2  
1174 N  N    . HIS   A 174 ? 0.43303 0.38430 0.42039 -0.09686 -0.02925 0.01858  326 HIS   A N    
1175 C  CA   . HIS   A 174 ? 0.44111 0.37923 0.41643 -0.08738 -0.02612 0.01839  326 HIS   A CA   
1176 C  C    . HIS   A 174 ? 0.48392 0.42783 0.45783 -0.08325 -0.01831 0.02781  326 HIS   A C    
1177 O  O    . HIS   A 174 ? 0.47552 0.42199 0.44243 -0.07497 -0.01578 0.02772  326 HIS   A O    
1178 C  CB   . HIS   A 174 ? 0.54094 0.45348 0.51498 -0.08954 -0.02993 0.01566  326 HIS   A CB   
1179 C  CG   . HIS   A 174 ? 0.65367 0.55533 0.61999 -0.07887 -0.02813 0.01491  326 HIS   A CG   
1180 N  ND1  . HIS   A 174 ? 0.62982 0.53587 0.59023 -0.06926 -0.02831 0.00439  326 HIS   A ND1  
1181 C  CD2  . HIS   A 174 ? 0.64152 0.53133 0.60582 -0.07676 -0.02659 0.02325  326 HIS   A CD2  
1182 C  CE1  . HIS   A 174 ? 0.69276 0.59181 0.65156 -0.06126 -0.02668 0.00548  326 HIS   A CE1  
1183 N  NE2  . HIS   A 174 ? 0.65317 0.54109 0.61378 -0.06516 -0.02677 0.01705  326 HIS   A NE2  
1184 N  N    . VAL   A 175 ? 0.47056 0.41819 0.45079 -0.09014 -0.01416 0.03524  327 VAL   A N    
1185 C  CA   . VAL   A 175 ? 0.40986 0.36345 0.38670 -0.08629 -0.00687 0.04124  327 VAL   A CA   
1186 C  C    . VAL   A 175 ? 0.50935 0.48194 0.49232 -0.08030 -0.00450 0.03952  327 VAL   A C    
1187 O  O    . VAL   A 175 ? 0.40244 0.37577 0.38083 -0.07354 -0.00100 0.04041  327 VAL   A O    
1188 C  CB   . VAL   A 175 ? 0.42129 0.37545 0.39942 -0.09625 -0.00208 0.04927  327 VAL   A CB   
1189 C  CG1  . VAL   A 175 ? 0.48178 0.41070 0.45294 -0.10148 -0.00713 0.05383  327 VAL   A CG1  
1190 C  CG2  . VAL   A 175 ? 0.40980 0.38392 0.40345 -0.10582 -0.00004 0.04932  327 VAL   A CG2  
1191 N  N    . LEU   A 176 ? 0.45317 0.44005 0.44771 -0.08243 -0.00804 0.03685  328 LEU   A N    
1192 C  CA   . LEU   A 176 ? 0.41876 0.42029 0.42053 -0.07459 -0.00904 0.03601  328 LEU   A CA   
1193 C  C    . LEU   A 176 ? 0.41242 0.40489 0.40222 -0.06728 -0.01319 0.03603  328 LEU   A C    
1194 O  O    . LEU   A 176 ? 0.46077 0.45370 0.45042 -0.06036 -0.01243 0.03826  328 LEU   A O    
1195 C  CB   . LEU   A 176 ? 0.40997 0.43062 0.42832 -0.07802 -0.01446 0.03373  328 LEU   A CB   
1196 C  CG   . LEU   A 176 ? 0.46285 0.50453 0.49995 -0.08379 -0.00851 0.03374  328 LEU   A CG   
1197 C  CD1  . LEU   A 176 ? 0.39235 0.45132 0.44628 -0.09178 -0.01547 0.03096  328 LEU   A CD1  
1198 C  CD2  . LEU   A 176 ? 0.38576 0.44211 0.43307 -0.07297 -0.00389 0.03213  328 LEU   A CD2  
1199 N  N    . LEU   A 177 ? 0.39500 0.37939 0.37487 -0.06940 -0.01732 0.03301  329 LEU   A N    
1200 C  CA   . LEU   A 177 ? 0.45146 0.43252 0.41871 -0.06469 -0.01918 0.03329  329 LEU   A CA   
1201 C  C    . LEU   A 177 ? 0.39550 0.36764 0.35669 -0.06113 -0.01326 0.03574  329 LEU   A C    
1202 O  O    . LEU   A 177 ? 0.36988 0.34239 0.32678 -0.05806 -0.01312 0.03966  329 LEU   A O    
1203 C  CB   . LEU   A 177 ? 0.46925 0.44783 0.42721 -0.06728 -0.02310 0.02594  329 LEU   A CB   
1204 C  CG   . LEU   A 177 ? 0.52378 0.50660 0.46700 -0.06454 -0.02389 0.02557  329 LEU   A CG   
1205 C  CD1  . LEU   A 177 ? 0.50924 0.50186 0.45103 -0.06355 -0.02925 0.03379  329 LEU   A CD1  
1206 C  CD2  . LEU   A 177 ? 0.44815 0.43178 0.38225 -0.06629 -0.02675 0.01396  329 LEU   A CD2  
1207 N  N    . MET   A 178 ? 0.44029 0.40383 0.40122 -0.06247 -0.00971 0.03448  330 MET   A N    
1208 C  CA   . MET   A 178 ? 0.45296 0.41080 0.40968 -0.05930 -0.00581 0.03644  330 MET   A CA   
1209 C  C    . MET   A 178 ? 0.42691 0.38842 0.38765 -0.05714 -0.00334 0.03965  330 MET   A C    
1210 O  O    . MET   A 178 ? 0.45413 0.41327 0.41213 -0.05468 -0.00282 0.04094  330 MET   A O    
1211 C  CB   . MET   A 178 ? 0.38110 0.32907 0.33642 -0.06093 -0.00498 0.03652  330 MET   A CB   
1212 C  CG   . MET   A 178 ? 0.51542 0.45470 0.46852 -0.05971 -0.00861 0.03125  330 MET   A CG   
1213 S  SD   . MET   A 178 ? 0.49338 0.41676 0.44484 -0.05844 -0.01073 0.03435  330 MET   A SD   
1214 C  CE   . MET   A 178 ? 0.48524 0.40353 0.43824 -0.06884 -0.01030 0.04205  330 MET   A CE   
1215 N  N    . ALA   A 179 ? 0.44207 0.41040 0.41102 -0.05837 -0.00174 0.03966  331 ALA   A N    
1216 C  CA   . ALA   A 179 ? 0.39421 0.36727 0.36900 -0.05417 0.00095  0.03880  331 ALA   A CA   
1217 C  C    . ALA   A 179 ? 0.41127 0.38362 0.39031 -0.04894 -0.00417 0.04028  331 ALA   A C    
1218 O  O    . ALA   A 179 ? 0.38216 0.34733 0.36072 -0.04530 -0.00440 0.04017  331 ALA   A O    
1219 C  CB   . ALA   A 179 ? 0.40567 0.39276 0.39090 -0.05633 0.00506  0.03679  331 ALA   A CB   
1220 N  N    . ILE   A 180 ? 0.41961 0.39785 0.40211 -0.04930 -0.00980 0.04231  332 ILE   A N    
1221 C  CA   . ILE   A 180 ? 0.41741 0.39333 0.40093 -0.04513 -0.01694 0.04725  332 ILE   A CA   
1222 C  C    . ILE   A 180 ? 0.48263 0.44693 0.45291 -0.04739 -0.01693 0.05201  332 ILE   A C    
1223 O  O    . ILE   A 180 ? 0.44248 0.39770 0.41359 -0.04512 -0.02033 0.05695  332 ILE   A O    
1224 C  CB   . ILE   A 180 ? 0.33965 0.32585 0.32467 -0.04657 -0.02438 0.04910  332 ILE   A CB   
1225 C  CG1  . ILE   A 180 ? 0.42760 0.42970 0.43185 -0.04444 -0.02554 0.04490  332 ILE   A CG1  
1226 C  CG2  . ILE   A 180 ? 0.38668 0.36841 0.36559 -0.04409 -0.03314 0.05786  332 ILE   A CG2  
1227 C  CD1  . ILE   A 180 ? 0.43208 0.44680 0.43890 -0.04908 -0.03246 0.04393  332 ILE   A CD1  
1228 N  N    . CYS   A 181 ? 0.44896 0.41373 0.40895 -0.05212 -0.01340 0.05023  333 CYS   A N    
1229 C  CA   . CYS   A 181 ? 0.53166 0.49258 0.48226 -0.05517 -0.01163 0.05339  333 CYS   A CA   
1230 C  C    . CYS   A 181 ? 0.46135 0.41340 0.41584 -0.05448 -0.00943 0.05355  333 CYS   A C    
1231 O  O    . CYS   A 181 ? 0.45730 0.40381 0.40943 -0.05757 -0.01091 0.05920  333 CYS   A O    
1232 C  CB   . CYS   A 181 ? 0.49253 0.45851 0.43682 -0.05731 -0.00780 0.04759  333 CYS   A CB   
1233 S  SG   . CYS   A 181 ? 0.47495 0.44548 0.41325 -0.06064 -0.00344 0.04848  333 CYS   A SG   
1234 N  N    . ILE   A 182 ? 0.45570 0.40658 0.41509 -0.05192 -0.00633 0.04760  334 ILE   A N    
1235 C  CA   . ILE   A 182 ? 0.47294 0.41696 0.43354 -0.05163 -0.00492 0.04499  334 ILE   A CA   
1236 C  C    . ILE   A 182 ? 0.48525 0.42009 0.45319 -0.04798 -0.00877 0.04531  334 ILE   A C    
1237 O  O    . ILE   A 182 ? 0.45728 0.38154 0.42557 -0.05027 -0.01110 0.04647  334 ILE   A O    
1238 C  CB   . ILE   A 182 ? 0.47736 0.42458 0.43654 -0.05062 -0.00092 0.03916  334 ILE   A CB   
1239 C  CG1  . ILE   A 182 ? 0.47285 0.42283 0.42625 -0.05302 0.00002  0.03975  334 ILE   A CG1  
1240 C  CG2  . ILE   A 182 ? 0.47279 0.41491 0.43138 -0.04987 -0.00057 0.03425  334 ILE   A CG2  
1241 C  CD1  . ILE   A 182 ? 0.47351 0.42393 0.42340 -0.05334 0.00190  0.03848  334 ILE   A CD1  
1242 N  N    A VAL   A 183 ? 0.47380 0.41235 0.45020 -0.04207 -0.01038 0.04353  335 VAL   A N    
1243 N  N    B VAL   A 183 ? 0.46795 0.40649 0.44425 -0.04216 -0.01051 0.04379  335 VAL   A N    
1244 C  CA   A VAL   A 183 ? 0.46169 0.39106 0.44897 -0.03507 -0.01509 0.04123  335 VAL   A CA   
1245 C  CA   B VAL   A 183 ? 0.47050 0.40039 0.45791 -0.03499 -0.01502 0.04118  335 VAL   A CA   
1246 C  C    A VAL   A 183 ? 0.45927 0.38046 0.44798 -0.03460 -0.02420 0.05241  335 VAL   A C    
1247 C  C    B VAL   A 183 ? 0.47712 0.39826 0.46610 -0.03442 -0.02425 0.05229  335 VAL   A C    
1248 O  O    A VAL   A 183 ? 0.53748 0.46227 0.53669 -0.02735 -0.02981 0.05338  335 VAL   A O    
1249 O  O    B VAL   A 183 ? 0.52575 0.44983 0.52543 -0.02702 -0.03007 0.05330  335 VAL   A O    
1250 C  CB   A VAL   A 183 ? 0.51044 0.45273 0.50989 -0.02724 -0.01168 0.03151  335 VAL   A CB   
1251 C  CB   B VAL   A 183 ? 0.50476 0.44863 0.50382 -0.02767 -0.01125 0.03172  335 VAL   A CB   
1252 C  CG1  A VAL   A 183 ? 0.49066 0.43902 0.48424 -0.02904 -0.00316 0.02221  335 VAL   A CG1  
1253 C  CG1  B VAL   A 183 ? 0.53473 0.49437 0.53890 -0.02805 -0.01233 0.03543  335 VAL   A CG1  
1254 C  CG2  A VAL   A 183 ? 0.56774 0.52700 0.57128 -0.02821 -0.01143 0.03456  335 VAL   A CG2  
1255 C  CG2  B VAL   A 183 ? 0.47522 0.41184 0.48864 -0.01714 -0.01493 0.02388  335 VAL   A CG2  
1256 N  N    . SER   A 184 ? 0.48127 0.39373 0.45965 -0.04278 -0.02609 0.06166  336 SER   A N    
1257 C  CA   . SER   A 184 ? 0.52193 0.42522 0.49713 -0.04478 -0.03504 0.07546  336 SER   A CA   
1258 C  C    . SER   A 184 ? 0.49929 0.37772 0.48077 -0.04441 -0.04196 0.07930  336 SER   A C    
1259 O  O    . SER   A 184 ? 0.55233 0.42286 0.53155 -0.05148 -0.03868 0.07706  336 SER   A O    
1260 C  CB   . SER   A 184 ? 0.53715 0.44915 0.49575 -0.05594 -0.03211 0.08451  336 SER   A CB   
1261 O  OG   . SER   A 184 ? 0.60389 0.53451 0.55788 -0.05606 -0.02551 0.07705  336 SER   A OG   
1262 N  N    . PRO   A 185 ? 0.52621 0.39084 0.51731 -0.03618 -0.05304 0.08463  337 PRO   A N    
1263 C  CA   . PRO   A 185 ? 0.48809 0.32295 0.48800 -0.03429 -0.06155 0.08643  337 PRO   A CA   
1264 C  C    . PRO   A 185 ? 0.56192 0.37931 0.54975 -0.04952 -0.06610 0.10462  337 PRO   A C    
1265 O  O    . PRO   A 185 ? 0.62057 0.41102 0.61494 -0.05230 -0.07218 0.10565  337 PRO   A O    
1266 C  CB   . PRO   A 185 ? 0.53524 0.36242 0.55099 -0.01883 -0.07362 0.08749  337 PRO   A CB   
1267 C  CG   . PRO   A 185 ? 0.54238 0.39244 0.55067 -0.01924 -0.07464 0.09599  337 PRO   A CG   
1268 C  CD   . PRO   A 185 ? 0.47316 0.34849 0.47050 -0.02706 -0.05984 0.08767  337 PRO   A CD   
1269 N  N    . ASP   A 186 ? 0.61117 0.44363 0.58179 -0.06039 -0.06316 0.11814  338 ASP   A N    
1270 C  CA   . ASP   A 186 ? 0.63836 0.45995 0.59615 -0.07692 -0.06596 0.13742  338 ASP   A CA   
1271 C  C    . ASP   A 186 ? 0.59432 0.42638 0.54821 -0.09090 -0.05449 0.13311  338 ASP   A C    
1272 O  O    . ASP   A 186 ? 0.69294 0.52416 0.63709 -0.10727 -0.05368 0.14829  338 ASP   A O    
1273 C  CB   . ASP   A 186 ? 0.56326 0.40056 0.50215 -0.08230 -0.06787 0.15343  338 ASP   A CB   
1274 C  CG   . ASP   A 186 ? 0.64030 0.51187 0.56929 -0.08403 -0.05482 0.14304  338 ASP   A CG   
1275 O  OD1  . ASP   A 186 ? 0.85564 0.74359 0.76618 -0.09551 -0.05029 0.15255  338 ASP   A OD1  
1276 O  OD2  . ASP   A 186 ? 0.69807 0.57987 0.63754 -0.07411 -0.04914 0.12502  338 ASP   A OD2  
1277 N  N    . ARG   A 187 ? 0.53793 0.38208 0.49936 -0.08551 -0.04607 0.11388  339 ARG   A N    
1278 C  CA   . ARG   A 187 ? 0.51221 0.36844 0.47288 -0.09689 -0.03744 0.10912  339 ARG   A CA   
1279 C  C    . ARG   A 187 ? 0.57459 0.40585 0.54315 -0.10735 -0.04369 0.11349  339 ARG   A C    
1280 O  O    . ARG   A 187 ? 0.64835 0.45185 0.62691 -0.09990 -0.05298 0.10915  339 ARG   A O    
1281 C  CB   . ARG   A 187 ? 0.46311 0.33415 0.42903 -0.08791 -0.03028 0.08946  339 ARG   A CB   
1282 C  CG   . ARG   A 187 ? 0.45537 0.34654 0.41580 -0.07895 -0.02518 0.08457  339 ARG   A CG   
1283 C  CD   . ARG   A 187 ? 0.53315 0.44795 0.48373 -0.08629 -0.01763 0.08782  339 ARG   A CD   
1284 N  NE   . ARG   A 187 ? 0.45546 0.38545 0.40302 -0.07799 -0.01353 0.07938  339 ARG   A NE   
1285 C  CZ   . ARG   A 187 ? 0.49045 0.43926 0.42997 -0.08029 -0.00827 0.07861  339 ARG   A CZ   
1286 N  NH1  . ARG   A 187 ? 0.45606 0.41631 0.38920 -0.09032 -0.00457 0.08540  339 ARG   A NH1  
1287 N  NH2  . ARG   A 187 ? 0.44445 0.40127 0.38288 -0.07320 -0.00651 0.07027  339 ARG   A NH2  
1288 N  N    . PRO   A 188 ? 0.75540 0.59667 0.72179 -0.12473 -0.03901 0.12062  340 PRO   A N    
1289 C  CA   . PRO   A 188 ? 0.76418 0.58122 0.73950 -0.13832 -0.04578 0.12572  340 PRO   A CA   
1290 C  C    . PRO   A 188 ? 0.63886 0.44566 0.62720 -0.13148 -0.04825 0.10441  340 PRO   A C    
1291 O  O    . PRO   A 188 ? 0.68826 0.51887 0.67744 -0.12649 -0.04083 0.08967  340 PRO   A O    
1292 C  CB   . PRO   A 188 ? 0.74136 0.58480 0.71313 -0.15866 -0.03687 0.13561  340 PRO   A CB   
1293 C  CG   . PRO   A 188 ? 0.82255 0.70428 0.78944 -0.15003 -0.02497 0.12435  340 PRO   A CG   
1294 C  CD   . PRO   A 188 ? 0.77881 0.65594 0.73703 -0.13286 -0.02726 0.12271  340 PRO   A CD   
1295 N  N    . GLY   A 189 ? 0.62717 0.39719 0.62467 -0.13092 -0.05984 0.10264  341 GLY   A N    
1296 C  CA   . GLY   A 189 ? 0.54628 0.30435 0.55414 -0.12555 -0.06341 0.08083  341 GLY   A CA   
1297 C  C    . GLY   A 189 ? 0.66108 0.41136 0.67186 -0.10282 -0.06533 0.06309  341 GLY   A C    
1298 O  O    . GLY   A 189 ? 0.61821 0.35996 0.63493 -0.09745 -0.06779 0.04292  341 GLY   A O    
1299 N  N    . VAL   A 190 ? 0.69307 0.44937 0.70010 -0.09001 -0.06405 0.06886  342 VAL   A N    
1300 C  CA   . VAL   A 190 ? 0.70253 0.45797 0.71563 -0.06924 -0.06445 0.05204  342 VAL   A CA   
1301 C  C    . VAL   A 190 ? 0.64402 0.36077 0.67132 -0.06148 -0.07757 0.04532  342 VAL   A C    
1302 O  O    . VAL   A 190 ? 0.71819 0.40657 0.74921 -0.06680 -0.08874 0.06242  342 VAL   A O    
1303 C  CB   . VAL   A 190 ? 0.60808 0.38192 0.61695 -0.05949 -0.06114 0.06058  342 VAL   A CB   
1304 C  CG1  . VAL   A 190 ? 0.56597 0.34084 0.58607 -0.03914 -0.06212 0.04444  342 VAL   A CG1  
1305 C  CG2  . VAL   A 190 ? 0.55887 0.36765 0.55541 -0.06490 -0.04879 0.06203  342 VAL   A CG2  
1306 N  N    . GLN   A 191 ? 0.68419 0.39893 0.71873 -0.04893 -0.07676 0.02015  343 GLN   A N    
1307 C  CA   . GLN   A 191 ? 0.81000 0.48963 0.86055 -0.03696 -0.08875 0.00739  343 GLN   A CA   
1308 C  C    . GLN   A 191 ? 0.63070 0.31477 0.69269 -0.01472 -0.09059 0.00332  343 GLN   A C    
1309 O  O    . GLN   A 191 ? 0.76850 0.42373 0.84274 -0.00741 -0.10413 0.01289  343 GLN   A O    
1310 C  CB   . GLN   A 191 ? 0.87110 0.54886 0.92324 -0.03434 -0.08686 -0.02143 343 GLN   A CB   
1311 C  CG   . GLN   A 191 ? 1.02038 0.68005 1.07017 -0.05469 -0.09253 -0.02053 343 GLN   A CG   
1312 C  CD   . GLN   A 191 ? 1.15716 0.76818 1.21954 -0.06183 -0.10909 -0.00912 343 GLN   A CD   
1313 O  OE1  . GLN   A 191 ? 1.23350 0.81685 1.30899 -0.04616 -0.11898 -0.01198 343 GLN   A OE1  
1314 N  NE2  . GLN   A 191 ? 1.21577 0.81642 1.27590 -0.08587 -0.11287 0.00444  343 GLN   A NE2  
1315 N  N    . ASP   A 192 ? 0.56409 0.28483 0.62339 -0.00445 -0.07794 -0.00976 344 ASP   A N    
1316 C  CA   . ASP   A 192 ? 0.69385 0.42725 0.76773 0.01606  -0.07793 -0.01702 344 ASP   A CA   
1317 C  C    . ASP   A 192 ? 0.58834 0.34425 0.65630 0.01324  -0.07533 0.00443  344 ASP   A C    
1318 O  O    . ASP   A 192 ? 0.54788 0.33877 0.61304 0.01675  -0.06416 -0.00022 344 ASP   A O    
1319 C  CB   . ASP   A 192 ? 0.76264 0.52481 0.83808 0.02693  -0.06516 -0.04452 344 ASP   A CB   
1320 C  CG   . ASP   A 192 ? 0.90671 0.64918 0.98485 0.02985  -0.06784 -0.06887 344 ASP   A CG   
1321 O  OD1  . ASP   A 192 ? 1.07660 0.77847 1.16160 0.02637  -0.08171 -0.06587 344 ASP   A OD1  
1322 O  OD2  . ASP   A 192 ? 0.91267 0.67970 0.98474 0.03430  -0.05657 -0.09073 344 ASP   A OD2  
1323 N  N    . ALA   A 193 ? 0.63631 0.37059 0.70135 0.00549  -0.08662 0.02855  345 ALA   A N    
1324 C  CA   . ALA   A 193 ? 0.63851 0.39233 0.69489 0.00175  -0.08604 0.04852  345 ALA   A CA   
1325 C  C    . ALA   A 193 ? 0.61669 0.39012 0.68947 0.02066  -0.08788 0.04184  345 ALA   A C    
1326 O  O    . ALA   A 193 ? 0.57450 0.37824 0.64115 0.01873  -0.08140 0.04694  345 ALA   A O    
1327 C  CB   . ALA   A 193 ? 0.66423 0.39070 0.71284 -0.00956 -0.09903 0.07554  345 ALA   A CB   
1328 N  N    . LYS   A 194 ? 0.60196 0.35978 0.69794 0.03923  -0.09705 0.02890  346 LYS   A N    
1329 C  CA   . LYS   A 194 ? 0.58172 0.36375 0.69864 0.05814  -0.09879 0.02086  346 LYS   A CA   
1330 C  C    . LYS   A 194 ? 0.61247 0.43673 0.73099 0.06060  -0.07991 0.00039  346 LYS   A C    
1331 O  O    . LYS   A 194 ? 0.60245 0.45965 0.72792 0.06443  -0.07575 0.00119  346 LYS   A O    
1332 C  CB   . LYS   A 194 ? 0.66150 0.41701 0.80645 0.07968  -0.11385 0.01012  346 LYS   A CB   
1333 C  CG   . LYS   A 194 ? 0.76968 0.49033 0.91764 0.08136  -0.13615 0.03558  346 LYS   A CG   
1334 C  CD   . LYS   A 194 ? 0.83351 0.51914 1.01023 0.10320  -0.15321 0.02438  346 LYS   A CD   
1335 C  CE   . LYS   A 194 ? 1.03039 0.68273 1.21046 0.10633  -0.17779 0.05313  346 LYS   A CE   
1336 N  NZ   . LYS   A 194 ? 1.13657 0.74312 1.29718 0.08693  -0.18565 0.07227  346 LYS   A NZ   
1337 N  N    . LEU   A 195 ? 0.64441 0.46858 0.75578 0.05697  -0.06912 -0.01719 347 LEU   A N    
1338 C  CA   . LEU   A 195 ? 0.60712 0.47004 0.71340 0.05525  -0.05102 -0.03214 347 LEU   A CA   
1339 C  C    . LEU   A 195 ? 0.54702 0.42920 0.63237 0.03804  -0.04306 -0.01562 347 LEU   A C    
1340 O  O    . LEU   A 195 ? 0.53949 0.45473 0.62665 0.03763  -0.03344 -0.01835 347 LEU   A O    
1341 C  CB   . LEU   A 195 ? 0.58373 0.44052 0.68146 0.05345  -0.04341 -0.05225 347 LEU   A CB   
1342 C  CG   . LEU   A 195 ? 0.69608 0.56434 0.81287 0.07209  -0.03915 -0.08128 347 LEU   A CG   
1343 C  CD1  . LEU   A 195 ? 0.81364 0.66432 0.96058 0.09228  -0.05408 -0.08443 347 LEU   A CD1  
1344 C  CD2  . LEU   A 195 ? 0.78885 0.64138 0.89354 0.06890  -0.03645 -0.09995 347 LEU   A CD2  
1345 N  N    . VAL   A 196 ? 0.46035 0.32276 0.52715 0.02334  -0.04681 0.00065  348 VAL   A N    
1346 C  CA   . VAL   A 196 ? 0.46251 0.34115 0.51129 0.00917  -0.04050 0.01437  348 VAL   A CA   
1347 C  C    . VAL   A 196 ? 0.50591 0.39888 0.56093 0.01220  -0.04552 0.02574  348 VAL   A C    
1348 O  O    . VAL   A 196 ? 0.47566 0.39405 0.52665 0.00775  -0.03799 0.02616  348 VAL   A O    
1349 C  CB   . VAL   A 196 ? 0.49200 0.35010 0.52378 -0.00561 -0.04354 0.02761  348 VAL   A CB   
1350 C  CG1  . VAL   A 196 ? 0.39868 0.27426 0.41440 -0.01743 -0.03751 0.03914  348 VAL   A CG1  
1351 C  CG2  . VAL   A 196 ? 0.48192 0.33005 0.50884 -0.00973 -0.03959 0.01498  348 VAL   A CG2  
1352 N  N    . GLU   A 197 ? 0.47546 0.35106 0.54037 0.01937  -0.05996 0.03547  349 GLU   A N    
1353 C  CA   . GLU   A 197 ? 0.55213 0.44275 0.62308 0.02310  -0.06748 0.04582  349 GLU   A CA   
1354 C  C    . GLU   A 197 ? 0.59854 0.52029 0.69228 0.03529  -0.06292 0.03078  349 GLU   A C    
1355 O  O    . GLU   A 197 ? 0.60302 0.54924 0.69907 0.03287  -0.06293 0.03501  349 GLU   A O    
1356 C  CB   . GLU   A 197 ? 0.58199 0.44589 0.65820 0.02914  -0.08628 0.06099  349 GLU   A CB   
1357 C  CG   . GLU   A 197 ? 0.69615 0.57466 0.77214 0.03035  -0.09668 0.07515  349 GLU   A CG   
1358 C  CD   . GLU   A 197 ? 0.86582 0.71521 0.93411 0.02945  -0.11504 0.09750  349 GLU   A CD   
1359 O  OE1  . GLU   A 197 ? 0.89232 0.71596 0.97795 0.04225  -0.12761 0.09758  349 GLU   A OE1  
1360 O  OE2  . GLU   A 197 ? 0.93743 0.78914 0.98165 0.01581  -0.11714 0.11488  349 GLU   A OE2  
1361 N  N    . ALA   A 198 ? 0.66604 0.58976 0.77735 0.04759  -0.05869 0.01199  350 ALA   A N    
1362 C  CA   . ALA   A 198 ? 0.65958 0.62011 0.79296 0.05723  -0.05070 -0.00378 350 ALA   A CA   
1363 C  C    . ALA   A 198 ? 0.64149 0.63003 0.76099 0.04225  -0.03537 -0.00405 350 ALA   A C    
1364 O  O    . ALA   A 198 ? 0.61696 0.63431 0.74737 0.04081  -0.03385 -0.00284 350 ALA   A O    
1365 C  CB   . ALA   A 198 ? 0.71725 0.67738 0.86705 0.07154  -0.04561 -0.02677 350 ALA   A CB   
1366 N  N    . ILE   A 199 ? 0.55267 0.53177 0.64897 0.03045  -0.02559 -0.00488 351 ILE   A N    
1367 C  CA   . ILE   A 199 ? 0.44754 0.44682 0.52971 0.01653  -0.01336 -0.00304 351 ILE   A CA   
1368 C  C    . ILE   A 199 ? 0.46562 0.46694 0.54020 0.00719  -0.01918 0.01239  351 ILE   A C    
1369 O  O    . ILE   A 199 ? 0.42772 0.45282 0.50754 0.00168  -0.01498 0.01257  351 ILE   A O    
1370 C  CB   . ILE   A 199 ? 0.50850 0.49408 0.56733 0.00729  -0.00569 -0.00492 351 ILE   A CB   
1371 C  CG1  . ILE   A 199 ? 0.50611 0.49278 0.57010 0.01599  0.00002  -0.02319 351 ILE   A CG1  
1372 C  CG2  . ILE   A 199 ? 0.49859 0.49978 0.54293 -0.00623 0.00386  -0.00015 351 ILE   A CG2  
1373 C  CD1  . ILE   A 199 ? 0.54065 0.51097 0.58285 0.00830  0.00319  -0.02559 351 ILE   A CD1  
1374 N  N    . GLN   A 200 ? 0.49572 0.47308 0.55761 0.00422  -0.02891 0.02491  352 GLN   A N    
1375 C  CA   . GLN   A 200 ? 0.46464 0.44464 0.51467 -0.00498 -0.03354 0.03719  352 GLN   A CA   
1376 C  C    . GLN   A 200 ? 0.42950 0.42933 0.49686 0.00027  -0.04184 0.03872  352 GLN   A C    
1377 O  O    . GLN   A 200 ? 0.55677 0.57164 0.62031 -0.00801 -0.04125 0.04090  352 GLN   A O    
1378 C  CB   . GLN   A 200 ? 0.39723 0.35254 0.43044 -0.00923 -0.04136 0.05010  352 GLN   A CB   
1379 C  CG   . GLN   A 200 ? 0.47030 0.42998 0.48453 -0.02072 -0.04112 0.05858  352 GLN   A CG   
1380 C  CD   . GLN   A 200 ? 0.49993 0.44288 0.49832 -0.02560 -0.04834 0.07239  352 GLN   A CD   
1381 O  OE1  . GLN   A 200 ? 0.50837 0.44026 0.51133 -0.02024 -0.05977 0.08129  352 GLN   A OE1  
1382 N  NE2  . GLN   A 200 ? 0.53119 0.47316 0.51152 -0.03594 -0.04192 0.07485  352 GLN   A NE2  
1383 N  N    . ASP   A 201 ? 0.46457 0.46399 0.55258 0.01443  -0.05132 0.03694  353 ASP   A N    
1384 C  CA   . ASP   A 201 ? 0.46618 0.48782 0.57449 0.02101  -0.06144 0.03809  353 ASP   A CA   
1385 C  C    . ASP   A 201 ? 0.51253 0.56979 0.63751 0.01748  -0.05071 0.02658  353 ASP   A C    
1386 O  O    . ASP   A 201 ? 0.46175 0.54019 0.59471 0.01306  -0.05605 0.02895  353 ASP   A O    
1387 C  CB   . ASP   A 201 ? 0.50848 0.52261 0.64017 0.03986  -0.07427 0.03672  353 ASP   A CB   
1388 C  CG   . ASP   A 201 ? 0.55635 0.53621 0.67257 0.04078  -0.08954 0.05397  353 ASP   A CG   
1389 O  OD1  . ASP   A 201 ? 0.68411 0.65326 0.77196 0.02638  -0.08909 0.06637  353 ASP   A OD1  
1390 O  OD2  . ASP   A 201 ? 0.68807 0.65186 0.82089 0.05573  -0.10196 0.05511  353 ASP   A OD2  
1391 N  N    . ARG   A 202 ? 0.48062 0.54601 0.61013 0.01775  -0.03585 0.01441  354 ARG   A N    
1392 C  CA   . ARG   A 202 ? 0.57261 0.67234 0.71487 0.01061  -0.02382 0.00616  354 ARG   A CA   
1393 C  C    . ARG   A 202 ? 0.54785 0.64525 0.66906 -0.00836 -0.01956 0.01395  354 ARG   A C    
1394 O  O    . ARG   A 202 ? 0.49977 0.62104 0.63222 -0.01697 -0.01860 0.01351  354 ARG   A O    
1395 C  CB   . ARG   A 202 ? 0.62900 0.73846 0.77517 0.01394  -0.00830 -0.00754 354 ARG   A CB   
1396 C  CG   . ARG   A 202 ? 0.84904 0.97731 1.02638 0.03318  -0.00847 -0.02275 354 ARG   A CG   
1397 C  CD   . ARG   A 202 ? 1.00132 1.10244 1.18647 0.04967  -0.02630 -0.01940 354 ARG   A CD   
1398 N  NE   . ARG   A 202 ? 1.13848 1.24578 1.35071 0.07069  -0.02756 -0.03611 354 ARG   A NE   
1399 C  CZ   . ARG   A 202 ? 1.22806 1.32995 1.43677 0.07610  -0.01689 -0.05168 354 ARG   A CZ   
1400 N  NH1  . ARG   A 202 ? 1.18498 1.27665 1.36376 0.06148  -0.00471 -0.05089 354 ARG   A NH1  
1401 N  NH2  . ARG   A 202 ? 1.26769 1.37497 1.50369 0.09735  -0.01958 -0.06948 354 ARG   A NH2  
1402 N  N    . LEU   A 203 ? 0.51617 0.58527 0.60924 -0.01494 -0.01761 0.02008  355 LEU   A N    
1403 C  CA   . LEU   A 203 ? 0.47884 0.54189 0.55347 -0.02975 -0.01584 0.02606  355 LEU   A CA   
1404 C  C    . LEU   A 203 ? 0.46004 0.52398 0.53351 -0.03206 -0.02883 0.03211  355 LEU   A C    
1405 O  O    . LEU   A 203 ? 0.45625 0.52881 0.52874 -0.04280 -0.02936 0.03196  355 LEU   A O    
1406 C  CB   . LEU   A 203 ? 0.40044 0.43682 0.44950 -0.03341 -0.01170 0.02958  355 LEU   A CB   
1407 C  CG   . LEU   A 203 ? 0.42842 0.46181 0.47336 -0.03174 -0.00106 0.02366  355 LEU   A CG   
1408 C  CD1  . LEU   A 203 ? 0.43895 0.44791 0.46203 -0.03456 -0.00077 0.02763  355 LEU   A CD1  
1409 C  CD2  . LEU   A 203 ? 0.38173 0.43328 0.42876 -0.04096 0.00959  0.02090  355 LEU   A CD2  
1410 N  N    . SER   A 204 ? 0.39092 0.44489 0.46316 -0.02290 -0.04033 0.03768  356 SER   A N    
1411 C  CA   . SER   A 204 ? 0.53028 0.58746 0.59774 -0.02491 -0.05388 0.04415  356 SER   A CA   
1412 C  C    . SER   A 204 ? 0.49357 0.58125 0.58610 -0.02520 -0.05958 0.03927  356 SER   A C    
1413 O  O    . SER   A 204 ? 0.51296 0.60931 0.60096 -0.03513 -0.06436 0.03884  356 SER   A O    
1414 C  CB   . SER   A 204 ? 0.60282 0.64402 0.66463 -0.01532 -0.06601 0.05400  356 SER   A CB   
1415 O  OG   . SER   A 204 ? 0.86598 0.88542 0.89913 -0.02200 -0.06484 0.06179  356 SER   A OG   
1416 N  N    A ASN   A 205 ? 0.44299 0.54909 0.56419 -0.01418 -0.05946 0.03378  357 ASN   A N    
1417 N  N    B ASN   A 205 ? 0.44635 0.55252 0.56754 -0.01425 -0.05939 0.03374  357 ASN   A N    
1418 C  CA   A ASN   A 205 ? 0.47739 0.61911 0.62832 -0.01414 -0.06444 0.02824  357 ASN   A CA   
1419 C  CA   B ASN   A 205 ? 0.47686 0.61856 0.62763 -0.01426 -0.06454 0.02830  357 ASN   A CA   
1420 C  C    A ASN   A 205 ? 0.45613 0.61419 0.61020 -0.03124 -0.05251 0.02267  357 ASN   A C    
1421 C  C    B ASN   A 205 ? 0.45468 0.61300 0.60900 -0.03122 -0.05249 0.02261  357 ASN   A C    
1422 O  O    A ASN   A 205 ? 0.42934 0.60811 0.59542 -0.04019 -0.05903 0.02108  357 ASN   A O    
1423 O  O    B ASN   A 205 ? 0.43442 0.61395 0.60127 -0.04010 -0.05888 0.02092  357 ASN   A O    
1424 C  CB   A ASN   A 205 ? 0.50907 0.67011 0.69291 0.00296  -0.06434 0.02078  357 ASN   A CB   
1425 C  CB   B ASN   A 205 ? 0.51090 0.67186 0.69467 0.00303  -0.06505 0.02110  357 ASN   A CB   
1426 C  CG   A ASN   A 205 ? 0.56792 0.70849 0.75200 0.02033  -0.07953 0.02752  357 ASN   A CG   
1427 C  CG   B ASN   A 205 ? 0.56718 0.72120 0.75932 0.01927  -0.08514 0.02797  357 ASN   A CG   
1428 O  OD1  A ASN   A 205 ? 0.57231 0.69791 0.73934 0.01907  -0.09428 0.03952  357 ASN   A OD1  
1429 O  OD1  B ASN   A 205 ? 0.61269 0.73410 0.78744 0.02630  -0.09016 0.03572  357 ASN   A OD1  
1430 N  ND2  A ASN   A 205 ? 0.59686 0.73574 0.79915 0.03617  -0.07636 0.01980  357 ASN   A ND2  
1431 N  ND2  B ASN   A 205 ? 0.55743 0.74205 0.77687 0.02438  -0.09807 0.02642  357 ASN   A ND2  
1432 N  N    . THR   A 206 ? 0.39703 0.54499 0.54009 -0.03693 -0.03638 0.02048  358 THR   A N    
1433 C  CA   . THR   A 206 ? 0.40052 0.55714 0.54246 -0.05471 -0.02613 0.01899  358 THR   A CA   
1434 C  C    . THR   A 206 ? 0.45425 0.59305 0.57675 -0.06708 -0.03385 0.02295  358 THR   A C    
1435 O  O    . THR   A 206 ? 0.49650 0.64834 0.62859 -0.08097 -0.03529 0.02105  358 THR   A O    
1436 C  CB   . THR   A 206 ? 0.38880 0.53285 0.51601 -0.05755 -0.01018 0.01869  358 THR   A CB   
1437 O  OG1  . THR   A 206 ? 0.42712 0.59067 0.57207 -0.04603 -0.00229 0.01126  358 THR   A OG1  
1438 C  CG2  . THR   A 206 ? 0.37281 0.52130 0.49643 -0.07689 -0.00135 0.02095  358 THR   A CG2  
1439 N  N    . LEU   A 207 ? 0.35548 0.46565 0.45173 -0.06273 -0.03880 0.02724  359 LEU   A N    
1440 C  CA   . LEU   A 207 ? 0.47026 0.56545 0.54743 -0.07204 -0.04535 0.02754  359 LEU   A CA   
1441 C  C    . LEU   A 207 ? 0.52568 0.63886 0.61268 -0.07374 -0.06052 0.02543  359 LEU   A C    
1442 O  O    . LEU   A 207 ? 0.46902 0.58526 0.55656 -0.08619 -0.06477 0.02059  359 LEU   A O    
1443 C  CB   . LEU   A 207 ? 0.43169 0.49981 0.48083 -0.06645 -0.04546 0.03159  359 LEU   A CB   
1444 C  CG   . LEU   A 207 ? 0.40085 0.45582 0.42896 -0.07329 -0.05069 0.02892  359 LEU   A CG   
1445 C  CD1  . LEU   A 207 ? 0.34361 0.39122 0.37274 -0.08532 -0.04583 0.02342  359 LEU   A CD1  
1446 C  CD2  . LEU   A 207 ? 0.38736 0.42300 0.39154 -0.06785 -0.04798 0.03271  359 LEU   A CD2  
1447 N  N    . GLN   A 208 ? 0.49530 0.61887 0.59002 -0.06135 -0.07061 0.02903  360 GLN   A N    
1448 C  CA   . GLN   A 208 ? 0.53925 0.68254 0.64310 -0.06178 -0.08758 0.02819  360 GLN   A CA   
1449 C  C    . GLN   A 208 ? 0.50615 0.68021 0.64118 -0.07161 -0.08797 0.02082  360 GLN   A C    
1450 O  O    . GLN   A 208 ? 0.51102 0.69312 0.64624 -0.08315 -0.09724 0.01598  360 GLN   A O    
1451 C  CB   . GLN   A 208 ? 0.56614 0.71510 0.67754 -0.04517 -0.09933 0.03552  360 GLN   A CB   
1452 C  CG   . GLN   A 208 ? 0.72802 0.84817 0.80804 -0.03916 -0.10217 0.04556  360 GLN   A CG   
1453 C  CD   . GLN   A 208 ? 0.84188 0.96040 0.93197 -0.02289 -0.11293 0.05482  360 GLN   A CD   
1454 O  OE1  . GLN   A 208 ? 0.89604 0.98964 0.97033 -0.01736 -0.11063 0.06298  360 GLN   A OE1  
1455 N  NE2  . GLN   A 208 ? 0.87540 1.02012 0.99414 -0.01519 -0.12594 0.05356  360 GLN   A NE2  
1456 N  N    . THR   A 209 ? 0.51782 0.71112 0.67964 -0.06834 -0.07744 0.01879  361 THR   A N    
1457 C  CA   . THR   A 209 ? 0.44735 0.67605 0.64196 -0.07941 -0.07569 0.01264  361 THR   A CA   
1458 C  C    . THR   A 209 ? 0.51563 0.73282 0.70073 -0.10130 -0.06818 0.01080  361 THR   A C    
1459 O  O    . THR   A 209 ? 0.44675 0.68407 0.65010 -0.11599 -0.07393 0.00647  361 THR   A O    
1460 C  CB   . THR   A 209 ? 0.43109 0.68589 0.65429 -0.07073 -0.06315 0.00964  361 THR   A CB   
1461 O  OG1  . THR   A 209 ? 0.49862 0.75677 0.73104 -0.04827 -0.07211 0.01056  361 THR   A OG1  
1462 C  CG2  . THR   A 209 ? 0.36689 0.66733 0.62849 -0.08232 -0.06123 0.00344  361 THR   A CG2  
1463 N  N    . TYR   A 210 ? 0.40845 0.59228 0.56658 -0.10398 -0.05700 0.01423  362 TYR   A N    
1464 C  CA   . TYR   A 210 ? 0.37134 0.53725 0.51937 -0.12285 -0.05287 0.01369  362 TYR   A CA   
1465 C  C    . TYR   A 210 ? 0.39386 0.54792 0.53057 -0.12988 -0.06825 0.00797  362 TYR   A C    
1466 O  O    . TYR   A 210 ? 0.48970 0.64480 0.63535 -0.14742 -0.07181 0.00379  362 TYR   A O    
1467 C  CB   . TYR   A 210 ? 0.41537 0.54722 0.53672 -0.12115 -0.04112 0.01862  362 TYR   A CB   
1468 C  CG   . TYR   A 210 ? 0.48263 0.59149 0.59467 -0.13860 -0.03946 0.01923  362 TYR   A CG   
1469 C  CD1  . TYR   A 210 ? 0.45467 0.53470 0.54651 -0.13995 -0.04843 0.01442  362 TYR   A CD1  
1470 C  CD2  . TYR   A 210 ? 0.47712 0.59347 0.60111 -0.15396 -0.02945 0.02444  362 TYR   A CD2  
1471 C  CE1  . TYR   A 210 ? 0.45610 0.51114 0.54231 -0.15397 -0.04911 0.01368  362 TYR   A CE1  
1472 C  CE2  . TYR   A 210 ? 0.48649 0.57666 0.60242 -0.17041 -0.03030 0.02736  362 TYR   A CE2  
1473 C  CZ   . TYR   A 210 ? 0.49244 0.55001 0.59083 -0.16933 -0.04103 0.02140  362 TYR   A CZ   
1474 O  OH   . TYR   A 210 ? 0.53762 0.56500 0.63047 -0.18372 -0.04382 0.02309  362 TYR   A OH   
1475 N  N    . ILE   A 211 ? 0.42829 0.57049 0.54394 -0.11761 -0.07742 0.00737  363 ILE   A N    
1476 C  CA   . ILE   A 211 ? 0.45293 0.58621 0.55312 -0.12335 -0.09121 -0.00033 363 ILE   A CA   
1477 C  C    . ILE   A 211 ? 0.50565 0.67124 0.63054 -0.13113 -0.10566 -0.00593 363 ILE   A C    
1478 O  O    . ILE   A 211 ? 0.50750 0.67032 0.63347 -0.14586 -0.11376 -0.01509 363 ILE   A O    
1479 C  CB   . ILE   A 211 ? 0.47497 0.59434 0.54533 -0.10961 -0.09603 0.00199  363 ILE   A CB   
1480 C  CG1  . ILE   A 211 ? 0.52015 0.60950 0.56868 -0.10479 -0.08236 0.00537  363 ILE   A CG1  
1481 C  CG2  . ILE   A 211 ? 0.42753 0.54563 0.48050 -0.11488 -0.11043 -0.00770 363 ILE   A CG2  
1482 C  CD1  . ILE   A 211 ? 0.46585 0.54523 0.48816 -0.09320 -0.08397 0.00978  363 ILE   A CD1  
1483 N  N    . ARG   A 212 ? 0.50239 0.69911 0.64990 -0.12111 -0.11027 -0.00164 364 ARG   A N    
1484 C  CA   . ARG   A 212 ? 0.60237 0.83541 0.77788 -0.12706 -0.12548 -0.00688 364 ARG   A CA   
1485 C  C    . ARG   A 212 ? 0.64585 0.89517 0.85008 -0.14790 -0.11976 -0.01185 364 ARG   A C    
1486 O  O    . ARG   A 212 ? 0.65178 0.91256 0.86623 -0.16277 -0.13248 -0.02010 364 ARG   A O    
1487 C  CB   . ARG   A 212 ? 0.68684 0.95056 0.88647 -0.10951 -0.13097 -0.00131 364 ARG   A CB   
1488 C  CG   . ARG   A 212 ? 0.72566 0.97074 0.90012 -0.08975 -0.13587 0.00752  364 ARG   A CG   
1489 C  CD   . ARG   A 212 ? 0.81404 1.08783 1.01677 -0.07232 -0.14660 0.01219  364 ARG   A CD   
1490 N  NE   . ARG   A 212 ? 0.95032 1.20282 1.12829 -0.05574 -0.15507 0.02317  364 ARG   A NE   
1491 C  CZ   . ARG   A 212 ? 1.02430 1.26850 1.20924 -0.03885 -0.14994 0.02986  364 ARG   A CZ   
1492 N  NH1  . ARG   A 212 ? 1.00791 1.26647 1.22260 -0.03465 -0.13549 0.02438  364 ARG   A NH1  
1493 N  NH2  . ARG   A 212 ? 1.08604 1.30754 1.24737 -0.02714 -0.15928 0.04173  364 ARG   A NH2  
1494 N  N    . CYS   A 213 ? 0.63082 0.88166 0.84706 -0.15084 -0.10098 -0.00664 365 CYS   A N    
1495 C  CA   . CYS   A 213 ? 0.73189 1.00658 0.97895 -0.17117 -0.09352 -0.00767 365 CYS   A CA   
1496 C  C    . CYS   A 213 ? 0.72537 0.96514 0.95658 -0.19186 -0.08735 -0.00685 365 CYS   A C    
1497 O  O    . CYS   A 213 ? 0.77624 1.02957 1.02960 -0.21432 -0.08810 -0.00836 365 CYS   A O    
1498 C  CB   . CYS   A 213 ? 0.78773 1.09025 1.05717 -0.16375 -0.07606 -0.00259 365 CYS   A CB   
1499 S  SG   . CYS   A 213 ? 0.93914 1.25900 1.22946 -0.18974 -0.05643 0.00183  365 CYS   A SG   
1500 N  N    . ARG   A 214 ? 0.66289 0.85807 0.85853 -0.18535 -0.08267 -0.00434 366 ARG   A N    
1501 C  CA   . ARG   A 214 ? 0.60492 0.76403 0.78732 -0.20165 -0.07756 -0.00234 366 ARG   A CA   
1502 C  C    . ARG   A 214 ? 0.55675 0.67594 0.71110 -0.20048 -0.08892 -0.01152 366 ARG   A C    
1503 O  O    . ARG   A 214 ? 0.64746 0.73803 0.79823 -0.21587 -0.09062 -0.01347 366 ARG   A O    
1504 C  CB   . ARG   A 214 ? 0.60216 0.74485 0.77133 -0.19666 -0.05924 0.00913  366 ARG   A CB   
1505 C  CG   . ARG   A 214 ? 0.64862 0.83054 0.84244 -0.19877 -0.04502 0.01599  366 ARG   A CG   
1506 C  CD   . ARG   A 214 ? 0.73276 0.92367 0.94426 -0.22615 -0.03818 0.02238  366 ARG   A CD   
1507 N  NE   . ARG   A 214 ? 0.87367 1.10032 1.10116 -0.22815 -0.02010 0.02929  366 ARG   A NE   
1508 C  CZ   . ARG   A 214 ? 0.92589 1.13822 1.13446 -0.22807 -0.00505 0.03922  366 ARG   A CZ   
1509 N  NH1  . ARG   A 214 ? 0.97649 1.13899 1.15244 -0.22546 -0.00710 0.04456  366 ARG   A NH1  
1510 N  NH2  . ARG   A 214 ? 0.93622 1.18667 1.15881 -0.23001 0.01170  0.04265  366 ARG   A NH2  
1511 N  N    . HIS   A 215 ? 0.52064 0.63686 0.65511 -0.18311 -0.09663 -0.01728 367 HIS   A N    
1512 C  CA   . HIS   A 215 ? 0.56033 0.64505 0.66802 -0.18149 -0.10563 -0.02879 367 HIS   A CA   
1513 C  C    . HIS   A 215 ? 0.65750 0.75721 0.77268 -0.19127 -0.12411 -0.04264 367 HIS   A C    
1514 O  O    . HIS   A 215 ? 0.70721 0.83768 0.82698 -0.18385 -0.13330 -0.04335 367 HIS   A O    
1515 C  CB   . HIS   A 215 ? 0.52214 0.59765 0.60122 -0.16060 -0.10293 -0.02759 367 HIS   A CB   
1516 C  CG   . HIS   A 215 ? 0.52705 0.56771 0.57892 -0.15746 -0.10376 -0.03765 367 HIS   A CG   
1517 N  ND1  . HIS   A 215 ? 0.50667 0.52224 0.54348 -0.14858 -0.09196 -0.03254 367 HIS   A ND1  
1518 C  CD2  . HIS   A 215 ? 0.53548 0.56458 0.57443 -0.16129 -0.11526 -0.05467 367 HIS   A CD2  
1519 C  CE1  . HIS   A 215 ? 0.53702 0.52866 0.55531 -0.14593 -0.09573 -0.04579 367 HIS   A CE1  
1520 N  NE2  . HIS   A 215 ? 0.56736 0.56597 0.58558 -0.15330 -0.10926 -0.06023 367 HIS   A NE2  
1521 N  N    . PRO   A 216 ? 0.64060 0.71844 0.75715 -0.20750 -0.13171 -0.05394 368 PRO   A N    
1522 C  CA   . PRO   A 216 ? 0.73772 0.83106 0.86331 -0.21927 -0.15055 -0.06908 368 PRO   A CA   
1523 C  C    . PRO   A 216 ? 0.70199 0.78852 0.79514 -0.20674 -0.16133 -0.08373 368 PRO   A C    
1524 O  O    . PRO   A 216 ? 0.64526 0.70228 0.71071 -0.19558 -0.15479 -0.08778 368 PRO   A O    
1525 C  CB   . PRO   A 216 ? 0.79479 0.85867 0.93211 -0.24168 -0.15359 -0.07559 368 PRO   A CB   
1526 C  CG   . PRO   A 216 ? 0.69289 0.71321 0.80965 -0.23346 -0.14110 -0.07036 368 PRO   A CG   
1527 C  CD   . PRO   A 216 ? 0.55583 0.59165 0.66712 -0.21623 -0.12509 -0.05310 368 PRO   A CD   
1528 N  N    . PRO   A 217 ? 0.71306 0.82990 0.80851 -0.20828 -0.17793 -0.09187 369 PRO   A N    
1529 C  CA   . PRO   A 217 ? 0.58709 0.69879 0.64823 -0.20044 -0.18914 -0.10765 369 PRO   A CA   
1530 C  C    . PRO   A 217 ? 0.66887 0.74619 0.72035 -0.21142 -0.19490 -0.12994 369 PRO   A C    
1531 O  O    . PRO   A 217 ? 0.79483 0.85842 0.87132 -0.22965 -0.19749 -0.13352 369 PRO   A O    
1532 C  CB   . PRO   A 217 ? 0.58590 0.74038 0.65749 -0.20347 -0.20824 -0.10968 369 PRO   A CB   
1533 C  CG   . PRO   A 217 ? 0.65892 0.83423 0.77612 -0.21983 -0.20989 -0.10427 369 PRO   A CG   
1534 C  CD   . PRO   A 217 ? 0.77443 0.93445 0.90427 -0.21745 -0.18768 -0.08764 369 PRO   A CD   
1535 N  N    . PRO   A 218 ? 0.71992 0.78224 0.73587 -0.20120 -0.19706 -0.14603 370 PRO   A N    
1536 C  CA   . PRO   A 218 ? 0.72469 0.80365 0.70716 -0.18383 -0.19528 -0.14310 370 PRO   A CA   
1537 C  C    . PRO   A 218 ? 0.69470 0.75857 0.66270 -0.16757 -0.17525 -0.12876 370 PRO   A C    
1538 O  O    . PRO   A 218 ? 0.72303 0.79877 0.66327 -0.15527 -0.17241 -0.12475 370 PRO   A O    
1539 C  CB   . PRO   A 218 ? 0.84320 0.91343 0.79679 -0.18506 -0.20605 -0.17192 370 PRO   A CB   
1540 C  CG   . PRO   A 218 ? 0.84975 0.87926 0.81635 -0.19341 -0.20377 -0.18747 370 PRO   A CG   
1541 C  CD   . PRO   A 218 ? 0.81892 0.84506 0.82629 -0.20791 -0.20208 -0.17080 370 PRO   A CD   
1542 N  N    . GLY   A 219 ? 0.62399 0.66294 0.60955 -0.16890 -0.16237 -0.12037 371 GLY   A N    
1543 C  CA   . GLY   A 219 ? 0.68766 0.71432 0.66172 -0.15437 -0.14496 -0.10732 371 GLY   A CA   
1544 C  C    . GLY   A 219 ? 0.65722 0.70871 0.63482 -0.14580 -0.13911 -0.08450 371 GLY   A C    
1545 O  O    . GLY   A 219 ? 0.66119 0.70951 0.62203 -0.13317 -0.12834 -0.07542 371 GLY   A O    
1546 N  N    . SER   A 220 ? 0.67320 0.74977 0.67490 -0.15231 -0.14656 -0.07592 372 SER   A N    
1547 C  CA   . SER   A 220 ? 0.67950 0.77766 0.68963 -0.14253 -0.14251 -0.05629 372 SER   A CA   
1548 C  C    . SER   A 220 ? 0.66214 0.77537 0.64581 -0.13143 -0.14977 -0.05194 372 SER   A C    
1549 O  O    . SER   A 220 ? 0.60886 0.73024 0.59372 -0.12075 -0.14567 -0.03511 372 SER   A O    
1550 C  CB   . SER   A 220 ? 0.83958 0.96542 0.88604 -0.15110 -0.14974 -0.05138 372 SER   A CB   
1551 O  OG   . SER   A 220 ? 1.02760 1.14347 1.09593 -0.16777 -0.14782 -0.05787 372 SER   A OG   
1552 N  N    . HIS   A 221 ? 0.66870 0.78489 0.62746 -0.13435 -0.16083 -0.06662 373 HIS   A N    
1553 C  CA   . HIS   A 221 ? 0.61734 0.75318 0.54980 -0.12774 -0.17131 -0.06100 373 HIS   A CA   
1554 C  C    . HIS   A 221 ? 0.60226 0.72975 0.51235 -0.11560 -0.15863 -0.04551 373 HIS   A C    
1555 O  O    . HIS   A 221 ? 0.66756 0.77833 0.55671 -0.11333 -0.14655 -0.05284 373 HIS   A O    
1556 C  CB   . HIS   A 221 ? 0.61446 0.75399 0.51853 -0.13401 -0.18264 -0.08257 373 HIS   A CB   
1557 C  CG   . HIS   A 221 ? 0.73348 0.89296 0.60256 -0.12874 -0.19219 -0.07559 373 HIS   A CG   
1558 N  ND1  . HIS   A 221 ? 0.70502 0.88967 0.57999 -0.12673 -0.20875 -0.06031 373 HIS   A ND1  
1559 C  CD2  . HIS   A 221 ? 0.79705 0.95630 0.62450 -0.12541 -0.18754 -0.08042 373 HIS   A CD2  
1560 C  CE1  . HIS   A 221 ? 0.78648 0.98211 0.62230 -0.12329 -0.21518 -0.05388 373 HIS   A CE1  
1561 N  NE2  . HIS   A 221 ? 0.82114 1.00351 0.62684 -0.12345 -0.20133 -0.06598 373 HIS   A NE2  
1562 N  N    . GLN   A 222 ? 0.66808 0.80768 0.58457 -0.10779 -0.16236 -0.02481 374 GLN   A N    
1563 C  CA   . GLN   A 222 ? 0.57626 0.70718 0.47396 -0.09830 -0.15291 -0.00771 374 GLN   A CA   
1564 C  C    . GLN   A 222 ? 0.50573 0.61302 0.40934 -0.09566 -0.13215 -0.00815 374 GLN   A C    
1565 O  O    . GLN   A 222 ? 0.47938 0.57736 0.36185 -0.09146 -0.12193 -0.00205 374 GLN   A O    
1566 C  CB   . GLN   A 222 ? 0.64069 0.77793 0.49476 -0.09916 -0.15707 -0.00830 374 GLN   A CB   
1567 C  CG   . GLN   A 222 ? 0.80036 0.96084 0.64215 -0.09998 -0.17907 -0.00067 374 GLN   A CG   
1568 C  CD   . GLN   A 222 ? 1.02771 1.18917 0.87079 -0.09111 -0.18467 0.02693  374 GLN   A CD   
1569 O  OE1  . GLN   A 222 ? 1.10264 1.27234 0.97630 -0.08553 -0.19570 0.03580  374 GLN   A OE1  
1570 N  NE2  . GLN   A 222 ? 1.07795 1.23111 0.88986 -0.08982 -0.17715 0.04025  374 GLN   A NE2  
1571 N  N    . LEU   A 223 ? 0.50164 0.60098 0.43390 -0.09934 -0.12645 -0.01450 375 LEU   A N    
1572 C  CA   . LEU   A 223 ? 0.51623 0.59305 0.45243 -0.09762 -0.10924 -0.01552 375 LEU   A CA   
1573 C  C    . LEU   A 223 ? 0.52249 0.59425 0.45992 -0.08834 -0.09991 0.00200  375 LEU   A C    
1574 O  O    . LEU   A 223 ? 0.52917 0.58689 0.45319 -0.08497 -0.08826 0.00328  375 LEU   A O    
1575 C  CB   . LEU   A 223 ? 0.47822 0.54861 0.44310 -0.10534 -0.10662 -0.02162 375 LEU   A CB   
1576 C  CG   . LEU   A 223 ? 0.47711 0.52222 0.44334 -0.10482 -0.09196 -0.02320 375 LEU   A CG   
1577 C  CD1  . LEU   A 223 ? 0.45504 0.48603 0.39518 -0.10099 -0.08775 -0.03402 375 LEU   A CD1  
1578 C  CD2  . LEU   A 223 ? 0.58685 0.62352 0.57538 -0.11621 -0.09228 -0.02899 375 LEU   A CD2  
1579 N  N    . TYR   A 224 ? 0.57316 0.65680 0.52867 -0.08364 -0.10572 0.01417  376 TYR   A N    
1580 C  CA   . TYR   A 224 ? 0.61885 0.69469 0.57656 -0.07449 -0.09888 0.02884  376 TYR   A CA   
1581 C  C    . TYR   A 224 ? 0.53994 0.61020 0.46688 -0.07200 -0.09936 0.03771  376 TYR   A C    
1582 O  O    . TYR   A 224 ? 0.60145 0.65769 0.52071 -0.06947 -0.08809 0.04329  376 TYR   A O    
1583 C  CB   . TYR   A 224 ? 0.61518 0.70548 0.59921 -0.06767 -0.10745 0.03745  376 TYR   A CB   
1584 C  CG   . TYR   A 224 ? 0.66375 0.74223 0.65374 -0.05770 -0.10070 0.04896  376 TYR   A CG   
1585 C  CD1  . TYR   A 224 ? 0.50197 0.56869 0.50122 -0.05716 -0.08531 0.04601  376 TYR   A CD1  
1586 C  CD2  . TYR   A 224 ? 0.66153 0.73832 0.64635 -0.04937 -0.11108 0.06290  376 TYR   A CD2  
1587 C  CE1  . TYR   A 224 ? 0.53787 0.59336 0.54186 -0.04862 -0.08005 0.05362  376 TYR   A CE1  
1588 C  CE2  . TYR   A 224 ? 0.61467 0.67631 0.60603 -0.04078 -0.10624 0.07168  376 TYR   A CE2  
1589 C  CZ   . TYR   A 224 ? 0.62060 0.67245 0.62174 -0.04049 -0.09043 0.06548  376 TYR   A CZ   
1590 O  OH   . TYR   A 224 ? 0.71730 0.75391 0.72443 -0.03252 -0.08635 0.07133  376 TYR   A OH   
1591 N  N    . ALA   A 225 ? 0.49105 0.57425 0.39937 -0.07417 -0.11262 0.03966  377 ALA   A N    
1592 C  CA   . ALA   A 225 ? 0.51761 0.59912 0.39303 -0.07482 -0.11258 0.04982  377 ALA   A CA   
1593 C  C    . ALA   A 225 ? 0.53335 0.60778 0.39017 -0.07889 -0.09707 0.03883  377 ALA   A C    
1594 O  O    . ALA   A 225 ? 0.67187 0.74009 0.51475 -0.07867 -0.08806 0.04828  377 ALA   A O    
1595 C  CB   . ALA   A 225 ? 0.48823 0.58792 0.34295 -0.07812 -0.13001 0.05213  377 ALA   A CB   
1596 N  N    . LYS   A 226 ? 0.52558 0.60096 0.38445 -0.08259 -0.09452 0.01838  378 LYS   A N    
1597 C  CA   . LYS   A 226 ? 0.47895 0.54796 0.32499 -0.08344 -0.08106 0.00527  378 LYS   A CA   
1598 C  C    . LYS   A 226 ? 0.52818 0.58055 0.39090 -0.07916 -0.06750 0.00993  378 LYS   A C    
1599 O  O    . LYS   A 226 ? 0.54455 0.59515 0.39622 -0.07798 -0.05644 0.00937  378 LYS   A O    
1600 C  CB   . LYS   A 226 ? 0.46035 0.52852 0.30850 -0.08697 -0.08411 -0.01854 378 LYS   A CB   
1601 C  CG   . LYS   A 226 ? 0.53700 0.62303 0.36330 -0.09193 -0.09699 -0.02851 378 LYS   A CG   
1602 C  CD   . LYS   A 226 ? 0.63115 0.71154 0.46782 -0.09649 -0.10315 -0.05217 378 LYS   A CD   
1603 C  CE   . LYS   A 226 ? 0.69852 0.79616 0.50868 -0.10127 -0.11445 -0.06819 378 LYS   A CE   
1604 N  NZ   . LYS   A 226 ? 0.75555 0.87363 0.55699 -0.10394 -0.12988 -0.05290 378 LYS   A NZ   
1605 N  N    . MET   A 227 ? 0.51248 0.55606 0.40176 -0.07730 -0.06814 0.01409  379 MET   A N    
1606 C  CA   . MET   A 227 ? 0.52604 0.55509 0.42873 -0.07377 -0.05658 0.01791  379 MET   A CA   
1607 C  C    . MET   A 227 ? 0.50819 0.53512 0.40506 -0.07058 -0.05265 0.03388  379 MET   A C    
1608 O  O    . MET   A 227 ? 0.51664 0.53593 0.41217 -0.06928 -0.04242 0.03469  379 MET   A O    
1609 C  CB   . MET   A 227 ? 0.48751 0.51218 0.41671 -0.07402 -0.05762 0.01837  379 MET   A CB   
1610 C  CG   . MET   A 227 ? 0.47505 0.49488 0.41269 -0.07990 -0.05914 0.00439  379 MET   A CG   
1611 S  SD   . MET   A 227 ? 0.49041 0.51094 0.45799 -0.08411 -0.05844 0.00802  379 MET   A SD   
1612 C  CE   . MET   A 227 ? 0.43506 0.43789 0.40377 -0.08010 -0.04462 0.01339  379 MET   A CE   
1613 N  N    . ILE   A 228 ? 0.44854 0.48105 0.34354 -0.06944 -0.06220 0.04691  380 ILE   A N    
1614 C  CA   . ILE   A 228 ? 0.54109 0.56665 0.43035 -0.06778 -0.06080 0.06323  380 ILE   A CA   
1615 C  C    . ILE   A 228 ? 0.62638 0.65776 0.48847 -0.07368 -0.05529 0.06606  380 ILE   A C    
1616 O  O    . ILE   A 228 ? 0.60385 0.62866 0.46276 -0.07544 -0.04771 0.07444  380 ILE   A O    
1617 C  CB   . ILE   A 228 ? 0.65910 0.68601 0.55471 -0.06372 -0.07512 0.07698  380 ILE   A CB   
1618 C  CG1  . ILE   A 228 ? 0.55206 0.57987 0.47857 -0.05731 -0.07792 0.07171  380 ILE   A CG1  
1619 C  CG2  . ILE   A 228 ? 0.76730 0.78070 0.65717 -0.06281 -0.07579 0.09477  380 ILE   A CG2  
1620 C  CD1  . ILE   A 228 ? 0.66733 0.68231 0.60991 -0.05366 -0.06643 0.06955  380 ILE   A CD1  
1621 N  N    . GLN   A 229 ? 0.59367 0.64005 0.43615 -0.07774 -0.05859 0.05791  381 GLN   A N    
1622 C  CA   . GLN   A 229 ? 0.59942 0.65792 0.41595 -0.08353 -0.05034 0.05647  381 GLN   A CA   
1623 C  C    . GLN   A 229 ? 0.60970 0.66541 0.43477 -0.08185 -0.03507 0.04462  381 GLN   A C    
1624 O  O    . GLN   A 229 ? 0.56644 0.63029 0.38079 -0.08595 -0.02539 0.04899  381 GLN   A O    
1625 C  CB   . GLN   A 229 ? 0.61654 0.69319 0.41129 -0.08683 -0.05601 0.04374  381 GLN   A CB   
1626 C  CG   . GLN   A 229 ? 0.67533 0.77133 0.44052 -0.09290 -0.04641 0.04020  381 GLN   A CG   
1627 C  CD   . GLN   A 229 ? 0.79659 0.89519 0.54601 -0.10005 -0.04445 0.06559  381 GLN   A CD   
1628 O  OE1  . GLN   A 229 ? 0.88619 0.97815 0.63056 -0.10179 -0.05754 0.08585  381 GLN   A OE1  
1629 N  NE2  . GLN   A 229 ? 0.71413 0.82227 0.45771 -0.10448 -0.02897 0.06507  381 GLN   A NE2  
1630 N  N    A LYS   A 230 ? 0.53885 0.58434 0.38407 -0.07653 -0.03341 0.03070  382 LYS   A N    
1631 N  N    B LYS   A 230 ? 0.54524 0.59075 0.39044 -0.07653 -0.03346 0.03067  382 LYS   A N    
1632 C  CA   A LYS   A 230 ? 0.52382 0.56483 0.37894 -0.07322 -0.02192 0.02090  382 LYS   A CA   
1633 C  CA   B LYS   A 230 ? 0.52092 0.56162 0.37640 -0.07315 -0.02204 0.02092  382 LYS   A CA   
1634 C  C    A LYS   A 230 ? 0.49074 0.52325 0.35603 -0.07321 -0.01644 0.03477  382 LYS   A C    
1635 C  C    B LYS   A 230 ? 0.50014 0.53300 0.36489 -0.07337 -0.01647 0.03505  382 LYS   A C    
1636 O  O    A LYS   A 230 ? 0.50407 0.54137 0.37110 -0.07305 -0.00697 0.03141  382 LYS   A O    
1637 O  O    B LYS   A 230 ? 0.50670 0.54508 0.37225 -0.07359 -0.00694 0.03221  382 LYS   A O    
1638 C  CB   A LYS   A 230 ? 0.50917 0.53701 0.38180 -0.06879 -0.02397 0.00693  382 LYS   A CB   
1639 C  CB   B LYS   A 230 ? 0.51146 0.53834 0.38530 -0.06876 -0.02423 0.00798  382 LYS   A CB   
1640 C  CG   A LYS   A 230 ? 0.56462 0.59779 0.42898 -0.06873 -0.02733 -0.01268 382 LYS   A CG   
1641 C  CG   B LYS   A 230 ? 0.56799 0.59886 0.43515 -0.06912 -0.02905 -0.01048 382 LYS   A CG   
1642 C  CD   A LYS   A 230 ? 0.65681 0.70542 0.50672 -0.06679 -0.01828 -0.02485 382 LYS   A CD   
1643 C  CD   B LYS   A 230 ? 0.64914 0.69469 0.50052 -0.06742 -0.02147 -0.02445 382 LYS   A CD   
1644 C  CE   A LYS   A 230 ? 0.72383 0.77817 0.56351 -0.06573 -0.02225 -0.04776 382 LYS   A CE   
1645 C  CE   B LYS   A 230 ? 0.70901 0.76365 0.54545 -0.06911 -0.02800 -0.04206 382 LYS   A CE   
1646 N  NZ   A LYS   A 230 ? 0.74305 0.81208 0.56123 -0.07246 -0.03091 -0.04502 382 LYS   A NZ   
1647 N  NZ   B LYS   A 230 ? 0.73626 0.81044 0.55594 -0.06661 -0.01899 -0.05823 382 LYS   A NZ   
1648 N  N    . LEU   A 231 ? 0.51985 0.54108 0.39372 -0.07286 -0.02293 0.04858  383 LEU   A N    
1649 C  CA   . LEU   A 231 ? 0.59189 0.60310 0.47390 -0.07342 -0.01941 0.06023  383 LEU   A CA   
1650 C  C    . LEU   A 231 ? 0.54723 0.56657 0.41288 -0.08144 -0.01650 0.07260  383 LEU   A C    
1651 O  O    . LEU   A 231 ? 0.51143 0.52870 0.38198 -0.08476 -0.00980 0.07681  383 LEU   A O    
1652 C  CB   . LEU   A 231 ? 0.60027 0.59787 0.49615 -0.06940 -0.02762 0.06884  383 LEU   A CB   
1653 C  CG   . LEU   A 231 ? 0.57961 0.57219 0.49361 -0.06390 -0.02789 0.05893  383 LEU   A CG   
1654 C  CD1  . LEU   A 231 ? 0.58057 0.56750 0.50904 -0.05913 -0.03506 0.06551  383 LEU   A CD1  
1655 C  CD2  . LEU   A 231 ? 0.47575 0.46179 0.39758 -0.06257 -0.01894 0.05237  383 LEU   A CD2  
1656 N  N    . ALA   A 232 ? 0.50025 0.53012 0.34577 -0.08617 -0.02195 0.07936  384 ALA   A N    
1657 C  CA   . ALA   A 232 ? 0.57591 0.61708 0.40147 -0.09671 -0.01787 0.09246  384 ALA   A CA   
1658 C  C    . ALA   A 232 ? 0.58330 0.64674 0.40350 -0.09974 -0.00334 0.07875  384 ALA   A C    
1659 O  O    . ALA   A 232 ? 0.56767 0.63883 0.38753 -0.10748 0.00530  0.08594  384 ALA   A O    
1660 C  CB   . ALA   A 232 ? 0.56924 0.61846 0.37057 -0.10123 -0.02814 0.10328  384 ALA   A CB   
1661 N  N    . ASP   A 233 ? 0.50395 0.57840 0.32255 -0.09356 -0.00104 0.05783  385 ASP   A N    
1662 C  CA   . ASP   A 233 ? 0.52984 0.62532 0.34842 -0.09236 0.01192  0.04068  385 ASP   A CA   
1663 C  C    . ASP   A 233 ? 0.47955 0.56855 0.32230 -0.08895 0.01865  0.03862  385 ASP   A C    
1664 O  O    . ASP   A 233 ? 0.50911 0.61856 0.35408 -0.09226 0.02959  0.03515  385 ASP   A O    
1665 C  CB   . ASP   A 233 ? 0.49691 0.59593 0.31491 -0.08379 0.01012  0.01661  385 ASP   A CB   
1666 C  CG   . ASP   A 233 ? 0.72641 0.83306 0.52069 -0.08737 0.00148  0.01596  385 ASP   A CG   
1667 O  OD1  . ASP   A 233 ? 0.67998 0.78310 0.47582 -0.08174 -0.00396 -0.00221 385 ASP   A OD1  
1668 O  OD2  . ASP   A 233 ? 0.63682 0.75205 0.41061 -0.09654 -0.00116 0.03413  385 ASP   A OD2  
1669 N  N    . LEU   A 234 ? 0.46207 0.52614 0.32313 -0.08276 0.01218  0.04030  386 LEU   A N    
1670 C  CA   . LEU   A 234 ? 0.50541 0.56289 0.38669 -0.07962 0.01637  0.03866  386 LEU   A CA   
1671 C  C    . LEU   A 234 ? 0.51374 0.57463 0.39568 -0.08980 0.01998  0.05441  386 LEU   A C    
1672 O  O    . LEU   A 234 ? 0.51606 0.58691 0.41032 -0.09092 0.02662  0.05090  386 LEU   A O    
1673 C  CB   . LEU   A 234 ? 0.50621 0.53853 0.40166 -0.07287 0.00891  0.03869  386 LEU   A CB   
1674 C  CG   . LEU   A 234 ? 0.51434 0.54077 0.41605 -0.06442 0.00667  0.02301  386 LEU   A CG   
1675 C  CD1  . LEU   A 234 ? 0.49265 0.49911 0.40303 -0.06220 -0.00044 0.02736  386 LEU   A CD1  
1676 C  CD2  . LEU   A 234 ? 0.45418 0.48493 0.36811 -0.05825 0.01186  0.01179  386 LEU   A CD2  
1677 N  N    . ARG   A 235 ? 0.48238 0.53390 0.35294 -0.09749 0.01407  0.07222  387 ARG   A N    
1678 C  CA   . ARG   A 235 ? 0.52768 0.57887 0.39738 -0.10979 0.01620  0.08891  387 ARG   A CA   
1679 C  C    . ARG   A 235 ? 0.52423 0.60840 0.38562 -0.11968 0.02867  0.08745  387 ARG   A C    
1680 O  O    . ARG   A 235 ? 0.55454 0.64763 0.42745 -0.12746 0.03502  0.09068  387 ARG   A O    
1681 C  CB   . ARG   A 235 ? 0.54395 0.57736 0.40088 -0.11547 0.00560  0.10919  387 ARG   A CB   
1682 C  CG   . ARG   A 235 ? 0.56666 0.57205 0.43616 -0.10514 -0.00588 0.10989  387 ARG   A CG   
1683 C  CD   . ARG   A 235 ? 0.61954 0.60926 0.50998 -0.10257 -0.00494 0.10632  387 ARG   A CD   
1684 N  NE   . ARG   A 235 ? 0.72667 0.69442 0.62870 -0.09239 -0.01388 0.10477  387 ARG   A NE   
1685 C  CZ   . ARG   A 235 ? 0.65091 0.59629 0.55865 -0.09254 -0.02241 0.11556  387 ARG   A CZ   
1686 N  NH1  . ARG   A 235 ? 0.58447 0.52166 0.48632 -0.10415 -0.02452 0.13123  387 ARG   A NH1  
1687 N  NH2  . ARG   A 235 ? 0.68790 0.61937 0.60840 -0.08135 -0.02882 0.11029  387 ARG   A NH2  
1688 N  N    A SER   A 236 ? 0.51651 0.62228 0.35853 -0.12004 0.03258  0.08114  388 SER   A N    
1689 N  N    B SER   A 236 ? 0.51700 0.62272 0.35898 -0.12005 0.03255  0.08118  388 SER   A N    
1690 C  CA   A SER   A 236 ? 0.52897 0.67281 0.36274 -0.12839 0.04672  0.07620  388 SER   A CA   
1691 C  CA   B SER   A 236 ? 0.52996 0.67383 0.36362 -0.12826 0.04669  0.07603  388 SER   A CA   
1692 C  C    A SER   A 236 ? 0.52162 0.68266 0.37958 -0.11906 0.05568  0.05491  388 SER   A C    
1693 C  C    B SER   A 236 ? 0.52060 0.68128 0.37871 -0.11907 0.05558  0.05505  388 SER   A C    
1694 O  O    A SER   A 236 ? 0.53163 0.71907 0.39878 -0.12710 0.06640  0.05510  388 SER   A O    
1695 O  O    B SER   A 236 ? 0.53114 0.71750 0.39879 -0.12715 0.06609  0.05554  388 SER   A O    
1696 C  CB   A SER   A 236 ? 0.54432 0.70822 0.35050 -0.12862 0.04849  0.06951  388 SER   A CB   
1697 C  CB   B SER   A 236 ? 0.54721 0.71093 0.35378 -0.12795 0.04840  0.06856  388 SER   A CB   
1698 O  OG   A SER   A 236 ? 0.57303 0.77887 0.37310 -0.13359 0.06434  0.05824  388 SER   A OG   
1699 O  OG   B SER   A 236 ? 0.57618 0.73312 0.35710 -0.13972 0.04109  0.09161  388 SER   A OG   
1700 N  N    . LEU   A 237 ? 0.48745 0.63451 0.35725 -0.10262 0.05056  0.03735  389 LEU   A N    
1701 C  CA   . LEU   A 237 ? 0.46606 0.62360 0.35998 -0.09168 0.05532  0.01919  389 LEU   A CA   
1702 C  C    . LEU   A 237 ? 0.50644 0.65486 0.42092 -0.09544 0.05364  0.02869  389 LEU   A C    
1703 O  O    . LEU   A 237 ? 0.52530 0.69600 0.45854 -0.09380 0.06003  0.02029  389 LEU   A O    
1704 C  CB   . LEU   A 237 ? 0.49802 0.63478 0.39814 -0.07544 0.04746  0.00306  389 LEU   A CB   
1705 C  CG   . LEU   A 237 ? 0.62632 0.77476 0.51234 -0.06929 0.04909  -0.01473 389 LEU   A CG   
1706 C  CD1  . LEU   A 237 ? 0.54471 0.66238 0.43400 -0.05915 0.03764  -0.02289 389 LEU   A CD1  
1707 C  CD2  . LEU   A 237 ? 0.71207 0.89328 0.60901 -0.06170 0.06002  -0.03595 389 LEU   A CD2  
1708 N  N    . ASN   A 238 ? 0.58686 0.70424 0.49943 -0.09973 0.04434  0.04438  390 ASN   A N    
1709 C  CA   . ASN   A 238 ? 0.57935 0.68669 0.50817 -0.10504 0.04182  0.05258  390 ASN   A CA   
1710 C  C    . ASN   A 238 ? 0.58604 0.71931 0.51734 -0.12166 0.05051  0.06176  390 ASN   A C    
1711 O  O    . ASN   A 238 ? 0.53721 0.68571 0.48870 -0.12378 0.05375  0.05714  390 ASN   A O    
1712 C  CB   . ASN   A 238 ? 0.49421 0.56526 0.41836 -0.10649 0.03098  0.06583  390 ASN   A CB   
1713 C  CG   . ASN   A 238 ? 0.54985 0.60583 0.49059 -0.10804 0.02651  0.06811  390 ASN   A CG   
1714 O  OD1  . ASN   A 238 ? 0.61289 0.68374 0.56455 -0.11714 0.03051  0.06984  390 ASN   A OD1  
1715 N  ND2  . ASN   A 238 ? 0.52870 0.55767 0.47148 -0.10001 0.01832  0.06721  390 ASN   A ND2  
1716 N  N    . GLU   A 239 ? 0.65749 0.79768 0.56826 -0.13483 0.05377  0.07588  391 GLU   A N    
1717 C  CA   . GLU   A 239 ? 0.74173 0.90629 0.65246 -0.15470 0.06255  0.08846  391 GLU   A CA   
1718 C  C    . GLU   A 239 ? 0.65890 0.87204 0.58201 -0.15371 0.07713  0.07184  391 GLU   A C    
1719 O  O    . GLU   A 239 ? 0.62585 0.86100 0.56829 -0.16393 0.08309  0.07322  391 GLU   A O    
1720 C  CB   . GLU   A 239 ? 0.87676 1.03891 0.75824 -0.16896 0.06232  0.10880  391 GLU   A CB   
1721 C  CG   . GLU   A 239 ? 1.08533 1.20345 0.96092 -0.17499 0.04801  0.13033  391 GLU   A CG   
1722 C  CD   . GLU   A 239 ? 1.34342 1.45228 1.19313 -0.17796 0.04179  0.14472  391 GLU   A CD   
1723 O  OE1  . GLU   A 239 ? 1.41774 1.49168 1.26228 -0.17259 0.02784  0.15455  391 GLU   A OE1  
1724 O  OE2  . GLU   A 239 ? 1.40073 1.53877 1.23678 -0.18459 0.05026  0.14507  391 GLU   A OE2  
1725 N  N    . GLU   A 240 ? 0.51484 0.74655 0.42921 -0.14109 0.08253  0.05431  392 GLU   A N    
1726 C  CA   . GLU   A 240 ? 0.51109 0.79088 0.43908 -0.13687 0.09656  0.03485  392 GLU   A CA   
1727 C  C    . GLU   A 240 ? 0.61692 0.89949 0.57957 -0.12336 0.09348  0.01984  392 GLU   A C    
1728 O  O    . GLU   A 240 ? 0.60993 0.93151 0.59445 -0.12717 0.10285  0.01299  392 GLU   A O    
1729 C  CB   . GLU   A 240 ? 0.48800 0.78144 0.39887 -0.12426 0.10090  0.01613  392 GLU   A CB   
1730 C  CG   . GLU   A 240 ? 0.59960 0.94386 0.52546 -0.11648 0.11568  -0.00844 392 GLU   A CG   
1731 C  CD   . GLU   A 240 ? 0.72555 1.11818 0.65238 -0.13730 0.13215  0.00068  392 GLU   A CD   
1732 O  OE1  . GLU   A 240 ? 0.73922 1.17288 0.69422 -0.13282 0.14244  -0.01523 392 GLU   A OE1  
1733 O  OE2  . GLU   A 240 ? 0.75960 1.14375 0.66207 -0.15582 0.13143  0.02378  392 GLU   A OE2  
1734 N  N    . HIS   A 241 ? 0.54327 0.78756 0.51163 -0.10817 0.08009  0.01532  393 HIS   A N    
1735 C  CA   . HIS   A 241 ? 0.57966 0.82423 0.57707 -0.09569 0.07479  0.00391  393 HIS   A CA   
1736 C  C    . HIS   A 241 ? 0.57202 0.82178 0.58608 -0.11014 0.07341  0.01608  393 HIS   A C    
1737 O  O    . HIS   A 241 ? 0.59199 0.86922 0.63291 -0.10684 0.07521  0.00653  393 HIS   A O    
1738 C  CB   . HIS   A 241 ? 0.51895 0.72043 0.51426 -0.08048 0.06089  0.00092  393 HIS   A CB   
1739 C  CG   . HIS   A 241 ? 0.54811 0.74501 0.56775 -0.07009 0.05290  -0.00546 393 HIS   A CG   
1740 N  ND1  . HIS   A 241 ? 0.50541 0.68303 0.53024 -0.07686 0.04476  0.00591  393 HIS   A ND1  
1741 C  CD2  . HIS   A 241 ? 0.48437 0.69389 0.52404 -0.05308 0.05052  -0.02215 393 HIS   A CD2  
1742 C  CE1  . HIS   A 241 ? 0.50301 0.68329 0.54736 -0.06553 0.03772  -0.00250 393 HIS   A CE1  
1743 N  NE2  . HIS   A 241 ? 0.48959 0.68807 0.54416 -0.05062 0.04039  -0.01835 393 HIS   A NE2  
1744 N  N    . SER   A 242 ? 0.54492 0.76794 0.54521 -0.12569 0.06872  0.03620  394 SER   A N    
1745 C  CA   . SER   A 242 ? 0.58293 0.80410 0.59836 -0.14058 0.06530  0.04679  394 SER   A CA   
1746 C  C    . SER   A 242 ? 0.61872 0.88855 0.64861 -0.15705 0.07826  0.04813  394 SER   A C    
1747 O  O    . SER   A 242 ? 0.69889 0.99018 0.75616 -0.15978 0.07761  0.04244  394 SER   A O    
1748 C  CB   . SER   A 242 ? 0.55210 0.73229 0.54981 -0.15295 0.05730  0.06677  394 SER   A CB   
1749 O  OG   . SER   A 242 ? 0.73617 0.87703 0.72789 -0.13840 0.04565  0.06376  394 SER   A OG   
1750 N  N    . LYS   A 243 ? 0.55415 0.84484 0.56565 -0.16942 0.09006  0.05613  395 LYS   A N    
1751 C  CA   . LYS   A 243 ? 0.63583 0.97876 0.65965 -0.18744 0.10510  0.05815  395 LYS   A CA   
1752 C  C    . LYS   A 243 ? 0.67605 1.06650 0.72964 -0.17181 0.11279  0.03275  395 LYS   A C    
1753 O  O    . LYS   A 243 ? 0.68691 1.11764 0.76807 -0.18257 0.11941  0.03044  395 LYS   A O    
1754 C  CB   . LYS   A 243 ? 0.74526 1.09586 0.73842 -0.19643 0.11362  0.06797  395 LYS   A CB   
1755 C  CG   . LYS   A 243 ? 0.93201 1.23445 0.90041 -0.20922 0.10260  0.09363  395 LYS   A CG   
1756 C  CD   . LYS   A 243 ? 1.07492 1.37356 1.00880 -0.20800 0.10464  0.09945  395 LYS   A CD   
1757 C  CE   . LYS   A 243 ? 1.19154 1.44349 1.10531 -0.21803 0.09159  0.12461  395 LYS   A CE   
1758 N  NZ   . LYS   A 243 ? 1.21918 1.47463 1.10141 -0.22055 0.09303  0.13285  395 LYS   A NZ   
1759 N  N    . GLN   A 244 ? 0.59729 0.98372 0.64823 -0.14629 0.11098  0.01314  396 GLN   A N    
1760 C  CA   . GLN   A 244 ? 0.55866 0.98251 0.64087 -0.12725 0.11445  -0.01182 396 GLN   A CA   
1761 C  C    . GLN   A 244 ? 0.60479 1.01252 0.71452 -0.11798 0.09936  -0.01483 396 GLN   A C    
1762 O  O    . GLN   A 244 ? 0.58800 1.03495 0.73149 -0.11103 0.10115  -0.02849 396 GLN   A O    
1763 C  CB   . GLN   A 244 ? 0.48669 0.90481 0.55803 -0.10309 0.11486  -0.03189 396 GLN   A CB   
1764 C  CG   . GLN   A 244 ? 0.60404 1.06095 0.65751 -0.10817 0.13267  -0.03958 396 GLN   A CG   
1765 C  CD   . GLN   A 244 ? 0.61430 1.06281 0.65812 -0.08422 0.13133  -0.06270 396 GLN   A CD   
1766 O  OE1  . GLN   A 244 ? 0.61688 1.05608 0.68303 -0.06092 0.12263  -0.08093 396 GLN   A OE1  
1767 N  NE2  . GLN   A 244 ? 0.70573 1.15596 0.71562 -0.09042 0.13848  -0.06167 396 GLN   A NE2  
1768 N  N    . TYR   A 245 ? 0.53820 0.89193 0.63439 -0.11734 0.08424  -0.00307 397 TYR   A N    
1769 C  CA   . TYR   A 245 ? 0.58153 0.92088 0.69854 -0.11030 0.06969  -0.00530 397 TYR   A CA   
1770 C  C    . TYR   A 245 ? 0.52491 0.88947 0.66355 -0.13140 0.07066  0.00254  397 TYR   A C    
1771 O  O    . TYR   A 245 ? 0.49798 0.88585 0.66669 -0.12538 0.06461  -0.00707 397 TYR   A O    
1772 C  CB   . TYR   A 245 ? 0.59454 0.87469 0.68979 -0.10590 0.05552  0.00410  397 TYR   A CB   
1773 C  CG   . TYR   A 245 ? 0.56706 0.83354 0.67800 -0.10051 0.04080  0.00233  397 TYR   A CG   
1774 C  CD1  . TYR   A 245 ? 0.50213 0.76816 0.62536 -0.07855 0.03185  -0.01030 397 TYR   A CD1  
1775 C  CD2  . TYR   A 245 ? 0.59442 0.84802 0.70711 -0.11776 0.03471  0.01316  397 TYR   A CD2  
1776 C  CE1  . TYR   A 245 ? 0.44349 0.69911 0.57728 -0.07436 0.01738  -0.01049 397 TYR   A CE1  
1777 C  CE2  . TYR   A 245 ? 0.55498 0.79889 0.67913 -0.11339 0.02084  0.00976  397 TYR   A CE2  
1778 C  CZ   . TYR   A 245 ? 0.55740 0.80388 0.69066 -0.09193 0.01233  -0.00130 397 TYR   A CZ   
1779 O  OH   . TYR   A 245 ? 0.53297 0.77124 0.67374 -0.08833 -0.00255 -0.00315 397 TYR   A OH   
1780 N  N    . ARG   A 246 ? 0.48183 0.84082 0.60639 -0.15677 0.07650  0.02064  398 ARG   A N    
1781 C  CA   . ARG   A 246 ? 0.53997 0.91932 0.68535 -0.18044 0.07675  0.02925  398 ARG   A CA   
1782 C  C    . ARG   A 246 ? 0.58474 1.03385 0.76181 -0.18469 0.09033  0.01803  398 ARG   A C    
1783 O  O    . ARG   A 246 ? 0.62238 1.09820 0.83082 -0.19360 0.08648  0.01518  398 ARG   A O    
1784 C  CB   . ARG   A 246 ? 0.66250 1.01743 0.78546 -0.20735 0.07951  0.05288  398 ARG   A CB   
1785 C  CG   . ARG   A 246 ? 0.83782 1.12905 0.93038 -0.20177 0.06805  0.06312  398 ARG   A CG   
1786 C  CD   . ARG   A 246 ? 1.01235 1.27871 1.08726 -0.22708 0.06815  0.08693  398 ARG   A CD   
1787 N  NE   . ARG   A 246 ? 1.09488 1.32578 1.13679 -0.22079 0.06636  0.09666  398 ARG   A NE   
1788 C  CZ   . ARG   A 246 ? 1.05443 1.29105 1.07413 -0.22418 0.07420  0.10559  398 ARG   A CZ   
1789 N  NH1  . ARG   A 246 ? 1.07863 1.35349 1.10401 -0.23382 0.08557  0.10589  398 ARG   A NH1  
1790 N  NH2  . ARG   A 246 ? 0.93613 1.14177 0.92820 -0.21777 0.06983  0.11372  398 ARG   A NH2  
1791 N  N    . SER   A 247 ? 0.59056 1.07303 0.76112 -0.17833 0.10627  0.00983  399 SER   A N    
1792 C  CA   . SER   A 247 ? 0.60297 1.14755 0.80166 -0.17639 0.11887  -0.00439 399 SER   A CA   
1793 C  C    . SER   A 247 ? 0.51980 1.09388 0.75701 -0.15114 0.11197  -0.02811 399 SER   A C    
1794 O  O    . SER   A 247 ? 0.56908 1.18425 0.84041 -0.15075 0.11293  -0.03706 399 SER   A O    
1795 C  CB   . SER   A 247 ? 0.62488 1.18747 0.79985 -0.17263 0.13522  -0.00916 399 SER   A CB   
1796 O  OG   . SER   A 247 ? 0.71203 1.29687 0.89743 -0.14486 0.13875  -0.03449 399 SER   A OG   
1797 N  N    . LEU   A 248 ? 0.53721 1.06943 0.76139 -0.12436 0.09961  -0.03668 400 LEU   A N    
1798 C  CA   . LEU   A 248 ? 0.49015 1.02983 0.74387 -0.09740 0.08658  -0.05472 400 LEU   A CA   
1799 C  C    . LEU   A 248 ? 0.57184 1.09944 0.84300 -0.10442 0.06927  -0.04719 400 LEU   A C    
1800 O  O    . LEU   A 248 ? 0.58974 1.15676 0.89935 -0.09717 0.06366  -0.05847 400 LEU   A O    
1801 C  CB   . LEU   A 248 ? 0.54077 1.03272 0.77278 -0.07119 0.07682  -0.06173 400 LEU   A CB   
1802 C  CG   . LEU   A 248 ? 0.53196 1.03897 0.75559 -0.05561 0.08934  -0.07833 400 LEU   A CG   
1803 C  CD1  . LEU   A 248 ? 0.50687 0.95423 0.70179 -0.03918 0.07831  -0.07826 400 LEU   A CD1  
1804 C  CD2  . LEU   A 248 ? 0.53083 1.09115 0.79596 -0.03447 0.09261  -0.10361 400 LEU   A CD2  
1805 N  N    . SER   A 249 ? 0.55540 1.03049 0.79944 -0.11797 0.05996  -0.02962 401 SER   A N    
1806 C  CA   . SER   A 249 ? 0.66312 1.12153 0.91788 -0.12431 0.04258  -0.02456 401 SER   A CA   
1807 C  C    . SER   A 249 ? 0.70918 1.21187 0.99386 -0.14939 0.04639  -0.02150 401 SER   A C    
1808 O  O    . SER   A 249 ? 0.74708 1.25388 1.05193 -0.15157 0.03147  -0.02393 401 SER   A O    
1809 C  CB   . SER   A 249 ? 0.55227 0.94609 0.77074 -0.13246 0.03390  -0.00945 401 SER   A CB   
1810 O  OG   . SER   A 249 ? 0.72554 1.08031 0.92458 -0.10913 0.02449  -0.01327 401 SER   A OG   
1811 N  N    . PHE   A 250 ? 0.81257 1.34902 1.09940 -0.17013 0.06551  -0.01551 402 PHE   A N    
1812 C  CA   . PHE   A 250 ? 0.87324 1.44049 1.18332 -0.19439 0.06881  -0.00998 402 PHE   A CA   
1813 C  C    . PHE   A 250 ? 0.84157 1.46227 1.19590 -0.18089 0.06551  -0.02773 402 PHE   A C    
1814 O  O    . PHE   A 250 ? 0.94163 1.57472 1.31803 -0.19448 0.05853  -0.02561 402 PHE   A O    
1815 C  CB   . PHE   A 250 ? 0.87660 1.44831 1.16640 -0.21128 0.08781  0.00206  402 PHE   A CB   
1816 C  CG   . PHE   A 250 ? 0.89312 1.45058 1.18273 -0.23973 0.08619  0.01863  402 PHE   A CG   
1817 C  CD1  . PHE   A 250 ? 0.87379 1.37400 1.14149 -0.25391 0.07471  0.03420  402 PHE   A CD1  
1818 C  CD2  . PHE   A 250 ? 0.87659 1.47744 1.18985 -0.25153 0.09566  0.01746  402 PHE   A CD2  
1819 C  CE1  . PHE   A 250 ? 0.91399 1.39754 1.18357 -0.27836 0.07193  0.04770  402 PHE   A CE1  
1820 C  CE2  . PHE   A 250 ? 0.89387 1.48082 1.20901 -0.27850 0.09368  0.03270  402 PHE   A CE2  
1821 C  CZ   . PHE   A 250 ? 0.94544 1.47224 1.23891 -0.29146 0.08136  0.04751  402 PHE   A CZ   
1822 N  N    . GLN   A 251 ? 0.77848 1.42904 1.14718 -0.15332 0.06928  -0.04585 403 GLN   A N    
1823 C  CA   . GLN   A 251 ? 0.66835 1.36512 1.07996 -0.13497 0.06335  -0.06357 403 GLN   A CA   
1824 C  C    . GLN   A 251 ? 0.59174 1.27383 1.01779 -0.11834 0.03781  -0.06935 403 GLN   A C    
1825 O  O    . GLN   A 251 ? 0.51687 1.15944 0.92183 -0.09498 0.02933  -0.07234 403 GLN   A O    
1826 C  CB   . GLN   A 251 ? 0.64191 1.37139 1.06211 -0.10997 0.07688  -0.08202 403 GLN   A CB   
1827 C  CG   . GLN   A 251 ? 0.83377 1.60622 1.26196 -0.12157 0.09760  -0.08432 403 GLN   A CG   
1828 C  CD   . GLN   A 251 ? 0.92530 1.67795 1.31365 -0.14869 0.11396  -0.06573 403 GLN   A CD   
1829 O  OE1  . GLN   A 251 ? 0.93105 1.68719 1.31869 -0.17607 0.11828  -0.05072 403 GLN   A OE1  
1830 N  NE2  . GLN   A 251 ? 0.90180 1.63174 1.25689 -0.14071 0.12153  -0.06623 403 GLN   A NE2  
1831 N  N    . PRO   A 252 ? 0.62132 1.31327 1.07025 -0.12685 0.02295  -0.06806 404 PRO   A N    
1832 C  CA   . PRO   A 252 ? 0.56408 1.23940 1.02022 -0.11158 -0.00377 -0.07218 404 PRO   A CA   
1833 C  C    . PRO   A 252 ? 0.51000 1.19545 0.98269 -0.07296 -0.01343 -0.08733 404 PRO   A C    
1834 O  O    . PRO   A 252 ? 0.56979 1.21213 1.02568 -0.05525 -0.03411 -0.08489 404 PRO   A O    
1835 C  CB   . PRO   A 252 ? 0.58546 1.27912 1.06617 -0.12854 -0.01486 -0.07012 404 PRO   A CB   
1836 C  CG   . PRO   A 252 ? 0.57647 1.26977 1.04782 -0.16050 0.00410  -0.05799 404 PRO   A CG   
1837 C  CD   . PRO   A 252 ? 0.58948 1.30202 1.05372 -0.15319 0.02832  -0.06096 404 PRO   A CD   
1838 N  N    . GLU   A 253 ? 0.57407 1.30426 1.07273 -0.05853 0.00055  -0.10121 405 GLU   A N    
1839 C  CA   . GLU   A 253 ? 0.51092 1.24739 1.02724 -0.02020 -0.00904 -0.11724 405 GLU   A CA   
1840 C  C    . GLU   A 253 ? 0.44915 1.12135 0.92274 -0.00456 -0.01182 -0.11286 405 GLU   A C    
1841 O  O    . GLU   A 253 ? 0.46555 1.10652 0.93633 0.02164  -0.03136 -0.11513 405 GLU   A O    
1842 C  CB   . GLU   A 253 ? 0.55441 1.33512 1.09395 -0.00898 0.00976  -0.13250 405 GLU   A CB   
1843 C  CG   . GLU   A 253 ? 0.72717 1.55111 1.28645 -0.03401 0.02250  -0.12928 405 GLU   A CG   
1844 C  CD   . GLU   A 253 ? 0.84366 1.66560 1.37403 -0.06405 0.04768  -0.11817 405 GLU   A CD   
1845 O  OE1  . GLU   A 253 ? 0.88489 1.70504 1.41097 -0.09504 0.04955  -0.10311 405 GLU   A OE1  
1846 O  OE2  . GLU   A 253 ? 0.90967 1.72868 1.42022 -0.05626 0.06410  -0.12423 405 GLU   A OE2  
1847 N  N    . ASN   A 254 ? 0.33979 0.98522 0.77604 -0.02138 0.00651  -0.10387 406 ASN   A N    
1848 C  CA   . ASN   A 254 ? 0.29960 0.88083 0.69252 -0.00941 0.00486  -0.09839 406 ASN   A CA   
1849 C  C    . ASN   A 254 ? 0.39372 0.91329 0.75252 -0.01742 -0.01215 -0.08050 406 ASN   A C    
1850 O  O    . ASN   A 254 ? 0.39422 0.86814 0.73327 0.00095  -0.02558 -0.07807 406 ASN   A O    
1851 C  CB   . ASN   A 254 ? 0.34386 0.92353 0.71049 -0.02391 0.02921  -0.09583 406 ASN   A CB   
1852 C  CG   . ASN   A 254 ? 0.43171 1.07047 0.82504 -0.01351 0.04769  -0.11617 406 ASN   A CG   
1853 O  OD1  . ASN   A 254 ? 0.49514 1.15757 0.91984 0.01436  0.04109  -0.13515 406 ASN   A OD1  
1854 N  ND2  . ASN   A 254 ? 0.53171 1.19525 0.91240 -0.03561 0.07062  -0.11250 406 ASN   A ND2  
1855 N  N    . SER   A 255 ? 0.46894 0.98666 0.82052 -0.04546 -0.01143 -0.06842 407 SER   A N    
1856 C  CA   . SER   A 255 ? 0.50624 0.96966 0.82619 -0.05338 -0.02609 -0.05481 407 SER   A CA   
1857 C  C    . SER   A 255 ? 0.45613 0.90956 0.78397 -0.03422 -0.05071 -0.05729 407 SER   A C    
1858 O  O    . SER   A 255 ? 0.45989 0.86335 0.75542 -0.03018 -0.06230 -0.04850 407 SER   A O    
1859 C  CB   . SER   A 255 ? 0.51675 0.98582 0.83652 -0.08530 -0.02332 -0.04576 407 SER   A CB   
1860 O  OG   . SER   A 255 ? 0.65586 1.15081 1.00324 -0.08865 -0.03986 -0.04994 407 SER   A OG   
1861 N  N    . MET   A 256 ? 0.43412 0.93681 0.80461 -0.02242 -0.05921 -0.06866 408 MET   A N    
1862 C  CA   . MET   A 256 ? 0.40987 0.90531 0.78875 -0.00242 -0.08504 -0.06965 408 MET   A CA   
1863 C  C    . MET   A 256 ? 0.41484 0.86484 0.77068 0.02304  -0.09226 -0.06731 408 MET   A C    
1864 O  O    . MET   A 256 ? 0.42024 0.83827 0.75932 0.03271  -0.11284 -0.05927 408 MET   A O    
1865 C  CB   . MET   A 256 ? 0.31003 0.87093 0.74422 0.00949  -0.09238 -0.08377 408 MET   A CB   
1866 C  CG   . MET   A 256 ? 0.42675 1.03161 0.88766 -0.01460 -0.09524 -0.08481 408 MET   A CG   
1867 S  SD   . MET   A 256 ? 0.50844 1.18337 1.03323 0.00538  -0.11402 -0.09998 408 MET   A SD   
1868 C  CE   . MET   A 256 ? 0.50361 1.19642 1.05083 0.03967  -0.10251 -0.11536 408 MET   A CE   
1869 N  N    . LYS   A 257 ? 0.42604 0.87310 0.77997 0.03289  -0.07618 -0.07411 409 LYS   A N    
1870 C  CA   . LYS   A 257 ? 0.37558 0.78033 0.71221 0.05606  -0.08309 -0.07366 409 LYS   A CA   
1871 C  C    . LYS   A 257 ? 0.35547 0.70039 0.64191 0.04506  -0.07880 -0.05920 409 LYS   A C    
1872 O  O    . LYS   A 257 ? 0.43196 0.73637 0.70033 0.06003  -0.08629 -0.05552 409 LYS   A O    
1873 C  CB   . LYS   A 257 ? 0.51827 0.94850 0.87794 0.07319  -0.06928 -0.09159 409 LYS   A CB   
1874 C  CG   . LYS   A 257 ? 0.58132 1.07299 0.99565 0.09043  -0.07417 -0.10924 409 LYS   A CG   
1875 C  CD   . LYS   A 257 ? 0.76453 1.24501 1.19576 0.12491  -0.08423 -0.12234 409 LYS   A CD   
1876 C  CE   . LYS   A 257 ? 0.85716 1.37823 1.31230 0.13487  -0.06277 -0.14584 409 LYS   A CE   
1877 N  NZ   . LYS   A 257 ? 0.90720 1.42518 1.39023 0.17177  -0.07527 -0.16367 409 LYS   A NZ   
1878 N  N    . LEU   A 258 ? 0.38580 0.72437 0.65168 0.01937  -0.06766 -0.05105 410 LEU   A N    
1879 C  CA   . LEU   A 258 ? 0.38109 0.66752 0.60357 0.00984  -0.06458 -0.03847 410 LEU   A CA   
1880 C  C    . LEU   A 258 ? 0.42807 0.68485 0.63071 0.00964  -0.08372 -0.02781 410 LEU   A C    
1881 O  O    . LEU   A 258 ? 0.44044 0.71618 0.66065 0.01536  -0.10021 -0.02916 410 LEU   A O    
1882 C  CB   . LEU   A 258 ? 0.42416 0.71323 0.63400 -0.01530 -0.04743 -0.03403 410 LEU   A CB   
1883 C  CG   . LEU   A 258 ? 0.42621 0.74952 0.65116 -0.01964 -0.02747 -0.04217 410 LEU   A CG   
1884 C  CD1  . LEU   A 258 ? 0.31777 0.63430 0.52423 -0.04534 -0.01354 -0.03266 410 LEU   A CD1  
1885 C  CD2  . LEU   A 258 ? 0.38804 0.69817 0.60624 -0.00068 -0.02213 -0.04961 410 LEU   A CD2  
1886 N  N    . THR   A 259 ? 0.45181 0.66491 0.61745 0.00309  -0.08156 -0.01767 411 THR   A N    
1887 C  CA   . THR   A 259 ? 0.46990 0.65694 0.61126 0.00034  -0.09619 -0.00813 411 THR   A CA   
1888 C  C    . THR   A 259 ? 0.43875 0.62258 0.56609 -0.02164 -0.09119 -0.00621 411 THR   A C    
1889 O  O    . THR   A 259 ? 0.45361 0.64307 0.58362 -0.03470 -0.07600 -0.00811 411 THR   A O    
1890 C  CB   . THR   A 259 ? 0.45291 0.59565 0.56345 0.00767  -0.09750 0.00123  411 THR   A CB   
1891 O  OG1  . THR   A 259 ? 0.50667 0.62979 0.59668 -0.00464 -0.08105 0.00357  411 THR   A OG1  
1892 C  CG2  . THR   A 259 ? 0.39307 0.53229 0.51831 0.02819  -0.10113 -0.00205 411 THR   A CG2  
1893 N  N    . PRO   A 260 ? 0.39894 0.57300 0.51050 -0.02625 -0.10472 -0.00276 412 PRO   A N    
1894 C  CA   . PRO   A 260 ? 0.45563 0.62151 0.55328 -0.04579 -0.10085 -0.00389 412 PRO   A CA   
1895 C  C    . PRO   A 260 ? 0.51854 0.65168 0.59078 -0.05222 -0.08616 0.00048  412 PRO   A C    
1896 O  O    . PRO   A 260 ? 0.38178 0.51300 0.45521 -0.06688 -0.07710 -0.00144 412 PRO   A O    
1897 C  CB   . PRO   A 260 ? 0.47250 0.63217 0.55279 -0.04514 -0.11919 -0.00263 412 PRO   A CB   
1898 C  CG   . PRO   A 260 ? 0.44631 0.62761 0.54627 -0.02884 -0.13477 -0.00172 412 PRO   A CG   
1899 C  CD   . PRO   A 260 ? 0.41708 0.59179 0.52576 -0.01434 -0.12571 0.00087  412 PRO   A CD   
1900 N  N    . LEU   A 261 ? 0.45002 0.55723 0.50099 -0.04208 -0.08463 0.00703  413 LEU   A N    
1901 C  CA   . LEU   A 261 ? 0.40732 0.48764 0.43753 -0.04730 -0.07166 0.01057  413 LEU   A CA   
1902 C  C    . LEU   A 261 ? 0.39923 0.48745 0.44337 -0.05075 -0.05725 0.00913  413 LEU   A C    
1903 O  O    . LEU   A 261 ? 0.50415 0.58115 0.54067 -0.06140 -0.04819 0.01033  413 LEU   A O    
1904 C  CB   . LEU   A 261 ? 0.45427 0.50990 0.46263 -0.03743 -0.07329 0.01821  413 LEU   A CB   
1905 C  CG   . LEU   A 261 ? 0.51201 0.54344 0.50050 -0.04237 -0.06131 0.02143  413 LEU   A CG   
1906 C  CD1  . LEU   A 261 ? 0.42949 0.45275 0.40277 -0.05277 -0.06041 0.01817  413 LEU   A CD1  
1907 C  CD2  . LEU   A 261 ? 0.41606 0.42777 0.38842 -0.03459 -0.06259 0.02955  413 LEU   A CD2  
1908 N  N    . VAL   A 262 ? 0.44213 0.54997 0.50608 -0.04113 -0.05560 0.00619  414 VAL   A N    
1909 C  CA   . VAL   A 262 ? 0.43725 0.55875 0.51230 -0.04487 -0.04138 0.00364  414 VAL   A CA   
1910 C  C    . VAL   A 262 ? 0.47233 0.61275 0.55926 -0.06264 -0.03614 0.00289  414 VAL   A C    
1911 O  O    . VAL   A 262 ? 0.44307 0.57720 0.52315 -0.07346 -0.02525 0.00687  414 VAL   A O    
1912 C  CB   . VAL   A 262 ? 0.42476 0.56955 0.52157 -0.02990 -0.04118 -0.00363 414 VAL   A CB   
1913 C  CG1  . VAL   A 262 ? 0.37142 0.54489 0.48319 -0.03647 -0.02620 -0.00888 414 VAL   A CG1  
1914 C  CG2  . VAL   A 262 ? 0.39687 0.51447 0.47998 -0.01541 -0.04376 -0.00200 414 VAL   A CG2  
1915 N  N    . LEU   A 263 ? 0.40988 0.57278 0.51484 -0.06693 -0.04524 -0.00113 415 LEU   A N    
1916 C  CA   . LEU   A 263 ? 0.46685 0.64687 0.58553 -0.08661 -0.04177 -0.00141 415 LEU   A CA   
1917 C  C    . LEU   A 263 ? 0.50256 0.64816 0.59943 -0.09971 -0.04175 0.00345  415 LEU   A C    
1918 O  O    . LEU   A 263 ? 0.55354 0.69723 0.65288 -0.11563 -0.03424 0.00776  415 LEU   A O    
1919 C  CB   . LEU   A 263 ? 0.50137 0.71264 0.64505 -0.08857 -0.05415 -0.00797 415 LEU   A CB   
1920 C  CG   . LEU   A 263 ? 0.51015 0.76623 0.68650 -0.07816 -0.05316 -0.01486 415 LEU   A CG   
1921 C  CD1  . LEU   A 263 ? 0.47077 0.75711 0.67220 -0.07901 -0.06884 -0.02106 415 LEU   A CD1  
1922 C  CD2  . LEU   A 263 ? 0.50696 0.79075 0.69877 -0.08990 -0.03512 -0.01494 415 LEU   A CD2  
1923 N  N    . GLU   A 264 ? 0.46339 0.58190 0.53894 -0.09308 -0.05028 0.00288  416 GLU   A N    
1924 C  CA   . GLU   A 264 ? 0.55732 0.64454 0.61399 -0.10207 -0.05031 0.00382  416 GLU   A CA   
1925 C  C    . GLU   A 264 ? 0.59198 0.65834 0.63618 -0.10223 -0.03835 0.01086  416 GLU   A C    
1926 O  O    . GLU   A 264 ? 0.59497 0.64702 0.63778 -0.11422 -0.03505 0.01402  416 GLU   A O    
1927 C  CB   . GLU   A 264 ? 0.61260 0.68250 0.64828 -0.09381 -0.06008 0.00010  416 GLU   A CB   
1928 C  CG   . GLU   A 264 ? 0.74248 0.79128 0.76593 -0.10330 -0.06431 -0.00601 416 GLU   A CG   
1929 C  CD   . GLU   A 264 ? 0.85159 0.88641 0.84945 -0.09467 -0.07015 -0.00991 416 GLU   A CD   
1930 O  OE1  . GLU   A 264 ? 0.82666 0.84408 0.80766 -0.08746 -0.06273 -0.00603 416 GLU   A OE1  
1931 O  OE2  . GLU   A 264 ? 0.84609 0.89000 0.84027 -0.09608 -0.08215 -0.01668 416 GLU   A OE2  
1932 N  N    . VAL   A 265 ? 0.55876 0.62201 0.59456 -0.08920 -0.03344 0.01368  417 VAL   A N    
1933 C  CA   . VAL   A 265 ? 0.55489 0.59954 0.57780 -0.08842 -0.02428 0.01955  417 VAL   A CA   
1934 C  C    . VAL   A 265 ? 0.58020 0.64102 0.61351 -0.09671 -0.01486 0.02420  417 VAL   A C    
1935 O  O    . VAL   A 265 ? 0.62164 0.66916 0.64944 -0.10670 -0.01092 0.03084  417 VAL   A O    
1936 C  CB   . VAL   A 265 ? 0.46469 0.50020 0.47543 -0.07384 -0.02348 0.02021  417 VAL   A CB   
1937 C  CG1  . VAL   A 265 ? 0.45997 0.48378 0.46171 -0.07336 -0.01471 0.02513  417 VAL   A CG1  
1938 C  CG2  . VAL   A 265 ? 0.41924 0.43742 0.41427 -0.06940 -0.03049 0.01873  417 VAL   A CG2  
1939 N  N    . PHE   A 266 ? 0.50281 0.59339 0.55097 -0.09240 -0.01141 0.02083  418 PHE   A N    
1940 C  CA   . PHE   A 266 ? 0.51286 0.62490 0.56802 -0.09979 -0.00024 0.02392  418 PHE   A CA   
1941 C  C    . PHE   A 266 ? 0.62085 0.75041 0.69065 -0.11939 0.00174  0.02792  418 PHE   A C    
1942 O  O    . PHE   A 266 ? 0.69513 0.83479 0.76370 -0.13111 0.01128  0.03539  418 PHE   A O    
1943 C  CB   . PHE   A 266 ? 0.52409 0.66483 0.59191 -0.08676 0.00369  0.01532  418 PHE   A CB   
1944 C  CG   . PHE   A 266 ? 0.52830 0.65076 0.58147 -0.07150 0.00414  0.01293  418 PHE   A CG   
1945 C  CD1  . PHE   A 266 ? 0.58491 0.72354 0.64878 -0.05654 0.00456  0.00310  418 PHE   A CD1  
1946 C  CD2  . PHE   A 266 ? 0.65471 0.74411 0.68605 -0.07210 0.00338  0.01951  418 PHE   A CD2  
1947 C  CE1  . PHE   A 266 ? 0.64916 0.76754 0.70062 -0.04442 0.00365  0.00055  418 PHE   A CE1  
1948 C  CE2  . PHE   A 266 ? 0.63611 0.71041 0.65625 -0.06070 0.00335  0.01743  418 PHE   A CE2  
1949 C  CZ   . PHE   A 266 ? 0.73582 0.82268 0.76519 -0.04785 0.00321  0.00829  418 PHE   A CZ   
1950 N  N    . GLY   A 267 ? 0.64385 0.77781 0.72642 -0.12477 -0.00748 0.02384  419 GLY   A N    
1951 C  CA   . GLY   A 267 ? 0.71748 0.86427 0.81538 -0.14599 -0.00755 0.02751  419 GLY   A CA   
1952 C  C    . GLY   A 267 ? 0.90075 1.09265 1.02833 -0.14818 -0.00925 0.01954  419 GLY   A C    
1953 O  O    . GLY   A 267 ? 0.78243 0.99843 0.92033 -0.13183 -0.00900 0.01146  419 GLY   A O    
1954 N  N    . ASN   A 268 ? 1.07185 1.27433 1.21550 -0.16899 -0.01216 0.02167  420 ASN   A N    
1955 C  CA   . ASN   A 268 ? 1.13295 1.38267 1.30962 -0.17499 -0.01459 0.01430  420 ASN   A CA   
1956 C  C    . ASN   A 268 ? 1.06751 1.35353 1.26214 -0.19606 -0.00043 0.02149  420 ASN   A C    
1957 O  O    . ASN   A 268 ? 0.93958 1.24455 1.15565 -0.21759 -0.00303 0.02301  420 ASN   A O    
1958 C  CB   . ASN   A 268 ? 1.12510 1.36528 1.30989 -0.18430 -0.03099 0.00881  420 ASN   A CB   
1959 C  CG   . ASN   A 268 ? 1.11120 1.33943 1.28635 -0.16305 -0.04505 -0.00079 420 ASN   A CG   
1960 O  OD1  . ASN   A 268 ? 1.10433 1.29468 1.25121 -0.15111 -0.04684 0.00062  420 ASN   A OD1  
1961 N  ND2  . ASN   A 268 ? 1.05834 1.32105 1.25728 -0.15900 -0.05551 -0.00968 420 ASN   A ND2  
1962 N  N    . LYS   B 1   ? 1.47707 1.64374 1.57870 -0.17723 -0.20497 0.29337  625 LYS   C N    
1963 C  CA   . LYS   B 1   ? 1.57534 1.63333 1.61522 -0.16283 -0.21421 0.29049  625 LYS   C CA   
1964 C  C    . LYS   B 1   ? 1.65449 1.63015 1.66008 -0.13045 -0.23895 0.24094  625 LYS   C C    
1965 O  O    . LYS   B 1   ? 1.75855 1.67124 1.71957 -0.09525 -0.24150 0.22353  625 LYS   C O    
1966 C  CB   . LYS   B 1   ? 1.62628 1.61847 1.64964 -0.21870 -0.23203 0.33024  625 LYS   C CB   
1967 C  CG   . LYS   B 1   ? 1.60629 1.67665 1.65501 -0.25575 -0.20146 0.38737  625 LYS   C CG   
1968 C  CD   . LYS   B 1   ? 1.55227 1.72209 1.60739 -0.20731 -0.15834 0.39072  625 LYS   C CD   
1969 C  CE   . LYS   B 1   ? 1.52866 1.63629 1.51967 -0.14645 -0.15288 0.36995  625 LYS   C CE   
1970 N  NZ   . LYS   B 1   ? 1.38688 1.59009 1.38985 -0.09615 -0.11925 0.35886  625 LYS   C NZ   
1971 N  N    . ASN   B 2   ? 1.59521 1.57679 1.62015 -0.13992 -0.25765 0.21743  626 ASN   C N    
1972 C  CA   . ASN   B 2   ? 1.52657 1.46556 1.52452 -0.10189 -0.26856 0.16981  626 ASN   C CA   
1973 C  C    . ASN   B 2   ? 1.32259 1.34451 1.34492 -0.07090 -0.24096 0.15515  626 ASN   C C    
1974 O  O    . ASN   B 2   ? 1.31647 1.42077 1.37881 -0.08281 -0.22818 0.17443  626 ASN   C O    
1975 C  CB   . ASN   B 2   ? 1.61281 1.49047 1.59849 -0.12502 -0.30893 0.15023  626 ASN   C CB   
1976 C  CG   . ASN   B 2   ? 1.77890 1.53529 1.71210 -0.12565 -0.34033 0.14028  626 ASN   C CG   
1977 O  OD1  . ASN   B 2   ? 1.85923 1.57978 1.76808 -0.11559 -0.33292 0.15604  626 ASN   C OD1  
1978 N  ND2  . ASN   B 2   ? 1.80579 1.49393 1.71331 -0.12977 -0.37787 0.11087  626 ASN   C ND2  
1979 N  N    . HIS   B 3   ? 1.15510 1.15452 1.15258 -0.03064 -0.23256 0.12071  627 HIS   C N    
1980 C  CA   . HIS   B 3   ? 0.96408 1.02101 0.97363 0.00067  -0.20259 0.11042  627 HIS   C CA   
1981 C  C    . HIS   B 3   ? 0.90723 0.95009 0.90131 0.01620  -0.20500 0.07857  627 HIS   C C    
1982 O  O    . HIS   B 3   ? 0.82539 0.84244 0.79887 0.04104  -0.19657 0.05099  627 HIS   C O    
1983 C  CB   . HIS   B 3   ? 0.87130 0.92147 0.86808 0.02982  -0.18505 0.10376  627 HIS   C CB   
1984 C  CG   . HIS   B 3   ? 0.85626 0.88079 0.84093 0.01850  -0.19165 0.12953  627 HIS   C CG   
1985 N  ND1  . HIS   B 3   ? 0.90221 0.97900 0.90074 0.01398  -0.17313 0.16224  627 HIS   C ND1  
1986 C  CD2  . HIS   B 3   ? 0.96329 0.91044 0.91535 0.01305  -0.21496 0.12916  627 HIS   C CD2  
1987 C  CE1  . HIS   B 3   ? 1.00308 1.03595 0.97634 0.00229  -0.18195 0.18480  627 HIS   C CE1  
1988 N  NE2  . HIS   B 3   ? 1.02349 0.97122 0.96701 0.00173  -0.20941 0.16547  627 HIS   C NE2  
1989 N  N    . PRO   B 4   ? 0.87430 0.93890 0.87717 0.00233  -0.21630 0.08185  628 PRO   C N    
1990 C  CA   . PRO   B 4   ? 0.94003 0.98687 0.91549 0.01858  -0.21779 0.05524  628 PRO   C CA   
1991 C  C    . PRO   B 4   ? 0.86215 0.93714 0.83400 0.04463  -0.18668 0.04959  628 PRO   C C    
1992 O  O    . PRO   B 4   ? 0.82536 0.87593 0.76873 0.05960  -0.17679 0.02712  628 PRO   C O    
1993 C  CB   . PRO   B 4   ? 0.89816 0.96323 0.88301 -0.00260 -0.24372 0.06345  628 PRO   C CB   
1994 C  CG   . PRO   B 4   ? 0.88613 1.01536 0.91932 -0.02252 -0.24008 0.09638  628 PRO   C CG   
1995 C  CD   . PRO   B 4   ? 0.88268 0.99352 0.92028 -0.02876 -0.22961 0.10928  628 PRO   C CD   
1996 N  N    . MET   B 5   ? 0.77025 0.89451 0.76754 0.05020  -0.17097 0.06923  629 MET   C N    
1997 C  CA   . MET   B 5   ? 0.66717 0.80117 0.65523 0.07385  -0.14651 0.06314  629 MET   C CA   
1998 C  C    . MET   B 5   ? 0.65345 0.76676 0.63748 0.08540  -0.12862 0.04543  629 MET   C C    
1999 O  O    . MET   B 5   ? 0.63412 0.73076 0.60179 0.09412  -0.11283 0.02899  629 MET   C O    
2000 C  CB   . MET   B 5   ? 0.62436 0.81233 0.63571 0.08421  -0.13960 0.08392  629 MET   C CB   
2001 C  CG   . MET   B 5   ? 0.71567 0.93814 0.73463 0.08102  -0.15659 0.09610  629 MET   C CG   
2002 S  SD   . MET   B 5   ? 0.83158 1.13424 0.88284 0.10231  -0.14873 0.11636  629 MET   C SD   
2003 C  CE   . MET   B 5   ? 0.84128 1.19349 0.93708 0.07308  -0.14966 0.13834  629 MET   C CE   
2004 N  N    . LEU   B 6   ? 0.62462 0.74088 0.62301 0.08434  -0.13136 0.04936  630 LEU   C N    
2005 C  CA   . LEU   B 6   ? 0.74709 0.84873 0.74377 0.09870  -0.12131 0.02815  630 LEU   C CA   
2006 C  C    . LEU   B 6   ? 0.73831 0.80679 0.71802 0.09968  -0.12610 0.00084  630 LEU   C C    
2007 O  O    . LEU   B 6   ? 0.72241 0.79427 0.70453 0.11041  -0.11102 -0.02266 630 LEU   C O    
2008 C  CB   . LEU   B 6   ? 0.61989 0.72537 0.62368 0.10181  -0.12796 0.04014  630 LEU   C CB   
2009 C  CG   . LEU   B 6   ? 0.77499 0.86685 0.77526 0.12139  -0.12710 0.01850  630 LEU   C CG   
2010 C  CD1  . LEU   B 6   ? 0.69939 0.80913 0.71094 0.13586  -0.10916 -0.00587 630 LEU   C CD1  
2011 C  CD2  . LEU   B 6   ? 0.75484 0.85376 0.75121 0.12738  -0.13138 0.04018  630 LEU   C CD2  
2012 N  N    . MET   B 7   ? 0.69646 0.73693 0.66018 0.08871  -0.14767 0.00138  631 MET   C N    
2013 C  CA   . MET   B 7   ? 0.72165 0.73118 0.66259 0.09792  -0.15460 -0.02839 631 MET   C CA   
2014 C  C    . MET   B 7   ? 0.82719 0.84728 0.75219 0.10123  -0.13522 -0.04176 631 MET   C C    
2015 O  O    . MET   B 7   ? 0.71055 0.73667 0.63081 0.11363  -0.12026 -0.06778 631 MET   C O    
2016 C  CB   . MET   B 7   ? 0.80225 0.76654 0.72267 0.08706  -0.18844 -0.02671 631 MET   C CB   
2017 C  CG   . MET   B 7   ? 1.06095 0.98155 0.95868 0.10687  -0.20488 -0.05608 631 MET   C CG   
2018 S  SD   . MET   B 7   ? 1.30946 1.15255 1.17568 0.09191  -0.25237 -0.05362 631 MET   C SD   
2019 C  CE   . MET   B 7   ? 1.23207 1.08618 1.12818 0.05467  -0.25761 -0.00371 631 MET   C CE   
2020 N  N    A ASN   B 8   ? 0.70702 0.73304 0.62212 0.09120  -0.13502 -0.02337 632 ASN   C N    
2021 N  N    B ASN   B 8   ? 0.70674 0.73303 0.62183 0.09134  -0.13451 -0.02352 632 ASN   C N    
2022 C  CA   A ASN   B 8   ? 0.75516 0.78125 0.64232 0.09456  -0.11605 -0.02902 632 ASN   C CA   
2023 C  CA   B ASN   B 8   ? 0.75601 0.78169 0.64264 0.09502  -0.11549 -0.03052 632 ASN   C CA   
2024 C  C    A ASN   B 8   ? 0.75015 0.79406 0.65118 0.09632  -0.08353 -0.03116 632 ASN   C C    
2025 C  C    B ASN   B 8   ? 0.75425 0.79796 0.65441 0.09611  -0.08317 -0.03033 632 ASN   C C    
2026 O  O    A ASN   B 8   ? 0.76464 0.80892 0.64797 0.09582  -0.06072 -0.04313 632 ASN   C O    
2027 O  O    B ASN   B 8   ? 0.77555 0.81806 0.65576 0.09500  -0.06020 -0.03974 632 ASN   C O    
2028 C  CB   A ASN   B 8   ? 0.76744 0.79318 0.63772 0.08929  -0.12822 -0.00757 632 ASN   C CB   
2029 C  CB   B ASN   B 8   ? 0.78002 0.80141 0.64472 0.08995  -0.12917 -0.01172 632 ASN   C CB   
2030 C  CG   A ASN   B 8   ? 0.84935 0.86408 0.67776 0.09523  -0.10897 -0.00677 632 ASN   C CG   
2031 C  CG   B ASN   B 8   ? 0.88474 0.88134 0.70198 0.09507  -0.14014 -0.02706 632 ASN   C CG   
2032 O  OD1  A ASN   B 8   ? 0.76395 0.78084 0.59136 0.09661  -0.08946 0.00675  632 ASN   C OD1  
2033 O  OD1  B ASN   B 8   ? 0.90751 0.89826 0.68671 0.10097  -0.12567 -0.02380 632 ASN   C OD1  
2034 N  ND2  A ASN   B 8   ? 0.91761 0.91311 0.70332 0.10030  -0.11568 -0.02078 632 ASN   C ND2  
2035 N  ND2  B ASN   B 8   ? 0.82461 0.79888 0.63572 0.09499  -0.16743 -0.04397 632 ASN   C ND2  
2036 N  N    . LEU   B 9   ? 0.66743 0.72665 0.59861 0.09675  -0.08097 -0.01985 633 LEU   C N    
2037 C  CA   . LEU   B 9   ? 0.73968 0.80847 0.68622 0.09673  -0.05718 -0.02669 633 LEU   C CA   
2038 C  C    . LEU   B 9   ? 0.71236 0.79800 0.67994 0.09928  -0.04802 -0.05637 633 LEU   C C    
2039 O  O    . LEU   B 9   ? 0.68570 0.78449 0.66844 0.09195  -0.02661 -0.06785 633 LEU   C O    
2040 C  CB   . LEU   B 9   ? 0.71653 0.79676 0.68428 0.10384  -0.06177 -0.01304 633 LEU   C CB   
2041 C  CG   . LEU   B 9   ? 0.82454 0.90064 0.77658 0.10849  -0.06561 0.01158  633 LEU   C CG   
2042 C  CD1  . LEU   B 9   ? 0.61705 0.71529 0.58926 0.12304  -0.06960 0.02059  633 LEU   C CD1  
2043 C  CD2  . LEU   B 9   ? 0.79610 0.84103 0.71740 0.10484  -0.04891 0.01396  633 LEU   C CD2  
2044 N  N    . LEU   B 10  ? 0.82112 0.90582 0.79039 0.10960  -0.06620 -0.07001 634 LEU   C N    
2045 C  CA   . LEU   B 10  ? 0.87162 0.97610 0.85588 0.12158  -0.06246 -0.10278 634 LEU   C CA   
2046 C  C    . LEU   B 10  ? 1.03789 1.14319 0.99551 0.12535  -0.05451 -0.12019 634 LEU   C C    
2047 O  O    . LEU   B 10  ? 1.11392 1.24435 1.08267 0.14161  -0.05179 -0.15110 634 LEU   C O    
2048 C  CB   . LEU   B 10  ? 0.76172 0.85312 0.75165 0.13942  -0.09077 -0.10924 634 LEU   C CB   
2049 C  CG   . LEU   B 10  ? 0.71940 0.81267 0.72626 0.14147  -0.09884 -0.09203 634 LEU   C CG   
2050 C  CD1  . LEU   B 10  ? 0.79419 0.85705 0.78746 0.15401  -0.12734 -0.08686 634 LEU   C CD1  
2051 C  CD2  . LEU   B 10  ? 0.72402 0.85328 0.76343 0.14799  -0.08490 -0.11254 634 LEU   C CD2  
2052 N  N    . LYS   B 11  ? 1.10446 1.18729 1.02450 0.11607  -0.05217 -0.10336 635 LYS   C N    
2053 C  CA   . LYS   B 11  ? 1.14625 1.22490 1.02675 0.12425  -0.04738 -0.11860 635 LYS   C CA   
2054 C  C    . LYS   B 11  ? 1.20284 1.26140 1.07041 0.14750  -0.07840 -0.14310 635 LYS   C C    
2055 O  O    . LYS   B 11  ? 1.23566 1.25105 1.07587 0.14743  -0.10943 -0.13490 635 LYS   C O    
2056 C  CB   . LYS   B 11  ? 1.16584 1.28941 1.05431 0.12006  -0.00719 -0.13484 635 LYS   C CB   
2057 C  CG   . LYS   B 11  ? 1.20308 1.33096 1.10067 0.09271  0.02195  -0.11115 635 LYS   C CG   
2058 C  CD   . LYS   B 11  ? 1.25998 1.44301 1.19786 0.07984  0.05594  -0.13025 635 LYS   C CD   
2059 C  CE   . LYS   B 11  ? 1.28338 1.45913 1.19998 0.04876  0.09272  -0.10757 635 LYS   C CE   
2060 N  NZ   . LYS   B 11  ? 1.27102 1.50165 1.18698 0.04076  0.13062  -0.12390 635 LYS   C NZ   
2061 C  C10  . A1L7X C .   ? 0.60303 0.72938 0.66571 0.01441  0.01203  -0.05765 501 A1L7X A C10  
2062 C  C13  . A1L7X C .   ? 0.63265 0.76130 0.73528 0.05425  -0.00114 -0.09014 501 A1L7X A C13  
2063 C  C15  . A1L7X C .   ? 0.75599 0.82023 0.80101 0.04599  0.00267  -0.10647 501 A1L7X A C15  
2064 C  C20  . A1L7X C .   ? 0.73280 0.58592 0.72859 0.01121  -0.06525 0.01711  501 A1L7X A C20  
2065 C  C21  . A1L7X C .   ? 0.71063 0.54560 0.68858 -0.00269 -0.06768 0.03765  501 A1L7X A C21  
2066 C  C22  . A1L7X C .   ? 0.75095 0.60959 0.71734 -0.01360 -0.05590 0.04255  501 A1L7X A C22  
2067 C  C24  . A1L7X C .   ? 0.54149 0.78374 0.67180 -0.00205 0.02090  -0.05491 501 A1L7X A C24  
2068 C  C26  . A1L7X C .   ? 0.46836 0.67700 0.58779 -0.00826 0.00805  -0.03925 501 A1L7X A C26  
2069 C  C28  . A1L7X C .   ? 0.53349 0.72967 0.66641 0.01037  -0.00828 -0.04310 501 A1L7X A C28  
2070 C  C01  . A1L7X C .   ? 0.61714 0.54275 0.65967 0.04853  -0.04610 -0.05888 501 A1L7X A C01  
2071 C  C02  . A1L7X C .   ? 0.62146 0.54909 0.65285 0.03621  -0.04458 -0.03850 501 A1L7X A C02  
2072 C  C03  . A1L7X C .   ? 0.59473 0.55583 0.62737 0.03163  -0.03525 -0.03659 501 A1L7X A C03  
2073 C  C04  . A1L7X C .   ? 0.63260 0.62808 0.67681 0.03723  -0.02615 -0.05228 501 A1L7X A C04  
2074 C  C05  . A1L7X C .   ? 0.59171 0.59111 0.64579 0.04952  -0.02550 -0.07281 501 A1L7X A C05  
2075 C  C06  . A1L7X C .   ? 0.60460 0.56742 0.65787 0.05604  -0.03603 -0.07741 501 A1L7X A C06  
2076 C  C08  . A1L7X C .   ? 0.67215 0.77085 0.74756 0.04371  -0.00006 -0.08245 501 A1L7X A C08  
2077 C  C09  . A1L7X C .   ? 0.60100 0.70137 0.65740 0.02441  0.00676  -0.06621 501 A1L7X A C09  
2078 C  C11  . A1L7X C .   ? 0.52117 0.67769 0.61016 0.02246  0.01141  -0.06530 501 A1L7X A C11  
2079 C  C12  . A1L7X C .   ? 0.55281 0.71244 0.66257 0.04322  0.00485  -0.08169 501 A1L7X A C12  
2080 C  C14  . A1L7X C .   ? 0.75349 0.81479 0.85536 0.08424  -0.01847 -0.12008 501 A1L7X A C14  
2081 C  C18  . A1L7X C .   ? 0.64059 0.50473 0.65602 0.02601  -0.05977 -0.01905 501 A1L7X A C18  
2082 C  C19  . A1L7X C .   ? 0.69958 0.54708 0.69801 0.01020  -0.06091 0.00283  501 A1L7X A C19  
2083 C  C23  . A1L7X C .   ? 0.52722 0.74728 0.65256 0.01659  0.01684  -0.06648 501 A1L7X A C23  
2084 C  C25  . A1L7X C .   ? 0.51248 0.80233 0.67926 0.00546  0.02169  -0.06712 501 A1L7X A C25  
2085 C  C27  . A1L7X C .   ? 0.48355 0.79711 0.65866 -0.01538 0.02481  -0.05639 501 A1L7X A C27  
2086 C  C33  . A1L7X C .   ? 0.67652 0.63768 0.69786 0.01941  -0.03462 -0.01806 501 A1L7X A C33  
2087 C  C37  . A1L7X C .   ? 0.59745 0.71958 0.64070 -0.00536 0.01750  -0.04072 501 A1L7X A C37  
2088 F  F34  . A1L7X C .   ? 0.74761 0.70041 0.75215 0.00651  -0.02894 -0.01094 501 A1L7X A F34  
2089 F  F35  . A1L7X C .   ? 0.71933 0.66000 0.73967 0.02203  -0.04613 -0.00685 501 A1L7X A F35  
2090 F  F36  . A1L7X C .   ? 0.73411 0.72591 0.76265 0.01746  -0.02836 -0.01951 501 A1L7X A F36  
2091 F  F38  . A1L7X C .   ? 0.56698 0.65996 0.59016 -0.00879 0.01519  -0.03532 501 A1L7X A F38  
2092 F  F39  . A1L7X C .   ? 0.50824 0.62467 0.55498 -0.01142 0.01196  -0.02875 501 A1L7X A F39  
2093 F  F40  . A1L7X C .   ? 0.54367 0.69796 0.58580 -0.01402 0.03003  -0.04365 501 A1L7X A F40  
2094 O  O16  . A1L7X C .   ? 0.48396 0.66597 0.57968 0.00931  0.01617  -0.05651 501 A1L7X A O16  
2095 O  O17  . A1L7X C .   ? 0.61379 0.51219 0.63285 0.02741  -0.05180 -0.02038 501 A1L7X A O17  
2096 O  O29  . A1L7X C .   ? 0.49888 0.75064 0.61215 -0.02003 0.03459  -0.04845 501 A1L7X A O29  
2097 O  O30  . A1L7X C .   ? 0.58044 0.46252 0.55202 -0.01218 -0.04720 0.03210  501 A1L7X A O30  
2098 O  O31  . A1L7X C .   ? 0.67672 0.53086 0.62866 -0.02372 -0.05522 0.05643  501 A1L7X A O31  
2099 O  O32  . A1L7X C .   ? 0.68825 0.55243 0.67590 -0.00225 -0.04906 0.00406  501 A1L7X A O32  
2100 SI SI07 . A1L7X C .   ? 0.69764 0.75343 0.76586 0.05537  -0.00970 -0.09461 501 A1L7X A SI07 
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