data_9M16
# 
_entry.id   9M16 
# 
_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   9M16         pdb_00009m16 10.2210/pdb9m16/pdb 
WWPDB D_1300056756 ?            ?                   
# 
_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                        9M16 
_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)-2,3-dimethyl-phenyl]-dimethyl-silyl]-2,3-dimethyl-phenoxy]-4-oxidanyl-pentanoic acid' 
516.742   1   ? ? ? ? 
4 water       nat water 18.015    209 ? ? ? ? 
# 
_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)-2,3-dimethyl-phenyl]-dimethyl-silyl]-2,3-dimethyl-phenoxy]-4-oxidanyl-pentanoic acid' 
A1L74 
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 
A1L74 non-polymer         . 
'(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)-2,3-dimethyl-phenyl]-dimethyl-silyl]-2,3-dimethyl-phenoxy]-4-oxidanyl-pentanoic acid' 
? 'C29 H44 O6 Si'  516.742 
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        A1L74 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L74 
_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 A1L74 1   501 501 A1L74 LIG A . 
D 4 HOH   1   601 46  HOH   HOH A . 
D 4 HOH   2   602 71  HOH   HOH A . 
D 4 HOH   3   603 68  HOH   HOH A . 
D 4 HOH   4   604 172 HOH   HOH A . 
D 4 HOH   5   605 111 HOH   HOH A . 
D 4 HOH   6   606 190 HOH   HOH A . 
D 4 HOH   7   607 225 HOH   HOH A . 
D 4 HOH   8   608 15  HOH   HOH A . 
D 4 HOH   9   609 208 HOH   HOH A . 
D 4 HOH   10  610 110 HOH   HOH A . 
D 4 HOH   11  611 52  HOH   HOH A . 
D 4 HOH   12  612 28  HOH   HOH A . 
D 4 HOH   13  613 78  HOH   HOH A . 
D 4 HOH   14  614 49  HOH   HOH A . 
D 4 HOH   15  615 43  HOH   HOH A . 
D 4 HOH   16  616 202 HOH   HOH A . 
D 4 HOH   17  617 51  HOH   HOH A . 
D 4 HOH   18  618 164 HOH   HOH A . 
D 4 HOH   19  619 83  HOH   HOH A . 
D 4 HOH   20  620 39  HOH   HOH A . 
D 4 HOH   21  621 76  HOH   HOH A . 
D 4 HOH   22  622 62  HOH   HOH A . 
D 4 HOH   23  623 75  HOH   HOH A . 
D 4 HOH   24  624 9   HOH   HOH A . 
D 4 HOH   25  625 200 HOH   HOH A . 
D 4 HOH   26  626 174 HOH   HOH A . 
D 4 HOH   27  627 23  HOH   HOH A . 
D 4 HOH   28  628 107 HOH   HOH A . 
D 4 HOH   29  629 93  HOH   HOH A . 
D 4 HOH   30  630 35  HOH   HOH A . 
D 4 HOH   31  631 113 HOH   HOH A . 
D 4 HOH   32  632 100 HOH   HOH A . 
D 4 HOH   33  633 121 HOH   HOH A . 
D 4 HOH   34  634 65  HOH   HOH A . 
D 4 HOH   35  635 44  HOH   HOH A . 
D 4 HOH   36  636 21  HOH   HOH A . 
D 4 HOH   37  637 117 HOH   HOH A . 
D 4 HOH   38  638 67  HOH   HOH A . 
D 4 HOH   39  639 11  HOH   HOH A . 
D 4 HOH   40  640 8   HOH   HOH A . 
D 4 HOH   41  641 5   HOH   HOH A . 
D 4 HOH   42  642 26  HOH   HOH A . 
D 4 HOH   43  643 19  HOH   HOH A . 
D 4 HOH   44  644 63  HOH   HOH A . 
D 4 HOH   45  645 64  HOH   HOH A . 
D 4 HOH   46  646 74  HOH   HOH A . 
D 4 HOH   47  647 82  HOH   HOH A . 
D 4 HOH   48  648 20  HOH   HOH A . 
D 4 HOH   49  649 10  HOH   HOH A . 
D 4 HOH   50  650 214 HOH   HOH A . 
D 4 HOH   51  651 185 HOH   HOH A . 
D 4 HOH   52  652 142 HOH   HOH A . 
D 4 HOH   53  653 187 HOH   HOH A . 
D 4 HOH   54  654 6   HOH   HOH A . 
D 4 HOH   55  655 205 HOH   HOH A . 
D 4 HOH   56  656 2   HOH   HOH A . 
D 4 HOH   57  657 33  HOH   HOH A . 
D 4 HOH   58  658 13  HOH   HOH A . 
D 4 HOH   59  659 25  HOH   HOH A . 
D 4 HOH   60  660 32  HOH   HOH A . 
D 4 HOH   61  661 27  HOH   HOH A . 
D 4 HOH   62  662 86  HOH   HOH A . 
D 4 HOH   63  663 3   HOH   HOH A . 
D 4 HOH   64  664 57  HOH   HOH A . 
D 4 HOH   65  665 22  HOH   HOH A . 
D 4 HOH   66  666 221 HOH   HOH A . 
D 4 HOH   67  667 34  HOH   HOH A . 
D 4 HOH   68  668 177 HOH   HOH A . 
D 4 HOH   69  669 162 HOH   HOH A . 
D 4 HOH   70  670 59  HOH   HOH A . 
D 4 HOH   71  671 126 HOH   HOH A . 
D 4 HOH   72  672 219 HOH   HOH A . 
D 4 HOH   73  673 72  HOH   HOH A . 
D 4 HOH   74  674 38  HOH   HOH A . 
D 4 HOH   75  675 29  HOH   HOH A . 
D 4 HOH   76  676 60  HOH   HOH A . 
D 4 HOH   77  677 42  HOH   HOH A . 
D 4 HOH   78  678 137 HOH   HOH A . 
D 4 HOH   79  679 115 HOH   HOH A . 
D 4 HOH   80  680 47  HOH   HOH A . 
D 4 HOH   81  681 81  HOH   HOH A . 
D 4 HOH   82  682 45  HOH   HOH A . 
D 4 HOH   83  683 41  HOH   HOH A . 
D 4 HOH   84  684 95  HOH   HOH A . 
D 4 HOH   85  685 53  HOH   HOH A . 
D 4 HOH   86  686 89  HOH   HOH A . 
D 4 HOH   87  687 186 HOH   HOH A . 
D 4 HOH   88  688 128 HOH   HOH A . 
D 4 HOH   89  689 69  HOH   HOH A . 
D 4 HOH   90  690 66  HOH   HOH A . 
D 4 HOH   91  691 7   HOH   HOH A . 
D 4 HOH   92  692 99  HOH   HOH A . 
D 4 HOH   93  693 192 HOH   HOH A . 
D 4 HOH   94  694 114 HOH   HOH A . 
D 4 HOH   95  695 48  HOH   HOH A . 
D 4 HOH   96  696 1   HOH   HOH A . 
D 4 HOH   97  697 24  HOH   HOH A . 
D 4 HOH   98  698 104 HOH   HOH A . 
D 4 HOH   99  699 118 HOH   HOH A . 
D 4 HOH   100 700 16  HOH   HOH A . 
D 4 HOH   101 701 224 HOH   HOH A . 
D 4 HOH   102 702 87  HOH   HOH A . 
D 4 HOH   103 703 206 HOH   HOH A . 
D 4 HOH   104 704 150 HOH   HOH A . 
D 4 HOH   105 705 129 HOH   HOH A . 
D 4 HOH   106 706 70  HOH   HOH A . 
D 4 HOH   107 707 132 HOH   HOH A . 
D 4 HOH   108 708 4   HOH   HOH A . 
D 4 HOH   109 709 54  HOH   HOH A . 
D 4 HOH   110 710 127 HOH   HOH A . 
D 4 HOH   111 711 173 HOH   HOH A . 
D 4 HOH   112 712 204 HOH   HOH A . 
D 4 HOH   113 713 199 HOH   HOH A . 
D 4 HOH   114 714 155 HOH   HOH A . 
D 4 HOH   115 715 195 HOH   HOH A . 
D 4 HOH   116 716 12  HOH   HOH A . 
D 4 HOH   117 717 73  HOH   HOH A . 
D 4 HOH   118 718 120 HOH   HOH A . 
D 4 HOH   119 719 61  HOH   HOH A . 
D 4 HOH   120 720 201 HOH   HOH A . 
D 4 HOH   121 721 97  HOH   HOH A . 
D 4 HOH   122 722 133 HOH   HOH A . 
D 4 HOH   123 723 103 HOH   HOH A . 
D 4 HOH   124 724 18  HOH   HOH A . 
D 4 HOH   125 725 109 HOH   HOH A . 
D 4 HOH   126 726 130 HOH   HOH A . 
D 4 HOH   127 727 90  HOH   HOH A . 
D 4 HOH   128 728 215 HOH   HOH A . 
D 4 HOH   129 729 98  HOH   HOH A . 
D 4 HOH   130 730 84  HOH   HOH A . 
D 4 HOH   131 731 17  HOH   HOH A . 
D 4 HOH   132 732 231 HOH   HOH A . 
D 4 HOH   133 733 14  HOH   HOH A . 
D 4 HOH   134 734 141 HOH   HOH A . 
D 4 HOH   135 735 151 HOH   HOH A . 
D 4 HOH   136 736 213 HOH   HOH A . 
D 4 HOH   137 737 119 HOH   HOH A . 
D 4 HOH   138 738 88  HOH   HOH A . 
D 4 HOH   139 739 196 HOH   HOH A . 
D 4 HOH   140 740 50  HOH   HOH A . 
D 4 HOH   141 741 138 HOH   HOH A . 
D 4 HOH   142 742 233 HOH   HOH A . 
D 4 HOH   143 743 106 HOH   HOH A . 
D 4 HOH   144 744 125 HOH   HOH A . 
D 4 HOH   145 745 135 HOH   HOH A . 
D 4 HOH   146 746 207 HOH   HOH A . 
D 4 HOH   147 747 158 HOH   HOH A . 
D 4 HOH   148 748 101 HOH   HOH A . 
D 4 HOH   149 749 211 HOH   HOH A . 
D 4 HOH   150 750 152 HOH   HOH A . 
D 4 HOH   151 751 166 HOH   HOH A . 
D 4 HOH   152 752 189 HOH   HOH A . 
D 4 HOH   153 753 170 HOH   HOH A . 
D 4 HOH   154 754 80  HOH   HOH A . 
D 4 HOH   155 755 229 HOH   HOH A . 
D 4 HOH   156 756 56  HOH   HOH A . 
D 4 HOH   157 757 148 HOH   HOH A . 
D 4 HOH   158 758 91  HOH   HOH A . 
D 4 HOH   159 759 176 HOH   HOH A . 
D 4 HOH   160 760 40  HOH   HOH A . 
D 4 HOH   161 761 223 HOH   HOH A . 
D 4 HOH   162 762 210 HOH   HOH A . 
D 4 HOH   163 763 37  HOH   HOH A . 
D 4 HOH   164 764 139 HOH   HOH A . 
D 4 HOH   165 765 198 HOH   HOH A . 
D 4 HOH   166 766 30  HOH   HOH A . 
D 4 HOH   167 767 55  HOH   HOH A . 
D 4 HOH   168 768 209 HOH   HOH A . 
D 4 HOH   169 769 222 HOH   HOH A . 
D 4 HOH   170 770 236 HOH   HOH A . 
D 4 HOH   171 771 144 HOH   HOH A . 
D 4 HOH   172 772 220 HOH   HOH A . 
D 4 HOH   173 773 181 HOH   HOH A . 
D 4 HOH   174 774 167 HOH   HOH A . 
D 4 HOH   175 775 96  HOH   HOH A . 
D 4 HOH   176 776 161 HOH   HOH A . 
D 4 HOH   177 777 182 HOH   HOH A . 
D 4 HOH   178 778 230 HOH   HOH A . 
D 4 HOH   179 779 193 HOH   HOH A . 
D 4 HOH   180 780 163 HOH   HOH A . 
D 4 HOH   181 781 159 HOH   HOH A . 
D 4 HOH   182 782 143 HOH   HOH A . 
D 4 HOH   183 783 226 HOH   HOH A . 
D 4 HOH   184 784 169 HOH   HOH A . 
D 4 HOH   185 785 235 HOH   HOH A . 
D 4 HOH   186 786 36  HOH   HOH A . 
D 4 HOH   187 787 102 HOH   HOH A . 
D 4 HOH   188 788 178 HOH   HOH A . 
D 4 HOH   189 789 134 HOH   HOH A . 
D 4 HOH   190 790 217 HOH   HOH A . 
D 4 HOH   191 791 203 HOH   HOH A . 
D 4 HOH   192 792 228 HOH   HOH A . 
D 4 HOH   193 793 184 HOH   HOH A . 
D 4 HOH   194 794 237 HOH   HOH A . 
D 4 HOH   195 795 179 HOH   HOH A . 
D 4 HOH   196 796 94  HOH   HOH A . 
D 4 HOH   197 797 188 HOH   HOH A . 
D 4 HOH   198 798 212 HOH   HOH A . 
D 4 HOH   199 799 154 HOH   HOH A . 
D 4 HOH   200 800 171 HOH   HOH A . 
D 4 HOH   201 801 234 HOH   HOH A . 
D 4 HOH   202 802 140 HOH   HOH A . 
E 4 HOH   1   701 105 HOH   HOH C . 
E 4 HOH   2   702 183 HOH   HOH C . 
E 4 HOH   3   703 31  HOH   HOH C . 
E 4 HOH   4   704 58  HOH   HOH C . 
E 4 HOH   5   705 194 HOH   HOH C . 
E 4 HOH   6   706 232 HOH   HOH C . 
E 4 HOH   7   707 156 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                   95.560 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9M16 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     154.612 
_cell.length_a_esd                 ? 
_cell.length_b                     42.568 
_cell.length_b_esd                 ? 
_cell.length_c                     42.271 
_cell.length_c_esd                 ? 
_cell.volume                       276898.697 
_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                         9M16 
_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                   9M16 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.15 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.85 
_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    'PEG 3350, Lithium citrate tribasic tetrahydrate, pH 8.4' 
_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 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-07-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8 
_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 BL32XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL32XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9M16 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.06 
_reflns.d_resolution_low                               32.76 
_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                                     17156 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          34.1 
_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                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.061 
_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                                    2.06 
_reflns_shell.d_res_low                                     2.12 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           17.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1316 
_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                                  0.987 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.229 
_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                               31.13 
_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                                 9M16 
_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                            2.06 
_refine.ls_d_res_low                             32.76 
_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                     17155 
_refine.ls_number_reflns_R_free                  859 
_refine.ls_number_reflns_R_work                  16296 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.85 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1679 
_refine.ls_R_factor_R_free                       0.1953 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1664 
_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                          1.40 
_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                 20.7338 
_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                            0.1696 
_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                       2.06 
_refine_hist.d_res_low                        32.76 
_refine_hist.number_atoms_solvent             209 
_refine_hist.number_atoms_total               2260 
_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         36 
_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' ? 0.0063  ? 2236 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8549  ? 3043 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0434  ? 329  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0047  ? 389  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 24.2357 ? 862  ? 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' 2.06 2.19  . . 140 2661 99.50  . . . . 0.1747 . . . . . . . . . . . . . . . 0.2333 
'X-RAY DIFFRACTION' 2.19 2.36  . . 144 2728 99.86  . . . . 0.1696 . . . . . . . . . . . . . . . 0.2085 
'X-RAY DIFFRACTION' 2.36 2.60  . . 141 2664 99.96  . . . . 0.1737 . . . . . . . . . . . . . . . 0.2232 
'X-RAY DIFFRACTION' 2.60 2.97  . . 143 2713 99.90  . . . . 0.1734 . . . . . . . . . . . . . . . 0.2033 
'X-RAY DIFFRACTION' 2.97 3.74  . . 144 2733 100.00 . . . . 0.1628 . . . . . . . . . . . . . . . 0.1994 
'X-RAY DIFFRACTION' 3.74 32.76 . . 147 2797 99.90  . . . . 0.1608 . . . . . . . . . . . . . . . 0.1686 
# 
_struct.entry_id                     9M16 
_struct.title                        'Vitamin D receptor complex with a bis(2,3-dimethylphenyl)dimethylsilane 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        9M16 
_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 9M16 A 11 ? 271 ? P13053 116 ? 423 ? 116 423 
2 2 9M16 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 9M16 GLY A 1  ? UNP P13053 ?   ?   'expression tag' 106 1  
1 9M16 SER A 2  ? UNP P13053 ?   ?   'expression tag' 107 2  
1 9M16 HIS A 3  ? UNP P13053 ?   ?   'expression tag' 108 3  
1 9M16 MET A 4  ? UNP P13053 ?   ?   'expression tag' 109 4  
1 9M16 GLY A 5  ? UNP P13053 ?   ?   'expression tag' 110 5  
1 9M16 SER A 6  ? UNP P13053 ?   ?   'expression tag' 111 6  
1 9M16 PRO A 7  ? UNP P13053 ?   ?   'expression tag' 112 7  
1 9M16 ASN A 8  ? UNP P13053 ?   ?   'expression tag' 113 8  
1 9M16 SER A 9  ? UNP P13053 ?   ?   'expression tag' 114 9  
1 9M16 PRO A 10 ? UNP P13053 ?   ?   'expression tag' 115 10 
1 9M16 ?   A ?  ? UNP P13053 TYR 166 deletion         ?   11 
1 9M16 ?   A ?  ? UNP P13053 SER 167 deletion         ?   12 
1 9M16 ?   A ?  ? UNP P13053 PRO 168 deletion         ?   13 
1 9M16 ?   A ?  ? UNP P13053 ARG 169 deletion         ?   14 
1 9M16 ?   A ?  ? UNP P13053 PRO 170 deletion         ?   15 
1 9M16 ?   A ?  ? UNP P13053 THR 171 deletion         ?   16 
1 9M16 ?   A ?  ? UNP P13053 LEU 172 deletion         ?   17 
1 9M16 ?   A ?  ? UNP P13053 SER 173 deletion         ?   18 
1 9M16 ?   A ?  ? UNP P13053 PHE 174 deletion         ?   19 
1 9M16 ?   A ?  ? UNP P13053 SER 175 deletion         ?   20 
1 9M16 ?   A ?  ? UNP P13053 GLY 176 deletion         ?   21 
1 9M16 ?   A ?  ? UNP P13053 ASN 177 deletion         ?   22 
1 9M16 ?   A ?  ? UNP P13053 SER 178 deletion         ?   23 
1 9M16 ?   A ?  ? UNP P13053 SER 179 deletion         ?   24 
1 9M16 ?   A ?  ? UNP P13053 SER 180 deletion         ?   25 
1 9M16 ?   A ?  ? UNP P13053 SER 181 deletion         ?   26 
1 9M16 ?   A ?  ? UNP P13053 SER 182 deletion         ?   27 
1 9M16 ?   A ?  ? UNP P13053 SER 183 deletion         ?   28 
1 9M16 ?   A ?  ? UNP P13053 ASP 184 deletion         ?   29 
1 9M16 ?   A ?  ? UNP P13053 LEU 185 deletion         ?   30 
1 9M16 ?   A ?  ? UNP P13053 TYR 186 deletion         ?   31 
1 9M16 ?   A ?  ? UNP P13053 THR 187 deletion         ?   32 
1 9M16 ?   A ?  ? UNP P13053 THR 188 deletion         ?   33 
1 9M16 ?   A ?  ? UNP P13053 SER 189 deletion         ?   34 
1 9M16 ?   A ?  ? UNP P13053 LEU 190 deletion         ?   35 
1 9M16 ?   A ?  ? UNP P13053 ASP 191 deletion         ?   36 
1 9M16 ?   A ?  ? UNP P13053 MET 192 deletion         ?   37 
1 9M16 ?   A ?  ? UNP P13053 MET 193 deletion         ?   38 
1 9M16 ?   A ?  ? UNP P13053 GLU 194 deletion         ?   39 
1 9M16 ?   A ?  ? UNP P13053 PRO 195 deletion         ?   40 
1 9M16 ?   A ?  ? UNP P13053 SER 196 deletion         ?   41 
1 9M16 ?   A ?  ? UNP P13053 GLY 197 deletion         ?   42 
1 9M16 ?   A ?  ? UNP P13053 PHE 198 deletion         ?   43 
1 9M16 ?   A ?  ? UNP P13053 SER 199 deletion         ?   44 
1 9M16 ?   A ?  ? UNP P13053 ASN 200 deletion         ?   45 
1 9M16 ?   A ?  ? UNP P13053 LEU 201 deletion         ?   46 
1 9M16 ?   A ?  ? UNP P13053 ASP 202 deletion         ?   47 
1 9M16 ?   A ?  ? UNP P13053 LEU 203 deletion         ?   48 
1 9M16 ?   A ?  ? UNP P13053 ASN 204 deletion         ?   49 
1 9M16 ?   A ?  ? UNP P13053 GLY 205 deletion         ?   50 
1 9M16 ?   A ?  ? UNP P13053 GLU 206 deletion         ?   51 
1 9M16 ?   A ?  ? UNP P13053 ASP 207 deletion         ?   52 
1 9M16 ?   A ?  ? UNP P13053 SER 208 deletion         ?   53 
1 9M16 ?   A ?  ? UNP P13053 ASP 209 deletion         ?   54 
1 9M16 ?   A ?  ? UNP P13053 ASP 210 deletion         ?   55 
1 9M16 ?   A ?  ? UNP P13053 PRO 211 deletion         ?   56 
1 9M16 ?   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)' 1070  ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  12130 ? 
# 
_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  ? MET A 91  ? MET A 222 MET A 243 1 ? 22 
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  ? ASN A 120 ? THR A 251 ASN A 272 1 ? 22 
HELX_P HELX_P6  AA6 SER A 134 ? ASP A 136 ? SER A 286 ASP A 288 5 ? 3  
HELX_P HELX_P7  AA7 ASP A 140 ? LYS A 146 ? ASP A 292 LYS A 298 1 ? 7  
HELX_P HELX_P8  AA8 THR A 150 ? ASN A 168 ? THR A 302 ASN A 320 1 ? 19 
HELX_P HELX_P9  AA9 HIS A 170 ? VAL A 183 ? HIS A 322 VAL A 335 1 ? 14 
HELX_P HELX_P10 AB1 ASP A 192 ? HIS A 215 ? ASP A 344 HIS A 367 1 ? 24 
HELX_P HELX_P11 AB2 GLN A 222 ? PHE A 250 ? GLN A 374 PHE A 402 1 ? 29 
HELX_P HELX_P12 AB3 GLN A 251 ? MET A 256 ? GLN A 403 MET A 408 1 ? 6  
HELX_P HELX_P13 AB4 THR A 259 ? GLY A 267 ? THR A 411 GLY A 419 1 ? 9  
HELX_P HELX_P14 AB5 HIS B 3   ? LYS B 11  ? HIS C 627 LYS C 635 1 ? 9  
# 
_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       3.02 
# 
_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                   9M16 
_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 CYS A 284 ? ? -104.16 47.63  
2 1 GLN A 343 ? ? -96.81  -60.73 
# 
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 19.3104416538 0.464374213808 19.4458613151 0.0935146709236 ? -0.0374700881917 ? 0.000480569978425 
? 0.140600319669 ? -0.0158652845464 ? 0.0991982222033 ? 2.19346583619   ? 0.294416234147    ? 0.736384076263  ? 0.71261407499    ? 
0.0200167059745 ? 0.948256760602   ? 0.0108203757402 ? -0.00245694425515 ? -0.133648946758 ? 0.0476373690008 ? 0.0168715156615 ? 
-0.0647258427688  ? -0.133149825068 ? 0.180723316964  ? 0.0965774670819   ? 
2 'X-RAY DIFFRACTION' ? refined 5.76194536354 -10.5881102576 11.2323271957 0.261937829764  ? 0.0475999896801  ? 0.00954289540453  
? 0.437049339663 ? -0.109305854398  ? 0.334704501608  ? 0.0167123428364 ? -0.00221984885492 ? 0.0101958240007 ? 0.00783162943814 ? 
-0.008999607949 ? 0.00926357288721 ? 0.0803296961185 ? 0.132746939934    ? -0.159506983458 ? 0.110018001577  ? -0.118310233423 ? 
-0.00688611239659 ? 0.0781294422373 ? -0.128929936056 ? 3.53848340152e-06 ? 
# 
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' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       802 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.67 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
A1L74 C10  C  Y N 1   
A1L74 C13  C  Y N 2   
A1L74 C15  C  N N 3   
A1L74 C20  C  N N 4   
A1L74 C21  C  N N 5   
A1L74 C22  C  N N 6   
A1L74 C24  C  N N 7   
A1L74 C26  C  N N 8   
A1L74 C28  C  N N 9   
A1L74 C01  C  Y N 10  
A1L74 C02  C  Y N 11  
A1L74 C03  C  Y N 12  
A1L74 C04  C  Y N 13  
A1L74 C05  C  Y N 14  
A1L74 C06  C  Y N 15  
A1L74 C08  C  Y N 16  
A1L74 C09  C  Y N 17  
A1L74 C11  C  Y N 18  
A1L74 C12  C  Y N 19  
A1L74 C14  C  N N 20  
A1L74 C18  C  N N 21  
A1L74 C19  C  N S 22  
A1L74 C23  C  N N 23  
A1L74 C25  C  N N 24  
A1L74 C27  C  N N 25  
A1L74 C31  C  N N 26  
A1L74 C32  C  N N 27  
A1L74 C35  C  N N 28  
A1L74 C36  C  N N 29  
A1L74 O16  O  N N 30  
A1L74 O17  O  N N 31  
A1L74 O29  O  N N 32  
A1L74 O30  O  N N 33  
A1L74 O33  O  N N 34  
A1L74 O34  O  N N 35  
A1L74 SI07 SI N N 36  
A1L74 H131 H  N N 37  
A1L74 H151 H  N N 38  
A1L74 H152 H  N N 39  
A1L74 H153 H  N N 40  
A1L74 H202 H  N N 41  
A1L74 H201 H  N N 42  
A1L74 H212 H  N N 43  
A1L74 H211 H  N N 44  
A1L74 H262 H  N N 45  
A1L74 H261 H  N N 46  
A1L74 H283 H  N N 47  
A1L74 H281 H  N N 48  
A1L74 H282 H  N N 49  
A1L74 H011 H  N N 50  
A1L74 H061 H  N N 51  
A1L74 H121 H  N N 52  
A1L74 H141 H  N N 53  
A1L74 H143 H  N N 54  
A1L74 H142 H  N N 55  
A1L74 H182 H  N N 56  
A1L74 H181 H  N N 57  
A1L74 H191 H  N N 58  
A1L74 H231 H  N N 59  
A1L74 H232 H  N N 60  
A1L74 H251 H  N N 61  
A1L74 H252 H  N N 62  
A1L74 H271 H  N N 63  
A1L74 H272 H  N N 64  
A1L74 H273 H  N N 65  
A1L74 H311 H  N N 66  
A1L74 H313 H  N N 67  
A1L74 H312 H  N N 68  
A1L74 H322 H  N N 69  
A1L74 H321 H  N N 70  
A1L74 H323 H  N N 71  
A1L74 H351 H  N N 72  
A1L74 H353 H  N N 73  
A1L74 H352 H  N N 74  
A1L74 H362 H  N N 75  
A1L74 H361 H  N N 76  
A1L74 H363 H  N N 77  
A1L74 H291 H  N N 78  
A1L74 H1   H  N N 79  
A1L74 H341 H  N N 80  
ALA   N    N  N N 81  
ALA   CA   C  N S 82  
ALA   C    C  N N 83  
ALA   O    O  N N 84  
ALA   CB   C  N N 85  
ALA   OXT  O  N N 86  
ALA   H    H  N N 87  
ALA   H2   H  N N 88  
ALA   HA   H  N N 89  
ALA   HB1  H  N N 90  
ALA   HB2  H  N N 91  
ALA   HB3  H  N N 92  
ALA   HXT  H  N N 93  
ARG   N    N  N N 94  
ARG   CA   C  N S 95  
ARG   C    C  N N 96  
ARG   O    O  N N 97  
ARG   CB   C  N N 98  
ARG   CG   C  N N 99  
ARG   CD   C  N N 100 
ARG   NE   N  N N 101 
ARG   CZ   C  N N 102 
ARG   NH1  N  N N 103 
ARG   NH2  N  N N 104 
ARG   OXT  O  N N 105 
ARG   H    H  N N 106 
ARG   H2   H  N N 107 
ARG   HA   H  N N 108 
ARG   HB2  H  N N 109 
ARG   HB3  H  N N 110 
ARG   HG2  H  N N 111 
ARG   HG3  H  N N 112 
ARG   HD2  H  N N 113 
ARG   HD3  H  N N 114 
ARG   HE   H  N N 115 
ARG   HH11 H  N N 116 
ARG   HH12 H  N N 117 
ARG   HH21 H  N N 118 
ARG   HH22 H  N N 119 
ARG   HXT  H  N N 120 
ASN   N    N  N N 121 
ASN   CA   C  N S 122 
ASN   C    C  N N 123 
ASN   O    O  N N 124 
ASN   CB   C  N N 125 
ASN   CG   C  N N 126 
ASN   OD1  O  N N 127 
ASN   ND2  N  N N 128 
ASN   OXT  O  N N 129 
ASN   H    H  N N 130 
ASN   H2   H  N N 131 
ASN   HA   H  N N 132 
ASN   HB2  H  N N 133 
ASN   HB3  H  N N 134 
ASN   HD21 H  N N 135 
ASN   HD22 H  N N 136 
ASN   HXT  H  N N 137 
ASP   N    N  N N 138 
ASP   CA   C  N S 139 
ASP   C    C  N N 140 
ASP   O    O  N N 141 
ASP   CB   C  N N 142 
ASP   CG   C  N N 143 
ASP   OD1  O  N N 144 
ASP   OD2  O  N N 145 
ASP   OXT  O  N N 146 
ASP   H    H  N N 147 
ASP   H2   H  N N 148 
ASP   HA   H  N N 149 
ASP   HB2  H  N N 150 
ASP   HB3  H  N N 151 
ASP   HD2  H  N N 152 
ASP   HXT  H  N N 153 
CYS   N    N  N N 154 
CYS   CA   C  N R 155 
CYS   C    C  N N 156 
CYS   O    O  N N 157 
CYS   CB   C  N N 158 
CYS   SG   S  N N 159 
CYS   OXT  O  N N 160 
CYS   H    H  N N 161 
CYS   H2   H  N N 162 
CYS   HA   H  N N 163 
CYS   HB2  H  N N 164 
CYS   HB3  H  N N 165 
CYS   HG   H  N N 166 
CYS   HXT  H  N N 167 
GLN   N    N  N N 168 
GLN   CA   C  N S 169 
GLN   C    C  N N 170 
GLN   O    O  N N 171 
GLN   CB   C  N N 172 
GLN   CG   C  N N 173 
GLN   CD   C  N N 174 
GLN   OE1  O  N N 175 
GLN   NE2  N  N N 176 
GLN   OXT  O  N N 177 
GLN   H    H  N N 178 
GLN   H2   H  N N 179 
GLN   HA   H  N N 180 
GLN   HB2  H  N N 181 
GLN   HB3  H  N N 182 
GLN   HG2  H  N N 183 
GLN   HG3  H  N N 184 
GLN   HE21 H  N N 185 
GLN   HE22 H  N N 186 
GLN   HXT  H  N N 187 
GLU   N    N  N N 188 
GLU   CA   C  N S 189 
GLU   C    C  N N 190 
GLU   O    O  N N 191 
GLU   CB   C  N N 192 
GLU   CG   C  N N 193 
GLU   CD   C  N N 194 
GLU   OE1  O  N N 195 
GLU   OE2  O  N N 196 
GLU   OXT  O  N N 197 
GLU   H    H  N N 198 
GLU   H2   H  N N 199 
GLU   HA   H  N N 200 
GLU   HB2  H  N N 201 
GLU   HB3  H  N N 202 
GLU   HG2  H  N N 203 
GLU   HG3  H  N N 204 
GLU   HE2  H  N N 205 
GLU   HXT  H  N N 206 
GLY   N    N  N N 207 
GLY   CA   C  N N 208 
GLY   C    C  N N 209 
GLY   O    O  N N 210 
GLY   OXT  O  N N 211 
GLY   H    H  N N 212 
GLY   H2   H  N N 213 
GLY   HA2  H  N N 214 
GLY   HA3  H  N N 215 
GLY   HXT  H  N N 216 
HIS   N    N  N N 217 
HIS   CA   C  N S 218 
HIS   C    C  N N 219 
HIS   O    O  N N 220 
HIS   CB   C  N N 221 
HIS   CG   C  Y N 222 
HIS   ND1  N  Y N 223 
HIS   CD2  C  Y N 224 
HIS   CE1  C  Y N 225 
HIS   NE2  N  Y N 226 
HIS   OXT  O  N N 227 
HIS   H    H  N N 228 
HIS   H2   H  N N 229 
HIS   HA   H  N N 230 
HIS   HB2  H  N N 231 
HIS   HB3  H  N N 232 
HIS   HD1  H  N N 233 
HIS   HD2  H  N N 234 
HIS   HE1  H  N N 235 
HIS   HE2  H  N N 236 
HIS   HXT  H  N N 237 
HOH   O    O  N N 238 
HOH   H1   H  N N 239 
HOH   H2   H  N N 240 
ILE   N    N  N N 241 
ILE   CA   C  N S 242 
ILE   C    C  N N 243 
ILE   O    O  N N 244 
ILE   CB   C  N S 245 
ILE   CG1  C  N N 246 
ILE   CG2  C  N N 247 
ILE   CD1  C  N N 248 
ILE   OXT  O  N N 249 
ILE   H    H  N N 250 
ILE   H2   H  N N 251 
ILE   HA   H  N N 252 
ILE   HB   H  N N 253 
ILE   HG12 H  N N 254 
ILE   HG13 H  N N 255 
ILE   HG21 H  N N 256 
ILE   HG22 H  N N 257 
ILE   HG23 H  N N 258 
ILE   HD11 H  N N 259 
ILE   HD12 H  N N 260 
ILE   HD13 H  N N 261 
ILE   HXT  H  N N 262 
LEU   N    N  N N 263 
LEU   CA   C  N S 264 
LEU   C    C  N N 265 
LEU   O    O  N N 266 
LEU   CB   C  N N 267 
LEU   CG   C  N N 268 
LEU   CD1  C  N N 269 
LEU   CD2  C  N N 270 
LEU   OXT  O  N N 271 
LEU   H    H  N N 272 
LEU   H2   H  N N 273 
LEU   HA   H  N N 274 
LEU   HB2  H  N N 275 
LEU   HB3  H  N N 276 
LEU   HG   H  N N 277 
LEU   HD11 H  N N 278 
LEU   HD12 H  N N 279 
LEU   HD13 H  N N 280 
LEU   HD21 H  N N 281 
LEU   HD22 H  N N 282 
LEU   HD23 H  N N 283 
LEU   HXT  H  N N 284 
LYS   N    N  N N 285 
LYS   CA   C  N S 286 
LYS   C    C  N N 287 
LYS   O    O  N N 288 
LYS   CB   C  N N 289 
LYS   CG   C  N N 290 
LYS   CD   C  N N 291 
LYS   CE   C  N N 292 
LYS   NZ   N  N N 293 
LYS   OXT  O  N N 294 
LYS   H    H  N N 295 
LYS   H2   H  N N 296 
LYS   HA   H  N N 297 
LYS   HB2  H  N N 298 
LYS   HB3  H  N N 299 
LYS   HG2  H  N N 300 
LYS   HG3  H  N N 301 
LYS   HD2  H  N N 302 
LYS   HD3  H  N N 303 
LYS   HE2  H  N N 304 
LYS   HE3  H  N N 305 
LYS   HZ1  H  N N 306 
LYS   HZ2  H  N N 307 
LYS   HZ3  H  N N 308 
LYS   HXT  H  N N 309 
MET   N    N  N N 310 
MET   CA   C  N S 311 
MET   C    C  N N 312 
MET   O    O  N N 313 
MET   CB   C  N N 314 
MET   CG   C  N N 315 
MET   SD   S  N N 316 
MET   CE   C  N N 317 
MET   OXT  O  N N 318 
MET   H    H  N N 319 
MET   H2   H  N N 320 
MET   HA   H  N N 321 
MET   HB2  H  N N 322 
MET   HB3  H  N N 323 
MET   HG2  H  N N 324 
MET   HG3  H  N N 325 
MET   HE1  H  N N 326 
MET   HE2  H  N N 327 
MET   HE3  H  N N 328 
MET   HXT  H  N N 329 
PHE   N    N  N N 330 
PHE   CA   C  N S 331 
PHE   C    C  N N 332 
PHE   O    O  N N 333 
PHE   CB   C  N N 334 
PHE   CG   C  Y N 335 
PHE   CD1  C  Y N 336 
PHE   CD2  C  Y N 337 
PHE   CE1  C  Y N 338 
PHE   CE2  C  Y N 339 
PHE   CZ   C  Y N 340 
PHE   OXT  O  N N 341 
PHE   H    H  N N 342 
PHE   H2   H  N N 343 
PHE   HA   H  N N 344 
PHE   HB2  H  N N 345 
PHE   HB3  H  N N 346 
PHE   HD1  H  N N 347 
PHE   HD2  H  N N 348 
PHE   HE1  H  N N 349 
PHE   HE2  H  N N 350 
PHE   HZ   H  N N 351 
PHE   HXT  H  N N 352 
PRO   N    N  N N 353 
PRO   CA   C  N S 354 
PRO   C    C  N N 355 
PRO   O    O  N N 356 
PRO   CB   C  N N 357 
PRO   CG   C  N N 358 
PRO   CD   C  N N 359 
PRO   OXT  O  N N 360 
PRO   H    H  N N 361 
PRO   HA   H  N N 362 
PRO   HB2  H  N N 363 
PRO   HB3  H  N N 364 
PRO   HG2  H  N N 365 
PRO   HG3  H  N N 366 
PRO   HD2  H  N N 367 
PRO   HD3  H  N N 368 
PRO   HXT  H  N N 369 
SER   N    N  N N 370 
SER   CA   C  N S 371 
SER   C    C  N N 372 
SER   O    O  N N 373 
SER   CB   C  N N 374 
SER   OG   O  N N 375 
SER   OXT  O  N N 376 
SER   H    H  N N 377 
SER   H2   H  N N 378 
SER   HA   H  N N 379 
SER   HB2  H  N N 380 
SER   HB3  H  N N 381 
SER   HG   H  N N 382 
SER   HXT  H  N N 383 
THR   N    N  N N 384 
THR   CA   C  N S 385 
THR   C    C  N N 386 
THR   O    O  N N 387 
THR   CB   C  N R 388 
THR   OG1  O  N N 389 
THR   CG2  C  N N 390 
THR   OXT  O  N N 391 
THR   H    H  N N 392 
THR   H2   H  N N 393 
THR   HA   H  N N 394 
THR   HB   H  N N 395 
THR   HG1  H  N N 396 
THR   HG21 H  N N 397 
THR   HG22 H  N N 398 
THR   HG23 H  N N 399 
THR   HXT  H  N N 400 
TRP   N    N  N N 401 
TRP   CA   C  N S 402 
TRP   C    C  N N 403 
TRP   O    O  N N 404 
TRP   CB   C  N N 405 
TRP   CG   C  Y N 406 
TRP   CD1  C  Y N 407 
TRP   CD2  C  Y N 408 
TRP   NE1  N  Y N 409 
TRP   CE2  C  Y N 410 
TRP   CE3  C  Y N 411 
TRP   CZ2  C  Y N 412 
TRP   CZ3  C  Y N 413 
TRP   CH2  C  Y N 414 
TRP   OXT  O  N N 415 
TRP   H    H  N N 416 
TRP   H2   H  N N 417 
TRP   HA   H  N N 418 
TRP   HB2  H  N N 419 
TRP   HB3  H  N N 420 
TRP   HD1  H  N N 421 
TRP   HE1  H  N N 422 
TRP   HE3  H  N N 423 
TRP   HZ2  H  N N 424 
TRP   HZ3  H  N N 425 
TRP   HH2  H  N N 426 
TRP   HXT  H  N N 427 
TYR   N    N  N N 428 
TYR   CA   C  N S 429 
TYR   C    C  N N 430 
TYR   O    O  N N 431 
TYR   CB   C  N N 432 
TYR   CG   C  Y N 433 
TYR   CD1  C  Y N 434 
TYR   CD2  C  Y N 435 
TYR   CE1  C  Y N 436 
TYR   CE2  C  Y N 437 
TYR   CZ   C  Y N 438 
TYR   OH   O  N N 439 
TYR   OXT  O  N N 440 
TYR   H    H  N N 441 
TYR   H2   H  N N 442 
TYR   HA   H  N N 443 
TYR   HB2  H  N N 444 
TYR   HB3  H  N N 445 
TYR   HD1  H  N N 446 
TYR   HD2  H  N N 447 
TYR   HE1  H  N N 448 
TYR   HE2  H  N N 449 
TYR   HH   H  N N 450 
TYR   HXT  H  N N 451 
VAL   N    N  N N 452 
VAL   CA   C  N S 453 
VAL   C    C  N N 454 
VAL   O    O  N N 455 
VAL   CB   C  N N 456 
VAL   CG1  C  N N 457 
VAL   CG2  C  N N 458 
VAL   OXT  O  N N 459 
VAL   H    H  N N 460 
VAL   H2   H  N N 461 
VAL   HA   H  N N 462 
VAL   HB   H  N N 463 
VAL   HG11 H  N N 464 
VAL   HG12 H  N N 465 
VAL   HG13 H  N N 466 
VAL   HG21 H  N N 467 
VAL   HG22 H  N N 468 
VAL   HG23 H  N N 469 
VAL   HXT  H  N N 470 
# 
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 
A1L74 C01  C02  doub Y N 1   
A1L74 C01  C06  sing Y N 2   
A1L74 C02  C03  sing Y N 3   
A1L74 C02  O17  sing N N 4   
A1L74 C03  C04  doub Y N 5   
A1L74 C03  C31  sing N N 6   
A1L74 C04  C05  sing Y N 7   
A1L74 C04  C35  sing N N 8   
A1L74 C05  C06  doub Y N 9   
A1L74 C05  SI07 sing N N 10  
A1L74 SI07 C08  sing N N 11  
A1L74 SI07 C14  sing N N 12  
A1L74 SI07 C15  sing N N 13  
A1L74 C08  C09  doub Y N 14  
A1L74 C08  C13  sing Y N 15  
A1L74 C09  C10  sing Y N 16  
A1L74 C09  C36  sing N N 17  
A1L74 C10  C11  doub Y N 18  
A1L74 C10  C32  sing N N 19  
A1L74 C11  C12  sing Y N 20  
A1L74 C11  O16  sing N N 21  
A1L74 C12  C13  doub Y N 22  
A1L74 O16  C23  sing N N 23  
A1L74 O17  C18  sing N N 24  
A1L74 C18  C19  sing N N 25  
A1L74 C19  C20  sing N N 26  
A1L74 C19  O34  sing N N 27  
A1L74 C20  C21  sing N N 28  
A1L74 C21  C22  sing N N 29  
A1L74 C22  O30  doub N N 30  
A1L74 C22  O33  sing N N 31  
A1L74 C23  C24  sing N N 32  
A1L74 C24  C25  sing N N 33  
A1L74 C24  C26  sing N N 34  
A1L74 C24  O29  sing N N 35  
A1L74 C25  C27  sing N N 36  
A1L74 C26  C28  sing N N 37  
A1L74 C13  H131 sing N N 38  
A1L74 C15  H151 sing N N 39  
A1L74 C15  H152 sing N N 40  
A1L74 C15  H153 sing N N 41  
A1L74 C20  H202 sing N N 42  
A1L74 C20  H201 sing N N 43  
A1L74 C21  H212 sing N N 44  
A1L74 C21  H211 sing N N 45  
A1L74 C26  H262 sing N N 46  
A1L74 C26  H261 sing N N 47  
A1L74 C28  H283 sing N N 48  
A1L74 C28  H281 sing N N 49  
A1L74 C28  H282 sing N N 50  
A1L74 C01  H011 sing N N 51  
A1L74 C06  H061 sing N N 52  
A1L74 C12  H121 sing N N 53  
A1L74 C14  H141 sing N N 54  
A1L74 C14  H143 sing N N 55  
A1L74 C14  H142 sing N N 56  
A1L74 C18  H182 sing N N 57  
A1L74 C18  H181 sing N N 58  
A1L74 C19  H191 sing N N 59  
A1L74 C23  H231 sing N N 60  
A1L74 C23  H232 sing N N 61  
A1L74 C25  H251 sing N N 62  
A1L74 C25  H252 sing N N 63  
A1L74 C27  H271 sing N N 64  
A1L74 C27  H272 sing N N 65  
A1L74 C27  H273 sing N N 66  
A1L74 C31  H311 sing N N 67  
A1L74 C31  H313 sing N N 68  
A1L74 C31  H312 sing N N 69  
A1L74 C32  H322 sing N N 70  
A1L74 C32  H321 sing N N 71  
A1L74 C32  H323 sing N N 72  
A1L74 C35  H351 sing N N 73  
A1L74 C35  H353 sing N N 74  
A1L74 C35  H352 sing N N 75  
A1L74 C36  H362 sing N N 76  
A1L74 C36  H361 sing N N 77  
A1L74 C36  H363 sing N N 78  
A1L74 O29  H291 sing N N 79  
A1L74 O33  H1   sing N N 80  
A1L74 O34  H341 sing N N 81  
ALA   N    CA   sing N N 82  
ALA   N    H    sing N N 83  
ALA   N    H2   sing N N 84  
ALA   CA   C    sing N N 85  
ALA   CA   CB   sing N N 86  
ALA   CA   HA   sing N N 87  
ALA   C    O    doub N N 88  
ALA   C    OXT  sing N N 89  
ALA   CB   HB1  sing N N 90  
ALA   CB   HB2  sing N N 91  
ALA   CB   HB3  sing N N 92  
ALA   OXT  HXT  sing N N 93  
ARG   N    CA   sing N N 94  
ARG   N    H    sing N N 95  
ARG   N    H2   sing N N 96  
ARG   CA   C    sing N N 97  
ARG   CA   CB   sing N N 98  
ARG   CA   HA   sing N N 99  
ARG   C    O    doub N N 100 
ARG   C    OXT  sing N N 101 
ARG   CB   CG   sing N N 102 
ARG   CB   HB2  sing N N 103 
ARG   CB   HB3  sing N N 104 
ARG   CG   CD   sing N N 105 
ARG   CG   HG2  sing N N 106 
ARG   CG   HG3  sing N N 107 
ARG   CD   NE   sing N N 108 
ARG   CD   HD2  sing N N 109 
ARG   CD   HD3  sing N N 110 
ARG   NE   CZ   sing N N 111 
ARG   NE   HE   sing N N 112 
ARG   CZ   NH1  sing N N 113 
ARG   CZ   NH2  doub N N 114 
ARG   NH1  HH11 sing N N 115 
ARG   NH1  HH12 sing N N 116 
ARG   NH2  HH21 sing N N 117 
ARG   NH2  HH22 sing N N 118 
ARG   OXT  HXT  sing N N 119 
ASN   N    CA   sing N N 120 
ASN   N    H    sing N N 121 
ASN   N    H2   sing N N 122 
ASN   CA   C    sing N N 123 
ASN   CA   CB   sing N N 124 
ASN   CA   HA   sing N N 125 
ASN   C    O    doub N N 126 
ASN   C    OXT  sing N N 127 
ASN   CB   CG   sing N N 128 
ASN   CB   HB2  sing N N 129 
ASN   CB   HB3  sing N N 130 
ASN   CG   OD1  doub N N 131 
ASN   CG   ND2  sing N N 132 
ASN   ND2  HD21 sing N N 133 
ASN   ND2  HD22 sing N N 134 
ASN   OXT  HXT  sing N N 135 
ASP   N    CA   sing N N 136 
ASP   N    H    sing N N 137 
ASP   N    H2   sing N N 138 
ASP   CA   C    sing N N 139 
ASP   CA   CB   sing N N 140 
ASP   CA   HA   sing N N 141 
ASP   C    O    doub N N 142 
ASP   C    OXT  sing N N 143 
ASP   CB   CG   sing N N 144 
ASP   CB   HB2  sing N N 145 
ASP   CB   HB3  sing N N 146 
ASP   CG   OD1  doub N N 147 
ASP   CG   OD2  sing N N 148 
ASP   OD2  HD2  sing N N 149 
ASP   OXT  HXT  sing N N 150 
CYS   N    CA   sing N N 151 
CYS   N    H    sing N N 152 
CYS   N    H2   sing N N 153 
CYS   CA   C    sing N N 154 
CYS   CA   CB   sing N N 155 
CYS   CA   HA   sing N N 156 
CYS   C    O    doub N N 157 
CYS   C    OXT  sing N N 158 
CYS   CB   SG   sing N N 159 
CYS   CB   HB2  sing N N 160 
CYS   CB   HB3  sing N N 161 
CYS   SG   HG   sing N N 162 
CYS   OXT  HXT  sing N N 163 
GLN   N    CA   sing N N 164 
GLN   N    H    sing N N 165 
GLN   N    H2   sing N N 166 
GLN   CA   C    sing N N 167 
GLN   CA   CB   sing N N 168 
GLN   CA   HA   sing N N 169 
GLN   C    O    doub N N 170 
GLN   C    OXT  sing N N 171 
GLN   CB   CG   sing N N 172 
GLN   CB   HB2  sing N N 173 
GLN   CB   HB3  sing N N 174 
GLN   CG   CD   sing N N 175 
GLN   CG   HG2  sing N N 176 
GLN   CG   HG3  sing N N 177 
GLN   CD   OE1  doub N N 178 
GLN   CD   NE2  sing N N 179 
GLN   NE2  HE21 sing N N 180 
GLN   NE2  HE22 sing N N 181 
GLN   OXT  HXT  sing N N 182 
GLU   N    CA   sing N N 183 
GLU   N    H    sing N N 184 
GLU   N    H2   sing N N 185 
GLU   CA   C    sing N N 186 
GLU   CA   CB   sing N N 187 
GLU   CA   HA   sing N N 188 
GLU   C    O    doub N N 189 
GLU   C    OXT  sing N N 190 
GLU   CB   CG   sing N N 191 
GLU   CB   HB2  sing N N 192 
GLU   CB   HB3  sing N N 193 
GLU   CG   CD   sing N N 194 
GLU   CG   HG2  sing N N 195 
GLU   CG   HG3  sing N N 196 
GLU   CD   OE1  doub N N 197 
GLU   CD   OE2  sing N N 198 
GLU   OE2  HE2  sing N N 199 
GLU   OXT  HXT  sing N N 200 
GLY   N    CA   sing N N 201 
GLY   N    H    sing N N 202 
GLY   N    H2   sing N N 203 
GLY   CA   C    sing N N 204 
GLY   CA   HA2  sing N N 205 
GLY   CA   HA3  sing N N 206 
GLY   C    O    doub N N 207 
GLY   C    OXT  sing N N 208 
GLY   OXT  HXT  sing N N 209 
HIS   N    CA   sing N N 210 
HIS   N    H    sing N N 211 
HIS   N    H2   sing N N 212 
HIS   CA   C    sing N N 213 
HIS   CA   CB   sing N N 214 
HIS   CA   HA   sing N N 215 
HIS   C    O    doub N N 216 
HIS   C    OXT  sing N N 217 
HIS   CB   CG   sing N N 218 
HIS   CB   HB2  sing N N 219 
HIS   CB   HB3  sing N N 220 
HIS   CG   ND1  sing Y N 221 
HIS   CG   CD2  doub Y N 222 
HIS   ND1  CE1  doub Y N 223 
HIS   ND1  HD1  sing N N 224 
HIS   CD2  NE2  sing Y N 225 
HIS   CD2  HD2  sing N N 226 
HIS   CE1  NE2  sing Y N 227 
HIS   CE1  HE1  sing N N 228 
HIS   NE2  HE2  sing N N 229 
HIS   OXT  HXT  sing N N 230 
HOH   O    H1   sing N N 231 
HOH   O    H2   sing N N 232 
ILE   N    CA   sing N N 233 
ILE   N    H    sing N N 234 
ILE   N    H2   sing N N 235 
ILE   CA   C    sing N N 236 
ILE   CA   CB   sing N N 237 
ILE   CA   HA   sing N N 238 
ILE   C    O    doub N N 239 
ILE   C    OXT  sing N N 240 
ILE   CB   CG1  sing N N 241 
ILE   CB   CG2  sing N N 242 
ILE   CB   HB   sing N N 243 
ILE   CG1  CD1  sing N N 244 
ILE   CG1  HG12 sing N N 245 
ILE   CG1  HG13 sing N N 246 
ILE   CG2  HG21 sing N N 247 
ILE   CG2  HG22 sing N N 248 
ILE   CG2  HG23 sing N N 249 
ILE   CD1  HD11 sing N N 250 
ILE   CD1  HD12 sing N N 251 
ILE   CD1  HD13 sing N N 252 
ILE   OXT  HXT  sing N N 253 
LEU   N    CA   sing N N 254 
LEU   N    H    sing N N 255 
LEU   N    H2   sing N N 256 
LEU   CA   C    sing N N 257 
LEU   CA   CB   sing N N 258 
LEU   CA   HA   sing N N 259 
LEU   C    O    doub N N 260 
LEU   C    OXT  sing N N 261 
LEU   CB   CG   sing N N 262 
LEU   CB   HB2  sing N N 263 
LEU   CB   HB3  sing N N 264 
LEU   CG   CD1  sing N N 265 
LEU   CG   CD2  sing N N 266 
LEU   CG   HG   sing N N 267 
LEU   CD1  HD11 sing N N 268 
LEU   CD1  HD12 sing N N 269 
LEU   CD1  HD13 sing N N 270 
LEU   CD2  HD21 sing N N 271 
LEU   CD2  HD22 sing N N 272 
LEU   CD2  HD23 sing N N 273 
LEU   OXT  HXT  sing N N 274 
LYS   N    CA   sing N N 275 
LYS   N    H    sing N N 276 
LYS   N    H2   sing N N 277 
LYS   CA   C    sing N N 278 
LYS   CA   CB   sing N N 279 
LYS   CA   HA   sing N N 280 
LYS   C    O    doub N N 281 
LYS   C    OXT  sing N N 282 
LYS   CB   CG   sing N N 283 
LYS   CB   HB2  sing N N 284 
LYS   CB   HB3  sing N N 285 
LYS   CG   CD   sing N N 286 
LYS   CG   HG2  sing N N 287 
LYS   CG   HG3  sing N N 288 
LYS   CD   CE   sing N N 289 
LYS   CD   HD2  sing N N 290 
LYS   CD   HD3  sing N N 291 
LYS   CE   NZ   sing N N 292 
LYS   CE   HE2  sing N N 293 
LYS   CE   HE3  sing N N 294 
LYS   NZ   HZ1  sing N N 295 
LYS   NZ   HZ2  sing N N 296 
LYS   NZ   HZ3  sing N N 297 
LYS   OXT  HXT  sing N N 298 
MET   N    CA   sing N N 299 
MET   N    H    sing N N 300 
MET   N    H2   sing N N 301 
MET   CA   C    sing N N 302 
MET   CA   CB   sing N N 303 
MET   CA   HA   sing N N 304 
MET   C    O    doub N N 305 
MET   C    OXT  sing N N 306 
MET   CB   CG   sing N N 307 
MET   CB   HB2  sing N N 308 
MET   CB   HB3  sing N N 309 
MET   CG   SD   sing N N 310 
MET   CG   HG2  sing N N 311 
MET   CG   HG3  sing N N 312 
MET   SD   CE   sing N N 313 
MET   CE   HE1  sing N N 314 
MET   CE   HE2  sing N N 315 
MET   CE   HE3  sing N N 316 
MET   OXT  HXT  sing N N 317 
PHE   N    CA   sing N N 318 
PHE   N    H    sing N N 319 
PHE   N    H2   sing N N 320 
PHE   CA   C    sing N N 321 
PHE   CA   CB   sing N N 322 
PHE   CA   HA   sing N N 323 
PHE   C    O    doub N N 324 
PHE   C    OXT  sing N N 325 
PHE   CB   CG   sing N N 326 
PHE   CB   HB2  sing N N 327 
PHE   CB   HB3  sing N N 328 
PHE   CG   CD1  doub Y N 329 
PHE   CG   CD2  sing Y N 330 
PHE   CD1  CE1  sing Y N 331 
PHE   CD1  HD1  sing N N 332 
PHE   CD2  CE2  doub Y N 333 
PHE   CD2  HD2  sing N N 334 
PHE   CE1  CZ   doub Y N 335 
PHE   CE1  HE1  sing N N 336 
PHE   CE2  CZ   sing Y N 337 
PHE   CE2  HE2  sing N N 338 
PHE   CZ   HZ   sing N N 339 
PHE   OXT  HXT  sing N N 340 
PRO   N    CA   sing N N 341 
PRO   N    CD   sing N N 342 
PRO   N    H    sing N N 343 
PRO   CA   C    sing N N 344 
PRO   CA   CB   sing N N 345 
PRO   CA   HA   sing N N 346 
PRO   C    O    doub N N 347 
PRO   C    OXT  sing N N 348 
PRO   CB   CG   sing N N 349 
PRO   CB   HB2  sing N N 350 
PRO   CB   HB3  sing N N 351 
PRO   CG   CD   sing N N 352 
PRO   CG   HG2  sing N N 353 
PRO   CG   HG3  sing N N 354 
PRO   CD   HD2  sing N N 355 
PRO   CD   HD3  sing N N 356 
PRO   OXT  HXT  sing N N 357 
SER   N    CA   sing N N 358 
SER   N    H    sing N N 359 
SER   N    H2   sing N N 360 
SER   CA   C    sing N N 361 
SER   CA   CB   sing N N 362 
SER   CA   HA   sing N N 363 
SER   C    O    doub N N 364 
SER   C    OXT  sing N N 365 
SER   CB   OG   sing N N 366 
SER   CB   HB2  sing N N 367 
SER   CB   HB3  sing N N 368 
SER   OG   HG   sing N N 369 
SER   OXT  HXT  sing N N 370 
THR   N    CA   sing N N 371 
THR   N    H    sing N N 372 
THR   N    H2   sing N N 373 
THR   CA   C    sing N N 374 
THR   CA   CB   sing N N 375 
THR   CA   HA   sing N N 376 
THR   C    O    doub N N 377 
THR   C    OXT  sing N N 378 
THR   CB   OG1  sing N N 379 
THR   CB   CG2  sing N N 380 
THR   CB   HB   sing N N 381 
THR   OG1  HG1  sing N N 382 
THR   CG2  HG21 sing N N 383 
THR   CG2  HG22 sing N N 384 
THR   CG2  HG23 sing N N 385 
THR   OXT  HXT  sing N N 386 
TRP   N    CA   sing N N 387 
TRP   N    H    sing N N 388 
TRP   N    H2   sing N N 389 
TRP   CA   C    sing N N 390 
TRP   CA   CB   sing N N 391 
TRP   CA   HA   sing N N 392 
TRP   C    O    doub N N 393 
TRP   C    OXT  sing N N 394 
TRP   CB   CG   sing N N 395 
TRP   CB   HB2  sing N N 396 
TRP   CB   HB3  sing N N 397 
TRP   CG   CD1  doub Y N 398 
TRP   CG   CD2  sing Y N 399 
TRP   CD1  NE1  sing Y N 400 
TRP   CD1  HD1  sing N N 401 
TRP   CD2  CE2  doub Y N 402 
TRP   CD2  CE3  sing Y N 403 
TRP   NE1  CE2  sing Y N 404 
TRP   NE1  HE1  sing N N 405 
TRP   CE2  CZ2  sing Y N 406 
TRP   CE3  CZ3  doub Y N 407 
TRP   CE3  HE3  sing N N 408 
TRP   CZ2  CH2  doub Y N 409 
TRP   CZ2  HZ2  sing N N 410 
TRP   CZ3  CH2  sing Y N 411 
TRP   CZ3  HZ3  sing N N 412 
TRP   CH2  HH2  sing N N 413 
TRP   OXT  HXT  sing N N 414 
TYR   N    CA   sing N N 415 
TYR   N    H    sing N N 416 
TYR   N    H2   sing N N 417 
TYR   CA   C    sing N N 418 
TYR   CA   CB   sing N N 419 
TYR   CA   HA   sing N N 420 
TYR   C    O    doub N N 421 
TYR   C    OXT  sing N N 422 
TYR   CB   CG   sing N N 423 
TYR   CB   HB2  sing N N 424 
TYR   CB   HB3  sing N N 425 
TYR   CG   CD1  doub Y N 426 
TYR   CG   CD2  sing Y N 427 
TYR   CD1  CE1  sing Y N 428 
TYR   CD1  HD1  sing N N 429 
TYR   CD2  CE2  doub Y N 430 
TYR   CD2  HD2  sing N N 431 
TYR   CE1  CZ   doub Y N 432 
TYR   CE1  HE1  sing N N 433 
TYR   CE2  CZ   sing Y N 434 
TYR   CE2  HE2  sing N N 435 
TYR   CZ   OH   sing N N 436 
TYR   OH   HH   sing N N 437 
TYR   OXT  HXT  sing N N 438 
VAL   N    CA   sing N N 439 
VAL   N    H    sing N N 440 
VAL   N    H2   sing N N 441 
VAL   CA   C    sing N N 442 
VAL   CA   CB   sing N N 443 
VAL   CA   HA   sing N N 444 
VAL   C    O    doub N N 445 
VAL   C    OXT  sing N N 446 
VAL   CB   CG1  sing N N 447 
VAL   CB   CG2  sing N N 448 
VAL   CB   HB   sing N N 449 
VAL   CG1  HG11 sing N N 450 
VAL   CG1  HG12 sing N N 451 
VAL   CG1  HG13 sing N N 452 
VAL   CG2  HG21 sing N N 453 
VAL   CG2  HG22 sing N N 454 
VAL   CG2  HG23 sing N N 455 
VAL   OXT  HXT  sing N N 456 
# 
_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                    9M16 
_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]   0.006468 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000630 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023492 
_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]   0.023769 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
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  ? 43.46300 -1.24400  1.76100  1.000 53.14638  ?  123 LYS   A N    1 
ATOM   2    C  CA   . LYS   A 1 18  ? 42.91100 -2.15100  2.76000  1.000 51.44820  ?  123 LYS   A CA   1 
ATOM   3    C  C    . LYS   A 1 18  ? 41.37800 -2.17300  2.74100  1.000 48.86046  ?  123 LYS   A C    1 
ATOM   4    O  O    . LYS   A 1 18  ? 40.77500 -3.24400  2.77600  1.000 49.24185  ?  123 LYS   A O    1 
ATOM   5    C  CB   . LYS   A 1 18  ? 43.39300 -1.77100  4.15800  1.000 49.99435  ?  123 LYS   A CB   1 
ATOM   6    C  CG   . LYS   A 1 18  ? 44.89000 -1.84000  4.37800  1.000 50.76174  ?  123 LYS   A CG   1 
ATOM   7    C  CD   . LYS   A 1 18  ? 45.20400 -2.53900  5.69100  1.000 49.68442  ?  123 LYS   A CD   1 
ATOM   8    C  CE   . LYS   A 1 18  ? 46.54800 -3.26200  5.63200  1.000 50.38098  ?  123 LYS   A CE   1 
ATOM   9    N  NZ   . LYS   A 1 18  ? 46.67000 -4.11600  4.41400  1.000 51.07697  ?  123 LYS   A NZ   1 
ATOM   10   N  N    . LEU   A 1 19  ? 40.74700 -0.99900  2.70100  1.000 47.62514  ?  124 LEU   A N    1 
ATOM   11   C  CA   . LEU   A 1 19  ? 39.28200 -0.91400  2.69100  1.000 47.16460  ?  124 LEU   A CA   1 
ATOM   12   C  C    . LEU   A 1 19  ? 38.79700 -1.20400  1.27500  1.000 47.17665  ?  124 LEU   A C    1 
ATOM   13   O  O    . LEU   A 1 19  ? 38.76800 -0.32800  0.41000  1.000 48.85622  ?  124 LEU   A O    1 
ATOM   14   C  CB   . LEU   A 1 19  ? 38.81600 0.45400   3.17700  1.000 46.83735  ?  124 LEU   A CB   1 
ATOM   15   C  CG   . LEU   A 1 19  ? 37.37400 0.64700   3.66200  1.000 44.77382  ?  124 LEU   A CG   1 
ATOM   16   C  CD1  . LEU   A 1 19  ? 36.98000 -0.34600  4.75900  1.000 42.03465  ?  124 LEU   A CD1  1 
ATOM   17   C  CD2  . LEU   A 1 19  ? 37.17800 2.08100   4.13800  1.000 44.25191  ?  124 LEU   A CD2  1 
ATOM   18   N  N    . SER   A 1 20  ? 38.40000 -2.45500  1.04300  1.000 45.96886  ?  125 SER   A N    1 
ATOM   19   C  CA   . SER   A 1 20  ? 38.06600 -2.92800  -0.29300 1.000 46.06358  ?  125 SER   A CA   1 
ATOM   20   C  C    . SER   A 1 20  ? 36.85300 -2.18300  -0.85700 1.000 47.18559  ?  125 SER   A C    1 
ATOM   21   O  O    . SER   A 1 20  ? 36.17000 -1.41900  -0.16200 1.000 44.20170  ?  125 SER   A O    1 
ATOM   22   C  CB   . SER   A 1 20  ? 37.77500 -4.42900  -0.26900 1.000 45.96883  ?  125 SER   A CB   1 
ATOM   23   O  OG   . SER   A 1 20  ? 36.50700 -4.68400  0.33900  1.000 44.51910  ?  125 SER   A OG   1 
ATOM   24   N  N    . GLU   A 1 21  ? 36.59800 -2.42800  -2.14800 1.000 49.18972  ?  126 GLU   A N    1 
ATOM   25   C  CA   . GLU   A 1 21  ? 35.41100 -1.89200  -2.81100 1.000 50.78442  ?  126 GLU   A CA   1 
ATOM   26   C  C    . GLU   A 1 21  ? 34.13200 -2.39800  -2.15300 1.000 45.09239  ?  126 GLU   A C    1 
ATOM   27   O  O    . GLU   A 1 21  ? 33.19500 -1.62800  -1.91700 1.000 40.47342  ?  126 GLU   A O    1 
ATOM   28   C  CB   . GLU   A 1 21  ? 35.42000 -2.28100  -4.29000 1.000 57.61484  ?  126 GLU   A CB   1 
ATOM   29   C  CG   . GLU   A 1 21  ? 36.63000 -1.79700  -5.06800 1.000 65.29692  ?  126 GLU   A CG   1 
ATOM   30   C  CD   . GLU   A 1 21  ? 36.29700 -0.62200  -5.96300 1.000 70.91576  ?  126 GLU   A CD   1 
ATOM   31   O  OE1  . GLU   A 1 21  ? 36.46500 -0.74700  -7.19700 1.000 76.34886  ?  126 GLU   A OE1  1 
ATOM   32   O  OE2  . GLU   A 1 21  ? 35.86400 0.42400   -5.42900 1.000 70.89583  ?  126 GLU   A OE2  1 
ATOM   33   N  N    . GLU   A 1 22  ? 34.07300 -3.70500  -1.88100 1.000 44.63265  ?  127 GLU   A N    1 
ATOM   34   C  CA   . GLU   A 1 22  ? 32.92300 -4.29100  -1.20800 1.000 43.48869  ?  127 GLU   A CA   1 
ATOM   35   C  C    . GLU   A 1 22  ? 32.69500 -3.65300  0.15600  1.000 38.27550  ?  127 GLU   A C    1 
ATOM   36   O  O    . GLU   A 1 22  ? 31.54700 -3.41400  0.55000  1.000 35.11470  ?  127 GLU   A O    1 
ATOM   37   C  CB   . GLU   A 1 22  ? 33.11600 -5.80200  -1.07000 1.000 49.16122  ?  127 GLU   A CB   1 
ATOM   38   C  CG   . GLU   A 1 22  ? 32.26000 -6.44600  0.01600  1.000 53.68824  ?  127 GLU   A CG   1 
ATOM   39   C  CD   . GLU   A 1 22  ? 31.89800 -7.88700  -0.29200 1.000 59.25675  ?  127 GLU   A CD   1 
ATOM   40   O  OE1  . GLU   A 1 22  ? 31.09600 -8.11400  -1.22100 1.000 61.21217  ?  127 GLU   A OE1  1 
ATOM   41   O  OE2  . GLU   A 1 22  ? 32.41400 -8.79100  0.40000  1.000 61.45643  ?  127 GLU   A OE2  1 
ATOM   42   N  N    . GLN   A 1 23  ? 33.77400 -3.36500  0.89100  1.000 38.27532  ?  128 GLN   A N    1 
ATOM   43   C  CA   . GLN   A 1 23  ? 33.62100 -2.79100  2.22400  1.000 35.03050  ?  128 GLN   A CA   1 
ATOM   44   C  C    . GLN   A 1 23  ? 33.12800 -1.35000  2.14800  1.000 34.73222  ?  128 GLN   A C    1 
ATOM   45   O  O    . GLN   A 1 23  ? 32.28500 -0.93300  2.95300  1.000 34.63243  ?  128 GLN   A O    1 
ATOM   46   C  CB   . GLN   A 1 23  ? 34.93900 -2.89900  3.00000  1.000 33.26286  ?  128 GLN   A CB   1 
ATOM   47   C  CG   . GLN   A 1 23  ? 35.29900 -4.34200  3.37900  1.000 32.71514  ?  128 GLN   A CG   1 
ATOM   48   C  CD   . GLN   A 1 23  ? 36.70900 -4.49000  3.94900  1.000 35.89067  ?  128 GLN   A CD   1 
ATOM   49   O  OE1  . GLN   A 1 23  ? 37.59100 -3.68400  3.67100  1.000 36.24414  ?  128 GLN   A OE1  1 
ATOM   50   N  NE2  . GLN   A 1 23  ? 36.91800 -5.52900  4.75200  1.000 37.11281  ?  128 GLN   A NE2  1 
ATOM   51   N  N    . GLN   A 1 24  ? 33.62200 -0.58100  1.17500  1.000 35.02200  ?  129 GLN   A N    1 
ATOM   52   C  CA   . GLN   A 1 24  ? 33.10500 0.76900   0.96800  1.000 35.48777  ?  129 GLN   A CA   1 
ATOM   53   C  C    . GLN   A 1 24  ? 31.64100 0.73100   0.56900  1.000 32.69624  ?  129 GLN   A C    1 
ATOM   54   O  O    . GLN   A 1 24  ? 30.85800 1.60900   0.95300  1.000 31.08438  ?  129 GLN   A O    1 
ATOM   55   C  CB   . GLN   A 1 24  ? 33.91000 1.49100   -0.11000 1.000 41.35525  ?  129 GLN   A CB   1 
ATOM   56   C  CG   . GLN   A 1 24  ? 35.17500 2.17400   0.37800  1.000 46.22097  ?  129 GLN   A CG   1 
ATOM   57   C  CD   . GLN   A 1 24  ? 36.10800 2.52000   -0.76500 1.000 53.50969  ?  129 GLN   A CD   1 
ATOM   58   O  OE1  . GLN   A 1 24  ? 36.11200 3.64900   -1.25700 1.000 56.14051  ?  129 GLN   A OE1  1 
ATOM   59   N  NE2  . GLN   A 1 24  ? 36.91000 1.55000   -1.19300 1.000 58.16269  ?  129 GLN   A NE2  1 
ATOM   60   N  N    . HIS   A 1 25  ? 31.26000 -0.27000  -0.22400 1.000 31.46520  ?  130 HIS   A N    1 
ATOM   61   C  CA   . HIS   A 1 25  ? 29.86600 -0.42500  -0.61300 1.000 32.78709  ?  130 HIS   A CA   1 
ATOM   62   C  C    . HIS   A 1 25  ? 29.00200 -0.73800  0.60200  1.000 30.74206  ?  130 HIS   A C    1 
ATOM   63   O  O    . HIS   A 1 25  ? 27.92500 -0.15900  0.77700  1.000 30.74828  ?  130 HIS   A O    1 
ATOM   64   C  CB   . HIS   A 1 25  ? 29.74700 -1.52300  -1.67000 1.000 34.99061  ?  130 HIS   A CB   1 
ATOM   65   C  CG   . HIS   A 1 25  ? 28.36600 -1.68600  -2.22600 1.000 37.19999  ?  130 HIS   A CG   1 
ATOM   66   N  ND1  . HIS   A 1 25  ? 27.67700 -0.65200  -2.82200 1.000 38.17746  ?  130 HIS   A ND1  1 
ATOM   67   C  CD2  . HIS   A 1 25  ? 27.55400 -2.76800  -2.29500 1.000 38.23540  ?  130 HIS   A CD2  1 
ATOM   68   C  CE1  . HIS   A 1 25  ? 26.49400 -1.08700  -3.22500 1.000 38.84677  ?  130 HIS   A CE1  1 
ATOM   69   N  NE2  . HIS   A 1 25  ? 26.39600 -2.36800  -2.92000 1.000 38.11555  ?  130 HIS   A NE2  1 
ATOM   70   N  N    . ILE   A 1 26  ? 29.46900 -1.65500  1.45400  1.000 31.64481  ?  131 ILE   A N    1 
ATOM   71   C  CA   . ILE   A 1 26  ? 28.74800 -1.99400  2.68000  1.000 28.87980  ?  131 ILE   A CA   1 
ATOM   72   C  C    . ILE   A 1 26  ? 28.46200 -0.73700  3.49300  1.000 26.67119  ?  131 ILE   A C    1 
ATOM   73   O  O    . ILE   A 1 26  ? 27.33200 -0.50200  3.93900  1.000 25.17325  ?  131 ILE   A O    1 
ATOM   74   C  CB   . ILE   A 1 26  ? 29.55000 -3.02500  3.49400  1.000 29.83813  ?  131 ILE   A CB   1 
ATOM   75   C  CG1  . ILE   A 1 26  ? 29.56200 -4.37400  2.77900  1.000 31.60651  ?  131 ILE   A CG1  1 
ATOM   76   C  CG2  . ILE   A 1 26  ? 28.97000 -3.17900  4.89500  1.000 28.89844  ?  131 ILE   A CG2  1 
ATOM   77   C  CD1  . ILE   A 1 26  ? 30.39100 -5.42100  3.48700  1.000 33.25005  ?  131 ILE   A CD1  1 
ATOM   78   N  N    . ILE   A 1 27  ? 29.48200 0.10100   3.67500  1.000 25.09062  ?  132 ILE   A N    1 
ATOM   79   C  CA   . ILE   A 1 27  ? 29.32600 1.29700   4.49600  1.000 24.52193  ?  132 ILE   A CA   1 
ATOM   80   C  C    . ILE   A 1 27  ? 28.34200 2.27700   3.85800  1.000 26.33194  ?  132 ILE   A C    1 
ATOM   81   O  O    . ILE   A 1 27  ? 27.54600 2.91400   4.55900  1.000 28.07862  ?  132 ILE   A O    1 
ATOM   82   C  CB   . ILE   A 1 27  ? 30.69800 1.94600   4.75300  1.000 27.30078  ?  132 ILE   A CB   1 
ATOM   83   C  CG1  . ILE   A 1 27  ? 31.57100 1.00700   5.59100  1.000 28.16895  ?  132 ILE   A CG1  1 
ATOM   84   C  CG2  . ILE   A 1 27  ? 30.53800 3.28000   5.45300  1.000 26.15562  ?  132 ILE   A CG2  1 
ATOM   85   C  CD1  . ILE   A 1 27  ? 32.99700 1.47400   5.76500  1.000 29.02419  ?  132 ILE   A CD1  1 
ATOM   86   N  N    . ALA   A 1 28  ? 28.37500 2.41700   2.52800  1.000 25.80312  ?  133 ALA   A N    1 
ATOM   87   C  CA   . ALA   A 1 28  ? 27.43400 3.31300   1.85100  1.000 24.94301  ?  133 ALA   A CA   1 
ATOM   88   C  C    . ALA   A 1 28  ? 25.99100 2.85800   2.03400  1.000 25.51674  ?  133 ALA   A C    1 
ATOM   89   O  O    . ALA   A 1 28  ? 25.09000 3.68400   2.23600  1.000 24.65364  ?  133 ALA   A O    1 
ATOM   90   C  CB   . ALA   A 1 28  ? 27.75900 3.40300   0.35700  1.000 24.56334  ?  133 ALA   A CB   1 
ATOM   91   N  N    . ILE   A 1 29  ? 25.74800 1.55000   1.93900  1.000 25.25316  ?  134 ILE   A N    1 
ATOM   92   C  CA   . ILE   A 1 29  ? 24.39300 1.03000   2.08900  1.000 24.30012  ?  134 ILE   A CA   1 
ATOM   93   C  C    . ILE   A 1 29  ? 23.88000 1.29400   3.49600  1.000 23.64352  ?  134 ILE   A C    1 
ATOM   94   O  O    . ILE   A 1 29  ? 22.73700 1.72000   3.69100  1.000 23.71261  ?  134 ILE   A O    1 
ATOM   95   C  CB   . ILE   A 1 29  ? 24.35700 -0.47000  1.75300  1.000 24.92000  ?  134 ILE   A CB   1 
ATOM   96   C  CG1  . ILE   A 1 29  ? 24.50500 -0.68200  0.24700  1.000 29.90622  ?  134 ILE   A CG1  1 
ATOM   97   C  CG2  . ILE   A 1 29  ? 23.05900 -1.10200  2.22700  1.000 21.32111  ?  134 ILE   A CG2  1 
ATOM   98   C  CD1  . ILE   A 1 29  ? 24.70900 -2.13700  -0.13100 1.000 32.62441  ?  134 ILE   A CD1  1 
ATOM   99   N  N    . LEU   A 1 30  ? 24.72200 1.03100   4.50000  1.000 22.81071  ?  135 LEU   A N    1 
ATOM   100  C  CA   . LEU   A 1 30  ? 24.31300 1.19700   5.89200  1.000 21.08175  ?  135 LEU   A CA   1 
ATOM   101  C  C    . LEU   A 1 30  ? 24.06700 2.66400   6.22900  1.000 20.56288  ?  135 LEU   A C    1 
ATOM   102  O  O    . LEU   A 1 30  ? 23.12300 2.99000   6.95700  1.000 18.66703  ?  135 LEU   A O    1 
ATOM   103  C  CB   . LEU   A 1 30  ? 25.37800 0.59900   6.81700  1.000 20.32993  ?  135 LEU   A CB   1 
ATOM   104  C  CG   . LEU   A 1 30  ? 25.50700 -0.92500  6.73800  1.000 19.93266  ?  135 LEU   A CG   1 
ATOM   105  C  CD1  . LEU   A 1 30  ? 26.51400 -1.45000  7.76000  1.000 19.33489  ?  135 LEU   A CD1  1 
ATOM   106  C  CD2  . LEU   A 1 30  ? 24.14900 -1.59000  6.92100  1.000 17.48172  ?  135 LEU   A CD2  1 
ATOM   107  N  N    . LEU   A 1 31  ? 24.90800 3.56700   5.72100  1.000 21.75986  ?  136 LEU   A N    1 
ATOM   108  C  CA   . LEU   A 1 31  ? 24.66200 4.99000   5.94000  1.000 23.17632  ?  136 LEU   A CA   1 
ATOM   109  C  C    . LEU   A 1 31  ? 23.32800 5.41200   5.33500  1.000 24.01653  ?  136 LEU   A C    1 
ATOM   110  O  O    . LEU   A 1 31  ? 22.54900 6.14300   5.96200  1.000 23.70970  ?  136 LEU   A O    1 
ATOM   111  C  CB   . LEU   A 1 31  ? 25.80100 5.81800   5.34900  1.000 24.33978  ?  136 LEU   A CB   1 
ATOM   112  C  CG   . LEU   A 1 31  ? 27.15100 5.70800   6.06800  1.000 23.49752  ?  136 LEU   A CG   1 
ATOM   113  C  CD1  . LEU   A 1 31  ? 28.25600 6.31900   5.21200  1.000 24.60835  ?  136 LEU   A CD1  1 
ATOM   114  C  CD2  . LEU   A 1 31  ? 27.07900 6.38800   7.42900  1.000 24.52668  ?  136 LEU   A CD2  1 
ATOM   115  N  N    . ASP   A 1 32  ? 23.04500 4.94800   4.11900  1.000 24.45189  ?  137 ASP   A N    1 
ATOM   116  C  CA   . ASP   A 1 32  ? 21.77500 5.27500   3.47900  1.000 25.62548  ?  137 ASP   A CA   1 
ATOM   117  C  C    . ASP   A 1 32  ? 20.61000 4.68600   4.25700  1.000 24.69456  ?  137 ASP   A C    1 
ATOM   118  O  O    . ASP   A 1 32  ? 19.59600 5.36100   4.47500  1.000 23.72009  ?  137 ASP   A O    1 
ATOM   119  C  CB   . ASP   A 1 32  ? 21.77700 4.76900   2.03500  1.000 28.30905  ?  137 ASP   A CB   1 
ATOM   120  C  CG   . ASP   A 1 32  ? 20.47700 5.07200   1.30700  1.000 31.94084  ?  137 ASP   A CG   1 
ATOM   121  O  OD1  . ASP   A 1 32  ? 19.77600 4.11400   0.91800  1.000 32.48632  ?  137 ASP   A OD1  1 
ATOM   122  O  OD2  . ASP   A 1 32  ? 20.15900 6.26700   1.13100  1.000 33.53967  ?  137 ASP   A OD2  1 
ATOM   123  N  N    . ALA   A 1 33  ? 20.73900 3.42600   4.68300  1.000 24.80643  ?  138 ALA   A N    1 
ATOM   124  C  CA   . ALA   A 1 33  ? 19.67200 2.78900   5.45000  1.000 22.26487  ?  138 ALA   A CA   1 
ATOM   125  C  C    . ALA   A 1 33  ? 19.37700 3.56100   6.72800  1.000 22.20231  ?  138 ALA   A C    1 
ATOM   126  O  O    . ALA   A 1 33  ? 18.21000 3.71900   7.11100  1.000 20.62152  ?  138 ALA   A O    1 
ATOM   127  C  CB   . ALA   A 1 33  ? 20.04500 1.34600   5.77300  1.000 21.21105  ?  138 ALA   A CB   1 
ATOM   128  N  N    . HIS   A 1 34  ? 20.42600 4.04500   7.40900  1.000 20.02974  ?  139 HIS   A N    1 
ATOM   129  C  CA   . HIS   A 1 34  ? 20.21500 4.85700   8.60600  1.000 20.22073  ?  139 HIS   A CA   1 
ATOM   130  C  C    . HIS   A 1 34  ? 19.50600 6.16000   8.26400  1.000 21.65247  ?  139 HIS   A C    1 
ATOM   131  O  O    . HIS   A 1 34  ? 18.56600 6.56600   8.95800  1.000 20.43010  ?  139 HIS   A O    1 
ATOM   132  C  CB   . HIS   A 1 34  ? 21.55100 5.15500   9.28900  1.000 21.33482  ?  139 HIS   A CB   1 
ATOM   133  C  CG   . HIS   A 1 34  ? 21.41800 5.93100   10.56300 1.000 22.29282  ?  139 HIS   A CG   1 
ATOM   134  N  ND1  . HIS   A 1 34  ? 20.58500 5.53700   11.58600 1.000 21.81920  ?  139 HIS   A ND1  1 
ATOM   135  C  CD2  . HIS   A 1 34  ? 22.02600 7.06600   10.98800 1.000 22.92491  ?  139 HIS   A CD2  1 
ATOM   136  C  CE1  . HIS   A 1 34  ? 20.67900 6.39700   12.58600 1.000 22.16826  ?  139 HIS   A CE1  1 
ATOM   137  N  NE2  . HIS   A 1 34  ? 21.54300 7.33700   12.24700 1.000 22.62216  ?  139 HIS   A NE2  1 
ATOM   138  N  N    A HIS   A 1 35  ? 19.93600 6.82800   7.19200  0.550 23.37387  ?  140 HIS   A N    1 
ATOM   139  N  N    B HIS   A 1 35  ? 19.95400 6.82500   7.19400  0.450 23.37130  ?  140 HIS   A N    1 
ATOM   140  C  CA   A HIS   A 1 35  ? 19.31100 8.09100   6.81500  0.550 23.99214  ?  140 HIS   A CA   1 
ATOM   141  C  CA   B HIS   A 1 35  ? 19.34400 8.07200   6.74200  0.450 24.05063  ?  140 HIS   A CA   1 
ATOM   142  C  C    A HIS   A 1 35  ? 17.84000 7.90500   6.46600  0.550 23.19069  ?  140 HIS   A C    1 
ATOM   143  C  C    B HIS   A 1 35  ? 17.85600 7.89300   6.47400  0.450 23.17695  ?  140 HIS   A C    1 
ATOM   144  O  O    A HIS   A 1 35  ? 17.02500 8.80200   6.71400  0.550 22.71178  ?  140 HIS   A O    1 
ATOM   145  O  O    B HIS   A 1 35  ? 17.04800 8.77700   6.78300  0.450 22.68503  ?  140 HIS   A O    1 
ATOM   146  C  CB   A HIS   A 1 35  ? 20.06800 8.71800   5.64200  0.550 25.84469  ?  140 HIS   A CB   1 
ATOM   147  C  CB   B HIS   A 1 35  ? 20.06900 8.55600   5.48300  0.450 25.79780  ?  140 HIS   A CB   1 
ATOM   148  C  CG   A HIS   A 1 35  ? 21.46600 9.13600   5.98600  0.550 27.41077  ?  140 HIS   A CG   1 
ATOM   149  C  CG   B HIS   A 1 35  ? 19.40200 9.69800   4.78000  0.450 26.77563  ?  140 HIS   A CG   1 
ATOM   150  N  ND1  A HIS   A 1 35  ? 21.81900 9.58900   7.23900  0.550 27.97535  ?  140 HIS   A ND1  1 
ATOM   151  N  ND1  B HIS   A 1 35  ? 19.58300 11.01200  5.15500  0.450 27.72985  ?  140 HIS   A ND1  1 
ATOM   152  C  CD2  A HIS   A 1 35  ? 22.59900 9.16300   5.24400  0.550 29.32522  ?  140 HIS   A CD2  1 
ATOM   153  C  CD2  B HIS   A 1 35  ? 18.58700 9.72600   3.69800  0.450 27.49020  ?  140 HIS   A CD2  1 
ATOM   154  C  CE1  A HIS   A 1 35  ? 23.10900 9.88000   7.25400  0.550 28.83321  ?  140 HIS   A CE1  1 
ATOM   155  C  CE1  B HIS   A 1 35  ? 18.89300 11.79800  4.34800  0.450 28.15442  ?  140 HIS   A CE1  1 
ATOM   156  N  NE2  A HIS   A 1 35  ? 23.60500 9.63100   6.05500  0.550 29.64054  ?  140 HIS   A NE2  1 
ATOM   157  N  NE2  B HIS   A 1 35  ? 18.28100 11.04300  3.45400  0.450 28.05438  ?  140 HIS   A NE2  1 
ATOM   158  N  N    . LYS   A 1 36  ? 17.47800 6.74900   5.91300  1.000 22.51971  ?  141 LYS   A N    1 
ATOM   159  C  CA   . LYS   A 1 36  ? 16.09300 6.48700   5.56300  1.000 23.34772  ?  141 LYS   A CA   1 
ATOM   160  C  C    . LYS   A 1 36  ? 15.24800 6.06200   6.75800  1.000 23.03613  ?  141 LYS   A C    1 
ATOM   161  O  O    . LYS   A 1 36  ? 14.02200 6.07300   6.65400  1.000 22.18214  ?  141 LYS   A O    1 
ATOM   162  C  CB   . LYS   A 1 36  ? 16.03600 5.42100   4.46500  1.000 24.66543  ?  141 LYS   A CB   1 
ATOM   163  C  CG   . LYS   A 1 36  ? 16.40400 5.95700   3.07500  1.000 29.30418  ?  141 LYS   A CG   1 
ATOM   164  C  CD   . LYS   A 1 36  ? 16.68000 4.83400   2.08500  1.000 32.66057  ?  141 LYS   A CD   1 
ATOM   165  C  CE   . LYS   A 1 36  ? 16.54700 5.31600   0.62900  1.000 36.76868  ?  141 LYS   A CE   1 
ATOM   166  N  NZ   . LYS   A 1 36  ? 17.23500 6.62300   0.37000  1.000 40.13164  ?  141 LYS   A NZ   1 
ATOM   167  N  N    . THR   A 1 37  ? 15.85500 5.70500   7.89100  1.000 21.48886  ?  142 THR   A N    1 
ATOM   168  C  CA   . THR   A 1 37  ? 15.09300 5.22300   9.03600  1.000 20.51569  ?  142 THR   A CA   1 
ATOM   169  C  C    . THR   A 1 37  ? 15.28900 6.04300   10.30400 1.000 21.66124  ?  142 THR   A C    1 
ATOM   170  O  O    . THR   A 1 37  ? 14.71600 5.68700   11.34200 1.000 22.01470  ?  142 THR   A O    1 
ATOM   171  C  CB   . THR   A 1 37  ? 15.44500 3.76100   9.33900  1.000 20.26759  ?  142 THR   A CB   1 
ATOM   172  O  OG1  . THR   A 1 37  ? 16.86800 3.63500   9.49300  1.000 20.65312  ?  142 THR   A OG1  1 
ATOM   173  C  CG2  . THR   A 1 37  ? 14.96700 2.84800   8.22900  1.000 19.47835  ?  142 THR   A CG2  1 
ATOM   174  N  N    . TYR   A 1 38  ? 16.09400 7.10100   10.27200 1.000 22.01104  ?  143 TYR   A N    1 
ATOM   175  C  CA   . TYR   A 1 38  ? 16.24700 8.00400   11.40800 1.000 22.39582  ?  143 TYR   A CA   1 
ATOM   176  C  C    . TYR   A 1 38  ? 15.88100 9.40400   10.93700 1.000 24.26040  ?  143 TYR   A C    1 
ATOM   177  O  O    . TYR   A 1 38  ? 16.54600 9.95800   10.05400 1.000 25.59190  ?  143 TYR   A O    1 
ATOM   178  C  CB   . TYR   A 1 38  ? 17.67600 7.97900   11.98100 1.000 21.28891  ?  143 TYR   A CB   1 
ATOM   179  C  CG   . TYR   A 1 38  ? 17.76100 8.62100   13.35300 1.000 20.26252  ?  143 TYR   A CG   1 
ATOM   180  C  CD1  . TYR   A 1 38  ? 17.73500 10.00200  13.49400 1.000 21.26910  ?  143 TYR   A CD1  1 
ATOM   181  C  CD2  . TYR   A 1 38  ? 17.82200 7.84600   14.50600 1.000 16.85967  ?  143 TYR   A CD2  1 
ATOM   182  C  CE1  . TYR   A 1 38  ? 17.78400 10.59500  14.73700 1.000 21.01684  ?  143 TYR   A CE1  1 
ATOM   183  C  CE2  . TYR   A 1 38  ? 17.86500 8.43500   15.76000 1.000 17.00263  ?  143 TYR   A CE2  1 
ATOM   184  C  CZ   . TYR   A 1 38  ? 17.84700 9.81100   15.86200 1.000 19.42168  ?  143 TYR   A CZ   1 
ATOM   185  O  OH   . TYR   A 1 38  ? 17.89300 10.41600  17.09300 1.000 22.05783  ?  143 TYR   A OH   1 
ATOM   186  N  N    . ASP   A 1 39  ? 14.82900 9.97400   11.53000 1.000 24.31530  ?  144 ASP   A N    1 
ATOM   187  C  CA   . ASP   A 1 39  ? 14.38200 11.31600  11.18900 1.000 26.07787  ?  144 ASP   A CA   1 
ATOM   188  C  C    . ASP   A 1 39  ? 14.84000 12.28400  12.27200 1.000 27.42343  ?  144 ASP   A C    1 
ATOM   189  O  O    . ASP   A 1 39  ? 14.19900 12.36900  13.33400 1.000 28.40444  ?  144 ASP   A O    1 
ATOM   190  C  CB   . ASP   A 1 39  ? 12.86000 11.34400  11.03400 1.000 27.59494  ?  144 ASP   A CB   1 
ATOM   191  C  CG   . ASP   A 1 39  ? 12.30300 12.74800  10.85000 1.000 29.49173  ?  144 ASP   A CG   1 
ATOM   192  O  OD1  . ASP   A 1 39  ? 13.07200 13.68500  10.55000 1.000 29.02759  ?  144 ASP   A OD1  1 
ATOM   193  O  OD2  . ASP   A 1 39  ? 11.07100 12.90900  10.99600 1.000 29.61780  ?  144 ASP   A OD2  1 
ATOM   194  N  N    . PRO   A 1 40  ? 15.92600 13.03900  12.05900 1.000 26.97168  ?  145 PRO   A N    1 
ATOM   195  C  CA   . PRO   A 1 40  ? 16.43000 13.93600  13.11000 1.000 27.57314  ?  145 PRO   A CA   1 
ATOM   196  C  C    . PRO   A 1 40  ? 15.56500 15.16000  13.34300 1.000 29.52901  ?  145 PRO   A C    1 
ATOM   197  O  O    . PRO   A 1 40  ? 15.91000 15.98200  14.19800 1.000 29.66593  ?  145 PRO   A O    1 
ATOM   198  C  CB   . PRO   A 1 40  ? 17.82200 14.34200  12.58900 1.000 26.90961  ?  145 PRO   A CB   1 
ATOM   199  C  CG   . PRO   A 1 40  ? 17.69500 14.28100  11.11400 1.000 27.49895  ?  145 PRO   A CG   1 
ATOM   200  C  CD   . PRO   A 1 40  ? 16.72500 13.13600  10.82100 1.000 27.65025  ?  145 PRO   A CD   1 
ATOM   201  N  N    . THR   A 1 41  ? 14.46900 15.32500  12.60300 1.000 29.91257  ?  146 THR   A N    1 
ATOM   202  C  CA   . THR   A 1 41  ? 13.49900 16.35900  12.92900 1.000 31.08649  ?  146 THR   A CA   1 
ATOM   203  C  C    . THR   A 1 41  ? 12.45400 15.89100  13.93400 1.000 30.20642  ?  146 THR   A C    1 
ATOM   204  O  O    . THR   A 1 41  ? 11.79300 16.73300  14.55400 1.000 31.69739  ?  146 THR   A O    1 
ATOM   205  C  CB   . THR   A 1 41  ? 12.80600 16.86400  11.65700 1.000 32.23292  ?  146 THR   A CB   1 
ATOM   206  O  OG1  . THR   A 1 41  ? 11.81100 15.92200  11.23300 1.000 30.99174  ?  146 THR   A OG1  1 
ATOM   207  C  CG2  . THR   A 1 41  ? 13.82400 17.05000  10.54700 1.000 33.40862  ?  146 THR   A CG2  1 
ATOM   208  N  N    . TYR   A 1 42  ? 12.30200 14.57600  14.11700 1.000 27.68332  ?  147 TYR   A N    1 
ATOM   209  C  CA   . TYR   A 1 42  ? 11.37100 14.00500  15.09600 1.000 26.18074  ?  147 TYR   A CA   1 
ATOM   210  C  C    . TYR   A 1 42  ? 9.94300  14.49900  14.87700 1.000 27.39949  ?  147 TYR   A C    1 
ATOM   211  O  O    . TYR   A 1 42  ? 9.18200  14.67200  15.83100 1.000 26.11096  ?  147 TYR   A O    1 
ATOM   212  C  CB   . TYR   A 1 42  ? 11.82900 14.29500  16.53000 1.000 25.59920  ?  147 TYR   A CB   1 
ATOM   213  C  CG   . TYR   A 1 42  ? 13.28600 13.92700  16.77500 1.000 25.97861  ?  147 TYR   A CG   1 
ATOM   214  C  CD1  . TYR   A 1 42  ? 14.26300 14.90500  16.89900 1.000 26.80667  ?  147 TYR   A CD1  1 
ATOM   215  C  CD2  . TYR   A 1 42  ? 13.67800 12.59800  16.85000 1.000 25.19719  ?  147 TYR   A CD2  1 
ATOM   216  C  CE1  . TYR   A 1 42  ? 15.59600 14.56500  17.10500 1.000 27.40831  ?  147 TYR   A CE1  1 
ATOM   217  C  CE2  . TYR   A 1 42  ? 14.99300 12.24700  17.04900 1.000 25.55122  ?  147 TYR   A CE2  1 
ATOM   218  C  CZ   . TYR   A 1 42  ? 15.95000 13.23200  17.17800 1.000 26.39733  ?  147 TYR   A CZ   1 
ATOM   219  O  OH   . TYR   A 1 42  ? 17.25500 12.86700  17.37500 1.000 27.49519  ?  147 TYR   A OH   1 
ATOM   220  N  N    . ALA   A 1 43  ? 9.57000  14.73200  13.61500 1.000 28.57349  ?  148 ALA   A N    1 
ATOM   221  C  CA   . ALA   A 1 43  ? 8.25300  15.30000  13.33300 1.000 29.60606  ?  148 ALA   A CA   1 
ATOM   222  C  C    . ALA   A 1 43  ? 7.12200  14.33500  13.67000 1.000 30.26458  ?  148 ALA   A C    1 
ATOM   223  O  O    . ALA   A 1 43  ? 6.00500  14.77800  13.95800 1.000 29.14930  ?  148 ALA   A O    1 
ATOM   224  C  CB   . ALA   A 1 43  ? 8.15600  15.71400  11.86500 1.000 29.56470  ?  148 ALA   A CB   1 
ATOM   225  N  N    . ASP   A 1 44  ? 7.38300  13.02300  13.63700 1.000 30.01852  ?  149 ASP   A N    1 
ATOM   226  C  CA   . ASP   A 1 44  ? 6.31900  12.04900  13.86900 1.000 29.18983  ?  149 ASP   A CA   1 
ATOM   227  C  C    . ASP   A 1 44  ? 5.88500  11.98300  15.32800 1.000 27.94132  ?  149 ASP   A C    1 
ATOM   228  O  O    . ASP   A 1 44  ? 4.80500  11.44900  15.61300 1.000 27.12489  ?  149 ASP   A O    1 
ATOM   229  C  CB   . ASP   A 1 44  ? 6.75700  10.65800  13.41300 1.000 29.30191  ?  149 ASP   A CB   1 
ATOM   230  C  CG   . ASP   A 1 44  ? 6.97700  10.57600  11.91400 1.000 33.05540  ?  149 ASP   A CG   1 
ATOM   231  O  OD1  . ASP   A 1 44  ? 6.30000  11.32000  11.16700 1.000 34.71513  ?  149 ASP   A OD1  1 
ATOM   232  O  OD2  . ASP   A 1 44  ? 7.82000  9.75900   11.48300 1.000 33.56975  ?  149 ASP   A OD2  1 
ATOM   233  N  N    . PHE   A 1 45  ? 6.69200  12.50900  16.25400 1.000 26.96059  ?  150 PHE   A N    1 
ATOM   234  C  CA   . PHE   A 1 45  ? 6.37200  12.39200  17.67500 1.000 27.42770  ?  150 PHE   A CA   1 
ATOM   235  C  C    . PHE   A 1 45  ? 5.01500  13.00000  18.01700 1.000 28.78531  ?  150 PHE   A C    1 
ATOM   236  O  O    . PHE   A 1 45  ? 4.43400  12.65400  19.05300 1.000 28.55304  ?  150 PHE   A O    1 
ATOM   237  C  CB   . PHE   A 1 45  ? 7.46200  13.05500  18.52900 1.000 26.76609  ?  150 PHE   A CB   1 
ATOM   238  C  CG   . PHE   A 1 45  ? 8.72700  12.23100  18.68700 1.000 26.61218  ?  150 PHE   A CG   1 
ATOM   239  C  CD1  . PHE   A 1 45  ? 9.25900  11.52100  17.62200 1.000 26.97244  ?  150 PHE   A CD1  1 
ATOM   240  C  CD2  . PHE   A 1 45  ? 9.40300  12.20600  19.89900 1.000 24.84868  ?  150 PHE   A CD2  1 
ATOM   241  C  CE1  . PHE   A 1 45  ? 10.43600 10.78500  17.77300 1.000 26.70146  ?  150 PHE   A CE1  1 
ATOM   242  C  CE2  . PHE   A 1 45  ? 10.57700 11.47000  20.05400 1.000 24.78014  ?  150 PHE   A CE2  1 
ATOM   243  C  CZ   . PHE   A 1 45  ? 11.09400 10.76800  18.99000 1.000 24.82644  ?  150 PHE   A CZ   1 
ATOM   244  N  N    . ARG   A 1 46  ? 4.49800  13.90100  17.18200 1.000 32.36327  ?  151 ARG   A N    1 
ATOM   245  C  CA   . ARG   A 1 46  ? 3.19300  14.48700  17.45800 1.000 35.92568  ?  151 ARG   A CA   1 
ATOM   246  C  C    . ARG   A 1 46  ? 2.06400  13.47800  17.26500 1.000 32.93773  ?  151 ARG   A C    1 
ATOM   247  O  O    . ARG   A 1 46  ? 0.94300  13.72600  17.72000 1.000 33.30153  ?  151 ARG   A O    1 
ATOM   248  C  CB   . ARG   A 1 46  ? 2.97500  15.72900  16.58000 1.000 42.93385  ?  151 ARG   A CB   1 
ATOM   249  C  CG   . ARG   A 1 46  ? 2.64000  15.45300  15.10900 1.000 49.30874  ?  151 ARG   A CG   1 
ATOM   250  C  CD   . ARG   A 1 46  ? 1.12500  15.39400  14.87000 1.000 55.35253  ?  151 ARG   A CD   1 
ATOM   251  N  NE   . ARG   A 1 46  ? 0.74700  15.61800  13.47600 1.000 60.31327  ?  151 ARG   A NE   1 
ATOM   252  C  CZ   . ARG   A 1 46  ? -0.50300 15.53200  13.02100 1.000 65.24522  ?  151 ARG   A CZ   1 
ATOM   253  N  NH1  . ARG   A 1 46  ? -0.76700 15.75000  11.73700 1.000 67.83798  ?  151 ARG   A NH1  1 
ATOM   254  N  NH2  . ARG   A 1 46  ? -1.49200 15.21700  13.85000 1.000 65.04989  ?  151 ARG   A NH2  1 
ATOM   255  N  N    . ASP   A 1 47  ? 2.33500  12.35200  16.60100 1.000 30.82562  ?  152 ASP   A N    1 
ATOM   256  C  CA   . ASP   A 1 47  ? 1.33200  11.31000  16.42400 1.000 29.82169  ?  152 ASP   A CA   1 
ATOM   257  C  C    . ASP   A 1 47  ? 1.17300  10.42500  17.64900 1.000 27.40922  ?  152 ASP   A C    1 
ATOM   258  O  O    . ASP   A 1 47  ? 0.18500  9.69000   17.73200 1.000 27.06920  ?  152 ASP   A O    1 
ATOM   259  C  CB   . ASP   A 1 47  ? 1.68300  10.41400  15.23500 1.000 31.29365  ?  152 ASP   A CB   1 
ATOM   260  C  CG   . ASP   A 1 47  ? 1.80700  11.18200  13.93500 1.000 35.62827  ?  152 ASP   A CG   1 
ATOM   261  O  OD1  . ASP   A 1 47  ? 1.23600  12.28800  13.83800 1.000 37.48697  ?  152 ASP   A OD1  1 
ATOM   262  O  OD2  . ASP   A 1 47  ? 2.46300  10.66700  13.00300 1.000 36.64414  ?  152 ASP   A OD2  1 
ATOM   263  N  N    . PHE   A 1 48  ? 2.13100  10.44800  18.57400 1.000 25.68443  ?  153 PHE   A N    1 
ATOM   264  C  CA   . PHE   A 1 48  ? 2.09300  9.56200   19.72500 1.000 23.71534  ?  153 PHE   A CA   1 
ATOM   265  C  C    . PHE   A 1 48  ? 1.07500  10.06300  20.74500 1.000 24.53766  ?  153 PHE   A C    1 
ATOM   266  O  O    . PHE   A 1 48  ? 0.71100  11.24100  20.77100 1.000 26.98766  ?  153 PHE   A O    1 
ATOM   267  C  CB   . PHE   A 1 48  ? 3.46500  9.46900   20.40600 1.000 22.64888  ?  153 PHE   A CB   1 
ATOM   268  C  CG   . PHE   A 1 48  ? 4.60100  9.10100   19.48400 1.000 22.32412  ?  153 PHE   A CG   1 
ATOM   269  C  CD1  . PHE   A 1 48  ? 5.90700  9.38500   19.84500 1.000 22.82255  ?  153 PHE   A CD1  1 
ATOM   270  C  CD2  . PHE   A 1 48  ? 4.37400  8.45200   18.28300 1.000 22.64353  ?  153 PHE   A CD2  1 
ATOM   271  C  CE1  . PHE   A 1 48  ? 6.96600  9.05000   19.02300 1.000 23.30300  ?  153 PHE   A CE1  1 
ATOM   272  C  CE2  . PHE   A 1 48  ? 5.42600  8.12000   17.44700 1.000 23.54741  ?  153 PHE   A CE2  1 
ATOM   273  C  CZ   . PHE   A 1 48  ? 6.73100  8.41500   17.82300 1.000 23.61107  ?  153 PHE   A CZ   1 
ATOM   274  N  N    . ARG   A 1 49  ? 0.63400  9.15400   21.61100 1.000 22.66878  ?  154 ARG   A N    1 
ATOM   275  C  CA   . ARG   A 1 49  ? -0.17100 9.58000   22.74000 1.000 24.65056  ?  154 ARG   A CA   1 
ATOM   276  C  C    . ARG   A 1 49  ? 0.63800  10.57100  23.57900 1.000 26.79669  ?  154 ARG   A C    1 
ATOM   277  O  O    . ARG   A 1 49  ? 1.86500  10.46300  23.66200 1.000 23.78796  ?  154 ARG   A O    1 
ATOM   278  C  CB   . ARG   A 1 49  ? -0.60500 8.37700   23.57600 1.000 25.02781  ?  154 ARG   A CB   1 
ATOM   279  C  CG   . ARG   A 1 49  ? -1.70600 7.55000   22.92800 1.000 24.25031  ?  154 ARG   A CG   1 
ATOM   280  C  CD   . ARG   A 1 49  ? -1.89000 6.21500   23.63100 1.000 23.89227  ?  154 ARG   A CD   1 
ATOM   281  N  NE   . ARG   A 1 49  ? -0.81900 5.27100   23.31500 1.000 23.05899  ?  154 ARG   A NE   1 
ATOM   282  C  CZ   . ARG   A 1 49  ? -0.59800 4.14200   23.98500 1.000 21.06010  ?  154 ARG   A CZ   1 
ATOM   283  N  NH1  . ARG   A 1 49  ? -1.36400 3.81700   25.01600 1.000 20.06536  ?  154 ARG   A NH1  1 
ATOM   284  N  NH2  . ARG   A 1 49  ? 0.38800  3.33400   23.62400 1.000 18.94624  ?  154 ARG   A NH2  1 
ATOM   285  N  N    . PRO   A 1 50  ? -0.02000 11.55400  24.19000 1.000 29.62517  ?  155 PRO   A N    1 
ATOM   286  C  CA   . PRO   A 1 50  ? 0.70100  12.70300  24.76800 1.000 29.51964  ?  155 PRO   A CA   1 
ATOM   287  C  C    . PRO   A 1 50  ? 1.54200  12.31200  25.97000 1.000 28.97835  ?  155 PRO   A C    1 
ATOM   288  O  O    . PRO   A 1 50  ? 1.12400  11.49600  26.80700 1.000 28.06701  ?  155 PRO   A O    1 
ATOM   289  C  CB   . PRO   A 1 50  ? -0.42800 13.66200  25.18300 1.000 31.73361  ?  155 PRO   A CB   1 
ATOM   290  C  CG   . PRO   A 1 50  ? -1.64100 13.21100  24.42000 1.000 32.79526  ?  155 PRO   A CG   1 
ATOM   291  C  CD   . PRO   A 1 50  ? -1.48200 11.73600  24.22700 1.000 31.48772  ?  155 PRO   A CD   1 
ATOM   292  N  N    . PRO   A 1 51  ? 2.72800  12.90400  26.10700 1.000 29.48056  ?  156 PRO   A N    1 
ATOM   293  C  CA   . PRO   A 1 51  ? 3.48800  12.74400  27.35000 1.000 30.75543  ?  156 PRO   A CA   1 
ATOM   294  C  C    . PRO   A 1 51  ? 2.73100  13.37300  28.50900 1.000 33.73094  ?  156 PRO   A C    1 
ATOM   295  O  O    . PRO   A 1 51  ? 2.09300  14.41600  28.36100 1.000 34.85615  ?  156 PRO   A O    1 
ATOM   296  C  CB   . PRO   A 1 51  ? 4.80600  13.48500  27.07100 1.000 30.85610  ?  156 PRO   A CB   1 
ATOM   297  C  CG   . PRO   A 1 51  ? 4.76200  13.91700  25.64000 1.000 30.87965  ?  156 PRO   A CG   1 
ATOM   298  C  CD   . PRO   A 1 51  ? 3.32600  13.90600  25.21200 1.000 30.65784  ?  156 PRO   A CD   1 
ATOM   299  N  N    . VAL   A 1 52  ? 2.78700  12.71800  29.66500 1.000 36.27915  ?  157 VAL   A N    1 
ATOM   300  C  CA   . VAL   A 1 52  ? 2.23600  13.26300  30.90200 1.000 40.74896  ?  157 VAL   A CA   1 
ATOM   301  C  C    . VAL   A 1 52  ? 3.31900  13.20500  31.97300 1.000 45.87412  ?  157 VAL   A C    1 
ATOM   302  O  O    . VAL   A 1 52  ? 3.79300  12.11700  32.32500 1.000 42.77155  ?  157 VAL   A O    1 
ATOM   303  C  CB   . VAL   A 1 52  ? 0.97400  12.51300  31.35600 1.000 39.47130  ?  157 VAL   A CB   1 
ATOM   304  C  CG1  . VAL   A 1 52  ? 0.36500  13.20100  32.56500 1.000 40.11593  ?  157 VAL   A CG1  1 
ATOM   305  C  CG2  . VAL   A 1 52  ? -0.04400 12.46400  30.22100 1.000 38.74954  ?  157 VAL   A CG2  1 
ATOM   306  N  N    . ARG   A 1 53  ? 3.70200  14.36900  32.49400 1.000 54.36985  ?  158 ARG   A N    1 
ATOM   307  C  CA   . ARG   A 1 53  ? 4.79400  14.46500  33.45500 1.000 62.33526  ?  158 ARG   A CA   1 
ATOM   308  C  C    . ARG   A 1 53  ? 4.36600  15.04800  34.79200 1.000 77.08833  ?  158 ARG   A C    1 
ATOM   309  O  O    . ARG   A 1 53  ? 4.70600  14.47900  35.83600 1.000 77.55068  ?  158 ARG   A O    1 
ATOM   310  C  CB   . ARG   A 1 53  ? 5.93700  15.30500  32.86600 1.000 57.86605  ?  158 ARG   A CB   1 
ATOM   311  C  CG   . ARG   A 1 53  ? 6.66700  14.62800  31.72300 1.000 52.84617  ?  158 ARG   A CG   1 
ATOM   312  C  CD   . ARG   A 1 53  ? 7.71500  15.53500  31.12600 1.000 50.13104  ?  158 ARG   A CD   1 
ATOM   313  N  NE   . ARG   A 1 53  ? 8.53600  14.83000  30.14900 1.000 46.58331  ?  158 ARG   A NE   1 
ATOM   314  C  CZ   . ARG   A 1 53  ? 8.32000  14.86000  28.83800 1.000 43.99038  ?  158 ARG   A CZ   1 
ATOM   315  N  NH1  . ARG   A 1 53  ? 7.30600  15.56000  28.34700 1.000 42.36265  ?  158 ARG   A NH1  1 
ATOM   316  N  NH2  . ARG   A 1 53  ? 9.12100  14.19300  28.01700 1.000 42.63263  ?  158 ARG   A NH2  1 
ATOM   317  N  N    . MET   A 1 54  ? 3.62300  16.15700  34.78100 1.000 91.03878  ?  159 MET   A N    1 
ATOM   318  C  CA   . MET   A 1 54  ? 3.31800  16.97600  35.96600 1.000 103.69976 ?  159 MET   A CA   1 
ATOM   319  C  C    . MET   A 1 54  ? 3.25900  16.22600  37.29500 1.000 105.55608 ?  159 MET   A C    1 
ATOM   320  O  O    . MET   A 1 54  ? 4.24600  16.18000  38.03000 1.000 106.50355 ?  159 MET   A O    1 
ATOM   321  C  CB   . MET   A 1 54  ? 1.98900  17.70900  35.76500 1.000 113.87835 ?  159 MET   A CB   1 
ATOM   322  C  CG   . MET   A 1 54  ? 2.13300  19.21000  35.56800 1.000 122.68231 ?  159 MET   A CG   1 
ATOM   323  S  SD   . MET   A 1 54  ? 2.94500  19.64400  34.01700 1.000 124.19130 ?  159 MET   A SD   1 
ATOM   324  C  CE   . MET   A 1 54  ? 1.58500  19.45500  32.86600 1.000 124.06507 ?  159 MET   A CE   1 
ATOM   325  N  N    . SER   A 1 66  ? 3.37700  6.23100   42.48000 1.000 93.27515  ?  218 SER   A N    1 
ATOM   326  C  CA   . SER   A 1 66  ? 2.69600  7.18600   41.61300 1.000 90.73711  ?  218 SER   A CA   1 
ATOM   327  C  C    . SER   A 1 66  ? 2.42600  6.57700   40.22800 1.000 83.12219  ?  218 SER   A C    1 
ATOM   328  O  O    . SER   A 1 66  ? 3.11500  5.64200   39.81100 1.000 82.98221  ?  218 SER   A O    1 
ATOM   329  C  CB   . SER   A 1 66  ? 3.51900  8.47500   41.49900 1.000 93.10703  ?  218 SER   A CB   1 
ATOM   330  O  OG   . SER   A 1 66  ? 4.86700  8.20000   41.16300 1.000 92.51599  ?  218 SER   A OG   1 
ATOM   331  N  N    . PRO   A 1 67  ? 1.41700  7.10200   39.52800 1.000 77.21829  ?  219 PRO   A N    1 
ATOM   332  C  CA   . PRO   A 1 67  ? 1.02900  6.52400   38.23600 1.000 69.97902  ?  219 PRO   A CA   1 
ATOM   333  C  C    . PRO   A 1 67  ? 2.17600  6.50600   37.23300 1.000 60.18330  ?  219 PRO   A C    1 
ATOM   334  O  O    . PRO   A 1 67  ? 3.13800  7.27400   37.31600 1.000 59.87247  ?  219 PRO   A O    1 
ATOM   335  C  CB   . PRO   A 1 67  ? -0.11000 7.44300   37.76300 1.000 72.20251  ?  219 PRO   A CB   1 
ATOM   336  C  CG   . PRO   A 1 67  ? 0.03100  8.69200   38.59500 1.000 75.77245  ?  219 PRO   A CG   1 
ATOM   337  C  CD   . PRO   A 1 67  ? 0.51200  8.19600   39.91700 1.000 78.78764  ?  219 PRO   A CD   1 
ATOM   338  N  N    . LEU   A 1 68  ? 2.06300  5.58400   36.28000 1.000 50.27255  ?  220 LEU   A N    1 
ATOM   339  C  CA   . LEU   A 1 68  ? 3.00200  5.47600   35.16400 1.000 41.29861  ?  220 LEU   A CA   1 
ATOM   340  C  C    . LEU   A 1 68  ? 2.55200  6.38100   34.01900 1.000 35.19447  ?  220 LEU   A C    1 
ATOM   341  O  O    . LEU   A 1 68  ? 2.20200  5.93800   32.92500 1.000 30.65874  ?  220 LEU   A O    1 
ATOM   342  C  CB   . LEU   A 1 68  ? 3.11900  4.02400   34.71800 1.000 40.26951  ?  220 LEU   A CB   1 
ATOM   343  C  CG   . LEU   A 1 68  ? 3.35900  3.00400   35.83200 1.000 42.41884  ?  220 LEU   A CG   1 
ATOM   344  C  CD1  . LEU   A 1 68  ? 3.31000  1.59600   35.28000 1.000 42.50128  ?  220 LEU   A CD1  1 
ATOM   345  C  CD2  . LEU   A 1 68  ? 4.69500  3.26600   36.51300 1.000 41.93424  ?  220 LEU   A CD2  1 
ATOM   346  N  N    . SER   A 1 69  ? 2.57700  7.68500   34.30200 1.000 34.51876  ?  221 SER   A N    1 
ATOM   347  C  CA   . SER   A 1 69  ? 1.97200  8.66300   33.40700 1.000 33.98908  ?  221 SER   A CA   1 
ATOM   348  C  C    . SER   A 1 69  ? 2.63900  8.71100   32.03800 1.000 31.53001  ?  221 SER   A C    1 
ATOM   349  O  O    . SER   A 1 69  ? 2.00400  9.14500   31.07000 1.000 30.99947  ?  221 SER   A O    1 
ATOM   350  C  CB   . SER   A 1 69  ? 2.02000  10.04700  34.04900 1.000 35.85767  ?  221 SER   A CB   1 
ATOM   351  O  OG   . SER   A 1 69  ? 3.34200  10.36700  34.45200 1.000 37.07289  ?  221 SER   A OG   1 
ATOM   352  N  N    . MET   A 1 70  ? 3.90200  8.29500   31.93300 1.000 29.74686  ?  222 MET   A N    1 
ATOM   353  C  CA   . MET   A 1 70  ? 4.61400  8.36400   30.66400 1.000 27.06223  ?  222 MET   A CA   1 
ATOM   354  C  C    . MET   A 1 70  ? 4.49600  7.09100   29.83900 1.000 24.48974  ?  222 MET   A C    1 
ATOM   355  O  O    . MET   A 1 70  ? 4.98200  7.06200   28.70400 1.000 24.70299  ?  222 MET   A O    1 
ATOM   356  C  CB   . MET   A 1 70  ? 6.10300  8.67500   30.90300 1.000 26.89235  ?  222 MET   A CB   1 
ATOM   357  C  CG   . MET   A 1 70  ? 6.40100  10.14000  31.21600 1.000 27.92362  ?  222 MET   A CG   1 
ATOM   358  S  SD   . MET   A 1 70  ? 5.87400  11.28000  29.92400 1.000 29.24507  ?  222 MET   A SD   1 
ATOM   359  C  CE   . MET   A 1 70  ? 7.19200  11.06300  28.72800 1.000 27.09599  ?  222 MET   A CE   1 
ATOM   360  N  N    . LEU   A 1 71  ? 3.87200  6.04200   30.37100 1.000 23.44379  ?  223 LEU   A N    1 
ATOM   361  C  CA   . LEU   A 1 71  ? 3.82600  4.77300   29.64900 1.000 20.87856  ?  223 LEU   A CA   1 
ATOM   362  C  C    . LEU   A 1 71  ? 3.08800  4.85000   28.31600 1.000 21.45009  ?  223 LEU   A C    1 
ATOM   363  O  O    . LEU   A 1 71  ? 3.57300  4.24500   27.34400 1.000 21.23305  ?  223 LEU   A O    1 
ATOM   364  C  CB   . LEU   A 1 71  ? 3.20700  3.68700   30.53700 1.000 19.61699  ?  223 LEU   A CB   1 
ATOM   365  C  CG   . LEU   A 1 71  ? 3.15100  2.29700   29.90100 1.000 19.19074  ?  223 LEU   A CG   1 
ATOM   366  C  CD1  . LEU   A 1 71  ? 4.54200  1.82200   29.53200 1.000 17.90225  ?  223 LEU   A CD1  1 
ATOM   367  C  CD2  . LEU   A 1 71  ? 2.44500  1.29300   30.81800 1.000 20.82894  ?  223 LEU   A CD2  1 
ATOM   368  N  N    . PRO   A 1 72  ? 1.94100  5.52400   28.18800 1.000 21.19652  ?  224 PRO   A N    1 
ATOM   369  C  CA   . PRO   A 1 72  ? 1.31800  5.60300   26.85300 1.000 19.85498  ?  224 PRO   A CA   1 
ATOM   370  C  C    . PRO   A 1 72  ? 2.22200  6.25200   25.82000 1.000 19.07014  ?  224 PRO   A C    1 
ATOM   371  O  O    . PRO   A 1 72  ? 2.39600  5.71100   24.72200 1.000 18.14022  ?  224 PRO   A O    1 
ATOM   372  C  CB   . PRO   A 1 72  ? 0.05000  6.42600   27.11700 1.000 20.55000  ?  224 PRO   A CB   1 
ATOM   373  C  CG   . PRO   A 1 72  ? -0.29400 6.12600   28.53900 1.000 21.32661  ?  224 PRO   A CG   1 
ATOM   374  C  CD   . PRO   A 1 72  ? 1.04000  6.03900   29.23900 1.000 22.59034  ?  224 PRO   A CD   1 
ATOM   375  N  N    . HIS   A 1 73  ? 2.81300  7.40300   26.14900 1.000 21.46638  ?  225 HIS   A N    1 
ATOM   376  C  CA   . HIS   A 1 73  ? 3.68900  8.07900   25.19900 1.000 21.82704  ?  225 HIS   A CA   1 
ATOM   377  C  C    . HIS   A 1 73  ? 4.91900  7.23700   24.88100 1.000 19.80121  ?  225 HIS   A C    1 
ATOM   378  O  O    . HIS   A 1 73  ? 5.31100  7.11000   23.71300 1.000 18.91572  ?  225 HIS   A O    1 
ATOM   379  C  CB   . HIS   A 1 73  ? 4.11100  9.44300   25.74600 1.000 21.66651  ?  225 HIS   A CB   1 
ATOM   380  C  CG   . HIS   A 1 73  ? 5.05400  10.18100  24.84900 1.000 21.59602  ?  225 HIS   A CG   1 
ATOM   381  N  ND1  . HIS   A 1 73  ? 4.64100  10.82400  23.70000 1.000 21.40832  ?  225 HIS   A ND1  1 
ATOM   382  C  CD2  . HIS   A 1 73  ? 6.39600  10.35900  24.92000 1.000 20.79828  ?  225 HIS   A CD2  1 
ATOM   383  C  CE1  . HIS   A 1 73  ? 5.68800  11.37800  23.11200 1.000 21.43699  ?  225 HIS   A CE1  1 
ATOM   384  N  NE2  . HIS   A 1 73  ? 6.76400  11.10900  23.83200 1.000 20.51774  ?  225 HIS   A NE2  1 
ATOM   385  N  N    . LEU   A 1 74  ? 5.55000  6.66600   25.90700 1.000 17.94820  ?  226 LEU   A N    1 
ATOM   386  C  CA   . LEU   A 1 74  ? 6.80300  5.95400   25.67600 1.000 18.63023  ?  226 LEU   A CA   1 
ATOM   387  C  C    . LEU   A 1 74  ? 6.56900  4.59900   25.01600 1.000 18.32979  ?  226 LEU   A C    1 
ATOM   388  O  O    . LEU   A 1 74  ? 7.43700  4.11300   24.28100 1.000 17.85603  ?  226 LEU   A O    1 
ATOM   389  C  CB   . LEU   A 1 74  ? 7.57400  5.80600   26.99300 1.000 19.59198  ?  226 LEU   A CB   1 
ATOM   390  C  CG   . LEU   A 1 74  ? 8.08300  7.15000   27.52800 1.000 21.84527  ?  226 LEU   A CG   1 
ATOM   391  C  CD1  . LEU   A 1 74  ? 8.81100  7.00800   28.88500 1.000 21.29252  ?  226 LEU   A CD1  1 
ATOM   392  C  CD2  . LEU   A 1 74  ? 8.98200  7.83800   26.49800 1.000 20.16698  ?  226 LEU   A CD2  1 
ATOM   393  N  N    . ALA   A 1 75  ? 5.39800  3.99500   25.22900 1.000 17.65435  ?  227 ALA   A N    1 
ATOM   394  C  CA   . ALA   A 1 75  ? 5.03600  2.80600   24.46300 1.000 15.64397  ?  227 ALA   A CA   1 
ATOM   395  C  C    . ALA   A 1 75  ? 4.96200  3.12300   22.97300 1.000 17.24249  ?  227 ALA   A C    1 
ATOM   396  O  O    . ALA   A 1 75  ? 5.50400  2.38800   22.14100 1.000 16.97865  ?  227 ALA   A O    1 
ATOM   397  C  CB   . ALA   A 1 75  ? 3.70200  2.23900   24.96100 1.000 15.66425  ?  227 ALA   A CB   1 
ATOM   398  N  N    . ASP   A 1 76  ? 4.28900  4.22400   22.61600 1.000 17.07189  ?  228 ASP   A N    1 
ATOM   399  C  CA   . ASP   A 1 76  ? 4.23800  4.64600   21.21800 1.000 17.61278  ?  228 ASP   A CA   1 
ATOM   400  C  C    . ASP   A 1 76  ? 5.63500  4.96800   20.67900 1.000 18.10943  ?  228 ASP   A C    1 
ATOM   401  O  O    . ASP   A 1 76  ? 5.97900  4.59300   19.55000 1.000 16.89758  ?  228 ASP   A O    1 
ATOM   402  C  CB   . ASP   A 1 76  ? 3.31200  5.85300   21.07800 1.000 18.18088  ?  228 ASP   A CB   1 
ATOM   403  C  CG   . ASP   A 1 76  ? 1.83100  5.48300   21.21500 1.000 20.43426  ?  228 ASP   A CG   1 
ATOM   404  O  OD1  . ASP   A 1 76  ? 1.01200  6.41300   21.36800 1.000 21.63052  ?  228 ASP   A OD1  1 
ATOM   405  O  OD2  . ASP   A 1 76  ? 1.48800  4.27700   21.18600 1.000 18.88338  ?  228 ASP   A OD2  1 
ATOM   406  N  N    . LEU   A 1 77  ? 6.45500  5.66500   21.47100 1.000 17.33158  ?  229 LEU   A N    1 
ATOM   407  C  CA   . LEU   A 1 77  ? 7.81400  5.98300   21.03000 1.000 16.93566  ?  229 LEU   A CA   1 
ATOM   408  C  C    . LEU   A 1 77  ? 8.60700  4.71000   20.75400 1.000 17.63860  ?  229 LEU   A C    1 
ATOM   409  O  O    . LEU   A 1 77  ? 9.22500  4.56900   19.69400 1.000 19.59687  ?  229 LEU   A O    1 
ATOM   410  C  CB   . LEU   A 1 77  ? 8.50900  6.86200   22.07600 1.000 16.37695  ?  229 LEU   A CB   1 
ATOM   411  C  CG   . LEU   A 1 77  ? 10.02500 7.09400   21.96500 1.000 19.11070  ?  229 LEU   A CG   1 
ATOM   412  C  CD1  . LEU   A 1 77  ? 10.37500 7.79700   20.66400 1.000 19.26081  ?  229 LEU   A CD1  1 
ATOM   413  C  CD2  . LEU   A 1 77  ? 10.51300 7.90800   23.15700 1.000 19.90815  ?  229 LEU   A CD2  1 
ATOM   414  N  N    . VAL   A 1 78  ? 8.57700  3.75700   21.69100 1.000 16.55239  ?  230 VAL   A N    1 
ATOM   415  C  CA   . VAL   A 1 78  ? 9.28100  2.49000   21.50200 1.000 15.33864  ?  230 VAL   A CA   1 
ATOM   416  C  C    . VAL   A 1 78  ? 8.75700  1.76900   20.26500 1.000 16.23698  ?  230 VAL   A C    1 
ATOM   417  O  O    . VAL   A 1 78  ? 9.52900  1.29000   19.42900 1.000 15.89508  ?  230 VAL   A O    1 
ATOM   418  C  CB   . VAL   A 1 78  ? 9.14700  1.61100   22.75900 1.000 15.66885  ?  230 VAL   A CB   1 
ATOM   419  C  CG1  . VAL   A 1 78  ? 9.57800  0.17400   22.44600 1.000 14.14639  ?  230 VAL   A CG1  1 
ATOM   420  C  CG2  . VAL   A 1 78  ? 9.97600  2.19200   23.90600 1.000 15.53631  ?  230 VAL   A CG2  1 
ATOM   421  N  N    . SER   A 1 79  ? 7.43000  1.66600   20.14500 1.000 16.49740  ?  231 SER   A N    1 
ATOM   422  C  CA   . SER   A 1 79  ? 6.82700  0.97800   19.00300 1.000 15.74334  ?  231 SER   A CA   1 
ATOM   423  C  C    . SER   A 1 79  ? 7.24800  1.61500   17.68200 1.000 15.55428  ?  231 SER   A C    1 
ATOM   424  O  O    . SER   A 1 79  ? 7.56900  0.91400   16.71600 1.000 15.50522  ?  231 SER   A O    1 
ATOM   425  C  CB   . SER   A 1 79  ? 5.30400  0.98800   19.15000 1.000 16.31242  ?  231 SER   A CB   1 
ATOM   426  O  OG   . SER   A 1 79  ? 4.70100  0.06700   18.26500 1.000 18.06266  ?  231 SER   A OG   1 
ATOM   427  N  N    . TYR   A 1 80  ? 7.23400  2.94500   17.62100 1.000 14.71656  ?  232 TYR   A N    1 
ATOM   428  C  CA   . TYR   A 1 80  ? 7.74400  3.66100   16.45600 1.000 15.09386  ?  232 TYR   A CA   1 
ATOM   429  C  C    . TYR   A 1 80  ? 9.18000  3.25500   16.14100 1.000 16.15220  ?  232 TYR   A C    1 
ATOM   430  O  O    . TYR   A 1 80  ? 9.53100  2.99000   14.98200 1.000 14.36715  ?  232 TYR   A O    1 
ATOM   431  C  CB   . TYR   A 1 80  ? 7.65300  5.15900   16.73200 1.000 16.74785  ?  232 TYR   A CB   1 
ATOM   432  C  CG   . TYR   A 1 80  ? 8.21600  6.06200   15.66700 1.000 20.50323  ?  232 TYR   A CG   1 
ATOM   433  C  CD1  . TYR   A 1 80  ? 7.44800  6.43400   14.58000 1.000 21.97066  ?  232 TYR   A CD1  1 
ATOM   434  C  CD2  . TYR   A 1 80  ? 9.50500  6.57800   15.76900 1.000 22.43513  ?  232 TYR   A CD2  1 
ATOM   435  C  CE1  . TYR   A 1 80  ? 7.94500  7.27200   13.60800 1.000 23.57772  ?  232 TYR   A CE1  1 
ATOM   436  C  CE2  . TYR   A 1 80  ? 10.01500 7.42400   14.79300 1.000 24.72833  ?  232 TYR   A CE2  1 
ATOM   437  C  CZ   . TYR   A 1 80  ? 9.22100  7.76900   13.71800 1.000 25.78826  ?  232 TYR   A CZ   1 
ATOM   438  O  OH   . TYR   A 1 80  ? 9.69700  8.60500   12.73800 1.000 28.30975  ?  232 TYR   A OH   1 
ATOM   439  N  N    . SER   A 1 81  ? 10.02000 3.18400   17.17600 1.000 14.15179  ?  233 SER   A N    1 
ATOM   440  C  CA   . SER   A 1 81  ? 11.42800 2.86200   16.98000 1.000 17.29587  ?  233 SER   A CA   1 
ATOM   441  C  C    . SER   A 1 81  ? 11.62600 1.42000   16.53200 1.000 16.03018  ?  233 SER   A C    1 
ATOM   442  O  O    . SER   A 1 81  ? 12.52900 1.14300   15.73200 1.000 13.93563  ?  233 SER   A O    1 
ATOM   443  C  CB   . SER   A 1 81  ? 12.20000 3.11700   18.27400 1.000 21.30239  ?  233 SER   A CB   1 
ATOM   444  O  OG   . SER   A 1 81  ? 13.57600 3.30600   17.99900 1.000 27.45348  ?  233 SER   A OG   1 
ATOM   445  N  N    . ILE   A 1 82  ? 10.80900 0.48700   17.04000 1.000 15.08597  ?  234 ILE   A N    1 
ATOM   446  C  CA   . ILE   A 1 82  ? 10.89900 -0.89400  16.56700 1.000 13.47740  ?  234 ILE   A CA   1 
ATOM   447  C  C    . ILE   A 1 82  ? 10.70100 -0.94100  15.05500 1.000 13.46763  ?  234 ILE   A C    1 
ATOM   448  O  O    . ILE   A 1 82  ? 11.42600 -1.64200  14.34200 1.000 14.31658  ?  234 ILE   A O    1 
ATOM   449  C  CB   . ILE   A 1 82  ? 9.88700  -1.79500  17.31000 1.000 14.71305  ?  234 ILE   A CB   1 
ATOM   450  C  CG1  . ILE   A 1 82  ? 10.29100 -2.00800  18.78400 1.000 13.89696  ?  234 ILE   A CG1  1 
ATOM   451  C  CG2  . ILE   A 1 82  ? 9.76900  -3.15600  16.63800 1.000 14.73579  ?  234 ILE   A CG2  1 
ATOM   452  C  CD1  . ILE   A 1 82  ? 9.15000  -2.67000  19.61000 1.000 14.48044  ?  234 ILE   A CD1  1 
ATOM   453  N  N    . GLN   A 1 83  ? 9.71400  -0.19700  14.54100 1.000 13.46875  ?  235 GLN   A N    1 
ATOM   454  C  CA   . GLN   A 1 83  ? 9.49400  -0.15500  13.09200 1.000 15.16558  ?  235 GLN   A CA   1 
ATOM   455  C  C    . GLN   A 1 83  ? 10.72800 0.35800   12.35500 1.000 16.08209  ?  235 GLN   A C    1 
ATOM   456  O  O    . GLN   A 1 83  ? 11.07600 -0.14800  11.28100 1.000 15.44263  ?  235 GLN   A O    1 
ATOM   457  C  CB   . GLN   A 1 83  ? 8.28600  0.72300   12.77200 1.000 18.53393  ?  235 GLN   A CB   1 
ATOM   458  C  CG   . GLN   A 1 83  ? 6.97300  0.18900   13.32100 1.000 20.02361  ?  235 GLN   A CG   1 
ATOM   459  C  CD   . GLN   A 1 83  ? 5.77200  0.94800   12.79400 1.000 23.96325  ?  235 GLN   A CD   1 
ATOM   460  O  OE1  . GLN   A 1 83  ? 5.59600  1.09600   11.58100 1.000 24.33441  ?  235 GLN   A OE1  1 
ATOM   461  N  NE2  . GLN   A 1 83  ? 4.94000  1.43600   13.70200 1.000 24.47729  ?  235 GLN   A NE2  1 
ATOM   462  N  N    . LYS   A 1 84  ? 11.40900 1.35700   12.92100 1.000 16.29111  ?  236 LYS   A N    1 
ATOM   463  C  CA   . LYS   A 1 84  ? 12.60500 1.88500   12.27300 1.000 15.19539  ?  236 LYS   A CA   1 
ATOM   464  C  C    . LYS   A 1 84  ? 13.72700 0.86100   12.28200 1.000 16.38214  ?  236 LYS   A C    1 
ATOM   465  O  O    . LYS   A 1 84  ? 14.46200 0.72600   11.29500 1.000 19.11226  ?  236 LYS   A O    1 
ATOM   466  C  CB   . LYS   A 1 84  ? 13.05700 3.17100   12.96400 1.000 15.96822  ?  236 LYS   A CB   1 
ATOM   467  C  CG   . LYS   A 1 84  ? 12.03000 4.28600   12.91300 1.000 18.42504  ?  236 LYS   A CG   1 
ATOM   468  C  CD   . LYS   A 1 84  ? 11.51700 4.46100   11.49000 1.000 21.41290  ?  236 LYS   A CD   1 
ATOM   469  C  CE   . LYS   A 1 84  ? 10.73500 5.75200   11.35900 1.000 24.29234  ?  236 LYS   A CE   1 
ATOM   470  N  NZ   . LYS   A 1 84  ? 11.62400 6.91100   11.67800 1.000 26.52345  ?  236 LYS   A NZ   1 
ATOM   471  N  N    . VAL   A 1 85  ? 13.88100 0.14000   13.39400 1.000 13.78359  ?  237 VAL   A N    1 
ATOM   472  C  CA   . VAL   A 1 85  ? 14.91600 -0.88500  13.49200 1.000 15.35929  ?  237 VAL   A CA   1 
ATOM   473  C  C    . VAL   A 1 85  ? 14.69700 -1.97100  12.44100 1.000 15.90612  ?  237 VAL   A C    1 
ATOM   474  O  O    . VAL   A 1 85  ? 15.64600 -2.44100  11.80500 1.000 17.41332  ?  237 VAL   A O    1 
ATOM   475  C  CB   . VAL   A 1 85  ? 14.95100 -1.46500  14.91700 1.000 14.12097  ?  237 VAL   A CB   1 
ATOM   476  C  CG1  . VAL   A 1 85  ? 15.86900 -2.68400  14.96500 1.000 13.53459  ?  237 VAL   A CG1  1 
ATOM   477  C  CG2  . VAL   A 1 85  ? 15.41100 -0.39100  15.92000 1.000 13.25077  ?  237 VAL   A CG2  1 
ATOM   478  N  N    . ILE   A 1 86  ? 13.44600 -2.38900  12.25000 1.000 14.18762  ?  238 ILE   A N    1 
ATOM   479  C  CA   . ILE   A 1 86  ? 13.13800 -3.39900  11.24200 1.000 16.17032  ?  238 ILE   A CA   1 
ATOM   480  C  C    . ILE   A 1 86  ? 13.47000 -2.87700  9.84800  1.000 16.94146  ?  238 ILE   A C    1 
ATOM   481  O  O    . ILE   A 1 86  ? 14.04400 -3.59500  9.02200  1.000 20.71727  ?  238 ILE   A O    1 
ATOM   482  C  CB   . ILE   A 1 86  ? 11.65500 -3.81800  11.34700 1.000 18.96262  ?  238 ILE   A CB   1 
ATOM   483  C  CG1  . ILE   A 1 86  ? 11.36700 -4.49500  12.69200 1.000 19.59526  ?  238 ILE   A CG1  1 
ATOM   484  C  CG2  . ILE   A 1 86  ? 11.26000 -4.72100  10.17900 1.000 17.87325  ?  238 ILE   A CG2  1 
ATOM   485  C  CD1  . ILE   A 1 86  ? 9.87600  -4.41700  13.09500 1.000 20.14873  ?  238 ILE   A CD1  1 
ATOM   486  N  N    . GLY   A 1 87  ? 13.10800 -1.62400  9.56200  1.000 17.00971  ?  239 GLY   A N    1 
ATOM   487  C  CA   . GLY   A 1 87  ? 13.45000 -1.04400  8.27200  1.000 19.05827  ?  239 GLY   A CA   1 
ATOM   488  C  C    . GLY   A 1 87  ? 14.94700 -0.99300  8.04300  1.000 19.27626  ?  239 GLY   A C    1 
ATOM   489  O  O    . GLY   A 1 87  ? 15.42700 -1.24000  6.93300  1.000 20.01453  ?  239 GLY   A O    1 
ATOM   490  N  N    . PHE   A 1 88  ? 15.70900 -0.69300  9.09700  1.000 15.24182  ?  240 PHE   A N    1 
ATOM   491  C  CA   . PHE   A 1 88  ? 17.16100 -0.68700  8.97500  1.000 15.97341  ?  240 PHE   A CA   1 
ATOM   492  C  C    . PHE   A 1 88  ? 17.68700 -2.09000  8.70900  1.000 17.61428  ?  240 PHE   A C    1 
ATOM   493  O  O    . PHE   A 1 88  ? 18.46700 -2.30300  7.77100  1.000 19.49407  ?  240 PHE   A O    1 
ATOM   494  C  CB   . PHE   A 1 88  ? 17.79100 -0.10700  10.24800 1.000 16.22450  ?  240 PHE   A CB   1 
ATOM   495  C  CG   . PHE   A 1 88  ? 19.29800 -0.13000  10.24600 1.000 18.52902  ?  240 PHE   A CG   1 
ATOM   496  C  CD1  . PHE   A 1 88  ? 20.01400 0.85300   9.58000  1.000 18.30761  ?  240 PHE   A CD1  1 
ATOM   497  C  CD2  . PHE   A 1 88  ? 19.99500 -1.12300  10.92600 1.000 18.92153  ?  240 PHE   A CD2  1 
ATOM   498  C  CE1  . PHE   A 1 88  ? 21.40400 0.84000   9.57900  1.000 18.86176  ?  240 PHE   A CE1  1 
ATOM   499  C  CE2  . PHE   A 1 88  ? 21.37700 -1.13600  10.93800 1.000 19.91965  ?  240 PHE   A CE2  1 
ATOM   500  C  CZ   . PHE   A 1 88  ? 22.08300 -0.15600  10.26400 1.000 20.01448  ?  240 PHE   A CZ   1 
ATOM   501  N  N    . ALA   A 1 89  ? 17.26000 -3.06100  9.52600  1.000 18.25741  ?  241 ALA   A N    1 
ATOM   502  C  CA   . ALA   A 1 89  ? 17.76300 -4.42800  9.41400  1.000 20.03981  ?  241 ALA   A CA   1 
ATOM   503  C  C    . ALA   A 1 89  ? 17.56700 -4.99100  8.01500  1.000 21.55728  ?  241 ALA   A C    1 
ATOM   504  O  O    . ALA   A 1 89  ? 18.43300 -5.70800  7.50300  1.000 22.22822  ?  241 ALA   A O    1 
ATOM   505  C  CB   . ALA   A 1 89  ? 17.07200 -5.32900  10.43800 1.000 19.86443  ?  241 ALA   A CB   1 
ATOM   506  N  N    . LYS   A 1 90  ? 16.43200 -4.67000  7.38200  1.000 21.48602  ?  242 LYS   A N    1 
ATOM   507  C  CA   . LYS   A 1 90  ? 16.12500 -5.19200  6.05500  1.000 22.39219  ?  242 LYS   A CA   1 
ATOM   508  C  C    . LYS   A 1 90  ? 17.15600 -4.77400  5.02100  1.000 23.24070  ?  242 LYS   A C    1 
ATOM   509  O  O    . LYS   A 1 90  ? 17.35600 -5.48200  4.02800  1.000 26.26914  ?  242 LYS   A O    1 
ATOM   510  C  CB   . LYS   A 1 90  ? 14.74100 -4.71400  5.61500  1.000 24.22593  ?  242 LYS   A CB   1 
ATOM   511  C  CG   . LYS   A 1 90  ? 13.60900 -5.56000  6.12400  1.000 27.26339  ?  242 LYS   A CG   1 
ATOM   512  C  CD   . LYS   A 1 90  ? 12.28500 -4.81800  5.97600  1.000 29.28009  ?  242 LYS   A CD   1 
ATOM   513  C  CE   . LYS   A 1 90  ? 11.74300 -4.91500  4.55700  1.000 30.21696  ?  242 LYS   A CE   1 
ATOM   514  N  NZ   . LYS   A 1 90  ? 10.37500 -4.28800  4.44300  1.000 31.60611  ?  242 LYS   A NZ   1 
ATOM   515  N  N    A MET   A 1 91  ? 17.80800 -3.63400  5.22000  0.720 23.57752  ?  243 MET   A N    1 
ATOM   516  N  N    B MET   A 1 91  ? 17.81300 -3.63300  5.22800  0.280 23.64137  ?  243 MET   A N    1 
ATOM   517  C  CA   A MET   A 1 91  ? 18.80600 -3.14600  4.27700  0.720 24.97707  ?  243 MET   A CA   1 
ATOM   518  C  CA   B MET   A 1 91  ? 18.81200 -3.12800  4.29500  0.280 25.01171  ?  243 MET   A CA   1 
ATOM   519  C  C    A MET   A 1 91  ? 20.23000 -3.58000  4.60700  0.720 25.36350  ?  243 MET   A C    1 
ATOM   520  C  C    B MET   A 1 91  ? 20.22000 -3.64000  4.57000  0.280 25.37184  ?  243 MET   A C    1 
ATOM   521  O  O    A MET   A 1 91  ? 21.15100 -3.19900  3.87800  0.720 26.29434  ?  243 MET   A O    1 
ATOM   522  O  O    B MET   A 1 91  ? 21.12000 -3.37100  3.76700  0.280 26.38002  ?  243 MET   A O    1 
ATOM   523  C  CB   A MET   A 1 91  ? 18.74600 -1.62100  4.19800  0.720 25.74196  ?  243 MET   A CB   1 
ATOM   524  C  CB   B MET   A 1 91  ? 18.83300 -1.59700  4.31500  0.280 25.74148  ?  243 MET   A CB   1 
ATOM   525  C  CG   A MET   A 1 91  ? 17.36500 -1.08900  3.86600  0.720 26.89397  ?  243 MET   A CG   1 
ATOM   526  C  CG   B MET   A 1 91  ? 17.50000 -0.93400  4.00800  0.280 26.68864  ?  243 MET   A CG   1 
ATOM   527  S  SD   A MET   A 1 91  ? 17.38000 0.67900   3.54700  0.720 28.25562  ?  243 MET   A SD   1 
ATOM   528  S  SD   B MET   A 1 91  ? 16.53400 -1.83700  2.78900  0.280 27.78327  ?  243 MET   A SD   1 
ATOM   529  C  CE   A MET   A 1 91  ? 16.43500 1.27300   4.93300  0.720 26.46665  ?  243 MET   A CE   1 
ATOM   530  C  CE   B MET   A 1 91  ? 17.34300 -1.35400  1.26600  0.280 29.33016  ?  243 MET   A CE   1 
ATOM   531  N  N    . ILE   A 1 92  ? 20.44200 -4.35200  5.67200  1.000 24.48174  ?  244 ILE   A N    1 
ATOM   532  C  CA   . ILE   A 1 92  ? 21.78000 -4.86300  5.99300  1.000 23.21699  ?  244 ILE   A CA   1 
ATOM   533  C  C    . ILE   A 1 92  ? 22.20500 -5.88100  4.93900  1.000 26.42746  ?  244 ILE   A C    1 
ATOM   534  O  O    . ILE   A 1 92  ? 21.49300 -6.87500  4.72100  1.000 25.83737  ?  244 ILE   A O    1 
ATOM   535  C  CB   . ILE   A 1 92  ? 21.84200 -5.50000  7.39200  1.000 21.37640  ?  244 ILE   A CB   1 
ATOM   536  C  CG1  . ILE   A 1 92  ? 21.48900 -4.49200  8.49000  1.000 18.73132  ?  244 ILE   A CG1  1 
ATOM   537  C  CG2  . ILE   A 1 92  ? 23.25700 -6.08900  7.65100  1.000 20.34693  ?  244 ILE   A CG2  1 
ATOM   538  C  CD1  . ILE   A 1 92  ? 21.42700 -5.12600  9.87800  1.000 18.22728  ?  244 ILE   A CD1  1 
ATOM   539  N  N    . PRO   A 1 93  ? 23.35000 -5.68900  4.27600  1.000 28.72321  ?  245 PRO   A N    1 
ATOM   540  C  CA   . PRO   A 1 93  ? 23.78000 -6.65000  3.24900  1.000 30.34868  ?  245 PRO   A CA   1 
ATOM   541  C  C    . PRO   A 1 93  ? 23.84300 -8.06500  3.81000  1.000 32.24942  ?  245 PRO   A C    1 
ATOM   542  O  O    . PRO   A 1 93  ? 24.46500 -8.31700  4.84800  1.000 31.94283  ?  245 PRO   A O    1 
ATOM   543  C  CB   . PRO   A 1 93  ? 25.17100 -6.13900  2.84300  1.000 32.15699  ?  245 PRO   A CB   1 
ATOM   544  C  CG   . PRO   A 1 93  ? 25.11500 -4.66200  3.10500  1.000 31.11912  ?  245 PRO   A CG   1 
ATOM   545  C  CD   . PRO   A 1 93  ? 24.25400 -4.52700  4.36100  1.000 28.96416  ?  245 PRO   A CD   1 
ATOM   546  N  N    . GLY   A 1 94  ? 23.15900 -8.98300  3.12800  1.000 32.69012  ?  246 GLY   A N    1 
ATOM   547  C  CA   . GLY   A 1 94  ? 23.09200 -10.36800 3.53000  1.000 32.88622  ?  246 GLY   A CA   1 
ATOM   548  C  C    . GLY   A 1 94  ? 21.93400 -10.72500 4.44200  1.000 32.64733  ?  246 GLY   A C    1 
ATOM   549  O  O    . GLY   A 1 94  ? 21.60600 -11.91100 4.55800  1.000 34.59088  ?  246 GLY   A O    1 
ATOM   550  N  N    . PHE   A 1 95  ? 21.30900 -9.73800  5.09700  1.000 30.99291  ?  247 PHE   A N    1 
ATOM   551  C  CA   . PHE   A 1 95  ? 20.27300 -10.03600 6.08700  1.000 31.34006  ?  247 PHE   A CA   1 
ATOM   552  C  C    . PHE   A 1 95  ? 19.11700 -10.82000 5.47300  1.000 35.36810  ?  247 PHE   A C    1 
ATOM   553  O  O    . PHE   A 1 95  ? 18.62900 -11.79200 6.06400  1.000 35.25660  ?  247 PHE   A O    1 
ATOM   554  C  CB   . PHE   A 1 95  ? 19.75600 -8.74000  6.71800  1.000 28.62009  ?  247 PHE   A CB   1 
ATOM   555  C  CG   . PHE   A 1 95  ? 18.73500 -8.95600  7.80500  1.000 27.23768  ?  247 PHE   A CG   1 
ATOM   556  C  CD1  . PHE   A 1 95  ? 19.13100 -9.29500  9.08900  1.000 27.71701  ?  247 PHE   A CD1  1 
ATOM   557  C  CD2  . PHE   A 1 95  ? 17.37800 -8.83000  7.54000  1.000 26.15690  ?  247 PHE   A CD2  1 
ATOM   558  C  CE1  . PHE   A 1 95  ? 18.19600 -9.49900  10.09000 1.000 26.87522  ?  247 PHE   A CE1  1 
ATOM   559  C  CE2  . PHE   A 1 95  ? 16.43200 -9.02600  8.53600  1.000 25.51313  ?  247 PHE   A CE2  1 
ATOM   560  C  CZ   . PHE   A 1 95  ? 16.83300 -9.36100  9.81100  1.000 25.73448  ?  247 PHE   A CZ   1 
ATOM   561  N  N    . ARG   A 1 96  ? 18.66100 -10.41600 4.29300  1.000 37.44622  ?  248 ARG   A N    1 
ATOM   562  C  CA   . ARG   A 1 96  ? 17.51000 -11.08900 3.70100  1.000 41.18939  ?  248 ARG   A CA   1 
ATOM   563  C  C    . ARG   A 1 96  ? 17.87900 -12.37800 2.97800  1.000 43.13151  ?  248 ARG   A C    1 
ATOM   564  O  O    . ARG   A 1 96  ? 16.99900 -13.01000 2.38800  1.000 44.33092  ?  248 ARG   A O    1 
ATOM   565  C  CB   . ARG   A 1 96  ? 16.76600 -10.13300 2.76800  1.000 44.63544  ?  248 ARG   A CB   1 
ATOM   566  C  CG   . ARG   A 1 96  ? 16.52800 -8.76500  3.39700  1.000 46.94271  ?  248 ARG   A CG   1 
ATOM   567  C  CD   . ARG   A 1 96  ? 15.12900 -8.22200  3.13800  1.000 50.22994  ?  248 ARG   A CD   1 
ATOM   568  N  NE   . ARG   A 1 96  ? 14.07900 -9.23500  3.26800  1.000 54.11899  ?  248 ARG   A NE   1 
ATOM   569  C  CZ   . ARG   A 1 96  ? 13.43500 -9.50700  4.40100  1.000 54.75297  ?  248 ARG   A CZ   1 
ATOM   570  N  NH1  . ARG   A 1 96  ? 13.74300 -8.85300  5.51300  1.000 54.15559  ?  248 ARG   A NH1  1 
ATOM   571  N  NH2  . ARG   A 1 96  ? 12.48900 -10.43900 4.43000  1.000 55.64000  ?  248 ARG   A NH2  1 
ATOM   572  N  N    . ASP   A 1 97  ? 19.14700 -12.79100 3.02400  1.000 44.06668  ?  249 ASP   A N    1 
ATOM   573  C  CA   . ASP   A 1 97  ? 19.50400 -14.14800 2.63800  1.000 45.79783  ?  249 ASP   A CA   1 
ATOM   574  C  C    . ASP   A 1 97  ? 19.17500 -15.15800 3.72700  1.000 43.90396  ?  249 ASP   A C    1 
ATOM   575  O  O    . ASP   A 1 97  ? 19.19600 -16.36500 3.45800  1.000 44.75207  ?  249 ASP   A O    1 
ATOM   576  C  CB   . ASP   A 1 97  ? 20.99400 -14.23600 2.29800  1.000 48.43704  ?  249 ASP   A CB   1 
ATOM   577  C  CG   . ASP   A 1 97  ? 21.38200 -13.34600 1.13100  1.000 50.10449  ?  249 ASP   A CG   1 
ATOM   578  O  OD1  . ASP   A 1 97  ? 22.58100 -13.02000 1.00300  1.000 51.31558  ?  249 ASP   A OD1  1 
ATOM   579  O  OD2  . ASP   A 1 97  ? 20.48800 -12.96500 0.34800  1.000 50.37488  ?  249 ASP   A OD2  1 
ATOM   580  N  N    . LEU   A 1 98  ? 18.88500 -14.69200 4.94100  1.000 39.57977  ?  250 LEU   A N    1 
ATOM   581  C  CA   . LEU   A 1 98  ? 18.48000 -15.56400 6.03100  1.000 36.12502  ?  250 LEU   A CA   1 
ATOM   582  C  C    . LEU   A 1 98  ? 17.03900 -16.00900 5.83900  1.000 35.11947  ?  250 LEU   A C    1 
ATOM   583  O  O    . LEU   A 1 98  ? 16.27900 -15.41800 5.07100  1.000 34.72625  ?  250 LEU   A O    1 
ATOM   584  C  CB   . LEU   A 1 98  ? 18.60400 -14.84800 7.37400  1.000 32.84649  ?  250 LEU   A CB   1 
ATOM   585  C  CG   . LEU   A 1 98  ? 20.03000 -14.46300 7.75600  1.000 31.62826  ?  250 LEU   A CG   1 
ATOM   586  C  CD1  . LEU   A 1 98  ? 20.01500 -13.49300 8.91400  1.000 29.96587  ?  250 LEU   A CD1  1 
ATOM   587  C  CD2  . LEU   A 1 98  ? 20.81400 -15.71700 8.10000  1.000 32.67798  ?  250 LEU   A CD2  1 
ATOM   588  N  N    . THR   A 1 99  ? 16.66300 -17.05400 6.57000  1.000 35.54410  ?  251 THR   A N    1 
ATOM   589  C  CA   . THR   A 1 99  ? 15.27700 -17.48100 6.58300  1.000 35.25130  ?  251 THR   A CA   1 
ATOM   590  C  C    . THR   A 1 99  ? 14.43600 -16.51400 7.40400  1.000 33.70910  ?  251 THR   A C    1 
ATOM   591  O  O    . THR   A 1 99  ? 14.93400 -15.80700 8.29300  1.000 31.54828  ?  251 THR   A O    1 
ATOM   592  C  CB   . THR   A 1 99  ? 15.13600 -18.88800 7.16200  1.000 37.12677  ?  251 THR   A CB   1 
ATOM   593  O  OG1  . THR   A 1 99  ? 15.40100 -18.85300 8.57100  1.000 35.42072  ?  251 THR   A OG1  1 
ATOM   594  C  CG2  . THR   A 1 99  ? 16.08500 -19.86000 6.46600  1.000 40.83937  ?  251 THR   A CG2  1 
ATOM   595  N  N    . SER   A 1 100 ? 13.13600 -16.50600 7.09700  1.000 32.90663  ?  252 SER   A N    1 
ATOM   596  C  CA   . SER   A 1 100 ? 12.18400 -15.68000 7.82800  1.000 34.05609  ?  252 SER   A CA   1 
ATOM   597  C  C    . SER   A 1 100 ? 12.29800 -15.90600 9.32500  1.000 32.76720  ?  252 SER   A C    1 
ATOM   598  O  O    . SER   A 1 100 ? 12.31400 -14.95400 10.10700 1.000 32.30222  ?  252 SER   A O    1 
ATOM   599  C  CB   . SER   A 1 100 ? 10.76100 -15.98500 7.36000  1.000 37.34245  ?  252 SER   A CB   1 
ATOM   600  O  OG   . SER   A 1 100 ? 10.54900 -15.44100 6.07400  1.000 41.62014  ?  252 SER   A OG   1 
ATOM   601  N  N    . ASP   A 1 101 ? 12.36400 -17.17200 9.73900  1.000 34.22608  ?  253 ASP   A N    1 
ATOM   602  C  CA   . ASP   A 1 101 ? 12.47200 -17.48400 11.16200 1.000 35.80694  ?  253 ASP   A CA   1 
ATOM   603  C  C    . ASP   A 1 101 ? 13.73100 -16.87500 11.76200 1.000 32.75408  ?  253 ASP   A C    1 
ATOM   604  O  O    . ASP   A 1 101 ? 13.69100 -16.33100 12.87000 1.000 31.76862  ?  253 ASP   A O    1 
ATOM   605  C  CB   . ASP   A 1 101 ? 12.44800 -18.99900 11.37200 1.000 39.43426  ?  253 ASP   A CB   1 
ATOM   606  C  CG   . ASP   A 1 101 ? 11.21600 -19.64300 10.76900 1.000 43.86804  ?  253 ASP   A CG   1 
ATOM   607  O  OD1  . ASP   A 1 101 ? 11.28400 -20.05800 9.59200  1.000 45.91917  ?  253 ASP   A OD1  1 
ATOM   608  O  OD2  . ASP   A 1 101 ? 10.17400 -19.70500 11.46000 1.000 45.21259  ?  253 ASP   A OD2  1 
ATOM   609  N  N    . ASP   A 1 102 ? 14.85200 -16.94800 11.04000 1.000 32.91609  ?  254 ASP   A N    1 
ATOM   610  C  CA   . ASP   A 1 102 ? 16.10500 -16.39000 11.54300 1.000 30.49190  ?  254 ASP   A CA   1 
ATOM   611  C  C    . ASP   A 1 102 ? 16.05600 -14.86800 11.59000 1.000 28.95294  ?  254 ASP   A C    1 
ATOM   612  O  O    . ASP   A 1 102 ? 16.55700 -14.25800 12.54100 1.000 29.67221  ?  254 ASP   A O    1 
ATOM   613  C  CB   . ASP   A 1 102 ? 17.27200 -16.86100 10.68100 1.000 31.80836  ?  254 ASP   A CB   1 
ATOM   614  C  CG   . ASP   A 1 102 ? 17.88900 -18.15600 11.19000 1.000 34.69607  ?  254 ASP   A CG   1 
ATOM   615  O  OD1  . ASP   A 1 102 ? 18.73900 -18.72800 10.47200 1.000 36.87632  ?  254 ASP   A OD1  1 
ATOM   616  O  OD2  . ASP   A 1 102 ? 17.52900 -18.60300 12.30400 1.000 34.11725  ?  254 ASP   A OD2  1 
ATOM   617  N  N    . GLN   A 1 103 ? 15.47300 -14.23900 10.56800 1.000 28.08621  ?  255 GLN   A N    1 
ATOM   618  C  CA   . GLN   A 1 103 ? 15.27600 -12.79200 10.60300 1.000 27.24085  ?  255 GLN   A CA   1 
ATOM   619  C  C    . GLN   A 1 103 ? 14.45300 -12.38200 11.81700 1.000 24.24708  ?  255 GLN   A C    1 
ATOM   620  O  O    . GLN   A 1 103 ? 14.76900 -11.39000 12.49000 1.000 20.41347  ?  255 GLN   A O    1 
ATOM   621  C  CB   . GLN   A 1 103 ? 14.60200 -12.32900 9.31000  1.000 27.04243  ?  255 GLN   A CB   1 
ATOM   622  C  CG   . GLN   A 1 103 ? 15.46300 -12.56600 8.08100  1.000 29.16656  ?  255 GLN   A CG   1 
ATOM   623  C  CD   . GLN   A 1 103 ? 14.77300 -12.15600 6.79800  1.000 30.94364  ?  255 GLN   A CD   1 
ATOM   624  O  OE1  . GLN   A 1 103 ? 13.99400 -11.21200 6.78200  1.000 29.14342  ?  255 GLN   A OE1  1 
ATOM   625  N  NE2  . GLN   A 1 103 ? 15.06200 -12.86600 5.71100  1.000 32.57473  ?  255 GLN   A NE2  1 
ATOM   626  N  N    . ILE   A 1 104 ? 13.41300 -13.15700 12.13100 1.000 22.78962  ?  256 ILE   A N    1 
ATOM   627  C  CA   . ILE   A 1 104 ? 12.54100 -12.82900 13.25500 1.000 21.68808  ?  256 ILE   A CA   1 
ATOM   628  C  C    . ILE   A 1 104 ? 13.27500 -12.99500 14.58600 1.000 21.32670  ?  256 ILE   A C    1 
ATOM   629  O  O    . ILE   A 1 104 ? 13.18600 -12.13700 15.47000 1.000 21.78825  ?  256 ILE   A O    1 
ATOM   630  C  CB   . ILE   A 1 104 ? 11.26000 -13.68300 13.19900 1.000 22.71414  ?  256 ILE   A CB   1 
ATOM   631  C  CG1  . ILE   A 1 104 ? 10.32000 -13.16300 12.10400 1.000 21.76596  ?  256 ILE   A CG1  1 
ATOM   632  C  CG2  . ILE   A 1 104 ? 10.55200 -13.69300 14.55200 1.000 24.06950  ?  256 ILE   A CG2  1 
ATOM   633  C  CD1  . ILE   A 1 104 ? 9.17200  -14.11400 11.80000 1.000 24.62252  ?  256 ILE   A CD1  1 
ATOM   634  N  N    A VAL   A 1 105 ? 13.98500 -14.11300 14.75200 0.560 22.16111  ?  257 VAL   A N    1 
ATOM   635  N  N    B VAL   A 1 105 ? 14.00900 -14.09700 14.75900 0.440 22.14874  ?  257 VAL   A N    1 
ATOM   636  C  CA   A VAL   A 1 105 ? 14.73200 -14.35800 15.98400 0.560 22.24518  ?  257 VAL   A CA   1 
ATOM   637  C  CA   B VAL   A 1 105 ? 14.67500 -14.29300 16.04600 0.440 22.17275  ?  257 VAL   A CA   1 
ATOM   638  C  C    A VAL   A 1 105 ? 15.73800 -13.24000 16.23100 0.560 21.24884  ?  257 VAL   A C    1 
ATOM   639  C  C    B VAL   A 1 105 ? 15.78000 -13.26100 16.25400 0.440 21.26683  ?  257 VAL   A C    1 
ATOM   640  O  O    A VAL   A 1 105 ? 15.89200 -12.75800 17.36100 0.560 20.99989  ?  257 VAL   A O    1 
ATOM   641  O  O    B VAL   A 1 105 ? 16.05400 -12.86000 17.39200 0.440 21.26156  ?  257 VAL   A O    1 
ATOM   642  C  CB   A VAL   A 1 105 ? 15.42000 -15.73500 15.91500 0.560 23.71217  ?  257 VAL   A CB   1 
ATOM   643  C  CB   B VAL   A 1 105 ? 15.20900 -15.73200 16.18500 0.440 23.62548  ?  257 VAL   A CB   1 
ATOM   644  C  CG1  A VAL   A 1 105 ? 16.59300 -15.80400 16.88100 0.560 23.81404  ?  257 VAL   A CG1  1 
ATOM   645  C  CG1  B VAL   A 1 105 ? 14.06600 -16.73800 16.09300 0.440 24.42184  ?  257 VAL   A CG1  1 
ATOM   646  C  CG2  A VAL   A 1 105 ? 14.41700 -16.84500 16.20100 0.560 24.73306  ?  257 VAL   A CG2  1 
ATOM   647  C  CG2  B VAL   A 1 105 ? 16.27200 -16.02400 15.14500 0.440 23.91271  ?  257 VAL   A CG2  1 
ATOM   648  N  N    . LEU   A 1 106 ? 16.41800 -12.79500 15.17600 1.000 20.11715  ?  258 LEU   A N    1 
ATOM   649  C  CA   . LEU   A 1 106 ? 17.46100 -11.78300 15.33600 1.000 20.98420  ?  258 LEU   A CA   1 
ATOM   650  C  C    . LEU   A 1 106 ? 16.86900 -10.43400 15.72000 1.000 20.93443  ?  258 LEU   A C    1 
ATOM   651  O  O    . LEU   A 1 106 ? 17.42100 -9.72500  16.57000 1.000 20.04163  ?  258 LEU   A O    1 
ATOM   652  C  CB   . LEU   A 1 106 ? 18.27700 -11.67100 14.05200 1.000 20.62820  ?  258 LEU   A CB   1 
ATOM   653  C  CG   . LEU   A 1 106 ? 19.15500 -12.88600 13.72700 1.000 22.27253  ?  258 LEU   A CG   1 
ATOM   654  C  CD1  . LEU   A 1 106 ? 19.86400 -12.70300 12.39600 1.000 21.72219  ?  258 LEU   A CD1  1 
ATOM   655  C  CD2  . LEU   A 1 106 ? 20.15700 -13.15700 14.83700 1.000 23.21556  ?  258 LEU   A CD2  1 
ATOM   656  N  N    . LEU   A 1 107 ? 15.74000 -10.06400 15.11400 1.000 21.99840  ?  259 LEU   A N    1 
ATOM   657  C  CA   . LEU   A 1 107 ? 15.13600 -8.77900  15.44000 1.000 22.84656  ?  259 LEU   A CA   1 
ATOM   658  C  C    . LEU   A 1 107 ? 14.47400 -8.80700  16.81000 1.000 21.55299  ?  259 LEU   A C    1 
ATOM   659  O  O    . LEU   A 1 107 ? 14.49500 -7.80500  17.53200 1.000 20.66743  ?  259 LEU   A O    1 
ATOM   660  C  CB   . LEU   A 1 107 ? 14.13300 -8.37900  14.35700 1.000 25.03886  ?  259 LEU   A CB   1 
ATOM   661  C  CG   . LEU   A 1 107 ? 14.81300 -7.69400  13.17200 1.000 28.07135  ?  259 LEU   A CG   1 
ATOM   662  C  CD1  . LEU   A 1 107 ? 13.91200 -7.72700  11.95500 1.000 29.70011  ?  259 LEU   A CD1  1 
ATOM   663  C  CD2  . LEU   A 1 107 ? 15.16000 -6.26500  13.54800 1.000 27.80999  ?  259 LEU   A CD2  1 
ATOM   664  N  N    . LYS   A 1 108 ? 13.87600 -9.94000  17.18700 1.000 22.15449  ?  260 LYS   A N    1 
ATOM   665  C  CA   . LYS   A 1 108 ? 13.24400 -10.03100 18.50300 1.000 23.45797  ?  260 LYS   A CA   1 
ATOM   666  C  C    . LYS   A 1 108 ? 14.26600 -9.86900  19.62200 1.000 23.30254  ?  260 LYS   A C    1 
ATOM   667  O  O    . LYS   A 1 108 ? 13.98300 -9.24700  20.65200 1.000 23.45196  ?  260 LYS   A O    1 
ATOM   668  C  CB   . LYS   A 1 108 ? 12.51700 -11.36800 18.64600 1.000 25.77439  ?  260 LYS   A CB   1 
ATOM   669  C  CG   . LYS   A 1 108 ? 11.04800 -11.33100 18.27000 1.000 30.33526  ?  260 LYS   A CG   1 
ATOM   670  C  CD   . LYS   A 1 108 ? 10.45100 -12.72600 18.35800 1.000 35.13282  ?  260 LYS   A CD   1 
ATOM   671  C  CE   . LYS   A 1 108 ? 10.05900 -13.06900 19.79200 1.000 38.19482  ?  260 LYS   A CE   1 
ATOM   672  N  NZ   . LYS   A 1 108 ? 9.14300  -12.04000 20.35200 1.000 38.45918  ?  260 LYS   A NZ   1 
ATOM   673  N  N    . SER   A 1 109 ? 15.45200 -10.43500 19.44900 1.000 22.83767  ?  261 SER   A N    1 
ATOM   674  C  CA   . SER   A 1 109 ? 16.44100 -10.36400 20.51700 1.000 24.45809  ?  261 SER   A CA   1 
ATOM   675  C  C    . SER   A 1 109 ? 17.24100 -9.07200  20.48800 1.000 21.58037  ?  261 SER   A C    1 
ATOM   676  O  O    . SER   A 1 109 ? 17.70600 -8.61900  21.53800 1.000 23.60289  ?  261 SER   A O    1 
ATOM   677  C  CB   . SER   A 1 109 ? 17.37700 -11.57100 20.43700 1.000 28.93601  ?  261 SER   A CB   1 
ATOM   678  O  OG   . SER   A 1 109 ? 17.94100 -11.67400 19.14200 1.000 32.71939  ?  261 SER   A OG   1 
ATOM   679  N  N    . SER   A 1 110 ? 17.38000 -8.43600  19.32600 1.000 19.90127  ?  262 SER   A N    1 
ATOM   680  C  CA   . SER   A 1 110 ? 18.24900 -7.26900  19.21700 1.000 18.90068  ?  262 SER   A CA   1 
ATOM   681  C  C    . SER   A 1 110 ? 17.51100 -5.94100  19.24800 1.000 17.34747  ?  262 SER   A C    1 
ATOM   682  O  O    . SER   A 1 110 ? 18.14800 -4.91900  19.52300 1.000 19.42123  ?  262 SER   A O    1 
ATOM   683  C  CB   . SER   A 1 110 ? 19.07800 -7.32800  17.92800 1.000 20.12425  ?  262 SER   A CB   1 
ATOM   684  O  OG   . SER   A 1 110 ? 18.24700 -7.14700  16.78100 1.000 19.90730  ?  262 SER   A OG   1 
ATOM   685  N  N    . ALA   A 1 111 ? 16.19700 -5.92300  18.98100 1.000 15.57292  ?  263 ALA   A N    1 
ATOM   686  C  CA   . ALA   A 1 111 ? 15.49100 -4.65300  18.82400 1.000 16.35151  ?  263 ALA   A CA   1 
ATOM   687  C  C    . ALA   A 1 111 ? 15.72700 -3.73000  20.01000 1.000 15.79395  ?  263 ALA   A C    1 
ATOM   688  O  O    . ALA   A 1 111 ? 16.02300 -2.54200  19.84000 1.000 16.10683  ?  263 ALA   A O    1 
ATOM   689  C  CB   . ALA   A 1 111 ? 13.98900 -4.89200  18.63300 1.000 16.96291  ?  263 ALA   A CB   1 
ATOM   690  N  N    . ILE   A 1 112 ? 15.58800 -4.25900  21.22600 1.000 15.26729  ?  264 ILE   A N    1 
ATOM   691  C  CA   . ILE   A 1 112 ? 15.77300 -3.42400  22.41000 1.000 16.41339  ?  264 ILE   A CA   1 
ATOM   692  C  C    . ILE   A 1 112 ? 17.17900 -2.83700  22.42700 1.000 16.87638  ?  264 ILE   A C    1 
ATOM   693  O  O    . ILE   A 1 112 ? 17.38200 -1.67200  22.79300 1.000 17.79502  ?  264 ILE   A O    1 
ATOM   694  C  CB   . ILE   A 1 112 ? 15.47400 -4.23300  23.68800 1.000 20.22533  ?  264 ILE   A CB   1 
ATOM   695  C  CG1  . ILE   A 1 112 ? 15.61200 -3.34500  24.92400 1.000 19.73430  ?  264 ILE   A CG1  1 
ATOM   696  C  CG2  . ILE   A 1 112 ? 16.39600 -5.45500  23.79900 1.000 20.94148  ?  264 ILE   A CG2  1 
ATOM   697  C  CD1  . ILE   A 1 112 ? 14.66800 -2.19500  24.90600 1.000 17.97227  ?  264 ILE   A CD1  1 
ATOM   698  N  N    . GLU   A 1 113 ? 18.16400 -3.62400  21.99600 1.000 15.57845  ?  265 GLU   A N    1 
ATOM   699  C  CA   . GLU   A 1 113 ? 19.54800 -3.15500  22.01200 1.000 17.57099  ?  265 GLU   A CA   1 
ATOM   700  C  C    . GLU   A 1 113 ? 19.78200 -2.09000  20.94400 1.000 17.14761  ?  265 GLU   A C    1 
ATOM   701  O  O    . GLU   A 1 113 ? 20.48500 -1.10200  21.18600 1.000 17.26525  ?  265 GLU   A O    1 
ATOM   702  C  CB   . GLU   A 1 113 ? 20.49700 -4.33600  21.80500 1.000 18.91165  ?  265 GLU   A CB   1 
ATOM   703  C  CG   . GLU   A 1 113 ? 20.53400 -5.34600  22.94600 1.000 19.12246  ?  265 GLU   A CG   1 
ATOM   704  C  CD   . GLU   A 1 113 ? 21.40900 -6.53800  22.60900 1.000 21.96032  ?  265 GLU   A CD   1 
ATOM   705  O  OE1  . GLU   A 1 113 ? 22.35300 -6.38000  21.79600 1.000 20.03456  ?  265 GLU   A OE1  1 
ATOM   706  O  OE2  . GLU   A 1 113 ? 21.14000 -7.63600  23.13600 1.000 23.76540  ?  265 GLU   A OE2  1 
ATOM   707  N  N    . VAL   A 1 114 ? 19.19900 -2.26500  19.75700 1.000 17.19091  ?  266 VAL   A N    1 
ATOM   708  C  CA   . VAL   A 1 114 ? 19.39500 -1.25000  18.72500 1.000 15.98437  ?  266 VAL   A CA   1 
ATOM   709  C  C    . VAL   A 1 114 ? 18.67400 0.04200   19.08800 1.000 14.51150  ?  266 VAL   A C    1 
ATOM   710  O  O    . VAL   A 1 114 ? 19.16500 1.13700   18.78700 1.000 16.64697  ?  266 VAL   A O    1 
ATOM   711  C  CB   . VAL   A 1 114 ? 18.94900 -1.77600  17.35300 1.000 14.93893  ?  266 VAL   A CB   1 
ATOM   712  C  CG1  . VAL   A 1 114 ? 19.30100 -0.75300  16.27600 1.000 12.46461  ?  266 VAL   A CG1  1 
ATOM   713  C  CG2  . VAL   A 1 114 ? 19.59500 -3.12800  17.07300 1.000 16.28270  ?  266 VAL   A CG2  1 
ATOM   714  N  N    . ILE   A 1 115 ? 17.51000 -0.05100  19.74100 1.000 13.00807  ?  267 ILE   A N    1 
ATOM   715  C  CA   . ILE   A 1 115 ? 16.84600 1.15900   20.21600 1.000 12.47282  ?  267 ILE   A CA   1 
ATOM   716  C  C    . ILE   A 1 115 ? 17.76300 1.92400   21.16600 1.000 15.92413  ?  267 ILE   A C    1 
ATOM   717  O  O    . ILE   A 1 115 ? 17.91300 3.15200   21.06600 1.000 17.52712  ?  267 ILE   A O    1 
ATOM   718  C  CB   . ILE   A 1 115 ? 15.49100 0.79900   20.86400 1.000 15.03602  ?  267 ILE   A CB   1 
ATOM   719  C  CG1  . ILE   A 1 115 ? 14.51700 0.31000   19.79000 1.000 15.71185  ?  267 ILE   A CG1  1 
ATOM   720  C  CG2  . ILE   A 1 115 ? 14.90100 1.99300   21.59100 1.000 14.91931  ?  267 ILE   A CG2  1 
ATOM   721  C  CD1  . ILE   A 1 115 ? 13.28200 -0.42400  20.34800 1.000 16.88637  ?  267 ILE   A CD1  1 
ATOM   722  N  N    . MET   A 1 116 ? 18.41700 1.20900   22.08200 1.000 14.34890  ?  268 MET   A N    1 
ATOM   723  C  CA   . MET   A 1 116 ? 19.36100 1.86700   22.98400 1.000 17.07235  ?  268 MET   A CA   1 
ATOM   724  C  C    . MET   A 1 116 ? 20.52000 2.48400   22.20800 1.000 16.90833  ?  268 MET   A C    1 
ATOM   725  O  O    . MET   A 1 116 ? 20.89900 3.63800   22.45400 1.000 16.82250  ?  268 MET   A O    1 
ATOM   726  C  CB   . MET   A 1 116 ? 19.86000 0.86800   24.03300 1.000 18.03731  ?  268 MET   A CB   1 
ATOM   727  C  CG   . MET   A 1 116 ? 18.76000 0.46700   25.03800 1.000 21.72929  ?  268 MET   A CG   1 
ATOM   728  S  SD   . MET   A 1 116 ? 19.18600 -0.91700  26.13700 1.000 24.05532  ?  268 MET   A SD   1 
ATOM   729  C  CE   . MET   A 1 116 ? 17.68800 -1.03200  27.11700 1.000 22.48251  ?  268 MET   A CE   1 
ATOM   730  N  N    . LEU   A 1 117 ? 21.06400 1.75000   21.23200 1.000 17.62662  ?  269 LEU   A N    1 
ATOM   731  C  CA   . LEU   A 1 117 ? 22.14800 2.29600   20.41400 1.000 19.97851  ?  269 LEU   A CA   1 
ATOM   732  C  C    . LEU   A 1 117 ? 21.68700 3.52200   19.64100 1.000 20.74503  ?  269 LEU   A C    1 
ATOM   733  O  O    . LEU   A 1 117 ? 22.34000 4.57300   19.67100 1.000 20.58996  ?  269 LEU   A O    1 
ATOM   734  C  CB   . LEU   A 1 117 ? 22.66700 1.24400   19.43600 1.000 21.71420  ?  269 LEU   A CB   1 
ATOM   735  C  CG   . LEU   A 1 117 ? 23.67900 0.19500   19.86500 1.000 24.11065  ?  269 LEU   A CG   1 
ATOM   736  C  CD1  . LEU   A 1 117 ? 23.87300 -0.77800  18.71400 1.000 24.64484  ?  269 LEU   A CD1  1 
ATOM   737  C  CD2  . LEU   A 1 117 ? 25.01300 0.85000   20.27300 1.000 25.75597  ?  269 LEU   A CD2  1 
ATOM   738  N  N    . ARG   A 1 118 ? 20.56100 3.39700   18.92400 1.000 19.27674  ?  270 ARG   A N    1 
ATOM   739  C  CA   . ARG   A 1 118 ? 20.05500 4.50100   18.11600 1.000 19.33305  ?  270 ARG   A CA   1 
ATOM   740  C  C    . ARG   A 1 118 ? 19.75500 5.72300   18.95900 1.000 17.14232  ?  270 ARG   A C    1 
ATOM   741  O  O    . ARG   A 1 118 ? 19.92700 6.85600   18.49400 1.000 21.12117  ?  270 ARG   A O    1 
ATOM   742  C  CB   . ARG   A 1 118 ? 18.78600 4.06800   17.37300 1.000 21.92179  ?  270 ARG   A CB   1 
ATOM   743  C  CG   . ARG   A 1 118 ? 19.07300 3.16800   16.20100 1.000 25.95737  ?  270 ARG   A CG   1 
ATOM   744  C  CD   . ARG   A 1 118 ? 17.82800 2.51700   15.61000 1.000 28.45828  ?  270 ARG   A CD   1 
ATOM   745  N  NE   . ARG   A 1 118 ? 17.20200 3.36100   14.60200 1.000 28.61920  ?  270 ARG   A NE   1 
ATOM   746  C  CZ   . ARG   A 1 118 ? 16.25400 4.24000   14.88100 1.000 27.51548  ?  270 ARG   A CZ   1 
ATOM   747  N  NH1  . ARG   A 1 118 ? 15.83500 4.37300   16.13400 1.000 26.77839  ?  270 ARG   A NH1  1 
ATOM   748  N  NH2  . ARG   A 1 118 ? 15.72100 4.97600   13.91400 1.000 28.12993  ?  270 ARG   A NH2  1 
ATOM   749  N  N    . SER   A 1 119 ? 19.29900 5.51500   20.19400 1.000 14.41330  ?  271 SER   A N    1 
ATOM   750  C  CA   . SER   A 1 119 ? 18.93900 6.63100   21.06100 1.000 17.86319  ?  271 SER   A CA   1 
ATOM   751  C  C    . SER   A 1 119 ? 20.13800 7.49200   21.43700 1.000 19.60426  ?  271 SER   A C    1 
ATOM   752  O  O    . SER   A 1 119 ? 19.95500 8.63100   21.88800 1.000 19.80337  ?  271 SER   A O    1 
ATOM   753  C  CB   . SER   A 1 119 ? 18.24400 6.10600   22.32000 1.000 18.34399  ?  271 SER   A CB   1 
ATOM   754  O  OG   . SER   A 1 119 ? 19.18500 5.72900   23.30000 1.000 20.54542  ?  271 SER   A OG   1 
ATOM   755  N  N    . ASN   A 1 120 ? 21.35900 6.98400   21.26200 1.000 20.25165  ?  272 ASN   A N    1 
ATOM   756  C  CA   . ASN   A 1 120 ? 22.53600 7.77400   21.60500 1.000 20.03715  ?  272 ASN   A CA   1 
ATOM   757  C  C    . ASN   A 1 120 ? 22.64900 9.03600   20.76300 1.000 22.14009  ?  272 ASN   A C    1 
ATOM   758  O  O    . ASN   A 1 120 ? 23.27100 10.01000  21.20400 1.000 21.54891  ?  272 ASN   A O    1 
ATOM   759  C  CB   . ASN   A 1 120 ? 23.79200 6.93000   21.44600 1.000 20.92010  ?  272 ASN   A CB   1 
ATOM   760  C  CG   . ASN   A 1 120 ? 24.98900 7.53700   22.15300 1.000 23.63745  ?  272 ASN   A CG   1 
ATOM   761  O  OD1  . ASN   A 1 120 ? 24.98100 7.72400   23.37500 1.000 24.68239  ?  272 ASN   A OD1  1 
ATOM   762  N  ND2  . ASN   A 1 120 ? 26.01300 7.87000   21.38700 1.000 23.47443  ?  272 ASN   A ND2  1 
ATOM   763  N  N    . GLN   A 1 121 ? 22.05500 9.04000   19.56700 1.000 22.16697  ?  273 GLN   A N    1 
ATOM   764  C  CA   . GLN   A 1 121 ? 22.11800 10.21100  18.70000 1.000 23.54398  ?  273 GLN   A CA   1 
ATOM   765  C  C    . GLN   A 1 121 ? 21.44700 11.41600  19.34900 1.000 24.95277  ?  273 GLN   A C    1 
ATOM   766  O  O    . GLN   A 1 121 ? 21.94000 12.54300  19.23500 1.000 27.31519  ?  273 GLN   A O    1 
ATOM   767  C  CB   . GLN   A 1 121 ? 21.48100 9.88500   17.34400 1.000 24.46302  ?  273 GLN   A CB   1 
ATOM   768  C  CG   . GLN   A 1 121 ? 21.52600 11.01400  16.30900 1.000 27.51681  ?  273 GLN   A CG   1 
ATOM   769  C  CD   . GLN   A 1 121 ? 21.30300 10.51800  14.87700 1.000 29.72302  ?  273 GLN   A CD   1 
ATOM   770  O  OE1  . GLN   A 1 121 ? 21.49500 9.33500   14.57000 1.000 29.58279  ?  273 GLN   A OE1  1 
ATOM   771  N  NE2  . GLN   A 1 121 ? 20.91900 11.43100  13.99100 1.000 30.22181  ?  273 GLN   A NE2  1 
ATOM   772  N  N    . SER   A 1 122 ? 20.33200 11.19900  20.05500 1.000 22.57188  ?  274 SER   A N    1 
ATOM   773  C  CA   . SER   A 1 122 ? 19.64900 12.28700  20.75100 1.000 23.93815  ?  274 SER   A CA   1 
ATOM   774  C  C    . SER   A 1 122 ? 20.15700 12.51800  22.16900 1.000 24.65046  ?  274 SER   A C    1 
ATOM   775  O  O    . SER   A 1 122 ? 19.80800 13.53800  22.77400 1.000 26.05020  ?  274 SER   A O    1 
ATOM   776  C  CB   . SER   A 1 122 ? 18.13900 12.02800  20.81600 1.000 24.46557  ?  274 SER   A CB   1 
ATOM   777  O  OG   . SER   A 1 122 ? 17.85000 10.92900  21.66300 1.000 24.93753  ?  274 SER   A OG   1 
ATOM   778  N  N    . PHE   A 1 123 ? 20.92400 11.58800  22.73000 1.000 23.61078  ?  275 PHE   A N    1 
ATOM   779  C  CA   . PHE   A 1 123 ? 21.43600 11.76100  24.08300 1.000 24.63958  ?  275 PHE   A CA   1 
ATOM   780  C  C    . PHE   A 1 123 ? 22.39000 12.94900  24.13200 1.000 27.05578  ?  275 PHE   A C    1 
ATOM   781  O  O    . PHE   A 1 123 ? 23.19300 13.15300  23.21900 1.000 29.22357  ?  275 PHE   A O    1 
ATOM   782  C  CB   . PHE   A 1 123 ? 22.15100 10.48600  24.53900 1.000 23.36085  ?  275 PHE   A CB   1 
ATOM   783  C  CG   . PHE   A 1 123 ? 22.52500 10.48400  26.00200 1.000 24.71001  ?  275 PHE   A CG   1 
ATOM   784  C  CD1  . PHE   A 1 123 ? 21.57800 10.19300  26.97300 1.000 25.73457  ?  275 PHE   A CD1  1 
ATOM   785  C  CD2  . PHE   A 1 123 ? 23.82400 10.77700  26.40200 1.000 24.63742  ?  275 PHE   A CD2  1 
ATOM   786  C  CE1  . PHE   A 1 123 ? 21.91600 10.19200  28.32300 1.000 25.63179  ?  275 PHE   A CE1  1 
ATOM   787  C  CE2  . PHE   A 1 123 ? 24.17500 10.76900  27.74900 1.000 26.45994  ?  275 PHE   A CE2  1 
ATOM   788  C  CZ   . PHE   A 1 123 ? 23.22500 10.47900  28.70900 1.000 26.33679  ?  275 PHE   A CZ   1 
ATOM   789  N  N    . THR   A 1 124 ? 22.28600 13.75100  25.19000 1.000 28.60731  ?  276 THR   A N    1 
ATOM   790  C  CA   . THR   A 1 124 ? 23.22600 14.84100  25.43300 1.000 31.91339  ?  276 THR   A CA   1 
ATOM   791  C  C    . THR   A 1 124 ? 23.82000 14.71000  26.82800 1.000 32.71227  ?  276 THR   A C    1 
ATOM   792  O  O    . THR   A 1 124 ? 23.08900 14.55200  27.81100 1.000 30.47884  ?  276 THR   A O    1 
ATOM   793  C  CB   . THR   A 1 124 ? 22.57300 16.22300  25.28000 1.000 34.43992  ?  276 THR   A CB   1 
ATOM   794  O  OG1  . THR   A 1 124 ? 23.46100 17.22000  25.80300 1.000 36.58637  ?  276 THR   A OG1  1 
ATOM   795  C  CG2  . THR   A 1 124 ? 21.25000 16.30000  26.03000 1.000 34.17812  ?  276 THR   A CG2  1 
ATOM   796  N  N    . MET   A 1 125 ? 25.14900 14.78900  26.91100 1.000 35.10395  ?  277 MET   A N    1 
ATOM   797  C  CA   . MET   A 1 125 ? 25.81800 14.72500  28.20400 1.000 37.71607  ?  277 MET   A CA   1 
ATOM   798  C  C    . MET   A 1 125 ? 25.67000 16.00900  29.01100 1.000 40.80645  ?  277 MET   A C    1 
ATOM   799  O  O    . MET   A 1 125 ? 26.05100 16.02000  30.18500 1.000 41.15305  ?  277 MET   A O    1 
ATOM   800  C  CB   . MET   A 1 125 ? 27.29600 14.38900  27.99800 1.000 36.49426  ?  277 MET   A CB   1 
ATOM   801  C  CG   . MET   A 1 125 ? 27.50800 12.98800  27.45100 1.000 36.27502  ?  277 MET   A CG   1 
ATOM   802  S  SD   . MET   A 1 125 ? 29.11600 12.25400  27.76700 1.000 39.74747  ?  277 MET   A SD   1 
ATOM   803  C  CE   . MET   A 1 125 ? 30.16600 13.18200  26.64500 1.000 40.16291  ?  277 MET   A CE   1 
ATOM   804  N  N    . ASP   A 1 126 ? 25.09500 17.05400  28.42700 1.000 43.09648  ?  278 ASP   A N    1 
ATOM   805  C  CA   . ASP   A 1 126 ? 24.89500 18.32400  29.16200 1.000 47.03487  ?  278 ASP   A CA   1 
ATOM   806  C  C    . ASP   A 1 126 ? 24.06100 18.05500  30.40500 1.000 46.11606  ?  278 ASP   A C    1 
ATOM   807  O  O    . ASP   A 1 126 ? 24.38200 18.56200  31.42900 1.000 46.33124  ?  278 ASP   A O    1 
ATOM   808  C  CB   . ASP   A 1 126 ? 24.13300 19.38300  28.37300 1.000 51.33777  ?  278 ASP   A CB   1 
ATOM   809  C  CG   . ASP   A 1 126 ? 24.77700 19.77900  27.07400 1.000 55.28370  ?  278 ASP   A CG   1 
ATOM   810  O  OD1  . ASP   A 1 126 ? 24.06000 20.25800  26.21200 1.000 57.51806  ?  278 ASP   A OD1  1 
ATOM   811  O  OD2  . ASP   A 1 126 ? 25.98000 19.61200  26.94200 1.000 56.90558  ?  278 ASP   A OD2  1 
ATOM   812  N  N    . ASP   A 1 127 ? 22.99400 17.29500  30.27100 1.000 44.64465  ?  279 ASP   A N    1 
ATOM   813  C  CA   . ASP   A 1 127 ? 22.15000 17.00000  31.42100 1.000 44.05964  ?  279 ASP   A CA   1 
ATOM   814  C  C    . ASP   A 1 127 ? 21.70200 15.54300  31.44200 1.000 40.05109  ?  279 ASP   A C    1 
ATOM   815  O  O    . ASP   A 1 127 ? 20.71000 15.22600  32.10400 1.000 40.38810  ?  279 ASP   A O    1 
ATOM   816  C  CB   . ASP   A 1 127 ? 20.94200 17.94500  31.45700 1.000 46.47984  ?  279 ASP   A CB   1 
ATOM   817  C  CG   . ASP   A 1 127 ? 20.10400 17.88600  30.19500 1.000 47.19294  ?  279 ASP   A CG   1 
ATOM   818  O  OD1  . ASP   A 1 127 ? 19.05600 18.56600  30.16300 1.000 48.49840  ?  279 ASP   A OD1  1 
ATOM   819  O  OD2  . ASP   A 1 127 ? 20.47800 17.17100  29.24300 1.000 46.60580  ?  279 ASP   A OD2  1 
ATOM   820  N  N    . MET   A 1 128 ? 22.41200 14.65400  30.73600 1.000 35.36684  ?  280 MET   A N    1 
ATOM   821  C  CA   . MET   A 1 128 ? 22.14800 13.21300  30.76300 1.000 32.07408  ?  280 MET   A CA   1 
ATOM   822  C  C    . MET   A 1 128 ? 20.69000 12.91000  30.41300 1.000 29.16142  ?  280 MET   A C    1 
ATOM   823  O  O    . MET   A 1 128 ? 19.99400 12.15900  31.10400 1.000 27.96875  ?  280 MET   A O    1 
ATOM   824  C  CB   . MET   A 1 128 ? 22.52900 12.62000  32.11900 1.000 33.58401  ?  280 MET   A CB   1 
ATOM   825  C  CG   . MET   A 1 128 ? 23.92200 13.03000  32.55600 1.000 34.96737  ?  280 MET   A CG   1 
ATOM   826  S  SD   . MET   A 1 128 ? 25.15100 12.45600  31.37900 1.000 34.80105  ?  280 MET   A SD   1 
ATOM   827  C  CE   . MET   A 1 128 ? 26.66600 13.09200  32.11800 1.000 33.86950  ?  280 MET   A CE   1 
ATOM   828  N  N    . SER   A 1 129 ? 20.22700 13.51400  29.32600 1.000 26.81451  ?  281 SER   A N    1 
ATOM   829  C  CA   . SER   A 1 129 ? 18.86300 13.33700  28.86400 1.000 28.17357  ?  281 SER   A CA   1 
ATOM   830  C  C    . SER   A 1 129 ? 18.88400 13.07700  27.36500 1.000 27.73705  ?  281 SER   A C    1 
ATOM   831  O  O    . SER   A 1 129 ? 19.90000 13.26800  26.69400 1.000 27.77911  ?  281 SER   A O    1 
ATOM   832  C  CB   . SER   A 1 129 ? 18.00200 14.56200  29.19800 1.000 29.49978  ?  281 SER   A CB   1 
ATOM   833  O  OG   . SER   A 1 129 ? 18.18400 15.57700  28.22900 1.000 31.46509  ?  281 SER   A OG   1 
ATOM   834  N  N    . TRP   A 1 130 ? 17.74700 12.63000  26.84100 1.000 27.48271  ?  282 TRP   A N    1 
ATOM   835  C  CA   . TRP   A 1 130 ? 17.57300 12.39500  25.41500 1.000 26.63422  ?  282 TRP   A CA   1 
ATOM   836  C  C    . TRP   A 1 130 ? 16.74000 13.53700  24.84800 1.000 27.91432  ?  282 TRP   A C    1 
ATOM   837  O  O    . TRP   A 1 130 ? 15.57200 13.69500  25.21500 1.000 30.18103  ?  282 TRP   A O    1 
ATOM   838  C  CB   . TRP   A 1 130 ? 16.89000 11.05600  25.16200 1.000 24.88493  ?  282 TRP   A CB   1 
ATOM   839  C  CG   . TRP   A 1 130 ? 17.68900 9.81600   25.52000 1.000 23.81581  ?  282 TRP   A CG   1 
ATOM   840  C  CD1  . TRP   A 1 130 ? 18.46300 9.06900   24.67900 1.000 23.29835  ?  282 TRP   A CD1  1 
ATOM   841  C  CD2  . TRP   A 1 130 ? 17.73000 9.15300   26.79200 1.000 22.26938  ?  282 TRP   A CD2  1 
ATOM   842  N  NE1  . TRP   A 1 130 ? 18.99400 7.99400   25.34900 1.000 22.56716  ?  282 TRP   A NE1  1 
ATOM   843  C  CE2  . TRP   A 1 130 ? 18.55800 8.02200   26.64700 1.000 21.79057  ?  282 TRP   A CE2  1 
ATOM   844  C  CE3  . TRP   A 1 130 ? 17.15400 9.41200   28.04000 1.000 22.95230  ?  282 TRP   A CE3  1 
ATOM   845  C  CZ2  . TRP   A 1 130 ? 18.83700 7.15800   27.70700 1.000 21.91046  ?  282 TRP   A CZ2  1 
ATOM   846  C  CZ3  . TRP   A 1 130 ? 17.42600 8.54300   29.09500 1.000 22.87165  ?  282 TRP   A CZ3  1 
ATOM   847  C  CH2  . TRP   A 1 130 ? 18.25900 7.43200   28.91800 1.000 21.66110  ?  282 TRP   A CH2  1 
ATOM   848  N  N    . ASP   A 1 131 ? 17.33800 14.32700  23.95900 1.000 27.57977  ?  283 ASP   A N    1 
ATOM   849  C  CA   . ASP   A 1 131 ? 16.73600 15.57100  23.48200 1.000 30.13284  ?  283 ASP   A CA   1 
ATOM   850  C  C    . ASP   A 1 131 ? 16.22000 15.34300  22.06800 1.000 29.25626  ?  283 ASP   A C    1 
ATOM   851  O  O    . ASP   A 1 131 ? 16.99200 15.32200  21.10500 1.000 29.44261  ?  283 ASP   A O    1 
ATOM   852  C  CB   . ASP   A 1 131 ? 17.74100 16.71800  23.54000 1.000 33.26505  ?  283 ASP   A CB   1 
ATOM   853  C  CG   . ASP   A 1 131 ? 17.09300 18.07700  23.32300 1.000 37.31629  ?  283 ASP   A CG   1 
ATOM   854  O  OD1  . ASP   A 1 131 ? 15.90300 18.12700  22.93200 1.000 37.96740  ?  283 ASP   A OD1  1 
ATOM   855  O  OD2  . ASP   A 1 131 ? 17.77900 19.09700  23.54500 1.000 39.35848  ?  283 ASP   A OD2  1 
ATOM   856  N  N    . CYS   A 1 132 ? 14.90900 15.18500  21.94500 1.000 29.97803  ?  284 CYS   A N    1 
ATOM   857  C  CA   . CYS   A 1 132 ? 14.28200 14.92100  20.65300 1.000 29.05561  ?  284 CYS   A CA   1 
ATOM   858  C  C    . CYS   A 1 132 ? 13.58000 16.15700  20.08900 1.000 31.92464  ?  284 CYS   A C    1 
ATOM   859  O  O    . CYS   A 1 132 ? 12.43800 16.09400  19.62600 1.000 29.25674  ?  284 CYS   A O    1 
ATOM   860  C  CB   . CYS   A 1 132 ? 13.33200 13.74000  20.77700 1.000 28.52062  ?  284 CYS   A CB   1 
ATOM   861  S  SG   . CYS   A 1 132 ? 14.23900 12.19400  20.99300 1.000 26.33021  ?  284 CYS   A SG   1 
ATOM   862  N  N    . GLY   A 1 133 ? 14.26800 17.30200  20.10400 1.000 36.61829  ?  285 GLY   A N    1 
ATOM   863  C  CA   . GLY   A 1 133 ? 13.87200 18.46700  19.33500 1.000 38.53239  ?  285 GLY   A CA   1 
ATOM   864  C  C    . GLY   A 1 133 ? 13.07700 19.52000  20.08300 1.000 40.53971  ?  285 GLY   A C    1 
ATOM   865  O  O    . GLY   A 1 133 ? 12.96000 20.64700  19.58700 1.000 42.04310  ?  285 GLY   A O    1 
ATOM   866  N  N    . SER   A 1 134 ? 12.52800 19.19700  21.25100 1.000 40.04826  ?  286 SER   A N    1 
ATOM   867  C  CA   . SER   A 1 134 ? 11.63400 20.11800  21.94300 1.000 41.83134  ?  286 SER   A CA   1 
ATOM   868  C  C    . SER   A 1 134 ? 11.43500 19.62900  23.36900 1.000 41.91454  ?  286 SER   A C    1 
ATOM   869  O  O    . SER   A 1 134 ? 11.73700 18.47900  23.69900 1.000 39.90596  ?  286 SER   A O    1 
ATOM   870  C  CB   . SER   A 1 134 ? 10.29000 20.24500  21.22300 1.000 43.44976  ?  286 SER   A CB   1 
ATOM   871  O  OG   . SER   A 1 134 ? 9.49600  19.09700  21.44500 1.000 42.96453  ?  286 SER   A OG   1 
ATOM   872  N  N    . GLN   A 1 135 ? 10.89700 20.52000  24.20600 1.000 44.60448  ?  287 GLN   A N    1 
ATOM   873  C  CA   . GLN   A 1 135 ? 10.81300 20.25100  25.63800 1.000 47.28670  ?  287 GLN   A CA   1 
ATOM   874  C  C    . GLN   A 1 135 ? 9.90900  19.06000  25.93600 1.000 46.14117  ?  287 GLN   A C    1 
ATOM   875  O  O    . GLN   A 1 135 ? 10.23300 18.22600  26.79100 1.000 45.05491  ?  287 GLN   A O    1 
ATOM   876  C  CB   . GLN   A 1 135 ? 10.32300 21.50200  26.37000 1.000 51.48059  ?  287 GLN   A CB   1 
ATOM   877  C  CG   . GLN   A 1 135 ? 10.57400 21.49700  27.86700 1.000 54.82996  ?  287 GLN   A CG   1 
ATOM   878  C  CD   . GLN   A 1 135 ? 12.03700 21.32500  28.21400 1.000 57.46636  ?  287 GLN   A CD   1 
ATOM   879  O  OE1  . GLN   A 1 135 ? 12.90700 21.98400  27.64100 1.000 59.01004  ?  287 GLN   A OE1  1 
ATOM   880  N  NE2  . GLN   A 1 135 ? 12.31900 20.43500  29.15800 1.000 57.76687  ?  287 GLN   A NE2  1 
ATOM   881  N  N    . ASP   A 1 136 ? 8.77000  18.96200  25.24600 1.000 46.41531  ?  288 ASP   A N    1 
ATOM   882  C  CA   . ASP   A 1 136 ? 7.86100  17.84900  25.50200 1.000 45.85115  ?  288 ASP   A CA   1 
ATOM   883  C  C    . ASP   A 1 136 ? 8.49000  16.51000  25.14600 1.000 40.03246  ?  288 ASP   A C    1 
ATOM   884  O  O    . ASP   A 1 136 ? 8.16300  15.49000  25.76100 1.000 39.11166  ?  288 ASP   A O    1 
ATOM   885  C  CB   . ASP   A 1 136 ? 6.55400  18.03800  24.73400 1.000 49.79736  ?  288 ASP   A CB   1 
ATOM   886  C  CG   . ASP   A 1 136 ? 5.62200  19.01800  25.41100 1.000 57.16999  ?  288 ASP   A CG   1 
ATOM   887  O  OD1  . ASP   A 1 136 ? 5.30100  20.05600  24.79600 1.000 61.36839  ?  288 ASP   A OD1  1 
ATOM   888  O  OD2  . ASP   A 1 136 ? 5.21900  18.75500  26.56500 1.000 60.46754  ?  288 ASP   A OD2  1 
ATOM   889  N  N    . TYR   A 1 137 ? 9.39000  16.49000  24.16700 1.000 36.37406  ?  289 TYR   A N    1 
ATOM   890  C  CA   . TYR   A 1 137 ? 10.05000 15.26400  23.73000 1.000 32.96707  ?  289 TYR   A CA   1 
ATOM   891  C  C    . TYR   A 1 137 ? 11.51900 15.25700  24.14300 1.000 31.38362  ?  289 TYR   A C    1 
ATOM   892  O  O    . TYR   A 1 137 ? 12.39400 14.81100  23.40500 1.000 31.09455  ?  289 TYR   A O    1 
ATOM   893  C  CB   . TYR   A 1 137 ? 9.89100  15.07600  22.22400 1.000 31.28986  ?  289 TYR   A CB   1 
ATOM   894  C  CG   . TYR   A 1 137 ? 8.47200  15.31400  21.75200 1.000 30.76658  ?  289 TYR   A CG   1 
ATOM   895  C  CD1  . TYR   A 1 137 ? 8.20800  16.08900  20.62700 1.000 32.20119  ?  289 TYR   A CD1  1 
ATOM   896  C  CD2  . TYR   A 1 137 ? 7.39800  14.76800  22.43400 1.000 29.86226  ?  289 TYR   A CD2  1 
ATOM   897  C  CE1  . TYR   A 1 137 ? 6.91000  16.31100  20.20300 1.000 31.79651  ?  289 TYR   A CE1  1 
ATOM   898  C  CE2  . TYR   A 1 137 ? 6.09800  14.98600  22.01700 1.000 30.69059  ?  289 TYR   A CE2  1 
ATOM   899  C  CZ   . TYR   A 1 137 ? 5.85800  15.76000  20.90300 1.000 31.97088  ?  289 TYR   A CZ   1 
ATOM   900  O  OH   . TYR   A 1 137 ? 4.55800  15.97200  20.48200 1.000 33.26015  ?  289 TYR   A OH   1 
ATOM   901  N  N    . LYS   A 1 138 ? 11.79800 15.76200  25.33500 1.000 30.99867  ?  290 LYS   A N    1 
ATOM   902  C  CA   . LYS   A 1 138 ? 13.10200 15.64100  25.96300 1.000 31.84811  ?  290 LYS   A CA   1 
ATOM   903  C  C    . LYS   A 1 138 ? 12.92700 14.72600  27.16600 1.000 29.88418  ?  290 LYS   A C    1 
ATOM   904  O  O    . LYS   A 1 138 ? 12.12900 15.02500  28.05800 1.000 28.94007  ?  290 LYS   A O    1 
ATOM   905  C  CB   . LYS   A 1 138 ? 13.63800 17.01300  26.36800 1.000 35.60825  ?  290 LYS   A CB   1 
ATOM   906  C  CG   . LYS   A 1 138 ? 15.10600 17.02500  26.77100 1.000 39.08845  ?  290 LYS   A CG   1 
ATOM   907  C  CD   . LYS   A 1 138 ? 15.52400 18.42600  27.18900 1.000 43.60896  ?  290 LYS   A CD   1 
ATOM   908  C  CE   . LYS   A 1 138 ? 16.79900 18.41100  28.01500 1.000 46.41554  ?  290 LYS   A CE   1 
ATOM   909  N  NZ   . LYS   A 1 138 ? 17.98900 18.78400  27.19900 1.000 48.31608  ?  290 LYS   A NZ   1 
ATOM   910  N  N    . TYR   A 1 139 ? 13.64500 13.60400  27.17800 1.000 28.59433  ?  291 TYR   A N    1 
ATOM   911  C  CA   . TYR   A 1 139 ? 13.40900 12.54200  28.15000 1.000 27.71474  ?  291 TYR   A CA   1 
ATOM   912  C  C    . TYR   A 1 139 ? 14.59000 12.41200  29.10200 1.000 27.85978  ?  291 TYR   A C    1 
ATOM   913  O  O    . TYR   A 1 139 ? 15.74300 12.34700  28.66200 1.000 26.71126  ?  291 TYR   A O    1 
ATOM   914  C  CB   . TYR   A 1 139 ? 13.14800 11.21500  27.43500 1.000 25.69602  ?  291 TYR   A CB   1 
ATOM   915  C  CG   . TYR   A 1 139 ? 12.12600 11.35400  26.33000 1.000 23.86374  ?  291 TYR   A CG   1 
ATOM   916  C  CD1  . TYR   A 1 139 ? 12.51300 11.37600  25.00000 1.000 23.07210  ?  291 TYR   A CD1  1 
ATOM   917  C  CD2  . TYR   A 1 139 ? 10.77200 11.49200  26.62300 1.000 24.44136  ?  291 TYR   A CD2  1 
ATOM   918  C  CE1  . TYR   A 1 139 ? 11.57800 11.51800  23.98400 1.000 23.64721  ?  291 TYR   A CE1  1 
ATOM   919  C  CE2  . TYR   A 1 139 ? 9.82400  11.62800  25.61000 1.000 23.30445  ?  291 TYR   A CE2  1 
ATOM   920  C  CZ   . TYR   A 1 139 ? 10.23700 11.64200  24.29400 1.000 23.69509  ?  291 TYR   A CZ   1 
ATOM   921  O  OH   . TYR   A 1 139 ? 9.31800  11.77700  23.27300 1.000 24.82668  ?  291 TYR   A OH   1 
ATOM   922  N  N    . ASP   A 1 140 ? 14.30000 12.37600  30.40100 1.000 29.37286  ?  292 ASP   A N    1 
ATOM   923  C  CA   . ASP   A 1 140 ? 15.31800 12.19400  31.43100 1.000 31.44840  ?  292 ASP   A CA   1 
ATOM   924  C  C    . ASP   A 1 140 ? 15.03900 10.90300  32.19800 1.000 28.71108  ?  292 ASP   A C    1 
ATOM   925  O  O    . ASP   A 1 140 ? 14.15700 10.11700  31.84000 1.000 27.78146  ?  292 ASP   A O    1 
ATOM   926  C  CB   . ASP   A 1 140 ? 15.37600 13.39800  32.38300 1.000 36.35733  ?  292 ASP   A CB   1 
ATOM   927  C  CG   . ASP   A 1 140 ? 14.02900 13.71300  33.02800 1.000 41.32603  ?  292 ASP   A CG   1 
ATOM   928  O  OD1  . ASP   A 1 140 ? 13.69800 14.90900  33.15900 1.000 44.89413  ?  292 ASP   A OD1  1 
ATOM   929  O  OD2  . ASP   A 1 140 ? 13.28900 12.77900  33.39800 1.000 41.97460  ?  292 ASP   A OD2  1 
ATOM   930  N  N    . VAL   A 1 141 ? 15.78000 10.70900  33.29000 1.000 28.03947  ?  293 VAL   A N    1 
ATOM   931  C  CA   . VAL   A 1 141 ? 15.64400 9.48000   34.06400 1.000 26.80038  ?  293 VAL   A CA   1 
ATOM   932  C  C    . VAL   A 1 141 ? 14.25600 9.38900   34.67900 1.000 27.34422  ?  293 VAL   A C    1 
ATOM   933  O  O    . VAL   A 1 141 ? 13.71700 8.29000   34.86800 1.000 27.58369  ?  293 VAL   A O    1 
ATOM   934  C  CB   . VAL   A 1 141 ? 16.74500 9.41700   35.13900 1.000 28.05756  ?  293 VAL   A CB   1 
ATOM   935  C  CG1  . VAL   A 1 141 ? 18.10400 9.12300   34.48200 1.000 28.42734  ?  293 VAL   A CG1  1 
ATOM   936  C  CG2  . VAL   A 1 141 ? 16.77400 10.71000  35.94200 1.000 27.86175  ?  293 VAL   A CG2  1 
ATOM   937  N  N    . THR   A 1 142 ? 13.65500 10.53500  35.00900 1.000 27.06948  ?  294 THR   A N    1 
ATOM   938  C  CA   . THR   A 1 142 ? 12.33600 10.52000  35.62900 1.000 29.21799  ?  294 THR   A CA   1 
ATOM   939  C  C    . THR   A 1 142 ? 11.27600 10.04200  34.64300 1.000 28.41680  ?  294 THR   A C    1 
ATOM   940  O  O    . THR   A 1 142 ? 10.34700 9.32200   35.02700 1.000 28.55878  ?  294 THR   A O    1 
ATOM   941  C  CB   . THR   A 1 142 ? 11.98900 11.90900  36.16100 1.000 31.78856  ?  294 THR   A CB   1 
ATOM   942  O  OG1  . THR   A 1 142 ? 13.07600 12.39100  36.96000 1.000 34.51807  ?  294 THR   A OG1  1 
ATOM   943  C  CG2  . THR   A 1 142 ? 10.73000 11.85000  37.01100 1.000 33.49719  ?  294 THR   A CG2  1 
ATOM   944  N  N    . ASP   A 1 143 ? 11.41000 10.41600  33.36700 1.000 27.72366  ?  295 ASP   A N    1 
ATOM   945  C  CA   . ASP   A 1 143 ? 10.46500 9.94300   32.35700 1.000 28.25714  ?  295 ASP   A CA   1 
ATOM   946  C  C    . ASP   A 1 143 ? 10.52200 8.42800   32.21500 1.000 26.62970  ?  295 ASP   A C    1 
ATOM   947  O  O    . ASP   A 1 143 ? 9.48000  7.76600   32.14100 1.000 26.48528  ?  295 ASP   A O    1 
ATOM   948  C  CB   . ASP   A 1 143 ? 10.74100 10.61900  31.01300 1.000 29.81968  ?  295 ASP   A CB   1 
ATOM   949  C  CG   . ASP   A 1 143 ? 10.37500 12.09000  31.01400 1.000 33.87501  ?  295 ASP   A CG   1 
ATOM   950  O  OD1  . ASP   A 1 143 ? 9.38600  12.46400  31.68200 1.000 35.65830  ?  295 ASP   A OD1  1 
ATOM   951  O  OD2  . ASP   A 1 143 ? 11.08000 12.87800  30.35400 1.000 34.51653  ?  295 ASP   A OD2  1 
ATOM   952  N  N    . VAL   A 1 144 ? 11.73000 7.86000   32.18500 1.000 25.73718  ?  296 VAL   A N    1 
ATOM   953  C  CA   . VAL   A 1 144 ? 11.86100 6.41500   32.04400 1.000 24.81438  ?  296 VAL   A CA   1 
ATOM   954  C  C    . VAL   A 1 144 ? 11.29700 5.71100   33.26600 1.000 25.97542  ?  296 VAL   A C    1 
ATOM   955  O  O    . VAL   A 1 144 ? 10.68000 4.64600   33.15500 1.000 26.65617  ?  296 VAL   A O    1 
ATOM   956  C  CB   . VAL   A 1 144 ? 13.33000 6.02700   31.79000 1.000 25.40221  ?  296 VAL   A CB   1 
ATOM   957  C  CG1  . VAL   A 1 144 ? 13.44600 4.52500   31.54800 1.000 24.31754  ?  296 VAL   A CG1  1 
ATOM   958  C  CG2  . VAL   A 1 144 ? 13.89000 6.80700   30.60500 1.000 24.04476  ?  296 VAL   A CG2  1 
ATOM   959  N  N    A SER   A 1 145 ? 11.50000 6.28700   34.45300 0.360 27.37213  ?  297 SER   A N    1 
ATOM   960  N  N    B SER   A 1 145 ? 11.49300 6.28600   34.45600 0.640 27.42240  ?  297 SER   A N    1 
ATOM   961  C  CA   A SER   A 1 145 ? 10.87800 5.73500   35.65100 0.360 28.39549  ?  297 SER   A CA   1 
ATOM   962  C  CA   B SER   A 1 145 ? 10.87700 5.70500   35.64400 0.640 28.33375  ?  297 SER   A CA   1 
ATOM   963  C  C    A SER   A 1 145 ? 9.35800  5.75700   35.54000 0.360 28.31054  ?  297 SER   A C    1 
ATOM   964  C  C    B SER   A 1 145 ? 9.35400  5.77400   35.57200 0.640 28.42116  ?  297 SER   A C    1 
ATOM   965  O  O    A SER   A 1 145 ? 8.67800  4.83600   36.00800 0.360 27.87520  ?  297 SER   A O    1 
ATOM   966  O  O    B SER   A 1 145 ? 8.66700  4.89200   36.10000 0.640 27.70433  ?  297 SER   A O    1 
ATOM   967  C  CB   A SER   A 1 145 ? 11.33500 6.51000   36.88700 0.360 30.23828  ?  297 SER   A CB   1 
ATOM   968  C  CB   B SER   A 1 145 ? 11.38900 6.40400   36.90700 0.640 30.21559  ?  297 SER   A CB   1 
ATOM   969  O  OG   A SER   A 1 145 ? 12.62200 6.09800   37.30100 0.360 29.85424  ?  297 SER   A OG   1 
ATOM   970  O  OG   B SER   A 1 145 ? 10.97400 7.75800   36.95100 0.640 32.10653  ?  297 SER   A OG   1 
ATOM   971  N  N    . LYS   A 1 146 ? 8.80800  6.79500   34.91100 1.000 28.73146  ?  298 LYS   A N    1 
ATOM   972  C  CA   . LYS   A 1 146 ? 7.36400  6.94200   34.77400 1.000 29.02229  ?  298 LYS   A CA   1 
ATOM   973  C  C    . LYS   A 1 146 ? 6.77900  6.05700   33.67700 1.000 28.05368  ?  298 LYS   A C    1 
ATOM   974  O  O    . LYS   A 1 146 ? 5.58000  6.15400   33.39600 1.000 28.48886  ?  298 LYS   A O    1 
ATOM   975  C  CB   . LYS   A 1 146 ? 7.01200  8.40900   34.51800 1.000 30.70331  ?  298 LYS   A CB   1 
ATOM   976  C  CG   . LYS   A 1 146 ? 7.28100  9.32800   35.72000 1.000 34.71462  ?  298 LYS   A CG   1 
ATOM   977  C  CD   . LYS   A 1 146 ? 6.57300  8.83000   36.96000 1.000 40.38240  ?  298 LYS   A CD   1 
ATOM   978  C  CE   . LYS   A 1 146 ? 5.77800  9.94100   37.63600 1.000 46.23876  ?  298 LYS   A CE   1 
ATOM   979  N  NZ   . LYS   A 1 146 ? 4.48000  9.45800   38.19500 1.000 50.54053  ?  298 LYS   A NZ   1 
ATOM   980  N  N    . ALA   A 1 147 ? 7.59300  5.21700   33.04200 1.000 26.33622  ?  299 ALA   A N    1 
ATOM   981  C  CA   . ALA   A 1 147 ? 7.10300  4.10900   32.23800 1.000 25.36960  ?  299 ALA   A CA   1 
ATOM   982  C  C    . ALA   A 1 147 ? 7.18300  2.78700   32.98800 1.000 25.53831  ?  299 ALA   A C    1 
ATOM   983  O  O    . ALA   A 1 147 ? 6.85700  1.74100   32.41800 1.000 24.38735  ?  299 ALA   A O    1 
ATOM   984  C  CB   . ALA   A 1 147 ? 7.88100  4.01400   30.91600 1.000 23.25048  ?  299 ALA   A CB   1 
ATOM   985  N  N    . GLY   A 1 148 ? 7.63200  2.81100   34.24700 1.000 26.42890  ?  300 GLY   A N    1 
ATOM   986  C  CA   . GLY   A 1 148 ? 7.64300  1.63800   35.09800 1.000 26.71898  ?  300 GLY   A CA   1 
ATOM   987  C  C    . GLY   A 1 148 ? 9.01300  1.09400   35.44900 1.000 27.04047  ?  300 GLY   A C    1 
ATOM   988  O  O    . GLY   A 1 148 ? 9.09100  0.13100   36.22000 1.000 28.39702  ?  300 GLY   A O    1 
ATOM   989  N  N    . HIS   A 1 149 ? 10.09300 1.67000   34.93100 1.000 24.74284  ?  301 HIS   A N    1 
ATOM   990  C  CA   . HIS   A 1 149 ? 11.40900 1.07100   35.08900 1.000 23.90740  ?  301 HIS   A CA   1 
ATOM   991  C  C    . HIS   A 1 149 ? 12.13800 1.65500   36.29500 1.000 25.28476  ?  301 HIS   A C    1 
ATOM   992  O  O    . HIS   A 1 149 ? 11.86000 2.77300   36.73100 1.000 25.81914  ?  301 HIS   A O    1 
ATOM   993  C  CB   . HIS   A 1 149 ? 12.23300 1.26300   33.81600 1.000 23.15840  ?  301 HIS   A CB   1 
ATOM   994  C  CG   . HIS   A 1 149 ? 11.80800 0.36100   32.69800 1.000 22.26576  ?  301 HIS   A CG   1 
ATOM   995  N  ND1  . HIS   A 1 149 ? 11.91800 -1.01200  32.76800 1.000 22.32649  ?  301 HIS   A ND1  1 
ATOM   996  C  CD2  . HIS   A 1 149 ? 11.24300 0.63300   31.49700 1.000 21.53413  ?  301 HIS   A CD2  1 
ATOM   997  C  CE1  . HIS   A 1 149 ? 11.44900 -1.54700  31.65300 1.000 21.89707  ?  301 HIS   A CE1  1 
ATOM   998  N  NE2  . HIS   A 1 149 ? 11.03800 -0.57000  30.86300 1.000 21.12981  ?  301 HIS   A NE2  1 
ATOM   999  N  N    . THR   A 1 150 ? 13.07700 0.87900   36.82700 1.000 26.38876  ?  302 THR   A N    1 
ATOM   1000 C  CA   . THR   A 1 150 ? 13.80900 1.20600   38.04400 1.000 26.65019  ?  302 THR   A CA   1 
ATOM   1001 C  C    . THR   A 1 150 ? 15.27800 1.47200   37.73500 1.000 26.40961  ?  302 THR   A C    1 
ATOM   1002 O  O    . THR   A 1 150 ? 15.76100 1.23500   36.62500 1.000 25.54607  ?  302 THR   A O    1 
ATOM   1003 C  CB   . THR   A 1 150 ? 13.69800 0.07000   39.06200 1.000 27.87933  ?  302 THR   A CB   1 
ATOM   1004 O  OG1  . THR   A 1 150 ? 14.50700 -1.03100  38.63000 1.000 28.85747  ?  302 THR   A OG1  1 
ATOM   1005 C  CG2  . THR   A 1 150 ? 12.25300 -0.39000  39.19700 1.000 29.54524  ?  302 THR   A CG2  1 
ATOM   1006 N  N    . LEU   A 1 151 ? 15.99400 1.95200   38.76000 1.000 25.93724  ?  303 LEU   A N    1 
ATOM   1007 C  CA   . LEU   A 1 151 ? 17.40900 2.29200   38.62200 1.000 26.84010  ?  303 LEU   A CA   1 
ATOM   1008 C  C    . LEU   A 1 151 ? 18.26000 1.08800   38.24400 1.000 26.36880  ?  303 LEU   A C    1 
ATOM   1009 O  O    . LEU   A 1 151 ? 19.34000 1.26000   37.66600 1.000 26.44684  ?  303 LEU   A O    1 
ATOM   1010 C  CB   . LEU   A 1 151 ? 17.91700 2.91700   39.92900 1.000 31.24180  ?  303 LEU   A CB   1 
ATOM   1011 C  CG   . LEU   A 1 151 ? 19.34100 3.48000   40.01500 1.000 35.53479  ?  303 LEU   A CG   1 
ATOM   1012 C  CD1  . LEU   A 1 151 ? 19.38600 4.72300   40.89700 1.000 38.02472  ?  303 LEU   A CD1  1 
ATOM   1013 C  CD2  . LEU   A 1 151 ? 20.31400 2.43700   40.54800 1.000 37.93803  ?  303 LEU   A CD2  1 
ATOM   1014 N  N    . GLU   A 1 152 ? 17.79900 -0.12400  38.55600 1.000 27.66845  ?  304 GLU   A N    1 
ATOM   1015 C  CA   . GLU   A 1 152 ? 18.49800 -1.32900  38.12900 1.000 29.85141  ?  304 GLU   A CA   1 
ATOM   1016 C  C    . GLU   A 1 152 ? 18.78400 -1.30700  36.63400 1.000 26.22211  ?  304 GLU   A C    1 
ATOM   1017 O  O    . GLU   A 1 152 ? 19.84000 -1.77200  36.18700 1.000 24.10620  ?  304 GLU   A O    1 
ATOM   1018 C  CB   . GLU   A 1 152 ? 17.66600 -2.55700  38.48600 1.000 36.92384  ?  304 GLU   A CB   1 
ATOM   1019 C  CG   . GLU   A 1 152 ? 17.73100 -2.95400  39.93500 1.000 44.29511  ?  304 GLU   A CG   1 
ATOM   1020 C  CD   . GLU   A 1 152 ? 18.39800 -4.29700  40.12600 1.000 50.49383  ?  304 GLU   A CD   1 
ATOM   1021 O  OE1  . GLU   A 1 152 ? 19.58000 -4.43900  39.74000 1.000 52.03739  ?  304 GLU   A OE1  1 
ATOM   1022 O  OE2  . GLU   A 1 152 ? 17.73600 -5.21300  40.65700 1.000 55.18639  ?  304 GLU   A OE2  1 
ATOM   1023 N  N    . LEU   A 1 153 ? 17.83700 -0.78900  35.84200 1.000 24.53530  ?  305 LEU   A N    1 
ATOM   1024 C  CA   . LEU   A 1 153 ? 18.02800 -0.59300  34.41000 1.000 21.24446  ?  305 LEU   A CA   1 
ATOM   1025 C  C    . LEU   A 1 153 ? 18.53600 0.80800   34.09400 1.000 22.69198  ?  305 LEU   A C    1 
ATOM   1026 O  O    . LEU   A 1 153 ? 19.44700 0.96800   33.27100 1.000 22.43746  ?  305 LEU   A O    1 
ATOM   1027 C  CB   . LEU   A 1 153 ? 16.71000 -0.84500  33.66000 1.000 18.55405  ?  305 LEU   A CB   1 
ATOM   1028 C  CG   . LEU   A 1 153 ? 16.68600 -0.59300  32.14300 1.000 16.93345  ?  305 LEU   A CG   1 
ATOM   1029 C  CD1  . LEU   A 1 153 ? 17.63000 -1.53800  31.42000 1.000 16.67396  ?  305 LEU   A CD1  1 
ATOM   1030 C  CD2  . LEU   A 1 153 ? 15.27300 -0.72500  31.58700 1.000 16.12748  ?  305 LEU   A CD2  1 
ATOM   1031 N  N    . ILE   A 1 154 ? 17.98300 1.82700   34.75700 1.000 22.80823  ?  306 ILE   A N    1 
ATOM   1032 C  CA   . ILE   A 1 154 ? 18.19000 3.19900   34.30100 1.000 23.62724  ?  306 ILE   A CA   1 
ATOM   1033 C  C    . ILE   A 1 154 ? 19.63100 3.64700   34.53300 1.000 24.07645  ?  306 ILE   A C    1 
ATOM   1034 O  O    . ILE   A 1 154 ? 20.24300 4.27700   33.65900 1.000 21.77941  ?  306 ILE   A O    1 
ATOM   1035 C  CB   . ILE   A 1 154 ? 17.18100 4.14200   34.97300 1.000 24.51729  ?  306 ILE   A CB   1 
ATOM   1036 C  CG1  . ILE   A 1 154 ? 15.76100 3.84300   34.47000 1.000 23.82321  ?  306 ILE   A CG1  1 
ATOM   1037 C  CG2  . ILE   A 1 154 ? 17.53600 5.58900   34.68200 1.000 25.34055  ?  306 ILE   A CG2  1 
ATOM   1038 C  CD1  . ILE   A 1 154 ? 14.70400 4.56600   35.25300 1.000 25.25236  ?  306 ILE   A CD1  1 
ATOM   1039 N  N    A GLU   A 1 155 ? 20.18900 3.35100   35.71200 0.510 26.79685  ?  307 GLU   A N    1 
ATOM   1040 N  N    B GLU   A 1 155 ? 20.19100 3.34500   35.70500 0.490 26.79160  ?  307 GLU   A N    1 
ATOM   1041 C  CA   A GLU   A 1 155 ? 21.57700 3.72700   35.98100 0.510 27.94561  ?  307 GLU   A CA   1 
ATOM   1042 C  CA   B GLU   A 1 155 ? 21.57500 3.73700   35.97400 0.490 27.94224  ?  307 GLU   A CA   1 
ATOM   1043 C  C    A GLU   A 1 155 ? 22.54500 3.10900   34.98500 0.510 27.10478  ?  307 GLU   A C    1 
ATOM   1044 C  C    B GLU   A 1 155 ? 22.55700 3.10900   34.99500 0.490 27.12629  ?  307 GLU   A C    1 
ATOM   1045 O  O    A GLU   A 1 155 ? 23.32900 3.85900   34.37800 0.510 27.39471  ?  307 GLU   A O    1 
ATOM   1046 O  O    B GLU   A 1 155 ? 23.36400 3.85200   34.41000 0.490 27.40859  ?  307 GLU   A O    1 
ATOM   1047 C  CB   A GLU   A 1 155 ? 21.95900 3.37000   37.42500 0.510 30.17616  ?  307 GLU   A CB   1 
ATOM   1048 C  CB   B GLU   A 1 155 ? 21.94000 3.41500   37.42900 0.490 30.19655  ?  307 GLU   A CB   1 
ATOM   1049 C  CG   A GLU   A 1 155 ? 23.32900 3.90800   37.84800 0.510 32.50128  ?  307 GLU   A CG   1 
ATOM   1050 C  CG   B GLU   A 1 155 ? 23.40900 3.65900   37.76700 0.490 32.42457  ?  307 GLU   A CG   1 
ATOM   1051 C  CD   A GLU   A 1 155 ? 24.32300 2.82000   38.24600 0.510 33.53589  ?  307 GLU   A CD   1 
ATOM   1052 C  CD   B GLU   A 1 155 ? 23.59500 4.72300   38.83600 0.490 34.04694  ?  307 GLU   A CD   1 
ATOM   1053 O  OE1  A GLU   A 1 155 ? 24.15200 1.64800   37.85100 0.510 33.56371  ?  307 GLU   A OE1  1 
ATOM   1054 O  OE1  B GLU   A 1 155 ? 22.61500 5.02600   39.54800 0.490 35.12368  ?  307 GLU   A OE1  1 
ATOM   1055 O  OE2  A GLU   A 1 155 ? 25.29000 3.14500   38.96100 0.510 35.21584  ?  307 GLU   A OE2  1 
ATOM   1056 O  OE2  B GLU   A 1 155 ? 24.71600 5.25800   38.96100 0.490 34.55645  ?  307 GLU   A OE2  1 
ATOM   1057 N  N    . PRO   A 1 156 ? 22.56200 1.79100   34.76000 1.000 26.84901  ?  308 PRO   A N    1 
ATOM   1058 C  CA   . PRO   A 1 156 ? 23.46400 1.25500   33.72600 1.000 26.22467  ?  308 PRO   A CA   1 
ATOM   1059 C  C    . PRO   A 1 156 ? 23.15100 1.77800   32.33200 1.000 25.33405  ?  308 PRO   A C    1 
ATOM   1060 O  O    . PRO   A 1 156 ? 24.06400 1.87600   31.50200 1.000 25.36835  ?  308 PRO   A O    1 
ATOM   1061 C  CB   . PRO   A 1 156 ? 23.25200 -0.26500  33.81600 1.000 28.41779  ?  308 PRO   A CB   1 
ATOM   1062 C  CG   . PRO   A 1 156 ? 22.65300 -0.49600  35.16700 1.000 30.55214  ?  308 PRO   A CG   1 
ATOM   1063 C  CD   . PRO   A 1 156 ? 21.79700 0.70400   35.40400 1.000 28.25301  ?  308 PRO   A CD   1 
ATOM   1064 N  N    . LEU   A 1 157 ? 21.88700 2.11900   32.04700 1.000 22.95615  ?  309 LEU   A N    1 
ATOM   1065 C  CA   . LEU   A 1 157 ? 21.55900 2.67700   30.73800 1.000 20.39398  ?  309 LEU   A CA   1 
ATOM   1066 C  C    . LEU   A 1 157 ? 22.22300 4.03600   30.54000 1.000 20.58695  ?  309 LEU   A C    1 
ATOM   1067 O  O    . LEU   A 1 157 ? 22.79600 4.31000   29.47500 1.000 19.55084  ?  309 LEU   A O    1 
ATOM   1068 C  CB   . LEU   A 1 157 ? 20.03400 2.78100   30.57800 1.000 20.00531  ?  309 LEU   A CB   1 
ATOM   1069 C  CG   . LEU   A 1 157 ? 19.55900 3.43400   29.27500 1.000 19.48449  ?  309 LEU   A CG   1 
ATOM   1070 C  CD1  . LEU   A 1 157 ? 20.08500 2.64100   28.09800 1.000 19.76588  ?  309 LEU   A CD1  1 
ATOM   1071 C  CD2  . LEU   A 1 157 ? 18.02600 3.52500   29.22000 1.000 19.48501  ?  309 LEU   A CD2  1 
ATOM   1072 N  N    . ILE   A 1 158 ? 22.15900 4.90200   31.55400 1.000 21.52486  ?  310 ILE   A N    1 
ATOM   1073 C  CA   . ILE   A 1 158 ? 22.83400 6.19600   31.46600 1.000 23.21221  ?  310 ILE   A CA   1 
ATOM   1074 C  C    . ILE   A 1 158 ? 24.34400 6.00700   31.34500 1.000 24.36968  ?  310 ILE   A C    1 
ATOM   1075 O  O    . ILE   A 1 158 ? 25.00600 6.68100   30.54600 1.000 25.39373  ?  310 ILE   A O    1 
ATOM   1076 C  CB   . ILE   A 1 158 ? 22.47500 7.07700   32.67700 1.000 25.06127  ?  310 ILE   A CB   1 
ATOM   1077 C  CG1  . ILE   A 1 158 ? 20.98700 7.44600   32.64900 1.000 26.27759  ?  310 ILE   A CG1  1 
ATOM   1078 C  CG2  . ILE   A 1 158 ? 23.37000 8.32700   32.72100 1.000 25.38690  ?  310 ILE   A CG2  1 
ATOM   1079 C  CD1  . ILE   A 1 158 ? 20.64500 8.48100   31.60000 1.000 27.66784  ?  310 ILE   A CD1  1 
ATOM   1080 N  N    . LYS   A 1 159 ? 24.91200 5.09000   32.13000 1.000 24.19171  ?  311 LYS   A N    1 
ATOM   1081 C  CA   . LYS   A 1 159 ? 26.34800 4.82600   32.01700 1.000 24.24425  ?  311 LYS   A CA   1 
ATOM   1082 C  C    . LYS   A 1 159 ? 26.70900 4.37600   30.60900 1.000 21.98351  ?  311 LYS   A C    1 
ATOM   1083 O  O    . LYS   A 1 159 ? 27.72400 4.80800   30.05300 1.000 21.34845  ?  311 LYS   A O    1 
ATOM   1084 C  CB   . LYS   A 1 159 ? 26.77900 3.77400   33.03600 1.000 27.42776  ?  311 LYS   A CB   1 
ATOM   1085 C  CG   . LYS   A 1 159 ? 27.04600 4.32200   34.42900 1.000 32.74959  ?  311 LYS   A CG   1 
ATOM   1086 C  CD   . LYS   A 1 159 ? 27.41800 3.20200   35.39300 1.000 37.44913  ?  311 LYS   A CD   1 
ATOM   1087 C  CE   . LYS   A 1 159 ? 27.58900 3.72500   36.81400 1.000 42.51998  ?  311 LYS   A CE   1 
ATOM   1088 N  NZ   . LYS   A 1 159 ? 27.15300 5.14700   36.92600 1.000 44.84991  ?  311 LYS   A NZ   1 
ATOM   1089 N  N    . PHE   A 1 160 ? 25.88100 3.51200   30.01500 1.000 20.78412  ?  312 PHE   A N    1 
ATOM   1090 C  CA   . PHE   A 1 160 ? 26.09400 3.09500   28.63300 1.000 20.86435  ?  312 PHE   A CA   1 
ATOM   1091 C  C    . PHE   A 1 160 ? 26.07900 4.29400   27.69300 1.000 22.33636  ?  312 PHE   A C    1 
ATOM   1092 O  O    . PHE   A 1 160 ? 26.99400 4.46900   26.87900 1.000 23.96876  ?  312 PHE   A O    1 
ATOM   1093 C  CB   . PHE   A 1 160 ? 25.02800 2.07100   28.23300 1.000 21.40199  ?  312 PHE   A CB   1 
ATOM   1094 C  CG   . PHE   A 1 160 ? 25.03800 1.71100   26.77100 1.000 21.70173  ?  312 PHE   A CG   1 
ATOM   1095 C  CD1  . PHE   A 1 160 ? 25.92700 0.76000   26.28600 1.000 22.73758  ?  312 PHE   A CD1  1 
ATOM   1096 C  CD2  . PHE   A 1 160 ? 24.15100 2.31300   25.88600 1.000 21.38787  ?  312 PHE   A CD2  1 
ATOM   1097 C  CE1  . PHE   A 1 160 ? 25.93900 0.42200   24.93700 1.000 22.29701  ?  312 PHE   A CE1  1 
ATOM   1098 C  CE2  . PHE   A 1 160 ? 24.15700 1.98100   24.53800 1.000 21.61246  ?  312 PHE   A CE2  1 
ATOM   1099 C  CZ   . PHE   A 1 160 ? 25.05900 1.03800   24.06500 1.000 20.23342  ?  312 PHE   A CZ   1 
ATOM   1100 N  N    . GLN   A 1 161 ? 25.03700 5.12900   27.78400 1.000 21.94753  ?  313 GLN   A N    1 
ATOM   1101 C  CA   . GLN   A 1 161 ? 24.92500 6.27800   26.88700 1.000 22.07256  ?  313 GLN   A CA   1 
ATOM   1102 C  C    . GLN   A 1 161 ? 26.12900 7.20400   27.02600 1.000 23.30887  ?  313 GLN   A C    1 
ATOM   1103 O  O    . GLN   A 1 161 ? 26.62500 7.75000   26.03500 1.000 24.58746  ?  313 GLN   A O    1 
ATOM   1104 C  CB   . GLN   A 1 161 ? 23.62700 7.04500   27.16400 1.000 20.54331  ?  313 GLN   A CB   1 
ATOM   1105 C  CG   . GLN   A 1 161 ? 22.32800 6.26000   26.90000 1.000 20.71409  ?  313 GLN   A CG   1 
ATOM   1106 C  CD   . GLN   A 1 161 ? 22.16000 5.87200   25.44400 1.000 20.17223  ?  313 GLN   A CD   1 
ATOM   1107 O  OE1  . GLN   A 1 161 ? 22.67000 6.54300   24.55300 1.000 22.56915  ?  313 GLN   A OE1  1 
ATOM   1108 N  NE2  . GLN   A 1 161 ? 21.45800 4.77400   25.19700 1.000 17.84952  ?  313 GLN   A NE2  1 
ATOM   1109 N  N    . VAL   A 1 162 ? 26.61500 7.38900   28.25100 1.000 22.52605  ?  314 VAL   A N    1 
ATOM   1110 C  CA   . VAL   A 1 162 ? 27.77200 8.25000   28.47200 1.000 21.59318  ?  314 VAL   A CA   1 
ATOM   1111 C  C    . VAL   A 1 162 ? 29.01200 7.65400   27.81600 1.000 22.17879  ?  314 VAL   A C    1 
ATOM   1112 O  O    . VAL   A 1 162 ? 29.75000 8.34200   27.10200 1.000 22.70643  ?  314 VAL   A O    1 
ATOM   1113 C  CB   . VAL   A 1 162 ? 27.97200 8.48200   29.97800 1.000 20.51728  ?  314 VAL   A CB   1 
ATOM   1114 C  CG1  . VAL   A 1 162 ? 29.34900 9.10900   30.26300 1.000 20.06169  ?  314 VAL   A CG1  1 
ATOM   1115 C  CG2  . VAL   A 1 162 ? 26.82800 9.33700   30.53400 1.000 17.43250  ?  314 VAL   A CG2  1 
ATOM   1116 N  N    . GLY   A 1 163 ? 29.24600 6.35700   28.02300 1.000 21.68076  ?  315 GLY   A N    1 
ATOM   1117 C  CA   . GLY   A 1 163 ? 30.44300 5.73900   27.48000 1.000 19.33774  ?  315 GLY   A CA   1 
ATOM   1118 C  C    . GLY   A 1 163 ? 30.41400 5.61800   25.97200 1.000 19.40855  ?  315 GLY   A C    1 
ATOM   1119 O  O    . GLY   A 1 163 ? 31.45700 5.70200   25.32200 1.000 16.90145  ?  315 GLY   A O    1 
ATOM   1120 N  N    . LEU   A 1 164 ? 29.23100 5.40000   25.39400 1.000 18.63188  ?  316 LEU   A N    1 
ATOM   1121 C  CA   . LEU   A 1 164 ? 29.12000 5.38200   23.94000 1.000 19.91521  ?  316 LEU   A CA   1 
ATOM   1122 C  C    . LEU   A 1 164 ? 29.37200 6.76700   23.36500 1.000 22.82976  ?  316 LEU   A C    1 
ATOM   1123 O  O    . LEU   A 1 164 ? 30.13100 6.92600   22.40000 1.000 24.23708  ?  316 LEU   A O    1 
ATOM   1124 C  CB   . LEU   A 1 164 ? 27.73400 4.87700   23.52800 1.000 18.77066  ?  316 LEU   A CB   1 
ATOM   1125 C  CG   . LEU   A 1 164 ? 27.48300 4.67500   22.03400 1.000 20.13698  ?  316 LEU   A CG   1 
ATOM   1126 C  CD1  . LEU   A 1 164 ? 28.49100 3.69600   21.46900 1.000 20.73663  ?  316 LEU   A CD1  1 
ATOM   1127 C  CD2  . LEU   A 1 164 ? 26.05100 4.16500   21.81700 1.000 18.88578  ?  316 LEU   A CD2  1 
ATOM   1128 N  N    . LYS   A 1 165 ? 28.74500 7.78700   23.95800 1.000 23.83428  ?  317 LYS   A N    1 
ATOM   1129 C  CA   . LYS   A 1 165 ? 28.92300 9.14900   23.47100 1.000 25.56979  ?  317 LYS   A CA   1 
ATOM   1130 C  C    . LYS   A 1 165 ? 30.39100 9.55800   23.51600 1.000 26.85907  ?  317 LYS   A C    1 
ATOM   1131 O  O    . LYS   A 1 165 ? 30.89200 10.22000  22.59700 1.000 29.48265  ?  317 LYS   A O    1 
ATOM   1132 C  CB   . LYS   A 1 165 ? 28.05400 10.10400  24.29200 1.000 25.51835  ?  317 LYS   A CB   1 
ATOM   1133 C  CG   . LYS   A 1 165 ? 27.61600 11.35100  23.55200 1.000 26.65115  ?  317 LYS   A CG   1 
ATOM   1134 C  CD   . LYS   A 1 165 ? 26.35700 11.11600  22.72800 1.000 26.41513  ?  317 LYS   A CD   1 
ATOM   1135 C  CE   . LYS   A 1 165 ? 25.95800 12.39100  22.01600 1.000 27.55770  ?  317 LYS   A CE   1 
ATOM   1136 N  NZ   . LYS   A 1 165 ? 24.88000 12.16700  21.02500 1.000 25.41092  ?  317 LYS   A NZ   1 
ATOM   1137 N  N    . LYS   A 1 166 ? 31.10500 9.14000   24.56100 1.000 26.57532  ?  318 LYS   A N    1 
ATOM   1138 C  CA   . LYS   A 1 166 ? 32.51600 9.48200   24.68900 1.000 27.36619  ?  318 LYS   A CA   1 
ATOM   1139 C  C    . LYS   A 1 166 ? 33.36500 8.84300   23.60200 1.000 27.90154  ?  318 LYS   A C    1 
ATOM   1140 O  O    . LYS   A 1 166 ? 34.45200 9.34600   23.31100 1.000 27.80641  ?  318 LYS   A O    1 
ATOM   1141 C  CB   . LYS   A 1 166 ? 33.03600 9.06600   26.06000 1.000 29.04863  ?  318 LYS   A CB   1 
ATOM   1142 C  CG   . LYS   A 1 166 ? 32.54900 9.94900   27.21100 1.000 31.31347  ?  318 LYS   A CG   1 
ATOM   1143 C  CD   . LYS   A 1 166 ? 33.08100 9.43200   28.53900 1.000 32.76816  ?  318 LYS   A CD   1 
ATOM   1144 C  CE   . LYS   A 1 166 ? 32.72900 10.35700  29.68900 1.000 35.28048  ?  318 LYS   A CE   1 
ATOM   1145 N  NZ   . LYS   A 1 166 ? 33.20300 9.79700   30.99100 1.000 37.13665  ?  318 LYS   A NZ   1 
ATOM   1146 N  N    . LEU   A 1 167 ? 32.89700 7.75700   22.98400 1.000 27.07500  ?  319 LEU   A N    1 
ATOM   1147 C  CA   . LEU   A 1 167 ? 33.66100 7.17400   21.88900 1.000 25.69038  ?  319 LEU   A CA   1 
ATOM   1148 C  C    . LEU   A 1 167 ? 33.71100 8.09200   20.67700 1.000 25.98316  ?  319 LEU   A C    1 
ATOM   1149 O  O    . LEU   A 1 167 ? 34.61300 7.94100   19.84300 1.000 27.46623  ?  319 LEU   A O    1 
ATOM   1150 C  CB   . LEU   A 1 167 ? 33.07700 5.81400   21.49500 1.000 23.55213  ?  319 LEU   A CB   1 
ATOM   1151 C  CG   . LEU   A 1 167 ? 33.25500 4.68900   22.51500 1.000 23.66902  ?  319 LEU   A CG   1 
ATOM   1152 C  CD1  . LEU   A 1 167 ? 32.77400 3.37300   21.93500 1.000 24.56165  ?  319 LEU   A CD1  1 
ATOM   1153 C  CD2  . LEU   A 1 167 ? 34.73800 4.59000   22.97100 1.000 21.99621  ?  319 LEU   A CD2  1 
ATOM   1154 N  N    A ASN   A 1 168 ? 32.78400 9.04200   20.57700 0.470 25.42220  ?  320 ASN   A N    1 
ATOM   1155 N  N    B ASN   A 1 168 ? 32.77700 9.03700   20.57100 0.530 25.37892  ?  320 ASN   A N    1 
ATOM   1156 C  CA   A ASN   A 1 168 ? 32.66600 9.95500   19.44000 0.470 26.34591  ?  320 ASN   A CA   1 
ATOM   1157 C  CA   B ASN   A 1 168 ? 32.69900 9.95800   19.43900 0.530 26.35695  ?  320 ASN   A CA   1 
ATOM   1158 C  C    A ASN   A 1 168 ? 32.79500 9.19600   18.12000 0.470 26.64503  ?  320 ASN   A C    1 
ATOM   1159 C  C    B ASN   A 1 168 ? 32.79200 9.20100   18.11500 0.530 26.67541  ?  320 ASN   A C    1 
ATOM   1160 O  O    A ASN   A 1 168 ? 33.64500 9.48100   17.27500 0.470 27.74964  ?  320 ASN   A O    1 
ATOM   1161 O  O    B ASN   A 1 168 ? 33.62700 9.49300   17.25500 0.530 27.78627  ?  320 ASN   A O    1 
ATOM   1162 C  CB   A ASN   A 1 168 ? 33.68600 11.09100  19.52700 0.470 27.68505  ?  320 ASN   A CB   1 
ATOM   1163 C  CB   B ASN   A 1 168 ? 33.77700 11.04100  19.53800 0.530 27.71333  ?  320 ASN   A CB   1 
ATOM   1164 C  CG   A ASN   A 1 168 ? 33.27900 12.30200  18.70000 0.470 28.56922  ?  320 ASN   A CG   1 
ATOM   1165 C  CG   B ASN   A 1 168 ? 33.80900 11.71100  20.90100 0.530 28.98640  ?  320 ASN   A CG   1 
ATOM   1166 O  OD1  A ASN   A 1 168 ? 32.16400 12.36500  18.17900 0.470 29.24854  ?  320 ASN   A OD1  1 
ATOM   1167 O  OD1  B ASN   A 1 168 ? 32.83800 12.33900  21.31800 0.530 29.88468  ?  320 ASN   A OD1  1 
ATOM   1168 N  ND2  A ASN   A 1 168 ? 34.18500 13.26800  18.57100 0.470 29.56008  ?  320 ASN   A ND2  1 
ATOM   1169 N  ND2  B ASN   A 1 168 ? 34.93100 11.57400  21.60300 0.530 30.63673  ?  320 ASN   A ND2  1 
ATOM   1170 N  N    . LEU   A 1 169 ? 31.93300 8.19400   17.97200 1.000 24.41788  ?  321 LEU   A N    1 
ATOM   1171 C  CA   . LEU   A 1 169 ? 31.94300 7.36700   16.77600 1.000 24.04708  ?  321 LEU   A CA   1 
ATOM   1172 C  C    . LEU   A 1 169 ? 31.69100 8.20500   15.53300 1.000 24.38876  ?  321 LEU   A C    1 
ATOM   1173 O  O    . LEU   A 1 169 ? 30.90000 9.14900   15.55000 1.000 23.63644  ?  321 LEU   A O    1 
ATOM   1174 C  CB   . LEU   A 1 169 ? 30.87200 6.27500   16.87100 1.000 22.36902  ?  321 LEU   A CB   1 
ATOM   1175 C  CG   . LEU   A 1 169 ? 31.01900 5.27000   18.01000 1.000 22.41009  ?  321 LEU   A CG   1 
ATOM   1176 C  CD1  . LEU   A 1 169 ? 30.04100 4.12100   17.83500 1.000 21.31645  ?  321 LEU   A CD1  1 
ATOM   1177 C  CD2  . LEU   A 1 169 ? 32.45000 4.76100   18.06500 1.000 22.03920  ?  321 LEU   A CD2  1 
ATOM   1178 N  N    . HIS   A 1 170 ? 32.39400 7.86500   14.45600 1.000 24.17109  ?  322 HIS   A N    1 
ATOM   1179 C  CA   . HIS   A 1 170 ? 31.95000 8.28000   13.13700 1.000 23.43133  ?  322 HIS   A CA   1 
ATOM   1180 C  C    . HIS   A 1 170 ? 30.58200 7.67000   12.86000 1.000 25.03595  ?  322 HIS   A C    1 
ATOM   1181 O  O    . HIS   A 1 170 ? 30.26300 6.57700   13.33200 1.000 26.02958  ?  322 HIS   A O    1 
ATOM   1182 C  CB   . HIS   A 1 170 ? 32.93600 7.82100   12.06600 1.000 21.74144  ?  322 HIS   A CB   1 
ATOM   1183 C  CG   . HIS   A 1 170 ? 34.29500 8.44200   12.18400 1.000 23.88660  ?  322 HIS   A CG   1 
ATOM   1184 N  ND1  . HIS   A 1 170 ? 35.32100 8.15000   11.31100 1.000 24.74462  ?  322 HIS   A ND1  1 
ATOM   1185 C  CD2  . HIS   A 1 170 ? 34.79700 9.33400   13.07100 1.000 23.96127  ?  322 HIS   A CD2  1 
ATOM   1186 C  CE1  . HIS   A 1 170 ? 36.39500 8.84300   11.65000 1.000 24.95607  ?  322 HIS   A CE1  1 
ATOM   1187 N  NE2  . HIS   A 1 170 ? 36.10100 9.57300   12.71100 1.000 25.10512  ?  322 HIS   A NE2  1 
ATOM   1188 N  N    . GLU   A 1 171 ? 29.77100 8.37200   12.07300 1.000 24.95942  ?  323 GLU   A N    1 
ATOM   1189 C  CA   . GLU   A 1 171 ? 28.49500 7.78500   11.67700 1.000 26.93659  ?  323 GLU   A CA   1 
ATOM   1190 C  C    . GLU   A 1 171 ? 28.71100 6.42900   11.01000 1.000 25.82977  ?  323 GLU   A C    1 
ATOM   1191 O  O    . GLU   A 1 171 ? 27.94000 5.49000   11.23000 1.000 24.70342  ?  323 GLU   A O    1 
ATOM   1192 C  CB   . GLU   A 1 171 ? 27.74800 8.74600   10.76000 1.000 30.50180  ?  323 GLU   A CB   1 
ATOM   1193 C  CG   . GLU   A 1 171 ? 26.30500 8.37800   10.51500 1.000 34.29548  ?  323 GLU   A CG   1 
ATOM   1194 C  CD   . GLU   A 1 171 ? 25.56100 9.47900   9.79500  1.000 37.40886  ?  323 GLU   A CD   1 
ATOM   1195 O  OE1  . GLU   A 1 171 ? 26.18100 10.16300  8.95100  1.000 39.22182  ?  323 GLU   A OE1  1 
ATOM   1196 O  OE2  . GLU   A 1 171 ? 24.36200 9.66500   10.07700 1.000 38.02533  ?  323 GLU   A OE2  1 
ATOM   1197 N  N    . GLU   A 1 172 ? 29.79200 6.29500   10.23500 1.000 24.87873  ?  324 GLU   A N    1 
ATOM   1198 C  CA   . GLU   A 1 172 ? 30.13600 4.99800   9.65600  1.000 24.97307  ?  324 GLU   A CA   1 
ATOM   1199 C  C    . GLU   A 1 172 ? 30.27900 3.92200   10.73000 1.000 23.41687  ?  324 GLU   A C    1 
ATOM   1200 O  O    . GLU   A 1 172 ? 29.80700 2.79100   10.55900 1.000 23.15722  ?  324 GLU   A O    1 
ATOM   1201 C  CB   . GLU   A 1 172 ? 31.43500 5.10900   8.85400  1.000 25.82704  ?  324 GLU   A CB   1 
ATOM   1202 C  CG   . GLU   A 1 172 ? 31.34800 5.91800   7.57300  1.000 28.19855  ?  324 GLU   A CG   1 
ATOM   1203 C  CD   . GLU   A 1 172 ? 31.42200 7.42100   7.79100  1.000 31.16117  ?  324 GLU   A CD   1 
ATOM   1204 O  OE1  . GLU   A 1 172 ? 31.66000 8.13900   6.80000  1.000 33.42579  ?  324 GLU   A OE1  1 
ATOM   1205 O  OE2  . GLU   A 1 172 ? 31.24200 7.89000   8.93300  1.000 31.26022  ?  324 GLU   A OE2  1 
ATOM   1206 N  N    . GLU   A 1 173 ? 30.93400 4.25000   11.84400 1.000 21.79929  ?  325 GLU   A N    1 
ATOM   1207 C  CA   . GLU   A 1 173 ? 31.10500 3.25800   12.89700 1.000 19.78732  ?  325 GLU   A CA   1 
ATOM   1208 C  C    . GLU   A 1 173 ? 29.78600 2.99400   13.61500 1.000 18.08545  ?  325 GLU   A C    1 
ATOM   1209 O  O    . GLU   A 1 173 ? 29.50200 1.85700   14.00500 1.000 17.58986  ?  325 GLU   A O    1 
ATOM   1210 C  CB   . GLU   A 1 173 ? 32.18900 3.72300   13.87700 1.000 19.92005  ?  325 GLU   A CB   1 
ATOM   1211 C  CG   . GLU   A 1 173 ? 33.60000 3.65400   13.27200 1.000 20.64490  ?  325 GLU   A CG   1 
ATOM   1212 C  CD   . GLU   A 1 173 ? 34.54400 4.71700   13.80000 1.000 24.30167  ?  325 GLU   A CD   1 
ATOM   1213 O  OE1  . GLU   A 1 173 ? 35.71900 4.70800   13.37300 1.000 27.36861  ?  325 GLU   A OE1  1 
ATOM   1214 O  OE2  . GLU   A 1 173 ? 34.13200 5.54000   14.64600 1.000 24.98587  ?  325 GLU   A OE2  1 
ATOM   1215 N  N    . HIS   A 1 174 ? 28.97600 4.03700   13.79200 1.000 18.81291  ?  326 HIS   A N    1 
ATOM   1216 C  CA   . HIS   A 1 174 ? 27.68700 3.90100   14.47000 1.000 21.27029  ?  326 HIS   A CA   1 
ATOM   1217 C  C    . HIS   A 1 174 ? 26.75900 2.93800   13.72800 1.000 20.61347  ?  326 HIS   A C    1 
ATOM   1218 O  O    . HIS   A 1 174 ? 26.12000 2.06800   14.34100 1.000 17.86042  ?  326 HIS   A O    1 
ATOM   1219 C  CB   . HIS   A 1 174 ? 27.05800 5.29200   14.60300 1.000 23.44611  ?  326 HIS   A CB   1 
ATOM   1220 C  CG   . HIS   A 1 174 ? 25.74500 5.31600   15.31600 1.000 24.26932  ?  326 HIS   A CG   1 
ATOM   1221 N  ND1  . HIS   A 1 174 ? 25.64200 5.31400   16.69300 1.000 24.09212  ?  326 HIS   A ND1  1 
ATOM   1222 C  CD2  . HIS   A 1 174 ? 24.47800 5.39000   14.84400 1.000 22.77627  ?  326 HIS   A CD2  1 
ATOM   1223 C  CE1  . HIS   A 1 174 ? 24.36700 5.35800   17.03600 1.000 23.13773  ?  326 HIS   A CE1  1 
ATOM   1224 N  NE2  . HIS   A 1 174 ? 23.64000 5.40900   15.93400 1.000 23.50055  ?  326 HIS   A NE2  1 
ATOM   1225 N  N    . VAL   A 1 175 ? 26.65500 3.07800   12.40400 1.000 20.38470  ?  327 VAL   A N    1 
ATOM   1226 C  CA   . VAL   A 1 175 ? 25.70400 2.21700   11.69700 1.000 17.92699  ?  327 VAL   A CA   1 
ATOM   1227 C  C    . VAL   A 1 175 ? 26.25900 0.80500   11.54700 1.000 16.88263  ?  327 VAL   A C    1 
ATOM   1228 O  O    . VAL   A 1 175 ? 25.49400 -0.16300  11.55500 1.000 18.68043  ?  327 VAL   A O    1 
ATOM   1229 C  CB   . VAL   A 1 175 ? 25.28900 2.81600   10.33600 1.000 19.02693  ?  327 VAL   A CB   1 
ATOM   1230 C  CG1  . VAL   A 1 175 ? 24.64300 4.17800   10.53700 1.000 17.10057  ?  327 VAL   A CG1  1 
ATOM   1231 C  CG2  . VAL   A 1 175 ? 26.48200 2.91900   9.37700  1.000 20.19371  ?  327 VAL   A CG2  1 
ATOM   1232 N  N    . LEU   A 1 176 ? 27.58200 0.64800   11.45000 1.000 17.52656  ?  328 LEU   A N    1 
ATOM   1233 C  CA   . LEU   A 1 176 ? 28.15100 -0.69800  11.45400 1.000 19.13866  ?  328 LEU   A CA   1 
ATOM   1234 C  C    . LEU   A 1 176 ? 27.87300 -1.41300  12.77400 1.000 19.07552  ?  328 LEU   A C    1 
ATOM   1235 O  O    . LEU   A 1 176 ? 27.57000 -2.61200  12.78800 1.000 20.51260  ?  328 LEU   A O    1 
ATOM   1236 C  CB   . LEU   A 1 176 ? 29.65700 -0.63800  11.19300 1.000 20.02278  ?  328 LEU   A CB   1 
ATOM   1237 C  CG   . LEU   A 1 176 ? 30.08800 -0.58600  9.72100  1.000 22.87002  ?  328 LEU   A CG   1 
ATOM   1238 C  CD1  . LEU   A 1 176 ? 31.52700 -0.11300  9.61600  1.000 21.99603  ?  328 LEU   A CD1  1 
ATOM   1239 C  CD2  . LEU   A 1 176 ? 29.89900 -1.93800  9.01100  1.000 22.83381  ?  328 LEU   A CD2  1 
ATOM   1240 N  N    . LEU   A 1 177 ? 27.99200 -0.70000  13.89700 1.000 18.30113  ?  329 LEU   A N    1 
ATOM   1241 C  CA   . LEU   A 1 177 ? 27.72100 -1.31500  15.19700 1.000 18.29328  ?  329 LEU   A CA   1 
ATOM   1242 C  C    . LEU   A 1 177 ? 26.26400 -1.75400  15.30400 1.000 18.53529  ?  329 LEU   A C    1 
ATOM   1243 O  O    . LEU   A 1 177 ? 25.96700 -2.85000  15.80300 1.000 18.21208  ?  329 LEU   A O    1 
ATOM   1244 C  CB   . LEU   A 1 177 ? 28.06700 -0.33300  16.31400 1.000 18.34237  ?  329 LEU   A CB   1 
ATOM   1245 C  CG   . LEU   A 1 177 ? 28.09000 -0.87600  17.75000 1.000 18.26122  ?  329 LEU   A CG   1 
ATOM   1246 C  CD1  . LEU   A 1 177 ? 29.09800 -2.01900  17.89400 1.000 17.66023  ?  329 LEU   A CD1  1 
ATOM   1247 C  CD2  . LEU   A 1 177 ? 28.39300 0.25400   18.72900 1.000 18.67891  ?  329 LEU   A CD2  1 
ATOM   1248 N  N    A MET   A 1 178 ? 25.33800 -0.89600  14.86500 0.480 18.38204  ?  330 MET   A N    1 
ATOM   1249 N  N    B MET   A 1 178 ? 25.33900 -0.92600  14.83100 0.520 18.40185  ?  330 MET   A N    1 
ATOM   1250 C  CA   A MET   A 1 178 ? 23.93000 -1.28400  14.79900 0.480 18.27538  ?  330 MET   A CA   1 
ATOM   1251 C  CA   B MET   A 1 178 ? 23.93800 -1.33500  14.85400 0.520 18.25535  ?  330 MET   A CA   1 
ATOM   1252 C  C    A MET   A 1 178 ? 23.77100 -2.59400  14.04500 0.480 18.27380  ?  330 MET   A C    1 
ATOM   1253 C  C    B MET   A 1 178 ? 23.71700 -2.58700  14.01800 0.520 18.27988  ?  330 MET   A C    1 
ATOM   1254 O  O    A MET   A 1 178 ? 23.12900 -3.53500  14.52600 0.480 18.92092  ?  330 MET   A O    1 
ATOM   1255 O  O    B MET   A 1 178 ? 22.97800 -3.49100  14.42400 0.520 18.93604  ?  330 MET   A O    1 
ATOM   1256 C  CB   A MET   A 1 178 ? 23.10400 -0.19100  14.11400 0.480 18.47800  ?  330 MET   A CB   1 
ATOM   1257 C  CB   B MET   A 1 178 ? 23.05800 -0.19000  14.36800 0.520 18.49783  ?  330 MET   A CB   1 
ATOM   1258 C  CG   A MET   A 1 178 ? 22.99400 1.12200   14.86700 0.480 19.87174  ?  330 MET   A CG   1 
ATOM   1259 C  CG   B MET   A 1 178 ? 23.12100 1.00200   15.29300 0.520 19.41150  ?  330 MET   A CG   1 
ATOM   1260 S  SD   A MET   A 1 178 ? 22.49500 2.47300   13.76600 0.480 20.78680  ?  330 MET   A SD   1 
ATOM   1261 S  SD   B MET   A 1 178 ? 21.85400 2.20500   14.90700 0.520 21.12055  ?  330 MET   A SD   1 
ATOM   1262 C  CE   A MET   A 1 178 ? 20.89800 1.88200   13.21100 0.480 20.25215  ?  330 MET   A CE   1 
ATOM   1263 C  CE   B MET   A 1 178 ? 22.51700 2.96300   13.42500 0.520 20.91304  ?  330 MET   A CE   1 
ATOM   1264 N  N    . ALA   A 1 179 ? 24.36900 -2.67000  12.85700 1.000 17.20536  ?  331 ALA   A N    1 
ATOM   1265 C  CA   . ALA   A 1 179 ? 24.19900 -3.84500  12.01000 1.000 18.70616  ?  331 ALA   A CA   1 
ATOM   1266 C  C    . ALA   A 1 179 ? 24.85700 -5.07900  12.62000 1.000 19.37478  ?  331 ALA   A C    1 
ATOM   1267 O  O    . ALA   A 1 179 ? 24.28400 -6.17300  12.58000 1.000 19.05421  ?  331 ALA   A O    1 
ATOM   1268 C  CB   . ALA   A 1 179 ? 24.75000 -3.55700  10.61600 1.000 19.42180  ?  331 ALA   A CB   1 
ATOM   1269 N  N    . ILE   A 1 180 ? 26.06000 -4.92500  13.18900 1.000 17.55820  ?  332 ILE   A N    1 
ATOM   1270 C  CA   . ILE   A 1 180 ? 26.71400 -6.05000  13.85000 1.000 18.79522  ?  332 ILE   A CA   1 
ATOM   1271 C  C    . ILE   A 1 180 ? 25.87400 -6.52700  15.02500 1.000 20.54189  ?  332 ILE   A C    1 
ATOM   1272 O  O    . ILE   A 1 180 ? 25.71500 -7.73400  15.25100 1.000 23.23181  ?  332 ILE   A O    1 
ATOM   1273 C  CB   . ILE   A 1 180 ? 28.13900 -5.64700  14.28100 1.000 19.99978  ?  332 ILE   A CB   1 
ATOM   1274 C  CG1  . ILE   A 1 180 ? 29.01800 -5.48500  13.04100 1.000 19.27154  ?  332 ILE   A CG1  1 
ATOM   1275 C  CG2  . ILE   A 1 180 ? 28.73300 -6.67900  15.20500 1.000 20.98938  ?  332 ILE   A CG2  1 
ATOM   1276 C  CD1  . ILE   A 1 180 ? 30.30200 -4.63400  13.27300 1.000 16.29987  ?  332 ILE   A CD1  1 
ATOM   1277 N  N    . CYS   A 1 181 ? 25.30300 -5.58300  15.77600 1.000 20.41439  ?  333 CYS   A N    1 
ATOM   1278 C  CA   . CYS   A 1 181 ? 24.39000 -5.93600  16.86400 1.000 22.70924  ?  333 CYS   A CA   1 
ATOM   1279 C  C    . CYS   A 1 181 ? 23.22800 -6.79700  16.37300 1.000 23.91857  ?  333 CYS   A C    1 
ATOM   1280 O  O    . CYS   A 1 181 ? 22.85900 -7.78600  17.02000 1.000 25.03441  ?  333 CYS   A O    1 
ATOM   1281 C  CB   . CYS   A 1 181 ? 23.85700 -4.66800  17.53700 1.000 21.43710  ?  333 CYS   A CB   1 
ATOM   1282 S  SG   . CYS   A 1 181 ? 22.72900 -4.97700  18.91600 1.000 20.51966  ?  333 CYS   A SG   1 
ATOM   1283 N  N    . ILE   A 1 182 ? 22.65000 -6.45100  15.22700 1.000 23.84839  ?  334 ILE   A N    1 
ATOM   1284 C  CA   . ILE   A 1 182 ? 21.47800 -7.17200  14.74000 1.000 23.39767  ?  334 ILE   A CA   1 
ATOM   1285 C  C    . ILE   A 1 182 ? 21.85600 -8.58500  14.29100 1.000 24.35186  ?  334 ILE   A C    1 
ATOM   1286 O  O    . ILE   A 1 182 ? 21.18900 -9.56700  14.64000 1.000 23.65743  ?  334 ILE   A O    1 
ATOM   1287 C  CB   . ILE   A 1 182 ? 20.80700 -6.37300  13.61000 1.000 22.56083  ?  334 ILE   A CB   1 
ATOM   1288 C  CG1  . ILE   A 1 182 ? 20.15800 -5.10700  14.17600 1.000 19.59500  ?  334 ILE   A CG1  1 
ATOM   1289 C  CG2  . ILE   A 1 182 ? 19.77100 -7.21500  12.88800 1.000 23.55624  ?  334 ILE   A CG2  1 
ATOM   1290 C  CD1  . ILE   A 1 182 ? 19.79200 -4.05300  13.12300 1.000 16.11225  ?  334 ILE   A CD1  1 
ATOM   1291 N  N    . VAL   A 1 183 ? 22.94200 -8.71400  13.52800 1.000 23.67362  ?  335 VAL   A N    1 
ATOM   1292 C  CA   . VAL   A 1 183 ? 23.31200 -10.01500 12.97400 1.000 25.57736  ?  335 VAL   A CA   1 
ATOM   1293 C  C    . VAL   A 1 183 ? 24.29500 -10.71900 13.90300 1.000 27.13267  ?  335 VAL   A C    1 
ATOM   1294 O  O    . VAL   A 1 183 ? 25.47800 -10.85000 13.58200 1.000 29.20727  ?  335 VAL   A O    1 
ATOM   1295 C  CB   . VAL   A 1 183 ? 23.88400 -9.86400  11.54900 1.000 28.36370  ?  335 VAL   A CB   1 
ATOM   1296 C  CG1  . VAL   A 1 183 ? 24.00000 -11.22000 10.87900 1.000 30.89452  ?  335 VAL   A CG1  1 
ATOM   1297 C  CG2  . VAL   A 1 183 ? 22.97500 -8.96600  10.71300 1.000 27.06482  ?  335 VAL   A CG2  1 
ATOM   1298 N  N    . SER   A 1 184 ? 23.81200 -11.17900 15.06300 1.000 27.82891  ?  336 SER   A N    1 
ATOM   1299 C  CA   . SER   A 1 184 ? 24.64400 -11.87600 16.03800 1.000 28.10283  ?  336 SER   A CA   1 
ATOM   1300 C  C    . SER   A 1 184 ? 24.33800 -13.36900 16.02500 1.000 27.29235  ?  336 SER   A C    1 
ATOM   1301 O  O    . SER   A 1 184 ? 23.16900 -13.75200 16.20800 1.000 26.66061  ?  336 SER   A O    1 
ATOM   1302 C  CB   . SER   A 1 184 ? 24.41700 -11.30300 17.43200 1.000 30.35753  ?  336 SER   A CB   1 
ATOM   1303 O  OG   . SER   A 1 184 ? 24.88500 -9.96200  17.52800 1.000 30.32891  ?  336 SER   A OG   1 
ATOM   1304 N  N    . PRO   A 1 185 ? 25.33900 -14.24800 15.84900 1.000 27.94698  ?  337 PRO   A N    1 
ATOM   1305 C  CA   . PRO   A 1 185 ? 25.03300 -15.68500 15.71800 1.000 28.56977  ?  337 PRO   A CA   1 
ATOM   1306 C  C    . PRO   A 1 185 ? 24.67300 -16.37900 17.02300 1.000 31.03215  ?  337 PRO   A C    1 
ATOM   1307 O  O    . PRO   A 1 185 ? 24.10200 -17.47800 16.98100 1.000 33.92426  ?  337 PRO   A O    1 
ATOM   1308 C  CB   . PRO   A 1 185 ? 26.32200 -16.26700 15.12000 1.000 30.26676  ?  337 PRO   A CB   1 
ATOM   1309 C  CG   . PRO   A 1 185 ? 27.41200 -15.32900 15.59800 1.000 29.65182  ?  337 PRO   A CG   1 
ATOM   1310 C  CD   . PRO   A 1 185 ? 26.77100 -13.95500 15.63200 1.000 27.58387  ?  337 PRO   A CD   1 
ATOM   1311 N  N    . ASP   A 1 186 ? 24.96400 -15.78800 18.17500 1.000 29.78799  ?  338 ASP   A N    1 
ATOM   1312 C  CA   . ASP   A 1 186 ? 24.70300 -16.45500 19.44100 1.000 31.78056  ?  338 ASP   A CA   1 
ATOM   1313 C  C    . ASP   A 1 186 ? 23.32500 -16.13900 20.00900 1.000 31.53488  ?  338 ASP   A C    1 
ATOM   1314 O  O    . ASP   A 1 186 ? 23.04900 -16.50600 21.15600 1.000 33.43460  ?  338 ASP   A O    1 
ATOM   1315 C  CB   . ASP   A 1 186 ? 25.77600 -16.08500 20.46800 1.000 31.03066  ?  338 ASP   A CB   1 
ATOM   1316 C  CG   . ASP   A 1 186 ? 25.82900 -14.59700 20.74000 1.000 32.10110  ?  338 ASP   A CG   1 
ATOM   1317 O  OD1  . ASP   A 1 186 ? 26.04700 -14.21800 21.90800 1.000 33.48815  ?  338 ASP   A OD1  1 
ATOM   1318 O  OD2  . ASP   A 1 186 ? 25.64900 -13.80700 19.79000 1.000 32.77342  ?  338 ASP   A OD2  1 
ATOM   1319 N  N    . ARG   A 1 187 ? 22.46700 -15.46700 19.25000 1.000 31.25134  ?  339 ARG   A N    1 
ATOM   1320 C  CA   . ARG   A 1 187 ? 21.13000 -15.17300 19.74500 1.000 32.40505  ?  339 ARG   A CA   1 
ATOM   1321 C  C    . ARG   A 1 187 ? 20.36000 -16.47500 19.96300 1.000 36.06619  ?  339 ARG   A C    1 
ATOM   1322 O  O    . ARG   A 1 187 ? 20.45500 -17.39600 19.14500 1.000 35.65875  ?  339 ARG   A O    1 
ATOM   1323 C  CB   . ARG   A 1 187 ? 20.36600 -14.27500 18.76700 1.000 29.88611  ?  339 ARG   A CB   1 
ATOM   1324 C  CG   . ARG   A 1 187 ? 21.01800 -12.91700 18.50700 1.000 29.23083  ?  339 ARG   A CG   1 
ATOM   1325 C  CD   . ARG   A 1 187 ? 21.04100 -12.02400 19.74500 1.000 26.88245  ?  339 ARG   A CD   1 
ATOM   1326 N  NE   . ARG   A 1 187 ? 21.31300 -10.63600 19.38000 1.000 24.46504  ?  339 ARG   A NE   1 
ATOM   1327 C  CZ   . ARG   A 1 187 ? 21.50700 -9.65100  20.25300 1.000 22.85219  ?  339 ARG   A CZ   1 
ATOM   1328 N  NH1  . ARG   A 1 187 ? 21.45600 -9.88500  21.56500 1.000 19.41575  ?  339 ARG   A NH1  1 
ATOM   1329 N  NH2  . ARG   A 1 187 ? 21.76600 -8.42500  19.81100 1.000 22.99613  ?  339 ARG   A NH2  1 
ATOM   1330 N  N    . PRO   A 1 188 ? 19.59600 -16.58600 21.04800 1.000 40.05304  ?  340 PRO   A N    1 
ATOM   1331 C  CA   . PRO   A 1 188 ? 18.85100 -17.82600 21.29500 1.000 41.28857  ?  340 PRO   A CA   1 
ATOM   1332 C  C    . PRO   A 1 188 ? 17.80000 -18.06200 20.22000 1.000 41.97419  ?  340 PRO   A C    1 
ATOM   1333 O  O    . PRO   A 1 188 ? 17.09900 -17.14300 19.79200 1.000 42.52460  ?  340 PRO   A O    1 
ATOM   1334 C  CB   . PRO   A 1 188 ? 18.21500 -17.59000 22.67000 1.000 41.96288  ?  340 PRO   A CB   1 
ATOM   1335 C  CG   . PRO   A 1 188 ? 18.14300 -16.09200 22.80000 1.000 41.79403  ?  340 PRO   A CG   1 
ATOM   1336 C  CD   . PRO   A 1 188 ? 19.38400 -15.58900 22.11200 1.000 41.22260  ?  340 PRO   A CD   1 
ATOM   1337 N  N    . GLY   A 1 189 ? 17.70400 -19.31300 19.77800 1.000 42.50791  ?  341 GLY   A N    1 
ATOM   1338 C  CA   . GLY   A 1 189 ? 16.75500 -19.69900 18.76000 1.000 42.17054  ?  341 GLY   A CA   1 
ATOM   1339 C  C    . GLY   A 1 189 ? 17.26600 -19.61800 17.34000 1.000 40.30475  ?  341 GLY   A C    1 
ATOM   1340 O  O    . GLY   A 1 189 ? 16.56000 -20.05200 16.42500 1.000 40.10024  ?  341 GLY   A O    1 
ATOM   1341 N  N    . VAL   A 1 190 ? 18.46100 -19.06600 17.11900 1.000 38.45828  ?  342 VAL   A N    1 
ATOM   1342 C  CA   . VAL   A 1 190 ? 18.99900 -18.99900 15.76500 1.000 38.47397  ?  342 VAL   A CA   1 
ATOM   1343 C  C    . VAL   A 1 190 ? 19.20500 -20.41500 15.24300 1.000 41.51114  ?  342 VAL   A C    1 
ATOM   1344 O  O    . VAL   A 1 190 ? 19.68000 -21.30300 15.96300 1.000 42.00490  ?  342 VAL   A O    1 
ATOM   1345 C  CB   . VAL   A 1 190 ? 20.31300 -18.19500 15.74000 1.000 37.13002  ?  342 VAL   A CB   1 
ATOM   1346 C  CG1  . VAL   A 1 190 ? 21.02600 -18.35300 14.39900 1.000 37.15714  ?  342 VAL   A CG1  1 
ATOM   1347 C  CG2  . VAL   A 1 190 ? 20.05100 -16.72300 16.02700 1.000 34.77146  ?  342 VAL   A CG2  1 
ATOM   1348 N  N    . GLN   A 1 191 ? 18.83400 -20.63900 13.98300 1.000 42.93255  ?  343 GLN   A N    1 
ATOM   1349 C  CA   . GLN   A 1 191 ? 18.99400 -21.95000 13.36500 1.000 46.40860  ?  343 GLN   A CA   1 
ATOM   1350 C  C    . GLN   A 1 191 ? 20.27500 -22.03400 12.53900 1.000 45.50787  ?  343 GLN   A C    1 
ATOM   1351 O  O    . GLN   A 1 191 ? 21.15400 -22.84500 12.84100 1.000 46.17338  ?  343 GLN   A O    1 
ATOM   1352 C  CB   . GLN   A 1 191 ? 17.75900 -22.28500 12.51100 1.000 49.93032  ?  343 GLN   A CB   1 
ATOM   1353 C  CG   . GLN   A 1 191 ? 17.63900 -23.76200 12.17200 1.000 53.75065  ?  343 GLN   A CG   1 
ATOM   1354 C  CD   . GLN   A 1 191 ? 18.17500 -24.08400 10.78700 1.000 57.67593  ?  343 GLN   A CD   1 
ATOM   1355 O  OE1  . GLN   A 1 191 ? 19.23900 -24.69300 10.63800 1.000 60.94115  ?  343 GLN   A OE1  1 
ATOM   1356 N  NE2  . GLN   A 1 191 ? 17.43100 -23.68000 9.76400  1.000 57.58290  ?  343 GLN   A NE2  1 
ATOM   1357 N  N    . ASP   A 1 192 ? 20.41100 -21.19600 11.51200 1.000 44.02425  ?  344 ASP   A N    1 
ATOM   1358 C  CA   . ASP   A 1 192 ? 21.59600 -21.21700 10.65300 1.000 44.40152  ?  344 ASP   A CA   1 
ATOM   1359 C  C    . ASP   A 1 192 ? 22.65500 -20.25000 11.19100 1.000 42.64090  ?  344 ASP   A C    1 
ATOM   1360 O  O    . ASP   A 1 192 ? 22.99700 -19.23300 10.58200 1.000 40.94907  ?  344 ASP   A O    1 
ATOM   1361 C  CB   . ASP   A 1 192 ? 21.21200 -20.88600 9.21900  1.000 45.11544  ?  344 ASP   A CB   1 
ATOM   1362 C  CG   . ASP   A 1 192 ? 22.29900 -21.25800 8.23100  1.000 47.85993  ?  344 ASP   A CG   1 
ATOM   1363 O  OD1  . ASP   A 1 192 ? 22.06500 -21.14300 7.01000  1.000 48.97407  ?  344 ASP   A OD1  1 
ATOM   1364 O  OD2  . ASP   A 1 192 ? 23.39400 -21.66400 8.67800  1.000 49.11420  ?  344 ASP   A OD2  1 
ATOM   1365 N  N    . ALA   A 1 193 ? 23.19600 -20.60900 12.35900 1.000 42.88517  ?  345 ALA   A N    1 
ATOM   1366 C  CA   . ALA   A 1 193 ? 24.19600 -19.76300 13.00700 1.000 42.66680  ?  345 ALA   A CA   1 
ATOM   1367 C  C    . ALA   A 1 193 ? 25.45700 -19.62000 12.16100 1.000 43.88529  ?  345 ALA   A C    1 
ATOM   1368 O  O    . ALA   A 1 193 ? 26.15900 -18.60700 12.26400 1.000 43.69469  ?  345 ALA   A O    1 
ATOM   1369 C  CB   . ALA   A 1 193 ? 24.54400 -20.31900 14.39000 1.000 42.50073  ?  345 ALA   A CB   1 
ATOM   1370 N  N    A LYS   A 1 194 ? 25.76500 -20.62400 11.33400 0.480 45.47145  ?  346 LYS   A N    1 
ATOM   1371 N  N    B LYS   A 1 194 ? 25.76100 -20.61100 11.31900 0.520 45.45993  ?  346 LYS   A N    1 
ATOM   1372 C  CA   A LYS   A 1 194 ? 26.91800 -20.52600 10.44400 0.480 46.72572  ?  346 LYS   A CA   1 
ATOM   1373 C  CA   B LYS   A 1 194 ? 26.93600 -20.50000 10.46000 0.520 46.70230  ?  346 LYS   A CA   1 
ATOM   1374 C  C    A LYS   A 1 194 ? 26.74600 -19.39000 9.44500  0.480 45.24392  ?  346 LYS   A C    1 
ATOM   1375 C  C    B LYS   A 1 194 ? 26.75800 -19.40300 9.41600  0.520 45.27498  ?  346 LYS   A C    1 
ATOM   1376 O  O    A LYS   A 1 194 ? 27.68700 -18.63300 9.18300  0.480 44.95361  ?  346 LYS   A O    1 
ATOM   1377 O  O    B LYS   A 1 194 ? 27.71100 -18.68500 9.09600  0.520 45.07861  ?  346 LYS   A O    1 
ATOM   1378 C  CB   A LYS   A 1 194 ? 27.13500 -21.85500 9.71700  0.480 49.42473  ?  346 LYS   A CB   1 
ATOM   1379 C  CB   B LYS   A 1 194 ? 27.23200 -21.84400 9.79400  0.520 49.45196  ?  346 LYS   A CB   1 
ATOM   1380 C  CG   A LYS   A 1 194 ? 28.20500 -21.81400 8.63300  0.480 51.06513  ?  346 LYS   A CG   1 
ATOM   1381 C  CG   B LYS   A 1 194 ? 28.17400 -22.73400 10.59400 0.520 51.12112  ?  346 LYS   A CG   1 
ATOM   1382 C  CD   A LYS   A 1 194 ? 28.31800 -23.15100 7.91100  0.480 53.66982  ?  346 LYS   A CD   1 
ATOM   1383 C  CD   B LYS   A 1 194 ? 28.57700 -23.96800 9.80400  0.520 53.93850  ?  346 LYS   A CD   1 
ATOM   1384 C  CE   A LYS   A 1 194 ? 29.69400 -23.33300 7.28600  0.480 55.74783  ?  346 LYS   A CE   1 
ATOM   1385 C  CE   B LYS   A 1 194 ? 27.66600 -25.14400 10.11400 0.520 55.26320  ?  346 LYS   A CE   1 
ATOM   1386 N  NZ   A LYS   A 1 194 ? 29.92400 -24.73500 6.83800  0.480 59.52610  ?  346 LYS   A NZ   1 
ATOM   1387 N  NZ   B LYS   A 1 194 ? 28.43600 -26.36800 10.47900 0.520 57.37635  ?  346 LYS   A NZ   1 
ATOM   1388 N  N    . LEU   A 1 195 ? 25.54700 -19.25000 8.88100  1.000 43.72716  ?  347 LEU   A N    1 
ATOM   1389 C  CA   . LEU   A 1 195 ? 25.30800 -18.18000 7.92000  1.000 40.63726  ?  347 LEU   A CA   1 
ATOM   1390 C  C    . LEU   A 1 195 ? 25.20800 -16.82400 8.61300  1.000 37.11423  ?  347 LEU   A C    1 
ATOM   1391 O  O    . LEU   A 1 195 ? 25.67600 -15.81500 8.07800  1.000 35.78100  ?  347 LEU   A O    1 
ATOM   1392 C  CB   . LEU   A 1 195 ? 24.04400 -18.47400 7.11300  1.000 39.86605  ?  347 LEU   A CB   1 
ATOM   1393 C  CG   . LEU   A 1 195 ? 23.47800 -17.36500 6.22100  1.000 39.45310  ?  347 LEU   A CG   1 
ATOM   1394 C  CD1  . LEU   A 1 195 ? 24.50900 -16.87000 5.22600  1.000 40.59740  ?  347 LEU   A CD1  1 
ATOM   1395 C  CD2  . LEU   A 1 195 ? 22.22700 -17.84300 5.48700  1.000 39.71466  ?  347 LEU   A CD2  1 
ATOM   1396 N  N    . VAL   A 1 196 ? 24.60100 -16.77800 9.80000  1.000 36.04655  ?  348 VAL   A N    1 
ATOM   1397 C  CA   . VAL   A 1 196 ? 24.55200 -15.52500 10.55000 1.000 32.29682  ?  348 VAL   A CA   1 
ATOM   1398 C  C    . VAL   A 1 196 ? 25.96600 -15.05700 10.87700 1.000 31.17228  ?  348 VAL   A C    1 
ATOM   1399 O  O    . VAL   A 1 196 ? 26.28900 -13.86800 10.75600 1.000 28.50899  ?  348 VAL   A O    1 
ATOM   1400 C  CB   . VAL   A 1 196 ? 23.69600 -15.69600 11.82000 1.000 30.85482  ?  348 VAL   A CB   1 
ATOM   1401 C  CG1  . VAL   A 1 196 ? 23.69500 -14.41800 12.64300 1.000 29.88880  ?  348 VAL   A CG1  1 
ATOM   1402 C  CG2  . VAL   A 1 196 ? 22.26700 -16.10000 11.46400 1.000 28.58856  ?  348 VAL   A CG2  1 
ATOM   1403 N  N    . GLU   A 1 197 ? 26.83800 -15.98900 11.26800 1.000 32.56115  ?  349 GLU   A N    1 
ATOM   1404 C  CA   . GLU   A 1 197 ? 28.21700 -15.62400 11.58500 1.000 35.32467  ?  349 GLU   A CA   1 
ATOM   1405 C  C    . GLU   A 1 197 ? 28.95000 -15.09800 10.35600 1.000 34.32358  ?  349 GLU   A C    1 
ATOM   1406 O  O    . GLU   A 1 197 ? 29.69500 -14.11700 10.44500 1.000 33.85932  ?  349 GLU   A O    1 
ATOM   1407 C  CB   . GLU   A 1 197 ? 28.95900 -16.81900 12.18400 1.000 40.67478  ?  349 GLU   A CB   1 
ATOM   1408 C  CG   . GLU   A 1 197 ? 30.41800 -16.51800 12.53600 1.000 45.32131  ?  349 GLU   A CG   1 
ATOM   1409 C  CD   . GLU   A 1 197 ? 31.03000 -17.54300 13.48300 1.000 50.21103  ?  349 GLU   A CD   1 
ATOM   1410 O  OE1  . GLU   A 1 197 ? 30.71000 -18.74600 13.35000 1.000 53.58358  ?  349 GLU   A OE1  1 
ATOM   1411 O  OE2  . GLU   A 1 197 ? 31.84000 -17.14500 14.35000 1.000 49.94246  ?  349 GLU   A OE2  1 
ATOM   1412 N  N    . ALA   A 1 198 ? 28.73700 -15.72200 9.19600  1.000 35.53365  ?  350 ALA   A N    1 
ATOM   1413 C  CA   . ALA   A 1 198 ? 29.40100 -15.26300 7.97800  1.000 35.76619  ?  350 ALA   A CA   1 
ATOM   1414 C  C    . ALA   A 1 198 ? 28.99000 -13.83800 7.61900  1.000 34.13273  ?  350 ALA   A C    1 
ATOM   1415 O  O    . ALA   A 1 198 ? 29.82500 -13.03400 7.18800  1.000 35.19447  ?  350 ALA   A O    1 
ATOM   1416 C  CB   . ALA   A 1 198 ? 29.09400 -16.21500 6.82400  1.000 36.38982  ?  350 ALA   A CB   1 
ATOM   1417 N  N    . ILE   A 1 199 ? 27.70700 -13.50600 7.77500  1.000 31.88067  ?  351 ILE   A N    1 
ATOM   1418 C  CA   . ILE   A 1 199 ? 27.26800 -12.13900 7.50700  1.000 30.09852  ?  351 ILE   A CA   1 
ATOM   1419 C  C    . ILE   A 1 199 ? 27.86400 -11.17500 8.52600  1.000 28.45885  ?  351 ILE   A C    1 
ATOM   1420 O  O    . ILE   A 1 199 ? 28.35700 -10.09800 8.17300  1.000 27.45684  ?  351 ILE   A O    1 
ATOM   1421 C  CB   . ILE   A 1 199 ? 25.73100 -12.05000 7.49400  1.000 29.79739  ?  351 ILE   A CB   1 
ATOM   1422 C  CG1  . ILE   A 1 199 ? 25.15200 -12.90700 6.37100  1.000 30.40432  ?  351 ILE   A CG1  1 
ATOM   1423 C  CG2  . ILE   A 1 199 ? 25.29900 -10.60200 7.36600  1.000 29.20664  ?  351 ILE   A CG2  1 
ATOM   1424 C  CD1  . ILE   A 1 199 ? 23.70600 -13.34100 6.62300  1.000 29.75790  ?  351 ILE   A CD1  1 
ATOM   1425 N  N    . GLN   A 1 200 ? 27.80300 -11.53100 9.81000  1.000 28.80383  ?  352 GLN   A N    1 
ATOM   1426 C  CA   . GLN   A 1 200 ? 28.38500 -10.66100 10.82300 1.000 27.49527  ?  352 GLN   A CA   1 
ATOM   1427 C  C    . GLN   A 1 200 ? 29.87500 -10.47300 10.58800 1.000 29.24833  ?  352 GLN   A C    1 
ATOM   1428 O  O    . GLN   A 1 200 ? 30.39600 -9.36100  10.72900 1.000 29.55948  ?  352 GLN   A O    1 
ATOM   1429 C  CB   . GLN   A 1 200 ? 28.15200 -11.22100 12.21900 1.000 28.35211  ?  352 GLN   A CB   1 
ATOM   1430 C  CG   . GLN   A 1 200 ? 28.52000 -10.21900 13.31200 1.000 28.40527  ?  352 GLN   A CG   1 
ATOM   1431 C  CD   . GLN   A 1 200 ? 28.51600 -10.81900 14.70300 1.000 29.33043  ?  352 GLN   A CD   1 
ATOM   1432 O  OE1  . GLN   A 1 200 ? 29.27600 -11.74200 14.99300 1.000 31.29502  ?  352 GLN   A OE1  1 
ATOM   1433 N  NE2  . GLN   A 1 200 ? 27.65500 -10.29200 15.57700 1.000 27.50723  ?  352 GLN   A NE2  1 
ATOM   1434 N  N    . ASP   A 1 201 ? 30.57400 -11.55100 10.21600 1.000 30.94053  ?  353 ASP   A N    1 
ATOM   1435 C  CA   . ASP   A 1 201 ? 32.02000 -11.45900 10.02100 1.000 34.05218  ?  353 ASP   A CA   1 
ATOM   1436 C  C    . ASP   A 1 201 ? 32.35400 -10.45800 8.92800  1.000 32.59126  ?  353 ASP   A C    1 
ATOM   1437 O  O    . ASP   A 1 201 ? 33.31000 -9.68400  9.05300  1.000 31.51627  ?  353 ASP   A O    1 
ATOM   1438 C  CB   . ASP   A 1 201 ? 32.60000 -12.83500 9.68600  1.000 38.58374  ?  353 ASP   A CB   1 
ATOM   1439 C  CG   . ASP   A 1 201 ? 32.82800 -13.68400 10.91900 1.000 43.08125  ?  353 ASP   A CG   1 
ATOM   1440 O  OD1  . ASP   A 1 201 ? 32.56600 -13.18800 12.03500 1.000 43.34934  ?  353 ASP   A OD1  1 
ATOM   1441 O  OD2  . ASP   A 1 201 ? 33.27200 -14.84300 10.77700 1.000 46.21087  ?  353 ASP   A OD2  1 
ATOM   1442 N  N    . ARG   A 1 202 ? 31.56800 -10.45100 7.85100  1.000 32.97287  ?  354 ARG   A N    1 
ATOM   1443 C  CA   . ARG   A 1 202 ? 31.77500 -9.46600  6.79600  1.000 35.29169  ?  354 ARG   A CA   1 
ATOM   1444 C  C    . ARG   A 1 202 ? 31.65300 -8.04900  7.34200  1.000 31.82716  ?  354 ARG   A C    1 
ATOM   1445 O  O    . ARG   A 1 202 ? 32.39500 -7.15000  6.93100  1.000 32.17734  ?  354 ARG   A O    1 
ATOM   1446 C  CB   . ARG   A 1 202 ? 30.77500 -9.69900  5.66000  1.000 39.44786  ?  354 ARG   A CB   1 
ATOM   1447 C  CG   . ARG   A 1 202 ? 31.10000 -8.95800  4.37700  1.000 44.83551  ?  354 ARG   A CG   1 
ATOM   1448 C  CD   . ARG   A 1 202 ? 30.35300 -9.53800  3.17000  1.000 49.99269  ?  354 ARG   A CD   1 
ATOM   1449 N  NE   . ARG   A 1 202 ? 30.31700 -11.00000 3.16400  1.000 55.01175  ?  354 ARG   A NE   1 
ATOM   1450 C  CZ   . ARG   A 1 202 ? 29.21500 -11.72200 2.96600  1.000 59.21368  ?  354 ARG   A CZ   1 
ATOM   1451 N  NH1  . ARG   A 1 202 ? 29.27400 -13.04900 2.97100  1.000 62.30578  ?  354 ARG   A NH1  1 
ATOM   1452 N  NH2  . ARG   A 1 202 ? 28.04800 -11.11800 2.76700  1.000 60.73488  ?  354 ARG   A NH2  1 
ATOM   1453 N  N    . LEU   A 1 203 ? 30.71800 -7.83000  8.26900  1.000 29.27458  ?  355 LEU   A N    1 
ATOM   1454 C  CA   . LEU   A 1 203 ? 30.53700 -6.50600  8.84900  1.000 26.22195  ?  355 LEU   A CA   1 
ATOM   1455 C  C    . LEU   A 1 203 ? 31.64000 -6.18600  9.85100  1.000 25.12870  ?  355 LEU   A C    1 
ATOM   1456 O  O    . LEU   A 1 203 ? 32.11900 -5.05100  9.89700  1.000 23.89286  ?  355 LEU   A O    1 
ATOM   1457 C  CB   . LEU   A 1 203 ? 29.16300 -6.40300  9.52200  1.000 23.99067  ?  355 LEU   A CB   1 
ATOM   1458 C  CG   . LEU   A 1 203 ? 27.91400 -6.63800  8.66000  1.000 25.00528  ?  355 LEU   A CG   1 
ATOM   1459 C  CD1  . LEU   A 1 203 ? 26.69800 -6.86700  9.53800  1.000 23.79825  ?  355 LEU   A CD1  1 
ATOM   1460 C  CD2  . LEU   A 1 203 ? 27.66100 -5.48300  7.69800  1.000 24.57867  ?  355 LEU   A CD2  1 
ATOM   1461 N  N    . SER   A 1 204 ? 32.04400 -7.17400  10.65900 1.000 27.67609  ?  356 SER   A N    1 
ATOM   1462 C  CA   . SER   A 1 204 ? 33.11300 -6.96700  11.63600 1.000 29.47045  ?  356 SER   A CA   1 
ATOM   1463 C  C    . SER   A 1 204 ? 34.42500 -6.58800  10.95500 1.000 31.11493  ?  356 SER   A C    1 
ATOM   1464 O  O    . SER   A 1 204 ? 35.11300 -5.65400  11.38300 1.000 31.14101  ?  356 SER   A O    1 
ATOM   1465 C  CB   . SER   A 1 204 ? 33.29800 -8.22600  12.48300 1.000 31.69768  ?  356 SER   A CB   1 
ATOM   1466 O  OG   . SER   A 1 204 ? 32.15500 -8.47600  13.28700 1.000 33.13049  ?  356 SER   A OG   1 
ATOM   1467 N  N    . ASN   A 1 205 ? 34.79800 -7.31400  9.89800  1.000 32.48157  ?  357 ASN   A N    1 
ATOM   1468 C  CA   . ASN   A 1 205 ? 36.01600 -6.96800  9.16900  1.000 33.67084  ?  357 ASN   A CA   1 
ATOM   1469 C  C    . ASN   A 1 205 ? 35.90100 -5.60400  8.49800  1.000 33.19640  ?  357 ASN   A C    1 
ATOM   1470 O  O    . ASN   A 1 205 ? 36.89000 -4.86800  8.42600  1.000 34.78122  ?  357 ASN   A O    1 
ATOM   1471 C  CB   . ASN   A 1 205 ? 36.34300 -8.04600  8.13900  1.000 35.72112  ?  357 ASN   A CB   1 
ATOM   1472 C  CG   . ASN   A 1 205 ? 36.76400 -9.35900  8.78100  1.000 37.94068  ?  357 ASN   A CG   1 
ATOM   1473 O  OD1  . ASN   A 1 205 ? 36.51700 -10.43500 8.23800  1.000 40.47703  ?  357 ASN   A OD1  1 
ATOM   1474 N  ND2  . ASN   A 1 205 ? 37.41000 -9.27300  9.93700  1.000 36.73048  ?  357 ASN   A ND2  1 
ATOM   1475 N  N    . THR   A 1 206 ? 34.71000 -5.24300  8.01600  1.000 31.72419  ?  358 THR   A N    1 
ATOM   1476 C  CA   . THR   A 1 206 ? 34.50000 -3.89200  7.50000  1.000 30.42979  ?  358 THR   A CA   1 
ATOM   1477 C  C    . THR   A 1 206 ? 34.78200 -2.84700  8.57400  1.000 30.78487  ?  358 THR   A C    1 
ATOM   1478 O  O    . THR   A 1 206 ? 35.48400 -1.85900  8.32800  1.000 32.53123  ?  358 THR   A O    1 
ATOM   1479 C  CB   . THR   A 1 206 ? 33.06800 -3.74500  6.97900  1.000 29.51166  ?  358 THR   A CB   1 
ATOM   1480 O  OG1  . THR   A 1 206 ? 32.79300 -4.77700  6.02400  1.000 30.02508  ?  358 THR   A OG1  1 
ATOM   1481 C  CG2  . THR   A 1 206 ? 32.86400 -2.38000  6.31300  1.000 28.05331  ?  358 THR   A CG2  1 
ATOM   1482 N  N    . LEU   A 1 207 ? 34.23800 -3.04800  9.77500  1.000 28.09289  ?  359 LEU   A N    1 
ATOM   1483 C  CA   . LEU   A 1 207 ? 34.44500 -2.07800  10.84400 1.000 26.78504  ?  359 LEU   A CA   1 
ATOM   1484 C  C    . LEU   A 1 207 ? 35.89900 -2.06600  11.29400 1.000 27.89468  ?  359 LEU   A C    1 
ATOM   1485 O  O    . LEU   A 1 207 ? 36.50300 -0.99700  11.44300 1.000 28.43669  ?  359 LEU   A O    1 
ATOM   1486 C  CB   . LEU   A 1 207 ? 33.51600 -2.38300  12.01600 1.000 25.55643  ?  359 LEU   A CB   1 
ATOM   1487 C  CG   . LEU   A 1 207 ? 33.74500 -1.59000  13.30400 1.000 23.72901  ?  359 LEU   A CG   1 
ATOM   1488 C  CD1  . LEU   A 1 207 ? 33.57800 -0.10300  13.05400 1.000 21.55699  ?  359 LEU   A CD1  1 
ATOM   1489 C  CD2  . LEU   A 1 207 ? 32.77300 -2.07800  14.38200 1.000 22.21928  ?  359 LEU   A CD2  1 
ATOM   1490 N  N    . GLN   A 1 208 ? 36.47700 -3.25100  11.52200 1.000 28.54665  ?  360 GLN   A N    1 
ATOM   1491 C  CA   . GLN   A 1 208 ? 37.87700 -3.32200  11.93800 1.000 31.93467  ?  360 GLN   A CA   1 
ATOM   1492 C  C    . GLN   A 1 208 ? 38.77900 -2.62300  10.93200 1.000 32.26135  ?  360 GLN   A C    1 
ATOM   1493 O  O    . GLN   A 1 208 ? 39.69100 -1.88200  11.31300 1.000 32.51922  ?  360 GLN   A O    1 
ATOM   1494 C  CB   . GLN   A 1 208 ? 38.30300 -4.78000  12.10900 1.000 35.67136  ?  360 GLN   A CB   1 
ATOM   1495 C  CG   . GLN   A 1 208 ? 37.72200 -5.45700  13.32800 1.000 38.87937  ?  360 GLN   A CG   1 
ATOM   1496 C  CD   . GLN   A 1 208 ? 38.21700 -6.87800  13.49100 1.000 44.57428  ?  360 GLN   A CD   1 
ATOM   1497 O  OE1  . GLN   A 1 208 ? 39.36100 -7.10600  13.88800 1.000 46.83663  ?  360 GLN   A OE1  1 
ATOM   1498 N  NE2  . GLN   A 1 208 ? 37.35500 -7.84500  13.18900 1.000 46.24246  ?  360 GLN   A NE2  1 
ATOM   1499 N  N    . THR   A 1 209 ? 38.52000 -2.82900  9.63700  1.000 32.83192  ?  361 THR   A N    1 
ATOM   1500 C  CA   . THR   A 1 209 ? 39.34500 -2.21000  8.60500  1.000 33.68167  ?  361 THR   A CA   1 
ATOM   1501 C  C    . THR   A 1 209 ? 39.07600 -0.71100  8.50100  1.000 31.73384  ?  361 THR   A C    1 
ATOM   1502 O  O    . THR   A 1 209 ? 40.01300 0.07700   8.31600  1.000 32.41830  ?  361 THR   A O    1 
ATOM   1503 C  CB   . THR   A 1 209 ? 39.11000 -2.90800  7.26200  1.000 36.01847  ?  361 THR   A CB   1 
ATOM   1504 O  OG1  . THR   A 1 209 ? 39.45400 -4.29800  7.37600  1.000 37.84920  ?  361 THR   A OG1  1 
ATOM   1505 C  CG2  . THR   A 1 209 ? 39.94400 -2.27400  6.16300  1.000 36.35447  ?  361 THR   A CG2  1 
ATOM   1506 N  N    . TYR   A 1 210 ? 37.80800 -0.29600  8.62400  1.000 28.79360  ?  362 TYR   A N    1 
ATOM   1507 C  CA   . TYR   A 1 210 ? 37.48200 1.13200   8.59300  1.000 27.83779  ?  362 TYR   A CA   1 
ATOM   1508 C  C    . TYR   A 1 210 ? 38.24800 1.88600   9.67100  1.000 28.85797  ?  362 TYR   A C    1 
ATOM   1509 O  O    . TYR   A 1 210 ? 38.83800 2.94300   9.41500  1.000 30.59312  ?  362 TYR   A O    1 
ATOM   1510 C  CB   . TYR   A 1 210 ? 35.96700 1.35800   8.76800  1.000 26.72547  ?  362 TYR   A CB   1 
ATOM   1511 C  CG   . TYR   A 1 210 ? 35.61600 2.84100   8.82700  1.000 26.46828  ?  362 TYR   A CG   1 
ATOM   1512 C  CD1  . TYR   A 1 210 ? 35.59200 3.53400   10.03900 1.000 24.67444  ?  362 TYR   A CD1  1 
ATOM   1513 C  CD2  . TYR   A 1 210 ? 35.34800 3.55400   7.66300  1.000 27.91735  ?  362 TYR   A CD2  1 
ATOM   1514 C  CE1  . TYR   A 1 210 ? 35.31000 4.89000   10.08300 1.000 24.58068  ?  362 TYR   A CE1  1 
ATOM   1515 C  CE2  . TYR   A 1 210 ? 35.05200 4.90600   7.69700  1.000 27.71307  ?  362 TYR   A CE2  1 
ATOM   1516 C  CZ   . TYR   A 1 210 ? 35.03500 5.56900   8.90500  1.000 27.29994  ?  362 TYR   A CZ   1 
ATOM   1517 O  OH   . TYR   A 1 210 ? 34.74900 6.91600   8.93000  1.000 27.63386  ?  362 TYR   A OH   1 
ATOM   1518 N  N    . ILE   A 1 211 ? 38.24300 1.36200   10.89400 1.000 28.03588  ?  363 ILE   A N    1 
ATOM   1519 C  CA   . ILE   A 1 211 ? 38.90000 2.06700   11.99100 1.000 26.99515  ?  363 ILE   A CA   1 
ATOM   1520 C  C    . ILE   A 1 211 ? 40.39300 2.20800   11.70900 1.000 32.23908  ?  363 ILE   A C    1 
ATOM   1521 O  O    . ILE   A 1 211 ? 40.97800 3.28500   11.88900 1.000 32.26564  ?  363 ILE   A O    1 
ATOM   1522 C  CB   . ILE   A 1 211 ? 38.62300 1.35100   13.32200 1.000 25.24621  ?  363 ILE   A CB   1 
ATOM   1523 C  CG1  . ILE   A 1 211 ? 37.12400 1.42400   13.65100 1.000 24.01836  ?  363 ILE   A CG1  1 
ATOM   1524 C  CG2  . ILE   A 1 211 ? 39.44200 1.97400   14.45100 1.000 26.62498  ?  363 ILE   A CG2  1 
ATOM   1525 C  CD1  . ILE   A 1 211 ? 36.72500 0.54100   14.79500 1.000 23.83715  ?  363 ILE   A CD1  1 
ATOM   1526 N  N    . ARG   A 1 212 ? 41.01700 1.10200   11.32200 1.000 36.77728  ?  364 ARG   A N    1 
ATOM   1527 C  CA   . ARG   A 1 212 ? 42.46700 1.03000   10.97700 1.000 41.44380  ?  364 ARG   A CA   1 
ATOM   1528 C  C    . ARG   A 1 212 ? 42.83700 1.99700   9.83900  1.000 41.60084  ?  364 ARG   A C    1 
ATOM   1529 O  O    . ARG   A 1 212 ? 43.85700 2.57300   9.94600  1.000 42.94069  ?  364 ARG   A O    1 
ATOM   1530 C  CB   . ARG   A 1 212 ? 42.95900 -0.41200  10.78700 1.000 46.63197  ?  364 ARG   A CB   1 
ATOM   1531 C  CG   . ARG   A 1 212 ? 42.95200 -1.25800  12.05500 1.000 51.19522  ?  364 ARG   A CG   1 
ATOM   1532 C  CD   . ARG   A 1 212 ? 43.75300 -2.55100  12.16100 1.000 56.26553  ?  364 ARG   A CD   1 
ATOM   1533 N  NE   . ARG   A 1 212 ? 43.53300 -3.40200  13.33000 1.000 58.43217  ?  364 ARG   A NE   1 
ATOM   1534 C  CZ   . ARG   A 1 212 ? 44.12500 -3.24500  14.50400 1.000 60.93066  ?  364 ARG   A CZ   1 
ATOM   1535 N  NH1  . ARG   A 1 212 ? 43.84600 -4.05000  15.51500 1.000 61.38871  ?  364 ARG   A NH1  1 
ATOM   1536 N  NH2  . ARG   A 1 212 ? 45.00600 -2.27900  14.67800 1.000 62.52741  ?  364 ARG   A NH2  1 
ATOM   1537 N  N    . CYS   A 1 213 ? 41.98100 2.25700   8.86300  1.000 39.75867  ?  365 CYS   A N    1 
ATOM   1538 C  CA   . CYS   A 1 213 ? 42.29800 3.09100   7.70500  1.000 42.01668  ?  365 CYS   A CA   1 
ATOM   1539 C  C    . CYS   A 1 213 ? 41.72800 4.50300   7.73800  1.000 40.76322  ?  365 CYS   A C    1 
ATOM   1540 O  O    . CYS   A 1 213 ? 42.29100 5.38100   7.07900  1.000 43.52392  ?  365 CYS   A O    1 
ATOM   1541 C  CB   . CYS   A 1 213 ? 41.81200 2.44300   6.40000  1.000 45.73968  ?  365 CYS   A CB   1 
ATOM   1542 S  SG   . CYS   A 1 213 ? 42.35700 0.76800   6.11300  1.000 50.38128  ?  365 CYS   A SG   1 
ATOM   1543 N  N    A ARG   A 1 214 ? 40.63300 4.75000   8.46200  0.410 37.79076  ?  366 ARG   A N    1 
ATOM   1544 N  N    B ARG   A 1 214 ? 40.63800 4.74900   8.46700  0.590 37.69180  ?  366 ARG   A N    1 
ATOM   1545 C  CA   A ARG   A 1 214 ? 39.95300 6.03700   8.37600  0.410 37.34170  ?  366 ARG   A CA   1 
ATOM   1546 C  CA   B ARG   A 1 214 ? 39.94400 6.02700   8.37500  0.590 37.25711  ?  366 ARG   A CA   1 
ATOM   1547 C  C    A ARG   A 1 214 ? 39.75800 6.75400   9.70400  0.410 35.78434  ?  366 ARG   A C    1 
ATOM   1548 C  C    B ARG   A 1 214 ? 39.74000 6.74600   9.70100  0.590 35.79087  ?  366 ARG   A C    1 
ATOM   1549 O  O    A ARG   A 1 214 ? 39.38700 7.93300   9.68900  0.410 36.31156  ?  366 ARG   A O    1 
ATOM   1550 O  O    B ARG   A 1 214 ? 39.34900 7.91800   9.68200  0.590 36.36686  ?  366 ARG   A O    1 
ATOM   1551 C  CB   A ARG   A 1 214 ? 38.57900 5.87400   7.70700  0.410 37.81070  ?  366 ARG   A CB   1 
ATOM   1552 C  CB   B ARG   A 1 214 ? 38.57300 5.84000   7.70400  0.590 37.81845  ?  366 ARG   A CB   1 
ATOM   1553 C  CG   A ARG   A 1 214 ? 38.60100 5.04100   6.43600  0.410 39.67736  ?  366 ARG   A CG   1 
ATOM   1554 C  CG   B ARG   A 1 214 ? 38.63600 5.18600   6.32800  0.590 39.82388  ?  366 ARG   A CG   1 
ATOM   1555 C  CD   A ARG   A 1 214 ? 38.88600 5.89200   5.20000  0.410 42.23402  ?  366 ARG   A CD   1 
ATOM   1556 C  CD   B ARG   A 1 214 ? 38.93600 6.20700   5.23300  0.590 42.49125  ?  366 ARG   A CD   1 
ATOM   1557 N  NE   A ARG   A 1 214 ? 38.58200 7.30700   5.40000  0.410 42.67072  ?  366 ARG   A NE   1 
ATOM   1558 N  NE   B ARG   A 1 214 ? 38.56000 5.72700   3.90200  0.590 43.73065  ?  366 ARG   A NE   1 
ATOM   1559 C  CZ   A ARG   A 1 214 ? 38.97500 8.27700   4.58000  0.410 44.61517  ?  366 ARG   A CZ   1 
ATOM   1560 C  CZ   B ARG   A 1 214 ? 39.31000 4.91800   3.15700  0.590 45.93678  ?  366 ARG   A CZ   1 
ATOM   1561 N  NH1  A ARG   A 1 214 ? 39.68900 7.98600   3.50000  0.410 46.87563  ?  366 ARG   A NH1  1 
ATOM   1562 N  NH1  B ARG   A 1 214 ? 40.48400 4.49300   3.60500  0.590 46.24466  ?  366 ARG   A NH1  1 
ATOM   1563 N  NH2  A ARG   A 1 214 ? 38.65600 9.53800   4.83700  0.410 44.77391  ?  366 ARG   A NH2  1 
ATOM   1564 N  NH2  B ARG   A 1 214 ? 38.88800 4.53500   1.96000  0.590 46.67186  ?  366 ARG   A NH2  1 
ATOM   1565 N  N    . HIS   A 1 215 ? 39.98000 6.10100   10.84500 1.000 32.35444  ?  367 HIS   A N    1 
ATOM   1566 C  CA   . HIS   A 1 215 ? 39.79500 6.78000   12.11800 1.000 29.38669  ?  367 HIS   A CA   1 
ATOM   1567 C  C    . HIS   A 1 215 ? 41.15400 7.20800   12.63900 1.000 29.38944  ?  367 HIS   A C    1 
ATOM   1568 O  O    . HIS   A 1 215 ? 41.97400 6.34200   12.97700 1.000 29.09176  ?  367 HIS   A O    1 
ATOM   1569 C  CB   . HIS   A 1 215 ? 39.08300 5.89300   13.13700 1.000 28.63106  ?  367 HIS   A CB   1 
ATOM   1570 C  CG   . HIS   A 1 215 ? 38.40000 6.66700   14.22300 1.000 28.72742  ?  367 HIS   A CG   1 
ATOM   1571 N  ND1  . HIS   A 1 215 ? 37.07000 6.49200   14.54300 1.000 27.63062  ?  367 HIS   A ND1  1 
ATOM   1572 C  CD2  . HIS   A 1 215 ? 38.86000 7.63700   15.04900 1.000 29.27016  ?  367 HIS   A CD2  1 
ATOM   1573 C  CE1  . HIS   A 1 215 ? 36.74100 7.31700   15.52000 1.000 26.99812  ?  367 HIS   A CE1  1 
ATOM   1574 N  NE2  . HIS   A 1 215 ? 37.80900 8.02300   15.84600 1.000 28.40187  ?  367 HIS   A NE2  1 
ATOM   1575 N  N    . PRO   A 1 216 ? 41.45100 8.50500   12.71900 1.000 30.33176  ?  368 PRO   A N    1 
ATOM   1576 C  CA   . PRO   A 1 216 ? 42.80500 8.92700   13.07600 1.000 30.95044  ?  368 PRO   A CA   1 
ATOM   1577 C  C    . PRO   A 1 216 ? 43.05900 8.73600   14.56000 1.000 28.43469  ?  368 PRO   A C    1 
ATOM   1578 O  O    . PRO   A 1 216 ? 42.11400 8.73000   15.37100 1.000 27.99937  ?  368 PRO   A O    1 
ATOM   1579 C  CB   . PRO   A 1 216 ? 42.83600 10.41600  12.69200 1.000 33.54109  ?  368 PRO   A CB   1 
ATOM   1580 C  CG   . PRO   A 1 216 ? 41.50700 10.69800  11.99400 1.000 34.39057  ?  368 PRO   A CG   1 
ATOM   1581 C  CD   . PRO   A 1 216 ? 40.56100 9.65000   12.46400 1.000 31.68898  ?  368 PRO   A CD   1 
ATOM   1582 N  N    . PRO   A 1 217 ? 44.31200 8.56200   14.96500 1.000 28.37721  ?  369 PRO   A N    1 
ATOM   1583 C  CA   . PRO   A 1 217 ? 44.63600 8.57200   16.39000 1.000 28.04835  ?  369 PRO   A CA   1 
ATOM   1584 C  C    . PRO   A 1 217 ? 44.52700 9.98000   16.94400 1.000 30.10460  ?  369 PRO   A C    1 
ATOM   1585 O  O    . PRO   A 1 217 ? 44.67500 10.96100  16.19700 1.000 30.72069  ?  369 PRO   A O    1 
ATOM   1586 C  CB   . PRO   A 1 217 ? 46.08700 8.06400   16.42600 1.000 29.51644  ?  369 PRO   A CB   1 
ATOM   1587 C  CG   . PRO   A 1 217 ? 46.64300 8.43500   15.07300 1.000 31.37375  ?  369 PRO   A CG   1 
ATOM   1588 C  CD   . PRO   A 1 217 ? 45.48600 8.26400   14.12400 1.000 29.56135  ?  369 PRO   A CD   1 
ATOM   1589 N  N    . PRO   A 1 218 ? 44.30700 10.13300  18.25800 1.000 30.97070  ?  370 PRO   A N    1 
ATOM   1590 C  CA   . PRO   A 1 218 ? 44.21700 9.06100   19.25900 1.000 30.86420  ?  370 PRO   A CA   1 
ATOM   1591 C  C    . PRO   A 1 218 ? 42.82200 8.43400   19.41300 1.000 28.60512  ?  370 PRO   A C    1 
ATOM   1592 O  O    . PRO   A 1 218 ? 42.67900 7.44100   20.12600 1.000 28.03069  ?  370 PRO   A O    1 
ATOM   1593 C  CB   . PRO   A 1 218 ? 44.63200 9.76900   20.55100 1.000 33.17474  ?  370 PRO   A CB   1 
ATOM   1594 C  CG   . PRO   A 1 218 ? 44.18700 11.18600  20.35500 1.000 33.62088  ?  370 PRO   A CG   1 
ATOM   1595 C  CD   . PRO   A 1 218 ? 44.29200 11.47400  18.87200 1.000 32.15016  ?  370 PRO   A CD   1 
ATOM   1596 N  N    . GLY   A 1 219 ? 41.81500 8.98500   18.73200 1.000 28.85262  ?  371 GLY   A N    1 
ATOM   1597 C  CA   . GLY   A 1 219 ? 40.46200 8.46100   18.87500 1.000 27.12173  ?  371 GLY   A CA   1 
ATOM   1598 C  C    . GLY   A 1 219 ? 40.32800 6.99400   18.51000 1.000 28.21878  ?  371 GLY   A C    1 
ATOM   1599 O  O    . GLY   A 1 219 ? 39.44100 6.30200   19.01700 1.000 28.74038  ?  371 GLY   A O    1 
ATOM   1600 N  N    . SER   A 1 220 ? 41.19800 6.49800   17.63300 1.000 27.63646  ?  372 SER   A N    1 
ATOM   1601 C  CA   . SER   A 1 220 ? 41.13200 5.11300   17.18300 1.000 28.36441  ?  372 SER   A CA   1 
ATOM   1602 C  C    . SER   A 1 220 ? 41.68700 4.11500   18.19300 1.000 28.27382  ?  372 SER   A C    1 
ATOM   1603 O  O    . SER   A 1 220 ? 41.55300 2.90700   17.97800 1.000 27.61773  ?  372 SER   A O    1 
ATOM   1604 C  CB   . SER   A 1 220 ? 41.90400 4.95800   15.87200 1.000 30.26251  ?  372 SER   A CB   1 
ATOM   1605 O  OG   . SER   A 1 220 ? 43.24800 5.36700   16.06600 1.000 31.63023  ?  372 SER   A OG   1 
ATOM   1606 N  N    . HIS   A 1 221 ? 42.32300 4.58100   19.26700 1.000 29.90170  ?  373 HIS   A N    1 
ATOM   1607 C  CA   . HIS   A 1 221 ? 43.02000 3.69800   20.19800 1.000 30.16398  ?  373 HIS   A CA   1 
ATOM   1608 C  C    . HIS   A 1 221 ? 42.07300 2.68600   20.83800 1.000 29.95963  ?  373 HIS   A C    1 
ATOM   1609 O  O    . HIS   A 1 221 ? 41.16900 3.07000   21.58500 1.000 28.94495  ?  373 HIS   A O    1 
ATOM   1610 C  CB   . HIS   A 1 221 ? 43.71500 4.51900   21.28400 1.000 30.79105  ?  373 HIS   A CB   1 
ATOM   1611 C  CG   . HIS   A 1 221 ? 44.38700 3.68400   22.33000 1.000 31.74606  ?  373 HIS   A CG   1 
ATOM   1612 N  ND1  . HIS   A 1 221 ? 45.33000 2.72600   22.02300 1.000 32.23656  ?  373 HIS   A ND1  1 
ATOM   1613 C  CD2  . HIS   A 1 221 ? 44.23100 3.64300   23.67400 1.000 31.28271  ?  373 HIS   A CD2  1 
ATOM   1614 C  CE1  . HIS   A 1 221 ? 45.73400 2.13900   23.13500 1.000 32.25282  ?  373 HIS   A CE1  1 
ATOM   1615 N  NE2  . HIS   A 1 221 ? 45.08200 2.67600   24.15000 1.000 32.55597  ?  373 HIS   A NE2  1 
ATOM   1616 N  N    A GLN   A 1 222 ? 42.28000 1.39800   20.54500 0.510 30.02672  ?  374 GLN   A N    1 
ATOM   1617 N  N    B GLN   A 1 222 ? 42.27500 1.39800   20.55000 0.490 30.02200  ?  374 GLN   A N    1 
ATOM   1618 C  CA   A GLN   A 1 222 ? 41.46700 0.30500   21.08600 0.510 29.33075  ?  374 GLN   A CA   1 
ATOM   1619 C  CA   B GLN   A 1 222 ? 41.46200 0.30800   21.09200 0.490 29.32679  ?  374 GLN   A CA   1 
ATOM   1620 C  C    A GLN   A 1 222 ? 39.98300 0.49700   20.78000 0.510 27.68062  ?  374 GLN   A C    1 
ATOM   1621 C  C    B GLN   A 1 222 ? 39.98400 0.46900   20.76100 0.490 27.69160  ?  374 GLN   A C    1 
ATOM   1622 O  O    A GLN   A 1 222 ? 39.12200 0.02100   21.52200 0.510 26.83966  ?  374 GLN   A O    1 
ATOM   1623 O  O    B GLN   A 1 222 ? 39.12500 -0.06100  21.47300 0.490 26.84626  ?  374 GLN   A O    1 
ATOM   1624 C  CB   A GLN   A 1 222 ? 41.68100 0.13800   22.59500 0.510 30.03562  ?  374 GLN   A CB   1 
ATOM   1625 C  CB   B GLN   A 1 222 ? 41.64200 0.17800   22.60900 0.490 29.99906  ?  374 GLN   A CB   1 
ATOM   1626 C  CG   A GLN   A 1 222 ? 43.04100 -0.43900  22.98000 0.510 32.47851  ?  374 GLN   A CG   1 
ATOM   1627 C  CG   B GLN   A 1 222 ? 43.05300 -0.18800  23.03100 0.490 32.36361  ?  374 GLN   A CG   1 
ATOM   1628 C  CD   A GLN   A 1 222 ? 43.28700 -0.42000  24.48200 0.510 33.56625  ?  374 GLN   A CD   1 
ATOM   1629 C  CD   B GLN   A 1 222 ? 43.35200 -1.65300  22.80700 0.490 33.68923  ?  374 GLN   A CD   1 
ATOM   1630 O  OE1  A GLN   A 1 222 ? 44.17100 -1.11200  24.98500 0.510 35.94491  ?  374 GLN   A OE1  1 
ATOM   1631 O  OE1  B GLN   A 1 222 ? 42.44300 -2.45900  22.59300 0.490 32.83980  ?  374 GLN   A OE1  1 
ATOM   1632 N  NE2  A GLN   A 1 222 ? 42.50600 0.37900   25.20400 0.510 33.56933  ?  374 GLN   A NE2  1 
ATOM   1633 N  NE2  B GLN   A 1 222 ? 44.63000 -2.00900  22.85700 0.490 36.03263  ?  374 GLN   A NE2  1 
ATOM   1634 N  N    . LEU   A 1 223 ? 39.67600 1.18500   19.67800 1.000 27.28702  ?  375 LEU   A N    1 
ATOM   1635 C  CA   . LEU   A 1 223 ? 38.29200 1.55400   19.40400 1.000 25.78336  ?  375 LEU   A CA   1 
ATOM   1636 C  C    . LEU   A 1 223 ? 37.42800 0.33500   19.10500 1.000 25.11292  ?  375 LEU   A C    1 
ATOM   1637 O  O    . LEU   A 1 223 ? 36.29200 0.24700   19.58600 1.000 25.54164  ?  375 LEU   A O    1 
ATOM   1638 C  CB   . LEU   A 1 223 ? 38.23700 2.55600   18.25400 1.000 25.90213  ?  375 LEU   A CB   1 
ATOM   1639 C  CG   . LEU   A 1 223 ? 36.82500 3.02800   17.89300 1.000 26.22848  ?  375 LEU   A CG   1 
ATOM   1640 C  CD1  . LEU   A 1 223 ? 36.09700 3.61300   19.12500 1.000 23.62876  ?  375 LEU   A CD1  1 
ATOM   1641 C  CD2  . LEU   A 1 223 ? 36.89800 4.03700   16.76200 1.000 27.67296  ?  375 LEU   A CD2  1 
ATOM   1642 N  N    . TYR   A 1 224 ? 37.93100 -0.60800  18.30500 1.000 26.12817  ?  376 TYR   A N    1 
ATOM   1643 C  CA   . TYR   A 1 224 ? 37.14000 -1.79800  17.99900 1.000 28.34318  ?  376 TYR   A CA   1 
ATOM   1644 C  C    . TYR   A 1 224 ? 36.79200 -2.56800  19.26700 1.000 27.31173  ?  376 TYR   A C    1 
ATOM   1645 O  O    . TYR   A 1 224 ? 35.64000 -2.97400  19.46600 1.000 26.07007  ?  376 TYR   A O    1 
ATOM   1646 C  CB   . TYR   A 1 224 ? 37.88500 -2.70800  17.02500 1.000 31.87415  ?  376 TYR   A CB   1 
ATOM   1647 C  CG   . TYR   A 1 224 ? 37.09700 -3.95300  16.68900 1.000 34.23232  ?  376 TYR   A CG   1 
ATOM   1648 C  CD1  . TYR   A 1 224 ? 35.93400 -3.87300  15.93300 1.000 34.69167  ?  376 TYR   A CD1  1 
ATOM   1649 C  CD2  . TYR   A 1 224 ? 37.49600 -5.20200  17.14800 1.000 35.65875  ?  376 TYR   A CD2  1 
ATOM   1650 C  CE1  . TYR   A 1 224 ? 35.20500 -4.99700  15.62900 1.000 35.70851  ?  376 TYR   A CE1  1 
ATOM   1651 C  CE2  . TYR   A 1 224 ? 36.76400 -6.33900  16.84500 1.000 36.58195  ?  376 TYR   A CE2  1 
ATOM   1652 C  CZ   . TYR   A 1 224 ? 35.62100 -6.22600  16.08200 1.000 36.83657  ?  376 TYR   A CZ   1 
ATOM   1653 O  OH   . TYR   A 1 224 ? 34.87900 -7.34200  15.76400 1.000 38.50063  ?  376 TYR   A OH   1 
ATOM   1654 N  N    . ALA   A 1 225 ? 37.79000 -2.79500  20.12700 1.000 26.31914  ?  377 ALA   A N    1 
ATOM   1655 C  CA   . ALA   A 1 225 ? 37.56200 -3.51700  21.37300 1.000 26.16653  ?  377 ALA   A CA   1 
ATOM   1656 C  C    . ALA   A 1 225 ? 36.58800 -2.76800  22.26800 1.000 25.48365  ?  377 ALA   A C    1 
ATOM   1657 O  O    . ALA   A 1 225 ? 35.78600 -3.38600  22.97400 1.000 25.76594  ?  377 ALA   A O    1 
ATOM   1658 C  CB   . ALA   A 1 225 ? 38.89700 -3.74500  22.09400 1.000 27.81906  ?  377 ALA   A CB   1 
ATOM   1659 N  N    . LYS   A 1 226 ? 36.65300 -1.43300  22.26400 1.000 24.39474  ?  378 LYS   A N    1 
ATOM   1660 C  CA   . LYS   A 1 226 ? 35.70000 -0.64100  23.03600 1.000 22.41531  ?  378 LYS   A CA   1 
ATOM   1661 C  C    . LYS   A 1 226 ? 34.28900 -0.77800  22.47100 1.000 22.58147  ?  378 LYS   A C    1 
ATOM   1662 O  O    . LYS   A 1 226 ? 33.30700 -0.81900  23.22300 1.000 21.04822  ?  378 LYS   A O    1 
ATOM   1663 C  CB   . LYS   A 1 226 ? 36.13200 0.82600   23.04600 1.000 23.45496  ?  378 LYS   A CB   1 
ATOM   1664 C  CG   . LYS   A 1 226 ? 37.35800 1.12900   23.92900 1.000 26.61011  ?  378 LYS   A CG   1 
ATOM   1665 C  CD   . LYS   A 1 226 ? 37.79500 2.58800   23.79800 1.000 28.55870  ?  378 LYS   A CD   1 
ATOM   1666 C  CE   . LYS   A 1 226 ? 39.12500 2.83300   24.51100 1.000 34.01330  ?  378 LYS   A CE   1 
ATOM   1667 N  NZ   . LYS   A 1 226 ? 39.68400 4.18500   24.22500 1.000 37.01446  ?  378 LYS   A NZ   1 
ATOM   1668 N  N    . MET   A 1 227 ? 34.17100 -0.85800  21.15000 1.000 22.65047  ?  379 MET   A N    1 
ATOM   1669 C  CA   . MET   A 1 227 ? 32.85300 -1.00300  20.54400 1.000 22.47285  ?  379 MET   A CA   1 
ATOM   1670 C  C    . MET   A 1 227 ? 32.26100 -2.37300  20.84600 1.000 22.52853  ?  379 MET   A C    1 
ATOM   1671 O  O    . MET   A 1 227 ? 31.07200 -2.48700  21.16800 1.000 21.42219  ?  379 MET   A O    1 
ATOM   1672 C  CB   . MET   A 1 227 ? 32.95400 -0.75800  19.03900 1.000 22.97897  ?  379 MET   A CB   1 
ATOM   1673 C  CG   . MET   A 1 227 ? 33.16500 0.71000   18.68700 1.000 22.12170  ?  379 MET   A CG   1 
ATOM   1674 S  SD   . MET   A 1 227 ? 33.44800 0.97700   16.93100 1.000 22.27201  ?  379 MET   A SD   1 
ATOM   1675 C  CE   . MET   A 1 227 ? 31.74100 0.77600   16.37500 1.000 18.61901  ?  379 MET   A CE   1 
ATOM   1676 N  N    . ILE   A 1 228 ? 33.08100 -3.42200  20.77600 1.000 25.00849  ?  380 ILE   A N    1 
ATOM   1677 C  CA   . ILE   A 1 228 ? 32.60300 -4.75500  21.12800 1.000 28.40168  ?  380 ILE   A CA   1 
ATOM   1678 C  C    . ILE   A 1 228 ? 32.22500 -4.81600  22.60300 1.000 27.22515  ?  380 ILE   A C    1 
ATOM   1679 O  O    . ILE   A 1 228 ? 31.25000 -5.47400  22.97600 1.000 28.80847  ?  380 ILE   A O    1 
ATOM   1680 C  CB   . ILE   A 1 228 ? 33.65600 -5.81600  20.75600 1.000 33.33552  ?  380 ILE   A CB   1 
ATOM   1681 C  CG1  . ILE   A 1 228 ? 33.83600 -5.87300  19.23500 1.000 33.96903  ?  380 ILE   A CG1  1 
ATOM   1682 C  CG2  . ILE   A 1 228 ? 33.26500 -7.18000  21.30300 1.000 35.36420  ?  380 ILE   A CG2  1 
ATOM   1683 C  CD1  . ILE   A 1 228 ? 32.54900 -6.03500  18.48100 1.000 35.90667  ?  380 ILE   A CD1  1 
ATOM   1684 N  N    . GLN   A 1 229 ? 32.96600 -4.10900  23.46400 1.000 24.43882  ?  381 GLN   A N    1 
ATOM   1685 C  CA   . GLN   A 1 229 ? 32.55800 -4.03700  24.86600 1.000 26.80566  ?  381 GLN   A CA   1 
ATOM   1686 C  C    . GLN   A 1 229 ? 31.14800 -3.46200  25.00100 1.000 26.19656  ?  381 GLN   A C    1 
ATOM   1687 O  O    . GLN   A 1 229 ? 30.36300 -3.90000  25.85400 1.000 24.10403  ?  381 GLN   A O    1 
ATOM   1688 C  CB   . GLN   A 1 229 ? 33.55600 -3.20800  25.67400 1.000 30.89868  ?  381 GLN   A CB   1 
ATOM   1689 C  CG   . GLN   A 1 229 ? 33.21400 -3.12700  27.16000 1.000 34.43174  ?  381 GLN   A CG   1 
ATOM   1690 C  CD   . GLN   A 1 229 ? 33.03800 -4.50300  27.79700 1.000 37.34515  ?  381 GLN   A CD   1 
ATOM   1691 O  OE1  . GLN   A 1 229 ? 33.85300 -5.40000  27.59200 1.000 40.08682  ?  381 GLN   A OE1  1 
ATOM   1692 N  NE2  . GLN   A 1 229 ? 31.95900 -4.67700  28.55100 1.000 36.03024  ?  381 GLN   A NE2  1 
ATOM   1693 N  N    . LYS   A 1 230 ? 30.80300 -2.48800  24.15800 1.000 25.38843  ?  382 LYS   A N    1 
ATOM   1694 C  CA   . LYS   A 1 230 ? 29.46600 -1.91400  24.22600 1.000 23.75264  ?  382 LYS   A CA   1 
ATOM   1695 C  C    . LYS   A 1 230 ? 28.40100 -2.92600  23.82300 1.000 22.38892  ?  382 LYS   A C    1 
ATOM   1696 O  O    . LYS   A 1 230 ? 27.28100 -2.87000  24.33800 1.000 21.90152  ?  382 LYS   A O    1 
ATOM   1697 C  CB   . LYS   A 1 230 ? 29.39300 -0.65400  23.36700 1.000 25.18987  ?  382 LYS   A CB   1 
ATOM   1698 C  CG   . LYS   A 1 230 ? 30.17600 0.52100   23.97300 1.000 27.37016  ?  382 LYS   A CG   1 
ATOM   1699 C  CD   . LYS   A 1 230 ? 29.49600 1.03400   25.23100 1.000 30.55296  ?  382 LYS   A CD   1 
ATOM   1700 C  CE   . LYS   A 1 230 ? 30.42300 1.89100   26.09400 1.000 34.33702  ?  382 LYS   A CE   1 
ATOM   1701 N  NZ   . LYS   A 1 230 ? 31.24900 1.08800   27.05800 1.000 36.97781  ?  382 LYS   A NZ   1 
ATOM   1702 N  N    . LEU   A 1 231 ? 28.73000 -3.86800  22.93100 1.000 22.43689  ?  383 LEU   A N    1 
ATOM   1703 C  CA   . LEU   A 1 231 ? 27.77900 -4.93600  22.60400 1.000 22.40031  ?  383 LEU   A CA   1 
ATOM   1704 C  C    . LEU   A 1 231 ? 27.57000 -5.88400  23.77900 1.000 22.43899  ?  383 LEU   A C    1 
ATOM   1705 O  O    . LEU   A 1 231 ? 26.47200 -6.43400  23.94700 1.000 21.04358  ?  383 LEU   A O    1 
ATOM   1706 C  CB   . LEU   A 1 231 ? 28.25500 -5.73700  21.39300 1.000 22.91404  ?  383 LEU   A CB   1 
ATOM   1707 C  CG   . LEU   A 1 231 ? 28.35100 -5.06900  20.02100 1.000 22.68237  ?  383 LEU   A CG   1 
ATOM   1708 C  CD1  . LEU   A 1 231 ? 28.95700 -6.05200  19.02900 1.000 22.75596  ?  383 LEU   A CD1  1 
ATOM   1709 C  CD2  . LEU   A 1 231 ? 26.96900 -4.61700  19.56900 1.000 22.80998  ?  383 LEU   A CD2  1 
ATOM   1710 N  N    . ALA   A 1 232 ? 28.62000 -6.12000  24.57100 1.000 21.83391  ?  384 ALA   A N    1 
ATOM   1711 C  CA   . ALA   A 1 232 ? 28.46400 -6.88800  25.80000 1.000 23.16370  ?  384 ALA   A CA   1 
ATOM   1712 C  C    . ALA   A 1 232 ? 27.63500 -6.12300  26.82600 1.000 22.66053  ?  384 ALA   A C    1 
ATOM   1713 O  O    . ALA   A 1 232 ? 26.81100 -6.71800  27.53200 1.000 24.09150  ?  384 ALA   A O    1 
ATOM   1714 C  CB   . ALA   A 1 232 ? 29.84100 -7.23900  26.37700 1.000 24.23019  ?  384 ALA   A CB   1 
ATOM   1715 N  N    . ASP   A 1 233 ? 27.85200 -4.80700  26.93900 1.000 20.68230  ?  385 ASP   A N    1 
ATOM   1716 C  CA   . ASP   A 1 233 ? 27.01800 -3.99700  27.81900 1.000 20.35692  ?  385 ASP   A CA   1 
ATOM   1717 C  C    . ASP   A 1 233 ? 25.55400 -4.08000  27.40400 1.000 19.91713  ?  385 ASP   A C    1 
ATOM   1718 O  O    . ASP   A 1 233 ? 24.65800 -4.08100  28.25400 1.000 21.64550  ?  385 ASP   A O    1 
ATOM   1719 C  CB   . ASP   A 1 233 ? 27.46200 -2.53500  27.79800 1.000 21.08536  ?  385 ASP   A CB   1 
ATOM   1720 C  CG   . ASP   A 1 233 ? 28.86000 -2.31600  28.36100 1.000 26.68184  ?  385 ASP   A CG   1 
ATOM   1721 O  OD1  . ASP   A 1 233 ? 29.32600 -1.16300  28.26500 1.000 27.68757  ?  385 ASP   A OD1  1 
ATOM   1722 O  OD2  . ASP   A 1 233 ? 29.48800 -3.26100  28.89400 1.000 26.80961  ?  385 ASP   A OD2  1 
ATOM   1723 N  N    . LEU   A 1 234 ? 25.29600 -4.11700  26.09300 1.000 19.10199  ?  386 LEU   A N    1 
ATOM   1724 C  CA   . LEU   A 1 234 ? 23.91700 -4.17700  25.61500 1.000 19.48154  ?  386 LEU   A CA   1 
ATOM   1725 C  C    . LEU   A 1 234 ? 23.25400 -5.49600  25.99200 1.000 20.07102  ?  386 LEU   A C    1 
ATOM   1726 O  O    . LEU   A 1 234 ? 22.04800 -5.53200  26.27300 1.000 20.36298  ?  386 LEU   A O    1 
ATOM   1727 C  CB   . LEU   A 1 234 ? 23.88100 -3.96600  24.10100 1.000 19.39743  ?  386 LEU   A CB   1 
ATOM   1728 C  CG   . LEU   A 1 234 ? 24.07500 -2.51800  23.64800 1.000 19.94925  ?  386 LEU   A CG   1 
ATOM   1729 C  CD1  . LEU   A 1 234 ? 24.44100 -2.46700  22.16700 1.000 19.68580  ?  386 LEU   A CD1  1 
ATOM   1730 C  CD2  . LEU   A 1 234 ? 22.79800 -1.71000  23.92600 1.000 19.93356  ?  386 LEU   A CD2  1 
ATOM   1731 N  N    . ARG   A 1 235 ? 24.01500 -6.59900  25.99700 1.000 20.66600  ?  387 ARG   A N    1 
ATOM   1732 C  CA   . ARG   A 1 235 ? 23.42400 -7.87100  26.41600 1.000 22.31127  ?  387 ARG   A CA   1 
ATOM   1733 C  C    . ARG   A 1 235 ? 22.92300 -7.79100  27.85200 1.000 23.67979  ?  387 ARG   A C    1 
ATOM   1734 O  O    . ARG   A 1 235 ? 21.84700 -8.30400  28.17400 1.000 24.30445  ?  387 ARG   A O    1 
ATOM   1735 C  CB   . ARG   A 1 235 ? 24.43200 -9.01200  26.27400 1.000 24.25784  ?  387 ARG   A CB   1 
ATOM   1736 C  CG   . ARG   A 1 235 ? 24.96900 -9.20400  24.88400 1.000 25.11081  ?  387 ARG   A CG   1 
ATOM   1737 C  CD   . ARG   A 1 235 ? 23.87400 -9.62700  23.91600 1.000 25.83281  ?  387 ARG   A CD   1 
ATOM   1738 N  NE   . ARG   A 1 235 ? 24.43500 -9.92900  22.60500 1.000 28.14852  ?  387 ARG   A NE   1 
ATOM   1739 C  CZ   . ARG   A 1 235 ? 24.64200 -11.15700 22.13700 1.000 29.78591  ?  387 ARG   A CZ   1 
ATOM   1740 N  NH1  . ARG   A 1 235 ? 24.34000 -12.21500 22.87500 1.000 30.29631  ?  387 ARG   A NH1  1 
ATOM   1741 N  NH2  . ARG   A 1 235 ? 25.16000 -11.32500 20.92800 1.000 30.60400  ?  387 ARG   A NH2  1 
ATOM   1742 N  N    . SER   A 1 236 ? 23.68500 -7.13700  28.72900 1.000 23.77296  ?  388 SER   A N    1 
ATOM   1743 C  CA   . SER   A 1 236 ? 23.26100 -6.99000  30.11800 1.000 24.92045  ?  388 SER   A CA   1 
ATOM   1744 C  C    . SER   A 1 236 ? 22.07400 -6.03700  30.24700 1.000 23.57420  ?  388 SER   A C    1 
ATOM   1745 O  O    . SER   A 1 236 ? 21.16200 -6.27200  31.05200 1.000 21.95030  ?  388 SER   A O    1 
ATOM   1746 C  CB   . SER   A 1 236 ? 24.44100 -6.51400  30.96300 1.000 29.07188  ?  388 SER   A CB   1 
ATOM   1747 O  OG   . SER   A 1 236 ? 23.98200 -6.03300  32.20700 1.000 32.72408  ?  388 SER   A OG   1 
ATOM   1748 N  N    . LEU   A 1 237 ? 22.06900 -4.95200  29.46600 1.000 21.73253  ?  389 LEU   A N    1 
ATOM   1749 C  CA   . LEU   A 1 237 ? 20.91400 -4.06200  29.44800 1.000 19.07757  ?  389 LEU   A CA   1 
ATOM   1750 C  C    . LEU   A 1 237 ? 19.69200 -4.76800  28.87400 1.000 18.43027  ?  389 LEU   A C    1 
ATOM   1751 O  O    . LEU   A 1 237 ? 18.56600 -4.56600  29.34700 1.000 15.32394  ?  389 LEU   A O    1 
ATOM   1752 C  CB   . LEU   A 1 237 ? 21.24000 -2.80000  28.64100 1.000 19.24386  ?  389 LEU   A CB   1 
ATOM   1753 C  CG   . LEU   A 1 237 ? 22.31700 -1.91300  29.28400 1.000 20.53772  ?  389 LEU   A CG   1 
ATOM   1754 C  CD1  . LEU   A 1 237 ? 22.91400 -0.93900  28.27600 1.000 19.44020  ?  389 LEU   A CD1  1 
ATOM   1755 C  CD2  . LEU   A 1 237 ? 21.73200 -1.16800  30.47400 1.000 23.05115  ?  389 LEU   A CD2  1 
ATOM   1756 N  N    . ASN   A 1 238 ? 19.90000 -5.59000  27.84500 1.000 18.60316  ?  390 ASN   A N    1 
ATOM   1757 C  CA   . ASN   A 1 238 ? 18.82500 -6.41400  27.30400 1.000 20.38551  ?  390 ASN   A CA   1 
ATOM   1758 C  C    . ASN   A 1 238 ? 18.22200 -7.30200  28.39100 1.000 22.53617  ?  390 ASN   A C    1 
ATOM   1759 O  O    . ASN   A 1 238 ? 17.00000 -7.34000  28.57100 1.000 22.25016  ?  390 ASN   A O    1 
ATOM   1760 C  CB   . ASN   A 1 238 ? 19.37500 -7.24600  26.14600 1.000 19.08701  ?  390 ASN   A CB   1 
ATOM   1761 C  CG   . ASN   A 1 238 ? 18.29800 -7.96200  25.35900 1.000 20.61634  ?  390 ASN   A CG   1 
ATOM   1762 O  OD1  . ASN   A 1 238 ? 17.22500 -8.26300  25.87100 1.000 19.83761  ?  390 ASN   A OD1  1 
ATOM   1763 N  ND2  . ASN   A 1 238 ? 18.59700 -8.26000  24.10600 1.000 20.36958  ?  390 ASN   A ND2  1 
ATOM   1764 N  N    . GLU   A 1 239 ? 19.07300 -8.01000  29.13800 1.000 24.89570  ?  391 GLU   A N    1 
ATOM   1765 C  CA   . GLU   A 1 239 ? 18.59300 -8.89500  30.19900 1.000 28.15834  ?  391 GLU   A CA   1 
ATOM   1766 C  C    . GLU   A 1 239 ? 17.75400 -8.14100  31.22200 1.000 24.80848  ?  391 GLU   A C    1 
ATOM   1767 O  O    . GLU   A 1 239 ? 16.66400 -8.58800  31.60200 1.000 24.16504  ?  391 GLU   A O    1 
ATOM   1768 C  CB   . GLU   A 1 239 ? 19.77400 -9.56400  30.90000 1.000 33.79823  ?  391 GLU   A CB   1 
ATOM   1769 C  CG   . GLU   A 1 239 ? 20.32800 -10.78800 30.21800 1.000 39.68224  ?  391 GLU   A CG   1 
ATOM   1770 C  CD   . GLU   A 1 239 ? 21.11800 -11.64900 31.18800 1.000 46.32578  ?  391 GLU   A CD   1 
ATOM   1771 O  OE1  . GLU   A 1 239 ? 22.04400 -11.11400 31.83900 1.000 47.61172  ?  391 GLU   A OE1  1 
ATOM   1772 O  OE2  . GLU   A 1 239 ? 20.80500 -12.85300 31.31500 1.000 49.60491  ?  391 GLU   A OE2  1 
ATOM   1773 N  N    . GLU   A 1 240 ? 18.25100 -6.99600  31.69000 1.000 23.51540  ?  392 GLU   A N    1 
ATOM   1774 C  CA   . GLU   A 1 240 ? 17.54500 -6.26100  32.73600 1.000 24.35632  ?  392 GLU   A CA   1 
ATOM   1775 C  C    . GLU   A 1 240 ? 16.24100 -5.65900  32.21300 1.000 23.62822  ?  392 GLU   A C    1 
ATOM   1776 O  O    . GLU   A 1 240 ? 15.21300 -5.70200  32.90500 1.000 25.43986  ?  392 GLU   A O    1 
ATOM   1777 C  CB   . GLU   A 1 240 ? 18.45700 -5.17900  33.32000 1.000 24.46541  ?  392 GLU   A CB   1 
ATOM   1778 C  CG   . GLU   A 1 240 ? 17.83400 -4.38900  34.47600 1.000 27.29111  ?  392 GLU   A CG   1 
ATOM   1779 C  CD   . GLU   A 1 240 ? 17.37900 -5.28400  35.63000 1.000 30.32252  ?  392 GLU   A CD   1 
ATOM   1780 O  OE1  . GLU   A 1 240 ? 16.31000 -5.00900  36.21900 1.000 31.34382  ?  392 GLU   A OE1  1 
ATOM   1781 O  OE2  . GLU   A 1 240 ? 18.09100 -6.26000  35.94900 1.000 31.49590  ?  392 GLU   A OE2  1 
ATOM   1782 N  N    . HIS   A 1 241 ? 16.25300 -5.08800  31.00200 1.000 19.40682  ?  393 HIS   A N    1 
ATOM   1783 C  CA   . HIS   A 1 241 ? 15.00700 -4.54200  30.45800 1.000 17.95412  ?  393 HIS   A CA   1 
ATOM   1784 C  C    . HIS   A 1 241 ? 13.96100 -5.63600  30.28900 1.000 19.58349  ?  393 HIS   A C    1 
ATOM   1785 O  O    . HIS   A 1 241 ? 12.78800 -5.44200  30.63000 1.000 19.30099  ?  393 HIS   A O    1 
ATOM   1786 C  CB   . HIS   A 1 241 ? 15.22600 -3.83400  29.11400 1.000 17.50571  ?  393 HIS   A CB   1 
ATOM   1787 C  CG   . HIS   A 1 241 ? 13.93200 -3.44600  28.44500 1.000 17.48940  ?  393 HIS   A CG   1 
ATOM   1788 N  ND1  . HIS   A 1 241 ? 13.26500 -4.28000  27.57700 1.000 17.26424  ?  393 HIS   A ND1  1 
ATOM   1789 C  CD2  . HIS   A 1 241 ? 13.15700 -2.34300  28.57200 1.000 17.00693  ?  393 HIS   A CD2  1 
ATOM   1790 C  CE1  . HIS   A 1 241 ? 12.13800 -3.70500  27.18800 1.000 17.37561  ?  393 HIS   A CE1  1 
ATOM   1791 N  NE2  . HIS   A 1 241 ? 12.04500 -2.52900  27.78000 1.000 17.04824  ?  393 HIS   A NE2  1 
ATOM   1792 N  N    . SER   A 1 242 ? 14.37300 -6.79800  29.77200 1.000 21.36531  ?  394 SER   A N    1 
ATOM   1793 C  CA   . SER   A 1 242 ? 13.45200 -7.91800  29.60100 1.000 23.42535  ?  394 SER   A CA   1 
ATOM   1794 C  C    . SER   A 1 242 ? 12.84700 -8.34400  30.93400 1.000 23.02847  ?  394 SER   A C    1 
ATOM   1795 O  O    . SER   A 1 242 ? 11.65500 -8.66700  31.01200 1.000 23.07747  ?  394 SER   A O    1 
ATOM   1796 C  CB   . SER   A 1 242 ? 14.18300 -9.09100  28.94400 1.000 26.88955  ?  394 SER   A CB   1 
ATOM   1797 O  OG   . SER   A 1 242 ? 14.68600 -8.71700  27.66900 1.000 29.32201  ?  394 SER   A OG   1 
ATOM   1798 N  N    A LYS   A 1 243 ? 13.65200 -8.34900  31.99800 0.310 23.59966  ?  395 LYS   A N    1 
ATOM   1799 N  N    B LYS   A 1 243 ? 13.66400 -8.37000  31.98700 0.690 23.72303  ?  395 LYS   A N    1 
ATOM   1800 C  CA   A LYS   A 1 243 ? 13.13500 -8.71800  33.31200 0.310 24.58652  ?  395 LYS   A CA   1 
ATOM   1801 C  CA   B LYS   A 1 243 ? 13.17200 -8.70200  33.31900 0.690 24.46614  ?  395 LYS   A CA   1 
ATOM   1802 C  C    A LYS   A 1 243 ? 12.07400 -7.72800  33.77900 0.310 24.00876  ?  395 LYS   A C    1 
ATOM   1803 C  C    B LYS   A 1 243 ? 12.08000 -7.72900  33.75200 0.690 24.01190  ?  395 LYS   A C    1 
ATOM   1804 O  O    A LYS   A 1 243 ? 10.98700 -8.12200  34.21500 0.310 24.57808  ?  395 LYS   A O    1 
ATOM   1805 O  O    B LYS   A 1 243 ? 10.97300 -8.13600  34.11900 0.690 24.42839  ?  395 LYS   A O    1 
ATOM   1806 C  CB   A LYS   A 1 243 ? 14.28200 -8.80500  34.32000 0.310 26.16422  ?  395 LYS   A CB   1 
ATOM   1807 C  CB   B LYS   A 1 243 ? 14.34400 -8.69500  34.30400 0.690 26.13755  ?  395 LYS   A CB   1 
ATOM   1808 C  CG   A LYS   A 1 243 ? 13.83100 -9.11600  35.74200 0.310 28.29716  ?  395 LYS   A CG   1 
ATOM   1809 C  CG   B LYS   A 1 243 ? 14.09000 -9.41000  35.61500 0.690 28.49747  ?  395 LYS   A CG   1 
ATOM   1810 C  CD   A LYS   A 1 243 ? 14.98400 -9.57900  36.64100 0.310 29.69686  ?  395 LYS   A CD   1 
ATOM   1811 C  CD   B LYS   A 1 243 ? 15.36300 -9.46000  36.47100 0.690 29.39874  ?  395 LYS   A CD   1 
ATOM   1812 C  CE   A LYS   A 1 243 ? 16.35000 -9.37700  36.00300 0.310 29.05446  ?  395 LYS   A CE   1 
ATOM   1813 C  CE   B LYS   A 1 243 ? 15.02600 -9.57700  37.95600 0.690 31.26452  ?  395 LYS   A CE   1 
ATOM   1814 N  NZ   A LYS   A 1 243 ? 16.86300 -10.61600 35.35400 0.310 29.68803  ?  395 LYS   A NZ   1 
ATOM   1815 N  NZ   B LYS   A 1 243 ? 16.19900 -10.01700 38.77700 0.690 32.03103  ?  395 LYS   A NZ   1 
ATOM   1816 N  N    . GLN   A 1 244 ? 12.36500 -6.42900  33.68000 1.000 22.44634  ?  396 GLN   A N    1 
ATOM   1817 C  CA   . GLN   A 1 244 ? 11.38500 -5.42800  34.09100 1.000 21.51614  ?  396 GLN   A CA   1 
ATOM   1818 C  C    . GLN   A 1 244 ? 10.18200 -5.37800  33.14200 1.000 22.39912  ?  396 GLN   A C    1 
ATOM   1819 O  O    . GLN   A 1 244 ? 9.04000  -5.17500  33.58200 1.000 23.59636  ?  396 GLN   A O    1 
ATOM   1820 C  CB   . GLN   A 1 244 ? 12.07700 -4.07200  34.19100 1.000 20.64362  ?  396 GLN   A CB   1 
ATOM   1821 C  CG   . GLN   A 1 244 ? 13.29600 -4.12000  35.13300 1.000 23.58062  ?  396 GLN   A CG   1 
ATOM   1822 C  CD   . GLN   A 1 244 ? 13.79200 -2.74900  35.54000 1.000 25.21351  ?  396 GLN   A CD   1 
ATOM   1823 O  OE1  . GLN   A 1 244 ? 13.15300 -1.73100  35.25500 1.000 25.33997  ?  396 GLN   A OE1  1 
ATOM   1824 N  NE2  . GLN   A 1 244 ? 14.93100 -2.71200  36.23000 1.000 25.82100  ?  396 GLN   A NE2  1 
ATOM   1825 N  N    . TYR   A 1 245 ? 10.40800 -5.57700  31.84300 1.000 19.56803  ?  397 TYR   A N    1 
ATOM   1826 C  CA   . TYR   A 1 245 ? 9.29000  -5.59200  30.90400 1.000 22.17507  ?  397 TYR   A CA   1 
ATOM   1827 C  C    . TYR   A 1 245 ? 8.31900  -6.72400  31.21700 1.000 23.63560  ?  397 TYR   A C    1 
ATOM   1828 O  O    . TYR   A 1 245 ? 7.10100  -6.53900  31.14800 1.000 23.53019  ?  397 TYR   A O    1 
ATOM   1829 C  CB   . TYR   A 1 245 ? 9.78700  -5.71900  29.46900 1.000 19.80688  ?  397 TYR   A CB   1 
ATOM   1830 C  CG   . TYR   A 1 245 ? 8.64500  -5.86100  28.48000 1.000 20.16890  ?  397 TYR   A CG   1 
ATOM   1831 C  CD1  . TYR   A 1 245 ? 7.98900  -4.74500  27.98400 1.000 19.27682  ?  397 TYR   A CD1  1 
ATOM   1832 C  CD2  . TYR   A 1 245 ? 8.20200  -7.11300  28.07500 1.000 21.05058  ?  397 TYR   A CD2  1 
ATOM   1833 C  CE1  . TYR   A 1 245 ? 6.92100  -4.87300  27.08600 1.000 19.55013  ?  397 TYR   A CE1  1 
ATOM   1834 C  CE2  . TYR   A 1 245 ? 7.14600  -7.24800  27.19500 1.000 21.06726  ?  397 TYR   A CE2  1 
ATOM   1835 C  CZ   . TYR   A 1 245 ? 6.51300  -6.13000  26.70200 1.000 21.09015  ?  397 TYR   A CZ   1 
ATOM   1836 O  OH   . TYR   A 1 245 ? 5.47000  -6.28700  25.81700 1.000 22.06688  ?  397 TYR   A OH   1 
ATOM   1837 N  N    . ARG   A 1 246 ? 8.84400  -7.91500  31.51500 1.000 25.90413  ?  398 ARG   A N    1 
ATOM   1838 C  CA   . ARG   A 1 246 ? 7.98600  -9.02800  31.90000 1.000 30.74599  ?  398 ARG   A CA   1 
ATOM   1839 C  C    . ARG   A 1 246 ? 7.19000  -8.69600  33.15700 1.000 31.03218  ?  398 ARG   A C    1 
ATOM   1840 O  O    . ARG   A 1 246 ? 5.99000  -8.99100  33.23800 1.000 30.37207  ?  398 ARG   A O    1 
ATOM   1841 C  CB   . ARG   A 1 246 ? 8.82600  -10.28400 32.11400 1.000 35.62778  ?  398 ARG   A CB   1 
ATOM   1842 C  CG   . ARG   A 1 246 ? 9.13100  -11.05000 30.84100 1.000 40.19273  ?  398 ARG   A CG   1 
ATOM   1843 C  CD   . ARG   A 1 246 ? 9.78800  -12.40000 31.13100 1.000 44.95774  ?  398 ARG   A CD   1 
ATOM   1844 N  NE   . ARG   A 1 246 ? 11.11700 -12.26600 31.72600 1.000 48.39578  ?  398 ARG   A NE   1 
ATOM   1845 C  CZ   . ARG   A 1 246 ? 12.23800 -12.10600 31.02500 1.000 49.68231  ?  398 ARG   A CZ   1 
ATOM   1846 N  NH1  . ARG   A 1 246 ? 12.18600 -12.05600 29.69700 1.000 49.47576  ?  398 ARG   A NH1  1 
ATOM   1847 N  NH2  . ARG   A 1 246 ? 13.40800 -11.99200 31.64700 1.000 49.28718  ?  398 ARG   A NH2  1 
ATOM   1848 N  N    . SER   A 1 247 ? 7.83900  -8.07100  34.14600 1.000 29.16867  ?  399 SER   A N    1 
ATOM   1849 C  CA   . SER   A 1 247 ? 7.12400  -7.67200  35.35200 1.000 30.71995  ?  399 SER   A CA   1 
ATOM   1850 C  C    . SER   A 1 247 ? 6.03400  -6.64800  35.03800 1.000 28.51526  ?  399 SER   A C    1 
ATOM   1851 O  O    . SER   A 1 247 ? 4.90300  -6.76900  35.51900 1.000 29.92130  ?  399 SER   A O    1 
ATOM   1852 C  CB   . SER   A 1 247 ? 8.10800  -7.11900  36.38400 1.000 34.28588  ?  399 SER   A CB   1 
ATOM   1853 O  OG   . SER   A 1 247 ? 7.47700  -6.19800  37.25600 1.000 38.14771  ?  399 SER   A OG   1 
ATOM   1854 N  N    . LEU   A 1 248 ? 6.35600  -5.62700  34.23900 1.000 26.21080  ?  400 LEU   A N    1 
ATOM   1855 C  CA   . LEU   A 1 248 ? 5.37200  -4.59500  33.91200 1.000 28.24629  ?  400 LEU   A CA   1 
ATOM   1856 C  C    . LEU   A 1 248 ? 4.24700  -5.15200  33.05000 1.000 29.50054  ?  400 LEU   A C    1 
ATOM   1857 O  O    . LEU   A 1 248 ? 3.06800  -4.89900  33.31900 1.000 30.59134  ?  400 LEU   A O    1 
ATOM   1858 C  CB   . LEU   A 1 248 ? 6.04600  -3.42000  33.20200 1.000 27.31703  ?  400 LEU   A CB   1 
ATOM   1859 C  CG   . LEU   A 1 248 ? 6.99700  -2.61200  34.08400 1.000 28.27058  ?  400 LEU   A CG   1 
ATOM   1860 C  CD1  . LEU   A 1 248 ? 7.94400  -1.78400  33.23300 1.000 27.17525  ?  400 LEU   A CD1  1 
ATOM   1861 C  CD2  . LEU   A 1 248 ? 6.20700  -1.72800  35.03500 1.000 28.71164  ?  400 LEU   A CD2  1 
ATOM   1862 N  N    . SER   A 1 249 ? 4.58800  -5.90300  32.00200 1.000 29.85724  ?  401 SER   A N    1 
ATOM   1863 C  CA   . SER   A 1 249 ? 3.56800  -6.37300  31.07000 1.000 30.05726  ?  401 SER   A CA   1 
ATOM   1864 C  C    . SER   A 1 249 ? 2.72100  -7.50300  31.63900 1.000 31.52935  ?  401 SER   A C    1 
ATOM   1865 O  O    . SER   A 1 249 ? 1.65900  -7.79900  31.08400 1.000 31.90222  ?  401 SER   A O    1 
ATOM   1866 C  CB   . SER   A 1 249 ? 4.21300  -6.82500  29.75800 1.000 28.66855  ?  401 SER   A CB   1 
ATOM   1867 O  OG   . SER   A 1 249 ? 5.04000  -7.95800  29.95500 1.000 30.35928  ?  401 SER   A OG   1 
ATOM   1868 N  N    . PHE   A 1 250 ? 3.16500  -8.14200  32.72000 1.000 32.39186  ?  402 PHE   A N    1 
ATOM   1869 C  CA   . PHE   A 1 250 ? 2.36100  -9.18600  33.34700 1.000 34.80080  ?  402 PHE   A CA   1 
ATOM   1870 C  C    . PHE   A 1 250 ? 1.07700  -8.62500  33.93700 1.000 33.98889  ?  402 PHE   A C    1 
ATOM   1871 O  O    . PHE   A 1 250 ? 0.09700  -9.35800  34.10000 1.000 33.81828  ?  402 PHE   A O    1 
ATOM   1872 C  CB   . PHE   A 1 250 ? 3.16600  -9.89400  34.43600 1.000 39.31355  ?  402 PHE   A CB   1 
ATOM   1873 C  CG   . PHE   A 1 250 ? 2.47400  -11.08700 35.02400 1.000 46.04864  ?  402 PHE   A CG   1 
ATOM   1874 C  CD1  . PHE   A 1 250 ? 1.93800  -11.03300 36.30200 1.000 49.96830  ?  402 PHE   A CD1  1 
ATOM   1875 C  CD2  . PHE   A 1 250 ? 2.35600  -12.26300 34.30200 1.000 48.27838  ?  402 PHE   A CD2  1 
ATOM   1876 C  CE1  . PHE   A 1 250 ? 1.29700  -12.13200 36.84900 1.000 52.93365  ?  402 PHE   A CE1  1 
ATOM   1877 C  CE2  . PHE   A 1 250 ? 1.71700  -13.36500 34.84200 1.000 51.03038  ?  402 PHE   A CE2  1 
ATOM   1878 C  CZ   . PHE   A 1 250 ? 1.18800  -13.29900 36.11700 1.000 53.30238  ?  402 PHE   A CZ   1 
ATOM   1879 N  N    . GLN   A 1 251 ? 1.06600  -7.34300  34.27900 1.000 31.51103  ?  403 GLN   A N    1 
ATOM   1880 C  CA   . GLN   A 1 251 ? -0.12900 -6.72700  34.81400 1.000 30.13662  ?  403 GLN   A CA   1 
ATOM   1881 C  C    . GLN   A 1 251 ? -1.00000 -6.25100  33.66200 1.000 28.04553  ?  403 GLN   A C    1 
ATOM   1882 O  O    . GLN   A 1 251 ? -0.53300 -5.45500  32.83300 1.000 24.05228  ?  403 GLN   A O    1 
ATOM   1883 C  CB   . GLN   A 1 251 ? 0.22600  -5.58300  35.74300 1.000 32.60895  ?  403 GLN   A CB   1 
ATOM   1884 C  CG   . GLN   A 1 251 ? 1.31600  -5.96600  36.76100 1.000 38.86575  ?  403 GLN   A CG   1 
ATOM   1885 C  CD   . GLN   A 1 251 ? 0.86200  -7.05700  37.72900 1.000 45.84304  ?  403 GLN   A CD   1 
ATOM   1886 O  OE1  . GLN   A 1 251 ? 1.68400  -7.75400  38.32600 1.000 49.14363  ?  403 GLN   A OE1  1 
ATOM   1887 N  NE2  . GLN   A 1 251 ? -0.45200 -7.20200  37.89000 1.000 48.67070  ?  403 GLN   A NE2  1 
ATOM   1888 N  N    . PRO   A 1 252 ? -2.24500 -6.72500  33.55900 1.000 28.97600  ?  404 PRO   A N    1 
ATOM   1889 C  CA   . PRO   A 1 252 ? -3.03700 -6.44600  32.34900 1.000 28.71136  ?  404 PRO   A CA   1 
ATOM   1890 C  C    . PRO   A 1 252 ? -3.26500 -4.96700  32.10900 1.000 30.54260  ?  404 PRO   A C    1 
ATOM   1891 O  O    . PRO   A 1 252 ? -3.27100 -4.52500  30.95400 1.000 31.61250  ?  404 PRO   A O    1 
ATOM   1892 C  CB   . PRO   A 1 252 ? -4.35600 -7.18800  32.61400 1.000 29.76568  ?  404 PRO   A CB   1 
ATOM   1893 C  CG   . PRO   A 1 252 ? -4.02700 -8.21700  33.66000 1.000 31.27417  ?  404 PRO   A CG   1 
ATOM   1894 C  CD   . PRO   A 1 252 ? -2.94600 -7.60400  34.51000 1.000 30.82679  ?  404 PRO   A CD   1 
ATOM   1895 N  N    . GLU   A 1 253 ? -3.43800 -4.18200  33.17300 1.000 32.34945  ?  405 GLU   A N    1 
ATOM   1896 C  CA   . GLU   A 1 253 ? -3.69800 -2.75800  33.00400 1.000 33.96944  ?  405 GLU   A CA   1 
ATOM   1897 C  C    . GLU   A 1 253 ? -2.50700 -2.01800  32.40600 1.000 31.50515  ?  405 GLU   A C    1 
ATOM   1898 O  O    . GLU   A 1 253 ? -2.70000 -0.97000  31.78200 1.000 30.77752  ?  405 GLU   A O    1 
ATOM   1899 C  CB   . GLU   A 1 253 ? -4.10600 -2.13800  34.34300 1.000 38.99587  ?  405 GLU   A CB   1 
ATOM   1900 C  CG   . GLU   A 1 253 ? -2.98400 -2.01600  35.37500 1.000 44.19153  ?  405 GLU   A CG   1 
ATOM   1901 C  CD   . GLU   A 1 253 ? -2.76400 -3.28000  36.20900 1.000 48.20868  ?  405 GLU   A CD   1 
ATOM   1902 O  OE1  . GLU   A 1 253 ? -3.43800 -4.30400  35.96200 1.000 48.22897  ?  405 GLU   A OE1  1 
ATOM   1903 O  OE2  . GLU   A 1 253 ? -1.91300 -3.23900  37.12800 1.000 51.42788  ?  405 GLU   A OE2  1 
ATOM   1904 N  N    . ASN   A 1 254 ? -1.28600 -2.53700  32.58300 1.000 28.83625  ?  406 ASN   A N    1 
ATOM   1905 C  CA   . ASN   A 1 254 ? -0.12500 -1.97900  31.89800 1.000 27.12451  ?  406 ASN   A CA   1 
ATOM   1906 C  C    . ASN   A 1 254 ? -0.08100 -2.44300  30.45200 1.000 25.35406  ?  406 ASN   A C    1 
ATOM   1907 O  O    . ASN   A 1 254 ? 0.15500  -1.64200  29.53900 1.000 23.67939  ?  406 ASN   A O    1 
ATOM   1908 C  CB   . ASN   A 1 254 ? 1.17100  -2.39000  32.60500 1.000 27.75645  ?  406 ASN   A CB   1 
ATOM   1909 C  CG   . ASN   A 1 254 ? 1.38700  -1.65400  33.92100 1.000 32.22515  ?  406 ASN   A CG   1 
ATOM   1910 O  OD1  . ASN   A 1 254 ? 0.84400  -0.57000  34.14100 1.000 34.52897  ?  406 ASN   A OD1  1 
ATOM   1911 N  ND2  . ASN   A 1 254 ? 2.18100  -2.25200  34.80800 1.000 31.33738  ?  406 ASN   A ND2  1 
ATOM   1912 N  N    . SER   A 1 255 ? -0.28800 -3.74700  30.23700 1.000 26.53041  ?  407 SER   A N    1 
ATOM   1913 C  CA   . SER   A 1 255 ? -0.30800 -4.30000  28.88900 1.000 26.57111  ?  407 SER   A CA   1 
ATOM   1914 C  C    . SER   A 1 255 ? -1.33800 -3.60500  28.01900 1.000 24.70010  ?  407 SER   A C    1 
ATOM   1915 O  O    . SER   A 1 255 ? -1.14000 -3.48200  26.80600 1.000 23.65312  ?  407 SER   A O    1 
ATOM   1916 C  CB   . SER   A 1 255 ? -0.59200 -5.80000  28.94300 1.000 30.52214  ?  407 SER   A CB   1 
ATOM   1917 O  OG   . SER   A 1 255 ? 0.60900  -6.53600  28.99300 1.000 34.10249  ?  407 SER   A OG   1 
ATOM   1918 N  N    . MET   A 1 256 ? -2.43000 -3.12800  28.62500 1.000 22.88934  ?  408 MET   A N    1 
ATOM   1919 C  CA   . MET   A 1 256 ? -3.47300 -2.45200  27.86100 1.000 24.93438  ?  408 MET   A CA   1 
ATOM   1920 C  C    . MET   A 1 256 ? -2.94600 -1.19900  27.18900 1.000 24.49321  ?  408 MET   A C    1 
ATOM   1921 O  O    . MET   A 1 256 ? -3.47300 -0.78200  26.14700 1.000 23.07666  ?  408 MET   A O    1 
ATOM   1922 C  CB   . MET   A 1 256 ? -4.64200 -2.06500  28.77200 1.000 25.68317  ?  408 MET   A CB   1 
ATOM   1923 C  CG   . MET   A 1 256 ? -5.70500 -3.09500  28.93800 1.000 31.08087  ?  408 MET   A CG   1 
ATOM   1924 S  SD   . MET   A 1 256 ? -7.23500 -2.27800  29.44800 1.000 35.15801  ?  408 MET   A SD   1 
ATOM   1925 C  CE   . MET   A 1 256 ? -6.68000 -1.26400  30.80800 1.000 33.78022  ?  408 MET   A CE   1 
ATOM   1926 N  N    . LYS   A 1 257 ? -1.93000 -0.57600  27.79100 1.000 22.27291  ?  409 LYS   A N    1 
ATOM   1927 C  CA   . LYS   A 1 257 ? -1.33900 0.67100   27.32400 1.000 22.68224  ?  409 LYS   A CA   1 
ATOM   1928 C  C    . LYS   A 1 257 ? -0.21600 0.46200   26.32400 1.000 19.91604  ?  409 LYS   A C    1 
ATOM   1929 O  O    . LYS   A 1 257 ? 0.30500  1.44600   25.78800 1.000 18.83217  ?  409 LYS   A O    1 
ATOM   1930 C  CB   . LYS   A 1 257 ? -0.78700 1.46900   28.51300 1.000 27.00642  ?  409 LYS   A CB   1 
ATOM   1931 C  CG   . LYS   A 1 257 ? -1.81600 1.81000   29.57100 1.000 32.72711  ?  409 LYS   A CG   1 
ATOM   1932 C  CD   . LYS   A 1 257 ? -2.74100 2.89900   29.06500 1.000 37.17298  ?  409 LYS   A CD   1 
ATOM   1933 C  CE   . LYS   A 1 257 ? -3.73800 3.32200   30.13500 1.000 42.72195  ?  409 LYS   A CE   1 
ATOM   1934 N  NZ   . LYS   A 1 257 ? -4.29300 4.67700   29.87200 1.000 44.56600  ?  409 LYS   A NZ   1 
ATOM   1935 N  N    . LEU   A 1 258 ? 0.19500  -0.77900  26.09700 1.000 18.71640  ?  410 LEU   A N    1 
ATOM   1936 C  CA   . LEU   A 1 258 ? 1.23800  -1.07700  25.13500 1.000 16.60460  ?  410 LEU   A CA   1 
ATOM   1937 C  C    . LEU   A 1 258 ? 0.64100  -1.07200  23.72500 1.000 18.26669  ?  410 LEU   A C    1 
ATOM   1938 O  O    . LEU   A 1 258 ? -0.56200 -0.88700  23.53800 1.000 19.07700  ?  410 LEU   A O    1 
ATOM   1939 C  CB   . LEU   A 1 258 ? 1.89300  -2.40900  25.48800 1.000 18.28158  ?  410 LEU   A CB   1 
ATOM   1940 C  CG   . LEU   A 1 258 ? 2.56900  -2.45800  26.87200 1.000 18.19605  ?  410 LEU   A CG   1 
ATOM   1941 C  CD1  . LEU   A 1 258 ? 3.36200  -3.74600  27.06200 1.000 16.00801  ?  410 LEU   A CD1  1 
ATOM   1942 C  CD2  . LEU   A 1 258 ? 3.46300  -1.23800  27.07800 1.000 18.15051  ?  410 LEU   A CD2  1 
ATOM   1943 N  N    . THR   A 1 259 ? 1.48300  -1.25100  22.71300 1.000 17.67464  ?  411 THR   A N    1 
ATOM   1944 C  CA   . THR   A 1 259 ? 0.94800  -1.36200  21.36300 1.000 18.21653  ?  411 THR   A CA   1 
ATOM   1945 C  C    . THR   A 1 259 ? 0.99900  -2.80800  20.90700 1.000 16.92229  ?  411 THR   A C    1 
ATOM   1946 O  O    . THR   A 1 259 ? 1.71700  -3.62500  21.48600 1.000 16.97641  ?  411 THR   A O    1 
ATOM   1947 C  CB   . THR   A 1 259 ? 1.74800  -0.49600  20.38300 1.000 19.77437  ?  411 THR   A CB   1 
ATOM   1948 O  OG1  . THR   A 1 259 ? 3.01400  -1.10900  20.16500 1.000 20.65242  ?  411 THR   A OG1  1 
ATOM   1949 C  CG2  . THR   A 1 259 ? 1.97200  0.90300   20.93600 1.000 21.36894  ?  411 THR   A CG2  1 
ATOM   1950 N  N    . PRO   A 1 260 ? 0.24800  -3.17300  19.86400 1.000 18.14529  ?  412 PRO   A N    1 
ATOM   1951 C  CA   . PRO   A 1 260 ? 0.32700  -4.56300  19.38400 1.000 17.46619  ?  412 PRO   A CA   1 
ATOM   1952 C  C    . PRO   A 1 260 ? 1.71600  -4.96600  18.91800 1.000 16.38569  ?  412 PRO   A C    1 
ATOM   1953 O  O    . PRO   A 1 260 ? 2.13500  -6.10200  19.16500 1.000 16.55188  ?  412 PRO   A O    1 
ATOM   1954 C  CB   . PRO   A 1 260 ? -0.70300 -4.59200  18.24200 1.000 19.77241  ?  412 PRO   A CB   1 
ATOM   1955 C  CG   . PRO   A 1 260 ? -1.68300 -3.52100  18.61100 1.000 20.34943  ?  412 PRO   A CG   1 
ATOM   1956 C  CD   . PRO   A 1 260 ? -0.82400 -2.42100  19.18900 1.000 18.44678  ?  412 PRO   A CD   1 
ATOM   1957 N  N    . LEU   A 1 261 ? 2.45900  -4.06400  18.26800 1.000 15.23710  ?  413 LEU   A N    1 
ATOM   1958 C  CA   . LEU   A 1 261 ? 3.80500  -4.42500  17.83000 1.000 15.80018  ?  413 LEU   A CA   1 
ATOM   1959 C  C    . LEU   A 1 261 ? 4.73100  -4.64700  19.02400 1.000 16.09485  ?  413 LEU   A C    1 
ATOM   1960 O  O    . LEU   A 1 261 ? 5.51700  -5.60100  19.03200 1.000 17.96984  ?  413 LEU   A O    1 
ATOM   1961 C  CB   . LEU   A 1 261 ? 4.37100  -3.35600  16.88700 1.000 15.53654  ?  413 LEU   A CB   1 
ATOM   1962 C  CG   . LEU   A 1 261 ? 5.77800  -3.64400  16.31600 1.000 16.95528  ?  413 LEU   A CG   1 
ATOM   1963 C  CD1  . LEU   A 1 261 ? 5.77400  -4.88800  15.42500 1.000 17.16144  ?  413 LEU   A CD1  1 
ATOM   1964 C  CD2  . LEU   A 1 261 ? 6.32400  -2.44300  15.55300 1.000 15.37848  ?  413 LEU   A CD2  1 
ATOM   1965 N  N    . VAL   A 1 262 ? 4.64200  -3.79000  20.04700 1.000 15.27063  ?  414 VAL   A N    1 
ATOM   1966 C  CA   . VAL   A 1 262 ? 5.45500  -3.97600  21.25400 1.000 16.19215  ?  414 VAL   A CA   1 
ATOM   1967 C  C    . VAL   A 1 262 ? 5.17800  -5.34000  21.87800 1.000 17.94006  ?  414 VAL   A C    1 
ATOM   1968 O  O    . VAL   A 1 262 ? 6.10400  -6.08100  22.24200 1.000 19.52724  ?  414 VAL   A O    1 
ATOM   1969 C  CB   . VAL   A 1 262 ? 5.20400  -2.82500  22.25000 1.000 16.61392  ?  414 VAL   A CB   1 
ATOM   1970 C  CG1  . VAL   A 1 262 ? 5.72600  -3.18700  23.67500 1.000 17.46193  ?  414 VAL   A CG1  1 
ATOM   1971 C  CG2  . VAL   A 1 262 ? 5.87000  -1.53900  21.74500 1.000 15.44845  ?  414 VAL   A CG2  1 
ATOM   1972 N  N    . LEU   A 1 263 ? 3.90100  -5.70900  21.97500 1.000 19.62469  ?  415 LEU   A N    1 
ATOM   1973 C  CA   . LEU   A 1 263 ? 3.53300  -6.98900  22.56900 1.000 19.68732  ?  415 LEU   A CA   1 
ATOM   1974 C  C    . LEU   A 1 263 ? 4.06400  -8.15500  21.74900 1.000 20.57980  ?  415 LEU   A C    1 
ATOM   1975 O  O    . LEU   A 1 263 ? 4.48400  -9.17800  22.30300 1.000 21.65648  ?  415 LEU   A O    1 
ATOM   1976 C  CB   . LEU   A 1 263 ? 2.00800  -7.08000  22.69600 1.000 19.17051  ?  415 LEU   A CB   1 
ATOM   1977 C  CG   . LEU   A 1 263 ? 1.40600  -6.25000  23.82600 1.000 19.13285  ?  415 LEU   A CG   1 
ATOM   1978 C  CD1  . LEU   A 1 263 ? -0.12900 -6.28700  23.76000 1.000 20.06846  ?  415 LEU   A CD1  1 
ATOM   1979 C  CD2  . LEU   A 1 263 ? 1.92400  -6.74800  25.17100 1.000 17.54764  ?  415 LEU   A CD2  1 
ATOM   1980 N  N    . GLU   A 1 264 ? 4.03300  -8.03100  20.42400 1.000 20.43521  ?  416 GLU   A N    1 
ATOM   1981 C  CA   . GLU   A 1 264 ? 4.53500  -9.10800  19.57500 1.000 22.25593  ?  416 GLU   A CA   1 
ATOM   1982 C  C    . GLU   A 1 264 ? 6.05300  -9.24500  19.66900 1.000 23.21000  ?  416 GLU   A C    1 
ATOM   1983 O  O    . GLU   A 1 264 ? 6.57800  -10.36300 19.73100 1.000 24.85854  ?  416 GLU   A O    1 
ATOM   1984 C  CB   . GLU   A 1 264 ? 4.12500  -8.85800  18.12800 1.000 23.62161  ?  416 GLU   A CB   1 
ATOM   1985 C  CG   . GLU   A 1 264 ? 4.33300  -10.05000 17.21600 1.000 25.43927  ?  416 GLU   A CG   1 
ATOM   1986 C  CD   . GLU   A 1 264 ? 4.12700  -9.68200  15.76700 1.000 26.24840  ?  416 GLU   A CD   1 
ATOM   1987 O  OE1  . GLU   A 1 264 ? 5.12500  -9.37300  15.08300 1.000 26.28712  ?  416 GLU   A OE1  1 
ATOM   1988 O  OE2  . GLU   A 1 264 ? 2.96400  -9.68900  15.31700 1.000 26.28141  ?  416 GLU   A OE2  1 
ATOM   1989 N  N    . VAL   A 1 265 ? 6.77800  -8.13100  19.65000 1.000 21.06871  ?  417 VAL   A N    1 
ATOM   1990 C  CA   . VAL   A 1 265 ? 8.24200  -8.18700  19.61300 1.000 21.67273  ?  417 VAL   A CA   1 
ATOM   1991 C  C    . VAL   A 1 265 ? 8.82900  -8.36400  21.00700 1.000 22.87079  ?  417 VAL   A C    1 
ATOM   1992 O  O    . VAL   A 1 265 ? 9.64900  -9.25800  21.23800 1.000 23.96832  ?  417 VAL   A O    1 
ATOM   1993 C  CB   . VAL   A 1 265 ? 8.80400  -6.92900  18.91300 1.000 20.91923  ?  417 VAL   A CB   1 
ATOM   1994 C  CG1  . VAL   A 1 265 ? 10.32100 -6.91500  18.95400 1.000 22.31224  ?  417 VAL   A CG1  1 
ATOM   1995 C  CG2  . VAL   A 1 265 ? 8.30100  -6.84900  17.47200 1.000 22.03552  ?  417 VAL   A CG2  1 
ATOM   1996 N  N    . PHE   A 1 266 ? 8.43300  -7.51900  21.96400 1.000 22.55221  ?  418 PHE   A N    1 
ATOM   1997 C  CA   . PHE   A 1 266 ? 9.00100  -7.63900  23.30300 1.000 24.69705  ?  418 PHE   A CA   1 
ATOM   1998 C  C    . PHE   A 1 266 ? 8.39300  -8.79600  24.08500 1.000 27.75465  ?  418 PHE   A C    1 
ATOM   1999 O  O    . PHE   A 1 266 ? 9.05300  -9.34800  24.97000 1.000 27.23370  ?  418 PHE   A O    1 
ATOM   2000 C  CB   . PHE   A 1 266 ? 8.82800  -6.33700  24.09400 1.000 23.64621  ?  418 PHE   A CB   1 
ATOM   2001 C  CG   . PHE   A 1 266 ? 9.76000  -5.23200  23.67200 1.000 20.78247  ?  418 PHE   A CG   1 
ATOM   2002 C  CD1  . PHE   A 1 266 ? 9.72900  -4.00300  24.31700 1.000 19.69397  ?  418 PHE   A CD1  1 
ATOM   2003 C  CD2  . PHE   A 1 266 ? 10.65900 -5.41800  22.62900 1.000 20.14724  ?  418 PHE   A CD2  1 
ATOM   2004 C  CE1  . PHE   A 1 266 ? 10.57300 -2.97900  23.92800 1.000 19.47992  ?  418 PHE   A CE1  1 
ATOM   2005 C  CE2  . PHE   A 1 266 ? 11.50000 -4.40700  22.23500 1.000 20.37019  ?  418 PHE   A CE2  1 
ATOM   2006 C  CZ   . PHE   A 1 266 ? 11.46500 -3.18400  22.88900 1.000 19.96395  ?  418 PHE   A CZ   1 
ATOM   2007 N  N    . GLY   A 1 267 ? 7.15200  -9.17200  23.79300 1.000 29.11550  ?  419 GLY   A N    1 
ATOM   2008 C  CA   . GLY   A 1 267 ? 6.59200  -10.33800 24.44200 1.000 31.05230  ?  419 GLY   A CA   1 
ATOM   2009 C  C    . GLY   A 1 267 ? 5.20800  -10.12800 25.01400 1.000 33.81656  ?  419 GLY   A C    1 
ATOM   2010 O  O    . GLY   A 1 267 ? 4.81600  -8.99700  25.32700 1.000 32.86349  ?  419 GLY   A O    1 
ATOM   2011 N  N    . ASN   A 1 268 ? 4.46800  -11.22500 25.16400 1.000 36.15589  ?  420 ASN   A N    1 
ATOM   2012 C  CA   . ASN   A 1 268 ? 3.08600  -11.19100 25.62200 1.000 37.88530  ?  420 ASN   A CA   1 
ATOM   2013 C  C    . ASN   A 1 268 ? 2.78000  -12.41900 26.48500 1.000 39.59420  ?  420 ASN   A C    1 
ATOM   2014 O  O    . ASN   A 1 268 ? 3.22200  -12.51400 27.63800 1.000 41.05520  ?  420 ASN   A O    1 
ATOM   2015 C  CB   . ASN   A 1 268 ? 2.14000  -11.11700 24.41400 1.000 38.68197  ?  420 ASN   A CB   1 
ATOM   2016 C  CG   . ASN   A 1 268 ? 0.70700  -10.79200 24.80100 1.000 41.25478  ?  420 ASN   A CG   1 
ATOM   2017 O  OD1  . ASN   A 1 268 ? -0.15800 -10.64400 23.93400 1.000 42.67224  ?  420 ASN   A OD1  1 
ATOM   2018 N  ND2  . ASN   A 1 268 ? 0.44600  -10.68000 26.10000 1.000 41.99890  ?  420 ASN   A ND2  1 
ATOM   2019 N  N    . LYS   B 2 1   ? 4.13100  -18.73800 19.10000 1.000 76.75594  ?  625 LYS   C N    1 
ATOM   2020 C  CA   . LYS   B 2 1   ? 4.45500  -17.37000 18.74900 1.000 76.12854  ?  625 LYS   C CA   1 
ATOM   2021 C  C    . LYS   B 2 1   ? 4.51200  -17.11800 17.25600 1.000 72.45460  ?  625 LYS   C C    1 
ATOM   2022 O  O    . LYS   B 2 1   ? 5.55000  -17.31900 16.60700 1.000 73.01098  ?  625 LYS   C O    1 
ATOM   2023 C  CB   . LYS   B 2 1   ? 5.79100  -16.93900 19.38100 1.000 78.75924  ?  625 LYS   C CB   1 
ATOM   2024 C  CG   . LYS   B 2 1   ? 5.79800  -16.98700 20.90100 1.000 80.77750  ?  625 LYS   C CG   1 
ATOM   2025 C  CD   . LYS   B 2 1   ? 7.17500  -17.26700 21.48400 1.000 81.89651  ?  625 LYS   C CD   1 
ATOM   2026 C  CE   . LYS   B 2 1   ? 7.04700  -17.97900 22.81100 1.000 82.83312  ?  625 LYS   C CE   1 
ATOM   2027 N  NZ   . LYS   B 2 1   ? 8.37700  -18.43200 23.27900 1.000 83.15197  ?  625 LYS   C NZ   1 
ATOM   2028 N  N    . ASN   B 2 2   ? 3.38000  -16.69800 16.70300 1.000 67.82113  ?  626 ASN   C N    1 
ATOM   2029 C  CA   . ASN   B 2 2   ? 3.33900  -16.16800 15.35200 1.000 63.48289  ?  626 ASN   C CA   1 
ATOM   2030 C  C    . ASN   B 2 2   ? 3.64400  -14.68000 15.42800 1.000 56.97049  ?  626 ASN   C C    1 
ATOM   2031 O  O    . ASN   B 2 2   ? 3.19600  -13.98900 16.35100 1.000 57.21771  ?  626 ASN   C O    1 
ATOM   2032 C  CB   . ASN   B 2 2   ? 1.97100  -16.39500 14.70700 1.000 65.29854  ?  626 ASN   C CB   1 
ATOM   2033 C  CG   . ASN   B 2 2   ? 1.52200  -17.84100 14.77900 1.000 67.23778  ?  626 ASN   C CG   1 
ATOM   2034 O  OD1  . ASN   B 2 2   ? 0.32800  -18.13000 14.70800 1.000 68.05095  ?  626 ASN   C OD1  1 
ATOM   2035 N  ND2  . ASN   B 2 2   ? 2.47500  -18.75700 14.90000 1.000 67.84427  ?  626 ASN   C ND2  1 
ATOM   2036 N  N    . HIS   B 2 3   ? 4.41500  -14.18400 14.46300 1.000 49.56839  ?  627 HIS   C N    1 
ATOM   2037 C  CA   . HIS   B 2 3   ? 4.81200  -12.77900 14.43800 1.000 43.07547  ?  627 HIS   C CA   1 
ATOM   2038 C  C    . HIS   B 2 3   ? 4.35700  -12.14700 13.13100 1.000 38.07402  ?  627 HIS   C C    1 
ATOM   2039 O  O    . HIS   B 2 3   ? 5.18600  -11.74200 12.30200 1.000 36.06824  ?  627 HIS   C O    1 
ATOM   2040 C  CB   . HIS   B 2 3   ? 6.31900  -12.62300 14.63200 1.000 41.36544  ?  627 HIS   C CB   1 
ATOM   2041 C  CG   . HIS   B 2 3   ? 6.81900  -13.23600 15.89900 1.000 40.83087  ?  627 HIS   C CG   1 
ATOM   2042 N  ND1  . HIS   B 2 3   ? 7.12200  -14.57600 16.00200 1.000 41.04642  ?  627 HIS   C ND1  1 
ATOM   2043 C  CD2  . HIS   B 2 3   ? 7.03800  -12.70500 17.12500 1.000 40.14588  ?  627 HIS   C CD2  1 
ATOM   2044 C  CE1  . HIS   B 2 3   ? 7.52100  -14.84300 17.23200 1.000 40.40551  ?  627 HIS   C CE1  1 
ATOM   2045 N  NE2  . HIS   B 2 3   ? 7.47200  -13.72600 17.93500 1.000 40.68841  ?  627 HIS   C NE2  1 
ATOM   2046 N  N    . PRO   B 2 4   ? 3.04000  -12.00000 12.93800 1.000 35.27758  ?  628 PRO   C N    1 
ATOM   2047 C  CA   . PRO   B 2 4   ? 2.54900  -11.50300 11.64800 1.000 33.06924  ?  628 PRO   C CA   1 
ATOM   2048 C  C    . PRO   B 2 4   ? 2.88400  -10.05000 11.38800 1.000 31.50589  ?  628 PRO   C C    1 
ATOM   2049 O  O    . PRO   B 2 4   ? 3.07200  -9.67900  10.22500 1.000 30.87144  ?  628 PRO   C O    1 
ATOM   2050 C  CB   . PRO   B 2 4   ? 1.03000  -11.72000 11.74900 1.000 32.74721  ?  628 PRO   C CB   1 
ATOM   2051 C  CG   . PRO   B 2 4   ? 0.74500  -11.60600 13.20300 1.000 33.34214  ?  628 PRO   C CG   1 
ATOM   2052 C  CD   . PRO   B 2 4   ? 1.93600  -12.24000 13.88700 1.000 34.70028  ?  628 PRO   C CD   1 
ATOM   2053 N  N    . MET   B 2 5   ? 2.94600  -9.20600  12.42500 1.000 30.53411  ?  629 MET   C N    1 
ATOM   2054 C  CA   . MET   B 2 5   ? 3.27700  -7.80500  12.18900 1.000 27.98371  ?  629 MET   C CA   1 
ATOM   2055 C  C    . MET   B 2 5   ? 4.76200  -7.64100  11.89700 1.000 34.60190  ?  629 MET   C C    1 
ATOM   2056 O  O    . MET   B 2 5   ? 5.14000  -6.91800  10.96900 1.000 27.60612  ?  629 MET   C O    1 
ATOM   2057 C  CB   . MET   B 2 5   ? 2.85700  -6.94700  13.38500 1.000 31.19232  ?  629 MET   C CB   1 
ATOM   2058 C  CG   . MET   B 2 5   ? 1.33700  -6.81000  13.52700 1.000 32.80374  ?  629 MET   C CG   1 
ATOM   2059 S  SD   . MET   B 2 5   ? 0.84400  -5.98900  15.05400 1.000 33.97721  ?  629 MET   C SD   1 
ATOM   2060 C  CE   . MET   B 2 5   ? 1.08900  -7.30300  16.23900 1.000 34.29116  ?  629 MET   C CE   1 
ATOM   2061 N  N    . LEU   B 2 6   ? 5.61100  -8.32400  12.66800 1.000 27.82413  ?  630 LEU   C N    1 
ATOM   2062 C  CA   . LEU   B 2 6   ? 7.03600  -8.34700  12.35700 1.000 33.15289  ?  630 LEU   C CA   1 
ATOM   2063 C  C    . LEU   B 2 6   ? 7.27200  -8.94700  10.97400 1.000 34.38530  ?  630 LEU   C C    1 
ATOM   2064 O  O    . LEU   B 2 6   ? 7.95800  -8.35500  10.13300 1.000 34.21667  ?  630 LEU   C O    1 
ATOM   2065 C  CB   . LEU   B 2 6   ? 7.78700  -9.12800  13.44200 1.000 33.38830  ?  630 LEU   C CB   1 
ATOM   2066 C  CG   . LEU   B 2 6   ? 9.29900  -9.31300  13.32100 1.000 34.37422  ?  630 LEU   C CG   1 
ATOM   2067 C  CD1  . LEU   B 2 6   ? 9.97300  -8.01700  12.92000 1.000 32.97774  ?  630 LEU   C CD1  1 
ATOM   2068 C  CD2  . LEU   B 2 6   ? 9.85800  -9.84000  14.63700 1.000 33.16000  ?  630 LEU   C CD2  1 
ATOM   2069 N  N    . MET   B 2 7   ? 6.66000  -10.10400 10.70700 1.000 36.19804  ?  631 MET   C N    1 
ATOM   2070 C  CA   . MET   B 2 7   ? 6.81500  -10.74300 9.40500  1.000 37.54721  ?  631 MET   C CA   1 
ATOM   2071 C  C    . MET   B 2 7   ? 6.36600  -9.82500  8.27600  1.000 34.36479  ?  631 MET   C C    1 
ATOM   2072 O  O    . MET   B 2 7   ? 7.02000  -9.75000  7.23100  1.000 34.34100  ?  631 MET   C O    1 
ATOM   2073 C  CB   . MET   B 2 7   ? 6.03500  -12.05500 9.36100  1.000 41.65521  ?  631 MET   C CB   1 
ATOM   2074 C  CG   . MET   B 2 7   ? 6.24400  -12.82200 8.07900  1.000 46.84329  ?  631 MET   C CG   1 
ATOM   2075 S  SD   . MET   B 2 7   ? 7.86300  -13.61100 8.08400  1.000 52.22268  ?  631 MET   C SD   1 
ATOM   2076 C  CE   . MET   B 2 7   ? 7.46100  -15.16400 8.87800  1.000 53.03552  ?  631 MET   C CE   1 
ATOM   2077 N  N    . ASN   B 2 8   ? 5.26700  -9.09700  8.47700  1.000 33.65192  ?  632 ASN   C N    1 
ATOM   2078 C  CA   . ASN   B 2 8   ? 4.76600  -8.22100  7.42300  1.000 34.64043  ?  632 ASN   C CA   1 
ATOM   2079 C  C    . ASN   B 2 8   ? 5.69100  -7.03400  7.19400  1.000 35.00637  ?  632 ASN   C C    1 
ATOM   2080 O  O    . ASN   B 2 8   ? 5.88200  -6.60500  6.05000  1.000 35.79831  ?  632 ASN   C O    1 
ATOM   2081 C  CB   . ASN   B 2 8   ? 3.35800  -7.73500  7.76200  1.000 36.10750  ?  632 ASN   C CB   1 
ATOM   2082 C  CG   . ASN   B 2 8   ? 2.89300  -6.62400  6.84300  1.000 37.27241  ?  632 ASN   C CG   1 
ATOM   2083 O  OD1  . ASN   B 2 8   ? 2.99200  -5.44000  7.17400  1.000 38.44353  ?  632 ASN   C OD1  1 
ATOM   2084 N  ND2  . ASN   B 2 8   ? 2.39500  -7.00000  5.67300  1.000 37.02258  ?  632 ASN   C ND2  1 
ATOM   2085 N  N    . LEU   B 2 9   ? 6.26300  -6.47600  8.26400  1.000 32.75806  ?  633 LEU   C N    1 
ATOM   2086 C  CA   . LEU   B 2 9   ? 7.21600  -5.38500  8.08700  1.000 33.21234  ?  633 LEU   C CA   1 
ATOM   2087 C  C    . LEU   B 2 9   ? 8.53000  -5.86400  7.47700  1.000 34.09072  ?  633 LEU   C C    1 
ATOM   2088 O  O    . LEU   B 2 9   ? 9.27600  -5.05100  6.91600  1.000 32.54214  ?  633 LEU   C O    1 
ATOM   2089 C  CB   . LEU   B 2 9   ? 7.48600  -4.68900  9.42500  1.000 34.32699  ?  633 LEU   C CB   1 
ATOM   2090 C  CG   . LEU   B 2 9   ? 6.39300  -3.74200  9.93100  1.000 33.72752  ?  633 LEU   C CG   1 
ATOM   2091 C  CD1  . LEU   B 2 9   ? 6.64800  -3.33500  11.37800 1.000 31.59116  ?  633 LEU   C CD1  1 
ATOM   2092 C  CD2  . LEU   B 2 9   ? 6.30300  -2.51700  9.03900  1.000 34.09199  ?  633 LEU   C CD2  1 
ATOM   2093 N  N    . LEU   B 2 10  ? 8.83300  -7.15900  7.58200  1.000 35.80302  ?  634 LEU   C N    1 
ATOM   2094 C  CA   . LEU   B 2 10  ? 10.02300 -7.70800  6.94600  1.000 39.51222  ?  634 LEU   C CA   1 
ATOM   2095 C  C    . LEU   B 2 10  ? 9.80900  -8.00200  5.47100  1.000 43.51951  ?  634 LEU   C C    1 
ATOM   2096 O  O    . LEU   B 2 10  ? 10.78500 -8.04000  4.71300  1.000 44.20230  ?  634 LEU   C O    1 
ATOM   2097 C  CB   . LEU   B 2 10  ? 10.46700 -8.98400  7.66300  1.000 38.82008  ?  634 LEU   C CB   1 
ATOM   2098 C  CG   . LEU   B 2 10  ? 11.23200 -8.74200  8.96100  1.000 38.13027  ?  634 LEU   C CG   1 
ATOM   2099 C  CD1  . LEU   B 2 10  ? 11.47000 -10.04800 9.70500  1.000 38.54301  ?  634 LEU   C CD1  1 
ATOM   2100 C  CD2  . LEU   B 2 10  ? 12.53500 -8.04500  8.66000  1.000 38.79696  ?  634 LEU   C CD2  1 
ATOM   2101 N  N    . LYS   B 2 11  ? 8.56200  -8.20500  5.05800  1.000 47.08625  ?  635 LYS   C N    1 
ATOM   2102 C  CA   . LYS   B 2 11  ? 8.21600  -8.43400  3.66400  1.000 50.40020  ?  635 LYS   C CA   1 
ATOM   2103 C  C    . LYS   B 2 11  ? 8.30500  -7.14300  2.84900  1.000 50.81641  ?  635 LYS   C C    1 
ATOM   2104 O  O    . LYS   B 2 11  ? 9.32200  -6.87100  2.21400  1.000 51.03433  ?  635 LYS   C O    1 
ATOM   2105 C  CB   . LYS   B 2 11  ? 6.80600  -9.01900  3.56900  1.000 53.43311  ?  635 LYS   C CB   1 
ATOM   2106 C  CG   . LYS   B 2 11  ? 6.44300  -9.61400  2.21900  1.000 56.90520  ?  635 LYS   C CG   1 
ATOM   2107 C  CD   . LYS   B 2 11  ? 5.00100  -9.27700  1.84100  1.000 59.31534  ?  635 LYS   C CD   1 
ATOM   2108 C  CE   . LYS   B 2 11  ? 4.72800  -9.48800  0.36000  1.000 61.06730  ?  635 LYS   C CE   1 
ATOM   2109 N  NZ   . LYS   B 2 11  ? 5.30700  -10.76800 -0.14500 1.000 62.48986  ?  635 LYS   C NZ   1 
HETATM 2110 C  C10  A A1L74 C 3 .   ? 12.61800 2.07900   26.49500 0.660 21.96884  ?  501 A1L74 A C10  1 
HETATM 2111 C  C10  B A1L74 C 3 .   ? 12.62800 2.07900   26.49000 0.340 22.08300  ?  501 A1L74 A C10  1 
HETATM 2112 C  C13  A A1L74 C 3 .   ? 11.63300 4.63000   27.03400 0.660 23.26897  ?  501 A1L74 A C13  1 
HETATM 2113 C  C13  B A1L74 C 3 .   ? 11.62400 4.63200   27.05600 0.340 23.22498  ?  501 A1L74 A C13  1 
HETATM 2114 C  C15  A A1L74 C 3 .   ? 12.92900 7.51100   26.65600 0.660 22.99384  ?  501 A1L74 A C15  1 
HETATM 2115 C  C15  B A1L74 C 3 .   ? 12.92500 7.55200   26.74000 0.340 23.05551  ?  501 A1L74 A C15  1 
HETATM 2116 C  C20  A A1L74 C 3 .   ? 13.60300 8.51500   16.75100 0.660 31.74020  ?  501 A1L74 A C20  1 
HETATM 2117 C  C20  B A1L74 C 3 .   ? 13.55800 8.39700   16.89500 0.340 31.71849  ?  501 A1L74 A C20  1 
HETATM 2118 C  C21  A A1L74 C 3 .   ? 14.37900 8.63500   15.41700 0.660 32.62442  ?  501 A1L74 A C21  1 
HETATM 2119 C  C21  B A1L74 C 3 .   ? 14.30600 8.64100   15.54900 0.340 32.61707  ?  501 A1L74 A C21  1 
HETATM 2120 C  C22  A A1L74 C 3 .   ? 13.58600 7.95800   14.29300 0.660 32.84681  ?  501 A1L74 A C22  1 
HETATM 2121 C  C22  B A1L74 C 3 .   ? 13.58500 7.95400   14.36800 0.340 32.92866  ?  501 A1L74 A C22  1 
HETATM 2122 C  C24  A A1L74 C 3 .   ? 8.78700  -0.28500  28.15900 0.660 20.24484  ?  501 A1L74 A C24  1 
HETATM 2123 C  C24  B A1L74 C 3 .   ? 8.76800  -0.27800  28.15000 0.340 20.75192  ?  501 A1L74 A C24  1 
HETATM 2124 C  C26  A A1L74 C 3 .   ? 8.34900  -0.79600  26.77100 0.660 19.84894  ?  501 A1L74 A C26  1 
HETATM 2125 C  C26  B A1L74 C 3 .   ? 8.33500  -0.78200  26.75900 0.340 19.86688  ?  501 A1L74 A C26  1 
HETATM 2126 C  C28  A A1L74 C 3 .   ? 7.52100  0.23700   26.00800 0.660 19.58875  ?  501 A1L74 A C28  1 
HETATM 2127 C  C28  B A1L74 C 3 .   ? 7.50400  0.27800   26.00700 0.340 19.41049  ?  501 A1L74 A C28  1 
HETATM 2128 C  C01  A A1L74 C 3 .   ? 13.46900 5.27800   21.79800 0.660 23.80462  ?  501 A1L74 A C01  1 
HETATM 2129 C  C01  B A1L74 C 3 .   ? 15.03900 7.72300   22.27600 0.340 25.69984  ?  501 A1L74 A C01  1 
HETATM 2130 C  C02  A A1L74 C 3 .   ? 14.08500 6.31500   21.15700 0.660 25.65985  ?  501 A1L74 A C02  1 
HETATM 2131 C  C02  B A1L74 C 3 .   ? 14.48700 6.86700   21.35500 0.340 25.44768  ?  501 A1L74 A C02  1 
HETATM 2132 C  C03  A A1L74 C 3 .   ? 14.69700 7.28400   21.91300 0.660 25.03149  ?  501 A1L74 A C03  1 
HETATM 2133 C  C03  B A1L74 C 3 .   ? 13.76400 5.77000   21.81200 0.340 24.70833  ?  501 A1L74 A C03  1 
HETATM 2134 C  C04  A A1L74 C 3 .   ? 14.64200 7.24700   23.29900 0.660 25.24848  ?  501 A1L74 A C04  1 
HETATM 2135 C  C04  B A1L74 C 3 .   ? 13.58500 5.54600   23.14200 0.340 24.17070  ?  501 A1L74 A C04  1 
HETATM 2136 C  C05  A A1L74 C 3 .   ? 13.98900 6.19600   23.98100 0.660 23.74281  ?  501 A1L74 A C05  1 
HETATM 2137 C  C05  B A1L74 C 3 .   ? 14.13800 6.42600   24.10300 0.340 23.93582  ?  501 A1L74 A C05  1 
HETATM 2138 C  C06  A A1L74 C 3 .   ? 13.41200 5.22900   23.20200 0.660 23.96336  ?  501 A1L74 A C06  1 
HETATM 2139 C  C06  B A1L74 C 3 .   ? 14.85600 7.50400   23.65800 0.340 25.33651  ?  501 A1L74 A C06  1 
HETATM 2140 C  C08  A A1L74 C 3 .   ? 12.89900 4.49700   26.42200 0.660 22.53606  ?  501 A1L74 A C08  1 
HETATM 2141 C  C08  B A1L74 C 3 .   ? 12.89300 4.50600   26.44100 0.340 22.71791  ?  501 A1L74 A C08  1 
HETATM 2142 C  C09  A A1L74 C 3 .   ? 13.39000 3.22000   26.16000 0.660 22.26292  ?  501 A1L74 A C09  1 
HETATM 2143 C  C09  B A1L74 C 3 .   ? 13.39800 3.23100   26.16600 0.340 22.33914  ?  501 A1L74 A C09  1 
HETATM 2144 C  C11  A A1L74 C 3 .   ? 11.37600 2.22900   27.11100 0.660 22.03422  ?  501 A1L74 A C11  1 
HETATM 2145 C  C11  B A1L74 C 3 .   ? 11.37800 2.21600   27.10000 0.340 22.21955  ?  501 A1L74 A C11  1 
HETATM 2146 C  C12  A A1L74 C 3 .   ? 10.87500 3.51600   27.38500 0.660 22.77651  ?  501 A1L74 A C12  1 
HETATM 2147 C  C12  B A1L74 C 3 .   ? 10.86500 3.50100   27.38700 0.340 22.85315  ?  501 A1L74 A C12  1 
HETATM 2148 C  C14  A A1L74 C 3 .   ? 15.60000 5.97100   26.80400 0.660 22.86637  ?  501 A1L74 A C14  1 
HETATM 2149 C  C14  B A1L74 C 3 .   ? 15.59600 5.98200   26.86100 0.340 22.73347  ?  501 A1L74 A C14  1 
HETATM 2150 C  C18  A A1L74 C 3 .   ? 13.48300 7.30600   18.91900 0.660 28.78157  ?  501 A1L74 A C18  1 
HETATM 2151 C  C18  B A1L74 C 3 .   ? 13.60200 7.00100   19.02600 0.340 28.68962  ?  501 A1L74 A C18  1 
HETATM 2152 C  C19  A A1L74 C 3 .   ? 14.13800 7.31300   17.55600 0.660 30.40951  ?  501 A1L74 A C19  1 
HETATM 2153 C  C19  B A1L74 C 3 .   ? 14.16200 7.15700   17.61800 0.340 30.48000  ?  501 A1L74 A C19  1 
HETATM 2154 C  C23  A A1L74 C 3 .   ? 9.46500  1.14700   28.06200 0.660 21.01953  ?  501 A1L74 A C23  1 
HETATM 2155 C  C23  B A1L74 C 3 .   ? 9.45100  1.15600   28.05200 0.340 21.19231  ?  501 A1L74 A C23  1 
HETATM 2156 C  C25  A A1L74 C 3 .   ? 7.54900  -0.18400  29.07500 0.660 20.94089  ?  501 A1L74 A C25  1 
HETATM 2157 C  C25  B A1L74 C 3 .   ? 7.53900  -0.18100  29.07300 0.340 20.99246  ?  501 A1L74 A C25  1 
HETATM 2158 C  C27  A A1L74 C 3 .   ? 6.84400  -1.49800  29.19200 0.660 20.87218  ?  501 A1L74 A C27  1 
HETATM 2159 C  C27  B A1L74 C 3 .   ? 6.84700  -1.51400  29.18400 0.340 20.76842  ?  501 A1L74 A C27  1 
HETATM 2160 C  C31  A A1L74 C 3 .   ? 15.33600 8.33400   21.08000 0.660 26.10668  ?  501 A1L74 A C31  1 
HETATM 2161 C  C31  B A1L74 C 3 .   ? 13.17600 4.82700   20.82700 0.340 24.35238  ?  501 A1L74 A C31  1 
HETATM 2162 C  C32  A A1L74 C 3 .   ? 13.12300 0.69700   26.21700 0.660 21.66593  ?  501 A1L74 A C32  1 
HETATM 2163 C  C32  B A1L74 C 3 .   ? 13.14300 0.70000   26.19800 0.340 21.51159  ?  501 A1L74 A C32  1 
HETATM 2164 C  C35  A A1L74 C 3 .   ? 15.27800 8.30900   24.18900 0.660 26.09666  ?  501 A1L74 A C35  1 
HETATM 2165 C  C35  B A1L74 C 3 .   ? 12.76600 4.32700   23.59700 0.340 23.31868  ?  501 A1L74 A C35  1 
HETATM 2166 C  C36  A A1L74 C 3 .   ? 14.76800 3.04700   25.48200 0.660 21.68008  ?  501 A1L74 A C36  1 
HETATM 2167 C  C36  B A1L74 C 3 .   ? 14.78600 3.06500   25.49200 0.340 21.57185  ?  501 A1L74 A C36  1 
HETATM 2168 O  O16  A A1L74 C 3 .   ? 10.66900 1.07200   27.41000 0.660 21.92723  ?  501 A1L74 A O16  1 
HETATM 2169 O  O16  B A1L74 C 3 .   ? 10.66400 1.04600   27.39500 0.340 21.79596  ?  501 A1L74 A O16  1 
HETATM 2170 O  O17  A A1L74 C 3 .   ? 14.19500 6.37700   19.71600 0.660 26.43598  ?  501 A1L74 A O17  1 
HETATM 2171 O  O17  B A1L74 C 3 .   ? 14.69100 7.08200   19.94800 0.340 26.84762  ?  501 A1L74 A O17  1 
HETATM 2172 O  O29  A A1L74 C 3 .   ? 9.68900  -1.22000  28.65400 0.660 20.28718  ?  501 A1L74 A O29  1 
HETATM 2173 O  O29  B A1L74 C 3 .   ? 9.68900  -1.21400  28.66600 0.340 20.19594  ?  501 A1L74 A O29  1 
HETATM 2174 O  O30  A A1L74 C 3 .   ? 13.38200 6.73900   14.36500 0.660 32.85041  ?  501 A1L74 A O30  1 
HETATM 2175 O  O30  B A1L74 C 3 .   ? 13.19500 8.62700   13.39300 0.340 33.09064  ?  501 A1L74 A O30  1 
HETATM 2176 O  O33  A A1L74 C 3 .   ? 13.18400 8.62600   13.34500 0.660 32.82609  -1 501 A1L74 A O33  1 
HETATM 2177 O  O33  B A1L74 C 3 .   ? 13.40700 6.72100   14.39400 0.340 32.69043  -1 501 A1L74 A O33  1 
HETATM 2178 O  O34  A A1L74 C 3 .   ? 13.88700 6.14200   16.88300 0.660 30.85120  ?  501 A1L74 A O34  1 
HETATM 2179 O  O34  B A1L74 C 3 .   ? 13.89600 6.03400   16.87000 0.340 30.36600  ?  501 A1L74 A O34  1 
HETATM 2180 SI SI07 A A1L74 C 3 .   ? 13.90600 6.07800   25.95300 0.660 22.60759  ?  501 A1L74 A SI07 1 
HETATM 2181 SI SI07 B A1L74 C 3 .   ? 13.89600 6.10900   26.01700 0.340 23.23306  ?  501 A1L74 A SI07 1 
HETATM 2182 O  O    . HOH   D 4 .   ? 18.60000 -18.61700 8.23900  1.000 36.93058  ?  601 HOH   A O    1 
HETATM 2183 O  O    . HOH   D 4 .   ? 35.29900 -9.22400  16.97500 1.000 39.40585  ?  602 HOH   A O    1 
HETATM 2184 O  O    . HOH   D 4 .   ? 43.44900 4.70900   12.25500 1.000 40.27380  ?  603 HOH   A O    1 
HETATM 2185 O  O    . HOH   D 4 .   ? 7.81000  -3.88700  37.56600 1.000 54.54124  ?  604 HOH   A O    1 
HETATM 2186 O  O    . HOH   D 4 .   ? 22.80800 10.50800  11.63700 1.000 46.61232  ?  605 HOH   A O    1 
HETATM 2187 O  O    . HOH   D 4 .   ? 11.79300 -19.40900 7.36400  1.000 49.81463  ?  606 HOH   A O    1 
HETATM 2188 O  O    . HOH   D 4 .   ? -4.27000 0.81100   31.99600 1.000 59.29720  ?  607 HOH   A O    1 
HETATM 2189 O  O    . HOH   D 4 .   ? 18.39500 12.17800  32.87700 1.000 25.38147  ?  608 HOH   A O    1 
HETATM 2190 O  O    . HOH   D 4 .   ? 18.92400 14.97800  33.67600 1.000 50.59284  ?  609 HOH   A O    1 
HETATM 2191 O  O    . HOH   D 4 .   ? 12.73000 -21.97400 9.12100  1.000 42.62693  ?  610 HOH   A O    1 
HETATM 2192 O  O    . HOH   D 4 .   ? 12.14500 10.71300  14.14900 1.000 44.43265  ?  611 HOH   A O    1 
HETATM 2193 O  O    . HOH   D 4 .   ? 3.64400  0.52400   16.08900 1.000 28.53456  ?  612 HOH   A O    1 
HETATM 2194 O  O    . HOH   D 4 .   ? 18.22000 9.14900   19.19200 1.000 48.18016  ?  613 HOH   A O    1 
HETATM 2195 O  O    . HOH   D 4 .   ? 33.24700 0.60400   25.67200 1.000 32.78212  ?  614 HOH   A O    1 
HETATM 2196 O  O    . HOH   D 4 .   ? 23.53000 -3.60900  32.66500 1.000 33.40055  ?  615 HOH   A O    1 
HETATM 2197 O  O    A HOH   D 4 .   ? 11.32200 15.14600  32.39100 0.540 30.54318  ?  616 HOH   A O    1 
HETATM 2198 O  O    B HOH   D 4 .   ? 11.57400 15.92100  30.73000 0.460 31.11474  ?  616 HOH   A O    1 
HETATM 2199 O  O    . HOH   D 4 .   ? 13.95800 -1.15200  4.89300  1.000 28.35967  ?  617 HOH   A O    1 
HETATM 2200 O  O    . HOH   D 4 .   ? 44.93000 3.85200   17.16400 1.000 40.48513  ?  618 HOH   A O    1 
HETATM 2201 O  O    . HOH   D 4 .   ? 39.83100 5.19100   21.78800 1.000 42.66987  ?  619 HOH   A O    1 
HETATM 2202 O  O    . HOH   D 4 .   ? 33.73500 5.34400   26.33000 1.000 27.79283  ?  620 HOH   A O    1 
HETATM 2203 O  O    . HOH   D 4 .   ? 30.21200 10.19900  6.63600  1.000 55.28471  ?  621 HOH   A O    1 
HETATM 2204 O  O    . HOH   D 4 .   ? 36.99300 7.53700   20.61800 1.000 37.87010  ?  622 HOH   A O    1 
HETATM 2205 O  O    . HOH   D 4 .   ? 30.14800 11.08100  17.32100 1.000 40.17587  ?  623 HOH   A O    1 
HETATM 2206 O  O    . HOH   D 4 .   ? -0.77600 3.53600   20.26400 1.000 22.19159  ?  624 HOH   A O    1 
HETATM 2207 O  O    . HOH   D 4 .   ? -1.35300 12.71800  14.37600 1.000 48.96201  ?  625 HOH   A O    1 
HETATM 2208 O  O    . HOH   D 4 .   ? 41.84200 1.31600   2.57300  1.000 49.51144  ?  626 HOH   A O    1 
HETATM 2209 O  O    . HOH   D 4 .   ? 25.30900 6.14200   1.53800  1.000 28.37839  ?  627 HOH   A O    1 
HETATM 2210 O  O    . HOH   D 4 .   ? 14.94400 -5.84600  38.23100 1.000 40.58788  ?  628 HOH   A O    1 
HETATM 2211 O  O    . HOH   D 4 .   ? 10.41600 17.76700  29.32000 1.000 47.40748  ?  629 HOH   A O    1 
HETATM 2212 O  O    . HOH   D 4 .   ? 15.89300 -11.30700 31.64000 1.000 36.80715  ?  630 HOH   A O    1 
HETATM 2213 O  O    . HOH   D 4 .   ? 8.86500  16.95000  17.01300 1.000 43.32401  ?  631 HOH   A O    1 
HETATM 2214 O  O    . HOH   D 4 .   ? 9.49000  -0.83500  9.35000  1.000 37.13584  ?  632 HOH   A O    1 
HETATM 2215 O  O    . HOH   D 4 .   ? 19.58600 -20.60000 6.48100  1.000 42.73174  ?  633 HOH   A O    1 
HETATM 2216 O  O    . HOH   D 4 .   ? 19.45100 -7.57600  3.27900  1.000 36.71497  ?  634 HOH   A O    1 
HETATM 2217 O  O    . HOH   D 4 .   ? 12.21100 -9.79400  22.47200 1.000 35.69466  ?  635 HOH   A O    1 
HETATM 2218 O  O    . HOH   D 4 .   ? -0.68200 13.43800  20.68300 1.000 37.42161  ?  636 HOH   A O    1 
HETATM 2219 O  O    . HOH   D 4 .   ? 31.51000 4.09000   1.40700  1.000 40.85411  ?  637 HOH   A O    1 
HETATM 2220 O  O    . HOH   D 4 .   ? 10.46200 -10.13700 35.80700 1.000 32.02537  ?  638 HOH   A O    1 
HETATM 2221 O  O    . HOH   D 4 .   ? 20.23500 -10.12800 17.02100 1.000 31.43413  ?  639 HOH   A O    1 
HETATM 2222 O  O    . HOH   D 4 .   ? 13.34600 -6.82900  26.40700 1.000 32.65163  ?  640 HOH   A O    1 
HETATM 2223 O  O    . HOH   D 4 .   ? 24.89500 -7.08500  21.79300 1.000 20.37558  ?  641 HOH   A O    1 
HETATM 2224 O  O    . HOH   D 4 .   ? 18.56900 2.88300   -1.08000 1.000 32.74313  ?  642 HOH   A O    1 
HETATM 2225 O  O    . HOH   D 4 .   ? 31.54400 -11.35100 13.63400 1.000 37.75620  ?  643 HOH   A O    1 
HETATM 2226 O  O    . HOH   D 4 .   ? 36.31800 -7.24800  0.97000  1.000 40.34156  ?  644 HOH   A O    1 
HETATM 2227 O  O    . HOH   D 4 .   ? 19.19000 -8.40400  34.84600 1.000 42.82816  ?  645 HOH   A O    1 
HETATM 2228 O  O    . HOH   D 4 .   ? 10.73400 17.80500  18.53300 1.000 49.43238  ?  646 HOH   A O    1 
HETATM 2229 O  O    . HOH   D 4 .   ? 30.26900 -19.13600 9.66100  1.000 39.59921  ?  647 HOH   A O    1 
HETATM 2230 O  O    . HOH   D 4 .   ? 26.05000 0.11400   31.35500 1.000 22.22580  ?  648 HOH   A O    1 
HETATM 2231 O  O    . HOH   D 4 .   ? 2.15900  9.26000   28.41700 1.000 22.70541  ?  649 HOH   A O    1 
HETATM 2232 O  O    . HOH   D 4 .   ? 31.88600 -7.27000  29.15900 1.000 45.29567  ?  650 HOH   A O    1 
HETATM 2233 O  O    . HOH   D 4 .   ? 46.94800 -4.86200  1.86800  1.000 54.15483  ?  651 HOH   A O    1 
HETATM 2234 O  O    A HOH   D 4 .   ? 31.89300 7.07900   4.36100  0.500 31.00387  ?  652 HOH   A O    1 
HETATM 2235 O  O    B HOH   D 4 .   ? 34.08200 5.94300   4.57700  0.500 29.79848  ?  652 HOH   A O    1 
HETATM 2236 O  O    . HOH   D 4 .   ? 13.94300 -3.53800  39.36000 1.000 46.36788  ?  653 HOH   A O    1 
HETATM 2237 O  O    . HOH   D 4 .   ? 27.41400 -9.18800  28.36100 1.000 20.40632  ?  654 HOH   A O    1 
HETATM 2238 O  O    . HOH   D 4 .   ? 11.78500 -12.80300 34.26700 1.000 61.43218  ?  655 HOH   A O    1 
HETATM 2239 O  O    . HOH   D 4 .   ? -5.80900 -1.47100  25.02300 1.000 15.81454  ?  656 HOH   A O    1 
HETATM 2240 O  O    . HOH   D 4 .   ? 15.38200 -9.22100  24.17100 1.000 32.48520  ?  657 HOH   A O    1 
HETATM 2241 O  O    . HOH   D 4 .   ? 3.00500  13.01800  21.29600 1.000 26.15543  ?  658 HOH   A O    1 
HETATM 2242 O  O    . HOH   D 4 .   ? 9.76100  11.80400  13.06800 1.000 40.79342  ?  659 HOH   A O    1 
HETATM 2243 O  O    . HOH   D 4 .   ? 29.86600 5.47900   31.53500 1.000 29.37964  ?  660 HOH   A O    1 
HETATM 2244 O  O    . HOH   D 4 .   ? 0.96000  -10.51200 16.91300 1.000 40.66853  ?  661 HOH   A O    1 
HETATM 2245 O  O    . HOH   D 4 .   ? 32.06000 -8.04500  15.95200 1.000 44.66052  ?  662 HOH   A O    1 
HETATM 2246 O  O    . HOH   D 4 .   ? 13.87100 -6.66600  21.47200 1.000 20.98754  ?  663 HOH   A O    1 
HETATM 2247 O  O    . HOH   D 4 .   ? 0.47900  -8.24400  19.34000 1.000 35.20898  ?  664 HOH   A O    1 
HETATM 2248 O  O    . HOH   D 4 .   ? -1.22000 8.54700   15.70400 1.000 29.53885  ?  665 HOH   A O    1 
HETATM 2249 O  O    . HOH   D 4 .   ? -1.255   10.421    27.586   1.000 30.45622  ?  666 HOH   A O    1 
HETATM 2250 O  O    . HOH   D 4 .   ? 28.32200 0.79100   29.87700 1.000 32.52403  ?  667 HOH   A O    1 
HETATM 2251 O  O    . HOH   D 4 .   ? 37.14800 9.77200   17.83000 1.000 62.74122  ?  668 HOH   A O    1 
HETATM 2252 O  O    A HOH   D 4 .   ? 19.05100 14.88400  17.84700 0.500 29.72432  ?  669 HOH   A O    1 
HETATM 2253 O  O    B HOH   D 4 .   ? 19.12300 15.72200  19.81800 0.500 30.65047  ?  669 HOH   A O    1 
HETATM 2254 O  O    . HOH   D 4 .   ? 16.07900 4.39300   19.40900 1.000 42.39238  ?  670 HOH   A O    1 
HETATM 2255 O  O    . HOH   D 4 .   ? 5.42100  -10.35100 28.64700 1.000 40.77675  ?  671 HOH   A O    1 
HETATM 2256 O  O    . HOH   D 4 .   ? 8.38400  -15.70200 4.37700  1.000 59.19021  ?  672 HOH   A O    1 
HETATM 2257 O  O    A HOH   D 4 .   ? 7.28200  0.77200   9.41200  0.490 14.39429  ?  673 HOH   A O    1 
HETATM 2258 O  O    B HOH   D 4 .   ? 8.24500  2.94600   9.91500  0.510 26.72983  ?  673 HOH   A O    1 
HETATM 2259 O  O    . HOH   D 4 .   ? 21.44300 -7.81100  33.34100 1.000 29.08821  ?  674 HOH   A O    1 
HETATM 2260 O  O    . HOH   D 4 .   ? 11.25500 -8.66800  26.51300 1.000 27.99820  ?  675 HOH   A O    1 
HETATM 2261 O  O    . HOH   D 4 .   ? 20.93700 15.82400  21.67600 1.000 39.68400  ?  676 HOH   A O    1 
HETATM 2262 O  O    . HOH   D 4 .   ? 27.64800 -12.53800 18.33900 1.000 37.42349  ?  677 HOH   A O    1 
HETATM 2263 O  O    . HOH   D 4 .   ? 44.23600 0.53700   18.76300 1.000 35.36331  ?  678 HOH   A O    1 
HETATM 2264 O  O    . HOH   D 4 .   ? 8.21700  3.96300   12.72800 1.000 38.65402  ?  679 HOH   A O    1 
HETATM 2265 O  O    . HOH   D 4 .   ? 28.11200 -10.23700 18.32400 1.000 29.99006  ?  680 HOH   A O    1 
HETATM 2266 O  O    A HOH   D 4 .   ? 20.78100 11.54400  11.20300 0.590 22.73358  ?  681 HOH   A O    1 
HETATM 2267 O  O    B HOH   D 4 .   ? 19.46200 10.52400  9.75300  0.410 17.12219  ?  681 HOH   A O    1 
HETATM 2268 O  O    . HOH   D 4 .   ? 20.86000 1.42100   1.64100  1.000 25.97287  ?  682 HOH   A O    1 
HETATM 2269 O  O    . HOH   D 4 .   ? 42.77900 0.80500   16.60000 1.000 33.98462  ?  683 HOH   A O    1 
HETATM 2270 O  O    . HOH   D 4 .   ? 37.75100 11.20300  14.27500 1.000 45.04208  ?  684 HOH   A O    1 
HETATM 2271 O  O    . HOH   D 4 .   ? 36.08700 -5.93200  24.09500 1.000 39.56835  ?  685 HOH   A O    1 
HETATM 2272 O  O    A HOH   D 4 .   ? -0.70000 9.38200   30.38800 0.630 29.53384  ?  686 HOH   A O    1 
HETATM 2273 O  O    B HOH   D 4 .   ? -1.06900 8.32700   31.20600 0.370 31.50336  ?  686 HOH   A O    1 
HETATM 2274 O  O    . HOH   D 4 .   ? 3.39500  2.51500   10.58700 1.000 47.09874  ?  687 HOH   A O    1 
HETATM 2275 O  O    . HOH   D 4 .   ? 32.18500 -13.96200 5.98500  1.000 46.39761  ?  688 HOH   A O    1 
HETATM 2276 O  O    . HOH   D 4 .   ? 30.04900 12.52400  20.97200 1.000 35.57478  ?  689 HOH   A O    1 
HETATM 2277 O  O    . HOH   D 4 .   ? 25.93000 -8.62000  19.77300 1.000 32.58828  ?  690 HOH   A O    1 
HETATM 2278 O  O    . HOH   D 4 .   ? 18.30600 3.90800   11.92200 1.000 23.53714  ?  691 HOH   A O    1 
HETATM 2279 O  O    . HOH   D 4 .   ? 28.42300 -19.70500 14.70300 1.000 44.50534  ?  692 HOH   A O    1 
HETATM 2280 O  O    . HOH   D 4 .   ? 14.66600 -14.55200 2.79400  1.000 54.31659  ?  693 HOH   A O    1 
HETATM 2281 O  O    . HOH   D 4 .   ? 39.73600 -5.72600  4.57500  1.000 46.86470  ?  694 HOH   A O    1 
HETATM 2282 O  O    . HOH   D 4 .   ? 23.71300 -12.65300 25.60400 1.000 31.49340  ?  695 HOH   A O    1 
HETATM 2283 O  O    . HOH   D 4 .   ? 21.01800 6.83500   15.82200 1.000 21.08982  ?  696 HOH   A O    1 
HETATM 2284 O  O    . HOH   D 4 .   ? 34.50100 -7.80500  5.14600  1.000 32.34426  ?  697 HOH   A O    1 
HETATM 2285 O  O    . HOH   D 4 .   ? 17.74700 -7.49200  38.49600 1.000 46.23584  ?  698 HOH   A O    1 
HETATM 2286 O  O    . HOH   D 4 .   ? 35.27400 -10.17800 5.68300  1.000 48.78688  ?  699 HOH   A O    1 
HETATM 2287 O  O    . HOH   D 4 .   ? 26.11200 10.24900  19.30400 1.000 34.73923  ?  700 HOH   A O    1 
HETATM 2288 O  O    . HOH   D 4 .   ? 2.09300  3.79500   43.25700 1.000 53.01321  ?  701 HOH   A O    1 
HETATM 2289 O  O    A HOH   D 4 .   ? 16.896   -4.281    43.239   0.530 18.67894  ?  702 HOH   A O    1 
HETATM 2290 O  O    B HOH   D 4 .   ? 16.232   -2.594    42.925   0.470 18.76658  ?  702 HOH   A O    1 
HETATM 2291 O  O    . HOH   D 4 .   ? 12.80900 19.10200  15.82500 1.000 49.16705  ?  703 HOH   A O    1 
HETATM 2292 O  O    . HOH   D 4 .   ? 14.01100 14.32600  7.91000  1.000 50.55999  ?  704 HOH   A O    1 
HETATM 2293 O  O    . HOH   D 4 .   ? 20.90000 14.02100  15.24600 1.000 47.10967  ?  705 HOH   A O    1 
HETATM 2294 O  O    . HOH   D 4 .   ? -1.35600 -11.69900 34.97500 1.000 50.38945  ?  706 HOH   A O    1 
HETATM 2295 O  O    . HOH   D 4 .   ? -0.05800 4.26500   32.25000 1.000 38.11327  ?  707 HOH   A O    1 
HETATM 2296 O  O    . HOH   D 4 .   ? 29.52800 8.00900   19.78700 1.000 21.34812  ?  708 HOH   A O    1 
HETATM 2297 O  O    . HOH   D 4 .   ? -2.65000 0.92500   22.66100 1.000 44.88718  ?  709 HOH   A O    1 
HETATM 2298 O  O    . HOH   D 4 .   ? 15.01400 -14.03500 19.83800 1.000 65.51744  ?  710 HOH   A O    1 
HETATM 2299 O  O    . HOH   D 4 .   ? 2.80200  -1.60900  37.57700 1.000 44.95225  ?  711 HOH   A O    1 
HETATM 2300 O  O    . HOH   D 4 .   ? -4.056   16.552    14.216   1.000 55.69036  ?  712 HOH   A O    1 
HETATM 2301 O  O    . HOH   D 4 .   ? 18.60800 -22.71800 7.27800  1.000 42.74491  ?  713 HOH   A O    1 
HETATM 2302 O  O    . HOH   D 4 .   ? 18.39500 16.38000  15.67200 1.000 43.89544  ?  714 HOH   A O    1 
HETATM 2303 O  O    . HOH   D 4 .   ? 2.078    1.775     13.247   1.000 47.54358  ?  715 HOH   A O    1 
HETATM 2304 O  O    . HOH   D 4 .   ? 3.80700  4.44800   17.60700 1.000 25.28802  ?  716 HOH   A O    1 
HETATM 2305 O  O    . HOH   D 4 .   ? -0.72000 1.78800   33.38400 1.000 35.14959  ?  717 HOH   A O    1 
HETATM 2306 O  O    . HOH   D 4 .   ? 19.06500 -21.40200 21.33200 1.000 44.11048  ?  718 HOH   A O    1 
HETATM 2307 O  O    . HOH   D 4 .   ? 40.57400 -2.38900  19.21500 1.000 32.35184  ?  719 HOH   A O    1 
HETATM 2308 O  O    . HOH   D 4 .   ? 39.87000 -8.00700  16.66100 1.000 51.64187  ?  720 HOH   A O    1 
HETATM 2309 O  O    . HOH   D 4 .   ? 19.15300 -19.16000 4.44100  1.000 38.54819  ?  721 HOH   A O    1 
HETATM 2310 O  O    . HOH   D 4 .   ? 30.20500 -13.62700 17.08300 1.000 47.69798  ?  722 HOH   A O    1 
HETATM 2311 O  O    . HOH   D 4 .   ? 32.27300 10.66700  9.12300  1.000 63.01484  ?  723 HOH   A O    1 
HETATM 2312 O  O    A HOH   D 4 .   ? -3.89000 4.95600   26.08700 0.500 22.43811  ?  724 HOH   A O    1 
HETATM 2313 O  O    B HOH   D 4 .   ? -5.15900 5.19200   24.74700 0.500 23.77826  ?  724 HOH   A O    1 
HETATM 2314 O  O    . HOH   D 4 .   ? 39.35200 -7.11100  6.40700  1.000 46.48069  ?  725 HOH   A O    1 
HETATM 2315 O  O    . HOH   D 4 .   ? 40.36500 -2.18100  14.19900 1.000 35.62154  ?  726 HOH   A O    1 
HETATM 2316 O  O    . HOH   D 4 .   ? 4.93000  -10.98400 31.29000 1.000 46.79149  ?  727 HOH   A O    1 
HETATM 2317 O  O    . HOH   D 4 .   ? 22.89900 -22.04800 4.26800  1.000 54.23862  ?  728 HOH   A O    1 
HETATM 2318 O  O    . HOH   D 4 .   ? 41.00000 -5.00300  15.28900 1.000 55.24744  ?  729 HOH   A O    1 
HETATM 2319 O  O    . HOH   D 4 .   ? 30.35400 11.28500  11.55000 1.000 36.65845  ?  730 HOH   A O    1 
HETATM 2320 O  O    . HOH   D 4 .   ? 40.55100 -0.95700  16.84100 1.000 25.97497  ?  731 HOH   A O    1 
HETATM 2321 O  O    . HOH   D 4 .   ? 25.65600 21.29600  31.71900 1.000 46.70430  ?  732 HOH   A O    1 
HETATM 2322 O  O    . HOH   D 4 .   ? 27.27100 6.69900   18.84800 1.000 24.87129  ?  733 HOH   A O    1 
HETATM 2323 O  O    . HOH   D 4 .   ? 34.15000 -7.49900  2.57900  1.000 48.92133  ?  734 HOH   A O    1 
HETATM 2324 O  O    . HOH   D 4 .   ? 20.68500 -24.58700 7.93000  1.000 56.43379  ?  735 HOH   A O    1 
HETATM 2325 O  O    . HOH   D 4 .   ? 4.49800  4.32200   14.65700 1.000 41.39143  ?  736 HOH   A O    1 
HETATM 2326 O  O    . HOH   D 4 .   ? 26.44200 15.50000  24.20600 1.000 46.95920  ?  737 HOH   A O    1 
HETATM 2327 O  O    . HOH   D 4 .   ? 20.57100 -12.30000 23.27400 1.000 35.45551  ?  738 HOH   A O    1 
HETATM 2328 O  O    . HOH   D 4 .   ? 2.87200  17.06100  31.22600 1.000 47.13908  ?  739 HOH   A O    1 
HETATM 2329 O  O    . HOH   D 4 .   ? 12.71300 7.95000   8.97300  1.000 39.84741  ?  740 HOH   A O    1 
HETATM 2330 O  O    . HOH   D 4 .   ? -4.37100 1.91700   24.90200 1.000 67.55074  ?  741 HOH   A O    1 
HETATM 2331 O  O    . HOH   D 4 .   ? 36.59600 -10.81900 12.70000 1.000 54.82294  ?  742 HOH   A O    1 
HETATM 2332 O  O    . HOH   D 4 .   ? 5.05400  -12.90700 20.66500 1.000 44.94968  ?  743 HOH   A O    1 
HETATM 2333 O  O    . HOH   D 4 .   ? 14.82700 -19.49900 13.59200 1.000 60.53667  ?  744 HOH   A O    1 
HETATM 2334 O  O    . HOH   D 4 .   ? 48.62100 -5.91400  6.06600  1.000 35.96645  ?  745 HOH   A O    1 
HETATM 2335 O  O    . HOH   D 4 .   ? 15.93800 18.30500  16.29100 1.000 75.74066  ?  746 HOH   A O    1 
HETATM 2336 O  O    . HOH   D 4 .   ? 35.87800 -6.07400  -2.88100 1.000 35.03189  ?  747 HOH   A O    1 
HETATM 2337 O  O    . HOH   D 4 .   ? 14.15700 9.38000   7.87900  1.000 39.86143  ?  748 HOH   A O    1 
HETATM 2338 O  O    . HOH   D 4 .   ? 37.88500 10.57600  21.10300 1.000 40.92278  ?  749 HOH   A O    1 
HETATM 2339 O  O    . HOH   D 4 .   ? 11.15000 -17.37500 14.46700 1.000 50.45812  ?  750 HOH   A O    1 
HETATM 2340 O  O    . HOH   D 4 .   ? 22.13400 -14.69500 23.63400 1.000 52.40389  ?  751 HOH   A O    1 
HETATM 2341 O  O    . HOH   D 4 .   ? 15.08200 -21.72500 10.77800 1.000 36.48129  ?  752 HOH   A O    1 
HETATM 2342 O  O    . HOH   D 4 .   ? 9.89300  -2.94100  36.84600 1.000 43.17855  ?  753 HOH   A O    1 
HETATM 2343 O  O    . HOH   D 4 .   ? 20.18000 -25.89800 13.51800 1.000 42.06980  ?  754 HOH   A O    1 
HETATM 2344 O  O    . HOH   D 4 .   ? 34.49300 -12.33600 6.49700  1.000 50.91174  ?  755 HOH   A O    1 
HETATM 2345 O  O    . HOH   D 4 .   ? 25.42600 -2.40700  30.97500 1.000 32.82742  ?  756 HOH   A O    1 
HETATM 2346 O  O    . HOH   D 4 .   ? 23.00000 7.98300   1.12600  1.000 51.71761  ?  757 HOH   A O    1 
HETATM 2347 O  O    . HOH   D 4 .   ? 27.85500 -4.02400  31.70300 1.000 42.30882  ?  758 HOH   A O    1 
HETATM 2348 O  O    . HOH   D 4 .   ? 9.02500  -17.30400 13.48800 1.000 50.47269  ?  759 HOH   A O    1 
HETATM 2349 O  O    . HOH   D 4 .   ? 32.05500 6.65500   30.72100 1.000 37.02414  ?  760 HOH   A O    1 
HETATM 2350 O  O    . HOH   D 4 .   ? 42.97500 -5.33100  4.35400  1.000 53.32489  ?  761 HOH   A O    1 
HETATM 2351 O  O    . HOH   D 4 .   ? 24.34400 -23.73700 11.33500 1.000 46.67936  ?  762 HOH   A O    1 
HETATM 2352 O  O    . HOH   D 4 .   ? 27.47400 9.23000   15.39100 1.000 33.98883  ?  763 HOH   A O    1 
HETATM 2353 O  O    . HOH   D 4 .   ? 16.037   -0.409    41.637   1.000 39.47156  ?  764 HOH   A O    1 
HETATM 2354 O  O    . HOH   D 4 .   ? 20.81800 13.27600  2.40300  1.000 60.08870  ?  765 HOH   A O    1 
HETATM 2355 O  O    . HOH   D 4 .   ? 13.30000 -7.74100  23.87400 1.000 29.34254  ?  766 HOH   A O    1 
HETATM 2356 O  O    . HOH   D 4 .   ? 28.92300 10.38300  19.52400 1.000 29.43253  ?  767 HOH   A O    1 
HETATM 2357 O  O    . HOH   D 4 .   ? 32.88100 -16.45500 7.47600  1.000 43.11487  ?  768 HOH   A O    1 
HETATM 2358 O  O    . HOH   D 4 .   ? 44.48600 1.94300   3.43700  1.000 48.33990  ?  769 HOH   A O    1 
HETATM 2359 O  O    . HOH   D 4 .   ? 24.20700 13.36600  8.93200  1.000 57.79299  ?  770 HOH   A O    1 
HETATM 2360 O  O    . HOH   D 4 .   ? -1.43200 6.26400   31.75800 1.000 34.97694  ?  771 HOH   A O    1 
HETATM 2361 O  O    . HOH   D 4 .   ? 26.95800 8.52000   35.15500 1.000 62.65746  ?  772 HOH   A O    1 
HETATM 2362 O  O    . HOH   D 4 .   ? 33.55500 -11.20900 15.60700 1.000 57.75674  ?  773 HOH   A O    1 
HETATM 2363 O  O    . HOH   D 4 .   ? 41.11100 -5.32800  17.94500 1.000 57.71091  ?  774 HOH   A O    1 
HETATM 2364 O  O    . HOH   D 4 .   ? 34.51000 3.02900   26.21200 1.000 30.04141  ?  775 HOH   A O    1 
HETATM 2365 O  O    . HOH   D 4 .   ? 40.32000 12.27900  17.21100 1.000 58.04676  ?  776 HOH   A O    1 
HETATM 2366 O  O    . HOH   D 4 .   ? 18.285   12.609    -0.286   1.000 48.83966  ?  777 HOH   A O    1 
HETATM 2367 O  O    A HOH   D 4 .   ? 10.76400 2.16800   7.91600  0.520 33.34830  ?  778 HOH   A O    1 
HETATM 2368 O  O    B HOH   D 4 .   ? 11.08800 1.87900   6.02300  0.480 33.38026  ?  778 HOH   A O    1 
HETATM 2369 O  O    . HOH   D 4 .   ? 30.92800 -9.32700  17.94600 1.000 35.44455  ?  779 HOH   A O    1 
HETATM 2370 O  O    A HOH   D 4 .   ? 14.39800 -13.55000 22.05000 0.460 44.31713  ?  780 HOH   A O    1 
HETATM 2371 O  O    B HOH   D 4 .   ? 13.89700 -12.67400 21.97200 0.540 44.32796  ?  780 HOH   A O    1 
HETATM 2372 O  O    A HOH   D 4 .   ? 11.45100 -4.11400  38.26300 0.520 19.00415  ?  781 HOH   A O    1 
HETATM 2373 O  O    B HOH   D 4 .   ? 11.73800 -6.34400  37.58100 0.480 24.54536  ?  781 HOH   A O    1 
HETATM 2374 O  O    . HOH   D 4 .   ? 36.40200 6.86800   26.11300 1.000 52.80023  ?  782 HOH   A O    1 
HETATM 2375 O  O    . HOH   D 4 .   ? 27.74000 -19.30300 4.91700  1.000 50.16976  ?  783 HOH   A O    1 
HETATM 2376 O  O    . HOH   D 4 .   ? 33.95700 4.89000   2.15900  1.000 58.01906  ?  784 HOH   A O    1 
HETATM 2377 O  O    . HOH   D 4 .   ? 21.76300 13.79700  10.53900 1.000 46.41717  ?  785 HOH   A O    1 
HETATM 2378 O  O    A HOH   D 4 .   ? 25.19500 9.62400   16.71100 0.500 14.59120  ?  786 HOH   A O    1 
HETATM 2379 O  O    B HOH   D 4 .   ? 25.24700 9.51500   14.46900 0.500 21.65329  ?  786 HOH   A O    1 
HETATM 2380 O  O    . HOH   D 4 .   ? -3.42300 -11.84000 33.68800 1.000 40.52809  ?  787 HOH   A O    1 
HETATM 2381 O  O    . HOH   D 4 .   ? 20.850   22.184    23.367   1.000 59.01426  ?  788 HOH   A O    1 
HETATM 2382 O  O    . HOH   D 4 .   ? 21.079   10.286    -0.323   1.000 47.76097  ?  789 HOH   A O    1 
HETATM 2383 O  O    A HOH   D 4 .   ? 5.69200  19.04700  32.21600 0.470 48.61944  ?  790 HOH   A O    1 
HETATM 2384 O  O    B HOH   D 4 .   ? 6.97500  19.20200  31.01700 0.530 48.49262  ?  790 HOH   A O    1 
HETATM 2385 O  O    . HOH   D 4 .   ? 27.24500 -0.00800  33.88300 1.000 42.66992  ?  791 HOH   A O    1 
HETATM 2386 O  O    . HOH   D 4 .   ? 29.398   -3.083    -6.086   1.000 45.35326  ?  792 HOH   A O    1 
HETATM 2387 O  O    . HOH   D 4 .   ? 15.61000 8.70900   39.32500 1.000 56.56173  ?  793 HOH   A O    1 
HETATM 2388 O  O    . HOH   D 4 .   ? 38.559   12.918    10.879   1.000 55.70844  ?  794 HOH   A O    1 
HETATM 2389 O  O    . HOH   D 4 .   ? 29.00700 7.54800   33.44700 1.000 57.77238  ?  795 HOH   A O    1 
HETATM 2390 O  O    . HOH   D 4 .   ? 33.77500 5.31900   29.28200 1.000 41.10621  ?  796 HOH   A O    1 
HETATM 2391 O  O    . HOH   D 4 .   ? 14.082   20.389    12.930   1.000 41.38108  ?  797 HOH   A O    1 
HETATM 2392 O  O    . HOH   D 4 .   ? 25.46200 12.38600  16.25200 1.000 64.91549  ?  798 HOH   A O    1 
HETATM 2393 O  O    . HOH   D 4 .   ? 5.85100  0.22700   6.95900  1.000 50.86484  ?  799 HOH   A O    1 
HETATM 2394 O  O    A HOH   D 4 .   ? 3.25400  6.59400   15.42400 0.480 30.06182  ?  800 HOH   A O    1 
HETATM 2395 O  O    B HOH   D 4 .   ? 3.85100  7.94700   13.80900 0.520 30.41181  ?  800 HOH   A O    1 
HETATM 2396 O  O    . HOH   D 4 .   ? 19.83400 15.47900  1.51500  1.000 50.32151  ?  801 HOH   A O    1 
HETATM 2397 O  O    . HOH   D 4 .   ? 21.73300 10.97600  42.42600 1.000 41.64161  ?  802 HOH   A O    1 
HETATM 2398 O  O    . HOH   E 4 .   ? 8.46200  -7.15600  -0.16000 1.000 47.77841  ?  701 HOH   C O    1 
HETATM 2399 O  O    . HOH   E 4 .   ? 7.658    -20.921   23.693   1.000 49.28913  ?  702 HOH   C O    1 
HETATM 2400 O  O    . HOH   E 4 .   ? 9.78300  -2.32800  6.98800  1.000 35.98325  ?  703 HOH   C O    1 
HETATM 2401 O  O    . HOH   E 4 .   ? 2.03200  -11.42300 8.29500  1.000 34.76483  ?  704 HOH   C O    1 
HETATM 2402 O  O    . HOH   E 4 .   ? 2.725    -4.665    10.564   1.000 53.78581  ?  705 HOH   C O    1 
HETATM 2403 O  O    . HOH   E 4 .   ? 8.48600  -4.04300  -0.53300 1.000 50.48836  ?  706 HOH   C O    1 
HETATM 2404 O  O    . HOH   E 4 .   ? 7.25300  -1.25900  5.67300  1.000 46.58602  ?  707 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  ? 0.46881 0.99880 0.55171 -0.07910 0.04906  -0.12116 123 LYS   A N    
2    C  CA   . LYS   A 18  ? 0.45183 0.95563 0.54734 -0.06720 0.04656  -0.12724 123 LYS   A CA   
3    C  C    . LYS   A 18  ? 0.43043 0.91011 0.51593 -0.06592 0.04420  -0.12479 123 LYS   A C    
4    O  O    . LYS   A 18  ? 0.43526 0.90595 0.52976 -0.05539 0.04268  -0.13681 123 LYS   A O    
5    C  CB   . LYS   A 18  ? 0.43666 0.92312 0.53978 -0.06789 0.04477  -0.11659 123 LYS   A CB   
6    C  CG   . LYS   A 18  ? 0.43497 0.94226 0.55149 -0.06791 0.04636  -0.11881 123 LYS   A CG   
7    C  CD   . LYS   A 18  ? 0.42013 0.91137 0.55628 -0.05856 0.04312  -0.12069 123 LYS   A CD   
8    C  CE   . LYS   A 18  ? 0.41433 0.92960 0.57032 -0.05240 0.04439  -0.13160 123 LYS   A CE   
9    N  NZ   . LYS   A 18  ? 0.41415 0.95277 0.57378 -0.04632 0.04719  -0.14945 123 LYS   A NZ   
10   N  N    . LEU   A 19  ? 0.42426 0.89285 0.49243 -0.07658 0.04332  -0.10915 124 LEU   A N    
11   C  CA   . LEU   A 19  ? 0.42904 0.87529 0.48771 -0.07610 0.04110  -0.10559 124 LEU   A CA   
12   C  C    . LEU   A 19  ? 0.42520 0.89013 0.47717 -0.07687 0.04171  -0.11394 124 LEU   A C    
13   O  O    . LEU   A 19  ? 0.44628 0.92506 0.48497 -0.08746 0.04191  -0.10560 124 LEU   A O    
14   C  CB   . LEU   A 19  ? 0.43588 0.86335 0.48038 -0.08688 0.03919  -0.08631 124 LEU   A CB   
15   C  CG   . LEU   A 19  ? 0.42192 0.81984 0.45944 -0.08582 0.03657  -0.08021 124 LEU   A CG   
16   C  CD1  . LEU   A 19  ? 0.38937 0.76726 0.44050 -0.07404 0.03546  -0.08728 124 LEU   A CD1  
17   C  CD2  . LEU   A 19  ? 0.42462 0.80679 0.44997 -0.09704 0.03423  -0.06186 124 LEU   A CD2  
18   N  N    . SER   A 20  ? 0.40628 0.87153 0.46880 -0.06577 0.04115  -0.13025 125 SER   A N    
19   C  CA   . SER   A 20  ? 0.40127 0.88756 0.46137 -0.06511 0.04124  -0.14155 125 SER   A CA   
20   C  C    . SER   A 20  ? 0.42342 0.90184 0.46758 -0.07278 0.03955  -0.13104 125 SER   A C    
21   O  O    . SER   A 20  ? 0.39665 0.85025 0.43256 -0.07697 0.03813  -0.11675 125 SER   A O    
22   C  CB   . SER   A 20  ? 0.39594 0.87826 0.47240 -0.05128 0.03951  -0.16078 125 SER   A CB   
23   O  OG   . SER   A 20  ? 0.38773 0.83977 0.46402 -0.04677 0.03661  -0.15800 125 SER   A OG   
24   N  N    . GLU   A 21  ? 0.44219 0.94345 0.48335 -0.07447 0.03948  -0.13870 126 GLU   A N    
25   C  CA   . GLU   A 21  ? 0.46786 0.96460 0.49712 -0.08056 0.03754  -0.13055 126 GLU   A CA   
26   C  C    . GLU   A 21  ? 0.40502 0.87072 0.43757 -0.07293 0.03513  -0.13203 126 GLU   A C    
27   O  O    . GLU   A 21  ? 0.35627 0.80277 0.37876 -0.07810 0.03366  -0.11844 126 GLU   A O    
28   C  CB   . GLU   A 21  ? 0.54338 1.07302 0.57270 -0.08208 0.03792  -0.14114 126 GLU   A CB   
29   C  CG   . GLU   A 21  ? 0.63020 1.19491 0.65588 -0.09028 0.04040  -0.13999 126 GLU   A CG   
30   C  CD   . GLU   A 21  ? 0.70216 1.27969 0.71262 -0.10421 0.03953  -0.12404 126 GLU   A CD   
31   O  OE1  . GLU   A 21  ? 0.76056 1.37075 0.76960 -0.10798 0.04031  -0.12996 126 GLU   A OE1  
32   O  OE2  . GLU   A 21  ? 0.71262 1.26778 0.71332 -0.11141 0.03769  -0.10562 126 GLU   A OE2  
33   N  N    . GLU   A 22  ? 0.39576 0.85677 0.44332 -0.06067 0.03427  -0.14861 127 GLU   A N    
34   C  CA   . GLU   A 22  ? 0.38909 0.82146 0.44183 -0.05299 0.03164  -0.15060 127 GLU   A CA   
35   C  C    . GLU   A 22  ? 0.33414 0.73722 0.38293 -0.05428 0.03165  -0.13638 127 GLU   A C    
36   O  O    . GLU   A 22  ? 0.30309 0.68419 0.34692 -0.05445 0.03013  -0.12912 127 GLU   A O    
37   C  CB   . GLU   A 22  ? 0.45456 0.88683 0.52651 -0.04002 0.02971  -0.17019 127 GLU   A CB   
38   C  CG   . GLU   A 22  ? 0.51984 0.91954 0.60053 -0.03148 0.02670  -0.17070 127 GLU   A CG   
39   C  CD   . GLU   A 22  ? 0.58496 0.98400 0.68253 -0.02076 0.02267  -0.18894 127 GLU   A CD   
40   O  OE1  . GLU   A 22  ? 0.60767 1.01456 0.70355 -0.02134 0.02111  -0.19411 127 GLU   A OE1  
41   O  OE2  . GLU   A 22  ? 0.61022 1.00072 0.72412 -0.01194 0.02052  -0.19749 127 GLU   A OE2  
42   N  N    . GLN   A 23  ? 0.33294 0.73663 0.38472 -0.05527 0.03333  -0.13235 128 GLN   A N    
43   C  CA   . GLN   A 23  ? 0.30099 0.67901 0.35100 -0.05644 0.03302  -0.11958 128 GLN   A CA   
44   C  C    . GLN   A 23  ? 0.30554 0.67619 0.33793 -0.06844 0.03281  -0.10168 128 GLN   A C    
45   O  O    . GLN   A 23  ? 0.31390 0.65983 0.34214 -0.06911 0.03145  -0.09254 128 GLN   A O    
46   C  CB   . GLN   A 23  ? 0.27367 0.65627 0.33389 -0.05440 0.03428  -0.12019 128 GLN   A CB   
47   C  CG   . GLN   A 23  ? 0.26017 0.64198 0.34088 -0.04135 0.03300  -0.13584 128 GLN   A CG   
48   C  CD   . GLN   A 23  ? 0.29310 0.68484 0.38575 -0.03941 0.03402  -0.13736 128 GLN   A CD   
49   O  OE1  . GLN   A 23  ? 0.29418 0.70269 0.38024 -0.04750 0.03651  -0.13129 128 GLN   A OE1  
50   N  NE2  . GLN   A 23  ? 0.30577 0.68714 0.41721 -0.02885 0.03141  -0.14472 128 GLN   A NE2  
51   N  N    . GLN   A 24  ? 0.30532 0.69725 0.32810 -0.07809 0.03358  -0.09640 129 GLN   A N    
52   C  CA   . GLN   A 24  ? 0.31875 0.70330 0.32633 -0.08963 0.03196  -0.07921 129 GLN   A CA   
53   C  C    . GLN   A 24  ? 0.28913 0.66167 0.29150 -0.08886 0.03006  -0.07784 129 GLN   A C    
54   O  O    . GLN   A 24  ? 0.27833 0.63072 0.27201 -0.09402 0.02808  -0.06475 129 GLN   A O    
55   C  CB   . GLN   A 24  ? 0.38626 0.79847 0.38658 -0.10001 0.03242  -0.07406 129 GLN   A CB   
56   C  CG   . GLN   A 24  ? 0.44591 0.86404 0.44623 -0.10597 0.03328  -0.06649 129 GLN   A CG   
57   C  CD   . GLN   A 24  ? 0.52816 0.97999 0.52497 -0.11396 0.03443  -0.06592 129 GLN   A CD   
58   O  OE1  . GLN   A 24  ? 0.56350 1.01984 0.54975 -0.12568 0.03227  -0.05162 129 GLN   A OE1  
59   N  NE2  . GLN   A 24  ? 0.57576 1.05189 0.58226 -0.10772 0.03743  -0.08146 129 GLN   A NE2  
60   N  N    . HIS   A 25  ? 0.26732 0.65244 0.27578 -0.08250 0.03034  -0.09150 130 HIS   A N    
61   C  CA   . HIS   A 25  ? 0.28835 0.66329 0.29412 -0.08091 0.02870  -0.09129 130 HIS   A CA   
62   C  C    . HIS   A 25  ? 0.27145 0.61550 0.28110 -0.07395 0.02781  -0.09039 130 HIS   A C    
63   O  O    . HIS   A 25  ? 0.27985 0.60636 0.28208 -0.07690 0.02651  -0.08068 130 HIS   A O    
64   C  CB   . HIS   A 25  ? 0.30646 0.70252 0.32050 -0.07497 0.02889  -0.10766 130 HIS   A CB   
65   C  CG   . HIS   A 25  ? 0.33724 0.72685 0.34933 -0.07384 0.02748  -0.10753 130 HIS   A CG   
66   N  ND1  . HIS   A 25  ? 0.35399 0.74302 0.35356 -0.08318 0.02680  -0.09350 130 HIS   A ND1  
67   C  CD2  . HIS   A 25  ? 0.34916 0.73256 0.37105 -0.06446 0.02636  -0.11943 130 HIS   A CD2  
68   C  CE1  . HIS   A 25  ? 0.36399 0.74705 0.36496 -0.07931 0.02609  -0.09677 130 HIS   A CE1  
69   N  NE2  . HIS   A 25  ? 0.35127 0.73116 0.36578 -0.06808 0.02583  -0.11248 130 HIS   A NE2  
70   N  N    . ILE   A 26  ? 0.28087 0.61857 0.30292 -0.06470 0.02836  -0.10015 131 ILE   A N    
71   C  CA   . ILE   A 26  ? 0.25314 0.56366 0.28050 -0.05821 0.02745  -0.09891 131 ILE   A CA   
72   C  C    . ILE   A 26  ? 0.23491 0.52710 0.25137 -0.06589 0.02728  -0.08190 131 ILE   A C    
73   O  O    . ILE   A 26  ? 0.22366 0.49645 0.23636 -0.06560 0.02626  -0.07618 131 ILE   A O    
74   C  CB   . ILE   A 26  ? 0.26047 0.56911 0.30413 -0.04866 0.02750  -0.10914 131 ILE   A CB   
75   C  CG1  . ILE   A 26  ? 0.27471 0.59506 0.33114 -0.03974 0.02606  -0.12700 131 ILE   A CG1  
76   C  CG2  . ILE   A 26  ? 0.25540 0.53764 0.30497 -0.04392 0.02623  -0.10407 131 ILE   A CG2  
77   C  CD1  . ILE   A 26  ? 0.29017 0.60853 0.36465 -0.03025 0.02497  -0.13699 131 ILE   A CD1  
78   N  N    . ILE   A 27  ? 0.21437 0.51279 0.22617 -0.07308 0.02790  -0.07390 132 ILE   A N    
79   C  CA   . ILE   A 27  ? 0.21609 0.49627 0.21936 -0.08043 0.02660  -0.05868 132 ILE   A CA   
80   C  C    . ILE   A 27  ? 0.24575 0.51912 0.23562 -0.08837 0.02456  -0.04781 132 ILE   A C    
81   O  O    . ILE   A 27  ? 0.27700 0.52805 0.26181 -0.09052 0.02282  -0.03881 132 ILE   A O    
82   C  CB   . ILE   A 27  ? 0.24832 0.53784 0.25114 -0.08652 0.02692  -0.05316 132 ILE   A CB   
83   C  CG1  . ILE   A 27  ? 0.25342 0.54560 0.27127 -0.07813 0.02827  -0.06231 132 ILE   A CG1  
84   C  CG2  . ILE   A 27  ? 0.24302 0.51388 0.23689 -0.09517 0.02426  -0.03770 132 ILE   A CG2  
85   C  CD1  . ILE   A 27  ? 0.25932 0.56440 0.27907 -0.08311 0.02891  -0.05889 132 ILE   A CD1  
86   N  N    . ALA   A 28  ? 0.23423 0.52699 0.21919 -0.09286 0.02432  -0.04830 133 ALA   A N    
87   C  CA   . ALA   A 28  ? 0.22883 0.51597 0.20292 -0.10022 0.02174  -0.03726 133 ALA   A CA   
88   C  C    . ALA   A 28  ? 0.24154 0.51171 0.21626 -0.09415 0.02147  -0.03977 133 ALA   A C    
89   O  O    . ALA   A 28  ? 0.23944 0.49110 0.20619 -0.09826 0.01913  -0.02875 133 ALA   A O    
90   C  CB   . ALA   A 28  ? 0.21588 0.53060 0.18682 -0.10570 0.02164  -0.03812 133 ALA   A CB   
91   N  N    . ILE   A 29  ? 0.23294 0.50890 0.21766 -0.08424 0.02334  -0.05431 134 ILE   A N    
92   C  CA   . ILE   A 29  ? 0.22523 0.48638 0.21169 -0.07805 0.02305  -0.05740 134 ILE   A CA   
93   C  C    . ILE   A 29  ? 0.22588 0.46065 0.21181 -0.07602 0.02279  -0.05169 134 ILE   A C    
94   O  O    . ILE   A 29  ? 0.23472 0.45233 0.21392 -0.07691 0.02167  -0.04494 134 ILE   A O    
95   C  CB   . ILE   A 29  ? 0.22498 0.49706 0.22481 -0.06762 0.02393  -0.07484 134 ILE   A CB   
96   C  CG1  . ILE   A 29  ? 0.27984 0.57730 0.27917 -0.06996 0.02404  -0.08022 134 ILE   A CG1  
97   C  CG2  . ILE   A 29  ? 0.18423 0.43758 0.18829 -0.06004 0.02326  -0.07838 134 ILE   A CG2  
98   C  CD1  . ILE   A 29  ? 0.30505 0.61545 0.31908 -0.06018 0.02402  -0.09870 134 ILE   A CD1  
99   N  N    . LEU   A 30  ? 0.21379 0.44568 0.20723 -0.07310 0.02374  -0.05437 135 LEU   A N    
100  C  CA   . LEU   A 30  ? 0.19830 0.40832 0.19439 -0.07120 0.02341  -0.04958 135 LEU   A CA   
101  C  C    . LEU   A 30  ? 0.20088 0.39586 0.18456 -0.08086 0.02128  -0.03438 135 LEU   A C    
102  O  O    . LEU   A 30  ? 0.18511 0.35789 0.16626 -0.07975 0.01925  -0.02919 135 LEU   A O    
103  C  CB   . LEU   A 30  ? 0.18378 0.39620 0.19247 -0.06639 0.02377  -0.05489 135 LEU   A CB   
104  C  CG   . LEU   A 30  ? 0.17094 0.39118 0.19524 -0.05521 0.02413  -0.06964 135 LEU   A CG   
105  C  CD1  . LEU   A 30  ? 0.15929 0.37863 0.19672 -0.05054 0.02319  -0.07234 135 LEU   A CD1  
106  C  CD2  . LEU   A 30  ? 0.14223 0.34996 0.17204 -0.04884 0.02298  -0.07326 135 LEU   A CD2  
107  N  N    . LEU   A 31  ? 0.21558 0.41899 0.19221 -0.08924 0.01989  -0.02724 136 LEU   A N    
108  C  CA   . LEU   A 31  ? 0.24225 0.42967 0.20867 -0.09821 0.01617  -0.01296 136 LEU   A CA   
109  C  C    . LEU   A 31  ? 0.25909 0.43631 0.21712 -0.10004 0.01417  -0.00707 136 LEU   A C    
110  O  O    . LEU   A 31  ? 0.26416 0.41897 0.21773 -0.10212 0.01143  0.00083  136 LEU   A O    
111  C  CB   . LEU   A 31  ? 0.25403 0.45464 0.21614 -0.10684 0.01437  -0.00643 136 LEU   A CB   
112  C  CG   . LEU   A 31  ? 0.23901 0.44617 0.20762 -0.10666 0.01551  -0.00908 136 LEU   A CG   
113  C  CD1  . LEU   A 31  ? 0.24783 0.47432 0.21286 -0.11473 0.01461  -0.00433 136 LEU   A CD1  
114  C  CD2  . LEU   A 31  ? 0.25983 0.44338 0.22869 -0.10820 0.01277  -0.00286 136 LEU   A CD2  
115  N  N    . ASP   A 32  ? 0.25965 0.45307 0.21634 -0.09901 0.01501  -0.01127 137 ASP   A N    
116  C  CA   . ASP   A 32  ? 0.27980 0.46491 0.22894 -0.10014 0.01272  -0.00582 137 ASP   A CA   
117  C  C    . ASP   A 32  ? 0.27379 0.44072 0.22377 -0.09210 0.01388  -0.01021 137 ASP   A C    
118  O  O    . ASP   A 32  ? 0.27045 0.41541 0.21539 -0.09213 0.00943  -0.00231 137 ASP   A O    
119  C  CB   . ASP   A 32  ? 0.30574 0.51453 0.25535 -0.10018 0.01355  -0.01105 137 ASP   A CB   
120  C  CG   . ASP   A 32  ? 0.35655 0.55829 0.29876 -0.10121 0.01081  -0.00527 137 ASP   A CG   
121  O  OD1  . ASP   A 32  ? 0.36103 0.56705 0.30626 -0.09405 0.01252  -0.01469 137 ASP   A OD1  
122  O  OD2  . ASP   A 32  ? 0.38299 0.57410 0.31727 -0.10889 0.00610  0.00865  137 ASP   A OD2  
123  N  N    . ALA   A 33  ? 0.27019 0.44110 0.23124 -0.08239 0.01668  -0.02328 138 ALA   A N    
124  C  CA   . ALA   A 33  ? 0.24316 0.39251 0.21029 -0.07226 0.01453  -0.02742 138 ALA   A CA   
125  C  C    . ALA   A 33  ? 0.25139 0.37465 0.21754 -0.07214 0.01138  -0.01943 138 ALA   A C    
126  O  O    . ALA   A 33  ? 0.23830 0.34212 0.20311 -0.06801 0.00857  -0.01669 138 ALA   A O    
127  C  CB   . ALA   A 33  ? 0.22223 0.38003 0.20366 -0.06312 0.01684  -0.04107 138 ALA   A CB   
128  N  N    . HIS   A 34  ? 0.22325 0.34723 0.19056 -0.07653 0.01176  -0.01648 139 HIS   A N    
129  C  CA   . HIS   A 34  ? 0.23393 0.33489 0.19947 -0.07700 0.00848  -0.01022 139 HIS   A CA   
130  C  C    . HIS   A 34  ? 0.26003 0.34676 0.21590 -0.08291 0.00427  0.00026  139 HIS   A C    
131  O  O    . HIS   A 34  ? 0.25197 0.31729 0.20699 -0.07895 0.00124  0.00242  139 HIS   A O    
132  C  CB   . HIS   A 34  ? 0.24513 0.35183 0.21366 -0.08166 0.00904  -0.00938 139 HIS   A CB   
133  C  CG   . HIS   A 34  ? 0.26506 0.35009 0.23188 -0.08196 0.00551  -0.00514 139 HIS   A CG   
134  N  ND1  . HIS   A 34  ? 0.26357 0.33243 0.23302 -0.07367 0.00458  -0.00823 139 HIS   A ND1  
135  C  CD2  . HIS   A 34  ? 0.27654 0.35485 0.23965 -0.08976 0.00253  0.00123  139 HIS   A CD2  
136  C  CE1  . HIS   A 34  ? 0.27383 0.32811 0.24035 -0.07584 0.00162  -0.00503 139 HIS   A CE1  
137  N  NE2  . HIS   A 34  ? 0.27936 0.33772 0.24245 -0.08537 -0.00007 0.00034  139 HIS   A NE2  
138  N  N    A HIS   A 35  ? 0.27976 0.37918 0.22916 -0.09245 0.00369  0.00710  140 HIS   A N    
139  N  N    B HIS   A 35  ? 0.27964 0.37928 0.22908 -0.09250 0.00373  0.00706  140 HIS   A N    
140  C  CA   A HIS   A 35  ? 0.29471 0.38026 0.23662 -0.09878 -0.00181 0.01871  140 HIS   A CA   
141  C  CA   B HIS   A 35  ? 0.29500 0.38207 0.23673 -0.09912 -0.00164 0.01874  140 HIS   A CA   
142  C  C    A HIS   A 35  ? 0.28874 0.36333 0.22907 -0.09239 -0.00392 0.01846  140 HIS   A C    
143  C  C    B HIS   A 35  ? 0.28848 0.36325 0.22889 -0.09236 -0.00385 0.01833  140 HIS   A C    
144  O  O    A HIS   A 35  ? 0.29009 0.34429 0.22857 -0.09247 -0.00918 0.02509  140 HIS   A O    
145  O  O    B HIS   A 35  ? 0.28975 0.34361 0.22857 -0.09215 -0.00902 0.02465  140 HIS   A O    
146  C  CB   A HIS   A 35  ? 0.31380 0.41881 0.24937 -0.11124 -0.00220 0.02758  140 HIS   A CB   
147  C  CB   B HIS   A 35  ? 0.31197 0.42083 0.24739 -0.11090 -0.00142 0.02654  140 HIS   A CB   
148  C  CG   A HIS   A 35  ? 0.33022 0.44296 0.26831 -0.11713 -0.00213 0.02921  140 HIS   A CG   
149  C  CG   B HIS   A 35  ? 0.33000 0.42899 0.25836 -0.11791 -0.00795 0.03978  140 HIS   A CG   
150  N  ND1  A HIS   A 35  ? 0.34161 0.43788 0.28344 -0.11734 -0.00394 0.02961  140 HIS   A ND1  
151  N  ND1  B HIS   A 35  ? 0.34803 0.42926 0.27632 -0.12364 -0.01482 0.04974  140 HIS   A ND1  
152  C  CD2  A HIS   A 35  ? 0.34713 0.48188 0.28521 -0.12155 -0.00141 0.02942  140 HIS   A CD2  
153  C  CD2  B HIS   A 35  ? 0.33910 0.44304 0.26236 -0.11853 -0.01020 0.04375  140 HIS   A CD2  
154  C  CE1  A HIS   A 35  ? 0.34834 0.45560 0.29159 -0.12158 -0.00420 0.03067  140 HIS   A CE1  
155  C  CE1  B HIS   A 35  ? 0.35673 0.43182 0.28119 -0.12732 -0.02114 0.05975  140 HIS   A CE1  
156  N  NE2  A HIS   A 35  ? 0.35147 0.48215 0.29258 -0.12433 -0.00253 0.03085  140 HIS   A NE2  
157  N  NE2  B HIS   A 35  ? 0.35192 0.44108 0.27294 -0.12472 -0.01840 0.05684  140 HIS   A NE2  
158  N  N    . LYS   A 36  ? 0.27516 0.36283 0.21766 -0.08649 -0.00042 0.01017  141 LYS   A N    
159  C  CA   . LYS   A 36  ? 0.28866 0.36775 0.23070 -0.08063 -0.00256 0.00946  141 LYS   A CA   
160  C  C    . LYS   A 36  ? 0.28876 0.34855 0.23796 -0.07051 -0.00277 0.00433  141 LYS   A C    
161  O  O    . LYS   A 36  ? 0.28124 0.33065 0.23094 -0.06601 -0.00526 0.00535  141 LYS   A O    
162  C  CB   . LYS   A 36  ? 0.29795 0.39930 0.23992 -0.07887 0.00054  0.00183  141 LYS   A CB   
163  C  CG   . LYS   A 36  ? 0.35338 0.47460 0.28544 -0.08907 -0.00017 0.00869  141 LYS   A CG   
164  C  CD   . LYS   A 36  ? 0.38666 0.53526 0.31903 -0.08742 0.00415  -0.00234 141 LYS   A CD   
165  C  CE   . LYS   A 36  ? 0.43560 0.60006 0.36138 -0.09464 0.00202  0.00448  141 LYS   A CE   
166  N  NZ   . LYS   A 36  ? 0.47921 0.64462 0.40098 -0.10561 -0.00112 0.01846  141 LYS   A NZ   
167  N  N    . THR   A 37  ? 0.26847 0.32472 0.22329 -0.06727 -0.00044 -0.00045 142 THR   A N    
168  C  CA   . THR   A 37  ? 0.25882 0.30078 0.21989 -0.05854 -0.00023 -0.00465 142 THR   A CA   
169  C  C    . THR   A 37  ? 0.27871 0.30518 0.23913 -0.05892 -0.00177 -0.00206 142 THR   A C    
170  O  O    . THR   A 37  ? 0.28488 0.30211 0.24948 -0.05235 -0.00118 -0.00531 142 THR   A O    
171  C  CB   . THR   A 37  ? 0.24910 0.30174 0.21923 -0.05267 0.00334  -0.01376 142 THR   A CB   
172  O  OG1  . THR   A 37  ? 0.24936 0.31421 0.22116 -0.05642 0.00548  -0.01583 142 THR   A OG1  
173  C  CG2  . THR   A 37  ? 0.23421 0.29888 0.20700 -0.05007 0.00405  -0.01896 142 THR   A CG2  
174  N  N    . TYR   A 38  ? 0.28534 0.31001 0.24097 -0.06676 -0.00390 0.00343  143 TYR   A N    
175  C  CA   . TYR   A 38  ? 0.29567 0.30471 0.25056 -0.06755 -0.00650 0.00491  143 TYR   A CA   
176  C  C    . TYR   A 38  ? 0.32499 0.32126 0.27554 -0.07312 -0.01232 0.01306  143 TYR   A C    
177  O  O    . TYR   A 38  ? 0.34062 0.34418 0.28758 -0.08215 -0.01424 0.01994  143 TYR   A O    
178  C  CB   . TYR   A 38  ? 0.27866 0.29572 0.23450 -0.07212 -0.00510 0.00348  143 TYR   A CB   
179  C  CG   . TYR   A 38  ? 0.27059 0.27298 0.22631 -0.07101 -0.00737 0.00198  143 TYR   A CG   
180  C  CD1  . TYR   A 38  ? 0.28928 0.27701 0.24184 -0.07603 -0.01270 0.00645  143 TYR   A CD1  
181  C  CD2  . TYR   A 38  ? 0.22603 0.22937 0.18519 -0.06497 -0.00490 -0.00400 143 TYR   A CD2  
182  C  CE1  . TYR   A 38  ? 0.29033 0.26535 0.24286 -0.07455 -0.01508 0.00294  143 TYR   A CE1  
183  C  CE2  . TYR   A 38  ? 0.23201 0.22438 0.18964 -0.06409 -0.00691 -0.00617 143 TYR   A CE2  
184  C  CZ   . TYR   A 38  ? 0.26843 0.24692 0.22258 -0.06861 -0.01179 -0.00372 143 TYR   A CZ   
185  O  OH   . TYR   A 38  ? 0.30568 0.27397 0.25844 -0.06747 -0.01412 -0.00791 143 TYR   A OH   
186  N  N    . ASP   A 39  ? 0.33124 0.30945 0.28318 -0.06787 -0.01546 0.01254  144 ASP   A N    
187  C  CA   . ASP   A 39  ? 0.35900 0.32199 0.30986 -0.07163 -0.02241 0.01962  144 ASP   A CA   
188  C  C    . ASP   A 39  ? 0.38048 0.32896 0.33252 -0.07330 -0.02598 0.01793  144 ASP   A C    
189  O  O    . ASP   A 39  ? 0.39559 0.33329 0.35036 -0.06569 -0.02583 0.01095  144 ASP   A O    
190  C  CB   . ASP   A 39  ? 0.38043 0.33381 0.33424 -0.06396 -0.02431 0.01908  144 ASP   A CB   
191  C  CG   . ASP   A 39  ? 0.40995 0.34491 0.36570 -0.06592 -0.03264 0.02535  144 ASP   A CG   
192  O  OD1  . ASP   A 39  ? 0.40610 0.33653 0.36028 -0.07493 -0.03770 0.03249  144 ASP   A OD1  
193  O  OD2  . ASP   A 39  ? 0.41329 0.33845 0.37360 -0.05842 -0.03467 0.02339  144 ASP   A OD2  
194  N  N    . PRO   A 40  ? 0.37521 0.32405 0.32554 -0.08333 -0.02939 0.02369  145 PRO   A N    
195  C  CA   . PRO   A 40  ? 0.38680 0.32195 0.33890 -0.08536 -0.03347 0.02093  145 PRO   A CA   
196  C  C    . PRO   A 40  ? 0.41797 0.32987 0.37413 -0.08318 -0.04142 0.02172  145 PRO   A C    
197  O  O    . PRO   A 40  ? 0.42321 0.32220 0.38176 -0.08445 -0.04585 0.01798  145 PRO   A O    
198  C  CB   . PRO   A 40  ? 0.37587 0.32036 0.32622 -0.09804 -0.03528 0.02855  145 PRO   A CB   
199  C  CG   . PRO   A 40  ? 0.38060 0.33591 0.32832 -0.10370 -0.03568 0.03847  145 PRO   A CG   
200  C  CD   . PRO   A 40  ? 0.38014 0.34339 0.32706 -0.09393 -0.02997 0.03312  145 PRO   A CD   
201  N  N    . THR   A 41  ? 0.42406 0.33033 0.38215 -0.07984 -0.04406 0.02594  146 THR   A N    
202  C  CA   . THR   A 41  ? 0.44401 0.32852 0.40862 -0.07492 -0.05139 0.02445  146 THR   A CA   
203  C  C    . THR   A 41  ? 0.43294 0.31432 0.40045 -0.06179 -0.04708 0.01214  146 THR   A C    
204  O  O    . THR   A 41  ? 0.45521 0.32018 0.42897 -0.05628 -0.05204 0.00657  146 THR   A O    
205  C  CB   . THR   A 41  ? 0.45939 0.33912 0.42620 -0.07788 -0.05772 0.03603  146 THR   A CB   
206  O  OG1  . THR   A 41  ? 0.44077 0.33013 0.40665 -0.07033 -0.05268 0.03415  146 THR   A OG1  
207  C  CG2  . THR   A 41  ? 0.47229 0.36297 0.43412 -0.09160 -0.05985 0.04933  146 THR   A CG2  
208  N  N    . TYR   A 42  ? 0.39673 0.29423 0.36088 -0.05688 -0.03831 0.00766  147 TYR   A N    
209  C  CA   . TYR   A 42  ? 0.37656 0.27506 0.34313 -0.04583 -0.03347 -0.00246 147 TYR   A CA   
210  C  C    . TYR   A 42  ? 0.39325 0.28111 0.36670 -0.03847 -0.03716 -0.00318 147 TYR   A C    
211  O  O    . TYR   A 42  ? 0.37713 0.26016 0.35481 -0.03003 -0.03618 -0.01233 147 TYR   A O    
212  C  CB   . TYR   A 42  ? 0.37074 0.26542 0.33649 -0.04380 -0.03260 -0.01209 147 TYR   A CB   
213  C  CG   . TYR   A 42  ? 0.37411 0.27852 0.33443 -0.05140 -0.03031 -0.01093 147 TYR   A CG   
214  C  CD1  . TYR   A 42  ? 0.38756 0.28354 0.34743 -0.05926 -0.03605 -0.00928 147 TYR   A CD1  
215  C  CD2  . TYR   A 42  ? 0.35933 0.28131 0.31674 -0.05077 -0.02319 -0.01123 147 TYR   A CD2  
216  C  CE1  . TYR   A 42  ? 0.39293 0.29946 0.34901 -0.06628 -0.03408 -0.00804 147 TYR   A CE1  
217  C  CE2  . TYR   A 42  ? 0.36155 0.29330 0.31597 -0.05695 -0.02153 -0.01033 147 TYR   A CE2  
218  C  CZ   . TYR   A 42  ? 0.37489 0.29973 0.32836 -0.06469 -0.02666 -0.00875 147 TYR   A CZ   
219  O  OH   . TYR   A 42  ? 0.38563 0.32187 0.33720 -0.07079 -0.02502 -0.00783 147 TYR   A OH   
220  N  N    . ALA   A 43  ? 0.40828 0.29425 0.38312 -0.04167 -0.04154 0.00643  148 ALA   A N    
221  C  CA   . ALA   A 43  ? 0.42226 0.29744 0.40519 -0.03511 -0.04663 0.00695  148 ALA   A CA   
222  C  C    . ALA   A 43  ? 0.42645 0.31111 0.41235 -0.02521 -0.04019 0.00056  148 ALA   A C    
223  O  O    . ALA   A 43  ? 0.41206 0.28916 0.40631 -0.01714 -0.04265 -0.00370 148 ALA   A O    
224  C  CB   . ALA   A 43  ? 0.42242 0.29556 0.40534 -0.04189 -0.05336 0.02039  148 ALA   A CB   
225  N  N    . ASP   A 44  ? 0.41945 0.32087 0.40025 -0.02568 -0.03247 -0.00019 149 ASP   A N    
226  C  CA   . ASP   A 44  ? 0.40452 0.31533 0.38923 -0.01778 -0.02717 -0.00439 149 ASP   A CA   
227  C  C    . ASP   A 44  ? 0.38748 0.29883 0.37533 -0.01019 -0.02292 -0.01466 149 ASP   A C    
228  O  O    . ASP   A 44  ? 0.37322 0.29088 0.36652 -0.00321 -0.01963 -0.01790 149 ASP   A O    
229  C  CB   . ASP   A 44  ? 0.40192 0.32915 0.38227 -0.02072 -0.02146 -0.00239 149 ASP   A CB   
230  C  CG   . ASP   A 44  ? 0.44910 0.38065 0.42620 -0.02708 -0.02465 0.00604  149 ASP   A CG   
231  O  OD1  . ASP   A 44  ? 0.47176 0.39573 0.45152 -0.02720 -0.03079 0.01147  149 ASP   A OD1  
232  O  OD2  . ASP   A 44  ? 0.45313 0.39692 0.42545 -0.03181 -0.02125 0.00700  149 ASP   A OD2  
233  N  N    . PHE   A 45  ? 0.37774 0.28442 0.36222 -0.01186 -0.02299 -0.01978 150 PHE   A N    
234  C  CA   . PHE   A 45  ? 0.38194 0.29289 0.36730 -0.00551 -0.01847 -0.02991 150 PHE   A CA   
235  C  C    . PHE   A 45  ? 0.39772 0.30380 0.39219 0.00375  -0.01998 -0.03626 150 PHE   A C    
236  O  O    . PHE   A 45  ? 0.39108 0.30668 0.38712 0.00994  -0.01465 -0.04404 150 PHE   A O    
237  C  CB   . PHE   A 45  ? 0.37713 0.28252 0.35735 -0.00925 -0.02003 -0.03496 150 PHE   A CB   
238  C  CG   . PHE   A 45  ? 0.37434 0.29008 0.34672 -0.01610 -0.01631 -0.03184 150 PHE   A CG   
239  C  CD1  . PHE   A 45  ? 0.37749 0.29955 0.34779 -0.02179 -0.01556 -0.02320 150 PHE   A CD1  
240  C  CD2  . PHE   A 45  ? 0.35215 0.27215 0.31983 -0.01668 -0.01408 -0.03826 150 PHE   A CD2  
241  C  CE1  . PHE   A 45  ? 0.37233 0.30447 0.33773 -0.02715 -0.01254 -0.02147 150 PHE   A CE1  
242  C  CE2  . PHE   A 45  ? 0.34993 0.27949 0.31212 -0.02262 -0.01155 -0.03510 150 PHE   A CE2  
243  C  CZ   . PHE   A 45  ? 0.34870 0.28397 0.31062 -0.02752 -0.01081 -0.02691 150 PHE   A CZ   
244  N  N    . ARG   A 46  ? 0.44520 0.33809 0.44637 0.00474  -0.02733 -0.03285 151 ARG   A N    
245  C  CA   . ARG   A 46  ? 0.48801 0.37669 0.50031 0.01442  -0.02939 -0.03935 151 ARG   A CA   
246  C  C    . ARG   A 46  ? 0.44383 0.34699 0.46066 0.01960  -0.02404 -0.03792 151 ARG   A C    
247  O  O    . ARG   A 46  ? 0.44442 0.35021 0.47068 0.02835  -0.02325 -0.04473 151 ARG   A O    
248  C  CB   . ARG   A 46  ? 0.58055 0.45010 0.60065 0.01380  -0.04031 -0.03463 151 ARG   A CB   
249  C  CG   . ARG   A 46  ? 0.66088 0.53062 0.68201 0.00988  -0.04413 -0.02148 151 ARG   A CG   
250  C  CD   . ARG   A 46  ? 0.73257 0.60518 0.76539 0.01895  -0.04504 -0.02284 151 ARG   A CD   
251  N  NE   . ARG   A 46  ? 0.79604 0.66347 0.83211 0.01568  -0.05255 -0.01082 151 ARG   A NE   
252  C  CZ   . ARG   A 46  ? 0.85422 0.72456 0.90024 0.02196  -0.05472 -0.00935 151 ARG   A CZ   
253  N  NH1  . ARG   A 46  ? 0.88783 0.75425 0.93545 0.01799  -0.06229 0.00243  151 ARG   A NH1  
254  N  NH2  . ARG   A 46  ? 0.84604 0.72518 0.90037 0.03178  -0.04935 -0.01925 151 ARG   A NH2  
255  N  N    . ASP   A 47  ? 0.41549 0.32872 0.42703 0.01446  -0.02065 -0.02990 152 ASP   A N    
256  C  CA   . ASP   A 47  ? 0.39662 0.32338 0.41308 0.01827  -0.01618 -0.02833 152 ASP   A CA   
257  C  C    . ASP   A 47  ? 0.36126 0.30345 0.37672 0.02115  -0.00775 -0.03403 152 ASP   A C    
258  O  O    . ASP   A 47  ? 0.35095 0.30470 0.37285 0.02505  -0.00418 -0.03369 152 ASP   A O    
259  C  CB   . ASP   A 47  ? 0.41503 0.34666 0.42733 0.01179  -0.01656 -0.01899 152 ASP   A CB   
260  C  CG   . ASP   A 47  ? 0.47375 0.39431 0.48565 0.00762  -0.02468 -0.01140 152 ASP   A CG   
261  O  OD1  . ASP   A 47  ? 0.49893 0.40777 0.51763 0.01130  -0.03082 -0.01193 152 ASP   A OD1  
262  O  OD2  . ASP   A 47  ? 0.48740 0.41209 0.49283 0.00066  -0.02523 -0.00486 152 ASP   A OD2  
263  N  N    . PHE   A 48  ? 0.34151 0.28517 0.34922 0.01848  -0.00498 -0.03808 153 PHE   A N    
264  C  CA   . PHE   A 48  ? 0.31198 0.27167 0.31743 0.01965  0.00235  -0.04128 153 PHE   A CA   
265  C  C    . PHE   A 48  ? 0.31824 0.28460 0.32948 0.02783  0.00515  -0.05081 153 PHE   A C    
266  O  O    . PHE   A 48  ? 0.35115 0.30713 0.36713 0.03269  0.00105  -0.05759 153 PHE   A O    
267  C  CB   . PHE   A 48  ? 0.30172 0.26193 0.29690 0.01403  0.00364  -0.04237 153 PHE   A CB   
268  C  CG   . PHE   A 48  ? 0.30097 0.25627 0.29098 0.00624  0.00112  -0.03479 153 PHE   A CG   
269  C  CD1  . PHE   A 48  ? 0.31100 0.26286 0.29329 0.00087  0.00007  -0.03567 153 PHE   A CD1  
270  C  CD2  . PHE   A 48  ? 0.30365 0.25994 0.29676 0.00429  -0.00006 -0.02766 153 PHE   A CD2  
271  C  CE1  . PHE   A 48  ? 0.31884 0.26923 0.29734 -0.00609 -0.00165 -0.02943 153 PHE   A CE1  
272  C  CE2  . PHE   A 48  ? 0.31709 0.27208 0.30552 -0.00248 -0.00176 -0.02236 153 PHE   A CE2  
273  C  CZ   . PHE   A 48  ? 0.32100 0.27366 0.30245 -0.00760 -0.00226 -0.02316 153 PHE   A CZ   
274  N  N    . ARG   A 49  ? 0.28826 0.27315 0.29990 0.02918  0.01194  -0.05139 154 ARG   A N    
275  C  CA   . ARG   A 49  ? 0.30841 0.30472 0.32348 0.03607  0.01599  -0.06139 154 ARG   A CA   
276  C  C    . ARG   A 49  ? 0.34024 0.33009 0.34782 0.03636  0.01457  -0.07142 154 ARG   A C    
277  O  O    . ARG   A 49  ? 0.30710 0.29157 0.30517 0.02978  0.01320  -0.06864 154 ARG   A O    
278  C  CB   . ARG   A 49  ? 0.30546 0.32509 0.32039 0.03511  0.02347  -0.05806 154 ARG   A CB   
279  C  CG   . ARG   A 49  ? 0.28930 0.31707 0.31503 0.03640  0.02471  -0.05085 154 ARG   A CG   
280  C  CD   . ARG   A 49  ? 0.27792 0.32621 0.30366 0.03260  0.03050  -0.04399 154 ARG   A CD   
281  N  NE   . ARG   A 49  ? 0.27071 0.31466 0.29077 0.02486  0.02888  -0.03498 154 ARG   A NE   
282  C  CZ   . ARG   A 49  ? 0.24113 0.29899 0.26007 0.02017  0.03201  -0.02805 154 ARG   A CZ   
283  N  NH1  . ARG   A 49  ? 0.22084 0.29925 0.24230 0.02131  0.03736  -0.02790 154 ARG   A NH1  
284  N  NH2  . ARG   A 49  ? 0.21711 0.26944 0.23332 0.01422  0.02948  -0.02099 154 ARG   A NH2  
285  N  N    . PRO   A 50  ? 0.37412 0.36458 0.38693 0.04412  0.01438  -0.08398 155 PRO   A N    
286  C  CA   . PRO   A 50  ? 0.37804 0.35723 0.38634 0.04499  0.01052  -0.09511 155 PRO   A CA   
287  C  C    . PRO   A 50  ? 0.37100 0.36345 0.36660 0.04076  0.01517  -0.09852 155 PRO   A C    
288  O  O    . PRO   A 50  ? 0.35276 0.36811 0.34555 0.04127  0.02252  -0.09831 155 PRO   A O    
289  C  CB   . PRO   A 50  ? 0.40166 0.38264 0.42144 0.05597  0.01000  -0.10925 155 PRO   A CB   
290  C  CG   . PRO   A 50  ? 0.40937 0.39575 0.44096 0.06005  0.01108  -0.10281 155 PRO   A CG   
291  C  CD   . PRO   A 50  ? 0.39037 0.39010 0.41592 0.05293  0.01643  -0.08916 155 PRO   A CD   
292  N  N    . PRO   A 51  ? 0.38420 0.36367 0.37226 0.03605  0.01054  -0.10118 156 PRO   A N    
293  C  CA   . PRO   A 51  ? 0.40005 0.39202 0.37650 0.03293  0.01380  -0.10683 156 PRO   A CA   
294  C  C    . PRO   A 51  ? 0.43282 0.43819 0.41062 0.04108  0.01713  -0.12371 156 PRO   A C    
295  O  O    . PRO   A 51  ? 0.44734 0.44221 0.43483 0.04739  0.01325  -0.13115 156 PRO   A O    
296  C  CB   . PRO   A 51  ? 0.40969 0.38159 0.38111 0.02691  0.00641  -0.10726 156 PRO   A CB   
297  C  CG   . PRO   A 51  ? 0.41435 0.36498 0.39396 0.02580  -0.00013 -0.09963 156 PRO   A CG   
298  C  CD   . PRO   A 51  ? 0.40674 0.36032 0.39780 0.03379  0.00141  -0.10037 156 PRO   A CD   
299  N  N    . VAL   A 52  ? 0.46015 0.48931 0.42898 0.03911  0.02367  -0.12421 157 VAL   A N    
300  C  CA   . VAL   A 52  ? 0.51209 0.55590 0.48029 0.04330  0.02639  -0.13385 157 VAL   A CA   
301  C  C    . VAL   A 52  ? 0.57899 0.63055 0.53347 0.03716  0.02642  -0.13534 157 VAL   A C    
302  O  O    . VAL   A 52  ? 0.53772 0.60395 0.48345 0.03098  0.03012  -0.12600 157 VAL   A O    
303  C  CB   . VAL   A 52  ? 0.48584 0.55547 0.45841 0.04679  0.03429  -0.13123 157 VAL   A CB   
304  C  CG1  . VAL   A 52  ? 0.48889 0.57336 0.46197 0.05139  0.03646  -0.14284 157 VAL   A CG1  
305  C  CG2  . VAL   A 52  ? 0.47443 0.53678 0.46110 0.05227  0.03387  -0.12829 157 VAL   A CG2  
306  N  N    . ARG   A 53  ? 0.69008 0.73201 0.64372 0.03875  0.02173  -0.14644 158 ARG   A N    
307  C  CA   . ARG   A 53  ? 0.79341 0.84007 0.73498 0.03310  0.02038  -0.14879 158 ARG   A CA   
308  C  C    . ARG   A 53  ? 0.97541 1.03842 0.91518 0.03698  0.02254  -0.16073 158 ARG   A C    
309  O  O    . ARG   A 53  ? 0.97789 1.06128 0.90740 0.03286  0.02602  -0.15872 158 ARG   A O    
310  C  CB   . ARG   A 53  ? 0.74604 0.76558 0.68702 0.02928  0.01169  -0.15060 158 ARG   A CB   
311  C  CG   . ARG   A 53  ? 0.68695 0.69435 0.62661 0.02302  0.00947  -0.13861 158 ARG   A CG   
312  C  CD   . ARG   A 53  ? 0.66076 0.64257 0.60142 0.01856  0.00057  -0.13973 158 ARG   A CD   
313  N  NE   . ARG   A 53  ? 0.61906 0.59335 0.55754 0.01128  -0.00128 -0.12859 158 ARG   A NE   
314  C  CZ   . ARG   A 53  ? 0.58858 0.54740 0.53546 0.01114  -0.00423 -0.12185 158 ARG   A CZ   
315  N  NH1  . ARG   A 53  ? 0.56780 0.51614 0.52565 0.01835  -0.00634 -0.12659 158 ARG   A NH1  
316  N  NH2  . ARG   A 53  ? 0.57330 0.52808 0.51846 0.00349  -0.00512 -0.10700 158 ARG   A NH2  
317  N  N    . MET   A 54  ? 1.15115 1.20654 1.10138 0.04468  0.02012  -0.17284 159 MET   A N    
318  C  CA   . MET   A 54  ? 1.30760 1.37469 1.25783 0.04903  0.02047  -0.18753 159 MET   A CA   
319  C  C    . MET   A 54  ? 1.32417 1.42302 1.26345 0.04611  0.02719  -0.18696 159 MET   A C    
320  O  O    . MET   A 54  ? 1.33850 1.44152 1.26663 0.04053  0.02573  -0.18733 159 MET   A O    
321  C  CB   . MET   A 54  ? 1.43153 1.49837 1.39696 0.05890  0.02063  -0.19714 159 MET   A CB   
322  C  CG   . MET   A 54  ? 1.54747 1.59128 1.52262 0.06357  0.01211  -0.20961 159 MET   A CG   
323  S  SD   . MET   A 54  ? 1.57736 1.58337 1.55797 0.05962  0.00269  -0.20033 159 MET   A SD   
324  C  CE   . MET   A 54  ? 1.57188 1.57407 1.56796 0.06636  0.00375  -0.19464 159 MET   A CE   
325  N  N    . SER   A 66  ? 1.12152 1.40939 1.01312 -0.00914 0.05463  -0.07401 218 SER   A N    
326  C  CA   . SER   A 66  ? 1.09257 1.36372 0.99131 0.00003  0.05655  -0.08792 218 SER   A CA   
327  C  C    . SER   A 66  ? 0.99878 1.25276 0.90673 0.00071  0.05659  -0.07788 218 SER   A C    
328  O  O    . SER   A 66  ? 0.99918 1.24698 0.90678 -0.00534 0.05386  -0.06320 218 SER   A O    
329  C  CB   . SER   A 66  ? 1.13080 1.38156 1.02528 0.00421  0.05275  -0.10430 218 SER   A CB   
330  O  OG   . SER   A 66  ? 1.13035 1.36539 1.01944 -0.00120 0.04762  -0.09713 218 SER   A OG   
331  N  N    . PRO   A 67  ? 0.92322 1.17041 0.84032 0.00821  0.05938  -0.08598 219 PRO   A N    
332  C  CA   . PRO   A 67  ? 0.83279 1.06666 0.75944 0.00910  0.05985  -0.07697 219 PRO   A CA   
333  C  C    . PRO   A 67  ? 0.71788 0.92599 0.64282 0.00726  0.05516  -0.07383 219 PRO   A C    
334  O  O    . PRO   A 67  ? 0.72060 0.91542 0.63886 0.00754  0.05136  -0.08244 219 PRO   A O    
335  C  CB   . PRO   A 67  ? 0.85929 1.08855 0.79552 0.01869  0.06247  -0.09047 219 PRO   A CB   
336  C  CG   . PRO   A 67  ? 0.90554 1.13659 0.83688 0.02326  0.06157  -0.10840 219 PRO   A CG   
337  C  CD   . PRO   A 67  ? 0.93979 1.19338 0.86040 0.01629  0.06210  -0.10338 219 PRO   A CD   
338  N  N    . LEU   A 68  ? 0.59210 0.79427 0.52375 0.00490  0.05526  -0.06103 220 LEU   A N    
339  C  CA   . LEU   A 68  ? 0.48586 0.66563 0.41766 0.00338  0.05147  -0.05772 220 LEU   A CA   
340  C  C    . LEU   A 68  ? 0.41263 0.57288 0.35171 0.01113  0.05127  -0.06893 220 LEU   A C    
341  O  O    . LEU   A 68  ? 0.35486 0.50764 0.30239 0.01218  0.05184  -0.06332 220 LEU   A O    
342  C  CB   . LEU   A 68  ? 0.46977 0.65367 0.40662 -0.00301 0.05112  -0.03875 220 LEU   A CB   
343  C  CG   . LEU   A 68  ? 0.49160 0.69511 0.42501 -0.01067 0.05015  -0.02516 220 LEU   A CG   
344  C  CD1  . LEU   A 68  ? 0.48923 0.69362 0.43201 -0.01607 0.04859  -0.00652 220 LEU   A CD1  
345  C  CD2  . LEU   A 68  ? 0.48997 0.69119 0.41215 -0.01460 0.04591  -0.02712 220 LEU   A CD2  
346  N  N    . SER   A 69  ? 0.40765 0.55944 0.34447 0.01652  0.04961  -0.08488 221 SER   A N    
347  C  CA   . SER   A 69  ? 0.40369 0.53813 0.34960 0.02460  0.04831  -0.09591 221 SER   A CA   
348  C  C    . SER   A 69  ? 0.37978 0.49003 0.32818 0.02387  0.04403  -0.09372 221 SER   A C    
349  O  O    . SER   A 69  ? 0.37419 0.47060 0.33304 0.02928  0.04247  -0.09665 221 SER   A O    
350  C  CB   . SER   A 69  ? 0.42998 0.55849 0.37396 0.02953  0.04573  -0.11235 221 SER   A CB   
351  O  OG   . SER   A 69  ? 0.45161 0.57187 0.38513 0.02469  0.04138  -0.11449 221 SER   A OG   
352  N  N    . MET   A 70  ? 0.36226 0.46477 0.30322 0.01659  0.04049  -0.08619 222 MET   A N    
353  C  CA   . MET   A 70  ? 0.33557 0.41171 0.28096 0.01407  0.03437  -0.07996 222 MET   A CA   
354  C  C    . MET   A 70  ? 0.30073 0.37652 0.25325 0.01033  0.03466  -0.06357 222 MET   A C    
355  O  O    . MET   A 70  ? 0.30829 0.36537 0.26494 0.00851  0.03030  -0.05858 222 MET   A O    
356  C  CB   . MET   A 70  ? 0.33974 0.40644 0.27561 0.00826  0.02954  -0.08103 222 MET   A CB   
357  C  CG   . MET   A 70  ? 0.35782 0.41308 0.29006 0.01153  0.02586  -0.09754 222 MET   A CG   
358  S  SD   . MET   A 70  ? 0.37962 0.40758 0.32398 0.01744  0.02068  -0.10348 222 MET   A SD   
359  C  CE   . MET   A 70  ? 0.35937 0.36661 0.30355 0.00900  0.01445  -0.09077 222 MET   A CE   
360  N  N    . LEU   A 71  ? 0.27986 0.37652 0.23437 0.00878  0.03930  -0.05522 223 LEU   A N    
361  C  CA   . LEU   A 71  ? 0.24504 0.34060 0.20764 0.00483  0.03839  -0.04018 223 LEU   A CA   
362  C  C    . LEU   A 71  ? 0.25321 0.33457 0.22723 0.00868  0.03687  -0.03921 223 LEU   A C    
363  O  O    . LEU   A 71  ? 0.25295 0.32240 0.23141 0.00554  0.03327  -0.03132 223 LEU   A O    
364  C  CB   . LEU   A 71  ? 0.22008 0.34107 0.18420 0.00185  0.04284  -0.03073 223 LEU   A CB   
365  C  CG   . LEU   A 71  ? 0.21158 0.33151 0.18607 -0.00257 0.04080  -0.01518 223 LEU   A CG   
366  C  CD1  . LEU   A 71  ? 0.20017 0.30723 0.17280 -0.00754 0.03530  -0.00925 223 LEU   A CD1  
367  C  CD2  . LEU   A 71  ? 0.22284 0.36821 0.20035 -0.00631 0.04445  -0.00462 223 LEU   A CD2  
368  N  N    . PRO   A 72  ? 0.24753 0.33062 0.22722 0.01539  0.03910  -0.04691 224 PRO   A N    
369  C  CA   . PRO   A 72  ? 0.23174 0.30064 0.22202 0.01843  0.03638  -0.04491 224 PRO   A CA   
370  C  C    . PRO   A 72  ? 0.23063 0.27528 0.21867 0.01720  0.03021  -0.04634 224 PRO   A C    
371  O  O    . PRO   A 72  ? 0.22045 0.25575 0.21304 0.01465  0.02725  -0.03878 224 PRO   A O    
372  C  CB   . PRO   A 72  ? 0.23616 0.31221 0.23244 0.02654  0.03934  -0.05507 224 PRO   A CB   
373  C  CG   . PRO   A 72  ? 0.23873 0.34114 0.23044 0.02630  0.04576  -0.05728 224 PRO   A CG   
374  C  CD   . PRO   A 72  ? 0.25921 0.36133 0.23778 0.02041  0.04450  -0.05646 224 PRO   A CD   
375  N  N    . HIS   A 73  ? 0.26631 0.30166 0.24765 0.01848  0.02797  -0.05603 225 HIS   A N    
376  C  CA   . HIS   A 73  ? 0.27872 0.29232 0.25828 0.01609  0.02179  -0.05612 225 HIS   A CA   
377  C  C    . HIS   A 73  ? 0.25524 0.26694 0.23018 0.00847  0.02026  -0.04702 225 HIS   A C    
378  O  O    . HIS   A 73  ? 0.24697 0.24733 0.22441 0.00579  0.01680  -0.04168 225 HIS   A O    
379  C  CB   . HIS   A 73  ? 0.28139 0.28592 0.25592 0.01816  0.01898  -0.06814 225 HIS   A CB   
380  C  CG   . HIS   A 73  ? 0.28807 0.27134 0.26115 0.01429  0.01217  -0.06689 225 HIS   A CG   
381  N  ND1  . HIS   A 73  ? 0.28853 0.25608 0.26881 0.01617  0.00733  -0.06542 225 HIS   A ND1  
382  C  CD2  . HIS   A 73  ? 0.28260 0.25938 0.24826 0.00785  0.00915  -0.06569 225 HIS   A CD2  
383  C  CE1  . HIS   A 73  ? 0.29495 0.24774 0.27182 0.01056  0.00181  -0.06288 225 HIS   A CE1  
384  N  NE2  . HIS   A 73  ? 0.28432 0.24254 0.25272 0.00556  0.00301  -0.06338 225 HIS   A NE2  
385  N  N    . LEU   A 74  ? 0.22979 0.25385 0.19831 0.00498  0.02254  -0.04540 226 LEU   A N    
386  C  CA   . LEU   A 74  ? 0.24001 0.26222 0.20564 -0.00151 0.02034  -0.03804 226 LEU   A CA   
387  C  C    . LEU   A 74  ? 0.23194 0.25872 0.20579 -0.00315 0.02088  -0.02770 226 LEU   A C    
388  O  O    . LEU   A 74  ? 0.22735 0.24834 0.20275 -0.00685 0.01814  -0.02302 226 LEU   A O    
389  C  CB   . LEU   A 74  ? 0.25122 0.28501 0.20818 -0.00474 0.02136  -0.03914 226 LEU   A CB   
390  C  CG   . LEU   A 74  ? 0.28479 0.31156 0.23367 -0.00422 0.01924  -0.05042 226 LEU   A CG   
391  C  CD1  . LEU   A 74  ? 0.27645 0.31688 0.21568 -0.00761 0.01997  -0.05220 226 LEU   A CD1  
392  C  CD2  . LEU   A 74  ? 0.26988 0.27727 0.21911 -0.00722 0.01387  -0.05071 226 LEU   A CD2  
393  N  N    . ALA   A 75  ? 0.21765 0.25518 0.19795 -0.00039 0.02409  -0.02476 227 ALA   A N    
394  C  CA   . ALA   A 75  ? 0.18833 0.22747 0.17860 -0.00156 0.02342  -0.01617 227 ALA   A CA   
395  C  C    . ALA   A 75  ? 0.21212 0.23663 0.20639 -0.00044 0.02022  -0.01721 227 ALA   A C    
396  O  O    . ALA   A 75  ? 0.20872 0.22954 0.20685 -0.00321 0.01776  -0.01284 227 ALA   A O    
397  C  CB   . ALA   A 75  ? 0.18143 0.23503 0.17871 0.00073  0.02711  -0.01290 227 ALA   A CB   
398  N  N    . ASP   A 76  ? 0.21259 0.22958 0.20649 0.00371  0.01981  -0.02323 228 ASP   A N    
399  C  CA   . ASP   A 76  ? 0.22299 0.22682 0.21939 0.00398  0.01598  -0.02306 228 ASP   A CA   
400  C  C    . ASP   A 76  ? 0.23460 0.22902 0.22446 -0.00097 0.01272  -0.02272 228 ASP   A C    
401  O  O    . ASP   A 76  ? 0.21983 0.21051 0.21169 -0.00351 0.01040  -0.01927 228 ASP   A O    
402  C  CB   . ASP   A 76  ? 0.23183 0.22893 0.23003 0.00936  0.01498  -0.02896 228 ASP   A CB   
403  C  CG   . ASP   A 76  ? 0.25393 0.26100 0.26148 0.01437  0.01771  -0.02860 228 ASP   A CG   
404  O  OD1  . ASP   A 76  ? 0.26870 0.27375 0.27941 0.01995  0.01758  -0.03466 228 ASP   A OD1  
405  O  OD2  . ASP   A 76  ? 0.22910 0.24620 0.24219 0.01276  0.01955  -0.02250 228 ASP   A OD2  
406  N  N    . LEU   A 77  ? 0.22804 0.22024 0.21024 -0.00264 0.01250  -0.02674 229 LEU   A N    
407  C  CA   . LEU   A 77  ? 0.22714 0.21234 0.20400 -0.00804 0.00948  -0.02598 229 LEU   A CA   
408  C  C    . LEU   A 77  ? 0.23269 0.22547 0.21203 -0.01172 0.00997  -0.02053 229 LEU   A C    
409  O  O    . LEU   A 77  ? 0.25826 0.24793 0.23841 -0.01479 0.00795  -0.01843 229 LEU   A O    
410  C  CB   . LEU   A 77  ? 0.22332 0.20633 0.19260 -0.00933 0.00886  -0.03161 229 LEU   A CB   
411  C  CG   . LEU   A 77  ? 0.26087 0.24036 0.22489 -0.01572 0.00615  -0.03064 229 LEU   A CG   
412  C  CD1  . LEU   A 77  ? 0.26649 0.23440 0.23094 -0.01897 0.00217  -0.02852 229 LEU   A CD1  
413  C  CD2  . LEU   A 77  ? 0.27350 0.25219 0.23073 -0.01643 0.00534  -0.03723 229 LEU   A CD2  
414  N  N    . VAL   A 78  ? 0.21452 0.21838 0.19602 -0.01141 0.01233  -0.01815 230 VAL   A N    
415  C  CA   . VAL   A 78  ? 0.19522 0.20546 0.18213 -0.01404 0.01166  -0.01316 230 VAL   A CA   
416  C  C    . VAL   A 78  ? 0.20414 0.21317 0.19963 -0.01287 0.01071  -0.01106 230 VAL   A C    
417  O  O    . VAL   A 78  ? 0.19887 0.20780 0.19727 -0.01501 0.00895  -0.01070 230 VAL   A O    
418  C  CB   . VAL   A 78  ? 0.19472 0.21670 0.18393 -0.01409 0.01324  -0.00908 230 VAL   A CB   
419  C  CG1  . VAL   A 78  ? 0.17039 0.19718 0.16992 -0.01562 0.01125  -0.00327 230 VAL   A CG1  
420  C  CG2  . VAL   A 78  ? 0.19511 0.22029 0.17491 -0.01641 0.01332  -0.01131 230 VAL   A CG2  
421  N  N    . SER   A 79  ? 0.20564 0.21540 0.20578 -0.00936 0.01184  -0.01041 231 SER   A N    
422  C  CA   . SER   A 79  ? 0.19351 0.20270 0.20197 -0.00831 0.01039  -0.00895 231 SER   A CA   
423  C  C    . SER   A 79  ? 0.19485 0.19676 0.19938 -0.00985 0.00809  -0.01138 231 SER   A C    
424  O  O    . SER   A 79  ? 0.19211 0.19608 0.20094 -0.01111 0.00648  -0.01145 231 SER   A O    
425  C  CB   . SER   A 79  ? 0.19821 0.20974 0.21185 -0.00450 0.01179  -0.00805 231 SER   A CB   
426  O  OG   . SER   A 79  ? 0.21659 0.22972 0.23998 -0.00398 0.00999  -0.00601 231 SER   A OG   
427  N  N    . TYR   A 80  ? 0.18936 0.18352 0.18628 -0.00995 0.00750  -0.01344 232 TYR   A N    
428  C  CA   . TYR   A 80  ? 0.19773 0.18580 0.18997 -0.01304 0.00474  -0.01360 232 TYR   A CA   
429  C  C    . TYR   A 80  ? 0.21033 0.20294 0.20045 -0.01776 0.00450  -0.01362 232 TYR   A C    
430  O  O    . TYR   A 80  ? 0.18650 0.18225 0.17714 -0.02010 0.00328  -0.01346 232 TYR   A O    
431  C  CB   . TYR   A 80  ? 0.22414 0.20201 0.21020 -0.01299 0.00311  -0.01508 232 TYR   A CB   
432  C  CG   . TYR   A 80  ? 0.27565 0.24657 0.25681 -0.01757 -0.00067 -0.01308 232 TYR   A CG   
433  C  CD1  . TYR   A 80  ? 0.29506 0.26202 0.27771 -0.01708 -0.00371 -0.01040 232 TYR   A CD1  
434  C  CD2  . TYR   A 80  ? 0.30263 0.27187 0.27793 -0.02307 -0.00170 -0.01286 232 TYR   A CD2  
435  C  CE1  . TYR   A 80  ? 0.31864 0.28064 0.29657 -0.02236 -0.00773 -0.00657 232 TYR   A CE1  
436  C  CE2  . TYR   A 80  ? 0.33465 0.29902 0.30589 -0.02857 -0.00541 -0.00931 232 TYR   A CE2  
437  C  CZ   . TYR   A 80  ? 0.34888 0.30976 0.32119 -0.02836 -0.00847 -0.00571 232 TYR   A CZ   
438  O  OH   . TYR   A 80  ? 0.38337 0.34080 0.35147 -0.03480 -0.01271 -0.00023 232 TYR   A OH   
439  N  N    . SER   A 81  ? 0.18489 0.17989 0.17291 -0.01912 0.00565  -0.01423 233 SER   A N    
440  C  CA   . SER   A 81  ? 0.22317 0.22351 0.21048 -0.02327 0.00528  -0.01451 233 SER   A CA   
441  C  C    . SER   A 81  ? 0.20096 0.21027 0.19784 -0.02206 0.00544  -0.01486 233 SER   A C    
442  O  O    . SER   A 81  ? 0.17209 0.18714 0.17026 -0.02456 0.00495  -0.01665 233 SER   A O    
443  C  CB   . SER   A 81  ? 0.27489 0.27606 0.25845 -0.02476 0.00572  -0.01490 233 SER   A CB   
444  O  OG   . SER   A 81  ? 0.35250 0.35682 0.33379 -0.02961 0.00471  -0.01527 233 SER   A OG   
445  N  N    . ILE   A 82  ? 0.18567 0.19713 0.19040 -0.01839 0.00584  -0.01348 234 ILE   A N    
446  C  CA   . ILE   A 82  ? 0.15933 0.17704 0.17571 -0.01696 0.00456  -0.01429 234 ILE   A CA   
447  C  C    . ILE   A 82  ? 0.15855 0.17743 0.17573 -0.01710 0.00363  -0.01782 234 ILE   A C    
448  O  O    . ILE   A 82  ? 0.16521 0.19090 0.18786 -0.01752 0.00272  -0.02178 234 ILE   A O    
449  C  CB   . ILE   A 82  ? 0.17160 0.19037 0.19705 -0.01402 0.00426  -0.01061 234 ILE   A CB   
450  C  CG1  . ILE   A 82  ? 0.16023 0.18223 0.18556 -0.01486 0.00468  -0.00634 234 ILE   A CG1  
451  C  CG2  . ILE   A 82  ? 0.16604 0.18836 0.20550 -0.01242 0.00152  -0.01203 234 ILE   A CG2  
452  C  CD1  . ILE   A 82  ? 0.16437 0.18940 0.19642 -0.01328 0.00494  -0.00074 234 ILE   A CD1  
453  N  N    . GLN   A 83  ? 0.16200 0.17560 0.17415 -0.01658 0.00357  -0.01690 235 GLN   A N    
454  C  CA   . GLN   A 83  ? 0.18302 0.19908 0.19412 -0.01749 0.00217  -0.01928 235 GLN   A CA   
455  C  C    . GLN   A 83  ? 0.19525 0.21654 0.19925 -0.02217 0.00242  -0.02102 235 GLN   A C    
456  O  O    . GLN   A 83  ? 0.18351 0.21382 0.18942 -0.02317 0.00194  -0.02507 235 GLN   A O    
457  C  CB   . GLN   A 83  ? 0.22950 0.23851 0.23619 -0.01648 0.00120  -0.01650 235 GLN   A CB   
458  C  CG   . GLN   A 83  ? 0.24624 0.25342 0.26114 -0.01208 0.00122  -0.01506 235 GLN   A CG   
459  C  CD   . GLN   A 83  ? 0.29837 0.30069 0.31143 -0.01049 -0.00035 -0.01323 235 GLN   A CD   
460  O  OE1  . GLN   A 83  ? 0.30332 0.30702 0.31426 -0.01192 -0.00281 -0.01367 235 GLN   A OE1  
461  N  NE2  . GLN   A 83  ? 0.30590 0.30404 0.32008 -0.00742 0.00086  -0.01139 235 GLN   A NE2  
462  N  N    . LYS   A 84  ? 0.20187 0.21906 0.19805 -0.02539 0.00309  -0.01843 236 LYS   A N    
463  C  CA   . LYS   A 84  ? 0.18793 0.21133 0.17810 -0.03098 0.00325  -0.01873 236 LYS   A CA   
464  C  C    . LYS   A 84  ? 0.19655 0.23200 0.19389 -0.03086 0.00450  -0.02345 236 LYS   A C    
465  O  O    . LYS   A 84  ? 0.22743 0.27456 0.22419 -0.03372 0.00510  -0.02658 236 LYS   A O    
466  C  CB   . LYS   A 84  ? 0.20320 0.21822 0.18530 -0.03473 0.00270  -0.01491 236 LYS   A CB   
467  C  CG   . LYS   A 84  ? 0.24023 0.24263 0.21721 -0.03440 0.00047  -0.01122 236 LYS   A CG   
468  C  CD   . LYS   A 84  ? 0.27788 0.28305 0.25266 -0.03624 -0.00145 -0.00908 236 LYS   A CD   
469  C  CE   . LYS   A 84  ? 0.32010 0.31230 0.29060 -0.03701 -0.00514 -0.00411 236 LYS   A CE   
470  N  NZ   . LYS   A 84  ? 0.35235 0.33811 0.31731 -0.04273 -0.00710 -0.00094 236 LYS   A NZ   
471  N  N    . VAL   A 85  ? 0.16161 0.19579 0.16631 -0.02762 0.00464  -0.02389 237 VAL   A N    
472  C  CA   . VAL   A 85  ? 0.17490 0.21933 0.18935 -0.02656 0.00462  -0.02809 237 VAL   A CA   
473  C  C    . VAL   A 85  ? 0.17591 0.22854 0.19991 -0.02343 0.00385  -0.03462 237 VAL   A C    
474  O  O    . VAL   A 85  ? 0.18922 0.25422 0.21819 -0.02376 0.00429  -0.04073 237 VAL   A O    
475  C  CB   . VAL   A 85  ? 0.15830 0.19891 0.17932 -0.02392 0.00364  -0.02525 237 VAL   A CB   
476  C  CG1  . VAL   A 85  ? 0.14314 0.19309 0.17802 -0.02169 0.00205  -0.02919 237 VAL   A CG1  
477  C  CG2  . VAL   A 85  ? 0.15226 0.18794 0.16328 -0.02740 0.00427  -0.02115 237 VAL   A CG2  
478  N  N    . ILE   A 86  ? 0.15486 0.20182 0.18239 -0.02022 0.00252  -0.03436 238 ILE   A N    
479  C  CA   . ILE   A 86  ? 0.17461 0.22838 0.21141 -0.01731 0.00093  -0.04155 238 ILE   A CA   
480  C  C    . ILE   A 86  ? 0.18376 0.24809 0.21185 -0.02073 0.00226  -0.04580 238 ILE   A C    
481  O  O    . ILE   A 86  ? 0.22518 0.30251 0.25947 -0.01962 0.00222  -0.05463 238 ILE   A O    
482  C  CB   . ILE   A 86  ? 0.21116 0.25645 0.25288 -0.01422 -0.00115 -0.03924 238 ILE   A CB   
483  C  CG1  . ILE   A 86  ? 0.21807 0.25678 0.26969 -0.01171 -0.00254 -0.03435 238 ILE   A CG1  
484  C  CG2  . ILE   A 86  ? 0.19245 0.24428 0.24237 -0.01191 -0.00350 -0.04744 238 ILE   A CG2  
485  C  CD1  . ILE   A 86  ? 0.22755 0.25834 0.27966 -0.01042 -0.00307 -0.02868 238 ILE   A CD1  
486  N  N    . GLY   A 87  ? 0.19070 0.25062 0.20498 -0.02501 0.00304  -0.03963 239 GLY   A N    
487  C  CA   . GLY   A 87  ? 0.21602 0.28718 0.22093 -0.02984 0.00380  -0.04092 239 GLY   A CA   
488  C  C    . GLY   A 87  ? 0.21418 0.29992 0.21831 -0.03340 0.00626  -0.04434 239 GLY   A C    
489  O  O    . GLY   A 87  ? 0.21819 0.32104 0.22124 -0.03526 0.00745  -0.05046 239 GLY   A O    
490  N  N    . PHE   A 88  ? 0.16432 0.24548 0.16932 -0.03444 0.00710  -0.04096 240 PHE   A N    
491  C  CA   . PHE   A 88  ? 0.16823 0.26408 0.17460 -0.03766 0.00924  -0.04408 240 PHE   A CA   
492  C  C    . PHE   A 88  ? 0.17965 0.28869 0.20092 -0.03205 0.00948  -0.05539 240 PHE   A C    
493  O  O    . PHE   A 88  ? 0.19659 0.32509 0.21900 -0.03361 0.01157  -0.06251 240 PHE   A O    
494  C  CB   . PHE   A 88  ? 0.17474 0.26193 0.17978 -0.03968 0.00912  -0.03819 240 PHE   A CB   
495  C  CG   . PHE   A 88  ? 0.19778 0.30015 0.20609 -0.04290 0.01087  -0.04093 240 PHE   A CG   
496  C  CD1  . PHE   A 88  ? 0.19475 0.30710 0.19375 -0.05108 0.01243  -0.03744 240 PHE   A CD1  
497  C  CD2  . PHE   A 88  ? 0.19665 0.30380 0.21849 -0.03815 0.01038  -0.04601 240 PHE   A CD2  
498  C  CE1  . PHE   A 88  ? 0.19506 0.32353 0.19807 -0.05448 0.01426  -0.03975 240 PHE   A CE1  
499  C  CE2  . PHE   A 88  ? 0.20278 0.32495 0.22913 -0.04071 0.01174  -0.04869 240 PHE   A CE2  
500  C  CZ   . PHE   A 88  ? 0.20333 0.33690 0.22022 -0.04887 0.01407  -0.04593 240 PHE   A CZ   
501  N  N    . ALA   A 89  ? 0.18681 0.28631 0.22058 -0.02558 0.00700  -0.05721 241 ALA   A N    
502  C  CA   . ALA   A 89  ? 0.20043 0.30913 0.25186 -0.01961 0.00552  -0.06757 241 ALA   A CA   
503  C  C    . ALA   A 89  ? 0.21412 0.33664 0.26832 -0.01777 0.00583  -0.07870 241 ALA   A C    
504  O  O    . ALA   A 89  ? 0.21370 0.35253 0.27833 -0.01498 0.00638  -0.08988 241 ALA   A O    
505  C  CB   . ALA   A 89  ? 0.19888 0.29292 0.26295 -0.01414 0.00148  -0.06507 241 ALA   A CB   
506  N  N    . LYS   A 90  ? 0.21786 0.33528 0.26323 -0.01908 0.00524  -0.07655 242 LYS   A N    
507  C  CA   . LYS   A 90  ? 0.22450 0.35526 0.27104 -0.01768 0.00492  -0.08718 242 LYS   A CA   
508  C  C    . LYS   A 90  ? 0.22982 0.38467 0.26855 -0.02225 0.00899  -0.09281 242 LYS   A C    
509  O  O    . LYS   A 90  ? 0.26057 0.43300 0.30453 -0.01973 0.00935  -0.10603 242 LYS   A O    
510  C  CB   . LYS   A 90  ? 0.25428 0.37552 0.29067 -0.01952 0.00326  -0.08136 242 LYS   A CB   
511  C  CG   . LYS   A 90  ? 0.29390 0.39990 0.34208 -0.01400 -0.00100 -0.08155 242 LYS   A CG   
512  C  CD   . LYS   A 90  ? 0.32666 0.42167 0.36418 -0.01636 -0.00221 -0.07263 242 LYS   A CD   
513  C  CE   . LYS   A 90  ? 0.33642 0.44286 0.36883 -0.01748 -0.00354 -0.07911 242 LYS   A CE   
514  N  NZ   . LYS   A 90  ? 0.36021 0.45548 0.38520 -0.01894 -0.00585 -0.07029 242 LYS   A NZ   
515  N  N    A MET   A 91  ? 0.23729 0.39460 0.26394 -0.02927 0.01190  -0.08338 243 MET   A N    
516  N  N    B MET   A 91  ? 0.23811 0.39536 0.26479 -0.02927 0.01191  -0.08334 243 MET   A N    
517  C  CA   A MET   A 91  ? 0.24943 0.43137 0.26821 -0.03534 0.01595  -0.08620 243 MET   A CA   
518  C  CA   B MET   A 91  ? 0.24999 0.43169 0.26866 -0.03543 0.01595  -0.08595 243 MET   A CA   
519  C  C    A MET   A 91  ? 0.24561 0.44239 0.27570 -0.03371 0.01841  -0.09318 243 MET   A C    
520  C  C    B MET   A 91  ? 0.24533 0.44270 0.27598 -0.03336 0.01838  -0.09395 243 MET   A C    
521  O  O    A MET   A 91  ? 0.25206 0.46883 0.27818 -0.03892 0.02068  -0.09371 243 MET   A O    
522  O  O    B MET   A 91  ? 0.25213 0.47021 0.27997 -0.03789 0.02039  -0.09565 243 MET   A O    
523  C  CB   A MET   A 91  ? 0.26665 0.44416 0.26726 -0.04520 0.01679  -0.07112 243 MET   A CB   
524  C  CB   B MET   A 91  ? 0.26672 0.44349 0.26785 -0.04523 0.01687  -0.07067 243 MET   A CB   
525  C  CG   A MET   A 91  ? 0.28940 0.45259 0.27986 -0.04672 0.01372  -0.06342 243 MET   A CG   
526  C  CG   B MET   A 91  ? 0.28737 0.44949 0.27718 -0.04758 0.01393  -0.06178 243 MET   A CG   
527  S  SD   A MET   A 91  ? 0.31386 0.47412 0.28561 -0.05847 0.01321  -0.04654 243 MET   A SD   
528  S  SD   B MET   A 91  ? 0.29740 0.46951 0.28872 -0.04337 0.01231  -0.07254 243 MET   A SD   
529  C  CE   A MET   A 91  ? 0.30227 0.42869 0.27465 -0.05547 0.00954  -0.03650 243 MET   A CE   
530  C  CE   B MET   A 91  ? 0.30983 0.51012 0.29446 -0.05072 0.01543  -0.07108 243 MET   A CE   
531  N  N    . ILE   A 92  ? 0.23304 0.41843 0.27872 -0.02702 0.01596  -0.09562 244 ILE   A N    
532  C  CA   . ILE   A 92  ? 0.20774 0.40737 0.26703 -0.02438 0.01724  -0.10279 244 ILE   A CA   
533  C  C    . ILE   A 92  ? 0.24080 0.45544 0.30788 -0.01944 0.01555  -0.11791 244 ILE   A C    
534  O  O    . ILE   A 92  ? 0.23157 0.44061 0.30952 -0.01281 0.01184  -0.12645 244 ILE   A O    
535  C  CB   . ILE   A 92  ? 0.18560 0.36707 0.25953 -0.01854 0.01298  -0.09990 244 ILE   A CB   
536  C  CG1  . ILE   A 92  ? 0.16297 0.32390 0.22484 -0.02367 0.01219  -0.08378 244 ILE   A CG1  
537  C  CG2  . ILE   A 92  ? 0.16528 0.35676 0.25105 -0.01496 0.01267  -0.10624 244 ILE   A CG2  
538  C  CD1  . ILE   A 92  ? 0.15786 0.30267 0.23203 -0.01868 0.00788  -0.07983 244 ILE   A CD1  
539  N  N    . PRO   A 93  ? 0.26459 0.49845 0.32831 -0.02292 0.01707  -0.12126 245 PRO   A N    
540  C  CA   . PRO   A 93  ? 0.27628 0.52726 0.34957 -0.01880 0.01483  -0.13591 245 PRO   A CA   
541  C  C    . PRO   A 93  ? 0.29724 0.53714 0.39095 -0.00826 0.01004  -0.14700 245 PRO   A C    
542  O  O    . PRO   A 93  ? 0.29389 0.52384 0.39595 -0.00473 0.00943  -0.14486 245 PRO   A O    
543  C  CB   . PRO   A 93  ? 0.29417 0.56559 0.36206 -0.02404 0.01767  -0.13577 245 PRO   A CB   
544  C  CG   . PRO   A 93  ? 0.28799 0.55598 0.33842 -0.03405 0.02097  -0.11917 245 PRO   A CG   
545  C  CD   . PRO   A 93  ? 0.26899 0.51111 0.32040 -0.03163 0.02049  -0.11130 245 PRO   A CD   
546  N  N    . GLY   A 94  ? 0.29915 0.54037 0.40255 -0.00366 0.00589  -0.15719 246 GLY   A N    
547  C  CA   . GLY   A 94  ? 0.29881 0.52800 0.42272 0.00531  -0.00042 -0.16720 246 GLY   A CA   
548  C  C    . GLY   A 94  ? 0.30243 0.50531 0.43271 0.00893  -0.00401 -0.16112 246 GLY   A C    
549  O  O    . GLY   A 94  ? 0.32466 0.51732 0.47231 0.01503  -0.01067 -0.16844 246 GLY   A O    
550  N  N    . PHE   A 95  ? 0.28918 0.48137 0.40704 0.00490  -0.00027 -0.14749 247 PHE   A N    
551  C  CA   . PHE   A 95  ? 0.29895 0.46769 0.42415 0.00820  -0.00351 -0.14005 247 PHE   A CA   
552  C  C    . PHE   A 95  ? 0.34921 0.51259 0.48203 0.01127  -0.00857 -0.14701 247 PHE   A C    
553  O  O    . PHE   A 95  ? 0.34842 0.49443 0.49674 0.01619  -0.01481 -0.14736 247 PHE   A O    
554  C  CB   . PHE   A 95  ? 0.27078 0.43453 0.38212 0.00196  0.00087  -0.12469 247 PHE   A CB   
555  C  CG   . PHE   A 95  ? 0.25974 0.39926 0.37590 0.00327  -0.00372 -0.11362 247 PHE   A CG   
556  C  CD1  . PHE   A 95  ? 0.26568 0.39461 0.39284 0.00519  -0.00692 -0.10644 247 PHE   A CD1  
557  C  CD2  . PHE   A 95  ? 0.25242 0.38039 0.36103 0.00214  -0.00505 -0.10960 247 PHE   A CD2  
558  C  CE1  . PHE   A 95  ? 0.26094 0.36968 0.39052 0.00547  -0.01082 -0.09526 247 PHE   A CE1  
559  C  CE2  . PHE   A 95  ? 0.24990 0.35739 0.36209 0.00285  -0.00875 -0.09896 247 PHE   A CE2  
560  C  CZ   . PHE   A 95  ? 0.25236 0.35088 0.37455 0.00428  -0.01138 -0.09168 247 PHE   A CZ   
561  N  N    . ARG   A 96  ? 0.37331 0.55231 0.49717 0.00801  -0.00617 -0.14961 248 ARG   A N    
562  C  CA   . ARG   A 96  ? 0.41949 0.59450 0.55102 0.01153  -0.00976 -0.15307 248 ARG   A CA   
563  C  C    . ARG   A 96  ? 0.43528 0.61913 0.58439 0.01673  -0.01521 -0.16687 248 ARG   A C    
564  O  O    . ARG   A 96  ? 0.44826 0.63114 0.60498 0.01984  -0.01846 -0.17124 248 ARG   A O    
565  C  CB   . ARG   A 96  ? 0.46806 0.64948 0.57840 0.00643  -0.00457 -0.14759 248 ARG   A CB   
566  C  CG   . ARG   A 96  ? 0.50767 0.67901 0.59693 -0.00039 -0.00035 -0.13359 248 ARG   A CG   
567  C  CD   . ARG   A 96  ? 0.55796 0.71704 0.63351 -0.00354 -0.00139 -0.12552 248 ARG   A CD   
568  N  NE   . ARG   A 96  ? 0.60716 0.75251 0.69660 0.00207  -0.00710 -0.12893 248 ARG   A NE   
569  C  CZ   . ARG   A 96  ? 0.61939 0.74416 0.71682 0.00353  -0.01126 -0.12296 248 ARG   A CZ   
570  N  NH1  . ARG   A 96  ? 0.61645 0.73192 0.70929 0.00058  -0.00977 -0.11197 248 ARG   A NH1  
571  N  NH2  . ARG   A 96  ? 0.62976 0.74378 0.74052 0.00774  -0.01653 -0.12484 248 ARG   A NH2  
572  N  N    . ASP   A 97  ? 0.44217 0.63411 0.59805 0.01796  -0.01648 -0.17446 249 ASP   A N    
573  C  CA   . ASP   A 97  ? 0.45651 0.65127 0.63232 0.02379  -0.02311 -0.18764 249 ASP   A CA   
574  C  C    . ASP   A 97  ? 0.43547 0.60403 0.62865 0.02817  -0.03084 -0.18489 249 ASP   A C    
575  O  O    . ASP   A 97  ? 0.44049 0.60755 0.65233 0.03279  -0.03776 -0.19412 249 ASP   A O    
576  C  CB   . ASP   A 97  ? 0.48273 0.69670 0.66096 0.02375  -0.02203 -0.19781 249 ASP   A CB   
577  C  CG   . ASP   A 97  ? 0.49936 0.74211 0.66227 0.01843  -0.01528 -0.20019 249 ASP   A CG   
578  O  OD1  . ASP   A 97  ? 0.51073 0.76922 0.66981 0.01616  -0.01254 -0.20387 249 ASP   A OD1  
579  O  OD2  . ASP   A 97  ? 0.50303 0.75304 0.65795 0.01617  -0.01284 -0.19777 249 ASP   A OD2  
580  N  N    . LEU   A 98  ? 0.38879 0.53793 0.57713 0.02640  -0.03012 -0.17225 250 LEU   A N    
581  C  CA   . LEU   A 98  ? 0.34794 0.47259 0.55205 0.02908  -0.03737 -0.16638 250 LEU   A CA   
582  C  C    . LEU   A 98  ? 0.33726 0.45130 0.54582 0.02982  -0.04097 -0.16200 250 LEU   A C    
583  O  O    . LEU   A 98  ? 0.33302 0.45596 0.53046 0.02846  -0.03683 -0.16165 250 LEU   A O    
584  C  CB   . LEU   A 98  ? 0.31344 0.42399 0.51059 0.02725  -0.03428 -0.15220 250 LEU   A CB   
585  C  CG   . LEU   A 98  ? 0.29604 0.41564 0.49006 0.02757  -0.03018 -0.15129 250 LEU   A CG   
586  C  CD1  . LEU   A 98  ? 0.28047 0.39341 0.46469 0.02457  -0.02583 -0.13379 250 LEU   A CD1  
587  C  CD2  . LEU   A 98  ? 0.30407 0.41809 0.51946 0.03214  -0.03766 -0.15716 250 LEU   A CD2  
588  N  N    . THR   A 99  ? 0.34300 0.43859 0.56892 0.03172  -0.04894 -0.15777 251 THR   A N    
589  C  CA   . THR   A 99  ? 0.34137 0.42565 0.57237 0.03174  -0.05275 -0.15130 251 THR   A CA   
590  C  C    . THR   A 99  ? 0.33049 0.40246 0.54784 0.02805  -0.04861 -0.13664 251 THR   A C    
591  O  O    . THR   A 99  ? 0.30717 0.37409 0.51744 0.02629  -0.04513 -0.12989 251 THR   A O    
592  C  CB   . THR   A 99  ? 0.36237 0.43191 0.61637 0.03350  -0.06286 -0.14923 251 THR   A CB   
593  O  OG1  . THR   A 99  ? 0.34531 0.39838 0.60214 0.03119  -0.06456 -0.13652 251 THR   A OG1  
594  C  CG2  . THR   A 99  ? 0.40026 0.48106 0.67039 0.03764  -0.06779 -0.16502 251 THR   A CG2  
595  N  N    . SER   A 100 ? 0.32147 0.39058 0.53825 0.02826  -0.04912 -0.13230 252 SER   A N    
596  C  CA   . SER   A 100 ? 0.34368 0.40029 0.55000 0.02605  -0.04567 -0.11963 252 SER   A CA   
597  C  C    . SER   A 100 ? 0.33076 0.37007 0.54417 0.02346  -0.04924 -0.10680 252 SER   A C    
598  O  O    . SER   A 100 ? 0.32839 0.36800 0.53094 0.01995  -0.04493 -0.09555 252 SER   A O    
599  C  CB   . SER   A 100 ? 0.38539 0.43813 0.59532 0.02640  -0.04860 -0.11797 252 SER   A CB   
600  O  OG   . SER   A 100 ? 0.43783 0.50644 0.63711 0.02700  -0.04446 -0.12796 252 SER   A OG   
601  N  N    . ASP   A 101 ? 0.34662 0.37636 0.57746 0.02391  -0.05712 -0.10447 253 ASP   A N    
602  C  CA   . ASP   A 101 ? 0.36804 0.38455 0.60791 0.02138  -0.06105 -0.09010 253 ASP   A CA   
603  C  C    . ASP   A 101 ? 0.32942 0.35149 0.56360 0.02153  -0.05727 -0.08830 253 ASP   A C    
604  O  O    . ASP   A 101 ? 0.31970 0.33994 0.54742 0.01874  -0.05503 -0.07259 253 ASP   A O    
605  C  CB   . ASP   A 101 ? 0.40952 0.41864 0.67016 0.02151  -0.07062 -0.08873 253 ASP   A CB   
606  C  CG   . ASP   A 101 ? 0.46389 0.47218 0.73072 0.02131  -0.07451 -0.08913 253 ASP   A CG   
607  O  OD1  . ASP   A 101 ? 0.48419 0.50397 0.75656 0.02545  -0.07605 -0.10309 253 ASP   A OD1  
608  O  OD2  . ASP   A 101 ? 0.48409 0.48250 0.75128 0.01794  -0.07578 -0.07526 253 ASP   A OD2  
609  N  N    . ASP   A 102 ? 0.32765 0.36053 0.56248 0.02443  -0.05609 -0.10287 254 ASP   A N    
610  C  CA   . ASP   A 102 ? 0.29635 0.33738 0.52482 0.02509  -0.05179 -0.10018 254 ASP   A CA   
611  C  C    . ASP   A 102 ? 0.28047 0.33236 0.48725 0.02219  -0.04253 -0.09431 254 ASP   A C    
612  O  O    . ASP   A 102 ? 0.29093 0.34459 0.49189 0.01986  -0.04021 -0.08344 254 ASP   A O    
613  C  CB   . ASP   A 102 ? 0.30715 0.35925 0.54217 0.02857  -0.05271 -0.11765 254 ASP   A CB   
614  C  CG   . ASP   A 102 ? 0.33923 0.38255 0.59652 0.03049  -0.06191 -0.11860 254 ASP   A CG   
615  O  OD1  . ASP   A 102 ? 0.36066 0.41313 0.62734 0.03350  -0.06443 -0.13379 254 ASP   A OD1  
616  O  OD2  . ASP   A 102 ? 0.33378 0.36280 0.59972 0.02854  -0.06696 -0.10383 254 ASP   A OD2  
617  N  N    . GLN   A 103 ? 0.27059 0.33068 0.46588 0.02137  -0.03802 -0.10155 255 GLN   A N    
618  C  CA   . GLN   A 103 ? 0.26344 0.33237 0.43922 0.01661  -0.03073 -0.09499 255 GLN   A CA   
619  C  C    . GLN   A 103 ? 0.23034 0.28849 0.40246 0.01250  -0.03139 -0.07764 255 GLN   A C    
620  O  O    . GLN   A 103 ? 0.18702 0.24555 0.34304 0.00854  -0.02651 -0.06836 255 GLN   A O    
621  C  CB   . GLN   A 103 ? 0.26139 0.33917 0.42693 0.01552  -0.02766 -0.10402 255 GLN   A CB   
622  C  CG   . GLN   A 103 ? 0.28305 0.37659 0.44855 0.01856  -0.02563 -0.12147 255 GLN   A CG   
623  C  CD   . GLN   A 103 ? 0.30567 0.40989 0.46016 0.01715  -0.02289 -0.12921 255 GLN   A CD   
624  O  OE1  . GLN   A 103 ? 0.28988 0.39039 0.42705 0.01164  -0.02020 -0.11978 255 GLN   A OE1  
625  N  NE2  . GLN   A 103 ? 0.31924 0.43702 0.48143 0.02071  -0.02417 -0.14139 255 GLN   A NE2  
626  N  N    . ILE   A 104 ? 0.21241 0.25842 0.39506 0.01300  -0.03668 -0.07227 256 ILE   A N    
627  C  CA   . ILE   A 104 ? 0.20281 0.24042 0.38082 0.00882  -0.03664 -0.05579 256 ILE   A CA   
628  C  C    . ILE   A 104 ? 0.19713 0.23285 0.38033 0.00776  -0.03870 -0.04501 256 ILE   A C    
629  O  O    . ILE   A 104 ? 0.20842 0.24349 0.37594 0.00377  -0.03435 -0.03404 256 ILE   A O    
630  C  CB   . ILE   A 104 ? 0.21503 0.24296 0.40504 0.00897  -0.04205 -0.05267 256 ILE   A CB   
631  C  CG1  . ILE   A 104 ? 0.20536 0.23627 0.38538 0.00825  -0.03918 -0.05936 256 ILE   A CG1  
632  C  CG2  . ILE   A 104 ? 0.23374 0.25554 0.42526 0.00488  -0.04342 -0.03491 256 ILE   A CG2  
633  C  CD1  . ILE   A 104 ? 0.24042 0.26246 0.43267 0.00921  -0.04474 -0.05935 256 ILE   A CD1  
634  N  N    A VAL   A 105 ? 0.20365 0.23509 0.40328 0.01118  -0.04465 -0.04745 257 VAL   A N    
635  N  N    B VAL   A 105 ? 0.20349 0.23513 0.40293 0.01117  -0.04456 -0.04745 257 VAL   A N    
636  C  CA   A VAL   A 105 ? 0.20356 0.23334 0.40832 0.01005  -0.04762 -0.03672 257 VAL   A CA   
637  C  CA   B VAL   A 105 ? 0.20290 0.23278 0.40678 0.00967  -0.04738 -0.03573 257 VAL   A CA   
638  C  C    A VAL   A 105 ? 0.19127 0.23289 0.38320 0.00853  -0.04203 -0.03725 257 VAL   A C    
639  C  C    B VAL   A 105 ? 0.19139 0.23300 0.38365 0.00859  -0.04217 -0.03717 257 VAL   A C    
640  O  O    A VAL   A 105 ? 0.19032 0.23256 0.37502 0.00474  -0.04123 -0.02521 257 VAL   A O    
641  O  O    B VAL   A 105 ? 0.19267 0.23539 0.37978 0.00518  -0.04201 -0.02557 257 VAL   A O    
642  C  CB   A VAL   A 105 ? 0.21814 0.24052 0.44230 0.01391  -0.05511 -0.04165 257 VAL   A CB   
643  C  CB   B VAL   A 105 ? 0.21761 0.23846 0.44160 0.01280  -0.05560 -0.03744 257 VAL   A CB   
644  C  CG1  A VAL   A 105 ? 0.21745 0.24250 0.44487 0.01370  -0.05713 -0.03491 257 VAL   A CG1  
645  C  CG1  B VAL   A 105 ? 0.22763 0.23586 0.46443 0.01192  -0.06171 -0.03442 257 VAL   A CG1  
646  C  CG2  A VAL   A 105 ? 0.23080 0.23934 0.46960 0.01242  -0.06248 -0.03474 257 VAL   A CG2  
647  C  CG2  B VAL   A 105 ? 0.21777 0.24422 0.44658 0.01784  -0.05521 -0.05517 257 VAL   A CG2  
648  N  N    . LEU   A 106 ? 0.17573 0.22679 0.36184 0.01060  -0.03761 -0.05085 258 LEU   A N    
649  C  CA   . LEU   A 106 ? 0.18769 0.24900 0.36061 0.00830  -0.03222 -0.05138 258 LEU   A CA   
650  C  C    . LEU   A 106 ? 0.19673 0.25503 0.34365 0.00242  -0.02542 -0.04257 258 LEU   A C    
651  O  O    . LEU   A 106 ? 0.18846 0.24821 0.32482 -0.00094 -0.02327 -0.03546 258 LEU   A O    
652  C  CB   . LEU   A 106 ? 0.17900 0.25304 0.35174 0.01109  -0.02887 -0.06734 258 LEU   A CB   
653  C  CG   . LEU   A 106 ? 0.19453 0.26810 0.38363 0.01704  -0.03341 -0.07652 258 LEU   A CG   
654  C  CD1  . LEU   A 106 ? 0.18421 0.27219 0.36894 0.01902  -0.02880 -0.09261 258 LEU   A CD1  
655  C  CD2  . LEU   A 106 ? 0.20415 0.27696 0.40097 0.01729  -0.03693 -0.06875 258 LEU   A CD2  
656  N  N    . LEU   A 107 ? 0.21478 0.26885 0.35220 0.00136  -0.02264 -0.04347 259 LEU   A N    
657  C  CA   . LEU   A 107 ? 0.23409 0.28466 0.34932 -0.00321 -0.01698 -0.03626 259 LEU   A CA   
658  C  C    . LEU   A 107 ? 0.22051 0.26398 0.33443 -0.00528 -0.01834 -0.02312 259 LEU   A C    
659  O  O    . LEU   A 107 ? 0.21474 0.25756 0.31297 -0.00862 -0.01459 -0.01719 259 LEU   A O    
660  C  CB   . LEU   A 107 ? 0.26508 0.31420 0.37209 -0.00337 -0.01436 -0.04093 259 LEU   A CB   
661  C  CG   . LEU   A 107 ? 0.30355 0.36241 0.40062 -0.00442 -0.01042 -0.05021 259 LEU   A CG   
662  C  CD1  . LEU   A 107 ? 0.32465 0.38452 0.41929 -0.00367 -0.01013 -0.05642 259 LEU   A CD1  
663  C  CD2  . LEU   A 107 ? 0.30682 0.36539 0.38444 -0.00936 -0.00567 -0.04427 259 LEU   A CD2  
664  N  N    . LYS   A 108 ? 0.22405 0.26311 0.35461 -0.00371 -0.02394 -0.01856 260 LYS   A N    
665  C  CA   . LYS   A 108 ? 0.24196 0.27781 0.37153 -0.00658 -0.02514 -0.00494 260 LYS   A CA   
666  C  C    . LYS   A 108 ? 0.23953 0.27944 0.36641 -0.00861 -0.02607 0.00159  260 LYS   A C    
667  O  O    . LYS   A 108 ? 0.24524 0.28631 0.35952 -0.01207 -0.02348 0.01019  260 LYS   A O    
668  C  CB   . LYS   A 108 ? 0.26581 0.29715 0.41635 -0.00557 -0.03217 -0.00003 260 LYS   A CB   
669  C  CG   . LYS   A 108 ? 0.32540 0.35300 0.47420 -0.00629 -0.03073 0.00137  260 LYS   A CG   
670  C  CD   . LYS   A 108 ? 0.37985 0.40287 0.55216 -0.00598 -0.03891 0.00606  260 LYS   A CD   
671  C  CE   . LYS   A 108 ? 0.41705 0.44138 0.59280 -0.01049 -0.04136 0.02312  260 LYS   A CE   
672  N  NZ   . LYS   A 108 ? 0.42543 0.45413 0.58172 -0.01370 -0.03381 0.02933  260 LYS   A NZ   
673  N  N    . SER   A 109 ? 0.22837 0.27176 0.36759 -0.00628 -0.03003 -0.00303 261 SER   A N    
674  C  CA   . SER   A 109 ? 0.24762 0.29550 0.38618 -0.00823 -0.03211 0.00372  261 SER   A CA   
675  C  C    . SER   A 109 ? 0.21578 0.26879 0.33539 -0.01051 -0.02609 -0.00057 261 SER   A C    
676  O  O    . SER   A 109 ? 0.24318 0.29922 0.35441 -0.01376 -0.02605 0.00630  261 SER   A O    
677  C  CB   . SER   A 109 ? 0.29560 0.34526 0.45858 -0.00441 -0.04013 0.00146  261 SER   A CB   
678  O  OG   . SER   A 109 ? 0.34016 0.39339 0.50964 -0.00001 -0.03891 -0.01370 261 SER   A OG   
679  N  N    . SER   A 110 ? 0.19646 0.25104 0.30866 -0.00965 -0.02138 -0.01112 262 SER   A N    
680  C  CA   . SER   A 110 ? 0.18710 0.24678 0.28426 -0.01261 -0.01684 -0.01457 262 SER   A CA   
681  C  C    . SER   A 110 ? 0.17618 0.23096 0.25199 -0.01615 -0.01120 -0.01290 262 SER   A C    
682  O  O    . SER   A 110 ? 0.20600 0.26270 0.26922 -0.01968 -0.00874 -0.01289 262 SER   A O    
683  C  CB   . SER   A 110 ? 0.19809 0.26583 0.30071 -0.01059 -0.01547 -0.02636 262 SER   A CB   
684  O  OG   . SER   A 110 ? 0.19753 0.26326 0.29560 -0.00968 -0.01248 -0.03242 262 SER   A OG   
685  N  N    . ALA   A 111 ? 0.15681 0.20517 0.22972 -0.01523 -0.00978 -0.01171 263 ALA   A N    
686  C  CA   . ALA   A 111 ? 0.17414 0.21770 0.22944 -0.01747 -0.00507 -0.01174 263 ALA   A CA   
687  C  C    . ALA   A 111 ? 0.17166 0.21440 0.21404 -0.02077 -0.00362 -0.00689 263 ALA   A C    
688  O  O    . ALA   A 111 ? 0.18053 0.22138 0.21008 -0.02345 -0.00104 -0.00943 263 ALA   A O    
689  C  CB   . ALA   A 111 ? 0.18326 0.22126 0.23999 -0.01558 -0.00459 -0.00969 263 ALA   A CB   
690  N  N    . ILE   A 112 ? 0.16322 0.20782 0.20905 -0.02102 -0.00582 0.00027  264 ILE   A N    
691  C  CA   . ILE   A 112 ? 0.18159 0.22754 0.21450 -0.02408 -0.00461 0.00374  264 ILE   A CA   
692  C  C    . ILE   A 112 ? 0.18786 0.23704 0.21632 -0.02686 -0.00524 0.00044  264 ILE   A C    
693  O  O    . ILE   A 112 ? 0.20467 0.25186 0.21961 -0.02973 -0.00337 -0.00137 264 ILE   A O    
694  C  CB   . ILE   A 112 ? 0.22650 0.27758 0.26439 -0.02468 -0.00737 0.01302  264 ILE   A CB   
695  C  CG1  . ILE   A 112 ? 0.22400 0.27895 0.24687 -0.02785 -0.00584 0.01516  264 ILE   A CG1  
696  C  CG2  . ILE   A 112 ? 0.22849 0.28410 0.28309 -0.02411 -0.01330 0.01671  264 ILE   A CG2  
697  C  CD1  . ILE   A 112 ? 0.20770 0.25808 0.21708 -0.02737 -0.00093 0.01066  264 ILE   A CD1  
698  N  N    . GLU   A 113 ? 0.16541 0.21991 0.20658 -0.02593 -0.00822 -0.00110 265 GLU   A N    
699  C  CA   . GLU   A 113 ? 0.18940 0.24957 0.22865 -0.02876 -0.00896 -0.00384 265 GLU   A CA   
700  C  C    . GLU   A 113 ? 0.18763 0.24603 0.21788 -0.03106 -0.00529 -0.01028 265 GLU   A C    
701  O  O    . GLU   A 113 ? 0.19199 0.25112 0.21289 -0.03541 -0.00476 -0.01107 265 GLU   A O    
702  C  CB   . GLU   A 113 ? 0.19755 0.26558 0.25542 -0.02621 -0.01322 -0.00455 265 GLU   A CB   
703  C  CG   . GLU   A 113 ? 0.19600 0.26633 0.26424 -0.02520 -0.01877 0.00397  265 GLU   A CG   
704  C  CD   . GLU   A 113 ? 0.22267 0.29893 0.31280 -0.02151 -0.02406 0.00225  265 GLU   A CD   
705  O  OE1  . GLU   A 113 ? 0.19470 0.27731 0.28921 -0.02075 -0.02293 -0.00580 265 GLU   A OE1  
706  O  OE2  . GLU   A 113 ? 0.24123 0.31645 0.34530 -0.01939 -0.02961 0.00890  265 GLU   A OE2  
707  N  N    . VAL   A 114 ? 0.18787 0.24435 0.22095 -0.02886 -0.00335 -0.01430 266 VAL   A N    
708  C  CA   . VAL   A 114 ? 0.17570 0.23185 0.19978 -0.03206 -0.00046 -0.01840 266 VAL   A CA   
709  C  C    . VAL   A 114 ? 0.16563 0.21125 0.17449 -0.03475 0.00106  -0.01621 266 VAL   A C    
710  O  O    . VAL   A 114 ? 0.19604 0.24015 0.19632 -0.03943 0.00164  -0.01704 266 VAL   A O    
711  C  CB   . VAL   A 114 ? 0.15957 0.21837 0.18967 -0.02935 0.00077  -0.02325 266 VAL   A CB   
712  C  CG1  . VAL   A 114 ? 0.13036 0.19218 0.15106 -0.03398 0.00326  -0.02577 266 VAL   A CG1  
713  C  CG2  . VAL   A 114 ? 0.16747 0.23603 0.21517 -0.02535 -0.00148 -0.02745 266 VAL   A CG2  
714  N  N    . ILE   A 115 ? 0.14964 0.18843 0.15618 -0.03194 0.00135  -0.01351 267 ILE   A N    
715  C  CA   . ILE   A 115 ? 0.15001 0.17984 0.14406 -0.03330 0.00247  -0.01313 267 ILE   A CA   
716  C  C    . ILE   A 115 ? 0.19591 0.22637 0.18276 -0.03736 0.00112  -0.01315 267 ILE   A C    
717  O  O    . ILE   A 115 ? 0.22129 0.24525 0.19941 -0.04072 0.00086  -0.01508 267 ILE   A O    
718  C  CB   . ILE   A 115 ? 0.18333 0.21005 0.17792 -0.02924 0.00346  -0.01078 267 ILE   A CB   
719  C  CG1  . ILE   A 115 ? 0.19066 0.21510 0.19122 -0.02605 0.00433  -0.01141 267 ILE   A CG1  
720  C  CG2  . ILE   A 115 ? 0.18784 0.20792 0.17111 -0.02961 0.00453  -0.01217 267 ILE   A CG2  
721  C  CD1  . ILE   A 115 ? 0.20363 0.22846 0.20951 -0.02240 0.00484  -0.00801 267 ILE   A CD1  
722  N  N    . MET   A 116 ? 0.17190 0.21002 0.16327 -0.03747 -0.00070 -0.01073 268 MET   A N    
723  C  CA   . MET   A 116 ? 0.20779 0.24816 0.19272 -0.04167 -0.00265 -0.01100 268 MET   A CA   
724  C  C    . MET   A 116 ? 0.20512 0.24735 0.18997 -0.04648 -0.00341 -0.01334 268 MET   A C    
725  O  O    . MET   A 116 ? 0.20845 0.24594 0.18478 -0.05095 -0.00451 -0.01505 268 MET   A O    
726  C  CB   . MET   A 116 ? 0.21480 0.26466 0.20588 -0.04106 -0.00530 -0.00657 268 MET   A CB   
727  C  CG   . MET   A 116 ? 0.26229 0.31264 0.25068 -0.03843 -0.00471 -0.00268 268 MET   A CG   
728  S  SD   . MET   A 116 ? 0.28464 0.34671 0.28264 -0.03826 -0.00898 0.00604  268 MET   A SD   
729  C  CE   . MET   A 116 ? 0.26638 0.33019 0.25765 -0.03680 -0.00666 0.01044  268 MET   A CE   
730  N  N    . LEU   A 117 ? 0.20833 0.25815 0.20325 -0.04581 -0.00296 -0.01388 269 LEU   A N    
731  C  CA   . LEU   A 117 ? 0.23608 0.29160 0.23141 -0.05091 -0.00290 -0.01571 269 LEU   A CA   
732  C  C    . LEU   A 117 ? 0.25206 0.29837 0.23778 -0.05458 -0.00176 -0.01615 269 LEU   A C    
733  O  O    . LEU   A 117 ? 0.25267 0.29692 0.23273 -0.06083 -0.00331 -0.01569 269 LEU   A O    
734  C  CB   . LEU   A 117 ? 0.24969 0.31743 0.25792 -0.04849 -0.00189 -0.01801 269 LEU   A CB   
735  C  CG   . LEU   A 117 ? 0.27147 0.35145 0.29318 -0.04642 -0.00424 -0.01841 269 LEU   A CG   
736  C  CD1  . LEU   A 117 ? 0.27049 0.36061 0.30529 -0.04246 -0.00290 -0.02337 269 LEU   A CD1  
737  C  CD2  . LEU   A 117 ? 0.29031 0.37782 0.31048 -0.05245 -0.00595 -0.01788 269 LEU   A CD2  
738  N  N    . ARG   A 118 ? 0.23566 0.27619 0.22059 -0.05111 0.00010  -0.01640 270 ARG   A N    
739  C  CA   . ARG   A 118 ? 0.24184 0.27359 0.21914 -0.05431 0.00017  -0.01555 270 ARG   A CA   
740  C  C    . ARG   A 118 ? 0.22144 0.23990 0.18999 -0.05641 -0.00218 -0.01536 270 ARG   A C    
741  O  O    . ARG   A 118 ? 0.27570 0.28738 0.23943 -0.06175 -0.00422 -0.01395 270 ARG   A O    
742  C  CB   . ARG   A 118 ? 0.27542 0.30340 0.25410 -0.04935 0.00185  -0.01578 270 ARG   A CB   
743  C  CG   . ARG   A 118 ? 0.32002 0.36036 0.30589 -0.04851 0.00356  -0.01758 270 ARG   A CG   
744  C  CD   . ARG   A 118 ? 0.35157 0.38922 0.34050 -0.04308 0.00452  -0.01867 270 ARG   A CD   
745  N  NE   . ARG   A 118 ? 0.35759 0.39024 0.33957 -0.04564 0.00426  -0.01675 270 ARG   A NE   
746  C  CZ   . ARG   A 118 ? 0.35017 0.36914 0.32615 -0.04507 0.00287  -0.01418 270 ARG   A CZ   
747  N  NH1  . ARG   A 118 ? 0.34376 0.35468 0.31901 -0.04197 0.00257  -0.01449 270 ARG   A NH1  
748  N  NH2  . ARG   A 118 ? 0.36098 0.37561 0.33221 -0.04749 0.00153  -0.01143 270 ARG   A NH2  
749  N  N    . SER   A 119 ? 0.18845 0.20375 0.15544 -0.05248 -0.00234 -0.01687 271 SER   A N    
750  C  CA   . SER   A 119 ? 0.23847 0.24263 0.19762 -0.05323 -0.00441 -0.01930 271 SER   A CA   
751  C  C    . SER   A 119 ? 0.26176 0.26541 0.21770 -0.06024 -0.00788 -0.02007 271 SER   A C    
752  O  O    . SER   A 119 ? 0.26987 0.26229 0.22028 -0.06204 -0.01081 -0.02303 271 SER   A O    
753  C  CB   . SER   A 119 ? 0.24440 0.25044 0.20215 -0.04787 -0.00314 -0.02104 271 SER   A CB   
754  O  OG   . SER   A 119 ? 0.26937 0.28428 0.22699 -0.04997 -0.00453 -0.02075 271 SER   A OG   
755  N  N    . ASN   A 120 ? 0.26436 0.28010 0.22500 -0.06408 -0.00809 -0.01811 272 ASN   A N    
756  C  CA   . ASN   A 120 ? 0.26191 0.27871 0.22070 -0.07144 -0.01167 -0.01835 272 ASN   A CA   
757  C  C    . ASN   A 120 ? 0.29264 0.29982 0.24877 -0.07799 -0.01427 -0.01656 272 ASN   A C    
758  O  O    . ASN   A 120 ? 0.28787 0.28949 0.24140 -0.08399 -0.01860 -0.01746 272 ASN   A O    
759  C  CB   . ASN   A 120 ? 0.26482 0.29864 0.23140 -0.07384 -0.01115 -0.01642 272 ASN   A CB   
760  C  CG   . ASN   A 120 ? 0.29843 0.33570 0.26398 -0.08056 -0.01514 -0.01687 272 ASN   A CG   
761  O  OD1  . ASN   A 120 ? 0.31419 0.34849 0.27513 -0.07987 -0.01764 -0.01944 272 ASN   A OD1  
762  N  ND2  . ASN   A 120 ? 0.29241 0.33747 0.26205 -0.08757 -0.01584 -0.01445 272 ASN   A ND2  
763  N  N    . GLN   A 121 ? 0.29332 0.29847 0.25045 -0.07745 -0.01251 -0.01352 273 GLN   A N    
764  C  CA   . GLN   A 121 ? 0.31428 0.31089 0.26940 -0.08441 -0.01580 -0.00945 273 GLN   A CA   
765  C  C    . GLN   A 121 ? 0.34019 0.31676 0.29114 -0.08399 -0.02064 -0.01231 273 GLN   A C    
766  O  O    . GLN   A 121 ? 0.37310 0.34106 0.32369 -0.09145 -0.02599 -0.01019 273 GLN   A O    
767  C  CB   . GLN   A 121 ? 0.32450 0.32433 0.28066 -0.08322 -0.01319 -0.00548 273 GLN   A CB   
768  C  CG   . GLN   A 121 ? 0.36597 0.35937 0.32017 -0.09133 -0.01701 0.00134  273 GLN   A CG   
769  C  CD   . GLN   A 121 ? 0.38988 0.39491 0.34455 -0.09231 -0.01395 0.00584  273 GLN   A CD   
770  O  OE1  . GLN   A 121 ? 0.38174 0.40269 0.33958 -0.08854 -0.00896 0.00294  273 GLN   A OE1  
771  N  NE2  . GLN   A 121 ? 0.39957 0.39707 0.35165 -0.09761 -0.01765 0.01281  273 GLN   A NE2  
772  N  N    . SER   A 122 ? 0.31300 0.28266 0.26197 -0.07537 -0.01917 -0.01756 274 SER   A N    
773  C  CA   . SER   A 122 ? 0.33686 0.28949 0.28318 -0.07326 -0.02337 -0.02296 274 SER   A CA   
774  C  C    . SER   A 122 ? 0.34684 0.29989 0.28987 -0.07341 -0.02528 -0.03013 274 SER   A C    
775  O  O    . SER   A 122 ? 0.36958 0.30927 0.31094 -0.07261 -0.02966 -0.03652 274 SER   A O    
776  C  CB   . SER   A 122 ? 0.34532 0.29264 0.29162 -0.06379 -0.02063 -0.02603 274 SER   A CB   
777  O  OG   . SER   A 122 ? 0.34788 0.30656 0.29308 -0.05769 -0.01565 -0.02924 274 SER   A OG   
778  N  N    . PHE   A 123 ? 0.32871 0.29703 0.27136 -0.07388 -0.02261 -0.02986 275 PHE   A N    
779  C  CA   . PHE   A 123 ? 0.34218 0.31322 0.28080 -0.07461 -0.02485 -0.03594 275 PHE   A CA   
780  C  C    . PHE   A 123 ? 0.37541 0.33837 0.31422 -0.08337 -0.03160 -0.03710 275 PHE   A C    
781  O  O    . PHE   A 123 ? 0.40081 0.36574 0.34382 -0.09080 -0.03318 -0.03034 275 PHE   A O    
782  C  CB   . PHE   A 123 ? 0.31934 0.30889 0.25937 -0.07416 -0.02182 -0.03309 275 PHE   A CB   
783  C  CG   . PHE   A 123 ? 0.33631 0.33149 0.27106 -0.07415 -0.02387 -0.03834 275 PHE   A CG   
784  C  CD1  . PHE   A 123 ? 0.35040 0.34765 0.27975 -0.06755 -0.02160 -0.04297 275 PHE   A CD1  
785  C  CD2  . PHE   A 123 ? 0.33354 0.33398 0.26859 -0.08125 -0.02815 -0.03839 275 PHE   A CD2  
786  C  CE1  . PHE   A 123 ? 0.34858 0.35374 0.27156 -0.06815 -0.02352 -0.04758 275 PHE   A CE1  
787  C  CE2  . PHE   A 123 ? 0.35633 0.36330 0.28573 -0.08162 -0.03063 -0.04317 275 PHE   A CE2  
788  C  CZ   . PHE   A 123 ? 0.35611 0.36576 0.27881 -0.07517 -0.02832 -0.04776 275 PHE   A CZ   
789  N  N    . THR   A 124 ? 0.39917 0.35393 0.33385 -0.08284 -0.03578 -0.04600 276 THR   A N    
790  C  CA   . THR   A 124 ? 0.44226 0.39056 0.37975 -0.08905 -0.04238 -0.04752 276 THR   A CA   
791  C  C    . THR   A 124 ? 0.45062 0.40823 0.38407 -0.08813 -0.04360 -0.05410 276 THR   A C    
792  O  O    . THR   A 124 ? 0.42396 0.38315 0.35094 -0.08202 -0.04221 -0.06242 276 THR   A O    
793  C  CB   . THR   A 124 ? 0.48006 0.40760 0.42090 -0.08786 -0.04795 -0.05239 276 THR   A CB   
794  O  OG1  . THR   A 124 ? 0.50726 0.43053 0.45232 -0.09210 -0.05417 -0.05581 276 THR   A OG1  
795  C  CG2  . THR   A 124 ? 0.48060 0.40151 0.41650 -0.07882 -0.04667 -0.06354 276 THR   A CG2  
796  N  N    . MET   A 125 ? 0.47707 0.44239 0.41433 -0.09425 -0.04615 -0.05009 277 MET   A N    
797  C  CA   . MET   A 125 ? 0.50831 0.48254 0.44219 -0.09417 -0.04842 -0.05541 277 MET   A CA   
798  C  C    . MET   A 125 ? 0.55187 0.51361 0.48499 -0.09317 -0.05472 -0.06643 277 MET   A C    
799  O  O    . MET   A 125 ? 0.55537 0.52420 0.48406 -0.09211 -0.05693 -0.07271 277 MET   A O    
800  C  CB   . MET   A 125 ? 0.48676 0.47358 0.42628 -0.10076 -0.04932 -0.04776 277 MET   A CB   
801  C  CG   . MET   A 125 ? 0.47799 0.48056 0.41974 -0.10010 -0.04357 -0.03968 277 MET   A CG   
802  S  SD   . MET   A 125 ? 0.51334 0.53577 0.46111 -0.10420 -0.04431 -0.03418 277 MET   A SD   
803  C  CE   . MET   A 125 ? 0.51668 0.53621 0.47312 -0.11244 -0.04660 -0.02836 277 MET   A CE   
804  N  N    . ASP   A 126 ? 0.58509 0.52923 0.52314 -0.09303 -0.05795 -0.06917 278 ASP   A N    
805  C  CA   . ASP   A 126 ? 0.63816 0.57005 0.57890 -0.09127 -0.06445 -0.08170 278 ASP   A CA   
806  C  C    . ASP   A 126 ? 0.62808 0.56488 0.55924 -0.08254 -0.06301 -0.09386 278 ASP   A C    
807  O  O    . ASP   A 126 ? 0.63113 0.56905 0.56020 -0.08145 -0.06771 -0.10332 278 ASP   A O    
808  C  CB   . ASP   A 126 ? 0.69642 0.60895 0.64523 -0.09074 -0.06708 -0.08326 278 ASP   A CB   
809  C  CG   . ASP   A 126 ? 0.74572 0.65220 0.70261 -0.09893 -0.06901 -0.06969 278 ASP   A CG   
810  O  OD1  . ASP   A 126 ? 0.77685 0.67052 0.73806 -0.09814 -0.06971 -0.06593 278 ASP   A OD1  
811  O  OD2  . ASP   A 126 ? 0.76258 0.67833 0.72125 -0.10581 -0.06989 -0.06266 278 ASP   A OD2  
812  N  N    . ASP   A 127 ? 0.61043 0.55026 0.53560 -0.07656 -0.05673 -0.09303 279 ASP   A N    
813  C  CA   . ASP   A 127 ? 0.60417 0.55095 0.51895 -0.06846 -0.05394 -0.10243 279 ASP   A CA   
814  C  C    . ASP   A 127 ? 0.54967 0.51369 0.45840 -0.06601 -0.04492 -0.09515 279 ASP   A C    
815  O  O    . ASP   A 127 ? 0.55378 0.52458 0.45620 -0.05903 -0.04039 -0.10053 279 ASP   A O    
816  C  CB   . ASP   A 127 ? 0.64066 0.56992 0.55544 -0.06152 -0.05635 -0.11302 279 ASP   A CB   
817  C  CG   . ASP   A 127 ? 0.65018 0.57017 0.57276 -0.06002 -0.05358 -0.10824 279 ASP   A CG   
818  O  OD1  . ASP   A 127 ? 0.67297 0.57742 0.59232 -0.05646 -0.05289 -0.11410 279 ASP   A OD1  
819  O  OD2  . ASP   A 127 ? 0.64022 0.56503 0.56556 -0.06533 -0.04988 -0.09579 279 ASP   A OD2  
820  N  N    . MET   A 128 ? 0.48666 0.45873 0.39839 -0.07147 -0.04245 -0.08291 280 MET   A N    
821  C  CA   . MET   A 128 ? 0.44062 0.42901 0.34904 -0.06976 -0.03574 -0.07549 280 MET   A CA   
822  C  C    . MET   A 128 ? 0.40517 0.39076 0.31207 -0.06331 -0.03029 -0.07743 280 MET   A C    
823  O  O    . MET   A 128 ? 0.38741 0.38607 0.28920 -0.05846 -0.02551 -0.07817 280 MET   A O    
824  C  CB   . MET   A 128 ? 0.45603 0.46225 0.35775 -0.06881 -0.03525 -0.07635 280 MET   A CB   
825  C  CG   . MET   A 128 ? 0.47229 0.48070 0.37561 -0.07469 -0.04119 -0.07598 280 MET   A CG   
826  S  SD   . MET   A 128 ? 0.46583 0.47714 0.37931 -0.08218 -0.04178 -0.06315 280 MET   A SD   
827  C  CE   . MET   A 128 ? 0.45224 0.46713 0.36752 -0.08813 -0.04878 -0.06485 280 MET   A CE   
828  N  N    . SER   A 129 ? 0.37893 0.34816 0.29174 -0.06295 -0.03120 -0.07675 281 SER   A N    
829  C  CA   . SER   A 129 ? 0.39668 0.36183 0.31196 -0.05516 -0.02655 -0.07678 281 SER   A CA   
830  C  C    . SER   A 129 ? 0.39081 0.34922 0.31385 -0.05711 -0.02566 -0.06585 281 SER   A C    
831  O  O    . SER   A 129 ? 0.39120 0.34673 0.31755 -0.06451 -0.02892 -0.05990 281 SER   A O    
832  C  CB   . SER   A 129 ? 0.41807 0.36939 0.33339 -0.05031 -0.02957 -0.08986 281 SER   A CB   
833  O  OG   . SER   A 129 ? 0.44726 0.37839 0.36988 -0.05388 -0.03563 -0.08855 281 SER   A OG   
834  N  N    . TRP   A 130 ? 0.38681 0.34473 0.31267 -0.05073 -0.02113 -0.06335 282 TRP   A N    
835  C  CA   . TRP   A 130 ? 0.37572 0.32833 0.30794 -0.05173 -0.02022 -0.05428 282 TRP   A CA   
836  C  C    . TRP   A 130 ? 0.39676 0.33115 0.33271 -0.04931 -0.02389 -0.05783 282 TRP   A C    
837  O  O    . TRP   A 130 ? 0.42610 0.35810 0.36254 -0.04161 -0.02208 -0.06418 282 TRP   A O    
838  C  CB   . TRP   A 130 ? 0.34894 0.31349 0.28308 -0.04668 -0.01373 -0.04858 282 TRP   A CB   
839  C  CG   . TRP   A 130 ? 0.32995 0.31102 0.26392 -0.04880 -0.01122 -0.04309 282 TRP   A CG   
840  C  CD1  . TRP   A 130 ? 0.31965 0.30685 0.25873 -0.05236 -0.01059 -0.03549 282 TRP   A CD1  
841  C  CD2  . TRP   A 130 ? 0.30735 0.30175 0.23704 -0.04705 -0.00944 -0.04466 282 TRP   A CD2  
842  N  NE1  . TRP   A 130 ? 0.30532 0.30685 0.24528 -0.05234 -0.00920 -0.03257 282 TRP   A NE1  
843  C  CE2  . TRP   A 130 ? 0.29603 0.30204 0.22987 -0.04963 -0.00874 -0.03694 282 TRP   A CE2  
844  C  CE3  . TRP   A 130 ? 0.31667 0.31580 0.23961 -0.04369 -0.00858 -0.05192 282 TRP   A CE3  
845  C  CZ2  . TRP   A 130 ? 0.29340 0.31369 0.22541 -0.04944 -0.00822 -0.03452 282 TRP   A CZ2  
846  C  CZ3  . TRP   A 130 ? 0.31139 0.32710 0.23053 -0.04413 -0.00722 -0.04939 282 TRP   A CZ3  
847  C  CH2  . TRP   A 130 ? 0.29130 0.31647 0.21526 -0.04719 -0.00752 -0.03989 282 TRP   A CH2  
848  N  N    . ASP   A 131 ? 0.39522 0.31787 0.33482 -0.05608 -0.02939 -0.05316 283 ASP   A N    
849  C  CA   . ASP   A 131 ? 0.43241 0.33543 0.37707 -0.05532 -0.03549 -0.05553 283 ASP   A CA   
850  C  C    . ASP   A 131 ? 0.42074 0.32107 0.36979 -0.05557 -0.03459 -0.04515 283 ASP   A C    
851  O  O    . ASP   A 131 ? 0.42225 0.32409 0.37235 -0.06356 -0.03616 -0.03540 283 ASP   A O    
852  C  CB   . ASP   A 131 ? 0.47554 0.36638 0.42199 -0.06390 -0.04397 -0.05657 283 ASP   A CB   
853  C  CG   . ASP   A 131 ? 0.53198 0.40039 0.48548 -0.06226 -0.05205 -0.06104 283 ASP   A CG   
854  O  OD1  . ASP   A 131 ? 0.54078 0.40358 0.49823 -0.05486 -0.05100 -0.06162 283 ASP   A OD1  
855  O  OD2  . ASP   A 131 ? 0.55819 0.41995 0.51730 -0.06637 -0.05748 -0.06260 283 ASP   A OD2  
856  N  N    . CYS   A 132 ? 0.42975 0.32792 0.38136 -0.04707 -0.03210 -0.04746 284 CYS   A N    
857  C  CA   . CYS   A 132 ? 0.41727 0.31407 0.37265 -0.04651 -0.03143 -0.03842 284 CYS   A CA   
858  C  C    . CYS   A 132 ? 0.45782 0.33512 0.42004 -0.04540 -0.03902 -0.03803 284 CYS   A C    
859  O  O    . CYS   A 132 ? 0.42354 0.29803 0.39005 -0.03913 -0.03843 -0.03714 284 CYS   A O    
860  C  CB   . CYS   A 132 ? 0.40636 0.31593 0.36136 -0.03863 -0.02383 -0.03922 284 CYS   A CB   
861  S  SG   . CYS   A 132 ? 0.37308 0.30372 0.32363 -0.04153 -0.01706 -0.03514 284 CYS   A SG   
862  N  N    . GLY   A 133 ? 0.52112 0.38437 0.48583 -0.05184 -0.04715 -0.03803 285 GLY   A N    
863  C  CA   . GLY   A 133 ? 0.54911 0.39303 0.52192 -0.05379 -0.05638 -0.03342 285 GLY   A CA   
864  C  C    . GLY   A 133 ? 0.57668 0.40597 0.55768 -0.04546 -0.06128 -0.04515 285 GLY   A C    
865  O  O    . GLY   A 133 ? 0.59668 0.41396 0.58681 -0.04650 -0.06811 -0.04061 285 GLY   A O    
866  N  N    . SER   A 134 ? 0.56955 0.40395 0.54815 -0.03658 -0.05679 -0.05945 286 SER   A N    
867  C  CA   . SER   A 134 ? 0.59166 0.41908 0.57867 -0.02689 -0.05857 -0.07113 286 SER   A CA   
868  C  C    . SER   A 134 ? 0.59061 0.43094 0.57101 -0.02022 -0.05196 -0.08617 286 SER   A C    
869  O  O    . SER   A 134 ? 0.56341 0.41866 0.53417 -0.02147 -0.04568 -0.08586 286 SER   A O    
870  C  CB   . SER   A 134 ? 0.61100 0.43310 0.60679 -0.01926 -0.05968 -0.06835 286 SER   A CB   
871  O  OG   . SER   A 134 ? 0.60213 0.43656 0.59377 -0.01252 -0.05229 -0.07244 286 SER   A OG   
872  N  N    . GLN   A 135 ? 0.62399 0.46106 0.60972 -0.01308 -0.05303 -0.09814 287 GLN   A N    
873  C  CA   . GLN   A 135 ? 0.65569 0.50691 0.63408 -0.00805 -0.04721 -0.11195 287 GLN   A CA   
874  C  C    . GLN   A 135 ? 0.63669 0.50590 0.61056 -0.00096 -0.03834 -0.11465 287 GLN   A C    
875  O  O    . GLN   A 135 ? 0.62062 0.50711 0.58415 -0.00157 -0.03231 -0.11842 287 GLN   A O    
876  C  CB   . GLN   A 135 ? 0.70856 0.55293 0.69453 -0.00151 -0.05069 -0.12400 287 GLN   A CB   
877  C  CG   . GLN   A 135 ? 0.74953 0.60696 0.72680 0.00075  -0.04679 -0.13734 287 GLN   A CG   
878  C  CD   . GLN   A 135 ? 0.78567 0.64476 0.75303 -0.00967 -0.04828 -0.13478 287 GLN   A CD   
879  O  OE1  . GLN   A 135 ? 0.80850 0.65351 0.78010 -0.01767 -0.05515 -0.12853 287 GLN   A OE1  
880  N  NE2  . GLN   A 135 ? 0.78734 0.66538 0.74216 -0.00992 -0.04204 -0.13859 287 GLN   A NE2  
881  N  N    . ASP   A 136 ? 0.63816 0.50507 0.62034 0.00547  -0.03761 -0.11190 288 ASP   A N    
882  C  CA   . ASP   A 136 ? 0.62574 0.51090 0.60549 0.01201  -0.02904 -0.11398 288 ASP   A CA   
883  C  C    . ASP   A 136 ? 0.55077 0.44892 0.52137 0.00504  -0.02340 -0.10114 288 ASP   A C    
884  O  O    . ASP   A 136 ? 0.53416 0.45253 0.49937 0.00737  -0.01516 -0.10115 288 ASP   A O    
885  C  CB   . ASP   A 136 ? 0.67339 0.55351 0.66517 0.01946  -0.02992 -0.11170 288 ASP   A CB   
886  C  CG   . ASP   A 136 ? 0.76369 0.64409 0.76442 0.02854  -0.03057 -0.12290 288 ASP   A CG   
887  O  OD1  . ASP   A 136 ? 0.81855 0.68251 0.83066 0.03022  -0.03813 -0.12118 288 ASP   A OD1  
888  O  OD2  . ASP   A 136 ? 0.80079 0.69922 0.79748 0.03362  -0.02385 -0.13296 288 ASP   A OD2  
889  N  N    . TYR   A 137 ? 0.50790 0.39670 0.47745 -0.00386 -0.02746 -0.08884 289 TYR   A N    
890  C  CA   . TYR   A 137 ? 0.46275 0.36423 0.42562 -0.01026 -0.02238 -0.07649 289 TYR   A CA   
891  C  C    . TYR   A 137 ? 0.44457 0.34789 0.39998 -0.01885 -0.02402 -0.07542 289 TYR   A C    
892  O  O    . TYR   A 137 ? 0.44103 0.34598 0.39444 -0.02640 -0.02433 -0.06482 289 TYR   A O    
893  C  CB   . TYR   A 137 ? 0.44212 0.33717 0.40958 -0.01336 -0.02441 -0.06357 289 TYR   A CB   
894  C  CG   . TYR   A 137 ? 0.43411 0.32443 0.41045 -0.00534 -0.02508 -0.06464 289 TYR   A CG   
895  C  CD1  . TYR   A 137 ? 0.45520 0.32959 0.43872 -0.00678 -0.03244 -0.05832 289 TYR   A CD1  
896  C  CD2  . TYR   A 137 ? 0.41778 0.32093 0.39592 0.00320  -0.01875 -0.07108 289 TYR   A CD2  
897  C  CE1  . TYR   A 137 ? 0.44829 0.31881 0.44102 0.00079  -0.03383 -0.05901 289 TYR   A CE1  
898  C  CE2  . TYR   A 137 ? 0.42603 0.32641 0.41366 0.01070  -0.01943 -0.07231 289 TYR   A CE2  
899  C  CZ   . TYR   A 137 ? 0.44534 0.32890 0.44051 0.00983  -0.02718 -0.06657 289 TYR   A CZ   
900  O  OH   . TYR   A 137 ? 0.45894 0.34019 0.46461 0.01751  -0.02858 -0.06739 289 TYR   A OH   
901  N  N    . LYS   A 138 ? 0.44052 0.34512 0.39217 -0.01762 -0.02515 -0.08723 290 LYS   A N    
902  C  CA   . LYS   A 138 ? 0.45192 0.36214 0.39602 -0.02488 -0.02611 -0.08757 290 LYS   A CA   
903  C  C    . LYS   A 138 ? 0.42247 0.35418 0.35881 -0.02146 -0.01895 -0.09216 290 LYS   A C    
904  O  O    . LYS   A 138 ? 0.40911 0.34603 0.34445 -0.01449 -0.01701 -0.10392 290 LYS   A O    
905  C  CB   . LYS   A 138 ? 0.50424 0.39853 0.45018 -0.02748 -0.03471 -0.09733 290 LYS   A CB   
906  C  CG   . LYS   A 138 ? 0.54927 0.44669 0.48923 -0.03684 -0.03755 -0.09576 290 LYS   A CG   
907  C  CD   . LYS   A 138 ? 0.61030 0.49269 0.55396 -0.03923 -0.04539 -0.10463 290 LYS   A CD   
908  C  CE   . LYS   A 138 ? 0.64550 0.53589 0.58219 -0.04652 -0.04682 -0.10689 290 LYS   A CE   
909  N  NZ   . LYS   A 138 ? 0.66949 0.55364 0.61266 -0.05679 -0.05221 -0.09667 290 LYS   A NZ   
910  N  N    . TYR   A 139 ? 0.40313 0.34847 0.33485 -0.02627 -0.01527 -0.08269 291 TYR   A N    
911  C  CA   . TYR   A 139 ? 0.38690 0.35332 0.31281 -0.02387 -0.00890 -0.08254 291 TYR   A CA   
912  C  C    . TYR   A 139 ? 0.38831 0.36397 0.30626 -0.02964 -0.01060 -0.08414 291 TYR   A C    
913  O  O    . TYR   A 139 ? 0.37478 0.34689 0.29324 -0.03669 -0.01395 -0.07781 291 TYR   A O    
914  C  CB   . TYR   A 139 ? 0.35722 0.33238 0.28673 -0.02384 -0.00413 -0.06979 291 TYR   A CB   
915  C  CG   . TYR   A 139 ? 0.33462 0.30005 0.27205 -0.01953 -0.00362 -0.06708 291 TYR   A CG   
916  C  CD1  . TYR   A 139 ? 0.32645 0.28173 0.26846 -0.02348 -0.00634 -0.05889 291 TYR   A CD1  
917  C  CD2  . TYR   A 139 ? 0.34000 0.30828 0.28038 -0.01169 -0.00057 -0.07290 291 TYR   A CD2  
918  C  CE1  . TYR   A 139 ? 0.33419 0.28159 0.28271 -0.02001 -0.00660 -0.05594 291 TYR   A CE1  
919  C  CE2  . TYR   A 139 ? 0.32573 0.28557 0.27416 -0.00772 -0.00083 -0.07012 291 TYR   A CE2  
920  C  CZ   . TYR   A 139 ? 0.33311 0.28205 0.28515 -0.01205 -0.00417 -0.06138 291 TYR   A CZ   
921  O  OH   . TYR   A 139 ? 0.34749 0.28909 0.30672 -0.00871 -0.00514 -0.05797 291 TYR   A OH   
922  N  N    . ASP   A 140 ? 0.40528 0.39474 0.31601 -0.02683 -0.00830 -0.09258 292 ASP   A N    
923  C  CA   . ASP   A 140 ? 0.43050 0.43182 0.33258 -0.03204 -0.01001 -0.09413 292 ASP   A CA   
924  C  C    . ASP   A 140 ? 0.38965 0.41437 0.28687 -0.03130 -0.00431 -0.08719 292 ASP   A C    
925  O  O    . ASP   A 140 ? 0.37452 0.40485 0.27620 -0.02759 0.00064  -0.08035 292 ASP   A O    
926  C  CB   . ASP   A 140 ? 0.49541 0.49239 0.39361 -0.02977 -0.01393 -0.10790 292 ASP   A CB   
927  C  CG   . ASP   A 140 ? 0.55637 0.55929 0.45453 -0.02063 -0.00959 -0.11677 292 ASP   A CG   
928  O  OD1  . ASP   A 140 ? 0.60488 0.59467 0.50622 -0.01666 -0.01300 -0.12739 292 ASP   A OD1  
929  O  OD2  . ASP   A 140 ? 0.55921 0.58031 0.45533 -0.01775 -0.00294 -0.11261 292 ASP   A OD2  
930  N  N    . VAL   A 141 ? 0.37927 0.41727 0.26884 -0.03482 -0.00577 -0.08749 293 VAL   A N    
931  C  CA   . VAL   A 141 ? 0.35742 0.41762 0.24325 -0.03554 -0.00192 -0.07830 293 VAL   A CA   
932  C  C    . VAL   A 141 ? 0.36074 0.43274 0.24547 -0.02890 0.00404  -0.08187 293 VAL   A C    
933  O  O    . VAL   A 141 ? 0.35842 0.44585 0.24379 -0.02885 0.00828  -0.07225 293 VAL   A O    
934  C  CB   . VAL   A 141 ? 0.37190 0.44219 0.25198 -0.04018 -0.00571 -0.07659 293 VAL   A CB   
935  C  CG1  . VAL   A 141 ? 0.37750 0.44151 0.26109 -0.04715 -0.01071 -0.06925 293 VAL   A CG1  
936  C  CG2  . VAL   A 141 ? 0.37262 0.43788 0.24812 -0.03769 -0.00828 -0.09047 293 VAL   A CG2  
937  N  N    . THR   A 142 ? 0.35954 0.42499 0.24398 -0.02342 0.00405  -0.09517 294 THR   A N    
938  C  CA   . THR   A 142 ? 0.38228 0.46087 0.26700 -0.01705 0.00985  -0.09950 294 THR   A CA   
939  C  C    . THR   A 142 ? 0.37040 0.44658 0.26273 -0.01319 0.01419  -0.09543 294 THR   A C    
940  O  O    . THR   A 142 ? 0.36609 0.45948 0.25953 -0.01097 0.01975  -0.09062 294 THR   A O    
941  C  CB   . THR   A 142 ? 0.41737 0.48866 0.30179 -0.01180 0.00814  -0.11560 294 THR   A CB   
942  O  OG1  . THR   A 142 ? 0.45425 0.52545 0.33183 -0.01596 0.00326  -0.11965 294 THR   A OG1  
943  C  CG2  . THR   A 142 ? 0.43266 0.52286 0.31722 -0.00603 0.01432  -0.12032 294 THR   A CG2  
944  N  N    . ASP   A 143 ? 0.36649 0.42222 0.26467 -0.01304 0.01142  -0.09657 295 ASP   A N    
945  C  CA   . ASP   A 143 ? 0.37161 0.42305 0.27898 -0.00942 0.01472  -0.09057 295 ASP   A CA   
946  C  C    . ASP   A 143 ? 0.34618 0.40980 0.25583 -0.01310 0.01754  -0.07377 295 ASP   A C    
947  O  O    . ASP   A 143 ? 0.33943 0.41288 0.25401 -0.01000 0.02223  -0.06874 295 ASP   A O    
948  C  CB   . ASP   A 143 ? 0.39739 0.42266 0.31296 -0.00948 0.00975  -0.08999 295 ASP   A CB   
949  C  CG   . ASP   A 143 ? 0.45281 0.46366 0.37063 -0.00461 0.00620  -0.10535 295 ASP   A CG   
950  O  OD1  . ASP   A 143 ? 0.47232 0.49196 0.39056 0.00220  0.00941  -0.11544 295 ASP   A OD1  
951  O  OD2  . ASP   A 143 ? 0.46663 0.45756 0.38728 -0.00768 -0.00021 -0.10641 295 ASP   A OD2  
952  N  N    . VAL   A 144 ? 0.33564 0.39892 0.24334 -0.01965 0.01416  -0.06511 296 VAL   A N    
953  C  CA   . VAL   A 144 ? 0.31916 0.39214 0.23154 -0.02278 0.01532  -0.04973 296 VAL   A CA   
954  C  C    . VAL   A 144 ? 0.32740 0.42507 0.23448 -0.02333 0.01917  -0.04582 296 VAL   A C    
955  O  O    . VAL   A 144 ? 0.33086 0.43747 0.24448 -0.02345 0.02166  -0.03482 296 VAL   A O    
956  C  CB   . VAL   A 144 ? 0.32799 0.39612 0.24106 -0.02892 0.01029  -0.04284 296 VAL   A CB   
957  C  CG1  . VAL   A 144 ? 0.30895 0.38476 0.23024 -0.03104 0.01038  -0.02800 296 VAL   A CG1  
958  C  CG2  . VAL   A 144 ? 0.31643 0.36328 0.23388 -0.02943 0.00689  -0.04650 296 VAL   A CG2  
959  N  N    A SER   A 145 ? 0.34486 0.45501 0.24015 -0.02428 0.01933  -0.05450 297 SER   A N    
960  N  N    B SER   A 145 ? 0.34547 0.45571 0.24075 -0.02425 0.01937  -0.05451 297 SER   A N    
961  C  CA   A SER   A 145 ? 0.35099 0.48398 0.24393 -0.02444 0.02268  -0.04971 297 SER   A CA   
962  C  CA   B SER   A 145 ? 0.35011 0.48328 0.24316 -0.02452 0.02270  -0.04936 297 SER   A CA   
963  C  C    A SER   A 145 ? 0.34595 0.48543 0.24429 -0.01859 0.02865  -0.05238 297 SER   A C    
964  C  C    B SER   A 145 ? 0.34731 0.48707 0.24549 -0.01855 0.02866  -0.05260 297 SER   A C    
965  O  O    A SER   A 145 ? 0.33361 0.49051 0.23502 -0.01995 0.03169  -0.04218 297 SER   A O    
966  O  O    B SER   A 145 ? 0.33134 0.48906 0.23224 -0.01983 0.03175  -0.04291 297 SER   A O    
967  C  CB   A SER   A 145 ? 0.37481 0.51453 0.25958 -0.02494 0.02081  -0.05858 297 SER   A CB   
968  C  CB   B SER   A 145 ? 0.37422 0.51486 0.25898 -0.02550 0.02066  -0.05722 297 SER   A CB   
969  O  OG   A SER   A 145 ? 0.37036 0.51278 0.25118 -0.03139 0.01584  -0.05153 297 SER   A OG   
970  O  OG   B SER   A 145 ? 0.40180 0.53282 0.28529 -0.01967 0.02121  -0.07404 297 SER   A OG   
971  N  N    . LYS   A 146 ? 0.35503 0.48046 0.25617 -0.01232 0.02962  -0.06534 298 LYS   A N    
972  C  CA   . LYS   A 146 ? 0.35462 0.48562 0.26247 -0.00591 0.03476  -0.06934 298 LYS   A CA   
973  C  C    . LYS   A 146 ? 0.34017 0.46842 0.25732 -0.00564 0.03699  -0.05901 298 LYS   A C    
974  O  O    . LYS   A 146 ? 0.34207 0.47389 0.26649 -0.00029 0.04092  -0.06177 298 LYS   A O    
975  C  CB   . LYS   A 146 ? 0.38035 0.49592 0.29032 0.00115  0.03352  -0.08655 298 LYS   A CB   
976  C  CG   . LYS   A 146 ? 0.43162 0.55236 0.33502 0.00220  0.03198  -0.09792 298 LYS   A CG   
977  C  CD   . LYS   A 146 ? 0.49501 0.64341 0.39593 0.00190  0.03677  -0.09531 298 LYS   A CD   
978  C  CE   . LYS   A 146 ? 0.56701 0.72042 0.46943 0.00879  0.03843  -0.11138 298 LYS   A CE   
979  N  NZ   . LYS   A 146 ? 0.61216 0.78953 0.51862 0.01116  0.04465  -0.10915 298 LYS   A NZ   
980  N  N    . ALA   A 147 ? 0.32029 0.43871 0.24165 -0.01076 0.03303  -0.04603 299 ALA   A N    
981  C  CA   . ALA   A 147 ? 0.30467 0.42128 0.23797 -0.01156 0.03346  -0.03273 299 ALA   A CA   
982  C  C    . ALA   A 147 ? 0.30015 0.43630 0.23389 -0.01744 0.03392  -0.01790 299 ALA   A C    
983  O  O    . ALA   A 147 ? 0.28222 0.41727 0.22712 -0.01896 0.03313  -0.00604 299 ALA   A O    
984  C  CB   . ALA   A 147 ? 0.28339 0.37654 0.22347 -0.01264 0.02845  -0.02923 299 ALA   A CB   
985  N  N    . GLY   A 148 ? 0.30937 0.46313 0.23168 -0.02116 0.03428  -0.01805 300 GLY   A N    
986  C  CA   . GLY   A 148 ? 0.30629 0.47934 0.22957 -0.02713 0.03359  -0.00287 300 GLY   A CA   
987  C  C    . GLY   A 148 ? 0.31162 0.48408 0.23171 -0.03337 0.02747  0.00574  300 GLY   A C    
988  O  O    . GLY   A 148 ? 0.32321 0.50938 0.24636 -0.03825 0.02496  0.01889  300 GLY   A O    
989  N  N    . HIS   A 149 ? 0.28920 0.44467 0.20625 -0.03319 0.02373  -0.00091 301 HIS   A N    
990  C  CA   . HIS   A 149 ? 0.27901 0.43264 0.19673 -0.03856 0.01736  0.00786  301 HIS   A CA   
991  C  C    . HIS   A 149 ? 0.29720 0.46159 0.20192 -0.04143 0.01545  0.00242  301 HIS   A C    
992  O  O    . HIS   A 149 ? 0.30653 0.47056 0.20392 -0.03800 0.01791  -0.01181 301 HIS   A O    
993  C  CB   . HIS   A 149 ? 0.27495 0.40421 0.20075 -0.03696 0.01360  0.00476  301 HIS   A CB   
994  C  CG   . HIS   A 149 ? 0.26166 0.38107 0.20327 -0.03520 0.01314  0.01272  301 HIS   A CG   
995  N  ND1  . HIS   A 149 ? 0.25677 0.38223 0.20931 -0.03831 0.00978  0.02745  301 HIS   A ND1  
996  C  CD2  . HIS   A 149 ? 0.25504 0.35939 0.20377 -0.03075 0.01496  0.00773  301 HIS   A CD2  
997  C  CE1  . HIS   A 149 ? 0.25064 0.36489 0.21646 -0.03559 0.00969  0.02978  301 HIS   A CE1  
998  N  NE2  . HIS   A 149 ? 0.24591 0.34810 0.20883 -0.03116 0.01302  0.01817  301 HIS   A NE2  
999  N  N    . THR   A 150 ? 0.30844 0.47971 0.21451 -0.04693 0.00995  0.01375  302 THR   A N    
1000 C  CA   . THR   A 150 ? 0.31092 0.49257 0.20910 -0.05003 0.00700  0.01142  302 THR   A CA   
1001 C  C    . THR   A 150 ? 0.31206 0.48297 0.20842 -0.05269 0.00110  0.00948  302 THR   A C    
1002 O  O    . THR   A 150 ? 0.30365 0.46146 0.20553 -0.05281 -0.00118 0.01190  302 THR   A O    
1003 C  CB   . THR   A 150 ? 0.31856 0.51984 0.22089 -0.05495 0.00465  0.02710  302 THR   A CB   
1004 O  OG1  . THR   A 150 ? 0.32893 0.52628 0.24124 -0.05879 -0.00173 0.04195  302 THR   A OG1  
1005 C  CG2  . THR   A 150 ? 0.33450 0.54632 0.24176 -0.05340 0.00957  0.03177  302 THR   A CG2  
1006 N  N    . LEU   A 151 ? 0.30611 0.48434 0.19504 -0.05515 -0.00150 0.00517  303 LEU   A N    
1007 C  CA   . LEU   A 151 ? 0.32075 0.49083 0.20823 -0.05806 -0.00731 0.00266  303 LEU   A CA   
1008 C  C    . LEU   A 151 ? 0.31114 0.48211 0.20864 -0.06202 -0.01337 0.01825  303 LEU   A C    
1009 O  O    . LEU   A 151 ? 0.31441 0.47595 0.21450 -0.06357 -0.01792 0.01661  303 LEU   A O    
1010 C  CB   . LEU   A 151 ? 0.37608 0.55664 0.25433 -0.06017 -0.00894 -0.00345 303 LEU   A CB   
1011 C  CG   . LEU   A 151 ? 0.43353 0.60740 0.30923 -0.06323 -0.01475 -0.00816 303 LEU   A CG   
1012 C  CD1  . LEU   A 151 ? 0.46811 0.64357 0.33309 -0.06206 -0.01398 -0.02306 303 LEU   A CD1  
1013 C  CD2  . LEU   A 151 ? 0.45854 0.64388 0.33905 -0.06874 -0.02084 0.00663  303 LEU   A CD2  
1014 N  N    . GLU   A 152 ? 0.32135 0.50352 0.22640 -0.06369 -0.01420 0.03341  304 GLU   A N    
1015 C  CA   . GLU   A 152 ? 0.34499 0.52617 0.26306 -0.06631 -0.02096 0.04866  304 GLU   A CA   
1016 C  C    . GLU   A 152 ? 0.30210 0.46312 0.23109 -0.06249 -0.02115 0.04445  304 GLU   A C    
1017 O  O    . GLU   A 152 ? 0.27338 0.42842 0.21412 -0.06302 -0.02679 0.04841  304 GLU   A O    
1018 C  CB   . GLU   A 152 ? 0.42786 0.61937 0.35571 -0.06767 -0.02127 0.06436  304 GLU   A CB   
1019 C  CG   . GLU   A 152 ? 0.51556 0.72590 0.44156 -0.07232 -0.02341 0.07231  304 GLU   A CG   
1020 C  CD   . GLU   A 152 ? 0.58769 0.80186 0.52899 -0.07638 -0.03201 0.09073  304 GLU   A CD   
1021 O  OE1  . GLU   A 152 ? 0.60787 0.81449 0.55482 -0.07670 -0.03818 0.09230  304 GLU   A OE1  
1022 O  OE2  . GLU   A 152 ? 0.64091 0.86565 0.59027 -0.07918 -0.03310 0.10344  304 GLU   A OE2  
1023 N  N    . LEU   A 153 ? 0.28452 0.43430 0.21341 -0.05776 -0.01460 0.03555  305 LEU   A N    
1024 C  CA   . LEU   A 153 ? 0.24594 0.37583 0.18543 -0.05371 -0.01356 0.02923  305 LEU   A CA   
1025 C  C    . LEU   A 153 ? 0.27084 0.39042 0.20093 -0.05331 -0.01231 0.01445  305 LEU   A C    
1026 O  O    . LEU   A 153 ? 0.26878 0.37797 0.20577 -0.05350 -0.01475 0.01179  305 LEU   A O    
1027 C  CB   . LEU   A 153 ? 0.21196 0.33526 0.15775 -0.04930 -0.00830 0.02921  305 LEU   A CB   
1028 C  CG   . LEU   A 153 ? 0.19468 0.29928 0.14943 -0.04517 -0.00660 0.02240  305 LEU   A CG   
1029 C  CD1  . LEU   A 153 ? 0.18761 0.28758 0.15834 -0.04532 -0.01166 0.02841  305 LEU   A CD1  
1030 C  CD2  . LEU   A 153 ? 0.18456 0.28516 0.14305 -0.04120 -0.00162 0.02188  305 LEU   A CD2  
1031 N  N    . ILE   A 154 ? 0.27599 0.39932 0.19130 -0.05301 -0.00894 0.00464  306 ILE   A N    
1032 C  CA   . ILE   A 154 ? 0.29297 0.40256 0.20220 -0.05182 -0.00797 -0.00979 306 ILE   A CA   
1033 C  C    . ILE   A 154 ? 0.29985 0.40857 0.20638 -0.05657 -0.01370 -0.01248 306 ILE   A C    
1034 O  O    . ILE   A 154 ? 0.27409 0.36882 0.18461 -0.05707 -0.01504 -0.01783 306 ILE   A O    
1035 C  CB   . ILE   A 154 ? 0.30703 0.42079 0.20372 -0.04923 -0.00360 -0.02105 306 ILE   A CB   
1036 C  CG1  . ILE   A 154 ? 0.29704 0.40904 0.19909 -0.04401 0.00222  -0.01967 306 ILE   A CG1  
1037 C  CG2  . ILE   A 154 ? 0.32407 0.42324 0.21552 -0.04874 -0.00489 -0.03582 306 ILE   A CG2  
1038 C  CD1  . ILE   A 154 ? 0.31543 0.43690 0.20715 -0.04089 0.00694  -0.02980 306 ILE   A CD1  
1039 N  N    A GLU   A 155 ? 0.33117 0.45606 0.23092 -0.06074 -0.01743 -0.00826 307 GLU   A N    
1040 N  N    B GLU   A 155 ? 0.33109 0.45592 0.23094 -0.06073 -0.01744 -0.00819 307 GLU   A N    
1041 C  CA   A GLU   A 155 ? 0.34601 0.47174 0.24406 -0.06561 -0.02353 -0.01026 307 GLU   A CA   
1042 C  CA   B GLU   A 155 ? 0.34602 0.47160 0.24406 -0.06559 -0.02351 -0.01037 307 GLU   A CA   
1043 C  C    A GLU   A 155 ? 0.33243 0.45100 0.24643 -0.06629 -0.02673 -0.00334 307 GLU   A C    
1044 C  C    B GLU   A 155 ? 0.33268 0.45137 0.24663 -0.06635 -0.02679 -0.00332 307 GLU   A C    
1045 O  O    A GLU   A 155 ? 0.33873 0.44745 0.25469 -0.06814 -0.02843 -0.00983 307 GLU   A O    
1046 O  O    B GLU   A 155 ? 0.33879 0.44795 0.25466 -0.06830 -0.02863 -0.00971 307 GLU   A O    
1047 C  CB   A GLU   A 155 ? 0.37011 0.51241 0.26403 -0.06805 -0.02610 -0.00469 307 GLU   A CB   
1048 C  CB   B GLU   A 155 ? 0.37058 0.51259 0.26417 -0.06796 -0.02596 -0.00521 307 GLU   A CB   
1049 C  CG   A GLU   A 155 ? 0.39993 0.54206 0.29291 -0.07198 -0.03159 -0.00809 307 GLU   A CG   
1050 C  CG   B GLU   A 155 ? 0.39788 0.54114 0.29297 -0.07231 -0.03221 -0.00537 307 GLU   A CG   
1051 C  CD   A GLU   A 155 ? 0.40641 0.56049 0.30731 -0.07569 -0.03772 0.00548  307 GLU   A CD   
1052 C  CD   B GLU   A 155 ? 0.42132 0.56689 0.30542 -0.07295 -0.03242 -0.01589 307 GLU   A CD   
1053 O  OE1  A GLU   A 155 ? 0.40212 0.56035 0.31280 -0.07521 -0.03917 0.01753  307 GLU   A OE1  
1054 O  OE1  B GLU   A 155 ? 0.43580 0.58702 0.31172 -0.07020 -0.02817 -0.02084 307 GLU   A OE1  
1055 O  OE2  A GLU   A 155 ? 0.42689 0.58575 0.32540 -0.07884 -0.04181 0.00412  307 GLU   A OE2  
1056 O  OE2  B GLU   A 155 ? 0.42868 0.57117 0.31314 -0.07610 -0.03704 -0.01950 307 GLU   A OE2  
1057 N  N    . PRO   A 156 ? 0.32329 0.44682 0.25003 -0.06501 -0.02799 0.00907  308 PRO   A N    
1058 C  CA   . PRO   A 156 ? 0.31193 0.42934 0.25515 -0.06445 -0.03056 0.01259  308 PRO   A CA   
1059 C  C    . PRO   A 156 ? 0.30440 0.40596 0.25221 -0.06143 -0.02597 0.00532  308 PRO   A C    
1060 O  O    . PRO   A 156 ? 0.30334 0.40086 0.25968 -0.06250 -0.02746 0.00364  308 PRO   A O    
1061 C  CB   . PRO   A 156 ? 0.33283 0.45746 0.28946 -0.06251 -0.03289 0.02596  308 PRO   A CB   
1062 C  CG   . PRO   A 156 ? 0.35892 0.49745 0.30447 -0.06485 -0.03369 0.03226  308 PRO   A CG   
1063 C  CD   . PRO   A 156 ? 0.33652 0.47190 0.26507 -0.06423 -0.02773 0.02051  308 PRO   A CD   
1064 N  N    . LEU   A 157 ? 0.27846 0.37268 0.22110 -0.05794 -0.02055 0.00135  309 LEU   A N    
1065 C  CA   . LEU   A 157 ? 0.24972 0.32938 0.19579 -0.05560 -0.01700 -0.00470 309 LEU   A CA   
1066 C  C    . LEU   A 157 ? 0.25715 0.32878 0.19628 -0.05929 -0.01833 -0.01370 309 LEU   A C    
1067 O  O    . LEU   A 157 ? 0.24417 0.30895 0.18972 -0.06067 -0.01853 -0.01505 309 LEU   A O    
1068 C  CB   . LEU   A 157 ? 0.24770 0.32223 0.19019 -0.05105 -0.01177 -0.00670 309 LEU   A CB   
1069 C  CG   . LEU   A 157 ? 0.24527 0.30493 0.19012 -0.04869 -0.00872 -0.01238 309 LEU   A CG   
1070 C  CD1  . LEU   A 157 ? 0.24488 0.30288 0.20326 -0.04816 -0.00929 -0.00799 309 LEU   A CD1  
1071 C  CD2  . LEU   A 157 ? 0.24729 0.30349 0.18956 -0.04391 -0.00415 -0.01420 309 LEU   A CD2  
1072 N  N    . ILE   A 158 ? 0.27270 0.34600 0.19915 -0.06134 -0.01959 -0.02005 310 ILE   A N    
1073 C  CA   . ILE   A 158 ? 0.29861 0.36344 0.21990 -0.06555 -0.02244 -0.02859 310 ILE   A CA   
1074 C  C    . ILE   A 158 ? 0.30917 0.37973 0.23704 -0.07099 -0.02723 -0.02485 310 ILE   A C    
1075 O  O    . ILE   A 158 ? 0.32344 0.38632 0.25508 -0.07456 -0.02860 -0.02736 310 ILE   A O    
1076 C  CB   . ILE   A 158 ? 0.32598 0.39294 0.23330 -0.06615 -0.02358 -0.03782 310 ILE   A CB   
1077 C  CG1  . ILE   A 158 ? 0.34490 0.40585 0.24768 -0.06020 -0.01854 -0.04367 310 ILE   A CG1  
1078 C  CG2  . ILE   A 158 ? 0.33392 0.39234 0.23832 -0.07122 -0.02845 -0.04599 310 ILE   A CG2  
1079 C  CD1  . ILE   A 158 ? 0.36796 0.40954 0.27376 -0.05896 -0.01810 -0.05016 310 ILE   A CD1  
1080 N  N    . LYS   A 159 ? 0.30124 0.38646 0.23148 -0.07206 -0.03020 -0.01804 311 LYS   A N    
1081 C  CA   . LYS   A 159 ? 0.29661 0.38907 0.23549 -0.07646 -0.03501 -0.01432 311 LYS   A CA   
1082 C  C    . LYS   A 159 ? 0.26428 0.35333 0.21766 -0.07506 -0.03292 -0.01136 311 LYS   A C    
1083 O  O    . LYS   A 159 ? 0.25431 0.34383 0.21301 -0.07937 -0.03483 -0.01287 311 LYS   A O    
1084 C  CB   . LYS   A 159 ? 0.33068 0.43934 0.27211 -0.07683 -0.03916 -0.00586 311 LYS   A CB   
1085 C  CG   . LYS   A 159 ? 0.39988 0.51648 0.32798 -0.08065 -0.04302 -0.00887 311 LYS   A CG   
1086 C  CD   . LYS   A 159 ? 0.45286 0.58565 0.38439 -0.08096 -0.04721 0.00204  311 LYS   A CD   
1087 C  CE   . LYS   A 159 ? 0.51897 0.65819 0.43841 -0.08274 -0.04860 -0.00067 311 LYS   A CE   
1088 N  NZ   . LYS   A 159 ? 0.55607 0.68398 0.46404 -0.08231 -0.04545 -0.01436 311 LYS   A NZ   
1089 N  N    . PHE   A 160 ? 0.24752 0.33464 0.20754 -0.06939 -0.02902 -0.00752 312 PHE   A N    
1090 C  CA   . PHE   A 160 ? 0.24509 0.32995 0.21771 -0.06748 -0.02657 -0.00666 312 PHE   A CA   
1091 C  C    . PHE   A 160 ? 0.26887 0.34287 0.23694 -0.07057 -0.02431 -0.01262 312 PHE   A C    
1092 O  O    . PHE   A 160 ? 0.28609 0.36339 0.26122 -0.07399 -0.02475 -0.01290 312 PHE   A O    
1093 C  CB   . PHE   A 160 ? 0.25044 0.33343 0.22931 -0.06100 -0.02328 -0.00295 312 PHE   A CB   
1094 C  CG   . PHE   A 160 ? 0.25148 0.33187 0.24121 -0.05851 -0.02031 -0.00422 312 PHE   A CG   
1095 C  CD1  . PHE   A 160 ? 0.25608 0.34620 0.26164 -0.05709 -0.02220 -0.00219 312 PHE   A CD1  
1096 C  CD2  . PHE   A 160 ? 0.25283 0.32236 0.23745 -0.05731 -0.01599 -0.00798 312 PHE   A CD2  
1097 C  CE1  . PHE   A 160 ? 0.24727 0.33767 0.26224 -0.05461 -0.01919 -0.00512 312 PHE   A CE1  
1098 C  CE2  . PHE   A 160 ? 0.25287 0.32228 0.24603 -0.05554 -0.01342 -0.00926 312 PHE   A CE2  
1099 C  CZ   . PHE   A 160 ? 0.22681 0.30740 0.23457 -0.05426 -0.01471 -0.00844 312 PHE   A CZ   
1100 N  N    . GLN   A 161 ? 0.27155 0.33353 0.22883 -0.06955 -0.02216 -0.01698 313 GLN   A N    
1101 C  CA   . GLN   A 161 ? 0.27821 0.32806 0.23238 -0.07251 -0.02126 -0.02115 313 GLN   A CA   
1102 C  C    . GLN   A 161 ? 0.29407 0.34455 0.24701 -0.08043 -0.02577 -0.02325 313 GLN   A C    
1103 O  O    . GLN   A 161 ? 0.30994 0.35758 0.26669 -0.08498 -0.02589 -0.02262 313 GLN   A O    
1104 C  CB   . GLN   A 161 ? 0.26640 0.30337 0.21078 -0.06939 -0.01962 -0.02619 313 GLN   A CB   
1105 C  CG   . GLN   A 161 ? 0.26834 0.30419 0.21451 -0.06218 -0.01499 -0.02405 313 GLN   A CG   
1106 C  CD   . GLN   A 161 ? 0.25956 0.29288 0.21402 -0.06081 -0.01230 -0.02105 313 GLN   A CD   
1107 O  OE1  . GLN   A 161 ? 0.29094 0.31995 0.24663 -0.06508 -0.01310 -0.02152 313 GLN   A OE1  
1108 N  NE2  . GLN   A 161 ? 0.22689 0.26407 0.18724 -0.05545 -0.00947 -0.01771 313 GLN   A NE2  
1109 N  N    . VAL   A 162 ? 0.28423 0.33975 0.23190 -0.08285 -0.02983 -0.02526 314 VAL   A N    
1110 C  CA   . VAL   A 162 ? 0.27226 0.32828 0.21990 -0.08997 -0.03454 -0.02714 314 VAL   A CA   
1111 C  C    . VAL   A 162 ? 0.27127 0.33982 0.23160 -0.09253 -0.03471 -0.02147 314 VAL   A C    
1112 O  O    . VAL   A 162 ? 0.27727 0.34366 0.24181 -0.09682 -0.03498 -0.02059 314 VAL   A O    
1113 C  CB   . VAL   A 162 ? 0.26008 0.31956 0.19992 -0.08984 -0.03812 -0.03046 314 VAL   A CB   
1114 C  CG1  . VAL   A 162 ? 0.25220 0.31436 0.19569 -0.09513 -0.04258 -0.03047 314 VAL   A CG1  
1115 C  CG2  . VAL   A 162 ? 0.22888 0.27611 0.15736 -0.08684 -0.03753 -0.03856 314 VAL   A CG2  
1116 N  N    . GLY   A 163 ? 0.25778 0.34042 0.22557 -0.08962 -0.03475 -0.01735 315 GLY   A N    
1117 C  CA   . GLY   A 163 ? 0.21904 0.31485 0.20085 -0.09035 -0.03500 -0.01351 315 GLY   A CA   
1118 C  C    . GLY   A 163 ? 0.21713 0.31365 0.20665 -0.08989 -0.03035 -0.01308 315 GLY   A C    
1119 O  O    . GLY   A 163 ? 0.17998 0.28455 0.17765 -0.09211 -0.02961 -0.01186 315 GLY   A O    
1120 N  N    . LEU   A 164 ? 0.21087 0.29945 0.19761 -0.08584 -0.02651 -0.01386 316 LEU   A N    
1121 C  CA   . LEU   A 164 ? 0.22513 0.31456 0.21700 -0.08582 -0.02217 -0.01380 316 LEU   A CA   
1122 C  C    . LEU   A 164 ? 0.26684 0.34808 0.25250 -0.09291 -0.02245 -0.01386 316 LEU   A C    
1123 O  O    . LEU   A 164 ? 0.28022 0.36920 0.27148 -0.09569 -0.02049 -0.01187 316 LEU   A O    
1124 C  CB   . LEU   A 164 ? 0.21439 0.29485 0.20395 -0.07851 -0.01816 -0.01413 316 LEU   A CB   
1125 C  CG   . LEU   A 164 ? 0.22931 0.31214 0.22367 -0.07744 -0.01379 -0.01444 316 LEU   A CG   
1126 C  CD1  . LEU   A 164 ? 0.22570 0.32741 0.23479 -0.07614 -0.01287 -0.01499 316 LEU   A CD1  
1127 C  CD2  . LEU   A 164 ? 0.21743 0.29074 0.20941 -0.07020 -0.01092 -0.01485 316 LEU   A CD2  
1128 N  N    . LYS   A 165 ? 0.28857 0.35386 0.26316 -0.09487 -0.02492 -0.01596 317 LYS   A N    
1129 C  CA   . LYS   A 165 ? 0.31555 0.36981 0.28618 -0.10055 -0.02649 -0.01513 317 LYS   A CA   
1130 C  C    . LYS   A 165 ? 0.32720 0.39021 0.30311 -0.10597 -0.02881 -0.01263 317 LYS   A C    
1131 O  O    . LYS   A 165 ? 0.35949 0.42311 0.33760 -0.11113 -0.02848 -0.00897 317 LYS   A O    
1132 C  CB   . LYS   A 165 ? 0.32435 0.36033 0.28490 -0.10009 -0.02981 -0.01980 317 LYS   A CB   
1133 C  CG   . LYS   A 165 ? 0.34489 0.36492 0.30282 -0.10359 -0.03148 -0.01899 317 LYS   A CG   
1134 C  CD   . LYS   A 165 ? 0.34491 0.35803 0.30072 -0.10018 -0.02823 -0.01847 317 LYS   A CD   
1135 C  CE   . LYS   A 165 ? 0.36523 0.36218 0.31966 -0.10384 -0.03128 -0.01631 317 LYS   A CE   
1136 N  NZ   . LYS   A 165 ? 0.33996 0.33213 0.29341 -0.10157 -0.02850 -0.01405 317 LYS   A NZ   
1137 N  N    . LYS   A 166 ? 0.32012 0.39135 0.29827 -0.10518 -0.03136 -0.01383 318 LYS   A N    
1138 C  CA   . LYS   A 166 ? 0.32524 0.40548 0.30907 -0.11011 -0.03391 -0.01178 318 LYS   A CA   
1139 C  C    . LYS   A 166 ? 0.32273 0.42009 0.31731 -0.11048 -0.03007 -0.00826 318 LYS   A C    
1140 O  O    . LYS   A 166 ? 0.31776 0.42207 0.31669 -0.11576 -0.03114 -0.00581 318 LYS   A O    
1141 C  CB   . LYS   A 166 ? 0.34443 0.43081 0.32847 -0.10864 -0.03780 -0.01357 318 LYS   A CB   
1142 C  CG   . LYS   A 166 ? 0.38134 0.45394 0.35449 -0.10961 -0.04225 -0.01839 318 LYS   A CG   
1143 C  CD   . LYS   A 166 ? 0.39687 0.47882 0.36935 -0.10831 -0.04594 -0.01933 318 LYS   A CD   
1144 C  CE   . LYS   A 166 ? 0.43589 0.50708 0.39753 -0.10924 -0.05028 -0.02560 318 LYS   A CE   
1145 N  NZ   . LYS   A 166 ? 0.45637 0.53872 0.41593 -0.10813 -0.05376 -0.02575 318 LYS   A NZ   
1146 N  N    . LEU   A 167 ? 0.30807 0.41313 0.30753 -0.10485 -0.02572 -0.00865 319 LEU   A N    
1147 C  CA   . LEU   A 167 ? 0.28141 0.40360 0.29110 -0.10427 -0.02175 -0.00746 319 LEU   A CA   
1148 C  C    . LEU   A 167 ? 0.28689 0.40759 0.29276 -0.11021 -0.01943 -0.00433 319 LEU   A C    
1149 O  O    . LEU   A 167 ? 0.29823 0.43476 0.31061 -0.11212 -0.01680 -0.00297 319 LEU   A O    
1150 C  CB   . LEU   A 167 ? 0.24945 0.37916 0.26626 -0.09625 -0.01824 -0.01007 319 LEU   A CB   
1151 C  CG   . LEU   A 167 ? 0.24611 0.38203 0.27118 -0.09034 -0.02114 -0.01130 319 LEU   A CG   
1152 C  CD1  . LEU   A 167 ? 0.25142 0.39490 0.28691 -0.08258 -0.01829 -0.01381 319 LEU   A CD1  
1153 C  CD2  . LEU   A 167 ? 0.21758 0.36647 0.25171 -0.09199 -0.02410 -0.01032 319 LEU   A CD2  
1154 N  N    A ASN   A 168 ? 0.28908 0.39188 0.28497 -0.11317 -0.02082 -0.00298 320 ASN   A N    
1155 N  N    B ASN   A 168 ? 0.28853 0.39134 0.28441 -0.11313 -0.02079 -0.00298 320 ASN   A N    
1156 C  CA   A ASN   A 168 ? 0.30331 0.40253 0.29519 -0.11906 -0.01997 0.00169  320 ASN   A CA   
1157 C  CA   B ASN   A 168 ? 0.30329 0.40284 0.29531 -0.11916 -0.01999 0.00174  320 ASN   A CA   
1158 C  C    A ASN   A 168 ? 0.29981 0.41650 0.29609 -0.11727 -0.01411 0.00229  320 ASN   A C    
1159 C  C    B ASN   A 168 ? 0.30022 0.41686 0.29646 -0.11730 -0.01411 0.00232  320 ASN   A C    
1160 O  O    A ASN   A 168 ? 0.30872 0.43844 0.30720 -0.12213 -0.01265 0.00573  320 ASN   A O    
1161 O  O    B ASN   A 168 ? 0.30929 0.43885 0.30761 -0.12219 -0.01263 0.00581  320 ASN   A O    
1162 C  CB   A ASN   A 168 ? 0.32046 0.41882 0.31263 -0.12745 -0.02405 0.00592  320 ASN   A CB   
1163 C  CB   B ASN   A 168 ? 0.32013 0.41993 0.31292 -0.12743 -0.02394 0.00586  320 ASN   A CB   
1164 C  CG   A ASN   A 168 ? 0.33743 0.42404 0.32403 -0.13397 -0.02612 0.01178  320 ASN   A CG   
1165 C  CG   B ASN   A 168 ? 0.34206 0.42734 0.33194 -0.12866 -0.03003 0.00325  320 ASN   A CG   
1166 O  OD1  A ASN   A 168 ? 0.35090 0.42789 0.33252 -0.13199 -0.02502 0.01239  320 ASN   A OD1  
1167 O  OD1  B ASN   A 168 ? 0.36204 0.42826 0.34518 -0.12796 -0.03294 0.00127  320 ASN   A OD1  
1168 N  ND2  A ASN   A 168 ? 0.34914 0.43657 0.33744 -0.14193 -0.02975 0.01673  320 ASN   A ND2  
1169 N  ND2  B ASN   A 168 ? 0.35788 0.45297 0.35320 -0.13012 -0.03217 0.00243  320 ASN   A ND2  
1170 N  N    . LEU   A 169 ? 0.27076 0.38857 0.26844 -0.11005 -0.01091 -0.00175 321 LEU   A N    
1171 C  CA   . LEU   A 169 ? 0.25907 0.39322 0.26139 -0.10692 -0.00555 -0.00358 321 LEU   A CA   
1172 C  C    . LEU   A 169 ? 0.26596 0.39986 0.26084 -0.11310 -0.00439 0.00166  321 LEU   A C    
1173 O  O    . LEU   A 169 ? 0.26513 0.38115 0.25180 -0.11681 -0.00739 0.00584  321 LEU   A O    
1174 C  CB   . LEU   A 169 ? 0.23781 0.36929 0.24282 -0.09849 -0.00348 -0.00869 321 LEU   A CB   
1175 C  CG   . LEU   A 169 ? 0.23491 0.36817 0.24840 -0.09187 -0.00526 -0.01268 321 LEU   A CG   
1176 C  CD1  . LEU   A 169 ? 0.21924 0.35285 0.23783 -0.08394 -0.00324 -0.01701 321 LEU   A CD1  
1177 C  CD2  . LEU   A 169 ? 0.22041 0.37183 0.24515 -0.09100 -0.00513 -0.01416 321 LEU   A CD2  
1178 N  N    . HIS   A 170 ? 0.25525 0.40972 0.25342 -0.11413 -0.00059 0.00136  322 HIS   A N    
1179 C  CA   . HIS   A 170 ? 0.24696 0.40528 0.23804 -0.11807 0.00112  0.00525  322 HIS   A CA   
1180 C  C    . HIS   A 170 ? 0.27051 0.42146 0.25928 -0.11208 0.00308  0.00165  322 HIS   A C    
1181 O  O    . HIS   A 170 ? 0.28030 0.43273 0.27597 -0.10393 0.00494  -0.00550 322 HIS   A O    
1182 C  CB   . HIS   A 170 ? 0.21534 0.40048 0.21026 -0.11895 0.00522  0.00325  322 HIS   A CB   
1183 C  CG   . HIS   A 170 ? 0.23839 0.43334 0.23585 -0.12567 0.00361  0.00747  322 HIS   A CG   
1184 N  ND1  . HIS   A 170 ? 0.23962 0.45985 0.24071 -0.12741 0.00691  0.00594  322 HIS   A ND1  
1185 C  CD2  . HIS   A 170 ? 0.24317 0.42675 0.24050 -0.13109 -0.00115 0.01260  322 HIS   A CD2  
1186 C  CE1  . HIS   A 170 ? 0.24024 0.46442 0.24357 -0.13400 0.00446  0.01091  322 HIS   A CE1  
1187 N  NE2  . HIS   A 170 ? 0.25029 0.45207 0.25152 -0.13639 -0.00062 0.01499  322 HIS   A NE2  
1188 N  N    . GLU   A 171 ? 0.27502 0.41827 0.25505 -0.11626 0.00201  0.00717  323 GLU   A N    
1189 C  CA   . GLU   A 171 ? 0.30222 0.44081 0.28044 -0.11105 0.00403  0.00392  323 GLU   A CA   
1190 C  C    . GLU   A 171 ? 0.27865 0.43878 0.26398 -0.10424 0.00937  -0.00499 323 GLU   A C    
1191 O  O    . GLU   A 171 ? 0.26364 0.42112 0.25385 -0.09670 0.01106  -0.01142 323 GLU   A O    
1192 C  CB   . GLU   A 171 ? 0.35322 0.48390 0.32180 -0.11709 0.00162  0.01206  323 GLU   A CB   
1193 C  CG   . GLU   A 171 ? 0.40533 0.52637 0.37137 -0.11272 0.00245  0.01028  323 GLU   A CG   
1194 C  CD   . GLU   A 171 ? 0.45155 0.56088 0.40894 -0.11880 -0.00170 0.01985  323 GLU   A CD   
1195 O  OE1  . GLU   A 171 ? 0.47263 0.59134 0.42629 -0.12578 -0.00361 0.02675  323 GLU   A OE1  
1196 O  OE2  . GLU   A 171 ? 0.46621 0.55722 0.42137 -0.11658 -0.00366 0.02077  323 GLU   A OE2  
1197 N  N    . GLU   A 172 ? 0.25881 0.44046 0.24601 -0.10646 0.01155  -0.00623 324 GLU   A N    
1198 C  CA   . GLU   A 172 ? 0.25036 0.45254 0.24597 -0.09909 0.01596  -0.01686 324 GLU   A CA   
1199 C  C    . GLU   A 172 ? 0.22722 0.42666 0.23585 -0.08997 0.01627  -0.02457 324 GLU   A C    
1200 O  O    . GLU   A 172 ? 0.22006 0.42346 0.23636 -0.08153 0.01809  -0.03316 324 GLU   A O    
1201 C  CB   . GLU   A 172 ? 0.25309 0.47875 0.24947 -0.10323 0.01763  -0.01736 324 GLU   A CB   
1202 C  CG   . GLU   A 172 ? 0.28377 0.51849 0.26916 -0.11157 0.01698  -0.01070 324 GLU   A CG   
1203 C  CD   . GLU   A 172 ? 0.32867 0.54957 0.30574 -0.12200 0.01214  0.00298  324 GLU   A CD   
1204 O  OE1  . GLU   A 172 ? 0.35620 0.58723 0.32659 -0.12990 0.01059  0.00996  324 GLU   A OE1  
1205 O  OE2  . GLU   A 172 ? 0.33652 0.53682 0.31441 -0.12237 0.00918  0.00654  324 GLU   A OE2  
1206 N  N    . GLU   A 173 ? 0.20789 0.40049 0.21990 -0.09159 0.01353  -0.02139 325 GLU   A N    
1207 C  CA   . GLU   A 173 ? 0.17893 0.36945 0.20345 -0.08360 0.01235  -0.02697 325 GLU   A CA   
1208 C  C    . GLU   A 173 ? 0.16399 0.33570 0.18748 -0.07955 0.01032  -0.02695 325 GLU   A C    
1209 O  O    . GLU   A 173 ? 0.15393 0.32620 0.18821 -0.07125 0.00990  -0.03278 325 GLU   A O    
1210 C  CB   . GLU   A 173 ? 0.17983 0.36975 0.20730 -0.08720 0.00931  -0.02315 325 GLU   A CB   
1211 C  CG   . GLU   A 173 ? 0.17981 0.39167 0.21293 -0.08917 0.01146  -0.02500 325 GLU   A CG   
1212 C  CD   . GLU   A 173 ? 0.22767 0.43816 0.25752 -0.09757 0.00858  -0.01778 325 GLU   A CD   
1213 O  OE1  . GLU   A 173 ? 0.25874 0.48752 0.29362 -0.09978 0.01014  -0.01863 325 GLU   A OE1  
1214 O  OE2  . GLU   A 173 ? 0.24489 0.43658 0.26787 -0.10172 0.00457  -0.01205 325 GLU   A OE2  
1215 N  N    . HIS   A 174 ? 0.18287 0.33761 0.19433 -0.08529 0.00842  -0.02031 326 HIS   A N    
1216 C  CA   . HIS   A 174 ? 0.22066 0.35768 0.22983 -0.08215 0.00649  -0.02028 326 HIS   A CA   
1217 C  C    . HIS   A 174 ? 0.21030 0.34984 0.22308 -0.07487 0.00913  -0.02568 326 HIS   A C    
1218 O  O    . HIS   A 174 ? 0.17671 0.30725 0.19466 -0.06643 0.00797  -0.02862 326 HIS   A O    
1219 C  CB   . HIS   A 174 ? 0.25874 0.37741 0.25469 -0.08942 0.00381  -0.01309 326 HIS   A CB   
1220 C  CG   . HIS   A 174 ? 0.27856 0.37473 0.26883 -0.08337 0.00194  -0.01296 326 HIS   A CG   
1221 N  ND1  . HIS   A 174 ? 0.28033 0.36502 0.27004 -0.08042 -0.00092 -0.01342 326 HIS   A ND1  
1222 C  CD2  . HIS   A 174 ? 0.26533 0.35003 0.25003 -0.07998 0.00254  -0.01227 326 HIS   A CD2  
1223 C  CE1  . HIS   A 174 ? 0.27545 0.34390 0.25978 -0.07530 -0.00135 -0.01345 326 HIS   A CE1  
1224 N  NE2  . HIS   A 174 ? 0.28119 0.34867 0.26306 -0.07478 0.00056  -0.01271 326 HIS   A NE2  
1225 N  N    . VAL   A 175 ? 0.20460 0.35585 0.21407 -0.07792 0.01224  -0.02647 327 VAL   A N    
1226 C  CA   . VAL   A 175 ? 0.17269 0.32425 0.18421 -0.07064 0.01401  -0.03209 327 VAL   A CA   
1227 C  C    . VAL   A 175 ? 0.14838 0.31683 0.17625 -0.06274 0.01552  -0.04260 327 VAL   A C    
1228 O  O    . VAL   A 175 ? 0.17101 0.33344 0.20532 -0.05435 0.01476  -0.04784 327 VAL   A O    
1229 C  CB   . VAL   A 175 ? 0.18762 0.34620 0.18912 -0.07638 0.01613  -0.02950 327 VAL   A CB   
1230 C  CG1  . VAL   A 175 ? 0.17437 0.31283 0.16255 -0.08307 0.01298  -0.01884 327 VAL   A CG1  
1231 C  CG2  . VAL   A 175 ? 0.19502 0.37647 0.19578 -0.08047 0.01862  -0.03103 327 VAL   A CG2  
1232 N  N    . LEU   A 176 ? 0.14979 0.33305 0.18309 -0.06300 0.01651  -0.04516 328 LEU   A N    
1233 C  CA   . LEU   A 176 ? 0.16119 0.35513 0.21086 -0.05367 0.01649  -0.05507 328 LEU   A CA   
1234 C  C    . LEU   A 176 ? 0.16077 0.34208 0.22193 -0.04769 0.01211  -0.05458 328 LEU   A C    
1235 O  O    . LEU   A 176 ? 0.17462 0.35563 0.24914 -0.03897 0.01045  -0.06136 328 LEU   A O    
1236 C  CB   . LEU   A 176 ? 0.16550 0.37662 0.21865 -0.05537 0.01791  -0.05713 328 LEU   A CB   
1237 C  CG   . LEU   A 176 ? 0.19677 0.42749 0.24470 -0.05746 0.02177  -0.06246 328 LEU   A CG   
1238 C  CD1  . LEU   A 176 ? 0.18073 0.42646 0.22856 -0.06245 0.02279  -0.06058 328 LEU   A CD1  
1239 C  CD2  . LEU   A 176 ? 0.18957 0.42939 0.24862 -0.04764 0.02253  -0.07617 328 LEU   A CD2  
1240 N  N    . LEU   A 177 ? 0.15620 0.32686 0.21230 -0.05252 0.00939  -0.04644 329 LEU   A N    
1241 C  CA   . LEU   A 177 ? 0.15747 0.31637 0.22121 -0.04767 0.00473  -0.04429 329 LEU   A CA   
1242 C  C    . LEU   A 177 ? 0.16756 0.30867 0.22802 -0.04227 0.00377  -0.04332 329 LEU   A C    
1243 O  O    . LEU   A 177 ? 0.16082 0.29768 0.23347 -0.03513 0.00058  -0.04486 329 LEU   A O    
1244 C  CB   . LEU   A 177 ? 0.16436 0.31406 0.21850 -0.05411 0.00219  -0.03611 329 LEU   A CB   
1245 C  CG   . LEU   A 177 ? 0.16432 0.30545 0.22407 -0.05026 -0.00284 -0.03256 329 LEU   A CG   
1246 C  CD1  . LEU   A 177 ? 0.14461 0.30127 0.22513 -0.04497 -0.00546 -0.03696 329 LEU   A CD1  
1247 C  CD2  . LEU   A 177 ? 0.17625 0.30971 0.22376 -0.05749 -0.00500 -0.02621 329 LEU   A CD2  
1248 N  N    A MET   A 178 ? 0.17424 0.30479 0.21941 -0.04595 0.00582  -0.03988 330 MET   A N    
1249 N  N    B MET   A 178 ? 0.17424 0.30520 0.21975 -0.04580 0.00588  -0.04014 330 MET   A N    
1250 C  CA   A MET   A 178 ? 0.17839 0.29482 0.22117 -0.04109 0.00537  -0.03952 330 MET   A CA   
1251 C  CA   B MET   A 178 ? 0.17797 0.29425 0.22140 -0.04080 0.00519  -0.03952 330 MET   A CA   
1252 C  C    A MET   A 178 ? 0.17058 0.29575 0.22799 -0.03388 0.00535  -0.04818 330 MET   A C    
1253 C  C    B MET   A 178 ? 0.17091 0.29568 0.22796 -0.03385 0.00540  -0.04817 330 MET   A C    
1254 O  O    A MET   A 178 ? 0.17850 0.29520 0.24520 -0.02771 0.00234  -0.04849 330 MET   A O    
1255 O  O    B MET   A 178 ? 0.17944 0.29522 0.24482 -0.02778 0.00263  -0.04852 330 MET   A O    
1256 C  CB   A MET   A 178 ? 0.18894 0.29738 0.21576 -0.04595 0.00750  -0.03602 330 MET   A CB   
1257 C  CB   B MET   A 178 ? 0.19004 0.29596 0.21683 -0.04563 0.00698  -0.03516 330 MET   A CB   
1258 C  CG   A MET   A 178 ? 0.21539 0.31066 0.22898 -0.05195 0.00634  -0.02848 330 MET   A CG   
1259 C  CG   B MET   A 178 ? 0.20937 0.30350 0.22468 -0.05120 0.00555  -0.02810 330 MET   A CG   
1260 S  SD   A MET   A 178 ? 0.23322 0.32431 0.23228 -0.05922 0.00764  -0.02430 330 MET   A SD   
1261 S  SD   B MET   A 178 ? 0.24165 0.31922 0.24161 -0.05432 0.00581  -0.02331 330 MET   A SD   
1262 C  CE   A MET   A 178 ? 0.22944 0.31181 0.22824 -0.05247 0.00808  -0.02620 330 MET   A CE   
1263 C  CE   B MET   A 178 ? 0.23621 0.32740 0.23099 -0.06250 0.00779  -0.02246 330 MET   A CE   
1264 N  N    . ALA   A 179 ? 0.15007 0.29337 0.21028 -0.03492 0.00840  -0.05554 331 ALA   A N    
1265 C  CA   . ALA   A 179 ? 0.16142 0.31428 0.23505 -0.02793 0.00839  -0.06637 331 ALA   A CA   
1266 C  C    . ALA   A 179 ? 0.16123 0.31831 0.25662 -0.02064 0.00439  -0.07163 331 ALA   A C    
1267 O  O    . ALA   A 179 ? 0.15460 0.30630 0.26308 -0.01350 0.00106  -0.07653 331 ALA   A O    
1268 C  CB   . ALA   A 179 ? 0.16427 0.33931 0.23436 -0.03136 0.01308  -0.07364 331 ALA   A CB   
1269 N  N    . ILE   A 180 ? 0.13390 0.29923 0.23400 -0.02236 0.00378  -0.06995 332 ILE   A N    
1270 C  CA   . ILE   A 180 ? 0.14351 0.30834 0.26229 -0.01517 -0.00113 -0.07218 332 ILE   A CA   
1271 C  C    . ILE   A 180 ? 0.16892 0.31742 0.29416 -0.01288 -0.00686 -0.06479 332 ILE   A C    
1272 O  O    . ILE   A 180 ? 0.19928 0.34228 0.34114 -0.00568 -0.01190 -0.06698 332 ILE   A O    
1273 C  CB   . ILE   A 180 ? 0.15501 0.33019 0.27470 -0.01826 -0.00086 -0.06976 332 ILE   A CB   
1274 C  CG1  . ILE   A 180 ? 0.14079 0.33380 0.25765 -0.01901 0.00425  -0.07815 332 ILE   A CG1  
1275 C  CG2  . ILE   A 180 ? 0.16213 0.33485 0.30053 -0.01203 -0.00721 -0.06881 332 ILE   A CG2  
1276 C  CD1  . ILE   A 180 ? 0.10110 0.30532 0.21290 -0.02546 0.00608  -0.07384 332 ILE   A CD1  
1277 N  N    . CYS   A 181 ? 0.17790 0.31270 0.28506 -0.01860 -0.00608 -0.05398 333 CYS   A N    
1278 C  CA   . CYS   A 181 ? 0.21280 0.33046 0.31959 -0.01694 -0.01019 -0.04523 333 CYS   A CA   
1279 C  C    . CYS   A 181 ? 0.22845 0.33798 0.34237 -0.01169 -0.01157 -0.04823 333 CYS   A C    
1280 O  O    . CYS   A 181 ? 0.24049 0.34287 0.36783 -0.00758 -0.01706 -0.04472 333 CYS   A O    
1281 C  CB   . CYS   A 181 ? 0.20765 0.31430 0.29257 -0.02349 -0.00788 -0.03632 333 CYS   A CB   
1282 S  SG   . CYS   A 181 ? 0.20235 0.29292 0.28439 -0.02232 -0.01152 -0.02586 333 CYS   A SG   
1283 N  N    . ILE   A 182 ? 0.22974 0.34080 0.33558 -0.01233 -0.00737 -0.05401 334 ILE   A N    
1284 C  CA   . ILE   A 182 ? 0.22485 0.32804 0.33611 -0.00812 -0.00888 -0.05687 334 ILE   A CA   
1285 C  C    . ILE   A 182 ? 0.22653 0.33652 0.36221 -0.00073 -0.01337 -0.06703 334 ILE   A C    
1286 O  O    . ILE   A 182 ? 0.21650 0.31665 0.36573 0.00343  -0.01880 -0.06538 334 ILE   A O    
1287 C  CB   . ILE   A 182 ? 0.21907 0.32348 0.31466 -0.01120 -0.00384 -0.06010 334 ILE   A CB   
1288 C  CG1  . ILE   A 182 ? 0.19213 0.28490 0.26749 -0.01699 -0.00140 -0.04966 334 ILE   A CG1  
1289 C  CG2  . ILE   A 182 ? 0.23038 0.33080 0.33385 -0.00657 -0.00573 -0.06591 334 ILE   A CG2  
1290 C  CD1  . ILE   A 182 ? 0.15266 0.24767 0.21186 -0.02158 0.00282  -0.05064 334 ILE   A CD1  
1291 N  N    . VAL   A 183 ? 0.21004 0.33700 0.35246 0.00097  -0.01153 -0.07766 335 VAL   A N    
1292 C  CA   . VAL   A 183 ? 0.22863 0.35609 0.38711 0.00871  -0.01493 -0.08796 335 VAL   A CA   
1293 C  C    . VAL   A 183 ? 0.24409 0.36961 0.41722 0.01198  -0.02018 -0.08457 335 VAL   A C    
1294 O  O    . VAL   A 183 ? 0.26506 0.40215 0.44253 0.01373  -0.01902 -0.09125 335 VAL   A O    
1295 C  CB   . VAL   A 183 ? 0.26027 0.40424 0.41318 0.00914  -0.00971 -0.10147 335 VAL   A CB   
1296 C  CG1  . VAL   A 183 ? 0.28744 0.43045 0.45596 0.01670  -0.01388 -0.11467 335 VAL   A CG1  
1297 C  CG2  . VAL   A 183 ? 0.24817 0.39601 0.38416 0.00412  -0.00464 -0.10183 335 VAL   A CG2  
1298 N  N    . SER   A 184 ? 0.25486 0.36683 0.43568 0.01241  -0.02624 -0.07352 336 SER   A N    
1299 C  CA   . SER   A 184 ? 0.25460 0.36397 0.44921 0.01484  -0.03242 -0.06789 336 SER   A CA   
1300 C  C    . SER   A 184 ? 0.24230 0.33905 0.45564 0.02099  -0.03983 -0.07043 336 SER   A C    
1301 O  O    . SER   A 184 ? 0.23803 0.32196 0.45299 0.02064  -0.04276 -0.06532 336 SER   A O    
1302 C  CB   . SER   A 184 ? 0.28653 0.39159 0.47533 0.00943  -0.03468 -0.05229 336 SER   A CB   
1303 O  OG   . SER   A 184 ? 0.28771 0.40356 0.46110 0.00311  -0.02911 -0.05099 336 SER   A OG   
1304 N  N    . PRO   A 185 ? 0.24465 0.34401 0.47321 0.02606  -0.04356 -0.07788 337 PRO   A N    
1305 C  CA   . PRO   A 185 ? 0.25066 0.33675 0.49810 0.03103  -0.05135 -0.08227 337 PRO   A CA   
1306 C  C    . PRO   A 185 ? 0.28340 0.35446 0.54122 0.02978  -0.05981 -0.06652 337 PRO   A C    
1307 O  O    . PRO   A 185 ? 0.31990 0.37725 0.59182 0.03157  -0.06658 -0.06719 337 PRO   A O    
1308 C  CB   . PRO   A 185 ? 0.26472 0.36065 0.52464 0.03619  -0.05240 -0.09610 337 PRO   A CB   
1309 C  CG   . PRO   A 185 ? 0.25474 0.36539 0.50651 0.03366  -0.04802 -0.09101 337 PRO   A CG   
1310 C  CD   . PRO   A 185 ? 0.23438 0.34964 0.46404 0.02707  -0.04073 -0.08419 337 PRO   A CD   
1311 N  N    . ASP   A 186 ? 0.26891 0.34269 0.52021 0.02578  -0.06016 -0.05225 338 ASP   A N    
1312 C  CA   . ASP   A 186 ? 0.29513 0.35728 0.55511 0.02373  -0.06835 -0.03640 338 ASP   A CA   
1313 C  C    . ASP   A 186 ? 0.29808 0.35206 0.54804 0.01849  -0.06806 -0.02372 338 ASP   A C    
1314 O  O    . ASP   A 186 ? 0.32328 0.37063 0.57646 0.01501  -0.07376 -0.00826 338 ASP   A O    
1315 C  CB   . ASP   A 186 ? 0.28318 0.35392 0.54192 0.02175  -0.07013 -0.02733 338 ASP   A CB   
1316 C  CG   . ASP   A 186 ? 0.29954 0.38250 0.53765 0.01633  -0.06303 -0.02350 338 ASP   A CG   
1317 O  OD1  . ASP   A 186 ? 0.31808 0.40352 0.55080 0.01179  -0.06559 -0.01063 338 ASP   A OD1  
1318 O  OD2  . ASP   A 186 ? 0.30934 0.39935 0.53655 0.01588  -0.05537 -0.03342 338 ASP   A OD2  
1319 N  N    . ARG   A 187 ? 0.29800 0.35356 0.53585 0.01746  -0.06162 -0.02941 339 ARG   A N    
1320 C  CA   . ARG   A 187 ? 0.31763 0.36656 0.54705 0.01281  -0.06115 -0.01816 339 ARG   A CA   
1321 C  C    . ARG   A 187 ? 0.36390 0.39750 0.60894 0.01321  -0.06890 -0.01245 339 ARG   A C    
1322 O  O    . ARG   A 187 ? 0.35616 0.38344 0.61527 0.01740  -0.07228 -0.02367 339 ARG   A O    
1323 C  CB   . ARG   A 187 ? 0.28894 0.34207 0.50452 0.01205  -0.05334 -0.02666 339 ARG   A CB   
1324 C  CG   . ARG   A 187 ? 0.28110 0.34850 0.48103 0.00962  -0.04579 -0.03156 339 ARG   A CG   
1325 C  CD   . ARG   A 187 ? 0.25375 0.32490 0.44277 0.00333  -0.04525 -0.01830 339 ARG   A CD   
1326 N  NE   . ARG   A 187 ? 0.22907 0.30612 0.39437 -0.00053 -0.03625 -0.02261 339 ARG   A NE   
1327 C  CZ   . ARG   A 187 ? 0.21442 0.29234 0.36153 -0.00604 -0.03326 -0.01466 339 ARG   A CZ   
1328 N  NH1  . ARG   A 187 ? 0.17149 0.24698 0.31925 -0.00847 -0.03777 -0.00209 339 ARG   A NH1  
1329 N  NH2  . ARG   A 187 ? 0.22112 0.30297 0.34966 -0.00953 -0.02629 -0.01923 339 ARG   A NH2  
1330 N  N    . PRO   A 188 ? 0.41668 0.44509 0.66006 0.00800  -0.07210 0.00461  340 PRO   A N    
1331 C  CA   . PRO   A 188 ? 0.43166 0.44621 0.69090 0.00647  -0.07982 0.01179  340 PRO   A CA   
1332 C  C    . PRO   A 188 ? 0.44174 0.44978 0.70331 0.00794  -0.07828 0.00220  340 PRO   A C    
1333 O  O    . PRO   A 188 ? 0.45193 0.46512 0.69869 0.00733  -0.07128 -0.00058 340 PRO   A O    
1334 C  CB   . PRO   A 188 ? 0.44225 0.45817 0.69397 -0.00070 -0.08118 0.03277  340 PRO   A CB   
1335 C  CG   . PRO   A 188 ? 0.44317 0.47205 0.67276 -0.00241 -0.07254 0.03256  340 PRO   A CG   
1336 C  CD   . PRO   A 188 ? 0.43419 0.47067 0.66141 0.00224  -0.06904 0.01805  340 PRO   A CD   
1337 N  N    . GLY   A 189 ? 0.44555 0.44265 0.72691 0.00930  -0.08560 -0.00336 341 GLY   A N    
1338 C  CA   . GLY   A 189 ? 0.44164 0.43258 0.72807 0.01013  -0.08603 -0.01327 341 GLY   A CA   
1339 C  C    . GLY   A 189 ? 0.41633 0.41242 0.70265 0.01624  -0.08280 -0.03567 341 GLY   A C    
1340 O  O    . GLY   A 189 ? 0.41309 0.40524 0.70530 0.01684  -0.08448 -0.04577 341 GLY   A O    
1341 N  N    . VAL   A 190 ? 0.39152 0.39843 0.67129 0.02006  -0.07834 -0.04367 342 VAL   A N    
1342 C  CA   . VAL   A 190 ? 0.38913 0.40435 0.66835 0.02505  -0.07493 -0.06468 342 VAL   A CA   
1343 C  C    . VAL   A 190 ? 0.42208 0.43024 0.72492 0.02727  -0.08429 -0.07603 342 VAL   A C    
1344 O  O    . VAL   A 190 ? 0.42504 0.42596 0.74500 0.02671  -0.09243 -0.06990 342 VAL   A O    
1345 C  CB   . VAL   A 190 ? 0.37037 0.40031 0.64009 0.02752  -0.06888 -0.06921 342 VAL   A CB   
1346 C  CG1  . VAL   A 190 ? 0.36630 0.40675 0.63875 0.03221  -0.06658 -0.09067 342 VAL   A CG1  
1347 C  CG2  . VAL   A 190 ? 0.34490 0.38415 0.59210 0.02409  -0.06010 -0.06136 342 VAL   A CG2  
1348 N  N    . GLN   A 191 ? 0.43818 0.45004 0.74302 0.02917  -0.08404 -0.09276 343 GLN   A N    
1349 C  CA   . GLN   A 191 ? 0.47514 0.48458 0.80359 0.03088  -0.09374 -0.10608 343 GLN   A CA   
1350 C  C    . GLN   A 191 ? 0.45796 0.48146 0.78967 0.03649  -0.09217 -0.12470 343 GLN   A C    
1351 O  O    . GLN   A 191 ? 0.46106 0.48267 0.81065 0.03885  -0.09885 -0.12746 343 GLN   A O    
1352 C  CB   . GLN   A 191 ? 0.51927 0.52849 0.84937 0.02971  -0.09560 -0.11172 343 GLN   A CB   
1353 C  CG   . GLN   A 191 ? 0.56047 0.56696 0.91484 0.03160  -0.10623 -0.11764 343 GLN   A CG   
1354 C  CD   . GLN   A 191 ? 0.60342 0.62511 0.96289 0.03726  -0.10636 -0.14044 343 GLN   A CD   
1355 O  OE1  . GLN   A 191 ? 0.63808 0.66415 1.01325 0.04064  -0.11136 -0.15155 343 GLN   A OE1  
1356 N  NE2  . GLN   A 191 ? 0.60321 0.63437 0.95030 0.03830  -0.10117 -0.14742 343 GLN   A NE2  
1357 N  N    . ASP   A 192 ? 0.43958 0.47857 0.75458 0.03827  -0.08352 -0.13696 344 ASP   A N    
1358 C  CA   . ASP   A 192 ? 0.43804 0.49433 0.75468 0.04272  -0.08118 -0.15464 344 ASP   A CA   
1359 C  C    . ASP   A 192 ? 0.41760 0.48221 0.72035 0.04356  -0.07302 -0.14820 344 ASP   A C    
1360 O  O    . ASP   A 192 ? 0.39687 0.47755 0.68146 0.04325  -0.06371 -0.15334 344 ASP   A O    
1361 C  CB   . ASP   A 192 ? 0.44472 0.51746 0.75200 0.04294  -0.07707 -0.17053 344 ASP   A CB   
1362 C  CG   . ASP   A 192 ? 0.47041 0.56274 0.78531 0.04719  -0.07748 -0.19043 344 ASP   A CG   
1363 O  OD1  . ASP   A 192 ? 0.48027 0.58987 0.79066 0.04743  -0.07551 -0.20394 344 ASP   A OD1  
1364 O  OD2  . ASP   A 192 ? 0.48261 0.57490 0.80861 0.05033  -0.07990 -0.19211 344 ASP   A OD2  
1365 N  N    . ALA   A 193 ? 0.42046 0.47552 0.73346 0.04390  -0.07754 -0.13607 345 ALA   A N    
1366 C  CA   . ALA   A 193 ? 0.41815 0.48200 0.72099 0.04415  -0.07157 -0.12821 345 ALA   A CA   
1367 C  C    . ALA   A 193 ? 0.42697 0.51040 0.73006 0.04803  -0.06749 -0.14466 345 ALA   A C    
1368 O  O    . ALA   A 193 ? 0.42477 0.52163 0.71380 0.04699  -0.05968 -0.14161 345 ALA   A O    
1369 C  CB   . ALA   A 193 ? 0.41573 0.46730 0.73181 0.04356  -0.07896 -0.11250 345 ALA   A CB   
1370 N  N    A LYS   A 194 ? 0.44031 0.52723 0.76017 0.05191  -0.07312 -0.16202 346 LYS   A N    
1371 N  N    B LYS   A 194 ? 0.44019 0.52732 0.75976 0.05188  -0.07299 -0.16215 346 LYS   A N    
1372 C  CA   A LYS   A 194 ? 0.44892 0.55723 0.76922 0.05544  -0.06921 -0.17886 346 LYS   A CA   
1373 C  CA   B LYS   A 194 ? 0.44868 0.55717 0.76863 0.05540  -0.06902 -0.17859 346 LYS   A CA   
1374 C  C    A LYS   A 194 ? 0.43190 0.55874 0.72842 0.05253  -0.05850 -0.18508 346 LYS   A C    
1375 C  C    B LYS   A 194 ? 0.43211 0.55933 0.72881 0.05260  -0.05853 -0.18558 346 LYS   A C    
1376 O  O    A LYS   A 194 ? 0.42563 0.57062 0.71178 0.05216  -0.05118 -0.18787 346 LYS   A O    
1377 O  O    B LYS   A 194 ? 0.42666 0.57261 0.71351 0.05240  -0.05135 -0.18938 346 LYS   A O    
1378 C  CB   A LYS   A 194 ? 0.47468 0.58452 0.81871 0.05992  -0.07833 -0.19713 346 LYS   A CB   
1379 C  CB   B LYS   A 194 ? 0.47490 0.58475 0.81930 0.06009  -0.07828 -0.19645 346 LYS   A CB   
1380 C  CG   A LYS   A 194 ? 0.48676 0.62193 0.83155 0.06353  -0.07448 -0.21686 346 LYS   A CG   
1381 C  CG   B LYS   A 194 ? 0.49079 0.59331 0.85827 0.06411  -0.08647 -0.19450 346 LYS   A CG   
1382 C  CD   A LYS   A 194 ? 0.51043 0.64835 0.88043 0.06814  -0.08447 -0.23576 346 LYS   A CD   
1383 C  CD   B LYS   A 194 ? 0.51649 0.62427 0.90865 0.06918  -0.09518 -0.21495 346 LYS   A CD   
1384 C  CE   A LYS   A 194 ? 0.52663 0.68693 0.90460 0.07316  -0.08283 -0.25264 346 LYS   A CE   
1385 C  CE   B LYS   A 194 ? 0.53299 0.62028 0.94648 0.06819  -0.10785 -0.21215 346 LYS   A CE   
1386 N  NZ   A LYS   A 194 ? 0.56449 0.72525 0.97197 0.07865  -0.09431 -0.26993 346 LYS   A NZ   
1387 N  NZ   B LYS   A 194 ? 0.55167 0.63276 0.99561 0.07265  -0.11948 -0.21737 346 LYS   A NZ   
1388 N  N    . LEU   A 195 ? 0.41664 0.54002 0.70477 0.04976  -0.05789 -0.18638 347 LEU   A N    
1389 C  CA   . LEU   A 195 ? 0.37907 0.52005 0.64491 0.04622  -0.04866 -0.19090 347 LEU   A CA   
1390 C  C    . LEU   A 195 ? 0.34169 0.48172 0.58677 0.04164  -0.04028 -0.17419 347 LEU   A C    
1391 O  O    . LEU   A 195 ? 0.32434 0.48248 0.55270 0.03847  -0.03205 -0.17586 347 LEU   A O    
1392 C  CB   . LEU   A 195 ? 0.37023 0.50909 0.63540 0.04474  -0.05155 -0.19684 347 LEU   A CB   
1393 C  CG   . LEU   A 195 ? 0.36769 0.52145 0.60990 0.04009  -0.04334 -0.19754 347 LEU   A CG   
1394 C  CD1  . LEU   A 195 ? 0.37574 0.55771 0.60906 0.03927  -0.03727 -0.20884 347 LEU   A CD1  
1395 C  CD2  . LEU   A 195 ? 0.36996 0.52223 0.61679 0.03950  -0.04810 -0.20285 347 LEU   A CD2  
1396 N  N    . VAL   A 196 ? 0.33411 0.45484 0.58066 0.04046  -0.04284 -0.15754 348 VAL   A N    
1397 C  CA   . VAL   A 196 ? 0.29197 0.41357 0.52159 0.03593  -0.03627 -0.14191 348 VAL   A CA   
1398 C  C    . VAL   A 196 ? 0.27359 0.40883 0.50199 0.03580  -0.03282 -0.14066 348 VAL   A C    
1399 O  O    . VAL   A 196 ? 0.24119 0.38923 0.45279 0.03111  -0.02525 -0.13675 348 VAL   A O    
1400 C  CB   . VAL   A 196 ? 0.27916 0.38024 0.51294 0.03453  -0.04110 -0.12457 348 VAL   A CB   
1401 C  CG1  . VAL   A 196 ? 0.27121 0.37544 0.48898 0.02929  -0.03559 -0.10955 348 VAL   A CG1  
1402 C  CG2  . VAL   A 196 ? 0.25421 0.34303 0.48900 0.03398  -0.04410 -0.12522 348 VAL   A CG2  
1403 N  N    . GLU   A 197 ? 0.28568 0.41876 0.53274 0.04043  -0.03881 -0.14397 349 GLU   A N    
1404 C  CA   . GLU   A 197 ? 0.31575 0.46248 0.56395 0.04070  -0.03622 -0.14308 349 GLU   A CA   
1405 C  C    . GLU   A 197 ? 0.29833 0.46891 0.53689 0.03974  -0.02892 -0.15691 349 GLU   A C    
1406 O  O    . GLU   A 197 ? 0.29152 0.47609 0.51890 0.03573  -0.02274 -0.15230 349 GLU   A O    
1407 C  CB   . GLU   A 197 ? 0.37794 0.51754 0.64998 0.04633  -0.04497 -0.14465 349 GLU   A CB   
1408 C  CG   . GLU   A 197 ? 0.43071 0.58501 0.70629 0.04715  -0.04306 -0.14384 349 GLU   A CG   
1409 C  CD   . GLU   A 197 ? 0.48852 0.63278 0.78648 0.05161  -0.05252 -0.13923 349 GLU   A CD   
1410 O  OE1  . GLU   A 197 ? 0.52955 0.66136 0.84502 0.05580  -0.06052 -0.14579 349 GLU   A OE1  
1411 O  OE2  . GLU   A 197 ? 0.48323 0.63255 0.78180 0.05030  -0.05262 -0.12896 349 GLU   A OE2  
1412 N  N    . ALA   A 198 ? 0.31025 0.48708 0.55278 0.04234  -0.03009 -0.17340 350 ALA   A N    
1413 C  CA   . ALA   A 198 ? 0.30792 0.51031 0.54072 0.04059  -0.02378 -0.18621 350 ALA   A CA   
1414 C  C    . ALA   A 198 ? 0.29266 0.50432 0.49991 0.03263  -0.01509 -0.17834 350 ALA   A C    
1415 O  O    . ALA   A 198 ? 0.30314 0.53466 0.49944 0.02849  -0.00883 -0.17908 350 ALA   A O    
1416 C  CB   . ALA   A 198 ? 0.31068 0.51922 0.55274 0.04406  -0.02806 -0.20479 350 ALA   A CB   
1417 N  N    . ILE   A 199 ? 0.27178 0.46962 0.46992 0.02993  -0.01502 -0.17037 351 ILE   A N    
1418 C  CA   . ILE   A 199 ? 0.25456 0.45932 0.42973 0.02215  -0.00766 -0.16183 351 ILE   A CA   
1419 C  C    . ILE   A 199 ? 0.23623 0.44042 0.40465 0.01772  -0.00426 -0.14709 351 ILE   A C    
1420 O  O    . ILE   A 199 ? 0.22367 0.44263 0.37694 0.01105  0.00187  -0.14366 351 ILE   A O    
1421 C  CB   . ILE   A 199 ? 0.25772 0.44751 0.42693 0.02091  -0.00892 -0.15693 351 ILE   A CB   
1422 C  CG1  . ILE   A 199 ? 0.26212 0.45582 0.43728 0.02381  -0.01268 -0.17175 351 ILE   A CG1  
1423 C  CG2  . ILE   A 199 ? 0.25585 0.45097 0.40291 0.01275  -0.00203 -0.14655 351 ILE   A CG2  
1424 C  CD1  . ILE   A 199 ? 0.25920 0.43294 0.43852 0.02523  -0.01732 -0.16796 351 ILE   A CD1  
1425 N  N    . GLN   A 200 ? 0.24245 0.43004 0.42193 0.02029  -0.00912 -0.13723 352 GLN   A N    
1426 C  CA   . GLN   A 200 ? 0.22737 0.41571 0.40161 0.01555  -0.00739 -0.12380 352 GLN   A CA   
1427 C  C    . GLN   A 200 ? 0.24259 0.44969 0.41903 0.01494  -0.00468 -0.12848 352 GLN   A C    
1428 O  O    . GLN   A 200 ? 0.24754 0.46405 0.41154 0.00790  -0.00008 -0.12126 352 GLN   A O    
1429 C  CB   . GLN   A 200 ? 0.23995 0.41033 0.42697 0.01832  -0.01449 -0.11304 352 GLN   A CB   
1430 C  CG   . GLN   A 200 ? 0.24319 0.41393 0.42216 0.01196  -0.01353 -0.09872 352 GLN   A CG   
1431 C  CD   . GLN   A 200 ? 0.25502 0.41271 0.44670 0.01416  -0.02128 -0.08818 352 GLN   A CD   
1432 O  OE1  . GLN   A 200 ? 0.27429 0.43211 0.48268 0.01951  -0.02630 -0.09072 352 GLN   A OE1  
1433 N  NE2  . GLN   A 200 ? 0.23816 0.38529 0.42170 0.00960  -0.02262 -0.07609 352 GLN   A NE2  
1434 N  N    . ASP   A 201 ? 0.25669 0.46938 0.44952 0.02190  -0.00793 -0.14077 353 ASP   A N    
1435 C  CA   . ASP   A 201 ? 0.28830 0.51989 0.48564 0.02204  -0.00571 -0.14575 353 ASP   A CA   
1436 C  C    . ASP   A 201 ? 0.26884 0.52170 0.44778 0.01506  0.00222  -0.14948 353 ASP   A C    
1437 O  O    . ASP   A 201 ? 0.25263 0.51879 0.42605 0.01003  0.00590  -0.14460 353 ASP   A O    
1438 C  CB   . ASP   A 201 ? 0.33770 0.57190 0.55641 0.03097  -0.01095 -0.16037 353 ASP   A CB   
1439 C  CG   . ASP   A 201 ? 0.39343 0.61153 0.63193 0.03638  -0.01913 -0.15366 353 ASP   A CG   
1440 O  OD1  . ASP   A 201 ? 0.40175 0.60894 0.63639 0.03291  -0.02055 -0.13765 353 ASP   A OD1  
1441 O  OD2  . ASP   A 201 ? 0.42692 0.64398 0.68490 0.04355  -0.02479 -0.16421 353 ASP   A OD2  
1442 N  N    . ARG   A 202 ? 0.27559 0.53231 0.44492 0.01388  0.00420  -0.15708 354 ARG   A N    
1443 C  CA   . ARG   A 202 ? 0.30448 0.58146 0.45498 0.00592  0.01066  -0.15812 354 ARG   A CA   
1444 C  C    . ARG   A 202 ? 0.26744 0.54095 0.40090 -0.00359 0.01458  -0.14124 354 ARG   A C    
1445 O  O    . ARG   A 202 ? 0.27010 0.56005 0.39244 -0.01094 0.01889  -0.13772 354 ARG   A O    
1446 C  CB   . ARG   A 202 ? 0.35847 0.63844 0.50193 0.00571  0.01051  -0.16675 354 ARG   A CB   
1447 C  CG   . ARG   A 202 ? 0.42343 0.72886 0.55125 -0.00180 0.01527  -0.16996 354 ARG   A CG   
1448 C  CD   . ARG   A 202 ? 0.48596 0.79984 0.61369 -0.00021 0.01313  -0.18221 354 ARG   A CD   
1449 N  NE   . ARG   A 202 ? 0.54440 0.85253 0.69327 0.00987  0.00709  -0.19702 354 ARG   A NE   
1450 C  CZ   . ARG   A 202 ? 0.59961 0.89535 0.75489 0.01377  0.00226  -0.20229 354 ARG   A CZ   
1451 N  NH1  . ARG   A 202 ? 0.63365 0.92397 0.80971 0.02212  -0.00427 -0.21533 354 ARG   A NH1  
1452 N  NH2  . ARG   A 202 ? 0.62563 0.91429 0.76773 0.00905  0.00341  -0.19415 354 ARG   A NH2  
1453 N  N    . LEU   A 203 ? 0.24274 0.49507 0.37449 -0.00408 0.01247  -0.13054 355 LEU   A N    
1454 C  CA   . LEU   A 203 ? 0.21080 0.45802 0.32750 -0.01318 0.01501  -0.11543 355 LEU   A CA   
1455 C  C    . LEU   A 203 ? 0.19449 0.44337 0.31692 -0.01508 0.01400  -0.10812 355 LEU   A C    
1456 O  O    . LEU   A 203 ? 0.18083 0.43603 0.29097 -0.02384 0.01694  -0.09991 355 LEU   A O    
1457 C  CB   . LEU   A 203 ? 0.19069 0.41639 0.30446 -0.01310 0.01260  -0.10754 355 LEU   A CB   
1458 C  CG   . LEU   A 203 ? 0.20668 0.42851 0.31489 -0.01174 0.01306  -0.11281 355 LEU   A CG   
1459 C  CD1  . LEU   A 203 ? 0.19731 0.39748 0.30944 -0.00930 0.00930  -0.10611 355 LEU   A CD1  
1460 C  CD2  . LEU   A 203 ? 0.20458 0.43705 0.29225 -0.02097 0.01792  -0.10919 355 LEU   A CD2  
1461 N  N    . SER   A 204 ? 0.22248 0.46518 0.36391 -0.00740 0.00897  -0.11032 356 SER   A N    
1462 C  CA   . SER   A 204 ? 0.24192 0.48728 0.39055 -0.00881 0.00693  -0.10354 356 SER   A CA   
1463 C  C    . SER   A 204 ? 0.25570 0.52377 0.40275 -0.01203 0.01113  -0.10817 356 SER   A C    
1464 O  O    . SER   A 204 ? 0.25649 0.52964 0.39709 -0.01931 0.01243  -0.09952 356 SER   A O    
1465 C  CB   . SER   A 204 ? 0.26594 0.50194 0.43649 0.00037  -0.00020 -0.10527 356 SER   A CB   
1466 O  OG   . SER   A 204 ? 0.29054 0.50621 0.46206 0.00173  -0.00473 -0.09788 356 SER   A OG   
1467 N  N    . ASN   A 205 ? 0.26619 0.54854 0.41942 -0.00697 0.01276  -0.12219 357 ASN   A N    
1468 C  CA   . ASN   A 205 ? 0.27377 0.58046 0.42511 -0.01036 0.01691  -0.12711 357 ASN   A CA   
1469 C  C    . ASN   A 205 ? 0.27232 0.58800 0.40100 -0.02203 0.02219  -0.11977 357 ASN   A C    
1470 O  O    . ASN   A 205 ? 0.28907 0.61897 0.41349 -0.02857 0.02465  -0.11528 357 ASN   A O    
1471 C  CB   . ASN   A 205 ? 0.29142 0.61240 0.45342 -0.00275 0.01696  -0.14495 357 ASN   A CB   
1472 C  CG   . ASN   A 205 ? 0.31357 0.62764 0.50036 0.00819  0.01092  -0.15199 357 ASN   A CG   
1473 O  OD1  . ASN   A 205 ? 0.34230 0.65571 0.53993 0.01587  0.00813  -0.16550 357 ASN   A OD1  
1474 N  ND2  . ASN   A 205 ? 0.29681 0.60568 0.49310 0.00840  0.00792  -0.14256 357 ASN   A ND2  
1475 N  N    . THR   A 206 ? 0.26112 0.56834 0.37591 -0.02514 0.02327  -0.11756 358 THR   A N    
1476 C  CA   . THR   A 206 ? 0.25020 0.56198 0.34402 -0.03681 0.02664  -0.10774 358 THR   A CA   
1477 C  C    . THR   A 206 ? 0.25998 0.56120 0.34851 -0.04415 0.02571  -0.09287 358 THR   A C    
1478 O  O    . THR   A 206 ? 0.28174 0.59337 0.36093 -0.05319 0.02760  -0.08601 358 THR   A O    
1479 C  CB   . THR   A 206 ? 0.24593 0.54711 0.32827 -0.03804 0.02668  -0.10679 358 THR   A CB   
1480 O  OG1  . THR   A 206 ? 0.24731 0.55769 0.33581 -0.03115 0.02636  -0.12153 358 THR   A OG1  
1481 C  CG2  . THR   A 206 ? 0.23250 0.53906 0.29434 -0.05020 0.02897  -0.09629 358 THR   A CG2  
1482 N  N    . LEU   A 207 ? 0.23070 0.51142 0.32528 -0.04083 0.02199  -0.08768 359 LEU   A N    
1483 C  CA   . LEU   A 207 ? 0.21947 0.48952 0.30872 -0.04788 0.02002  -0.07483 359 LEU   A CA   
1484 C  C    . LEU   A 207 ? 0.22614 0.50849 0.32524 -0.04864 0.01922  -0.07431 359 LEU   A C    
1485 O  O    . LEU   A 207 ? 0.23472 0.52046 0.32528 -0.05773 0.01976  -0.06605 359 LEU   A O    
1486 C  CB   . LEU   A 207 ? 0.20991 0.45775 0.30337 -0.04411 0.01554  -0.07037 359 LEU   A CB   
1487 C  CG   . LEU   A 207 ? 0.19172 0.42814 0.28173 -0.04992 0.01201  -0.05931 359 LEU   A CG   
1488 C  CD1  . LEU   A 207 ? 0.17189 0.40438 0.24280 -0.06130 0.01384  -0.05047 359 LEU   A CD1  
1489 C  CD2  . LEU   A 207 ? 0.17739 0.39501 0.27184 -0.04548 0.00729  -0.05640 359 LEU   A CD2  
1490 N  N    . GLN   A 208 ? 0.22603 0.51443 0.34418 -0.03916 0.01724  -0.08286 360 GLN   A N    
1491 C  CA   . GLN   A 208 ? 0.26078 0.56208 0.39050 -0.03914 0.01615  -0.08282 360 GLN   A CA   
1492 C  C    . GLN   A 208 ? 0.26022 0.58359 0.38197 -0.04620 0.02118  -0.08404 360 GLN   A C    
1493 O  O    . GLN   A 208 ? 0.26169 0.59150 0.38239 -0.05290 0.02093  -0.07715 360 GLN   A O    
1494 C  CB   . GLN   A 208 ? 0.29927 0.60454 0.45154 -0.02718 0.01302  -0.09305 360 GLN   A CB   
1495 C  CG   . GLN   A 208 ? 0.34289 0.62828 0.50606 -0.02135 0.00619  -0.08865 360 GLN   A CG   
1496 C  CD   . GLN   A 208 ? 0.40626 0.69453 0.59283 -0.01010 0.00180  -0.09721 360 GLN   A CD   
1497 O  OE1  . GLN   A 208 ? 0.42711 0.72571 0.62675 -0.00848 -0.00041 -0.09725 360 GLN   A OE1  
1498 N  NE2  . GLN   A 208 ? 0.42865 0.70701 0.62135 -0.00239 -0.00012 -0.10433 360 GLN   A NE2  
1499 N  N    . THR   A 209 ? 0.26538 0.60106 0.38102 -0.04545 0.02519  -0.09239 361 THR   A N    
1500 C  CA   . THR   A 209 ? 0.27098 0.63022 0.37856 -0.05264 0.02944  -0.09323 361 THR   A CA   
1501 C  C    . THR   A 209 ? 0.25465 0.60868 0.34241 -0.06577 0.03015  -0.07907 361 THR   A C    
1502 O  O    . THR   A 209 ? 0.26013 0.62754 0.34408 -0.07393 0.03130  -0.07332 361 THR   A O    
1503 C  CB   . THR   A 209 ? 0.29563 0.67066 0.40224 -0.04827 0.03228  -0.10667 361 THR   A CB   
1504 O  OG1  . THR   A 209 ? 0.31083 0.68960 0.43767 -0.03598 0.03062  -0.12053 361 THR   A OG1  
1505 C  CG2  . THR   A 209 ? 0.29379 0.69594 0.39157 -0.05642 0.03613  -0.10697 361 THR   A CG2  
1506 N  N    . TYR   A 210 ? 0.22791 0.56213 0.30398 -0.06802 0.02892  -0.07310 362 TYR   A N    
1507 C  CA   . TYR   A 210 ? 0.22444 0.55003 0.28324 -0.07998 0.02823  -0.05937 362 TYR   A CA   
1508 C  C    . TYR   A 210 ? 0.23889 0.55772 0.29987 -0.08562 0.02542  -0.04991 362 TYR   A C    
1509 O  O    . TYR   A 210 ? 0.26146 0.58656 0.31437 -0.09575 0.02530  -0.04149 362 TYR   A O    
1510 C  CB   . TYR   A 210 ? 0.22117 0.52398 0.27029 -0.07990 0.02663  -0.05514 362 TYR   A CB   
1511 C  CG   . TYR   A 210 ? 0.22720 0.51796 0.26052 -0.09159 0.02466  -0.04102 362 TYR   A CG   
1512 C  CD1  . TYR   A 210 ? 0.21116 0.48289 0.24347 -0.09515 0.02097  -0.03244 362 TYR   A CD1  
1513 C  CD2  . TYR   A 210 ? 0.24725 0.54593 0.26755 -0.09917 0.02545  -0.03638 362 TYR   A CD2  
1514 C  CE1  . TYR   A 210 ? 0.21837 0.47768 0.23791 -0.10531 0.01823  -0.02067 362 TYR   A CE1  
1515 C  CE2  . TYR   A 210 ? 0.25286 0.53918 0.26093 -0.10954 0.02235  -0.02303 362 TYR   A CE2  
1516 C  CZ   . TYR   A 210 ? 0.25443 0.52030 0.26255 -0.11228 0.01879  -0.01569 362 TYR   A CZ   
1517 O  OH   . TYR   A 210 ? 0.26681 0.51884 0.26431 -0.12202 0.01483  -0.00349 362 TYR   A OH   
1518 N  N    . ILE   A 211 ? 0.22901 0.53503 0.30119 -0.07956 0.02225  -0.05076 363 ILE   A N    
1519 C  CA   . ILE   A 211 ? 0.21774 0.51644 0.29151 -0.08496 0.01854  -0.04232 363 ILE   A CA   
1520 C  C    . ILE   A 211 ? 0.27426 0.59549 0.35518 -0.08834 0.01997  -0.04306 363 ILE   A C    
1521 O  O    . ILE   A 211 ? 0.27646 0.59822 0.35127 -0.09806 0.01855  -0.03424 363 ILE   A O    
1522 C  CB   . ILE   A 211 ? 0.19688 0.48058 0.28178 -0.07752 0.01404  -0.04351 363 ILE   A CB   
1523 C  CG1  . ILE   A 211 ? 0.19178 0.45320 0.26760 -0.07620 0.01253  -0.04099 363 ILE   A CG1  
1524 C  CG2  . ILE   A 211 ? 0.21487 0.49436 0.30240 -0.08269 0.00960  -0.03642 363 ILE   A CG2  
1525 C  CD1  . ILE   A 211 ? 0.18986 0.43923 0.27662 -0.06829 0.00812  -0.04270 363 ILE   A CD1  
1526 N  N    . ARG   A 212 ? 0.32099 0.66013 0.41625 -0.08002 0.02220  -0.05390 364 ARG   A N    
1527 C  CA   . ARG   A 212 ? 0.36855 0.73270 0.47342 -0.08145 0.02414  -0.05699 364 ARG   A CA   
1528 C  C    . ARG   A 212 ? 0.36958 0.75022 0.46084 -0.09213 0.02770  -0.05244 364 ARG   A C    
1529 O  O    . ARG   A 212 ? 0.38204 0.77397 0.47554 -0.09859 0.02746  -0.04757 364 ARG   A O    
1530 C  CB   . ARG   A 212 ? 0.42312 0.80145 0.54724 -0.06920 0.02521  -0.07079 364 ARG   A CB   
1531 C  CG   . ARG   A 212 ? 0.47987 0.84453 0.62079 -0.06044 0.01974  -0.07200 364 ARG   A CG   
1532 C  CD   . ARG   A 212 ? 0.53209 0.90940 0.69634 -0.04936 0.01839  -0.08262 364 ARG   A CD   
1533 N  NE   . ARG   A 212 ? 0.55967 0.92134 0.73915 -0.04115 0.01170  -0.08193 364 ARG   A NE   
1534 C  CZ   . ARG   A 212 ? 0.59004 0.94708 0.77798 -0.04276 0.00616  -0.07432 364 ARG   A CZ   
1535 N  NH1  . ARG   A 212 ? 0.59605 0.93969 0.79675 -0.03577 -0.00069 -0.07267 364 ARG   A NH1  
1536 N  NH2  . ARG   A 212 ? 0.60866 0.97478 0.79232 -0.05186 0.00673  -0.06781 364 ARG   A NH2  
1537 N  N    . CYS   A 213 ? 0.35105 0.73133 0.42827 -0.09490 0.02985  -0.05217 365 CYS   A N    
1538 C  CA   . CYS   A 213 ? 0.37790 0.77575 0.44280 -0.10504 0.03216  -0.04726 365 CYS   A CA   
1539 C  C    . CYS   A 213 ? 0.37297 0.75446 0.42139 -0.11684 0.02905  -0.03214 365 CYS   A C    
1540 O  O    . CYS   A 213 ? 0.40585 0.80075 0.44711 -0.12714 0.02911  -0.02447 365 CYS   A O    
1541 C  CB   . CYS   A 213 ? 0.42141 0.83450 0.48199 -0.10110 0.03564  -0.05721 365 CYS   A CB   
1542 S  SG   . CYS   A 213 ? 0.46752 0.89967 0.54707 -0.08682 0.03860  -0.07726 365 CYS   A SG   
1543 N  N    A ARG   A 214 ? 0.34648 0.69993 0.38947 -0.11573 0.02587  -0.02760 366 ARG   A N    
1544 N  N    B ARG   A 214 ? 0.34520 0.69866 0.38826 -0.11572 0.02587  -0.02760 366 ARG   A N    
1545 C  CA   A ARG   A 214 ? 0.35132 0.68809 0.37941 -0.12577 0.02246  -0.01470 366 ARG   A CA   
1546 C  CA   B ARG   A 214 ? 0.35026 0.68698 0.37836 -0.12567 0.02248  -0.01479 366 ARG   A CA   
1547 C  C    A ARG   A 214 ? 0.34040 0.65122 0.36803 -0.12865 0.01740  -0.00686 366 ARG   A C    
1548 C  C    B ARG   A 214 ? 0.34055 0.65121 0.36813 -0.12856 0.01742  -0.00693 366 ARG   A C    
1549 O  O    A ARG   A 214 ? 0.35514 0.65210 0.37243 -0.13753 0.01367  0.00388  366 ARG   A O    
1550 O  O    B ARG   A 214 ? 0.35600 0.65263 0.37314 -0.13734 0.01371  0.00376  366 ARG   A O    
1551 C  CB   A ARG   A 214 ? 0.36352 0.69120 0.38191 -0.12335 0.02298  -0.01611 366 ARG   A CB   
1552 C  CB   B ARG   A 214 ? 0.36348 0.69135 0.38209 -0.12307 0.02307  -0.01644 366 ARG   A CB   
1553 C  CG   A ARG   A 214 ? 0.37897 0.73076 0.39783 -0.11924 0.02724  -0.02614 366 ARG   A CG   
1554 C  CG   B ARG   A 214 ? 0.38089 0.73394 0.39830 -0.12079 0.02709  -0.02478 366 ARG   A CG   
1555 C  CD   A ARG   A 214 ? 0.40895 0.77871 0.41705 -0.13012 0.02705  -0.01864 366 ARG   A CD   
1556 C  CD   B ARG   A 214 ? 0.41341 0.78136 0.41969 -0.13284 0.02617  -0.01515 366 ARG   A CD   
1557 N  NE   A ARG   A 214 ? 0.42360 0.77616 0.42154 -0.14107 0.02211  -0.00269 366 ARG   A NE   
1558 N  NE   B ARG   A 214 ? 0.42427 0.81141 0.42588 -0.13164 0.02849  -0.02160 366 ARG   A NE   
1559 C  CZ   A ARG   A 214 ? 0.44673 0.81136 0.43709 -0.15243 0.02010  0.00767  366 ARG   A CZ   
1560 C  CZ   B ARG   A 214 ? 0.44057 0.85645 0.44837 -0.12794 0.03241  -0.03292 366 ARG   A CZ   
1561 N  NH1  A ARG   A 214 ? 0.46478 0.86084 0.45544 -0.15475 0.02317  0.00374  366 ARG   A NH1  
1562 N  NH1  B ARG   A 214 ? 0.43637 0.86486 0.45586 -0.12480 0.03469  -0.03859 366 ARG   A NH1  
1563 N  NH2  A ARG   A 214 ? 0.45741 0.80311 0.44069 -0.16148 0.01451  0.02182  366 ARG   A NH2  
1564 N  NH2  B ARG   A 214 ? 0.44581 0.87854 0.44896 -0.12738 0.03366  -0.03899 366 ARG   A NH2  
1565 N  N    . HIS   A 215 ? 0.29560 0.59928 0.33444 -0.12155 0.01630  -0.01190 367 HIS   A N    
1566 C  CA   . HIS   A 215 ? 0.26615 0.54677 0.30364 -0.12450 0.01093  -0.00550 367 HIS   A CA   
1567 C  C    . HIS   A 215 ? 0.26058 0.55064 0.30545 -0.12974 0.00882  -0.00220 367 HIS   A C    
1568 O  O    . HIS   A 215 ? 0.24769 0.55153 0.30613 -0.12376 0.01004  -0.00883 367 HIS   A O    
1569 C  CB   . HIS   A 215 ? 0.25952 0.52516 0.30317 -0.11463 0.00957  -0.01146 367 HIS   A CB   
1570 C  CG   . HIS   A 215 ? 0.27183 0.51117 0.30851 -0.11777 0.00426  -0.00546 367 HIS   A CG   
1571 N  ND1  . HIS   A 215 ? 0.26607 0.48666 0.29711 -0.11359 0.00340  -0.00647 367 HIS   A ND1  
1572 C  CD2  . HIS   A 215 ? 0.28283 0.51200 0.31730 -0.12466 -0.00065 0.00076  367 HIS   A CD2  
1573 C  CE1  . HIS   A 215 ? 0.26667 0.46719 0.29195 -0.11750 -0.00159 -0.00162 367 HIS   A CE1  
1574 N  NE2  . HIS   A 215 ? 0.28238 0.48718 0.30959 -0.12411 -0.00431 0.00246  367 HIS   A NE2  
1575 N  N    . PRO   A 216 ? 0.27712 0.56030 0.31505 -0.14061 0.00508  0.00778  368 PRO   A N    
1576 C  CA   . PRO   A 216 ? 0.27854 0.57344 0.32399 -0.14642 0.00321  0.01097  368 PRO   A CA   
1577 C  C    . PRO   A 216 ? 0.24813 0.53077 0.30149 -0.14290 -0.00123 0.00889  368 PRO   A C    
1578 O  O    . PRO   A 216 ? 0.25148 0.51190 0.30047 -0.13940 -0.00427 0.00819  368 PRO   A O    
1579 C  CB   . PRO   A 216 ? 0.31725 0.60465 0.35251 -0.15921 -0.00057 0.02283  368 PRO   A CB   
1580 C  CG   . PRO   A 216 ? 0.33659 0.61074 0.35935 -0.15947 -0.00031 0.02561  368 PRO   A CG   
1581 C  CD   . PRO   A 216 ? 0.30521 0.56926 0.32956 -0.14799 0.00174  0.01666  368 PRO   A CD   
1582 N  N    . PRO   A 217 ? 0.23857 0.53609 0.30355 -0.14372 -0.00204 0.00776  369 PRO   A N    
1583 C  CA   . PRO   A 217 ? 0.23605 0.52241 0.30725 -0.14242 -0.00770 0.00740  369 PRO   A CA   
1584 C  C    . PRO   A 217 ? 0.27154 0.53869 0.33360 -0.15239 -0.01376 0.01545  369 PRO   A C    
1585 O  O    . PRO   A 217 ? 0.28102 0.54952 0.33671 -0.16163 -0.01394 0.02252  369 PRO   A O    
1586 C  CB   . PRO   A 217 ? 0.24120 0.55227 0.32802 -0.14152 -0.00671 0.00455  369 PRO   A CB   
1587 C  CG   . PRO   A 217 ? 0.25845 0.59045 0.34316 -0.14784 -0.00183 0.00726  369 PRO   A CG   
1588 C  CD   . PRO   A 217 ? 0.24083 0.56802 0.31435 -0.14527 0.00222  0.00594  369 PRO   A CD   
1589 N  N    . PRO   A 218 ? 0.28849 0.53805 0.35021 -0.15102 -0.01949 0.01455  370 PRO   A N    
1590 C  CA   . PRO   A 218 ? 0.28509 0.53335 0.35425 -0.14149 -0.02094 0.00813  370 PRO   A CA   
1591 C  C    . PRO   A 218 ? 0.26351 0.49700 0.32635 -0.13351 -0.01965 0.00441  370 PRO   A C    
1592 O  O    . PRO   A 218 ? 0.25394 0.48763 0.32346 -0.12537 -0.02082 -0.00012 370 PRO   A O    
1593 C  CB   . PRO   A 218 ? 0.31842 0.55509 0.38699 -0.14617 -0.02847 0.01017  370 PRO   A CB   
1594 C  CG   . PRO   A 218 ? 0.33371 0.55327 0.39047 -0.15538 -0.03119 0.01584  370 PRO   A CG   
1595 C  CD   . PRO   A 218 ? 0.31178 0.54313 0.36665 -0.15996 -0.02603 0.02021  370 PRO   A CD   
1596 N  N    . GLY   A 219 ? 0.27454 0.49611 0.32562 -0.13594 -0.01772 0.00687  371 GLY   A N    
1597 C  CA   . GLY   A 219 ? 0.25929 0.46676 0.30445 -0.12903 -0.01663 0.00363  371 GLY   A CA   
1598 C  C    . GLY   A 219 ? 0.26561 0.48634 0.32023 -0.11888 -0.01221 -0.00284 371 GLY   A C    
1599 O  O    . GLY   A 219 ? 0.27557 0.48654 0.32989 -0.11193 -0.01285 -0.00605 371 GLY   A O    
1600 N  N    . SER   A 220 ? 0.24767 0.49091 0.31148 -0.11780 -0.00804 -0.00520 372 SER   A N    
1601 C  CA   . SER   A 220 ? 0.24889 0.50518 0.32364 -0.10768 -0.00419 -0.01283 372 SER   A CA   
1602 C  C    . SER   A 220 ? 0.24117 0.50182 0.33128 -0.10033 -0.00788 -0.01657 372 SER   A C    
1603 O  O    . SER   A 220 ? 0.22669 0.49459 0.32807 -0.09098 -0.00633 -0.02288 372 SER   A O    
1604 C  CB   . SER   A 220 ? 0.26351 0.54371 0.34262 -0.10890 0.00140  -0.01540 372 SER   A CB   
1605 O  OG   . SER   A 220 ? 0.27399 0.56776 0.36005 -0.11429 -0.00004 -0.01279 372 SER   A OG   
1606 N  N    . HIS   A 221 ? 0.26264 0.51922 0.35426 -0.10432 -0.01341 -0.01281 373 HIS   A N    
1607 C  CA   . HIS   A 221 ? 0.25862 0.52188 0.36559 -0.09845 -0.01792 -0.01500 373 HIS   A CA   
1608 C  C    . HIS   A 221 ? 0.25853 0.51108 0.36872 -0.08961 -0.02054 -0.01731 373 HIS   A C    
1609 O  O    . HIS   A 221 ? 0.25572 0.49019 0.35387 -0.09124 -0.02346 -0.01437 373 HIS   A O    
1610 C  CB   . HIS   A 221 ? 0.26897 0.52752 0.37343 -0.10538 -0.02404 -0.01015 373 HIS   A CB   
1611 C  CG   . HIS   A 221 ? 0.27431 0.53879 0.39311 -0.10013 -0.02990 -0.01115 373 HIS   A CG   
1612 N  ND1  . HIS   A 221 ? 0.26740 0.55141 0.40604 -0.09424 -0.02940 -0.01486 373 HIS   A ND1  
1613 C  CD2  . HIS   A 221 ? 0.27280 0.52671 0.38909 -0.09972 -0.03684 -0.00883 373 HIS   A CD2  
1614 C  CE1  . HIS   A 221 ? 0.26411 0.54835 0.41300 -0.09056 -0.03642 -0.01393 373 HIS   A CE1  
1615 N  NE2  . HIS   A 221 ? 0.27852 0.54531 0.41315 -0.09405 -0.04092 -0.01006 373 HIS   A NE2  
1616 N  N    A GLN   A 222 ? 0.25000 0.51387 0.37701 -0.08029 -0.01986 -0.02261 374 GLN   A N    
1617 N  N    B GLN   A 222 ? 0.24998 0.51376 0.37696 -0.08029 -0.01988 -0.02260 374 GLN   A N    
1618 C  CA   A GLN   A 222 ? 0.24175 0.49715 0.37554 -0.07161 -0.02320 -0.02413 374 GLN   A CA   
1619 C  CA   B GLN   A 222 ? 0.24176 0.49705 0.37547 -0.07163 -0.02322 -0.02410 374 GLN   A CA   
1620 C  C    A GLN   A 222 ? 0.23101 0.47064 0.35009 -0.07150 -0.02027 -0.02404 374 GLN   A C    
1621 C  C    B GLN   A 222 ? 0.23094 0.47084 0.35038 -0.07129 -0.02021 -0.02419 374 GLN   A C    
1622 O  O    A GLN   A 222 ? 0.22470 0.45240 0.34268 -0.06784 -0.02395 -0.02243 374 GLN   A O    
1623 O  O    B GLN   A 222 ? 0.22419 0.45256 0.34328 -0.06725 -0.02382 -0.02282 374 GLN   A O    
1624 C  CB   A GLN   A 222 ? 0.25172 0.50069 0.38880 -0.07151 -0.03169 -0.01936 374 GLN   A CB   
1625 C  CB   B GLN   A 222 ? 0.25179 0.50006 0.38798 -0.07176 -0.03166 -0.01920 374 GLN   A CB   
1626 C  CG   A GLN   A 222 ? 0.27088 0.53542 0.42774 -0.06877 -0.03619 -0.01979 374 GLN   A CG   
1627 C  CG   B GLN   A 222 ? 0.27094 0.53430 0.42443 -0.07064 -0.03604 -0.01907 374 GLN   A CG   
1628 C  CD   A GLN   A 222 ? 0.28664 0.54538 0.44335 -0.07036 -0.04494 -0.01432 374 GLN   A CD   
1629 C  CD   B GLN   A 222 ? 0.27645 0.55004 0.45355 -0.06002 -0.03802 -0.02312 374 GLN   A CD   
1630 O  OE1  A GLN   A 222 ? 0.30758 0.57628 0.48188 -0.06657 -0.05054 -0.01386 374 GLN   A OE1  
1631 O  OE1  B GLN   A 222 ? 0.26679 0.53376 0.44721 -0.05343 -0.03775 -0.02506 374 GLN   A OE1  
1632 N  NE2  A GLN   A 222 ? 0.29858 0.54172 0.43519 -0.07590 -0.04634 -0.01037 374 GLN   A NE2  
1633 N  NE2  B GLN   A 222 ? 0.29496 0.58443 0.48969 -0.05824 -0.04049 -0.02428 374 GLN   A NE2  
1634 N  N    . LEU   A 223 ? 0.22941 0.46993 0.33745 -0.07577 -0.01400 -0.02518 375 LEU   A N    
1635 C  CA   . LEU   A 223 ? 0.22048 0.44542 0.31374 -0.07692 -0.01174 -0.02420 375 LEU   A CA   
1636 C  C    . LEU   A 223 ? 0.20982 0.43315 0.31120 -0.06739 -0.01078 -0.02928 375 LEU   A C    
1637 O  O    . LEU   A 223 ? 0.22243 0.43088 0.31716 -0.06600 -0.01248 -0.02745 375 LEU   A O    
1638 C  CB   . LEU   A 223 ? 0.22523 0.45273 0.30620 -0.08404 -0.00636 -0.02308 375 LEU   A CB   
1639 C  CG   . LEU   A 223 ? 0.23962 0.45110 0.30584 -0.08572 -0.00447 -0.02148 375 LEU   A CG   
1640 C  CD1  . LEU   A 223 ? 0.21692 0.40765 0.27321 -0.08840 -0.00941 -0.01693 375 LEU   A CD1  
1641 C  CD2  . LEU   A 223 ? 0.26027 0.47552 0.31566 -0.09349 -0.00064 -0.01862 375 LEU   A CD2  
1642 N  N    . TYR   A 224 ? 0.21281 0.45121 0.32873 -0.06070 -0.00825 -0.03616 376 TYR   A N    
1643 C  CA   . TYR   A 224 ? 0.23865 0.47440 0.36386 -0.05125 -0.00816 -0.04179 376 TYR   A CA   
1644 C  C    . TYR   A 224 ? 0.22579 0.45149 0.36043 -0.04641 -0.01558 -0.03815 376 TYR   A C    
1645 O  O    . TYR   A 224 ? 0.21479 0.42853 0.34722 -0.04325 -0.01683 -0.03752 376 TYR   A O    
1646 C  CB   . TYR   A 224 ? 0.27235 0.52588 0.41284 -0.04431 -0.00522 -0.05110 376 TYR   A CB   
1647 C  CG   . TYR   A 224 ? 0.30026 0.54930 0.45111 -0.03426 -0.00594 -0.05790 376 TYR   A CG   
1648 C  CD1  . TYR   A 224 ? 0.31209 0.55388 0.45216 -0.03396 -0.00211 -0.06083 376 TYR   A CD1  
1649 C  CD2  . TYR   A 224 ? 0.31072 0.56157 0.48258 -0.02528 -0.01131 -0.06079 376 TYR   A CD2  
1650 C  CE1  . TYR   A 224 ? 0.32350 0.56005 0.47321 -0.02508 -0.00333 -0.06733 376 TYR   A CE1  
1651 C  CE2  . TYR   A 224 ? 0.32135 0.56561 0.50299 -0.01632 -0.01286 -0.06679 376 TYR   A CE2  
1652 C  CZ   . TYR   A 224 ? 0.33073 0.56778 0.50111 -0.01633 -0.00875 -0.07044 376 TYR   A CZ   
1653 O  OH   . TYR   A 224 ? 0.35112 0.58053 0.53120 -0.00782 -0.01074 -0.07680 376 TYR   A OH   
1654 N  N    . ALA   A 225 ? 0.20756 0.43917 0.35327 -0.04611 -0.02100 -0.03512 377 ALA   A N    
1655 C  CA   . ALA   A 225 ? 0.20505 0.42939 0.35976 -0.04249 -0.02919 -0.02997 377 ALA   A CA   
1656 C  C    . ALA   A 225 ? 0.20783 0.41663 0.34381 -0.04841 -0.03103 -0.02337 377 ALA   A C    
1657 O  O    . ALA   A 225 ? 0.21339 0.41399 0.35161 -0.04524 -0.03552 -0.01984 377 ALA   A O    
1658 C  CB   . ALA   A 225 ? 0.21785 0.45270 0.38645 -0.04234 -0.03493 -0.02733 377 ALA   A CB   
1659 N  N    . LYS   A 226 ? 0.20151 0.40630 0.31907 -0.05714 -0.02797 -0.02133 378 LYS   A N    
1660 C  CA   . LYS   A 226 ? 0.18796 0.37724 0.28648 -0.06247 -0.02917 -0.01648 378 LYS   A CA   
1661 C  C    . LYS   A 226 ? 0.19570 0.37506 0.28723 -0.06026 -0.02544 -0.01821 378 LYS   A C    
1662 O  O    . LYS   A 226 ? 0.18246 0.35104 0.26623 -0.06041 -0.02786 -0.01466 378 LYS   A O    
1663 C  CB   . LYS   A 226 ? 0.20739 0.39335 0.29045 -0.07176 -0.02742 -0.01477 378 LYS   A CB   
1664 C  CG   . LYS   A 226 ? 0.24404 0.43648 0.33054 -0.07532 -0.03240 -0.01199 378 LYS   A CG   
1665 C  CD   . LYS   A 226 ? 0.27428 0.46311 0.34771 -0.08456 -0.03092 -0.01072 378 LYS   A CD   
1666 C  CE   . LYS   A 226 ? 0.33844 0.53613 0.41778 -0.08794 -0.03556 -0.00885 378 LYS   A CE   
1667 N  NZ   . LYS   A 226 ? 0.37993 0.57601 0.45044 -0.09694 -0.03439 -0.00761 378 LYS   A NZ   
1668 N  N    . MET   A 227 ? 0.19426 0.37834 0.28802 -0.05835 -0.01958 -0.02361 379 MET   A N    
1669 C  CA   . MET   A 227 ? 0.19685 0.37227 0.28475 -0.05615 -0.01623 -0.02570 379 MET   A CA   
1670 C  C    . MET   A 227 ? 0.19308 0.36738 0.29552 -0.04766 -0.01971 -0.02681 379 MET   A C    
1671 O  O    . MET   A 227 ? 0.18543 0.34735 0.28117 -0.04657 -0.02025 -0.02429 379 MET   A O    
1672 C  CB   . MET   A 227 ? 0.20143 0.38426 0.28741 -0.05657 -0.00960 -0.03106 379 MET   A CB   
1673 C  CG   . MET   A 227 ? 0.19696 0.37713 0.26643 -0.06617 -0.00679 -0.02759 379 MET   A CG   
1674 S  SD   . MET   A 227 ? 0.19525 0.38879 0.26220 -0.06798 0.00013  -0.03184 379 MET   A SD   
1675 C  CE   . MET   A 227 ? 0.15553 0.33682 0.21509 -0.06512 0.00234  -0.03356 379 MET   A CE   
1676 N  N    . ILE   A 228 ? 0.21438 0.39908 0.33675 -0.04109 -0.02253 -0.02977 380 ILE   A N    
1677 C  CA   . ILE   A 228 ? 0.25278 0.43466 0.39170 -0.03297 -0.02767 -0.02962 380 ILE   A CA   
1678 C  C    . ILE   A 228 ? 0.24158 0.41583 0.37702 -0.03518 -0.03439 -0.01984 380 ILE   A C    
1679 O  O    . ILE   A 228 ? 0.26551 0.42740 0.40168 -0.03120 -0.03680 -0.01565 380 ILE   A O    
1680 C  CB   . ILE   A 228 ? 0.30429 0.49706 0.46524 -0.02543 -0.03002 -0.03439 380 ILE   A CB   
1681 C  CG1  . ILE   A 228 ? 0.30965 0.50998 0.47103 -0.02250 -0.02268 -0.04495 380 ILE   A CG1  
1682 C  CG2  . ILE   A 228 ? 0.32623 0.51286 0.50459 -0.01759 -0.03728 -0.03168 380 ILE   A CG2  
1683 C  CD1  . ILE   A 228 ? 0.33928 0.53068 0.49433 -0.02022 -0.01912 -0.04913 380 ILE   A CD1  
1684 N  N    . GLN   A 229 ? 0.20748 0.38547 0.33562 -0.04146 -0.03706 -0.01482 381 GLN   A N    
1685 C  CA   . GLN   A 229 ? 0.24385 0.41246 0.36218 -0.04393 -0.04237 -0.00504 381 GLN   A CA   
1686 C  C    . GLN   A 229 ? 0.24884 0.40027 0.34624 -0.04584 -0.03825 -0.00275 381 GLN   A C    
1687 O  O    . GLN   A 229 ? 0.22629 0.36947 0.32008 -0.04430 -0.04133 0.00415  381 GLN   A O    
1688 C  CB   . GLN   A 229 ? 0.29622 0.47077 0.40702 -0.05075 -0.04517 -0.00206 381 GLN   A CB   
1689 C  CG   . GLN   A 229 ? 0.34638 0.51553 0.44635 -0.05389 -0.05100 0.00715  381 GLN   A CG   
1690 C  CD   . GLN   A 229 ? 0.37779 0.54772 0.49344 -0.04782 -0.05811 0.01461  381 GLN   A CD   
1691 O  OE1  . GLN   A 229 ? 0.40314 0.58018 0.53980 -0.04216 -0.06183 0.01336  381 GLN   A OE1  
1692 N  NE2  . GLN   A 229 ? 0.36799 0.52814 0.47285 -0.04813 -0.05930 0.02180  381 GLN   A NE2  
1693 N  N    . LYS   A 230 ? 0.24440 0.39146 0.32878 -0.04935 -0.03155 -0.00795 382 LYS   A N    
1694 C  CA   . LYS   A 230 ? 0.23489 0.36611 0.30149 -0.05039 -0.02794 -0.00661 382 LYS   A CA   
1695 C  C    . LYS   A 230 ? 0.21741 0.34186 0.29141 -0.04334 -0.02704 -0.00651 382 LYS   A C    
1696 O  O    . LYS   A 230 ? 0.21826 0.33165 0.28225 -0.04285 -0.02650 -0.00246 382 LYS   A O    
1697 C  CB   . LYS   A 230 ? 0.25857 0.38643 0.31210 -0.05582 -0.02241 -0.01119 382 LYS   A CB   
1698 C  CG   . LYS   A 230 ? 0.28906 0.41857 0.33231 -0.06408 -0.02428 -0.01010 382 LYS   A CG   
1699 C  CD   . LYS   A 230 ? 0.33819 0.45634 0.36634 -0.06591 -0.02667 -0.00657 382 LYS   A CD   
1700 C  CE   . LYS   A 230 ? 0.38696 0.50902 0.40867 -0.07306 -0.03086 -0.00597 382 LYS   A CE   
1701 N  NZ   . LYS   A 230 ? 0.41320 0.54717 0.44462 -0.07211 -0.03697 -0.00164 382 LYS   A NZ   
1702 N  N    . LEU   A 231 ? 0.20939 0.34132 0.30179 -0.03782 -0.02714 -0.01154 383 LEU   A N    
1703 C  CA   . LEU   A 231 ? 0.20786 0.33307 0.31018 -0.03113 -0.02791 -0.01176 383 LEU   A CA   
1704 C  C    . LEU   A 231 ? 0.20641 0.32841 0.31776 -0.02867 -0.03515 -0.00250 383 LEU   A C    
1705 O  O    . LEU   A 231 ? 0.19169 0.30429 0.30358 -0.02619 -0.03595 0.00160  383 LEU   A O    
1706 C  CB   . LEU   A 231 ? 0.20476 0.33977 0.32610 -0.02541 -0.02715 -0.02131 383 LEU   A CB   
1707 C  CG   . LEU   A 231 ? 0.20182 0.34329 0.31672 -0.02723 -0.01999 -0.03044 383 LEU   A CG   
1708 C  CD1  . LEU   A 231 ? 0.19092 0.34634 0.32736 -0.02065 -0.02024 -0.04090 383 LEU   A CD1  
1709 C  CD2  . LEU   A 231 ? 0.21306 0.34095 0.31266 -0.02812 -0.01573 -0.02990 383 LEU   A CD2  
1710 N  N    . ALA   A 232 ? 0.19302 0.32390 0.31267 -0.02972 -0.04096 0.00168  384 ALA   A N    
1711 C  CA   . ALA   A 232 ? 0.20843 0.33755 0.33413 -0.02919 -0.04860 0.01298  384 ALA   A CA   
1712 C  C    . ALA   A 232 ? 0.21201 0.33449 0.31450 -0.03483 -0.04697 0.02043  384 ALA   A C    
1713 O  O    . ALA   A 232 ? 0.23160 0.34956 0.33421 -0.03435 -0.04999 0.02929  384 ALA   A O    
1714 C  CB   . ALA   A 232 ? 0.21311 0.35467 0.35286 -0.02932 -0.05572 0.01579  384 ALA   A CB   
1715 N  N    . ASP   A 233 ? 0.19320 0.31603 0.27660 -0.04040 -0.04257 0.01678  385 ASP   A N    
1716 C  CA   . ASP   A 233 ? 0.19831 0.31518 0.25998 -0.04477 -0.04042 0.02053  385 ASP   A CA   
1717 C  C    . ASP   A 233 ? 0.19817 0.30435 0.25424 -0.04210 -0.03559 0.02005  385 ASP   A C    
1718 O  O    . ASP   A 233 ? 0.22406 0.32779 0.27058 -0.04326 -0.03557 0.02606  385 ASP   A O    
1719 C  CB   . ASP   A 233 ? 0.21325 0.32974 0.25817 -0.05047 -0.03694 0.01436  385 ASP   A CB   
1720 C  CG   . ASP   A 233 ? 0.27929 0.40695 0.32755 -0.05445 -0.04200 0.01531  385 ASP   A CG   
1721 O  OD1  . ASP   A 233 ? 0.29571 0.42313 0.33316 -0.05963 -0.04006 0.01023  385 ASP   A OD1  
1722 O  OD2  . ASP   A 233 ? 0.27331 0.40962 0.33571 -0.05274 -0.04853 0.02142  385 ASP   A OD2  
1723 N  N    . LEU   A 234 ? 0.18754 0.28919 0.24906 -0.03886 -0.03133 0.01273  386 LEU   A N    
1724 C  CA   . LEU   A 234 ? 0.19706 0.28903 0.25412 -0.03637 -0.02714 0.01190  386 LEU   A CA   
1725 C  C    . LEU   A 234 ? 0.20042 0.29126 0.27093 -0.03279 -0.03142 0.01961  386 LEU   A C    
1726 O  O    . LEU   A 234 ? 0.20812 0.29350 0.27208 -0.03270 -0.02943 0.02349  386 LEU   A O    
1727 C  CB   . LEU   A 234 ? 0.19577 0.28528 0.25596 -0.03422 -0.02255 0.00265  386 LEU   A CB   
1728 C  CG   . LEU   A 234 ? 0.20890 0.29609 0.25300 -0.03886 -0.01778 -0.00280 386 LEU   A CG   
1729 C  CD1  . LEU   A 234 ? 0.20236 0.29324 0.25237 -0.03788 -0.01459 -0.01033 386 LEU   A CD1  
1730 C  CD2  . LEU   A 234 ? 0.21783 0.29403 0.24552 -0.03994 -0.01431 -0.00190 386 LEU   A CD2  
1731 N  N    . ARG   A 235 ? 0.19933 0.29554 0.29034 -0.02987 -0.03781 0.02215  387 ARG   A N    
1732 C  CA   . ARG   A 235 ? 0.21595 0.30989 0.32189 -0.02731 -0.04365 0.03115  387 ARG   A CA   
1733 C  C    . ARG   A 235 ? 0.23622 0.33269 0.33081 -0.03204 -0.04585 0.04361  387 ARG   A C    
1734 O  O    . ARG   A 235 ? 0.24486 0.33809 0.34050 -0.03223 -0.04643 0.05099  387 ARG   A O    
1735 C  CB   . ARG   A 235 ? 0.23037 0.32923 0.36208 -0.02322 -0.05170 0.03181  387 ARG   A CB   
1736 C  CG   . ARG   A 235 ? 0.23640 0.33668 0.38102 -0.01801 -0.04956 0.01826  387 ARG   A CG   
1737 C  CD   . ARG   A 235 ? 0.24694 0.33858 0.39601 -0.01426 -0.04674 0.01296  387 ARG   A CD   
1738 N  NE   . ARG   A 235 ? 0.27036 0.36632 0.43283 -0.00904 -0.04535 -0.00075 387 ARG   A NE   
1739 C  CZ   . ARG   A 235 ? 0.28252 0.37865 0.47056 -0.00260 -0.05140 -0.00512 387 ARG   A CZ   
1740 N  NH1  . ARG   A 235 ? 0.28849 0.37578 0.48685 -0.00106 -0.05845 0.00478  387 ARG   A NH1  
1741 N  NH2  . ARG   A 235 ? 0.28957 0.39022 0.48302 0.00209  -0.04789 -0.01922 387 ARG   A NH2  
1742 N  N    . SER   A 236 ? 0.23862 0.34263 0.32201 -0.03638 -0.04706 0.04593  388 SER   A N    
1743 C  CA   . SER   A 236 ? 0.25558 0.36536 0.32592 -0.04131 -0.04880 0.05651  388 SER   A CA   
1744 C  C    . SER   A 236 ? 0.24680 0.35287 0.29604 -0.04309 -0.04076 0.05298  388 SER   A C    
1745 O  O    . SER   A 236 ? 0.22696 0.33678 0.27027 -0.04518 -0.04063 0.06140  388 SER   A O    
1746 C  CB   . SER   A 236 ? 0.30702 0.42662 0.37096 -0.04539 -0.05266 0.05812  388 SER   A CB   
1747 O  OG   . SER   A 236 ? 0.35719 0.48363 0.40255 -0.05056 -0.05222 0.06435  388 SER   A OG   
1748 N  N    . LEU   A 237 ? 0.22908 0.32889 0.26777 -0.04243 -0.03431 0.04094  389 LEU   A N    
1749 C  CA   . LEU   A 237 ? 0.20267 0.29734 0.22486 -0.04280 -0.02738 0.03646  389 LEU   A CA   
1750 C  C    . LEU   A 237 ? 0.19361 0.28257 0.22409 -0.03930 -0.02536 0.03889  389 LEU   A C    
1751 O  O    . LEU   A 237 ? 0.15692 0.24685 0.17847 -0.03992 -0.02199 0.04148  389 LEU   A O    
1752 C  CB   . LEU   A 237 ? 0.21034 0.29808 0.22276 -0.04307 -0.02268 0.02443  389 LEU   A CB   
1753 C  CG   . LEU   A 237 ? 0.22844 0.32111 0.23079 -0.04760 -0.02456 0.02147  389 LEU   A CG   
1754 C  CD1  . LEU   A 237 ? 0.21756 0.30391 0.21717 -0.04860 -0.02193 0.01191  389 LEU   A CD1  
1755 C  CD2  . LEU   A 237 ? 0.26510 0.36124 0.24949 -0.05042 -0.02312 0.02155  389 LEU   A CD2  
1756 N  N    . ASN   A 238 ? 0.19151 0.27570 0.23963 -0.03553 -0.02745 0.03715  390 ASN   A N    
1757 C  CA   . ASN   A 238 ? 0.21224 0.29115 0.27116 -0.03247 -0.02723 0.03966  390 ASN   A CA   
1758 C  C    . ASN   A 238 ? 0.23582 0.32056 0.29990 -0.03476 -0.03154 0.05361  390 ASN   A C    
1759 O  O    . ASN   A 238 ? 0.23362 0.31811 0.29367 -0.03530 -0.02852 0.05726  390 ASN   A O    
1760 C  CB   . ASN   A 238 ? 0.19048 0.26550 0.26924 -0.02806 -0.03039 0.03449  390 ASN   A CB   
1761 C  CG   . ASN   A 238 ? 0.20856 0.27674 0.29803 -0.02473 -0.03007 0.03374  390 ASN   A CG   
1762 O  OD1  . ASN   A 238 ? 0.19923 0.26679 0.28772 -0.02604 -0.03000 0.04144  390 ASN   A OD1  
1763 N  ND2  . ASN   A 238 ? 0.20300 0.26773 0.30322 -0.02069 -0.03002 0.02419  390 ASN   A ND2  
1764 N  N    . GLU   A 239 ? 0.26037 0.35174 0.33382 -0.03661 -0.03893 0.06242  391 GLU   A N    
1765 C  CA   . GLU   A 239 ? 0.29747 0.39581 0.37662 -0.04008 -0.04432 0.07823  391 GLU   A CA   
1766 C  C    . GLU   A 239 ? 0.25916 0.36670 0.31676 -0.04462 -0.03895 0.08224  391 GLU   A C    
1767 O  O    . GLU   A 239 ? 0.24936 0.36076 0.30804 -0.04654 -0.03826 0.09091  391 GLU   A O    
1768 C  CB   . GLU   A 239 ? 0.36300 0.46796 0.45322 -0.04186 -0.05363 0.08710  391 GLU   A CB   
1769 C  CG   . GLU   A 239 ? 0.43025 0.52874 0.54875 -0.03743 -0.06182 0.08835  391 GLU   A CG   
1770 C  CD   . GLU   A 239 ? 0.50757 0.61334 0.63926 -0.04004 -0.07284 0.10265  391 GLU   A CD   
1771 O  OE1  . GLU   A 239 ? 0.52417 0.63854 0.64631 -0.04261 -0.07406 0.10318  391 GLU   A OE1  
1772 O  OE2  . GLU   A 239 ? 0.54490 0.64528 0.69458 -0.03974 -0.07956 0.11280  391 GLU   A OE2  
1773 N  N    . GLU   A 240 ? 0.24748 0.35983 0.28617 -0.04648 -0.03530 0.07548  392 GLU   A N    
1774 C  CA   . GLU   A 240 ? 0.26124 0.38444 0.27975 -0.05021 -0.03058 0.07706  392 GLU   A CA   
1775 C  C    . GLU   A 240 ? 0.25619 0.37428 0.26729 -0.04750 -0.02231 0.06945  392 GLU   A C    
1776 O  O    . GLU   A 240 ? 0.27798 0.40596 0.28266 -0.04957 -0.01931 0.07505  392 GLU   A O    
1777 C  CB   . GLU   A 240 ? 0.26648 0.39473 0.26836 -0.05251 -0.02984 0.06973  392 GLU   A CB   
1778 C  CG   . GLU   A 240 ? 0.30492 0.44634 0.28567 -0.05597 -0.02550 0.06890  392 GLU   A CG   
1779 C  CD   . GLU   A 240 ? 0.33738 0.49605 0.31868 -0.06090 -0.02896 0.08546  392 GLU   A CD   
1780 O  OE1  . GLU   A 240 ? 0.35043 0.51989 0.32060 -0.06234 -0.02358 0.08629  392 GLU   A OE1  
1781 O  OE2  . GLU   A 240 ? 0.34685 0.50937 0.34049 -0.06349 -0.03735 0.09804  392 GLU   A OE2  
1782 N  N    . HIS   A 241 ? 0.20690 0.31139 0.21908 -0.04312 -0.01866 0.05716  393 HIS   A N    
1783 C  CA   . HIS   A 241 ? 0.19200 0.29124 0.19894 -0.04027 -0.01189 0.05069  393 HIS   A CA   
1784 C  C    . HIS   A 241 ? 0.20773 0.30809 0.22826 -0.03981 -0.01291 0.05999  393 HIS   A C    
1785 O  O    . HIS   A 241 ? 0.20403 0.31034 0.21898 -0.04011 -0.00838 0.06153  393 HIS   A O    
1786 C  CB   . HIS   A 241 ? 0.19105 0.27595 0.19814 -0.03642 -0.00913 0.03811  393 HIS   A CB   
1787 C  CG   . HIS   A 241 ? 0.19345 0.27234 0.19873 -0.03321 -0.00379 0.03319  393 HIS   A CG   
1788 N  ND1  . HIS   A 241 ? 0.18771 0.26135 0.20690 -0.03077 -0.00453 0.03559  393 HIS   A ND1  
1789 C  CD2  . HIS   A 241 ? 0.19189 0.26993 0.18436 -0.03190 0.00163  0.02606  393 HIS   A CD2  
1790 C  CE1  . HIS   A 241 ? 0.19179 0.26219 0.20621 -0.02843 0.00034  0.03093  393 HIS   A CE1  
1791 N  NE2  . HIS   A 241 ? 0.19201 0.26488 0.19087 -0.02874 0.00412  0.02515  393 HIS   A NE2  
1792 N  N    . SER   A 242 ? 0.22557 0.32084 0.26537 -0.03905 -0.01923 0.06580  394 SER   A N    
1793 C  CA   . SER   A 242 ? 0.24657 0.34143 0.30206 -0.03923 -0.02194 0.07509  394 SER   A CA   
1794 C  C    . SER   A 242 ? 0.23739 0.34779 0.28980 -0.04489 -0.02306 0.08981  394 SER   A C    
1795 O  O    . SER   A 242 ? 0.23551 0.35013 0.29119 -0.04608 -0.02089 0.09541  394 SER   A O    
1796 C  CB   . SER   A 242 ? 0.28557 0.37239 0.36372 -0.03731 -0.03016 0.07779  394 SER   A CB   
1797 O  OG   . SER   A 242 ? 0.31918 0.39527 0.39965 -0.03239 -0.02830 0.06374  394 SER   A OG   
1798 N  N    A LYS   A 243 ? 0.24323 0.36419 0.28926 -0.04898 -0.02654 0.09673  395 LYS   A N    
1799 N  N    B LYS   A 243 ? 0.24472 0.36550 0.29115 -0.04896 -0.02670 0.09683  395 LYS   A N    
1800 C  CA   A LYS   A 243 ? 0.25133 0.39052 0.29232 -0.05540 -0.02762 0.11156  395 LYS   A CA   
1801 C  CA   B LYS   A 243 ? 0.24990 0.38907 0.29064 -0.05539 -0.02767 0.11139  395 LYS   A CA   
1802 C  C    A LYS   A 243 ? 0.24661 0.39703 0.26857 -0.05582 -0.01791 0.10568  395 LYS   A C    
1803 C  C    B LYS   A 243 ? 0.24672 0.39672 0.26891 -0.05570 -0.01793 0.10549  395 LYS   A C    
1804 O  O    A LYS   A 243 ? 0.24946 0.41137 0.27303 -0.05889 -0.01585 0.11474  395 LYS   A O    
1805 O  O    B LYS   A 243 ? 0.24771 0.40821 0.27226 -0.05849 -0.01586 0.11422  395 LYS   A O    
1806 C  CB   A LYS   A 243 ? 0.26968 0.41883 0.30561 -0.05966 -0.03349 0.11886  395 LYS   A CB   
1807 C  CB   B LYS   A 243 ? 0.26993 0.41875 0.30443 -0.05938 -0.03306 0.11742  395 LYS   A CB   
1808 C  CG   A LYS   A 243 ? 0.29195 0.46329 0.31992 -0.06724 -0.03469 0.13443  395 LYS   A CG   
1809 C  CG   B LYS   A 243 ? 0.29358 0.46169 0.32750 -0.06715 -0.03764 0.13684  395 LYS   A CG   
1810 C  CD   A LYS   A 243 ? 0.30600 0.48487 0.33747 -0.07120 -0.04322 0.14272  395 LYS   A CD   
1811 C  CD   B LYS   A 243 ? 0.30351 0.47912 0.33439 -0.07034 -0.04418 0.14098  395 LYS   A CD   
1812 C  CE   A LYS   A 243 ? 0.30088 0.46714 0.33592 -0.06765 -0.04790 0.13644  395 LYS   A CE   
1813 C  CE   B LYS   A 243 ? 0.32228 0.51918 0.34644 -0.07633 -0.04376 0.14727  395 LYS   A CE   
1814 N  NZ   A LYS   A 243 ? 0.30380 0.45760 0.36661 -0.06546 -0.05764 0.14395  395 LYS   A NZ   
1815 N  NZ   B LYS   A 243 ? 0.32837 0.53169 0.35697 -0.08070 -0.05152 0.15536  395 LYS   A NZ   
1816 N  N    . GLN   A 244 ? 0.23333 0.38095 0.23858 -0.05270 -0.01216 0.09018  396 GLN   A N    
1817 C  CA   . GLN   A 244 ? 0.22371 0.38097 0.21283 -0.05171 -0.00348 0.08206  396 GLN   A CA   
1818 C  C    . GLN   A 244 ? 0.23520 0.38420 0.23167 -0.04732 0.00130  0.07714  396 GLN   A C    
1819 O  O    . GLN   A 244 ? 0.24768 0.40948 0.23939 -0.04774 0.00685  0.07793  396 GLN   A O    
1820 C  CB   . GLN   A 244 ? 0.21949 0.37305 0.19182 -0.04943 -0.00047 0.06652  396 GLN   A CB   
1821 C  CG   . GLN   A 244 ? 0.25604 0.41859 0.22133 -0.05412 -0.00584 0.07116  396 GLN   A CG   
1822 C  CD   . GLN   A 244 ? 0.28248 0.44617 0.22935 -0.05331 -0.00284 0.05649  396 GLN   A CD   
1823 O  OE1  . GLN   A 244 ? 0.28829 0.44735 0.22717 -0.04926 0.00328  0.04316  396 GLN   A OE1  
1824 N  NE2  . GLN   A 244 ? 0.29005 0.45983 0.23120 -0.05719 -0.00798 0.05886  396 GLN   A NE2  
1825 N  N    . TYR   A 245 ? 0.20181 0.33154 0.21015 -0.04321 -0.00080 0.07196  397 TYR   A N    
1826 C  CA   . TYR   A 245 ? 0.23481 0.35706 0.25068 -0.03944 0.00264  0.06799  397 TYR   A CA   
1827 C  C    . TYR   A 245 ? 0.24573 0.37781 0.27450 -0.04303 0.00088  0.08237  397 TYR   A C    
1828 O  O    . TYR   A 245 ? 0.24245 0.38037 0.27121 -0.04201 0.00589  0.08145  397 TYR   A O    
1829 C  CB   . TYR   A 245 ? 0.20798 0.31046 0.23413 -0.03528 -0.00014 0.06069  397 TYR   A CB   
1830 C  CG   . TYR   A 245 ? 0.21197 0.30757 0.24679 -0.03199 0.00212  0.05775  397 TYR   A CG   
1831 C  CD1  . TYR   A 245 ? 0.20518 0.29648 0.23077 -0.02797 0.00801  0.04658  397 TYR   A CD1  
1832 C  CD2  . TYR   A 245 ? 0.21768 0.31115 0.27099 -0.03309 -0.00255 0.06645  397 TYR   A CD2  
1833 C  CE1  . TYR   A 245 ? 0.20764 0.29374 0.24143 -0.02510 0.00947  0.04448  397 TYR   A CE1  
1834 C  CE2  . TYR   A 245 ? 0.21702 0.30520 0.27825 -0.03052 -0.00101 0.06362  397 TYR   A CE2  
1835 C  CZ   . TYR   A 245 ? 0.22173 0.30686 0.27274 -0.02656 0.00512  0.05287  397 TYR   A CZ   
1836 O  OH   . TYR   A 245 ? 0.23278 0.31340 0.29225 -0.02416 0.00588  0.05068  397 TYR   A OH   
1837 N  N    . ARG   A 246 ? 0.26964 0.40312 0.31148 -0.04729 -0.00695 0.09604  398 ARG   A N    
1838 C  CA   . ARG   A 246 ? 0.32328 0.46622 0.37870 -0.05224 -0.01010 0.11207  398 ARG   A CA   
1839 C  C    . ARG   A 246 ? 0.32399 0.48912 0.36597 -0.05553 -0.00533 0.11643  398 ARG   A C    
1840 O  O    . ARG   A 246 ? 0.31193 0.48350 0.35857 -0.05563 -0.00355 0.11937  398 ARG   A O    
1841 C  CB   . ARG   A 246 ? 0.38069 0.52031 0.45269 -0.05616 -0.02095 0.12598  398 ARG   A CB   
1842 C  CG   . ARG   A 246 ? 0.43838 0.55744 0.53132 -0.05193 -0.02728 0.12205  398 ARG   A CG   
1843 C  CD   . ARG   A 246 ? 0.49273 0.60917 0.60628 -0.05556 -0.03915 0.13674  398 ARG   A CD   
1844 N  NE   . ARG   A 246 ? 0.53726 0.65630 0.64526 -0.05631 -0.04303 0.13812  398 ARG   A NE   
1845 C  CZ   . ARG   A 246 ? 0.55644 0.66333 0.66793 -0.05102 -0.04535 0.12673  398 ARG   A CZ   
1846 N  NH1  . ARG   A 246 ? 0.55615 0.64830 0.67540 -0.04477 -0.04387 0.11303  398 ARG   A NH1  
1847 N  NH2  . ARG   A 246 ? 0.55140 0.66276 0.65853 -0.05229 -0.04912 0.12909  398 ARG   A NH2  
1848 N  N    . SER   A 247 ? 0.30221 0.47836 0.32770 -0.05706 -0.00404 0.11392  399 SER   A N    
1849 C  CA   . SER   A 247 ? 0.31913 0.51592 0.33217 -0.05859 0.00002  0.11307  399 SER   A CA   
1850 C  C    . SER   A 247 ? 0.29318 0.49256 0.29771 -0.05365 0.00980  0.09983  399 SER   A C    
1851 O  O    . SER   A 247 ? 0.30626 0.51901 0.31161 -0.05420 0.01260  0.10201  399 SER   A O    
1852 C  CB   . SER   A 247 ? 0.36601 0.57263 0.36408 -0.06075 -0.00083 0.11013  399 SER   A CB   
1853 O  OG   . SER   A 247 ? 0.41461 0.63742 0.39741 -0.05970 0.00596  0.10073  399 SER   A OG   
1854 N  N    . LEU   A 248 ? 0.27036 0.45796 0.26757 -0.04885 0.01466  0.08616  400 LEU   A N    
1855 C  CA   . LEU   A 248 ? 0.29772 0.48697 0.28855 -0.04337 0.02305  0.07280  400 LEU   A CA   
1856 C  C    . LEU   A 248 ? 0.30977 0.49497 0.31614 -0.04199 0.02408  0.07691  400 LEU   A C    
1857 O  O    . LEU   A 248 ? 0.32012 0.51618 0.32603 -0.04006 0.02876  0.07398  400 LEU   A O    
1858 C  CB   . LEU   A 248 ? 0.29439 0.46719 0.27635 -0.03789 0.02510  0.05653  400 LEU   A CB   
1859 C  CG   . LEU   A 248 ? 0.31023 0.48888 0.27504 -0.03897 0.02531  0.04949  400 LEU   A CG   
1860 C  CD1  . LEU   A 248 ? 0.30505 0.46067 0.26681 -0.03485 0.02310  0.03683  400 LEU   A CD1  
1861 C  CD2  . LEU   A 248 ? 0.31431 0.50872 0.26788 -0.03646 0.03106  0.03945  400 LEU   A CD2  
1862 N  N    . SER   A 249 ? 0.31507 0.48304 0.33633 -0.04213 0.01869  0.08169  401 SER   A N    
1863 C  CA   . SER   A 249 ? 0.31476 0.47614 0.35114 -0.04025 0.01861  0.08311  401 SER   A CA   
1864 C  C    . SER   A 249 ? 0.32575 0.49912 0.37311 -0.04523 0.01541  0.09774  401 SER   A C    
1865 O  O    . SER   A 249 ? 0.32728 0.49967 0.38520 -0.04409 0.01622  0.09865  401 SER   A O    
1866 C  CB   . SER   A 249 ? 0.30141 0.43826 0.34961 -0.03744 0.01229  0.07980  401 SER   A CB   
1867 O  OG   . SER   A 249 ? 0.32021 0.45420 0.37911 -0.04202 0.00425  0.09152  401 SER   A OG   
1868 N  N    . PHE   A 250 ? 0.33425 0.51715 0.37934 -0.05012 0.01040  0.10818  402 PHE   A N    
1869 C  CA   . PHE   A 250 ? 0.35796 0.55198 0.41232 -0.05457 0.00604  0.12147  402 PHE   A CA   
1870 C  C    . PHE   A 250 ? 0.34403 0.55661 0.39079 -0.05370 0.01351  0.11758  402 PHE   A C    
1871 O  O    . PHE   A 250 ? 0.33608 0.55648 0.39238 -0.05643 0.01164  0.12641  402 PHE   A O    
1872 C  CB   . PHE   A 250 ? 0.41240 0.61532 0.46602 -0.06019 -0.00125 0.13345  402 PHE   A CB   
1873 C  CG   . PHE   A 250 ? 0.49007 0.70369 0.55588 -0.06558 -0.00767 0.14908  402 PHE   A CG   
1874 C  CD1  . PHE   A 250 ? 0.53434 0.77252 0.59171 -0.06972 -0.00581 0.15429  402 PHE   A CD1  
1875 C  CD2  . PHE   A 250 ? 0.51603 0.71585 0.60248 -0.06661 -0.01605 0.15807  402 PHE   A CD2  
1876 C  CE1  . PHE   A 250 ? 0.56415 0.81388 0.63321 -0.07553 -0.01207 0.16978  402 PHE   A CE1  
1877 C  CE2  . PHE   A 250 ? 0.54359 0.75315 0.64219 -0.07183 -0.02282 0.17283  402 PHE   A CE2  
1878 C  CZ   . PHE   A 250 ? 0.56683 0.80180 0.65662 -0.07668 -0.02079 0.17947  402 PHE   A CZ   
1879 N  N    . GLN   A 251 ? 0.31554 0.53559 0.34615 -0.04980 0.02147  0.10409  403 GLN   A N    
1880 C  CA   . GLN   A 251 ? 0.29424 0.53188 0.31894 -0.04775 0.02863  0.09798  403 GLN   A CA   
1881 C  C    . GLN   A 251 ? 0.26838 0.49689 0.30033 -0.04202 0.03347  0.08915  403 GLN   A C    
1882 O  O    . GLN   A 251 ? 0.22338 0.43810 0.25240 -0.03697 0.03600  0.07802  403 GLN   A O    
1883 C  CB   . GLN   A 251 ? 0.32772 0.57727 0.33400 -0.04546 0.03381  0.08606  403 GLN   A CB   
1884 C  CG   . GLN   A 251 ? 0.40700 0.66353 0.40620 -0.05102 0.02830  0.09360  403 GLN   A CG   
1885 C  CD   . GLN   A 251 ? 0.48711 0.76247 0.49224 -0.05829 0.02357  0.10996  403 GLN   A CD   
1886 O  OE1  . GLN   A 251 ? 0.52743 0.80603 0.53378 -0.06381 0.01657  0.12095  403 GLN   A OE1  
1887 N  NE2  . GLN   A 251 ? 0.51696 0.80572 0.52659 -0.05851 0.02705  0.11194  403 GLN   A NE2  
1888 N  N    . PRO   A 252 ? 0.27417 0.51048 0.31631 -0.04290 0.03427  0.09423  404 PRO   A N    
1889 C  CA   . PRO   A 252 ? 0.27066 0.49715 0.32310 -0.03805 0.03705  0.08770  404 PRO   A CA   
1890 C  C    . PRO   A 252 ? 0.29650 0.52401 0.33997 -0.03004 0.04497  0.06993  404 PRO   A C    
1891 O  O    . PRO   A 252 ? 0.31274 0.52640 0.36199 -0.02524 0.04581  0.06267  404 PRO   A O    
1892 C  CB   . PRO   A 252 ? 0.27616 0.51594 0.33886 -0.04132 0.03658  0.09680  404 PRO   A CB   
1893 C  CG   . PRO   A 252 ? 0.29206 0.54196 0.35425 -0.04905 0.03054  0.11202  404 PRO   A CG   
1894 C  CD   . PRO   A 252 ? 0.29021 0.54497 0.33610 -0.04899 0.03172  0.10732  404 PRO   A CD   
1895 N  N    . GLU   A 253 ? 0.31839 0.56201 0.34873 -0.02819 0.04998  0.06223  405 GLU   A N    
1896 C  CA   . GLU   A 253 ? 0.34131 0.58468 0.36469 -0.01966 0.05632  0.04402  405 GLU   A CA   
1897 C  C    . GLU   A 253 ? 0.31866 0.54381 0.33458 -0.01611 0.05545  0.03476  405 GLU   A C    
1898 O  O    . GLU   A 253 ? 0.31220 0.52978 0.32743 -0.00855 0.05858  0.02097  405 GLU   A O    
1899 C  CB   . GLU   A 253 ? 0.40167 0.66616 0.41384 -0.01860 0.06073  0.03703  405 GLU   A CB   
1900 C  CG   . GLU   A 253 ? 0.47087 0.73985 0.46835 -0.02213 0.05869  0.03699  405 GLU   A CG   
1901 C  CD   . GLU   A 253 ? 0.51733 0.79851 0.51588 -0.03158 0.05367  0.05508  405 GLU   A CD   
1902 O  OE1  . GLU   A 253 ? 0.51250 0.79664 0.52334 -0.03571 0.05118  0.06817  405 GLU   A OE1  
1903 O  OE2  . GLU   A 253 ? 0.55946 0.84731 0.54726 -0.03492 0.05149  0.05616  405 GLU   A OE2  
1904 N  N    . ASN   A 254 ? 0.28884 0.50690 0.29991 -0.02131 0.05068  0.04211  406 ASN   A N    
1905 C  CA   . ASN   A 254 ? 0.27482 0.47547 0.28032 -0.01909 0.04933  0.03518  406 ASN   A CA   
1906 C  C    . ASN   A 254 ? 0.25586 0.43295 0.27454 -0.01770 0.04412  0.03761  406 ASN   A C    
1907 O  O    . ASN   A 254 ? 0.24183 0.39909 0.25879 -0.01198 0.04290  0.02635  406 ASN   A O    
1908 C  CB   . ASN   A 254 ? 0.28605 0.48583 0.28274 -0.02488 0.04475  0.04173  406 ASN   A CB   
1909 C  CG   . ASN   A 254 ? 0.34348 0.55637 0.32456 -0.02449 0.04683  0.03390  406 ASN   A CG   
1910 O  OD1  . ASN   A 254 ? 0.37324 0.59030 0.34841 -0.01854 0.05162  0.01959  406 ASN   A OD1  
1911 N  ND2  . ASN   A 254 ? 0.33170 0.55121 0.30777 -0.03065 0.04242  0.04302  406 ASN   A ND2  
1912 N  N    . SER   A 255 ? 0.26573 0.44442 0.29788 -0.02327 0.04011  0.05230  407 SER   A N    
1913 C  CA   . SER   A 255 ? 0.26869 0.42668 0.31421 -0.02207 0.03458  0.05369  407 SER   A CA   
1914 C  C    . SER   A 255 ? 0.24523 0.39797 0.29529 -0.01551 0.03732  0.04405  407 SER   A C    
1915 O  O    . SER   A 255 ? 0.23730 0.37002 0.29139 -0.01232 0.03358  0.03884  407 SER   A O    
1916 C  CB   . SER   A 255 ? 0.31157 0.47509 0.37304 -0.02906 0.02974  0.07039  407 SER   A CB   
1917 O  OG   . SER   A 255 ? 0.35957 0.51343 0.42274 -0.03299 0.02311  0.07713  407 SER   A OG   
1918 N  N    . MET   A 256 ? 0.21602 0.38811 0.26557 -0.01338 0.04372  0.04138  408 MET   A N    
1919 C  CA   . MET   A 256 ? 0.24097 0.40976 0.29666 -0.00665 0.04587  0.03255  408 MET   A CA   
1920 C  C    . MET   A 256 ? 0.24505 0.39374 0.29183 0.00031  0.04498  0.01801  408 MET   A C    
1921 O  O    . MET   A 256 ? 0.22903 0.36575 0.28203 0.00508  0.04323  0.01263  408 MET   A O    
1922 C  CB   . MET   A 256 ? 0.24108 0.43715 0.29762 -0.00480 0.05347  0.03045  408 MET   A CB   
1923 C  CG   . MET   A 256 ? 0.29975 0.51128 0.36990 -0.00978 0.05354  0.04269  408 MET   A CG   
1924 S  SD   . MET   A 256 ? 0.34465 0.57486 0.41633 -0.00366 0.06028  0.03310  408 MET   A SD   
1925 C  CE   . MET   A 256 ? 0.33050 0.57083 0.38216 -0.00107 0.06504  0.02194  408 MET   A CE   
1926 N  N    . LYS   A 257 ? 0.22267 0.36827 0.25533 0.00040  0.04560  0.01228  409 LYS   A N    
1927 C  CA   . LYS   A 257 ? 0.23678 0.36437 0.26067 0.00574  0.04431  -0.00067 409 LYS   A CA   
1928 C  C    . LYS   A 257 ? 0.20976 0.31456 0.23240 0.00356  0.03810  0.00102  409 LYS   A C    
1929 O  O    . LYS   A 257 ? 0.20335 0.29233 0.21987 0.00671  0.03617  -0.00769 409 LYS   A O    
1930 C  CB   . LYS   A 257 ? 0.29322 0.42988 0.30301 0.00641  0.04765  -0.00855 409 LYS   A CB   
1931 C  CG   . LYS   A 257 ? 0.35732 0.51968 0.36648 0.00922  0.05459  -0.01326 409 LYS   A CG   
1932 C  CD   . LYS   A 257 ? 0.41338 0.57081 0.42821 0.01828  0.05607  -0.02606 409 LYS   A CD   
1933 C  CE   . LYS   A 257 ? 0.47438 0.65946 0.48940 0.02234  0.06348  -0.03365 409 LYS   A CE   
1934 N  NZ   . LYS   A 257 ? 0.49905 0.67699 0.51727 0.03252  0.06393  -0.05049 409 LYS   A NZ   
1935 N  N    . LEU   A 258 ? 0.19280 0.29658 0.22175 -0.00189 0.03468  0.01180  410 LEU   A N    
1936 C  CA   . LEU   A 258 ? 0.17198 0.25752 0.20140 -0.00355 0.02921  0.01242  410 LEU   A CA   
1937 C  C    . LEU   A 258 ? 0.19409 0.26781 0.23214 -0.00068 0.02653  0.01024  410 LEU   A C    
1938 O  O    . LEU   A 258 ? 0.20044 0.27950 0.24490 0.00241  0.02838  0.00921  410 LEU   A O    
1939 C  CB   . LEU   A 258 ? 0.18998 0.27973 0.22490 -0.00956 0.02595  0.02344  410 LEU   A CB   
1940 C  CG   . LEU   A 258 ? 0.18778 0.29001 0.21358 -0.01327 0.02747  0.02722  410 LEU   A CG   
1941 C  CD1  . LEU   A 258 ? 0.15749 0.26014 0.19060 -0.01885 0.02223  0.03853  410 LEU   A CD1  
1942 C  CD2  . LEU   A 258 ? 0.19452 0.28959 0.20553 -0.01114 0.02849  0.01669  410 LEU   A CD2  
1943 N  N    . THR   A 259 ? 0.19137 0.25064 0.22955 -0.00169 0.02213  0.00914  411 THR   A N    
1944 C  CA   . THR   A 259 ? 0.19866 0.24921 0.24428 0.00015  0.01914  0.00762  411 THR   A CA   
1945 C  C    . THR   A 259 ? 0.17796 0.22911 0.23590 -0.00318 0.01520  0.01412  411 THR   A C    
1946 O  O    . THR   A 259 ? 0.17681 0.23116 0.23706 -0.00672 0.01379  0.01936  411 THR   A O    
1947 C  CB   . THR   A 259 ? 0.22600 0.26187 0.26346 0.00122  0.01677  0.00105  411 THR   A CB   
1948 O  OG1  . THR   A 259 ? 0.23886 0.27079 0.27504 -0.00234 0.01420  0.00239  411 THR   A OG1  
1949 C  CG2  . THR   A 259 ? 0.25102 0.28372 0.27719 0.00358  0.01909  -0.00522 411 THR   A CG2  
1950 N  N    . PRO   A 260 ? 0.19146 0.23932 0.25866 -0.00209 0.01246  0.01373  412 PRO   A N    
1951 C  CA   . PRO   A 260 ? 0.17872 0.22578 0.25913 -0.00499 0.00764  0.01808  412 PRO   A CA   
1952 C  C    . PRO   A 260 ? 0.16831 0.20737 0.24691 -0.00643 0.00426  0.01528  412 PRO   A C    
1953 O  O    . PRO   A 260 ? 0.16663 0.20698 0.25529 -0.00902 0.00080  0.01982  412 PRO   A O    
1954 C  CB   . PRO   A 260 ? 0.20633 0.25079 0.29414 -0.00299 0.00528  0.01546  412 PRO   A CB   
1955 C  CG   . PRO   A 260 ? 0.21338 0.26308 0.29672 0.00042  0.00964  0.01412  412 PRO   A CG   
1956 C  CD   . PRO   A 260 ? 0.19546 0.24176 0.26368 0.00181  0.01300  0.00985  412 PRO   A CD   
1957 N  N    . LEU   A 261 ? 0.16004 0.19162 0.22728 -0.00500 0.00481  0.00829  413 LEU   A N    
1958 C  CA   . LEU   A 261 ? 0.16905 0.19617 0.23511 -0.00639 0.00228  0.00514  413 LEU   A CA   
1959 C  C    . LEU   A 261 ? 0.17236 0.20309 0.23608 -0.00853 0.00310  0.00924  413 LEU   A C    
1960 O  O    . LEU   A 261 ? 0.19335 0.22414 0.26528 -0.00991 -0.00042 0.01060  413 LEU   A O    
1961 C  CB   . LEU   A 261 ? 0.17177 0.19258 0.22598 -0.00562 0.00288  -0.00171 413 LEU   A CB   
1962 C  CG   . LEU   A 261 ? 0.19070 0.21004 0.24348 -0.00719 0.00102  -0.00590 413 LEU   A CG   
1963 C  CD1  . LEU   A 261 ? 0.18844 0.20914 0.25447 -0.00677 -0.00319 -0.00885 413 LEU   A CD1  
1964 C  CD2  . LEU   A 261 ? 0.17638 0.19176 0.21617 -0.00795 0.00210  -0.01031 413 LEU   A CD2  
1965 N  N    . VAL   A 262 ? 0.16413 0.19852 0.21756 -0.00859 0.00714  0.01073  414 VAL   A N    
1966 C  CA   . VAL   A 262 ? 0.17512 0.21496 0.22515 -0.01109 0.00764  0.01507  414 VAL   A CA   
1967 C  C    . VAL   A 262 ? 0.19032 0.23727 0.25405 -0.01366 0.00472  0.02458  414 VAL   A C    
1968 O  O    . VAL   A 262 ? 0.20848 0.25614 0.27732 -0.01584 0.00119  0.02845  414 VAL   A O    
1969 C  CB   . VAL   A 262 ? 0.18327 0.22777 0.22021 -0.01044 0.01245  0.01360  414 VAL   A CB   
1970 C  CG1  . VAL   A 262 ? 0.19152 0.24632 0.22563 -0.01368 0.01294  0.01989  414 VAL   A CG1  
1971 C  CG2  . VAL   A 262 ? 0.17564 0.21084 0.20049 -0.00915 0.01327  0.00528  414 VAL   A CG2  
1972 N  N    . LEU   A 263 ? 0.20726 0.25961 0.27878 -0.01371 0.00538  0.02911  415 LEU   A N    
1973 C  CA   . LEU   A 263 ? 0.20094 0.26029 0.28681 -0.01733 0.00192  0.04001  415 LEU   A CA   
1974 C  C    . LEU   A 263 ? 0.20989 0.26081 0.31124 -0.01771 -0.00526 0.03991  415 LEU   A C    
1975 O  O    . LEU   A 263 ? 0.21917 0.27203 0.33164 -0.02076 -0.01016 0.04808  415 LEU   A O    
1976 C  CB   . LEU   A 263 ? 0.18959 0.25719 0.28161 -0.01762 0.00416  0.04429  415 LEU   A CB   
1977 C  CG   . LEU   A 263 ? 0.18813 0.26962 0.26921 -0.01774 0.01091  0.04619  415 LEU   A CG   
1978 C  CD1  . LEU   A 263 ? 0.19433 0.28501 0.28317 -0.01717 0.01340  0.04868  415 LEU   A CD1  
1979 C  CD2  . LEU   A 263 ? 0.16477 0.25790 0.24406 -0.02274 0.01062  0.05627  415 LEU   A CD2  
1980 N  N    . GLU   A 264 ? 0.21036 0.25262 0.31347 -0.01460 -0.00653 0.03057  416 GLU   A N    
1981 C  CA   . GLU   A 264 ? 0.23068 0.26628 0.34867 -0.01407 -0.01320 0.02739  416 GLU   A CA   
1982 C  C    . GLU   A 264 ? 0.24407 0.27716 0.36064 -0.01370 -0.01519 0.02437  416 GLU   A C    
1983 O  O    . GLU   A 264 ? 0.26038 0.29161 0.39253 -0.01424 -0.02148 0.02684  416 GLU   A O    
1984 C  CB   . GLU   A 264 ? 0.24986 0.28001 0.36764 -0.01108 -0.01354 0.01721  416 GLU   A CB   
1985 C  CG   . GLU   A 264 ? 0.26871 0.29410 0.40377 -0.01021 -0.02060 0.01232  416 GLU   A CG   
1986 C  CD   . GLU   A 264 ? 0.28124 0.30386 0.41221 -0.00757 -0.02049 0.00102  416 GLU   A CD   
1987 O  OE1  . GLU   A 264 ? 0.28427 0.30599 0.40853 -0.00595 -0.01985 -0.00764 416 GLU   A OE1  
1988 O  OE2  . GLU   A 264 ? 0.28042 0.30341 0.41474 -0.00755 -0.02109 0.00130  416 GLU   A OE2  
1989 N  N    . VAL   A 265 ? 0.22262 0.25544 0.32246 -0.01274 -0.01063 0.01888  417 VAL   A N    
1990 C  CA   . VAL   A 265 ? 0.23097 0.26277 0.32972 -0.01244 -0.01225 0.01504  417 VAL   A CA   
1991 C  C    . VAL   A 265 ? 0.24474 0.28177 0.34248 -0.01524 -0.01311 0.02414  417 VAL   A C    
1992 O  O    . VAL   A 265 ? 0.25458 0.29174 0.36436 -0.01560 -0.01848 0.02684  417 VAL   A O    
1993 C  CB   . VAL   A 265 ? 0.22754 0.25731 0.30998 -0.01134 -0.00780 0.00600  417 VAL   A CB   
1994 C  CG1  . VAL   A 265 ? 0.24511 0.27634 0.32631 -0.01170 -0.00889 0.00265  417 VAL   A CG1  
1995 C  CG2  . VAL   A 265 ? 0.24236 0.26884 0.32605 -0.00926 -0.00798 -0.00197 417 VAL   A CG2  
1996 N  N    . PHE   A 266 ? 0.24356 0.28583 0.32749 -0.01707 -0.00831 0.02854  418 PHE   A N    
1997 C  CA   . PHE   A 266 ? 0.26934 0.31887 0.35017 -0.02026 -0.00914 0.03691  418 PHE   A CA   
1998 C  C    . PHE   A 266 ? 0.30148 0.35698 0.39609 -0.02348 -0.01339 0.04996  418 PHE   A C    
1999 O  O    . PHE   A 266 ? 0.29188 0.35226 0.39061 -0.02641 -0.01737 0.05849  418 PHE   A O    
2000 C  CB   . PHE   A 266 ? 0.26082 0.31566 0.32197 -0.02109 -0.00283 0.03550  418 PHE   A CB   
2001 C  CG   . PHE   A 266 ? 0.23061 0.28011 0.27892 -0.01982 -0.00053 0.02578  418 PHE   A CG   
2002 C  CD1  . PHE   A 266 ? 0.22149 0.27335 0.25344 -0.02026 0.00391  0.02254  418 PHE   A CD1  
2003 C  CD2  . PHE   A 266 ? 0.22297 0.26612 0.27641 -0.01845 -0.00303 0.01954  418 PHE   A CD2  
2004 C  CE1  . PHE   A 266 ? 0.22416 0.27014 0.24585 -0.02002 0.00501  0.01462  418 PHE   A CE1  
2005 C  CE2  . PHE   A 266 ? 0.23057 0.27051 0.27290 -0.01853 -0.00103 0.01221  418 PHE   A CE2  
2006 C  CZ   . PHE   A 266 ? 0.23047 0.27084 0.25723 -0.01968 0.00259  0.01044  418 PHE   A CZ   
2007 N  N    . GLY   A 267 ? 0.31597 0.37190 0.41839 -0.02362 -0.01320 0.05277  419 GLY   A N    
2008 C  CA   . GLY   A 267 ? 0.33355 0.39485 0.45145 -0.02773 -0.01823 0.06634  419 GLY   A CA   
2009 C  C    . GLY   A 267 ? 0.36603 0.43813 0.48072 -0.03034 -0.01371 0.07321  419 GLY   A C    
2010 O  O    . GLY   A 267 ? 0.35743 0.43577 0.45547 -0.02904 -0.00620 0.06855  419 GLY   A O    
2011 N  N    . ASN   A 268 ? 0.38890 0.46384 0.52102 -0.03406 -0.01866 0.08414  420 ASN   A N    
2012 C  CA   . ASN   A 268 ? 0.40644 0.49369 0.53934 -0.03715 -0.01487 0.09158  420 ASN   A CA   
2013 C  C    . ASN   A 268 ? 0.42231 0.51545 0.56664 -0.04258 -0.02142 0.10789  420 ASN   A C    
2014 O  O    . ASN   A 268 ? 0.43984 0.54294 0.57714 -0.04601 -0.02210 0.11702  420 ASN   A O    
2015 C  CB   . ASN   A 268 ? 0.41674 0.49662 0.55637 -0.03359 -0.01416 0.08318  420 ASN   A CB   
2016 C  CG   . ASN   A 268 ? 0.44513 0.53899 0.58337 -0.03536 -0.00859 0.08778  420 ASN   A CG   
2017 O  OD1  . ASN   A 268 ? 0.46267 0.55301 0.60567 -0.03271 -0.00773 0.08190  420 ASN   A OD1  
2018 N  ND2  . ASN   A 268 ? 0.45168 0.56207 0.58202 -0.03922 -0.00500 0.09725  420 ASN   A ND2  
2019 N  N    . LYS   B 1   ? 0.91890 1.01288 0.98459 -0.00040 0.00554  -0.11035 625 LYS   C N    
2020 C  CA   . LYS   B 1   ? 0.91008 1.00925 0.97320 0.00438  0.00603  -0.10736 625 LYS   C CA   
2021 C  C    . LYS   B 1   ? 0.85756 0.96969 0.92569 0.01022  0.00628  -0.11084 625 LYS   C C    
2022 O  O    . LYS   B 1   ? 0.86345 0.97576 0.93487 0.01344  0.00421  -0.11033 625 LYS   C O    
2023 C  CB   . LYS   B 1   ? 0.94793 1.03689 1.00767 0.00498  0.00372  -0.10099 625 LYS   C CB   
2024 C  CG   . LYS   B 1   ? 0.97970 1.05574 1.03373 -0.00040 0.00350  -0.09680 625 LYS   C CG   
2025 C  CD   . LYS   B 1   ? 0.99822 1.06233 1.05114 -0.00120 0.00056  -0.09207 625 LYS   C CD   
2026 C  CE   . LYS   B 1   ? 1.01526 1.06690 1.06513 -0.00761 0.00010  -0.09029 625 LYS   C CE   
2027 N  NZ   . LYS   B 1   ? 1.02309 1.06351 1.07280 -0.00847 -0.00287 -0.08639 625 LYS   C NZ   
2028 N  N    . ASN   B 2   ? 0.79502 0.91808 0.86379 0.01155  0.00884  -0.11449 626 ASN   C N    
2029 C  CA   . ASN   B 2   ? 0.73454 0.87059 0.80694 0.01739  0.00948  -0.11719 626 ASN   C CA   
2030 C  C    . ASN   B 2   ? 0.65288 0.79097 0.72076 0.02092  0.01004  -0.11275 626 ASN   C C    
2031 O  O    . ASN   B 2   ? 0.65918 0.79342 0.72142 0.01868  0.01132  -0.10979 626 ASN   C O    
2032 C  CB   . ASN   B 2   ? 0.75292 0.89998 0.82815 0.01724  0.01199  -0.12321 626 ASN   C CB   
2033 C  CG   . ASN   B 2   ? 0.77705 0.92158 0.85610 0.01308  0.01170  -0.12752 626 ASN   C CG   
2034 O  OD1  . ASN   B 2   ? 0.78532 0.93508 0.86523 0.01103  0.01376  -0.13157 626 ASN   C OD1  
2035 N  ND2  . ASN   B 2   ? 0.78656 0.92322 0.86800 0.01189  0.00914  -0.12671 626 ASN   C ND2  
2036 N  N    . HIS   B 3   ? 0.55632 0.70040 0.62665 0.02644  0.00905  -0.11224 627 HIS   C N    
2037 C  CA   . HIS   B 3   ? 0.47462 0.62094 0.54110 0.03025  0.00935  -0.10800 627 HIS   C CA   
2038 C  C    . HIS   B 3   ? 0.40531 0.56644 0.47489 0.03559  0.01086  -0.11144 627 HIS   C C    
2039 O  O    . HIS   B 3   ? 0.37771 0.54321 0.44951 0.04051  0.00966  -0.11056 627 HIS   C O    
2040 C  CB   . HIS   B 3   ? 0.45592 0.59421 0.52156 0.03198  0.00655  -0.10301 627 HIS   C CB   
2041 C  CG   . HIS   B 3   ? 0.45502 0.57869 0.51767 0.02687  0.00498  -0.09951 627 HIS   C CG   
2042 N  ND1  . HIS   B 3   ? 0.45854 0.57632 0.52472 0.02390  0.00337  -0.10148 627 HIS   C ND1  
2043 C  CD2  . HIS   B 3   ? 0.45171 0.56548 0.50817 0.02412  0.00480  -0.09427 627 HIS   C CD2  
2044 C  CE1  . HIS   B 3   ? 0.45601 0.56088 0.51833 0.01956  0.00226  -0.09755 627 HIS   C CE1  
2045 N  NE2  . HIS   B 3   ? 0.46246 0.56467 0.51884 0.01958  0.00311  -0.09316 627 HIS   C NE2  
2046 N  N    . PRO   B 4   ? 0.36722 0.53634 0.43683 0.03479  0.01352  -0.11521 628 PRO   C N    
2047 C  CA   . PRO   B 4   ? 0.33329 0.51688 0.40632 0.03971  0.01498  -0.11899 628 PRO   C CA   
2048 C  C    . PRO   B 4   ? 0.31296 0.50120 0.38293 0.04435  0.01545  -0.11546 628 PRO   C C    
2049 O  O    . PRO   B 4   ? 0.30044 0.49868 0.37386 0.04947  0.01550  -0.11733 628 PRO   C O    
2050 C  CB   . PRO   B 4   ? 0.32743 0.51645 0.40036 0.03680  0.01772  -0.12332 628 PRO   C CB   
2051 C  CG   . PRO   B 4   ? 0.34051 0.51888 0.40746 0.03165  0.01819  -0.11976 628 PRO   C CG   
2052 C  CD   . PRO   B 4   ? 0.36219 0.52766 0.42860 0.02946  0.01535  -0.11609 628 PRO   C CD   
2053 N  N    . MET   B 5   ? 0.30503 0.48651 0.36862 0.04276  0.01584  -0.11046 629 MET   C N    
2054 C  CA   . MET   B 5   ? 0.27229 0.45807 0.33289 0.04719  0.01626  -0.10699 629 MET   C CA   
2055 C  C    . MET   B 5   ? 0.35704 0.53903 0.41865 0.05058  0.01354  -0.10337 629 MET   C C    
2056 O  O    . MET   B 5   ? 0.26518 0.45530 0.32842 0.05593  0.01345  -0.10323 629 MET   C O    
2057 C  CB   . MET   B 5   ? 0.31729 0.49715 0.37073 0.04444  0.01755  -0.10285 629 MET   C CB   
2058 C  CG   . MET   B 5   ? 0.33610 0.52203 0.38826 0.04222  0.02058  -0.10627 629 MET   C CG   
2059 S  SD   . MET   B 5   ? 0.35657 0.53404 0.40036 0.03817  0.02196  -0.10151 629 MET   C SD   
2060 C  CE   . MET   B 5   ? 0.36570 0.52852 0.40869 0.03144  0.02040  -0.10056 629 MET   C CE   
2061 N  N    . LEU   B 6   ? 0.27555 0.44532 0.33632 0.04752  0.01132  -0.10049 630 LEU   C N    
2062 C  CA   . LEU   B 6   ? 0.34378 0.50971 0.40617 0.05048  0.00859  -0.09751 630 LEU   C CA   
2063 C  C    . LEU   B 6   ? 0.35401 0.52899 0.42348 0.05424  0.00787  -0.10209 630 LEU   C C    
2064 O  O    . LEU   B 6   ? 0.34940 0.53007 0.42061 0.05942  0.00709  -0.10116 630 LEU   C O    
2065 C  CB   . LEU   B 6   ? 0.35226 0.50348 0.41286 0.04598  0.00644  -0.09425 630 LEU   C CB   
2066 C  CG   . LEU   B 6   ? 0.36637 0.51133 0.42836 0.04803  0.00341  -0.09086 630 LEU   C CG   
2067 C  CD1  . LEU   B 6   ? 0.34804 0.49688 0.40808 0.05324  0.00308  -0.08711 630 LEU   C CD1  
2068 C  CD2  . LEU   B 6   ? 0.35718 0.48702 0.41573 0.04303  0.00178  -0.08689 630 LEU   C CD2  
2069 N  N    . MET   B 7   ? 0.37496 0.55181 0.44859 0.05173  0.00824  -0.10719 631 MET   C N    
2070 C  CA   . MET   B 7   ? 0.38690 0.57236 0.46737 0.05503  0.00763  -0.11188 631 MET   C CA   
2071 C  C    . MET   B 7   ? 0.34135 0.54092 0.42344 0.06039  0.00931  -0.11411 631 MET   C C    
2072 O  O    . MET   B 7   ? 0.33767 0.54341 0.42372 0.06508  0.00824  -0.11504 631 MET   C O    
2073 C  CB   . MET   B 7   ? 0.43760 0.62333 0.52177 0.05117  0.00815  -0.11718 631 MET   C CB   
2074 C  CG   . MET   B 7   ? 0.49833 0.69189 0.58962 0.05420  0.00733  -0.12198 631 MET   C CG   
2075 S  SD   . MET   B 7   ? 0.56874 0.75284 0.66264 0.05465  0.00365  -0.11939 631 MET   C SD   
2076 C  CE   . MET   B 7   ? 0.58169 0.75655 0.67687 0.04785  0.00314  -0.12190 631 MET   C CE   
2077 N  N    . ASN   B 8   ? 0.33161 0.53639 0.41061 0.05982  0.01192  -0.11485 632 ASN   C N    
2078 C  CA   . ASN   B 8   ? 0.33911 0.55749 0.41957 0.06475  0.01365  -0.11710 632 ASN   C CA   
2079 C  C    . ASN   B 8   ? 0.34414 0.56357 0.42237 0.06947  0.01276  -0.11244 632 ASN   C C    
2080 O  O    . ASN   B 8   ? 0.34974 0.57923 0.43121 0.07465  0.01284  -0.11407 632 ASN   C O    
2081 C  CB   . ASN   B 8   ? 0.35710 0.58025 0.43456 0.06275  0.01667  -0.11887 632 ASN   C CB   
2082 C  CG   . ASN   B 8   ? 0.36745 0.60353 0.44521 0.06778  0.01847  -0.12010 632 ASN   C CG   
2083 O  OD1  . ASN   B 8   ? 0.38381 0.61986 0.45701 0.06943  0.01910  -0.11616 632 ASN   C OD1  
2084 N  ND2  . ASN   B 8   ? 0.35876 0.60599 0.44195 0.07030  0.01929  -0.12557 632 ASN   C ND2  
2085 N  N    . LEU   B 9   ? 0.32090 0.53017 0.39359 0.06779  0.01193  -0.10661 633 LEU   C N    
2086 C  CA   . LEU   B 9   ? 0.32729 0.53678 0.39785 0.07214  0.01089  -0.10193 633 LEU   C CA   
2087 C  C    . LEU   B 9   ? 0.33773 0.54525 0.41231 0.07497  0.00810  -0.10111 633 LEU   C C    
2088 O  O    . LEU   B 9   ? 0.31686 0.52806 0.39153 0.07974  0.00731  -0.09868 633 LEU   C O    
2089 C  CB   . LEU   B 9   ? 0.34733 0.54609 0.41085 0.06944  0.01069  -0.09587 633 LEU   C CB   
2090 C  CG   . LEU   B 9   ? 0.34032 0.54222 0.39895 0.06834  0.01340  -0.09529 633 LEU   C CG   
2091 C  CD1  . LEU   B 9   ? 0.31962 0.50914 0.37156 0.06461  0.01300  -0.08966 633 LEU   C CD1  
2092 C  CD2  . LEU   B 9   ? 0.34117 0.55438 0.39980 0.07404  0.01453  -0.09513 633 LEU   C CD2  
2093 N  N    . LEU   B 10  ? 0.36024 0.56198 0.43812 0.07213  0.00659  -0.10302 634 LEU   C N    
2094 C  CA   . LEU   B 10  ? 0.40625 0.60662 0.48842 0.07474  0.00400  -0.10278 634 LEU   C CA   
2095 C  C    . LEU   B 10  ? 0.45061 0.66373 0.53920 0.07892  0.00439  -0.10814 634 LEU   C C    
2096 O  O    . LEU   B 10  ? 0.45749 0.67265 0.54934 0.08282  0.00260  -0.10763 634 LEU   C O    
2097 C  CB   . LEU   B 10  ? 0.40103 0.58981 0.48415 0.07002  0.00214  -0.10257 634 LEU   C CB   
2098 C  CG   . LEU   B 10  ? 0.39872 0.57368 0.47638 0.06708  0.00067  -0.09629 634 LEU   C CG   
2099 C  CD1  . LEU   B 10  ? 0.40730 0.57130 0.48586 0.06191  -0.00082 -0.09663 634 LEU   C CD1  
2100 C  CD2  . LEU   B 10  ? 0.40775 0.58139 0.48497 0.07146  -0.00130 -0.09188 634 LEU   C CD2  
2101 N  N    . LYS   B 11  ? 0.49234 0.71397 0.58275 0.07820  0.00669  -0.11321 635 LYS   C N    
2102 C  CA   . LYS   B 11  ? 0.52808 0.76252 0.62437 0.08206  0.00736  -0.11856 635 LYS   C CA   
2103 C  C    . LYS   B 11  ? 0.53013 0.77470 0.62596 0.08788  0.00822  -0.11752 635 LYS   C C    
2104 O  O    . LYS   B 11  ? 0.53169 0.77793 0.62945 0.09209  0.00656  -0.11582 635 LYS   C O    
2105 C  CB   . LYS   B 11  ? 0.56413 0.80403 0.66206 0.07914  0.00963  -0.12408 635 LYS   C CB   
2106 C  CG   . LYS   B 11  ? 0.60204 0.85343 0.70667 0.08201  0.01005  -0.13023 635 LYS   C CG   
2107 C  CD   . LYS   B 11  ? 0.62899 0.89094 0.73378 0.08208  0.01309  -0.13443 635 LYS   C CD   
2108 C  CE   . LYS   B 11  ? 0.64471 0.91992 0.75564 0.08637  0.01363  -0.13979 635 LYS   C CE   
2109 N  NZ   . LYS   B 11  ? 0.66147 0.93485 0.77801 0.08610  0.01164  -0.14265 635 LYS   C NZ   
2110 C  C10  A A1L74 C .   ? 0.27559 0.31774 0.24139 -0.02534 0.00978  -0.00882 501 A1L74 A C10  
2111 C  C10  B A1L74 C .   ? 0.27704 0.31915 0.24286 -0.02536 0.00975  -0.00882 501 A1L74 A C10  
2112 C  C13  A A1L74 C .   ? 0.30079 0.33262 0.25071 -0.02116 0.01249  -0.02625 501 A1L74 A C13  
2113 C  C13  B A1L74 C .   ? 0.30020 0.33222 0.25002 -0.02113 0.01253  -0.02630 501 A1L74 A C13  
2114 C  C15  A A1L74 C .   ? 0.31003 0.31487 0.24876 -0.02466 0.00551  -0.04280 501 A1L74 A C15  
2115 C  C15  B A1L74 C .   ? 0.31088 0.31603 0.24910 -0.02460 0.00552  -0.04331 501 A1L74 A C15  
2116 C  C20  A A1L74 C .   ? 0.42697 0.39169 0.38732 -0.04204 -0.00642 -0.01269 501 A1L74 A C20  
2117 C  C20  B A1L74 C .   ? 0.42636 0.39180 0.38699 -0.04124 -0.00592 -0.01328 501 A1L74 A C20  
2118 C  C21  A A1L74 C .   ? 0.43681 0.40691 0.39586 -0.04929 -0.00786 -0.00719 501 A1L74 A C21  
2119 C  C21  B A1L74 C .   ? 0.43695 0.40624 0.39611 -0.04861 -0.00780 -0.00771 501 A1L74 A C21  
2120 C  C22  A A1L74 C .   ? 0.43695 0.41273 0.39835 -0.04682 -0.00663 -0.00513 501 A1L74 A C22  
2121 C  C22  B A1L74 C .   ? 0.43804 0.41360 0.39950 -0.04660 -0.00655 -0.00538 501 A1L74 A C22  
2122 C  C24  A A1L74 C .   ? 0.23699 0.31456 0.21766 -0.02084 0.01812  0.00991  501 A1L74 A C24  
2123 C  C24  B A1L74 C .   ? 0.24342 0.32093 0.22413 -0.02077 0.01818  0.00984  501 A1L74 A C24  
2124 C  C26  A A1L74 C .   ? 0.23155 0.29815 0.22447 -0.01861 0.01680  0.01114  501 A1L74 A C26  
2125 C  C26  B A1L74 C .   ? 0.23183 0.29830 0.22472 -0.01854 0.01685  0.01101  501 A1L74 A C26  
2126 C  C28  A A1L74 C .   ? 0.23201 0.28967 0.22260 -0.01411 0.01938  0.00243  501 A1L74 A C28  
2127 C  C28  B A1L74 C .   ? 0.22987 0.28741 0.22023 -0.01400 0.01947  0.00214  501 A1L74 A C28  
2128 C  C01  A A1L74 C .   ? 0.31481 0.31092 0.27873 -0.02875 0.00454  -0.02135 501 A1L74 A C01  
2129 C  C01  B A1L74 C .   ? 0.34782 0.32910 0.29956 -0.03737 -0.00183 -0.02813 501 A1L74 A C01  
2130 C  C02  A A1L74 C .   ? 0.34228 0.32997 0.30271 -0.03284 0.00180  -0.02258 501 A1L74 A C02  
2131 C  C02  B A1L74 C .   ? 0.34157 0.32627 0.29905 -0.03497 0.00035  -0.02400 501 A1L74 A C02  
2132 C  C03  A A1L74 C .   ? 0.33783 0.32099 0.29226 -0.03575 -0.00053 -0.02626 501 A1L74 A C03  
2133 C  C03  B A1L74 C .   ? 0.32813 0.32116 0.28951 -0.03033 0.00347  -0.02261 501 A1L74 A C03  
2134 C  C04  A A1L74 C .   ? 0.34023 0.32835 0.29075 -0.03404 0.00030  -0.02985 501 A1L74 A C04  
2135 C  C04  B A1L74 C .   ? 0.32010 0.31951 0.27877 -0.02854 0.00479  -0.02418 501 A1L74 A C04  
2136 C  C05  A A1L74 C .   ? 0.31687 0.31571 0.26954 -0.03005 0.00365  -0.02794 501 A1L74 A C05  
2137 C  C05  B A1L74 C .   ? 0.32016 0.31795 0.27134 -0.03072 0.00309  -0.02903 501 A1L74 A C05  
2138 C  C06  A A1L74 C .   ? 0.31619 0.31801 0.27629 -0.02766 0.00549  -0.02318 501 A1L74 A C06  
2139 C  C06  B A1L74 C .   ? 0.34219 0.33001 0.29048 -0.03487 -0.00042 -0.03153 501 A1L74 A C06  
2140 C  C08  A A1L74 C .   ? 0.29276 0.31919 0.24431 -0.02541 0.00907  -0.02364 501 A1L74 A C08  
2141 C  C08  B A1L74 C .   ? 0.29508 0.32160 0.24650 -0.02539 0.00909  -0.02372 501 A1L74 A C08  
2142 C  C09  A A1L74 C .   ? 0.28463 0.31730 0.24396 -0.02712 0.00816  -0.01552 501 A1L74 A C09  
2143 C  C09  B A1L74 C .   ? 0.28564 0.31828 0.24487 -0.02714 0.00814  -0.01558 501 A1L74 A C09  
2144 C  C11  A A1L74 C .   ? 0.27529 0.32327 0.23864 -0.02235 0.01324  -0.00991 501 A1L74 A C11  
2145 C  C11  B A1L74 C .   ? 0.27760 0.32555 0.24108 -0.02236 0.01322  -0.00982 501 A1L74 A C11  
2146 C  C12  A A1L74 C .   ? 0.28880 0.33260 0.24401 -0.01984 0.01504  -0.01932 501 A1L74 A C12  
2147 C  C12  B A1L74 C .   ? 0.28969 0.33363 0.24499 -0.01983 0.01507  -0.01922 501 A1L74 A C12  
2148 C  C14  A A1L74 C .   ? 0.30309 0.32196 0.24377 -0.03547 0.00159  -0.03024 501 A1L74 A C14  
2149 C  C14  B A1L74 C .   ? 0.30142 0.32058 0.24177 -0.03546 0.00160  -0.03041 501 A1L74 A C14  
2150 C  C18  A A1L74 C .   ? 0.38579 0.36014 0.34764 -0.03486 -0.00121 -0.01932 501 A1L74 A C18  
2151 C  C18  B A1L74 C .   ? 0.38339 0.36079 0.34590 -0.03470 -0.00048 -0.01921 501 A1L74 A C18  
2152 C  C19  A A1L74 C .   ? 0.40540 0.38225 0.36778 -0.04018 -0.00250 -0.01513 501 A1L74 A C19  
2153 C  C19  B A1L74 C .   ? 0.40568 0.38392 0.36850 -0.03984 -0.00207 -0.01528 501 A1L74 A C19  
2154 C  C23  A A1L74 C .   ? 0.25394 0.32164 0.22307 -0.01975 0.01819  -0.00178 501 A1L74 A C23  
2155 C  C23  B A1L74 C .   ? 0.25615 0.32375 0.22531 -0.01969 0.01822  -0.00186 501 A1L74 A C23  
2156 C  C25  A A1L74 C .   ? 0.24160 0.33471 0.21935 -0.01968 0.02292  0.01065  501 A1L74 A C25  
2157 C  C25  B A1L74 C .   ? 0.24224 0.33536 0.22001 -0.01965 0.02295  0.01062  501 A1L74 A C25  
2158 C  C27  A A1L74 C .   ? 0.23347 0.33656 0.22301 -0.02190 0.02246  0.02307  501 A1L74 A C27  
2159 C  C27  B A1L74 C .   ? 0.23212 0.33515 0.22184 -0.02193 0.02240  0.02320  501 A1L74 A C27  
2160 C  C31  A A1L74 C .   ? 0.35511 0.32892 0.30791 -0.04124 -0.00429 -0.02559 501 A1L74 A C31  
2161 C  C31  B A1L74 C .   ? 0.32016 0.31620 0.28891 -0.02797 0.00490  -0.01908 501 A1L74 A C31  
2162 C  C32  A A1L74 C .   ? 0.26648 0.31331 0.24341 -0.02671 0.00735  -0.00063 501 A1L74 A C32  
2163 C  C32  B A1L74 C .   ? 0.26456 0.31123 0.24155 -0.02673 0.00730  -0.00068 501 A1L74 A C32  
2164 C  C35  A A1L74 C .   ? 0.35467 0.33848 0.29841 -0.03699 -0.00276 -0.03577 501 A1L74 A C35  
2165 C  C35  B A1L74 C .   ? 0.30417 0.31369 0.26814 -0.02482 0.00766  -0.02034 501 A1L74 A C35  
2166 C  C36  A A1L74 C .   ? 0.27705 0.30692 0.23978 -0.03097 0.00496  -0.01400 501 A1L74 A C36  
2167 C  C36  B A1L74 C .   ? 0.27574 0.30558 0.23831 -0.03104 0.00492  -0.01408 501 A1L74 A C36  
2168 O  O16  A A1L74 C .   ? 0.26803 0.32623 0.23887 -0.02197 0.01434  -0.00163 501 A1L74 A O16  
2169 O  O16  B A1L74 C .   ? 0.26628 0.32447 0.23739 -0.02197 0.01431  -0.00146 501 A1L74 A O16  
2170 O  O17  A A1L74 C .   ? 0.35214 0.33718 0.31512 -0.03512 0.00082  -0.01965 501 A1L74 A O17  
2171 O  O17  B A1L74 C .   ? 0.35983 0.34093 0.31932 -0.03802 -0.00101 -0.02080 501 A1L74 A O17  
2172 O  O29  A A1L74 C .   ? 0.23447 0.31789 0.21846 -0.02513 0.01425  0.01866  501 A1L74 A O29  
2173 O  O29  B A1L74 C .   ? 0.23332 0.31685 0.21719 -0.02514 0.01427  0.01864  501 A1L74 A O29  
2174 O  O30  A A1L74 C .   ? 0.43252 0.41758 0.39807 -0.04256 -0.00309 -0.00793 501 A1L74 A O30  
2175 O  O30  B A1L74 C .   ? 0.44220 0.41319 0.40190 -0.04937 -0.00983 -0.00067 501 A1L74 A O30  
2176 O  O33  A A1L74 C .   ? 0.43881 0.40995 0.39848 -0.04946 -0.00987 -0.00050 501 A1L74 A O33  
2177 O  O33  B A1L74 C .   ? 0.43042 0.41566 0.39601 -0.04255 -0.00301 -0.00803 501 A1L74 A O33  
2178 O  O34  A A1L74 C .   ? 0.40620 0.39246 0.37355 -0.03792 -0.00004 -0.01399 501 A1L74 A O34  
2179 O  O34  B A1L74 C .   ? 0.39960 0.38678 0.36739 -0.03774 0.00018  -0.01401 501 A1L74 A O34  
2180 SI SI07 A A1L74 C .   ? 0.30078 0.31207 0.24614 -0.02898 0.00505  -0.03127 501 A1L74 A SI07 
2181 SI SI07 B A1L74 C .   ? 0.30877 0.32025 0.25373 -0.02894 0.00507  -0.03158 501 A1L74 A SI07 
# 
