data_9M1B
# 
_entry.id   9M1B 
# 
_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   9M1B         pdb_00009m1b 10.2210/pdb9m1b/pdb 
WWPDB D_1300056793 ?            ?                   
# 
_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                        9M1B 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ito.str@tmd.ac.jp 
_pdbx_contact_author.name_first         Nobutoshi 
_pdbx_contact_author.name_last          Ito 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0839-0384 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Thilakarathne, N.M.H.N.' 1 ? 
'Hanazono, Y.'            2 ? 
'Ito, N.'                 3 ? 
'Kagechika, H.'           4 ? 
'Fujii, S.'               5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_id_ASTM           BMECEP 
_citation.journal_id_CSD            1200 
_citation.journal_id_ISSN           1464-3391 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                118261 
_citation.page_last                 ? 
_citation.title                     
;Structure-activity relationship and crystallographic analyses of non-secosteroidal vitamin D receptor ligands bearing diphenylsilane core as a hydrophobic pharmacophore
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2025.118261 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mudiyanselage, H.N.T.N.' 1 ? 
primary 'Misawa, T.'              2 ? 
primary 'Ochiai, K.'              3 ? 
primary 'Demizu, Y.'              4 ? 
primary 'Hanazono, Y.'            5 ? 
primary 'Ito, N.'                 6 ? 
primary 'Fujii, S.'               7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Vitamin D3 receptor' 30595.037 1   ? ? ? ? 
2 polymer     syn 'Mediator of RNA polymerase II transcription subunit 1' 1570.898  1   ? ? ? ? 
3 non-polymer syn 
'(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)-3-methyl-phenyl]-dipropyl-silyl]-2-methyl-phenoxy]-4-oxidanyl-pentanoic acid' 
544.795   1   ? ? ? ? 
4 water       nat water 18.015    105 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'VDR,1,25-dihydroxyvitamin D3 receptor,Nuclear receptor subfamily 1 group I member 1' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GSHMGSPNSPLKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGSVTLDLSPLSMLPHLADLVSY
SIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLRSNQSFTMDDMSWDCGSQDYKYDVTDVSKAGHTLELIEPLIKF
QVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAKLVEAIQDRLSNTLQTYIRCRHPPPGSHQLYAKMIQKLADLRSLNEE
HSKQYRSLSFQPENSMKLTPLVLEVFGNEIS
;
;GSHMGSPNSPLKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGSVTLDLSPLSMLPHLADLVSY
SIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLRSNQSFTMDDMSWDCGSQDYKYDVTDVSKAGHTLELIEPLIKF
QVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAKLVEAIQDRLSNTLQTYIRCRHPPPGSHQLYAKMIQKLADLRSLNEE
HSKQYRSLSFQPENSMKLTPLVLEVFGNEIS
;
A ? 
2 'polypeptide(L)' no no KNHPMLMNLLKDN KNHPMLMNLLKDN C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)-3-methyl-phenyl]-dipropyl-silyl]-2-methyl-phenoxy]-4-oxidanyl-pentanoic acid' 
A1L79 
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 
A1L79 non-polymer         . 
'(4~{S})-5-[4-[[4-(2-ethyl-2-oxidanyl-butoxy)-3-methyl-phenyl]-dipropyl-silyl]-2-methyl-phenoxy]-4-oxidanyl-pentanoic acid' ? 
'C31 H48 O6 Si'  544.795 
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 ?   ?   ?   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 ?   ?   ?   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        A1L79 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L79 
_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 A1L79 1   501 501 A1L79 LIG A . 
D 4 HOH   1   601 34  HOH   HOH A . 
D 4 HOH   2   602 75  HOH   HOH A . 
D 4 HOH   3   603 99  HOH   HOH A . 
D 4 HOH   4   604 16  HOH   HOH A . 
D 4 HOH   5   605 7   HOH   HOH A . 
D 4 HOH   6   606 12  HOH   HOH A . 
D 4 HOH   7   607 102 HOH   HOH A . 
D 4 HOH   8   608 62  HOH   HOH A . 
D 4 HOH   9   609 113 HOH   HOH A . 
D 4 HOH   10  610 110 HOH   HOH A . 
D 4 HOH   11  611 44  HOH   HOH A . 
D 4 HOH   12  612 55  HOH   HOH A . 
D 4 HOH   13  613 98  HOH   HOH A . 
D 4 HOH   14  614 43  HOH   HOH A . 
D 4 HOH   15  615 9   HOH   HOH A . 
D 4 HOH   16  616 84  HOH   HOH A . 
D 4 HOH   17  617 85  HOH   HOH A . 
D 4 HOH   18  618 29  HOH   HOH A . 
D 4 HOH   19  619 68  HOH   HOH A . 
D 4 HOH   20  620 52  HOH   HOH A . 
D 4 HOH   21  621 57  HOH   HOH A . 
D 4 HOH   22  622 53  HOH   HOH A . 
D 4 HOH   23  623 10  HOH   HOH A . 
D 4 HOH   24  624 3   HOH   HOH A . 
D 4 HOH   25  625 4   HOH   HOH A . 
D 4 HOH   26  626 49  HOH   HOH A . 
D 4 HOH   27  627 11  HOH   HOH A . 
D 4 HOH   28  628 105 HOH   HOH A . 
D 4 HOH   29  629 107 HOH   HOH A . 
D 4 HOH   30  630 22  HOH   HOH A . 
D 4 HOH   31  631 30  HOH   HOH A . 
D 4 HOH   32  632 65  HOH   HOH A . 
D 4 HOH   33  633 73  HOH   HOH A . 
D 4 HOH   34  634 70  HOH   HOH A . 
D 4 HOH   35  635 23  HOH   HOH A . 
D 4 HOH   36  636 101 HOH   HOH A . 
D 4 HOH   37  637 35  HOH   HOH A . 
D 4 HOH   38  638 15  HOH   HOH A . 
D 4 HOH   39  639 28  HOH   HOH A . 
D 4 HOH   40  640 21  HOH   HOH A . 
D 4 HOH   41  641 1   HOH   HOH A . 
D 4 HOH   42  642 26  HOH   HOH A . 
D 4 HOH   43  643 5   HOH   HOH A . 
D 4 HOH   44  644 13  HOH   HOH A . 
D 4 HOH   45  645 106 HOH   HOH A . 
D 4 HOH   46  646 6   HOH   HOH A . 
D 4 HOH   47  647 24  HOH   HOH A . 
D 4 HOH   48  648 111 HOH   HOH A . 
D 4 HOH   49  649 2   HOH   HOH A . 
D 4 HOH   50  650 51  HOH   HOH A . 
D 4 HOH   51  651 76  HOH   HOH A . 
D 4 HOH   52  652 71  HOH   HOH A . 
D 4 HOH   53  653 91  HOH   HOH A . 
D 4 HOH   54  654 90  HOH   HOH A . 
D 4 HOH   55  655 79  HOH   HOH A . 
D 4 HOH   56  656 8   HOH   HOH A . 
D 4 HOH   57  657 47  HOH   HOH A . 
D 4 HOH   58  658 109 HOH   HOH A . 
D 4 HOH   59  659 72  HOH   HOH A . 
D 4 HOH   60  660 20  HOH   HOH A . 
D 4 HOH   61  661 36  HOH   HOH A . 
D 4 HOH   62  662 80  HOH   HOH A . 
D 4 HOH   63  663 108 HOH   HOH A . 
D 4 HOH   64  664 19  HOH   HOH A . 
D 4 HOH   65  665 88  HOH   HOH A . 
D 4 HOH   66  666 81  HOH   HOH A . 
D 4 HOH   67  667 14  HOH   HOH A . 
D 4 HOH   68  668 38  HOH   HOH A . 
D 4 HOH   69  669 40  HOH   HOH A . 
D 4 HOH   70  670 59  HOH   HOH A . 
D 4 HOH   71  671 87  HOH   HOH A . 
D 4 HOH   72  672 46  HOH   HOH A . 
D 4 HOH   73  673 32  HOH   HOH A . 
D 4 HOH   74  674 92  HOH   HOH A . 
D 4 HOH   75  675 41  HOH   HOH A . 
D 4 HOH   76  676 42  HOH   HOH A . 
D 4 HOH   77  677 89  HOH   HOH A . 
D 4 HOH   78  678 115 HOH   HOH A . 
D 4 HOH   79  679 25  HOH   HOH A . 
D 4 HOH   80  680 56  HOH   HOH A . 
D 4 HOH   81  681 100 HOH   HOH A . 
D 4 HOH   82  682 83  HOH   HOH A . 
D 4 HOH   83  683 95  HOH   HOH A . 
D 4 HOH   84  684 93  HOH   HOH A . 
D 4 HOH   85  685 50  HOH   HOH A . 
D 4 HOH   86  686 104 HOH   HOH A . 
D 4 HOH   87  687 103 HOH   HOH A . 
D 4 HOH   88  688 114 HOH   HOH A . 
D 4 HOH   89  689 37  HOH   HOH A . 
D 4 HOH   90  690 116 HOH   HOH A . 
D 4 HOH   91  691 31  HOH   HOH A . 
D 4 HOH   92  692 45  HOH   HOH A . 
D 4 HOH   93  693 74  HOH   HOH A . 
D 4 HOH   94  694 77  HOH   HOH A . 
D 4 HOH   95  695 112 HOH   HOH A . 
D 4 HOH   96  696 39  HOH   HOH A . 
D 4 HOH   97  697 67  HOH   HOH A . 
D 4 HOH   98  698 97  HOH   HOH A . 
D 4 HOH   99  699 64  HOH   HOH A . 
D 4 HOH   100 700 61  HOH   HOH A . 
D 4 HOH   101 701 78  HOH   HOH A . 
D 4 HOH   102 702 96  HOH   HOH A . 
E 4 HOH   1   701 18  HOH   HOH C . 
E 4 HOH   2   702 82  HOH   HOH C . 
E 4 HOH   3   703 66  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                   96.375 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9M1B 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     154.790 
_cell.length_a_esd                 ? 
_cell.length_b                     42.370 
_cell.length_b_esd                 ? 
_cell.length_c                     42.280 
_cell.length_c_esd                 ? 
_cell.volume                       275576.722 
_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                         9M1B 
_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                   9M1B 
_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             2.14 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.57 
_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, Cesium chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-22 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SPRING-8 BEAMLINE BL45XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL45XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9M1B 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.77 
_reflns.d_resolution_low                               42.03 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     26417 
_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                           98.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.8 
_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                              0.107 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.77 
_reflns_shell.d_res_low                                     1.88 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.13 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4277 
_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                                  0.717 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  3.60 
_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                               46.54 
_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                                 9M1B 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.77 
_refine.ls_d_res_low                             42.02 
_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                     26300 
_refine.ls_number_reflns_R_free                  1319 
_refine.ls_number_reflns_R_work                  24981 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.96 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1943 
_refine.ls_R_factor_R_free                       0.2127 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1932 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      2ZLC 
_refine.pdbx_stereochemistry_target_values       'CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.4076 
_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                            0.2998 
_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                       1.77 
_refine_hist.d_res_low                        42.02 
_refine_hist.number_atoms_solvent             105 
_refine_hist.number_atoms_total               2143 
_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        2000 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         38 
_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' ? 0.0044  ? 2233 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6751  ? 3042 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0373  ? 337  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0047  ? 394  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 24.4628 ? 868  ? 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' 1.77 1.84  . . 144 2699 95.63 . . . . 0.4381 . . . . . . . . . . . . . . . 0.4846 
'X-RAY DIFFRACTION' 1.84 1.92  . . 144 2734 96.97 . . . . 0.3414 . . . . . . . . . . . . . . . 0.3707 
'X-RAY DIFFRACTION' 1.92 2.03  . . 143 2708 97.54 . . . . 0.2581 . . . . . . . . . . . . . . . 0.2994 
'X-RAY DIFFRACTION' 2.03 2.15  . . 147 2754 97.28 . . . . 0.2209 . . . . . . . . . . . . . . . 0.2643 
'X-RAY DIFFRACTION' 2.15 2.32  . . 144 2754 98.14 . . . . 0.1960 . . . . . . . . . . . . . . . 0.2210 
'X-RAY DIFFRACTION' 2.32 2.55  . . 147 2783 98.49 . . . . 0.1971 . . . . . . . . . . . . . . . 0.2181 
'X-RAY DIFFRACTION' 2.55 2.92  . . 146 2789 98.76 . . . . 0.1863 . . . . . . . . . . . . . . . 0.2183 
'X-RAY DIFFRACTION' 2.92 3.68  . . 150 2837 99.24 . . . . 0.1831 . . . . . . . . . . . . . . . 0.2108 
'X-RAY DIFFRACTION' 3.68 42.02 . . 154 2923 99.48 . . . . 0.1664 . . . . . . . . . . . . . . . 0.1748 
# 
_struct.entry_id                     9M1B 
_struct.title                        'Vitamin D receptor complex with a diphenydipropylsilane 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        9M1B 
_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 9M1B A 11 ? 271 ? P13053 116 ? 423 ? 116 423 
2 2 9M1B 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 9M1B GLY A 1  ? UNP P13053 ?   ?   'expression tag' 106 1  
1 9M1B SER A 2  ? UNP P13053 ?   ?   'expression tag' 107 2  
1 9M1B HIS A 3  ? UNP P13053 ?   ?   'expression tag' 108 3  
1 9M1B MET A 4  ? UNP P13053 ?   ?   'expression tag' 109 4  
1 9M1B GLY A 5  ? UNP P13053 ?   ?   'expression tag' 110 5  
1 9M1B SER A 6  ? UNP P13053 ?   ?   'expression tag' 111 6  
1 9M1B PRO A 7  ? UNP P13053 ?   ?   'expression tag' 112 7  
1 9M1B ASN A 8  ? UNP P13053 ?   ?   'expression tag' 113 8  
1 9M1B SER A 9  ? UNP P13053 ?   ?   'expression tag' 114 9  
1 9M1B PRO A 10 ? UNP P13053 ?   ?   'expression tag' 115 10 
1 9M1B ?   A ?  ? UNP P13053 TYR 166 deletion         ?   11 
1 9M1B ?   A ?  ? UNP P13053 SER 167 deletion         ?   12 
1 9M1B ?   A ?  ? UNP P13053 PRO 168 deletion         ?   13 
1 9M1B ?   A ?  ? UNP P13053 ARG 169 deletion         ?   14 
1 9M1B ?   A ?  ? UNP P13053 PRO 170 deletion         ?   15 
1 9M1B ?   A ?  ? UNP P13053 THR 171 deletion         ?   16 
1 9M1B ?   A ?  ? UNP P13053 LEU 172 deletion         ?   17 
1 9M1B ?   A ?  ? UNP P13053 SER 173 deletion         ?   18 
1 9M1B ?   A ?  ? UNP P13053 PHE 174 deletion         ?   19 
1 9M1B ?   A ?  ? UNP P13053 SER 175 deletion         ?   20 
1 9M1B ?   A ?  ? UNP P13053 GLY 176 deletion         ?   21 
1 9M1B ?   A ?  ? UNP P13053 ASN 177 deletion         ?   22 
1 9M1B ?   A ?  ? UNP P13053 SER 178 deletion         ?   23 
1 9M1B ?   A ?  ? UNP P13053 SER 179 deletion         ?   24 
1 9M1B ?   A ?  ? UNP P13053 SER 180 deletion         ?   25 
1 9M1B ?   A ?  ? UNP P13053 SER 181 deletion         ?   26 
1 9M1B ?   A ?  ? UNP P13053 SER 182 deletion         ?   27 
1 9M1B ?   A ?  ? UNP P13053 SER 183 deletion         ?   28 
1 9M1B ?   A ?  ? UNP P13053 ASP 184 deletion         ?   29 
1 9M1B ?   A ?  ? UNP P13053 LEU 185 deletion         ?   30 
1 9M1B ?   A ?  ? UNP P13053 TYR 186 deletion         ?   31 
1 9M1B ?   A ?  ? UNP P13053 THR 187 deletion         ?   32 
1 9M1B ?   A ?  ? UNP P13053 THR 188 deletion         ?   33 
1 9M1B ?   A ?  ? UNP P13053 SER 189 deletion         ?   34 
1 9M1B ?   A ?  ? UNP P13053 LEU 190 deletion         ?   35 
1 9M1B ?   A ?  ? UNP P13053 ASP 191 deletion         ?   36 
1 9M1B ?   A ?  ? UNP P13053 MET 192 deletion         ?   37 
1 9M1B ?   A ?  ? UNP P13053 MET 193 deletion         ?   38 
1 9M1B ?   A ?  ? UNP P13053 GLU 194 deletion         ?   39 
1 9M1B ?   A ?  ? UNP P13053 PRO 195 deletion         ?   40 
1 9M1B ?   A ?  ? UNP P13053 SER 196 deletion         ?   41 
1 9M1B ?   A ?  ? UNP P13053 GLY 197 deletion         ?   42 
1 9M1B ?   A ?  ? UNP P13053 PHE 198 deletion         ?   43 
1 9M1B ?   A ?  ? UNP P13053 SER 199 deletion         ?   44 
1 9M1B ?   A ?  ? UNP P13053 ASN 200 deletion         ?   45 
1 9M1B ?   A ?  ? UNP P13053 LEU 201 deletion         ?   46 
1 9M1B ?   A ?  ? UNP P13053 ASP 202 deletion         ?   47 
1 9M1B ?   A ?  ? UNP P13053 LEU 203 deletion         ?   48 
1 9M1B ?   A ?  ? UNP P13053 ASN 204 deletion         ?   49 
1 9M1B ?   A ?  ? UNP P13053 GLY 205 deletion         ?   50 
1 9M1B ?   A ?  ? UNP P13053 GLU 206 deletion         ?   51 
1 9M1B ?   A ?  ? UNP P13053 ASP 207 deletion         ?   52 
1 9M1B ?   A ?  ? UNP P13053 SER 208 deletion         ?   53 
1 9M1B ?   A ?  ? UNP P13053 ASP 209 deletion         ?   54 
1 9M1B ?   A ?  ? UNP P13053 ASP 210 deletion         ?   55 
1 9M1B ?   A ?  ? UNP P13053 PRO 211 deletion         ?   56 
1 9M1B ?   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)' 2340  ? 
1 MORE         -13   ? 
1 'SSA (A^2)'  11810 ? 
# 
_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  ? SER A 119 ? THR A 251 SER A 271 1 ? 21 
HELX_P HELX_P6  AA6 ASP A 140 ? LYS A 146 ? ASP A 292 LYS A 298 1 ? 7  
HELX_P HELX_P7  AA7 THR A 150 ? LEU A 167 ? THR A 302 LEU A 319 1 ? 18 
HELX_P HELX_P8  AA8 HIS A 170 ? VAL A 183 ? HIS A 322 VAL A 335 1 ? 14 
HELX_P HELX_P9  AA9 ASP A 192 ? HIS A 215 ? ASP A 344 HIS A 367 1 ? 24 
HELX_P HELX_P10 AB1 GLN A 222 ? GLN A 251 ? GLN A 374 GLN A 403 1 ? 30 
HELX_P HELX_P11 AB2 GLN A 251 ? MET A 256 ? GLN A 403 MET A 408 1 ? 6  
HELX_P HELX_P12 AB3 THR A 259 ? GLY A 267 ? THR A 411 GLY A 419 1 ? 9  
HELX_P HELX_P13 AB4 HIS B 3   ? 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       3.24 
# 
_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                   9M1B 
_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 ASP A 279 ? ? -145.30 22.13   
2 1 ASP A 292 ? ? -125.79 -165.36 
3 1 ASP A 292 ? ? -125.79 -163.92 
# 
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 19.1242170205 0.337223680962 19.4622935777 0.263673596843 ? -0.0320256294141 ? -0.0227030556129 ? 
0.29794015995  ? -0.0234137612716 ? 0.240906171757 ? 4.70506397332 ? 0.753283329433  ? 0.28389094594  ? 1.69192284715 ? 
-0.140232910466 ? 2.00409601879 ? 0.0580130121784 ? -0.120430594087 ? -0.0511164971959 ? 0.0395183108274 ? -0.0167872917632  ? 
-0.0473195197713 ? -0.120320188018 ? 0.116246348014  ? -0.0422343318978 ? 
2 'X-RAY DIFFRACTION' ? refined 5.84989753005 -9.98792915802 10.1868279832 0.477876091983 ? -0.0406502564025 ? -0.0154752403481 ? 
0.630936214523 ? -0.122041689876  ? 0.61708906769  ? 8.8390917381  ? 0.0469703568474 ? 0.936503060418 ? 4.27307989026 ? 
0.833069078705  ? 5.38592162903 ? 0.0596211164911 ? 0.413049621703  ? -1.00188606484   ? -0.301894453482 ? -0.00956721948211 ? 
0.135347858536   ? 0.699649199129  ? -0.312181990182 ? -0.0628132152256 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 'Chain A' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 'Chain C' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 106 ? A GLY 1   
2  1 Y 1 A SER 107 ? A SER 2   
3  1 Y 1 A HIS 108 ? A HIS 3   
4  1 Y 1 A MET 109 ? A MET 4   
5  1 Y 1 A GLY 110 ? A GLY 5   
6  1 Y 1 A SER 111 ? A SER 6   
7  1 Y 1 A PRO 112 ? A PRO 7   
8  1 Y 1 A ASN 113 ? A ASN 8   
9  1 Y 1 A SER 114 ? A SER 9   
10 1 Y 1 A PRO 115 ? A PRO 10  
11 1 Y 1 A LEU 116 ? A LEU 11  
12 1 Y 1 A LYS 117 ? A LYS 12  
13 1 Y 1 A ASP 118 ? A ASP 13  
14 1 Y 1 A SER 119 ? A SER 14  
15 1 Y 1 A LEU 120 ? A LEU 15  
16 1 Y 1 A ARG 121 ? A ARG 16  
17 1 Y 1 A PRO 122 ? A PRO 17  
18 1 Y 1 A ASP 207 ? A ASP 55  
19 1 Y 1 A GLY 208 ? A GLY 56  
20 1 Y 1 A SER 209 ? A SER 57  
21 1 Y 1 A THR 210 ? A THR 58  
22 1 Y 1 A GLY 211 ? A GLY 59  
23 1 Y 1 A SER 212 ? A SER 60  
24 1 Y 1 A VAL 213 ? A VAL 61  
25 1 Y 1 A THR 214 ? A THR 62  
26 1 Y 1 A LEU 215 ? A LEU 63  
27 1 Y 1 A ASP 216 ? A ASP 64  
28 1 Y 1 A LEU 217 ? A LEU 65  
29 1 Y 1 A SER 218 ? A SER 66  
30 1 Y 1 A GLU 421 ? A GLU 269 
31 1 Y 1 A ILE 422 ? A ILE 270 
32 1 Y 1 A SER 423 ? A SER 271 
33 1 Y 1 C LYS 625 ? B LYS 1   
34 1 Y 1 C ASP 636 ? B ASP 12  
35 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 
A1L79 C10  C  N N 1   
A1L79 C13  C  Y N 2   
A1L79 C15  C  Y N 3   
A1L79 C20  C  N N 4   
A1L79 C21  C  N N 5   
A1L79 C22  C  N N 6   
A1L79 C26  C  N S 7   
A1L79 C28  C  N N 8   
A1L79 C01  C  Y N 9   
A1L79 C02  C  Y N 10  
A1L79 C03  C  Y N 11  
A1L79 C04  C  Y N 12  
A1L79 C05  C  Y N 13  
A1L79 C06  C  Y N 14  
A1L79 C09  C  Y N 15  
A1L79 C11  C  N N 16  
A1L79 C12  C  Y N 17  
A1L79 C14  C  Y N 18  
A1L79 C16  C  Y N 19  
A1L79 C18  C  N N 20  
A1L79 C19  C  N N 21  
A1L79 C23  C  N N 22  
A1L79 C25  C  N N 23  
A1L79 C29  C  N N 24  
A1L79 C30  C  N N 25  
A1L79 C33  C  N N 26  
A1L79 C34  C  N N 27  
A1L79 C35  C  N N 28  
A1L79 C36  C  N N 29  
A1L79 C37  C  N N 30  
A1L79 C38  C  N N 31  
A1L79 O07  O  N N 32  
A1L79 O17  O  N N 33  
A1L79 O24  O  N N 34  
A1L79 O27  O  N N 35  
A1L79 O31  O  N N 36  
A1L79 O32  O  N N 37  
A1L79 SI08 SI N N 38  
A1L79 H102 H  N N 39  
A1L79 H101 H  N N 40  
A1L79 H151 H  N N 41  
A1L79 H202 H  N N 42  
A1L79 H201 H  N N 43  
A1L79 H213 H  N N 44  
A1L79 H211 H  N N 45  
A1L79 H212 H  N N 46  
A1L79 H221 H  N N 47  
A1L79 H222 H  N N 48  
A1L79 H261 H  N N 49  
A1L79 H282 H  N N 50  
A1L79 H281 H  N N 51  
A1L79 H011 H  N N 52  
A1L79 H041 H  N N 53  
A1L79 H061 H  N N 54  
A1L79 H111 H  N N 55  
A1L79 H112 H  N N 56  
A1L79 H121 H  N N 57  
A1L79 H161 H  N N 58  
A1L79 H181 H  N N 59  
A1L79 H182 H  N N 60  
A1L79 H231 H  N N 61  
A1L79 H233 H  N N 62  
A1L79 H232 H  N N 63  
A1L79 H252 H  N N 64  
A1L79 H251 H  N N 65  
A1L79 H292 H  N N 66  
A1L79 H291 H  N N 67  
A1L79 H331 H  N N 68  
A1L79 H332 H  N N 69  
A1L79 H333 H  N N 70  
A1L79 H342 H  N N 71  
A1L79 H341 H  N N 72  
A1L79 H343 H  N N 73  
A1L79 H352 H  N N 74  
A1L79 H351 H  N N 75  
A1L79 H363 H  N N 76  
A1L79 H362 H  N N 77  
A1L79 H361 H  N N 78  
A1L79 H372 H  N N 79  
A1L79 H371 H  N N 80  
A1L79 H383 H  N N 81  
A1L79 H381 H  N N 82  
A1L79 H382 H  N N 83  
A1L79 H241 H  N N 84  
A1L79 H271 H  N N 85  
A1L79 H1   H  N N 86  
ALA   N    N  N N 87  
ALA   CA   C  N S 88  
ALA   C    C  N N 89  
ALA   O    O  N N 90  
ALA   CB   C  N N 91  
ALA   OXT  O  N N 92  
ALA   H    H  N N 93  
ALA   H2   H  N N 94  
ALA   HA   H  N N 95  
ALA   HB1  H  N N 96  
ALA   HB2  H  N N 97  
ALA   HB3  H  N N 98  
ALA   HXT  H  N N 99  
ARG   N    N  N N 100 
ARG   CA   C  N S 101 
ARG   C    C  N N 102 
ARG   O    O  N N 103 
ARG   CB   C  N N 104 
ARG   CG   C  N N 105 
ARG   CD   C  N N 106 
ARG   NE   N  N N 107 
ARG   CZ   C  N N 108 
ARG   NH1  N  N N 109 
ARG   NH2  N  N N 110 
ARG   OXT  O  N N 111 
ARG   H    H  N N 112 
ARG   H2   H  N N 113 
ARG   HA   H  N N 114 
ARG   HB2  H  N N 115 
ARG   HB3  H  N N 116 
ARG   HG2  H  N N 117 
ARG   HG3  H  N N 118 
ARG   HD2  H  N N 119 
ARG   HD3  H  N N 120 
ARG   HE   H  N N 121 
ARG   HH11 H  N N 122 
ARG   HH12 H  N N 123 
ARG   HH21 H  N N 124 
ARG   HH22 H  N N 125 
ARG   HXT  H  N N 126 
ASN   N    N  N N 127 
ASN   CA   C  N S 128 
ASN   C    C  N N 129 
ASN   O    O  N N 130 
ASN   CB   C  N N 131 
ASN   CG   C  N N 132 
ASN   OD1  O  N N 133 
ASN   ND2  N  N N 134 
ASN   OXT  O  N N 135 
ASN   H    H  N N 136 
ASN   H2   H  N N 137 
ASN   HA   H  N N 138 
ASN   HB2  H  N N 139 
ASN   HB3  H  N N 140 
ASN   HD21 H  N N 141 
ASN   HD22 H  N N 142 
ASN   HXT  H  N N 143 
ASP   N    N  N N 144 
ASP   CA   C  N S 145 
ASP   C    C  N N 146 
ASP   O    O  N N 147 
ASP   CB   C  N N 148 
ASP   CG   C  N N 149 
ASP   OD1  O  N N 150 
ASP   OD2  O  N N 151 
ASP   OXT  O  N N 152 
ASP   H    H  N N 153 
ASP   H2   H  N N 154 
ASP   HA   H  N N 155 
ASP   HB2  H  N N 156 
ASP   HB3  H  N N 157 
ASP   HD2  H  N N 158 
ASP   HXT  H  N N 159 
CYS   N    N  N N 160 
CYS   CA   C  N R 161 
CYS   C    C  N N 162 
CYS   O    O  N N 163 
CYS   CB   C  N N 164 
CYS   SG   S  N N 165 
CYS   OXT  O  N N 166 
CYS   H    H  N N 167 
CYS   H2   H  N N 168 
CYS   HA   H  N N 169 
CYS   HB2  H  N N 170 
CYS   HB3  H  N N 171 
CYS   HG   H  N N 172 
CYS   HXT  H  N N 173 
GLN   N    N  N N 174 
GLN   CA   C  N S 175 
GLN   C    C  N N 176 
GLN   O    O  N N 177 
GLN   CB   C  N N 178 
GLN   CG   C  N N 179 
GLN   CD   C  N N 180 
GLN   OE1  O  N N 181 
GLN   NE2  N  N N 182 
GLN   OXT  O  N N 183 
GLN   H    H  N N 184 
GLN   H2   H  N N 185 
GLN   HA   H  N N 186 
GLN   HB2  H  N N 187 
GLN   HB3  H  N N 188 
GLN   HG2  H  N N 189 
GLN   HG3  H  N N 190 
GLN   HE21 H  N N 191 
GLN   HE22 H  N N 192 
GLN   HXT  H  N N 193 
GLU   N    N  N N 194 
GLU   CA   C  N S 195 
GLU   C    C  N N 196 
GLU   O    O  N N 197 
GLU   CB   C  N N 198 
GLU   CG   C  N N 199 
GLU   CD   C  N N 200 
GLU   OE1  O  N N 201 
GLU   OE2  O  N N 202 
GLU   OXT  O  N N 203 
GLU   H    H  N N 204 
GLU   H2   H  N N 205 
GLU   HA   H  N N 206 
GLU   HB2  H  N N 207 
GLU   HB3  H  N N 208 
GLU   HG2  H  N N 209 
GLU   HG3  H  N N 210 
GLU   HE2  H  N N 211 
GLU   HXT  H  N N 212 
GLY   N    N  N N 213 
GLY   CA   C  N N 214 
GLY   C    C  N N 215 
GLY   O    O  N N 216 
GLY   OXT  O  N N 217 
GLY   H    H  N N 218 
GLY   H2   H  N N 219 
GLY   HA2  H  N N 220 
GLY   HA3  H  N N 221 
GLY   HXT  H  N N 222 
HIS   N    N  N N 223 
HIS   CA   C  N S 224 
HIS   C    C  N N 225 
HIS   O    O  N N 226 
HIS   CB   C  N N 227 
HIS   CG   C  Y N 228 
HIS   ND1  N  Y N 229 
HIS   CD2  C  Y N 230 
HIS   CE1  C  Y N 231 
HIS   NE2  N  Y N 232 
HIS   OXT  O  N N 233 
HIS   H    H  N N 234 
HIS   H2   H  N N 235 
HIS   HA   H  N N 236 
HIS   HB2  H  N N 237 
HIS   HB3  H  N N 238 
HIS   HD1  H  N N 239 
HIS   HD2  H  N N 240 
HIS   HE1  H  N N 241 
HIS   HE2  H  N N 242 
HIS   HXT  H  N N 243 
HOH   O    O  N N 244 
HOH   H1   H  N N 245 
HOH   H2   H  N N 246 
ILE   N    N  N N 247 
ILE   CA   C  N S 248 
ILE   C    C  N N 249 
ILE   O    O  N N 250 
ILE   CB   C  N S 251 
ILE   CG1  C  N N 252 
ILE   CG2  C  N N 253 
ILE   CD1  C  N N 254 
ILE   OXT  O  N N 255 
ILE   H    H  N N 256 
ILE   H2   H  N N 257 
ILE   HA   H  N N 258 
ILE   HB   H  N N 259 
ILE   HG12 H  N N 260 
ILE   HG13 H  N N 261 
ILE   HG21 H  N N 262 
ILE   HG22 H  N N 263 
ILE   HG23 H  N N 264 
ILE   HD11 H  N N 265 
ILE   HD12 H  N N 266 
ILE   HD13 H  N N 267 
ILE   HXT  H  N N 268 
LEU   N    N  N N 269 
LEU   CA   C  N S 270 
LEU   C    C  N N 271 
LEU   O    O  N N 272 
LEU   CB   C  N N 273 
LEU   CG   C  N N 274 
LEU   CD1  C  N N 275 
LEU   CD2  C  N N 276 
LEU   OXT  O  N N 277 
LEU   H    H  N N 278 
LEU   H2   H  N N 279 
LEU   HA   H  N N 280 
LEU   HB2  H  N N 281 
LEU   HB3  H  N N 282 
LEU   HG   H  N N 283 
LEU   HD11 H  N N 284 
LEU   HD12 H  N N 285 
LEU   HD13 H  N N 286 
LEU   HD21 H  N N 287 
LEU   HD22 H  N N 288 
LEU   HD23 H  N N 289 
LEU   HXT  H  N N 290 
LYS   N    N  N N 291 
LYS   CA   C  N S 292 
LYS   C    C  N N 293 
LYS   O    O  N N 294 
LYS   CB   C  N N 295 
LYS   CG   C  N N 296 
LYS   CD   C  N N 297 
LYS   CE   C  N N 298 
LYS   NZ   N  N N 299 
LYS   OXT  O  N N 300 
LYS   H    H  N N 301 
LYS   H2   H  N N 302 
LYS   HA   H  N N 303 
LYS   HB2  H  N N 304 
LYS   HB3  H  N N 305 
LYS   HG2  H  N N 306 
LYS   HG3  H  N N 307 
LYS   HD2  H  N N 308 
LYS   HD3  H  N N 309 
LYS   HE2  H  N N 310 
LYS   HE3  H  N N 311 
LYS   HZ1  H  N N 312 
LYS   HZ2  H  N N 313 
LYS   HZ3  H  N N 314 
LYS   HXT  H  N N 315 
MET   N    N  N N 316 
MET   CA   C  N S 317 
MET   C    C  N N 318 
MET   O    O  N N 319 
MET   CB   C  N N 320 
MET   CG   C  N N 321 
MET   SD   S  N N 322 
MET   CE   C  N N 323 
MET   OXT  O  N N 324 
MET   H    H  N N 325 
MET   H2   H  N N 326 
MET   HA   H  N N 327 
MET   HB2  H  N N 328 
MET   HB3  H  N N 329 
MET   HG2  H  N N 330 
MET   HG3  H  N N 331 
MET   HE1  H  N N 332 
MET   HE2  H  N N 333 
MET   HE3  H  N N 334 
MET   HXT  H  N N 335 
PHE   N    N  N N 336 
PHE   CA   C  N S 337 
PHE   C    C  N N 338 
PHE   O    O  N N 339 
PHE   CB   C  N N 340 
PHE   CG   C  Y N 341 
PHE   CD1  C  Y N 342 
PHE   CD2  C  Y N 343 
PHE   CE1  C  Y N 344 
PHE   CE2  C  Y N 345 
PHE   CZ   C  Y N 346 
PHE   OXT  O  N N 347 
PHE   H    H  N N 348 
PHE   H2   H  N N 349 
PHE   HA   H  N N 350 
PHE   HB2  H  N N 351 
PHE   HB3  H  N N 352 
PHE   HD1  H  N N 353 
PHE   HD2  H  N N 354 
PHE   HE1  H  N N 355 
PHE   HE2  H  N N 356 
PHE   HZ   H  N N 357 
PHE   HXT  H  N N 358 
PRO   N    N  N N 359 
PRO   CA   C  N S 360 
PRO   C    C  N N 361 
PRO   O    O  N N 362 
PRO   CB   C  N N 363 
PRO   CG   C  N N 364 
PRO   CD   C  N N 365 
PRO   OXT  O  N N 366 
PRO   H    H  N N 367 
PRO   HA   H  N N 368 
PRO   HB2  H  N N 369 
PRO   HB3  H  N N 370 
PRO   HG2  H  N N 371 
PRO   HG3  H  N N 372 
PRO   HD2  H  N N 373 
PRO   HD3  H  N N 374 
PRO   HXT  H  N N 375 
SER   N    N  N N 376 
SER   CA   C  N S 377 
SER   C    C  N N 378 
SER   O    O  N N 379 
SER   CB   C  N N 380 
SER   OG   O  N N 381 
SER   OXT  O  N N 382 
SER   H    H  N N 383 
SER   H2   H  N N 384 
SER   HA   H  N N 385 
SER   HB2  H  N N 386 
SER   HB3  H  N N 387 
SER   HG   H  N N 388 
SER   HXT  H  N N 389 
THR   N    N  N N 390 
THR   CA   C  N S 391 
THR   C    C  N N 392 
THR   O    O  N N 393 
THR   CB   C  N R 394 
THR   OG1  O  N N 395 
THR   CG2  C  N N 396 
THR   OXT  O  N N 397 
THR   H    H  N N 398 
THR   H2   H  N N 399 
THR   HA   H  N N 400 
THR   HB   H  N N 401 
THR   HG1  H  N N 402 
THR   HG21 H  N N 403 
THR   HG22 H  N N 404 
THR   HG23 H  N N 405 
THR   HXT  H  N N 406 
TRP   N    N  N N 407 
TRP   CA   C  N S 408 
TRP   C    C  N N 409 
TRP   O    O  N N 410 
TRP   CB   C  N N 411 
TRP   CG   C  Y N 412 
TRP   CD1  C  Y N 413 
TRP   CD2  C  Y N 414 
TRP   NE1  N  Y N 415 
TRP   CE2  C  Y N 416 
TRP   CE3  C  Y N 417 
TRP   CZ2  C  Y N 418 
TRP   CZ3  C  Y N 419 
TRP   CH2  C  Y N 420 
TRP   OXT  O  N N 421 
TRP   H    H  N N 422 
TRP   H2   H  N N 423 
TRP   HA   H  N N 424 
TRP   HB2  H  N N 425 
TRP   HB3  H  N N 426 
TRP   HD1  H  N N 427 
TRP   HE1  H  N N 428 
TRP   HE3  H  N N 429 
TRP   HZ2  H  N N 430 
TRP   HZ3  H  N N 431 
TRP   HH2  H  N N 432 
TRP   HXT  H  N N 433 
TYR   N    N  N N 434 
TYR   CA   C  N S 435 
TYR   C    C  N N 436 
TYR   O    O  N N 437 
TYR   CB   C  N N 438 
TYR   CG   C  Y N 439 
TYR   CD1  C  Y N 440 
TYR   CD2  C  Y N 441 
TYR   CE1  C  Y N 442 
TYR   CE2  C  Y N 443 
TYR   CZ   C  Y N 444 
TYR   OH   O  N N 445 
TYR   OXT  O  N N 446 
TYR   H    H  N N 447 
TYR   H2   H  N N 448 
TYR   HA   H  N N 449 
TYR   HB2  H  N N 450 
TYR   HB3  H  N N 451 
TYR   HD1  H  N N 452 
TYR   HD2  H  N N 453 
TYR   HE1  H  N N 454 
TYR   HE2  H  N N 455 
TYR   HH   H  N N 456 
TYR   HXT  H  N N 457 
VAL   N    N  N N 458 
VAL   CA   C  N S 459 
VAL   C    C  N N 460 
VAL   O    O  N N 461 
VAL   CB   C  N N 462 
VAL   CG1  C  N N 463 
VAL   CG2  C  N N 464 
VAL   OXT  O  N N 465 
VAL   H    H  N N 466 
VAL   H2   H  N N 467 
VAL   HA   H  N N 468 
VAL   HB   H  N N 469 
VAL   HG11 H  N N 470 
VAL   HG12 H  N N 471 
VAL   HG13 H  N N 472 
VAL   HG21 H  N N 473 
VAL   HG22 H  N N 474 
VAL   HG23 H  N N 475 
VAL   HXT  H  N N 476 
# 
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 
A1L79 C01  C02  doub Y N 1   
A1L79 C01  C06  sing Y N 2   
A1L79 C02  C03  sing Y N 3   
A1L79 C02  O07  sing N N 4   
A1L79 C03  C04  doub Y N 5   
A1L79 C03  C33  sing N N 6   
A1L79 C04  C05  sing Y N 7   
A1L79 C05  C06  doub Y N 8   
A1L79 C05  SI08 sing N N 9   
A1L79 O07  C25  sing N N 10  
A1L79 SI08 C09  sing N N 11  
A1L79 SI08 C10  sing N N 12  
A1L79 SI08 C11  sing N N 13  
A1L79 C09  C12  doub Y N 14  
A1L79 C09  C16  sing Y N 15  
A1L79 C10  C37  sing N N 16  
A1L79 C11  C35  sing N N 17  
A1L79 C12  C13  sing Y N 18  
A1L79 C13  C14  doub Y N 19  
A1L79 C13  C34  sing N N 20  
A1L79 C14  C15  sing Y N 21  
A1L79 C14  O17  sing N N 22  
A1L79 C15  C16  doub Y N 23  
A1L79 O17  C18  sing N N 24  
A1L79 C18  C19  sing N N 25  
A1L79 C19  C20  sing N N 26  
A1L79 C19  C22  sing N N 27  
A1L79 C19  O24  sing N N 28  
A1L79 C20  C21  sing N N 29  
A1L79 C22  C23  sing N N 30  
A1L79 C25  C26  sing N N 31  
A1L79 C26  O27  sing N N 32  
A1L79 C26  C28  sing N N 33  
A1L79 C28  C29  sing N N 34  
A1L79 C29  C30  sing N N 35  
A1L79 C30  O31  doub N N 36  
A1L79 C30  O32  sing N N 37  
A1L79 C35  C36  sing N N 38  
A1L79 C37  C38  sing N N 39  
A1L79 C10  H102 sing N N 40  
A1L79 C10  H101 sing N N 41  
A1L79 C15  H151 sing N N 42  
A1L79 C20  H202 sing N N 43  
A1L79 C20  H201 sing N N 44  
A1L79 C21  H213 sing N N 45  
A1L79 C21  H211 sing N N 46  
A1L79 C21  H212 sing N N 47  
A1L79 C22  H221 sing N N 48  
A1L79 C22  H222 sing N N 49  
A1L79 C26  H261 sing N N 50  
A1L79 C28  H282 sing N N 51  
A1L79 C28  H281 sing N N 52  
A1L79 C01  H011 sing N N 53  
A1L79 C04  H041 sing N N 54  
A1L79 C06  H061 sing N N 55  
A1L79 C11  H111 sing N N 56  
A1L79 C11  H112 sing N N 57  
A1L79 C12  H121 sing N N 58  
A1L79 C16  H161 sing N N 59  
A1L79 C18  H181 sing N N 60  
A1L79 C18  H182 sing N N 61  
A1L79 C23  H231 sing N N 62  
A1L79 C23  H233 sing N N 63  
A1L79 C23  H232 sing N N 64  
A1L79 C25  H252 sing N N 65  
A1L79 C25  H251 sing N N 66  
A1L79 C29  H292 sing N N 67  
A1L79 C29  H291 sing N N 68  
A1L79 C33  H331 sing N N 69  
A1L79 C33  H332 sing N N 70  
A1L79 C33  H333 sing N N 71  
A1L79 C34  H342 sing N N 72  
A1L79 C34  H341 sing N N 73  
A1L79 C34  H343 sing N N 74  
A1L79 C35  H352 sing N N 75  
A1L79 C35  H351 sing N N 76  
A1L79 C36  H363 sing N N 77  
A1L79 C36  H362 sing N N 78  
A1L79 C36  H361 sing N N 79  
A1L79 C37  H372 sing N N 80  
A1L79 C37  H371 sing N N 81  
A1L79 C38  H383 sing N N 82  
A1L79 C38  H381 sing N N 83  
A1L79 C38  H382 sing N N 84  
A1L79 O24  H241 sing N N 85  
A1L79 O27  H271 sing N N 86  
A1L79 O32  H1   sing N N 87  
ALA   N    CA   sing N N 88  
ALA   N    H    sing N N 89  
ALA   N    H2   sing N N 90  
ALA   CA   C    sing N N 91  
ALA   CA   CB   sing N N 92  
ALA   CA   HA   sing N N 93  
ALA   C    O    doub N N 94  
ALA   C    OXT  sing N N 95  
ALA   CB   HB1  sing N N 96  
ALA   CB   HB2  sing N N 97  
ALA   CB   HB3  sing N N 98  
ALA   OXT  HXT  sing N N 99  
ARG   N    CA   sing N N 100 
ARG   N    H    sing N N 101 
ARG   N    H2   sing N N 102 
ARG   CA   C    sing N N 103 
ARG   CA   CB   sing N N 104 
ARG   CA   HA   sing N N 105 
ARG   C    O    doub N N 106 
ARG   C    OXT  sing N N 107 
ARG   CB   CG   sing N N 108 
ARG   CB   HB2  sing N N 109 
ARG   CB   HB3  sing N N 110 
ARG   CG   CD   sing N N 111 
ARG   CG   HG2  sing N N 112 
ARG   CG   HG3  sing N N 113 
ARG   CD   NE   sing N N 114 
ARG   CD   HD2  sing N N 115 
ARG   CD   HD3  sing N N 116 
ARG   NE   CZ   sing N N 117 
ARG   NE   HE   sing N N 118 
ARG   CZ   NH1  sing N N 119 
ARG   CZ   NH2  doub N N 120 
ARG   NH1  HH11 sing N N 121 
ARG   NH1  HH12 sing N N 122 
ARG   NH2  HH21 sing N N 123 
ARG   NH2  HH22 sing N N 124 
ARG   OXT  HXT  sing N N 125 
ASN   N    CA   sing N N 126 
ASN   N    H    sing N N 127 
ASN   N    H2   sing N N 128 
ASN   CA   C    sing N N 129 
ASN   CA   CB   sing N N 130 
ASN   CA   HA   sing N N 131 
ASN   C    O    doub N N 132 
ASN   C    OXT  sing N N 133 
ASN   CB   CG   sing N N 134 
ASN   CB   HB2  sing N N 135 
ASN   CB   HB3  sing N N 136 
ASN   CG   OD1  doub N N 137 
ASN   CG   ND2  sing N N 138 
ASN   ND2  HD21 sing N N 139 
ASN   ND2  HD22 sing N N 140 
ASN   OXT  HXT  sing N N 141 
ASP   N    CA   sing N N 142 
ASP   N    H    sing N N 143 
ASP   N    H2   sing N N 144 
ASP   CA   C    sing N N 145 
ASP   CA   CB   sing N N 146 
ASP   CA   HA   sing N N 147 
ASP   C    O    doub N N 148 
ASP   C    OXT  sing N N 149 
ASP   CB   CG   sing N N 150 
ASP   CB   HB2  sing N N 151 
ASP   CB   HB3  sing N N 152 
ASP   CG   OD1  doub N N 153 
ASP   CG   OD2  sing N N 154 
ASP   OD2  HD2  sing N N 155 
ASP   OXT  HXT  sing N N 156 
CYS   N    CA   sing N N 157 
CYS   N    H    sing N N 158 
CYS   N    H2   sing N N 159 
CYS   CA   C    sing N N 160 
CYS   CA   CB   sing N N 161 
CYS   CA   HA   sing N N 162 
CYS   C    O    doub N N 163 
CYS   C    OXT  sing N N 164 
CYS   CB   SG   sing N N 165 
CYS   CB   HB2  sing N N 166 
CYS   CB   HB3  sing N N 167 
CYS   SG   HG   sing N N 168 
CYS   OXT  HXT  sing N N 169 
GLN   N    CA   sing N N 170 
GLN   N    H    sing N N 171 
GLN   N    H2   sing N N 172 
GLN   CA   C    sing N N 173 
GLN   CA   CB   sing N N 174 
GLN   CA   HA   sing N N 175 
GLN   C    O    doub N N 176 
GLN   C    OXT  sing N N 177 
GLN   CB   CG   sing N N 178 
GLN   CB   HB2  sing N N 179 
GLN   CB   HB3  sing N N 180 
GLN   CG   CD   sing N N 181 
GLN   CG   HG2  sing N N 182 
GLN   CG   HG3  sing N N 183 
GLN   CD   OE1  doub N N 184 
GLN   CD   NE2  sing N N 185 
GLN   NE2  HE21 sing N N 186 
GLN   NE2  HE22 sing N N 187 
GLN   OXT  HXT  sing N N 188 
GLU   N    CA   sing N N 189 
GLU   N    H    sing N N 190 
GLU   N    H2   sing N N 191 
GLU   CA   C    sing N N 192 
GLU   CA   CB   sing N N 193 
GLU   CA   HA   sing N N 194 
GLU   C    O    doub N N 195 
GLU   C    OXT  sing N N 196 
GLU   CB   CG   sing N N 197 
GLU   CB   HB2  sing N N 198 
GLU   CB   HB3  sing N N 199 
GLU   CG   CD   sing N N 200 
GLU   CG   HG2  sing N N 201 
GLU   CG   HG3  sing N N 202 
GLU   CD   OE1  doub N N 203 
GLU   CD   OE2  sing N N 204 
GLU   OE2  HE2  sing N N 205 
GLU   OXT  HXT  sing N N 206 
GLY   N    CA   sing N N 207 
GLY   N    H    sing N N 208 
GLY   N    H2   sing N N 209 
GLY   CA   C    sing N N 210 
GLY   CA   HA2  sing N N 211 
GLY   CA   HA3  sing N N 212 
GLY   C    O    doub N N 213 
GLY   C    OXT  sing N N 214 
GLY   OXT  HXT  sing N N 215 
HIS   N    CA   sing N N 216 
HIS   N    H    sing N N 217 
HIS   N    H2   sing N N 218 
HIS   CA   C    sing N N 219 
HIS   CA   CB   sing N N 220 
HIS   CA   HA   sing N N 221 
HIS   C    O    doub N N 222 
HIS   C    OXT  sing N N 223 
HIS   CB   CG   sing N N 224 
HIS   CB   HB2  sing N N 225 
HIS   CB   HB3  sing N N 226 
HIS   CG   ND1  sing Y N 227 
HIS   CG   CD2  doub Y N 228 
HIS   ND1  CE1  doub Y N 229 
HIS   ND1  HD1  sing N N 230 
HIS   CD2  NE2  sing Y N 231 
HIS   CD2  HD2  sing N N 232 
HIS   CE1  NE2  sing Y N 233 
HIS   CE1  HE1  sing N N 234 
HIS   NE2  HE2  sing N N 235 
HIS   OXT  HXT  sing N N 236 
HOH   O    H1   sing N N 237 
HOH   O    H2   sing N N 238 
ILE   N    CA   sing N N 239 
ILE   N    H    sing N N 240 
ILE   N    H2   sing N N 241 
ILE   CA   C    sing N N 242 
ILE   CA   CB   sing N N 243 
ILE   CA   HA   sing N N 244 
ILE   C    O    doub N N 245 
ILE   C    OXT  sing N N 246 
ILE   CB   CG1  sing N N 247 
ILE   CB   CG2  sing N N 248 
ILE   CB   HB   sing N N 249 
ILE   CG1  CD1  sing N N 250 
ILE   CG1  HG12 sing N N 251 
ILE   CG1  HG13 sing N N 252 
ILE   CG2  HG21 sing N N 253 
ILE   CG2  HG22 sing N N 254 
ILE   CG2  HG23 sing N N 255 
ILE   CD1  HD11 sing N N 256 
ILE   CD1  HD12 sing N N 257 
ILE   CD1  HD13 sing N N 258 
ILE   OXT  HXT  sing N N 259 
LEU   N    CA   sing N N 260 
LEU   N    H    sing N N 261 
LEU   N    H2   sing N N 262 
LEU   CA   C    sing N N 263 
LEU   CA   CB   sing N N 264 
LEU   CA   HA   sing N N 265 
LEU   C    O    doub N N 266 
LEU   C    OXT  sing N N 267 
LEU   CB   CG   sing N N 268 
LEU   CB   HB2  sing N N 269 
LEU   CB   HB3  sing N N 270 
LEU   CG   CD1  sing N N 271 
LEU   CG   CD2  sing N N 272 
LEU   CG   HG   sing N N 273 
LEU   CD1  HD11 sing N N 274 
LEU   CD1  HD12 sing N N 275 
LEU   CD1  HD13 sing N N 276 
LEU   CD2  HD21 sing N N 277 
LEU   CD2  HD22 sing N N 278 
LEU   CD2  HD23 sing N N 279 
LEU   OXT  HXT  sing N N 280 
LYS   N    CA   sing N N 281 
LYS   N    H    sing N N 282 
LYS   N    H2   sing N N 283 
LYS   CA   C    sing N N 284 
LYS   CA   CB   sing N N 285 
LYS   CA   HA   sing N N 286 
LYS   C    O    doub N N 287 
LYS   C    OXT  sing N N 288 
LYS   CB   CG   sing N N 289 
LYS   CB   HB2  sing N N 290 
LYS   CB   HB3  sing N N 291 
LYS   CG   CD   sing N N 292 
LYS   CG   HG2  sing N N 293 
LYS   CG   HG3  sing N N 294 
LYS   CD   CE   sing N N 295 
LYS   CD   HD2  sing N N 296 
LYS   CD   HD3  sing N N 297 
LYS   CE   NZ   sing N N 298 
LYS   CE   HE2  sing N N 299 
LYS   CE   HE3  sing N N 300 
LYS   NZ   HZ1  sing N N 301 
LYS   NZ   HZ2  sing N N 302 
LYS   NZ   HZ3  sing N N 303 
LYS   OXT  HXT  sing N N 304 
MET   N    CA   sing N N 305 
MET   N    H    sing N N 306 
MET   N    H2   sing N N 307 
MET   CA   C    sing N N 308 
MET   CA   CB   sing N N 309 
MET   CA   HA   sing N N 310 
MET   C    O    doub N N 311 
MET   C    OXT  sing N N 312 
MET   CB   CG   sing N N 313 
MET   CB   HB2  sing N N 314 
MET   CB   HB3  sing N N 315 
MET   CG   SD   sing N N 316 
MET   CG   HG2  sing N N 317 
MET   CG   HG3  sing N N 318 
MET   SD   CE   sing N N 319 
MET   CE   HE1  sing N N 320 
MET   CE   HE2  sing N N 321 
MET   CE   HE3  sing N N 322 
MET   OXT  HXT  sing N N 323 
PHE   N    CA   sing N N 324 
PHE   N    H    sing N N 325 
PHE   N    H2   sing N N 326 
PHE   CA   C    sing N N 327 
PHE   CA   CB   sing N N 328 
PHE   CA   HA   sing N N 329 
PHE   C    O    doub N N 330 
PHE   C    OXT  sing N N 331 
PHE   CB   CG   sing N N 332 
PHE   CB   HB2  sing N N 333 
PHE   CB   HB3  sing N N 334 
PHE   CG   CD1  doub Y N 335 
PHE   CG   CD2  sing Y N 336 
PHE   CD1  CE1  sing Y N 337 
PHE   CD1  HD1  sing N N 338 
PHE   CD2  CE2  doub Y N 339 
PHE   CD2  HD2  sing N N 340 
PHE   CE1  CZ   doub Y N 341 
PHE   CE1  HE1  sing N N 342 
PHE   CE2  CZ   sing Y N 343 
PHE   CE2  HE2  sing N N 344 
PHE   CZ   HZ   sing N N 345 
PHE   OXT  HXT  sing N N 346 
PRO   N    CA   sing N N 347 
PRO   N    CD   sing N N 348 
PRO   N    H    sing N N 349 
PRO   CA   C    sing N N 350 
PRO   CA   CB   sing N N 351 
PRO   CA   HA   sing N N 352 
PRO   C    O    doub N N 353 
PRO   C    OXT  sing N N 354 
PRO   CB   CG   sing N N 355 
PRO   CB   HB2  sing N N 356 
PRO   CB   HB3  sing N N 357 
PRO   CG   CD   sing N N 358 
PRO   CG   HG2  sing N N 359 
PRO   CG   HG3  sing N N 360 
PRO   CD   HD2  sing N N 361 
PRO   CD   HD3  sing N N 362 
PRO   OXT  HXT  sing N N 363 
SER   N    CA   sing N N 364 
SER   N    H    sing N N 365 
SER   N    H2   sing N N 366 
SER   CA   C    sing N N 367 
SER   CA   CB   sing N N 368 
SER   CA   HA   sing N N 369 
SER   C    O    doub N N 370 
SER   C    OXT  sing N N 371 
SER   CB   OG   sing N N 372 
SER   CB   HB2  sing N N 373 
SER   CB   HB3  sing N N 374 
SER   OG   HG   sing N N 375 
SER   OXT  HXT  sing N N 376 
THR   N    CA   sing N N 377 
THR   N    H    sing N N 378 
THR   N    H2   sing N N 379 
THR   CA   C    sing N N 380 
THR   CA   CB   sing N N 381 
THR   CA   HA   sing N N 382 
THR   C    O    doub N N 383 
THR   C    OXT  sing N N 384 
THR   CB   OG1  sing N N 385 
THR   CB   CG2  sing N N 386 
THR   CB   HB   sing N N 387 
THR   OG1  HG1  sing N N 388 
THR   CG2  HG21 sing N N 389 
THR   CG2  HG22 sing N N 390 
THR   CG2  HG23 sing N N 391 
THR   OXT  HXT  sing N N 392 
TRP   N    CA   sing N N 393 
TRP   N    H    sing N N 394 
TRP   N    H2   sing N N 395 
TRP   CA   C    sing N N 396 
TRP   CA   CB   sing N N 397 
TRP   CA   HA   sing N N 398 
TRP   C    O    doub N N 399 
TRP   C    OXT  sing N N 400 
TRP   CB   CG   sing N N 401 
TRP   CB   HB2  sing N N 402 
TRP   CB   HB3  sing N N 403 
TRP   CG   CD1  doub Y N 404 
TRP   CG   CD2  sing Y N 405 
TRP   CD1  NE1  sing Y N 406 
TRP   CD1  HD1  sing N N 407 
TRP   CD2  CE2  doub Y N 408 
TRP   CD2  CE3  sing Y N 409 
TRP   NE1  CE2  sing Y N 410 
TRP   NE1  HE1  sing N N 411 
TRP   CE2  CZ2  sing Y N 412 
TRP   CE3  CZ3  doub Y N 413 
TRP   CE3  HE3  sing N N 414 
TRP   CZ2  CH2  doub Y N 415 
TRP   CZ2  HZ2  sing N N 416 
TRP   CZ3  CH2  sing Y N 417 
TRP   CZ3  HZ3  sing N N 418 
TRP   CH2  HH2  sing N N 419 
TRP   OXT  HXT  sing N N 420 
TYR   N    CA   sing N N 421 
TYR   N    H    sing N N 422 
TYR   N    H2   sing N N 423 
TYR   CA   C    sing N N 424 
TYR   CA   CB   sing N N 425 
TYR   CA   HA   sing N N 426 
TYR   C    O    doub N N 427 
TYR   C    OXT  sing N N 428 
TYR   CB   CG   sing N N 429 
TYR   CB   HB2  sing N N 430 
TYR   CB   HB3  sing N N 431 
TYR   CG   CD1  doub Y N 432 
TYR   CG   CD2  sing Y N 433 
TYR   CD1  CE1  sing Y N 434 
TYR   CD1  HD1  sing N N 435 
TYR   CD2  CE2  doub Y N 436 
TYR   CD2  HD2  sing N N 437 
TYR   CE1  CZ   doub Y N 438 
TYR   CE1  HE1  sing N N 439 
TYR   CE2  CZ   sing Y N 440 
TYR   CE2  HE2  sing N N 441 
TYR   CZ   OH   sing N N 442 
TYR   OH   HH   sing N N 443 
TYR   OXT  HXT  sing N N 444 
VAL   N    CA   sing N N 445 
VAL   N    H    sing N N 446 
VAL   N    H2   sing N N 447 
VAL   CA   C    sing N N 448 
VAL   CA   CB   sing N N 449 
VAL   CA   HA   sing N N 450 
VAL   C    O    doub N N 451 
VAL   C    OXT  sing N N 452 
VAL   CB   CG1  sing N N 453 
VAL   CB   CG2  sing N N 454 
VAL   CB   HB   sing N N 455 
VAL   CG1  HG11 sing N N 456 
VAL   CG1  HG12 sing N N 457 
VAL   CG1  HG13 sing N N 458 
VAL   CG2  HG21 sing N N 459 
VAL   CG2  HG22 sing N N 460 
VAL   CG2  HG23 sing N N 461 
VAL   OXT  HXT  sing N N 462 
# 
_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                    9M1B 
_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]   0.006460 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000722 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023602 
_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]   0.023799 
_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    A LYS   A 1 18  ? 43.38700 -1.37200  2.04000  0.590 70.68237  ?  123 LYS   A N    1 
ATOM   2    N  N    B LYS   A 1 18  ? 43.33600 -1.31200  1.91000  0.410 71.26927  ?  123 LYS   A N    1 
ATOM   3    C  CA   A LYS   A 1 18  ? 42.85500 -2.18800  3.12400  0.590 70.94426  ?  123 LYS   A CA   1 
ATOM   4    C  CA   B LYS   A 1 18  ? 42.86800 -2.16200  2.99900  0.410 71.20594  ?  123 LYS   A CA   1 
ATOM   5    C  C    A LYS   A 1 18  ? 41.32900 -2.19500  3.10300  0.590 68.98038  ?  123 LYS   A C    1 
ATOM   6    C  C    B LYS   A 1 18  ? 41.34500 -2.19400  3.04600  0.410 69.11651  ?  123 LYS   A C    1 
ATOM   7    O  O    A LYS   A 1 18  ? 40.70500 -3.24200  3.27500  0.590 69.60040  ?  123 LYS   A O    1 
ATOM   8    O  O    B LYS   A 1 18  ? 40.74000 -3.25100  3.22500  0.410 69.46051  ?  123 LYS   A O    1 
ATOM   9    C  CB   A LYS   A 1 18  ? 43.36200 -1.67900  4.47500  0.590 71.95804  ?  123 LYS   A CB   1 
ATOM   10   C  CB   B LYS   A 1 18  ? 43.42900 -1.67800  4.33800  0.410 72.21587  ?  123 LYS   A CB   1 
ATOM   11   C  CG   A LYS   A 1 18  ? 44.24000 -2.65500  5.25500  0.590 74.63824  ?  123 LYS   A CG   1 
ATOM   12   C  CG   B LYS   A 1 18  ? 43.90100 -2.79000  5.27000  0.410 74.08113  ?  123 LYS   A CG   1 
ATOM   13   C  CD   A LYS   A 1 18  ? 44.25800 -4.04700  4.64200  0.590 76.90318  ?  123 LYS   A CD   1 
ATOM   14   C  CD   B LYS   A 1 18  ? 44.21000 -4.07700  4.51600  0.410 76.84232  ?  123 LYS   A CD   1 
ATOM   15   C  CE   A LYS   A 1 18  ? 45.65200 -4.65400  4.70300  0.590 79.62085  ?  123 LYS   A CE   1 
ATOM   16   C  CE   B LYS   A 1 18  ? 43.26700 -5.19900  4.92300  0.410 74.12474  ?  123 LYS   A CE   1 
ATOM   17   N  NZ   A LYS   A 1 18  ? 46.39500 -4.21700  5.91800  0.590 78.97035  ?  123 LYS   A NZ   1 
ATOM   18   N  NZ   B LYS   A 1 18  ? 43.06800 -6.18100  3.82000  0.410 75.59876  ?  123 LYS   A NZ   1 
ATOM   19   N  N    . LEU   A 1 19  ? 40.73200 -1.02400  2.89100  1.000 67.81351  ?  124 LEU   A N    1 
ATOM   20   C  CA   . LEU   A 1 19  ? 39.27600 -0.89800  2.83900  1.000 69.35457  ?  124 LEU   A CA   1 
ATOM   21   C  C    . LEU   A 1 19  ? 38.82500 -1.24700  1.42700  1.000 70.43171  ?  124 LEU   A C    1 
ATOM   22   O  O    . LEU   A 1 19  ? 38.85000 -0.40500  0.52700  1.000 73.44887  ?  124 LEU   A O    1 
ATOM   23   C  CB   . LEU   A 1 19  ? 38.84200 0.50800   3.23700  1.000 70.69560  ?  124 LEU   A CB   1 
ATOM   24   C  CG   . LEU   A 1 19  ? 37.37400 0.71100   3.62200  1.000 69.02312  ?  124 LEU   A CG   1 
ATOM   25   C  CD1  . LEU   A 1 19  ? 36.96000 -0.24800  4.72900  1.000 60.97164  ?  124 LEU   A CD1  1 
ATOM   26   C  CD2  . LEU   A 1 19  ? 37.12700 2.15300   4.04100  1.000 70.26368  ?  124 LEU   A CD2  1 
ATOM   27   N  N    . SER   A 1 20  ? 38.40900 -2.49700  1.23200  1.000 64.55757  ?  125 SER   A N    1 
ATOM   28   C  CA   . SER   A 1 20  ? 38.08400 -2.98900  -0.09700 1.000 62.61374  ?  125 SER   A CA   1 
ATOM   29   C  C    . SER   A 1 20  ? 36.86900 -2.25800  -0.66900 1.000 61.04985  ?  125 SER   A C    1 
ATOM   30   O  O    . SER   A 1 20  ? 36.15800 -1.52500  0.02400  1.000 59.10946  ?  125 SER   A O    1 
ATOM   31   C  CB   . SER   A 1 20  ? 37.82200 -4.49400  -0.05800 1.000 61.82407  ?  125 SER   A CB   1 
ATOM   32   O  OG   . SER   A 1 20  ? 36.62800 -4.78600  0.64600  1.000 58.38920  ?  125 SER   A OG   1 
ATOM   33   N  N    A GLU   A 1 21  ? 36.63300 -2.46900  -1.96700 0.530 63.02024  ?  126 GLU   A N    1 
ATOM   34   N  N    B GLU   A 1 21  ? 36.64800 -2.46800  -1.97000 0.470 63.08235  ?  126 GLU   A N    1 
ATOM   35   C  CA   A GLU   A 1 21  ? 35.48500 -1.84000  -2.61400 0.530 63.97329  ?  126 GLU   A CA   1 
ATOM   36   C  CA   B GLU   A 1 21  ? 35.49800 -1.87100  -2.64100 0.470 64.04552  ?  126 GLU   A CA   1 
ATOM   37   C  C    A GLU   A 1 21  ? 34.17400 -2.37900  -2.05600 0.530 60.63272  ?  126 GLU   A C    1 
ATOM   38   C  C    B GLU   A 1 21  ? 34.19200 -2.37600  -2.04400 0.470 60.65479  ?  126 GLU   A C    1 
ATOM   39   O  O    A GLU   A 1 21  ? 33.19000 -1.63700  -1.94400 0.530 58.90294  ?  126 GLU   A O    1 
ATOM   40   O  O    B GLU   A 1 21  ? 33.23000 -1.61300  -1.89500 0.470 58.85154  ?  126 GLU   A O    1 
ATOM   41   C  CB   A GLU   A 1 21  ? 35.55200 -2.04600  -4.12700 0.530 68.42799  ?  126 GLU   A CB   1 
ATOM   42   C  CB   B GLU   A 1 21  ? 35.55200 -2.17300  -4.14000 0.470 68.48645  ?  126 GLU   A CB   1 
ATOM   43   C  CG   A GLU   A 1 21  ? 34.87900 -0.94100  -4.92200 0.530 70.61614  ?  126 GLU   A CG   1 
ATOM   44   C  CG   B GLU   A 1 21  ? 36.93900 -2.05800  -4.76200 0.470 71.61557  ?  126 GLU   A CG   1 
ATOM   45   C  CD   A GLU   A 1 21  ? 35.65700 0.35900   -4.88200 0.530 73.35530  ?  126 GLU   A CD   1 
ATOM   46   C  CD   B GLU   A 1 21  ? 37.72700 -3.35600  -4.69400 0.470 70.48902  ?  126 GLU   A CD   1 
ATOM   47   O  OE1  A GLU   A 1 21  ? 35.02900 1.42500   -4.71800 0.530 72.98314  ?  126 GLU   A OE1  1 
ATOM   48   O  OE1  B GLU   A 1 21  ? 38.36500 -3.61500  -3.65100 0.470 65.87354  ?  126 GLU   A OE1  1 
ATOM   49   O  OE2  A GLU   A 1 21  ? 36.89900 0.31600   -5.01300 0.530 76.05687  ?  126 GLU   A OE2  1 
ATOM   50   O  OE2  B GLU   A 1 21  ? 37.70700 -4.11800  -5.68300 0.470 72.97876  ?  126 GLU   A OE2  1 
ATOM   51   N  N    . GLU   A 1 22  ? 34.14100 -3.66500  -1.69700 1.000 61.50390  ?  127 GLU   A N    1 
ATOM   52   C  CA   . GLU   A 1 22  ? 32.94100 -4.22600  -1.08700 1.000 54.65348  ?  127 GLU   A CA   1 
ATOM   53   C  C    . GLU   A 1 22  ? 32.68000 -3.60700  0.28000  1.000 50.05950  ?  127 GLU   A C    1 
ATOM   54   O  O    . GLU   A 1 22  ? 31.52400 -3.37400  0.65400  1.000 49.10531  ?  127 GLU   A O    1 
ATOM   55   C  CB   . GLU   A 1 22  ? 33.07800 -5.74400  -0.96700 1.000 63.27906  ?  127 GLU   A CB   1 
ATOM   56   C  CG   . GLU   A 1 22  ? 31.83200 -6.44600  -0.44900 1.000 69.47715  ?  127 GLU   A CG   1 
ATOM   57   C  CD   . GLU   A 1 22  ? 31.86500 -7.94300  -0.69000 1.000 79.10621  ?  127 GLU   A CD   1 
ATOM   58   O  OE1  . GLU   A 1 22  ? 32.31800 -8.36100  -1.77700 1.000 85.86517  ?  127 GLU   A OE1  1 
ATOM   59   O  OE2  . GLU   A 1 22  ? 31.44100 -8.70100  0.20700  1.000 80.76766  ?  127 GLU   A OE2  1 
ATOM   60   N  N    . GLN   A 1 23  ? 33.74300 -3.33000  1.03800  1.000 46.86849  ?  128 GLN   A N    1 
ATOM   61   C  CA   . GLN   A 1 23  ? 33.57000 -2.74200  2.36100  1.000 47.25454  ?  128 GLN   A CA   1 
ATOM   62   C  C    . GLN   A 1 23  ? 33.07500 -1.30400  2.26500  1.000 47.68836  ?  128 GLN   A C    1 
ATOM   63   O  O    . GLN   A 1 23  ? 32.24700 -0.87300  3.07700  1.000 48.51977  ?  128 GLN   A O    1 
ATOM   64   C  CB   . GLN   A 1 23  ? 34.88100 -2.82200  3.14300  1.000 49.05993  ?  128 GLN   A CB   1 
ATOM   65   C  CG   . GLN   A 1 23  ? 35.16700 -4.21200  3.69800  1.000 51.49253  ?  128 GLN   A CG   1 
ATOM   66   C  CD   . GLN   A 1 23  ? 36.58200 -4.36900  4.22000  1.000 55.01556  ?  128 GLN   A CD   1 
ATOM   67   O  OE1  . GLN   A 1 23  ? 37.48100 -3.60900  3.85900  1.000 53.31834  ?  128 GLN   A OE1  1 
ATOM   68   N  NE2  . GLN   A 1 23  ? 36.78800 -5.36500  5.07500  1.000 53.13626  ?  128 GLN   A NE2  1 
ATOM   69   N  N    . GLN   A 1 24  ? 33.56500 -0.54800  1.27800  1.000 47.46666  ?  129 GLN   A N    1 
ATOM   70   C  CA   . GLN   A 1 24  ? 33.02800 0.78900   1.04000  1.000 50.47315  ?  129 GLN   A CA   1 
ATOM   71   C  C    . GLN   A 1 24  ? 31.56500 0.72100   0.62300  1.000 47.27400  ?  129 GLN   A C    1 
ATOM   72   O  O    . GLN   A 1 24  ? 30.76700 1.59700   0.97600  1.000 48.15995  ?  129 GLN   A O    1 
ATOM   73   C  CB   . GLN   A 1 24  ? 33.85100 1.50800   -0.02900 1.000 55.25083  ?  129 GLN   A CB   1 
ATOM   74   C  CG   . GLN   A 1 24  ? 35.10100 2.19500   0.49500  1.000 61.55545  ?  129 GLN   A CG   1 
ATOM   75   C  CD   . GLN   A 1 24  ? 35.95600 2.76800   -0.61800 1.000 73.10868  ?  129 GLN   A CD   1 
ATOM   76   O  OE1  . GLN   A 1 24  ? 36.82300 2.08600   -1.16700 1.000 75.58238  ?  129 GLN   A OE1  1 
ATOM   77   N  NE2  . GLN   A 1 24  ? 35.71000 4.02600   -0.96500 1.000 79.34119  ?  129 GLN   A NE2  1 
ATOM   78   N  N    . HIS   A 1 25  ? 31.19900 -0.31400  -0.13500 1.000 50.08754  ?  130 HIS   A N    1 
ATOM   79   C  CA   . HIS   A 1 25  ? 29.80500 -0.51100  -0.52200 1.000 49.41171  ?  130 HIS   A CA   1 
ATOM   80   C  C    . HIS   A 1 25  ? 28.93000 -0.76400  0.70000  1.000 47.58907  ?  130 HIS   A C    1 
ATOM   81   O  O    . HIS   A 1 25  ? 27.84300 -0.18900  0.83100  1.000 47.74227  ?  130 HIS   A O    1 
ATOM   82   C  CB   . HIS   A 1 25  ? 29.71100 -1.67500  -1.51000 1.000 55.66001  ?  130 HIS   A CB   1 
ATOM   83   C  CG   . HIS   A 1 25  ? 28.34700 -1.87100  -2.09400 1.000 59.44963  ?  130 HIS   A CG   1 
ATOM   84   N  ND1  . HIS   A 1 25  ? 27.64800 -0.85800  -2.71300 1.000 62.31594  ?  130 HIS   A ND1  1 
ATOM   85   C  CD2  . HIS   A 1 25  ? 27.55800 -2.96900  -2.16200 1.000 64.25522  ?  130 HIS   A CD2  1 
ATOM   86   C  CE1  . HIS   A 1 25  ? 26.48400 -1.32200  -3.13400 1.000 64.85418  ?  130 HIS   A CE1  1 
ATOM   87   N  NE2  . HIS   A 1 25  ? 26.40600 -2.60100  -2.81400 1.000 62.64116  ?  130 HIS   A NE2  1 
ATOM   88   N  N    . ILE   A 1 26  ? 29.39800 -1.62200  1.61000  1.000 47.56468  ?  131 ILE   A N    1 
ATOM   89   C  CA   . ILE   A 1 26  ? 28.63000 -1.95600  2.80800  1.000 40.97090  ?  131 ILE   A CA   1 
ATOM   90   C  C    . ILE   A 1 26  ? 28.35100 -0.70500  3.63300  1.000 43.07804  ?  131 ILE   A C    1 
ATOM   91   O  O    . ILE   A 1 26  ? 27.22800 -0.48500  4.10400  1.000 39.31301  ?  131 ILE   A O    1 
ATOM   92   C  CB   . ILE   A 1 26  ? 29.37500 -3.02000  3.63400  1.000 42.79550  ?  131 ILE   A CB   1 
ATOM   93   C  CG1  . ILE   A 1 26  ? 29.42000 -4.34700  2.87500  1.000 46.68006  ?  131 ILE   A CG1  1 
ATOM   94   C  CG2  . ILE   A 1 26  ? 28.73100 -3.19300  5.00400  1.000 40.44860  ?  131 ILE   A CG2  1 
ATOM   95   C  CD1  . ILE   A 1 26  ? 30.26900 -5.40100  3.54400  1.000 49.50077  ?  131 ILE   A CD1  1 
ATOM   96   N  N    . ILE   A 1 27  ? 29.37300 0.13300   3.82200  1.000 45.41685  ?  132 ILE   A N    1 
ATOM   97   C  CA   . ILE   A 1 27  ? 29.20800 1.34600   4.61800  1.000 43.22033  ?  132 ILE   A CA   1 
ATOM   98   C  C    . ILE   A 1 27  ? 28.21900 2.29500   3.95200  1.000 41.62941  ?  132 ILE   A C    1 
ATOM   99   O  O    . ILE   A 1 27  ? 27.37400 2.90400   4.62100  1.000 41.99537  ?  132 ILE   A O    1 
ATOM   100  C  CB   . ILE   A 1 27  ? 30.57600 2.01500   4.84800  1.000 44.99126  ?  132 ILE   A CB   1 
ATOM   101  C  CG1  . ILE   A 1 27  ? 31.42100 1.17600   5.81000  1.000 42.10352  ?  132 ILE   A CG1  1 
ATOM   102  C  CG2  . ILE   A 1 27  ? 30.40100 3.42500   5.37400  1.000 44.47308  ?  132 ILE   A CG2  1 
ATOM   103  C  CD1  . ILE   A 1 27  ? 32.88000 1.58600   5.85800  1.000 45.19398  ?  132 ILE   A CD1  1 
ATOM   104  N  N    . ALA   A 1 28  ? 28.29700 2.42400   2.62500  1.000 40.87494  ?  133 ALA   A N    1 
ATOM   105  C  CA   . ALA   A 1 28  ? 27.38200 3.31000   1.91000  1.000 42.29368  ?  133 ALA   A CA   1 
ATOM   106  C  C    . ALA   A 1 28  ? 25.93200 2.87500   2.09200  1.000 43.16448  ?  133 ALA   A C    1 
ATOM   107  O  O    . ALA   A 1 28  ? 25.04400 3.71500   2.28600  1.000 42.70895  ?  133 ALA   A O    1 
ATOM   108  C  CB   . ALA   A 1 28  ? 27.74700 3.35300   0.42600  1.000 42.07440  ?  133 ALA   A CB   1 
ATOM   109  N  N    . ILE   A 1 29  ? 25.67300 1.56700   2.03800  1.000 44.46971  ?  134 ILE   A N    1 
ATOM   110  C  CA   . ILE   A 1 29  ? 24.30800 1.07100   2.18700  1.000 42.08703  ?  134 ILE   A CA   1 
ATOM   111  C  C    . ILE   A 1 29  ? 23.79000 1.33600   3.59500  1.000 41.41770  ?  134 ILE   A C    1 
ATOM   112  O  O    . ILE   A 1 29  ? 22.64500 1.76700   3.78000  1.000 40.25379  ?  134 ILE   A O    1 
ATOM   113  C  CB   . ILE   A 1 29  ? 24.25000 -0.42700  1.84000  1.000 42.18441  ?  134 ILE   A CB   1 
ATOM   114  C  CG1  . ILE   A 1 29  ? 24.39700 -0.63500  0.33500  1.000 47.87237  ?  134 ILE   A CG1  1 
ATOM   115  C  CG2  . ILE   A 1 29  ? 22.96000 -1.05100  2.33900  1.000 38.47080  ?  134 ILE   A CG2  1 
ATOM   116  C  CD1  . ILE   A 1 29  ? 25.01800 -1.95500  -0.00900 1.000 51.40658  ?  134 ILE   A CD1  1 
ATOM   117  N  N    . LEU   A 1 30  ? 24.62200 1.08000   4.60700  1.000 40.12023  ?  135 LEU   A N    1 
ATOM   118  C  CA   . LEU   A 1 30  ? 24.18400 1.25300   5.98800  1.000 33.94213  ?  135 LEU   A CA   1 
ATOM   119  C  C    . LEU   A 1 30  ? 23.95300 2.72300   6.31600  1.000 35.60270  ?  135 LEU   A C    1 
ATOM   120  O  O    . LEU   A 1 30  ? 23.03400 3.05600   7.07500  1.000 36.12388  ?  135 LEU   A O    1 
ATOM   121  C  CB   . LEU   A 1 30  ? 25.20800 0.63400   6.93900  1.000 34.75844  ?  135 LEU   A CB   1 
ATOM   122  C  CG   . LEU   A 1 30  ? 25.33100 -0.88900  6.84000  1.000 35.90709  ?  135 LEU   A CG   1 
ATOM   123  C  CD1  . LEU   A 1 30  ? 26.38300 -1.41000  7.79900  1.000 35.84519  ?  135 LEU   A CD1  1 
ATOM   124  C  CD2  . LEU   A 1 30  ? 23.98600 -1.55200  7.10300  1.000 36.41802  ?  135 LEU   A CD2  1 
ATOM   125  N  N    A LEU   A 1 31  ? 24.77600 3.61600   5.76600  0.930 35.88203  ?  136 LEU   A N    1 
ATOM   126  N  N    B LEU   A 1 31  ? 24.77900 3.61200   5.75800  0.070 36.66446  ?  136 LEU   A N    1 
ATOM   127  C  CA   A LEU   A 1 31  ? 24.53600 5.04400   5.94900  0.930 38.05983  ?  136 LEU   A CA   1 
ATOM   128  C  CA   B LEU   A 1 31  ? 24.56200 5.04700   5.92400  0.070 37.00536  ?  136 LEU   A CA   1 
ATOM   129  C  C    A LEU   A 1 31  ? 23.19700 5.44700   5.34600  0.930 37.76313  ?  136 LEU   A C    1 
ATOM   130  C  C    B LEU   A 1 31  ? 23.22000 5.46400   5.33400  0.070 37.53519  ?  136 LEU   A C    1 
ATOM   131  O  O    A LEU   A 1 31  ? 22.40200 6.15200   5.97900  0.930 36.58540  ?  136 LEU   A O    1 
ATOM   132  O  O    B LEU   A 1 31  ? 22.45200 6.20400   5.95900  0.070 36.86603  ?  136 LEU   A O    1 
ATOM   133  C  CB   A LEU   A 1 31  ? 25.67200 5.85600   5.32600  0.930 37.74624  ?  136 LEU   A CB   1 
ATOM   134  C  CB   B LEU   A 1 31  ? 25.69800 5.83000   5.26100  0.070 38.20165  ?  136 LEU   A CB   1 
ATOM   135  C  CG   A LEU   A 1 31  ? 27.02800 5.86400   6.03600  0.930 37.23394  ?  136 LEU   A CG   1 
ATOM   136  C  CG   B LEU   A 1 31  ? 26.90800 6.28000   6.08400  0.070 37.71332  ?  136 LEU   A CG   1 
ATOM   137  C  CD1  A LEU   A 1 31  ? 28.07800 6.53900   5.16500  0.930 37.03200  ?  136 LEU   A CD1  1 
ATOM   138  C  CD1  B LEU   A 1 31  ? 27.46200 5.15100   6.93100  0.070 37.21507  ?  136 LEU   A CD1  1 
ATOM   139  C  CD2  A LEU   A 1 31  ? 26.93300 6.55200   7.39000  0.930 39.87726  ?  136 LEU   A CD2  1 
ATOM   140  C  CD2  B LEU   A 1 31  ? 27.98900 6.83500   5.16700  0.070 38.71596  ?  136 LEU   A CD2  1 
ATOM   141  N  N    . ASP   A 1 32  ? 22.92800 4.99600   4.11900  1.000 37.55232  ?  137 ASP   A N    1 
ATOM   142  C  CA   . ASP   A 1 32  ? 21.66700 5.32900   3.46700  1.000 38.76984  ?  137 ASP   A CA   1 
ATOM   143  C  C    . ASP   A 1 32  ? 20.48500 4.69300   4.18800  1.000 39.64223  ?  137 ASP   A C    1 
ATOM   144  O  O    . ASP   A 1 32  ? 19.42500 5.31600   4.32400  1.000 41.48632  ?  137 ASP   A O    1 
ATOM   145  C  CB   . ASP   A 1 32  ? 21.71800 4.87900   2.00700  1.000 41.96791  ?  137 ASP   A CB   1 
ATOM   146  C  CG   . ASP   A 1 32  ? 20.42900 5.15200   1.26400  1.000 46.81799  ?  137 ASP   A CG   1 
ATOM   147  O  OD1  . ASP   A 1 32  ? 19.78500 4.17900   0.82100  1.000 50.57077  ?  137 ASP   A OD1  1 
ATOM   148  O  OD2  . ASP   A 1 32  ? 20.06800 6.33700   1.11400  1.000 49.61985  ?  137 ASP   A OD2  1 
ATOM   149  N  N    . ALA   A 1 33  ? 20.64900 3.45200   4.65400  1.000 39.63164  ?  138 ALA   A N    1 
ATOM   150  C  CA   . ALA   A 1 33  ? 19.57700 2.78300   5.38400  1.000 36.58737  ?  138 ALA   A CA   1 
ATOM   151  C  C    . ALA   A 1 33  ? 19.21800 3.54000   6.65500  1.000 39.10278  ?  138 ALA   A C    1 
ATOM   152  O  O    . ALA   A 1 33  ? 18.03700 3.66900   6.99800  1.000 33.09497  ?  138 ALA   A O    1 
ATOM   153  C  CB   . ALA   A 1 33  ? 19.98500 1.34800   5.71500  1.000 36.82966  ?  138 ALA   A CB   1 
ATOM   154  N  N    . HIS   A 1 34  ? 20.22600 4.04200   7.37100  1.000 31.55934  ?  139 HIS   A N    1 
ATOM   155  C  CA   . HIS   A 1 34  ? 19.96800 4.80900   8.58600  1.000 35.49509  ?  139 HIS   A CA   1 
ATOM   156  C  C    . HIS   A 1 34  ? 19.29800 6.14000   8.27000  1.000 35.21024  ?  139 HIS   A C    1 
ATOM   157  O  O    . HIS   A 1 34  ? 18.37300 6.55900   8.97500  1.000 36.47795  ?  139 HIS   A O    1 
ATOM   158  C  CB   . HIS   A 1 34  ? 21.27400 5.03600   9.34500  1.000 33.55116  ?  139 HIS   A CB   1 
ATOM   159  C  CG   . HIS   A 1 34  ? 21.12400 5.88400   10.56900 1.000 36.10960  ?  139 HIS   A CG   1 
ATOM   160  N  ND1  . HIS   A 1 34  ? 20.33200 5.51900   11.63500 1.000 32.95623  ?  139 HIS   A ND1  1 
ATOM   161  C  CD2  . HIS   A 1 34  ? 21.66600 7.08100   10.89600 1.000 37.01902  ?  139 HIS   A CD2  1 
ATOM   162  C  CE1  . HIS   A 1 34  ? 20.39100 6.45400   12.56600 1.000 33.67640  ?  139 HIS   A CE1  1 
ATOM   163  N  NE2  . HIS   A 1 34  ? 21.19300 7.41400   12.14200 1.000 35.21847  ?  139 HIS   A NE2  1 
ATOM   164  N  N    . HIS   A 1 35  ? 19.75700 6.82200   7.21800  1.000 35.55989  ?  140 HIS   A N    1 
ATOM   165  C  CA   . HIS   A 1 35  ? 19.16300 8.10300   6.85400  1.000 38.06095  ?  140 HIS   A CA   1 
ATOM   166  C  C    . HIS   A 1 35  ? 17.71200 7.94300   6.42200  1.000 40.11378  ?  140 HIS   A C    1 
ATOM   167  O  O    . HIS   A 1 35  ? 16.90400 8.85900   6.60900  1.000 38.94232  ?  140 HIS   A O    1 
ATOM   168  C  CB   . HIS   A 1 35  ? 19.98300 8.76300   5.74600  1.000 44.90920  ?  140 HIS   A CB   1 
ATOM   169  C  CG   . HIS   A 1 35  ? 21.34500 9.20000   6.18500  1.000 52.29113  ?  140 HIS   A CG   1 
ATOM   170  N  ND1  . HIS   A 1 35  ? 22.42200 9.25700   5.32700  1.000 53.26513  ?  140 HIS   A ND1  1 
ATOM   171  C  CD2  . HIS   A 1 35  ? 21.80700 9.59800   7.39500  1.000 52.26159  ?  140 HIS   A CD2  1 
ATOM   172  C  CE1  . HIS   A 1 35  ? 23.48800 9.67400   5.98800  1.000 54.66570  ?  140 HIS   A CE1  1 
ATOM   173  N  NE2  . HIS   A 1 35  ? 23.14100 9.88800   7.24500  1.000 52.18940  ?  140 HIS   A NE2  1 
ATOM   174  N  N    . LYS   A 1 36  ? 17.36100 6.78800   5.85800  1.000 36.14738  ?  141 LYS   A N    1 
ATOM   175  C  CA   . LYS   A 1 36  ? 15.99100 6.53900   5.43200  1.000 36.87059  ?  141 LYS   A CA   1 
ATOM   176  C  C    . LYS   A 1 36  ? 15.09500 6.04500   6.56100  1.000 34.79608  ?  141 LYS   A C    1 
ATOM   177  O  O    . LYS   A 1 36  ? 13.87300 6.01500   6.38700  1.000 33.87355  ?  141 LYS   A O    1 
ATOM   178  C  CB   . LYS   A 1 36  ? 15.97600 5.52900   4.27900  1.000 35.97563  ?  141 LYS   A CB   1 
ATOM   179  C  CG   . LYS   A 1 36  ? 16.49300 6.08800   2.96000  1.000 45.57118  ?  141 LYS   A CG   1 
ATOM   180  C  CD   . LYS   A 1 36  ? 16.24000 5.12600   1.80800  1.000 55.29957  ?  141 LYS   A CD   1 
ATOM   181  C  CE   . LYS   A 1 36  ? 16.60200 5.75100   0.46700  1.000 61.97176  ?  141 LYS   A CE   1 
ATOM   182  N  NZ   . LYS   A 1 36  ? 16.79600 7.22600   0.56500  1.000 67.10501  ?  141 LYS   A NZ   1 
ATOM   183  N  N    . THR   A 1 37  ? 15.66100 5.66600   7.70800  1.000 31.27220  ?  142 THR   A N    1 
ATOM   184  C  CA   . THR   A 1 37  ? 14.87800 5.14700   8.82000  1.000 34.23519  ?  142 THR   A CA   1 
ATOM   185  C  C    . THR   A 1 37  ? 14.98500 5.98000   10.09100 1.000 36.01934  ?  142 THR   A C    1 
ATOM   186  O  O    . THR   A 1 37  ? 14.34400 5.63400   11.09000 1.000 35.26964  ?  142 THR   A O    1 
ATOM   187  C  CB   . THR   A 1 37  ? 15.28400 3.69900   9.13400  1.000 34.34211  ?  142 THR   A CB   1 
ATOM   188  O  OG1  . THR   A 1 37  ? 16.70300 3.62800   9.33200  1.000 34.09927  ?  142 THR   A OG1  1 
ATOM   189  C  CG2  . THR   A 1 37  ? 14.89200 2.77500   7.99400  1.000 32.50240  ?  142 THR   A CG2  1 
ATOM   190  N  N    . TYR   A 1 38  ? 15.77200 7.05400   10.09400 1.000 33.67196  ?  143 TYR   A N    1 
ATOM   191  C  CA   . TYR   A 1 38  ? 15.88500 7.94100   11.24800 1.000 32.10734  ?  143 TYR   A CA   1 
ATOM   192  C  C    . TYR   A 1 38  ? 15.54100 9.35700   10.81300 1.000 35.70829  ?  143 TYR   A C    1 
ATOM   193  O  O    . TYR   A 1 38  ? 16.22100 9.92600   9.95300  1.000 36.04627  ?  143 TYR   A O    1 
ATOM   194  C  CB   . TYR   A 1 38  ? 17.28800 7.89100   11.86100 1.000 34.27418  ?  143 TYR   A CB   1 
ATOM   195  C  CG   . TYR   A 1 38  ? 17.38000 8.56100   13.21800 1.000 30.09668  ?  143 TYR   A CG   1 
ATOM   196  C  CD1  . TYR   A 1 38  ? 17.53100 9.93800   13.32900 1.000 32.76502  ?  143 TYR   A CD1  1 
ATOM   197  C  CD2  . TYR   A 1 38  ? 17.30700 7.81600   14.38800 1.000 29.88275  ?  143 TYR   A CD2  1 
ATOM   198  C  CE1  . TYR   A 1 38  ? 17.60900 10.55400  14.56600 1.000 31.50033  ?  143 TYR   A CE1  1 
ATOM   199  C  CE2  . TYR   A 1 38  ? 17.38600 8.42300   15.62900 1.000 31.95071  ?  143 TYR   A CE2  1 
ATOM   200  C  CZ   . TYR   A 1 38  ? 17.53700 9.79100   15.71100 1.000 35.47357  ?  143 TYR   A CZ   1 
ATOM   201  O  OH   . TYR   A 1 38  ? 17.61400 10.40100  16.94200 1.000 35.28591  ?  143 TYR   A OH   1 
ATOM   202  N  N    . ASP   A 1 39  ? 14.49200 9.92500   11.41300 1.000 32.47117  ?  144 ASP   A N    1 
ATOM   203  C  CA   . ASP   A 1 39  ? 14.03400 11.27000  11.09600 1.000 35.89649  ?  144 ASP   A CA   1 
ATOM   204  C  C    . ASP   A 1 39  ? 14.47900 12.21400  12.20400 1.000 39.62029  ?  144 ASP   A C    1 
ATOM   205  O  O    . ASP   A 1 39  ? 13.84400 12.25100  13.27000 1.000 34.31203  ?  144 ASP   A O    1 
ATOM   206  C  CB   . ASP   A 1 39  ? 12.50900 11.29700  10.94000 1.000 39.07354  ?  144 ASP   A CB   1 
ATOM   207  C  CG   . ASP   A 1 39  ? 11.96200 12.69700  10.70100 1.000 45.12459  ?  144 ASP   A CG   1 
ATOM   208  O  OD1  . ASP   A 1 39  ? 12.75200 13.62600  10.42500 1.000 43.74940  ?  144 ASP   A OD1  1 
ATOM   209  O  OD2  . ASP   A 1 39  ? 10.72700 12.86600  10.78600 1.000 45.08589  ?  144 ASP   A OD2  1 
ATOM   210  N  N    . PRO   A 1 40  ? 15.54100 13.00300  12.00700 1.000 40.12776  ?  145 PRO   A N    1 
ATOM   211  C  CA   . PRO   A 1 40  ? 16.01100 13.89700  13.07600 1.000 42.69207  ?  145 PRO   A CA   1 
ATOM   212  C  C    . PRO   A 1 40  ? 15.12700 15.11200  13.30000 1.000 45.32708  ?  145 PRO   A C    1 
ATOM   213  O  O    . PRO   A 1 40  ? 15.43200 15.92100  14.18400 1.000 45.10332  ?  145 PRO   A O    1 
ATOM   214  C  CB   . PRO   A 1 40  ? 17.40900 14.31000  12.59200 1.000 41.78228  ?  145 PRO   A CB   1 
ATOM   215  C  CG   . PRO   A 1 40  ? 17.31900 14.24400  11.11000 1.000 43.73042  ?  145 PRO   A CG   1 
ATOM   216  C  CD   . PRO   A 1 40  ? 16.35900 13.11800  10.78600 1.000 40.87254  ?  145 PRO   A CD   1 
ATOM   217  N  N    . THR   A 1 41  ? 14.05100 15.28000  12.52900 1.000 45.43437  ?  146 THR   A N    1 
ATOM   218  C  CA   . THR   A 1 41  ? 13.08100 16.32500  12.82200 1.000 44.13290  ?  146 THR   A CA   1 
ATOM   219  C  C    . THR   A 1 41  ? 12.05000 15.87900  13.84900 1.000 44.44648  ?  146 THR   A C    1 
ATOM   220  O  O    . THR   A 1 41  ? 11.40700 16.73200  14.47200 1.000 41.71839  ?  146 THR   A O    1 
ATOM   221  C  CB   . THR   A 1 41  ? 12.37200 16.77200  11.54200 1.000 51.73918  ?  146 THR   A CB   1 
ATOM   222  O  OG1  . THR   A 1 41  ? 11.41700 15.78000  11.14800 1.000 51.96784  ?  146 THR   A OG1  1 
ATOM   223  C  CG2  . THR   A 1 41  ? 13.37900 16.97300  10.42000 1.000 56.90079  ?  146 THR   A CG2  1 
ATOM   224  N  N    . TYR   A 1 42  ? 11.88400 14.56600  14.03400 1.000 37.68175  ?  147 TYR   A N    1 
ATOM   225  C  CA   . TYR   A 1 42  ? 10.97500 14.00100  15.03400 1.000 36.71082  ?  147 TYR   A CA   1 
ATOM   226  C  C    . TYR   A 1 42  ? 9.53800  14.47200  14.83000 1.000 41.13609  ?  147 TYR   A C    1 
ATOM   227  O  O    . TYR   A 1 42  ? 8.79100  14.65900  15.79400 1.000 46.15250  ?  147 TYR   A O    1 
ATOM   228  C  CB   . TYR   A 1 42  ? 11.45600 14.32000  16.45300 1.000 38.47345  ?  147 TYR   A CB   1 
ATOM   229  C  CG   . TYR   A 1 42  ? 12.89900 13.93200  16.68900 1.000 37.74187  ?  147 TYR   A CG   1 
ATOM   230  C  CD1  . TYR   A 1 42  ? 13.87800 14.89800  16.86900 1.000 41.76759  ?  147 TYR   A CD1  1 
ATOM   231  C  CD2  . TYR   A 1 42  ? 13.28200 12.59700  16.71700 1.000 37.07642  ?  147 TYR   A CD2  1 
ATOM   232  C  CE1  . TYR   A 1 42  ? 15.20100 14.54700  17.07900 1.000 41.81289  ?  147 TYR   A CE1  1 
ATOM   233  C  CE2  . TYR   A 1 42  ? 14.60100 12.23500  16.92600 1.000 41.93204  ?  147 TYR   A CE2  1 
ATOM   234  C  CZ   . TYR   A 1 42  ? 15.55600 13.21400  17.10600 1.000 44.69821  ?  147 TYR   A CZ   1 
ATOM   235  O  OH   . TYR   A 1 42  ? 16.86900 12.85700  17.31400 1.000 41.25114  ?  147 TYR   A OH   1 
ATOM   236  N  N    . ALA   A 1 43  ? 9.13700  14.65600  13.57000 1.000 40.87368  ?  148 ALA   A N    1 
ATOM   237  C  CA   . ALA   A 1 43  ? 7.80500  15.17700  13.28200 1.000 43.93662  ?  148 ALA   A CA   1 
ATOM   238  C  C    . ALA   A 1 43  ? 6.71000  14.18100  13.64100 1.000 48.28078  ?  148 ALA   A C    1 
ATOM   239  O  O    . ALA   A 1 43  ? 5.61200  14.58900  14.03800 1.000 53.01391  ?  148 ALA   A O    1 
ATOM   240  C  CB   . ALA   A 1 43  ? 7.70100  15.56600  11.80800 1.000 44.57407  ?  148 ALA   A CB   1 
ATOM   241  N  N    . ASP   A 1 44  ? 6.98200  12.88000  13.51300 1.000 44.14543  ?  149 ASP   A N    1 
ATOM   242  C  CA   . ASP   A 1 44  ? 5.96600  11.86600  13.77000 1.000 42.25386  ?  149 ASP   A CA   1 
ATOM   243  C  C    . ASP   A 1 44  ? 5.58500  11.76200  15.24000 1.000 44.17280  ?  149 ASP   A C    1 
ATOM   244  O  O    . ASP   A 1 44  ? 4.57600  11.12000  15.55300 1.000 41.88255  ?  149 ASP   A O    1 
ATOM   245  C  CB   . ASP   A 1 44  ? 6.44400  10.50200  13.27100 1.000 41.69232  ?  149 ASP   A CB   1 
ATOM   246  C  CG   . ASP   A 1 44  ? 6.71000  10.48700  11.77900 1.000 46.49014  ?  149 ASP   A CG   1 
ATOM   247  O  OD1  . ASP   A 1 44  ? 6.02500  11.23100  11.04500 1.000 47.63196  ?  149 ASP   A OD1  1 
ATOM   248  O  OD2  . ASP   A 1 44  ? 7.60200  9.73100   11.34000 1.000 49.69420  ?  149 ASP   A OD2  1 
ATOM   249  N  N    . PHE   A 1 45  ? 6.35700  12.37600  16.14200 1.000 43.72157  ?  150 PHE   A N    1 
ATOM   250  C  CA   . PHE   A 1 45  ? 6.05400  12.30300  17.56800 1.000 41.66358  ?  150 PHE   A CA   1 
ATOM   251  C  C    . PHE   A 1 45  ? 4.70200  12.92000  17.90300 1.000 41.49711  ?  150 PHE   A C    1 
ATOM   252  O  O    . PHE   A 1 45  ? 4.15000  12.63400  18.97100 1.000 46.62229  ?  150 PHE   A O    1 
ATOM   253  C  CB   . PHE   A 1 45  ? 7.15100  12.99800  18.38000 1.000 43.57806  ?  150 PHE   A CB   1 
ATOM   254  C  CG   . PHE   A 1 45  ? 8.39500  12.16800  18.57000 1.000 43.02656  ?  150 PHE   A CG   1 
ATOM   255  C  CD1  . PHE   A 1 45  ? 8.94400  11.45600  17.51600 1.000 43.49728  ?  150 PHE   A CD1  1 
ATOM   256  C  CD2  . PHE   A 1 45  ? 9.02100  12.11400  19.80400 1.000 42.95520  ?  150 PHE   A CD2  1 
ATOM   257  C  CE1  . PHE   A 1 45  ? 10.08800 10.70100  17.69100 1.000 41.36963  ?  150 PHE   A CE1  1 
ATOM   258  C  CE2  . PHE   A 1 45  ? 10.16500 11.36000  19.98600 1.000 37.28150  ?  150 PHE   A CE2  1 
ATOM   259  C  CZ   . PHE   A 1 45  ? 10.70000 10.65500  18.92800 1.000 36.55602  ?  150 PHE   A CZ   1 
ATOM   260  N  N    . ARG   A 1 46  ? 4.15900  13.76000  17.01900 1.000 43.21198  ?  151 ARG   A N    1 
ATOM   261  C  CA   . ARG   A 1 46  ? 2.84400  14.34200  17.25200 1.000 48.96340  ?  151 ARG   A CA   1 
ATOM   262  C  C    . ARG   A 1 46  ? 1.72600  13.31500  17.12400 1.000 49.50494  ?  151 ARG   A C    1 
ATOM   263  O  O    . ARG   A 1 46  ? 0.61200  13.56900  17.59400 1.000 54.08964  ?  151 ARG   A O    1 
ATOM   264  C  CB   . ARG   A 1 46  ? 2.60200  15.49800  16.28000 1.000 58.71383  ?  151 ARG   A CB   1 
ATOM   265  C  CG   . ARG   A 1 46  ? 2.46000  15.07900  14.82300 1.000 64.64874  ?  151 ARG   A CG   1 
ATOM   266  C  CD   . ARG   A 1 46  ? 1.41800  15.92900  14.10900 1.000 74.15041  ?  151 ARG   A CD   1 
ATOM   267  N  NE   . ARG   A 1 46  ? 1.08000  15.40100  12.79000 1.000 76.60922  ?  151 ARG   A NE   1 
ATOM   268  C  CZ   . ARG   A 1 46  ? -0.13700 15.00400  12.43400 1.000 80.03086  ?  151 ARG   A CZ   1 
ATOM   269  N  NH1  . ARG   A 1 46  ? -1.13900 15.07200  13.30100 1.000 81.13784  ?  151 ARG   A NH1  1 
ATOM   270  N  NH2  . ARG   A 1 46  ? -0.35500 14.53700  11.21200 1.000 79.60657  ?  151 ARG   A NH2  1 
ATOM   271  N  N    . ASP   A 1 47  ? 1.99500  12.16700  16.50200 1.000 49.33004  ?  152 ASP   A N    1 
ATOM   272  C  CA   . ASP   A 1 47  ? 0.97800  11.13500  16.34800 1.000 50.58566  ?  152 ASP   A CA   1 
ATOM   273  C  C    . ASP   A 1 47  ? 0.85900  10.23700  17.57100 1.000 48.10326  ?  152 ASP   A C    1 
ATOM   274  O  O    . ASP   A 1 47  ? -0.13300 9.51000   17.69300 1.000 45.13858  ?  152 ASP   A O    1 
ATOM   275  C  CB   . ASP   A 1 47  ? 1.27800  10.27700  15.11800 1.000 54.40521  ?  152 ASP   A CB   1 
ATOM   276  C  CG   . ASP   A 1 47  ? 1.23400  11.07300  13.82800 1.000 60.34213  ?  152 ASP   A CG   1 
ATOM   277  O  OD1  . ASP   A 1 47  ? 0.55300  12.11900  13.79600 1.000 61.12041  ?  152 ASP   A OD1  1 
ATOM   278  O  OD2  . ASP   A 1 47  ? 1.88400  10.65300  12.84900 1.000 61.42760  ?  152 ASP   A OD2  1 
ATOM   279  N  N    . PHE   A 1 48  ? 1.84000  10.26400  18.47000 1.000 41.36458  ?  153 PHE   A N    1 
ATOM   280  C  CA   . PHE   A 1 48  ? 1.79800  9.41000   19.64500 1.000 37.64416  ?  153 PHE   A CA   1 
ATOM   281  C  C    . PHE   A 1 48  ? 0.74800  9.91400   20.63000 1.000 41.15725  ?  153 PHE   A C    1 
ATOM   282  O  O    . PHE   A 1 48  ? 0.34200  11.08000  20.60600 1.000 42.88791  ?  153 PHE   A O    1 
ATOM   283  C  CB   . PHE   A 1 48  ? 3.16100  9.36600   20.34300 1.000 34.10438  ?  153 PHE   A CB   1 
ATOM   284  C  CG   . PHE   A 1 48  ? 4.30900  8.99300   19.44400 1.000 35.48757  ?  153 PHE   A CG   1 
ATOM   285  C  CD1  . PHE   A 1 48  ? 5.60400  9.34600   19.79000 1.000 36.44494  ?  153 PHE   A CD1  1 
ATOM   286  C  CD2  . PHE   A 1 48  ? 4.10600  8.27700   18.27400 1.000 36.43734  ?  153 PHE   A CD2  1 
ATOM   287  C  CE1  . PHE   A 1 48  ? 6.66900  9.00900   18.98200 1.000 37.11229  ?  153 PHE   A CE1  1 
ATOM   288  C  CE2  . PHE   A 1 48  ? 5.17000  7.93800   17.45900 1.000 36.66374  ?  153 PHE   A CE2  1 
ATOM   289  C  CZ   . PHE   A 1 48  ? 6.45300  8.30300   17.81500 1.000 39.57666  ?  153 PHE   A CZ   1 
ATOM   290  N  N    . ARG   A 1 49  ? 0.30800  9.01600   21.50500 1.000 38.02103  ?  154 ARG   A N    1 
ATOM   291  C  CA   . ARG   A 1 49  ? -0.49800 9.44500   22.63600 1.000 42.83081  ?  154 ARG   A CA   1 
ATOM   292  C  C    . ARG   A 1 49  ? 0.30600  10.44000  23.47000 1.000 46.40272  ?  154 ARG   A C    1 
ATOM   293  O  O    . ARG   A 1 49  ? 1.51400  10.25300  23.66400 1.000 43.53625  ?  154 ARG   A O    1 
ATOM   294  C  CB   . ARG   A 1 49  ? -0.92500 8.24700   23.48600 1.000 43.59115  ?  154 ARG   A CB   1 
ATOM   295  C  CG   . ARG   A 1 49  ? -2.04500 7.42100   22.86000 1.000 46.11744  ?  154 ARG   A CG   1 
ATOM   296  C  CD   . ARG   A 1 49  ? -2.22300 6.08800   23.56900 1.000 46.72388  ?  154 ARG   A CD   1 
ATOM   297  N  NE   . ARG   A 1 49  ? -1.13300 5.16500   23.26700 1.000 43.48188  ?  154 ARG   A NE   1 
ATOM   298  C  CZ   . ARG   A 1 49  ? -0.96400 3.98800   23.85900 1.000 41.66796  ?  154 ARG   A CZ   1 
ATOM   299  N  NH1  . ARG   A 1 49  ? -1.81500 3.58300   24.79000 1.000 42.39742  ?  154 ARG   A NH1  1 
ATOM   300  N  NH2  . ARG   A 1 49  ? 0.05700  3.21300   23.51900 1.000 38.85338  ?  154 ARG   A NH2  1 
ATOM   301  N  N    . PRO   A 1 50  ? -0.32100 11.51100  23.96200 1.000 52.07994  ?  155 PRO   A N    1 
ATOM   302  C  CA   . PRO   A 1 50  ? 0.45600  12.62200  24.50600 1.000 51.97072  ?  155 PRO   A CA   1 
ATOM   303  C  C    . PRO   A 1 50  ? 1.18400  12.21700  25.77600 1.000 54.56056  ?  155 PRO   A C    1 
ATOM   304  O  O    . PRO   A 1 50  ? 0.70300  11.36400  26.54100 1.000 50.93346  ?  155 PRO   A O    1 
ATOM   305  C  CB   . PRO   A 1 50  ? -0.61100 13.69400  24.79100 1.000 54.48465  ?  155 PRO   A CB   1 
ATOM   306  C  CG   . PRO   A 1 50  ? -1.88100 12.92900  24.94700 1.000 58.31708  ?  155 PRO   A CG   1 
ATOM   307  C  CD   . PRO   A 1 50  ? -1.76900 11.77600  23.99500 1.000 55.26814  ?  155 PRO   A CD   1 
ATOM   308  N  N    . PRO   A 1 51  ? 2.35000  12.80200  26.03900 1.000 53.12942  ?  156 PRO   A N    1 
ATOM   309  C  CA   . PRO   A 1 51  ? 3.01400  12.55700  27.32200 1.000 54.87179  ?  156 PRO   A CA   1 
ATOM   310  C  C    . PRO   A 1 51  ? 2.28700  13.28100  28.44000 1.000 55.19060  ?  156 PRO   A C    1 
ATOM   311  O  O    . PRO   A 1 51  ? 1.85500  14.42600  28.28900 1.000 53.66590  ?  156 PRO   A O    1 
ATOM   312  C  CB   . PRO   A 1 51  ? 4.42700  13.11500  27.11500 1.000 53.64592  ?  156 PRO   A CB   1 
ATOM   313  C  CG   . PRO   A 1 51  ? 4.32400  14.06500  25.97200 1.000 55.14121  ?  156 PRO   A CG   1 
ATOM   314  C  CD   . PRO   A 1 51  ? 3.05500  13.79600  25.21200 1.000 55.72936  ?  156 PRO   A CD   1 
ATOM   315  N  N    . VAL   A 1 52  ? 2.14200  12.59400  29.56700 1.000 56.10696  ?  157 VAL   A N    1 
ATOM   316  C  CA   . VAL   A 1 52  ? 1.52600  13.15500  30.76000 1.000 60.16524  ?  157 VAL   A CA   1 
ATOM   317  C  C    . VAL   A 1 52  ? 2.51800  12.99900  31.90100 1.000 65.12973  ?  157 VAL   A C    1 
ATOM   318  O  O    . VAL   A 1 52  ? 2.86200  11.87300  32.28100 1.000 59.44375  ?  157 VAL   A O    1 
ATOM   319  C  CB   . VAL   A 1 52  ? 0.18900  12.47300  31.09100 1.000 61.47200  ?  157 VAL   A CB   1 
ATOM   320  C  CG1  . VAL   A 1 52  ? -0.34300 12.95800  32.43300 1.000 65.74888  ?  157 VAL   A CG1  1 
ATOM   321  C  CG2  . VAL   A 1 52  ? -0.82700 12.72400  29.98900 1.000 63.28124  ?  157 VAL   A CG2  1 
ATOM   322  N  N    . ARG   A 1 53  ? 2.98200  14.12300  32.43600 1.000 71.83924  ?  158 ARG   A N    1 
ATOM   323  C  CA   . ARG   A 1 53  ? 3.91700  14.14300  33.55600 1.000 75.35054  ?  158 ARG   A CA   1 
ATOM   324  C  C    . ARG   A 1 53  ? 3.14900  14.62700  34.78300 1.000 84.50675  ?  158 ARG   A C    1 
ATOM   325  O  O    . ARG   A 1 53  ? 2.91800  15.82700  34.95000 1.000 86.78434  ?  158 ARG   A O    1 
ATOM   326  C  CB   . ARG   A 1 53  ? 5.11700  15.03300  33.24500 1.000 72.45506  ?  158 ARG   A CB   1 
ATOM   327  C  CG   . ARG   A 1 53  ? 6.15800  14.37500  32.34700 1.000 66.84226  ?  158 ARG   A CG   1 
ATOM   328  C  CD   . ARG   A 1 53  ? 6.39900  15.18800  31.08300 1.000 65.39160  ?  158 ARG   A CD   1 
ATOM   329  N  NE   . ARG   A 1 53  ? 7.40400  14.57000  30.22200 1.000 62.74237  ?  158 ARG   A NE   1 
ATOM   330  C  CZ   . ARG   A 1 53  ? 7.54400  14.83000  28.92600 1.000 57.70221  ?  158 ARG   A CZ   1 
ATOM   331  N  NH1  . ARG   A 1 53  ? 6.74000  15.70000  28.33000 1.000 53.39334  ?  158 ARG   A NH1  1 
ATOM   332  N  NH2  . ARG   A 1 53  ? 8.48700  14.21700  28.22400 1.000 51.26363  ?  158 ARG   A NH2  1 
ATOM   333  N  N    . MET   A 1 54  ? 2.74900  13.68700  35.63300 1.000 92.33196  ?  159 MET   A N    1 
ATOM   334  C  CA   . MET   A 1 54  ? 1.97200  13.99900  36.82300 1.000 101.85142 ?  159 MET   A CA   1 
ATOM   335  C  C    . MET   A 1 54  ? 2.50700  13.25900  38.04400 1.000 103.96411 ?  159 MET   A C    1 
ATOM   336  O  O    . MET   A 1 54  ? 1.73800  12.81100  38.89500 1.000 106.82554 ?  159 MET   A O    1 
ATOM   337  C  CB   . MET   A 1 54  ? 0.49800  13.66000  36.60600 1.000 105.64673 ?  159 MET   A CB   1 
ATOM   338  C  CG   . MET   A 1 54  ? -0.31900 14.79100  36.00100 1.000 110.98064 ?  159 MET   A CG   1 
ATOM   339  S  SD   . MET   A 1 54  ? -2.08200 14.42100  35.88900 1.000 116.71271 ?  159 MET   A SD   1 
ATOM   340  C  CE   . MET   A 1 54  ? -2.06700 12.63000  35.91500 1.000 112.31020 ?  159 MET   A CE   1 
ATOM   341  N  N    . PRO   A 1 67  ? 0.61500  5.21900   38.91300 1.000 91.22024  ?  219 PRO   A N    1 
ATOM   342  C  CA   . PRO   A 1 67  ? -0.22700 5.68700   37.80600 1.000 88.68060  ?  219 PRO   A CA   1 
ATOM   343  C  C    . PRO   A 1 67  ? 0.37900  5.37400   36.44100 1.000 82.97305  ?  219 PRO   A C    1 
ATOM   344  O  O    . PRO   A 1 67  ? -0.35900 5.08800   35.49700 1.000 88.18580  ?  219 PRO   A O    1 
ATOM   345  C  CB   . PRO   A 1 67  ? -0.30600 7.20600   38.03100 1.000 90.60852  ?  219 PRO   A CB   1 
ATOM   346  C  CG   . PRO   A 1 67  ? 0.35200  7.46800   39.36200 1.000 93.63614  ?  219 PRO   A CG   1 
ATOM   347  C  CD   . PRO   A 1 67  ? 1.28200  6.33200   39.60500 1.000 93.06867  ?  219 PRO   A CD   1 
ATOM   348  N  N    . LEU   A 1 68  ? 1.71000  5.42900   36.35400 1.000 70.70310  ?  220 LEU   A N    1 
ATOM   349  C  CA   . LEU   A 1 68  ? 2.44200  5.15900   35.11300 1.000 60.03224  ?  220 LEU   A CA   1 
ATOM   350  C  C    . LEU   A 1 68  ? 1.96700  6.07800   33.98700 1.000 50.81568  ?  220 LEU   A C    1 
ATOM   351  O  O    . LEU   A 1 68  ? 1.60700  5.63500   32.89500 1.000 44.79935  ?  220 LEU   A O    1 
ATOM   352  C  CB   . LEU   A 1 68  ? 2.32600  3.68500   34.71300 1.000 61.28770  ?  220 LEU   A CB   1 
ATOM   353  C  CG   . LEU   A 1 68  ? 2.85100  2.64300   35.70500 1.000 63.58181  ?  220 LEU   A CG   1 
ATOM   354  C  CD1  . LEU   A 1 68  ? 3.21100  1.35500   34.98100 1.000 59.12056  ?  220 LEU   A CD1  1 
ATOM   355  C  CD2  . LEU   A 1 68  ? 4.04800  3.17200   36.48500 1.000 63.80074  ?  220 LEU   A CD2  1 
ATOM   356  N  N    . SER   A 1 69  ? 1.99400  7.38400   34.26200 1.000 51.99101  ?  221 SER   A N    1 
ATOM   357  C  CA   . SER   A 1 69  ? 1.39900  8.36600   33.36300 1.000 54.67816  ?  221 SER   A CA   1 
ATOM   358  C  C    . SER   A 1 69  ? 2.12200  8.47300   32.02600 1.000 53.48542  ?  221 SER   A C    1 
ATOM   359  O  O    . SER   A 1 69  ? 1.55400  9.02200   31.07600 1.000 51.00650  ?  221 SER   A O    1 
ATOM   360  C  CB   . SER   A 1 69  ? 1.36600  9.73500   34.04200 1.000 61.64397  ?  221 SER   A CB   1 
ATOM   361  O  OG   . SER   A 1 69  ? 2.64700  10.08400  34.54200 1.000 60.83856  ?  221 SER   A OG   1 
ATOM   362  N  N    . MET   A 1 70  ? 3.35300  7.97400   31.92700 1.000 49.05259  ?  222 MET   A N    1 
ATOM   363  C  CA   . MET   A 1 70  ? 4.12700  8.06200   30.69600 1.000 44.80576  ?  222 MET   A CA   1 
ATOM   364  C  C    . MET   A 1 70  ? 4.10500  6.77500   29.88300 1.000 41.11836  ?  222 MET   A C    1 
ATOM   365  O  O    . MET   A 1 70  ? 4.69300  6.73800   28.79700 1.000 42.51729  ?  222 MET   A O    1 
ATOM   366  C  CB   . MET   A 1 70  ? 5.57800  8.44600   31.01000 1.000 48.47989  ?  222 MET   A CB   1 
ATOM   367  C  CG   . MET   A 1 70  ? 5.78400  9.92200   31.32300 1.000 52.66713  ?  222 MET   A CG   1 
ATOM   368  S  SD   . MET   A 1 70  ? 5.39600  11.01900  29.94400 1.000 47.25194  ?  222 MET   A SD   1 
ATOM   369  C  CE   . MET   A 1 70  ? 6.80500  10.72700  28.87900 1.000 44.35138  ?  222 MET   A CE   1 
ATOM   370  N  N    . LEU   A 1 71  ? 3.44900  5.72600   30.37600 1.000 42.06880  ?  223 LEU   A N    1 
ATOM   371  C  CA   . LEU   A 1 71  ? 3.40900  4.46300   29.63900 1.000 39.16972  ?  223 LEU   A CA   1 
ATOM   372  C  C    . LEU   A 1 71  ? 2.77900  4.58900   28.25600 1.000 36.35014  ?  223 LEU   A C    1 
ATOM   373  O  O    . LEU   A 1 71  ? 3.35200  4.04500   27.29600 1.000 38.41796  ?  223 LEU   A O    1 
ATOM   374  C  CB   . LEU   A 1 71  ? 2.69100  3.39800   30.47300 1.000 39.69082  ?  223 LEU   A CB   1 
ATOM   375  C  CG   . LEU   A 1 71  ? 2.69100  1.99800   29.85100 1.000 42.06275  ?  223 LEU   A CG   1 
ATOM   376  C  CD1  . LEU   A 1 71  ? 4.10300  1.58000   29.45100 1.000 39.78527  ?  223 LEU   A CD1  1 
ATOM   377  C  CD2  . LEU   A 1 71  ? 2.06000  0.97400   30.78800 1.000 41.88797  ?  223 LEU   A CD2  1 
ATOM   378  N  N    . PRO   A 1 72  ? 1.62800  5.25100   28.06900 1.000 36.05710  ?  224 PRO   A N    1 
ATOM   379  C  CA   . PRO   A 1 72  ? 1.06000  5.31800   26.70800 1.000 38.07987  ?  224 PRO   A CA   1 
ATOM   380  C  C    . PRO   A 1 72  ? 1.97400  6.00300   25.70500 1.000 39.28821  ?  224 PRO   A C    1 
ATOM   381  O  O    . PRO   A 1 72  ? 2.15600  5.49800   24.58900 1.000 36.87859  ?  224 PRO   A O    1 
ATOM   382  C  CB   . PRO   A 1 72  ? -0.25000 6.09300   26.91600 1.000 42.76963  ?  224 PRO   A CB   1 
ATOM   383  C  CG   . PRO   A 1 72  ? -0.58700 5.89800   28.34700 1.000 44.10812  ?  224 PRO   A CG   1 
ATOM   384  C  CD   . PRO   A 1 72  ? 0.73100  5.88300   29.05500 1.000 38.69450  ?  224 PRO   A CD   1 
ATOM   385  N  N    . HIS   A 1 73  ? 2.55700  7.14500   26.07200 1.000 40.42990  ?  225 HIS   A N    1 
ATOM   386  C  CA   . HIS   A 1 73  ? 3.44000  7.85400   25.15200 1.000 43.51639  ?  225 HIS   A CA   1 
ATOM   387  C  C    . HIS   A 1 73  ? 4.69400  7.04000   24.85800 1.000 36.42022  ?  225 HIS   A C    1 
ATOM   388  O  O    . HIS   A 1 73  ? 5.11700  6.92300   23.70100 1.000 37.07078  ?  225 HIS   A O    1 
ATOM   389  C  CB   . HIS   A 1 73  ? 3.80900  9.22200   25.72800 1.000 43.22148  ?  225 HIS   A CB   1 
ATOM   390  C  CG   . HIS   A 1 73  ? 4.68200  10.03900  24.82800 1.000 43.01383  ?  225 HIS   A CG   1 
ATOM   391  N  ND1  . HIS   A 1 73  ? 4.19300  10.72100  23.73400 1.000 40.54257  ?  225 HIS   A ND1  1 
ATOM   392  C  CD2  . HIS   A 1 73  ? 6.01500  10.27800  24.85600 1.000 40.59136  ?  225 HIS   A CD2  1 
ATOM   393  C  CE1  . HIS   A 1 73  ? 5.18600  11.34900  23.13000 1.000 40.65482  ?  225 HIS   A CE1  1 
ATOM   394  N  NE2  . HIS   A 1 73  ? 6.30200  11.09600  23.79000 1.000 41.28703  ?  225 HIS   A NE2  1 
ATOM   395  N  N    . LEU   A 1 74  ? 5.30300  6.46300   25.89700 1.000 35.55927  ?  226 LEU   A N    1 
ATOM   396  C  CA   . LEU   A 1 74  ? 6.53200  5.70200   25.69700 1.000 36.49756  ?  226 LEU   A CA   1 
ATOM   397  C  C    . LEU   A 1 74  ? 6.26800  4.38000   24.98900 1.000 33.85456  ?  226 LEU   A C    1 
ATOM   398  O  O    . LEU   A 1 74  ? 7.15400  3.86600   24.29600 1.000 33.83244  ?  226 LEU   A O    1 
ATOM   399  C  CB   . LEU   A 1 74  ? 7.23200  5.46400   27.03500 1.000 40.85525  ?  226 LEU   A CB   1 
ATOM   400  C  CG   . LEU   A 1 74  ? 7.83000  6.70500   27.70300 1.000 45.37351  ?  226 LEU   A CG   1 
ATOM   401  C  CD1  . LEU   A 1 74  ? 8.90700  6.31600   28.70200 1.000 43.41045  ?  226 LEU   A CD1  1 
ATOM   402  C  CD2  . LEU   A 1 74  ? 8.37900  7.67200   26.66300 1.000 42.02260  ?  226 LEU   A CD2  1 
ATOM   403  N  N    . ALA   A 1 75  ? 5.06900  3.81200   25.14700 1.000 34.60400  ?  227 ALA   A N    1 
ATOM   404  C  CA   . ALA   A 1 75  ? 4.72400  2.61500   24.38600 1.000 29.19679  ?  227 ALA   A CA   1 
ATOM   405  C  C    . ALA   A 1 75  ? 4.62700  2.92400   22.89800 1.000 30.96945  ?  227 ALA   A C    1 
ATOM   406  O  O    . ALA   A 1 75  ? 5.09400  2.14100   22.06400 1.000 31.41410  ?  227 ALA   A O    1 
ATOM   407  C  CB   . ALA   A 1 75  ? 3.41200  2.01700   24.89500 1.000 29.37422  ?  227 ALA   A CB   1 
ATOM   408  N  N    . ASP   A 1 76  ? 4.02100  4.06200   22.54900 1.000 35.13004  ?  228 ASP   A N    1 
ATOM   409  C  CA   . ASP   A 1 76  ? 3.94100  4.45900   21.14600 1.000 33.27197  ?  228 ASP   A CA   1 
ATOM   410  C  C    . ASP   A 1 76  ? 5.31600  4.81000   20.59300 1.000 31.45780  ?  228 ASP   A C    1 
ATOM   411  O  O    . ASP   A 1 76  ? 5.62900  4.48800   19.44000 1.000 32.09628  ?  228 ASP   A O    1 
ATOM   412  C  CB   . ASP   A 1 76  ? 2.98800  5.64300   20.99200 1.000 33.26673  ?  228 ASP   A CB   1 
ATOM   413  C  CG   . ASP   A 1 76  ? 1.53500  5.24900   21.16900 1.000 38.51593  ?  228 ASP   A CG   1 
ATOM   414  O  OD1  . ASP   A 1 76  ? 0.70800  6.14200   21.44500 1.000 39.07628  ?  228 ASP   A OD1  1 
ATOM   415  O  OD2  . ASP   A 1 76  ? 1.22100  4.04700   21.03100 1.000 37.36429  ?  228 ASP   A OD2  1 
ATOM   416  N  N    . LEU   A 1 77  ? 6.14400  5.48000   21.39700 1.000 31.23666  ?  229 LEU   A N    1 
ATOM   417  C  CA   . LEU   A 1 77  ? 7.50000  5.81600   20.97000 1.000 29.98811  ?  229 LEU   A CA   1 
ATOM   418  C  C    . LEU   A 1 77  ? 8.30900  4.55800   20.67400 1.000 31.00956  ?  229 LEU   A C    1 
ATOM   419  O  O    . LEU   A 1 77  ? 8.96200  4.45600   19.62800 1.000 29.99773  ?  229 LEU   A O    1 
ATOM   420  C  CB   . LEU   A 1 77  ? 8.17900  6.66400   22.04700 1.000 29.94228  ?  229 LEU   A CB   1 
ATOM   421  C  CG   . LEU   A 1 77  ? 9.67400  6.96400   21.92100 1.000 33.44995  ?  229 LEU   A CG   1 
ATOM   422  C  CD1  . LEU   A 1 77  ? 9.97700  7.70400   20.62800 1.000 34.57077  ?  229 LEU   A CD1  1 
ATOM   423  C  CD2  . LEU   A 1 77  ? 10.14700 7.76600   23.12200 1.000 37.77573  ?  229 LEU   A CD2  1 
ATOM   424  N  N    . VAL   A 1 78  ? 8.26900  3.58300   21.58500 1.000 31.28064  ?  230 VAL   A N    1 
ATOM   425  C  CA   . VAL   A 1 78  ? 9.00100  2.33500   21.38300 1.000 29.35231  ?  230 VAL   A CA   1 
ATOM   426  C  C    . VAL   A 1 78  ? 8.45400  1.58400   20.17700 1.000 32.90617  ?  230 VAL   A C    1 
ATOM   427  O  O    . VAL   A 1 78  ? 9.21300  1.07300   19.34400 1.000 32.42169  ?  230 VAL   A O    1 
ATOM   428  C  CB   . VAL   A 1 78  ? 8.94500  1.47200   22.65600 1.000 34.15789  ?  230 VAL   A CB   1 
ATOM   429  C  CG1  . VAL   A 1 78  ? 9.35500  0.03900   22.34700 1.000 34.83916  ?  230 VAL   A CG1  1 
ATOM   430  C  CG2  . VAL   A 1 78  ? 9.83600  2.06400   23.72700 1.000 38.84686  ?  230 VAL   A CG2  1 
ATOM   431  N  N    . SER   A 1 79  ? 7.12500  1.50200   20.06800 1.000 30.88298  ?  231 SER   A N    1 
ATOM   432  C  CA   . SER   A 1 79  ? 6.51000  0.81100   18.93900 1.000 27.99084  ?  231 SER   A CA   1 
ATOM   433  C  C    . SER   A 1 79  ? 6.91800  1.44900   17.61700 1.000 30.01627  ?  231 SER   A C    1 
ATOM   434  O  O    . SER   A 1 79  ? 7.25000  0.74900   16.65400 1.000 29.79597  ?  231 SER   A O    1 
ATOM   435  C  CB   . SER   A 1 79  ? 4.99000  0.81600   19.09600 1.000 28.91918  ?  231 SER   A CB   1 
ATOM   436  O  OG   . SER   A 1 79  ? 4.36800  -0.03900  18.15300 1.000 35.36391  ?  231 SER   A OG   1 
ATOM   437  N  N    . TYR   A 1 80  ? 6.90700  2.78200   17.55900 1.000 27.25019  ?  232 TYR   A N    1 
ATOM   438  C  CA   . TYR   A 1 80  ? 7.37900  3.49800   16.37800 1.000 25.72069  ?  232 TYR   A CA   1 
ATOM   439  C  C    . TYR   A 1 80  ? 8.81600  3.12200   16.04100 1.000 28.41935  ?  232 TYR   A C    1 
ATOM   440  O  O    . TYR   A 1 80  ? 9.15900  2.91900   14.87000 1.000 26.27906  ?  232 TYR   A O    1 
ATOM   441  C  CB   . TYR   A 1 80  ? 7.25300  5.00200   16.62500 1.000 31.25602  ?  232 TYR   A CB   1 
ATOM   442  C  CG   . TYR   A 1 80  ? 7.81000  5.90600   15.54800 1.000 35.60860  ?  232 TYR   A CG   1 
ATOM   443  C  CD1  . TYR   A 1 80  ? 7.06600  6.21300   14.41700 1.000 35.07386  ?  232 TYR   A CD1  1 
ATOM   444  C  CD2  . TYR   A 1 80  ? 9.06800  6.48200   15.68200 1.000 39.29261  ?  232 TYR   A CD2  1 
ATOM   445  C  CE1  . TYR   A 1 80  ? 7.56700  7.05200   13.44000 1.000 38.78497  ?  232 TYR   A CE1  1 
ATOM   446  C  CE2  . TYR   A 1 80  ? 9.57600  7.32300   14.71100 1.000 38.49033  ?  232 TYR   A CE2  1 
ATOM   447  C  CZ   . TYR   A 1 80  ? 8.82100  7.60500   13.59400 1.000 38.47189  ?  232 TYR   A CZ   1 
ATOM   448  O  OH   . TYR   A 1 80  ? 9.32000  8.44100   12.62300 1.000 43.83806  ?  232 TYR   A OH   1 
ATOM   449  N  N    . SER   A 1 81  ? 9.67000  3.00700   17.05600 1.000 32.32647  ?  233 SER   A N    1 
ATOM   450  C  CA   . SER   A 1 81  ? 11.08000 2.76000   16.78600 1.000 30.28205  ?  233 SER   A CA   1 
ATOM   451  C  C    . SER   A 1 81  ? 11.34000 1.31500   16.38500 1.000 31.19500  ?  233 SER   A C    1 
ATOM   452  O  O    . SER   A 1 81  ? 12.25500 1.05400   15.59600 1.000 29.70660  ?  233 SER   A O    1 
ATOM   453  C  CB   . SER   A 1 81  ? 11.91100 3.14900   18.00000 1.000 43.11113  ?  233 SER   A CB   1 
ATOM   454  O  OG   . SER   A 1 81  ? 11.69000 4.51700   18.28700 1.000 47.48164  ?  233 SER   A OG   1 
ATOM   455  N  N    . ILE   A 1 82  ? 10.55100 0.36800   16.90000 1.000 27.87287  ?  234 ILE   A N    1 
ATOM   456  C  CA   . ILE   A 1 82  ? 10.65800 -1.01100  16.43000 1.000 31.62992  ?  234 ILE   A CA   1 
ATOM   457  C  C    . ILE   A 1 82  ? 10.44300 -1.06800  14.92300 1.000 33.02972  ?  234 ILE   A C    1 
ATOM   458  O  O    . ILE   A 1 82  ? 11.17000 -1.76400  14.20300 1.000 29.61714  ?  234 ILE   A O    1 
ATOM   459  C  CB   . ILE   A 1 82  ? 9.66600  -1.91700  17.18300 1.000 29.56798  ?  234 ILE   A CB   1 
ATOM   460  C  CG1  . ILE   A 1 82  ? 10.08000 -2.06700  18.64700 1.000 29.88237  ?  234 ILE   A CG1  1 
ATOM   461  C  CG2  . ILE   A 1 82  ? 9.58200  -3.28200  16.51900 1.000 27.57514  ?  234 ILE   A CG2  1 
ATOM   462  C  CD1  . ILE   A 1 82  ? 8.99700  -2.66900  19.53100 1.000 32.12698  ?  234 ILE   A CD1  1 
ATOM   463  N  N    . GLN   A 1 83  ? 9.45200  -0.32100  14.42100 1.000 28.88052  ?  235 GLN   A N    1 
ATOM   464  C  CA   . GLN   A 1 83  ? 9.21700  -0.26000  12.98000 1.000 30.49243  ?  235 GLN   A CA   1 
ATOM   465  C  C    . GLN   A 1 83  ? 10.42800 0.29000   12.24000 1.000 30.31884  ?  235 GLN   A C    1 
ATOM   466  O  O    . GLN   A 1 83  ? 10.78900 -0.21000  11.16800 1.000 28.32024  ?  235 GLN   A O    1 
ATOM   467  C  CB   . GLN   A 1 83  ? 7.99100  0.60200   12.67800 1.000 29.07152  ?  235 GLN   A CB   1 
ATOM   468  C  CG   . GLN   A 1 83  ? 6.71700  0.13800   13.34600 1.000 30.70257  ?  235 GLN   A CG   1 
ATOM   469  C  CD   . GLN   A 1 83  ? 5.49900  0.86900   12.82100 1.000 34.60702  ?  235 GLN   A CD   1 
ATOM   470  O  OE1  . GLN   A 1 83  ? 5.31200  0.99300   11.61000 1.000 38.69292  ?  235 GLN   A OE1  1 
ATOM   471  N  NE2  . GLN   A 1 83  ? 4.66300  1.35900   13.73000 1.000 40.32791  ?  235 GLN   A NE2  1 
ATOM   472  N  N    . LYS   A 1 84  ? 11.05400 1.33700   12.78400 1.000 31.01001  ?  236 LYS   A N    1 
ATOM   473  C  CA   . LYS   A 1 84  ? 12.24900 1.89000   12.15500 1.000 30.58946  ?  236 LYS   A CA   1 
ATOM   474  C  C    . LYS   A 1 84  ? 13.40100 0.89300   12.18800 1.000 30.72178  ?  236 LYS   A C    1 
ATOM   475  O  O    . LYS   A 1 84  ? 14.16400 0.78200   11.22100 1.000 28.25875  ?  236 LYS   A O    1 
ATOM   476  C  CB   . LYS   A 1 84  ? 12.64700 3.19500   12.84300 1.000 26.30185  ?  236 LYS   A CB   1 
ATOM   477  C  CG   . LYS   A 1 84  ? 11.57000 4.27000   12.80100 1.000 33.79699  ?  236 LYS   A CG   1 
ATOM   478  C  CD   . LYS   A 1 84  ? 11.01500 4.43500   11.39400 1.000 37.98099  ?  236 LYS   A CD   1 
ATOM   479  C  CE   . LYS   A 1 84  ? 10.50800 5.84700   11.16000 1.000 42.06775  ?  236 LYS   A CE   1 
ATOM   480  N  NZ   . LYS   A 1 84  ? 11.55400 6.87200   11.43400 1.000 42.98616  ?  236 LYS   A NZ   1 
ATOM   481  N  N    . VAL   A 1 85  ? 13.53800 0.15400   13.29200 1.000 26.38936  ?  237 VAL   A N    1 
ATOM   482  C  CA   . VAL   A 1 85  ? 14.61200 -0.83000  13.40400 1.000 28.32247  ?  237 VAL   A CA   1 
ATOM   483  C  C    . VAL   A 1 85  ? 14.43100 -1.93900  12.37600 1.000 28.92096  ?  237 VAL   A C    1 
ATOM   484  O  O    . VAL   A 1 85  ? 15.40300 -2.41300  11.77500 1.000 30.05455  ?  237 VAL   A O    1 
ATOM   485  C  CB   . VAL   A 1 85  ? 14.67600 -1.38600  14.83900 1.000 30.45995  ?  237 VAL   A CB   1 
ATOM   486  C  CG1  . VAL   A 1 85  ? 15.60200 -2.59200  14.90800 1.000 29.01799  ?  237 VAL   A CG1  1 
ATOM   487  C  CG2  . VAL   A 1 85  ? 15.14000 -0.30500  15.80100 1.000 31.06129  ?  237 VAL   A CG2  1 
ATOM   488  N  N    . ILE   A 1 86  ? 13.18600 -2.36700  12.15000 1.000 27.96381  ?  238 ILE   A N    1 
ATOM   489  C  CA   . ILE   A 1 86  ? 12.92700 -3.39600  11.14500 1.000 28.47240  ?  238 ILE   A CA   1 
ATOM   490  C  C    . ILE   A 1 86  ? 13.30600 -2.89500  9.75700  1.000 28.30226  ?  238 ILE   A C    1 
ATOM   491  O  O    . ILE   A 1 86  ? 13.90100 -3.62800  8.95800  1.000 33.81582  ?  238 ILE   A O    1 
ATOM   492  C  CB   . ILE   A 1 86  ? 11.45400 -3.84300  11.20500 1.000 29.92915  ?  238 ILE   A CB   1 
ATOM   493  C  CG1  . ILE   A 1 86  ? 11.16300 -4.54600  12.53300 1.000 34.64441  ?  238 ILE   A CG1  1 
ATOM   494  C  CG2  . ILE   A 1 86  ? 11.12000 -4.75500  10.03600 1.000 36.01849  ?  238 ILE   A CG2  1 
ATOM   495  C  CD1  . ILE   A 1 86  ? 9.70800  -4.47500  12.95600 1.000 33.40060  ?  238 ILE   A CD1  1 
ATOM   496  N  N    . GLY   A 1 87  ? 12.97300 -1.63900  9.44900  1.000 29.73711  ?  239 GLY   A N    1 
ATOM   497  C  CA   . GLY   A 1 87  ? 13.31400 -1.09400  8.14400  1.000 30.69450  ?  239 GLY   A CA   1 
ATOM   498  C  C    . GLY   A 1 87  ? 14.81200 -1.01400  7.92100  1.000 31.89788  ?  239 GLY   A C    1 
ATOM   499  O  O    . GLY   A 1 87  ? 15.29800 -1.24200  6.81000  1.000 31.99658  ?  239 GLY   A O    1 
ATOM   500  N  N    . PHE   A 1 88  ? 15.56300 -0.68900  8.97400  1.000 31.71278  ?  240 PHE   A N    1 
ATOM   501  C  CA   . PHE   A 1 88  ? 17.01900 -0.68500  8.87800  1.000 27.87752  ?  240 PHE   A CA   1 
ATOM   502  C  C    . PHE   A 1 88  ? 17.55500 -2.09800  8.68500  1.000 30.41976  ?  240 PHE   A C    1 
ATOM   503  O  O    . PHE   A 1 88  ? 18.40000 -2.34100  7.81400  1.000 34.53230  ?  240 PHE   A O    1 
ATOM   504  C  CB   . PHE   A 1 88  ? 17.61400 -0.03700  10.13200 1.000 27.28570  ?  240 PHE   A CB   1 
ATOM   505  C  CG   . PHE   A 1 88  ? 19.12100 -0.07400  10.19700 1.000 31.93454  ?  240 PHE   A CG   1 
ATOM   506  C  CD1  . PHE   A 1 88  ? 19.88100 0.88400   9.54400  1.000 31.90388  ?  240 PHE   A CD1  1 
ATOM   507  C  CD2  . PHE   A 1 88  ? 19.77400 -1.04800  10.93800 1.000 33.82457  ?  240 PHE   A CD2  1 
ATOM   508  C  CE1  . PHE   A 1 88  ? 21.26500 0.86200   9.61200  1.000 32.38892  ?  240 PHE   A CE1  1 
ATOM   509  C  CE2  . PHE   A 1 88  ? 21.15600 -1.07700  11.01200 1.000 31.17739  ?  240 PHE   A CE2  1 
ATOM   510  C  CZ   . PHE   A 1 88  ? 21.90300 -0.12000  10.34800 1.000 29.38492  ?  240 PHE   A CZ   1 
ATOM   511  N  N    . ALA   A 1 89  ? 17.06000 -3.04900  9.48400  1.000 30.48902  ?  241 ALA   A N    1 
ATOM   512  C  CA   . ALA   A 1 89  ? 17.57500 -4.41400  9.43300  1.000 31.59039  ?  241 ALA   A CA   1 
ATOM   513  C  C    . ALA   A 1 89  ? 17.39900 -5.03000  8.05100  1.000 34.37440  ?  241 ALA   A C    1 
ATOM   514  O  O    . ALA   A 1 89  ? 18.28000 -5.75300  7.57000  1.000 32.38205  ?  241 ALA   A O    1 
ATOM   515  C  CB   . ALA   A 1 89  ? 16.88500 -5.27200  10.49400 1.000 29.17019  ?  241 ALA   A CB   1 
ATOM   516  N  N    . LYS   A 1 90  ? 16.26900 -4.74800  7.39200  1.000 31.48059  ?  242 LYS   A N    1 
ATOM   517  C  CA   . LYS   A 1 90  ? 16.00800 -5.30500  6.06800  1.000 33.38200  ?  242 LYS   A CA   1 
ATOM   518  C  C    . LYS   A 1 90  ? 17.04500 -4.87900  5.04000  1.000 37.69531  ?  242 LYS   A C    1 
ATOM   519  O  O    . LYS   A 1 90  ? 17.22000 -5.57000  4.03000  1.000 37.58979  ?  242 LYS   A O    1 
ATOM   520  C  CB   . LYS   A 1 90  ? 14.61300 -4.89200  5.58300  1.000 31.86520  ?  242 LYS   A CB   1 
ATOM   521  C  CG   . LYS   A 1 90  ? 13.46500 -5.50500  6.35900  1.000 43.24868  ?  242 LYS   A CG   1 
ATOM   522  C  CD   . LYS   A 1 90  ? 12.24200 -5.68700  5.46900  1.000 51.17755  ?  242 LYS   A CD   1 
ATOM   523  C  CE   . LYS   A 1 90  ? 11.81000 -4.37300  4.83900  1.000 52.11987  ?  242 LYS   A CE   1 
ATOM   524  N  NZ   . LYS   A 1 90  ? 10.36400 -4.37600  4.47300  1.000 54.71920  ?  242 LYS   A NZ   1 
ATOM   525  N  N    . MET   A 1 91  ? 17.73500 -3.76400  5.27000  1.000 37.11845  ?  243 MET   A N    1 
ATOM   526  C  CA   . MET   A 1 91  ? 18.70900 -3.24000  4.32300  1.000 39.00465  ?  243 MET   A CA   1 
ATOM   527  C  C    . MET   A 1 91  ? 20.14300 -3.63400  4.65400  1.000 36.39734  ?  243 MET   A C    1 
ATOM   528  O  O    . MET   A 1 91  ? 21.06000 -3.23200  3.93200  1.000 39.22623  ?  243 MET   A O    1 
ATOM   529  C  CB   . MET   A 1 91  ? 18.59200 -1.71500  4.24800  1.000 46.30795  ?  243 MET   A CB   1 
ATOM   530  C  CG   . MET   A 1 91  ? 17.16000 -1.22500  4.07500  1.000 52.90923  ?  243 MET   A CG   1 
ATOM   531  S  SD   . MET   A 1 91  ? 17.01600 0.56800   3.95700  1.000 54.34137  ?  243 MET   A SD   1 
ATOM   532  C  CE   . MET   A 1 91  ? 17.80700 0.87100   2.38200  1.000 54.78964  ?  243 MET   A CE   1 
ATOM   533  N  N    . ILE   A 1 92  ? 20.36200 -4.40600  5.71500  1.000 34.91029  ?  244 ILE   A N    1 
ATOM   534  C  CA   . ILE   A 1 92  ? 21.70100 -4.87500  6.06800  1.000 36.15889  ?  244 ILE   A CA   1 
ATOM   535  C  C    . ILE   A 1 92  ? 22.17100 -5.86900  5.01200  1.000 37.87570  ?  244 ILE   A C    1 
ATOM   536  O  O    . ILE   A 1 92  ? 21.46700 -6.85000  4.73400  1.000 39.42627  ?  244 ILE   A O    1 
ATOM   537  C  CB   . ILE   A 1 92  ? 21.72400 -5.51400  7.46500  1.000 35.26645  ?  244 ILE   A CB   1 
ATOM   538  C  CG1  . ILE   A 1 92  ? 21.41100 -4.47200  8.54100  1.000 29.95058  ?  244 ILE   A CG1  1 
ATOM   539  C  CG2  . ILE   A 1 92  ? 23.07600 -6.16800  7.72700  1.000 36.32021  ?  244 ILE   A CG2  1 
ATOM   540  C  CD1  . ILE   A 1 92  ? 21.17000 -5.07200  9.91400  1.000 26.44409  ?  244 ILE   A CD1  1 
ATOM   541  N  N    . PRO   A 1 93  ? 23.34300 -5.66000  4.39700  1.000 40.16949  ?  245 PRO   A N    1 
ATOM   542  C  CA   . PRO   A 1 93  ? 23.83700 -6.61800  3.39700  1.000 43.47077  ?  245 PRO   A CA   1 
ATOM   543  C  C    . PRO   A 1 93  ? 23.92400 -8.03700  3.93700  1.000 49.52989  ?  245 PRO   A C    1 
ATOM   544  O  O    . PRO   A 1 93  ? 24.64800 -8.30100  4.90100  1.000 48.62160  ?  245 PRO   A O    1 
ATOM   545  C  CB   . PRO   A 1 93  ? 25.22300 -6.06600  3.04100  1.000 47.97416  ?  245 PRO   A CB   1 
ATOM   546  C  CG   . PRO   A 1 93  ? 25.12100 -4.60200  3.31400  1.000 45.01574  ?  245 PRO   A CG   1 
ATOM   547  C  CD   . PRO   A 1 93  ? 24.21300 -4.47700  4.51200  1.000 37.29593  ?  245 PRO   A CD   1 
ATOM   548  N  N    . GLY   A 1 94  ? 23.17100 -8.95300  3.32700  1.000 53.48190  ?  246 GLY   A N    1 
ATOM   549  C  CA   . GLY   A 1 94  ? 23.15700 -10.34400 3.72300  1.000 53.30330  ?  246 GLY   A CA   1 
ATOM   550  C  C    . GLY   A 1 94  ? 22.02000 -10.74600 4.64000  1.000 52.68072  ?  246 GLY   A C    1 
ATOM   551  O  O    . GLY   A 1 94  ? 21.78800 -11.94800 4.81300  1.000 57.00964  ?  246 GLY   A O    1 
ATOM   552  N  N    . PHE   A 1 95  ? 21.30400 -9.78200  5.22600  1.000 48.20066  ?  247 PHE   A N    1 
ATOM   553  C  CA   . PHE   A 1 95  ? 20.26200 -10.11300 6.19600  1.000 43.28997  ?  247 PHE   A CA   1 
ATOM   554  C  C    . PHE   A 1 95  ? 19.14000 -10.92000 5.55600  1.000 51.76239  ?  247 PHE   A C    1 
ATOM   555  O  O    . PHE   A 1 95  ? 18.65000 -11.89200 6.14600  1.000 53.12790  ?  247 PHE   A O    1 
ATOM   556  C  CB   . PHE   A 1 95  ? 19.70800 -8.83300  6.82400  1.000 41.70729  ?  247 PHE   A CB   1 
ATOM   557  C  CG   . PHE   A 1 95  ? 18.65700 -9.07400  7.87100  1.000 40.98671  ?  247 PHE   A CG   1 
ATOM   558  C  CD1  . PHE   A 1 95  ? 19.01300 -9.43400  9.16100  1.000 39.31161  ?  247 PHE   A CD1  1 
ATOM   559  C  CD2  . PHE   A 1 95  ? 17.31100 -8.93600  7.56500  1.000 42.60117  ?  247 PHE   A CD2  1 
ATOM   560  C  CE1  . PHE   A 1 95  ? 18.04500 -9.65600  10.12600 1.000 43.95093  ?  247 PHE   A CE1  1 
ATOM   561  C  CE2  . PHE   A 1 95  ? 16.33900 -9.15500  8.52400  1.000 42.04138  ?  247 PHE   A CE2  1 
ATOM   562  C  CZ   . PHE   A 1 95  ? 16.70500 -9.51600  9.80600  1.000 42.27323  ?  247 PHE   A CZ   1 
ATOM   563  N  N    . ARG   A 1 96  ? 18.72100 -10.53300 4.35300  1.000 49.43856  ?  248 ARG   A N    1 
ATOM   564  C  CA   . ARG   A 1 96  ? 17.61600 -11.19700 3.67300  1.000 54.60929  ?  248 ARG   A CA   1 
ATOM   565  C  C    . ARG   A 1 96  ? 18.01200 -12.53900 3.06400  1.000 55.75661  ?  248 ARG   A C    1 
ATOM   566  O  O    . ARG   A 1 96  ? 17.13700 -13.26000 2.56800  1.000 60.01812  ?  248 ARG   A O    1 
ATOM   567  C  CB   . ARG   A 1 96  ? 17.01800 -10.26400 2.61200  1.000 61.93075  ?  248 ARG   A CB   1 
ATOM   568  C  CG   . ARG   A 1 96  ? 15.58200 -10.61500 2.26000  1.000 76.40180  ?  248 ARG   A CG   1 
ATOM   569  C  CD   . ARG   A 1 96  ? 14.64200 -10.35800 3.43900  1.000 81.49603  ?  248 ARG   A CD   1 
ATOM   570  N  NE   . ARG   A 1 96  ? 13.36100 -11.07000 3.37700  1.000 85.77182  ?  248 ARG   A NE   1 
ATOM   571  C  CZ   . ARG   A 1 96  ? 13.20000 -12.38400 3.23300  1.000 88.31601  ?  248 ARG   A CZ   1 
ATOM   572  N  NH1  . ARG   A 1 96  ? 11.97100 -12.88100 3.19900  1.000 86.82603  ?  248 ARG   A NH1  1 
ATOM   573  N  NH2  . ARG   A 1 96  ? 14.24000 -13.20600 3.15300  1.000 90.23614  ?  248 ARG   A NH2  1 
ATOM   574  N  N    . ASP   A 1 97  ? 19.29200 -12.91500 3.13400  1.000 56.27885  ?  249 ASP   A N    1 
ATOM   575  C  CA   . ASP   A 1 97  ? 19.70300 -14.27100 2.78500  1.000 58.84176  ?  249 ASP   A CA   1 
ATOM   576  C  C    . ASP   A 1 97  ? 19.27600 -15.29600 3.82600  1.000 56.93440  ?  249 ASP   A C    1 
ATOM   577  O  O    . ASP   A 1 97  ? 19.29900 -16.49700 3.53600  1.000 58.42798  ?  249 ASP   A O    1 
ATOM   578  C  CB   . ASP   A 1 97  ? 21.22200 -14.33500 2.60600  1.000 69.18025  ?  249 ASP   A CB   1 
ATOM   579  C  CG   . ASP   A 1 97  ? 21.69100 -13.65800 1.33400  1.000 76.05703  ?  249 ASP   A CG   1 
ATOM   580  O  OD1  . ASP   A 1 97  ? 20.83000 -13.22000 0.54200  1.000 79.47471  ?  249 ASP   A OD1  1 
ATOM   581  O  OD2  . ASP   A 1 97  ? 22.92100 -13.56400 1.12600  1.000 80.31262  ?  249 ASP   A OD2  1 
ATOM   582  N  N    . LEU   A 1 98  ? 18.89000 -14.85200 5.01900  1.000 49.92281  ?  250 LEU   A N    1 
ATOM   583  C  CA   . LEU   A 1 98  ? 18.47500 -15.74000 6.09200  1.000 49.72598  ?  250 LEU   A CA   1 
ATOM   584  C  C    . LEU   A 1 98  ? 17.02300 -16.16700 5.91300  1.000 49.18207  ?  250 LEU   A C    1 
ATOM   585  O  O    . LEU   A 1 98  ? 16.24900 -15.54100 5.18500  1.000 52.16919  ?  250 LEU   A O    1 
ATOM   586  C  CB   . LEU   A 1 98  ? 18.63600 -15.05300 7.44800  1.000 45.47826  ?  250 LEU   A CB   1 
ATOM   587  C  CG   . LEU   A 1 98  ? 20.05100 -14.63600 7.84300  1.000 44.03857  ?  250 LEU   A CG   1 
ATOM   588  C  CD1  . LEU   A 1 98  ? 20.00300 -13.50900 8.86100  1.000 45.04903  ?  250 LEU   A CD1  1 
ATOM   589  C  CD2  . LEU   A 1 98  ? 20.81000 -15.82600 8.39300  1.000 46.10700  ?  250 LEU   A CD2  1 
ATOM   590  N  N    . THR   A 1 99  ? 16.65400 -17.24300 6.60400  1.000 52.07498  ?  251 THR   A N    1 
ATOM   591  C  CA   . THR   A 1 99  ? 15.26500 -17.66800 6.61900  1.000 51.59641  ?  251 THR   A CA   1 
ATOM   592  C  C    . THR   A 1 99  ? 14.41700 -16.66800 7.40000  1.000 47.57253  ?  251 THR   A C    1 
ATOM   593  O  O    . THR   A 1 99  ? 14.91900 -15.87400 8.20400  1.000 42.41249  ?  251 THR   A O    1 
ATOM   594  C  CB   . THR   A 1 99  ? 15.12500 -19.06400 7.23300  1.000 59.46698  ?  251 THR   A CB   1 
ATOM   595  O  OG1  . THR   A 1 99  ? 13.73700 -19.41300 7.33600  1.000 72.20940  ?  251 THR   A OG1  1 
ATOM   596  C  CG2  . THR   A 1 99  ? 15.75600 -19.10700 8.61500  1.000 55.35646  ?  251 THR   A CG2  1 
ATOM   597  N  N    A SER   A 1 100 ? 13.10700 -16.71500 7.14500  0.530 45.02108  ?  252 SER   A N    1 
ATOM   598  N  N    B SER   A 1 100 ? 13.10500 -16.71400 7.15200  0.470 45.17393  ?  252 SER   A N    1 
ATOM   599  C  CA   A SER   A 1 100 ? 12.18200 -15.82900 7.84300  0.530 44.26132  ?  252 SER   A CA   1 
ATOM   600  C  CA   B SER   A 1 100 ? 12.19200 -15.81500 7.85100  0.470 44.32638  ?  252 SER   A CA   1 
ATOM   601  C  C    A SER   A 1 100 ? 12.21500 -16.07400 9.34600  0.530 44.39612  ?  252 SER   A C    1 
ATOM   602  C  C    B SER   A 1 100 ? 12.20600 -16.07200 9.35200  0.470 44.39945  ?  252 SER   A C    1 
ATOM   603  O  O    A SER   A 1 100 ? 12.12000 -15.12900 10.13900 0.530 42.64860  ?  252 SER   A O    1 
ATOM   604  O  O    B SER   A 1 100 ? 12.08800 -15.13500 10.15000 0.470 42.85413  ?  252 SER   A O    1 
ATOM   605  C  CB   A SER   A 1 100 ? 10.76800 -16.02100 7.29700  0.530 48.89318  ?  252 SER   A CB   1 
ATOM   606  C  CB   B SER   A 1 100 ? 10.77500 -15.96600 7.29500  0.470 48.75951  ?  252 SER   A CB   1 
ATOM   607  O  OG   A SER   A 1 100 ? 10.59700 -15.34500 6.06400  0.530 50.14595  ?  252 SER   A OG   1 
ATOM   608  O  OG   B SER   A 1 100 ? 9.93100  -16.62500 8.22400  0.470 50.96152  ?  252 SER   A OG   1 
ATOM   609  N  N    . ASP   A 1 101 ? 12.35300 -17.33800 9.75400  1.000 46.61901  ?  253 ASP   A N    1 
ATOM   610  C  CA   . ASP   A 1 101 ? 12.43000 -17.65800 11.17600 1.000 48.69347  ?  253 ASP   A CA   1 
ATOM   611  C  C    . ASP   A 1 101 ? 13.64100 -16.99900 11.82500 1.000 41.87167  ?  253 ASP   A C    1 
ATOM   612  O  O    . ASP   A 1 101 ? 13.53600 -16.43600 12.92100 1.000 41.74393  ?  253 ASP   A O    1 
ATOM   613  C  CB   . ASP   A 1 101 ? 12.48400 -19.17400 11.37100 1.000 46.77067  ?  253 ASP   A CB   1 
ATOM   614  C  CG   . ASP   A 1 101 ? 11.16100 -19.85300 11.06900 1.000 57.95195  ?  253 ASP   A CG   1 
ATOM   615  O  OD1  . ASP   A 1 101 ? 11.13300 -21.10100 11.02400 1.000 62.23497  ?  253 ASP   A OD1  1 
ATOM   616  O  OD2  . ASP   A 1 101 ? 10.14900 -19.14400 10.88000 1.000 56.45345  ?  253 ASP   A OD2  1 
ATOM   617  N  N    . ASP   A 1 102 ? 14.79700 -17.04800 11.15800 1.000 43.43914  ?  254 ASP   A N    1 
ATOM   618  C  CA   . ASP   A 1 102 ? 16.00400 -16.46100 11.73200 1.000 43.47871  ?  254 ASP   A CA   1 
ATOM   619  C  C    . ASP   A 1 102 ? 15.92800 -14.93900 11.75700 1.000 42.17982  ?  254 ASP   A C    1 
ATOM   620  O  O    . ASP   A 1 102 ? 16.41200 -14.30800 12.70200 1.000 39.30246  ?  254 ASP   A O    1 
ATOM   621  C  CB   . ASP   A 1 102 ? 17.23900 -16.92300 10.96000 1.000 46.14690  ?  254 ASP   A CB   1 
ATOM   622  C  CG   . ASP   A 1 102 ? 17.72300 -18.29100 11.40100 1.000 48.12365  ?  254 ASP   A CG   1 
ATOM   623  O  OD1  . ASP   A 1 102 ? 18.53200 -18.90200 10.67100 1.000 51.11140  ?  254 ASP   A OD1  1 
ATOM   624  O  OD2  . ASP   A 1 102 ? 17.29300 -18.75600 12.47800 1.000 49.61315  ?  254 ASP   A OD2  1 
ATOM   625  N  N    . GLN   A 1 103 ? 15.33300 -14.32900 10.72800 1.000 38.70089  ?  255 GLN   A N    1 
ATOM   626  C  CA   . GLN   A 1 103 ? 15.14300 -12.88100 10.74900 1.000 40.61422  ?  255 GLN   A CA   1 
ATOM   627  C  C    . GLN   A 1 103 ? 14.28600 -12.45900 11.93300 1.000 40.22154  ?  255 GLN   A C    1 
ATOM   628  O  O    . GLN   A 1 103 ? 14.53500 -11.41700 12.55300 1.000 32.96534  ?  255 GLN   A O    1 
ATOM   629  C  CB   . GLN   A 1 103 ? 14.50900 -12.40900 9.44100  1.000 41.25197  ?  255 GLN   A CB   1 
ATOM   630  C  CG   . GLN   A 1 103 ? 15.38200 -12.64200 8.22600  1.000 47.25481  ?  255 GLN   A CG   1 
ATOM   631  C  CD   . GLN   A 1 103 ? 14.71500 -12.23000 6.93100  1.000 53.93379  ?  255 GLN   A CD   1 
ATOM   632  O  OE1  . GLN   A 1 103 ? 13.83100 -11.37300 6.91500  1.000 54.40752  ?  255 GLN   A OE1  1 
ATOM   633  N  NE2  . GLN   A 1 103 ? 15.13400 -12.84500 5.83400  1.000 55.55047  ?  255 GLN   A NE2  1 
ATOM   634  N  N    . ILE   A 1 104 ? 13.27500 -13.26400 12.26600 1.000 37.72626  ?  256 ILE   A N    1 
ATOM   635  C  CA   . ILE   A 1 104 ? 12.37600 -12.91700 13.36000 1.000 34.94531  ?  256 ILE   A CA   1 
ATOM   636  C  C    . ILE   A 1 104 ? 13.07900 -13.06000 14.70300 1.000 35.53165  ?  256 ILE   A C    1 
ATOM   637  O  O    . ILE   A 1 104 ? 12.95200 -12.19600 15.57900 1.000 35.79780  ?  256 ILE   A O    1 
ATOM   638  C  CB   . ILE   A 1 104 ? 11.09900 -13.77400 13.29300 1.000 38.06698  ?  256 ILE   A CB   1 
ATOM   639  C  CG1  . ILE   A 1 104 ? 10.23000 -13.33700 12.11500 1.000 40.41165  ?  256 ILE   A CG1  1 
ATOM   640  C  CG2  . ILE   A 1 104 ? 10.31600 -13.67400 14.59100 1.000 33.81529  ?  256 ILE   A CG2  1 
ATOM   641  C  CD1  . ILE   A 1 104 ? 9.09400  -14.29500 11.81500 1.000 41.78386  ?  256 ILE   A CD1  1 
ATOM   642  N  N    A VAL   A 1 105 ? 13.84400 -14.13900 14.89300 0.220 38.61857  ?  257 VAL   A N    1 
ATOM   643  N  N    B VAL   A 1 105 ? 13.80900 -14.16300 14.89000 0.780 37.48971  ?  257 VAL   A N    1 
ATOM   644  C  CA   A VAL   A 1 105 ? 14.51600 -14.32100 16.17800 0.220 40.11132  ?  257 VAL   A CA   1 
ATOM   645  C  CA   B VAL   A 1 105 ? 14.56100 -14.36800 16.12500 0.780 40.99201  ?  257 VAL   A CA   1 
ATOM   646  C  C    A VAL   A 1 105 ? 15.59500 -13.26300 16.38100 0.220 37.40932  ?  257 VAL   A C    1 
ATOM   647  C  C    B VAL   A 1 105 ? 15.52500 -13.21200 16.35400 0.780 36.12946  ?  257 VAL   A C    1 
ATOM   648  O  O    A VAL   A 1 105 ? 15.83300 -12.82400 17.51300 0.220 38.11660  ?  257 VAL   A O    1 
ATOM   649  O  O    B VAL   A 1 105 ? 15.60700 -12.65300 17.45400 0.780 35.66456  ?  257 VAL   A O    1 
ATOM   650  C  CB   A VAL   A 1 105 ? 15.08700 -15.74800 16.31200 0.220 44.76045  ?  257 VAL   A CB   1 
ATOM   651  C  CB   B VAL   A 1 105 ? 15.30000 -15.71800 16.08200 0.780 44.61154  ?  257 VAL   A CB   1 
ATOM   652  C  CG1  A VAL   A 1 105 ? 13.98900 -16.78300 16.11800 0.220 47.42384  ?  257 VAL   A CG1  1 
ATOM   653  C  CG1  B VAL   A 1 105 ? 16.38800 -15.76700 17.14500 0.780 46.77577  ?  257 VAL   A CG1  1 
ATOM   654  C  CG2  A VAL   A 1 105 ? 16.23400 -15.98300 15.34200 0.220 45.49943  ?  257 VAL   A CG2  1 
ATOM   655  C  CG2  B VAL   A 1 105 ? 14.31800 -16.86700 16.25500 0.780 49.97709  ?  257 VAL   A CG2  1 
ATOM   656  N  N    . LEU   A 1 106 ? 16.25000 -12.82000 15.30400 1.000 38.32232  ?  258 LEU   A N    1 
ATOM   657  C  CA   . LEU   A 1 106 ? 17.26900 -11.78200 15.44000 1.000 35.71267  ?  258 LEU   A CA   1 
ATOM   658  C  C    . LEU   A 1 106 ? 16.65100 -10.43800 15.80200 1.000 31.56760  ?  258 LEU   A C    1 
ATOM   659  O  O    . LEU   A 1 106 ? 17.20000 -9.69900  16.62600 1.000 30.06197  ?  258 LEU   A O    1 
ATOM   660  C  CB   . LEU   A 1 106 ? 18.07800 -11.66500 14.14900 1.000 34.29389  ?  258 LEU   A CB   1 
ATOM   661  C  CG   . LEU   A 1 106 ? 18.96400 -12.86000 13.79200 1.000 37.01676  ?  258 LEU   A CG   1 
ATOM   662  C  CD1  . LEU   A 1 106 ? 19.71600 -12.60600 12.49400 1.000 37.15832  ?  258 LEU   A CD1  1 
ATOM   663  C  CD2  . LEU   A 1 106 ? 19.92600 -13.17500 14.92600 1.000 37.36962  ?  258 LEU   A CD2  1 
ATOM   664  N  N    . LEU   A 1 107 ? 15.50700 -10.10500 15.20700 1.000 35.37834  ?  259 LEU   A N    1 
ATOM   665  C  CA   . LEU   A 1 107 ? 14.90100 -8.81100  15.49600 1.000 33.61972  ?  259 LEU   A CA   1 
ATOM   666  C  C    . LEU   A 1 107 ? 14.18100 -8.81100  16.83900 1.000 30.20285  ?  259 LEU   A C    1 
ATOM   667  O  O    . LEU   A 1 107 ? 14.19600 -7.79900  17.54700 1.000 29.79633  ?  259 LEU   A O    1 
ATOM   668  C  CB   . LEU   A 1 107 ? 13.95400 -8.41400  14.36700 1.000 42.83091  ?  259 LEU   A CB   1 
ATOM   669  C  CG   . LEU   A 1 107 ? 14.71700 -7.71200  13.24400 1.000 49.55217  ?  259 LEU   A CG   1 
ATOM   670  C  CD1  . LEU   A 1 107 ? 14.07900 -8.00600  11.90700 1.000 55.40838  ?  259 LEU   A CD1  1 
ATOM   671  C  CD2  . LEU   A 1 107 ? 14.78800 -6.21600  13.50100 1.000 45.67219  ?  259 LEU   A CD2  1 
ATOM   672  N  N    . LYS   A 1 108 ? 13.55800 -9.93400  17.21100 1.000 29.43729  ?  260 LYS   A N    1 
ATOM   673  C  CA   . LYS   A 1 108 ? 12.91200 -10.01900 18.52000 1.000 31.05421  ?  260 LYS   A CA   1 
ATOM   674  C  C    . LYS   A 1 108 ? 13.91800 -9.83100  19.65000 1.000 33.00985  ?  260 LYS   A C    1 
ATOM   675  O  O    . LYS   A 1 108 ? 13.63100 -9.15700  20.64500 1.000 33.93597  ?  260 LYS   A O    1 
ATOM   676  C  CB   . LYS   A 1 108 ? 12.19500 -11.36200 18.67100 1.000 35.38729  ?  260 LYS   A CB   1 
ATOM   677  C  CG   . LYS   A 1 108 ? 10.80500 -11.39600 18.07300 1.000 42.59630  ?  260 LYS   A CG   1 
ATOM   678  C  CD   . LYS   A 1 108 ? 10.13400 -12.72600 18.36400 1.000 47.66863  ?  260 LYS   A CD   1 
ATOM   679  C  CE   . LYS   A 1 108 ? 9.71500  -12.82200 19.82400 1.000 55.01017  ?  260 LYS   A CE   1 
ATOM   680  N  NZ   . LYS   A 1 108 ? 9.28800  -14.20200 20.18600 1.000 58.59625  ?  260 LYS   A NZ   1 
ATOM   681  N  N    . SER   A 1 109 ? 15.10600 -10.41300 19.50600 1.000 33.45265  ?  261 SER   A N    1 
ATOM   682  C  CA   . SER   A 1 109 ? 16.11900 -10.36400 20.55300 1.000 36.35325  ?  261 SER   A CA   1 
ATOM   683  C  C    . SER   A 1 109 ? 16.94500 -9.08700  20.51700 1.000 32.80976  ?  261 SER   A C    1 
ATOM   684  O  O    . SER   A 1 109 ? 17.48100 -8.67800  21.54900 1.000 35.69473  ?  261 SER   A O    1 
ATOM   685  C  CB   . SER   A 1 109 ? 17.02800 -11.59300 20.44100 1.000 46.38710  ?  261 SER   A CB   1 
ATOM   686  O  OG   . SER   A 1 109 ? 17.75500 -11.52200 19.22400 1.000 53.06753  ?  261 SER   A OG   1 
ATOM   687  N  N    . SER   A 1 110 ? 17.05700 -8.44000  19.36800 1.000 29.25640  ?  262 SER   A N    1 
ATOM   688  C  CA   . SER   A 1 110 ? 17.90900 -7.26400  19.25900 1.000 30.45257  ?  262 SER   A CA   1 
ATOM   689  C  C    . SER   A 1 110 ? 17.15500 -5.93900  19.34300 1.000 30.48435  ?  262 SER   A C    1 
ATOM   690  O  O    . SER   A 1 110 ? 17.79300 -4.89900  19.55600 1.000 28.75374  ?  262 SER   A O    1 
ATOM   691  C  CB   . SER   A 1 110 ? 18.70700 -7.30000  17.94100 1.000 32.49399  ?  262 SER   A CB   1 
ATOM   692  O  OG   . SER   A 1 110 ? 17.89400 -7.11300  16.79700 1.000 32.14306  ?  262 SER   A OG   1 
ATOM   693  N  N    . ALA   A 1 111 ? 15.82400 -5.94700  19.18800 1.000 28.82431  ?  263 ALA   A N    1 
ATOM   694  C  CA   . ALA   A 1 111 ? 15.07500 -4.70300  19.01800 1.000 29.28657  ?  263 ALA   A CA   1 
ATOM   695  C  C    . ALA   A 1 111 ? 15.34900 -3.71500  20.14400 1.000 27.20685  ?  263 ALA   A C    1 
ATOM   696  O  O    . ALA   A 1 111 ? 15.61900 -2.53600  19.89300 1.000 28.59017  ?  263 ALA   A O    1 
ATOM   697  C  CB   . ALA   A 1 111 ? 13.57500 -4.99200  18.92000 1.000 28.18954  ?  263 ALA   A CB   1 
ATOM   698  N  N    . ILE   A 1 112 ? 15.27800 -4.17200  21.39800 1.000 24.93125  ?  264 ILE   A N    1 
ATOM   699  C  CA   . ILE   A 1 112 ? 15.48700 -3.25900  22.52000 1.000 28.36390  ?  264 ILE   A CA   1 
ATOM   700  C  C    . ILE   A 1 112 ? 16.92000 -2.73800  22.53800 1.000 30.52584  ?  264 ILE   A C    1 
ATOM   701  O  O    . ILE   A 1 112 ? 17.16900 -1.58700  22.92400 1.000 27.73720  ?  264 ILE   A O    1 
ATOM   702  C  CB   . ILE   A 1 112 ? 15.10700 -3.94700  23.85000 1.000 35.60805  ?  264 ILE   A CB   1 
ATOM   703  C  CG1  . ILE   A 1 112 ? 15.12800 -2.94400  25.00700 1.000 38.34541  ?  264 ILE   A CG1  1 
ATOM   704  C  CG2  . ILE   A 1 112 ? 16.02700 -5.13000  24.13800 1.000 38.17976  ?  264 ILE   A CG2  1 
ATOM   705  C  CD1  . ILE   A 1 112 ? 14.25700 -1.73000  24.77800 1.000 34.41458  ?  264 ILE   A CD1  1 
ATOM   706  N  N    . GLU   A 1 113 ? 17.88000 -3.55600  22.10100 1.000 28.22007  ?  265 GLU   A N    1 
ATOM   707  C  CA   . GLU   A 1 113 ? 19.27100 -3.11500  22.08000 1.000 28.71831  ?  265 GLU   A CA   1 
ATOM   708  C  C    . GLU   A 1 113 ? 19.50500 -2.07600  20.98900 1.000 27.06205  ?  265 GLU   A C    1 
ATOM   709  O  O    . GLU   A 1 113 ? 20.20300 -1.07900  21.21300 1.000 28.73410  ?  265 GLU   A O    1 
ATOM   710  C  CB   . GLU   A 1 113 ? 20.19800 -4.31500  21.88600 1.000 30.12930  ?  265 GLU   A CB   1 
ATOM   711  C  CG   . GLU   A 1 113 ? 20.14700 -5.34100  23.00800 1.000 26.21033  ?  265 GLU   A CG   1 
ATOM   712  C  CD   . GLU   A 1 113 ? 20.99600 -6.56300  22.71500 1.000 35.45441  ?  265 GLU   A CD   1 
ATOM   713  O  OE1  . GLU   A 1 113 ? 21.94900 -6.44800  21.91300 1.000 34.74717  ?  265 GLU   A OE1  1 
ATOM   714  O  OE2  . GLU   A 1 113 ? 20.71200 -7.63600  23.28600 1.000 35.72654  ?  265 GLU   A OE2  1 
ATOM   715  N  N    . VAL   A 1 114 ? 18.93300 -2.28800  19.80200 1.000 27.70525  ?  266 VAL   A N    1 
ATOM   716  C  CA   . VAL   A 1 114 ? 19.10500 -1.31800  18.72500 1.000 27.12508  ?  266 VAL   A CA   1 
ATOM   717  C  C    . VAL   A 1 114 ? 18.41500 -0.00300  19.06700 1.000 28.34914  ?  266 VAL   A C    1 
ATOM   718  O  O    . VAL   A 1 114 ? 18.89100 1.07400   18.68600 1.000 27.98725  ?  266 VAL   A O    1 
ATOM   719  C  CB   . VAL   A 1 114 ? 18.59000 -1.90200  17.39800 1.000 32.11023  ?  266 VAL   A CB   1 
ATOM   720  C  CG1  . VAL   A 1 114 ? 18.85400 -0.94000  16.24800 1.000 30.02153  ?  266 VAL   A CG1  1 
ATOM   721  C  CG2  . VAL   A 1 114 ? 19.24200 -3.24700  17.13400 1.000 30.60527  ?  266 VAL   A CG2  1 
ATOM   722  N  N    . ILE   A 1 115 ? 17.29100 -0.06000  19.78300 1.000 28.35828  ?  267 ILE   A N    1 
ATOM   723  C  CA   . ILE   A 1 115 ? 16.64000 1.16900   20.22500 1.000 25.18317  ?  267 ILE   A CA   1 
ATOM   724  C  C    . ILE   A 1 115 ? 17.54600 1.93700   21.18100 1.000 28.12456  ?  267 ILE   A C    1 
ATOM   725  O  O    . ILE   A 1 115 ? 17.67800 3.16400   21.08700 1.000 30.51858  ?  267 ILE   A O    1 
ATOM   726  C  CB   . ILE   A 1 115 ? 15.27500 0.84700   20.86000 1.000 29.27522  ?  267 ILE   A CB   1 
ATOM   727  C  CG1  . ILE   A 1 115 ? 14.28700 0.40000   19.78400 1.000 28.90347  ?  267 ILE   A CG1  1 
ATOM   728  C  CG2  . ILE   A 1 115 ? 14.73300 2.04600   21.60600 1.000 31.06751  ?  267 ILE   A CG2  1 
ATOM   729  C  CD1  . ILE   A 1 115 ? 13.07700 -0.33400  20.34000 1.000 30.47395  ?  267 ILE   A CD1  1 
ATOM   730  N  N    . MET   A 1 116 ? 18.19400 1.22900   22.10800 1.000 26.06354  ?  268 MET   A N    1 
ATOM   731  C  CA   . MET   A 1 116 ? 19.13700 1.88800   23.00600 1.000 29.67741  ?  268 MET   A CA   1 
ATOM   732  C  C    . MET   A 1 116 ? 20.28000 2.53500   22.22900 1.000 27.93479  ?  268 MET   A C    1 
ATOM   733  O  O    . MET   A 1 116 ? 20.69000 3.65900   22.53900 1.000 29.90692  ?  268 MET   A O    1 
ATOM   734  C  CB   . MET   A 1 116 ? 19.67000 0.88800   24.03400 1.000 30.20266  ?  268 MET   A CB   1 
ATOM   735  C  CG   . MET   A 1 116 ? 18.65700 0.54300   25.12700 1.000 33.19749  ?  268 MET   A CG   1 
ATOM   736  S  SD   . MET   A 1 116 ? 19.06700 -0.92300  26.09800 1.000 36.80566  ?  268 MET   A SD   1 
ATOM   737  C  CE   . MET   A 1 116 ? 17.61600 -1.05000  27.14400 1.000 37.51856  ?  268 MET   A CE   1 
ATOM   738  N  N    . LEU   A 1 117 ? 20.79100 1.85100   21.20100 1.000 27.86258  ?  269 LEU   A N    1 
ATOM   739  C  CA   . LEU   A 1 117 ? 21.88800 2.41000   20.41300 1.000 27.16556  ?  269 LEU   A CA   1 
ATOM   740  C  C    . LEU   A 1 117 ? 21.43200 3.62200   19.60900 1.000 30.65578  ?  269 LEU   A C    1 
ATOM   741  O  O    . LEU   A 1 117 ? 22.07700 4.67500   19.63800 1.000 28.43649  ?  269 LEU   A O    1 
ATOM   742  C  CB   . LEU   A 1 117 ? 22.46900 1.34700   19.47800 1.000 26.32087  ?  269 LEU   A CB   1 
ATOM   743  C  CG   . LEU   A 1 117 ? 23.27500 0.20300   20.08500 1.000 28.37702  ?  269 LEU   A CG   1 
ATOM   744  C  CD1  . LEU   A 1 117 ? 23.41400 -0.92500  19.07400 1.000 30.03104  ?  269 LEU   A CD1  1 
ATOM   745  C  CD2  . LEU   A 1 117 ? 24.64700 0.69700   20.53400 1.000 26.37285  ?  269 LEU   A CD2  1 
ATOM   746  N  N    . ARG   A 1 118 ? 20.31900 3.49300   18.87900 1.000 29.43025  ?  270 ARG   A N    1 
ATOM   747  C  CA   . ARG   A 1 118 ? 19.90400 4.57900   17.99600 1.000 27.27603  ?  270 ARG   A CA   1 
ATOM   748  C  C    . ARG   A 1 118 ? 19.41600 5.79100   18.77800 1.000 28.80265  ?  270 ARG   A C    1 
ATOM   749  O  O    . ARG   A 1 118 ? 19.51600 6.92100   18.28500 1.000 32.41195  ?  270 ARG   A O    1 
ATOM   750  C  CB   . ARG   A 1 118 ? 18.82400 4.09700   17.02300 1.000 27.69348  ?  270 ARG   A CB   1 
ATOM   751  C  CG   . ARG   A 1 118 ? 17.45600 3.88800   17.64200 1.000 27.75229  ?  270 ARG   A CG   1 
ATOM   752  C  CD   . ARG   A 1 118 ? 16.63400 2.87400   16.84600 1.000 32.18648  ?  270 ARG   A CD   1 
ATOM   753  N  NE   . ARG   A 1 118 ? 16.63100 3.17200   15.41500 1.000 38.53703  ?  270 ARG   A NE   1 
ATOM   754  C  CZ   . ARG   A 1 118 ? 15.86300 4.09400   14.84600 1.000 42.51578  ?  270 ARG   A CZ   1 
ATOM   755  N  NH1  . ARG   A 1 118 ? 15.02400 4.80900   15.58500 1.000 47.26699  ?  270 ARG   A NH1  1 
ATOM   756  N  NH2  . ARG   A 1 118 ? 15.93100 4.30100   13.53600 1.000 35.68782  ?  270 ARG   A NH2  1 
ATOM   757  N  N    . SER   A 1 119 ? 18.90200 5.58800   19.99400 1.000 28.01596  ?  271 SER   A N    1 
ATOM   758  C  CA   . SER   A 1 119 ? 18.47300 6.71500   20.81400 1.000 32.40241  ?  271 SER   A CA   1 
ATOM   759  C  C    . SER   A 1 119 ? 19.64100 7.56500   21.29600 1.000 30.89607  ?  271 SER   A C    1 
ATOM   760  O  O    . SER   A 1 119 ? 19.41500 8.67800   21.78400 1.000 32.69908  ?  271 SER   A O    1 
ATOM   761  C  CB   . SER   A 1 119 ? 17.66000 6.22100   22.01400 1.000 33.54552  ?  271 SER   A CB   1 
ATOM   762  O  OG   . SER   A 1 119 ? 18.50400 5.70400   23.02600 1.000 36.98318  ?  271 SER   A OG   1 
ATOM   763  N  N    . ASN   A 1 120 ? 20.87500 7.07200   21.16900 1.000 28.81267  ?  272 ASN   A N    1 
ATOM   764  C  CA   . ASN   A 1 120 ? 22.04200 7.86300   21.54300 1.000 29.42794  ?  272 ASN   A CA   1 
ATOM   765  C  C    . ASN   A 1 120 ? 22.18600 9.11200   20.68600 1.000 32.46245  ?  272 ASN   A C    1 
ATOM   766  O  O    . ASN   A 1 120 ? 22.80400 10.08600  21.12800 1.000 33.90719  ?  272 ASN   A O    1 
ATOM   767  C  CB   . ASN   A 1 120 ? 23.30400 7.00700   21.43500 1.000 30.71271  ?  272 ASN   A CB   1 
ATOM   768  C  CG   . ASN   A 1 120 ? 24.50000 7.63500   22.12700 1.000 34.27964  ?  272 ASN   A CG   1 
ATOM   769  O  OD1  . ASN   A 1 120 ? 25.48800 7.98700   21.48500 1.000 37.73317  ?  272 ASN   A OD1  1 
ATOM   770  N  ND2  . ASN   A 1 120 ? 24.41500 7.77600   23.44700 1.000 31.62013  ?  272 ASN   A ND2  1 
ATOM   771  N  N    . GLN   A 1 121 ? 21.62300 9.10600   19.47500 1.000 32.34769  ?  273 GLN   A N    1 
ATOM   772  C  CA   . GLN   A 1 121 ? 21.73700 10.26500  18.59600 1.000 36.03900  ?  273 GLN   A CA   1 
ATOM   773  C  C    . GLN   A 1 121 ? 21.06700 11.49400  19.19400 1.000 39.71549  ?  273 GLN   A C    1 
ATOM   774  O  O    . GLN   A 1 121 ? 21.51900 12.62100  18.96400 1.000 41.06795  ?  273 GLN   A O    1 
ATOM   775  C  CB   . GLN   A 1 121 ? 21.13200 9.94000   17.22900 1.000 39.51896  ?  273 GLN   A CB   1 
ATOM   776  C  CG   . GLN   A 1 121 ? 21.26400 11.04600  16.19700 1.000 39.04411  ?  273 GLN   A CG   1 
ATOM   777  C  CD   . GLN   A 1 121 ? 21.07400 10.54200  14.78000 1.000 37.64980  ?  273 GLN   A CD   1 
ATOM   778  O  OE1  . GLN   A 1 121 ? 21.21100 9.34800   14.51000 1.000 33.63209  ?  273 GLN   A OE1  1 
ATOM   779  N  NE2  . GLN   A 1 121 ? 20.75800 11.45200  13.86600 1.000 36.57752  ?  273 GLN   A NE2  1 
ATOM   780  N  N    . SER   A 1 122 ? 19.99400 11.30300  19.96200 1.000 38.36806  ?  274 SER   A N    1 
ATOM   781  C  CA   . SER   A 1 122 ? 19.28300 12.40700  20.59400 1.000 39.83268  ?  274 SER   A CA   1 
ATOM   782  C  C    . SER   A 1 122 ? 19.69000 12.62900  22.04500 1.000 40.21038  ?  274 SER   A C    1 
ATOM   783  O  O    . SER   A 1 122 ? 19.26500 13.62200  22.64500 1.000 43.36534  ?  274 SER   A O    1 
ATOM   784  C  CB   . SER   A 1 122 ? 17.76800 12.17200  20.52600 1.000 40.47146  ?  274 SER   A CB   1 
ATOM   785  O  OG   . SER   A 1 122 ? 17.38300 11.10200  21.37000 1.000 40.54275  ?  274 SER   A OG   1 
ATOM   786  N  N    . PHE   A 1 123 ? 20.49000 11.73500  22.61900 1.000 36.83137  ?  275 PHE   A N    1 
ATOM   787  C  CA   . PHE   A 1 123 ? 20.91800 11.88700  24.00200 1.000 38.34457  ?  275 PHE   A CA   1 
ATOM   788  C  C    . PHE   A 1 123 ? 21.87400 13.06600  24.13400 1.000 41.00222  ?  275 PHE   A C    1 
ATOM   789  O  O    . PHE   A 1 123 ? 22.75200 13.27100  23.29400 1.000 45.55693  ?  275 PHE   A O    1 
ATOM   790  C  CB   . PHE   A 1 123 ? 21.59200 10.60300  24.48600 1.000 38.13901  ?  275 PHE   A CB   1 
ATOM   791  C  CG   . PHE   A 1 123 ? 21.92200 10.60300  25.95200 1.000 38.29799  ?  275 PHE   A CG   1 
ATOM   792  C  CD1  . PHE   A 1 123 ? 20.92800 10.41600  26.89900 1.000 39.23736  ?  275 PHE   A CD1  1 
ATOM   793  C  CD2  . PHE   A 1 123 ? 23.22900 10.78300  26.38300 1.000 34.00022  ?  275 PHE   A CD2  1 
ATOM   794  C  CE1  . PHE   A 1 123 ? 21.22900 10.41000  28.24900 1.000 40.92860  ?  275 PHE   A CE1  1 
ATOM   795  C  CE2  . PHE   A 1 123 ? 23.53700 10.77900  27.73100 1.000 37.73526  ?  275 PHE   A CE2  1 
ATOM   796  C  CZ   . PHE   A 1 123 ? 22.53600 10.59300  28.66600 1.000 43.12861  ?  275 PHE   A CZ   1 
ATOM   797  N  N    . THR   A 1 124 ? 21.69200 13.85200  25.19200 1.000 43.78199  ?  276 THR   A N    1 
ATOM   798  C  CA   . THR   A 1 124 ? 22.56400 14.98000  25.48200 1.000 49.65201  ?  276 THR   A CA   1 
ATOM   799  C  C    . THR   A 1 124 ? 23.22000 14.78400  26.84000 1.000 49.65786  ?  276 THR   A C    1 
ATOM   800  O  O    . THR   A 1 124 ? 22.57200 14.36500  27.80500 1.000 47.43531  ?  276 THR   A O    1 
ATOM   801  C  CB   . THR   A 1 124 ? 21.80100 16.31800  25.45600 1.000 59.25601  ?  276 THR   A CB   1 
ATOM   802  O  OG1  . THR   A 1 124 ? 22.67400 17.37700  25.87000 1.000 65.63503  ?  276 THR   A OG1  1 
ATOM   803  C  CG2  . THR   A 1 124 ? 20.58700 16.27800  26.37000 1.000 58.15252  ?  276 THR   A CG2  1 
ATOM   804  N  N    . MET   A 1 125 ? 24.51800 15.06700  26.90300 1.000 50.23304  ?  277 MET   A N    1 
ATOM   805  C  CA   . MET   A 1 125 ? 25.23500 15.04000  28.16700 1.000 54.01435  ?  277 MET   A CA   1 
ATOM   806  C  C    . MET   A 1 125 ? 25.14400 16.36400  28.91300 1.000 58.43534  ?  277 MET   A C    1 
ATOM   807  O  O    . MET   A 1 125 ? 25.61700 16.45000  30.05000 1.000 65.38666  ?  277 MET   A O    1 
ATOM   808  C  CB   . MET   A 1 125 ? 26.70000 14.66000  27.93300 1.000 57.07944  ?  277 MET   A CB   1 
ATOM   809  C  CG   . MET   A 1 125 ? 26.87000 13.22600  27.45000 1.000 54.64372  ?  277 MET   A CG   1 
ATOM   810  S  SD   . MET   A 1 125 ? 28.52700 12.55900  27.67700 1.000 67.99293  ?  277 MET   A SD   1 
ATOM   811  C  CE   . MET   A 1 125 ? 29.43100 13.44500  26.41000 1.000 68.32067  ?  277 MET   A CE   1 
ATOM   812  N  N    . ASP   A 1 126 ? 24.54500 17.38700  28.29800 1.000 61.00321  ?  278 ASP   A N    1 
ATOM   813  C  CA   . ASP   A 1 126 ? 24.27000 18.63000  29.01200 1.000 69.33303  ?  278 ASP   A CA   1 
ATOM   814  C  C    . ASP   A 1 126 ? 23.40800 18.37400  30.24200 1.000 66.82675  ?  278 ASP   A C    1 
ATOM   815  O  O    . ASP   A 1 126 ? 23.65600 18.94200  31.31300 1.000 67.75606  ?  278 ASP   A O    1 
ATOM   816  C  CB   . ASP   A 1 126 ? 23.58200 19.62800  28.08000 1.000 79.97850  ?  278 ASP   A CB   1 
ATOM   817  C  CG   . ASP   A 1 126 ? 24.54500 20.28700  27.10900 1.000 88.70756  ?  278 ASP   A CG   1 
ATOM   818  O  OD1  . ASP   A 1 126 ? 25.75900 20.32500  27.40100 1.000 92.32492  ?  278 ASP   A OD1  1 
ATOM   819  O  OD2  . ASP   A 1 126 ? 24.08600 20.76400  26.05100 1.000 91.37022  ?  278 ASP   A OD2  1 
ATOM   820  N  N    . ASP   A 1 127 ? 22.38800 17.51000  30.11100 1.000 61.22143  ?  279 ASP   A N    1 
ATOM   821  C  CA   . ASP   A 1 127 ? 21.52200 17.22000  31.24900 1.000 62.44518  ?  279 ASP   A CA   1 
ATOM   822  C  C    . ASP   A 1 127 ? 21.03000 15.77300  31.27900 1.000 61.76888  ?  279 ASP   A C    1 
ATOM   823  O  O    . ASP   A 1 127 ? 20.00000 15.50400  31.90900 1.000 62.82264  ?  279 ASP   A O    1 
ATOM   824  C  CB   . ASP   A 1 127 ? 20.32100 18.18500  31.26000 1.000 70.21598  ?  279 ASP   A CB   1 
ATOM   825  C  CG   . ASP   A 1 127 ? 19.58000 18.22000  29.93400 1.000 70.39184  ?  279 ASP   A CG   1 
ATOM   826  O  OD1  . ASP   A 1 127 ? 19.03900 19.29100  29.58900 1.000 73.41100  ?  279 ASP   A OD1  1 
ATOM   827  O  OD2  . ASP   A 1 127 ? 19.52700 17.18500  29.24000 1.000 66.13519  ?  279 ASP   A OD2  1 
ATOM   828  N  N    . MET   A 1 128 ? 21.72500 14.84300  30.62000 1.000 57.23455  ?  280 MET   A N    1 
ATOM   829  C  CA   . MET   A 1 128 ? 21.39900 13.41500  30.66500 1.000 52.55627  ?  280 MET   A CA   1 
ATOM   830  C  C    . MET   A 1 128 ? 19.95800 13.15000  30.22800 1.000 49.80876  ?  280 MET   A C    1 
ATOM   831  O  O    . MET   A 1 128 ? 19.20400 12.43100  30.88700 1.000 50.56768  ?  280 MET   A O    1 
ATOM   832  C  CB   . MET   A 1 128 ? 21.66200 12.83600  32.05800 1.000 54.96557  ?  280 MET   A CB   1 
ATOM   833  C  CG   . MET   A 1 128 ? 23.05300 13.12100  32.59400 1.000 57.95454  ?  280 MET   A CG   1 
ATOM   834  S  SD   . MET   A 1 128 ? 24.32200 12.29500  31.62000 1.000 57.97208  ?  280 MET   A SD   1 
ATOM   835  C  CE   . MET   A 1 128 ? 25.57900 13.56700  31.54800 1.000 58.84999  ?  280 MET   A CE   1 
ATOM   836  N  N    . SER   A 1 129 ? 19.57900 13.73300  29.09500 1.000 49.17639  ?  281 SER   A N    1 
ATOM   837  C  CA   . SER   A 1 129 ? 18.23000 13.58900  28.57400 1.000 48.78397  ?  281 SER   A CA   1 
ATOM   838  C  C    . SER   A 1 129 ? 18.27700 13.22700  27.09600 1.000 44.92249  ?  281 SER   A C    1 
ATOM   839  O  O    . SER   A 1 129 ? 19.29000 13.41100  26.41700 1.000 42.59823  ?  281 SER   A O    1 
ATOM   840  C  CB   . SER   A 1 129 ? 17.41100 14.87200  28.77400 1.000 53.65319  ?  281 SER   A CB   1 
ATOM   841  O  OG   . SER   A 1 129 ? 17.62700 15.78200  27.71200 1.000 59.77077  ?  281 SER   A OG   1 
ATOM   842  N  N    . TRP   A 1 130 ? 17.16100 12.69600  26.60800 1.000 44.31946  ?  282 TRP   A N    1 
ATOM   843  C  CA   . TRP   A 1 130 ? 16.96100 12.44200  25.18400 1.000 42.35045  ?  282 TRP   A CA   1 
ATOM   844  C  C    . TRP   A 1 130 ? 16.18100 13.63100  24.63100 1.000 41.74145  ?  282 TRP   A C    1 
ATOM   845  O  O    . TRP   A 1 130 ? 14.97000 13.73900  24.83500 1.000 45.49676  ?  282 TRP   A O    1 
ATOM   846  C  CB   . TRP   A 1 130 ? 16.21800 11.13000  24.95600 1.000 34.84165  ?  282 TRP   A CB   1 
ATOM   847  C  CG   . TRP   A 1 130 ? 16.99800 9.88300   25.29200 1.000 35.91458  ?  282 TRP   A CG   1 
ATOM   848  C  CD1  . TRP   A 1 130 ? 17.71600 9.10800   24.42700 1.000 37.09145  ?  282 TRP   A CD1  1 
ATOM   849  C  CD2  . TRP   A 1 130 ? 17.10300 9.25200   26.57500 1.000 36.11664  ?  282 TRP   A CD2  1 
ATOM   850  N  NE1  . TRP   A 1 130 ? 18.27400 8.04300   25.09400 1.000 34.00969  ?  282 TRP   A NE1  1 
ATOM   851  C  CE2  . TRP   A 1 130 ? 17.91200 8.10700   26.41400 1.000 35.24702  ?  282 TRP   A CE2  1 
ATOM   852  C  CE3  . TRP   A 1 130 ? 16.59800 9.54600   27.84500 1.000 39.58326  ?  282 TRP   A CE3  1 
ATOM   853  C  CZ2  . TRP   A 1 130 ? 18.22600 7.26000   27.47300 1.000 35.02011  ?  282 TRP   A CZ2  1 
ATOM   854  C  CZ3  . TRP   A 1 130 ? 16.91100 8.70300   28.89600 1.000 39.46371  ?  282 TRP   A CZ3  1 
ATOM   855  C  CH2  . TRP   A 1 130 ? 17.71800 7.57400   28.70400 1.000 39.89365  ?  282 TRP   A CH2  1 
ATOM   856  N  N    . ASP   A 1 131 ? 16.87600 14.52900  23.93700 1.000 43.54559  ?  283 ASP   A N    1 
ATOM   857  C  CA   . ASP   A 1 131 ? 16.26000 15.73500  23.39100 1.000 48.93958  ?  283 ASP   A CA   1 
ATOM   858  C  C    . ASP   A 1 131 ? 15.79300 15.44500  21.97100 1.000 45.19061  ?  283 ASP   A C    1 
ATOM   859  O  O    . ASP   A 1 131 ? 16.61200 15.26500  21.06500 1.000 51.14572  ?  283 ASP   A O    1 
ATOM   860  C  CB   . ASP   A 1 131 ? 17.24000 16.90600  23.42600 1.000 52.74712  ?  283 ASP   A CB   1 
ATOM   861  C  CG   . ASP   A 1 131 ? 16.59500 18.22600  23.02900 1.000 60.99900  ?  283 ASP   A CG   1 
ATOM   862  O  OD1  . ASP   A 1 131 ? 15.40800 18.22800  22.63600 1.000 59.99211  ?  283 ASP   A OD1  1 
ATOM   863  O  OD2  . ASP   A 1 131 ? 17.27800 19.26800  23.11200 1.000 64.90572  ?  283 ASP   A OD2  1 
ATOM   864  N  N    . CYS   A 1 132 ? 14.47700 15.41600  21.77400 1.000 48.42527  ?  284 CYS   A N    1 
ATOM   865  C  CA   . CYS   A 1 132 ? 13.88000 15.10600  20.48100 1.000 45.25154  ?  284 CYS   A CA   1 
ATOM   866  C  C    . CYS   A 1 132 ? 13.13400 16.30800  19.90500 1.000 48.53365  ?  284 CYS   A C    1 
ATOM   867  O  O    . CYS   A 1 132 ? 12.08700 16.16300  19.27000 1.000 48.44201  ?  284 CYS   A O    1 
ATOM   868  C  CB   . CYS   A 1 132 ? 12.95300 13.89800  20.59800 1.000 45.48307  ?  284 CYS   A CB   1 
ATOM   869  S  SG   . CYS   A 1 132 ? 13.82200 12.31200  20.70800 1.000 40.75562  ?  284 CYS   A SG   1 
ATOM   870  N  N    . GLY   A 1 133 ? 13.65400 17.51400  20.13900 1.000 51.64200  ?  285 GLY   A N    1 
ATOM   871  C  CA   . GLY   A 1 133 ? 13.23000 18.70000  19.42500 1.000 53.12991  ?  285 GLY   A CA   1 
ATOM   872  C  C    . GLY   A 1 133 ? 12.34200 19.65700  20.19600 1.000 59.82976  ?  285 GLY   A C    1 
ATOM   873  O  O    . GLY   A 1 133 ? 12.28500 20.84200  19.83900 1.000 62.81089  ?  285 GLY   A O    1 
ATOM   874  N  N    A SER   A 1 134 ? 11.65100 19.18900  21.23300 0.430 61.66513  ?  286 SER   A N    1 
ATOM   875  N  N    B SER   A 1 134 ? 11.64900 19.19300  21.23300 0.570 61.74936  ?  286 SER   A N    1 
ATOM   876  C  CA   A SER   A 1 134 ? 10.70900 20.02900  21.95900 0.430 64.65985  ?  286 SER   A CA   1 
ATOM   877  C  CA   B SER   A 1 134 ? 10.73500 20.05700  21.96400 0.570 64.66785  ?  286 SER   A CA   1 
ATOM   878  C  C    A SER   A 1 134 ? 10.73500 19.65900  23.43600 0.430 64.40410  ?  286 SER   A C    1 
ATOM   879  C  C    B SER   A 1 134 ? 10.71000 19.64600  23.42900 0.570 64.38753  ?  286 SER   A C    1 
ATOM   880  O  O    A SER   A 1 134 ? 11.35200 18.67000  23.84200 0.430 61.82056  ?  286 SER   A O    1 
ATOM   881  O  O    B SER   A 1 134 ? 11.26800 18.61700  23.82000 0.570 61.59965  ?  286 SER   A O    1 
ATOM   882  C  CB   A SER   A 1 134 ? 9.29100  19.89500  21.39200 0.430 65.78545  ?  286 SER   A CB   1 
ATOM   883  C  CB   B SER   A 1 134 ? 9.32600  20.01700  21.36000 0.570 66.16061  ?  286 SER   A CB   1 
ATOM   884  O  OG   A SER   A 1 134 ? 9.25100  20.28100  20.03000 0.430 66.76615  ?  286 SER   A OG   1 
ATOM   885  O  OG   B SER   A 1 134 ? 8.47100  19.17800  22.11500 0.570 64.34553  ?  286 SER   A OG   1 
ATOM   886  N  N    . GLN   A 1 135 ? 10.04900 20.47500  24.24100 1.000 68.07041  ?  287 GLN   A N    1 
ATOM   887  C  CA   . GLN   A 1 135 ? 9.98200  20.21700  25.67700 1.000 71.51159  ?  287 GLN   A CA   1 
ATOM   888  C  C    . GLN   A 1 135 ? 9.12100  18.99800  25.98300 1.000 66.85461  ?  287 GLN   A C    1 
ATOM   889  O  O    . GLN   A 1 135 ? 9.46700  18.19200  26.85500 1.000 62.10847  ?  287 GLN   A O    1 
ATOM   890  C  CB   . GLN   A 1 135 ? 9.44500  21.44700  26.40800 1.000 77.76885  ?  287 GLN   A CB   1 
ATOM   891  C  CG   . GLN   A 1 135 ? 10.52600 22.37200  26.94000 1.000 83.16557  ?  287 GLN   A CG   1 
ATOM   892  C  CD   . GLN   A 1 135 ? 11.38200 21.71800  28.00800 1.000 85.42001  ?  287 GLN   A CD   1 
ATOM   893  O  OE1  . GLN   A 1 135 ? 10.93500 20.81100  28.71100 1.000 86.15940  ?  287 GLN   A OE1  1 
ATOM   894  N  NE2  . GLN   A 1 135 ? 12.62200 22.17500  28.13300 1.000 85.52064  ?  287 GLN   A NE2  1 
ATOM   895  N  N    . ASP   A 1 136 ? 7.99100  18.85200  25.28500 1.000 65.18105  ?  288 ASP   A N    1 
ATOM   896  C  CA   . ASP   A 1 136 ? 7.17200  17.65700  25.45200 1.000 65.48371  ?  288 ASP   A CA   1 
ATOM   897  C  C    . ASP   A 1 136 ? 7.95100  16.39700  25.11000 1.000 58.07537  ?  288 ASP   A C    1 
ATOM   898  O  O    . ASP   A 1 136 ? 7.68500  15.32900  25.67400 1.000 58.48403  ?  288 ASP   A O    1 
ATOM   899  C  CB   . ASP   A 1 136 ? 5.91700  17.74500  24.58200 1.000 70.27321  ?  288 ASP   A CB   1 
ATOM   900  C  CG   . ASP   A 1 136 ? 4.94000  18.79500  25.06700 1.000 81.43258  ?  288 ASP   A CG   1 
ATOM   901  O  OD1  . ASP   A 1 136 ? 5.08700  19.26100  26.21600 1.000 85.85120  ?  288 ASP   A OD1  1 
ATOM   902  O  OD2  . ASP   A 1 136 ? 4.02100  19.15000  24.29900 1.000 85.22135  ?  288 ASP   A OD2  1 
ATOM   903  N  N    . TYR   A 1 137 ? 8.91700  16.50100  24.19700 1.000 52.54119  ?  289 TYR   A N    1 
ATOM   904  C  CA   . TYR   A 1 137 ? 9.68500  15.35700  23.72500 1.000 47.18980  ?  289 TYR   A CA   1 
ATOM   905  C  C    . TYR   A 1 137 ? 11.14900 15.43600  24.15300 1.000 42.90981  ?  289 TYR   A C    1 
ATOM   906  O  O    . TYR   A 1 137 ? 12.04200 15.00300  23.42300 1.000 46.54975  ?  289 TYR   A O    1 
ATOM   907  C  CB   . TYR   A 1 137 ? 9.56200  15.23100  22.20700 1.000 45.79774  ?  289 TYR   A CB   1 
ATOM   908  C  CG   . TYR   A 1 137 ? 8.13600  15.37300  21.71300 1.000 48.57482  ?  289 TYR   A CG   1 
ATOM   909  C  CD1  . TYR   A 1 137 ? 7.84300  16.11700  20.57800 1.000 49.71177  ?  289 TYR   A CD1  1 
ATOM   910  C  CD2  . TYR   A 1 137 ? 7.08400  14.76000  22.38400 1.000 45.29981  ?  289 TYR   A CD2  1 
ATOM   911  C  CE1  . TYR   A 1 137 ? 6.54100  16.25000  20.13000 1.000 53.70588  ?  289 TYR   A CE1  1 
ATOM   912  C  CE2  . TYR   A 1 137 ? 5.78300  14.88800  21.94500 1.000 53.16904  ?  289 TYR   A CE2  1 
ATOM   913  C  CZ   . TYR   A 1 137 ? 5.51600  15.63300  20.81700 1.000 55.35696  ?  289 TYR   A CZ   1 
ATOM   914  O  OH   . TYR   A 1 137 ? 4.21800  15.76000  20.37600 1.000 57.08769  ?  289 TYR   A OH   1 
ATOM   915  N  N    . LYS   A 1 138 ? 11.40400 15.99900  25.33100 1.000 47.55564  ?  290 LYS   A N    1 
ATOM   916  C  CA   . LYS   A 1 138 ? 12.69600 15.90100  26.00200 1.000 47.85240  ?  290 LYS   A CA   1 
ATOM   917  C  C    . LYS   A 1 138 ? 12.50000 14.97300  27.19300 1.000 48.84991  ?  290 LYS   A C    1 
ATOM   918  O  O    . LYS   A 1 138 ? 11.79500 15.31900  28.14700 1.000 48.30038  ?  290 LYS   A O    1 
ATOM   919  C  CB   . LYS   A 1 138 ? 13.20900 17.27100  26.44300 1.000 56.10554  ?  290 LYS   A CB   1 
ATOM   920  C  CG   . LYS   A 1 138 ? 14.69300 17.28600  26.79000 1.000 54.55787  ?  290 LYS   A CG   1 
ATOM   921  C  CD   . LYS   A 1 138 ? 15.19700 18.69500  27.07200 1.000 64.41220  ?  290 LYS   A CD   1 
ATOM   922  C  CE   . LYS   A 1 138 ? 16.71400 18.76300  26.98100 1.000 66.46613  ?  290 LYS   A CE   1 
ATOM   923  N  NZ   . LYS   A 1 138 ? 17.29100 19.78600  27.89700 1.000 74.18134  ?  290 LYS   A NZ   1 
ATOM   924  N  N    . TYR   A 1 139 ? 13.11500 13.79600  27.13400 1.000 46.17774  ?  291 TYR   A N    1 
ATOM   925  C  CA   . TYR   A 1 139 ? 12.86300 12.72900  28.09100 1.000 48.61150  ?  291 TYR   A CA   1 
ATOM   926  C  C    . TYR   A 1 139 ? 14.04800 12.55300  29.02800 1.000 51.15836  ?  291 TYR   A C    1 
ATOM   927  O  O    . TYR   A 1 139 ? 15.20400 12.56300  28.59200 1.000 46.72971  ?  291 TYR   A O    1 
ATOM   928  C  CB   . TYR   A 1 139 ? 12.57700 11.41200  27.36900 1.000 43.02725  ?  291 TYR   A CB   1 
ATOM   929  C  CG   . TYR   A 1 139 ? 11.58900 11.54100  26.23300 1.000 41.29177  ?  291 TYR   A CG   1 
ATOM   930  C  CD1  . TYR   A 1 139 ? 12.02100 11.63500  24.91600 1.000 38.80712  ?  291 TYR   A CD1  1 
ATOM   931  C  CD2  . TYR   A 1 139 ? 10.22200 11.56500  26.47800 1.000 40.05167  ?  291 TYR   A CD2  1 
ATOM   932  C  CE1  . TYR   A 1 139 ? 11.11800 11.75200  23.87300 1.000 38.43284  ?  291 TYR   A CE1  1 
ATOM   933  C  CE2  . TYR   A 1 139 ? 9.31300  11.68100  25.44400 1.000 40.36940  ?  291 TYR   A CE2  1 
ATOM   934  C  CZ   . TYR   A 1 139 ? 9.76400  11.77400  24.14500 1.000 40.32294  ?  291 TYR   A CZ   1 
ATOM   935  O  OH   . TYR   A 1 139 ? 8.85700  11.89000  23.11500 1.000 39.59242  ?  291 TYR   A OH   1 
ATOM   936  N  N    . ASP   A 1 140 ? 13.75600 12.37900  30.31600 1.000 55.15249  ?  292 ASP   A N    1 
ATOM   937  C  CA   . ASP   A 1 140 ? 14.80800 12.15000  31.29900 1.000 55.73135  ?  292 ASP   A CA   1 
ATOM   938  C  C    . ASP   A 1 140 ? 14.54900 10.87800  32.10000 1.000 52.45862  ?  292 ASP   A C    1 
ATOM   939  O  O    . ASP   A 1 140 ? 13.72400 10.04600  31.70900 1.000 52.57329  ?  292 ASP   A O    1 
ATOM   940  C  CB   . ASP   A 1 140 ? 14.95000 13.36200  32.22500 1.000 60.39300  ?  292 ASP   A CB   1 
ATOM   941  C  CG   . ASP   A 1 140 ? 13.65600 13.72700  32.92500 1.000 65.27392  ?  292 ASP   A CG   1 
ATOM   942  O  OD1  . ASP   A 1 140 ? 13.23700 14.89800  32.82200 1.000 68.61370  ?  292 ASP   A OD1  1 
ATOM   943  O  OD2  . ASP   A 1 140 ? 13.06100 12.85400  33.58600 1.000 65.02389  ?  292 ASP   A OD2  1 
ATOM   944  N  N    A VAL   A 1 141 ? 15.26000 10.71400  33.21800 0.670 51.15855  ?  293 VAL   A N    1 
ATOM   945  N  N    B VAL   A 1 141 ? 15.24400 10.73800  33.23200 0.330 51.26794  ?  293 VAL   A N    1 
ATOM   946  C  CA   A VAL   A 1 141 ? 15.14200 9.48300   33.99300 0.670 49.92240  ?  293 VAL   A CA   1 
ATOM   947  C  CA   B VAL   A 1 141 ? 15.11600 9.53900   34.05800 0.330 50.12681  ?  293 VAL   A CA   1 
ATOM   948  C  C    A VAL   A 1 141 ? 13.76900 9.37000   34.64200 0.670 51.16763  ?  293 VAL   A C    1 
ATOM   949  C  C    B VAL   A 1 141 ? 13.70600 9.42400   34.62700 0.330 51.42413  ?  293 VAL   A C    1 
ATOM   950  O  O    A VAL   A 1 141 ? 13.27000 8.26000   34.86400 0.670 51.46693  ?  293 VAL   A O    1 
ATOM   951  O  O    B VAL   A 1 141 ? 13.14300 8.32600   34.71200 0.330 51.09692  ?  293 VAL   A O    1 
ATOM   952  C  CB   A VAL   A 1 141 ? 16.26800 9.40600   35.04100 0.670 49.54571  ?  293 VAL   A CB   1 
ATOM   953  C  CB   B VAL   A 1 141 ? 16.18200 9.55500   35.17100 0.330 50.23602  ?  293 VAL   A CB   1 
ATOM   954  C  CG1  A VAL   A 1 141 ? 17.60300 9.15000   34.36100 0.670 49.67614  ?  293 VAL   A CG1  1 
ATOM   955  C  CG1  B VAL   A 1 141 ? 15.79100 8.63200   36.31800 0.330 49.79846  ?  293 VAL   A CG1  1 
ATOM   956  C  CG2  A VAL   A 1 141 ? 16.32100 10.68800  35.85800 0.670 51.08177  ?  293 VAL   A CG2  1 
ATOM   957  C  CG2  B VAL   A 1 141 ? 17.54400 9.17500   34.60500 0.330 50.12280  ?  293 VAL   A CG2  1 
ATOM   958  N  N    A THR   A 1 142 ? 13.13300 10.50300  34.95400 0.670 54.23838  ?  294 THR   A N    1 
ATOM   959  N  N    B THR   A 1 142 ? 13.11100 10.55600  35.01700 0.330 53.95345  ?  294 THR   A N    1 
ATOM   960  C  CA   A THR   A 1 142 ? 11.82200 10.45800  35.59300 0.670 53.83822  ?  294 THR   A CA   1 
ATOM   961  C  CA   B THR   A 1 142 ? 11.77500 10.52900  35.60500 0.330 54.29079  ?  294 THR   A CA   1 
ATOM   962  C  C    A THR   A 1 142 ? 10.73900 10.00300  34.62500 0.670 52.24566  ?  294 THR   A C    1 
ATOM   963  C  C    B THR   A 1 142 ? 10.73800 9.99500   34.62400 0.330 52.33082  ?  294 THR   A C    1 
ATOM   964  O  O    A THR   A 1 142 ? 9.72800  9.43400   35.05200 0.670 52.75158  ?  294 THR   A O    1 
ATOM   965  O  O    B THR   A 1 142 ? 9.76900  9.34700   35.03700 0.330 52.63734  ?  294 THR   A O    1 
ATOM   966  C  CB   A THR   A 1 142 ? 11.47200 11.82800  36.17500 0.670 57.45389  ?  294 THR   A CB   1 
ATOM   967  C  CB   B THR   A 1 142 ? 11.38300 11.92900  36.08300 0.330 57.47378  ?  294 THR   A CB   1 
ATOM   968  O  OG1  A THR   A 1 142 ? 11.32800 12.77800  35.11200 0.670 57.26497  ?  294 THR   A OG1  1 
ATOM   969  O  OG1  B THR   A 1 142 ? 12.42200 12.45900  36.91500 0.330 59.56009  ?  294 THR   A OG1  1 
ATOM   970  C  CG2  A THR   A 1 142 ? 12.56600 12.29700  37.12100 0.670 59.51170  ?  294 THR   A CG2  1 
ATOM   971  C  CG2  B THR   A 1 142 ? 10.08300 11.88900  36.87300 0.330 59.17874  ?  294 THR   A CG2  1 
ATOM   972  N  N    . ASP   A 1 143 ? 10.92600 10.24200  33.32500 1.000 51.97194  ?  295 ASP   A N    1 
ATOM   973  C  CA   . ASP   A 1 143 ? 9.96300  9.76000   32.34000 1.000 51.82920  ?  295 ASP   A CA   1 
ATOM   974  C  C    . ASP   A 1 143 ? 10.02300 8.24300   32.20600 1.000 49.65944  ?  295 ASP   A C    1 
ATOM   975  O  O    . ASP   A 1 143 ? 8.98700  7.58800   32.04500 1.000 46.56097  ?  295 ASP   A O    1 
ATOM   976  C  CB   . ASP   A 1 143 ? 10.20700 10.43300  30.99000 1.000 49.31846  ?  295 ASP   A CB   1 
ATOM   977  C  CG   . ASP   A 1 143 ? 9.92100  11.92100  31.02300 1.000 54.77565  ?  295 ASP   A CG   1 
ATOM   978  O  OD1  . ASP   A 1 143 ? 8.86200  12.31200  31.55800 1.000 57.90113  ?  295 ASP   A OD1  1 
ATOM   979  O  OD2  . ASP   A 1 143 ? 10.75400 12.70200  30.51700 1.000 54.69700  ?  295 ASP   A OD2  1 
ATOM   980  N  N    . VAL   A 1 144 ? 11.22700 7.66800   32.26900 1.000 47.54512  ?  296 VAL   A N    1 
ATOM   981  C  CA   . VAL   A 1 144 ? 11.35600 6.21300   32.24000 1.000 45.73087  ?  296 VAL   A CA   1 
ATOM   982  C  C    . VAL   A 1 144 ? 10.70000 5.60000   33.47000 1.000 46.55652  ?  296 VAL   A C    1 
ATOM   983  O  O    . VAL   A 1 144 ? 10.04000 4.55600   33.38500 1.000 44.32510  ?  296 VAL   A O    1 
ATOM   984  C  CB   . VAL   A 1 144 ? 12.83700 5.80800   32.13200 1.000 50.28457  ?  296 VAL   A CB   1 
ATOM   985  C  CG1  . VAL   A 1 144 ? 12.96400 4.29600   32.01900 1.000 47.39326  ?  296 VAL   A CG1  1 
ATOM   986  C  CG2  . VAL   A 1 144 ? 13.49300 6.49600   30.94700 1.000 50.93860  ?  296 VAL   A CG2  1 
ATOM   987  N  N    A SER   A 1 145 ? 10.87900 6.23400   34.63200 0.420 48.90314  ?  297 SER   A N    1 
ATOM   988  N  N    B SER   A 1 145 ? 10.86500 6.23500   34.63200 0.580 48.78222  ?  297 SER   A N    1 
ATOM   989  C  CA   A SER   A 1 145 ? 10.24900 5.74700   35.85500 0.420 52.39929  ?  297 SER   A CA   1 
ATOM   990  C  CA   B SER   A 1 145 ? 10.24400 5.71400   35.84500 0.580 52.31532  ?  297 SER   A CA   1 
ATOM   991  C  C    A SER   A 1 145 ? 8.73100  5.80800   35.75200 0.420 52.69219  ?  297 SER   A C    1 
ATOM   992  C  C    B SER   A 1 145 ? 8.72600  5.83100   35.79400 0.580 52.97094  ?  297 SER   A C    1 
ATOM   993  O  O    A SER   A 1 145 ? 8.03100  4.90300   36.22200 0.420 51.93811  ?  297 SER   A O    1 
ATOM   994  O  O    B SER   A 1 145 ? 8.02200  4.98100   36.35100 0.580 51.57556  ?  297 SER   A O    1 
ATOM   995  C  CB   A SER   A 1 145 ? 10.73500 6.56100   37.05400 0.420 57.51949  ?  297 SER   A CB   1 
ATOM   996  C  CB   B SER   A 1 145 ? 10.79200 6.43800   37.07500 0.580 57.47390  ?  297 SER   A CB   1 
ATOM   997  O  OG   A SER   A 1 145 ? 11.42000 5.74200   37.98500 0.420 60.73275  ?  297 SER   A OG   1 
ATOM   998  O  OG   B SER   A 1 145 ? 10.34400 7.78000   37.11900 0.580 60.65254  ?  297 SER   A OG   1 
ATOM   999  N  N    . LYS   A 1 146 ? 8.20400  6.86500   35.13400 1.000 51.79049  ?  298 LYS   A N    1 
ATOM   1000 C  CA   . LYS   A 1 146 ? 6.76500  7.01000   34.96000 1.000 52.38844  ?  298 LYS   A CA   1 
ATOM   1001 C  C    . LYS   A 1 146 ? 6.20900  6.08400   33.88700 1.000 51.60979  ?  298 LYS   A C    1 
ATOM   1002 O  O    . LYS   A 1 146 ? 5.01500  6.16800   33.57800 1.000 51.34254  ?  298 LYS   A O    1 
ATOM   1003 C  CB   . LYS   A 1 146 ? 6.41800  8.46700   34.63900 1.000 55.11105  ?  298 LYS   A CB   1 
ATOM   1004 C  CG   . LYS   A 1 146 ? 6.51500  9.38400   35.85200 1.000 62.41917  ?  298 LYS   A CG   1 
ATOM   1005 C  CD   . LYS   A 1 146 ? 6.29400  10.84400  35.49400 1.000 66.10983  ?  298 LYS   A CD   1 
ATOM   1006 C  CE   . LYS   A 1 146 ? 6.36300  11.72000  36.73800 1.000 72.64854  ?  298 LYS   A CE   1 
ATOM   1007 N  NZ   . LYS   A 1 146 ? 6.10800  13.15600  36.43900 1.000 76.02365  ?  298 LYS   A NZ   1 
ATOM   1008 N  N    . ALA   A 1 147 ? 7.04100  5.22000   33.31000 1.000 45.94168  ?  299 ALA   A N    1 
ATOM   1009 C  CA   . ALA   A 1 147 ? 6.59200  4.12200   32.46900 1.000 45.46719  ?  299 ALA   A CA   1 
ATOM   1010 C  C    . ALA   A 1 147 ? 6.64600  2.78300   33.19000 1.000 46.08605  ?  299 ALA   A C    1 
ATOM   1011 O  O    . ALA   A 1 147 ? 6.28300  1.76100   32.59900 1.000 45.80235  ?  299 ALA   A O    1 
ATOM   1012 C  CB   . ALA   A 1 147 ? 7.43000  4.05600   31.18800 1.000 45.04324  ?  299 ALA   A CB   1 
ATOM   1013 N  N    . GLY   A 1 148 ? 7.09900  2.76200   34.44400 1.000 44.98990  ?  300 GLY   A N    1 
ATOM   1014 C  CA   . GLY   A 1 148 ? 7.10000  1.56000   35.25600 1.000 45.07862  ?  300 GLY   A CA   1 
ATOM   1015 C  C    . GLY   A 1 148 ? 8.46200  0.96700   35.55100 1.000 45.42061  ?  300 GLY   A C    1 
ATOM   1016 O  O    . GLY   A 1 148 ? 8.53300  -0.03000  36.27900 1.000 46.07182  ?  300 GLY   A O    1 
ATOM   1017 N  N    . HIS   A 1 149 ? 9.54200  1.54000   35.02900 1.000 44.24719  ?  301 HIS   A N    1 
ATOM   1018 C  CA   . HIS   A 1 149 ? 10.86100 0.94600   35.18900 1.000 41.06275  ?  301 HIS   A CA   1 
ATOM   1019 C  C    . HIS   A 1 149 ? 11.58300 1.51800   36.40700 1.000 47.84242  ?  301 HIS   A C    1 
ATOM   1020 O  O    . HIS   A 1 149 ? 11.28500 2.61700   36.88200 1.000 50.73979  ?  301 HIS   A O    1 
ATOM   1021 C  CB   . HIS   A 1 149 ? 11.69400 1.15200   33.92400 1.000 39.22205  ?  301 HIS   A CB   1 
ATOM   1022 C  CG   . HIS   A 1 149 ? 11.26400 0.28800   32.77900 1.000 37.39826  ?  301 HIS   A CG   1 
ATOM   1023 N  ND1  . HIS   A 1 149 ? 11.41500 -1.08200  32.78500 1.000 37.30229  ?  301 HIS   A ND1  1 
ATOM   1024 C  CD2  . HIS   A 1 149 ? 10.67700 0.59700   31.59900 1.000 37.46708  ?  301 HIS   A CD2  1 
ATOM   1025 C  CE1  . HIS   A 1 149 ? 10.94300 -1.58000  31.65600 1.000 39.72592  ?  301 HIS   A CE1  1 
ATOM   1026 N  NE2  . HIS   A 1 149 ? 10.49100 -0.58200  30.91800 1.000 39.27644  ?  301 HIS   A NE2  1 
ATOM   1027 N  N    . THR   A 1 150 ? 12.54500 0.74700   36.91000 1.000 49.40777  ?  302 THR   A N    1 
ATOM   1028 C  CA   . THR   A 1 150 ? 13.26400 1.04500   38.14100 1.000 48.57080  ?  302 THR   A CA   1 
ATOM   1029 C  C    . THR   A 1 150 ? 14.72400 1.37500   37.83700 1.000 47.14446  ?  302 THR   A C    1 
ATOM   1030 O  O    . THR   A 1 150 ? 15.18700 1.28600   36.69600 1.000 46.81086  ?  302 THR   A O    1 
ATOM   1031 C  CB   . THR   A 1 150 ? 13.17100 -0.13200  39.11600 1.000 51.72592  ?  302 THR   A CB   1 
ATOM   1032 O  OG1  . THR   A 1 150 ? 14.01600 -1.19800  38.66500 1.000 54.85044  ?  302 THR   A OG1  1 
ATOM   1033 C  CG2  . THR   A 1 150 ? 11.74000 -0.63500  39.21100 1.000 54.55261  ?  302 THR   A CG2  1 
ATOM   1034 N  N    . LEU   A 1 151 ? 15.45700 1.75200   38.89000 1.000 45.77183  ?  303 LEU   A N    1 
ATOM   1035 C  CA   . LEU   A 1 151 ? 16.87100 2.08300   38.74600 1.000 46.89832  ?  303 LEU   A CA   1 
ATOM   1036 C  C    . LEU   A 1 151 ? 17.71600 0.88200   38.34900 1.000 49.10113  ?  303 LEU   A C    1 
ATOM   1037 O  O    . LEU   A 1 151 ? 18.81600 1.07000   37.81800 1.000 51.75698  ?  303 LEU   A O    1 
ATOM   1038 C  CB   . LEU   A 1 151 ? 17.41500 2.67900   40.04400 1.000 51.81280  ?  303 LEU   A CB   1 
ATOM   1039 C  CG   . LEU   A 1 151 ? 18.38500 3.84700   39.86000 1.000 58.09837  ?  303 LEU   A CG   1 
ATOM   1040 C  CD1  . LEU   A 1 151 ? 17.66000 5.06200   39.29400 1.000 64.83682  ?  303 LEU   A CD1  1 
ATOM   1041 C  CD2  . LEU   A 1 151 ? 19.08400 4.18800   41.16600 1.000 59.38947  ?  303 LEU   A CD2  1 
ATOM   1042 N  N    A GLU   A 1 152 ? 17.23500 -0.33900  38.60800 0.560 49.04110  ?  304 GLU   A N    1 
ATOM   1043 N  N    B GLU   A 1 152 ? 17.23700 -0.34100  38.60200 0.440 49.22722  ?  304 GLU   A N    1 
ATOM   1044 C  CA   A GLU   A 1 152 ? 17.93500 -1.53600  38.15300 0.560 50.69025  ?  304 GLU   A CA   1 
ATOM   1045 C  CA   B GLU   A 1 152 ? 17.95700 -1.52800  38.15100 0.440 50.63399  ?  304 GLU   A CA   1 
ATOM   1046 C  C    A GLU   A 1 152 ? 18.22500 -1.47800  36.66100 0.560 47.26016  ?  304 GLU   A C    1 
ATOM   1047 C  C    B GLU   A 1 152 ? 18.23000 -1.47900  36.65600 0.440 47.07870  ?  304 GLU   A C    1 
ATOM   1048 O  O    A GLU   A 1 152 ? 19.23400 -2.02200  36.19800 0.560 44.80865  ?  304 GLU   A O    1 
ATOM   1049 O  O    B GLU   A 1 152 ? 19.23200 -2.03000  36.18400 0.440 45.06036  ?  304 GLU   A O    1 
ATOM   1050 C  CB   A GLU   A 1 152 ? 17.10700 -2.78000  38.47900 0.560 54.42514  ?  304 GLU   A CB   1 
ATOM   1051 C  CB   B GLU   A 1 152 ? 17.16300 -2.78800  38.49700 0.440 54.25941  ?  304 GLU   A CB   1 
ATOM   1052 C  CG   A GLU   A 1 152 ? 17.30500 -3.32000  39.88300 0.560 58.57555  ?  304 GLU   A CG   1 
ATOM   1053 C  CG   B GLU   A 1 152 ? 17.95200 -3.83800  39.25900 0.440 57.80990  ?  304 GLU   A CG   1 
ATOM   1054 C  CD   A GLU   A 1 152 ? 18.34700 -4.42000  39.93900 0.560 61.30900  ?  304 GLU   A CD   1 
ATOM   1055 C  CD   B GLU   A 1 152 ? 17.66300 -3.81500  40.74600 0.440 62.54494  ?  304 GLU   A CD   1 
ATOM   1056 O  OE1  A GLU   A 1 152 ? 17.97300 -5.57800  40.21900 0.560 63.06913  ?  304 GLU   A OE1  1 
ATOM   1057 O  OE1  B GLU   A 1 152 ? 16.68000 -3.15700  41.14800 0.440 62.57652  ?  304 GLU   A OE1  1 
ATOM   1058 O  OE2  A GLU   A 1 152 ? 19.53800 -4.12700  39.70300 0.560 59.35605  ?  304 GLU   A OE2  1 
ATOM   1059 O  OE2  B GLU   A 1 152 ? 18.41200 -4.45800  41.51200 0.440 64.37465  ?  304 GLU   A OE2  1 
ATOM   1060 N  N    . LEU   A 1 153 ? 17.35400 -0.82300  35.89700 1.000 42.55183  ?  305 LEU   A N    1 
ATOM   1061 C  CA   . LEU   A 1 153 ? 17.54100 -0.61500  34.47000 1.000 38.93143  ?  305 LEU   A CA   1 
ATOM   1062 C  C    . LEU   A 1 153 ? 18.01500 0.79400   34.14100 1.000 39.97108  ?  305 LEU   A C    1 
ATOM   1063 O  O    . LEU   A 1 153 ? 18.87000 0.96600   33.26900 1.000 42.69403  ?  305 LEU   A O    1 
ATOM   1064 C  CB   . LEU   A 1 153 ? 16.23100 -0.89600  33.72600 1.000 37.42411  ?  305 LEU   A CB   1 
ATOM   1065 C  CG   . LEU   A 1 153 ? 16.22900 -0.67500  32.21300 1.000 34.17110  ?  305 LEU   A CG   1 
ATOM   1066 C  CD1  . LEU   A 1 153 ? 17.11700 -1.69700  31.52300 1.000 34.42595  ?  305 LEU   A CD1  1 
ATOM   1067 C  CD2  . LEU   A 1 153 ? 14.80900 -0.73100  31.66200 1.000 32.02883  ?  305 LEU   A CD2  1 
ATOM   1068 N  N    . ILE   A 1 154 ? 17.49100 1.80400   34.83900 1.000 43.26235  ?  306 ILE   A N    1 
ATOM   1069 C  CA   . ILE   A 1 154 ? 17.73500 3.19000   34.44900 1.000 44.00133  ?  306 ILE   A CA   1 
ATOM   1070 C  C    . ILE   A 1 154 ? 19.18500 3.58600   34.70400 1.000 41.81768  ?  306 ILE   A C    1 
ATOM   1071 O  O    . ILE   A 1 154 ? 19.80700 4.26300   33.87700 1.000 39.28013  ?  306 ILE   A O    1 
ATOM   1072 C  CB   . ILE   A 1 154 ? 16.75400 4.12600   35.17600 1.000 46.65058  ?  306 ILE   A CB   1 
ATOM   1073 C  CG1  . ILE   A 1 154 ? 15.31400 3.81000   34.76500 1.000 43.47410  ?  306 ILE   A CG1  1 
ATOM   1074 C  CG2  . ILE   A 1 154 ? 17.07600 5.57200   34.86900 1.000 48.28554  ?  306 ILE   A CG2  1 
ATOM   1075 C  CD1  . ILE   A 1 154 ? 14.27400 4.55400   35.57500 1.000 48.45367  ?  306 ILE   A CD1  1 
ATOM   1076 N  N    . GLU   A 1 155 ? 19.74600 3.18800   35.85000 1.000 47.16432  ?  307 GLU   A N    1 
ATOM   1077 C  CA   . GLU   A 1 155 ? 21.13800 3.53100   36.13800 1.000 44.46306  ?  307 GLU   A CA   1 
ATOM   1078 C  C    . GLU   A 1 155 ? 22.09700 2.94100   35.11000 1.000 43.89798  ?  307 GLU   A C    1 
ATOM   1079 O  O    . GLU   A 1 155 ? 22.89000 3.70000   34.52600 1.000 46.95771  ?  307 GLU   A O    1 
ATOM   1080 C  CB   . GLU   A 1 155 ? 21.49400 3.11700   37.56900 1.000 52.22054  ?  307 GLU   A CB   1 
ATOM   1081 C  CG   . GLU   A 1 155 ? 22.82200 3.68200   38.06700 1.000 60.77479  ?  307 GLU   A CG   1 
ATOM   1082 C  CD   . GLU   A 1 155 ? 23.88900 2.61500   38.23400 1.000 67.55043  ?  307 GLU   A CD   1 
ATOM   1083 O  OE1  . GLU   A 1 155 ? 23.60900 1.43600   37.93300 1.000 68.50831  ?  307 GLU   A OE1  1 
ATOM   1084 O  OE2  . GLU   A 1 155 ? 25.01100 2.95400   38.66700 1.000 71.18014  ?  307 GLU   A OE2  1 
ATOM   1085 N  N    . PRO   A 1 156 ? 22.08300 1.63200   34.82700 1.000 43.61880  ?  308 PRO   A N    1 
ATOM   1086 C  CA   . PRO   A 1 156 ? 22.96700 1.12900   33.76200 1.000 42.93268  ?  308 PRO   A CA   1 
ATOM   1087 C  C    . PRO   A 1 156 ? 22.63500 1.69500   32.39300 1.000 43.77129  ?  308 PRO   A C    1 
ATOM   1088 O  O    . PRO   A 1 156 ? 23.51700 1.75600   31.52700 1.000 40.37259  ?  308 PRO   A O    1 
ATOM   1089 C  CB   . PRO   A 1 156 ? 22.75200 -0.39100  33.81300 1.000 48.49191  ?  308 PRO   A CB   1 
ATOM   1090 C  CG   . PRO   A 1 156 ? 22.17100 -0.65900  35.16100 1.000 51.43146  ?  308 PRO   A CG   1 
ATOM   1091 C  CD   . PRO   A 1 156 ? 21.32700 0.53400   35.45500 1.000 47.23713  ?  308 PRO   A CD   1 
ATOM   1092 N  N    . LEU   A 1 157 ? 21.38600 2.11100   32.16900 1.000 38.51414  ?  309 LEU   A N    1 
ATOM   1093 C  CA   . LEU   A 1 157 ? 21.01600 2.69900   30.88600 1.000 37.56850  ?  309 LEU   A CA   1 
ATOM   1094 C  C    . LEU   A 1 157 ? 21.69400 4.04800   30.68300 1.000 39.53733  ?  309 LEU   A C    1 
ATOM   1095 O  O    . LEU   A 1 157 ? 22.22700 4.33200   29.60200 1.000 38.80769  ?  309 LEU   A O    1 
ATOM   1096 C  CB   . LEU   A 1 157 ? 19.49500 2.84400   30.80000 1.000 38.22672  ?  309 LEU   A CB   1 
ATOM   1097 C  CG   . LEU   A 1 157 ? 18.93300 3.48700   29.53100 1.000 38.27993  ?  309 LEU   A CG   1 
ATOM   1098 C  CD1  . LEU   A 1 157 ? 19.45100 2.77900   28.28600 1.000 38.61067  ?  309 LEU   A CD1  1 
ATOM   1099 C  CD2  . LEU   A 1 157 ? 17.41100 3.49500   29.55700 1.000 38.04061  ?  309 LEU   A CD2  1 
ATOM   1100 N  N    . ILE   A 1 158 ? 21.67800 4.89900   31.71300 1.000 40.58728  ?  310 ILE   A N    1 
ATOM   1101 C  CA   . ILE   A 1 158 ? 22.32100 6.20500   31.60500 1.000 42.72890  ?  310 ILE   A CA   1 
ATOM   1102 C  C    . ILE   A 1 158 ? 23.82700 6.04700   31.44800 1.000 39.86357  ?  310 ILE   A C    1 
ATOM   1103 O  O    . ILE   A 1 158 ? 24.45200 6.72600   30.62300 1.000 40.53983  ?  310 ILE   A O    1 
ATOM   1104 C  CB   . ILE   A 1 158 ? 21.96300 7.08200   32.81800 1.000 46.11223  ?  310 ILE   A CB   1 
ATOM   1105 C  CG1  . ILE   A 1 158 ? 20.47500 7.43700   32.79400 1.000 46.31457  ?  310 ILE   A CG1  1 
ATOM   1106 C  CG2  . ILE   A 1 158 ? 22.81500 8.34600   32.83400 1.000 47.92690  ?  310 ILE   A CG2  1 
ATOM   1107 C  CD1  . ILE   A 1 158 ? 20.09400 8.37800   31.66800 1.000 47.55285  ?  310 ILE   A CD1  1 
ATOM   1108 N  N    A LYS   A 1 159 ? 24.43600 5.15300   32.23300 0.440 41.85545  ?  311 LYS   A N    1 
ATOM   1109 N  N    B LYS   A 1 159 ? 24.43400 5.15000   32.23200 0.560 41.94223  ?  311 LYS   A N    1 
ATOM   1110 C  CA   A LYS   A 1 159 ? 25.86800 4.90400   32.09600 0.440 42.02338  ?  311 LYS   A CA   1 
ATOM   1111 C  CA   B LYS   A 1 159 ? 25.86500 4.89600   32.09800 0.560 41.87703  ?  311 LYS   A CA   1 
ATOM   1112 C  C    A LYS   A 1 159 ? 26.21500 4.40100   30.70200 0.440 39.88513  ?  311 LYS   A C    1 
ATOM   1113 C  C    B LYS   A 1 159 ? 26.21000 4.41200   30.69600 0.560 40.02212  ?  311 LYS   A C    1 
ATOM   1114 O  O    A LYS   A 1 159 ? 27.29100 4.71200   30.17900 0.440 39.24884  ?  311 LYS   A O    1 
ATOM   1115 O  O    B LYS   A 1 159 ? 27.27300 4.74300   30.15900 0.560 38.89927  ?  311 LYS   A O    1 
ATOM   1116 C  CB   A LYS   A 1 159 ? 26.33600 3.90100   33.15000 0.440 46.52633  ?  311 LYS   A CB   1 
ATOM   1117 C  CB   B LYS   A 1 159 ? 26.32000 3.87500   33.14200 0.560 46.43597  ?  311 LYS   A CB   1 
ATOM   1118 C  CG   A LYS   A 1 159 ? 26.25300 4.41600   34.57700 0.440 52.85106  ?  311 LYS   A CG   1 
ATOM   1119 C  CG   B LYS   A 1 159 ? 26.27700 4.37700   34.57600 0.560 52.97169  ?  311 LYS   A CG   1 
ATOM   1120 C  CD   A LYS   A 1 159 ? 26.48200 3.29900   35.58500 0.440 56.79445  ?  311 LYS   A CD   1 
ATOM   1121 C  CD   B LYS   A 1 159 ? 26.69500 3.28500   35.55000 0.560 56.99307  ?  311 LYS   A CD   1 
ATOM   1122 C  CE   A LYS   A 1 159 ? 27.96300 3.10400   35.87000 0.440 59.83415  ?  311 LYS   A CE   1 
ATOM   1123 C  CE   B LYS   A 1 159 ? 27.49500 3.84500   36.71700 0.560 61.12028  ?  311 LYS   A CE   1 
ATOM   1124 N  NZ   A LYS   A 1 159 ? 28.60500 2.17000   34.90300 0.440 59.70557  ?  311 LYS   A NZ   1 
ATOM   1125 N  NZ   B LYS   A 1 159 ? 27.26600 5.30300   36.90700 0.560 63.04885  ?  311 LYS   A NZ   1 
ATOM   1126 N  N    . PHE   A 1 160 ? 25.31800 3.62900   30.08400 1.000 37.41953  ?  312 PHE   A N    1 
ATOM   1127 C  CA   . PHE   A 1 160 ? 25.55400 3.16400   28.72200 1.000 32.77307  ?  312 PHE   A CA   1 
ATOM   1128 C  C    . PHE   A 1 160 ? 25.49000 4.32000   27.73200 1.000 35.47764  ?  312 PHE   A C    1 
ATOM   1129 O  O    . PHE   A 1 160 ? 26.35400 4.44900   26.85600 1.000 35.87729  ?  312 PHE   A O    1 
ATOM   1130 C  CB   . PHE   A 1 160 ? 24.53800 2.08100   28.35300 1.000 35.73192  ?  312 PHE   A CB   1 
ATOM   1131 C  CG   . PHE   A 1 160 ? 24.57500 1.68600   26.90300 1.000 37.21633  ?  312 PHE   A CG   1 
ATOM   1132 C  CD1  . PHE   A 1 160 ? 25.45100 0.70800   26.46000 1.000 39.71849  ?  312 PHE   A CD1  1 
ATOM   1133 C  CD2  . PHE   A 1 160 ? 23.73800 2.29500   25.98200 1.000 35.31899  ?  312 PHE   A CD2  1 
ATOM   1134 C  CE1  . PHE   A 1 160 ? 25.49100 0.34600   25.12500 1.000 36.42878  ?  312 PHE   A CE1  1 
ATOM   1135 C  CE2  . PHE   A 1 160 ? 23.77600 1.93900   24.64800 1.000 37.32046  ?  312 PHE   A CE2  1 
ATOM   1136 C  CZ   . PHE   A 1 160 ? 24.65400 0.96300   24.21900 1.000 35.47879  ?  312 PHE   A CZ   1 
ATOM   1137 N  N    . GLN   A 1 161 ? 24.46100 5.16500   27.84800 1.000 35.58895  ?  313 GLN   A N    1 
ATOM   1138 C  CA   . GLN   A 1 161 ? 24.32500 6.30100   26.94000 1.000 34.28823  ?  313 GLN   A CA   1 
ATOM   1139 C  C    . GLN   A 1 161 ? 25.52200 7.23700   27.04700 1.000 32.51732  ?  313 GLN   A C    1 
ATOM   1140 O  O    . GLN   A 1 161 ? 26.00100 7.76400   26.03600 1.000 35.77099  ?  313 GLN   A O    1 
ATOM   1141 C  CB   . GLN   A 1 161 ? 23.02800 7.05700   27.23500 1.000 34.81947  ?  313 GLN   A CB   1 
ATOM   1142 C  CG   . GLN   A 1 161 ? 21.75500 6.25800   26.98800 1.000 32.36895  ?  313 GLN   A CG   1 
ATOM   1143 C  CD   . GLN   A 1 161 ? 21.58200 5.86700   25.53400 1.000 33.49104  ?  313 GLN   A CD   1 
ATOM   1144 O  OE1  . GLN   A 1 161 ? 21.94600 6.61800   24.63000 1.000 33.21828  ?  313 GLN   A OE1  1 
ATOM   1145 N  NE2  . GLN   A 1 161 ? 21.02500 4.68500   25.30200 1.000 33.15538  ?  313 GLN   A NE2  1 
ATOM   1146 N  N    . VAL   A 1 162 ? 26.01900 7.45200   28.26500 1.000 36.48302  ?  314 VAL   A N    1 
ATOM   1147 C  CA   . VAL   A 1 162 ? 27.16500 8.33600   28.45700 1.000 37.83219  ?  314 VAL   A CA   1 
ATOM   1148 C  C    . VAL   A 1 162 ? 28.42000 7.71600   27.85600 1.000 38.52884  ?  314 VAL   A C    1 
ATOM   1149 O  O    . VAL   A 1 162 ? 29.17800 8.37900   27.13600 1.000 39.37688  ?  314 VAL   A O    1 
ATOM   1150 C  CB   . VAL   A 1 162 ? 27.35000 8.65300   29.95100 1.000 40.66973  ?  314 VAL   A CB   1 
ATOM   1151 C  CG1  . VAL   A 1 162 ? 28.70100 9.32100   30.19800 1.000 39.63623  ?  314 VAL   A CG1  1 
ATOM   1152 C  CG2  . VAL   A 1 162 ? 26.21500 9.53300   30.44200 1.000 38.23259  ?  314 VAL   A CG2  1 
ATOM   1153 N  N    . GLY   A 1 163 ? 28.65600 6.43100   28.13600 1.000 42.22134  ?  315 GLY   A N    1 
ATOM   1154 C  CA   . GLY   A 1 163 ? 29.83700 5.77300   27.60000 1.000 39.66831  ?  315 GLY   A CA   1 
ATOM   1155 C  C    . GLY   A 1 163 ? 29.83200 5.67700   26.08800 1.000 36.35842  ?  315 GLY   A C    1 
ATOM   1156 O  O    . GLY   A 1 163 ? 30.88600 5.76500   25.45400 1.000 35.32696  ?  315 GLY   A O    1 
ATOM   1157 N  N    . LEU   A 1 164 ? 28.65100 5.49800   25.49000 1.000 32.89235  ?  316 LEU   A N    1 
ATOM   1158 C  CA   . LEU   A 1 164 ? 28.56000 5.44800   24.03500 1.000 34.73764  ?  316 LEU   A CA   1 
ATOM   1159 C  C    . LEU   A 1 164 ? 28.78300 6.82300   23.42000 1.000 35.69252  ?  316 LEU   A C    1 
ATOM   1160 O  O    . LEU   A 1 164 ? 29.44100 6.94600   22.37900 1.000 36.67205  ?  316 LEU   A O    1 
ATOM   1161 C  CB   . LEU   A 1 164 ? 27.20200 4.88700   23.61400 1.000 33.92282  ?  316 LEU   A CB   1 
ATOM   1162 C  CG   . LEU   A 1 164 ? 26.94100 4.73800   22.11500 1.000 33.24309  ?  316 LEU   A CG   1 
ATOM   1163 C  CD1  . LEU   A 1 164 ? 27.99800 3.86200   21.46400 1.000 33.23928  ?  316 LEU   A CD1  1 
ATOM   1164 C  CD2  . LEU   A 1 164 ? 25.55100 4.16700   21.88200 1.000 28.49188  ?  316 LEU   A CD2  1 
ATOM   1165 N  N    . LYS   A 1 165 ? 28.23900 7.87000   24.04800 1.000 32.70234  ?  317 LYS   A N    1 
ATOM   1166 C  CA   . LYS   A 1 165 ? 28.45600 9.22600   23.55200 1.000 39.33957  ?  317 LYS   A CA   1 
ATOM   1167 C  C    . LYS   A 1 165 ? 29.92900 9.60800   23.62600 1.000 39.84311  ?  317 LYS   A C    1 
ATOM   1168 O  O    . LYS   A 1 165 ? 30.45300 10.27100  22.72300 1.000 47.98509  ?  317 LYS   A O    1 
ATOM   1169 C  CB   . LYS   A 1 165 ? 27.60800 10.21800  24.34700 1.000 44.40776  ?  317 LYS   A CB   1 
ATOM   1170 C  CG   . LYS   A 1 165 ? 27.21900 11.46300  23.56900 1.000 45.87396  ?  317 LYS   A CG   1 
ATOM   1171 C  CD   . LYS   A 1 165 ? 26.06300 11.18600  22.62500 1.000 46.47065  ?  317 LYS   A CD   1 
ATOM   1172 C  CE   . LYS   A 1 165 ? 25.51600 12.47500  22.03900 1.000 48.87795  ?  317 LYS   A CE   1 
ATOM   1173 N  NZ   . LYS   A 1 165 ? 24.58500 12.21600  20.90900 1.000 41.80650  ?  317 LYS   A NZ   1 
ATOM   1174 N  N    . LYS   A 1 166 ? 30.61300 9.19400   24.69600 1.000 39.75116  ?  318 LYS   A N    1 
ATOM   1175 C  CA   . LYS   A 1 166 ? 32.02600 9.52000   24.85900 1.000 40.19650  ?  318 LYS   A CA   1 
ATOM   1176 C  C    . LYS   A 1 166 ? 32.89600 8.87500   23.78900 1.000 43.96015  ?  318 LYS   A C    1 
ATOM   1177 O  O    . LYS   A 1 166 ? 34.03700 9.30600   23.59300 1.000 39.51276  ?  318 LYS   A O    1 
ATOM   1178 C  CB   . LYS   A 1 166 ? 32.51200 9.09300   26.24500 1.000 43.77827  ?  318 LYS   A CB   1 
ATOM   1179 C  CG   . LYS   A 1 166 ? 32.03300 9.98700   27.37500 1.000 50.12099  ?  318 LYS   A CG   1 
ATOM   1180 C  CD   . LYS   A 1 166 ? 32.49800 9.46000   28.72200 1.000 51.59100  ?  318 LYS   A CD   1 
ATOM   1181 C  CE   . LYS   A 1 166 ? 32.24500 10.46900  29.83000 1.000 59.26558  ?  318 LYS   A CE   1 
ATOM   1182 N  NZ   . LYS   A 1 166 ? 32.77600 9.99400   31.14000 1.000 57.31879  ?  318 LYS   A NZ   1 
ATOM   1183 N  N    . LEU   A 1 167 ? 32.39100 7.85300   23.09600 1.000 40.06702  ?  319 LEU   A N    1 
ATOM   1184 C  CA   . LEU   A 1 167 ? 33.16600 7.24100   22.02600 1.000 40.56707  ?  319 LEU   A CA   1 
ATOM   1185 C  C    . LEU   A 1 167 ? 33.26200 8.13900   20.80000 1.000 42.21325  ?  319 LEU   A C    1 
ATOM   1186 O  O    . LEU   A 1 167 ? 34.18400 7.96100   19.99500 1.000 40.97677  ?  319 LEU   A O    1 
ATOM   1187 C  CB   . LEU   A 1 167 ? 32.56200 5.88900   21.64600 1.000 35.28759  ?  319 LEU   A CB   1 
ATOM   1188 C  CG   . LEU   A 1 167 ? 32.70600 4.79100   22.70300 1.000 36.66604  ?  319 LEU   A CG   1 
ATOM   1189 C  CD1  . LEU   A 1 167 ? 32.21500 3.45300   22.17400 1.000 37.69360  ?  319 LEU   A CD1  1 
ATOM   1190 C  CD2  . LEU   A 1 167 ? 34.15300 4.68700   23.17100 1.000 38.47966  ?  319 LEU   A CD2  1 
ATOM   1191 N  N    A ASN   A 1 168 ? 32.34100 9.09000   20.64400 0.550 40.39410  ?  320 ASN   A N    1 
ATOM   1192 N  N    B ASN   A 1 168 ? 32.35200 9.10700   20.66500 0.450 40.55709  ?  320 ASN   A N    1 
ATOM   1193 C  CA   A ASN   A 1 168 ? 32.33800 10.01600  19.51100 0.550 41.09547  ?  320 ASN   A CA   1 
ATOM   1194 C  CA   B ASN   A 1 168 ? 32.29100 10.01700  19.51900 0.450 41.07681  ?  320 ASN   A CA   1 
ATOM   1195 C  C    A ASN   A 1 168 ? 32.43400 9.26200   18.18700 0.550 40.04657  ?  320 ASN   A C    1 
ATOM   1196 C  C    B ASN   A 1 168 ? 32.43400 9.25600   18.20400 0.450 40.05829  ?  320 ASN   A C    1 
ATOM   1197 O  O    A ASN   A 1 168 ? 33.27400 9.55600   17.33300 0.550 42.05540  ?  320 ASN   A O    1 
ATOM   1198 O  O    B ASN   A 1 168 ? 33.29900 9.54400   17.37500 0.450 42.02790  ?  320 ASN   A O    1 
ATOM   1199 C  CB   A ASN   A 1 168 ? 33.46600 11.04200  19.63700 0.550 43.93202  ?  320 ASN   A CB   1 
ATOM   1200 C  CB   B ASN   A 1 168 ? 33.34000 11.12500  19.63100 0.450 44.09568  ?  320 ASN   A CB   1 
ATOM   1201 C  CG   A ASN   A 1 168 ? 33.43200 11.79000  20.95400 0.550 47.42288  ?  320 ASN   A CG   1 
ATOM   1202 C  CG   B ASN   A 1 168 ? 32.96800 12.35800  18.82400 0.450 45.28384  ?  320 ASN   A CG   1 
ATOM   1203 O  OD1  A ASN   A 1 168 ? 32.48500 12.52200  21.24000 0.550 47.82118  ?  320 ASN   A OD1  1 
ATOM   1204 O  OD1  B ASN   A 1 168 ? 31.83600 12.48800  18.35500 0.450 45.80071  ?  320 ASN   A OD1  1 
ATOM   1205 N  ND2  A ASN   A 1 168 ? 34.47100 11.61500  21.76200 0.550 53.13961  ?  320 ASN   A ND2  1 
ATOM   1206 N  ND2  B ASN   A 1 168 ? 33.92100 13.26700  18.65600 0.450 46.94037  ?  320 ASN   A ND2  1 
ATOM   1207 N  N    . LEU   A 1 169 ? 31.56800 8.26200   18.02800 1.000 35.55835  ?  321 LEU   A N    1 
ATOM   1208 C  CA   . LEU   A 1 169 ? 31.60600 7.43500   16.83300 1.000 40.16103  ?  321 LEU   A CA   1 
ATOM   1209 C  C    . LEU   A 1 169 ? 31.33800 8.26800   15.58900 1.000 40.55794  ?  321 LEU   A C    1 
ATOM   1210 O  O    . LEU   A 1 169 ? 30.51600 9.18800   15.60000 1.000 40.82681  ?  321 LEU   A O    1 
ATOM   1211 C  CB   . LEU   A 1 169 ? 30.56900 6.31500   16.93100 1.000 37.19809  ?  321 LEU   A CB   1 
ATOM   1212 C  CG   . LEU   A 1 169 ? 30.70400 5.30000   18.06500 1.000 35.15177  ?  321 LEU   A CG   1 
ATOM   1213 C  CD1  . LEU   A 1 169 ? 29.63300 4.22500   17.93800 1.000 33.64862  ?  321 LEU   A CD1  1 
ATOM   1214 C  CD2  . LEU   A 1 169 ? 32.09300 4.68100   18.06700 1.000 33.21689  ?  321 LEU   A CD2  1 
ATOM   1215 N  N    . HIS   A 1 170 ? 32.05500 7.95500   14.51400 1.000 38.75931  ?  322 HIS   A N    1 
ATOM   1216 C  CA   . HIS   A 1 170 ? 31.62100 8.40600   13.20400 1.000 35.72548  ?  322 HIS   A CA   1 
ATOM   1217 C  C    . HIS   A 1 170 ? 30.25700 7.79900   12.90500 1.000 34.79935  ?  322 HIS   A C    1 
ATOM   1218 O  O    . HIS   A 1 170 ? 29.89800 6.74200   13.43300 1.000 37.64388  ?  322 HIS   A O    1 
ATOM   1219 C  CB   . HIS   A 1 170 ? 32.62400 7.99700   12.12400 1.000 36.47331  ?  322 HIS   A CB   1 
ATOM   1220 C  CG   . HIS   A 1 170 ? 33.99100 8.57900   12.30900 1.000 39.32058  ?  322 HIS   A CG   1 
ATOM   1221 N  ND1  . HIS   A 1 170 ? 35.03500 8.31000   11.45100 1.000 39.65696  ?  322 HIS   A ND1  1 
ATOM   1222 C  CD2  . HIS   A 1 170 ? 34.48600 9.41500   13.25200 1.000 40.65369  ?  322 HIS   A CD2  1 
ATOM   1223 C  CE1  . HIS   A 1 170 ? 36.11400 8.95500   11.85600 1.000 40.13809  ?  322 HIS   A CE1  1 
ATOM   1224 N  NE2  . HIS   A 1 170 ? 35.80800 9.63200   12.94800 1.000 40.29968  ?  322 HIS   A NE2  1 
ATOM   1225 N  N    . GLU   A 1 171 ? 29.48000 8.48300   12.06300 1.000 34.85027  ?  323 GLU   A N    1 
ATOM   1226 C  CA   . GLU   A 1 171 ? 28.20700 7.90800   11.64200 1.000 33.96841  ?  323 GLU   A CA   1 
ATOM   1227 C  C    . GLU   A 1 171 ? 28.40800 6.54200   11.00200 1.000 36.78677  ?  323 GLU   A C    1 
ATOM   1228 O  O    . GLU   A 1 171 ? 27.55500 5.65900   11.13800 1.000 36.48017  ?  323 GLU   A O    1 
ATOM   1229 C  CB   . GLU   A 1 171 ? 27.49300 8.84700   10.67300 1.000 40.12284  ?  323 GLU   A CB   1 
ATOM   1230 C  CG   . GLU   A 1 171 ? 25.99800 8.59800   10.57400 1.000 46.24127  ?  323 GLU   A CG   1 
ATOM   1231 C  CD   . GLU   A 1 171 ? 25.31600 9.54300   9.61000  1.000 50.56121  ?  323 GLU   A CD   1 
ATOM   1232 O  OE1  . GLU   A 1 171 ? 26.02200 10.33800  8.95200  1.000 53.91010  ?  323 GLU   A OE1  1 
ATOM   1233 O  OE2  . GLU   A 1 171 ? 24.07300 9.49100   9.51000  1.000 53.45868  ?  323 GLU   A OE2  1 
ATOM   1234 N  N    . GLU   A 1 172 ? 29.53800 6.35100   10.31800 1.000 34.15771  ?  324 GLU   A N    1 
ATOM   1235 C  CA   . GLU   A 1 172 ? 29.85500 5.05100   9.73700  1.000 36.48876  ?  324 GLU   A CA   1 
ATOM   1236 C  C    . GLU   A 1 172 ? 29.97700 3.97600   10.81200 1.000 36.51530  ?  324 GLU   A C    1 
ATOM   1237 O  O    . GLU   A 1 172 ? 29.50500 2.84800   10.62900 1.000 37.82292  ?  324 GLU   A O    1 
ATOM   1238 C  CB   . GLU   A 1 172 ? 31.15200 5.15100   8.93100  1.000 34.12595  ?  324 GLU   A CB   1 
ATOM   1239 C  CG   . GLU   A 1 172 ? 31.04700 5.99800   7.67000  1.000 42.23450  ?  324 GLU   A CG   1 
ATOM   1240 C  CD   . GLU   A 1 172 ? 31.24800 7.48300   7.92200  1.000 48.73618  ?  324 GLU   A CD   1 
ATOM   1241 O  OE1  . GLU   A 1 172 ? 31.43300 8.22800   6.93700  1.000 51.56506  ?  324 GLU   A OE1  1 
ATOM   1242 O  OE2  . GLU   A 1 172 ? 31.21800 7.90900   9.09500  1.000 44.95060  ?  324 GLU   A OE2  1 
ATOM   1243 N  N    . GLU   A 1 173 ? 30.61600 4.30500   11.93700 1.000 29.43498  ?  325 GLU   A N    1 
ATOM   1244 C  CA   . GLU   A 1 173 ? 30.74800 3.33800   13.02300 1.000 28.64940  ?  325 GLU   A CA   1 
ATOM   1245 C  C    . GLU   A 1 173 ? 29.42200 3.13500   13.74700 1.000 33.41543  ?  325 GLU   A C    1 
ATOM   1246 O  O    . GLU   A 1 173 ? 29.12100 2.02700   14.20700 1.000 31.35499  ?  325 GLU   A O    1 
ATOM   1247 C  CB   . GLU   A 1 173 ? 31.83700 3.79500   13.99900 1.000 31.18005  ?  325 GLU   A CB   1 
ATOM   1248 C  CG   . GLU   A 1 173 ? 33.24100 3.75800   13.41200 1.000 34.15528  ?  325 GLU   A CG   1 
ATOM   1249 C  CD   . GLU   A 1 173 ? 34.15600 4.82900   13.98600 1.000 35.76861  ?  325 GLU   A CD   1 
ATOM   1250 O  OE1  . GLU   A 1 173 ? 35.34900 4.85300   13.61600 1.000 41.55888  ?  325 GLU   A OE1  1 
ATOM   1251 O  OE2  . GLU   A 1 173 ? 33.69300 5.64600   14.80900 1.000 33.46525  ?  325 GLU   A OE2  1 
ATOM   1252 N  N    . HIS   A 1 174 ? 28.61700 4.19300   13.85000 1.000 31.83668  ?  326 HIS   A N    1 
ATOM   1253 C  CA   . HIS   A 1 174 ? 27.31300 4.09200   14.50100 1.000 32.37356  ?  326 HIS   A CA   1 
ATOM   1254 C  C    . HIS   A 1 174 ? 26.41400 3.09000   13.78200 1.000 33.49780  ?  326 HIS   A C    1 
ATOM   1255 O  O    . HIS   A 1 174 ? 25.79400 2.22500   14.41500 1.000 31.18258  ?  326 HIS   A O    1 
ATOM   1256 C  CB   . HIS   A 1 174 ? 26.66300 5.47700   14.55100 1.000 30.50293  ?  326 HIS   A CB   1 
ATOM   1257 C  CG   . HIS   A 1 174 ? 25.33800 5.50800   15.24700 1.000 33.89741  ?  326 HIS   A CG   1 
ATOM   1258 N  ND1  . HIS   A 1 174 ? 25.20200 5.30500   16.60300 1.000 33.46542  ?  326 HIS   A ND1  1 
ATOM   1259 C  CD2  . HIS   A 1 174 ? 24.09000 5.73600   14.77400 1.000 33.23811  ?  326 HIS   A CD2  1 
ATOM   1260 C  CE1  . HIS   A 1 174 ? 23.92600 5.39800   16.93500 1.000 34.65362  ?  326 HIS   A CE1  1 
ATOM   1261 N  NE2  . HIS   A 1 174 ? 23.23000 5.66000   15.84300 1.000 32.21977  ?  326 HIS   A NE2  1 
ATOM   1262 N  N    . VAL   A 1 175 ? 26.34300 3.18000   12.45200 1.000 30.65007  ?  327 VAL   A N    1 
ATOM   1263 C  CA   . VAL   A 1 175 ? 25.45700 2.28900   11.70900 1.000 28.51093  ?  327 VAL   A CA   1 
ATOM   1264 C  C    . VAL   A 1 175 ? 26.04400 0.88500   11.60500 1.000 31.39405  ?  327 VAL   A C    1 
ATOM   1265 O  O    . VAL   A 1 175 ? 25.29500 -0.09600  11.55800 1.000 29.86440  ?  327 VAL   A O    1 
ATOM   1266 C  CB   . VAL   A 1 175 ? 25.14600 2.87700   10.32200 1.000 29.68369  ?  327 VAL   A CB   1 
ATOM   1267 C  CG1  . VAL   A 1 175 ? 24.57700 4.28000   10.46500 1.000 34.48210  ?  327 VAL   A CG1  1 
ATOM   1268 C  CG2  . VAL   A 1 175 ? 26.38500 2.89100   9.44600  1.000 28.38781  ?  327 VAL   A CG2  1 
ATOM   1269 N  N    . LEU   A 1 176 ? 27.37400 0.75400   11.57700 1.000 28.04962  ?  328 LEU   A N    1 
ATOM   1270 C  CA   . LEU   A 1 176 ? 27.97400 -0.57700  11.57600 1.000 30.86345  ?  328 LEU   A CA   1 
ATOM   1271 C  C    . LEU   A 1 176 ? 27.67500 -1.31000  12.87700 1.000 30.53672  ?  328 LEU   A C    1 
ATOM   1272 O  O    . LEU   A 1 176 ? 27.38500 -2.51300  12.87100 1.000 31.86957  ?  328 LEU   A O    1 
ATOM   1273 C  CB   . LEU   A 1 176 ? 29.48500 -0.47900  11.34900 1.000 28.52664  ?  328 LEU   A CB   1 
ATOM   1274 C  CG   . LEU   A 1 176 ? 29.93500 -0.39800  9.88900  1.000 33.45432  ?  328 LEU   A CG   1 
ATOM   1275 C  CD1  . LEU   A 1 176 ? 31.38600 0.06300   9.79300  1.000 31.36631  ?  328 LEU   A CD1  1 
ATOM   1276 C  CD2  . LEU   A 1 176 ? 29.75000 -1.74000  9.19400  1.000 35.78303  ?  328 LEU   A CD2  1 
ATOM   1277 N  N    . LEU   A 1 177 ? 27.72000 -0.59500  14.00300 1.000 30.53725  ?  329 LEU   A N    1 
ATOM   1278 C  CA   . LEU   A 1 177 ? 27.47300 -1.22100  15.29800 1.000 27.37308  ?  329 LEU   A CA   1 
ATOM   1279 C  C    . LEU   A 1 177 ? 26.03100 -1.69900  15.41800 1.000 27.27355  ?  329 LEU   A C    1 
ATOM   1280 O  O    . LEU   A 1 177 ? 25.76900 -2.77200  15.97400 1.000 28.20283  ?  329 LEU   A O    1 
ATOM   1281 C  CB   . LEU   A 1 177 ? 27.80800 -0.23900  16.41900 1.000 29.11059  ?  329 LEU   A CB   1 
ATOM   1282 C  CG   . LEU   A 1 177 ? 27.77400 -0.78100  17.84900 1.000 34.06945  ?  329 LEU   A CG   1 
ATOM   1283 C  CD1  . LEU   A 1 177 ? 28.73900 -1.94800  18.01100 1.000 32.51911  ?  329 LEU   A CD1  1 
ATOM   1284 C  CD2  . LEU   A 1 177 ? 28.09000 0.32500   18.84700 1.000 34.06516  ?  329 LEU   A CD2  1 
ATOM   1285 N  N    . MET   A 1 178 ? 25.08200 -0.91200  14.90900 1.000 27.77148  ?  330 MET   A N    1 
ATOM   1286 C  CA   . MET   A 1 178 ? 23.68700 -1.33700  14.93600 1.000 27.05202  ?  330 MET   A CA   1 
ATOM   1287 C  C    . MET   A 1 178 ? 23.48400 -2.60600  14.11600 1.000 28.73779  ?  330 MET   A C    1 
ATOM   1288 O  O    . MET   A 1 178 ? 22.75100 -3.51200  14.53000 1.000 31.37288  ?  330 MET   A O    1 
ATOM   1289 C  CB   . MET   A 1 178 ? 22.78700 -0.21300  14.42300 1.000 28.32494  ?  330 MET   A CB   1 
ATOM   1290 C  CG   . MET   A 1 178 ? 22.66500 0.96900   15.37700 1.000 31.84573  ?  330 MET   A CG   1 
ATOM   1291 S  SD   . MET   A 1 178 ? 21.33200 2.10900   14.94100 1.000 34.53466  ?  330 MET   A SD   1 
ATOM   1292 C  CE   . MET   A 1 178 ? 22.02800 2.88700   13.48300 1.000 30.76606  ?  330 MET   A CE   1 
ATOM   1293 N  N    . ALA   A 1 179 ? 24.13600 -2.69200  12.95300 1.000 26.78847  ?  331 ALA   A N    1 
ATOM   1294 C  CA   . ALA   A 1 179 ? 23.98200 -3.86400  12.09500 1.000 31.11215  ?  331 ALA   A CA   1 
ATOM   1295 C  C    . ALA   A 1 179 ? 24.59100 -5.10900  12.73100 1.000 34.59892  ?  331 ALA   A C    1 
ATOM   1296 O  O    . ALA   A 1 179 ? 24.00700 -6.19700  12.66000 1.000 35.52584  ?  331 ALA   A O    1 
ATOM   1297 C  CB   . ALA   A 1 179 ? 24.61300 -3.59800  10.73000 1.000 27.90952  ?  331 ALA   A CB   1 
ATOM   1298 N  N    . ILE   A 1 180 ? 25.76700 -4.97100  13.34800 1.000 29.62385  ?  332 ILE   A N    1 
ATOM   1299 C  CA   . ILE   A 1 180 ? 26.41100 -6.10800  13.99900 1.000 29.00808  ?  332 ILE   A CA   1 
ATOM   1300 C  C    . ILE   A 1 180 ? 25.56800 -6.60800  15.16900 1.000 30.57987  ?  332 ILE   A C    1 
ATOM   1301 O  O    . ILE   A 1 180 ? 25.44400 -7.81900  15.39200 1.000 34.95572  ?  332 ILE   A O    1 
ATOM   1302 C  CB   . ILE   A 1 180 ? 27.83200 -5.71500  14.44300 1.000 30.19456  ?  332 ILE   A CB   1 
ATOM   1303 C  CG1  . ILE   A 1 180 ? 28.72300 -5.48900  13.21900 1.000 31.75026  ?  332 ILE   A CG1  1 
ATOM   1304 C  CG2  . ILE   A 1 180 ? 28.42400 -6.77500  15.35400 1.000 34.26388  ?  332 ILE   A CG2  1 
ATOM   1305 C  CD1  . ILE   A 1 180 ? 29.96900 -4.66900  13.51700 1.000 29.22126  ?  332 ILE   A CD1  1 
ATOM   1306 N  N    . CYS   A 1 181 ? 24.99100 -5.68400  15.94200 1.000 32.25356  ?  333 CYS   A N    1 
ATOM   1307 C  CA   . CYS   A 1 181 ? 24.07700 -6.04700  17.02300 1.000 31.21894  ?  333 CYS   A CA   1 
ATOM   1308 C  C    . CYS   A 1 181 ? 22.93000 -6.92400  16.53100 1.000 35.28993  ?  333 CYS   A C    1 
ATOM   1309 O  O    . CYS   A 1 181 ? 22.56900 -7.91900  17.17500 1.000 33.97020  ?  333 CYS   A O    1 
ATOM   1310 C  CB   . CYS   A 1 181 ? 23.53200 -4.76800  17.66600 1.000 27.81851  ?  333 CYS   A CB   1 
ATOM   1311 S  SG   . CYS   A 1 181 ? 22.33600 -5.02000  18.97300 1.000 31.58281  ?  333 CYS   A SG   1 
ATOM   1312 N  N    . ILE   A 1 182 ? 22.34600 -6.56800  15.38700 1.000 32.29324  ?  334 ILE   A N    1 
ATOM   1313 C  CA   . ILE   A 1 182 ? 21.18800 -7.29500  14.87900 1.000 27.79722  ?  334 ILE   A CA   1 
ATOM   1314 C  C    . ILE   A 1 182 ? 21.57900 -8.70500  14.44800 1.000 32.47502  ?  334 ILE   A C    1 
ATOM   1315 O  O    . ILE   A 1 182 ? 20.91300 -9.68900  14.79700 1.000 31.95061  ?  334 ILE   A O    1 
ATOM   1316 C  CB   . ILE   A 1 182 ? 20.54400 -6.50800  13.72600 1.000 33.12103  ?  334 ILE   A CB   1 
ATOM   1317 C  CG1  . ILE   A 1 182 ? 19.95400 -5.19300  14.24800 1.000 30.38660  ?  334 ILE   A CG1  1 
ATOM   1318 C  CG2  . ILE   A 1 182 ? 19.48100 -7.32900  13.03000 1.000 33.99443  ?  334 ILE   A CG2  1 
ATOM   1319 C  CD1  . ILE   A 1 182 ? 19.63900 -4.18000  13.15800 1.000 31.10088  ?  334 ILE   A CD1  1 
ATOM   1320 N  N    . VAL   A 1 183 ? 22.67000 -8.82900  13.69400 1.000 32.26206  ?  335 VAL   A N    1 
ATOM   1321 C  CA   . VAL   A 1 183 ? 23.06900 -10.11800 13.14000 1.000 33.66766  ?  335 VAL   A CA   1 
ATOM   1322 C  C    . VAL   A 1 183 ? 24.05100 -10.80700 14.08000 1.000 36.79139  ?  335 VAL   A C    1 
ATOM   1323 O  O    . VAL   A 1 183 ? 25.24300 -10.91000 13.77900 1.000 42.29790  ?  335 VAL   A O    1 
ATOM   1324 C  CB   . VAL   A 1 183 ? 23.67300 -9.94800  11.73200 1.000 40.57414  ?  335 VAL   A CB   1 
ATOM   1325 C  CG1  . VAL   A 1 183 ? 23.81000 -11.29800 11.03600 1.000 42.02165  ?  335 VAL   A CG1  1 
ATOM   1326 C  CG2  . VAL   A 1 183 ? 22.81900 -9.00200  10.90100 1.000 39.33929  ?  335 VAL   A CG2  1 
ATOM   1327 N  N    . SER   A 1 184 ? 23.56000 -11.29100 15.22000 1.000 40.67013  ?  336 SER   A N    1 
ATOM   1328 C  CA   . SER   A 1 184 ? 24.40200 -11.98300 16.18500 1.000 40.27630  ?  336 SER   A CA   1 
ATOM   1329 C  C    . SER   A 1 184 ? 24.04900 -13.46000 16.22900 1.000 42.00239  ?  336 SER   A C    1 
ATOM   1330 O  O    . SER   A 1 184 ? 22.87600 -13.80200 16.42700 1.000 41.33575  ?  336 SER   A O    1 
ATOM   1331 C  CB   . SER   A 1 184 ? 24.24200 -11.36600 17.58000 1.000 41.87778  ?  336 SER   A CB   1 
ATOM   1332 O  OG   . SER   A 1 184 ? 24.48600 -9.97100  17.54800 1.000 39.75991  ?  336 SER   A OG   1 
ATOM   1333 N  N    . PRO   A 1 185 ? 25.02100 -14.36000 16.04700 1.000 36.53358  ?  337 PRO   A N    1 
ATOM   1334 C  CA   . PRO   A 1 185 ? 24.69600 -15.79100 15.93600 1.000 40.27500  ?  337 PRO   A CA   1 
ATOM   1335 C  C    . PRO   A 1 185 ? 24.37200 -16.48300 17.25100 1.000 48.85813  ?  337 PRO   A C    1 
ATOM   1336 O  O    . PRO   A 1 185 ? 23.86900 -17.61500 17.21700 1.000 56.12580  ?  337 PRO   A O    1 
ATOM   1337 C  CB   . PRO   A 1 185 ? 25.96500 -16.38700 15.30800 1.000 46.41879  ?  337 PRO   A CB   1 
ATOM   1338 C  CG   . PRO   A 1 185 ? 27.05600 -15.46000 15.72000 1.000 44.15028  ?  337 PRO   A CG   1 
ATOM   1339 C  CD   . PRO   A 1 185 ? 26.43900 -14.08800 15.75000 1.000 36.86301  ?  337 PRO   A CD   1 
ATOM   1340 N  N    . ASP   A 1 186 ? 24.62700 -15.85900 18.39800 1.000 46.38772  ?  338 ASP   A N    1 
ATOM   1341 C  CA   . ASP   A 1 186 ? 24.40200 -16.50400 19.68500 1.000 49.23448  ?  338 ASP   A CA   1 
ATOM   1342 C  C    . ASP   A 1 186 ? 23.04200 -16.17300 20.29000 1.000 45.49671  ?  338 ASP   A C    1 
ATOM   1343 O  O    . ASP   A 1 186 ? 22.80500 -16.48400 21.46200 1.000 47.36804  ?  338 ASP   A O    1 
ATOM   1344 C  CB   . ASP   A 1 186 ? 25.51900 -16.13500 20.66500 1.000 43.99356  ?  338 ASP   A CB   1 
ATOM   1345 C  CG   . ASP   A 1 186 ? 25.57600 -14.65000 20.95200 1.000 47.93414  ?  338 ASP   A CG   1 
ATOM   1346 O  OD1  . ASP   A 1 186 ? 25.88000 -14.28000 22.10600 1.000 53.73078  ?  338 ASP   A OD1  1 
ATOM   1347 O  OD2  . ASP   A 1 186 ? 25.31600 -13.85200 20.02700 1.000 45.76916  ?  338 ASP   A OD2  1 
ATOM   1348 N  N    . ARG   A 1 187 ? 22.14600 -15.56200 19.52500 1.000 44.81103  ?  339 ARG   A N    1 
ATOM   1349 C  CA   . ARG   A 1 187 ? 20.81200 -15.29200 20.03700 1.000 42.99613  ?  339 ARG   A CA   1 
ATOM   1350 C  C    . ARG   A 1 187 ? 20.04500 -16.60200 20.20600 1.000 46.01727  ?  339 ARG   A C    1 
ATOM   1351 O  O    . ARG   A 1 187 ? 20.17600 -17.50900 19.37900 1.000 42.09079  ?  339 ARG   A O    1 
ATOM   1352 C  CB   . ARG   A 1 187 ? 20.05400 -14.35900 19.09500 1.000 41.66103  ?  339 ARG   A CB   1 
ATOM   1353 C  CG   . ARG   A 1 187 ? 20.79700 -13.07700 18.74900 1.000 42.69763  ?  339 ARG   A CG   1 
ATOM   1354 C  CD   . ARG   A 1 187 ? 20.78900 -12.09800 19.90800 1.000 39.37127  ?  339 ARG   A CD   1 
ATOM   1355 N  NE   . ARG   A 1 187 ? 21.09000 -10.73900 19.47100 1.000 34.21382  ?  339 ARG   A NE   1 
ATOM   1356 C  CZ   . ARG   A 1 187 ? 21.19200 -9.69800  20.29000 1.000 32.46687  ?  339 ARG   A CZ   1 
ATOM   1357 N  NH1  . ARG   A 1 187 ? 21.01000 -9.85500  21.59500 1.000 33.74502  ?  339 ARG   A NH1  1 
ATOM   1358 N  NH2  . ARG   A 1 187 ? 21.46700 -8.49700  19.80200 1.000 32.61895  ?  339 ARG   A NH2  1 
ATOM   1359 N  N    . PRO   A 1 188 ? 19.24900 -16.73800 21.26600 1.000 56.14072  ?  340 PRO   A N    1 
ATOM   1360 C  CA   . PRO   A 1 188 ? 18.49800 -17.98500 21.46300 1.000 59.06369  ?  340 PRO   A CA   1 
ATOM   1361 C  C    . PRO   A 1 188 ? 17.44200 -18.17200 20.38600 1.000 53.46354  ?  340 PRO   A C    1 
ATOM   1362 O  O    . PRO   A 1 188 ? 16.72500 -17.23700 20.02100 1.000 49.56388  ?  340 PRO   A O    1 
ATOM   1363 C  CB   . PRO   A 1 188 ? 17.86200 -17.80200 22.84600 1.000 61.61933  ?  340 PRO   A CB   1 
ATOM   1364 C  CG   . PRO   A 1 188 ? 17.78800 -16.32100 23.03000 1.000 61.33107  ?  340 PRO   A CG   1 
ATOM   1365 C  CD   . PRO   A 1 188 ? 19.01700 -15.77700 22.35700 1.000 60.98768  ?  340 PRO   A CD   1 
ATOM   1366 N  N    . GLY   A 1 189 ? 17.35500 -19.39800 19.87400 1.000 55.44852  ?  341 GLY   A N    1 
ATOM   1367 C  CA   . GLY   A 1 189 ? 16.40600 -19.73100 18.83500 1.000 55.32796  ?  341 GLY   A CA   1 
ATOM   1368 C  C    . GLY   A 1 189 ? 16.93500 -19.64400 17.42100 1.000 52.21686  ?  341 GLY   A C    1 
ATOM   1369 O  O    . GLY   A 1 189 ? 16.17700 -19.90600 16.47800 1.000 51.09849  ?  341 GLY   A O    1 
ATOM   1370 N  N    . VAL   A 1 190 ? 18.20600 -19.28500 17.23800 1.000 48.34534  ?  342 VAL   A N    1 
ATOM   1371 C  CA   . VAL   A 1 190 ? 18.77800 -19.19200 15.90000 1.000 46.72139  ?  342 VAL   A CA   1 
ATOM   1372 C  C    . VAL   A 1 190 ? 18.94100 -20.58900 15.31500 1.000 50.06942  ?  342 VAL   A C    1 
ATOM   1373 O  O    . VAL   A 1 190 ? 19.47000 -21.49800 15.96900 1.000 53.80533  ?  342 VAL   A O    1 
ATOM   1374 C  CB   . VAL   A 1 190 ? 20.11800 -18.44000 15.93700 1.000 46.82671  ?  342 VAL   A CB   1 
ATOM   1375 C  CG1  . VAL   A 1 190 ? 20.82600 -18.54600 14.59800 1.000 48.94133  ?  342 VAL   A CG1  1 
ATOM   1376 C  CG2  . VAL   A 1 190 ? 19.89100 -16.97900 16.28800 1.000 46.62014  ?  342 VAL   A CG2  1 
ATOM   1377 N  N    A GLN   A 1 191 ? 18.49800 -20.76900 14.07200 0.520 52.14243  ?  343 GLN   A N    1 
ATOM   1378 N  N    B GLN   A 1 191 ? 18.46000 -20.76600 14.08400 0.480 52.08555  ?  343 GLN   A N    1 
ATOM   1379 C  CA   A GLN   A 1 191 ? 18.64300 -22.06100 13.40800 0.520 55.22157  ?  343 GLN   A CA   1 
ATOM   1380 C  CA   B GLN   A 1 191 ? 18.61000 -22.03400 13.37200 0.480 55.20807  ?  343 GLN   A CA   1 
ATOM   1381 C  C    A GLN   A 1 191 ? 19.98100 -22.16900 12.67900 0.520 57.76020  ?  343 GLN   A C    1 
ATOM   1382 C  C    B GLN   A 1 191 ? 19.98600 -22.12100 12.71900 0.480 57.54850  ?  343 GLN   A C    1 
ATOM   1383 O  O    A GLN   A 1 191 ? 20.80600 -23.02800 13.00700 0.520 59.49972  ?  343 GLN   A O    1 
ATOM   1384 O  O    B GLN   A 1 191 ? 20.84100 -22.90900 13.13600 0.480 59.22225  ?  343 GLN   A O    1 
ATOM   1385 C  CB   A GLN   A 1 191 ? 17.47900 -22.29200 12.43800 0.520 55.48091  ?  343 GLN   A CB   1 
ATOM   1386 C  CB   B GLN   A 1 191 ? 17.50800 -22.17500 12.31600 0.480 55.18206  ?  343 GLN   A CB   1 
ATOM   1387 C  CG   A GLN   A 1 191 ? 17.34300 -23.73600 11.98300 0.520 57.47760  ?  343 GLN   A CG   1 
ATOM   1388 C  CG   B GLN   A 1 191 ? 16.25700 -22.89900 12.77400 0.480 54.10401  ?  343 GLN   A CG   1 
ATOM   1389 C  CD   A GLN   A 1 191 ? 17.83400 -23.94500 10.56600 0.520 60.44104  ?  343 GLN   A CD   1 
ATOM   1390 C  CD   B GLN   A 1 191 ? 15.01100 -22.39400 12.06600 0.480 51.24839  ?  343 GLN   A CD   1 
ATOM   1391 O  OE1  A GLN   A 1 191 ? 17.22700 -23.46400 9.61000  0.520 59.83294  ?  343 GLN   A OE1  1 
ATOM   1392 O  OE1  B GLN   A 1 191 ? 15.04600 -22.06900 10.87900 0.480 48.26757  ?  343 GLN   A OE1  1 
ATOM   1393 N  NE2  A GLN   A 1 191 ? 18.94500 -24.66100 10.42300 0.520 60.30283  ?  343 GLN   A NE2  1 
ATOM   1394 N  NE2  B GLN   A 1 191 ? 13.90100 -22.33100 12.79300 0.480 47.39556  ?  343 GLN   A NE2  1 
ATOM   1395 N  N    . ASP   A 1 192 ? 20.20800 -21.30400 11.69100 1.000 56.38502  ?  344 ASP   A N    1 
ATOM   1396 C  CA   . ASP   A 1 192 ? 21.44100 -21.33600 10.90300 1.000 56.15033  ?  344 ASP   A CA   1 
ATOM   1397 C  C    . ASP   A 1 192 ? 22.45200 -20.35200 11.49600 1.000 57.70406  ?  344 ASP   A C    1 
ATOM   1398 O  O    . ASP   A 1 192 ? 22.77200 -19.30700 10.92700 1.000 54.96028  ?  344 ASP   A O    1 
ATOM   1399 C  CB   . ASP   A 1 192 ? 21.13300 -21.02400 9.44400  1.000 56.37099  ?  344 ASP   A CB   1 
ATOM   1400 C  CG   . ASP   A 1 192 ? 22.24900 -21.43500 8.50600  1.000 62.59165  ?  344 ASP   A CG   1 
ATOM   1401 O  OD1  . ASP   A 1 192 ? 22.03200 -21.39000 7.27700  1.000 61.76277  ?  344 ASP   A OD1  1 
ATOM   1402 O  OD2  . ASP   A 1 192 ? 23.34100 -21.80200 8.99200  1.000 63.85006  ?  344 ASP   A OD2  1 
ATOM   1403 N  N    . ALA   A 1 193 ? 22.96100 -20.72000 12.67600 1.000 56.82304  ?  345 ALA   A N    1 
ATOM   1404 C  CA   . ALA   A 1 193 ? 23.93300 -19.87300 13.36200 1.000 57.65932  ?  345 ALA   A CA   1 
ATOM   1405 C  C    . ALA   A 1 193 ? 25.20000 -19.69400 12.53900 1.000 58.87504  ?  345 ALA   A C    1 
ATOM   1406 O  O    . ALA   A 1 193 ? 25.89200 -18.67900 12.67500 1.000 55.53797  ?  345 ALA   A O    1 
ATOM   1407 C  CB   . ALA   A 1 193 ? 24.26900 -20.46000 14.73300 1.000 58.51698  ?  345 ALA   A CB   1 
ATOM   1408 N  N    . LYS   A 1 194 ? 25.51400 -20.66400 11.67900 1.000 63.85064  ?  346 LYS   A N    1 
ATOM   1409 C  CA   . LYS   A 1 194 ? 26.71400 -20.57100 10.85500 1.000 63.18420  ?  346 LYS   A CA   1 
ATOM   1410 C  C    . LYS   A 1 194 ? 26.56500 -19.47800 9.80300  1.000 58.99728  ?  346 LYS   A C    1 
ATOM   1411 O  O    . LYS   A 1 194 ? 27.52800 -18.76800 9.49500  1.000 57.85906  ?  346 LYS   A O    1 
ATOM   1412 C  CB   . LYS   A 1 194 ? 27.01000 -21.92000 10.18500 1.000 72.07815  ?  346 LYS   A CB   1 
ATOM   1413 C  CG   . LYS   A 1 194 ? 27.48500 -23.07600 11.09600 1.000 76.60288  ?  346 LYS   A CG   1 
ATOM   1414 C  CD   . LYS   A 1 194 ? 26.53300 -23.39400 12.24500 1.000 79.04228  ?  346 LYS   A CD   1 
ATOM   1415 C  CE   . LYS   A 1 194 ? 25.21300 -23.94600 11.74000 1.000 80.27609  ?  346 LYS   A CE   1 
ATOM   1416 N  NZ   . LYS   A 1 194 ? 24.14400 -23.89300 12.77300 1.000 76.78828  ?  346 LYS   A NZ   1 
ATOM   1417 N  N    . LEU   A 1 195 ? 25.36200 -19.32900 9.24300  1.000 56.11391  ?  347 LEU   A N    1 
ATOM   1418 C  CA   . LEU   A 1 195 ? 25.12400 -18.27800 8.26000  1.000 54.45059  ?  347 LEU   A CA   1 
ATOM   1419 C  C    . LEU   A 1 195 ? 25.06700 -16.90600 8.92100  1.000 47.32289  ?  347 LEU   A C    1 
ATOM   1420 O  O    . LEU   A 1 195 ? 25.55100 -15.91800 8.35400  1.000 50.95105  ?  347 LEU   A O    1 
ATOM   1421 C  CB   . LEU   A 1 195 ? 23.82900 -18.56300 7.49900  1.000 55.36116  ?  347 LEU   A CB   1 
ATOM   1422 C  CG   . LEU   A 1 195 ? 23.40100 -17.56100 6.42600  1.000 53.76469  ?  347 LEU   A CG   1 
ATOM   1423 C  CD1  . LEU   A 1 195 ? 24.50200 -17.37100 5.39900  1.000 53.13249  ?  347 LEU   A CD1  1 
ATOM   1424 C  CD2  . LEU   A 1 195 ? 22.11400 -18.02200 5.75900  1.000 56.23568  ?  347 LEU   A CD2  1 
ATOM   1425 N  N    . VAL   A 1 196 ? 24.47000 -16.82200 10.11300 1.000 44.62808  ?  348 VAL   A N    1 
ATOM   1426 C  CA   . VAL   A 1 196 ? 24.41800 -15.55300 10.83400 1.000 39.40126  ?  348 VAL   A CA   1 
ATOM   1427 C  C    . VAL   A 1 196 ? 25.82600 -15.07400 11.16400 1.000 39.35528  ?  348 VAL   A C    1 
ATOM   1428 O  O    . VAL   A 1 196 ? 26.13200 -13.87900 11.06300 1.000 41.93908  ?  348 VAL   A O    1 
ATOM   1429 C  CB   . VAL   A 1 196 ? 23.55700 -15.69500 12.10200 1.000 38.14510  ?  348 VAL   A CB   1 
ATOM   1430 C  CG1  . VAL   A 1 196 ? 23.49200 -14.37700 12.85100 1.000 40.21605  ?  348 VAL   A CG1  1 
ATOM   1431 C  CG2  . VAL   A 1 196 ? 22.15400 -16.17500 11.74700 1.000 38.64432  ?  348 VAL   A CG2  1 
ATOM   1432 N  N    . GLU   A 1 197 ? 26.70700 -15.99900 11.55300 1.000 41.38670  ?  349 GLU   A N    1 
ATOM   1433 C  CA   . GLU   A 1 197 ? 28.08000 -15.62400 11.87500 1.000 43.20200  ?  349 GLU   A CA   1 
ATOM   1434 C  C    . GLU   A 1 197 ? 28.82000 -15.11900 10.64300 1.000 47.06977  ?  349 GLU   A C    1 
ATOM   1435 O  O    . GLU   A 1 197 ? 29.57700 -14.14500 10.72000 1.000 44.81500  ?  349 GLU   A O    1 
ATOM   1436 C  CB   . GLU   A 1 197 ? 28.81700 -16.81200 12.49200 1.000 50.67619  ?  349 GLU   A CB   1 
ATOM   1437 C  CG   . GLU   A 1 197 ? 30.18400 -16.46500 13.06000 1.000 56.18233  ?  349 GLU   A CG   1 
ATOM   1438 C  CD   . GLU   A 1 197 ? 30.74500 -17.56200 13.94500 1.000 68.68013  ?  349 GLU   A CD   1 
ATOM   1439 O  OE1  . GLU   A 1 197 ? 30.52300 -18.75100 13.63300 1.000 73.89475  ?  349 GLU   A OE1  1 
ATOM   1440 O  OE2  . GLU   A 1 197 ? 31.41200 -17.23600 14.95000 1.000 70.79979  ?  349 GLU   A OE2  1 
ATOM   1441 N  N    . ALA   A 1 198 ? 28.61300 -15.77000 9.49500  1.000 50.09048  ?  350 ALA   A N    1 
ATOM   1442 C  CA   . ALA   A 1 198 ? 29.28200 -15.34100 8.27100  1.000 52.13864  ?  350 ALA   A CA   1 
ATOM   1443 C  C    . ALA   A 1 198 ? 28.86000 -13.93200 7.87400  1.000 50.90095  ?  350 ALA   A C    1 
ATOM   1444 O  O    . ALA   A 1 198 ? 29.68400 -13.13800 7.40500  1.000 48.72277  ?  350 ALA   A O    1 
ATOM   1445 C  CB   . ALA   A 1 198 ? 28.99200 -16.32800 7.14200  1.000 55.56600  ?  350 ALA   A CB   1 
ATOM   1446 N  N    . ILE   A 1 199 ? 27.58100 -13.60000 8.05700  1.000 47.87171  ?  351 ILE   A N    1 
ATOM   1447 C  CA   . ILE   A 1 199 ? 27.10600 -12.26100 7.72300  1.000 46.64213  ?  351 ILE   A CA   1 
ATOM   1448 C  C    . ILE   A 1 199 ? 27.68800 -11.23300 8.68800  1.000 43.31413  ?  351 ILE   A C    1 
ATOM   1449 O  O    . ILE   A 1 199 ? 28.14400 -10.16000 8.27600  1.000 42.78945  ?  351 ILE   A O    1 
ATOM   1450 C  CB   . ILE   A 1 199 ? 25.56800 -12.22600 7.71500  1.000 44.80448  ?  351 ILE   A CB   1 
ATOM   1451 C  CG1  . ILE   A 1 199 ? 25.02800 -13.05500 6.54900  1.000 50.25529  ?  351 ILE   A CG1  1 
ATOM   1452 C  CG2  . ILE   A 1 199 ? 25.06500 -10.79300 7.63300  1.000 44.33860  ?  351 ILE   A CG2  1 
ATOM   1453 C  CD1  . ILE   A 1 199 ? 23.65900 -13.64300 6.80600  1.000 51.15300  ?  351 ILE   A CD1  1 
ATOM   1454 N  N    . GLN   A 1 200 ? 27.68000 -11.54400 9.98700  1.000 44.37913  ?  352 GLN   A N    1 
ATOM   1455 C  CA   . GLN   A 1 200 ? 28.25400 -10.62500 10.96600 1.000 42.35314  ?  352 GLN   A CA   1 
ATOM   1456 C  C    . GLN   A 1 200 ? 29.74800 -10.43900 10.74000 1.000 42.66880  ?  352 GLN   A C    1 
ATOM   1457 O  O    . GLN   A 1 200 ? 30.28100 -9.34100  10.94100 1.000 44.10525  ?  352 GLN   A O    1 
ATOM   1458 C  CB   . GLN   A 1 200 ? 27.99800 -11.13200 12.38300 1.000 43.81475  ?  352 GLN   A CB   1 
ATOM   1459 C  CG   . GLN   A 1 200 ? 28.23500 -10.08300 13.45900 1.000 43.84532  ?  352 GLN   A CG   1 
ATOM   1460 C  CD   . GLN   A 1 200 ? 28.16300 -10.65400 14.86200 1.000 42.32643  ?  352 GLN   A CD   1 
ATOM   1461 O  OE1  . GLN   A 1 200 ? 27.40400 -10.16900 15.70200 1.000 39.39979  ?  352 GLN   A OE1  1 
ATOM   1462 N  NE2  . GLN   A 1 200 ? 28.96100 -11.68300 15.12500 1.000 46.00729  ?  352 GLN   A NE2  1 
ATOM   1463 N  N    . ASP   A 1 201 ? 30.44200 -11.50400 10.32900 1.000 45.03999  ?  353 ASP   A N    1 
ATOM   1464 C  CA   . ASP   A 1 201 ? 31.88300 -11.41300 10.11400 1.000 50.04585  ?  353 ASP   A CA   1 
ATOM   1465 C  C    . ASP   A 1 201 ? 32.21400 -10.41700 9.01100  1.000 51.09270  ?  353 ASP   A C    1 
ATOM   1466 O  O    . ASP   A 1 201 ? 33.17700 -9.64900  9.12600  1.000 51.61293  ?  353 ASP   A O    1 
ATOM   1467 C  CB   . ASP   A 1 201 ? 32.45300 -12.79100 9.77900  1.000 52.32386  ?  353 ASP   A CB   1 
ATOM   1468 C  CG   . ASP   A 1 201 ? 32.60800 -13.67000 11.00300 1.000 52.76718  ?  353 ASP   A CG   1 
ATOM   1469 O  OD1  . ASP   A 1 201 ? 32.38900 -13.17200 12.12700 1.000 52.65436  ?  353 ASP   A OD1  1 
ATOM   1470 O  OD2  . ASP   A 1 201 ? 32.94900 -14.86000 10.83900 1.000 57.73306  ?  353 ASP   A OD2  1 
ATOM   1471 N  N    . ARG   A 1 202 ? 31.43200 -10.42200 7.92900  1.000 46.31279  ?  354 ARG   A N    1 
ATOM   1472 C  CA   . ARG   A 1 202 ? 31.60400 -9.41700  6.88500  1.000 49.87521  ?  354 ARG   A CA   1 
ATOM   1473 C  C    . ARG   A 1 202 ? 31.44900 -8.01200  7.45200  1.000 45.38558  ?  354 ARG   A C    1 
ATOM   1474 O  O    . ARG   A 1 202 ? 32.16800 -7.08800  7.05200  1.000 46.61240  ?  354 ARG   A O    1 
ATOM   1475 C  CB   . ARG   A 1 202 ? 30.59900 -9.65800  5.75800  1.000 55.13673  ?  354 ARG   A CB   1 
ATOM   1476 C  CG   . ARG   A 1 202 ? 30.89700 -8.91000  4.46700  1.000 58.93284  ?  354 ARG   A CG   1 
ATOM   1477 C  CD   . ARG   A 1 202 ? 30.42200 -9.69400  3.24600  1.000 65.51384  ?  354 ARG   A CD   1 
ATOM   1478 N  NE   . ARG   A 1 202 ? 29.15100 -10.37800 3.47900  1.000 75.50922  ?  354 ARG   A NE   1 
ATOM   1479 C  CZ   . ARG   A 1 202 ? 27.98200 -9.98200  2.98200  1.000 79.29766  ?  354 ARG   A CZ   1 
ATOM   1480 N  NH1  . ARG   A 1 202 ? 26.87800 -10.66700 3.24700  1.000 73.82295  ?  354 ARG   A NH1  1 
ATOM   1481 N  NH2  . ARG   A 1 202 ? 27.91400 -8.89900  2.21800  1.000 83.26057  ?  354 ARG   A NH2  1 
ATOM   1482 N  N    . LEU   A 1 203 ? 30.52200 -7.83600  8.39900  1.000 38.41161  ?  355 LEU   A N    1 
ATOM   1483 C  CA   . LEU   A 1 203 ? 30.31700 -6.52500  9.00600  1.000 36.99375  ?  355 LEU   A CA   1 
ATOM   1484 C  C    . LEU   A 1 203 ? 31.41900 -6.19700  10.00600 1.000 37.87556  ?  355 LEU   A C    1 
ATOM   1485 O  O    . LEU   A 1 203 ? 31.89900 -5.05900  10.05500 1.000 39.45211  ?  355 LEU   A O    1 
ATOM   1486 C  CB   . LEU   A 1 203 ? 28.95200 -6.47100  9.69000  1.000 35.25874  ?  355 LEU   A CB   1 
ATOM   1487 C  CG   . LEU   A 1 203 ? 27.72600 -6.75700  8.82400  1.000 34.53125  ?  355 LEU   A CG   1 
ATOM   1488 C  CD1  . LEU   A 1 203 ? 26.51000 -6.97000  9.70400  1.000 33.06965  ?  355 LEU   A CD1  1 
ATOM   1489 C  CD2  . LEU   A 1 203 ? 27.49000 -5.62100  7.84600  1.000 40.73982  ?  355 LEU   A CD2  1 
ATOM   1490 N  N    . SER   A 1 204 ? 31.82300 -7.17800  10.82000 1.000 37.40534  ?  356 SER   A N    1 
ATOM   1491 C  CA   . SER   A 1 204 ? 32.85300 -6.93200  11.82500 1.000 44.72179  ?  356 SER   A CA   1 
ATOM   1492 C  C    . SER   A 1 204 ? 34.18600 -6.58400  11.17500 1.000 46.28176  ?  356 SER   A C    1 
ATOM   1493 O  O    . SER   A 1 204 ? 34.88400 -5.66900  11.62500 1.000 42.41214  ?  356 SER   A O    1 
ATOM   1494 C  CB   . SER   A 1 204 ? 32.99900 -8.15200  12.73500 1.000 43.86534  ?  356 SER   A CB   1 
ATOM   1495 O  OG   . SER   A 1 204 ? 31.78000 -8.43200  13.40500 1.000 44.61933  ?  356 SER   A OG   1 
ATOM   1496 N  N    . ASN   A 1 205 ? 34.55300 -7.29900  10.10800 1.000 49.75215  ?  357 ASN   A N    1 
ATOM   1497 C  CA   . ASN   A 1 205 ? 35.79100 -6.98400  9.40300  1.000 50.28594  ?  357 ASN   A CA   1 
ATOM   1498 C  C    . ASN   A 1 205 ? 35.70700 -5.62000  8.72900  1.000 49.40232  ?  357 ASN   A C    1 
ATOM   1499 O  O    . ASN   A 1 205 ? 36.70900 -4.90000  8.64700  1.000 51.81633  ?  357 ASN   A O    1 
ATOM   1500 C  CB   . ASN   A 1 205 ? 36.10300 -8.07200  8.37700  1.000 53.31628  ?  357 ASN   A CB   1 
ATOM   1501 C  CG   . ASN   A 1 205 ? 36.50800 -9.38200  9.02400  1.000 58.70629  ?  357 ASN   A CG   1 
ATOM   1502 O  OD1  . ASN   A 1 205 ? 36.26700 -10.45700 8.47600  1.000 62.81224  ?  357 ASN   A OD1  1 
ATOM   1503 N  ND2  . ASN   A 1 205 ? 37.12800 -9.29800  10.19500 1.000 60.61200  ?  357 ASN   A ND2  1 
ATOM   1504 N  N    . THR   A 1 206 ? 34.52200 -5.25000  8.24000  1.000 47.93530  ?  358 THR   A N    1 
ATOM   1505 C  CA   . THR   A 1 206 ? 34.33500 -3.91900  7.66900  1.000 48.21850  ?  358 THR   A CA   1 
ATOM   1506 C  C    . THR   A 1 206 ? 34.56400 -2.83800  8.71800  1.000 46.49519  ?  358 THR   A C    1 
ATOM   1507 O  O    . THR   A 1 206 ? 35.22900 -1.82900  8.45500  1.000 43.80327  ?  358 THR   A O    1 
ATOM   1508 C  CB   . THR   A 1 206 ? 32.93200 -3.79700  7.07100  1.000 44.18353  ?  358 THR   A CB   1 
ATOM   1509 O  OG1  . THR   A 1 206 ? 32.72800 -4.83300  6.10200  1.000 46.85314  ?  358 THR   A OG1  1 
ATOM   1510 C  CG2  . THR   A 1 206 ? 32.75100 -2.44000  6.40700  1.000 44.35476  ?  358 THR   A CG2  1 
ATOM   1511 N  N    . LEU   A 1 207 ? 34.01100 -3.03100  9.91800  1.000 37.39083  ?  359 LEU   A N    1 
ATOM   1512 C  CA   . LEU   A 1 207 ? 34.20200 -2.06400  10.99300 1.000 33.77970  ?  359 LEU   A CA   1 
ATOM   1513 C  C    . LEU   A 1 207 ? 35.66100 -2.01100  11.43400 1.000 36.39914  ?  359 LEU   A C    1 
ATOM   1514 O  O    . LEU   A 1 207 ? 36.23900 -0.92600  11.57500 1.000 38.57743  ?  359 LEU   A O    1 
ATOM   1515 C  CB   . LEU   A 1 207 ? 33.29500 -2.41500  12.17200 1.000 34.25788  ?  359 LEU   A CB   1 
ATOM   1516 C  CG   . LEU   A 1 207 ? 33.46200 -1.58300  13.44500 1.000 36.22208  ?  359 LEU   A CG   1 
ATOM   1517 C  CD1  . LEU   A 1 207 ? 33.25900 -0.10100  13.16300 1.000 32.23308  ?  359 LEU   A CD1  1 
ATOM   1518 C  CD2  . LEU   A 1 207 ? 32.50500 -2.07000  14.52500 1.000 35.63335  ?  359 LEU   A CD2  1 
ATOM   1519 N  N    . GLN   A 1 208 ? 36.27200 -3.17800  11.65700 1.000 38.45807  ?  360 GLN   A N    1 
ATOM   1520 C  CA   . GLN   A 1 208 ? 37.66100 -3.21300  12.10600 1.000 38.08595  ?  360 GLN   A CA   1 
ATOM   1521 C  C    . GLN   A 1 208 ? 38.58400 -2.53700  11.10200 1.000 43.57745  ?  360 GLN   A C    1 
ATOM   1522 O  O    . GLN   A 1 208 ? 39.50000 -1.80200  11.48600 1.000 45.48542  ?  360 GLN   A O    1 
ATOM   1523 C  CB   . GLN   A 1 208 ? 38.10000 -4.65700  12.34800 1.000 48.49976  ?  360 GLN   A CB   1 
ATOM   1524 C  CG   . GLN   A 1 208 ? 37.42900 -5.31700  13.53900 1.000 50.70521  ?  360 GLN   A CG   1 
ATOM   1525 C  CD   . GLN   A 1 208 ? 37.84800 -6.76200  13.71800 1.000 62.50739  ?  360 GLN   A CD   1 
ATOM   1526 O  OE1  . GLN   A 1 208 ? 37.13700 -7.68000  13.31000 1.000 69.55707  ?  360 GLN   A OE1  1 
ATOM   1527 N  NE2  . GLN   A 1 208 ? 39.00600 -6.97300  14.33500 1.000 64.53810  ?  360 GLN   A NE2  1 
ATOM   1528 N  N    . THR   A 1 209 ? 38.35300 -2.76600  9.80800  1.000 45.14586  ?  361 THR   A N    1 
ATOM   1529 C  CA   . THR   A 1 209 ? 39.17800 -2.12200  8.79200  1.000 46.85424  ?  361 THR   A CA   1 
ATOM   1530 C  C    . THR   A 1 209 ? 38.86700 -0.63300  8.68800  1.000 46.53593  ?  361 THR   A C    1 
ATOM   1531 O  O    . THR   A 1 209 ? 39.77000 0.17800   8.45100  1.000 49.75126  ?  361 THR   A O    1 
ATOM   1532 C  CB   . THR   A 1 209 ? 38.98500 -2.81800  7.44200  1.000 54.29193  ?  361 THR   A CB   1 
ATOM   1533 O  OG1  . THR   A 1 209 ? 39.41300 -4.18200  7.54200  1.000 55.37695  ?  361 THR   A OG1  1 
ATOM   1534 C  CG2  . THR   A 1 209 ? 39.78800 -2.12400  6.35200  1.000 55.89108  ?  361 THR   A CG2  1 
ATOM   1535 N  N    . TYR   A 1 210 ? 37.59700 -0.24900  8.87100  1.000 44.89487  ?  362 TYR   A N    1 
ATOM   1536 C  CA   . TYR   A 1 210 ? 37.24800 1.16700   8.79800  1.000 39.28873  ?  362 TYR   A CA   1 
ATOM   1537 C  C    . TYR   A 1 210 ? 37.96900 1.96600   9.87400  1.000 41.08258  ?  362 TYR   A C    1 
ATOM   1538 O  O    . TYR   A 1 210 ? 38.45700 3.07300   9.61400  1.000 45.13384  ?  362 TYR   A O    1 
ATOM   1539 C  CB   . TYR   A 1 210 ? 35.73400 1.36600   8.93000  1.000 40.73562  ?  362 TYR   A CB   1 
ATOM   1540 C  CG   . TYR   A 1 210 ? 35.36000 2.83400   8.96500  1.000 40.49605  ?  362 TYR   A CG   1 
ATOM   1541 C  CD1  . TYR   A 1 210 ? 35.25400 3.52100   10.17000 1.000 39.84893  ?  362 TYR   A CD1  1 
ATOM   1542 C  CD2  . TYR   A 1 210 ? 35.15400 3.54200   7.78900  1.000 41.02856  ?  362 TYR   A CD2  1 
ATOM   1543 C  CE1  . TYR   A 1 210 ? 34.93800 4.86500   10.20000 1.000 39.97126  ?  362 TYR   A CE1  1 
ATOM   1544 C  CE2  . TYR   A 1 210 ? 34.83400 4.88600   7.81000  1.000 37.84311  ?  362 TYR   A CE2  1 
ATOM   1545 C  CZ   . TYR   A 1 210 ? 34.72700 5.54300   9.01700  1.000 40.76011  ?  362 TYR   A CZ   1 
ATOM   1546 O  OH   . TYR   A 1 210 ? 34.41100 6.88200   9.04100  1.000 41.45689  ?  362 TYR   A OH   1 
ATOM   1547 N  N    . ILE   A 1 211 ? 38.02500 1.43200   11.09400 1.000 40.70897  ?  363 ILE   A N    1 
ATOM   1548 C  CA   . ILE   A 1 211 ? 38.69100 2.14300   12.17800 1.000 37.93057  ?  363 ILE   A CA   1 
ATOM   1549 C  C    . ILE   A 1 211 ? 40.17500 2.29300   11.87600 1.000 40.07640  ?  363 ILE   A C    1 
ATOM   1550 O  O    . ILE   A 1 211 ? 40.76700 3.35200   12.11900 1.000 46.44548  ?  363 ILE   A O    1 
ATOM   1551 C  CB   . ILE   A 1 211 ? 38.45000 1.41900   13.51400 1.000 36.42121  ?  363 ILE   A CB   1 
ATOM   1552 C  CG1  . ILE   A 1 211 ? 36.96600 1.49300   13.88300 1.000 34.34677  ?  363 ILE   A CG1  1 
ATOM   1553 C  CG2  . ILE   A 1 211 ? 39.29400 2.03700   14.62300 1.000 45.58619  ?  363 ILE   A CG2  1 
ATOM   1554 C  CD1  . ILE   A 1 211 ? 36.54300 0.50700   14.95700 1.000 35.97532  ?  363 ILE   A CD1  1 
ATOM   1555 N  N    . ARG   A 1 212 ? 40.76900 1.25000   11.28400 1.000 46.25825  ?  364 ARG   A N    1 
ATOM   1556 C  CA   . ARG   A 1 212 ? 42.23300 1.21100   11.00300 1.000 49.50952  ?  364 ARG   A CA   1 
ATOM   1557 C  C    . ARG   A 1 212 ? 42.63500 2.02600   9.76200  1.000 53.77114  ?  364 ARG   A C    1 
ATOM   1558 O  O    . ARG   A 1 212 ? 43.82800 2.37700   9.67400  1.000 59.30665  ?  364 ARG   A O    1 
ATOM   1559 C  CB   . ARG   A 1 212 ? 42.70500 -0.24100  10.86400 1.000 59.25941  ?  364 ARG   A CB   1 
ATOM   1560 C  CG   . ARG   A 1 212 ? 42.53100 -1.07400  12.12600 1.000 72.92972  ?  364 ARG   A CG   1 
ATOM   1561 C  CD   . ARG   A 1 212 ? 43.77000 -1.88500  12.45700 1.000 81.74786  ?  364 ARG   A CD   1 
ATOM   1562 N  NE   . ARG   A 1 212 ? 43.87400 -2.18200  13.87800 1.000 88.93631  ?  364 ARG   A NE   1 
ATOM   1563 C  CZ   . ARG   A 1 212 ? 43.61200 -3.36500  14.42100 1.000 90.25347  ?  364 ARG   A CZ   1 
ATOM   1564 N  NH1  . ARG   A 1 212 ? 43.22500 -4.37200  13.65800 1.000 89.72358  ?  364 ARG   A NH1  1 
ATOM   1565 N  NH2  . ARG   A 1 212 ? 43.73600 -3.53700  15.72500 1.000 89.67079  ?  364 ARG   A NH2  1 
ATOM   1566 N  N    A CYS   A 1 213 ? 41.65800 2.56200   9.02800  0.600 55.38734  ?  365 CYS   A N    1 
ATOM   1567 N  N    B CYS   A 1 213 ? 41.64500 2.56700   9.03900  0.400 55.64194  ?  365 CYS   A N    1 
ATOM   1568 C  CA   A CYS   A 1 213 ? 41.95600 3.36400   7.85000  0.600 59.28853  ?  365 CYS   A CA   1 
ATOM   1569 C  CA   B CYS   A 1 213 ? 41.91700 3.33200   7.83100  0.400 59.24025  ?  365 CYS   A CA   1 
ATOM   1570 C  C    A CYS   A 1 213 ? 41.39000 4.77300   7.89200  0.600 58.57223  ?  365 CYS   A C    1 
ATOM   1571 C  C    B CYS   A 1 213 ? 41.35100 4.74400   7.84600  0.400 58.36994  ?  365 CYS   A C    1 
ATOM   1572 O  O    A CYS   A 1 213 ? 41.96800 5.67000   7.27600  0.600 60.40159  ?  365 CYS   A O    1 
ATOM   1573 O  O    B CYS   A 1 213 ? 41.90000 5.61900   7.17300  0.400 60.98472  ?  365 CYS   A O    1 
ATOM   1574 C  CB   A CYS   A 1 213 ? 41.43600 2.66200   6.59000  0.600 61.72463  ?  365 CYS   A CB   1 
ATOM   1575 C  CB   B CYS   A 1 213 ? 41.36400 2.58200   6.61000  0.400 61.39004  ?  365 CYS   A CB   1 
ATOM   1576 S  SG   A CYS   A 1 213 ? 42.37600 1.19400   6.13900  0.600 64.60920  ?  365 CYS   A SG   1 
ATOM   1577 S  SG   B CYS   A 1 213 ? 41.49700 3.44800   5.03400  0.400 66.46795  ?  365 CYS   A SG   1 
ATOM   1578 N  N    . ARG   A 1 214 ? 40.28200 4.99600   8.60000  1.000 52.45060  ?  366 ARG   A N    1 
ATOM   1579 C  CA   . ARG   A 1 214 ? 39.61000 6.28700   8.56600  1.000 52.65306  ?  366 ARG   A CA   1 
ATOM   1580 C  C    . ARG   A 1 214 ? 39.46100 6.98000   9.91300  1.000 50.48732  ?  366 ARG   A C    1 
ATOM   1581 O  O    . ARG   A 1 214 ? 39.17500 8.18300   9.92600  1.000 54.35647  ?  366 ARG   A O    1 
ATOM   1582 C  CB   . ARG   A 1 214 ? 38.21500 6.14200   7.93600  1.000 47.99597  ?  366 ARG   A CB   1 
ATOM   1583 C  CG   . ARG   A 1 214 ? 38.23000 5.52900   6.54700  1.000 54.58094  ?  366 ARG   A CG   1 
ATOM   1584 C  CD   . ARG   A 1 214 ? 38.56500 6.56700   5.49000  1.000 62.89934  ?  366 ARG   A CD   1 
ATOM   1585 N  NE   . ARG   A 1 214 ? 39.01500 5.95400   4.24400  1.000 75.28705  ?  366 ARG   A NE   1 
ATOM   1586 C  CZ   . ARG   A 1 214 ? 38.20500 5.60300   3.25100  1.000 79.54369  ?  366 ARG   A CZ   1 
ATOM   1587 N  NH1  . ARG   A 1 214 ? 36.89700 5.79900   3.35900  1.000 78.99867  ?  366 ARG   A NH1  1 
ATOM   1588 N  NH2  . ARG   A 1 214 ? 38.70100 5.05300   2.15000  1.000 81.55685  ?  366 ARG   A NH2  1 
ATOM   1589 N  N    . HIS   A 1 215 ? 39.62900 6.28400   11.03500 1.000 42.21429  ?  367 HIS   A N    1 
ATOM   1590 C  CA   . HIS   A 1 215 ? 39.50100 6.94100   12.32600 1.000 39.74644  ?  367 HIS   A CA   1 
ATOM   1591 C  C    . HIS   A 1 215 ? 40.87900 7.33600   12.82500 1.000 43.26428  ?  367 HIS   A C    1 
ATOM   1592 O  O    . HIS   A 1 215 ? 41.66900 6.45400   13.19300 1.000 48.38659  ?  367 HIS   A O    1 
ATOM   1593 C  CB   . HIS   A 1 215 ? 38.80600 6.03700   13.34000 1.000 38.57775  ?  367 HIS   A CB   1 
ATOM   1594 C  CG   . HIS   A 1 215 ? 38.07500 6.79200   14.40600 1.000 43.78666  ?  367 HIS   A CG   1 
ATOM   1595 N  ND1  . HIS   A 1 215 ? 36.73200 6.61400   14.65900 1.000 41.91482  ?  367 HIS   A ND1  1 
ATOM   1596 C  CD2  . HIS   A 1 215 ? 38.49900 7.73900   15.27600 1.000 45.48205  ?  367 HIS   A CD2  1 
ATOM   1597 C  CE1  . HIS   A 1 215 ? 36.36100 7.41500   15.64200 1.000 38.90764  ?  367 HIS   A CE1  1 
ATOM   1598 N  NE2  . HIS   A 1 215 ? 37.41500 8.10700   16.03500 1.000 42.86226  ?  367 HIS   A NE2  1 
ATOM   1599 N  N    . PRO   A 1 216 ? 41.21300 8.62700   12.86100 1.000 47.86613  ?  368 PRO   A N    1 
ATOM   1600 C  CA   . PRO   A 1 216 ? 42.56500 9.01500   13.24800 1.000 51.41256  ?  368 PRO   A CA   1 
ATOM   1601 C  C    . PRO   A 1 216 ? 42.77700 8.82200   14.73700 1.000 44.11058  ?  368 PRO   A C    1 
ATOM   1602 O  O    . PRO   A 1 216 ? 41.82400 8.89800   15.53100 1.000 43.47063  ?  368 PRO   A O    1 
ATOM   1603 C  CB   . PRO   A 1 216 ? 42.62600 10.50400  12.86300 1.000 57.11417  ?  368 PRO   A CB   1 
ATOM   1604 C  CG   . PRO   A 1 216 ? 41.20800 10.95900  12.96500 1.000 56.59017  ?  368 PRO   A CG   1 
ATOM   1605 C  CD   . PRO   A 1 216 ? 40.37300 9.78800   12.52100 1.000 51.76598  ?  368 PRO   A CD   1 
ATOM   1606 N  N    . PRO   A 1 217 ? 44.00700 8.55700   15.16400 1.000 45.61697  ?  369 PRO   A N    1 
ATOM   1607 C  CA   . PRO   A 1 217 ? 44.30600 8.53400   16.59600 1.000 45.61357  ?  369 PRO   A CA   1 
ATOM   1608 C  C    . PRO   A 1 217 ? 44.25600 9.93900   17.16700 1.000 54.98247  ?  369 PRO   A C    1 
ATOM   1609 O  O    . PRO   A 1 217 ? 44.42400 10.92000  16.42500 1.000 52.41927  ?  369 PRO   A O    1 
ATOM   1610 C  CB   . PRO   A 1 217 ? 45.73000 7.95700   16.64800 1.000 47.53901  ?  369 PRO   A CB   1 
ATOM   1611 C  CG   . PRO   A 1 217 ? 46.32100 8.31600   15.32500 1.000 50.44253  ?  369 PRO   A CG   1 
ATOM   1612 C  CD   . PRO   A 1 217 ? 45.18700 8.23600   14.34200 1.000 47.64618  ?  369 PRO   A CD   1 
ATOM   1613 N  N    . PRO   A 1 218 ? 44.04600 10.08800  18.48500 1.000 52.55244  ?  370 PRO   A N    1 
ATOM   1614 C  CA   . PRO   A 1 218 ? 43.91500 9.03500   19.50000 1.000 52.60459  ?  370 PRO   A CA   1 
ATOM   1615 C  C    . PRO   A 1 218 ? 42.51500 8.42700   19.61500 1.000 48.70271  ?  370 PRO   A C    1 
ATOM   1616 O  O    . PRO   A 1 218 ? 42.33200 7.48200   20.38300 1.000 48.94808  ?  370 PRO   A O    1 
ATOM   1617 C  CB   . PRO   A 1 218 ? 44.27700 9.76700   20.79200 1.000 58.29784  ?  370 PRO   A CB   1 
ATOM   1618 C  CG   . PRO   A 1 218 ? 43.80600 11.15600  20.55800 1.000 56.98613  ?  370 PRO   A CG   1 
ATOM   1619 C  CD   . PRO   A 1 218 ? 44.02400 11.43300  19.09000 1.000 55.93103  ?  370 PRO   A CD   1 
ATOM   1620 N  N    . GLY   A 1 219 ? 41.54900 8.95600   18.86000 1.000 44.50587  ?  371 GLY   A N    1 
ATOM   1621 C  CA   . GLY   A 1 219 ? 40.18600 8.46300   18.96600 1.000 47.33386  ?  371 GLY   A CA   1 
ATOM   1622 C  C    . GLY   A 1 219 ? 40.04100 6.98800   18.63900 1.000 46.09451  ?  371 GLY   A C    1 
ATOM   1623 O  O    . GLY   A 1 219 ? 39.14700 6.31800   19.16200 1.000 43.41228  ?  371 GLY   A O    1 
ATOM   1624 N  N    . SER   A 1 220 ? 40.91100 6.47100   17.78700 1.000 47.54938  ?  372 SER   A N    1 
ATOM   1625 C  CA   . SER   A 1 220 ? 40.84000 5.06500   17.32100 1.000 48.20790  ?  372 SER   A CA   1 
ATOM   1626 C  C    . SER   A 1 220 ? 41.38700 4.05500   18.32900 1.000 48.18955  ?  372 SER   A C    1 
ATOM   1627 O  O    . SER   A 1 220 ? 41.21000 2.87500   18.09800 1.000 42.56704  ?  372 SER   A O    1 
ATOM   1628 C  CB   . SER   A 1 220 ? 41.60600 4.93800   16.04400 1.000 46.34526  ?  372 SER   A CB   1 
ATOM   1629 O  OG   . SER   A 1 220 ? 42.96800 5.24200   16.26500 1.000 47.18126  ?  372 SER   A OG   1 
ATOM   1630 N  N    . HIS   A 1 221 ? 41.99500 4.50700   19.41900 1.000 47.01273  ?  373 HIS   A N    1 
ATOM   1631 C  CA   . HIS   A 1 221 ? 42.68200 3.59200   20.32400 1.000 49.54783  ?  373 HIS   A CA   1 
ATOM   1632 C  C    . HIS   A 1 221 ? 41.70600 2.61200   20.96300 1.000 44.66109  ?  373 HIS   A C    1 
ATOM   1633 O  O    . HIS   A 1 221 ? 40.79800 3.01800   21.69600 1.000 44.34338  ?  373 HIS   A O    1 
ATOM   1634 C  CB   . HIS   A 1 221 ? 43.42200 4.38200   21.40200 1.000 51.53913  ?  373 HIS   A CB   1 
ATOM   1635 C  CG   . HIS   A 1 221 ? 44.08500 3.51800   22.42900 1.000 50.12235  ?  373 HIS   A CG   1 
ATOM   1636 N  ND1  . HIS   A 1 221 ? 45.08200 2.62000   22.11300 1.000 51.24703  ?  373 HIS   A ND1  1 
ATOM   1637 C  CD2  . HIS   A 1 221 ? 43.88800 3.40600   23.76400 1.000 48.03763  ?  373 HIS   A CD2  1 
ATOM   1638 C  CE1  . HIS   A 1 221 ? 45.47400 1.99600   23.20900 1.000 47.35272  ?  373 HIS   A CE1  1 
ATOM   1639 N  NE2  . HIS   A 1 221 ? 44.76500 2.45400   24.22500 1.000 50.81663  ?  373 HIS   A NE2  1 
ATOM   1640 N  N    A GLN   A 1 222 ? 41.90500 1.32000   20.68600 0.590 40.45554  ?  374 GLN   A N    1 
ATOM   1641 N  N    B GLN   A 1 222 ? 41.90100 1.32200   20.67700 0.410 41.24637  ?  374 GLN   A N    1 
ATOM   1642 C  CA   A GLN   A 1 222 ? 41.07100 0.24600   21.22900 0.590 42.33627  ?  374 GLN   A CA   1 
ATOM   1643 C  CA   B GLN   A 1 222 ? 41.07100 0.24500   21.22300 0.410 42.51247  ?  374 GLN   A CA   1 
ATOM   1644 C  C    A GLN   A 1 222 ? 39.59200 0.46700   20.92300 0.590 40.47340  ?  374 GLN   A C    1 
ATOM   1645 C  C    B GLN   A 1 222 ? 39.59100 0.47200   20.92700 0.410 40.50568  ?  374 GLN   A C    1 
ATOM   1646 O  O    A GLN   A 1 222 ? 38.72000 0.01500   21.67000 0.590 39.35779  ?  374 GLN   A O    1 
ATOM   1647 O  O    B GLN   A 1 222 ? 38.71900 0.03000   21.67900 0.410 39.50723  ?  374 GLN   A O    1 
ATOM   1648 C  CB   A GLN   A 1 222 ? 41.28200 0.08500   22.73900 0.590 46.10565  ?  374 GLN   A CB   1 
ATOM   1649 C  CB   B GLN   A 1 222 ? 41.29700 0.07700   22.72800 0.410 46.38634  ?  374 GLN   A CB   1 
ATOM   1650 C  CG   A GLN   A 1 222 ? 42.61300 -0.54600  23.12700 0.590 52.95404  ?  374 GLN   A CG   1 
ATOM   1651 C  CG   B GLN   A 1 222 ? 42.54700 -0.71500  23.09100 0.410 53.20967  ?  374 GLN   A CG   1 
ATOM   1652 C  CD   A GLN   A 1 222 ? 42.85100 -1.87800  22.44100 0.590 61.06049  ?  374 GLN   A CD   1 
ATOM   1653 C  CD   B GLN   A 1 222 ? 42.81700 -0.72400  24.58400 0.410 53.52050  ?  374 GLN   A CD   1 
ATOM   1654 O  OE1  A GLN   A 1 222 ? 43.70600 -1.99300  21.56200 0.590 77.72755  ?  374 GLN   A OE1  1 
ATOM   1655 O  OE1  B GLN   A 1 222 ? 42.21000 0.03400   25.33800 0.410 54.13975  ?  374 GLN   A OE1  1 
ATOM   1656 N  NE2  A GLN   A 1 222 ? 42.08800 -2.89200  22.83500 0.590 55.31493  ?  374 GLN   A NE2  1 
ATOM   1657 N  NE2  B GLN   A 1 222 ? 43.73200 -1.58600  25.01800 0.410 56.02129  ?  374 GLN   A NE2  1 
ATOM   1658 N  N    . LEU   A 1 223 ? 39.30000 1.15900   19.82000 1.000 39.76020  ?  375 LEU   A N    1 
ATOM   1659 C  CA   . LEU   A 1 223 ? 37.92000 1.54000   19.53100 1.000 36.99079  ?  375 LEU   A CA   1 
ATOM   1660 C  C    . LEU   A 1 223 ? 37.04600 0.32900   19.22500 1.000 42.94772  ?  375 LEU   A C    1 
ATOM   1661 O  O    . LEU   A 1 223 ? 35.89400 0.27000   19.66900 1.000 37.85156  ?  375 LEU   A O    1 
ATOM   1662 C  CB   . LEU   A 1 223 ? 37.87600 2.54100   18.37600 1.000 36.60257  ?  375 LEU   A CB   1 
ATOM   1663 C  CG   . LEU   A 1 223 ? 36.47900 3.05700   18.01700 1.000 37.08825  ?  375 LEU   A CG   1 
ATOM   1664 C  CD1  . LEU   A 1 223 ? 35.75500 3.56000   19.25900 1.000 35.72185  ?  375 LEU   A CD1  1 
ATOM   1665 C  CD2  . LEU   A 1 223 ? 36.57000 4.15200   16.97200 1.000 40.41205  ?  375 LEU   A CD2  1 
ATOM   1666 N  N    . TYR   A 1 224 ? 37.56200 -0.64500  18.46900 1.000 42.92534  ?  376 TYR   A N    1 
ATOM   1667 C  CA   . TYR   A 1 224 ? 36.75300 -1.82500  18.17000 1.000 41.39071  ?  376 TYR   A CA   1 
ATOM   1668 C  C    . TYR   A 1 224 ? 36.42300 -2.59800  19.43900 1.000 40.44225  ?  376 TYR   A C    1 
ATOM   1669 O  O    . TYR   A 1 224 ? 35.27800 -3.02200  19.63700 1.000 38.63619  ?  376 TYR   A O    1 
ATOM   1670 C  CB   . TYR   A 1 224 ? 37.46000 -2.73400  17.16600 1.000 42.22743  ?  376 TYR   A CB   1 
ATOM   1671 C  CG   . TYR   A 1 224 ? 36.67100 -3.98800  16.85700 1.000 39.61553  ?  376 TYR   A CG   1 
ATOM   1672 C  CD1  . TYR   A 1 224 ? 35.46200 -3.91800  16.17400 1.000 38.98088  ?  376 TYR   A CD1  1 
ATOM   1673 C  CD2  . TYR   A 1 224 ? 37.12200 -5.23700  17.26200 1.000 45.18949  ?  376 TYR   A CD2  1 
ATOM   1674 C  CE1  . TYR   A 1 224 ? 34.73100 -5.05700  15.89400 1.000 41.76542  ?  376 TYR   A CE1  1 
ATOM   1675 C  CE2  . TYR   A 1 224 ? 36.39700 -6.38300  16.98600 1.000 44.67046  ?  376 TYR   A CE2  1 
ATOM   1676 C  CZ   . TYR   A 1 224 ? 35.20300 -6.28600  16.30100 1.000 43.67382  ?  376 TYR   A CZ   1 
ATOM   1677 O  OH   . TYR   A 1 224 ? 34.47400 -7.42000  16.02200 1.000 48.49790  ?  376 TYR   A OH   1 
ATOM   1678 N  N    . ALA   A 1 225 ? 37.41400 -2.78800  20.31400 1.000 39.61253  ?  377 ALA   A N    1 
ATOM   1679 C  CA   . ALA   A 1 225 ? 37.17000 -3.49000  21.56900 1.000 39.01923  ?  377 ALA   A CA   1 
ATOM   1680 C  C    . ALA   A 1 225 ? 36.17500 -2.73400  22.43900 1.000 40.35091  ?  377 ALA   A C    1 
ATOM   1681 O  O    . ALA   A 1 225 ? 35.34600 -3.34600  23.12400 1.000 43.65059  ?  377 ALA   A O    1 
ATOM   1682 C  CB   . ALA   A 1 225 ? 38.48500 -3.70400  22.31800 1.000 42.92323  ?  377 ALA   A CB   1 
ATOM   1683 N  N    . LYS   A 1 226 ? 36.24100 -1.39900  22.42700 1.000 39.72586  ?  378 LYS   A N    1 
ATOM   1684 C  CA   . LYS   A 1 226 ? 35.28000 -0.60900  23.19000 1.000 35.15515  ?  378 LYS   A CA   1 
ATOM   1685 C  C    . LYS   A 1 226 ? 33.87400 -0.73800  22.62200 1.000 38.06654  ?  378 LYS   A C    1 
ATOM   1686 O  O    . LYS   A 1 226 ? 32.89600 -0.72800  23.37900 1.000 36.13303  ?  378 LYS   A O    1 
ATOM   1687 C  CB   . LYS   A 1 226 ? 35.71000 0.85900   23.21900 1.000 35.42359  ?  378 LYS   A CB   1 
ATOM   1688 C  CG   . LYS   A 1 226 ? 36.91400 1.13400   24.11200 1.000 40.63337  ?  378 LYS   A CG   1 
ATOM   1689 C  CD   . LYS   A 1 226 ? 37.23100 2.62100   24.18200 1.000 43.26073  ?  378 LYS   A CD   1 
ATOM   1690 C  CE   . LYS   A 1 226 ? 38.52200 2.87200   24.95000 1.000 54.58334  ?  378 LYS   A CE   1 
ATOM   1691 N  NZ   . LYS   A 1 226 ? 39.11800 4.20100   24.63600 1.000 57.90915  ?  378 LYS   A NZ   1 
ATOM   1692 N  N    . MET   A 1 227 ? 33.74900 -0.86700  21.30000 1.000 33.33860  ?  379 MET   A N    1 
ATOM   1693 C  CA   . MET   A 1 227 ? 32.42800 -1.03400  20.70500 1.000 32.11283  ?  379 MET   A CA   1 
ATOM   1694 C  C    . MET   A 1 227 ? 31.87200 -2.42600  20.98200 1.000 36.27996  ?  379 MET   A C    1 
ATOM   1695 O  O    . MET   A 1 227 ? 30.66100 -2.58800  21.16800 1.000 32.63169  ?  379 MET   A O    1 
ATOM   1696 C  CB   . MET   A 1 227 ? 32.49400 -0.76000  19.20300 1.000 31.90814  ?  379 MET   A CB   1 
ATOM   1697 C  CG   . MET   A 1 227 ? 32.83700 0.68200   18.86200 1.000 32.54893  ?  379 MET   A CG   1 
ATOM   1698 S  SD   . MET   A 1 227 ? 33.10600 0.95800   17.10100 1.000 32.64293  ?  379 MET   A SD   1 
ATOM   1699 C  CE   . MET   A 1 227 ? 31.41800 0.83900   16.49700 1.000 27.59614  ?  379 MET   A CE   1 
ATOM   1700 N  N    . ILE   A 1 228 ? 32.73900 -3.44100  21.01300 1.000 39.69104  ?  380 ILE   A N    1 
ATOM   1701 C  CA   . ILE   A 1 228 ? 32.28400 -4.78700  21.35000 1.000 44.96472  ?  380 ILE   A CA   1 
ATOM   1702 C  C    . ILE   A 1 228 ? 31.87800 -4.86400  22.81700 1.000 42.11630  ?  380 ILE   A C    1 
ATOM   1703 O  O    . ILE   A 1 228 ? 30.95100 -5.60200  23.17300 1.000 40.57831  ?  380 ILE   A O    1 
ATOM   1704 C  CB   . ILE   A 1 228 ? 33.37200 -5.82200  21.00200 1.000 49.91393  ?  380 ILE   A CB   1 
ATOM   1705 C  CG1  . ILE   A 1 228 ? 33.65400 -5.81300  19.49800 1.000 45.50345  ?  380 ILE   A CG1  1 
ATOM   1706 C  CG2  . ILE   A 1 228 ? 32.95400 -7.22000  21.43900 1.000 51.79479  ?  380 ILE   A CG2  1 
ATOM   1707 C  CD1  . ILE   A 1 228 ? 32.40600 -5.85800  18.64000 1.000 49.90047  ?  380 ILE   A CD1  1 
ATOM   1708 N  N    . GLN   A 1 229 ? 32.55000 -4.10700  23.69000 1.000 34.99692  ?  381 GLN   A N    1 
ATOM   1709 C  CA   . GLN   A 1 229 ? 32.12000 -4.03500  25.08300 1.000 36.22776  ?  381 GLN   A CA   1 
ATOM   1710 C  C    . GLN   A 1 229 ? 30.71300 -3.46000  25.19300 1.000 36.61992  ?  381 GLN   A C    1 
ATOM   1711 O  O    . GLN   A 1 229 ? 29.91900 -3.89500  26.03600 1.000 33.73062  ?  381 GLN   A O    1 
ATOM   1712 C  CB   . GLN   A 1 229 ? 33.10500 -3.19500  25.89500 1.000 42.87288  ?  381 GLN   A CB   1 
ATOM   1713 C  CG   . GLN   A 1 229 ? 32.78700 -3.14400  27.38000 1.000 48.17419  ?  381 GLN   A CG   1 
ATOM   1714 C  CD   . GLN   A 1 229 ? 32.61200 -4.52400  27.98500 1.000 53.38891  ?  381 GLN   A CD   1 
ATOM   1715 O  OE1  . GLN   A 1 229 ? 33.44100 -5.41100  27.78300 1.000 54.91432  ?  381 GLN   A OE1  1 
ATOM   1716 N  NE2  . GLN   A 1 229 ? 31.52800 -4.71300  28.73000 1.000 47.55196  ?  381 GLN   A NE2  1 
ATOM   1717 N  N    . LYS   A 1 230 ? 30.38500 -2.48200  24.34600 1.000 33.74207  ?  382 LYS   A N    1 
ATOM   1718 C  CA   . LYS   A 1 230 ? 29.04300 -1.91100  24.36700 1.000 32.19053  ?  382 LYS   A CA   1 
ATOM   1719 C  C    . LYS   A 1 230 ? 27.99200 -2.92800  23.94400 1.000 34.33178  ?  382 LYS   A C    1 
ATOM   1720 O  O    . LYS   A 1 230 ? 26.85300 -2.87200  24.42300 1.000 33.27317  ?  382 LYS   A O    1 
ATOM   1721 C  CB   . LYS   A 1 230 ? 28.98600 -0.67400  23.47200 1.000 37.03503  ?  382 LYS   A CB   1 
ATOM   1722 C  CG   . LYS   A 1 230 ? 29.68100 0.53800   24.06800 1.000 34.79332  ?  382 LYS   A CG   1 
ATOM   1723 C  CD   . LYS   A 1 230 ? 29.06000 0.91500   25.40400 1.000 42.28842  ?  382 LYS   A CD   1 
ATOM   1724 C  CE   . LYS   A 1 230 ? 29.99800 1.78000   26.23400 1.000 47.19739  ?  382 LYS   A CE   1 
ATOM   1725 N  NZ   . LYS   A 1 230 ? 30.78100 0.96800   27.20900 1.000 49.40385  ?  382 LYS   A NZ   1 
ATOM   1726 N  N    . LEU   A 1 231 ? 28.34600 -3.86200  23.05700 1.000 30.71440  ?  383 LEU   A N    1 
ATOM   1727 C  CA   . LEU   A 1 231 ? 27.41600 -4.93400  22.71200 1.000 32.96175  ?  383 LEU   A CA   1 
ATOM   1728 C  C    . LEU   A 1 231 ? 27.19000 -5.86100  23.89900 1.000 33.32225  ?  383 LEU   A C    1 
ATOM   1729 O  O    . LEU   A 1 231 ? 26.07900 -6.36500  24.10000 1.000 33.37323  ?  383 LEU   A O    1 
ATOM   1730 C  CB   . LEU   A 1 231 ? 27.93800 -5.71800  21.50700 1.000 30.27952  ?  383 LEU   A CB   1 
ATOM   1731 C  CG   . LEU   A 1 231 ? 27.99500 -4.96900  20.17600 1.000 32.59921  ?  383 LEU   A CG   1 
ATOM   1732 C  CD1  . LEU   A 1 231 ? 28.58300 -5.85400  19.08700 1.000 34.18930  ?  383 LEU   A CD1  1 
ATOM   1733 C  CD2  . LEU   A 1 231 ? 26.61000 -4.47700  19.78300 1.000 35.56385  ?  383 LEU   A CD2  1 
ATOM   1734 N  N    . ALA   A 1 232 ? 28.23500 -6.10000  24.69400 1.000 31.93510  ?  384 ALA   A N    1 
ATOM   1735 C  CA   . ALA   A 1 232 ? 28.07900 -6.89200  25.90800 1.000 32.57079  ?  384 ALA   A CA   1 
ATOM   1736 C  C    . ALA   A 1 232 ? 27.23000 -6.15800  26.93700 1.000 36.28938  ?  384 ALA   A C    1 
ATOM   1737 O  O    . ALA   A 1 232 ? 26.38500 -6.77100  27.60100 1.000 36.37094  ?  384 ALA   A O    1 
ATOM   1738 C  CB   . ALA   A 1 232 ? 29.45200 -7.23500  26.49000 1.000 35.32142  ?  384 ALA   A CB   1 
ATOM   1739 N  N    . ASP   A 1 233 ? 27.44300 -4.84700  27.08500 1.000 31.98913  ?  385 ASP   A N    1 
ATOM   1740 C  CA   . ASP   A 1 233 ? 26.58700 -4.05100  27.96000 1.000 33.89728  ?  385 ASP   A CA   1 
ATOM   1741 C  C    . ASP   A 1 233 ? 25.12600 -4.16200  27.54400 1.000 32.65992  ?  385 ASP   A C    1 
ATOM   1742 O  O    . ASP   A 1 233 ? 24.22900 -4.19200  28.39500 1.000 36.04831  ?  385 ASP   A O    1 
ATOM   1743 C  CB   . ASP   A 1 233 ? 27.02100 -2.58500  27.93900 1.000 30.68619  ?  385 ASP   A CB   1 
ATOM   1744 C  CG   . ASP   A 1 233 ? 28.42000 -2.37800  28.47900 1.000 40.83023  ?  385 ASP   A CG   1 
ATOM   1745 O  OD1  . ASP   A 1 233 ? 28.96100 -1.26900  28.29400 1.000 42.17088  ?  385 ASP   A OD1  1 
ATOM   1746 O  OD2  . ASP   A 1 233 ? 28.97500 -3.31600  29.09000 1.000 43.42792  ?  385 ASP   A OD2  1 
ATOM   1747 N  N    . LEU   A 1 234 ? 24.87100 -4.22800  26.23600 1.000 29.85639  ?  386 LEU   A N    1 
ATOM   1748 C  CA   . LEU   A 1 234 ? 23.49800 -4.29800  25.74800 1.000 27.31312  ?  386 LEU   A CA   1 
ATOM   1749 C  C    . LEU   A 1 234 ? 22.83000 -5.61700  26.11000 1.000 33.33134  ?  386 LEU   A C    1 
ATOM   1750 O  O    . LEU   A 1 234 ? 21.61700 -5.64700  26.34600 1.000 31.16666  ?  386 LEU   A O    1 
ATOM   1751 C  CB   . LEU   A 1 234 ? 23.46900 -4.08700  24.23600 1.000 28.27875  ?  386 LEU   A CB   1 
ATOM   1752 C  CG   . LEU   A 1 234 ? 23.70500 -2.64300  23.79600 1.000 33.73231  ?  386 LEU   A CG   1 
ATOM   1753 C  CD1  . LEU   A 1 234 ? 24.07500 -2.58200  22.32600 1.000 29.55374  ?  386 LEU   A CD1  1 
ATOM   1754 C  CD2  . LEU   A 1 234 ? 22.47700 -1.79300  24.08400 1.000 34.80884  ?  386 LEU   A CD2  1 
ATOM   1755 N  N    . ARG   A 1 235 ? 23.59200 -6.71400  26.14600 1.000 36.19309  ?  387 ARG   A N    1 
ATOM   1756 C  CA   . ARG   A 1 235 ? 23.01700 -7.99000  26.56100 1.000 38.61703  ?  387 ARG   A CA   1 
ATOM   1757 C  C    . ARG   A 1 235 ? 22.48800 -7.91300  27.98700 1.000 42.69405  ?  387 ARG   A C    1 
ATOM   1758 O  O    . ARG   A 1 235 ? 21.39400 -8.40900  28.27900 1.000 36.91136  ?  387 ARG   A O    1 
ATOM   1759 C  CB   . ARG   A 1 235 ? 24.05500 -9.10600  26.43300 1.000 40.82118  ?  387 ARG   A CB   1 
ATOM   1760 C  CG   . ARG   A 1 235 ? 24.61400 -9.29000  25.03100 1.000 40.02676  ?  387 ARG   A CG   1 
ATOM   1761 C  CD   . ARG   A 1 235 ? 23.53200 -9.69000  24.04400 1.000 38.52455  ?  387 ARG   A CD   1 
ATOM   1762 N  NE   . ARG   A 1 235 ? 24.07700 -9.98400  22.72100 1.000 38.52046  ?  387 ARG   A NE   1 
ATOM   1763 C  CZ   . ARG   A 1 235 ? 24.36500 -11.20600 22.28300 1.000 41.60954  ?  387 ARG   A CZ   1 
ATOM   1764 N  NH1  . ARG   A 1 235 ? 24.16600 -12.26100 23.06200 1.000 47.34461  ?  387 ARG   A NH1  1 
ATOM   1765 N  NH2  . ARG   A 1 235 ? 24.85200 -11.37600 21.06100 1.000 39.35842  ?  387 ARG   A NH2  1 
ATOM   1766 N  N    . SER   A 1 236 ? 23.24800 -7.28400  28.88600 1.000 38.62383  ?  388 SER   A N    1 
ATOM   1767 C  CA   . SER   A 1 236 ? 22.79800 -7.13000  30.26600 1.000 40.01430  ?  388 SER   A CA   1 
ATOM   1768 C  C    . SER   A 1 236 ? 21.59900 -6.19200  30.35800 1.000 36.95740  ?  388 SER   A C    1 
ATOM   1769 O  O    . SER   A 1 236 ? 20.65800 -6.45100  31.11900 1.000 40.35459  ?  388 SER   A O    1 
ATOM   1770 C  CB   . SER   A 1 236 ? 23.94900 -6.62000  31.13500 1.000 46.40831  ?  388 SER   A CB   1 
ATOM   1771 O  OG   . SER   A 1 236 ? 23.47700 -5.77300  32.16600 1.000 56.18219  ?  388 SER   A OG   1 
ATOM   1772 N  N    . LEU   A 1 237 ? 21.61700 -5.09500  29.59600 1.000 34.11118  ?  389 LEU   A N    1 
ATOM   1773 C  CA   . LEU   A 1 237 ? 20.46700 -4.19600  29.57100 1.000 31.29028  ?  389 LEU   A CA   1 
ATOM   1774 C  C    . LEU   A 1 237 ? 19.24600 -4.88700  28.98000 1.000 32.40507  ?  389 LEU   A C    1 
ATOM   1775 O  O    . LEU   A 1 237 ? 18.11700 -4.66400  29.43300 1.000 33.42213  ?  389 LEU   A O    1 
ATOM   1776 C  CB   . LEU   A 1 237 ? 20.80700 -2.93300  28.78000 1.000 30.88802  ?  389 LEU   A CB   1 
ATOM   1777 C  CG   . LEU   A 1 237 ? 21.82300 -2.00000  29.44200 1.000 34.60295  ?  389 LEU   A CG   1 
ATOM   1778 C  CD1  . LEU   A 1 237 ? 22.41500 -1.03000  28.42800 1.000 30.42798  ?  389 LEU   A CD1  1 
ATOM   1779 C  CD2  . LEU   A 1 237 ? 21.17800 -1.24700  30.59500 1.000 38.33050  ?  389 LEU   A CD2  1 
ATOM   1780 N  N    . ASN   A 1 238 ? 19.45600 -5.72500  27.96200 1.000 32.80680  ?  390 ASN   A N    1 
ATOM   1781 C  CA   . ASN   A 1 238 ? 18.36900 -6.51700  27.39400 1.000 33.85555  ?  390 ASN   A CA   1 
ATOM   1782 C  C    . ASN   A 1 238 ? 17.71800 -7.39300  28.45800 1.000 35.29284  ?  390 ASN   A C    1 
ATOM   1783 O  O    . ASN   A 1 238 ? 16.48800 -7.46000  28.55900 1.000 36.23107  ?  390 ASN   A O    1 
ATOM   1784 C  CB   . ASN   A 1 238 ? 18.90900 -7.37100  26.24400 1.000 31.24622  ?  390 ASN   A CB   1 
ATOM   1785 C  CG   . ASN   A 1 238 ? 17.81500 -7.95600  25.37400 1.000 37.04355  ?  390 ASN   A CG   1 
ATOM   1786 O  OD1  . ASN   A 1 238 ? 16.68900 -8.17600  25.82400 1.000 35.08421  ?  390 ASN   A OD1  1 
ATOM   1787 N  ND2  . ASN   A 1 238 ? 18.14800 -8.22700  24.11800 1.000 32.73036  ?  390 ASN   A ND2  1 
ATOM   1788 N  N    . GLU   A 1 239 ? 18.53600 -8.07300  29.26600 1.000 38.66370  ?  391 GLU   A N    1 
ATOM   1789 C  CA   . GLU   A 1 239 ? 17.99900 -8.98100  30.27500 1.000 42.84399  ?  391 GLU   A CA   1 
ATOM   1790 C  C    . GLU   A 1 239 ? 17.19500 -8.23300  31.33100 1.000 43.64766  ?  391 GLU   A C    1 
ATOM   1791 O  O    . GLU   A 1 239 ? 16.10900 -8.67700  31.72200 1.000 43.24101  ?  391 GLU   A O    1 
ATOM   1792 C  CB   . GLU   A 1 239 ? 19.13500 -9.76900  30.92500 1.000 45.49066  ?  391 GLU   A CB   1 
ATOM   1793 C  CG   . GLU   A 1 239 ? 19.93300 -10.61900 29.95300 1.000 56.02077  ?  391 GLU   A CG   1 
ATOM   1794 C  CD   . GLU   A 1 239 ? 20.43700 -11.90200 30.57800 1.000 69.05895  ?  391 GLU   A CD   1 
ATOM   1795 O  OE1  . GLU   A 1 239 ? 21.45600 -11.85000 31.30000 1.000 70.93396  ?  391 GLU   A OE1  1 
ATOM   1796 O  OE2  . GLU   A 1 239 ? 19.81700 -12.96100 30.34600 1.000 71.90203  ?  391 GLU   A OE2  1 
ATOM   1797 N  N    . GLU   A 1 240 ? 17.71000 -7.09700  31.80600 1.000 41.51319  ?  392 GLU   A N    1 
ATOM   1798 C  CA   . GLU   A 1 240 ? 16.99500 -6.35500  32.83900 1.000 43.54247  ?  392 GLU   A CA   1 
ATOM   1799 C  C    . GLU   A 1 240 ? 15.70200 -5.75800  32.30000 1.000 39.00582  ?  392 GLU   A C    1 
ATOM   1800 O  O    . GLU   A 1 240 ? 14.68200 -5.74600  32.99800 1.000 39.59719  ?  392 GLU   A O    1 
ATOM   1801 C  CB   . GLU   A 1 240 ? 17.88500 -5.25900  33.42400 1.000 42.29009  ?  392 GLU   A CB   1 
ATOM   1802 C  CG   . GLU   A 1 240 ? 17.26500 -4.54800  34.62100 1.000 44.45208  ?  392 GLU   A CG   1 
ATOM   1803 C  CD   . GLU   A 1 240 ? 16.94000 -5.49400  35.76500 1.000 46.64900  ?  392 GLU   A CD   1 
ATOM   1804 O  OE1  . GLU   A 1 240 ? 15.87600 -5.32300  36.39700 1.000 46.80586  ?  392 GLU   A OE1  1 
ATOM   1805 O  OE2  . GLU   A 1 240 ? 17.75200 -6.40400  36.03600 1.000 49.02938  ?  392 GLU   A OE2  1 
ATOM   1806 N  N    . HIS   A 1 241 ? 15.72000 -5.25600  31.06300 1.000 31.43749  ?  393 HIS   A N    1 
ATOM   1807 C  CA   . HIS   A 1 241 ? 14.49400 -4.71200  30.48800 1.000 34.78887  ?  393 HIS   A CA   1 
ATOM   1808 C  C    . HIS   A 1 241 ? 13.43500 -5.79500  30.33300 1.000 35.53200  ?  393 HIS   A C    1 
ATOM   1809 O  O    . HIS   A 1 241 ? 12.26700 -5.58900  30.68100 1.000 34.60884  ?  393 HIS   A O    1 
ATOM   1810 C  CB   . HIS   A 1 241 ? 14.76600 -4.04800  29.13900 1.000 34.42622  ?  393 HIS   A CB   1 
ATOM   1811 C  CG   . HIS   A 1 241 ? 13.51700 -3.60000  28.44400 1.000 34.21807  ?  393 HIS   A CG   1 
ATOM   1812 N  ND1  . HIS   A 1 241 ? 12.85300 -4.38400  27.52600 1.000 35.20868  ?  393 HIS   A ND1  1 
ATOM   1813 C  CD2  . HIS   A 1 241 ? 12.79000 -2.46300  28.56300 1.000 35.53756  ?  393 HIS   A CD2  1 
ATOM   1814 C  CE1  . HIS   A 1 241 ? 11.78000 -3.74400  27.09700 1.000 37.53476  ?  393 HIS   A CE1  1 
ATOM   1815 N  NE2  . HIS   A 1 241 ? 11.71800 -2.57600  27.71100 1.000 33.24399  ?  393 HIS   A NE2  1 
ATOM   1816 N  N    . SER   A 1 242 ? 13.82400 -6.96000  29.80600 1.000 37.30376  ?  394 SER   A N    1 
ATOM   1817 C  CA   . SER   A 1 242 ? 12.87200 -8.05700  29.65400 1.000 40.57775  ?  394 SER   A CA   1 
ATOM   1818 C  C    . SER   A 1 242 ? 12.29800 -8.47700  31.00000 1.000 41.53898  ?  394 SER   A C    1 
ATOM   1819 O  O    . SER   A 1 242 ? 11.10900 -8.80100  31.10500 1.000 40.33280  ?  394 SER   A O    1 
ATOM   1820 C  CB   . SER   A 1 242 ? 13.54400 -9.24500  28.96600 1.000 49.78420  ?  394 SER   A CB   1 
ATOM   1821 O  OG   . SER   A 1 242 ? 14.14600 -8.86000  27.74300 1.000 53.85016  ?  394 SER   A OG   1 
ATOM   1822 N  N    . LYS   A 1 243 ? 13.13300 -8.48100  32.04100 1.000 41.55226  ?  395 LYS   A N    1 
ATOM   1823 C  CA   . LYS   A 1 243 ? 12.66200 -8.78300  33.38800 1.000 42.98352  ?  395 LYS   A CA   1 
ATOM   1824 C  C    . LYS   A 1 243 ? 11.58100 -7.80000  33.82200 1.000 42.58505  ?  395 LYS   A C    1 
ATOM   1825 O  O    . LYS   A 1 243 ? 10.47600 -8.19700  34.21000 1.000 48.45764  ?  395 LYS   A O    1 
ATOM   1826 C  CB   . LYS   A 1 243 ? 13.84300 -8.75400  34.36100 1.000 46.38254  ?  395 LYS   A CB   1 
ATOM   1827 C  CG   . LYS   A 1 243 ? 13.56100 -9.35900  35.72400 1.000 52.98690  ?  395 LYS   A CG   1 
ATOM   1828 C  CD   . LYS   A 1 243 ? 14.85200 -9.52600  36.51500 1.000 51.43225  ?  395 LYS   A CD   1 
ATOM   1829 C  CE   . LYS   A 1 243 ? 14.57700 -9.72300  37.99800 1.000 55.46710  ?  395 LYS   A CE   1 
ATOM   1830 N  NZ   . LYS   A 1 243 ? 15.77800 -9.40200  38.82700 1.000 57.10364  ?  395 LYS   A NZ   1 
ATOM   1831 N  N    . GLN   A 1 244 ? 11.88600 -6.50200  33.75800 1.000 43.32704  ?  396 GLN   A N    1 
ATOM   1832 C  CA   . GLN   A 1 244 ? 10.91100 -5.49700  34.16200 1.000 41.12611  ?  396 GLN   A CA   1 
ATOM   1833 C  C    . GLN   A 1 244 ? 9.72300  -5.45100  33.21000 1.000 42.56656  ?  396 GLN   A C    1 
ATOM   1834 O  O    . GLN   A 1 244 ? 8.59400  -5.20000  33.64700 1.000 41.16614  ?  396 GLN   A O    1 
ATOM   1835 C  CB   . GLN   A 1 244 ? 11.57900 -4.12700  34.25600 1.000 40.38742  ?  396 GLN   A CB   1 
ATOM   1836 C  CG   . GLN   A 1 244 ? 12.80600 -4.11000  35.15100 1.000 45.59067  ?  396 GLN   A CG   1 
ATOM   1837 C  CD   . GLN   A 1 244 ? 13.20500 -2.71000  35.57200 1.000 48.89947  ?  396 GLN   A CD   1 
ATOM   1838 O  OE1  . GLN   A 1 244 ? 12.61000 -1.72500  35.13800 1.000 43.42990  ?  396 GLN   A OE1  1 
ATOM   1839 N  NE2  . GLN   A 1 244 ? 14.22500 -2.61500  36.41800 1.000 46.70543  ?  396 GLN   A NE2  1 
ATOM   1840 N  N    . TYR   A 1 245 ? 9.94800  -5.69300  31.91600 1.000 37.16747  ?  397 TYR   A N    1 
ATOM   1841 C  CA   . TYR   A 1 245 ? 8.82900  -5.74300  30.98000 1.000 41.23310  ?  397 TYR   A CA   1 
ATOM   1842 C  C    . TYR   A 1 245 ? 7.88500  -6.89000  31.31400 1.000 44.85371  ?  397 TYR   A C    1 
ATOM   1843 O  O    . TYR   A 1 245 ? 6.66000  -6.73700  31.24100 1.000 39.55623  ?  397 TYR   A O    1 
ATOM   1844 C  CB   . TYR   A 1 245 ? 9.33500  -5.87500  29.54300 1.000 35.32301  ?  397 TYR   A CB   1 
ATOM   1845 C  CG   . TYR   A 1 245 ? 8.21300  -6.04000  28.53900 1.000 36.71993  ?  397 TYR   A CG   1 
ATOM   1846 C  CD1  . TYR   A 1 245 ? 7.52900  -4.93700  28.04700 1.000 32.79068  ?  397 TYR   A CD1  1 
ATOM   1847 C  CD2  . TYR   A 1 245 ? 7.82400  -7.30100  28.10200 1.000 39.35288  ?  397 TYR   A CD2  1 
ATOM   1848 C  CE1  . TYR   A 1 245 ? 6.49400  -5.08400  27.14000 1.000 35.21042  ?  397 TYR   A CE1  1 
ATOM   1849 C  CE2  . TYR   A 1 245 ? 6.79000  -7.45800  27.19800 1.000 39.81193  ?  397 TYR   A CE2  1 
ATOM   1850 C  CZ   . TYR   A 1 245 ? 6.13000  -6.34500  26.72000 1.000 38.72554  ?  397 TYR   A CZ   1 
ATOM   1851 O  OH   . TYR   A 1 245 ? 5.10500  -6.49800  25.81700 1.000 39.55958  ?  397 TYR   A OH   1 
ATOM   1852 N  N    . ARG   A 1 246 ? 8.43600  -8.05200  31.67500 1.000 45.48172  ?  398 ARG   A N    1 
ATOM   1853 C  CA   . ARG   A 1 246 ? 7.59200  -9.20300  31.97900 1.000 50.33515  ?  398 ARG   A CA   1 
ATOM   1854 C  C    . ARG   A 1 246 ? 6.75700  -8.96200  33.23000 1.000 50.68105  ?  398 ARG   A C    1 
ATOM   1855 O  O    . ARG   A 1 246 ? 5.60300  -9.39800  33.30500 1.000 47.55005  ?  398 ARG   A O    1 
ATOM   1856 C  CB   . ARG   A 1 246 ? 8.45100  -10.46100 32.12700 1.000 56.64918  ?  398 ARG   A CB   1 
ATOM   1857 C  CG   . ARG   A 1 246 ? 8.67900  -11.19000 30.81100 1.000 60.92703  ?  398 ARG   A CG   1 
ATOM   1858 C  CD   . ARG   A 1 246 ? 9.74600  -12.27800 30.90000 1.000 66.12742  ?  398 ARG   A CD   1 
ATOM   1859 N  NE   . ARG   A 1 246 ? 10.13900 -12.59700 32.27000 1.000 72.16572  ?  398 ARG   A NE   1 
ATOM   1860 C  CZ   . ARG   A 1 246 ? 11.40000 -12.70300 32.67900 1.000 75.65957  ?  398 ARG   A CZ   1 
ATOM   1861 N  NH1  . ARG   A 1 246 ? 12.39600 -12.51200 31.82400 1.000 73.57749  ?  398 ARG   A NH1  1 
ATOM   1862 N  NH2  . ARG   A 1 246 ? 11.66700 -12.99900 33.94400 1.000 77.60623  ?  398 ARG   A NH2  1 
ATOM   1863 N  N    . SER   A 1 247 ? 7.31600  -8.25800  34.21800 1.000 49.66826  ?  399 SER   A N    1 
ATOM   1864 C  CA   . SER   A 1 247 ? 6.54900  -7.94400  35.41900 1.000 53.81211  ?  399 SER   A CA   1 
ATOM   1865 C  C    . SER   A 1 247 ? 5.50000  -6.87500  35.13900 1.000 51.97734  ?  399 SER   A C    1 
ATOM   1866 O  O    . SER   A 1 247 ? 4.37200  -6.95900  35.64000 1.000 53.01517  ?  399 SER   A O    1 
ATOM   1867 C  CB   . SER   A 1 247 ? 7.48400  -7.49700  36.54200 1.000 57.99424  ?  399 SER   A CB   1 
ATOM   1868 O  OG   . SER   A 1 247 ? 6.81900  -6.62200  37.43900 1.000 62.56927  ?  399 SER   A OG   1 
ATOM   1869 N  N    . LEU   A 1 248 ? 5.85000  -5.86300  34.34300 1.000 48.16200  ?  400 LEU   A N    1 
ATOM   1870 C  CA   . LEU   A 1 248 ? 4.88600  -4.82100  34.00400 1.000 47.90272  ?  400 LEU   A CA   1 
ATOM   1871 C  C    . LEU   A 1 248 ? 3.75100  -5.38200  33.15500 1.000 42.67926  ?  400 LEU   A C    1 
ATOM   1872 O  O    . LEU   A 1 248 ? 2.57100  -5.15900  33.45200 1.000 49.39299  ?  400 LEU   A O    1 
ATOM   1873 C  CB   . LEU   A 1 248 ? 5.58900  -3.67400  33.27600 1.000 44.13921  ?  400 LEU   A CB   1 
ATOM   1874 C  CG   . LEU   A 1 248 ? 6.55400  -2.82600  34.11100 1.000 51.50534  ?  400 LEU   A CG   1 
ATOM   1875 C  CD1  . LEU   A 1 248 ? 7.06100  -1.63100  33.31400 1.000 51.12835  ?  400 LEU   A CD1  1 
ATOM   1876 C  CD2  . LEU   A 1 248 ? 5.89600  -2.37200  35.40400 1.000 55.43257  ?  400 LEU   A CD2  1 
ATOM   1877 N  N    . SER   A 1 249 ? 4.08800  -6.13100  32.10400 1.000 48.92262  ?  401 SER   A N    1 
ATOM   1878 C  CA   . SER   A 1 249 ? 3.07800  -6.65500  31.19200 1.000 48.59942  ?  401 SER   A CA   1 
ATOM   1879 C  C    . SER   A 1 249 ? 2.24400  -7.77500  31.80000 1.000 51.88808  ?  401 SER   A C    1 
ATOM   1880 O  O    . SER   A 1 249 ? 1.22300  -8.14700  31.21100 1.000 46.83294  ?  401 SER   A O    1 
ATOM   1881 C  CB   . SER   A 1 249 ? 3.73800  -7.14800  29.90100 1.000 48.07208  ?  401 SER   A CB   1 
ATOM   1882 O  OG   . SER   A 1 249 ? 4.60500  -8.24000  30.15200 1.000 51.93279  ?  401 SER   A OG   1 
ATOM   1883 N  N    . PHE   A 1 250 ? 2.64200  -8.32300  32.95200 1.000 54.23608  ?  402 PHE   A N    1 
ATOM   1884 C  CA   . PHE   A 1 250 ? 1.83500  -9.36700  33.57700 1.000 54.82750  ?  402 PHE   A CA   1 
ATOM   1885 C  C    . PHE   A 1 250 ? 0.52900  -8.81300  34.12800 1.000 55.64572  ?  402 PHE   A C    1 
ATOM   1886 O  O    . PHE   A 1 250 ? -0.45800 -9.54800  34.23700 1.000 52.65780  ?  402 PHE   A O    1 
ATOM   1887 C  CB   . PHE   A 1 250 ? 2.62200  -10.06100 34.68900 1.000 59.96911  ?  402 PHE   A CB   1 
ATOM   1888 C  CG   . PHE   A 1 250 ? 2.04900  -11.39000 35.09400 1.000 66.79496  ?  402 PHE   A CG   1 
ATOM   1889 C  CD1  . PHE   A 1 250 ? 1.36100  -11.52700 36.28900 1.000 73.48919  ?  402 PHE   A CD1  1 
ATOM   1890 C  CD2  . PHE   A 1 250 ? 2.18800  -12.49900 34.27500 1.000 68.83944  ?  402 PHE   A CD2  1 
ATOM   1891 C  CE1  . PHE   A 1 250 ? 0.82600  -12.74700 36.66200 1.000 76.96797  ?  402 PHE   A CE1  1 
ATOM   1892 C  CE2  . PHE   A 1 250 ? 1.65500  -13.72200 34.64300 1.000 73.16937  ?  402 PHE   A CE2  1 
ATOM   1893 C  CZ   . PHE   A 1 250 ? 0.97400  -13.84500 35.83800 1.000 77.09568  ?  402 PHE   A CZ   1 
ATOM   1894 N  N    . GLN   A 1 251 ? 0.50500  -7.53800  34.48500 1.000 55.58603  ?  403 GLN   A N    1 
ATOM   1895 C  CA   . GLN   A 1 251 ? -0.72500 -6.90600  34.94400 1.000 52.83763  ?  403 GLN   A CA   1 
ATOM   1896 C  C    . GLN   A 1 251 ? -1.53700 -6.44900  33.73700 1.000 47.41309  ?  403 GLN   A C    1 
ATOM   1897 O  O    . GLN   A 1 251 ? -1.05700 -5.61600  32.95900 1.000 44.15985  ?  403 GLN   A O    1 
ATOM   1898 C  CB   . GLN   A 1 251 ? -0.41100 -5.73300  35.86000 1.000 58.07701  ?  403 GLN   A CB   1 
ATOM   1899 C  CG   . GLN   A 1 251 ? 0.69100  -6.02200  36.88100 1.000 64.65369  ?  403 GLN   A CG   1 
ATOM   1900 C  CD   . GLN   A 1 251 ? 0.33500  -7.17300  37.80900 1.000 74.85741  ?  403 GLN   A CD   1 
ATOM   1901 O  OE1  . GLN   A 1 251 ? 1.16400  -8.03500  38.10500 1.000 78.40002  ?  403 GLN   A OE1  1 
ATOM   1902 N  NE2  . GLN   A 1 251 ? -0.91100 -7.19300  38.26700 1.000 74.27545  ?  403 GLN   A NE2  1 
ATOM   1903 N  N    . PRO   A 1 252 ? -2.75300 -6.97100  33.53500 1.000 50.91129  ?  404 PRO   A N    1 
ATOM   1904 C  CA   . PRO   A 1 252 ? -3.50500 -6.63100  32.31600 1.000 49.57954  ?  404 PRO   A CA   1 
ATOM   1905 C  C    . PRO   A 1 252 ? -3.76300 -5.14700  32.14700 1.000 49.28125  ?  404 PRO   A C    1 
ATOM   1906 O  O    . PRO   A 1 252 ? -3.82500 -4.67200  31.00700 1.000 49.79432  ?  404 PRO   A O    1 
ATOM   1907 C  CB   . PRO   A 1 252 ? -4.81300 -7.41600  32.48800 1.000 57.03702  ?  404 PRO   A CB   1 
ATOM   1908 C  CG   . PRO   A 1 252 ? -4.43500 -8.58000  33.33700 1.000 61.75446  ?  404 PRO   A CG   1 
ATOM   1909 C  CD   . PRO   A 1 252 ? -3.42700 -8.02200  34.31800 1.000 55.37915  ?  404 PRO   A CD   1 
ATOM   1910 N  N    . GLU   A 1 253 ? -3.91100 -4.39700  33.24300 1.000 55.29159  ?  405 GLU   A N    1 
ATOM   1911 C  CA   . GLU   A 1 253 ? -4.09200 -2.95300  33.12900 1.000 55.02251  ?  405 GLU   A CA   1 
ATOM   1912 C  C    . GLU   A 1 253 ? -2.90900 -2.29600  32.43000 1.000 51.59793  ?  405 GLU   A C    1 
ATOM   1913 O  O    . GLU   A 1 253 ? -3.07500 -1.26700  31.76400 1.000 49.96101  ?  405 GLU   A O    1 
ATOM   1914 C  CB   . GLU   A 1 253 ? -4.29900 -2.33500  34.51300 1.000 61.60722  ?  405 GLU   A CB   1 
ATOM   1915 C  CG   . GLU   A 1 253 ? -5.15900 -3.17000  35.45100 1.000 75.55932  ?  405 GLU   A CG   1 
ATOM   1916 C  CD   . GLU   A 1 253 ? -4.33500 -4.05100  36.36900 1.000 83.91900  ?  405 GLU   A CD   1 
ATOM   1917 O  OE1  . GLU   A 1 253 ? -4.57400 -4.02000  37.59500 1.000 91.15108  ?  405 GLU   A OE1  1 
ATOM   1918 O  OE2  . GLU   A 1 253 ? -3.45100 -4.77600  35.86600 1.000 81.28666  ?  405 GLU   A OE2  1 
ATOM   1919 N  N    . ASN   A 1 254 ? -1.71300 -2.87400  32.56600 1.000 44.77141  ?  406 ASN   A N    1 
ATOM   1920 C  CA   . ASN   A 1 254 ? -0.53500 -2.32400  31.90500 1.000 40.33612  ?  406 ASN   A CA   1 
ATOM   1921 C  C    . ASN   A 1 254 ? -0.45200 -2.77100  30.45100 1.000 38.79958  ?  406 ASN   A C    1 
ATOM   1922 O  O    . ASN   A 1 254 ? -0.16300 -1.96200  29.56200 1.000 41.14870  ?  406 ASN   A O    1 
ATOM   1923 C  CB   . ASN   A 1 254 ? 0.73200  -2.73200  32.65700 1.000 45.32967  ?  406 ASN   A CB   1 
ATOM   1924 C  CG   . ASN   A 1 254 ? 0.92100  -1.95900  33.94400 1.000 54.64763  ?  406 ASN   A CG   1 
ATOM   1925 O  OD1  . ASN   A 1 254 ? 0.33800  -0.89100  34.13100 1.000 54.88104  ?  406 ASN   A OD1  1 
ATOM   1926 N  ND2  . ASN   A 1 254 ? 1.74500  -2.49200  34.84000 1.000 52.64885  ?  406 ASN   A ND2  1 
ATOM   1927 N  N    A SER   A 1 255 ? -0.69200 -4.05800  30.18400 0.440 41.21699  ?  407 SER   A N    1 
ATOM   1928 N  N    B SER   A 1 255 ? -0.68700 -4.06500  30.20000 0.560 40.97863  ?  407 SER   A N    1 
ATOM   1929 C  CA   A SER   A 1 255 ? -0.64300 -4.53700  28.80600 0.440 41.15762  ?  407 SER   A CA   1 
ATOM   1930 C  CA   B SER   A 1 255 ? -0.68900 -4.58400  28.83700 0.560 41.42415  ?  407 SER   A CA   1 
ATOM   1931 C  C    A SER   A 1 255 ? -1.70900 -3.88400  27.93700 0.440 39.92537  ?  407 SER   A C    1 
ATOM   1932 C  C    B SER   A 1 255 ? -1.67900 -3.83900  27.95700 0.560 39.71676  ?  407 SER   A C    1 
ATOM   1933 O  O    A SER   A 1 255 ? -1.55100 -3.83900  26.71200 0.440 39.80325  ?  407 SER   A O    1 
ATOM   1934 O  O    B SER   A 1 255 ? -1.44600 -3.67700  26.75300 0.560 37.16143  ?  407 SER   A O    1 
ATOM   1935 C  CB   A SER   A 1 255 ? -0.79200 -6.05900  28.76400 0.440 44.37779  ?  407 SER   A CB   1 
ATOM   1936 C  CB   B SER   A 1 255 ? -1.02400 -6.07800  28.84600 0.560 45.04907  ?  407 SER   A CB   1 
ATOM   1937 O  OG   A SER   A 1 255 ? -1.90200 -6.48700  29.53100 0.440 49.54070  ?  407 SER   A OG   1 
ATOM   1938 O  OG   B SER   A 1 255 ? 0.14700  -6.87300  28.85100 0.560 48.61300  ?  407 SER   A OG   1 
ATOM   1939 N  N    . MET   A 1 256 ? -2.78400 -3.37100  28.54400 1.000 41.73570  ?  408 MET   A N    1 
ATOM   1940 C  CA   . MET   A 1 256 ? -3.81100 -2.67100  27.78000 1.000 42.66046  ?  408 MET   A CA   1 
ATOM   1941 C  C    . MET   A 1 256 ? -3.28000 -1.39100  27.14900 1.000 47.20398  ?  408 MET   A C    1 
ATOM   1942 O  O    . MET   A 1 256 ? -3.80900 -0.94000  26.12500 1.000 43.17545  ?  408 MET   A O    1 
ATOM   1943 C  CB   . MET   A 1 256 ? -4.99500 -2.34500  28.69000 1.000 42.89278  ?  408 MET   A CB   1 
ATOM   1944 C  CG   . MET   A 1 256 ? -6.23500 -3.17000  28.44600 1.000 52.16763  ?  408 MET   A CG   1 
ATOM   1945 S  SD   . MET   A 1 256 ? -7.44100 -2.87200  29.74600 1.000 56.99765  ?  408 MET   A SD   1 
ATOM   1946 C  CE   . MET   A 1 256 ? -7.40900 -1.08400  29.82700 1.000 56.00188  ?  408 MET   A CE   1 
ATOM   1947 N  N    . LYS   A 1 257 ? -2.25400 -0.78700  27.74600 1.000 36.67951  ?  409 LYS   A N    1 
ATOM   1948 C  CA   . LYS   A 1 257 ? -1.69600 0.46300   27.25000 1.000 35.87328  ?  409 LYS   A CA   1 
ATOM   1949 C  C    . LYS   A 1 257 ? -0.56700 0.25800   26.25000 1.000 33.59611  ?  409 LYS   A C    1 
ATOM   1950 O  O    . LYS   A 1 257 ? -0.10200 1.23800   25.65800 1.000 37.38794  ?  409 LYS   A O    1 
ATOM   1951 C  CB   . LYS   A 1 257 ? -1.19100 1.31900   28.41800 1.000 43.29166  ?  409 LYS   A CB   1 
ATOM   1952 C  CG   . LYS   A 1 257 ? -2.04200 1.22200   29.67000 1.000 54.59256  ?  409 LYS   A CG   1 
ATOM   1953 C  CD   . LYS   A 1 257 ? -3.32200 2.02800   29.52800 1.000 64.02856  ?  409 LYS   A CD   1 
ATOM   1954 C  CE   . LYS   A 1 257 ? -3.02800 3.49300   29.24600 1.000 67.33711  ?  409 LYS   A CE   1 
ATOM   1955 N  NZ   . LYS   A 1 257 ? -4.26900 4.31900   29.18900 1.000 68.83958  ?  409 LYS   A NZ   1 
ATOM   1956 N  N    . LEU   A 1 258 ? -0.12200 -0.97800  26.04400 1.000 33.61368  ?  410 LEU   A N    1 
ATOM   1957 C  CA   . LEU   A 1 258 ? 0.91500  -1.25400  25.06400 1.000 33.78433  ?  410 LEU   A CA   1 
ATOM   1958 C  C    . LEU   A 1 258 ? 0.30600  -1.29300  23.66400 1.000 34.68898  ?  410 LEU   A C    1 
ATOM   1959 O  O    . LEU   A 1 258 ? -0.90500 -1.14800  23.48000 1.000 38.18341  ?  410 LEU   A O    1 
ATOM   1960 C  CB   . LEU   A 1 258 ? 1.62600  -2.56400  25.39800 1.000 34.92546  ?  410 LEU   A CB   1 
ATOM   1961 C  CG   . LEU   A 1 258 ? 2.24100  -2.66800  26.79600 1.000 37.70545  ?  410 LEU   A CG   1 
ATOM   1962 C  CD1  . LEU   A 1 258 ? 2.82600  -4.05500  27.03000 1.000 34.92597  ?  410 LEU   A CD1  1 
ATOM   1963 C  CD2  . LEU   A 1 258 ? 3.30100  -1.59600  27.00300 1.000 37.49995  ?  410 LEU   A CD2  1 
ATOM   1964 N  N    . THR   A 1 259 ? 1.15300  -1.47900  22.65900 1.000 29.95247  ?  411 THR   A N    1 
ATOM   1965 C  CA   . THR   A 1 259 ? 0.67400  -1.61100  21.29200 1.000 34.67698  ?  411 THR   A CA   1 
ATOM   1966 C  C    . THR   A 1 259 ? 0.74500  -3.06400  20.84700 1.000 33.19906  ?  411 THR   A C    1 
ATOM   1967 O  O    . THR   A 1 259 ? 1.45500  -3.87400  21.45000 1.000 32.07517  ?  411 THR   A O    1 
ATOM   1968 C  CB   . THR   A 1 259 ? 1.50000  -0.73300  20.34400 1.000 33.73310  ?  411 THR   A CB   1 
ATOM   1969 O  OG1  . THR   A 1 259 ? 2.77300  -1.34600  20.10500 1.000 37.61539  ?  411 THR   A OG1  1 
ATOM   1970 C  CG2  . THR   A 1 259 ? 1.70900  0.65000   20.94400 1.000 36.10801  ?  411 THR   A CG2  1 
ATOM   1971 N  N    . PRO   A 1 260 ? -0.00600 -3.44000  19.80700 1.000 33.74846  ?  412 PRO   A N    1 
ATOM   1972 C  CA   . PRO   A 1 260 ? 0.08300  -4.82700  19.31700 1.000 32.40076  ?  412 PRO   A CA   1 
ATOM   1973 C  C    . PRO   A 1 260 ? 1.48400  -5.23200  18.89900 1.000 33.83543  ?  412 PRO   A C    1 
ATOM   1974 O  O    . PRO   A 1 260 ? 1.89700  -6.37000  19.15500 1.000 34.16368  ?  412 PRO   A O    1 
ATOM   1975 C  CB   . PRO   A 1 260 ? -0.89000 -4.83200  18.13200 1.000 33.32351  ?  412 PRO   A CB   1 
ATOM   1976 C  CG   . PRO   A 1 260 ? -1.90200 -3.79300  18.49300 1.000 36.59426  ?  412 PRO   A CG   1 
ATOM   1977 C  CD   . PRO   A 1 260 ? -1.10700 -2.70300  19.16000 1.000 36.73842  ?  412 PRO   A CD   1 
ATOM   1978 N  N    . LEU   A 1 261 ? 2.23100  -4.32900  18.25900 1.000 31.09077  ?  413 LEU   A N    1 
ATOM   1979 C  CA   . LEU   A 1 261 ? 3.58600  -4.66400  17.83100 1.000 30.86107  ?  413 LEU   A CA   1 
ATOM   1980 C  C    . LEU   A 1 261 ? 4.50400  -4.88800  19.02500 1.000 29.86419  ?  413 LEU   A C    1 
ATOM   1981 O  O    . LEU   A 1 261 ? 5.33400  -5.80500  19.01000 1.000 34.18301  ?  413 LEU   A O    1 
ATOM   1982 C  CB   . LEU   A 1 261 ? 4.13900  -3.56300  16.92600 1.000 27.45230  ?  413 LEU   A CB   1 
ATOM   1983 C  CG   . LEU   A 1 261 ? 5.53700  -3.81500  16.34800 1.000 34.10047  ?  413 LEU   A CG   1 
ATOM   1984 C  CD1  . LEU   A 1 261 ? 5.54500  -5.05600  15.46600 1.000 35.32405  ?  413 LEU   A CD1  1 
ATOM   1985 C  CD2  . LEU   A 1 261 ? 6.02400  -2.60200  15.57700 1.000 28.52430  ?  413 LEU   A CD2  1 
ATOM   1986 N  N    . VAL   A 1 262 ? 4.36800  -4.06500  20.06800 1.000 27.32072  ?  414 VAL   A N    1 
ATOM   1987 C  CA   . VAL   A 1 262 ? 5.18400  -4.23600  21.26800 1.000 30.68885  ?  414 VAL   A CA   1 
ATOM   1988 C  C    . VAL   A 1 262 ? 4.91700  -5.59500  21.90400 1.000 33.96428  ?  414 VAL   A C    1 
ATOM   1989 O  O    . VAL   A 1 262 ? 5.84700  -6.29800  22.31900 1.000 34.06793  ?  414 VAL   A O    1 
ATOM   1990 C  CB   . VAL   A 1 262 ? 4.92400  -3.08600  22.26000 1.000 31.43208  ?  414 VAL   A CB   1 
ATOM   1991 C  CG1  . VAL   A 1 262 ? 5.48900  -3.41900  23.63400 1.000 31.88184  ?  414 VAL   A CG1  1 
ATOM   1992 C  CG2  . VAL   A 1 262 ? 5.51800  -1.78700  21.73400 1.000 31.35412  ?  414 VAL   A CG2  1 
ATOM   1993 N  N    . LEU   A 1 263 ? 3.64400  -5.99300  21.97600 1.000 32.89714  ?  415 LEU   A N    1 
ATOM   1994 C  CA   . LEU   A 1 263 ? 3.30600  -7.28800  22.55900 1.000 31.87149  ?  415 LEU   A CA   1 
ATOM   1995 C  C    . LEU   A 1 263 ? 3.86400  -8.43500  21.72600 1.000 34.71597  ?  415 LEU   A C    1 
ATOM   1996 O  O    . LEU   A 1 263 ? 4.26900  -9.46700  22.27000 1.000 39.55548  ?  415 LEU   A O    1 
ATOM   1997 C  CB   . LEU   A 1 263 ? 1.78900  -7.42000  22.70100 1.000 32.14666  ?  415 LEU   A CB   1 
ATOM   1998 C  CG   . LEU   A 1 263 ? 1.12300  -6.55400  23.77100 1.000 33.16508  ?  415 LEU   A CG   1 
ATOM   1999 C  CD1  . LEU   A 1 263 ? -0.37900 -6.49300  23.54000 1.000 33.85121  ?  415 LEU   A CD1  1 
ATOM   2000 C  CD2  . LEU   A 1 263 ? 1.43300  -7.08800  25.16000 1.000 34.09000  ?  415 LEU   A CD2  1 
ATOM   2001 N  N    . GLU   A 1 264 ? 3.88700  -8.27700  20.40200 1.000 34.19358  ?  416 GLU   A N    1 
ATOM   2002 C  CA   . GLU   A 1 264 ? 4.42800  -9.33400  19.55300 1.000 39.93475  ?  416 GLU   A CA   1 
ATOM   2003 C  C    . GLU   A 1 264 ? 5.94100  -9.43400  19.69500 1.000 38.42414  ?  416 GLU   A C    1 
ATOM   2004 O  O    . GLU   A 1 264 ? 6.49200  -10.53700 19.78300 1.000 39.95288  ?  416 GLU   A O    1 
ATOM   2005 C  CB   . GLU   A 1 264 ? 4.04400  -9.08400  18.09500 1.000 45.12457  ?  416 GLU   A CB   1 
ATOM   2006 C  CG   . GLU   A 1 264 ? 4.13100  -10.31600 17.21300 1.000 49.90240  ?  416 GLU   A CG   1 
ATOM   2007 C  CD   . GLU   A 1 264 ? 3.86500  -10.00400 15.75500 1.000 46.14595  ?  416 GLU   A CD   1 
ATOM   2008 O  OE1  . GLU   A 1 264 ? 4.83800  -9.76100  15.01100 1.000 44.76328  ?  416 GLU   A OE1  1 
ATOM   2009 O  OE2  . GLU   A 1 264 ? 2.68400  -10.00300 15.35400 1.000 46.77091  ?  416 GLU   A OE2  1 
ATOM   2010 N  N    . VAL   A 1 265 ? 6.62700  -8.29300  19.73300 1.000 31.91016  ?  417 VAL   A N    1 
ATOM   2011 C  CA   . VAL   A 1 265 ? 8.08500  -8.30300  19.73700 1.000 31.41961  ?  417 VAL   A CA   1 
ATOM   2012 C  C    . VAL   A 1 265 ? 8.62400  -8.57000  21.13700 1.000 42.94216  ?  417 VAL   A C    1 
ATOM   2013 O  O    . VAL   A 1 265 ? 9.46500  -9.45400  21.33500 1.000 43.50629  ?  417 VAL   A O    1 
ATOM   2014 C  CB   . VAL   A 1 265 ? 8.62700  -6.98000  19.16500 1.000 29.82480  ?  417 VAL   A CB   1 
ATOM   2015 C  CG1  . VAL   A 1 265 ? 10.14300 -6.89400  19.35400 1.000 30.52894  ?  417 VAL   A CG1  1 
ATOM   2016 C  CG2  . VAL   A 1 265 ? 8.25700  -6.84900  17.69900 1.000 32.77844  ?  417 VAL   A CG2  1 
ATOM   2017 N  N    . PHE   A 1 266 ? 8.15200  -7.81100  22.12800 1.000 39.20642  ?  418 PHE   A N    1 
ATOM   2018 C  CA   . PHE   A 1 266 ? 8.69000  -7.93200  23.47800 1.000 40.63730  ?  418 PHE   A CA   1 
ATOM   2019 C  C    . PHE   A 1 266 ? 8.06200  -9.07300  24.26800 1.000 44.27193  ?  418 PHE   A C    1 
ATOM   2020 O  O    . PHE   A 1 266 ? 8.68500  -9.56800  25.21200 1.000 45.92896  ?  418 PHE   A O    1 
ATOM   2021 C  CB   . PHE   A 1 266 ? 8.50600  -6.61800  24.24100 1.000 36.73979  ?  418 PHE   A CB   1 
ATOM   2022 C  CG   . PHE   A 1 266 ? 9.38900  -5.50200  23.75600 1.000 33.79154  ?  418 PHE   A CG   1 
ATOM   2023 C  CD1  . PHE   A 1 266 ? 9.19500  -4.20700  24.20800 1.000 34.88544  ?  418 PHE   A CD1  1 
ATOM   2024 C  CD2  . PHE   A 1 266 ? 10.41200 -5.74600  22.85200 1.000 37.80147  ?  418 PHE   A CD2  1 
ATOM   2025 C  CE1  . PHE   A 1 266 ? 10.00300 -3.17600  23.76800 1.000 40.18543  ?  418 PHE   A CE1  1 
ATOM   2026 C  CE2  . PHE   A 1 266 ? 11.22400 -4.72000  22.40700 1.000 40.84853  ?  418 PHE   A CE2  1 
ATOM   2027 C  CZ   . PHE   A 1 266 ? 11.02100 -3.43300  22.86500 1.000 41.46996  ?  418 PHE   A CZ   1 
ATOM   2028 N  N    . GLY   A 1 267 ? 6.85400  -9.49600  23.91200 1.000 42.85345  ?  419 GLY   A N    1 
ATOM   2029 C  CA   . GLY   A 1 267 ? 6.19300  -10.59400 24.59600 1.000 45.01856  ?  419 GLY   A CA   1 
ATOM   2030 C  C    . GLY   A 1 267 ? 4.82200  -10.20600 25.11400 1.000 49.45616  ?  419 GLY   A C    1 
ATOM   2031 O  O    . GLY   A 1 267 ? 4.54300  -9.03700  25.39300 1.000 43.33583  ?  419 GLY   A O    1 
ATOM   2032 N  N    . ASN   A 1 268 ? 3.94900  -11.20100 25.23700 1.000 54.10621  ?  420 ASN   A N    1 
ATOM   2033 C  CA   . ASN   A 1 268 ? 2.60500  -10.98300 25.75900 1.000 60.22057  ?  420 ASN   A CA   1 
ATOM   2034 C  C    . ASN   A 1 268 ? 2.47900  -11.60400 27.14800 1.000 63.61947  ?  420 ASN   A C    1 
ATOM   2035 O  O    . ASN   A 1 268 ? 2.75500  -12.78900 27.33800 1.000 66.14547  ?  420 ASN   A O    1 
ATOM   2036 C  CB   . ASN   A 1 268 ? 1.55600  -11.57000 24.80900 1.000 67.14382  ?  420 ASN   A CB   1 
ATOM   2037 C  CG   . ASN   A 1 268 ? 0.19300  -10.91100 24.95600 1.000 71.76111  ?  420 ASN   A CG   1 
ATOM   2038 O  OD1  . ASN   A 1 268 ? -0.54000 -10.75900 23.97800 1.000 74.21910  ?  420 ASN   A OD1  1 
ATOM   2039 N  ND2  . ASN   A 1 268 ? -0.15600 -10.52300 26.17800 1.000 72.66746  ?  420 ASN   A ND2  1 
ATOM   2040 N  N    . ASN   B 2 2   ? 2.48900  -16.83200 14.05500 1.000 92.29023  ?  626 ASN   C N    1 
ATOM   2041 C  CA   . ASN   B 2 2   ? 3.02400  -16.55900 15.38500 1.000 89.94609  ?  626 ASN   C CA   1 
ATOM   2042 C  C    . ASN   B 2 2   ? 3.39200  -15.09500 15.53400 1.000 78.77216  ?  626 ASN   C C    1 
ATOM   2043 O  O    . ASN   B 2 2   ? 2.95600  -14.42200 16.47000 1.000 79.26264  ?  626 ASN   C O    1 
ATOM   2044 C  CB   . ASN   B 2 2   ? 4.23700  -17.44800 15.66600 1.000 95.00142  ?  626 ASN   C CB   1 
ATOM   2045 C  CG   . ASN   B 2 2   ? 4.47400  -17.65700 17.14700 1.000 99.67119  ?  626 ASN   C CG   1 
ATOM   2046 O  OD1  . ASN   B 2 2   ? 3.59700  -17.39300 17.96900 1.000 100.17673 ?  626 ASN   C OD1  1 
ATOM   2047 N  ND2  . ASN   B 2 2   ? 5.65900  -18.14600 17.49500 1.000 102.05086 ?  626 ASN   C ND2  1 
ATOM   2048 N  N    . HIS   B 2 3   ? 4.19500  -14.58200 14.60400 1.000 66.35982  ?  627 HIS   C N    1 
ATOM   2049 C  CA   . HIS   B 2 3   ? 4.59900  -13.17600 14.57300 1.000 57.34917  ?  627 HIS   C CA   1 
ATOM   2050 C  C    . HIS   B 2 3   ? 4.15500  -12.55500 13.25100 1.000 52.35028  ?  627 HIS   C C    1 
ATOM   2051 O  O    . HIS   B 2 3   ? 4.99200  -12.21600 12.40400 1.000 52.70209  ?  627 HIS   C O    1 
ATOM   2052 C  CB   . HIS   B 2 3   ? 6.10900  -13.02800 14.75600 1.000 54.03677  ?  627 HIS   C CB   1 
ATOM   2053 C  CG   . HIS   B 2 3   ? 6.63900  -13.70700 15.98100 1.000 55.02940  ?  627 HIS   C CG   1 
ATOM   2054 N  ND1  . HIS   B 2 3   ? 7.11400  -15.00100 15.97200 1.000 58.74186  ?  627 HIS   C ND1  1 
ATOM   2055 C  CD2  . HIS   B 2 3   ? 6.77000  -13.26800 17.25600 1.000 55.21976  ?  627 HIS   C CD2  1 
ATOM   2056 C  CE1  . HIS   B 2 3   ? 7.51600  -15.32900 17.18800 1.000 57.44176  ?  627 HIS   C CE1  1 
ATOM   2057 N  NE2  . HIS   B 2 3   ? 7.31500  -14.29700 17.98600 1.000 55.65581  ?  627 HIS   C NE2  1 
ATOM   2058 N  N    . PRO   B 2 4   ? 2.84500  -12.37800 13.04700 1.000 52.35590  ?  628 PRO   C N    1 
ATOM   2059 C  CA   . PRO   B 2 4   ? 2.37700  -11.88900 11.73900 1.000 50.51893  ?  628 PRO   C CA   1 
ATOM   2060 C  C    . PRO   B 2 4   ? 2.73800  -10.44100 11.46100 1.000 47.58495  ?  628 PRO   C C    1 
ATOM   2061 O  O    . PRO   B 2 4   ? 2.96100  -10.09000 10.29600 1.000 47.35298  ?  628 PRO   C O    1 
ATOM   2062 C  CB   . PRO   B 2 4   ? 0.85700  -12.08600 11.81500 1.000 52.55806  ?  628 PRO   C CB   1 
ATOM   2063 C  CG   . PRO   B 2 4   ? 0.55100  -12.03800 13.26800 1.000 55.02965  ?  628 PRO   C CG   1 
ATOM   2064 C  CD   . PRO   B 2 4   ? 1.72400  -12.66100 13.96200 1.000 54.84384  ?  628 PRO   C CD   1 
ATOM   2065 N  N    . MET   B 2 5   ? 2.79600  -9.58500  12.48400 1.000 48.66603  ?  629 MET   C N    1 
ATOM   2066 C  CA   . MET   B 2 5   ? 3.12800  -8.18500  12.24000 1.000 43.80191  ?  629 MET   C CA   1 
ATOM   2067 C  C    . MET   B 2 5   ? 4.61200  -8.01400  11.93700 1.000 48.79354  ?  629 MET   C C    1 
ATOM   2068 O  O    . MET   B 2 5   ? 4.98400  -7.25300  11.03700 1.000 41.91518  ?  629 MET   C O    1 
ATOM   2069 C  CB   . MET   B 2 5   ? 2.71000  -7.32600  13.43400 1.000 43.14491  ?  629 MET   C CB   1 
ATOM   2070 C  CG   . MET   B 2 5   ? 1.19800  -7.14300  13.55100 1.000 52.12903  ?  629 MET   C CG   1 
ATOM   2071 S  SD   . MET   B 2 5   ? 0.66900  -6.30800  15.06300 1.000 55.45991  ?  629 MET   C SD   1 
ATOM   2072 C  CE   . MET   B 2 5   ? 0.77300  -7.63800  16.25600 1.000 57.24946  ?  629 MET   C CE   1 
ATOM   2073 N  N    . LEU   B 2 6   ? 5.47300  -8.71300  12.68200 1.000 44.98552  ?  630 LEU   C N    1 
ATOM   2074 C  CA   . LEU   B 2 6   ? 6.89700  -8.72800  12.36200 1.000 43.45572  ?  630 LEU   C CA   1 
ATOM   2075 C  C    . LEU   B 2 6   ? 7.14300  -9.31900  10.98000 1.000 43.93504  ?  630 LEU   C C    1 
ATOM   2076 O  O    . LEU   B 2 6   ? 7.96300  -8.80300  10.21000 1.000 45.19605  ?  630 LEU   C O    1 
ATOM   2077 C  CB   . LEU   B 2 6   ? 7.65200  -9.52300  13.42800 1.000 46.89781  ?  630 LEU   C CB   1 
ATOM   2078 C  CG   . LEU   B 2 6   ? 9.18000  -9.51500  13.43900 1.000 55.00853  ?  630 LEU   C CG   1 
ATOM   2079 C  CD1  . LEU   B 2 6   ? 9.73900  -8.16700  13.00600 1.000 54.14140  ?  630 LEU   C CD1  1 
ATOM   2080 C  CD2  . LEU   B 2 6   ? 9.69000  -9.89900  14.82100 1.000 54.90371  ?  630 LEU   C CD2  1 
ATOM   2081 N  N    A MET   B 2 7   ? 6.44800  -10.41300 10.65900 0.520 46.13357  ?  631 MET   C N    1 
ATOM   2082 N  N    B MET   B 2 7   ? 6.43900  -10.40200 10.64200 0.480 46.23403  ?  631 MET   C N    1 
ATOM   2083 C  CA   A MET   B 2 7   ? 6.57900  -11.04600 9.35000  0.520 49.05670  ?  631 MET   C CA   1 
ATOM   2084 C  CA   B MET   B 2 7   ? 6.62800  -11.02500 9.33500  0.480 48.98280  ?  631 MET   C CA   1 
ATOM   2085 C  C    A MET   B 2 7   ? 6.21100  -10.08100 8.23100  0.520 47.60018  ?  631 MET   C C    1 
ATOM   2086 C  C    B MET   B 2 7   ? 6.20400  -10.09100 8.20800  0.480 47.68735  ?  631 MET   C C    1 
ATOM   2087 O  O    A MET   B 2 7   ? 6.93000  -9.96400  7.23200  0.520 47.94038  ?  631 MET   C O    1 
ATOM   2088 O  O    B MET   B 2 7   ? 6.88100  -10.00600 7.17600  0.480 48.08710  ?  631 MET   C O    1 
ATOM   2089 C  CB   A MET   B 2 7   ? 5.69300  -12.29000 9.29400  0.520 55.20492  ?  631 MET   C CB   1 
ATOM   2090 C  CB   B MET   B 2 7   ? 5.85600  -12.34100 9.25900  0.480 55.23750  ?  631 MET   C CB   1 
ATOM   2091 C  CG   A MET   B 2 7   ? 5.74200  -13.05100 7.98400  0.520 63.65051  ?  631 MET   C CG   1 
ATOM   2092 C  CG   B MET   B 2 7   ? 6.73600  -13.57000 9.08200  0.480 63.85805  ?  631 MET   C CG   1 
ATOM   2093 S  SD   A MET   B 2 7   ? 5.94500  -14.81900 8.25500  0.520 72.88205  ?  631 MET   C SD   1 
ATOM   2094 S  SD   B MET   B 2 7   ? 5.80200  -15.03500 8.59900  0.480 72.16868  ?  631 MET   C SD   1 
ATOM   2095 C  CE   A MET   B 2 7   ? 7.70500  -14.88700 8.54800  0.520 68.77398  ?  631 MET   C CE   1 
ATOM   2096 C  CE   B MET   B 2 7   ? 5.05000  -15.48900 10.15900 0.480 71.96779  ?  631 MET   C CE   1 
ATOM   2097 N  N    . ASN   B 2 8   ? 5.08500  -9.38200  8.38400  1.000 46.39849  ?  632 ASN   C N    1 
ATOM   2098 C  CA   . ASN   B 2 8   ? 4.62400  -8.47100  7.34000  1.000 46.66404  ?  632 ASN   C CA   1 
ATOM   2099 C  C    . ASN   B 2 8   ? 5.58900  -7.30700  7.14600  1.000 46.09319  ?  632 ASN   C C    1 
ATOM   2100 O  O    . ASN   B 2 8   ? 5.83200  -6.87700  6.01300  1.000 47.73375  ?  632 ASN   C O    1 
ATOM   2101 C  CB   . ASN   B 2 8   ? 3.22500  -7.95500  7.67400  1.000 46.61766  ?  632 ASN   C CB   1 
ATOM   2102 C  CG   . ASN   B 2 8   ? 2.73500  -6.92200  6.68100  1.000 54.43252  ?  632 ASN   C CG   1 
ATOM   2103 O  OD1  . ASN   B 2 8   ? 2.74700  -5.72300  6.95800  1.000 55.18300  ?  632 ASN   C OD1  1 
ATOM   2104 N  ND2  . ASN   B 2 8   ? 2.30000  -7.38300  5.51400  1.000 58.93239  ?  632 ASN   C ND2  1 
ATOM   2105 N  N    A LEU   B 2 9   ? 6.15100  -6.78600  8.24000  0.550 43.23965  ?  633 LEU   C N    1 
ATOM   2106 N  N    B LEU   B 2 9   ? 6.14400  -6.77900  8.24000  0.450 43.23637  ?  633 LEU   C N    1 
ATOM   2107 C  CA   A LEU   B 2 9   ? 7.11000  -5.69500  8.13100  0.550 42.36720  ?  633 LEU   C CA   1 
ATOM   2108 C  CA   B LEU   B 2 9   ? 7.10900  -5.69300  8.13000  0.450 42.36744  ?  633 LEU   C CA   1 
ATOM   2109 C  C    A LEU   B 2 9   ? 8.44000  -6.15300  7.55000  0.550 43.25399  ?  633 LEU   C C    1 
ATOM   2110 C  C    B LEU   B 2 9   ? 8.43000  -6.15500  7.52900  0.450 43.28241  ?  633 LEU   C C    1 
ATOM   2111 O  O    A LEU   B 2 9   ? 9.18600  -5.32600  7.01300  0.550 44.01781  ?  633 LEU   C O    1 
ATOM   2112 O  O    B LEU   B 2 9   ? 9.15700  -5.33600  6.95600  0.450 44.08289  ?  633 LEU   C O    1 
ATOM   2113 C  CB   A LEU   B 2 9   ? 7.32800  -5.04500  9.49900  0.550 40.60173  ?  633 LEU   C CB   1 
ATOM   2114 C  CB   B LEU   B 2 9   ? 7.34600  -5.06300  9.50400  0.450 40.60188  ?  633 LEU   C CB   1 
ATOM   2115 C  CG   A LEU   B 2 9   ? 6.12600  -4.28500  10.06900 0.550 41.46442  ?  633 LEU   C CG   1 
ATOM   2116 C  CG   B LEU   B 2 9   ? 6.14100  -4.33900  10.10700 0.450 41.36132  ?  633 LEU   C CG   1 
ATOM   2117 C  CD1  A LEU   B 2 9   ? 6.41400  -3.79400  11.48000 0.550 40.39581  ?  633 LEU   C CD1  1 
ATOM   2118 C  CD1  B LEU   B 2 9   ? 6.51700  -3.64600  11.40700 0.450 40.12867  ?  633 LEU   C CD1  1 
ATOM   2119 C  CD2  A LEU   B 2 9   ? 5.74500  -3.12700  9.16000  0.550 41.62778  ?  633 LEU   C CD2  1 
ATOM   2120 C  CD2  B LEU   B 2 9   ? 5.56100  -3.34300  9.11100  0.450 41.28843  ?  633 LEU   C CD2  1 
ATOM   2121 N  N    . LEU   B 2 10  ? 8.75100  -7.44500  7.64100  1.000 44.19060  ?  634 LEU   C N    1 
ATOM   2122 C  CA   . LEU   B 2 10  ? 9.97500  -7.98800  7.07100  1.000 48.65597  ?  634 LEU   C CA   1 
ATOM   2123 C  C    . LEU   B 2 10  ? 9.82700  -8.36900  5.60700  1.000 52.32018  ?  634 LEU   C C    1 
ATOM   2124 O  O    . LEU   B 2 10  ? 10.84200 -8.60100  4.94000  1.000 51.31978  ?  634 LEU   C O    1 
ATOM   2125 C  CB   . LEU   B 2 10  ? 10.43400 -9.21300  7.86700  1.000 48.37603  ?  634 LEU   C CB   1 
ATOM   2126 C  CG   . LEU   B 2 10  ? 11.21100 -8.89600  9.14100  1.000 46.15251  ?  634 LEU   C CG   1 
ATOM   2127 C  CD1  . LEU   B 2 10  ? 11.48800 -10.15900 9.94300  1.000 48.91132  ?  634 LEU   C CD1  1 
ATOM   2128 C  CD2  . LEU   B 2 10  ? 12.50100 -8.18400  8.77500  1.000 49.95975  ?  634 LEU   C CD2  1 
ATOM   2129 N  N    . LYS   B 2 11  ? 8.59900  -8.43900  5.10000  1.000 52.91378  ?  635 LYS   C N    1 
ATOM   2130 C  CA   . LYS   B 2 11  ? 8.33400  -8.79800  3.71200  1.000 61.73421  ?  635 LYS   C CA   1 
ATOM   2131 C  C    . LYS   B 2 11  ? 9.01000  -7.84000  2.73600  1.000 67.13550  ?  635 LYS   C C    1 
ATOM   2132 O  O    . LYS   B 2 11  ? 8.74300  -6.63900  2.74600  1.000 70.24637  ?  635 LYS   C O    1 
ATOM   2133 C  CB   . LYS   B 2 11  ? 6.82600  -8.82200  3.45700  1.000 65.60064  ?  635 LYS   C CB   1 
ATOM   2134 C  CG   . LYS   B 2 11  ? 6.37100  -9.87000  2.45800  1.000 72.10738  ?  635 LYS   C CG   1 
ATOM   2135 C  CD   . LYS   B 2 11  ? 4.92800  -9.63200  2.04200  0.840 72.95694  ?  635 LYS   C CD   1 
ATOM   2136 C  CE   . LYS   B 2 11  ? 4.67200  -10.12800 0.63000  1.000 75.85014  ?  635 LYS   C CE   1 
ATOM   2137 N  NZ   . LYS   B 2 11  ? 4.76100  -9.02500  -0.36500 0.970 78.50304  ?  635 LYS   C NZ   1 
HETATM 2138 C  C10  . A1L79 C 3 .   ? 15.81100 4.91800   26.16700 1.000 36.38813  ?  501 A1L79 A C10  1 
HETATM 2139 C  C13  . A1L79 C 3 .   ? 12.44600 2.29100   27.83600 1.000 50.38670  ?  501 A1L79 A C13  1 
HETATM 2140 C  C15  . A1L79 C 3 .   ? 10.62900 3.31800   26.76200 1.000 41.71157  ?  501 A1L79 A C15  1 
HETATM 2141 C  C20  . A1L79 C 3 .   ? 7.76500  -0.96700  26.84500 1.000 40.76883  ?  501 A1L79 A C20  1 
HETATM 2142 C  C21  . A1L79 C 3 .   ? 7.01000  0.07600   26.05900 1.000 42.94977  ?  501 A1L79 A C21  1 
HETATM 2143 C  C22  . A1L79 C 3 .   ? 7.60600  0.08900   29.09900 1.000 43.24507  ?  501 A1L79 A C22  1 
HETATM 2144 C  C26  . A1L79 C 3 .   ? 14.51500 8.04900   18.16200 1.000 48.86420  ?  501 A1L79 A C26  1 
HETATM 2145 C  C28  . A1L79 C 3 .   ? 13.41900 7.58400   17.18100 1.000 42.92831  ?  501 A1L79 A C28  1 
HETATM 2146 C  C01  . A1L79 C 3 .   ? 14.13100 7.92600   22.47200 1.000 37.95205  ?  501 A1L79 A C01  1 
HETATM 2147 C  C02  . A1L79 C 3 .   ? 13.62500 7.04400   21.55600 1.000 38.42793  ?  501 A1L79 A C02  1 
HETATM 2148 C  C03  . A1L79 C 3 .   ? 13.24200 5.79000   21.97300 1.000 36.83092  ?  501 A1L79 A C03  1 
HETATM 2149 C  C04  . A1L79 C 3 .   ? 13.37800 5.37600   23.27300 1.000 35.87455  ?  501 A1L79 A C04  1 
HETATM 2150 C  C05  . A1L79 C 3 .   ? 13.87600 6.24500   24.19400 1.000 34.59386  ?  501 A1L79 A C05  1 
HETATM 2151 C  C06  . A1L79 C 3 .   ? 14.24700 7.50000   23.78900 1.000 36.79221  ?  501 A1L79 A C06  1 
HETATM 2152 C  C09  . A1L79 C 3 .   ? 12.81000 4.32400   26.59100 1.000 44.51307  ?  501 A1L79 A C09  1 
HETATM 2153 C  C11  . A1L79 C 3 .   ? 14.13600 7.17600   27.13100 1.000 43.37509  ?  501 A1L79 A C11  1 
HETATM 2154 C  C12  . A1L79 C 3 .   ? 13.27800 3.30400   27.36700 1.000 46.09255  ?  501 A1L79 A C12  1 
HETATM 2155 C  C14  . A1L79 C 3 .   ? 11.11200 2.28800   27.51600 1.000 42.42908  ?  501 A1L79 A C14  1 
HETATM 2156 C  C16  . A1L79 C 3 .   ? 11.46900 4.33300   26.28300 1.000 48.82942  ?  501 A1L79 A C16  1 
HETATM 2157 C  C18  . A1L79 C 3 .   ? 9.16000  0.93000   27.35100 1.000 45.35116  ?  501 A1L79 A C18  1 
HETATM 2158 C  C19  . A1L79 C 3 .   ? 8.52700  -0.31400  27.97200 1.000 37.67618  ?  501 A1L79 A C19  1 
HETATM 2159 C  C23  . A1L79 C 3 .   ? 6.76600  -1.10100  29.50400 1.000 41.26917  ?  501 A1L79 A C23  1 
HETATM 2160 C  C25  . A1L79 C 3 .   ? 14.11600 8.38100   19.58600 1.000 54.23418  ?  501 A1L79 A C25  1 
HETATM 2161 C  C29  . A1L79 C 3 .   ? 13.52600 8.37400   15.87400 1.000 41.69847  ?  501 A1L79 A C29  1 
HETATM 2162 C  C30  . A1L79 C 3 .   ? 13.36500 7.58500   14.55600 1.000 45.87211  ?  501 A1L79 A C30  1 
HETATM 2163 C  C33  . A1L79 C 3 .   ? 12.68400 4.82000   20.97100 1.000 37.66295  ?  501 A1L79 A C33  1 
HETATM 2164 C  C34  . A1L79 C 3 .   ? 13.03900 1.19600   28.69500 1.000 54.05583  ?  501 A1L79 A C34  1 
HETATM 2165 C  C35  . A1L79 C 3 .   ? 12.75000 7.48500   27.61800 1.000 51.19552  ?  501 A1L79 A C35  1 
HETATM 2166 C  C36  . A1L79 C 3 .   ? 12.03500 7.95600   26.37200 1.000 53.56438  ?  501 A1L79 A C36  1 
HETATM 2167 C  C37  . A1L79 C 3 .   ? 16.18500 4.12700   24.93300 1.000 37.22756  ?  501 A1L79 A C37  1 
HETATM 2168 C  C38  . A1L79 C 3 .   ? 15.73200 2.69300   25.11700 1.000 38.03687  ?  501 A1L79 A C38  1 
HETATM 2169 O  O07  . A1L79 C 3 .   ? 13.43400 7.34800   20.19500 1.000 46.21664  ?  501 A1L79 A O07  1 
HETATM 2170 O  O17  . A1L79 C 3 .   ? 10.30500 1.26100   28.02200 1.000 48.67718  ?  501 A1L79 A O17  1 
HETATM 2171 O  O24  . A1L79 C 3 .   ? 9.40100  -1.25100  28.47000 1.000 39.60488  ?  501 A1L79 A O24  1 
HETATM 2172 O  O27  . A1L79 C 3 .   ? 15.42700 7.05800   18.28400 1.000 50.45106  ?  501 A1L79 A O27  1 
HETATM 2173 O  O31  . A1L79 C 3 .   ? 13.72000 6.41600   14.51800 1.000 42.66822  ?  501 A1L79 A O31  1 
HETATM 2174 O  O32  . A1L79 C 3 .   ? 12.92000 8.12000   13.51600 1.000 38.27921  -1 501 A1L79 A O32  1 
HETATM 2175 SI SI08 . A1L79 C 3 .   ? 14.07300 5.66500   26.00400 1.000 37.56789  ?  501 A1L79 A SI08 1 
HETATM 2176 O  O    . HOH   D 4 .   ? 3.52400  0.46000   16.10200 1.000 42.25281  ?  601 HOH   A O    1 
HETATM 2177 O  O    . HOH   D 4 .   ? 35.09500 -9.45400  16.84300 1.000 56.75479  ?  602 HOH   A O    1 
HETATM 2178 O  O    . HOH   D 4 .   ? 11.49900 -19.52900 7.86700  1.000 61.78582  ?  603 HOH   A O    1 
HETATM 2179 O  O    . HOH   D 4 .   ? 18.62200 3.32400   -1.03500 1.000 47.55581  ?  604 HOH   A O    1 
HETATM 2180 O  O    . HOH   D 4 .   ? 13.74400 -6.84100  26.54100 1.000 48.39424  ?  605 HOH   A O    1 
HETATM 2181 O  O    . HOH   D 4 .   ? 17.85000 12.14500  32.85700 1.000 43.35863  ?  606 HOH   A O    1 
HETATM 2182 O  O    . HOH   D 4 .   ? 0.85600  -10.92200 16.64600 1.000 63.67449  ?  607 HOH   A O    1 
HETATM 2183 O  O    . HOH   D 4 .   ? 16.08700 -4.11300  43.29800 1.000 55.22105  ?  608 HOH   A O    1 
HETATM 2184 O  O    . HOH   D 4 .   ? 30.15900 10.26100  6.49700  1.000 66.97154  ?  609 HOH   A O    1 
HETATM 2185 O  O    . HOH   D 4 .   ? 18.04800 -23.02400 7.34300  1.000 71.06606  ?  610 HOH   A O    1 
HETATM 2186 O  O    . HOH   D 4 .   ? 32.84600 0.35100   25.94600 1.000 45.54483  ?  611 HOH   A O    1 
HETATM 2187 O  O    . HOH   D 4 .   ? 36.46500 -7.21600  1.24600  1.000 53.06640  ?  612 HOH   A O    1 
HETATM 2188 O  O    . HOH   D 4 .   ? 9.01200  13.25800  33.91600 1.000 72.63272  ?  613 HOH   A O    1 
HETATM 2189 O  O    . HOH   D 4 .   ? 25.33400 6.18700   1.67500  1.000 46.93079  ?  614 HOH   A O    1 
HETATM 2190 O  O    . HOH   D 4 .   ? 19.82600 -10.14700 17.07400 1.000 40.75701  ?  615 HOH   A O    1 
HETATM 2191 O  O    . HOH   D 4 .   ? 42.39400 1.01100   16.79400 1.000 43.63728  ?  616 HOH   A O    1 
HETATM 2192 O  O    . HOH   D 4 .   ? 29.63800 11.46300  17.48400 1.000 55.21166  ?  617 HOH   A O    1 
HETATM 2193 O  O    A HOH   D 4 .   ? 33.25700 5.45300   26.42000 0.630 29.45843  ?  618 HOH   A O    1 
HETATM 2194 O  O    B HOH   D 4 .   ? 34.06500 2.93200   26.38600 0.370 24.29922  ?  618 HOH   A O    1 
HETATM 2195 O  O    . HOH   D 4 .   ? 18.14300 2.01300   13.66300 1.000 43.28970  ?  619 HOH   A O    1 
HETATM 2196 O  O    . HOH   D 4 .   ? 10.80300 -9.17400  26.65900 1.000 46.09350  ?  620 HOH   A O    1 
HETATM 2197 O  O    . HOH   D 4 .   ? 19.58300 -20.76500 6.63400  1.000 61.70633  ?  621 HOH   A O    1 
HETATM 2198 O  O    . HOH   D 4 .   ? 27.94900 -10.15700 18.26200 1.000 44.96962  ?  622 HOH   A O    1 
HETATM 2199 O  O    . HOH   D 4 .   ? -1.11000 3.10900   20.26000 1.000 38.06993  ?  623 HOH   A O    1 
HETATM 2200 O  O    . HOH   D 4 .   ? 29.13800 7.90700   19.93400 1.000 32.38997  ?  624 HOH   A O    1 
HETATM 2201 O  O    . HOH   D 4 .   ? 24.51100 -7.11800  21.91800 1.000 32.25769  ?  625 HOH   A O    1 
HETATM 2202 O  O    . HOH   D 4 .   ? 27.30800 -9.13200  5.98000  1.000 46.73530  ?  626 HOH   A O    1 
HETATM 2203 O  O    . HOH   D 4 .   ? 27.01700 -9.27800  28.20600 1.000 34.74160  ?  627 HOH   A O    1 
HETATM 2204 O  O    . HOH   D 4 .   ? 36.73800 7.54000   20.60600 1.000 47.08110  ?  628 HOH   A O    1 
HETATM 2205 O  O    . HOH   D 4 .   ? 34.43500 5.51300   4.35200  1.000 68.15965  ?  629 HOH   A O    1 
HETATM 2206 O  O    . HOH   D 4 .   ? 18.69400 10.67900  9.25000  1.000 47.46382  ?  630 HOH   A O    1 
HETATM 2207 O  O    . HOH   D 4 .   ? -0.86500 13.48800  20.75800 1.000 60.24564  ?  631 HOH   A O    1 
HETATM 2208 O  O    . HOH   D 4 .   ? 19.29900 -7.51000  3.25900  1.000 46.26705  ?  632 HOH   A O    1 
HETATM 2209 O  O    . HOH   D 4 .   ? 9.19900  -1.03600  9.13200  1.000 57.26690  ?  633 HOH   A O    1 
HETATM 2210 O  O    . HOH   D 4 .   ? 30.89600 -1.98400  30.47100 1.000 51.30746  ?  634 HOH   A O    1 
HETATM 2211 O  O    . HOH   D 4 .   ? 13.89700 -6.74100  21.85500 1.000 46.29813  ?  635 HOH   A O    1 
HETATM 2212 O  O    A HOH   D 4 .   ? 20.90300 11.45400  11.14600 0.530 42.54012  ?  636 HOH   A O    1 
HETATM 2213 O  O    B HOH   D 4 .   ? 22.95700 10.14100  11.58600 0.470 40.66308  ?  636 HOH   A O    1 
HETATM 2214 O  O    . HOH   D 4 .   ? 30.20400 -19.19000 9.85100  1.000 53.78178  ?  637 HOH   A O    1 
HETATM 2215 O  O    . HOH   D 4 .   ? 2.77300  12.92500  21.31800 1.000 41.97691  ?  638 HOH   A O    1 
HETATM 2216 O  O    . HOH   D 4 .   ? 10.83000 15.34800  31.22800 1.000 55.52142  ?  639 HOH   A O    1 
HETATM 2217 O  O    . HOH   D 4 .   ? 31.42300 -11.30600 13.89500 1.000 48.81099  ?  640 HOH   A O    1 
HETATM 2218 O  O    . HOH   D 4 .   ? 20.71200 6.91500   15.68300 1.000 31.85154  ?  641 HOH   A O    1 
HETATM 2219 O  O    . HOH   D 4 .   ? 1.76200  9.09100   28.33400 1.000 41.25464  ?  642 HOH   A O    1 
HETATM 2220 O  O    . HOH   D 4 .   ? -6.18200 -1.74600  24.96600 1.000 30.24753  ?  643 HOH   A O    1 
HETATM 2221 O  O    . HOH   D 4 .   ? 9.57900  11.60200  12.96600 1.000 47.15586  ?  644 HOH   A O    1 
HETATM 2222 O  O    . HOH   D 4 .   ? 35.79100 -5.44500  -3.04700 1.000 60.21056  ?  645 HOH   A O    1 
HETATM 2223 O  O    . HOH   D 4 .   ? 11.80500 10.56100  14.23300 1.000 43.33833  ?  646 HOH   A O    1 
HETATM 2224 O  O    . HOH   D 4 .   ? -1.41000 8.10100   15.66100 1.000 40.88918  ?  647 HOH   A O    1 
HETATM 2225 O  O    . HOH   D 4 .   ? 39.735   -0.755    26.360   1.000 68.21123  ?  648 HOH   A O    1 
HETATM 2226 O  O    . HOH   D 4 .   ? 18.16000 3.61400   11.71500 1.000 30.78904  ?  649 HOH   A O    1 
HETATM 2227 O  O    . HOH   D 4 .   ? 25.62700 10.19000  19.28800 1.000 51.02902  ?  650 HOH   A O    1 
HETATM 2228 O  O    . HOH   D 4 .   ? 31.70700 4.19700   1.42200  1.000 50.85265  ?  651 HOH   A O    1 
HETATM 2229 O  O    . HOH   D 4 .   ? 35.61100 -5.85800  24.34700 1.000 47.83149  ?  652 HOH   A O    1 
HETATM 2230 O  O    A HOH   D 4 .   ? 43.91000 0.13300   19.12100 0.630 38.58500  ?  653 HOH   A O    1 
HETATM 2231 O  O    B HOH   D 4 .   ? 43.84300 -2.20200  19.60200 0.370 48.09025  ?  653 HOH   A O    1 
HETATM 2232 O  O    . HOH   D 4 .   ? 18.939   20.768    21.418   1.000 55.05409  ?  654 HOH   A O    1 
HETATM 2233 O  O    . HOH   D 4 .   ? 37.36600 11.48400  14.43000 1.000 52.22353  ?  655 HOH   A O    1 
HETATM 2234 O  O    . HOH   D 4 .   ? 3.60700  4.28900   17.45500 1.000 33.76000  ?  656 HOH   A O    1 
HETATM 2235 O  O    . HOH   D 4 .   ? 32.44000 0.94400   -3.64300 1.000 53.64252  ?  657 HOH   A O    1 
HETATM 2236 O  O    . HOH   D 4 .   ? 21.90200 -14.83100 23.60000 1.000 67.72235  ?  658 HOH   A O    1 
HETATM 2237 O  O    . HOH   D 4 .   ? 21.01000 -8.23300  33.31600 1.000 48.04947  ?  659 HOH   A O    1 
HETATM 2238 O  O    A HOH   D 4 .   ? -4.51300 4.17300   25.50600 0.550 36.18395  ?  660 HOH   A O    1 
HETATM 2239 O  O    B HOH   D 4 .   ? -4.12800 5.51200   26.47800 0.450 39.01425  ?  660 HOH   A O    1 
HETATM 2240 O  O    . HOH   D 4 .   ? 25.57800 -0.20900  31.26600 1.000 41.81547  ?  661 HOH   A O    1 
HETATM 2241 O  O    . HOH   D 4 .   ? 9.56000  9.44500   9.27400  1.000 53.84702  ?  662 HOH   A O    1 
HETATM 2242 O  O    . HOH   D 4 .   ? 20.68100 14.12600  14.90100 1.000 60.73289  ?  663 HOH   A O    1 
HETATM 2243 O  O    . HOH   D 4 .   ? 27.36400 -12.62000 18.43000 1.000 48.72253  ?  664 HOH   A O    1 
HETATM 2244 O  O    . HOH   D 4 .   ? 9.99000  -10.40700 35.98900 1.000 59.09878  ?  665 HOH   A O    1 
HETATM 2245 O  O    . HOH   D 4 .   ? 30.23600 11.19900  11.47600 1.000 48.07997  ?  666 HOH   A O    1 
HETATM 2246 O  O    . HOH   D 4 .   ? -3.01900 0.77300   22.98000 1.000 45.63562  ?  667 HOH   A O    1 
HETATM 2247 O  O    . HOH   D 4 .   ? 25.66700 -8.67300  19.86100 1.000 38.58378  ?  668 HOH   A O    1 
HETATM 2248 O  O    . HOH   D 4 .   ? 0.39300  -8.84700  19.37300 1.000 44.11091  ?  669 HOH   A O    1 
HETATM 2249 O  O    . HOH   D 4 .   ? 20.82200 1.53900   1.50700  1.000 44.74454  ?  670 HOH   A O    1 
HETATM 2250 O  O    . HOH   D 4 .   ? 29.58300 12.80800  20.97600 1.000 55.99528  ?  671 HOH   A O    1 
HETATM 2251 O  O    . HOH   D 4 .   ? 27.70100 0.86100   29.85900 1.000 44.73900  ?  672 HOH   A O    1 
HETATM 2252 O  O    . HOH   D 4 .   ? 23.19300 -12.98700 25.75100 1.000 43.86136  ?  673 HOH   A O    1 
HETATM 2253 O  O    . HOH   D 4 .   ? -1.85900 -12.15800 33.98900 1.000 61.70559  ?  674 HOH   A O    1 
HETATM 2254 O  O    . HOH   D 4 .   ? 1.71400  1.70700   13.53700 1.000 48.92950  ?  675 HOH   A O    1 
HETATM 2255 O  O    . HOH   D 4 .   ? 6.99600  0.28700   9.25900  1.000 44.47066  ?  676 HOH   A O    1 
HETATM 2256 O  O    . HOH   D 4 .   ? 40.82200 -4.66100  15.39900 1.000 60.99945  ?  677 HOH   A O    1 
HETATM 2257 O  O    . HOH   D 4 .   ? 35.02500 11.56300  15.93900 1.000 57.12465  ?  678 HOH   A O    1 
HETATM 2258 O  O    . HOH   D 4 .   ? 40.20400 -0.97600  17.07300 1.000 38.84902  ?  679 HOH   A O    1 
HETATM 2259 O  O    . HOH   D 4 .   ? 28.04400 -19.90000 14.93200 1.000 52.69091  ?  680 HOH   A O    1 
HETATM 2260 O  O    . HOH   D 4 .   ? 25.87400 15.67100  24.25800 1.000 62.42983  ?  681 HOH   A O    1 
HETATM 2261 O  O    . HOH   D 4 .   ? -1.39500 8.87500   30.35000 1.000 51.72412  ?  682 HOH   A O    1 
HETATM 2262 O  O    . HOH   D 4 .   ? 12.42300 7.92900   8.70500  1.000 50.16608  ?  683 HOH   A O    1 
HETATM 2263 O  O    . HOH   D 4 .   ? 20.10300 -25.99700 13.42000 1.000 54.92532  ?  684 HOH   A O    1 
HETATM 2264 O  O    . HOH   D 4 .   ? 26.81500 6.73700   18.84400 1.000 41.31613  ?  685 HOH   A O    1 
HETATM 2265 O  O    . HOH   D 4 .   ? 32.75900 7.16100   4.32200  1.000 71.40196  ?  686 HOH   A O    1 
HETATM 2266 O  O    . HOH   D 4 .   ? 2.08300  16.89600  31.28200 1.000 66.86354  ?  687 HOH   A O    1 
HETATM 2267 O  O    . HOH   D 4 .   ? 10.87500 -1.27900  4.69700  1.000 62.62276  ?  688 HOH   A O    1 
HETATM 2268 O  O    . HOH   D 4 .   ? 25.03600 -2.56500  31.00800 1.000 45.49558  ?  689 HOH   A O    1 
HETATM 2269 O  O    . HOH   D 4 .   ? 7.03400  21.55000  23.72200 1.000 62.87408  ?  690 HOH   A O    1 
HETATM 2270 O  O    . HOH   D 4 .   ? 40.43200 -2.54800  19.22000 1.000 38.22329  ?  691 HOH   A O    1 
HETATM 2271 O  O    . HOH   D 4 .   ? 19.06000 -19.61600 4.38800  1.000 53.74858  ?  692 HOH   A O    1 
HETATM 2272 O  O    . HOH   D 4 .   ? 15.433   -0.222    41.738   1.000 56.38486  ?  693 HOH   A O    1 
HETATM 2273 O  O    A HOH   D 4 .   ? 35.24600 -9.85600  5.39700  0.490 36.61481  ?  694 HOH   A O    1 
HETATM 2274 O  O    B HOH   D 4 .   ? 34.53500 -7.82200  5.39200  0.510 36.34409  ?  694 HOH   A O    1 
HETATM 2275 O  O    . HOH   D 4 .   ? 25.26900 -9.99200  0.41000  1.000 62.36316  ?  695 HOH   A O    1 
HETATM 2276 O  O    A HOH   D 4 .   ? 15.16500 21.75800  23.90300 0.560 53.45498  ?  696 HOH   A O    1 
HETATM 2277 O  O    B HOH   D 4 .   ? 14.71600 21.20200  22.39300 0.440 54.07900  ?  696 HOH   A O    1 
HETATM 2278 O  O    . HOH   D 4 .   ? 40.06600 -2.31600  14.78400 1.000 43.68478  ?  697 HOH   A O    1 
HETATM 2279 O  O    . HOH   D 4 .   ? 13.01300 -8.16800  24.13500 1.000 61.67839  ?  698 HOH   A O    1 
HETATM 2280 O  O    . HOH   D 4 .   ? 28.58700 10.56800  19.48100 1.000 46.96870  ?  699 HOH   A O    1 
HETATM 2281 O  O    . HOH   D 4 .   ? 30.56200 -9.36500  17.78800 1.000 49.07328  ?  700 HOH   A O    1 
HETATM 2282 O  O    . HOH   D 4 .   ? 24.99600 -10.92300 29.87600 1.000 54.55358  ?  701 HOH   A O    1 
HETATM 2283 O  O    A HOH   D 4 .   ? 24.85800 9.72500   16.57500 0.380 26.40087  ?  702 HOH   A O    1 
HETATM 2284 O  O    B HOH   D 4 .   ? 26.97000 9.52900   15.46700 0.370 34.92590  ?  702 HOH   A O    1 
HETATM 2285 O  O    C HOH   D 4 .   ? 25.11800 9.89200   14.36800 0.240 34.87760  ?  702 HOH   A O    1 
HETATM 2286 O  O    . HOH   E 4 .   ? 1.91600  -11.56700 8.17800  1.000 42.22913  ?  701 HOH   C O    1 
HETATM 2287 O  O    . HOH   E 4 .   ? 9.63800  -2.26000  7.06500  1.000 51.20482  ?  702 HOH   C O    1 
HETATM 2288 O  O    . HOH   E 4 .   ? 8.23100  -6.79600  -0.42700 1.000 61.76376  ?  703 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    A LYS   A 18  ? 0.57840 1.32736 0.77985 -0.07648 0.18349  -0.15532 123 LYS   A N    
2    N  N    B LYS   A 18  ? 0.58706 1.33714 0.78371 -0.07809 0.18416  -0.15468 123 LYS   A N    
3    C  CA   A LYS   A 18  ? 0.58436 1.30093 0.81027 -0.05829 0.17346  -0.16666 123 LYS   A CA   
4    C  CA   B LYS   A 18  ? 0.58780 1.30673 0.81097 -0.05924 0.17456  -0.16694 123 LYS   A CA   
5    C  C    A LYS   A 18  ? 0.58243 1.26394 0.77457 -0.05957 0.16679  -0.16676 123 LYS   A C    
6    C  C    B LYS   A 18  ? 0.58402 1.26678 0.77531 -0.05980 0.16731  -0.16711 123 LYS   A C    
7    O  O    A LYS   A 18  ? 0.59416 1.25466 0.79567 -0.04188 0.16412  -0.18876 123 LYS   A O    
8    O  O    B LYS   A 18  ? 0.59193 1.25394 0.79332 -0.04191 0.16469  -0.18932 123 LYS   A O    
9    C  CB   A LYS   A 18  ? 0.58983 1.29917 0.84508 -0.06196 0.16219  -0.14653 123 LYS   A CB   
10   C  CB   B LYS   A 18  ? 0.59233 1.30522 0.84632 -0.06239 0.16378  -0.14741 123 LYS   A CB   
11   C  CG   A LYS   A 18  ? 0.60346 1.32035 0.91210 -0.04096 0.15904  -0.15989 123 LYS   A CG   
12   C  CG   B LYS   A 18  ? 0.60091 1.30899 0.90484 -0.03878 0.15781  -0.16267 123 LYS   A CG   
13   C  CD   A LYS   A 18  ? 0.62598 1.34507 0.95092 -0.01780 0.16732  -0.19242 123 LYS   A CD   
14   C  CD   B LYS   A 18  ? 0.62608 1.34561 0.94797 -0.01782 0.16849  -0.19424 123 LYS   A CD   
15   C  CE   A LYS   A 18  ? 0.63485 1.38376 1.00662 -0.00446 0.17298  -0.20199 123 LYS   A CE   
16   C  CE   B LYS   A 18  ? 0.60029 1.28308 0.93303 0.00223  0.16113  -0.21291 123 LYS   A CE   
17   N  NZ   A LYS   A 18  ? 0.61410 1.36820 1.01821 -0.00720 0.16117  -0.18024 123 LYS   A NZ   
18   N  NZ   B LYS   A 18  ? 0.62024 1.30509 0.94708 0.01381  0.17185  -0.24390 123 LYS   A NZ   
19   N  N    . LEU   A 19  ? 0.58265 1.25616 0.73779 -0.08050 0.16349  -0.14108 124 LEU   A N    
20   C  CA   . LEU   A 19  ? 0.62848 1.25956 0.74712 -0.08226 0.15328  -0.13535 124 LEU   A CA   
21   C  C    . LEU   A 19  ? 0.64385 1.29928 0.73295 -0.08389 0.16395  -0.15175 124 LEU   A C    
22   O  O    . LEU   A 19  ? 0.68606 1.35912 0.74554 -0.10099 0.16674  -0.13433 124 LEU   A O    
23   C  CB   . LEU   A 19  ? 0.66309 1.26536 0.75766 -0.10163 0.14150  -0.09920 124 LEU   A CB   
24   C  CG   . LEU   A 19  ? 0.66990 1.21595 0.73671 -0.10033 0.12577  -0.08915 124 LEU   A CG   
25   C  CD1  . LEU   A 19  ? 0.57476 1.08019 0.66169 -0.08053 0.11398  -0.10291 124 LEU   A CD1  
26   C  CD2  . LEU   A 19  ? 0.69903 1.21970 0.75098 -0.11847 0.11574  -0.05557 124 LEU   A CD2  
27   N  N    . SER   A 20  ? 0.56976 1.21636 0.66677 -0.06581 0.16513  -0.18310 125 SER   A N    
28   C  CA   . SER   A 20  ? 0.54795 1.21069 0.62040 -0.06593 0.17071  -0.20236 125 SER   A CA   
29   C  C    . SER   A 20  ? 0.54779 1.19904 0.57278 -0.08092 0.16382  -0.18412 125 SER   A C    
30   O  O    . SER   A 20  ? 0.53647 1.16049 0.54893 -0.08794 0.15500  -0.16043 125 SER   A O    
31   C  CB   . SER   A 20  ? 0.53527 1.18288 0.63088 -0.04430 0.17090  -0.23970 125 SER   A CB   
32   O  OG   . SER   A 20  ? 0.50723 1.11312 0.59817 -0.03797 0.16013  -0.24069 125 SER   A OG   
33   N  N    A GLU   A 21  ? 0.57335 1.24762 0.57351 -0.08594 0.16735  -0.19517 126 GLU   A N    
34   N  N    B GLU   A 21  ? 0.57394 1.24859 0.57431 -0.08596 0.16747  -0.19520 126 GLU   A N    
35   C  CA   A GLU   A 21  ? 0.60160 1.26936 0.55974 -0.09926 0.15918  -0.17734 126 GLU   A CA   
36   C  CA   B GLU   A 21  ? 0.60215 1.27076 0.56053 -0.09902 0.15944  -0.17835 126 GLU   A CA   
37   C  C    A GLU   A 21  ? 0.57504 1.20145 0.52727 -0.08996 0.14862  -0.18657 126 GLU   A C    
38   C  C    B GLU   A 21  ? 0.57514 1.20163 0.52784 -0.08991 0.14873  -0.18649 126 GLU   A C    
39   O  O    A GLU   A 21  ? 0.56857 1.17497 0.49450 -0.09909 0.13881  -0.16254 126 GLU   A O    
40   O  O    B GLU   A 21  ? 0.56766 1.17373 0.49470 -0.09907 0.13898  -0.16185 126 GLU   A O    
41   C  CB   A GLU   A 21  ? 0.65184 1.35915 0.58897 -0.10639 0.16456  -0.18918 126 GLU   A CB   
42   C  CB   B GLU   A 21  ? 0.65203 1.35933 0.59081 -0.10488 0.16493  -0.19292 126 GLU   A CB   
43   C  CG   A GLU   A 21  ? 0.68909 1.40680 0.58720 -0.12577 0.15762  -0.15688 126 GLU   A CG   
44   C  CG   B GLU   A 21  ? 0.67251 1.42547 0.62309 -0.10935 0.17814  -0.19657 126 GLU   A CG   
45   C  CD   A GLU   A 21  ? 0.71968 1.45186 0.61563 -0.14144 0.15976  -0.12048 126 GLU   A CD   
46   C  CD   B GLU   A 21  ? 0.64296 1.40596 0.62934 -0.09090 0.18797  -0.23652 126 GLU   A CD   
47   O  OE1  A GLU   A 21  ? 0.72728 1.44051 0.60524 -0.15333 0.14998  -0.08559 126 GLU   A OE1  
48   O  OE1  B GLU   A 21  ? 0.57789 1.32549 0.59952 -0.07911 0.18964  -0.23980 126 GLU   A OE1  
49   O  OE2  A GLU   A 21  ? 0.73792 1.49924 0.65266 -0.14189 0.17081  -0.12652 126 GLU   A OE2  
50   O  OE2  B GLU   A 21  ? 0.66816 1.45499 0.64971 -0.08823 0.19341  -0.26424 126 GLU   A OE2  
51   N  N    . GLU   A 22  ? 0.58213 1.19384 0.56090 -0.07169 0.14981  -0.22018 127 GLU   A N    
52   C  CA   . GLU   A 22  ? 0.50952 1.08017 0.48689 -0.06270 0.13951  -0.22919 127 GLU   A CA   
53   C  C    . GLU   A 22  ? 0.46194 0.99253 0.44756 -0.06159 0.12927  -0.20290 127 GLU   A C    
54   O  O    . GLU   A 22  ? 0.46831 0.95988 0.43759 -0.06306 0.11484  -0.18865 127 GLU   A O    
55   C  CB   . GLU   A 22  ? 0.61118 1.17046 0.62268 -0.04362 0.14165  -0.26816 127 GLU   A CB   
56   C  CG   . GLU   A 22  ? 0.70346 1.22026 0.71610 -0.03511 0.13050  -0.27962 127 GLU   A CG   
57   C  CD   . GLU   A 22  ? 0.81842 1.32577 0.86149 -0.02045 0.13160  -0.31736 127 GLU   A CD   
58   O  OE1  . GLU   A 22  ? 0.89407 1.43214 0.93628 -0.02257 0.13911  -0.33662 127 GLU   A OE1  
59   O  OE2  . GLU   A 22  ? 0.84342 1.31249 0.91289 -0.00736 0.12472  -0.32714 127 GLU   A OE2  
60   N  N    . GLN   A 23  ? 0.41179 0.94338 0.42562 -0.05905 0.13152  -0.19253 128 GLN   A N    
61   C  CA   . GLN   A 23  ? 0.42867 0.91446 0.45233 -0.05863 0.11661  -0.16545 128 GLN   A CA   
62   C  C    . GLN   A 23  ? 0.44767 0.92458 0.43969 -0.07674 0.10991  -0.13043 128 GLN   A C    
63   O  O    . GLN   A 23  ? 0.47504 0.90751 0.46098 -0.07675 0.09560  -0.11286 128 GLN   A O    
64   C  CB   . GLN   A 23  ? 0.43555 0.93092 0.49758 -0.05268 0.12006  -0.16465 128 GLN   A CB   
65   C  CG   . GLN   A 23  ? 0.45689 0.94104 0.55855 -0.03137 0.11950  -0.19089 128 GLN   A CG   
66   C  CD   . GLN   A 23  ? 0.48015 0.98765 0.62255 -0.02482 0.12489  -0.19252 128 GLN   A CD   
67   O  OE1  . GLN   A 23  ? 0.44632 0.99153 0.58800 -0.03628 0.13419  -0.18271 128 GLN   A OE1  
68   N  NE2  . GLN   A 23  ? 0.45055 0.93737 0.63102 -0.00682 0.11841  -0.20308 128 GLN   A NE2  
69   N  N    . GLN   A 24  ? 0.43675 0.95635 0.41041 -0.09228 0.12033  -0.11946 129 GLN   A N    
70   C  CA   . GLN   A 24  ? 0.48699 0.99815 0.43261 -0.10958 0.11352  -0.08477 129 GLN   A CA   
71   C  C    . GLN   A 24  ? 0.46270 0.95394 0.37956 -0.10930 0.10386  -0.08273 129 GLN   A C    
72   O  O    . GLN   A 24  ? 0.48882 0.94750 0.39354 -0.11509 0.09154  -0.05647 129 GLN   A O    
73   C  CB   . GLN   A 24  ? 0.53359 1.09951 0.46617 -0.12729 0.12711  -0.07195 129 GLN   A CB   
74   C  CG   . GLN   A 24  ? 0.60157 1.17865 0.55861 -0.13536 0.13169  -0.05662 129 GLN   A CG   
75   C  CD   . GLN   A 24  ? 0.73484 1.36011 0.68284 -0.15064 0.14229  -0.04518 129 GLN   A CD   
76   O  OE1  . GLN   A 24  ? 0.75093 1.40978 0.71108 -0.14448 0.15249  -0.06726 129 GLN   A OE1  
77   N  NE2  . GLN   A 24  ? 0.82186 1.44140 0.75134 -0.16853 0.13614  -0.00965 129 GLN   A NE2  
78   N  N    . HIS   A 25  ? 0.49439 1.00613 0.40257 -0.10259 0.10921  -0.11172 130 HIS   A N    
79   C  CA   . HIS   A 25  ? 0.49922 0.99519 0.38301 -0.10217 0.09919  -0.11320 130 HIS   A CA   
80   C  C    . HIS   A 25  ? 0.49105 0.92786 0.38926 -0.09043 0.08404  -0.11068 130 HIS   A C    
81   O  O    . HIS   A 25  ? 0.50680 0.91814 0.38905 -0.09401 0.07190  -0.09112 130 HIS   A O    
82   C  CB   . HIS   A 25  ? 0.56923 1.10005 0.44554 -0.09757 0.10848  -0.15087 130 HIS   A CB   
83   C  CG   . HIS   A 25  ? 0.62838 1.14965 0.48079 -0.09969 0.09697  -0.15227 130 HIS   A CG   
84   N  ND1  . HIS   A 25  ? 0.67206 1.19975 0.49591 -0.11322 0.08834  -0.12101 130 HIS   A ND1  
85   C  CD2  . HIS   A 25  ? 0.69265 1.19905 0.54970 -0.09029 0.09190  -0.18015 130 HIS   A CD2  
86   C  CE1  . HIS   A 25  ? 0.71081 1.23121 0.52215 -0.11168 0.07864  -0.12986 130 HIS   A CE1  
87   N  NE2  . HIS   A 25  ? 0.68081 1.18802 0.51125 -0.09876 0.08074  -0.16600 130 HIS   A NE2  
88   N  N    . ILE   A 26  ? 0.48667 0.90379 0.41678 -0.07630 0.08464  -0.12905 131 ILE   A N    
89   C  CA   . ILE   A 26  ? 0.41543 0.78152 0.35975 -0.06586 0.07136  -0.12660 131 ILE   A CA   
90   C  C    . ILE   A 26  ? 0.45369 0.79021 0.39287 -0.07258 0.06158  -0.09363 131 ILE   A C    
91   O  O    . ILE   A 26  ? 0.41944 0.72329 0.35098 -0.07097 0.05024  -0.08327 131 ILE   A O    
92   C  CB   . ILE   A 26  ? 0.42946 0.78546 0.41111 -0.05103 0.07380  -0.14673 131 ILE   A CB   
93   C  CG1  . ILE   A 26  ? 0.46883 0.84445 0.46035 -0.04217 0.08179  -0.18295 131 ILE   A CG1  
94   C  CG2  . ILE   A 26  ? 0.41130 0.71881 0.40676 -0.04308 0.06017  -0.13701 131 ILE   A CG2  
95   C  CD1  . ILE   A 26  ? 0.49233 0.86214 0.52633 -0.02663 0.08510  -0.20216 131 ILE   A CD1  
96   N  N    . ILE   A 27  ? 0.47709 0.82570 0.42284 -0.08044 0.06622  -0.07836 132 ILE   A N    
97   C  CA   . ILE   A 27  ? 0.45922 0.77912 0.40384 -0.08754 0.05754  -0.05074 132 ILE   A CA   
98   C  C    . ILE   A 27  ? 0.44949 0.76459 0.36765 -0.09752 0.05187  -0.02902 132 ILE   A C    
99   O  O    . ILE   A 27  ? 0.46666 0.74583 0.38314 -0.09672 0.04120  -0.01433 132 ILE   A O    
100  C  CB   . ILE   A 27  ? 0.47075 0.80858 0.43013 -0.09611 0.06394  -0.04086 132 ILE   A CB   
101  C  CG1  . ILE   A 27  ? 0.42488 0.75993 0.41493 -0.08461 0.06494  -0.05736 132 ILE   A CG1  
102  C  CG2  . ILE   A 27  ? 0.47389 0.78634 0.42954 -0.10736 0.05609  -0.01295 132 ILE   A CG2  
103  C  CD1  . ILE   A 27  ? 0.44809 0.81276 0.45632 -0.09212 0.07289  -0.05307 132 ILE   A CD1  
104  N  N    . ALA   A 28  ? 0.43370 0.78749 0.33187 -0.10672 0.05883  -0.02657 133 ALA   A N    
105  C  CA   . ALA   A 28  ? 0.45953 0.81378 0.33365 -0.11648 0.05216  -0.00228 133 ALA   A CA   
106  C  C    . ALA   A 28  ? 0.48186 0.80956 0.34863 -0.10734 0.04088  -0.00763 133 ALA   A C    
107  O  O    . ALA   A 28  ? 0.48591 0.78926 0.34758 -0.10946 0.03050  0.01469  133 ALA   A O    
108  C  CB   . ALA   A 28  ? 0.44612 0.85469 0.29782 -0.12838 0.06182  -0.00037 133 ALA   A CB   
109  N  N    . ILE   A 29  ? 0.49599 0.82794 0.36572 -0.09709 0.04272  -0.03728 134 ILE   A N    
110  C  CA   . ILE   A 29  ? 0.47469 0.78468 0.33974 -0.08992 0.03230  -0.04348 134 ILE   A CA   
111  C  C    . ILE   A 29  ? 0.47641 0.73852 0.35875 -0.08196 0.02315  -0.03460 134 ILE   A C    
112  O  O    . ILE   A 29  ? 0.47021 0.71199 0.34726 -0.08093 0.01322  -0.02148 134 ILE   A O    
113  C  CB   . ILE   A 29  ? 0.46997 0.79367 0.33917 -0.08208 0.03675  -0.07896 134 ILE   A CB   
114  C  CG1  . ILE   A 29  ? 0.53323 0.90701 0.37869 -0.09106 0.04416  -0.08973 134 ILE   A CG1  
115  C  CG2  . ILE   A 29  ? 0.43140 0.72495 0.30536 -0.07408 0.02576  -0.08638 134 ILE   A CG2  
116  C  CD1  . ILE   A 29  ? 0.56721 0.96204 0.42396 -0.08432 0.05485  -0.12847 134 ILE   A CD1  
117  N  N    . LEU   A 30  ? 0.45781 0.70504 0.36153 -0.07628 0.02640  -0.04185 135 LEU   A N    
118  C  CA   . LEU   A 30  ? 0.38807 0.59557 0.30601 -0.06956 0.01856  -0.03598 135 LEU   A CA   
119  C  C    . LEU   A 30  ? 0.41630 0.60606 0.33039 -0.07653 0.01349  -0.00984 135 LEU   A C    
120  O  O    . LEU   A 30  ? 0.43151 0.59215 0.34889 -0.07212 0.00568  -0.00312 135 LEU   A O    
121  C  CB   . LEU   A 30  ? 0.39258 0.59491 0.33317 -0.06321 0.02229  -0.04822 135 LEU   A CB   
122  C  CG   . LEU   A 30  ? 0.40030 0.61032 0.35369 -0.05332 0.02544  -0.07392 135 LEU   A CG   
123  C  CD1  . LEU   A 30  ? 0.39212 0.59830 0.37153 -0.04659 0.02748  -0.08072 135 LEU   A CD1  
124  C  CD2  . LEU   A 30  ? 0.41454 0.60241 0.36677 -0.04712 0.01729  -0.07958 135 LEU   A CD2  
125  N  N    A LEU   A 31  ? 0.41549 0.62258 0.32529 -0.08760 0.01826  0.00463  136 LEU   A N    
126  N  N    B LEU   A 31  ? 0.42534 0.63268 0.33506 -0.08762 0.01831  0.00457  136 LEU   A N    
127  C  CA   A LEU   A 31  ? 0.44939 0.63773 0.35899 -0.09513 0.01297  0.03016  136 LEU   A CA   
128  C  CA   B LEU   A 31  ? 0.43579 0.62503 0.34522 -0.09539 0.01318  0.03026  136 LEU   A CA   
129  C  C    A LEU   A 31  ? 0.45179 0.63445 0.34859 -0.09473 0.00493  0.04421  136 LEU   A C    
130  C  C    B LEU   A 31  ? 0.44879 0.63184 0.34554 -0.09500 0.00505  0.04453  136 LEU   A C    
131  O  O    A LEU   A 31  ? 0.44461 0.59680 0.34867 -0.09135 -0.00271 0.05527  136 LEU   A O    
132  O  O    B LEU   A 31  ? 0.44800 0.60064 0.35210 -0.09198 -0.00251 0.05618  136 LEU   A O    
133  C  CB   A LEU   A 31  ? 0.43800 0.64941 0.34677 -0.10923 0.01964  0.04511  136 LEU   A CB   
134  C  CB   B LEU   A 31  ? 0.44326 0.65691 0.35132 -0.10951 0.02007  0.04491  136 LEU   A CB   
135  C  CG   A LEU   A 31  ? 0.42448 0.63932 0.35092 -0.11222 0.02566  0.03807  136 LEU   A CG   
136  C  CG   B LEU   A 31  ? 0.43291 0.64053 0.35950 -0.11470 0.02367  0.04548  136 LEU   A CG   
137  C  CD1  A LEU   A 31  ? 0.41191 0.65888 0.33625 -0.12775 0.03360  0.05291  136 LEU   A CD1  
138  C  CD1  B LEU   A 31  ? 0.42189 0.63004 0.36207 -0.10423 0.02652  0.02065  136 LEU   A CD1  
139  C  CD2  A LEU   A 31  ? 0.46582 0.64170 0.40764 -0.11080 0.01860  0.04212  136 LEU   A CD2  
140  C  CD2  B LEU   A 31  ? 0.43490 0.67710 0.35903 -0.12984 0.03213  0.05878  136 LEU   A CD2  
141  N  N    . ASP   A 32  ? 0.44447 0.65913 0.32322 -0.09796 0.00646  0.04269  137 ASP   A N    
142  C  CA   . ASP   A 32  ? 0.46354 0.67941 0.33013 -0.09824 -0.00266 0.05722  137 ASP   A CA   
143  C  C    . ASP   A 32  ? 0.48038 0.67170 0.35415 -0.08580 -0.00993 0.04440  137 ASP   A C    
144  O  O    . ASP   A 32  ? 0.50836 0.68267 0.38526 -0.08282 -0.01894 0.05960  137 ASP   A O    
145  C  CB   . ASP   A 32  ? 0.49640 0.75860 0.33959 -0.10593 0.00065  0.05490  137 ASP   A CB   
146  C  CG   . ASP   A 32  ? 0.55964 0.83004 0.38919 -0.10717 -0.01037 0.07042  137 ASP   A CG   
147  O  OD1  . ASP   A 32  ? 0.60519 0.89181 0.42446 -0.10383 -0.01258 0.05165  137 ASP   A OD1  
148  O  OD2  . ASP   A 32  ? 0.59757 0.85862 0.42914 -0.11171 -0.01750 0.10154  137 ASP   A OD2  
149  N  N    . ALA   A 33  ? 0.47873 0.66889 0.35820 -0.07846 -0.00612 0.01761  138 ALA   A N    
150  C  CA   . ALA   A 33  ? 0.44452 0.61303 0.33260 -0.06842 -0.01233 0.00668  138 ALA   A CA   
151  C  C    . ALA   A 33  ? 0.48318 0.61621 0.38634 -0.06332 -0.01634 0.01693  138 ALA   A C    
152  O  O    . ALA   A 33  ? 0.41049 0.52890 0.31807 -0.05784 -0.02321 0.02129  138 ALA   A O    
153  C  CB   . ALA   A 33  ? 0.44399 0.61520 0.34017 -0.06253 -0.00741 -0.02086 138 ALA   A CB   
154  N  N    . HIS   A 34  ? 0.38844 0.51015 0.30052 -0.06541 -0.01183 0.01909  139 HIS   A N    
155  C  CA   . HIS   A 34  ? 0.44426 0.53499 0.36940 -0.06193 -0.01488 0.02508  139 HIS   A CA   
156  C  C    . HIS   A 34  ? 0.44401 0.52333 0.37049 -0.06445 -0.02038 0.04706  139 HIS   A C    
157  O  O    . HIS   A 34  ? 0.46408 0.52142 0.40049 -0.05774 -0.02493 0.04942  139 HIS   A O    
158  C  CB   . HIS   A 34  ? 0.41838 0.50418 0.35222 -0.06570 -0.00973 0.02098  139 HIS   A CB   
159  C  CG   . HIS   A 34  ? 0.45638 0.51389 0.40173 -0.06429 -0.01242 0.02389  139 HIS   A CG   
160  N  ND1  . HIS   A 34  ? 0.42006 0.46119 0.37094 -0.05584 -0.01512 0.01476  139 HIS   A ND1  
161  C  CD2  . HIS   A 34  ? 0.46979 0.51409 0.42268 -0.07123 -0.01240 0.03324  139 HIS   A CD2  
162  C  CE1  . HIS   A 34  ? 0.43301 0.45415 0.39239 -0.05701 -0.01603 0.01623  139 HIS   A CE1  
163  N  NE2  . HIS   A 34  ? 0.45190 0.47244 0.41380 -0.06624 -0.01487 0.02652  139 HIS   A NE2  
164  N  N    . HIS   A 35  ? 0.44567 0.54098 0.36446 -0.07397 -0.01983 0.06416  140 HIS   A N    
165  C  CA   . HIS   A 35  ? 0.47942 0.56317 0.40355 -0.07651 -0.02631 0.08925  140 HIS   A CA   
166  C  C    . HIS   A 35  ? 0.50512 0.59215 0.42687 -0.06929 -0.03458 0.09510  140 HIS   A C    
167  O  O    . HIS   A 35  ? 0.49208 0.55998 0.42757 -0.06492 -0.04111 0.11026  140 HIS   A O    
168  C  CB   . HIS   A 35  ? 0.56183 0.66716 0.47736 -0.09010 -0.02427 0.10987  140 HIS   A CB   
169  C  CG   . HIS   A 35  ? 0.65425 0.75482 0.57776 -0.09872 -0.01736 0.10897  140 HIS   A CG   
170  N  ND1  . HIS   A 35  ? 0.65970 0.79026 0.57387 -0.11131 -0.01090 0.11684  140 HIS   A ND1  
171  C  CD2  . HIS   A 35  ? 0.65748 0.73049 0.59773 -0.09756 -0.01598 0.10041  140 HIS   A CD2  
172  C  CE1  . HIS   A 35  ? 0.67640 0.79707 0.60357 -0.11744 -0.00626 0.11423  140 HIS   A CE1  
173  N  NE2  . HIS   A 35  ? 0.65168 0.73724 0.59404 -0.10955 -0.00985 0.10388  140 HIS   A NE2  
174  N  N    . LYS   A 36  ? 0.45149 0.56280 0.35914 -0.06779 -0.03469 0.08207  141 LYS   A N    
175  C  CA   . LYS   A 36  ? 0.45870 0.57761 0.36460 -0.06242 -0.04333 0.08591  141 LYS   A CA   
176  C  C    . LYS   A 36  ? 0.43468 0.53228 0.35513 -0.05104 -0.04491 0.07097  141 LYS   A C    
177  O  O    . LYS   A 36  ? 0.42035 0.52107 0.34562 -0.04583 -0.05238 0.07598  141 LYS   A O    
178  C  CB   . LYS   A 36  ? 0.44194 0.59841 0.32656 -0.06791 -0.04336 0.07643  141 LYS   A CB   
179  C  CG   . LYS   A 36  ? 0.55912 0.74654 0.42583 -0.07994 -0.04367 0.09587  141 LYS   A CG   
180  C  CD   . LYS   A 36  ? 0.67624 0.90440 0.52049 -0.08521 -0.04487 0.08402  141 LYS   A CD   
181  C  CE   . LYS   A 36  ? 0.75532 1.02064 0.57868 -0.09831 -0.04614 0.10681  141 LYS   A CE   
182  N  NZ   . LYS   A 36  ? 0.82235 1.07049 0.65685 -0.10173 -0.04952 0.14176  141 LYS   A NZ   
183  N  N    . THR   A 37  ? 0.39349 0.47323 0.32148 -0.04781 -0.03840 0.05441  142 THR   A N    
184  C  CA   . THR   A 37  ? 0.43226 0.49644 0.37208 -0.03885 -0.03882 0.04153  142 THR   A CA   
185  C  C    . THR   A 37  ? 0.45909 0.49583 0.41365 -0.03467 -0.03622 0.04153  142 THR   A C    
186  O  O    . THR   A 37  ? 0.44992 0.47692 0.41325 -0.02798 -0.03546 0.03155  142 THR   A O    
187  C  CB   . THR   A 37  ? 0.43250 0.50401 0.36833 -0.03859 -0.03454 0.02032  142 THR   A CB   
188  O  OG1  . THR   A 37  ? 0.43026 0.50204 0.36332 -0.04301 -0.02785 0.01463  142 THR   A OG1  
189  C  CG2  . THR   A 37  ? 0.40451 0.50099 0.32944 -0.04148 -0.03759 0.01412  142 THR   A CG2  
190  N  N    . TYR   A 38  ? 0.43192 0.45773 0.38973 -0.03956 -0.03458 0.05147  143 TYR   A N    
191  C  CA   . TYR   A 38  ? 0.41587 0.41563 0.38842 -0.03691 -0.03251 0.04860  143 TYR   A CA   
192  C  C    . TYR   A 38  ? 0.46181 0.44737 0.44757 -0.03702 -0.03700 0.06812  143 TYR   A C    
193  O  O    . TYR   A 38  ? 0.46569 0.45608 0.44782 -0.04579 -0.03815 0.08416  143 TYR   A O    
194  C  CB   . TYR   A 38  ? 0.44541 0.44178 0.41507 -0.04392 -0.02679 0.03915  143 TYR   A CB   
195  C  CG   . TYR   A 38  ? 0.39594 0.36982 0.37778 -0.04199 -0.02473 0.02946  143 TYR   A CG   
196  C  CD1  . TYR   A 38  ? 0.43207 0.38537 0.42748 -0.04496 -0.02578 0.03704  143 TYR   A CD1  
197  C  CD2  . TYR   A 38  ? 0.39357 0.36787 0.37397 -0.03805 -0.02202 0.01259  143 TYR   A CD2  
198  C  CE1  . TYR   A 38  ? 0.41880 0.35285 0.42523 -0.04387 -0.02359 0.02355  143 TYR   A CE1  
199  C  CE2  . TYR   A 38  ? 0.42217 0.38151 0.41030 -0.03753 -0.01993 0.00178  143 TYR   A CE2  
200  C  CZ   . TYR   A 38  ? 0.46924 0.40865 0.46994 -0.04037 -0.02043 0.00505  143 TYR   A CZ   
201  O  OH   . TYR   A 38  ? 0.46890 0.39455 0.47726 -0.04052 -0.01804 -0.01016 143 TYR   A OH   
202  N  N    . ASP   A 39  ? 0.42037 0.38943 0.42395 -0.02726 -0.03923 0.06747  144 ASP   A N    
203  C  CA   . ASP   A 39  ? 0.46279 0.41440 0.48671 -0.02441 -0.04424 0.08547  144 ASP   A CA   
204  C  C    . ASP   A 39  ? 0.51407 0.43605 0.55527 -0.02419 -0.03993 0.07457  144 ASP   A C    
205  O  O    . ASP   A 39  ? 0.44662 0.35814 0.49894 -0.01520 -0.03668 0.05726  144 ASP   A O    
206  C  CB   . ASP   A 39  ? 0.49711 0.45271 0.53479 -0.01213 -0.04990 0.09117  144 ASP   A CB   
207  C  CG   . ASP   A 39  ? 0.57103 0.50649 0.63700 -0.00624 -0.05574 0.10998  144 ASP   A CG   
208  O  OD1  . ASP   A 39  ? 0.55669 0.47601 0.62959 -0.01370 -0.05672 0.12306  144 ASP   A OD1  
209  O  OD2  . ASP   A 39  ? 0.56412 0.50019 0.64874 0.00596  -0.05962 0.11252  144 ASP   A OD2  
210  N  N    . PRO   A 40  ? 0.52339 0.43323 0.56805 -0.03482 -0.03951 0.08293  145 PRO   A N    
211  C  CA   . PRO   A 40  ? 0.55954 0.44125 0.62132 -0.03659 -0.03601 0.06915  145 PRO   A CA   
212  C  C    . PRO   A 40  ? 0.59164 0.44509 0.68550 -0.02715 -0.03921 0.07346  145 PRO   A C    
213  O  O    . PRO   A 40  ? 0.59148 0.41970 0.70255 -0.02821 -0.03627 0.05867  145 PRO   A O    
214  C  CB   . PRO   A 40  ? 0.54965 0.43096 0.60693 -0.05281 -0.03561 0.08016  145 PRO   A CB   
215  C  CG   . PRO   A 40  ? 0.57083 0.47105 0.61968 -0.05692 -0.04055 0.10858  145 PRO   A CG   
216  C  CD   . PRO   A 40  ? 0.53179 0.45601 0.56517 -0.04713 -0.04192 0.10487  145 PRO   A CD   
217  N  N    . THR   A 41  ? 0.58794 0.44557 0.69278 -0.01785 -0.04557 0.09226  146 THR   A N    
218  C  CA   . THR   A 41  ? 0.56787 0.40056 0.70842 -0.00513 -0.04838 0.09421  146 THR   A CA   
219  C  C    . THR   A 41  ? 0.56842 0.40545 0.71490 0.00928  -0.04295 0.06871  146 THR   A C    
220  O  O    . THR   A 41  ? 0.53078 0.34623 0.70810 0.02024  -0.04132 0.05867  146 THR   A O    
221  C  CB   . THR   A 41  ? 0.65796 0.49583 0.81206 -0.00104 -0.05909 0.12904  146 THR   A CB   
222  O  OG1  . THR   A 41  ? 0.65518 0.52384 0.79552 0.00664  -0.06180 0.13097  146 THR   A OG1  
223  C  CG2  . THR   A 41  ? 0.72545 0.57111 0.86540 -0.01755 -0.06360 0.15666  146 THR   A CG2  
224  N  N    . TYR   A 42  ? 0.48226 0.34731 0.60216 0.00917  -0.03967 0.05797  147 TYR   A N    
225  C  CA   . TYR   A 42  ? 0.46598 0.34078 0.58809 0.01985  -0.03363 0.03560  147 TYR   A CA   
226  C  C    . TYR   A 42  ? 0.51222 0.38688 0.66388 0.03571  -0.03718 0.04307  147 TYR   A C    
227  O  O    . TYR   A 42  ? 0.57091 0.44299 0.73969 0.04650  -0.03075 0.02338  147 TYR   A O    
228  C  CB   . TYR   A 42  ? 0.49236 0.35274 0.61671 0.01839  -0.02459 0.00662  147 TYR   A CB   
229  C  CG   . TYR   A 42  ? 0.49076 0.35296 0.59031 0.00299  -0.02249 0.00053  147 TYR   A CG   
230  C  CD1  . TYR   A 42  ? 0.54654 0.38545 0.65499 -0.00592 -0.02247 -0.00228 147 TYR   A CD1  
231  C  CD2  . TYR   A 42  ? 0.48340 0.37082 0.55452 -0.00265 -0.02110 -0.00196 147 TYR   A CD2  
232  C  CE1  . TYR   A 42  ? 0.55184 0.39640 0.64046 -0.02010 -0.02109 -0.00721 147 TYR   A CE1  
233  C  CE2  . TYR   A 42  ? 0.54961 0.44096 0.60265 -0.01508 -0.01966 -0.00665 147 TYR   A CE2  
234  C  CZ   . TYR   A 42  ? 0.58839 0.46022 0.64972 -0.02379 -0.01966 -0.00907 147 TYR   A CZ   
235  O  OH   . TYR   A 42  ? 0.54726 0.42683 0.59327 -0.03624 -0.01871 -0.01325 147 TYR   A OH   
236  N  N    . ALA   A 43  ? 0.50440 0.38599 0.66262 0.03711  -0.04746 0.07181  148 ALA   A N    
237  C  CA   . ALA   A 43  ? 0.53185 0.41498 0.72257 0.05257  -0.05306 0.08316  148 ALA   A CA   
238  C  C    . ALA   A 43  ? 0.57842 0.49030 0.76573 0.06064  -0.05032 0.07140  148 ALA   A C    
239  O  O    . ALA   A 43  ? 0.62783 0.54049 0.84597 0.07551  -0.04907 0.06632  148 ALA   A O    
240  C  CB   . ALA   A 43  ? 0.53638 0.42540 0.73183 0.05000  -0.06656 0.12028  148 ALA   A CB   
241  N  N    . ASP   A 44  ? 0.52924 0.46508 0.68301 0.05111  -0.04914 0.06675  149 ASP   A N    
242  C  CA   . ASP   A 44  ? 0.49688 0.46021 0.64836 0.05595  -0.04763 0.05841  149 ASP   A CA   
243  C  C    . ASP   A 44  ? 0.51867 0.48091 0.67878 0.06247  -0.03530 0.03129  149 ASP   A C    
244  O  O    . ASP   A 44  ? 0.47996 0.46489 0.64649 0.06794  -0.03310 0.02558  149 ASP   A O    
245  C  CB   . ASP   A 44  ? 0.49426 0.47895 0.61091 0.04316  -0.04957 0.05904  149 ASP   A CB   
246  C  CG   . ASP   A 44  ? 0.55549 0.55060 0.66033 0.03604  -0.06079 0.08304  149 ASP   A CG   
247  O  OD1  . ASP   A 44  ? 0.56240 0.56009 0.68730 0.04259  -0.06988 0.10348  149 ASP   A OD1  
248  O  OD2  . ASP   A 44  ? 0.60286 0.60604 0.67926 0.02406  -0.06053 0.08165  149 ASP   A OD2  
249  N  N    . PHE   A 45  ? 0.52042 0.46017 0.68063 0.06073  -0.02729 0.01445  150 PHE   A N    
250  C  CA   . PHE   A 45  ? 0.49174 0.43519 0.65610 0.06525  -0.01506 -0.01274 150 PHE   A CA   
251  C  C    . PHE   A 45  ? 0.47548 0.42431 0.67691 0.08234  -0.01171 -0.01863 150 PHE   A C    
252  O  O    . PHE   A 45  ? 0.53415 0.49867 0.73861 0.08663  -0.00106 -0.03931 150 PHE   A O    
253  C  CB   . PHE   A 45  ? 0.52585 0.44497 0.68494 0.05938  -0.00883 -0.03026 150 PHE   A CB   
254  C  CG   . PHE   A 45  ? 0.52944 0.45276 0.65261 0.04365  -0.00811 -0.03323 150 PHE   A CG   
255  C  CD1  . PHE   A 45  ? 0.53957 0.47003 0.64310 0.03485  -0.01585 -0.01398 150 PHE   A CD1  
256  C  CD2  . PHE   A 45  ? 0.53294 0.45571 0.64345 0.03796  0.00017  -0.05604 150 PHE   A CD2  
257  C  CE1  . PHE   A 45  ? 0.52024 0.45527 0.59635 0.02242  -0.01481 -0.01755 150 PHE   A CE1  
258  C  CE2  . PHE   A 45  ? 0.46875 0.39725 0.55053 0.02467  -0.00041 -0.05676 150 PHE   A CE2  
259  C  CZ   . PHE   A 45  ? 0.46292 0.39644 0.52960 0.01776  -0.00766 -0.03754 150 PHE   A CZ   
260  N  N    . ARG   A 46  ? 0.49059 0.42954 0.72172 0.09222  -0.02048 0.00017  151 ARG   A N    
261  C  CA   . ARG   A 46  ? 0.54732 0.49343 0.81963 0.11049  -0.01826 -0.00365 151 ARG   A CA   
262  C  C    . ARG   A 46  ? 0.54127 0.52638 0.81331 0.11346  -0.01914 0.00088  151 ARG   A C    
263  O  O    . ARG   A 46  ? 0.58392 0.58388 0.88737 0.12756  -0.01365 -0.00817 151 ARG   A O    
264  C  CB   . ARG   A 46  ? 0.66612 0.59134 0.97339 0.12024  -0.02977 0.02014  151 ARG   A CB   
265  C  CG   . ARG   A 46  ? 0.73945 0.68016 1.03675 0.11493  -0.04568 0.05495  151 ARG   A CG   
266  C  CD   . ARG   A 46  ? 0.84427 0.78611 1.18699 0.13121  -0.05630 0.07749  151 ARG   A CD   
267  N  NE   . ARG   A 46  ? 0.87054 0.83834 1.20192 0.12590  -0.07178 0.10875  151 ARG   A NE   
268  C  CZ   . ARG   A 46  ? 0.89724 0.89779 1.24577 0.13427  -0.07817 0.11793  151 ARG   A CZ   
269  N  NH1  . ARG   A 46  ? 0.89715 0.90903 1.27670 0.14905  -0.06932 0.09925  151 ARG   A NH1  
270  N  NH2  . ARG   A 46  ? 0.88813 0.91365 1.22291 0.12709  -0.09319 0.14476  151 ARG   A NH2  
271  N  N    . ASP   A 47  ? 0.54386 0.54653 0.78392 0.10031  -0.02557 0.01322  152 ASP   A N    
272  C  CA   . ASP   A 47  ? 0.54777 0.58611 0.78814 0.10031  -0.02747 0.01714  152 ASP   A CA   
273  C  C    . ASP   A 47  ? 0.51533 0.57130 0.74107 0.09519  -0.01425 -0.00474 152 ASP   A C    
274  O  O    . ASP   A 47  ? 0.46497 0.55096 0.69913 0.09637  -0.01309 -0.00441 152 ASP   A O    
275  C  CB   . ASP   A 47  ? 0.60084 0.65040 0.81591 0.08787  -0.04042 0.03737  152 ASP   A CB   
276  C  CG   . ASP   A 47  ? 0.67407 0.71664 0.90201 0.09155  -0.05471 0.06351  152 ASP   A CG   
277  O  OD1  . ASP   A 47  ? 0.67357 0.70977 0.93896 0.10641  -0.05702 0.07033  152 ASP   A OD1  
278  O  OD2  . ASP   A 47  ? 0.69571 0.74075 0.89750 0.07965  -0.06350 0.07761  152 ASP   A OD2  
279  N  N    . PHE   A 48  ? 0.44209 0.48272 0.64686 0.08836  -0.00506 -0.02181 153 PHE   A N    
280  C  CA   . PHE   A 48  ? 0.39400 0.45382 0.58249 0.08195  0.00642  -0.03880 153 PHE   A CA   
281  C  C    . PHE   A 48  ? 0.42343 0.50037 0.63999 0.09462  0.01881  -0.05641 153 PHE   A C    
282  O  O    . PHE   A 48  ? 0.43887 0.50381 0.68686 0.10899  0.02044  -0.06188 153 PHE   A O    
283  C  CB   . PHE   A 48  ? 0.36480 0.40712 0.52389 0.07113  0.01140  -0.05100 153 PHE   A CB   
284  C  CG   . PHE   A 48  ? 0.39593 0.42189 0.53055 0.05981  0.00135  -0.03673 153 PHE   A CG   
285  C  CD1  . PHE   A 48  ? 0.42082 0.42598 0.53794 0.05244  0.00310  -0.04426 153 PHE   A CD1  
286  C  CD2  . PHE   A 48  ? 0.40671 0.44156 0.53618 0.05585  -0.00933 -0.01782 153 PHE   A CD2  
287  C  CE1  . PHE   A 48  ? 0.43959 0.43387 0.53664 0.04243  -0.00462 -0.03213 153 PHE   A CE1  
288  C  CE2  . PHE   A 48  ? 0.42066 0.44448 0.52792 0.04579  -0.01663 -0.00784 153 PHE   A CE2  
289  C  CZ   . PHE   A 48  ? 0.46927 0.47329 0.56118 0.03954  -0.01375 -0.01450 153 PHE   A CZ   
290  N  N    . ARG   A 49  ? 0.37705 0.48341 0.58417 0.08912  0.02796  -0.06503 154 ARG   A N    
291  C  CA   . ARG   A 49  ? 0.42436 0.55167 0.65134 0.09851  0.04317  -0.08608 154 ARG   A CA   
292  C  C    . ARG   A 49  ? 0.47864 0.58364 0.70081 0.10086  0.05192  -0.10970 154 ARG   A C    
293  O  O    . ARG   A 49  ? 0.45840 0.54617 0.64961 0.08867  0.04980  -0.11154 154 ARG   A O    
294  C  CB   . ARG   A 49  ? 0.42677 0.59112 0.63837 0.08807  0.05175  -0.08857 154 ARG   A CB   
295  C  CG   . ARG   A 49  ? 0.44395 0.63609 0.67221 0.08767  0.04602  -0.07107 154 ARG   A CG   
296  C  CD   . ARG   A 49  ? 0.44799 0.66972 0.65759 0.07264  0.05158  -0.06785 154 ARG   A CD   
297  N  NE   . ARG   A 49  ? 0.42403 0.62790 0.60018 0.05701  0.04259  -0.05647 154 ARG   A NE   
298  C  CZ   . ARG   A 49  ? 0.40203 0.62173 0.55943 0.04251  0.04503  -0.05097 154 ARG   A CZ   
299  N  NH1  . ARG   A 49  ? 0.39650 0.65232 0.56209 0.03964  0.05642  -0.05408 154 ARG   A NH1  
300  N  NH2  . ARG   A 49  ? 0.38093 0.58159 0.51373 0.03090  0.03625  -0.04139 154 ARG   A NH2  
301  N  N    . PRO   A 50  ? 0.53967 0.64484 0.79429 0.11635  0.06146  -0.12937 155 PRO   A N    
302  C  CA   . PRO   A 50  ? 0.54732 0.62345 0.80387 0.11922  0.06678  -0.15213 155 PRO   A CA   
303  C  C    . PRO   A 50  ? 0.58763 0.67714 0.80828 0.10559  0.07752  -0.17327 155 PRO   A C    
304  O  O    . PRO   A 50  ? 0.53351 0.66151 0.74022 0.09987  0.08653  -0.17728 155 PRO   A O    
305  C  CB   . PRO   A 50  ? 0.56162 0.64179 0.86675 0.14042  0.07601  -0.17062 155 PRO   A CB   
306  C  CG   . PRO   A 50  ? 0.59083 0.71667 0.90828 0.14484  0.08188  -0.16547 155 PRO   A CG   
307  C  CD   . PRO   A 50  ? 0.55765 0.68932 0.85297 0.13244  0.06738  -0.13256 155 PRO   A CD   
308  N  N    . PRO   A 51  ? 0.58406 0.64518 0.78943 0.09885  0.07619  -0.18546 156 PRO   A N    
309  C  CA   . PRO   A 51  ? 0.61128 0.68873 0.78486 0.08647  0.08588  -0.20786 156 PRO   A CA   
310  C  C    . PRO   A 51  ? 0.60233 0.70025 0.79441 0.09641  0.10331  -0.24340 156 PRO   A C    
311  O  O    . PRO   A 51  ? 0.57695 0.65504 0.80707 0.11205  0.10664  -0.25930 156 PRO   A O    
312  C  CB   . PRO   A 51  ? 0.61314 0.65277 0.77239 0.07739  0.07755  -0.21015 156 PRO   A CB   
313  C  CG   . PRO   A 51  ? 0.63340 0.63494 0.82677 0.08886  0.06845  -0.19855 156 PRO   A CG   
314  C  CD   . PRO   A 51  ? 0.62733 0.64287 0.84727 0.10199  0.06589  -0.17950 156 PRO   A CD   
315  N  N    . VAL   A 52  ? 0.60859 0.74817 0.77504 0.08726  0.11465  -0.25548 157 VAL   A N    
316  C  CA   . VAL   A 52  ? 0.64704 0.81590 0.82307 0.09361  0.13343  -0.29222 157 VAL   A CA   
317  C  C    . VAL   A 52  ? 0.71894 0.90254 0.85315 0.07622  0.13812  -0.31138 157 VAL   A C    
318  O  O    . VAL   A 52  ? 0.64996 0.86045 0.74818 0.06050  0.13578  -0.29399 157 VAL   A O    
319  C  CB   . VAL   A 52  ? 0.64342 0.86185 0.83038 0.09880  0.14472  -0.28782 157 VAL   A CB   
320  C  CG1  . VAL   A 52  ? 0.68365 0.94077 0.87374 0.10264  0.16629  -0.32769 157 VAL   A CG1  
321  C  CG2  . VAL   A 52  ? 0.65499 0.86224 0.88717 0.11669  0.13927  -0.27099 157 VAL   A CG2  
322  N  N    . ARG   A 53  ? 0.80755 0.97354 0.94848 0.07861  0.14364  -0.34644 158 ARG   A N    
323  C  CA   . ARG   A 53  ? 0.85960 1.04075 0.96262 0.06169  0.14684  -0.36781 158 ARG   A CA   
324  C  C    . ARG   A 53  ? 0.96415 1.17756 1.06916 0.06343  0.16016  -0.39195 158 ARG   A C    
325  O  O    . ARG   A 53  ? 0.99125 1.18258 1.12358 0.07319  0.16336  -0.41507 158 ARG   A O    
326  C  CB   . ARG   A 53  ? 0.83876 0.97088 0.94333 0.05683  0.13591  -0.37689 158 ARG   A CB   
327  C  CG   . ARG   A 53  ? 0.78238 0.88962 0.86771 0.04570  0.11825  -0.34202 158 ARG   A CG   
328  C  CD   . ARG   A 53  ? 0.77130 0.82337 0.88991 0.05502  0.10701  -0.32954 158 ARG   A CD   
329  N  NE   . ARG   A 53  ? 0.75077 0.78327 0.84989 0.04356  0.09089  -0.29571 158 ARG   A NE   
330  C  CZ   . ARG   A 53  ? 0.69227 0.68849 0.81166 0.04898  0.07953  -0.27100 158 ARG   A CZ   
331  N  NH1  . ARG   A 53  ? 0.63137 0.60498 0.79235 0.06581  0.08070  -0.27287 158 ARG   A NH1  
332  N  NH2  . ARG   A 53  ? 0.62114 0.60636 0.72028 0.03773  0.06702  -0.24385 158 ARG   A NH2  
333  N  N    . MET   A 54  ? 1.05495 1.32091 1.13233 0.05350  0.16771  -0.38547 159 MET   A N    
334  C  CA   . MET   A 54  ? 1.16320 1.46696 1.23973 0.05371  0.18112  -0.40648 159 MET   A CA   
335  C  C    . MET   A 54  ? 1.19125 1.53879 1.22013 0.03201  0.18199  -0.40398 159 MET   A C    
336  O  O    . MET   A 54  ? 1.21489 1.60991 1.23408 0.02807  0.19232  -0.40417 159 MET   A O    
337  C  CB   . MET   A 54  ? 1.19315 1.52420 1.29674 0.06721  0.19168  -0.39817 159 MET   A CB   
338  C  CG   . MET   A 54  ? 1.25311 1.55456 1.40909 0.09041  0.19520  -0.41290 159 MET   A CG   
339  S  SD   . MET   A 54  ? 1.30141 1.64261 1.49053 0.10554  0.20774  -0.40414 159 MET   A SD   
340  C  CE   . MET   A 54  ? 1.24288 1.62868 1.39571 0.08755  0.20624  -0.36896 159 MET   A CE   
341  N  N    . PRO   A 67  ? 0.99116 1.55236 0.92243 -0.03581 0.17924  -0.20934 219 PRO   A N    
342  C  CA   . PRO   A 67  ? 0.95207 1.49329 0.92410 -0.01663 0.18483  -0.21818 219 PRO   A CA   
343  C  C    . PRO   A 67  ? 0.89137 1.38773 0.87350 -0.01256 0.17042  -0.19961 219 PRO   A C    
344  O  O    . PRO   A 67  ? 0.95216 1.43417 0.96433 -0.00424 0.16621  -0.18344 219 PRO   A O    
345  C  CB   . PRO   A 67  ? 0.97797 1.50001 0.96473 -0.00158 0.19188  -0.26032 219 PRO   A CB   
346  C  CG   . PRO   A 67  ? 1.02144 1.56203 0.97427 -0.01483 0.19212  -0.27481 219 PRO   A CG   
347  C  CD   . PRO   A 67  ? 1.02240 1.57320 0.94059 -0.03439 0.17991  -0.24311 219 PRO   A CD   
348  N  N    . LEU   A 68  ? 0.75438 1.21903 0.71299 -0.01918 0.15706  -0.19710 220 LEU   A N    
349  C  CA   . LEU   A 68  ? 0.63506 1.04482 0.60108 -0.01663 0.13753  -0.17561 220 LEU   A CA   
350  C  C    . LEU   A 68  ? 0.51911 0.88987 0.52179 0.00297  0.13601  -0.18784 220 LEU   A C    
351  O  O    . LEU   A 68  ? 0.44335 0.79265 0.46617 0.00793  0.12660  -0.16600 220 LEU   A O    
352  C  CB   . LEU   A 68  ? 0.65001 1.06398 0.61466 -0.02713 0.12727  -0.13445 220 LEU   A CB   
353  C  CG   . LEU   A 68  ? 0.67842 1.12593 0.61147 -0.04684 0.12507  -0.11309 220 LEU   A CG   
354  C  CD1  . LEU   A 68  ? 0.62797 1.05359 0.56475 -0.05439 0.10872  -0.07481 220 LEU   A CD1  
355  C  CD2  . LEU   A 68  ? 0.69100 1.14035 0.59279 -0.05361 0.12302  -0.12979 220 LEU   A CD2  
356  N  N    . SER   A 69  ? 0.53387 0.89563 0.54592 0.01361  0.14455  -0.22327 221 SER   A N    
357  C  CA   . SER   A 69  ? 0.56496 0.89573 0.61684 0.03348  0.14505  -0.23571 221 SER   A CA   
358  C  C    . SER   A 69  ? 0.56549 0.84124 0.62547 0.03696  0.12647  -0.21718 221 SER   A C    
359  O  O    . SER   A 69  ? 0.53085 0.78304 0.62413 0.05173  0.12317  -0.21521 221 SER   A O    
360  C  CB   . SER   A 69  ? 0.64981 0.98050 0.71188 0.04318  0.15815  -0.27934 221 SER   A CB   
361  O  OG   . SER   A 69  ? 0.65424 0.97018 0.68716 0.03230  0.15352  -0.29338 221 SER   A OG   
362  N  N    . MET   A 70  ? 0.52471 0.78283 0.55624 0.02383  0.11437  -0.20295 222 MET   A N    
363  C  CA   . MET   A 70  ? 0.48494 0.69607 0.52141 0.02560  0.09827  -0.18667 222 MET   A CA   
364  C  C    . MET   A 70  ? 0.44021 0.64934 0.47276 0.01945  0.08680  -0.15203 222 MET   A C    
365  O  O    . MET   A 70  ? 0.46811 0.64360 0.50375 0.02042  0.07417  -0.13802 222 MET   A O    
366  C  CB   . MET   A 70  ? 0.54602 0.73721 0.55878 0.01613  0.09226  -0.19614 222 MET   A CB   
367  C  CG   . MET   A 70  ? 0.60105 0.77376 0.62630 0.02343  0.09845  -0.22998 222 MET   A CG   
368  S  SD   . MET   A 70  ? 0.53407 0.65893 0.60236 0.04159  0.09286  -0.22878 222 MET   A SD   
369  C  CE   . MET   A 70  ? 0.51488 0.60196 0.56831 0.03168  0.07438  -0.20303 222 MET   A CE   
370  N  N    . LEU   A 71  ? 0.44216 0.68718 0.46908 0.01234  0.09119  -0.13867 223 LEU   A N    
371  C  CA   . LEU   A 71  ? 0.40674 0.64816 0.43337 0.00560  0.08024  -0.10824 223 LEU   A CA   
372  C  C    . LEU   A 71  ? 0.36915 0.58877 0.42322 0.01625  0.07274  -0.09870 223 LEU   A C    
373  O  O    . LEU   A 71  ? 0.40459 0.60009 0.45502 0.01276  0.05978  -0.08190 223 LEU   A O    
374  C  CB   . LEU   A 71  ? 0.40074 0.68540 0.42193 -0.00457 0.08717  -0.09565 223 LEU   A CB   
375  C  CG   . LEU   A 71  ? 0.43175 0.71199 0.45445 -0.01377 0.07580  -0.06535 223 LEU   A CG   
376  C  CD1  . LEU   A 71  ? 0.41908 0.66866 0.42393 -0.02006 0.06240  -0.05490 223 LEU   A CD1  
377  C  CD2  . LEU   A 71  ? 0.41696 0.73936 0.43524 -0.02619 0.08251  -0.05055 223 LEU   A CD2  
378  N  N    . PRO   A 72  ? 0.35272 0.58222 0.43507 0.02909  0.07967  -0.10813 224 PRO   A N    
379  C  CA   . PRO   A 72  ? 0.37574 0.58806 0.48307 0.03794  0.06984  -0.09531 224 PRO   A CA   
380  C  C    . PRO   A 72  ? 0.40572 0.57546 0.51160 0.04235  0.05845  -0.09354 224 PRO   A C    
381  O  O    . PRO   A 72  ? 0.38021 0.53485 0.48615 0.03988  0.04605  -0.07561 224 PRO   A O    
382  C  CB   . PRO   A 72  ? 0.41706 0.65083 0.55716 0.05246  0.08064  -0.10883 224 PRO   A CB   
383  C  CG   . PRO   A 72  ? 0.42427 0.69713 0.55450 0.04704  0.09679  -0.12265 224 PRO   A CG   
384  C  CD   . PRO   A 72  ? 0.37122 0.63284 0.46616 0.03612  0.09651  -0.12977 224 PRO   A CD   
385  N  N    . HIS   A 73  ? 0.42652 0.57810 0.53153 0.04772  0.06263  -0.11241 225 HIS   A N    
386  C  CA   . HIS   A 73  ? 0.47853 0.59083 0.58406 0.05029  0.05239  -0.10891 225 HIS   A CA   
387  C  C    . HIS   A 73  ? 0.40260 0.50219 0.47902 0.03645  0.04308  -0.09570 225 HIS   A C    
388  O  O    . HIS   A 73  ? 0.41759 0.49701 0.49392 0.03564  0.03206  -0.08073 225 HIS   A O    
389  C  CB   . HIS   A 73  ? 0.47781 0.57319 0.59122 0.05690  0.05929  -0.13352 225 HIS   A CB   
390  C  CG   . HIS   A 73  ? 0.48704 0.54237 0.60492 0.05836  0.04936  -0.12846 225 HIS   A CG   
391  N  ND1  . HIS   A 73  ? 0.45264 0.48904 0.59875 0.06971  0.04240  -0.11715 225 HIS   A ND1  
392  C  CD2  . HIS   A 73  ? 0.47001 0.50350 0.56877 0.04883  0.04487  -0.13091 225 HIS   A CD2  
393  C  CE1  . HIS   A 73  ? 0.46579 0.46992 0.60899 0.06640  0.03464  -0.11193 225 HIS   A CE1  
394  N  NE2  . HIS   A 73  ? 0.48386 0.48565 0.59921 0.05374  0.03637  -0.12107 225 HIS   A NE2  
395  N  N    . LEU   A 74  ? 0.39480 0.50915 0.44714 0.02556  0.04738  -0.10072 226 LEU   A N    
396  C  CA   . LEU   A 74  ? 0.41787 0.52175 0.44712 0.01396  0.03866  -0.08878 226 LEU   A CA   
397  C  C    . LEU   A 74  ? 0.38241 0.49248 0.41143 0.00924  0.03116  -0.06726 226 LEU   A C    
398  O  O    . LEU   A 74  ? 0.39048 0.48487 0.41013 0.00401  0.02214  -0.05667 226 LEU   A O    
399  C  CB   . LEU   A 74  ? 0.47506 0.59611 0.48114 0.00393  0.04378  -0.09790 226 LEU   A CB   
400  C  CG   . LEU   A 74  ? 0.53674 0.64877 0.53847 0.00485  0.04889  -0.12197 226 LEU   A CG   
401  C  CD1  . LEU   A 74  ? 0.51646 0.64213 0.49082 -0.00825 0.04792  -0.12504 226 LEU   A CD1  
402  C  CD2  . LEU   A 74  ? 0.50267 0.57697 0.51703 0.01035  0.04218  -0.12316 226 LEU   A CD2  
403  N  N    . ALA   A 75  ? 0.37996 0.51368 0.42116 0.01054  0.03507  -0.06208 227 ALA   A N    
404  C  CA   . ALA   A 75  ? 0.30881 0.44596 0.35457 0.00563  0.02718  -0.04399 227 ALA   A CA   
405  C  C    . ALA   A 75  ? 0.33408 0.45127 0.39134 0.01177  0.01767  -0.03803 227 ALA   A C    
406  O  O    . ALA   A 75  ? 0.34488 0.45230 0.39641 0.00624  0.00864  -0.02778 227 ALA   A O    
407  C  CB   . ALA   A 75  ? 0.29594 0.46480 0.35535 0.00424  0.03353  -0.03980 227 ALA   A CB   
408  N  N    . ASP   A 76  ? 0.38249 0.49516 0.45713 0.02325  0.01948  -0.04434 228 ASP   A N    
409  C  CA   . ASP   A 76  ? 0.36089 0.45778 0.44551 0.02854  0.00949  -0.03548 228 ASP   A CA   
410  C  C    . ASP   A 76  ? 0.35230 0.42257 0.42038 0.02494  0.00375  -0.03394 228 ASP   A C    
411  O  O    . ASP   A 76  ? 0.36433 0.42696 0.42822 0.02210  -0.00546 -0.02326 228 ASP   A O    
412  C  CB   . ASP   A 76  ? 0.35140 0.44972 0.46287 0.04258  0.01216  -0.03990 228 ASP   A CB   
413  C  CG   . ASP   A 76  ? 0.40063 0.52901 0.53379 0.04680  0.01553  -0.03787 228 ASP   A CG   
414  O  OD1  . ASP   A 76  ? 0.39688 0.53305 0.55479 0.05920  0.02153  -0.04562 228 ASP   A OD1  
415  O  OD2  . ASP   A 76  ? 0.38226 0.52662 0.51079 0.03768  0.01223  -0.02901 228 ASP   A OD2  
416  N  N    . LEU   A 77  ? 0.35632 0.41542 0.41512 0.02410  0.00935  -0.04556 229 LEU   A N    
417  C  CA   . LEU   A 77  ? 0.35255 0.38947 0.39740 0.01912  0.00461  -0.04422 229 LEU   A CA   
418  C  C    . LEU   A 77  ? 0.37043 0.41022 0.39757 0.00907  -0.00060 -0.03588 229 LEU   A C    
419  O  O    . LEU   A 77  ? 0.36291 0.39206 0.38480 0.00642  -0.00735 -0.02816 229 LEU   A O    
420  C  CB   . LEU   A 77  ? 0.35647 0.38538 0.39582 0.01811  0.01150  -0.06054 229 LEU   A CB   
421  C  CG   . LEU   A 77  ? 0.41169 0.42261 0.43665 0.01041  0.00785  -0.06140 229 LEU   A CG   
422  C  CD1  . LEU   A 77  ? 0.43001 0.41982 0.46370 0.01274  0.00105  -0.05096 229 LEU   A CD1  
423  C  CD2  . LEU   A 77  ? 0.46865 0.47679 0.48987 0.00837  0.01458  -0.08076 229 LEU   A CD2  
424  N  N    . VAL   A 78  ? 0.37110 0.42672 0.39071 0.00347  0.00270  -0.03689 230 VAL   A N    
425  C  CA   . VAL   A 78  ? 0.34981 0.40658 0.35887 -0.00467 -0.00243 -0.02891 230 VAL   A CA   
426  C  C    . VAL   A 78  ? 0.39179 0.44981 0.40868 -0.00467 -0.00921 -0.02016 230 VAL   A C    
427  O  O    . VAL   A 78  ? 0.39025 0.44033 0.40129 -0.00816 -0.01485 -0.01688 230 VAL   A O    
428  C  CB   . VAL   A 78  ? 0.40669 0.48105 0.41011 -0.01071 0.00161  -0.02783 230 VAL   A CB   
429  C  CG1  . VAL   A 78  ? 0.41543 0.49025 0.41804 -0.01723 -0.00467 -0.01695 230 VAL   A CG1  
430  C  CG2  . VAL   A 78  ? 0.47031 0.54544 0.46026 -0.01364 0.00570  -0.03662 230 VAL   A CG2  
431  N  N    . SER   A 79  ? 0.35711 0.42811 0.38820 -0.00116 -0.00852 -0.01794 231 SER   A N    
432  C  CA   . SER   A 79  ? 0.31623 0.39197 0.35533 -0.00253 -0.01597 -0.01135 231 SER   A CA   
433  C  C    . SER   A 79  ? 0.34687 0.41133 0.38228 0.00012  -0.02244 -0.00889 231 SER   A C    
434  O  O    . SER   A 79  ? 0.34601 0.40998 0.37613 -0.00461 -0.02874 -0.00681 231 SER   A O    
435  C  CB   . SER   A 79  ? 0.31538 0.41031 0.37311 0.00103  -0.01426 -0.00933 231 SER   A CB   
436  O  OG   . SER   A 79  ? 0.39153 0.49483 0.45731 -0.00313 -0.02219 -0.00399 231 SER   A OG   
437  N  N    . TYR   A 80  ? 0.31334 0.36956 0.35247 0.00716  -0.02076 -0.00924 232 TYR   A N    
438  C  CA   . TYR   A 80  ? 0.29859 0.34463 0.33405 0.00834  -0.02677 -0.00283 232 TYR   A CA   
439  C  C    . TYR   A 80  ? 0.34192 0.37860 0.35929 0.00095  -0.02775 -0.00412 232 TYR   A C    
440  O  O    . TYR   A 80  ? 0.31639 0.35542 0.32667 -0.00245 -0.03335 0.00082  232 TYR   A O    
441  C  CB   . TYR   A 80  ? 0.36903 0.40297 0.41559 0.01652  -0.02400 -0.00276 232 TYR   A CB   
442  C  CG   . TYR   A 80  ? 0.42886 0.45025 0.47385 0.01672  -0.02984 0.00764  232 TYR   A CG   
443  C  CD1  . TYR   A 80  ? 0.41626 0.44573 0.47065 0.02021  -0.03816 0.02141  232 TYR   A CD1  
444  C  CD2  . TYR   A 80  ? 0.48451 0.48870 0.51974 0.01237  -0.02755 0.00558  232 TYR   A CD2  
445  C  CE1  . TYR   A 80  ? 0.46673 0.48761 0.51931 0.01907  -0.04386 0.03495  232 TYR   A CE1  
446  C  CE2  . TYR   A 80  ? 0.47765 0.47199 0.51281 0.01079  -0.03246 0.01784  232 TYR   A CE2  
447  C  CZ   . TYR   A 80  ? 0.47193 0.47465 0.51518 0.01407  -0.04048 0.03353  232 TYR   A CZ   
448  O  OH   . TYR   A 80  ? 0.54240 0.53820 0.58504 0.01116  -0.04582 0.04969  232 TYR   A OH   
449  N  N    . SER   A 81  ? 0.39606 0.42610 0.40610 -0.00189 -0.02231 -0.01108 233 SER   A N    
450  C  CA   . SER   A 81  ? 0.37675 0.39996 0.37387 -0.00778 -0.02301 -0.01215 233 SER   A CA   
451  C  C    . SER   A 81  ? 0.38684 0.41794 0.38049 -0.01246 -0.02589 -0.01315 233 SER   A C    
452  O  O    . SER   A 81  ? 0.37064 0.40096 0.35711 -0.01581 -0.02769 -0.01378 233 SER   A O    
453  C  CB   . SER   A 81  ? 0.54305 0.55954 0.53544 -0.00959 -0.01785 -0.01877 233 SER   A CB   
454  O  OG   . SER   A 81  ? 0.59974 0.60622 0.59813 -0.00551 -0.01518 -0.02136 233 SER   A OG   
455  N  N    . ILE   A 82  ? 0.33959 0.37881 0.34064 -0.01303 -0.02595 -0.01384 234 ILE   A N    
456  C  CA   . ILE   A 82  ? 0.38496 0.42827 0.38857 -0.01737 -0.02963 -0.01559 234 ILE   A CA   
457  C  C    . ILE   A 82  ? 0.40175 0.45022 0.40301 -0.01833 -0.03494 -0.01663 234 ILE   A C    
458  O  O    . ILE   A 82  ? 0.35964 0.40874 0.35694 -0.02157 -0.03663 -0.02239 234 ILE   A O    
459  C  CB   . ILE   A 82  ? 0.35226 0.40329 0.36789 -0.01930 -0.02948 -0.01343 234 ILE   A CB   
460  C  CG1  . ILE   A 82  ? 0.35674 0.40768 0.37097 -0.02066 -0.02474 -0.01097 234 ILE   A CG1  
461  C  CG2  . ILE   A 82  ? 0.32395 0.37616 0.34762 -0.02415 -0.03460 -0.01631 234 ILE   A CG2  
462  C  CD1  . ILE   A 82  ? 0.37757 0.44080 0.40231 -0.02332 -0.02275 -0.00556 234 ILE   A CD1  
463  N  N    . GLN   A 83  ? 0.34597 0.40097 0.35039 -0.01531 -0.03769 -0.01142 235 GLN   A N    
464  C  CA   . GLN   A 83  ? 0.36464 0.42974 0.36420 -0.01721 -0.04404 -0.00982 235 GLN   A CA   
465  C  C    . GLN   A 83  ? 0.36835 0.43028 0.35334 -0.01911 -0.04313 -0.00886 235 GLN   A C    
466  O  O    . GLN   A 83  ? 0.34247 0.41481 0.31876 -0.02371 -0.04586 -0.01339 235 GLN   A O    
467  C  CB   . GLN   A 83  ? 0.34082 0.41460 0.34916 -0.01247 -0.04818 -0.00033 235 GLN   A CB   
468  C  CG   . GLN   A 83  ? 0.35293 0.43547 0.37815 -0.01081 -0.04838 -0.00070 235 GLN   A CG   
469  C  CD   . GLN   A 83  ? 0.39370 0.48999 0.43122 -0.00569 -0.05406 0.00848  235 GLN   A CD   
470  O  OE1  . GLN   A 83  ? 0.44319 0.55096 0.47601 -0.00780 -0.06229 0.01373  235 GLN   A OE1  
471  N  NE2  . GLN   A 83  ? 0.45990 0.55836 0.51402 0.00119  -0.04975 0.01056  235 GLN   A NE2  
472  N  N    . LYS   A 84  ? 0.38188 0.43167 0.36469 -0.01658 -0.03894 -0.00401 236 LYS   A N    
473  C  CA   . LYS   A 84  ? 0.38101 0.42889 0.35236 -0.02006 -0.03749 -0.00138 236 LYS   A CA   
474  C  C    . LYS   A 84  ? 0.38382 0.43350 0.34997 -0.02397 -0.03406 -0.01216 236 LYS   A C    
475  O  O    . LYS   A 84  ? 0.35244 0.41192 0.30935 -0.02805 -0.03354 -0.01409 236 LYS   A O    
476  C  CB   . LYS   A 84  ? 0.33086 0.36319 0.30530 -0.01780 -0.03417 0.00458  236 LYS   A CB   
477  C  CG   . LYS   A 84  ? 0.42355 0.45149 0.40910 -0.01190 -0.03719 0.01456  236 LYS   A CG   
478  C  CD   . LYS   A 84  ? 0.47264 0.51515 0.45531 -0.01308 -0.04469 0.02657  236 LYS   A CD   
479  C  CE   . LYS   A 84  ? 0.52306 0.55737 0.51795 -0.00812 -0.04832 0.04232  236 LYS   A CE   
480  N  NZ   . LYS   A 84  ? 0.54082 0.55630 0.53616 -0.01063 -0.04447 0.04623  236 LYS   A NZ   
481  N  N    . VAL   A 85  ? 0.32876 0.37162 0.30230 -0.02260 -0.03162 -0.01844 237 VAL   A N    
482  C  CA   . VAL   A 85  ? 0.35254 0.39624 0.32734 -0.02447 -0.02942 -0.02698 237 VAL   A CA   
483  C  C    . VAL   A 85  ? 0.35617 0.41019 0.33250 -0.02637 -0.03190 -0.03657 237 VAL   A C    
484  O  O    . VAL   A 85  ? 0.36902 0.42935 0.34357 -0.02780 -0.02953 -0.04516 237 VAL   A O    
485  C  CB   . VAL   A 85  ? 0.37910 0.41514 0.36310 -0.02293 -0.02816 -0.02721 237 VAL   A CB   
486  C  CG1  . VAL   A 85  ? 0.35785 0.39473 0.34997 -0.02333 -0.02797 -0.03383 237 VAL   A CG1  
487  C  CG2  . VAL   A 85  ? 0.39031 0.41979 0.37009 -0.02263 -0.02517 -0.02275 237 VAL   A CG2  
488  N  N    . ILE   A 86  ? 0.34114 0.39895 0.32241 -0.02674 -0.03641 -0.03720 238 ILE   A N    
489  C  CA   . ILE   A 86  ? 0.34350 0.41167 0.32665 -0.03009 -0.03966 -0.04938 238 ILE   A CA   
490  C  C    . ILE   A 86  ? 0.34123 0.42635 0.30777 -0.03337 -0.03988 -0.05173 238 ILE   A C    
491  O  O    . ILE   A 86  ? 0.40854 0.50388 0.37243 -0.03600 -0.03826 -0.06637 238 ILE   A O    
492  C  CB   . ILE   A 86  ? 0.35767 0.42897 0.35053 -0.03160 -0.04544 -0.04838 238 ILE   A CB   
493  C  CG1  . ILE   A 86  ? 0.41599 0.47467 0.42567 -0.03053 -0.04434 -0.04571 238 ILE   A CG1  
494  C  CG2  . ILE   A 86  ? 0.43035 0.51459 0.42359 -0.03692 -0.05007 -0.06293 238 ILE   A CG2  
495  C  CD1  . ILE   A 86  ? 0.39556 0.45903 0.41448 -0.03128 -0.04750 -0.03820 238 ILE   A CD1  
496  N  N    . GLY   A 87  ? 0.36122 0.45095 0.31770 -0.03337 -0.04167 -0.03713 239 GLY   A N    
497  C  CA   . GLY   A 87  ? 0.37255 0.48147 0.31223 -0.03802 -0.04254 -0.03399 239 GLY   A CA   
498  C  C    . GLY   A 87  ? 0.38901 0.50141 0.32155 -0.04006 -0.03502 -0.03866 239 GLY   A C    
499  O  O    . GLY   A 87  ? 0.38713 0.52103 0.30756 -0.04503 -0.03319 -0.04613 239 GLY   A O    
500  N  N    . PHE   A 88  ? 0.38989 0.48508 0.32996 -0.03691 -0.03039 -0.03509 240 PHE   A N    
501  C  CA   . PHE   A 88  ? 0.34034 0.44058 0.27831 -0.03875 -0.02346 -0.03983 240 PHE   A CA   
502  C  C    . PHE   A 88  ? 0.36748 0.47449 0.31385 -0.03716 -0.02031 -0.06054 240 PHE   A C    
503  O  O    . PHE   A 88  ? 0.41507 0.54110 0.35589 -0.03984 -0.01511 -0.07045 240 PHE   A O    
504  C  CB   . PHE   A 88  ? 0.33640 0.41823 0.28211 -0.03653 -0.02110 -0.03193 240 PHE   A CB   
505  C  CG   . PHE   A 88  ? 0.39239 0.48056 0.34042 -0.03846 -0.01492 -0.03627 240 PHE   A CG   
506  C  CD1  . PHE   A 88  ? 0.39132 0.49056 0.33032 -0.04475 -0.01151 -0.02762 240 PHE   A CD1  
507  C  CD2  . PHE   A 88  ? 0.41290 0.49728 0.37500 -0.03432 -0.01307 -0.04664 240 PHE   A CD2  
508  C  CE1  . PHE   A 88  ? 0.39273 0.50144 0.33646 -0.04722 -0.00553 -0.03135 240 PHE   A CE1  
509  C  CE2  . PHE   A 88  ? 0.37442 0.46779 0.34239 -0.03526 -0.00803 -0.04999 240 PHE   A CE2  
510  C  CZ   . PHE   A 88  ? 0.35041 0.45698 0.30910 -0.04188 -0.00384 -0.04333 240 PHE   A CZ   
511  N  N    . ALA   A 89  ? 0.36797 0.46044 0.33004 -0.03287 -0.02306 -0.06723 241 ALA   A N    
512  C  CA   . ALA   A 89  ? 0.37666 0.46952 0.35412 -0.03016 -0.02092 -0.08571 241 ALA   A CA   
513  C  C    . ALA   A 89  ? 0.40750 0.52019 0.37838 -0.03369 -0.02036 -0.10391 241 ALA   A C    
514  O  O    . ALA   A 89  ? 0.37658 0.49908 0.35471 -0.03213 -0.01483 -0.12189 241 ALA   A O    
515  C  CB   . ALA   A 89  ? 0.34620 0.41951 0.34263 -0.02687 -0.02553 -0.08486 241 ALA   A CB   
516  N  N    . LYS   A 90  ? 0.37213 0.49378 0.33021 -0.03841 -0.02611 -0.10074 242 LYS   A N    
517  C  CA   . LYS   A 90  ? 0.39162 0.53659 0.34015 -0.04370 -0.02694 -0.11898 242 LYS   A CA   
518  C  C    . LYS   A 90  ? 0.44300 0.61533 0.37392 -0.04737 -0.01940 -0.12425 242 LYS   A C    
519  O  O    . LYS   A 90  ? 0.43608 0.63047 0.36169 -0.05078 -0.01660 -0.14674 242 LYS   A O    
520  C  CB   . LYS   A 90  ? 0.37320 0.52743 0.31010 -0.04883 -0.03617 -0.10963 242 LYS   A CB   
521  C  CG   . LYS   A 90  ? 0.51739 0.65316 0.47270 -0.04731 -0.04311 -0.10889 242 LYS   A CG   
522  C  CD   . LYS   A 90  ? 0.61381 0.76856 0.56215 -0.05415 -0.05203 -0.11341 242 LYS   A CD   
523  C  CE   . LYS   A 90  ? 0.62627 0.80035 0.55370 -0.05673 -0.05645 -0.09235 242 LYS   A CE   
524  N  NZ   . LYS   A 90  ? 0.65448 0.84143 0.58317 -0.06076 -0.06759 -0.08742 242 LYS   A NZ   
525  N  N    . MET   A 91  ? 0.43822 0.61139 0.36072 -0.04776 -0.01563 -0.10519 243 MET   A N    
526  C  CA   . MET   A 91  ? 0.45806 0.65986 0.36408 -0.05322 -0.00809 -0.10527 243 MET   A CA   
527  C  C    . MET   A 91  ? 0.41979 0.62291 0.34023 -0.04889 0.00202  -0.11676 243 MET   A C    
528  O  O    . MET   A 91  ? 0.45035 0.67996 0.36011 -0.05362 0.01001  -0.11737 243 MET   A O    
529  C  CB   . MET   A 91  ? 0.55499 0.75874 0.44576 -0.05831 -0.01074 -0.07523 243 MET   A CB   
530  C  CG   . MET   A 91  ? 0.64231 0.84261 0.52538 -0.06006 -0.02175 -0.06011 243 MET   A CG   
531  S  SD   . MET   A 91  ? 0.66435 0.86330 0.53707 -0.06440 -0.02570 -0.02406 243 MET   A SD   
532  C  CE   . MET   A 91  ? 0.66349 0.90748 0.51079 -0.07631 -0.02045 -0.02097 243 MET   A CE   
533  N  N    . ILE   A 92  ? 0.40079 0.57921 0.34644 -0.04047 0.00162  -0.12404 244 ILE   A N    
534  C  CA   . ILE   A 92  ? 0.40943 0.59035 0.37409 -0.03483 0.00959  -0.13437 244 ILE   A CA   
535  C  C    . ILE   A 92  ? 0.42142 0.62706 0.39063 -0.03370 0.01713  -0.16444 244 ILE   A C    
536  O  O    . ILE   A 92  ? 0.44039 0.64059 0.41703 -0.03200 0.01372  -0.18330 244 ILE   A O    
537  C  CB   . ILE   A 92  ? 0.39939 0.54963 0.39094 -0.02629 0.00515  -0.13172 244 ILE   A CB   
538  C  CG1  . ILE   A 92  ? 0.34035 0.47163 0.32601 -0.02786 -0.00020 -0.10576 244 ILE   A CG1  
539  C  CG2  . ILE   A 92  ? 0.40263 0.55871 0.41867 -0.01913 0.01185  -0.14351 244 ILE   A CG2  
540  C  CD1  . ILE   A 92  ? 0.29768 0.40334 0.30374 -0.02175 -0.00574 -0.10072 244 ILE   A CD1  
541  N  N    . PRO   A 93  ? 0.44173 0.67625 0.40828 -0.03516 0.02790  -0.17155 245 PRO   A N    
542  C  CA   . PRO   A 93  ? 0.47249 0.73419 0.44502 -0.03315 0.03715  -0.20454 245 PRO   A CA   
543  C  C    . PRO   A 93  ? 0.54440 0.78373 0.55378 -0.02119 0.03620  -0.22764 245 PRO   A C    
544  O  O    . PRO   A 93  ? 0.52919 0.75188 0.56632 -0.01230 0.03645  -0.22216 245 PRO   A O    
545  C  CB   . PRO   A 93  ? 0.51954 0.81259 0.49068 -0.03507 0.04943  -0.20268 245 PRO   A CB   
546  C  CG   . PRO   A 93  ? 0.49012 0.78020 0.44008 -0.04424 0.04531  -0.16756 245 PRO   A CG   
547  C  CD   . PRO   A 93  ? 0.40432 0.65105 0.36170 -0.04028 0.03256  -0.15043 245 PRO   A CD   
548  N  N    . GLY   A 94  ? 0.59390 0.83279 0.60538 -0.02165 0.03393  -0.25239 246 GLY   A N    
549  C  CA   . GLY   A 94  ? 0.58682 0.80213 0.63633 -0.01157 0.03228  -0.27527 246 GLY   A CA   
550  C  C    . GLY   A 94  ? 0.58804 0.76391 0.64968 -0.01105 0.01891  -0.26229 246 GLY   A C    
551  O  O    . GLY   A 94  ? 0.63935 0.79518 0.73158 -0.00560 0.01603  -0.28122 246 GLY   A O    
552  N  N    . PHE   A 95  ? 0.54181 0.70669 0.58290 -0.01674 0.01116  -0.23107 247 PHE   A N    
553  C  CA   . PHE   A 95  ? 0.48657 0.61830 0.53995 -0.01639 0.00002  -0.21690 247 PHE   A CA   
554  C  C    . PHE   A 95  ? 0.59416 0.72330 0.64927 -0.02178 -0.00564 -0.23660 247 PHE   A C    
555  O  O    . PHE   A 95  ? 0.61091 0.71360 0.69411 -0.01925 -0.01163 -0.24083 247 PHE   A O    
556  C  CB   . PHE   A 95  ? 0.47609 0.60240 0.50620 -0.02119 -0.00520 -0.18391 247 PHE   A CB   
557  C  CG   . PHE   A 95  ? 0.47262 0.57090 0.51379 -0.02113 -0.01472 -0.16849 247 PHE   A CG   
558  C  CD1  . PHE   A 95  ? 0.45103 0.52711 0.51553 -0.01488 -0.01684 -0.15593 247 PHE   A CD1  
559  C  CD2  . PHE   A 95  ? 0.49721 0.59574 0.52571 -0.02800 -0.02165 -0.16534 247 PHE   A CD2  
560  C  CE1  . PHE   A 95  ? 0.51379 0.56931 0.58684 -0.01624 -0.02444 -0.14070 247 PHE   A CE1  
561  C  CE2  . PHE   A 95  ? 0.49335 0.57070 0.53334 -0.02855 -0.02899 -0.15124 247 PHE   A CE2  
562  C  CZ   . PHE   A 95  ? 0.49621 0.55249 0.55750 -0.02307 -0.02975 -0.13898 247 PHE   A CZ   
563  N  N    . ARG   A 96  ? 0.56478 0.72281 0.59084 -0.03052 -0.00463 -0.24749 248 ARG   A N    
564  C  CA   . ARG   A 96  ? 0.62982 0.79113 0.65396 -0.03794 -0.01133 -0.26657 248 ARG   A CA   
565  C  C    . ARG   A 96  ? 0.63563 0.79831 0.68455 -0.03512 -0.00659 -0.30765 248 ARG   A C    
566  O  O    . ARG   A 96  ? 0.68836 0.85004 0.74201 -0.04177 -0.01267 -0.32809 248 ARG   A O    
567  C  CB   . ARG   A 96  ? 0.72459 0.92055 0.70794 -0.04895 -0.01367 -0.26103 248 ARG   A CB   
568  C  CG   . ARG   A 96  ? 0.90894 1.10565 0.88833 -0.05780 -0.02523 -0.26638 248 ARG   A CG   
569  C  CD   . ARG   A 96  ? 0.97942 1.14619 0.97086 -0.05642 -0.03453 -0.23745 248 ARG   A CD   
570  N  NE   . ARG   A 96  ? 1.03194 1.19191 1.03509 -0.06338 -0.04494 -0.24594 248 ARG   A NE   
571  C  CZ   . ARG   A 96  ? 1.05948 1.20742 1.08871 -0.06529 -0.04664 -0.27445 248 ARG   A CZ   
572  N  NH1  . ARG   A 96  ? 1.03877 1.18245 1.07777 -0.07375 -0.05701 -0.27814 248 ARG   A NH1  
573  N  NH2  . ARG   A 96  ? 1.07987 1.21922 1.12947 -0.05872 -0.03838 -0.29897 248 ARG   A NH2  
574  N  N    . ASP   A 97  ? 0.63513 0.79912 0.70410 -0.02516 0.00369  -0.32115 249 ASP   A N    
575  C  CA   . ASP   A 97  ? 0.65823 0.81517 0.76232 -0.01901 0.00815  -0.35994 249 ASP   A CA   
576  C  C    . ASP   A 97  ? 0.63474 0.74587 0.78264 -0.01363 -0.00069 -0.35567 249 ASP   A C    
577  O  O    . ASP   A 97  ? 0.64693 0.74582 0.82724 -0.01030 -0.00017 -0.37996 249 ASP   A O    
578  C  CB   . ASP   A 97  ? 0.77900 0.95276 0.89677 -0.00817 0.02197  -0.37252 249 ASP   A CB   
579  C  CG   . ASP   A 97  ? 0.86164 1.08442 0.94376 -0.01487 0.03213  -0.37812 249 ASP   A CG   
580  O  OD1  . ASP   A 97  ? 0.90958 1.15211 0.95799 -0.02717 0.02784  -0.37373 249 ASP   A OD1  
581  O  OD2  . ASP   A 97  ? 0.90615 1.14935 0.99601 -0.00817 0.04392  -0.38495 249 ASP   A OD2  
582  N  N    . LEU   A 98  ? 0.55319 0.64084 0.70281 -0.01307 -0.00843 -0.31762 250 LEU   A N    
583  C  CA   . LEU   A 98  ? 0.55096 0.59903 0.73937 -0.00976 -0.01701 -0.30645 250 LEU   A CA   
584  C  C    . LEU   A 98  ? 0.54769 0.58536 0.73565 -0.02161 -0.02705 -0.31070 250 LEU   A C    
585  O  O    . LEU   A 98  ? 0.58932 0.65004 0.74283 -0.03193 -0.02932 -0.31274 250 LEU   A O    
586  C  CB   . LEU   A 98  ? 0.50243 0.53664 0.68889 -0.00606 -0.02050 -0.26458 250 LEU   A CB   
587  C  CG   . LEU   A 98  ? 0.47979 0.52246 0.67101 0.00457  -0.01300 -0.25569 250 LEU   A CG   
588  C  CD1  . LEU   A 98  ? 0.50018 0.54188 0.66960 0.00279  -0.01611 -0.21768 250 LEU   A CD1  
589  C  CD2  . LEU   A 98  ? 0.49633 0.51671 0.73882 0.01647  -0.01348 -0.26298 250 LEU   A CD2  
590  N  N    . THR   A 99  ? 0.58193 0.58569 0.81100 -0.02064 -0.03391 -0.30956 251 THR   A N    
591  C  CA   . THR   A 99  ? 0.57805 0.57026 0.81212 -0.03301 -0.04411 -0.30879 251 THR   A CA   
592  C  C    . THR   A 99  ? 0.53462 0.53033 0.74258 -0.03883 -0.04957 -0.26952 251 THR   A C    
593  O  O    . THR   A 99  ? 0.47304 0.46944 0.66900 -0.03255 -0.04674 -0.24166 251 THR   A O    
594  C  CB   . THR   A 99  ? 0.67247 0.62596 0.96104 -0.03155 -0.05008 -0.31328 251 THR   A CB   
595  O  OG1  . THR   A 99  ? 0.83522 0.77912 1.12929 -0.04559 -0.06017 -0.30825 251 THR   A OG1  
596  C  CG2  . THR   A 99  ? 0.62023 0.55164 0.93142 -0.02164 -0.05103 -0.27855 251 THR   A CG2  
597  N  N    A SER   A 100 ? 0.50328 0.50304 0.70428 -0.05117 -0.05745 -0.26960 252 SER   A N    
598  N  N    B SER   A 100 ? 0.50523 0.50489 0.70629 -0.05116 -0.05747 -0.26941 252 SER   A N    
599  C  CA   A SER   A 100 ? 0.49850 0.50347 0.67976 -0.05617 -0.06218 -0.23579 252 SER   A CA   
600  C  CA   B SER   A 100 ? 0.49939 0.50444 0.68037 -0.05605 -0.06210 -0.23546 252 SER   A CA   
601  C  C    A SER   A 100 ? 0.50089 0.47986 0.70610 -0.05235 -0.06407 -0.20506 252 SER   A C    
602  C  C    B SER   A 100 ? 0.50094 0.47989 0.70614 -0.05241 -0.06412 -0.20486 252 SER   A C    
603  O  O    A SER   A 100 ? 0.48319 0.46775 0.66952 -0.05016 -0.06284 -0.17646 252 SER   A O    
604  O  O    B SER   A 100 ? 0.48576 0.47019 0.67232 -0.05040 -0.06302 -0.17614 252 SER   A O    
605  C  CB   A SER   A 100 ? 0.55475 0.56997 0.73300 -0.06995 -0.07093 -0.24341 252 SER   A CB   
606  C  CB   B SER   A 100 ? 0.55327 0.56942 0.72995 -0.06978 -0.07077 -0.24269 252 SER   A CB   
607  O  OG   A SER   A 100 ? 0.57095 0.61995 0.71441 -0.07435 -0.07057 -0.25903 252 SER   A OG   
608  O  OG   B SER   A 100 ? 0.57858 0.57276 0.78497 -0.07574 -0.07751 -0.22628 252 SER   A OG   
609  N  N    . ASP   A 101 ? 0.52408 0.47543 0.77180 -0.05193 -0.06726 -0.21058 253 ASP   A N    
610  C  CA   . ASP   A 101 ? 0.54969 0.47933 0.82111 -0.04941 -0.06993 -0.17878 253 ASP   A CA   
611  C  C    . ASP   A 101 ? 0.46586 0.39898 0.72609 -0.03712 -0.06389 -0.16210 253 ASP   A C    
612  O  O    . ASP   A 101 ? 0.46703 0.40148 0.71756 -0.03683 -0.06450 -0.13104 253 ASP   A O    
613  C  CB   . ASP   A 101 ? 0.51846 0.41671 0.84190 -0.05069 -0.07516 -0.18764 253 ASP   A CB   
614  C  CG   . ASP   A 101 ? 0.65680 0.54832 0.99679 -0.06590 -0.08293 -0.19600 253 ASP   A CG   
615  O  OD1  . ASP   A 101 ? 0.70524 0.56993 1.08948 -0.06889 -0.08766 -0.20873 253 ASP   A OD1  
616  O  OD2  . ASP   A 101 ? 0.63998 0.55290 0.95209 -0.07492 -0.08479 -0.18969 253 ASP   A OD2  
617  N  N    . ASP   A 102 ? 0.48368 0.42162 0.74519 -0.02763 -0.05772 -0.18380 254 ASP   A N    
618  C  CA   . ASP   A 102 ? 0.48463 0.42822 0.73914 -0.01681 -0.05254 -0.16930 254 ASP   A CA   
619  C  C    . ASP   A 102 ? 0.47560 0.44324 0.68380 -0.01856 -0.04854 -0.15521 254 ASP   A C    
620  O  O    . ASP   A 102 ? 0.44134 0.41089 0.64108 -0.01475 -0.04759 -0.13145 254 ASP   A O    
621  C  CB   . ASP   A 102 ? 0.51186 0.45830 0.78322 -0.00639 -0.04602 -0.19760 254 ASP   A CB   
622  C  CG   . ASP   A 102 ? 0.52816 0.44643 0.85389 0.00089  -0.04983 -0.20115 254 ASP   A CG   
623  O  OD1  . ASP   A 102 ? 0.55853 0.47620 0.90726 0.00944  -0.04473 -0.23079 254 ASP   A OD1  
624  O  OD2  . ASP   A 102 ? 0.54664 0.44460 0.89383 -0.00188 -0.05775 -0.17376 254 ASP   A OD2  
625  N  N    . GLN   A 103 ? 0.43482 0.42144 0.61420 -0.02469 -0.04693 -0.16934 255 GLN   A N    
626  C  CA   . GLN   A 103 ? 0.46557 0.47144 0.60615 -0.02654 -0.04446 -0.15359 255 GLN   A CA   
627  C  C    . GLN   A 103 ? 0.46406 0.46300 0.60118 -0.03010 -0.04878 -0.12455 255 GLN   A C    
628  O  O    . GLN   A 103 ? 0.37646 0.38186 0.49421 -0.02774 -0.04615 -0.10647 255 GLN   A O    
629  C  CB   . GLN   A 103 ? 0.47495 0.50280 0.58964 -0.03328 -0.04441 -0.17006 255 GLN   A CB   
630  C  CG   . GLN   A 103 ? 0.54718 0.59089 0.65740 -0.03097 -0.03817 -0.19914 255 GLN   A CG   
631  C  CD   . GLN   A 103 ? 0.63210 0.70244 0.71469 -0.03951 -0.03944 -0.21371 255 GLN   A CD   
632  O  OE1  . GLN   A 103 ? 0.64195 0.72234 0.70295 -0.04487 -0.04399 -0.19653 255 GLN   A OE1  
633  N  NE2  . GLN   A 103 ? 0.64736 0.73166 0.73165 -0.04063 -0.03561 -0.24594 255 GLN   A NE2  
634  N  N    . ILE   A 104 ? 0.42970 0.41687 0.58686 -0.03654 -0.05491 -0.12103 256 ILE   A N    
635  C  CA   . ILE   A 104 ? 0.39569 0.38171 0.55037 -0.04091 -0.05764 -0.09491 256 ILE   A CA   
636  C  C    . ILE   A 104 ? 0.40272 0.37839 0.56893 -0.03629 -0.05699 -0.07314 256 ILE   A C    
637  O  O    . ILE   A 104 ? 0.40917 0.39297 0.55801 -0.03607 -0.05502 -0.05384 256 ILE   A O    
638  C  CB   . ILE   A 104 ? 0.43040 0.41063 0.60534 -0.05094 -0.06411 -0.09670 256 ILE   A CB   
639  C  CG1  . ILE   A 104 ? 0.45997 0.45863 0.61687 -0.05675 -0.06618 -0.11254 256 ILE   A CG1  
640  C  CG2  . ILE   A 104 ? 0.37504 0.35470 0.55509 -0.05546 -0.06557 -0.06854 256 ILE   A CG2  
641  C  CD1  . ILE   A 104 ? 0.47096 0.46595 0.65069 -0.06791 -0.07345 -0.12099 256 ILE   A CD1  
642  N  N    A VAL   A 105 ? 0.43714 0.39630 0.63388 -0.03237 -0.05901 -0.07628 257 VAL   A N    
643  N  N    B VAL   A 105 ? 0.42276 0.38165 0.62003 -0.03263 -0.05916 -0.07632 257 VAL   A N    
644  C  CA   A VAL   A 105 ? 0.45410 0.40692 0.66303 -0.02852 -0.06042 -0.05235 257 VAL   A CA   
645  C  CA   B VAL   A 105 ? 0.46504 0.41722 0.67526 -0.02818 -0.06042 -0.05369 257 VAL   A CA   
646  C  C    A VAL   A 105 ? 0.42331 0.38962 0.60846 -0.02132 -0.05531 -0.04895 257 VAL   A C    
647  C  C    B VAL   A 105 ? 0.40746 0.37442 0.59088 -0.02174 -0.05518 -0.04920 257 VAL   A C    
648  O  O    A VAL   A 105 ? 0.43307 0.40480 0.61038 -0.02124 -0.05587 -0.02717 257 VAL   A O    
649  O  O    B VAL   A 105 ? 0.40318 0.37685 0.57505 -0.02253 -0.05532 -0.02769 257 VAL   A O    
650  C  CB   A VAL   A 105 ? 0.50546 0.43658 0.75866 -0.02488 -0.06525 -0.05409 257 VAL   A CB   
651  C  CB   B VAL   A 105 ? 0.50355 0.43536 0.75612 -0.02297 -0.06421 -0.05994 257 VAL   A CB   
652  C  CG1  A VAL   A 105 ? 0.53563 0.45108 0.81518 -0.03416 -0.07087 -0.05761 257 VAL   A CG1  
653  C  CG1  B VAL   A 105 ? 0.52759 0.45874 0.79094 -0.01576 -0.06581 -0.03837 257 VAL   A CG1  
654  C  CG2  A VAL   A 105 ? 0.51198 0.44170 0.77509 -0.01485 -0.06133 -0.08076 257 VAL   A CG2  
655  C  CG2  B VAL   A 105 ? 0.56711 0.48054 0.85125 -0.03157 -0.07095 -0.05547 257 VAL   A CG2  
656  N  N    . LEU   A 106 ? 0.43625 0.41086 0.60896 -0.01670 -0.05027 -0.07029 258 LEU   A N    
657  C  CA   . LEU   A 106 ? 0.40559 0.39370 0.55763 -0.01183 -0.04541 -0.06680 258 LEU   A CA   
658  C  C    . LEU   A 106 ? 0.36040 0.35977 0.47926 -0.01651 -0.04343 -0.05486 258 LEU   A C    
659  O  O    . LEU   A 106 ? 0.34316 0.34853 0.45053 -0.01533 -0.04223 -0.04175 258 LEU   A O    
660  C  CB   . LEU   A 106 ? 0.38579 0.38344 0.53378 -0.00741 -0.03961 -0.09147 258 LEU   A CB   
661  C  CG   . LEU   A 106 ? 0.41122 0.40090 0.59436 0.00025  -0.03922 -0.10753 258 LEU   A CG   
662  C  CD1  . LEU   A 106 ? 0.41030 0.41717 0.58438 0.00360  -0.03111 -0.13354 258 LEU   A CD1  
663  C  CD2  . LEU   A 106 ? 0.40995 0.39462 0.61531 0.00698  -0.04230 -0.08900 258 LEU   A CD2  
664  N  N    . LEU   A 107 ? 0.41187 0.41487 0.51748 -0.02172 -0.04356 -0.06005 259 LEU   A N    
665  C  CA   . LEU   A 107 ? 0.39507 0.40766 0.47466 -0.02419 -0.04155 -0.04998 259 LEU   A CA   
666  C  C    . LEU   A 107 ? 0.35132 0.36239 0.43385 -0.02732 -0.04332 -0.03088 259 LEU   A C    
667  O  O    . LEU   A 107 ? 0.34950 0.36735 0.41528 -0.02704 -0.04054 -0.02158 259 LEU   A O    
668  C  CB   . LEU   A 107 ? 0.51326 0.53394 0.58018 -0.02761 -0.04199 -0.06017 259 LEU   A CB   
669  C  CG   . LEU   A 107 ? 0.60061 0.63201 0.65014 -0.02569 -0.03823 -0.07171 259 LEU   A CG   
670  C  CD1  . LEU   A 107 ? 0.67293 0.71389 0.71845 -0.02961 -0.04043 -0.08734 259 LEU   A CD1  
671  C  CD2  . LEU   A 107 ? 0.55669 0.59412 0.58453 -0.02507 -0.03543 -0.05991 259 LEU   A CD2  
672  N  N    . LYS   A 108 ? 0.33682 0.34030 0.44137 -0.03116 -0.04751 -0.02546 260 LYS   A N    
673  C  CA   . LYS   A 108 ? 0.35514 0.36208 0.46270 -0.03562 -0.04838 -0.00527 260 LYS   A CA   
674  C  C    . LYS   A 108 ? 0.37998 0.39015 0.48409 -0.03316 -0.04802 0.00859  260 LYS   A C    
675  O  O    . LYS   A 108 ? 0.39270 0.41465 0.48206 -0.03562 -0.04559 0.02034  260 LYS   A O    
676  C  CB   . LYS   A 108 ? 0.40366 0.40130 0.53959 -0.04177 -0.05353 0.00048  260 LYS   A CB   
677  C  CG   . LYS   A 108 ? 0.49288 0.49533 0.63026 -0.04805 -0.05443 -0.00576 260 LYS   A CG   
678  C  CD   . LYS   A 108 ? 0.54997 0.54286 0.71836 -0.05636 -0.05979 0.00221  260 LYS   A CD   
679  C  CE   . LYS   A 108 ? 0.63892 0.64074 0.81048 -0.06193 -0.05891 0.02911  260 LYS   A CE   
680  N  NZ   . LYS   A 108 ? 0.67684 0.66693 0.88262 -0.07085 -0.06483 0.04194  260 LYS   A NZ   
681  N  N    . SER   A 109 ? 0.38332 0.38593 0.50180 -0.02824 -0.05044 0.00599  261 SER   A N    
682  C  CA   . SER   A 109 ? 0.41787 0.42622 0.53717 -0.02620 -0.05233 0.02048  261 SER   A CA   
683  C  C    . SER   A 109 ? 0.37758 0.39651 0.47253 -0.02326 -0.04805 0.01396  261 SER   A C    
684  O  O    . SER   A 109 ? 0.41341 0.44300 0.49983 -0.02453 -0.04912 0.02567  261 SER   A O    
685  C  CB   . SER   A 109 ? 0.53788 0.53453 0.69009 -0.02111 -0.05773 0.02204  261 SER   A CB   
686  O  OG   . SER   A 109 ? 0.62274 0.61562 0.77796 -0.01447 -0.05448 -0.00061 261 SER   A OG   
687  N  N    . SER   A 110 ? 0.33666 0.35462 0.42032 -0.02077 -0.04375 -0.00356 262 SER   A N    
688  C  CA   . SER   A 110 ? 0.35533 0.38151 0.42023 -0.01931 -0.04003 -0.00840 262 SER   A CA   
689  C  C    . SER   A 110 ? 0.36246 0.39298 0.40282 -0.02249 -0.03600 -0.00927 262 SER   A C    
690  O  O    . SER   A 110 ? 0.34347 0.37901 0.37002 -0.02302 -0.03365 -0.01040 262 SER   A O    
691  C  CB   . SER   A 110 ? 0.37999 0.40586 0.44877 -0.01517 -0.03723 -0.02476 262 SER   A CB   
692  O  OG   . SER   A 110 ? 0.37887 0.40320 0.43922 -0.01650 -0.03488 -0.03646 262 SER   A OG   
693  N  N    . ALA   A 111 ? 0.34274 0.37154 0.38091 -0.02456 -0.03546 -0.00905 263 ALA   A N    
694  C  CA   . ALA   A 111 ? 0.35327 0.38520 0.37428 -0.02510 -0.03176 -0.01182 263 ALA   A CA   
695  C  C    . ALA   A 111 ? 0.32931 0.36698 0.33745 -0.02634 -0.02906 -0.00738 263 ALA   A C    
696  O  O    . ALA   A 111 ? 0.35114 0.38746 0.34769 -0.02563 -0.02627 -0.01267 263 ALA   A O    
697  C  CB   . ALA   A 111 ? 0.33718 0.37074 0.36315 -0.02685 -0.03227 -0.00991 263 ALA   A CB   
698  N  N    . ILE   A 112 ? 0.29724 0.34239 0.30764 -0.02921 -0.03012 0.00237  264 ILE   A N    
699  C  CA   . ILE   A 112 ? 0.34224 0.39711 0.33834 -0.03169 -0.02742 0.00333  264 ILE   A CA   
700  C  C    . ILE   A 112 ? 0.37140 0.42618 0.36226 -0.03201 -0.02883 -0.00047 264 ILE   A C    
701  O  O    . ILE   A 112 ? 0.33949 0.39649 0.31791 -0.03387 -0.02607 -0.00696 264 ILE   A O    
702  C  CB   . ILE   A 112 ? 0.42874 0.49807 0.42613 -0.03642 -0.02853 0.01629  264 ILE   A CB   
703  C  CG1  . ILE   A 112 ? 0.46443 0.54870 0.44383 -0.03990 -0.02446 0.01294  264 ILE   A CG1  
704  C  CG2  . ILE   A 112 ? 0.45645 0.52668 0.46752 -0.03748 -0.03561 0.02876  264 ILE   A CG2  
705  C  CD1  . ILE   A 112 ? 0.41816 0.49957 0.38987 -0.03702 -0.01730 -0.00056 264 ILE   A CD1  
706  N  N    . GLU   A 113 ? 0.33884 0.39139 0.34201 -0.03026 -0.03295 0.00211  265 GLU   A N    
707  C  CA   . GLU   A 113 ? 0.34429 0.40078 0.34610 -0.03081 -0.03423 -0.00089 265 GLU   A CA   
708  C  C    . GLU   A 113 ? 0.32816 0.37731 0.32276 -0.03024 -0.03002 -0.01180 265 GLU   A C    
709  O  O    . GLU   A 113 ? 0.35113 0.40285 0.33779 -0.03377 -0.02900 -0.01543 265 GLU   A O    
710  C  CB   . GLU   A 113 ? 0.35475 0.41315 0.37688 -0.02739 -0.03909 0.00444  265 GLU   A CB   
711  C  CG   . GLU   A 113 ? 0.29901 0.36487 0.33199 -0.02852 -0.04520 0.02048  265 GLU   A CG   
712  C  CD   . GLU   A 113 ? 0.40764 0.47132 0.46814 -0.02295 -0.05049 0.02579  265 GLU   A CD   
713  O  OE1  . GLU   A 113 ? 0.39612 0.45977 0.46435 -0.01880 -0.04897 0.01593  265 GLU   A OE1  
714  O  OE2  . GLU   A 113 ? 0.40599 0.46869 0.48277 -0.02270 -0.05585 0.04018  265 GLU   A OE2  
715  N  N    . VAL   A 114 ? 0.33785 0.37934 0.33549 -0.02715 -0.02819 -0.01620 266 VAL   A N    
716  C  CA   . VAL   A 114 ? 0.33429 0.37207 0.32427 -0.02770 -0.02491 -0.02233 266 VAL   A CA   
717  C  C    . VAL   A 114 ? 0.35544 0.38746 0.33424 -0.02951 -0.02261 -0.02283 266 VAL   A C    
718  O  O    . VAL   A 114 ? 0.35376 0.38207 0.32756 -0.03211 -0.02089 -0.02471 266 VAL   A O    
719  C  CB   . VAL   A 114 ? 0.39673 0.43285 0.39046 -0.02502 -0.02450 -0.02658 266 VAL   A CB   
720  C  CG1  . VAL   A 114 ? 0.37293 0.41042 0.35734 -0.02693 -0.02174 -0.02913 266 VAL   A CG1  
721  C  CG2  . VAL   A 114 ? 0.37127 0.41097 0.38062 -0.02221 -0.02611 -0.03007 266 VAL   A CG2  
722  N  N    . ILE   A 115 ? 0.35610 0.38766 0.33372 -0.02824 -0.02216 -0.02126 267 ILE   A N    
723  C  CA   . ILE   A 115 ? 0.31947 0.34647 0.29091 -0.02823 -0.01903 -0.02468 267 ILE   A CA   
724  C  C    . ILE   A 115 ? 0.35808 0.38698 0.32355 -0.03298 -0.01835 -0.02924 267 ILE   A C    
725  O  O    . ILE   A 115 ? 0.39205 0.41200 0.35551 -0.03446 -0.01640 -0.03467 267 ILE   A O    
726  C  CB   . ILE   A 115 ? 0.36891 0.40092 0.34249 -0.02576 -0.01732 -0.02339 267 ILE   A CB   
727  C  CG1  . ILE   A 115 ? 0.36257 0.39250 0.34314 -0.02219 -0.01870 -0.02061 267 ILE   A CG1  
728  C  CG2  . ILE   A 115 ? 0.39323 0.42407 0.36312 -0.02482 -0.01272 -0.03046 267 ILE   A CG2  
729  C  CD1  . ILE   A 115 ? 0.37735 0.41611 0.36441 -0.02159 -0.01803 -0.01710 267 ILE   A CD1  
730  N  N    . MET   A 116 ? 0.32833 0.36925 0.29272 -0.03613 -0.02093 -0.02651 268 MET   A N    
731  C  CA   . MET   A 116 ? 0.37403 0.42143 0.33215 -0.04225 -0.02192 -0.03138 268 MET   A CA   
732  C  C    . MET   A 116 ? 0.35294 0.39430 0.31415 -0.04544 -0.02276 -0.03376 268 MET   A C    
733  O  O    . MET   A 116 ? 0.38044 0.41754 0.33834 -0.05074 -0.02188 -0.04131 268 MET   A O    
734  C  CB   . MET   A 116 ? 0.37471 0.44033 0.33252 -0.04513 -0.02665 -0.02372 268 MET   A CB   
735  C  CG   . MET   A 116 ? 0.41099 0.48841 0.36196 -0.04595 -0.02507 -0.02087 268 MET   A CG   
736  S  SD   . MET   A 116 ? 0.44844 0.54674 0.40326 -0.04887 -0.03219 -0.00292 268 MET   A SD   
737  C  CE   . MET   A 116 ? 0.45595 0.56890 0.40069 -0.05132 -0.02714 -0.00011 268 MET   A CE   
738  N  N    . LEU   A 117 ? 0.34927 0.39120 0.31818 -0.04300 -0.02386 -0.02853 269 LEU   A N    
739  C  CA   . LEU   A 117 ? 0.33939 0.38110 0.31168 -0.04692 -0.02332 -0.02950 269 LEU   A CA   
740  C  C    . LEU   A 117 ? 0.38956 0.41639 0.35883 -0.04833 -0.02005 -0.03090 269 LEU   A C    
741  O  O    . LEU   A 117 ? 0.36277 0.38500 0.33269 -0.05504 -0.01964 -0.03313 269 LEU   A O    
742  C  CB   . LEU   A 117 ? 0.32283 0.37267 0.30458 -0.04318 -0.02353 -0.02619 269 LEU   A CB   
743  C  CG   . LEU   A 117 ? 0.34045 0.40431 0.33344 -0.04115 -0.02764 -0.02295 269 LEU   A CG   
744  C  CD1  . LEU   A 117 ? 0.35632 0.42284 0.36188 -0.03458 -0.02646 -0.02370 269 LEU   A CD1  
745  C  CD2  . LEU   A 117 ? 0.30943 0.38617 0.30645 -0.04745 -0.02983 -0.02329 269 LEU   A CD2  
746  N  N    . ARG   A 118 ? 0.37677 0.39637 0.34508 -0.04269 -0.01866 -0.02821 270 ARG   A N    
747  C  CA   . ARG   A 118 ? 0.35354 0.36110 0.32172 -0.04336 -0.01722 -0.02501 270 ARG   A CA   
748  C  C    . ARG   A 118 ? 0.37707 0.37035 0.34695 -0.04420 -0.01629 -0.03017 270 ARG   A C    
749  O  O    . ARG   A 118 ? 0.42546 0.40598 0.40007 -0.04721 -0.01600 -0.02724 270 ARG   A O    
750  C  CB   . ARG   A 118 ? 0.35893 0.36685 0.32645 -0.03734 -0.01763 -0.02015 270 ARG   A CB   
751  C  CG   . ARG   A 118 ? 0.36028 0.36479 0.32939 -0.03118 -0.01778 -0.02222 270 ARG   A CG   
752  C  CD   . ARG   A 118 ? 0.41375 0.42545 0.38373 -0.02709 -0.01960 -0.01929 270 ARG   A CD   
753  N  NE   . ARG   A 118 ? 0.49431 0.50828 0.46164 -0.02812 -0.02096 -0.01351 270 ARG   A NE   
754  C  CZ   . ARG   A 118 ? 0.54598 0.55451 0.51492 -0.02633 -0.02257 -0.00633 270 ARG   A CZ   
755  N  NH1  . ARG   A 118 ? 0.60704 0.60553 0.58336 -0.02186 -0.02205 -0.00689 270 ARG   A NH1  
756  N  NH2  . ARG   A 118 ? 0.45871 0.47424 0.42302 -0.02880 -0.02470 0.00168  270 ARG   A NH2  
757  N  N    . SER   A 119 ? 0.36695 0.36301 0.33452 -0.04201 -0.01553 -0.03801 271 SER   A N    
758  C  CA   . SER   A 119 ? 0.42531 0.41048 0.39535 -0.04246 -0.01323 -0.04823 271 SER   A CA   
759  C  C    . SER   A 119 ? 0.40727 0.38852 0.37812 -0.05212 -0.01418 -0.05563 271 SER   A C    
760  O  O    . SER   A 119 ? 0.43278 0.40051 0.40912 -0.05366 -0.01240 -0.06638 271 SER   A O    
761  C  CB   . SER   A 119 ? 0.43775 0.43409 0.40274 -0.03900 -0.01086 -0.05591 271 SER   A CB   
762  O  OG   . SER   A 119 ? 0.47881 0.49115 0.43523 -0.04540 -0.01274 -0.05944 271 SER   A OG   
763  N  N    . ASN   A 120 ? 0.37767 0.37093 0.34614 -0.05859 -0.01698 -0.05143 272 ASN   A N    
764  C  CA   . ASN   A 120 ? 0.38469 0.37727 0.35617 -0.06944 -0.01877 -0.05741 272 ASN   A CA   
765  C  C    . ASN   A 120 ? 0.42645 0.39827 0.40870 -0.07383 -0.01790 -0.05388 272 ASN   A C    
766  O  O    . ASN   A 120 ? 0.44548 0.40879 0.43405 -0.08310 -0.01892 -0.06218 272 ASN   A O    
767  C  CB   . ASN   A 120 ? 0.39415 0.40746 0.36533 -0.07404 -0.02193 -0.05126 272 ASN   A CB   
768  C  CG   . ASN   A 120 ? 0.43595 0.45642 0.41010 -0.08611 -0.02517 -0.05863 272 ASN   A CG   
769  O  OD1  . ASN   A 120 ? 0.47613 0.49901 0.45855 -0.09342 -0.02574 -0.05369 272 ASN   A OD1  
770  N  ND2  . ASN   A 120 ? 0.40228 0.42973 0.36941 -0.08944 -0.02729 -0.07080 272 ASN   A ND2  
771  N  N    . GLN   A 121 ? 0.42644 0.39091 0.41172 -0.06845 -0.01683 -0.04089 273 GLN   A N    
772  C  CA   . GLN   A 121 ? 0.47546 0.42200 0.47185 -0.07318 -0.01703 -0.03183 273 GLN   A CA   
773  C  C    . GLN   A 121 ? 0.52636 0.44762 0.53503 -0.07188 -0.01661 -0.04173 273 GLN   A C    
774  O  O    . GLN   A 121 ? 0.54490 0.44823 0.56727 -0.07982 -0.01776 -0.03941 273 GLN   A O    
775  C  CB   . GLN   A 121 ? 0.51930 0.46842 0.51382 -0.06739 -0.01702 -0.01490 273 GLN   A CB   
776  C  CG   . GLN   A 121 ? 0.51437 0.44989 0.51924 -0.07314 -0.01825 0.00094  273 GLN   A CG   
777  C  CD   . GLN   A 121 ? 0.49425 0.44488 0.49139 -0.07163 -0.01862 0.01840  273 GLN   A CD   
778  O  OE1  . GLN   A 121 ? 0.44019 0.41230 0.42537 -0.06875 -0.01718 0.01574  273 GLN   A OE1  
779  N  NE2  . GLN   A 121 ? 0.48151 0.42177 0.48650 -0.07396 -0.02098 0.03627  273 GLN   A NE2  
780  N  N    . SER   A 122 ? 0.51040 0.43029 0.51711 -0.06218 -0.01450 -0.05328 274 SER   A N    
781  C  CA   . SER   A 122 ? 0.53137 0.42984 0.55224 -0.05861 -0.01248 -0.06721 274 SER   A CA   
782  C  C    . SER   A 122 ? 0.53609 0.43944 0.55227 -0.06462 -0.01077 -0.09174 274 SER   A C    
783  O  O    . SER   A 122 ? 0.57756 0.46347 0.60666 -0.06326 -0.00829 -0.10889 274 SER   A O    
784  C  CB   . SER   A 122 ? 0.53841 0.43631 0.56301 -0.04389 -0.00994 -0.06645 274 SER   A CB   
785  O  OG   . SER   A 122 ? 0.53687 0.45752 0.54605 -0.04017 -0.00723 -0.07528 274 SER   A OG   
786  N  N    . PHE   A 123 ? 0.49066 0.41868 0.49008 -0.07100 -0.01238 -0.09429 275 PHE   A N    
787  C  CA   . PHE   A 123 ? 0.50863 0.44804 0.50025 -0.07834 -0.01227 -0.11576 275 PHE   A CA   
788  C  C    . PHE   A 123 ? 0.54345 0.46704 0.54741 -0.09151 -0.01489 -0.12610 275 PHE   A C    
789  O  O    . PHE   A 123 ? 0.60037 0.51860 0.61199 -0.09921 -0.01823 -0.11195 275 PHE   A O    
790  C  CB   . PHE   A 123 ? 0.50134 0.47268 0.47509 -0.08192 -0.01552 -0.11018 275 PHE   A CB   
791  C  CG   . PHE   A 123 ? 0.50081 0.49191 0.46244 -0.08941 -0.01662 -0.12890 275 PHE   A CG   
792  C  CD1  . PHE   A 123 ? 0.51231 0.51458 0.46395 -0.08385 -0.01191 -0.14137 275 PHE   A CD1  
793  C  CD2  . PHE   A 123 ? 0.44294 0.44609 0.40282 -0.10300 -0.02248 -0.13361 275 PHE   A CD2  
794  C  CE1  . PHE   A 123 ? 0.53064 0.55683 0.46763 -0.09215 -0.01287 -0.15823 275 PHE   A CE1  
795  C  CE2  . PHE   A 123 ? 0.48703 0.51310 0.43364 -0.11118 -0.02488 -0.15042 275 PHE   A CE2  
796  C  CZ   . PHE   A 123 ? 0.55565 0.59383 0.48921 -0.10599 -0.02001 -0.16277 275 PHE   A CZ   
797  N  N    . THR   A 124 ? 0.57967 0.49727 0.58658 -0.09497 -0.01289 -0.15213 276 THR   A N    
798  C  CA   . THR   A 124 ? 0.65473 0.55693 0.67489 -0.10914 -0.01582 -0.16701 276 THR   A CA   
799  C  C    . THR   A 124 ? 0.65128 0.58079 0.65470 -0.12026 -0.01829 -0.18894 276 THR   A C    
800  O  O    . THR   A 124 ? 0.62198 0.57092 0.60942 -0.11522 -0.01473 -0.20337 276 THR   A O    
801  C  CB   . THR   A 124 ? 0.78027 0.64569 0.82550 -0.10465 -0.01202 -0.18239 276 THR   A CB   
802  O  OG1  . THR   A 124 ? 0.86145 0.71151 0.92087 -0.12029 -0.01529 -0.20053 276 THR   A OG1  
803  C  CG2  . THR   A 124 ? 0.76592 0.63750 0.80612 -0.09255 -0.00472 -0.20478 276 THR   A CG2  
804  N  N    . MET   A 125 ? 0.65554 0.59066 0.66242 -0.13639 -0.02475 -0.18980 277 MET   A N    
805  C  CA   . MET   A 125 ? 0.69898 0.66112 0.69220 -0.14949 -0.02922 -0.21102 277 MET   A CA   
806  C  C    . MET   A 125 ? 0.75757 0.70015 0.76256 -0.15825 -0.02780 -0.24538 277 MET   A C    
807  O  O    . MET   A 125 ? 0.84199 0.80851 0.83390 -0.16995 -0.03122 -0.26849 277 MET   A O    
808  C  CB   . MET   A 125 ? 0.73074 0.71371 0.72431 -0.16301 -0.03773 -0.19652 277 MET   A CB   
809  C  CG   . MET   A 125 ? 0.69528 0.70368 0.67726 -0.15420 -0.03921 -0.16884 277 MET   A CG   
810  S  SD   . MET   A 125 ? 0.85189 0.89897 0.83256 -0.16755 -0.04940 -0.15824 277 MET   A SD   
811  C  CE   . MET   A 125 ? 0.85448 0.87924 0.86216 -0.17807 -0.04949 -0.14703 277 MET   A CE   
812  N  N    . ASP   A 126 ? 0.79550 0.69608 0.82626 -0.15289 -0.02341 -0.24936 278 ASP   A N    
813  C  CA   . ASP   A 126 ? 0.90332 0.78077 0.95025 -0.15780 -0.02066 -0.28537 278 ASP   A CA   
814  C  C    . ASP   A 126 ? 0.87051 0.77179 0.89681 -0.14986 -0.01399 -0.31238 278 ASP   A C    
815  O  O    . ASP   A 126 ? 0.88086 0.79274 0.90081 -0.15485 -0.01430 -0.33435 278 ASP   A O    
816  C  CB   . ASP   A 126 ? 1.04304 0.87099 1.12479 -0.14858 -0.01699 -0.27934 278 ASP   A CB   
817  C  CG   . ASP   A 126 ? 1.15397 0.95648 1.26003 -0.16188 -0.02360 -0.25936 278 ASP   A CG   
818  O  OD1  . ASP   A 126 ? 1.19599 1.01382 1.29812 -0.18082 -0.03017 -0.26316 278 ASP   A OD1  
819  O  OD2  . ASP   A 126 ? 1.19058 0.96079 1.32028 -0.15408 -0.02257 -0.23816 278 ASP   A OD2  
820  N  N    . ASP   A 127 ? 0.79942 0.71379 0.81292 -0.13353 -0.00785 -0.30022 279 ASP   A N    
821  C  CA   . ASP   A 127 ? 0.81230 0.75386 0.80647 -0.12711 -0.00015 -0.32391 279 ASP   A CA   
822  C  C    . ASP   A 127 ? 0.80079 0.77679 0.76936 -0.11796 0.00135  -0.29969 279 ASP   A C    
823  O  O    . ASP   A 127 ? 0.81171 0.80521 0.77005 -0.10868 0.00992  -0.31144 279 ASP   A O    
824  C  CB   . ASP   A 127 ? 0.91230 0.82455 0.93104 -0.11167 0.00992  -0.34189 279 ASP   A CB   
825  C  CG   . ASP   A 127 ? 0.91726 0.79656 0.96075 -0.09708 0.01181  -0.31844 279 ASP   A CG   
826  O  OD1  . ASP   A 127 ? 0.95701 0.79850 1.03378 -0.08943 0.01531  -0.32962 279 ASP   A OD1  
827  O  OD2  . ASP   A 127 ? 0.86317 0.75574 0.89392 -0.09182 0.00906  -0.28488 279 ASP   A OD2  
828  N  N    . MET   A 128 ? 0.74250 0.72901 0.70314 -0.12033 -0.00621 -0.26682 280 MET   A N    
829  C  CA   . MET   A 128 ? 0.67995 0.69718 0.61976 -0.11334 -0.00645 -0.24322 280 MET   A CA   
830  C  C    . MET   A 128 ? 0.64631 0.65380 0.59240 -0.09540 0.00240  -0.23578 280 MET   A C    
831  O  O    . MET   A 128 ? 0.65222 0.68684 0.58228 -0.09028 0.00730  -0.23641 280 MET   A O    
832  C  CB   . MET   A 128 ? 0.70475 0.76760 0.61608 -0.12268 -0.00842 -0.25481 280 MET   A CB   
833  C  CG   . MET   A 128 ? 0.73949 0.81777 0.64475 -0.14127 -0.01846 -0.26401 280 MET   A CG   
834  S  SD   . MET   A 128 ? 0.73658 0.81758 0.64852 -0.14506 -0.02985 -0.22725 280 MET   A SD   
835  C  CE   . MET   A 128 ? 0.74737 0.81189 0.67677 -0.16335 -0.03652 -0.24529 280 MET   A CE   
836  N  N    . SER   A 129 ? 0.64227 0.61329 0.61291 -0.08677 0.00380  -0.22657 281 SER   A N    
837  C  CA   . SER   A 129 ? 0.63705 0.59835 0.61817 -0.06996 0.01057  -0.21868 281 SER   A CA   
838  C  C    . SER   A 129 ? 0.59053 0.53399 0.58233 -0.06428 0.00591  -0.18676 281 SER   A C    
839  O  O    . SER   A 129 ? 0.56338 0.49515 0.56001 -0.07259 -0.00052 -0.17462 281 SER   A O    
840  C  CB   . SER   A 129 ? 0.69911 0.63528 0.70419 -0.06238 0.01804  -0.24460 281 SER   A CB   
841  O  OG   . SER   A 129 ? 0.78064 0.67672 0.81366 -0.06094 0.01423  -0.23523 281 SER   A OG   
842  N  N    . TRP   A 130 ? 0.58113 0.52657 0.57624 -0.05097 0.00948  -0.17390 282 TRP   A N    
843  C  CA   . TRP   A 130 ? 0.55770 0.48819 0.56323 -0.04452 0.00575  -0.14700 282 TRP   A CA   
844  C  C    . TRP   A 130 ? 0.55078 0.45055 0.58465 -0.03522 0.00808  -0.15047 282 TRP   A C    
845  O  O    . TRP   A 130 ? 0.59444 0.49583 0.63839 -0.02296 0.01381  -0.15742 282 TRP   A O    
846  C  CB   . TRP   A 130 ? 0.45916 0.41127 0.45340 -0.03696 0.00656  -0.13095 282 TRP   A CB   
847  C  CG   . TRP   A 130 ? 0.47132 0.44905 0.44422 -0.04460 0.00263  -0.12154 282 TRP   A CG   
848  C  CD1  . TRP   A 130 ? 0.48669 0.46679 0.45582 -0.04740 -0.00317 -0.10182 282 TRP   A CD1  
849  C  CD2  . TRP   A 130 ? 0.47036 0.47655 0.42536 -0.04966 0.00411  -0.13051 282 TRP   A CD2  
850  N  NE1  . TRP   A 130 ? 0.44444 0.44922 0.39856 -0.05255 -0.00585 -0.09806 282 TRP   A NE1  
851  C  CE2  . TRP   A 130 ? 0.45775 0.47935 0.40213 -0.05463 -0.00223 -0.11313 282 TRP   A CE2  
852  C  CE3  . TRP   A 130 ? 0.51132 0.53403 0.45864 -0.05069 0.01035  -0.15145 282 TRP   A CE3  
853  C  CZ2  . TRP   A 130 ? 0.45054 0.50136 0.37870 -0.06047 -0.00415 -0.11207 282 TRP   A CZ2  
854  C  CZ3  . TRP   A 130 ? 0.50578 0.56139 0.43227 -0.05807 0.00913  -0.15093 282 TRP   A CZ3  
855  C  CH2  . TRP   A 130 ? 0.50982 0.57825 0.42772 -0.06287 0.00112  -0.12941 282 TRP   A CH2  
856  N  N    . ASP   A 131 ? 0.57730 0.45030 0.62693 -0.04113 0.00344  -0.14416 283 ASP   A N    
857  C  CA   . ASP   A 131 ? 0.64595 0.48623 0.72730 -0.03329 0.00376  -0.14380 283 ASP   A CA   
858  C  C    . ASP   A 131 ? 0.59775 0.43355 0.68574 -0.02604 -0.00089 -0.11163 283 ASP   A C    
859  O  O    . ASP   A 131 ? 0.67553 0.51026 0.75751 -0.03458 -0.00654 -0.09048 283 ASP   A O    
860  C  CB   . ASP   A 131 ? 0.69781 0.51071 0.79563 -0.04541 0.00053  -0.15229 283 ASP   A CB   
861  C  CG   . ASP   A 131 ? 0.80199 0.57727 0.93842 -0.03706 0.00063  -0.15391 283 ASP   A CG   
862  O  OD1  . ASP   A 131 ? 0.78545 0.55793 0.93605 -0.02097 0.00249  -0.14585 283 ASP   A OD1  
863  O  OD2  . ASP   A 131 ? 0.85400 0.60237 1.00975 -0.04678 -0.00183 -0.16261 283 ASP   A OD2  
864  N  N    . CYS   A 132 ? 0.63414 0.47091 0.73490 -0.01085 0.00158  -0.10863 284 CYS   A N    
865  C  CA   . CYS   A 132 ? 0.59172 0.42978 0.69786 -0.00373 -0.00370 -0.07962 284 CYS   A CA   
866  C  C    . CYS   A 132 ? 0.63033 0.44069 0.77304 0.00666  -0.00626 -0.07152 284 CYS   A C    
867  O  O    . CYS   A 132 ? 0.62346 0.43955 0.77757 0.01855  -0.00858 -0.05669 284 CYS   A O    
868  C  CB   . CYS   A 132 ? 0.58964 0.45719 0.68132 0.00436  -0.00108 -0.07756 284 CYS   A CB   
869  S  SG   . CYS   A 132 ? 0.53234 0.42923 0.58697 -0.00684 -0.00220 -0.07240 284 CYS   A SG   
870  N  N    . GLY   A 133 ? 0.67252 0.45258 0.83706 0.00215  -0.00666 -0.08094 285 GLY   A N    
871  C  CA   . GLY   A 133 ? 0.68916 0.43766 0.89188 0.00915  -0.01161 -0.06637 285 GLY   A CA   
872  C  C    . GLY   A 133 ? 0.76879 0.49683 1.00764 0.02337  -0.00603 -0.09130 285 GLY   A C    
873  O  O    . GLY   A 133 ? 0.80563 0.49889 1.08200 0.02660  -0.01005 -0.08505 285 GLY   A O    
874  N  N    A SER   A 134 ? 0.78759 0.53681 1.01860 0.03185  0.00341  -0.11895 286 SER   A N    
875  N  N    B SER   A 134 ? 0.78864 0.53776 1.01979 0.03189  0.00341  -0.11897 286 SER   A N    
876  C  CA   A SER   A 134 ? 0.81814 0.55427 1.08436 0.04732  0.01080  -0.14558 286 SER   A CA   
877  C  CA   B SER   A 134 ? 0.81842 0.55362 1.08504 0.04704  0.01075  -0.14587 286 SER   A CA   
878  C  C    A SER   A 134 ? 0.81421 0.57326 1.05960 0.04460  0.02271  -0.18561 286 SER   A C    
879  C  C    B SER   A 134 ? 0.81382 0.57334 1.05928 0.04491  0.02274  -0.18533 286 SER   A C    
880  O  O    A SER   A 134 ? 0.78584 0.57228 0.99079 0.03236  0.02378  -0.18736 286 SER   A O    
881  O  O    B SER   A 134 ? 0.78248 0.57064 0.98739 0.03336  0.02394  -0.18641 286 SER   A O    
882  C  CB   A SER   A 134 ? 0.82131 0.56798 1.11026 0.06705  0.00994  -0.12955 286 SER   A CB   
883  C  CB   B SER   A 134 ? 0.82628 0.56900 1.11852 0.06706  0.00947  -0.12927 286 SER   A CB   
884  O  OG   A SER   A 134 ? 0.83342 0.56245 1.14094 0.06886  -0.00232 -0.09099 286 SER   A OG   
885  O  OG   B SER   A 134 ? 0.79593 0.57498 1.07393 0.07510  0.01900  -0.14673 286 SER   A OG   
886  N  N    . GLN   A 135 ? 0.85398 0.60329 1.12910 0.05644  0.03166  -0.21777 287 GLN   A N    
887  C  CA   . GLN   A 135 ? 0.89521 0.67092 1.15099 0.05393  0.04412  -0.25801 287 GLN   A CA   
888  C  C    . GLN   A 135 ? 0.82885 0.65099 1.06033 0.06012  0.05053  -0.25379 287 GLN   A C    
889  O  O    . GLN   A 135 ? 0.77035 0.62487 0.96463 0.04957  0.05566  -0.26672 287 GLN   A O    
890  C  CB   . GLN   A 135 ? 0.96791 0.72239 1.26456 0.06562  0.05328  -0.29670 287 GLN   A CB   
891  C  CG   . GLN   A 135 ? 1.04436 0.77618 1.33937 0.05012  0.05098  -0.31554 287 GLN   A CG   
892  C  CD   . GLN   A 135 ? 1.07795 0.84124 1.32637 0.03185  0.05485  -0.33806 287 GLN   A CD   
893  O  OE1  . GLN   A 135 ? 1.08258 0.88729 1.30380 0.03337  0.06320  -0.34974 287 GLN   A OE1  
894  N  NE2  . GLN   A 135 ? 1.08773 0.83443 1.32724 0.01375  0.04806  -0.34146 287 GLN   A NE2  
895  N  N    . ASP   A 136 ? 0.79848 0.62577 1.05233 0.07634  0.04954  -0.23431 288 ASP   A N    
896  C  CA   . ASP   A 136 ? 0.79465 0.66512 1.02831 0.08029  0.05420  -0.22629 288 ASP   A CA   
897  C  C    . ASP   A 136 ? 0.70946 0.59809 0.89905 0.06425  0.04685  -0.20203 288 ASP   A C    
898  O  O    . ASP   A 136 ? 0.71133 0.63619 0.87461 0.06040  0.05190  -0.20352 288 ASP   A O    
899  C  CB   . ASP   A 136 ? 0.84354 0.71519 1.11133 0.09864  0.05124  -0.20548 288 ASP   A CB   
900  C  CG   . ASP   A 136 ? 0.97191 0.83551 1.28665 0.11796  0.06085  -0.23172 288 ASP   A CG   
901  O  OD1  . ASP   A 136 ? 1.02696 0.89288 1.34212 0.11704  0.07274  -0.27066 288 ASP   A OD1  
902  O  OD2  . ASP   A 136 ? 1.00950 0.86666 1.36186 0.13429  0.05636  -0.21420 288 ASP   A OD2  
903  N  N    . TYR   A 137 ? 0.64937 0.51420 0.83276 0.05469  0.03535  -0.17940 289 TYR   A N    
904  C  CA   . TYR   A 137 ? 0.58853 0.46829 0.73617 0.04140  0.02828  -0.15661 289 TYR   A CA   
905  C  C    . TYR   A 137 ? 0.54430 0.41631 0.66976 0.02415  0.02604  -0.16535 289 TYR   A C    
906  O  O    . TYR   A 137 ? 0.59674 0.46546 0.70648 0.01395  0.01793  -0.14421 289 TYR   A O    
907  C  CB   . TYR   A 137 ? 0.57165 0.44067 0.72779 0.04412  0.01723  -0.12121 289 TYR   A CB   
908  C  CG   . TYR   A 137 ? 0.59548 0.47010 0.78004 0.06129  0.01708  -0.11163 289 TYR   A CG   
909  C  CD1  . TYR   A 137 ? 0.60777 0.46064 0.82041 0.06864  0.00809  -0.08885 289 TYR   A CD1  
910  C  CD2  . TYR   A 137 ? 0.54390 0.44882 0.72846 0.06938  0.02540  -0.12328 289 TYR   A CD2  
911  C  CE1  . TYR   A 137 ? 0.64610 0.50739 0.88709 0.08466  0.00641  -0.07861 289 TYR   A CE1  
912  C  CE2  . TYR   A 137 ? 0.63100 0.54473 0.84445 0.08486  0.02499  -0.11465 289 TYR   A CE2  
913  C  CZ   . TYR   A 137 ? 0.65642 0.54838 0.89852 0.09298  0.01497  -0.09257 289 TYR   A CZ   
914  O  OH   . TYR   A 137 ? 0.66399 0.56793 0.93714 0.10875  0.01304  -0.08237 289 TYR   A OH   
915  N  N    . LYS   A 138 ? 0.60328 0.47525 0.72836 0.02054  0.03330  -0.19785 290 LYS   A N    
916  C  CA   . LYS   A 138 ? 0.61383 0.49029 0.71405 0.00322  0.03163  -0.20996 290 LYS   A CA   
917  C  C    . LYS   A 138 ? 0.62244 0.54026 0.69337 -0.00046 0.03880  -0.22488 290 LYS   A C    
918  O  O    . LYS   A 138 ? 0.60931 0.54033 0.68556 0.00533  0.04907  -0.25232 290 LYS   A O    
919  C  CB   . LYS   A 138 ? 0.72120 0.56813 0.84242 -0.00112 0.03283  -0.23632 290 LYS   A CB   
920  C  CG   . LYS   A 138 ? 0.70840 0.55511 0.80943 -0.02102 0.02726  -0.24172 290 LYS   A CG   
921  C  CD   . LYS   A 138 ? 0.83589 0.64867 0.96281 -0.02688 0.02691  -0.26619 290 LYS   A CD   
922  C  CE   . LYS   A 138 ? 0.86775 0.67555 0.98211 -0.04727 0.01833  -0.26072 290 LYS   A CE   
923  N  NZ   . LYS   A 138 ? 0.96656 0.76062 1.09137 -0.05836 0.01971  -0.29759 290 LYS   A NZ   
924  N  N    . TYR   A 139 ? 0.59103 0.53069 0.63282 -0.00996 0.03366  -0.20631 291 TYR   A N    
925  C  CA   . TYR   A 139 ? 0.61721 0.59713 0.63268 -0.01345 0.03837  -0.20977 291 TYR   A CA   
926  C  C    . TYR   A 139 ? 0.65248 0.64890 0.64241 -0.02960 0.03564  -0.22127 291 TYR   A C    
927  O  O    . TYR   A 139 ? 0.60201 0.58610 0.58741 -0.03920 0.02682  -0.21097 291 TYR   A O    
928  C  CB   . TYR   A 139 ? 0.54512 0.53878 0.55094 -0.01136 0.03373  -0.17867 291 TYR   A CB   
929  C  CG   . TYR   A 139 ? 0.52037 0.49858 0.54995 0.00199  0.03276  -0.16301 291 TYR   A CG   
930  C  CD1  . TYR   A 139 ? 0.49395 0.44896 0.53158 0.00200  0.02375  -0.14125 291 TYR   A CD1  
931  C  CD2  . TYR   A 139 ? 0.49544 0.48691 0.53943 0.01393  0.04072  -0.16944 291 TYR   A CD2  
932  C  CE1  . TYR   A 139 ? 0.48575 0.43130 0.54322 0.01306  0.02134  -0.12548 291 TYR   A CE1  
933  C  CE2  . TYR   A 139 ? 0.49518 0.47628 0.56239 0.02586  0.03822  -0.15397 291 TYR   A CE2  
934  C  CZ   . TYR   A 139 ? 0.50032 0.45856 0.57321 0.02514  0.02784  -0.13161 291 TYR   A CZ   
935  O  OH   . TYR   A 139 ? 0.48591 0.43831 0.58011 0.03593  0.02391  -0.11490 291 TYR   A OH   
936  N  N    . ASP   A 140 ? 0.69787 0.72654 0.67114 -0.03313 0.04313  -0.24180 292 ASP   A N    
937  C  CA   . ASP   A 140 ? 0.70618 0.75843 0.65292 -0.04913 0.03948  -0.25158 292 ASP   A CA   
938  C  C    . ASP   A 140 ? 0.65870 0.75598 0.57850 -0.05352 0.04109  -0.23981 292 ASP   A C    
939  O  O    . ASP   A 140 ? 0.65656 0.76192 0.57906 -0.04567 0.04318  -0.21947 292 ASP   A O    
940  C  CB   . ASP   A 140 ? 0.76475 0.81501 0.71490 -0.05388 0.04545  -0.29206 292 ASP   A CB   
941  C  CG   . ASP   A 140 ? 0.81885 0.88520 0.77606 -0.04344 0.06007  -0.31752 292 ASP   A CG   
942  O  OD1  . ASP   A 140 ? 0.86085 0.90033 0.84583 -0.03509 0.06604  -0.34238 292 ASP   A OD1  
943  O  OD2  . ASP   A 140 ? 0.80881 0.91539 0.74641 -0.04362 0.06589  -0.31255 292 ASP   A OD2  
944  N  N    A VAL   A 141 ? 0.64038 0.76829 0.53513 -0.06725 0.03912  -0.25091 293 VAL   A N    
945  N  N    B VAL   A 141 ? 0.64171 0.76962 0.53662 -0.06716 0.03938  -0.25171 293 VAL   A N    
946  C  CA   A VAL   A 141 ? 0.61854 0.79034 0.48795 -0.07344 0.03852  -0.23420 293 VAL   A CA   
947  C  CA   B VAL   A 141 ? 0.62090 0.79378 0.48991 -0.07359 0.03917  -0.23645 293 VAL   A CA   
948  C  C    A VAL   A 141 ? 0.62603 0.82504 0.49306 -0.06694 0.05247  -0.24470 293 VAL   A C    
949  C  C    B VAL   A 141 ? 0.62918 0.82716 0.49754 -0.06617 0.05318  -0.24603 293 VAL   A C    
950  O  O    A VAL   A 141 ? 0.62415 0.85039 0.48097 -0.06763 0.05336  -0.22196 293 VAL   A O    
951  O  O    B VAL   A 141 ? 0.61971 0.84092 0.48083 -0.06534 0.05415  -0.22219 293 VAL   A O    
952  C  CB   A VAL   A 141 ? 0.61247 0.81421 0.45583 -0.09052 0.03145  -0.24195 293 VAL   A CB   
953  C  CB   B VAL   A 141 ? 0.62081 0.82432 0.46361 -0.09063 0.03318  -0.24763 293 VAL   A CB   
954  C  CG1  A VAL   A 141 ? 0.61894 0.80254 0.46599 -0.09659 0.01697  -0.22244 293 VAL   A CG1  
955  C  CG1  B VAL   A 141 ? 0.60660 0.86344 0.42208 -0.09768 0.03631  -0.23959 293 VAL   A CG1  
956  C  CG2  A VAL   A 141 ? 0.63157 0.83613 0.47317 -0.09546 0.03808  -0.28386 293 VAL   A CG2  
957  C  CG2  B VAL   A 141 ? 0.62358 0.81409 0.46677 -0.09790 0.01807  -0.22621 293 VAL   A CG2  
958  N  N    A THR   A 142 ? 0.66288 0.85559 0.54234 -0.06060 0.06388  -0.27915 294 THR   A N    
959  N  N    B THR   A 142 ? 0.65898 0.85286 0.53815 -0.06070 0.06457  -0.28150 294 THR   A N    
960  C  CA   A THR   A 142 ? 0.64756 0.87052 0.52753 -0.05372 0.07901  -0.29231 294 THR   A CA   
961  C  CA   B THR   A 142 ? 0.65307 0.87551 0.53422 -0.05312 0.07980  -0.29449 294 THR   A CA   
962  C  C    A THR   A 142 ? 0.62411 0.83296 0.52802 -0.03899 0.08184  -0.26986 294 THR   A C    
963  C  C    B THR   A 142 ? 0.62518 0.83414 0.52902 -0.03901 0.08181  -0.26965 294 THR   A C    
964  O  O    A THR   A 142 ? 0.62049 0.86213 0.52170 -0.03617 0.09119  -0.26511 294 THR   A O    
965  O  O    B THR   A 142 ? 0.61928 0.86147 0.51923 -0.03684 0.09037  -0.26257 294 THR   A O    
966  C  CB   A THR   A 142 ? 0.69056 0.90675 0.58567 -0.04878 0.08911  -0.33224 294 THR   A CB   
967  C  CB   B THR   A 142 ? 0.69084 0.90292 0.58999 -0.04686 0.08994  -0.33404 294 THR   A CB   
968  O  OG1  A THR   A 142 ? 0.69355 0.85956 0.62270 -0.03617 0.08925  -0.34373 294 THR   A OG1  
969  O  OG1  B THR   A 142 ? 0.72017 0.93710 0.60575 -0.06006 0.08371  -0.34726 294 THR   A OG1  
970  C  CG2  A THR   A 142 ? 0.71903 0.94458 0.59756 -0.06344 0.08247  -0.34472 294 THR   A CG2  
971  C  CG2  B THR   A 142 ? 0.69950 0.94683 0.60219 -0.04005 0.10470  -0.34384 294 THR   A CG2  
972  N  N    . ASP   A 143 ? 0.62785 0.79186 0.55499 -0.03080 0.07372  -0.25539 295 ASP   A N    
973  C  CA   . ASP   A 143 ? 0.62269 0.77586 0.57072 -0.01854 0.07396  -0.23269 295 ASP   A CA   
974  C  C    . ASP   A 143 ? 0.59388 0.76693 0.52602 -0.02526 0.06731  -0.19848 295 ASP   A C    
975  O  O    . ASP   A 143 ? 0.54679 0.73523 0.48709 -0.01999 0.07172  -0.18510 295 ASP   A O    
976  C  CB   . ASP   A 143 ? 0.59853 0.70290 0.57244 -0.00991 0.06613  -0.22533 295 ASP   A CB   
977  C  CG   . ASP   A 143 ? 0.66715 0.74750 0.66657 -0.00075 0.07267  -0.25547 295 ASP   A CG   
978  O  OD1  . ASP   A 143 ? 0.69685 0.79347 0.70966 0.00872  0.08519  -0.27562 295 ASP   A OD1  
979  O  OD2  . ASP   A 143 ? 0.67461 0.72013 0.68350 -0.00305 0.06561  -0.25907 295 ASP   A OD2  
980  N  N    . VAL   A 144 ? 0.57353 0.74641 0.48656 -0.03689 0.05636  -0.18414 296 VAL   A N    
981  C  CA   . VAL   A 144 ? 0.54851 0.73904 0.45002 -0.04318 0.04963  -0.15280 296 VAL   A CA   
982  C  C    . VAL   A 144 ? 0.54866 0.78683 0.43345 -0.04984 0.05789  -0.15192 296 VAL   A C    
983  O  O    . VAL   A 144 ? 0.51441 0.76771 0.40203 -0.05029 0.05813  -0.12898 296 VAL   A O    
984  C  CB   . VAL   A 144 ? 0.61307 0.79568 0.50183 -0.05290 0.03649  -0.13983 296 VAL   A CB   
985  C  CG1  . VAL   A 144 ? 0.57366 0.76922 0.45784 -0.05720 0.02899  -0.10739 296 VAL   A CG1  
986  C  CG2  . VAL   A 144 ? 0.63012 0.77052 0.53480 -0.04790 0.03013  -0.14157 296 VAL   A CG2  
987  N  N    A SER   A 145 ? 0.57554 0.83991 0.44265 -0.05652 0.06473  -0.17697 297 SER   A N    
988  N  N    B SER   A 145 ? 0.57392 0.83840 0.44118 -0.05643 0.06486  -0.17703 297 SER   A N    
989  C  CA   A SER   A 145 ? 0.60881 0.92509 0.45703 -0.06423 0.07410  -0.17765 297 SER   A CA   
990  C  CA   B SER   A 145 ? 0.60769 0.92409 0.45597 -0.06428 0.07394  -0.17670 297 SER   A CA   
991  C  C    A SER   A 145 ? 0.60239 0.93041 0.46926 -0.05380 0.08803  -0.18283 297 SER   A C    
992  C  C    B SER   A 145 ? 0.60571 0.93494 0.47200 -0.05397 0.08844  -0.18384 297 SER   A C    
993  O  O    A SER   A 145 ? 0.58306 0.94631 0.44404 -0.05885 0.09276  -0.16479 297 SER   A O    
994  O  O    B SER   A 145 ? 0.57786 0.94488 0.43689 -0.05936 0.09402  -0.16800 297 SER   A O    
995  C  CB   A SER   A 145 ? 0.67235 1.01566 0.49747 -0.07337 0.07940  -0.20952 297 SER   A CB   
996  C  CB   B SER   A 145 ? 0.67175 1.01691 0.49509 -0.07449 0.07831  -0.20608 297 SER   A CB   
997  O  OG   A SER   A 145 ? 0.71018 1.09224 0.50515 -0.08955 0.07245  -0.19226 297 SER   A OG   
998  O  OG   B SER   A 145 ? 0.71169 1.04392 0.54892 -0.06539 0.08972  -0.24584 297 SER   A OG   
999  N  N    . LYS   A 146 ? 0.59183 0.89171 0.48426 -0.03948 0.09423  -0.20546 298 LYS   A N    
1000 C  CA   . LYS   A 146 ? 0.58792 0.89859 0.50401 -0.02748 0.10670  -0.21112 298 LYS   A CA   
1001 C  C    . LYS   A 146 ? 0.57673 0.87298 0.51122 -0.02270 0.09960  -0.17797 298 LYS   A C    
1002 O  O    . LYS   A 146 ? 0.56305 0.86652 0.52121 -0.01253 0.10758  -0.17933 298 LYS   A O    
1003 C  CB   . LYS   A 146 ? 0.62257 0.90643 0.56497 -0.01253 0.11400  -0.24467 298 LYS   A CB   
1004 C  CG   . LYS   A 146 ? 0.71111 1.01924 0.64129 -0.01565 0.12646  -0.28544 298 LYS   A CG   
1005 C  CD   . LYS   A 146 ? 0.75887 1.03241 0.72059 -0.00066 0.13198  -0.31896 298 LYS   A CD   
1006 C  CE   . LYS   A 146 ? 0.83860 1.12799 0.79372 -0.00496 0.13891  -0.35024 298 LYS   A CE   
1007 N  NZ   . LYS   A 146 ? 0.88195 1.13348 0.87312 0.00944  0.14243  -0.37838 298 LYS   A NZ   
1008 N  N    . ALA   A 147 ? 0.51390 0.79149 0.44019 -0.02962 0.08486  -0.15034 299 ALA   A N    
1009 C  CA   . ALA   A 147 ? 0.50595 0.77660 0.44499 -0.02901 0.07785  -0.11977 299 ALA   A CA   
1010 C  C    . ALA   A 147 ? 0.50852 0.81179 0.43075 -0.04310 0.07558  -0.09440 299 ALA   A C    
1011 O  O    . ALA   A 147 ? 0.50257 0.80126 0.43645 -0.04471 0.06961  -0.06926 299 ALA   A O    
1012 C  CB   . ALA   A 147 ? 0.51306 0.73860 0.45978 -0.02569 0.06346  -0.10766 299 ALA   A CB   
1013 N  N    . GLY   A 148 ? 0.49230 0.82866 0.38845 -0.05412 0.07934  -0.09977 300 GLY   A N    
1014 C  CA   . GLY   A 148 ? 0.48659 0.85904 0.36715 -0.06835 0.07747  -0.07312 300 GLY   A CA   
1015 C  C    . GLY   A 148 ? 0.49835 0.86769 0.35973 -0.07901 0.06344  -0.05545 300 GLY   A C    
1016 O  O    . GLY   A 148 ? 0.50041 0.90004 0.35006 -0.09119 0.06028  -0.03001 300 GLY   A O    
1017 N  N    . HIS   A 149 ? 0.49502 0.83111 0.35507 -0.07524 0.05467  -0.06610 301 HIS   A N    
1018 C  CA   . HIS   A 149 ? 0.45990 0.79263 0.30767 -0.08374 0.04042  -0.04820 301 HIS   A CA   
1019 C  C    . HIS   A 149 ? 0.54475 0.90911 0.36394 -0.09397 0.04126  -0.06390 301 HIS   A C    
1020 O  O    . HIS   A 149 ? 0.58058 0.95575 0.39155 -0.09238 0.05207  -0.09649 301 HIS   A O    
1021 C  CB   . HIS   A 149 ? 0.44759 0.73197 0.31071 -0.07564 0.03017  -0.04876 301 HIS   A CB   
1022 C  CG   . HIS   A 149 ? 0.42521 0.68404 0.31171 -0.06932 0.02541  -0.02848 301 HIS   A CG   
1023 N  ND1  . HIS   A 149 ? 0.42046 0.68438 0.31248 -0.07501 0.01711  0.00176  301 HIS   A ND1  
1024 C  CD2  . HIS   A 149 ? 0.42919 0.65855 0.33583 -0.05847 0.02720  -0.03471 301 HIS   A CD2  
1025 C  CE1  . HIS   A 149 ? 0.45248 0.69038 0.36654 -0.06833 0.01461  0.00982  301 HIS   A CE1  
1026 N  NE2  . HIS   A 149 ? 0.45068 0.66957 0.37208 -0.05863 0.02034  -0.01131 301 HIS   A NE2  
1027 N  N    . THR   A 150 ? 0.56371 0.94382 0.36974 -0.10450 0.02904  -0.04087 302 THR   A N    
1028 C  CA   . THR   A 150 ? 0.54996 0.96893 0.32658 -0.11725 0.02672  -0.04869 302 THR   A CA   
1029 C  C    . THR   A 150 ? 0.53939 0.93676 0.31512 -0.11846 0.01310  -0.05278 302 THR   A C    
1030 O  O    . THR   A 150 ? 0.54217 0.89701 0.33942 -0.10974 0.00623  -0.04702 302 THR   A O    
1031 C  CB   . THR   A 150 ? 0.57957 1.04423 0.34155 -0.13037 0.02241  -0.01423 302 THR   A CB   
1032 O  OG1  . THR   A 150 ? 0.62055 1.06720 0.39631 -0.13101 0.00555  0.02066  302 THR   A OG1  
1033 C  CG2  . THR   A 150 ? 0.60707 1.08878 0.37690 -0.12964 0.03476  -0.00360 302 THR   A CG2  
1034 N  N    . LEU   A 151 ? 0.51895 0.94839 0.27178 -0.12989 0.00928  -0.06263 303 LEU   A N    
1035 C  CA   . LEU   A 151 ? 0.53761 0.95394 0.29038 -0.13315 -0.00385 -0.06653 303 LEU   A CA   
1036 C  C    . LEU   A 151 ? 0.56379 0.97555 0.32628 -0.13419 -0.02031 -0.02794 303 LEU   A C    
1037 O  O    . LEU   A 151 ? 0.60104 0.99164 0.37385 -0.13260 -0.03042 -0.02904 303 LEU   A O    
1038 C  CB   . LEU   A 151 ? 0.59394 1.04031 0.33440 -0.14305 -0.00435 -0.08161 303 LEU   A CB   
1039 C  CG   . LEU   A 151 ? 0.67982 1.10530 0.42236 -0.14419 -0.00780 -0.11100 303 LEU   A CG   
1040 C  CD1  . LEU   A 151 ? 0.77269 1.16747 0.52334 -0.13545 0.00561  -0.14826 303 LEU   A CD1  
1041 C  CD2  . LEU   A 151 ? 0.68883 1.14893 0.41876 -0.15609 -0.01153 -0.11865 303 LEU   A CD2  
1042 N  N    A GLU   A 152 ? 0.55618 0.98541 0.32175 -0.13615 -0.02281 0.00641  304 GLU   A N    
1043 N  N    B GLU   A 152 ? 0.55857 0.98757 0.32427 -0.13609 -0.02284 0.00647  304 GLU   A N    
1044 C  CA   A GLU   A 152 ? 0.57449 0.99079 0.36072 -0.13373 -0.03754 0.04304  304 GLU   A CA   
1045 C  CA   B GLU   A 152 ? 0.57382 0.99000 0.36004 -0.13374 -0.03771 0.04288  304 GLU   A CA   
1046 C  C    A GLU   A 152 ? 0.53935 0.90149 0.35483 -0.11982 -0.03898 0.03750  304 GLU   A C    
1047 C  C    B GLU   A 152 ? 0.53707 0.89904 0.35267 -0.11978 -0.03903 0.03753  304 GLU   A C    
1048 O  O    A GLU   A 152 ? 0.50724 0.85587 0.33941 -0.11692 -0.05116 0.05342  304 GLU   A O    
1049 O  O    B GLU   A 152 ? 0.51047 0.85864 0.34298 -0.11679 -0.05117 0.05356  304 GLU   A O    
1050 C  CB   A GLU   A 152 ? 0.61421 1.04727 0.40642 -0.13660 -0.03736 0.07784  304 GLU   A CB   
1051 C  CB   B GLU   A 152 ? 0.61198 1.04566 0.40397 -0.13685 -0.03800 0.07836  304 GLU   A CB   
1052 C  CG   A GLU   A 152 ? 0.65497 1.13448 0.43615 -0.14910 -0.04239 0.09955  304 GLU   A CG   
1053 C  CG   B GLU   A 152 ? 0.64696 1.10701 0.44253 -0.14485 -0.05330 0.11575  304 GLU   A CG   
1054 C  CD   A GLU   A 152 ? 0.68337 1.16300 0.48309 -0.15024 -0.06060 0.13665  304 GLU   A CD   
1055 C  CD   B GLU   A 152 ? 0.69655 1.20210 0.47778 -0.15637 -0.04871 0.11827  304 GLU   A CD   
1056 O  OE1  A GLU   A 152 ? 0.69791 1.18607 0.51236 -0.15307 -0.06478 0.17146  304 GLU   A OE1  
1057 O  OE1  B GLU   A 152 ? 0.69686 1.21707 0.46370 -0.15845 -0.03370 0.09533  304 GLU   A OE1  
1058 O  OE2  A GLU   A 152 ? 0.66036 1.13123 0.46367 -0.14811 -0.07065 0.13087  304 GLU   A OE2  
1059 O  OE2  B GLU   A 152 ? 0.71048 1.23891 0.49655 -0.16307 -0.06020 0.14311  304 GLU   A OE2  
1060 N  N    . LEU   A 153 ? 0.48665 0.82069 0.30943 -0.11105 -0.02665 0.01541  305 LEU   A N    
1061 C  CA   . LEU   A 153 ? 0.44862 0.73588 0.29472 -0.09919 -0.02683 0.00792  305 LEU   A CA   
1062 C  C    . LEU   A 153 ? 0.46898 0.73892 0.31082 -0.09764 -0.02334 -0.02414 305 LEU   A C    
1063 O  O    . LEU   A 153 ? 0.50750 0.75172 0.36295 -0.09354 -0.02907 -0.02557 305 LEU   A O    
1064 C  CB   . LEU   A 153 ? 0.43122 0.69877 0.29195 -0.09069 -0.01767 0.00955  305 LEU   A CB   
1065 C  CG   . LEU   A 153 ? 0.39744 0.62142 0.27948 -0.07917 -0.01714 0.00196  305 LEU   A CG   
1066 C  CD1  . LEU   A 153 ? 0.39979 0.60825 0.29998 -0.07639 -0.02849 0.02261  305 LEU   A CD1  
1067 C  CD2  . LEU   A 153 ? 0.37042 0.58362 0.26291 -0.07257 -0.00781 -0.00065 305 LEU   A CD2  
1068 N  N    . ILE   A 154 ? 0.51137 0.79603 0.33637 -0.10142 -0.01370 -0.05026 306 ILE   A N    
1069 C  CA   . ILE   A 154 ? 0.52776 0.78904 0.35505 -0.09899 -0.00917 -0.08176 306 ILE   A CA   
1070 C  C    . ILE   A 154 ? 0.50036 0.76667 0.32186 -0.10783 -0.01974 -0.08741 306 ILE   A C    
1071 O  O    . ILE   A 154 ? 0.47380 0.71012 0.30855 -0.10508 -0.02181 -0.09769 306 ILE   A O    
1072 C  CB   . ILE   A 154 ? 0.56043 0.83620 0.37588 -0.09969 0.00452  -0.11076 306 ILE   A CB   
1073 C  CG1  . ILE   A 154 ? 0.51837 0.78779 0.34566 -0.08962 0.01507  -0.10551 306 ILE   A CG1  
1074 C  CG2  . ILE   A 154 ? 0.58774 0.83749 0.40941 -0.09806 0.00791  -0.14338 306 ILE   A CG2  
1075 C  CD1  . ILE   A 154 ? 0.57694 0.86884 0.39524 -0.08930 0.02984  -0.13191 306 ILE   A CD1  
1076 N  N    . GLU   A 155 ? 0.56088 0.86800 0.36315 -0.11961 -0.02704 -0.07950 307 GLU   A N    
1077 C  CA   . GLU   A 155 ? 0.52468 0.84193 0.32278 -0.12907 -0.03858 -0.08401 307 GLU   A CA   
1078 C  C    . GLU   A 155 ? 0.51733 0.81138 0.33921 -0.12335 -0.04871 -0.06287 307 GLU   A C    
1079 O  O    . GLU   A 155 ? 0.55942 0.83327 0.39149 -0.12426 -0.05105 -0.07653 307 GLU   A O    
1080 C  CB   . GLU   A 155 ? 0.61342 0.98322 0.38750 -0.14242 -0.04559 -0.07516 307 GLU   A CB   
1081 C  CG   . GLU   A 155 ? 0.71824 1.09798 0.49295 -0.15119 -0.05447 -0.08399 307 GLU   A CG   
1082 C  CD   . GLU   A 155 ? 0.79474 1.19461 0.57726 -0.15397 -0.07051 -0.04993 307 GLU   A CD   
1083 O  OE1  . GLU   A 155 ? 0.80361 1.20594 0.59345 -0.14854 -0.07521 -0.01930 307 GLU   A OE1  
1084 O  OE2  . GLU   A 155 ? 0.83581 1.24864 0.62007 -0.16121 -0.07868 -0.05348 307 GLU   A OE2  
1085 N  N    . PRO   A 156 ? 0.50923 0.80491 0.34317 -0.11766 -0.05436 -0.03107 308 PRO   A N    
1086 C  CA   . PRO   A 156 ? 0.49966 0.77243 0.35915 -0.11052 -0.06170 -0.01668 308 PRO   A CA   
1087 C  C    . PRO   A 156 ? 0.51940 0.74924 0.39447 -0.10073 -0.05318 -0.03004 308 PRO   A C    
1088 O  O    . PRO   A 156 ? 0.47621 0.68994 0.36782 -0.09787 -0.05707 -0.02851 308 PRO   A O    
1089 C  CB   . PRO   A 156 ? 0.56343 0.84464 0.43440 -0.10567 -0.06748 0.01663  308 PRO   A CB   
1090 C  CG   . PRO   A 156 ? 0.59560 0.91508 0.44348 -0.11499 -0.06769 0.02491  308 PRO   A CG   
1091 C  CD   . PRO   A 156 ? 0.54935 0.86823 0.37722 -0.11812 -0.05455 -0.00668 308 PRO   A CD   
1092 N  N    . LEU   A 157 ? 0.45930 0.67369 0.33037 -0.09574 -0.04177 -0.04191 309 LEU   A N    
1093 C  CA   . LEU   A 157 ? 0.45511 0.63192 0.34040 -0.08697 -0.03497 -0.05216 309 LEU   A CA   
1094 C  C    . LEU   A 157 ? 0.48436 0.64781 0.37007 -0.09194 -0.03422 -0.07425 309 LEU   A C    
1095 O  O    . LEU   A 157 ? 0.47793 0.61824 0.37834 -0.08888 -0.03513 -0.07344 309 LEU   A O    
1096 C  CB   . LEU   A 157 ? 0.46692 0.63526 0.35026 -0.08048 -0.02421 -0.05841 309 LEU   A CB   
1097 C  CG   . LEU   A 157 ? 0.47448 0.60782 0.37216 -0.07123 -0.01799 -0.06692 309 LEU   A CG   
1098 C  CD1  . LEU   A 157 ? 0.47920 0.59501 0.39282 -0.06580 -0.02308 -0.05096 309 LEU   A CD1  
1099 C  CD2  . LEU   A 157 ? 0.47159 0.60366 0.37013 -0.06460 -0.00879 -0.07031 309 LEU   A CD2  
1100 N  N    . ILE   A 158 ? 0.49765 0.67656 0.36792 -0.10069 -0.03228 -0.09479 310 ILE   A N    
1101 C  CA   . ILE   A 158 ? 0.52844 0.69308 0.40199 -0.10728 -0.03221 -0.11743 310 ILE   A CA   
1102 C  C    . ILE   A 158 ? 0.48708 0.66016 0.36739 -0.11498 -0.04327 -0.10861 310 ILE   A C    
1103 O  O    . ILE   A 158 ? 0.49823 0.64917 0.39293 -0.11648 -0.04380 -0.11355 310 ILE   A O    
1104 C  CB   . ILE   A 158 ? 0.57132 0.75311 0.42762 -0.11556 -0.02763 -0.14529 310 ILE   A CB   
1105 C  CG1  . ILE   A 158 ? 0.57766 0.74752 0.43457 -0.10589 -0.01468 -0.15764 310 ILE   A CG1  
1106 C  CG2  . ILE   A 158 ? 0.59672 0.76568 0.45860 -0.12540 -0.03009 -0.16892 310 ILE   A CG2  
1107 C  CD1  . ILE   A 158 ? 0.60055 0.72687 0.47937 -0.09727 -0.00903 -0.16707 310 ILE   A CD1  
1108 N  N    A LYS   A 159 ? 0.50358 0.71102 0.37572 -0.12024 -0.05252 -0.09357 311 LYS   A N    
1109 N  N    B LYS   A 159 ? 0.50468 0.71211 0.37683 -0.12021 -0.05251 -0.09351 311 LYS   A N    
1110 C  CA   A LYS   A 159 ? 0.49794 0.71794 0.38083 -0.12602 -0.06367 -0.08315 311 LYS   A CA   
1111 C  CA   B LYS   A 159 ? 0.49606 0.71616 0.37892 -0.12598 -0.06368 -0.08301 311 LYS   A CA   
1112 C  C    A LYS   A 159 ? 0.47082 0.66742 0.37721 -0.11587 -0.06309 -0.06749 311 LYS   A C    
1113 C  C    B LYS   A 159 ? 0.47266 0.66896 0.37905 -0.11586 -0.06300 -0.06768 311 LYS   A C    
1114 O  O    A LYS   A 159 ? 0.45880 0.65340 0.37908 -0.11989 -0.06714 -0.06771 311 LYS   A O    
1115 O  O    B LYS   A 159 ? 0.45469 0.64833 0.37498 -0.11986 -0.06685 -0.06821 311 LYS   A O    
1116 C  CB   A LYS   A 159 ? 0.54406 0.80600 0.41773 -0.13095 -0.07469 -0.06459 311 LYS   A CB   
1117 C  CB   B LYS   A 159 ? 0.54291 0.80473 0.41671 -0.13067 -0.07463 -0.06408 311 LYS   A CB   
1118 C  CG   A LYS   A 159 ? 0.62181 0.91721 0.46908 -0.14445 -0.07711 -0.08049 311 LYS   A CG   
1119 C  CG   B LYS   A 159 ? 0.62301 0.91904 0.47063 -0.14437 -0.07747 -0.07949 311 LYS   A CG   
1120 C  CD   A LYS   A 159 ? 0.66085 0.99975 0.49733 -0.14842 -0.08783 -0.05542 311 LYS   A CD   
1121 C  CD   B LYS   A 159 ? 0.66213 1.00230 0.50104 -0.14902 -0.08970 -0.05413 311 LYS   A CD   
1122 C  CE   A LYS   A 159 ? 0.68747 1.05271 0.53325 -0.15627 -0.10326 -0.04456 311 LYS   A CE   
1123 C  CE   B LYS   A 159 ? 0.70819 1.07949 0.53461 -0.16226 -0.09567 -0.06480 311 LYS   A CE   
1124 N  NZ   A LYS   A 159 ? 0.67984 1.03241 0.55629 -0.14493 -0.10881 -0.01916 311 LYS   A NZ   
1125 N  NZ   B LYS   A 159 ? 0.74084 1.09584 0.55889 -0.16834 -0.08600 -0.10204 311 LYS   A NZ   
1126 N  N    . PHE   A 160 ? 0.44297 0.62453 0.35427 -0.10370 -0.05774 -0.05511 312 PHE   A N    
1127 C  CA   . PHE   A 160 ? 0.38426 0.54543 0.31554 -0.09440 -0.05604 -0.04435 312 PHE   A CA   
1128 C  C    . PHE   A 160 ? 0.42620 0.55884 0.36295 -0.09484 -0.04905 -0.05833 312 PHE   A C    
1129 O  O    . PHE   A 160 ? 0.42841 0.55555 0.37921 -0.09555 -0.04998 -0.05505 312 PHE   A O    
1130 C  CB   . PHE   A 160 ? 0.42333 0.57629 0.35802 -0.08316 -0.05268 -0.03056 312 PHE   A CB   
1131 C  CG   . PHE   A 160 ? 0.44347 0.57517 0.39541 -0.07398 -0.04934 -0.02511 312 PHE   A CG   
1132 C  CD1  . PHE   A 160 ? 0.46651 0.60608 0.43653 -0.06953 -0.05454 -0.01230 312 PHE   A CD1  
1133 C  CD2  . PHE   A 160 ? 0.42809 0.53465 0.37922 -0.06965 -0.04117 -0.03338 312 PHE   A CD2  
1134 C  CE1  . PHE   A 160 ? 0.42530 0.54930 0.40952 -0.06173 -0.05033 -0.01116 312 PHE   A CE1  
1135 C  CE2  . PHE   A 160 ? 0.45402 0.54652 0.41747 -0.06285 -0.03849 -0.02894 312 PHE   A CE2  
1136 C  CZ   . PHE   A 160 ? 0.42250 0.52440 0.40113 -0.05929 -0.04242 -0.01947 312 PHE   A CZ   
1137 N  N    . GLN   A 161 ? 0.43616 0.55199 0.36407 -0.09425 -0.04184 -0.07267 313 GLN   A N    
1138 C  CA   . GLN   A 161 ? 0.42654 0.51356 0.36270 -0.09438 -0.03635 -0.08265 313 GLN   A CA   
1139 C  C    . GLN   A 161 ? 0.40168 0.49021 0.34361 -0.10706 -0.04043 -0.09218 313 GLN   A C    
1140 O  O    . GLN   A 161 ? 0.44392 0.51634 0.39887 -0.10892 -0.03906 -0.08926 313 GLN   A O    
1141 C  CB   . GLN   A 161 ? 0.44052 0.51183 0.37063 -0.09066 -0.02885 -0.09725 313 GLN   A CB   
1142 C  CG   . GLN   A 161 ? 0.41098 0.47989 0.33901 -0.07889 -0.02415 -0.08794 313 GLN   A CG   
1143 C  CD   . GLN   A 161 ? 0.42698 0.47855 0.36697 -0.07082 -0.02305 -0.07393 313 GLN   A CD   
1144 O  OE1  . GLN   A 161 ? 0.42638 0.46031 0.37545 -0.07220 -0.02227 -0.07451 313 GLN   A OE1  
1145 N  NE2  . GLN   A 161 ? 0.42050 0.47859 0.36067 -0.06361 -0.02319 -0.06113 313 GLN   A NE2  
1146 N  N    . VAL   A 162 ? 0.44777 0.55839 0.38002 -0.11734 -0.04579 -0.10302 314 VAL   A N    
1147 C  CA   . VAL   A 162 ? 0.46130 0.57602 0.40014 -0.13158 -0.05087 -0.11383 314 VAL   A CA   
1148 C  C    . VAL   A 162 ? 0.46024 0.59034 0.41334 -0.13349 -0.05691 -0.09664 314 VAL   A C    
1149 O  O    . VAL   A 162 ? 0.46927 0.58989 0.43698 -0.14030 -0.05669 -0.09719 314 VAL   A O    
1150 C  CB   . VAL   A 162 ? 0.49414 0.63417 0.41695 -0.14301 -0.05599 -0.13145 314 VAL   A CB   
1151 C  CG1  . VAL   A 162 ? 0.47426 0.62646 0.40528 -0.15940 -0.06413 -0.14009 314 VAL   A CG1  
1152 C  CG2  . VAL   A 162 ? 0.47201 0.59507 0.38558 -0.14197 -0.04779 -0.15503 314 VAL   A CG2  
1153 N  N    . GLY   A 163 ? 0.49912 0.65400 0.45110 -0.12741 -0.06206 -0.08043 315 GLY   A N    
1154 C  CA   . GLY   A 163 ? 0.45513 0.62696 0.42512 -0.12682 -0.06722 -0.06561 315 GLY   A CA   
1155 C  C    . GLY   A 163 ? 0.41512 0.56672 0.39961 -0.11895 -0.05967 -0.05788 315 GLY   A C    
1156 O  O    . GLY   A 163 ? 0.39361 0.55418 0.39448 -0.12297 -0.06050 -0.05350 315 GLY   A O    
1157 N  N    . LEU   A 164 ? 0.38102 0.50920 0.35954 -0.10849 -0.05217 -0.05623 316 LEU   A N    
1158 C  CA   . LEU   A 164 ? 0.40644 0.51859 0.39484 -0.10224 -0.04533 -0.04972 316 LEU   A CA   
1159 C  C    . LEU   A 164 ? 0.42311 0.51735 0.41570 -0.11189 -0.04153 -0.05625 316 LEU   A C    
1160 O  O    . LEU   A 164 ? 0.43111 0.52699 0.43528 -0.11410 -0.03856 -0.04938 316 LEU   A O    
1161 C  CB   . LEU   A 164 ? 0.40424 0.49951 0.38516 -0.08983 -0.04013 -0.04613 316 LEU   A CB   
1162 C  CG   . LEU   A 164 ? 0.39786 0.48021 0.38502 -0.08332 -0.03382 -0.04002 316 LEU   A CG   
1163 C  CD1  . LEU   A 164 ? 0.38650 0.48812 0.38832 -0.08059 -0.03432 -0.03279 316 LEU   A CD1  
1164 C  CD2  . LEU   A 164 ? 0.34449 0.41374 0.32433 -0.07268 -0.03071 -0.03787 316 LEU   A CD2  
1165 N  N    . LYS   A 165 ? 0.39323 0.47099 0.37832 -0.11798 -0.04119 -0.06947 317 LYS   A N    
1166 C  CA   . LYS   A 165 ? 0.48130 0.53822 0.47520 -0.12796 -0.03883 -0.07488 317 LYS   A CA   
1167 C  C    . LYS   A 165 ? 0.47758 0.55215 0.48412 -0.14267 -0.04358 -0.07515 317 LYS   A C    
1168 O  O    . LYS   A 165 ? 0.57911 0.64555 0.59856 -0.15015 -0.04095 -0.06895 317 LYS   A O    
1169 C  CB   . LYS   A 165 ? 0.55448 0.59042 0.54239 -0.13051 -0.03778 -0.09279 317 LYS   A CB   
1170 C  CG   . LYS   A 165 ? 0.58024 0.58248 0.58028 -0.13328 -0.03361 -0.09386 317 LYS   A CG   
1171 C  CD   . LYS   A 165 ? 0.59382 0.57961 0.59225 -0.11896 -0.02814 -0.08193 317 LYS   A CD   
1172 C  CE   . LYS   A 165 ? 0.63096 0.58304 0.64314 -0.12032 -0.02558 -0.08195 317 LYS   A CE   
1173 N  NZ   . LYS   A 165 ? 0.54479 0.48656 0.55711 -0.10841 -0.02219 -0.06535 317 LYS   A NZ   
1174 N  N    . LYS   A 166 ? 0.46821 0.57016 0.47199 -0.14792 -0.05109 -0.08046 318 LYS   A N    
1175 C  CA   . LYS   A 166 ? 0.46190 0.58579 0.47960 -0.16249 -0.05702 -0.08110 318 LYS   A CA   
1176 C  C    . LYS   A 166 ? 0.49830 0.63981 0.53218 -0.15934 -0.05455 -0.06438 318 LYS   A C    
1177 O  O    . LYS   A 166 ? 0.43136 0.58864 0.48131 -0.17193 -0.05678 -0.06284 318 LYS   A O    
1178 C  CB   . LYS   A 166 ? 0.49929 0.65433 0.50975 -0.16762 -0.06718 -0.08796 318 LYS   A CB   
1179 C  CG   . LYS   A 166 ? 0.58710 0.73373 0.58353 -0.17722 -0.06992 -0.11025 318 LYS   A CG   
1180 C  CD   . LYS   A 166 ? 0.59673 0.78155 0.58194 -0.18285 -0.08062 -0.11450 318 LYS   A CD   
1181 C  CE   . LYS   A 166 ? 0.69907 0.88190 0.67085 -0.19622 -0.08333 -0.14154 318 LYS   A CE   
1182 N  NZ   . LYS   A 166 ? 0.66424 0.89113 0.62248 -0.20436 -0.09502 -0.14480 318 LYS   A NZ   
1183 N  N    . LEU   A 167 ? 0.44990 0.59111 0.48135 -0.14348 -0.04956 -0.05357 319 LEU   A N    
1184 C  CA   . LEU   A 167 ? 0.44509 0.60415 0.49212 -0.13956 -0.04530 -0.04193 319 LEU   A CA   
1185 C  C    . LEU   A 167 ? 0.46874 0.61372 0.52145 -0.14694 -0.03737 -0.03719 319 LEU   A C    
1186 O  O    . LEU   A 167 ? 0.44110 0.60746 0.50837 -0.14996 -0.03346 -0.02975 319 LEU   A O    
1187 C  CB   . LEU   A 167 ? 0.37852 0.53985 0.42240 -0.12120 -0.04235 -0.03534 319 LEU   A CB   
1188 C  CG   . LEU   A 167 ? 0.38883 0.56995 0.43436 -0.11378 -0.05071 -0.03315 319 LEU   A CG   
1189 C  CD1  . LEU   A 167 ? 0.40070 0.58124 0.45025 -0.09675 -0.04751 -0.02624 319 LEU   A CD1  
1190 C  CD2  . LEU   A 167 ? 0.39408 0.60948 0.45850 -0.12130 -0.05805 -0.03069 319 LEU   A CD2  
1191 N  N    A ASN   A 168 ? 0.45978 0.57182 0.50320 -0.14980 -0.03488 -0.04017 320 ASN   A N    
1192 N  N    B ASN   A 168 ? 0.46181 0.57386 0.50532 -0.15008 -0.03502 -0.04038 320 ASN   A N    
1193 C  CA   A ASN   A 168 ? 0.47180 0.56843 0.52121 -0.15754 -0.02888 -0.03136 320 ASN   A CA   
1194 C  CA   B ASN   A 168 ? 0.47206 0.56773 0.52094 -0.15718 -0.02887 -0.03151 320 ASN   A CA   
1195 C  C    A ASN   A 168 ? 0.45315 0.56526 0.50317 -0.14957 -0.02120 -0.01873 320 ASN   A C    
1196 C  C    B ASN   A 168 ? 0.45329 0.56545 0.50329 -0.14952 -0.02129 -0.01889 320 ASN   A C    
1197 O  O    A ASN   A 168 ? 0.46953 0.59788 0.53050 -0.15875 -0.01663 -0.00967 320 ASN   A O    
1198 O  O    B ASN   A 168 ? 0.46892 0.59781 0.53015 -0.15882 -0.01688 -0.01005 320 ASN   A O    
1199 C  CB   A ASN   A 168 ? 0.49997 0.60301 0.56624 -0.17777 -0.03153 -0.03192 320 ASN   A CB   
1200 C  CB   B ASN   A 168 ? 0.50375 0.60265 0.56903 -0.17756 -0.03140 -0.03217 320 ASN   A CB   
1201 C  CG   A ASN   A 168 ? 0.54858 0.63881 0.61447 -0.18724 -0.03939 -0.04893 320 ASN   A CG   
1202 C  CG   B ASN   A 168 ? 0.52677 0.59626 0.59755 -0.18662 -0.02771 -0.02361 320 ASN   A CG   
1203 O  OD1  A ASN   A 168 ? 0.56649 0.62410 0.62639 -0.18638 -0.03935 -0.05703 320 ASN   A OD1  
1204 O  OD1  B ASN   A 168 ? 0.54463 0.58954 0.60606 -0.17706 -0.02471 -0.01905 320 ASN   A OD1  
1205 N  ND2  A ASN   A 168 ? 0.60905 0.72739 0.68263 -0.19628 -0.04628 -0.05566 320 ASN   A ND2  
1206 N  ND2  B ASN   A 168 ? 0.54070 0.61357 0.62925 -0.20562 -0.02872 -0.01952 320 ASN   A ND2  
1207 N  N    . LEU   A 169 ? 0.40101 0.51057 0.43948 -0.13326 -0.01943 -0.01932 321 LEU   A N    
1208 C  CA   . LEU   A 169 ? 0.45406 0.57970 0.49218 -0.12509 -0.01236 -0.01247 321 LEU   A CA   
1209 C  C    . LEU   A 169 ? 0.46328 0.58010 0.49764 -0.13192 -0.00644 -0.00083 321 LEU   A C    
1210 O  O    . LEU   A 169 ? 0.47816 0.56620 0.50687 -0.13492 -0.00829 0.00284  321 LEU   A O    
1211 C  CB   . LEU   A 169 ? 0.42241 0.54119 0.44976 -0.10819 -0.01271 -0.01657 321 LEU   A CB   
1212 C  CG   . LEU   A 169 ? 0.39199 0.52046 0.42316 -0.10003 -0.01878 -0.02311 321 LEU   A CG   
1213 C  CD1  . LEU   A 169 ? 0.37843 0.49830 0.40177 -0.08529 -0.01811 -0.02436 321 LEU   A CD1  
1214 C  CD2  . LEU   A 169 ? 0.35011 0.51141 0.40057 -0.10084 -0.01907 -0.02273 321 LEU   A CD2  
1215 N  N    . HIS   A 170 ? 0.42978 0.57396 0.46893 -0.13446 0.00076  0.00565  322 HIS   A N    
1216 C  CA   . HIS   A 170 ? 0.39483 0.53762 0.42496 -0.13804 0.00660  0.01853  322 HIS   A CA   
1217 C  C    . HIS   A 170 ? 0.39370 0.52122 0.40729 -0.12368 0.00599  0.01616  322 HIS   A C    
1218 O  O    . HIS   A 170 ? 0.43034 0.55812 0.44183 -0.11081 0.00406  0.00452  322 HIS   A O    
1219 C  CB   . HIS   A 170 ? 0.38909 0.57204 0.42470 -0.14245 0.01598  0.02274  322 HIS   A CB   
1220 C  CG   . HIS   A 170 ? 0.41193 0.61557 0.46650 -0.15773 0.01740  0.02667  322 HIS   A CG   
1221 N  ND1  . HIS   A 170 ? 0.39938 0.64424 0.46316 -0.16340 0.02687  0.02997  322 HIS   A ND1  
1222 C  CD2  . HIS   A 170 ? 0.42868 0.62009 0.49589 -0.16938 0.01070  0.02646  322 HIS   A CD2  
1223 C  CE1  . HIS   A 170 ? 0.39497 0.65244 0.47765 -0.17807 0.02567  0.03373  322 HIS   A CE1  
1224 N  NE2  . HIS   A 170 ? 0.40725 0.63188 0.49207 -0.18241 0.01529  0.03126  322 HIS   A NE2  
1225 N  N    . GLU   A 171 ? 0.40183 0.51662 0.40571 -0.12664 0.00669  0.02913  323 GLU   A N    
1226 C  CA   . GLU   A 171 ? 0.39839 0.50448 0.38777 -0.11435 0.00573  0.02785  323 GLU   A CA   
1227 C  C    . GLU   A 171 ? 0.42617 0.56103 0.41053 -0.10584 0.01127  0.01791  323 GLU   A C    
1228 O  O    . GLU   A 171 ? 0.42654 0.55478 0.40475 -0.09378 0.00921  0.00868  323 GLU   A O    
1229 C  CB   . GLU   A 171 ? 0.48214 0.57837 0.46397 -0.11992 0.00497  0.04676  323 GLU   A CB   
1230 C  CG   . GLU   A 171 ? 0.56888 0.64778 0.54029 -0.10815 0.00052  0.04651  323 GLU   A CG   
1231 C  CD   . GLU   A 171 ? 0.62737 0.69934 0.59438 -0.11315 -0.00203 0.06837  323 GLU   A CD   
1232 O  OE1  . GLU   A 171 ? 0.66546 0.74693 0.63594 -0.12653 0.00019  0.08526  323 GLU   A OE1  
1233 O  OE2  . GLU   A 171 ? 0.67017 0.72898 0.63204 -0.10415 -0.00674 0.07059  323 GLU   A OE2  
1234 N  N    . GLU   A 172 ? 0.38026 0.54774 0.36983 -0.11226 0.01874  0.01836  324 GLU   A N    
1235 C  CA   . GLU   A 172 ? 0.40020 0.59626 0.38995 -0.10352 0.02528  0.00448  324 GLU   A CA   
1236 C  C    . GLU   A 172 ? 0.39816 0.58818 0.40108 -0.09090 0.02159  -0.01139 324 GLU   A C    
1237 O  O    . GLU   A 172 ? 0.41430 0.60651 0.41629 -0.07920 0.02229  -0.02340 324 GLU   A O    
1238 C  CB   . GLU   A 172 ? 0.35476 0.59007 0.35180 -0.11307 0.03521  0.00672  324 GLU   A CB   
1239 C  CG   . GLU   A 172 ? 0.45742 0.70786 0.43943 -0.12603 0.04011  0.02440  324 GLU   A CG   
1240 C  CD   . GLU   A 172 ? 0.54401 0.77691 0.53084 -0.14152 0.03591  0.04596  324 GLU   A CD   
1241 O  OE1  . GLU   A 172 ? 0.57667 0.82595 0.55662 -0.15479 0.04006  0.06472  324 GLU   A OE1  
1242 O  OE2  . GLU   A 172 ? 0.50210 0.70569 0.50013 -0.14125 0.02837  0.04417  324 GLU   A OE2  
1243 N  N    . GLU   A 173 ? 0.30620 0.48968 0.32251 -0.09410 0.01687  -0.01083 325 GLU   A N    
1244 C  CA   . GLU   A 173 ? 0.29320 0.47348 0.32187 -0.08340 0.01167  -0.02112 325 GLU   A CA   
1245 C  C    . GLU   A 173 ? 0.36740 0.51705 0.38519 -0.07582 0.00452  -0.02235 325 GLU   A C    
1246 O  O    . GLU   A 173 ? 0.34016 0.48751 0.36367 -0.06476 0.00174  -0.02952 325 GLU   A O    
1247 C  CB   . GLU   A 173 ? 0.31738 0.50567 0.36165 -0.09096 0.00758  -0.01913 325 GLU   A CB   
1248 C  CG   . GLU   A 173 ? 0.33716 0.56191 0.39867 -0.09673 0.01468  -0.01927 325 GLU   A CG   
1249 C  CD   . GLU   A 173 ? 0.35239 0.58281 0.42384 -0.11227 0.01138  -0.01229 325 GLU   A CD   
1250 O  OE1  . GLU   A 173 ? 0.40920 0.67211 0.49774 -0.11843 0.01669  -0.01139 325 GLU   A OE1  
1251 O  OE2  . GLU   A 173 ? 0.33451 0.53853 0.39849 -0.11874 0.00382  -0.00933 325 GLU   A OE2  
1252 N  N    . HIS   A 174 ? 0.35931 0.48596 0.36438 -0.08162 0.00171  -0.01477 326 HIS   A N    
1253 C  CA   . HIS   A 174 ? 0.37757 0.47882 0.37366 -0.07466 -0.00362 -0.01632 326 HIS   A CA   
1254 C  C    . HIS   A 174 ? 0.39361 0.49578 0.38337 -0.06474 -0.00203 -0.02046 326 HIS   A C    
1255 O  O    . HIS   A 174 ? 0.36632 0.46047 0.35800 -0.05619 -0.00555 -0.02581 326 HIS   A O    
1256 C  CB   . HIS   A 174 ? 0.36388 0.44255 0.35255 -0.08166 -0.00559 -0.00835 326 HIS   A CB   
1257 C  CG   . HIS   A 174 ? 0.41664 0.47245 0.39886 -0.07452 -0.00974 -0.01104 326 HIS   A CG   
1258 N  ND1  . HIS   A 174 ? 0.41279 0.46198 0.39676 -0.07193 -0.01366 -0.01844 326 HIS   A ND1  
1259 C  CD2  . HIS   A 174 ? 0.41532 0.45744 0.39013 -0.06989 -0.01038 -0.00676 326 HIS   A CD2  
1260 C  CE1  . HIS   A 174 ? 0.43529 0.46814 0.41326 -0.06597 -0.01510 -0.01972 326 HIS   A CE1  
1261 N  NE2  . HIS   A 174 ? 0.40753 0.43512 0.38155 -0.06410 -0.01347 -0.01277 326 HIS   A NE2  
1262 N  N    . VAL   A 175 ? 0.35601 0.47027 0.33829 -0.06717 0.00296  -0.01777 327 VAL   A N    
1263 C  CA   . VAL   A 175 ? 0.33038 0.44737 0.30553 -0.05971 0.00369  -0.02393 327 VAL   A CA   
1264 C  C    . VAL   A 175 ? 0.35718 0.49052 0.34514 -0.05194 0.00681  -0.03846 327 VAL   A C    
1265 O  O    . VAL   A 175 ? 0.33928 0.46671 0.32872 -0.04411 0.00484  -0.04689 327 VAL   A O    
1266 C  CB   . VAL   A 175 ? 0.34625 0.47485 0.30674 -0.06605 0.00692  -0.01596 327 VAL   A CB   
1267 C  CG1  . VAL   A 175 ? 0.41555 0.52445 0.37016 -0.07240 0.00268  0.00066  327 VAL   A CG1  
1268 C  CG2  . VAL   A 175 ? 0.31886 0.47862 0.28112 -0.07282 0.01524  -0.01699 327 VAL   A CG2  
1269 N  N    . LEU   A 176 ? 0.30362 0.45739 0.30474 -0.05377 0.01145  -0.04186 328 LEU   A N    
1270 C  CA   . LEU   A 176 ? 0.32826 0.49585 0.34856 -0.04419 0.01402  -0.05600 328 LEU   A CA   
1271 C  C    . LEU   A 176 ? 0.32599 0.47487 0.35939 -0.03605 0.00586  -0.05604 328 LEU   A C    
1272 O  O    . LEU   A 176 ? 0.33989 0.48542 0.38558 -0.02663 0.00478  -0.06537 328 LEU   A O    
1273 C  CB   . LEU   A 176 ? 0.28395 0.48029 0.31964 -0.04731 0.02058  -0.05828 328 LEU   A CB   
1274 C  CG   . LEU   A 176 ? 0.33843 0.56506 0.36762 -0.05189 0.03172  -0.06455 328 LEU   A CG   
1275 C  CD1  . LEU   A 176 ? 0.29764 0.55334 0.34079 -0.05870 0.03820  -0.06157 328 LEU   A CD1  
1276 C  CD2  . LEU   A 176 ? 0.36176 0.59899 0.39885 -0.04093 0.03655  -0.08543 328 LEU   A CD2  
1277 N  N    . LEU   A 177 ? 0.33060 0.46786 0.36182 -0.04056 -0.00012 -0.04559 329 LEU   A N    
1278 C  CA   . LEU   A 177 ? 0.29140 0.41677 0.33189 -0.03495 -0.00797 -0.04284 329 LEU   A CA   
1279 C  C    . LEU   A 177 ? 0.29980 0.40495 0.33152 -0.03038 -0.01113 -0.04308 329 LEU   A C    
1280 O  O    . LEU   A 177 ? 0.30907 0.40881 0.35369 -0.02337 -0.01531 -0.04359 329 LEU   A O    
1281 C  CB   . LEU   A 177 ? 0.31608 0.43817 0.35182 -0.04291 -0.01297 -0.03441 329 LEU   A CB   
1282 C  CG   . LEU   A 177 ? 0.37748 0.49655 0.42045 -0.03976 -0.02136 -0.02962 329 LEU   A CG   
1283 C  CD1  . LEU   A 177 ? 0.34335 0.47944 0.41279 -0.03187 -0.02365 -0.02991 329 LEU   A CD1  
1284 C  CD2  . LEU   A 177 ? 0.38025 0.49958 0.41449 -0.04981 -0.02555 -0.02561 329 LEU   A CD2  
1285 N  N    . MET   A 178 ? 0.31592 0.41070 0.32857 -0.03462 -0.00975 -0.04090 330 MET   A N    
1286 C  CA   . MET   A 178 ? 0.31391 0.39367 0.32028 -0.03080 -0.01254 -0.04125 330 MET   A CA   
1287 C  C    . MET   A 178 ? 0.33043 0.41489 0.34659 -0.02460 -0.01097 -0.05206 330 MET   A C    
1288 O  O    . MET   A 178 ? 0.36458 0.43859 0.38886 -0.02005 -0.01491 -0.05323 330 MET   A O    
1289 C  CB   . MET   A 178 ? 0.33882 0.41029 0.32711 -0.03559 -0.01181 -0.03613 330 MET   A CB   
1290 C  CG   . MET   A 178 ? 0.38926 0.44915 0.37158 -0.04021 -0.01394 -0.02879 330 MET   A CG   
1291 S  SD   . MET   A 178 ? 0.43232 0.47756 0.40228 -0.04170 -0.01456 -0.02238 330 MET   A SD   
1292 C  CE   . MET   A 178 ? 0.38268 0.43943 0.34687 -0.04879 -0.01078 -0.01648 330 MET   A CE   
1293 N  N    . ALA   A 179 ? 0.29992 0.40144 0.31648 -0.02526 -0.00484 -0.06098 331 ALA   A N    
1294 C  CA   . ALA   A 179 ? 0.34944 0.45725 0.37543 -0.01988 -0.00235 -0.07656 331 ALA   A CA   
1295 C  C    . ALA   A 179 ? 0.38474 0.49000 0.43986 -0.01115 -0.00426 -0.08259 331 ALA   A C    
1296 O  O    . ALA   A 179 ? 0.39547 0.49069 0.46367 -0.00602 -0.00678 -0.09090 331 ALA   A O    
1297 C  CB   . ALA   A 179 ? 0.30330 0.43599 0.32114 -0.02346 0.00608  -0.08610 331 ALA   A CB   
1298 N  N    . ILE   A 180 ? 0.31418 0.42873 0.38266 -0.00973 -0.00398 -0.07755 332 ILE   A N    
1299 C  CA   . ILE   A 180 ? 0.29610 0.40990 0.39618 -0.00055 -0.00737 -0.07924 332 ILE   A CA   
1300 C  C    . ILE   A 180 ? 0.32148 0.41400 0.42642 0.00099  -0.01679 -0.06658 332 ILE   A C    
1301 O  O    . ILE   A 180 ? 0.37173 0.45500 0.50143 0.00820  -0.02050 -0.06883 332 ILE   A O    
1302 C  CB   . ILE   A 180 ? 0.30060 0.43346 0.41319 -0.00059 -0.00647 -0.07377 332 ILE   A CB   
1303 C  CG1  . ILE   A 180 ? 0.31110 0.46971 0.42555 -0.00131 0.00443  -0.08762 332 ILE   A CG1  
1304 C  CG2  . ILE   A 180 ? 0.34130 0.47309 0.48748 0.00890  -0.01320 -0.06877 332 ILE   A CG2  
1305 C  CD1  . ILE   A 180 ? 0.27051 0.45056 0.38920 -0.00652 0.00627  -0.07994 332 ILE   A CD1  
1306 N  N    . CYS   A 181 ? 0.35222 0.43765 0.43561 -0.00610 -0.02039 -0.05310 333 CYS   A N    
1307 C  CA   . CYS   A 181 ? 0.34410 0.41470 0.42737 -0.00649 -0.02754 -0.04106 333 CYS   A CA   
1308 C  C    . CYS   A 181 ? 0.39866 0.45524 0.48696 -0.00424 -0.02823 -0.04723 333 CYS   A C    
1309 O  O    . CYS   A 181 ? 0.37921 0.42586 0.48564 -0.00139 -0.03378 -0.04040 333 CYS   A O    
1310 C  CB   . CYS   A 181 ? 0.31069 0.37871 0.36757 -0.01445 -0.02821 -0.03224 333 CYS   A CB   
1311 S  SG   . CYS   A 181 ? 0.36360 0.42106 0.41535 -0.01652 -0.03413 -0.01912 333 CYS   A SG   
1312 N  N    . ILE   A 182 ? 0.36550 0.42267 0.43883 -0.00670 -0.02347 -0.05874 334 ILE   A N    
1313 C  CA   . ILE   A 182 ? 0.31109 0.35781 0.38726 -0.00667 -0.02502 -0.06583 334 ILE   A CA   
1314 C  C    . ILE   A 182 ? 0.36157 0.40471 0.46762 -0.00006 -0.02529 -0.07940 334 ILE   A C    
1315 O  O    . ILE   A 182 ? 0.35384 0.38230 0.47783 0.00101  -0.03034 -0.07763 334 ILE   A O    
1316 C  CB   . ILE   A 182 ? 0.38427 0.43772 0.43646 -0.01150 -0.02123 -0.07365 334 ILE   A CB   
1317 C  CG1  . ILE   A 182 ? 0.35780 0.40892 0.38783 -0.01650 -0.02215 -0.05949 334 ILE   A CG1  
1318 C  CG2  . ILE   A 182 ? 0.39561 0.44371 0.45232 -0.01229 -0.02338 -0.08462 334 ILE   A CG2  
1319 C  CD1  . ILE   A 182 ? 0.37099 0.43082 0.37988 -0.02081 -0.01913 -0.06151 334 ILE   A CD1  
1320 N  N    . VAL   A 183 ? 0.35142 0.40822 0.46617 0.00431  -0.01946 -0.09355 335 VAL   A N    
1321 C  CA   . VAL   A 183 ? 0.35970 0.41415 0.50537 0.01194  -0.01798 -0.11212 335 VAL   A CA   
1322 C  C    . VAL   A 183 ? 0.38922 0.44014 0.56854 0.02046  -0.02192 -0.10266 335 VAL   A C    
1323 O  O    . VAL   A 183 ? 0.44856 0.51467 0.64390 0.02698  -0.01712 -0.11140 335 VAL   A O    
1324 C  CB   . VAL   A 183 ? 0.44227 0.51855 0.58081 0.01261  -0.00805 -0.13582 335 VAL   A CB   
1325 C  CG1  . VAL   A 183 ? 0.45164 0.52437 0.62062 0.01990  -0.00566 -0.16183 335 VAL   A CG1  
1326 C  CG2  . VAL   A 183 ? 0.43612 0.52142 0.53718 0.00285  -0.00578 -0.13725 335 VAL   A CG2  
1327 N  N    . SER   A 184 ? 0.43985 0.47400 0.63142 0.02022  -0.03087 -0.08329 336 SER   A N    
1328 C  CA   . SER   A 184 ? 0.42470 0.45661 0.64900 0.02763  -0.03714 -0.06897 336 SER   A CA   
1329 C  C    . SER   A 184 ? 0.44073 0.45093 0.70424 0.03347  -0.04244 -0.07183 336 SER   A C    
1330 O  O    . SER   A 184 ? 0.43902 0.43263 0.69892 0.02721  -0.04658 -0.06611 336 SER   A O    
1331 C  CB   . SER   A 184 ? 0.44953 0.48381 0.65782 0.02150  -0.04422 -0.04052 336 SER   A CB   
1332 O  OG   . SER   A 184 ? 0.42873 0.47878 0.60318 0.01517  -0.03968 -0.03993 336 SER   A OG   
1333 N  N    . PRO   A 185 ? 0.35794 0.36748 0.66269 0.04530  -0.04249 -0.08066 337 PRO   A N    
1334 C  CA   . PRO   A 185 ? 0.39923 0.38399 0.74704 0.05136  -0.04705 -0.08750 337 PRO   A CA   
1335 C  C    . PRO   A 185 ? 0.50588 0.47325 0.87726 0.05044  -0.05981 -0.05470 337 PRO   A C    
1336 O  O    . PRO   A 185 ? 0.59484 0.53744 1.00025 0.05215  -0.06471 -0.05633 337 PRO   A O    
1337 C  CB   . PRO   A 185 ? 0.46142 0.45459 0.84769 0.06607  -0.04167 -0.10888 337 PRO   A CB   
1338 C  CG   . PRO   A 185 ? 0.42776 0.44898 0.80077 0.06791  -0.03981 -0.09662 337 PRO   A CG   
1339 C  CD   . PRO   A 185 ? 0.35063 0.38308 0.66692 0.05377  -0.03687 -0.08935 337 PRO   A CD   
1340 N  N    . ASP   A 186 ? 0.47566 0.45620 0.83065 0.04656  -0.06558 -0.02513 338 ASP   A N    
1341 C  CA   . ASP   A 186 ? 0.50813 0.47920 0.88336 0.04465  -0.07789 0.00908  338 ASP   A CA   
1342 C  C    . ASP   A 186 ? 0.47286 0.43890 0.81691 0.03017  -0.08030 0.02575  338 ASP   A C    
1343 O  O    . ASP   A 186 ? 0.49441 0.46072 0.84464 0.02542  -0.08936 0.05728  338 ASP   A O    
1344 C  CB   . ASP   A 186 ? 0.43314 0.42695 0.81146 0.04833  -0.08411 0.03235  338 ASP   A CB   
1345 C  CG   . ASP   A 186 ? 0.49206 0.51023 0.81898 0.03907  -0.07971 0.03429  338 ASP   A CG   
1346 O  OD1  . ASP   A 186 ? 0.56346 0.59805 0.88001 0.03457  -0.08719 0.05968  338 ASP   A OD1  
1347 O  OD2  . ASP   A 186 ? 0.47324 0.49469 0.77109 0.03574  -0.06932 0.01060  338 ASP   A OD2  
1348 N  N    . ARG   A 187 ? 0.47524 0.44003 0.78734 0.02304  -0.07251 0.00648  339 ARG   A N    
1349 C  CA   . ARG   A 187 ? 0.46128 0.42318 0.74919 0.01060  -0.07397 0.02017  339 ARG   A CA   
1350 C  C    . ARG   A 187 ? 0.49561 0.43367 0.81917 0.00771  -0.08068 0.02936  339 ARG   A C    
1351 O  O    . ARG   A 187 ? 0.44096 0.36036 0.79794 0.01367  -0.08062 0.00985  339 ARG   A O    
1352 C  CB   . ARG   A 187 ? 0.45490 0.42202 0.70601 0.00511  -0.06517 -0.00221 339 ARG   A CB   
1353 C  CG   . ARG   A 187 ? 0.47175 0.45885 0.69172 0.00707  -0.05829 -0.01238 339 ARG   A CG   
1354 C  CD   . ARG   A 187 ? 0.43376 0.43609 0.62608 0.00121  -0.05990 0.00885  339 ARG   A CD   
1355 N  NE   . ARG   A 187 ? 0.37468 0.39093 0.53436 -0.00041 -0.05296 -0.00254 339 ARG   A NE   
1356 C  CZ   . ARG   A 187 ? 0.35659 0.38591 0.49109 -0.00537 -0.05280 0.00822  339 ARG   A CZ   
1357 N  NH1  . ARG   A 187 ? 0.37109 0.40593 0.50513 -0.00945 -0.05864 0.02967  339 ARG   A NH1  
1358 N  NH2  . ARG   A 187 ? 0.36379 0.40156 0.47402 -0.00715 -0.04686 -0.00261 339 ARG   A NH2  
1359 N  N    . PRO   A 188 ? 0.62498 0.56416 0.94395 -0.00212 -0.08616 0.05804  340 PRO   A N    
1360 C  CA   . PRO   A 188 ? 0.65740 0.57405 1.01270 -0.00719 -0.09295 0.07041  340 PRO   A CA   
1361 C  C    . PRO   A 188 ? 0.59149 0.49438 0.94550 -0.01276 -0.08844 0.04399  340 PRO   A C    
1362 O  O    . PRO   A 188 ? 0.55029 0.46654 0.86637 -0.01866 -0.08202 0.03270  340 PRO   A O    
1363 C  CB   . PRO   A 188 ? 0.69012 0.62161 1.02952 -0.01872 -0.09736 0.10731  340 PRO   A CB   
1364 C  CG   . PRO   A 188 ? 0.69494 0.65309 0.98227 -0.02153 -0.08971 0.10144  340 PRO   A CG   
1365 C  CD   . PRO   A 188 ? 0.69078 0.65368 0.97280 -0.00988 -0.08600 0.08002  340 PRO   A CD   
1366 N  N    . GLY   A 189 ? 0.61068 0.48694 1.00917 -0.01083 -0.09267 0.03382  341 GLY   A N    
1367 C  CA   . GLY   A 189 ? 0.61209 0.47548 1.01464 -0.01716 -0.09022 0.00675  341 GLY   A CA   
1368 C  C    . GLY   A 189 ? 0.57348 0.43578 0.97474 -0.00855 -0.08345 -0.03575 341 GLY   A C    
1369 O  O    . GLY   A 189 ? 0.56129 0.41681 0.96341 -0.01449 -0.08192 -0.06131 341 GLY   A O    
1370 N  N    . VAL   A 190 ? 0.52181 0.39440 0.92069 0.00417  -0.07932 -0.04425 342 VAL   A N    
1371 C  CA   . VAL   A 190 ? 0.50031 0.37787 0.89702 0.01190  -0.07129 -0.08423 342 VAL   A CA   
1372 C  C    . VAL   A 190 ? 0.53388 0.38450 0.98403 0.01742  -0.07391 -0.10693 342 VAL   A C    
1373 O  O    . VAL   A 190 ? 0.57222 0.40363 1.06850 0.02457  -0.08066 -0.09103 342 VAL   A O    
1374 C  CB   . VAL   A 190 ? 0.49902 0.39794 0.88223 0.02300  -0.06570 -0.08476 342 VAL   A CB   
1375 C  CG1  . VAL   A 190 ? 0.52136 0.42749 0.91069 0.03155  -0.05669 -0.12499 342 VAL   A CG1  
1376 C  CG2  . VAL   A 190 ? 0.50607 0.42949 0.83579 0.01629  -0.06210 -0.07064 342 VAL   A CG2  
1377 N  N    A GLN   A 191 ? 0.56183 0.41162 1.00773 0.01411  -0.06910 -0.14472 343 GLN   A N    
1378 N  N    B GLN   A 191 ? 0.56131 0.41095 1.00675 0.01367  -0.06926 -0.14419 343 GLN   A N    
1379 C  CA   A GLN   A 191 ? 0.59239 0.41710 1.08868 0.01894  -0.07040 -0.17428 343 GLN   A CA   
1380 C  CA   B GLN   A 191 ? 0.59256 0.41800 1.08709 0.01851  -0.07019 -0.17516 343 GLN   A CA   
1381 C  C    A GLN   A 191 ? 0.61606 0.45059 1.12797 0.03536  -0.06163 -0.20430 343 GLN   A C    
1382 C  C    B GLN   A 191 ? 0.61366 0.44904 1.12388 0.03526  -0.06167 -0.20262 343 GLN   A C    
1383 O  O    A GLN   A 191 ? 0.62700 0.44477 1.18895 0.04801  -0.06422 -0.20214 343 GLN   A O    
1384 O  O    B GLN   A 191 ? 0.62402 0.44297 1.18318 0.04815  -0.06461 -0.19752 343 GLN   A O    
1385 C  CB   A GLN   A 191 ? 0.60008 0.42162 1.08632 0.00571  -0.07032 -0.20325 343 GLN   A CB   
1386 C  CB   B GLN   A 191 ? 0.59685 0.42226 1.07755 0.00586  -0.06910 -0.20645 343 GLN   A CB   
1387 C  CG   A GLN   A 191 ? 0.61712 0.41828 1.14849 0.00657  -0.07267 -0.22248 343 GLN   A CG   
1388 C  CG   B GLN   A 191 ? 0.58406 0.38526 1.08639 -0.00845 -0.07921 -0.19155 343 GLN   A CG   
1389 C  CD   A GLN   A 191 ? 0.65052 0.47049 1.17547 0.01239  -0.06248 -0.26835 343 GLN   A CD   
1390 C  CD   B GLN   A 191 ? 0.55484 0.37247 1.01989 -0.02401 -0.07891 -0.20566 343 GLN   A CD   
1391 O  OE1  A GLN   A 191 ? 0.64829 0.48843 1.13665 0.00348  -0.05840 -0.29184 343 GLN   A OE1  
1392 O  OE1  B GLN   A 191 ? 0.51863 0.35564 0.95968 -0.02424 -0.07270 -0.24071 343 GLN   A OE1  
1393 N  NE2  A GLN   A 191 ? 0.63788 0.45497 1.19839 0.02682  -0.05853 -0.27969 343 GLN   A NE2  
1394 N  NE2  B GLN   A 191 ? 0.50880 0.32309 0.96892 -0.03726 -0.08561 -0.17677 343 GLN   A NE2  
1395 N  N    . ASP   A 192 ? 0.60233 0.46726 1.07279 0.03512  -0.05108 -0.23028 344 ASP   A N    
1396 C  CA   . ASP   A 192 ? 0.59012 0.47198 1.07136 0.04899  -0.04046 -0.26102 344 ASP   A CA   
1397 C  C    . ASP   A 192 ? 0.60864 0.51500 1.06886 0.05622  -0.03685 -0.23624 344 ASP   A C    
1398 O  O    . ASP   A 192 ? 0.57745 0.51538 0.99541 0.05417  -0.02798 -0.24438 344 ASP   A O    
1399 C  CB   . ASP   A 192 ? 0.59580 0.50085 1.04519 0.04271  -0.03096 -0.30318 344 ASP   A CB   
1400 C  CG   . ASP   A 192 ? 0.66251 0.58957 1.12612 0.05376  -0.01937 -0.33439 344 ASP   A CG   
1401 O  OD1  . ASP   A 192 ? 0.65226 0.60352 1.09093 0.04742  -0.01186 -0.36443 344 ASP   A OD1  
1402 O  OD2  . ASP   A 192 ? 0.66771 0.59122 1.16709 0.06803  -0.01815 -0.32686 344 ASP   A OD2  
1403 N  N    . ALA   A 193 ? 0.59152 0.48349 1.08400 0.06372  -0.04490 -0.20399 345 ALA   A N    
1404 C  CA   . ALA   A 193 ? 0.59950 0.51439 1.07690 0.06955  -0.04375 -0.17928 345 ALA   A CA   
1405 C  C    . ALA   A 193 ? 0.60378 0.54428 1.08893 0.08198  -0.03187 -0.20744 345 ALA   A C    
1406 O  O    . ALA   A 193 ? 0.56146 0.53028 1.01845 0.08233  -0.02719 -0.19709 345 ALA   A O    
1407 C  CB   . ALA   A 193 ? 0.60347 0.50105 1.11886 0.07527  -0.05609 -0.14079 345 ALA   A CB   
1408 N  N    . LYS   A 194 ? 0.65639 0.58872 1.18092 0.09161  -0.02633 -0.24449 346 LYS   A N    
1409 C  CA   . LYS   A 194 ? 0.63484 0.59563 1.17024 0.10392  -0.01310 -0.27457 346 LYS   A CA   
1410 C  C    . LYS   A 194 ? 0.58972 0.58594 1.06596 0.09338  -0.00087 -0.29476 346 LYS   A C    
1411 O  O    . LYS   A 194 ? 0.56871 0.59885 1.03083 0.09737  0.00880  -0.29875 346 LYS   A O    
1412 C  CB   . LYS   A 194 ? 0.73660 0.68672 1.31533 0.11050  -0.01040 -0.30288 346 LYS   A CB   
1413 C  CG   . LYS   A 194 ? 0.78306 0.70649 1.42101 0.12056  -0.02132 -0.28015 346 LYS   A CG   
1414 C  CD   . LYS   A 194 ? 0.82210 0.71071 1.47044 0.11331  -0.03736 -0.24245 346 LYS   A CD   
1415 C  CE   . LYS   A 194 ? 0.84742 0.71526 1.48745 0.09930  -0.03986 -0.25720 346 LYS   A CE   
1416 N  NZ   . LYS   A 194 ? 0.81343 0.65601 1.44817 0.08839  -0.05292 -0.22063 346 LYS   A NZ   
1417 N  N    . LEU   A 195 ? 0.56617 0.55684 1.00906 0.07915  -0.00186 -0.30547 347 LEU   A N    
1418 C  CA   . LEU   A 195 ? 0.55263 0.57720 0.93905 0.06806  0.00746  -0.31926 347 LEU   A CA   
1419 C  C    . LEU   A 195 ? 0.47261 0.51099 0.81445 0.05970  0.00470  -0.28135 347 LEU   A C    
1420 O  O    . LEU   A 195 ? 0.51884 0.59017 0.82690 0.05609  0.01372  -0.28435 347 LEU   A O    
1421 C  CB   . LEU   A 195 ? 0.57322 0.58938 0.94087 0.05546  0.00500  -0.34010 347 LEU   A CB   
1422 C  CG   . LEU   A 195 ? 0.56052 0.61179 0.87051 0.04262  0.01195  -0.35229 347 LEU   A CG   
1423 C  CD1  . LEU   A 195 ? 0.54120 0.63150 0.84609 0.04849  0.02760  -0.38232 347 LEU   A CD1  
1424 C  CD2  . LEU   A 195 ? 0.59816 0.64060 0.89794 0.03076  0.00679  -0.37267 347 LEU   A CD2  
1425 N  N    . VAL   A 196 ? 0.44640 0.46089 0.78837 0.05572  -0.00736 -0.24608 348 VAL   A N    
1426 C  CA   . VAL   A 196 ? 0.38926 0.41486 0.69295 0.04844  -0.00999 -0.21303 348 VAL   A CA   
1427 C  C    . VAL   A 196 ? 0.37891 0.42598 0.69043 0.05669  -0.00528 -0.20435 348 VAL   A C    
1428 O  O    . VAL   A 196 ? 0.41575 0.48577 0.69197 0.05054  -0.00071 -0.19518 348 VAL   A O    
1429 C  CB   . VAL   A 196 ? 0.38110 0.38027 0.68797 0.04335  -0.02275 -0.18009 348 VAL   A CB   
1430 C  CG1  . VAL   A 196 ? 0.41613 0.42752 0.68437 0.03614  -0.02451 -0.15104 348 VAL   A CG1  
1431 C  CG2  . VAL   A 196 ? 0.39503 0.37610 0.69718 0.03408  -0.02718 -0.18877 348 VAL   A CG2  
1432 N  N    . GLU   A 197 ? 0.39035 0.43060 0.75156 0.07052  -0.00692 -0.20657 349 GLU   A N    
1433 C  CA   . GLU   A 197 ? 0.40102 0.46491 0.77555 0.07889  -0.00338 -0.19855 349 GLU   A CA   
1434 C  C    . GLU   A 197 ? 0.44293 0.54263 0.80288 0.07957  0.01221  -0.22686 349 GLU   A C    
1435 O  O    . GLU   A 197 ? 0.41160 0.53821 0.75296 0.07655  0.01670  -0.21608 349 GLU   A O    
1436 C  CB   . GLU   A 197 ? 0.47958 0.52940 0.91649 0.09506  -0.00942 -0.19491 349 GLU   A CB   
1437 C  CG   . GLU   A 197 ? 0.53496 0.60959 0.99012 0.10356  -0.00944 -0.17980 349 GLU   A CG   
1438 C  CD   . GLU   A 197 ? 0.67846 0.73692 1.19415 0.11837  -0.02028 -0.16414 349 GLU   A CD   
1439 O  OE1  . GLU   A 197 ? 0.73849 0.77277 1.29640 0.12787  -0.02125 -0.18135 349 GLU   A OE1  
1440 O  OE2  . GLU   A 197 ? 0.69903 0.76937 1.22168 0.12009  -0.02860 -0.13434 349 GLU   A OE2  
1441 N  N    . ALA   A 198 ? 0.47747 0.58014 0.84560 0.08217  0.02076  -0.26367 350 ALA   A N    
1442 C  CA   . ALA   A 198 ? 0.49550 0.63779 0.84774 0.08158  0.03677  -0.29170 350 ALA   A CA   
1443 C  C    . ALA   A 198 ? 0.49311 0.65629 0.78460 0.06472  0.03985  -0.27876 350 ALA   A C    
1444 O  O    . ALA   A 198 ? 0.45916 0.65761 0.73447 0.06188  0.04991  -0.27997 350 ALA   A O    
1445 C  CB   . ALA   A 198 ? 0.53347 0.67567 0.90211 0.08566  0.04458  -0.33582 350 ALA   A CB   
1446 N  N    . ILE   A 199 ? 0.47198 0.61446 0.73247 0.05335  0.03117  -0.26500 351 ILE   A N    
1447 C  CA   . ILE   A 199 ? 0.46860 0.62708 0.67651 0.03866  0.03246  -0.25025 351 ILE   A CA   
1448 C  C    . ILE   A 199 ? 0.42841 0.59050 0.62683 0.03611  0.02906  -0.21764 351 ILE   A C    
1449 O  O    . ILE   A 199 ? 0.42196 0.60999 0.59386 0.02849  0.03559  -0.21134 351 ILE   A O    
1450 C  CB   . ILE   A 199 ? 0.46076 0.59690 0.64470 0.02902  0.02348  -0.24436 351 ILE   A CB   
1451 C  CG1  . ILE   A 199 ? 0.52740 0.66865 0.71343 0.02782  0.02754  -0.28001 351 ILE   A CG1  
1452 C  CG2  . ILE   A 199 ? 0.46688 0.61385 0.60394 0.01617  0.02223  -0.22215 351 ILE   A CG2  
1453 C  CD1  . ILE   A 199 ? 0.54807 0.65878 0.73674 0.02304  0.01639  -0.27862 351 ILE   A CD1  
1454 N  N    . GLN   A 200 ? 0.44286 0.58031 0.66303 0.04114  0.01839  -0.19616 352 GLN   A N    
1455 C  CA   . GLN   A 200 ? 0.41813 0.56073 0.63037 0.03804  0.01426  -0.16823 352 GLN   A CA   
1456 C  C    . GLN   A 200 ? 0.40569 0.57952 0.63600 0.04344  0.02268  -0.17413 352 GLN   A C    
1457 O  O    . GLN   A 200 ? 0.42440 0.61537 0.63603 0.03576  0.02431  -0.15947 352 GLN   A O    
1458 C  CB   . GLN   A 200 ? 0.43852 0.55467 0.67157 0.04219  0.00114  -0.14563 352 GLN   A CB   
1459 C  CG   . GLN   A 200 ? 0.44387 0.56350 0.65856 0.03525  -0.00487 -0.11763 352 GLN   A CG   
1460 C  CD   . GLN   A 200 ? 0.42317 0.52571 0.65933 0.03924  -0.01735 -0.09538 352 GLN   A CD   
1461 O  OE1  . GLN   A 200 ? 0.39727 0.48809 0.61165 0.03142  -0.02422 -0.07658 352 GLN   A OE1  
1462 N  NE2  . GLN   A 200 ? 0.45478 0.55825 0.73504 0.05157  -0.02022 -0.09682 352 GLN   A NE2  
1463 N  N    . ASP   A 201 ? 0.41978 0.60171 0.68982 0.05660  0.02822  -0.19634 353 ASP   A N    
1464 C  CA   . ASP   A 201 ? 0.46420 0.67973 0.75759 0.06329  0.03701  -0.20331 353 ASP   A CA   
1465 C  C    . ASP   A 201 ? 0.47672 0.72806 0.73651 0.05239  0.05058  -0.21305 353 ASP   A C    
1466 O  O    . ASP   A 201 ? 0.47472 0.75280 0.73353 0.04851  0.05476  -0.20261 353 ASP   A O    
1467 C  CB   . ASP   A 201 ? 0.47517 0.69208 0.82082 0.08108  0.04162  -0.22950 353 ASP   A CB   
1468 C  CG   . ASP   A 201 ? 0.47490 0.66532 0.86470 0.09312  0.02780  -0.21184 353 ASP   A CG   
1469 O  OD1  . ASP   A 201 ? 0.48193 0.65979 0.85891 0.08688  0.01557  -0.17955 353 ASP   A OD1  
1470 O  OD2  . ASP   A 201 ? 0.52402 0.70722 0.96235 0.10866  0.02908  -0.23025 353 ASP   A OD2  
1471 N  N    . ARG   A 202 ? 0.42407 0.67874 0.65686 0.04613  0.05698  -0.23174 354 ARG   A N    
1472 C  CA   . ARG   A 202 ? 0.46995 0.75916 0.66592 0.03331  0.06820  -0.23518 354 ARG   A CA   
1473 C  C    . ARG   A 202 ? 0.42511 0.71014 0.58919 0.01943  0.06192  -0.20193 354 ARG   A C    
1474 O  O    . ARG   A 202 ? 0.43515 0.75018 0.58573 0.01052  0.06963  -0.19477 354 ARG   A O    
1475 C  CB   . ARG   A 202 ? 0.54482 0.83619 0.71393 0.02753  0.07213  -0.25623 354 ARG   A CB   
1476 C  CG   . ARG   A 202 ? 0.58882 0.92483 0.72553 0.01599  0.08560  -0.26512 354 ARG   A CG   
1477 C  CD   . ARG   A 202 ? 0.66923 1.02132 0.79868 0.01651  0.09341  -0.30115 354 ARG   A CD   
1478 N  NE   . ARG   A 202 ? 0.80870 1.12236 0.93795 0.01815  0.08158  -0.30666 354 ARG   A NE   
1479 C  CZ   . ARG   A 202 ? 0.87040 1.18030 0.96224 0.00625  0.07588  -0.30200 354 ARG   A CZ   
1480 N  NH1  . ARG   A 202 ? 0.81030 1.08706 0.90757 0.00774  0.06520  -0.30746 354 ARG   A NH1  
1481 N  NH2  . ARG   A 202 ? 0.92389 1.26454 0.97510 -0.00766 0.08024  -0.28991 354 ARG   A NH2  
1482 N  N    . LEU   A 203 ? 0.35228 0.60082 0.50637 0.01706  0.04836  -0.18201 355 LEU   A N    
1483 C  CA   . LEU   A 203 ? 0.34571 0.58688 0.47300 0.00505  0.04232  -0.15408 355 LEU   A CA   
1484 C  C    . LEU   A 203 ? 0.34762 0.59563 0.49585 0.00659  0.03915  -0.13909 355 LEU   A C    
1485 O  O    . LEU   A 203 ? 0.36797 0.62970 0.50133 -0.00432 0.04092  -0.12524 355 LEU   A O    
1486 C  CB   . LEU   A 203 ? 0.34129 0.54568 0.45270 0.00270  0.03041  -0.14107 355 LEU   A CB   
1487 C  CG   . LEU   A 203 ? 0.34136 0.53798 0.43270 -0.00009 0.03060  -0.15294 355 LEU   A CG   
1488 C  CD1  . LEU   A 203 ? 0.33546 0.49731 0.42373 0.00037  0.01880  -0.14098 355 LEU   A CD1  
1489 C  CD2  . LEU   A 203 ? 0.42542 0.64165 0.48085 -0.01274 0.03583  -0.14764 355 LEU   A CD2  
1490 N  N    . SER   A 204 ? 0.33263 0.57153 0.51707 0.01926  0.03332  -0.14038 356 SER   A N    
1491 C  CA   . SER   A 204 ? 0.41500 0.66367 0.62056 0.02068  0.02802  -0.12501 356 SER   A CA   
1492 C  C    . SER   A 204 ? 0.41655 0.70657 0.63538 0.01938  0.03957  -0.13286 356 SER   A C    
1493 O  O    . SER   A 204 ? 0.36379 0.66842 0.57926 0.01034  0.03788  -0.11789 356 SER   A O    
1494 C  CB   . SER   A 204 ? 0.39618 0.62973 0.64077 0.03529  0.01859  -0.12272 356 SER   A CB   
1495 O  OG   . SER   A 204 ? 0.42149 0.62007 0.65377 0.03430  0.00817  -0.11226 356 SER   A OG   
1496 N  N    . ASN   A 205 ? 0.44803 0.75945 0.68288 0.02747  0.05192  -0.15781 357 ASN   A N    
1497 C  CA   . ASN   A 205 ? 0.43556 0.79224 0.68283 0.02576  0.06531  -0.16682 357 ASN   A CA   
1498 C  C    . ASN   A 205 ? 0.43234 0.80588 0.63884 0.00626  0.07196  -0.15682 357 ASN   A C    
1499 O  O    . ASN   A 205 ? 0.45088 0.85540 0.66250 -0.00180 0.07761  -0.14913 357 ASN   A O    
1500 C  CB   . ASN   A 205 ? 0.45884 0.83621 0.73072 0.03892  0.07855  -0.19970 357 ASN   A CB   
1501 C  CG   . ASN   A 205 ? 0.51340 0.87908 0.83809 0.05948  0.07294  -0.20846 357 ASN   A CG   
1502 O  OD1  . ASN   A 205 ? 0.56058 0.92021 0.90579 0.07179  0.07796  -0.23447 357 ASN   A OD1  
1503 N  ND2  . ASN   A 205 ? 0.53051 0.89339 0.87908 0.06286  0.06171  -0.18653 357 ASN   A ND2  
1504 N  N    . THR   A 206 ? 0.43277 0.78710 0.60145 -0.00195 0.07069  -0.15508 358 THR   A N    
1505 C  CA   . THR   A 206 ? 0.44499 0.81012 0.57697 -0.02032 0.07434  -0.14030 358 THR   A CA   
1506 C  C    . THR   A 206 ? 0.42926 0.78028 0.55706 -0.03050 0.06457  -0.11393 358 THR   A C    
1507 O  O    . THR   A 206 ? 0.39012 0.76305 0.51116 -0.04395 0.06945  -0.10234 358 THR   A O    
1508 C  CB   . THR   A 206 ? 0.41237 0.75714 0.50926 -0.02510 0.07174  -0.14114 358 THR   A CB   
1509 O  OG1  . THR   A 206 ? 0.43997 0.79944 0.54079 -0.01694 0.08021  -0.16915 358 THR   A OG1  
1510 C  CG2  . THR   A 206 ? 0.42177 0.77889 0.48462 -0.04323 0.07483  -0.12316 358 THR   A CG2  
1511 N  N    . LEU   A 207 ? 0.32433 0.64000 0.45635 -0.02544 0.05084  -0.10475 359 LEU   A N    
1512 C  CA   . LEU   A 207 ? 0.28413 0.58720 0.41214 -0.03490 0.04126  -0.08422 359 LEU   A CA   
1513 C  C    . LEU   A 207 ? 0.29740 0.63005 0.45555 -0.03529 0.04239  -0.08185 359 LEU   A C    
1514 O  O    . LEU   A 207 ? 0.32278 0.66697 0.47601 -0.04955 0.04246  -0.06971 359 LEU   A O    
1515 C  CB   . LEU   A 207 ? 0.30344 0.56908 0.42913 -0.02892 0.02764  -0.07743 359 LEU   A CB   
1516 C  CG   . LEU   A 207 ? 0.33322 0.58715 0.45590 -0.03720 0.01703  -0.06082 359 LEU   A CG   
1517 C  CD1  . LEU   A 207 ? 0.29281 0.54192 0.38998 -0.05388 0.01876  -0.05053 359 LEU   A CD1  
1518 C  CD2  . LEU   A 207 ? 0.33728 0.56056 0.45607 -0.03088 0.00563  -0.05580 359 LEU   A CD2  
1519 N  N    . GLN   A 208 ? 0.30766 0.65292 0.50065 -0.01980 0.04261  -0.09299 360 GLN   A N    
1520 C  CA   . GLN   A 208 ? 0.28120 0.65791 0.50798 -0.01830 0.04243  -0.09016 360 GLN   A CA   
1521 C  C    . GLN   A 208 ? 0.33667 0.75473 0.56434 -0.02901 0.05684  -0.09356 360 GLN   A C    
1522 O  O    . GLN   A 208 ? 0.35031 0.78942 0.58850 -0.03963 0.05527  -0.08251 360 GLN   A O    
1523 C  CB   . GLN   A 208 ? 0.39684 0.78035 0.66559 0.00263  0.04106  -0.10207 360 GLN   A CB   
1524 C  CG   . GLN   A 208 ? 0.43428 0.78297 0.70931 0.01140  0.02499  -0.09214 360 GLN   A CG   
1525 C  CD   . GLN   A 208 ? 0.56709 0.91959 0.88832 0.03225  0.02294  -0.10125 360 GLN   A CD   
1526 O  OE1  . GLN   A 208 ? 0.66152 0.99371 0.98763 0.04292  0.02511  -0.11449 360 GLN   A OE1  
1527 N  NE2  . GLN   A 208 ? 0.57174 0.95015 0.93027 0.03804  0.01788  -0.09390 360 GLN   A NE2  
1528 N  N    . THR   A 209 ? 0.35539 0.78839 0.57155 -0.02794 0.07090  -0.10861 361 THR   A N    
1529 C  CA   . THR   A 209 ? 0.36319 0.84011 0.57694 -0.03983 0.08591  -0.11011 361 THR   A CA   
1530 C  C    . THR   A 209 ? 0.37335 0.84120 0.55360 -0.06240 0.08366  -0.08821 361 THR   A C    
1531 O  O    . THR   A 209 ? 0.40200 0.90027 0.58805 -0.07664 0.08958  -0.07846 361 THR   A O    
1532 C  CB   . THR   A 209 ? 0.45175 0.95131 0.65979 -0.03306 0.10162  -0.13368 361 THR   A CB   
1533 O  OG1  . THR   A 209 ? 0.44942 0.95780 0.69685 -0.01154 0.10448  -0.15625 361 THR   A OG1  
1534 C  CG2  . THR   A 209 ? 0.45737 1.00763 0.65860 -0.04734 0.11829  -0.13332 361 THR   A CG2  
1535 N  N    . TYR   A 210 ? 0.37700 0.80316 0.52564 -0.06604 0.07498  -0.07966 362 TYR   A N    
1536 C  CA   . TYR   A 210 ? 0.31930 0.73218 0.44131 -0.08563 0.07192  -0.05874 362 TYR   A CA   
1537 C  C    . TYR   A 210 ? 0.33836 0.74732 0.47527 -0.09585 0.06304  -0.04468 362 TYR   A C    
1538 O  O    . TYR   A 210 ? 0.38680 0.80807 0.52001 -0.11406 0.06587  -0.03073 362 TYR   A O    
1539 C  CB   . TYR   A 210 ? 0.36246 0.73083 0.45447 -0.08459 0.06318  -0.05341 362 TYR   A CB   
1540 C  CG   . TYR   A 210 ? 0.37242 0.72241 0.44384 -0.10250 0.05865  -0.03173 362 TYR   A CG   
1541 C  CD1  . TYR   A 210 ? 0.37303 0.69348 0.44756 -0.10755 0.04675  -0.02171 362 TYR   A CD1  
1542 C  CD2  . TYR   A 210 ? 0.38129 0.74540 0.43220 -0.11482 0.06621  -0.02130 362 TYR   A CD2  
1543 C  CE1  . TYR   A 210 ? 0.38545 0.68652 0.44675 -0.12310 0.04292  -0.00457 362 TYR   A CE1  
1544 C  CE2  . TYR   A 210 ? 0.35167 0.69651 0.38968 -0.13058 0.06130  0.00061  362 TYR   A CE2  
1545 C  CZ   . TYR   A 210 ? 0.39742 0.70869 0.44259 -0.13408 0.04988  0.00763  362 TYR   A CZ   
1546 O  OH   . TYR   A 210 ? 0.41630 0.70525 0.45362 -0.14889 0.04517  0.02685  362 TYR   A OH   
1547 N  N    . ILE   A 211 ? 0.33350 0.72600 0.48725 -0.08575 0.05150  -0.04736 363 ILE   A N    
1548 C  CA   . ILE   A 211 ? 0.29437 0.68609 0.46073 -0.09606 0.04159  -0.03650 363 ILE   A CA   
1549 C  C    . ILE   A 211 ? 0.29592 0.73587 0.49093 -0.10310 0.04924  -0.03616 363 ILE   A C    
1550 O  O    . ILE   A 211 ? 0.37288 0.82084 0.57099 -0.12134 0.04691  -0.02462 363 ILE   A O    
1551 C  CB   . ILE   A 211 ? 0.27841 0.64996 0.45547 -0.08357 0.02753  -0.03863 363 ILE   A CB   
1552 C  CG1  . ILE   A 211 ? 0.27714 0.60305 0.42483 -0.08059 0.02043  -0.03665 363 ILE   A CG1  
1553 C  CG2  . ILE   A 211 ? 0.38636 0.76734 0.57836 -0.09436 0.01703  -0.03017 363 ILE   A CG2  
1554 C  CD1  . ILE   A 211 ? 0.30069 0.60968 0.45654 -0.06624 0.00944  -0.03891 363 ILE   A CD1  
1555 N  N    . ARG   A 212 ? 0.35542 0.82872 0.57346 -0.08915 0.05931  -0.05006 364 ARG   A N    
1556 C  CA   . ARG   A 212 ? 0.36761 0.89374 0.61979 -0.09232 0.06798  -0.05236 364 ARG   A CA   
1557 C  C    . ARG   A 212 ? 0.41457 0.97266 0.65582 -0.10967 0.08386  -0.04745 364 ARG   A C    
1558 O  O    . ARG   A 212 ? 0.46237 1.06216 0.72886 -0.11941 0.08941  -0.04341 364 ARG   A O    
1559 C  CB   . ARG   A 212 ? 0.47188 1.02173 0.75797 -0.06870 0.07332  -0.07100 364 ARG   A CB   
1560 C  CG   . ARG   A 212 ? 0.64669 1.17261 0.95170 -0.05269 0.05688  -0.07067 364 ARG   A CG   
1561 C  CD   . ARG   A 212 ? 0.72811 1.29330 1.08464 -0.03923 0.05670  -0.07622 364 ARG   A CD   
1562 N  NE   . ARG   A 212 ? 0.81837 1.36928 1.19153 -0.03357 0.03705  -0.06476 364 ARG   A NE   
1563 C  CZ   . ARG   A 212 ? 0.83315 1.36889 1.22718 -0.01296 0.02875  -0.06788 364 ARG   A CZ   
1564 N  NH1  . ARG   A 212 ? 0.82552 1.35481 1.22875 0.00439  0.03861  -0.08525 364 ARG   A NH1  
1565 N  NH2  . ARG   A 212 ? 0.82434 1.35231 1.23043 -0.01078 0.01020  -0.05333 364 ARG   A NH2  
1566 N  N    A CYS   A 213 ? 0.45462 0.99105 0.65879 -0.11779 0.08751  -0.04167 365 CYS   A N    
1567 N  N    B CYS   A 213 ? 0.45816 0.99391 0.66207 -0.11780 0.08731  -0.04155 365 CYS   A N    
1568 C  CA   A CYS   A 213 ? 0.49839 1.06507 0.68924 -0.13580 0.10122  -0.03209 365 CYS   A CA   
1569 C  CA   B CYS   A 213 ? 0.49827 1.06427 0.68832 -0.13518 0.10132  -0.03262 365 CYS   A CA   
1570 C  C    A CYS   A 213 ? 0.50817 1.04394 0.67336 -0.15712 0.09426  -0.00839 365 CYS   A C    
1571 C  C    B CYS   A 213 ? 0.50599 1.04175 0.67006 -0.15663 0.09465  -0.00882 365 CYS   A C    
1572 O  O    A CYS   A 213 ? 0.52277 1.08413 0.68809 -0.17708 0.10174  0.00685  365 CYS   A O    
1573 O  O    B CYS   A 213 ? 0.53071 1.09272 0.69371 -0.17628 0.10270  0.00617  365 CYS   A O    
1574 C  CB   A CYS   A 213 ? 0.52978 1.11339 0.70208 -0.12680 0.11504  -0.04656 365 CYS   A CB   
1575 C  CB   B CYS   A 213 ? 0.52654 1.10771 0.69829 -0.12517 0.11459  -0.04788 365 CYS   A CB   
1576 S  SG   A CYS   A 213 ? 0.53730 1.17178 0.74578 -0.10585 0.12988  -0.07693 365 CYS   A SG   
1577 S  SG   B CYS   A 213 ? 0.58594 1.20758 0.73196 -0.14683 0.13143  -0.03471 365 CYS   A SG   
1578 N  N    . ARG   A 214 ? 0.45482 0.93710 0.60096 -0.15354 0.08049  -0.00448 366 ARG   A N    
1579 C  CA   . ARG   A 214 ? 0.47564 0.92498 0.59996 -0.17062 0.07437  0.01579  366 ARG   A CA   
1580 C  C    . ARG   A 214 ? 0.45933 0.86950 0.58946 -0.17633 0.05861  0.02113  366 ARG   A C    
1581 O  O    . ARG   A 214 ? 0.51901 0.90554 0.64074 -0.19281 0.05427  0.03717  366 ARG   A O    
1582 C  CB   . ARG   A 214 ? 0.43644 0.85888 0.52831 -0.16337 0.07411  0.01651  366 ARG   A CB   
1583 C  CG   . ARG   A 214 ? 0.51078 0.97219 0.59086 -0.15991 0.08900  0.00966  366 ARG   A CG   
1584 C  CD   . ARG   A 214 ? 0.61081 1.09897 0.68010 -0.18191 0.09771  0.03178  366 ARG   A CD   
1585 N  NE   . ARG   A 214 ? 0.75122 1.29413 0.81522 -0.18113 0.11477  0.02233  366 ARG   A NE   
1586 C  CZ   . ARG   A 214 ? 0.81179 1.36293 0.84758 -0.17743 0.11979  0.01853  366 ARG   A CZ   
1587 N  NH1  . ARG   A 214 ? 0.82707 1.33468 0.83984 -0.17355 0.10839  0.02543  366 ARG   A NH1  
1588 N  NH2  . ARG   A 214 ? 0.82051 1.42659 0.85169 -0.17782 0.13633  0.00648  366 ARG   A NH2  
1589 N  N    . HIS   A 215 ? 0.35206 0.75519 0.49670 -0.16384 0.04971  0.00850  367 HIS   A N    
1590 C  CA   . HIS   A 215 ? 0.33041 0.70225 0.47753 -0.17060 0.03519  0.01120  367 HIS   A CA   
1591 C  C    . HIS   A 215 ? 0.35500 0.75780 0.53105 -0.18415 0.03292  0.01350  367 HIS   A C    
1592 O  O    . HIS   A 215 ? 0.40196 0.83556 0.60095 -0.17408 0.03244  0.00469  367 HIS   A O    
1593 C  CB   . HIS   A 215 ? 0.32512 0.67290 0.46776 -0.15188 0.02514  -0.00064 367 HIS   A CB   
1594 C  CG   . HIS   A 215 ? 0.40918 0.71559 0.53891 -0.15759 0.01265  0.00113  367 HIS   A CG   
1595 N  ND1  . HIS   A 215 ? 0.40521 0.67460 0.51276 -0.14722 0.00853  -0.00180 367 HIS   A ND1  
1596 C  CD2  . HIS   A 215 ? 0.43087 0.72932 0.56793 -0.17305 0.00404  0.00327  367 HIS   A CD2  
1597 C  CE1  . HIS   A 215 ? 0.37832 0.61991 0.48008 -0.15495 -0.00099 -0.00217 367 HIS   A CE1  
1598 N  NE2  . HIS   A 215 ? 0.41745 0.67490 0.53622 -0.17080 -0.00412 -0.00024 367 HIS   A NE2  
1599 N  N    . PRO   A 216 ? 0.41435 0.81059 0.59375 -0.20690 0.03070  0.02550  368 PRO   A N    
1600 C  CA   . PRO   A 216 ? 0.43808 0.86819 0.64718 -0.22223 0.02879  0.02773  368 PRO   A CA   
1601 C  C    . PRO   A 216 ? 0.34482 0.76692 0.56425 -0.21907 0.01319  0.01752  368 PRO   A C    
1602 O  O    . PRO   A 216 ? 0.35651 0.73815 0.55702 -0.21321 0.00335  0.01198  368 PRO   A O    
1603 C  CB   . PRO   A 216 ? 0.51584 0.93075 0.72349 -0.24843 0.02954  0.04413  368 PRO   A CB   
1604 C  CG   . PRO   A 216 ? 0.53706 0.89628 0.71683 -0.24420 0.02417  0.04615  368 PRO   A CG   
1605 C  CD   . PRO   A 216 ? 0.48303 0.84067 0.64318 -0.21978 0.02940  0.03830  368 PRO   A CD   
1606 N  N    . PRO   A 217 ? 0.34002 0.80380 0.58942 -0.22293 0.01036  0.01509  369 PRO   A N    
1607 C  CA   . PRO   A 217 ? 0.33739 0.79945 0.59626 -0.22464 -0.00633 0.00811  369 PRO   A CA   
1608 C  C    . PRO   A 217 ? 0.46647 0.90190 0.72072 -0.24925 -0.01512 0.00984  369 PRO   A C    
1609 O  O    . PRO   A 217 ? 0.43462 0.86541 0.69166 -0.26773 -0.00821 0.01977  369 PRO   A O    
1610 C  CB   . PRO   A 217 ? 0.32949 0.85051 0.62626 -0.22392 -0.00554 0.00803  369 PRO   A CB   
1611 C  CG   . PRO   A 217 ? 0.35279 0.90290 0.66091 -0.23437 0.01142  0.01638  369 PRO   A CG   
1612 C  CD   . PRO   A 217 ? 0.33793 0.85751 0.61490 -0.22559 0.02254  0.01846  369 PRO   A CD   
1613 N  N    . PRO   A 218 ? 0.44317 0.86188 0.69170 -0.25122 -0.03043 0.00020  370 PRO   A N    
1614 C  CA   . PRO   A 218 ? 0.44180 0.86905 0.68788 -0.23343 -0.04093 -0.00759 370 PRO   A CA   
1615 C  C    . PRO   A 218 ? 0.41512 0.80412 0.63124 -0.21333 -0.04025 -0.01147 370 PRO   A C    
1616 O  O    . PRO   A 218 ? 0.41686 0.81205 0.63089 -0.19822 -0.04810 -0.01469 370 PRO   A O    
1617 C  CB   . PRO   A 218 ? 0.51298 0.94018 0.76189 -0.25126 -0.05700 -0.01554 370 PRO   A CB   
1618 C  CG   . PRO   A 218 ? 0.51315 0.90108 0.75099 -0.27066 -0.05464 -0.01737 370 PRO   A CG   
1619 C  CD   . PRO   A 218 ? 0.49508 0.88816 0.74188 -0.27500 -0.03897 -0.00352 370 PRO   A CD   
1620 N  N    . GLY   A 219 ? 0.38117 0.73329 0.57655 -0.21376 -0.03165 -0.00910 371 GLY   A N    
1621 C  CA   . GLY   A 219 ? 0.43756 0.75464 0.60627 -0.19653 -0.03130 -0.01279 371 GLY   A CA   
1622 C  C    . GLY   A 219 ? 0.41569 0.74873 0.58696 -0.17319 -0.02708 -0.01243 371 GLY   A C    
1623 O  O    . GLY   A 219 ? 0.39320 0.70694 0.54933 -0.15884 -0.03143 -0.01612 371 GLY   A O    
1624 N  N    . SER   A 220 ? 0.41513 0.78388 0.60765 -0.16959 -0.01823 -0.00891 372 SER   A N    
1625 C  CA   . SER   A 220 ? 0.41575 0.79959 0.61634 -0.14704 -0.01240 -0.01166 372 SER   A CA   
1626 C  C    . SER   A 220 ? 0.40110 0.80693 0.62295 -0.13495 -0.02338 -0.01316 372 SER   A C    
1627 O  O    . SER   A 220 ? 0.32540 0.73584 0.55612 -0.11543 -0.02063 -0.01565 372 SER   A O    
1628 C  CB   . SER   A 220 ? 0.37536 0.79287 0.59267 -0.14801 0.00233  -0.01028 372 SER   A CB   
1629 O  OG   . SER   A 220 ? 0.36270 0.82039 0.60958 -0.15971 0.00060  -0.00736 372 SER   A OG   
1630 N  N    . HIS   A 221 ? 0.37923 0.79756 0.60948 -0.14665 -0.03633 -0.01135 373 HIS   A N    
1631 C  CA   . HIS   A 221 ? 0.39343 0.84132 0.64784 -0.13683 -0.04804 -0.00856 373 HIS   A CA   
1632 C  C    . HIS   A 221 ? 0.34379 0.76844 0.58469 -0.11905 -0.05490 -0.00738 373 HIS   A C    
1633 O  O    . HIS   A 221 ? 0.35911 0.75445 0.57129 -0.12406 -0.06153 -0.00868 373 HIS   A O    
1634 C  CB   . HIS   A 221 ? 0.41044 0.87686 0.67095 -0.15599 -0.06216 -0.00726 373 HIS   A CB   
1635 C  CG   . HIS   A 221 ? 0.37407 0.87329 0.65706 -0.14761 -0.07713 -0.00115 373 HIS   A CG   
1636 N  ND1  . HIS   A 221 ? 0.36148 0.90117 0.68450 -0.13483 -0.07590 0.00410  373 HIS   A ND1  
1637 C  CD2  . HIS   A 221 ? 0.35101 0.85108 0.62312 -0.14992 -0.09395 0.00170  373 HIS   A CD2  
1638 C  CE1  . HIS   A 221 ? 0.29966 0.86193 0.63760 -0.12920 -0.09266 0.01239  373 HIS   A CE1  
1639 N  NE2  . HIS   A 221 ? 0.36168 0.90202 0.66710 -0.13907 -0.10399 0.01180  373 HIS   A NE2  
1640 N  N    A GLN   A 222 ? 0.27800 0.71672 0.54241 -0.09855 -0.05286 -0.00533 374 GLN   A N    
1641 N  N    B GLN   A 222 ? 0.28810 0.72667 0.55240 -0.09855 -0.05274 -0.00538 374 GLN   A N    
1642 C  CA   A GLN   A 222 ? 0.31017 0.72908 0.56934 -0.08140 -0.05939 -0.00148 374 GLN   A CA   
1643 C  CA   B GLN   A 222 ? 0.31239 0.73129 0.57160 -0.08137 -0.05932 -0.00151 374 GLN   A CA   
1644 C  C    A GLN   A 222 ? 0.31418 0.68760 0.53602 -0.08055 -0.05328 -0.00640 374 GLN   A C    
1645 C  C    B GLN   A 222 ? 0.31464 0.68801 0.53637 -0.08063 -0.05332 -0.00639 374 GLN   A C    
1646 O  O    A GLN   A 222 ? 0.31190 0.66469 0.51883 -0.07458 -0.06080 -0.00232 374 GLN   A O    
1647 O  O    B GLN   A 222 ? 0.31391 0.66664 0.52054 -0.07481 -0.06087 -0.00232 374 GLN   A O    
1648 C  CB   A GLN   A 222 ? 0.35308 0.78463 0.61410 -0.08455 -0.07850 0.00892  374 GLN   A CB   
1649 C  CB   B GLN   A 222 ? 0.35630 0.78829 0.61788 -0.08441 -0.07842 0.00892  374 GLN   A CB   
1650 C  CG   A GLN   A 222 ? 0.41006 0.88776 0.71419 -0.07872 -0.08775 0.01786  374 GLN   A CG   
1651 C  CG   B GLN   A 222 ? 0.41335 0.88929 0.71908 -0.07575 -0.08740 0.01832  374 GLN   A CG   
1652 C  CD   A GLN   A 222 ? 0.49824 0.98367 0.83811 -0.05478 -0.08148 0.01896  374 GLN   A CD   
1653 C  CD   B GLN   A 222 ? 0.41142 0.90631 0.71580 -0.08264 -0.10792 0.03072  374 GLN   A CD   
1654 O  OE1  A GLN   A 222 ? 0.69108 1.20192 1.06029 -0.05033 -0.07117 0.01259  374 GLN   A OE1  
1655 O  OE1  B GLN   A 222 ? 0.43606 0.91555 0.70546 -0.09716 -0.11403 0.02846  374 GLN   A OE1  
1656 N  NE2  A GLN   A 222 ? 0.43278 0.89686 0.77208 -0.03969 -0.08707 0.02608  374 GLN   A NE2  
1657 N  NE2  B GLN   A 222 ? 0.41802 0.94892 0.76161 -0.07201 -0.11881 0.04355  374 GLN   A NE2  
1658 N  N    . LEU   A 223 ? 0.31409 0.67472 0.52189 -0.08696 -0.03991 -0.01337 375 LEU   A N    
1659 C  CA   . LEU   A 223 ? 0.30379 0.62403 0.47766 -0.08788 -0.03538 -0.01667 375 LEU   A CA   
1660 C  C    . LEU   A 223 ? 0.38527 0.68849 0.55806 -0.06908 -0.03268 -0.01852 375 LEU   A C    
1661 O  O    . LEU   A 223 ? 0.33780 0.61210 0.48829 -0.06685 -0.03630 -0.01751 375 LEU   A O    
1662 C  CB   . LEU   A 223 ? 0.30461 0.61915 0.46698 -0.09929 -0.02316 -0.01966 375 LEU   A CB   
1663 C  CG   . LEU   A 223 ? 0.33451 0.60964 0.46504 -0.10066 -0.01940 -0.02100 375 LEU   A CG   
1664 C  CD1  . LEU   A 223 ? 0.33140 0.58223 0.44363 -0.10587 -0.03002 -0.02085 375 LEU   A CD1  
1665 C  CD2  . LEU   A 223 ? 0.37999 0.65293 0.50255 -0.11417 -0.00996 -0.01869 375 LEU   A CD2  
1666 N  N    . TYR   A 224 ? 0.37032 0.69166 0.56898 -0.05576 -0.02595 -0.02274 376 TYR   A N    
1667 C  CA   . TYR   A 224 ? 0.35595 0.65928 0.55743 -0.03887 -0.02393 -0.02679 376 TYR   A CA   
1668 C  C    . TYR   A 224 ? 0.34480 0.63901 0.55281 -0.03135 -0.03805 -0.01644 376 TYR   A C    
1669 O  O    . TYR   A 224 ? 0.33636 0.60278 0.52885 -0.02641 -0.04005 -0.01514 376 TYR   A O    
1670 C  CB   . TYR   A 224 ? 0.34858 0.67467 0.58120 -0.02572 -0.01386 -0.03711 376 TYR   A CB   
1671 C  CG   . TYR   A 224 ? 0.31969 0.62568 0.55983 -0.00900 -0.01237 -0.04418 376 TYR   A CG   
1672 C  CD1  . TYR   A 224 ? 0.33007 0.60913 0.54189 -0.00994 -0.00632 -0.05136 376 TYR   A CD1  
1673 C  CD2  . TYR   A 224 ? 0.37504 0.68856 0.65340 0.00725  -0.01813 -0.04284 376 TYR   A CD2  
1674 C  CE1  . TYR   A 224 ? 0.36867 0.62945 0.58878 0.00332  -0.00567 -0.05916 376 TYR   A CE1  
1675 C  CE2  . TYR   A 224 ? 0.37217 0.66393 0.66118 0.02129  -0.01730 -0.04982 376 TYR   A CE2  
1676 C  CZ   . TYR   A 224 ? 0.37824 0.64386 0.63730 0.01848  -0.01090 -0.05901 376 TYR   A CZ   
1677 O  OH   . TYR   A 224 ? 0.44250 0.68674 0.71346 0.03051  -0.01066 -0.06732 376 TYR   A OH   
1678 N  N    . ALA   A 225 ? 0.31771 0.63818 0.54921 -0.03137 -0.04848 -0.00715 377 ALA   A N    
1679 C  CA   . ALA   A 225 ? 0.30932 0.62689 0.54634 -0.02608 -0.06328 0.00703  377 ALA   A CA   
1680 C  C    . ALA   A 225 ? 0.34634 0.64296 0.54385 -0.03851 -0.06908 0.01106  377 ALA   A C    
1681 O  O    . ALA   A 225 ? 0.39587 0.67732 0.58533 -0.03370 -0.07562 0.01971  377 ALA   A O    
1682 C  CB   . ALA   A 225 ? 0.33549 0.69113 0.60426 -0.02568 -0.07463 0.01784  377 ALA   A CB   
1683 N  N    . LYS   A 226 ? 0.34614 0.64228 0.52098 -0.05481 -0.06629 0.00455  378 LYS   A N    
1684 C  CA   . LYS   A 226 ? 0.30671 0.58247 0.44656 -0.06563 -0.06984 0.00371  378 LYS   A CA   
1685 C  C    . LYS   A 226 ? 0.36204 0.60310 0.48121 -0.05984 -0.06157 -0.00114 378 LYS   A C    
1686 O  O    . LYS   A 226 ? 0.34940 0.57528 0.44821 -0.06113 -0.06551 0.00164  378 LYS   A O    
1687 C  CB   . LYS   A 226 ? 0.31309 0.59285 0.44000 -0.08383 -0.06840 -0.00425 378 LYS   A CB   
1688 C  CG   . LYS   A 226 ? 0.36284 0.67711 0.50394 -0.09390 -0.07988 -0.00011 378 LYS   A CG   
1689 C  CD   . LYS   A 226 ? 0.40056 0.71375 0.52941 -0.11392 -0.07892 -0.00998 378 LYS   A CD   
1690 C  CE   . LYS   A 226 ? 0.52526 0.87692 0.67174 -0.12534 -0.09055 -0.00730 378 LYS   A CE   
1691 N  NZ   . LYS   A 226 ? 0.56642 0.92010 0.71377 -0.14460 -0.08739 -0.01660 378 LYS   A NZ   
1692 N  N    . MET   A 227 ? 0.30350 0.53569 0.42752 -0.05406 -0.05013 -0.00853 379 MET   A N    
1693 C  CA   . MET   A 227 ? 0.30361 0.50673 0.40980 -0.04887 -0.04358 -0.01288 379 MET   A CA   
1694 C  C    . MET   A 227 ? 0.35494 0.55050 0.47303 -0.03539 -0.04764 -0.00733 379 MET   A C    
1695 O  O    . MET   A 227 ? 0.32149 0.49539 0.42298 -0.03388 -0.04772 -0.00623 379 MET   A O    
1696 C  CB   . MET   A 227 ? 0.30164 0.50306 0.40767 -0.04842 -0.03124 -0.02188 379 MET   A CB   
1697 C  CG   . MET   A 227 ? 0.31338 0.51664 0.40670 -0.06337 -0.02709 -0.02367 379 MET   A CG   
1698 S  SD   . MET   A 227 ? 0.31143 0.52322 0.40564 -0.06486 -0.01305 -0.02916 379 MET   A SD   
1699 C  CE   . MET   A 227 ? 0.26625 0.44653 0.33574 -0.05934 -0.00970 -0.03160 379 MET   A CE   
1700 N  N    . ILE   A 228 ? 0.38149 0.59475 0.53183 -0.02553 -0.05118 -0.00318 380 ILE   A N    
1701 C  CA   . ILE   A 228 ? 0.44554 0.64955 0.61336 -0.01328 -0.05663 0.00456  380 ILE   A CA   
1702 C  C    . ILE   A 228 ? 0.41289 0.61743 0.56991 -0.01806 -0.06884 0.02111  380 ILE   A C    
1703 O  O    . ILE   A 228 ? 0.39933 0.58780 0.55466 -0.01371 -0.07194 0.02889  380 ILE   A O    
1704 C  CB   . ILE   A 228 ? 0.48768 0.70994 0.69888 -0.00019 -0.05748 0.00454  380 ILE   A CB   
1705 C  CG1  . ILE   A 228 ? 0.42837 0.65324 0.64731 0.00441  -0.04318 -0.01493 380 ILE   A CG1  
1706 C  CG2  . ILE   A 228 ? 0.50762 0.71736 0.74299 0.01213  -0.06496 0.01515  380 ILE   A CG2  
1707 C  CD1  . ILE   A 228 ? 0.50031 0.69851 0.69717 0.00471  -0.03492 -0.02618 380 ILE   A CD1  
1708 N  N    . GLN   A 229 ? 0.31837 0.54389 0.46746 -0.02845 -0.07588 0.02647  381 GLN   A N    
1709 C  CA   . GLN   A 229 ? 0.33786 0.56900 0.46964 -0.03559 -0.08639 0.03953  381 GLN   A CA   
1710 C  C    . GLN   A 229 ? 0.36229 0.56941 0.45969 -0.04153 -0.08059 0.03310  381 GLN   A C    
1711 O  O    . GLN   A 229 ? 0.33001 0.53440 0.41720 -0.04215 -0.08546 0.04393  381 GLN   A O    
1712 C  CB   . GLN   A 229 ? 0.41401 0.67409 0.54088 -0.04777 -0.09431 0.04107  381 GLN   A CB   
1713 C  CG   . GLN   A 229 ? 0.48273 0.75717 0.59050 -0.05634 -0.10579 0.05333  381 GLN   A CG   
1714 C  CD   . GLN   A 229 ? 0.54062 0.82106 0.66686 -0.04675 -0.11546 0.07651  381 GLN   A CD   
1715 O  OE1  . GLN   A 229 ? 0.54390 0.83589 0.70670 -0.03616 -0.12112 0.08751  381 GLN   A OE1  
1716 N  NE2  . GLN   A 229 ? 0.47652 0.74981 0.58043 -0.05035 -0.11718 0.08479  381 GLN   A NE2  
1717 N  N    . LYS   A 230 ? 0.33634 0.52805 0.41765 -0.04596 -0.07022 0.01709  382 LYS   A N    
1718 C  CA   . LYS   A 230 ? 0.33325 0.50264 0.38720 -0.04963 -0.06458 0.01070  382 LYS   A CA   
1719 C  C    . LYS   A 230 ? 0.36493 0.51586 0.42366 -0.03977 -0.06170 0.01461  382 LYS   A C    
1720 O  O    . LYS   A 230 ? 0.36065 0.50126 0.40233 -0.04174 -0.06093 0.01648  382 LYS   A O    
1721 C  CB   . LYS   A 230 ? 0.40288 0.55975 0.44453 -0.05556 -0.05554 -0.00374 382 LYS   A CB   
1722 C  CG   . LYS   A 230 ? 0.37371 0.54197 0.40631 -0.06877 -0.05838 -0.00945 382 LYS   A CG   
1723 C  CD   . LYS   A 230 ? 0.47461 0.64552 0.48664 -0.07565 -0.06338 -0.01023 382 LYS   A CD   
1724 C  CE   . LYS   A 230 ? 0.53140 0.72229 0.53960 -0.08903 -0.06986 -0.01574 382 LYS   A CE   
1725 N  NZ   . LYS   A 230 ? 0.54563 0.76819 0.56330 -0.08959 -0.08182 -0.00264 382 LYS   A NZ   
1726 N  N    . LEU   A 231 ? 0.31186 0.45991 0.39524 -0.02961 -0.05972 0.01421  383 LEU   A N    
1727 C  CA   . LEU   A 231 ? 0.34310 0.47383 0.43546 -0.02136 -0.05859 0.01692  383 LEU   A CA   
1728 C  C    . LEU   A 231 ? 0.34274 0.47879 0.44456 -0.02008 -0.06861 0.03621  383 LEU   A C    
1729 O  O    . LEU   A 231 ? 0.34936 0.47202 0.44664 -0.01963 -0.06859 0.04183  383 LEU   A O    
1730 C  CB   . LEU   A 231 ? 0.30121 0.42926 0.42001 -0.01114 -0.05398 0.00796  383 LEU   A CB   
1731 C  CG   . LEU   A 231 ? 0.33516 0.46027 0.44320 -0.01280 -0.04316 -0.00924 383 LEU   A CG   
1732 C  CD1  . LEU   A 231 ? 0.34500 0.47436 0.47968 -0.00277 -0.03809 -0.02016 383 LEU   A CD1  
1733 C  CD2  . LEU   A 231 ? 0.38770 0.49334 0.47023 -0.01666 -0.03853 -0.01416 383 LEU   A CD2  
1734 N  N    . ALA   A 232 ? 0.31302 0.47120 0.42917 -0.02035 -0.07783 0.04858  384 ALA   A N    
1735 C  CA   . ALA   A 232 ? 0.31540 0.48375 0.43840 -0.02109 -0.08892 0.07157  384 ALA   A CA   
1736 C  C    . ALA   A 232 ? 0.37224 0.54709 0.45950 -0.03309 -0.08948 0.07519  384 ALA   A C    
1737 O  O    . ALA   A 232 ? 0.37491 0.54834 0.45868 -0.03470 -0.09264 0.08996  384 ALA   A O    
1738 C  CB   . ALA   A 232 ? 0.33325 0.52851 0.48029 -0.01882 -0.09998 0.08509  384 ALA   A CB   
1739 N  N    . ASP   A 233 ? 0.32335 0.50626 0.38583 -0.04206 -0.08595 0.06115  385 ASP   A N    
1740 C  CA   . ASP   A 233 ? 0.35686 0.54458 0.38650 -0.05240 -0.08398 0.05775  385 ASP   A CA   
1741 C  C    . ASP   A 233 ? 0.35210 0.51674 0.37208 -0.04977 -0.07525 0.05314  385 ASP   A C    
1742 O  O    . ASP   A 233 ? 0.39818 0.56961 0.40188 -0.05486 -0.07502 0.05946  385 ASP   A O    
1743 C  CB   . ASP   A 233 ? 0.32105 0.51292 0.33196 -0.06115 -0.08015 0.03845  385 ASP   A CB   
1744 C  CG   . ASP   A 233 ? 0.43775 0.65708 0.45653 -0.06675 -0.08964 0.04220  385 ASP   A CG   
1745 O  OD1  . ASP   A 233 ? 0.45666 0.67781 0.46783 -0.07414 -0.08714 0.02668  385 ASP   A OD1  
1746 O  OD2  . ASP   A 233 ? 0.45856 0.69811 0.49339 -0.06426 -0.10034 0.06186  385 ASP   A OD2  
1747 N  N    . LEU   A 234 ? 0.32105 0.46240 0.35095 -0.04252 -0.06801 0.04217  386 LEU   A N    
1748 C  CA   . LEU   A 234 ? 0.29783 0.41962 0.32032 -0.04040 -0.06079 0.03720  386 LEU   A CA   
1749 C  C    . LEU   A 234 ? 0.37004 0.48955 0.40684 -0.03755 -0.06496 0.05451  386 LEU   A C    
1750 O  O    . LEU   A 234 ? 0.34766 0.46259 0.37394 -0.04017 -0.06123 0.05620  386 LEU   A O    
1751 C  CB   . LEU   A 234 ? 0.31426 0.41693 0.34327 -0.03461 -0.05371 0.02246  386 LEU   A CB   
1752 C  CG   . LEU   A 234 ? 0.38977 0.48967 0.40223 -0.03920 -0.04798 0.00754  386 LEU   A CG   
1753 C  CD1  . LEU   A 234 ? 0.33699 0.42724 0.35868 -0.03463 -0.04288 -0.00180 386 LEU   A CD1  
1754 C  CD2  . LEU   A 234 ? 0.41302 0.50475 0.40480 -0.04283 -0.04285 0.00129  386 LEU   A CD2  
1755 N  N    . ARG   A 235 ? 0.39611 0.51870 0.46036 -0.03220 -0.07268 0.06799  387 ARG   A N    
1756 C  CA   . ARG   A 235 ? 0.42207 0.54060 0.50460 -0.03064 -0.07809 0.08767  387 ARG   A CA   
1757 C  C    . ARG   A 235 ? 0.47297 0.61272 0.53649 -0.04052 -0.08197 0.10556  387 ARG   A C    
1758 O  O    . ARG   A 235 ? 0.40135 0.53738 0.46374 -0.04380 -0.08047 0.11548  387 ARG   A O    
1759 C  CB   . ARG   A 235 ? 0.43753 0.55584 0.55765 -0.02221 -0.08676 0.09979  387 ARG   A CB   
1760 C  CG   . ARG   A 235 ? 0.42589 0.52817 0.56677 -0.01208 -0.08158 0.08002  387 ARG   A CG   
1761 C  CD   . ARG   A 235 ? 0.41401 0.49140 0.55834 -0.00959 -0.07465 0.06736  387 ARG   A CD   
1762 N  NE   . ARG   A 235 ? 0.41103 0.47771 0.57486 -0.00057 -0.06975 0.04761  387 ARG   A NE   
1763 C  CZ   . ARG   A 235 ? 0.44158 0.49651 0.64288 0.00836  -0.07267 0.04713  387 ARG   A CZ   
1764 N  NH1  . ARG   A 235 ? 0.50793 0.55699 0.73395 0.00935  -0.08175 0.06888  387 ARG   A NH1  
1765 N  NH2  . ARG   A 235 ? 0.41005 0.45990 0.62549 0.01598  -0.06628 0.02473  387 ARG   A NH2  
1766 N  N    . SER   A 236 ? 0.41802 0.58349 0.46601 -0.04659 -0.08672 0.10912  388 SER   A N    
1767 C  CA   . SER   A 236 ? 0.43424 0.62665 0.45948 -0.05740 -0.08971 0.12329  388 SER   A CA   
1768 C  C    . SER   A 236 ? 0.40590 0.59650 0.40181 -0.06288 -0.07794 0.10599  388 SER   A C    
1769 O  O    . SER   A 236 ? 0.44824 0.65186 0.43319 -0.06912 -0.07606 0.11731  388 SER   A O    
1770 C  CB   . SER   A 236 ? 0.50856 0.73151 0.52323 -0.06348 -0.09813 0.12697  388 SER   A CB   
1771 O  OG   . SER   A 236 ? 0.63587 0.88331 0.61548 -0.07522 -0.09518 0.12136  388 SER   A OG   
1772 N  N    . LEU   A 237 ? 0.37818 0.55436 0.36353 -0.06061 -0.06982 0.07977  389 LEU   A N    
1773 C  CA   . LEU   A 237 ? 0.35105 0.52227 0.31557 -0.06312 -0.05886 0.06290  389 LEU   A CA   
1774 C  C    . LEU   A 237 ? 0.36708 0.52120 0.34296 -0.05885 -0.05404 0.06748  389 LEU   A C    
1775 O  O    . LEU   A 237 ? 0.38146 0.54340 0.34502 -0.06255 -0.04755 0.06607  389 LEU   A O    
1776 C  CB   . LEU   A 237 ? 0.35344 0.50936 0.31081 -0.06096 -0.05299 0.03797  389 LEU   A CB   
1777 C  CG   . LEU   A 237 ? 0.39932 0.57240 0.34304 -0.06815 -0.05629 0.02863  389 LEU   A CG   
1778 C  CD1  . LEU   A 237 ? 0.35165 0.50553 0.29894 -0.06589 -0.05273 0.01047  389 LEU   A CD1  
1779 C  CD2  . LEU   A 237 ? 0.44841 0.64146 0.36652 -0.07661 -0.05197 0.01940  389 LEU   A CD2  
1780 N  N    . ASN   A 238 ? 0.37095 0.50389 0.37167 -0.05145 -0.05682 0.07110  390 ASN   A N    
1781 C  CA   . ASN   A 238 ? 0.38467 0.50216 0.39953 -0.04893 -0.05428 0.07541  390 ASN   A CA   
1782 C  C    . ASN   A 238 ? 0.39640 0.52997 0.41459 -0.05581 -0.05762 0.09925  390 ASN   A C    
1783 O  O    . ASN   A 238 ? 0.40892 0.54421 0.42349 -0.05919 -0.05195 0.10045  390 ASN   A O    
1784 C  CB   . ASN   A 238 ? 0.34968 0.44529 0.39224 -0.04081 -0.05796 0.07366  390 ASN   A CB   
1785 C  CG   . ASN   A 238 ? 0.42504 0.50219 0.48025 -0.03873 -0.05472 0.06935  390 ASN   A CG   
1786 O  OD1  . ASN   A 238 ? 0.39959 0.48153 0.45191 -0.04391 -0.05262 0.07731  390 ASN   A OD1  
1787 N  ND2  . ASN   A 238 ? 0.37153 0.43085 0.44122 -0.03201 -0.05422 0.05603  390 ASN   A ND2  
1788 N  N    . GLU   A 239 ? 0.43139 0.57958 0.45807 -0.05848 -0.06724 0.12055  391 GLU   A N    
1789 C  CA   . GLU   A 239 ? 0.47695 0.64212 0.50881 -0.06630 -0.07180 0.14887  391 GLU   A CA   
1790 C  C    . GLU   A 239 ? 0.48776 0.68309 0.48757 -0.07632 -0.06462 0.14813  391 GLU   A C    
1791 O  O    . GLU   A 239 ? 0.47946 0.68371 0.47979 -0.08247 -0.06086 0.16040  391 GLU   A O    
1792 C  CB   . GLU   A 239 ? 0.50100 0.67826 0.54918 -0.06662 -0.08516 0.17410  391 GLU   A CB   
1793 C  CG   . GLU   A 239 ? 0.63098 0.78065 0.71690 -0.05534 -0.09165 0.17457  391 GLU   A CG   
1794 C  CD   . GLU   A 239 ? 0.78422 0.93872 0.90098 -0.05539 -0.10499 0.20869  391 GLU   A CD   
1795 O  OE1  . GLU   A 239 ? 0.80072 0.97789 0.91656 -0.05611 -0.11416 0.22265  391 GLU   A OE1  
1796 O  OE2  . GLU   A 239 ? 0.81731 0.95310 0.96154 -0.05510 -0.10720 0.22235  391 GLU   A OE2  
1797 N  N    . GLU   A 240 ? 0.46372 0.67653 0.43707 -0.07866 -0.06209 0.13234  392 GLU   A N    
1798 C  CA   . GLU   A 240 ? 0.48909 0.73285 0.43248 -0.08772 -0.05422 0.12669  392 GLU   A CA   
1799 C  C    . GLU   A 240 ? 0.43689 0.66915 0.37601 -0.08467 -0.04092 0.10668  392 GLU   A C    
1800 O  O    . GLU   A 240 ? 0.44033 0.69540 0.36878 -0.09112 -0.03361 0.11074  392 GLU   A O    
1801 C  CB   . GLU   A 240 ? 0.47508 0.73766 0.39409 -0.09128 -0.05509 0.11001  392 GLU   A CB   
1802 C  CG   . GLU   A 240 ? 0.50055 0.80025 0.38818 -0.10147 -0.04732 0.10177  392 GLU   A CG   
1803 C  CD   . GLU   A 240 ? 0.51812 0.85444 0.39989 -0.11235 -0.05171 0.13370  392 GLU   A CD   
1804 O  OE1  . GLU   A 240 ? 0.51726 0.87776 0.38338 -0.11880 -0.04145 0.13178  392 GLU   A OE1  
1805 O  OE2  . GLU   A 240 ? 0.54184 0.88467 0.43638 -0.11447 -0.06536 0.16192  392 GLU   A OE2  
1806 N  N    . HIS   A 241 ? 0.34855 0.54914 0.29679 -0.07510 -0.03768 0.08622  393 HIS   A N    
1807 C  CA   . HIS   A 241 ? 0.39444 0.58495 0.34243 -0.07125 -0.02703 0.07002  393 HIS   A CA   
1808 C  C    . HIS   A 241 ? 0.39827 0.58757 0.36421 -0.07337 -0.02654 0.08735  393 HIS   A C    
1809 O  O    . HIS   A 241 ? 0.38300 0.58779 0.34419 -0.07640 -0.01788 0.08514  393 HIS   A O    
1810 C  CB   . HIS   A 241 ? 0.39795 0.55700 0.35308 -0.06163 -0.02577 0.04990  393 HIS   A CB   
1811 C  CG   . HIS   A 241 ? 0.39726 0.54619 0.35668 -0.05688 -0.01751 0.03765  393 HIS   A CG   
1812 N  ND1  . HIS   A 241 ? 0.40850 0.54201 0.38726 -0.05393 -0.01908 0.04358  393 HIS   A ND1  
1813 C  CD2  . HIS   A 241 ? 0.41564 0.56954 0.36509 -0.05450 -0.00827 0.01984  393 HIS   A CD2  
1814 C  CE1  . HIS   A 241 ? 0.43833 0.57012 0.41769 -0.05026 -0.01198 0.03180  393 HIS   A CE1  
1815 N  NE2  . HIS   A 241 ? 0.38554 0.52866 0.34893 -0.04958 -0.00514 0.01786  393 HIS   A NE2  
1816 N  N    . SER   A 242 ? 0.41875 0.59015 0.40847 -0.07194 -0.03555 0.10356  394 SER   A N    
1817 C  CA   . SER   A 242 ? 0.45448 0.62193 0.46537 -0.07572 -0.03647 0.12019  394 SER   A CA   
1818 C  C    . SER   A 242 ? 0.45780 0.65949 0.46100 -0.08758 -0.03482 0.14319  394 SER   A C    
1819 O  O    . SER   A 242 ? 0.43717 0.64807 0.44722 -0.09289 -0.02929 0.14975  394 SER   A O    
1820 C  CB   . SER   A 242 ? 0.56984 0.71136 0.61037 -0.07225 -0.04709 0.13189  394 SER   A CB   
1821 O  OG   . SER   A 242 ? 0.62826 0.74440 0.67340 -0.06223 -0.04754 0.11014  394 SER   A OG   
1822 N  N    . LYS   A 243 ? 0.45506 0.67976 0.44398 -0.09291 -0.03983 0.15669  395 LYS   A N    
1823 C  CA   . LYS   A 243 ? 0.46421 0.72902 0.43995 -0.10575 -0.03802 0.17920  395 LYS   A CA   
1824 C  C    . LYS   A 243 ? 0.45812 0.74880 0.41112 -0.10869 -0.02279 0.16007  395 LYS   A C    
1825 O  O    . LYS   A 243 ? 0.52464 0.83495 0.48158 -0.11620 -0.01630 0.17207  395 LYS   A O    
1826 C  CB   . LYS   A 243 ? 0.50462 0.79321 0.46450 -0.11054 -0.04684 0.19266  395 LYS   A CB   
1827 C  CG   . LYS   A 243 ? 0.57740 0.90909 0.52677 -0.12528 -0.04908 0.22507  395 LYS   A CG   
1828 C  CD   . LYS   A 243 ? 0.55392 0.90607 0.49420 -0.12919 -0.06218 0.24312  395 LYS   A CD   
1829 C  CE   . LYS   A 243 ? 0.59475 1.00186 0.51089 -0.14555 -0.06235 0.26897  395 LYS   A CE   
1830 N  NZ   . LYS   A 243 ? 0.61231 1.04612 0.51125 -0.14890 -0.07199 0.27106  395 LYS   A NZ   
1831 N  N    . GLN   A 244 ? 0.47423 0.76549 0.40651 -0.10276 -0.01663 0.12971  396 GLN   A N    
1832 C  CA   . GLN   A 244 ? 0.44455 0.75845 0.35960 -0.10323 -0.00173 0.10771  396 GLN   A CA   
1833 C  C    . GLN   A 244 ? 0.46235 0.75773 0.39726 -0.09644 0.00553  0.09790  396 GLN   A C    
1834 O  O    . GLN   A 244 ? 0.43701 0.75807 0.36905 -0.09937 0.01707  0.09345  396 GLN   A O    
1835 C  CB   . GLN   A 244 ? 0.44258 0.75517 0.33678 -0.09816 0.00176  0.07677  396 GLN   A CB   
1836 C  CG   . GLN   A 244 ? 0.50816 0.84109 0.38298 -0.10565 -0.00684 0.08401  396 GLN   A CG   
1837 C  CD   . GLN   A 244 ? 0.55449 0.89765 0.40582 -0.10518 -0.00089 0.05142  396 GLN   A CD   
1838 O  OE1  . GLN   A 244 ? 0.48919 0.81924 0.34171 -0.09765 0.00954  0.02356  396 GLN   A OE1  
1839 N  NE2  . GLN   A 244 ? 0.52521 0.89174 0.35764 -0.11346 -0.00849 0.05497  396 GLN   A NE2  
1840 N  N    . TYR   A 245 ? 0.40051 0.65578 0.35590 -0.08776 -0.00095 0.09408  397 TYR   A N    
1841 C  CA   . TYR   A 245 ? 0.45036 0.69130 0.42501 -0.08275 0.00353  0.08714  397 TYR   A CA   
1842 C  C    . TYR   A 245 ? 0.48531 0.74231 0.47661 -0.09277 0.00375  0.11176  397 TYR   A C    
1843 O  O    . TYR   A 245 ? 0.41101 0.68182 0.41013 -0.09347 0.01236  0.10728  397 TYR   A O    
1844 C  CB   . TYR   A 245 ? 0.38394 0.58368 0.37449 -0.07367 -0.00448 0.07928  397 TYR   A CB   
1845 C  CG   . TYR   A 245 ? 0.39900 0.58696 0.40923 -0.07018 -0.00245 0.07408  397 TYR   A CG   
1846 C  CD1  . TYR   A 245 ? 0.35022 0.53766 0.35802 -0.06209 0.00496  0.05336  397 TYR   A CD1  
1847 C  CD2  . TYR   A 245 ? 0.42774 0.60601 0.46147 -0.07544 -0.00883 0.09027  397 TYR   A CD2  
1848 C  CE1  . TYR   A 245 ? 0.37671 0.55805 0.40308 -0.05931 0.00524  0.05036  397 TYR   A CE1  
1849 C  CE2  . TYR   A 245 ? 0.43003 0.60119 0.48145 -0.07397 -0.00811 0.08448  397 TYR   A CE2  
1850 C  CZ   . TYR   A 245 ? 0.41667 0.59140 0.46333 -0.06592 -0.00140 0.06524  397 TYR   A CZ   
1851 O  OH   . TYR   A 245 ? 0.42218 0.59386 0.48705 -0.06473 -0.00231 0.06110  397 TYR   A OH   
1852 N  N    . ARG   A 246 ? 0.49067 0.74630 0.49112 -0.10075 -0.00610 0.13920  398 ARG   A N    
1853 C  CA   . ARG   A 246 ? 0.54154 0.80902 0.56194 -0.11207 -0.00719 0.16594  398 ARG   A CA   
1854 C  C    . ARG   A 246 ? 0.53492 0.85190 0.53883 -0.12266 0.00434  0.17460  398 ARG   A C    
1855 O  O    . ARG   A 246 ? 0.48506 0.81796 0.50367 -0.12994 0.01005  0.18456  398 ARG   A O    
1856 C  CB   . ARG   A 246 ? 0.62072 0.87344 0.65825 -0.11745 -0.02122 0.19496  398 ARG   A CB   
1857 C  CG   . ARG   A 246 ? 0.67961 0.88733 0.74801 -0.11083 -0.03040 0.19076  398 ARG   A CG   
1858 C  CD   . ARG   A 246 ? 0.74507 0.93406 0.83340 -0.11181 -0.04417 0.21348  398 ARG   A CD   
1859 N  NE   . ARG   A 246 ? 0.81475 1.03482 0.89240 -0.12163 -0.04762 0.24355  398 ARG   A NE   
1860 C  CZ   . ARG   A 246 ? 0.86032 1.08067 0.93373 -0.11872 -0.05682 0.25393  398 ARG   A CZ   
1861 N  NH1  . ARG   A 246 ? 0.84148 1.03238 0.92175 -0.10599 -0.06208 0.23547  398 ARG   A NH1  
1862 N  NH2  . ARG   A 246 ? 0.87740 1.13137 0.93991 -0.12914 -0.06091 0.28372  398 ARG   A NH2  
1863 N  N    . SER   A 247 ? 0.52290 0.86787 0.49640 -0.12450 0.00834  0.16938  399 SER   A N    
1864 C  CA   . SER   A 247 ? 0.56432 0.96178 0.51852 -0.13450 0.02117  0.17270  399 SER   A CA   
1865 C  C    . SER   A 247 ? 0.53833 0.94561 0.49096 -0.12628 0.03669  0.14101  399 SER   A C    
1866 O  O    . SER   A 247 ? 0.53856 0.98124 0.49453 -0.13314 0.04819  0.14566  399 SER   A O    
1867 C  CB   . SER   A 247 ? 0.61854 1.04554 0.53943 -0.13967 0.02021  0.17309  399 SER   A CB   
1868 O  OG   . SER   A 247 ? 0.66937 1.14214 0.56584 -0.14334 0.03634  0.15492  399 SER   A OG   
1869 N  N    . LEU   A 248 ? 0.50059 0.87845 0.45090 -0.11159 0.03722  0.11011  400 LEU   A N    
1870 C  CA   . LEU   A 248 ? 0.49414 0.87719 0.44875 -0.10165 0.05023  0.08148  400 LEU   A CA   
1871 C  C    . LEU   A 248 ? 0.42065 0.79472 0.40625 -0.10049 0.05062  0.08902  400 LEU   A C    
1872 O  O    . LEU   A 248 ? 0.49281 0.89759 0.48631 -0.10158 0.06285  0.08432  400 LEU   A O    
1873 C  CB   . LEU   A 248 ? 0.45956 0.80901 0.40852 -0.08723 0.04821  0.05215  400 LEU   A CB   
1874 C  CG   . LEU   A 248 ? 0.55865 0.91969 0.47863 -0.08799 0.05010  0.03601  400 LEU   A CG   
1875 C  CD1  . LEU   A 248 ? 0.56514 0.89166 0.48585 -0.07452 0.04928  0.00723  400 LEU   A CD1  
1876 C  CD2  . LEU   A 248 ? 0.59711 1.00987 0.49920 -0.09448 0.06517  0.02623  400 LEU   A CD2  
1877 N  N    . SER   A 249 ? 0.50636 0.84151 0.51096 -0.09883 0.03746  0.09952  401 SER   A N    
1878 C  CA   . SER   A 249 ? 0.49593 0.82077 0.52986 -0.09857 0.03573  0.10365  401 SER   A CA   
1879 C  C    . SER   A 249 ? 0.52321 0.87596 0.57234 -0.11451 0.03753  0.13152  401 SER   A C    
1880 O  O    . SER   A 249 ? 0.45048 0.80419 0.52477 -0.11659 0.03806  0.13396  401 SER   A O    
1881 C  CB   . SER   A 249 ? 0.50033 0.77787 0.54831 -0.09336 0.02141  0.10340  401 SER   A CB   
1882 O  OG   . SER   A 249 ? 0.55250 0.81741 0.60330 -0.10163 0.01090  0.12592  401 SER   A OG   
1883 N  N    . PHE   A 250 ? 0.54924 0.92662 0.58487 -0.12695 0.03773  0.15422  402 PHE   A N    
1884 C  CA   . PHE   A 250 ? 0.54195 0.94845 0.59279 -0.14402 0.03979  0.18455  402 PHE   A CA   
1885 C  C    . PHE   A 250 ? 0.53631 0.99100 0.58698 -0.14674 0.05741  0.17608  402 PHE   A C    
1886 O  O    . PHE   A 250 ? 0.48418 0.95956 0.55701 -0.15867 0.06036  0.19496  402 PHE   A O    
1887 C  CB   . PHE   A 250 ? 0.60625 1.03027 0.64204 -0.15707 0.03459  0.21481  402 PHE   A CB   
1888 C  CG   . PHE   A 250 ? 0.68016 1.11869 0.73906 -0.17555 0.03091  0.25373  402 PHE   A CG   
1889 C  CD1  . PHE   A 250 ? 0.75084 1.24229 0.79913 -0.18899 0.04103  0.27108  402 PHE   A CD1  
1890 C  CD2  . PHE   A 250 ? 0.70877 1.10561 0.80120 -0.17855 0.01664  0.27001  402 PHE   A CD2  
1891 C  CE1  . PHE   A 250 ? 0.78699 1.28035 0.85710 -0.20102 0.03352  0.30124  402 PHE   A CE1  
1892 C  CE2  . PHE   A 250 ? 0.75177 1.15833 0.87000 -0.19658 0.01258  0.30645  402 PHE   A CE2  
1893 C  CZ   . PHE   A 250 ? 0.79108 1.24156 0.89665 -0.20502 0.01945  0.31965  402 PHE   A CZ   
1894 N  N    . GLN   A 251 ? 0.53644 1.01006 0.56552 -0.13614 0.06948  0.14735  403 GLN   A N    
1895 C  CA   . GLN   A 251 ? 0.48526 1.00435 0.51799 -0.13520 0.08762  0.13356  403 GLN   A CA   
1896 C  C    . GLN   A 251 ? 0.41420 0.91225 0.47503 -0.12164 0.08781  0.11392  403 GLN   A C    
1897 O  O    . GLN   A 251 ? 0.38546 0.84913 0.44328 -0.10564 0.08351  0.09019  403 GLN   A O    
1898 C  CB   . GLN   A 251 ? 0.55250 1.10049 0.55367 -0.12911 0.10072  0.10802  403 GLN   A CB   
1899 C  CG   . GLN   A 251 ? 0.64215 1.20375 0.61065 -0.14020 0.09617  0.12309  403 GLN   A CG   
1900 C  CD   . GLN   A 251 ? 0.76043 1.35483 0.72898 -0.15925 0.09432  0.15971  403 GLN   A CD   
1901 O  OE1  . GLN   A 251 ? 0.81142 1.39323 0.77419 -0.16831 0.07993  0.18746  403 GLN   A OE1  
1902 N  NE2  . GLN   A 251 ? 0.73862 1.36619 0.71732 -0.16202 0.10522  0.15783  403 GLN   A NE2  
1903 N  N    . PRO   A 252 ? 0.44190 0.96122 0.53128 -0.12842 0.09173  0.12486  404 PRO   A N    
1904 C  CA   . PRO   A 252 ? 0.42179 0.92238 0.53962 -0.11664 0.08864  0.10949  404 PRO   A CA   
1905 C  C    . PRO   A 252 ? 0.41735 0.92287 0.53224 -0.09656 0.09881  0.07551  404 PRO   A C    
1906 O  O    . PRO   A 252 ? 0.42964 0.90373 0.55859 -0.08319 0.09111  0.06173  404 PRO   A O    
1907 C  CB   . PRO   A 252 ? 0.49412 1.03200 0.64103 -0.13068 0.09402  0.12844  404 PRO   A CB   
1908 C  CG   . PRO   A 252 ? 0.55267 1.10208 0.69164 -0.15173 0.09087  0.16195  404 PRO   A CG   
1909 C  CD   . PRO   A 252 ? 0.48198 1.04073 0.58145 -0.14925 0.09618  0.15617  404 PRO   A CD   
1910 N  N    . GLU   A 253 ? 0.48604 1.03068 0.58411 -0.09427 0.11564  0.06142  405 GLU   A N    
1911 C  CA   . GLU   A 253 ? 0.48220 1.02727 0.58114 -0.07426 0.12533  0.02687  405 GLU   A CA   
1912 C  C    . GLU   A 253 ? 0.46163 0.95299 0.54587 -0.06210 0.11357  0.01222  405 GLU   A C    
1913 O  O    . GLU   A 253 ? 0.44296 0.91573 0.53961 -0.04472 0.11414  -0.00985 405 GLU   A O    
1914 C  CB   . GLU   A 253 ? 0.55485 1.15071 0.63523 -0.07567 0.14557  0.01122  405 GLU   A CB   
1915 C  CG   . GLU   A 253 ? 0.71073 1.36541 0.79477 -0.09371 0.15730  0.03241  405 GLU   A CG   
1916 C  CD   . GLU   A 253 ? 0.82492 1.48659 0.87703 -0.11294 0.15165  0.05813  405 GLU   A CD   
1917 O  OE1  . GLU   A 253 ? 0.91278 1.60574 0.94480 -0.11898 0.15913  0.05684  405 GLU   A OE1  
1918 O  OE2  . GLU   A 253 ? 0.80570 1.42953 0.85330 -0.11931 0.13488  0.07859  405 GLU   A OE2  
1919 N  N    . ASN   A 254 ? 0.39103 0.85844 0.45164 -0.07108 0.10260  0.02590  406 ASN   A N    
1920 C  CA   . ASN   A 254 ? 0.35512 0.77479 0.40268 -0.06147 0.09160  0.01403  406 ASN   A CA   
1921 C  C    . ASN   A 254 ? 0.34324 0.72117 0.40980 -0.05757 0.07594  0.02250  406 ASN   A C    
1922 O  O    . ASN   A 254 ? 0.38192 0.72928 0.45226 -0.04421 0.07099  0.00697  406 ASN   A O    
1923 C  CB   . ASN   A 254 ? 0.42987 0.84565 0.44680 -0.07195 0.08633  0.02434  406 ASN   A CB   
1924 C  CG   . ASN   A 254 ? 0.54460 0.99554 0.53622 -0.07330 0.09991  0.00704  406 ASN   A CG   
1925 O  OD1  . ASN   A 254 ? 0.54096 1.00681 0.53746 -0.06248 0.11279  -0.02007 406 ASN   A OD1  
1926 N  ND2  . ASN   A 254 ? 0.52303 0.98858 0.48880 -0.08649 0.09665  0.02185  406 ASN   A ND2  
1927 N  N    A SER   A 255 ? 0.37005 0.74686 0.44915 -0.07004 0.06779  0.04694  407 SER   A N    
1928 N  N    B SER   A 255 ? 0.36701 0.74413 0.44586 -0.07021 0.06786  0.04711  407 SER   A N    
1929 C  CA   A SER   A 255 ? 0.37547 0.71639 0.47194 -0.06773 0.05334  0.05152  407 SER   A CA   
1930 C  CA   B SER   A 255 ? 0.37805 0.72066 0.47522 -0.06842 0.05358  0.05245  407 SER   A CA   
1931 C  C    A SER   A 255 ? 0.35052 0.69552 0.47095 -0.05649 0.05484  0.03881  407 SER   A C    
1932 C  C    B SER   A 255 ? 0.34826 0.69303 0.46777 -0.05607 0.05511  0.03811  407 SER   A C    
1933 O  O    A SER   A 255 ? 0.35609 0.67155 0.48470 -0.05059 0.04344  0.03538  407 SER   A O    
1934 O  O    B SER   A 255 ? 0.32408 0.63804 0.44985 -0.04893 0.04417  0.03305  407 SER   A O    
1935 C  CB   A SER   A 255 ? 0.41198 0.75228 0.52189 -0.08422 0.04512  0.07755  407 SER   A CB   
1936 C  CB   B SER   A 255 ? 0.41714 0.76446 0.53006 -0.08519 0.04688  0.07845  407 SER   A CB   
1937 O  OG   A SER   A 255 ? 0.45863 0.84168 0.58202 -0.09493 0.05485  0.09008  407 SER   A OG   
1938 O  OG   B SER   A 255 ? 0.47512 0.79481 0.57714 -0.09180 0.03610  0.09157  407 SER   A OG   
1939 N  N    . MET   A 256 ? 0.35636 0.74056 0.48884 -0.05329 0.06864  0.03197  408 MET   A N    
1940 C  CA   . MET   A 256 ? 0.35670 0.74826 0.51594 -0.04063 0.06988  0.02064  408 MET   A CA   
1941 C  C    . MET   A 256 ? 0.42581 0.78789 0.57984 -0.02249 0.06721  0.00095  408 MET   A C    
1942 O  O    . MET   A 256 ? 0.37083 0.72420 0.54544 -0.01225 0.06080  -0.00287 408 MET   A O    
1943 C  CB   . MET   A 256 ? 0.33717 0.78040 0.51216 -0.03965 0.08731  0.01559  408 MET   A CB   
1944 C  CG   . MET   A 256 ? 0.43454 0.90727 0.64032 -0.04919 0.08662  0.03083  408 MET   A CG   
1945 S  SD   . MET   A 256 ? 0.46841 1.00908 0.68816 -0.05065 0.11026  0.02597  408 MET   A SD   
1946 C  CE   . MET   A 256 ? 0.45643 0.99425 0.67713 -0.02415 0.12115  -0.00852 408 MET   A CE   
1947 N  N    . LYS   A 257 ? 0.30572 0.65400 0.43393 -0.01932 0.07125  -0.01023 409 LYS   A N    
1948 C  CA   . LYS   A 257 ? 0.30630 0.62580 0.43093 -0.00403 0.06934  -0.02817 409 LYS   A CA   
1949 C  C    . LYS   A 257 ? 0.29641 0.57243 0.40766 -0.00524 0.05383  -0.02199 409 LYS   A C    
1950 O  O    . LYS   A 257 ? 0.35322 0.60372 0.46363 0.00577  0.05034  -0.03262 409 LYS   A O    
1951 C  CB   . LYS   A 257 ? 0.40339 0.73209 0.50940 -0.00074 0.08217  -0.04727 409 LYS   A CB   
1952 C  CG   . LYS   A 257 ? 0.52899 0.90774 0.63754 -0.00516 0.09916  -0.05214 409 LYS   A CG   
1953 C  CD   . LYS   A 257 ? 0.62997 1.03094 0.77189 0.00958  0.10912  -0.06641 409 LYS   A CD   
1954 C  CE   . LYS   A 257 ? 0.67802 1.05298 0.82750 0.02796  0.11087  -0.09094 409 LYS   A CE   
1955 N  NZ   . LYS   A 257 ? 0.67703 1.07441 0.86415 0.04455  0.12106  -0.10553 409 LYS   A NZ   
1956 N  N    . LEU   A 258 ? 0.30201 0.56978 0.40537 -0.01826 0.04493  -0.00522 410 LEU   A N    
1957 C  CA   . LEU   A 258 ? 0.31982 0.55079 0.41304 -0.01917 0.03154  -0.00127 410 LEU   A CA   
1958 C  C    . LEU   A 258 ? 0.32805 0.54970 0.44027 -0.01468 0.02162  0.00124  410 LEU   A C    
1959 O  O    . LEU   A 258 ? 0.35760 0.60098 0.49221 -0.01114 0.02386  0.00163  410 LEU   A O    
1960 C  CB   . LEU   A 258 ? 0.33966 0.56543 0.42191 -0.03327 0.02612  0.01376  410 LEU   A CB   
1961 C  CG   . LEU   A 258 ? 0.37665 0.61691 0.43908 -0.03998 0.03349  0.01639  410 LEU   A CG   
1962 C  CD1  . LEU   A 258 ? 0.34418 0.57926 0.40359 -0.05322 0.02590  0.03640  410 LEU   A CD1  
1963 C  CD2  . LEU   A 258 ? 0.38614 0.61026 0.42842 -0.03261 0.03515  0.00098  410 LEU   A CD2  
1964 N  N    . THR   A 259 ? 0.28056 0.47352 0.38398 -0.01509 0.01050  0.00268  411 THR   A N    
1965 C  CA   . THR   A 259 ? 0.33785 0.52532 0.45440 -0.01329 -0.00015 0.00520  411 THR   A CA   
1966 C  C    . THR   A 259 ? 0.31938 0.50299 0.43904 -0.02626 -0.00870 0.01356  411 THR   A C    
1967 O  O    . THR   A 259 ? 0.31071 0.48676 0.42124 -0.03453 -0.00798 0.01846  411 THR   A O    
1968 C  CB   . THR   A 259 ? 0.33807 0.50021 0.44343 -0.00511 -0.00624 -0.00017 411 THR   A CB   
1969 O  OG1  . THR   A 259 ? 0.40062 0.54120 0.48740 -0.01165 -0.01112 0.00061  411 THR   A OG1  
1970 C  CG2  . THR   A 259 ? 0.37055 0.52856 0.47283 0.00594  0.00226  -0.00942 411 THR   A CG2  
1971 N  N    . PRO   A 260 ? 0.31925 0.50879 0.45425 -0.02861 -0.01756 0.01523  412 PRO   A N    
1972 C  CA   . PRO   A 260 ? 0.30259 0.48541 0.44308 -0.04146 -0.02616 0.01898  412 PRO   A CA   
1973 C  C    . PRO   A 260 ? 0.33640 0.49022 0.45898 -0.04315 -0.03100 0.01489  412 PRO   A C    
1974 O  O    . PRO   A 260 ? 0.34254 0.48692 0.46860 -0.05245 -0.03327 0.01869  412 PRO   A O    
1975 C  CB   . PRO   A 260 ? 0.30469 0.50036 0.46109 -0.04188 -0.03563 0.01711  412 PRO   A CB   
1976 C  CG   . PRO   A 260 ? 0.33354 0.55357 0.50330 -0.03198 -0.02932 0.01871  412 PRO   A CG   
1977 C  CD   . PRO   A 260 ? 0.34533 0.55260 0.49796 -0.02073 -0.02013 0.01423  412 PRO   A CD   
1978 N  N    . LEU   A 261 ? 0.31154 0.45172 0.41805 -0.03435 -0.03258 0.00815  413 LEU   A N    
1979 C  CA   . LEU   A 261 ? 0.32148 0.43858 0.41251 -0.03555 -0.03598 0.00343  413 LEU   A CA   
1980 C  C    . LEU   A 261 ? 0.31471 0.42306 0.39694 -0.03691 -0.02970 0.00734  413 LEU   A C    
1981 O  O    . LEU   A 261 ? 0.37412 0.46889 0.45579 -0.04180 -0.03291 0.00787  413 LEU   A O    
1982 C  CB   . LEU   A 261 ? 0.28584 0.39480 0.36242 -0.02726 -0.03816 -0.00190 413 LEU   A CB   
1983 C  CG   . LEU   A 261 ? 0.38132 0.47175 0.44259 -0.02836 -0.04069 -0.00773 413 LEU   A CG   
1984 C  CD1  . LEU   A 261 ? 0.39517 0.48394 0.46304 -0.03618 -0.04804 -0.01408 413 LEU   A CD1  
1985 C  CD2  . LEU   A 261 ? 0.31669 0.40274 0.36436 -0.02164 -0.04155 -0.00914 413 LEU   A CD2  
1986 N  N    . VAL   A 262 ? 0.28117 0.39897 0.35793 -0.03249 -0.02111 0.00936  414 VAL   A N    
1987 C  CA   . VAL   A 262 ? 0.32797 0.44389 0.39418 -0.03514 -0.01595 0.01363  414 VAL   A CA   
1988 C  C    . VAL   A 262 ? 0.36308 0.48596 0.44145 -0.04593 -0.01728 0.02600  414 VAL   A C    
1989 O  O    . VAL   A 262 ? 0.36885 0.48159 0.44398 -0.05008 -0.01977 0.03236  414 VAL   A O    
1990 C  CB   . VAL   A 262 ? 0.33536 0.46511 0.39381 -0.02952 -0.00596 0.00976  414 VAL   A CB   
1991 C  CG1  . VAL   A 262 ? 0.34170 0.48023 0.38943 -0.03540 -0.00094 0.01580  414 VAL   A CG1  
1992 C  CG2  . VAL   A 262 ? 0.34274 0.45789 0.39069 -0.02003 -0.00568 -0.00089 414 VAL   A CG2  
1993 N  N    . LEU   A 263 ? 0.33780 0.47866 0.43348 -0.05094 -0.01631 0.03133  415 LEU   A N    
1994 C  CA   . LEU   A 263 ? 0.31753 0.46493 0.42851 -0.06316 -0.01791 0.04585  415 LEU   A CA   
1995 C  C    . LEU   A 263 ? 0.35785 0.48099 0.48020 -0.06828 -0.02837 0.04561  415 LEU   A C    
1996 O  O    . LEU   A 263 ? 0.41841 0.53434 0.55017 -0.07592 -0.03111 0.05794  415 LEU   A O    
1997 C  CB   . LEU   A 263 ? 0.30587 0.47972 0.43584 -0.06839 -0.01463 0.05077  415 LEU   A CB   
1998 C  CG   . LEU   A 263 ? 0.31035 0.51451 0.43526 -0.06511 -0.00203 0.05192  415 LEU   A CG   
1999 C  CD1  . LEU   A 263 ? 0.30279 0.53325 0.45016 -0.06668 0.00042  0.05234  415 LEU   A CD1  
2000 C  CD2  . LEU   A 263 ? 0.31980 0.53781 0.43765 -0.07424 0.00380  0.06706  415 LEU   A CD2  
2001 N  N    . GLU   A 264 ? 0.35483 0.46651 0.47786 -0.06420 -0.03439 0.03162  416 GLU   A N    
2002 C  CA   . GLU   A 264 ? 0.43098 0.52155 0.56480 -0.06845 -0.04307 0.02573  416 GLU   A CA   
2003 C  C    . GLU   A 264 ? 0.42203 0.49309 0.54482 -0.06354 -0.04343 0.02407  416 GLU   A C    
2004 O  O    . GLU   A 264 ? 0.44146 0.49737 0.57920 -0.06787 -0.04790 0.02788  416 GLU   A O    
2005 C  CB   . GLU   A 264 ? 0.49683 0.58731 0.63039 -0.06639 -0.04891 0.00987  416 GLU   A CB   
2006 C  CG   . GLU   A 264 ? 0.55631 0.63284 0.70691 -0.07403 -0.05748 0.00018  416 GLU   A CG   
2007 C  CD   . GLU   A 264 ? 0.50912 0.59085 0.65336 -0.07275 -0.06338 -0.01685 416 GLU   A CD   
2008 O  OE1  . GLU   A 264 ? 0.49998 0.57181 0.62901 -0.06717 -0.06411 -0.02870 416 GLU   A OE1  
2009 O  OE2  . GLU   A 264 ? 0.50775 0.60704 0.66230 -0.07802 -0.06745 -0.01747 416 GLU   A OE2  
2010 N  N    . VAL   A 265 ? 0.34695 0.41824 0.44725 -0.05454 -0.03910 0.01887  417 VAL   A N    
2011 C  CA   . VAL   A 265 ? 0.34890 0.40506 0.43985 -0.04999 -0.03979 0.01586  417 VAL   A CA   
2012 C  C    . VAL   A 265 ? 0.49405 0.55361 0.58394 -0.05237 -0.03749 0.03142  417 VAL   A C    
2013 O  O    . VAL   A 265 ? 0.50153 0.54937 0.60214 -0.05368 -0.04176 0.03725  417 VAL   A O    
2014 C  CB   . VAL   A 265 ? 0.33608 0.39159 0.40554 -0.04160 -0.03691 0.00513  417 VAL   A CB   
2015 C  CG1  . VAL   A 265 ? 0.35148 0.39646 0.41202 -0.03798 -0.03656 0.00368  417 VAL   A CG1  
2016 C  CG2  . VAL   A 265 ? 0.37383 0.42823 0.44338 -0.04043 -0.04097 -0.00721 417 VAL   A CG2  
2017 N  N    . PHE   A 266 ? 0.44458 0.52248 0.52261 -0.05277 -0.03092 0.03807  418 PHE   A N    
2018 C  CA   . PHE   A 266 ? 0.46173 0.54933 0.53297 -0.05604 -0.02877 0.05209  418 PHE   A CA   
2019 C  C    . PHE   A 266 ? 0.49867 0.59604 0.58742 -0.06647 -0.03042 0.07222  418 PHE   A C    
2020 O  O    . PHE   A 266 ? 0.51817 0.62015 0.60677 -0.07059 -0.03244 0.08844  418 PHE   A O    
2021 C  CB   . PHE   A 266 ? 0.41346 0.51922 0.46327 -0.05289 -0.02019 0.04719  418 PHE   A CB   
2022 C  CG   . PHE   A 266 ? 0.38518 0.47993 0.41881 -0.04466 -0.01923 0.03215  418 PHE   A CG   
2023 C  CD1  . PHE   A 266 ? 0.40066 0.50537 0.41947 -0.04072 -0.01202 0.02282  418 PHE   A CD1  
2024 C  CD2  . PHE   A 266 ? 0.44181 0.51701 0.47746 -0.04133 -0.02501 0.02672  418 PHE   A CD2  
2025 C  CE1  . PHE   A 266 ? 0.47567 0.56820 0.48299 -0.03481 -0.01172 0.01070  418 PHE   A CE1  
2026 C  CE2  . PHE   A 266 ? 0.48750 0.55501 0.50956 -0.03569 -0.02379 0.01534  418 PHE   A CE2  
2027 C  CZ   . PHE   A 266 ? 0.49753 0.57226 0.50589 -0.03304 -0.01772 0.00851  418 PHE   A CZ   
2028 N  N    . GLY   A 267 ? 0.47356 0.57614 0.57854 -0.07177 -0.03036 0.07351  419 GLY   A N    
2029 C  CA   . GLY   A 267 ? 0.49122 0.60302 0.61626 -0.08375 -0.03199 0.09422  419 GLY   A CA   
2030 C  C    . GLY   A 267 ? 0.53734 0.67922 0.66255 -0.08906 -0.02383 0.09852  419 GLY   A C    
2031 O  O    . GLY   A 267 ? 0.46012 0.61948 0.56696 -0.08276 -0.01541 0.08854  419 GLY   A O    
2032 N  N    . ASN   A 268 ? 0.58598 0.73421 0.73560 -0.10085 -0.02611 0.11283  420 ASN   A N    
2033 C  CA   . ASN   A 268 ? 0.65060 0.83199 0.80551 -0.10757 -0.01793 0.11917  420 ASN   A CA   
2034 C  C    . ASN   A 268 ? 0.68517 0.89003 0.84206 -0.12025 -0.01420 0.14685  420 ASN   A C    
2035 O  O    . ASN   A 268 ? 0.71519 0.90686 0.89118 -0.13014 -0.02201 0.16680  420 ASN   A O    
2036 C  CB   . ASN   A 268 ? 0.73025 0.90813 0.91277 -0.11371 -0.02302 0.11484  420 ASN   A CB   
2037 C  CG   . ASN   A 268 ? 0.77579 0.98851 0.96229 -0.11445 -0.01428 0.11163  420 ASN   A CG   
2038 O  OD1  . ASN   A 268 ? 0.80258 1.01567 1.00174 -0.11254 -0.01779 0.09915  420 ASN   A OD1  
2039 N  ND2  . ASN   A 268 ? 0.77961 1.02518 0.95624 -0.11722 -0.00291 0.12244  420 ASN   A ND2  
2040 N  N    . ASN   B 2   ? 1.08138 1.04538 1.37984 -0.17246 -0.02813 -0.02657 626 ASN   C N    
2041 C  CA   . ASN   B 2   ? 1.05467 1.02876 1.33411 -0.16156 -0.01964 0.01851  626 ASN   C CA   
2042 C  C    . ASN   B 2   ? 0.90439 0.93929 1.14931 -0.13708 -0.01311 0.01177  626 ASN   C C    
2043 O  O    . ASN   B 2   ? 0.89850 0.98305 1.13007 -0.14191 -0.00345 0.03420  626 ASN   C O    
2044 C  CB   . ASN   B 2   ? 1.13946 1.04566 1.42450 -0.14168 -0.02721 0.03383  626 ASN   C CB   
2045 C  CG   . ASN   B 2   ? 1.20236 1.10848 1.47621 -0.14330 -0.02336 0.09147  626 ASN   C CG   
2046 O  OD1  . ASN   B 2   ? 1.19687 1.14679 1.46259 -0.16703 -0.01255 0.12063  626 ASN   C OD1  
2047 N  ND2  . ASN   B 2   ? 1.24693 1.11017 1.52036 -0.11694 -0.03246 0.10802  626 ASN   C ND2  
2048 N  N    . HIS   B 3   ? 0.75228 0.78491 0.98418 -0.11162 -0.01742 -0.02074 627 HIS   C N    
2049 C  CA   . HIS   B 3   ? 0.63102 0.71152 0.83647 -0.09079 -0.01275 -0.02913 627 HIS   C CA   
2050 C  C    . HIS   B 3   ? 0.56176 0.66463 0.76268 -0.08987 -0.01621 -0.06415 627 HIS   C C    
2051 O  O    . HIS   B 3   ? 0.57240 0.67027 0.75976 -0.07104 -0.01755 -0.08510 627 HIS   C O    
2052 C  CB   . HIS   B 3   ? 0.59827 0.66279 0.79209 -0.06224 -0.01371 -0.02707 627 HIS   C CB   
2053 C  CG   . HIS   B 3   ? 0.61722 0.65985 0.81380 -0.05893 -0.01570 0.00900  627 HIS   C CG   
2054 N  ND1  . HIS   B 3   ? 0.67699 0.66044 0.89449 -0.05601 -0.02346 0.01807  627 HIS   C ND1  
2055 C  CD2  . HIS   B 3   ? 0.61506 0.68832 0.79472 -0.05655 -0.01284 0.03873  627 HIS   C CD2  
2056 C  CE1  . HIS   B 3   ? 0.66412 0.64172 0.87669 -0.05167 -0.02650 0.05831  627 HIS   C CE1  
2057 N  NE2  . HIS   B 3   ? 0.63092 0.66661 0.81714 -0.05286 -0.01983 0.07054  627 HIS   C NE2  
2058 N  N    . PRO   B 4   ? 0.54750 0.68209 0.75970 -0.10985 -0.01784 -0.06909 628 PRO   C N    
2059 C  CA   . PRO   B 4   ? 0.51851 0.67575 0.72522 -0.10837 -0.02613 -0.09946 628 PRO   C CA   
2060 C  C    . PRO   B 4   ? 0.47826 0.66900 0.66075 -0.08616 -0.02428 -0.10139 628 PRO   C C    
2061 O  O    . PRO   B 4   ? 0.47926 0.67475 0.64519 -0.07718 -0.03015 -0.12084 628 PRO   C O    
2062 C  CB   . PRO   B 4   ? 0.52437 0.71455 0.75806 -0.13528 -0.03002 -0.09942 628 PRO   C CB   
2063 C  CG   . PRO   B 4   ? 0.54672 0.75399 0.79016 -0.14415 -0.01732 -0.06645 628 PRO   C CG   
2064 C  CD   . PRO   B 4   ? 0.56452 0.72240 0.79689 -0.13529 -0.01252 -0.04661 628 PRO   C CD   
2065 N  N    . MET   B 5   ? 0.48514 0.69926 0.66469 -0.07809 -0.01658 -0.08212 629 MET   C N    
2066 C  CA   . MET   B 5   ? 0.42115 0.65769 0.58543 -0.05891 -0.01636 -0.08455 629 MET   C CA   
2067 C  C    . MET   B 5   ? 0.49866 0.71000 0.64527 -0.04272 -0.01295 -0.08675 629 MET   C C    
2068 O  O    . MET   B 5   ? 0.41416 0.63171 0.54672 -0.03300 -0.01454 -0.09398 629 MET   C O    
2069 C  CB   . MET   B 5   ? 0.39961 0.66872 0.57098 -0.05497 -0.01000 -0.07216 629 MET   C CB   
2070 C  CG   . MET   B 5   ? 0.49164 0.80357 0.68545 -0.06571 -0.01175 -0.07468 629 MET   C CG   
2071 S  SD   . MET   B 5   ? 0.51473 0.87362 0.71887 -0.06011 0.00023  -0.06751 629 MET   C SD   
2072 C  CE   . MET   B 5   ? 0.54079 0.89229 0.74214 -0.08187 0.01232  -0.04417 629 MET   C CE   
2073 N  N    . LEU   B 6   ? 0.45766 0.64466 0.60692 -0.03995 -0.00844 -0.07771 630 LEU   C N    
2074 C  CA   . LEU   B 6   ? 0.44636 0.61621 0.58855 -0.02450 -0.00545 -0.08291 630 LEU   C CA   
2075 C  C    . LEU   B 6   ? 0.45935 0.61415 0.59583 -0.02319 -0.00674 -0.10585 630 LEU   C C    
2076 O  O    . LEU   B 6   ? 0.47638 0.64027 0.60059 -0.01251 -0.00185 -0.11508 630 LEU   C O    
2077 C  CB   . LEU   B 6   ? 0.49374 0.64296 0.64521 -0.01964 -0.00486 -0.06785 630 LEU   C CB   
2078 C  CG   . LEU   B 6   ? 0.59761 0.74045 0.75201 -0.00088 -0.00308 -0.07047 630 LEU   C CG   
2079 C  CD1  . LEU   B 6   ? 0.57985 0.75085 0.72642 0.00587  0.00182  -0.07785 630 LEU   C CD1  
2080 C  CD2  . LEU   B 6   ? 0.59539 0.73490 0.75580 0.00490  -0.00720 -0.04758 630 LEU   C CD2  
2081 N  N    A MET   B 7   ? 0.49069 0.62536 0.63681 -0.03580 -0.01251 -0.11689 631 MET   C N    
2082 N  N    B MET   B 7   ? 0.49191 0.62700 0.63778 -0.03585 -0.01255 -0.11713 631 MET   C N    
2083 C  CA   A MET   B 7   ? 0.53369 0.65702 0.67323 -0.03515 -0.01534 -0.14757 631 MET   C CA   
2084 C  CA   B MET   B 7   ? 0.53285 0.65647 0.67180 -0.03437 -0.01501 -0.14774 631 MET   C CA   
2085 C  C    A MET   B 7   ? 0.51165 0.67211 0.62483 -0.03451 -0.01746 -0.15771 631 MET   C C    
2086 C  C    B MET   B 7   ? 0.51282 0.67332 0.62577 -0.03461 -0.01758 -0.15824 631 MET   C C    
2087 O  O    A MET   B 7   ? 0.51983 0.68901 0.61267 -0.02476 -0.01256 -0.17445 631 MET   C O    
2088 O  O    B MET   B 7   ? 0.52182 0.69104 0.61424 -0.02539 -0.01315 -0.17601 631 MET   C O    
2089 C  CB   A MET   B 7   ? 0.61389 0.70932 0.77432 -0.05401 -0.02439 -0.15957 631 MET   C CB   
2090 C  CB   B MET   B 7   ? 0.61546 0.70781 0.77550 -0.05164 -0.02368 -0.16112 631 MET   C CB   
2091 C  CG   A MET   B 7   ? 0.72666 0.80930 0.88247 -0.05462 -0.02992 -0.20064 631 MET   C CG   
2092 C  CG   B MET   B 7   ? 0.73513 0.77984 0.91134 -0.04194 -0.02341 -0.17959 631 MET   C CG   
2093 S  SD   A MET   B 7   ? 0.85402 0.86731 1.04785 -0.06016 -0.03519 -0.21598 631 MET   C SD   
2094 S  SD   B MET   B 7   ? 0.84544 0.84767 1.04897 -0.06494 -0.03633 -0.20767 631 MET   C SD   
2095 C  CE   A MET   B 7   ? 0.80743 0.80280 1.00286 -0.02632 -0.02403 -0.21245 631 MET   C CE   
2096 C  CE   B MET   B 7   ? 0.84070 0.81970 1.07405 -0.08753 -0.03783 -0.16094 631 MET   C CE   
2097 N  N    . ASN   B 8   ? 0.48746 0.67419 0.60128 -0.04376 -0.02464 -0.14598 632 ASN   C N    
2098 C  CA   . ASN   B 8   ? 0.48735 0.70764 0.57804 -0.04133 -0.03149 -0.14925 632 ASN   C CA   
2099 C  C    . ASN   B 8   ? 0.48332 0.71308 0.55493 -0.02667 -0.02228 -0.13396 632 ASN   C C    
2100 O  O    . ASN   B 8   ? 0.50770 0.75485 0.55111 -0.02272 -0.02253 -0.13764 632 ASN   C O    
2101 C  CB   . ASN   B 8   ? 0.47230 0.72031 0.57864 -0.04971 -0.04254 -0.13889 632 ASN   C CB   
2102 C  CG   . ASN   B 8   ? 0.56694 0.84833 0.65292 -0.04255 -0.05377 -0.13513 632 ASN   C CG   
2103 O  OD1  . ASN   B 8   ? 0.57302 0.86433 0.65936 -0.03123 -0.05307 -0.11456 632 ASN   C OD1  
2104 N  ND2  . ASN   B 8   ? 0.62431 0.92207 0.69278 -0.04857 -0.06628 -0.15529 632 ASN   C ND2  
2105 N  N    A LEU   B 9   ? 0.44511 0.66641 0.53138 -0.02074 -0.01436 -0.11619 633 LEU   C N    
2106 N  N    B LEU   B 9   ? 0.44502 0.66648 0.53129 -0.02075 -0.01442 -0.11610 633 LEU   C N    
2107 C  CA   A LEU   B 9   ? 0.43491 0.66231 0.51254 -0.01150 -0.00611 -0.10307 633 LEU   C CA   
2108 C  CA   B LEU   B 9   ? 0.43491 0.66234 0.51251 -0.01150 -0.00612 -0.10305 633 LEU   C CA   
2109 C  C    A LEU   B 9   ? 0.45032 0.67435 0.51878 -0.00596 0.00635  -0.11407 633 LEU   C C    
2110 C  C    B LEU   B 9   ? 0.45075 0.67500 0.51879 -0.00602 0.00628  -0.11424 633 LEU   C C    
2111 O  O    A LEU   B 9   ? 0.45912 0.69714 0.51622 -0.00325 0.01485  -0.10499 633 LEU   C O    
2112 O  O    B LEU   B 9   ? 0.46018 0.69878 0.51599 -0.00341 0.01465  -0.10541 633 LEU   C O    
2113 C  CB   A LEU   B 9   ? 0.40683 0.63019 0.50566 -0.00806 -0.00369 -0.08881 633 LEU   C CB   
2114 C  CB   B LEU   B 9   ? 0.40690 0.62999 0.50580 -0.00804 -0.00355 -0.08896 633 LEU   C CB   
2115 C  CG   A LEU   B 9   ? 0.40960 0.64585 0.52001 -0.00885 -0.01223 -0.08095 633 LEU   C CG   
2116 C  CG   B LEU   B 9   ? 0.40834 0.64407 0.51913 -0.00905 -0.01198 -0.08126 633 LEU   C CG   
2117 C  CD1  A LEU   B 9   ? 0.39025 0.62697 0.51764 -0.00486 -0.00848 -0.07582 633 LEU   C CD1  
2118 C  CD1  B LEU   B 9   ? 0.38724 0.62346 0.51401 -0.00397 -0.00829 -0.07519 633 LEU   C CD1  
2119 C  CD2  A LEU   B 9   ? 0.41140 0.65776 0.51250 -0.00413 -0.01917 -0.07170 633 LEU   C CD2  
2120 C  CD2  B LEU   B 9   ? 0.40667 0.65483 0.50728 -0.00550 -0.02041 -0.07406 633 LEU   C CD2  
2121 N  N    . LEU   B 10  ? 0.46493 0.67150 0.54261 -0.00421 0.00821  -0.13298 634 LEU   C N    
2122 C  CA   . LEU   B 10  ? 0.52151 0.72958 0.59762 0.00567  0.02032  -0.15039 634 LEU   C CA   
2123 C  C    . LEU   B 10  ? 0.57209 0.79657 0.61927 0.00467  0.02225  -0.17574 634 LEU   C C    
2124 O  O    . LEU   B 10  ? 0.55644 0.79660 0.59688 0.01373  0.03629  -0.19245 634 LEU   C O    
2125 C  CB   . LEU   B 10  ? 0.51867 0.69583 0.62357 0.01323  0.01923  -0.15989 634 LEU   C CB   
2126 C  CG   . LEU   B 10  ? 0.48368 0.65838 0.61152 0.02066  0.02082  -0.13887 634 LEU   C CG   
2127 C  CD1  . LEU   B 10  ? 0.52128 0.66266 0.67447 0.02880  0.01487  -0.14000 634 LEU   C CD1  
2128 C  CD2  . LEU   B 10  ? 0.52113 0.72532 0.65179 0.02928  0.03399  -0.13950 634 LEU   C CD2  
2129 N  N    . LYS   B 11  ? 0.58351 0.81262 0.61435 -0.00565 0.00844  -0.18146 635 LYS   C N    
2130 C  CA   . LYS   B 11  ? 0.69881 0.95036 0.69645 -0.00774 0.00577  -0.20865 635 LYS   C CA   
2131 C  C    . LYS   B 11  ? 0.76638 1.05771 0.72676 -0.00383 0.01851  -0.19692 635 LYS   C C    
2132 O  O    . LYS   B 11  ? 0.80512 1.10929 0.75463 -0.00735 0.01553  -0.16263 635 LYS   C O    
2133 C  CB   . LYS   B 11  ? 0.74745 1.00655 0.73853 -0.02067 -0.01566 -0.21089 635 LYS   C CB   
2134 C  CG   . LYS   B 11  ? 0.83265 1.09824 0.80886 -0.02655 -0.02552 -0.25436 635 LYS   C CG   
2135 C  CD   . LYS   B 11  ? 0.83784 1.12894 0.80525 -0.03947 -0.04883 -0.25364 635 LYS   C CD   
2136 C  CE   . LYS   B 11  ? 0.87657 1.19966 0.80573 -0.04260 -0.05912 -0.29308 635 LYS   C CE   
2137 N  NZ   . LYS   B 11  ? 0.91144 1.28440 0.78691 -0.03581 -0.05993 -0.27192 635 LYS   C NZ   
2138 C  C10  . A1L79 C .   ? 0.46217 0.51906 0.40136 -0.04056 -0.00069 -0.07561 501 A1L79 A C10  
2139 C  C13  . A1L79 C .   ? 0.61893 0.73907 0.55647 -0.03722 0.01117  -0.05270 501 A1L79 A C13  
2140 C  C15  . A1L79 C .   ? 0.50615 0.61045 0.46825 -0.02200 0.01956  -0.06407 501 A1L79 A C15  
2141 C  C20  . A1L79 C .   ? 0.46717 0.62476 0.45710 -0.03396 0.01701  -0.00789 501 A1L79 A C20  
2142 C  C21  . A1L79 C .   ? 0.49398 0.64228 0.49563 -0.02332 0.02040  -0.02114 501 A1L79 A C21  
2143 C  C22  . A1L79 C .   ? 0.49196 0.69334 0.45782 -0.03843 0.03338  -0.02551 501 A1L79 A C22  
2144 C  C26  . A1L79 C .   ? 0.63255 0.59008 0.63399 -0.01611 -0.01411 -0.02524 501 A1L79 A C26  
2145 C  C28  . A1L79 C .   ? 0.55327 0.51926 0.55855 -0.00971 -0.01761 -0.01375 501 A1L79 A C28  
2146 C  C01  . A1L79 C .   ? 0.49064 0.47030 0.48106 -0.01719 0.00102  -0.07295 501 A1L79 A C01  
2147 C  C02  . A1L79 C .   ? 0.49446 0.47998 0.48565 -0.01360 -0.00218 -0.05796 501 A1L79 A C02  
2148 C  C03  . A1L79 C .   ? 0.47022 0.47495 0.45424 -0.01406 -0.00172 -0.05443 501 A1L79 A C03  
2149 C  C04  . A1L79 C .   ? 0.45600 0.47668 0.43040 -0.01822 0.00157  -0.06179 501 A1L79 A C04  
2150 C  C05  . A1L79 C .   ? 0.44168 0.46116 0.41157 -0.02190 0.00476  -0.07664 501 A1L79 A C05  
2151 C  C06  . A1L79 C .   ? 0.47380 0.47179 0.45235 -0.02135 0.00454  -0.08379 501 A1L79 A C06  
2152 C  C09  . A1L79 C .   ? 0.55432 0.63299 0.50399 -0.02807 0.01209  -0.07428 501 A1L79 A C09  
2153 C  C11  . A1L79 C .   ? 0.54956 0.59928 0.49922 -0.03194 0.01541  -0.11465 501 A1L79 A C11  
2154 C  C12  . A1L79 C .   ? 0.57151 0.67075 0.50904 -0.03583 0.00912  -0.06436 501 A1L79 A C12  
2155 C  C14  . A1L79 C .   ? 0.51325 0.63578 0.46308 -0.03090 0.01675  -0.05285 501 A1L79 A C14  
2156 C  C16  . A1L79 C .   ? 0.60395 0.68506 0.56629 -0.02038 0.01695  -0.07365 501 A1L79 A C16  
2157 C  C18  . A1L79 C .   ? 0.53692 0.68126 0.50496 -0.02951 0.02049  -0.03438 501 A1L79 A C18  
2158 C  C19  . A1L79 C .   ? 0.43085 0.59972 0.40095 -0.03702 0.02132  -0.01729 501 A1L79 A C19  
2159 C  C23  . A1L79 C .   ? 0.45640 0.68214 0.42950 -0.04620 0.03474  -0.00588 501 A1L79 A C23  
2160 C  C25  . A1L79 C .   ? 0.69969 0.65605 0.70490 -0.01329 -0.00875 -0.04206 501 A1L79 A C25  
2161 C  C29  . A1L79 C .   ? 0.53852 0.49669 0.54913 -0.01073 -0.02259 0.00227  501 A1L79 A C29  
2162 C  C30  . A1L79 C .   ? 0.58890 0.56392 0.59011 -0.01255 -0.02761 0.01469  501 A1L79 A C30  
2163 C  C33  . A1L79 C .   ? 0.47804 0.48785 0.46513 -0.01146 -0.00569 -0.04139 501 A1L79 A C33  
2164 C  C34  . A1L79 C .   ? 0.66187 0.80335 0.58866 -0.04633 0.00629  -0.03751 501 A1L79 A C34  
2165 C  C35  . A1L79 C .   ? 0.64260 0.70269 0.59990 -0.02398 0.02504  -0.12613 501 A1L79 A C35  
2166 C  C36  . A1L79 C .   ? 0.67313 0.70919 0.65288 -0.01295 0.02429  -0.11945 501 A1L79 A C36  
2167 C  C37  . A1L79 C .   ? 0.47376 0.52062 0.42010 -0.03827 -0.00635 -0.05924 501 A1L79 A C37  
2168 C  C38  . A1L79 C .   ? 0.47907 0.54081 0.42535 -0.03755 -0.00815 -0.04557 501 A1L79 A C38  
2169 O  O07  . A1L79 C .   ? 0.59403 0.56837 0.59362 -0.01040 -0.00646 -0.04545 501 A1L79 A O07  
2170 O  O17  . A1L79 C .   ? 0.58424 0.72961 0.53566 -0.03448 0.01891  -0.03999 501 A1L79 A O17  
2171 O  O24  . A1L79 C .   ? 0.45650 0.63044 0.41787 -0.04569 0.01479  -0.00211 501 A1L79 A O24  
2172 O  O27  . A1L79 C .   ? 0.65304 0.62272 0.64115 -0.02238 -0.01445 -0.02623 501 A1L79 A O27  
2173 O  O31  . A1L79 C .   ? 0.54782 0.53631 0.53707 -0.01585 -0.02682 0.00932  501 A1L79 A O31  
2174 O  O32  . A1L79 C .   ? 0.49070 0.46686 0.49688 -0.01124 -0.03284 0.02983  501 A1L79 A O32  
2175 SI SI08 . A1L79 C .   ? 0.47516 0.52529 0.42696 -0.02973 0.00833  -0.08539 501 A1L79 A SI08 
# 
