data_9M19
# 
_entry.id   9M19 
# 
_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   9M19         pdb_00009m19 10.2210/pdb9m19/pdb 
WWPDB D_1300056791 ?            ?                   
# 
_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                        9M19 
_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-[dibutyl-[4-(2-ethyl-2-oxidanyl-butoxy)-3-methyl-phenyl]silyl]-2-methyl-phenoxy]-4-oxidanyl-pentanoic acid' 572.848 
1  ? ? ? ? 
4 water       nat water 18.015    93 ? ? ? ? 
# 
_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-[dibutyl-[4-(2-ethyl-2-oxidanyl-butoxy)-3-methyl-phenyl]silyl]-2-methyl-phenoxy]-4-oxidanyl-pentanoic acid' A1L77 
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 
A1L77 non-polymer         . 
'(4~{S})-5-[4-[dibutyl-[4-(2-ethyl-2-oxidanyl-butoxy)-3-methyl-phenyl]silyl]-2-methyl-phenoxy]-4-oxidanyl-pentanoic acid' ? 
'C33 H52 O6 Si'  572.848 
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  206 ?   ?   ?   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   625 625 LYS LYS C . n 
B 2 2   ASN 2   626 626 ASN ASN C . n 
B 2 3   HIS 3   627 627 HIS HIS C . n 
B 2 4   PRO 4   628 628 PRO PRO C . n 
B 2 5   MET 5   629 629 MET MET C . n 
B 2 6   LEU 6   630 630 LEU LEU C . n 
B 2 7   MET 7   631 631 MET MET C . n 
B 2 8   ASN 8   632 632 ASN ASN C . n 
B 2 9   LEU 9   633 633 LEU LEU C . n 
B 2 10  LEU 10  634 634 LEU LEU C . n 
B 2 11  LYS 11  635 635 LYS LYS C . n 
B 2 12  ASP 12  636 ?   ?   ?   C . n 
B 2 13  ASN 13  637 ?   ?   ?   C . n 
# 
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 A1L77 1  501 501 A1L77 LIG A . 
D 4 HOH   1  601 17  HOH   HOH A . 
D 4 HOH   2  602 61  HOH   HOH A . 
D 4 HOH   3  603 4   HOH   HOH A . 
D 4 HOH   4  604 13  HOH   HOH A . 
D 4 HOH   5  605 56  HOH   HOH A . 
D 4 HOH   6  606 15  HOH   HOH A . 
D 4 HOH   7  607 43  HOH   HOH A . 
D 4 HOH   8  608 92  HOH   HOH A . 
D 4 HOH   9  609 16  HOH   HOH A . 
D 4 HOH   10 610 99  HOH   HOH A . 
D 4 HOH   11 611 83  HOH   HOH A . 
D 4 HOH   12 612 5   HOH   HOH A . 
D 4 HOH   13 613 40  HOH   HOH A . 
D 4 HOH   14 614 74  HOH   HOH A . 
D 4 HOH   15 615 98  HOH   HOH A . 
D 4 HOH   16 616 18  HOH   HOH A . 
D 4 HOH   17 617 32  HOH   HOH A . 
D 4 HOH   18 618 66  HOH   HOH A . 
D 4 HOH   19 619 7   HOH   HOH A . 
D 4 HOH   20 620 3   HOH   HOH A . 
D 4 HOH   21 621 55  HOH   HOH A . 
D 4 HOH   22 622 54  HOH   HOH A . 
D 4 HOH   23 623 1   HOH   HOH A . 
D 4 HOH   24 624 19  HOH   HOH A . 
D 4 HOH   25 625 60  HOH   HOH A . 
D 4 HOH   26 626 41  HOH   HOH A . 
D 4 HOH   27 627 10  HOH   HOH A . 
D 4 HOH   28 628 91  HOH   HOH A . 
D 4 HOH   29 629 24  HOH   HOH A . 
D 4 HOH   30 630 9   HOH   HOH A . 
D 4 HOH   31 631 2   HOH   HOH A . 
D 4 HOH   32 632 62  HOH   HOH A . 
D 4 HOH   33 633 80  HOH   HOH A . 
D 4 HOH   34 634 8   HOH   HOH A . 
D 4 HOH   35 635 6   HOH   HOH A . 
D 4 HOH   36 636 64  HOH   HOH A . 
D 4 HOH   37 637 67  HOH   HOH A . 
D 4 HOH   38 638 86  HOH   HOH A . 
D 4 HOH   39 639 49  HOH   HOH A . 
D 4 HOH   40 640 35  HOH   HOH A . 
D 4 HOH   41 641 51  HOH   HOH A . 
D 4 HOH   42 642 22  HOH   HOH A . 
D 4 HOH   43 643 23  HOH   HOH A . 
D 4 HOH   44 644 12  HOH   HOH A . 
D 4 HOH   45 645 88  HOH   HOH A . 
D 4 HOH   46 646 36  HOH   HOH A . 
D 4 HOH   47 647 58  HOH   HOH A . 
D 4 HOH   48 648 85  HOH   HOH A . 
D 4 HOH   49 649 27  HOH   HOH A . 
D 4 HOH   50 650 96  HOH   HOH A . 
D 4 HOH   51 651 93  HOH   HOH A . 
D 4 HOH   52 652 72  HOH   HOH A . 
D 4 HOH   53 653 71  HOH   HOH A . 
D 4 HOH   54 654 14  HOH   HOH A . 
D 4 HOH   55 655 37  HOH   HOH A . 
D 4 HOH   56 656 81  HOH   HOH A . 
D 4 HOH   57 657 70  HOH   HOH A . 
D 4 HOH   58 658 30  HOH   HOH A . 
D 4 HOH   59 659 57  HOH   HOH A . 
D 4 HOH   60 660 29  HOH   HOH A . 
D 4 HOH   61 661 52  HOH   HOH A . 
D 4 HOH   62 662 65  HOH   HOH A . 
D 4 HOH   63 663 31  HOH   HOH A . 
D 4 HOH   64 664 73  HOH   HOH A . 
D 4 HOH   65 665 87  HOH   HOH A . 
D 4 HOH   66 666 77  HOH   HOH A . 
D 4 HOH   67 667 95  HOH   HOH A . 
D 4 HOH   68 668 78  HOH   HOH A . 
D 4 HOH   69 669 63  HOH   HOH A . 
D 4 HOH   70 670 47  HOH   HOH A . 
D 4 HOH   71 671 59  HOH   HOH A . 
D 4 HOH   72 672 33  HOH   HOH A . 
D 4 HOH   73 673 89  HOH   HOH A . 
D 4 HOH   74 674 82  HOH   HOH A . 
D 4 HOH   75 675 69  HOH   HOH A . 
D 4 HOH   76 676 94  HOH   HOH A . 
D 4 HOH   77 677 11  HOH   HOH A . 
D 4 HOH   78 678 21  HOH   HOH A . 
D 4 HOH   79 679 50  HOH   HOH A . 
D 4 HOH   80 680 45  HOH   HOH A . 
D 4 HOH   81 681 84  HOH   HOH A . 
D 4 HOH   82 682 42  HOH   HOH A . 
D 4 HOH   83 683 53  HOH   HOH A . 
D 4 HOH   84 684 25  HOH   HOH A . 
D 4 HOH   85 685 26  HOH   HOH A . 
D 4 HOH   86 686 28  HOH   HOH A . 
D 4 HOH   87 687 75  HOH   HOH A . 
D 4 HOH   88 688 100 HOH   HOH A . 
D 4 HOH   89 689 20  HOH   HOH A . 
D 4 HOH   90 690 97  HOH   HOH A . 
D 4 HOH   91 691 90  HOH   HOH A . 
D 4 HOH   92 692 79  HOH   HOH A . 
E 4 HOH   1  701 76  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                   97.036 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9M19 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     154.694 
_cell.length_a_esd                 ? 
_cell.length_b                     42.192 
_cell.length_b_esd                 ? 
_cell.length_c                     42.576 
_cell.length_c_esd                 ? 
_cell.volume                       275794.472 
_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                         9M19 
_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                   9M19 
_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          42.62 
_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, Tacsimate pH 7.0, HEPES pH 7.5' 
_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         2024-03-12 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.98 
_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                        'PHOTON FACTORY BEAMLINE BL-17A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL-17A 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9M19 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.05 
_reflns.d_resolution_low                               42.26 
_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                                     17097 
_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                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.3 
_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                              0.054 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.05 
_reflns_shell.d_res_low                                     2.11 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1325 
_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                                  0.906 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.515 
_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                               49.04 
_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                                 9M19 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.05 
_refine.ls_d_res_low                             40.68 
_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                     17054 
_refine.ls_number_reflns_R_free                  854 
_refine.ls_number_reflns_R_work                  16200 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.12 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1944 
_refine.ls_R_factor_R_free                       0.2298 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1926 
_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                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      2ZLC 
_refine.pdbx_stereochemistry_target_values       'CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.4460 
_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                            0.2077 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.05 
_refine_hist.d_res_low                        40.68 
_refine_hist.number_atoms_solvent             93 
_refine_hist.number_atoms_total               2134 
_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        2001 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0056  ? 2127 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6764  ? 2877 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0379  ? 318  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0031  ? 366  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 26.8700 ? 825  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.05 2.18  . . 139 2635 97.37 . . . . 0.2553 . . . . . . . . . . . . . . . 0.2898 
'X-RAY DIFFRACTION' 2.18 2.35  . . 141 2667 97.53 . . . . 0.2270 . . . . . . . . . . . . . . . 0.2524 
'X-RAY DIFFRACTION' 2.35 2.58  . . 141 2687 98.37 . . . . 0.2083 . . . . . . . . . . . . . . . 0.2664 
'X-RAY DIFFRACTION' 2.58 2.96  . . 142 2706 98.61 . . . . 0.1927 . . . . . . . . . . . . . . . 0.2162 
'X-RAY DIFFRACTION' 2.96 3.72  . . 143 2718 98.66 . . . . 0.1794 . . . . . . . . . . . . . . . 0.2178 
'X-RAY DIFFRACTION' 3.72 40.68 . . 148 2787 98.26 . . . . 0.1822 . . . . . . . . . . . . . . . 0.2206 
# 
_struct.entry_id                     9M19 
_struct.title                        'Vitamin D receptor complex with a dibutyldiphenylsilane 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        9M19 
_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 9M19 A 11 ? 271 ? P13053 116 ? 423 ? 116 423 
2 2 9M19 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 9M19 GLY A 1  ? UNP P13053 ?   ?   'expression tag' 106 1  
1 9M19 SER A 2  ? UNP P13053 ?   ?   'expression tag' 107 2  
1 9M19 HIS A 3  ? UNP P13053 ?   ?   'expression tag' 108 3  
1 9M19 MET A 4  ? UNP P13053 ?   ?   'expression tag' 109 4  
1 9M19 GLY A 5  ? UNP P13053 ?   ?   'expression tag' 110 5  
1 9M19 SER A 6  ? UNP P13053 ?   ?   'expression tag' 111 6  
1 9M19 PRO A 7  ? UNP P13053 ?   ?   'expression tag' 112 7  
1 9M19 ASN A 8  ? UNP P13053 ?   ?   'expression tag' 113 8  
1 9M19 SER A 9  ? UNP P13053 ?   ?   'expression tag' 114 9  
1 9M19 PRO A 10 ? UNP P13053 ?   ?   'expression tag' 115 10 
1 9M19 ?   A ?  ? UNP P13053 TYR 166 deletion         ?   11 
1 9M19 ?   A ?  ? UNP P13053 SER 167 deletion         ?   12 
1 9M19 ?   A ?  ? UNP P13053 PRO 168 deletion         ?   13 
1 9M19 ?   A ?  ? UNP P13053 ARG 169 deletion         ?   14 
1 9M19 ?   A ?  ? UNP P13053 PRO 170 deletion         ?   15 
1 9M19 ?   A ?  ? UNP P13053 THR 171 deletion         ?   16 
1 9M19 ?   A ?  ? UNP P13053 LEU 172 deletion         ?   17 
1 9M19 ?   A ?  ? UNP P13053 SER 173 deletion         ?   18 
1 9M19 ?   A ?  ? UNP P13053 PHE 174 deletion         ?   19 
1 9M19 ?   A ?  ? UNP P13053 SER 175 deletion         ?   20 
1 9M19 ?   A ?  ? UNP P13053 GLY 176 deletion         ?   21 
1 9M19 ?   A ?  ? UNP P13053 ASN 177 deletion         ?   22 
1 9M19 ?   A ?  ? UNP P13053 SER 178 deletion         ?   23 
1 9M19 ?   A ?  ? UNP P13053 SER 179 deletion         ?   24 
1 9M19 ?   A ?  ? UNP P13053 SER 180 deletion         ?   25 
1 9M19 ?   A ?  ? UNP P13053 SER 181 deletion         ?   26 
1 9M19 ?   A ?  ? UNP P13053 SER 182 deletion         ?   27 
1 9M19 ?   A ?  ? UNP P13053 SER 183 deletion         ?   28 
1 9M19 ?   A ?  ? UNP P13053 ASP 184 deletion         ?   29 
1 9M19 ?   A ?  ? UNP P13053 LEU 185 deletion         ?   30 
1 9M19 ?   A ?  ? UNP P13053 TYR 186 deletion         ?   31 
1 9M19 ?   A ?  ? UNP P13053 THR 187 deletion         ?   32 
1 9M19 ?   A ?  ? UNP P13053 THR 188 deletion         ?   33 
1 9M19 ?   A ?  ? UNP P13053 SER 189 deletion         ?   34 
1 9M19 ?   A ?  ? UNP P13053 LEU 190 deletion         ?   35 
1 9M19 ?   A ?  ? UNP P13053 ASP 191 deletion         ?   36 
1 9M19 ?   A ?  ? UNP P13053 MET 192 deletion         ?   37 
1 9M19 ?   A ?  ? UNP P13053 MET 193 deletion         ?   38 
1 9M19 ?   A ?  ? UNP P13053 GLU 194 deletion         ?   39 
1 9M19 ?   A ?  ? UNP P13053 PRO 195 deletion         ?   40 
1 9M19 ?   A ?  ? UNP P13053 SER 196 deletion         ?   41 
1 9M19 ?   A ?  ? UNP P13053 GLY 197 deletion         ?   42 
1 9M19 ?   A ?  ? UNP P13053 PHE 198 deletion         ?   43 
1 9M19 ?   A ?  ? UNP P13053 SER 199 deletion         ?   44 
1 9M19 ?   A ?  ? UNP P13053 ASN 200 deletion         ?   45 
1 9M19 ?   A ?  ? UNP P13053 LEU 201 deletion         ?   46 
1 9M19 ?   A ?  ? UNP P13053 ASP 202 deletion         ?   47 
1 9M19 ?   A ?  ? UNP P13053 LEU 203 deletion         ?   48 
1 9M19 ?   A ?  ? UNP P13053 ASN 204 deletion         ?   49 
1 9M19 ?   A ?  ? UNP P13053 GLY 205 deletion         ?   50 
1 9M19 ?   A ?  ? UNP P13053 GLU 206 deletion         ?   51 
1 9M19 ?   A ?  ? UNP P13053 ASP 207 deletion         ?   52 
1 9M19 ?   A ?  ? UNP P13053 SER 208 deletion         ?   53 
1 9M19 ?   A ?  ? UNP P13053 ASP 209 deletion         ?   54 
1 9M19 ?   A ?  ? UNP P13053 ASP 210 deletion         ?   55 
1 9M19 ?   A ?  ? UNP P13053 PRO 211 deletion         ?   56 
1 9M19 ?   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)' 1180  ? 
1 MORE         -8    ? 
1 'SSA (A^2)'  11660 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 20  ? TYR A 38  ? SER A 125 TYR A 143 1 ? 19 
HELX_P HELX_P2  AA2 TYR A 42  ? PHE A 48  ? TYR A 147 PHE A 153 5 ? 7  
HELX_P HELX_P3  AA3 MET A 70  ? MET A 91  ? MET A 222 MET A 243 1 ? 22 
HELX_P HELX_P4  AA4 GLY A 94  ? LEU A 98  ? GLY A 246 LEU A 250 5 ? 5  
HELX_P HELX_P5  AA5 THR A 99  ? ASN A 120 ? THR A 251 ASN A 272 1 ? 22 
HELX_P HELX_P6  AA6 SER A 134 ? ASP A 136 ? SER A 286 ASP A 288 5 ? 3  
HELX_P HELX_P7  AA7 ASP A 140 ? LYS A 146 ? ASP A 292 LYS A 298 1 ? 7  
HELX_P HELX_P8  AA8 THR A 150 ? LEU A 167 ? THR A 302 LEU A 319 1 ? 18 
HELX_P HELX_P9  AA9 HIS A 170 ? VAL A 183 ? HIS A 322 VAL A 335 1 ? 14 
HELX_P HELX_P10 AB1 ASP A 192 ? HIS A 215 ? ASP A 344 HIS A 367 1 ? 24 
HELX_P HELX_P11 AB2 GLN A 222 ? PHE A 250 ? GLN A 374 PHE A 402 1 ? 29 
HELX_P HELX_P12 AB3 GLN A 251 ? MET A 256 ? GLN A 403 MET A 408 1 ? 6  
HELX_P HELX_P13 AB4 THR A 259 ? GLY A 267 ? THR A 411 GLY A 419 1 ? 9  
HELX_P HELX_P14 AB5 HIS B 3   ? LEU B 10  ? HIS C 627 LEU C 634 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           217 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            369 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    218 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     370 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       2.25 
# 
_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                   9M19 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASP 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     292 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -124.05 
_pdbx_validate_torsion.psi             -168.01 
# 
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 18.7227371422 0.286063604114 19.4838247948 0.286496327282 ? -0.014827372606  ? -0.00575008655078 ? 
0.242435614387 ? -0.0230127690478 ? 0.244733906277 ? 3.2267315764     ? 0.593117499645    ? 0.324262740375   ? 0.746880504915  ? 
0.0671606260198  ? 1.2231102085    ? 0.0683771551535  ? -0.0220966786492 ? -0.212551823161 ? -0.00260370054572 ? -0.00997311531916 
? -0.0446197145558 ? -0.221121462821 ? 0.0778157623886 ? 0.00537773031256 ? 
2 'X-RAY DIFFRACTION' ? refined 5.47434975355 -10.4961689269 11.1309341426 0.363609753177 ? 0.00372456948321 ? 0.0165445335438   ? 
0.606110087971 ? -0.133566852228  ? 0.646894866356 ? 0.00118487260039 ? -4.3910766397e-05 ? -0.0133868972268 ? 0.0468397821733 ? 
-0.0455659218741 ? 0.0108482353531 ? -0.0952436471312 ? 0.288633879295   ? -0.429897744698 ? 0.149071773278    ? -0.508729135383   
? 0.297663179568   ? -0.265243104332 ? -0.101777219437 ? 1.7961070252e-05 ? 
# 
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 MET 206 ? A MET 54  
19 1 Y 1 A ASP 207 ? A ASP 55  
20 1 Y 1 A GLY 208 ? A GLY 56  
21 1 Y 1 A SER 209 ? A SER 57  
22 1 Y 1 A THR 210 ? A THR 58  
23 1 Y 1 A GLY 211 ? A GLY 59  
24 1 Y 1 A SER 212 ? A SER 60  
25 1 Y 1 A VAL 213 ? A VAL 61  
26 1 Y 1 A THR 214 ? A THR 62  
27 1 Y 1 A LEU 215 ? A LEU 63  
28 1 Y 1 A ASP 216 ? A ASP 64  
29 1 Y 1 A LEU 217 ? A LEU 65  
30 1 Y 1 A SER 218 ? A SER 66  
31 1 Y 1 A GLU 421 ? A GLU 269 
32 1 Y 1 A ILE 422 ? A ILE 270 
33 1 Y 1 A SER 423 ? A SER 271 
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 
A1L77 C10  C  N N 1   
A1L77 C13  C  Y N 2   
A1L77 C15  C  Y N 3   
A1L77 C17  C  N N 4   
A1L77 C20  C  N N 5   
A1L77 C21  C  N N 6   
A1L77 C22  C  N N 7   
A1L77 C24  C  N N 8   
A1L77 C28  C  N N 9   
A1L77 C01  C  Y N 10  
A1L77 C02  C  Y N 11  
A1L77 C03  C  Y N 12  
A1L77 C04  C  Y N 13  
A1L77 C05  C  Y N 14  
A1L77 C06  C  Y N 15  
A1L77 C09  C  Y N 16  
A1L77 C11  C  Y N 17  
A1L77 C12  C  Y N 18  
A1L77 C14  C  Y N 19  
A1L77 C18  C  N N 20  
A1L77 C19  C  N N 21  
A1L77 C25  C  N S 22  
A1L77 C27  C  N N 23  
A1L77 C29  C  N N 24  
A1L77 C32  C  N N 25  
A1L77 C33  C  N N 26  
A1L77 C34  C  N N 27  
A1L77 C35  C  N N 28  
A1L77 C36  C  N N 29  
A1L77 C37  C  N N 30  
A1L77 C38  C  N N 31  
A1L77 C39  C  N N 32  
A1L77 C40  C  N N 33  
A1L77 O07  O  N N 34  
A1L77 O16  O  N N 35  
A1L77 O23  O  N N 36  
A1L77 O26  O  N N 37  
A1L77 O30  O  N N 38  
A1L77 O31  O  N N 39  
A1L77 SI08 SI N N 40  
A1L77 H102 H  N N 41  
A1L77 H101 H  N N 42  
A1L77 H151 H  N N 43  
A1L77 H172 H  N N 44  
A1L77 H171 H  N N 45  
A1L77 H202 H  N N 46  
A1L77 H203 H  N N 47  
A1L77 H201 H  N N 48  
A1L77 H212 H  N N 49  
A1L77 H211 H  N N 50  
A1L77 H223 H  N N 51  
A1L77 H221 H  N N 52  
A1L77 H222 H  N N 53  
A1L77 H242 H  N N 54  
A1L77 H241 H  N N 55  
A1L77 H282 H  N N 56  
A1L77 H281 H  N N 57  
A1L77 H011 H  N N 58  
A1L77 H041 H  N N 59  
A1L77 H061 H  N N 60  
A1L77 H111 H  N N 61  
A1L77 H141 H  N N 62  
A1L77 H191 H  N N 63  
A1L77 H192 H  N N 64  
A1L77 H251 H  N N 65  
A1L77 H272 H  N N 66  
A1L77 H271 H  N N 67  
A1L77 H321 H  N N 68  
A1L77 H323 H  N N 69  
A1L77 H322 H  N N 70  
A1L77 H333 H  N N 71  
A1L77 H331 H  N N 72  
A1L77 H332 H  N N 73  
A1L77 H341 H  N N 74  
A1L77 H342 H  N N 75  
A1L77 H352 H  N N 76  
A1L77 H351 H  N N 77  
A1L77 H361 H  N N 78  
A1L77 H362 H  N N 79  
A1L77 H372 H  N N 80  
A1L77 H371 H  N N 81  
A1L77 H373 H  N N 82  
A1L77 H382 H  N N 83  
A1L77 H381 H  N N 84  
A1L77 H391 H  N N 85  
A1L77 H392 H  N N 86  
A1L77 H401 H  N N 87  
A1L77 H403 H  N N 88  
A1L77 H402 H  N N 89  
A1L77 H231 H  N N 90  
A1L77 H261 H  N N 91  
A1L77 H1   H  N N 92  
ALA   N    N  N N 93  
ALA   CA   C  N S 94  
ALA   C    C  N N 95  
ALA   O    O  N N 96  
ALA   CB   C  N N 97  
ALA   OXT  O  N N 98  
ALA   H    H  N N 99  
ALA   H2   H  N N 100 
ALA   HA   H  N N 101 
ALA   HB1  H  N N 102 
ALA   HB2  H  N N 103 
ALA   HB3  H  N N 104 
ALA   HXT  H  N N 105 
ARG   N    N  N N 106 
ARG   CA   C  N S 107 
ARG   C    C  N N 108 
ARG   O    O  N N 109 
ARG   CB   C  N N 110 
ARG   CG   C  N N 111 
ARG   CD   C  N N 112 
ARG   NE   N  N N 113 
ARG   CZ   C  N N 114 
ARG   NH1  N  N N 115 
ARG   NH2  N  N N 116 
ARG   OXT  O  N N 117 
ARG   H    H  N N 118 
ARG   H2   H  N N 119 
ARG   HA   H  N N 120 
ARG   HB2  H  N N 121 
ARG   HB3  H  N N 122 
ARG   HG2  H  N N 123 
ARG   HG3  H  N N 124 
ARG   HD2  H  N N 125 
ARG   HD3  H  N N 126 
ARG   HE   H  N N 127 
ARG   HH11 H  N N 128 
ARG   HH12 H  N N 129 
ARG   HH21 H  N N 130 
ARG   HH22 H  N N 131 
ARG   HXT  H  N N 132 
ASN   N    N  N N 133 
ASN   CA   C  N S 134 
ASN   C    C  N N 135 
ASN   O    O  N N 136 
ASN   CB   C  N N 137 
ASN   CG   C  N N 138 
ASN   OD1  O  N N 139 
ASN   ND2  N  N N 140 
ASN   OXT  O  N N 141 
ASN   H    H  N N 142 
ASN   H2   H  N N 143 
ASN   HA   H  N N 144 
ASN   HB2  H  N N 145 
ASN   HB3  H  N N 146 
ASN   HD21 H  N N 147 
ASN   HD22 H  N N 148 
ASN   HXT  H  N N 149 
ASP   N    N  N N 150 
ASP   CA   C  N S 151 
ASP   C    C  N N 152 
ASP   O    O  N N 153 
ASP   CB   C  N N 154 
ASP   CG   C  N N 155 
ASP   OD1  O  N N 156 
ASP   OD2  O  N N 157 
ASP   OXT  O  N N 158 
ASP   H    H  N N 159 
ASP   H2   H  N N 160 
ASP   HA   H  N N 161 
ASP   HB2  H  N N 162 
ASP   HB3  H  N N 163 
ASP   HD2  H  N N 164 
ASP   HXT  H  N N 165 
CYS   N    N  N N 166 
CYS   CA   C  N R 167 
CYS   C    C  N N 168 
CYS   O    O  N N 169 
CYS   CB   C  N N 170 
CYS   SG   S  N N 171 
CYS   OXT  O  N N 172 
CYS   H    H  N N 173 
CYS   H2   H  N N 174 
CYS   HA   H  N N 175 
CYS   HB2  H  N N 176 
CYS   HB3  H  N N 177 
CYS   HG   H  N N 178 
CYS   HXT  H  N N 179 
GLN   N    N  N N 180 
GLN   CA   C  N S 181 
GLN   C    C  N N 182 
GLN   O    O  N N 183 
GLN   CB   C  N N 184 
GLN   CG   C  N N 185 
GLN   CD   C  N N 186 
GLN   OE1  O  N N 187 
GLN   NE2  N  N N 188 
GLN   OXT  O  N N 189 
GLN   H    H  N N 190 
GLN   H2   H  N N 191 
GLN   HA   H  N N 192 
GLN   HB2  H  N N 193 
GLN   HB3  H  N N 194 
GLN   HG2  H  N N 195 
GLN   HG3  H  N N 196 
GLN   HE21 H  N N 197 
GLN   HE22 H  N N 198 
GLN   HXT  H  N N 199 
GLU   N    N  N N 200 
GLU   CA   C  N S 201 
GLU   C    C  N N 202 
GLU   O    O  N N 203 
GLU   CB   C  N N 204 
GLU   CG   C  N N 205 
GLU   CD   C  N N 206 
GLU   OE1  O  N N 207 
GLU   OE2  O  N N 208 
GLU   OXT  O  N N 209 
GLU   H    H  N N 210 
GLU   H2   H  N N 211 
GLU   HA   H  N N 212 
GLU   HB2  H  N N 213 
GLU   HB3  H  N N 214 
GLU   HG2  H  N N 215 
GLU   HG3  H  N N 216 
GLU   HE2  H  N N 217 
GLU   HXT  H  N N 218 
GLY   N    N  N N 219 
GLY   CA   C  N N 220 
GLY   C    C  N N 221 
GLY   O    O  N N 222 
GLY   OXT  O  N N 223 
GLY   H    H  N N 224 
GLY   H2   H  N N 225 
GLY   HA2  H  N N 226 
GLY   HA3  H  N N 227 
GLY   HXT  H  N N 228 
HIS   N    N  N N 229 
HIS   CA   C  N S 230 
HIS   C    C  N N 231 
HIS   O    O  N N 232 
HIS   CB   C  N N 233 
HIS   CG   C  Y N 234 
HIS   ND1  N  Y N 235 
HIS   CD2  C  Y N 236 
HIS   CE1  C  Y N 237 
HIS   NE2  N  Y N 238 
HIS   OXT  O  N N 239 
HIS   H    H  N N 240 
HIS   H2   H  N N 241 
HIS   HA   H  N N 242 
HIS   HB2  H  N N 243 
HIS   HB3  H  N N 244 
HIS   HD1  H  N N 245 
HIS   HD2  H  N N 246 
HIS   HE1  H  N N 247 
HIS   HE2  H  N N 248 
HIS   HXT  H  N N 249 
HOH   O    O  N N 250 
HOH   H1   H  N N 251 
HOH   H2   H  N N 252 
ILE   N    N  N N 253 
ILE   CA   C  N S 254 
ILE   C    C  N N 255 
ILE   O    O  N N 256 
ILE   CB   C  N S 257 
ILE   CG1  C  N N 258 
ILE   CG2  C  N N 259 
ILE   CD1  C  N N 260 
ILE   OXT  O  N N 261 
ILE   H    H  N N 262 
ILE   H2   H  N N 263 
ILE   HA   H  N N 264 
ILE   HB   H  N N 265 
ILE   HG12 H  N N 266 
ILE   HG13 H  N N 267 
ILE   HG21 H  N N 268 
ILE   HG22 H  N N 269 
ILE   HG23 H  N N 270 
ILE   HD11 H  N N 271 
ILE   HD12 H  N N 272 
ILE   HD13 H  N N 273 
ILE   HXT  H  N N 274 
LEU   N    N  N N 275 
LEU   CA   C  N S 276 
LEU   C    C  N N 277 
LEU   O    O  N N 278 
LEU   CB   C  N N 279 
LEU   CG   C  N N 280 
LEU   CD1  C  N N 281 
LEU   CD2  C  N N 282 
LEU   OXT  O  N N 283 
LEU   H    H  N N 284 
LEU   H2   H  N N 285 
LEU   HA   H  N N 286 
LEU   HB2  H  N N 287 
LEU   HB3  H  N N 288 
LEU   HG   H  N N 289 
LEU   HD11 H  N N 290 
LEU   HD12 H  N N 291 
LEU   HD13 H  N N 292 
LEU   HD21 H  N N 293 
LEU   HD22 H  N N 294 
LEU   HD23 H  N N 295 
LEU   HXT  H  N N 296 
LYS   N    N  N N 297 
LYS   CA   C  N S 298 
LYS   C    C  N N 299 
LYS   O    O  N N 300 
LYS   CB   C  N N 301 
LYS   CG   C  N N 302 
LYS   CD   C  N N 303 
LYS   CE   C  N N 304 
LYS   NZ   N  N N 305 
LYS   OXT  O  N N 306 
LYS   H    H  N N 307 
LYS   H2   H  N N 308 
LYS   HA   H  N N 309 
LYS   HB2  H  N N 310 
LYS   HB3  H  N N 311 
LYS   HG2  H  N N 312 
LYS   HG3  H  N N 313 
LYS   HD2  H  N N 314 
LYS   HD3  H  N N 315 
LYS   HE2  H  N N 316 
LYS   HE3  H  N N 317 
LYS   HZ1  H  N N 318 
LYS   HZ2  H  N N 319 
LYS   HZ3  H  N N 320 
LYS   HXT  H  N N 321 
MET   N    N  N N 322 
MET   CA   C  N S 323 
MET   C    C  N N 324 
MET   O    O  N N 325 
MET   CB   C  N N 326 
MET   CG   C  N N 327 
MET   SD   S  N N 328 
MET   CE   C  N N 329 
MET   OXT  O  N N 330 
MET   H    H  N N 331 
MET   H2   H  N N 332 
MET   HA   H  N N 333 
MET   HB2  H  N N 334 
MET   HB3  H  N N 335 
MET   HG2  H  N N 336 
MET   HG3  H  N N 337 
MET   HE1  H  N N 338 
MET   HE2  H  N N 339 
MET   HE3  H  N N 340 
MET   HXT  H  N N 341 
PHE   N    N  N N 342 
PHE   CA   C  N S 343 
PHE   C    C  N N 344 
PHE   O    O  N N 345 
PHE   CB   C  N N 346 
PHE   CG   C  Y N 347 
PHE   CD1  C  Y N 348 
PHE   CD2  C  Y N 349 
PHE   CE1  C  Y N 350 
PHE   CE2  C  Y N 351 
PHE   CZ   C  Y N 352 
PHE   OXT  O  N N 353 
PHE   H    H  N N 354 
PHE   H2   H  N N 355 
PHE   HA   H  N N 356 
PHE   HB2  H  N N 357 
PHE   HB3  H  N N 358 
PHE   HD1  H  N N 359 
PHE   HD2  H  N N 360 
PHE   HE1  H  N N 361 
PHE   HE2  H  N N 362 
PHE   HZ   H  N N 363 
PHE   HXT  H  N N 364 
PRO   N    N  N N 365 
PRO   CA   C  N S 366 
PRO   C    C  N N 367 
PRO   O    O  N N 368 
PRO   CB   C  N N 369 
PRO   CG   C  N N 370 
PRO   CD   C  N N 371 
PRO   OXT  O  N N 372 
PRO   H    H  N N 373 
PRO   HA   H  N N 374 
PRO   HB2  H  N N 375 
PRO   HB3  H  N N 376 
PRO   HG2  H  N N 377 
PRO   HG3  H  N N 378 
PRO   HD2  H  N N 379 
PRO   HD3  H  N N 380 
PRO   HXT  H  N N 381 
SER   N    N  N N 382 
SER   CA   C  N S 383 
SER   C    C  N N 384 
SER   O    O  N N 385 
SER   CB   C  N N 386 
SER   OG   O  N N 387 
SER   OXT  O  N N 388 
SER   H    H  N N 389 
SER   H2   H  N N 390 
SER   HA   H  N N 391 
SER   HB2  H  N N 392 
SER   HB3  H  N N 393 
SER   HG   H  N N 394 
SER   HXT  H  N N 395 
THR   N    N  N N 396 
THR   CA   C  N S 397 
THR   C    C  N N 398 
THR   O    O  N N 399 
THR   CB   C  N R 400 
THR   OG1  O  N N 401 
THR   CG2  C  N N 402 
THR   OXT  O  N N 403 
THR   H    H  N N 404 
THR   H2   H  N N 405 
THR   HA   H  N N 406 
THR   HB   H  N N 407 
THR   HG1  H  N N 408 
THR   HG21 H  N N 409 
THR   HG22 H  N N 410 
THR   HG23 H  N N 411 
THR   HXT  H  N N 412 
TRP   N    N  N N 413 
TRP   CA   C  N S 414 
TRP   C    C  N N 415 
TRP   O    O  N N 416 
TRP   CB   C  N N 417 
TRP   CG   C  Y N 418 
TRP   CD1  C  Y N 419 
TRP   CD2  C  Y N 420 
TRP   NE1  N  Y N 421 
TRP   CE2  C  Y N 422 
TRP   CE3  C  Y N 423 
TRP   CZ2  C  Y N 424 
TRP   CZ3  C  Y N 425 
TRP   CH2  C  Y N 426 
TRP   OXT  O  N N 427 
TRP   H    H  N N 428 
TRP   H2   H  N N 429 
TRP   HA   H  N N 430 
TRP   HB2  H  N N 431 
TRP   HB3  H  N N 432 
TRP   HD1  H  N N 433 
TRP   HE1  H  N N 434 
TRP   HE3  H  N N 435 
TRP   HZ2  H  N N 436 
TRP   HZ3  H  N N 437 
TRP   HH2  H  N N 438 
TRP   HXT  H  N N 439 
TYR   N    N  N N 440 
TYR   CA   C  N S 441 
TYR   C    C  N N 442 
TYR   O    O  N N 443 
TYR   CB   C  N N 444 
TYR   CG   C  Y N 445 
TYR   CD1  C  Y N 446 
TYR   CD2  C  Y N 447 
TYR   CE1  C  Y N 448 
TYR   CE2  C  Y N 449 
TYR   CZ   C  Y N 450 
TYR   OH   O  N N 451 
TYR   OXT  O  N N 452 
TYR   H    H  N N 453 
TYR   H2   H  N N 454 
TYR   HA   H  N N 455 
TYR   HB2  H  N N 456 
TYR   HB3  H  N N 457 
TYR   HD1  H  N N 458 
TYR   HD2  H  N N 459 
TYR   HE1  H  N N 460 
TYR   HE2  H  N N 461 
TYR   HH   H  N N 462 
TYR   HXT  H  N N 463 
VAL   N    N  N N 464 
VAL   CA   C  N S 465 
VAL   C    C  N N 466 
VAL   O    O  N N 467 
VAL   CB   C  N N 468 
VAL   CG1  C  N N 469 
VAL   CG2  C  N N 470 
VAL   OXT  O  N N 471 
VAL   H    H  N N 472 
VAL   H2   H  N N 473 
VAL   HA   H  N N 474 
VAL   HB   H  N N 475 
VAL   HG11 H  N N 476 
VAL   HG12 H  N N 477 
VAL   HG13 H  N N 478 
VAL   HG21 H  N N 479 
VAL   HG22 H  N N 480 
VAL   HG23 H  N N 481 
VAL   HXT  H  N N 482 
# 
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 
A1L77 C01  C02  doub Y N 1   
A1L77 C01  C06  sing Y N 2   
A1L77 C02  C03  sing Y N 3   
A1L77 C02  O07  sing N N 4   
A1L77 C03  C04  doub Y N 5   
A1L77 C03  C32  sing N N 6   
A1L77 C04  C05  sing Y N 7   
A1L77 C05  C06  doub Y N 8   
A1L77 C05  SI08 sing N N 9   
A1L77 O07  C24  sing N N 10  
A1L77 SI08 C09  sing N N 11  
A1L77 SI08 C10  sing N N 12  
A1L77 SI08 C34  sing N N 13  
A1L77 C09  C11  doub Y N 14  
A1L77 C09  C15  sing Y N 15  
A1L77 C10  C38  sing N N 16  
A1L77 C11  C12  sing Y N 17  
A1L77 C12  C13  doub Y N 18  
A1L77 C12  C33  sing N N 19  
A1L77 C13  C14  sing Y N 20  
A1L77 C13  O16  sing N N 21  
A1L77 C14  C15  doub Y N 22  
A1L77 O16  C17  sing N N 23  
A1L77 C17  C18  sing N N 24  
A1L77 C18  C19  sing N N 25  
A1L77 C18  C21  sing N N 26  
A1L77 C18  O23  sing N N 27  
A1L77 C19  C20  sing N N 28  
A1L77 C21  C22  sing N N 29  
A1L77 C24  C25  sing N N 30  
A1L77 C25  O26  sing N N 31  
A1L77 C25  C27  sing N N 32  
A1L77 C27  C28  sing N N 33  
A1L77 C28  C29  sing N N 34  
A1L77 C29  O30  doub N N 35  
A1L77 C29  O31  sing N N 36  
A1L77 C34  C35  sing N N 37  
A1L77 C35  C36  sing N N 38  
A1L77 C36  C37  sing N N 39  
A1L77 C38  C39  sing N N 40  
A1L77 C39  C40  sing N N 41  
A1L77 C10  H102 sing N N 42  
A1L77 C10  H101 sing N N 43  
A1L77 C15  H151 sing N N 44  
A1L77 C17  H172 sing N N 45  
A1L77 C17  H171 sing N N 46  
A1L77 C20  H202 sing N N 47  
A1L77 C20  H203 sing N N 48  
A1L77 C20  H201 sing N N 49  
A1L77 C21  H212 sing N N 50  
A1L77 C21  H211 sing N N 51  
A1L77 C22  H223 sing N N 52  
A1L77 C22  H221 sing N N 53  
A1L77 C22  H222 sing N N 54  
A1L77 C24  H242 sing N N 55  
A1L77 C24  H241 sing N N 56  
A1L77 C28  H282 sing N N 57  
A1L77 C28  H281 sing N N 58  
A1L77 C01  H011 sing N N 59  
A1L77 C04  H041 sing N N 60  
A1L77 C06  H061 sing N N 61  
A1L77 C11  H111 sing N N 62  
A1L77 C14  H141 sing N N 63  
A1L77 C19  H191 sing N N 64  
A1L77 C19  H192 sing N N 65  
A1L77 C25  H251 sing N N 66  
A1L77 C27  H272 sing N N 67  
A1L77 C27  H271 sing N N 68  
A1L77 C32  H321 sing N N 69  
A1L77 C32  H323 sing N N 70  
A1L77 C32  H322 sing N N 71  
A1L77 C33  H333 sing N N 72  
A1L77 C33  H331 sing N N 73  
A1L77 C33  H332 sing N N 74  
A1L77 C34  H341 sing N N 75  
A1L77 C34  H342 sing N N 76  
A1L77 C35  H352 sing N N 77  
A1L77 C35  H351 sing N N 78  
A1L77 C36  H361 sing N N 79  
A1L77 C36  H362 sing N N 80  
A1L77 C37  H372 sing N N 81  
A1L77 C37  H371 sing N N 82  
A1L77 C37  H373 sing N N 83  
A1L77 C38  H382 sing N N 84  
A1L77 C38  H381 sing N N 85  
A1L77 C39  H391 sing N N 86  
A1L77 C39  H392 sing N N 87  
A1L77 C40  H401 sing N N 88  
A1L77 C40  H403 sing N N 89  
A1L77 C40  H402 sing N N 90  
A1L77 O23  H231 sing N N 91  
A1L77 O26  H261 sing N N 92  
A1L77 O31  H1   sing N N 93  
ALA   N    CA   sing N N 94  
ALA   N    H    sing N N 95  
ALA   N    H2   sing N N 96  
ALA   CA   C    sing N N 97  
ALA   CA   CB   sing N N 98  
ALA   CA   HA   sing N N 99  
ALA   C    O    doub N N 100 
ALA   C    OXT  sing N N 101 
ALA   CB   HB1  sing N N 102 
ALA   CB   HB2  sing N N 103 
ALA   CB   HB3  sing N N 104 
ALA   OXT  HXT  sing N N 105 
ARG   N    CA   sing N N 106 
ARG   N    H    sing N N 107 
ARG   N    H2   sing N N 108 
ARG   CA   C    sing N N 109 
ARG   CA   CB   sing N N 110 
ARG   CA   HA   sing N N 111 
ARG   C    O    doub N N 112 
ARG   C    OXT  sing N N 113 
ARG   CB   CG   sing N N 114 
ARG   CB   HB2  sing N N 115 
ARG   CB   HB3  sing N N 116 
ARG   CG   CD   sing N N 117 
ARG   CG   HG2  sing N N 118 
ARG   CG   HG3  sing N N 119 
ARG   CD   NE   sing N N 120 
ARG   CD   HD2  sing N N 121 
ARG   CD   HD3  sing N N 122 
ARG   NE   CZ   sing N N 123 
ARG   NE   HE   sing N N 124 
ARG   CZ   NH1  sing N N 125 
ARG   CZ   NH2  doub N N 126 
ARG   NH1  HH11 sing N N 127 
ARG   NH1  HH12 sing N N 128 
ARG   NH2  HH21 sing N N 129 
ARG   NH2  HH22 sing N N 130 
ARG   OXT  HXT  sing N N 131 
ASN   N    CA   sing N N 132 
ASN   N    H    sing N N 133 
ASN   N    H2   sing N N 134 
ASN   CA   C    sing N N 135 
ASN   CA   CB   sing N N 136 
ASN   CA   HA   sing N N 137 
ASN   C    O    doub N N 138 
ASN   C    OXT  sing N N 139 
ASN   CB   CG   sing N N 140 
ASN   CB   HB2  sing N N 141 
ASN   CB   HB3  sing N N 142 
ASN   CG   OD1  doub N N 143 
ASN   CG   ND2  sing N N 144 
ASN   ND2  HD21 sing N N 145 
ASN   ND2  HD22 sing N N 146 
ASN   OXT  HXT  sing N N 147 
ASP   N    CA   sing N N 148 
ASP   N    H    sing N N 149 
ASP   N    H2   sing N N 150 
ASP   CA   C    sing N N 151 
ASP   CA   CB   sing N N 152 
ASP   CA   HA   sing N N 153 
ASP   C    O    doub N N 154 
ASP   C    OXT  sing N N 155 
ASP   CB   CG   sing N N 156 
ASP   CB   HB2  sing N N 157 
ASP   CB   HB3  sing N N 158 
ASP   CG   OD1  doub N N 159 
ASP   CG   OD2  sing N N 160 
ASP   OD2  HD2  sing N N 161 
ASP   OXT  HXT  sing N N 162 
CYS   N    CA   sing N N 163 
CYS   N    H    sing N N 164 
CYS   N    H2   sing N N 165 
CYS   CA   C    sing N N 166 
CYS   CA   CB   sing N N 167 
CYS   CA   HA   sing N N 168 
CYS   C    O    doub N N 169 
CYS   C    OXT  sing N N 170 
CYS   CB   SG   sing N N 171 
CYS   CB   HB2  sing N N 172 
CYS   CB   HB3  sing N N 173 
CYS   SG   HG   sing N N 174 
CYS   OXT  HXT  sing N N 175 
GLN   N    CA   sing N N 176 
GLN   N    H    sing N N 177 
GLN   N    H2   sing N N 178 
GLN   CA   C    sing N N 179 
GLN   CA   CB   sing N N 180 
GLN   CA   HA   sing N N 181 
GLN   C    O    doub N N 182 
GLN   C    OXT  sing N N 183 
GLN   CB   CG   sing N N 184 
GLN   CB   HB2  sing N N 185 
GLN   CB   HB3  sing N N 186 
GLN   CG   CD   sing N N 187 
GLN   CG   HG2  sing N N 188 
GLN   CG   HG3  sing N N 189 
GLN   CD   OE1  doub N N 190 
GLN   CD   NE2  sing N N 191 
GLN   NE2  HE21 sing N N 192 
GLN   NE2  HE22 sing N N 193 
GLN   OXT  HXT  sing N N 194 
GLU   N    CA   sing N N 195 
GLU   N    H    sing N N 196 
GLU   N    H2   sing N N 197 
GLU   CA   C    sing N N 198 
GLU   CA   CB   sing N N 199 
GLU   CA   HA   sing N N 200 
GLU   C    O    doub N N 201 
GLU   C    OXT  sing N N 202 
GLU   CB   CG   sing N N 203 
GLU   CB   HB2  sing N N 204 
GLU   CB   HB3  sing N N 205 
GLU   CG   CD   sing N N 206 
GLU   CG   HG2  sing N N 207 
GLU   CG   HG3  sing N N 208 
GLU   CD   OE1  doub N N 209 
GLU   CD   OE2  sing N N 210 
GLU   OE2  HE2  sing N N 211 
GLU   OXT  HXT  sing N N 212 
GLY   N    CA   sing N N 213 
GLY   N    H    sing N N 214 
GLY   N    H2   sing N N 215 
GLY   CA   C    sing N N 216 
GLY   CA   HA2  sing N N 217 
GLY   CA   HA3  sing N N 218 
GLY   C    O    doub N N 219 
GLY   C    OXT  sing N N 220 
GLY   OXT  HXT  sing N N 221 
HIS   N    CA   sing N N 222 
HIS   N    H    sing N N 223 
HIS   N    H2   sing N N 224 
HIS   CA   C    sing N N 225 
HIS   CA   CB   sing N N 226 
HIS   CA   HA   sing N N 227 
HIS   C    O    doub N N 228 
HIS   C    OXT  sing N N 229 
HIS   CB   CG   sing N N 230 
HIS   CB   HB2  sing N N 231 
HIS   CB   HB3  sing N N 232 
HIS   CG   ND1  sing Y N 233 
HIS   CG   CD2  doub Y N 234 
HIS   ND1  CE1  doub Y N 235 
HIS   ND1  HD1  sing N N 236 
HIS   CD2  NE2  sing Y N 237 
HIS   CD2  HD2  sing N N 238 
HIS   CE1  NE2  sing Y N 239 
HIS   CE1  HE1  sing N N 240 
HIS   NE2  HE2  sing N N 241 
HIS   OXT  HXT  sing N N 242 
HOH   O    H1   sing N N 243 
HOH   O    H2   sing N N 244 
ILE   N    CA   sing N N 245 
ILE   N    H    sing N N 246 
ILE   N    H2   sing N N 247 
ILE   CA   C    sing N N 248 
ILE   CA   CB   sing N N 249 
ILE   CA   HA   sing N N 250 
ILE   C    O    doub N N 251 
ILE   C    OXT  sing N N 252 
ILE   CB   CG1  sing N N 253 
ILE   CB   CG2  sing N N 254 
ILE   CB   HB   sing N N 255 
ILE   CG1  CD1  sing N N 256 
ILE   CG1  HG12 sing N N 257 
ILE   CG1  HG13 sing N N 258 
ILE   CG2  HG21 sing N N 259 
ILE   CG2  HG22 sing N N 260 
ILE   CG2  HG23 sing N N 261 
ILE   CD1  HD11 sing N N 262 
ILE   CD1  HD12 sing N N 263 
ILE   CD1  HD13 sing N N 264 
ILE   OXT  HXT  sing N N 265 
LEU   N    CA   sing N N 266 
LEU   N    H    sing N N 267 
LEU   N    H2   sing N N 268 
LEU   CA   C    sing N N 269 
LEU   CA   CB   sing N N 270 
LEU   CA   HA   sing N N 271 
LEU   C    O    doub N N 272 
LEU   C    OXT  sing N N 273 
LEU   CB   CG   sing N N 274 
LEU   CB   HB2  sing N N 275 
LEU   CB   HB3  sing N N 276 
LEU   CG   CD1  sing N N 277 
LEU   CG   CD2  sing N N 278 
LEU   CG   HG   sing N N 279 
LEU   CD1  HD11 sing N N 280 
LEU   CD1  HD12 sing N N 281 
LEU   CD1  HD13 sing N N 282 
LEU   CD2  HD21 sing N N 283 
LEU   CD2  HD22 sing N N 284 
LEU   CD2  HD23 sing N N 285 
LEU   OXT  HXT  sing N N 286 
LYS   N    CA   sing N N 287 
LYS   N    H    sing N N 288 
LYS   N    H2   sing N N 289 
LYS   CA   C    sing N N 290 
LYS   CA   CB   sing N N 291 
LYS   CA   HA   sing N N 292 
LYS   C    O    doub N N 293 
LYS   C    OXT  sing N N 294 
LYS   CB   CG   sing N N 295 
LYS   CB   HB2  sing N N 296 
LYS   CB   HB3  sing N N 297 
LYS   CG   CD   sing N N 298 
LYS   CG   HG2  sing N N 299 
LYS   CG   HG3  sing N N 300 
LYS   CD   CE   sing N N 301 
LYS   CD   HD2  sing N N 302 
LYS   CD   HD3  sing N N 303 
LYS   CE   NZ   sing N N 304 
LYS   CE   HE2  sing N N 305 
LYS   CE   HE3  sing N N 306 
LYS   NZ   HZ1  sing N N 307 
LYS   NZ   HZ2  sing N N 308 
LYS   NZ   HZ3  sing N N 309 
LYS   OXT  HXT  sing N N 310 
MET   N    CA   sing N N 311 
MET   N    H    sing N N 312 
MET   N    H2   sing N N 313 
MET   CA   C    sing N N 314 
MET   CA   CB   sing N N 315 
MET   CA   HA   sing N N 316 
MET   C    O    doub N N 317 
MET   C    OXT  sing N N 318 
MET   CB   CG   sing N N 319 
MET   CB   HB2  sing N N 320 
MET   CB   HB3  sing N N 321 
MET   CG   SD   sing N N 322 
MET   CG   HG2  sing N N 323 
MET   CG   HG3  sing N N 324 
MET   SD   CE   sing N N 325 
MET   CE   HE1  sing N N 326 
MET   CE   HE2  sing N N 327 
MET   CE   HE3  sing N N 328 
MET   OXT  HXT  sing N N 329 
PHE   N    CA   sing N N 330 
PHE   N    H    sing N N 331 
PHE   N    H2   sing N N 332 
PHE   CA   C    sing N N 333 
PHE   CA   CB   sing N N 334 
PHE   CA   HA   sing N N 335 
PHE   C    O    doub N N 336 
PHE   C    OXT  sing N N 337 
PHE   CB   CG   sing N N 338 
PHE   CB   HB2  sing N N 339 
PHE   CB   HB3  sing N N 340 
PHE   CG   CD1  doub Y N 341 
PHE   CG   CD2  sing Y N 342 
PHE   CD1  CE1  sing Y N 343 
PHE   CD1  HD1  sing N N 344 
PHE   CD2  CE2  doub Y N 345 
PHE   CD2  HD2  sing N N 346 
PHE   CE1  CZ   doub Y N 347 
PHE   CE1  HE1  sing N N 348 
PHE   CE2  CZ   sing Y N 349 
PHE   CE2  HE2  sing N N 350 
PHE   CZ   HZ   sing N N 351 
PHE   OXT  HXT  sing N N 352 
PRO   N    CA   sing N N 353 
PRO   N    CD   sing N N 354 
PRO   N    H    sing N N 355 
PRO   CA   C    sing N N 356 
PRO   CA   CB   sing N N 357 
PRO   CA   HA   sing N N 358 
PRO   C    O    doub N N 359 
PRO   C    OXT  sing N N 360 
PRO   CB   CG   sing N N 361 
PRO   CB   HB2  sing N N 362 
PRO   CB   HB3  sing N N 363 
PRO   CG   CD   sing N N 364 
PRO   CG   HG2  sing N N 365 
PRO   CG   HG3  sing N N 366 
PRO   CD   HD2  sing N N 367 
PRO   CD   HD3  sing N N 368 
PRO   OXT  HXT  sing N N 369 
SER   N    CA   sing N N 370 
SER   N    H    sing N N 371 
SER   N    H2   sing N N 372 
SER   CA   C    sing N N 373 
SER   CA   CB   sing N N 374 
SER   CA   HA   sing N N 375 
SER   C    O    doub N N 376 
SER   C    OXT  sing N N 377 
SER   CB   OG   sing N N 378 
SER   CB   HB2  sing N N 379 
SER   CB   HB3  sing N N 380 
SER   OG   HG   sing N N 381 
SER   OXT  HXT  sing N N 382 
THR   N    CA   sing N N 383 
THR   N    H    sing N N 384 
THR   N    H2   sing N N 385 
THR   CA   C    sing N N 386 
THR   CA   CB   sing N N 387 
THR   CA   HA   sing N N 388 
THR   C    O    doub N N 389 
THR   C    OXT  sing N N 390 
THR   CB   OG1  sing N N 391 
THR   CB   CG2  sing N N 392 
THR   CB   HB   sing N N 393 
THR   OG1  HG1  sing N N 394 
THR   CG2  HG21 sing N N 395 
THR   CG2  HG22 sing N N 396 
THR   CG2  HG23 sing N N 397 
THR   OXT  HXT  sing N N 398 
TRP   N    CA   sing N N 399 
TRP   N    H    sing N N 400 
TRP   N    H2   sing N N 401 
TRP   CA   C    sing N N 402 
TRP   CA   CB   sing N N 403 
TRP   CA   HA   sing N N 404 
TRP   C    O    doub N N 405 
TRP   C    OXT  sing N N 406 
TRP   CB   CG   sing N N 407 
TRP   CB   HB2  sing N N 408 
TRP   CB   HB3  sing N N 409 
TRP   CG   CD1  doub Y N 410 
TRP   CG   CD2  sing Y N 411 
TRP   CD1  NE1  sing Y N 412 
TRP   CD1  HD1  sing N N 413 
TRP   CD2  CE2  doub Y N 414 
TRP   CD2  CE3  sing Y N 415 
TRP   NE1  CE2  sing Y N 416 
TRP   NE1  HE1  sing N N 417 
TRP   CE2  CZ2  sing Y N 418 
TRP   CE3  CZ3  doub Y N 419 
TRP   CE3  HE3  sing N N 420 
TRP   CZ2  CH2  doub Y N 421 
TRP   CZ2  HZ2  sing N N 422 
TRP   CZ3  CH2  sing Y N 423 
TRP   CZ3  HZ3  sing N N 424 
TRP   CH2  HH2  sing N N 425 
TRP   OXT  HXT  sing N N 426 
TYR   N    CA   sing N N 427 
TYR   N    H    sing N N 428 
TYR   N    H2   sing N N 429 
TYR   CA   C    sing N N 430 
TYR   CA   CB   sing N N 431 
TYR   CA   HA   sing N N 432 
TYR   C    O    doub N N 433 
TYR   C    OXT  sing N N 434 
TYR   CB   CG   sing N N 435 
TYR   CB   HB2  sing N N 436 
TYR   CB   HB3  sing N N 437 
TYR   CG   CD1  doub Y N 438 
TYR   CG   CD2  sing Y N 439 
TYR   CD1  CE1  sing Y N 440 
TYR   CD1  HD1  sing N N 441 
TYR   CD2  CE2  doub Y N 442 
TYR   CD2  HD2  sing N N 443 
TYR   CE1  CZ   doub Y N 444 
TYR   CE1  HE1  sing N N 445 
TYR   CE2  CZ   sing Y N 446 
TYR   CE2  HE2  sing N N 447 
TYR   CZ   OH   sing N N 448 
TYR   OH   HH   sing N N 449 
TYR   OXT  HXT  sing N N 450 
VAL   N    CA   sing N N 451 
VAL   N    H    sing N N 452 
VAL   N    H2   sing N N 453 
VAL   CA   C    sing N N 454 
VAL   CA   CB   sing N N 455 
VAL   CA   HA   sing N N 456 
VAL   C    O    doub N N 457 
VAL   C    OXT  sing N N 458 
VAL   CB   CG1  sing N N 459 
VAL   CB   CG2  sing N N 460 
VAL   CB   HB   sing N N 461 
VAL   CG1  HG11 sing N N 462 
VAL   CG1  HG12 sing N N 463 
VAL   CG1  HG13 sing N N 464 
VAL   CG2  HG21 sing N N 465 
VAL   CG2  HG22 sing N N 466 
VAL   CG2  HG23 sing N N 467 
VAL   OXT  HXT  sing N N 468 
# 
_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                    9M19 
_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]   0.006464 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000798 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023701 
_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]   0.023666 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
SI 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . LYS   A 1 18  ? 43.31600 -0.66900  2.24900  1.000 76.72109  ?  123 LYS   A N    1 
ATOM   2    C  CA   . LYS   A 1 18  ? 42.91400 -1.74600  3.14500  1.000 72.44046  ?  123 LYS   A CA   1 
ATOM   3    C  C    . LYS   A 1 18  ? 41.39300 -1.84600  3.22200  1.000 61.47880  ?  123 LYS   A C    1 
ATOM   4    O  O    . LYS   A 1 18  ? 40.83400 -2.94300  3.23000  1.000 58.29060  ?  123 LYS   A O    1 
ATOM   5    C  CB   . LYS   A 1 18  ? 43.50500 -1.53200  4.53800  1.000 75.19562  ?  123 LYS   A CB   1 
ATOM   6    C  CG   . LYS   A 1 18  ? 43.86900 -2.81500  5.26600  1.000 78.02142  ?  123 LYS   A CG   1 
ATOM   7    C  CD   . LYS   A 1 18  ? 45.35100 -3.12300  5.12200  1.000 90.65871  ?  123 LYS   A CD   1 
ATOM   8    C  CE   . LYS   A 1 18  ? 45.76500 -4.28600  6.00800  1.000 90.79398  ?  123 LYS   A CE   1 
ATOM   9    N  NZ   . LYS   A 1 18  ? 46.18400 -3.83500  7.36400  1.000 81.20533  ?  123 LYS   A NZ   1 
ATOM   10   N  N    . LEU   A 1 19  ? 40.72700 -0.69500  3.28200  1.000 58.72602  ?  124 LEU   A N    1 
ATOM   11   C  CA   . LEU   A 1 19  ? 39.26700 -0.64400  3.23000  1.000 63.08849  ?  124 LEU   A CA   1 
ATOM   12   C  C    . LEU   A 1 19  ? 38.82200 -0.98200  1.81400  1.000 57.08757  ?  124 LEU   A C    1 
ATOM   13   O  O    . LEU   A 1 19  ? 38.81800 -0.12400  0.92900  1.000 70.37544  ?  124 LEU   A O    1 
ATOM   14   C  CB   . LEU   A 1 19  ? 38.76300 0.73300   3.65100  1.000 63.28631  ?  124 LEU   A CB   1 
ATOM   15   C  CG   . LEU   A 1 19  ? 37.34900 0.83000   4.23700  1.000 59.44056  ?  124 LEU   A CG   1 
ATOM   16   C  CD1  . LEU   A 1 19  ? 36.99600 -0.39300  5.07700  1.000 55.02264  ?  124 LEU   A CD1  1 
ATOM   17   C  CD2  . LEU   A 1 19  ? 37.19400 2.10600   5.05000  1.000 61.70671  ?  124 LEU   A CD2  1 
ATOM   18   N  N    . SER   A 1 20  ? 38.45000 -2.24100  1.59000  1.000 50.31548  ?  125 SER   A N    1 
ATOM   19   C  CA   . SER   A 1 20  ? 38.03500 -2.67300  0.26400  1.000 52.59806  ?  125 SER   A CA   1 
ATOM   20   C  C    . SER   A 1 20  ? 36.77200 -1.93300  -0.16700 1.000 58.06595  ?  125 SER   A C    1 
ATOM   21   O  O    . SER   A 1 20  ? 36.03000 -1.38200  0.65100  1.000 56.24500  ?  125 SER   A O    1 
ATOM   22   C  CB   . SER   A 1 20  ? 37.79400 -4.18400  0.24100  1.000 50.01253  ?  125 SER   A CB   1 
ATOM   23   O  OG   . SER   A 1 20  ? 36.48400 -4.49900  0.68600  1.000 52.04945  ?  125 SER   A OG   1 
ATOM   24   N  N    . GLU   A 1 21  ? 36.53500 -1.91500  -1.48100 1.000 57.32407  ?  126 GLU   A N    1 
ATOM   25   C  CA   . GLU   A 1 21  ? 35.35500 -1.23300  -1.99700 1.000 61.88117  ?  126 GLU   A CA   1 
ATOM   26   C  C    . GLU   A 1 21  ? 34.07500 -2.00100  -1.70100 1.000 53.87507  ?  126 GLU   A C    1 
ATOM   27   O  O    . GLU   A 1 21  ? 33.00200 -1.39200  -1.64600 1.000 53.98966  ?  126 GLU   A O    1 
ATOM   28   C  CB   . GLU   A 1 21  ? 35.49900 -0.98500  -3.49700 1.000 73.54670  ?  126 GLU   A CB   1 
ATOM   29   C  CG   . GLU   A 1 21  ? 36.28800 0.27500   -3.81300 1.000 88.79450  ?  126 GLU   A CG   1 
ATOM   30   C  CD   . GLU   A 1 21  ? 36.63300 0.40000   -5.28100 1.000 104.74489 ?  126 GLU   A CD   1 
ATOM   31   O  OE1  . GLU   A 1 21  ? 37.83900 0.43500   -5.60400 1.000 111.57077 ?  126 GLU   A OE1  1 
ATOM   32   O  OE2  . GLU   A 1 21  ? 35.70000 0.47000   -6.10900 1.000 106.57346 ?  126 GLU   A OE2  1 
ATOM   33   N  N    . GLU   A 1 22  ? 34.16200 -3.32000  -1.51300 1.000 53.21346  ?  127 GLU   A N    1 
ATOM   34   C  CA   . GLU   A 1 22  ? 33.03600 -4.05600  -0.95200 1.000 46.13431  ?  127 GLU   A CA   1 
ATOM   35   C  C    . GLU   A 1 22  ? 32.70800 -3.56200  0.45100  1.000 44.69973  ?  127 GLU   A C    1 
ATOM   36   O  O    . GLU   A 1 22  ? 31.53400 -3.50800  0.83400  1.000 45.32834  ?  127 GLU   A O    1 
ATOM   37   C  CB   . GLU   A 1 22  ? 33.34300 -5.55600  -0.93900 1.000 53.78048  ?  127 GLU   A CB   1 
ATOM   38   C  CG   . GLU   A 1 22  ? 32.53100 -6.36900  0.06100  1.000 72.32659  ?  127 GLU   A CG   1 
ATOM   39   C  CD   . GLU   A 1 22  ? 32.27900 -7.79300  -0.40400 1.000 85.22558  ?  127 GLU   A CD   1 
ATOM   40   O  OE1  . GLU   A 1 22  ? 32.29000 -8.03000  -1.63000 1.000 92.43050  ?  127 GLU   A OE1  1 
ATOM   41   O  OE2  . GLU   A 1 22  ? 32.06900 -8.67600  0.45600  1.000 85.19178  ?  127 GLU   A OE2  1 
ATOM   42   N  N    . GLN   A 1 23  ? 33.72900 -3.17100  1.21800  1.000 44.03682  ?  128 GLN   A N    1 
ATOM   43   C  CA   . GLN   A 1 23  ? 33.50800 -2.67600  2.57200  1.000 44.60026  ?  128 GLN   A CA   1 
ATOM   44   C  C    . GLN   A 1 23  ? 32.99200 -1.24100  2.56800  1.000 49.89334  ?  128 GLN   A C    1 
ATOM   45   O  O    . GLN   A 1 23  ? 32.11100 -0.89700  3.36500  1.000 45.69369  ?  128 GLN   A O    1 
ATOM   46   C  CB   . GLN   A 1 23  ? 34.79900 -2.78200  3.38400  1.000 49.83616  ?  128 GLN   A CB   1 
ATOM   47   C  CG   . GLN   A 1 23  ? 35.13800 -4.20400  3.80700  1.000 48.82708  ?  128 GLN   A CG   1 
ATOM   48   C  CD   . GLN   A 1 23  ? 36.53800 -4.32900  4.37300  1.000 48.13262  ?  128 GLN   A CD   1 
ATOM   49   O  OE1  . GLN   A 1 23  ? 37.41400 -3.51600  4.07700  1.000 45.34797  ?  128 GLN   A OE1  1 
ATOM   50   N  NE2  . GLN   A 1 23  ? 36.75800 -5.35300  5.18900  1.000 46.60259  ?  128 GLN   A NE2  1 
ATOM   51   N  N    . GLN   A 1 24  ? 33.53100 -0.38800  1.69200  1.000 46.46774  ?  129 GLN   A N    1 
ATOM   52   C  CA   . GLN   A 1 24  ? 32.97400 0.95300   1.53800  1.000 49.62847  ?  129 GLN   A CA   1 
ATOM   53   C  C    . GLN   A 1 24  ? 31.52900 0.88900   1.06300  1.000 47.85187  ?  129 GLN   A C    1 
ATOM   54   O  O    . GLN   A 1 24  ? 30.69200 1.70000   1.47900  1.000 46.78886  ?  129 GLN   A O    1 
ATOM   55   C  CB   . GLN   A 1 24  ? 33.81700 1.77100   0.56000  1.000 51.03689  ?  129 GLN   A CB   1 
ATOM   56   C  CG   . GLN   A 1 24  ? 35.23800 2.04200   1.01700  1.000 56.42769  ?  129 GLN   A CG   1 
ATOM   57   C  CD   . GLN   A 1 24  ? 36.12100 2.53400   -0.11300 1.000 67.63816  ?  129 GLN   A CD   1 
ATOM   58   O  OE1  . GLN   A 1 24  ? 35.78300 3.49400   -0.80700 1.000 66.62649  ?  129 GLN   A OE1  1 
ATOM   59   N  NE2  . GLN   A 1 24  ? 37.25900 1.87900   -0.30400 1.000 71.52548  ?  129 GLN   A NE2  1 
ATOM   60   N  N    . HIS   A 1 25  ? 31.22300 -0.06700  0.18300  1.000 42.16768  ?  130 HIS   A N    1 
ATOM   61   C  CA   . HIS   A 1 25  ? 29.85100 -0.25400  -0.27900 1.000 47.63229  ?  130 HIS   A CA   1 
ATOM   62   C  C    . HIS   A 1 25  ? 28.92800 -0.61300  0.87800  1.000 46.74590  ?  130 HIS   A C    1 
ATOM   63   O  O    . HIS   A 1 25  ? 27.81800 -0.07900  0.98600  1.000 50.01463  ?  130 HIS   A O    1 
ATOM   64   C  CB   . HIS   A 1 25  ? 29.81800 -1.33700  -1.35900 1.000 52.21228  ?  130 HIS   A CB   1 
ATOM   65   C  CG   . HIS   A 1 25  ? 28.48500 -1.50300  -2.01900 1.000 52.29383  ?  130 HIS   A CG   1 
ATOM   66   N  ND1  . HIS   A 1 25  ? 27.77000 -0.44400  -2.53600 1.000 57.15910  ?  130 HIS   A ND1  1 
ATOM   67   C  CD2  . HIS   A 1 25  ? 27.74500 -2.61100  -2.26400 1.000 57.93882  ?  130 HIS   A CD2  1 
ATOM   68   C  CE1  . HIS   A 1 25  ? 26.64400 -0.89100  -3.06200 1.000 58.02639  ?  130 HIS   A CE1  1 
ATOM   69   N  NE2  . HIS   A 1 25  ? 26.60500 -2.20200  -2.91100 1.000 57.97484  ?  130 HIS   A NE2  1 
ATOM   70   N  N    . ILE   A 1 26  ? 29.37800 -1.50900  1.76000  1.000 42.29091  ?  131 ILE   A N    1 
ATOM   71   C  CA   . ILE   A 1 26  ? 28.57000 -1.90800  2.91100  1.000 41.32370  ?  131 ILE   A CA   1 
ATOM   72   C  C    . ILE   A 1 26  ? 28.27200 -0.70300  3.79500  1.000 35.55361  ?  131 ILE   A C    1 
ATOM   73   O  O    . ILE   A 1 26  ? 27.13300 -0.49600  4.23200  1.000 36.25409  ?  131 ILE   A O    1 
ATOM   74   C  CB   . ILE   A 1 26  ? 29.28100 -3.02100  3.70200  1.000 48.13767  ?  131 ILE   A CB   1 
ATOM   75   C  CG1  . ILE   A 1 26  ? 29.26700 -4.33300  2.91500  1.000 47.13813  ?  131 ILE   A CG1  1 
ATOM   76   C  CG2  . ILE   A 1 26  ? 28.64400 -3.20000  5.07200  1.000 47.15510  ?  131 ILE   A CG2  1 
ATOM   77   C  CD1  . ILE   A 1 26  ? 30.35100 -5.30000  3.33700  1.000 54.24169  ?  131 ILE   A CD1  1 
ATOM   78   N  N    . ILE   A 1 27  ? 29.29400 0.11000   4.06800  1.000 35.24568  ?  132 ILE   A N    1 
ATOM   79   C  CA   . ILE   A 1 27  ? 29.11600 1.26400   4.94600  1.000 43.68351  ?  132 ILE   A CA   1 
ATOM   80   C  C    . ILE   A 1 27  ? 28.12700 2.25200   4.34000  1.000 46.11520  ?  132 ILE   A C    1 
ATOM   81   O  O    . ILE   A 1 27  ? 27.30000 2.84000   5.04800  1.000 45.10319  ?  132 ILE   A O    1 
ATOM   82   C  CB   . ILE   A 1 27  ? 30.47900 1.91900   5.23600  1.000 43.99683  ?  132 ILE   A CB   1 
ATOM   83   C  CG1  . ILE   A 1 27  ? 31.31200 1.02000   6.15400  1.000 41.39904  ?  132 ILE   A CG1  1 
ATOM   84   C  CG2  . ILE   A 1 27  ? 30.29600 3.29500   5.84900  1.000 36.89263  ?  132 ILE   A CG2  1 
ATOM   85   C  CD1  . ILE   A 1 27  ? 32.77300 1.40400   6.23400  1.000 47.59125  ?  132 ILE   A CD1  1 
ATOM   86   N  N    . ALA   A 1 28  ? 28.17900 2.43500   3.02000  1.000 38.64608  ?  133 ALA   A N    1 
ATOM   87   C  CA   . ALA   A 1 28  ? 27.28700 3.39100   2.37300  1.000 43.96454  ?  133 ALA   A CA   1 
ATOM   88   C  C    . ALA   A 1 28  ? 25.83700 2.91900   2.40500  1.000 37.92534  ?  133 ALA   A C    1 
ATOM   89   O  O    . ALA   A 1 28  ? 24.91900 3.73400   2.55200  1.000 35.99062  ?  133 ALA   A O    1 
ATOM   90   C  CB   . ALA   A 1 28  ? 27.73900 3.63500   0.93800  1.000 42.73215  ?  133 ALA   A CB   1 
ATOM   91   N  N    . ILE   A 1 29  ? 25.60900 1.61100   2.25500  1.000 39.36469  ?  134 ILE   A N    1 
ATOM   92   C  CA   . ILE   A 1 29  ? 24.24900 1.08000   2.33900  1.000 40.56515  ?  134 ILE   A CA   1 
ATOM   93   C  C    . ILE   A 1 29  ? 23.68900 1.28600   3.74000  1.000 41.81357  ?  134 ILE   A C    1 
ATOM   94   O  O    . ILE   A 1 29  ? 22.53500 1.69900   3.91600  1.000 36.63604  ?  134 ILE   A O    1 
ATOM   95   C  CB   . ILE   A 1 29  ? 24.22300 -0.40600  1.93700  1.000 37.95501  ?  134 ILE   A CB   1 
ATOM   96   C  CG1  . ILE   A 1 29  ? 24.44300 -0.56700  0.43200  1.000 44.16913  ?  134 ILE   A CG1  1 
ATOM   97   C  CG2  . ILE   A 1 29  ? 22.91500 -1.05900  2.36000  1.000 36.47659  ?  134 ILE   A CG2  1 
ATOM   98   C  CD1  . ILE   A 1 29  ? 25.23200 -1.80600  0.06600  1.000 40.80884  ?  134 ILE   A CD1  1 
ATOM   99   N  N    . LEU   A 1 30  ? 24.50400 1.00700   4.76000  1.000 34.79392  ?  135 LEU   A N    1 
ATOM   100  C  CA   . LEU   A 1 30  ? 24.05000 1.15400   6.13900  1.000 35.21856  ?  135 LEU   A CA   1 
ATOM   101  C  C    . LEU   A 1 30  ? 23.82300 2.61600   6.49600  1.000 32.61150  ?  135 LEU   A C    1 
ATOM   102  O  O    . LEU   A 1 30  ? 22.91000 2.93800   7.26600  1.000 33.33484  ?  135 LEU   A O    1 
ATOM   103  C  CB   . LEU   A 1 30  ? 25.06200 0.52200   7.09300  1.000 39.85072  ?  135 LEU   A CB   1 
ATOM   104  C  CG   . LEU   A 1 30  ? 25.20300 -0.99600  6.99400  1.000 39.25370  ?  135 LEU   A CG   1 
ATOM   105  C  CD1  . LEU   A 1 30  ? 26.31200 -1.48800  7.91000  1.000 38.06417  ?  135 LEU   A CD1  1 
ATOM   106  C  CD2  . LEU   A 1 30  ? 23.88300 -1.67100  7.32500  1.000 28.81248  ?  135 LEU   A CD2  1 
ATOM   107  N  N    . LEU   A 1 31  ? 24.64800 3.51600   5.95900  1.000 36.02130  ?  136 LEU   A N    1 
ATOM   108  C  CA   . LEU   A 1 31  ? 24.41900 4.94000   6.17300  1.000 31.24128  ?  136 LEU   A CA   1 
ATOM   109  C  C    . LEU   A 1 31  ? 23.10000 5.37000   5.54600  1.000 36.99918  ?  136 LEU   A C    1 
ATOM   110  O  O    . LEU   A 1 31  ? 22.27500 6.02600   6.19200  1.000 39.35121  ?  136 LEU   A O    1 
ATOM   111  C  CB   . LEU   A 1 31  ? 25.58200 5.75300   5.60100  1.000 33.33288  ?  136 LEU   A CB   1 
ATOM   112  C  CG   . LEU   A 1 31  ? 26.89500 5.76700   6.38700  1.000 31.86195  ?  136 LEU   A CG   1 
ATOM   113  C  CD1  . LEU   A 1 31  ? 27.99300 6.44000   5.57100  1.000 31.69617  ?  136 LEU   A CD1  1 
ATOM   114  C  CD2  . LEU   A 1 31  ? 26.71800 6.46500   7.72600  1.000 34.52705  ?  136 LEU   A CD2  1 
ATOM   115  N  N    . ASP   A 1 32  ? 22.87800 4.99100   4.28400  1.000 38.35759  ?  137 ASP   A N    1 
ATOM   116  C  CA   . ASP   A 1 32  ? 21.62400 5.32100   3.61500  1.000 38.73782  ?  137 ASP   A CA   1 
ATOM   117  C  C    . ASP   A 1 32  ? 20.43100 4.71000   4.33900  1.000 38.47906  ?  137 ASP   A C    1 
ATOM   118  O  O    . ASP   A 1 32  ? 19.37900 5.34700   4.46500  1.000 41.07090  ?  137 ASP   A O    1 
ATOM   119  C  CB   . ASP   A 1 32  ? 21.66800 4.84800   2.16300  1.000 40.78925  ?  137 ASP   A CB   1 
ATOM   120  C  CG   . ASP   A 1 32  ? 20.39400 5.17000   1.40700  1.000 48.50743  ?  137 ASP   A CG   1 
ATOM   121  O  OD1  . ASP   A 1 32  ? 19.68200 4.22400   1.00900  1.000 55.88772  ?  137 ASP   A OD1  1 
ATOM   122  O  OD2  . ASP   A 1 32  ? 20.10300 6.36900   1.21600  1.000 54.22881  ?  137 ASP   A OD2  1 
ATOM   123  N  N    . ALA   A 1 33  ? 20.57700 3.47400   4.82300  1.000 43.16371  ?  138 ALA   A N    1 
ATOM   124  C  CA   . ALA   A 1 33  ? 19.47600 2.82000   5.52400  1.000 37.06915  ?  138 ALA   A CA   1 
ATOM   125  C  C    . ALA   A 1 33  ? 19.12500 3.55700   6.80900  1.000 41.08145  ?  138 ALA   A C    1 
ATOM   126  O  O    . ALA   A 1 33  ? 17.94300 3.75100   7.12000  1.000 37.18651  ?  138 ALA   A O    1 
ATOM   127  C  CB   . ALA   A 1 33  ? 19.83300 1.36500   5.82200  1.000 28.10977  ?  138 ALA   A CB   1 
ATOM   128  N  N    . HIS   A 1 34  ? 20.13900 3.97800   7.56900  1.000 33.55559  ?  139 HIS   A N    1 
ATOM   129  C  CA   . HIS   A 1 34  ? 19.88100 4.70800   8.80600  1.000 36.71165  ?  139 HIS   A CA   1 
ATOM   130  C  C    . HIS   A 1 34  ? 19.20900 6.04500   8.52600  1.000 35.55843  ?  139 HIS   A C    1 
ATOM   131  O  O    . HIS   A 1 34  ? 18.26800 6.43600   9.22700  1.000 39.73915  ?  139 HIS   A O    1 
ATOM   132  C  CB   . HIS   A 1 34  ? 21.18800 4.91300   9.57100  1.000 32.08734  ?  139 HIS   A CB   1 
ATOM   133  C  CG   . HIS   A 1 34  ? 21.04200 5.75000   10.80300 1.000 32.02563  ?  139 HIS   A CG   1 
ATOM   134  N  ND1  . HIS   A 1 34  ? 20.20700 5.40600   11.84500 1.000 33.46996  ?  139 HIS   A ND1  1 
ATOM   135  C  CD2  . HIS   A 1 34  ? 21.62300 6.92100   11.15800 1.000 39.53695  ?  139 HIS   A CD2  1 
ATOM   136  C  CE1  . HIS   A 1 34  ? 20.28200 6.32800   12.78900 1.000 34.83658  ?  139 HIS   A CE1  1 
ATOM   137  N  NE2  . HIS   A 1 34  ? 21.13300 7.25800   12.39600 1.000 36.93245  ?  139 HIS   A NE2  1 
ATOM   138  N  N    . HIS   A 1 35  ? 19.67600 6.76200   7.50100  1.000 34.73720  ?  140 HIS   A N    1 
ATOM   139  C  CA   . HIS   A 1 35  ? 19.07700 8.05100   7.17700  1.000 44.99675  ?  140 HIS   A CA   1 
ATOM   140  C  C    . HIS   A 1 35  ? 17.64600 7.89600   6.67600  1.000 45.45581  ?  140 HIS   A C    1 
ATOM   141  O  O    . HIS   A 1 35  ? 16.84000 8.82300   6.81400  1.000 43.71390  ?  140 HIS   A O    1 
ATOM   142  C  CB   . HIS   A 1 35  ? 19.93400 8.78500   6.14500  1.000 52.63314  ?  140 HIS   A CB   1 
ATOM   143  C  CG   . HIS   A 1 35  ? 21.20400 9.34500   6.70600  1.000 72.56692  ?  140 HIS   A CG   1 
ATOM   144  N  ND1  . HIS   A 1 35  ? 21.25800 10.55700  7.35900  1.000 79.55822  ?  140 HIS   A ND1  1 
ATOM   145  C  CD2  . HIS   A 1 35  ? 22.46700 8.85800   6.71500  1.000 77.23942  ?  140 HIS   A CD2  1 
ATOM   146  C  CE1  . HIS   A 1 35  ? 22.49900 10.79300  7.74500  1.000 78.79170  ?  140 HIS   A CE1  1 
ATOM   147  N  NE2  . HIS   A 1 35  ? 23.25300 9.77600   7.36700  1.000 74.93353  ?  140 HIS   A NE2  1 
ATOM   148  N  N    . LYS   A 1 36  ? 17.31000 6.73600   6.10900  1.000 38.81037  ?  141 LYS   A N    1 
ATOM   149  C  CA   . LYS   A 1 36  ? 15.94900 6.47300   5.65900  1.000 43.66295  ?  141 LYS   A CA   1 
ATOM   150  C  C    . LYS   A 1 36  ? 15.02800 6.03600   6.79100  1.000 47.51048  ?  141 LYS   A C    1 
ATOM   151  O  O    . LYS   A 1 36  ? 13.80500 6.05800   6.61600  1.000 38.13355  ?  141 LYS   A O    1 
ATOM   152  C  CB   . LYS   A 1 36  ? 15.94900 5.39800   4.56900  1.000 34.18033  ?  141 LYS   A CB   1 
ATOM   153  C  CG   . LYS   A 1 36  ? 16.18800 5.92300   3.16200  1.000 39.06650  ?  141 LYS   A CG   1 
ATOM   154  C  CD   . LYS   A 1 36  ? 16.33300 4.77600   2.17400  1.000 49.56516  ?  141 LYS   A CD   1 
ATOM   155  C  CE   . LYS   A 1 36  ? 16.34800 5.27600   0.73700  1.000 60.66354  ?  141 LYS   A CE   1 
ATOM   156  N  NZ   . LYS   A 1 36  ? 17.27000 6.43300   0.55600  1.000 60.57803  ?  141 LYS   A NZ   1 
ATOM   157  N  N    . THR   A 1 37  ? 15.58000 5.64000   7.93900  1.000 38.42818  ?  142 THR   A N    1 
ATOM   158  C  CA   . THR   A 1 37  ? 14.78800 5.09100   9.03500  1.000 39.85724  ?  142 THR   A CA   1 
ATOM   159  C  C    . THR   A 1 37  ? 14.90100 5.90300   10.31800 1.000 36.32423  ?  142 THR   A C    1 
ATOM   160  O  O    . THR   A 1 37  ? 14.36100 5.48700   11.35000 1.000 36.35158  ?  142 THR   A O    1 
ATOM   161  C  CB   . THR   A 1 37  ? 15.19500 3.64000   9.30900  1.000 40.60346  ?  142 THR   A CB   1 
ATOM   162  O  OG1  . THR   A 1 37  ? 16.62100 3.55800   9.43100  1.000 39.19768  ?  142 THR   A OG1  1 
ATOM   163  C  CG2  . THR   A 1 37  ? 14.73600 2.73700   8.17700  1.000 29.77828  ?  142 THR   A CG2  1 
ATOM   164  N  N    . TYR   A 1 38  ? 15.58900 7.04200   10.29100 1.000 39.34945  ?  143 TYR   A N    1 
ATOM   165  C  CA   . TYR   A 1 38  ? 15.72000 7.90800   11.45700 1.000 41.74775  ?  143 TYR   A CA   1 
ATOM   166  C  C    . TYR   A 1 38  ? 15.36200 9.32600   11.04400 1.000 44.88468  ?  143 TYR   A C    1 
ATOM   167  O  O    . TYR   A 1 38  ? 16.03500 9.91400   10.19000 1.000 45.61515  ?  143 TYR   A O    1 
ATOM   168  C  CB   . TYR   A 1 38  ? 17.13800 7.85200   12.03800 1.000 38.90704  ?  143 TYR   A CB   1 
ATOM   169  C  CG   . TYR   A 1 38  ? 17.26000 8.45800   13.42200 1.000 37.42491  ?  143 TYR   A CG   1 
ATOM   170  C  CD1  . TYR   A 1 38  ? 17.42000 9.82800   13.59100 1.000 41.91375  ?  143 TYR   A CD1  1 
ATOM   171  C  CD2  . TYR   A 1 38  ? 17.21600 7.65900   14.55900 1.000 38.47283  ?  143 TYR   A CD2  1 
ATOM   172  C  CE1  . TYR   A 1 38  ? 17.53100 10.38600  14.85200 1.000 45.53017  ?  143 TYR   A CE1  1 
ATOM   173  C  CE2  . TYR   A 1 38  ? 17.32600 8.20900   15.82600 1.000 36.26480  ?  143 TYR   A CE2  1 
ATOM   174  C  CZ   . TYR   A 1 38  ? 17.48300 9.57300   15.96500 1.000 41.62607  ?  143 TYR   A CZ   1 
ATOM   175  O  OH   . TYR   A 1 38  ? 17.59400 10.12800  17.21900 1.000 47.99218  ?  143 TYR   A OH   1 
ATOM   176  N  N    . ASP   A 1 39  ? 14.30400 9.87200   11.64700 1.000 44.89529  ?  144 ASP   A N    1 
ATOM   177  C  CA   . ASP   A 1 39  ? 13.84700 11.22400  11.36300 1.000 49.18971  ?  144 ASP   A CA   1 
ATOM   178  C  C    . ASP   A 1 39  ? 14.26100 12.13400  12.51300 1.000 57.13201  ?  144 ASP   A C    1 
ATOM   179  O  O    . ASP   A 1 39  ? 13.61600 12.11600  13.57300 1.000 52.05820  ?  144 ASP   A O    1 
ATOM   180  C  CB   . ASP   A 1 39  ? 12.32700 11.24700  11.17200 1.000 56.86197  ?  144 ASP   A CB   1 
ATOM   181  C  CG   . ASP   A 1 39  ? 11.80000 12.61700  10.77500 1.000 59.59402  ?  144 ASP   A CG   1 
ATOM   182  O  OD1  . ASP   A 1 39  ? 12.60700 13.55500  10.60600 1.000 53.67802  ?  144 ASP   A OD1  1 
ATOM   183  O  OD2  . ASP   A 1 39  ? 10.56700 12.75100  10.62700 1.000 59.90917  ?  144 ASP   A OD2  1 
ATOM   184  N  N    . PRO   A 1 40  ? 15.31800 12.94100  12.36500 1.000 53.70985  ?  145 PRO   A N    1 
ATOM   185  C  CA   . PRO   A 1 40  ? 15.73600 13.82600  13.46200 1.000 59.65261  ?  145 PRO   A CA   1 
ATOM   186  C  C    . PRO   A 1 40  ? 14.79500 14.99300  13.71500 1.000 62.00836  ?  145 PRO   A C    1 
ATOM   187  O  O    . PRO   A 1 40  ? 15.05700 15.78800  14.62500 1.000 63.72860  ?  145 PRO   A O    1 
ATOM   188  C  CB   . PRO   A 1 40  ? 17.11900 14.32100  13.01000 1.000 56.44548  ?  145 PRO   A CB   1 
ATOM   189  C  CG   . PRO   A 1 40  ? 17.12700 14.16300  11.53500 1.000 52.75503  ?  145 PRO   A CG   1 
ATOM   190  C  CD   . PRO   A 1 40  ? 16.22200 13.01200  11.20400 1.000 51.14604  ?  145 PRO   A CD   1 
ATOM   191  N  N    . THR   A 1 41  ? 13.71700 15.13800  12.94300 1.000 64.78302  ?  146 THR   A N    1 
ATOM   192  C  CA   . THR   A 1 41  ? 12.69100 16.11200  13.29100 1.000 62.58522  ?  146 THR   A CA   1 
ATOM   193  C  C    . THR   A 1 41  ? 11.71800 15.57000  14.32700 1.000 60.92418  ?  146 THR   A C    1 
ATOM   194  O  O    . THR   A 1 41  ? 11.05100 16.36100  15.00300 1.000 66.24917  ?  146 THR   A O    1 
ATOM   195  C  CB   . THR   A 1 41  ? 11.91600 16.55400  12.04600 1.000 63.70776  ?  146 THR   A CB   1 
ATOM   196  O  OG1  . THR   A 1 41  ? 11.03600 15.50400  11.62600 1.000 56.76334  ?  146 THR   A OG1  1 
ATOM   197  C  CG2  . THR   A 1 41  ? 12.87100 16.89600  10.91300 1.000 65.78739  ?  146 THR   A CG2  1 
ATOM   198  N  N    . TYR   A 1 42  ? 11.62900 14.24300  14.46400 1.000 51.81401  ?  147 TYR   A N    1 
ATOM   199  C  CA   . TYR   A 1 42  ? 10.72400 13.59500  15.41400 1.000 53.62034  ?  147 TYR   A CA   1 
ATOM   200  C  C    . TYR   A 1 42  ? 9.28000  14.04000  15.20300 1.000 55.22424  ?  147 TYR   A C    1 
ATOM   201  O  O    . TYR   A 1 42  ? 8.49700  14.12800  16.15200 1.000 48.83931  ?  147 TYR   A O    1 
ATOM   202  C  CB   . TYR   A 1 42  ? 11.17000 13.84500  16.85800 1.000 49.30175  ?  147 TYR   A CB   1 
ATOM   203  C  CG   . TYR   A 1 42  ? 12.63700 13.54800  17.08500 1.000 46.03856  ?  147 TYR   A CG   1 
ATOM   204  C  CD1  . TYR   A 1 42  ? 13.56700 14.57600  17.19200 1.000 44.93197  ?  147 TYR   A CD1  1 
ATOM   205  C  CD2  . TYR   A 1 42  ? 13.09500 12.23900  17.17900 1.000 44.13523  ?  147 TYR   A CD2  1 
ATOM   206  C  CE1  . TYR   A 1 42  ? 14.91000 14.30800  17.39400 1.000 47.55905  ?  147 TYR   A CE1  1 
ATOM   207  C  CE2  . TYR   A 1 42  ? 14.43700 11.96200  17.37900 1.000 51.93408  ?  147 TYR   A CE2  1 
ATOM   208  C  CZ   . TYR   A 1 42  ? 15.33800 13.00000  17.48600 1.000 52.03099  ?  147 TYR   A CZ   1 
ATOM   209  O  OH   . TYR   A 1 42  ? 16.67200 12.72700  17.68600 1.000 51.34815  ?  147 TYR   A OH   1 
ATOM   210  N  N    . ALA   A 1 43  ? 8.92400  14.31700  13.94600 1.000 61.63512  ?  148 ALA   A N    1 
ATOM   211  C  CA   . ALA   A 1 43  ? 7.58900  14.81800  13.64000 1.000 60.20544  ?  148 ALA   A CA   1 
ATOM   212  C  C    . ALA   A 1 43  ? 6.51900  13.77700  13.94100 1.000 57.94634  ?  148 ALA   A C    1 
ATOM   213  O  O    . ALA   A 1 43  ? 5.40700  14.12600  14.35100 1.000 65.85832  ?  148 ALA   A O    1 
ATOM   214  C  CB   . ALA   A 1 43  ? 7.51500  15.25200  12.17700 1.000 63.72664  ?  148 ALA   A CB   1 
ATOM   215  N  N    . ASP   A 1 44  ? 6.83300  12.49500  13.74900 1.000 48.64628  ?  149 ASP   A N    1 
ATOM   216  C  CA   . ASP   A 1 44  ? 5.84500  11.44800  13.98100 1.000 53.82761  ?  149 ASP   A CA   1 
ATOM   217  C  C    . ASP   A 1 44  ? 5.44700  11.32400  15.44600 1.000 57.20732  ?  149 ASP   A C    1 
ATOM   218  O  O    . ASP   A 1 44  ? 4.47400  10.62400  15.74700 1.000 62.41798  ?  149 ASP   A O    1 
ATOM   219  C  CB   . ASP   A 1 44  ? 6.37600  10.10600  13.47400 1.000 46.52311  ?  149 ASP   A CB   1 
ATOM   220  C  CG   . ASP   A 1 44  ? 6.66300  10.12000  11.98600 1.000 58.77222  ?  149 ASP   A CG   1 
ATOM   221  O  OD1  . ASP   A 1 44  ? 5.94200  10.82400  11.24900 1.000 63.67636  ?  149 ASP   A OD1  1 
ATOM   222  O  OD2  . ASP   A 1 44  ? 7.61200  9.43100   11.55500 1.000 67.26842  ?  149 ASP   A OD2  1 
ATOM   223  N  N    . PHE   A 1 45  ? 6.16100  11.99300  16.35600 1.000 61.67893  ?  150 PHE   A N    1 
ATOM   224  C  CA   . PHE   A 1 45  ? 5.84800  11.90200  17.77700 1.000 57.41431  ?  150 PHE   A CA   1 
ATOM   225  C  C    . PHE   A 1 45  ? 4.48000  12.48800  18.11000 1.000 68.79745  ?  150 PHE   A C    1 
ATOM   226  O  O    . PHE   A 1 45  ? 3.90700  12.13900  19.14800 1.000 63.65253  ?  150 PHE   A O    1 
ATOM   227  C  CB   . PHE   A 1 45  ? 6.92500  12.61100  18.60400 1.000 49.80952  ?  150 PHE   A CB   1 
ATOM   228  C  CG   . PHE   A 1 45  ? 8.19200  11.81200  18.78600 1.000 57.91004  ?  150 PHE   A CG   1 
ATOM   229  C  CD1  . PHE   A 1 45  ? 8.64600  10.95200  17.79700 1.000 57.85384  ?  150 PHE   A CD1  1 
ATOM   230  C  CD2  . PHE   A 1 45  ? 8.93200  11.92800  19.95300 1.000 57.61432  ?  150 PHE   A CD2  1 
ATOM   231  C  CE1  . PHE   A 1 45  ? 9.81000  10.22500  17.96900 1.000 58.74563  ?  150 PHE   A CE1  1 
ATOM   232  C  CE2  . PHE   A 1 45  ? 10.09700 11.20200  20.13100 1.000 56.31166  ?  150 PHE   A CE2  1 
ATOM   233  C  CZ   . PHE   A 1 45  ? 10.53700 10.35000  19.13700 1.000 56.72484  ?  150 PHE   A CZ   1 
ATOM   234  N  N    A ARG   A 1 46  ? 3.94800  13.36700  17.25700 0.820 77.27022  ?  151 ARG   A N    1 
ATOM   235  N  N    B ARG   A 1 46  ? 3.94300  13.36900  17.26000 0.180 77.61011  ?  151 ARG   A N    1 
ATOM   236  C  CA   A ARG   A 1 46  ? 2.64200  13.96500  17.51100 0.820 82.08586  ?  151 ARG   A CA   1 
ATOM   237  C  CA   B ARG   A 1 46  ? 2.63500  13.95200  17.54100 0.180 82.04848  ?  151 ARG   A CA   1 
ATOM   238  C  C    A ARG   A 1 46  ? 1.50600  12.96400  17.35400 0.820 78.68126  ?  151 ARG   A C    1 
ATOM   239  C  C    B ARG   A 1 46  ? 1.52100  12.92100  17.41800 0.180 78.24974  ?  151 ARG   A C    1 
ATOM   240  O  O    A ARG   A 1 46  ? 0.42700  13.17700  17.91700 0.820 79.79313  ?  151 ARG   A O    1 
ATOM   241  O  O    B ARG   A 1 46  ? 0.47300  13.06500  18.05700 0.180 79.82308  ?  151 ARG   A O    1 
ATOM   242  C  CB   A ARG   A 1 46  ? 2.42100  15.15300  16.57500 0.820 89.48467  ?  151 ARG   A CB   1 
ATOM   243  C  CB   B ARG   A 1 46  ? 2.35200  15.13000  16.60600 0.180 89.45163  ?  151 ARG   A CB   1 
ATOM   244  C  CG   A ARG   A 1 46  ? 3.65800  16.00900  16.36800 0.820 94.41727  ?  151 ARG   A CG   1 
ATOM   245  C  CG   B ARG   A 1 46  ? 3.57800  15.87800  16.10600 0.180 94.63864  ?  151 ARG   A CG   1 
ATOM   246  C  CD   A ARG   A 1 46  ? 3.54200  17.33300  17.09800 0.820 100.95681 ?  151 ARG   A CD   1 
ATOM   247  C  CD   B ARG   A 1 46  ? 4.33200  16.58900  17.22100 0.180 98.98322  ?  151 ARG   A CD   1 
ATOM   248  N  NE   A ARG   A 1 46  ? 4.21800  18.40600  16.37700 0.820 105.25578 ?  151 ARG   A NE   1 
ATOM   249  N  NE   B ARG   A 1 46  ? 4.08400  18.03000  17.24400 0.180 104.26190 ?  151 ARG   A NE   1 
ATOM   250  C  CZ   A ARG   A 1 46  ? 4.41000  19.62700  16.86400 0.820 108.18098 ?  151 ARG   A CZ   1 
ATOM   251  C  CZ   B ARG   A 1 46  ? 4.42900  18.88300  16.28200 0.180 106.38801 ?  151 ARG   A CZ   1 
ATOM   252  N  NH1  A ARG   A 1 46  ? 3.97400  19.93500  18.07800 0.820 108.20630 ?  151 ARG   A NH1  1 
ATOM   253  N  NH1  B ARG   A 1 46  ? 4.14600  20.17000  16.41500 0.180 109.20516 ?  151 ARG   A NH1  1 
ATOM   254  N  NH2  A ARG   A 1 46  ? 5.03700  20.53900  16.13400 0.820 110.20649 ?  151 ARG   A NH2  1 
ATOM   255  N  NH2  B ARG   A 1 46  ? 5.06100  18.46300  15.19400 0.180 105.95738 ?  151 ARG   A NH2  1 
ATOM   256  N  N    . ASP   A 1 47  ? 1.72200  11.88300  16.60400 1.000 65.92716  ?  152 ASP   A N    1 
ATOM   257  C  CA   . ASP   A 1 47  ? 0.71000  10.84900  16.44200 1.000 60.88603  ?  152 ASP   A CA   1 
ATOM   258  C  C    . ASP   A 1 47  ? 0.65500  9.88800   17.62000 1.000 59.37912  ?  152 ASP   A C    1 
ATOM   259  O  O    . ASP   A 1 47  ? -0.29100 9.09700   17.70900 1.000 63.23676  ?  152 ASP   A O    1 
ATOM   260  C  CB   . ASP   A 1 47  ? 0.95500  10.06800  15.14800 1.000 57.97174  ?  152 ASP   A CB   1 
ATOM   261  C  CG   . ASP   A 1 47  ? 0.85800  10.94400  13.91400 1.000 63.62811  ?  152 ASP   A CG   1 
ATOM   262  O  OD1  . ASP   A 1 47  ? -0.02300 11.82800  13.88200 1.000 66.97741  ?  152 ASP   A OD1  1 
ATOM   263  O  OD2  . ASP   A 1 47  ? 1.66000  10.74600  12.97700 1.000 65.34203  ?  152 ASP   A OD2  1 
ATOM   264  N  N    . PHE   A 1 48  ? 1.63700  9.93500   18.51700 1.000 51.85303  ?  153 PHE   A N    1 
ATOM   265  C  CA   . PHE   A 1 48  ? 1.60800  9.09900   19.70500 1.000 50.03821  ?  153 PHE   A CA   1 
ATOM   266  C  C    . PHE   A 1 48  ? 0.52000  9.57700   20.66100 1.000 50.67321  ?  153 PHE   A C    1 
ATOM   267  O  O    . PHE   A 1 48  ? -0.00700 10.68800  20.54500 1.000 52.73503  ?  153 PHE   A O    1 
ATOM   268  C  CB   . PHE   A 1 48  ? 2.95300  9.12600   20.43600 1.000 45.86760  ?  153 PHE   A CB   1 
ATOM   269  C  CG   . PHE   A 1 48  ? 4.12900  8.70900   19.59300 1.000 50.10437  ?  153 PHE   A CG   1 
ATOM   270  C  CD1  . PHE   A 1 48  ? 5.41700  9.03500   19.99000 1.000 41.42980  ?  153 PHE   A CD1  1 
ATOM   271  C  CD2  . PHE   A 1 48  ? 3.95800  7.98600   18.42300 1.000 46.16284  ?  153 PHE   A CD2  1 
ATOM   272  C  CE1  . PHE   A 1 48  ? 6.50800  8.65800   19.23500 1.000 51.78996  ?  153 PHE   A CE1  1 
ATOM   273  C  CE2  . PHE   A 1 48  ? 5.04800  7.60900   17.66000 1.000 49.38742  ?  153 PHE   A CE2  1 
ATOM   274  C  CZ   . PHE   A 1 48  ? 6.32400  7.94500   18.06800 1.000 49.48505  ?  153 PHE   A CZ   1 
ATOM   275  N  N    . ARG   A 1 49  ? 0.18900  8.72300   21.61900 1.000 38.97106  ?  154 ARG   A N    1 
ATOM   276  C  CA   . ARG   A 1 49  ? -0.61200 9.18000   22.73900 1.000 46.47416  ?  154 ARG   A CA   1 
ATOM   277  C  C    . ARG   A 1 49  ? 0.19200  10.20300  23.54000 1.000 45.32087  ?  154 ARG   A C    1 
ATOM   278  O  O    . ARG   A 1 49  ? 1.40400  10.04400  23.70500 1.000 46.42558  ?  154 ARG   A O    1 
ATOM   279  C  CB   . ARG   A 1 49  ? -1.02900 8.00200   23.61300 1.000 50.06115  ?  154 ARG   A CB   1 
ATOM   280  C  CG   . ARG   A 1 49  ? -2.07700 7.13300   22.94000 1.000 45.29429  ?  154 ARG   A CG   1 
ATOM   281  C  CD   . ARG   A 1 49  ? -2.26900 5.82400   23.66300 1.000 40.89864  ?  154 ARG   A CD   1 
ATOM   282  N  NE   . ARG   A 1 49  ? -1.15400 4.90000   23.48400 1.000 40.73209  ?  154 ARG   A NE   1 
ATOM   283  C  CZ   . ARG   A 1 49  ? -1.08200 3.69800   24.04900 1.000 36.84330  ?  154 ARG   A CZ   1 
ATOM   284  N  NH1  . ARG   A 1 49  ? -2.05700 3.27200   24.84200 1.000 37.78878  ?  154 ARG   A NH1  1 
ATOM   285  N  NH2  . ARG   A 1 49  ? -0.03100 2.92200   23.82500 1.000 35.33804  ?  154 ARG   A NH2  1 
ATOM   286  N  N    . PRO   A 1 50  ? -0.44900 11.26600  24.03300 1.000 47.23767  ?  155 PRO   A N    1 
ATOM   287  C  CA   . PRO   A 1 50  ? 0.31700  12.41300  24.51500 1.000 54.13954  ?  155 PRO   A CA   1 
ATOM   288  C  C    . PRO   A 1 50  ? 1.12400  12.05900  25.75200 1.000 59.80880  ?  155 PRO   A C    1 
ATOM   289  O  O    . PRO   A 1 50  ? 0.70400  11.22000  26.56500 1.000 58.49370  ?  155 PRO   A O    1 
ATOM   290  C  CB   . PRO   A 1 50  ? -0.77300 13.45400  24.83400 1.000 49.58629  ?  155 PRO   A CB   1 
ATOM   291  C  CG   . PRO   A 1 50  ? -1.99000 12.64100  25.10700 1.000 52.15281  ?  155 PRO   A CG   1 
ATOM   292  C  CD   . PRO   A 1 50  ? -1.89900 11.46200  24.18400 1.000 47.11215  ?  155 PRO   A CD   1 
ATOM   293  N  N    . PRO   A 1 51  ? 2.29400  12.67000  25.92800 1.000 62.24774  ?  156 PRO   A N    1 
ATOM   294  C  CA   . PRO   A 1 51  ? 3.04100  12.47800  27.17800 1.000 62.93844  ?  156 PRO   A CA   1 
ATOM   295  C  C    . PRO   A 1 51  ? 2.26000  13.06200  28.34300 1.000 69.53022  ?  156 PRO   A C    1 
ATOM   296  O  O    . PRO   A 1 51  ? 1.78900  14.20000  28.28900 1.000 69.94752  ?  156 PRO   A O    1 
ATOM   297  C  CB   . PRO   A 1 51  ? 4.35400  13.23500  26.94000 1.000 53.37053  ?  156 PRO   A CB   1 
ATOM   298  C  CG   . PRO   A 1 51  ? 4.39500  13.54000  25.48300 1.000 56.88118  ?  156 PRO   A CG   1 
ATOM   299  C  CD   . PRO   A 1 51  ? 2.98300  13.57900  25.00100 1.000 58.82712  ?  156 PRO   A CD   1 
ATOM   300  N  N    . VAL   A 1 52  ? 2.11000  12.26800  29.39500 1.000 67.67356  ?  157 VAL   A N    1 
ATOM   301  C  CA   . VAL   A 1 52  ? 1.34100  12.66200  30.56500 1.000 66.48124  ?  157 VAL   A CA   1 
ATOM   302  C  C    . VAL   A 1 52  ? 2.27100  12.57600  31.76300 1.000 70.66656  ?  157 VAL   A C    1 
ATOM   303  O  O    . VAL   A 1 52  ? 2.72400  11.48400  32.13000 1.000 64.35716  ?  157 VAL   A O    1 
ATOM   304  C  CB   . VAL   A 1 52  ? 0.09200  11.78900  30.75800 1.000 67.37856  ?  157 VAL   A CB   1 
ATOM   305  C  CG1  . VAL   A 1 52  ? -0.45300 11.92600  32.17100 1.000 73.57703  ?  157 VAL   A CG1  1 
ATOM   306  C  CG2  . VAL   A 1 52  ? -0.96900 12.15100  29.72600 1.000 64.35973  ?  157 VAL   A CG2  1 
ATOM   307  N  N    . ARG   A 1 53  ? 2.58000  13.71000  32.39000 1.000 79.67480  ?  158 ARG   A N    1 
ATOM   308  C  CA   . ARG   A 1 53  ? 3.48400  13.67800  33.57300 1.000 83.01465  ?  158 ARG   A CA   1 
ATOM   309  C  C    . ARG   A 1 53  ? 2.68300  13.93500  34.85200 1.000 93.35048  ?  158 ARG   A C    1 
ATOM   310  O  O    . ARG   A 1 53  ? 2.12200  15.02800  34.93900 1.000 96.54747  ?  158 ARG   A O    1 
ATOM   311  C  CB   . ARG   A 1 53  ? 4.62400  14.68400  33.43200 1.000 78.75664  ?  158 ARG   A CB   1 
ATOM   312  C  CG   . ARG   A 1 53  ? 5.88700  14.11900  32.80400 1.000 75.97570  ?  158 ARG   A CG   1 
ATOM   313  C  CD   . ARG   A 1 53  ? 6.04600  14.66300  31.40800 1.000 73.01190  ?  158 ARG   A CD   1 
ATOM   314  N  NE   . ARG   A 1 53  ? 7.25700  14.27800  30.71100 1.000 70.55061  ?  158 ARG   A NE   1 
ATOM   315  C  CZ   . ARG   A 1 53  ? 7.49700  14.55800  29.44700 1.000 68.10934  ?  158 ARG   A CZ   1 
ATOM   316  N  NH1  . ARG   A 1 53  ? 6.61200  15.23400  28.74400 1.000 63.09339  ?  158 ARG   A NH1  1 
ATOM   317  N  NH2  . ARG   A 1 53  ? 8.62100  14.16800  28.88900 1.000 64.56572  ?  158 ARG   A NH2  1 
ATOM   318  N  N    . PRO   A 1 67  ? 0.20800  7.14100   38.54100 1.000 113.62427 ?  219 PRO   A N    1 
ATOM   319  C  CA   . PRO   A 1 67  ? 1.46500  6.42600   38.39300 1.000 108.97158 ?  219 PRO   A CA   1 
ATOM   320  C  C    . PRO   A 1 67  ? 1.46800  5.72600   37.03100 1.000 96.74024  ?  219 PRO   A C    1 
ATOM   321  O  O    . PRO   A 1 67  ? 0.44500  5.36400   36.53400 1.000 95.53057  ?  219 PRO   A O    1 
ATOM   322  C  CB   . PRO   A 1 67  ? 1.34200  5.43300   39.55100 1.000 113.00156 ?  219 PRO   A CB   1 
ATOM   323  C  CG   . PRO   A 1 67  ? -0.07600 4.97000   39.43700 1.000 115.66711 ?  219 PRO   A CG   1 
ATOM   324  C  CD   . PRO   A 1 67  ? -0.81000 6.12200   38.78200 1.000 115.70986 ?  219 PRO   A CD   1 
ATOM   325  N  N    . LEU   A 1 68  ? 2.63900  5.50400   36.46400 1.000 89.09357  ?  220 LEU   A N    1 
ATOM   326  C  CA   . LEU   A 1 68  ? 2.63000  4.90800   35.12500 1.000 67.88759  ?  220 LEU   A CA   1 
ATOM   327  C  C    . LEU   A 1 68  ? 1.97100  5.82300   34.09500 1.000 48.01003  ?  220 LEU   A C    1 
ATOM   328  O  O    . LEU   A 1 68  ? 1.43900  5.35700   33.08400 1.000 45.41772  ?  220 LEU   A O    1 
ATOM   329  C  CB   . LEU   A 1 68  ? 1.95400  3.53300   35.12700 1.000 66.56303  ?  220 LEU   A CB   1 
ATOM   330  C  CG   . LEU   A 1 68  ? 2.42500  2.48700   36.14200 1.000 71.37674  ?  220 LEU   A CG   1 
ATOM   331  C  CD1  . LEU   A 1 68  ? 2.12000  1.08700   35.63900 1.000 74.94607  ?  220 LEU   A CD1  1 
ATOM   332  C  CD2  . LEU   A 1 68  ? 3.90600  2.62400   36.44700 1.000 70.10779  ?  220 LEU   A CD2  1 
ATOM   333  N  N    . SER   A 1 69  ? 2.02300  7.13500   34.33400 1.000 48.32717  ?  221 SER   A N    1 
ATOM   334  C  CA   . SER   A 1 69  ? 1.38600  8.08900   33.43400 1.000 54.38890  ?  221 SER   A CA   1 
ATOM   335  C  C    . SER   A 1 69  ? 2.08100  8.18000   32.08200 1.000 51.16015  ?  221 SER   A C    1 
ATOM   336  O  O    . SER   A 1 69  ? 1.45600  8.60700   31.10500 1.000 44.19877  ?  221 SER   A O    1 
ATOM   337  C  CB   . SER   A 1 69  ? 1.34300  9.46800   34.08800 1.000 55.54848  ?  221 SER   A CB   1 
ATOM   338  O  OG   . SER   A 1 69  ? 2.64900  9.99700   34.24400 1.000 64.31032  ?  221 SER   A OG   1 
ATOM   339  N  N    . MET   A 1 70  ? 3.34900  7.79000   31.99800 1.000 46.57364  ?  222 MET   A N    1 
ATOM   340  C  CA   . MET   A 1 70  ? 4.09300  7.86100   30.74800 1.000 41.32658  ?  222 MET   A CA   1 
ATOM   341  C  C    . MET   A 1 70  ? 4.06600  6.55800   29.96200 1.000 38.26156  ?  222 MET   A C    1 
ATOM   342  O  O    . MET   A 1 70  ? 4.61600  6.50900   28.85600 1.000 43.25456  ?  222 MET   A O    1 
ATOM   343  C  CB   . MET   A 1 70  ? 5.54600  8.26600   31.02000 1.000 43.14729  ?  222 MET   A CB   1 
ATOM   344  C  CG   . MET   A 1 70  ? 5.71200  9.72400   31.40700 1.000 52.21680  ?  222 MET   A CG   1 
ATOM   345  S  SD   . MET   A 1 70  ? 5.34300  10.83400  30.03500 1.000 51.77429  ?  222 MET   A SD   1 
ATOM   346  C  CE   . MET   A 1 70  ? 6.79200  10.58100  29.01300 1.000 44.03188  ?  222 MET   A CE   1 
ATOM   347  N  N    . LEU   A 1 71  ? 3.44500  5.50900   30.50200 1.000 40.62098  ?  223 LEU   A N    1 
ATOM   348  C  CA   . LEU   A 1 71  ? 3.41600  4.22100   29.81200 1.000 41.65232  ?  223 LEU   A CA   1 
ATOM   349  C  C    . LEU   A 1 71  ? 2.75400  4.29000   28.44100 1.000 49.07784  ?  223 LEU   A C    1 
ATOM   350  O  O    . LEU   A 1 71  ? 3.31200  3.72200   27.48600 1.000 45.65532  ?  223 LEU   A O    1 
ATOM   351  C  CB   . LEU   A 1 71  ? 2.74200  3.17400   30.70500 1.000 43.82522  ?  223 LEU   A CB   1 
ATOM   352  C  CG   . LEU   A 1 71  ? 2.57000  1.78200   30.09400 1.000 51.75332  ?  223 LEU   A CG   1 
ATOM   353  C  CD1  . LEU   A 1 71  ? 3.89900  1.24800   29.57700 1.000 46.76032  ?  223 LEU   A CD1  1 
ATOM   354  C  CD2  . LEU   A 1 71  ? 1.95600  0.82100   31.10100 1.000 57.70023  ?  223 LEU   A CD2  1 
ATOM   355  N  N    . PRO   A 1 72  ? 1.59100  4.93300   28.25800 1.000 45.91029  ?  224 PRO   A N    1 
ATOM   356  C  CA   . PRO   A 1 72  ? 1.02300  4.99700   26.89900 1.000 38.36250  ?  224 PRO   A CA   1 
ATOM   357  C  C    . PRO   A 1 72  ? 1.92700  5.70000   25.90300 1.000 44.07869  ?  224 PRO   A C    1 
ATOM   358  O  O    . PRO   A 1 72  ? 2.09800  5.21300   24.77800 1.000 41.45624  ?  224 PRO   A O    1 
ATOM   359  C  CB   . PRO   A 1 72  ? -0.29800 5.75300   27.10800 1.000 39.53033  ?  224 PRO   A CB   1 
ATOM   360  C  CG   . PRO   A 1 72  ? -0.64600 5.51200   28.52900 1.000 40.46011  ?  224 PRO   A CG   1 
ATOM   361  C  CD   . PRO   A 1 72  ? 0.66600  5.51100   29.25200 1.000 38.48482  ?  224 PRO   A CD   1 
ATOM   362  N  N    . HIS   A 1 73  ? 2.52300  6.83200   26.28700 1.000 44.07523  ?  225 HIS   A N    1 
ATOM   363  C  CA   . HIS   A 1 73  ? 3.40600  7.54200   25.36700 1.000 46.50784  ?  225 HIS   A CA   1 
ATOM   364  C  C    . HIS   A 1 73  ? 4.67100  6.74200   25.08200 1.000 44.66508  ?  225 HIS   A C    1 
ATOM   365  O  O    . HIS   A 1 73  ? 5.12200  6.67500   23.93200 1.000 49.00099  ?  225 HIS   A O    1 
ATOM   366  C  CB   . HIS   A 1 73  ? 3.76100  8.91900   25.92900 1.000 46.10387  ?  225 HIS   A CB   1 
ATOM   367  C  CG   . HIS   A 1 73  ? 4.55800  9.76500   24.98600 1.000 49.42143  ?  225 HIS   A CG   1 
ATOM   368  N  ND1  . HIS   A 1 73  ? 4.00100  10.37700  23.88400 1.000 45.47553  ?  225 HIS   A ND1  1 
ATOM   369  C  CD2  . HIS   A 1 73  ? 5.87200  10.09400  24.97500 1.000 39.43642  ?  225 HIS   A CD2  1 
ATOM   370  C  CE1  . HIS   A 1 73  ? 4.93700  11.04900  23.23600 1.000 43.48897  ?  225 HIS   A CE1  1 
ATOM   371  N  NE2  . HIS   A 1 73  ? 6.08100  10.89400  23.87800 1.000 44.44015  ?  225 HIS   A NE2  1 
ATOM   372  N  N    . LEU   A 1 74  ? 5.25400  6.12500   26.11200 1.000 41.28464  ?  226 LEU   A N    1 
ATOM   373  C  CA   . LEU   A 1 74  ? 6.48100  5.36100   25.91000 1.000 42.96819  ?  226 LEU   A CA   1 
ATOM   374  C  C    . LEU   A 1 74  ? 6.21700  4.05600   25.16800 1.000 38.61114  ?  226 LEU   A C    1 
ATOM   375  O  O    . LEU   A 1 74  ? 7.10800  3.55100   24.47600 1.000 34.15538  ?  226 LEU   A O    1 
ATOM   376  C  CB   . LEU   A 1 74  ? 7.16000  5.08500   27.25200 1.000 40.81653  ?  226 LEU   A CB   1 
ATOM   377  C  CG   . LEU   A 1 74  ? 8.35000  5.98800   27.58300 1.000 53.95008  ?  226 LEU   A CG   1 
ATOM   378  C  CD1  . LEU   A 1 74  ? 8.01900  7.44900   27.30800 1.000 51.89870  ?  226 LEU   A CD1  1 
ATOM   379  C  CD2  . LEU   A 1 74  ? 8.79000  5.79300   29.02300 1.000 55.15250  ?  226 LEU   A CD2  1 
ATOM   380  N  N    . ALA   A 1 75  ? 5.01300  3.49500   25.30300 1.000 37.81872  ?  227 ALA   A N    1 
ATOM   381  C  CA   . ALA   A 1 75  ? 4.66700  2.31000   24.52400 1.000 36.89674  ?  227 ALA   A CA   1 
ATOM   382  C  C    . ALA   A 1 75  ? 4.56300  2.64100   23.04100 1.000 37.77159  ?  227 ALA   A C    1 
ATOM   383  O  O    . ALA   A 1 75  ? 5.03400  1.87400   22.19400 1.000 39.52802  ?  227 ALA   A O    1 
ATOM   384  C  CB   . ALA   A 1 75  ? 3.35800  1.70600   25.03200 1.000 37.79089  ?  227 ALA   A CB   1 
ATOM   385  N  N    . ASP   A 1 76  ? 3.94600  3.77800   22.70900 1.000 43.45698  ?  228 ASP   A N    1 
ATOM   386  C  CA   . ASP   A 1 76  ? 3.88800  4.20800   21.31700 1.000 40.52761  ?  228 ASP   A CA   1 
ATOM   387  C  C    . ASP   A 1 76  ? 5.27800  4.53600   20.78600 1.000 41.42186  ?  228 ASP   A C    1 
ATOM   388  O  O    . ASP   A 1 76  ? 5.58300  4.26600   19.61800 1.000 34.48189  ?  228 ASP   A O    1 
ATOM   389  C  CB   . ASP   A 1 76  ? 2.95900  5.41500   21.18200 1.000 37.54311  ?  228 ASP   A CB   1 
ATOM   390  C  CG   . ASP   A 1 76  ? 1.49600  5.04800   21.34700 1.000 41.08102  ?  228 ASP   A CG   1 
ATOM   391  O  OD1  . ASP   A 1 76  ? 0.67500  5.95800   21.58800 1.000 43.58768  ?  228 ASP   A OD1  1 
ATOM   392  O  OD2  . ASP   A 1 76  ? 1.16600  3.84900   21.23900 1.000 41.06685  ?  228 ASP   A OD2  1 
ATOM   393  N  N    . LEU   A 1 77  ? 6.13500  5.11200   21.63300 1.000 35.22392  ?  229 LEU   A N    1 
ATOM   394  C  CA   . LEU   A 1 77  ? 7.49000  5.45100   21.20900 1.000 35.27286  ?  229 LEU   A CA   1 
ATOM   395  C  C    . LEU   A 1 77  ? 8.28400  4.19900   20.85300 1.000 35.50079  ?  229 LEU   A C    1 
ATOM   396  O  O    . LEU   A 1 77  ? 8.95400  4.14900   19.81600 1.000 40.12531  ?  229 LEU   A O    1 
ATOM   397  C  CB   . LEU   A 1 77  ? 8.19300  6.24700   22.31000 1.000 43.76376  ?  229 LEU   A CB   1 
ATOM   398  C  CG   . LEU   A 1 77  ? 9.67800  6.56700   22.11600 1.000 54.81962  ?  229 LEU   A CG   1 
ATOM   399  C  CD1  . LEU   A 1 77  ? 9.90400  7.32500   20.81600 1.000 49.96744  ?  229 LEU   A CD1  1 
ATOM   400  C  CD2  . LEU   A 1 77  ? 10.21700 7.35500   23.30300 1.000 52.34811  ?  229 LEU   A CD2  1 
ATOM   401  N  N    . VAL   A 1 78  ? 8.21600  3.17500   21.70500 1.000 38.20887  ?  230 VAL   A N    1 
ATOM   402  C  CA   . VAL   A 1 78  ? 8.92400  1.92700   21.43300 1.000 36.52138  ?  230 VAL   A CA   1 
ATOM   403  C  C    . VAL   A 1 78  ? 8.33200  1.23200   20.21500 1.000 30.06576  ?  230 VAL   A C    1 
ATOM   404  O  O    . VAL   A 1 78  ? 9.06100  0.73800   19.34600 1.000 32.74122  ?  230 VAL   A O    1 
ATOM   405  C  CB   . VAL   A 1 78  ? 8.88800  1.00900   22.66500 1.000 41.86456  ?  230 VAL   A CB   1 
ATOM   406  C  CG1  . VAL   A 1 78  ? 9.45200  -0.34800  22.31400 1.000 52.20528  ?  230 VAL   A CG1  1 
ATOM   407  C  CG2  . VAL   A 1 78  ? 9.67400  1.61900   23.78500 1.000 53.54900  ?  230 VAL   A CG2  1 
ATOM   408  N  N    . SER   A 1 79  ? 7.00000  1.16500   20.14700 1.000 30.43996  ?  231 SER   A N    1 
ATOM   409  C  CA   . SER   A 1 79  ? 6.34600  0.53700   19.00400 1.000 21.39110  ?  231 SER   A CA   1 
ATOM   410  C  C    . SER   A 1 79  ? 6.76200  1.20400   17.70000 1.000 26.39038  ?  231 SER   A C    1 
ATOM   411  O  O    . SER   A 1 79  ? 7.07200  0.52400   16.71500 1.000 31.39805  ?  231 SER   A O    1 
ATOM   412  C  CB   . SER   A 1 79  ? 4.82800  0.60000   19.17700 1.000 25.11565  ?  231 SER   A CB   1 
ATOM   413  O  OG   . SER   A 1 79  ? 4.17600  -0.25200  18.25200 1.000 37.08908  ?  231 SER   A OG   1 
ATOM   414  N  N    . TYR   A 1 80  ? 6.77000  2.53800   17.68000 1.000 30.11376  ?  232 TYR   A N    1 
ATOM   415  C  CA   . TYR   A 1 80  ? 7.25200  3.26800   16.51300 1.000 26.90591  ?  232 TYR   A CA   1 
ATOM   416  C  C    . TYR   A 1 80  ? 8.71100  2.93100   16.21700 1.000 32.73948  ?  232 TYR   A C    1 
ATOM   417  O  O    . TYR   A 1 80  ? 9.08200  2.70300   15.06000 1.000 30.41134  ?  232 TYR   A O    1 
ATOM   418  C  CB   . TYR   A 1 80  ? 7.07000  4.76900   16.74800 1.000 31.16596  ?  232 TYR   A CB   1 
ATOM   419  C  CG   . TYR   A 1 80  ? 7.72400  5.66700   15.72600 1.000 41.60048  ?  232 TYR   A CG   1 
ATOM   420  C  CD1  . TYR   A 1 80  ? 7.06300  6.01500   14.55600 1.000 42.83386  ?  232 TYR   A CD1  1 
ATOM   421  C  CD2  . TYR   A 1 80  ? 8.99300  6.19000   15.94300 1.000 45.35970  ?  232 TYR   A CD2  1 
ATOM   422  C  CE1  . TYR   A 1 80  ? 7.65400  6.84400   13.62200 1.000 40.76553  ?  232 TYR   A CE1  1 
ATOM   423  C  CE2  . TYR   A 1 80  ? 9.59200  7.01800   15.01400 1.000 39.80809  ?  232 TYR   A CE2  1 
ATOM   424  C  CZ   . TYR   A 1 80  ? 8.91900  7.34200   13.85700 1.000 41.36332  ?  232 TYR   A CZ   1 
ATOM   425  O  OH   . TYR   A 1 80  ? 9.51400  8.17000   12.93300 1.000 49.98317  ?  232 TYR   A OH   1 
ATOM   426  N  N    . SER   A 1 81  ? 9.54800  2.87600   17.25700 1.000 31.48422  ?  233 SER   A N    1 
ATOM   427  C  CA   . SER   A 1 81  ? 10.96800 2.59500   17.05700 1.000 36.48821  ?  233 SER   A CA   1 
ATOM   428  C  C    . SER   A 1 81  ? 11.19100 1.17800   16.54100 1.000 29.24674  ?  233 SER   A C    1 
ATOM   429  O  O    . SER   A 1 81  ? 12.09300 0.94500   15.72600 1.000 28.79937  ?  233 SER   A O    1 
ATOM   430  C  CB   . SER   A 1 81  ? 11.74000 2.81400   18.36000 1.000 36.60413  ?  233 SER   A CB   1 
ATOM   431  O  OG   . SER   A 1 81  ? 11.74500 4.17900   18.73600 1.000 43.14013  ?  233 SER   A OG   1 
ATOM   432  N  N    . ILE   A 1 82  ? 10.38700 0.21900   17.00800 1.000 27.07625  ?  234 ILE   A N    1 
ATOM   433  C  CA   . ILE   A 1 82  ? 10.48600 -1.14500  16.49500 1.000 27.75619  ?  234 ILE   A CA   1 
ATOM   434  C  C    . ILE   A 1 82  ? 10.29800 -1.15600  14.98300 1.000 31.71110  ?  234 ILE   A C    1 
ATOM   435  O  O    . ILE   A 1 82  ? 11.02300 -1.84700  14.25700 1.000 31.51320  ?  234 ILE   A O    1 
ATOM   436  C  CB   . ILE   A 1 82  ? 9.46700  -2.05800  17.20100 1.000 30.10454  ?  234 ILE   A CB   1 
ATOM   437  C  CG1  . ILE   A 1 82  ? 9.88200  -2.31000  18.65100 1.000 34.81027  ?  234 ILE   A CG1  1 
ATOM   438  C  CG2  . ILE   A 1 82  ? 9.32300  -3.37800  16.46100 1.000 29.33854  ?  234 ILE   A CG2  1 
ATOM   439  C  CD1  . ILE   A 1 82  ? 8.75300  -2.83700  19.52400 1.000 30.05447  ?  234 ILE   A CD1  1 
ATOM   440  N  N    . GLN   A 1 83  ? 9.33600  -0.37200  14.48300 1.000 34.49282  ?  235 GLN   A N    1 
ATOM   441  C  CA   . GLN   A 1 83  ? 9.11300  -0.29000  13.04200 1.000 35.82096  ?  235 GLN   A CA   1 
ATOM   442  C  C    . GLN   A 1 83  ? 10.34800 0.22900   12.31900 1.000 28.18143  ?  235 GLN   A C    1 
ATOM   443  O  O    . GLN   A 1 83  ? 10.69700 -0.26300  11.23900 1.000 28.81103  ?  235 GLN   A O    1 
ATOM   444  C  CB   . GLN   A 1 83  ? 7.91300  0.61000   12.74700 1.000 33.04382  ?  235 GLN   A CB   1 
ATOM   445  C  CG   . GLN   A 1 83  ? 6.59600  0.11400   13.31700 1.000 38.00718  ?  235 GLN   A CG   1 
ATOM   446  C  CD   . GLN   A 1 83  ? 5.40600  0.88400   12.77900 1.000 47.69779  ?  235 GLN   A CD   1 
ATOM   447  O  OE1  . GLN   A 1 83  ? 5.19500  0.95700   11.56800 1.000 43.42789  ?  235 GLN   A OE1  1 
ATOM   448  N  NE2  . GLN   A 1 83  ? 4.62300  1.46700   13.67900 1.000 57.78223  ?  235 GLN   A NE2  1 
ATOM   449  N  N    . LYS   A 1 84  ? 11.02100 1.22600   12.89800 1.000 29.82774  ?  236 LYS   A N    1 
ATOM   450  C  CA   . LYS   A 1 84  ? 12.21000 1.78800   12.26500 1.000 41.69074  ?  236 LYS   A CA   1 
ATOM   451  C  C    . LYS   A 1 84  ? 13.36600 0.79600   12.28000 1.000 35.58340  ?  236 LYS   A C    1 
ATOM   452  O  O    . LYS   A 1 84  ? 14.11600 0.69500   11.30100 1.000 32.85233  ?  236 LYS   A O    1 
ATOM   453  C  CB   . LYS   A 1 84  ? 12.61400 3.08900   12.96100 1.000 38.56368  ?  236 LYS   A CB   1 
ATOM   454  C  CG   . LYS   A 1 84  ? 11.46900 4.06600   13.19800 1.000 37.53673  ?  236 LYS   A CG   1 
ATOM   455  C  CD   . LYS   A 1 84  ? 10.62400 4.26400   11.94800 1.000 43.18088  ?  236 LYS   A CD   1 
ATOM   456  C  CE   . LYS   A 1 84  ? 11.18200 5.36500   11.06300 1.000 40.22519  ?  236 LYS   A CE   1 
ATOM   457  N  NZ   . LYS   A 1 84  ? 11.40600 6.63000   11.81800 1.000 38.92419  ?  236 LYS   A NZ   1 
ATOM   458  N  N    . VAL   A 1 85  ? 13.52500 0.05800   13.38200 1.000 31.82984  ?  237 VAL   A N    1 
ATOM   459  C  CA   . VAL   A 1 85  ? 14.58900 -0.93900  13.46600 1.000 35.73863  ?  237 VAL   A CA   1 
ATOM   460  C  C    . VAL   A 1 85  ? 14.39100 -2.02000  12.41100 1.000 32.95249  ?  237 VAL   A C    1 
ATOM   461  O  O    . VAL   A 1 85  ? 15.35600 -2.50100  11.80400 1.000 30.19492  ?  237 VAL   A O    1 
ATOM   462  C  CB   . VAL   A 1 85  ? 14.65100 -1.53300  14.88600 1.000 31.62665  ?  237 VAL   A CB   1 
ATOM   463  C  CG1  . VAL   A 1 85  ? 15.60700 -2.71700  14.93400 1.000 31.03228  ?  237 VAL   A CG1  1 
ATOM   464  C  CG2  . VAL   A 1 85  ? 15.06200 -0.46600  15.89100 1.000 28.03404  ?  237 VAL   A CG2  1 
ATOM   465  N  N    . ILE   A 1 86  ? 13.13800 -2.41000  12.16600 1.000 29.22580  ?  238 ILE   A N    1 
ATOM   466  C  CA   . ILE   A 1 86  ? 12.86000 -3.41000  11.13600 1.000 25.54766  ?  238 ILE   A CA   1 
ATOM   467  C  C    . ILE   A 1 86  ? 13.25400 -2.87800  9.76400  1.000 23.74636  ?  238 ILE   A C    1 
ATOM   468  O  O    . ILE   A 1 86  ? 13.89800 -3.57400  8.97000  1.000 34.04554  ?  238 ILE   A O    1 
ATOM   469  C  CB   . ILE   A 1 86  ? 11.37900 -3.82800  11.17200 1.000 31.72247  ?  238 ILE   A CB   1 
ATOM   470  C  CG1  . ILE   A 1 86  ? 11.04400 -4.51500  12.49600 1.000 31.08714  ?  238 ILE   A CG1  1 
ATOM   471  C  CG2  . ILE   A 1 86  ? 11.06200 -4.75100  10.00500 1.000 30.99648  ?  238 ILE   A CG2  1 
ATOM   472  C  CD1  . ILE   A 1 86  ? 9.58800  -4.37600  12.89500 1.000 34.86868  ?  238 ILE   A CD1  1 
ATOM   473  N  N    . GLY   A 1 87  ? 12.87200 -1.63300  9.46700  1.000 31.75000  ?  239 GLY   A N    1 
ATOM   474  C  CA   . GLY   A 1 87  ? 13.23400 -1.04500  8.18600  1.000 28.64070  ?  239 GLY   A CA   1 
ATOM   475  C  C    . GLY   A 1 87  ? 14.73600 -0.96000  7.98900  1.000 32.12521  ?  239 GLY   A C    1 
ATOM   476  O  O    . GLY   A 1 87  ? 15.24300 -1.21000  6.89200  1.000 31.54695  ?  239 GLY   A O    1 
ATOM   477  N  N    . PHE   A 1 88  ? 15.46700 -0.61200  9.04900  1.000 28.95242  ?  240 PHE   A N    1 
ATOM   478  C  CA   . PHE   A 1 88  ? 16.92600 -0.60200  8.97500  1.000 25.78725  ?  240 PHE   A CA   1 
ATOM   479  C  C    . PHE   A 1 88  ? 17.46800 -2.00800  8.75900  1.000 23.76395  ?  240 PHE   A C    1 
ATOM   480  O  O    . PHE   A 1 88  ? 18.30500 -2.23500  7.87900  1.000 34.41372  ?  240 PHE   A O    1 
ATOM   481  C  CB   . PHE   A 1 88  ? 17.50600 0.01400   10.25100 1.000 23.86676  ?  240 PHE   A CB   1 
ATOM   482  C  CG   . PHE   A 1 88  ? 19.01300 -0.05600  10.34200 1.000 33.35689  ?  240 PHE   A CG   1 
ATOM   483  C  CD1  . PHE   A 1 88  ? 19.80500 0.87900   9.69300  1.000 26.44361  ?  240 PHE   A CD1  1 
ATOM   484  C  CD2  . PHE   A 1 88  ? 19.63300 -1.04300  11.09700 1.000 31.41028  ?  240 PHE   A CD2  1 
ATOM   485  C  CE1  . PHE   A 1 88  ? 21.18800 0.82200   9.78200  1.000 25.13701  ?  240 PHE   A CE1  1 
ATOM   486  C  CE2  . PHE   A 1 88  ? 21.01400 -1.10600  11.18900 1.000 30.44758  ?  240 PHE   A CE2  1 
ATOM   487  C  CZ   . PHE   A 1 88  ? 21.79200 -0.17100  10.53300 1.000 32.70524  ?  240 PHE   A CZ   1 
ATOM   488  N  N    . ALA   A 1 89  ? 16.98700 -2.97000  9.55300  1.000 28.67510  ?  241 ALA   A N    1 
ATOM   489  C  CA   . ALA   A 1 89  ? 17.51200 -4.33100  9.48900  1.000 28.13484  ?  241 ALA   A CA   1 
ATOM   490  C  C    . ALA   A 1 89  ? 17.33100 -4.94000  8.10500  1.000 36.31272  ?  241 ALA   A C    1 
ATOM   491  O  O    . ALA   A 1 89  ? 18.20000 -5.68300  7.63100  1.000 36.07956  ?  241 ALA   A O    1 
ATOM   492  C  CB   . ALA   A 1 89  ? 16.83500 -5.20100  10.54800 1.000 28.43474  ?  241 ALA   A CB   1 
ATOM   493  N  N    . LYS   A 1 90  ? 16.21000 -4.63500  7.44100  1.000 31.28687  ?  242 LYS   A N    1 
ATOM   494  C  CA   . LYS   A 1 90  ? 15.94500 -5.19300  6.11800  1.000 26.41014  ?  242 LYS   A CA   1 
ATOM   495  C  C    . LYS   A 1 90  ? 17.01500 -4.79500  5.11200  1.000 27.48012  ?  242 LYS   A C    1 
ATOM   496  O  O    . LYS   A 1 90  ? 17.24800 -5.51700  4.13600  1.000 33.56188  ?  242 LYS   A O    1 
ATOM   497  C  CB   . LYS   A 1 90  ? 14.57200 -4.73500  5.61600  1.000 29.37916  ?  242 LYS   A CB   1 
ATOM   498  C  CG   . LYS   A 1 90  ? 13.38500 -5.42200  6.27000  1.000 34.97437  ?  242 LYS   A CG   1 
ATOM   499  C  CD   . LYS   A 1 90  ? 12.15700 -5.36000  5.36500  1.000 52.12683  ?  242 LYS   A CD   1 
ATOM   500  C  CE   . LYS   A 1 90  ? 11.68300 -3.92700  5.17100  1.000 54.58576  ?  242 LYS   A CE   1 
ATOM   501  N  NZ   . LYS   A 1 90  ? 10.27300 -3.86100  4.69200  1.000 55.15054  ?  242 LYS   A NZ   1 
ATOM   502  N  N    . MET   A 1 91  ? 17.66800 -3.65800  5.32700  1.000 32.25937  ?  243 MET   A N    1 
ATOM   503  C  CA   . MET   A 1 91  ? 18.67400 -3.15400  4.40400  1.000 37.62306  ?  243 MET   A CA   1 
ATOM   504  C  C    . MET   A 1 91  ? 20.09200 -3.57000  4.77700  1.000 41.15947  ?  243 MET   A C    1 
ATOM   505  O  O    . MET   A 1 91  ? 21.03100 -3.21600  4.05700  1.000 35.10378  ?  243 MET   A O    1 
ATOM   506  C  CB   . MET   A 1 91  ? 18.58200 -1.62900  4.32000  1.000 45.74130  ?  243 MET   A CB   1 
ATOM   507  C  CG   . MET   A 1 91  ? 17.18000 -1.12700  4.00500  1.000 56.61397  ?  243 MET   A CG   1 
ATOM   508  S  SD   . MET   A 1 91  ? 17.12700 0.61200   3.53900  1.000 58.81901  ?  243 MET   A SD   1 
ATOM   509  C  CE   . MET   A 1 91  ? 16.10000 1.27700   4.84800  1.000 48.07378  ?  243 MET   A CE   1 
ATOM   510  N  N    . ILE   A 1 92  ? 20.27200 -4.30400  5.87200  1.000 42.78807  ?  244 ILE   A N    1 
ATOM   511  C  CA   . ILE   A 1 92  ? 21.60600 -4.83100  6.18700  1.000 39.04669  ?  244 ILE   A CA   1 
ATOM   512  C  C    . ILE   A 1 92  ? 22.02000 -5.81500  5.10100  1.000 37.45775  ?  244 ILE   A C    1 
ATOM   513  O  O    . ILE   A 1 92  ? 21.24700 -6.73800  4.77700  1.000 37.41493  ?  244 ILE   A O    1 
ATOM   514  C  CB   . ILE   A 1 92  ? 21.61400 -5.51400  7.56500  1.000 37.77231  ?  244 ILE   A CB   1 
ATOM   515  C  CG1  . ILE   A 1 92  ? 21.17100 -4.54200  8.66000  1.000 32.72084  ?  244 ILE   A CG1  1 
ATOM   516  C  CG2  . ILE   A 1 92  ? 23.00100 -6.08300  7.86400  1.000 31.97387  ?  244 ILE   A CG2  1 
ATOM   517  C  CD1  . ILE   A 1 92  ? 21.09700 -5.17300  10.03500 1.000 29.38286  ?  244 ILE   A CD1  1 
ATOM   518  N  N    . PRO   A 1 93  ? 23.20300 -5.67100  4.50300  1.000 36.75408  ?  245 PRO   A N    1 
ATOM   519  C  CA   . PRO   A 1 93  ? 23.63300 -6.62700  3.47000  1.000 44.07122  ?  245 PRO   A CA   1 
ATOM   520  C  C    . PRO   A 1 93  ? 23.66900 -8.04600  4.01700  1.000 50.88207  ?  245 PRO   A C    1 
ATOM   521  O  O    . PRO   A 1 93  ? 24.33100 -8.33100  5.01900  1.000 48.33533  ?  245 PRO   A O    1 
ATOM   522  C  CB   . PRO   A 1 93  ? 25.03000 -6.12700  3.08700  1.000 47.68373  ?  245 PRO   A CB   1 
ATOM   523  C  CG   . PRO   A 1 93  ? 25.02500 -4.67600  3.44800  1.000 49.06164  ?  245 PRO   A CG   1 
ATOM   524  C  CD   . PRO   A 1 93  ? 24.15600 -4.56100  4.66800  1.000 38.90170  ?  245 PRO   A CD   1 
ATOM   525  N  N    . GLY   A 1 94  ? 22.93000 -8.93800  3.35700  1.000 49.93712  ?  246 GLY   A N    1 
ATOM   526  C  CA   . GLY   A 1 94  ? 22.85400 -10.32500 3.75200  1.000 43.46658  ?  246 GLY   A CA   1 
ATOM   527  C  C    . GLY   A 1 94  ? 21.69100 -10.67800 4.65800  1.000 44.55495  ?  246 GLY   A C    1 
ATOM   528  O  O    . GLY   A 1 94  ? 21.37200 -11.86400 4.79200  1.000 49.99672  ?  246 GLY   A O    1 
ATOM   529  N  N    . PHE   A 1 95  ? 21.04000 -9.68600  5.27500  1.000 45.98906  ?  247 PHE   A N    1 
ATOM   530  C  CA   . PHE   A 1 95  ? 19.95700 -9.98100  6.21200  1.000 47.28597  ?  247 PHE   A CA   1 
ATOM   531  C  C    . PHE   A 1 95  ? 18.81100 -10.72100 5.53200  1.000 53.12017  ?  247 PHE   A C    1 
ATOM   532  O  O    . PHE   A 1 95  ? 18.19300 -11.60800 6.13400  1.000 53.73273  ?  247 PHE   A O    1 
ATOM   533  C  CB   . PHE   A 1 95  ? 19.44900 -8.68700  6.85500  1.000 39.78866  ?  247 PHE   A CB   1 
ATOM   534  C  CG   . PHE   A 1 95  ? 18.43000 -8.90800  7.94200  1.000 39.59872  ?  247 PHE   A CG   1 
ATOM   535  C  CD1  . PHE   A 1 95  ? 18.82500 -9.27400  9.22000  1.000 37.10538  ?  247 PHE   A CD1  1 
ATOM   536  C  CD2  . PHE   A 1 95  ? 17.07600 -8.75400  7.68400  1.000 35.67636  ?  247 PHE   A CD2  1 
ATOM   537  C  CE1  . PHE   A 1 95  ? 17.88900 -9.48000  10.22000 1.000 43.53061  ?  247 PHE   A CE1  1 
ATOM   538  C  CE2  . PHE   A 1 95  ? 16.13600 -8.95800  8.68000  1.000 40.42617  ?  247 PHE   A CE2  1 
ATOM   539  C  CZ   . PHE   A 1 95  ? 16.54200 -9.32300  9.95000  1.000 35.21577  ?  247 PHE   A CZ   1 
ATOM   540  N  N    A ARG   A 1 96  ? 18.51500 -10.37300 4.27700  0.520 60.98891  ?  248 ARG   A N    1 
ATOM   541  N  N    B ARG   A 1 96  ? 18.51300 -10.37500 4.27700  0.480 60.91842  ?  248 ARG   A N    1 
ATOM   542  C  CA   A ARG   A 1 96  ? 17.40300 -10.99500 3.56500  0.520 62.39102  ?  248 ARG   A CA   1 
ATOM   543  C  CA   B ARG   A 1 96  ? 17.39500 -11.01000 3.58400  0.480 62.39470  ?  248 ARG   A CA   1 
ATOM   544  C  C    A ARG   A 1 96  ? 17.68900 -12.44400 3.19000  0.520 66.18932  ?  248 ARG   A C    1 
ATOM   545  C  C    B ARG   A 1 96  ? 17.68800 -12.47200 3.26500  0.480 66.23233  ?  248 ARG   A C    1 
ATOM   546  O  O    A ARG   A 1 96  ? 16.74600 -13.21500 2.98900  0.520 71.03826  ?  248 ARG   A O    1 
ATOM   547  O  O    B ARG   A 1 96  ? 16.76200 -13.28900 3.19800  0.480 70.77342  ?  248 ARG   A O    1 
ATOM   548  C  CB   A ARG   A 1 96  ? 17.06700 -10.19200 2.30600  0.520 61.77890  ?  248 ARG   A CB   1 
ATOM   549  C  CB   B ARG   A 1 96  ? 17.06000 -10.22900 2.30900  0.480 61.89216  ?  248 ARG   A CB   1 
ATOM   550  C  CG   A ARG   A 1 96  ? 16.57400 -8.78000  2.58300  0.520 56.03825  ?  248 ARG   A CG   1 
ATOM   551  C  CG   B ARG   A 1 96  ? 16.08700 -10.92500 1.36000  0.480 69.17385  ?  248 ARG   A CG   1 
ATOM   552  C  CD   A ARG   A 1 96  ? 15.47100 -8.78400  3.62400  0.520 56.41641  ?  248 ARG   A CD   1 
ATOM   553  C  CD   B ARG   A 1 96  ? 14.73300 -11.18000 2.01500  0.480 68.03069  ?  248 ARG   A CD   1 
ATOM   554  N  NE   A ARG   A 1 96  ? 14.18100 -8.39800  3.06000  0.520 53.96990  ?  248 ARG   A NE   1 
ATOM   555  N  NE   B ARG   A 1 96  ? 14.46900 -12.60900 2.17900  0.480 69.17984  ?  248 ARG   A NE   1 
ATOM   556  C  CZ   A ARG   A 1 96  ? 13.01000 -8.85700  3.48800  0.520 53.07557  ?  248 ARG   A CZ   1 
ATOM   557  C  CZ   B ARG   A 1 96  ? 13.43300 -13.10900 2.84700  0.480 73.63710  ?  248 ARG   A CZ   1 
ATOM   558  N  NH1  A ARG   A 1 96  ? 11.88700 -8.44900  2.91600  0.520 59.55782  ?  248 ARG   A NH1  1 
ATOM   559  N  NH1  B ARG   A 1 96  ? 12.55400 -12.29800 3.41800  0.480 74.01864  ?  248 ARG   A NH1  1 
ATOM   560  N  NH2  A ARG   A 1 96  ? 12.96000 -9.72400  4.49200  0.520 46.29651  ?  248 ARG   A NH2  1 
ATOM   561  N  NH2  B ARG   A 1 96  ? 13.27600 -14.42300 2.94400  0.480 77.87980  ?  248 ARG   A NH2  1 
ATOM   562  N  N    . ASP   A 1 97  ? 18.96500 -12.82500 3.09000  1.000 69.80924  ?  249 ASP   A N    1 
ATOM   563  C  CA   . ASP   A 1 97  ? 19.32600 -14.20100 2.76200  1.000 73.97843  ?  249 ASP   A CA   1 
ATOM   564  C  C    . ASP   A 1 97  ? 18.99900 -15.17300 3.88500  1.000 65.60406  ?  249 ASP   A C    1 
ATOM   565  O  O    . ASP   A 1 97  ? 18.97000 -16.38600 3.65000  1.000 66.13486  ?  249 ASP   A O    1 
ATOM   566  C  CB   . ASP   A 1 97  ? 20.81200 -14.29100 2.41600  1.000 83.78959  ?  249 ASP   A CB   1 
ATOM   567  C  CG   . ASP   A 1 97  ? 21.19500 -13.40700 1.24800  1.000 91.57947  ?  249 ASP   A CG   1 
ATOM   568  O  OD1  . ASP   A 1 97  ? 20.29100 -13.03500 0.47200  1.000 93.30356  ?  249 ASP   A OD1  1 
ATOM   569  O  OD2  . ASP   A 1 97  ? 22.39900 -13.09100 1.09500  1.000 95.41191  ?  249 ASP   A OD2  1 
ATOM   570  N  N    . LEU   A 1 98  ? 18.76500 -14.67000 5.09400  1.000 47.59166  ?  250 LEU   A N    1 
ATOM   571  C  CA   . LEU   A 1 98  ? 18.26300 -15.50100 6.17400  1.000 49.42037  ?  250 LEU   A CA   1 
ATOM   572  C  C    . LEU   A 1 98  ? 16.80600 -15.88100 5.91800  1.000 50.04047  ?  250 LEU   A C    1 
ATOM   573  O  O    . LEU   A 1 98  ? 16.06800 -15.18900 5.21200  1.000 52.85901  ?  250 LEU   A O    1 
ATOM   574  C  CB   . LEU   A 1 98  ? 18.37100 -14.77100 7.51500  1.000 54.66403  ?  250 LEU   A CB   1 
ATOM   575  C  CG   . LEU   A 1 98  ? 19.76100 -14.28500 7.93200  1.000 48.43261  ?  250 LEU   A CG   1 
ATOM   576  C  CD1  . LEU   A 1 98  ? 19.65100 -13.27000 9.05700  1.000 48.85927  ?  250 LEU   A CD1  1 
ATOM   577  C  CD2  . LEU   A 1 98  ? 20.60500 -15.46500 8.34700  1.000 46.19842  ?  250 LEU   A CD2  1 
ATOM   578  N  N    . THR   A 1 99  ? 16.39300 -16.99900 6.51100  1.000 52.43641  ?  251 THR   A N    1 
ATOM   579  C  CA   . THR   A 1 99  ? 14.98400 -17.35800 6.49300  1.000 51.97201  ?  251 THR   A CA   1 
ATOM   580  C  C    . THR   A 1 99  ? 14.17200 -16.33200 7.27900  1.000 52.25701  ?  251 THR   A C    1 
ATOM   581  O  O    . THR   A 1 99  ? 14.69500 -15.60400 8.12800  1.000 44.98646  ?  251 THR   A O    1 
ATOM   582  C  CB   . THR   A 1 99  ? 14.76800 -18.74800 7.09000  1.000 59.58638  ?  251 THR   A CB   1 
ATOM   583  O  OG1  . THR   A 1 99  ? 15.10700 -18.72400 8.48300  1.000 58.68318  ?  251 THR   A OG1  1 
ATOM   584  C  CG2  . THR   A 1 99  ? 15.63200 -19.77600 6.37800  1.000 62.42341  ?  251 THR   A CG2  1 
ATOM   585  N  N    . SER   A 1 100 ? 12.87200 -16.27300 6.97400  1.000 50.55697  ?  252 SER   A N    1 
ATOM   586  C  CA   . SER   A 1 100 ? 11.98100 -15.39200 7.72100  1.000 45.15538  ?  252 SER   A CA   1 
ATOM   587  C  C    . SER   A 1 100 ? 12.00700 -15.71100 9.21000  1.000 42.20058  ?  252 SER   A C    1 
ATOM   588  O  O    . SER   A 1 100 ? 11.90700 -14.80200 10.04300 1.000 46.77424  ?  252 SER   A O    1 
ATOM   589  C  CB   . SER   A 1 100 ? 10.55400 -15.49900 7.17800  1.000 51.31240  ?  252 SER   A CB   1 
ATOM   590  O  OG   . SER   A 1 100 ? 10.47400 -14.99600 5.85700  1.000 62.12362  ?  252 SER   A OG   1 
ATOM   591  N  N    . ASP   A 1 101 ? 12.15200 -16.99000 9.56000  1.000 43.50699  ?  253 ASP   A N    1 
ATOM   592  C  CA   . ASP   A 1 101 ? 12.23300 -17.37500 10.96500 1.000 45.61726  ?  253 ASP   A CA   1 
ATOM   593  C  C    . ASP   A 1 101 ? 13.45700 -16.76000 11.63300 1.000 44.12999  ?  253 ASP   A C    1 
ATOM   594  O  O    . ASP   A 1 101 ? 13.35500 -16.15000 12.70400 1.000 42.47447  ?  253 ASP   A O    1 
ATOM   595  C  CB   . ASP   A 1 101 ? 12.26300 -18.89900 11.08700 1.000 50.64237  ?  253 ASP   A CB   1 
ATOM   596  C  CG   . ASP   A 1 101 ? 11.08300 -19.55900 10.40600 1.000 72.97485  ?  253 ASP   A CG   1 
ATOM   597  O  OD1  . ASP   A 1 101 ? 11.16300 -19.81000 9.18400  1.000 78.67530  ?  253 ASP   A OD1  1 
ATOM   598  O  OD2  . ASP   A 1 101 ? 10.07200 -19.82100 11.09200 1.000 73.64854  ?  253 ASP   A OD2  1 
ATOM   599  N  N    . ASP   A 1 102 ? 14.62900 -16.90700 11.00900 1.000 45.80977  ?  254 ASP   A N    1 
ATOM   600  C  CA   . ASP   A 1 102 ? 15.84400 -16.34400 11.59000 1.000 43.22472  ?  254 ASP   A CA   1 
ATOM   601  C  C    . ASP   A 1 102 ? 15.78400 -14.82200 11.62700 1.000 44.91462  ?  254 ASP   A C    1 
ATOM   602  O  O    . ASP   A 1 102 ? 16.28400 -14.20000 12.57100 1.000 43.98362  ?  254 ASP   A O    1 
ATOM   603  C  CB   . ASP   A 1 102 ? 17.07200 -16.82400 10.81700 1.000 47.34093  ?  254 ASP   A CB   1 
ATOM   604  C  CG   . ASP   A 1 102 ? 17.57400 -18.17200 11.30200 1.000 59.33787  ?  254 ASP   A CG   1 
ATOM   605  O  OD1  . ASP   A 1 102 ? 18.37200 -18.81000 10.58300 1.000 57.47106  ?  254 ASP   A OD1  1 
ATOM   606  O  OD2  . ASP   A 1 102 ? 17.16500 -18.59400 12.40500 1.000 59.48672  ?  254 ASP   A OD2  1 
ATOM   607  N  N    . GLN   A 1 103 ? 15.17100 -14.20400 10.61200 1.000 42.84014  ?  255 GLN   A N    1 
ATOM   608  C  CA   . GLN   A 1 103 ? 14.98400 -12.75600 10.63600 1.000 43.05834  ?  255 GLN   A CA   1 
ATOM   609  C  C    . GLN   A 1 103 ? 14.11700 -12.33300 11.81500 1.000 44.98777  ?  255 GLN   A C    1 
ATOM   610  O  O    . GLN   A 1 103 ? 14.34800 -11.28000 12.42100 1.000 31.14576  ?  255 GLN   A O    1 
ATOM   611  C  CB   . GLN   A 1 103 ? 14.35800 -12.28100 9.32500  1.000 42.89842  ?  255 GLN   A CB   1 
ATOM   612  C  CG   . GLN   A 1 103 ? 15.23300 -12.45800 8.09500  1.000 54.28018  ?  255 GLN   A CG   1 
ATOM   613  C  CD   . GLN   A 1 103 ? 14.52400 -12.04700 6.81600  1.000 53.08297  ?  255 GLN   A CD   1 
ATOM   614  O  OE1  . GLN   A 1 103 ? 13.82200 -11.03700 6.77800  1.000 47.12039  ?  255 GLN   A OE1  1 
ATOM   615  N  NE2  . GLN   A 1 103 ? 14.70100 -12.83500 5.76200  1.000 56.54024  ?  255 GLN   A NE2  1 
ATOM   616  N  N    . ILE   A 1 104 ? 13.11900 -13.14900 12.16100 1.000 35.75449  ?  256 ILE   A N    1 
ATOM   617  C  CA   . ILE   A 1 104 ? 12.19200 -12.78700 13.22800 1.000 41.69541  ?  256 ILE   A CA   1 
ATOM   618  C  C    . ILE   A 1 104 ? 12.86200 -12.91600 14.59200 1.000 31.77148  ?  256 ILE   A C    1 
ATOM   619  O  O    . ILE   A 1 104 ? 12.74600 -12.02500 15.44200 1.000 36.98844  ?  256 ILE   A O    1 
ATOM   620  C  CB   . ILE   A 1 104 ? 10.91500 -13.64200 13.14100 1.000 39.67268  ?  256 ILE   A CB   1 
ATOM   621  C  CG1  . ILE   A 1 104 ? 10.02700 -13.15900 11.99500 1.000 41.43525  ?  256 ILE   A CG1  1 
ATOM   622  C  CG2  . ILE   A 1 104 ? 10.14700 -13.59500 14.45600 1.000 38.26161  ?  256 ILE   A CG2  1 
ATOM   623  C  CD1  . ILE   A 1 104 ? 8.74200  -13.94000 11.85000 1.000 40.04146  ?  256 ILE   A CD1  1 
ATOM   624  N  N    . VAL   A 1 105 ? 13.56400 -14.02700 14.82800 1.000 31.80545  ?  257 VAL   A N    1 
ATOM   625  C  CA   . VAL   A 1 105 ? 14.19100 -14.21200 16.13400 1.000 43.04494  ?  257 VAL   A CA   1 
ATOM   626  C  C    . VAL   A 1 105 ? 15.28200 -13.17200 16.36400 1.000 36.60376  ?  257 VAL   A C    1 
ATOM   627  O  O    . VAL   A 1 105 ? 15.47800 -12.71200 17.49500 1.000 34.08348  ?  257 VAL   A O    1 
ATOM   628  C  CB   . VAL   A 1 105 ? 14.72200 -15.65200 16.28900 1.000 49.66740  ?  257 VAL   A CB   1 
ATOM   629  C  CG1  . VAL   A 1 105 ? 13.63300 -16.65600 15.94600 1.000 50.94878  ?  257 VAL   A CG1  1 
ATOM   630  C  CG2  . VAL   A 1 105 ? 15.95200 -15.88800 15.42500 1.000 55.54708  ?  257 VAL   A CG2  1 
ATOM   631  N  N    . LEU   A 1 106 ? 15.98600 -12.76000 15.30500 1.000 34.63989  ?  258 LEU   A N    1 
ATOM   632  C  CA   . LEU   A 1 106 ? 17.03100 -11.75300 15.46700 1.000 43.07344  ?  258 LEU   A CA   1 
ATOM   633  C  C    . LEU   A 1 106 ? 16.43700 -10.39600 15.82000 1.000 36.06698  ?  258 LEU   A C    1 
ATOM   634  O  O    . LEU   A 1 106 ? 16.94900 -9.69900  16.70300 1.000 29.24364  ?  258 LEU   A O    1 
ATOM   635  C  CB   . LEU   A 1 106 ? 17.87200 -11.65500 14.19300 1.000 35.76647  ?  258 LEU   A CB   1 
ATOM   636  C  CG   . LEU   A 1 106 ? 18.84800 -12.80100 13.91700 1.000 32.83835  ?  258 LEU   A CG   1 
ATOM   637  C  CD1  . LEU   A 1 106 ? 19.58100 -12.56800 12.60800 1.000 32.96861  ?  258 LEU   A CD1  1 
ATOM   638  C  CD2  . LEU   A 1 106 ? 19.83500 -12.96500 15.06100 1.000 35.15382  ?  258 LEU   A CD2  1 
ATOM   639  N  N    . LEU   A 1 107 ? 15.35000 -10.01100 15.14800 1.000 37.44656  ?  259 LEU   A N    1 
ATOM   640  C  CA   . LEU   A 1 107 ? 14.71900 -8.72900  15.44200 1.000 37.11173  ?  259 LEU   A CA   1 
ATOM   641  C  C    . LEU   A 1 107 ? 14.02000 -8.75300  16.79400 1.000 35.02571  ?  259 LEU   A C    1 
ATOM   642  O  O    . LEU   A 1 107 ? 14.06200 -7.76400  17.53400 1.000 28.57732  ?  259 LEU   A O    1 
ATOM   643  C  CB   . LEU   A 1 107 ? 13.73500 -8.36000  14.33200 1.000 35.23647  ?  259 LEU   A CB   1 
ATOM   644  C  CG   . LEU   A 1 107 ? 14.40900 -7.75300  13.10200 1.000 43.83296  ?  259 LEU   A CG   1 
ATOM   645  C  CD1  . LEU   A 1 107 ? 13.50400 -7.83000  11.88300 1.000 47.91241  ?  259 LEU   A CD1  1 
ATOM   646  C  CD2  . LEU   A 1 107 ? 14.81700 -6.31700  13.38500 1.000 43.46870  ?  259 LEU   A CD2  1 
ATOM   647  N  N    . LYS   A 1 108 ? 13.36400 -9.86700  17.13100 1.000 35.78349  ?  260 LYS   A N    1 
ATOM   648  C  CA   . LYS   A 1 108 ? 12.74900 -9.98900  18.44900 1.000 38.43106  ?  260 LYS   A CA   1 
ATOM   649  C  C    . LYS   A 1 108 ? 13.77900 -9.82400  19.55600 1.000 39.73862  ?  260 LYS   A C    1 
ATOM   650  O  O    . LYS   A 1 108 ? 13.51900 -9.15700  20.56400 1.000 39.53440  ?  260 LYS   A O    1 
ATOM   651  C  CB   . LYS   A 1 108 ? 12.05000 -11.34000 18.59000 1.000 32.76841  ?  260 LYS   A CB   1 
ATOM   652  C  CG   . LYS   A 1 108 ? 10.56800 -11.32900 18.28100 1.000 43.33047  ?  260 LYS   A CG   1 
ATOM   653  C  CD   . LYS   A 1 108 ? 9.96300  -12.69900 18.53200 1.000 44.72539  ?  260 LYS   A CD   1 
ATOM   654  C  CE   . LYS   A 1 108 ? 9.81600  -12.97200 20.02100 1.000 61.39438  ?  260 LYS   A CE   1 
ATOM   655  N  NZ   . LYS   A 1 108 ? 8.78300  -14.00500 20.31300 1.000 69.55993  ?  260 LYS   A NZ   1 
ATOM   656  N  N    . SER   A 1 109 ? 14.95800 -10.42100 19.38700 1.000 28.92393  ?  261 SER   A N    1 
ATOM   657  C  CA   . SER   A 1 109 ? 15.94300 -10.39600 20.46100 1.000 37.32403  ?  261 SER   A CA   1 
ATOM   658  C  C    . SER   A 1 109 ? 16.70200 -9.07500  20.49400 1.000 30.08361  ?  261 SER   A C    1 
ATOM   659  O  O    . SER   A 1 109 ? 17.02200 -8.57100  21.57700 1.000 31.60943  ?  261 SER   A O    1 
ATOM   660  C  CB   . SER   A 1 109 ? 16.90800 -11.57500 20.31100 1.000 44.13921  ?  261 SER   A CB   1 
ATOM   661  O  OG   . SER   A 1 109 ? 17.89700 -11.55200 21.32400 1.000 52.42218  ?  261 SER   A OG   1 
ATOM   662  N  N    . SER   A 1 110 ? 16.97100 -8.48600  19.32800 1.000 33.59004  ?  262 SER   A N    1 
ATOM   663  C  CA   . SER   A 1 110 ? 17.82200 -7.30800  19.23400 1.000 30.19098  ?  262 SER   A CA   1 
ATOM   664  C  C    . SER   A 1 110 ? 17.07500 -5.98100  19.29400 1.000 28.55107  ?  262 SER   A C    1 
ATOM   665  O  O    . SER   A 1 110 ? 17.71900 -4.95500  19.52600 1.000 27.43614  ?  262 SER   A O    1 
ATOM   666  C  CB   . SER   A 1 110 ? 18.65100 -7.36400  17.94300 1.000 39.24842  ?  262 SER   A CB   1 
ATOM   667  O  OG   . SER   A 1 110 ? 17.98100 -6.71800  16.88000 1.000 37.94138  ?  262 SER   A OG   1 
ATOM   668  N  N    . ALA   A 1 111 ? 15.74900 -5.97100  19.11300 1.000 33.02486  ?  263 ALA   A N    1 
ATOM   669  C  CA   . ALA   A 1 111 ? 15.02700 -4.71200  18.92900 1.000 30.42615  ?  263 ALA   A CA   1 
ATOM   670  C  C    . ALA   A 1 111 ? 15.30200 -3.72200  20.05500 1.000 27.03881  ?  263 ALA   A C    1 
ATOM   671  O  O    . ALA   A 1 111 ? 15.65100 -2.56300  19.80400 1.000 26.27696  ?  263 ALA   A O    1 
ATOM   672  C  CB   . ALA   A 1 111 ? 13.52300 -4.97400  18.81200 1.000 32.40923  ?  263 ALA   A CB   1 
ATOM   673  N  N    . ILE   A 1 112 ? 15.15200 -4.15900  21.30800 1.000 26.59913  ?  264 ILE   A N    1 
ATOM   674  C  CA   . ILE   A 1 112 ? 15.33600 -3.23300  22.42200 1.000 26.75604  ?  264 ILE   A CA   1 
ATOM   675  C  C    . ILE   A 1 112 ? 16.78000 -2.74900  22.49900 1.000 29.87278  ?  264 ILE   A C    1 
ATOM   676  O  O    . ILE   A 1 112 ? 17.04100 -1.61700  22.92800 1.000 27.57965  ?  264 ILE   A O    1 
ATOM   677  C  CB   . ILE   A 1 112 ? 14.87400 -3.88000  23.74400 1.000 31.73828  ?  264 ILE   A CB   1 
ATOM   678  C  CG1  . ILE   A 1 112 ? 14.72700 -2.81500  24.83500 1.000 33.20681  ?  264 ILE   A CG1  1 
ATOM   679  C  CG2  . ILE   A 1 112 ? 15.80800 -5.00800  24.17100 1.000 31.55612  ?  264 ILE   A CG2  1 
ATOM   680  C  CD1  . ILE   A 1 112 ? 13.70600 -1.74500  24.48900 1.000 39.98817  ?  264 ILE   A CD1  1 
ATOM   681  N  N    . GLU   A 1 113 ? 17.73900 -3.57400  22.07100 1.000 26.54703  ?  265 GLU   A N    1 
ATOM   682  C  CA   . GLU   A 1 113 ? 19.13500 -3.14200  22.08600 1.000 26.83769  ?  265 GLU   A CA   1 
ATOM   683  C  C    . GLU   A 1 113 ? 19.40200 -2.10600  21.00100 1.000 27.42812  ?  265 GLU   A C    1 
ATOM   684  O  O    . GLU   A 1 113 ? 20.08500 -1.10500  21.24500 1.000 29.76972  ?  265 GLU   A O    1 
ATOM   685  C  CB   . GLU   A 1 113 ? 20.05800 -4.34600  21.91700 1.000 26.55291  ?  265 GLU   A CB   1 
ATOM   686  C  CG   . GLU   A 1 113 ? 19.89100 -5.41100  22.98600 1.000 26.17738  ?  265 GLU   A CG   1 
ATOM   687  C  CD   . GLU   A 1 113 ? 20.78000 -6.61400  22.74400 1.000 36.71597  ?  265 GLU   A CD   1 
ATOM   688  O  OE1  . GLU   A 1 113 ? 21.82400 -6.46000  22.06900 1.000 33.46005  ?  265 GLU   A OE1  1 
ATOM   689  O  OE2  . GLU   A 1 113 ? 20.43300 -7.71400  23.22400 1.000 33.39240  ?  265 GLU   A OE2  1 
ATOM   690  N  N    . VAL   A 1 114 ? 18.87000 -2.32400  19.79700 1.000 32.46111  ?  266 VAL   A N    1 
ATOM   691  C  CA   . VAL   A 1 114 ? 19.03600 -1.34100  18.73100 1.000 30.09839  ?  266 VAL   A CA   1 
ATOM   692  C  C    . VAL   A 1 114 ? 18.34100 -0.03700  19.09600 1.000 22.39030  ?  266 VAL   A C    1 
ATOM   693  O  O    . VAL   A 1 114 ? 18.82700 1.05400   18.77400 1.000 31.86070  ?  266 VAL   A O    1 
ATOM   694  C  CB   . VAL   A 1 114 ? 18.51900 -1.90500  17.39600 1.000 33.06335  ?  266 VAL   A CB   1 
ATOM   695  C  CG1  . VAL   A 1 114 ? 18.83700 -0.94600  16.25800 1.000 23.45975  ?  266 VAL   A CG1  1 
ATOM   696  C  CG2  . VAL   A 1 114 ? 19.13400 -3.26700  17.13500 1.000 28.77060  ?  266 VAL   A CG2  1 
ATOM   697  N  N    . ILE   A 1 115 ? 17.19500 -0.12600  19.77500 1.000 30.14881  ?  267 ILE   A N    1 
ATOM   698  C  CA   . ILE   A 1 115 ? 16.52200 1.08100   20.24600 1.000 25.89263  ?  267 ILE   A CA   1 
ATOM   699  C  C    . ILE   A 1 115 ? 17.40600 1.82400   21.23900 1.000 29.28426  ?  267 ILE   A C    1 
ATOM   700  O  O    . ILE   A 1 115 ? 17.52200 3.05500   21.18900 1.000 26.26621  ?  267 ILE   A O    1 
ATOM   701  C  CB   . ILE   A 1 115 ? 15.15100 0.72400   20.85000 1.000 30.70463  ?  267 ILE   A CB   1 
ATOM   702  C  CG1  . ILE   A 1 115 ? 14.16000 0.37200   19.73600 1.000 25.13133  ?  267 ILE   A CG1  1 
ATOM   703  C  CG2  . ILE   A 1 115 ? 14.62200 1.87100   21.69600 1.000 27.00377  ?  267 ILE   A CG2  1 
ATOM   704  C  CD1  . ILE   A 1 115 ? 13.02100 -0.51500  20.18400 1.000 30.07533  ?  267 ILE   A CD1  1 
ATOM   705  N  N    . MET   A 1 116 ? 18.05200 1.08900   22.14800 1.000 25.40566  ?  268 MET   A N    1 
ATOM   706  C  CA   . MET   A 1 116 ? 19.00600 1.71200   23.06200 1.000 32.24180  ?  268 MET   A CA   1 
ATOM   707  C  C    . MET   A 1 116 ? 20.12700 2.40800   22.29800 1.000 31.81541  ?  268 MET   A C    1 
ATOM   708  O  O    . MET   A 1 116 ? 20.52200 3.52700   22.64500 1.000 30.94249  ?  268 MET   A O    1 
ATOM   709  C  CB   . MET   A 1 116 ? 19.58300 0.66600   24.01600 1.000 28.15053  ?  268 MET   A CB   1 
ATOM   710  C  CG   . MET   A 1 116 ? 18.65800 0.28200   25.16000 1.000 37.95687  ?  268 MET   A CG   1 
ATOM   711  S  SD   . MET   A 1 116 ? 19.11200 -1.28100  25.93900 1.000 41.95618  ?  268 MET   A SD   1 
ATOM   712  C  CE   . MET   A 1 116 ? 17.85700 -1.41500  27.20900 1.000 42.34519  ?  268 MET   A CE   1 
ATOM   713  N  N    . LEU   A 1 117 ? 20.64200 1.76300   21.24800 1.000 25.97805  ?  269 LEU   A N    1 
ATOM   714  C  CA   . LEU   A 1 117 ? 21.72700 2.35300   20.46900 1.000 29.83967  ?  269 LEU   A CA   1 
ATOM   715  C  C    . LEU   A 1 117 ? 21.25600 3.58700   19.70900 1.000 34.50903  ?  269 LEU   A C    1 
ATOM   716  O  O    . LEU   A 1 117 ? 21.86600 4.65700   19.80600 1.000 27.03202  ?  269 LEU   A O    1 
ATOM   717  C  CB   . LEU   A 1 117 ? 22.30500 1.32100   19.50000 1.000 28.45810  ?  269 LEU   A CB   1 
ATOM   718  C  CG   . LEU   A 1 117 ? 23.15600 0.19800   20.09000 1.000 35.88627  ?  269 LEU   A CG   1 
ATOM   719  C  CD1  . LEU   A 1 117 ? 23.38500 -0.89300  19.05200 1.000 31.74428  ?  269 LEU   A CD1  1 
ATOM   720  C  CD2  . LEU   A 1 117 ? 24.48400 0.73700   20.60900 1.000 37.47728  ?  269 LEU   A CD2  1 
ATOM   721  N  N    . ARG   A 1 118 ? 20.17200 3.45900   18.93800 1.000 31.19440  ?  270 ARG   A N    1 
ATOM   722  C  CA   . ARG   A 1 118 ? 19.72000 4.58800   18.13500 1.000 30.50436  ?  270 ARG   A CA   1 
ATOM   723  C  C    . ARG   A 1 118 ? 19.18500 5.72900   18.99000 1.000 28.11273  ?  270 ARG   A C    1 
ATOM   724  O  O    . ARG   A 1 118 ? 19.18700 6.87800   18.53400 1.000 31.07798  ?  270 ARG   A O    1 
ATOM   725  C  CB   . ARG   A 1 118 ? 18.66400 4.13300   17.12000 1.000 30.71776  ?  270 ARG   A CB   1 
ATOM   726  C  CG   . ARG   A 1 118 ? 17.30600 3.81400   17.70900 1.000 32.16697  ?  270 ARG   A CG   1 
ATOM   727  C  CD   . ARG   A 1 118 ? 16.52400 2.88400   16.79200 1.000 44.66065  ?  270 ARG   A CD   1 
ATOM   728  N  NE   . ARG   A 1 118 ? 16.65100 3.25600   15.38400 1.000 46.12563  ?  270 ARG   A NE   1 
ATOM   729  C  CZ   . ARG   A 1 118 ? 15.85300 4.12000   14.76600 1.000 40.05250  ?  270 ARG   A CZ   1 
ATOM   730  N  NH1  . ARG   A 1 118 ? 14.86700 4.70000   15.43200 1.000 55.24973  ?  270 ARG   A NH1  1 
ATOM   731  N  NH2  . ARG   A 1 118 ? 16.03700 4.40400   13.48400 1.000 36.28301  ?  270 ARG   A NH2  1 
ATOM   732  N  N    . SER   A 1 119 ? 18.74900 5.44600   20.22100 1.000 25.82937  ?  271 SER   A N    1 
ATOM   733  C  CA   . SER   A 1 119 ? 18.32500 6.50800   21.12900 1.000 31.39549  ?  271 SER   A CA   1 
ATOM   734  C  C    . SER   A 1 119 ? 19.48000 7.40200   21.55900 1.000 34.43476  ?  271 SER   A C    1 
ATOM   735  O  O    . SER   A 1 119 ? 19.24200 8.52600   22.01400 1.000 40.56250  ?  271 SER   A O    1 
ATOM   736  C  CB   . SER   A 1 119 ? 17.65800 5.91100   22.37000 1.000 24.26845  ?  271 SER   A CB   1 
ATOM   737  O  OG   . SER   A 1 119 ? 18.60300 5.71300   23.41000 1.000 34.32331  ?  271 SER   A OG   1 
ATOM   738  N  N    . ASN   A 1 120 ? 20.72200 6.93200   21.42500 1.000 29.25576  ?  272 ASN   A N    1 
ATOM   739  C  CA   . ASN   A 1 120 ? 21.87300 7.71700   21.85800 1.000 30.53352  ?  272 ASN   A CA   1 
ATOM   740  C  C    . ASN   A 1 120 ? 22.06000 8.98400   21.03400 1.000 36.11733  ?  272 ASN   A C    1 
ATOM   741  O  O    . ASN   A 1 120 ? 22.69600 9.93000   21.51300 1.000 36.93363  ?  272 ASN   A O    1 
ATOM   742  C  CB   . ASN   A 1 120 ? 23.14100 6.86400   21.79500 1.000 33.89907  ?  272 ASN   A CB   1 
ATOM   743  C  CG   . ASN   A 1 120 ? 24.32300 7.51500   22.49200 1.000 41.78248  ?  272 ASN   A CG   1 
ATOM   744  O  OD1  . ASN   A 1 120 ? 25.32200 7.84900   21.85500 1.000 34.91831  ?  272 ASN   A OD1  1 
ATOM   745  N  ND2  . ASN   A 1 120 ? 24.21700 7.69200   23.80600 1.000 38.71338  ?  272 ASN   A ND2  1 
ATOM   746  N  N    A GLN   A 1 121 ? 21.51900 9.03400   19.81600 0.580 37.78216  ?  273 GLN   A N    1 
ATOM   747  N  N    B GLN   A 1 121 ? 21.53300 9.01600   19.80700 0.420 38.05372  ?  273 GLN   A N    1 
ATOM   748  C  CA   A GLN   A 1 121 ? 21.68700 10.22400  18.98800 0.580 42.51756  ?  273 GLN   A CA   1 
ATOM   749  C  CA   B GLN   A 1 121 ? 21.65200 10.20700  18.97100 0.420 42.49962  ?  273 GLN   A CA   1 
ATOM   750  C  C    A GLN   A 1 121 ? 20.91600 11.41600  19.54400 0.580 43.82479  ?  273 GLN   A C    1 
ATOM   751  C  C    B GLN   A 1 121 ? 20.95600 11.40100  19.61000 0.420 43.52753  ?  273 GLN   A C    1 
ATOM   752  O  O    A GLN   A 1 121 ? 21.32400 12.56400  19.33700 0.580 47.42225  ?  273 GLN   A O    1 
ATOM   753  O  O    B GLN   A 1 121 ? 21.45100 12.53200  19.53400 0.420 47.52372  ?  273 GLN   A O    1 
ATOM   754  C  CB   A GLN   A 1 121 ? 21.25500 9.92900   17.55400 0.580 45.13900  ?  273 GLN   A CB   1 
ATOM   755  C  CB   B GLN   A 1 121 ? 21.07200 9.93500   17.58300 0.420 45.13247  ?  273 GLN   A CB   1 
ATOM   756  C  CG   A GLN   A 1 121 ? 21.87600 8.67000   16.97000 0.580 44.37152  ?  273 GLN   A CG   1 
ATOM   757  C  CG   B GLN   A 1 121 ? 22.09800 9.53900   16.53600 0.420 45.86167  ?  273 GLN   A CG   1 
ATOM   758  C  CD   A GLN   A 1 121 ? 21.08200 8.12500   15.80100 0.580 40.67829  ?  273 GLN   A CD   1 
ATOM   759  C  CD   B GLN   A 1 121 ? 21.54600 9.61400   15.12300 0.420 40.70801  ?  273 GLN   A CD   1 
ATOM   760  O  OE1  A GLN   A 1 121 ? 20.60000 6.99100   15.83500 0.580 22.58664  ?  273 GLN   A OE1  1 
ATOM   761  O  OE1  B GLN   A 1 121 ? 21.78100 8.72400   14.30500 0.420 39.82989  ?  273 GLN   A OE1  1 
ATOM   762  N  NE2  A GLN   A 1 121 ? 20.93400 8.93700   14.76000 0.580 37.62430  ?  273 GLN   A NE2  1 
ATOM   763  N  NE2  B GLN   A 1 121 ? 20.80800 10.67900  14.83000 0.420 32.76761  ?  273 GLN   A NE2  1 
ATOM   764  N  N    . SER   A 1 122 ? 19.80800 11.17000  20.24300 1.000 33.68562  ?  274 SER   A N    1 
ATOM   765  C  CA   . SER   A 1 122 ? 19.04900 12.23300  20.88700 1.000 38.05058  ?  274 SER   A CA   1 
ATOM   766  C  C    . SER   A 1 122 ? 19.44700 12.44600  22.34100 1.000 43.86674  ?  274 SER   A C    1 
ATOM   767  O  O    . SER   A 1 122 ? 19.02600 13.43900  22.94400 1.000 48.73440  ?  274 SER   A O    1 
ATOM   768  C  CB   . SER   A 1 122 ? 17.54900 11.93300  20.81400 1.000 42.11826  ?  274 SER   A CB   1 
ATOM   769  O  OG   . SER   A 1 122 ? 17.18100 10.96400  21.78100 1.000 44.44753  ?  274 SER   A OG   1 
ATOM   770  N  N    . PHE   A 1 123 ? 20.23200 11.53800  22.91400 1.000 37.07822  ?  275 PHE   A N    1 
ATOM   771  C  CA   . PHE   A 1 123 ? 20.68300 11.69200  24.28800 1.000 38.45817  ?  275 PHE   A CA   1 
ATOM   772  C  C    . PHE   A 1 123 ? 21.67200 12.84600  24.38700 1.000 45.73960  ?  275 PHE   A C    1 
ATOM   773  O  O    . PHE   A 1 123 ? 22.53800 13.01700  23.52700 1.000 47.86133  ?  275 PHE   A O    1 
ATOM   774  C  CB   . PHE   A 1 123 ? 21.32900 10.39400  24.77400 1.000 39.59999  ?  275 PHE   A CB   1 
ATOM   775  C  CG   . PHE   A 1 123 ? 21.71600 10.40800  26.22500 1.000 40.16811  ?  275 PHE   A CG   1 
ATOM   776  C  CD1  . PHE   A 1 123 ? 20.76600 10.19100  27.21100 1.000 42.35829  ?  275 PHE   A CD1  1 
ATOM   777  C  CD2  . PHE   A 1 123 ? 23.03100 10.62900  26.60300 1.000 32.97481  ?  275 PHE   A CD2  1 
ATOM   778  C  CE1  . PHE   A 1 123 ? 21.11900 10.19900  28.54800 1.000 42.10343  ?  275 PHE   A CE1  1 
ATOM   779  C  CE2  . PHE   A 1 123 ? 23.39200 10.63800  27.93800 1.000 32.95783  ?  275 PHE   A CE2  1 
ATOM   780  C  CZ   . PHE   A 1 123 ? 22.43600 10.42200  28.91300 1.000 42.38636  ?  275 PHE   A CZ   1 
ATOM   781  N  N    . THR   A 1 124 ? 21.52900 13.65400  25.43300 1.000 47.32089  ?  276 THR   A N    1 
ATOM   782  C  CA   . THR   A 1 124 ? 22.44000 14.76100  25.68900 1.000 53.38857  ?  276 THR   A CA   1 
ATOM   783  C  C    . THR   A 1 124 ? 23.03800 14.61800  27.08100 1.000 52.78137  ?  276 THR   A C    1 
ATOM   784  O  O    . THR   A 1 124 ? 22.32700 14.31600  28.04500 1.000 54.80382  ?  276 THR   A O    1 
ATOM   785  C  CB   . THR   A 1 124 ? 21.73500 16.12000  25.55100 1.000 60.05614  ?  276 THR   A CB   1 
ATOM   786  O  OG1  . THR   A 1 124 ? 22.59000 17.15700  26.05000 1.000 66.77286  ?  276 THR   A OG1  1 
ATOM   787  C  CG2  . THR   A 1 124 ? 20.42100 16.13500  26.31700 1.000 57.99865  ?  276 THR   A CG2  1 
ATOM   788  N  N    . MET   A 1 125 ? 24.35100 14.82600  27.17800 1.000 57.67853  ?  277 MET   A N    1 
ATOM   789  C  CA   . MET   A 1 125 ? 25.04500 14.69700  28.45200 1.000 63.02803  ?  277 MET   A CA   1 
ATOM   790  C  C    . MET   A 1 125 ? 24.98400 15.96300  29.29600 1.000 66.42648  ?  277 MET   A C    1 
ATOM   791  O  O    . MET   A 1 125 ? 25.41600 15.93400  30.45300 1.000 64.52340  ?  277 MET   A O    1 
ATOM   792  C  CB   . MET   A 1 125 ? 26.50700 14.30800  28.22000 1.000 60.37822  ?  277 MET   A CB   1 
ATOM   793  C  CG   . MET   A 1 125 ? 26.69300 12.96200  27.54200 1.000 62.68993  ?  277 MET   A CG   1 
ATOM   794  S  SD   . MET   A 1 125 ? 28.28900 12.22900  27.94600 1.000 72.10324  ?  277 MET   A SD   1 
ATOM   795  C  CE   . MET   A 1 125 ? 29.32700 12.96200  26.68300 1.000 66.31355  ?  277 MET   A CE   1 
ATOM   796  N  N    . ASP   A 1 126 ? 24.46400 17.06600  28.75200 1.000 71.40871  ?  278 ASP   A N    1 
ATOM   797  C  CA   . ASP   A 1 126 ? 24.33600 18.28600  29.54300 1.000 78.54102  ?  278 ASP   A CA   1 
ATOM   798  C  C    . ASP   A 1 126 ? 23.32200 18.12700  30.66800 1.000 75.03450  ?  278 ASP   A C    1 
ATOM   799  O  O    . ASP   A 1 126 ? 23.46500 18.75900  31.72000 1.000 79.95794  ?  278 ASP   A O    1 
ATOM   800  C  CB   . ASP   A 1 126 ? 23.95700 19.46300  28.64600 1.000 91.06552  ?  278 ASP   A CB   1 
ATOM   801  C  CG   . ASP   A 1 126 ? 24.93700 19.66700  27.50700 1.000 99.83160  ?  278 ASP   A CG   1 
ATOM   802  O  OD1  . ASP   A 1 126 ? 24.52200 20.17000  26.44000 1.000 102.49389 ?  278 ASP   A OD1  1 
ATOM   803  O  OD2  . ASP   A 1 126 ? 26.12200 19.31600  27.67700 1.000 101.71285 ?  278 ASP   A OD2  1 
ATOM   804  N  N    . ASP   A 1 127 ? 22.30100 17.29000  30.47100 1.000 70.63480  ?  279 ASP   A N    1 
ATOM   805  C  CA   . ASP   A 1 127 ? 21.34800 17.00100  31.53500 1.000 69.80109  ?  279 ASP   A CA   1 
ATOM   806  C  C    . ASP   A 1 127 ? 20.95900 15.52700  31.60100 1.000 59.76634  ?  279 ASP   A C    1 
ATOM   807  O  O    . ASP   A 1 127 ? 20.00200 15.18900  32.31100 1.000 68.03404  ?  279 ASP   A O    1 
ATOM   808  C  CB   . ASP   A 1 127 ? 20.08400 17.86600  31.39300 1.000 75.96336  ?  279 ASP   A CB   1 
ATOM   809  C  CG   . ASP   A 1 127 ? 19.51200 17.84900  29.98500 1.000 77.71441  ?  279 ASP   A CG   1 
ATOM   810  O  OD1  . ASP   A 1 127 ? 19.13400 18.92900  29.48500 1.000 78.91309  ?  279 ASP   A OD1  1 
ATOM   811  O  OD2  . ASP   A 1 127 ? 19.43200 16.76100  29.38000 1.000 76.27746  ?  279 ASP   A OD2  1 
ATOM   812  N  N    . MET   A 1 128 ? 21.66400 14.64600  30.88700 1.000 57.65688  ?  280 MET   A N    1 
ATOM   813  C  CA   . MET   A 1 128 ? 21.42500 13.20100  30.93600 1.000 49.35221  ?  280 MET   A CA   1 
ATOM   814  C  C    . MET   A 1 128 ? 19.98800 12.86100  30.54400 1.000 53.93731  ?  280 MET   A C    1 
ATOM   815  O  O    . MET   A 1 128 ? 19.28900 12.11300  31.23000 1.000 48.84499  ?  280 MET   A O    1 
ATOM   816  C  CB   . MET   A 1 128 ? 21.76400 12.63600  32.31800 1.000 50.43038  ?  280 MET   A CB   1 
ATOM   817  C  CG   . MET   A 1 128 ? 23.15400 12.99500  32.80700 1.000 55.94845  ?  280 MET   A CG   1 
ATOM   818  S  SD   . MET   A 1 128 ? 24.42900 12.31900  31.73100 1.000 56.39554  ?  280 MET   A SD   1 
ATOM   819  C  CE   . MET   A 1 128 ? 25.85300 13.29000  32.21900 1.000 62.00770  ?  280 MET   A CE   1 
ATOM   820  N  N    . SER   A 1 129 ? 19.54800 13.41700  29.41800 1.000 51.05324  ?  281 SER   A N    1 
ATOM   821  C  CA   . SER   A 1 129 ? 18.18500 13.22400  28.95000 1.000 52.63982  ?  281 SER   A CA   1 
ATOM   822  C  C    . SER   A 1 129 ? 18.19800 12.97900  27.44900 1.000 50.16896  ?  281 SER   A C    1 
ATOM   823  O  O    . SER   A 1 129 ? 19.20100 13.20200  26.76600 1.000 49.05145  ?  281 SER   A O    1 
ATOM   824  C  CB   . SER   A 1 129 ? 17.30300 14.43000  29.29400 1.000 53.23744  ?  281 SER   A CB   1 
ATOM   825  O  OG   . SER   A 1 129 ? 17.52500 15.49800  28.39000 1.000 55.38234  ?  281 SER   A OG   1 
ATOM   826  N  N    . TRP   A 1 130 ? 17.06500 12.50400  26.93800 1.000 51.29314  ?  282 TRP   A N    1 
ATOM   827  C  CA   . TRP   A 1 130 ? 16.85300 12.33100  25.50600 1.000 50.99421  ?  282 TRP   A CA   1 
ATOM   828  C  C    . TRP   A 1 130 ? 16.02100 13.50900  25.01200 1.000 46.01766  ?  282 TRP   A C    1 
ATOM   829  O  O    . TRP   A 1 130 ? 14.81800 13.58400  25.28500 1.000 48.03975  ?  282 TRP   A O    1 
ATOM   830  C  CB   . TRP   A 1 130 ? 16.15300 11.00800  25.20400 1.000 45.43992  ?  282 TRP   A CB   1 
ATOM   831  C  CG   . TRP   A 1 130 ? 16.95700 9.77900   25.51000 1.000 43.43928  ?  282 TRP   A CG   1 
ATOM   832  C  CD1  . TRP   A 1 130 ? 17.68600 9.03500   24.62700 1.000 42.35500  ?  282 TRP   A CD1  1 
ATOM   833  C  CD2  . TRP   A 1 130 ? 17.09100 9.13400   26.78300 1.000 41.01067  ?  282 TRP   A CD2  1 
ATOM   834  N  NE1  . TRP   A 1 130 ? 18.27100 7.97200   25.27200 1.000 40.82129  ?  282 TRP   A NE1  1 
ATOM   835  C  CE2  . TRP   A 1 130 ? 17.92000 8.00900   26.59600 1.000 36.99466  ?  282 TRP   A CE2  1 
ATOM   836  C  CE3  . TRP   A 1 130 ? 16.59200 9.39900   28.06100 1.000 38.82651  ?  282 TRP   A CE3  1 
ATOM   837  C  CZ2  . TRP   A 1 130 ? 18.26100 7.15200   27.64000 1.000 38.26786  ?  282 TRP   A CZ2  1 
ATOM   838  C  CZ3  . TRP   A 1 130 ? 16.93300 8.54800   29.09600 1.000 42.98961  ?  282 TRP   A CZ3  1 
ATOM   839  C  CH2  . TRP   A 1 130 ? 17.76100 7.43900   28.88000 1.000 40.85056  ?  282 TRP   A CH2  1 
ATOM   840  N  N    . ASP   A 1 131 ? 16.65900 14.42600  24.29200 1.000 48.18297  ?  283 ASP   A N    1 
ATOM   841  C  CA   . ASP   A 1 131 ? 16.00600 15.63300  23.79600 1.000 59.35945  ?  283 ASP   A CA   1 
ATOM   842  C  C    . ASP   A 1 131 ? 15.60200 15.40200  22.34400 1.000 56.47961  ?  283 ASP   A C    1 
ATOM   843  O  O    . ASP   A 1 131 ? 16.46000 15.26900  21.46600 1.000 60.12880  ?  283 ASP   A O    1 
ATOM   844  C  CB   . ASP   A 1 131 ? 16.92900 16.84200  23.92900 1.000 66.42361  ?  283 ASP   A CB   1 
ATOM   845  C  CG   . ASP   A 1 131 ? 16.28900 18.13100  23.43500 1.000 78.95063  ?  283 ASP   A CG   1 
ATOM   846  O  OD1  . ASP   A 1 131 ? 15.06900 18.14000  23.16300 1.000 78.77609  ?  283 ASP   A OD1  1 
ATOM   847  O  OD2  . ASP   A 1 131 ? 17.01300 19.14300  23.32100 1.000 86.42216  ?  283 ASP   A OD2  1 
ATOM   848  N  N    . CYS   A 1 132 ? 14.29300 15.35800  22.09600 1.000 62.48253  ?  284 CYS   A N    1 
ATOM   849  C  CA   . CYS   A 1 132 ? 13.77300 15.19000  20.74500 1.000 65.25647  ?  284 CYS   A CA   1 
ATOM   850  C  C    . CYS   A 1 132 ? 13.02800 16.43900  20.29100 1.000 70.27810  ?  284 CYS   A C    1 
ATOM   851  O  O    . CYS   A 1 132 ? 11.89600 16.35100  19.80500 1.000 71.60129  ?  284 CYS   A O    1 
ATOM   852  C  CB   . CYS   A 1 132 ? 12.85300 13.97000  20.66900 1.000 59.19579  ?  284 CYS   A CB   1 
ATOM   853  S  SG   . CYS   A 1 132 ? 13.64000 12.41300  21.12200 1.000 46.40747  ?  284 CYS   A SG   1 
ATOM   854  N  N    . GLY   A 1 133 ? 13.65000 17.60500  20.44900 1.000 77.36287  ?  285 GLY   A N    1 
ATOM   855  C  CA   . GLY   A 1 133 ? 13.04500 18.84500  20.00400 1.000 87.59571  ?  285 GLY   A CA   1 
ATOM   856  C  C    . GLY   A 1 133 ? 12.32500 19.60800  21.09700 1.000 93.88671  ?  285 GLY   A C    1 
ATOM   857  O  O    . GLY   A 1 133 ? 12.95700 20.29500  21.90500 1.000 99.06794  ?  285 GLY   A O    1 
ATOM   858  N  N    . SER   A 1 134 ? 11.00000 19.49500  21.13200 1.000 92.97339  ?  286 SER   A N    1 
ATOM   859  C  CA   . SER   A 1 134 ? 10.20400 20.24400  22.09200 1.000 90.24614  ?  286 SER   A CA   1 
ATOM   860  C  C    . SER   A 1 134 ? 10.36900 19.67800  23.50100 1.000 86.97543  ?  286 SER   A C    1 
ATOM   861  O  O    . SER   A 1 134 ? 10.87400 18.57000  23.70500 1.000 85.31474  ?  286 SER   A O    1 
ATOM   862  C  CB   . SER   A 1 134 ? 8.72900  20.23000  21.69000 1.000 89.49397  ?  286 SER   A CB   1 
ATOM   863  O  OG   . SER   A 1 134 ? 8.04800  19.13900  22.28700 1.000 88.36235  ?  286 SER   A OG   1 
ATOM   864  N  N    . GLN   A 1 135 ? 9.92900  20.46800  24.48600 1.000 91.13745  ?  287 GLN   A N    1 
ATOM   865  C  CA   . GLN   A 1 135 ? 10.03500 20.05400  25.88300 1.000 95.12849  ?  287 GLN   A CA   1 
ATOM   866  C  C    . GLN   A 1 135 ? 9.10500  18.88900  26.19600 1.000 89.96879  ?  287 GLN   A C    1 
ATOM   867  O  O    . GLN   A 1 135 ? 9.43800  18.02700  27.01700 1.000 84.28709  ?  287 GLN   A O    1 
ATOM   868  C  CB   . GLN   A 1 135 ? 9.73500  21.23100  26.80800 1.000 103.63267 ?  287 GLN   A CB   1 
ATOM   869  C  CG   . GLN   A 1 135 ? 10.27900 22.57000  26.32800 1.000 112.33239 ?  287 GLN   A CG   1 
ATOM   870  C  CD   . GLN   A 1 135 ? 9.26200  23.37100  25.53900 1.000 118.59527 ?  287 GLN   A CD   1 
ATOM   871  O  OE1  . GLN   A 1 135 ? 8.28500  23.87600  26.09400 1.000 121.14959 ?  287 GLN   A OE1  1 
ATOM   872  N  NE2  . GLN   A 1 135 ? 9.49300  23.50100  24.23700 1.000 118.45058 ?  287 GLN   A NE2  1 
ATOM   873  N  N    . ASP   A 1 136 ? 7.93500  18.84600  25.55500 1.000 90.05844  ?  288 ASP   A N    1 
ATOM   874  C  CA   . ASP   A 1 136 ? 7.03500  17.71100  25.71800 1.000 88.85606  ?  288 ASP   A CA   1 
ATOM   875  C  C    . ASP   A 1 136 ? 7.71500  16.40700  25.33700 1.000 82.50604  ?  288 ASP   A C    1 
ATOM   876  O  O    . ASP   A 1 136 ? 7.40400  15.35600  25.90600 1.000 73.57973  ?  288 ASP   A O    1 
ATOM   877  C  CB   . ASP   A 1 136 ? 5.77700  17.91600  24.87200 1.000 90.93350  ?  288 ASP   A CB   1 
ATOM   878  C  CG   . ASP   A 1 136 ? 4.80200  18.89000  25.49500 1.000 98.20041  ?  288 ASP   A CG   1 
ATOM   879  O  OD1  . ASP   A 1 136 ? 5.20300  19.64800  26.40400 1.000 101.88048 ?  288 ASP   A OD1  1 
ATOM   880  O  OD2  . ASP   A 1 136 ? 3.62800  18.90200  25.06800 1.000 101.24570 ?  288 ASP   A OD2  1 
ATOM   881  N  N    . TYR   A 1 137 ? 8.64200  16.45400  24.38500 1.000 82.26932  ?  289 TYR   A N    1 
ATOM   882  C  CA   . TYR   A 1 137 ? 9.35100  15.27600  23.90200 1.000 73.70093  ?  289 TYR   A CA   1 
ATOM   883  C  C    . TYR   A 1 137 ? 10.82100 15.31800  24.31000 1.000 59.63253  ?  289 TYR   A C    1 
ATOM   884  O  O    . TYR   A 1 137 ? 11.71200 14.92700  23.55400 1.000 53.52414  ?  289 TYR   A O    1 
ATOM   885  C  CB   . TYR   A 1 137 ? 9.18400  15.14600  22.39100 1.000 73.04293  ?  289 TYR   A CB   1 
ATOM   886  C  CG   . TYR   A 1 137 ? 7.72600  15.18200  21.98700 1.000 69.28688  ?  289 TYR   A CG   1 
ATOM   887  C  CD1  . TYR   A 1 137 ? 7.29500  15.94000  20.90600 1.000 73.05774  ?  289 TYR   A CD1  1 
ATOM   888  C  CD2  . TYR   A 1 137 ? 6.77600  14.46200  22.70100 1.000 64.80180  ?  289 TYR   A CD2  1 
ATOM   889  C  CE1  . TYR   A 1 137 ? 5.95800  15.97500  20.54600 1.000 72.68226  ?  289 TYR   A CE1  1 
ATOM   890  C  CE2  . TYR   A 1 137 ? 5.44200  14.49000  22.34700 1.000 67.60973  ?  289 TYR   A CE2  1 
ATOM   891  C  CZ   . TYR   A 1 137 ? 5.03700  15.24600  21.27200 1.000 70.51193  ?  289 TYR   A CZ   1 
ATOM   892  O  OH   . TYR   A 1 137 ? 3.70600  15.27000  20.92600 1.000 70.22667  ?  289 TYR   A OH   1 
ATOM   893  N  N    . LYS   A 1 138 ? 11.07700 15.80800  25.52100 1.000 55.28311  ?  290 LYS   A N    1 
ATOM   894  C  CA   . LYS   A 1 138 ? 12.38700 15.75400  26.16200 1.000 57.81258  ?  290 LYS   A CA   1 
ATOM   895  C  C    . LYS   A 1 138 ? 12.24100 14.86200  27.38900 1.000 63.12298  ?  290 LYS   A C    1 
ATOM   896  O  O    . LYS   A 1 138 ? 11.52500 15.21100  28.33300 1.000 63.97858  ?  290 LYS   A O    1 
ATOM   897  C  CB   . LYS   A 1 138 ? 12.87900 17.15300  26.53400 1.000 65.97916  ?  290 LYS   A CB   1 
ATOM   898  C  CG   . LYS   A 1 138 ? 14.07000 17.17300  27.48000 1.000 72.77023  ?  290 LYS   A CG   1 
ATOM   899  C  CD   . LYS   A 1 138 ? 15.06800 18.24800  27.07900 1.000 77.64898  ?  290 LYS   A CD   1 
ATOM   900  C  CE   . LYS   A 1 138 ? 16.14300 18.42800  28.13800 1.000 78.90301  ?  290 LYS   A CE   1 
ATOM   901  N  NZ   . LYS   A 1 138 ? 17.33900 19.13600  27.60400 1.000 78.94636  ?  290 LYS   A NZ   1 
ATOM   902  N  N    . TYR   A 1 139 ? 12.90900 13.71200  27.37000 1.000 58.04796  ?  291 TYR   A N    1 
ATOM   903  C  CA   . TYR   A 1 139 ? 12.66400 12.63900  28.32200 1.000 57.03195  ?  291 TYR   A CA   1 
ATOM   904  C  C    . TYR   A 1 139 ? 13.85500 12.45700  29.25300 1.000 62.62364  ?  291 TYR   A C    1 
ATOM   905  O  O    . TYR   A 1 139 ? 15.00500 12.45600  28.80400 1.000 61.50909  ?  291 TYR   A O    1 
ATOM   906  C  CB   . TYR   A 1 139 ? 12.39300 11.32700  27.58400 1.000 51.26720  ?  291 TYR   A CB   1 
ATOM   907  C  CG   . TYR   A 1 139 ? 11.37700 11.42800  26.46600 1.000 50.90961  ?  291 TYR   A CG   1 
ATOM   908  C  CD1  . TYR   A 1 139 ? 11.78300 11.53500  25.14200 1.000 48.95930  ?  291 TYR   A CD1  1 
ATOM   909  C  CD2  . TYR   A 1 139 ? 10.01400 11.40100  26.73400 1.000 47.38110  ?  291 TYR   A CD2  1 
ATOM   910  C  CE1  . TYR   A 1 139 ? 10.86000 11.62200  24.11600 1.000 43.16893  ?  291 TYR   A CE1  1 
ATOM   911  C  CE2  . TYR   A 1 139 ? 9.08300  11.48800  25.71500 1.000 48.41485  ?  291 TYR   A CE2  1 
ATOM   912  C  CZ   . TYR   A 1 139 ? 9.51000  11.59800  24.40800 1.000 54.21181  ?  291 TYR   A CZ   1 
ATOM   913  O  OH   . TYR   A 1 139 ? 8.58300  11.68400  23.39200 1.000 53.08960  ?  291 TYR   A OH   1 
ATOM   914  N  N    . ASP   A 1 140 ? 13.57700 12.27500  30.54500 1.000 64.94206  ?  292 ASP   A N    1 
ATOM   915  C  CA   . ASP   A 1 140 ? 14.61100 12.00900  31.53800 1.000 66.35441  ?  292 ASP   A CA   1 
ATOM   916  C  C    . ASP   A 1 140 ? 14.30600 10.70600  32.28300 1.000 60.62148  ?  292 ASP   A C    1 
ATOM   917  O  O    . ASP   A 1 140 ? 13.42500 9.93400   31.89600 1.000 58.90736  ?  292 ASP   A O    1 
ATOM   918  C  CB   . ASP   A 1 140 ? 14.76200 13.20100  32.49000 1.000 69.71233  ?  292 ASP   A CB   1 
ATOM   919  C  CG   . ASP   A 1 140 ? 13.48600 13.52700  33.25700 1.000 69.30091  ?  292 ASP   A CG   1 
ATOM   920  O  OD1  . ASP   A 1 140 ? 13.30000 14.71500  33.59300 1.000 75.78300  ?  292 ASP   A OD1  1 
ATOM   921  O  OD2  . ASP   A 1 140 ? 12.67300 12.62300  33.53500 1.000 67.32994  ?  292 ASP   A OD2  1 
ATOM   922  N  N    . VAL   A 1 141 ? 15.03600 10.48100  33.37900 1.000 58.59864  ?  293 VAL   A N    1 
ATOM   923  C  CA   . VAL   A 1 141 ? 14.91000 9.23700   34.13100 1.000 50.22915  ?  293 VAL   A CA   1 
ATOM   924  C  C    . VAL   A 1 141 ? 13.54900 9.13900   34.80600 1.000 51.14914  ?  293 VAL   A C    1 
ATOM   925  O  O    . VAL   A 1 141 ? 12.99800 8.04000   34.95100 1.000 51.11624  ?  293 VAL   A O    1 
ATOM   926  C  CB   . VAL   A 1 141 ? 16.05600 9.11900   35.15400 1.000 43.63627  ?  293 VAL   A CB   1 
ATOM   927  C  CG1  . VAL   A 1 141 ? 17.36600 8.85300   34.44500 1.000 45.52132  ?  293 VAL   A CG1  1 
ATOM   928  C  CG2  . VAL   A 1 141 ? 16.15000 10.37800  35.99900 1.000 46.04656  ?  293 VAL   A CG2  1 
ATOM   929  N  N    . THR   A 1 142 ? 12.98900 10.27000  35.24200 1.000 52.90900  ?  294 THR   A N    1 
ATOM   930  C  CA   . THR   A 1 142 ? 11.67800 10.24000  35.88100 1.000 55.59192  ?  294 THR   A CA   1 
ATOM   931  C  C    . THR   A 1 142 ? 10.59200 9.80900   34.90500 1.000 48.86736  ?  294 THR   A C    1 
ATOM   932  O  O    . THR   A 1 142 ? 9.57900  9.23300   35.32000 1.000 49.56745  ?  294 THR   A O    1 
ATOM   933  C  CB   . THR   A 1 142 ? 11.34900 11.60700  36.48000 1.000 55.52959  ?  294 THR   A CB   1 
ATOM   934  O  OG1  . THR   A 1 142 ? 11.19100 12.56700  35.42700 1.000 66.30028  ?  294 THR   A OG1  1 
ATOM   935  C  CG2  . THR   A 1 142 ? 12.46600 12.06000  37.40800 1.000 53.89681  ?  294 THR   A CG2  1 
ATOM   936  N  N    . ASP   A 1 143 ? 10.78400 10.07000  33.61100 1.000 49.31832  ?  295 ASP   A N    1 
ATOM   937  C  CA   . ASP   A 1 143 ? 9.83300  9.58700   32.61500 1.000 45.89696  ?  295 ASP   A CA   1 
ATOM   938  C  C    . ASP   A 1 143 ? 9.90400  8.07100   32.48200 1.000 42.37419  ?  295 ASP   A C    1 
ATOM   939  O  O    . ASP   A 1 143 ? 8.87800  7.41200   32.27600 1.000 42.65350  ?  295 ASP   A O    1 
ATOM   940  C  CB   . ASP   A 1 143 ? 10.09500 10.26300  31.26900 1.000 45.67495  ?  295 ASP   A CB   1 
ATOM   941  C  CG   . ASP   A 1 143 ? 9.67900  11.72300  31.25900 1.000 51.57885  ?  295 ASP   A CG   1 
ATOM   942  O  OD1  . ASP   A 1 143 ? 8.69800  12.07000  31.95000 1.000 55.65270  ?  295 ASP   A OD1  1 
ATOM   943  O  OD2  . ASP   A 1 143 ? 10.33500 12.52600  30.56400 1.000 51.43610  ?  295 ASP   A OD2  1 
ATOM   944  N  N    . VAL   A 1 144 ? 11.10400 7.50000   32.60300 1.000 45.61589  ?  296 VAL   A N    1 
ATOM   945  C  CA   . VAL   A 1 144 ? 11.24200 6.04800   32.54200 1.000 43.44886  ?  296 VAL   A CA   1 
ATOM   946  C  C    . VAL   A 1 144 ? 10.59100 5.40100   33.75700 1.000 38.47466  ?  296 VAL   A C    1 
ATOM   947  O  O    . VAL   A 1 144 ? 9.92000  4.36900   33.64300 1.000 40.04552  ?  296 VAL   A O    1 
ATOM   948  C  CB   . VAL   A 1 144 ? 12.72500 5.65400   32.42300 1.000 48.34595  ?  296 VAL   A CB   1 
ATOM   949  C  CG1  . VAL   A 1 144 ? 12.86000 4.14600   32.28300 1.000 44.59410  ?  296 VAL   A CG1  1 
ATOM   950  C  CG2  . VAL   A 1 144 ? 13.37500 6.36800   31.25400 1.000 49.68651  ?  296 VAL   A CG2  1 
ATOM   951  N  N    . SER   A 1 145 ? 10.78400 5.99200   34.93900 1.000 45.21082  ?  297 SER   A N    1 
ATOM   952  C  CA   . SER   A 1 145 ? 10.16300 5.44700   36.14000 1.000 46.74192  ?  297 SER   A CA   1 
ATOM   953  C  C    . SER   A 1 145 ? 8.65100  5.62800   36.11600 1.000 49.66979  ?  297 SER   A C    1 
ATOM   954  O  O    . SER   A 1 145 ? 7.91900  4.77500   36.63100 1.000 44.46850  ?  297 SER   A O    1 
ATOM   955  C  CB   . SER   A 1 145 ? 10.76500 6.09600   37.38700 1.000 49.87093  ?  297 SER   A CB   1 
ATOM   956  O  OG   . SER   A 1 145 ? 10.18000 7.36000   37.64200 1.000 57.00922  ?  297 SER   A OG   1 
ATOM   957  N  N    . LYS   A 1 146 ? 8.16300  6.71500   35.51400 1.000 45.81983  ?  298 LYS   A N    1 
ATOM   958  C  CA   . LYS   A 1 146 ? 6.73400  6.91500   35.32000 1.000 49.98924  ?  298 LYS   A CA   1 
ATOM   959  C  C    . LYS   A 1 146 ? 6.16700  6.04400   34.20500 1.000 54.90637  ?  298 LYS   A C    1 
ATOM   960  O  O    . LYS   A 1 146 ? 5.05600  6.30700   33.72800 1.000 49.88213  ?  298 LYS   A O    1 
ATOM   961  C  CB   . LYS   A 1 146 ? 6.43700  8.39100   35.04500 1.000 52.71696  ?  298 LYS   A CB   1 
ATOM   962  C  CG   . LYS   A 1 146 ? 6.16000  9.19300   36.30900 1.000 63.90237  ?  298 LYS   A CG   1 
ATOM   963  C  CD   . LYS   A 1 146 ? 6.28000  10.68900  36.07600 1.000 75.13044  ?  298 LYS   A CD   1 
ATOM   964  C  CE   . LYS   A 1 146 ? 6.95200  11.37100  37.25800 1.000 81.77907  ?  298 LYS   A CE   1 
ATOM   965  N  NZ   . LYS   A 1 146 ? 6.40800  12.73600  37.49700 1.000 84.87704  ?  298 LYS   A NZ   1 
ATOM   966  N  N    . ALA   A 1 147 ? 6.91700  5.03100   33.76800 1.000 48.58390  ?  299 ALA   A N    1 
ATOM   967  C  CA   . ALA   A 1 147 ? 6.40600  3.98500   32.89700 1.000 43.66294  ?  299 ALA   A CA   1 
ATOM   968  C  C    . ALA   A 1 147 ? 6.49200  2.60500   33.53400 1.000 51.43334  ?  299 ALA   A C    1 
ATOM   969  O  O    . ALA   A 1 147 ? 6.16800  1.61200   32.87200 1.000 48.34607  ?  299 ALA   A O    1 
ATOM   970  C  CB   . ALA   A 1 147 ? 7.15700  3.97800   31.55900 1.000 41.76678  ?  299 ALA   A CB   1 
ATOM   971  N  N    . GLY   A 1 148 ? 6.93100  2.51400   34.78900 1.000 49.52613  ?  300 GLY   A N    1 
ATOM   972  C  CA   . GLY   A 1 148 ? 6.98100  1.25800   35.51200 1.000 51.56433  ?  300 GLY   A CA   1 
ATOM   973  C  C    . GLY   A 1 148 ? 8.36600  0.69800   35.74900 1.000 50.53318  ?  300 GLY   A C    1 
ATOM   974  O  O    . GLY   A 1 148 ? 8.48300  -0.36200  36.37700 1.000 43.54867  ?  300 GLY   A O    1 
ATOM   975  N  N    . HIS   A 1 149 ? 9.41700  1.36400   35.28600 1.000 38.93772  ?  301 HIS   A N    1 
ATOM   976  C  CA   . HIS   A 1 149 ? 10.76100 0.81600   35.36500 1.000 39.61777  ?  301 HIS   A CA   1 
ATOM   977  C  C    . HIS   A 1 149 ? 11.51300 1.37500   36.56700 1.000 39.75863  ?  301 HIS   A C    1 
ATOM   978  O  O    . HIS   A 1 149 ? 11.29300 2.51100   36.99300 1.000 45.24464  ?  301 HIS   A O    1 
ATOM   979  C  CB   . HIS   A 1 149 ? 11.53000 1.09800   34.07400 1.000 40.49750  ?  301 HIS   A CB   1 
ATOM   980  C  CG   . HIS   A 1 149 ? 11.13200 0.20800   32.93900 1.000 42.98017  ?  301 HIS   A CG   1 
ATOM   981  N  ND1  . HIS   A 1 149 ? 11.42800 -1.13800  32.91000 1.000 43.06339  ?  301 HIS   A ND1  1 
ATOM   982  C  CD2  . HIS   A 1 149 ? 10.43900 0.46500   31.80400 1.000 40.40559  ?  301 HIS   A CD2  1 
ATOM   983  C  CE1  . HIS   A 1 149 ? 10.94600 -1.66800  31.79900 1.000 45.77857  ?  301 HIS   A CE1  1 
ATOM   984  N  NE2  . HIS   A 1 149 ? 10.34200 -0.71600  31.11100 1.000 36.18602  ?  301 HIS   A NE2  1 
ATOM   985  N  N    . THR   A 1 150 ? 12.40800 0.55500   37.10900 1.000 41.42928  ?  302 THR   A N    1 
ATOM   986  C  CA   . THR   A 1 150 ? 13.11500 0.83100   38.35000 1.000 41.96929  ?  302 THR   A CA   1 
ATOM   987  C  C    . THR   A 1 150 ? 14.57400 1.17900   38.06300 1.000 38.80945  ?  302 THR   A C    1 
ATOM   988  O  O    . THR   A 1 150 ? 15.03200 1.16900   36.91700 1.000 39.47924  ?  302 THR   A O    1 
ATOM   989  C  CB   . THR   A 1 150 ? 13.01600 -0.37000  39.29300 1.000 42.99637  ?  302 THR   A CB   1 
ATOM   990  O  OG1  . THR   A 1 150 ? 13.88600 -1.41000  38.83200 1.000 46.20659  ?  302 THR   A OG1  1 
ATOM   991  C  CG2  . THR   A 1 150 ? 11.58500 -0.89600  39.33400 1.000 45.83494  ?  302 THR   A CG2  1 
ATOM   992  N  N    . LEU   A 1 151 ? 15.31200 1.48500   39.13400 1.000 40.69826  ?  303 LEU   A N    1 
ATOM   993  C  CA   . LEU   A 1 151 ? 16.71600 1.85200   38.98800 1.000 43.75885  ?  303 LEU   A CA   1 
ATOM   994  C  C    . LEU   A 1 151 ? 17.57600 0.68500   38.52300 1.000 37.71061  ?  303 LEU   A C    1 
ATOM   995  O  O    . LEU   A 1 151 ? 18.63000 0.91400   37.91700 1.000 37.94147  ?  303 LEU   A O    1 
ATOM   996  C  CB   . LEU   A 1 151 ? 17.25700 2.40500   40.30600 1.000 47.99883  ?  303 LEU   A CB   1 
ATOM   997  C  CG   . LEU   A 1 151 ? 18.58500 3.15700   40.20100 1.000 63.92328  ?  303 LEU   A CG   1 
ATOM   998  C  CD1  . LEU   A 1 151 ? 18.35600 4.65300   40.05000 1.000 76.21002  ?  303 LEU   A CD1  1 
ATOM   999  C  CD2  . LEU   A 1 151 ? 19.46500 2.86300   41.39900 1.000 69.52415  ?  303 LEU   A CD2  1 
ATOM   1000 N  N    . GLU   A 1 152 ? 17.14700 -0.55500  38.78300 1.000 38.67363  ?  304 GLU   A N    1 
ATOM   1001 C  CA   . GLU   A 1 152 ? 17.88900 -1.72400  38.31600 1.000 40.44180  ?  304 GLU   A CA   1 
ATOM   1002 C  C    . GLU   A 1 152 ? 18.14800 -1.66400  36.81700 1.000 45.23794  ?  304 GLU   A C    1 
ATOM   1003 O  O    . GLU   A 1 152 ? 19.15900 -2.19000  36.33600 1.000 41.66818  ?  304 GLU   A O    1 
ATOM   1004 C  CB   . GLU   A 1 152 ? 17.12600 -3.00500  38.66500 1.000 42.43158  ?  304 GLU   A CB   1 
ATOM   1005 C  CG   . GLU   A 1 152 ? 17.58200 -3.67100  39.95300 1.000 55.53223  ?  304 GLU   A CG   1 
ATOM   1006 C  CD   . GLU   A 1 152 ? 16.63100 -3.42400  41.10900 1.000 72.64547  ?  304 GLU   A CD   1 
ATOM   1007 O  OE1  . GLU   A 1 152 ? 16.75300 -4.11700  42.14200 1.000 82.50832  ?  304 GLU   A OE1  1 
ATOM   1008 O  OE2  . GLU   A 1 152 ? 15.76000 -2.53900  40.98300 1.000 80.58714  ?  304 GLU   A OE2  1 
ATOM   1009 N  N    . LEU   A 1 153 ? 17.25100 -1.02900  36.06600 1.000 37.46062  ?  305 LEU   A N    1 
ATOM   1010 C  CA   . LEU   A 1 153 ? 17.44900 -0.77300  34.64600 1.000 33.14935  ?  305 LEU   A CA   1 
ATOM   1011 C  C    . LEU   A 1 153 ? 17.88700 0.65700   34.36200 1.000 36.35101  ?  305 LEU   A C    1 
ATOM   1012 O  O    . LEU   A 1 153 ? 18.75000 0.87600   33.50600 1.000 36.30531  ?  305 LEU   A O    1 
ATOM   1013 C  CB   . LEU   A 1 153 ? 16.15900 -1.07200  33.87100 1.000 30.88328  ?  305 LEU   A CB   1 
ATOM   1014 C  CG   . LEU   A 1 153 ? 16.11900 -0.68500  32.39000 1.000 34.04776  ?  305 LEU   A CG   1 
ATOM   1015 C  CD1  . LEU   A 1 153 ? 17.10000 -1.52700  31.59200 1.000 31.40740  ?  305 LEU   A CD1  1 
ATOM   1016 C  CD2  . LEU   A 1 153 ? 14.70500 -0.82000  31.82800 1.000 38.27951  ?  305 LEU   A CD2  1 
ATOM   1017 N  N    . ILE   A 1 154 ? 17.33300 1.63000   35.08900 1.000 34.40742  ?  306 ILE   A N    1 
ATOM   1018 C  CA   . ILE   A 1 154 ? 17.51400 3.03500   34.73000 1.000 34.41856  ?  306 ILE   A CA   1 
ATOM   1019 C  C    . ILE   A 1 154 ? 18.97000 3.45700   34.89200 1.000 36.90707  ?  306 ILE   A C    1 
ATOM   1020 O  O    . ILE   A 1 154 ? 19.54100 4.11000   34.01000 1.000 36.24264  ?  306 ILE   A O    1 
ATOM   1021 C  CB   . ILE   A 1 154 ? 16.57000 3.92500   35.55900 1.000 42.96474  ?  306 ILE   A CB   1 
ATOM   1022 C  CG1  . ILE   A 1 154 ? 15.13600 3.79700   35.04000 1.000 46.77088  ?  306 ILE   A CG1  1 
ATOM   1023 C  CG2  . ILE   A 1 154 ? 17.02800 5.37200   35.51600 1.000 47.74930  ?  306 ILE   A CG2  1 
ATOM   1024 C  CD1  . ILE   A 1 154 ? 14.08700 4.26200   36.02600 1.000 56.18278  ?  306 ILE   A CD1  1 
ATOM   1025 N  N    . GLU   A 1 155 ? 19.59600 3.09900   36.01700 1.000 39.47196  ?  307 GLU   A N    1 
ATOM   1026 C  CA   . GLU   A 1 155 ? 20.97400 3.54300   36.22900 1.000 36.60673  ?  307 GLU   A CA   1 
ATOM   1027 C  C    . GLU   A 1 155 ? 21.96000 2.87900   35.27400 1.000 36.74290  ?  307 GLU   A C    1 
ATOM   1028 O  O    . GLU   A 1 155 ? 22.81300 3.59200   34.71600 1.000 39.61665  ?  307 GLU   A O    1 
ATOM   1029 C  CB   . GLU   A 1 155 ? 21.38000 3.34700   37.69100 1.000 53.34050  ?  307 GLU   A CB   1 
ATOM   1030 C  CG   . GLU   A 1 155 ? 22.47200 4.31800   38.12300 1.000 71.40718  ?  307 GLU   A CG   1 
ATOM   1031 C  CD   . GLU   A 1 155 ? 23.31700 3.79200   39.25700 1.000 81.00515  ?  307 GLU   A CD   1 
ATOM   1032 O  OE1  . GLU   A 1 155 ? 23.28300 4.39100   40.34700 1.000 86.49037  ?  307 GLU   A OE1  1 
ATOM   1033 O  OE2  . GLU   A 1 155 ? 24.01500 2.77900   39.05500 1.000 81.63887  ?  307 GLU   A OE2  1 
ATOM   1034 N  N    . PRO   A 1 156 ? 21.92400 1.56000   35.04000 1.000 36.13806  ?  308 PRO   A N    1 
ATOM   1035 C  CA   . PRO   A 1 156 ? 22.80200 1.00600   33.99300 1.000 35.51537  ?  308 PRO   A CA   1 
ATOM   1036 C  C    . PRO   A 1 156 ? 22.51100 1.56800   32.61200 1.000 38.05351  ?  308 PRO   A C    1 
ATOM   1037 O  O    . PRO   A 1 156 ? 23.41600 1.61000   31.76800 1.000 36.81355  ?  308 PRO   A O    1 
ATOM   1038 C  CB   . PRO   A 1 156 ? 22.52700 -0.50500  34.05600 1.000 44.13843  ?  308 PRO   A CB   1 
ATOM   1039 C  CG   . PRO   A 1 156 ? 21.94300 -0.74100  35.40100 1.000 48.27512  ?  308 PRO   A CG   1 
ATOM   1040 C  CD   . PRO   A 1 156 ? 21.16900 0.49600   35.72900 1.000 33.09707  ?  308 PRO   A CD   1 
ATOM   1041 N  N    . LEU   A 1 157 ? 21.27400 2.00400   32.35700 1.000 38.40429  ?  309 LEU   A N    1 
ATOM   1042 C  CA   . LEU   A 1 157 ? 20.93000 2.55000   31.04700 1.000 30.01460  ?  309 LEU   A CA   1 
ATOM   1043 C  C    . LEU   A 1 157 ? 21.56000 3.92100   30.83900 1.000 30.65781  ?  309 LEU   A C    1 
ATOM   1044 O  O    . LEU   A 1 157 ? 22.09600 4.21200   29.76300 1.000 28.33149  ?  309 LEU   A O    1 
ATOM   1045 C  CB   . LEU   A 1 157 ? 19.41100 2.62800   30.89200 1.000 30.51638  ?  309 LEU   A CB   1 
ATOM   1046 C  CG   . LEU   A 1 157 ? 18.89900 3.36500   29.65400 1.000 32.84415  ?  309 LEU   A CG   1 
ATOM   1047 C  CD1  . LEU   A 1 157 ? 19.34700 2.64800   28.38600 1.000 30.12461  ?  309 LEU   A CD1  1 
ATOM   1048 C  CD2  . LEU   A 1 157 ? 17.38100 3.50300   29.69000 1.000 34.31417  ?  309 LEU   A CD2  1 
ATOM   1049 N  N    . ILE   A 1 158 ? 21.50100 4.78200   31.85900 1.000 36.25034  ?  310 ILE   A N    1 
ATOM   1050 C  CA   . ILE   A 1 158 ? 22.14000 6.09200   31.76000 1.000 39.60373  ?  310 ILE   A CA   1 
ATOM   1051 C  C    . ILE   A 1 158 ? 23.65200 5.93900   31.63600 1.000 37.54133  ?  310 ILE   A C    1 
ATOM   1052 O  O    . ILE   A 1 158 ? 24.29600 6.63900   30.84400 1.000 38.70617  ?  310 ILE   A O    1 
ATOM   1053 C  CB   . ILE   A 1 158 ? 21.75200 6.97300   32.96200 1.000 41.24561  ?  310 ILE   A CB   1 
ATOM   1054 C  CG1  . ILE   A 1 158 ? 20.25100 7.27100   32.94800 1.000 44.55938  ?  310 ILE   A CG1  1 
ATOM   1055 C  CG2  . ILE   A 1 158 ? 22.55700 8.26700   32.95600 1.000 44.84703  ?  310 ILE   A CG2  1 
ATOM   1056 C  CD1  . ILE   A 1 158 ? 19.81400 8.17400   31.80900 1.000 48.19522  ?  310 ILE   A CD1  1 
ATOM   1057 N  N    . LYS   A 1 159 ? 24.24300 5.02200   32.41100 1.000 35.73289  ?  311 LYS   A N    1 
ATOM   1058 C  CA   . LYS   A 1 159 ? 25.67700 4.76700   32.28800 1.000 41.21667  ?  311 LYS   A CA   1 
ATOM   1059 C  C    . LYS   A 1 159 ? 26.03100 4.31300   30.87800 1.000 37.19970  ?  311 LYS   A C    1 
ATOM   1060 O  O    . LYS   A 1 159 ? 27.06900 4.70600   30.33200 1.000 38.44273  ?  311 LYS   A O    1 
ATOM   1061 C  CB   . LYS   A 1 159 ? 26.12300 3.72300   33.31700 1.000 46.73823  ?  311 LYS   A CB   1 
ATOM   1062 C  CG   . LYS   A 1 159 ? 27.62600 3.46800   33.37100 1.000 72.93972  ?  311 LYS   A CG   1 
ATOM   1063 C  CD   . LYS   A 1 159 ? 28.06400 2.35700   32.43400 1.000 84.86562  ?  311 LYS   A CD   1 
ATOM   1064 C  CE   . LYS   A 1 159 ? 29.47800 2.57900   31.93800 1.000 91.76579  ?  311 LYS   A CE   1 
ATOM   1065 N  NZ   . LYS   A 1 159 ? 29.72700 1.86800   30.64200 1.000 92.54096  ?  311 LYS   A NZ   1 
ATOM   1066 N  N    . PHE   A 1 160 ? 25.18600 3.47300   30.27900 1.000 35.14095  ?  312 PHE   A N    1 
ATOM   1067 C  CA   . PHE   A 1 160 ? 25.43500 3.02300   28.91500 1.000 34.75344  ?  312 PHE   A CA   1 
ATOM   1068 C  C    . PHE   A 1 160 ? 25.38300 4.19100   27.94100 1.000 38.33183  ?  312 PHE   A C    1 
ATOM   1069 O  O    . PHE   A 1 160 ? 26.26900 4.34600   27.09200 1.000 35.98386  ?  312 PHE   A O    1 
ATOM   1070 C  CB   . PHE   A 1 160 ? 24.42000 1.94700   28.52500 1.000 31.58312  ?  312 PHE   A CB   1 
ATOM   1071 C  CG   . PHE   A 1 160 ? 24.51300 1.52300   27.08900 1.000 29.48996  ?  312 PHE   A CG   1 
ATOM   1072 C  CD1  . PHE   A 1 160 ? 25.43600 0.56700   26.69600 1.000 31.53940  ?  312 PHE   A CD1  1 
ATOM   1073 C  CD2  . PHE   A 1 160 ? 23.68700 2.08700   26.13000 1.000 33.05362  ?  312 PHE   A CD2  1 
ATOM   1074 C  CE1  . PHE   A 1 160 ? 25.53200 0.18100   25.37000 1.000 34.21718  ?  312 PHE   A CE1  1 
ATOM   1075 C  CE2  . PHE   A 1 160 ? 23.77900 1.70500   24.80600 1.000 36.86239  ?  312 PHE   A CE2  1 
ATOM   1076 C  CZ   . PHE   A 1 160 ? 24.70200 0.75100   24.42600 1.000 30.83414  ?  312 PHE   A CZ   1 
ATOM   1077 N  N    . GLN   A 1 161 ? 24.34500 5.02700   28.05100 1.000 40.33973  ?  313 GLN   A N    1 
ATOM   1078 C  CA   . GLN   A 1 161 ? 24.20500 6.16900   27.15300 1.000 35.92460  ?  313 GLN   A CA   1 
ATOM   1079 C  C    . GLN   A 1 161 ? 25.39000 7.12000   27.27500 1.000 36.41477  ?  313 GLN   A C    1 
ATOM   1080 O  O    . GLN   A 1 161 ? 25.86200 7.67000   26.27300 1.000 36.07121  ?  313 GLN   A O    1 
ATOM   1081 C  CB   . GLN   A 1 161 ? 22.89700 6.90600   27.44600 1.000 34.21268  ?  313 GLN   A CB   1 
ATOM   1082 C  CG   . GLN   A 1 161 ? 21.64200 6.08200   27.19500 1.000 31.43334  ?  313 GLN   A CG   1 
ATOM   1083 C  CD   . GLN   A 1 161 ? 21.46600 5.72600   25.73300 1.000 31.99417  ?  313 GLN   A CD   1 
ATOM   1084 O  OE1  . GLN   A 1 161 ? 21.75600 6.53200   24.85100 1.000 36.49102  ?  313 GLN   A OE1  1 
ATOM   1085 N  NE2  . GLN   A 1 161 ? 20.98400 4.51700   25.46900 1.000 30.16961  ?  313 GLN   A NE2  1 
ATOM   1086 N  N    . VAL   A 1 162 ? 25.88400 7.32500   28.49700 1.000 33.14426  ?  314 VAL   A N    1 
ATOM   1087 C  CA   . VAL   A 1 162 ? 27.02900 8.20700   28.69800 1.000 34.17797  ?  314 VAL   A CA   1 
ATOM   1088 C  C    . VAL   A 1 162 ? 28.29000 7.58600   28.10800 1.000 31.95681  ?  314 VAL   A C    1 
ATOM   1089 O  O    . VAL   A 1 162 ? 29.06500 8.25400   27.41300 1.000 35.59148  ?  314 VAL   A O    1 
ATOM   1090 C  CB   . VAL   A 1 162 ? 27.20300 8.52600   30.19400 1.000 35.34752  ?  314 VAL   A CB   1 
ATOM   1091 C  CG1  . VAL   A 1 162 ? 28.52200 9.23900   30.44000 1.000 33.98154  ?  314 VAL   A CG1  1 
ATOM   1092 C  CG2  . VAL   A 1 162 ? 26.03700 9.36100   30.69200 1.000 32.87819  ?  314 VAL   A CG2  1 
ATOM   1093 N  N    . GLY   A 1 163 ? 28.50800 6.29400   28.37000 1.000 37.70912  ?  315 GLY   A N    1 
ATOM   1094 C  CA   . GLY   A 1 163 ? 29.69800 5.63400   27.85400 1.000 32.47241  ?  315 GLY   A CA   1 
ATOM   1095 C  C    . GLY   A 1 163 ? 29.70600 5.53700   26.34100 1.000 36.81668  ?  315 GLY   A C    1 
ATOM   1096 O  O    . GLY   A 1 163 ? 30.75700 5.66700   25.70700 1.000 33.06548  ?  315 GLY   A O    1 
ATOM   1097 N  N    . LEU   A 1 164 ? 28.53600 5.30300   25.74100 1.000 29.45326  ?  316 LEU   A N    1 
ATOM   1098 C  CA   . LEU   A 1 164 ? 28.44300 5.28200   24.28700 1.000 34.80153  ?  316 LEU   A CA   1 
ATOM   1099 C  C    . LEU   A 1 164 ? 28.70200 6.66500   23.70600 1.000 37.79987  ?  316 LEU   A C    1 
ATOM   1100 O  O    . LEU   A 1 164 ? 29.42300 6.80100   22.71000 1.000 33.67217  ?  316 LEU   A O    1 
ATOM   1101 C  CB   . LEU   A 1 164 ? 27.07100 4.75900   23.85800 1.000 31.31193  ?  316 LEU   A CB   1 
ATOM   1102 C  CG   . LEU   A 1 164 ? 26.84200 4.62900   22.35200 1.000 34.96955  ?  316 LEU   A CG   1 
ATOM   1103 C  CD1  . LEU   A 1 164 ? 27.88800 3.72100   21.72900 1.000 36.06444  ?  316 LEU   A CD1  1 
ATOM   1104 C  CD2  . LEU   A 1 164 ? 25.44300 4.10600   22.06300 1.000 35.49224  ?  316 LEU   A CD2  1 
ATOM   1105 N  N    . LYS   A 1 165 ? 28.12800 7.70500   24.31900 1.000 31.58255  ?  317 LYS   A N    1 
ATOM   1106 C  CA   . LYS   A 1 165 ? 28.38800 9.06800   23.86600 1.000 37.21355  ?  317 LYS   A CA   1 
ATOM   1107 C  C    . LYS   A 1 165 ? 29.86700 9.41900   23.98100 1.000 41.54375  ?  317 LYS   A C    1 
ATOM   1108 O  O    . LYS   A 1 165 ? 30.42800 10.07300  23.09400 1.000 42.40593  ?  317 LYS   A O    1 
ATOM   1109 C  CB   . LYS   A 1 165 ? 27.54200 10.05800  24.66600 1.000 40.61018  ?  317 LYS   A CB   1 
ATOM   1110 C  CG   . LYS   A 1 165 ? 27.34000 11.39200  23.97400 1.000 47.37828  ?  317 LYS   A CG   1 
ATOM   1111 C  CD   . LYS   A 1 165 ? 26.56300 11.21800  22.68300 1.000 49.67531  ?  317 LYS   A CD   1 
ATOM   1112 C  CE   . LYS   A 1 165 ? 25.30700 12.05900  22.69600 1.000 49.77394  ?  317 LYS   A CE   1 
ATOM   1113 N  NZ   . LYS   A 1 165 ? 24.46400 11.84000  21.48900 1.000 49.45235  ?  317 LYS   A NZ   1 
ATOM   1114 N  N    . LYS   A 1 166 ? 30.51600 8.98300   25.06300 1.000 36.20753  ?  318 LYS   A N    1 
ATOM   1115 C  CA   . LYS   A 1 166 ? 31.93300 9.27600   25.25600 1.000 34.99203  ?  318 LYS   A CA   1 
ATOM   1116 C  C    . LYS   A 1 166 ? 32.80300 8.64100   24.18100 1.000 43.93859  ?  318 LYS   A C    1 
ATOM   1117 O  O    . LYS   A 1 166 ? 33.92900 9.09800   23.96100 1.000 43.46011  ?  318 LYS   A O    1 
ATOM   1118 C  CB   . LYS   A 1 166 ? 32.38700 8.80100   26.63700 1.000 34.56560  ?  318 LYS   A CB   1 
ATOM   1119 C  CG   . LYS   A 1 166 ? 32.02600 9.74200   27.77500 1.000 45.94117  ?  318 LYS   A CG   1 
ATOM   1120 C  CD   . LYS   A 1 166 ? 32.30700 9.10000   29.12600 1.000 49.97889  ?  318 LYS   A CD   1 
ATOM   1121 C  CE   . LYS   A 1 166 ? 32.33500 10.13500  30.24000 1.000 55.71999  ?  318 LYS   A CE   1 
ATOM   1122 N  NZ   . LYS   A 1 166 ? 32.54200 9.50600   31.57400 1.000 55.61078  ?  318 LYS   A NZ   1 
ATOM   1123 N  N    . LEU   A 1 167 ? 32.31000 7.59900   23.50800 1.000 47.65076  ?  319 LEU   A N    1 
ATOM   1124 C  CA   . LEU   A 1 167 ? 33.07200 6.99100   22.42600 1.000 49.12539  ?  319 LEU   A CA   1 
ATOM   1125 C  C    . LEU   A 1 167 ? 33.18100 7.90600   21.21500 1.000 46.67174  ?  319 LEU   A C    1 
ATOM   1126 O  O    . LEU   A 1 167 ? 34.10000 7.73200   20.40900 1.000 45.50610  ?  319 LEU   A O    1 
ATOM   1127 C  CB   . LEU   A 1 167 ? 32.44000 5.66000   22.01700 1.000 40.85928  ?  319 LEU   A CB   1 
ATOM   1128 C  CG   . LEU   A 1 167 ? 32.51700 4.53600   23.05400 1.000 38.82403  ?  319 LEU   A CG   1 
ATOM   1129 C  CD1  . LEU   A 1 167 ? 32.04700 3.22000   22.45600 1.000 44.22580  ?  319 LEU   A CD1  1 
ATOM   1130 C  CD2  . LEU   A 1 167 ? 33.92600 4.40500   23.61700 1.000 34.95264  ?  319 LEU   A CD2  1 
ATOM   1131 N  N    . ASN   A 1 168 ? 32.27100 8.87300   21.07600 1.000 42.78553  ?  320 ASN   A N    1 
ATOM   1132 C  CA   . ASN   A 1 168 ? 32.28900 9.82800   19.96800 1.000 50.89369  ?  320 ASN   A CA   1 
ATOM   1133 C  C    . ASN   A 1 168 ? 32.38700 9.10500   18.62800 1.000 50.71493  ?  320 ASN   A C    1 
ATOM   1134 O  O    . ASN   A 1 168 ? 33.27500 9.36300   17.81200 1.000 47.98760  ?  320 ASN   A O    1 
ATOM   1135 C  CB   . ASN   A 1 168 ? 33.42500 10.83900  20.13500 1.000 57.84385  ?  320 ASN   A CB   1 
ATOM   1136 C  CG   . ASN   A 1 168 ? 33.48600 11.42200  21.53500 1.000 70.78775  ?  320 ASN   A CG   1 
ATOM   1137 O  OD1  . ASN   A 1 168 ? 32.55500 12.09400  21.98200 1.000 80.73502  ?  320 ASN   A OD1  1 
ATOM   1138 N  ND2  . ASN   A 1 168 ? 34.58800 11.17400  22.23300 1.000 71.33334  ?  320 ASN   A ND2  1 
ATOM   1139 N  N    . LEU   A 1 169 ? 31.46400 8.17200   18.41500 1.000 38.71337  ?  321 LEU   A N    1 
ATOM   1140 C  CA   . LEU   A 1 169 ? 31.50300 7.33600   17.22500 1.000 35.71304  ?  321 LEU   A CA   1 
ATOM   1141 C  C    . LEU   A 1 169 ? 31.25900 8.16400   15.97100 1.000 40.48859  ?  321 LEU   A C    1 
ATOM   1142 O  O    . LEU   A 1 169 ? 30.45000 9.09500   15.96900 1.000 38.36914  ?  321 LEU   A O    1 
ATOM   1143 C  CB   . LEU   A 1 169 ? 30.45300 6.22600   17.32100 1.000 38.76449  ?  321 LEU   A CB   1 
ATOM   1144 C  CG   . LEU   A 1 169 ? 30.63200 5.15600   18.39800 1.000 38.10131  ?  321 LEU   A CG   1 
ATOM   1145 C  CD1  . LEU   A 1 169 ? 29.62300 4.02900   18.20600 1.000 38.95437  ?  321 LEU   A CD1  1 
ATOM   1146 C  CD2  . LEU   A 1 169 ? 32.05400 4.61000   18.39200 1.000 31.48364  ?  321 LEU   A CD2  1 
ATOM   1147 N  N    . HIS   A 1 170 ? 31.98300 7.83200   14.90500 1.000 37.68125  ?  322 HIS   A N    1 
ATOM   1148 C  CA   . HIS   A 1 170 ? 31.57700 8.27400   13.58100 1.000 33.25064  ?  322 HIS   A CA   1 
ATOM   1149 C  C    . HIS   A 1 170 ? 30.22600 7.65500   13.24500 1.000 32.88227  ?  322 HIS   A C    1 
ATOM   1150 O  O    . HIS   A 1 170 ? 29.88400 6.57100   13.72700 1.000 36.31318  ?  322 HIS   A O    1 
ATOM   1151 C  CB   . HIS   A 1 170 ? 32.60900 7.86400   12.52900 1.000 32.72993  ?  322 HIS   A CB   1 
ATOM   1152 C  CG   . HIS   A 1 170 ? 33.97500 8.44100   12.75100 1.000 38.29918  ?  322 HIS   A CG   1 
ATOM   1153 N  ND1  . HIS   A 1 170 ? 35.00200 8.28100   11.84600 1.000 42.30023  ?  322 HIS   A ND1  1 
ATOM   1154 C  CD2  . HIS   A 1 170 ? 34.48300 9.17400   13.77000 1.000 40.16822  ?  322 HIS   A CD2  1 
ATOM   1155 C  CE1  . HIS   A 1 170 ? 36.08300 8.89000   12.29600 1.000 40.46519  ?  322 HIS   A CE1  1 
ATOM   1156 N  NE2  . HIS   A 1 170 ? 35.79600 9.44000   13.46300 1.000 42.59220  ?  322 HIS   A NE2  1 
ATOM   1157 N  N    . GLU   A 1 171 ? 29.44800 8.35300   12.41400 1.000 33.00028  ?  323 GLU   A N    1 
ATOM   1158 C  CA   . GLU   A 1 171 ? 28.18000 7.78100   11.97300 1.000 37.08353  ?  323 GLU   A CA   1 
ATOM   1159 C  C    . GLU   A 1 171 ? 28.39500 6.44400   11.27700 1.000 36.97759  ?  323 GLU   A C    1 
ATOM   1160 O  O    . GLU   A 1 171 ? 27.55400 5.54400   11.38600 1.000 38.92241  ?  323 GLU   A O    1 
ATOM   1161 C  CB   . GLU   A 1 171 ? 27.44200 8.75200   11.05000 1.000 45.60196  ?  323 GLU   A CB   1 
ATOM   1162 C  CG   . GLU   A 1 171 ? 25.99600 8.34900   10.77800 1.000 56.65820  ?  323 GLU   A CG   1 
ATOM   1163 C  CD   . GLU   A 1 171 ? 25.21500 9.41900   10.03900 1.000 65.50621  ?  323 GLU   A CD   1 
ATOM   1164 O  OE1  . GLU   A 1 171 ? 25.83500 10.19900  9.28400  1.000 71.80943  ?  323 GLU   A OE1  1 
ATOM   1165 O  OE2  . GLU   A 1 171 ? 23.97900 9.47900   10.21200 1.000 67.34878  ?  323 GLU   A OE2  1 
ATOM   1166 N  N    . GLU   A 1 172 ? 29.51900 6.29400   10.57000 1.000 32.31808  ?  324 GLU   A N    1 
ATOM   1167 C  CA   . GLU   A 1 172 ? 29.85600 5.00900   9.96500  1.000 36.86414  ?  324 GLU   A CA   1 
ATOM   1168 C  C    . GLU   A 1 172 ? 29.96900 3.91400   11.02000 1.000 39.59909  ?  324 GLU   A C    1 
ATOM   1169 O  O    . GLU   A 1 172 ? 29.48900 2.79300   10.81700 1.000 37.22988  ?  324 GLU   A O    1 
ATOM   1170 C  CB   . GLU   A 1 172 ? 31.16300 5.12600   9.17900  1.000 34.71018  ?  324 GLU   A CB   1 
ATOM   1171 C  CG   . GLU   A 1 172 ? 31.09100 6.03500   7.95900  1.000 38.78522  ?  324 GLU   A CG   1 
ATOM   1172 C  CD   . GLU   A 1 172 ? 31.28200 7.50200   8.29500  1.000 48.60711  ?  324 GLU   A CD   1 
ATOM   1173 O  OE1  . GLU   A 1 172 ? 31.49600 8.30000   7.35900  1.000 51.41593  ?  324 GLU   A OE1  1 
ATOM   1174 O  OE2  . GLU   A 1 172 ? 31.21800 7.85800   9.49000  1.000 45.87247  ?  324 GLU   A OE2  1 
ATOM   1175 N  N    . GLU   A 1 173 ? 30.60000 4.22300   12.15700 1.000 32.76944  ?  325 GLU   A N    1 
ATOM   1176 C  CA   . GLU   A 1 173 ? 30.72200 3.23700   13.22500 1.000 31.97648  ?  325 GLU   A CA   1 
ATOM   1177 C  C    . GLU   A 1 173 ? 29.39300 3.01100   13.93400 1.000 24.57641  ?  325 GLU   A C    1 
ATOM   1178 O  O    . GLU   A 1 173 ? 29.11000 1.89100   14.37500 1.000 30.37644  ?  325 GLU   A O    1 
ATOM   1179 C  CB   . GLU   A 1 173 ? 31.79600 3.67400   14.22600 1.000 26.90074  ?  325 GLU   A CB   1 
ATOM   1180 C  CG   . GLU   A 1 173 ? 33.20700 3.68300   13.64500 1.000 26.71788  ?  325 GLU   A CG   1 
ATOM   1181 C  CD   . GLU   A 1 173 ? 34.10900 4.73400   14.26900 1.000 45.21899  ?  325 GLU   A CD   1 
ATOM   1182 O  OE1  . GLU   A 1 173 ? 35.32600 4.71500   13.97900 1.000 43.06698  ?  325 GLU   A OE1  1 
ATOM   1183 O  OE2  . GLU   A 1 173 ? 33.61200 5.57600   15.04700 1.000 37.71796  ?  325 GLU   A OE2  1 
ATOM   1184 N  N    . HIS   A 1 174 ? 28.57100 4.05600   14.05000 1.000 28.81075  ?  326 HIS   A N    1 
ATOM   1185 C  CA   . HIS   A 1 174 ? 27.28100 3.92700   14.71900 1.000 38.13756  ?  326 HIS   A CA   1 
ATOM   1186 C  C    . HIS   A 1 174 ? 26.36600 2.95900   13.97500 1.000 41.31573  ?  326 HIS   A C    1 
ATOM   1187 O  O    . HIS   A 1 174 ? 25.75100 2.07400   14.58400 1.000 34.49239  ?  326 HIS   A O    1 
ATOM   1188 C  CB   . HIS   A 1 174 ? 26.62900 5.30500   14.84800 1.000 41.18949  ?  326 HIS   A CB   1 
ATOM   1189 C  CG   . HIS   A 1 174 ? 25.30600 5.29100   15.54800 1.000 43.11783  ?  326 HIS   A CG   1 
ATOM   1190 N  ND1  . HIS   A 1 174 ? 25.18600 5.13400   16.91200 1.000 42.70631  ?  326 HIS   A ND1  1 
ATOM   1191 C  CD2  . HIS   A 1 174 ? 24.04500 5.42500   15.07300 1.000 41.71849  ?  326 HIS   A CD2  1 
ATOM   1192 C  CE1  . HIS   A 1 174 ? 23.90800 5.16700   17.24600 1.000 43.35335  ?  326 HIS   A CE1  1 
ATOM   1193 N  NE2  . HIS   A 1 174 ? 23.19400 5.34300   16.14900 1.000 43.66724  ?  326 HIS   A NE2  1 
ATOM   1194 N  N    . VAL   A 1 175 ? 26.26400 3.10700   12.65100 1.000 32.34127  ?  327 VAL   A N    1 
ATOM   1195 C  CA   . VAL   A 1 175 ? 25.36100 2.24200   11.89700 1.000 29.81332  ?  327 VAL   A CA   1 
ATOM   1196 C  C    . VAL   A 1 175 ? 25.92900 0.83300   11.78000 1.000 32.85691  ?  327 VAL   A C    1 
ATOM   1197 O  O    . VAL   A 1 175 ? 25.17100 -0.14300  11.71800 1.000 27.88098  ?  327 VAL   A O    1 
ATOM   1198 C  CB   . VAL   A 1 175 ? 25.05100 2.85600   10.51700 1.000 33.28005  ?  327 VAL   A CB   1 
ATOM   1199 C  CG1  . VAL   A 1 175 ? 24.46600 4.24900   10.68800 1.000 29.20045  ?  327 VAL   A CG1  1 
ATOM   1200 C  CG2  . VAL   A 1 175 ? 26.29900 2.90600   9.64300  1.000 31.17941  ?  327 VAL   A CG2  1 
ATOM   1201 N  N    . LEU   A 1 176 ? 27.25800 0.69500   11.76500 1.000 26.57315  ?  328 LEU   A N    1 
ATOM   1202 C  CA   . LEU   A 1 176 ? 27.85900 -0.63500  11.76600 1.000 28.55962  ?  328 LEU   A CA   1 
ATOM   1203 C  C    . LEU   A 1 176 ? 27.57500 -1.36400  13.07300 1.000 29.35563  ?  328 LEU   A C    1 
ATOM   1204 O  O    . LEU   A 1 176 ? 27.32400 -2.57400  13.07300 1.000 31.43144  ?  328 LEU   A O    1 
ATOM   1205 C  CB   . LEU   A 1 176 ? 29.36700 -0.53200  11.52900 1.000 27.40283  ?  328 LEU   A CB   1 
ATOM   1206 C  CG   . LEU   A 1 176 ? 29.82500 -0.39500  10.07600 1.000 36.18596  ?  328 LEU   A CG   1 
ATOM   1207 C  CD1  . LEU   A 1 176 ? 31.26400 0.09900   10.00900 1.000 38.56194  ?  328 LEU   A CD1  1 
ATOM   1208 C  CD2  . LEU   A 1 176 ? 29.66900 -1.71300  9.32800  1.000 27.48082  ?  328 LEU   A CD2  1 
ATOM   1209 N  N    . LEU   A 1 177 ? 27.60600 -0.64300  14.19600 1.000 25.48650  ?  329 LEU   A N    1 
ATOM   1210 C  CA   . LEU   A 1 177 ? 27.35400 -1.27200  15.48800 1.000 25.18102  ?  329 LEU   A CA   1 
ATOM   1211 C  C    . LEU   A 1 177 ? 25.90800 -1.73700  15.60300 1.000 25.77321  ?  329 LEU   A C    1 
ATOM   1212 O  O    . LEU   A 1 177 ? 25.63600 -2.80100  16.17300 1.000 28.07455  ?  329 LEU   A O    1 
ATOM   1213 C  CB   . LEU   A 1 177 ? 27.70100 -0.30300  16.61800 1.000 26.40631  ?  329 LEU   A CB   1 
ATOM   1214 C  CG   . LEU   A 1 177 ? 27.70000 -0.86600  18.04200 1.000 33.94710  ?  329 LEU   A CG   1 
ATOM   1215 C  CD1  . LEU   A 1 177 ? 28.59300 -2.09500  18.14500 1.000 23.51647  ?  329 LEU   A CD1  1 
ATOM   1216 C  CD2  . LEU   A 1 177 ? 28.12600 0.20300   19.03800 1.000 29.73599  ?  329 LEU   A CD2  1 
ATOM   1217 N  N    . MET   A 1 178 ? 24.96700 -0.95500  15.06900 1.000 27.63112  ?  330 MET   A N    1 
ATOM   1218 C  CA   . MET   A 1 178 ? 23.57000 -1.37500  15.08100 1.000 31.76898  ?  330 MET   A CA   1 
ATOM   1219 C  C    . MET   A 1 178 ? 23.36500 -2.63000  14.24100 1.000 25.88502  ?  330 MET   A C    1 
ATOM   1220 O  O    . MET   A 1 178 ? 22.63400 -3.54200  14.64400 1.000 30.57055  ?  330 MET   A O    1 
ATOM   1221 C  CB   . MET   A 1 178 ? 22.67300 -0.24100  14.58300 1.000 27.07579  ?  330 MET   A CB   1 
ATOM   1222 C  CG   . MET   A 1 178 ? 22.57000 0.93300   15.54300 1.000 29.48691  ?  330 MET   A CG   1 
ATOM   1223 S  SD   . MET   A 1 178 ? 21.31300 2.12800   15.04800 1.000 39.85049  ?  330 MET   A SD   1 
ATOM   1224 C  CE   . MET   A 1 178 ? 22.10200 2.87900   13.62700 1.000 34.44076  ?  330 MET   A CE   1 
ATOM   1225 N  N    . ALA   A 1 179 ? 24.01100 -2.70100  13.07500 1.000 27.13710  ?  331 ALA   A N    1 
ATOM   1226 C  CA   . ALA   A 1 179 ? 23.86300 -3.87600  12.22000 1.000 23.85872  ?  331 ALA   A CA   1 
ATOM   1227 C  C    . ALA   A 1 179 ? 24.51000 -5.10400  12.85100 1.000 36.62815  ?  331 ALA   A C    1 
ATOM   1228 O  O    . ALA   A 1 179 ? 23.93900 -6.20100  12.82100 1.000 30.94328  ?  331 ALA   A O    1 
ATOM   1229 C  CB   . ALA   A 1 179 ? 24.45600 -3.60100  10.83800 1.000 26.66798  ?  331 ALA   A CB   1 
ATOM   1230 N  N    . ILE   A 1 180 ? 25.70500 -4.94100  13.42800 1.000 28.50748  ?  332 ILE   A N    1 
ATOM   1231 C  CA   . ILE   A 1 180 ? 26.37200 -6.06200  14.08500 1.000 28.11620  ?  332 ILE   A CA   1 
ATOM   1232 C  C    . ILE   A 1 180 ? 25.52900 -6.57600  15.24800 1.000 28.41000  ?  332 ILE   A C    1 
ATOM   1233 O  O    . ILE   A 1 180 ? 25.40000 -7.78800  15.45400 1.000 30.09255  ?  332 ILE   A O    1 
ATOM   1234 C  CB   . ILE   A 1 180 ? 27.78400 -5.64500  14.54100 1.000 28.88662  ?  332 ILE   A CB   1 
ATOM   1235 C  CG1  . ILE   A 1 180 ? 28.68600 -5.40500  13.32800 1.000 34.76584  ?  332 ILE   A CG1  1 
ATOM   1236 C  CG2  . ILE   A 1 180 ? 28.38100 -6.70000  15.45100 1.000 34.73797  ?  332 ILE   A CG2  1 
ATOM   1237 C  CD1  . ILE   A 1 180 ? 29.97100 -4.66400  13.65700 1.000 32.38487  ?  332 ILE   A CD1  1 
ATOM   1238 N  N    . CYS   A 1 181 ? 24.94700 -5.66200  16.02600 1.000 26.85379  ?  333 CYS   A N    1 
ATOM   1239 C  CA   . CYS   A 1 181 ? 24.02700 -6.03700  17.10000 1.000 35.75833  ?  333 CYS   A CA   1 
ATOM   1240 C  C    . CYS   A 1 181 ? 22.92200 -6.97200  16.61500 1.000 36.97174  ?  333 CYS   A C    1 
ATOM   1241 O  O    . CYS   A 1 181 ? 22.65800 -8.01600  17.22500 1.000 29.53176  ?  333 CYS   A O    1 
ATOM   1242 C  CB   . CYS   A 1 181 ? 23.41700 -4.77600  17.71200 1.000 33.03732  ?  333 CYS   A CB   1 
ATOM   1243 S  SG   . CYS   A 1 181 ? 22.31300 -5.04900  19.12100 1.000 33.07274  ?  333 CYS   A SG   1 
ATOM   1244 N  N    . ILE   A 1 182 ? 22.27300 -6.61300  15.50700 1.000 32.49610  ?  334 ILE   A N    1 
ATOM   1245 C  CA   . ILE   A 1 182 ? 21.11700 -7.37000  15.03300 1.000 32.35763  ?  334 ILE   A CA   1 
ATOM   1246 C  C    . ILE   A 1 182 ? 21.52800 -8.78000  14.62500 1.000 36.98936  ?  334 ILE   A C    1 
ATOM   1247 O  O    . ILE   A 1 182 ? 20.90000 -9.77300  15.01500 1.000 36.15114  ?  334 ILE   A O    1 
ATOM   1248 C  CB   . ILE   A 1 182 ? 20.44000 -6.62000  13.87200 1.000 36.42180  ?  334 ILE   A CB   1 
ATOM   1249 C  CG1  . ILE   A 1 182 ? 19.76600 -5.34600  14.37800 1.000 30.70535  ?  334 ILE   A CG1  1 
ATOM   1250 C  CG2  . ILE   A 1 182 ? 19.44600 -7.51400  13.16000 1.000 35.23183  ?  334 ILE   A CG2  1 
ATOM   1251 C  CD1  . ILE   A 1 182 ? 19.59500 -4.26700  13.32000 1.000 38.27444  ?  334 ILE   A CD1  1 
ATOM   1252 N  N    . VAL   A 1 183 ? 22.60000 -8.88600  13.84500 1.000 32.97724  ?  335 VAL   A N    1 
ATOM   1253 C  CA   . VAL   A 1 183 ? 23.03300 -10.15600 13.28100 1.000 36.86775  ?  335 VAL   A CA   1 
ATOM   1254 C  C    . VAL   A 1 183 ? 24.04300 -10.78300 14.23600 1.000 36.93503  ?  335 VAL   A C    1 
ATOM   1255 O  O    . VAL   A 1 183 ? 25.25100 -10.76000 13.98700 1.000 44.10064  ?  335 VAL   A O    1 
ATOM   1256 C  CB   . VAL   A 1 183 ? 23.61500 -9.94300  11.86800 1.000 52.34814  ?  335 VAL   A CB   1 
ATOM   1257 C  CG1  . VAL   A 1 183 ? 24.09500 -11.25200 11.25200 1.000 61.25119  ?  335 VAL   A CG1  1 
ATOM   1258 C  CG2  . VAL   A 1 183 ? 22.58600 -9.24800  10.97300 1.000 40.04054  ?  335 VAL   A CG2  1 
ATOM   1259 N  N    . SER   A 1 184 ? 23.55700 -11.31600 15.35600 1.000 36.67398  ?  336 SER   A N    1 
ATOM   1260 C  CA   . SER   A 1 184 ? 24.40300 -12.03300 16.30300 1.000 38.93984  ?  336 SER   A CA   1 
ATOM   1261 C  C    . SER   A 1 184 ? 23.97600 -13.49100 16.35300 1.000 40.35770  ?  336 SER   A C    1 
ATOM   1262 O  O    . SER   A 1 184 ? 22.79200 -13.77600 16.59200 1.000 42.87429  ?  336 SER   A O    1 
ATOM   1263 C  CB   . SER   A 1 184 ? 24.33800 -11.40400 17.69600 1.000 37.14768  ?  336 SER   A CB   1 
ATOM   1264 O  OG   . SER   A 1 184 ? 24.37700 -9.98600  17.62500 1.000 47.55788  ?  336 SER   A OG   1 
ATOM   1265 N  N    . PRO   A 1 185 ? 24.89000 -14.44000 16.12800 1.000 33.32030  ?  337 PRO   A N    1 
ATOM   1266 C  CA   . PRO   A 1 185 ? 24.47300 -15.84800 16.00600 1.000 37.18124  ?  337 PRO   A CA   1 
ATOM   1267 C  C    . PRO   A 1 185 ? 24.07700 -16.49900 17.32000 1.000 46.51664  ?  337 PRO   A C    1 
ATOM   1268 O  O    . PRO   A 1 185 ? 23.51400 -17.60200 17.29100 1.000 55.12797  ?  337 PRO   A O    1 
ATOM   1269 C  CB   . PRO   A 1 185 ? 25.70800 -16.53200 15.40000 1.000 43.42550  ?  337 PRO   A CB   1 
ATOM   1270 C  CG   . PRO   A 1 185 ? 26.85300 -15.66300 15.78900 1.000 41.99533  ?  337 PRO   A CG   1 
ATOM   1271 C  CD   . PRO   A 1 185 ? 26.32300 -14.25300 15.84100 1.000 34.44977  ?  337 PRO   A CD   1 
ATOM   1272 N  N    . ASP   A 1 186 ? 24.33600 -15.86500 18.46100 1.000 51.70161  ?  338 ASP   A N    1 
ATOM   1273 C  CA   . ASP   A 1 186 ? 24.03700 -16.45300 19.75900 1.000 46.68991  ?  338 ASP   A CA   1 
ATOM   1274 C  C    . ASP   A 1 186 ? 22.69000 -16.01100 20.31600 1.000 48.63417  ?  338 ASP   A C    1 
ATOM   1275 O  O    . ASP   A 1 186 ? 22.41100 -16.25000 21.49600 1.000 46.91375  ?  338 ASP   A O    1 
ATOM   1276 C  CB   . ASP   A 1 186 ? 25.14700 -16.12100 20.75800 1.000 37.19047  ?  338 ASP   A CB   1 
ATOM   1277 C  CG   . ASP   A 1 186 ? 25.32300 -14.63200 20.95800 1.000 45.84624  ?  338 ASP   A CG   1 
ATOM   1278 O  OD1  . ASP   A 1 186 ? 25.67900 -14.22300 22.08300 1.000 57.10155  ?  338 ASP   A OD1  1 
ATOM   1279 O  OD2  . ASP   A 1 186 ? 25.10900 -13.86900 19.99300 1.000 48.23645  ?  338 ASP   A OD2  1 
ATOM   1280 N  N    . ARG   A 1 187 ? 21.85300 -15.37400 19.50400 1.000 46.62743  ?  339 ARG   A N    1 
ATOM   1281 C  CA   . ARG   A 1 187 ? 20.52000 -15.01300 19.96200 1.000 43.08237  ?  339 ARG   A CA   1 
ATOM   1282 C  C    . ARG   A 1 187 ? 19.67700 -16.27500 20.14100 1.000 47.74054  ?  339 ARG   A C    1 
ATOM   1283 O  O    . ARG   A 1 187 ? 19.81900 -17.23100 19.37200 1.000 44.15742  ?  339 ARG   A O    1 
ATOM   1284 C  CB   . ARG   A 1 187 ? 19.84600 -14.06300 18.97000 1.000 40.47737  ?  339 ARG   A CB   1 
ATOM   1285 C  CG   . ARG   A 1 187 ? 20.67000 -12.82600 18.61900 1.000 35.74370  ?  339 ARG   A CG   1 
ATOM   1286 C  CD   . ARG   A 1 187 ? 20.45200 -11.71900 19.62600 1.000 33.21478  ?  339 ARG   A CD   1 
ATOM   1287 N  NE   . ARG   A 1 187 ? 20.98200 -10.42700 19.20200 1.000 33.19863  ?  339 ARG   A NE   1 
ATOM   1288 C  CZ   . ARG   A 1 187 ? 21.05300 -9.37100  20.00600 1.000 37.82596  ?  339 ARG   A CZ   1 
ATOM   1289 N  NH1  . ARG   A 1 187 ? 20.62900 -9.47300  21.25800 1.000 36.57125  ?  339 ARG   A NH1  1 
ATOM   1290 N  NH2  . ARG   A 1 187 ? 21.54900 -8.22000  19.57200 1.000 35.52699  ?  339 ARG   A NH2  1 
ATOM   1291 N  N    . PRO   A 1 188 ? 18.80400 -16.31600 21.14700 1.000 59.85219  ?  340 PRO   A N    1 
ATOM   1292 C  CA   . PRO   A 1 188 ? 18.01000 -17.53000 21.37400 1.000 56.68683  ?  340 PRO   A CA   1 
ATOM   1293 C  C    . PRO   A 1 188 ? 17.04200 -17.78400 20.23000 1.000 49.16312  ?  340 PRO   A C    1 
ATOM   1294 O  O    . PRO   A 1 188 ? 16.41200 -16.86300 19.70500 1.000 49.50434  ?  340 PRO   A O    1 
ATOM   1295 C  CB   . PRO   A 1 188 ? 17.26800 -17.23300 22.68300 1.000 66.41251  ?  340 PRO   A CB   1 
ATOM   1296 C  CG   . PRO   A 1 188 ? 17.23200 -15.74400 22.76500 1.000 66.93844  ?  340 PRO   A CG   1 
ATOM   1297 C  CD   . PRO   A 1 188 ? 18.51100 -15.26900 22.14000 1.000 59.73298  ?  340 PRO   A CD   1 
ATOM   1298 N  N    . GLY   A 1 189 ? 16.93100 -19.05400 19.84400 1.000 50.83846  ?  341 GLY   A N    1 
ATOM   1299 C  CA   . GLY   A 1 189 ? 16.05100 -19.45200 18.76800 1.000 54.22858  ?  341 GLY   A CA   1 
ATOM   1300 C  C    . GLY   A 1 189 ? 16.64400 -19.35600 17.38000 1.000 52.01918  ?  341 GLY   A C    1 
ATOM   1301 O  O    . GLY   A 1 189 ? 15.94800 -19.67100 16.40600 1.000 51.65782  ?  341 GLY   A O    1 
ATOM   1302 N  N    . VAL   A 1 190 ? 17.90100 -18.93000 17.25300 1.000 49.32940  ?  342 VAL   A N    1 
ATOM   1303 C  CA   . VAL   A 1 190 ? 18.53600 -18.84600 15.94300 1.000 49.10605  ?  342 VAL   A CA   1 
ATOM   1304 C  C    . VAL   A 1 190 ? 18.75900 -20.25000 15.40000 1.000 53.45958  ?  342 VAL   A C    1 
ATOM   1305 O  O    . VAL   A 1 190 ? 19.28400 -21.12800 16.09600 1.000 56.53644  ?  342 VAL   A O    1 
ATOM   1306 C  CB   . VAL   A 1 190 ? 19.85500 -18.06400 16.03300 1.000 50.10953  ?  342 VAL   A CB   1 
ATOM   1307 C  CG1  . VAL   A 1 190 ? 20.70900 -18.30800 14.79400 1.000 55.89439  ?  342 VAL   A CG1  1 
ATOM   1308 C  CG2  . VAL   A 1 190 ? 19.58200 -16.57800 16.20500 1.000 46.03523  ?  342 VAL   A CG2  1 
ATOM   1309 N  N    . GLN   A 1 191 ? 18.35100 -20.47000 14.15000 1.000 48.45168  ?  343 GLN   A N    1 
ATOM   1310 C  CA   . GLN   A 1 191 ? 18.51700 -21.76300 13.49300 1.000 52.98546  ?  343 GLN   A CA   1 
ATOM   1311 C  C    . GLN   A 1 191 ? 19.85300 -21.85100 12.75900 1.000 54.69271  ?  343 GLN   A C    1 
ATOM   1312 O  O    . GLN   A 1 191 ? 20.70800 -22.67300 13.10400 1.000 60.45006  ?  343 GLN   A O    1 
ATOM   1313 C  CB   . GLN   A 1 191 ? 17.35700 -22.01200 12.52300 1.000 56.29539  ?  343 GLN   A CB   1 
ATOM   1314 C  CG   . GLN   A 1 191 ? 16.14300 -22.67100 13.15300 1.000 61.14365  ?  343 GLN   A CG   1 
ATOM   1315 C  CD   . GLN   A 1 191 ? 14.85400 -22.33000 12.42800 1.000 71.84866  ?  343 GLN   A CD   1 
ATOM   1316 O  OE1  . GLN   A 1 191 ? 14.85300 -22.08800 11.22000 1.000 63.90941  ?  343 GLN   A OE1  1 
ATOM   1317 N  NE2  . GLN   A 1 191 ? 13.74900 -22.30800 13.16400 1.000 72.49727  ?  343 GLN   A NE2  1 
ATOM   1318 N  N    . ASP   A 1 192 ? 20.04600 -21.00500 11.74700 1.000 55.61511  ?  344 ASP   A N    1 
ATOM   1319 C  CA   . ASP   A 1 192 ? 21.25100 -21.04700 10.91600 1.000 60.19620  ?  344 ASP   A CA   1 
ATOM   1320 C  C    . ASP   A 1 192 ? 22.30500 -20.10000 11.49100 1.000 54.70249  ?  344 ASP   A C    1 
ATOM   1321 O  O    . ASP   A 1 192 ? 22.58000 -19.01700 10.97200 1.000 57.42378  ?  344 ASP   A O    1 
ATOM   1322 C  CB   . ASP   A 1 192 ? 20.90700 -20.70300 9.47200  1.000 65.02767  ?  344 ASP   A CB   1 
ATOM   1323 C  CG   . ASP   A 1 192 ? 21.98600 -21.12700 8.49600  1.000 72.66203  ?  344 ASP   A CG   1 
ATOM   1324 O  OD1  . ASP   A 1 192 ? 21.76200 -21.00100 7.27300  1.000 70.80157  ?  344 ASP   A OD1  1 
ATOM   1325 O  OD2  . ASP   A 1 192 ? 23.05900 -21.58000 8.94800  1.000 72.13265  ?  344 ASP   A OD2  1 
ATOM   1326 N  N    . ALA   A 1 193 ? 22.91500 -20.55000 12.59200 1.000 55.00061  ?  345 ALA   A N    1 
ATOM   1327 C  CA   . ALA   A 1 193 ? 23.87200 -19.71000 13.30500 1.000 50.85749  ?  345 ALA   A CA   1 
ATOM   1328 C  C    . ALA   A 1 193 ? 25.11500 -19.42800 12.47000 1.000 48.73844  ?  345 ALA   A C    1 
ATOM   1329 O  O    . ALA   A 1 193 ? 25.70700 -18.34900 12.58500 1.000 44.34655  ?  345 ALA   A O    1 
ATOM   1330 C  CB   . ALA   A 1 193 ? 24.26400 -20.36400 14.63100 1.000 55.74724  ?  345 ALA   A CB   1 
ATOM   1331 N  N    . LYS   A 1 194 ? 25.52400 -20.37000 11.62200 1.000 53.25207  ?  346 LYS   A N    1 
ATOM   1332 C  CA   . LYS   A 1 194 ? 26.73300 -20.15300 10.83300 1.000 62.68296  ?  346 LYS   A CA   1 
ATOM   1333 C  C    . LYS   A 1 194 ? 26.49900 -19.13500 9.72000  1.000 53.61833  ?  346 LYS   A C    1 
ATOM   1334 O  O    . LYS   A 1 194 ? 27.40500 -18.36800 9.37600  1.000 49.26523  ?  346 LYS   A O    1 
ATOM   1335 C  CB   . LYS   A 1 194 ? 27.23600 -21.47900 10.26700 1.000 71.05972  ?  346 LYS   A CB   1 
ATOM   1336 C  CG   . LYS   A 1 194 ? 28.43700 -22.03800 11.02300 1.000 85.58546  ?  346 LYS   A CG   1 
ATOM   1337 C  CD   . LYS   A 1 194 ? 29.67200 -22.14000 10.14600 1.000 90.22551  ?  346 LYS   A CD   1 
ATOM   1338 C  CE   . LYS   A 1 194 ? 30.88100 -22.56800 10.95500 1.000 94.91712  ?  346 LYS   A CE   1 
ATOM   1339 N  NZ   . LYS   A 1 194 ? 32.06100 -22.84800 10.10500 1.000 94.90687  ?  346 LYS   A NZ   1 
ATOM   1340 N  N    . LEU   A 1 195 ? 25.29000 -19.09900 9.15600  1.000 55.73594  ?  347 LEU   A N    1 
ATOM   1341 C  CA   . LEU   A 1 195 ? 24.98400 -18.06800 8.17100  1.000 54.93140  ?  347 LEU   A CA   1 
ATOM   1342 C  C    . LEU   A 1 195 ? 24.86900 -16.70400 8.83600  1.000 51.28423  ?  347 LEU   A C    1 
ATOM   1343 O  O    . LEU   A 1 195 ? 25.33800 -15.70200 8.28700  1.000 51.58823  ?  347 LEU   A O    1 
ATOM   1344 C  CB   . LEU   A 1 195 ? 23.70100 -18.41300 7.41600  1.000 53.83455  ?  347 LEU   A CB   1 
ATOM   1345 C  CG   . LEU   A 1 195 ? 23.15300 -17.34700 6.46600  1.000 54.26742  ?  347 LEU   A CG   1 
ATOM   1346 C  CD1  . LEU   A 1 195 ? 24.20300 -16.94500 5.43800  1.000 53.36512  ?  347 LEU   A CD1  1 
ATOM   1347 C  CD2  . LEU   A 1 195 ? 21.88000 -17.82400 5.78000  1.000 45.99508  ?  347 LEU   A CD2  1 
ATOM   1348 N  N    . VAL   A 1 196 ? 24.24400 -16.64700 10.01400 1.000 48.14355  ?  348 VAL   A N    1 
ATOM   1349 C  CA   . VAL   A 1 196 ? 24.22100 -15.40600 10.78500 1.000 40.58448  ?  348 VAL   A CA   1 
ATOM   1350 C  C    . VAL   A 1 196 ? 25.64200 -14.97200 11.12800 1.000 37.60369  ?  348 VAL   A C    1 
ATOM   1351 O  O    . VAL   A 1 196 ? 25.98100 -13.78400 11.06100 1.000 44.40691  ?  348 VAL   A O    1 
ATOM   1352 C  CB   . VAL   A 1 196 ? 23.35700 -15.58300 12.04800 1.000 35.23845  ?  348 VAL   A CB   1 
ATOM   1353 C  CG1  . VAL   A 1 196 ? 23.37500 -14.32400 12.89500 1.000 36.75493  ?  348 VAL   A CG1  1 
ATOM   1354 C  CG2  . VAL   A 1 196 ? 21.93300 -15.95600 11.66600 1.000 34.98059  ?  348 VAL   A CG2  1 
ATOM   1355 N  N    . GLU   A 1 197 ? 26.50100 -15.93200 11.47800 1.000 36.80404  ?  349 GLU   A N    1 
ATOM   1356 C  CA   . GLU   A 1 197 ? 27.87900 -15.60100 11.82900 1.000 43.79198  ?  349 GLU   A CA   1 
ATOM   1357 C  C    . GLU   A 1 197 ? 28.64700 -15.06800 10.62400 1.000 43.04853  ?  349 GLU   A C    1 
ATOM   1358 O  O    . GLU   A 1 197 ? 29.46800 -14.15200 10.76000 1.000 42.34018  ?  349 GLU   A O    1 
ATOM   1359 C  CB   . GLU   A 1 197 ? 28.57800 -16.82900 12.41600 1.000 48.20082  ?  349 GLU   A CB   1 
ATOM   1360 C  CG   . GLU   A 1 197 ? 30.05700 -16.63000 12.70800 1.000 58.04552  ?  349 GLU   A CG   1 
ATOM   1361 C  CD   . GLU   A 1 197 ? 30.55100 -17.52000 13.83100 1.000 70.56509  ?  349 GLU   A CD   1 
ATOM   1362 O  OE1  . GLU   A 1 197 ? 30.26400 -18.73600 13.79500 1.000 74.05979  ?  349 GLU   A OE1  1 
ATOM   1363 O  OE2  . GLU   A 1 197 ? 31.22600 -17.00500 14.74800 1.000 76.12356  ?  349 GLU   A OE2  1 
ATOM   1364 N  N    . ALA   A 1 198 ? 28.39100 -15.62100 9.43500  1.000 46.41876  ?  350 ALA   A N    1 
ATOM   1365 C  CA   . ALA   A 1 198 ? 29.07800 -15.14700 8.23700  1.000 50.41401  ?  350 ALA   A CA   1 
ATOM   1366 C  C    . ALA   A 1 198 ? 28.69100 -13.71000 7.90800  1.000 47.26482  ?  350 ALA   A C    1 
ATOM   1367 O  O    . ALA   A 1 198 ? 29.55000 -12.89600 7.55000  1.000 46.12427  ?  350 ALA   A O    1 
ATOM   1368 C  CB   . ALA   A 1 198 ? 28.77500 -16.06800 7.05500  1.000 56.39749  ?  350 ALA   A CB   1 
ATOM   1369 N  N    . ILE   A 1 199 ? 27.40200 -13.37900 8.02500  1.000 43.77477  ?  351 ILE   A N    1 
ATOM   1370 C  CA   . ILE   A 1 199 ? 26.96000 -12.01100 7.76400  1.000 43.89226  ?  351 ILE   A CA   1 
ATOM   1371 C  C    . ILE   A 1 199 ? 27.57400 -11.05000 8.77400  1.000 39.97560  ?  351 ILE   A C    1 
ATOM   1372 O  O    . ILE   A 1 199 ? 28.04200 -9.96100  8.41500  1.000 41.15809  ?  351 ILE   A O    1 
ATOM   1373 C  CB   . ILE   A 1 199 ? 25.42300 -11.93500 7.77800  1.000 41.48739  ?  351 ILE   A CB   1 
ATOM   1374 C  CG1  . ILE   A 1 199 ? 24.83700 -12.81100 6.67200  1.000 47.38017  ?  351 ILE   A CG1  1 
ATOM   1375 C  CG2  . ILE   A 1 199 ? 24.96000 -10.48900 7.64000  1.000 37.86739  ?  351 ILE   A CG2  1 
ATOM   1376 C  CD1  . ILE   A 1 199 ? 23.37400 -13.14100 6.87600  1.000 44.87318  ?  351 ILE   A CD1  1 
ATOM   1377 N  N    . GLN   A 1 200 ? 27.58300 -11.43600 10.05300 1.000 41.25102  ?  352 GLN   A N    1 
ATOM   1378 C  CA   . GLN   A 1 200 ? 28.16900 -10.58400 11.08300 1.000 38.02503  ?  352 GLN   A CA   1 
ATOM   1379 C  C    . GLN   A 1 200 ? 29.66700 -10.41200 10.87800 1.000 41.89443  ?  352 GLN   A C    1 
ATOM   1380 O  O    . GLN   A 1 200 ? 30.21100 -9.32400  11.10000 1.000 42.55917  ?  352 GLN   A O    1 
ATOM   1381 C  CB   . GLN   A 1 200 ? 27.89500 -11.16700 12.46800 1.000 33.10216  ?  352 GLN   A CB   1 
ATOM   1382 C  CG   . GLN   A 1 200 ? 28.24300 -10.22200 13.61000 1.000 39.06900  ?  352 GLN   A CG   1 
ATOM   1383 C  CD   . GLN   A 1 200 ? 28.17200 -10.89500 14.96700 1.000 46.60261  ?  352 GLN   A CD   1 
ATOM   1384 O  OE1  . GLN   A 1 200 ? 28.84000 -11.90000 15.21000 1.000 50.06232  ?  352 GLN   A OE1  1 
ATOM   1385 N  NE2  . GLN   A 1 200 ? 27.35200 -10.34600 15.85600 1.000 43.32069  ?  352 GLN   A NE2  1 
ATOM   1386 N  N    . ASP   A 1 201 ? 30.35400 -11.48100 10.46500 1.000 41.57702  ?  353 ASP   A N    1 
ATOM   1387 C  CA   . ASP   A 1 201 ? 31.79800 -11.40100 10.27300 1.000 46.02675  ?  353 ASP   A CA   1 
ATOM   1388 C  C    . ASP   A 1 201 ? 32.15400 -10.40000 9.18200  1.000 47.27524  ?  353 ASP   A C    1 
ATOM   1389 O  O    . ASP   A 1 201 ? 33.14500 -9.66900  9.30100  1.000 50.63169  ?  353 ASP   A O    1 
ATOM   1390 C  CB   . ASP   A 1 201 ? 32.36000 -12.78400 9.94100  1.000 48.07694  ?  353 ASP   A CB   1 
ATOM   1391 C  CG   . ASP   A 1 201 ? 32.47000 -13.67600 11.16200 1.000 56.63917  ?  353 ASP   A CG   1 
ATOM   1392 O  OD1  . ASP   A 1 201 ? 32.21000 -13.19000 12.28300 1.000 57.44197  ?  353 ASP   A OD1  1 
ATOM   1393 O  OD2  . ASP   A 1 201 ? 32.81500 -14.86600 11.00100 1.000 64.18376  ?  353 ASP   A OD2  1 
ATOM   1394 N  N    . ARG   A 1 202 ? 31.35500 -10.34600 8.11300  1.000 45.91045  ?  354 ARG   A N    1 
ATOM   1395 C  CA   . ARG   A 1 202 ? 31.60300 -9.36500  7.06100  1.000 49.71914  ?  354 ARG   A CA   1 
ATOM   1396 C  C    . ARG   A 1 202 ? 31.43000 -7.94400  7.58600  1.000 43.93452  ?  354 ARG   A C    1 
ATOM   1397 O  O    . ARG   A 1 202 ? 32.20000 -7.04400  7.23000  1.000 43.75522  ?  354 ARG   A O    1 
ATOM   1398 C  CB   . ARG   A 1 202 ? 30.67600 -9.61700  5.87100  1.000 52.05459  ?  354 ARG   A CB   1 
ATOM   1399 C  CG   . ARG   A 1 202 ? 30.94300 -8.70200  4.68500  1.000 58.10285  ?  354 ARG   A CG   1 
ATOM   1400 C  CD   . ARG   A 1 202 ? 30.17000 -9.12400  3.44300  1.000 70.82191  ?  354 ARG   A CD   1 
ATOM   1401 N  NE   . ARG   A 1 202 ? 29.93200 -10.56300 3.38700  1.000 82.44613  ?  354 ARG   A NE   1 
ATOM   1402 C  CZ   . ARG   A 1 202 ? 28.72800 -11.11700 3.27400  1.000 95.13957  ?  354 ARG   A CZ   1 
ATOM   1403 N  NH1  . ARG   A 1 202 ? 27.64700 -10.35200 3.20300  1.000 92.62189  ?  354 ARG   A NH1  1 
ATOM   1404 N  NH2  . ARG   A 1 202 ? 28.60500 -12.43700 3.23000  1.000 99.30183  ?  354 ARG   A NH2  1 
ATOM   1405 N  N    . LEU   A 1 203 ? 30.42400 -7.72500  8.43800  1.000 39.80841  ?  355 LEU   A N    1 
ATOM   1406 C  CA   . LEU   A 1 203 ? 30.24800 -6.41200  9.05000  1.000 30.61736  ?  355 LEU   A CA   1 
ATOM   1407 C  C    . LEU   A 1 203 ? 31.31400 -6.14100  10.10400 1.000 36.39301  ?  355 LEU   A C    1 
ATOM   1408 O  O    . LEU   A 1 203 ? 31.74000 -4.99300  10.27400 1.000 35.21899  ?  355 LEU   A O    1 
ATOM   1409 C  CB   . LEU   A 1 203 ? 28.84900 -6.30100  9.66300  1.000 33.93162  ?  355 LEU   A CB   1 
ATOM   1410 C  CG   . LEU   A 1 203 ? 27.66500 -6.57100  8.72700  1.000 37.25011  ?  355 LEU   A CG   1 
ATOM   1411 C  CD1  . LEU   A 1 203 ? 26.38600 -6.81800  9.51900  1.000 31.85775  ?  355 LEU   A CD1  1 
ATOM   1412 C  CD2  . LEU   A 1 203 ? 27.47500 -5.42300  7.74800  1.000 35.76070  ?  355 LEU   A CD2  1 
ATOM   1413 N  N    . SER   A 1 204 ? 31.76200 -7.18200  10.81200 1.000 38.25229  ?  356 SER   A N    1 
ATOM   1414 C  CA   . SER   A 1 204 ? 32.78700 -7.00400  11.83700 1.000 47.77600  ?  356 SER   A CA   1 
ATOM   1415 C  C    . SER   A 1 204 ? 34.12000 -6.59800  11.21800 1.000 46.07454  ?  356 SER   A C    1 
ATOM   1416 O  O    . SER   A 1 204 ? 34.75700 -5.63700  11.66500 1.000 45.65238  ?  356 SER   A O    1 
ATOM   1417 C  CB   . SER   A 1 204 ? 32.94500 -8.29100  12.65000 1.000 60.19243  ?  356 SER   A CB   1 
ATOM   1418 O  OG   . SER   A 1 204 ? 32.13000 -8.27100  13.80900 1.000 64.68975  ?  356 SER   A OG   1 
ATOM   1419 N  N    . ASN   A 1 205 ? 34.55800 -7.32500  10.18700 1.000 46.96249  ?  357 ASN   A N    1 
ATOM   1420 C  CA   . ASN   A 1 205 ? 35.79800 -6.96800  9.50500  1.000 51.15242  ?  357 ASN   A CA   1 
ATOM   1421 C  C    . ASN   A 1 205 ? 35.70000 -5.59600  8.85300  1.000 46.32675  ?  357 ASN   A C    1 
ATOM   1422 O  O    . ASN   A 1 205 ? 36.70500 -4.88200  8.75700  1.000 47.18788  ?  357 ASN   A O    1 
ATOM   1423 C  CB   . ASN   A 1 205 ? 36.15300 -8.03000  8.46400  1.000 50.27550  ?  357 ASN   A CB   1 
ATOM   1424 C  CG   . ASN   A 1 205 ? 36.42900 -9.38600  9.08500  1.000 55.65113  ?  357 ASN   A CG   1 
ATOM   1425 O  OD1  . ASN   A 1 205 ? 36.88000 -9.47800  10.22800 1.000 57.74601  ?  357 ASN   A OD1  1 
ATOM   1426 N  ND2  . ASN   A 1 205 ? 36.16200 -10.44700 8.33300  1.000 57.85328  ?  357 ASN   A ND2  1 
ATOM   1427 N  N    . THR   A 1 206 ? 34.50500 -5.21000  8.40000  1.000 40.94741  ?  358 THR   A N    1 
ATOM   1428 C  CA   . THR   A 1 206 ? 34.31600 -3.86600  7.86500  1.000 45.29334  ?  358 THR   A CA   1 
ATOM   1429 C  C    . THR   A 1 206 ? 34.51500 -2.81300  8.94700  1.000 46.65276  ?  358 THR   A C    1 
ATOM   1430 O  O    . THR   A 1 206 ? 35.14600 -1.77600  8.70900  1.000 42.46262  ?  358 THR   A O    1 
ATOM   1431 C  CB   . THR   A 1 206 ? 32.92500 -3.73800  7.24400  1.000 47.15037  ?  358 THR   A CB   1 
ATOM   1432 O  OG1  . THR   A 1 206 ? 32.72400 -4.79000  6.29200  1.000 51.08963  ?  358 THR   A OG1  1 
ATOM   1433 C  CG2  . THR   A 1 206 ? 32.77000 -2.39300  6.55100  1.000 55.61944  ?  358 THR   A CG2  1 
ATOM   1434 N  N    . LEU   A 1 207 ? 33.98400 -3.06300  10.14600 1.000 33.89342  ?  359 LEU   A N    1 
ATOM   1435 C  CA   . LEU   A 1 207 ? 34.14100 -2.11000  11.23900 1.000 35.69640  ?  359 LEU   A CA   1 
ATOM   1436 C  C    . LEU   A 1 207 ? 35.58800 -2.05100  11.71200 1.000 33.44557  ?  359 LEU   A C    1 
ATOM   1437 O  O    . LEU   A 1 207 ? 36.13300 -0.96300  11.93800 1.000 35.45513  ?  359 LEU   A O    1 
ATOM   1438 C  CB   . LEU   A 1 207 ? 33.21300 -2.48000  12.39500 1.000 36.43330  ?  359 LEU   A CB   1 
ATOM   1439 C  CG   . LEU   A 1 207 ? 33.37600 -1.62700  13.65400 1.000 40.06596  ?  359 LEU   A CG   1 
ATOM   1440 C  CD1  . LEU   A 1 207 ? 33.08100 -0.16200  13.35600 1.000 34.51692  ?  359 LEU   A CD1  1 
ATOM   1441 C  CD2  . LEU   A 1 207 ? 32.49000 -2.14700  14.77500 1.000 35.66219  ?  359 LEU   A CD2  1 
ATOM   1442 N  N    . GLN   A 1 208 ? 36.22600 -3.21400  11.87200 1.000 31.86222  ?  360 GLN   A N    1 
ATOM   1443 C  CA   . GLN   A 1 208 ? 37.62200 -3.24500  12.30100 1.000 37.40480  ?  360 GLN   A CA   1 
ATOM   1444 C  C    . GLN   A 1 208 ? 38.51400 -2.51500  11.30600 1.000 40.96456  ?  360 GLN   A C    1 
ATOM   1445 O  O    . GLN   A 1 208 ? 39.38200 -1.72300  11.69300 1.000 45.85358  ?  360 GLN   A O    1 
ATOM   1446 C  CB   . GLN   A 1 208 ? 38.09200 -4.69100  12.47000 1.000 44.06459  ?  360 GLN   A CB   1 
ATOM   1447 C  CG   . GLN   A 1 208 ? 37.42000 -5.45400  13.59700 1.000 49.24865  ?  360 GLN   A CG   1 
ATOM   1448 C  CD   . GLN   A 1 208 ? 38.10200 -6.77800  13.88400 1.000 64.67725  ?  360 GLN   A CD   1 
ATOM   1449 O  OE1  . GLN   A 1 208 ? 39.26600 -6.81600  14.28400 1.000 67.33710  ?  360 GLN   A OE1  1 
ATOM   1450 N  NE2  . GLN   A 1 208 ? 37.38000 -7.87300  13.67700 1.000 76.89066  ?  360 GLN   A NE2  1 
ATOM   1451 N  N    . THR   A 1 209 ? 38.31000 -2.77200  10.01300 1.000 43.82574  ?  361 THR   A N    1 
ATOM   1452 C  CA   . THR   A 1 209 ? 39.12300 -2.12100  8.99200  1.000 45.05369  ?  361 THR   A CA   1 
ATOM   1453 C  C    . THR   A 1 209 ? 38.82200 -0.62900  8.91600  1.000 47.17787  ?  361 THR   A C    1 
ATOM   1454 O  O    . THR   A 1 209 ? 39.73200 0.18000   8.70700  1.000 36.20385  ?  361 THR   A O    1 
ATOM   1455 C  CB   . THR   A 1 209 ? 38.89500 -2.79200  7.63700  1.000 49.53358  ?  361 THR   A CB   1 
ATOM   1456 O  OG1  . THR   A 1 209 ? 39.14000 -4.20000  7.75300  1.000 46.20139  ?  361 THR   A OG1  1 
ATOM   1457 C  CG2  . THR   A 1 209 ? 39.82900 -2.21400  6.58700  1.000 54.19790  ?  361 THR   A CG2  1 
ATOM   1458 N  N    . TYR   A 1 210 ? 37.55300 -0.24200  9.09500  1.000 38.69676  ?  362 TYR   A N    1 
ATOM   1459 C  CA   . TYR   A 1 210 ? 37.21000 1.17700   9.05600  1.000 37.74343  ?  362 TYR   A CA   1 
ATOM   1460 C  C    . TYR   A 1 210 ? 37.91600 1.94900   10.16300 1.000 34.43067  ?  362 TYR   A C    1 
ATOM   1461 O  O    . TYR   A 1 210 ? 38.39100 3.06900   9.94300  1.000 42.03940  ?  362 TYR   A O    1 
ATOM   1462 C  CB   . TYR   A 1 210 ? 35.69600 1.38000   9.16800  1.000 36.98806  ?  362 TYR   A CB   1 
ATOM   1463 C  CG   . TYR   A 1 210 ? 35.31300 2.84600   9.22900  1.000 36.67512  ?  362 TYR   A CG   1 
ATOM   1464 C  CD1  . TYR   A 1 210 ? 35.17800 3.50600   10.44700 1.000 35.86774  ?  362 TYR   A CD1  1 
ATOM   1465 C  CD2  . TYR   A 1 210 ? 35.11400 3.57800   8.06500  1.000 41.02036  ?  362 TYR   A CD2  1 
ATOM   1466 C  CE1  . TYR   A 1 210 ? 34.84800 4.85000   10.50100 1.000 37.01448  ?  362 TYR   A CE1  1 
ATOM   1467 C  CE2  . TYR   A 1 210 ? 34.77900 4.92000   8.11000  1.000 36.64046  ?  362 TYR   A CE2  1 
ATOM   1468 C  CZ   . TYR   A 1 210 ? 34.64800 5.55100   9.32800  1.000 40.44339  ?  362 TYR   A CZ   1 
ATOM   1469 O  OH   . TYR   A 1 210 ? 34.31700 6.88600   9.37300  1.000 41.38706  ?  362 TYR   A OH   1 
ATOM   1470 N  N    . ILE   A 1 211 ? 37.97500 1.37600   11.36600 1.000 39.76836  ?  363 ILE   A N    1 
ATOM   1471 C  CA   . ILE   A 1 211 ? 38.57900 2.08000   12.49500 1.000 37.64841  ?  363 ILE   A CA   1 
ATOM   1472 C  C    . ILE   A 1 211 ? 40.06600 2.30600   12.25100 1.000 42.98292  ?  363 ILE   A C    1 
ATOM   1473 O  O    . ILE   A 1 211 ? 40.59500 3.39400   12.51200 1.000 47.35605  ?  363 ILE   A O    1 
ATOM   1474 C  CB   . ILE   A 1 211 ? 38.32500 1.30300   13.80100 1.000 32.20896  ?  363 ILE   A CB   1 
ATOM   1475 C  CG1  . ILE   A 1 211 ? 36.85300 1.41300   14.21000 1.000 35.77339  ?  363 ILE   A CG1  1 
ATOM   1476 C  CG2  . ILE   A 1 211 ? 39.24000 1.80600   14.91400 1.000 35.50960  ?  363 ILE   A CG2  1 
ATOM   1477 C  CD1  . ILE   A 1 211 ? 36.44900 0.46200   15.32100 1.000 31.51040  ?  363 ILE   A CD1  1 
ATOM   1478 N  N    . ARG   A 1 212 ? 40.75900 1.29200   11.72700 1.000 47.97978  ?  364 ARG   A N    1 
ATOM   1479 C  CA   . ARG   A 1 212 ? 42.20100 1.40300   11.52900 1.000 56.35984  ?  364 ARG   A CA   1 
ATOM   1480 C  C    . ARG   A 1 212 ? 42.55500 2.39900   10.43300 1.000 50.48996  ?  364 ARG   A C    1 
ATOM   1481 O  O    . ARG   A 1 212 ? 43.57300 3.09100   10.53400 1.000 52.60256  ?  364 ARG   A O    1 
ATOM   1482 C  CB   . ARG   A 1 212 ? 42.79600 0.03100   11.20900 1.000 65.21706  ?  364 ARG   A CB   1 
ATOM   1483 C  CG   . ARG   A 1 212 ? 42.95000 -0.85700  12.43300 1.000 79.38888  ?  364 ARG   A CG   1 
ATOM   1484 C  CD   . ARG   A 1 212 ? 42.86100 -2.33100  12.07700 1.000 90.93193  ?  364 ARG   A CD   1 
ATOM   1485 N  NE   . ARG   A 1 212 ? 42.28200 -3.11800  13.16200 1.000 100.54198 ?  364 ARG   A NE   1 
ATOM   1486 C  CZ   . ARG   A 1 212 ? 42.88300 -3.37200  14.32200 1.000 102.26185 ?  364 ARG   A CZ   1 
ATOM   1487 N  NH1  . ARG   A 1 212 ? 42.26300 -4.09600  15.24000 1.000 102.27515 ?  364 ARG   A NH1  1 
ATOM   1488 N  NH2  . ARG   A 1 212 ? 44.10300 -2.91400  14.56700 1.000 103.17570 ?  364 ARG   A NH2  1 
ATOM   1489 N  N    . CYS   A 1 213 ? 41.72800 2.49900   9.39500  1.000 46.16280  ?  365 CYS   A N    1 
ATOM   1490 C  CA   . CYS   A 1 213 ? 42.04400 3.32400   8.23500  1.000 51.27343  ?  365 CYS   A CA   1 
ATOM   1491 C  C    . CYS   A 1 213 ? 41.42400 4.71000   8.27900  1.000 44.79519  ?  365 CYS   A C    1 
ATOM   1492 O  O    . CYS   A 1 213 ? 41.97300 5.63800   7.67700  1.000 56.17589  ?  365 CYS   A O    1 
ATOM   1493 C  CB   . CYS   A 1 213 ? 41.58800 2.63000   6.94800  1.000 53.05908  ?  365 CYS   A CB   1 
ATOM   1494 S  SG   . CYS   A 1 213 ? 42.38300 1.03800   6.63300  1.000 63.06167  ?  365 CYS   A SG   1 
ATOM   1495 N  N    . ARG   A 1 214 ? 40.29400 4.88000   8.96200  1.000 42.61102  ?  366 ARG   A N    1 
ATOM   1496 C  CA   . ARG   A 1 214 ? 39.56100 6.13500   8.89700  1.000 41.25421  ?  366 ARG   A CA   1 
ATOM   1497 C  C    . ARG   A 1 214 ? 39.33300 6.80900   10.24300 1.000 45.61849  ?  366 ARG   A C    1 
ATOM   1498 O  O    . ARG   A 1 214 ? 38.92000 7.97500   10.26000 1.000 52.22432  ?  366 ARG   A O    1 
ATOM   1499 C  CB   . ARG   A 1 214 ? 38.20600 5.92500   8.20100  1.000 42.57840  ?  366 ARG   A CB   1 
ATOM   1500 C  CG   . ARG   A 1 214 ? 38.32800 5.28700   6.81900  1.000 49.16815  ?  366 ARG   A CG   1 
ATOM   1501 C  CD   . ARG   A 1 214 ? 38.54500 6.34000   5.74000  1.000 59.20392  ?  366 ARG   A CD   1 
ATOM   1502 N  NE   . ARG   A 1 214 ? 38.27800 5.82600   4.39800  1.000 73.38751  ?  366 ARG   A NE   1 
ATOM   1503 C  CZ   . ARG   A 1 214 ? 39.16300 5.16800   3.65400  1.000 82.80245  ?  366 ARG   A CZ   1 
ATOM   1504 N  NH1  . ARG   A 1 214 ? 38.82400 4.74000   2.44500  1.000 80.94804  ?  366 ARG   A NH1  1 
ATOM   1505 N  NH2  . ARG   A 1 214 ? 40.38500 4.93700   4.11500  1.000 78.16755  ?  366 ARG   A NH2  1 
ATOM   1506 N  N    . HIS   A 1 215 ? 39.58500 6.13300   11.36400 1.000 34.42042  ?  367 HIS   A N    1 
ATOM   1507 C  CA   . HIS   A 1 215 ? 39.45800 6.78100   12.66100 1.000 35.07453  ?  367 HIS   A CA   1 
ATOM   1508 C  C    . HIS   A 1 215 ? 40.84200 7.14500   13.17200 1.000 39.95968  ?  367 HIS   A C    1 
ATOM   1509 O  O    . HIS   A 1 215 ? 41.62600 6.24200   13.50300 1.000 48.23066  ?  367 HIS   A O    1 
ATOM   1510 C  CB   . HIS   A 1 215 ? 38.74000 5.88200   13.66200 1.000 33.38176  ?  367 HIS   A CB   1 
ATOM   1511 C  CG   . HIS   A 1 215 ? 37.99100 6.64000   14.71400 1.000 38.69974  ?  367 HIS   A CG   1 
ATOM   1512 N  ND1  . HIS   A 1 215 ? 36.63400 6.49700   14.91300 1.000 33.35018  ?  367 HIS   A ND1  1 
ATOM   1513 C  CD2  . HIS   A 1 215 ? 38.40800 7.56000   15.61600 1.000 37.06282  ?  367 HIS   A CD2  1 
ATOM   1514 C  CE1  . HIS   A 1 215 ? 36.25000 7.29000   15.89800 1.000 28.52254  ?  367 HIS   A CE1  1 
ATOM   1515 N  NE2  . HIS   A 1 215 ? 37.30700 7.94600   16.34100 1.000 38.74697  ?  367 HIS   A NE2  1 
ATOM   1516 N  N    . PRO   A 1 216 ? 41.18900 8.42500   13.25900 1.000 41.07645  ?  368 PRO   A N    1 
ATOM   1517 C  CA   . PRO   A 1 216 ? 42.54600 8.80100   13.66400 1.000 41.76857  ?  368 PRO   A CA   1 
ATOM   1518 C  C    . PRO   A 1 216 ? 42.74300 8.63300   15.15900 1.000 39.18089  ?  368 PRO   A C    1 
ATOM   1519 O  O    . PRO   A 1 216 ? 41.78100 8.71300   15.93800 1.000 42.50990  ?  368 PRO   A O    1 
ATOM   1520 C  CB   . PRO   A 1 216 ? 42.63600 10.27800  13.25400 1.000 46.29298  ?  368 PRO   A CB   1 
ATOM   1521 C  CG   . PRO   A 1 216 ? 41.22700 10.76300  13.33700 1.000 47.08391  ?  368 PRO   A CG   1 
ATOM   1522 C  CD   . PRO   A 1 216 ? 40.35800 9.59800   12.93700 1.000 40.60136  ?  368 PRO   A CD   1 
ATOM   1523 N  N    . PRO   A 1 217 ? 43.97300 8.39500   15.59800 1.000 40.29987  ?  369 PRO   A N    1 
ATOM   1524 C  CA   . PRO   A 1 217 ? 44.26500 8.40500   17.03200 1.000 38.79134  ?  369 PRO   A CA   1 
ATOM   1525 C  C    . PRO   A 1 217 ? 44.08900 9.80200   17.59500 1.000 41.62628  ?  369 PRO   A C    1 
ATOM   1526 O  O    . PRO   A 1 217 ? 44.17900 10.79100  16.85200 1.000 37.85279  ?  369 PRO   A O    1 
ATOM   1527 C  CB   . PRO   A 1 217 ? 45.73300 7.95200   17.09500 1.000 40.68181  ?  369 PRO   A CB   1 
ATOM   1528 C  CG   . PRO   A 1 217 ? 46.29500 8.33500   15.76600 1.000 36.67345  ?  369 PRO   A CG   1 
ATOM   1529 C  CD   . PRO   A 1 217 ? 45.17400 8.12400   14.78900 1.000 37.27914  ?  369 PRO   A CD   1 
ATOM   1530 N  N    . PRO   A 1 218 ? 43.84700 9.93600   18.90900 1.000 43.75231  ?  370 PRO   A N    1 
ATOM   1531 C  CA   . PRO   A 1 218 ? 43.77300 8.86300   19.90900 1.000 43.43899  ?  370 PRO   A CA   1 
ATOM   1532 C  C    . PRO   A 1 218 ? 42.38900 8.23000   20.05500 1.000 45.60553  ?  370 PRO   A C    1 
ATOM   1533 O  O    . PRO   A 1 218 ? 42.23200 7.28500   20.82900 1.000 45.56594  ?  370 PRO   A O    1 
ATOM   1534 C  CB   . PRO   A 1 218 ? 44.17000 9.58000   21.19900 1.000 45.17044  ?  370 PRO   A CB   1 
ATOM   1535 C  CG   . PRO   A 1 218 ? 43.65700 10.96800  21.00900 1.000 44.97805  ?  370 PRO   A CG   1 
ATOM   1536 C  CD   . PRO   A 1 218 ? 43.74200 11.27000  19.52900 1.000 42.20879  ?  370 PRO   A CD   1 
ATOM   1537 N  N    . GLY   A 1 219 ? 41.40000 8.74400   19.32200 1.000 43.74303  ?  371 GLY   A N    1 
ATOM   1538 C  CA   . GLY   A 1 219 ? 40.05500 8.20000   19.42800 1.000 41.61667  ?  371 GLY   A CA   1 
ATOM   1539 C  C    . GLY   A 1 219 ? 39.96000 6.74300   19.02000 1.000 40.59436  ?  371 GLY   A C    1 
ATOM   1540 O  O    . GLY   A 1 219 ? 39.11700 6.00300   19.53500 1.000 37.75971  ?  371 GLY   A O    1 
ATOM   1541 N  N    . SER   A 1 220 ? 40.82400 6.30700   18.10300 1.000 37.45852  ?  372 SER   A N    1 
ATOM   1542 C  CA   . SER   A 1 220 ? 40.79400 4.93500   17.61300 1.000 39.31657  ?  372 SER   A CA   1 
ATOM   1543 C  C    . SER   A 1 220 ? 41.30300 3.92000   18.62700 1.000 39.14636  ?  372 SER   A C    1 
ATOM   1544 O  O    . SER   A 1 220 ? 41.10700 2.71900   18.41500 1.000 48.35422  ?  372 SER   A O    1 
ATOM   1545 C  CB   . SER   A 1 220 ? 41.62400 4.82200   16.33400 1.000 41.81824  ?  372 SER   A CB   1 
ATOM   1546 O  OG   . SER   A 1 220 ? 42.96100 5.23100   16.56800 1.000 45.58348  ?  372 SER   A OG   1 
ATOM   1547 N  N    . HIS   A 1 221 ? 41.94800 4.36500   19.70900 1.000 45.76278  ?  373 HIS   A N    1 
ATOM   1548 C  CA   . HIS   A 1 221 ? 42.60600 3.46000   20.64700 1.000 46.46383  ?  373 HIS   A CA   1 
ATOM   1549 C  C    . HIS   A 1 221 ? 41.64200 2.44100   21.23800 1.000 45.47681  ?  373 HIS   A C    1 
ATOM   1550 O  O    . HIS   A 1 221 ? 40.72700 2.80400   21.98600 1.000 37.53850  ?  373 HIS   A O    1 
ATOM   1551 C  CB   . HIS   A 1 221 ? 43.27500 4.24600   21.77700 1.000 46.77193  ?  373 HIS   A CB   1 
ATOM   1552 C  CG   . HIS   A 1 221 ? 43.90400 3.37500   22.82000 1.000 50.12478  ?  373 HIS   A CG   1 
ATOM   1553 N  ND1  . HIS   A 1 221 ? 44.94500 2.51500   22.54300 1.000 48.81790  ?  373 HIS   A ND1  1 
ATOM   1554 C  CD2  . HIS   A 1 221 ? 43.62900 3.22000   24.13600 1.000 49.01900  ?  373 HIS   A CD2  1 
ATOM   1555 C  CE1  . HIS   A 1 221 ? 45.28900 1.87400   23.64500 1.000 53.80434  ?  373 HIS   A CE1  1 
ATOM   1556 N  NE2  . HIS   A 1 221 ? 44.50500 2.28300   24.62700 1.000 49.61259  ?  373 HIS   A NE2  1 
ATOM   1557 N  N    . GLN   A 1 222 ? 41.85000 1.16400   20.90900 1.000 41.18572  ?  374 GLN   A N    1 
ATOM   1558 C  CA   . GLN   A 1 222 ? 41.02200 0.06800   21.40900 1.000 31.22099  ?  374 GLN   A CA   1 
ATOM   1559 C  C    . GLN   A 1 222 ? 39.54300 0.30300   21.11700 1.000 38.09837  ?  374 GLN   A C    1 
ATOM   1560 O  O    . GLN   A 1 222 ? 38.67500 -0.15900  21.86000 1.000 34.33882  ?  374 GLN   A O    1 
ATOM   1561 C  CB   . GLN   A 1 222 ? 41.23700 -0.15300  22.91000 1.000 44.78642  ?  374 GLN   A CB   1 
ATOM   1562 C  CG   . GLN   A 1 222 ? 42.58000 -0.77100  23.27600 1.000 64.06326  ?  374 GLN   A CG   1 
ATOM   1563 C  CD   . GLN   A 1 222 ? 42.81500 -2.10500  22.59800 1.000 78.50485  ?  374 GLN   A CD   1 
ATOM   1564 O  OE1  . GLN   A 1 222 ? 43.65000 -2.22000  21.70100 1.000 88.45330  ?  374 GLN   A OE1  1 
ATOM   1565 N  NE2  . GLN   A 1 222 ? 42.07300 -3.12200  23.02100 1.000 73.00910  ?  374 GLN   A NE2  1 
ATOM   1566 N  N    . LEU   A 1 223 ? 39.25000 1.02600   20.03200 1.000 36.50431  ?  375 LEU   A N    1 
ATOM   1567 C  CA   . LEU   A 1 223 ? 37.87300 1.42500   19.76000 1.000 35.67590  ?  375 LEU   A CA   1 
ATOM   1568 C  C    . LEU   A 1 223 ? 36.99100 0.22100   19.45800 1.000 40.45415  ?  375 LEU   A C    1 
ATOM   1569 O  O    . LEU   A 1 223 ? 35.85100 0.15000   19.93200 1.000 46.17745  ?  375 LEU   A O    1 
ATOM   1570 C  CB   . LEU   A 1 223 ? 37.82600 2.42400   18.60400 1.000 35.72942  ?  375 LEU   A CB   1 
ATOM   1571 C  CG   . LEU   A 1 223 ? 36.43600 2.98300   18.27100 1.000 39.12038  ?  375 LEU   A CG   1 
ATOM   1572 C  CD1  . LEU   A 1 223 ? 35.70500 3.43400   19.53000 1.000 33.68196  ?  375 LEU   A CD1  1 
ATOM   1573 C  CD2  . LEU   A 1 223 ? 36.53500 4.12100   17.27000 1.000 47.49072  ?  375 LEU   A CD2  1 
ATOM   1574 N  N    . TYR   A 1 224 ? 37.49400 -0.73300  18.67000 1.000 34.35782  ?  376 TYR   A N    1 
ATOM   1575 C  CA   . TYR   A 1 224 ? 36.70700 -1.92700  18.38700 1.000 39.51063  ?  376 TYR   A CA   1 
ATOM   1576 C  C    . TYR   A 1 224 ? 36.40200 -2.69700  19.66400 1.000 40.63901  ?  376 TYR   A C    1 
ATOM   1577 O  O    . TYR   A 1 224 ? 35.27700 -3.17400  19.85600 1.000 38.87910  ?  376 TYR   A O    1 
ATOM   1578 C  CB   . TYR   A 1 224 ? 37.43200 -2.82300  17.38300 1.000 36.21123  ?  376 TYR   A CB   1 
ATOM   1579 C  CG   . TYR   A 1 224 ? 36.63800 -4.05700  17.01500 1.000 42.67001  ?  376 TYR   A CG   1 
ATOM   1580 C  CD1  . TYR   A 1 224 ? 35.48900 -3.95800  16.24000 1.000 38.49698  ?  376 TYR   A CD1  1 
ATOM   1581 C  CD2  . TYR   A 1 224 ? 37.02600 -5.31600  17.45400 1.000 45.98486  ?  376 TYR   A CD2  1 
ATOM   1582 C  CE1  . TYR   A 1 224 ? 34.75400 -5.07800  15.90500 1.000 48.37260  ?  376 TYR   A CE1  1 
ATOM   1583 C  CE2  . TYR   A 1 224 ? 36.29600 -6.44400  17.12400 1.000 42.63612  ?  376 TYR   A CE2  1 
ATOM   1584 C  CZ   . TYR   A 1 224 ? 35.16100 -6.31800  16.34800 1.000 49.72606  ?  376 TYR   A CZ   1 
ATOM   1585 O  OH   . TYR   A 1 224 ? 34.42900 -7.43500  16.01500 1.000 51.93495  ?  376 TYR   A OH   1 
ATOM   1586 N  N    . ALA   A 1 225 ? 37.38600 -2.81400  20.55900 1.000 33.49010  ?  377 ALA   A N    1 
ATOM   1587 C  CA   . ALA   A 1 225 ? 37.16000 -3.51400  21.81900 1.000 33.78020  ?  377 ALA   A CA   1 
ATOM   1588 C  C    . ALA   A 1 225 ? 36.11500 -2.80000  22.66900 1.000 38.42716  ?  377 ALA   A C    1 
ATOM   1589 O  O    . ALA   A 1 225 ? 35.28100 -3.44600  23.31300 1.000 37.12822  ?  377 ALA   A O    1 
ATOM   1590 C  CB   . ALA   A 1 225 ? 38.47400 -3.65500  22.58700 1.000 41.84380  ?  377 ALA   A CB   1 
ATOM   1591 N  N    . LYS   A 1 226 ? 36.14100 -1.46400  22.67900 1.000 35.79142  ?  378 LYS   A N    1 
ATOM   1592 C  CA   . LYS   A 1 226 ? 35.15400 -0.71500  23.44900 1.000 28.92430  ?  378 LYS   A CA   1 
ATOM   1593 C  C    . LYS   A 1 226 ? 33.75500 -0.85900  22.86100 1.000 37.37122  ?  378 LYS   A C    1 
ATOM   1594 O  O    . LYS   A 1 226 ? 32.77000 -0.88300  23.60800 1.000 32.92948  ?  378 LYS   A O    1 
ATOM   1595 C  CB   . LYS   A 1 226 ? 35.55600 0.75900   23.52300 1.000 27.93580  ?  378 LYS   A CB   1 
ATOM   1596 C  CG   . LYS   A 1 226 ? 36.85500 1.01000   24.28200 1.000 34.05117  ?  378 LYS   A CG   1 
ATOM   1597 C  CD   . LYS   A 1 226 ? 37.14000 2.50000   24.42300 1.000 36.20835  ?  378 LYS   A CD   1 
ATOM   1598 C  CE   . LYS   A 1 226 ? 38.44900 2.75000   25.16300 1.000 50.61799  ?  378 LYS   A CE   1 
ATOM   1599 N  NZ   . LYS   A 1 226 ? 39.01800 4.08800   24.84100 1.000 42.26921  ?  378 LYS   A NZ   1 
ATOM   1600 N  N    . MET   A 1 227 ? 33.64500 -0.96400  21.53600 1.000 32.95143  ?  379 MET   A N    1 
ATOM   1601 C  CA   . MET   A 1 227 ? 32.33200 -1.12700  20.92000 1.000 32.45793  ?  379 MET   A CA   1 
ATOM   1602 C  C    . MET   A 1 227 ? 31.75900 -2.51200  21.19400 1.000 32.54236  ?  379 MET   A C    1 
ATOM   1603 O  O    . MET   A 1 227 ? 30.56500 -2.64700  21.48400 1.000 34.37918  ?  379 MET   A O    1 
ATOM   1604 C  CB   . MET   A 1 227 ? 32.42400 -0.85500  19.41900 1.000 29.30336  ?  379 MET   A CB   1 
ATOM   1605 C  CG   . MET   A 1 227 ? 32.80500 0.58200   19.09100 1.000 25.83120  ?  379 MET   A CG   1 
ATOM   1606 S  SD   . MET   A 1 227 ? 33.01300 0.89000   17.32900 1.000 33.19017  ?  379 MET   A SD   1 
ATOM   1607 C  CE   . MET   A 1 227 ? 31.31800 0.69000   16.76900 1.000 28.49981  ?  379 MET   A CE   1 
ATOM   1608 N  N    . ILE   A 1 228 ? 32.59400 -3.55300  21.11700 1.000 34.59087  ?  380 ILE   A N    1 
ATOM   1609 C  CA   . ILE   A 1 228 ? 32.12500 -4.90000  21.43200 1.000 44.44801  ?  380 ILE   A CA   1 
ATOM   1610 C  C    . ILE   A 1 228 ? 31.71600 -4.99500  22.89600 1.000 47.45787  ?  380 ILE   A C    1 
ATOM   1611 O  O    . ILE   A 1 228 ? 30.80100 -5.75100  23.24800 1.000 48.34780  ?  380 ILE   A O    1 
ATOM   1612 C  CB   . ILE   A 1 228 ? 33.20400 -5.94400  21.07300 1.000 51.68362  ?  380 ILE   A CB   1 
ATOM   1613 C  CG1  . ILE   A 1 228 ? 33.61100 -5.81800  19.60300 1.000 48.68709  ?  380 ILE   A CG1  1 
ATOM   1614 C  CG2  . ILE   A 1 228 ? 32.70300 -7.35400  21.34500 1.000 55.10110  ?  380 ILE   A CG2  1 
ATOM   1615 C  CD1  . ILE   A 1 228 ? 32.44600 -5.76000  18.63900 1.000 53.08194  ?  380 ILE   A CD1  1 
ATOM   1616 N  N    . GLN   A 1 229 ? 32.37200 -4.22700  23.77100 1.000 42.40351  ?  381 GLN   A N    1 
ATOM   1617 C  CA   . GLN   A 1 229 ? 31.95300 -4.17800  25.16800 1.000 38.97931  ?  381 GLN   A CA   1 
ATOM   1618 C  C    . GLN   A 1 229 ? 30.54600 -3.60400  25.30000 1.000 33.89926  ?  381 GLN   A C    1 
ATOM   1619 O  O    . GLN   A 1 229 ? 29.74500 -4.08500  26.11000 1.000 37.28650  ?  381 GLN   A O    1 
ATOM   1620 C  CB   . GLN   A 1 229 ? 32.95000 -3.36000  25.98800 1.000 39.87284  ?  381 GLN   A CB   1 
ATOM   1621 C  CG   . GLN   A 1 229 ? 32.56300 -3.18700  27.44900 1.000 40.46606  ?  381 GLN   A CG   1 
ATOM   1622 C  CD   . GLN   A 1 229 ? 32.42900 -4.51200  28.18000 1.000 49.89653  ?  381 GLN   A CD   1 
ATOM   1623 O  OE1  . GLN   A 1 229 ? 31.47300 -4.73000  28.92400 1.000 49.90290  ?  381 GLN   A OE1  1 
ATOM   1624 N  NE2  . GLN   A 1 229 ? 33.39200 -5.40300  27.97100 1.000 53.45027  ?  381 GLN   A NE2  1 
ATOM   1625 N  N    . LYS   A 1 230 ? 30.22700 -2.57600  24.50800 1.000 32.71379  ?  382 LYS   A N    1 
ATOM   1626 C  CA   . LYS   A 1 230 ? 28.87600 -2.02100  24.52700 1.000 35.49545  ?  382 LYS   A CA   1 
ATOM   1627 C  C    . LYS   A 1 230 ? 27.84400 -3.05200  24.09100 1.000 33.16371  ?  382 LYS   A C    1 
ATOM   1628 O  O    . LYS   A 1 230 ? 26.71700 -3.05200  24.59700 1.000 32.62755  ?  382 LYS   A O    1 
ATOM   1629 C  CB   . LYS   A 1 230 ? 28.79700 -0.78100  23.63400 1.000 36.37255  ?  382 LYS   A CB   1 
ATOM   1630 C  CG   . LYS   A 1 230 ? 29.58400 0.41300   24.14800 1.000 39.03096  ?  382 LYS   A CG   1 
ATOM   1631 C  CD   . LYS   A 1 230 ? 29.18900 0.76700   25.57300 1.000 46.19895  ?  382 LYS   A CD   1 
ATOM   1632 C  CE   . LYS   A 1 230 ? 30.22300 1.67800   26.21800 1.000 54.09764  ?  382 LYS   A CE   1 
ATOM   1633 N  NZ   . LYS   A 1 230 ? 30.71000 1.13800   27.51900 1.000 53.27978  ?  382 LYS   A NZ   1 
ATOM   1634 N  N    . LEU   A 1 231 ? 28.20800 -3.93800  23.15900 1.000 30.56253  ?  383 LEU   A N    1 
ATOM   1635 C  CA   . LEU   A 1 231 ? 27.30600 -5.02000  22.77900 1.000 33.90797  ?  383 LEU   A CA   1 
ATOM   1636 C  C    . LEU   A 1 231 ? 27.04900 -5.95500  23.95300 1.000 33.70328  ?  383 LEU   A C    1 
ATOM   1637 O  O    . LEU   A 1 231 ? 25.93400 -6.46400  24.12200 1.000 31.16602  ?  383 LEU   A O    1 
ATOM   1638 C  CB   . LEU   A 1 231 ? 27.88100 -5.79200  21.59200 1.000 33.65274  ?  383 LEU   A CB   1 
ATOM   1639 C  CG   . LEU   A 1 231 ? 27.92900 -5.03900  20.26200 1.000 40.05660  ?  383 LEU   A CG   1 
ATOM   1640 C  CD1  . LEU   A 1 231 ? 28.66100 -5.85700  19.20600 1.000 43.65844  ?  383 LEU   A CD1  1 
ATOM   1641 C  CD2  . LEU   A 1 231 ? 26.52300 -4.68700  19.79800 1.000 37.06020  ?  383 LEU   A CD2  1 
ATOM   1642 N  N    . ALA   A 1 232 ? 28.07400 -6.19700  24.77400 1.000 29.23711  ?  384 ALA   A N    1 
ATOM   1643 C  CA   . ALA   A 1 232 ? 27.88100 -6.98700  25.98500 1.000 32.78308  ?  384 ALA   A CA   1 
ATOM   1644 C  C    . ALA   A 1 232 ? 26.98500 -6.25900  26.97900 1.000 29.13511  ?  384 ALA   A C    1 
ATOM   1645 O  O    . ALA   A 1 232 ? 26.09600 -6.87100  27.58300 1.000 34.33414  ?  384 ALA   A O    1 
ATOM   1646 C  CB   . ALA   A 1 232 ? 29.23400 -7.31600  26.62100 1.000 34.83477  ?  384 ALA   A CB   1 
ATOM   1647 N  N    . ASP   A 1 233 ? 27.20400 -4.95200  27.16300 1.000 26.03918  ?  385 ASP   A N    1 
ATOM   1648 C  CA   . ASP   A 1 233 ? 26.33700 -4.17300  28.04300 1.000 33.30426  ?  385 ASP   A CA   1 
ATOM   1649 C  C    . ASP   A 1 233 ? 24.89000 -4.22300  27.57100 1.000 34.38886  ?  385 ASP   A C    1 
ATOM   1650 O  O    . ASP   A 1 233 ? 23.96100 -4.23100  28.38900 1.000 33.63224  ?  385 ASP   A O    1 
ATOM   1651 C  CB   . ASP   A 1 233 ? 26.81000 -2.72000  28.11000 1.000 26.44138  ?  385 ASP   A CB   1 
ATOM   1652 C  CG   . ASP   A 1 233 ? 28.24700 -2.58700  28.57700 1.000 35.99141  ?  385 ASP   A CG   1 
ATOM   1653 O  OD1  . ASP   A 1 233 ? 28.82800 -1.50400  28.36900 1.000 33.33310  ?  385 ASP   A OD1  1 
ATOM   1654 O  OD2  . ASP   A 1 233 ? 28.79000 -3.55000  29.15900 1.000 34.41665  ?  385 ASP   A OD2  1 
ATOM   1655 N  N    . LEU   A 1 234 ? 24.68200 -4.25700  26.25200 1.000 28.82073  ?  386 LEU   A N    1 
ATOM   1656 C  CA   . LEU   A 1 234 ? 23.33100 -4.28100  25.70400 1.000 31.46591  ?  386 LEU   A CA   1 
ATOM   1657 C  C    . LEU   A 1 234 ? 22.61500 -5.58200  26.03900 1.000 35.24614  ?  386 LEU   A C    1 
ATOM   1658 O  O    . LEU   A 1 234 ? 21.40600 -5.57900  26.30300 1.000 33.10746  ?  386 LEU   A O    1 
ATOM   1659 C  CB   . LEU   A 1 234 ? 23.37800 -4.06700  24.19300 1.000 31.40107  ?  386 LEU   A CB   1 
ATOM   1660 C  CG   . LEU   A 1 234 ? 23.57600 -2.61700  23.75500 1.000 31.34681  ?  386 LEU   A CG   1 
ATOM   1661 C  CD1  . LEU   A 1 234 ? 24.04800 -2.55400  22.31500 1.000 32.35547  ?  386 LEU   A CD1  1 
ATOM   1662 C  CD2  . LEU   A 1 234 ? 22.28300 -1.83100  23.94000 1.000 37.50522  ?  386 LEU   A CD2  1 
ATOM   1663 N  N    . ARG   A 1 235 ? 23.33700 -6.70700  26.01900 1.000 27.51269  ?  387 ARG   A N    1 
ATOM   1664 C  CA   . ARG   A 1 235 ? 22.73300 -7.97000  26.43600 1.000 38.80562  ?  387 ARG   A CA   1 
ATOM   1665 C  C    . ARG   A 1 235 ? 22.28000 -7.90000  27.88500 1.000 42.27213  ?  387 ARG   A C    1 
ATOM   1666 O  O    . ARG   A 1 235 ? 21.18700 -8.36900  28.22800 1.000 36.22767  ?  387 ARG   A O    1 
ATOM   1667 C  CB   . ARG   A 1 235 ? 23.71700 -9.12300  26.24900 1.000 34.22711  ?  387 ARG   A CB   1 
ATOM   1668 C  CG   . ARG   A 1 235 ? 24.26000 -9.27000  24.84400 1.000 38.98867  ?  387 ARG   A CG   1 
ATOM   1669 C  CD   . ARG   A 1 235 ? 23.16900 -9.61600  23.84200 1.000 37.39297  ?  387 ARG   A CD   1 
ATOM   1670 N  NE   . ARG   A 1 235 ? 23.76000 -10.07800 22.59100 1.000 46.60820  ?  387 ARG   A NE   1 
ATOM   1671 C  CZ   . ARG   A 1 235 ? 23.85500 -11.35400 22.23400 1.000 43.18457  ?  387 ARG   A CZ   1 
ATOM   1672 N  NH1  . ARG   A 1 235 ? 23.37800 -12.30700 23.02300 1.000 40.09022  ?  387 ARG   A NH1  1 
ATOM   1673 N  NH2  . ARG   A 1 235 ? 24.42100 -11.67500 21.07900 1.000 44.77669  ?  387 ARG   A NH2  1 
ATOM   1674 N  N    . SER   A 1 236 ? 23.11100 -7.31400  28.75100 1.000 38.05836  ?  388 SER   A N    1 
ATOM   1675 C  CA   . SER   A 1 236 ? 22.73100 -7.14900  30.14800 1.000 42.05955  ?  388 SER   A CA   1 
ATOM   1676 C  C    . SER   A 1 236 ? 21.52400 -6.22700  30.28200 1.000 37.27762  ?  388 SER   A C    1 
ATOM   1677 O  O    . SER   A 1 236 ? 20.59200 -6.51600  31.04200 1.000 34.23738  ?  388 SER   A O    1 
ATOM   1678 C  CB   . SER   A 1 236 ? 23.92000 -6.61100  30.94800 1.000 41.20058  ?  388 SER   A CB   1 
ATOM   1679 O  OG   . SER   A 1 236 ? 23.48600 -5.78300  32.01000 1.000 48.38139  ?  388 SER   A OG   1 
ATOM   1680 N  N    . LEU   A 1 237 ? 21.52500 -5.10900  29.55200 1.000 31.71962  ?  389 LEU   A N    1 
ATOM   1681 C  CA   . LEU   A 1 237 ? 20.38500 -4.19600  29.59100 1.000 34.50346  ?  389 LEU   A CA   1 
ATOM   1682 C  C    . LEU   A 1 237 ? 19.13800 -4.84700  29.00600 1.000 29.24376  ?  389 LEU   A C    1 
ATOM   1683 O  O    . LEU   A 1 237 ? 18.02300 -4.61200  29.48800 1.000 32.61308  ?  389 LEU   A O    1 
ATOM   1684 C  CB   . LEU   A 1 237 ? 20.72100 -2.90900  28.83800 1.000 38.55090  ?  389 LEU   A CB   1 
ATOM   1685 C  CG   . LEU   A 1 237 ? 21.75600 -2.00100  29.50100 1.000 43.71868  ?  389 LEU   A CG   1 
ATOM   1686 C  CD1  . LEU   A 1 237 ? 22.25300 -0.94800  28.52300 1.000 33.78465  ?  389 LEU   A CD1  1 
ATOM   1687 C  CD2  . LEU   A 1 237 ? 21.17100 -1.34900  30.74400 1.000 40.77526  ?  389 LEU   A CD2  1 
ATOM   1688 N  N    . ASN   A 1 238 ? 19.31000 -5.66100  27.96200 1.000 32.17367  ?  390 ASN   A N    1 
ATOM   1689 C  CA   . ASN   A 1 238 ? 18.19100 -6.40600  27.39400 1.000 34.32868  ?  390 ASN   A CA   1 
ATOM   1690 C  C    . ASN   A 1 238 ? 17.56000 -7.31800  28.43900 1.000 38.54224  ?  390 ASN   A C    1 
ATOM   1691 O  O    . ASN   A 1 238 ? 16.33400 -7.34600  28.59900 1.000 36.00410  ?  390 ASN   A O    1 
ATOM   1692 C  CB   . ASN   A 1 238 ? 18.67600 -7.21500  26.18800 1.000 28.34960  ?  390 ASN   A CB   1 
ATOM   1693 C  CG   . ASN   A 1 238 ? 17.54100 -7.81400  25.37600 1.000 34.48879  ?  390 ASN   A CG   1 
ATOM   1694 O  OD1  . ASN   A 1 238 ? 16.44100 -8.03500  25.88100 1.000 36.14296  ?  390 ASN   A OD1  1 
ATOM   1695 N  ND2  . ASN   A 1 238 ? 17.81400 -8.09700  24.10800 1.000 29.39931  ?  390 ASN   A ND2  1 
ATOM   1696 N  N    . GLU   A 1 239 ? 18.39100 -8.06800  29.16800 1.000 31.59680  ?  391 GLU   A N    1 
ATOM   1697 C  CA   . GLU   A 1 239 ? 17.87200 -9.00400  30.16000 1.000 38.60756  ?  391 GLU   A CA   1 
ATOM   1698 C  C    . GLU   A 1 239 ? 17.10500 -8.28100  31.25900 1.000 42.65977  ?  391 GLU   A C    1 
ATOM   1699 O  O    . GLU   A 1 239 ? 16.05100 -8.75100  31.70300 1.000 40.16637  ?  391 GLU   A O    1 
ATOM   1700 C  CB   . GLU   A 1 239 ? 19.01800 -9.82200  30.75800 1.000 39.61910  ?  391 GLU   A CB   1 
ATOM   1701 C  CG   . GLU   A 1 239 ? 19.35200 -11.08300 29.98000 1.000 59.86733  ?  391 GLU   A CG   1 
ATOM   1702 C  CD   . GLU   A 1 239 ? 20.57200 -11.79700 30.52600 1.000 82.35832  ?  391 GLU   A CD   1 
ATOM   1703 O  OE1  . GLU   A 1 239 ? 20.44700 -12.48000 31.56500 1.000 89.93993  ?  391 GLU   A OE1  1 
ATOM   1704 O  OE2  . GLU   A 1 239 ? 21.65700 -11.67700 29.91600 1.000 89.38783  ?  391 GLU   A OE2  1 
ATOM   1705 N  N    . GLU   A 1 240 ? 17.61500 -7.13100  31.71000 1.000 37.77069  ?  392 GLU   A N    1 
ATOM   1706 C  CA   . GLU   A 1 240 ? 16.94600 -6.40600  32.78400 1.000 45.00051  ?  392 GLU   A CA   1 
ATOM   1707 C  C    . GLU   A 1 240 ? 15.64500 -5.77600  32.30200 1.000 43.82697  ?  392 GLU   A C    1 
ATOM   1708 O  O    . GLU   A 1 240 ? 14.65300 -5.74900  33.04000 1.000 34.21643  ?  392 GLU   A O    1 
ATOM   1709 C  CB   . GLU   A 1 240 ? 17.87400 -5.33900  33.36300 1.000 40.94013  ?  392 GLU   A CB   1 
ATOM   1710 C  CG   . GLU   A 1 240 ? 17.30700 -4.62300  34.58100 1.000 51.32836  ?  392 GLU   A CG   1 
ATOM   1711 C  CD   . GLU   A 1 240 ? 16.91500 -5.57900  35.69600 1.000 51.21968  ?  392 GLU   A CD   1 
ATOM   1712 O  OE1  . GLU   A 1 240 ? 15.91400 -5.30400  36.39200 1.000 45.74957  ?  392 GLU   A OE1  1 
ATOM   1713 O  OE2  . GLU   A 1 240 ? 17.60700 -6.60300  35.88200 1.000 52.23275  ?  392 GLU   A OE2  1 
ATOM   1714 N  N    . HIS   A 1 241 ? 15.63100 -5.25500  31.07300 1.000 30.08151  ?  393 HIS   A N    1 
ATOM   1715 C  CA   . HIS   A 1 241 ? 14.39300 -4.70300  30.53800 1.000 38.33983  ?  393 HIS   A CA   1 
ATOM   1716 C  C    . HIS   A 1 241 ? 13.34600 -5.79100  30.34500 1.000 30.78346  ?  393 HIS   A C    1 
ATOM   1717 O  O    . HIS   A 1 241 ? 12.15900 -5.57100  30.61800 1.000 32.73277  ?  393 HIS   A O    1 
ATOM   1718 C  CB   . HIS   A 1 241 ? 14.65100 -3.97300  29.22100 1.000 37.45226  ?  393 HIS   A CB   1 
ATOM   1719 C  CG   . HIS   A 1 241 ? 13.40300 -3.45800  28.57200 1.000 36.44103  ?  393 HIS   A CG   1 
ATOM   1720 N  ND1  . HIS   A 1 241 ? 12.67600 -4.19900  27.66600 1.000 33.41153  ?  393 HIS   A ND1  1 
ATOM   1721 C  CD2  . HIS   A 1 241 ? 12.74300 -2.28400  28.71400 1.000 30.02813  ?  393 HIS   A CD2  1 
ATOM   1722 C  CE1  . HIS   A 1 241 ? 11.62600 -3.50000  27.27000 1.000 36.18087  ?  393 HIS   A CE1  1 
ATOM   1723 N  NE2  . HIS   A 1 241 ? 11.64400 -2.33400  27.89000 1.000 35.24999  ?  393 HIS   A NE2  1 
ATOM   1724 N  N    . SER   A 1 242 ? 13.76600 -6.97300  29.88400 1.000 31.19245  ?  394 SER   A N    1 
ATOM   1725 C  CA   . SER   A 1 242 ? 12.82400 -8.07800  29.73000 1.000 36.43260  ?  394 SER   A CA   1 
ATOM   1726 C  C    . SER   A 1 242 ? 12.22000 -8.47400  31.06800 1.000 44.02333  ?  394 SER   A C    1 
ATOM   1727 O  O    . SER   A 1 242 ? 11.02500 -8.78700  31.14900 1.000 36.05720  ?  394 SER   A O    1 
ATOM   1728 C  CB   . SER   A 1 242 ? 13.52100 -9.27400  29.07600 1.000 44.54936  ?  394 SER   A CB   1 
ATOM   1729 O  OG   . SER   A 1 242 ? 13.96700 -8.94000  27.76700 1.000 52.54880  ?  394 SER   A OG   1 
ATOM   1730 N  N    A LYS   A 1 243 ? 13.02700 -8.47600  32.13000 0.620 39.51581  ?  395 LYS   A N    1 
ATOM   1731 N  N    B LYS   A 1 243 ? 13.03100 -8.48200  32.12700 0.380 39.75059  ?  395 LYS   A N    1 
ATOM   1732 C  CA   A LYS   A 1 243 ? 12.51400 -8.81700  33.45300 0.620 38.81202  ?  395 LYS   A CA   1 
ATOM   1733 C  CA   B LYS   A 1 243 ? 12.52600 -8.81100  33.45600 0.380 39.77307  ?  395 LYS   A CA   1 
ATOM   1734 C  C    A LYS   A 1 243 ? 11.45000 -7.82200  33.90000 0.620 40.70119  ?  395 LYS   A C    1 
ATOM   1735 C  C    B LYS   A 1 243 ? 11.45200 -7.82200  33.89400 0.380 40.22651  ?  395 LYS   A C    1 
ATOM   1736 O  O    A LYS   A 1 243 ? 10.36700 -8.21100  34.35600 0.620 40.84812  ?  395 LYS   A O    1 
ATOM   1737 O  O    B LYS   A 1 243 ? 10.36600 -8.21700  34.33700 0.380 40.92974  ?  395 LYS   A O    1 
ATOM   1738 C  CB   A LYS   A 1 243 ? 13.66400 -8.86800  34.46300 0.620 44.44759  ?  395 LYS   A CB   1 
ATOM   1739 C  CB   B LYS   A 1 243 ? 13.68000 -8.83000  34.46100 0.380 44.14119  ?  395 LYS   A CB   1 
ATOM   1740 C  CG   A LYS   A 1 243 ? 14.34800 -10.21900 34.56900 0.620 48.06937  ?  395 LYS   A CG   1 
ATOM   1741 C  CG   B LYS   A 1 243 ? 14.27000 -10.20300 34.72000 0.380 47.95914  ?  395 LYS   A CG   1 
ATOM   1742 C  CD   A LYS   A 1 243 ? 15.38700 -10.22000 35.68200 0.620 49.50575  ?  395 LYS   A CD   1 
ATOM   1743 C  CD   B LYS   A 1 243 ? 15.18400 -10.18300 35.93800 0.380 49.74492  ?  395 LYS   A CD   1 
ATOM   1744 C  CE   A LYS   A 1 243 ? 16.79900 -10.23500 35.12000 0.620 49.12780  ?  395 LYS   A CE   1 
ATOM   1745 C  CE   B LYS   A 1 243 ? 14.50900 -9.50800  37.12100 0.380 50.34498  ?  395 LYS   A CE   1 
ATOM   1746 N  NZ   A LYS   A 1 243 ? 17.66400 -11.22900 35.81500 0.620 55.40365  ?  395 LYS   A NZ   1 
ATOM   1747 N  NZ   B LYS   A 1 243 ? 14.98400 -10.05300 38.42200 0.380 55.69577  ?  395 LYS   A NZ   1 
ATOM   1748 N  N    . GLN   A 1 244 ? 11.74000 -6.52600  33.77200 1.000 34.96468  ?  396 GLN   A N    1 
ATOM   1749 C  CA   . GLN   A 1 244 ? 10.78200 -5.51400  34.19900 1.000 30.07531  ?  396 GLN   A CA   1 
ATOM   1750 C  C    . GLN   A 1 244 ? 9.57800  -5.45900  33.26600 1.000 37.50435  ?  396 GLN   A C    1 
ATOM   1751 O  O    . GLN   A 1 244 ? 8.44800  -5.23900  33.71900 1.000 38.12899  ?  396 GLN   A O    1 
ATOM   1752 C  CB   . GLN   A 1 244 ? 11.47500 -4.15800  34.29000 1.000 29.57722  ?  396 GLN   A CB   1 
ATOM   1753 C  CG   . GLN   A 1 244 ? 12.70500 -4.18000  35.19300 1.000 33.24073  ?  396 GLN   A CG   1 
ATOM   1754 C  CD   . GLN   A 1 244 ? 13.18000 -2.79500  35.57500 1.000 38.76141  ?  396 GLN   A CD   1 
ATOM   1755 O  OE1  . GLN   A 1 244 ? 12.51000 -1.80300  35.30000 1.000 38.93569  ?  396 GLN   A OE1  1 
ATOM   1756 N  NE2  . GLN   A 1 244 ? 14.34300 -2.72100  36.21400 1.000 47.44110  ?  396 GLN   A NE2  1 
ATOM   1757 N  N    . TYR   A 1 245 ? 9.79200  -5.66300  31.96300 1.000 35.12225  ?  397 TYR   A N    1 
ATOM   1758 C  CA   . TYR   A 1 245 ? 8.66800  -5.70300  31.03300 1.000 41.12870  ?  397 TYR   A CA   1 
ATOM   1759 C  C    . TYR   A 1 245 ? 7.74700  -6.87600  31.34400 1.000 44.14003  ?  397 TYR   A C    1 
ATOM   1760 O  O    . TYR   A 1 245 ? 6.52000  -6.72700  31.37100 1.000 38.92163  ?  397 TYR   A O    1 
ATOM   1761 C  CB   . TYR   A 1 245 ? 9.16600  -5.78700  29.58900 1.000 37.25564  ?  397 TYR   A CB   1 
ATOM   1762 C  CG   . TYR   A 1 245 ? 8.04300  -5.97600  28.58700 1.000 31.75550  ?  397 TYR   A CG   1 
ATOM   1763 C  CD1  . TYR   A 1 245 ? 7.36200  -4.88400  28.06700 1.000 31.25190  ?  397 TYR   A CD1  1 
ATOM   1764 C  CD2  . TYR   A 1 245 ? 7.65800  -7.24600  28.17300 1.000 34.09801  ?  397 TYR   A CD2  1 
ATOM   1765 C  CE1  . TYR   A 1 245 ? 6.33100  -5.04900  27.15800 1.000 37.28369  ?  397 TYR   A CE1  1 
ATOM   1766 C  CE2  . TYR   A 1 245 ? 6.62600  -7.42100  27.26800 1.000 38.93259  ?  397 TYR   A CE2  1 
ATOM   1767 C  CZ   . TYR   A 1 245 ? 5.96800  -6.31900  26.76300 1.000 40.48914  ?  397 TYR   A CZ   1 
ATOM   1768 O  OH   . TYR   A 1 245 ? 4.94300  -6.48900  25.85900 1.000 43.26736  ?  397 TYR   A OH   1 
ATOM   1769 N  N    . ARG   A 1 246 ? 8.32800  -8.06000  31.56300 1.000 39.11294  ?  398 ARG   A N    1 
ATOM   1770 C  CA   . ARG   A 1 246 ? 7.52900  -9.23000  31.91100 1.000 40.64530  ?  398 ARG   A CA   1 
ATOM   1771 C  C    . ARG   A 1 246 ? 6.72100  -8.98300  33.17600 1.000 49.16584  ?  398 ARG   A C    1 
ATOM   1772 O  O    . ARG   A 1 246 ? 5.55500  -9.38500  33.26800 1.000 48.51039  ?  398 ARG   A O    1 
ATOM   1773 C  CB   . ARG   A 1 246 ? 8.43500  -10.45000 32.08400 1.000 49.99226  ?  398 ARG   A CB   1 
ATOM   1774 C  CG   . ARG   A 1 246 ? 8.32400  -11.48400 30.97400 1.000 61.05022  ?  398 ARG   A CG   1 
ATOM   1775 C  CD   . ARG   A 1 246 ? 9.65000  -12.20200 30.75000 1.000 71.99804  ?  398 ARG   A CD   1 
ATOM   1776 N  NE   . ARG   A 1 246 ? 10.14200 -12.85000 31.96300 1.000 73.31330  ?  398 ARG   A NE   1 
ATOM   1777 C  CZ   . ARG   A 1 246 ? 11.42600 -12.93400 32.30000 1.000 83.87418  ?  398 ARG   A CZ   1 
ATOM   1778 N  NH1  . ARG   A 1 246 ? 12.35700 -12.41100 31.51300 1.000 81.82699  ?  398 ARG   A NH1  1 
ATOM   1779 N  NH2  . ARG   A 1 246 ? 11.78000 -13.54200 33.42500 1.000 85.40707  ?  398 ARG   A NH2  1 
ATOM   1780 N  N    . SER   A 1 247 ? 7.32200  -8.31100  34.16000 1.000 42.73354  ?  399 SER   A N    1 
ATOM   1781 C  CA   . SER   A 1 247 ? 6.60800  -8.00500  35.39400 1.000 52.51598  ?  399 SER   A CA   1 
ATOM   1782 C  C    . SER   A 1 247 ? 5.51400  -6.97200  35.15400 1.000 45.52011  ?  399 SER   A C    1 
ATOM   1783 O  O    . SER   A 1 247 ? 4.38900  -7.11900  35.64600 1.000 48.01307  ?  399 SER   A O    1 
ATOM   1784 C  CB   . SER   A 1 247 ? 7.59000  -7.51400  36.45800 1.000 57.27252  ?  399 SER   A CB   1 
ATOM   1785 O  OG   . SER   A 1 247 ? 6.90000  -7.01100  37.58800 1.000 73.80863  ?  399 SER   A OG   1 
ATOM   1786 N  N    . LEU   A 1 248 ? 5.82600  -5.91700  34.39900 1.000 41.62823  ?  400 LEU   A N    1 
ATOM   1787 C  CA   . LEU   A 1 248 ? 4.84200  -4.86900  34.14900 1.000 43.22261  ?  400 LEU   A CA   1 
ATOM   1788 C  C    . LEU   A 1 248 ? 3.68800  -5.39000  33.30100 1.000 44.65526  ?  400 LEU   A C    1 
ATOM   1789 O  O    . LEU   A 1 248 ? 2.51600  -5.16500  33.62300 1.000 49.76321  ?  400 LEU   A O    1 
ATOM   1790 C  CB   . LEU   A 1 248 ? 5.51000  -3.67000  33.47400 1.000 41.59635  ?  400 LEU   A CB   1 
ATOM   1791 C  CG   . LEU   A 1 248 ? 6.45000  -2.82200  34.33500 1.000 57.55281  ?  400 LEU   A CG   1 
ATOM   1792 C  CD1  . LEU   A 1 248 ? 7.16600  -1.78200  33.48300 1.000 50.70862  ?  400 LEU   A CD1  1 
ATOM   1793 C  CD2  . LEU   A 1 248 ? 5.69400  -2.16400  35.47900 1.000 65.93961  ?  400 LEU   A CD2  1 
ATOM   1794 N  N    . SER   A 1 249 ? 4.00200  -6.10000  32.21400 1.000 50.42789  ?  401 SER   A N    1 
ATOM   1795 C  CA   . SER   A 1 249 ? 2.97000  -6.61100  31.31900 1.000 49.11592  ?  401 SER   A CA   1 
ATOM   1796 C  C    . SER   A 1 249 ? 2.18100  -7.76700  31.92200 1.000 50.88369  ?  401 SER   A C    1 
ATOM   1797 O  O    . SER   A 1 249 ? 1.14500  -8.14000  31.36100 1.000 49.48169  ?  401 SER   A O    1 
ATOM   1798 C  CB   . SER   A 1 249 ? 3.59500  -7.04200  29.98900 1.000 39.80398  ?  401 SER   A CB   1 
ATOM   1799 O  OG   . SER   A 1 249 ? 4.20400  -8.31700  30.09500 1.000 47.52391  ?  401 SER   A OG   1 
ATOM   1800 N  N    . PHE   A 1 250 ? 2.64000  -8.33800  33.04000 1.000 52.38813  ?  402 PHE   A N    1 
ATOM   1801 C  CA   . PHE   A 1 250 ? 1.86000  -9.37100  33.71500 1.000 55.79927  ?  402 PHE   A CA   1 
ATOM   1802 C  C    . PHE   A 1 250 ? 0.52400  -8.82900  34.20200 1.000 57.35761  ?  402 PHE   A C    1 
ATOM   1803 O  O    . PHE   A 1 250 ? -0.44200 -9.58700  34.33900 1.000 51.93301  ?  402 PHE   A O    1 
ATOM   1804 C  CB   . PHE   A 1 250 ? 2.65200  -9.95400  34.88600 1.000 53.29626  ?  402 PHE   A CB   1 
ATOM   1805 C  CG   . PHE   A 1 250 ? 1.97100  -11.11100 35.56300 1.000 62.47642  ?  402 PHE   A CG   1 
ATOM   1806 C  CD1  . PHE   A 1 250 ? 1.28900  -10.93200 36.75600 1.000 69.85091  ?  402 PHE   A CD1  1 
ATOM   1807 C  CD2  . PHE   A 1 250 ? 2.01100  -12.37700 35.00400 1.000 73.43222  ?  402 PHE   A CD2  1 
ATOM   1808 C  CE1  . PHE   A 1 250 ? 0.66000  -11.99500 37.37900 1.000 78.34313  ?  402 PHE   A CE1  1 
ATOM   1809 C  CE2  . PHE   A 1 250 ? 1.38400  -13.44400 35.62100 1.000 79.99637  ?  402 PHE   A CE2  1 
ATOM   1810 C  CZ   . PHE   A 1 250 ? 0.70900  -13.25300 36.81000 1.000 82.29794  ?  402 PHE   A CZ   1 
ATOM   1811 N  N    . GLN   A 1 251 ? 0.45300  -7.53300  34.47800 1.000 55.82806  ?  403 GLN   A N    1 
ATOM   1812 C  CA   . GLN   A 1 251 ? -0.81000 -6.90200  34.82800 1.000 50.25751  ?  403 GLN   A CA   1 
ATOM   1813 C  C    . GLN   A 1 251 ? -1.59100 -6.59700  33.55700 1.000 46.46588  ?  403 GLN   A C    1 
ATOM   1814 O  O    . GLN   A 1 251 ? -1.09200 -5.85700  32.70100 1.000 45.13490  ?  403 GLN   A O    1 
ATOM   1815 C  CB   . GLN   A 1 251 ? -0.57200 -5.62000  35.61300 1.000 58.78629  ?  403 GLN   A CB   1 
ATOM   1816 C  CG   . GLN   A 1 251 ? -0.41900 -5.81800  37.10900 1.000 79.10712  ?  403 GLN   A CG   1 
ATOM   1817 C  CD   . GLN   A 1 251 ? 1.02500  -6.00000  37.52500 1.000 85.76863  ?  403 GLN   A CD   1 
ATOM   1818 O  OE1  . GLN   A 1 251 ? 1.46000  -7.11100  37.82500 1.000 92.04834  ?  403 GLN   A OE1  1 
ATOM   1819 N  NE2  . GLN   A 1 251 ? 1.78000  -4.90600  37.54000 1.000 89.46717  ?  403 GLN   A NE2  1 
ATOM   1820 N  N    . PRO   A 1 252 ? -2.79600 -7.14700  33.38300 1.000 42.91365  ?  404 PRO   A N    1 
ATOM   1821 C  CA   . PRO   A 1 252 ? -3.59400 -6.78300  32.20000 1.000 38.50548  ?  404 PRO   A CA   1 
ATOM   1822 C  C    . PRO   A 1 252 ? -3.87400 -5.29500  32.10600 1.000 40.77490  ?  404 PRO   A C    1 
ATOM   1823 O  O    . PRO   A 1 252 ? -3.96400 -4.75900  30.99400 1.000 47.20911  ?  404 PRO   A O    1 
ATOM   1824 C  CB   . PRO   A 1 252 ? -4.88400 -7.59500  32.38600 1.000 43.35660  ?  404 PRO   A CB   1 
ATOM   1825 C  CG   . PRO   A 1 252 ? -4.48900 -8.74200  33.26000 1.000 47.28007  ?  404 PRO   A CG   1 
ATOM   1826 C  CD   . PRO   A 1 252 ? -3.43600 -8.20100  34.18800 1.000 45.73778  ?  404 PRO   A CD   1 
ATOM   1827 N  N    . GLU   A 1 253 ? -4.00400 -4.60800  33.24500 1.000 44.73620  ?  405 GLU   A N    1 
ATOM   1828 C  CA   . GLU   A 1 253 ? -4.19600 -3.16200  33.23000 1.000 46.59366  ?  405 GLU   A CA   1 
ATOM   1829 C  C    . GLU   A 1 253 ? -3.02900 -2.44700  32.55900 1.000 50.10746  ?  405 GLU   A C    1 
ATOM   1830 O  O    . GLU   A 1 253 ? -3.22200 -1.39800  31.93400 1.000 52.34180  ?  405 GLU   A O    1 
ATOM   1831 C  CB   . GLU   A 1 253 ? -4.38800 -2.64600  34.65700 1.000 55.68050  ?  405 GLU   A CB   1 
ATOM   1832 C  CG   . GLU   A 1 253 ? -3.38200 -3.19700  35.66300 1.000 67.02481  ?  405 GLU   A CG   1 
ATOM   1833 C  CD   . GLU   A 1 253 ? -3.86800 -4.46000  36.35200 1.000 75.56581  ?  405 GLU   A CD   1 
ATOM   1834 O  OE1  . GLU   A 1 253 ? -4.20400 -5.43400  35.64700 1.000 78.08682  ?  405 GLU   A OE1  1 
ATOM   1835 O  OE2  . GLU   A 1 253 ? -3.90700 -4.48200  37.60000 1.000 87.54012  ?  405 GLU   A OE2  1 
ATOM   1836 N  N    . ASN   A 1 254 ? -1.81600 -2.99400  32.67600 1.000 41.87502  ?  406 ASN   A N    1 
ATOM   1837 C  CA   . ASN   A 1 254 ? -0.67000 -2.41200  31.98700 1.000 40.98897  ?  406 ASN   A CA   1 
ATOM   1838 C  C    . ASN   A 1 254 ? -0.60000 -2.87400  30.53800 1.000 36.88178  ?  406 ASN   A C    1 
ATOM   1839 O  O    . ASN   A 1 254 ? -0.29000 -2.07900  29.64500 1.000 34.78729  ?  406 ASN   A O    1 
ATOM   1840 C  CB   . ASN   A 1 254 ? 0.62600  -2.77200  32.71500 1.000 42.65648  ?  406 ASN   A CB   1 
ATOM   1841 C  CG   . ASN   A 1 254 ? 0.76300  -2.06800  34.04900 1.000 44.38454  ?  406 ASN   A CG   1 
ATOM   1842 O  OD1  . ASN   A 1 254 ? 0.13900  -1.03400  34.28500 1.000 51.97275  ?  406 ASN   A OD1  1 
ATOM   1843 N  ND2  . ASN   A 1 254 ? 1.58200  -2.62800  34.93200 1.000 48.91585  ?  406 ASN   A ND2  1 
ATOM   1844 N  N    . SER   A 1 255 ? -0.88200 -4.15800  30.29200 1.000 36.77882  ?  407 SER   A N    1 
ATOM   1845 C  CA   . SER   A 1 255 ? -0.87200 -4.68100  28.92900 1.000 40.92617  ?  407 SER   A CA   1 
ATOM   1846 C  C    . SER   A 1 255 ? -1.88800 -3.97200  28.04400 1.000 34.76242  ?  407 SER   A C    1 
ATOM   1847 O  O    . SER   A 1 255 ? -1.70700 -3.91100  26.82200 1.000 33.27331  ?  407 SER   A O    1 
ATOM   1848 C  CB   . SER   A 1 255 ? -1.14900 -6.18300  28.94000 1.000 50.76989  ?  407 SER   A CB   1 
ATOM   1849 O  OG   . SER   A 1 255 ? 0.04000  -6.92900  29.10200 1.000 62.74460  ?  407 SER   A OG   1 
ATOM   1850 N  N    . MET   A 1 256 ? -2.91000 -3.40600  28.64400 1.000 38.98236  ?  408 MET   A N    1 
ATOM   1851 C  CA   . MET   A 1 256 ? -3.95000 -2.74600  27.83800 1.000 45.78208  ?  408 MET   A CA   1 
ATOM   1852 C  C    . MET   A 1 256 ? -3.40000 -1.47300  27.21500 1.000 47.59640  ?  408 MET   A C    1 
ATOM   1853 O  O    . MET   A 1 256 ? -3.85700 -1.13900  26.18300 1.000 43.21837  ?  408 MET   A O    1 
ATOM   1854 C  CB   . MET   A 1 256 ? -5.13800 -2.38100  28.71700 1.000 40.60225  ?  408 MET   A CB   1 
ATOM   1855 C  CG   . MET   A 1 256 ? -6.19600 -3.39100  28.67100 1.000 53.22671  ?  408 MET   A CG   1 
ATOM   1856 S  SD   . MET   A 1 256 ? -7.46600 -3.03700  29.85400 1.000 61.75162  ?  408 MET   A SD   1 
ATOM   1857 C  CE   . MET   A 1 256 ? -7.51800 -1.25700  29.85400 1.000 67.91942  ?  408 MET   A CE   1 
ATOM   1858 N  N    . LYS   A 1 257 ? -2.46500 -0.80300  27.86400 1.000 41.20118  ?  409 LYS   A N    1 
ATOM   1859 C  CA   . LYS   A 1 257 ? -1.91000 0.44400   27.35900 1.000 42.57319  ?  409 LYS   A CA   1 
ATOM   1860 C  C    . LYS   A 1 257 ? -0.75700 0.23000   26.38800 1.000 36.28819  ?  409 LYS   A C    1 
ATOM   1861 O  O    . LYS   A 1 257 ? -0.24200 1.21000   25.84100 1.000 39.30243  ?  409 LYS   A O    1 
ATOM   1862 C  CB   . LYS   A 1 257 ? -1.44100 1.33200   28.52000 1.000 49.18748  ?  409 LYS   A CB   1 
ATOM   1863 C  CG   . LYS   A 1 257 ? -2.41100 1.42200   29.70600 1.000 59.22029  ?  409 LYS   A CG   1 
ATOM   1864 C  CD   . LYS   A 1 257 ? -2.96000 2.82700   29.86300 1.000 68.58621  ?  409 LYS   A CD   1 
ATOM   1865 C  CE   . LYS   A 1 257 ? -3.96800 3.14700   28.76300 1.000 80.86936  ?  409 LYS   A CE   1 
ATOM   1866 N  NZ   . LYS   A 1 257 ? -4.45300 4.56800   28.81800 1.000 82.16153  ?  409 LYS   A NZ   1 
ATOM   1867 N  N    . LEU   A 1 258 ? -0.32900 -1.01200  26.17700 1.000 33.81462  ?  410 LEU   A N    1 
ATOM   1868 C  CA   . LEU   A 1 258 ? 0.70700  -1.30100  25.19900 1.000 31.46187  ?  410 LEU   A CA   1 
ATOM   1869 C  C    . LEU   A 1 258 ? 0.10800  -1.33500  23.79300 1.000 37.30495  ?  410 LEU   A C    1 
ATOM   1870 O  O    . LEU   A 1 258 ? -1.10100 -1.18800  23.59400 1.000 32.25778  ?  410 LEU   A O    1 
ATOM   1871 C  CB   . LEU   A 1 258 ? 1.40600  -2.62000  25.53100 1.000 36.66174  ?  410 LEU   A CB   1 
ATOM   1872 C  CG   . LEU   A 1 258 ? 1.99000  -2.75400  26.94100 1.000 43.38680  ?  410 LEU   A CG   1 
ATOM   1873 C  CD1  . LEU   A 1 258 ? 2.70800  -4.08500  27.10600 1.000 30.22633  ?  410 LEU   A CD1  1 
ATOM   1874 C  CD2  . LEU   A 1 258 ? 2.92700  -1.59500  27.24400 1.000 38.16302  ?  410 LEU   A CD2  1 
ATOM   1875 N  N    . THR   A 1 259 ? 0.96200  -1.52300  22.80100 1.000 38.43869  ?  411 THR   A N    1 
ATOM   1876 C  CA   . THR   A 1 259 ? 0.51200  -1.62700  21.42400 1.000 38.08406  ?  411 THR   A CA   1 
ATOM   1877 C  C    . THR   A 1 259 ? 0.55900  -3.07400  20.96000 1.000 32.67044  ?  411 THR   A C    1 
ATOM   1878 O  O    . THR   A 1 259 ? 1.27600  -3.89800  21.53500 1.000 38.92818  ?  411 THR   A O    1 
ATOM   1879 C  CB   . THR   A 1 259 ? 1.38300  -0.76200  20.50800 1.000 38.71104  ?  411 THR   A CB   1 
ATOM   1880 O  OG1  . THR   A 1 259 ? 2.64700  -1.40700  20.30500 1.000 45.73377  ?  411 THR   A OG1  1 
ATOM   1881 C  CG2  . THR   A 1 259 ? 1.60800  0.60700   21.12800 1.000 35.73968  ?  411 THR   A CG2  1 
ATOM   1882 N  N    . PRO   A 1 260 ? -0.21100 -3.42700  19.92600 1.000 35.19108  ?  412 PRO   A N    1 
ATOM   1883 C  CA   . PRO   A 1 260 ? -0.14900 -4.80900  19.42000 1.000 38.14220  ?  412 PRO   A CA   1 
ATOM   1884 C  C    . PRO   A 1 260 ? 1.24300  -5.22300  18.97500 1.000 33.27183  ?  412 PRO   A C    1 
ATOM   1885 O  O    . PRO   A 1 260 ? 1.65800  -6.35900  19.23800 1.000 37.40537  ?  412 PRO   A O    1 
ATOM   1886 C  CB   . PRO   A 1 260 ? -1.14100 -4.79400  18.25000 1.000 35.02955  ?  412 PRO   A CB   1 
ATOM   1887 C  CG   . PRO   A 1 260 ? -2.09400 -3.70100  18.58400 1.000 38.95333  ?  412 PRO   A CG   1 
ATOM   1888 C  CD   . PRO   A 1 260 ? -1.26900 -2.64600  19.26200 1.000 33.00079  ?  412 PRO   A CD   1 
ATOM   1889 N  N    . LEU   A 1 261 ? 1.98000  -4.33200  18.30800 1.000 30.41688  ?  413 LEU   A N    1 
ATOM   1890 C  CA   . LEU   A 1 261 ? 3.33000  -4.67600  17.87000 1.000 36.34078  ?  413 LEU   A CA   1 
ATOM   1891 C  C    . LEU   A 1 261 ? 4.24500  -4.94000  19.05900 1.000 28.20141  ?  413 LEU   A C    1 
ATOM   1892 O  O    . LEU   A 1 261 ? 5.02200  -5.90200  19.05100 1.000 32.33759  ?  413 LEU   A O    1 
ATOM   1893 C  CB   . LEU   A 1 261 ? 3.90200  -3.56300  16.99100 1.000 37.47186  ?  413 LEU   A CB   1 
ATOM   1894 C  CG   . LEU   A 1 261 ? 5.25600  -3.84700  16.33000 1.000 43.04367  ?  413 LEU   A CG   1 
ATOM   1895 C  CD1  . LEU   A 1 261 ? 5.17600  -5.03000  15.36700 1.000 36.43665  ?  413 LEU   A CD1  1 
ATOM   1896 C  CD2  . LEU   A 1 261 ? 5.77300  -2.60600  15.62000 1.000 34.79017  ?  413 LEU   A CD2  1 
ATOM   1897 N  N    . VAL   A 1 262 ? 4.15900  -4.10100  20.09600 1.000 26.54119  ?  414 VAL   A N    1 
ATOM   1898 C  CA   . VAL   A 1 262 ? 4.98400  -4.29000  21.28700 1.000 24.81998  ?  414 VAL   A CA   1 
ATOM   1899 C  C    . VAL   A 1 262 ? 4.67600  -5.63000  21.94400 1.000 35.73991  ?  414 VAL   A C    1 
ATOM   1900 O  O    . VAL   A 1 262 ? 5.58600  -6.36100  22.35500 1.000 34.44684  ?  414 VAL   A O    1 
ATOM   1901 C  CB   . VAL   A 1 262 ? 4.78000  -3.11600  22.26400 1.000 33.94271  ?  414 VAL   A CB   1 
ATOM   1902 C  CG1  . VAL   A 1 262 ? 5.21800  -3.50200  23.67200 1.000 42.31327  ?  414 VAL   A CG1  1 
ATOM   1903 C  CG2  . VAL   A 1 262 ? 5.53900  -1.89000  21.78400 1.000 34.78930  ?  414 VAL   A CG2  1 
ATOM   1904 N  N    . LEU   A 1 263 ? 3.39100  -5.97600  22.04700 1.000 35.25455  ?  415 LEU   A N    1 
ATOM   1905 C  CA   . LEU   A 1 263 ? 3.00900  -7.25300  22.64100 1.000 31.13971  ?  415 LEU   A CA   1 
ATOM   1906 C  C    . LEU   A 1 263 ? 3.51100  -8.42600  21.80800 1.000 34.86001  ?  415 LEU   A C    1 
ATOM   1907 O  O    . LEU   A 1 263 ? 3.92600  -9.45200  22.35900 1.000 35.73662  ?  415 LEU   A O    1 
ATOM   1908 C  CB   . LEU   A 1 263 ? 1.48800  -7.31900  22.80300 1.000 32.13486  ?  415 LEU   A CB   1 
ATOM   1909 C  CG   . LEU   A 1 263 ? 0.91300  -6.43100  23.90500 1.000 32.76100  ?  415 LEU   A CG   1 
ATOM   1910 C  CD1  . LEU   A 1 263 ? -0.59800 -6.29600  23.77100 1.000 39.36432  ?  415 LEU   A CD1  1 
ATOM   1911 C  CD2  . LEU   A 1 263 ? 1.29300  -6.98400  25.27200 1.000 33.42786  ?  415 LEU   A CD2  1 
ATOM   1912 N  N    . GLU   A 1 264 ? 3.48100  -8.29400  20.48100 1.000 32.65135  ?  416 GLU   A N    1 
ATOM   1913 C  CA   . GLU   A 1 264 ? 3.99300  -9.35700  19.62100 1.000 39.07075  ?  416 GLU   A CA   1 
ATOM   1914 C  C    . GLU   A 1 264 ? 5.50200  -9.51200  19.77100 1.000 44.87306  ?  416 GLU   A C    1 
ATOM   1915 O  O    . GLU   A 1 264 ? 6.01200  -10.63000 19.90700 1.000 45.79411  ?  416 GLU   A O    1 
ATOM   1916 C  CB   . GLU   A 1 264 ? 3.63000  -9.07300  18.16400 1.000 35.71231  ?  416 GLU   A CB   1 
ATOM   1917 C  CG   . GLU   A 1 264 ? 3.87000  -10.24700 17.22700 1.000 47.65623  ?  416 GLU   A CG   1 
ATOM   1918 C  CD   . GLU   A 1 264 ? 3.62200  -9.89000  15.77600 1.000 53.27523  ?  416 GLU   A CD   1 
ATOM   1919 O  OE1  . GLU   A 1 264 ? 4.58100  -9.47200  15.09300 1.000 51.08569  ?  416 GLU   A OE1  1 
ATOM   1920 O  OE2  . GLU   A 1 264 ? 2.47000  -10.02500 15.31600 1.000 51.71801  ?  416 GLU   A OE2  1 
ATOM   1921 N  N    . VAL   A 1 265 ? 6.23500  -8.39800  19.74800 1.000 38.88882  ?  417 VAL   A N    1 
ATOM   1922 C  CA   . VAL   A 1 265 ? 7.69300  -8.46700  19.76000 1.000 41.04085  ?  417 VAL   A CA   1 
ATOM   1923 C  C    . VAL   A 1 265 ? 8.21000  -8.77300  21.15900 1.000 43.75129  ?  417 VAL   A C    1 
ATOM   1924 O  O    . VAL   A 1 265 ? 8.97000  -9.72700  21.36300 1.000 44.86910  ?  417 VAL   A O    1 
ATOM   1925 C  CB   . VAL   A 1 265 ? 8.29700  -7.16000  19.21300 1.000 43.02461  ?  417 VAL   A CB   1 
ATOM   1926 C  CG1  . VAL   A 1 265 ? 9.80400  -7.13600  19.44000 1.000 46.95848  ?  417 VAL   A CG1  1 
ATOM   1927 C  CG2  . VAL   A 1 265 ? 7.97000  -7.00200  17.73800 1.000 36.29486  ?  417 VAL   A CG2  1 
ATOM   1928 N  N    . PHE   A 1 266 ? 7.80800  -7.97100  22.14500 1.000 44.50395  ?  418 PHE   A N    1 
ATOM   1929 C  CA   . PHE   A 1 266 ? 8.37200  -8.11100  23.48200 1.000 45.62200  ?  418 PHE   A CA   1 
ATOM   1930 C  C    . PHE   A 1 266 ? 7.74500  -9.26200  24.26100 1.000 52.32375  ?  418 PHE   A C    1 
ATOM   1931 O  O    . PHE   A 1 266 ? 8.38900  -9.81300  25.16200 1.000 52.58906  ?  418 PHE   A O    1 
ATOM   1932 C  CB   . PHE   A 1 266 ? 8.22500  -6.79800  24.25300 1.000 48.15582  ?  418 PHE   A CB   1 
ATOM   1933 C  CG   . PHE   A 1 266 ? 9.11400  -5.69500  23.74700 1.000 41.77780  ?  418 PHE   A CG   1 
ATOM   1934 C  CD1  . PHE   A 1 266 ? 8.97600  -4.40300  24.22100 1.000 33.80394  ?  418 PHE   A CD1  1 
ATOM   1935 C  CD2  . PHE   A 1 266 ? 10.09100 -5.95500  22.79800 1.000 47.32406  ?  418 PHE   A CD2  1 
ATOM   1936 C  CE1  . PHE   A 1 266 ? 9.79700  -3.39200  23.76100 1.000 43.95537  ?  418 PHE   A CE1  1 
ATOM   1937 C  CE2  . PHE   A 1 266 ? 10.91100 -4.94600  22.33000 1.000 42.96005  ?  418 PHE   A CE2  1 
ATOM   1938 C  CZ   . PHE   A 1 266 ? 10.76500 -3.66300  22.81200 1.000 41.51529  ?  418 PHE   A CZ   1 
ATOM   1939 N  N    . GLY   A 1 267 ? 6.51600  -9.63700  23.94200 1.000 52.89066  ?  419 GLY   A N    1 
ATOM   1940 C  CA   . GLY   A 1 267 ? 5.87800  -10.78900 24.54800 1.000 52.17414  ?  419 GLY   A CA   1 
ATOM   1941 C  C    . GLY   A 1 267 ? 4.57800  -10.43200 25.24700 1.000 61.11155  ?  419 GLY   A C    1 
ATOM   1942 O  O    . GLY   A 1 267 ? 4.24500  -9.26900  25.47000 1.000 50.15864  ?  419 GLY   A O    1 
ATOM   1943 N  N    . ASN   A 1 268 ? 3.84700  -11.48800 25.59300 1.000 69.65916  ?  420 ASN   A N    1 
ATOM   1944 C  CA   . ASN   A 1 268 ? 2.56200  -11.37500 26.27300 1.000 75.40285  ?  420 ASN   A CA   1 
ATOM   1945 C  C    . ASN   A 1 268 ? 2.72200  -11.51700 27.78400 1.000 70.73235  ?  420 ASN   A C    1 
ATOM   1946 O  O    . ASN   A 1 268 ? 2.28400  -12.50700 28.37300 1.000 72.04573  ?  420 ASN   A O    1 
ATOM   1947 C  CB   . ASN   A 1 268 ? 1.58900  -12.43700 25.75400 1.000 83.91461  ?  420 ASN   A CB   1 
ATOM   1948 C  CG   . ASN   A 1 268 ? 0.85400  -11.99700 24.50500 1.000 95.03908  ?  420 ASN   A CG   1 
ATOM   1949 O  OD1  . ASN   A 1 268 ? 1.24700  -12.33200 23.38600 1.000 99.78696  ?  420 ASN   A OD1  1 
ATOM   1950 N  ND2  . ASN   A 1 268 ? -0.22300 -11.24300 24.68800 1.000 94.63157  ?  420 ASN   A ND2  1 
ATOM   1951 N  N    . LYS   B 2 1   ? 5.40000  -19.64700 18.17500 1.000 92.11549  ?  625 LYS   C N    1 
ATOM   1952 C  CA   . LYS   B 2 1   ? 4.29500  -18.70400 18.04400 1.000 94.47685  ?  625 LYS   C CA   1 
ATOM   1953 C  C    . LYS   B 2 1   ? 4.47900  -17.87400 16.77000 1.000 91.49774  ?  625 LYS   C C    1 
ATOM   1954 O  O    . LYS   B 2 1   ? 5.60400  -17.65200 16.31200 1.000 88.82161  ?  625 LYS   C O    1 
ATOM   1955 C  CB   . LYS   B 2 1   ? 4.21200  -17.81000 19.28400 1.000 93.64880  ?  625 LYS   C CB   1 
ATOM   1956 C  CG   . LYS   B 2 1   ? 3.29900  -16.59000 19.17800 1.000 87.08491  ?  625 LYS   C CG   1 
ATOM   1957 C  CD   . LYS   B 2 1   ? 4.09700  -15.29700 19.12100 1.000 86.17722  ?  625 LYS   C CD   1 
ATOM   1958 C  CE   . LYS   B 2 1   ? 4.60200  -14.89900 20.49700 1.000 85.58262  ?  625 LYS   C CE   1 
ATOM   1959 N  NZ   . LYS   B 2 1   ? 4.68800  -13.42100 20.64800 1.000 78.62891  ?  625 LYS   C NZ   1 
ATOM   1960 N  N    . ASN   B 2 2   ? 3.36700  -17.43500 16.18900 1.000 91.59756  ?  626 ASN   C N    1 
ATOM   1961 C  CA   . ASN   B 2 2   ? 3.37800  -16.67000 14.95000 1.000 89.88868  ?  626 ASN   C CA   1 
ATOM   1962 C  C    . ASN   B 2 2   ? 3.46400  -15.17600 15.23600 1.000 80.67505  ?  626 ASN   C C    1 
ATOM   1963 O  O    . ASN   B 2 2   ? 2.92800  -14.67900 16.23000 1.000 79.46007  ?  626 ASN   C O    1 
ATOM   1964 C  CB   . ASN   B 2 2   ? 2.12400  -16.97100 14.12900 1.000 93.84793  ?  626 ASN   C CB   1 
ATOM   1965 C  CG   . ASN   B 2 2   ? 2.18300  -18.32600 13.45900 1.000 100.47333 ?  626 ASN   C CG   1 
ATOM   1966 O  OD1  . ASN   B 2 2   ? 3.26300  -18.86800 13.23300 1.000 103.46770 ?  626 ASN   C OD1  1 
ATOM   1967 N  ND2  . ASN   B 2 2   ? 1.02000  -18.88200 13.13800 1.000 101.87196 ?  626 ASN   C ND2  1 
ATOM   1968 N  N    . HIS   B 2 3   ? 4.15000  -14.45900 14.34300 1.000 72.85153  ?  627 HIS   C N    1 
ATOM   1969 C  CA   . HIS   B 2 3   ? 4.37000  -13.01900 14.45400 1.000 61.43197  ?  627 HIS   C CA   1 
ATOM   1970 C  C    . HIS   B 2 3   ? 3.89300  -12.35600 13.16700 1.000 50.20368  ?  627 HIS   C C    1 
ATOM   1971 O  O    . HIS   B 2 3   ? 4.71000  -11.93500 12.33400 1.000 49.82747  ?  627 HIS   C O    1 
ATOM   1972 C  CB   . HIS   B 2 3   ? 5.84200  -12.70600 14.72100 1.000 63.77254  ?  627 HIS   C CB   1 
ATOM   1973 C  CG   . HIS   B 2 3   ? 6.40500  -13.42800 15.90700 1.000 65.26265  ?  627 HIS   C CG   1 
ATOM   1974 N  ND1  . HIS   B 2 3   ? 6.83900  -14.73500 15.84500 1.000 67.04255  ?  627 HIS   C ND1  1 
ATOM   1975 C  CD2  . HIS   B 2 3   ? 6.59500  -13.02900 17.18700 1.000 68.01973  ?  627 HIS   C CD2  1 
ATOM   1976 C  CE1  . HIS   B 2 3   ? 7.27600  -15.10900 17.03400 1.000 66.92430  ?  627 HIS   C CE1  1 
ATOM   1977 N  NE2  . HIS   B 2 3   ? 7.13600  -14.09300 17.86700 1.000 63.31124  ?  627 HIS   C NE2  1 
ATOM   1978 N  N    . PRO   B 2 4   ? 2.57500  -12.23700 12.97300 1.000 51.61814  ?  628 PRO   C N    1 
ATOM   1979 C  CA   . PRO   B 2 4   ? 2.07300  -11.68400 11.70400 1.000 52.05616  ?  628 PRO   C CA   1 
ATOM   1980 C  C    . PRO   B 2 4   ? 2.40600  -10.21800 11.49800 1.000 47.56766  ?  628 PRO   C C    1 
ATOM   1981 O  O    . PRO   B 2 4   ? 2.59300  -9.79800  10.35000 1.000 45.55234  ?  628 PRO   C O    1 
ATOM   1982 C  CB   . PRO   B 2 4   ? 0.55700  -11.90700 11.80100 1.000 52.22601  ?  628 PRO   C CB   1 
ATOM   1983 C  CG   . PRO   B 2 4   ? 0.27900  -11.99700 13.26600 1.000 44.41722  ?  628 PRO   C CG   1 
ATOM   1984 C  CD   . PRO   B 2 4   ? 1.48200  -12.66000 13.86600 1.000 54.39253  ?  628 PRO   C CD   1 
ATOM   1985 N  N    . MET   B 2 5   ? 2.47200  -9.41800  12.56500 1.000 43.65338  ?  629 MET   C N    1 
ATOM   1986 C  CA   . MET   B 2 5   ? 2.79700  -8.00600  12.39000 1.000 46.23795  ?  629 MET   C CA   1 
ATOM   1987 C  C    . MET   B 2 5   ? 4.27500  -7.81900  12.07700 1.000 48.03412  ?  629 MET   C C    1 
ATOM   1988 O  O    . MET   B 2 5   ? 4.63800  -6.98900  11.23400 1.000 42.31260  ?  629 MET   C O    1 
ATOM   1989 C  CB   . MET   B 2 5   ? 2.39800  -7.21600  13.63400 1.000 42.87164  ?  629 MET   C CB   1 
ATOM   1990 C  CG   . MET   B 2 5   ? 0.89100  -7.12200  13.83700 1.000 52.19976  ?  629 MET   C CG   1 
ATOM   1991 S  SD   . MET   B 2 5   ? 0.44700  -6.40400  15.42800 1.000 53.10105  ?  629 MET   C SD   1 
ATOM   1992 C  CE   . MET   B 2 5   ? 0.41000  -7.85900  16.47000 1.000 58.83597  ?  629 MET   C CE   1 
ATOM   1993 N  N    . LEU   B 2 6   ? 5.14100  -8.58300  12.74700 1.000 42.17695  ?  630 LEU   C N    1 
ATOM   1994 C  CA   . LEU   B 2 6   ? 6.56100  -8.57100  12.41300 1.000 44.88483  ?  630 LEU   C CA   1 
ATOM   1995 C  C    . LEU   B 2 6   ? 6.79000  -9.07100  10.99300 1.000 41.86780  ?  630 LEU   C C    1 
ATOM   1996 O  O    . LEU   B 2 6   ? 7.55900  -8.47200  10.23200 1.000 43.33900  ?  630 LEU   C O    1 
ATOM   1997 C  CB   . LEU   B 2 6   ? 7.33800  -9.42500  13.41600 1.000 45.95795  ?  630 LEU   C CB   1 
ATOM   1998 C  CG   . LEU   B 2 6   ? 8.40700  -8.73400  14.26200 1.000 62.19643  ?  630 LEU   C CG   1 
ATOM   1999 C  CD1  . LEU   B 2 6   ? 9.22400  -9.76100  15.03200 1.000 53.69804  ?  630 LEU   C CD1  1 
ATOM   2000 C  CD2  . LEU   B 2 6   ? 9.30400  -7.89100  13.38000 1.000 62.77489  ?  630 LEU   C CD2  1 
ATOM   2001 N  N    . MET   B 2 7   ? 6.12100  -10.16400 10.61700 1.000 57.35863  ?  631 MET   C N    1 
ATOM   2002 C  CA   . MET   B 2 7   ? 6.28300  -10.71700 9.27500  1.000 52.23828  ?  631 MET   C CA   1 
ATOM   2003 C  C    . MET   B 2 7   ? 5.82400  -9.73200  8.20700  1.000 49.22392  ?  631 MET   C C    1 
ATOM   2004 O  O    . MET   B 2 7   ? 6.41800  -9.65600  7.12400  1.000 50.85898  ?  631 MET   C O    1 
ATOM   2005 C  CB   . MET   B 2 7   ? 5.51000  -12.03000 9.15600  1.000 52.04554  ?  631 MET   C CB   1 
ATOM   2006 C  CG   . MET   B 2 7   ? 5.92200  -12.89200 7.97900  1.000 61.53006  ?  631 MET   C CG   1 
ATOM   2007 S  SD   . MET   B 2 7   ? 7.43600  -13.81600 8.30000  1.000 67.58675  ?  631 MET   C SD   1 
ATOM   2008 C  CE   . MET   B 2 7   ? 6.76600  -15.30100 9.04600  1.000 75.96777  ?  631 MET   C CE   1 
ATOM   2009 N  N    . ASN   B 2 8   ? 4.76700  -8.96700  8.49200  1.000 48.58425  ?  632 ASN   C N    1 
ATOM   2010 C  CA   . ASN   B 2 8   ? 4.25800  -8.01500  7.51000  1.000 47.41080  ?  632 ASN   C CA   1 
ATOM   2011 C  C    . ASN   B 2 8   ? 5.20800  -6.83800  7.33500  1.000 49.08296  ?  632 ASN   C C    1 
ATOM   2012 O  O    . ASN   B 2 8   ? 5.43100  -6.37700  6.20900  1.000 45.71078  ?  632 ASN   C O    1 
ATOM   2013 C  CB   . ASN   B 2 8   ? 2.87100  -7.52400  7.92200  1.000 44.10346  ?  632 ASN   C CB   1 
ATOM   2014 C  CG   . ASN   B 2 8   ? 2.32400  -6.46900  6.97900  1.000 57.75411  ?  632 ASN   C CG   1 
ATOM   2015 O  OD1  . ASN   B 2 8   ? 2.34600  -5.27600  7.28300  1.000 62.09353  ?  632 ASN   C OD1  1 
ATOM   2016 N  ND2  . ASN   B 2 8   ? 1.83300  -6.90500  5.82600  1.000 59.06112  ?  632 ASN   C ND2  1 
ATOM   2017 N  N    . LEU   B 2 9   ? 5.77000  -6.33200  8.43500  1.000 42.71591  ?  633 LEU   C N    1 
ATOM   2018 C  CA   . LEU   B 2 9   ? 6.73900  -5.24700  8.33100  1.000 41.64347  ?  633 LEU   C CA   1 
ATOM   2019 C  C    . LEU   B 2 9   ? 8.02200  -5.71000  7.65300  1.000 50.41570  ?  633 LEU   C C    1 
ATOM   2020 O  O    . LEU   B 2 9   ? 8.70100  -4.90800  7.00100  1.000 51.94586  ?  633 LEU   C O    1 
ATOM   2021 C  CB   . LEU   B 2 9   ? 7.03800  -4.67300  9.71600  1.000 41.27310  ?  633 LEU   C CB   1 
ATOM   2022 C  CG   . LEU   B 2 9   ? 5.87600  -3.92600  10.37500 1.000 49.30959  ?  633 LEU   C CG   1 
ATOM   2023 C  CD1  . LEU   B 2 9   ? 6.13700  -3.70200  11.86000 1.000 45.77009  ?  633 LEU   C CD1  1 
ATOM   2024 C  CD2  . LEU   B 2 9   ? 5.61400  -2.60700  9.66300  1.000 54.06375  ?  633 LEU   C CD2  1 
ATOM   2025 N  N    . LEU   B 2 10  ? 8.36700  -6.99100  7.79100  1.000 44.72301  ?  634 LEU   C N    1 
ATOM   2026 C  CA   . LEU   B 2 10  ? 9.48500  -7.56300  7.05100  1.000 50.36307  ?  634 LEU   C CA   1 
ATOM   2027 C  C    . LEU   B 2 10  ? 9.18400  -7.71600  5.56900  1.000 62.29108  ?  634 LEU   C C    1 
ATOM   2028 O  O    . LEU   B 2 10  ? 10.08200 -8.12300  4.82300  1.000 58.40151  ?  634 LEU   C O    1 
ATOM   2029 C  CB   . LEU   B 2 10  ? 9.86800  -8.92300  7.63900  1.000 46.58338  ?  634 LEU   C CB   1 
ATOM   2030 C  CG   . LEU   B 2 10  ? 10.76500 -8.91800  8.87900  1.000 54.30472  ?  634 LEU   C CG   1 
ATOM   2031 C  CD1  . LEU   B 2 10  ? 10.82400 -10.30500 9.50300  1.000 58.36374  ?  634 LEU   C CD1  1 
ATOM   2032 C  CD2  . LEU   B 2 10  ? 12.16100 -8.42600  8.52400  1.000 58.90112  ?  634 LEU   C CD2  1 
ATOM   2033 N  N    . LYS   B 2 11  ? 7.95900  -7.39300  5.14700  1.000 62.46786  ?  635 LYS   C N    1 
ATOM   2034 C  CA   . LYS   B 2 11  ? 7.47300  -7.52800  3.77100  1.000 73.02559  ?  635 LYS   C CA   1 
ATOM   2035 C  C    . LYS   B 2 11  ? 7.96800  -8.80100  3.09300  1.000 82.94693  ?  635 LYS   C C    1 
ATOM   2036 O  O    . LYS   B 2 11  ? 7.64700  -9.90600  3.53100  1.000 88.21289  ?  635 LYS   C O    1 
ATOM   2037 C  CB   . LYS   B 2 11  ? 7.85900  -6.30000  2.93500  1.000 74.73665  ?  635 LYS   C CB   1 
ATOM   2038 C  CG   . LYS   B 2 11  ? 9.32700  -6.20500  2.55600  1.000 78.42755  ?  635 LYS   C CG   1 
ATOM   2039 C  CD   . LYS   B 2 11  ? 9.50200  -5.85000  1.09300  1.000 82.64732  ?  635 LYS   C CD   1 
ATOM   2040 C  CE   . LYS   B 2 11  ? 10.87800 -6.25700  0.60000  1.000 78.45557  ?  635 LYS   C CE   1 
ATOM   2041 N  NZ   . LYS   B 2 11  ? 10.97900 -6.20800  -0.88400 1.000 74.84102  ?  635 LYS   C NZ   1 
HETATM 2042 C  C10  . A1L77 C 3 .   ? 15.76400 4.43000   25.80800 1.000 46.31999  ?  501 A1L77 A C10  1 
HETATM 2043 C  C13  . A1L77 C 3 .   ? 10.85200 2.62600   27.51000 1.000 45.69568  ?  501 A1L77 A C13  1 
HETATM 2044 C  C15  . A1L77 C 3 .   ? 11.64300 4.06000   25.76700 1.000 48.33773  ?  501 A1L77 A C15  1 
HETATM 2045 C  C17  . A1L77 C 3 .   ? 9.49300  0.78900   27.21300 1.000 50.22564  ?  501 A1L77 A C17  1 
HETATM 2046 C  C20  . A1L77 C 3 .   ? 7.05100  -0.64200  29.71100 1.000 48.03764  ?  501 A1L77 A C20  1 
HETATM 2047 C  C21  . A1L77 C 3 .   ? 7.80500  -0.95800  26.98300 1.000 49.25071  ?  501 A1L77 A C21  1 
HETATM 2048 C  C22  . A1L77 C 3 .   ? 6.98100  0.05800   26.25100 1.000 51.84981  ?  501 A1L77 A C22  1 
HETATM 2049 C  C24  . A1L77 C 3 .   ? 14.40300 7.52500   19.17400 1.000 60.81233  ?  501 A1L77 A C24  1 
HETATM 2050 C  C28  . A1L77 C 3 .   ? 13.72700 8.17700   15.87700 1.000 49.25398  ?  501 A1L77 A C28  1 
HETATM 2051 C  C01  . A1L77 C 3 .   ? 13.27000 5.44500   21.64600 1.000 37.14170  ?  501 A1L77 A C01  1 
HETATM 2052 C  C02  . A1L77 C 3 .   ? 13.54600 6.74100   21.29400 1.000 47.80954  ?  501 A1L77 A C02  1 
HETATM 2053 C  C03  . A1L77 C 3 .   ? 13.98400 7.55500   22.30100 1.000 48.41397  ?  501 A1L77 A C03  1 
HETATM 2054 C  C04  . A1L77 C 3 .   ? 14.13400 7.11400   23.58500 1.000 43.25286  ?  501 A1L77 A C04  1 
HETATM 2055 C  C05  . A1L77 C 3 .   ? 13.85600 5.83300   23.91600 1.000 42.58577  ?  501 A1L77 A C05  1 
HETATM 2056 C  C06  . A1L77 C 3 .   ? 13.42200 4.98700   22.93000 1.000 39.80301  ?  501 A1L77 A C06  1 
HETATM 2057 C  C09  . A1L77 C 3 .   ? 12.80500 4.24400   26.42900 1.000 46.97947  ?  501 A1L77 A C09  1 
HETATM 2058 C  C11  . A1L77 C 3 .   ? 12.98100 3.63300   27.63500 1.000 47.74565  ?  501 A1L77 A C11  1 
HETATM 2059 C  C12  . A1L77 C 3 .   ? 12.02400 2.83100   28.18800 1.000 45.52204  ?  501 A1L77 A C12  1 
HETATM 2060 C  C14  . A1L77 C 3 .   ? 10.68300 3.25500   26.32000 1.000 47.96578  ?  501 A1L77 A C14  1 
HETATM 2061 C  C18  . A1L77 C 3 .   ? 8.65700  -0.21400  27.96600 1.000 47.36506  ?  501 A1L77 A C18  1 
HETATM 2062 C  C19  . A1L77 C 3 .   ? 7.75200  0.45400   28.94300 1.000 46.37302  ?  501 A1L77 A C19  1 
HETATM 2063 C  C25  . A1L77 C 3 .   ? 14.34000 6.81400   17.83500 1.000 62.87377  ?  501 A1L77 A C25  1 
HETATM 2064 C  C27  . A1L77 C 3 .   ? 13.20500 7.28600   16.97200 1.000 51.69229  ?  501 A1L77 A C27  1 
HETATM 2065 C  C29  . A1L77 C 3 .   ? 13.29600 7.69000   14.52700 1.000 49.58009  ?  501 A1L77 A C29  1 
HETATM 2066 C  C32  . A1L77 C 3 .   ? 14.31700 8.98800   22.04500 1.000 54.82151  ?  501 A1L77 A C32  1 
HETATM 2067 C  C33  . A1L77 C 3 .   ? 12.32300 2.15900   29.51300 1.000 46.82054  ?  501 A1L77 A C33  1 
HETATM 2068 C  C34  . A1L77 C 3 .   ? 14.55700 6.86000   26.58500 1.000 56.48800  ?  501 A1L77 A C34  1 
HETATM 2069 C  C35  . A1L77 C 3 .   ? 13.59000 7.12500   27.67700 1.000 60.80788  ?  501 A1L77 A C35  1 
HETATM 2070 C  C36  . A1L77 C 3 .   ? 12.35200 7.62700   27.01800 1.000 63.84928  ?  501 A1L77 A C36  1 
HETATM 2071 C  C37  . A1L77 C 3 .   ? 11.63700 8.30900   28.16400 1.000 61.92335  ?  501 A1L77 A C37  1 
HETATM 2072 C  C38  . A1L77 C 3 .   ? 15.64700 3.01100   25.39800 1.000 49.12408  ?  501 A1L77 A C38  1 
HETATM 2073 C  C39  . A1L77 C 3 .   ? 15.75400 2.21700   26.66400 1.000 49.24591  ?  501 A1L77 A C39  1 
HETATM 2074 C  C40  . A1L77 C 3 .   ? 15.12100 0.87800   26.48400 1.000 43.10241  ?  501 A1L77 A C40  1 
HETATM 2075 O  O07  . A1L77 C 3 .   ? 13.34900 7.19100   19.97800 1.000 60.93012  ?  501 A1L77 A O07  1 
HETATM 2076 O  O16  . A1L77 C 3 .   ? 9.86200  1.82300   28.01700 1.000 49.79799  ?  501 A1L77 A O16  1 
HETATM 2077 O  O23  . A1L77 C 3 .   ? 9.39200  -1.14500  28.60000 1.000 40.71689  ?  501 A1L77 A O23  1 
HETATM 2078 O  O26  . A1L77 C 3 .   ? 14.14900 5.45800   18.03300 1.000 68.82782  ?  501 A1L77 A O26  1 
HETATM 2079 O  O30  . A1L77 C 3 .   ? 13.43500 6.52000   14.28700 1.000 46.88800  ?  501 A1L77 A O30  1 
HETATM 2080 O  O31  . A1L77 C 3 .   ? 12.83600 8.45900   13.68800 1.000 44.07527  -1 501 A1L77 A O31  1 
HETATM 2081 SI SI08 . A1L77 C 3 .   ? 14.14000 5.30600   25.69700 1.000 46.74620  ?  501 A1L77 A SI08 1 
HETATM 2082 O  O    . HOH   D 4 .   ? 22.48100 -4.00500  32.96500 1.000 54.67446  ?  601 HOH   A O    1 
HETATM 2083 O  O    . HOH   D 4 .   ? 15.56600 -0.25300  41.44900 1.000 88.15452  ?  602 HOH   A O    1 
HETATM 2084 O  O    . HOH   D 4 .   ? 13.75400 -6.75600  26.75600 1.000 47.60636  ?  603 HOH   A O    1 
HETATM 2085 O  O    . HOH   D 4 .   ? 39.43500 4.98200   22.62900 1.000 56.20740  ?  604 HOH   A O    1 
HETATM 2086 O  O    A HOH   D 4 .   ? 11.53400 -19.59500 6.76700  0.540 51.61137  ?  605 HOH   A O    1 
HETATM 2087 O  O    B HOH   D 4 .   ? 9.40600  -19.91500 6.88700  0.460 47.91531  ?  605 HOH   A O    1 
HETATM 2088 O  O    . HOH   D 4 .   ? 19.38700 -7.42700  3.31200  1.000 48.08942  ?  606 HOH   A O    1 
HETATM 2089 O  O    . HOH   D 4 .   ? 11.70300 10.60000  14.28800 1.000 56.61887  ?  607 HOH   A O    1 
HETATM 2090 O  O    . HOH   D 4 .   ? 31.42200 -11.44600 13.92300 1.000 53.85245  ?  608 HOH   A O    1 
HETATM 2091 O  O    . HOH   D 4 .   ? 18.43900 -18.29300 8.11000  1.000 43.37636  ?  609 HOH   A O    1 
HETATM 2092 O  O    . HOH   D 4 .   ? 21.98300 -24.15600 11.42100 1.000 111.40835 ?  610 HOH   A O    1 
HETATM 2093 O  O    . HOH   D 4 .   ? 29.90000 10.32300  7.16000  1.000 74.16050  ?  611 HOH   A O    1 
HETATM 2094 O  O    . HOH   D 4 .   ? 24.34100 -6.96000  21.63600 1.000 28.00136  ?  612 HOH   A O    1 
HETATM 2095 O  O    . HOH   D 4 .   ? 43.18000 4.24000   12.84600 1.000 46.39230  ?  613 HOH   A O    1 
HETATM 2096 O  O    A HOH   D 4 .   ? 18.01200 2.21100   1.08300  0.440 62.52707  ?  614 HOH   A O    1 
HETATM 2097 O  O    B HOH   D 4 .   ? 19.52800 -0.15600  1.09200  0.560 82.79970  ?  614 HOH   A O    1 
HETATM 2098 O  O    . HOH   D 4 .   ? 24.25600 -11.35000 29.71900 1.000 69.95404  ?  615 HOH   A O    1 
HETATM 2099 O  O    . HOH   D 4 .   ? 17.80200 11.93900  33.41100 1.000 57.52906  ?  616 HOH   A O    1 
HETATM 2100 O  O    . HOH   D 4 .   ? 19.27200 -20.31100 6.69500  1.000 56.74176  ?  617 HOH   A O    1 
HETATM 2101 O  O    . HOH   D 4 .   ? -0.89700 13.29100  20.34100 1.000 71.26452  ?  618 HOH   A O    1 
HETATM 2102 O  O    . HOH   D 4 .   ? 1.52600  8.75200   28.43400 1.000 40.67970  ?  619 HOH   A O    1 
HETATM 2103 O  O    . HOH   D 4 .   ? 18.03200 3.66800   11.85700 1.000 36.05790  ?  620 HOH   A O    1 
HETATM 2104 O  O    . HOH   D 4 .   ? 25.08900 -8.93100  20.56600 1.000 47.70284  ?  621 HOH   A O    1 
HETATM 2105 O  O    . HOH   D 4 .   ? 15.15100 21.47700  22.92000 1.000 69.52595  ?  622 HOH   A O    1 
HETATM 2106 O  O    . HOH   D 4 .   ? 29.09400 7.83800   20.23900 1.000 38.97846  ?  623 HOH   A O    1 
HETATM 2107 O  O    . HOH   D 4 .   ? 33.10300 5.01900   26.94400 1.000 47.05534  ?  624 HOH   A O    1 
HETATM 2108 O  O    . HOH   D 4 .   ? 2.39200  12.63800  21.37400 1.000 50.55929  ?  625 HOH   A O    1 
HETATM 2109 O  O    A HOH   D 4 .   ? -4.28000 5.02900   26.12200 0.720 53.77188  ?  626 HOH   A O    1 
HETATM 2110 O  O    B HOH   D 4 .   ? -5.47400 4.04000   25.37900 0.280 58.74457  ?  626 HOH   A O    1 
HETATM 2111 O  O    . HOH   D 4 .   ? 32.94900 -0.01400  26.21100 1.000 47.03355  ?  627 HOH   A O    1 
HETATM 2112 O  O    . HOH   D 4 .   ? 15.20200 -6.31900  38.84900 1.000 93.65781  ?  628 HOH   A O    1 
HETATM 2113 O  O    . HOH   D 4 .   ? 18.32700 1.73900   13.81100 1.000 44.70384  ?  629 HOH   A O    1 
HETATM 2114 O  O    . HOH   D 4 .   ? 9.33900  11.68600  12.93500 1.000 49.55584  ?  630 HOH   A O    1 
HETATM 2115 O  O    . HOH   D 4 .   ? 13.84800 -6.76000  21.89300 1.000 44.24577  ?  631 HOH   A O    1 
HETATM 2116 O  O    . HOH   D 4 .   ? 14.12200 1.58900   41.67200 1.000 58.81785  ?  632 HOH   A O    1 
HETATM 2117 O  O    . HOH   D 4 .   ? 1.81100  1.45400   14.05200 1.000 73.25721  ?  633 HOH   A O    1 
HETATM 2118 O  O    . HOH   D 4 .   ? -1.19600 2.73400   20.11200 1.000 41.81784  ?  634 HOH   A O    1 
HETATM 2119 O  O    . HOH   D 4 .   ? -6.431   -1.732    25.114   1.000 28.05024  ?  635 HOH   A O    1 
HETATM 2120 O  O    . HOH   D 4 .   ? 40.81900 11.06700  17.72500 1.000 54.12558  ?  636 HOH   A O    1 
HETATM 2121 O  O    . HOH   D 4 .   ? -1.59100 7.68400   15.53700 1.000 53.39834  ?  637 HOH   A O    1 
HETATM 2122 O  O    . HOH   D 4 .   ? 32.80500 10.30300  9.37300  1.000 74.57977  ?  638 HOH   A O    1 
HETATM 2123 O  O    . HOH   D 4 .   ? 44.56000 3.66800   14.67600 1.000 64.83387  ?  639 HOH   A O    1 
HETATM 2124 O  O    . HOH   D 4 .   ? 21.27800 -8.59700  32.99800 1.000 54.19590  ?  640 HOH   A O    1 
HETATM 2125 O  O    . HOH   D 4 .   ? 10.27900 -10.60700 36.07300 1.000 71.95729  ?  641 HOH   A O    1 
HETATM 2126 O  O    . HOH   D 4 .   ? 10.80600 -9.34800  26.79200 1.000 48.17671  ?  642 HOH   A O    1 
HETATM 2127 O  O    . HOH   D 4 .   ? 18.83600 10.81200  9.58900  1.000 63.00265  ?  643 HOH   A O    1 
HETATM 2128 O  O    . HOH   D 4 .   ? 40.23000 -0.99900  17.45900 1.000 40.74658  ?  644 HOH   A O    1 
HETATM 2129 O  O    . HOH   D 4 .   ? -0.91300 14.64700  13.31400 1.000 71.93543  ?  645 HOH   A O    1 
HETATM 2130 O  O    . HOH   D 4 .   ? 18.96800 -19.31700 4.35000  1.000 50.92712  ?  646 HOH   A O    1 
HETATM 2131 O  O    . HOH   D 4 .   ? 37.52500 11.47000  14.86900 1.000 57.89323  ?  647 HOH   A O    1 
HETATM 2132 O  O    . HOH   D 4 .   ? 37.98900 10.27700  8.53000  1.000 59.04513  ?  648 HOH   A O    1 
HETATM 2133 O  O    . HOH   D 4 .   ? 44.12200 0.00200   19.27900 1.000 60.74167  ?  649 HOH   A O    1 
HETATM 2134 O  O    . HOH   D 4 .   ? 30.88600 -21.26400 15.35600 1.000 82.80001  ?  650 HOH   A O    1 
HETATM 2135 O  O    . HOH   D 4 .   ? 10.81200 15.36300  31.58300 1.000 68.90191  ?  651 HOH   A O    1 
HETATM 2136 O  O    . HOH   D 4 .   ? 25.27700 9.45700   19.26000 1.000 58.38158  ?  652 HOH   A O    1 
HETATM 2137 O  O    . HOH   D 4 .   ? 30.12700 -13.89200 17.17700 1.000 59.54472  ?  653 HOH   A O    1 
HETATM 2138 O  O    . HOH   D 4 .   ? 40.34300 -2.89000  19.63100 1.000 43.71894  ?  654 HOH   A O    1 
HETATM 2139 O  O    A HOH   D 4 .   ? 39.89900 -2.08800  15.23600 0.430 25.80333  ?  655 HOH   A O    1 
HETATM 2140 O  O    B HOH   D 4 .   ? 40.20800 -5.12600  15.55500 0.570 63.45213  ?  655 HOH   A O    1 
HETATM 2141 O  O    . HOH   D 4 .   ? 24.74700 -22.30300 6.43400  1.000 64.33645  ?  656 HOH   A O    1 
HETATM 2142 O  O    . HOH   D 4 .   ? 29.11600 10.88000  20.37600 1.000 56.37411  ?  657 HOH   A O    1 
HETATM 2143 O  O    . HOH   D 4 .   ? -3.571   0.730     23.353   1.000 49.65471  ?  658 HOH   A O    1 
HETATM 2144 O  O    . HOH   D 4 .   ? 42.88000 8.08600   9.45700  1.000 65.07937  ?  659 HOH   A O    1 
HETATM 2145 O  O    . HOH   D 4 .   ? 3.08900  4.15500   17.65300 1.000 49.41282  ?  660 HOH   A O    1 
HETATM 2146 O  O    . HOH   D 4 .   ? 26.14000 15.63500  24.66000 1.000 72.94743  ?  661 HOH   A O    1 
HETATM 2147 O  O    . HOH   D 4 .   ? 29.96000 11.47700  11.96000 1.000 57.67666  ?  662 HOH   A O    1 
HETATM 2148 O  O    . HOH   D 4 .   ? 25.83900 -0.47900  31.58300 1.000 56.17839  ?  663 HOH   A O    1 
HETATM 2149 O  O    . HOH   D 4 .   ? 34.64900 -8.04400  5.41800  1.000 50.89093  ?  664 HOH   A O    1 
HETATM 2150 O  O    . HOH   D 4 .   ? 6.63300  -1.05800  38.93000 1.000 82.43078  ?  665 HOH   A O    1 
HETATM 2151 O  O    . HOH   D 4 .   ? 26.99200 6.83800   19.03400 1.000 54.19387  ?  666 HOH   A O    1 
HETATM 2152 O  O    . HOH   D 4 .   ? 8.76300  -22.76100 11.67200 1.000 71.00718  ?  667 HOH   A O    1 
HETATM 2153 O  O    . HOH   D 4 .   ? 12.98200 -22.73400 16.31600 1.000 65.90805  ?  668 HOH   A O    1 
HETATM 2154 O  O    . HOH   D 4 .   ? 12.28100 7.96000   8.94400  1.000 69.25762  ?  669 HOH   A O    1 
HETATM 2155 O  O    . HOH   D 4 .   ? -2.53200 -12.12400 34.21300 1.000 73.12678  ?  670 HOH   A O    1 
HETATM 2156 O  O    . HOH   D 4 .   ? 7.27600  -13.51700 23.22000 1.000 60.33007  ?  671 HOH   A O    1 
HETATM 2157 O  O    . HOH   D 4 .   ? 42.75200 0.14700   17.10000 1.000 58.26337  ?  672 HOH   A O    1 
HETATM 2158 O  O    . HOH   D 4 .   ? 35.01200 11.54900  15.99500 1.000 69.51585  ?  673 HOH   A O    1 
HETATM 2159 O  O    . HOH   D 4 .   ? 24.69800 12.96300  7.65400  1.000 81.70291  ?  674 HOH   A O    1 
HETATM 2160 O  O    A HOH   D 4 .   ? -0.92500 -13.46800 29.03700 0.440 58.50534  ?  675 HOH   A O    1 
HETATM 2161 O  O    B HOH   D 4 .   ? -2.37200 -14.27600 27.95800 0.560 56.39742  ?  675 HOH   A O    1 
HETATM 2162 O  O    . HOH   D 4 .   ? 31.46900 6.27600   31.15900 1.000 65.66545  ?  676 HOH   A O    1 
HETATM 2163 O  O    . HOH   D 4 .   ? 48.71800 -5.73500  5.98100  1.000 68.35158  ?  677 HOH   A O    1 
HETATM 2164 O  O    . HOH   D 4 .   ? 7.10800  -3.57600  38.16200 1.000 69.02875  ?  678 HOH   A O    1 
HETATM 2165 O  O    A HOH   D 4 .   ? 17.74400 12.04900  7.83500  0.660 45.04437  ?  679 HOH   A O    1 
HETATM 2166 O  O    B HOH   D 4 .   ? 19.09000 11.89600  6.43600  0.340 43.63493  ?  679 HOH   A O    1 
HETATM 2167 O  O    . HOH   D 4 .   ? 21.17500 11.42400  11.21200 1.000 59.73201  ?  680 HOH   A O    1 
HETATM 2168 O  O    . HOH   D 4 .   ? 45.24400 5.27400   6.30000  1.000 71.39703  ?  681 HOH   A O    1 
HETATM 2169 O  O    . HOH   D 4 .   ? 25.50900 -2.75600  31.54900 1.000 64.64722  ?  682 HOH   A O    1 
HETATM 2170 O  O    A HOH   D 4 .   ? 0.54700  3.59400   17.58400 0.850 67.23403  ?  683 HOH   A O    1 
HETATM 2171 O  O    B HOH   D 4 .   ? -1.77500 4.77400   16.12600 0.150 48.77579  ?  683 HOH   A O    1 
HETATM 2172 O  O    . HOH   D 4 .   ? -1.87200 -9.98500  30.05500 1.000 60.82467  ?  684 HOH   A O    1 
HETATM 2173 O  O    . HOH   D 4 .   ? 9.39700  -3.75200  37.63900 1.000 66.71871  ?  685 HOH   A O    1 
HETATM 2174 O  O    . HOH   D 4 .   ? 13.03700 -8.13100  24.13000 1.000 65.80619  ?  686 HOH   A O    1 
HETATM 2175 O  O    . HOH   D 4 .   ? 31.68700 12.98100  18.44100 1.000 72.43711  ?  687 HOH   A O    1 
HETATM 2176 O  O    . HOH   D 4 .   ? 46.96400 1.41700   10.47700 1.000 65.96071  ?  688 HOH   A O    1 
HETATM 2177 O  O    . HOH   D 4 .   ? -1.30900 -11.81000 31.35900 1.000 60.69517  ?  689 HOH   A O    1 
HETATM 2178 O  O    . HOH   D 4 .   ? 24.00600 -8.99800  34.05500 1.000 80.20654  ?  690 HOH   A O    1 
HETATM 2179 O  O    . HOH   D 4 .   ? 19.86100 -7.92100  0.72200  1.000 80.52452  ?  691 HOH   A O    1 
HETATM 2180 O  O    . HOH   D 4 .   ? 47.81900 0.08400   4.67600  1.000 74.40646  ?  692 HOH   A O    1 
HETATM 2181 O  O    . HOH   E 4 .   ? 1.66600  -11.27000 7.75600  1.000 43.17790  ?  701 HOH   C O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N    . LYS   A 18  ? 0.75894 1.30799 0.84812 -0.13684 0.10551  -0.21482 123 LYS   A N    
2    C  CA   . LYS   A 18  ? 0.70410 1.22496 0.82335 -0.11781 0.09809  -0.22417 123 LYS   A CA   
3    C  C    . LYS   A 18  ? 0.58313 1.06689 0.68590 -0.11107 0.09193  -0.21766 123 LYS   A C    
4    O  O    . LYS   A 18  ? 0.53712 1.01502 0.66264 -0.09685 0.08953  -0.23433 123 LYS   A O    
5    C  CB   . LYS   A 18  ? 0.74358 1.23860 0.87490 -0.11603 0.09092  -0.20935 123 LYS   A CB   
6    C  CG   . LYS   A 18  ? 0.76487 1.25794 0.94165 -0.09865 0.08637  -0.22439 123 LYS   A CG   
7    C  CD   . LYS   A 18  ? 0.90096 1.43638 1.10727 -0.09976 0.09195  -0.23818 123 LYS   A CD   
8    C  CE   . LYS   A 18  ? 0.88899 1.41842 1.14235 -0.08267 0.08530  -0.24767 123 LYS   A CE   
9    N  NZ   . LYS   A 18  ? 0.77546 1.28075 1.02921 -0.08489 0.07657  -0.22543 123 LYS   A NZ   
10   N  N    . LEU   A 19  ? 0.56908 1.02780 0.63444 -0.12137 0.08914  -0.19341 124 LEU   A N    
11   C  CA   . LEU   A 19  ? 0.64076 1.06875 0.68757 -0.11657 0.08401  -0.18603 124 LEU   A CA   
12   C  C    . LEU   A 19  ? 0.55601 1.01794 0.59512 -0.11848 0.09029  -0.20204 124 LEU   A C    
13   O  O    . LEU   A 19  ? 0.72694 1.20907 0.73794 -0.13246 0.09473  -0.19260 124 LEU   A O    
14   C  CB   . LEU   A 19  ? 0.66594 1.06053 0.67812 -0.12694 0.07955  -0.15656 124 LEU   A CB   
15   C  CG   . LEU   A 19  ? 0.63630 0.98601 0.63615 -0.11901 0.07146  -0.14478 124 LEU   A CG   
16   C  CD1  . LEU   A 19  ? 0.57640 0.90823 0.60598 -0.10202 0.06616  -0.15688 124 LEU   A CD1  
17   C  CD2  . LEU   A 19  ? 0.68431 0.99879 0.66148 -0.12706 0.06663  -0.11888 124 LEU   A CD2  
18   N  N    . SER   A 20  ? 0.45901 0.92869 0.52406 -0.10509 0.09032  -0.22620 125 SER   A N    
19   C  CA   . SER   A 20  ? 0.47764 0.98271 0.53814 -0.10648 0.09624  -0.24573 125 SER   A CA   
20   C  C    . SER   A 20  ? 0.56477 1.05302 0.58845 -0.11239 0.09273  -0.22788 125 SER   A C    
21   O  O    . SER   A 20  ? 0.56123 1.00499 0.57084 -0.11049 0.08498  -0.20561 125 SER   A O    
22   C  CB   . SER   A 20  ? 0.43064 0.94009 0.52952 -0.09019 0.09553  -0.27551 125 SER   A CB   
23   O  OG   . SER   A 20  ? 0.47026 0.94074 0.56664 -0.08129 0.08732  -0.26950 125 SER   A OG   
24   N  N    . GLU   A 21  ? 0.54738 1.07470 0.55597 -0.11980 0.09853  -0.23818 126 GLU   A N    
25   C  CA   . GLU   A 21  ? 0.61973 1.13673 0.59474 -0.12562 0.09481  -0.22095 126 GLU   A CA   
26   C  C    . GLU   A 21  ? 0.52488 1.01303 0.50910 -0.11187 0.08790  -0.22837 126 GLU   A C    
27   O  O    . GLU   A 21  ? 0.54269 1.00539 0.50329 -0.11317 0.08192  -0.20872 126 GLU   A O    
28   C  CB   . GLU   A 21  ? 0.75768 1.31567 0.72109 -0.13695 0.09566  -0.22119 126 GLU   A CB   
29   C  CG   . GLU   A 21  ? 0.95375 1.52573 0.89431 -0.15406 0.09792  -0.19774 126 GLU   A CG   
30   C  CD   . GLU   A 21  ? 1.14229 1.76015 1.07739 -0.16507 0.09870  -0.20066 126 GLU   A CD   
31   O  OE1  . GLU   A 21  ? 1.21574 1.86344 1.16000 -0.17207 0.10277  -0.20715 126 GLU   A OE1  
32   O  OE2  . GLU   A 21  ? 1.16722 1.79302 1.08906 -0.16704 0.09505  -0.19635 126 GLU   A OE2  
33   N  N    . GLU   A 22  ? 0.50336 0.99511 0.52341 -0.09886 0.08833  -0.25593 127 GLU   A N    
34   C  CA   . GLU   A 22  ? 0.42080 0.87771 0.45439 -0.08574 0.08065  -0.25964 127 GLU   A CA   
35   C  C    . GLU   A 22  ? 0.42149 0.82529 0.45160 -0.08116 0.07242  -0.23335 127 GLU   A C    
36   O  O    . GLU   A 22  ? 0.44277 0.81534 0.46416 -0.07624 0.06569  -0.22244 127 GLU   A O    
37   C  CB   . GLU   A 22  ? 0.49884 0.96784 0.57674 -0.07325 0.08226  -0.29291 127 GLU   A CB   
38   C  CG   . GLU   A 22  ? 0.74014 1.16599 0.84194 -0.05916 0.07339  -0.29266 127 GLU   A CG   
39   C  CD   . GLU   A 22  ? 0.88681 1.32666 1.02471 -0.04939 0.07361  -0.32525 127 GLU   A CD   
40   O  OE1  . GLU   A 22  ? 0.96755 1.43970 1.10469 -0.05518 0.07477  -0.33685 127 GLU   A OE1  
41   O  OE2  . GLU   A 22  ? 0.88484 1.29689 1.05517 -0.03734 0.06805  -0.33038 127 GLU   A OE2  
42   N  N    . GLN   A 23  ? 0.41371 0.80956 0.44994 -0.08339 0.07304  -0.22345 128 GLN   A N    
43   C  CA   . GLN   A 23  ? 0.43736 0.78742 0.46982 -0.08026 0.06571  -0.20032 128 GLN   A CA   
44   C  C    . GLN   A 23  ? 0.52344 0.85523 0.51706 -0.09066 0.06360  -0.17256 128 GLN   A C    
45   O  O    . GLN   A 23  ? 0.48604 0.77952 0.47060 -0.08642 0.05687  -0.15664 128 GLN   A O    
46   C  CB   . GLN   A 23  ? 0.49624 0.84739 0.54992 -0.07956 0.06660  -0.20062 128 GLN   A CB   
47   C  CG   . GLN   A 23  ? 0.46791 0.82183 0.56547 -0.06590 0.06504  -0.22179 128 GLN   A CG   
48   C  CD   . GLN   A 23  ? 0.44759 0.81335 0.56788 -0.06589 0.06668  -0.22415 128 GLN   A CD   
49   O  OE1  . GLN   A 23  ? 0.41033 0.79648 0.51621 -0.07724 0.07190  -0.21827 128 GLN   A OE1  
50   N  NE2  . GLN   A 23  ? 0.41975 0.77382 0.57712 -0.05356 0.06172  -0.23163 128 GLN   A NE2  
51   N  N    . GLN   A 24  ? 0.47807 0.83729 0.45020 -0.10441 0.06915  -0.16613 129 GLN   A N    
52   C  CA   . GLN   A 24  ? 0.53494 0.87779 0.47293 -0.11433 0.06652  -0.13955 129 GLN   A CA   
53   C  C    . GLN   A 24  ? 0.52002 0.85365 0.44449 -0.10999 0.06230  -0.13670 129 GLN   A C    
54   O  O    . GLN   A 24  ? 0.52332 0.82438 0.43006 -0.11012 0.05652  -0.11564 129 GLN   A O    
55   C  CB   . GLN   A 24  ? 0.54671 0.92574 0.46672 -0.13089 0.07311  -0.13298 129 GLN   A CB   
56   C  CG   . GLN   A 24  ? 0.60847 0.99681 0.53872 -0.13756 0.07709  -0.13210 129 GLN   A CG   
57   C  CD   . GLN   A 24  ? 0.73876 1.17426 0.65693 -0.15351 0.08519  -0.13192 129 GLN   A CD   
58   O  OE1  . GLN   A 24  ? 0.73311 1.17448 0.62391 -0.16557 0.08503  -0.11306 129 GLN   A OE1  
59   N  NE2  . GLN   A 24  ? 0.76894 1.23990 0.70881 -0.15383 0.09214  -0.15210 129 GLN   A NE2  
60   N  N    . HIS   A 25  ? 0.43488 0.79838 0.36892 -0.10612 0.06509  -0.15896 130 HIS   A N    
61   C  CA   . HIS   A 25  ? 0.50917 0.86742 0.43322 -0.10179 0.06076  -0.15888 130 HIS   A CA   
62   C  C    . HIS   A 25  ? 0.50930 0.82206 0.44478 -0.08891 0.05317  -0.15410 130 HIS   A C    
63   O  O    . HIS   A 25  ? 0.56376 0.85403 0.48254 -0.08750 0.04768  -0.13824 130 HIS   A O    
64   C  CB   . HIS   A 25  ? 0.54874 0.94949 0.48560 -0.10011 0.06549  -0.18842 130 HIS   A CB   
65   C  CG   . HIS   A 25  ? 0.55256 0.95692 0.47745 -0.09819 0.06152  -0.18976 130 HIS   A CG   
66   N  ND1  . HIS   A 25  ? 0.62499 1.02874 0.51805 -0.10627 0.05824  -0.16619 130 HIS   A ND1  
67   C  CD2  . HIS   A 25  ? 0.61643 1.02632 0.55866 -0.08948 0.05985  -0.21183 130 HIS   A CD2  
68   C  CE1  . HIS   A 25  ? 0.63472 1.04503 0.52499 -0.10237 0.05466  -0.17345 130 HIS   A CE1  
69   N  NE2  . HIS   A 25  ? 0.62312 1.03722 0.54244 -0.09266 0.05576  -0.20166 130 HIS   A NE2  
70   N  N    . ILE   A 26  ? 0.44715 0.74762 0.41209 -0.07962 0.05257  -0.16668 131 ILE   A N    
71   C  CA   . ILE   A 26  ? 0.44405 0.70492 0.42114 -0.06851 0.04553  -0.16132 131 ILE   A CA   
72   C  C    . ILE   A 26  ? 0.38969 0.61545 0.34574 -0.07137 0.04131  -0.13402 131 ILE   A C    
73   O  O    . ILE   A 26  ? 0.40998 0.60933 0.35818 -0.06639 0.03592  -0.12340 131 ILE   A O    
74   C  CB   . ILE   A 26  ? 0.51946 0.77666 0.53290 -0.05975 0.04525  -0.17634 131 ILE   A CB   
75   C  CG1  . ILE   A 26  ? 0.48897 0.77342 0.52864 -0.05406 0.04788  -0.20549 131 ILE   A CG1  
76   C  CG2  . ILE   A 26  ? 0.51757 0.73428 0.53983 -0.05128 0.03791  -0.16416 131 ILE   A CG2  
77   C  CD1  . ILE   A 26  ? 0.56355 0.85675 0.64064 -0.04787 0.04960  -0.22235 131 ILE   A CD1  
78   N  N    . ILE   A 27  ? 0.38829 0.61446 0.33642 -0.07961 0.04387  -0.12365 132 ILE   A N    
79   C  CA   . ILE   A 27  ? 0.51192 0.70482 0.44304 -0.08285 0.04013  -0.10064 132 ILE   A CA   
80   C  C    . ILE   A 27  ? 0.55436 0.73929 0.45852 -0.08726 0.03784  -0.08435 132 ILE   A C    
81   O  O    . ILE   A 27  ? 0.55526 0.70769 0.45077 -0.08365 0.03285  -0.07027 132 ILE   A O    
82   C  CB   . ILE   A 27  ? 0.51439 0.71336 0.44392 -0.09249 0.04353  -0.09476 132 ILE   A CB   
83   C  CG1  . ILE   A 27  ? 0.47214 0.67094 0.42989 -0.08613 0.04337  -0.10642 132 ILE   A CG1  
84   C  CG2  . ILE   A 27  ? 0.44133 0.61018 0.35024 -0.09878 0.04036  -0.07202 132 ILE   A CG2  
85   C  CD1  . ILE   A 27  ? 0.54363 0.75955 0.50507 -0.09529 0.04756  -0.10604 132 ILE   A CD1  
86   N  N    . ALA   A 28  ? 0.45341 0.66992 0.34505 -0.09495 0.04124  -0.08609 133 ALA   A N    
87   C  CA   . ALA   A 28  ? 0.53036 0.74253 0.39756 -0.09975 0.03817  -0.06806 133 ALA   A CA   
88   C  C    . ALA   A 28  ? 0.45777 0.65677 0.32645 -0.08911 0.03292  -0.07034 133 ALA   A C    
89   O  O    . ALA   A 28  ? 0.44544 0.62178 0.30026 -0.08794 0.02793  -0.05264 133 ALA   A O    
90   C  CB   . ALA   A 28  ? 0.50503 0.76004 0.35856 -0.11176 0.04284  -0.06857 133 ALA   A CB   
91   N  N    . ILE   A 29  ? 0.46498 0.67829 0.35241 -0.08135 0.03379  -0.09233 134 ILE   A N    
92   C  CA   . ILE   A 29  ? 0.48277 0.68416 0.37435 -0.07181 0.02873  -0.09552 134 ILE   A CA   
93   C  C    . ILE   A 29  ? 0.51098 0.66997 0.40777 -0.06361 0.02390  -0.08467 134 ILE   A C    
94   O  O    . ILE   A 29  ? 0.45452 0.59506 0.34243 -0.05935 0.01911  -0.07340 134 ILE   A O    
95   C  CB   . ILE   A 29  ? 0.43437 0.65870 0.34905 -0.06610 0.03066  -0.12286 134 ILE   A CB   
96   C  CG1  . ILE   A 29  ? 0.50074 0.77068 0.40681 -0.07408 0.03502  -0.13501 134 ILE   A CG1  
97   C  CG2  . ILE   A 29  ? 0.41852 0.62397 0.34346 -0.05583 0.02500  -0.12609 134 ILE   A CG2  
98   C  CD1  . ILE   A 29  ? 0.44017 0.73881 0.37156 -0.07218 0.04042  -0.16472 134 ILE   A CD1  
99   N  N    . LEU   A 30  ? 0.42152 0.56731 0.33317 -0.06150 0.02506  -0.08802 135 LEU   A N    
100  C  CA   . LEU   A 30  ? 0.43704 0.54763 0.35348 -0.05481 0.02091  -0.07894 135 LEU   A CA   
101  C  C    . LEU   A 30  ? 0.41883 0.50638 0.31388 -0.05916 0.01906  -0.05799 135 LEU   A C    
102  O  O    . LEU   A 30  ? 0.43744 0.49921 0.32993 -0.05324 0.01514  -0.04956 135 LEU   A O    
103  C  CB   . LEU   A 30  ? 0.49005 0.59704 0.42705 -0.05286 0.02208  -0.08642 135 LEU   A CB   
104  C  CG   . LEU   A 30  ? 0.46798 0.59017 0.43331 -0.04618 0.02241  -0.10637 135 LEU   A CG   
105  C  CD1  . LEU   A 30  ? 0.44674 0.56667 0.43285 -0.04483 0.02279  -0.11024 135 LEU   A CD1  
106  C  CD2  . LEU   A 30  ? 0.33748 0.44560 0.31166 -0.03734 0.01761  -0.10799 135 LEU   A CD2  
107  N  N    . LEU   A 31  ? 0.46347 0.56033 0.34485 -0.06972 0.02190  -0.04981 136 LEU   A N    
108  C  CA   . LEU   A 31  ? 0.41636 0.49068 0.27999 -0.07449 0.01963  -0.02986 136 LEU   A CA   
109  C  C    . LEU   A 31  ? 0.49467 0.56465 0.34649 -0.07120 0.01553  -0.01995 136 LEU   A C    
110  O  O    . LEU   A 31  ? 0.53510 0.57701 0.38306 -0.06618 0.01158  -0.00932 136 LEU   A O    
111  C  CB   . LEU   A 31  ? 0.44169 0.52978 0.29503 -0.08798 0.02324  -0.02228 136 LEU   A CB   
112  C  CG   . LEU   A 31  ? 0.42080 0.50681 0.28299 -0.09286 0.02628  -0.02634 136 LEU   A CG   
113  C  CD1  . LEU   A 31  ? 0.41461 0.52234 0.26737 -0.10726 0.03042  -0.02010 136 LEU   A CD1  
114  C  CD2  . LEU   A 31  ? 0.46692 0.51637 0.32858 -0.09048 0.02294  -0.01778 136 LEU   A CD2  
115  N  N    . ASP   A 32  ? 0.50345 0.60352 0.35044 -0.07385 0.01635  -0.02427 137 ASP   A N    
116  C  CA   . ASP   A 32  ? 0.51140 0.61242 0.34804 -0.07094 0.01171  -0.01479 137 ASP   A CA   
117  C  C    . ASP   A 32  ? 0.51057 0.59338 0.35808 -0.05812 0.00791  -0.02048 137 ASP   A C    
118  O  O    . ASP   A 32  ? 0.55119 0.61675 0.39257 -0.05340 0.00322  -0.00799 137 ASP   A O    
119  C  CB   . ASP   A 32  ? 0.52551 0.66826 0.35603 -0.07676 0.01352  -0.02192 137 ASP   A CB   
120  C  CG   . ASP   A 32  ? 0.62499 0.77354 0.44454 -0.07461 0.00794  -0.01130 137 ASP   A CG   
121  O  OD1  . ASP   A 32  ? 0.71074 0.87588 0.53686 -0.06924 0.00683  -0.02522 137 ASP   A OD1  
122  O  OD2  . ASP   A 32  ? 0.70595 0.84239 0.51211 -0.07835 0.00418  0.01116  137 ASP   A OD2  
123  N  N    . ALA   A 33  ? 0.56247 0.64952 0.42804 -0.05247 0.00966  -0.03866 138 ALA   A N    
124  C  CA   . ALA   A 33  ? 0.48635 0.55840 0.36371 -0.04172 0.00617  -0.04337 138 ALA   A CA   
125  C  C    . ALA   A 33  ? 0.54909 0.58669 0.42513 -0.03720 0.00402  -0.03168 138 ALA   A C    
126  O  O    . ALA   A 33  ? 0.50452 0.52851 0.37988 -0.03026 0.00034  -0.02599 138 ALA   A O    
127  C  CB   . ALA   A 33  ? 0.36197 0.44423 0.26185 -0.03783 0.00802  -0.06321 138 ALA   A CB   
128  N  N    . HIS   A 34  ? 0.45775 0.48321 0.33401 -0.04130 0.00641  -0.02917 139 HIS   A N    
129  C  CA   . HIS   A 34  ? 0.50821 0.50381 0.38286 -0.03813 0.00486  -0.02065 139 HIS   A CA   
130  C  C    . HIS   A 34  ? 0.50353 0.48380 0.36373 -0.03862 0.00214  -0.00496 139 HIS   A C    
131  O  O    . HIS   A 34  ? 0.56281 0.52316 0.42394 -0.03150 -0.00043 -0.00049 139 HIS   A O    
132  C  CB   . HIS   A 34  ? 0.45070 0.44054 0.32793 -0.04410 0.00771  -0.02199 139 HIS   A CB   
133  C  CG   . HIS   A 34  ? 0.46009 0.42252 0.33422 -0.04276 0.00653  -0.01516 139 HIS   A CG   
134  N  ND1  . HIS   A 34  ? 0.48028 0.42992 0.36151 -0.03453 0.00467  -0.01748 139 HIS   A ND1  
135  C  CD2  . HIS   A 34  ? 0.56328 0.51031 0.42863 -0.04929 0.00711  -0.00725 139 HIS   A CD2  
136  C  CE1  . HIS   A 34  ? 0.50604 0.43538 0.38221 -0.03571 0.00456  -0.01274 139 HIS   A CE1  
137  N  NE2  . HIS   A 34  ? 0.53669 0.46261 0.40396 -0.04447 0.00581  -0.00701 139 HIS   A NE2  
138  N  N    . HIS   A 35  ? 0.49368 0.48416 0.34201 -0.04706 0.00252  0.00403  140 HIS   A N    
139  C  CA   . HIS   A 35  ? 0.63226 0.60756 0.46985 -0.04783 -0.00114 0.02145  140 HIS   A CA   
140  C  C    . HIS   A 35  ? 0.63679 0.61608 0.47425 -0.03942 -0.00562 0.02491  140 HIS   A C    
141  O  O    . HIS   A 35  ? 0.62185 0.58215 0.45692 -0.03504 -0.00958 0.03725  140 HIS   A O    
142  C  CB   . HIS   A 35  ? 0.72842 0.71714 0.55426 -0.06031 -0.00023 0.03270  140 HIS   A CB   
143  C  CG   . HIS   A 35  ? 0.98453 0.96286 0.80982 -0.06919 0.00301  0.03414  140 HIS   A CG   
144  N  ND1  . HIS   A 35  ? 1.08371 1.03193 0.90721 -0.07117 0.00114  0.04520  140 HIS   A ND1  
145  C  CD2  . HIS   A 35  ? 1.03727 1.03219 0.86529 -0.07666 0.00783  0.02498  140 HIS   A CD2  
146  C  CE1  . HIS   A 35  ? 1.07429 1.02126 0.89818 -0.08039 0.00452  0.04305  140 HIS   A CE1  
147  N  NE2  . HIS   A 35  ? 1.01497 0.99066 0.84150 -0.08366 0.00859  0.03148  140 HIS   A NE2  
148  N  N    . LYS   A 36  ? 0.54288 0.54677 0.38497 -0.03691 -0.00531 0.01334  141 LYS   A N    
149  C  CA   . LYS   A 36  ? 0.60167 0.61231 0.44501 -0.02942 -0.00973 0.01481  141 LYS   A CA   
150  C  C    . LYS   A 36  ? 0.65226 0.64506 0.50787 -0.01846 -0.01087 0.00864  141 LYS   A C    
151  O  O    . LYS   A 36  ? 0.53280 0.52588 0.39022 -0.01147 -0.01487 0.01232  141 LYS   A O    
152  C  CB   . LYS   A 36  ? 0.46949 0.51545 0.31376 -0.03226 -0.00901 0.00289  141 LYS   A CB   
153  C  CG   . LYS   A 36  ? 0.52797 0.59930 0.35708 -0.04143 -0.01015 0.01277  141 LYS   A CG   
154  C  CD   . LYS   A 36  ? 0.64756 0.75703 0.47866 -0.04500 -0.00811 -0.00425 141 LYS   A CD   
155  C  CE   . LYS   A 36  ? 0.78339 0.92388 0.59766 -0.05421 -0.00995 0.00623  141 LYS   A CE   
156  N  NZ   . LYS   A 36  ? 0.78820 0.92358 0.58990 -0.06402 -0.00867 0.02403  141 LYS   A NZ   
157  N  N    . THR   A 37  ? 0.53859 0.51870 0.40281 -0.01736 -0.00765 0.00020  142 THR   A N    
158  C  CA   . THR   A 37  ? 0.55660 0.52522 0.43257 -0.00868 -0.00825 -0.00571 142 THR   A CA   
159  C  C    . THR   A 37  ? 0.52073 0.46316 0.39627 -0.00672 -0.00718 -0.00144 142 THR   A C    
160  O  O    . THR   A 37  ? 0.52060 0.45578 0.40482 -0.00089 -0.00696 -0.00615 142 THR   A O    
161  C  CB   . THR   A 37  ? 0.55694 0.53880 0.44701 -0.00879 -0.00625 -0.02047 142 THR   A CB   
162  O  OG1  . THR   A 37  ? 0.53811 0.52290 0.42832 -0.01593 -0.00272 -0.02441 142 THR   A OG1  
163  C  CG2  . THR   A 37  ? 0.41010 0.41676 0.30459 -0.00858 -0.00776 -0.02844 142 THR   A CG2  
164  N  N    . TYR   A 38  ? 0.56642 0.49603 0.43264 -0.01226 -0.00650 0.00689  143 TYR   A N    
165  C  CA   . TYR   A 38  ? 0.60500 0.51015 0.47107 -0.01128 -0.00551 0.00885  143 TYR   A CA   
166  C  C    . TYR   A 38  ? 0.65244 0.54104 0.51193 -0.01110 -0.00826 0.02192  143 TYR   A C    
167  O  O    . TYR   A 38  ? 0.66344 0.55456 0.51516 -0.01911 -0.00887 0.03083  143 TYR   A O    
168  C  CB   . TYR   A 38  ? 0.56971 0.47338 0.43520 -0.01968 -0.00204 0.00406  143 TYR   A CB   
169  C  CG   . TYR   A 38  ? 0.55718 0.44074 0.42406 -0.01889 -0.00082 0.00165  143 TYR   A CG   
170  C  CD1  . TYR   A 38  ? 0.62275 0.48555 0.48423 -0.02174 -0.00126 0.00794  143 TYR   A CD1  
171  C  CD2  . TYR   A 38  ? 0.56687 0.45352 0.44140 -0.01597 0.00049  -0.00697 143 TYR   A CD2  
172  C  CE1  . TYR   A 38  ? 0.67342 0.51990 0.53662 -0.02151 0.00012  0.00268  143 TYR   A CE1  
173  C  CE2  . TYR   A 38  ? 0.54350 0.41659 0.41781 -0.01625 0.00174  -0.01018 143 TYR   A CE2  
174  C  CZ   . TYR   A 38  ? 0.61992 0.47337 0.48832 -0.01893 0.00183  -0.00686 143 TYR   A CZ   
175  O  OH   . TYR   A 38  ? 0.70435 0.54615 0.57298 -0.01968 0.00334  -0.01301 143 TYR   A OH   
176  N  N    . ASP   A 39  ? 0.65626 0.52897 0.52058 -0.00210 -0.01003 0.02347  144 ASP   A N    
177  C  CA   . ASP   A 39  ? 0.71723 0.57114 0.58062 0.00023  -0.01341 0.03547  144 ASP   A CA   
178  C  C    . ASP   A 39  ? 0.82531 0.65397 0.69148 -0.00077 -0.01125 0.03150  144 ASP   A C    
179  O  O    . ASP   A 39  ? 0.76138 0.58218 0.63441 0.00680  -0.00976 0.02250  144 ASP   A O    
180  C  CB   . ASP   A 39  ? 0.81172 0.66695 0.68183 0.01206  -0.01717 0.03872  144 ASP   A CB   
181  C  CG   . ASP   A 39  ? 0.85159 0.68823 0.72449 0.01578  -0.02188 0.05281  144 ASP   A CG   
182  O  OD1  . ASP   A 39  ? 0.78279 0.60437 0.65237 0.00836  -0.02244 0.06092  144 ASP   A OD1  
183  O  OD2  . ASP   A 39  ? 0.85287 0.69017 0.73324 0.02611  -0.02545 0.05638  144 ASP   A OD2  
184  N  N    . PRO   A 40  ? 0.78731 0.60465 0.64877 -0.01065 -0.01085 0.03701  145 PRO   A N    
185  C  CA   . PRO   A 40  ? 0.86929 0.66293 0.73431 -0.01263 -0.00899 0.03117  145 PRO   A CA   
186  C  C    . PRO   A 40  ? 0.90420 0.67333 0.77851 -0.00416 -0.01192 0.03470  145 PRO   A C    
187  O  O    . PRO   A 40  ? 0.93111 0.67995 0.81033 -0.00526 -0.01039 0.02745  145 PRO   A O    
188  C  CB   . PRO   A 40  ? 0.83172 0.62285 0.69010 -0.02680 -0.00842 0.03782  145 PRO   A CB   
189  C  CG   . PRO   A 40  ? 0.78157 0.58912 0.63376 -0.03045 -0.01122 0.05197  145 PRO   A CG   
190  C  CD   . PRO   A 40  ? 0.75379 0.58294 0.60659 -0.02165 -0.01165 0.04752  145 PRO   A CD   
191  N  N    . THR   A 41  ? 0.93729 0.70838 0.81579 0.00431  -0.01633 0.04477  146 THR   A N    
192  C  CA   . THR   A 41  ? 0.91215 0.66204 0.80376 0.01515  -0.01908 0.04592  146 THR   A CA   
193  C  C    . THR   A 41  ? 0.88691 0.64238 0.78555 0.02654  -0.01596 0.03030  146 THR   A C    
194  O  O    . THR   A 41  ? 0.95608 0.69432 0.86677 0.03498  -0.01592 0.02427  146 THR   A O    
195  C  CB   . THR   A 41  ? 0.92480 0.67577 0.82003 0.01986  -0.02606 0.06507  146 THR   A CB   
196  O  OG1  . THR   A 41  ? 0.82903 0.60540 0.72232 0.02677  -0.02692 0.06415  146 THR   A OG1  
197  C  CG2  . THR   A 41  ? 0.95326 0.70744 0.83892 0.00682  -0.02896 0.08242  146 THR   A CG2  
198  N  N    . TYR   A 42  ? 0.76527 0.54519 0.65824 0.02660  -0.01331 0.02347  147 TYR   A N    
199  C  CA   . TYR   A 42  ? 0.78285 0.57254 0.68194 0.03552  -0.01036 0.01082  147 TYR   A CA   
200  C  C    . TYR   A 42  ? 0.80020 0.58683 0.71123 0.04888  -0.01359 0.01431  147 TYR   A C    
201  O  O    . TYR   A 42  ? 0.71665 0.50244 0.63658 0.05727  -0.01090 0.00330  147 TYR   A O    
202  C  CB   . TYR   A 42  ? 0.73067 0.51176 0.63081 0.03329  -0.00525 -0.00430 147 TYR   A CB   
203  C  CG   . TYR   A 42  ? 0.69191 0.47532 0.58202 0.02012  -0.00291 -0.00670 147 TYR   A CG   
204  C  CD1  . TYR   A 42  ? 0.68500 0.44877 0.57344 0.01230  -0.00286 -0.00616 147 TYR   A CD1  
205  C  CD2  . TYR   A 42  ? 0.66231 0.46761 0.54701 0.01546  -0.00118 -0.00929 147 TYR   A CD2  
206  C  CE1  . TYR   A 42  ? 0.71950 0.48774 0.59978 0.00010  -0.00089 -0.00829 147 TYR   A CE1  
207  C  CE2  . TYR   A 42  ? 0.76207 0.57104 0.64014 0.00433  0.00055  -0.01123 147 TYR   A CE2  
208  C  CZ   . TYR   A 42  ? 0.77006 0.56163 0.64525 -0.00336 0.00081  -0.01076 147 TYR   A CZ   
209  O  OH   . TYR   A 42  ? 0.76132 0.55881 0.63086 -0.01456 0.00240  -0.01270 147 TYR   A OH   
210  N  N    . ALA   A 43  ? 0.88077 0.66871 0.79237 0.05062  -0.01948 0.02995  148 ALA   A N    
211  C  CA   . ALA   A 43  ? 0.85912 0.64459 0.78382 0.06345  -0.02386 0.03582  148 ALA   A CA   
212  C  C    . ALA   A 43  ? 0.82148 0.62982 0.75039 0.07132  -0.02238 0.02795  148 ALA   A C    
213  O  O    . ALA   A 43  ? 0.91772 0.72442 0.86018 0.08307  -0.02281 0.02421  148 ALA   A O    
214  C  CB   . ALA   A 43  ? 0.90393 0.69064 0.82676 0.06181  -0.03140 0.05673  148 ALA   A CB   
215  N  N    . ASP   A 44  ? 0.69954 0.52964 0.61916 0.06494  -0.02067 0.02496  149 ASP   A N    
216  C  CA   . ASP   A 44  ? 0.75613 0.60792 0.68115 0.07070  -0.01982 0.01874  149 ASP   A CA   
217  C  C    . ASP   A 44  ? 0.79676 0.64813 0.72873 0.07528  -0.01407 0.00439  149 ASP   A C    
218  O  O    . ASP   A 44  ? 0.85467 0.72316 0.79377 0.08087  -0.01328 0.00007  149 ASP   A O    
219  C  CB   . ASP   A 44  ? 0.65955 0.53205 0.57607 0.06204  -0.01945 0.01766  149 ASP   A CB   
220  C  CG   . ASP   A 44  ? 0.81449 0.69504 0.72355 0.05721  -0.02457 0.02969  149 ASP   A CG   
221  O  OD1  . ASP   A 44  ? 0.87586 0.75501 0.78854 0.06296  -0.02995 0.04084  149 ASP   A OD1  
222  O  OD2  . ASP   A 44  ? 0.92175 0.81204 0.82210 0.04761  -0.02333 0.02806  149 ASP   A OD2  
223  N  N    . PHE   A 45  ? 0.85959 0.69421 0.78972 0.07224  -0.01008 -0.00318 150 PHE   A N    
224  C  CA   . PHE   A 45  ? 0.80276 0.64114 0.73758 0.07510  -0.00427 -0.01765 150 PHE   A CA   
225  C  C    . PHE   A 45  ? 0.94173 0.78060 0.89166 0.08860  -0.00407 -0.02208 150 PHE   A C    
226  O  O    . PHE   A 45  ? 0.87052 0.72281 0.82517 0.09183  0.00074  -0.03333 150 PHE   A O    
227  C  CB   . PHE   A 45  ? 0.71389 0.53525 0.64340 0.06834  -0.00063 -0.02573 150 PHE   A CB   
228  C  CG   . PHE   A 45  ? 0.81837 0.64655 0.73540 0.05560  0.00109  -0.02617 150 PHE   A CG   
229  C  CD1  . PHE   A 45  ? 0.81633 0.65461 0.72724 0.04998  -0.00185 -0.01680 150 PHE   A CD1  
230  C  CD2  . PHE   A 45  ? 0.81666 0.64307 0.72935 0.04938  0.00551  -0.03690 150 PHE   A CD2  
231  C  CE1  . PHE   A 45  ? 0.82804 0.67299 0.73104 0.03952  -0.00034 -0.01807 150 PHE   A CE1  
232  C  CE2  . PHE   A 45  ? 0.80075 0.63460 0.70424 0.03834  0.00636  -0.03631 150 PHE   A CE2  
233  C  CZ   . PHE   A 45  ? 0.80439 0.64673 0.70416 0.03395  0.00345  -0.02683 150 PHE   A CZ   
234  N  N    A ARG   A 46  ? 1.05025 0.87680 1.00887 0.09638  -0.00935 -0.01281 151 ARG   A N    
235  N  N    B ARG   A 46  ? 1.05453 0.88109 1.01321 0.09643  -0.00934 -0.01285 151 ARG   A N    
236  C  CA   A ARG   A 46  ? 1.10508 0.93226 1.08155 0.11059  -0.00975 -0.01677 151 ARG   A CA   
237  C  CA   B ARG   A 46  ? 1.10448 0.93200 1.08098 0.11060  -0.00958 -0.01716 151 ARG   A CA   
238  C  C    A ARG   A 46  ? 1.05094 0.90606 1.03253 0.11590  -0.01038 -0.01571 151 ARG   A C    
239  C  C    B ARG   A 46  ? 1.04536 0.90117 1.02660 0.11558  -0.00998 -0.01645 151 ARG   A C    
240  O  O    A ARG   A 46  ? 1.05745 0.92101 1.05332 0.12644  -0.00825 -0.02344 151 ARG   A O    
241  O  O    B ARG   A 46  ? 1.05759 0.92299 1.05233 0.12545  -0.00731 -0.02503 151 ARG   A O    
242  C  CB   A ARG   A 46  ? 1.20231 1.00862 1.18908 0.11734  -0.01672 -0.00406 151 ARG   A CB   
243  C  CB   B ARG   A 46  ? 1.20133 1.00870 1.18873 0.11791  -0.01658 -0.00456 151 ARG   A CB   
244  C  CG   A ARG   A 46  ? 1.27586 1.05534 1.25623 0.10884  -0.01801 0.00069  151 ARG   A CG   
245  C  CG   B ARG   A 46  ? 1.27787 1.06065 1.25732 0.10883  -0.01931 0.00424  151 ARG   A CG   
246  C  CD   A ARG   A 46  ? 1.36170 1.11584 1.35836 0.11598  -0.01645 -0.00936 151 ARG   A CD   
247  C  CD   B ARG   A 46  ? 1.33918 1.10230 1.31944 0.10517  -0.01369 -0.01080 151 ARG   A CD   
248  N  NE   A ARG   A 46  ? 1.42443 1.15058 1.42423 0.11233  -0.02213 0.00394  151 ARG   A NE   
249  N  NE   B ARG   A 46  ? 1.40911 1.14462 1.40775 0.11325  -0.01646 -0.01084 151 ARG   A NE   
250  C  CZ   A ARG   A 46  ? 1.46599 1.16417 1.48023 0.11539  -0.02186 -0.00305 151 ARG   A CZ   
251  C  CZ   B ARG   A 46  ? 1.44163 1.15598 1.44465 0.11170  -0.02353 0.00638  151 ARG   A CZ   
252  N  NH1  A ARG   A 46  ? 1.46297 1.15944 1.48893 0.12264  -0.01562 -0.02552 151 ARG   A NH1  
253  N  NH1  B ARG   A 46  ? 1.47915 1.16701 1.50314 0.11980  -0.02621 0.00534  151 ARG   A NH1  
254  N  NH2  A ARG   A 46  ? 1.49879 1.17195 1.51661 0.11054  -0.02782 0.01208  151 ARG   A NH2  
255  N  NH2  B ARG   A 46  ? 1.43920 1.15961 1.42709 0.10177  -0.02795 0.02450  151 ARG   A NH2  
256  N  N    . ASP   A 47  ? 0.88753 0.75810 0.85930 0.10863  -0.01311 -0.00751 152 ASP   A N    
257  C  CA   . ASP   A 47  ? 0.81304 0.71006 0.79029 0.11167  -0.01401 -0.00710 152 ASP   A CA   
258  C  C    . ASP   A 47  ? 0.78873 0.70239 0.76501 0.10734  -0.00742 -0.01850 152 ASP   A C    
259  O  O    . ASP   A 47  ? 0.82774 0.76334 0.81163 0.11001  -0.00733 -0.01940 152 ASP   A O    
260  C  CB   . ASP   A 47  ? 0.77530 0.68295 0.74441 0.10513  -0.01973 0.00413  152 ASP   A CB   
261  C  CG   . ASP   A 47  ? 0.84983 0.74811 0.81965 0.10877  -0.02712 0.01831  152 ASP   A CG   
262  O  OD1  . ASP   A 47  ? 0.88956 0.78226 0.87302 0.12021  -0.02986 0.02156  152 ASP   A OD1  
263  O  OD2  . ASP   A 47  ? 0.87555 0.77377 0.83337 0.10011  -0.03033 0.02661  152 ASP   A OD2  
264  N  N    . PHE   A 48  ? 0.69904 0.60440 0.66673 0.10000  -0.00244 -0.02598 153 PHE   A N    
265  C  CA   . PHE   A 48  ? 0.67058 0.59326 0.63739 0.09525  0.00326  -0.03462 153 PHE   A CA   
266  C  C    . PHE   A 48  ? 0.67129 0.60411 0.64995 0.10460  0.00793  -0.04495 153 PHE   A C    
267  O  O    . PHE   A 48  ? 0.69808 0.61939 0.68622 0.11495  0.00743  -0.04812 153 PHE   A O    
268  C  CB   . PHE   A 48  ? 0.62493 0.53816 0.57966 0.08502  0.00672  -0.03940 153 PHE   A CB   
269  C  CG   . PHE   A 48  ? 0.68495 0.58961 0.62917 0.07576  0.00315  -0.03121 153 PHE   A CG   
270  C  CD1  . PHE   A 48  ? 0.58266 0.47452 0.51697 0.06757  0.00500  -0.03395 153 PHE   A CD1  
271  C  CD2  . PHE   A 48  ? 0.63236 0.54440 0.57722 0.07482  -0.00178 -0.02227 153 PHE   A CD2  
272  C  CE1  . PHE   A 48  ? 0.71833 0.60509 0.64436 0.05923  0.00233  -0.02740 153 PHE   A CE1  
273  C  CE2  . PHE   A 48  ? 0.67766 0.58509 0.61374 0.06640  -0.00418 -0.01713 153 PHE   A CE2  
274  C  CZ   . PHE   A 48  ? 0.68607 0.58102 0.61312 0.05886  -0.00195 -0.01943 153 PHE   A CZ   
275  N  N    . ARG   A 49  ? 0.51510 0.47088 0.49475 0.10073  0.01244  -0.05001 154 ARG   A N    
276  C  CA   . ARG   A 49  ? 0.60292 0.57194 0.59095 0.10699  0.01873  -0.06249 154 ARG   A CA   
277  C  C    . ARG   A 49  ? 0.59571 0.54849 0.57779 0.10560  0.02309  -0.07442 154 ARG   A C    
278  O  O    . ARG   A 49  ? 0.61730 0.56038 0.58628 0.09530  0.02298  -0.07300 154 ARG   A O    
279  C  CB   . ARG   A 49  ? 0.63790 0.63766 0.62654 0.10046  0.02252  -0.06306 154 ARG   A CB   
280  C  CG   . ARG   A 49  ? 0.56808 0.58556 0.56734 0.10319  0.01885  -0.05442 154 ARG   A CG   
281  C  CD   . ARG   A 49  ? 0.50331 0.54731 0.50335 0.09360  0.02103  -0.05100 154 ARG   A CD   
282  N  NE   . ARG   A 49  ? 0.50637 0.54397 0.49730 0.08162  0.01789  -0.04280 154 ARG   A NE   
283  C  CZ   . ARG   A 49  ? 0.45043 0.50621 0.44324 0.07183  0.01820  -0.03700 154 ARG   A CZ   
284  N  NH1  . ARG   A 49  ? 0.45048 0.53345 0.45187 0.07122  0.02181  -0.03753 154 ARG   A NH1  
285  N  NH2  . ARG   A 49  ? 0.43574 0.48338 0.42356 0.06251  0.01474  -0.03011 154 ARG   A NH2  
286  N  N    . PRO   A 50  ? 0.61722 0.56719 0.61040 0.11587  0.02678  -0.08733 155 PRO   A N    
287  C  CA   . PRO   A 50  ? 0.71279 0.64081 0.70346 0.11558  0.02933  -0.09915 155 PRO   A CA   
288  C  C    . PRO   A 50  ? 0.78479 0.72570 0.76197 0.10366  0.03512  -0.10869 155 PRO   A C    
289  O  O    . PRO   A 50  ? 0.75868 0.73006 0.73376 0.09956  0.03929  -0.11099 155 PRO   A O    
290  C  CB   . PRO   A 50  ? 0.64851 0.57658 0.65897 0.13051  0.03242  -0.11299 155 PRO   A CB   
291  C  CG   . PRO   A 50  ? 0.66712 0.62899 0.68547 0.13475  0.03501  -0.11279 155 PRO   A CG   
292  C  CD   . PRO   A 50  ? 0.60390 0.57150 0.61465 0.12823  0.02887  -0.09306 155 PRO   A CD   
293  N  N    . PRO   A 51  ? 0.82559 0.74584 0.79370 0.09696  0.03508  -0.11318 156 PRO   A N    
294  C  CA   . PRO   A 51  ? 0.83360 0.76811 0.78967 0.08595  0.04033  -0.12384 156 PRO   A CA   
295  C  C    . PRO   A 51  ? 0.90821 0.86135 0.87227 0.09162  0.04808  -0.14508 156 PRO   A C    
296  O  O    . PRO   A 51  ? 0.91395 0.85184 0.89190 0.10242  0.04953  -0.15790 156 PRO   A O    
297  C  CB   . PRO   A 51  ? 0.72484 0.62979 0.67320 0.07947  0.03789  -0.12506 156 PRO   A CB   
298  C  CG   . PRO   A 51  ? 0.77648 0.65483 0.72992 0.08461  0.03094  -0.11040 156 PRO   A CG   
299  C  CD   . PRO   A 51  ? 0.79377 0.67873 0.76266 0.09824  0.02993  -0.10788 156 PRO   A CD   
300  N  N    . VAL   A 52  ? 0.87558 0.86339 0.83232 0.08424  0.05295  -0.14861 157 VAL   A N    
301  C  CA   . VAL   A 52  ? 0.84962 0.86429 0.81207 0.08786  0.06128  -0.16901 157 VAL   A CA   
302  C  C    . VAL   A 52  ? 0.90237 0.93389 0.84875 0.07405  0.06530  -0.17863 157 VAL   A C    
303  O  O    . VAL   A 52  ? 0.81975 0.87192 0.75361 0.06212  0.06402  -0.16557 157 VAL   A O    
304  C  CB   . VAL   A 52  ? 0.84710 0.89621 0.81677 0.09143  0.06384  -0.16357 157 VAL   A CB   
305  C  CG1  . VAL   A 52  ? 0.91289 1.00006 0.88264 0.08971  0.07334  -0.18291 157 VAL   A CG1  
306  C  CG2  . VAL   A 52  ? 0.80701 0.84279 0.79557 0.10702  0.06079  -0.15985 157 VAL   A CG2  
307  N  N    . ARG   A 53  ? 1.01861 1.04224 0.96643 0.07509  0.06964  -0.20134 158 ARG   A N    
308  C  CA   . ARG   A 53  ? 1.05981 1.10292 0.99145 0.06094  0.07327  -0.21219 158 ARG   A CA   
309  C  C    . ARG   A 53  ? 1.17675 1.25916 1.11098 0.06209  0.08285  -0.23531 158 ARG   A C    
310  O  O    . ARG   A 53  ? 1.21548 1.28802 1.16486 0.07336  0.08714  -0.25744 158 ARG   A O    
311  C  CB   . ARG   A 53  ? 1.01812 1.02751 0.94676 0.05725  0.07100  -0.22195 158 ARG   A CB   
312  C  CG   . ARG   A 53  ? 0.99328 0.98451 0.90894 0.04651  0.06356  -0.20099 158 ARG   A CG   
313  C  CD   . ARG   A 53  ? 0.96699 0.91496 0.89217 0.05432  0.05742  -0.19071 158 ARG   A CD   
314  N  NE   . ARG   A 53  ? 0.94543 0.87503 0.86014 0.04495  0.05100  -0.17327 158 ARG   A NE   
315  C  CZ   . ARG   A 53  ? 0.92343 0.82126 0.84315 0.04900  0.04530  -0.16044 158 ARG   A CZ   
316  N  NH1  . ARG   A 53  ? 0.86079 0.74043 0.79604 0.06228  0.04431  -0.16139 158 ARG   A NH1  
317  N  NH2  . ARG   A 53  ? 0.88555 0.77216 0.79549 0.03966  0.04048  -0.14637 158 ARG   A NH2  
318  N  N    . PRO   A 67  ? 1.36194 1.69071 1.26455 0.00861  0.09038  -0.15101 219 PRO   A N    
319  C  CA   . PRO   A 67  ? 1.31121 1.62542 1.20380 -0.00275 0.08166  -0.13028 219 PRO   A CA   
320  C  C    . PRO   A 67  ? 1.16436 1.44279 1.06854 0.00296  0.07313  -0.10932 219 PRO   A C    
321  O  O    . PRO   A 67  ? 1.14374 1.42511 1.06087 0.00973  0.07348  -0.10368 219 PRO   A O    
322  C  CB   . PRO   A 67  ? 1.34744 1.71375 1.23235 -0.01854 0.08279  -0.11541 219 PRO   A CB   
323  C  CG   . PRO   A 67  ? 1.36934 1.75743 1.26806 -0.01349 0.08648  -0.11047 219 PRO   A CG   
324  C  CD   . PRO   A 67  ? 1.37408 1.73841 1.28396 0.00484  0.09166  -0.13503 219 PRO   A CD   
325  N  N    . LEU   A 68  ? 1.07912 1.32735 0.97868 -0.00072 0.06558  -0.09845 220 LEU   A N    
326  C  CA   . LEU   A 68  ? 0.81753 1.03359 0.72829 0.00512  0.05826  -0.08235 220 LEU   A CA   
327  C  C    . LEU   A 68  ? 0.57244 0.75881 0.49291 0.02129  0.05974  -0.09543 220 LEU   A C    
328  O  O    . LEU   A 68  ? 0.54051 0.71279 0.47237 0.02763  0.05570  -0.08493 220 LEU   A O    
329  C  CB   . LEU   A 68  ? 0.78994 1.02834 0.71081 -0.00019 0.05519  -0.06051 220 LEU   A CB   
330  C  CG   . LEU   A 68  ? 0.84176 1.11271 0.75752 -0.01640 0.05259  -0.04235 220 LEU   A CG   
331  C  CD1  . LEU   A 68  ? 0.88170 1.15342 0.81249 -0.02034 0.04571  -0.01749 220 LEU   A CD1  
332  C  CD2  . LEU   A 68  ? 0.83328 1.09395 0.73655 -0.02432 0.04864  -0.04077 220 LEU   A CD2  
333  N  N    . SER   A 69  ? 0.58074 0.75743 0.49804 0.02776  0.06491  -0.11823 221 SER   A N    
334  C  CA   . SER   A 69  ? 0.66279 0.81197 0.59177 0.04345  0.06577  -0.12982 221 SER   A CA   
335  C  C    . SER   A 69  ? 0.63580 0.74182 0.56624 0.04725  0.05797  -0.11953 221 SER   A C    
336  O  O    . SER   A 69  ? 0.55065 0.63638 0.49232 0.05919  0.05617  -0.12011 221 SER   A O    
337  C  CB   . SER   A 69  ? 0.67799 0.82631 0.60629 0.04878  0.07279  -0.15729 221 SER   A CB   
338  O  OG   . SER   A 69  ? 0.79948 0.92796 0.71606 0.04193  0.07088  -0.16287 221 SER   A OG   
339  N  N    . MET   A 70  ? 0.58514 0.67942 0.50502 0.03723  0.05323  -0.10978 222 MET   A N    
340  C  CA   . MET   A 70  ? 0.53078 0.58848 0.45097 0.03936  0.04655  -0.10075 222 MET   A CA   
341  C  C    . MET   A 70  ? 0.49015 0.54824 0.41537 0.03665  0.04035  -0.07999 222 MET   A C    
342  O  O    . MET   A 70  ? 0.56176 0.59400 0.48771 0.03824  0.03508  -0.07268 222 MET   A O    
343  C  CB   . MET   A 70  ? 0.56260 0.60639 0.47041 0.03053  0.04510  -0.10404 222 MET   A CB   
344  C  CG   . MET   A 70  ? 0.68258 0.71314 0.58828 0.03427  0.04957  -0.12565 222 MET   A CG   
345  S  SD   . MET   A 70  ? 0.68686 0.67593 0.60440 0.04863  0.04711  -0.12913 222 MET   A SD   
346  C  CE   . MET   A 70  ? 0.60088 0.56178 0.51036 0.04092  0.03968  -0.11356 222 MET   A CE   
347  N  N    . LEU   A 71  ? 0.50866 0.59640 0.43836 0.03201  0.04090  -0.07087 223 LEU   A N    
348  C  CA   . LEU   A 71  ? 0.51901 0.60690 0.45669 0.02873  0.03477  -0.05253 223 LEU   A CA   
349  C  C    . LEU   A 71  ? 0.61610 0.68485 0.56379 0.03906  0.03154  -0.05046 223 LEU   A C    
350  O  O    . LEU   A 71  ? 0.57747 0.62988 0.52735 0.03739  0.02570  -0.04102 223 LEU   A O    
351  C  CB   . LEU   A 71  ? 0.53271 0.65654 0.47591 0.02156  0.03606  -0.04303 223 LEU   A CB   
352  C  CG   . LEU   A 71  ? 0.62830 0.75389 0.58420 0.01769  0.02971  -0.02487 223 LEU   A CG   
353  C  CD1  . LEU   A 71  ? 0.57228 0.67767 0.52672 0.01208  0.02326  -0.01589 223 LEU   A CD1  
354  C  CD2  . LEU   A 71  ? 0.68958 0.85118 0.65159 0.00885  0.03085  -0.01389 223 LEU   A CD2  
355  N  N    . PRO   A 72  ? 0.57252 0.64445 0.52741 0.04968  0.03472  -0.05888 224 PRO   A N    
356  C  CA   . PRO   A 72  ? 0.47949 0.53473 0.44339 0.05884  0.03037  -0.05505 224 PRO   A CA   
357  C  C    . PRO   A 72  ? 0.56500 0.58710 0.52268 0.06152  0.02652  -0.05548 224 PRO   A C    
358  O  O    . PRO   A 72  ? 0.53468 0.54556 0.49491 0.06163  0.02094  -0.04651 224 PRO   A O    
359  C  CB   . PRO   A 72  ? 0.48741 0.55399 0.46057 0.07012  0.03499  -0.06560 224 PRO   A CB   
360  C  CG   . PRO   A 72  ? 0.48896 0.58769 0.46065 0.06447  0.04152  -0.07089 224 PRO   A CG   
361  C  CD   . PRO   A 72  ? 0.46991 0.56521 0.42713 0.05375  0.04211  -0.07155 224 PRO   A CD   
362  N  N    . HIS   A 73  ? 0.57234 0.57998 0.52234 0.06279  0.02942  -0.06613 225 HIS   A N    
363  C  CA   . HIS   A 73  ? 0.61519 0.59208 0.55981 0.06391  0.02577  -0.06506 225 HIS   A CA   
364  C  C    . HIS   A 73  ? 0.59632 0.56781 0.53294 0.05308  0.02199  -0.05559 225 HIS   A C    
365  O  O    . HIS   A 73  ? 0.65691 0.61220 0.59271 0.05327  0.01739  -0.04871 225 HIS   A O    
366  C  CB   . HIS   A 73  ? 0.61614 0.57871 0.55689 0.06652  0.02964  -0.07924 225 HIS   A CB   
367  C  CG   . HIS   A 73  ? 0.66988 0.60060 0.60731 0.06755  0.02583  -0.07700 225 HIS   A CG   
368  N  ND1  . HIS   A 73  ? 0.62282 0.53673 0.56832 0.07718  0.02215  -0.07259 225 HIS   A ND1  
369  C  CD2  . HIS   A 73  ? 0.55210 0.46678 0.47952 0.05933  0.02480  -0.07708 225 HIS   A CD2  
370  C  CE1  . HIS   A 73  ? 0.60780 0.49661 0.54798 0.07430  0.01910  -0.06918 225 HIS   A CE1  
371  N  NE2  . HIS   A 73  ? 0.62352 0.51211 0.55289 0.06349  0.02093  -0.07249 225 HIS   A NE2  
372  N  N    . LEU   A 74  ? 0.54993 0.53722 0.48148 0.04352  0.02372  -0.05494 226 LEU   A N    
373  C  CA   . LEU   A 74  ? 0.57403 0.55740 0.50116 0.03403  0.01989  -0.04625 226 LEU   A CA   
374  C  C    . LEU   A 74  ? 0.51332 0.50339 0.45034 0.03293  0.01527  -0.03457 226 LEU   A C    
375  O  O    . LEU   A 74  ? 0.45998 0.44071 0.39706 0.02879  0.01137  -0.02894 226 LEU   A O    
376  C  CB   . LEU   A 74  ? 0.54332 0.54359 0.46393 0.02427  0.02205  -0.04736 226 LEU   A CB   
377  C  CG   . LEU   A 74  ? 0.71798 0.70473 0.62714 0.01941  0.02312  -0.05501 226 LEU   A CG   
378  C  CD1  . LEU   A 74  ? 0.69921 0.66619 0.60651 0.02738  0.02606  -0.06784 226 LEU   A CD1  
379  C  CD2  . LEU   A 74  ? 0.72779 0.73753 0.63022 0.01017  0.02549  -0.05753 226 LEU   A CD2  
380  N  N    . ALA   A 75  ? 0.49428 0.50153 0.44112 0.03625  0.01580  -0.03203 227 ALA   A N    
381  C  CA   . ALA   A 75  ? 0.47707 0.48924 0.43560 0.03534  0.01114  -0.02289 227 ALA   A CA   
382  C  C    . ALA   A 75  ? 0.49364 0.48850 0.45301 0.04169  0.00779  -0.02349 227 ALA   A C    
383  O  O    . ALA   A 75  ? 0.51582 0.50659 0.47948 0.03858  0.00356  -0.01891 227 ALA   A O    
384  C  CB   . ALA   A 75  ? 0.47692 0.51257 0.44638 0.03656  0.01255  -0.02012 227 ALA   A CB   
385  N  N    . ASP   A 76  ? 0.56949 0.55567 0.52601 0.05053  0.00941  -0.02915 228 ASP   A N    
386  C  CA   . ASP   A 76  ? 0.53750 0.50892 0.49344 0.05581  0.00560  -0.02741 228 ASP   A CA   
387  C  C    . ASP   A 76  ? 0.55827 0.51159 0.50398 0.05068  0.00406  -0.02640 228 ASP   A C    
388  O  O    . ASP   A 76  ? 0.47210 0.42055 0.41750 0.04979  0.00022  -0.02248 228 ASP   A O    
389  C  CB   . ASP   A 76  ? 0.50105 0.46666 0.45876 0.06664  0.00697  -0.03183 228 ASP   A CB   
390  C  CG   . ASP   A 76  ? 0.53513 0.52057 0.50519 0.07280  0.00754  -0.03207 228 ASP   A CG   
391  O  OD1  . ASP   A 76  ? 0.56527 0.55093 0.53994 0.08198  0.00987  -0.03751 228 ASP   A OD1  
392  O  OD2  . ASP   A 76  ? 0.52738 0.52843 0.50454 0.06843  0.00558  -0.02723 228 ASP   A OD2  
393  N  N    . LEU   A 77  ? 0.48501 0.43097 0.42237 0.04653  0.00717  -0.03059 229 LEU   A N    
394  C  CA   . LEU   A 77  ? 0.49376 0.42433 0.42212 0.04071  0.00602  -0.02968 229 LEU   A CA   
395  C  C    . LEU   A 77  ? 0.49313 0.43105 0.42469 0.03339  0.00324  -0.02473 229 LEU   A C    
396  O  O    . LEU   A 77  ? 0.55496 0.48560 0.48402 0.03127  0.00082  -0.02254 229 LEU   A O    
397  C  CB   . LEU   A 77  ? 0.60602 0.53046 0.52634 0.03685  0.00978  -0.03633 229 LEU   A CB   
398  C  CG   . LEU   A 77  ? 0.75324 0.66479 0.66486 0.02901  0.00903  -0.03586 229 LEU   A CG   
399  C  CD1  . LEU   A 77  ? 0.69892 0.59228 0.60733 0.03132  0.00659  -0.03239 229 LEU   A CD1  
400  C  CD2  . LEU   A 77  ? 0.72525 0.63369 0.63005 0.02494  0.01263  -0.04421 229 LEU   A CD2  
401  N  N    . VAL   A 78  ? 0.51982 0.47346 0.45848 0.02933  0.00346  -0.02279 230 VAL   A N    
402  C  CA   . VAL   A 78  ? 0.49363 0.45351 0.44051 0.02332  0.00025  -0.01828 230 VAL   A CA   
403  C  C    . VAL   A 78  ? 0.40771 0.37058 0.36408 0.02647  -0.00313 -0.01711 230 VAL   A C    
404  O  O    . VAL   A 78  ? 0.44140 0.40194 0.40067 0.02368  -0.00551 -0.01757 230 VAL   A O    
405  C  CB   . VAL   A 78  ? 0.55319 0.52934 0.50814 0.01820  0.00026  -0.01377 230 VAL   A CB   
406  C  CG1  . VAL   A 78  ? 0.67767 0.65879 0.64710 0.01359  -0.00405 -0.00859 230 VAL   A CG1  
407  C  CG2  . VAL   A 78  ? 0.70455 0.68107 0.64900 0.01332  0.00291  -0.01546 230 VAL   A CG2  
408  N  N    . SER   A 79  ? 0.40792 0.37861 0.37004 0.03197  -0.00327 -0.01679 231 SER   A N    
409  C  CA   . SER   A 79  ? 0.28856 0.26457 0.25963 0.03448  -0.00683 -0.01668 231 SER   A CA   
410  C  C    . SER   A 79  ? 0.35833 0.32427 0.32012 0.03632  -0.00833 -0.01842 231 SER   A C    
411  O  O    . SER   A 79  ? 0.41886 0.38887 0.38525 0.03384  -0.01112 -0.02010 231 SER   A O    
412  C  CB   . SER   A 79  ? 0.33010 0.31673 0.30745 0.04048  -0.00653 -0.01604 231 SER   A CB   
413  O  OG   . SER   A 79  ? 0.47485 0.47073 0.46364 0.04097  -0.01047 -0.01605 231 SER   A OG   
414  N  N    . TYR   A 80  ? 0.41350 0.36741 0.36328 0.04019  -0.00660 -0.01816 232 TYR   A N    
415  C  CA   . TYR   A 80  ? 0.37917 0.32365 0.31948 0.04043  -0.00829 -0.01669 232 TYR   A CA   
416  C  C    . TYR   A 80  ? 0.45543 0.39693 0.39160 0.03244  -0.00804 -0.01795 232 TYR   A C    
417  O  O    . TYR   A 80  ? 0.42512 0.37078 0.35959 0.03011  -0.01008 -0.01820 232 TYR   A O    
418  C  CB   . TYR   A 80  ? 0.44102 0.37031 0.37283 0.04535  -0.00675 -0.01516 232 TYR   A CB   
419  C  CG   . TYR   A 80  ? 0.58051 0.49776 0.50236 0.04380  -0.00854 -0.01071 232 TYR   A CG   
420  C  CD1  . TYR   A 80  ? 0.59537 0.51543 0.51669 0.04802  -0.01255 -0.00490 232 TYR   A CD1  
421  C  CD2  . TYR   A 80  ? 0.63508 0.54006 0.54833 0.03732  -0.00660 -0.01104 232 TYR   A CD2  
422  C  CE1  . TYR   A 80  ? 0.57512 0.48651 0.48727 0.04537  -0.01462 0.00190  232 TYR   A CE1  
423  C  CE2  . TYR   A 80  ? 0.57082 0.46612 0.47559 0.03453  -0.00824 -0.00530 232 TYR   A CE2  
424  C  CZ   . TYR   A 80  ? 0.58963 0.48829 0.49370 0.03838  -0.01226 0.00187  232 TYR   A CZ   
425  O  OH   . TYR   A 80  ? 0.70412 0.59536 0.59965 0.03439  -0.01430 0.01019  232 TYR   A OH   
426  N  N    . SER   A 81  ? 0.44127 0.37871 0.37627 0.02791  -0.00554 -0.01923 233 SER   A N    
427  C  CA   . SER   A 81  ? 0.50589 0.44178 0.43872 0.02072  -0.00529 -0.02044 233 SER   A CA   
428  C  C    . SER   A 81  ? 0.40527 0.35422 0.35175 0.01819  -0.00756 -0.02315 233 SER   A C    
429  O  O    . SER   A 81  ? 0.39889 0.35035 0.34501 0.01434  -0.00791 -0.02600 233 SER   A O    
430  C  CB   . SER   A 81  ? 0.50976 0.44132 0.43972 0.01645  -0.00289 -0.02079 233 SER   A CB   
431  O  OG   . SER   A 81  ? 0.60093 0.51899 0.51920 0.01768  -0.00064 -0.02127 233 SER   A OG   
432  N  N    . ILE   A 82  ? 0.37013 0.32825 0.33039 0.01994  -0.00900 -0.02293 234 ILE   A N    
433  C  CA   . ILE   A 82  ? 0.36954 0.33815 0.34691 0.01791  -0.01175 -0.02657 234 ILE   A CA   
434  C  C    . ILE   A 82  ? 0.41853 0.39259 0.39376 0.01903  -0.01323 -0.03181 234 ILE   A C    
435  O  O    . ILE   A 82  ? 0.41140 0.39192 0.39403 0.01580  -0.01400 -0.03835 234 ILE   A O    
436  C  CB   . ILE   A 82  ? 0.39131 0.36808 0.38444 0.01913  -0.01352 -0.02381 234 ILE   A CB   
437  C  CG1  . ILE   A 82  ? 0.44946 0.42648 0.44669 0.01564  -0.01273 -0.01776 234 ILE   A CG1  
438  C  CG2  . ILE   A 82  ? 0.37199 0.35773 0.38501 0.01775  -0.01702 -0.02903 234 ILE   A CG2  
439  C  CD1  . ILE   A 82  ? 0.38272 0.36919 0.39002 0.01621  -0.01340 -0.01214 234 ILE   A CD1  
440  N  N    . GLN   A 83  ? 0.45710 0.43073 0.42275 0.02360  -0.01374 -0.02932 235 GLN   A N    
441  C  CA   . GLN   A 83  ? 0.47247 0.45476 0.43380 0.02392  -0.01578 -0.03237 235 GLN   A CA   
442  C  C    . GLN   A 83  ? 0.38024 0.36076 0.32977 0.01918  -0.01425 -0.03344 235 GLN   A C    
443  O  O    . GLN   A 83  ? 0.38327 0.37689 0.33453 0.01604  -0.01509 -0.03998 235 GLN   A O    
444  C  CB   . GLN   A 83  ? 0.44019 0.42176 0.39357 0.03004  -0.01732 -0.02643 235 GLN   A CB   
445  C  CG   . GLN   A 83  ? 0.49693 0.48472 0.46244 0.03463  -0.01866 -0.02591 235 GLN   A CG   
446  C  CD   . GLN   A 83  ? 0.61998 0.61145 0.58087 0.04120  -0.02105 -0.02120 235 GLN   A CD   
447  O  OE1  . GLN   A 83  ? 0.56396 0.56513 0.52097 0.04102  -0.02427 -0.02128 235 GLN   A OE1  
448  N  NE2  . GLN   A 83  ? 0.74912 0.73520 0.71114 0.04703  -0.01960 -0.01727 235 GLN   A NE2  
449  N  N    . LYS   A 84  ? 0.40968 0.37602 0.34762 0.01791  -0.01179 -0.02798 236 LYS   A N    
450  C  CA   . LYS   A 84  ? 0.56402 0.52905 0.49099 0.01226  -0.01018 -0.02755 236 LYS   A CA   
451  C  C    . LYS   A 84  ? 0.48050 0.45377 0.41774 0.00707  -0.00878 -0.03568 236 LYS   A C    
452  O  O    . LYS   A 84  ? 0.44327 0.42733 0.37764 0.00263  -0.00792 -0.04015 236 LYS   A O    
453  C  CB   . LYS   A 84  ? 0.53464 0.48122 0.44938 0.01156  -0.00824 -0.02041 236 LYS   A CB   
454  C  CG   . LYS   A 84  ? 0.52688 0.46267 0.43667 0.01829  -0.00946 -0.01385 236 LYS   A CG   
455  C  CD   . LYS   A 84  ? 0.59633 0.54122 0.50312 0.02136  -0.01297 -0.00969 236 LYS   A CD   
456  C  CE   . LYS   A 84  ? 0.56502 0.50486 0.45850 0.01742  -0.01380 -0.00127 236 LYS   A CE   
457  N  NZ   . LYS   A 84  ? 0.55797 0.47473 0.44624 0.01830  -0.01255 0.00454  236 LYS   A NZ   
458  N  N    . VAL   A 85  ? 0.42958 0.39986 0.37995 0.00750  -0.00868 -0.03724 237 VAL   A N    
459  C  CA   . VAL   A 85  ? 0.47185 0.44938 0.43668 0.00383  -0.00833 -0.04397 237 VAL   A CA   
460  C  C    . VAL   A 85  ? 0.42660 0.41989 0.40555 0.00417  -0.00989 -0.05459 237 VAL   A C    
461  O  O    . VAL   A 85  ? 0.38602 0.38936 0.37189 0.00094  -0.00868 -0.06325 237 VAL   A O    
462  C  CB   . VAL   A 85  ? 0.41716 0.38968 0.39483 0.00427  -0.00930 -0.04037 237 VAL   A CB   
463  C  CG1  . VAL   A 85  ? 0.40003 0.38041 0.39864 0.00191  -0.01045 -0.04624 237 VAL   A CG1  
464  C  CG2  . VAL   A 85  ? 0.38042 0.34117 0.34358 0.00241  -0.00729 -0.03324 237 VAL   A CG2  
465  N  N    . ILE   A 86  ? 0.37623 0.37359 0.36063 0.00789  -0.01241 -0.05556 238 ILE   A N    
466  C  CA   . ILE   A 86  ? 0.31979 0.33308 0.31782 0.00762  -0.01416 -0.06765 238 ILE   A CA   
467  C  C    . ILE   A 86  ? 0.29748 0.32414 0.28064 0.00448  -0.01260 -0.07276 238 ILE   A C    
468  O  O    . ILE   A 86  ? 0.41979 0.46162 0.41216 0.00155  -0.01162 -0.08581 238 ILE   A O    
469  C  CB   . ILE   A 86  ? 0.39458 0.41047 0.40026 0.01136  -0.01748 -0.06676 238 ILE   A CB   
470  C  CG1  . ILE   A 86  ? 0.38376 0.39091 0.40650 0.01274  -0.01895 -0.06144 238 ILE   A CG1  
471  C  CG2  . ILE   A 86  ? 0.37530 0.40903 0.39340 0.01013  -0.01947 -0.08096 238 ILE   A CG2  
472  C  CD1  . ILE   A 86  ? 0.43201 0.43860 0.45424 0.01632  -0.02077 -0.05476 238 ILE   A CD1  
473  N  N    . GLY   A 87  ? 0.40751 0.43012 0.36872 0.00484  -0.01246 -0.06238 239 GLY   A N    
474  C  CA   . GLY   A 87  ? 0.36854 0.40545 0.31422 0.00058  -0.01156 -0.06324 239 GLY   A CA   
475  C  C    . GLY   A 87  ? 0.41199 0.45349 0.35513 -0.00540 -0.00763 -0.06744 239 GLY   A C    
476  O  O    . GLY   A 87  ? 0.39821 0.46096 0.33947 -0.00998 -0.00609 -0.07654 239 GLY   A O    
477  N  N    . PHE   A 88  ? 0.37739 0.40200 0.32067 -0.00591 -0.00582 -0.06163 240 PHE   A N    
478  C  CA   . PHE   A 88  ? 0.33538 0.36522 0.27920 -0.01156 -0.00227 -0.06581 240 PHE   A CA   
479  C  C    . PHE   A 88  ? 0.29689 0.34174 0.26429 -0.01135 -0.00161 -0.08235 240 PHE   A C    
480  O  O    . PHE   A 88  ? 0.42495 0.48888 0.39374 -0.01566 0.00127  -0.09252 240 PHE   A O    
481  C  CB   . PHE   A 88  ? 0.31889 0.32846 0.25948 -0.01218 -0.00132 -0.05657 240 PHE   A CB   
482  C  CG   . PHE   A 88  ? 0.43596 0.45122 0.38024 -0.01779 0.00178  -0.06060 240 PHE   A CG   
483  C  CD1  . PHE   A 88  ? 0.35201 0.37245 0.28027 -0.02477 0.00458  -0.05665 240 PHE   A CD1  
484  C  CD2  . PHE   A 88  ? 0.40403 0.42022 0.36920 -0.01638 0.00143  -0.06685 240 PHE   A CD2  
485  C  CE1  . PHE   A 88  ? 0.33155 0.35946 0.26409 -0.03030 0.00760  -0.06050 240 PHE   A CE1  
486  C  CE2  . PHE   A 88  ? 0.38773 0.41093 0.35821 -0.02093 0.00389  -0.07039 240 PHE   A CE2  
487  C  CZ   . PHE   A 88  ? 0.41972 0.44936 0.37357 -0.02792 0.00729  -0.06795 240 PHE   A CZ   
488  N  N    . ALA   A 89  ? 0.35474 0.39212 0.34266 -0.00650 -0.00431 -0.08530 241 ALA   A N    
489  C  CA   . ALA   A 89  ? 0.33531 0.38255 0.35113 -0.00554 -0.00464 -0.09994 241 ALA   A CA   
490  C  C    . ALA   A 89  ? 0.42926 0.49960 0.45086 -0.00670 -0.00392 -0.11694 241 ALA   A C    
491  O  O    . ALA   A 89  ? 0.41585 0.50084 0.45417 -0.00792 -0.00183 -0.13236 241 ALA   A O    
492  C  CB   . ALA   A 89  ? 0.33633 0.37089 0.37316 -0.00097 -0.00876 -0.09665 241 ALA   A CB   
493  N  N    . LYS   A 90  ? 0.36794 0.44398 0.37684 -0.00632 -0.00569 -0.11536 242 LYS   A N    
494  C  CA   . LYS   A 90  ? 0.29648 0.39794 0.30905 -0.00834 -0.00546 -0.13206 242 LYS   A CA   
495  C  C    . LYS   A 90  ? 0.30663 0.43039 0.30710 -0.01452 -0.00064 -0.13947 242 LYS   A C    
496  O  O    . LYS   A 90  ? 0.37198 0.52084 0.38238 -0.01675 0.00109  -0.15912 242 LYS   A O    
497  C  CB   . LYS   A 90  ? 0.33788 0.44312 0.33527 -0.00748 -0.00883 -0.12535 242 LYS   A CB   
498  C  CG   . LYS   A 90  ? 0.40713 0.50076 0.42098 -0.00241 -0.01335 -0.12429 242 LYS   A CG   
499  C  CD   . LYS   A 90  ? 0.62179 0.73102 0.62777 -0.00257 -0.01662 -0.12649 242 LYS   A CD   
500  C  CE   . LYS   A 90  ? 0.66362 0.76978 0.64062 -0.00241 -0.01742 -0.10768 242 LYS   A CE   
501  N  NZ   . LYS   A 90  ? 0.66887 0.78441 0.64219 -0.00033 -0.02213 -0.10486 242 LYS   A NZ   
502  N  N    . MET   A 91  ? 0.37637 0.49303 0.35631 -0.01798 0.00174  -0.12491 243 MET   A N    
503  C  CA   . MET   A 91  ? 0.44146 0.58017 0.40788 -0.02535 0.00642  -0.12843 243 MET   A CA   
504  C  C    . MET   A 91  ? 0.48012 0.62171 0.46205 -0.02668 0.01048  -0.13718 243 MET   A C    
505  O  O    . MET   A 91  ? 0.39943 0.56180 0.37256 -0.03326 0.01511  -0.14129 243 MET   A O    
506  C  CB   . MET   A 91  ? 0.55698 0.68735 0.49363 -0.02968 0.00622  -0.10654 243 MET   A CB   
507  C  CG   . MET   A 91  ? 0.70043 0.82705 0.62360 -0.02724 0.00147  -0.09560 243 MET   A CG   
508  S  SD   . MET   A 91  ? 0.73988 0.86295 0.63203 -0.03304 0.00057  -0.07134 243 MET   A SD   
509  C  CE   . MET   A 91  ? 0.61687 0.70125 0.50847 -0.02442 -0.00378 -0.05468 243 MET   A CE   
510  N  N    . ILE   A 92  ? 0.49897 0.62254 0.50424 -0.02104 0.00862  -0.13902 244 ILE   A N    
511  C  CA   . ILE   A 92  ? 0.44326 0.57233 0.46801 -0.02133 0.01154  -0.14824 244 ILE   A CA   
512  C  C    . ILE   A 92  ? 0.40694 0.56593 0.45035 -0.02178 0.01466  -0.17383 244 ILE   A C    
513  O  O    . ILE   A 92  ? 0.39939 0.56266 0.45954 -0.01795 0.01215  -0.18712 244 ILE   A O    
514  C  CB   . ILE   A 92  ? 0.42697 0.53278 0.47543 -0.01510 0.00749  -0.14344 244 ILE   A CB   
515  C  CG1  . ILE   A 92  ? 0.37793 0.45788 0.40743 -0.01506 0.00503  -0.12082 244 ILE   A CG1  
516  C  CG2  . ILE   A 92  ? 0.34342 0.45668 0.41476 -0.01475 0.00952  -0.15207 244 ILE   A CG2  
517  C  CD1  . ILE   A 92  ? 0.33513 0.39649 0.38480 -0.01032 0.00085  -0.11412 244 ILE   A CD1  
518  N  N    . PRO   A 93  ? 0.39071 0.57258 0.43320 -0.02670 0.02028  -0.18297 245 PRO   A N    
519  C  CA   . PRO   A 93  ? 0.46618 0.67997 0.52836 -0.02685 0.02412  -0.21077 245 PRO   A CA   
520  C  C    . PRO   A 93  ? 0.54142 0.74611 0.64576 -0.01815 0.02107  -0.22642 245 PRO   A C    
521  O  O    . PRO   A 93  ? 0.50818 0.69663 0.63172 -0.01413 0.01936  -0.22068 245 PRO   A O    
522  C  CB   . PRO   A 93  ? 0.50682 0.74258 0.56237 -0.03327 0.03075  -0.21355 245 PRO   A CB   
523  C  CG   . PRO   A 93  ? 0.54055 0.76118 0.56238 -0.03950 0.03034  -0.18629 245 PRO   A CG   
524  C  CD   . PRO   A 93  ? 0.42452 0.60676 0.44681 -0.03335 0.02374  -0.16903 245 PRO   A CD   
525  N  N    . GLY   A 94  ? 0.52067 0.73618 0.64053 -0.01571 0.01970  -0.24551 246 GLY   A N    
526  C  CA   . GLY   A 94  ? 0.42739 0.63392 0.59023 -0.00807 0.01614  -0.26128 246 GLY   A CA   
527  C  C    . GLY   A 94  ? 0.44863 0.62436 0.61990 -0.00355 0.00851  -0.24741 246 GLY   A C    
528  O  O    . GLY   A 94  ? 0.50775 0.67766 0.71423 0.00137  0.00479  -0.26088 246 GLY   A O    
529  N  N    . PHE   A 95  ? 0.48301 0.63972 0.62465 -0.00534 0.00615  -0.22145 247 PHE   A N    
530  C  CA   . PHE   A 95  ? 0.50575 0.63601 0.65489 -0.00148 -0.00040 -0.20751 247 PHE   A CA   
531  C  C    . PHE   A 95  ? 0.57359 0.71113 0.73361 -0.00080 -0.00320 -0.22186 247 PHE   A C    
532  O  O    . PHE   A 95  ? 0.57778 0.69970 0.76412 0.00291  -0.00846 -0.22168 247 PHE   A O    
533  C  CB   . PHE   A 95  ? 0.42812 0.54153 0.54214 -0.00356 -0.00126 -0.18071 247 PHE   A CB   
534  C  CG   . PHE   A 95  ? 0.43166 0.52066 0.55225 0.00005  -0.00701 -0.16547 247 PHE   A CG   
535  C  CD1  . PHE   A 95  ? 0.40018 0.47110 0.53855 0.00280  -0.00999 -0.15422 247 PHE   A CD1  
536  C  CD2  . PHE   A 95  ? 0.38632 0.47365 0.49557 0.00017  -0.00955 -0.16183 247 PHE   A CD2  
537  C  CE1  . PHE   A 95  ? 0.48588 0.53867 0.62942 0.00488  -0.01485 -0.13965 247 PHE   A CE1  
538  C  CE2  . PHE   A 95  ? 0.45065 0.51899 0.56638 0.00292  -0.01417 -0.14823 247 PHE   A CE2  
539  C  CZ   . PHE   A 95  ? 0.38468 0.43631 0.51705 0.00492  -0.01656 -0.13715 247 PHE   A CZ   
540  N  N    A ARG   A 96  ? 0.67131 0.83422 0.81177 -0.00528 -0.00011 -0.23367 248 ARG   A N    
541  N  N    B ARG   A 96  ? 0.67040 0.83331 0.81091 -0.00528 -0.00012 -0.23369 248 ARG   A N    
542  C  CA   A ARG   A 96  ? 0.68304 0.85660 0.83093 -0.00581 -0.00298 -0.24788 248 ARG   A CA   
543  C  CA   B ARG   A 96  ? 0.68307 0.85615 0.83149 -0.00571 -0.00307 -0.24780 248 ARG   A CA   
544  C  C    A ARG   A 96  ? 0.71383 0.89690 0.90416 -0.00330 -0.00337 -0.27723 248 ARG   A C    
545  C  C    B ARG   A 96  ? 0.71452 0.89576 0.90624 -0.00299 -0.00364 -0.27646 248 ARG   A C    
546  O  O    A ARG   A 96  ? 0.76969 0.95199 0.97744 -0.00274 -0.00751 -0.28777 248 ARG   A O    
547  O  O    B ARG   A 96  ? 0.76674 0.94395 0.97838 -0.00190 -0.00817 -0.28552 248 ARG   A O    
548  C  CB   A ARG   A 96  ? 0.67691 0.87918 0.79122 -0.01213 -0.00007 -0.25142 248 ARG   A CB   
549  C  CB   B ARG   A 96  ? 0.67803 0.88022 0.79337 -0.01203 -0.00015 -0.25195 248 ARG   A CB   
550  C  CG   A ARG   A 96  ? 0.62056 0.81203 0.69661 -0.01410 -0.00105 -0.22261 248 ARG   A CG   
551  C  CG   B ARG   A 96  ? 0.76081 0.98327 0.88421 -0.01395 -0.00253 -0.27200 248 ARG   A CG   
552  C  CD   A ARG   A 96  ? 0.63383 0.79626 0.71348 -0.00944 -0.00688 -0.20498 248 ARG   A CD   
553  C  CD   B ARG   A 96  ? 0.75144 0.95187 0.88155 -0.01094 -0.00942 -0.26011 248 ARG   A CD   
554  N  NE   A ARG   A 96  ? 0.60587 0.77680 0.66794 -0.01086 -0.01023 -0.19999 248 ARG   A NE   
555  N  NE   B ARG   A 96  ? 0.75397 0.94855 0.92600 -0.00823 -0.01273 -0.27963 248 ARG   A NE   
556  C  CZ   A ARG   A 96  ? 0.59452 0.75395 0.66816 -0.00786 -0.01534 -0.19675 248 ARG   A CZ   
557  C  CZ   B ARG   A 96  ? 0.81173 0.98674 0.99941 -0.00606 -0.01871 -0.27181 248 ARG   A CZ   
558  N  NH1  A ARG   A 96  ? 0.67837 0.84877 0.73579 -0.00916 -0.01842 -0.19217 248 ARG   A NH1  
559  N  NH1  B ARG   A 96  ? 0.82886 0.99017 0.99334 -0.00552 -0.02144 -0.24647 248 ARG   A NH1  
560  N  NH2  A ARG   A 96  ? 0.50608 0.64460 0.60838 -0.00400 -0.01775 -0.19677 248 ARG   A NH2  
561  N  NH2  B ARG   A 96  ? 0.85364 1.02331 1.08212 -0.00461 -0.02194 -0.28964 248 ARG   A NH2  
562  N  N    . ASP   A 97  ? 0.75029 0.94253 0.95962 -0.00176 0.00071  -0.29128 249 ASP   A N    
563  C  CA   . ASP   A 97  ? 0.78540 0.98551 1.03993 0.00184  0.00039  -0.32007 249 ASP   A CA   
564  C  C    . ASP   A 97  ? 0.67713 0.84520 0.97033 0.00779  -0.00694 -0.31338 249 ASP   A C    
565  O  O    . ASP   A 97  ? 0.66976 0.84116 1.00190 0.01038  -0.00925 -0.32663 249 ASP   A O    
566  C  CB   . ASP   A 97  ? 0.89945 1.11895 1.16522 0.00254  0.00654  -0.33091 249 ASP   A CB   
567  C  CG   . ASP   A 97  ? 0.99800 1.25299 1.22861 -0.00485 0.01384  -0.33571 249 ASP   A CG   
568  O  OD1  . ASP   A 97  ? 1.02308 1.29274 1.22928 -0.00993 0.01373  -0.33510 249 ASP   A OD1  
569  O  OD2  . ASP   A 97  ? 1.04233 1.31213 1.27076 -0.00605 0.01935  -0.33900 249 ASP   A OD2  
570  N  N    . LEU   A 98  ? 0.46177 0.60287 0.74362 0.00907  -0.01072 -0.28237 250 LEU   A N    
571  C  CA   . LEU   A 98  ? 0.48371 0.59720 0.79684 0.01276  -0.01824 -0.27063 250 LEU   A CA   
572  C  C    . LEU   A 98  ? 0.49187 0.60254 0.80690 0.01048  -0.02252 -0.27337 250 LEU   A C    
573  O  O    . LEU   A 98  ? 0.53368 0.65836 0.81636 0.00644  -0.02053 -0.27407 250 LEU   A O    
574  C  CB   . LEU   A 98  ? 0.56332 0.65454 0.85913 0.01338  -0.02045 -0.23717 250 LEU   A CB   
575  C  CG   . LEU   A 98  ? 0.48546 0.57809 0.77667 0.01466  -0.01709 -0.23026 250 LEU   A CG   
576  C  CD1  . LEU   A 98  ? 0.50625 0.58203 0.76815 0.01307  -0.01825 -0.19919 250 LEU   A CD1  
577  C  CD2  . LEU   A 98  ? 0.44264 0.52956 0.78314 0.02007  -0.02049 -0.23905 250 LEU   A CD2  
578  N  N    . THR   A 99  ? 0.51482 0.60770 0.86983 0.01274  -0.02905 -0.27358 251 THR   A N    
579  C  CA   . THR   A 99  ? 0.50959 0.59685 0.86826 0.00989  -0.03388 -0.27153 251 THR   A CA   
580  C  C    . THR   A 99  ? 0.52919 0.60519 0.85114 0.00808  -0.03495 -0.24031 251 THR   A C    
581  O  O    . THR   A 99  ? 0.44650 0.51209 0.75069 0.00944  -0.03369 -0.21872 251 THR   A O    
582  C  CB   . THR   A 99  ? 0.59482 0.66335 1.00584 0.01177  -0.04111 -0.27379 251 THR   A CB   
583  O  OG1  . THR   A 99  ? 0.58829 0.63400 1.00740 0.01398  -0.04497 -0.24528 251 THR   A OG1  
584  C  CG2  . THR   A 99  ? 0.61387 0.69866 1.05928 0.01537  -0.03889 -0.29396 251 THR   A CG2  
585  N  N    . SER   A 100 ? 0.50979 0.58969 0.82146 0.00494  -0.03724 -0.23961 252 SER   A N    
586  C  CA   . SER   A 100 ? 0.45440 0.52465 0.73664 0.00403  -0.03843 -0.21233 252 SER   A CA   
587  C  C    . SER   A 100 ? 0.41916 0.46576 0.71851 0.00541  -0.04254 -0.18867 252 SER   A C    
588  O  O    . SER   A 100 ? 0.48849 0.52717 0.76156 0.00585  -0.04138 -0.16563 252 SER   A O    
589  C  CB   . SER   A 100 ? 0.53088 0.61037 0.80839 0.00081  -0.04121 -0.21707 252 SER   A CB   
590  O  OG   . SER   A 100 ? 0.66717 0.77184 0.92141 -0.00125 -0.03777 -0.23402 252 SER   A OG   
591  N  N    . ASP   A 101 ? 0.42419 0.46048 0.76839 0.00575  -0.04757 -0.19402 253 ASP   A N    
592  C  CA   . ASP   A 101 ? 0.45118 0.46800 0.81407 0.00603  -0.05235 -0.16975 253 ASP   A CA   
593  C  C    . ASP   A 101 ? 0.43811 0.45049 0.78815 0.00887  -0.04969 -0.15688 253 ASP   A C    
594  O  O    . ASP   A 101 ? 0.42585 0.43041 0.75758 0.00806  -0.05011 -0.13212 253 ASP   A O    
595  C  CB   . ASP   A 101 ? 0.49988 0.50667 0.91763 0.00575  -0.05901 -0.17846 253 ASP   A CB   
596  C  CG   . ASP   A 101 ? 0.77594 0.78741 1.20936 0.00186  -0.06197 -0.19334 253 ASP   A CG   
597  O  OD1  . ASP   A 101 ? 0.84165 0.86734 1.28032 0.00199  -0.05964 -0.22263 253 ASP   A OD1  
598  O  OD2  . ASP   A 101 ? 0.78490 0.78831 1.22509 -0.00204 -0.06651 -0.17616 253 ASP   A OD2  
599  N  N    . ASP   A 102 ? 0.45370 0.47339 0.81348 0.01181  -0.04671 -0.17470 254 ASP   A N    
600  C  CA   . ASP   A 102 ? 0.42510 0.44278 0.77446 0.01400  -0.04432 -0.16382 254 ASP   A CA   
601  C  C    . ASP   A 102 ? 0.46198 0.48488 0.75968 0.01228  -0.03864 -0.15214 254 ASP   A C    
602  O  O    . ASP   A 102 ? 0.45737 0.47344 0.74037 0.01215  -0.03828 -0.13302 254 ASP   A O    
603  C  CB   . ASP   A 102 ? 0.46627 0.49424 0.83823 0.01748  -0.04174 -0.18761 254 ASP   A CB   
604  C  CG   . ASP   A 102 ? 0.60375 0.62042 1.03040 0.02098  -0.04835 -0.18995 254 ASP   A CG   
605  O  OD1  . ASP   A 102 ? 0.56783 0.59291 1.02290 0.02468  -0.04697 -0.21422 254 ASP   A OD1  
606  O  OD2  . ASP   A 102 ? 0.60571 0.60628 1.04824 0.01992  -0.05505 -0.16719 254 ASP   A OD2  
607  N  N    . GLN   A 103 ? 0.44042 0.47587 0.71144 0.01064  -0.03469 -0.16317 255 GLN   A N    
608  C  CA   . GLN   A 103 ? 0.45757 0.49555 0.68290 0.00918  -0.03037 -0.15056 255 GLN   A CA   
609  C  C    . GLN   A 103 ? 0.49071 0.51491 0.70370 0.00857  -0.03300 -0.12613 255 GLN   A C    
610  O  O    . GLN   A 103 ? 0.32612 0.34557 0.51170 0.00826  -0.03049 -0.11116 255 GLN   A O    
611  C  CB   . GLN   A 103 ? 0.45718 0.51218 0.66058 0.00741  -0.02734 -0.16461 255 GLN   A CB   
612  C  CG   . GLN   A 103 ? 0.59345 0.66855 0.80039 0.00667  -0.02319 -0.18873 255 GLN   A CG   
613  C  CD   . GLN   A 103 ? 0.57861 0.67442 0.76387 0.00368  -0.02120 -0.20090 255 GLN   A CD   
614  O  OE1  . GLN   A 103 ? 0.51363 0.60942 0.66731 0.00248  -0.02084 -0.18681 255 GLN   A OE1  
615  N  NE2  . GLN   A 103 ? 0.60989 0.72493 0.81346 0.00251  -0.02023 -0.22757 255 GLN   A NE2  
616  N  N    . ILE   A 104 ? 0.36846 0.38744 0.60261 0.00788  -0.03788 -0.12275 256 ILE   A N    
617  C  CA   . ILE   A 104 ? 0.45016 0.46092 0.67316 0.00672  -0.03976 -0.10110 256 ILE   A CA   
618  C  C    . ILE   A 104 ? 0.32487 0.32549 0.55682 0.00622  -0.04191 -0.08247 256 ILE   A C    
619  O  O    . ILE   A 104 ? 0.40014 0.39783 0.60743 0.00553  -0.04009 -0.06621 256 ILE   A O    
620  C  CB   . ILE   A 104 ? 0.41739 0.42882 0.66117 0.00485  -0.04423 -0.10296 256 ILE   A CB   
621  C  CG1  . ILE   A 104 ? 0.44203 0.46611 0.66622 0.00482  -0.04215 -0.11546 256 ILE   A CG1  
622  C  CG2  . ILE   A 104 ? 0.40210 0.40659 0.64508 0.00285  -0.04674 -0.07962 256 ILE   A CG2  
623  C  CD1  . ILE   A 104 ? 0.41693 0.44411 0.66035 0.00231  -0.04654 -0.11840 256 ILE   A CD1  
624  N  N    . VAL   A 105 ? 0.31449 0.31082 0.58315 0.00653  -0.04618 -0.08482 257 VAL   A N    
625  C  CA   . VAL   A 105 ? 0.45569 0.44514 0.73469 0.00553  -0.04953 -0.06494 257 VAL   A CA   
626  C  C    . VAL   A 105 ? 0.38226 0.37392 0.63459 0.00635  -0.04506 -0.06149 257 VAL   A C    
627  O  O    . VAL   A 105 ? 0.35511 0.34460 0.59531 0.00433  -0.04573 -0.04293 257 VAL   A O    
628  C  CB   . VAL   A 105 ? 0.52494 0.50887 0.85333 0.00632  -0.05621 -0.06711 257 VAL   A CB   
629  C  CG1  . VAL   A 105 ? 0.53298 0.51387 0.88897 0.00456  -0.06057 -0.07297 257 VAL   A CG1  
630  C  CG2  . VAL   A 105 ? 0.59331 0.58137 0.93586 0.01042  -0.05413 -0.08772 257 VAL   A CG2  
631  N  N    . LEU   A 106 ? 0.35866 0.35680 0.60069 0.00833  -0.04032 -0.07932 258 LEU   A N    
632  C  CA   . LEU   A 106 ? 0.47278 0.47348 0.69033 0.00796  -0.03605 -0.07619 258 LEU   A CA   
633  C  C    . LEU   A 106 ? 0.39841 0.39695 0.57502 0.00603  -0.03224 -0.06520 258 LEU   A C    
634  O  O    . LEU   A 106 ? 0.31813 0.31395 0.47905 0.00423  -0.03135 -0.05269 258 LEU   A O    
635  C  CB   . LEU   A 106 ? 0.37694 0.38816 0.59387 0.00940  -0.03158 -0.09761 258 LEU   A CB   
636  C  CG   . LEU   A 106 ? 0.32513 0.34035 0.58223 0.01227  -0.03400 -0.11062 258 LEU   A CG   
637  C  CD1  . LEU   A 106 ? 0.32350 0.35427 0.57489 0.01290  -0.02803 -0.13333 258 LEU   A CD1  
638  C  CD2  . LEU   A 106 ? 0.35139 0.36201 0.62228 0.01257  -0.03751 -0.09523 258 LEU   A CD2  
639  N  N    . LEU   A 107 ? 0.42055 0.42094 0.58132 0.00648  -0.03033 -0.07032 259 LEU   A N    
640  C  CA   . LEU   A 107 ? 0.42883 0.42632 0.55492 0.00593  -0.02712 -0.06080 259 LEU   A CA   
641  C  C    . LEU   A 107 ? 0.40402 0.39639 0.53041 0.00479  -0.02956 -0.04340 259 LEU   A C    
642  O  O    . LEU   A 107 ? 0.33101 0.32041 0.43439 0.00383  -0.02712 -0.03373 259 LEU   A O    
643  C  CB   . LEU   A 107 ? 0.40785 0.41075 0.52022 0.00727  -0.02540 -0.06996 259 LEU   A CB   
644  C  CG   . LEU   A 107 ? 0.51926 0.53031 0.61588 0.00682  -0.02143 -0.08235 259 LEU   A CG   
645  C  CD1  . LEU   A 107 ? 0.56864 0.59043 0.66139 0.00742  -0.02155 -0.09351 259 LEU   A CD1  
646  C  CD2  . LEU   A 107 ? 0.52686 0.53238 0.59237 0.00569  -0.01771 -0.07283 259 LEU   A CD2  
647  N  N    . LYS   A 108 ? 0.40468 0.39736 0.55756 0.00421  -0.03425 -0.03971 260 LYS   A N    
648  C  CA   . LYS   A 108 ? 0.43771 0.42983 0.59267 0.00171  -0.03661 -0.02184 260 LYS   A CA   
649  C  C    . LYS   A 108 ? 0.45492 0.44660 0.60837 -0.00082 -0.03753 -0.00958 260 LYS   A C    
650  O  O    . LYS   A 108 ? 0.45758 0.45164 0.59291 -0.00304 -0.03609 0.00234  260 LYS   A O    
651  C  CB   . LYS   A 108 ? 0.35453 0.34739 0.54313 0.00004  -0.04233 -0.01859 260 LYS   A CB   
652  C  CG   . LYS   A 108 ? 0.48833 0.48497 0.67307 0.00009  -0.04198 -0.02007 260 LYS   A CG   
653  C  CD   . LYS   A 108 ? 0.49395 0.49081 0.71459 -0.00324 -0.04813 -0.01511 260 LYS   A CD   
654  C  CE   . LYS   A 108 ? 0.70194 0.70142 0.92936 -0.00803 -0.05105 0.00780  260 LYS   A CE   
655  N  NZ   . LYS   A 108 ? 0.79543 0.79777 1.04976 -0.01258 -0.05600 0.01614  260 LYS   A NZ   
656  N  N    . SER   A 109 ? 0.31168 0.30250 0.48480 -0.00053 -0.03993 -0.01332 261 SER   A N    
657  C  CA   . SER   A 109 ? 0.41651 0.40939 0.59224 -0.00325 -0.04221 -0.00037 261 SER   A CA   
658  C  C    . SER   A 109 ? 0.33532 0.32855 0.47917 -0.00390 -0.03686 -0.00324 261 SER   A C    
659  O  O    . SER   A 109 ? 0.35774 0.35433 0.48894 -0.00740 -0.03704 0.00861  261 SER   A O    
660  C  CB   . SER   A 109 ? 0.49042 0.48292 0.70374 -0.00199 -0.04761 -0.00240 261 SER   A CB   
661  O  OG   . SER   A 109 ? 0.59277 0.58944 0.80959 -0.00452 -0.05065 0.01117  261 SER   A OG   
662  N  N    . SER   A 110 ? 0.38486 0.37611 0.51531 -0.00153 -0.03222 -0.01857 262 SER   A N    
663  C  CA   . SER   A 110 ? 0.35053 0.34132 0.45527 -0.00306 -0.02767 -0.02141 262 SER   A CA   
664  C  C    . SER   A 110 ? 0.34244 0.32851 0.41386 -0.00343 -0.02307 -0.02006 262 SER   A C    
665  O  O    . SER   A 110 ? 0.33583 0.31968 0.38694 -0.00588 -0.02006 -0.01928 262 SER   A O    
666  C  CB   . SER   A 110 ? 0.46270 0.45661 0.57195 -0.00152 -0.02515 -0.03723 262 SER   A CB   
667  O  OG   . SER   A 110 ? 0.45273 0.44588 0.54299 -0.00021 -0.02114 -0.04642 262 SER   A OG   
668  N  N    . ALA   A 111 ? 0.40091 0.38544 0.46845 -0.00105 -0.02276 -0.01989 263 ALA   A N    
669  C  CA   . ALA   A 111 ? 0.37884 0.35856 0.41865 0.00036  -0.01860 -0.02083 263 ALA   A CA   
670  C  C    . ALA   A 111 ? 0.34313 0.32012 0.36411 -0.00240 -0.01649 -0.01344 263 ALA   A C    
671  O  O    . ALA   A 111 ? 0.34244 0.31303 0.34293 -0.00293 -0.01301 -0.01674 263 ALA   A O    
672  C  CB   . ALA   A 111 ? 0.40237 0.38376 0.44527 0.00345  -0.01943 -0.01978 263 ALA   A CB   
673  N  N    . ILE   A 112 ? 0.33313 0.31611 0.36140 -0.00495 -0.01878 -0.00341 264 ILE   A N    
674  C  CA   . ILE   A 112 ? 0.34082 0.32498 0.35080 -0.00822 -0.01656 0.00141  264 ILE   A CA   
675  C  C    . ILE   A 112 ? 0.38313 0.36544 0.38646 -0.01219 -0.01601 -0.00057 264 ILE   A C    
676  O  O    . ILE   A 112 ? 0.36195 0.34052 0.34542 -0.01456 -0.01288 -0.00243 264 ILE   A O    
677  C  CB   . ILE   A 112 ? 0.39677 0.39336 0.41578 -0.01148 -0.01932 0.01341  264 ILE   A CB   
678  C  CG1  . ILE   A 112 ? 0.42109 0.42226 0.41836 -0.01438 -0.01579 0.01476  264 ILE   A CG1  
679  C  CG2  . ILE   A 112 ? 0.38445 0.38838 0.42616 -0.01525 -0.02507 0.02215  264 ILE   A CG2  
680  C  CD1  . ILE   A 112 ? 0.51523 0.50884 0.49530 -0.00939 -0.01069 0.00653  264 ILE   A CD1  
681  N  N    . GLU   A 113 ? 0.33401 0.31926 0.35539 -0.01299 -0.01897 -0.00138 265 GLU   A N    
682  C  CA   . GLU   A 113 ? 0.33897 0.32495 0.35579 -0.01688 -0.01839 -0.00357 265 GLU   A CA   
683  C  C    . GLU   A 113 ? 0.35533 0.33232 0.35449 -0.01642 -0.01368 -0.01345 265 GLU   A C    
684  O  O    . GLU   A 113 ? 0.39147 0.36511 0.37453 -0.02065 -0.01136 -0.01448 265 GLU   A O    
685  C  CB   . GLU   A 113 ? 0.32362 0.31707 0.36820 -0.01683 -0.02286 -0.00231 265 GLU   A CB   
686  C  CG   . GLU   A 113 ? 0.30897 0.31114 0.37451 -0.01801 -0.02891 0.01085  265 GLU   A CG   
687  C  CD   . GLU   A 113 ? 0.42994 0.43716 0.52794 -0.01657 -0.03405 0.01184  265 GLU   A CD   
688  O  OE1  . GLU   A 113 ? 0.38752 0.39557 0.48824 -0.01614 -0.03245 0.00288  265 GLU   A OE1  
689  O  OE2  . GLU   A 113 ? 0.37842 0.38930 0.50103 -0.01593 -0.03975 0.02166  265 GLU   A OE2  
690  N  N    . VAL   A 114 ? 0.41895 0.39321 0.42121 -0.01223 -0.01260 -0.02020 266 VAL   A N    
691  C  CA   . VAL   A 114 ? 0.39677 0.36504 0.38180 -0.01259 -0.00875 -0.02674 266 VAL   A CA   
692  C  C    . VAL   A 114 ? 0.31035 0.26751 0.27287 -0.01244 -0.00620 -0.02409 266 VAL   A C    
693  O  O    . VAL   A 114 ? 0.43794 0.38778 0.38484 -0.01548 -0.00363 -0.02550 266 VAL   A O    
694  C  CB   . VAL   A 114 ? 0.43042 0.40254 0.42329 -0.00870 -0.00872 -0.03412 266 VAL   A CB   
695  C  CG1  . VAL   A 114 ? 0.31510 0.28561 0.29065 -0.01063 -0.00531 -0.03859 266 VAL   A CG1  
696  C  CG2  . VAL   A 114 ? 0.36361 0.34612 0.38342 -0.00802 -0.01131 -0.03923 266 VAL   A CG2  
697  N  N    . ILE   A 115 ? 0.40895 0.36512 0.37145 -0.00904 -0.00688 -0.02043 267 ILE   A N    
698  C  CA   . ILE   A 115 ? 0.36403 0.31088 0.30889 -0.00788 -0.00429 -0.01980 267 ILE   A CA   
699  C  C    . ILE   A 115 ? 0.41099 0.35565 0.34603 -0.01382 -0.00304 -0.01929 267 ILE   A C    
700  O  O    . ILE   A 115 ? 0.38147 0.31472 0.30181 -0.01515 -0.00051 -0.02211 267 ILE   A O    
701  C  CB   . ILE   A 115 ? 0.42206 0.37317 0.37141 -0.00330 -0.00484 -0.01698 267 ILE   A CB   
702  C  CG1  . ILE   A 115 ? 0.34967 0.30080 0.30440 0.00243  -0.00571 -0.01895 267 ILE   A CG1  
703  C  CG2  . ILE   A 115 ? 0.38193 0.32737 0.31673 -0.00248 -0.00184 -0.01802 267 ILE   A CG2  
704  C  CD1  . ILE   A 115 ? 0.40498 0.36522 0.37253 0.00538  -0.00749 -0.01567 267 ILE   A CD1  
705  N  N    . MET   A 116 ? 0.35497 0.31092 0.29941 -0.01788 -0.00536 -0.01536 268 MET   A N    
706  C  CA   . MET   A 116 ? 0.44382 0.40156 0.37965 -0.02469 -0.00487 -0.01532 268 MET   A CA   
707  C  C    . MET   A 116 ? 0.44314 0.39344 0.37226 -0.02885 -0.00339 -0.01948 268 MET   A C    
708  O  O    . MET   A 116 ? 0.43918 0.38186 0.35463 -0.03335 -0.00132 -0.02259 268 MET   A O    
709  C  CB   . MET   A 116 ? 0.38184 0.35613 0.33162 -0.02844 -0.00898 -0.00804 268 MET   A CB   
710  C  CG   . MET   A 116 ? 0.50190 0.48700 0.45329 -0.02817 -0.01010 -0.00194 268 MET   A CG   
711  S  SD   . MET   A 116 ? 0.53825 0.54262 0.51327 -0.03128 -0.01688 0.01154  268 MET   A SD   
712  C  CE   . MET   A 116 ? 0.53995 0.55839 0.51058 -0.03251 -0.01668 0.01887  268 MET   A CE   
713  N  N    . LEU   A 117 ? 0.36462 0.31824 0.30419 -0.02794 -0.00423 -0.02040 269 LEU   A N    
714  C  CA   . LEU   A 117 ? 0.41626 0.36726 0.35026 -0.03280 -0.00241 -0.02373 269 LEU   A CA   
715  C  C    . LEU   A 117 ? 0.48601 0.42183 0.40335 -0.03243 0.00059  -0.02552 269 LEU   A C    
716  O  O    . LEU   A 117 ? 0.39787 0.32538 0.30384 -0.03831 0.00223  -0.02621 269 LEU   A O    
717  C  CB   . LEU   A 117 ? 0.38961 0.35168 0.33999 -0.03146 -0.00335 -0.02628 269 LEU   A CB   
718  C  CG   . LEU   A 117 ? 0.47207 0.44832 0.44313 -0.03252 -0.00685 -0.02438 269 LEU   A CG   
719  C  CD1  . LEU   A 117 ? 0.40987 0.39534 0.40093 -0.02861 -0.00751 -0.02995 269 LEU   A CD1  
720  C  CD2  . LEU   A 117 ? 0.49198 0.47305 0.45894 -0.04023 -0.00672 -0.02363 269 LEU   A CD2  
721  N  N    . ARG   A 118 ? 0.44525 0.37751 0.36249 -0.02594 0.00073  -0.02552 270 ARG   A N    
722  C  CA   . ARG   A 118 ? 0.44533 0.36449 0.34920 -0.02520 0.00238  -0.02465 270 ARG   A CA   
723  C  C    . ARG   A 118 ? 0.42355 0.32747 0.31713 -0.02458 0.00339  -0.02449 270 ARG   A C    
724  O  O    . ARG   A 118 ? 0.46894 0.35885 0.35303 -0.02620 0.00434  -0.02310 270 ARG   A O    
725  C  CB   . ARG   A 118 ? 0.44587 0.36823 0.35304 -0.01841 0.00146  -0.02428 270 ARG   A CB   
726  C  CG   . ARG   A 118 ? 0.46326 0.38433 0.37461 -0.01100 0.00034  -0.02369 270 ARG   A CG   
727  C  CD   . ARG   A 118 ? 0.61514 0.54604 0.53573 -0.00594 -0.00140 -0.02486 270 ARG   A CD   
728  N  NE   . ARG   A 118 ? 0.63531 0.56800 0.54925 -0.00703 -0.00121 -0.02481 270 ARG   A NE   
729  C  CZ   . ARG   A 118 ? 0.56401 0.48948 0.46832 -0.00394 -0.00175 -0.02060 270 ARG   A CZ   
730  N  NH1  . ARG   A 118 ? 0.76082 0.67559 0.66282 0.00153  -0.00206 -0.01807 270 ARG   A NH1  
731  N  NH2  . ARG   A 118 ? 0.51653 0.44758 0.41448 -0.00634 -0.00212 -0.01863 270 ARG   A NH2  
732  N  N    . SER   A 119 ? 0.39249 0.29995 0.28896 -0.02272 0.00315  -0.02601 271 SER   A N    
733  C  CA   . SER   A 119 ? 0.46949 0.36597 0.35743 -0.02256 0.00484  -0.02940 271 SER   A CA   
734  C  C    . SER   A 119 ? 0.51267 0.40243 0.39327 -0.03155 0.00583  -0.03241 271 SER   A C    
735  O  O    . SER   A 119 ? 0.59705 0.47321 0.47094 -0.03215 0.00738  -0.03708 271 SER   A O    
736  C  CB   . SER   A 119 ? 0.37386 0.28218 0.26605 -0.02004 0.00478  -0.03070 271 SER   A CB   
737  O  OG   . SER   A 119 ? 0.49785 0.41660 0.38968 -0.02755 0.00423  -0.03153 271 SER   A OG   
738  N  N    . ASN   A 120 ? 0.44285 0.34223 0.32650 -0.03850 0.00489  -0.03081 272 ASN   A N    
739  C  CA   . ASN   A 120 ? 0.46217 0.35798 0.33998 -0.04817 0.00550  -0.03361 272 ASN   A CA   
740  C  C    . ASN   A 120 ? 0.54188 0.41840 0.41201 -0.05145 0.00682  -0.03312 272 ASN   A C    
741  O  O    . ASN   A 120 ? 0.55691 0.42450 0.42190 -0.05896 0.00749  -0.03688 272 ASN   A O    
742  C  CB   . ASN   A 120 ? 0.49652 0.40947 0.38202 -0.05406 0.00395  -0.03134 272 ASN   A CB   
743  C  CG   . ASN   A 120 ? 0.59732 0.51188 0.47835 -0.06460 0.00392  -0.03435 272 ASN   A CG   
744  O  OD1  . ASN   A 120 ? 0.51064 0.42498 0.39112 -0.07133 0.00449  -0.03347 272 ASN   A OD1  
745  N  ND2  . ASN   A 120 ? 0.55806 0.47703 0.43584 -0.06689 0.00332  -0.03825 272 ASN   A ND2  
746  N  N    A GLN   A 121 ? 0.56496 0.43568 0.43490 -0.04678 0.00673  -0.02795 273 GLN   A N    
747  N  N    B GLN   A 121 ? 0.56827 0.43930 0.43830 -0.04683 0.00672  -0.02790 273 GLN   A N    
748  C  CA   A GLN   A 121 ? 0.63271 0.48632 0.49645 -0.05062 0.00705  -0.02388 273 GLN   A CA   
749  C  CA   B GLN   A 121 ? 0.63243 0.48612 0.49625 -0.05031 0.00703  -0.02379 273 GLN   A CA   
750  C  C    A GLN   A 121 ? 0.65746 0.48914 0.51854 -0.04752 0.00728  -0.02726 273 GLN   A C    
751  C  C    B GLN   A 121 ? 0.65353 0.48570 0.51462 -0.04782 0.00734  -0.02770 273 GLN   A C    
752  O  O    A GLN   A 121 ? 0.70967 0.52415 0.56801 -0.05343 0.00717  -0.02577 273 GLN   A O    
753  O  O    B GLN   A 121 ? 0.71054 0.52631 0.56883 -0.05444 0.00738  -0.02729 273 GLN   A O    
754  C  CB   A GLN   A 121 ? 0.66459 0.52208 0.52840 -0.04677 0.00627  -0.01634 273 GLN   A CB   
755  C  CB   B GLN   A 121 ? 0.66481 0.52124 0.52878 -0.04540 0.00616  -0.01642 273 GLN   A CB   
756  C  CG   A GLN   A 121 ? 0.64533 0.52595 0.51464 -0.04818 0.00650  -0.01655 273 GLN   A CG   
757  C  CG   B GLN   A 121 ? 0.66934 0.54024 0.53296 -0.05249 0.00669  -0.01251 273 GLN   A CG   
758  C  CD   A GLN   A 121 ? 0.59541 0.48404 0.46614 -0.04191 0.00564  -0.01317 273 GLN   A CD   
759  C  CD   B GLN   A 121 ? 0.60425 0.47778 0.46469 -0.04995 0.00581  -0.00498 273 GLN   A CD   
760  O  OE1  A GLN   A 121 ? 0.35936 0.26047 0.23835 -0.03584 0.00497  -0.01674 273 GLN   A OE1  
761  O  OE1  B GLN   A 121 ? 0.58566 0.47887 0.44882 -0.05011 0.00630  -0.00562 273 GLN   A OE1  
762  N  NE2  A GLN   A 121 ? 0.56128 0.44357 0.42470 -0.04406 0.00516  -0.00567 273 GLN   A NE2  
763  N  NE2  B GLN   A 121 ? 0.51135 0.36640 0.36726 -0.04759 0.00421  0.00179  273 GLN   A NE2  
764  N  N    . SER   A 122 ? 0.52790 0.36035 0.39165 -0.03851 0.00764  -0.03214 274 SER   A N    
765  C  CA   . SER   A 122 ? 0.58900 0.40376 0.45299 -0.03437 0.00851  -0.03870 274 SER   A CA   
766  C  C    . SER   A 122 ? 0.66188 0.48068 0.52418 -0.03933 0.01035  -0.05063 274 SER   A C    
767  O  O    . SER   A 122 ? 0.72799 0.53249 0.59121 -0.03773 0.01165  -0.05966 274 SER   A O    
768  C  CB   . SER   A 122 ? 0.63852 0.45477 0.50701 -0.02166 0.00841  -0.03847 274 SER   A CB   
769  O  OG   . SER   A 122 ? 0.66104 0.49644 0.53132 -0.01899 0.00966  -0.04373 274 SER   A OG   
770  N  N    . PHE   A 123 ? 0.56947 0.40874 0.43059 -0.04516 0.01018  -0.05127 275 PHE   A N    
771  C  CA   . PHE   A 123 ? 0.58495 0.43309 0.44320 -0.05135 0.01120  -0.06128 275 PHE   A CA   
772  C  C    . PHE   A 123 ? 0.68310 0.51662 0.53817 -0.06174 0.01137  -0.06660 275 PHE   A C    
773  O  O    . PHE   A 123 ? 0.71188 0.53985 0.56678 -0.06802 0.01022  -0.05946 275 PHE   A O    
774  C  CB   . PHE   A 123 ? 0.59001 0.46464 0.44998 -0.05516 0.00959  -0.05709 275 PHE   A CB   
775  C  CG   . PHE   A 123 ? 0.59326 0.48332 0.44962 -0.06169 0.00977  -0.06505 275 PHE   A CG   
776  C  CD1  . PHE   A 123 ? 0.61745 0.51927 0.47270 -0.05718 0.01120  -0.07036 275 PHE   A CD1  
777  C  CD2  . PHE   A 123 ? 0.50091 0.39715 0.35483 -0.07310 0.00846  -0.06705 275 PHE   A CD2  
778  C  CE1  . PHE   A 123 ? 0.60953 0.53026 0.45995 -0.06431 0.01131  -0.07740 275 PHE   A CE1  
779  C  CE2  . PHE   A 123 ? 0.49616 0.41014 0.34595 -0.07994 0.00802  -0.07415 275 PHE   A CE2  
780  C  CZ   . PHE   A 123 ? 0.61206 0.53900 0.45943 -0.07575 0.00943  -0.07926 275 PHE   A CZ   
781  N  N    . THR   A 124 ? 0.70538 0.53393 0.55867 -0.06412 0.01301  -0.08008 276 THR   A N    
782  C  CA   . THR   A 124 ? 0.78720 0.60215 0.63917 -0.07498 0.01300  -0.08780 276 THR   A CA   
783  C  C    . THR   A 124 ? 0.77420 0.60978 0.62147 -0.08338 0.01343  -0.09938 276 THR   A C    
784  O  O    . THR   A 124 ? 0.79549 0.64600 0.64080 -0.07909 0.01506  -0.10747 276 THR   A O    
785  C  CB   . THR   A 124 ? 0.87981 0.66505 0.73700 -0.07081 0.01411  -0.09576 276 THR   A CB   
786  O  OG1  . THR   A 124 ? 0.96861 0.74211 0.82635 -0.08228 0.01410  -0.10659 276 THR   A OG1  
787  C  CG2  . THR   A 124 ? 0.85168 0.64069 0.71131 -0.05978 0.01674  -0.10696 276 THR   A CG2  
788  N  N    . MET   A 125 ? 0.83558 0.67499 0.68095 -0.09607 0.01184  -0.09954 277 MET   A N    
789  C  CA   . MET   A 125 ? 0.89738 0.75935 0.73804 -0.10561 0.01124  -0.10925 277 MET   A CA   
790  C  C    . MET   A 125 ? 0.94472 0.79505 0.78413 -0.11122 0.01313  -0.12915 277 MET   A C    
791  O  O    . MET   A 125 ? 0.91523 0.78691 0.74946 -0.11922 0.01290  -0.14003 277 MET   A O    
792  C  CB   . MET   A 125 ? 0.85942 0.73436 0.70031 -0.11682 0.00830  -0.10117 277 MET   A CB   
793  C  CG   . MET   A 125 ? 0.88199 0.77303 0.72691 -0.11179 0.00642  -0.08486 277 MET   A CG   
794  S  SD   . MET   A 125 ? 0.99061 0.91083 0.83815 -0.12340 0.00261  -0.07961 277 MET   A SD   
795  C  CE   . MET   A 125 ? 0.92204 0.82499 0.77258 -0.13168 0.00317  -0.07509 277 MET   A CE   
796  N  N    . ASP   A 126 ? 1.01657 0.83470 0.86194 -0.10741 0.01457  -0.13436 278 ASP   A N    
797  C  CA   . ASP   A 126 ? 1.11045 0.91509 0.95866 -0.11158 0.01643  -0.15582 278 ASP   A CA   
798  C  C    . ASP   A 126 ? 1.06111 0.88326 0.90659 -0.10451 0.01981  -0.17145 278 ASP   A C    
799  O  O    . ASP   A 126 ? 1.12170 0.95061 0.96572 -0.11113 0.02153  -0.19225 278 ASP   A O    
800  C  CB   . ASP   A 126 ? 1.27876 1.04312 1.13819 -0.10783 0.01635  -0.15553 278 ASP   A CB   
801  C  CG   . ASP   A 126 ? 1.39398 1.14370 1.25547 -0.11623 0.01328  -0.13870 278 ASP   A CG   
802  O  OD1  . ASP   A 126 ? 1.43393 1.15761 1.30277 -0.11094 0.01221  -0.12774 278 ASP   A OD1  
803  O  OD2  . ASP   A 126 ? 1.41389 1.18070 1.27003 -0.12838 0.01180  -0.13572 278 ASP   A OD2  
804  N  N    . ASP   A 127 ? 1.00227 0.83427 0.84725 -0.09198 0.02098  -0.16262 279 ASP   A N    
805  C  CA   . ASP   A 127 ? 0.98523 0.83985 0.82705 -0.08618 0.02447  -0.17506 279 ASP   A CA   
806  C  C    . ASP   A 127 ? 0.85025 0.73350 0.68710 -0.08116 0.02359  -0.15919 279 ASP   A C    
807  O  O    . ASP   A 127 ? 0.94920 0.85137 0.78442 -0.07516 0.02655  -0.16534 279 ASP   A O    
808  C  CB   . ASP   A 127 ? 1.06733 0.89959 0.91934 -0.07377 0.02804  -0.18729 279 ASP   A CB   
809  C  CG   . ASP   A 127 ? 1.09543 0.90153 0.95584 -0.06279 0.02622  -0.16992 279 ASP   A CG   
810  O  OD1  . ASP   A 127 ? 1.11726 0.89198 0.98910 -0.05784 0.02631  -0.17522 279 ASP   A OD1  
811  O  OD2  . ASP   A 127 ? 1.07462 0.89218 0.93140 -0.05927 0.02432  -0.15110 279 ASP   A OD2  
812  N  N    . MET   A 128 ? 0.82231 0.70993 0.65846 -0.08364 0.01973  -0.13963 280 MET   A N    
813  C  CA   . MET   A 128 ? 0.70902 0.62207 0.54406 -0.07991 0.01795  -0.12428 280 MET   A CA   
814  C  C    . MET   A 128 ? 0.76689 0.67575 0.60673 -0.06592 0.02017  -0.12054 280 MET   A C    
815  O  O    . MET   A 128 ? 0.69483 0.62775 0.53330 -0.06270 0.02120  -0.11917 280 MET   A O    
816  C  CB   . MET   A 128 ? 0.71285 0.66261 0.54067 -0.08819 0.01718  -0.12796 280 MET   A CB   
817  C  CG   . MET   A 128 ? 0.78157 0.73944 0.60478 -0.10253 0.01456  -0.13284 280 MET   A CG   
818  S  SD   . MET   A 128 ? 0.78699 0.73983 0.61595 -0.10664 0.00943  -0.11315 280 MET   A SD   
819  C  CE   . MET   A 128 ? 0.85934 0.81254 0.68413 -0.12305 0.00789  -0.12506 280 MET   A CE   
820  N  N    . SER   A 129 ? 0.73804 0.61771 0.58404 -0.05825 0.02050  -0.11760 281 SER   A N    
821  C  CA   . SER   A 129 ? 0.75802 0.63225 0.60980 -0.04487 0.02209  -0.11442 281 SER   A CA   
822  C  C    . SER   A 129 ? 0.73111 0.58748 0.58761 -0.04001 0.01928  -0.09871 281 SER   A C    
823  O  O    . SER   A 129 ? 0.72107 0.56605 0.57661 -0.04669 0.01703  -0.09260 281 SER   A O    
824  C  CB   . SER   A 129 ? 0.76922 0.62794 0.62562 -0.03846 0.02591  -0.13180 281 SER   A CB   
825  O  OG   . SER   A 129 ? 0.80563 0.63047 0.66818 -0.03742 0.02459  -0.13175 281 SER   A OG   
826  N  N    . TRP   A 130 ? 0.74343 0.60053 0.60494 -0.02897 0.01951  -0.09248 282 TRP   A N    
827  C  CA   . TRP   A 130 ? 0.74296 0.58588 0.60870 -0.02343 0.01700  -0.07937 282 TRP   A CA   
828  C  C    . TRP   A 130 ? 0.68629 0.50420 0.55798 -0.01522 0.01768  -0.08355 282 TRP   A C    
829  O  O    . TRP   A 130 ? 0.70924 0.52978 0.58628 -0.00533 0.01954  -0.08868 282 TRP   A O    
830  C  CB   . TRP   A 130 ? 0.66549 0.52639 0.53463 -0.01718 0.01591  -0.06955 282 TRP   A CB   
831  C  CG   . TRP   A 130 ? 0.63326 0.51579 0.50144 -0.02403 0.01399  -0.06270 282 TRP   A CG   
832  C  CD1  . TRP   A 130 ? 0.61793 0.50272 0.48864 -0.02681 0.01115  -0.05254 282 TRP   A CD1  
833  C  CD2  . TRP   A 130 ? 0.59503 0.50161 0.46158 -0.02864 0.01442  -0.06508 282 TRP   A CD2  
834  N  NE1  . TRP   A 130 ? 0.59056 0.49665 0.46382 -0.03186 0.00946  -0.04867 282 TRP   A NE1  
835  C  CE2  . TRP   A 130 ? 0.53850 0.45838 0.40875 -0.03346 0.01097  -0.05457 282 TRP   A CE2  
836  C  CE3  . TRP   A 130 ? 0.56398 0.48432 0.42692 -0.02942 0.01732  -0.07505 282 TRP   A CE3  
837  C  CZ2  . TRP   A 130 ? 0.54601 0.49054 0.41746 -0.03891 0.00932  -0.05105 282 TRP   A CZ2  
838  C  CZ3  . TRP   A 130 ? 0.60813 0.55593 0.46935 -0.03598 0.01618  -0.07172 282 TRP   A CZ3  
839  C  CH2  . TRP   A 130 ? 0.57584 0.53456 0.44174 -0.04061 0.01172  -0.05849 282 TRP   A CH2  
840  N  N    . ASP   A 131 ? 0.72121 0.51585 0.59368 -0.01943 0.01589  -0.08047 283 ASP   A N    
841  C  CA   . ASP   A 131 ? 0.86882 0.63670 0.74987 -0.01261 0.01523  -0.08207 283 ASP   A CA   
842  C  C    . ASP   A 131 ? 0.83369 0.59515 0.71713 -0.00704 0.01164  -0.06456 283 ASP   A C    
843  O  O    . ASP   A 131 ? 0.88220 0.64139 0.76103 -0.01439 0.00928  -0.05298 283 ASP   A O    
844  C  CB   . ASP   A 131 ? 0.96520 0.71090 0.84770 -0.02187 0.01477  -0.08817 283 ASP   A CB   
845  C  CG   . ASP   A 131 ? 1.12974 0.84488 1.02514 -0.01495 0.01313  -0.08863 283 ASP   A CG   
846  O  OD1  . ASP   A 131 ? 1.12553 0.83869 1.02891 -0.00193 0.01283  -0.08687 283 ASP   A OD1  
847  O  OD2  . ASP   A 131 ? 1.23040 0.92344 1.12982 -0.02272 0.01169  -0.09016 283 ASP   A OD2  
848  N  N    . CYS   A 132 ? 0.90726 0.66881 0.79797 0.00552  0.01131  -0.06318 284 CYS   A N    
849  C  CA   . CYS   A 132 ? 0.94270 0.70081 0.83594 0.01124  0.00739  -0.04729 284 CYS   A CA   
850  C  C    . CYS   A 132 ? 1.01060 0.74389 0.91576 0.01946  0.00485  -0.04483 284 CYS   A C    
851  O  O    . CYS   A 132 ? 1.02418 0.75978 0.93656 0.03057  0.00293  -0.03950 284 CYS   A O    
852  C  CB   . CYS   A 132 ? 0.85802 0.63959 0.75157 0.01875  0.00771  -0.04477 284 CYS   A CB   
853  S  SG   . CYS   A 132 ? 0.68967 0.49893 0.57467 0.01035  0.00927  -0.04496 284 CYS   A SG   
854  N  N    . GLY   A 133 ? 1.10685 0.81635 1.01624 0.01402  0.00430  -0.04834 285 GLY   A N    
855  C  CA   . GLY   A 133 ? 1.24040 0.92298 1.16486 0.02127  0.00089  -0.04453 285 GLY   A CA   
856  C  C    . GLY   A 133 ? 1.31886 0.99110 1.25731 0.02987  0.00403  -0.06462 285 GLY   A C    
857  O  O    . GLY   A 133 ? 1.38766 1.04797 1.32849 0.02336  0.00640  -0.07909 285 GLY   A O    
858  N  N    . SER   A 134 ? 1.30174 0.98046 1.25037 0.04428  0.00425  -0.06707 286 SER   A N    
859  C  CA   . SER   A 134 ? 1.26431 0.93560 1.22903 0.05418  0.00763  -0.08729 286 SER   A CA   
860  C  C    . SER   A 134 ? 1.21809 0.91302 1.17357 0.05003  0.01490  -0.10859 286 SER   A C    
861  O  O    . SER   A 134 ? 1.19475 0.91344 1.13338 0.04205  0.01659  -0.10505 286 SER   A O    
862  C  CB   . SER   A 134 ? 1.24853 0.92413 1.22770 0.07091  0.00581  -0.08304 286 SER   A CB   
863  O  OG   . SER   A 134 ? 1.22569 0.93357 1.19811 0.07510  0.01043  -0.09042 286 SER   A OG   
864  N  N    . GLN   A 135 ? 1.26840 0.95777 1.23664 0.05553  0.01900  -0.13110 287 GLN   A N    
865  C  CA   . GLN   A 135 ? 1.31331 1.02820 1.27294 0.05105  0.02600  -0.15244 287 GLN   A CA   
866  C  C    . GLN   A 135 ? 1.23831 0.98775 1.19234 0.05738  0.02915  -0.15112 287 GLN   A C    
867  O  O    . GLN   A 135 ? 1.16185 0.93914 1.10154 0.04950  0.03282  -0.15609 287 GLN   A O    
868  C  CB   . GLN   A 135 ? 1.41963 1.12225 1.39569 0.05565  0.02999  -0.17925 287 GLN   A CB   
869  C  CG   . GLN   A 135 ? 1.53846 1.19996 1.52970 0.05366  0.02565  -0.17947 287 GLN   A CG   
870  C  CD   . GLN   A 135 ? 1.61759 1.25439 1.63410 0.06943  0.02137  -0.17261 287 GLN   A CD   
871  O  OE1  . GLN   A 135 ? 1.64345 1.28092 1.67876 0.08221  0.02469  -0.19105 287 GLN   A OE1  
872  N  NE2  . GLN   A 135 ? 1.62188 1.23885 1.63986 0.06852  0.01380  -0.14582 287 GLN   A NE2  
873  N  N    . ASP   A 136 ? 1.23549 0.98451 1.20181 0.07103  0.02724  -0.14328 288 ASP   A N    
874  C  CA   . ASP   A 136 ? 1.21089 0.99193 1.17330 0.07619  0.02947  -0.13958 288 ASP   A CA   
875  C  C    . ASP   A 136 ? 1.13115 0.92859 1.07511 0.06568  0.02727  -0.12261 288 ASP   A C    
876  O  O    . ASP   A 136 ? 1.01055 0.83756 0.94758 0.06378  0.03018  -0.12316 288 ASP   A O    
877  C  CB   . ASP   A 136 ? 1.23340 1.00898 1.21267 0.09157  0.02614  -0.13083 288 ASP   A CB   
878  C  CG   . ASP   A 136 ? 1.31969 1.09105 1.32043 0.10471  0.02986  -0.15071 288 ASP   A CG   
879  O  OD1  . ASP   A 136 ? 1.36747 1.13177 1.37175 0.10179  0.03420  -0.17158 288 ASP   A OD1  
880  O  OD2  . ASP   A 136 ? 1.35170 1.12800 1.36718 0.11811  0.02839  -0.14654 288 ASP   A OD2  
881  N  N    . TYR   A 137 ? 1.13623 0.91584 1.07379 0.05862  0.02215  -0.10754 289 TYR   A N    
882  C  CA   . TYR   A 137 ? 1.02793 0.82116 0.95121 0.04945  0.01987  -0.09273 289 TYR   A CA   
883  C  C    . TYR   A 137 ? 0.85482 0.64460 0.76634 0.03508  0.02043  -0.09543 289 TYR   A C    
884  O  O    . TYR   A 137 ? 0.78114 0.56757 0.68496 0.02733  0.01714  -0.08251 289 TYR   A O    
885  C  CB   . TYR   A 137 ? 1.02232 0.80542 0.94756 0.05281  0.01384  -0.07323 289 TYR   A CB   
886  C  CG   . TYR   A 137 ? 0.96906 0.75639 0.90713 0.06698  0.01249  -0.07045 289 TYR   A CG   
887  C  CD1  . TYR   A 137 ? 1.01986 0.78817 0.96783 0.07422  0.00712  -0.05927 289 TYR   A CD1  
888  C  CD2  . TYR   A 137 ? 0.90286 0.71529 0.84402 0.07257  0.01624  -0.07787 289 TYR   A CD2  
889  C  CE1  . TYR   A 137 ? 1.00875 0.78305 0.96979 0.08746  0.00524  -0.05628 289 TYR   A CE1  
890  C  CE2  . TYR   A 137 ? 0.93208 0.75069 0.88610 0.08526  0.01506  -0.07573 289 TYR   A CE2  
891  C  CZ   . TYR   A 137 ? 0.97179 0.77137 0.93597 0.09307  0.00944  -0.06535 289 TYR   A CZ   
892  O  OH   . TYR   A 137 ? 0.96075 0.76859 0.93896 0.10595  0.00765  -0.06274 289 TYR   A OH   
893  N  N    . LYS   A 138 ? 0.79892 0.59199 0.70960 0.03129  0.02475  -0.11351 290 LYS   A N    
894  C  CA   . LYS   A 138 ? 0.83332 0.63050 0.73279 0.01728  0.02564  -0.11853 290 LYS   A CA   
895  C  C    . LYS   A 138 ? 0.89171 0.72289 0.78378 0.01382  0.02961  -0.12654 290 LYS   A C    
896  O  O    . LYS   A 138 ? 0.89753 0.73980 0.79357 0.01820  0.03421  -0.14285 290 LYS   A O    
897  C  CB   . LYS   A 138 ? 0.94288 0.71612 0.84791 0.01382  0.02656  -0.13319 290 LYS   A CB   
898  C  CG   . LYS   A 138 ? 1.02922 0.81207 0.92365 -0.00044 0.02826  -0.14358 290 LYS   A CG   
899  C  CD   . LYS   A 138 ? 1.09984 0.85317 0.99730 -0.00856 0.02567  -0.14454 290 LYS   A CD   
900  C  CE   . LYS   A 138 ? 1.11509 0.87871 1.00415 -0.02239 0.02751  -0.15884 290 LYS   A CE   
901  N  NZ   . LYS   A 138 ? 1.12328 0.86359 1.01274 -0.03350 0.02415  -0.15409 290 LYS   A NZ   
902  N  N    . TYR   A 139 ? 0.82456 0.67368 0.70731 0.00596  0.02771  -0.11478 291 TYR   A N    
903  C  CA   . TYR   A 139 ? 0.80216 0.68480 0.67999 0.00315  0.02973  -0.11500 291 TYR   A CA   
904  C  C    . TYR   A 139 ? 0.87152 0.76871 0.73918 -0.01033 0.02981  -0.11915 291 TYR   A C    
905  O  O    . TYR   A 139 ? 0.86207 0.74909 0.72590 -0.01810 0.02657  -0.11249 291 TYR   A O    
906  C  CB   . TYR   A 139 ? 0.72502 0.61839 0.60450 0.00550  0.02644  -0.09676 291 TYR   A CB   
907  C  CG   . TYR   A 139 ? 0.72195 0.60195 0.61043 0.01716  0.02492  -0.09012 291 TYR   A CG   
908  C  CD1  . TYR   A 139 ? 0.70346 0.56394 0.59283 0.01772  0.02076  -0.07885 291 TYR   A CD1  
909  C  CD2  . TYR   A 139 ? 0.67126 0.56171 0.56730 0.02701  0.02754  -0.09477 291 TYR   A CD2  
910  C  CE1  . TYR   A 139 ? 0.63055 0.48234 0.52733 0.02756  0.01863  -0.07182 291 TYR   A CE1  
911  C  CE2  . TYR   A 139 ? 0.68466 0.56524 0.58964 0.03752  0.02542  -0.08810 291 TYR   A CE2  
912  C  CZ   . TYR   A 139 ? 0.76451 0.62586 0.66943 0.03765  0.02064  -0.07630 291 TYR   A CZ   
913  O  OH   . TYR   A 139 ? 0.74974 0.60463 0.66279 0.04737  0.01783  -0.06880 291 TYR   A OH   
914  N  N    . ASP   A 140 ? 0.89325 0.81762 0.75663 -0.01356 0.03338  -0.12952 292 ASP   A N    
915  C  CA   . ASP   A 140 ? 0.90757 0.85269 0.76091 -0.02671 0.03286  -0.13230 292 ASP   A CA   
916  C  C    . ASP   A 140 ? 0.82376 0.80550 0.67407 -0.02987 0.03243  -0.12206 292 ASP   A C    
917  O  O    . ASP   A 140 ? 0.79793 0.78576 0.65451 -0.02277 0.03205  -0.11142 292 ASP   A O    
918  C  CB   . ASP   A 140 ? 0.95117 0.89642 0.80116 -0.03083 0.03707  -0.15618 292 ASP   A CB   
919  C  CG   . ASP   A 140 ? 0.93944 0.90074 0.79294 -0.02334 0.04321  -0.17229 292 ASP   A CG   
920  O  OD1  . ASP   A 140 ? 1.02416 0.97337 0.88188 -0.02106 0.04697  -0.19391 292 ASP   A OD1  
921  O  OD2  . ASP   A 140 ? 0.90606 0.89242 0.75976 -0.01993 0.04443  -0.16440 292 ASP   A OD2  
922  N  N    . VAL   A 141 ? 0.79258 0.79991 0.63399 -0.04138 0.03203  -0.12477 293 VAL   A N    
923  C  CA   . VAL   A 141 ? 0.67537 0.71852 0.51459 -0.04654 0.03026  -0.11153 293 VAL   A CA   
924  C  C    . VAL   A 141 ? 0.67906 0.74515 0.51923 -0.04141 0.03554  -0.11794 293 VAL   A C    
925  O  O    . VAL   A 141 ? 0.67045 0.75726 0.51447 -0.04107 0.03407  -0.10272 293 VAL   A O    
926  C  CB   . VAL   A 141 ? 0.58721 0.65423 0.41655 -0.06073 0.02780  -0.11210 293 VAL   A CB   
927  C  CG1  . VAL   A 141 ? 0.61579 0.66650 0.44732 -0.06555 0.02178  -0.10050 293 VAL   A CG1  
928  C  CG2  . VAL   A 141 ? 0.61924 0.69031 0.44001 -0.06520 0.03279  -0.13766 293 VAL   A CG2  
929  N  N    . THR   A 142 ? 0.70263 0.76650 0.54117 -0.03765 0.04177  -0.14085 294 THR   A N    
930  C  CA   . THR   A 142 ? 0.72776 0.81604 0.56844 -0.03227 0.04773  -0.14931 294 THR   A CA   
931  C  C    . THR   A 142 ? 0.64291 0.71783 0.49600 -0.01965 0.04746  -0.13861 294 THR   A C    
932  O  O    . THR   A 142 ? 0.64210 0.74297 0.49827 -0.01714 0.05026  -0.13520 294 THR   A O    
933  C  CB   . THR   A 142 ? 0.72784 0.81437 0.56767 -0.02963 0.05464  -0.17922 294 THR   A CB   
934  O  OG1  . THR   A 142 ? 0.87513 0.91825 0.72573 -0.01882 0.05457  -0.18668 294 THR   A OG1  
935  C  CG2  . THR   A 142 ? 0.70678 0.80672 0.53434 -0.04323 0.05450  -0.19154 294 THR   A CG2  
936  N  N    . ASP   A 143 ? 0.65877 0.69620 0.51890 -0.01256 0.04398  -0.13275 295 ASP   A N    
937  C  CA   . ASP   A 143 ? 0.61527 0.64212 0.48648 -0.00178 0.04259  -0.12129 295 ASP   A CA   
938  C  C    . ASP   A 143 ? 0.56436 0.60827 0.43739 -0.00644 0.03792  -0.09889 295 ASP   A C    
939  O  O    . ASP   A 143 ? 0.56164 0.61628 0.44272 -0.00100 0.03828  -0.09125 295 ASP   A O    
940  C  CB   . ASP   A 143 ? 0.62416 0.61028 0.50100 0.00531  0.03954  -0.11982 295 ASP   A CB   
941  C  CG   . ASP   A 143 ? 0.70387 0.67015 0.58574 0.01305  0.04350  -0.13960 295 ASP   A CG   
942  O  OD1  . ASP   A 143 ? 0.74864 0.73094 0.63497 0.01870  0.04900  -0.15353 295 ASP   A OD1  
943  O  OD2  . ASP   A 143 ? 0.71200 0.64728 0.59505 0.01333  0.04107  -0.14121 295 ASP   A OD2  
944  N  N    . VAL   A 144 ? 0.60618 0.65293 0.47408 -0.01648 0.03322  -0.08839 296 VAL   A N    
945  C  CA   . VAL   A 144 ? 0.57180 0.63387 0.44520 -0.02095 0.02815  -0.06748 296 VAL   A CA   
946  C  C    . VAL   A 144 ? 0.49612 0.59750 0.36824 -0.02638 0.03024  -0.06335 296 VAL   A C    
947  O  O    . VAL   A 144 ? 0.50873 0.62254 0.39028 -0.02543 0.02828  -0.04910 296 VAL   A O    
948  C  CB   . VAL   A 144 ? 0.63642 0.69311 0.50739 -0.02965 0.02248  -0.05822 296 VAL   A CB   
949  C  CG1  . VAL   A 144 ? 0.58120 0.65030 0.46287 -0.03277 0.01662  -0.03712 296 VAL   A CG1  
950  C  CG2  . VAL   A 144 ? 0.66507 0.68657 0.53622 -0.02567 0.02123  -0.06271 296 VAL   A CG2  
951  N  N    . SER   A 145 ? 0.57792 0.70122 0.43867 -0.03315 0.03418  -0.07578 297 SER   A N    
952  C  CA   . SER   A 145 ? 0.58419 0.75003 0.44177 -0.03967 0.03674  -0.07209 297 SER   A CA   
953  C  C    . SER   A 145 ? 0.61628 0.79083 0.48011 -0.03054 0.04290  -0.07984 297 SER   A C    
954  O  O    . SER   A 145 ? 0.53913 0.74369 0.40678 -0.03392 0.04341  -0.06831 297 SER   A O    
955  C  CB   . SER   A 145 ? 0.62061 0.81107 0.46318 -0.04981 0.03973  -0.08595 297 SER   A CB   
956  O  OG   . SER   A 145 ? 0.71335 0.90066 0.55207 -0.04384 0.04769  -0.11290 297 SER   A OG   
957  N  N    . LYS   A 146 ? 0.57492 0.72429 0.44173 -0.01914 0.04717  -0.09797 298 LYS   A N    
958  C  CA   . LYS   A 146 ? 0.62298 0.77727 0.49911 -0.00843 0.05224  -0.10496 298 LYS   A CA   
959  C  C    . LYS   A 146 ? 0.68560 0.82575 0.57484 -0.00195 0.04757  -0.08709 298 LYS   A C    
960  O  O    . LYS   A 146 ? 0.62018 0.75613 0.51898 0.00875  0.05038  -0.09236 298 LYS   A O    
961  C  CB   . LYS   A 146 ? 0.66455 0.79559 0.54286 0.00220  0.05726  -0.12946 298 LYS   A CB   
962  C  CG   . LYS   A 146 ? 0.79920 0.95775 0.67105 -0.00043 0.06532  -0.15318 298 LYS   A CG   
963  C  CD   . LYS   A 146 ? 0.94998 1.07930 0.82534 0.00769  0.06860  -0.17787 298 LYS   A CD   
964  C  CE   . LYS   A 146 ? 1.03202 1.17963 0.89558 -0.00205 0.07279  -0.19858 298 LYS   A CE   
965  N  NZ   . LYS   A 146 ? 1.07136 1.21014 0.94344 0.00727  0.07975  -0.22934 298 LYS   A NZ   
966  N  N    . ALA   A 147 ? 0.60709 0.74042 0.49846 -0.00799 0.04033  -0.06735 299 ALA   A N    
967  C  CA   . ALA   A 147 ? 0.54226 0.66976 0.44697 -0.00467 0.03570  -0.05049 299 ALA   A CA   
968  C  C    . ALA   A 147 ? 0.62994 0.78501 0.53929 -0.01538 0.03176  -0.03038 299 ALA   A C    
969  O  O    . ALA   A 147 ? 0.58789 0.73844 0.51061 -0.01435 0.02712  -0.01593 299 ALA   A O    
970  C  CB   . ALA   A 147 ? 0.52931 0.62007 0.43757 -0.00061 0.03010  -0.04587 299 ALA   A CB   
971  N  N    . GLY   A 148 ? 0.59937 0.78324 0.49916 -0.02613 0.03292  -0.02869 300 GLY   A N    
972  C  CA   . GLY   A 148 ? 0.61367 0.82693 0.51862 -0.03723 0.02869  -0.00727 300 GLY   A CA   
973  C  C    . GLY   A 148 ? 0.60153 0.81348 0.50501 -0.04665 0.02146  0.00629  300 GLY   A C    
974  O  O    . GLY   A 148 ? 0.50292 0.73883 0.41290 -0.05618 0.01667  0.02658  300 GLY   A O    
975  N  N    . HIS   A 149 ? 0.46550 0.65168 0.36228 -0.04469 0.02012  -0.00301 301 HIS   A N    
976  C  CA   . HIS   A 149 ? 0.47456 0.65783 0.37290 -0.05229 0.01287  0.00960  301 HIS   A CA   
977  C  C    . HIS   A 149 ? 0.47389 0.68104 0.35572 -0.06233 0.01413  0.00366  301 HIS   A C    
978  O  O    . HIS   A 149 ? 0.54661 0.75789 0.41459 -0.06116 0.02101  -0.01719 301 HIS   A O    
979  C  CB   . HIS   A 149 ? 0.49752 0.64128 0.39992 -0.04538 0.01019  0.00464  301 HIS   A CB   
980  C  CG   . HIS   A 149 ? 0.52889 0.65478 0.44938 -0.03895 0.00631  0.01481  301 HIS   A CG   
981  N  ND1  . HIS   A 149 ? 0.52209 0.65459 0.45954 -0.04343 -0.00085 0.03455  301 HIS   A ND1  
982  C  CD2  . HIS   A 149 ? 0.50220 0.60535 0.42767 -0.02869 0.00826  0.00747  301 HIS   A CD2  
983  C  CE1  . HIS   A 149 ? 0.55777 0.67190 0.50971 -0.03640 -0.00264 0.03661  301 HIS   A CE1  
984  N  NE2  . HIS   A 149 ? 0.44451 0.54214 0.38825 -0.02772 0.00273  0.02083  301 HIS   A NE2  
985  N  N    . THR   A 150 ? 0.48845 0.71204 0.37363 -0.07223 0.00697  0.02185  302 THR   A N    
986  C  CA   . THR   A 150 ? 0.48974 0.74431 0.36059 -0.08404 0.00634  0.02134  302 THR   A CA   
987  C  C    . THR   A 150 ? 0.45672 0.69330 0.32456 -0.08636 0.00195  0.01812  302 THR   A C    
988  O  O    . THR   A 150 ? 0.47375 0.67559 0.35070 -0.07911 -0.00026 0.01708  302 THR   A O    
989  C  CB   . THR   A 150 ? 0.48776 0.78054 0.36536 -0.09489 0.00052  0.04760  302 THR   A CB   
990  O  OG1  . THR   A 150 ? 0.52658 0.80673 0.42232 -0.09616 -0.00954 0.06919  302 THR   A OG1  
991  C  CG2  . THR   A 150 ? 0.51666 0.82259 0.40227 -0.09237 0.00388  0.05437  302 THR   A CG2  
992  N  N    . LEU   A 151 ? 0.47587 0.73992 0.33055 -0.09745 0.00072  0.01640  303 LEU   A N    
993  C  CA   . LEU   A 151 ? 0.51969 0.77184 0.37111 -0.10122 -0.00345 0.01295  303 LEU   A CA   
994  C  C    . LEU   A 151 ? 0.43908 0.68412 0.30963 -0.10200 -0.01343 0.03695  303 LEU   A C    
995  O  O    . LEU   A 151 ? 0.44794 0.67202 0.32164 -0.10079 -0.01628 0.03351  303 LEU   A O    
996  C  CB   . LEU   A 151 ? 0.56747 0.85551 0.40076 -0.11396 -0.00294 0.00542  303 LEU   A CB   
997  C  CG   . LEU   A 151 ? 0.77565 1.05108 0.60206 -0.11811 -0.00496 -0.00617 303 LEU   A CG   
998  C  CD1  . LEU   A 151 ? 0.94197 1.19856 0.75510 -0.11457 0.00391  -0.03789 303 LEU   A CD1  
999  C  CD2  . LEU   A 151 ? 0.83537 1.15196 0.65427 -0.13273 -0.01120 0.00427  303 LEU   A CD2  
1000 N  N    . GLU   A 152 ? 0.44063 0.70278 0.32601 -0.10401 -0.01877 0.06078  304 GLU   A N    
1001 C  CA   . GLU   A 152 ? 0.45803 0.71167 0.36690 -0.10339 -0.02853 0.08285  304 GLU   A CA   
1002 C  C    . GLU   A 152 ? 0.52917 0.73979 0.44987 -0.09191 -0.02778 0.07405  304 GLU   A C    
1003 O  O    . GLU   A 152 ? 0.48250 0.68242 0.41828 -0.09107 -0.03417 0.08232  304 GLU   A O    
1004 C  CB   . GLU   A 152 ? 0.47135 0.74320 0.39766 -0.10572 -0.03344 0.10774  304 GLU   A CB   
1005 C  CG   . GLU   A 152 ? 0.62289 0.93638 0.55070 -0.11890 -0.04127 0.13123  304 GLU   A CG   
1006 C  CD   . GLU   A 152 ? 0.83241 1.18536 0.74243 -0.12752 -0.03630 0.13177  304 GLU   A CD   
1007 O  OE1  . GLU   A 152 ? 0.94382 1.33471 0.85640 -0.13899 -0.04284 0.15518  304 GLU   A OE1  
1008 O  OE2  . GLU   A 152 ? 0.93987 1.28766 0.83441 -0.12289 -0.02598 0.10918  304 GLU   A OE2  
1009 N  N    . LEU   A 153 ? 0.44013 0.62832 0.35488 -0.08309 -0.02016 0.05743  305 LEU   A N    
1010 C  CA   . LEU   A 153 ? 0.39584 0.54657 0.31711 -0.07323 -0.01855 0.04711  305 LEU   A CA   
1011 C  C    . LEU   A 153 ? 0.44818 0.58192 0.35107 -0.07204 -0.01275 0.02503  305 LEU   A C    
1012 O  O    . LEU   A 153 ? 0.45360 0.56581 0.36003 -0.06961 -0.01399 0.02069  305 LEU   A O    
1013 C  CB   . LEU   A 153 ? 0.36912 0.50560 0.29870 -0.06414 -0.01533 0.04580  305 LEU   A CB   
1014 C  CG   . LEU   A 153 ? 0.41973 0.52135 0.35258 -0.05407 -0.01273 0.03380  305 LEU   A CG   
1015 C  CD1  . LEU   A 153 ? 0.38411 0.47357 0.33566 -0.05281 -0.01903 0.04224  305 LEU   A CD1  
1016 C  CD2  . LEU   A 153 ? 0.47430 0.56841 0.41173 -0.04625 -0.00921 0.03117  305 LEU   A CD2  
1017 N  N    . ILE   A 154 ? 0.42604 0.57043 0.31086 -0.07430 -0.00649 0.01078  306 ILE   A N    
1018 C  CA   . ILE   A 154 ? 0.43780 0.56105 0.30890 -0.07174 -0.00064 -0.01137 306 ILE   A CA   
1019 C  C    . ILE   A 154 ? 0.47138 0.59367 0.33725 -0.07944 -0.00374 -0.01454 306 ILE   A C    
1020 O  O    . ILE   A 154 ? 0.47220 0.56750 0.33736 -0.07660 -0.00261 -0.02345 306 ILE   A O    
1021 C  CB   . ILE   A 154 ? 0.54618 0.68327 0.40301 -0.07214 0.00666  -0.02758 306 ILE   A CB   
1022 C  CG1  . ILE   A 154 ? 0.59507 0.72384 0.45817 -0.06180 0.01083  -0.02890 306 ILE   A CG1  
1023 C  CG2  . ILE   A 154 ? 0.61653 0.73673 0.46100 -0.07285 0.01112  -0.05003 306 ILE   A CG2  
1024 C  CD1  . ILE   A 154 ? 0.70904 0.86264 0.56301 -0.06260 0.01735  -0.04002 306 ILE   A CD1  
1025 N  N    . GLU   A 155 ? 0.49456 0.64829 0.35691 -0.09004 -0.00798 -0.00638 307 GLU   A N    
1026 C  CA   . GLU   A 155 ? 0.45921 0.61510 0.31658 -0.09807 -0.01110 -0.01023 307 GLU   A CA   
1027 C  C    . GLU   A 155 ? 0.46085 0.60050 0.33471 -0.09552 -0.01689 0.00143  307 GLU   A C    
1028 O  O    . GLU   A 155 ? 0.50420 0.62605 0.37501 -0.09664 -0.01599 -0.00848 307 GLU   A O    
1029 C  CB   . GLU   A 155 ? 0.66008 0.85759 0.50902 -0.11057 -0.01473 -0.00427 307 GLU   A CB   
1030 C  CG   . GLU   A 155 ? 0.89159 1.09355 0.72801 -0.11981 -0.01479 -0.01863 307 GLU   A CG   
1031 C  CD   . GLU   A 155 ? 1.00047 1.24240 0.83496 -0.13229 -0.02221 -0.00546 307 GLU   A CD   
1032 O  OE1  . GLU   A 155 ? 1.06627 1.33588 0.88409 -0.14174 -0.02016 -0.01662 307 GLU   A OE1  
1033 O  OE2  . GLU   A 155 ? 1.00140 1.24834 0.85217 -0.13258 -0.03033 0.01564  307 GLU   A OE2  
1034 N  N    . PRO   A 156 ? 0.44497 0.59018 0.33793 -0.09245 -0.02273 0.02121  308 PRO   A N    
1035 C  CA   . PRO   A 156 ? 0.43703 0.56477 0.34762 -0.08828 -0.02684 0.02746  308 PRO   A CA   
1036 C  C    . PRO   A 156 ? 0.48083 0.57428 0.39075 -0.07941 -0.02130 0.01462  308 PRO   A C    
1037 O  O    . PRO   A 156 ? 0.46736 0.54724 0.38415 -0.07833 -0.02240 0.01267  308 PRO   A O    
1038 C  CB   . PRO   A 156 ? 0.53484 0.67393 0.46828 -0.08561 -0.03349 0.04889  308 PRO   A CB   
1039 C  CG   . PRO   A 156 ? 0.57923 0.74963 0.50537 -0.09274 -0.03506 0.05850  308 PRO   A CG   
1040 C  CD   . PRO   A 156 ? 0.39569 0.56452 0.29733 -0.09349 -0.02624 0.03886  308 PRO   A CD   
1041 N  N    . LEU   A 157 ? 0.49176 0.57339 0.39403 -0.07333 -0.01554 0.00642  309 LEU   A N    
1042 C  CA   . LEU   A 157 ? 0.39584 0.44721 0.29737 -0.06514 -0.01113 -0.00358 309 LEU   A CA   
1043 C  C    . LEU   A 157 ? 0.41383 0.45001 0.30101 -0.06864 -0.00739 -0.01858 309 LEU   A C    
1044 O  O    . LEU   A 157 ? 0.38996 0.40674 0.27977 -0.06656 -0.00676 -0.02157 309 LEU   A O    
1045 C  CB   . LEU   A 157 ? 0.40489 0.45045 0.30414 -0.05758 -0.00689 -0.00687 309 LEU   A CB   
1046 C  CG   . LEU   A 157 ? 0.44493 0.46189 0.34110 -0.04936 -0.00252 -0.01702 309 LEU   A CG   
1047 C  CD1  . LEU   A 157 ? 0.40992 0.41470 0.31998 -0.04529 -0.00541 -0.01095 309 LEU   A CD1  
1048 C  CD2  . LEU   A 157 ? 0.46455 0.48037 0.35886 -0.04222 0.00130  -0.02047 309 LEU   A CD2  
1049 N  N    . ILE   A 158 ? 0.48625 0.53221 0.35889 -0.07470 -0.00482 -0.02859 310 ILE   A N    
1050 C  CA   . ILE   A 158 ? 0.53734 0.56860 0.39882 -0.07941 -0.00190 -0.04336 310 ILE   A CA   
1051 C  C    . ILE   A 158 ? 0.50831 0.54416 0.37393 -0.08720 -0.00628 -0.03872 310 ILE   A C    
1052 O  O    . ILE   A 158 ? 0.53003 0.54633 0.39430 -0.08858 -0.00491 -0.04467 310 ILE   A O    
1053 C  CB   . ILE   A 158 ? 0.55866 0.60245 0.40603 -0.08466 0.00168  -0.05755 310 ILE   A CB   
1054 C  CG1  . ILE   A 158 ? 0.60356 0.64077 0.44872 -0.07564 0.00700  -0.06477 310 ILE   A CG1  
1055 C  CG2  . ILE   A 158 ? 0.61189 0.64131 0.45078 -0.09140 0.00360  -0.07298 310 ILE   A CG2  
1056 C  CD1  . ILE   A 158 ? 0.66100 0.66299 0.50721 -0.06738 0.01069  -0.07356 310 ILE   A CD1  
1057 N  N    . LYS   A 159 ? 0.47418 0.53735 0.34616 -0.09267 -0.01194 -0.02687 311 LYS   A N    
1058 C  CA   . LYS   A 159 ? 0.53873 0.60915 0.41817 -0.09900 -0.01673 -0.02134 311 LYS   A CA   
1059 C  C    . LYS   A 159 ? 0.48936 0.54125 0.38281 -0.09227 -0.01704 -0.01671 311 LYS   A C    
1060 O  O    . LYS   A 159 ? 0.50674 0.55223 0.40168 -0.09629 -0.01715 -0.02008 311 LYS   A O    
1061 C  CB   . LYS   A 159 ? 0.59475 0.69846 0.48263 -0.10423 -0.02393 -0.00612 311 LYS   A CB   
1062 C  CG   . LYS   A 159 ? 0.91930 1.03567 0.81641 -0.11100 -0.02969 -0.00017 311 LYS   A CG   
1063 C  CD   . LYS   A 159 ? 1.06406 1.17535 0.98509 -0.10378 -0.03353 0.01196  311 LYS   A CD   
1064 C  CE   . LYS   A 159 ? 1.14919 1.26040 1.07709 -0.10813 -0.03522 0.00941  311 LYS   A CE   
1065 N  NZ   . LYS   A 159 ? 1.15686 1.25480 1.10448 -0.09943 -0.03508 0.01255  311 LYS   A NZ   
1066 N  N    . PHE   A 160 ? 0.46179 0.50743 0.36598 -0.08277 -0.01705 -0.00969 312 PHE   A N    
1067 C  CA   . PHE   A 160 ? 0.45748 0.48839 0.37460 -0.07642 -0.01684 -0.00780 312 PHE   A CA   
1068 C  C    . PHE   A 160 ? 0.51494 0.52122 0.42028 -0.07560 -0.01122 -0.01940 312 PHE   A C    
1069 O  O    . PHE   A 160 ? 0.48586 0.48624 0.39512 -0.07752 -0.01083 -0.02086 312 PHE   A O    
1070 C  CB   . PHE   A 160 ? 0.41331 0.44295 0.34376 -0.06719 -0.01794 -0.00011 312 PHE   A CB   
1071 C  CG   . PHE   A 160 ? 0.38736 0.40334 0.32978 -0.06054 -0.01700 -0.00144 312 PHE   A CG   
1072 C  CD1  . PHE   A 160 ? 0.40353 0.42833 0.36650 -0.05989 -0.02106 0.00398  312 PHE   A CD1  
1073 C  CD2  . PHE   A 160 ? 0.44174 0.43830 0.37584 -0.05497 -0.01220 -0.00867 312 PHE   A CD2  
1074 C  CE1  . PHE   A 160 ? 0.43680 0.45262 0.41068 -0.05425 -0.01950 -0.00006 312 PHE   A CE1  
1075 C  CE2  . PHE   A 160 ? 0.48956 0.47804 0.43300 -0.05004 -0.01134 -0.01047 312 PHE   A CE2  
1076 C  CZ   . PHE   A 160 ? 0.40333 0.40213 0.36609 -0.04991 -0.01457 -0.00729 312 PHE   A CZ   
1077 N  N    . GLN   A 161 ? 0.54916 0.54216 0.44141 -0.07287 -0.00697 -0.02705 313 GLN   A N    
1078 C  CA   . GLN   A 161 ? 0.50449 0.47280 0.38768 -0.07179 -0.00263 -0.03564 313 GLN   A CA   
1079 C  C    . GLN   A 161 ? 0.51408 0.47903 0.39048 -0.08212 -0.00227 -0.04174 313 GLN   A C    
1080 O  O    . GLN   A 161 ? 0.51493 0.46509 0.39052 -0.08372 -0.00065 -0.04306 313 GLN   A O    
1081 C  CB   . GLN   A 161 ? 0.48984 0.44653 0.36355 -0.06668 0.00109  -0.04299 313 GLN   A CB   
1082 C  CG   . GLN   A 161 ? 0.45174 0.41048 0.33211 -0.05668 0.00118  -0.03748 313 GLN   A CG   
1083 C  CD   . GLN   A 161 ? 0.46065 0.40672 0.34826 -0.05026 0.00117  -0.03324 313 GLN   A CD   
1084 O  OE1  . GLN   A 161 ? 0.52477 0.45418 0.40754 -0.05097 0.00292  -0.03640 313 GLN   A OE1  
1085 N  NE2  . GLN   A 161 ? 0.43043 0.38567 0.33020 -0.04474 -0.00102 -0.02596 313 GLN   A NE2  
1086 N  N    . VAL   A 162 ? 0.46906 0.44975 0.34052 -0.09022 -0.00395 -0.04511 314 VAL   A N    
1087 C  CA   . VAL   A 162 ? 0.48433 0.46396 0.35032 -0.10132 -0.00410 -0.05173 314 VAL   A CA   
1088 C  C    . VAL   A 162 ? 0.44910 0.43883 0.32628 -0.10501 -0.00711 -0.04387 314 VAL   A C    
1089 O  O    . VAL   A 162 ? 0.49895 0.47839 0.37498 -0.11055 -0.00565 -0.04674 314 VAL   A O    
1090 C  CB   . VAL   A 162 ? 0.49562 0.49405 0.35337 -0.10958 -0.00547 -0.05853 314 VAL   A CB   
1091 C  CG1  . VAL   A 162 ? 0.47804 0.48033 0.33277 -0.12228 -0.00685 -0.06442 314 VAL   A CG1  
1092 C  CG2  . VAL   A 162 ? 0.47146 0.45900 0.31876 -0.10641 -0.00112 -0.07082 314 VAL   A CG2  
1093 N  N    . GLY   A 163 ? 0.51065 0.52134 0.40078 -0.10202 -0.01143 -0.03355 315 GLY   A N    
1094 C  CA   . GLY   A 163 ? 0.43553 0.45805 0.34021 -0.10412 -0.01437 -0.02737 315 GLY   A CA   
1095 C  C    . GLY   A 163 ? 0.49341 0.50135 0.40410 -0.09861 -0.01115 -0.02744 315 GLY   A C    
1096 O  O    . GLY   A 163 ? 0.44300 0.45446 0.35887 -0.10337 -0.01067 -0.02812 315 GLY   A O    
1097 N  N    . LEU   A 164 ? 0.40486 0.39936 0.31487 -0.08913 -0.00885 -0.02690 316 LEU   A N    
1098 C  CA   . LEU   A 164 ? 0.47540 0.45841 0.38850 -0.08463 -0.00575 -0.02762 316 LEU   A CA   
1099 C  C    . LEU   A 164 ? 0.52382 0.48945 0.42295 -0.09119 -0.00191 -0.03285 316 LEU   A C    
1100 O  O    . LEU   A 164 ? 0.47044 0.43668 0.37227 -0.09445 -0.00018 -0.03248 316 LEU   A O    
1101 C  CB   . LEU   A 164 ? 0.43345 0.40786 0.34840 -0.07379 -0.00487 -0.02594 316 LEU   A CB   
1102 C  CG   . LEU   A 164 ? 0.48142 0.44803 0.39923 -0.06890 -0.00219 -0.02681 316 LEU   A CG   
1103 C  CD1  . LEU   A 164 ? 0.48408 0.46730 0.41890 -0.06939 -0.00329 -0.02623 316 LEU   A CD1  
1104 C  CD2  . LEU   A 164 ? 0.48944 0.44976 0.40934 -0.05892 -0.00208 -0.02554 316 LEU   A CD2  
1105 N  N    . LYS   A 165 ? 0.45444 0.40543 0.34012 -0.09356 -0.00055 -0.03785 317 LYS   A N    
1106 C  CA   . LYS   A 165 ? 0.53546 0.46743 0.41106 -0.10047 0.00214  -0.04201 317 LYS   A CA   
1107 C  C    . LYS   A 165 ? 0.58647 0.52832 0.46369 -0.11288 0.00132  -0.04307 317 LYS   A C    
1108 O  O    . LYS   A 165 ? 0.60075 0.53436 0.47611 -0.11891 0.00328  -0.04187 317 LYS   A O    
1109 C  CB   . LYS   A 165 ? 0.58734 0.50301 0.45265 -0.10025 0.00332  -0.04961 317 LYS   A CB   
1110 C  CG   . LYS   A 165 ? 0.68411 0.57295 0.54310 -0.10289 0.00570  -0.05201 317 LYS   A CG   
1111 C  CD   . LYS   A 165 ? 0.71631 0.59451 0.57662 -0.09412 0.00687  -0.04462 317 LYS   A CD   
1112 C  CE   . LYS   A 165 ? 0.72652 0.58192 0.58274 -0.08720 0.00801  -0.04778 317 LYS   A CE   
1113 N  NZ   . LYS   A 165 ? 0.72438 0.57271 0.58187 -0.07834 0.00825  -0.03970 317 LYS   A NZ   
1114 N  N    . LYS   A 166 ? 0.51094 0.47273 0.39205 -0.11748 -0.00189 -0.04416 318 LYS   A N    
1115 C  CA   . LYS   A 166 ? 0.49036 0.46491 0.37427 -0.12949 -0.00328 -0.04530 318 LYS   A CA   
1116 C  C    . LYS   A 166 ? 0.59558 0.58239 0.49149 -0.12952 -0.00273 -0.03977 318 LYS   A C    
1117 O  O    . LYS   A 166 ? 0.58670 0.58032 0.48427 -0.13986 -0.00234 -0.04063 318 LYS   A O    
1118 C  CB   . LYS   A 166 ? 0.47621 0.47410 0.36302 -0.13349 -0.00787 -0.04585 318 LYS   A CB   
1119 C  CG   . LYS   A 166 ? 0.62661 0.61882 0.50013 -0.13964 -0.00787 -0.05547 318 LYS   A CG   
1120 C  CD   . LYS   A 166 ? 0.66763 0.68840 0.54294 -0.14274 -0.01281 -0.05394 318 LYS   A CD   
1121 C  CE   . LYS   A 166 ? 0.74433 0.76620 0.60658 -0.15284 -0.01272 -0.06664 318 LYS   A CE   
1122 N  NZ   . LYS   A 166 ? 0.73229 0.78648 0.59418 -0.15667 -0.01780 -0.06410 318 LYS   A NZ   
1123 N  N    . LEU   A 167 ? 0.63794 0.62931 0.54326 -0.11862 -0.00246 -0.03540 319 LEU   A N    
1124 C  CA   . LEU   A 167 ? 0.64805 0.65272 0.56576 -0.11793 -0.00107 -0.03328 319 LEU   A CA   
1125 C  C    . LEU   A 167 ? 0.62423 0.61623 0.53284 -0.12312 0.00363  -0.03359 319 LEU   A C    
1126 O  O    . LEU   A 167 ? 0.60217 0.60877 0.51808 -0.12739 0.00558  -0.03318 319 LEU   A O    
1127 C  CB   . LEU   A 167 ? 0.53643 0.54822 0.46781 -0.10510 -0.00200 -0.03095 319 LEU   A CB   
1128 C  CG   . LEU   A 167 ? 0.50007 0.52844 0.44663 -0.10036 -0.00755 -0.02719 319 LEU   A CG   
1129 C  CD1  . LEU   A 167 ? 0.56049 0.59468 0.52520 -0.08879 -0.00845 -0.02557 319 LEU   A CD1  
1130 C  CD2  . LEU   A 167 ? 0.44033 0.49032 0.39739 -0.10820 -0.01078 -0.02604 319 LEU   A CD2  
1131 N  N    . ASN   A 168 ? 0.58816 0.55513 0.48237 -0.12297 0.00529  -0.03367 320 ASN   A N    
1132 C  CA   . ASN   A 168 ? 0.69823 0.65150 0.58400 -0.12849 0.00860  -0.03070 320 ASN   A CA   
1133 C  C    . ASN   A 168 ? 0.68923 0.65662 0.58109 -0.12438 0.01113  -0.02775 320 ASN   A C    
1134 O  O    . ASN   A 168 ? 0.65067 0.62914 0.54350 -0.13275 0.01366  -0.02578 320 ASN   A O    
1135 C  CB   . ASN   A 168 ? 0.78745 0.74019 0.67016 -0.14380 0.00900  -0.03122 320 ASN   A CB   
1136 C  CG   . ASN   A 168 ? 0.95531 0.90030 0.83400 -0.14887 0.00632  -0.03738 320 ASN   A CG   
1137 O  OD1  . ASN   A 168 ? 1.09132 1.01427 0.96197 -0.14602 0.00610  -0.04052 320 ASN   A OD1  
1138 N  ND2  . ASN   A 168 ? 0.95332 0.91862 0.83840 -0.15648 0.00423  -0.04005 320 ASN   A ND2  
1139 N  N    . LEU   A 169 ? 0.53502 0.50430 0.43161 -0.11200 0.01060  -0.02836 321 LEU   A N    
1140 C  CA   . LEU   A 169 ? 0.48902 0.47455 0.39336 -0.10729 0.01281  -0.02892 321 LEU   A CA   
1141 C  C    . LEU   A 169 ? 0.55590 0.53438 0.44810 -0.11176 0.01590  -0.02389 321 LEU   A C    
1142 O  O    . LEU   A 169 ? 0.54082 0.49613 0.42090 -0.11187 0.01524  -0.01899 321 LEU   A O    
1143 C  CB   . LEU   A 169 ? 0.52473 0.51096 0.43719 -0.09380 0.01100  -0.03113 321 LEU   A CB   
1144 C  CG   . LEU   A 169 ? 0.50747 0.50447 0.43574 -0.08853 0.00724  -0.03330 321 LEU   A CG   
1145 C  CD1  . LEU   A 169 ? 0.51433 0.51272 0.45304 -0.07648 0.00578  -0.03463 321 LEU   A CD1  
1146 C  CD2  . LEU   A 169 ? 0.41052 0.43119 0.35452 -0.09311 0.00706  -0.03593 321 LEU   A CD2  
1147 N  N    . HIS   A 170 ? 0.51152 0.51201 0.40819 -0.11571 0.01911  -0.02484 322 HIS   A N    
1148 C  CA   . HIS   A 170 ? 0.45857 0.45985 0.34495 -0.11797 0.02165  -0.01946 322 HIS   A CA   
1149 C  C    . HIS   A 170 ? 0.45592 0.45162 0.34184 -0.10532 0.02033  -0.02083 322 HIS   A C    
1150 O  O    . HIS   A 170 ? 0.49366 0.49438 0.39170 -0.09558 0.01876  -0.02789 322 HIS   A O    
1151 C  CB   . HIS   A 170 ? 0.43942 0.47250 0.33167 -0.12433 0.02600  -0.02267 322 HIS   A CB   
1152 C  CG   . HIS   A 170 ? 0.50615 0.54895 0.40009 -0.13762 0.02765  -0.02109 322 HIS   A CG   
1153 N  ND1  . HIS   A 170 ? 0.54531 0.61823 0.44368 -0.14567 0.03223  -0.02320 322 HIS   A ND1  
1154 C  CD2  . HIS   A 170 ? 0.53506 0.56377 0.42738 -0.14486 0.02546  -0.01856 322 HIS   A CD2  
1155 C  CE1  . HIS   A 170 ? 0.52043 0.59677 0.42030 -0.15733 0.03263  -0.02084 322 HIS   A CE1  
1156 N  NE2  . HIS   A 170 ? 0.55761 0.60690 0.45380 -0.15724 0.02832  -0.01824 322 HIS   A NE2  
1157 N  N    . GLU   A 171 ? 0.46501 0.45074 0.33811 -0.10596 0.02038  -0.01287 323 GLU   A N    
1158 C  CA   . GLU   A 171 ? 0.51742 0.50146 0.39013 -0.09485 0.01900  -0.01409 323 GLU   A CA   
1159 C  C    . GLU   A 171 ? 0.50243 0.51526 0.38729 -0.09027 0.02111  -0.02471 323 GLU   A C    
1160 O  O    . GLU   A 171 ? 0.52433 0.53737 0.41717 -0.07979 0.01939  -0.03063 323 GLU   A O    
1161 C  CB   . GLU   A 171 ? 0.63351 0.60748 0.49167 -0.09735 0.01821  -0.00230 323 GLU   A CB   
1162 C  CG   . GLU   A 171 ? 0.77577 0.74410 0.63289 -0.08571 0.01570  -0.00230 323 GLU   A CG   
1163 C  CD   . GLU   A 171 ? 0.89631 0.85184 0.74079 -0.08735 0.01345  0.01164  323 GLU   A CD   
1164 O  OE1  . GLU   A 171 ? 0.97698 0.93795 0.81351 -0.09833 0.01442  0.02152  323 GLU   A OE1  
1165 O  OE2  . GLU   A 171 ? 0.92467 0.86583 0.76845 -0.07787 0.01038  0.01378  323 GLU   A OE2  
1166 N  N    . GLU   A 172 ? 0.43392 0.47195 0.32206 -0.09824 0.02496  -0.02825 324 GLU   A N    
1167 C  CA   . GLU   A 172 ? 0.47672 0.54365 0.38030 -0.09376 0.02748  -0.04186 324 GLU   A CA   
1168 C  C    . GLU   A 172 ? 0.50498 0.57005 0.42956 -0.08471 0.02502  -0.05089 324 GLU   A C    
1169 O  O    . GLU   A 172 ? 0.46744 0.54094 0.40619 -0.07561 0.02427  -0.06044 324 GLU   A O    
1170 C  CB   . GLU   A 172 ? 0.43932 0.53524 0.34428 -0.10449 0.03262  -0.04498 324 GLU   A CB   
1171 C  CG   . GLU   A 172 ? 0.49406 0.59975 0.37984 -0.11456 0.03516  -0.03517 324 GLU   A CG   
1172 C  CD   . GLU   A 172 ? 0.63102 0.71413 0.50170 -0.12503 0.03360  -0.01822 324 GLU   A CD   
1173 O  OE1  . GLU   A 172 ? 0.66770 0.76056 0.52532 -0.13589 0.03544  -0.00758 324 GLU   A OE1  
1174 O  OE2  . GLU   A 172 ? 0.60454 0.66119 0.47721 -0.12299 0.03037  -0.01560 324 GLU   A OE2  
1175 N  N    . GLU   A 173 ? 0.42084 0.47568 0.34857 -0.08774 0.02322  -0.04739 325 GLU   A N    
1176 C  CA   . GLU   A 173 ? 0.40441 0.45884 0.35171 -0.08022 0.01981  -0.05238 325 GLU   A CA   
1177 C  C    . GLU   A 173 ? 0.31843 0.35153 0.26383 -0.07122 0.01569  -0.04896 325 GLU   A C    
1178 O  O    . GLU   A 173 ? 0.38474 0.42121 0.34822 -0.06293 0.01293  -0.05345 325 GLU   A O    
1179 C  CB   . GLU   A 173 ? 0.33950 0.39340 0.28920 -0.08735 0.01863  -0.04891 325 GLU   A CB   
1180 C  CG   . GLU   A 173 ? 0.32611 0.40566 0.28338 -0.09554 0.02250  -0.05344 325 GLU   A CG   
1181 C  CD   . GLU   A 173 ? 0.56482 0.64000 0.51329 -0.10746 0.02236  -0.04686 325 GLU   A CD   
1182 O  OE1  . GLU   A 173 ? 0.52737 0.62483 0.48415 -0.11454 0.02505  -0.05010 325 GLU   A OE1  
1183 O  OE2  . GLU   A 173 ? 0.48256 0.53342 0.41713 -0.10998 0.01972  -0.03972 325 GLU   A OE2  
1184 N  N    . HIS   A 174 ? 0.38570 0.39749 0.31149 -0.07281 0.01510  -0.04080 326 HIS   A N    
1185 C  CA   . HIS   A 174 ? 0.51053 0.50435 0.43417 -0.06454 0.01188  -0.03806 326 HIS   A CA   
1186 C  C    . HIS   A 174 ? 0.54560 0.54667 0.47754 -0.05583 0.01143  -0.04325 326 HIS   A C    
1187 O  O    . HIS   A 174 ? 0.45575 0.45455 0.40025 -0.04827 0.00853  -0.04520 326 HIS   A O    
1188 C  CB   . HIS   A 174 ? 0.56345 0.53455 0.46702 -0.06753 0.01178  -0.02994 326 HIS   A CB   
1189 C  CG   . HIS   A 174 ? 0.59412 0.54875 0.49541 -0.05920 0.00922  -0.02806 326 HIS   A CG   
1190 N  ND1  . HIS   A 174 ? 0.58967 0.53811 0.49487 -0.05728 0.00712  -0.02839 326 HIS   A ND1  
1191 C  CD2  . HIS   A 174 ? 0.58113 0.52718 0.47679 -0.05274 0.00849  -0.02570 326 HIS   A CD2  
1192 C  CE1  . HIS   A 174 ? 0.60263 0.53982 0.50478 -0.05006 0.00586  -0.02699 326 HIS   A CE1  
1193 N  NE2  . HIS   A 174 ? 0.60910 0.54385 0.50621 -0.04680 0.00652  -0.02541 326 HIS   A NE2  
1194 N  N    . VAL   A 175 ? 0.43061 0.44225 0.35596 -0.05774 0.01405  -0.04525 327 VAL   A N    
1195 C  CA   . VAL   A 175 ? 0.39346 0.41361 0.32570 -0.05046 0.01345  -0.05166 327 VAL   A CA   
1196 C  C    . VAL   A 175 ? 0.41717 0.45669 0.37455 -0.04659 0.01371  -0.06446 327 VAL   A C    
1197 O  O    . VAL   A 175 ? 0.34907 0.39015 0.32013 -0.03907 0.01156  -0.07055 327 VAL   A O    
1198 C  CB   . VAL   A 175 ? 0.43969 0.46871 0.35609 -0.05450 0.01563  -0.04943 327 VAL   A CB   
1199 C  CG1  . VAL   A 175 ? 0.40215 0.40895 0.29838 -0.05728 0.01424  -0.03532 327 VAL   A CG1  
1200 C  CG2  . VAL   A 175 ? 0.40491 0.45838 0.32138 -0.06313 0.02009  -0.05428 327 VAL   A CG2  
1201 N  N    . LEU   A 176 ? 0.32967 0.38395 0.29604 -0.05149 0.01603  -0.06897 328 LEU   A N    
1202 C  CA   . LEU   A 176 ? 0.33964 0.41085 0.33464 -0.04665 0.01571  -0.08128 328 LEU   A CA   
1203 C  C    . LEU   A 176 ? 0.34835 0.40641 0.36062 -0.04008 0.01025  -0.07734 328 LEU   A C    
1204 O  O    . LEU   A 176 ? 0.36491 0.42797 0.40137 -0.03295 0.00785  -0.08489 328 LEU   A O    
1205 C  CB   . LEU   A 176 ? 0.31615 0.40721 0.31782 -0.05320 0.01931  -0.08608 328 LEU   A CB   
1206 C  CG   . LEU   A 176 ? 0.42066 0.53741 0.41683 -0.05856 0.02529  -0.09547 328 LEU   A CG   
1207 C  CD1  . LEU   A 176 ? 0.44530 0.57853 0.44135 -0.06762 0.02909  -0.09535 328 LEU   A CD1  
1208 C  CD2  . LEU   A 176 ? 0.29611 0.43232 0.31571 -0.05122 0.02635  -0.11382 328 LEU   A CD2  
1209 N  N    . LEU   A 177 ? 0.30835 0.35071 0.30931 -0.04307 0.00804  -0.06552 329 LEU   A N    
1210 C  CA   . LEU   A 177 ? 0.30267 0.33661 0.31748 -0.03852 0.00276  -0.05973 329 LEU   A CA   
1211 C  C    . LEU   A 177 ? 0.31351 0.33615 0.32960 -0.03160 0.00018  -0.05795 329 LEU   A C    
1212 O  O    . LEU   A 177 ? 0.33526 0.35843 0.37302 -0.02628 -0.00401 -0.05722 329 LEU   A O    
1213 C  CB   . LEU   A 177 ? 0.32671 0.35037 0.32625 -0.04463 0.00160  -0.04949 329 LEU   A CB   
1214 C  CG   . LEU   A 177 ? 0.41871 0.44041 0.43072 -0.04256 -0.00387 -0.04215 329 LEU   A CG   
1215 C  CD1  . LEU   A 177 ? 0.27063 0.30888 0.31400 -0.03938 -0.00699 -0.04524 329 LEU   A CD1  
1216 C  CD2  . LEU   A 177 ? 0.37324 0.38890 0.36770 -0.05022 -0.00422 -0.03526 329 LEU   A CD2  
1217 N  N    . MET   A 178 ? 0.34736 0.36038 0.34211 -0.03186 0.00218  -0.05612 330 MET   A N    
1218 C  CA   . MET   A 178 ? 0.40190 0.40692 0.39826 -0.02547 -0.00004 -0.05512 330 MET   A CA   
1219 C  C    . MET   A 178 ? 0.31581 0.33340 0.33430 -0.02052 -0.00073 -0.06646 330 MET   A C    
1220 O  O    . MET   A 178 ? 0.37069 0.38506 0.40579 -0.01532 -0.00437 -0.06622 330 MET   A O    
1221 C  CB   . MET   A 178 ? 0.35447 0.34877 0.32551 -0.02636 0.00188  -0.05089 330 MET   A CB   
1222 C  CG   . MET   A 178 ? 0.39641 0.37439 0.34957 -0.02946 0.00192  -0.04142 330 MET   A CG   
1223 S  SD   . MET   A 178 ? 0.54004 0.50301 0.47109 -0.02763 0.00280  -0.03608 330 MET   A SD   
1224 C  CE   . MET   A 178 ? 0.47292 0.44393 0.39175 -0.03475 0.00598  -0.03661 330 MET   A CE   
1225 N  N    . ALA   A 179 ? 0.32586 0.35930 0.34593 -0.02275 0.00284  -0.07718 331 ALA   A N    
1226 C  CA   . ALA   A 179 ? 0.27225 0.31988 0.31439 -0.01842 0.00274  -0.09182 331 ALA   A CA   
1227 C  C    . ALA   A 179 ? 0.42130 0.47278 0.49762 -0.01435 -0.00056 -0.09627 331 ALA   A C    
1228 O  O    . ALA   A 179 ? 0.34164 0.39270 0.44137 -0.00889 -0.00381 -0.10230 331 ALA   A O    
1229 C  CB   . ALA   A 179 ? 0.30353 0.37185 0.33788 -0.02275 0.00804  -0.10330 331 ALA   A CB   
1230 N  N    . ILE   A 180 ? 0.31540 0.37076 0.39699 -0.01716 -0.00039 -0.09272 332 ILE   A N    
1231 C  CA   . ILE   A 180 ? 0.29763 0.35705 0.41361 -0.01298 -0.00463 -0.09420 332 ILE   A CA   
1232 C  C    . ILE   A 180 ? 0.30332 0.34721 0.42892 -0.00954 -0.01112 -0.08117 332 ILE   A C    
1233 O  O    . ILE   A 180 ? 0.31389 0.35805 0.47144 -0.00430 -0.01572 -0.08357 332 ILE   A O    
1234 C  CB   . ILE   A 180 ? 0.30420 0.37226 0.42110 -0.01739 -0.00370 -0.09062 332 ILE   A CB   
1235 C  CG1  . ILE   A 180 ? 0.37241 0.46112 0.48741 -0.02065 0.00283  -0.10522 332 ILE   A CG1  
1236 C  CG2  . ILE   A 180 ? 0.36602 0.43634 0.51753 -0.01291 -0.00988 -0.08675 332 ILE   A CG2  
1237 C  CD1  . ILE   A 180 ? 0.34185 0.43931 0.44932 -0.02743 0.00491  -0.10051 332 ILE   A CD1  
1238 N  N    . CYS   A 181 ? 0.29653 0.32769 0.39610 -0.01282 -0.01158 -0.06736 333 CYS   A N    
1239 C  CA   . CYS   A 181 ? 0.41144 0.43153 0.51569 -0.01075 -0.01668 -0.05489 333 CYS   A CA   
1240 C  C    . CYS   A 181 ? 0.42231 0.43959 0.54286 -0.00557 -0.01871 -0.06042 333 CYS   A C    
1241 O  O    . CYS   A 181 ? 0.32000 0.33523 0.46684 -0.00273 -0.02425 -0.05510 333 CYS   A O    
1242 C  CB   . CYS   A 181 ? 0.39169 0.40097 0.46260 -0.01464 -0.01486 -0.04472 333 CYS   A CB   
1243 S  SG   . CYS   A 181 ? 0.39453 0.39572 0.46636 -0.01366 -0.01967 -0.02963 333 CYS   A SG   
1244 N  N    . ILE   A 182 ? 0.37011 0.38834 0.47625 -0.00503 -0.01479 -0.07030 334 ILE   A N    
1245 C  CA   . ILE   A 182 ? 0.36498 0.38144 0.48303 -0.00118 -0.01670 -0.07594 334 ILE   A CA   
1246 C  C    . ILE   A 182 ? 0.40815 0.43214 0.56514 0.00259  -0.01948 -0.08835 334 ILE   A C    
1247 O  O    . ILE   A 182 ? 0.39116 0.40972 0.57270 0.00534  -0.02454 -0.08575 334 ILE   A O    
1248 C  CB   . ILE   A 182 ? 0.42358 0.44326 0.51702 -0.00204 -0.01234 -0.08369 334 ILE   A CB   
1249 C  CG1  . ILE   A 182 ? 0.36556 0.37391 0.42719 -0.00401 -0.01103 -0.07049 334 ILE   A CG1  
1250 C  CG2  . ILE   A 182 ? 0.40209 0.42540 0.51116 0.00128  -0.01422 -0.09395 334 ILE   A CG2  
1251 C  CD1  . ILE   A 182 ? 0.46931 0.48091 0.50403 -0.00630 -0.00682 -0.07382 334 ILE   A CD1  
1252 N  N    . VAL   A 183 ? 0.35025 0.38737 0.51536 0.00254  -0.01620 -0.10228 335 VAL   A N    
1253 C  CA   . VAL   A 183 ? 0.38374 0.42993 0.58714 0.00687  -0.01774 -0.11896 335 VAL   A CA   
1254 C  C    . VAL   A 183 ? 0.37541 0.42031 0.60764 0.00898  -0.02237 -0.11125 335 VAL   A C    
1255 O  O    . VAL   A 183 ? 0.45922 0.51623 0.70018 0.00917  -0.02001 -0.11882 335 VAL   A O    
1256 C  CB   . VAL   A 183 ? 0.57523 0.64114 0.77262 0.00570  -0.01104 -0.14019 335 VAL   A CB   
1257 C  CG1  . VAL   A 183 ? 0.67020 0.74766 0.90941 0.01070  -0.01182 -0.16170 335 VAL   A CG1  
1258 C  CG2  . VAL   A 183 ? 0.42854 0.49745 0.59537 0.00283  -0.00763 -0.14381 335 VAL   A CG2  
1259 N  N    . SER   A 184 ? 0.37140 0.40379 0.61825 0.01006  -0.02924 -0.09463 336 SER   A N    
1260 C  CA   . SER   A 184 ? 0.38990 0.42190 0.66773 0.01208  -0.03551 -0.08422 336 SER   A CA   
1261 C  C    . SER   A 184 ? 0.39502 0.42085 0.71753 0.01701  -0.04225 -0.08684 336 SER   A C    
1262 O  O    . SER   A 184 ? 0.43037 0.44621 0.75245 0.01611  -0.04511 -0.07984 336 SER   A O    
1263 C  CB   . SER   A 184 ? 0.37575 0.40172 0.63397 0.00756  -0.03875 -0.05937 336 SER   A CB   
1264 O  OG   . SER   A 184 ? 0.52163 0.54868 0.73667 0.00253  -0.03254 -0.05778 336 SER   A OG   
1265 N  N    . PRO   A 185 ? 0.29027 0.32173 0.65402 0.02222  -0.04508 -0.09706 337 PRO   A N    
1266 C  CA   . PRO   A 185 ? 0.32611 0.34992 0.73669 0.02716  -0.05140 -0.10316 337 PRO   A CA   
1267 C  C    . PRO   A 185 ? 0.44146 0.45266 0.87331 0.02625  -0.06143 -0.07635 337 PRO   A C    
1268 O  O    . PRO   A 185 ? 0.54151 0.54329 1.00981 0.02870  -0.06729 -0.07769 337 PRO   A O    
1269 C  CB   . PRO   A 185 ? 0.38880 0.42384 0.83733 0.03360  -0.05091 -0.12285 337 PRO   A CB   
1270 C  CG   . PRO   A 185 ? 0.37357 0.42003 0.80203 0.03156  -0.04809 -0.11495 337 PRO   A CG   
1271 C  CD   . PRO   A 185 ? 0.29726 0.34335 0.66833 0.02401  -0.04201 -0.10650 337 PRO   A CD   
1272 N  N    . ASP   A 186 ? 0.51378 0.52590 0.92474 0.02195  -0.06377 -0.05220 338 ASP   A N    
1273 C  CA   . ASP   A 186 ? 0.44639 0.45191 0.87570 0.01973  -0.07342 -0.02460 338 ASP   A CA   
1274 C  C    . ASP   A 186 ? 0.48297 0.48241 0.88250 0.01355  -0.07304 -0.00978 338 ASP   A C    
1275 O  O    . ASP   A 186 ? 0.45984 0.45859 0.86407 0.00950  -0.07970 0.01545  338 ASP   A O    
1276 C  CB   . ASP   A 186 ? 0.32361 0.33857 0.75089 0.01800  -0.07714 -0.00662 338 ASP   A CB   
1277 C  CG   . ASP   A 186 ? 0.44837 0.47079 0.82278 0.01226  -0.06979 -0.00461 338 ASP   A CG   
1278 O  OD1  . ASP   A 186 ? 0.59304 0.62169 0.95487 0.00751  -0.07335 0.01572  338 ASP   A OD1  
1279 O  OD2  . ASP   A 186 ? 0.48786 0.51065 0.83425 0.01204  -0.06086 -0.02315 338 ASP   A OD2  
1280 N  N    . ARG   A 187 ? 0.46809 0.46567 0.83787 0.01257  -0.06557 -0.02426 339 ARG   A N    
1281 C  CA   . ARG   A 187 ? 0.43269 0.42571 0.77854 0.00786  -0.06509 -0.01229 339 ARG   A CA   
1282 C  C    . ARG   A 187 ? 0.48194 0.46678 0.86520 0.00783  -0.07239 -0.00576 339 ARG   A C    
1283 O  O    . ARG   A 187 ? 0.42595 0.40621 0.84563 0.01223  -0.07469 -0.02147 339 ARG   A O    
1284 C  CB   . ARG   A 187 ? 0.41170 0.40538 0.72088 0.00770  -0.05625 -0.02930 339 ARG   A CB   
1285 C  CG   . ARG   A 187 ? 0.36090 0.36130 0.63590 0.00711  -0.04907 -0.03686 339 ARG   A CG   
1286 C  CD   . ARG   A 187 ? 0.34084 0.34158 0.57959 0.00218  -0.04737 -0.01971 339 ARG   A CD   
1287 N  NE   . ARG   A 187 ? 0.35115 0.35513 0.55512 0.00068  -0.04027 -0.02741 339 ARG   A NE   
1288 C  CZ   . ARG   A 187 ? 0.41960 0.42389 0.59372 -0.00356 -0.03828 -0.01648 339 ARG   A CZ   
1289 N  NH1  . ARG   A 187 ? 0.40378 0.40863 0.57713 -0.00663 -0.04233 0.00144  339 ARG   A NH1  
1290 N  NH2  . ARG   A 187 ? 0.39951 0.40480 0.54555 -0.00542 -0.03234 -0.02355 339 ARG   A NH2  
1291 N  N    . PRO   A 188 ? 0.63778 0.62176 1.01457 0.00241  -0.07605 0.01652  340 PRO   A N    
1292 C  CA   . PRO   A 188 ? 0.58770 0.56437 1.00177 0.00080  -0.08355 0.02557  340 PRO   A CA   
1293 C  C    . PRO   A 188 ? 0.49315 0.46416 0.91067 0.00241  -0.08017 0.00411  340 PRO   A C    
1294 O  O    . PRO   A 188 ? 0.50861 0.48323 0.88910 0.00192  -0.07278 -0.00618 340 PRO   A O    
1295 C  CB   . PRO   A 188 ? 0.71506 0.69782 1.11050 -0.00677 -0.08593 0.05356  340 PRO   A CB   
1296 C  CG   . PRO   A 188 ? 0.73663 0.72711 1.07961 -0.00793 -0.07713 0.04973  340 PRO   A CG   
1297 C  CD   . PRO   A 188 ? 0.64714 0.63848 0.98396 -0.00311 -0.07342 0.03385  340 PRO   A CD   
1298 N  N    . GLY   A 189 ? 0.50159 0.46402 0.96602 0.00423  -0.08626 -0.00262 341 GLY   A N    
1299 C  CA   . GLY   A 189 ? 0.54277 0.50128 1.01639 0.00496  -0.08428 -0.02428 341 GLY   A CA   
1300 C  C    . GLY   A 189 ? 0.51328 0.47540 0.98782 0.01091  -0.07847 -0.05737 341 GLY   A C    
1301 O  O    . GLY   A 189 ? 0.50653 0.46877 0.98746 0.01109  -0.07669 -0.07791 341 GLY   A O    
1302 N  N    . VAL   A 190 ? 0.47942 0.44735 0.94751 0.01498  -0.07539 -0.06344 342 VAL   A N    
1303 C  CA   . VAL   A 190 ? 0.47357 0.44937 0.94286 0.01983  -0.06933 -0.09473 342 VAL   A CA   
1304 C  C    . VAL   A 190 ? 0.51172 0.48168 1.03782 0.02405  -0.07450 -0.11281 342 VAL   A C    
1305 O  O    . VAL   A 190 ? 0.53980 0.50091 1.10742 0.02625  -0.08247 -0.10064 342 VAL   A O    
1306 C  CB   . VAL   A 190 ? 0.48940 0.47446 0.94007 0.02221  -0.06497 -0.09472 342 VAL   A CB   
1307 C  CG1  . VAL   A 190 ? 0.55401 0.54950 1.02022 0.02738  -0.06018 -0.12604 342 VAL   A CG1  
1308 C  CG2  . VAL   A 190 ? 0.45497 0.44583 0.84833 0.01810  -0.05823 -0.08570 342 VAL   A CG2  
1309 N  N    . GLN   A 191 ? 0.44520 0.42091 0.97483 0.02505  -0.07039 -0.14218 343 GLN   A N    
1310 C  CA   . GLN   A 191 ? 0.48609 0.46125 1.06586 0.02825  -0.07387 -0.16382 343 GLN   A CA   
1311 C  C    . GLN   A 191 ? 0.49891 0.49028 1.08888 0.03336  -0.06919 -0.18573 343 GLN   A C    
1312 O  O    . GLN   A 191 ? 0.55966 0.55077 1.18640 0.03582  -0.07419 -0.18201 343 GLN   A O    
1313 C  CB   . GLN   A 191 ? 0.52755 0.50972 1.10170 0.02482  -0.07154 -0.18258 343 GLN   A CB   
1314 C  CG   . GLN   A 191 ? 0.58770 0.55718 1.17829 0.01996  -0.07875 -0.16466 343 GLN   A CG   
1315 C  CD   . GLN   A 191 ? 0.72965 0.70407 1.29621 0.01552  -0.07550 -0.17673 343 GLN   A CD   
1316 O  OE1  . GLN   A 191 ? 0.62845 0.61967 1.18015 0.01656  -0.06918 -0.20342 343 GLN   A OE1  
1317 N  NE2  . GLN   A 191 ? 0.74303 0.70588 1.30565 0.00968  -0.08003 -0.15618 343 GLN   A NE2  
1318 N  N    . ASP   A 192 ? 0.51618 0.52331 1.07363 0.03395  -0.05983 -0.20793 344 ASP   A N    
1319 C  CA   . ASP   A 192 ? 0.56516 0.59267 1.12935 0.03730  -0.05421 -0.23073 344 ASP   A CA   
1320 C  C    . ASP   A 192 ? 0.50177 0.52896 1.04772 0.04082  -0.05107 -0.22009 344 ASP   A C    
1321 O  O    . ASP   A 192 ? 0.54516 0.58789 1.04879 0.03835  -0.04283 -0.22549 344 ASP   A O    
1322 C  CB   . ASP   A 192 ? 0.62678 0.67725 1.16672 0.03478  -0.04588 -0.25889 344 ASP   A CB   
1323 C  CG   . ASP   A 192 ? 0.70933 0.78465 1.26684 0.03661  -0.04136 -0.28471 344 ASP   A CG   
1324 O  OD1  . ASP   A 192 ? 0.68291 0.78158 1.22565 0.03393  -0.03516 -0.30746 344 ASP   A OD1  
1325 O  OD2  . ASP   A 192 ? 0.69389 0.76701 1.27981 0.04020  -0.04425 -0.28172 344 ASP   A OD2  
1326 N  N    . ALA   A 193 ? 0.50033 0.51570 1.07374 0.04358  -0.05845 -0.19857 345 ALA   A N    
1327 C  CA   . ALA   A 193 ? 0.45343 0.47345 1.00547 0.04393  -0.05699 -0.18048 345 ALA   A CA   
1328 C  C    . ALA   A 193 ? 0.41928 0.46079 0.97177 0.04767  -0.04940 -0.20413 345 ALA   A C    
1329 O  O    . ALA   A 193 ? 0.37252 0.42484 0.88761 0.04457  -0.04407 -0.19625 345 ALA   A O    
1330 C  CB   . ALA   A 193 ? 0.50860 0.51456 1.09497 0.04620  -0.06765 -0.15302 345 ALA   A CB   
1331 N  N    . LYS   A 194 ? 0.46189 0.51315 1.04830 0.05013  -0.04891 -0.22984 346 LYS   A N    
1332 C  CA   . LYS   A 194 ? 0.57356 0.64875 1.15936 0.05196  -0.04165 -0.25145 346 LYS   A CA   
1333 C  C    . LYS   A 194 ? 0.46622 0.56229 1.00874 0.04860  -0.03020 -0.27100 346 LYS   A C    
1334 O  O    . LYS   A 194 ? 0.41056 0.52603 0.93526 0.04905  -0.02256 -0.27870 346 LYS   A O    
1335 C  CB   . LYS   A 194 ? 0.66281 0.74473 1.29240 0.05247  -0.04513 -0.27052 346 LYS   A CB   
1336 C  CG   . LYS   A 194 ? 0.83703 0.91383 1.50100 0.05688  -0.05107 -0.26011 346 LYS   A CG   
1337 C  CD   . LYS   A 194 ? 0.88448 0.98562 1.55806 0.05880  -0.04492 -0.28610 346 LYS   A CD   
1338 C  CE   . LYS   A 194 ? 0.93544 1.03145 1.63952 0.06377  -0.05061 -0.27378 346 LYS   A CE   
1339 N  NZ   . LYS   A 194 ? 0.92251 1.04127 1.64224 0.06596  -0.04549 -0.30031 346 LYS   A NZ   
1340 N  N    . LEU   A 195 ? 0.49960 0.59398 1.02414 0.04428  -0.02909 -0.27751 347 LEU   A N    
1341 C  CA   . LEU   A 195 ? 0.49817 0.61168 0.97729 0.03962  -0.01945 -0.29108 347 LEU   A CA   
1342 C  C    . LEU   A 195 ? 0.47111 0.57820 0.89926 0.03404  -0.01785 -0.26188 347 LEU   A C    
1343 O  O    . LEU   A 195 ? 0.48073 0.60612 0.87327 0.02959  -0.01032 -0.26466 347 LEU   A O    
1344 C  CB   . LEU   A 195 ? 0.48586 0.60201 0.95760 0.03502  -0.02027 -0.30083 347 LEU   A CB   
1345 C  CG   . LEU   A 195 ? 0.50177 0.63607 0.92407 0.02895  -0.01250 -0.30920 347 LEU   A CG   
1346 C  CD1  . LEU   A 195 ? 0.48321 0.65137 0.89305 0.02655  -0.00377 -0.32764 347 LEU   A CD1  
1347 C  CD2  . LEU   A 195 ? 0.39585 0.53426 0.81749 0.02538  -0.01460 -0.31744 347 LEU   A CD2  
1348 N  N    . VAL   A 196 ? 0.44080 0.52344 0.86499 0.03321  -0.02496 -0.23320 348 VAL   A N    
1349 C  CA   . VAL   A 196 ? 0.36185 0.43806 0.74212 0.02814  -0.02399 -0.20583 348 VAL   A CA   
1350 C  C    . VAL   A 196 ? 0.32110 0.40688 0.70080 0.02875  -0.02166 -0.20114 348 VAL   A C    
1351 O  O    . VAL   A 196 ? 0.41790 0.51128 0.75809 0.02347  -0.01632 -0.19366 348 VAL   A O    
1352 C  CB   . VAL   A 196 ? 0.30143 0.35362 0.68385 0.02737  -0.03208 -0.17831 348 VAL   A CB   
1353 C  CG1  . VAL   A 196 ? 0.33655 0.38354 0.67643 0.02243  -0.03084 -0.15307 348 VAL   A CG1  
1354 C  CG2  . VAL   A 196 ? 0.30069 0.34584 0.68257 0.02595  -0.03393 -0.18317 348 VAL   A CG2  
1355 N  N    . GLU   A 197 ? 0.29557 0.38149 0.72132 0.03510  -0.02598 -0.20560 349 GLU   A N    
1356 C  CA   . GLU   A 197 ? 0.37905 0.47617 0.80868 0.03607  -0.02452 -0.20131 349 GLU   A CA   
1357 C  C    . GLU   A 197 ? 0.36547 0.49033 0.77985 0.03407  -0.01420 -0.22501 349 GLU   A C    
1358 O  O    . GLU   A 197 ? 0.36101 0.49657 0.75115 0.02982  -0.01010 -0.21732 349 GLU   A O    
1359 C  CB   . GLU   A 197 ? 0.41725 0.50946 0.90470 0.04439  -0.03235 -0.20110 349 GLU   A CB   
1360 C  CG   . GLU   A 197 ? 0.53316 0.64040 1.03191 0.04656  -0.03140 -0.19931 349 GLU   A CG   
1361 C  CD   . GLU   A 197 ? 0.68035 0.77645 1.22435 0.05271  -0.04244 -0.18180 349 GLU   A CD   
1362 O  OE1  . GLU   A 197 ? 0.71229 0.79816 1.30349 0.05954  -0.04863 -0.18917 349 GLU   A OE1  
1363 O  OE2  . GLU   A 197 ? 0.75359 0.85171 1.28704 0.05025  -0.04544 -0.16022 349 GLU   A OE2  
1364 N  N    . ALA   A 198 ? 0.39893 0.53781 0.82696 0.03606  -0.00984 -0.25410 350 ALA   A N    
1365 C  CA   . ALA   A 198 ? 0.44411 0.61447 0.85692 0.03300  0.00039  -0.27717 350 ALA   A CA   
1366 C  C    . ALA   A 198 ? 0.42226 0.59801 0.77557 0.02295  0.00607  -0.26489 350 ALA   A C    
1367 O  O    . ALA   A 198 ? 0.40844 0.60373 0.74034 0.01795  0.01260  -0.26582 350 ALA   A O    
1368 C  CB   . ALA   A 198 ? 0.50575 0.69220 0.94489 0.03645  0.00357  -0.31198 350 ALA   A CB   
1369 N  N    . ILE   A 199 ? 0.39211 0.55095 0.72018 0.01980  0.00338  -0.25272 351 ILE   A N    
1370 C  CA   . ILE   A 199 ? 0.41059 0.57138 0.68573 0.01129  0.00753  -0.23920 351 ILE   A CA   
1371 C  C    . ILE   A 199 ? 0.37165 0.52155 0.62569 0.00777  0.00666  -0.21383 351 ILE   A C    
1372 O  O    . ILE   A 199 ? 0.39341 0.55502 0.61539 0.00080  0.01226  -0.20933 351 ILE   A O    
1373 C  CB   . ILE   A 199 ? 0.39126 0.53557 0.64951 0.01020  0.00389  -0.23118 351 ILE   A CB   
1374 C  CG1  . ILE   A 199 ? 0.45492 0.61387 0.73144 0.01203  0.00508  -0.25842 351 ILE   A CG1  
1375 C  CG2  . ILE   A 199 ? 0.36288 0.50574 0.57017 0.00272  0.00694  -0.21429 351 ILE   A CG2  
1376 C  CD1  . ILE   A 199 ? 0.42943 0.57024 0.70531 0.01277  -0.00059 -0.25214 351 ILE   A CD1  
1377 N  N    . GLN   A 200 ? 0.38885 0.51748 0.66102 0.01163  -0.00065 -0.19659 352 GLN   A N    
1378 C  CA   . GLN   A 200 ? 0.35688 0.47708 0.61082 0.00787  -0.00205 -0.17403 352 GLN   A CA   
1379 C  C    . GLN   A 200 ? 0.39597 0.53709 0.65874 0.00664  0.00214  -0.18159 352 GLN   A C    
1380 O  O    . GLN   A 200 ? 0.41278 0.55706 0.64722 -0.00022 0.00513  -0.17032 352 GLN   A O    
1381 C  CB   . GLN   A 200 ? 0.29479 0.39365 0.56930 0.01179  -0.01116 -0.15508 352 GLN   A CB   
1382 C  CG   . GLN   A 200 ? 0.38130 0.47140 0.63174 0.00673  -0.01307 -0.13131 352 GLN   A CG   
1383 C  CD   . GLN   A 200 ? 0.47335 0.54996 0.74737 0.00986  -0.02222 -0.11306 352 GLN   A CD   
1384 O  OE1  . GLN   A 200 ? 0.50218 0.58325 0.81671 0.01542  -0.02687 -0.11600 352 GLN   A OE1  
1385 N  NE2  . GLN   A 200 ? 0.44479 0.50644 0.69476 0.00625  -0.02501 -0.09382 352 GLN   A NE2  
1386 N  N    . ASP   A 201 ? 0.37319 0.52910 0.67744 0.01323  0.00233  -0.20132 353 ASP   A N    
1387 C  CA   . ASP   A 201 ? 0.41758 0.59639 0.73484 0.01295  0.00639  -0.20989 353 ASP   A CA   
1388 C  C    . ASP   A 201 ? 0.43687 0.63956 0.71981 0.00428  0.01639  -0.21953 353 ASP   A C    
1389 O  O    . ASP   A 201 ? 0.47927 0.69451 0.74999 -0.00127 0.01981  -0.21375 353 ASP   A O    
1390 C  CB   . ASP   A 201 ? 0.42133 0.61221 0.79316 0.02296  0.00500  -0.23242 353 ASP   A CB   
1391 C  CG   . ASP   A 201 ? 0.52337 0.69470 0.93396 0.03060  -0.00570 -0.21782 353 ASP   A CG   
1392 O  OD1  . ASP   A 201 ? 0.54568 0.69850 0.93835 0.02722  -0.01138 -0.19053 353 ASP   A OD1  
1393 O  OD2  . ASP   A 201 ? 0.60100 0.77654 1.06114 0.03977  -0.00866 -0.23364 353 ASP   A OD2  
1394 N  N    . ARG   A 202 ? 0.42212 0.63296 0.68931 0.00209  0.02076  -0.23309 354 ARG   A N    
1395 C  CA   . ARG   A 202 ? 0.47387 0.70878 0.70645 -0.00744 0.02948  -0.23869 354 ARG   A CA   
1396 C  C    . ARG   A 202 ? 0.42022 0.63967 0.60942 -0.01645 0.02914  -0.21191 354 ARG   A C    
1397 O  O    . ARG   A 202 ? 0.41938 0.65533 0.58779 -0.02496 0.03466  -0.20864 354 ARG   A O    
1398 C  CB   . ARG   A 202 ? 0.50212 0.74957 0.72615 -0.00828 0.03275  -0.25632 354 ARG   A CB   
1399 C  CG   . ARG   A 202 ? 0.57972 0.85762 0.77030 -0.01875 0.04139  -0.26209 354 ARG   A CG   
1400 C  CD   . ARG   A 202 ? 0.73498 1.03347 0.92246 -0.01949 0.04454  -0.28343 354 ARG   A CD   
1401 N  NE   . ARG   A 202 ? 0.86794 1.16567 1.09897 -0.00929 0.04178  -0.30685 354 ARG   A NE   
1402 C  CZ   . ARG   A 202 ? 1.03155 1.31565 1.26767 -0.00581 0.03721  -0.31151 354 ARG   A CZ   
1403 N  NH1  . ARG   A 202 ? 1.01582 1.28760 1.21579 -0.01094 0.03502  -0.29435 354 ARG   A NH1  
1404 N  NH2  . ARG   A 202 ? 1.07022 1.35302 1.34978 0.00279  0.03455  -0.33346 354 ARG   A NH2  
1405 N  N    . LEU   A 203 ? 0.38243 0.57089 0.55922 -0.01502 0.02279  -0.19318 355 LEU   A N    
1406 C  CA   . LEU   A 203 ? 0.28384 0.45542 0.42406 -0.02241 0.02205  -0.16964 355 LEU   A CA   
1407 C  C    . LEU   A 203 ? 0.35597 0.52357 0.50323 -0.02407 0.01993  -0.15780 355 LEU   A C    
1408 O  O    . LEU   A 203 ? 0.35030 0.51690 0.47097 -0.03267 0.02223  -0.14585 355 LEU   A O    
1409 C  CB   . LEU   A 203 ? 0.33960 0.48261 0.46705 -0.01975 0.01645  -0.15570 355 LEU   A CB   
1410 C  CG   . LEU   A 203 ? 0.38301 0.52859 0.50374 -0.01806 0.01717  -0.16540 355 LEU   A CG   
1411 C  CD1  . LEU   A 203 ? 0.32348 0.44254 0.44443 -0.01335 0.01070  -0.15367 355 LEU   A CD1  
1412 C  CD2  . LEU   A 203 ? 0.37253 0.52967 0.45654 -0.02655 0.02239  -0.16266 355 LEU   A CD2  
1413 N  N    . SER   A 204 ? 0.36776 0.53364 0.55202 -0.01637 0.01500  -0.16051 356 SER   A N    
1414 C  CA   . SER   A 204 ? 0.48553 0.65094 0.67880 -0.01781 0.01191  -0.14886 356 SER   A CA   
1415 C  C    . SER   A 204 ? 0.45449 0.64802 0.64812 -0.02343 0.01854  -0.15828 356 SER   A C    
1416 O  O    . SER   A 204 ? 0.45539 0.64942 0.62977 -0.03162 0.01944  -0.14610 356 SER   A O    
1417 C  CB   . SER   A 204 ? 0.63032 0.79003 0.86670 -0.00791 0.00418  -0.14844 356 SER   A CB   
1418 O  OG   . SER   A 204 ? 0.69784 0.83239 0.92769 -0.00702 -0.00315 -0.12858 356 SER   A OG   
1419 N  N    . ASN   A 205 ? 0.44970 0.66850 0.66616 -0.01962 0.02346  -0.18113 357 ASN   A N    
1420 C  CA   . ASN   A 205 ? 0.49191 0.74249 0.70916 -0.02541 0.03086  -0.19180 357 ASN   A CA   
1421 C  C    . ASN   A 205 ? 0.44382 0.70019 0.61620 -0.03855 0.03718  -0.18436 357 ASN   A C    
1422 O  O    . ASN   A 205 ? 0.45221 0.72546 0.61526 -0.04717 0.04135  -0.18115 357 ASN   A O    
1423 C  CB   . ASN   A 205 ? 0.46044 0.73927 0.71054 -0.01854 0.03568  -0.22073 357 ASN   A CB   
1424 C  CG   . ASN   A 205 ? 0.51318 0.78703 0.81428 -0.00537 0.02907  -0.22828 357 ASN   A CG   
1425 O  OD1  . ASN   A 205 ? 0.53919 0.80076 0.85414 -0.00292 0.02220  -0.21238 357 ASN   A OD1  
1426 N  ND2  . ASN   A 205 ? 0.52779 0.81196 0.85840 0.00281  0.03063  -0.25246 357 ASN   A ND2  
1427 N  N    . THR   A 206 ? 0.38891 0.63199 0.53492 -0.04055 0.03748  -0.18050 358 THR   A N    
1428 C  CA   . THR   A 206 ? 0.45729 0.70153 0.56211 -0.05269 0.04173  -0.16922 358 THR   A CA   
1429 C  C    . THR   A 206 ? 0.48878 0.70987 0.57394 -0.05916 0.03812  -0.14635 358 THR   A C    
1430 O  O    . THR   A 206 ? 0.43966 0.66931 0.50441 -0.07046 0.04199  -0.13875 358 THR   A O    
1431 C  CB   . THR   A 206 ? 0.49110 0.72477 0.57562 -0.05190 0.04120  -0.16846 358 THR   A CB   
1432 O  OG1  . THR   A 206 ? 0.52681 0.78271 0.63165 -0.04606 0.04405  -0.19205 358 THR   A OG1  
1433 C  CG2  . THR   A 206 ? 0.60981 0.84793 0.65554 -0.06421 0.04515  -0.15646 358 THR   A CG2  
1434 N  N    . LEU   A 207 ? 0.33437 0.52746 0.42597 -0.05294 0.03072  -0.13556 359 LEU   A N    
1435 C  CA   . LEU   A 207 ? 0.36978 0.54269 0.44383 -0.05897 0.02724  -0.11661 359 LEU   A CA   
1436 C  C    . LEU   A 207 ? 0.33101 0.52030 0.41947 -0.06323 0.02765  -0.11645 359 LEU   A C    
1437 O  O    . LEU   A 207 ? 0.36343 0.55150 0.43221 -0.07395 0.02915  -0.10659 359 LEU   A O    
1438 C  CB   . LEU   A 207 ? 0.38700 0.53197 0.46533 -0.05161 0.01965  -0.10658 359 LEU   A CB   
1439 C  CG   . LEU   A 207 ? 0.44392 0.57105 0.50735 -0.05715 0.01574  -0.08985 359 LEU   A CG   
1440 C  CD1  . LEU   A 207 ? 0.38934 0.50505 0.41709 -0.06717 0.01905  -0.08116 359 LEU   A CD1  
1441 C  CD2  . LEU   A 207 ? 0.39272 0.49921 0.46307 -0.04994 0.00871  -0.08134 359 LEU   A CD2  
1442 N  N    . GLN   A 208 ? 0.29364 0.49833 0.41865 -0.05495 0.02589  -0.12727 360 GLN   A N    
1443 C  CA   . GLN   A 208 ? 0.35162 0.57522 0.49438 -0.05788 0.02576  -0.12763 360 GLN   A CA   
1444 C  C    . GLN   A 208 ? 0.39179 0.64250 0.52217 -0.06870 0.03437  -0.13425 360 GLN   A C    
1445 O  O    . GLN   A 208 ? 0.45469 0.71134 0.57620 -0.07842 0.03501  -0.12590 360 GLN   A O    
1446 C  CB   . GLN   A 208 ? 0.41623 0.65313 0.60489 -0.04553 0.02238  -0.13954 360 GLN   A CB   
1447 C  CG   . GLN   A 208 ? 0.48412 0.69735 0.68976 -0.03633 0.01268  -0.12929 360 GLN   A CG   
1448 C  CD   . GLN   A 208 ? 0.65880 0.88515 0.91350 -0.02534 0.00797  -0.13714 360 GLN   A CD   
1449 O  OE1  . GLN   A 208 ? 0.68093 0.92449 0.95308 -0.02642 0.00653  -0.13557 360 GLN   A OE1  
1450 N  NE2  . GLN   A 208 ? 0.80794 1.02623 1.08732 -0.01472 0.00508  -0.14548 360 GLN   A NE2  
1451 N  N    . THR   A 209 ? 0.42198 0.69162 0.55158 -0.06814 0.04104  -0.14927 361 THR   A N    
1452 C  CA   . THR   A 209 ? 0.43138 0.73163 0.54883 -0.07942 0.04970  -0.15511 361 THR   A CA   
1453 C  C    . THR   A 209 ? 0.47688 0.76229 0.55337 -0.09342 0.05098  -0.13682 361 THR   A C    
1454 O  O    . THR   A 209 ? 0.33588 0.63737 0.40233 -0.10570 0.05503  -0.13199 361 THR   A O    
1455 C  CB   . THR   A 209 ? 0.47648 0.80356 0.60201 -0.07581 0.05633  -0.17630 361 THR   A CB   
1456 O  OG1  . THR   A 209 ? 0.41678 0.75393 0.58473 -0.06193 0.05452  -0.19463 361 THR   A OG1  
1457 C  CG2  . THR   A 209 ? 0.52598 0.89181 0.64148 -0.08803 0.06578  -0.18293 361 THR   A CG2  
1458 N  N    . TYR   A 210 ? 0.38699 0.64160 0.44171 -0.09183 0.04729  -0.12624 362 TYR   A N    
1459 C  CA   . TYR   A 210 ? 0.39238 0.62956 0.41215 -0.10377 0.04762  -0.10873 362 TYR   A CA   
1460 C  C    . TYR   A 210 ? 0.35626 0.58002 0.37193 -0.11119 0.04434  -0.09593 362 TYR   A C    
1461 O  O    . TYR   A 210 ? 0.45821 0.68385 0.45525 -0.12477 0.04698  -0.08642 362 TYR   A O    
1462 C  CB   . TYR   A 210 ? 0.39907 0.60518 0.40113 -0.09855 0.04353  -0.10065 362 TYR   A CB   
1463 C  CG   . TYR   A 210 ? 0.41278 0.59726 0.38345 -0.10920 0.04284  -0.08244 362 TYR   A CG   
1464 C  CD1  . TYR   A 210 ? 0.41487 0.56976 0.37819 -0.11076 0.03779  -0.07026 362 TYR   A CD1  
1465 C  CD2  . TYR   A 210 ? 0.47115 0.66636 0.42108 -0.11815 0.04700  -0.07753 362 TYR   A CD2  
1466 C  CE1  . TYR   A 210 ? 0.44464 0.57842 0.38333 -0.11999 0.03707  -0.05565 362 TYR   A CE1  
1467 C  CE2  . TYR   A 210 ? 0.43105 0.60472 0.35640 -0.12757 0.04552  -0.05968 362 TYR   A CE2  
1468 C  CZ   . TYR   A 210 ? 0.49131 0.63295 0.41240 -0.12801 0.04065  -0.04975 362 TYR   A CZ   
1469 O  OH   . TYR   A 210 ? 0.51781 0.63647 0.41824 -0.13678 0.03906  -0.03395 362 TYR   A OH   
1470 N  N    . ILE   A 211 ? 0.42238 0.63315 0.45548 -0.10330 0.03813  -0.09487 363 ILE   A N    
1471 C  CA   . ILE   A 211 ? 0.40081 0.60031 0.42935 -0.11051 0.03428  -0.08371 363 ILE   A CA   
1472 C  C    . ILE   A 211 ? 0.45505 0.68476 0.49335 -0.12017 0.03828  -0.08726 363 ILE   A C    
1473 O  O    . ILE   A 211 ? 0.51684 0.74279 0.53969 -0.13330 0.03877  -0.07789 363 ILE   A O    
1474 C  CB   . ILE   A 211 ? 0.33076 0.51614 0.37689 -0.10020 0.02642  -0.08139 363 ILE   A CB   
1475 C  CG1  . ILE   A 211 ? 0.39170 0.54529 0.42224 -0.09430 0.02265  -0.07448 363 ILE   A CG1  
1476 C  CG2  . ILE   A 211 ? 0.37185 0.55785 0.41950 -0.10782 0.02259  -0.07354 363 ILE   A CG2  
1477 C  CD1  . ILE   A 211 ? 0.33473 0.47857 0.38395 -0.08366 0.01540  -0.07224 363 ILE   A CD1  
1478 N  N    . ARG   A 212 ? 0.49884 0.75963 0.56454 -0.11403 0.04135  -0.10176 364 ARG   A N    
1479 C  CA   . ARG   A 212 ? 0.58961 0.88309 0.66872 -0.12198 0.04528  -0.10650 364 ARG   A CA   
1480 C  C    . ARG   A 212 ? 0.51709 0.82732 0.57397 -0.13716 0.05327  -0.10437 364 ARG   A C    
1481 O  O    . ARG   A 212 ? 0.53983 0.86447 0.59436 -0.14977 0.05527  -0.09956 364 ARG   A O    
1482 C  CB   . ARG   A 212 ? 0.67909 1.00231 0.79655 -0.11002 0.04679  -0.12449 364 ARG   A CB   
1483 C  CG   . ARG   A 212 ? 0.85203 1.16636 0.99803 -0.09850 0.03794  -0.12274 364 ARG   A CG   
1484 C  CD   . ARG   A 212 ? 0.98164 1.30905 1.16430 -0.08242 0.03753  -0.13940 364 ARG   A CD   
1485 N  NE   . ARG   A 212 ? 1.10547 1.40920 1.30547 -0.07074 0.02770  -0.13240 364 ARG   A NE   
1486 C  CZ   . ARG   A 212 ? 1.12124 1.42462 1.33963 -0.06861 0.01993  -0.12294 364 ARG   A CZ   
1487 N  NH1  . ARG   A 212 ? 1.12332 1.40677 1.35590 -0.05895 0.01101  -0.11482 364 ARG   A NH1  
1488 N  NH2  . ARG   A 212 ? 1.12402 1.44910 1.34708 -0.07681 0.02071  -0.12068 364 ARG   A NH2  
1489 N  N    . CYS   A 213 ? 0.46785 0.77769 0.50844 -0.13713 0.05738  -0.10653 365 CYS   A N    
1490 C  CA   . CYS   A 213 ? 0.53189 0.86324 0.55302 -0.15158 0.06484  -0.10356 365 CYS   A CA   
1491 C  C    . CYS   A 213 ? 0.47084 0.77241 0.45876 -0.16333 0.06283  -0.08333 365 CYS   A C    
1492 O  O    . CYS   A 213 ? 0.61519 0.93048 0.58876 -0.17909 0.06710  -0.07479 365 CYS   A O    
1493 C  CB   . CYS   A 213 ? 0.54559 0.90162 0.56880 -0.14624 0.07070  -0.11806 365 CYS   A CB   
1494 S  SG   . CYS   A 213 ? 0.64470 1.04081 0.71055 -0.13323 0.07474  -0.14611 365 CYS   A SG   
1495 N  N    . ARG   A 214 ? 0.45997 0.72197 0.43708 -0.15627 0.05644  -0.07528 366 ARG   A N    
1496 C  CA   . ARG   A 214 ? 0.46189 0.69491 0.41067 -0.16501 0.05450  -0.05800 366 ARG   A CA   
1497 C  C    . ARG   A 214 ? 0.53157 0.72726 0.47447 -0.16596 0.04780  -0.04780 366 ARG   A C    
1498 O  O    . ARG   A 214 ? 0.62989 0.80152 0.55287 -0.17465 0.04627  -0.03422 366 ARG   A O    
1499 C  CB   . ARG   A 214 ? 0.48630 0.70848 0.42300 -0.15696 0.05402  -0.05761 366 ARG   A CB   
1500 C  CG   . ARG   A 214 ? 0.55562 0.81681 0.49574 -0.15681 0.06065  -0.06928 366 ARG   A CG   
1501 C  CD   . ARG   A 214 ? 0.68473 0.96178 0.60297 -0.17339 0.06503  -0.05671 366 ARG   A CD   
1502 N  NE   . ARG   A 214 ? 0.85414 1.16525 0.76899 -0.17296 0.07035  -0.06592 366 ARG   A NE   
1503 C  CZ   . ARG   A 214 ? 0.95368 1.31065 0.88178 -0.17540 0.07765  -0.08209 366 ARG   A CZ   
1504 N  NH1  . ARG   A 214 ? 0.92135 1.30985 0.84446 -0.17547 0.08237  -0.09164 366 ARG   A NH1  
1505 N  NH2  . ARG   A 214 ? 0.88309 1.25677 0.83016 -0.17781 0.08025  -0.08967 366 ARG   A NH2  
1506 N  N    . HIS   A 215 ? 0.38541 0.57664 0.34576 -0.15769 0.04354  -0.05382 367 HIS   A N    
1507 C  CA   . HIS   A 215 ? 0.40552 0.56754 0.35961 -0.16020 0.03765  -0.04585 367 HIS   A CA   
1508 C  C    . HIS   A 215 ? 0.45911 0.63741 0.42176 -0.17173 0.03775  -0.04547 367 HIS   A C    
1509 O  O    . HIS   A 215 ? 0.54845 0.75033 0.53377 -0.16674 0.03714  -0.05385 367 HIS   A O    
1510 C  CB   . HIS   A 215 ? 0.38547 0.53249 0.35040 -0.14518 0.03190  -0.04985 367 HIS   A CB   
1511 C  CG   . HIS   A 215 ? 0.46927 0.58178 0.41936 -0.14590 0.02685  -0.04176 367 HIS   A CG   
1512 N  ND1  . HIS   A 215 ? 0.41213 0.50079 0.35424 -0.13584 0.02433  -0.03997 367 HIS   A ND1  
1513 C  CD2  . HIS   A 215 ? 0.45528 0.55507 0.39787 -0.15578 0.02419  -0.03669 367 HIS   A CD2  
1514 C  CE1  . HIS   A 215 ? 0.36311 0.42679 0.29382 -0.13891 0.02076  -0.03466 367 HIS   A CE1  
1515 N  NE2  . HIS   A 215 ? 0.49071 0.56013 0.42137 -0.15105 0.02055  -0.03323 367 HIS   A NE2  
1516 N  N    . PRO   A 216 ? 0.48200 0.64897 0.42975 -0.18707 0.03799  -0.03597 368 PRO   A N    
1517 C  CA   . PRO   A 216 ? 0.48182 0.66712 0.43808 -0.19980 0.03829  -0.03594 368 PRO   A CA   
1518 C  C    . PRO   A 216 ? 0.44966 0.62487 0.41417 -0.19672 0.03151  -0.03787 368 PRO   A C    
1519 O  O    . PRO   A 216 ? 0.50413 0.65066 0.46040 -0.18970 0.02687  -0.03599 368 PRO   A O    
1520 C  CB   . PRO   A 216 ? 0.55049 0.72096 0.48747 -0.21740 0.03997  -0.02402 368 PRO   A CB   
1521 C  CG   . PRO   A 216 ? 0.57904 0.71097 0.49896 -0.21136 0.03706  -0.01764 368 PRO   A CG   
1522 C  CD   . PRO   A 216 ? 0.49359 0.63073 0.41834 -0.19374 0.03770  -0.02452 368 PRO   A CD   
1523 N  N    . PRO   A 217 ? 0.44971 0.65085 0.43065 -0.20211 0.03069  -0.04147 369 PRO   A N    
1524 C  CA   . PRO   A 217 ? 0.43077 0.62592 0.41721 -0.20267 0.02367  -0.04144 369 PRO   A CA   
1525 C  C    . PRO   A 217 ? 0.48267 0.64986 0.44908 -0.21640 0.02158  -0.03544 369 PRO   A C    
1526 O  O    . PRO   A 217 ? 0.44159 0.60098 0.39566 -0.22873 0.02552  -0.03012 369 PRO   A O    
1527 C  CB   . PRO   A 217 ? 0.43413 0.66844 0.44316 -0.20752 0.02410  -0.04579 369 PRO   A CB   
1528 C  CG   . PRO   A 217 ? 0.37747 0.63155 0.38441 -0.21732 0.03226  -0.04595 369 PRO   A CG   
1529 C  CD   . PRO   A 217 ? 0.39337 0.63409 0.38897 -0.20854 0.03623  -0.04591 369 PRO   A CD   
1530 N  N    . PRO   A 218 ? 0.51535 0.66792 0.47912 -0.21534 0.01524  -0.03623 370 PRO   A N    
1531 C  CA   . PRO   A 218 ? 0.50339 0.66611 0.48098 -0.20324 0.00940  -0.03919 370 PRO   A CA   
1532 C  C    . PRO   A 218 ? 0.53915 0.68148 0.51217 -0.18711 0.00782  -0.03887 370 PRO   A C    
1533 O  O    . PRO   A 218 ? 0.53200 0.68211 0.51719 -0.17696 0.00279  -0.03919 370 PRO   A O    
1534 C  CB   . PRO   A 218 ? 0.52874 0.68688 0.50065 -0.21419 0.00389  -0.03941 370 PRO   A CB   
1535 C  CG   . PRO   A 218 ? 0.54397 0.67054 0.49446 -0.22492 0.00630  -0.03810 370 PRO   A CG   
1536 C  CD   . PRO   A 218 ? 0.50960 0.63683 0.45731 -0.22868 0.01319  -0.03417 370 PRO   A CD   
1537 N  N    . GLY   A 219 ? 0.52916 0.64691 0.48596 -0.18529 0.01157  -0.03694 371 GLY   A N    
1538 C  CA   . GLY   A 219 ? 0.50989 0.60907 0.46228 -0.17080 0.01023  -0.03672 371 GLY   A CA   
1539 C  C    . GLY   A 219 ? 0.48422 0.60210 0.45608 -0.15655 0.01025  -0.03969 371 GLY   A C    
1540 O  O    . GLY   A 219 ? 0.44964 0.55949 0.42556 -0.14476 0.00676  -0.03936 371 GLY   A O    
1541 N  N    . SER   A 220 ? 0.43118 0.57510 0.41697 -0.15778 0.01424  -0.04333 372 SER   A N    
1542 C  CA   . SER   A 220 ? 0.44123 0.60352 0.44910 -0.14433 0.01478  -0.04914 372 SER   A CA   
1543 C  C    . SER   A 220 ? 0.42572 0.60350 0.45816 -0.13714 0.00820  -0.04944 372 SER   A C    
1544 O  O    . SER   A 220 ? 0.53217 0.71917 0.58591 -0.12430 0.00699  -0.05348 372 SER   A O    
1545 C  CB   . SER   A 220 ? 0.46104 0.65036 0.47750 -0.14845 0.02170  -0.05526 372 SER   A CB   
1546 O  OG   . SER   A 220 ? 0.49923 0.70989 0.52285 -0.16016 0.02208  -0.05500 372 SER   A OG   
1547 N  N    . HIS   A 221 ? 0.50862 0.69018 0.53998 -0.14542 0.00343  -0.04502 373 HIS   A N    
1548 C  CA   . HIS   A 221 ? 0.50259 0.70436 0.55846 -0.14046 -0.00365 -0.04290 373 HIS   A CA   
1549 C  C    . HIS   A 221 ? 0.49030 0.68189 0.55572 -0.12637 -0.00922 -0.03903 373 HIS   A C    
1550 O  O    . HIS   A 221 ? 0.40275 0.57333 0.45021 -0.12662 -0.01201 -0.03398 373 HIS   A O    
1551 C  CB   . HIS   A 221 ? 0.50787 0.71388 0.55537 -0.15322 -0.00839 -0.03827 373 HIS   A CB   
1552 C  CG   . HIS   A 221 ? 0.53511 0.76342 0.60598 -0.14902 -0.01697 -0.03335 373 HIS   A CG   
1553 N  ND1  . HIS   A 221 ? 0.49810 0.75654 0.60022 -0.14439 -0.01832 -0.03519 373 HIS   A ND1  
1554 C  CD2  . HIS   A 221 ? 0.52232 0.74921 0.59097 -0.14871 -0.02500 -0.02589 373 HIS   A CD2  
1555 C  CE1  . HIS   A 221 ? 0.55074 0.82370 0.66989 -0.14113 -0.02761 -0.02744 373 HIS   A CE1  
1556 N  NE2  . HIS   A 221 ? 0.51053 0.76590 0.60862 -0.14431 -0.03182 -0.02115 373 HIS   A NE2  
1557 N  N    . GLN   A 222 ? 0.42069 0.62797 0.51620 -0.11436 -0.01080 -0.04183 374 GLN   A N    
1558 C  CA   . GLN   A 222 ? 0.29212 0.49152 0.40262 -0.10124 -0.01667 -0.03712 374 GLN   A CA   
1559 C  C    . GLN   A 222 ? 0.39618 0.56676 0.48463 -0.09735 -0.01376 -0.03728 374 GLN   A C    
1560 O  O    . GLN   A 222 ? 0.35239 0.51111 0.44123 -0.09132 -0.01886 -0.03031 374 GLN   A O    
1561 C  CB   . GLN   A 222 ? 0.45978 0.66557 0.57633 -0.10281 -0.02641 -0.02510 374 GLN   A CB   
1562 C  CG   . GLN   A 222 ? 0.68329 0.91993 0.83089 -0.10240 -0.03189 -0.02255 374 GLN   A CG   
1563 C  CD   . GLN   A 222 ? 0.84929 1.09815 1.03539 -0.08831 -0.03253 -0.02759 374 GLN   A CD   
1564 O  OE1  . GLN   A 222 ? 0.96418 1.23082 1.16581 -0.08769 -0.02737 -0.03833 374 GLN   A OE1  
1565 N  NE2  . GLN   A 222 ? 0.77692 1.01710 0.97999 -0.07726 -0.03873 -0.02056 374 GLN   A NE2  
1566 N  N    . LEU   A 223 ? 0.38534 0.54661 0.45506 -0.10125 -0.00584 -0.04410 375 LEU   A N    
1567 C  CA   . LEU   A 223 ? 0.39125 0.52583 0.43844 -0.09866 -0.00340 -0.04332 375 LEU   A CA   
1568 C  C    . LEU   A 223 ? 0.44752 0.57800 0.51156 -0.08477 -0.00496 -0.04556 375 LEU   A C    
1569 O  O    . LEU   A 223 ? 0.52938 0.64121 0.58394 -0.08038 -0.00743 -0.04056 375 LEU   A O    
1570 C  CB   . LEU   A 223 ? 0.40085 0.52951 0.42720 -0.10614 0.00440  -0.04787 375 LEU   A CB   
1571 C  CG   . LEU   A 223 ? 0.46060 0.56221 0.46359 -0.10402 0.00652  -0.04589 375 LEU   A CG   
1572 C  CD1  . LEU   A 223 ? 0.40298 0.48441 0.39237 -0.10459 0.00191  -0.03903 375 LEU   A CD1  
1573 C  CD2  . LEU   A 223 ? 0.57500 0.67169 0.55774 -0.11373 0.01265  -0.04628 375 LEU   A CD2  
1574 N  N    . TYR   A 224 ? 0.35549 0.50403 0.44592 -0.07800 -0.00339 -0.05418 376 TYR   A N    
1575 C  CA   . TYR   A 224 ? 0.41543 0.55994 0.52586 -0.06528 -0.00535 -0.05793 376 TYR   A CA   
1576 C  C    . TYR   A 224 ? 0.42598 0.56563 0.55249 -0.05960 -0.01447 -0.04664 376 TYR   A C    
1577 O  O    . TYR   A 224 ? 0.40871 0.53312 0.53541 -0.05321 -0.01693 -0.04318 376 TYR   A O    
1578 C  CB   . TYR   A 224 ? 0.35622 0.52335 0.49629 -0.05922 -0.00217 -0.07185 376 TYR   A CB   
1579 C  CG   . TYR   A 224 ? 0.43186 0.59419 0.59522 -0.04665 -0.00408 -0.07842 376 TYR   A CG   
1580 C  CD1  . TYR   A 224 ? 0.38895 0.53767 0.53609 -0.04448 -0.00023 -0.08372 376 TYR   A CD1  
1581 C  CD2  . TYR   A 224 ? 0.45757 0.62876 0.66089 -0.03726 -0.01042 -0.07873 376 TYR   A CD2  
1582 C  CE1  . TYR   A 224 ? 0.50808 0.65271 0.67714 -0.03407 -0.00218 -0.09076 376 TYR   A CE1  
1583 C  CE2  . TYR   A 224 ? 0.40929 0.57411 0.63659 -0.02650 -0.01259 -0.08513 376 TYR   A CE2  
1584 C  CZ   . TYR   A 224 ? 0.50938 0.66113 0.71885 -0.02535 -0.00823 -0.09191 376 TYR   A CZ   
1585 O  OH   . TYR   A 224 ? 0.53116 0.67702 0.76512 -0.01567 -0.01055 -0.09937 376 TYR   A OH   
1586 N  N    . ALA   A 225 ? 0.32602 0.48048 0.46597 -0.06269 -0.01990 -0.03954 377 ALA   A N    
1587 C  CA   . ALA   A 225 ? 0.32502 0.47890 0.47957 -0.05889 -0.02940 -0.02584 377 ALA   A CA   
1588 C  C    . ALA   A 225 ? 0.40040 0.53562 0.52405 -0.06379 -0.03069 -0.01653 377 ALA   A C    
1589 O  O    . ALA   A 225 ? 0.38420 0.51215 0.51436 -0.05864 -0.03589 -0.00758 377 ALA   A O    
1590 C  CB   . ALA   A 225 ? 0.41345 0.59036 0.58606 -0.06264 -0.03527 -0.01925 377 ALA   A CB   
1591 N  N    . LYS   A 226 ? 0.38017 0.50807 0.47168 -0.07394 -0.02592 -0.01887 378 LYS   A N    
1592 C  CA   . LYS   A 226 ? 0.30821 0.41899 0.37179 -0.07807 -0.02628 -0.01328 378 LYS   A CA   
1593 C  C    . LYS   A 226 ? 0.42477 0.51542 0.47974 -0.07090 -0.02296 -0.01610 378 LYS   A C    
1594 O  O    . LYS   A 226 ? 0.37483 0.45572 0.42062 -0.06934 -0.02543 -0.00959 378 LYS   A O    
1595 C  CB   . LYS   A 226 ? 0.30657 0.41253 0.34233 -0.09029 -0.02207 -0.01704 378 LYS   A CB   
1596 C  CG   . LYS   A 226 ? 0.37539 0.50178 0.41663 -0.09928 -0.02601 -0.01394 378 LYS   A CG   
1597 C  CD   . LYS   A 226 ? 0.41433 0.53292 0.42851 -0.11232 -0.02223 -0.01834 378 LYS   A CD   
1598 C  CE   . LYS   A 226 ? 0.58741 0.72834 0.60750 -0.12233 -0.02639 -0.01624 378 LYS   A CE   
1599 N  NZ   . LYS   A 226 ? 0.48962 0.62507 0.49135 -0.13534 -0.02149 -0.02294 378 LYS   A NZ   
1600 N  N    . MET   A 227 ? 0.36894 0.45624 0.42682 -0.06696 -0.01740 -0.02587 379 MET   A N    
1601 C  CA   . MET   A 227 ? 0.37054 0.44147 0.42125 -0.06040 -0.01478 -0.02881 379 MET   A CA   
1602 C  C    . MET   A 227 ? 0.36240 0.43484 0.43922 -0.05063 -0.02014 -0.02496 379 MET   A C    
1603 O  O    . MET   A 227 ? 0.39227 0.45189 0.46209 -0.04716 -0.02127 -0.02073 379 MET   A O    
1604 C  CB   . MET   A 227 ? 0.33195 0.40350 0.37795 -0.06025 -0.00783 -0.04001 379 MET   A CB   
1605 C  CG   . MET   A 227 ? 0.29852 0.36515 0.31780 -0.07075 -0.00284 -0.04102 379 MET   A CG   
1606 S  SD   . MET   A 227 ? 0.39125 0.46497 0.40486 -0.07266 0.00482  -0.05093 379 MET   A SD   
1607 C  CE   . MET   A 227 ? 0.34091 0.39692 0.34503 -0.06431 0.00550  -0.05173 379 MET   A CE   
1608 N  N    . ILE   A 228 ? 0.37230 0.46044 0.48156 -0.04618 -0.02372 -0.02614 380 ILE   A N    
1609 C  CA   . ILE   A 228 ? 0.48722 0.57547 0.62613 -0.03742 -0.02998 -0.02101 380 ILE   A CA   
1610 C  C    . ILE   A 228 ? 0.52696 0.61370 0.66253 -0.03988 -0.03700 -0.00381 380 ILE   A C    
1611 O  O    . ILE   A 228 ? 0.53681 0.61697 0.68322 -0.03510 -0.04103 0.00343  380 ILE   A O    
1612 C  CB   . ILE   A 228 ? 0.56004 0.66540 0.73831 -0.03178 -0.03282 -0.02627 380 ILE   A CB   
1613 C  CG1  . ILE   A 228 ? 0.51938 0.63131 0.69920 -0.03034 -0.02475 -0.04528 380 ILE   A CG1  
1614 C  CG2  . ILE   A 228 ? 0.59266 0.69512 0.80582 -0.02265 -0.03991 -0.02085 380 ILE   A CG2  
1615 C  CD1  . ILE   A 228 ? 0.58396 0.68270 0.75021 -0.02737 -0.01959 -0.05458 380 ILE   A CD1  
1616 N  N    . GLN   A 229 ? 0.46531 0.56021 0.58562 -0.04832 -0.03854 0.00279  381 GLN   A N    
1617 C  CA   . GLN   A 229 ? 0.42387 0.52141 0.53575 -0.05240 -0.04432 0.01773  381 GLN   A CA   
1618 C  C    . GLN   A 229 ? 0.37411 0.45469 0.45922 -0.05293 -0.04052 0.01733  381 GLN   A C    
1619 O  O    . GLN   A 229 ? 0.41599 0.49702 0.50370 -0.05184 -0.04480 0.02836  381 GLN   A O    
1620 C  CB   . GLN   A 229 ? 0.43500 0.54650 0.53349 -0.06244 -0.04595 0.02126  381 GLN   A CB   
1621 C  CG   . GLN   A 229 ? 0.44420 0.56329 0.53004 -0.06845 -0.05126 0.03462  381 GLN   A CG   
1622 C  CD   . GLN   A 229 ? 0.55007 0.68106 0.66472 -0.06394 -0.06079 0.05172  381 GLN   A CD   
1623 O  OE1  . GLN   A 229 ? 0.55258 0.68280 0.66070 -0.06462 -0.06336 0.06181  381 GLN   A OE1  
1624 N  NE2  . GLN   A 229 ? 0.57980 0.72278 0.72829 -0.05946 -0.06623 0.05557  381 GLN   A NE2  
1625 N  N    . LYS   A 230 ? 0.37181 0.43874 0.43242 -0.05474 -0.03270 0.00562  382 LYS   A N    
1626 C  CA   . LYS   A 230 ? 0.41987 0.47059 0.45821 -0.05374 -0.02908 0.00427  382 LYS   A CA   
1627 C  C    . LYS   A 230 ? 0.38700 0.43140 0.44167 -0.04495 -0.03037 0.00566  382 LYS   A C    
1628 O  O    . LYS   A 230 ? 0.38507 0.42353 0.43109 -0.04377 -0.03079 0.01070  382 LYS   A O    
1629 C  CB   . LYS   A 230 ? 0.44363 0.48071 0.45766 -0.05662 -0.02153 -0.00695 382 LYS   A CB   
1630 C  CG   . LYS   A 230 ? 0.48301 0.52189 0.47809 -0.06664 -0.02000 -0.00865 382 LYS   A CG   
1631 C  CD   . LYS   A 230 ? 0.57681 0.61898 0.55955 -0.07118 -0.02284 -0.00256 382 LYS   A CD   
1632 C  CE   . LYS   A 230 ? 0.67803 0.72816 0.64927 -0.08196 -0.02318 -0.00463 382 LYS   A CE   
1633 N  NZ   . LYS   A 230 ? 0.65749 0.72963 0.63727 -0.08606 -0.03012 0.00508  382 LYS   A NZ   
1634 N  N    . LEU   A 231 ? 0.34493 0.39196 0.42435 -0.03906 -0.03085 -0.00001 383 LEU   A N    
1635 C  CA   . LEU   A 231 ? 0.38233 0.42424 0.48178 -0.03139 -0.03297 0.00029  383 LEU   A CA   
1636 C  C    . LEU   A 231 ? 0.37112 0.41961 0.48984 -0.03084 -0.04108 0.01652  383 LEU   A C    
1637 O  O    . LEU   A 231 ? 0.33955 0.38194 0.46268 -0.02799 -0.04273 0.02165  383 LEU   A O    
1638 C  CB   . LEU   A 231 ? 0.36923 0.41528 0.49414 -0.02573 -0.03192 -0.01172 383 LEU   A CB   
1639 C  CG   . LEU   A 231 ? 0.45737 0.49997 0.56462 -0.02630 -0.02390 -0.02706 383 LEU   A CG   
1640 C  CD1  . LEU   A 231 ? 0.49033 0.54386 0.62463 -0.02161 -0.02272 -0.04030 383 LEU   A CD1  
1641 C  CD2  . LEU   A 231 ? 0.43026 0.45903 0.51883 -0.02428 -0.02072 -0.02962 383 LEU   A CD2  
1642 N  N    . ALA   A 232 ? 0.30565 0.36847 0.43676 -0.03419 -0.04663 0.02608  384 ALA   A N    
1643 C  CA   . ALA   A 232 ? 0.34207 0.41440 0.48914 -0.03546 -0.05517 0.04511  384 ALA   A CA   
1644 C  C    . ALA   A 232 ? 0.30556 0.37859 0.42285 -0.04165 -0.05398 0.05300  384 ALA   A C    
1645 O  O    . ALA   A 232 ? 0.36853 0.44328 0.49274 -0.04133 -0.05776 0.06500  384 ALA   A O    
1646 C  CB   . ALA   A 232 ? 0.35579 0.44618 0.52160 -0.03808 -0.06187 0.05424  384 ALA   A CB   
1647 N  N    . ASP   A 233 ? 0.27706 0.34970 0.36260 -0.04769 -0.04864 0.04577  385 ASP   A N    
1648 C  CA   . ASP   A 233 ? 0.37805 0.45157 0.43579 -0.05288 -0.04632 0.04877  385 ASP   A CA   
1649 C  C    . ASP   A 233 ? 0.39864 0.45776 0.45022 -0.04760 -0.04226 0.04484  385 ASP   A C    
1650 O  O    . ASP   A 233 ? 0.39012 0.45449 0.43326 -0.04962 -0.04282 0.05240  385 ASP   A O    
1651 C  CB   . ASP   A 233 ? 0.30181 0.37272 0.33012 -0.05927 -0.04070 0.03766  385 ASP   A CB   
1652 C  CG   . ASP   A 233 ? 0.41587 0.50270 0.44894 -0.06567 -0.04456 0.04055  385 ASP   A CG   
1653 O  OD1  . ASP   A 233 ? 0.38951 0.47248 0.40451 -0.07080 -0.04016 0.03008  385 ASP   A OD1  
1654 O  OD2  . ASP   A 233 ? 0.38272 0.48619 0.43877 -0.06590 -0.05243 0.05404  385 ASP   A OD2  
1655 N  N    . LEU   A 234 ? 0.33181 0.37575 0.38749 -0.04131 -0.03813 0.03292  386 LEU   A N    
1656 C  CA   . LEU   A 234 ? 0.37121 0.40282 0.42153 -0.03628 -0.03464 0.02852  386 LEU   A CA   
1657 C  C    . LEU   A 234 ? 0.40933 0.44545 0.48442 -0.03337 -0.04029 0.04013  386 LEU   A C    
1658 O  O    . LEU   A 234 ? 0.38530 0.41942 0.45322 -0.03266 -0.03903 0.04319  386 LEU   A O    
1659 C  CB   . LEU   A 234 ? 0.37484 0.39368 0.42458 -0.03135 -0.02982 0.01387  386 LEU   A CB   
1660 C  CG   . LEU   A 234 ? 0.38665 0.39667 0.40771 -0.03430 -0.02336 0.00391  386 LEU   A CG   
1661 C  CD1  . LEU   A 234 ? 0.39994 0.40501 0.42441 -0.03169 -0.01999 -0.00736 386 LEU   A CD1  
1662 C  CD2  . LEU   A 234 ? 0.47501 0.47533 0.47468 -0.03317 -0.01965 0.00246  386 LEU   A CD2  
1663 N  N    . ARG   A 235 ? 0.29883 0.34106 0.40547 -0.03167 -0.04671 0.04677  387 ARG   A N    
1664 C  CA   . ARG   A 235 ? 0.43155 0.47735 0.56553 -0.03009 -0.05337 0.06043  387 ARG   A CA   
1665 C  C    . ARG   A 235 ? 0.47396 0.53434 0.59785 -0.03701 -0.05668 0.07817  387 ARG   A C    
1666 O  O    . ARG   A 235 ? 0.39551 0.45725 0.52372 -0.03744 -0.05801 0.08673  387 ARG   A O    
1667 C  CB   . ARG   A 235 ? 0.35939 0.40896 0.53213 -0.02693 -0.06051 0.06501  387 ARG   A CB   
1668 C  CG   . ARG   A 235 ? 0.41856 0.45907 0.60377 -0.02048 -0.05693 0.04573  387 ARG   A CG   
1669 C  CD   . ARG   A 235 ? 0.40112 0.42891 0.59074 -0.01539 -0.05364 0.03438  387 ARG   A CD   
1670 N  NE   . ARG   A 235 ? 0.51212 0.53673 0.72205 -0.00959 -0.05193 0.01706  387 ARG   A NE   
1671 C  CZ   . ARG   A 235 ? 0.45595 0.47899 0.70588 -0.00457 -0.05702 0.01492  387 ARG   A CZ   
1672 N  NH1  . ARG   A 235 ? 0.40879 0.43100 0.68346 -0.00502 -0.06482 0.03159  387 ARG   A NH1  
1673 N  NH2  . ARG   A 235 ? 0.47058 0.49384 0.73689 0.00048  -0.05424 -0.00430 387 ARG   A NH2  
1674 N  N    . SER   A 236 ? 0.42056 0.49469 0.53079 -0.04333 -0.05795 0.08347  388 SER   A N    
1675 C  CA   . SER   A 236 ? 0.46933 0.56235 0.56638 -0.05118 -0.06045 0.09841  388 SER   A CA   
1676 C  C    . SER   A 236 ? 0.41995 0.50943 0.48699 -0.05216 -0.05260 0.08982  388 SER   A C    
1677 O  O    . SER   A 236 ? 0.37823 0.47921 0.44342 -0.05533 -0.05367 0.10076  388 SER   A O    
1678 C  CB   . SER   A 236 ? 0.45629 0.56608 0.54307 -0.05818 -0.06298 0.10217  388 SER   A CB   
1679 O  OG   . SER   A 236 ? 0.55181 0.67670 0.60976 -0.06596 -0.06026 0.10395  388 SER   A OG   
1680 N  N    . LEU   A 237 ? 0.36185 0.43658 0.40677 -0.04955 -0.04482 0.07088  389 LEU   A N    
1681 C  CA   . LEU   A 237 ? 0.40720 0.47650 0.42728 -0.04879 -0.03761 0.06158  389 LEU   A CA   
1682 C  C    . LEU   A 237 ? 0.33952 0.40038 0.37123 -0.04281 -0.03688 0.06248  389 LEU   A C    
1683 O  O    . LEU   A 237 ? 0.38384 0.45053 0.40478 -0.04350 -0.03397 0.06381  389 LEU   A O    
1684 C  CB   . LEU   A 237 ? 0.47097 0.52393 0.46985 -0.04699 -0.03081 0.04327  389 LEU   A CB   
1685 C  CG   . LEU   A 237 ? 0.53926 0.60007 0.52178 -0.05431 -0.03018 0.03960  389 LEU   A CG   
1686 C  CD1  . LEU   A 237 ? 0.42408 0.46597 0.39361 -0.05272 -0.02487 0.02406  389 LEU   A CD1  
1687 C  CD2  . LEU   A 237 ? 0.50362 0.57936 0.46629 -0.06012 -0.02797 0.03988  389 LEU   A CD2  
1688 N  N    . ASN   A 238 ? 0.37301 0.42196 0.42747 -0.03717 -0.03929 0.06034  390 ASN   A N    
1689 C  CA   . ASN   A 238 ? 0.39762 0.43994 0.46677 -0.03245 -0.03970 0.06098  390 ASN   A CA   
1690 C  C    . ASN   A 238 ? 0.44090 0.49891 0.52462 -0.03698 -0.04507 0.08002  390 ASN   A C    
1691 O  O    . ASN   A 238 ? 0.40925 0.47011 0.48864 -0.03683 -0.04284 0.08189  390 ASN   A O    
1692 C  CB   . ASN   A 238 ? 0.31747 0.34796 0.41173 -0.02685 -0.04214 0.05420  390 ASN   A CB   
1693 C  CG   . ASN   A 238 ? 0.39392 0.41597 0.50052 -0.02202 -0.04164 0.04954  390 ASN   A CG   
1694 O  OD1  . ASN   A 238 ? 0.41323 0.44048 0.51956 -0.02349 -0.04200 0.05731  390 ASN   A OD1  
1695 N  ND2  . ASN   A 238 ? 0.32911 0.34080 0.44713 -0.01687 -0.04078 0.03622  390 ASN   A ND2  
1696 N  N    . GLU   A 239 ? 0.34281 0.41288 0.44484 -0.04148 -0.05252 0.09563  391 GLU   A N    
1697 C  CA   . GLU   A 239 ? 0.42064 0.50713 0.53915 -0.04705 -0.05888 0.11751  391 GLU   A CA   
1698 C  C    . GLU   A 239 ? 0.47462 0.58045 0.56581 -0.05362 -0.05481 0.12237  391 GLU   A C    
1699 O  O    . GLU   A 239 ? 0.43799 0.55391 0.53424 -0.05650 -0.05548 0.13294  391 GLU   A O    
1700 C  CB   . GLU   A 239 ? 0.42186 0.51901 0.56448 -0.05070 -0.06838 0.13478  391 GLU   A CB   
1701 C  CG   . GLU   A 239 ? 0.66911 0.75258 0.85300 -0.04506 -0.07503 0.13755  391 GLU   A CG   
1702 C  CD   . GLU   A 239 ? 0.94207 1.03531 1.15187 -0.04712 -0.08463 0.15360  391 GLU   A CD   
1703 O  OE1  . GLU   A 239 ? 1.02789 1.13768 1.25174 -0.05364 -0.09248 0.17839  391 GLU   A OE1  
1704 O  OE2  . GLU   A 239 ? 1.03106 1.11724 1.24803 -0.04245 -0.08458 0.14238  391 GLU   A OE2  
1705 N  N    . GLU   A 240 ? 0.41983 0.53239 0.48290 -0.05650 -0.05030 0.11361  392 GLU   A N    
1706 C  CA   . GLU   A 240 ? 0.51286 0.64624 0.55071 -0.06273 -0.04588 0.11474  392 GLU   A CA   
1707 C  C    . GLU   A 240 ? 0.50586 0.62985 0.52952 -0.05736 -0.03760 0.10038  392 GLU   A C    
1708 O  O    . GLU   A 240 ? 0.38049 0.52262 0.39695 -0.06103 -0.03517 0.10558  392 GLU   A O    
1709 C  CB   . GLU   A 240 ? 0.46644 0.60859 0.48050 -0.06743 -0.04350 0.10643  392 GLU   A CB   
1710 C  CG   . GLU   A 240 ? 0.59754 0.76568 0.58702 -0.07487 -0.03920 0.10571  392 GLU   A CG   
1711 C  CD   . GLU   A 240 ? 0.58236 0.78149 0.58226 -0.08348 -0.04513 0.13007  392 GLU   A CD   
1712 O  OE1  . GLU   A 240 ? 0.51105 0.72986 0.49736 -0.08733 -0.04045 0.12995  392 GLU   A OE1  
1713 O  OE2  . GLU   A 240 ? 0.58551 0.79063 0.60846 -0.08657 -0.05459 0.14989  392 GLU   A OE2  
1714 N  N    . HIS   A 241 ? 0.34158 0.43991 0.36147 -0.04894 -0.03331 0.08287  393 HIS   A N    
1715 C  CA   . HIS   A 241 ? 0.45256 0.54200 0.46218 -0.04301 -0.02669 0.07089  393 HIS   A CA   
1716 C  C    . HIS   A 241 ? 0.34882 0.44138 0.37943 -0.04188 -0.02952 0.08113  393 HIS   A C    
1717 O  O    . HIS   A 241 ? 0.37281 0.47441 0.39647 -0.04143 -0.02544 0.07991  393 HIS   A O    
1718 C  CB   . HIS   A 241 ? 0.45238 0.51570 0.45494 -0.03514 -0.02285 0.05317  393 HIS   A CB   
1719 C  CG   . HIS   A 241 ? 0.44514 0.49924 0.44021 -0.02833 -0.01748 0.04274  393 HIS   A CG   
1720 N  ND1  . HIS   A 241 ? 0.40393 0.45010 0.41546 -0.02343 -0.01913 0.04324  393 HIS   A ND1  
1721 C  CD2  . HIS   A 241 ? 0.37112 0.42376 0.34605 -0.02547 -0.01096 0.03141  393 HIS   A CD2  
1722 C  CE1  . HIS   A 241 ? 0.44416 0.48569 0.44486 -0.01795 -0.01413 0.03395  393 HIS   A CE1  
1723 N  NE2  . HIS   A 241 ? 0.43842 0.48295 0.41797 -0.01852 -0.00916 0.02687  393 HIS   A NE2  
1724 N  N    . SER   A 242 ? 0.34699 0.43279 0.40539 -0.04152 -0.03652 0.09050  394 SER   A N    
1725 C  CA   . SER   A 242 ? 0.40478 0.49273 0.48677 -0.04177 -0.04014 0.10069  394 SER   A CA   
1726 C  C    . SER   A 242 ? 0.49153 0.60667 0.57449 -0.05071 -0.04206 0.11973  394 SER   A C    
1727 O  O    . SER   A 242 ? 0.38648 0.50920 0.47433 -0.05165 -0.04066 0.12376  394 SER   A O    
1728 C  CB   . SER   A 242 ? 0.50072 0.57623 0.61573 -0.04012 -0.04784 0.10613  394 SER   A CB   
1729 O  OG   . SER   A 242 ? 0.60943 0.66400 0.72318 -0.03237 -0.04519 0.08716  394 SER   A OG   
1730 N  N    A LYS   A 243 ? 0.43000 0.56299 0.50844 -0.05815 -0.04544 0.13226  395 LYS   A N    
1731 N  N    B LYS   A 243 ? 0.43294 0.56585 0.51155 -0.05814 -0.04549 0.13231  395 LYS   A N    
1732 C  CA   A LYS   A 243 ? 0.41117 0.57538 0.48813 -0.06825 -0.04733 0.15168  395 LYS   A CA   
1733 C  CA   B LYS   A 243 ? 0.42338 0.58760 0.50021 -0.06826 -0.04733 0.15164  395 LYS   A CA   
1734 C  C    A LYS   A 243 ? 0.43913 0.61846 0.48887 -0.06867 -0.03780 0.14043  395 LYS   A C    
1735 C  C    B LYS   A 243 ? 0.43315 0.61233 0.48294 -0.06863 -0.03780 0.14037  395 LYS   A C    
1736 O  O    A LYS   A 243 ? 0.43360 0.63083 0.48761 -0.07282 -0.03675 0.14984  395 LYS   A O    
1737 O  O    B LYS   A 243 ? 0.43470 0.63147 0.48897 -0.07269 -0.03678 0.14974  395 LYS   A O    
1738 C  CB   A LYS   A 243 ? 0.47733 0.66027 0.55120 -0.07624 -0.05276 0.16550  395 LYS   A CB   
1739 C  CB   B LYS   A 243 ? 0.47378 0.65659 0.54680 -0.07615 -0.05257 0.16490  395 LYS   A CB   
1740 C  CG   A LYS   A 243 ? 0.51171 0.69433 0.62038 -0.07955 -0.06452 0.18869  395 LYS   A CG   
1741 C  CG   B LYS   A 243 ? 0.50959 0.69615 0.61649 -0.08075 -0.06438 0.19035  395 LYS   A CG   
1742 C  CD   A LYS   A 243 ? 0.52333 0.73020 0.62746 -0.08821 -0.07040 0.20469  395 LYS   A CD   
1743 C  CD   B LYS   A 243 ? 0.52518 0.73930 0.62559 -0.09038 -0.06983 0.20726  395 LYS   A CD   
1744 C  CE   A LYS   A 243 ? 0.52084 0.71028 0.63551 -0.08307 -0.07469 0.19886  395 LYS   A CE   
1745 C  CE   B LYS   A 243 ? 0.53091 0.77968 0.60229 -0.09954 -0.06428 0.20983  395 LYS   A CE   
1746 N  NZ   A LYS   A 243 ? 0.58669 0.79092 0.72748 -0.08909 -0.08689 0.22581  395 LYS   A NZ   
1747 N  NZ   B LYS   A 243 ? 0.58550 0.86970 0.66099 -0.11224 -0.07258 0.23759  395 LYS   A NZ   
1748 N  N    . GLN   A 244 ? 0.37741 0.55010 0.40099 -0.06443 -0.03076 0.11987  396 GLN   A N    
1749 C  CA   . GLN   A 244 ? 0.31876 0.50471 0.31925 -0.06353 -0.02162 0.10656  396 GLN   A CA   
1750 C  C    . GLN   A 244 ? 0.41590 0.58724 0.42185 -0.05487 -0.01743 0.09660  396 GLN   A C    
1751 O  O    . GLN   A 244 ? 0.41969 0.60936 0.41968 -0.05566 -0.01232 0.09494  396 GLN   A O    
1752 C  CB   . GLN   A 244 ? 0.32293 0.50257 0.29830 -0.06137 -0.01621 0.08715  396 GLN   A CB   
1753 C  CG   . GLN   A 244 ? 0.36584 0.56173 0.33542 -0.07048 -0.02073 0.09587  396 GLN   A CG   
1754 C  CD   . GLN   A 244 ? 0.44391 0.64155 0.38730 -0.07112 -0.01460 0.07623  396 GLN   A CD   
1755 O  OE1  . GLN   A 244 ? 0.45355 0.64216 0.38367 -0.06495 -0.00675 0.05693  396 GLN   A OE1  
1756 N  NE2  . GLN   A 244 ? 0.55180 0.76111 0.48964 -0.07866 -0.01867 0.08103  396 GLN   A NE2  
1757 N  N    . TYR   A 245 ? 0.39179 0.53330 0.40939 -0.04689 -0.01950 0.08958  397 TYR   A N    
1758 C  CA   . TYR   A 245 ? 0.46949 0.59948 0.49374 -0.03943 -0.01684 0.08153  397 TYR   A CA   
1759 C  C    . TYR   A 245 ? 0.49525 0.64115 0.54072 -0.04472 -0.02052 0.09830  397 TYR   A C    
1760 O  O    . TYR   A 245 ? 0.42621 0.58253 0.47010 -0.04308 -0.01625 0.09525  397 TYR   A O    
1761 C  CB   . TYR   A 245 ? 0.42773 0.52730 0.46051 -0.03163 -0.01906 0.07163  397 TYR   A CB   
1762 C  CG   . TYR   A 245 ? 0.35811 0.44858 0.39987 -0.02506 -0.01787 0.06494  397 TYR   A CG   
1763 C  CD1  . TYR   A 245 ? 0.35945 0.44306 0.38492 -0.01727 -0.01166 0.04959  397 TYR   A CD1  
1764 C  CD2  . TYR   A 245 ? 0.37930 0.46864 0.44763 -0.02690 -0.02354 0.07417  397 TYR   A CD2  
1765 C  CE1  . TYR   A 245 ? 0.43486 0.51314 0.46860 -0.01151 -0.01132 0.04444  397 TYR   A CE1  
1766 C  CE2  . TYR   A 245 ? 0.43976 0.52335 0.51615 -0.02186 -0.02279 0.06723  397 TYR   A CE2  
1767 C  CZ   . TYR   A 245 ? 0.46697 0.54628 0.52516 -0.01420 -0.01676 0.05280  397 TYR   A CZ   
1768 O  OH   . TYR   A 245 ? 0.50045 0.57668 0.56683 -0.00935 -0.01677 0.04682  397 TYR   A OH   
1769 N  N    . ARG   A 246 ? 0.42349 0.57123 0.49140 -0.05111 -0.02885 0.11657  398 ARG   A N    
1770 C  CA   . ARG   A 246 ? 0.43036 0.59231 0.52166 -0.05781 -0.03348 0.13528  398 ARG   A CA   
1771 C  C    . ARG   A 246 ? 0.53086 0.72809 0.60913 -0.06586 -0.02922 0.14460  398 ARG   A C    
1772 O  O    . ARG   A 246 ? 0.51519 0.72558 0.60241 -0.06838 -0.02791 0.15025  398 ARG   A O    
1773 C  CB   . ARG   A 246 ? 0.54084 0.69906 0.65958 -0.06362 -0.04386 0.15486  398 ARG   A CB   
1774 C  CG   . ARG   A 246 ? 0.67803 0.81295 0.82865 -0.05968 -0.04965 0.15416  398 ARG   A CG   
1775 C  CD   . ARG   A 246 ? 0.81427 0.93455 0.98678 -0.05939 -0.05782 0.16060  398 ARG   A CD   
1776 N  NE   . ARG   A 246 ? 0.82050 0.96051 1.00456 -0.06945 -0.06492 0.18701  398 ARG   A NE   
1777 C  CZ   . ARG   A 246 ? 0.95317 1.09272 1.14095 -0.07050 -0.06994 0.19388  398 ARG   A CZ   
1778 N  NH1  . ARG   A 246 ? 0.93598 1.05622 1.11685 -0.06238 -0.06795 0.17534  398 ARG   A NH1  
1779 N  NH2  . ARG   A 246 ? 0.96186 1.12246 1.16076 -0.08022 -0.07725 0.22040  398 ARG   A NH2  
1780 N  N    . SER   A 247 ? 0.45038 0.66586 0.50744 -0.07054 -0.02674 0.14519  399 SER   A N    
1781 C  CA   . SER   A 247 ? 0.56642 0.82014 0.60881 -0.07870 -0.02175 0.15120  399 SER   A CA   
1782 C  C    . SER   A 247 ? 0.48240 0.73910 0.50805 -0.07098 -0.01131 0.12938  399 SER   A C    
1783 O  O    . SER   A 247 ? 0.50495 0.78736 0.53196 -0.07486 -0.00754 0.13398  399 SER   A O    
1784 C  CB   . SER   A 247 ? 0.62633 0.89994 0.64983 -0.08583 -0.02190 0.15441  399 SER   A CB   
1785 O  OG   . SER   A 247 ? 0.82895 1.14142 0.83403 -0.09284 -0.01520 0.15380  399 SER   A OG   
1786 N  N    . LEU   A 248 ? 0.44624 0.67778 0.45766 -0.06010 -0.00679 0.10630  400 LEU   A N    
1787 C  CA   . LEU   A 248 ? 0.47065 0.70279 0.46882 -0.05146 0.00228  0.08577  400 LEU   A CA   
1788 C  C    . LEU   A 248 ? 0.48533 0.71042 0.50094 -0.04627 0.00190  0.08650  400 LEU   A C    
1789 O  O    . LEU   A 248 ? 0.54351 0.78962 0.55764 -0.04555 0.00752  0.08295  400 LEU   A O    
1790 C  CB   . LEU   A 248 ? 0.46470 0.66867 0.44711 -0.04168 0.00558  0.06418  400 LEU   A CB   
1791 C  CG   . LEU   A 248 ? 0.67075 0.88340 0.63259 -0.04590 0.00820  0.05678  400 LEU   A CG   
1792 C  CD1  . LEU   A 248 ? 0.59857 0.77814 0.54998 -0.03704 0.00989  0.03834  400 LEU   A CD1  
1793 C  CD2  . LEU   A 248 ? 0.77030 1.01739 0.71772 -0.04934 0.01617  0.04883  400 LEU   A CD2  
1794 N  N    . SER   A 249 ? 0.56166 0.75954 0.59483 -0.04292 -0.00462 0.09002  401 SER   A N    
1795 C  CA   . SER   A 249 ? 0.54178 0.73241 0.59199 -0.03851 -0.00575 0.08907  401 SER   A CA   
1796 C  C    . SER   A 249 ? 0.54945 0.76454 0.61936 -0.04875 -0.00897 0.10906  401 SER   A C    
1797 O  O    . SER   A 249 ? 0.52694 0.74279 0.61035 -0.04661 -0.00901 0.10811  401 SER   A O    
1798 C  CB   . SER   A 249 ? 0.43065 0.58798 0.49374 -0.03296 -0.01162 0.08480  401 SER   A CB   
1799 O  OG   . SER   A 249 ? 0.52182 0.67659 0.60728 -0.04067 -0.01991 0.10186  401 SER   A OG   
1800 N  N    . PHE   A 250 ? 0.56058 0.79685 0.63308 -0.06047 -0.01215 0.12813  402 PHE   A N    
1801 C  CA   . PHE   A 250 ? 0.58889 0.85181 0.67942 -0.07184 -0.01508 0.14975  402 PHE   A CA   
1802 C  C    . PHE   A 250 ? 0.60190 0.89496 0.68246 -0.07201 -0.00632 0.14357  402 PHE   A C    
1803 O  O    . PHE   A 250 ? 0.52173 0.83209 0.61940 -0.07845 -0.00752 0.15600  402 PHE   A O    
1804 C  CB   . PHE   A 250 ? 0.54970 0.83312 0.64219 -0.08478 -0.02031 0.17293  402 PHE   A CB   
1805 C  CG   . PHE   A 250 ? 0.65014 0.95958 0.76409 -0.09814 -0.02500 0.19977  402 PHE   A CG   
1806 C  CD1  . PHE   A 250 ? 0.73291 1.08624 0.83487 -0.10799 -0.01974 0.20927  402 PHE   A CD1  
1807 C  CD2  . PHE   A 250 ? 0.78385 1.07498 0.93126 -0.10144 -0.03462 0.21508  402 PHE   A CD2  
1808 C  CE1  . PHE   A 250 ? 0.82518 1.20441 0.94709 -0.12174 -0.02421 0.23623  402 PHE   A CE1  
1809 C  CE2  . PHE   A 250 ? 0.85213 1.16556 1.02180 -0.11469 -0.03961 0.24139  402 PHE   A CE2  
1810 C  CZ   . PHE   A 250 ? 0.87089 1.22877 1.02728 -0.12527 -0.03451 0.25335  402 PHE   A CZ   
1811 N  N    . GLN   A 251 ? 0.58856 0.88889 0.64376 -0.06523 0.00247  0.12410  403 GLN   A N    
1812 C  CA   . GLN   A 251 ? 0.51165 0.83870 0.55920 -0.06254 0.01154  0.11352  403 GLN   A CA   
1813 C  C    . GLN   A 251 ? 0.46864 0.77288 0.52397 -0.04962 0.01286  0.09795  403 GLN   A C    
1814 O  O    . GLN   A 251 ? 0.46484 0.73837 0.51172 -0.03838 0.01314  0.08162  403 GLN   A O    
1815 C  CB   . GLN   A 251 ? 0.62333 0.96617 0.64412 -0.05963 0.02022  0.09645  403 GLN   A CB   
1816 C  CG   . GLN   A 251 ? 0.86956 1.25536 0.88079 -0.07395 0.02218  0.10974  403 GLN   A CG   
1817 C  CD   . GLN   A 251 ? 0.95888 1.33710 0.96284 -0.08065 0.01601  0.11966  403 GLN   A CD   
1818 O  OE1  . GLN   A 251 ? 1.03191 1.41563 1.04987 -0.09147 0.00754  0.14514  403 GLN   A OE1  
1819 N  NE2  . GLN   A 251 ? 1.01665 1.38200 1.00070 -0.07428 0.01973  0.09999  403 GLN   A NE2  
1820 N  N    . PRO   A 252 ? 0.41311 0.73269 0.48472 -0.05151 0.01320  0.10344  404 PRO   A N    
1821 C  CA   . PRO   A 252 ? 0.36091 0.66323 0.43889 -0.03917 0.01431  0.08823  404 PRO   A CA   
1822 C  C    . PRO   A 252 ? 0.39638 0.69735 0.45553 -0.02587 0.02271  0.06479  404 PRO   A C    
1823 O  O    . PRO   A 252 ? 0.48663 0.76138 0.54571 -0.01382 0.02184  0.05148  404 PRO   A O    
1824 C  CB   . PRO   A 252 ? 0.40665 0.73667 0.50403 -0.04633 0.01429  0.09974  404 PRO   A CB   
1825 C  CG   . PRO   A 252 ? 0.44727 0.79354 0.55561 -0.06302 0.00901  0.12535  404 PRO   A CG   
1826 C  CD   . PRO   A 252 ? 0.43275 0.78538 0.51971 -0.06602 0.01133  0.12587  404 PRO   A CD   
1827 N  N    . GLU   A 253 ? 0.44202 0.77146 0.48629 -0.02799 0.03057  0.05925  405 GLU   A N    
1828 C  CA   . GLU   A 253 ? 0.47154 0.79800 0.50080 -0.01520 0.03843  0.03541  405 GLU   A CA   
1829 C  C    . GLU   A 253 ? 0.53333 0.81992 0.55061 -0.00743 0.03576  0.02487  405 GLU   A C    
1830 O  O    . GLU   A 253 ? 0.56920 0.83784 0.58170 0.00569  0.03868  0.00742  405 GLU   A O    
1831 C  CB   . GLU   A 253 ? 0.57783 0.94387 0.59391 -0.02081 0.04718  0.03008  405 GLU   A CB   
1832 C  CG   . GLU   A 253 ? 0.71980 1.10014 0.72669 -0.03578 0.04450  0.04542  405 GLU   A CG   
1833 C  CD   . GLU   A 253 ? 0.81239 1.22684 0.83193 -0.05132 0.04179  0.07048  405 GLU   A CD   
1834 O  OE1  . GLU   A 253 ? 0.84174 1.24392 0.88128 -0.05346 0.03502  0.08466  405 GLU   A OE1  
1835 O  OE2  . GLU   A 253 ? 0.95384 1.40844 0.96385 -0.06221 0.04619  0.07618  405 GLU   A OE2  
1836 N  N    . ASN   A 254 ? 0.43463 0.70786 0.44857 -0.01551 0.02993  0.03616  406 ASN   A N    
1837 C  CA   . ASN   A 254 ? 0.43878 0.67567 0.44294 -0.00945 0.02708  0.02763  406 ASN   A CA   
1838 C  C    . ASN   A 254 ? 0.39292 0.59876 0.40965 -0.00373 0.02032  0.02968  406 ASN   A C    
1839 O  O    . ASN   A 254 ? 0.37746 0.55655 0.38775 0.00613  0.02022  0.01743  406 ASN   A O    
1840 C  CB   . ASN   A 254 ? 0.46208 0.70030 0.45837 -0.02007 0.02373  0.03782  406 ASN   A CB   
1841 C  CG   . ASN   A 254 ? 0.48028 0.74680 0.45933 -0.02506 0.03052  0.03113  406 ASN   A CG   
1842 O  OD1  . ASN   A 254 ? 0.57617 0.85164 0.54692 -0.01783 0.03834  0.01298  406 ASN   A OD1  
1843 N  ND2  . ASN   A 254 ? 0.53381 0.81605 0.50871 -0.03743 0.02729  0.04524  406 ASN   A ND2  
1844 N  N    . SER   A 255 ? 0.38390 0.59419 0.41933 -0.01056 0.01447  0.04504  407 SER   A N    
1845 C  CA   . SER   A 255 ? 0.44037 0.62547 0.48917 -0.00618 0.00820  0.04494  407 SER   A CA   
1846 C  C    . SER   A 255 ? 0.36372 0.54416 0.41293 0.00565  0.01078  0.03174  407 SER   A C    
1847 O  O    . SER   A 255 ? 0.35175 0.50890 0.40359 0.01190  0.00688  0.02621  407 SER   A O    
1848 C  CB   . SER   A 255 ? 0.55437 0.74812 0.62653 -0.01622 0.00186  0.06216  407 SER   A CB   
1849 O  OG   . SER   A 255 ? 0.70794 0.89031 0.78576 -0.02355 -0.00409 0.07316  407 SER   A OG   
1850 N  N    . MET   A 256 ? 0.41014 0.61414 0.45687 0.00884  0.01722  0.02643  408 MET   A N    
1851 C  CA   . MET   A 256 ? 0.49565 0.69782 0.54604 0.02077  0.01902  0.01526  408 MET   A CA   
1852 C  C    . MET   A 256 ? 0.53222 0.70788 0.56835 0.03223  0.02028  0.00134  408 MET   A C    
1853 O  O    . MET   A 256 ? 0.47929 0.64327 0.51955 0.04095  0.01800  -0.00372 408 MET   A O    
1854 C  CB   . MET   A 256 ? 0.41796 0.65402 0.47072 0.02220  0.02635  0.01148  408 MET   A CB   
1855 C  CG   . MET   A 256 ? 0.56405 0.82252 0.63580 0.01636  0.02435  0.02174  408 MET   A CG   
1856 S  SD   . MET   A 256 ? 0.65595 0.96024 0.73010 0.01576  0.03388  0.01825  408 MET   A SD   
1857 C  CE   . MET   A 256 ? 0.74169 1.03721 0.80172 0.03269  0.04118  -0.00529 408 MET   A CE   
1858 N  N    . LYS   A 257 ? 0.45874 0.62733 0.47939 0.03114  0.02345  -0.00361 409 LYS   A N    
1859 C  CA   . LYS   A 257 ? 0.48870 0.63177 0.49712 0.04062  0.02465  -0.01603 409 LYS   A CA   
1860 C  C    . LYS   A 257 ? 0.42033 0.53368 0.42478 0.03918  0.01841  -0.01249 409 LYS   A C    
1861 O  O    . LYS   A 257 ? 0.46908 0.56013 0.46410 0.04576  0.01853  -0.02040 409 LYS   A O    
1862 C  CB   . LYS   A 257 ? 0.57482 0.72484 0.56924 0.03952  0.03123  -0.02546 409 LYS   A CB   
1863 C  CG   . LYS   A 257 ? 0.68889 0.87549 0.68572 0.03801  0.03847  -0.02962 409 LYS   A CG   
1864 C  CD   . LYS   A 257 ? 0.80853 0.99458 0.80285 0.05027  0.04501  -0.04880 409 LYS   A CD   
1865 C  CE   . LYS   A 257 ? 0.96281 1.13953 0.97033 0.06311  0.04289  -0.05159 409 LYS   A CE   
1866 N  NZ   . LYS   A 257 ? 0.98036 1.15182 0.98959 0.07679  0.04800  -0.06961 409 LYS   A NZ   
1867 N  N    . LEU   A 258 ? 0.38620 0.49946 0.39914 0.03053  0.01308  -0.00106 410 LEU   A N    
1868 C  CA   . LEU   A 258 ? 0.36488 0.45369 0.37684 0.02948  0.00759  0.00053  410 LEU   A CA   
1869 C  C    . LEU   A 258 ? 0.43963 0.51895 0.45883 0.03639  0.00381  -0.00240 410 LEU   A C    
1870 O  O    . LEU   A 258 ? 0.36943 0.46066 0.39556 0.04185  0.00471  -0.00436 410 LEU   A O    
1871 C  CB   . LEU   A 258 ? 0.42610 0.51882 0.44806 0.01845  0.00317  0.01237  410 LEU   A CB   
1872 C  CG   . LEU   A 258 ? 0.50842 0.61541 0.52467 0.00989  0.00538  0.01900  410 LEU   A CG   
1873 C  CD1  . LEU   A 258 ? 0.33678 0.44461 0.36707 0.00013  -0.00079 0.03285  410 LEU   A CD1  
1874 C  CD2  . LEU   A 258 ? 0.45277 0.54777 0.44948 0.01218  0.00884  0.00988  410 LEU   A CD2  
1875 N  N    . THR   A 259 ? 0.46076 0.52130 0.47843 0.03588  -0.00049 -0.00302 411 THR   A N    
1876 C  CA   . THR   A 259 ? 0.45638 0.51116 0.47948 0.04065  -0.00460 -0.00576 411 THR   A CA   
1877 C  C    . THR   A 259 ? 0.38064 0.43990 0.42078 0.03365  -0.00982 -0.00158 411 THR   A C    
1878 O  O    . THR   A 259 ? 0.45762 0.51702 0.50446 0.02584  -0.01104 0.00391  411 THR   A O    
1879 C  CB   . THR   A 259 ? 0.47591 0.50960 0.48533 0.04468  -0.00555 -0.01066 411 THR   A CB   
1880 O  OG1  . THR   A 259 ? 0.56798 0.59231 0.57739 0.03772  -0.00784 -0.00934 411 THR   A OG1  
1881 C  CG2  . THR   A 259 ? 0.44596 0.47107 0.44092 0.04957  -0.00072 -0.01471 411 THR   A CG2  
1882 N  N    . PRO   A 260 ? 0.40798 0.47169 0.45743 0.03612  -0.01349 -0.00422 412 PRO   A N    
1883 C  CA   . PRO   A 260 ? 0.43812 0.50487 0.50623 0.02924  -0.01864 -0.00322 412 PRO   A CA   
1884 C  C    . PRO   A 260 ? 0.38163 0.43326 0.44929 0.02534  -0.02088 -0.00589 412 PRO   A C    
1885 O  O    . PRO   A 260 ? 0.42824 0.48024 0.51275 0.01838  -0.02374 -0.00254 412 PRO   A O    
1886 C  CB   . PRO   A 260 ? 0.39461 0.46869 0.46766 0.03367  -0.02186 -0.00868 412 PRO   A CB   
1887 C  CG   . PRO   A 260 ? 0.44457 0.52655 0.50892 0.04182  -0.01830 -0.00803 412 PRO   A CG   
1888 C  CD   . PRO   A 260 ? 0.37948 0.44845 0.42595 0.04492  -0.01352 -0.00803 412 PRO   A CD   
1889 N  N    . LEU   A 261 ? 0.35534 0.39430 0.40606 0.02955  -0.01984 -0.01132 413 LEU   A N    
1890 C  CA   . LEU   A 261 ? 0.43432 0.46185 0.48462 0.02589  -0.02125 -0.01476 413 LEU   A CA   
1891 C  C    . LEU   A 261 ? 0.33206 0.35558 0.38389 0.02085  -0.01979 -0.00822 413 LEU   A C    
1892 O  O    . LEU   A 261 ? 0.38059 0.40146 0.44663 0.01581  -0.02264 -0.00768 413 LEU   A O    
1893 C  CB   . LEU   A 261 ? 0.45861 0.47596 0.48919 0.03033  -0.01997 -0.01986 413 LEU   A CB   
1894 C  CG   . LEU   A 261 ? 0.53222 0.54163 0.56161 0.02669  -0.02091 -0.02509 413 LEU   A CG   
1895 C  CD1  . LEU   A 261 ? 0.44001 0.45716 0.48726 0.02371  -0.02498 -0.03286 413 LEU   A CD1  
1896 C  CD2  . LEU   A 261 ? 0.43754 0.43851 0.44582 0.02984  -0.01915 -0.02696 413 LEU   A CD2  
1897 N  N    . VAL   A 262 ? 0.31505 0.33961 0.35379 0.02218  -0.01565 -0.00374 414 VAL   A N    
1898 C  CA   . VAL   A 262 ? 0.29327 0.31830 0.33147 0.01661  -0.01454 0.00304  414 VAL   A CA   
1899 C  C    . VAL   A 262 ? 0.42024 0.45708 0.48063 0.00985  -0.01792 0.01250  414 VAL   A C    
1900 O  O    . VAL   A 262 ? 0.40112 0.43589 0.47180 0.00429  -0.02074 0.01835  414 VAL   A O    
1901 C  CB   . VAL   A 262 ? 0.41381 0.44176 0.43409 0.01900  -0.00914 0.00340  414 VAL   A CB   
1902 C  CG1  . VAL   A 262 ? 0.51572 0.55421 0.53778 0.01176  -0.00838 0.01210  414 VAL   A CG1  
1903 C  CG2  . VAL   A 262 ? 0.43621 0.44790 0.43773 0.02310  -0.00684 -0.00378 414 VAL   A CG2  
1904 N  N    . LEU   A 263 ? 0.40656 0.45644 0.47652 0.00999  -0.01817 0.01522  415 LEU   A N    
1905 C  CA   . LEU   A 263 ? 0.34294 0.40429 0.43594 0.00243  -0.02181 0.02597  415 LEU   A CA   
1906 C  C    . LEU   A 263 ? 0.38561 0.43765 0.50127 -0.00054 -0.02793 0.02370  415 LEU   A C    
1907 O  O    . LEU   A 263 ? 0.38974 0.44288 0.52521 -0.00724 -0.03201 0.03350  415 LEU   A O    
1908 C  CB   . LEU   A 263 ? 0.34793 0.42633 0.44673 0.00299  -0.02052 0.02815  415 LEU   A CB   
1909 C  CG   . LEU   A 263 ? 0.35589 0.44959 0.43929 0.00434  -0.01433 0.03132  415 LEU   A CG   
1910 C  CD1  . LEU   A 263 ? 0.43247 0.54246 0.52073 0.00763  -0.01246 0.02946  415 LEU   A CD1  
1911 C  CD2  . LEU   A 263 ? 0.35849 0.46521 0.44641 -0.00509 -0.01441 0.04543  415 LEU   A CD2  
1912 N  N    . GLU   A 264 ? 0.36067 0.40483 0.47510 0.00422  -0.02889 0.01071  416 GLU   A N    
1913 C  CA   . GLU   A 264 ? 0.43715 0.47418 0.57317 0.00183  -0.03392 0.00419  416 GLU   A CA   
1914 C  C    . GLU   A 264 ? 0.51387 0.53982 0.65128 0.00048  -0.03473 0.00431  416 GLU   A C    
1915 O  O    . GLU   A 264 ? 0.51809 0.54094 0.68094 -0.00382 -0.03935 0.00748  416 GLU   A O    
1916 C  CB   . GLU   A 264 ? 0.39670 0.43286 0.52734 0.00662  -0.03418 -0.01079 416 GLU   A CB   
1917 C  CG   . GLU   A 264 ? 0.54039 0.57440 0.69593 0.00371  -0.03906 -0.02114 416 GLU   A CG   
1918 C  CD   . GLU   A 264 ? 0.61343 0.65095 0.75983 0.00748  -0.03907 -0.03654 416 GLU   A CD   
1919 O  OE1  . GLU   A 264 ? 0.59141 0.62355 0.72606 0.00961  -0.03753 -0.04494 416 GLU   A OE1  
1920 O  OE2  . GLU   A 264 ? 0.58870 0.63679 0.73957 0.00765  -0.04078 -0.03961 416 GLU   A OE2  
1921 N  N    . VAL   A 265 ? 0.44841 0.46830 0.56089 0.00409  -0.03063 0.00105  417 VAL   A N    
1922 C  CA   . VAL   A 265 ? 0.47841 0.48953 0.59143 0.00296  -0.03117 -0.00042 417 VAL   A CA   
1923 C  C    . VAL   A 265 ? 0.50977 0.52410 0.62848 -0.00209 -0.03247 0.01446  417 VAL   A C    
1924 O  O    . VAL   A 265 ? 0.51737 0.52932 0.65813 -0.00542 -0.03695 0.01895  417 VAL   A O    
1925 C  CB   . VAL   A 265 ? 0.51506 0.51934 0.60034 0.00721  -0.02666 -0.00836 417 VAL   A CB   
1926 C  CG1  . VAL   A 265 ? 0.56723 0.56524 0.65174 0.00511  -0.02666 -0.00811 417 VAL   A CG1  
1927 C  CG2  . VAL   A 265 ? 0.43109 0.43497 0.51298 0.01085  -0.02662 -0.02133 417 VAL   A CG2  
1928 N  N    . PHE   A 266 ? 0.52311 0.54461 0.62323 -0.00275 -0.02884 0.02209  418 PHE   A N    
1929 C  CA   . PHE   A 266 ? 0.53474 0.56335 0.63533 -0.00838 -0.02975 0.03572  418 PHE   A CA   
1930 C  C    . PHE   A 266 ? 0.60774 0.64834 0.73198 -0.01478 -0.03427 0.05092  418 PHE   A C    
1931 O  O    . PHE   A 266 ? 0.60578 0.65189 0.74047 -0.02057 -0.03794 0.06457  418 PHE   A O    
1932 C  CB   . PHE   A 266 ? 0.57453 0.60880 0.64637 -0.00739 -0.02377 0.03554  418 PHE   A CB   
1933 C  CG   . PHE   A 266 ? 0.50491 0.52644 0.55601 -0.00350 -0.02039 0.02468  418 PHE   A CG   
1934 C  CD1  . PHE   A 266 ? 0.41177 0.43388 0.43875 -0.00154 -0.01500 0.02067  418 PHE   A CD1  
1935 C  CD2  . PHE   A 266 ? 0.57691 0.58679 0.63440 -0.00225 -0.02251 0.01794  418 PHE   A CD2  
1936 C  CE1  . PHE   A 266 ? 0.55028 0.55942 0.56040 0.00089  -0.01245 0.01200  418 PHE   A CE1  
1937 C  CE2  . PHE   A 266 ? 0.53113 0.53113 0.57003 -0.00008 -0.01940 0.00958  418 PHE   A CE2  
1938 C  CZ   . PHE   A 266 ? 0.52114 0.51966 0.53658 0.00115  -0.01469 0.00753  418 PHE   A CZ   
1939 N  N    . GLY   A 267 ? 0.60995 0.65595 0.74370 -0.01454 -0.03459 0.05024  419 GLY   A N    
1940 C  CA   . GLY   A 267 ? 0.58886 0.64546 0.74807 -0.02165 -0.03932 0.06495  419 GLY   A CA   
1941 C  C    . GLY   A 267 ? 0.69886 0.77449 0.84861 -0.02382 -0.03546 0.07133  419 GLY   A C    
1942 O  O    . GLY   A 267 ? 0.56685 0.64830 0.69065 -0.01960 -0.02902 0.06506  419 GLY   A O    
1943 N  N    . ASN   A 268 ? 0.79565 0.88133 0.96975 -0.03074 -0.03967 0.08382  420 ASN   A N    
1944 C  CA   . ASN   A 268 ? 0.86212 0.96992 1.03292 -0.03451 -0.03649 0.09160  420 ASN   A CA   
1945 C  C    . ASN   A 268 ? 0.79697 0.92546 0.96507 -0.04360 -0.03644 0.11157  420 ASN   A C    
1946 O  O    . ASN   A 268 ? 0.80208 0.94339 0.99194 -0.05302 -0.04089 0.12941  420 ASN   A O    
1947 C  CB   . ASN   A 268 ? 0.95977 1.06950 1.15910 -0.03840 -0.04107 0.09417  420 ASN   A CB   
1948 C  CG   . ASN   A 268 ? 1.10452 1.20805 1.29848 -0.03031 -0.03879 0.07501  420 ASN   A CG   
1949 O  OD1  . ASN   A 268 ? 1.16697 1.25362 1.37085 -0.02675 -0.04210 0.06271  420 ASN   A OD1  
1950 N  ND2  . ASN   A 268 ? 1.09898 1.21863 1.27796 -0.02739 -0.03324 0.07215  420 ASN   A ND2  
1951 N  N    . LYS   B 1   ? 0.93633 1.15702 1.40662 -0.06275 0.16535  -0.12824 625 LYS   C N    
1952 C  CA   . LYS   B 1   ? 0.97085 1.18854 1.43030 -0.05497 0.15595  -0.14595 625 LYS   C CA   
1953 C  C    . LYS   B 1   ? 0.93465 1.16333 1.37851 -0.04524 0.13867  -0.14775 625 LYS   C C    
1954 O  O    . LYS   B 1   ? 0.90536 1.13499 1.33447 -0.04683 0.13066  -0.12821 625 LYS   C O    
1955 C  CB   . LYS   B 1   ? 0.97853 1.16914 1.41055 -0.06191 0.15168  -0.13375 625 LYS   C CB   
1956 C  CG   . LYS   B 1   ? 0.90421 1.08812 1.31649 -0.05470 0.13860  -0.14610 625 LYS   C CG   
1957 C  CD   . LYS   B 1   ? 0.91064 1.08043 1.28327 -0.05580 0.12039  -0.12454 625 LYS   C CD   
1958 C  CE   . LYS   B 1   ? 0.91947 1.06252 1.26976 -0.06738 0.12135  -0.10240 625 LYS   C CE   
1959 N  NZ   . LYS   B 1   ? 0.84959 0.97598 1.16196 -0.06630 0.10384  -0.09216 625 LYS   C NZ   
1960 N  N    . ASN   B 2   ? 0.93173 1.16907 1.37949 -0.03510 0.13313  -0.17148 626 ASN   C N    
1961 C  CA   . ASN   B 2   ? 0.91031 1.15934 1.34571 -0.02493 0.11727  -0.17671 626 ASN   C CA   
1962 C  C    . ASN   B 2   ? 0.81274 1.04316 1.20939 -0.02474 0.10029  -0.16536 626 ASN   C C    
1963 O  O    . ASN   B 2   ? 0.80723 1.01969 1.19220 -0.02848 0.10082  -0.16578 626 ASN   C O    
1964 C  CB   . ASN   B 2   ? 0.94565 1.21443 1.40571 -0.01376 0.11987  -0.20868 626 ASN   C CB   
1965 C  CG   . ASN   B 2   ? 1.01015 1.30147 1.50591 -0.01165 0.13276  -0.21941 626 ASN   C CG   
1966 O  OD1  . ASN   B 2   ? 1.04554 1.34147 1.54430 -0.01600 0.13548  -0.20292 626 ASN   C OD1  
1967 N  ND2  . ASN   B 2   ? 1.01511 1.31921 1.53635 -0.00510 0.14022  -0.24647 626 ASN   C ND2  
1968 N  N    . HIS   B 3   ? 0.71880 0.95375 1.09548 -0.02027 0.08509  -0.15514 627 HIS   C N    
1969 C  CA   . HIS   B 3   ? 0.59211 0.81115 0.93087 -0.01955 0.06751  -0.14278 627 HIS   C CA   
1970 C  C    . HIS   B 3   ? 0.44631 0.68056 0.78064 -0.00690 0.05395  -0.15835 627 HIS   C C    
1971 O  O    . HIS   B 3   ? 0.44438 0.68455 0.76429 -0.00396 0.04235  -0.14663 627 HIS   C O    
1972 C  CB   . HIS   B 3   ? 0.63393 0.84077 0.94836 -0.02779 0.06122  -0.11061 627 HIS   C CB   
1973 C  CG   . HIS   B 3   ? 0.65543 0.84888 0.97538 -0.04025 0.07472  -0.09440 627 HIS   C CG   
1974 N  ND1  . HIS   B 3   ? 0.66485 0.86997 1.01249 -0.04413 0.08928  -0.09299 627 HIS   C ND1  
1975 C  CD2  . HIS   B 3   ? 0.70452 0.87391 1.00601 -0.04969 0.07597  -0.07909 627 HIS   C CD2  
1976 C  CE1  . HIS   B 3   ? 0.66929 0.85821 1.01531 -0.05542 0.09887  -0.07744 627 HIS   C CE1  
1977 N  NE2  . HIS   B 3   ? 0.64006 0.80714 0.95833 -0.05901 0.09109  -0.06880 627 HIS   C NE2  
1978 N  N    . PRO   B 4   ? 0.45808 0.69887 0.80430 0.00083  0.05492  -0.18472 628 PRO   C N    
1979 C  CA   . PRO   B 4   ? 0.45880 0.71566 0.80344 0.01324  0.04284  -0.20116 628 PRO   C CA   
1980 C  C    . PRO   B 4   ? 0.41849 0.66373 0.72513 0.01579  0.02307  -0.18887 628 PRO   C C    
1981 O  O    . PRO   B 4   ? 0.39069 0.64894 0.69116 0.02392  0.01146  -0.19174 628 PRO   C O    
1982 C  CB   . PRO   B 4   ? 0.45200 0.71486 0.81749 0.01917  0.05000  -0.23084 628 PRO   C CB   
1983 C  CG   . PRO   B 4   ? 0.36081 0.60306 0.72379 0.00984  0.05953  -0.22566 628 PRO   C CG   
1984 C  CD   . PRO   B 4   ? 0.48947 0.72441 0.85278 -0.00123 0.06760  -0.20129 628 PRO   C CD   
1985 N  N    . MET   B 5   ? 0.38551 0.60670 0.66642 0.00925  0.01876  -0.17554 629 MET   C N    
1986 C  CA   . MET   B 5   ? 0.43438 0.64397 0.67848 0.01151  -0.00017 -0.16344 629 MET   C CA   
1987 C  C    . MET   B 5   ? 0.46396 0.67137 0.68974 0.00722  -0.00800 -0.13624 629 MET   C C    
1988 O  O    . MET   B 5   ? 0.39667 0.60805 0.60297 0.01309  -0.02345 -0.13135 629 MET   C O    
1989 C  CB   . MET   B 5   ? 0.40736 0.59179 0.62978 0.00584  -0.00218 -0.15784 629 MET   C CB   
1990 C  CG   . MET   B 5   ? 0.52091 0.70668 0.75577 0.01159  0.00179  -0.18492 629 MET   C CG   
1991 S  SD   . MET   B 5   ? 0.54942 0.70534 0.76284 0.00355  0.00267  -0.17791 629 MET   C SD   
1992 C  CE   . MET   B 5   ? 0.61275 0.76631 0.85643 -0.00631 0.02587  -0.17817 629 MET   C CE   
1993 N  N    . LEU   B 6   ? 0.38987 0.59101 0.62165 -0.00300 0.00249  -0.11827 630 LEU   C N    
1994 C  CA   . LEU   B 6   ? 0.42859 0.62972 0.64711 -0.00717 -0.00315 -0.09314 630 LEU   C CA   
1995 C  C    . LEU   B 6   ? 0.37609 0.60283 0.61186 0.00116  -0.00500 -0.10186 630 LEU   C C    
1996 O  O    . LEU   B 6   ? 0.39977 0.62988 0.61704 0.00418  -0.01827 -0.08959 630 LEU   C O    
1997 C  CB   . LEU   B 6   ? 0.44310 0.63405 0.66904 -0.01957 0.01041  -0.07479 630 LEU   C CB   
1998 C  CG   . LEU   B 6   ? 0.66729 0.83502 0.86087 -0.02948 0.00349  -0.04415 630 LEU   C CG   
1999 C  CD1  . LEU   B 6   ? 0.55718 0.71982 0.76327 -0.04070 0.01784  -0.02759 630 LEU   C CD1  
2000 C  CD2  . LEU   B 6   ? 0.68212 0.85239 0.85065 -0.02578 -0.01376 -0.02903 630 LEU   C CD2  
2001 N  N    . MET   B 7   ? 0.55440 0.79938 0.82559 0.00503  0.00814  -0.12319 631 MET   C N    
2002 C  CA   . MET   B 7   ? 0.47500 0.74496 0.76485 0.01300  0.00752  -0.13289 631 MET   C CA   
2003 C  C    . MET   B 7   ? 0.43841 0.71720 0.71467 0.02459  -0.00887 -0.14486 631 MET   C C    
2004 O  O    . MET   B 7   ? 0.45539 0.74782 0.72921 0.02983  -0.01693 -0.14106 631 MET   C O    
2005 C  CB   . MET   B 7   ? 0.45354 0.74015 0.78381 0.01508  0.02492  -0.15542 631 MET   C CB   
2006 C  CG   . MET   B 7   ? 0.55806 0.86893 0.91087 0.02014  0.02830  -0.16059 631 MET   C CG   
2007 S  SD   . MET   B 7   ? 0.63369 0.94277 0.99153 0.00924  0.03746  -0.13336 631 MET   C SD   
2008 C  CE   . MET   B 7   ? 0.72523 1.03905 1.12215 0.00427  0.06121  -0.14829 631 MET   C CE   
2009 N  N    . ASN   B 8   ? 0.43584 0.70703 0.70311 0.02875  -0.01399 -0.15939 632 ASN   C N    
2010 C  CA   . ASN   B 8   ? 0.42250 0.70176 0.67713 0.03988  -0.02938 -0.17182 632 ASN   C CA   
2011 C  C    . ASN   B 8   ? 0.46001 0.72773 0.67719 0.03890  -0.04707 -0.14878 632 ASN   C C    
2012 O  O    . ASN   B 8   ? 0.41578 0.69567 0.62535 0.04684  -0.05911 -0.15058 632 ASN   C O    
2013 C  CB   . ASN   B 8   ? 0.38240 0.65584 0.63750 0.04416  -0.02960 -0.19310 632 ASN   C CB   
2014 C  CG   . ASN   B 8   ? 0.55801 0.83816 0.79822 0.05535  -0.04592 -0.20542 632 ASN   C CG   
2015 O  OD1  . ASN   B 8   ? 0.62842 0.89288 0.83797 0.05522  -0.05885 -0.19669 632 ASN   C OD1  
2016 N  ND2  . ASN   B 8   ? 0.55955 0.86309 0.82141 0.06510  -0.04541 -0.22575 632 ASN   C ND2  
2017 N  N    . LEU   B 9   ? 0.39514 0.63937 0.58850 0.02926  -0.04898 -0.12708 633 LEU   C N    
2018 C  CA   . LEU   B 9   ? 0.39744 0.62981 0.55502 0.02749  -0.06528 -0.10357 633 LEU   C CA   
2019 C  C    . LEU   B 9   ? 0.50468 0.74712 0.66377 0.02568  -0.06651 -0.08603 633 LEU   C C    
2020 O  O    . LEU   B 9   ? 0.53166 0.77428 0.66777 0.02874  -0.08143 -0.07366 633 LEU   C O    
2021 C  CB   . LEU   B 9   ? 0.41008 0.61480 0.54331 0.01708  -0.06589 -0.08448 633 LEU   C CB   
2022 C  CG   . LEU   B 9   ? 0.51938 0.71116 0.64300 0.01901  -0.06846 -0.09835 633 LEU   C CG   
2023 C  CD1  . LEU   B 9   ? 0.48859 0.65440 0.59606 0.00742  -0.06419 -0.08102 633 LEU   C CD1  
2024 C  CD2  . LEU   B 9   ? 0.58818 0.77966 0.68633 0.02773  -0.08748 -0.10213 633 LEU   C CD2  
2025 N  N    . LEU   B 10  ? 0.42086 0.67174 0.60667 0.02081  -0.05106 -0.08471 634 LEU   C N    
2026 C  CA   . LEU   B 10  ? 0.48606 0.74948 0.67803 0.02005  -0.05078 -0.07134 634 LEU   C CA   
2027 C  C    . LEU   B 10  ? 0.62399 0.91241 0.83038 0.03194  -0.05575 -0.08910 634 LEU   C C    
2028 O  O    . LEU   B 10  ? 0.56933 0.86954 0.78012 0.03256  -0.05689 -0.07920 634 LEU   C O    
2029 C  CB   . LEU   B 10  ? 0.42883 0.69442 0.64671 0.01159  -0.03209 -0.06627 634 LEU   C CB   
2030 C  CG   . LEU   B 10  ? 0.53922 0.78274 0.74138 -0.00156 -0.02811 -0.03941 634 LEU   C CG   
2031 C  CD1  . LEU   B 10  ? 0.57968 0.82628 0.81160 -0.00883 -0.00805 -0.04053 634 LEU   C CD1  
2032 C  CD2  . LEU   B 10  ? 0.60690 0.84636 0.78472 -0.00452 -0.03959 -0.01228 634 LEU   C CD2  
2033 N  N    . LYS   B 11  ? 0.62129 0.91754 0.83466 0.04118  -0.05873 -0.11452 635 LYS   C N    
2034 C  CA   . LYS   B 11  ? 0.74196 1.06205 0.97062 0.05313  -0.06295 -0.13498 635 LYS   C CA   
2035 C  C    . LYS   B 11  ? 0.85131 1.19139 1.10891 0.05352  -0.05215 -0.13684 635 LYS   C C    
2036 O  O    . LYS   B 11  ? 0.90725 1.25189 1.19255 0.04981  -0.03557 -0.14536 635 LYS   C O    
2037 C  CB   . LYS   B 11  ? 0.77336 1.09358 0.97272 0.05967  -0.08324 -0.12756 635 LYS   C CB   
2038 C  CG   . LYS   B 11  ? 0.82540 1.14521 1.00928 0.05595  -0.09008 -0.10132 635 LYS   C CG   
2039 C  CD   . LYS   B 11  ? 0.87373 1.21181 1.05468 0.06646  -0.10238 -0.10709 635 LYS   C CD   
2040 C  CE   . LYS   B 11  ? 0.81921 1.16344 0.99831 0.06314  -0.10339 -0.08596 635 LYS   C CE   
2041 N  NZ   . LYS   B 11  ? 0.76452 1.13026 0.94883 0.07362  -0.11184 -0.09487 635 LYS   C NZ   
2042 C  C10  . A1L77 C .   ? 0.63546 0.58868 0.53581 -0.01814 0.00540  -0.02918 501 A1L77 A C10  
2043 C  C13  . A1L77 C .   ? 0.60279 0.60916 0.52428 -0.00282 0.00967  -0.02045 501 A1L77 A C13  
2044 C  C15  . A1L77 C .   ? 0.65276 0.61870 0.56515 0.00303  0.00984  -0.03018 501 A1L77 A C15  
2045 C  C17  . A1L77 C .   ? 0.64631 0.67099 0.59104 -0.00060 0.00574  -0.00564 501 A1L77 A C17  
2046 C  C20  . A1L77 C .   ? 0.59130 0.68416 0.54976 -0.00882 0.00928  0.01120  501 A1L77 A C20  
2047 C  C21  . A1L77 C .   ? 0.61871 0.66317 0.58943 0.00092  0.00223  0.00780  501 A1L77 A C21  
2048 C  C22  . A1L77 C .   ? 0.65763 0.69084 0.62159 0.01049  0.00579  -0.00329 501 A1L77 A C22  
2049 C  C24  . A1L77 C .   ? 0.84869 0.72390 0.73800 0.00388  0.00379  -0.02433 501 A1L77 A C24  
2050 C  C28  . A1L77 C .   ? 0.70580 0.57535 0.59028 0.00856  -0.00191 -0.00839 501 A1L77 A C28  
2051 C  C01  . A1L77 C .   ? 0.53205 0.44270 0.43646 0.00675  0.00523  -0.02885 501 A1L77 A C01  
2052 C  C02  . A1L77 C .   ? 0.67590 0.56878 0.57186 0.00673  0.00633  -0.03144 501 A1L77 A C02  
2053 C  C03  . A1L77 C .   ? 0.68735 0.57489 0.57726 0.00289  0.00874  -0.03776 501 A1L77 A C03  
2054 C  C04  . A1L77 C .   ? 0.61702 0.51938 0.50701 -0.00098 0.01005  -0.04100 501 A1L77 A C04  
2055 C  C05  . A1L77 C .   ? 0.59977 0.52097 0.49732 -0.00114 0.00861  -0.03581 501 A1L77 A C05  
2056 C  C06  . A1L77 C .   ? 0.56088 0.48459 0.46686 0.00290  0.00612  -0.02982 501 A1L77 A C06  
2057 C  C09  . A1L77 C .   ? 0.63698 0.60517 0.54286 -0.00498 0.00962  -0.03125 501 A1L77 A C09  
2058 C  C11  . A1L77 C .   ? 0.63909 0.62929 0.54574 -0.01147 0.00912  -0.02706 501 A1L77 A C11  
2059 C  C12  . A1L77 C .   ? 0.60200 0.61157 0.51606 -0.01068 0.00908  -0.02095 501 A1L77 A C12  
2060 C  C14  . A1L77 C .   ? 0.63910 0.62397 0.55941 0.00415  0.00994  -0.02556 501 A1L77 A C14  
2061 C  C18  . A1L77 C .   ? 0.59848 0.64695 0.55422 -0.00394 0.00482  0.00432  501 A1L77 A C18  
2062 C  C19  . A1L77 C .   ? 0.58291 0.64890 0.53015 -0.00310 0.01061  -0.00167 501 A1L77 A C19  
2063 C  C25  . A1L77 C .   ? 0.87104 0.75473 0.76314 0.00473  0.00140  -0.01928 501 A1L77 A C25  
2064 C  C27  . A1L77 C .   ? 0.73094 0.61010 0.62303 0.01219  -0.00052 -0.01502 501 A1L77 A C27  
2065 C  C29  . A1L77 C .   ? 0.70564 0.58771 0.59047 0.01029  -0.00474 -0.00331 501 A1L77 A C29  
2066 C  C32  . A1L77 C .   ? 0.77768 0.64381 0.66147 0.00192  0.00964  -0.04127 501 A1L77 A C32  
2067 C  C33  . A1L77 C .   ? 0.60944 0.64557 0.52395 -0.01955 0.00770  -0.01320 501 A1L77 A C33  
2068 C  C34  . A1L77 C .   ? 0.77551 0.71173 0.65905 -0.01229 0.01341  -0.04997 501 A1L77 A C34  
2069 C  C35  . A1L77 C .   ? 0.82625 0.77622 0.70795 -0.00989 0.01712  -0.05760 501 A1L77 A C35  
2070 C  C36  . A1L77 C .   ? 0.86720 0.80534 0.75344 0.00114  0.01897  -0.06099 501 A1L77 A C36  
2071 C  C37  . A1L77 C .   ? 0.84014 0.78903 0.72364 0.00294  0.02398  -0.07412 501 A1L77 A C37  
2072 C  C38  . A1L77 C .   ? 0.66275 0.62584 0.57790 -0.01672 0.00168  -0.01967 501 A1L77 A C38  
2073 C  C39  . A1L77 C .   ? 0.65537 0.64015 0.57560 -0.02206 -0.00033 -0.01284 501 A1L77 A C39  
2074 C  C40  . A1L77 C .   ? 0.56865 0.56314 0.50591 -0.01947 -0.00365 -0.00333 501 A1L77 A C40  
2075 O  O07  . A1L77 C .   ? 0.84607 0.72838 0.74062 0.00992  0.00465  -0.02739 501 A1L77 A O07  
2076 O  O16  . A1L77 C .   ? 0.64525 0.67146 0.57539 -0.00272 0.00966  -0.01396 501 A1L77 A O16  
2077 O  O23  . A1L77 C .   ? 0.50795 0.56817 0.47094 -0.01236 0.00063  0.01624  501 A1L77 A O23  
2078 O  O26  . A1L77 C .   ? 0.93782 0.83797 0.83936 0.00561  0.00062  -0.02071 501 A1L77 A O26  
2079 O  O30  . A1L77 C .   ? 0.66443 0.56299 0.55411 0.00898  -0.00477 -0.00725 501 A1L77 A O30  
2080 O  O31  . A1L77 C .   ? 0.63893 0.51552 0.52021 0.01259  -0.00732 0.00457  501 A1L77 A O31  
2081 SI SI08 . A1L77 C .   ? 0.64497 0.58957 0.54161 -0.00836 0.00946  -0.03653 501 A1L77 A SI08 
# 
