data_9M1A
# 
_entry.id   9M1A 
# 
_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   9M1A         pdb_00009m1a 10.2210/pdb9m1a/pdb 
WWPDB D_1300056792 ?            ?                   
# 
_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                        9M1A 
_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-[diethyl-[4-(2-ethyl-2-oxidanyl-butoxy)-3-methyl-phenyl]silyl]-2-methyl-phenoxy]-4-oxidanyl-pentanoic acid' 516.742 
1   ? ? ? ? 
4 water       nat water 18.015    159 ? ? ? ? 
# 
_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-[diethyl-[4-(2-ethyl-2-oxidanyl-butoxy)-3-methyl-phenyl]silyl]-2-methyl-phenoxy]-4-oxidanyl-pentanoic acid' A1L78 
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 
A1L78 non-polymer         . 
'(4~{S})-5-[4-[diethyl-[4-(2-ethyl-2-oxidanyl-butoxy)-3-methyl-phenyl]silyl]-2-methyl-phenoxy]-4-oxidanyl-pentanoic acid' ? 
'C29 H44 O6 Si'  516.742 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   106 ?   ?   ?   A . n 
A 1 2   SER 2   107 ?   ?   ?   A . n 
A 1 3   HIS 3   108 ?   ?   ?   A . n 
A 1 4   MET 4   109 ?   ?   ?   A . n 
A 1 5   GLY 5   110 ?   ?   ?   A . n 
A 1 6   SER 6   111 ?   ?   ?   A . n 
A 1 7   PRO 7   112 ?   ?   ?   A . n 
A 1 8   ASN 8   113 ?   ?   ?   A . n 
A 1 9   SER 9   114 ?   ?   ?   A . n 
A 1 10  PRO 10  115 ?   ?   ?   A . n 
A 1 11  LEU 11  116 ?   ?   ?   A . n 
A 1 12  LYS 12  117 ?   ?   ?   A . n 
A 1 13  ASP 13  118 ?   ?   ?   A . n 
A 1 14  SER 14  119 ?   ?   ?   A . n 
A 1 15  LEU 15  120 ?   ?   ?   A . n 
A 1 16  ARG 16  121 ?   ?   ?   A . n 
A 1 17  PRO 17  122 ?   ?   ?   A . n 
A 1 18  LYS 18  123 123 LYS LYS A . n 
A 1 19  LEU 19  124 124 LEU LEU A . n 
A 1 20  SER 20  125 125 SER SER A . n 
A 1 21  GLU 21  126 126 GLU GLU A . n 
A 1 22  GLU 22  127 127 GLU GLU A . n 
A 1 23  GLN 23  128 128 GLN GLN A . n 
A 1 24  GLN 24  129 129 GLN GLN A . n 
A 1 25  HIS 25  130 130 HIS HIS A . n 
A 1 26  ILE 26  131 131 ILE ILE A . n 
A 1 27  ILE 27  132 132 ILE ILE A . n 
A 1 28  ALA 28  133 133 ALA ALA A . n 
A 1 29  ILE 29  134 134 ILE ILE A . n 
A 1 30  LEU 30  135 135 LEU LEU A . n 
A 1 31  LEU 31  136 136 LEU LEU A . n 
A 1 32  ASP 32  137 137 ASP ASP A . n 
A 1 33  ALA 33  138 138 ALA ALA A . n 
A 1 34  HIS 34  139 139 HIS HIS A . n 
A 1 35  HIS 35  140 140 HIS HIS A . n 
A 1 36  LYS 36  141 141 LYS LYS A . n 
A 1 37  THR 37  142 142 THR THR A . n 
A 1 38  TYR 38  143 143 TYR TYR A . n 
A 1 39  ASP 39  144 144 ASP ASP A . n 
A 1 40  PRO 40  145 145 PRO PRO A . n 
A 1 41  THR 41  146 146 THR THR A . n 
A 1 42  TYR 42  147 147 TYR TYR A . n 
A 1 43  ALA 43  148 148 ALA ALA A . n 
A 1 44  ASP 44  149 149 ASP ASP A . n 
A 1 45  PHE 45  150 150 PHE PHE A . n 
A 1 46  ARG 46  151 151 ARG ARG A . n 
A 1 47  ASP 47  152 152 ASP ASP A . n 
A 1 48  PHE 48  153 153 PHE PHE A . n 
A 1 49  ARG 49  154 154 ARG ARG A . n 
A 1 50  PRO 50  155 155 PRO PRO A . n 
A 1 51  PRO 51  156 156 PRO PRO A . n 
A 1 52  VAL 52  157 157 VAL VAL A . n 
A 1 53  ARG 53  158 158 ARG ARG A . n 
A 1 54  MET 54  159 159 MET MET A . n 
A 1 55  ASP 55  207 ?   ?   ?   A . n 
A 1 56  GLY 56  208 ?   ?   ?   A . n 
A 1 57  SER 57  209 ?   ?   ?   A . n 
A 1 58  THR 58  210 ?   ?   ?   A . n 
A 1 59  GLY 59  211 ?   ?   ?   A . n 
A 1 60  SER 60  212 ?   ?   ?   A . n 
A 1 61  VAL 61  213 ?   ?   ?   A . n 
A 1 62  THR 62  214 ?   ?   ?   A . n 
A 1 63  LEU 63  215 ?   ?   ?   A . n 
A 1 64  ASP 64  216 ?   ?   ?   A . n 
A 1 65  LEU 65  217 ?   ?   ?   A . n 
A 1 66  SER 66  218 218 SER SER A . n 
A 1 67  PRO 67  219 219 PRO PRO A . n 
A 1 68  LEU 68  220 220 LEU LEU A . n 
A 1 69  SER 69  221 221 SER SER A . n 
A 1 70  MET 70  222 222 MET MET A . n 
A 1 71  LEU 71  223 223 LEU LEU A . n 
A 1 72  PRO 72  224 224 PRO PRO A . n 
A 1 73  HIS 73  225 225 HIS HIS A . n 
A 1 74  LEU 74  226 226 LEU LEU A . n 
A 1 75  ALA 75  227 227 ALA ALA A . n 
A 1 76  ASP 76  228 228 ASP ASP A . n 
A 1 77  LEU 77  229 229 LEU LEU A . n 
A 1 78  VAL 78  230 230 VAL VAL A . n 
A 1 79  SER 79  231 231 SER SER A . n 
A 1 80  TYR 80  232 232 TYR TYR A . n 
A 1 81  SER 81  233 233 SER SER A . n 
A 1 82  ILE 82  234 234 ILE ILE A . n 
A 1 83  GLN 83  235 235 GLN GLN A . n 
A 1 84  LYS 84  236 236 LYS LYS A . n 
A 1 85  VAL 85  237 237 VAL VAL A . n 
A 1 86  ILE 86  238 238 ILE ILE A . n 
A 1 87  GLY 87  239 239 GLY GLY A . n 
A 1 88  PHE 88  240 240 PHE PHE A . n 
A 1 89  ALA 89  241 241 ALA ALA A . n 
A 1 90  LYS 90  242 242 LYS LYS A . n 
A 1 91  MET 91  243 243 MET MET A . n 
A 1 92  ILE 92  244 244 ILE ILE A . n 
A 1 93  PRO 93  245 245 PRO PRO A . n 
A 1 94  GLY 94  246 246 GLY GLY A . n 
A 1 95  PHE 95  247 247 PHE PHE A . n 
A 1 96  ARG 96  248 248 ARG ARG A . n 
A 1 97  ASP 97  249 249 ASP ASP A . n 
A 1 98  LEU 98  250 250 LEU LEU A . n 
A 1 99  THR 99  251 251 THR THR A . n 
A 1 100 SER 100 252 252 SER SER A . n 
A 1 101 ASP 101 253 253 ASP ASP A . n 
A 1 102 ASP 102 254 254 ASP ASP A . n 
A 1 103 GLN 103 255 255 GLN GLN A . n 
A 1 104 ILE 104 256 256 ILE ILE A . n 
A 1 105 VAL 105 257 257 VAL VAL A . n 
A 1 106 LEU 106 258 258 LEU LEU A . n 
A 1 107 LEU 107 259 259 LEU LEU A . n 
A 1 108 LYS 108 260 260 LYS LYS A . n 
A 1 109 SER 109 261 261 SER SER A . n 
A 1 110 SER 110 262 262 SER SER A . n 
A 1 111 ALA 111 263 263 ALA ALA A . n 
A 1 112 ILE 112 264 264 ILE ILE A . n 
A 1 113 GLU 113 265 265 GLU GLU A . n 
A 1 114 VAL 114 266 266 VAL VAL A . n 
A 1 115 ILE 115 267 267 ILE ILE A . n 
A 1 116 MET 116 268 268 MET MET A . n 
A 1 117 LEU 117 269 269 LEU LEU A . n 
A 1 118 ARG 118 270 270 ARG ARG A . n 
A 1 119 SER 119 271 271 SER SER A . n 
A 1 120 ASN 120 272 272 ASN ASN A . n 
A 1 121 GLN 121 273 273 GLN GLN A . n 
A 1 122 SER 122 274 274 SER SER A . n 
A 1 123 PHE 123 275 275 PHE PHE A . n 
A 1 124 THR 124 276 276 THR THR A . n 
A 1 125 MET 125 277 277 MET MET A . n 
A 1 126 ASP 126 278 278 ASP ASP A . n 
A 1 127 ASP 127 279 279 ASP ASP A . n 
A 1 128 MET 128 280 280 MET MET A . n 
A 1 129 SER 129 281 281 SER SER A . n 
A 1 130 TRP 130 282 282 TRP TRP A . n 
A 1 131 ASP 131 283 283 ASP ASP A . n 
A 1 132 CYS 132 284 284 CYS CYS A . n 
A 1 133 GLY 133 285 285 GLY GLY A . n 
A 1 134 SER 134 286 286 SER SER A . n 
A 1 135 GLN 135 287 287 GLN GLN A . n 
A 1 136 ASP 136 288 288 ASP ASP A . n 
A 1 137 TYR 137 289 289 TYR TYR A . n 
A 1 138 LYS 138 290 290 LYS LYS A . n 
A 1 139 TYR 139 291 291 TYR TYR A . n 
A 1 140 ASP 140 292 292 ASP ASP A . n 
A 1 141 VAL 141 293 293 VAL VAL A . n 
A 1 142 THR 142 294 294 THR THR A . n 
A 1 143 ASP 143 295 295 ASP ASP A . n 
A 1 144 VAL 144 296 296 VAL VAL A . n 
A 1 145 SER 145 297 297 SER SER A . n 
A 1 146 LYS 146 298 298 LYS LYS A . n 
A 1 147 ALA 147 299 299 ALA ALA A . n 
A 1 148 GLY 148 300 300 GLY GLY A . n 
A 1 149 HIS 149 301 301 HIS HIS A . n 
A 1 150 THR 150 302 302 THR THR A . n 
A 1 151 LEU 151 303 303 LEU LEU A . n 
A 1 152 GLU 152 304 304 GLU GLU A . n 
A 1 153 LEU 153 305 305 LEU LEU A . n 
A 1 154 ILE 154 306 306 ILE ILE A . n 
A 1 155 GLU 155 307 307 GLU GLU A . n 
A 1 156 PRO 156 308 308 PRO PRO A . n 
A 1 157 LEU 157 309 309 LEU LEU A . n 
A 1 158 ILE 158 310 310 ILE ILE A . n 
A 1 159 LYS 159 311 311 LYS LYS A . n 
A 1 160 PHE 160 312 312 PHE PHE A . n 
A 1 161 GLN 161 313 313 GLN GLN A . n 
A 1 162 VAL 162 314 314 VAL VAL A . n 
A 1 163 GLY 163 315 315 GLY GLY A . n 
A 1 164 LEU 164 316 316 LEU LEU A . n 
A 1 165 LYS 165 317 317 LYS LYS A . n 
A 1 166 LYS 166 318 318 LYS LYS A . n 
A 1 167 LEU 167 319 319 LEU LEU A . n 
A 1 168 ASN 168 320 320 ASN ASN A . n 
A 1 169 LEU 169 321 321 LEU LEU A . n 
A 1 170 HIS 170 322 322 HIS HIS A . n 
A 1 171 GLU 171 323 323 GLU GLU A . n 
A 1 172 GLU 172 324 324 GLU GLU A . n 
A 1 173 GLU 173 325 325 GLU GLU A . n 
A 1 174 HIS 174 326 326 HIS HIS A . n 
A 1 175 VAL 175 327 327 VAL VAL A . n 
A 1 176 LEU 176 328 328 LEU LEU A . n 
A 1 177 LEU 177 329 329 LEU LEU A . n 
A 1 178 MET 178 330 330 MET MET A . n 
A 1 179 ALA 179 331 331 ALA ALA A . n 
A 1 180 ILE 180 332 332 ILE ILE A . n 
A 1 181 CYS 181 333 333 CYS CYS A . n 
A 1 182 ILE 182 334 334 ILE ILE A . n 
A 1 183 VAL 183 335 335 VAL VAL A . n 
A 1 184 SER 184 336 336 SER SER A . n 
A 1 185 PRO 185 337 337 PRO PRO A . n 
A 1 186 ASP 186 338 338 ASP ASP A . n 
A 1 187 ARG 187 339 339 ARG ARG A . n 
A 1 188 PRO 188 340 340 PRO PRO A . n 
A 1 189 GLY 189 341 341 GLY GLY A . n 
A 1 190 VAL 190 342 342 VAL VAL A . n 
A 1 191 GLN 191 343 343 GLN GLN A . n 
A 1 192 ASP 192 344 344 ASP ASP A . n 
A 1 193 ALA 193 345 345 ALA ALA A . n 
A 1 194 LYS 194 346 346 LYS LYS A . n 
A 1 195 LEU 195 347 347 LEU LEU A . n 
A 1 196 VAL 196 348 348 VAL VAL A . n 
A 1 197 GLU 197 349 349 GLU GLU A . n 
A 1 198 ALA 198 350 350 ALA ALA A . n 
A 1 199 ILE 199 351 351 ILE ILE A . n 
A 1 200 GLN 200 352 352 GLN GLN A . n 
A 1 201 ASP 201 353 353 ASP ASP A . n 
A 1 202 ARG 202 354 354 ARG ARG A . n 
A 1 203 LEU 203 355 355 LEU LEU A . n 
A 1 204 SER 204 356 356 SER SER A . n 
A 1 205 ASN 205 357 357 ASN ASN A . n 
A 1 206 THR 206 358 358 THR THR A . n 
A 1 207 LEU 207 359 359 LEU LEU A . n 
A 1 208 GLN 208 360 360 GLN GLN A . n 
A 1 209 THR 209 361 361 THR THR A . n 
A 1 210 TYR 210 362 362 TYR TYR A . n 
A 1 211 ILE 211 363 363 ILE ILE A . n 
A 1 212 ARG 212 364 364 ARG ARG A . n 
A 1 213 CYS 213 365 365 CYS CYS A . n 
A 1 214 ARG 214 366 366 ARG ARG A . n 
A 1 215 HIS 215 367 367 HIS HIS A . n 
A 1 216 PRO 216 368 368 PRO PRO A . n 
A 1 217 PRO 217 369 369 PRO PRO A . n 
A 1 218 PRO 218 370 370 PRO PRO A . n 
A 1 219 GLY 219 371 371 GLY GLY A . n 
A 1 220 SER 220 372 372 SER SER A . n 
A 1 221 HIS 221 373 373 HIS HIS A . n 
A 1 222 GLN 222 374 374 GLN GLN A . n 
A 1 223 LEU 223 375 375 LEU LEU A . n 
A 1 224 TYR 224 376 376 TYR TYR A . n 
A 1 225 ALA 225 377 377 ALA ALA A . n 
A 1 226 LYS 226 378 378 LYS LYS A . n 
A 1 227 MET 227 379 379 MET MET A . n 
A 1 228 ILE 228 380 380 ILE ILE A . n 
A 1 229 GLN 229 381 381 GLN GLN A . n 
A 1 230 LYS 230 382 382 LYS LYS A . n 
A 1 231 LEU 231 383 383 LEU LEU A . n 
A 1 232 ALA 232 384 384 ALA ALA A . n 
A 1 233 ASP 233 385 385 ASP ASP A . n 
A 1 234 LEU 234 386 386 LEU LEU A . n 
A 1 235 ARG 235 387 387 ARG ARG A . n 
A 1 236 SER 236 388 388 SER SER A . n 
A 1 237 LEU 237 389 389 LEU LEU A . n 
A 1 238 ASN 238 390 390 ASN ASN A . n 
A 1 239 GLU 239 391 391 GLU GLU A . n 
A 1 240 GLU 240 392 392 GLU GLU A . n 
A 1 241 HIS 241 393 393 HIS HIS A . n 
A 1 242 SER 242 394 394 SER SER A . n 
A 1 243 LYS 243 395 395 LYS LYS A . n 
A 1 244 GLN 244 396 396 GLN GLN A . n 
A 1 245 TYR 245 397 397 TYR TYR A . n 
A 1 246 ARG 246 398 398 ARG ARG A . n 
A 1 247 SER 247 399 399 SER SER A . n 
A 1 248 LEU 248 400 400 LEU LEU A . n 
A 1 249 SER 249 401 401 SER SER A . n 
A 1 250 PHE 250 402 402 PHE PHE A . n 
A 1 251 GLN 251 403 403 GLN GLN A . n 
A 1 252 PRO 252 404 404 PRO PRO A . n 
A 1 253 GLU 253 405 405 GLU GLU A . n 
A 1 254 ASN 254 406 406 ASN ASN A . n 
A 1 255 SER 255 407 407 SER SER A . n 
A 1 256 MET 256 408 408 MET MET A . n 
A 1 257 LYS 257 409 409 LYS LYS A . n 
A 1 258 LEU 258 410 410 LEU LEU A . n 
A 1 259 THR 259 411 411 THR THR A . n 
A 1 260 PRO 260 412 412 PRO PRO A . n 
A 1 261 LEU 261 413 413 LEU LEU A . n 
A 1 262 VAL 262 414 414 VAL VAL A . n 
A 1 263 LEU 263 415 415 LEU LEU A . n 
A 1 264 GLU 264 416 416 GLU GLU A . n 
A 1 265 VAL 265 417 417 VAL VAL A . n 
A 1 266 PHE 266 418 418 PHE PHE A . n 
A 1 267 GLY 267 419 419 GLY GLY A . n 
A 1 268 ASN 268 420 420 ASN ASN A . n 
A 1 269 GLU 269 421 ?   ?   ?   A . n 
A 1 270 ILE 270 422 ?   ?   ?   A . n 
A 1 271 SER 271 423 ?   ?   ?   A . n 
B 2 1   LYS 1   625 625 LYS LYS C . n 
B 2 2   ASN 2   626 626 ASN ASN C . n 
B 2 3   HIS 3   627 627 HIS HIS C . n 
B 2 4   PRO 4   628 628 PRO PRO C . n 
B 2 5   MET 5   629 629 MET MET C . n 
B 2 6   LEU 6   630 630 LEU LEU C . n 
B 2 7   MET 7   631 631 MET MET C . n 
B 2 8   ASN 8   632 632 ASN ASN C . n 
B 2 9   LEU 9   633 633 LEU LEU C . n 
B 2 10  LEU 10  634 634 LEU LEU C . n 
B 2 11  LYS 11  635 635 LYS LYS C . n 
B 2 12  ASP 12  636 ?   ?   ?   C . n 
B 2 13  ASN 13  637 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1L78 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L78 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1L78 1   501 501 A1L78 LIG A . 
D 4 HOH   1   601 20  HOH   HOH A . 
D 4 HOH   2   602 144 HOH   HOH A . 
D 4 HOH   3   603 27  HOH   HOH A . 
D 4 HOH   4   604 154 HOH   HOH A . 
D 4 HOH   5   605 143 HOH   HOH A . 
D 4 HOH   6   606 128 HOH   HOH A . 
D 4 HOH   7   607 171 HOH   HOH A . 
D 4 HOH   8   608 124 HOH   HOH A . 
D 4 HOH   9   609 98  HOH   HOH A . 
D 4 HOH   10  610 15  HOH   HOH A . 
D 4 HOH   11  611 11  HOH   HOH A . 
D 4 HOH   12  612 32  HOH   HOH A . 
D 4 HOH   13  613 158 HOH   HOH A . 
D 4 HOH   14  614 26  HOH   HOH A . 
D 4 HOH   15  615 79  HOH   HOH A . 
D 4 HOH   16  616 99  HOH   HOH A . 
D 4 HOH   17  617 73  HOH   HOH A . 
D 4 HOH   18  618 2   HOH   HOH A . 
D 4 HOH   19  619 12  HOH   HOH A . 
D 4 HOH   20  620 166 HOH   HOH A . 
D 4 HOH   21  621 65  HOH   HOH A . 
D 4 HOH   22  622 80  HOH   HOH A . 
D 4 HOH   23  623 19  HOH   HOH A . 
D 4 HOH   24  624 18  HOH   HOH A . 
D 4 HOH   25  625 38  HOH   HOH A . 
D 4 HOH   26  626 96  HOH   HOH A . 
D 4 HOH   27  627 34  HOH   HOH A . 
D 4 HOH   28  628 3   HOH   HOH A . 
D 4 HOH   29  629 54  HOH   HOH A . 
D 4 HOH   30  630 52  HOH   HOH A . 
D 4 HOH   31  631 9   HOH   HOH A . 
D 4 HOH   32  632 7   HOH   HOH A . 
D 4 HOH   33  633 28  HOH   HOH A . 
D 4 HOH   34  634 40  HOH   HOH A . 
D 4 HOH   35  635 8   HOH   HOH A . 
D 4 HOH   36  636 1   HOH   HOH A . 
D 4 HOH   37  637 5   HOH   HOH A . 
D 4 HOH   38  638 14  HOH   HOH A . 
D 4 HOH   39  639 37  HOH   HOH A . 
D 4 HOH   40  640 33  HOH   HOH A . 
D 4 HOH   41  641 92  HOH   HOH A . 
D 4 HOH   42  642 167 HOH   HOH A . 
D 4 HOH   43  643 23  HOH   HOH A . 
D 4 HOH   44  644 119 HOH   HOH A . 
D 4 HOH   45  645 51  HOH   HOH A . 
D 4 HOH   46  646 82  HOH   HOH A . 
D 4 HOH   47  647 41  HOH   HOH A . 
D 4 HOH   48  648 63  HOH   HOH A . 
D 4 HOH   49  649 48  HOH   HOH A . 
D 4 HOH   50  650 69  HOH   HOH A . 
D 4 HOH   51  651 4   HOH   HOH A . 
D 4 HOH   52  652 100 HOH   HOH A . 
D 4 HOH   53  653 39  HOH   HOH A . 
D 4 HOH   54  654 44  HOH   HOH A . 
D 4 HOH   55  655 50  HOH   HOH A . 
D 4 HOH   56  656 64  HOH   HOH A . 
D 4 HOH   57  657 74  HOH   HOH A . 
D 4 HOH   58  658 56  HOH   HOH A . 
D 4 HOH   59  659 6   HOH   HOH A . 
D 4 HOH   60  660 126 HOH   HOH A . 
D 4 HOH   61  661 57  HOH   HOH A . 
D 4 HOH   62  662 162 HOH   HOH A . 
D 4 HOH   63  663 150 HOH   HOH A . 
D 4 HOH   64  664 129 HOH   HOH A . 
D 4 HOH   65  665 70  HOH   HOH A . 
D 4 HOH   66  666 133 HOH   HOH A . 
D 4 HOH   67  667 77  HOH   HOH A . 
D 4 HOH   68  668 16  HOH   HOH A . 
D 4 HOH   69  669 76  HOH   HOH A . 
D 4 HOH   70  670 42  HOH   HOH A . 
D 4 HOH   71  671 55  HOH   HOH A . 
D 4 HOH   72  672 153 HOH   HOH A . 
D 4 HOH   73  673 47  HOH   HOH A . 
D 4 HOH   74  674 10  HOH   HOH A . 
D 4 HOH   75  675 148 HOH   HOH A . 
D 4 HOH   76  676 58  HOH   HOH A . 
D 4 HOH   77  677 113 HOH   HOH A . 
D 4 HOH   78  678 60  HOH   HOH A . 
D 4 HOH   79  679 49  HOH   HOH A . 
D 4 HOH   80  680 163 HOH   HOH A . 
D 4 HOH   81  681 30  HOH   HOH A . 
D 4 HOH   82  682 13  HOH   HOH A . 
D 4 HOH   83  683 157 HOH   HOH A . 
D 4 HOH   84  684 89  HOH   HOH A . 
D 4 HOH   85  685 45  HOH   HOH A . 
D 4 HOH   86  686 72  HOH   HOH A . 
D 4 HOH   87  687 46  HOH   HOH A . 
D 4 HOH   88  688 168 HOH   HOH A . 
D 4 HOH   89  689 118 HOH   HOH A . 
D 4 HOH   90  690 161 HOH   HOH A . 
D 4 HOH   91  691 122 HOH   HOH A . 
D 4 HOH   92  692 88  HOH   HOH A . 
D 4 HOH   93  693 81  HOH   HOH A . 
D 4 HOH   94  694 29  HOH   HOH A . 
D 4 HOH   95  695 164 HOH   HOH A . 
D 4 HOH   96  696 22  HOH   HOH A . 
D 4 HOH   97  697 141 HOH   HOH A . 
D 4 HOH   98  698 31  HOH   HOH A . 
D 4 HOH   99  699 142 HOH   HOH A . 
D 4 HOH   100 700 36  HOH   HOH A . 
D 4 HOH   101 701 111 HOH   HOH A . 
D 4 HOH   102 702 21  HOH   HOH A . 
D 4 HOH   103 703 78  HOH   HOH A . 
D 4 HOH   104 704 97  HOH   HOH A . 
D 4 HOH   105 705 108 HOH   HOH A . 
D 4 HOH   106 706 67  HOH   HOH A . 
D 4 HOH   107 707 35  HOH   HOH A . 
D 4 HOH   108 708 160 HOH   HOH A . 
D 4 HOH   109 709 146 HOH   HOH A . 
D 4 HOH   110 710 165 HOH   HOH A . 
D 4 HOH   111 711 17  HOH   HOH A . 
D 4 HOH   112 712 115 HOH   HOH A . 
D 4 HOH   113 713 152 HOH   HOH A . 
D 4 HOH   114 714 59  HOH   HOH A . 
D 4 HOH   115 715 137 HOH   HOH A . 
D 4 HOH   116 716 139 HOH   HOH A . 
D 4 HOH   117 717 130 HOH   HOH A . 
D 4 HOH   118 718 121 HOH   HOH A . 
D 4 HOH   119 719 151 HOH   HOH A . 
D 4 HOH   120 720 155 HOH   HOH A . 
D 4 HOH   121 721 87  HOH   HOH A . 
D 4 HOH   122 722 131 HOH   HOH A . 
D 4 HOH   123 723 140 HOH   HOH A . 
D 4 HOH   124 724 85  HOH   HOH A . 
D 4 HOH   125 725 136 HOH   HOH A . 
D 4 HOH   126 726 159 HOH   HOH A . 
D 4 HOH   127 727 134 HOH   HOH A . 
D 4 HOH   128 728 102 HOH   HOH A . 
D 4 HOH   129 729 123 HOH   HOH A . 
D 4 HOH   130 730 114 HOH   HOH A . 
D 4 HOH   131 731 25  HOH   HOH A . 
D 4 HOH   132 732 106 HOH   HOH A . 
D 4 HOH   133 733 149 HOH   HOH A . 
D 4 HOH   134 734 75  HOH   HOH A . 
D 4 HOH   135 735 125 HOH   HOH A . 
D 4 HOH   136 736 95  HOH   HOH A . 
D 4 HOH   137 737 105 HOH   HOH A . 
D 4 HOH   138 738 135 HOH   HOH A . 
D 4 HOH   139 739 170 HOH   HOH A . 
D 4 HOH   140 740 103 HOH   HOH A . 
D 4 HOH   141 741 93  HOH   HOH A . 
D 4 HOH   142 742 147 HOH   HOH A . 
D 4 HOH   143 743 62  HOH   HOH A . 
D 4 HOH   144 744 172 HOH   HOH A . 
D 4 HOH   145 745 116 HOH   HOH A . 
D 4 HOH   146 746 53  HOH   HOH A . 
D 4 HOH   147 747 66  HOH   HOH A . 
D 4 HOH   148 748 169 HOH   HOH A . 
D 4 HOH   149 749 71  HOH   HOH A . 
D 4 HOH   150 750 138 HOH   HOH A . 
D 4 HOH   151 751 68  HOH   HOH A . 
D 4 HOH   152 752 132 HOH   HOH A . 
D 4 HOH   153 753 117 HOH   HOH A . 
D 4 HOH   154 754 112 HOH   HOH A . 
D 4 HOH   155 755 43  HOH   HOH A . 
D 4 HOH   156 756 127 HOH   HOH A . 
E 4 HOH   1   701 24  HOH   HOH C . 
E 4 HOH   2   702 145 HOH   HOH C . 
E 4 HOH   3   703 61  HOH   HOH C . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.14_3260 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.276 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9M1A 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     154.307 
_cell.length_a_esd                 ? 
_cell.length_b                     41.785 
_cell.length_b_esd                 ? 
_cell.length_c                     42.274 
_cell.length_c_esd                 ? 
_cell.volume                       270937.268 
_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                         9M1A 
_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                   9M1A 
_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             2.11 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.59 
_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' 
_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                                       9M1A 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.78 
_reflns.d_resolution_low                               42.02 
_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                                     25689 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.6 
_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                              0.047 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.78 
_reflns_shell.d_res_low                                     1.82 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1464 
_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                                  0.998 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.665 
_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                               35.68 
_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                                 9M1A 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.78 
_refine.ls_d_res_low                             40.32 
_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                     25670 
_refine.ls_number_reflns_R_free                  1284 
_refine.ls_number_reflns_R_work                  24386 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.88 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1808 
_refine.ls_R_factor_R_free                       0.2112 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1793 
_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                 23.4696 
_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                            0.1922 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.78 
_refine_hist.d_res_low                        40.32 
_refine_hist.number_atoms_solvent             159 
_refine_hist.number_atoms_total               2210 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2015 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0061  ? 2224 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7829  ? 3025 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0430  ? 332  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0040  ? 393  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 26.8915 ? 867  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.78 1.85  . . 142 2709 99.51 . . . . 0.2617 . . . . . . . . . . . . . . . 0.3190 
'X-RAY DIFFRACTION' 1.85 1.94  . . 141 2684 99.61 . . . . 0.2299 . . . . . . . . . . . . . . . 0.2731 
'X-RAY DIFFRACTION' 1.94 2.04  . . 144 2719 99.51 . . . . 0.2005 . . . . . . . . . . . . . . . 0.2327 
'X-RAY DIFFRACTION' 2.04 2.17  . . 142 2703 99.68 . . . . 0.1823 . . . . . . . . . . . . . . . 0.2346 
'X-RAY DIFFRACTION' 2.17 2.33  . . 144 2718 99.55 . . . . 0.1793 . . . . . . . . . . . . . . . 0.2193 
'X-RAY DIFFRACTION' 2.33 2.57  . . 141 2700 99.02 . . . . 0.1777 . . . . . . . . . . . . . . . 0.1934 
'X-RAY DIFFRACTION' 2.57 2.94  . . 143 2718 99.00 . . . . 0.1654 . . . . . . . . . . . . . . . 0.1978 
'X-RAY DIFFRACTION' 2.94 3.70  . . 142 2691 97.56 . . . . 0.1619 . . . . . . . . . . . . . . . 0.1998 
'X-RAY DIFFRACTION' 3.70 40.32 . . 145 2744 96.62 . . . . 0.1787 . . . . . . . . . . . . . . . 0.2015 
# 
_struct.entry_id                     9M1A 
_struct.title                        'Vitamin D receptor complex with a diethyldiphenylsilane 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        9M1A 
_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 9M1A A 11 ? 271 ? P13053 116 ? 423 ? 116 423 
2 2 9M1A 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 9M1A GLY A 1  ? UNP P13053 ?   ?   'expression tag' 106 1  
1 9M1A SER A 2  ? UNP P13053 ?   ?   'expression tag' 107 2  
1 9M1A HIS A 3  ? UNP P13053 ?   ?   'expression tag' 108 3  
1 9M1A MET A 4  ? UNP P13053 ?   ?   'expression tag' 109 4  
1 9M1A GLY A 5  ? UNP P13053 ?   ?   'expression tag' 110 5  
1 9M1A SER A 6  ? UNP P13053 ?   ?   'expression tag' 111 6  
1 9M1A PRO A 7  ? UNP P13053 ?   ?   'expression tag' 112 7  
1 9M1A ASN A 8  ? UNP P13053 ?   ?   'expression tag' 113 8  
1 9M1A SER A 9  ? UNP P13053 ?   ?   'expression tag' 114 9  
1 9M1A PRO A 10 ? UNP P13053 ?   ?   'expression tag' 115 10 
1 9M1A ?   A ?  ? UNP P13053 TYR 166 deletion         ?   11 
1 9M1A ?   A ?  ? UNP P13053 SER 167 deletion         ?   12 
1 9M1A ?   A ?  ? UNP P13053 PRO 168 deletion         ?   13 
1 9M1A ?   A ?  ? UNP P13053 ARG 169 deletion         ?   14 
1 9M1A ?   A ?  ? UNP P13053 PRO 170 deletion         ?   15 
1 9M1A ?   A ?  ? UNP P13053 THR 171 deletion         ?   16 
1 9M1A ?   A ?  ? UNP P13053 LEU 172 deletion         ?   17 
1 9M1A ?   A ?  ? UNP P13053 SER 173 deletion         ?   18 
1 9M1A ?   A ?  ? UNP P13053 PHE 174 deletion         ?   19 
1 9M1A ?   A ?  ? UNP P13053 SER 175 deletion         ?   20 
1 9M1A ?   A ?  ? UNP P13053 GLY 176 deletion         ?   21 
1 9M1A ?   A ?  ? UNP P13053 ASN 177 deletion         ?   22 
1 9M1A ?   A ?  ? UNP P13053 SER 178 deletion         ?   23 
1 9M1A ?   A ?  ? UNP P13053 SER 179 deletion         ?   24 
1 9M1A ?   A ?  ? UNP P13053 SER 180 deletion         ?   25 
1 9M1A ?   A ?  ? UNP P13053 SER 181 deletion         ?   26 
1 9M1A ?   A ?  ? UNP P13053 SER 182 deletion         ?   27 
1 9M1A ?   A ?  ? UNP P13053 SER 183 deletion         ?   28 
1 9M1A ?   A ?  ? UNP P13053 ASP 184 deletion         ?   29 
1 9M1A ?   A ?  ? UNP P13053 LEU 185 deletion         ?   30 
1 9M1A ?   A ?  ? UNP P13053 TYR 186 deletion         ?   31 
1 9M1A ?   A ?  ? UNP P13053 THR 187 deletion         ?   32 
1 9M1A ?   A ?  ? UNP P13053 THR 188 deletion         ?   33 
1 9M1A ?   A ?  ? UNP P13053 SER 189 deletion         ?   34 
1 9M1A ?   A ?  ? UNP P13053 LEU 190 deletion         ?   35 
1 9M1A ?   A ?  ? UNP P13053 ASP 191 deletion         ?   36 
1 9M1A ?   A ?  ? UNP P13053 MET 192 deletion         ?   37 
1 9M1A ?   A ?  ? UNP P13053 MET 193 deletion         ?   38 
1 9M1A ?   A ?  ? UNP P13053 GLU 194 deletion         ?   39 
1 9M1A ?   A ?  ? UNP P13053 PRO 195 deletion         ?   40 
1 9M1A ?   A ?  ? UNP P13053 SER 196 deletion         ?   41 
1 9M1A ?   A ?  ? UNP P13053 GLY 197 deletion         ?   42 
1 9M1A ?   A ?  ? UNP P13053 PHE 198 deletion         ?   43 
1 9M1A ?   A ?  ? UNP P13053 SER 199 deletion         ?   44 
1 9M1A ?   A ?  ? UNP P13053 ASN 200 deletion         ?   45 
1 9M1A ?   A ?  ? UNP P13053 LEU 201 deletion         ?   46 
1 9M1A ?   A ?  ? UNP P13053 ASP 202 deletion         ?   47 
1 9M1A ?   A ?  ? UNP P13053 LEU 203 deletion         ?   48 
1 9M1A ?   A ?  ? UNP P13053 ASN 204 deletion         ?   49 
1 9M1A ?   A ?  ? UNP P13053 GLY 205 deletion         ?   50 
1 9M1A ?   A ?  ? UNP P13053 GLU 206 deletion         ?   51 
1 9M1A ?   A ?  ? UNP P13053 ASP 207 deletion         ?   52 
1 9M1A ?   A ?  ? UNP P13053 SER 208 deletion         ?   53 
1 9M1A ?   A ?  ? UNP P13053 ASP 209 deletion         ?   54 
1 9M1A ?   A ?  ? UNP P13053 ASP 210 deletion         ?   55 
1 9M1A ?   A ?  ? UNP P13053 PRO 211 deletion         ?   56 
1 9M1A ?   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)' 1130  ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  11750 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 20  ? TYR A 38  ? SER A 125 TYR A 143 1 ? 19 
HELX_P HELX_P2  AA2 TYR A 42  ? PHE A 48  ? TYR A 147 PHE A 153 5 ? 7  
HELX_P HELX_P3  AA3 MET A 70  ? LYS A 90  ? MET A 222 LYS A 242 1 ? 21 
HELX_P HELX_P4  AA4 GLY A 94  ? LEU A 98  ? GLY A 246 LEU A 250 5 ? 5  
HELX_P HELX_P5  AA5 THR A 99  ? ASN A 120 ? THR A 251 ASN A 272 1 ? 22 
HELX_P HELX_P6  AA6 ASP A 140 ? LYS A 146 ? ASP A 292 LYS A 298 1 ? 7  
HELX_P HELX_P7  AA7 THR A 150 ? LEU A 167 ? THR A 302 LEU A 319 1 ? 18 
HELX_P HELX_P8  AA8 HIS A 170 ? VAL A 183 ? HIS A 322 VAL A 335 1 ? 14 
HELX_P HELX_P9  AA9 ASP A 192 ? HIS A 215 ? ASP A 344 HIS A 367 1 ? 24 
HELX_P HELX_P10 AB1 GLN A 222 ? GLN A 251 ? GLN A 374 GLN A 403 1 ? 30 
HELX_P HELX_P11 AB2 GLN A 251 ? MET A 256 ? GLN A 403 MET A 408 1 ? 6  
HELX_P HELX_P12 AB3 THR A 259 ? GLY A 267 ? THR A 411 GLY A 419 1 ? 9  
HELX_P HELX_P13 AB4 HIS B 3   ? 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       3.69 
# 
_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                   9M1A 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    VAL 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     335 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    B 
_pdbx_validate_torsion.phi             -94.29 
_pdbx_validate_torsion.psi             57.99 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 19.0862813724 0.371085501852 19.2038845438 0.213553859734 ? -0.0215014900123 ? -0.018442285987  ? 
0.213344079364 ? -0.020828540885  ? 0.20076964873  ? 3.17278591799 ? 0.478129281251 ? 0.0561232886723 ? 1.15967946992 ? 
-0.0532571987256 ? 1.39336879583  ? 0.0880282127833 ? 0.00491531710307 ? -0.151325938371 ? 0.00250048938395 ? 0.00959523132775 ? 
-0.0351947164295 ? -0.110810553678 ? 0.0999026592955 ? -0.0733671663059 ? 
2 'X-RAY DIFFRACTION' ? refined 5.52668090153 -10.4387341166 11.0649910331 0.283079160077 ? 0.0394408043195  ? 0.00841663560703 ? 
0.409322751595 ? -0.0927631004628 ? 0.413511213266 ? 5.91175664372 ? 3.53890162394  ? 0.117203941177  ? 5.13353302305 ? 
0.774435397613   ? 0.189923447841 ? 0.0122539288812 ? 0.242018098281   ? -0.58933727262  ? 0.0443666911676  ? -0.171573257311  ? 
-0.18521215318   ? 0.281811766902  ? 0.101286786031  ? 0.120051649211   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 'Chain A' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 'Chain C' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 106 ? A GLY 1   
2  1 Y 1 A SER 107 ? A SER 2   
3  1 Y 1 A HIS 108 ? A HIS 3   
4  1 Y 1 A MET 109 ? A MET 4   
5  1 Y 1 A GLY 110 ? A GLY 5   
6  1 Y 1 A SER 111 ? A SER 6   
7  1 Y 1 A PRO 112 ? A PRO 7   
8  1 Y 1 A ASN 113 ? A ASN 8   
9  1 Y 1 A SER 114 ? A SER 9   
10 1 Y 1 A PRO 115 ? A PRO 10  
11 1 Y 1 A LEU 116 ? A LEU 11  
12 1 Y 1 A LYS 117 ? A LYS 12  
13 1 Y 1 A ASP 118 ? A ASP 13  
14 1 Y 1 A SER 119 ? A SER 14  
15 1 Y 1 A LEU 120 ? A LEU 15  
16 1 Y 1 A ARG 121 ? A ARG 16  
17 1 Y 1 A PRO 122 ? A PRO 17  
18 1 Y 1 A ASP 207 ? A ASP 55  
19 1 Y 1 A GLY 208 ? A GLY 56  
20 1 Y 1 A SER 209 ? A SER 57  
21 1 Y 1 A THR 210 ? A THR 58  
22 1 Y 1 A GLY 211 ? A GLY 59  
23 1 Y 1 A SER 212 ? A SER 60  
24 1 Y 1 A VAL 213 ? A VAL 61  
25 1 Y 1 A THR 214 ? A THR 62  
26 1 Y 1 A LEU 215 ? A LEU 63  
27 1 Y 1 A ASP 216 ? A ASP 64  
28 1 Y 1 A LEU 217 ? A LEU 65  
29 1 Y 1 A GLU 421 ? A GLU 269 
30 1 Y 1 A ILE 422 ? A ILE 270 
31 1 Y 1 A SER 423 ? A SER 271 
32 1 Y 1 C ASP 636 ? B ASP 12  
33 1 Y 1 C ASN 637 ? B ASN 13  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1L78 C10  C  N N 1   
A1L78 C13  C  Y N 2   
A1L78 C15  C  Y N 3   
A1L78 C20  C  N N 4   
A1L78 C21  C  N N 5   
A1L78 C22  C  N N 6   
A1L78 C26  C  N S 7   
A1L78 C28  C  N N 8   
A1L78 C01  C  Y N 9   
A1L78 C02  C  Y N 10  
A1L78 C03  C  Y N 11  
A1L78 C04  C  Y N 12  
A1L78 C05  C  Y N 13  
A1L78 C06  C  Y N 14  
A1L78 C09  C  Y N 15  
A1L78 C11  C  N N 16  
A1L78 C12  C  Y N 17  
A1L78 C14  C  Y N 18  
A1L78 C16  C  Y N 19  
A1L78 C18  C  N N 20  
A1L78 C19  C  N N 21  
A1L78 C23  C  N N 22  
A1L78 C25  C  N N 23  
A1L78 C29  C  N N 24  
A1L78 C30  C  N N 25  
A1L78 C33  C  N N 26  
A1L78 C34  C  N N 27  
A1L78 C35  C  N N 28  
A1L78 C36  C  N N 29  
A1L78 O07  O  N N 30  
A1L78 O17  O  N N 31  
A1L78 O24  O  N N 32  
A1L78 O27  O  N N 33  
A1L78 O31  O  N N 34  
A1L78 O32  O  N N 35  
A1L78 SI08 SI N N 36  
A1L78 H102 H  N N 37  
A1L78 H101 H  N N 38  
A1L78 H151 H  N N 39  
A1L78 H201 H  N N 40  
A1L78 H202 H  N N 41  
A1L78 H211 H  N N 42  
A1L78 H212 H  N N 43  
A1L78 H213 H  N N 44  
A1L78 H222 H  N N 45  
A1L78 H221 H  N N 46  
A1L78 H261 H  N N 47  
A1L78 H282 H  N N 48  
A1L78 H281 H  N N 49  
A1L78 H011 H  N N 50  
A1L78 H041 H  N N 51  
A1L78 H061 H  N N 52  
A1L78 H111 H  N N 53  
A1L78 H112 H  N N 54  
A1L78 H121 H  N N 55  
A1L78 H161 H  N N 56  
A1L78 H181 H  N N 57  
A1L78 H182 H  N N 58  
A1L78 H233 H  N N 59  
A1L78 H231 H  N N 60  
A1L78 H232 H  N N 61  
A1L78 H251 H  N N 62  
A1L78 H252 H  N N 63  
A1L78 H292 H  N N 64  
A1L78 H291 H  N N 65  
A1L78 H331 H  N N 66  
A1L78 H332 H  N N 67  
A1L78 H333 H  N N 68  
A1L78 H342 H  N N 69  
A1L78 H341 H  N N 70  
A1L78 H343 H  N N 71  
A1L78 H352 H  N N 72  
A1L78 H353 H  N N 73  
A1L78 H351 H  N N 74  
A1L78 H361 H  N N 75  
A1L78 H363 H  N N 76  
A1L78 H362 H  N N 77  
A1L78 H241 H  N N 78  
A1L78 H271 H  N N 79  
A1L78 H1   H  N N 80  
ALA   N    N  N N 81  
ALA   CA   C  N S 82  
ALA   C    C  N N 83  
ALA   O    O  N N 84  
ALA   CB   C  N N 85  
ALA   OXT  O  N N 86  
ALA   H    H  N N 87  
ALA   H2   H  N N 88  
ALA   HA   H  N N 89  
ALA   HB1  H  N N 90  
ALA   HB2  H  N N 91  
ALA   HB3  H  N N 92  
ALA   HXT  H  N N 93  
ARG   N    N  N N 94  
ARG   CA   C  N S 95  
ARG   C    C  N N 96  
ARG   O    O  N N 97  
ARG   CB   C  N N 98  
ARG   CG   C  N N 99  
ARG   CD   C  N N 100 
ARG   NE   N  N N 101 
ARG   CZ   C  N N 102 
ARG   NH1  N  N N 103 
ARG   NH2  N  N N 104 
ARG   OXT  O  N N 105 
ARG   H    H  N N 106 
ARG   H2   H  N N 107 
ARG   HA   H  N N 108 
ARG   HB2  H  N N 109 
ARG   HB3  H  N N 110 
ARG   HG2  H  N N 111 
ARG   HG3  H  N N 112 
ARG   HD2  H  N N 113 
ARG   HD3  H  N N 114 
ARG   HE   H  N N 115 
ARG   HH11 H  N N 116 
ARG   HH12 H  N N 117 
ARG   HH21 H  N N 118 
ARG   HH22 H  N N 119 
ARG   HXT  H  N N 120 
ASN   N    N  N N 121 
ASN   CA   C  N S 122 
ASN   C    C  N N 123 
ASN   O    O  N N 124 
ASN   CB   C  N N 125 
ASN   CG   C  N N 126 
ASN   OD1  O  N N 127 
ASN   ND2  N  N N 128 
ASN   OXT  O  N N 129 
ASN   H    H  N N 130 
ASN   H2   H  N N 131 
ASN   HA   H  N N 132 
ASN   HB2  H  N N 133 
ASN   HB3  H  N N 134 
ASN   HD21 H  N N 135 
ASN   HD22 H  N N 136 
ASN   HXT  H  N N 137 
ASP   N    N  N N 138 
ASP   CA   C  N S 139 
ASP   C    C  N N 140 
ASP   O    O  N N 141 
ASP   CB   C  N N 142 
ASP   CG   C  N N 143 
ASP   OD1  O  N N 144 
ASP   OD2  O  N N 145 
ASP   OXT  O  N N 146 
ASP   H    H  N N 147 
ASP   H2   H  N N 148 
ASP   HA   H  N N 149 
ASP   HB2  H  N N 150 
ASP   HB3  H  N N 151 
ASP   HD2  H  N N 152 
ASP   HXT  H  N N 153 
CYS   N    N  N N 154 
CYS   CA   C  N R 155 
CYS   C    C  N N 156 
CYS   O    O  N N 157 
CYS   CB   C  N N 158 
CYS   SG   S  N N 159 
CYS   OXT  O  N N 160 
CYS   H    H  N N 161 
CYS   H2   H  N N 162 
CYS   HA   H  N N 163 
CYS   HB2  H  N N 164 
CYS   HB3  H  N N 165 
CYS   HG   H  N N 166 
CYS   HXT  H  N N 167 
GLN   N    N  N N 168 
GLN   CA   C  N S 169 
GLN   C    C  N N 170 
GLN   O    O  N N 171 
GLN   CB   C  N N 172 
GLN   CG   C  N N 173 
GLN   CD   C  N N 174 
GLN   OE1  O  N N 175 
GLN   NE2  N  N N 176 
GLN   OXT  O  N N 177 
GLN   H    H  N N 178 
GLN   H2   H  N N 179 
GLN   HA   H  N N 180 
GLN   HB2  H  N N 181 
GLN   HB3  H  N N 182 
GLN   HG2  H  N N 183 
GLN   HG3  H  N N 184 
GLN   HE21 H  N N 185 
GLN   HE22 H  N N 186 
GLN   HXT  H  N N 187 
GLU   N    N  N N 188 
GLU   CA   C  N S 189 
GLU   C    C  N N 190 
GLU   O    O  N N 191 
GLU   CB   C  N N 192 
GLU   CG   C  N N 193 
GLU   CD   C  N N 194 
GLU   OE1  O  N N 195 
GLU   OE2  O  N N 196 
GLU   OXT  O  N N 197 
GLU   H    H  N N 198 
GLU   H2   H  N N 199 
GLU   HA   H  N N 200 
GLU   HB2  H  N N 201 
GLU   HB3  H  N N 202 
GLU   HG2  H  N N 203 
GLU   HG3  H  N N 204 
GLU   HE2  H  N N 205 
GLU   HXT  H  N N 206 
GLY   N    N  N N 207 
GLY   CA   C  N N 208 
GLY   C    C  N N 209 
GLY   O    O  N N 210 
GLY   OXT  O  N N 211 
GLY   H    H  N N 212 
GLY   H2   H  N N 213 
GLY   HA2  H  N N 214 
GLY   HA3  H  N N 215 
GLY   HXT  H  N N 216 
HIS   N    N  N N 217 
HIS   CA   C  N S 218 
HIS   C    C  N N 219 
HIS   O    O  N N 220 
HIS   CB   C  N N 221 
HIS   CG   C  Y N 222 
HIS   ND1  N  Y N 223 
HIS   CD2  C  Y N 224 
HIS   CE1  C  Y N 225 
HIS   NE2  N  Y N 226 
HIS   OXT  O  N N 227 
HIS   H    H  N N 228 
HIS   H2   H  N N 229 
HIS   HA   H  N N 230 
HIS   HB2  H  N N 231 
HIS   HB3  H  N N 232 
HIS   HD1  H  N N 233 
HIS   HD2  H  N N 234 
HIS   HE1  H  N N 235 
HIS   HE2  H  N N 236 
HIS   HXT  H  N N 237 
HOH   O    O  N N 238 
HOH   H1   H  N N 239 
HOH   H2   H  N N 240 
ILE   N    N  N N 241 
ILE   CA   C  N S 242 
ILE   C    C  N N 243 
ILE   O    O  N N 244 
ILE   CB   C  N S 245 
ILE   CG1  C  N N 246 
ILE   CG2  C  N N 247 
ILE   CD1  C  N N 248 
ILE   OXT  O  N N 249 
ILE   H    H  N N 250 
ILE   H2   H  N N 251 
ILE   HA   H  N N 252 
ILE   HB   H  N N 253 
ILE   HG12 H  N N 254 
ILE   HG13 H  N N 255 
ILE   HG21 H  N N 256 
ILE   HG22 H  N N 257 
ILE   HG23 H  N N 258 
ILE   HD11 H  N N 259 
ILE   HD12 H  N N 260 
ILE   HD13 H  N N 261 
ILE   HXT  H  N N 262 
LEU   N    N  N N 263 
LEU   CA   C  N S 264 
LEU   C    C  N N 265 
LEU   O    O  N N 266 
LEU   CB   C  N N 267 
LEU   CG   C  N N 268 
LEU   CD1  C  N N 269 
LEU   CD2  C  N N 270 
LEU   OXT  O  N N 271 
LEU   H    H  N N 272 
LEU   H2   H  N N 273 
LEU   HA   H  N N 274 
LEU   HB2  H  N N 275 
LEU   HB3  H  N N 276 
LEU   HG   H  N N 277 
LEU   HD11 H  N N 278 
LEU   HD12 H  N N 279 
LEU   HD13 H  N N 280 
LEU   HD21 H  N N 281 
LEU   HD22 H  N N 282 
LEU   HD23 H  N N 283 
LEU   HXT  H  N N 284 
LYS   N    N  N N 285 
LYS   CA   C  N S 286 
LYS   C    C  N N 287 
LYS   O    O  N N 288 
LYS   CB   C  N N 289 
LYS   CG   C  N N 290 
LYS   CD   C  N N 291 
LYS   CE   C  N N 292 
LYS   NZ   N  N N 293 
LYS   OXT  O  N N 294 
LYS   H    H  N N 295 
LYS   H2   H  N N 296 
LYS   HA   H  N N 297 
LYS   HB2  H  N N 298 
LYS   HB3  H  N N 299 
LYS   HG2  H  N N 300 
LYS   HG3  H  N N 301 
LYS   HD2  H  N N 302 
LYS   HD3  H  N N 303 
LYS   HE2  H  N N 304 
LYS   HE3  H  N N 305 
LYS   HZ1  H  N N 306 
LYS   HZ2  H  N N 307 
LYS   HZ3  H  N N 308 
LYS   HXT  H  N N 309 
MET   N    N  N N 310 
MET   CA   C  N S 311 
MET   C    C  N N 312 
MET   O    O  N N 313 
MET   CB   C  N N 314 
MET   CG   C  N N 315 
MET   SD   S  N N 316 
MET   CE   C  N N 317 
MET   OXT  O  N N 318 
MET   H    H  N N 319 
MET   H2   H  N N 320 
MET   HA   H  N N 321 
MET   HB2  H  N N 322 
MET   HB3  H  N N 323 
MET   HG2  H  N N 324 
MET   HG3  H  N N 325 
MET   HE1  H  N N 326 
MET   HE2  H  N N 327 
MET   HE3  H  N N 328 
MET   HXT  H  N N 329 
PHE   N    N  N N 330 
PHE   CA   C  N S 331 
PHE   C    C  N N 332 
PHE   O    O  N N 333 
PHE   CB   C  N N 334 
PHE   CG   C  Y N 335 
PHE   CD1  C  Y N 336 
PHE   CD2  C  Y N 337 
PHE   CE1  C  Y N 338 
PHE   CE2  C  Y N 339 
PHE   CZ   C  Y N 340 
PHE   OXT  O  N N 341 
PHE   H    H  N N 342 
PHE   H2   H  N N 343 
PHE   HA   H  N N 344 
PHE   HB2  H  N N 345 
PHE   HB3  H  N N 346 
PHE   HD1  H  N N 347 
PHE   HD2  H  N N 348 
PHE   HE1  H  N N 349 
PHE   HE2  H  N N 350 
PHE   HZ   H  N N 351 
PHE   HXT  H  N N 352 
PRO   N    N  N N 353 
PRO   CA   C  N S 354 
PRO   C    C  N N 355 
PRO   O    O  N N 356 
PRO   CB   C  N N 357 
PRO   CG   C  N N 358 
PRO   CD   C  N N 359 
PRO   OXT  O  N N 360 
PRO   H    H  N N 361 
PRO   HA   H  N N 362 
PRO   HB2  H  N N 363 
PRO   HB3  H  N N 364 
PRO   HG2  H  N N 365 
PRO   HG3  H  N N 366 
PRO   HD2  H  N N 367 
PRO   HD3  H  N N 368 
PRO   HXT  H  N N 369 
SER   N    N  N N 370 
SER   CA   C  N S 371 
SER   C    C  N N 372 
SER   O    O  N N 373 
SER   CB   C  N N 374 
SER   OG   O  N N 375 
SER   OXT  O  N N 376 
SER   H    H  N N 377 
SER   H2   H  N N 378 
SER   HA   H  N N 379 
SER   HB2  H  N N 380 
SER   HB3  H  N N 381 
SER   HG   H  N N 382 
SER   HXT  H  N N 383 
THR   N    N  N N 384 
THR   CA   C  N S 385 
THR   C    C  N N 386 
THR   O    O  N N 387 
THR   CB   C  N R 388 
THR   OG1  O  N N 389 
THR   CG2  C  N N 390 
THR   OXT  O  N N 391 
THR   H    H  N N 392 
THR   H2   H  N N 393 
THR   HA   H  N N 394 
THR   HB   H  N N 395 
THR   HG1  H  N N 396 
THR   HG21 H  N N 397 
THR   HG22 H  N N 398 
THR   HG23 H  N N 399 
THR   HXT  H  N N 400 
TRP   N    N  N N 401 
TRP   CA   C  N S 402 
TRP   C    C  N N 403 
TRP   O    O  N N 404 
TRP   CB   C  N N 405 
TRP   CG   C  Y N 406 
TRP   CD1  C  Y N 407 
TRP   CD2  C  Y N 408 
TRP   NE1  N  Y N 409 
TRP   CE2  C  Y N 410 
TRP   CE3  C  Y N 411 
TRP   CZ2  C  Y N 412 
TRP   CZ3  C  Y N 413 
TRP   CH2  C  Y N 414 
TRP   OXT  O  N N 415 
TRP   H    H  N N 416 
TRP   H2   H  N N 417 
TRP   HA   H  N N 418 
TRP   HB2  H  N N 419 
TRP   HB3  H  N N 420 
TRP   HD1  H  N N 421 
TRP   HE1  H  N N 422 
TRP   HE3  H  N N 423 
TRP   HZ2  H  N N 424 
TRP   HZ3  H  N N 425 
TRP   HH2  H  N N 426 
TRP   HXT  H  N N 427 
TYR   N    N  N N 428 
TYR   CA   C  N S 429 
TYR   C    C  N N 430 
TYR   O    O  N N 431 
TYR   CB   C  N N 432 
TYR   CG   C  Y N 433 
TYR   CD1  C  Y N 434 
TYR   CD2  C  Y N 435 
TYR   CE1  C  Y N 436 
TYR   CE2  C  Y N 437 
TYR   CZ   C  Y N 438 
TYR   OH   O  N N 439 
TYR   OXT  O  N N 440 
TYR   H    H  N N 441 
TYR   H2   H  N N 442 
TYR   HA   H  N N 443 
TYR   HB2  H  N N 444 
TYR   HB3  H  N N 445 
TYR   HD1  H  N N 446 
TYR   HD2  H  N N 447 
TYR   HE1  H  N N 448 
TYR   HE2  H  N N 449 
TYR   HH   H  N N 450 
TYR   HXT  H  N N 451 
VAL   N    N  N N 452 
VAL   CA   C  N S 453 
VAL   C    C  N N 454 
VAL   O    O  N N 455 
VAL   CB   C  N N 456 
VAL   CG1  C  N N 457 
VAL   CG2  C  N N 458 
VAL   OXT  O  N N 459 
VAL   H    H  N N 460 
VAL   H2   H  N N 461 
VAL   HA   H  N N 462 
VAL   HB   H  N N 463 
VAL   HG11 H  N N 464 
VAL   HG12 H  N N 465 
VAL   HG13 H  N N 466 
VAL   HG21 H  N N 467 
VAL   HG22 H  N N 468 
VAL   HG23 H  N N 469 
VAL   HXT  H  N N 470 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1L78 C01  C02  doub Y N 1   
A1L78 C01  C06  sing Y N 2   
A1L78 C02  C03  sing Y N 3   
A1L78 C02  O07  sing N N 4   
A1L78 C03  C04  doub Y N 5   
A1L78 C03  C33  sing N N 6   
A1L78 C04  C05  sing Y N 7   
A1L78 C05  C06  doub Y N 8   
A1L78 C05  SI08 sing N N 9   
A1L78 O07  C25  sing N N 10  
A1L78 SI08 C09  sing N N 11  
A1L78 SI08 C10  sing N N 12  
A1L78 SI08 C11  sing N N 13  
A1L78 C09  C12  doub Y N 14  
A1L78 C09  C16  sing Y N 15  
A1L78 C10  C35  sing N N 16  
A1L78 C11  C36  sing N N 17  
A1L78 C12  C13  sing Y N 18  
A1L78 C13  C14  doub Y N 19  
A1L78 C13  C34  sing N N 20  
A1L78 C14  C15  sing Y N 21  
A1L78 C14  O17  sing N N 22  
A1L78 C15  C16  doub Y N 23  
A1L78 O17  C18  sing N N 24  
A1L78 C18  C19  sing N N 25  
A1L78 C19  C20  sing N N 26  
A1L78 C19  C22  sing N N 27  
A1L78 C19  O24  sing N N 28  
A1L78 C20  C21  sing N N 29  
A1L78 C22  C23  sing N N 30  
A1L78 C25  C26  sing N N 31  
A1L78 C26  O27  sing N N 32  
A1L78 C26  C28  sing N N 33  
A1L78 C28  C29  sing N N 34  
A1L78 C29  C30  sing N N 35  
A1L78 C30  O31  doub N N 36  
A1L78 C30  O32  sing N N 37  
A1L78 C10  H102 sing N N 38  
A1L78 C10  H101 sing N N 39  
A1L78 C15  H151 sing N N 40  
A1L78 C20  H201 sing N N 41  
A1L78 C20  H202 sing N N 42  
A1L78 C21  H211 sing N N 43  
A1L78 C21  H212 sing N N 44  
A1L78 C21  H213 sing N N 45  
A1L78 C22  H222 sing N N 46  
A1L78 C22  H221 sing N N 47  
A1L78 C26  H261 sing N N 48  
A1L78 C28  H282 sing N N 49  
A1L78 C28  H281 sing N N 50  
A1L78 C01  H011 sing N N 51  
A1L78 C04  H041 sing N N 52  
A1L78 C06  H061 sing N N 53  
A1L78 C11  H111 sing N N 54  
A1L78 C11  H112 sing N N 55  
A1L78 C12  H121 sing N N 56  
A1L78 C16  H161 sing N N 57  
A1L78 C18  H181 sing N N 58  
A1L78 C18  H182 sing N N 59  
A1L78 C23  H233 sing N N 60  
A1L78 C23  H231 sing N N 61  
A1L78 C23  H232 sing N N 62  
A1L78 C25  H251 sing N N 63  
A1L78 C25  H252 sing N N 64  
A1L78 C29  H292 sing N N 65  
A1L78 C29  H291 sing N N 66  
A1L78 C33  H331 sing N N 67  
A1L78 C33  H332 sing N N 68  
A1L78 C33  H333 sing N N 69  
A1L78 C34  H342 sing N N 70  
A1L78 C34  H341 sing N N 71  
A1L78 C34  H343 sing N N 72  
A1L78 C35  H352 sing N N 73  
A1L78 C35  H353 sing N N 74  
A1L78 C35  H351 sing N N 75  
A1L78 C36  H361 sing N N 76  
A1L78 C36  H363 sing N N 77  
A1L78 C36  H362 sing N N 78  
A1L78 O24  H241 sing N N 79  
A1L78 O27  H271 sing N N 80  
A1L78 O32  H1   sing N N 81  
ALA   N    CA   sing N N 82  
ALA   N    H    sing N N 83  
ALA   N    H2   sing N N 84  
ALA   CA   C    sing N N 85  
ALA   CA   CB   sing N N 86  
ALA   CA   HA   sing N N 87  
ALA   C    O    doub N N 88  
ALA   C    OXT  sing N N 89  
ALA   CB   HB1  sing N N 90  
ALA   CB   HB2  sing N N 91  
ALA   CB   HB3  sing N N 92  
ALA   OXT  HXT  sing N N 93  
ARG   N    CA   sing N N 94  
ARG   N    H    sing N N 95  
ARG   N    H2   sing N N 96  
ARG   CA   C    sing N N 97  
ARG   CA   CB   sing N N 98  
ARG   CA   HA   sing N N 99  
ARG   C    O    doub N N 100 
ARG   C    OXT  sing N N 101 
ARG   CB   CG   sing N N 102 
ARG   CB   HB2  sing N N 103 
ARG   CB   HB3  sing N N 104 
ARG   CG   CD   sing N N 105 
ARG   CG   HG2  sing N N 106 
ARG   CG   HG3  sing N N 107 
ARG   CD   NE   sing N N 108 
ARG   CD   HD2  sing N N 109 
ARG   CD   HD3  sing N N 110 
ARG   NE   CZ   sing N N 111 
ARG   NE   HE   sing N N 112 
ARG   CZ   NH1  sing N N 113 
ARG   CZ   NH2  doub N N 114 
ARG   NH1  HH11 sing N N 115 
ARG   NH1  HH12 sing N N 116 
ARG   NH2  HH21 sing N N 117 
ARG   NH2  HH22 sing N N 118 
ARG   OXT  HXT  sing N N 119 
ASN   N    CA   sing N N 120 
ASN   N    H    sing N N 121 
ASN   N    H2   sing N N 122 
ASN   CA   C    sing N N 123 
ASN   CA   CB   sing N N 124 
ASN   CA   HA   sing N N 125 
ASN   C    O    doub N N 126 
ASN   C    OXT  sing N N 127 
ASN   CB   CG   sing N N 128 
ASN   CB   HB2  sing N N 129 
ASN   CB   HB3  sing N N 130 
ASN   CG   OD1  doub N N 131 
ASN   CG   ND2  sing N N 132 
ASN   ND2  HD21 sing N N 133 
ASN   ND2  HD22 sing N N 134 
ASN   OXT  HXT  sing N N 135 
ASP   N    CA   sing N N 136 
ASP   N    H    sing N N 137 
ASP   N    H2   sing N N 138 
ASP   CA   C    sing N N 139 
ASP   CA   CB   sing N N 140 
ASP   CA   HA   sing N N 141 
ASP   C    O    doub N N 142 
ASP   C    OXT  sing N N 143 
ASP   CB   CG   sing N N 144 
ASP   CB   HB2  sing N N 145 
ASP   CB   HB3  sing N N 146 
ASP   CG   OD1  doub N N 147 
ASP   CG   OD2  sing N N 148 
ASP   OD2  HD2  sing N N 149 
ASP   OXT  HXT  sing N N 150 
CYS   N    CA   sing N N 151 
CYS   N    H    sing N N 152 
CYS   N    H2   sing N N 153 
CYS   CA   C    sing N N 154 
CYS   CA   CB   sing N N 155 
CYS   CA   HA   sing N N 156 
CYS   C    O    doub N N 157 
CYS   C    OXT  sing N N 158 
CYS   CB   SG   sing N N 159 
CYS   CB   HB2  sing N N 160 
CYS   CB   HB3  sing N N 161 
CYS   SG   HG   sing N N 162 
CYS   OXT  HXT  sing N N 163 
GLN   N    CA   sing N N 164 
GLN   N    H    sing N N 165 
GLN   N    H2   sing N N 166 
GLN   CA   C    sing N N 167 
GLN   CA   CB   sing N N 168 
GLN   CA   HA   sing N N 169 
GLN   C    O    doub N N 170 
GLN   C    OXT  sing N N 171 
GLN   CB   CG   sing N N 172 
GLN   CB   HB2  sing N N 173 
GLN   CB   HB3  sing N N 174 
GLN   CG   CD   sing N N 175 
GLN   CG   HG2  sing N N 176 
GLN   CG   HG3  sing N N 177 
GLN   CD   OE1  doub N N 178 
GLN   CD   NE2  sing N N 179 
GLN   NE2  HE21 sing N N 180 
GLN   NE2  HE22 sing N N 181 
GLN   OXT  HXT  sing N N 182 
GLU   N    CA   sing N N 183 
GLU   N    H    sing N N 184 
GLU   N    H2   sing N N 185 
GLU   CA   C    sing N N 186 
GLU   CA   CB   sing N N 187 
GLU   CA   HA   sing N N 188 
GLU   C    O    doub N N 189 
GLU   C    OXT  sing N N 190 
GLU   CB   CG   sing N N 191 
GLU   CB   HB2  sing N N 192 
GLU   CB   HB3  sing N N 193 
GLU   CG   CD   sing N N 194 
GLU   CG   HG2  sing N N 195 
GLU   CG   HG3  sing N N 196 
GLU   CD   OE1  doub N N 197 
GLU   CD   OE2  sing N N 198 
GLU   OE2  HE2  sing N N 199 
GLU   OXT  HXT  sing N N 200 
GLY   N    CA   sing N N 201 
GLY   N    H    sing N N 202 
GLY   N    H2   sing N N 203 
GLY   CA   C    sing N N 204 
GLY   CA   HA2  sing N N 205 
GLY   CA   HA3  sing N N 206 
GLY   C    O    doub N N 207 
GLY   C    OXT  sing N N 208 
GLY   OXT  HXT  sing N N 209 
HIS   N    CA   sing N N 210 
HIS   N    H    sing N N 211 
HIS   N    H2   sing N N 212 
HIS   CA   C    sing N N 213 
HIS   CA   CB   sing N N 214 
HIS   CA   HA   sing N N 215 
HIS   C    O    doub N N 216 
HIS   C    OXT  sing N N 217 
HIS   CB   CG   sing N N 218 
HIS   CB   HB2  sing N N 219 
HIS   CB   HB3  sing N N 220 
HIS   CG   ND1  sing Y N 221 
HIS   CG   CD2  doub Y N 222 
HIS   ND1  CE1  doub Y N 223 
HIS   ND1  HD1  sing N N 224 
HIS   CD2  NE2  sing Y N 225 
HIS   CD2  HD2  sing N N 226 
HIS   CE1  NE2  sing Y N 227 
HIS   CE1  HE1  sing N N 228 
HIS   NE2  HE2  sing N N 229 
HIS   OXT  HXT  sing N N 230 
HOH   O    H1   sing N N 231 
HOH   O    H2   sing N N 232 
ILE   N    CA   sing N N 233 
ILE   N    H    sing N N 234 
ILE   N    H2   sing N N 235 
ILE   CA   C    sing N N 236 
ILE   CA   CB   sing N N 237 
ILE   CA   HA   sing N N 238 
ILE   C    O    doub N N 239 
ILE   C    OXT  sing N N 240 
ILE   CB   CG1  sing N N 241 
ILE   CB   CG2  sing N N 242 
ILE   CB   HB   sing N N 243 
ILE   CG1  CD1  sing N N 244 
ILE   CG1  HG12 sing N N 245 
ILE   CG1  HG13 sing N N 246 
ILE   CG2  HG21 sing N N 247 
ILE   CG2  HG22 sing N N 248 
ILE   CG2  HG23 sing N N 249 
ILE   CD1  HD11 sing N N 250 
ILE   CD1  HD12 sing N N 251 
ILE   CD1  HD13 sing N N 252 
ILE   OXT  HXT  sing N N 253 
LEU   N    CA   sing N N 254 
LEU   N    H    sing N N 255 
LEU   N    H2   sing N N 256 
LEU   CA   C    sing N N 257 
LEU   CA   CB   sing N N 258 
LEU   CA   HA   sing N N 259 
LEU   C    O    doub N N 260 
LEU   C    OXT  sing N N 261 
LEU   CB   CG   sing N N 262 
LEU   CB   HB2  sing N N 263 
LEU   CB   HB3  sing N N 264 
LEU   CG   CD1  sing N N 265 
LEU   CG   CD2  sing N N 266 
LEU   CG   HG   sing N N 267 
LEU   CD1  HD11 sing N N 268 
LEU   CD1  HD12 sing N N 269 
LEU   CD1  HD13 sing N N 270 
LEU   CD2  HD21 sing N N 271 
LEU   CD2  HD22 sing N N 272 
LEU   CD2  HD23 sing N N 273 
LEU   OXT  HXT  sing N N 274 
LYS   N    CA   sing N N 275 
LYS   N    H    sing N N 276 
LYS   N    H2   sing N N 277 
LYS   CA   C    sing N N 278 
LYS   CA   CB   sing N N 279 
LYS   CA   HA   sing N N 280 
LYS   C    O    doub N N 281 
LYS   C    OXT  sing N N 282 
LYS   CB   CG   sing N N 283 
LYS   CB   HB2  sing N N 284 
LYS   CB   HB3  sing N N 285 
LYS   CG   CD   sing N N 286 
LYS   CG   HG2  sing N N 287 
LYS   CG   HG3  sing N N 288 
LYS   CD   CE   sing N N 289 
LYS   CD   HD2  sing N N 290 
LYS   CD   HD3  sing N N 291 
LYS   CE   NZ   sing N N 292 
LYS   CE   HE2  sing N N 293 
LYS   CE   HE3  sing N N 294 
LYS   NZ   HZ1  sing N N 295 
LYS   NZ   HZ2  sing N N 296 
LYS   NZ   HZ3  sing N N 297 
LYS   OXT  HXT  sing N N 298 
MET   N    CA   sing N N 299 
MET   N    H    sing N N 300 
MET   N    H2   sing N N 301 
MET   CA   C    sing N N 302 
MET   CA   CB   sing N N 303 
MET   CA   HA   sing N N 304 
MET   C    O    doub N N 305 
MET   C    OXT  sing N N 306 
MET   CB   CG   sing N N 307 
MET   CB   HB2  sing N N 308 
MET   CB   HB3  sing N N 309 
MET   CG   SD   sing N N 310 
MET   CG   HG2  sing N N 311 
MET   CG   HG3  sing N N 312 
MET   SD   CE   sing N N 313 
MET   CE   HE1  sing N N 314 
MET   CE   HE2  sing N N 315 
MET   CE   HE3  sing N N 316 
MET   OXT  HXT  sing N N 317 
PHE   N    CA   sing N N 318 
PHE   N    H    sing N N 319 
PHE   N    H2   sing N N 320 
PHE   CA   C    sing N N 321 
PHE   CA   CB   sing N N 322 
PHE   CA   HA   sing N N 323 
PHE   C    O    doub N N 324 
PHE   C    OXT  sing N N 325 
PHE   CB   CG   sing N N 326 
PHE   CB   HB2  sing N N 327 
PHE   CB   HB3  sing N N 328 
PHE   CG   CD1  doub Y N 329 
PHE   CG   CD2  sing Y N 330 
PHE   CD1  CE1  sing Y N 331 
PHE   CD1  HD1  sing N N 332 
PHE   CD2  CE2  doub Y N 333 
PHE   CD2  HD2  sing N N 334 
PHE   CE1  CZ   doub Y N 335 
PHE   CE1  HE1  sing N N 336 
PHE   CE2  CZ   sing Y N 337 
PHE   CE2  HE2  sing N N 338 
PHE   CZ   HZ   sing N N 339 
PHE   OXT  HXT  sing N N 340 
PRO   N    CA   sing N N 341 
PRO   N    CD   sing N N 342 
PRO   N    H    sing N N 343 
PRO   CA   C    sing N N 344 
PRO   CA   CB   sing N N 345 
PRO   CA   HA   sing N N 346 
PRO   C    O    doub N N 347 
PRO   C    OXT  sing N N 348 
PRO   CB   CG   sing N N 349 
PRO   CB   HB2  sing N N 350 
PRO   CB   HB3  sing N N 351 
PRO   CG   CD   sing N N 352 
PRO   CG   HG2  sing N N 353 
PRO   CG   HG3  sing N N 354 
PRO   CD   HD2  sing N N 355 
PRO   CD   HD3  sing N N 356 
PRO   OXT  HXT  sing N N 357 
SER   N    CA   sing N N 358 
SER   N    H    sing N N 359 
SER   N    H2   sing N N 360 
SER   CA   C    sing N N 361 
SER   CA   CB   sing N N 362 
SER   CA   HA   sing N N 363 
SER   C    O    doub N N 364 
SER   C    OXT  sing N N 365 
SER   CB   OG   sing N N 366 
SER   CB   HB2  sing N N 367 
SER   CB   HB3  sing N N 368 
SER   OG   HG   sing N N 369 
SER   OXT  HXT  sing N N 370 
THR   N    CA   sing N N 371 
THR   N    H    sing N N 372 
THR   N    H2   sing N N 373 
THR   CA   C    sing N N 374 
THR   CA   CB   sing N N 375 
THR   CA   HA   sing N N 376 
THR   C    O    doub N N 377 
THR   C    OXT  sing N N 378 
THR   CB   OG1  sing N N 379 
THR   CB   CG2  sing N N 380 
THR   CB   HB   sing N N 381 
THR   OG1  HG1  sing N N 382 
THR   CG2  HG21 sing N N 383 
THR   CG2  HG22 sing N N 384 
THR   CG2  HG23 sing N N 385 
THR   OXT  HXT  sing N N 386 
TRP   N    CA   sing N N 387 
TRP   N    H    sing N N 388 
TRP   N    H2   sing N N 389 
TRP   CA   C    sing N N 390 
TRP   CA   CB   sing N N 391 
TRP   CA   HA   sing N N 392 
TRP   C    O    doub N N 393 
TRP   C    OXT  sing N N 394 
TRP   CB   CG   sing N N 395 
TRP   CB   HB2  sing N N 396 
TRP   CB   HB3  sing N N 397 
TRP   CG   CD1  doub Y N 398 
TRP   CG   CD2  sing Y N 399 
TRP   CD1  NE1  sing Y N 400 
TRP   CD1  HD1  sing N N 401 
TRP   CD2  CE2  doub Y N 402 
TRP   CD2  CE3  sing Y N 403 
TRP   NE1  CE2  sing Y N 404 
TRP   NE1  HE1  sing N N 405 
TRP   CE2  CZ2  sing Y N 406 
TRP   CE3  CZ3  doub Y N 407 
TRP   CE3  HE3  sing N N 408 
TRP   CZ2  CH2  doub Y N 409 
TRP   CZ2  HZ2  sing N N 410 
TRP   CZ3  CH2  sing Y N 411 
TRP   CZ3  HZ3  sing N N 412 
TRP   CH2  HH2  sing N N 413 
TRP   OXT  HXT  sing N N 414 
TYR   N    CA   sing N N 415 
TYR   N    H    sing N N 416 
TYR   N    H2   sing N N 417 
TYR   CA   C    sing N N 418 
TYR   CA   CB   sing N N 419 
TYR   CA   HA   sing N N 420 
TYR   C    O    doub N N 421 
TYR   C    OXT  sing N N 422 
TYR   CB   CG   sing N N 423 
TYR   CB   HB2  sing N N 424 
TYR   CB   HB3  sing N N 425 
TYR   CG   CD1  doub Y N 426 
TYR   CG   CD2  sing Y N 427 
TYR   CD1  CE1  sing Y N 428 
TYR   CD1  HD1  sing N N 429 
TYR   CD2  CE2  doub Y N 430 
TYR   CD2  HD2  sing N N 431 
TYR   CE1  CZ   doub Y N 432 
TYR   CE1  HE1  sing N N 433 
TYR   CE2  CZ   sing Y N 434 
TYR   CE2  HE2  sing N N 435 
TYR   CZ   OH   sing N N 436 
TYR   OH   HH   sing N N 437 
TYR   OXT  HXT  sing N N 438 
VAL   N    CA   sing N N 439 
VAL   N    H    sing N N 440 
VAL   N    H2   sing N N 441 
VAL   CA   C    sing N N 442 
VAL   CA   CB   sing N N 443 
VAL   CA   HA   sing N N 444 
VAL   C    O    doub N N 445 
VAL   C    OXT  sing N N 446 
VAL   CB   CG1  sing N N 447 
VAL   CB   CG2  sing N N 448 
VAL   CB   HB   sing N N 449 
VAL   CG1  HG11 sing N N 450 
VAL   CG1  HG12 sing N N 451 
VAL   CG1  HG13 sing N N 452 
VAL   CG2  HG21 sing N N 453 
VAL   CG2  HG22 sing N N 454 
VAL   CG2  HG23 sing N N 455 
VAL   OXT  HXT  sing N N 456 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2ZLC 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9M1A 
_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]   0.006481 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000713 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023932 
_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]   0.023798 
_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  ? 43.29000 -0.66200  2.11100  1.000 58.75326 ?  123 LYS   A N    1 
ATOM   2    C  CA   . LYS   A 1 18  ? 42.85000 -1.78200  2.93500  1.000 54.57538 ?  123 LYS   A CA   1 
ATOM   3    C  C    . LYS   A 1 18  ? 41.32900 -1.90900  2.97100  1.000 45.74706 ?  123 LYS   A C    1 
ATOM   4    O  O    . LYS   A 1 18  ? 40.79600 -3.01800  2.94700  1.000 52.62714 ?  123 LYS   A O    1 
ATOM   5    C  CB   . LYS   A 1 18  ? 43.39400 -1.64400  4.35700  1.000 42.71010 ?  123 LYS   A CB   1 
ATOM   6    C  CG   . LYS   A 1 18  ? 44.89000 -1.41100  4.41700  1.000 45.72510 ?  123 LYS   A CG   1 
ATOM   7    C  CD   . LYS   A 1 18  ? 45.50200 -2.02500  5.66400  1.000 55.01735 ?  123 LYS   A CD   1 
ATOM   8    C  CE   . LYS   A 1 18  ? 46.75200 -2.82200  5.31900  1.000 49.80411 ?  123 LYS   A CE   1 
ATOM   9    N  NZ   . LYS   A 1 18  ? 46.48800 -3.79700  4.22400  1.000 50.03921 ?  123 LYS   A NZ   1 
ATOM   10   N  N    . LEU   A 1 19  ? 40.63400 -0.77500  3.04500  1.000 47.93962 ?  124 LEU   A N    1 
ATOM   11   C  CA   . LEU   A 1 19  ? 39.17500 -0.76600  2.98600  1.000 46.47032 ?  124 LEU   A CA   1 
ATOM   12   C  C    . LEU   A 1 19  ? 38.75000 -1.06300  1.55300  1.000 49.05867 ?  124 LEU   A C    1 
ATOM   13   O  O    . LEU   A 1 19  ? 38.84200 -0.19700  0.67700  1.000 49.13239 ?  124 LEU   A O    1 
ATOM   14   C  CB   . LEU   A 1 19  ? 38.62400 0.57500   3.46300  1.000 52.60573 ?  124 LEU   A CB   1 
ATOM   15   C  CG   . LEU   A 1 19  ? 37.15900 0.60600   3.91100  1.000 51.88049 ?  124 LEU   A CG   1 
ATOM   16   C  CD1  . LEU   A 1 19  ? 36.90600 -0.38100  5.04500  1.000 41.80961 ?  124 LEU   A CD1  1 
ATOM   17   C  CD2  . LEU   A 1 19  ? 36.74900 2.01300   4.31900  1.000 45.46031 ?  124 LEU   A CD2  1 
ATOM   18   N  N    . SER   A 1 20  ? 38.28400 -2.28600  1.31500  1.000 43.98946 ?  125 SER   A N    1 
ATOM   19   C  CA   . SER   A 1 20  ? 37.99200 -2.73700  -0.03600 1.000 43.41828 ?  125 SER   A CA   1 
ATOM   20   C  C    . SER   A 1 20  ? 36.77200 -2.01300  -0.60100 1.000 45.98040 ?  125 SER   A C    1 
ATOM   21   O  O    . SER   A 1 20  ? 35.99400 -1.38400  0.12000  1.000 38.97160 ?  125 SER   A O    1 
ATOM   22   C  CB   . SER   A 1 20  ? 37.75800 -4.24700  -0.05900 1.000 42.87202 ?  125 SER   A CB   1 
ATOM   23   O  OG   . SER   A 1 20  ? 36.56300 -4.59200  0.62500  1.000 40.09652 ?  125 SER   A OG   1 
ATOM   24   N  N    . GLU   A 1 21  ? 36.58100 -2.12400  -1.90600 1.000 47.44071 ?  126 GLU   A N    1 
ATOM   25   C  CA   . GLU   A 1 21  ? 35.42800 -1.47900  -2.57700 1.000 49.28173 ?  126 GLU   A CA   1 
ATOM   26   C  C    . GLU   A 1 21  ? 34.12600 -2.05700  -2.00400 1.000 46.31446 ?  126 GLU   A C    1 
ATOM   27   O  O    . GLU   A 1 21  ? 33.18600 -1.32700  -1.85000 1.000 43.14164 ?  126 GLU   A O    1 
ATOM   28   C  CB   . GLU   A 1 21  ? 35.52900 -1.78800  -4.06600 1.000 54.23796 ?  126 GLU   A CB   1 
ATOM   29   C  CG   . GLU   A 1 21  ? 36.15000 -3.15300  -4.29700 1.000 66.96396 ?  126 GLU   A CG   1 
ATOM   30   C  CD   . GLU   A 1 21  ? 37.66500 -3.16300  -4.46900 1.000 74.13538 ?  126 GLU   A CD   1 
ATOM   31   O  OE1  . GLU   A 1 21  ? 38.37900 -3.70200  -3.60400 1.000 71.69753 ?  126 GLU   A OE1  1 
ATOM   32   O  OE2  . GLU   A 1 21  ? 38.12900 -2.63500  -5.48800 1.000 79.83631 ?  126 GLU   A OE2  1 
ATOM   33   N  N    . GLU   A 1 22  ? 34.09700 -3.34300  -1.73300 1.000 42.69943 ?  127 GLU   A N    1 
ATOM   34   C  CA   . GLU   A 1 22  ? 32.86400 -3.90500  -1.19400 1.000 38.21992 ?  127 GLU   A CA   1 
ATOM   35   C  C    . GLU   A 1 22  ? 32.61700 -3.42500  0.23300  1.000 35.84420 ?  127 GLU   A C    1 
ATOM   36   O  O    . GLU   A 1 22  ? 31.46600 -3.21300  0.63200  1.000 35.32931 ?  127 GLU   A O    1 
ATOM   37   C  CB   . GLU   A 1 22  ? 32.88900 -5.43700  -1.24900 1.000 60.48248 ?  127 GLU   A CB   1 
ATOM   38   C  CG   . GLU   A 1 22  ? 31.58800 -6.05900  -0.74100 1.000 67.71843 ?  127 GLU   A CG   1 
ATOM   39   C  CD   . GLU   A 1 22  ? 31.67300 -7.55100  -0.48600 1.000 77.31636 ?  127 GLU   A CD   1 
ATOM   40   O  OE1  . GLU   A 1 22  ? 32.79400 -8.07500  -0.34000 1.000 82.68189 ?  127 GLU   A OE1  1 
ATOM   41   O  OE2  . GLU   A 1 22  ? 30.60700 -8.20000  -0.43900 1.000 82.74042 ?  127 GLU   A OE2  1 
ATOM   42   N  N    . GLN   A 1 23  ? 33.69700 -3.24000  1.00100  1.000 35.56361 ?  128 GLN   A N    1 
ATOM   43   C  CA   . GLN   A 1 23  ? 33.54400 -2.71800  2.35500  1.000 33.56073 ?  128 GLN   A CA   1 
ATOM   44   C  C    . GLN   A 1 23  ? 33.03000 -1.28200  2.34100  1.000 36.98948 ?  128 GLN   A C    1 
ATOM   45   O  O    . GLN   A 1 23  ? 32.19400 -0.90900  3.17400  1.000 33.23758 ?  128 GLN   A O    1 
ATOM   46   C  CB   . GLN   A 1 23  ? 34.86900 -2.81800  3.10900  1.000 40.10705 ?  128 GLN   A CB   1 
ATOM   47   C  CG   . GLN   A 1 23  ? 35.19000 -4.23600  3.58400  1.000 38.54622 ?  128 GLN   A CG   1 
ATOM   48   C  CD   . GLN   A 1 23  ? 36.57600 -4.37200  4.19200  1.000 38.74041 ?  128 GLN   A CD   1 
ATOM   49   O  OE1  . GLN   A 1 23  ? 37.49500 -3.62700  3.85100  1.000 35.56704 ?  128 GLN   A OE1  1 
ATOM   50   N  NE2  . GLN   A 1 23  ? 36.72900 -5.33000  5.10400  1.000 35.49426 ?  128 GLN   A NE2  1 
ATOM   51   N  N    . GLN   A 1 24  ? 33.51300 -0.46000  1.40500  1.000 34.00544 ?  129 GLN   A N    1 
ATOM   52   C  CA   . GLN   A 1 24  ? 32.95900 0.88300   1.25400  1.000 34.56669 ?  129 GLN   A CA   1 
ATOM   53   C  C    . GLN   A 1 24  ? 31.50400 0.82300   0.81200  1.000 33.18063 ?  129 GLN   A C    1 
ATOM   54   O  O    . GLN   A 1 24  ? 30.67400 1.62700   1.25400  1.000 34.40350 ?  129 GLN   A O    1 
ATOM   55   C  CB   . GLN   A 1 24  ? 33.78400 1.68200   0.24600  1.000 37.34791 ?  129 GLN   A CB   1 
ATOM   56   C  CG   . GLN   A 1 24  ? 35.25100 1.84200   0.60800  1.000 39.73165 ?  129 GLN   A CG   1 
ATOM   57   C  CD   . GLN   A 1 24  ? 36.04500 2.49300   -0.50900 1.000 52.42362 ?  129 GLN   A CD   1 
ATOM   58   O  OE1  . GLN   A 1 24  ? 35.64100 3.52000   -1.05200 1.000 53.97064 ?  129 GLN   A OE1  1 
ATOM   59   N  NE2  . GLN   A 1 24  ? 37.17400 1.89100   -0.86400 1.000 57.39952 ?  129 GLN   A NE2  1 
ATOM   60   N  N    . HIS   A 1 25  ? 31.18000 -0.12500  -0.07100 1.000 34.25298 ?  130 HIS   A N    1 
ATOM   61   C  CA   . HIS   A 1 25  ? 29.80200 -0.31600  -0.51100 1.000 36.46707 ?  130 HIS   A CA   1 
ATOM   62   C  C    . HIS   A 1 25  ? 28.89700 -0.65400  0.66600  1.000 36.43630 ?  130 HIS   A C    1 
ATOM   63   O  O    . HIS   A 1 25  ? 27.81000 -0.08200  0.81500  1.000 33.84968 ?  130 HIS   A O    1 
ATOM   64   C  CB   . HIS   A 1 25  ? 29.75800 -1.42100  -1.56800 1.000 40.65092 ?  130 HIS   A CB   1 
ATOM   65   C  CG   . HIS   A 1 25  ? 28.41200 -1.62600  -2.19200 1.000 43.65996 ?  130 HIS   A CG   1 
ATOM   66   N  ND1  . HIS   A 1 25  ? 27.69200 -0.60600  -2.77600 1.000 43.54854 ?  130 HIS   A ND1  1 
ATOM   67   C  CD2  . HIS   A 1 25  ? 27.66600 -2.74700  -2.34300 1.000 49.26513 ?  130 HIS   A CD2  1 
ATOM   68   C  CE1  . HIS   A 1 25  ? 26.55600 -1.08800  -3.25100 1.000 47.88407 ?  130 HIS   A CE1  1 
ATOM   69   N  NE2  . HIS   A 1 25  ? 26.51600 -2.38400  -3.00100 1.000 48.88623 ?  130 HIS   A NE2  1 
ATOM   70   N  N    . ILE   A 1 26  ? 29.33900 -1.58200  1.51900  1.000 35.64781 ?  131 ILE   A N    1 
ATOM   71   C  CA   . ILE   A 1 26  ? 28.56900 -1.97100  2.70000  1.000 30.73752 ?  131 ILE   A CA   1 
ATOM   72   C  C    . ILE   A 1 26  ? 28.27200 -0.75300  3.56400  1.000 32.01373 ?  131 ILE   A C    1 
ATOM   73   O  O    . ILE   A 1 26  ? 27.14100 -0.55000  4.02100  1.000 31.75729 ?  131 ILE   A O    1 
ATOM   74   C  CB   . ILE   A 1 26  ? 29.32900 -3.04500  3.49800  1.000 32.14857 ?  131 ILE   A CB   1 
ATOM   75   C  CG1  . ILE   A 1 26  ? 29.25700 -4.39500  2.78000  1.000 36.16109 ?  131 ILE   A CG1  1 
ATOM   76   C  CG2  . ILE   A 1 26  ? 28.79400 -3.14000  4.92300  1.000 31.41914 ?  131 ILE   A CG2  1 
ATOM   77   C  CD1  . ILE   A 1 26  ? 30.21200 -5.43100  3.33400  1.000 39.22682 ?  131 ILE   A CD1  1 
ATOM   78   N  N    . ILE   A 1 27  ? 29.29200 0.07100   3.80100  1.000 32.47737 ?  132 ILE   A N    1 
ATOM   79   C  CA   . ILE   A 1 27  ? 29.11500 1.26500   4.62300  1.000 30.50479 ?  132 ILE   A CA   1 
ATOM   80   C  C    . ILE   A 1 27  ? 28.11600 2.21600   3.97300  1.000 33.14683 ?  132 ILE   A C    1 
ATOM   81   O  O    . ILE   A 1 27  ? 27.23700 2.77500   4.64100  1.000 34.82410 ?  132 ILE   A O    1 
ATOM   82   C  CB   . ILE   A 1 27  ? 30.47700 1.94100   4.86400  1.000 27.85955 ?  132 ILE   A CB   1 
ATOM   83   C  CG1  . ILE   A 1 27  ? 31.32300 1.08900   5.80900  1.000 29.84988 ?  132 ILE   A CG1  1 
ATOM   84   C  CG2  . ILE   A 1 27  ? 30.30100 3.33900   5.41500  1.000 34.08594 ?  132 ILE   A CG2  1 
ATOM   85   C  CD1  . ILE   A 1 27  ? 32.75000 1.57200   5.95400  1.000 32.90195 ?  132 ILE   A CD1  1 
ATOM   86   N  N    . ALA   A 1 28  ? 28.23300 2.40700   2.65700  1.000 34.29401 ?  133 ALA   A N    1 
ATOM   87   C  CA   . ALA   A 1 28  ? 27.31100 3.29500   1.95600  1.000 29.40075 ?  133 ALA   A CA   1 
ATOM   88   C  C    . ALA   A 1 28  ? 25.87100 2.81300   2.07900  1.000 30.90301 ?  133 ALA   A C    1 
ATOM   89   O  O    . ALA   A 1 28  ? 24.95300 3.61900   2.27800  1.000 29.56405 ?  133 ALA   A O    1 
ATOM   90   C  CB   . ALA   A 1 28  ? 27.71600 3.41300   0.48800  1.000 31.44441 ?  133 ALA   A CB   1 
ATOM   91   N  N    . ILE   A 1 29  ? 25.65200 1.50100   1.96500  1.000 29.89127 ?  134 ILE   A N    1 
ATOM   92   C  CA   . ILE   A 1 29  ? 24.30500 0.95200   2.10600  1.000 28.96079 ?  134 ILE   A CA   1 
ATOM   93   C  C    . ILE   A 1 29  ? 23.76300 1.22200   3.50500  1.000 29.32695 ?  134 ILE   A C    1 
ATOM   94   O  O    . ILE   A 1 29  ? 22.60500 1.62600   3.67600  1.000 27.01864 ?  134 ILE   A O    1 
ATOM   95   C  CB   . ILE   A 1 29  ? 24.31200 -0.55400  1.78800  1.000 30.02287 ?  134 ILE   A CB   1 
ATOM   96   C  CG1  . ILE   A 1 29  ? 24.50300 -0.78600  0.29000  1.000 32.82732 ?  134 ILE   A CG1  1 
ATOM   97   C  CG2  . ILE   A 1 29  ? 23.02500 -1.20800  2.25500  1.000 27.62222 ?  134 ILE   A CG2  1 
ATOM   98   C  CD1  . ILE   A 1 29  ? 24.99900 -2.17900  -0.04200 1.000 38.96345 ?  134 ILE   A CD1  1 
ATOM   99   N  N    . LEU   A 1 30  ? 24.59200 1.00100   4.53000  1.000 26.53986 ?  135 LEU   A N    1 
ATOM   100  C  CA   . LEU   A 1 30  ? 24.13300 1.15900   5.90600  1.000 27.15932 ?  135 LEU   A CA   1 
ATOM   101  C  C    . LEU   A 1 30  ? 23.89000 2.62300   6.24400  1.000 26.40423 ?  135 LEU   A C    1 
ATOM   102  O  O    . LEU   A 1 30  ? 22.96000 2.94600   6.99500  1.000 24.34733 ?  135 LEU   A O    1 
ATOM   103  C  CB   . LEU   A 1 30  ? 25.14900 0.54100   6.86600  1.000 28.55406 ?  135 LEU   A CB   1 
ATOM   104  C  CG   . LEU   A 1 30  ? 25.26500 -0.98400  6.81200  1.000 27.65161 ?  135 LEU   A CG   1 
ATOM   105  C  CD1  . LEU   A 1 30  ? 26.35500 -1.47500  7.74600  1.000 29.35161 ?  135 LEU   A CD1  1 
ATOM   106  C  CD2  . LEU   A 1 30  ? 23.93600 -1.64100  7.14600  1.000 24.08729 ?  135 LEU   A CD2  1 
ATOM   107  N  N    A LEU   A 1 31  ? 24.71800 3.52600   5.71600  0.960 25.28843 ?  136 LEU   A N    1 
ATOM   108  N  N    B LEU   A 1 31  ? 24.72400 3.52000   5.71000  0.040 26.87174 ?  136 LEU   A N    1 
ATOM   109  C  CA   A LEU   A 1 31  ? 24.46300 4.94800   5.91300  0.960 28.32503 ?  136 LEU   A CA   1 
ATOM   110  C  CA   B LEU   A 1 31  ? 24.50100 4.95400   5.87400  0.040 27.50384 ?  136 LEU   A CA   1 
ATOM   111  C  C    A LEU   A 1 31  ? 23.13900 5.35500   5.28000  0.960 30.43235 ?  136 LEU   A C    1 
ATOM   112  C  C    B LEU   A 1 31  ? 23.16400 5.36700   5.27000  0.040 28.93080 ?  136 LEU   A C    1 
ATOM   113  O  O    A LEU   A 1 31  ? 22.34700 6.08400   5.89000  0.960 28.90228 ?  136 LEU   A O    1 
ATOM   114  O  O    B LEU   A 1 31  ? 22.39300 6.11700   5.88000  0.040 28.96008 ?  136 LEU   A O    1 
ATOM   115  C  CB   A LEU   A 1 31  ? 25.60800 5.77800   5.33600  0.960 26.83585 ?  136 LEU   A CB   1 
ATOM   116  C  CB   B LEU   A 1 31  ? 25.64200 5.73500   5.21600  0.040 28.08488 ?  136 LEU   A CB   1 
ATOM   117  C  CG   A LEU   A 1 31  ? 26.93500 5.79000   6.09200  0.960 26.92806 ?  136 LEU   A CG   1 
ATOM   118  C  CG   B LEU   A 1 31  ? 26.84800 6.19600   6.03900  0.040 28.17642 ?  136 LEU   A CG   1 
ATOM   119  C  CD1  A LEU   A 1 31  ? 27.99600 6.51100   5.27700  0.960 31.73066 ?  136 LEU   A CD1  1 
ATOM   120  C  CD1  B LEU   A 1 31  ? 27.44300 5.06000   6.84800  0.040 26.65925 ?  136 LEU   A CD1  1 
ATOM   121  C  CD2  A LEU   A 1 31  ? 26.78200 6.42200   7.46300  0.960 27.87639 ?  136 LEU   A CD2  1 
ATOM   122  C  CD2  B LEU   A 1 31  ? 27.90400 6.80800   5.12700  0.040 29.78848 ?  136 LEU   A CD2  1 
ATOM   123  N  N    . ASP   A 1 32  ? 22.88000 4.88700   4.05700  1.000 28.86445 ?  137 ASP   A N    1 
ATOM   124  C  CA   . ASP   A 1 32  ? 21.62400 5.21300   3.39000  1.000 26.24235 ?  137 ASP   A CA   1 
ATOM   125  C  C    . ASP   A 1 32  ? 20.43800 4.58900   4.11200  1.000 28.70068 ?  137 ASP   A C    1 
ATOM   126  O  O    . ASP   A 1 32  ? 19.38000 5.21800   4.24100  1.000 32.89543 ?  137 ASP   A O    1 
ATOM   127  C  CB   . ASP   A 1 32  ? 21.68700 4.74400   1.93700  1.000 31.20184 ?  137 ASP   A CB   1 
ATOM   128  C  CG   . ASP   A 1 32  ? 20.47500 5.15800   1.13400  1.000 37.79375 ?  137 ASP   A CG   1 
ATOM   129  O  OD1  . ASP   A 1 32  ? 19.74500 4.26200   0.66000  1.000 39.83031 ?  137 ASP   A OD1  1 
ATOM   130  O  OD2  . ASP   A 1 32  ? 20.25500 6.37400   0.96100  1.000 38.99524 ?  137 ASP   A OD2  1 
ATOM   131  N  N    . ALA   A 1 33  ? 20.59700 3.35200   4.59000  1.000 30.53382 ?  138 ALA   A N    1 
ATOM   132  C  CA   . ALA   A 1 33  ? 19.53100 2.69600   5.34100  1.000 25.68761 ?  138 ALA   A CA   1 
ATOM   133  C  C    . ALA   A 1 33  ? 19.16600 3.49600   6.58400  1.000 28.93769 ?  138 ALA   A C    1 
ATOM   134  O  O    . ALA   A 1 33  ? 17.98300 3.68300   6.89400  1.000 27.97143 ?  138 ALA   A O    1 
ATOM   135  C  CB   . ALA   A 1 33  ? 19.95900 1.27800   5.71800  1.000 23.58045 ?  138 ALA   A CB   1 
ATOM   136  N  N    . HIS   A 1 34  ? 20.17600 3.97800   7.31000  1.000 22.69146 ?  139 HIS   A N    1 
ATOM   137  C  CA   . HIS   A 1 34  ? 19.92400 4.79400   8.49400  1.000 22.86272 ?  139 HIS   A CA   1 
ATOM   138  C  C    . HIS   A 1 34  ? 19.26000 6.11300   8.12300  1.000 27.92094 ?  139 HIS   A C    1 
ATOM   139  O  O    . HIS   A 1 34  ? 18.34700 6.57300   8.81900  1.000 25.60192 ?  139 HIS   A O    1 
ATOM   140  C  CB   . HIS   A 1 34  ? 21.23400 5.04100   9.24000  1.000 22.56677 ?  139 HIS   A CB   1 
ATOM   141  C  CG   . HIS   A 1 34  ? 21.07500 5.83600   10.49600 1.000 23.20371 ?  139 HIS   A CG   1 
ATOM   142  N  ND1  . HIS   A 1 34  ? 20.26000 5.43400   11.53200 1.000 26.69219 ?  139 HIS   A ND1  1 
ATOM   143  C  CD2  . HIS   A 1 34  ? 21.63200 7.00700   10.88700 1.000 25.89399 ?  139 HIS   A CD2  1 
ATOM   144  C  CE1  . HIS   A 1 34  ? 20.31800 6.32500   12.50600 1.000 26.66724 ?  139 HIS   A CE1  1 
ATOM   145  N  NE2  . HIS   A 1 34  ? 21.14300 7.28900   12.14000 1.000 26.15473 ?  139 HIS   A NE2  1 
ATOM   146  N  N    A HIS   A 1 35  ? 19.69500 6.74100   7.03000  0.570 29.37960 ?  140 HIS   A N    1 
ATOM   147  N  N    B HIS   A 1 35  ? 19.71300 6.72900   7.02600  0.430 29.49817 ?  140 HIS   A N    1 
ATOM   148  C  CA   A HIS   A 1 35  ? 19.08000 8.00200   6.63200  0.570 30.45636 ?  140 HIS   A CA   1 
ATOM   149  C  CA   B HIS   A 1 35  ? 19.12900 7.97900   6.55000  0.430 30.72831 ?  140 HIS   A CA   1 
ATOM   150  C  C    A HIS   A 1 35  ? 17.62000 7.81400   6.24300  0.570 31.31829 ?  140 HIS   A C    1 
ATOM   151  C  C    B HIS   A 1 35  ? 17.65100 7.81300   6.22600  0.430 31.21440 ?  140 HIS   A C    1 
ATOM   152  O  O    A HIS   A 1 35  ? 16.79900 8.71200   6.46400  0.570 31.09216 ?  140 HIS   A O    1 
ATOM   153  O  O    B HIS   A 1 35  ? 16.84700 8.72100   6.46800  0.430 31.21771 ?  140 HIS   A O    1 
ATOM   154  C  CB   A HIS   A 1 35  ? 19.86800 8.63000   5.48600  0.570 33.99473 ?  140 HIS   A CB   1 
ATOM   155  C  CB   B HIS   A 1 35  ? 19.90100 8.46400   5.32100  0.430 33.57918 ?  140 HIS   A CB   1 
ATOM   156  C  CG   A HIS   A 1 35  ? 21.24900 9.05500   5.87500  0.570 36.06244 ?  140 HIS   A CG   1 
ATOM   157  C  CG   B HIS   A 1 35  ? 19.32000 9.68300   4.67400  0.430 36.02651 ?  140 HIS   A CG   1 
ATOM   158  N  ND1  A HIS   A 1 35  ? 21.63600 9.20200   7.18900  0.570 35.71273 ?  140 HIS   A ND1  1 
ATOM   159  N  ND1  B HIS   A 1 35  ? 18.47400 9.61600   3.58700  0.430 38.99489 ?  140 HIS   A ND1  1 
ATOM   160  C  CD2  A HIS   A 1 35  ? 22.33500 9.35800   5.12600  0.570 35.32082 ?  140 HIS   A CD2  1 
ATOM   161  C  CD2  B HIS   A 1 35  ? 19.48100 11.00000  4.94300  0.430 38.13577 ?  140 HIS   A CD2  1 
ATOM   162  C  CE1  A HIS   A 1 35  ? 22.90000 9.58200   7.23200  0.570 30.98918 ?  140 HIS   A CE1  1 
ATOM   163  C  CE1  B HIS   A 1 35  ? 18.12900 10.83800  3.22400  0.430 38.46162 ?  140 HIS   A CE1  1 
ATOM   164  N  NE2  A HIS   A 1 35  ? 23.34800 9.68200   5.99400  0.570 37.52874 ?  140 HIS   A NE2  1 
ATOM   165  N  NE2  B HIS   A 1 35  ? 18.72700 11.69700  4.03100  0.430 36.42070 ?  140 HIS   A NE2  1 
ATOM   166  N  N    . LYS   A 1 36  ? 17.27200 6.65600   5.68600  1.000 27.49547 ?  141 LYS   A N    1 
ATOM   167  C  CA   . LYS   A 1 36  ? 15.89400 6.40300   5.29600  1.000 26.17138 ?  141 LYS   A CA   1 
ATOM   168  C  C    . LYS   A 1 36  ? 15.01400 5.95400   6.45900  1.000 28.82735 ?  141 LYS   A C    1 
ATOM   169  O  O    . LYS   A 1 36  ? 13.78800 5.94300   6.31200  1.000 28.88699 ?  141 LYS   A O    1 
ATOM   170  C  CB   . LYS   A 1 36  ? 15.86400 5.36600   4.16800  1.000 28.66150 ?  141 LYS   A CB   1 
ATOM   171  C  CG   . LYS   A 1 36  ? 16.34400 5.92300   2.83000  1.000 37.08796 ?  141 LYS   A CG   1 
ATOM   172  C  CD   . LYS   A 1 36  ? 16.38800 4.86700   1.73300  1.000 45.21807 ?  141 LYS   A CD   1 
ATOM   173  C  CE   . LYS   A 1 36  ? 16.38200 5.51600   0.35400  1.000 50.68218 ?  141 LYS   A CE   1 
ATOM   174  N  NZ   . LYS   A 1 36  ? 17.15100 6.79300   0.34000  1.000 56.88348 ?  141 LYS   A NZ   1 
ATOM   175  N  N    . THR   A 1 37  ? 15.59700 5.61400   7.61300  1.000 25.95491 ?  142 THR   A N    1 
ATOM   176  C  CA   . THR   A 1 37  ? 14.82800 5.09700   8.73900  1.000 21.79798 ?  142 THR   A CA   1 
ATOM   177  C  C    . THR   A 1 37  ? 14.94100 5.92800   10.01200 1.000 27.22084 ?  142 THR   A C    1 
ATOM   178  O  O    . THR   A 1 37  ? 14.25300 5.61700   10.99200 1.000 29.71796 ?  142 THR   A O    1 
ATOM   179  C  CB   . THR   A 1 37  ? 15.23800 3.65000   9.05400  1.000 25.26649 ?  142 THR   A CB   1 
ATOM   180  O  OG1  . THR   A 1 37  ? 16.65600 3.58100   9.24700  1.000 25.59219 ?  142 THR   A OG1  1 
ATOM   181  C  CG2  . THR   A 1 37  ? 14.84600 2.72400   7.91900  1.000 25.83352 ?  142 THR   A CG2  1 
ATOM   182  N  N    . TYR   A 1 38  ? 15.77900 6.96300   10.04200 1.000 27.11771 ?  143 TYR   A N    1 
ATOM   183  C  CA   . TYR   A 1 38  ? 15.88500 7.83800   11.20400 1.000 26.02717 ?  143 TYR   A CA   1 
ATOM   184  C  C    . TYR   A 1 38  ? 15.52300 9.25500   10.78300 1.000 27.74355 ?  143 TYR   A C    1 
ATOM   185  O  O    . TYR   A 1 38  ? 16.22600 9.86100   9.96800  1.000 30.68362 ?  143 TYR   A O    1 
ATOM   186  C  CB   . TYR   A 1 38  ? 17.29300 7.79900   11.80800 1.000 25.13859 ?  143 TYR   A CB   1 
ATOM   187  C  CG   . TYR   A 1 38  ? 17.39300 8.46600   13.16500 1.000 22.05762 ?  143 TYR   A CG   1 
ATOM   188  C  CD1  . TYR   A 1 38  ? 17.49300 9.84900   13.28300 1.000 26.40405 ?  143 TYR   A CD1  1 
ATOM   189  C  CD2  . TYR   A 1 38  ? 17.38600 7.71400   14.32700 1.000 23.09642 ?  143 TYR   A CD2  1 
ATOM   190  C  CE1  . TYR   A 1 38  ? 17.58200 10.45600  14.52000 1.000 25.13970 ?  143 TYR   A CE1  1 
ATOM   191  C  CE2  . TYR   A 1 38  ? 17.48400 8.31300   15.55700 1.000 22.23953 ?  143 TYR   A CE2  1 
ATOM   192  C  CZ   . TYR   A 1 38  ? 17.57200 9.68100   15.65600 1.000 24.13400 ?  143 TYR   A CZ   1 
ATOM   193  O  OH   . TYR   A 1 38  ? 17.66200 10.26900  16.89800 1.000 26.31704 ?  143 TYR   A OH   1 
ATOM   194  N  N    . ASP   A 1 39  ? 14.43200 9.78100   11.34900 1.000 23.50831 ?  144 ASP   A N    1 
ATOM   195  C  CA   . ASP   A 1 39  ? 13.94800 11.11800  11.03100 1.000 28.88215 ?  144 ASP   A CA   1 
ATOM   196  C  C    . ASP   A 1 39  ? 14.39400 12.07100  12.13400 1.000 33.65504 ?  144 ASP   A C    1 
ATOM   197  O  O    . ASP   A 1 39  ? 13.78900 12.08400  13.21900 1.000 31.96512 ?  144 ASP   A O    1 
ATOM   198  C  CB   . ASP   A 1 39  ? 12.42000 11.11800  10.89200 1.000 27.57801 ?  144 ASP   A CB   1 
ATOM   199  C  CG   . ASP   A 1 39  ? 11.83800 12.51000  10.68600 1.000 35.75510 ?  144 ASP   A CG   1 
ATOM   200  O  OD1  . ASP   A 1 39  ? 12.60100 13.47200  10.46200 1.000 32.16906 ?  144 ASP   A OD1  1 
ATOM   201  O  OD2  . ASP   A 1 39  ? 10.59600 12.63600  10.74000 1.000 38.02292 ?  144 ASP   A OD2  1 
ATOM   202  N  N    . PRO   A 1 40  ? 15.43100 12.88400  11.91800 1.000 32.12346 ?  145 PRO   A N    1 
ATOM   203  C  CA   . PRO   A 1 40  ? 15.90100 13.79300  12.97100 1.000 32.30252 ?  145 PRO   A CA   1 
ATOM   204  C  C    . PRO   A 1 40  ? 14.99000 14.98300  13.22900 1.000 32.07908 ?  145 PRO   A C    1 
ATOM   205  O  O    . PRO   A 1 40  ? 15.30500 15.79600  14.10400 1.000 33.56420 ?  145 PRO   A O    1 
ATOM   206  C  CB   . PRO   A 1 40  ? 17.26600 14.25700  12.43600 1.000 31.04570 ?  145 PRO   A CB   1 
ATOM   207  C  CG   . PRO   A 1 40  ? 17.13200 14.18700  10.95800 1.000 31.86117 ?  145 PRO   A CG   1 
ATOM   208  C  CD   . PRO   A 1 40  ? 16.22000 13.01500  10.67700 1.000 30.58896 ?  145 PRO   A CD   1 
ATOM   209  N  N    . THR   A 1 41  ? 13.88500 15.12200  12.49500 1.000 32.31784 ?  146 THR   A N    1 
ATOM   210  C  CA   . THR   A 1 41  ? 12.90000 16.14600  12.81900 1.000 31.26357 ?  146 THR   A CA   1 
ATOM   211  C  C    . THR   A 1 41  ? 11.90100 15.67300  13.86200 1.000 33.31706 ?  146 THR   A C    1 
ATOM   212  O  O    . THR   A 1 41  ? 11.22600 16.50600  14.47700 1.000 31.20180 ?  146 THR   A O    1 
ATOM   213  C  CB   . THR   A 1 41  ? 12.14400 16.58600  11.56300 1.000 37.69444 ?  146 THR   A CB   1 
ATOM   214  O  OG1  . THR   A 1 41  ? 11.24000 15.54900  11.16100 1.000 36.02380 ?  146 THR   A OG1  1 
ATOM   215  C  CG2  . THR   A 1 41  ? 13.11400 16.88600  10.43300 1.000 45.80402 ?  146 THR   A CG2  1 
ATOM   216  N  N    . TYR   A 1 42  ? 11.79300 14.35800  14.06200 1.000 31.55370 ?  147 TYR   A N    1 
ATOM   217  C  CA   . TYR   A 1 42  ? 10.89800 13.75600  15.04600 1.000 27.89352 ?  147 TYR   A CA   1 
ATOM   218  C  C    . TYR   A 1 42  ? 9.45200  14.16700  14.82400 1.000 33.59531 ?  147 TYR   A C    1 
ATOM   219  O  O    . TYR   A 1 42  ? 8.65900  14.20600  15.76900 1.000 31.63599 ?  147 TYR   A O    1 
ATOM   220  C  CB   . TYR   A 1 42  ? 11.35500 14.09100  16.46700 1.000 27.83462 ?  147 TYR   A CB   1 
ATOM   221  C  CG   . TYR   A 1 42  ? 12.80800 13.74400  16.68000 1.000 27.03373 ?  147 TYR   A CG   1 
ATOM   222  C  CD1  . TYR   A 1 42  ? 13.77000 14.73500  16.82000 1.000 35.58035 ?  147 TYR   A CD1  1 
ATOM   223  C  CD2  . TYR   A 1 42  ? 13.21800 12.42100  16.71000 1.000 25.23687 ?  147 TYR   A CD2  1 
ATOM   224  C  CE1  . TYR   A 1 42  ? 15.10200 14.41100  17.00300 1.000 32.44753 ?  147 TYR   A CE1  1 
ATOM   225  C  CE2  . TYR   A 1 42  ? 14.54200 12.08800  16.89000 1.000 31.34923 ?  147 TYR   A CE2  1 
ATOM   226  C  CZ   . TYR   A 1 42  ? 15.48100 13.08400  17.03700 1.000 31.83163 ?  147 TYR   A CZ   1 
ATOM   227  O  OH   . TYR   A 1 42  ? 16.80100 12.74800  17.21700 1.000 30.30213 ?  147 TYR   A OH   1 
ATOM   228  N  N    . ALA   A 1 43  ? 9.10800  14.46000  13.56800 1.000 34.04508 ?  148 ALA   A N    1 
ATOM   229  C  CA   . ALA   A 1 43  ? 7.78700  14.99000  13.25200 1.000 35.30334 ?  148 ALA   A CA   1 
ATOM   230  C  C    . ALA   A 1 43  ? 6.68500  14.00300  13.61400 1.000 35.25329 ?  148 ALA   A C    1 
ATOM   231  O  O    . ALA   A 1 43  ? 5.60700  14.40700  14.06400 1.000 41.06625 ?  148 ALA   A O    1 
ATOM   232  C  CB   . ALA   A 1 43  ? 7.71600  15.35100  11.76900 1.000 34.06359 ?  148 ALA   A CB   1 
ATOM   233  N  N    . ASP   A 1 44  ? 6.93500  12.70400  13.42600 1.000 29.78014 ?  149 ASP   A N    1 
ATOM   234  C  CA   . ASP   A 1 44  ? 5.90900  11.69700  13.67400 1.000 29.51493 ?  149 ASP   A CA   1 
ATOM   235  C  C    . ASP   A 1 44  ? 5.53000  11.57900  15.14300 1.000 32.19950 ?  149 ASP   A C    1 
ATOM   236  O  O    . ASP   A 1 44  ? 4.49800  10.97000  15.44700 1.000 29.53680 ?  149 ASP   A O    1 
ATOM   237  C  CB   . ASP   A 1 44  ? 6.36700  10.33200  13.16000 1.000 32.44900 ?  149 ASP   A CB   1 
ATOM   238  C  CG   . ASP   A 1 44  ? 6.60900  10.32100  11.66600 1.000 38.67605 ?  149 ASP   A CG   1 
ATOM   239  O  OD1  . ASP   A 1 44  ? 5.92300  11.07400  10.94300 1.000 41.69165 ?  149 ASP   A OD1  1 
ATOM   240  O  OD2  . ASP   A 1 44  ? 7.47800  9.54700   11.21100 1.000 40.75506 ?  149 ASP   A OD2  1 
ATOM   241  N  N    . PHE   A 1 45  ? 6.32500  12.14600  16.05500 1.000 27.43574 ?  150 PHE   A N    1 
ATOM   242  C  CA   . PHE   A 1 45  ? 6.00100  12.07900  17.47700 1.000 29.77782 ?  150 PHE   A CA   1 
ATOM   243  C  C    . PHE   A 1 45  ? 4.64700  12.70900  17.78400 1.000 29.17025 ?  150 PHE   A C    1 
ATOM   244  O  O    . PHE   A 1 45  ? 4.03800  12.37700  18.80600 1.000 31.89981 ?  150 PHE   A O    1 
ATOM   245  C  CB   . PHE   A 1 45  ? 7.09000  12.76500  18.30900 1.000 29.85519 ?  150 PHE   A CB   1 
ATOM   246  C  CG   . PHE   A 1 45  ? 8.36000  11.95700  18.46200 1.000 29.14557 ?  150 PHE   A CG   1 
ATOM   247  C  CD1  . PHE   A 1 45  ? 8.88400  11.23500  17.39900 1.000 26.56888 ?  150 PHE   A CD1  1 
ATOM   248  C  CD2  . PHE   A 1 45  ? 9.03000  11.93000  19.67500 1.000 29.81507 ?  150 PHE   A CD2  1 
ATOM   249  C  CE1  . PHE   A 1 45  ? 10.05000 10.50100  17.54500 1.000 27.31116 ?  150 PHE   A CE1  1 
ATOM   250  C  CE2  . PHE   A 1 45  ? 10.19800 11.19900  19.82700 1.000 26.93780 ?  150 PHE   A CE2  1 
ATOM   251  C  CZ   . PHE   A 1 45  ? 10.70800 10.48300  18.75800 1.000 27.55361 ?  150 PHE   A CZ   1 
ATOM   252  N  N    A ARG   A 1 46  ? 4.16100  13.60700  16.92100 0.680 32.81597 ?  151 ARG   A N    1 
ATOM   253  N  N    B ARG   A 1 46  ? 4.16500  13.60800  16.92100 0.320 33.98142 ?  151 ARG   A N    1 
ATOM   254  C  CA   A ARG   A 1 46  ? 2.84600  14.20300  17.11800 0.680 38.83200 ?  151 ARG   A CA   1 
ATOM   255  C  CA   B ARG   A 1 46  ? 2.84800  14.20300  17.11200 0.320 38.75325 ?  151 ARG   A CA   1 
ATOM   256  C  C    A ARG   A 1 46  ? 1.72200  13.18400  16.99100 0.680 37.03839 ?  151 ARG   A C    1 
ATOM   257  C  C    B ARG   A 1 46  ? 1.73000  13.17400  17.01200 0.320 37.10312 ?  151 ARG   A C    1 
ATOM   258  O  O    A ARG   A 1 46  ? 0.60400  13.45400  17.44400 0.680 39.21712 ?  151 ARG   A O    1 
ATOM   259  O  O    B ARG   A 1 46  ? 0.62400  13.42600  17.50500 0.320 39.01649 ?  151 ARG   A O    1 
ATOM   260  C  CB   A ARG   A 1 46  ? 2.63100  15.34200  16.12000 0.680 45.21329 ?  151 ARG   A CB   1 
ATOM   261  C  CB   B ARG   A 1 46  ? 2.62600  15.31500  16.08500 0.320 45.36318 ?  151 ARG   A CB   1 
ATOM   262  C  CG   A ARG   A 1 46  ? 2.42500  14.88500  14.68400 0.680 50.51553 ?  151 ARG   A CG   1 
ATOM   263  C  CG   B ARG   A 1 46  ? 2.27100  14.80800  14.69800 0.320 50.40678 ?  151 ARG   A CG   1 
ATOM   264  C  CD   A ARG   A 1 46  ? 1.58800  15.88800  13.90700 0.680 56.80465 ?  151 ARG   A CD   1 
ATOM   265  C  CD   B ARG   A 1 46  ? 1.40800  15.81000  13.94600 0.320 56.15558 ?  151 ARG   A CD   1 
ATOM   266  N  NE   A ARG   A 1 46  ? 1.05200  15.31800  12.67500 0.680 58.25794 ?  151 ARG   A NE   1 
ATOM   267  N  NE   B ARG   A 1 46  ? 1.19300  15.43100  12.55100 0.320 57.56799 ?  151 ARG   A NE   1 
ATOM   268  C  CZ   A ARG   A 1 46  ? -0.18200 14.84300  12.54600 0.680 57.03734 ?  151 ARG   A CZ   1 
ATOM   269  C  CZ   B ARG   A 1 46  ? 2.14100  15.39200  11.61800 0.320 55.22335 ?  151 ARG   A CZ   1 
ATOM   270  N  NH1  A ARG   A 1 46  ? -0.58200 14.34400  11.38400 0.680 54.93690 ?  151 ARG   A NH1  1 
ATOM   271  N  NH1  B ARG   A 1 46  ? 1.83300  15.03100  10.38000 0.320 53.48730 ?  151 ARG   A NH1  1 
ATOM   272  N  NH2  A ARG   A 1 46  ? -1.01700 14.86700  13.57500 0.680 56.30893 ?  151 ARG   A NH2  1 
ATOM   273  N  NH2  B ARG   A 1 46  ? 3.39300  15.72200  11.91100 0.320 51.48116 ?  151 ARG   A NH2  1 
ATOM   274  N  N    . ASP   A 1 47  ? 1.98900  12.02600  16.38400 1.000 32.55994 ?  152 ASP   A N    1 
ATOM   275  C  CA   . ASP   A 1 47  ? 0.98300  10.98100  16.25300 1.000 39.03053 ?  152 ASP   A CA   1 
ATOM   276  C  C    . ASP   A 1 47  ? 0.85600  10.12800  17.50500 1.000 33.91355 ?  152 ASP   A C    1 
ATOM   277  O  O    . ASP   A 1 47  ? -0.13400 9.39900   17.63900 1.000 33.12501 ?  152 ASP   A O    1 
ATOM   278  C  CB   . ASP   A 1 47  ? 1.31000  10.06800  15.06700 1.000 40.58228 ?  152 ASP   A CB   1 
ATOM   279  C  CG   . ASP   A 1 47  ? 1.31300  10.80500  13.74700 1.000 49.56731 ?  152 ASP   A CG   1 
ATOM   280  O  OD1  . ASP   A 1 47  ? 0.61700  11.83500  13.64100 1.000 51.01758 ?  152 ASP   A OD1  1 
ATOM   281  O  OD2  . ASP   A 1 47  ? 2.00800  10.35200  12.81200 1.000 50.90511 ?  152 ASP   A OD2  1 
ATOM   282  N  N    . PHE   A 1 48  ? 1.82600  10.19400  18.41100 1.000 30.93847 ?  153 PHE   A N    1 
ATOM   283  C  CA   . PHE   A 1 48  ? 1.79200  9.35300   19.59400 1.000 24.31845 ?  153 PHE   A CA   1 
ATOM   284  C  C    . PHE   A 1 48  ? 0.73900  9.85400   20.57400 1.000 25.50132 ?  153 PHE   A C    1 
ATOM   285  O  O    . PHE   A 1 48  ? 0.32500  11.01800  20.54700 1.000 30.71702 ?  153 PHE   A O    1 
ATOM   286  C  CB   . PHE   A 1 48  ? 3.15500  9.32700   20.29500 1.000 24.19988 ?  153 PHE   A CB   1 
ATOM   287  C  CG   . PHE   A 1 48  ? 4.30700  8.92700   19.41000 1.000 29.09004 ?  153 PHE   A CG   1 
ATOM   288  C  CD1  . PHE   A 1 48  ? 5.60800  9.18900   19.81000 1.000 25.16173 ?  153 PHE   A CD1  1 
ATOM   289  C  CD2  . PHE   A 1 48  ? 4.10100  8.28700   18.19600 1.000 29.07109 ?  153 PHE   A CD2  1 
ATOM   290  C  CE1  . PHE   A 1 48  ? 6.67700  8.83400   19.01700 1.000 25.43637 ?  153 PHE   A CE1  1 
ATOM   291  C  CE2  . PHE   A 1 48  ? 5.16900  7.93000   17.39500 1.000 27.10146 ?  153 PHE   A CE2  1 
ATOM   292  C  CZ   . PHE   A 1 48  ? 6.45900  8.20000   17.81000 1.000 27.27538 ?  153 PHE   A CZ   1 
ATOM   293  N  N    . ARG   A 1 49  ? 0.30600  8.95400   21.44900 1.000 25.24544 ?  154 ARG   A N    1 
ATOM   294  C  CA   . ARG   A 1 49  ? -0.46900 9.38300   22.59700 1.000 28.13469 ?  154 ARG   A CA   1 
ATOM   295  C  C    . ARG   A 1 49  ? 0.36000  10.37500  23.41100 1.000 29.46114 ?  154 ARG   A C    1 
ATOM   296  O  O    . ARG   A 1 49  ? 1.58100  10.22300  23.53700 1.000 30.46345 ?  154 ARG   A O    1 
ATOM   297  C  CB   . ARG   A 1 49  ? -0.87600 8.18200   23.44700 1.000 28.53870 ?  154 ARG   A CB   1 
ATOM   298  C  CG   . ARG   A 1 49  ? -1.98900 7.35600   22.81900 1.000 31.54428 ?  154 ARG   A CG   1 
ATOM   299  C  CD   . ARG   A 1 49  ? -2.18500 6.03000   23.52700 1.000 32.50773 ?  154 ARG   A CD   1 
ATOM   300  N  NE   . ARG   A 1 49  ? -1.09300 5.10200   23.25000 1.000 32.15844 ?  154 ARG   A NE   1 
ATOM   301  C  CZ   . ARG   A 1 49  ? -0.92200 3.94300   23.87800 1.000 29.74065 ?  154 ARG   A CZ   1 
ATOM   302  N  NH1  . ARG   A 1 49  ? -1.77600 3.56800   24.82000 1.000 31.01778 ?  154 ARG   A NH1  1 
ATOM   303  N  NH2  . ARG   A 1 49  ? 0.10500  3.16300   23.56900 1.000 26.85509 ?  154 ARG   A NH2  1 
ATOM   304  N  N    . PRO   A 1 50  ? -0.27100 11.41800  23.95000 1.000 32.77595 ?  155 PRO   A N    1 
ATOM   305  C  CA   . PRO   A 1 50  ? 0.49500  12.54000  24.48700 1.000 33.54638 ?  155 PRO   A CA   1 
ATOM   306  C  C    . PRO   A 1 50  ? 1.29400  12.12900  25.70700 1.000 37.37763 ?  155 PRO   A C    1 
ATOM   307  O  O    . PRO   A 1 50  ? 0.84900  11.28600  26.50700 1.000 33.54562 ?  155 PRO   A O    1 
ATOM   308  C  CB   . PRO   A 1 50  ? -0.58900 13.57000  24.85300 1.000 34.03222 ?  155 PRO   A CB   1 
ATOM   309  C  CG   . PRO   A 1 50  ? -1.86300 12.78100  24.94000 1.000 37.83595 ?  155 PRO   A CG   1 
ATOM   310  C  CD   . PRO   A 1 50  ? -1.72200 11.67100  23.95600 1.000 32.82827 ?  155 PRO   A CD   1 
ATOM   311  N  N    . PRO   A 1 51  ? 2.48300  12.69700  25.89900 1.000 32.97805 ?  156 PRO   A N    1 
ATOM   312  C  CA   . PRO   A 1 51  ? 3.19900  12.48700  27.15800 1.000 36.91477 ?  156 PRO   A CA   1 
ATOM   313  C  C    . PRO   A 1 51  ? 2.46400  13.16700  28.29900 1.000 38.85515 ?  156 PRO   A C    1 
ATOM   314  O  O    . PRO   A 1 51  ? 1.90000  14.25200  28.14000 1.000 39.28715 ?  156 PRO   A O    1 
ATOM   315  C  CB   . PRO   A 1 51  ? 4.56300  13.13300  26.90400 1.000 35.52943 ?  156 PRO   A CB   1 
ATOM   316  C  CG   . PRO   A 1 51  ? 4.27800  14.20000  25.89500 1.000 40.50585 ?  156 PRO   A CG   1 
ATOM   317  C  CD   . PRO   A 1 51  ? 3.15400  13.68300  25.03300 1.000 36.74889 ?  156 PRO   A CD   1 
ATOM   318  N  N    . VAL   A 1 52  ? 2.46200  12.51100  29.45500 1.000 36.38063 ?  157 VAL   A N    1 
ATOM   319  C  CA   . VAL   A 1 52  ? 1.83300  13.04100  30.65700 1.000 38.65904 ?  157 VAL   A CA   1 
ATOM   320  C  C    . VAL   A 1 52  ? 2.81700  12.87400  31.80400 1.000 41.50044 ?  157 VAL   A C    1 
ATOM   321  O  O    . VAL   A 1 52  ? 3.26200  11.75500  32.08700 1.000 37.46075 ?  157 VAL   A O    1 
ATOM   322  C  CB   . VAL   A 1 52  ? 0.50000  12.34200  30.97300 1.000 39.07934 ?  157 VAL   A CB   1 
ATOM   323  C  CG1  . VAL   A 1 52  ? -0.03400 12.80600  32.31600 1.000 38.30187 ?  157 VAL   A CG1  1 
ATOM   324  C  CG2  . VAL   A 1 52  ? -0.51300 12.60500  29.86800 1.000 36.42578 ?  157 VAL   A CG2  1 
ATOM   325  N  N    . ARG   A 1 53  ? 3.16600  13.97700  32.45000 1.000 47.54113 ?  158 ARG   A N    1 
ATOM   326  C  CA   . ARG   A 1 53  ? 4.08000  13.97300  33.58600 1.000 55.17165 ?  158 ARG   A CA   1 
ATOM   327  C  C    . ARG   A 1 53  ? 3.26300  14.36500  34.81400 1.000 66.31088 ?  158 ARG   A C    1 
ATOM   328  O  O    . ARG   A 1 53  ? 3.03100  15.55100  35.06600 1.000 70.00524 ?  158 ARG   A O    1 
ATOM   329  C  CB   . ARG   A 1 53  ? 5.25600  14.91600  33.33800 1.000 53.68988 ?  158 ARG   A CB   1 
ATOM   330  C  CG   . ARG   A 1 53  ? 6.34300  14.31900  32.43900 1.000 47.94338 ?  158 ARG   A CG   1 
ATOM   331  C  CD   . ARG   A 1 53  ? 6.50700  15.10100  31.13200 1.000 46.42467 ?  158 ARG   A CD   1 
ATOM   332  N  NE   . ARG   A 1 53  ? 7.56800  14.55200  30.28700 1.000 44.82766 ?  158 ARG   A NE   1 
ATOM   333  C  CZ   . ARG   A 1 53  ? 7.65600  14.74400  28.97300 1.000 39.78175 ?  158 ARG   A CZ   1 
ATOM   334  N  NH1  . ARG   A 1 53  ? 6.74900  15.47400  28.34200 1.000 36.15230 ?  158 ARG   A NH1  1 
ATOM   335  N  NH2  . ARG   A 1 53  ? 8.65600  14.20600  28.28600 1.000 36.19018 ?  158 ARG   A NH2  1 
ATOM   336  N  N    . MET   A 1 54  ? 2.81200  13.36300  35.56300 1.000 73.93517 ?  159 MET   A N    1 
ATOM   337  C  CA   . MET   A 1 54  ? 1.92700  13.58800  36.70100 1.000 82.16569 ?  159 MET   A CA   1 
ATOM   338  C  C    . MET   A 1 54  ? 2.19800  12.59400  37.83100 1.000 85.58277 ?  159 MET   A C    1 
ATOM   339  O  O    . MET   A 1 54  ? 2.41900  11.40400  37.59500 1.000 88.06387 ?  159 MET   A O    1 
ATOM   340  C  CB   . MET   A 1 54  ? 0.46000  13.51000  36.25600 1.000 83.88014 ?  159 MET   A CB   1 
ATOM   341  C  CG   . MET   A 1 54  ? -0.00900 12.11100  35.87600 1.000 88.28467 ?  159 MET   A CG   1 
ATOM   342  S  SD   . MET   A 1 54  ? -1.75900 11.97900  35.45900 1.000 95.57655 ?  159 MET   A SD   1 
ATOM   343  C  CE   . MET   A 1 54  ? -2.43500 13.41000  36.29700 1.000 96.96087 ?  159 MET   A CE   1 
ATOM   344  N  N    . SER   A 1 66  ? 2.32500  7.18900   41.69500 1.000 86.15516 ?  218 SER   A N    1 
ATOM   345  C  CA   . SER   A 1 66  ? 2.03600  5.78200   41.41600 1.000 84.64527 ?  218 SER   A CA   1 
ATOM   346  C  C    . SER   A 1 66  ? 1.67400  5.46400   39.95100 1.000 82.67495 ?  218 SER   A C    1 
ATOM   347  O  O    . SER   A 1 66  ? 2.16000  4.46600   39.41600 1.000 82.30861 ?  218 SER   A O    1 
ATOM   348  C  CB   . SER   A 1 66  ? 0.91500  5.28400   42.33500 1.000 86.79472 ?  218 SER   A CB   1 
ATOM   349  O  OG   . SER   A 1 66  ? 1.06600  3.90000   42.60100 1.000 85.73616 ?  218 SER   A OG   1 
ATOM   350  N  N    . PRO   A 1 67  ? 0.83000  6.27400   39.30100 1.000 79.41999 ?  219 PRO   A N    1 
ATOM   351  C  CA   . PRO   A 1 67  ? 0.44000  5.94900   37.92400 1.000 72.77625 ?  219 PRO   A CA   1 
ATOM   352  C  C    . PRO   A 1 67  ? 1.61200  6.02800   36.95800 1.000 62.17971 ?  219 PRO   A C    1 
ATOM   353  O  O    . PRO   A 1 67  ? 2.51700  6.85500   37.09800 1.000 64.09221 ?  219 PRO   A O    1 
ATOM   354  C  CB   . PRO   A 1 67  ? -0.62000 7.00700   37.59600 1.000 75.89058 ?  219 PRO   A CB   1 
ATOM   355  C  CG   . PRO   A 1 67  ? -0.29200 8.14100   38.49500 1.000 81.84480 ?  219 PRO   A CG   1 
ATOM   356  C  CD   . PRO   A 1 67  ? 0.11500  7.47500   39.77100 1.000 83.56998 ?  219 PRO   A CD   1 
ATOM   357  N  N    . LEU   A 1 68  ? 1.58000  5.14300   35.96200 1.000 50.64577 ?  220 LEU   A N    1 
ATOM   358  C  CA   . LEU   A 1 68  ? 2.60200  5.09400   34.91700 1.000 36.60610 ?  220 LEU   A CA   1 
ATOM   359  C  C    . LEU   A 1 68  ? 2.19400  6.03000   33.77700 1.000 30.74460 ?  220 LEU   A C    1 
ATOM   360  O  O    . LEU   A 1 68  ? 1.85800  5.61700   32.66600 1.000 30.03366 ?  220 LEU   A O    1 
ATOM   361  C  CB   . LEU   A 1 68  ? 2.79400  3.66100   34.43700 1.000 40.68655 ?  220 LEU   A CB   1 
ATOM   362  C  CG   . LEU   A 1 68  ? 3.09900  2.63200   35.53000 1.000 42.87935 ?  220 LEU   A CG   1 
ATOM   363  C  CD1  . LEU   A 1 68  ? 3.50100  1.29600   34.92700 1.000 42.60050 ?  220 LEU   A CD1  1 
ATOM   364  C  CD2  . LEU   A 1 68  ? 4.18700  3.14700   36.45600 1.000 43.88122 ?  220 LEU   A CD2  1 
ATOM   365  N  N    . SER   A 1 69  ? 2.24700  7.33000   34.08200 1.000 31.65426 ?  221 SER   A N    1 
ATOM   366  C  CA   . SER   A 1 69  ? 1.66300  8.34100   33.20600 1.000 36.96629 ?  221 SER   A CA   1 
ATOM   367  C  C    . SER   A 1 69  ? 2.38100  8.46300   31.86800 1.000 37.65224 ?  221 SER   A C    1 
ATOM   368  O  O    . SER   A 1 69  ? 1.77300  8.93000   30.89900 1.000 35.78058 ?  221 SER   A O    1 
ATOM   369  C  CB   . SER   A 1 69  ? 1.64600  9.69800   33.91100 1.000 40.20897 ?  221 SER   A CB   1 
ATOM   370  O  OG   . SER   A 1 69  ? 2.95900  10.19700  34.11400 1.000 42.28909 ?  221 SER   A OG   1 
ATOM   371  N  N    . MET   A 1 70  ? 3.64700  8.06500   31.78500 1.000 30.14829 ?  222 MET   A N    1 
ATOM   372  C  CA   . MET   A 1 70  ? 4.38100  8.13200   30.52800 1.000 26.56565 ?  222 MET   A CA   1 
ATOM   373  C  C    . MET   A 1 70  ? 4.33000  6.83200   29.73800 1.000 25.19267 ?  222 MET   A C    1 
ATOM   374  O  O    . MET   A 1 70  ? 4.88000  6.77600   28.63300 1.000 29.51782 ?  222 MET   A O    1 
ATOM   375  C  CB   . MET   A 1 70  ? 5.84400  8.51300   30.78500 1.000 31.03907 ?  222 MET   A CB   1 
ATOM   376  C  CG   . MET   A 1 70  ? 6.05200  9.97300   31.14400 1.000 33.82084 ?  222 MET   A CG   1 
ATOM   377  S  SD   . MET   A 1 70  ? 5.60700  11.09100  29.79900 1.000 31.10918 ?  222 MET   A SD   1 
ATOM   378  C  CE   . MET   A 1 70  ? 6.89200  10.72900  28.60500 1.000 32.87836 ?  222 MET   A CE   1 
ATOM   379  N  N    . LEU   A 1 71  ? 3.68200  5.79500   30.27100 1.000 27.16420 ?  223 LEU   A N    1 
ATOM   380  C  CA   . LEU   A 1 71  ? 3.63300  4.51200   29.57000 1.000 26.18165 ?  223 LEU   A CA   1 
ATOM   381  C  C    . LEU   A 1 71  ? 2.96000  4.59900   28.20600 1.000 25.90292 ?  223 LEU   A C    1 
ATOM   382  O  O    . LEU   A 1 71  ? 3.52100  4.05800   27.23700 1.000 28.43334 ?  223 LEU   A O    1 
ATOM   383  C  CB   . LEU   A 1 71  ? 2.95600  3.46100   30.45700 1.000 27.62915 ?  223 LEU   A CB   1 
ATOM   384  C  CG   . LEU   A 1 71  ? 2.91300  2.04900   29.85800 1.000 29.08302 ?  223 LEU   A CG   1 
ATOM   385  C  CD1  . LEU   A 1 71  ? 4.30100  1.61500   29.41300 1.000 26.85405 ?  223 LEU   A CD1  1 
ATOM   386  C  CD2  . LEU   A 1 71  ? 2.31600  1.04200   30.83100 1.000 30.97467 ?  223 LEU   A CD2  1 
ATOM   387  N  N    . PRO   A 1 72  ? 1.78500  5.22400   28.04400 1.000 25.04807 ?  224 PRO   A N    1 
ATOM   388  C  CA   . PRO   A 1 72  ? 1.20000  5.29100   26.69000 1.000 24.30743 ?  224 PRO   A CA   1 
ATOM   389  C  C    . PRO   A 1 72  ? 2.10500  5.97000   25.67600 1.000 27.14524 ?  224 PRO   A C    1 
ATOM   390  O  O    . PRO   A 1 72  ? 2.30200  5.44300   24.57300 1.000 24.92873 ?  224 PRO   A O    1 
ATOM   391  C  CB   . PRO   A 1 72  ? -0.09900 6.07700   26.91600 1.000 27.70873 ?  224 PRO   A CB   1 
ATOM   392  C  CG   . PRO   A 1 72  ? -0.44600 5.82700   28.34200 1.000 29.00740 ?  224 PRO   A CG   1 
ATOM   393  C  CD   . PRO   A 1 72  ? 0.86500  5.77900   29.05900 1.000 28.02138 ?  224 PRO   A CD   1 
ATOM   394  N  N    . HIS   A 1 73  ? 2.66700  7.13100   26.02200 1.000 28.41533 ?  225 HIS   A N    1 
ATOM   395  C  CA   . HIS   A 1 73  ? 3.51200  7.85300   25.07500 1.000 28.79134 ?  225 HIS   A CA   1 
ATOM   396  C  C    . HIS   A 1 73  ? 4.77200  7.06600   24.74300 1.000 28.66178 ?  225 HIS   A C    1 
ATOM   397  O  O    . HIS   A 1 73  ? 5.15700  6.96300   23.57200 1.000 26.81997 ?  225 HIS   A O    1 
ATOM   398  C  CB   . HIS   A 1 73  ? 3.87800  9.22600   25.63500 1.000 27.19676 ?  225 HIS   A CB   1 
ATOM   399  C  CG   . HIS   A 1 73  ? 4.78300  10.01900  24.74200 1.000 28.48343 ?  225 HIS   A CG   1 
ATOM   400  N  ND1  . HIS   A 1 73  ? 4.34000  10.64300  23.59600 1.000 26.42939 ?  225 HIS   A ND1  1 
ATOM   401  C  CD2  . HIS   A 1 73  ? 6.10800  10.28700  24.82900 1.000 26.45209 ?  225 HIS   A CD2  1 
ATOM   402  C  CE1  . HIS   A 1 73  ? 5.35300  11.26200  23.01500 1.000 28.35574 ?  225 HIS   A CE1  1 
ATOM   403  N  NE2  . HIS   A 1 73  ? 6.43700  11.06100  23.74200 1.000 27.95126 ?  225 HIS   A NE2  1 
ATOM   404  N  N    . LEU   A 1 74  ? 5.43000  6.50400   25.75800 1.000 24.45881 ?  226 LEU   A N    1 
ATOM   405  C  CA   . LEU   A 1 74  ? 6.67300  5.78600   25.51100 1.000 23.70242 ?  226 LEU   A CA   1 
ATOM   406  C  C    . LEU   A 1 74  ? 6.43000  4.43500   24.85500 1.000 20.26336 ?  226 LEU   A C    1 
ATOM   407  O  O    . LEU   A 1 74  ? 7.31200  3.92800   24.15200 1.000 22.00036 ?  226 LEU   A O    1 
ATOM   408  C  CB   . LEU   A 1 74  ? 7.45300  5.61800   26.81700 1.000 29.05395 ?  226 LEU   A CB   1 
ATOM   409  C  CG   . LEU   A 1 74  ? 8.00700  6.92900   27.38100 1.000 31.20728 ?  226 LEU   A CG   1 
ATOM   410  C  CD1  . LEU   A 1 74  ? 8.86800  6.68600   28.61400 1.000 30.71285 ?  226 LEU   A CD1  1 
ATOM   411  C  CD2  . LEU   A 1 74  ? 8.78100  7.69800   26.31800 1.000 26.82378 ?  226 LEU   A CD2  1 
ATOM   412  N  N    . ALA   A 1 75  ? 5.25000  3.84200   25.05700 1.000 22.45560 ?  227 ALA   A N    1 
ATOM   413  C  CA   . ALA   A 1 75  ? 4.90600  2.63700   24.30800 1.000 21.74967 ?  227 ALA   A CA   1 
ATOM   414  C  C    . ALA   A 1 75  ? 4.75800  2.94300   22.82400 1.000 21.44713 ?  227 ALA   A C    1 
ATOM   415  O  O    . ALA   A 1 75  ? 5.22000  2.17300   21.97400 1.000 22.99366 ?  227 ALA   A O    1 
ATOM   416  C  CB   . ALA   A 1 75  ? 3.61900  2.01900   24.85800 1.000 21.59159 ?  227 ALA   A CB   1 
ATOM   417  N  N    . ASP   A 1 76  ? 4.11300  4.06500   22.49300 1.000 21.50193 ?  228 ASP   A N    1 
ATOM   418  C  CA   . ASP   A 1 76  ? 4.00400  4.47400   21.09600 1.000 21.20777 ?  228 ASP   A CA   1 
ATOM   419  C  C    . ASP   A 1 76  ? 5.37100  4.81000   20.51600 1.000 24.12684 ?  228 ASP   A C    1 
ATOM   420  O  O    . ASP   A 1 76  ? 5.66800  4.47700   19.36200 1.000 21.29529 ?  228 ASP   A O    1 
ATOM   421  C  CB   . ASP   A 1 76  ? 3.06600  5.67400   20.97200 1.000 23.55506 ?  228 ASP   A CB   1 
ATOM   422  C  CG   . ASP   A 1 76  ? 1.61500  5.30400   21.18000 1.000 27.18515 ?  228 ASP   A CG   1 
ATOM   423  O  OD1  . ASP   A 1 76  ? 0.79400  6.22000   21.39200 1.000 27.51961 ?  228 ASP   A OD1  1 
ATOM   424  O  OD2  . ASP   A 1 76  ? 1.29100  4.09800   21.12800 1.000 25.18327 ?  228 ASP   A OD2  1 
ATOM   425  N  N    . LEU   A 1 77  ? 6.21700  5.47400   21.30400 1.000 20.47676 ?  229 LEU   A N    1 
ATOM   426  C  CA   . LEU   A 1 77  ? 7.57000  5.79000   20.85800 1.000 20.90057 ?  229 LEU   A CA   1 
ATOM   427  C  C    . LEU   A 1 77  ? 8.35900  4.52100   20.55700 1.000 25.54377 ?  229 LEU   A C    1 
ATOM   428  O  O    . LEU   A 1 77  ? 9.01200  4.41200   19.51300 1.000 23.28427 ?  229 LEU   A O    1 
ATOM   429  C  CB   . LEU   A 1 77  ? 8.27700  6.62600   21.92700 1.000 21.43016 ?  229 LEU   A CB   1 
ATOM   430  C  CG   . LEU   A 1 77  ? 9.77600  6.87900   21.75500 1.000 28.07505 ?  229 LEU   A CG   1 
ATOM   431  C  CD1  . LEU   A 1 77  ? 10.05700 7.53800   20.41600 1.000 23.32748 ?  229 LEU   A CD1  1 
ATOM   432  C  CD2  . LEU   A 1 77  ? 10.33100 7.72200   22.90100 1.000 30.04695 ?  229 LEU   A CD2  1 
ATOM   433  N  N    . VAL   A 1 78  ? 8.31000  3.55000   21.47300 1.000 21.16772 ?  230 VAL   A N    1 
ATOM   434  C  CA   . VAL   A 1 78  ? 9.04100  2.30000   21.28800 1.000 22.05373 ?  230 VAL   A CA   1 
ATOM   435  C  C    . VAL   A 1 78  ? 8.48800  1.52700   20.09900 1.000 22.83869 ?  230 VAL   A C    1 
ATOM   436  O  O    . VAL   A 1 78  ? 9.24600  0.99800   19.27600 1.000 23.01817 ?  230 VAL   A O    1 
ATOM   437  C  CB   . VAL   A 1 78  ? 8.99000  1.46400   22.58000 1.000 26.79269 ?  230 VAL   A CB   1 
ATOM   438  C  CG1  . VAL   A 1 78  ? 9.43300  0.03200   22.31300 1.000 27.41127 ?  230 VAL   A CG1  1 
ATOM   439  C  CG2  . VAL   A 1 78  ? 9.84400  2.11200   23.64600 1.000 25.19427 ?  230 VAL   A CG2  1 
ATOM   440  N  N    . SER   A 1 79  ? 7.15800  1.44700   19.99100 1.000 21.87129 ?  231 SER   A N    1 
ATOM   441  C  CA   . SER   A 1 79  ? 6.54000  0.76400   18.85700 1.000 19.90003 ?  231 SER   A CA   1 
ATOM   442  C  C    . SER   A 1 79  ? 6.96100  1.39900   17.53900 1.000 21.06909 ?  231 SER   A C    1 
ATOM   443  O  O    . SER   A 1 79  ? 7.29000  0.69600   16.57700 1.000 20.10425 ?  231 SER   A O    1 
ATOM   444  C  CB   . SER   A 1 79  ? 5.01900  0.79400   19.00700 1.000 22.08077 ?  231 SER   A CB   1 
ATOM   445  O  OG   . SER   A 1 79  ? 4.39500  -0.18200  18.19200 1.000 26.91920 ?  231 SER   A OG   1 
ATOM   446  N  N    . TYR   A 1 80  ? 6.95100  2.73100   17.48000 1.000 18.84876 ?  232 TYR   A N    1 
ATOM   447  C  CA   . TYR   A 1 80  ? 7.42200  3.44900   16.30100 1.000 19.27845 ?  232 TYR   A CA   1 
ATOM   448  C  C    . TYR   A 1 80  ? 8.86900  3.09100   15.98200 1.000 23.73226 ?  232 TYR   A C    1 
ATOM   449  O  O    . TYR   A 1 80  ? 9.21800  2.82400   14.82500 1.000 19.63730 ?  232 TYR   A O    1 
ATOM   450  C  CB   . TYR   A 1 80  ? 7.26600  4.95000   16.54400 1.000 20.19728 ?  232 TYR   A CB   1 
ATOM   451  C  CG   . TYR   A 1 80  ? 7.79800  5.85200   15.45800 1.000 23.31373 ?  232 TYR   A CG   1 
ATOM   452  C  CD1  . TYR   A 1 80  ? 7.04300  6.13400   14.32900 1.000 23.88006 ?  232 TYR   A CD1  1 
ATOM   453  C  CD2  . TYR   A 1 80  ? 9.04900  6.44100   15.57800 1.000 24.40326 ?  232 TYR   A CD2  1 
ATOM   454  C  CE1  . TYR   A 1 80  ? 7.52600  6.97100   13.34100 1.000 30.10029 ?  232 TYR   A CE1  1 
ATOM   455  C  CE2  . TYR   A 1 80  ? 9.54100  7.27600   14.59500 1.000 28.44445 ?  232 TYR   A CE2  1 
ATOM   456  C  CZ   . TYR   A 1 80  ? 8.77400  7.53900   13.47700 1.000 31.26441 ?  232 TYR   A CZ   1 
ATOM   457  O  OH   . TYR   A 1 80  ? 9.26000  8.37200   12.49500 1.000 36.57594 ?  232 TYR   A OH   1 
ATOM   458  N  N    . SER   A 1 81  ? 9.72600  3.06900   17.00700 1.000 22.38851 ?  233 SER   A N    1 
ATOM   459  C  CA   . SER   A 1 81  ? 11.14200 2.79100   16.78900 1.000 24.22542 ?  233 SER   A CA   1 
ATOM   460  C  C    . SER   A 1 81  ? 11.36500 1.36000   16.32000 1.000 23.03329 ?  233 SER   A C    1 
ATOM   461  O  O    . SER   A 1 81  ? 12.27100 1.09800   15.52100 1.000 22.99871 ?  233 SER   A O    1 
ATOM   462  C  CB   . SER   A 1 81  ? 11.92800 3.05400   18.07000 1.000 25.15832 ?  233 SER   A CB   1 
ATOM   463  O  OG   . SER   A 1 81  ? 13.32100 3.12500   17.82200 1.000 28.16874 ?  233 SER   A OG   1 
ATOM   464  N  N    . ILE   A 1 82  ? 10.55900 0.41900   16.81700 1.000 21.05381 ?  234 ILE   A N    1 
ATOM   465  C  CA   . ILE   A 1 82  ? 10.66500 -0.96200  16.35500 1.000 21.94567 ?  234 ILE   A CA   1 
ATOM   466  C  C    . ILE   A 1 82  ? 10.45300 -1.02700  14.84800 1.000 23.01952 ?  234 ILE   A C    1 
ATOM   467  O  O    . ILE   A 1 82  ? 11.18200 -1.72000  14.12800 1.000 20.35863 ?  234 ILE   A O    1 
ATOM   468  C  CB   . ILE   A 1 82  ? 9.66300  -1.86100  17.10200 1.000 20.43525 ?  234 ILE   A CB   1 
ATOM   469  C  CG1  . ILE   A 1 82  ? 10.08600 -2.04000  18.55900 1.000 23.24108 ?  234 ILE   A CG1  1 
ATOM   470  C  CG2  . ILE   A 1 82  ? 9.54800  -3.21800  16.42600 1.000 21.82443 ?  234 ILE   A CG2  1 
ATOM   471  C  CD1  . ILE   A 1 82  ? 9.03000  -2.71900  19.41100 1.000 27.92878 ?  234 ILE   A CD1  1 
ATOM   472  N  N    . GLN   A 1 83  ? 9.44900  -0.30000  14.35200 1.000 21.14111 ?  235 GLN   A N    1 
ATOM   473  C  CA   . GLN   A 1 83  ? 9.20800  -0.25100  12.91400 1.000 23.92902 ?  235 GLN   A CA   1 
ATOM   474  C  C    . GLN   A 1 83  ? 10.42400 0.28200   12.16700 1.000 24.26072 ?  235 GLN   A C    1 
ATOM   475  O  O    . GLN   A 1 83  ? 10.77900 -0.22900  11.09900 1.000 23.21762 ?  235 GLN   A O    1 
ATOM   476  C  CB   . GLN   A 1 83  ? 7.98100  0.61300   12.61900 1.000 24.99969 ?  235 GLN   A CB   1 
ATOM   477  C  CG   . GLN   A 1 83  ? 6.68900  0.11100   13.23600 1.000 25.68382 ?  235 GLN   A CG   1 
ATOM   478  C  CD   . GLN   A 1 83  ? 5.49300  0.96000   12.85000 1.000 33.08326 ?  235 GLN   A CD   1 
ATOM   479  O  OE1  . GLN   A 1 83  ? 5.26400  1.22400   11.67000 1.000 35.63641 ?  235 GLN   A OE1  1 
ATOM   480  N  NE2  . GLN   A 1 83  ? 4.72500  1.39200   13.84300 1.000 37.27060 ?  235 GLN   A NE2  1 
ATOM   481  N  N    . LYS   A 1 84  ? 11.07400 1.31400   12.71100 1.000 22.32907 ?  236 LYS   A N    1 
ATOM   482  C  CA   . LYS   A 1 84  ? 12.26600 1.86000   12.07000 1.000 23.22833 ?  236 LYS   A CA   1 
ATOM   483  C  C    . LYS   A 1 84  ? 13.41600 0.86100   12.10400 1.000 23.01424 ?  236 LYS   A C    1 
ATOM   484  O  O    . LYS   A 1 84  ? 14.15500 0.72400   11.12200 1.000 24.24583 ?  236 LYS   A O    1 
ATOM   485  C  CB   . LYS   A 1 84  ? 12.66900 3.17300   12.74300 1.000 21.77272 ?  236 LYS   A CB   1 
ATOM   486  C  CG   . LYS   A 1 84  ? 11.59700 4.25100   12.68000 1.000 28.71809 ?  236 LYS   A CG   1 
ATOM   487  C  CD   . LYS   A 1 84  ? 11.07100 4.42100   11.26600 1.000 32.76894 ?  236 LYS   A CD   1 
ATOM   488  C  CE   . LYS   A 1 84  ? 10.48900 5.81000   11.05900 1.000 36.65540 ?  236 LYS   A CE   1 
ATOM   489  N  NZ   . LYS   A 1 84  ? 11.52800 6.87400   11.13800 1.000 34.48570 ?  236 LYS   A NZ   1 
ATOM   490  N  N    . VAL   A 1 85  ? 13.57300 0.14800   13.22300 1.000 19.86657 ?  237 VAL   A N    1 
ATOM   491  C  CA   . VAL   A 1 85  ? 14.64200 -0.84100  13.33700 1.000 25.45136 ?  237 VAL   A CA   1 
ATOM   492  C  C    . VAL   A 1 85  ? 14.45200 -1.95200  12.31300 1.000 24.72791 ?  237 VAL   A C    1 
ATOM   493  O  O    . VAL   A 1 85  ? 15.41900 -2.42600  11.70300 1.000 24.65594 ?  237 VAL   A O    1 
ATOM   494  C  CB   . VAL   A 1 85  ? 14.71000 -1.39100  14.77600 1.000 23.52334 ?  237 VAL   A CB   1 
ATOM   495  C  CG1  . VAL   A 1 85  ? 15.63800 -2.59900  14.84900 1.000 22.66100 ?  237 VAL   A CG1  1 
ATOM   496  C  CG2  . VAL   A 1 85  ? 15.16800 -0.30500  15.73900 1.000 23.37243 ?  237 VAL   A CG2  1 
ATOM   497  N  N    . ILE   A 1 86  ? 13.20500 -2.37800  12.09800 1.000 20.16997 ?  238 ILE   A N    1 
ATOM   498  C  CA   . ILE   A 1 86  ? 12.93100 -3.40500  11.09600 1.000 19.44004 ?  238 ILE   A CA   1 
ATOM   499  C  C    . ILE   A 1 86  ? 13.29400 -2.89900  9.70600  1.000 21.96639 ?  238 ILE   A C    1 
ATOM   500  O  O    . ILE   A 1 86  ? 13.90100 -3.62000  8.90300  1.000 26.19258 ?  238 ILE   A O    1 
ATOM   501  C  CB   . ILE   A 1 86  ? 11.45500 -3.84100  11.16600 1.000 21.15382 ?  238 ILE   A CB   1 
ATOM   502  C  CG1  . ILE   A 1 86  ? 11.17100 -4.58400  12.47000 1.000 24.84974 ?  238 ILE   A CG1  1 
ATOM   503  C  CG2  . ILE   A 1 86  ? 11.10100 -4.72200  9.97700  1.000 24.88667 ?  238 ILE   A CG2  1 
ATOM   504  C  CD1  . ILE   A 1 86  ? 9.71700  -4.51600  12.89400 1.000 25.14616 ?  238 ILE   A CD1  1 
ATOM   505  N  N    . GLY   A 1 87  ? 12.92700 -1.65300  9.39800  1.000 21.19070 ?  239 GLY   A N    1 
ATOM   506  C  CA   . GLY   A 1 87  ? 13.26600 -1.09000  8.10200  1.000 24.04574 ?  239 GLY   A CA   1 
ATOM   507  C  C    . GLY   A 1 87  ? 14.76400 -1.01700  7.87600  1.000 24.16370 ?  239 GLY   A C    1 
ATOM   508  O  O    . GLY   A 1 87  ? 15.24800 -1.26500  6.76900  1.000 26.67342 ?  239 GLY   A O    1 
ATOM   509  N  N    . PHE   A 1 88  ? 15.51500 -0.68000  8.92300  1.000 23.03445 ?  240 PHE   A N    1 
ATOM   510  C  CA   . PHE   A 1 88  ? 16.97000 -0.66000  8.82300  1.000 21.96326 ?  240 PHE   A CA   1 
ATOM   511  C  C    . PHE   A 1 88  ? 17.52200 -2.06700  8.62900  1.000 21.64518 ?  240 PHE   A C    1 
ATOM   512  O  O    . PHE   A 1 88  ? 18.38000 -2.29700  7.76900  1.000 24.45426 ?  240 PHE   A O    1 
ATOM   513  C  CB   . PHE   A 1 88  ? 17.55700 -0.01500  10.07800 1.000 19.29642 ?  240 PHE   A CB   1 
ATOM   514  C  CG   . PHE   A 1 88  ? 19.05800 -0.04800  10.13700 1.000 23.13713 ?  240 PHE   A CG   1 
ATOM   515  C  CD1  . PHE   A 1 88  ? 19.80800 0.87700   9.43100  1.000 23.14879 ?  240 PHE   A CD1  1 
ATOM   516  C  CD2  . PHE   A 1 88  ? 19.71400 -0.99000  10.91400 1.000 23.71424 ?  240 PHE   A CD2  1 
ATOM   517  C  CE1  . PHE   A 1 88  ? 21.19800 0.85800   9.48900  1.000 23.51262 ?  240 PHE   A CE1  1 
ATOM   518  C  CE2  . PHE   A 1 88  ? 21.10600 -1.01900  10.97400 1.000 21.65023 ?  240 PHE   A CE2  1 
ATOM   519  C  CZ   . PHE   A 1 88  ? 21.84900 -0.09000  10.26000 1.000 23.39255 ?  240 PHE   A CZ   1 
ATOM   520  N  N    . ALA   A 1 89  ? 17.02800 -3.02300  9.42000  1.000 22.49978 ?  241 ALA   A N    1 
ATOM   521  C  CA   . ALA   A 1 89  ? 17.54800 -4.38700  9.36200  1.000 25.05519 ?  241 ALA   A CA   1 
ATOM   522  C  C    . ALA   A 1 89  ? 17.37000 -4.99800  7.97900  1.000 27.41865 ?  241 ALA   A C    1 
ATOM   523  O  O    . ALA   A 1 89  ? 18.25000 -5.72200  7.49600  1.000 26.16066 ?  241 ALA   A O    1 
ATOM   524  C  CB   . ALA   A 1 89  ? 16.86000 -5.25200  10.41600 1.000 25.75337 ?  241 ALA   A CB   1 
ATOM   525  N  N    . LYS   A 1 90  ? 16.23800 -4.71800  7.32500  1.000 23.59458 ?  242 LYS   A N    1 
ATOM   526  C  CA   . LYS   A 1 90  ? 15.98200 -5.27100  5.99900  1.000 23.68527 ?  242 LYS   A CA   1 
ATOM   527  C  C    . LYS   A 1 90  ? 17.02100 -4.83900  4.97400  1.000 28.69382 ?  242 LYS   A C    1 
ATOM   528  O  O    . LYS   A 1 90  ? 17.17700 -5.50900  3.94800  1.000 31.33503 ?  242 LYS   A O    1 
ATOM   529  C  CB   . LYS   A 1 90  ? 14.58300 -4.86100  5.52100  1.000 26.12820 ?  242 LYS   A CB   1 
ATOM   530  C  CG   . LYS   A 1 90  ? 13.44500 -5.58100  6.22600  1.000 36.92979 ?  242 LYS   A CG   1 
ATOM   531  C  CD   . LYS   A 1 90  ? 12.14100 -4.82000  6.07100  1.000 39.19459 ?  242 LYS   A CD   1 
ATOM   532  C  CE   . LYS   A 1 90  ? 11.63700 -4.86600  4.63400  1.000 39.87764 ?  242 LYS   A CE   1 
ATOM   533  N  NZ   . LYS   A 1 90  ? 10.39200 -4.06700  4.45600  1.000 38.14605 ?  242 LYS   A NZ   1 
ATOM   534  N  N    . MET   A 1 91  ? 17.74100 -3.74700  5.22600  1.000 25.68687 ?  243 MET   A N    1 
ATOM   535  C  CA   . MET   A 1 91  ? 18.72700 -3.23000  4.28600  1.000 32.98565 ?  243 MET   A CA   1 
ATOM   536  C  C    . MET   A 1 91  ? 20.15600 -3.62600  4.63600  1.000 30.50135 ?  243 MET   A C    1 
ATOM   537  O  O    . MET   A 1 91  ? 21.07600 -3.29100  3.88400  1.000 33.34947 ?  243 MET   A O    1 
ATOM   538  C  CB   . MET   A 1 91  ? 18.61600 -1.70500  4.20000  1.000 36.45219 ?  243 MET   A CB   1 
ATOM   539  C  CG   . MET   A 1 91  ? 17.24300 -1.21600  3.77800  1.000 45.60442 ?  243 MET   A CG   1 
ATOM   540  S  SD   . MET   A 1 91  ? 17.18300 0.54700   3.40000  1.000 49.30543 ?  243 MET   A SD   1 
ATOM   541  C  CE   . MET   A 1 91  ? 16.22300 1.16700   4.78100  1.000 46.34717 ?  243 MET   A CE   1 
ATOM   542  N  N    . ILE   A 1 92  ? 20.36300 -4.32600  5.74400  1.000 27.71673 ?  244 ILE   A N    1 
ATOM   543  C  CA   . ILE   A 1 92  ? 21.70400 -4.82400  6.07000  1.000 25.82992 ?  244 ILE   A CA   1 
ATOM   544  C  C    . ILE   A 1 92  ? 22.12300 -5.84400  5.01600  1.000 30.46724 ?  244 ILE   A C    1 
ATOM   545  O  O    . ILE   A 1 92  ? 21.35500 -6.78100  4.72700  1.000 30.94854 ?  244 ILE   A O    1 
ATOM   546  C  CB   . ILE   A 1 92  ? 21.72000 -5.44500  7.46600  1.000 27.27818 ?  244 ILE   A CB   1 
ATOM   547  C  CG1  . ILE   A 1 92  ? 21.32700 -4.41600  8.52500  1.000 23.01828 ?  244 ILE   A CG1  1 
ATOM   548  C  CG2  . ILE   A 1 92  ? 23.09800 -6.01100  7.78000  1.000 23.93372 ?  244 ILE   A CG2  1 
ATOM   549  C  CD1  . ILE   A 1 92  ? 21.13700 -5.01800  9.90300  1.000 22.65201 ?  244 ILE   A CD1  1 
ATOM   550  N  N    . PRO   A 1 93  ? 23.30300 -5.70200  4.40900  1.000 30.14551 ?  245 PRO   A N    1 
ATOM   551  C  CA   . PRO   A 1 93  ? 23.75400 -6.69600  3.42600  1.000 32.61108 ?  245 PRO   A CA   1 
ATOM   552  C  C    . PRO   A 1 93  ? 23.78400 -8.09300  4.02600  1.000 37.60319 ?  245 PRO   A C    1 
ATOM   553  O  O    . PRO   A 1 93  ? 24.43300 -8.33900  5.04500  1.000 35.79895 ?  245 PRO   A O    1 
ATOM   554  C  CB   . PRO   A 1 93  ? 25.16000 -6.20900  3.05700  1.000 37.02974 ?  245 PRO   A CB   1 
ATOM   555  C  CG   . PRO   A 1 93  ? 25.10800 -4.73900  3.27700  1.000 36.09185 ?  245 PRO   A CG   1 
ATOM   556  C  CD   . PRO   A 1 93  ? 24.21100 -4.54400  4.47600  1.000 32.06528 ?  245 PRO   A CD   1 
ATOM   557  N  N    . GLY   A 1 94  ? 23.06300 -9.01000  3.38400  1.000 39.46712 ?  246 GLY   A N    1 
ATOM   558  C  CA   . GLY   A 1 94  ? 22.98000 -10.38100 3.82400  1.000 38.00965 ?  246 GLY   A CA   1 
ATOM   559  C  C    . GLY   A 1 94  ? 21.76400 -10.71800 4.66200  1.000 36.71794 ?  246 GLY   A C    1 
ATOM   560  O  O    . GLY   A 1 94  ? 21.39100 -11.89300 4.73400  1.000 42.59953 ?  246 GLY   A O    1 
ATOM   561  N  N    . PHE   A 1 95  ? 21.12600 -9.72100  5.28300  1.000 33.93786 ?  247 PHE   A N    1 
ATOM   562  C  CA   . PHE   A 1 95  ? 20.05700 -10.00100 6.23900  1.000 33.50141 ?  247 PHE   A CA   1 
ATOM   563  C  C    . PHE   A 1 95  ? 18.90300 -10.76200 5.59400  1.000 42.65445 ?  247 PHE   A C    1 
ATOM   564  O  O    . PHE   A 1 95  ? 18.37100 -11.71000 6.18300  1.000 41.55449 ?  247 PHE   A O    1 
ATOM   565  C  CB   . PHE   A 1 95  ? 19.55600 -8.69900  6.86400  1.000 29.90623 ?  247 PHE   A CB   1 
ATOM   566  C  CG   . PHE   A 1 95  ? 18.50900 -8.90100  7.92200  1.000 33.95873 ?  247 PHE   A CG   1 
ATOM   567  C  CD1  . PHE   A 1 95  ? 18.86800 -9.24900  9.21600  1.000 30.14479 ?  247 PHE   A CD1  1 
ATOM   568  C  CD2  . PHE   A 1 95  ? 17.16300 -8.74800  7.62300  1.000 28.65636 ?  247 PHE   A CD2  1 
ATOM   569  C  CE1  . PHE   A 1 95  ? 17.90300 -9.43800  10.19300 1.000 29.11047 ?  247 PHE   A CE1  1 
ATOM   570  C  CE2  . PHE   A 1 95  ? 16.19100 -8.93500  8.59100  1.000 29.04872 ?  247 PHE   A CE2  1 
ATOM   571  C  CZ   . PHE   A 1 95  ? 16.56100 -9.28000  9.87900  1.000 27.68680 ?  247 PHE   A CZ   1 
ATOM   572  N  N    A ARG   A 1 96  ? 18.49900 -10.36500 4.38800  0.600 40.29132 ?  248 ARG   A N    1 
ATOM   573  N  N    B ARG   A 1 96  ? 18.50200 -10.36300 4.38700  0.400 41.32352 ?  248 ARG   A N    1 
ATOM   574  C  CA   A ARG   A 1 96  ? 17.38900 -11.03000 3.71800  0.600 46.56344 ?  248 ARG   A CA   1 
ATOM   575  C  CA   B ARG   A 1 96  ? 17.39700 -11.01600 3.69700  0.400 46.25822 ?  248 ARG   A CA   1 
ATOM   576  C  C    A ARG   A 1 96  ? 17.77800 -12.37500 3.11700  0.600 47.13104 ?  248 ARG   A C    1 
ATOM   577  C  C    B ARG   A 1 96  ? 17.78000 -12.36800 3.10800  0.400 47.22934 ?  248 ARG   A C    1 
ATOM   578  O  O    A ARG   A 1 96  ? 16.91100 -13.06300 2.56600  0.600 48.67164 ?  248 ARG   A O    1 
ATOM   579  O  O    B ARG   A 1 96  ? 16.91200 -13.05400 2.55700  0.400 48.60015 ?  248 ARG   A O    1 
ATOM   580  C  CB   A ARG   A 1 96  ? 16.80300 -10.12100 2.63600  0.600 49.30222 ?  248 ARG   A CB   1 
ATOM   581  C  CB   B ARG   A 1 96  ? 16.84800 -10.10100 2.60000  0.400 49.39458 ?  248 ARG   A CB   1 
ATOM   582  C  CG   A ARG   A 1 96  ? 15.91800 -9.01700  3.18900  0.600 51.23810 ?  248 ARG   A CG   1 
ATOM   583  C  CG   B ARG   A 1 96  ? 16.29400 -8.78500  3.12700  0.400 50.68705 ?  248 ARG   A CG   1 
ATOM   584  C  CD   A ARG   A 1 96  ? 14.43900 -9.31800  2.98700  0.600 55.55933 ?  248 ARG   A CD   1 
ATOM   585  C  CD   B ARG   A 1 96  ? 14.85800 -8.54800  2.67900  0.400 54.07755 ?  248 ARG   A CD   1 
ATOM   586  N  NE   A ARG   A 1 96  ? 14.05700 -10.62500 3.51200  0.600 58.34260 ?  248 ARG   A NE   1 
ATOM   587  N  NE   B ARG   A 1 96  ? 14.00400 -9.71400  2.88900  0.400 56.33668 ?  248 ARG   A NE   1 
ATOM   588  C  CZ   A ARG   A 1 96  ? 13.58800 -11.61900 2.76500  0.600 56.74330 ?  248 ARG   A CZ   1 
ATOM   589  C  CZ   B ARG   A 1 96  ? 13.31700 -9.94900  4.00300  0.400 53.44606 ?  248 ARG   A CZ   1 
ATOM   590  N  NH1  A ARG   A 1 96  ? 13.44300 -11.45400 1.45800  0.600 59.61553 ?  248 ARG   A NH1  1 
ATOM   591  N  NH1  B ARG   A 1 96  ? 12.56400 -11.03600 4.10200  0.400 55.39210 ?  248 ARG   A NH1  1 
ATOM   592  N  NH2  A ARG   A 1 96  ? 13.26200 -12.77900 3.32100  0.600 57.43532 ?  248 ARG   A NH2  1 
ATOM   593  N  NH2  B ARG   A 1 96  ? 13.38100 -9.09800  5.01800  0.400 39.93090 ?  248 ARG   A NH2  1 
ATOM   594  N  N    . ASP   A 1 97  ? 19.05100 -12.76400 3.20200  1.000 46.18152 ?  249 ASP   A N    1 
ATOM   595  C  CA   . ASP   A 1 97  ? 19.45100 -14.11400 2.83000  1.000 49.84712 ?  249 ASP   A CA   1 
ATOM   596  C  C    . ASP   A 1 97  ? 19.05700 -15.13100 3.89200  1.000 49.32152 ?  249 ASP   A C    1 
ATOM   597  O  O    . ASP   A 1 97  ? 19.05100 -16.33500 3.61400  1.000 46.19317 ?  249 ASP   A O    1 
ATOM   598  C  CB   . ASP   A 1 97  ? 20.96300 -14.18300 2.59700  1.000 58.41575 ?  249 ASP   A CB   1 
ATOM   599  C  CG   . ASP   A 1 97  ? 21.38700 -13.53700 1.29400  1.000 63.11103 ?  249 ASP   A CG   1 
ATOM   600  O  OD1  . ASP   A 1 97  ? 20.50600 -13.19200 0.48000  1.000 66.96889 ?  249 ASP   A OD1  1 
ATOM   601  O  OD2  . ASP   A 1 97  ? 22.60800 -13.37400 1.08700  1.000 64.87531 ?  249 ASP   A OD2  1 
ATOM   602  N  N    . LEU   A 1 98  ? 18.73800 -14.66900 5.09800  1.000 39.52346 ?  250 LEU   A N    1 
ATOM   603  C  CA   . LEU   A 1 98  ? 18.30200 -15.52700 6.18500  1.000 38.69820 ?  250 LEU   A CA   1 
ATOM   604  C  C    . LEU   A 1 98  ? 16.86000 -15.97200 5.96800  1.000 40.61934 ?  250 LEU   A C    1 
ATOM   605  O  O    . LEU   A 1 98  ? 16.09800 -15.35900 5.21700  1.000 42.15582 ?  250 LEU   A O    1 
ATOM   606  C  CB   . LEU   A 1 98  ? 18.41300 -14.79100 7.52100  1.000 30.25815 ?  250 LEU   A CB   1 
ATOM   607  C  CG   . LEU   A 1 98  ? 19.81300 -14.36000 7.95100  1.000 30.12558 ?  250 LEU   A CG   1 
ATOM   608  C  CD1  . LEU   A 1 98  ? 19.73100 -13.26200 8.99200  1.000 31.60956 ?  250 LEU   A CD1  1 
ATOM   609  C  CD2  . LEU   A 1 98  ? 20.58200 -15.55100 8.48600  1.000 35.96565 ?  250 LEU   A CD2  1 
ATOM   610  N  N    . THR   A 1 99  ? 16.49000 -17.05900 6.64000  1.000 39.52496 ?  251 THR   A N    1 
ATOM   611  C  CA   . THR   A 1 99  ? 15.09900 -17.47900 6.64100  1.000 39.50549 ?  251 THR   A CA   1 
ATOM   612  C  C    . THR   A 1 99  ? 14.23700 -16.45700 7.37900  1.000 35.58093 ?  251 THR   A C    1 
ATOM   613  O  O    . THR   A 1 99  ? 14.72800 -15.63900 8.16600  1.000 31.77513 ?  251 THR   A O    1 
ATOM   614  C  CB   . THR   A 1 99  ? 14.93700 -18.85200 7.29600  1.000 45.36632 ?  251 THR   A CB   1 
ATOM   615  O  OG1  . THR   A 1 99  ? 15.31300 -18.77700 8.67700  1.000 42.56251 ?  251 THR   A OG1  1 
ATOM   616  C  CG2  . THR   A 1 99  ? 15.79500 -19.89300 6.59300  1.000 49.98133 ?  251 THR   A CG2  1 
ATOM   617  N  N    . SER   A 1 100 ? 12.93100 -16.51200 7.10800  1.000 34.50344 ?  252 SER   A N    1 
ATOM   618  C  CA   . SER   A 1 100 ? 11.98300 -15.67200 7.83200  1.000 33.28852 ?  252 SER   A CA   1 
ATOM   619  C  C    . SER   A 1 100 ? 12.09600 -15.90300 9.33300  1.000 29.71952 ?  252 SER   A C    1 
ATOM   620  O  O    . SER   A 1 100 ? 12.10000 -14.95200 10.12300 1.000 31.75131 ?  252 SER   A O    1 
ATOM   621  C  CB   . SER   A 1 100 ? 10.55700 -15.96400 7.35100  1.000 37.53292 ?  252 SER   A CB   1 
ATOM   622  O  OG   . SER   A 1 100 ? 10.26600 -15.29200 6.13800  1.000 48.48909 ?  252 SER   A OG   1 
ATOM   623  N  N    . ASP   A 1 101 ? 12.20700 -17.17300 9.73800  1.000 33.68133 ?  253 ASP   A N    1 
ATOM   624  C  CA   . ASP   A 1 101 ? 12.35200 -17.50300 11.15400 1.000 36.94120 ?  253 ASP   A CA   1 
ATOM   625  C  C    . ASP   A 1 101 ? 13.55500 -16.80200 11.76900 1.000 31.91999 ?  253 ASP   A C    1 
ATOM   626  O  O    . ASP   A 1 101 ? 13.45600 -16.22200 12.85800 1.000 31.18583 ?  253 ASP   A O    1 
ATOM   627  C  CB   . ASP   A 1 101 ? 12.47800 -19.01800 11.33200 1.000 35.45212 ?  253 ASP   A CB   1 
ATOM   628  C  CG   . ASP   A 1 101 ? 11.13900 -19.72500 11.28800 1.000 43.38937 ?  253 ASP   A CG   1 
ATOM   629  O  OD1  . ASP   A 1 101 ? 11.11600 -20.97500 11.33500 1.000 49.32105 ?  253 ASP   A OD1  1 
ATOM   630  O  OD2  . ASP   A 1 101 ? 10.10600 -19.03000 11.19900 1.000 41.03073 ?  253 ASP   A OD2  1 
ATOM   631  N  N    . ASP   A 1 102 ? 14.70200 -16.84000 11.08600 1.000 33.08529 ?  254 ASP   A N    1 
ATOM   632  C  CA   . ASP   A 1 102 ? 15.91800 -16.27500 11.66000 1.000 32.80237 ?  254 ASP   A CA   1 
ATOM   633  C  C    . ASP   A 1 102 ? 15.87500 -14.75200 11.67500 1.000 32.55646 ?  254 ASP   A C    1 
ATOM   634  O  O    . ASP   A 1 102 ? 16.36200 -14.12400 12.62200 1.000 29.53606 ?  254 ASP   A O    1 
ATOM   635  C  CB   . ASP   A 1 102 ? 17.14200 -16.77500 10.89700 1.000 31.48942 ?  254 ASP   A CB   1 
ATOM   636  C  CG   . ASP   A 1 102 ? 17.66100 -18.09400 11.43500 1.000 38.19423 ?  254 ASP   A CG   1 
ATOM   637  O  OD1  . ASP   A 1 102 ? 18.47500 -18.74200 10.74400 1.000 39.58081 ?  254 ASP   A OD1  1 
ATOM   638  O  OD2  . ASP   A 1 102 ? 17.25000 -18.48200 12.54800 1.000 39.27910 ?  254 ASP   A OD2  1 
ATOM   639  N  N    . GLN   A 1 103 ? 15.30900 -14.13700 10.63300 1.000 28.04060 ?  255 GLN   A N    1 
ATOM   640  C  CA   . GLN   A 1 103 ? 15.11700 -12.69000 10.65700 1.000 26.81584 ?  255 GLN   A CA   1 
ATOM   641  C  C    . GLN   A 1 103 ? 14.24500 -12.28000 11.83700 1.000 27.44679 ?  255 GLN   A C    1 
ATOM   642  O  O    . GLN   A 1 103 ? 14.51300 -11.27100 12.50000 1.000 23.65382 ?  255 GLN   A O    1 
ATOM   643  C  CB   . GLN   A 1 103 ? 14.48900 -12.21700 9.34600  1.000 27.73227 ?  255 GLN   A CB   1 
ATOM   644  C  CG   . GLN   A 1 103 ? 15.34000 -12.46700 8.11400  1.000 34.79109 ?  255 GLN   A CG   1 
ATOM   645  C  CD   . GLN   A 1 103 ? 14.64000 -12.04500 6.83900  1.000 41.68831 ?  255 GLN   A CD   1 
ATOM   646  O  OE1  . GLN   A 1 103 ? 13.76600 -11.17800 6.85900  1.000 41.42648 ?  255 GLN   A OE1  1 
ATOM   647  N  NE2  . GLN   A 1 103 ? 15.01800 -12.66000 5.72100  1.000 41.12615 ?  255 GLN   A NE2  1 
ATOM   648  N  N    . ILE   A 1 104 ? 13.20100 -13.06100 12.11700 1.000 29.92084 ?  256 ILE   A N    1 
ATOM   649  C  CA   . ILE   A 1 104 ? 12.28200 -12.73500 13.20300 1.000 28.57949 ?  256 ILE   A CA   1 
ATOM   650  C  C    . ILE   A 1 104 ? 12.97900 -12.85700 14.55200 1.000 24.47311 ?  256 ILE   A C    1 
ATOM   651  O  O    . ILE   A 1 104 ? 12.87900 -11.96300 15.40000 1.000 26.95315 ?  256 ILE   A O    1 
ATOM   652  C  CB   . ILE   A 1 104 ? 11.03400 -13.63400 13.12700 1.000 28.68135 ?  256 ILE   A CB   1 
ATOM   653  C  CG1  . ILE   A 1 104 ? 10.11500 -13.17600 11.99200 1.000 32.06121 ?  256 ILE   A CG1  1 
ATOM   654  C  CG2  . ILE   A 1 104 ? 10.29400 -13.66500 14.46100 1.000 32.48703 ?  256 ILE   A CG2  1 
ATOM   655  C  CD1  . ILE   A 1 104 ? 8.94900  -14.10600 11.75000 1.000 30.91554 ?  256 ILE   A CD1  1 
ATOM   656  N  N    A VAL   A 1 105 ? 13.70900 -13.95200 14.77500 0.640 27.72709 ?  257 VAL   A N    1 
ATOM   657  N  N    B VAL   A 1 105 ? 13.67900 -13.97300 14.76400 0.360 28.19857 ?  257 VAL   A N    1 
ATOM   658  C  CA   A VAL   A 1 105 ? 14.34300 -14.13700 16.07900 0.640 30.41424 ?  257 VAL   A CA   1 
ATOM   659  C  CA   B VAL   A 1 105 ? 14.39300 -14.21300 16.01400 0.360 30.25300 ?  257 VAL   A CA   1 
ATOM   660  C  C    A VAL   A 1 105 ? 15.43800 -13.09900 16.29600 0.640 29.12930 ?  257 VAL   A C    1 
ATOM   661  C  C    B VAL   A 1 105 ? 15.41200 -13.11000 16.26800 0.360 28.99801 ?  257 VAL   A C    1 
ATOM   662  O  O    A VAL   A 1 105 ? 15.64400 -12.62200 17.41800 0.640 28.95499 ?  257 VAL   A O    1 
ATOM   663  O  O    B VAL   A 1 105 ? 15.53800 -12.60400 17.39000 0.360 27.51266 ?  257 VAL   A O    1 
ATOM   664  C  CB   A VAL   A 1 105 ? 14.87800 -15.57400 16.23700 0.640 32.07285 ?  257 VAL   A CB   1 
ATOM   665  C  CB   B VAL   A 1 105 ? 15.06200 -15.60000 15.96800 0.360 33.08654 ?  257 VAL   A CB   1 
ATOM   666  C  CG1  A VAL   A 1 105 ? 13.74100 -16.57700 16.12900 0.640 34.76231 ?  257 VAL   A CG1  1 
ATOM   667  C  CG1  B VAL   A 1 105 ? 16.24100 -15.66200 16.91900 0.360 33.88703 ?  257 VAL   A CG1  1 
ATOM   668  C  CG2  A VAL   A 1 105 ? 15.96700 -15.87500 15.22200 0.640 34.58986 ?  257 VAL   A CG2  1 
ATOM   669  C  CG2  B VAL   A 1 105 ? 14.05000 -16.69300 16.27400 0.360 34.69515 ?  257 VAL   A CG2  1 
ATOM   670  N  N    . LEU   A 1 106 ? 16.15200 -12.72400 15.22800 1.000 28.37192 ?  258 LEU   A N    1 
ATOM   671  C  CA   . LEU   A 1 106 ? 17.18100 -11.70200 15.37700 1.000 28.32514 ?  258 LEU   A CA   1 
ATOM   672  C  C    . LEU   A 1 106 ? 16.57100 -10.35300 15.72900 1.000 25.98799 ?  258 LEU   A C    1 
ATOM   673  O  O    . LEU   A 1 106 ? 17.13100 -9.61000  16.54000 1.000 22.05235 ?  258 LEU   A O    1 
ATOM   674  C  CB   . LEU   A 1 106 ? 18.01500 -11.59400 14.10000 1.000 26.96965 ?  258 LEU   A CB   1 
ATOM   675  C  CG   . LEU   A 1 106 ? 18.96200 -12.75500 13.78800 1.000 28.20822 ?  258 LEU   A CG   1 
ATOM   676  C  CD1  . LEU   A 1 106 ? 19.69900 -12.49700 12.48900 1.000 26.82197 ?  258 LEU   A CD1  1 
ATOM   677  C  CD2  . LEU   A 1 106 ? 19.94200 -12.98400 14.92600 1.000 25.41519 ?  258 LEU   A CD2  1 
ATOM   678  N  N    . LEU   A 1 107 ? 15.41900 -10.02100 15.14300 1.000 24.79591 ?  259 LEU   A N    1 
ATOM   679  C  CA   . LEU   A 1 107 ? 14.80700 -8.72900  15.43400 1.000 24.44521 ?  259 LEU   A CA   1 
ATOM   680  C  C    . LEU   A 1 107 ? 14.13000 -8.72500  16.79800 1.000 22.43344 ?  259 LEU   A C    1 
ATOM   681  O  O    . LEU   A 1 107 ? 14.19600 -7.72600  17.52100 1.000 22.51743 ?  259 LEU   A O    1 
ATOM   682  C  CB   . LEU   A 1 107 ? 13.81200 -8.35500  14.33200 1.000 27.96868 ?  259 LEU   A CB   1 
ATOM   683  C  CG   . LEU   A 1 107 ? 14.47700 -7.76900  13.08800 1.000 31.38359 ?  259 LEU   A CG   1 
ATOM   684  C  CD1  . LEU   A 1 107 ? 13.54900 -7.81900  11.89200 1.000 34.97943 ?  259 LEU   A CD1  1 
ATOM   685  C  CD2  . LEU   A 1 107 ? 14.92600 -6.34700  13.36400 1.000 29.94176 ?  259 LEU   A CD2  1 
ATOM   686  N  N    . LYS   A 1 108 ? 13.47400 -9.82900  17.16800 1.000 21.60210 ?  260 LYS   A N    1 
ATOM   687  C  CA   . LYS   A 1 108 ? 12.88300 -9.92300  18.50000 1.000 25.35041 ?  260 LYS   A CA   1 
ATOM   688  C  C    . LYS   A 1 108 ? 13.94400 -9.78100  19.58200 1.000 27.13706 ?  260 LYS   A C    1 
ATOM   689  O  O    . LYS   A 1 108 ? 13.73700 -9.08100  20.58100 1.000 26.14200 ?  260 LYS   A O    1 
ATOM   690  C  CB   . LYS   A 1 108 ? 12.14700 -11.25200 18.66400 1.000 29.49932 ?  260 LYS   A CB   1 
ATOM   691  C  CG   . LYS   A 1 108 ? 10.83800 -11.34200 17.91800 1.000 38.42687 ?  260 LYS   A CG   1 
ATOM   692  C  CD   . LYS   A 1 108 ? 10.12300 -12.63100 18.27100 1.000 45.18405 ?  260 LYS   A CD   1 
ATOM   693  C  CE   . LYS   A 1 108 ? 9.58500  -12.58700 19.69400 1.000 49.93732 ?  260 LYS   A CE   1 
ATOM   694  N  NZ   . LYS   A 1 108 ? 8.97700  -13.88300 20.11400 1.000 54.70222 ?  260 LYS   A NZ   1 
ATOM   695  N  N    A SER   A 1 109 ? 15.09100 -10.43500 19.39800 0.550 24.29264 ?  261 SER   A N    1 
ATOM   696  N  N    B SER   A 1 109 ? 15.08700 -10.44300 19.40400 0.450 25.04031 ?  261 SER   A N    1 
ATOM   697  C  CA   A SER   A 1 109 ? 16.13500 -10.39200 20.41300 0.550 31.16883 ?  261 SER   A CA   1 
ATOM   698  C  CA   B SER   A 1 109 ? 16.13700 -10.39100 20.41400 0.450 30.81169 ?  261 SER   A CA   1 
ATOM   699  C  C    A SER   A 1 109 ? 16.88100 -9.06100  20.41500 0.550 27.96539 ?  261 SER   A C    1 
ATOM   700  C  C    B SER   A 1 109 ? 16.88400 -9.06400  20.41300 0.450 27.93468 ?  261 SER   A C    1 
ATOM   701  O  O    A SER   A 1 109 ? 17.31300 -8.59900  21.47600 0.550 25.91527 ?  261 SER   A O    1 
ATOM   702  O  O    B SER   A 1 109 ? 17.32100 -8.60800  21.47400 0.450 26.17460 ?  261 SER   A O    1 
ATOM   703  C  CB   A SER   A 1 109 ? 17.11000 -11.54900 20.19800 0.550 32.05401 ?  261 SER   A CB   1 
ATOM   704  C  CB   B SER   A 1 109 ? 17.12900 -11.53900 20.20800 0.450 32.07808 ?  261 SER   A CB   1 
ATOM   705  O  OG   A SER   A 1 109 ? 18.15800 -11.52100 21.15000 0.550 32.71418 ?  261 SER   A OG   1 
ATOM   706  O  OG   B SER   A 1 109 ? 17.58000 -11.59000 18.86500 0.450 33.09304 ?  261 SER   A OG   1 
ATOM   707  N  N    . SER   A 1 110 ? 17.03900 -8.43200  19.25000 1.000 24.90254 ?  262 SER   A N    1 
ATOM   708  C  CA   . SER   A 1 110 ? 17.88800 -7.25400  19.12300 1.000 22.09496 ?  262 SER   A CA   1 
ATOM   709  C  C    . SER   A 1 110 ? 17.15000 -5.92300  19.22100 1.000 22.83565 ?  262 SER   A C    1 
ATOM   710  O  O    . SER   A 1 110 ? 17.80600 -4.89900  19.44600 1.000 20.51464 ?  262 SER   A O    1 
ATOM   711  C  CB   . SER   A 1 110 ? 18.65700 -7.29400  17.79700 1.000 25.32084 ?  262 SER   A CB   1 
ATOM   712  O  OG   . SER   A 1 110 ? 17.80000 -7.00200  16.70700 1.000 28.04712 ?  262 SER   A OG   1 
ATOM   713  N  N    . ALA   A 1 111 ? 15.82100 -5.90600  19.07700 1.000 21.57869 ?  263 ALA   A N    1 
ATOM   714  C  CA   . ALA   A 1 111 ? 15.10100 -4.64300  18.91400 1.000 20.17606 ?  263 ALA   A CA   1 
ATOM   715  C  C    . ALA   A 1 111 ? 15.36300 -3.68800  20.07200 1.000 18.98016 ?  263 ALA   A C    1 
ATOM   716  O  O    . ALA   A 1 111 ? 15.64700 -2.50400  19.86000 1.000 19.79461 ?  263 ALA   A O    1 
ATOM   717  C  CB   . ALA   A 1 111 ? 13.60000 -4.90600  18.76800 1.000 22.79119 ?  263 ALA   A CB   1 
ATOM   718  N  N    . ILE   A 1 112 ? 15.27200 -4.18400  21.30600 1.000 18.57774 ?  264 ILE   A N    1 
ATOM   719  C  CA   . ILE   A 1 112 ? 15.49100 -3.32600  22.46700 1.000 20.91702 ?  264 ILE   A CA   1 
ATOM   720  C  C    . ILE   A 1 112 ? 16.90300 -2.74800  22.44900 1.000 23.45855 ?  264 ILE   A C    1 
ATOM   721  O  O    . ILE   A 1 112 ? 17.12600 -1.58900  22.82800 1.000 18.75344 ?  264 ILE   A O    1 
ATOM   722  C  CB   . ILE   A 1 112 ? 15.20700 -4.11300  23.76200 1.000 27.35025 ?  264 ILE   A CB   1 
ATOM   723  C  CG1  . ILE   A 1 112 ? 15.43900 -3.23300  24.98500 1.000 29.15160 ?  264 ILE   A CG1  1 
ATOM   724  C  CG2  . ILE   A 1 112 ? 16.06500 -5.37500  23.83800 1.000 24.94183 ?  264 ILE   A CG2  1 
ATOM   725  C  CD1  . ILE   A 1 112 ? 14.57300 -2.03500  25.01300 1.000 26.41778 ?  264 ILE   A CD1  1 
ATOM   726  N  N    . GLU   A 1 113 ? 17.87500 -3.53900  21.99300 1.000 18.61399 ?  265 GLU   A N    1 
ATOM   727  C  CA   . GLU   A 1 113 ? 19.26000 -3.08300  21.99100 1.000 19.84829 ?  265 GLU   A CA   1 
ATOM   728  C  C    . GLU   A 1 113 ? 19.49200 -2.02800  20.91700 1.000 19.90836 ?  265 GLU   A C    1 
ATOM   729  O  O    . GLU   A 1 113 ? 20.19400 -1.03800  21.15400 1.000 19.78474 ?  265 GLU   A O    1 
ATOM   730  C  CB   . GLU   A 1 113 ? 20.19600 -4.27400  21.78500 1.000 22.37378 ?  265 GLU   A CB   1 
ATOM   731  C  CG   . GLU   A 1 113 ? 20.11900 -5.32200  22.87900 1.000 20.47607 ?  265 GLU   A CG   1 
ATOM   732  C  CD   . GLU   A 1 113 ? 21.02700 -6.50400  22.60600 1.000 25.91644 ?  265 GLU   A CD   1 
ATOM   733  O  OE1  . GLU   A 1 113 ? 22.01700 -6.33800  21.86200 1.000 24.91503 ?  265 GLU   A OE1  1 
ATOM   734  O  OE2  . GLU   A 1 113 ? 20.74400 -7.60100  23.12900 1.000 27.93104 ?  265 GLU   A OE2  1 
ATOM   735  N  N    . VAL   A 1 114 ? 18.91200 -2.22200  19.72900 1.000 22.18887 ?  266 VAL   A N    1 
ATOM   736  C  CA   . VAL   A 1 114 ? 19.07000 -1.23700  18.66400 1.000 18.19767 ?  266 VAL   A CA   1 
ATOM   737  C  C    . VAL   A 1 114 ? 18.36200 0.05900   19.03200 1.000 20.35140 ?  266 VAL   A C    1 
ATOM   738  O  O    . VAL   A 1 114 ? 18.82800 1.15200   18.69300 1.000 20.12345 ?  266 VAL   A O    1 
ATOM   739  C  CB   . VAL   A 1 114 ? 18.55800 -1.80300  17.32800 1.000 21.04176 ?  266 VAL   A CB   1 
ATOM   740  C  CG1  . VAL   A 1 114 ? 18.82500 -0.82000  16.19100 1.000 20.51037 ?  266 VAL   A CG1  1 
ATOM   741  C  CG2  . VAL   A 1 114 ? 19.20900 -3.13600  17.04400 1.000 22.65347 ?  266 VAL   A CG2  1 
ATOM   742  N  N    . ILE   A 1 115 ? 17.23200 -0.04000  19.73500 1.000 19.36324 ?  267 ILE   A N    1 
ATOM   743  C  CA   . ILE   A 1 115 ? 16.55100 1.15900   20.21200 1.000 19.06761 ?  267 ILE   A CA   1 
ATOM   744  C  C    . ILE   A 1 115 ? 17.45500 1.94100   21.15800 1.000 18.00788 ?  267 ILE   A C    1 
ATOM   745  O  O    . ILE   A 1 115 ? 17.56700 3.16900   21.06000 1.000 21.31384 ?  267 ILE   A O    1 
ATOM   746  C  CB   . ILE   A 1 115 ? 15.21100 0.78200   20.87400 1.000 20.62719 ?  267 ILE   A CB   1 
ATOM   747  C  CG1  . ILE   A 1 115 ? 14.17000 0.44500   19.80300 1.000 20.33531 ?  267 ILE   A CG1  1 
ATOM   748  C  CG2  . ILE   A 1 115 ? 14.71200 1.90100   21.77600 1.000 18.85799 ?  267 ILE   A CG2  1 
ATOM   749  C  CD1  . ILE   A 1 115 ? 12.98400 -0.34500  20.32300 1.000 22.86631 ?  267 ILE   A CD1  1 
ATOM   750  N  N    . MET   A 1 116 ? 18.12500 1.24000   22.07900 1.000 19.91904 ?  268 MET   A N    1 
ATOM   751  C  CA   . MET   A 1 116 ? 19.04900 1.91000   22.99100 1.000 22.28238 ?  268 MET   A CA   1 
ATOM   752  C  C    . MET   A 1 116 ? 20.21500 2.53300   22.23200 1.000 17.62221 ?  268 MET   A C    1 
ATOM   753  O  O    . MET   A 1 116 ? 20.64400 3.65100   22.54800 1.000 22.22222 ?  268 MET   A O    1 
ATOM   754  C  CB   . MET   A 1 116 ? 19.55200 0.92400   24.04800 1.000 23.34361 ?  268 MET   A CB   1 
ATOM   755  C  CG   . MET   A 1 116 ? 18.47800 0.47700   25.03200 1.000 24.91955 ?  268 MET   A CG   1 
ATOM   756  S  SD   . MET   A 1 116 ? 18.99800 -0.86700  26.11500 1.000 26.49921 ?  268 MET   A SD   1 
ATOM   757  C  CE   . MET   A 1 116 ? 17.58200 -0.99000  27.20500 1.000 24.54563 ?  268 MET   A CE   1 
ATOM   758  N  N    . LEU   A 1 117 ? 20.72600 1.83600   21.21200 1.000 18.33032 ?  269 LEU   A N    1 
ATOM   759  C  CA   . LEU   A 1 117 ? 21.82000 2.38800   20.41500 1.000 19.84902 ?  269 LEU   A CA   1 
ATOM   760  C  C    . LEU   A 1 117 ? 21.37100 3.60500   19.61700 1.000 24.38858 ?  269 LEU   A C    1 
ATOM   761  O  O    . LEU   A 1 117 ? 22.00500 4.66500   19.67400 1.000 20.83782 ?  269 LEU   A O    1 
ATOM   762  C  CB   . LEU   A 1 117 ? 22.38200 1.32800   19.46700 1.000 22.36293 ?  269 LEU   A CB   1 
ATOM   763  C  CG   . LEU   A 1 117 ? 23.33900 0.25400   19.98000 1.000 30.82274 ?  269 LEU   A CG   1 
ATOM   764  C  CD1  . LEU   A 1 117 ? 23.50300 -0.83000  18.92800 1.000 30.96867 ?  269 LEU   A CD1  1 
ATOM   765  C  CD2  . LEU   A 1 117 ? 24.67900 0.85500   20.36500 1.000 28.65322 ?  269 LEU   A CD2  1 
ATOM   766  N  N    . ARG   A 1 118 ? 20.28100 3.47000   18.85400 1.000 21.55867 ?  270 ARG   A N    1 
ATOM   767  C  CA   . ARG   A 1 118 ? 19.86500 4.55900   17.97700 1.000 18.55819 ?  270 ARG   A CA   1 
ATOM   768  C  C    . ARG   A 1 118 ? 19.36600 5.76300   18.76600 1.000 19.41798 ?  270 ARG   A C    1 
ATOM   769  O  O    . ARG   A 1 118 ? 19.47200 6.89900   18.28900 1.000 23.15872 ?  270 ARG   A O    1 
ATOM   770  C  CB   . ARG   A 1 118 ? 18.79100 4.07400   16.99600 1.000 21.90335 ?  270 ARG   A CB   1 
ATOM   771  C  CG   . ARG   A 1 118 ? 17.43800 3.79300   17.62100 1.000 21.21932 ?  270 ARG   A CG   1 
ATOM   772  C  CD   . ARG   A 1 118 ? 16.57000 2.92300   16.72000 1.000 28.99669 ?  270 ARG   A CD   1 
ATOM   773  N  NE   . ARG   A 1 118 ? 16.04300 3.66200   15.57500 1.000 29.70217 ?  270 ARG   A NE   1 
ATOM   774  C  CZ   . ARG   A 1 118 ? 16.53400 3.58300   14.34400 1.000 26.43631 ?  270 ARG   A CZ   1 
ATOM   775  N  NH1  . ARG   A 1 118 ? 15.99200 4.29200   13.36200 1.000 24.42449 ?  270 ARG   A NH1  1 
ATOM   776  N  NH2  . ARG   A 1 118 ? 17.57100 2.79600   14.08700 1.000 37.66929 ?  270 ARG   A NH2  1 
ATOM   777  N  N    . SER   A 1 119 ? 18.84100 5.54500   19.97500 1.000 19.08233 ?  271 SER   A N    1 
ATOM   778  C  CA   . SER   A 1 119 ? 18.42500 6.66700   20.80900 1.000 20.23358 ?  271 SER   A CA   1 
ATOM   779  C  C    . SER   A 1 119 ? 19.59700 7.54100   21.22700 1.000 24.47258 ?  271 SER   A C    1 
ATOM   780  O  O    . SER   A 1 119 ? 19.38400 8.69500   21.61200 1.000 24.23686 ?  271 SER   A O    1 
ATOM   781  C  CB   . SER   A 1 119 ? 17.69900 6.15800   22.05500 1.000 19.94790 ?  271 SER   A CB   1 
ATOM   782  O  OG   . SER   A 1 119 ? 18.61800 5.65200   23.00600 1.000 23.33639 ?  271 SER   A OG   1 
ATOM   783  N  N    . ASN   A 1 120 ? 20.82400 7.01900   21.15400 1.000 22.00139 ?  272 ASN   A N    1 
ATOM   784  C  CA   . ASN   A 1 120 ? 21.99600 7.81100   21.50600 1.000 21.93055 ?  272 ASN   A CA   1 
ATOM   785  C  C    . ASN   A 1 120 ? 22.14700 9.03700   20.62100 1.000 26.88081 ?  272 ASN   A C    1 
ATOM   786  O  O    . ASN   A 1 120 ? 22.80000 10.00200  21.02900 1.000 25.59963 ?  272 ASN   A O    1 
ATOM   787  C  CB   . ASN   A 1 120 ? 23.25800 6.94900   21.41800 1.000 18.69187 ?  272 ASN   A CB   1 
ATOM   788  C  CG   . ASN   A 1 120 ? 24.46100 7.60500   22.07200 1.000 24.44344 ?  272 ASN   A CG   1 
ATOM   789  O  OD1  . ASN   A 1 120 ? 25.43300 7.95800   21.40300 1.000 27.86065 ?  272 ASN   A OD1  1 
ATOM   790  N  ND2  . ASN   A 1 120 ? 24.40300 7.76100   23.38900 1.000 24.50169 ?  272 ASN   A ND2  1 
ATOM   791  N  N    . GLN   A 1 121 ? 21.55900 9.02100   19.42300 1.000 24.28895 ?  273 GLN   A N    1 
ATOM   792  C  CA   . GLN   A 1 121 ? 21.65400 10.17500  18.53600 1.000 24.83823 ?  273 GLN   A CA   1 
ATOM   793  C  C    . GLN   A 1 121 ? 20.94600 11.39200  19.11800 1.000 28.84617 ?  273 GLN   A C    1 
ATOM   794  O  O    . GLN   A 1 121 ? 21.38400 12.52600  18.89400 1.000 29.36961 ?  273 GLN   A O    1 
ATOM   795  C  CB   . GLN   A 1 121 ? 21.07700 9.82200   17.16500 1.000 31.37451 ?  273 GLN   A CB   1 
ATOM   796  C  CG   . GLN   A 1 121 ? 21.34800 10.85100  16.08400 1.000 32.36414 ?  273 GLN   A CG   1 
ATOM   797  C  CD   . GLN   A 1 121 ? 21.07100 10.31400  14.69100 1.000 34.36767 ?  273 GLN   A CD   1 
ATOM   798  O  OE1  . GLN   A 1 121 ? 21.19500 9.11700   14.43900 1.000 29.13312 ?  273 GLN   A OE1  1 
ATOM   799  N  NE2  . GLN   A 1 121 ? 20.70500 11.20000  13.77800 1.000 36.38363 ?  273 GLN   A NE2  1 
ATOM   800  N  N    . SER   A 1 122 ? 19.86300 11.18100  19.86400 1.000 24.13992 ?  274 SER   A N    1 
ATOM   801  C  CA   . SER   A 1 122 ? 19.14600 12.26900  20.51600 1.000 23.80024 ?  274 SER   A CA   1 
ATOM   802  C  C    . SER   A 1 122 ? 19.64500 12.54400  21.92800 1.000 29.52691 ?  274 SER   A C    1 
ATOM   803  O  O    . SER   A 1 122 ? 19.27300 13.56800  22.51200 1.000 31.32926 ?  274 SER   A O    1 
ATOM   804  C  CB   . SER   A 1 122 ? 17.64400 11.96600  20.56600 1.000 24.23349 ?  274 SER   A CB   1 
ATOM   805  O  OG   . SER   A 1 122 ? 17.36600 10.90300  21.46400 1.000 31.12975 ?  274 SER   A OG   1 
ATOM   806  N  N    . PHE   A 1 123 ? 20.46900 11.66000  22.48300 1.000 26.61433 ?  275 PHE   A N    1 
ATOM   807  C  CA   . PHE   A 1 123 ? 20.95700 11.83500  23.84300 1.000 25.88381 ?  275 PHE   A CA   1 
ATOM   808  C  C    . PHE   A 1 123 ? 21.93800 12.99900  23.91200 1.000 30.25859 ?  275 PHE   A C    1 
ATOM   809  O  O    . PHE   A 1 123 ? 22.78500 13.17200  23.03100 1.000 31.35219 ?  275 PHE   A O    1 
ATOM   810  C  CB   . PHE   A 1 123 ? 21.63100 10.55000  24.32500 1.000 24.68470 ?  275 PHE   A CB   1 
ATOM   811  C  CG   . PHE   A 1 123 ? 21.95100 10.54500  25.79000 1.000 23.96036 ?  275 PHE   A CG   1 
ATOM   812  C  CD1  . PHE   A 1 123 ? 20.95700 10.31500  26.72600 1.000 27.70964 ?  275 PHE   A CD1  1 
ATOM   813  C  CD2  . PHE   A 1 123 ? 23.24700 10.77200  26.22900 1.000 22.36638 ?  275 PHE   A CD2  1 
ATOM   814  C  CE1  . PHE   A 1 123 ? 21.24500 10.30500  28.07800 1.000 29.01924 ?  275 PHE   A CE1  1 
ATOM   815  C  CE2  . PHE   A 1 123 ? 23.54600 10.76600  27.58100 1.000 29.78618 ?  275 PHE   A CE2  1 
ATOM   816  C  CZ   . PHE   A 1 123 ? 22.54500 10.53100  28.50700 1.000 29.25558 ?  275 PHE   A CZ   1 
ATOM   817  N  N    . THR   A 1 124 ? 21.81800 13.80600  24.96400 1.000 28.94569 ?  276 THR   A N    1 
ATOM   818  C  CA   . THR   A 1 124 ? 22.74800 14.89900  25.21100 1.000 34.17192 ?  276 THR   A CA   1 
ATOM   819  C  C    . THR   A 1 124 ? 23.31500 14.75500  26.61300 1.000 33.58566 ?  276 THR   A C    1 
ATOM   820  O  O    . THR   A 1 124 ? 22.56700 14.53000  27.57000 1.000 30.94148 ?  276 THR   A O    1 
ATOM   821  C  CB   . THR   A 1 124 ? 22.08200 16.27400  25.04300 1.000 37.88492 ?  276 THR   A CB   1 
ATOM   822  O  OG1  . THR   A 1 124 ? 22.97700 17.29800  25.49700 1.000 44.05804 ?  276 THR   A OG1  1 
ATOM   823  C  CG2  . THR   A 1 124 ? 20.78300 16.35800  25.83600 1.000 34.81073 ?  276 THR   A CG2  1 
ATOM   824  N  N    . MET   A 1 125 ? 24.63700 14.86600  26.72900 1.000 32.38377 ?  277 MET   A N    1 
ATOM   825  C  CA   . MET   A 1 125 ? 25.28500 14.83900  28.03200 1.000 33.37095 ?  277 MET   A CA   1 
ATOM   826  C  C    . MET   A 1 125 ? 25.16800 16.16600  28.76900 1.000 43.59080 ?  277 MET   A C    1 
ATOM   827  O  O    . MET   A 1 125 ? 25.51600 16.22800  29.95300 1.000 46.53567 ?  277 MET   A O    1 
ATOM   828  C  CB   . MET   A 1 125 ? 26.75800 14.45000  27.87400 1.000 39.64930 ?  277 MET   A CB   1 
ATOM   829  C  CG   . MET   A 1 125 ? 26.96400 12.98600  27.50800 1.000 38.64377 ?  277 MET   A CG   1 
ATOM   830  S  SD   . MET   A 1 125 ? 28.69800 12.49800  27.42200 1.000 45.72402 ?  277 MET   A SD   1 
ATOM   831  C  CE   . MET   A 1 125 ? 29.24500 13.42300  25.98700 1.000 46.36140 ?  277 MET   A CE   1 
ATOM   832  N  N    . ASP   A 1 126 ? 24.67500 17.21600  28.10100 1.000 40.68565 ?  278 ASP   A N    1 
ATOM   833  C  CA   . ASP   A 1 126 ? 24.47800 18.50000  28.76800 1.000 46.43539 ?  278 ASP   A CA   1 
ATOM   834  C  C    . ASP   A 1 126 ? 23.56300 18.36000  29.97800 1.000 45.35671 ?  278 ASP   A C    1 
ATOM   835  O  O    . ASP   A 1 126 ? 23.83800 18.92800  31.04100 1.000 48.12038 ?  278 ASP   A O    1 
ATOM   836  C  CB   . ASP   A 1 126 ? 23.91600 19.52800  27.78300 1.000 55.07035 ?  278 ASP   A CB   1 
ATOM   837  C  CG   . ASP   A 1 126 ? 24.91600 19.91800  26.71200 1.000 69.13786 ?  278 ASP   A CG   1 
ATOM   838  O  OD1  . ASP   A 1 126 ? 24.51600 20.57400  25.72600 1.000 73.64620 ?  278 ASP   A OD1  1 
ATOM   839  O  OD2  . ASP   A 1 126 ? 26.10400 19.56700  26.86000 1.000 72.58411 ?  278 ASP   A OD2  1 
ATOM   840  N  N    . ASP   A 1 127 ? 22.47000 17.59900  29.83900 1.000 45.48958 ?  279 ASP   A N    1 
ATOM   841  C  CA   . ASP   A 1 127 ? 21.60600 17.33200  30.98300 1.000 44.88802 ?  279 ASP   A CA   1 
ATOM   842  C  C    . ASP   A 1 127 ? 21.13100 15.88200  31.03300 1.000 40.61258 ?  279 ASP   A C    1 
ATOM   843  O  O    . ASP   A 1 127 ? 20.10700 15.60100  31.66700 1.000 42.30610 ?  279 ASP   A O    1 
ATOM   844  C  CB   . ASP   A 1 127 ? 20.39600 18.27800  31.00100 1.000 53.20249 ?  279 ASP   A CB   1 
ATOM   845  C  CG   . ASP   A 1 127 ? 19.54600 18.18300  29.74600 1.000 58.69953 ?  279 ASP   A CG   1 
ATOM   846  O  OD1  . ASP   A 1 127 ? 18.52200 18.89300  29.68900 1.000 61.46673 ?  279 ASP   A OD1  1 
ATOM   847  O  OD2  . ASP   A 1 127 ? 19.89100 17.41600  28.82300 1.000 56.67806 ?  279 ASP   A OD2  1 
ATOM   848  N  N    . MET   A 1 128 ? 21.84500 14.96300  30.37900 1.000 36.00275 ?  280 MET   A N    1 
ATOM   849  C  CA   . MET   A 1 128 ? 21.58800 13.52400  30.48800 1.000 34.91146 ?  280 MET   A CA   1 
ATOM   850  C  C    . MET   A 1 128 ? 20.15200 13.17800  30.09700 1.000 34.40561 ?  280 MET   A C    1 
ATOM   851  O  O    . MET   A 1 128 ? 19.44500 12.45700  30.80500 1.000 33.92923 ?  280 MET   A O    1 
ATOM   852  C  CB   . MET   A 1 128 ? 21.90900 13.02300  31.89600 1.000 38.67797 ?  280 MET   A CB   1 
ATOM   853  C  CG   . MET   A 1 128 ? 23.31800 13.34500  32.34400 1.000 41.78121 ?  280 MET   A CG   1 
ATOM   854  S  SD   . MET   A 1 128 ? 24.54000 12.55400  31.28700 1.000 40.35094 ?  280 MET   A SD   1 
ATOM   855  C  CE   . MET   A 1 128 ? 26.05500 13.16500  32.01700 1.000 40.55566 ?  280 MET   A CE   1 
ATOM   856  N  N    . SER   A 1 129 ? 19.72500 13.69500  28.94900 1.000 28.48902 ?  281 SER   A N    1 
ATOM   857  C  CA   . SER   A 1 129 ? 18.36500 13.49900  28.47500 1.000 29.48802 ?  281 SER   A CA   1 
ATOM   858  C  C    . SER   A 1 129 ? 18.37300 13.14100  26.99500 1.000 30.45671 ?  281 SER   A C    1 
ATOM   859  O  O    . SER   A 1 129 ? 19.33700 13.40500  26.27100 1.000 30.69634 ?  281 SER   A O    1 
ATOM   860  C  CB   . SER   A 1 129 ? 17.51200 14.75100  28.69800 1.000 32.79875 ?  281 SER   A CB   1 
ATOM   861  O  OG   . SER   A 1 129 ? 17.65900 15.64100  27.60700 1.000 40.46720 ?  281 SER   A OG   1 
ATOM   862  N  N    . TRP   A 1 130 ? 17.27000 12.53500  26.55600 1.000 29.57027 ?  282 TRP   A N    1 
ATOM   863  C  CA   . TRP   A 1 130 ? 17.02800 12.23600  25.14700 1.000 27.35846 ?  282 TRP   A CA   1 
ATOM   864  C  C    . TRP   A 1 130 ? 16.19900 13.38000  24.56800 1.000 30.76561 ?  282 TRP   A C    1 
ATOM   865  O  O    . TRP   A 1 130 ? 14.98100 13.43600  24.77000 1.000 34.86129 ?  282 TRP   A O    1 
ATOM   866  C  CB   . TRP   A 1 130 ? 16.30600 10.89800  24.98700 1.000 22.18125 ?  282 TRP   A CB   1 
ATOM   867  C  CG   . TRP   A 1 130 ? 17.13000 9.68600   25.35200 1.000 23.72289 ?  282 TRP   A CG   1 
ATOM   868  C  CD1  . TRP   A 1 130 ? 17.89800 8.93100   24.51200 1.000 24.05848 ?  282 TRP   A CD1  1 
ATOM   869  C  CD2  . TRP   A 1 130 ? 17.23300 9.07400   26.64500 1.000 24.35268 ?  282 TRP   A CD2  1 
ATOM   870  N  NE1  . TRP   A 1 130 ? 18.48500 7.89800   25.20500 1.000 24.38895 ?  282 TRP   A NE1  1 
ATOM   871  C  CE2  . TRP   A 1 130 ? 18.09400 7.96500   26.51600 1.000 23.13361 ?  282 TRP   A CE2  1 
ATOM   872  C  CE3  . TRP   A 1 130 ? 16.68800 9.36300   27.90000 1.000 27.09679 ?  282 TRP   A CE3  1 
ATOM   873  C  CZ2  . TRP   A 1 130 ? 18.42200 7.14500   27.59500 1.000 26.60389 ?  282 TRP   A CZ2  1 
ATOM   874  C  CZ3  . TRP   A 1 130 ? 17.01600 8.54600   28.96900 1.000 27.77651 ?  282 TRP   A CZ3  1 
ATOM   875  C  CH2  . TRP   A 1 130 ? 17.87400 7.45100   28.80900 1.000 26.58485 ?  282 TRP   A CH2  1 
ATOM   876  N  N    . ASP   A 1 131 ? 16.85700 14.28600  23.84400 1.000 29.95967 ?  283 ASP   A N    1 
ATOM   877  C  CA   . ASP   A 1 131 ? 16.23400 15.51000  23.34700 1.000 35.97538 ?  283 ASP   A CA   1 
ATOM   878  C  C    . ASP   A 1 131 ? 15.75500 15.27000  21.91900 1.000 31.42898 ?  283 ASP   A C    1 
ATOM   879  O  O    . ASP   A 1 131 ? 16.56800 15.15900  20.99500 1.000 35.99786 ?  283 ASP   A O    1 
ATOM   880  C  CB   . ASP   A 1 131 ? 17.21900 16.67700  23.41000 1.000 36.95900 ?  283 ASP   A CB   1 
ATOM   881  C  CG   . ASP   A 1 131 ? 16.56600 18.01800  23.11300 1.000 44.36809 ?  283 ASP   A CG   1 
ATOM   882  O  OD1  . ASP   A 1 131 ? 17.21900 19.05700  23.34600 1.000 48.59353 ?  283 ASP   A OD1  1 
ATOM   883  O  OD2  . ASP   A 1 131 ? 15.40100 18.04000  22.66300 1.000 41.63646 ?  283 ASP   A OD2  1 
ATOM   884  N  N    . CYS   A 1 132 ? 14.43600 15.21400  21.73700 1.000 34.70116 ?  284 CYS   A N    1 
ATOM   885  C  CA   . CYS   A 1 132 ? 13.82000 14.92700  20.44600 1.000 34.92921 ?  284 CYS   A CA   1 
ATOM   886  C  C    . CYS   A 1 132 ? 13.05400 16.13000  19.89700 1.000 38.24835 ?  284 CYS   A C    1 
ATOM   887  O  O    . CYS   A 1 132 ? 11.95900 15.99000  19.34900 1.000 34.14422 ?  284 CYS   A O    1 
ATOM   888  C  CB   . CYS   A 1 132 ? 12.90000 13.71200  20.54900 1.000 33.65711 ?  284 CYS   A CB   1 
ATOM   889  S  SG   . CYS   A 1 132 ? 13.76700 12.13900  20.75300 1.000 29.20701 ?  284 CYS   A SG   1 
ATOM   890  N  N    . GLY   A 1 133 ? 13.61600 17.32900  20.05200 1.000 42.73098 ?  285 GLY   A N    1 
ATOM   891  C  CA   . GLY   A 1 133 ? 13.16400 18.49400  19.32100 1.000 44.26148 ?  285 GLY   A CA   1 
ATOM   892  C  C    . GLY   A 1 133 ? 12.35100 19.50900  20.09900 1.000 47.64116 ?  285 GLY   A C    1 
ATOM   893  O  O    . GLY   A 1 133 ? 12.19000 20.63800  19.61700 1.000 50.93555 ?  285 GLY   A O    1 
ATOM   894  N  N    . SER   A 1 134 ? 11.82900 19.15400  21.27000 1.000 44.34666 ?  286 SER   A N    1 
ATOM   895  C  CA   . SER   A 1 134 ? 10.97700 20.06800  22.02300 1.000 46.60683 ?  286 SER   A CA   1 
ATOM   896  C  C    . SER   A 1 134 ? 10.85700 19.56000  23.45400 1.000 44.39506 ?  286 SER   A C    1 
ATOM   897  O  O    . SER   A 1 134 ? 11.19000 18.41100  23.75800 1.000 41.31015 ?  286 SER   A O    1 
ATOM   898  C  CB   . SER   A 1 134 ? 9.59600  20.21400  21.37300 1.000 48.81119 ?  286 SER   A CB   1 
ATOM   899  O  OG   . SER   A 1 134 ? 8.96000  18.95800  21.22200 1.000 48.84723 ?  286 SER   A OG   1 
ATOM   900  N  N    . GLN   A 1 135 ? 10.36300 20.44000  24.33200 1.000 41.91482 ?  287 GLN   A N    1 
ATOM   901  C  CA   . GLN   A 1 135 ? 10.26100 20.10600  25.75000 1.000 46.06790 ?  287 GLN   A CA   1 
ATOM   902  C  C    . GLN   A 1 135 ? 9.33100  18.92100  25.97800 1.000 45.92190 ?  287 GLN   A C    1 
ATOM   903  O  O    . GLN   A 1 135 ? 9.59600  18.07300  26.83800 1.000 44.22052 ?  287 GLN   A O    1 
ATOM   904  C  CB   . GLN   A 1 135 ? 9.78400  21.32300  26.54200 1.000 47.81472 ?  287 GLN   A CB   1 
ATOM   905  C  CG   . GLN   A 1 135 ? 10.91000 22.20400  27.05500 1.000 62.68529 ?  287 GLN   A CG   1 
ATOM   906  C  CD   . GLN   A 1 135 ? 11.78500 21.49000  28.06200 1.000 69.84009 ?  287 GLN   A CD   1 
ATOM   907  O  OE1  . GLN   A 1 135 ? 11.30500 20.67600  28.84900 1.000 73.27991 ?  287 GLN   A OE1  1 
ATOM   908  N  NE2  . GLN   A 1 135 ? 13.07900 21.78800  28.04000 1.000 70.58788 ?  287 GLN   A NE2  1 
ATOM   909  N  N    . ASP   A 1 136 ? 8.23300  18.84500  25.22300 1.000 40.67358 ?  288 ASP   A N    1 
ATOM   910  C  CA   . ASP   A 1 136 ? 7.30400  17.73100  25.38300 1.000 40.04494 ?  288 ASP   A CA   1 
ATOM   911  C  C    . ASP   A 1 136 ? 7.96300  16.40500  25.02700 1.000 37.90965 ?  288 ASP   A C    1 
ATOM   912  O  O    . ASP   A 1 136 ? 7.67700  15.37500  25.64800 1.000 36.76450 ?  288 ASP   A O    1 
ATOM   913  C  CB   . ASP   A 1 136 ? 6.05200  17.95500  24.53000 1.000 45.63076 ?  288 ASP   A CB   1 
ATOM   914  C  CG   . ASP   A 1 136 ? 5.08200  18.93100  25.16900 1.000 57.07540 ?  288 ASP   A CG   1 
ATOM   915  O  OD1  . ASP   A 1 136 ? 5.37300  19.40800  26.28500 1.000 63.02083 ?  288 ASP   A OD1  1 
ATOM   916  O  OD2  . ASP   A 1 136 ? 4.02200  19.21000  24.56500 1.000 63.60306 ?  288 ASP   A OD2  1 
ATOM   917  N  N    . TYR   A 1 137 ? 8.85200  16.41400  24.03500 1.000 37.53676 ?  289 TYR   A N    1 
ATOM   918  C  CA   . TYR   A 1 137 ? 9.54700  15.21500  23.57900 1.000 30.29561 ?  289 TYR   A CA   1 
ATOM   919  C  C    . TYR   A 1 137 ? 11.01600 15.23900  23.98700 1.000 28.80646 ?  289 TYR   A C    1 
ATOM   920  O  O    . TYR   A 1 137 ? 11.90100 14.85000  23.22400 1.000 32.27230 ?  289 TYR   A O    1 
ATOM   921  C  CB   . TYR   A 1 137 ? 9.40700  15.04800  22.06900 1.000 32.81097 ?  289 TYR   A CB   1 
ATOM   922  C  CG   . TYR   A 1 137 ? 7.99000  15.22900  21.57800 1.000 29.57235 ?  289 TYR   A CG   1 
ATOM   923  C  CD1  . TYR   A 1 137 ? 7.72000  15.94900  20.42200 1.000 36.23022 ?  289 TYR   A CD1  1 
ATOM   924  C  CD2  . TYR   A 1 137 ? 6.92100  14.69300  22.28300 1.000 32.02976 ?  289 TYR   A CD2  1 
ATOM   925  C  CE1  . TYR   A 1 137 ? 6.42300  16.11800  19.97800 1.000 40.60252 ?  289 TYR   A CE1  1 
ATOM   926  C  CE2  . TYR   A 1 137 ? 5.62400  14.86100  21.84900 1.000 37.44125 ?  289 TYR   A CE2  1 
ATOM   927  C  CZ   . TYR   A 1 137 ? 5.38000  15.57300  20.69500 1.000 39.55679 ?  289 TYR   A CZ   1 
ATOM   928  O  OH   . TYR   A 1 137 ? 4.08900  15.74300  20.25500 1.000 38.97842 ?  289 TYR   A OH   1 
ATOM   929  N  N    . LYS   A 1 138 ? 11.28400 15.71000  25.20100 1.000 29.84575 ?  290 LYS   A N    1 
ATOM   930  C  CA   . LYS   A 1 138 ? 12.60100 15.62400  25.81500 1.000 28.17287 ?  290 LYS   A CA   1 
ATOM   931  C  C    . LYS   A 1 138 ? 12.45800 14.76100  27.05900 1.000 31.94140 ?  290 LYS   A C    1 
ATOM   932  O  O    . LYS   A 1 138 ? 11.70800 15.11100  27.97800 1.000 35.39211 ?  290 LYS   A O    1 
ATOM   933  C  CB   . LYS   A 1 138 ? 13.13700 17.01400  26.16000 1.000 35.28263 ?  290 LYS   A CB   1 
ATOM   934  C  CG   . LYS   A 1 138 ? 14.47000 17.02200  26.88700 1.000 43.63529 ?  290 LYS   A CG   1 
ATOM   935  C  CD   . LYS   A 1 138 ? 15.09400 18.40600  26.81100 1.000 53.79475 ?  290 LYS   A CD   1 
ATOM   936  C  CE   . LYS   A 1 138 ? 16.44500 18.45300  27.48600 1.000 56.53681 ?  290 LYS   A CE   1 
ATOM   937  N  NZ   . LYS   A 1 138 ? 16.60600 19.66800  28.33000 1.000 64.89153 ?  290 LYS   A NZ   1 
ATOM   938  N  N    . TYR   A 1 139 ? 13.16800 13.63900  27.08600 1.000 29.49115 ?  291 TYR   A N    1 
ATOM   939  C  CA   . TYR   A 1 139 ? 12.93100 12.57900  28.05600 1.000 29.98338 ?  291 TYR   A CA   1 
ATOM   940  C  C    . TYR   A 1 139 ? 14.13500 12.42600  28.97500 1.000 32.19273 ?  291 TYR   A C    1 
ATOM   941  O  O    . TYR   A 1 139 ? 15.27800 12.39800  28.50500 1.000 27.35106 ?  291 TYR   A O    1 
ATOM   942  C  CB   . TYR   A 1 139 ? 12.63900 11.26100  27.33500 1.000 26.25118 ?  291 TYR   A CB   1 
ATOM   943  C  CG   . TYR   A 1 139 ? 11.65200 11.40400  26.19400 1.000 28.30588 ?  291 TYR   A CG   1 
ATOM   944  C  CD1  . TYR   A 1 139 ? 12.08300 11.42700  24.87300 1.000 27.80308 ?  291 TYR   A CD1  1 
ATOM   945  C  CD2  . TYR   A 1 139 ? 10.29000 11.52300  26.44200 1.000 28.39465 ?  291 TYR   A CD2  1 
ATOM   946  C  CE1  . TYR   A 1 139 ? 11.18300 11.55700  23.82900 1.000 24.43858 ?  291 TYR   A CE1  1 
ATOM   947  C  CE2  . TYR   A 1 139 ? 9.38300  11.65400  25.40500 1.000 29.09161 ?  291 TYR   A CE2  1 
ATOM   948  C  CZ   . TYR   A 1 139 ? 9.83500  11.67000  24.10000 1.000 30.10628 ?  291 TYR   A CZ   1 
ATOM   949  O  OH   . TYR   A 1 139 ? 8.93400  11.80200  23.06800 1.000 29.48723 ?  291 TYR   A OH   1 
ATOM   950  N  N    . ASP   A 1 140 ? 13.87900 12.32500  30.27700 1.000 36.14866 ?  292 ASP   A N    1 
ATOM   951  C  CA   . ASP   A 1 140 ? 14.92500 12.11900  31.27200 1.000 37.06912 ?  292 ASP   A CA   1 
ATOM   952  C  C    . ASP   A 1 140 ? 14.63100 10.84600  32.07000 1.000 32.26252 ?  292 ASP   A C    1 
ATOM   953  O  O    . ASP   A 1 140 ? 13.68200 10.11200  31.78300 1.000 34.56620 ?  292 ASP   A O    1 
ATOM   954  C  CB   . ASP   A 1 140 ? 15.07700 13.35300  32.17400 1.000 41.15196 ?  292 ASP   A CB   1 
ATOM   955  C  CG   . ASP   A 1 140 ? 13.84400 13.63900  33.03400 1.000 43.43835 ?  292 ASP   A CG   1 
ATOM   956  O  OD1  . ASP   A 1 140 ? 13.84500 14.68900  33.71400 1.000 49.05246 ?  292 ASP   A OD1  1 
ATOM   957  O  OD2  . ASP   A 1 140 ? 12.87800 12.84600  33.04400 1.000 39.35204 ?  292 ASP   A OD2  1 
ATOM   958  N  N    . VAL   A 1 141 ? 15.46100 10.59700  33.08800 1.000 34.59379 ?  293 VAL   A N    1 
ATOM   959  C  CA   . VAL   A 1 141 ? 15.34300 9.37500   33.88000 1.000 32.24307 ?  293 VAL   A CA   1 
ATOM   960  C  C    . VAL   A 1 141 ? 13.97700 9.27700   34.54600 1.000 33.44855 ?  293 VAL   A C    1 
ATOM   961  O  O    . VAL   A 1 141 ? 13.45400 8.17400   34.74700 1.000 34.05722 ?  293 VAL   A O    1 
ATOM   962  C  CB   . VAL   A 1 141 ? 16.48200 9.30200   34.91600 1.000 31.92242 ?  293 VAL   A CB   1 
ATOM   963  C  CG1  . VAL   A 1 141 ? 17.81600 9.16100   34.22100 1.000 31.63288 ?  293 VAL   A CG1  1 
ATOM   964  C  CG2  . VAL   A 1 141 ? 16.47600 10.53100  35.81300 1.000 35.24915 ?  293 VAL   A CG2  1 
ATOM   965  N  N    . THR   A 1 142 ? 13.37500 10.41400  34.89700 1.000 36.50605 ?  294 THR   A N    1 
ATOM   966  C  CA   . THR   A 1 142 ? 12.06700 10.38100  35.54000 1.000 33.84885 ?  294 THR   A CA   1 
ATOM   967  C  C    . THR   A 1 142 ? 10.97900 9.94200   34.56900 1.000 30.14216 ?  294 THR   A C    1 
ATOM   968  O  O    . THR   A 1 142 ? 10.01200 9.28800   34.97900 1.000 32.88887 ?  294 THR   A O    1 
ATOM   969  C  CB   . THR   A 1 142 ? 11.73300 11.75100  36.13300 1.000 41.52006 ?  294 THR   A CB   1 
ATOM   970  O  OG1  . THR   A 1 142 ? 11.61400 12.71200  35.08000 1.000 52.93488 ?  294 THR   A OG1  1 
ATOM   971  C  CG2  . THR   A 1 142 ? 12.82600 12.19700  37.09500 1.000 38.04014 ?  294 THR   A CG2  1 
ATOM   972  N  N    . ASP   A 1 143 ? 11.12100 10.28700  33.28500 1.000 31.09604 ?  295 ASP   A N    1 
ATOM   973  C  CA   . ASP   A 1 143 ? 10.15600 9.83200   32.28900 1.000 32.12073 ?  295 ASP   A CA   1 
ATOM   974  C  C    . ASP   A 1 143 ? 10.18300 8.31600   32.14800 1.000 30.47323 ?  295 ASP   A C    1 
ATOM   975  O  O    . ASP   A 1 143 ? 9.13000  7.67200   32.07900 1.000 29.78667 ?  295 ASP   A O    1 
ATOM   976  C  CB   . ASP   A 1 143 ? 10.43200 10.49800  30.94000 1.000 30.66626 ?  295 ASP   A CB   1 
ATOM   977  C  CG   . ASP   A 1 143 ? 10.02300 11.95900  30.91400 1.000 35.25436 ?  295 ASP   A CG   1 
ATOM   978  O  OD1  . ASP   A 1 143 ? 9.01300  12.30700  31.55900 1.000 37.26177 ?  295 ASP   A OD1  1 
ATOM   979  O  OD2  . ASP   A 1 143 ? 10.70200 12.75900  30.23900 1.000 38.65696 ?  295 ASP   A OD2  1 
ATOM   980  N  N    . VAL   A 1 144 ? 11.38300 7.72800   32.10700 1.000 28.92009 ?  296 VAL   A N    1 
ATOM   981  C  CA   . VAL   A 1 144 ? 11.49900 6.27700   32.02000 1.000 26.40514 ?  296 VAL   A CA   1 
ATOM   982  C  C    . VAL   A 1 144 ? 10.94200 5.62000   33.27700 1.000 27.44321 ?  296 VAL   A C    1 
ATOM   983  O  O    . VAL   A 1 144 ? 10.34100 4.54100   33.20800 1.000 28.68446 ?  296 VAL   A O    1 
ATOM   984  C  CB   . VAL   A 1 144 ? 12.96500 5.87500   31.77100 1.000 32.19973 ?  296 VAL   A CB   1 
ATOM   985  C  CG1  . VAL   A 1 144 ? 13.08500 4.36800   31.56800 1.000 28.01274 ?  296 VAL   A CG1  1 
ATOM   986  C  CG2  . VAL   A 1 144 ? 13.53300 6.63100   30.58100 1.000 31.66298 ?  296 VAL   A CG2  1 
ATOM   987  N  N    . SER   A 1 145 ? 11.12000 6.25600   34.43900 1.000 28.92190 ?  297 SER   A N    1 
ATOM   988  C  CA   . SER   A 1 145 ? 10.52600 5.73300   35.66500 1.000 29.23809 ?  297 SER   A CA   1 
ATOM   989  C  C    . SER   A 1 145 ? 9.00400  5.75900   35.59400 1.000 32.95280 ?  297 SER   A C    1 
ATOM   990  O  O    . SER   A 1 145 ? 8.33700  4.85200   36.10600 1.000 29.97978 ?  297 SER   A O    1 
ATOM   991  C  CB   . SER   A 1 145 ? 11.02300 6.53200   36.87000 1.000 36.76999 ?  297 SER   A CB   1 
ATOM   992  O  OG   . SER   A 1 145 ? 10.83200 5.81800   38.08100 1.000 49.19340 ?  297 SER   A OG   1 
ATOM   993  N  N    . LYS   A 1 146 ? 8.43900  6.78300   34.95700 1.000 31.81924 ?  298 LYS   A N    1 
ATOM   994  C  CA   . LYS   A 1 146 ? 6.99300  6.90200   34.82300 1.000 33.36207 ?  298 LYS   A CA   1 
ATOM   995  C  C    . LYS   A 1 146 ? 6.42200  6.00300   33.73400 1.000 33.53140 ?  298 LYS   A C    1 
ATOM   996  O  O    . LYS   A 1 146 ? 5.22700  6.09900   33.43600 1.000 33.95165 ?  298 LYS   A O    1 
ATOM   997  C  CB   . LYS   A 1 146 ? 6.61000  8.36200   34.56200 1.000 34.62876 ?  298 LYS   A CB   1 
ATOM   998  C  CG   . LYS   A 1 146 ? 6.75900  9.24500   35.79300 1.000 41.21930 ?  298 LYS   A CG   1 
ATOM   999  C  CD   . LYS   A 1 146 ? 6.47500  10.70700  35.49600 1.000 50.70944 ?  298 LYS   A CD   1 
ATOM   1000 C  CE   . LYS   A 1 146 ? 6.70500  11.55900  36.73500 1.000 57.22104 ?  298 LYS   A CE   1 
ATOM   1001 N  NZ   . LYS   A 1 146 ? 6.95100  12.99100  36.41300 1.000 56.26582 ?  298 LYS   A NZ   1 
ATOM   1002 N  N    . ALA   A 1 147 ? 7.24600  5.15300   33.12500 1.000 29.72326 ?  299 ALA   A N    1 
ATOM   1003 C  CA   . ALA   A 1 147 ? 6.77600  4.05700   32.29000 1.000 30.63122 ?  299 ALA   A CA   1 
ATOM   1004 C  C    . ALA   A 1 147 ? 6.87300  2.71500   33.00000 1.000 33.09748 ?  299 ALA   A C    1 
ATOM   1005 O  O    . ALA   A 1 147 ? 6.56300  1.68100   32.39800 1.000 31.02199 ?  299 ALA   A O    1 
ATOM   1006 C  CB   . ALA   A 1 147 ? 7.56200  4.01100   30.97600 1.000 31.02461 ?  299 ALA   A CB   1 
ATOM   1007 N  N    . GLY   A 1 148 ? 7.30600  2.70900   34.25900 1.000 31.38223 ?  300 GLY   A N    1 
ATOM   1008 C  CA   . GLY   A 1 148 ? 7.32600  1.51400   35.07800 1.000 34.27356 ?  300 GLY   A CA   1 
ATOM   1009 C  C    . GLY   A 1 148 ? 8.70000  0.98400   35.42300 1.000 35.66263 ?  300 GLY   A C    1 
ATOM   1010 O  O    . GLY   A 1 148 ? 8.79100  0.01200   36.18300 1.000 35.48217 ?  300 GLY   A O    1 
ATOM   1011 N  N    . HIS   A 1 149 ? 9.77000  1.57700   34.90700 1.000 29.77968 ?  301 HIS   A N    1 
ATOM   1012 C  CA   . HIS   A 1 149 ? 11.09200 1.00200   35.10000 1.000 27.58268 ?  301 HIS   A CA   1 
ATOM   1013 C  C    . HIS   A 1 149 ? 11.77700 1.58600   36.33200 1.000 32.04988 ?  301 HIS   A C    1 
ATOM   1014 O  O    . HIS   A 1 149 ? 11.43500 2.66700   36.81900 1.000 34.60595 ?  301 HIS   A O    1 
ATOM   1015 C  CB   . HIS   A 1 149 ? 11.95600 1.20800   33.85600 1.000 24.92195 ?  301 HIS   A CB   1 
ATOM   1016 C  CG   . HIS   A 1 149 ? 11.54600 0.34900   32.70000 1.000 24.98137 ?  301 HIS   A CG   1 
ATOM   1017 N  ND1  . HIS   A 1 149 ? 11.63100 -1.02800  32.73300 1.000 24.20777 ?  301 HIS   A ND1  1 
ATOM   1018 C  CD2  . HIS   A 1 149 ? 11.03600 0.66600   31.48700 1.000 26.66338 ?  301 HIS   A CD2  1 
ATOM   1019 C  CE1  . HIS   A 1 149 ? 11.19700 -1.52000  31.58600 1.000 25.89927 ?  301 HIS   A CE1  1 
ATOM   1020 N  NE2  . HIS   A 1 149 ? 10.83000 -0.51400  30.81200 1.000 25.78334 ?  301 HIS   A NE2  1 
ATOM   1021 N  N    . THR   A 1 150 ? 12.75500 0.83900   36.83600 1.000 31.39623 ?  302 THR   A N    1 
ATOM   1022 C  CA   . THR   A 1 150 ? 13.45000 1.13900   38.07600 1.000 33.20098 ?  302 THR   A CA   1 
ATOM   1023 C  C    . THR   A 1 150 ? 14.91600 1.44900   37.79400 1.000 31.17200 ?  302 THR   A C    1 
ATOM   1024 O  O    . THR   A 1 150 ? 15.40000 1.32100   36.66600 1.000 30.97811 ?  302 THR   A O    1 
ATOM   1025 C  CB   . THR   A 1 150 ? 13.33800 -0.03000  39.06300 1.000 36.38327 ?  302 THR   A CB   1 
ATOM   1026 O  OG1  . THR   A 1 150 ? 14.10700 -1.14000  38.58300 1.000 38.12838 ?  302 THR   A OG1  1 
ATOM   1027 C  CG2  . THR   A 1 150 ? 11.88800 -0.46300  39.21800 1.000 36.42620 ?  302 THR   A CG2  1 
ATOM   1028 N  N    . LEU   A 1 151 ? 15.62400 1.85500   38.85300 1.000 29.85304 ?  303 LEU   A N    1 
ATOM   1029 C  CA   . LEU   A 1 151 ? 17.03300 2.21500   38.71800 1.000 29.68627 ?  303 LEU   A CA   1 
ATOM   1030 C  C    . LEU   A 1 151 ? 17.88600 1.03200   38.28000 1.000 30.93514 ?  303 LEU   A C    1 
ATOM   1031 O  O    . LEU   A 1 151 ? 18.94200 1.22800   37.66900 1.000 33.06967 ?  303 LEU   A O    1 
ATOM   1032 C  CB   . LEU   A 1 151 ? 17.55600 2.78500   40.03900 1.000 31.63305 ?  303 LEU   A CB   1 
ATOM   1033 C  CG   . LEU   A 1 151 ? 18.94100 3.43700   40.02000 1.000 47.92241 ?  303 LEU   A CG   1 
ATOM   1034 C  CD1  . LEU   A 1 151 ? 18.93800 4.71400   40.83800 1.000 48.46200 ?  303 LEU   A CD1  1 
ATOM   1035 C  CD2  . LEU   A 1 151 ? 19.99600 2.47300   40.54400 1.000 52.11095 ?  303 LEU   A CD2  1 
ATOM   1036 N  N    . GLU   A 1 152 ? 17.45200 -0.19500  38.58900 1.000 32.35388 ?  304 GLU   A N    1 
ATOM   1037 C  CA   . GLU   A 1 152 ? 18.17900 -1.37800  38.14000 1.000 33.90049 ?  304 GLU   A CA   1 
ATOM   1038 C  C    . GLU   A 1 152 ? 18.42700 -1.35000  36.64100 1.000 31.87658 ?  304 GLU   A C    1 
ATOM   1039 O  O    . GLU   A 1 152 ? 19.45600 -1.84700  36.16800 1.000 31.96166 ?  304 GLU   A O    1 
ATOM   1040 C  CB   . GLU   A 1 152 ? 17.41700 -2.64900  38.51300 1.000 43.58907 ?  304 GLU   A CB   1 
ATOM   1041 C  CG   . GLU   A 1 152 ? 17.64700 -3.12700  39.93400 1.000 57.68899 ?  304 GLU   A CG   1 
ATOM   1042 C  CD   . GLU   A 1 152 ? 16.60300 -2.61700  40.90600 1.000 71.23430 ?  304 GLU   A CD   1 
ATOM   1043 O  OE1  . GLU   A 1 152 ? 16.28900 -3.34400  41.87100 1.000 77.31608 ?  304 GLU   A OE1  1 
ATOM   1044 O  OE2  . GLU   A 1 152 ? 16.09500 -1.49500  40.70500 1.000 74.64973 ?  304 GLU   A OE2  1 
ATOM   1045 N  N    . LEU   A 1 153 ? 17.49700 -0.78300  35.87800 1.000 26.40520 ?  305 LEU   A N    1 
ATOM   1046 C  CA   . LEU   A 1 153 ? 17.67900 -0.56400  34.45000 1.000 24.48931 ?  305 LEU   A CA   1 
ATOM   1047 C  C    . LEU   A 1 153 ? 18.14300 0.84800   34.12400 1.000 27.88146 ?  305 LEU   A C    1 
ATOM   1048 O  O    . LEU   A 1 153 ? 19.01800 1.02300   33.27200 1.000 27.71407 ?  305 LEU   A O    1 
ATOM   1049 C  CB   . LEU   A 1 153 ? 16.37100 -0.85200  33.70100 1.000 23.69645 ?  305 LEU   A CB   1 
ATOM   1050 C  CG   . LEU   A 1 153 ? 16.37000 -0.53700  32.20400 1.000 22.79347 ?  305 LEU   A CG   1 
ATOM   1051 C  CD1  . LEU   A 1 153 ? 17.34500 -1.44200  31.47000 1.000 26.16417 ?  305 LEU   A CD1  1 
ATOM   1052 C  CD2  . LEU   A 1 153 ? 14.97200 -0.65700  31.62100 1.000 22.84574 ?  305 LEU   A CD2  1 
ATOM   1053 N  N    . ILE   A 1 154 ? 17.59700 1.85800   34.81000 1.000 29.47377 ?  306 ILE   A N    1 
ATOM   1054 C  CA   . ILE   A 1 154 ? 17.75600 3.23800   34.36000 1.000 26.47452 ?  306 ILE   A CA   1 
ATOM   1055 C  C    . ILE   A 1 154 ? 19.18900 3.72600   34.55900 1.000 27.91790 ?  306 ILE   A C    1 
ATOM   1056 O  O    . ILE   A 1 154 ? 19.75800 4.37900   33.67400 1.000 27.05685 ?  306 ILE   A O    1 
ATOM   1057 C  CB   . ILE   A 1 154 ? 16.73300 4.14800   35.06400 1.000 28.22616 ?  306 ILE   A CB   1 
ATOM   1058 C  CG1  . ILE   A 1 154 ? 15.31600 3.81200   34.59000 1.000 28.45605 ?  306 ILE   A CG1  1 
ATOM   1059 C  CG2  . ILE   A 1 154 ? 17.04100 5.61100   34.79600 1.000 28.02694 ?  306 ILE   A CG2  1 
ATOM   1060 C  CD1  . ILE   A 1 154 ? 14.21900 4.47800   35.39900 1.000 29.28858 ?  306 ILE   A CD1  1 
ATOM   1061 N  N    A GLU   A 1 155 ? 19.79500 3.42800   35.71000 0.470 30.53374 ?  307 GLU   A N    1 
ATOM   1062 N  N    B GLU   A 1 155 ? 19.79200 3.43400   35.71500 0.530 30.74028 ?  307 GLU   A N    1 
ATOM   1063 C  CA   A GLU   A 1 155 ? 21.17700 3.84900   35.93200 0.470 28.57875 ?  307 GLU   A CA   1 
ATOM   1064 C  CA   B GLU   A 1 155 ? 21.17800 3.84400   35.93600 0.530 28.23431 ?  307 GLU   A CA   1 
ATOM   1065 C  C    A GLU   A 1 155 ? 22.15200 3.20200   34.95300 0.470 30.07849 ?  307 GLU   A C    1 
ATOM   1066 C  C    B GLU   A 1 155 ? 22.13900 3.20200   34.94200 0.530 30.14317 ?  307 GLU   A C    1 
ATOM   1067 O  O    A GLU   A 1 155 ? 22.95500 3.93300   34.35000 0.470 31.56725 ?  307 GLU   A O    1 
ATOM   1068 O  O    B GLU   A 1 155 ? 22.92100 3.93900   34.31900 0.530 31.42326 ?  307 GLU   A O    1 
ATOM   1069 C  CB   A GLU   A 1 155 ? 21.57700 3.58800   37.38900 0.470 34.35304 ?  307 GLU   A CB   1 
ATOM   1070 C  CB   B GLU   A 1 155 ? 21.59300 3.55700   37.38300 0.530 34.37976 ?  307 GLU   A CB   1 
ATOM   1071 C  CG   A GLU   A 1 155 ? 23.05200 3.82400   37.68000 0.470 39.58446 ?  307 GLU   A CG   1 
ATOM   1072 C  CG   B GLU   A 1 155 ? 23.06800 3.83200   37.66600 0.530 39.58969 ?  307 GLU   A CG   1 
ATOM   1073 C  CD   A GLU   A 1 155 ? 23.27300 4.67200   38.91900 0.470 41.25532 ?  307 GLU   A CD   1 
ATOM   1074 C  CD   B GLU   A 1 155 ? 23.79000 2.63000   38.24900 0.530 47.86744 ?  307 GLU   A CD   1 
ATOM   1075 O  OE1  A GLU   A 1 155 ? 24.44300 4.86500   39.31100 0.470 45.30621 ?  307 GLU   A OE1  1 
ATOM   1076 O  OE1  B GLU   A 1 155 ? 23.12400 1.61400   38.52900 0.530 54.21566 ?  307 GLU   A OE1  1 
ATOM   1077 O  OE2  A GLU   A 1 155 ? 22.27600 5.14900   39.50300 0.470 47.52376 ?  307 GLU   A OE2  1 
ATOM   1078 O  OE2  B GLU   A 1 155 ? 25.02300 2.69500   38.43500 0.530 54.68985 ?  307 GLU   A OE2  1 
ATOM   1079 N  N    . PRO   A 1 156 ? 22.14600 1.87800   34.73800 1.000 28.10927 ?  308 PRO   A N    1 
ATOM   1080 C  CA   . PRO   A 1 156 ? 23.03900 1.32800   33.70100 1.000 26.72681 ?  308 PRO   A CA   1 
ATOM   1081 C  C    . PRO   A 1 156 ? 22.72100 1.84000   32.30900 1.000 27.96840 ?  308 PRO   A C    1 
ATOM   1082 O  O    . PRO   A 1 156 ? 23.62600 1.92800   31.47000 1.000 27.10648 ?  308 PRO   A O    1 
ATOM   1083 C  CB   . PRO   A 1 156 ? 22.81400 -0.18800  33.80900 1.000 28.86733 ?  308 PRO   A CB   1 
ATOM   1084 C  CG   . PRO   A 1 156 ? 22.30500 -0.39900  35.18000 1.000 34.28280 ?  308 PRO   A CG   1 
ATOM   1085 C  CD   . PRO   A 1 156 ? 21.43900 0.79300   35.44600 1.000 28.74994 ?  308 PRO   A CD   1 
ATOM   1086 N  N    . LEU   A 1 157 ? 21.46200 2.19700   32.04200 1.000 25.85967 ?  309 LEU   A N    1 
ATOM   1087 C  CA   . LEU   A 1 157 ? 21.11000 2.72600   30.72900 1.000 23.09371 ?  309 LEU   A CA   1 
ATOM   1088 C  C    . LEU   A 1 157 ? 21.70000 4.11400   30.51400 1.000 24.69866 ?  309 LEU   A C    1 
ATOM   1089 O  O    . LEU   A 1 157 ? 22.17900 4.42500   29.41800 1.000 24.34098 ?  309 LEU   A O    1 
ATOM   1090 C  CB   . LEU   A 1 157 ? 19.58900 2.76000   30.57100 1.000 23.62160 ?  309 LEU   A CB   1 
ATOM   1091 C  CG   . LEU   A 1 157 ? 19.04800 3.41900   29.30000 1.000 24.19694 ?  309 LEU   A CG   1 
ATOM   1092 C  CD1  . LEU   A 1 157 ? 19.54400 2.69200   28.05600 1.000 22.38424 ?  309 LEU   A CD1  1 
ATOM   1093 C  CD2  . LEU   A 1 157 ? 17.52800 3.46200   29.33000 1.000 26.54718 ?  309 LEU   A CD2  1 
ATOM   1094 N  N    . ILE   A 1 158 ? 21.66800 4.96300   31.54400 1.000 23.88644 ?  310 ILE   A N    1 
ATOM   1095 C  CA   . ILE   A 1 158 ? 22.27500 6.28700   31.42700 1.000 25.94025 ?  310 ILE   A CA   1 
ATOM   1096 C  C    . ILE   A 1 158 ? 23.78200 6.16900   31.25300 1.000 27.72175 ?  310 ILE   A C    1 
ATOM   1097 O  O    . ILE   A 1 158 ? 24.38200 6.86100   30.42000 1.000 28.36788 ?  310 ILE   A O    1 
ATOM   1098 C  CB   . ILE   A 1 158 ? 21.91300 7.15200   32.64800 1.000 30.97966 ?  310 ILE   A CB   1 
ATOM   1099 C  CG1  . ILE   A 1 158 ? 20.47400 7.64300   32.52600 1.000 33.55945 ?  310 ILE   A CG1  1 
ATOM   1100 C  CG2  . ILE   A 1 158 ? 22.87100 8.33000   32.77500 1.000 34.74414 ?  310 ILE   A CG2  1 
ATOM   1101 C  CD1  . ILE   A 1 158 ? 20.25500 8.57300   31.35400 1.000 35.18547 ?  310 ILE   A CD1  1 
ATOM   1102 N  N    . LYS   A 1 159 ? 24.41800 5.29000   32.03000 1.000 27.74934 ?  311 LYS   A N    1 
ATOM   1103 C  CA   . LYS   A 1 159 ? 25.86000 5.10900   31.90800 1.000 29.98745 ?  311 LYS   A CA   1 
ATOM   1104 C  C    . LYS   A 1 159 ? 26.23400 4.56100   30.53700 1.000 25.94787 ?  311 LYS   A C    1 
ATOM   1105 O  O    . LYS   A 1 159 ? 27.28600 4.90800   29.98800 1.000 27.53782 ?  311 LYS   A O    1 
ATOM   1106 C  CB   . LYS   A 1 159 ? 26.36200 4.19600   33.02400 1.000 32.56666 ?  311 LYS   A CB   1 
ATOM   1107 C  CG   . LYS   A 1 159 ? 26.39000 4.90100   34.37000 1.000 42.52009 ?  311 LYS   A CG   1 
ATOM   1108 C  CD   . LYS   A 1 159 ? 26.54600 3.96100   35.54900 1.000 50.46588 ?  311 LYS   A CD   1 
ATOM   1109 C  CE   . LYS   A 1 159 ? 26.62900 4.76700   36.83600 1.000 55.23132 ?  311 LYS   A CE   1 
ATOM   1110 N  NZ   . LYS   A 1 159 ? 27.99200 5.32000   37.05500 1.000 62.00913 ?  311 LYS   A NZ   1 
ATOM   1111 N  N    . PHE   A 1 160 ? 25.38300 3.70500   29.96500 1.000 26.03676 ?  312 PHE   A N    1 
ATOM   1112 C  CA   . PHE   A 1 160 ? 25.60600 3.24400   28.59900 1.000 26.20464 ?  312 PHE   A CA   1 
ATOM   1113 C  C    . PHE   A 1 160 ? 25.55000 4.40500   27.61500 1.000 28.85656 ?  312 PHE   A C    1 
ATOM   1114 O  O    . PHE   A 1 160 ? 26.42900 4.55100   26.75600 1.000 24.12842 ?  312 PHE   A O    1 
ATOM   1115 C  CB   . PHE   A 1 160 ? 24.57600 2.17500   28.22600 1.000 24.46724 ?  312 PHE   A CB   1 
ATOM   1116 C  CG   . PHE   A 1 160 ? 24.60300 1.79200   26.77300 1.000 23.15598 ?  312 PHE   A CG   1 
ATOM   1117 C  CD1  . PHE   A 1 160 ? 25.48600 0.82700   26.31200 1.000 26.77664 ?  312 PHE   A CD1  1 
ATOM   1118 C  CD2  . PHE   A 1 160 ? 23.74800 2.40100   25.87000 1.000 21.91974 ?  312 PHE   A CD2  1 
ATOM   1119 C  CE1  . PHE   A 1 160 ? 25.51500 0.47800   24.97100 1.000 27.18620 ?  312 PHE   A CE1  1 
ATOM   1120 C  CE2  . PHE   A 1 160 ? 23.77300 2.05900   24.53300 1.000 27.92518 ?  312 PHE   A CE2  1 
ATOM   1121 C  CZ   . PHE   A 1 160 ? 24.65700 1.09400   24.08100 1.000 28.57665 ?  312 PHE   A CZ   1 
ATOM   1122 N  N    . GLN   A 1 161 ? 24.51300 5.24000   27.72200 1.000 25.11965 ?  313 GLN   A N    1 
ATOM   1123 C  CA   . GLN   A 1 161 ? 24.38300 6.38500   26.82500 1.000 26.23221 ?  313 GLN   A CA   1 
ATOM   1124 C  C    . GLN   A 1 161 ? 25.58400 7.31300   26.93700 1.000 24.41263 ?  313 GLN   A C    1 
ATOM   1125 O  O    . GLN   A 1 161 ? 26.10100 7.79600   25.92200 1.000 21.69349 ?  313 GLN   A O    1 
ATOM   1126 C  CB   . GLN   A 1 161 ? 23.09300 7.14800   27.12900 1.000 24.62413 ?  313 GLN   A CB   1 
ATOM   1127 C  CG   . GLN   A 1 161 ? 21.82500 6.35700   26.89300 1.000 22.22707 ?  313 GLN   A CG   1 
ATOM   1128 C  CD   . GLN   A 1 161 ? 21.63900 5.97500   25.44400 1.000 20.48093 ?  313 GLN   A CD   1 
ATOM   1129 O  OE1  . GLN   A 1 161 ? 22.08200 6.68600   24.54100 1.000 24.10386 ?  313 GLN   A OE1  1 
ATOM   1130 N  NE2  . GLN   A 1 161 ? 20.97600 4.84800   25.20900 1.000 23.30847 ?  313 GLN   A NE2  1 
ATOM   1131 N  N    . VAL   A 1 162 ? 26.04800 7.56500   28.16200 1.000 24.39510 ?  314 VAL   A N    1 
ATOM   1132 C  CA   . VAL   A 1 162 ? 27.20500 8.43500   28.36000 1.000 26.85459 ?  314 VAL   A CA   1 
ATOM   1133 C  C    . VAL   A 1 162 ? 28.45600 7.79300   27.77800 1.000 26.68229 ?  314 VAL   A C    1 
ATOM   1134 O  O    . VAL   A 1 162 ? 29.24000 8.44300   27.07400 1.000 27.30613 ?  314 VAL   A O    1 
ATOM   1135 C  CB   . VAL   A 1 162 ? 27.38000 8.75700   29.85400 1.000 30.27249 ?  314 VAL   A CB   1 
ATOM   1136 C  CG1  . VAL   A 1 162 ? 28.71800 9.43800   30.09900 1.000 28.81774 ?  314 VAL   A CG1  1 
ATOM   1137 C  CG2  . VAL   A 1 162 ? 26.23700 9.62400   30.34500 1.000 26.88752 ?  314 VAL   A CG2  1 
ATOM   1138 N  N    . GLY   A 1 163 ? 28.66400 6.50600   28.05900 1.000 28.42441 ?  315 GLY   A N    1 
ATOM   1139 C  CA   . GLY   A 1 163 ? 29.83600 5.82400   27.53500 1.000 27.01923 ?  315 GLY   A CA   1 
ATOM   1140 C  C    . GLY   A 1 163 ? 29.84000 5.74600   26.02000 1.000 25.99937 ?  315 GLY   A C    1 
ATOM   1141 O  O    . GLY   A 1 163 ? 30.88800 5.89300   25.38600 1.000 25.25927 ?  315 GLY   A O    1 
ATOM   1142 N  N    . LEU   A 1 164 ? 28.66900 5.51600   25.42000 1.000 22.72832 ?  316 LEU   A N    1 
ATOM   1143 C  CA   . LEU   A 1 164 ? 28.58300 5.46700   23.96400 1.000 23.53420 ?  316 LEU   A CA   1 
ATOM   1144 C  C    . LEU   A 1 164 ? 28.81100 6.84400   23.35400 1.000 25.94517 ?  316 LEU   A C    1 
ATOM   1145 O  O    . LEU   A 1 164 ? 29.48800 6.97100   22.32600 1.000 27.85949 ?  316 LEU   A O    1 
ATOM   1146 C  CB   . LEU   A 1 164 ? 27.22700 4.90600   23.54000 1.000 23.70893 ?  316 LEU   A CB   1 
ATOM   1147 C  CG   . LEU   A 1 164 ? 26.98500 4.68900   22.04600 1.000 26.83974 ?  316 LEU   A CG   1 
ATOM   1148 C  CD1  . LEU   A 1 164 ? 27.99100 3.70500   21.47600 1.000 26.18155 ?  316 LEU   A CD1  1 
ATOM   1149 C  CD2  . LEU   A 1 164 ? 25.56600 4.20100   21.81700 1.000 24.80127 ?  316 LEU   A CD2  1 
ATOM   1150 N  N    . LYS   A 1 165 ? 28.24900 7.88700   23.97200 1.000 23.85875 ?  317 LYS   A N    1 
ATOM   1151 C  CA   . LYS   A 1 165 ? 28.45900 9.24800   23.48900 1.000 25.34176 ?  317 LYS   A CA   1 
ATOM   1152 C  C    . LYS   A 1 165 ? 29.93100 9.63600   23.55400 1.000 31.48088 ?  317 LYS   A C    1 
ATOM   1153 O  O    . LYS   A 1 165 ? 30.44200 10.32200  22.66000 1.000 32.92656 ?  317 LYS   A O    1 
ATOM   1154 C  CB   . LYS   A 1 165 ? 27.61400 10.22300  24.31200 1.000 34.49687 ?  317 LYS   A CB   1 
ATOM   1155 C  CG   . LYS   A 1 165 ? 27.18600 11.48300  23.57800 1.000 37.09589 ?  317 LYS   A CG   1 
ATOM   1156 C  CD   . LYS   A 1 165 ? 25.97800 11.23400  22.68600 1.000 36.03932 ?  317 LYS   A CD   1 
ATOM   1157 C  CE   . LYS   A 1 165 ? 25.73600 12.40400  21.74000 1.000 37.74692 ?  317 LYS   A CE   1 
ATOM   1158 N  NZ   . LYS   A 1 165 ? 24.46200 12.27200  20.97400 1.000 27.77438 ?  317 LYS   A NZ   1 
ATOM   1159 N  N    . LYS   A 1 166 ? 30.63000 9.20100   24.60600 1.000 27.82368 ?  318 LYS   A N    1 
ATOM   1160 C  CA   . LYS   A 1 166 ? 32.04200 9.53200   24.76800 1.000 25.26165 ?  318 LYS   A CA   1 
ATOM   1161 C  C    . LYS   A 1 166 ? 32.92200 8.88400   23.71100 1.000 30.69953 ?  318 LYS   A C    1 
ATOM   1162 O  O    . LYS   A 1 166 ? 34.05500 9.33400   23.50700 1.000 30.87693 ?  318 LYS   A O    1 
ATOM   1163 C  CB   . LYS   A 1 166 ? 32.52900 9.11100   26.15400 1.000 31.88823 ?  318 LYS   A CB   1 
ATOM   1164 C  CG   . LYS   A 1 166 ? 32.09500 10.02600  27.27800 1.000 38.16066 ?  318 LYS   A CG   1 
ATOM   1165 C  CD   . LYS   A 1 166 ? 32.55200 9.47100   28.61300 1.000 38.46825 ?  318 LYS   A CD   1 
ATOM   1166 C  CE   . LYS   A 1 166 ? 32.28100 10.44500  29.74000 1.000 43.78329 ?  318 LYS   A CE   1 
ATOM   1167 N  NZ   . LYS   A 1 166 ? 32.87700 9.97200   31.01800 1.000 40.74583 ?  318 LYS   A NZ   1 
ATOM   1168 N  N    . LEU   A 1 167 ? 32.44400 7.83000   23.04800 1.000 28.36575 ?  319 LEU   A N    1 
ATOM   1169 C  CA   . LEU   A 1 167 ? 33.22400 7.23600   21.97100 1.000 27.52251 ?  319 LEU   A CA   1 
ATOM   1170 C  C    . LEU   A 1 167 ? 33.30400 8.15000   20.75600 1.000 34.15606 ?  319 LEU   A C    1 
ATOM   1171 O  O    . LEU   A 1 167 ? 34.22900 8.00000   19.94900 1.000 33.69464 ?  319 LEU   A O    1 
ATOM   1172 C  CB   . LEU   A 1 167 ? 32.63900 5.87900   21.57000 1.000 27.47710 ?  319 LEU   A CB   1 
ATOM   1173 C  CG   . LEU   A 1 167 ? 32.75100 4.74200   22.59000 1.000 31.60419 ?  319 LEU   A CG   1 
ATOM   1174 C  CD1  . LEU   A 1 167 ? 32.22300 3.43300   22.01600 1.000 31.33307 ?  319 LEU   A CD1  1 
ATOM   1175 C  CD2  . LEU   A 1 167 ? 34.18300 4.58300   23.07500 1.000 30.67419 ?  319 LEU   A CD2  1 
ATOM   1176 N  N    A ASN   A 1 168 ? 32.37600 9.09600   20.63100 0.560 30.29487 ?  320 ASN   A N    1 
ATOM   1177 N  N    B ASN   A 1 168 ? 32.36500 9.08700   20.61200 0.440 30.40649 ?  320 ASN   A N    1 
ATOM   1178 C  CA   A ASN   A 1 168 ? 32.27400 10.01000  19.49400 0.560 31.25896 ?  320 ASN   A CA   1 
ATOM   1179 C  CA   B ASN   A 1 168 ? 32.32500 10.01700  19.48400 0.440 31.30529 ?  320 ASN   A CA   1 
ATOM   1180 C  C    A ASN   A 1 168 ? 32.43900 9.26000   18.17500 0.560 30.66512 ?  320 ASN   A C    1 
ATOM   1181 C  C    B ASN   A 1 168 ? 32.43500 9.27000   18.15800 0.440 30.73685 ?  320 ASN   A C    1 
ATOM   1182 O  O    A ASN   A 1 168 ? 33.32400 9.54000   17.36500 0.560 32.47383 ?  320 ASN   A O    1 
ATOM   1183 O  O    B ASN   A 1 168 ? 33.29100 9.55900   17.31700 0.440 32.71156 ?  320 ASN   A O    1 
ATOM   1184 C  CB   A ASN   A 1 168 ? 33.28000 11.15300  19.60400 0.560 33.97931 ?  320 ASN   A CB   1 
ATOM   1185 C  CB   B ASN   A 1 168 ? 33.41900 11.07800  19.61000 0.440 33.83266 ?  320 ASN   A CB   1 
ATOM   1186 C  CG   A ASN   A 1 168 ? 32.86900 12.36100  18.78300 0.560 35.84684 ?  320 ASN   A CG   1 
ATOM   1187 C  CG   B ASN   A 1 168 ? 33.29700 11.88800  20.88200 0.440 36.90679 ?  320 ASN   A CG   1 
ATOM   1188 O  OD1  A ASN   A 1 168 ? 31.71600 12.47800  18.36900 0.560 37.59709 ?  320 ASN   A OD1  1 
ATOM   1189 O  OD1  B ASN   A 1 168 ? 34.07800 11.71500  21.81700 0.440 41.41527 ?  320 ASN   A OD1  1 
ATOM   1190 N  ND2  A ASN   A 1 168 ? 33.81000 13.26900  18.54600 0.560 37.22927 ?  320 ASN   A ND2  1 
ATOM   1191 N  ND2  B ASN   A 1 168 ? 32.31300 12.77800  20.92500 0.440 37.40293 ?  320 ASN   A ND2  1 
ATOM   1192 N  N    . LEU   A 1 169 ? 31.55900 8.28200   17.98500 1.000 27.81095 ?  321 LEU   A N    1 
ATOM   1193 C  CA   . LEU   A 1 169 ? 31.60900 7.44300   16.80000 1.000 27.19179 ?  321 LEU   A CA   1 
ATOM   1194 C  C    . LEU   A 1 169 ? 31.33800 8.26100   15.54700 1.000 28.64781 ?  321 LEU   A C    1 
ATOM   1195 O  O    . LEU   A 1 169 ? 30.52700 9.19000   15.55300 1.000 31.02749 ?  321 LEU   A O    1 
ATOM   1196 C  CB   . LEU   A 1 169 ? 30.58100 6.31300   16.90800 1.000 26.21177 ?  321 LEU   A CB   1 
ATOM   1197 C  CG   . LEU   A 1 169 ? 30.72900 5.31400   18.05600 1.000 26.92083 ?  321 LEU   A CG   1 
ATOM   1198 C  CD1  . LEU   A 1 169 ? 29.74400 4.16900   17.88900 1.000 24.98793 ?  321 LEU   A CD1  1 
ATOM   1199 C  CD2  . LEU   A 1 169 ? 32.15100 4.78800   18.12900 1.000 22.75759 ?  321 LEU   A CD2  1 
ATOM   1200 N  N    . HIS   A 1 170 ? 32.03400 7.87200   14.49900 1.000 26.69532 ?  322 HIS   A N    1 
ATOM   1201 C  CA   . HIS   A 1 170 ? 31.62800 8.40700   13.19600 1.000 24.94976 ?  322 HIS   A CA   1 
ATOM   1202 C  C    . HIS   A 1 170 ? 30.25400 7.79800   12.90500 1.000 28.98865 ?  322 HIS   A C    1 
ATOM   1203 O  O    . HIS   A 1 170 ? 29.98100 6.71600   13.37000 1.000 31.17591 ?  322 HIS   A O    1 
ATOM   1204 C  CB   . HIS   A 1 170 ? 32.59900 7.91600   12.14000 1.000 24.77488 ?  322 HIS   A CB   1 
ATOM   1205 C  CG   . HIS   A 1 170 ? 33.96900 8.46300   12.29400 1.000 26.78569 ?  322 HIS   A CG   1 
ATOM   1206 N  ND1  . HIS   A 1 170 ? 34.96600 8.23300   11.39000 1.000 28.39740 ?  322 HIS   A ND1  1 
ATOM   1207 C  CD2  . HIS   A 1 170 ? 34.50200 9.24500   13.23600 1.000 28.40268 ?  322 HIS   A CD2  1 
ATOM   1208 C  CE1  . HIS   A 1 170 ? 36.04600 8.83700   11.78400 1.000 29.30290 ?  322 HIS   A CE1  1 
ATOM   1209 N  NE2  . HIS   A 1 170 ? 35.78900 9.46300   12.89500 1.000 29.16289 ?  322 HIS   A NE2  1 
ATOM   1210 N  N    . GLU   A 1 171 ? 29.48200 8.43900   12.02300 1.000 25.81933 ?  323 GLU   A N    1 
ATOM   1211 C  CA   . GLU   A 1 171 ? 28.16400 7.88300   11.61400 1.000 26.09219 ?  323 GLU   A CA   1 
ATOM   1212 C  C    . GLU   A 1 171 ? 28.39000 6.46800   11.06000 1.000 26.87539 ?  323 GLU   A C    1 
ATOM   1213 O  O    . GLU   A 1 171 ? 27.56400 5.58100   11.35100 1.000 27.61265 ?  323 GLU   A O    1 
ATOM   1214 C  CB   . GLU   A 1 171 ? 27.50400 8.78600   10.57100 1.000 30.95585 ?  323 GLU   A CB   1 
ATOM   1215 C  CG   . GLU   A 1 171 ? 26.02400 8.50700   10.38000 1.000 40.56684 ?  323 GLU   A CG   1 
ATOM   1216 C  CD   . GLU   A 1 171 ? 25.28700 9.54200   9.54800  1.000 46.64837 ?  323 GLU   A CD   1 
ATOM   1217 O  OE1  . GLU   A 1 171 ? 25.95100 10.25300  8.76800  1.000 54.69483 ?  323 GLU   A OE1  1 
ATOM   1218 O  OE2  . GLU   A 1 171 ? 24.05000 9.63400   9.68300  1.000 53.09655 ?  323 GLU   A OE2  1 
ATOM   1219 N  N    . GLU   A 1 172 ? 29.47700 6.29700   10.30100 1.000 27.49661 ?  324 GLU   A N    1 
ATOM   1220 C  CA   . GLU   A 1 172 ? 29.84200 4.99200   9.69000  1.000 28.85809 ?  324 GLU   A CA   1 
ATOM   1221 C  C    . GLU   A 1 172 ? 29.96700 3.93700   10.79400 1.000 28.05030 ?  324 GLU   A C    1 
ATOM   1222 O  O    . GLU   A 1 172 ? 29.48800 2.80700   10.57900 1.000 26.00783 ?  324 GLU   A O    1 
ATOM   1223 C  CB   . GLU   A 1 172 ? 31.14700 5.11900   8.90200  1.000 27.24119 ?  324 GLU   A CB   1 
ATOM   1224 C  CG   . GLU   A 1 172 ? 31.00800 5.94000   7.63200  1.000 29.23799 ?  324 GLU   A CG   1 
ATOM   1225 C  CD   . GLU   A 1 172 ? 31.20700 7.43400   7.81900  1.000 32.43443 ?  324 GLU   A CD   1 
ATOM   1226 O  OE1  . GLU   A 1 172 ? 31.51600 8.11700   6.82300  1.000 35.10209 ?  324 GLU   A OE1  1 
ATOM   1227 O  OE2  . GLU   A 1 172 ? 31.05200 7.91100   8.96100  1.000 28.76166 ?  324 GLU   A OE2  1 
ATOM   1228 N  N    . GLU   A 1 173 ? 30.58500 4.29200   11.92700 1.000 22.63068 ?  325 GLU   A N    1 
ATOM   1229 C  CA   . GLU   A 1 173 ? 30.72500 3.31700   13.00500 1.000 22.26693 ?  325 GLU   A CA   1 
ATOM   1230 C  C    . GLU   A 1 173 ? 29.40200 3.09500   13.72800 1.000 22.70881 ?  325 GLU   A C    1 
ATOM   1231 O  O    . GLU   A 1 173 ? 29.10900 1.98000   14.17300 1.000 21.99899 ?  325 GLU   A O    1 
ATOM   1232 C  CB   . GLU   A 1 173 ? 31.81200 3.77600   13.97900 1.000 22.38374 ?  325 GLU   A CB   1 
ATOM   1233 C  CG   . GLU   A 1 173 ? 33.20900 3.74800   13.37100 1.000 23.53303 ?  325 GLU   A CG   1 
ATOM   1234 C  CD   . GLU   A 1 173 ? 34.13300 4.81200   13.94100 1.000 28.63957 ?  325 GLU   A CD   1 
ATOM   1235 O  OE1  . GLU   A 1 173 ? 35.32400 4.82200   13.57000 1.000 31.17734 ?  325 GLU   A OE1  1 
ATOM   1236 O  OE2  . GLU   A 1 173 ? 33.66800 5.63800   14.75000 1.000 25.84068 ?  325 GLU   A OE2  1 
ATOM   1237 N  N    . HIS   A 1 174 ? 28.58500 4.14400   13.84300 1.000 24.03315 ?  326 HIS   A N    1 
ATOM   1238 C  CA   . HIS   A 1 174 ? 27.28400 4.01700   14.49500 1.000 25.85802 ?  326 HIS   A CA   1 
ATOM   1239 C  C    . HIS   A 1 174 ? 26.38400 3.03200   13.75500 1.000 22.91035 ?  326 HIS   A C    1 
ATOM   1240 O  O    . HIS   A 1 174 ? 25.75700 2.16000   14.37000 1.000 21.44765 ?  326 HIS   A O    1 
ATOM   1241 C  CB   . HIS   A 1 174 ? 26.62100 5.39200   14.58900 1.000 24.72911 ?  326 HIS   A CB   1 
ATOM   1242 C  CG   . HIS   A 1 174 ? 25.36100 5.40600   15.39500 1.000 25.39341 ?  326 HIS   A CG   1 
ATOM   1243 N  ND1  . HIS   A 1 174 ? 24.12100 5.60400   14.82700 1.000 27.76008 ?  326 HIS   A ND1  1 
ATOM   1244 C  CD2  . HIS   A 1 174 ? 25.14700 5.25800   16.72400 1.000 21.05294 ?  326 HIS   A CD2  1 
ATOM   1245 C  CE1  . HIS   A 1 174 ? 23.19700 5.57200   15.77000 1.000 21.97352 ?  326 HIS   A CE1  1 
ATOM   1246 N  NE2  . HIS   A 1 174 ? 23.79300 5.36400   16.93000 1.000 29.43871 ?  326 HIS   A NE2  1 
ATOM   1247 N  N    . VAL   A 1 175 ? 26.30800 3.15300   12.42700 1.000 23.00439 ?  327 VAL   A N    1 
ATOM   1248 C  CA   . VAL   A 1 175 ? 25.41100 2.28100   11.67500 1.000 21.92394 ?  327 VAL   A CA   1 
ATOM   1249 C  C    . VAL   A 1 175 ? 25.98200 0.87300   11.57100 1.000 22.87590 ?  327 VAL   A C    1 
ATOM   1250 O  O    . VAL   A 1 175 ? 25.22700 -0.10700  11.52300 1.000 24.05337 ?  327 VAL   A O    1 
ATOM   1251 C  CB   . VAL   A 1 175 ? 25.12100 2.87500   10.28500 1.000 23.63582 ?  327 VAL   A CB   1 
ATOM   1252 C  CG1  . VAL   A 1 175 ? 24.49400 4.25100   10.42300 1.000 25.15085 ?  327 VAL   A CG1  1 
ATOM   1253 C  CG2  . VAL   A 1 175 ? 26.38200 2.93400   9.45000  1.000 21.88521 ?  327 VAL   A CG2  1 
ATOM   1254 N  N    . LEU   A 1 176 ? 27.31100 0.73800   11.53400 1.000 21.47204 ?  328 LEU   A N    1 
ATOM   1255 C  CA   . LEU   A 1 176 ? 27.90500 -0.59300  11.52100 1.000 21.47566 ?  328 LEU   A CA   1 
ATOM   1256 C  C    . LEU   A 1 176 ? 27.63200 -1.31900  12.82900 1.000 27.23912 ?  328 LEU   A C    1 
ATOM   1257 O  O    . LEU   A 1 176 ? 27.34000 -2.52000  12.83300 1.000 23.86746 ?  328 LEU   A O    1 
ATOM   1258 C  CB   . LEU   A 1 176 ? 29.41100 -0.49600  11.26500 1.000 22.39784 ?  328 LEU   A CB   1 
ATOM   1259 C  CG   . LEU   A 1 176 ? 29.84600 -0.45300  9.79900  1.000 23.53909 ?  328 LEU   A CG   1 
ATOM   1260 C  CD1  . LEU   A 1 176 ? 31.27000 0.05100   9.66700  1.000 24.40323 ?  328 LEU   A CD1  1 
ATOM   1261 C  CD2  . LEU   A 1 176 ? 29.69200 -1.82300  9.16700  1.000 26.59771 ?  328 LEU   A CD2  1 
ATOM   1262 N  N    . LEU   A 1 177 ? 27.69700 -0.59700  13.95100 1.000 23.56149 ?  329 LEU   A N    1 
ATOM   1263 C  CA   . LEU   A 1 177 ? 27.44700 -1.21100  15.25100 1.000 19.82659 ?  329 LEU   A CA   1 
ATOM   1264 C  C    . LEU   A 1 177 ? 26.00100 -1.67700  15.37300 1.000 19.24365 ?  329 LEU   A C    1 
ATOM   1265 O  O    . LEU   A 1 177 ? 25.73200 -2.74800  15.93200 1.000 24.18790 ?  329 LEU   A O    1 
ATOM   1266 C  CB   . LEU   A 1 177 ? 27.79000 -0.22800  16.37000 1.000 20.96854 ?  329 LEU   A CB   1 
ATOM   1267 C  CG   . LEU   A 1 177 ? 27.74600 -0.77800  17.79700 1.000 25.39096 ?  329 LEU   A CG   1 
ATOM   1268 C  CD1  . LEU   A 1 177 ? 28.72000 -1.93500  17.93900 1.000 24.32278 ?  329 LEU   A CD1  1 
ATOM   1269 C  CD2  . LEU   A 1 177 ? 28.05000 0.31400   18.80900 1.000 23.26568 ?  329 LEU   A CD2  1 
ATOM   1270 N  N    . MET   A 1 178 ? 25.05600 -0.88600  14.85900 1.000 20.48386 ?  330 MET   A N    1 
ATOM   1271 C  CA   . MET   A 1 178 ? 23.65800 -1.30300  14.87500 1.000 21.61720 ?  330 MET   A CA   1 
ATOM   1272 C  C    . MET   A 1 178 ? 23.44900 -2.55600  14.03400 1.000 22.35567 ?  330 MET   A C    1 
ATOM   1273 O  O    . MET   A 1 178 ? 22.73100 -3.47700  14.44100 1.000 23.14553 ?  330 MET   A O    1 
ATOM   1274 C  CB   . MET   A 1 178 ? 22.76200 -0.16800  14.37700 1.000 19.56324 ?  330 MET   A CB   1 
ATOM   1275 C  CG   . MET   A 1 178 ? 22.57000 0.96200   15.38000 1.000 23.19552 ?  330 MET   A CG   1 
ATOM   1276 S  SD   . MET   A 1 178 ? 21.28100 2.12700   14.88800 1.000 25.52494 ?  330 MET   A SD   1 
ATOM   1277 C  CE   . MET   A 1 178 ? 22.00100 2.81200   13.39800 1.000 22.46286 ?  330 MET   A CE   1 
ATOM   1278 N  N    . ALA   A 1 179 ? 24.07700 -2.61200  12.85800 1.000 21.07559 ?  331 ALA   A N    1 
ATOM   1279 C  CA   . ALA   A 1 179 ? 23.94600 -3.78700  12.00300 1.000 21.33272 ?  331 ALA   A CA   1 
ATOM   1280 C  C    . ALA   A 1 179 ? 24.57200 -5.01600  12.65000 1.000 26.60005 ?  331 ALA   A C    1 
ATOM   1281 O  O    . ALA   A 1 179 ? 23.98800 -6.10500  12.61400 1.000 28.66456 ?  331 ALA   A O    1 
ATOM   1282 C  CB   . ALA   A 1 179 ? 24.58300 -3.51400  10.64100 1.000 21.61629 ?  331 ALA   A CB   1 
ATOM   1283 N  N    . ILE   A 1 180 ? 25.75800 -4.86100  13.24200 1.000 22.03317 ?  332 ILE   A N    1 
ATOM   1284 C  CA   . ILE   A 1 180 ? 26.40300 -5.98000  13.92500 1.000 24.23344 ?  332 ILE   A CA   1 
ATOM   1285 C  C    . ILE   A 1 180 ? 25.55400 -6.44500  15.09700 1.000 24.90569 ?  332 ILE   A C    1 
ATOM   1286 O  O    . ILE   A 1 180 ? 25.41500 -7.64900  15.34600 1.000 23.48196 ?  332 ILE   A O    1 
ATOM   1287 C  CB   . ILE   A 1 180 ? 27.82000 -5.58200  14.37700 1.000 23.26761 ?  332 ILE   A CB   1 
ATOM   1288 C  CG1  . ILE   A 1 180 ? 28.72300 -5.36300  13.16400 1.000 24.58711 ?  332 ILE   A CG1  1 
ATOM   1289 C  CG2  . ILE   A 1 180 ? 28.41800 -6.63700  15.29800 1.000 25.04992 ?  332 ILE   A CG2  1 
ATOM   1290 C  CD1  . ILE   A 1 180 ? 29.97000 -4.56900  13.48300 1.000 23.77273 ?  332 ILE   A CD1  1 
ATOM   1291 N  N    . CYS   A 1 181 ? 24.97900 -5.49800  15.84000 1.000 21.18811 ?  333 CYS   A N    1 
ATOM   1292 C  CA   . CYS   A 1 181 ? 24.11800 -5.85700  16.96100 1.000 25.88233 ?  333 CYS   A CA   1 
ATOM   1293 C  C    . CYS   A 1 181 ? 22.97900 -6.76200  16.51000 1.000 31.66617 ?  333 CYS   A C    1 
ATOM   1294 O  O    . CYS   A 1 181 ? 22.64700 -7.74100  17.18700 1.000 26.29193 ?  333 CYS   A O    1 
ATOM   1295 C  CB   . CYS   A 1 181 ? 23.57600 -4.58900  17.61900 1.000 22.52633 ?  333 CYS   A CB   1 
ATOM   1296 S  SG   . CYS   A 1 181 ? 22.39000 -4.85800  18.95000 1.000 24.82807 ?  333 CYS   A SG   1 
ATOM   1297 N  N    . ILE   A 1 182 ? 22.38900 -6.47200  15.34900 1.000 26.38445 ?  334 ILE   A N    1 
ATOM   1298 C  CA   . ILE   A 1 182 ? 21.21100 -7.21200  14.90000 1.000 24.12681 ?  334 ILE   A CA   1 
ATOM   1299 C  C    . ILE   A 1 182 ? 21.58300 -8.63400  14.49400 1.000 28.57491 ?  334 ILE   A C    1 
ATOM   1300 O  O    . ILE   A 1 182 ? 20.91500 -9.60200  14.87800 1.000 27.55642 ?  334 ILE   A O    1 
ATOM   1301 C  CB   . ILE   A 1 182 ? 20.52200 -6.46400  13.74500 1.000 28.50973 ?  334 ILE   A CB   1 
ATOM   1302 C  CG1  . ILE   A 1 182 ? 19.86800 -5.18400  14.26700 1.000 25.30887 ?  334 ILE   A CG1  1 
ATOM   1303 C  CG2  . ILE   A 1 182 ? 19.50500 -7.36400  13.04700 1.000 30.36815 ?  334 ILE   A CG2  1 
ATOM   1304 C  CD1  . ILE   A 1 182 ? 19.54000 -4.17300  13.19200 1.000 24.51237 ?  334 ILE   A CD1  1 
ATOM   1305 N  N    A VAL   A 1 183 ? 22.64500 -8.77200  13.70800 0.620 28.59715 ?  335 VAL   A N    1 
ATOM   1306 N  N    B VAL   A 1 183 ? 22.65900 -8.79200  13.72500 0.380 28.18152 ?  335 VAL   A N    1 
ATOM   1307 C  CA   A VAL   A 1 183 ? 23.05700 -10.05100 13.14600 0.620 26.97533 ?  335 VAL   A CA   1 
ATOM   1308 C  CA   B VAL   A 1 183 ? 22.99700 -10.09300 13.14700 0.380 27.62201 ?  335 VAL   A CA   1 
ATOM   1309 C  C    A VAL   A 1 183 ? 24.06000 -10.71000 14.08300 0.620 29.04542 ?  335 VAL   A C    1 
ATOM   1310 C  C    B VAL   A 1 183 ? 23.98600 -10.85400 14.02800 0.380 28.92926 ?  335 VAL   A C    1 
ATOM   1311 O  O    A VAL   A 1 183 ? 25.23700 -10.85800 13.74200 0.620 30.34260 ?  335 VAL   A O    1 
ATOM   1312 O  O    B VAL   A 1 183 ? 25.06500 -11.25200 13.57600 0.380 30.70585 ?  335 VAL   A O    1 
ATOM   1313 C  CB   A VAL   A 1 183 ? 23.65400 -9.86200  11.73700 0.620 28.90230 ?  335 VAL   A CB   1 
ATOM   1314 C  CB   B VAL   A 1 183 ? 23.54700 -9.93400  11.71500 0.380 28.98561 ?  335 VAL   A CB   1 
ATOM   1315 C  CG1  A VAL   A 1 183 ? 23.80900 -11.19700 11.02800 0.620 25.76609 ?  335 VAL   A CG1  1 
ATOM   1316 C  CG1  B VAL   A 1 183 ? 22.45100 -9.44900  10.78100 0.380 28.51691 ?  335 VAL   A CG1  1 
ATOM   1317 C  CG2  A VAL   A 1 183 ? 22.79500 -8.91000  10.92000 0.620 28.37219 ?  335 VAL   A CG2  1 
ATOM   1318 C  CG2  B VAL   A 1 183 ? 24.72700 -8.97600  11.69200 0.380 27.03063 ?  335 VAL   A CG2  1 
ATOM   1319 N  N    . SER   A 1 184 ? 23.61500 -11.09500 15.27400 1.000 28.78898 ?  336 SER   A N    1 
ATOM   1320 C  CA   . SER   A 1 184 ? 24.50600 -11.82400 16.16900 1.000 30.45986 ?  336 SER   A CA   1 
ATOM   1321 C  C    . SER   A 1 184 ? 24.10100 -13.28900 16.24900 1.000 32.87883 ?  336 SER   A C    1 
ATOM   1322 O  O    . SER   A 1 184 ? 22.92700 -13.58700 16.50900 1.000 35.00831 ?  336 SER   A O    1 
ATOM   1323 C  CB   . SER   A 1 184 ? 24.51000 -11.19000 17.56100 1.000 37.81579 ?  336 SER   A CB   1 
ATOM   1324 O  OG   . SER   A 1 184 ? 24.58900 -9.77600  17.46100 1.000 41.33577 ?  336 SER   A OG   1 
ATOM   1325 N  N    . PRO   A 1 185 ? 25.03300 -14.22400 16.01500 1.000 29.15986 ?  337 PRO   A N    1 
ATOM   1326 C  CA   . PRO   A 1 185 ? 24.64700 -15.64200 15.91100 1.000 32.43453 ?  337 PRO   A CA   1 
ATOM   1327 C  C    . PRO   A 1 185 ? 24.25900 -16.29900 17.22300 1.000 41.89282 ?  337 PRO   A C    1 
ATOM   1328 O  O    . PRO   A 1 185 ? 23.64200 -17.37300 17.19000 1.000 43.26049 ?  337 PRO   A O    1 
ATOM   1329 C  CB   . PRO   A 1 185 ? 25.90300 -16.31100 15.32400 1.000 36.12304 ?  337 PRO   A CB   1 
ATOM   1330 C  CG   . PRO   A 1 185 ? 27.02700 -15.40500 15.68200 1.000 34.37536 ?  337 PRO   A CG   1 
ATOM   1331 C  CD   . PRO   A 1 185 ? 26.45000 -14.01000 15.67300 1.000 29.18097 ?  337 PRO   A CD   1 
ATOM   1332 N  N    . ASP   A 1 186 ? 24.59900 -15.71100 18.36600 1.000 37.36354 ?  338 ASP   A N    1 
ATOM   1333 C  CA   . ASP   A 1 186 ? 24.32800 -16.32600 19.65900 1.000 40.68888 ?  338 ASP   A CA   1 
ATOM   1334 C  C    . ASP   A 1 186 ? 22.97700 -15.92800 20.23800 1.000 39.31355 ?  338 ASP   A C    1 
ATOM   1335 O  O    . ASP   A 1 186 ? 22.72400 -16.18400 21.42100 1.000 45.08833 ?  338 ASP   A O    1 
ATOM   1336 C  CB   . ASP   A 1 186 ? 25.44500 -15.97900 20.64900 1.000 32.97582 ?  338 ASP   A CB   1 
ATOM   1337 C  CG   . ASP   A 1 186 ? 25.56200 -14.49000 20.89400 1.000 38.75691 ?  338 ASP   A CG   1 
ATOM   1338 O  OD1  . ASP   A 1 186 ? 25.87800 -14.09200 22.03600 1.000 46.28331 ?  338 ASP   A OD1  1 
ATOM   1339 O  OD2  . ASP   A 1 186 ? 25.33800 -13.71200 19.94300 1.000 37.50589 ?  338 ASP   A OD2  1 
ATOM   1340 N  N    . ARG   A 1 187 ? 22.10700 -15.32200 19.43800 1.000 35.52340 ?  339 ARG   A N    1 
ATOM   1341 C  CA   . ARG   A 1 187 ? 20.78000 -14.96800 19.91800 1.000 32.10093 ?  339 ARG   A CA   1 
ATOM   1342 C  C    . ARG   A 1 187 ? 19.95600 -16.22900 20.17400 1.000 38.61135 ?  339 ARG   A C    1 
ATOM   1343 O  O    . ARG   A 1 187 ? 20.08400 -17.21500 19.44100 1.000 32.52802 ?  339 ARG   A O    1 
ATOM   1344 C  CB   . ARG   A 1 187 ? 20.06100 -14.07700 18.90700 1.000 30.23569 ?  339 ARG   A CB   1 
ATOM   1345 C  CG   . ARG   A 1 187 ? 20.82100 -12.81800 18.53600 1.000 33.69894 ?  339 ARG   A CG   1 
ATOM   1346 C  CD   . ARG   A 1 187 ? 20.83300 -11.83500 19.68900 1.000 27.99064 ?  339 ARG   A CD   1 
ATOM   1347 N  NE   . ARG   A 1 187 ? 21.15900 -10.47700 19.27000 1.000 27.47512 ?  339 ARG   A NE   1 
ATOM   1348 C  CZ   . ARG   A 1 187 ? 21.19500 -9.43300  20.09100 1.000 25.79333 ?  339 ARG   A CZ   1 
ATOM   1349 N  NH1  . ARG   A 1 187 ? 20.91900 -9.58700  21.37900 1.000 30.21166 ?  339 ARG   A NH1  1 
ATOM   1350 N  NH2  . ARG   A 1 187 ? 21.49400 -8.22700  19.62100 1.000 25.58554 ?  339 ARG   A NH2  1 
ATOM   1351 N  N    . PRO   A 1 188 ? 19.10200 -16.22600 21.19500 1.000 45.97611 ?  340 PRO   A N    1 
ATOM   1352 C  CA   . PRO   A 1 188 ? 18.26600 -17.40500 21.45200 1.000 44.95798 ?  340 PRO   A CA   1 
ATOM   1353 C  C    . PRO   A 1 188 ? 17.29500 -17.64100 20.30600 1.000 40.05962 ?  340 PRO   A C    1 
ATOM   1354 O  O    . PRO   A 1 188 ? 16.59900 -16.72600 19.86000 1.000 42.05838 ?  340 PRO   A O    1 
ATOM   1355 C  CB   . PRO   A 1 188 ? 17.53400 -17.04200 22.75100 1.000 53.22080 ?  340 PRO   A CB   1 
ATOM   1356 C  CG   . PRO   A 1 188 ? 17.53400 -15.54400 22.77600 1.000 54.55153 ?  340 PRO   A CG   1 
ATOM   1357 C  CD   . PRO   A 1 188 ? 18.84200 -15.14200 22.15800 1.000 50.82716 ?  340 PRO   A CD   1 
ATOM   1358 N  N    . GLY   A 1 189 ? 17.26300 -18.88100 19.82100 1.000 44.11444 ?  341 GLY   A N    1 
ATOM   1359 C  CA   . GLY   A 1 189 ? 16.34100 -19.28600 18.78300 1.000 45.44621 ?  341 GLY   A CA   1 
ATOM   1360 C  C    . GLY   A 1 189 ? 16.91100 -19.29900 17.38000 1.000 41.40886 ?  341 GLY   A C    1 
ATOM   1361 O  O    . GLY   A 1 189 ? 16.19600 -19.68900 16.44800 1.000 40.62001 ?  341 GLY   A O    1 
ATOM   1362 N  N    . VAL   A 1 190 ? 18.16800 -18.88800 17.20000 1.000 36.34208 ?  342 VAL   A N    1 
ATOM   1363 C  CA   . VAL   A 1 190 ? 18.75000 -18.84800 15.86300 1.000 34.33865 ?  342 VAL   A CA   1 
ATOM   1364 C  C    . VAL   A 1 190 ? 18.87400 -20.26200 15.31600 1.000 36.97295 ?  342 VAL   A C    1 
ATOM   1365 O  O    . VAL   A 1 190 ? 19.35600 -21.17200 16.00200 1.000 44.77215 ?  342 VAL   A O    1 
ATOM   1366 C  CB   . VAL   A 1 190 ? 20.11100 -18.13700 15.89200 1.000 39.21031 ?  342 VAL   A CB   1 
ATOM   1367 C  CG1  . VAL   A 1 190 ? 20.81200 -18.28100 14.55100 1.000 39.75474 ?  342 VAL   A CG1  1 
ATOM   1368 C  CG2  . VAL   A 1 190 ? 19.93500 -16.66800 16.23700 1.000 35.53713 ?  342 VAL   A CG2  1 
ATOM   1369 N  N    . GLN   A 1 191 ? 18.42200 -20.45400 14.07700 1.000 40.68490 ?  343 GLN   A N    1 
ATOM   1370 C  CA   . GLN   A 1 191 ? 18.53600 -21.75400 13.40400 1.000 45.08229 ?  343 GLN   A CA   1 
ATOM   1371 C  C    . GLN   A 1 191 ? 19.89800 -21.86900 12.72600 1.000 48.35121 ?  343 GLN   A C    1 
ATOM   1372 O  O    . GLN   A 1 191 ? 20.72700 -22.70100 13.10700 1.000 48.32735 ?  343 GLN   A O    1 
ATOM   1373 C  CB   . GLN   A 1 191 ? 17.40500 -21.93200 12.39000 1.000 50.84226 ?  343 GLN   A CB   1 
ATOM   1374 C  CG   . GLN   A 1 191 ? 16.15500 -22.59700 12.93300 1.000 58.58382 ?  343 GLN   A CG   1 
ATOM   1375 C  CD   . GLN   A 1 191 ? 14.90100 -22.11800 12.23100 1.000 60.33671 ?  343 GLN   A CD   1 
ATOM   1376 O  OE1  . GLN   A 1 191 ? 13.86400 -21.90900 12.85800 1.000 53.73544 ?  343 GLN   A OE1  1 
ATOM   1377 N  NE2  . GLN   A 1 191 ? 14.99300 -21.93000 10.92000 1.000 55.32097 ?  343 GLN   A NE2  1 
ATOM   1378 N  N    . ASP   A 1 192 ? 20.13400 -21.03000 11.71800 1.000 45.31388 ?  344 ASP   A N    1 
ATOM   1379 C  CA   . ASP   A 1 192 ? 21.34700 -21.08900 10.90200 1.000 42.97475 ?  344 ASP   A CA   1 
ATOM   1380 C  C    . ASP   A 1 192 ? 22.40400 -20.15200 11.48900 1.000 44.44354 ?  344 ASP   A C    1 
ATOM   1381 O  O    . ASP   A 1 192 ? 22.73400 -19.10200 10.93500 1.000 40.78317 ?  344 ASP   A O    1 
ATOM   1382 C  CB   . ASP   A 1 192 ? 21.02300 -20.73500 9.45600  1.000 43.88484 ?  344 ASP   A CB   1 
ATOM   1383 C  CG   . ASP   A 1 192 ? 22.10100 -21.17400 8.48600  1.000 51.18091 ?  344 ASP   A CG   1 
ATOM   1384 O  OD1  . ASP   A 1 192 ? 21.81400 -21.24100 7.27200  1.000 49.24682 ?  344 ASP   A OD1  1 
ATOM   1385 O  OD2  . ASP   A 1 192 ? 23.23700 -21.44800 8.93000  1.000 48.56534 ?  344 ASP   A OD2  1 
ATOM   1386 N  N    . ALA   A 1 193 ? 22.94600 -20.57100 12.63700 1.000 42.23557 ?  345 ALA   A N    1 
ATOM   1387 C  CA   . ALA   A 1 193 ? 23.92100 -19.74500 13.34500 1.000 45.76284 ?  345 ALA   A CA   1 
ATOM   1388 C  C    . ALA   A 1 193 ? 25.15400 -19.48600 12.49200 1.000 42.59184 ?  345 ALA   A C    1 
ATOM   1389 O  O    . ALA   A 1 193 ? 25.75900 -18.41000 12.57300 1.000 39.27959 ?  345 ALA   A O    1 
ATOM   1390 C  CB   . ALA   A 1 193 ? 24.31800 -20.41100 14.66400 1.000 44.12075 ?  345 ALA   A CB   1 
ATOM   1391 N  N    . LYS   A 1 194 ? 25.54500 -20.45700 11.66300 1.000 48.66741 ?  346 LYS   A N    1 
ATOM   1392 C  CA   . LYS   A 1 194 ? 26.72600 -20.27800 10.82600 1.000 49.94007 ?  346 LYS   A CA   1 
ATOM   1393 C  C    . LYS   A 1 194 ? 26.50400 -19.20500 9.76600  1.000 43.53439 ?  346 LYS   A C    1 
ATOM   1394 O  O    . LYS   A 1 194 ? 27.41500 -18.42300 9.46700  1.000 40.04739 ?  346 LYS   A O    1 
ATOM   1395 C  CB   . LYS   A 1 194 ? 27.11700 -21.60500 10.16800 1.000 59.89923 ?  346 LYS   A CB   1 
ATOM   1396 C  CG   . LYS   A 1 194 ? 28.35300 -22.25600 10.78100 1.000 67.78083 ?  346 LYS   A CG   1 
ATOM   1397 C  CD   . LYS   A 1 194 ? 29.59300 -21.40600 10.53300 1.000 75.16252 ?  346 LYS   A CD   1 
ATOM   1398 C  CE   . LYS   A 1 194 ? 30.79900 -21.91300 11.32200 1.000 79.83073 ?  346 LYS   A CE   1 
ATOM   1399 N  NZ   . LYS   A 1 194 ? 31.58100 -20.80900 11.96500 1.000 80.77750 ?  346 LYS   A NZ   1 
ATOM   1400 N  N    . LEU   A 1 195 ? 25.30400 -19.16500 9.17800  1.000 37.44978 ?  347 LEU   A N    1 
ATOM   1401 C  CA   . LEU   A 1 195 ? 25.02000 -18.11900 8.20100  1.000 40.29981 ?  347 LEU   A CA   1 
ATOM   1402 C  C    . LEU   A 1 195 ? 24.96600 -16.74900 8.86700  1.000 39.19016 ?  347 LEU   A C    1 
ATOM   1403 O  O    . LEU   A 1 195 ? 25.49700 -15.76900 8.32800  1.000 37.93798 ?  347 LEU   A O    1 
ATOM   1404 C  CB   . LEU   A 1 195 ? 23.71400 -18.41700 7.47000  1.000 41.79102 ?  347 LEU   A CB   1 
ATOM   1405 C  CG   . LEU   A 1 195 ? 23.26500 -17.34300 6.47300  1.000 39.88547 ?  347 LEU   A CG   1 
ATOM   1406 C  CD1  . LEU   A 1 195 ? 24.34200 -17.09500 5.43000  1.000 38.51538 ?  347 LEU   A CD1  1 
ATOM   1407 C  CD2  . LEU   A 1 195 ? 21.94900 -17.71800 5.80700  1.000 37.42606 ?  347 LEU   A CD2  1 
ATOM   1408 N  N    . VAL   A 1 196 ? 24.32500 -16.65700 10.03600 1.000 37.66981 ?  348 VAL   A N    1 
ATOM   1409 C  CA   . VAL   A 1 196 ? 24.32300 -15.40300 10.78500 1.000 30.69378 ?  348 VAL   A CA   1 
ATOM   1410 C  C    . VAL   A 1 196 ? 25.74900 -14.97300 11.10000 1.000 30.68294 ?  348 VAL   A C    1 
ATOM   1411 O  O    . VAL   A 1 196 ? 26.08900 -13.78700 11.01900 1.000 30.53990 ?  348 VAL   A O    1 
ATOM   1412 C  CB   . VAL   A 1 196 ? 23.48100 -15.54200 12.06700 1.000 29.76915 ?  348 VAL   A CB   1 
ATOM   1413 C  CG1  . VAL   A 1 196 ? 23.52300 -14.25600 12.86500 1.000 32.81588 ?  348 VAL   A CG1  1 
ATOM   1414 C  CG2  . VAL   A 1 196 ? 22.04900 -15.91900 11.73500 1.000 29.83587 ?  348 VAL   A CG2  1 
ATOM   1415 N  N    . GLU   A 1 197 ? 26.61200 -15.93200 11.45100 1.000 32.15582 ?  349 GLU   A N    1 
ATOM   1416 C  CA   . GLU   A 1 197 ? 28.00600 -15.60400 11.73500 1.000 35.81500 ?  349 GLU   A CA   1 
ATOM   1417 C  C    . GLU   A 1 197 ? 28.70300 -15.04500 10.50000 1.000 33.86528 ?  349 GLU   A C    1 
ATOM   1418 O  O    . GLU   A 1 197 ? 29.44800 -14.06200 10.58500 1.000 34.56653 ?  349 GLU   A O    1 
ATOM   1419 C  CB   . GLU   A 1 197 ? 28.74700 -16.83800 12.25400 1.000 41.67370 ?  349 GLU   A CB   1 
ATOM   1420 C  CG   . GLU   A 1 197 ? 30.21800 -16.58400 12.55100 1.000 52.71681 ?  349 GLU   A CG   1 
ATOM   1421 C  CD   . GLU   A 1 197 ? 30.76400 -17.48200 13.64300 1.000 63.86362 ?  349 GLU   A CD   1 
ATOM   1422 O  OE1  . GLU   A 1 197 ? 30.34200 -18.65500 13.72100 1.000 67.84283 ?  349 GLU   A OE1  1 
ATOM   1423 O  OE2  . GLU   A 1 197 ? 31.61900 -17.01500 14.42500 1.000 65.70542 ?  349 GLU   A OE2  1 
ATOM   1424 N  N    . ALA   A 1 198 ? 28.46900 -15.66300 9.33900  1.000 36.88129 ?  350 ALA   A N    1 
ATOM   1425 C  CA   . ALA   A 1 198 ? 29.12000 -15.21000 8.11500  1.000 40.36765 ?  350 ALA   A CA   1 
ATOM   1426 C  C    . ALA   A 1 198 ? 28.70200 -13.78900 7.75600  1.000 40.68186 ?  350 ALA   A C    1 
ATOM   1427 O  O    . ALA   A 1 198 ? 29.53100 -12.98400 7.31500  1.000 39.76212 ?  350 ALA   A O    1 
ATOM   1428 C  CB   . ALA   A 1 198 ? 28.80900 -16.17500 6.97000  1.000 44.95944 ?  350 ALA   A CB   1 
ATOM   1429 N  N    . ILE   A 1 199 ? 27.42300 -13.45700 7.94600  1.000 36.37539 ?  351 ILE   A N    1 
ATOM   1430 C  CA   . ILE   A 1 199 ? 26.96100 -12.09900 7.67200  1.000 34.00823 ?  351 ILE   A CA   1 
ATOM   1431 C  C    . ILE   A 1 199 ? 27.60000 -11.11000 8.63800  1.000 32.49581 ?  351 ILE   A C    1 
ATOM   1432 O  O    . ILE   A 1 199 ? 28.07500 -10.04300 8.23000  1.000 29.55406 ?  351 ILE   A O    1 
ATOM   1433 C  CB   . ILE   A 1 199 ? 25.42400 -12.03500 7.74000  1.000 34.05252 ?  351 ILE   A CB   1 
ATOM   1434 C  CG1  . ILE   A 1 199 ? 24.80000 -12.96900 6.70500  1.000 39.20157 ?  351 ILE   A CG1  1 
ATOM   1435 C  CG2  . ILE   A 1 199 ? 24.93000 -10.61400 7.52600  1.000 32.58251 ?  351 ILE   A CG2  1 
ATOM   1436 C  CD1  . ILE   A 1 199 ? 23.30400 -13.14500 6.87800  1.000 36.04077 ?  351 ILE   A CD1  1 
ATOM   1437 N  N    . GLN   A 1 200 ? 27.61900 -11.44200 9.93300  1.000 34.50652 ?  352 GLN   A N    1 
ATOM   1438 C  CA   . GLN   A 1 200 ? 28.18900 -10.53100 10.92100 1.000 28.39599 ?  352 GLN   A CA   1 
ATOM   1439 C  C    . GLN   A 1 200 ? 29.68500 -10.35000 10.71800 1.000 28.29099 ?  352 GLN   A C    1 
ATOM   1440 O  O    . GLN   A 1 200 ? 30.20600 -9.24000  10.87700 1.000 30.18776 ?  352 GLN   A O    1 
ATOM   1441 C  CB   . GLN   A 1 200 ? 27.92200 -11.04000 12.33200 1.000 36.50895 ?  352 GLN   A CB   1 
ATOM   1442 C  CG   . GLN   A 1 200 ? 28.18100 -9.99800  13.41000 1.000 35.95605 ?  352 GLN   A CG   1 
ATOM   1443 C  CD   . GLN   A 1 200 ? 28.19400 -10.59400 14.80000 1.000 35.36090 ?  352 GLN   A CD   1 
ATOM   1444 O  OE1  . GLN   A 1 200 ? 28.93200 -11.54000 15.07200 1.000 34.65487 ?  352 GLN   A OE1  1 
ATOM   1445 N  NE2  . GLN   A 1 200 ? 27.37000 -10.05000 15.68700 1.000 27.79686 ?  352 GLN   A NE2  1 
ATOM   1446 N  N    . ASP   A 1 201 ? 30.39300 -11.43400 10.39000 1.000 30.19723 ?  353 ASP   A N    1 
ATOM   1447 C  CA   . ASP   A 1 201 ? 31.83600 -11.34500 10.19100 1.000 34.16326 ?  353 ASP   A CA   1 
ATOM   1448 C  C    . ASP   A 1 201 ? 32.17200 -10.37200 9.07000  1.000 36.84296 ?  353 ASP   A C    1 
ATOM   1449 O  O    . ASP   A 1 201 ? 33.17100 -9.64400  9.14900  1.000 37.94616 ?  353 ASP   A O    1 
ATOM   1450 C  CB   . ASP   A 1 201 ? 32.41000 -12.73000 9.89500  1.000 34.49927 ?  353 ASP   A CB   1 
ATOM   1451 C  CG   . ASP   A 1 201 ? 32.54000 -13.58200 11.14400 1.000 43.20118 ?  353 ASP   A CG   1 
ATOM   1452 O  OD1  . ASP   A 1 201 ? 32.24800 -13.06900 12.24500 1.000 42.39939 ?  353 ASP   A OD1  1 
ATOM   1453 O  OD2  . ASP   A 1 201 ? 32.93400 -14.76000 11.02600 1.000 50.59072 ?  353 ASP   A OD2  1 
ATOM   1454 N  N    A ARG   A 1 202 ? 31.35100 -10.34400 8.02000  0.460 38.41038 ?  354 ARG   A N    1 
ATOM   1455 N  N    B ARG   A 1 202 ? 31.35200 -10.34100 8.01800  0.540 38.34396 ?  354 ARG   A N    1 
ATOM   1456 C  CA   A ARG   A 1 202 ? 31.54000 -9.36700  6.95300  0.460 40.48327 ?  354 ARG   A CA   1 
ATOM   1457 C  CA   B ARG   A 1 202 ? 31.55300 -9.36200  6.95500  0.540 40.56213 ?  354 ARG   A CA   1 
ATOM   1458 C  C    A ARG   A 1 202 ? 31.41000 -7.94500  7.48500  0.460 36.92684 ?  354 ARG   A C    1 
ATOM   1459 C  C    B ARG   A 1 202 ? 31.41400 -7.94100  7.48800  0.540 37.04824 ?  354 ARG   A C    1 
ATOM   1460 O  O    A ARG   A 1 202 ? 32.18900 -7.05900  7.11200  0.460 34.98331 ?  354 ARG   A O    1 
ATOM   1461 O  O    B ARG   A 1 202 ? 32.19400 -7.05300  7.12200  0.540 34.75557 ?  354 ARG   A O    1 
ATOM   1462 C  CB   A ARG   A 1 202 ? 30.53100 -9.61900  5.83400  0.460 43.80291 ?  354 ARG   A CB   1 
ATOM   1463 C  CB   B ARG   A 1 202 ? 30.56200 -9.61200  5.81800  0.540 43.87001 ?  354 ARG   A CB   1 
ATOM   1464 C  CG   A ARG   A 1 202 ? 30.75700 -8.79100  4.58400  0.460 46.04510 ?  354 ARG   A CG   1 
ATOM   1465 C  CG   B ARG   A 1 202 ? 30.85200 -8.83200  4.54400  0.540 46.06417 ?  354 ARG   A CG   1 
ATOM   1466 C  CD   A ARG   A 1 202 ? 30.28300 -9.53300  3.34500  0.460 49.85445 ?  354 ARG   A CD   1 
ATOM   1467 C  CD   B ARG   A 1 202 ? 30.46600 -9.63400  3.30800  0.540 49.79138 ?  354 ARG   A CD   1 
ATOM   1468 N  NE   A ARG   A 1 202 ? 31.00300 -10.78900 3.15100  0.460 53.36084 ?  354 ARG   A NE   1 
ATOM   1469 N  NE   B ARG   A 1 202 ? 29.08700 -10.11400 3.36700  0.540 53.47298 ?  354 ARG   A NE   1 
ATOM   1470 C  CZ   A ARG   A 1 202 ? 32.12900 -10.90200 2.45500  0.460 53.65817 ?  354 ARG   A CZ   1 
ATOM   1471 C  CZ   B ARG   A 1 202 ? 28.08500 -9.60400  2.65700  0.540 57.48149 ?  354 ARG   A CZ   1 
ATOM   1472 N  NH1  A ARG   A 1 202 ? 32.71900 -12.08300 2.32800  0.460 53.39172 ?  354 ARG   A NH1  1 
ATOM   1473 N  NH1  B ARG   A 1 202 ? 28.30500 -8.59100  1.83000  0.540 60.98072 ?  354 ARG   A NH1  1 
ATOM   1474 N  NH2  A ARG   A 1 202 ? 32.66600 -9.83200  1.88400  0.460 50.75696 ?  354 ARG   A NH2  1 
ATOM   1475 N  NH2  B ARG   A 1 202 ? 26.86300 -10.10400 2.77500  0.540 52.40415 ?  354 ARG   A NH2  1 
ATOM   1476 N  N    . LEU   A 1 203 ? 30.43300 -7.70800  8.36300  1.000 31.45580 ?  355 LEU   A N    1 
ATOM   1477 C  CA   . LEU   A 1 203 ? 30.26600 -6.38200  8.94900  1.000 28.51112 ?  355 LEU   A CA   1 
ATOM   1478 C  C    . LEU   A 1 203 ? 31.36100 -6.08100  9.96300  1.000 26.71325 ?  355 LEU   A C    1 
ATOM   1479 O  O    . LEU   A 1 203 ? 31.89100 -4.96300  9.99700  1.000 30.35008 ?  355 LEU   A O    1 
ATOM   1480 C  CB   . LEU   A 1 203 ? 28.89000 -6.26700  9.60500  1.000 26.19837 ?  355 LEU   A CB   1 
ATOM   1481 C  CG   . LEU   A 1 203 ? 27.67200 -6.56700  8.73300  1.000 27.84226 ?  355 LEU   A CG   1 
ATOM   1482 C  CD1  . LEU   A 1 203 ? 26.43900 -6.71700  9.59500  1.000 24.39147 ?  355 LEU   A CD1  1 
ATOM   1483 C  CD2  . LEU   A 1 203 ? 27.47300 -5.47200  7.70500  1.000 31.49070 ?  355 LEU   A CD2  1 
ATOM   1484 N  N    . SER   A 1 204 ? 31.70800 -7.06300  10.80000 1.000 28.82734 ?  356 SER   A N    1 
ATOM   1485 C  CA   . SER   A 1 204 ? 32.75500 -6.85900  11.79700 1.000 30.29499 ?  356 SER   A CA   1 
ATOM   1486 C  C    . SER   A 1 204 ? 34.07800 -6.49700  11.13500 1.000 34.74657 ?  356 SER   A C    1 
ATOM   1487 O  O    . SER   A 1 204 ? 34.75600 -5.54800  11.54900 1.000 32.83014 ?  356 SER   A O    1 
ATOM   1488 C  CB   . SER   A 1 204 ? 32.90800 -8.11200  12.66000 1.000 35.96140 ?  356 SER   A CB   1 
ATOM   1489 O  OG   . SER   A 1 204 ? 31.72200 -8.38100  13.38500 1.000 41.76835 ?  356 SER   A OG   1 
ATOM   1490 N  N    . ASN   A 1 205 ? 34.45700 -7.23800  10.09100 1.000 31.59383 ?  357 ASN   A N    1 
ATOM   1491 C  CA   . ASN   A 1 205 ? 35.69500 -6.94000  9.37900  1.000 35.96281 ?  357 ASN   A CA   1 
ATOM   1492 C  C    . ASN   A 1 205 ? 35.63200 -5.57700  8.70300  1.000 34.27922 ?  357 ASN   A C    1 
ATOM   1493 O  O    . ASN   A 1 205 ? 36.63900 -4.86200  8.64100  1.000 33.80564 ?  357 ASN   A O    1 
ATOM   1494 C  CB   . ASN   A 1 205 ? 35.98200 -8.03800  8.35700  1.000 40.22765 ?  357 ASN   A CB   1 
ATOM   1495 C  CG   . ASN   A 1 205 ? 36.42700 -9.33000  9.00600  1.000 48.85688 ?  357 ASN   A CG   1 
ATOM   1496 O  OD1  . ASN   A 1 205 ? 36.19000 -10.41600 8.47700  1.000 52.55484 ?  357 ASN   A OD1  1 
ATOM   1497 N  ND2  . ASN   A 1 205 ? 37.07200 -9.22100  10.16200 1.000 49.01093 ?  357 ASN   A ND2  1 
ATOM   1498 N  N    . THR   A 1 206 ? 34.45800 -5.20200  8.18700  1.000 32.70401 ?  358 THR   A N    1 
ATOM   1499 C  CA   . THR   A 1 206 ? 34.28900 -3.86300  7.63200  1.000 33.12668 ?  358 THR   A CA   1 
ATOM   1500 C  C    . THR   A 1 206 ? 34.50600 -2.79700  8.69800  1.000 38.21572 ?  358 THR   A C    1 
ATOM   1501 O  O    . THR   A 1 206 ? 35.15200 -1.77300  8.44300  1.000 33.71088 ?  358 THR   A O    1 
ATOM   1502 C  CB   . THR   A 1 206 ? 32.89500 -3.72400  7.01900  1.000 31.30321 ?  358 THR   A CB   1 
ATOM   1503 O  OG1  . THR   A 1 206 ? 32.74400 -4.67600  5.95800  1.000 32.20501 ?  358 THR   A OG1  1 
ATOM   1504 C  CG2  . THR   A 1 206 ? 32.68000 -2.32200  6.47000  1.000 31.87350 ?  358 THR   A CG2  1 
ATOM   1505 N  N    . LEU   A 1 207 ? 33.97100 -3.02100  9.90200  1.000 27.01402 ?  359 LEU   A N    1 
ATOM   1506 C  CA   . LEU   A 1 207 ? 34.14000 -2.05600  10.98400 1.000 26.10603 ?  359 LEU   A CA   1 
ATOM   1507 C  C    . LEU   A 1 207 ? 35.59400 -1.97700  11.42900 1.000 29.08738 ?  359 LEU   A C    1 
ATOM   1508 O  O    . LEU   A 1 207 ? 36.15100 -0.88200  11.57000 1.000 29.18805 ?  359 LEU   A O    1 
ATOM   1509 C  CB   . LEU   A 1 207 ? 33.23700 -2.42400  12.16200 1.000 27.29795 ?  359 LEU   A CB   1 
ATOM   1510 C  CG   . LEU   A 1 207 ? 33.43900 -1.61000  13.44200 1.000 30.39360 ?  359 LEU   A CG   1 
ATOM   1511 C  CD1  . LEU   A 1 207 ? 33.30100 -0.11700  13.16300 1.000 27.10552 ?  359 LEU   A CD1  1 
ATOM   1512 C  CD2  . LEU   A 1 207 ? 32.46800 -2.05500  14.52400 1.000 26.74847 ?  359 LEU   A CD2  1 
ATOM   1513 N  N    . GLN   A 1 208 ? 36.22500 -3.13100  11.66400 1.000 27.82876 ?  360 GLN   A N    1 
ATOM   1514 C  CA   . GLN   A 1 208 ? 37.61800 -3.14500  12.10800 1.000 28.83632 ?  360 GLN   A CA   1 
ATOM   1515 C  C    . GLN   A 1 208 ? 38.51900 -2.43000  11.10900 1.000 30.78231 ?  360 GLN   A C    1 
ATOM   1516 O  O    . GLN   A 1 208 ? 39.39200 -1.64300  11.49400 1.000 33.75951 ?  360 GLN   A O    1 
ATOM   1517 C  CB   . GLN   A 1 208 ? 38.08700 -4.58600  12.31800 1.000 35.80706 ?  360 GLN   A CB   1 
ATOM   1518 C  CG   . GLN   A 1 208 ? 37.32200 -5.33800  13.39000 1.000 36.86584 ?  360 GLN   A CG   1 
ATOM   1519 C  CD   . GLN   A 1 208 ? 37.76600 -6.78100  13.52100 1.000 51.77660 ?  360 GLN   A CD   1 
ATOM   1520 O  OE1  . GLN   A 1 208 ? 36.95800 -7.70400  13.41700 1.000 59.09818 ?  360 GLN   A OE1  1 
ATOM   1521 N  NE2  . GLN   A 1 208 ? 39.05700 -6.98300  13.74900 1.000 52.70237 ?  360 GLN   A NE2  1 
ATOM   1522 N  N    . THR   A 1 209 ? 38.31700 -2.68700  9.81600  1.000 34.02931 ?  361 THR   A N    1 
ATOM   1523 C  CA   . THR   A 1 209 ? 39.14600 -2.04200  8.80300  1.000 34.28601 ?  361 THR   A CA   1 
ATOM   1524 C  C    . THR   A 1 209 ? 38.81100 -0.55800  8.66600  1.000 32.43238 ?  361 THR   A C    1 
ATOM   1525 O  O    . THR   A 1 209 ? 39.70200 0.26100   8.40300  1.000 34.38147 ?  361 THR   A O    1 
ATOM   1526 C  CB   . THR   A 1 209 ? 38.99000 -2.76000  7.46000  1.000 38.10659 ?  361 THR   A CB   1 
ATOM   1527 O  OG1  . THR   A 1 209 ? 39.33800 -4.14400  7.61200  1.000 39.18690 ?  361 THR   A OG1  1 
ATOM   1528 C  CG2  . THR   A 1 209 ? 39.89800 -2.13300  6.40800  1.000 39.10822 ?  361 THR   A CG2  1 
ATOM   1529 N  N    . TYR   A 1 210 ? 37.53500 -0.18800  8.82500  1.000 29.82912 ?  362 TYR   A N    1 
ATOM   1530 C  CA   . TYR   A 1 210 ? 37.18500 1.23000   8.77700  1.000 29.78712 ?  362 TYR   A CA   1 
ATOM   1531 C  C    . TYR   A 1 210 ? 37.92600 2.00700   9.85400  1.000 29.13184 ?  362 TYR   A C    1 
ATOM   1532 O  O    . TYR   A 1 210 ? 38.47900 3.08200   9.59200  1.000 34.61517 ?  362 TYR   A O    1 
ATOM   1533 C  CB   . TYR   A 1 210 ? 35.67500 1.43400   8.93300  1.000 30.28621 ?  362 TYR   A CB   1 
ATOM   1534 C  CG   . TYR   A 1 210 ? 35.30700 2.90600   8.94300  1.000 27.55131 ?  362 TYR   A CG   1 
ATOM   1535 C  CD1  . TYR   A 1 210 ? 35.27300 3.63100   10.13200 1.000 26.98837 ?  362 TYR   A CD1  1 
ATOM   1536 C  CD2  . TYR   A 1 210 ? 35.03500 3.57800   7.76000  1.000 28.27764 ?  362 TYR   A CD2  1 
ATOM   1537 C  CE1  . TYR   A 1 210 ? 34.96600 4.97700   10.13900 1.000 27.90120 ?  362 TYR   A CE1  1 
ATOM   1538 C  CE2  . TYR   A 1 210 ? 34.72300 4.92200   7.75900  1.000 29.79373 ?  362 TYR   A CE2  1 
ATOM   1539 C  CZ   . TYR   A 1 210 ? 34.69000 5.61800   8.94900  1.000 33.09386 ?  362 TYR   A CZ   1 
ATOM   1540 O  OH   . TYR   A 1 210 ? 34.37700 6.95700   8.94600  1.000 33.16870 ?  362 TYR   A OH   1 
ATOM   1541 N  N    . ILE   A 1 211 ? 37.93200 1.48100   11.08000 1.000 28.41211 ?  363 ILE   A N    1 
ATOM   1542 C  CA   . ILE   A 1 211 ? 38.59800 2.16800   12.18000 1.000 28.35803 ?  363 ILE   A CA   1 
ATOM   1543 C  C    . ILE   A 1 211 ? 40.08700 2.30700   11.88500 1.000 29.90976 ?  363 ILE   A C    1 
ATOM   1544 O  O    . ILE   A 1 211 ? 40.68100 3.37300   12.07900 1.000 32.73370 ?  363 ILE   A O    1 
ATOM   1545 C  CB   . ILE   A 1 211 ? 38.35100 1.42800   13.50700 1.000 27.58605 ?  363 ILE   A CB   1 
ATOM   1546 C  CG1  . ILE   A 1 211 ? 36.86700 1.47200   13.87900 1.000 26.12781 ?  363 ILE   A CG1  1 
ATOM   1547 C  CG2  . ILE   A 1 211 ? 39.18700 2.04000   14.62100 1.000 32.34884 ?  363 ILE   A CG2  1 
ATOM   1548 C  CD1  . ILE   A 1 211 ? 36.49200 0.52600   15.00000 1.000 30.38333 ?  363 ILE   A CD1  1 
ATOM   1549 N  N    . ARG   A 1 212 ? 40.70400 1.23200   11.38400 1.000 34.15804 ?  364 ARG   A N    1 
ATOM   1550 C  CA   . ARG   A 1 212 ? 42.13800 1.25200   11.10600 1.000 37.55161 ?  364 ARG   A CA   1 
ATOM   1551 C  C    . ARG   A 1 212 ? 42.49700 2.30800   10.06800 1.000 35.74891 ?  364 ARG   A C    1 
ATOM   1552 O  O    . ARG   A 1 212 ? 43.53100 2.97800   10.18700 1.000 38.49018 ?  364 ARG   A O    1 
ATOM   1553 C  CB   . ARG   A 1 212 ? 42.59300 -0.13300  10.64200 1.000 33.61618 ?  364 ARG   A CB   1 
ATOM   1554 C  CG   . ARG   A 1 212 ? 44.04300 -0.21100  10.19000 1.000 40.59265 ?  364 ARG   A CG   1 
ATOM   1555 C  CD   . ARG   A 1 212 ? 45.01700 0.06300   11.32700 1.000 39.56740 ?  364 ARG   A CD   1 
ATOM   1556 N  NE   . ARG   A 1 212 ? 46.40300 0.00900   10.87100 1.000 49.20911 ?  364 ARG   A NE   1 
ATOM   1557 C  CZ   . ARG   A 1 212 ? 47.05500 1.03800   10.33900 1.000 50.68457 ?  364 ARG   A CZ   1 
ATOM   1558 N  NH1  . ARG   A 1 212 ? 46.44900 2.20800   10.19600 1.000 54.81873 ?  364 ARG   A NH1  1 
ATOM   1559 N  NH2  . ARG   A 1 212 ? 48.31700 0.89900   9.94900  1.000 56.38007 ?  364 ARG   A NH2  1 
ATOM   1560 N  N    . CYS   A 1 213 ? 41.65400 2.48400   9.04800  1.000 35.48622 ?  365 CYS   A N    1 
ATOM   1561 C  CA   . CYS   A 1 213 ? 42.01100 3.32000   7.91100  1.000 39.04332 ?  365 CYS   A CA   1 
ATOM   1562 C  C    . CYS   A 1 213 ? 41.37000 4.70000   7.92200  1.000 36.51121 ?  365 CYS   A C    1 
ATOM   1563 O  O    . CYS   A 1 213 ? 41.88300 5.60400   7.25300  1.000 40.01358 ?  365 CYS   A O    1 
ATOM   1564 C  CB   . CYS   A 1 213 ? 41.61600 2.62400   6.60200  1.000 43.77223 ?  365 CYS   A CB   1 
ATOM   1565 S  SG   . CYS   A 1 213 ? 42.38500 1.01700   6.33100  1.000 48.21359 ?  365 CYS   A SG   1 
ATOM   1566 N  N    A ARG   A 1 214 ? 40.27200 4.88700   8.65400  0.580 33.55077 ?  366 ARG   A N    1 
ATOM   1567 N  N    B ARG   A 1 214 ? 40.27400 4.88900   8.65800  0.420 33.72781 ?  366 ARG   A N    1 
ATOM   1568 C  CA   A ARG   A 1 214 ? 39.53300 6.14300   8.60400  0.580 34.54948 ?  366 ARG   A CA   1 
ATOM   1569 C  CA   B ARG   A 1 214 ? 39.53800 6.14500   8.60000  0.420 34.54034 ?  366 ARG   A CA   1 
ATOM   1570 C  C    A ARG   A 1 214 ? 39.39400 6.85300   9.94000  0.580 35.89316 ?  366 ARG   A C    1 
ATOM   1571 C  C    B ARG   A 1 214 ? 39.36300 6.84600   9.94000  0.420 35.59699 ?  366 ARG   A C    1 
ATOM   1572 O  O    A ARG   A 1 214 ? 39.07000 8.04800   9.94100  0.580 37.14980 ?  366 ARG   A O    1 
ATOM   1573 O  O    B ARG   A 1 214 ? 38.98600 8.02400   9.94400  0.420 36.26227 ?  366 ARG   A O    1 
ATOM   1574 C  CB   A ARG   A 1 214 ? 38.12800 5.91700   8.02500  0.580 32.89548 ?  366 ARG   A CB   1 
ATOM   1575 C  CB   B ARG   A 1 214 ? 38.15000 5.92600   7.97500  0.420 33.46087 ?  366 ARG   A CB   1 
ATOM   1576 C  CG   A ARG   A 1 214 ? 38.13100 5.34700   6.61900  0.580 37.11128 ?  366 ARG   A CG   1 
ATOM   1577 C  CG   B ARG   A 1 214 ? 38.19100 5.29800   6.58900  0.420 37.21575 ?  366 ARG   A CG   1 
ATOM   1578 C  CD   A ARG   A 1 214 ? 38.40100 6.43100   5.58900  0.580 44.77844 ?  366 ARG   A CD   1 
ATOM   1579 C  CD   B ARG   A 1 214 ? 38.49400 6.33600   5.51800  0.420 44.59284 ?  366 ARG   A CD   1 
ATOM   1580 N  NE   A ARG   A 1 214 ? 38.60200 5.86200   4.26100  0.580 49.49077 ?  366 ARG   A NE   1 
ATOM   1581 N  NE   B ARG   A 1 214 ? 38.09500 5.88000   4.19000  0.420 49.75783 ?  366 ARG   A NE   1 
ATOM   1582 C  CZ   A ARG   A 1 214 ? 37.61600 5.59100   3.41200  0.580 52.16577 ?  366 ARG   A CZ   1 
ATOM   1583 C  CZ   B ARG   A 1 214 ? 38.88800 5.21200   3.35800  0.420 54.11047 ?  366 ARG   A CZ   1 
ATOM   1584 N  NH1  A ARG   A 1 214 ? 36.35900 5.84000   3.75200  0.580 50.96793 ?  366 ARG   A NH1  1 
ATOM   1585 N  NH1  B ARG   A 1 214 ? 40.13200 4.92100   3.71200  0.420 49.16033 ?  366 ARG   A NH1  1 
ATOM   1586 N  NH2  A ARG   A 1 214 ? 37.88600 5.06900   2.22400  0.580 57.07121 ?  366 ARG   A NH2  1 
ATOM   1587 N  NH2  B ARG   A 1 214 ? 38.43600 4.83400   2.17000  0.420 57.08709 ?  366 ARG   A NH2  1 
ATOM   1588 N  N    . HIS   A 1 215 ? 39.62000 6.18400   11.06900 1.000 31.57823 ?  367 HIS   A N    1 
ATOM   1589 C  CA   . HIS   A 1 215 ? 39.47200 6.84100   12.35900 1.000 29.56670 ?  367 HIS   A CA   1 
ATOM   1590 C  C    . HIS   A 1 215 ? 40.84100 7.23800   12.88300 1.000 32.62233 ?  367 HIS   A C    1 
ATOM   1591 O  O    . HIS   A 1 215 ? 41.64200 6.35400   13.22700 1.000 36.25026 ?  367 HIS   A O    1 
ATOM   1592 C  CB   . HIS   A 1 215 ? 38.75500 5.94800   13.36800 1.000 29.23045 ?  367 HIS   A CB   1 
ATOM   1593 C  CG   . HIS   A 1 215 ? 38.06800 6.71100   14.46200 1.000 32.29568 ?  367 HIS   A CG   1 
ATOM   1594 N  ND1  . HIS   A 1 215 ? 36.72100 6.58200   14.72800 1.000 28.33105 ?  367 HIS   A ND1  1 
ATOM   1595 C  CD2  . HIS   A 1 215 ? 38.53800 7.62900   15.34100 1.000 31.71252 ?  367 HIS   A CD2  1 
ATOM   1596 C  CE1  . HIS   A 1 215 ? 36.39300 7.37800   15.73000 1.000 25.86539 ?  367 HIS   A CE1  1 
ATOM   1597 N  NE2  . HIS   A 1 215 ? 37.47800 8.02400   16.12100 1.000 28.27798 ?  367 HIS   A NE2  1 
ATOM   1598 N  N    . PRO   A 1 216 ? 41.14900 8.52700   12.97600 1.000 36.48605 ?  368 PRO   A N    1 
ATOM   1599 C  CA   . PRO   A 1 216 ? 42.48600 8.94400   13.38800 1.000 38.20058 ?  368 PRO   A CA   1 
ATOM   1600 C  C    . PRO   A 1 216 ? 42.68600 8.75200   14.87900 1.000 33.23862 ?  368 PRO   A C    1 
ATOM   1601 O  O    . PRO   A 1 216 ? 41.73700 8.87200   15.66900 1.000 34.00543 ?  368 PRO   A O    1 
ATOM   1602 C  CB   . PRO   A 1 216 ? 42.51700 10.43300  13.01300 1.000 45.61616 ?  368 PRO   A CB   1 
ATOM   1603 C  CG   . PRO   A 1 216 ? 41.09600 10.86500  13.13500 1.000 42.11826 ?  368 PRO   A CG   1 
ATOM   1604 C  CD   . PRO   A 1 216 ? 40.27000 9.67700   12.70000 1.000 35.75396 ?  368 PRO   A CD   1 
ATOM   1605 N  N    . PRO   A 1 217 ? 43.90700 8.45200   15.30300 1.000 34.03740 ?  369 PRO   A N    1 
ATOM   1606 C  CA   . PRO   A 1 217 ? 44.22300 8.48100   16.72700 1.000 33.37291 ?  369 PRO   A CA   1 
ATOM   1607 C  C    . PRO   A 1 217 ? 44.13800 9.90200   17.25000 1.000 37.34101 ?  369 PRO   A C    1 
ATOM   1608 O  O    . PRO   A 1 217 ? 44.29000 10.86200  16.47700 1.000 34.67822 ?  369 PRO   A O    1 
ATOM   1609 C  CB   . PRO   A 1 217 ? 45.66400 7.94700   16.77700 1.000 34.80437 ?  369 PRO   A CB   1 
ATOM   1610 C  CG   . PRO   A 1 217 ? 46.22400 8.27900   15.43000 1.000 36.36887 ?  369 PRO   A CG   1 
ATOM   1611 C  CD   . PRO   A 1 217 ? 45.07900 8.11000   14.47800 1.000 34.80234 ?  369 PRO   A CD   1 
ATOM   1612 N  N    . PRO   A 1 218 ? 43.90800 10.09000  18.56000 1.000 34.86768 ?  370 PRO   A N    1 
ATOM   1613 C  CA   . PRO   A 1 218 ? 43.79500 9.06200   19.60400 1.000 34.70291 ?  370 PRO   A CA   1 
ATOM   1614 C  C    . PRO   A 1 218 ? 42.42300 8.38700   19.70000 1.000 33.69614 ?  370 PRO   A C    1 
ATOM   1615 O  O    . PRO   A 1 218 ? 42.30500 7.38100   20.39900 1.000 37.38452 ?  370 PRO   A O    1 
ATOM   1616 C  CB   . PRO   A 1 218 ? 44.08600 9.84700   20.88400 1.000 40.55693 ?  370 PRO   A CB   1 
ATOM   1617 C  CG   . PRO   A 1 218 ? 43.59500 11.22200  20.58500 1.000 40.86085 ?  370 PRO   A CG   1 
ATOM   1618 C  CD   . PRO   A 1 218 ? 43.87300 11.45100  19.12400 1.000 36.67448 ?  370 PRO   A CD   1 
ATOM   1619 N  N    . GLY   A 1 219 ? 41.41200 8.92700   19.01500 1.000 32.22189 ?  371 GLY   A N    1 
ATOM   1620 C  CA   . GLY   A 1 219 ? 40.06800 8.37400   19.10300 1.000 33.38689 ?  371 GLY   A CA   1 
ATOM   1621 C  C    . GLY   A 1 219 ? 39.96500 6.91400   18.71200 1.000 31.66305 ?  371 GLY   A C    1 
ATOM   1622 O  O    . GLY   A 1 219 ? 39.08400 6.20700   19.21200 1.000 32.08820 ?  371 GLY   A O    1 
ATOM   1623 N  N    . SER   A 1 220 ? 40.85300 6.44200   17.83500 1.000 35.65700 ?  372 SER   A N    1 
ATOM   1624 C  CA   . SER   A 1 220 ? 40.81200 5.06500   17.35700 1.000 34.09413 ?  372 SER   A CA   1 
ATOM   1625 C  C    . SER   A 1 220 ? 41.32700 4.05700   18.37400 1.000 35.55061 ?  372 SER   A C    1 
ATOM   1626 O  O    . SER   A 1 220 ? 41.14700 2.85200   18.16100 1.000 34.35564 ?  372 SER   A O    1 
ATOM   1627 C  CB   . SER   A 1 220 ? 41.62800 4.93700   16.07000 1.000 30.72275 ?  372 SER   A CB   1 
ATOM   1628 O  OG   . SER   A 1 220 ? 42.97300 5.33800   16.27500 1.000 33.63688 ?  372 SER   A OG   1 
ATOM   1629 N  N    . HIS   A 1 221 ? 41.95900 4.51100   19.45700 1.000 36.56099 ?  373 HIS   A N    1 
ATOM   1630 C  CA   . HIS   A 1 221 ? 42.64300 3.61300   20.38000 1.000 37.40271 ?  373 HIS   A CA   1 
ATOM   1631 C  C    . HIS   A 1 221 ? 41.68700 2.58200   20.96300 1.000 34.51160 ?  373 HIS   A C    1 
ATOM   1632 O  O    . HIS   A 1 221 ? 40.75400 2.93500   21.69300 1.000 33.96775 ?  373 HIS   A O    1 
ATOM   1633 C  CB   . HIS   A 1 221 ? 43.30300 4.40400   21.50800 1.000 37.58568 ?  373 HIS   A CB   1 
ATOM   1634 C  CG   . HIS   A 1 221 ? 43.92300 3.53700   22.55700 1.000 38.87923 ?  373 HIS   A CG   1 
ATOM   1635 N  ND1  . HIS   A 1 221 ? 44.91500 2.62400   22.27400 1.000 39.80432 ?  373 HIS   A ND1  1 
ATOM   1636 C  CD2  . HIS   A 1 221 ? 43.67000 3.41900   23.88200 1.000 37.46229 ?  373 HIS   A CD2  1 
ATOM   1637 C  CE1  . HIS   A 1 221 ? 45.25900 1.99200   23.38200 1.000 40.07211 ?  373 HIS   A CE1  1 
ATOM   1638 N  NE2  . HIS   A 1 221 ? 44.51800 2.45600   24.37200 1.000 41.39674 ?  373 HIS   A NE2  1 
ATOM   1639 N  N    A GLN   A 1 222 ? 41.91700 1.30500   20.64600 0.610 32.60603 ?  374 GLN   A N    1 
ATOM   1640 N  N    B GLN   A 1 222 ? 41.93000 1.30800   20.63700 0.390 32.61891 ?  374 GLN   A N    1 
ATOM   1641 C  CA   A GLN   A 1 222 ? 41.10200 0.20000   21.15100 0.610 30.19588 ?  374 GLN   A CA   1 
ATOM   1642 C  CA   B GLN   A 1 222 ? 41.11700 0.18800   21.11600 0.390 31.02810 ?  374 GLN   A CA   1 
ATOM   1643 C  C    A GLN   A 1 222 ? 39.61900 0.41400   20.86200 0.610 29.70747 ?  374 GLN   A C    1 
ATOM   1644 C  C    B GLN   A 1 222 ? 39.63000 0.43100   20.87200 0.390 29.72595 ?  374 GLN   A C    1 
ATOM   1645 O  O    A GLN   A 1 222 ? 38.75400 -0.08300  21.59000 0.610 29.64042 ?  374 GLN   A O    1 
ATOM   1646 O  O    B GLN   A 1 222 ? 38.77500 -0.03200  21.63200 0.390 29.65764 ?  374 GLN   A O    1 
ATOM   1647 C  CB   A GLN   A 1 222 ? 41.32400 -0.01300  22.65100 0.610 35.35145 ?  374 GLN   A CB   1 
ATOM   1648 C  CB   B GLN   A 1 222 ? 41.38800 -0.09700  22.59700 0.390 35.70167 ?  374 GLN   A CB   1 
ATOM   1649 C  CG   A GLN   A 1 222 ? 42.69700 -0.55400  23.00300 0.610 39.09956 ?  374 GLN   A CG   1 
ATOM   1650 C  CG   B GLN   A 1 222 ? 42.55100 -1.05500  22.83700 0.390 41.63724 ?  374 GLN   A CG   1 
ATOM   1651 C  CD   A GLN   A 1 222 ? 42.96400 -1.90600  22.37800 0.610 42.95858 ?  374 GLN   A CD   1 
ATOM   1652 C  CD   B GLN   A 1 222 ? 43.16500 -0.91200  24.21700 0.390 42.59290 ?  374 GLN   A CD   1 
ATOM   1653 O  OE1  A GLN   A 1 222 ? 42.10100 -2.78500  22.38200 0.610 44.14534 ?  374 GLN   A OE1  1 
ATOM   1654 O  OE1  B GLN   A 1 222 ? 42.50800 -0.47200  25.16100 0.390 38.44887 ?  374 GLN   A OE1  1 
ATOM   1655 N  NE2  A GLN   A 1 222 ? 44.16300 -2.08100  21.83000 0.610 49.82918 ?  374 GLN   A NE2  1 
ATOM   1656 N  NE2  B GLN   A 1 222 ? 44.43500 -1.28600  24.34100 0.390 48.68280 ?  374 GLN   A NE2  1 
ATOM   1657 N  N    . LEU   A 1 223 ? 39.31500 1.15400   19.79300 1.000 27.27826 ?  375 LEU   A N    1 
ATOM   1658 C  CA   . LEU   A 1 223 ? 37.93400 1.54900   19.53600 1.000 25.96454 ?  375 LEU   A CA   1 
ATOM   1659 C  C    . LEU   A 1 223 ? 37.04900 0.35300   19.21200 1.000 32.89615 ?  375 LEU   A C    1 
ATOM   1660 O  O    . LEU   A 1 223 ? 35.90300 0.28800   19.67100 1.000 24.40881 ?  375 LEU   A O    1 
ATOM   1661 C  CB   . LEU   A 1 223 ? 37.88100 2.56700   18.39800 1.000 26.07691 ?  375 LEU   A CB   1 
ATOM   1662 C  CG   . LEU   A 1 223 ? 36.47500 3.07600   18.06500 1.000 27.43655 ?  375 LEU   A CG   1 
ATOM   1663 C  CD1  . LEU   A 1 223 ? 35.75100 3.53100   19.32600 1.000 30.40653 ?  375 LEU   A CD1  1 
ATOM   1664 C  CD2  . LEU   A 1 223 ? 36.52700 4.19600   17.04200 1.000 30.66333 ?  375 LEU   A CD2  1 
ATOM   1665 N  N    . TYR   A 1 224 ? 37.54200 -0.58800  18.40200 1.000 30.92010 ?  376 TYR   A N    1 
ATOM   1666 C  CA   . TYR   A 1 224 ? 36.73800 -1.76700  18.09400 1.000 32.26547 ?  376 TYR   A CA   1 
ATOM   1667 C  C    . TYR   A 1 224 ? 36.41100 -2.54300  19.36200 1.000 32.35150 ?  376 TYR   A C    1 
ATOM   1668 O  O    . TYR   A 1 224 ? 35.26700 -2.96200  19.57000 1.000 31.66185 ?  376 TYR   A O    1 
ATOM   1669 C  CB   . TYR   A 1 224 ? 37.45700 -2.66900  17.09000 1.000 34.95616 ?  376 TYR   A CB   1 
ATOM   1670 C  CG   . TYR   A 1 224 ? 36.65700 -3.91100  16.76400 1.000 29.93579 ?  376 TYR   A CG   1 
ATOM   1671 C  CD1  . TYR   A 1 224 ? 35.49900 -3.82700  16.00300 1.000 32.75352 ?  376 TYR   A CD1  1 
ATOM   1672 C  CD2  . TYR   A 1 224 ? 37.04600 -5.16000  17.23100 1.000 35.47434 ?  376 TYR   A CD2  1 
ATOM   1673 C  CE1  . TYR   A 1 224 ? 34.75700 -4.95100  15.70700 1.000 35.71541 ?  376 TYR   A CE1  1 
ATOM   1674 C  CE2  . TYR   A 1 224 ? 36.30900 -6.29300  16.93800 1.000 37.64487 ?  376 TYR   A CE2  1 
ATOM   1675 C  CZ   . TYR   A 1 224 ? 35.16500 -6.18100  16.17500 1.000 37.08600 ?  376 TYR   A CZ   1 
ATOM   1676 O  OH   . TYR   A 1 224 ? 34.42700 -7.30500  15.88200 1.000 41.67255 ?  376 TYR   A OH   1 
ATOM   1677 N  N    . ALA   A 1 225 ? 37.41100 -2.73700  20.22600 1.000 30.56636 ?  377 ALA   A N    1 
ATOM   1678 C  CA   . ALA   A 1 225 ? 37.18300 -3.44900  21.47800 1.000 29.99027 ?  377 ALA   A CA   1 
ATOM   1679 C  C    . ALA   A 1 225 ? 36.18500 -2.70900  22.36100 1.000 29.75553 ?  377 ALA   A C    1 
ATOM   1680 O  O    . ALA   A 1 225 ? 35.34000 -3.33500  23.01300 1.000 31.82211 ?  377 ALA   A O    1 
ATOM   1681 C  CB   . ALA   A 1 225 ? 38.50800 -3.65300  22.21200 1.000 32.33274 ?  377 ALA   A CB   1 
ATOM   1682 N  N    . LYS   A 1 226 ? 36.26300 -1.37500  22.39400 1.000 26.78627 ?  378 LYS   A N    1 
ATOM   1683 C  CA   . LYS   A 1 226 ? 35.29800 -0.59900  23.16700 1.000 25.16912 ?  378 LYS   A CA   1 
ATOM   1684 C  C    . LYS   A 1 226 ? 33.89700 -0.72100  22.59000 1.000 27.49151 ?  378 LYS   A C    1 
ATOM   1685 O  O    . LYS   A 1 226 ? 32.91400 -0.73100  23.34200 1.000 25.36085 ?  378 LYS   A O    1 
ATOM   1686 C  CB   . LYS   A 1 226 ? 35.71300 0.87300   23.21500 1.000 24.65987 ?  378 LYS   A CB   1 
ATOM   1687 C  CG   . LYS   A 1 226 ? 36.98500 1.14700   23.99400 1.000 28.64879 ?  378 LYS   A CG   1 
ATOM   1688 C  CD   . LYS   A 1 226 ? 37.37000 2.61100   23.87600 1.000 31.79010 ?  378 LYS   A CD   1 
ATOM   1689 C  CE   . LYS   A 1 226 ? 38.71600 2.88300   24.51300 1.000 38.43313 ?  378 LYS   A CE   1 
ATOM   1690 N  NZ   . LYS   A 1 226 ? 39.18600 4.26500   24.22900 1.000 41.81475 ?  378 LYS   A NZ   1 
ATOM   1691 N  N    . MET   A 1 227 ? 33.78300 -0.82300  21.26600 1.000 24.27097 ?  379 MET   A N    1 
ATOM   1692 C  CA   . MET   A 1 227 ? 32.46400 -0.95600  20.65900 1.000 24.39196 ?  379 MET   A CA   1 
ATOM   1693 C  C    . MET   A 1 227 ? 31.86800 -2.33000  20.93300 1.000 26.26134 ?  379 MET   A C    1 
ATOM   1694 O  O    . MET   A 1 227 ? 30.65900 -2.45500  21.15800 1.000 23.49888 ?  379 MET   A O    1 
ATOM   1695 C  CB   . MET   A 1 227 ? 32.54400 -0.70300  19.15400 1.000 25.51823 ?  379 MET   A CB   1 
ATOM   1696 C  CG   . MET   A 1 227 ? 32.68000 0.75900   18.77600 1.000 24.06640 ?  379 MET   A CG   1 
ATOM   1697 S  SD   . MET   A 1 227 ? 33.10400 1.00300   17.04200 1.000 25.03714 ?  379 MET   A SD   1 
ATOM   1698 C  CE   . MET   A 1 227 ? 31.45800 1.01000   16.34300 1.000 23.74790 ?  379 MET   A CE   1 
ATOM   1699 N  N    . ILE   A 1 228 ? 32.69800 -3.37600  20.90500 1.000 29.29775 ?  380 ILE   A N    1 
ATOM   1700 C  CA   . ILE   A 1 228 ? 32.20900 -4.70800  21.24100 1.000 33.64117 ?  380 ILE   A CA   1 
ATOM   1701 C  C    . ILE   A 1 228 ? 31.85600 -4.78800  22.72100 1.000 31.18186 ?  380 ILE   A C    1 
ATOM   1702 O  O    . ILE   A 1 228 ? 30.94800 -5.53300  23.11000 1.000 29.14075 ?  380 ILE   A O    1 
ATOM   1703 C  CB   . ILE   A 1 228 ? 33.24300 -5.77500  20.83500 1.000 40.01689 ?  380 ILE   A CB   1 
ATOM   1704 C  CG1  . ILE   A 1 228 ? 33.51400 -5.70900  19.33200 1.000 31.80600 ?  380 ILE   A CG1  1 
ATOM   1705 C  CG2  . ILE   A 1 228 ? 32.76100 -7.16900  21.21400 1.000 45.74961 ?  380 ILE   A CG2  1 
ATOM   1706 C  CD1  . ILE   A 1 228 ? 32.26200 -5.60800  18.48400 1.000 39.99170 ?  380 ILE   A CD1  1 
ATOM   1707 N  N    . GLN   A 1 229 ? 32.55300 -4.02600  23.57000 1.000 26.40144 ?  381 GLN   A N    1 
ATOM   1708 C  CA   . GLN   A 1 229 ? 32.15600 -3.94200  24.97100 1.000 28.57628 ?  381 GLN   A CA   1 
ATOM   1709 C  C    . GLN   A 1 229 ? 30.75700 -3.35600  25.11200 1.000 27.95564 ?  381 GLN   A C    1 
ATOM   1710 O  O    . GLN   A 1 229 ? 29.97300 -3.79300  25.96300 1.000 27.42844 ?  381 GLN   A O    1 
ATOM   1711 C  CB   . GLN   A 1 229 ? 33.16800 -3.11000  25.75900 1.000 32.26618 ?  381 GLN   A CB   1 
ATOM   1712 C  CG   . GLN   A 1 229 ? 32.82400 -2.96300  27.23500 1.000 36.74597 ?  381 GLN   A CG   1 
ATOM   1713 C  CD   . GLN   A 1 229 ? 32.65200 -4.30100  27.93200 1.000 45.25582 ?  381 GLN   A CD   1 
ATOM   1714 O  OE1  . GLN   A 1 229 ? 33.51400 -5.17600  27.84300 1.000 45.51094 ?  381 GLN   A OE1  1 
ATOM   1715 N  NE2  . GLN   A 1 229 ? 31.52800 -4.47000  28.62300 1.000 43.30912 ?  381 GLN   A NE2  1 
ATOM   1716 N  N    . LYS   A 1 230 ? 30.42300 -2.36500  24.28200 1.000 24.59273 ?  382 LYS   A N    1 
ATOM   1717 C  CA   . LYS   A 1 230 ? 29.08000 -1.79800  24.32100 1.000 23.69091 ?  382 LYS   A CA   1 
ATOM   1718 C  C    . LYS   A 1 230 ? 28.03000 -2.80900  23.88100 1.000 26.79157 ?  382 LYS   A C    1 
ATOM   1719 O  O    . LYS   A 1 230 ? 26.89000 -2.76200  24.35500 1.000 23.57902 ?  382 LYS   A O    1 
ATOM   1720 C  CB   . LYS   A 1 230 ? 29.01700 -0.54200  23.45400 1.000 27.31264 ?  382 LYS   A CB   1 
ATOM   1721 C  CG   . LYS   A 1 230 ? 29.77900 0.64000   24.03200 1.000 26.74143 ?  382 LYS   A CG   1 
ATOM   1722 C  CD   . LYS   A 1 230 ? 29.13200 1.14400   25.31800 1.000 33.71457 ?  382 LYS   A CD   1 
ATOM   1723 C  CE   . LYS   A 1 230 ? 30.11300 1.95900   26.15000 1.000 43.55438 ?  382 LYS   A CE   1 
ATOM   1724 N  NZ   . LYS   A 1 230 ? 30.74000 1.14400   27.22500 1.000 46.54255 ?  382 LYS   A NZ   1 
ATOM   1725 N  N    . LEU   A 1 231 ? 28.39000 -3.73000  22.98400 1.000 20.95000 ?  383 LEU   A N    1 
ATOM   1726 C  CA   . LEU   A 1 231 ? 27.46900 -4.80800  22.63800 1.000 24.78303 ?  383 LEU   A CA   1 
ATOM   1727 C  C    . LEU   A 1 231 ? 27.24600 -5.73700  23.82400 1.000 25.83848 ?  383 LEU   A C    1 
ATOM   1728 O  O    . LEU   A 1 231 ? 26.14000 -6.26000  24.01100 1.000 24.89778 ?  383 LEU   A O    1 
ATOM   1729 C  CB   . LEU   A 1 231 ? 27.99600 -5.59400  21.43700 1.000 25.73268 ?  383 LEU   A CB   1 
ATOM   1730 C  CG   . LEU   A 1 231 ? 28.03100 -4.87000  20.09200 1.000 23.64564 ?  383 LEU   A CG   1 
ATOM   1731 C  CD1  . LEU   A 1 231 ? 28.63200 -5.75300  19.00600 1.000 26.97914 ?  383 LEU   A CD1  1 
ATOM   1732 C  CD2  . LEU   A 1 231 ? 26.64000 -4.40200  19.69700 1.000 22.26597 ?  383 LEU   A CD2  1 
ATOM   1733 N  N    . ALA   A 1 232 ? 28.28900 -5.95900  24.63100 1.000 22.48111 ?  384 ALA   A N    1 
ATOM   1734 C  CA   . ALA   A 1 232 ? 28.12500 -6.74600  25.84700 1.000 25.96793 ?  384 ALA   A CA   1 
ATOM   1735 C  C    . ALA   A 1 232 ? 27.26600 -6.00700  26.86500 1.000 26.13404 ?  384 ALA   A C    1 
ATOM   1736 O  O    . ALA   A 1 232 ? 26.39700 -6.60900  27.50700 1.000 27.27053 ?  384 ALA   A O    1 
ATOM   1737 C  CB   . ALA   A 1 232 ? 29.48900 -7.08800  26.44300 1.000 25.62281 ?  384 ALA   A CB   1 
ATOM   1738 N  N    . ASP   A 1 233 ? 27.50300 -4.70300  27.03400 1.000 24.48554 ?  385 ASP   A N    1 
ATOM   1739 C  CA   . ASP   A 1 233 ? 26.62600 -3.89300  27.87400 1.000 25.71758 ?  385 ASP   A CA   1 
ATOM   1740 C  C    . ASP   A 1 233 ? 25.17400 -4.03200  27.43800 1.000 24.24254 ?  385 ASP   A C    1 
ATOM   1741 O  O    . ASP   A 1 233 ? 24.26600 -4.09700  28.27700 1.000 26.17318 ?  385 ASP   A O    1 
ATOM   1742 C  CB   . ASP   A 1 233 ? 27.04700 -2.42200  27.82300 1.000 24.08819 ?  385 ASP   A CB   1 
ATOM   1743 C  CG   . ASP   A 1 233 ? 28.44400 -2.19200  28.36100 1.000 28.80006 ?  385 ASP   A CG   1 
ATOM   1744 O  OD1  . ASP   A 1 233 ? 29.01600 -1.11400  28.09200 1.000 30.90353 ?  385 ASP   A OD1  1 
ATOM   1745 O  OD2  . ASP   A 1 233 ? 28.97500 -3.08800  29.04700 1.000 28.99970 ?  385 ASP   A OD2  1 
ATOM   1746 N  N    . LEU   A 1 234 ? 24.93500 -4.08800  26.12600 1.000 21.58064 ?  386 LEU   A N    1 
ATOM   1747 C  CA   . LEU   A 1 234 ? 23.56700 -4.13100  25.62300 1.000 21.91039 ?  386 LEU   A CA   1 
ATOM   1748 C  C    . LEU   A 1 234 ? 22.88100 -5.44500  25.97200 1.000 24.88448 ?  386 LEU   A C    1 
ATOM   1749 O  O    . LEU   A 1 234 ? 21.68100 -5.46400  26.26800 1.000 21.88288 ?  386 LEU   A O    1 
ATOM   1750 C  CB   . LEU   A 1 234 ? 23.56600 -3.90900  24.11200 1.000 20.86028 ?  386 LEU   A CB   1 
ATOM   1751 C  CG   . LEU   A 1 234 ? 23.74500 -2.45800  23.67600 1.000 26.45936 ?  386 LEU   A CG   1 
ATOM   1752 C  CD1  . LEU   A 1 234 ? 24.09100 -2.37900  22.20400 1.000 23.26483 ?  386 LEU   A CD1  1 
ATOM   1753 C  CD2  . LEU   A 1 234 ? 22.48500 -1.66900  23.97900 1.000 28.15246 ?  386 LEU   A CD2  1 
ATOM   1754 N  N    . ARG   A 1 235 ? 23.62300 -6.55600  25.93000 1.000 26.08285 ?  387 ARG   A N    1 
ATOM   1755 C  CA   . ARG   A 1 235 ? 23.05900 -7.83500  26.35100 1.000 30.29697 ?  387 ARG   A CA   1 
ATOM   1756 C  C    . ARG   A 1 235 ? 22.57300 -7.77000  27.79400 1.000 31.09542 ?  387 ARG   A C    1 
ATOM   1757 O  O    . ARG   A 1 235 ? 21.50700 -8.30100  28.12500 1.000 28.23435 ?  387 ARG   A O    1 
ATOM   1758 C  CB   . ARG   A 1 235 ? 24.09800 -8.94400  26.19500 1.000 28.84474 ?  387 ARG   A CB   1 
ATOM   1759 C  CG   . ARG   A 1 235 ? 24.60900 -9.14400  24.78300 1.000 29.59517 ?  387 ARG   A CG   1 
ATOM   1760 C  CD   . ARG   A 1 235 ? 23.50400 -9.49600  23.81000 1.000 31.26996 ?  387 ARG   A CD   1 
ATOM   1761 N  NE   . ARG   A 1 235 ? 24.06300 -9.83700  22.50700 1.000 38.47751 ?  387 ARG   A NE   1 
ATOM   1762 C  CZ   . ARG   A 1 235 ? 24.27500 -11.08100 22.08700 1.000 33.90274 ?  387 ARG   A CZ   1 
ATOM   1763 N  NH1  . ARG   A 1 235 ? 23.96700 -12.10800 22.86800 1.000 41.42317 ?  387 ARG   A NH1  1 
ATOM   1764 N  NH2  . ARG   A 1 235 ? 24.79600 -11.29700 20.88700 1.000 41.06803 ?  387 ARG   A NH2  1 
ATOM   1765 N  N    . SER   A 1 236 ? 23.34600 -7.12000  28.66700 1.000 27.09666 ?  388 SER   A N    1 
ATOM   1766 C  CA   . SER   A 1 236 ? 22.94700 -7.00300  30.06500 1.000 29.58231 ?  388 SER   A CA   1 
ATOM   1767 C  C    . SER   A 1 236 ? 21.75400 -6.06700  30.22300 1.000 28.25161 ?  388 SER   A C    1 
ATOM   1768 O  O    . SER   A 1 236 ? 20.84400 -6.34200  31.01400 1.000 27.58630 ?  388 SER   A O    1 
ATOM   1769 C  CB   . SER   A 1 236 ? 24.13300 -6.52200  30.90000 1.000 37.44921 ?  388 SER   A CB   1 
ATOM   1770 O  OG   . SER   A 1 236 ? 23.70400 -5.70400  31.97100 1.000 43.49100 ?  388 SER   A OG   1 
ATOM   1771 N  N    . LEU   A 1 237 ? 21.74200 -4.95300  29.48700 1.000 23.84067 ?  389 LEU   A N    1 
ATOM   1772 C  CA   . LEU   A 1 237 ? 20.57900 -4.07100  29.50300 1.000 24.05156 ?  389 LEU   A CA   1 
ATOM   1773 C  C    . LEU   A 1 237 ? 19.35400 -4.77500  28.93700 1.000 25.27931 ?  389 LEU   A C    1 
ATOM   1774 O  O    . LEU   A 1 237 ? 18.23500 -4.58600  29.43100 1.000 25.00381 ?  389 LEU   A O    1 
ATOM   1775 C  CB   . LEU   A 1 237 ? 20.87900 -2.79900  28.71200 1.000 22.99726 ?  389 LEU   A CB   1 
ATOM   1776 C  CG   . LEU   A 1 237 ? 21.92800 -1.87100  29.32200 1.000 27.15108 ?  389 LEU   A CG   1 
ATOM   1777 C  CD1  . LEU   A 1 237 ? 22.46700 -0.90700  28.27700 1.000 21.72678 ?  389 LEU   A CD1  1 
ATOM   1778 C  CD2  . LEU   A 1 237 ? 21.35100 -1.12200  30.50900 1.000 29.58598 ?  389 LEU   A CD2  1 
ATOM   1779 N  N    . ASN   A 1 238 ? 19.55300 -5.59300  27.90100 1.000 21.28572 ?  390 ASN   A N    1 
ATOM   1780 C  CA   . ASN   A 1 238 ? 18.46300 -6.38700  27.34000 1.000 26.02737 ?  390 ASN   A CA   1 
ATOM   1781 C  C    . ASN   A 1 238 ? 17.86100 -7.30200  28.39900 1.000 27.33410 ?  390 ASN   A C    1 
ATOM   1782 O  O    . ASN   A 1 238 ? 16.63700 -7.35300  28.57300 1.000 24.84669 ?  390 ASN   A O    1 
ATOM   1783 C  CB   . ASN   A 1 238 ? 18.98800 -7.19800  26.15100 1.000 24.86218 ?  390 ASN   A CB   1 
ATOM   1784 C  CG   . ASN   A 1 238 ? 17.88800 -7.88700  25.35700 1.000 31.43133 ?  390 ASN   A CG   1 
ATOM   1785 O  OD1  . ASN   A 1 238 ? 16.81700 -8.20500  25.87400 1.000 28.85108 ?  390 ASN   A OD1  1 
ATOM   1786 N  ND2  . ASN   A 1 238 ? 18.16000 -8.12300  24.08100 1.000 26.82873 ?  390 ASN   A ND2  1 
ATOM   1787 N  N    . GLU   A 1 239 ? 18.71400 -8.03000  29.12200 1.000 25.78694 ?  391 GLU   A N    1 
ATOM   1788 C  CA   . GLU   A 1 239 ? 18.23100 -8.94900  30.14900 1.000 32.39762 ?  391 GLU   A CA   1 
ATOM   1789 C  C    . GLU   A 1 239 ? 17.42300 -8.21700  31.21200 1.000 30.71372 ?  391 GLU   A C    1 
ATOM   1790 O  O    . GLU   A 1 239 ? 16.34600 -8.67100  31.61400 1.000 29.94810 ?  391 GLU   A O    1 
ATOM   1791 C  CB   . GLU   A 1 239 ? 19.40600 -9.68000  30.79600 1.000 37.50856 ?  391 GLU   A CB   1 
ATOM   1792 C  CG   . GLU   A 1 239 ? 20.06900 -10.72700 29.92500 1.000 51.31909 ?  391 GLU   A CG   1 
ATOM   1793 C  CD   . GLU   A 1 239 ? 21.46600 -11.06300 30.40400 1.000 66.66292 ?  391 GLU   A CD   1 
ATOM   1794 O  OE1  . GLU   A 1 239 ? 22.35900 -11.26200 29.55500 1.000 70.49895 ?  391 GLU   A OE1  1 
ATOM   1795 O  OE2  . GLU   A 1 239 ? 21.67000 -11.12100 31.63500 1.000 70.65174 ?  391 GLU   A OE2  1 
ATOM   1796 N  N    . GLU   A 1 240 ? 17.93600 -7.08300  31.69100 1.000 29.98987 ?  392 GLU   A N    1 
ATOM   1797 C  CA   . GLU   A 1 240 ? 17.23000 -6.35000  32.73600 1.000 31.91270 ?  392 GLU   A CA   1 
ATOM   1798 C  C    . GLU   A 1 240 ? 15.93500 -5.73800  32.21300 1.000 29.92063 ?  392 GLU   A C    1 
ATOM   1799 O  O    . GLU   A 1 240 ? 14.91600 -5.74500  32.91500 1.000 28.56661 ?  392 GLU   A O    1 
ATOM   1800 C  CB   . GLU   A 1 240 ? 18.13600 -5.27300  33.33200 1.000 30.13940 ?  392 GLU   A CB   1 
ATOM   1801 C  CG   . GLU   A 1 240 ? 17.50700 -4.52700  34.49900 1.000 32.35982 ?  392 GLU   A CG   1 
ATOM   1802 C  CD   . GLU   A 1 240 ? 17.13800 -5.44500  35.65200 1.000 36.26484 ?  392 GLU   A CD   1 
ATOM   1803 O  OE1  . GLU   A 1 240 ? 16.11100 -5.19300  36.31900 1.000 33.66699 ?  392 GLU   A OE1  1 
ATOM   1804 O  OE2  . GLU   A 1 240 ? 17.87600 -6.42200  35.90100 1.000 39.24114 ?  392 GLU   A OE2  1 
ATOM   1805 N  N    . HIS   A 1 241 ? 15.94700 -5.19500  30.99000 1.000 22.31524 ?  393 HIS   A N    1 
ATOM   1806 C  CA   . HIS   A 1 241 ? 14.71700 -4.62900  30.44000 1.000 21.65843 ?  393 HIS   A CA   1 
ATOM   1807 C  C    . HIS   A 1 241 ? 13.63700 -5.69100  30.29700 1.000 28.63759 ?  393 HIS   A C    1 
ATOM   1808 O  O    . HIS   A 1 241 ? 12.47300 -5.45200  30.63500 1.000 27.36954 ?  393 HIS   A O    1 
ATOM   1809 C  CB   . HIS   A 1 241 ? 14.96400 -3.96700  29.08500 1.000 23.07582 ?  393 HIS   A CB   1 
ATOM   1810 C  CG   . HIS   A 1 241 ? 13.69900 -3.53800  28.40600 1.000 22.54586 ?  393 HIS   A CG   1 
ATOM   1811 N  ND1  . HIS   A 1 241 ? 13.03400 -4.33400  27.50000 1.000 22.95802 ?  393 HIS   A ND1  1 
ATOM   1812 C  CD2  . HIS   A 1 241 ? 12.95000 -2.41800  28.54400 1.000 23.99290 ?  393 HIS   A CD2  1 
ATOM   1813 C  CE1  . HIS   A 1 241 ? 11.94200 -3.71400  27.08800 1.000 24.31254 ?  393 HIS   A CE1  1 
ATOM   1814 N  NE2  . HIS   A 1 241 ? 11.86700 -2.55000  27.70700 1.000 21.61585 ?  393 HIS   A NE2  1 
ATOM   1815 N  N    . SER   A 1 242 ? 14.00500 -6.87000  29.79300 1.000 29.75327 ?  394 SER   A N    1 
ATOM   1816 C  CA   . SER   A 1 242 ? 13.02500 -7.94200  29.63900 1.000 29.63901 ?  394 SER   A CA   1 
ATOM   1817 C  C    . SER   A 1 242 ? 12.45400 -8.36100  30.98300 1.000 30.26702 ?  394 SER   A C    1 
ATOM   1818 O  O    . SER   A 1 242 ? 11.24600 -8.62300  31.09800 1.000 31.37020 ?  394 SER   A O    1 
ATOM   1819 C  CB   . SER   A 1 242 ? 13.66000 -9.13900  28.92600 1.000 34.87480 ?  394 SER   A CB   1 
ATOM   1820 O  OG   . SER   A 1 242 ? 14.55000 -8.71800  27.91000 1.000 46.28416 ?  394 SER   A OG   1 
ATOM   1821 N  N    A LYS   A 1 243 ? 13.29500 -8.44000  32.02000 0.490 30.54704 ?  395 LYS   A N    1 
ATOM   1822 N  N    B LYS   A 1 243 ? 13.29500 -8.43300  32.01900 0.510 30.57320 ?  395 LYS   A N    1 
ATOM   1823 C  CA   A LYS   A 1 243 ? 12.80600 -8.75700  33.35800 0.490 31.92427 ?  395 LYS   A CA   1 
ATOM   1824 C  CA   B LYS   A 1 243 ? 12.81900 -8.74900  33.36000 0.510 31.95295 ?  395 LYS   A CA   1 
ATOM   1825 C  C    A LYS   A 1 243 ? 11.75100 -7.75300  33.80500 0.490 30.92641 ?  395 LYS   A C    1 
ATOM   1826 C  C    B LYS   A 1 243 ? 11.75900 -7.75300  33.81300 0.510 30.93591 ?  395 LYS   A C    1 
ATOM   1827 O  O    A LYS   A 1 243 ? 10.65900 -8.13200  34.24100 0.490 31.88887 ?  395 LYS   A O    1 
ATOM   1828 O  O    B LYS   A 1 243 ? 10.67000 -8.13600  34.25700 0.510 31.90251 ?  395 LYS   A O    1 
ATOM   1829 C  CB   A LYS   A 1 243 ? 13.96600 -8.79100  34.35200 0.490 34.31746 ?  395 LYS   A CB   1 
ATOM   1830 C  CB   B LYS   A 1 243 ? 13.99900 -8.76100  34.33300 0.510 34.31581 ?  395 LYS   A CB   1 
ATOM   1831 C  CG   A LYS   A 1 243 ? 14.78100 -10.07100 34.32500 0.490 32.35467 ?  395 LYS   A CG   1 
ATOM   1832 C  CG   B LYS   A 1 243 ? 13.69800 -9.37900  35.68800 0.510 35.85178 ?  395 LYS   A CG   1 
ATOM   1833 C  CD   A LYS   A 1 243 ? 15.87900 -10.04300 35.37600 0.490 36.96443 ?  395 LYS   A CD   1 
ATOM   1834 C  CD   B LYS   A 1 243 ? 14.96800 -9.54300  36.50500 0.510 34.73297 ?  395 LYS   A CD   1 
ATOM   1835 C  CE   A LYS   A 1 243 ? 16.98200 -11.03700 35.05400 0.490 41.46780 ?  395 LYS   A CE   1 
ATOM   1836 C  CE   B LYS   A 1 243 ? 14.69600 -9.38500  37.99200 0.510 41.36168 ?  395 LYS   A CE   1 
ATOM   1837 N  NZ   A LYS   A 1 243 ? 18.28500 -10.62600 35.64600 0.490 44.69678 ?  395 LYS   A NZ   1 
ATOM   1838 N  NZ   B LYS   A 1 243 ? 15.22300 -10.53700 38.77400 0.510 49.99204 ?  395 LYS   A NZ   1 
ATOM   1839 N  N    . GLN   A 1 244 ? 12.06500 -6.46000  33.69700 1.000 32.00486 ?  396 GLN   A N    1 
ATOM   1840 C  CA   . GLN   A 1 244 ? 11.11000 -5.43200  34.09100 1.000 29.32173 ?  396 GLN   A CA   1 
ATOM   1841 C  C    . GLN   A 1 244 ? 9.91500  -5.39900  33.14800 1.000 32.01817 ?  396 GLN   A C    1 
ATOM   1842 O  O    . GLN   A 1 244 ? 8.77500  -5.21700  33.59200 1.000 30.64540 ?  396 GLN   A O    1 
ATOM   1843 C  CB   . GLN   A 1 244 ? 11.81100 -4.07800  34.13100 1.000 30.44661 ?  396 GLN   A CB   1 
ATOM   1844 C  CG   . GLN   A 1 244 ? 13.07600 -4.09200  34.98000 1.000 33.11461 ?  396 GLN   A CG   1 
ATOM   1845 C  CD   . GLN   A 1 244 ? 13.47900 -2.71400  35.46100 1.000 34.67844 ?  396 GLN   A CD   1 
ATOM   1846 O  OE1  . GLN   A 1 244 ? 12.78100 -1.73400  35.21600 1.000 30.65610 ?  396 GLN   A OE1  1 
ATOM   1847 N  NE2  . GLN   A 1 244 ? 14.61300 -2.63300  36.14900 1.000 33.63838 ?  396 GLN   A NE2  1 
ATOM   1848 N  N    . TYR   A 1 245 ? 10.15000 -5.57700  31.84500 1.000 25.31288 ?  397 TYR   A N    1 
ATOM   1849 C  CA   . TYR   A 1 245 ? 9.03400  -5.62900  30.90600 1.000 28.31965 ?  397 TYR   A CA   1 
ATOM   1850 C  C    . TYR   A 1 245 ? 8.09100  -6.77500  31.24400 1.000 31.87540 ?  397 TYR   A C    1 
ATOM   1851 O  O    . TYR   A 1 245 ? 6.86700  -6.61300  31.22200 1.000 29.05855 ?  397 TYR   A O    1 
ATOM   1852 C  CB   . TYR   A 1 245 ? 9.53700  -5.76400  29.46800 1.000 27.42857 ?  397 TYR   A CB   1 
ATOM   1853 C  CG   . TYR   A 1 245 ? 8.40000  -5.89400  28.47800 1.000 23.86770 ?  397 TYR   A CG   1 
ATOM   1854 C  CD1  . TYR   A 1 245 ? 7.76600  -4.76800  27.97100 1.000 21.79782 ?  397 TYR   A CD1  1 
ATOM   1855 C  CD2  . TYR   A 1 245 ? 7.94400  -7.14300  28.07300 1.000 28.55727 ?  397 TYR   A CD2  1 
ATOM   1856 C  CE1  . TYR   A 1 245 ? 6.71900  -4.88200  27.07500 1.000 23.61091 ?  397 TYR   A CE1  1 
ATOM   1857 C  CE2  . TYR   A 1 245 ? 6.89600  -7.26600  27.18200 1.000 25.95598 ?  397 TYR   A CE2  1 
ATOM   1858 C  CZ   . TYR   A 1 245 ? 6.28500  -6.13200  26.68600 1.000 28.82088 ?  397 TYR   A CZ   1 
ATOM   1859 O  OH   . TYR   A 1 245 ? 5.24300  -6.24900  25.79600 1.000 30.53287 ?  397 TYR   A OH   1 
ATOM   1860 N  N    . ARG   A 1 246 ? 8.64700  -7.95100  31.55300 1.000 29.64991 ?  398 ARG   A N    1 
ATOM   1861 C  CA   . ARG   A 1 246 ? 7.80500  -9.09600  31.88400 1.000 33.08860 ?  398 ARG   A CA   1 
ATOM   1862 C  C    . ARG   A 1 246 ? 6.94500  -8.81100  33.11000 1.000 35.43909 ?  398 ARG   A C    1 
ATOM   1863 O  O    . ARG   A 1 246 ? 5.75200  -9.13300  33.12800 1.000 34.23495 ?  398 ARG   A O    1 
ATOM   1864 C  CB   . ARG   A 1 246 ? 8.66300  -10.34700 32.09800 1.000 42.94341 ?  398 ARG   A CB   1 
ATOM   1865 C  CG   . ARG   A 1 246 ? 9.22500  -10.93300 30.80700 1.000 49.50671 ?  398 ARG   A CG   1 
ATOM   1866 C  CD   . ARG   A 1 246 ? 9.74500  -12.36000 30.97700 1.000 56.16187 ?  398 ARG   A CD   1 
ATOM   1867 N  NE   . ARG   A 1 246 ? 10.51600 -12.56400 32.19800 1.000 61.98468 ?  398 ARG   A NE   1 
ATOM   1868 C  CZ   . ARG   A 1 246 ? 11.84500 -12.55300 32.24900 1.000 70.22182 ?  398 ARG   A CZ   1 
ATOM   1869 N  NH1  . ARG   A 1 246 ? 12.54900 -12.33800 31.14500 1.000 71.55956 ?  398 ARG   A NH1  1 
ATOM   1870 N  NH2  . ARG   A 1 246 ? 12.47100 -12.75200 33.40000 1.000 70.28521 ?  398 ARG   A NH2  1 
ATOM   1871 N  N    . SER   A 1 247 ? 7.52900  -8.18700  34.13600 1.000 32.16471 ?  399 SER   A N    1 
ATOM   1872 C  CA   . SER   A 1 247 ? 6.75900  -7.84500  35.32900 1.000 39.47390 ?  399 SER   A CA   1 
ATOM   1873 C  C    . SER   A 1 247 ? 5.71400  -6.77800  35.03000 1.000 37.36170 ?  399 SER   A C    1 
ATOM   1874 O  O    . SER   A 1 247 ? 4.57900  -6.85900  35.51600 1.000 39.23679 ?  399 SER   A O    1 
ATOM   1875 C  CB   . SER   A 1 247 ? 7.69200  -7.37700  36.44400 1.000 45.86401 ?  399 SER   A CB   1 
ATOM   1876 O  OG   . SER   A 1 247 ? 8.80400  -8.24400  36.57800 1.000 60.64161 ?  399 SER   A OG   1 
ATOM   1877 N  N    . LEU   A 1 248 ? 6.07500  -5.76400  34.24200 1.000 35.77113 ?  400 LEU   A N    1 
ATOM   1878 C  CA   . LEU   A 1 248 ? 5.11500  -4.72500  33.88900 1.000 32.95237 ?  400 LEU   A CA   1 
ATOM   1879 C  C    . LEU   A 1 248 ? 4.00700  -5.28300  33.00400 1.000 30.11208 ?  400 LEU   A C    1 
ATOM   1880 O  O    . LEU   A 1 248 ? 2.82000  -5.08000  33.27100 1.000 33.27831 ?  400 LEU   A O    1 
ATOM   1881 C  CB   . LEU   A 1 248 ? 5.83000  -3.56400  33.19500 1.000 28.11571 ?  400 LEU   A CB   1 
ATOM   1882 C  CG   . LEU   A 1 248 ? 6.75000  -2.70500  34.06100 1.000 34.80243 ?  400 LEU   A CG   1 
ATOM   1883 C  CD1  . LEU   A 1 248 ? 7.58500  -1.79200  33.18800 1.000 31.61176 ?  400 LEU   A CD1  1 
ATOM   1884 C  CD2  . LEU   A 1 248 ? 5.95100  -1.90600  35.07900 1.000 39.60726 ?  400 LEU   A CD2  1 
ATOM   1885 N  N    . SER   A 1 249 ? 4.38300  -6.00700  31.94800 1.000 34.09402 ?  401 SER   A N    1 
ATOM   1886 C  CA   . SER   A 1 249 ? 3.39600  -6.55500  31.02600 1.000 34.45976 ?  401 SER   A CA   1 
ATOM   1887 C  C    . SER   A 1 249 ? 2.51200  -7.61700  31.66600 1.000 34.34187 ?  401 SER   A C    1 
ATOM   1888 O  O    . SER   A 1 249 ? 1.42600  -7.89400  31.14500 1.000 32.71534 ?  401 SER   A O    1 
ATOM   1889 C  CB   . SER   A 1 249 ? 4.09100  -7.13700  29.80100 1.000 35.87832 ?  401 SER   A CB   1 
ATOM   1890 O  OG   . SER   A 1 249 ? 4.78900  -8.32500  30.13100 1.000 44.40114 ?  401 SER   A OG   1 
ATOM   1891 N  N    . PHE   A 1 250 ? 2.94300  -8.21500  32.78000 1.000 36.57982 ?  402 PHE   A N    1 
ATOM   1892 C  CA   . PHE   A 1 250 ? 2.13500  -9.24500  33.42400 1.000 40.82160 ?  402 PHE   A CA   1 
ATOM   1893 C  C    . PHE   A 1 250 ? 0.83900  -8.67500  33.98400 1.000 39.71910 ?  402 PHE   A C    1 
ATOM   1894 O  O    . PHE   A 1 250 ? -0.15100 -9.40200  34.11900 1.000 37.40944 ?  402 PHE   A O    1 
ATOM   1895 C  CB   . PHE   A 1 250 ? 2.93600  -9.92500  34.52900 1.000 42.22565 ?  402 PHE   A CB   1 
ATOM   1896 C  CG   . PHE   A 1 250 ? 2.32200  -11.20100 35.01800 1.000 49.56811 ?  402 PHE   A CG   1 
ATOM   1897 C  CD1  . PHE   A 1 250 ? 1.71700  -11.25600 36.26100 1.000 56.88059 ?  402 PHE   A CD1  1 
ATOM   1898 C  CD2  . PHE   A 1 250 ? 2.34600  -12.34600 34.23600 1.000 54.56776 ?  402 PHE   A CD2  1 
ATOM   1899 C  CE1  . PHE   A 1 250 ? 1.14700  -12.42600 36.72000 1.000 61.28068 ?  402 PHE   A CE1  1 
ATOM   1900 C  CE2  . PHE   A 1 250 ? 1.77800  -13.52200 34.68900 1.000 59.31772 ?  402 PHE   A CE2  1 
ATOM   1901 C  CZ   . PHE   A 1 250 ? 1.17800  -13.56100 35.93300 1.000 62.91810 ?  402 PHE   A CZ   1 
ATOM   1902 N  N    . GLN   A 1 251 ? 0.82700  -7.38900  34.32000 1.000 38.33088 ?  403 GLN   A N    1 
ATOM   1903 C  CA   . GLN   A 1 251 ? -0.38700 -6.73400  34.78000 1.000 33.45271 ?  403 GLN   A CA   1 
ATOM   1904 C  C    . GLN   A 1 251 ? -1.21400 -6.31000  33.57400 1.000 33.55503 ?  403 GLN   A C    1 
ATOM   1905 O  O    . GLN   A 1 251 ? -0.74700 -5.48400  32.77900 1.000 32.37046 ?  403 GLN   A O    1 
ATOM   1906 C  CB   . GLN   A 1 251 ? -0.05100 -5.52900  35.63800 1.000 40.23190 ?  403 GLN   A CB   1 
ATOM   1907 C  CG   . GLN   A 1 251 ? 0.97000  -5.82600  36.72600 1.000 49.66437 ?  403 GLN   A CG   1 
ATOM   1908 C  CD   . GLN   A 1 251 ? 0.32800  -6.19300  38.05200 1.000 71.54262 ?  403 GLN   A CD   1 
ATOM   1909 O  OE1  . GLN   A 1 251 ? 0.41200  -5.44200  39.02400 1.000 83.01938 ?  403 GLN   A OE1  1 
ATOM   1910 N  NE2  . GLN   A 1 251 ? -0.31600 -7.35400  38.09800 1.000 73.62569 ?  403 GLN   A NE2  1 
ATOM   1911 N  N    . PRO   A 1 252 ? -2.42400 -6.84700  33.39300 1.000 36.32400 ?  404 PRO   A N    1 
ATOM   1912 C  CA   . PRO   A 1 252 ? -3.21200 -6.49600  32.19800 1.000 32.89753 ?  404 PRO   A CA   1 
ATOM   1913 C  C    . PRO   A 1 252 ? -3.48700 -5.01000  32.05700 1.000 36.72045 ?  404 PRO   A C    1 
ATOM   1914 O  O    . PRO   A 1 252 ? -3.61100 -4.52100  30.92700 1.000 37.50888 ?  404 PRO   A O    1 
ATOM   1915 C  CB   . PRO   A 1 252 ? -4.50800 -7.29400  32.39600 1.000 36.06375 ?  404 PRO   A CB   1 
ATOM   1916 C  CG   . PRO   A 1 252 ? -4.11000 -8.44200  33.27000 1.000 44.94544 ?  404 PRO   A CG   1 
ATOM   1917 C  CD   . PRO   A 1 252 ? -3.05800 -7.91100  34.19000 1.000 41.46556 ?  404 PRO   A CD   1 
ATOM   1918 N  N    . GLU   A 1 253 ? -3.58800 -4.27500  33.16900 1.000 39.29887 ?  405 GLU   A N    1 
ATOM   1919 C  CA   . GLU   A 1 253 ? -3.80600 -2.83400  33.08000 1.000 41.36050 ?  405 GLU   A CA   1 
ATOM   1920 C  C    . GLU   A 1 253 ? -2.64300 -2.13800  32.38700 1.000 34.39246 ?  405 GLU   A C    1 
ATOM   1921 O  O    . GLU   A 1 253 ? -2.84600 -1.13800  31.68900 1.000 34.78431 ?  405 GLU   A O    1 
ATOM   1922 C  CB   . GLU   A 1 253 ? -4.02900 -2.23900  34.47300 1.000 48.19491 ?  405 GLU   A CB   1 
ATOM   1923 C  CG   . GLU   A 1 253 ? -3.09300 -2.76600  35.55300 1.000 57.13202 ?  405 GLU   A CG   1 
ATOM   1924 C  CD   . GLU   A 1 253 ? -3.61200 -4.03200  36.21300 1.000 59.77083 ?  405 GLU   A CD   1 
ATOM   1925 O  OE1  . GLU   A 1 253 ? -4.26000 -3.93300  37.27600 1.000 72.07889 ?  405 GLU   A OE1  1 
ATOM   1926 O  OE2  . GLU   A 1 253 ? -3.37400 -5.12700  35.66400 1.000 58.63716 ?  405 GLU   A OE2  1 
ATOM   1927 N  N    . ASN   A 1 254 ? -1.42300 -2.65100  32.56300 1.000 28.93671 ?  406 ASN   A N    1 
ATOM   1928 C  CA   . ASN   A 1 254 ? -0.27400 -2.11300  31.84400 1.000 27.45328 ?  406 ASN   A CA   1 
ATOM   1929 C  C    . ASN   A 1 254 ? -0.25700 -2.58700  30.39600 1.000 31.64541 ?  406 ASN   A C    1 
ATOM   1930 O  O    . ASN   A 1 254 ? -0.02400 -1.79300  29.47800 1.000 31.94772 ?  406 ASN   A O    1 
ATOM   1931 C  CB   . ASN   A 1 254 ? 1.02800  -2.51800  32.54300 1.000 28.81997 ?  406 ASN   A CB   1 
ATOM   1932 C  CG   . ASN   A 1 254 ? 1.21800  -1.82800  33.88000 1.000 40.45478 ?  406 ASN   A CG   1 
ATOM   1933 O  OD1  . ASN   A 1 254 ? 1.92400  -2.32600  34.75600 1.000 43.16372 ?  406 ASN   A OD1  1 
ATOM   1934 N  ND2  . ASN   A 1 254 ? 0.58500  -0.67500  34.04300 1.000 41.64184 ?  406 ASN   A ND2  1 
ATOM   1935 N  N    . SER   A 1 255 ? -0.48400 -3.88700  30.17800 1.000 32.67531 ?  407 SER   A N    1 
ATOM   1936 C  CA   . SER   A 1 255 ? -0.47300 -4.42500  28.82100 1.000 29.99465 ?  407 SER   A CA   1 
ATOM   1937 C  C    . SER   A 1 255 ? -1.53200 -3.76400  27.94900 1.000 26.35384 ?  407 SER   A C    1 
ATOM   1938 O  O    . SER   A 1 255 ? -1.34800 -3.65000  26.73100 1.000 29.16007 ?  407 SER   A O    1 
ATOM   1939 C  CB   . SER   A 1 255 ? -0.68400 -5.94200  28.85700 1.000 39.26543 ?  407 SER   A CB   1 
ATOM   1940 O  OG   . SER   A 1 255 ? 0.55000  -6.63000  28.95900 1.000 51.02216 ?  407 SER   A OG   1 
ATOM   1941 N  N    . MET   A 1 256 ? -2.64000 -3.32100  28.55400 1.000 28.97286 ?  408 MET   A N    1 
ATOM   1942 C  CA   . MET   A 1 256 ? -3.67100 -2.60400  27.81000 1.000 27.74420 ?  408 MET   A CA   1 
ATOM   1943 C  C    . MET   A 1 256 ? -3.13300 -1.32500  27.18300 1.000 31.16178 ?  408 MET   A C    1 
ATOM   1944 O  O    . MET   A 1 256 ? -3.65600 -0.87200  26.15900 1.000 30.98082 ?  408 MET   A O    1 
ATOM   1945 C  CB   . MET   A 1 256 ? -4.84800 -2.26600  28.72700 1.000 31.76108 ?  408 MET   A CB   1 
ATOM   1946 C  CG   . MET   A 1 256 ? -5.93300 -3.32200  28.80800 1.000 40.26692 ?  408 MET   A CG   1 
ATOM   1947 S  SD   . MET   A 1 256 ? -7.42500 -2.62400  29.53500 1.000 44.79014 ?  408 MET   A SD   1 
ATOM   1948 C  CE   . MET   A 1 256 ? -6.72900 -1.79900  30.96500 1.000 35.27065 ?  408 MET   A CE   1 
ATOM   1949 N  N    . LYS   A 1 257 ? -2.10600 -0.72500  27.78100 1.000 27.72693 ?  409 LYS   A N    1 
ATOM   1950 C  CA   . LYS   A 1 257 ? -1.55600 0.53700   27.30400 1.000 26.06614 ?  409 LYS   A CA   1 
ATOM   1951 C  C    . LYS   A 1 257 ? -0.43100 0.35700   26.29300 1.000 23.74684 ?  409 LYS   A C    1 
ATOM   1952 O  O    . LYS   A 1 257 ? 0.03800  1.35000   25.72800 1.000 27.48263 ?  409 LYS   A O    1 
ATOM   1953 C  CB   . LYS   A 1 257 ? -1.05500 1.37500   28.48500 1.000 31.66509 ?  409 LYS   A CB   1 
ATOM   1954 C  CG   . LYS   A 1 257 ? -2.11300 1.66100   29.54100 1.000 36.73933 ?  409 LYS   A CG   1 
ATOM   1955 C  CD   . LYS   A 1 257 ? -3.41100 2.15200   28.91800 1.000 47.13896 ?  409 LYS   A CD   1 
ATOM   1956 C  CE   . LYS   A 1 257 ? -4.10800 3.16200   29.81600 1.000 64.00578 ?  409 LYS   A CE   1 
ATOM   1957 N  NZ   . LYS   A 1 257 ? -4.15800 4.51700   29.19800 1.000 66.95799 ?  409 LYS   A NZ   1 
ATOM   1958 N  N    . LEU   A 1 258 ? 0.00900  -0.87300  26.04700 1.000 23.24374 ?  410 LEU   A N    1 
ATOM   1959 C  CA   . LEU   A 1 258 ? 1.04900  -1.12500  25.06000 1.000 26.03800 ?  410 LEU   A CA   1 
ATOM   1960 C  C    . LEU   A 1 258 ? 0.42600  -1.11600  23.66500 1.000 27.96601 ?  410 LEU   A C    1 
ATOM   1961 O  O    . LEU   A 1 258 ? -0.77000 -0.86600  23.49200 1.000 28.26970 ?  410 LEU   A O    1 
ATOM   1962 C  CB   . LEU   A 1 258 ? 1.76100  -2.44100  25.36900 1.000 30.57594 ?  410 LEU   A CB   1 
ATOM   1963 C  CG   . LEU   A 1 258 ? 2.37300  -2.54200  26.76700 1.000 31.83153 ?  410 LEU   A CG   1 
ATOM   1964 C  CD1  . LEU   A 1 258 ? 3.05400  -3.88800  26.98500 1.000 29.46529 ?  410 LEU   A CD1  1 
ATOM   1965 C  CD2  . LEU   A 1 258 ? 3.34400  -1.39900  27.01000 1.000 28.36913 ?  410 LEU   A CD2  1 
ATOM   1966 N  N    . THR   A 1 259 ? 1.23200  -1.38200  22.64800 1.000 22.65145 ?  411 THR   A N    1 
ATOM   1967 C  CA   . THR   A 1 259 ? 0.74200  -1.49900  21.28600 1.000 24.63744 ?  411 THR   A CA   1 
ATOM   1968 C  C    . THR   A 1 259 ? 0.78200  -2.95400  20.83800 1.000 21.82704 ?  411 THR   A C    1 
ATOM   1969 O  O    . THR   A 1 259 ? 1.49400  -3.77500  21.42700 1.000 26.01242 ?  411 THR   A O    1 
ATOM   1970 C  CB   . THR   A 1 259 ? 1.57300  -0.63600  20.32500 1.000 24.81777 ?  411 THR   A CB   1 
ATOM   1971 O  OG1  . THR   A 1 259 ? 2.84400  -1.25500  20.10500 1.000 27.50451 ?  411 THR   A OG1  1 
ATOM   1972 C  CG2  . THR   A 1 259 ? 1.79400  0.74900   20.90700 1.000 25.55044 ?  411 THR   A CG2  1 
ATOM   1973 N  N    . PRO   A 1 260 ? 0.00600  -3.32000  19.81400 1.000 23.65893 ?  412 PRO   A N    1 
ATOM   1974 C  CA   . PRO   A 1 260 ? 0.07200  -4.70700  19.31700 1.000 23.24295 ?  412 PRO   A CA   1 
ATOM   1975 C  C    . PRO   A 1 260 ? 1.46100  -5.12400  18.86800 1.000 23.54525 ?  412 PRO   A C    1 
ATOM   1976 O  O    . PRO   A 1 260 ? 1.86200  -6.27300  19.09700 1.000 26.58759 ?  412 PRO   A O    1 
ATOM   1977 C  CB   . PRO   A 1 260 ? -0.92400 -4.69400  18.14900 1.000 26.18278 ?  412 PRO   A CB   1 
ATOM   1978 C  CG   . PRO   A 1 260 ? -1.91700 -3.65100  18.54600 1.000 27.77717 ?  412 PRO   A CG   1 
ATOM   1979 C  CD   . PRO   A 1 260 ? -1.09900 -2.57000  19.18900 1.000 24.49851 ?  412 PRO   A CD   1 
ATOM   1980 N  N    . LEU   A 1 261 ? 2.21300  -4.22000  18.23500 1.000 24.07599 ?  413 LEU   A N    1 
ATOM   1981 C  CA   . LEU   A 1 261 ? 3.56000  -4.56300  17.78800 1.000 23.50773 ?  413 LEU   A CA   1 
ATOM   1982 C  C    . LEU   A 1 261 ? 4.49700  -4.78600  18.96800 1.000 21.76723 ?  413 LEU   A C    1 
ATOM   1983 O  O    . LEU   A 1 261 ? 5.32000  -5.70800  18.94300 1.000 25.55591 ?  413 LEU   A O    1 
ATOM   1984 C  CB   . LEU   A 1 261 ? 4.10800  -3.47000  16.86900 1.000 22.27148 ?  413 LEU   A CB   1 
ATOM   1985 C  CG   . LEU   A 1 261 ? 5.50600  -3.71800  16.30100 1.000 26.79565 ?  413 LEU   A CG   1 
ATOM   1986 C  CD1  . LEU   A 1 261 ? 5.52400  -4.96200  15.42900 1.000 27.86951 ?  413 LEU   A CD1  1 
ATOM   1987 C  CD2  . LEU   A 1 261 ? 5.99000  -2.50800  15.52400 1.000 25.28117 ?  413 LEU   A CD2  1 
ATOM   1988 N  N    . VAL   A 1 262 ? 4.38900  -3.95400  20.00700 1.000 19.53421 ?  414 VAL   A N    1 
ATOM   1989 C  CA   . VAL   A 1 262 ? 5.22500  -4.13200  21.19100 1.000 20.40980 ?  414 VAL   A CA   1 
ATOM   1990 C  C    . VAL   A 1 262 ? 4.93400  -5.47500  21.84700 1.000 22.91966 ?  414 VAL   A C    1 
ATOM   1991 O  O    . VAL   A 1 262 ? 5.85200  -6.20000  22.25400 1.000 26.19715 ?  414 VAL   A O    1 
ATOM   1992 C  CB   . VAL   A 1 262 ? 5.01700  -2.96400  22.17300 1.000 23.11500 ?  414 VAL   A CB   1 
ATOM   1993 C  CG1  . VAL   A 1 262 ? 5.58600  -3.30700  23.53700 1.000 25.31716 ?  414 VAL   A CG1  1 
ATOM   1994 C  CG2  . VAL   A 1 262 ? 5.65700  -1.69500  21.63200 1.000 25.99108 ?  414 VAL   A CG2  1 
ATOM   1995 N  N    . LEU   A 1 263 ? 3.65400  -5.83800  21.94000 1.000 24.88495 ?  415 LEU   A N    1 
ATOM   1996 C  CA   . LEU   A 1 263 ? 3.29600  -7.12100  22.53200 1.000 25.67720 ?  415 LEU   A CA   1 
ATOM   1997 C  C    . LEU   A 1 263 ? 3.82800  -8.28100  21.70100 1.000 24.00473 ?  415 LEU   A C    1 
ATOM   1998 O  O    . LEU   A 1 263 ? 4.25100  -9.30500  22.24900 1.000 28.20722 ?  415 LEU   A O    1 
ATOM   1999 C  CB   . LEU   A 1 263 ? 1.77900  -7.21800  22.68000 1.000 25.53541 ?  415 LEU   A CB   1 
ATOM   2000 C  CG   . LEU   A 1 263 ? 1.16900  -6.38400  23.80400 1.000 24.98262 ?  415 LEU   A CG   1 
ATOM   2001 C  CD1  . LEU   A 1 263 ? -0.34300 -6.34400  23.69100 1.000 23.71937 ?  415 LEU   A CD1  1 
ATOM   2002 C  CD2  . LEU   A 1 263 ? 1.59900  -6.93200  25.15500 1.000 26.52547 ?  415 LEU   A CD2  1 
ATOM   2003 N  N    . GLU   A 1 264 ? 3.81100  -8.14000  20.37500 1.000 25.21335 ?  416 GLU   A N    1 
ATOM   2004 C  CA   . GLU   A 1 264 ? 4.31700  -9.20500  19.51500 1.000 29.65717 ?  416 GLU   A CA   1 
ATOM   2005 C  C    . GLU   A 1 264 ? 5.82800  -9.34400  19.63500 1.000 27.02542 ?  416 GLU   A C    1 
ATOM   2006 O  O    . GLU   A 1 264 ? 6.34800  -10.46100 19.73300 1.000 32.30144 ?  416 GLU   A O    1 
ATOM   2007 C  CB   . GLU   A 1 264 ? 3.92800  -8.94000  18.06100 1.000 30.10586 ?  416 GLU   A CB   1 
ATOM   2008 C  CG   . GLU   A 1 264 ? 4.07400  -10.15400 17.16400 1.000 28.63215 ?  416 GLU   A CG   1 
ATOM   2009 C  CD   . GLU   A 1 264 ? 3.82600  -9.83900  15.70400 1.000 30.18978 ?  416 GLU   A CD   1 
ATOM   2010 O  OE1  . GLU   A 1 264 ? 4.80200  -9.55100  14.97800 1.000 37.20408 ?  416 GLU   A OE1  1 
ATOM   2011 O  OE2  . GLU   A 1 264 ? 2.65400  -9.89200  15.27800 1.000 33.01139 ?  416 GLU   A OE2  1 
ATOM   2012 N  N    . VAL   A 1 265 ? 6.54800  -8.22200  19.63700 1.000 24.03054 ?  417 VAL   A N    1 
ATOM   2013 C  CA   . VAL   A 1 265 ? 8.00600  -8.27000  19.58500 1.000 26.03031 ?  417 VAL   A CA   1 
ATOM   2014 C  C    . VAL   A 1 265 ? 8.59300  -8.49300  20.97400 1.000 35.18594 ?  417 VAL   A C    1 
ATOM   2015 O  O    . VAL   A 1 265 ? 9.44100  -9.37000  21.17000 1.000 31.10549 ?  417 VAL   A O    1 
ATOM   2016 C  CB   . VAL   A 1 265 ? 8.56000  -6.98700  18.93700 1.000 24.66638 ?  417 VAL   A CB   1 
ATOM   2017 C  CG1  . VAL   A 1 265 ? 10.08200 -6.95200  19.02300 1.000 31.60434 ?  417 VAL   A CG1  1 
ATOM   2018 C  CG2  . VAL   A 1 265 ? 8.09700  -6.87900  17.49000 1.000 26.21755 ?  417 VAL   A CG2  1 
ATOM   2019 N  N    . PHE   A 1 266 ? 8.15600  -7.70600  21.96100 1.000 31.38936 ?  418 PHE   A N    1 
ATOM   2020 C  CA   . PHE   A 1 266 ? 8.74300  -7.80700  23.29400 1.000 31.44524 ?  418 PHE   A CA   1 
ATOM   2021 C  C    . PHE   A 1 266 ? 8.20300  -8.99100  24.08900 1.000 37.18251 ?  418 PHE   A C    1 
ATOM   2022 O  O    . PHE   A 1 266 ? 8.92800  -9.54600  24.92400 1.000 37.32804 ?  418 PHE   A O    1 
ATOM   2023 C  CB   . PHE   A 1 266 ? 8.52000  -6.51200  24.07900 1.000 26.84303 ?  418 PHE   A CB   1 
ATOM   2024 C  CG   . PHE   A 1 266 ? 9.41200  -5.38000  23.65100 1.000 26.97519 ?  418 PHE   A CG   1 
ATOM   2025 C  CD1  . PHE   A 1 266 ? 9.29600  -4.13300  24.24400 1.000 28.77103 ?  418 PHE   A CD1  1 
ATOM   2026 C  CD2  . PHE   A 1 266 ? 10.36300 -5.56100  22.65600 1.000 30.86982 ?  418 PHE   A CD2  1 
ATOM   2027 C  CE1  . PHE   A 1 266 ? 10.11000 -3.08900  23.85800 1.000 30.07792 ?  418 PHE   A CE1  1 
ATOM   2028 C  CE2  . PHE   A 1 266 ? 11.18200 -4.52000  22.26200 1.000 28.09132 ?  418 PHE   A CE2  1 
ATOM   2029 C  CZ   . PHE   A 1 266 ? 11.05500 -3.28200  22.86300 1.000 31.33851 ?  418 PHE   A CZ   1 
ATOM   2030 N  N    . GLY   A 1 267 ? 6.95500  -9.38100  23.87200 1.000 34.88865 ?  419 GLY   A N    1 
ATOM   2031 C  CA   . GLY   A 1 267 ? 6.38000  -10.53400 24.54500 1.000 37.16744 ?  419 GLY   A CA   1 
ATOM   2032 C  C    . GLY   A 1 267 ? 4.95000  -10.37000 25.03000 1.000 44.53948 ?  419 GLY   A C    1 
ATOM   2033 O  O    . GLY   A 1 267 ? 4.50400  -9.27600  25.37800 1.000 37.61366 ?  419 GLY   A O    1 
ATOM   2034 N  N    . ASN   A 1 268 ? 4.22100  -11.48600 25.06100 1.000 50.58523 ?  420 ASN   A N    1 
ATOM   2035 C  CA   . ASN   A 1 268 ? 2.82100  -11.52900 25.49100 1.000 58.78047 ?  420 ASN   A CA   1 
ATOM   2036 C  C    . ASN   A 1 268 ? 1.96400  -10.50200 24.75400 1.000 61.19672 ?  420 ASN   A C    1 
ATOM   2037 O  O    . ASN   A 1 268 ? 1.43400  -10.77400 23.67700 1.000 63.83280 ?  420 ASN   A O    1 
ATOM   2038 C  CB   . ASN   A 1 268 ? 2.71100  -11.30800 27.00300 1.000 60.29075 ?  420 ASN   A CB   1 
ATOM   2039 C  CG   . ASN   A 1 268 ? 2.68200  -12.60800 27.78100 1.000 66.14788 ?  420 ASN   A CG   1 
ATOM   2040 O  OD1  . ASN   A 1 268 ? 2.38200  -12.62500 28.97500 1.000 72.88518 ?  420 ASN   A OD1  1 
ATOM   2041 N  ND2  . ASN   A 1 268 ? 3.00100  -13.70600 27.10800 1.000 69.15075 ?  420 ASN   A ND2  1 
ATOM   2042 N  N    . LYS   B 2 1   ? 5.71200  -18.08700 18.87700 1.000 77.84480 ?  625 LYS   C N    1 
ATOM   2043 C  CA   . LYS   B 2 1   ? 4.35100  -17.96200 18.36900 1.000 72.74088 ?  625 LYS   C CA   1 
ATOM   2044 C  C    . LYS   B 2 1   ? 4.34900  -17.48800 16.92100 1.000 67.72700 ?  625 LYS   C C    1 
ATOM   2045 O  O    . LYS   B 2 1   ? 5.35800  -17.58800 16.22300 1.000 69.60476 ?  625 LYS   C O    1 
ATOM   2046 C  CB   . LYS   B 2 1   ? 3.54000  -16.99700 19.24000 1.000 71.46250 ?  625 LYS   C CB   1 
ATOM   2047 C  CG   . LYS   B 2 1   ? 4.04900  -15.55900 19.23200 1.000 69.21415 ?  625 LYS   C CG   1 
ATOM   2048 C  CD   . LYS   B 2 1   ? 4.22500  -15.02400 20.64400 1.000 69.61553 ?  625 LYS   C CD   1 
ATOM   2049 C  CE   . LYS   B 2 1   ? 4.32000  -13.50600 20.65700 1.000 66.14456 ?  625 LYS   C CE   1 
ATOM   2050 N  NZ   . LYS   B 2 1   ? 5.58500  -13.00600 20.05300 1.000 65.04807 ?  625 LYS   C NZ   1 
ATOM   2051 N  N    . ASN   B 2 2   ? 3.20100  -16.96200 16.51000 1.000 62.32375 ?  626 ASN   C N    1 
ATOM   2052 C  CA   . ASN   B 2 2   ? 3.04700  -16.37300 15.16200 1.000 58.99048 ?  626 ASN   C CA   1 
ATOM   2053 C  C    . ASN   B 2 2   ? 3.35000  -14.87800 15.28300 1.000 52.66238 ?  626 ASN   C C    1 
ATOM   2054 O  O    . ASN   B 2 2   ? 2.91200  -14.30000 16.27300 1.000 51.18099 ?  626 ASN   C O    1 
ATOM   2055 C  CB   . ASN   B 2 2   ? 1.66100  -16.66000 14.59900 1.000 67.44238 ?  626 ASN   C CB   1 
ATOM   2056 C  CG   . ASN   B 2 2   ? 1.40100  -18.14900 14.52600 1.000 79.28559 ?  626 ASN   C CG   1 
ATOM   2057 O  OD1  . ASN   B 2 2   ? 1.56300  -18.76300 13.47900 1.000 82.95828 ?  626 ASN   C OD1  1 
ATOM   2058 N  ND2  . ASN   B 2 2   ? 1.04700  -18.74300 15.64800 1.000 83.58010 ?  626 ASN   C ND2  1 
ATOM   2059 N  N    . HIS   B 2 3   ? 4.08900  -14.31200 14.33100 1.000 44.18196 ?  627 HIS   C N    1 
ATOM   2060 C  CA   . HIS   B 2 3   ? 4.46500  -12.89900 14.33800 1.000 37.19583 ?  627 HIS   C CA   1 
ATOM   2061 C  C    . HIS   B 2 3   ? 3.98800  -12.21800 13.05800 1.000 34.90755 ?  627 HIS   C C    1 
ATOM   2062 O  O    . HIS   B 2 3   ? 4.80100  -11.76200 12.24500 1.000 37.55330 ?  627 HIS   C O    1 
ATOM   2063 C  CB   . HIS   B 2 3   ? 5.97400  -12.74400 14.50700 1.000 35.84983 ?  627 HIS   C CB   1 
ATOM   2064 C  CG   . HIS   B 2 3   ? 6.50500  -13.36100 15.76400 1.000 38.55542 ?  627 HIS   C CG   1 
ATOM   2065 N  ND1  . HIS   B 2 3   ? 6.74800  -14.71300 15.88300 1.000 45.09326 ?  627 HIS   C ND1  1 
ATOM   2066 C  CD2  . HIS   B 2 3   ? 6.82700  -12.81500 16.96000 1.000 40.09868 ?  627 HIS   C CD2  1 
ATOM   2067 C  CE1  . HIS   B 2 3   ? 7.20200  -14.97200 17.09600 1.000 41.58266 ?  627 HIS   C CE1  1 
ATOM   2068 N  NE2  . HIS   B 2 3   ? 7.25800  -13.83700 17.76900 1.000 42.22561 ?  627 HIS   C NE2  1 
ATOM   2069 N  N    . PRO   B 2 4   ? 2.66800  -12.11400 12.85700 1.000 36.11509 ?  628 PRO   C N    1 
ATOM   2070 C  CA   . PRO   B 2 4   ? 2.17400  -11.57000 11.58200 1.000 36.24870 ?  628 PRO   C CA   1 
ATOM   2071 C  C    . PRO   B 2 4   ? 2.54200  -10.11600 11.35700 1.000 30.38140 ?  628 PRO   C C    1 
ATOM   2072 O  O    . PRO   B 2 4   ? 2.72700  -9.71400  10.20200 1.000 31.94937 ?  628 PRO   C O    1 
ATOM   2073 C  CB   . PRO   B 2 4   ? 0.65300  -11.75400 11.68600 1.000 31.65593 ?  628 PRO   C CB   1 
ATOM   2074 C  CG   . PRO   B 2 4   ? 0.37800  -11.75900 13.15000 1.000 36.69053 ?  628 PRO   C CG   1 
ATOM   2075 C  CD   . PRO   B 2 4   ? 1.56600  -12.43500 13.78200 1.000 38.98211 ?  628 PRO   C CD   1 
ATOM   2076 N  N    . MET   B 2 5   ? 2.65100  -9.31200  12.41600 1.000 28.53145 ?  629 MET   C N    1 
ATOM   2077 C  CA   . MET   B 2 5   ? 2.98100  -7.90300  12.23200 1.000 29.06634 ?  629 MET   C CA   1 
ATOM   2078 C  C    . MET   B 2 5   ? 4.45800  -7.72400  11.89300 1.000 30.59654 ?  629 MET   C C    1 
ATOM   2079 O  O    . MET   B 2 5   ? 4.81000  -6.93700  11.00600 1.000 30.25591 ?  629 MET   C O    1 
ATOM   2080 C  CB   . MET   B 2 5   ? 2.59500  -7.11000  13.48300 1.000 30.11258 ?  629 MET   C CB   1 
ATOM   2081 C  CG   . MET   B 2 5   ? 1.09000  -6.94400  13.65200 1.000 34.51779 ?  629 MET   C CG   1 
ATOM   2082 S  SD   . MET   B 2 5   ? 0.59000  -6.16200  15.19800 1.000 41.02738 ?  629 MET   C SD   1 
ATOM   2083 C  CE   . MET   B 2 5   ? 0.78200  -7.52300  16.34200 1.000 45.61690 ?  629 MET   C CE   1 
ATOM   2084 N  N    . LEU   B 2 6   ? 5.34000  -8.45900  12.57600 1.000 31.64172 ?  630 LEU   C N    1 
ATOM   2085 C  CA   . LEU   B 2 6   ? 6.75600  -8.42200  12.22000 1.000 34.43723 ?  630 LEU   C CA   1 
ATOM   2086 C  C    . LEU   B 2 6   ? 6.98200  -9.00000  10.82800 1.000 34.29765 ?  630 LEU   C C    1 
ATOM   2087 O  O    . LEU   B 2 6   ? 7.73000  -8.43500  10.02200 1.000 38.69564 ?  630 LEU   C O    1 
ATOM   2088 C  CB   . LEU   B 2 6   ? 7.58600  -9.17900  13.25600 1.000 34.79323 ?  630 LEU   C CB   1 
ATOM   2089 C  CG   . LEU   B 2 6   ? 9.05900  -9.37200  12.89800 1.000 47.49153 ?  630 LEU   C CG   1 
ATOM   2090 C  CD1  . LEU   B 2 6   ? 9.74900  -8.03400  12.74100 1.000 41.31856 ?  630 LEU   C CD1  1 
ATOM   2091 C  CD2  . LEU   B 2 6   ? 9.73500  -10.18400 13.98100 1.000 53.62233 ?  630 LEU   C CD2  1 
ATOM   2092 N  N    . MET   B 2 7   ? 6.33400  -10.13100 10.53100 1.000 36.94668 ?  631 MET   C N    1 
ATOM   2093 C  CA   . MET   B 2 7   ? 6.42600  -10.71600 9.19700  1.000 39.91825 ?  631 MET   C CA   1 
ATOM   2094 C  C    . MET   B 2 7   ? 6.00000  -9.71500  8.13000  1.000 35.21089 ?  631 MET   C C    1 
ATOM   2095 O  O    . MET   B 2 7   ? 6.67200  -9.56000  7.10300  1.000 38.81883 ?  631 MET   C O    1 
ATOM   2096 C  CB   . MET   B 2 7   ? 5.56300  -11.97700 9.10700  1.000 44.84867 ?  631 MET   C CB   1 
ATOM   2097 C  CG   . MET   B 2 7   ? 6.25400  -13.26700 9.52300  1.000 54.73047 ?  631 MET   C CG   1 
ATOM   2098 S  SD   . MET   B 2 7   ? 7.58300  -13.79200 8.41700  1.000 53.79635 ?  631 MET   C SD   1 
ATOM   2099 C  CE   . MET   B 2 7   ? 6.95500  -13.29400 6.81300  1.000 63.46089 ?  631 MET   C CE   1 
ATOM   2100 N  N    . ASN   B 2 8   ? 4.87900  -9.02600  8.35900  1.000 33.59238 ?  632 ASN   C N    1 
ATOM   2101 C  CA   . ASN   B 2 8   ? 4.38200  -8.06300  7.38200  1.000 31.95452 ?  632 ASN   C CA   1 
ATOM   2102 C  C    . ASN   B 2 8   ? 5.36700  -6.91600  7.18500  1.000 34.18005 ?  632 ASN   C C    1 
ATOM   2103 O  O    . ASN   B 2 8   ? 5.57800  -6.45500  6.05700  1.000 38.21838 ?  632 ASN   C O    1 
ATOM   2104 C  CB   . ASN   B 2 8   ? 3.01500  -7.53700  7.82200  1.000 34.48199 ?  632 ASN   C CB   1 
ATOM   2105 C  CG   . ASN   B 2 8   ? 2.43900  -6.52500  6.85400  1.000 43.32569 ?  632 ASN   C CG   1 
ATOM   2106 O  OD1  . ASN   B 2 8   ? 2.49400  -5.31900  7.09600  1.000 46.11983 ?  632 ASN   C OD1  1 
ATOM   2107 N  ND2  . ASN   B 2 8   ? 1.88300  -7.01000  5.75100  1.000 43.85185 ?  632 ASN   C ND2  1 
ATOM   2108 N  N    . LEU   B 2 9   ? 5.98800  -6.44800  8.27200  1.000 28.05653 ?  633 LEU   C N    1 
ATOM   2109 C  CA   . LEU   B 2 9   ? 6.96100  -5.36700  8.16100  1.000 30.53614 ?  633 LEU   C CA   1 
ATOM   2110 C  C    . LEU   B 2 9   ? 8.24900  -5.83800  7.50200  1.000 31.63338 ?  633 LEU   C C    1 
ATOM   2111 O  O    . LEU   B 2 9   ? 8.94200  -5.04100  6.85800  1.000 37.91152 ?  633 LEU   C O    1 
ATOM   2112 C  CB   . LEU   B 2 9   ? 7.24300  -4.77200  9.54000  1.000 35.39863 ?  633 LEU   C CB   1 
ATOM   2113 C  CG   . LEU   B 2 9   ? 6.05800  -4.03900  10.16800 1.000 33.94104 ?  633 LEU   C CG   1 
ATOM   2114 C  CD1  . LEU   B 2 9   ? 6.39400  -3.59200  11.57900 1.000 30.27008 ?  633 LEU   C CD1  1 
ATOM   2115 C  CD2  . LEU   B 2 9   ? 5.64100  -2.85800  9.30700  1.000 36.15505 ?  633 LEU   C CD2  1 
ATOM   2116 N  N    . LEU   B 2 10  ? 8.58000  -7.12000  7.64300  1.000 35.23760 ?  634 LEU   C N    1 
ATOM   2117 C  CA   . LEU   B 2 10  ? 9.68800  -7.70800  6.90400  1.000 37.28336 ?  634 LEU   C CA   1 
ATOM   2118 C  C    . LEU   B 2 10  ? 9.35400  -7.93200  5.43500  1.000 47.44601 ?  634 LEU   C C    1 
ATOM   2119 O  O    . LEU   B 2 10  ? 10.24400 -8.31600  4.66900  1.000 48.64731 ?  634 LEU   C O    1 
ATOM   2120 C  CB   . LEU   B 2 10  ? 10.09700 -9.03900  7.54300  1.000 35.05832 ?  634 LEU   C CB   1 
ATOM   2121 C  CG   . LEU   B 2 10  ? 10.89700 -8.96000  8.84700  1.000 38.09588 ?  634 LEU   C CG   1 
ATOM   2122 C  CD1  . LEU   B 2 10  ? 11.01800 -10.32600 9.51200  1.000 43.92663 ?  634 LEU   C CD1  1 
ATOM   2123 C  CD2  . LEU   B 2 10  ? 12.26700 -8.35900  8.60000  1.000 42.10187 ?  634 LEU   C CD2  1 
ATOM   2124 N  N    . LYS   B 2 11  ? 8.10700  -7.69400  5.03300  1.000 45.57827 ?  635 LYS   C N    1 
ATOM   2125 C  CA   . LYS   B 2 11  ? 7.61700  -7.96600  3.68200  1.000 57.43912 ?  635 LYS   C CA   1 
ATOM   2126 C  C    . LYS   B 2 11  ? 7.77400  -9.44300  3.33100  1.000 67.69791 ?  635 LYS   C C    1 
ATOM   2127 O  O    . LYS   B 2 11  ? 6.91800  -10.26300 3.67000  1.000 70.86589 ?  635 LYS   C O    1 
ATOM   2128 C  CB   . LYS   B 2 11  ? 8.33200  -7.09600  2.64300  1.000 59.82150 ?  635 LYS   C CB   1 
ATOM   2129 C  CG   . LYS   B 2 11  ? 7.70200  -7.18200  1.26200  1.000 64.80465 ?  635 LYS   C CG   1 
ATOM   2130 C  CD   . LYS   B 2 11  ? 8.64400  -6.73000  0.16500  1.000 68.20573 ?  635 LYS   C CD   1 
ATOM   2131 C  CE   . LYS   B 2 11  ? 10.08700 -7.04000  0.49700  1.000 69.54410 ?  635 LYS   C CE   1 
ATOM   2132 N  NZ   . LYS   B 2 11  ? 10.85000 -7.45400  -0.70900 1.000 72.07067 ?  635 LYS   C NZ   1 
HETATM 2133 C  C10  . A1L78 C 3 .   ? 16.01300 5.05000   26.07400 1.000 22.08636 ?  501 A1L78 A C10  1 
HETATM 2134 C  C13  . A1L78 C 3 .   ? 12.33300 1.87300   25.98300 1.000 40.00250 ?  501 A1L78 A C13  1 
HETATM 2135 C  C15  . A1L78 C 3 .   ? 11.15900 3.28500   27.41700 1.000 37.50048 ?  501 A1L78 A C15  1 
HETATM 2136 C  C20  . A1L78 C 3 .   ? 7.56600  -0.03200  29.00500 1.000 31.81261 ?  501 A1L78 A C20  1 
HETATM 2137 C  C21  . A1L78 C 3 .   ? 6.80900  -1.29600  29.31600 1.000 34.22951 ?  501 A1L78 A C21  1 
HETATM 2138 C  C22  . A1L78 C 3 .   ? 8.18800  -0.73500  26.69100 1.000 28.56184 ?  501 A1L78 A C22  1 
HETATM 2139 C  C26  . A1L78 C 3 .   ? 14.49100 7.83300   18.33000 1.000 36.88568 ?  501 A1L78 A C26  1 
HETATM 2140 C  C28  . A1L78 C 3 .   ? 13.29900 7.83700   17.41300 1.000 33.47868 ?  501 A1L78 A C28  1 
HETATM 2141 C  C01  . A1L78 C 3 .   ? 14.22000 7.84700   22.47800 1.000 23.99782 ?  501 A1L78 A C01  1 
HETATM 2142 C  C02  . A1L78 C 3 .   ? 13.76900 7.00800   21.55200 1.000 27.38841 ?  501 A1L78 A C02  1 
HETATM 2143 C  C03  . A1L78 C 3 .   ? 13.41300 5.73000   21.89300 1.000 26.89284 ?  501 A1L78 A C03  1 
HETATM 2144 C  C04  . A1L78 C 3 .   ? 13.55000 5.28500   23.16800 1.000 25.59601 ?  501 A1L78 A C04  1 
HETATM 2145 C  C05  . A1L78 C 3 .   ? 14.01400 6.14800   24.07300 1.000 23.93975 ?  501 A1L78 A C05  1 
HETATM 2146 C  C06  . A1L78 C 3 .   ? 14.32800 7.40000   23.75200 1.000 24.90373 ?  501 A1L78 A C06  1 
HETATM 2147 C  C09  . A1L78 C 3 .   ? 13.07500 4.14900   26.22700 1.000 31.77090 ?  501 A1L78 A C09  1 
HETATM 2148 C  C11  . A1L78 C 3 .   ? 13.97200 7.01600   27.01500 1.000 29.28104 ?  501 A1L78 A C11  1 
HETATM 2149 C  C12  . A1L78 C 3 .   ? 13.20700 2.91400   25.67500 1.000 40.35581 ?  501 A1L78 A C12  1 
HETATM 2150 C  C14  . A1L78 C 3 .   ? 11.30800 2.05000   26.88900 1.000 31.56476 ?  501 A1L78 A C14  1 
HETATM 2151 C  C16  . A1L78 C 3 .   ? 12.04600 4.31800   27.08000 1.000 45.43717 ?  501 A1L78 A C16  1 
HETATM 2152 C  C18  . A1L78 C 3 .   ? 9.36600  1.11200   27.91000 1.000 32.32976 ?  501 A1L78 A C18  1 
HETATM 2153 C  C19  . A1L78 C 3 .   ? 8.71000  -0.26100  28.04200 1.000 27.33297 ?  501 A1L78 A C19  1 
HETATM 2154 C  C23  . A1L78 C 3 .   ? 7.12300  0.13200   26.09700 1.000 26.59829 ?  501 A1L78 A C23  1 
HETATM 2155 C  C25  . A1L78 C 3 .   ? 14.10000 6.84500   19.34700 1.000 34.63714 ?  501 A1L78 A C25  1 
HETATM 2156 C  C29  . A1L78 C 3 .   ? 13.64800 7.94300   15.96000 1.000 37.26866 ?  501 A1L78 A C29  1 
HETATM 2157 C  C30  . A1L78 C 3 .   ? 13.84400 6.53400   15.49100 1.000 44.83970 ?  501 A1L78 A C30  1 
HETATM 2158 C  C33  . A1L78 C 3 .   ? 12.90100 4.76900   20.87900 1.000 24.97854 ?  501 A1L78 A C33  1 
HETATM 2159 C  C34  . A1L78 C 3 .   ? 12.50600 0.51700   25.32700 1.000 39.87474 ?  501 A1L78 A C34  1 
HETATM 2160 C  C35  . A1L78 C 3 .   ? 16.32000 3.86900   25.20600 1.000 23.12133 ?  501 A1L78 A C35  1 
HETATM 2161 C  C36  . A1L78 C 3 .   ? 12.66700 7.66000   26.72200 1.000 29.82593 ?  501 A1L78 A C36  1 
HETATM 2162 O  O07  . A1L78 C 3 .   ? 13.64200 7.55200   20.32000 1.000 33.93464 ?  501 A1L78 A O07  1 
HETATM 2163 O  O17  . A1L78 C 3 .   ? 10.46800 0.99900   27.14700 1.000 29.12905 ?  501 A1L78 A O17  1 
HETATM 2164 O  O24  . A1L78 C 3 .   ? 9.55600  -1.22400  28.50700 1.000 24.74554 ?  501 A1L78 A O24  1 
HETATM 2165 O  O27  . A1L78 C 3 .   ? 15.53000 7.15700   17.84400 1.000 35.09282 ?  501 A1L78 A O27  1 
HETATM 2166 O  O31  . A1L78 C 3 .   ? 14.14200 5.61200   16.29400 1.000 39.12683 ?  501 A1L78 A O31  1 
HETATM 2167 O  O32  . A1L78 C 3 .   ? 13.68200 6.37900   14.30400 1.000 31.81768 -1 501 A1L78 A O32  1 
HETATM 2168 SI SI08 . A1L78 C 3 .   ? 14.23000 5.59800   25.82900 1.000 24.90281 ?  501 A1L78 A SI08 1 
HETATM 2169 O  O    . HOH   D 4 .   ? 23.05900 -3.73100  32.80700 1.000 37.50785 ?  601 HOH   A O    1 
HETATM 2170 O  O    . HOH   D 4 .   ? 24.61400 -10.95900 29.57100 1.000 49.76405 ?  602 HOH   A O    1 
HETATM 2171 O  O    . HOH   D 4 .   ? 39.47000 5.17200   22.15300 1.000 43.98928 ?  603 HOH   A O    1 
HETATM 2172 O  O    . HOH   D 4 .   ? 11.32100 -12.79400 4.86300  1.000 62.11690 ?  604 HOH   A O    1 
HETATM 2173 O  O    . HOH   D 4 .   ? 34.85400 -9.31100  16.92400 1.000 70.51684 ?  605 HOH   A O    1 
HETATM 2174 O  O    . HOH   D 4 .   ? 19.21400 -8.56500  35.01500 1.000 42.17037 ?  606 HOH   A O    1 
HETATM 2175 O  O    . HOH   D 4 .   ? 12.88300 8.18600   13.02700 1.000 32.38552 ?  607 HOH   A O    1 
HETATM 2176 O  O    . HOH   D 4 .   ? 14.01500 -6.76500  26.64500 1.000 40.74758 ?  608 HOH   A O    1 
HETATM 2177 O  O    . HOH   D 4 .   ? 32.77800 -14.90900 14.40700 1.000 50.01129 ?  609 HOH   A O    1 
HETATM 2178 O  O    . HOH   D 4 .   ? 18.72900 2.75900   -0.91900 1.000 40.35148 ?  610 HOH   A O    1 
HETATM 2179 O  O    . HOH   D 4 .   ? 43.14600 4.55400   12.49000 1.000 37.95653 ?  611 HOH   A O    1 
HETATM 2180 O  O    . HOH   D 4 .   ? 3.44600  0.57200   16.01300 1.000 37.40189 ?  612 HOH   A O    1 
HETATM 2181 O  O    . HOH   D 4 .   ? 11.06800 -1.67100  4.62500  1.000 58.95363 ?  613 HOH   A O    1 
HETATM 2182 O  O    . HOH   D 4 .   ? 31.37000 -11.27800 13.77100 1.000 41.72159 ?  614 HOH   A O    1 
HETATM 2183 O  O    . HOH   D 4 .   ? 36.13800 -7.02800  1.15100  1.000 45.18302 ?  615 HOH   A O    1 
HETATM 2184 O  O    . HOH   D 4 .   ? 2.20000  1.15300   13.43500 1.000 72.49687 ?  616 HOH   A O    1 
HETATM 2185 O  O    . HOH   D 4 .   ? 14.79100 -6.12500  38.31900 1.000 46.56475 ?  617 HOH   A O    1 
HETATM 2186 O  O    . HOH   D 4 .   ? 24.51800 -6.91800  21.66600 1.000 22.86091 ?  618 HOH   A O    1 
HETATM 2187 O  O    . HOH   D 4 .   ? 9.51100  11.47500  12.77300 1.000 40.71227 ?  619 HOH   A O    1 
HETATM 2188 O  O    . HOH   D 4 .   ? 4.28600  -10.73100 30.92200 1.000 61.92589 ?  620 HOH   A O    1 
HETATM 2189 O  O    . HOH   D 4 .   ? 29.71700 11.14400  17.42100 1.000 37.01003 ?  621 HOH   A O    1 
HETATM 2190 O  O    . HOH   D 4 .   ? 27.96500 -9.91700  18.20800 1.000 45.30105 ?  622 HOH   A O    1 
HETATM 2191 O  O    . HOH   D 4 .   ? 18.51700 -18.44000 8.15200  1.000 38.76387 ?  623 HOH   A O    1 
HETATM 2192 O  O    . HOH   D 4 .   ? 13.93100 -6.73200  21.72200 1.000 34.23185 ?  624 HOH   A O    1 
HETATM 2193 O  O    . HOH   D 4 .   ? -0.58600 13.47200  20.47300 1.000 46.39364 ?  625 HOH   A O    1 
HETATM 2194 O  O    A HOH   D 4 .   ? 32.19700 10.22500  9.42000  0.560 46.32603 ?  626 HOH   A O    1 
HETATM 2195 O  O    B HOH   D 4 .   ? 33.17800 11.18000  9.48800  0.440 47.36044 ?  626 HOH   A O    1 
HETATM 2196 O  O    . HOH   D 4 .   ? 28.12900 -19.62600 14.78900 1.000 50.45811 ?  627 HOH   A O    1 
HETATM 2197 O  O    . HOH   D 4 .   ? 29.14900 7.93400   19.86300 1.000 28.20299 ?  628 HOH   A O    1 
HETATM 2198 O  O    . HOH   D 4 .   ? 9.20000  13.34900  34.14200 1.000 56.10622 ?  629 HOH   A O    1 
HETATM 2199 O  O    . HOH   D 4 .   ? 19.27600 -7.37200  3.15500  1.000 40.76096 ?  630 HOH   A O    1 
HETATM 2200 O  O    . HOH   D 4 .   ? 17.99300 12.17600  33.03200 1.000 34.65724 ?  631 HOH   A O    1 
HETATM 2201 O  O    . HOH   D 4 .   ? -1.09000 3.20700   20.26200 1.000 29.97141 ?  632 HOH   A O    1 
HETATM 2202 O  O    . HOH   D 4 .   ? 32.97700 0.41700   25.77000 1.000 35.66917 ?  633 HOH   A O    1 
HETATM 2203 O  O    . HOH   D 4 .   ? 19.27900 -20.47300 6.75600  1.000 41.02126 ?  634 HOH   A O    1 
HETATM 2204 O  O    . HOH   D 4 .   ? 1.89600  9.05700   28.19800 1.000 28.81423 ?  635 HOH   A O    1 
HETATM 2205 O  O    . HOH   D 4 .   ? 20.49500 6.79100   15.63500 1.000 25.60108 ?  636 HOH   A O    1 
HETATM 2206 O  O    . HOH   D 4 .   ? 18.05800 3.69600   11.56600 1.000 29.10045 ?  637 HOH   A O    1 
HETATM 2207 O  O    . HOH   D 4 .   ? 27.00200 -9.14100  28.27300 1.000 28.66840 ?  638 HOH   A O    1 
HETATM 2208 O  O    . HOH   D 4 .   ? 42.32600 0.84100   16.76300 1.000 37.56504 ?  639 HOH   A O    1 
HETATM 2209 O  O    . HOH   D 4 .   ? 0.69500  -10.75100 16.95600 1.000 45.14387 ?  640 HOH   A O    1 
HETATM 2210 O  O    . HOH   D 4 .   ? 33.38200 5.62500   26.45900 1.000 38.95840 ?  641 HOH   A O    1 
HETATM 2211 O  O    . HOH   D 4 .   ? 4.81900  6.78200   42.72600 1.000 72.05232 ?  642 HOH   A O    1 
HETATM 2212 O  O    . HOH   D 4 .   ? 25.26300 6.24300   1.55000  1.000 33.80061 ?  643 HOH   A O    1 
HETATM 2213 O  O    . HOH   D 4 .   ? 17.72300 -7.78300  38.27600 1.000 64.92595 ?  644 HOH   A O    1 
HETATM 2214 O  O    . HOH   D 4 .   ? 27.79600 0.79900   29.63700 1.000 43.34046 ?  645 HOH   A O    1 
HETATM 2215 O  O    . HOH   D 4 .   ? 10.27100 -10.45100 35.84600 1.000 45.39143 ?  646 HOH   A O    1 
HETATM 2216 O  O    . HOH   D 4 .   ? 13.61400 -1.18000  4.55500  1.000 40.64040 ?  647 HOH   A O    1 
HETATM 2217 O  O    . HOH   D 4 .   ? 14.88200 -19.55900 14.03000 1.000 54.10114 ?  648 HOH   A O    1 
HETATM 2218 O  O    . HOH   D 4 .   ? 36.78700 7.30200   20.70100 1.000 35.90486 ?  649 HOH   A O    1 
HETATM 2219 O  O    . HOH   D 4 .   ? 12.18000 -18.43900 5.27700  1.000 45.51073 ?  650 HOH   A O    1 
HETATM 2220 O  O    . HOH   D 4 .   ? -6.061   -1.675    25.020   1.000 21.83817 ?  651 HOH   A O    1 
HETATM 2221 O  O    . HOH   D 4 .   ? 34.09900 -7.60400  2.74100  1.000 53.18414 ?  652 HOH   A O    1 
HETATM 2222 O  O    . HOH   D 4 .   ? 10.87900 -8.80000  26.76600 1.000 35.57104 ?  653 HOH   A O    1 
HETATM 2223 O  O    . HOH   D 4 .   ? 12.34500 7.81100   8.64500  1.000 43.13599 ?  654 HOH   A O    1 
HETATM 2224 O  O    . HOH   D 4 .   ? 25.57800 -8.77200  20.00000 1.000 36.20076 ?  655 HOH   A O    1 
HETATM 2225 O  O    . HOH   D 4 .   ? 27.18800 -8.77800  5.90100  1.000 55.45548 ?  656 HOH   A O    1 
HETATM 2226 O  O    . HOH   D 4 .   ? -1.49100 10.16200  27.54300 1.000 42.37700 ?  657 HOH   A O    1 
HETATM 2227 O  O    . HOH   D 4 .   ? 43.92100 0.21700   19.00400 1.000 44.97203 ?  658 HOH   A O    1 
HETATM 2228 O  O    . HOH   D 4 .   ? 11.74300 10.44000  14.19200 1.000 32.47824 ?  659 HOH   A O    1 
HETATM 2229 O  O    . HOH   D 4 .   ? 15.13900 -9.86100  24.36200 1.000 47.76438 ?  660 HOH   A O    1 
HETATM 2230 O  O    . HOH   D 4 .   ? 0.16100  -8.48700  19.36600 1.000 42.88590 ?  661 HOH   A O    1 
HETATM 2231 O  O    . HOH   D 4 .   ? 18.86300 14.66300  17.12900 1.000 60.54032 ?  662 HOH   A O    1 
HETATM 2232 O  O    . HOH   D 4 .   ? 10.56500 17.28300  29.36900 1.000 59.44928 ?  663 HOH   A O    1 
HETATM 2233 O  O    . HOH   D 4 .   ? 21.18200 -7.93700  33.32700 1.000 43.06161 ?  664 HOH   A O    1 
HETATM 2234 O  O    . HOH   D 4 .   ? 30.89500 -1.83400  30.72100 1.000 52.61540 ?  665 HOH   A O    1 
HETATM 2235 O  O    . HOH   D 4 .   ? 36.08200 -5.32300  -3.20200 1.000 56.58510 ?  666 HOH   A O    1 
HETATM 2236 O  O    . HOH   D 4 .   ? 11.15200 15.33700  31.35000 1.000 56.60419 ?  667 HOH   A O    1 
HETATM 2237 O  O    . HOH   D 4 .   ? 2.71600  12.74100  21.29700 1.000 32.93123 ?  668 HOH   A O    1 
HETATM 2238 O  O    . HOH   D 4 .   ? -1.14700 1.53900   33.60500 1.000 51.42801 ?  669 HOH   A O    1 
HETATM 2239 O  O    . HOH   D 4 .   ? 18.86100 10.76600  9.34800  1.000 49.94360 ?  670 HOH   A O    1 
HETATM 2240 O  O    . HOH   D 4 .   ? 35.42400 8.54500   6.81400  1.000 42.19263 ?  671 HOH   A O    1 
HETATM 2241 O  O    . HOH   D 4 .   ? 40.55500 -5.04600  15.22600 1.000 60.09765 ?  672 HOH   A O    1 
HETATM 2242 O  O    . HOH   D 4 .   ? 9.91100  17.78800  18.46000 1.000 53.47689 ?  673 HOH   A O    1 
HETATM 2243 O  O    A HOH   D 4 .   ? -4.44000 4.46000   25.40200 0.560 27.14902 ?  674 HOH   A O    1 
HETATM 2244 O  O    B HOH   D 4 .   ? -3.90500 5.71100   27.01500 0.200 28.00906 ?  674 HOH   A O    1 
HETATM 2245 O  O    C HOH   D 4 .   ? -6.06100 3.81800   24.31100 0.230 29.02592 ?  674 HOH   A O    1 
HETATM 2246 O  O    . HOH   D 4 .   ? 31.83800 7.29600   30.93400 1.000 58.04592 ?  675 HOH   A O    1 
HETATM 2247 O  O    . HOH   D 4 .   ? 25.65200 -0.07200  31.07700 1.000 40.40438 ?  676 HOH   A O    1 
HETATM 2248 O  O    . HOH   D 4 .   ? 25.93700 0.54200   36.75900 1.000 57.94024 ?  677 HOH   A O    1 
HETATM 2249 O  O    . HOH   D 4 .   ? -3.02400 0.77900   22.78400 1.000 43.14640 ?  678 HOH   A O    1 
HETATM 2250 O  O    . HOH   D 4 .   ? -1.59000 8.08600   15.51200 1.000 33.02901 ?  679 HOH   A O    1 
HETATM 2251 O  O    . HOH   D 4 .   ? 32.69500 6.90500   4.47500  1.000 60.87794 ?  680 HOH   A O    1 
HETATM 2252 O  O    . HOH   D 4 .   ? 27.40500 -12.51100 18.31100 1.000 39.30373 ?  681 HOH   A O    1 
HETATM 2253 O  O    . HOH   D 4 .   ? 3.65000  4.21600   17.30200 1.000 32.54110 ?  682 HOH   A O    1 
HETATM 2254 O  O    . HOH   D 4 .   ? 14.88900 -14.32300 19.64700 1.000 48.94806 ?  683 HOH   A O    1 
HETATM 2255 O  O    . HOH   D 4 .   ? 22.83400 7.73800   1.01100  1.000 49.95072 ?  684 HOH   A O    1 
HETATM 2256 O  O    . HOH   D 4 .   ? 18.93200 -19.17900 4.27500  1.000 43.08743 ?  685 HOH   A O    1 
HETATM 2257 O  O    . HOH   D 4 .   ? 20.70200 1.44200   1.45100  1.000 35.92589 ?  686 HOH   A O    1 
HETATM 2258 O  O    . HOH   D 4 .   ? 30.06900 11.25900  11.42300 1.000 44.37449 ?  687 HOH   A O    1 
HETATM 2259 O  O    . HOH   D 4 .   ? 20.67800 13.93400  14.87100 1.000 54.29979 ?  688 HOH   A O    1 
HETATM 2260 O  O    . HOH   D 4 .   ? 8.48400  16.87900  17.00300 1.000 56.69129 ?  689 HOH   A O    1 
HETATM 2261 O  O    . HOH   D 4 .   ? 15.96800 -11.59500 31.74700 1.000 51.49480 ?  690 HOH   A O    1 
HETATM 2262 O  O    . HOH   D 4 .   ? 39.94900 -5.61800  4.05800  1.000 50.45909 ?  691 HOH   A O    1 
HETATM 2263 O  O    A HOH   D 4 .   ? -1.13300 8.91400   30.37600 0.590 34.61578 ?  692 HOH   A O    1 
HETATM 2264 O  O    B HOH   D 4 .   ? -2.68800 8.54400   29.09000 0.410 32.79301 ?  692 HOH   A O    1 
HETATM 2265 O  O    . HOH   D 4 .   ? 23.34200 -12.90500 25.64700 1.000 43.73419 ?  693 HOH   A O    1 
HETATM 2266 O  O    . HOH   D 4 .   ? 26.12800 15.29200  24.20800 1.000 42.02828 ?  694 HOH   A O    1 
HETATM 2267 O  O    . HOH   D 4 .   ? 7.50200  -0.05800  38.84700 1.000 67.72631 ?  695 HOH   A O    1 
HETATM 2268 O  O    . HOH   D 4 .   ? 37.35800 11.42700  14.45900 1.000 42.35883 ?  696 HOH   A O    1 
HETATM 2269 O  O    . HOH   D 4 .   ? 29.78800 10.52900  6.46500  1.000 71.33439 ?  697 HOH   A O    1 
HETATM 2270 O  O    . HOH   D 4 .   ? 34.41400 -7.50400  5.16300  1.000 42.13283 ?  698 HOH   A O    1 
HETATM 2271 O  O    . HOH   D 4 .   ? 20.67400 15.92000  21.29400 1.000 54.89791 ?  699 HOH   A O    1 
HETATM 2272 O  O    . HOH   D 4 .   ? 25.52300 9.99400   19.19900 1.000 38.48753 ?  700 HOH   A O    1 
HETATM 2273 O  O    A HOH   D 4 .   ? 27.80100 -4.73700  31.28500 0.670 48.03498 ?  701 HOH   A O    1 
HETATM 2274 O  O    B HOH   D 4 .   ? 29.14400 -6.61800  30.71700 0.330 56.20909 ?  701 HOH   A O    1 
HETATM 2275 O  O    . HOH   D 4 .   ? 40.24800 -1.00200  17.06300 1.000 31.46204 ?  702 HOH   A O    1 
HETATM 2276 O  O    . HOH   D 4 .   ? 9.65800  9.00900   9.14500  1.000 46.12348 ?  703 HOH   A O    1 
HETATM 2277 O  O    . HOH   D 4 .   ? 9.32300  -0.82300  8.48100  1.000 56.16658 ?  704 HOH   A O    1 
HETATM 2278 O  O    . HOH   D 4 .   ? 2.93000  -1.84000  37.60200 1.000 55.90504 ?  705 HOH   A O    1 
HETATM 2279 O  O    . HOH   D 4 .   ? 11.58200 -19.47200 7.81400  1.000 49.30279 ?  706 HOH   A O    1 
HETATM 2280 O  O    . HOH   D 4 .   ? 20.88700 11.00900  10.72700 1.000 58.89478 ?  707 HOH   A O    1 
HETATM 2281 O  O    . HOH   D 4 .   ? 13.76700 -4.02400  39.61700 1.000 68.32020 ?  708 HOH   A O    1 
HETATM 2282 O  O    . HOH   D 4 .   ? 23.23400 -22.24800 4.71200  1.000 63.30681 ?  709 HOH   A O    1 
HETATM 2283 O  O    . HOH   D 4 .   ? -4.63400 1.73800   24.79500 1.000 65.93835 ?  710 HOH   A O    1 
HETATM 2284 O  O    . HOH   D 4 .   ? 40.33100 -2.43300  19.20500 1.000 31.44692 ?  711 HOH   A O    1 
HETATM 2285 O  O    . HOH   D 4 .   ? 41.73700 2.11900   2.77000  1.000 50.06131 ?  712 HOH   A O    1 
HETATM 2286 O  O    . HOH   D 4 .   ? 12.62400 -21.45700 8.63700  1.000 61.66219 ?  713 HOH   A O    1 
HETATM 2287 O  O    A HOH   D 4 .   ? 15.09500 21.12400  22.22100 0.480 41.68441 ?  714 HOH   A O    1 
HETATM 2288 O  O    B HOH   D 4 .   ? 15.50100 21.29200  24.00000 0.520 43.57934 ?  714 HOH   A O    1 
HETATM 2289 O  O    A HOH   D 4 .   ? 40.57600 11.43000  17.05800 0.640 33.90198 ?  715 HOH   A O    1 
HETATM 2290 O  O    B HOH   D 4 .   ? 39.49800 12.41400  17.18400 0.360 34.42089 ?  715 HOH   A O    1 
HETATM 2291 O  O    . HOH   D 4 .   ? 2.35300  16.76900  31.28000 1.000 55.03925 ?  716 HOH   A O    1 
HETATM 2292 O  O    . HOH   D 4 .   ? 18.99900 20.57100  21.24700 1.000 50.66628 ?  717 HOH   A O    1 
HETATM 2293 O  O    . HOH   D 4 .   ? 7.69300  -20.67100 12.38900 1.000 63.36746 ?  718 HOH   A O    1 
HETATM 2294 O  O    . HOH   D 4 .   ? 12.24000 23.78800  19.93300 1.000 59.12819 ?  719 HOH   A O    1 
HETATM 2295 O  O    . HOH   D 4 .   ? 13.072   -22.908   15.761   1.000 53.96243 ?  720 HOH   A O    1 
HETATM 2296 O  O    . HOH   D 4 .   ? 13.96800 9.47300   7.67800  1.000 45.47342 ?  721 HOH   A O    1 
HETATM 2297 O  O    . HOH   D 4 .   ? 24.23400 -23.35100 11.67400 1.000 48.94678 ?  722 HOH   A O    1 
HETATM 2298 O  O    A HOH   D 4 .   ? 39.40700 -7.10800  6.44700  0.600 41.46604 ?  723 HOH   A O    1 
HETATM 2299 O  O    B HOH   D 4 .   ? 39.17600 -7.86300  8.19500  0.400 41.85616 ?  723 HOH   A O    1 
HETATM 2300 O  O    . HOH   D 4 .   ? 18.01700 -12.29100 24.24000 1.000 65.43926 ?  724 HOH   A O    1 
HETATM 2301 O  O    A HOH   D 4 .   ? 9.29900  -17.47800 13.88300 0.740 49.50869 ?  725 HOH   A O    1 
HETATM 2302 O  O    B HOH   D 4 .   ? 9.97400  -17.73400 14.96800 0.260 48.59091 ?  725 HOH   A O    1 
HETATM 2303 O  O    . HOH   D 4 .   ? 8.31800  -17.01600 20.53400 1.000 72.15604 ?  726 HOH   A O    1 
HETATM 2304 O  O    . HOH   D 4 .   ? 30.30000 2.28200   30.21700 1.000 59.92084 ?  727 HOH   A O    1 
HETATM 2305 O  O    . HOH   D 4 .   ? 35.23000 -9.70100  5.46900  1.000 49.71125 ?  728 HOH   A O    1 
HETATM 2306 O  O    . HOH   D 4 .   ? 26.82400 6.73300   18.74600 1.000 35.01536 ?  729 HOH   A O    1 
HETATM 2307 O  O    . HOH   D 4 .   ? 20.30400 -11.96500 23.57100 1.000 44.22870 ?  730 HOH   A O    1 
HETATM 2308 O  O    . HOH   D 4 .   ? 7.38300  -13.28000 22.92400 1.000 43.72501 ?  731 HOH   A O    1 
HETATM 2309 O  O    . HOH   D 4 .   ? 48.50900 -5.54100  6.18600  1.000 43.54964 ?  732 HOH   A O    1 
HETATM 2310 O  O    A HOH   D 4 .   ? 35.69000 -10.80100 12.74700 0.540 42.98656 ?  733 HOH   A O    1 
HETATM 2311 O  O    B HOH   D 4 .   ? 36.81900 -12.10600 11.10900 0.460 40.82665 ?  733 HOH   A O    1 
HETATM 2312 O  O    . HOH   D 4 .   ? 40.02100 -2.27600  14.74000 1.000 41.79541 ?  734 HOH   A O    1 
HETATM 2313 O  O    A HOH   D 4 .   ? 27.12800 9.12200   15.27100 0.570 33.59976 ?  735 HOH   A O    1 
HETATM 2314 O  O    B HOH   D 4 .   ? 25.09500 9.76800   14.29900 0.430 38.53697 ?  735 HOH   A O    1 
HETATM 2315 O  O    . HOH   D 4 .   ? 25.18400 -2.33800  31.10200 1.000 45.84552 ?  736 HOH   A O    1 
HETATM 2316 O  O    . HOH   D 4 .   ? 14.69300 23.19200  25.26000 1.000 65.32929 ?  737 HOH   A O    1 
HETATM 2317 O  O    A HOH   D 4 .   ? 39.63200 -7.45300  17.17800 0.420 38.46177 ?  738 HOH   A O    1 
HETATM 2318 O  O    B HOH   D 4 .   ? 40.74600 -6.43800  18.59500 0.580 43.34616 ?  738 HOH   A O    1 
HETATM 2319 O  O    . HOH   D 4 .   ? 45.64900 -4.86200  7.47000  1.000 83.06486 ?  739 HOH   A O    1 
HETATM 2320 O  O    . HOH   D 4 .   ? 18.58200 12.31600  7.52600  1.000 82.03568 ?  740 HOH   A O    1 
HETATM 2321 O  O    . HOH   D 4 .   ? 32.66000 -10.44900 16.67000 1.000 57.23245 ?  741 HOH   A O    1 
HETATM 2322 O  O    . HOH   D 4 .   ? 20.24500 7.91800   38.12800 1.000 55.88083 ?  742 HOH   A O    1 
HETATM 2323 O  O    . HOH   D 4 .   ? 13.10000 -7.86000  24.04200 1.000 46.68103 ?  743 HOH   A O    1 
HETATM 2324 O  O    . HOH   D 4 .   ? 37.50900 10.16300  21.04900 1.000 51.55662 ?  744 HOH   A O    1 
HETATM 2325 O  O    . HOH   D 4 .   ? 20.50500 -11.37700 25.94000 1.000 55.60694 ?  745 HOH   A O    1 
HETATM 2326 O  O    . HOH   D 4 .   ? 30.78500 -9.37400  17.75400 1.000 45.23459 ?  746 HOH   A O    1 
HETATM 2327 O  O    . HOH   D 4 .   ? 28.30900 10.44900  19.37300 1.000 57.40845 ?  747 HOH   A O    1 
HETATM 2328 O  O    . HOH   D 4 .   ? 10.59800 -4.85200  37.83000 1.000 58.22366 ?  748 HOH   A O    1 
HETATM 2329 O  O    . HOH   D 4 .   ? 40.296   10.598    22.651   1.000 54.56780 ?  749 HOH   A O    1 
HETATM 2330 O  O    . HOH   D 4 .   ? 20.27400 -24.69700 9.07900  1.000 60.80833 ?  750 HOH   A O    1 
HETATM 2331 O  O    . HOH   D 4 .   ? 24.76500 9.64800   16.63900 1.000 42.43417 ?  751 HOH   A O    1 
HETATM 2332 O  O    A HOH   D 4 .   ? 7.69900  -3.76800  37.99400 0.690 51.35591 ?  752 HOH   A O    1 
HETATM 2333 O  O    B HOH   D 4 .   ? 9.03100  -3.18400  37.83900 0.310 49.19037 ?  752 HOH   A O    1 
HETATM 2334 O  O    A HOH   D 4 .   ? 35.15700 -0.20600  27.16600 0.420 31.82575 ?  753 HOH   A O    1 
HETATM 2335 O  O    B HOH   D 4 .   ? 36.58700 -2.25500  26.64800 0.580 46.71617 ?  753 HOH   A O    1 
HETATM 2336 O  O    . HOH   D 4 .   ? -3.75300 -12.14100 33.57700 1.000 46.68459 ?  754 HOH   A O    1 
HETATM 2337 O  O    . HOH   D 4 .   ? -1.974   -13.775   27.801   1.000 55.35801 ?  755 HOH   A O    1 
HETATM 2338 O  O    A HOH   D 4 .   ? 23.864   7.160     43.532   0.500 39.11107 ?  756 HOH   A O    1 
HETATM 2339 O  O    B HOH   D 4 .   ? 22.490   6.917     41.842   0.500 34.58585 ?  756 HOH   A O    1 
HETATM 2340 O  O    . HOH   E 4 .   ? 1.82600  -11.29100 8.12500  1.000 37.85884 ?  701 HOH   C O    1 
HETATM 2341 O  O    . HOH   E 4 .   ? 4.69900  -9.01100  0.33700  1.000 54.99606 ?  702 HOH   C O    1 
HETATM 2342 O  O    . HOH   E 4 .   ? -1.73400 -14.57100 16.48400 1.000 67.06986 ?  703 HOH   C O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N    . LYS   A 18  ? 0.52427 1.04813 0.65996 -0.06733 0.13323  -0.17702 123 LYS   A N    
2    C  CA   . LYS   A 18  ? 0.46914 0.97579 0.62868 -0.05137 0.12573  -0.19013 123 LYS   A CA   
3    C  C    . LYS   A 18  ? 0.37746 0.84836 0.51236 -0.04868 0.11684  -0.18672 123 LYS   A C    
4    O  O    . LYS   A 18  ? 0.46465 0.92498 0.60997 -0.03592 0.11331  -0.20295 123 LYS   A O    
5    C  CB   . LYS   A 18  ? 0.31594 0.80774 0.49911 -0.04962 0.11566  -0.17843 123 LYS   A CB   
6    C  CG   . LYS   A 18  ? 0.33416 0.86090 0.54228 -0.05367 0.12267  -0.17901 123 LYS   A CG   
7    C  CD   . LYS   A 18  ? 0.44113 0.96314 0.68614 -0.04336 0.11296  -0.17944 123 LYS   A CD   
8    C  CE   . LYS   A 18  ? 0.35632 0.90440 0.63161 -0.03360 0.11813  -0.19336 123 LYS   A CE   
9    N  NZ   . LYS   A 18  ? 0.35946 0.91001 0.63180 -0.02317 0.12438  -0.21398 123 LYS   A NZ   
10   N  N    . LEU   A 19  ? 0.42178 0.87326 0.52645 -0.06064 0.11291  -0.16543 124 LEU   A N    
11   C  CA   . LEU   A 19  ? 0.42151 0.84252 0.50163 -0.05918 0.10508  -0.16047 124 LEU   A CA   
12   C  C    . LEU   A 19  ? 0.45304 0.89686 0.51411 -0.06021 0.11361  -0.17359 124 LEU   A C    
13   O  O    . LEU   A 19  ? 0.45498 0.91883 0.49300 -0.07247 0.12124  -0.16412 124 LEU   A O    
14   C  CB   . LEU   A 19  ? 0.51533 0.91111 0.57234 -0.07094 0.09914  -0.13438 124 LEU   A CB   
15   C  CG   . LEU   A 19  ? 0.52450 0.88195 0.56477 -0.06737 0.08797  -0.12643 124 LEU   A CG   
16   C  CD1  . LEU   A 19  ? 0.39729 0.73155 0.45973 -0.05451 0.07793  -0.13375 124 LEU   A CD1  
17   C  CD2  . LEU   A 19  ? 0.45685 0.79265 0.47778 -0.07888 0.08405  -0.10217 124 LEU   A CD2  
18   N  N    . SER   A 20  ? 0.38630 0.82782 0.45727 -0.04808 0.11205  -0.19508 125 SER   A N    
19   C  CA   . SER   A 20  ? 0.37736 0.83883 0.43351 -0.04832 0.11754  -0.21047 125 SER   A CA   
20   C  C    . SER   A 20  ? 0.42546 0.87742 0.44416 -0.05702 0.11398  -0.19646 125 SER   A C    
21   O  O    . SER   A 20  ? 0.34989 0.77368 0.35717 -0.05966 0.10615  -0.17826 125 SER   A O    
22   C  CB   . SER   A 20  ? 0.36551 0.81888 0.44455 -0.03370 0.11382  -0.23590 125 SER   A CB   
23   O  OG   . SER   A 20  ? 0.34093 0.76434 0.41822 -0.02785 0.10510  -0.23580 125 SER   A OG   
24   N  N    . GLU   A 21  ? 0.44389 0.91331 0.44533 -0.06091 0.11591  -0.20192 126 GLU   A N    
25   C  CA   . GLU   A 21  ? 0.48008 0.94443 0.44797 -0.06866 0.11139  -0.18773 126 GLU   A CA   
26   C  C    . GLU   A 21  ? 0.45255 0.88791 0.41928 -0.06077 0.10184  -0.19308 126 GLU   A C    
27   O  O    . GLU   A 21  ? 0.42464 0.84474 0.36980 -0.06559 0.09654  -0.17556 126 GLU   A O    
28   C  CB   . GLU   A 21  ? 0.53710 1.02977 0.49393 -0.07216 0.11479  -0.19799 126 GLU   A CB   
29   C  CG   . GLU   A 21  ? 0.68544 1.18967 0.66921 -0.06199 0.11800  -0.22804 126 GLU   A CG   
30   C  CD   . GLU   A 21  ? 0.76205 1.29148 0.76328 -0.06280 0.12761  -0.23411 126 GLU   A CD   
31   O  OE1  . GLU   A 21  ? 0.72351 1.24630 0.75437 -0.05405 0.12881  -0.24342 126 GLU   A OE1  
32   O  OE2  . GLU   A 21  ? 0.83018 1.38714 0.81610 -0.07213 0.13358  -0.22890 126 GLU   A OE2  
33   N  N    . GLU   A 22  ? 0.40118 0.82914 0.39206 -0.04905 0.09951  -0.21628 127 GLU   A N    
34   C  CA   . GLU   A 22  ? 0.35374 0.75352 0.34492 -0.04234 0.09000  -0.22078 127 GLU   A CA   
35   C  C    . GLU   A 22  ? 0.33280 0.69810 0.33101 -0.04030 0.08207  -0.20147 127 GLU   A C    
36   O  O    . GLU   A 22  ? 0.33902 0.67746 0.32588 -0.04031 0.07223  -0.18944 127 GLU   A O    
37   C  CB   . GLU   A 22  ? 0.62771 1.02315 0.64720 -0.03088 0.08782  -0.24784 127 GLU   A CB   
38   C  CG   . GLU   A 22  ? 0.72855 1.09442 0.75002 -0.02509 0.07741  -0.25197 127 GLU   A CG   
39   C  CD   . GLU   A 22  ? 0.84242 1.19669 0.89856 -0.01352 0.07447  -0.27502 127 GLU   A CD   
40   O  OE1  . GLU   A 22  ? 0.89836 1.26183 0.98135 -0.00752 0.07967  -0.28588 127 GLU   A OE1  
41   O  OE2  . GLU   A 22  ? 0.91674 1.25234 0.97468 -0.01073 0.06650  -0.28113 127 GLU   A OE2  
42   N  N    . GLN   A 23  ? 0.32272 0.68736 0.34118 -0.03897 0.08456  -0.19626 128 GLN   A N    
43   C  CA   . GLN   A 23  ? 0.30616 0.63807 0.33092 -0.03856 0.07546  -0.17580 128 GLN   A CA   
44   C  C    . GLN   A 23  ? 0.36231 0.68435 0.35877 -0.04984 0.07340  -0.15003 128 GLN   A C    
45   O  O    . GLN   A 23  ? 0.32683 0.61775 0.31829 -0.04922 0.06414  -0.13574 128 GLN   A O    
46   C  CB   . GLN   A 23  ? 0.37770 0.71631 0.42988 -0.03580 0.07828  -0.17657 128 GLN   A CB   
47   C  CG   . GLN   A 23  ? 0.34770 0.68246 0.43442 -0.02196 0.07570  -0.19586 128 GLN   A CG   
48   C  CD   . GLN   A 23  ? 0.33596 0.68412 0.45187 -0.01864 0.07873  -0.19712 128 GLN   A CD   
49   O  OE1  . GLN   A 23  ? 0.28879 0.66149 0.40111 -0.02657 0.08693  -0.19242 128 GLN   A OE1  
50   N  NE2  . GLN   A 23  ? 0.28972 0.62286 0.43604 -0.00723 0.07164  -0.20216 128 GLN   A NE2  
51   N  N    . GLN   A 24  ? 0.32147 0.67001 0.30057 -0.06022 0.08222  -0.14343 129 GLN   A N    
52   C  CA   . GLN   A 24  ? 0.34030 0.67910 0.29398 -0.07071 0.08015  -0.11830 129 GLN   A CA   
53   C  C    . GLN   A 24  ? 0.33336 0.66034 0.26702 -0.06921 0.07315  -0.11524 129 GLN   A C    
54   O  O    . GLN   A 24  ? 0.36098 0.66272 0.28347 -0.07165 0.06608  -0.09589 129 GLN   A O    
55   C  CB   . GLN   A 24  ? 0.36869 0.74126 0.30910 -0.08269 0.09128  -0.11102 129 GLN   A CB   
56   C  CG   . GLN   A 24  ? 0.38687 0.77537 0.34739 -0.08592 0.09882  -0.11277 129 GLN   A CG   
57   C  CD   . GLN   A 24  ? 0.53893 0.96600 0.48692 -0.09818 0.11115  -0.10743 129 GLN   A CD   
58   O  OE1  . GLN   A 24  ? 0.56605 0.99389 0.49069 -0.10882 0.11163  -0.08689 129 GLN   A OE1  
59   N  NE2  . GLN   A 24  ? 0.58579 1.04417 0.55096 -0.09631 0.12039  -0.12466 129 GLN   A NE2  
60   N  N    . HIS   A 25  ? 0.34161 0.68794 0.27190 -0.06526 0.07509  -0.13533 130 HIS   A N    
61   C  CA   . HIS   A 25  ? 0.37780 0.71638 0.29140 -0.06387 0.06769  -0.13513 130 HIS   A CA   
62   C  C    . HIS   A 25  ? 0.38638 0.68590 0.31213 -0.05582 0.05636  -0.13170 130 HIS   A C    
63   O  O    . HIS   A 25  ? 0.36417 0.64569 0.27628 -0.05724 0.04895  -0.11601 130 HIS   A O    
64   C  CB   . HIS   A 25  ? 0.42162 0.78887 0.33407 -0.06107 0.07203  -0.16256 130 HIS   A CB   
65   C  CG   . HIS   A 25  ? 0.46599 0.83237 0.36051 -0.06150 0.06456  -0.16387 130 HIS   A CG   
66   N  ND1  . HIS   A 25  ? 0.47202 0.84226 0.34037 -0.06940 0.06092  -0.14124 130 HIS   A ND1  
67   C  CD2  . HIS   A 25  ? 0.53594 0.89582 0.44009 -0.05492 0.05854  -0.18265 130 HIS   A CD2  
68   C  CE1  . HIS   A 25  ? 0.52964 0.89810 0.39164 -0.06735 0.05296  -0.14656 130 HIS   A CE1  
69   N  NE2  . HIS   A 25  ? 0.53744 0.89949 0.42052 -0.05925 0.05161  -0.17188 130 HIS   A NE2  
70   N  N    . ILE   A 26  ? 0.37142 0.65896 0.32407 -0.04724 0.05499  -0.14532 131 ILE   A N    
71   C  CA   . ILE   A 26  ? 0.31642 0.56958 0.28189 -0.04021 0.04487  -0.14144 131 ILE   A CA   
72   C  C    . ILE   A 26  ? 0.34329 0.57313 0.29996 -0.04451 0.04058  -0.11614 131 ILE   A C    
73   O  O    . ILE   A 26  ? 0.34949 0.55713 0.30001 -0.04289 0.03289  -0.10648 131 ILE   A O    
74   C  CB   . ILE   A 26  ? 0.32566 0.57305 0.32279 -0.03140 0.04470  -0.15595 131 ILE   A CB   
75   C  CG1  . ILE   A 26  ? 0.36775 0.62855 0.37765 -0.02504 0.04657  -0.18278 131 ILE   A CG1  
76   C  CG2  . ILE   A 26  ? 0.32372 0.53759 0.33247 -0.02674 0.03515  -0.14472 131 ILE   A CG2  
77   C  CD1  . ILE   A 26  ? 0.39513 0.65601 0.43931 -0.01602 0.04828  -0.19786 131 ILE   A CD1  
78   N  N    . ILE   A 27  ? 0.34699 0.58240 0.30461 -0.05026 0.04585  -0.10636 132 ILE   A N    
79   C  CA   . ILE   A 27  ? 0.33151 0.54473 0.28281 -0.05512 0.04257  -0.08494 132 ILE   A CA   
80   C  C    . ILE   A 27  ? 0.37426 0.58338 0.30178 -0.06044 0.04066  -0.06906 132 ILE   A C    
81   O  O    . ILE   A 27  ? 0.40529 0.58896 0.32890 -0.05940 0.03435  -0.05638 132 ILE   A O    
82   C  CB   . ILE   A 27  ? 0.29227 0.51586 0.25041 -0.06191 0.04905  -0.07950 132 ILE   A CB   
83   C  CG1  . ILE   A 27  ? 0.30911 0.53154 0.29351 -0.05545 0.04793  -0.09104 132 ILE   A CG1  
84   C  CG2  . ILE   A 27  ? 0.38085 0.58470 0.32956 -0.06950 0.04713  -0.05834 132 ILE   A CG2  
85   C  CD1  . ILE   A 27  ? 0.33876 0.57798 0.33338 -0.06175 0.05434  -0.08897 132 ILE   A CD1  
86   N  N    . ALA   A 28  ? 0.38499 0.62101 0.29701 -0.06599 0.04611  -0.06928 133 ALA   A N    
87   C  CA   . ALA   A 28  ? 0.33044 0.56607 0.22058 -0.07099 0.04350  -0.05193 133 ALA   A CA   
88   C  C    . ALA   A 28  ? 0.35548 0.57609 0.24261 -0.06401 0.03428  -0.05402 133 ALA   A C    
89   O  O    . ALA   A 28  ? 0.34705 0.55011 0.22614 -0.06448 0.02880  -0.03668 133 ALA   A O    
90   C  CB   . ALA   A 28  ? 0.34951 0.62233 0.22291 -0.07839 0.05071  -0.05299 133 ALA   A CB   
91   N  N    . ILE   A 29  ? 0.33753 0.56481 0.23339 -0.05750 0.03253  -0.07538 134 ILE   A N    
92   C  CA   . ILE   A 29  ? 0.33012 0.54435 0.22590 -0.05179 0.02373  -0.07861 134 ILE   A CA   
93   C  C    . ILE   A 29  ? 0.34250 0.52242 0.24937 -0.04716 0.01767  -0.06833 134 ILE   A C    
94   O  O    . ILE   A 29  ? 0.31987 0.48604 0.22068 -0.04568 0.01137  -0.05717 134 ILE   A O    
95   C  CB   . ILE   A 29  ? 0.33578 0.56170 0.24325 -0.04653 0.02359  -0.10515 134 ILE   A CB   
96   C  CG1  . ILE   A 29  ? 0.36441 0.62652 0.25636 -0.05147 0.02865  -0.11672 134 ILE   A CG1  
97   C  CG2  . ILE   A 29  ? 0.30937 0.51649 0.22365 -0.04082 0.01422  -0.10854 134 ILE   A CG2  
98   C  CD1  . ILE   A 29  ? 0.43211 0.70889 0.33943 -0.04701 0.03234  -0.14664 134 ILE   A CD1  
99   N  N    . LEU   A 30  ? 0.30553 0.47369 0.22918 -0.04484 0.01950  -0.07212 135 LEU   A N    
100  C  CA   . LEU   A 30  ? 0.31970 0.45911 0.25312 -0.04097 0.01417  -0.06449 135 LEU   A CA   
101  C  C    . LEU   A 30  ? 0.31844 0.44335 0.24145 -0.04552 0.01409  -0.04416 135 LEU   A C    
102  O  O    . LEU   A 30  ? 0.29905 0.40315 0.22289 -0.04248 0.00908  -0.03619 135 LEU   A O    
103  C  CB   . LEU   A 30  ? 0.33224 0.46727 0.28542 -0.03806 0.01552  -0.07300 135 LEU   A CB   
104  C  CG   . LEU   A 30  ? 0.31292 0.45437 0.28334 -0.03141 0.01411  -0.09214 135 LEU   A CG   
105  C  CD1  . LEU   A 30  ? 0.32831 0.46721 0.31971 -0.02837 0.01496  -0.09680 135 LEU   A CD1  
106  C  CD2  . LEU   A 30  ? 0.27171 0.39795 0.24554 -0.02654 0.00651  -0.09367 135 LEU   A CD2  
107  N  N    A LEU   A 31  ? 0.30346 0.43895 0.21844 -0.05296 0.02000  -0.03584 136 LEU   A N    
108  N  N    B LEU   A 31  ? 0.32344 0.45913 0.23844 -0.05297 0.02003  -0.03594 136 LEU   A N    
109  C  CA   A LEU   A 31  ? 0.34958 0.46998 0.25666 -0.05774 0.01994  -0.01633 136 LEU   A CA   
110  C  CA   B LEU   A 31  ? 0.33895 0.46029 0.24578 -0.05800 0.02020  -0.01634 136 LEU   A CA   
111  C  C    A LEU   A 31  ? 0.38120 0.49895 0.27615 -0.05605 0.01516  -0.00530 136 LEU   A C    
112  C  C    B LEU   A 31  ? 0.36212 0.48014 0.25699 -0.05622 0.01530  -0.00521 136 LEU   A C    
113  O  O    A LEU   A 31  ? 0.36878 0.46461 0.26476 -0.05386 0.01150  0.00608  136 LEU   A O    
114  O  O    B LEU   A 31  ? 0.36949 0.46552 0.26535 -0.05419 0.01176  0.00636  136 LEU   A O    
115  C  CB   A LEU   A 31  ? 0.32776 0.46207 0.22981 -0.06735 0.02727  -0.00861 136 LEU   A CB   
116  C  CB   B LEU   A 31  ? 0.34291 0.48002 0.24417 -0.06760 0.02765  -0.00912 136 LEU   A CB   
117  C  CG   A LEU   A 31  ? 0.32445 0.45897 0.23972 -0.07082 0.03164  -0.01427 136 LEU   A CG   
118  C  CG   B LEU   A 31  ? 0.34235 0.47351 0.25471 -0.07273 0.03179  -0.00864 136 LEU   A CG   
119  C  CD1  A LEU   A 31  ? 0.38042 0.53479 0.29041 -0.08129 0.03947  -0.00696 136 LEU   A CD1  
120  C  CD1  B LEU   A 31  ? 0.31694 0.45027 0.24572 -0.06711 0.03100  -0.02594 136 LEU   A CD1  
121  C  CD2  A LEU   A 31  ? 0.34342 0.44920 0.26656 -0.07045 0.02823  -0.00846 136 LEU   A CD2  
122  C  CD2  B LEU   A 31  ? 0.35724 0.51064 0.26395 -0.08300 0.03970  -0.00223 136 LEU   A CD2  
123  N  N    . ASP   A 32  ? 0.35691 0.49871 0.24110 -0.05690 0.01504  -0.00928 137 ASP   A N    
124  C  CA   . ASP   A 32  ? 0.32671 0.47071 0.19967 -0.05550 0.00927  0.00154  137 ASP   A CA   
125  C  C    . ASP   A 32  ? 0.36030 0.48806 0.24213 -0.04716 0.00197  -0.00418 137 ASP   A C    
126  O  O    . ASP   A 32  ? 0.41798 0.53378 0.29812 -0.04442 -0.00299 0.00900  137 ASP   A O    
127  C  CB   . ASP   A 32  ? 0.38302 0.56101 0.24150 -0.05933 0.01057  -0.00418 137 ASP   A CB   
128  C  CG   . ASP   A 32  ? 0.46829 0.65408 0.31362 -0.05925 0.00387  0.00935  137 ASP   A CG   
129  O  OD1  . ASP   A 32  ? 0.49054 0.68977 0.33306 -0.05638 -0.00097 -0.00270 137 ASP   A OD1  
130  O  OD2  . ASP   A 32  ? 0.48778 0.66680 0.32706 -0.06223 0.00302  0.03219  137 ASP   A OD2  
131  N  N    . ALA   A 33  ? 0.37972 0.50736 0.27307 -0.04302 0.00136  -0.02300 138 ALA   A N    
132  C  CA   . ALA   A 33  ? 0.31988 0.43271 0.22343 -0.03632 -0.00504 -0.02780 138 ALA   A CA   
133  C  C    . ALA   A 33  ? 0.36778 0.45387 0.27785 -0.03379 -0.00613 -0.01607 138 ALA   A C    
134  O  O    . ALA   A 33  ? 0.35832 0.43428 0.27018 -0.02973 -0.01097 -0.00965 138 ALA   A O    
135  C  CB   . ALA   A 33  ? 0.28768 0.40279 0.20548 -0.03315 -0.00491 -0.04787 138 ALA   A CB   
136  N  N    . HIS   A 34  ? 0.29052 0.36680 0.20485 -0.03641 -0.00145 -0.01431 139 HIS   A N    
137  C  CA   . HIS   A 34  ? 0.29888 0.35143 0.21837 -0.03512 -0.00169 -0.00575 139 HIS   A CA   
138  C  C    . HIS   A 34  ? 0.36808 0.41258 0.28021 -0.03604 -0.00220 0.01130  139 HIS   A C    
139  O  O    . HIS   A 34  ? 0.34271 0.37049 0.25955 -0.03166 -0.00461 0.01696  139 HIS   A O    
140  C  CB   . HIS   A 34  ? 0.29495 0.34257 0.21991 -0.03932 0.00296  -0.00866 139 HIS   A CB   
141  C  CG   . HIS   A 34  ? 0.30886 0.33433 0.23845 -0.03915 0.00303  -0.00336 139 HIS   A CG   
142  N  ND1  . HIS   A 34  ? 0.35480 0.36846 0.29092 -0.03371 -0.00039 -0.00650 139 HIS   A ND1  
143  C  CD2  . HIS   A 34  ? 0.34692 0.36107 0.27586 -0.04446 0.00647  0.00366  139 HIS   A CD2  
144  C  CE1  . HIS   A 34  ? 0.35929 0.35676 0.29718 -0.03529 0.00129  -0.00282 139 HIS   A CE1  
145  N  NE2  . HIS   A 34  ? 0.35442 0.35062 0.28873 -0.04178 0.00519  0.00268  139 HIS   A NE2  
146  N  N    A HIS   A 35  ? 0.38579 0.44281 0.28769 -0.04156 0.00022  0.02037  140 HIS   A N    
147  N  N    B HIS   A 35  ? 0.38722 0.44448 0.28910 -0.04162 0.00028  0.02017  140 HIS   A N    
148  C  CA   A HIS   A 35  ? 0.40368 0.45250 0.30102 -0.04223 -0.00099 0.03936  140 HIS   A CA   
149  C  CA   B HIS   A 35  ? 0.40680 0.45735 0.30339 -0.04262 -0.00085 0.03929  140 HIS   A CA   
150  C  C    A HIS   A 35  ? 0.41387 0.46601 0.31007 -0.03569 -0.00783 0.04417  140 HIS   A C    
151  C  C    B HIS   A 35  ? 0.41250 0.46501 0.30849 -0.03589 -0.00771 0.04413  140 HIS   A C    
152  O  O    A HIS   A 35  ? 0.41447 0.45199 0.31490 -0.03201 -0.01014 0.05722  140 HIS   A O    
153  O  O    B HIS   A 35  ? 0.41611 0.45357 0.31645 -0.03226 -0.00992 0.05714  140 HIS   A O    
154  C  CB   A HIS   A 35  ? 0.44682 0.51169 0.33313 -0.05055 0.00273  0.05024  140 HIS   A CB   
155  C  CB   B HIS   A 35  ? 0.44049 0.51012 0.32524 -0.05079 0.00268  0.04874  140 HIS   A CB   
156  C  CG   A HIS   A 35  ? 0.47324 0.53410 0.36287 -0.05794 0.00952  0.04873  140 HIS   A CG   
157  C  CG   B HIS   A 35  ? 0.47452 0.54005 0.35428 -0.05223 0.00062  0.07147  140 HIS   A CG   
158  N  ND1  A HIS   A 35  ? 0.47186 0.51216 0.37290 -0.05728 0.01111  0.04200  140 HIS   A ND1  
159  N  ND1  B HIS   A 35  ? 0.50934 0.59308 0.37921 -0.05080 -0.00464 0.08070  140 HIS   A ND1  
160  C  CD2  A HIS   A 35  ? 0.46044 0.53785 0.34374 -0.06686 0.01506  0.05297  140 HIS   A CD2  
161  C  CD2  B HIS   A 35  ? 0.50616 0.55184 0.39099 -0.05518 0.00265  0.08743  140 HIS   A CD2  
162  C  CE1  A HIS   A 35  ? 0.41040 0.45415 0.31290 -0.06548 0.01664  0.04197  140 HIS   A CE1  
163  C  CE1  B HIS   A 35  ? 0.50546 0.58094 0.37496 -0.05207 -0.00614 0.10338  140 HIS   A CE1  
164  N  NE2  A HIS   A 35  ? 0.48914 0.55504 0.38174 -0.07134 0.01950  0.04875  140 HIS   A NE2  
165  N  NE2  B HIS   A 35  ? 0.48451 0.53533 0.36398 -0.05461 -0.00149 0.10756  140 HIS   A NE2  
166  N  N    . LYS   A 36  ? 0.36023 0.43149 0.25299 -0.03407 -0.01122 0.03295  141 LYS   A N    
167  C  CA   . LYS   A 36  ? 0.34138 0.41900 0.23401 -0.02896 -0.01843 0.03631  141 LYS   A CA   
168  C  C    . LYS   A 36  ? 0.37584 0.43708 0.28238 -0.02198 -0.02121 0.02982  141 LYS   A C    
169  O  O    . LYS   A 36  ? 0.37467 0.43842 0.28448 -0.01733 -0.02688 0.03484  141 LYS   A O    
170  C  CB   . LYS   A 36  ? 0.36644 0.47280 0.24976 -0.03156 -0.02110 0.02545  141 LYS   A CB   
171  C  CG   . LYS   A 36  ? 0.47125 0.60017 0.33776 -0.03833 -0.01966 0.03580  141 LYS   A CG   
172  C  CD   . LYS   A 36  ? 0.56729 0.72743 0.42336 -0.04162 -0.02127 0.02116  141 LYS   A CD   
173  C  CE   . LYS   A 36  ? 0.63404 0.82054 0.47111 -0.04777 -0.02243 0.03592  141 LYS   A CE   
174  N  NZ   . LYS   A 36  ? 0.71667 0.89473 0.54991 -0.05235 -0.01701 0.05577  141 LYS   A NZ   
175  N  N    . THR   A 37  ? 0.34145 0.38827 0.25646 -0.02153 -0.01749 0.02005  142 THR   A N    
176  C  CA   . THR   A 37  ? 0.28882 0.32364 0.21576 -0.01616 -0.01952 0.01415  142 THR   A CA   
177  C  C    . THR   A 37  ? 0.36276 0.37534 0.29617 -0.01461 -0.01566 0.01793  142 THR   A C    
178  O  O    . THR   A 37  ? 0.39421 0.39861 0.33633 -0.01050 -0.01654 0.01434  142 THR   A O    
179  C  CB   . THR   A 37  ? 0.32875 0.36971 0.26155 -0.01673 -0.02004 -0.00227 142 THR   A CB   
180  O  OG1  . THR   A 37  ? 0.33336 0.37398 0.26505 -0.02084 -0.01507 -0.00793 142 THR   A OG1  
181  C  CG2  . THR   A 37  ? 0.33018 0.39160 0.25977 -0.01750 -0.02441 -0.00974 142 THR   A CG2  
182  N  N    . TYR   A 38  ? 0.36564 0.36937 0.29535 -0.01855 -0.01120 0.02432  143 TYR   A N    
183  C  CA   . TYR   A 38  ? 0.35677 0.33958 0.29256 -0.01799 -0.00751 0.02589  143 TYR   A CA   
184  C  C    . TYR   A 38  ? 0.38201 0.35397 0.31815 -0.01723 -0.00666 0.04070  143 TYR   A C    
185  O  O    . TYR   A 38  ? 0.42028 0.39528 0.35028 -0.02270 -0.00509 0.04917  143 TYR   A O    
186  C  CB   . TYR   A 38  ? 0.34685 0.32639 0.28192 -0.02433 -0.00317 0.01848  143 TYR   A CB   
187  C  CG   . TYR   A 38  ? 0.31204 0.27318 0.25286 -0.02457 -0.00006 0.01563  143 TYR   A CG   
188  C  CD1  . TYR   A 38  ? 0.37190 0.31695 0.31438 -0.02665 0.00318  0.02272  143 TYR   A CD1  
189  C  CD2  . TYR   A 38  ? 0.32401 0.28453 0.26902 -0.02325 -0.00044 0.00575  143 TYR   A CD2  
190  C  CE1  . TYR   A 38  ? 0.35943 0.28871 0.30705 -0.02744 0.00632  0.01694  143 TYR   A CE1  
191  C  CE2  . TYR   A 38  ? 0.31647 0.26411 0.26441 -0.02438 0.00245  0.00189  143 TYR   A CE2  
192  C  CZ   . TYR   A 38  ? 0.34526 0.27747 0.29426 -0.02645 0.00601  0.00594  143 TYR   A CZ   
193  O  OH   . TYR   A 38  ? 0.37591 0.29622 0.32780 -0.02808 0.00918  -0.00108 143 TYR   A OH   
194  N  N    . ASP   A 39  ? 0.32944 0.28923 0.27453 -0.01041 -0.00741 0.04431  144 ASP   A N    
195  C  CA   . ASP   A 39  ? 0.39995 0.34693 0.35050 -0.00759 -0.00708 0.05861  144 ASP   A CA   
196  C  C    . ASP   A 39  ? 0.46576 0.38921 0.42377 -0.00908 -0.00120 0.05448  144 ASP   A C    
197  O  O    . ASP   A 39  ? 0.44470 0.35910 0.41073 -0.00408 0.00067  0.04605  144 ASP   A O    
198  C  CB   . ASP   A 39  ? 0.37947 0.32981 0.33855 0.00195  -0.01162 0.06452  144 ASP   A CB   
199  C  CG   . ASP   A 39  ? 0.48450 0.41976 0.45427 0.00702  -0.01152 0.07955  144 ASP   A CG   
200  O  OD1  . ASP   A 39  ? 0.44346 0.36587 0.41295 0.00222  -0.00860 0.08752  144 ASP   A OD1  
201  O  OD2  . ASP   A 39  ? 0.50916 0.44568 0.48985 0.01594  -0.01452 0.08394  144 ASP   A OD2  
202  N  N    . PRO   A 40  ? 0.45007 0.36442 0.40606 -0.01659 0.00212  0.05927  145 PRO   A N    
203  C  CA   . PRO   A 40  ? 0.45719 0.34927 0.42089 -0.01948 0.00743  0.05300  145 PRO   A CA   
204  C  C    . PRO   A 40  ? 0.45654 0.32746 0.43486 -0.01256 0.00871  0.05950  145 PRO   A C    
205  O  O    . PRO   A 40  ? 0.47929 0.33047 0.46553 -0.01479 0.01344  0.05217  145 PRO   A O    
206  C  CB   . PRO   A 40  ? 0.44313 0.33490 0.40156 -0.03068 0.00986  0.05814  145 PRO   A CB   
207  C  CG   . PRO   A 40  ? 0.45066 0.35778 0.40214 -0.03118 0.00636  0.07429  145 PRO   A CG   
208  C  CD   . PRO   A 40  ? 0.42986 0.35584 0.37654 -0.02378 0.00141  0.07037  145 PRO   A CD   
209  N  N    . THR   A 41  ? 0.45642 0.33150 0.44001 -0.00423 0.00449  0.07231  146 THR   A N    
210  C  CA   . THR   A 41  ? 0.44332 0.29971 0.44485 0.00482  0.00557  0.07729  146 THR   A CA   
211  C  C    . THR   A 41  ? 0.46634 0.32463 0.47493 0.01352  0.00705  0.06337  146 THR   A C    
212  O  O    . THR   A 41  ? 0.43964 0.28146 0.46443 0.02071  0.01046  0.06074  146 THR   A O    
213  C  CB   . THR   A 41  ? 0.52127 0.38297 0.52798 0.01041  -0.00036 0.09970  146 THR   A CB   
214  O  OG1  . THR   A 41  ? 0.49377 0.37939 0.49558 0.01623  -0.00606 0.10005  146 THR   A OG1  
215  C  CG2  . THR   A 41  ? 0.62577 0.49258 0.62199 0.00059  -0.00195 0.11512  146 THR   A CG2  
216  N  N    . TYR   A 42  ? 0.44075 0.31914 0.43901 0.01286  0.00494  0.05453  147 TYR   A N    
217  C  CA   . TYR   A 42  ? 0.39072 0.27492 0.39418 0.01919  0.00642  0.04262  147 TYR   A CA   
218  C  C    . TYR   A 42  ? 0.45741 0.34227 0.47679 0.03097  0.00457  0.05059  147 TYR   A C    
219  O  O    . TYR   A 42  ? 0.42970 0.31296 0.45936 0.03736  0.00845  0.04124  147 TYR   A O    
220  C  CB   . TYR   A 42  ? 0.39384 0.26487 0.39887 0.01622  0.01359  0.02612  147 TYR   A CB   
221  C  CG   . TYR   A 42  ? 0.38784 0.25995 0.37936 0.00465  0.01450  0.01953  147 TYR   A CG   
222  C  CD1  . TYR   A 42  ? 0.50146 0.35635 0.49408 -0.00221 0.01804  0.01815  147 TYR   A CD1  
223  C  CD2  . TYR   A 42  ? 0.36268 0.25332 0.34289 0.00061  0.01151  0.01513  147 TYR   A CD2  
224  C  CE1  . TYR   A 42  ? 0.46396 0.32286 0.44604 -0.01290 0.01852  0.01246  147 TYR   A CE1  
225  C  CE2  . TYR   A 42  ? 0.44226 0.33578 0.41309 -0.00879 0.01200  0.00973  147 TYR   A CE2  
226  C  CZ   . TYR   A 42  ? 0.45300 0.33203 0.42443 -0.01556 0.01545  0.00847  147 TYR   A CZ   
227  O  OH   . TYR   A 42  ? 0.43426 0.31898 0.39811 -0.02501 0.01564  0.00329  147 TYR   A OH   
228  N  N    . ALA   A 43  ? 0.46062 0.35072 0.48222 0.03372  -0.00144 0.06831  148 ALA   A N    
229  C  CA   . ALA   A 43  ? 0.47027 0.36138 0.50972 0.04538  -0.00433 0.07899  148 ALA   A CA   
230  C  C    . ALA   A 43  ? 0.46169 0.37262 0.50516 0.05114  -0.00632 0.07213  148 ALA   A C    
231  O  O    . ALA   A 43  ? 0.52969 0.43919 0.59145 0.06123  -0.00450 0.07155  148 ALA   A O    
232  C  CB   . ALA   A 43  ? 0.45269 0.35106 0.49052 0.04551  -0.01200 0.10124  148 ALA   A CB   
233  N  N    . ASP   A 44  ? 0.39103 0.32073 0.41975 0.04479  -0.00975 0.06664  149 ASP   A N    
234  C  CA   . ASP   A 44  ? 0.37966 0.32867 0.41311 0.04844  -0.01241 0.06161  149 ASP   A CA   
235  C  C    . ASP   A 44  ? 0.41252 0.35712 0.45380 0.05115  -0.00480 0.04717  149 ASP   A C    
236  O  O    . ASP   A 44  ? 0.37086 0.33048 0.42092 0.05538  -0.00573 0.04473  149 ASP   A O    
237  C  CB   . ASP   A 44  ? 0.41610 0.38285 0.43396 0.04018  -0.01746 0.05771  149 ASP   A CB   
238  C  CG   . ASP   A 44  ? 0.49432 0.47219 0.50301 0.03721  -0.02485 0.07005  149 ASP   A CG   
239  O  OD1  . ASP   A 44  ? 0.52887 0.50942 0.54580 0.04319  -0.02908 0.08460  149 ASP   A OD1  
240  O  OD2  . ASP   A 44  ? 0.52300 0.50873 0.51677 0.02904  -0.02646 0.06533  149 ASP   A OD2  
241  N  N    . PHE   A 45  ? 0.35916 0.28590 0.39738 0.04801  0.00267  0.03751  150 PHE   A N    
242  C  CA   . PHE   A 45  ? 0.38757 0.31310 0.43075 0.04963  0.01034  0.02309  150 PHE   A CA   
243  C  C    . PHE   A 45  ? 0.37222 0.29928 0.43684 0.06154  0.01353  0.02375  150 PHE   A C    
244  O  O    . PHE   A 45  ? 0.40211 0.33807 0.47187 0.06369  0.01902  0.01338  150 PHE   A O    
245  C  CB   . PHE   A 45  ? 0.39704 0.30365 0.43367 0.04394  0.01717  0.01240  150 PHE   A CB   
246  C  CG   . PHE   A 45  ? 0.39322 0.30318 0.41100 0.03245  0.01568  0.00749  150 PHE   A CG   
247  C  CD1  . PHE   A 45  ? 0.36093 0.27968 0.36888 0.02769  0.00873  0.01585  150 PHE   A CD1  
248  C  CD2  . PHE   A 45  ? 0.40527 0.31149 0.41607 0.02662  0.02123  -0.00607 150 PHE   A CD2  
249  C  CE1  . PHE   A 45  ? 0.37369 0.29604 0.36796 0.01850  0.00778  0.01075  150 PHE   A CE1  
250  C  CE2  . PHE   A 45  ? 0.37216 0.28289 0.36846 0.01695  0.01914  -0.00931 150 PHE   A CE2  
251  C  CZ   . PHE   A 45  ? 0.37980 0.29791 0.36921 0.01347  0.01261  -0.00087 150 PHE   A CZ   
252  N  N    A ARG   A 46  ? 0.41607 0.33641 0.49438 0.06943  0.01027  0.03661  151 ARG   A N    
253  N  N    B ARG   A 46  ? 0.43086 0.35115 0.50912 0.06941  0.01028  0.03660  151 ARG   A N    
254  C  CA   A ARG   A 46  ? 0.48316 0.40654 0.58575 0.08231  0.01257  0.03850  151 ARG   A CA   
255  C  CA   B ARG   A 46  ? 0.48217 0.40555 0.58473 0.08230  0.01253  0.03857  151 ARG   A CA   
256  C  C    A ARG   A 46  ? 0.44927 0.40042 0.55760 0.08538  0.00829  0.04101  151 ARG   A C    
257  C  C    B ARG   A 46  ? 0.45015 0.40131 0.55829 0.08526  0.00842  0.04071  151 ARG   A C    
258  O  O    A ARG   A 46  ? 0.46751 0.42657 0.59600 0.09510  0.01199  0.03863  151 ARG   A O    
259  O  O    B ARG   A 46  ? 0.46514 0.42424 0.59307 0.09476  0.01239  0.03777  151 ARG   A O    
260  C  CB   A ARG   A 46  ? 0.56330 0.47399 0.68062 0.09001  0.00819  0.05530  151 ARG   A CB   
261  C  CB   B ARG   A 46  ? 0.56508 0.47641 0.68210 0.08990  0.00786  0.05573  151 ARG   A CB   
262  C  CG   A ARG   A 46  ? 0.62674 0.55395 0.73867 0.08892  -0.00375 0.07440  151 ARG   A CG   
263  C  CG   B ARG   A 46  ? 0.62396 0.55395 0.73732 0.08976  -0.00403 0.07432  151 ARG   A CG   
264  C  CD   A ARG   A 46  ? 0.69967 0.62426 0.83439 0.10079  -0.00857 0.09252  151 ARG   A CD   
265  C  CD   B ARG   A 46  ? 0.68978 0.61745 0.82643 0.10189  -0.00872 0.09209  151 ARG   A CD   
266  N  NE   A ARG   A 46  ? 0.71093 0.66020 0.84241 0.10088  -0.02047 0.10909  151 ARG   A NE   
267  N  NE   B ARG   A 46  ? 0.70345 0.65026 0.83361 0.10024  -0.02093 0.11114  151 ARG   A NE   
268  C  CZ   A ARG   A 46  ? 0.68304 0.65600 0.82812 0.10782  -0.02503 0.11195  151 ARG   A CZ   
269  C  CZ   B ARG   A 46  ? 0.68070 0.62596 0.79157 0.09108  -0.02611 0.12129  151 ARG   A CZ   
270  N  NH1  A ARG   A 46  ? 0.65023 0.64652 0.79060 0.10626  -0.03663 0.12611  151 ARG   A NH1  
271  N  NH1  B ARG   A 46  ? 0.65351 0.62058 0.75818 0.08972  -0.03696 0.13711  151 ARG   A NH1  
272  N  NH2  A ARG   A 46  ? 0.66683 0.64245 0.83020 0.11565  -0.01786 0.10008  151 ARG   A NH2  
273  N  NH2  B ARG   A 46  ? 0.64459 0.56901 0.74245 0.08280  -0.02039 0.11534  151 ARG   A NH2  
274  N  N    . ASP   A 47  ? 0.39253 0.35906 0.48554 0.07718  0.00089  0.04484  152 ASP   A N    
275  C  CA   . ASP   A 47  ? 0.46397 0.45621 0.56280 0.07790  -0.00370 0.04624  152 ASP   A CA   
276  C  C    . ASP   A 47  ? 0.39724 0.39806 0.49326 0.07336  0.00291  0.03252  152 ASP   A C    
277  O  O    . ASP   A 47  ? 0.37709 0.39847 0.48304 0.07463  0.00135  0.03284  152 ASP   A O    
278  C  CB   . ASP   A 47  ? 0.48400 0.48886 0.56908 0.07043  -0.01434 0.05400  152 ASP   A CB   
279  C  CG   . ASP   A 47  ? 0.59782 0.60135 0.68416 0.07398  -0.02191 0.07002  152 ASP   A CG   
280  O  OD1  . ASP   A 47  ? 0.61159 0.61060 0.71625 0.08445  -0.02147 0.07854  152 ASP   A OD1  
281  O  OD2  . ASP   A 47  ? 0.61873 0.62692 0.68852 0.06641  -0.02822 0.07448  152 ASP   A OD2  
282  N  N    . PHE   A 48  ? 0.36830 0.35577 0.45146 0.06735  0.00976  0.02167  153 PHE   A N    
283  C  CA   . PHE   A 48  ? 0.28274 0.28029 0.36096 0.06183  0.01521  0.01116  153 PHE   A CA   
284  C  C    . PHE   A 48  ? 0.28961 0.29468 0.38465 0.06978  0.02430  0.00421  153 PHE   A C    
285  O  O    . PHE   A 48  ? 0.35400 0.34962 0.46349 0.07955  0.02834  0.00355  153 PHE   A O    
286  C  CB   . PHE   A 48  ? 0.29198 0.27598 0.35153 0.05304  0.01911  0.00234  153 PHE   A CB   
287  C  CG   . PHE   A 48  ? 0.36137 0.33819 0.40573 0.04563  0.01193  0.00734  153 PHE   A CG   
288  C  CD1  . PHE   A 48  ? 0.32084 0.28380 0.35140 0.03898  0.01461  0.00131  153 PHE   A CD1  
289  C  CD2  . PHE   A 48  ? 0.35804 0.34429 0.40224 0.04488  0.00284  0.01676  153 PHE   A CD2  
290  C  CE1  . PHE   A 48  ? 0.32976 0.28855 0.34816 0.03250  0.00907  0.00519  153 PHE   A CE1  
291  C  CE2  . PHE   A 48  ? 0.33909 0.32112 0.36952 0.03824  -0.00239 0.01931  153 PHE   A CE2  
292  C  CZ   . PHE   A 48  ? 0.34990 0.31834 0.36810 0.03238  0.00108  0.01380  153 PHE   A CZ   
293  N  N    . ARG   A 49  ? 0.28062 0.30348 0.37511 0.06548  0.02787  -0.00082 154 ARG   A N    
294  C  CA   . ARG   A 49  ? 0.31038 0.34241 0.41620 0.07068  0.03889  -0.01053 154 ARG   A CA   
295  C  C    . ARG   A 49  ? 0.33625 0.34950 0.43363 0.07045  0.04749  -0.02348 154 ARG   A C    
296  O  O    . ARG   A 49  ? 0.35937 0.36047 0.43763 0.06167  0.04573  -0.02606 154 ARG   A O    
297  C  CB   . ARG   A 49  ? 0.30890 0.36387 0.41157 0.06318  0.04137  -0.01217 154 ARG   A CB   
298  C  CG   . ARG   A 49  ? 0.33490 0.41085 0.45279 0.06438  0.03504  -0.00206 154 ARG   A CG   
299  C  CD   . ARG   A 49  ? 0.34216 0.43703 0.45595 0.05413  0.03562  -0.00087 154 ARG   A CD   
300  N  NE   . ARG   A 49  ? 0.34670 0.43231 0.44286 0.04353  0.02808  0.00261  154 ARG   A NE   
301  C  CZ   . ARG   A 49  ? 0.31467 0.41022 0.40511 0.03352  0.02754  0.00478  154 ARG   A CZ   
302  N  NH1  . ARG   A 49  ? 0.32111 0.43749 0.41994 0.03151  0.03429  0.00482  154 ARG   A NH1  
303  N  NH2  . ARG   A 49  ? 0.28573 0.37113 0.36351 0.02564  0.02052  0.00755  154 ARG   A NH2  
304  N  N    . PRO   A 50  ? 0.37381 0.38463 0.48689 0.08005  0.05676  -0.03275 155 PRO   A N    
305  C  CA   . PRO   A 50  ? 0.39232 0.38108 0.50121 0.08066  0.06375  -0.04574 155 PRO   A CA   
306  C  C    . PRO   A 50  ? 0.44634 0.44001 0.53383 0.06932  0.06948  -0.05854 155 PRO   A C    
307  O  O    . PRO   A 50  ? 0.39143 0.40879 0.47436 0.06499  0.07309  -0.06092 155 PRO   A O    
308  C  CB   . PRO   A 50  ? 0.38939 0.37937 0.52431 0.09446  0.07307  -0.05437 155 PRO   A CB   
309  C  CG   . PRO   A 50  ? 0.42324 0.44338 0.57098 0.09824  0.07356  -0.04904 155 PRO   A CG   
310  C  CD   . PRO   A 50  ? 0.36040 0.38775 0.49918 0.09157  0.06055  -0.03167 155 PRO   A CD   
311  N  N    . PRO   A 51  ? 0.40171 0.37532 0.47599 0.06350  0.07012  -0.06599 156 PRO   A N    
312  C  CA   . PRO   A 51  ? 0.45562 0.43590 0.51108 0.05339  0.07591  -0.07979 156 PRO   A CA   
313  C  C    . PRO   A 51  ? 0.47407 0.46394 0.53830 0.05856  0.08917  -0.09826 156 PRO   A C    
314  O  O    . PRO   A 51  ? 0.47692 0.45455 0.56126 0.06954  0.09469  -0.10541 156 PRO   A O    
315  C  CB   . PRO   A 51  ? 0.45007 0.40525 0.49464 0.04732  0.07285  -0.08323 156 PRO   A CB   
316  C  CG   . PRO   A 51  ? 0.51417 0.44684 0.57803 0.05745  0.07143  -0.07806 156 PRO   A CG   
317  C  CD   . PRO   A 51  ? 0.45758 0.40283 0.53589 0.06603  0.06633  -0.06251 156 PRO   A CD   
318  N  N    . VAL   A 52  ? 0.43972 0.45290 0.48967 0.05070  0.09440  -0.10567 157 VAL   A N    
319  C  CA   . VAL   A 52  ? 0.46221 0.49056 0.51610 0.05346  0.10807  -0.12514 157 VAL   A CA   
320  C  C    . VAL   A 52  ? 0.50404 0.54073 0.53206 0.04015  0.11103  -0.13733 157 VAL   A C    
321  O  O    . VAL   A 52  ? 0.45352 0.50603 0.46379 0.02972  0.10531  -0.12667 157 VAL   A O    
322  C  CB   . VAL   A 52  ? 0.45358 0.51285 0.51841 0.05768  0.11288  -0.12016 157 VAL   A CB   
323  C  CG1  . VAL   A 52  ? 0.43681 0.51668 0.50180 0.05858  0.12816  -0.14158 157 VAL   A CG1  
324  C  CG2  . VAL   A 52  ? 0.41265 0.46618 0.50518 0.07130  0.10967  -0.10934 157 VAL   A CG2  
325  N  N    . ARG   A 53  ? 0.58434 0.61052 0.61149 0.04032  0.11930  -0.15938 158 ARG   A N    
326  C  CA   . ARG   A 53  ? 0.68576 0.72181 0.68870 0.02747  0.12233  -0.17393 158 ARG   A CA   
327  C  C    . ARG   A 53  ? 0.81828 0.87866 0.82257 0.02957  0.13732  -0.19561 158 ARG   A C    
328  O  O    . ARG   A 53  ? 0.86488 0.91265 0.88235 0.03641  0.14675  -0.21738 158 ARG   A O    
329  C  CB   . ARG   A 53  ? 0.67831 0.68386 0.67780 0.02351  0.11925  -0.18387 158 ARG   A CB   
330  C  CG   . ARG   A 53  ? 0.61354 0.60506 0.60304 0.01653  0.10520  -0.16421 158 ARG   A CG   
331  C  CD   . ARG   A 53  ? 0.59962 0.55723 0.60708 0.02418  0.10040  -0.15679 158 ARG   A CD   
332  N  NE   . ARG   A 53  ? 0.58617 0.53362 0.58346 0.01707  0.08840  -0.13992 158 ARG   A NE   
333  C  CZ   . ARG   A 53  ? 0.52521 0.45258 0.53373 0.02221  0.08166  -0.12506 158 ARG   A CZ   
334  N  NH1  . ARG   A 53  ? 0.47616 0.39052 0.50694 0.03463  0.08447  -0.12283 158 ARG   A NH1  
335  N  NH2  . ARG   A 53  ? 0.48494 0.40717 0.48295 0.01503  0.07210  -0.11207 158 ARG   A NH2  
336  N  N    . MET   A 54  ? 0.90715 1.00279 0.89927 0.02364  0.13986  -0.18956 159 MET   A N    
337  C  CA   . MET   A 54  ? 1.00117 1.12680 0.99395 0.02518  0.15482  -0.20771 159 MET   A CA   
338  C  C    . MET   A 54  ? 1.04142 1.20400 1.00633 0.01043  0.15554  -0.20375 159 MET   A C    
339  O  O    . MET   A 54  ? 1.07282 1.24460 1.02861 0.00355  0.14548  -0.17951 159 MET   A O    
340  C  CB   . MET   A 54  ? 1.01051 1.14599 1.03056 0.03878  0.16032  -0.20116 159 MET   A CB   
341  C  CG   . MET   A 54  ? 1.06018 1.21491 1.07933 0.03531  0.15244  -0.17351 159 MET   A CG   
342  S  SD   . MET   A 54  ? 1.13574 1.30847 1.18727 0.04926  0.15890  -0.16670 159 MET   A SD   
343  C  CE   . MET   A 54  ? 1.14607 1.32489 1.21311 0.06032  0.17831  -0.20056 159 MET   A CE   
344  N  N    . SER   A 66  ? 1.02347 1.35024 0.89980 -0.04820 0.14713  -0.12998 218 SER   A N    
345  C  CA   . SER   A 66  ? 0.99928 1.33550 0.88135 -0.05287 0.13848  -0.09797 218 SER   A CA   
346  C  C    . SER   A 66  ? 0.97593 1.28049 0.88485 -0.04249 0.13008  -0.08435 218 SER   A C    
347  O  O    . SER   A 66  ? 0.97432 1.26803 0.88500 -0.04669 0.11690  -0.06178 218 SER   A O    
348  C  CB   . SER   A 66  ? 1.01225 1.39235 0.89320 -0.05786 0.15012  -0.09253 218 SER   A CB   
349  O  OG   . SER   A 66  ? 0.99529 1.39223 0.87007 -0.06927 0.14108  -0.06199 218 SER   A OG   
350  N  N    . PRO   A 67  ? 0.93198 1.22312 0.86249 -0.02910 0.13718  -0.09761 219 PRO   A N    
351  C  CA   . PRO   A 67  ? 0.84819 1.11435 0.80262 -0.02024 0.12862  -0.08391 219 PRO   A CA   
352  C  C    . PRO   A 67  ? 0.72722 0.95626 0.67906 -0.01908 0.11502  -0.07974 219 PRO   A C    
353  O  O    . PRO   A 67  ? 0.76045 0.97416 0.70061 -0.01950 0.11496  -0.09471 219 PRO   A O    
354  C  CB   . PRO   A 67  ? 0.88149 1.14414 0.85786 -0.00593 0.13980  -0.10149 219 PRO   A CB   
355  C  CG   . PRO   A 67  ? 0.95971 1.22677 0.92325 -0.00565 0.15103  -0.12874 219 PRO   A CG   
356  C  CD   . PRO   A 67  ? 0.97947 1.27964 0.91616 -0.02093 0.15321  -0.12490 219 PRO   A CD   
357  N  N    . LEU   A 68  ? 0.58153 0.79754 0.54525 -0.01822 0.10374  -0.05987 220 LEU   A N    
358  C  CA   . LEU   A 68  ? 0.41455 0.59825 0.37806 -0.01681 0.09112  -0.05445 220 LEU   A CA   
359  C  C    . LEU   A 68  ? 0.34257 0.50129 0.32429 -0.00360 0.09166  -0.06281 220 LEU   A C    
360  O  O    . LEU   A 68  ? 0.33249 0.47950 0.32915 0.00118  0.08425  -0.05135 220 LEU   A O    
361  C  CB   . LEU   A 68  ? 0.46498 0.64852 0.43240 -0.02274 0.07923  -0.03102 220 LEU   A CB   
362  C  CG   . LEU   A 68  ? 0.48899 0.69755 0.44268 -0.03549 0.07763  -0.01776 220 LEU   A CG   
363  C  CD1  . LEU   A 68  ? 0.48590 0.68593 0.44680 -0.04016 0.06448  0.00389  220 LEU   A CD1  
364  C  CD2  . LEU   A 68  ? 0.50800 0.72133 0.43795 -0.04195 0.07892  -0.02797 220 LEU   A CD2  
365  N  N    . SER   A 69  ? 0.35704 0.50809 0.33759 0.00190  0.10036  -0.08338 221 SER   A N    
366  C  CA   . SER   A 69  ? 0.42408 0.55549 0.42498 0.01538  0.10314  -0.09140 221 SER   A CA   
367  C  C    . SER   A 69  ? 0.44191 0.54178 0.44692 0.01856  0.09146  -0.08306 221 SER   A C    
368  O  O    . SER   A 69  ? 0.41624 0.50321 0.44005 0.02902  0.09012  -0.08071 221 SER   A O    
369  C  CB   . SER   A 69  ? 0.46642 0.59464 0.46670 0.01988  0.11525  -0.11633 221 SER   A CB   
370  O  OG   . SER   A 69  ? 0.50421 0.61510 0.48748 0.01343  0.11214  -0.12553 221 SER   A OG   
371  N  N    . MET   A 70  ? 0.35579 0.44533 0.34438 0.00989  0.08306  -0.07806 222 MET   A N    
372  C  CA   . MET   A 70  ? 0.31828 0.38154 0.30956 0.01187  0.07284  -0.07037 222 MET   A CA   
373  C  C    . MET   A 70  ? 0.29859 0.36506 0.29355 0.00934  0.06232  -0.05135 222 MET   A C    
374  O  O    . MET   A 70  ? 0.35871 0.40713 0.35571 0.01077  0.05403  -0.04495 222 MET   A O    
375  C  CB   . MET   A 70  ? 0.38507 0.43492 0.35935 0.00439  0.06993  -0.07723 222 MET   A CB   
376  C  CG   . MET   A 70  ? 0.42475 0.46086 0.39942 0.00746  0.07803  -0.09693 222 MET   A CG   
377  S  SD   . MET   A 70  ? 0.39273 0.39968 0.38959 0.02061  0.07775  -0.09680 222 MET   A SD   
378  C  CE   . MET   A 70  ? 0.42406 0.41137 0.41380 0.01542  0.06477  -0.08285 222 MET   A CE   
379  N  N    . LEU   A 71  ? 0.31536 0.40481 0.31195 0.00510  0.06283  -0.04273 223 LEU   A N    
380  C  CA   . LEU   A 71  ? 0.30038 0.39164 0.30276 0.00182  0.05287  -0.02621 223 LEU   A CA   
381  C  C    . LEU   A 71  ? 0.29454 0.37563 0.31403 0.01013  0.04806  -0.02139 223 LEU   A C    
382  O  O    . LEU   A 71  ? 0.33055 0.39967 0.35012 0.00867  0.03843  -0.01405 223 LEU   A O    
383  C  CB   . LEU   A 71  ? 0.30937 0.42716 0.31326 -0.00485 0.05519  -0.01733 223 LEU   A CB   
384  C  CG   . LEU   A 71  ? 0.32464 0.44353 0.33686 -0.00965 0.04502  -0.00087 223 LEU   A CG   
385  C  CD1  . LEU   A 71  ? 0.30527 0.40683 0.30823 -0.01376 0.03541  0.00288  223 LEU   A CD1  
386  C  CD2  . LEU   A 71  ? 0.33946 0.48366 0.35378 -0.01777 0.04751  0.00975  223 LEU   A CD2  
387  N  N    . PRO   A 72  ? 0.27658 0.36379 0.31133 0.01887  0.05384  -0.02501 224 PRO   A N    
388  C  CA   . PRO   A 72  ? 0.26450 0.34422 0.31485 0.02625  0.04736  -0.01858 224 PRO   A CA   
389  C  C    . PRO   A 72  ? 0.31055 0.36515 0.35569 0.02937  0.04157  -0.01945 224 PRO   A C    
390  O  O    . PRO   A 72  ? 0.28383 0.33261 0.33074 0.02863  0.03217  -0.01113 224 PRO   A O    
391  C  CB   . PRO   A 72  ? 0.29786 0.38919 0.36575 0.03605  0.05604  -0.02405 224 PRO   A CB   
392  C  CG   . PRO   A 72  ? 0.30854 0.42174 0.37187 0.03107  0.06601  -0.02949 224 PRO   A CG   
393  C  CD   . PRO   A 72  ? 0.30638 0.41164 0.34667 0.02232  0.06612  -0.03420 224 PRO   A CD   
394  N  N    . HIS   A 73  ? 0.33338 0.37387 0.37240 0.03208  0.04727  -0.02989 225 HIS   A N    
395  C  CA   . HIS   A 73  ? 0.34714 0.36419 0.38262 0.03421  0.04251  -0.02937 225 HIS   A CA   
396  C  C    . HIS   A 73  ? 0.35259 0.36340 0.37303 0.02505  0.03467  -0.02454 225 HIS   A C    
397  O  O    . HIS   A 73  ? 0.33237 0.33372 0.35295 0.02564  0.02728  -0.01777 225 HIS   A O    
398  C  CB   . HIS   A 73  ? 0.33228 0.33487 0.36620 0.03736  0.05065  -0.04246 225 HIS   A CB   
399  C  CG   . HIS   A 73  ? 0.35758 0.33585 0.38881 0.03806  0.04645  -0.04083 225 HIS   A CG   
400  N  ND1  . HIS   A 73  ? 0.33068 0.29827 0.37525 0.04640  0.04289  -0.03285 225 HIS   A ND1  
401  C  CD2  . HIS   A 73  ? 0.34105 0.30562 0.35839 0.03076  0.04512  -0.04484 225 HIS   A CD2  
402  C  CE1  . HIS   A 73  ? 0.36373 0.31157 0.40209 0.04378  0.04004  -0.03137 225 HIS   A CE1  
403  N  NE2  . HIS   A 73  ? 0.36466 0.31024 0.38712 0.03427  0.04154  -0.03922 225 HIS   A NE2  
404  N  N    . LEU   A 74  ? 0.30112 0.31916 0.30905 0.01668  0.03619  -0.02773 226 LEU   A N    
405  C  CA   . LEU   A 74  ? 0.29704 0.30989 0.29366 0.00902  0.02899  -0.02354 226 LEU   A CA   
406  C  C    . LEU   A 74  ? 0.24890 0.26963 0.25138 0.00689  0.02097  -0.01276 226 LEU   A C    
407  O  O    . LEU   A 74  ? 0.27458 0.28818 0.27316 0.00375  0.01416  -0.00938 226 LEU   A O    
408  C  CB   . LEU   A 74  ? 0.36698 0.38697 0.34997 0.00101  0.03201  -0.02886 226 LEU   A CB   
409  C  CG   . LEU   A 74  ? 0.40016 0.41004 0.37553 0.00078  0.03853  -0.04221 226 LEU   A CG   
410  C  CD1  . LEU   A 74  ? 0.39549 0.41583 0.35563 -0.00856 0.03967  -0.04716 226 LEU   A CD1  
411  C  CD2  . LEU   A 74  ? 0.35181 0.33963 0.32774 0.00267  0.03518  -0.04275 226 LEU   A CD2  
412  N  N    . ALA   A 75  ? 0.26801 0.30387 0.28134 0.00825  0.02195  -0.00833 227 ALA   A N    
413  C  CA   . ALA   A 75  ? 0.25423 0.29572 0.27644 0.00620  0.01407  0.00038  227 ALA   A CA   
414  C  C    . ALA   A 75  ? 0.25148 0.28426 0.27916 0.01150  0.00846  0.00191  227 ALA   A C    
415  O  O    . ALA   A 75  ? 0.27209 0.30193 0.29963 0.00858  0.00095  0.00486  227 ALA   A O    
416  C  CB   . ALA   A 75  ? 0.24174 0.30244 0.27620 0.00554  0.01672  0.00489  227 ALA   A CB   
417  N  N    . ASP   A 76  ? 0.25134 0.28107 0.28457 0.01942  0.01199  -0.00003 228 ASP   A N    
418  C  CA   . ASP   A 76  ? 0.24856 0.27172 0.28553 0.02426  0.00628  0.00372  228 ASP   A CA   
419  C  C    . ASP   A 76  ? 0.29520 0.30261 0.31890 0.02147  0.00359  0.00244  228 ASP   A C    
420  O  O    . ASP   A 76  ? 0.26027 0.26668 0.28218 0.02050  -0.00320 0.00609  228 ASP   A O    
421  C  CB   . ASP   A 76  ? 0.27478 0.29732 0.32288 0.03404  0.01062  0.00380  228 ASP   A CB   
422  C  CG   . ASP   A 76  ? 0.30876 0.35052 0.37363 0.03772  0.01169  0.00654  228 ASP   A CG   
423  O  OD1  . ASP   A 76  ? 0.30819 0.35240 0.38503 0.04626  0.01712  0.00508  228 ASP   A OD1  
424  O  OD2  . ASP   A 76  ? 0.27802 0.33256 0.34627 0.03207  0.00721  0.00996  228 ASP   A OD2  
425  N  N    . LEU   A 77  ? 0.25550 0.25265 0.26987 0.01947  0.00909  -0.00349 229 LEU   A N    
426  C  CA   . LEU   A 77  ? 0.26900 0.25310 0.27202 0.01561  0.00715  -0.00480 229 LEU   A CA   
427  C  C    . LEU   A 77  ? 0.32784 0.31679 0.32591 0.00912  0.00101  -0.00326 229 LEU   A C    
428  O  O    . LEU   A 77  ? 0.30172 0.28694 0.29604 0.00785  -0.00344 -0.00152 229 LEU   A O    
429  C  CB   . LEU   A 77  ? 0.28120 0.25638 0.27667 0.01316  0.01393  -0.01288 229 LEU   A CB   
430  C  CG   . LEU   A 77  ? 0.37259 0.33716 0.35698 0.00710  0.01255  -0.01524 229 LEU   A CG   
431  C  CD1  . LEU   A 77  ? 0.31572 0.26978 0.30084 0.00938  0.00973  -0.00989 229 LEU   A CD1  
432  C  CD2  . LEU   A 77  ? 0.40176 0.35984 0.38004 0.00387  0.01900  -0.02489 229 LEU   A CD2  
433  N  N    . VAL   A 78  ? 0.26902 0.26711 0.26814 0.00500  0.00101  -0.00363 230 VAL   A N    
434  C  CA   . VAL   A 78  ? 0.27933 0.28059 0.27802 -0.00029 -0.00480 -0.00199 230 VAL   A CA   
435  C  C    . VAL   A 78  ? 0.28485 0.29087 0.29205 0.00101  -0.01111 0.00070  230 VAL   A C    
436  O  O    . VAL   A 78  ? 0.28833 0.29232 0.29393 -0.00103 -0.01568 -0.00085 230 VAL   A O    
437  C  CB   . VAL   A 78  ? 0.33583 0.34610 0.33607 -0.00486 -0.00380 0.00001  230 VAL   A CB   
438  C  CG1  . VAL   A 78  ? 0.34051 0.35364 0.34735 -0.00883 -0.01064 0.00363  230 VAL   A CG1  
439  C  CG2  . VAL   A 78  ? 0.32018 0.32808 0.30901 -0.00799 0.00071  -0.00399 230 VAL   A CG2  
440  N  N    . SER   A 79  ? 0.26653 0.28093 0.28356 0.00414  -0.01129 0.00357  231 SER   A N    
441  C  CA   . SER   A 79  ? 0.23650 0.25778 0.26183 0.00455  -0.01789 0.00500  231 SER   A CA   
442  C  C    . SER   A 79  ? 0.25509 0.27207 0.27337 0.00697  -0.02076 0.00432  231 SER   A C    
443  O  O    . SER   A 79  ? 0.24189 0.26219 0.25979 0.00445  -0.02627 0.00187  231 SER   A O    
444  C  CB   . SER   A 79  ? 0.25606 0.28905 0.29386 0.00771  -0.01723 0.00860  231 SER   A CB   
445  O  OG   . SER   A 79  ? 0.31076 0.35330 0.35874 0.00543  -0.02428 0.00921  231 SER   A OG   
446  N  N    . TYR   A 80  ? 0.23089 0.24106 0.24422 0.01153  -0.01682 0.00641  232 TYR   A N    
447  C  CA   . TYR   A 80  ? 0.24019 0.24617 0.24613 0.01297  -0.01902 0.00876  232 TYR   A CA   
448  C  C    . TYR   A 80  ? 0.30163 0.30280 0.29729 0.00753  -0.01978 0.00450  232 TYR   A C    
449  O  O    . TYR   A 80  ? 0.24946 0.25589 0.24078 0.00590  -0.02391 0.00412  232 TYR   A O    
450  C  CB   . TYR   A 80  ? 0.25546 0.25107 0.26087 0.01824  -0.01382 0.01235  232 TYR   A CB   
451  C  CG   . TYR   A 80  ? 0.29930 0.28866 0.29786 0.01908  -0.01533 0.01788  232 TYR   A CG   
452  C  CD1  . TYR   A 80  ? 0.30251 0.30022 0.30460 0.02298  -0.02052 0.02620  232 TYR   A CD1  
453  C  CD2  . TYR   A 80  ? 0.32042 0.29733 0.30946 0.01527  -0.01181 0.01606  232 TYR   A CD2  
454  C  CE1  . TYR   A 80  ? 0.38489 0.37861 0.38018 0.02299  -0.02204 0.03402  232 TYR   A CE1  
455  C  CE2  . TYR   A 80  ? 0.37510 0.34708 0.35857 0.01485  -0.01274 0.02297  232 TYR   A CE2  
456  C  CZ   . TYR   A 80  ? 0.40714 0.38748 0.39329 0.01872  -0.01777 0.03270  232 TYR   A CZ   
457  O  OH   . TYR   A 80  ? 0.47748 0.45469 0.45755 0.01756  -0.01889 0.04223  232 TYR   A OH   
458  N  N    . SER   A 81  ? 0.28829 0.28212 0.28025 0.00449  -0.01578 0.00083  233 SER   A N    
459  C  CA   . SER   A 81  ? 0.31499 0.30575 0.29971 -0.00015 -0.01619 -0.00300 233 SER   A CA   
460  C  C    . SER   A 81  ? 0.29538 0.29449 0.28529 -0.00273 -0.02130 -0.00708 233 SER   A C    
461  O  O    . SER   A 81  ? 0.29557 0.29677 0.28151 -0.00487 -0.02271 -0.01083 233 SER   A O    
462  C  CB   . SER   A 81  ? 0.33021 0.31426 0.31143 -0.00300 -0.01186 -0.00557 233 SER   A CB   
463  O  OG   . SER   A 81  ? 0.37133 0.35264 0.34631 -0.00700 -0.01166 -0.00835 233 SER   A OG   
464  N  N    . ILE   A 82  ? 0.26516 0.26931 0.26547 -0.00281 -0.02365 -0.00692 234 ILE   A N    
465  C  CA   . ILE   A 82  ? 0.27169 0.28139 0.28076 -0.00526 -0.02878 -0.01154 234 ILE   A CA   
466  C  C    . ILE   A 82  ? 0.28357 0.30074 0.29032 -0.00480 -0.03255 -0.01529 234 ILE   A C    
467  O  O    . ILE   A 82  ? 0.24863 0.26901 0.25590 -0.00686 -0.03473 -0.02274 234 ILE   A O    
468  C  CB   . ILE   A 82  ? 0.24680 0.26036 0.26928 -0.00632 -0.03071 -0.00879 234 ILE   A CB   
469  C  CG1  . ILE   A 82  ? 0.28324 0.29306 0.30676 -0.00835 -0.02774 -0.00487 234 ILE   A CG1  
470  C  CG2  . ILE   A 82  ? 0.25892 0.27670 0.29360 -0.00891 -0.03663 -0.01434 234 ILE   A CG2  
471  C  CD1  . ILE   A 82  ? 0.33686 0.35247 0.37183 -0.01012 -0.02817 0.00076  234 ILE   A CD1  
472  N  N    . GLN   A 83  ? 0.25886 0.28086 0.26355 -0.00193 -0.03337 -0.01039 235 GLN   A N    
473  C  CA   . GLN   A 83  ? 0.29215 0.32479 0.29226 -0.00201 -0.03765 -0.01205 235 GLN   A CA   
474  C  C    . GLN   A 83  ? 0.30106 0.33291 0.28783 -0.00348 -0.03548 -0.01371 235 GLN   A C    
475  O  O    . GLN   A 83  ? 0.28567 0.32787 0.26863 -0.00599 -0.03821 -0.02043 235 GLN   A O    
476  C  CB   . GLN   A 83  ? 0.30351 0.34180 0.30456 0.00218  -0.03915 -0.00327 235 GLN   A CB   
477  C  CG   . GLN   A 83  ? 0.30555 0.34912 0.32119 0.00337  -0.04104 -0.00159 235 GLN   A CG   
478  C  CD   . GLN   A 83  ? 0.39524 0.44720 0.41457 0.00851  -0.04297 0.00693  235 GLN   A CD   
479  O  OE1  . GLN   A 83  ? 0.42566 0.48814 0.44023 0.00899  -0.04799 0.00949  235 GLN   A OE1  
480  N  NE2  . GLN   A 83  ? 0.44609 0.49551 0.47451 0.01253  -0.03899 0.01157  235 GLN   A NE2  
481  N  N    . LYS   A 84  ? 0.28247 0.30349 0.26244 -0.00264 -0.03021 -0.00850 236 LYS   A N    
482  C  CA   . LYS   A 84  ? 0.29766 0.31845 0.26646 -0.00521 -0.02755 -0.00885 236 LYS   A CA   
483  C  C    . LYS   A 84  ? 0.29343 0.31658 0.26442 -0.00855 -0.02693 -0.01923 236 LYS   A C    
484  O  O    . LYS   A 84  ? 0.30801 0.34039 0.27283 -0.01099 -0.02659 -0.02399 236 LYS   A O    
485  C  CB   . LYS   A 84  ? 0.28532 0.29248 0.24946 -0.00456 -0.02224 -0.00175 236 LYS   A CB   
486  C  CG   . LYS   A 84  ? 0.37428 0.37730 0.33958 0.00006  -0.02227 0.00828  236 LYS   A CG   
487  C  CD   . LYS   A 84  ? 0.42273 0.43878 0.38356 0.00082  -0.02701 0.01438  236 LYS   A CD   
488  C  CE   . LYS   A 84  ? 0.47398 0.48340 0.43535 0.00508  -0.02638 0.02763  236 LYS   A CE   
489  N  NZ   . LYS   A 84  ? 0.45295 0.44913 0.40822 0.00232  -0.02119 0.03223  236 LYS   A NZ   
490  N  N    . VAL   A 85  ? 0.25250 0.26912 0.23323 -0.00851 -0.02673 -0.02230 237 VAL   A N    
491  C  CA   . VAL   A 85  ? 0.32054 0.33878 0.30771 -0.01036 -0.02686 -0.03077 237 VAL   A CA   
492  C  C    . VAL   A 85  ? 0.30578 0.33452 0.29925 -0.01078 -0.03075 -0.04084 237 VAL   A C    
493  O  O    . VAL   A 85  ? 0.30246 0.33749 0.29687 -0.01190 -0.02970 -0.04989 237 VAL   A O    
494  C  CB   . VAL   A 85  ? 0.29533 0.30574 0.29271 -0.01021 -0.02713 -0.02876 237 VAL   A CB   
495  C  CG1  . VAL   A 85  ? 0.27974 0.29212 0.28916 -0.01082 -0.02898 -0.03608 237 VAL   A CG1  
496  C  CG2  . VAL   A 85  ? 0.29860 0.30138 0.28807 -0.01105 -0.02284 -0.02270 237 VAL   A CG2  
497  N  N    . ILE   A 86  ? 0.24511 0.27724 0.24401 -0.01017 -0.03504 -0.04078 238 ILE   A N    
498  C  CA   . ILE   A 86  ? 0.23031 0.27298 0.23535 -0.01164 -0.03922 -0.05236 238 ILE   A CA   
499  C  C    . ILE   A 86  ? 0.26256 0.31939 0.25267 -0.01314 -0.03835 -0.05649 238 ILE   A C    
500  O  O    . ILE   A 86  ? 0.31243 0.37880 0.30398 -0.01481 -0.03831 -0.06984 238 ILE   A O    
501  C  CB   . ILE   A 86  ? 0.24820 0.29336 0.26219 -0.01186 -0.04438 -0.05043 238 ILE   A CB   
502  C  CG1  . ILE   A 86  ? 0.29322 0.32739 0.32356 -0.01188 -0.04504 -0.04703 238 ILE   A CG1  
503  C  CG2  . ILE   A 86  ? 0.28979 0.34804 0.30775 -0.01460 -0.04922 -0.06365 238 ILE   A CG2  
504  C  CD1  . ILE   A 86  ? 0.29425 0.33042 0.33077 -0.01189 -0.04754 -0.03937 238 ILE   A CD1  
505  N  N    . GLY   A 87  ? 0.25648 0.31578 0.23289 -0.01257 -0.03743 -0.04493 239 GLY   A N    
506  C  CA   . GLY   A 87  ? 0.29277 0.36711 0.25375 -0.01483 -0.03674 -0.04495 239 GLY   A CA   
507  C  C    . GLY   A 87  ? 0.29527 0.37191 0.25093 -0.01698 -0.03093 -0.05044 239 GLY   A C    
508  O  O    . GLY   A 87  ? 0.32392 0.41752 0.27202 -0.01982 -0.02998 -0.05899 239 GLY   A O    
509  N  N    . PHE   A 88  ? 0.28444 0.34666 0.24411 -0.01609 -0.02685 -0.04621 240 PHE   A N    
510  C  CA   . PHE   A 88  ? 0.27031 0.33583 0.22837 -0.01820 -0.02157 -0.05141 240 PHE   A CA   
511  C  C    . PHE   A 88  ? 0.25969 0.33188 0.23085 -0.01748 -0.02203 -0.06844 240 PHE   A C    
512  O  O    . PHE   A 88  ? 0.29146 0.37817 0.25952 -0.01928 -0.01859 -0.07821 240 PHE   A O    
513  C  CB   . PHE   A 88  ? 0.24086 0.29058 0.20173 -0.01792 -0.01845 -0.04343 240 PHE   A CB   
514  C  CG   . PHE   A 88  ? 0.28750 0.34137 0.25024 -0.02022 -0.01377 -0.04839 240 PHE   A CG   
515  C  CD1  . PHE   A 88  ? 0.28887 0.35084 0.23984 -0.02444 -0.00907 -0.04418 240 PHE   A CD1  
516  C  CD2  . PHE   A 88  ? 0.29080 0.34152 0.26871 -0.01836 -0.01432 -0.05569 240 PHE   A CD2  
517  C  CE1  . PHE   A 88  ? 0.29021 0.35852 0.24463 -0.02707 -0.00445 -0.04872 240 PHE   A CE1  
518  C  CE2  . PHE   A 88  ? 0.26116 0.31814 0.24330 -0.01993 -0.01043 -0.05992 240 PHE   A CE2  
519  C  CZ   . PHE   A 88  ? 0.28399 0.35043 0.25439 -0.02444 -0.00522 -0.05714 240 PHE   A CZ   
520  N  N    . ALA   A 89  ? 0.26845 0.33057 0.25586 -0.01488 -0.02593 -0.07208 241 ALA   A N    
521  C  CA   . ALA   A 89  ? 0.29430 0.35843 0.29926 -0.01342 -0.02678 -0.08724 241 ALA   A CA   
522  C  C    . ALA   A 89  ? 0.31930 0.40045 0.32203 -0.01500 -0.02754 -0.10296 241 ALA   A C    
523  O  O    . ALA   A 89  ? 0.29782 0.38724 0.30893 -0.01430 -0.02474 -0.11813 241 ALA   A O    
524  C  CB   . ALA   A 89  ? 0.30188 0.35170 0.32494 -0.01140 -0.03162 -0.08497 241 ALA   A CB   
525  N  N    . LYS   A 90  ? 0.27194 0.36042 0.26413 -0.01708 -0.03134 -0.10043 242 LYS   A N    
526  C  CA   . LYS   A 90  ? 0.26810 0.37600 0.25583 -0.01981 -0.03294 -0.11596 242 LYS   A CA   
527  C  C    . LYS   A 90  ? 0.33001 0.45748 0.30275 -0.02221 -0.02672 -0.12211 242 LYS   A C    
528  O  O    . LYS   A 90  ? 0.35781 0.50333 0.32945 -0.02427 -0.02604 -0.14026 242 LYS   A O    
529  C  CB   . LYS   A 90  ? 0.30003 0.41526 0.27746 -0.02198 -0.03898 -0.10847 242 LYS   A CB   
530  C  CG   . LYS   A 90  ? 0.43513 0.53837 0.42967 -0.02110 -0.04527 -0.10796 242 LYS   A CG   
531  C  CD   . LYS   A 90  ? 0.46512 0.57364 0.45046 -0.02178 -0.05023 -0.09417 242 LYS   A CD   
532  C  CE   . LYS   A 90  ? 0.46951 0.60325 0.44241 -0.02595 -0.05447 -0.10219 242 LYS   A CE   
533  N  NZ   . LYS   A 90  ? 0.44757 0.58862 0.41319 -0.02578 -0.06011 -0.08659 242 LYS   A NZ   
534  N  N    . MET   A 91  ? 0.29622 0.42174 0.25802 -0.02271 -0.02178 -0.10835 243 MET   A N    
535  C  CA   . MET   A 91  ? 0.38684 0.53226 0.33421 -0.02624 -0.01524 -0.11098 243 MET   A CA   
536  C  C    . MET   A 91  ? 0.35128 0.49652 0.31111 -0.02451 -0.00871 -0.12025 243 MET   A C    
537  O  O    . MET   A 91  ? 0.38419 0.54818 0.33476 -0.02763 -0.00216 -0.12405 243 MET   A O    
538  C  CB   . MET   A 91  ? 0.43712 0.58224 0.36566 -0.02922 -0.01398 -0.08881 243 MET   A CB   
539  C  CG   . MET   A 91  ? 0.55569 0.70371 0.47336 -0.02999 -0.02060 -0.07767 243 MET   A CG   
540  S  SD   . MET   A 91  ? 0.60839 0.75870 0.50629 -0.03326 -0.01911 -0.05187 243 MET   A SD   
541  C  CE   . MET   A 91  ? 0.57744 0.69764 0.48591 -0.02780 -0.02311 -0.03629 243 MET   A CE   
542  N  N    . ILE   A 92  ? 0.31503 0.44188 0.29620 -0.01984 -0.01045 -0.12285 244 ILE   A N    
543  C  CA   . ILE   A 92  ? 0.28528 0.41389 0.28225 -0.01715 -0.00548 -0.13193 244 ILE   A CA   
544  C  C    . ILE   A 92  ? 0.33506 0.48272 0.33984 -0.01622 -0.00229 -0.15619 244 ILE   A C    
545  O  O    . ILE   A 92  ? 0.33882 0.48469 0.35240 -0.01494 -0.00675 -0.16897 244 ILE   A O    
546  C  CB   . ILE   A 92  ? 0.30365 0.41008 0.32271 -0.01228 -0.00966 -0.12789 244 ILE   A CB   
547  C  CG1  . ILE   A 92  ? 0.25804 0.34842 0.26812 -0.01366 -0.01181 -0.10663 244 ILE   A CG1  
548  C  CG2  . ILE   A 92  ? 0.25363 0.36382 0.29192 -0.00864 -0.00575 -0.13637 244 ILE   A CG2  
549  C  CD1  . ILE   A 92  ? 0.25361 0.32534 0.28173 -0.01008 -0.01656 -0.10104 244 ILE   A CD1  
550  N  N    . PRO   A 93  ? 0.32516 0.49232 0.32791 -0.01728 0.00569  -0.16439 245 PRO   A N    
551  C  CA   . PRO   A 93  ? 0.34672 0.53382 0.35853 -0.01576 0.01008  -0.19054 245 PRO   A CA   
552  C  C    . PRO   A 93  ? 0.40433 0.57567 0.44875 -0.00837 0.00657  -0.20530 245 PRO   A C    
553  O  O    . PRO   A 93  ? 0.37942 0.53667 0.44411 -0.00337 0.00596  -0.19953 245 PRO   A O    
554  C  CB   . PRO   A 93  ? 0.39680 0.60447 0.40569 -0.01727 0.01992  -0.19246 245 PRO   A CB   
555  C  CG   . PRO   A 93  ? 0.39324 0.59841 0.37968 -0.02337 0.02031  -0.16717 245 PRO   A CG   
556  C  CD   . PRO   A 93  ? 0.35107 0.52569 0.34157 -0.02112 0.01166  -0.15070 245 PRO   A CD   
557  N  N    . GLY   A 94  ? 0.42504 0.59924 0.47529 -0.00824 0.00364  -0.22384 246 GLY   A N    
558  C  CA   . GLY   A 94  ? 0.40105 0.55909 0.48406 -0.00211 -0.00006 -0.23867 246 GLY   A CA   
559  C  C    . GLY   A 94  ? 0.39052 0.52293 0.48166 -0.00225 -0.00994 -0.22711 246 GLY   A C    
560  O  O    . GLY   A 94  ? 0.46065 0.58185 0.57609 0.00031  -0.01388 -0.24118 246 GLY   A O    
561  N  N    . PHE   A 95  ? 0.36441 0.48774 0.43734 -0.00542 -0.01360 -0.20248 247 PHE   A N    
562  C  CA   . PHE   A 95  ? 0.36336 0.46389 0.44565 -0.00525 -0.02177 -0.18973 247 PHE   A CA   
563  C  C    . PHE   A 95  ? 0.47755 0.57928 0.56385 -0.00840 -0.02711 -0.20343 247 PHE   A C    
564  O  O    . PHE   A 95  ? 0.46162 0.54583 0.57142 -0.00705 -0.03257 -0.20544 247 PHE   A O    
565  C  CB   . PHE   A 95  ? 0.32704 0.42187 0.38739 -0.00807 -0.02326 -0.16416 247 PHE   A CB   
566  C  CG   . PHE   A 95  ? 0.38216 0.45681 0.45130 -0.00790 -0.03015 -0.15040 247 PHE   A CG   
567  C  CD1  . PHE   A 95  ? 0.33359 0.39113 0.42064 -0.00445 -0.03186 -0.14013 247 PHE   A CD1  
568  C  CD2  . PHE   A 95  ? 0.31778 0.39347 0.37756 -0.01156 -0.03499 -0.14706 247 PHE   A CD2  
569  C  CE1  . PHE   A 95  ? 0.32326 0.36552 0.41729 -0.00519 -0.03737 -0.12691 247 PHE   A CE1  
570  C  CE2  . PHE   A 95  ? 0.32496 0.38501 0.39376 -0.01180 -0.04034 -0.13462 247 PHE   A CE2  
571  C  CZ   . PHE   A 95  ? 0.30774 0.35124 0.39299 -0.00888 -0.04107 -0.12459 247 PHE   A CZ   
572  N  N    A ARG   A 96  ? 0.44777 0.57125 0.51186 -0.01343 -0.02608 -0.21213 248 ARG   A N    
573  N  N    B ARG   A 96  ? 0.46085 0.58437 0.52489 -0.01343 -0.02606 -0.21213 248 ARG   A N    
574  C  CA   A ARG   A 96  ? 0.52485 0.65331 0.59104 -0.01769 -0.03190 -0.22596 248 ARG   A CA   
575  C  CA   B ARG   A 96  ? 0.52098 0.64994 0.58668 -0.01775 -0.03180 -0.22607 248 ARG   A CA   
576  C  C    A ARG   A 96  ? 0.52320 0.65499 0.61258 -0.01633 -0.03042 -0.25676 248 ARG   A C    
577  C  C    B ARG   A 96  ? 0.52445 0.65647 0.61358 -0.01636 -0.03038 -0.25679 248 ARG   A C    
578  O  O    A ARG   A 96  ? 0.54011 0.67427 0.63493 -0.01971 -0.03428 -0.26583 248 ARG   A O    
579  O  O    B ARG   A 96  ? 0.53922 0.67363 0.63374 -0.01975 -0.03425 -0.26582 248 ARG   A O    
580  C  CB   A ARG   A 96  ? 0.56196 0.71555 0.59575 -0.02390 -0.03248 -0.22322 248 ARG   A CB   
581  C  CB   B ARG   A 96  ? 0.56305 0.71757 0.59615 -0.02392 -0.03214 -0.22355 248 ARG   A CB   
582  C  CG   A ARG   A 96  ? 0.59410 0.74082 0.61190 -0.02531 -0.03690 -0.19525 248 ARG   A CG   
583  C  CG   B ARG   A 96  ? 0.58757 0.73711 0.60120 -0.02484 -0.03438 -0.19402 248 ARG   A CG   
584  C  CD   A ARG   A 96  ? 0.64795 0.79613 0.66693 -0.02937 -0.04575 -0.19556 248 ARG   A CD   
585  C  CD   B ARG   A 96  ? 0.63150 0.78943 0.63378 -0.02954 -0.04220 -0.18866 248 ARG   A CD   
586  N  NE   A ARG   A 96  ? 0.67899 0.80996 0.72780 -0.02879 -0.04993 -0.20772 248 ARG   A NE   
587  N  NE   B ARG   A 96  ? 0.65592 0.80406 0.68055 -0.03081 -0.04877 -0.20092 248 ARG   A NE   
588  C  CZ   A ARG   A 96  ? 0.65251 0.79181 0.71167 -0.03290 -0.05370 -0.23070 248 ARG   A CZ   
589  C  CZ   B ARG   A 96  ? 0.62111 0.74717 0.66243 -0.02921 -0.05321 -0.18835 248 ARG   A CZ   
590  N  NH1  A ARG   A 96  ? 0.68658 0.85215 0.72639 -0.03702 -0.05269 -0.24063 248 ARG   A NH1  
591  N  NH1  B ARG   A 96  ? 0.64107 0.75987 0.70370 -0.03177 -0.05898 -0.19967 248 ARG   A NH1  
592  N  NH2  A ARG   A 96  ? 0.65759 0.77781 0.74688 -0.03275 -0.05750 -0.23953 248 ARG   A NH2  
593  N  NH2  B ARG   A 96  ? 0.45599 0.56822 0.49299 -0.02579 -0.05160 -0.16502 248 ARG   A NH2  
594  N  N    . ASP   A 97  ? 0.50610 0.63761 0.61098 -0.01047 -0.02363 -0.26656 249 ASP   A N    
595  C  CA   . ASP   A 97  ? 0.54355 0.67264 0.67778 -0.00645 -0.02108 -0.28563 249 ASP   A CA   
596  C  C    . ASP   A 97  ? 0.53560 0.63418 0.70421 -0.00308 -0.02781 -0.28254 249 ASP   A C    
597  O  O    . ASP   A 97  ? 0.48905 0.58228 0.68379 -0.00104 -0.02793 -0.29644 249 ASP   A O    
598  C  CB   . ASP   A 97  ? 0.64530 0.78614 0.78810 -0.00061 -0.01177 -0.29528 249 ASP   A CB   
599  C  CG   . ASP   A 97  ? 0.70269 0.87726 0.81798 -0.00487 -0.00404 -0.30234 249 ASP   A CG   
600  O  OD1  . ASP   A 97  ? 0.75458 0.94332 0.84661 -0.01180 -0.00628 -0.30147 249 ASP   A OD1  
601  O  OD2  . ASP   A 97  ? 0.71961 0.90777 0.83758 -0.00156 0.00406  -0.30763 249 ASP   A OD2  
602  N  N    . LEU   A 98  ? 0.41757 0.49698 0.58716 -0.00295 -0.03328 -0.26296 250 LEU   A N    
603  C  CA   . LEU   A 98  ? 0.40624 0.45802 0.60610 -0.00105 -0.03991 -0.25344 250 LEU   A CA   
604  C  C    . LEU   A 98  ? 0.43153 0.47876 0.63305 -0.00807 -0.04683 -0.25521 250 LEU   A C    
605  O  O    . LEU   A 98  ? 0.45407 0.51837 0.62928 -0.01409 -0.04778 -0.25644 250 LEU   A O    
606  C  CB   . LEU   A 98  ? 0.30543 0.34484 0.49940 0.00092  -0.04144 -0.22160 250 LEU   A CB   
607  C  CG   . LEU   A 98  ? 0.30235 0.34524 0.49705 0.00725  -0.03580 -0.21475 250 LEU   A CG   
608  C  CD1  . LEU   A 98  ? 0.32897 0.36733 0.50471 0.00603  -0.03680 -0.18583 250 LEU   A CD1  
609  C  CD2  . LEU   A 98  ? 0.36789 0.39605 0.60259 0.01459  -0.03695 -0.22094 250 LEU   A CD2  
610  N  N    . THR   A 99  ? 0.41430 0.43972 0.64775 -0.00721 -0.05159 -0.25206 251 THR   A N    
611  C  CA   . THR   A 99  ? 0.41462 0.43434 0.65207 -0.01430 -0.05811 -0.24884 251 THR   A CA   
612  C  C    . THR   A 99  ? 0.37177 0.38992 0.59023 -0.01912 -0.06293 -0.22662 251 THR   A C    
613  O  O    . THR   A 99  ? 0.32849 0.34446 0.53436 -0.01517 -0.06012 -0.20549 251 THR   A O    
614  C  CB   . THR   A 99  ? 0.48346 0.47986 0.76040 -0.01277 -0.06175 -0.24670 251 THR   A CB   
615  O  OG1  . THR   A 99  ? 0.44948 0.42627 0.74144 -0.00943 -0.06454 -0.22584 251 THR   A OG1  
616  C  CG2  . THR   A 99  ? 0.53381 0.53259 0.83267 -0.00707 -0.05683 -0.26741 251 THR   A CG2  
617  N  N    . SER   A 100 ? 0.35802 0.38043 0.57252 -0.02674 -0.06857 -0.22684 252 SER   A N    
618  C  CA   . SER   A 100 ? 0.34773 0.37054 0.54655 -0.02962 -0.07134 -0.20074 252 SER   A CA   
619  C  C    . SER   A 100 ? 0.30378 0.30520 0.52023 -0.02694 -0.07216 -0.17768 252 SER   A C    
620  O  O    . SER   A 100 ? 0.33503 0.33702 0.53435 -0.02494 -0.07011 -0.15568 252 SER   A O    
621  C  CB   . SER   A 100 ? 0.39822 0.42856 0.59930 -0.03823 -0.07805 -0.20642 252 SER   A CB   
622  O  OG   . SER   A 100 ? 0.53742 0.59342 0.71153 -0.04112 -0.07812 -0.21756 252 SER   A OG   
623  N  N    . ASP   A 101 ? 0.34846 0.33134 0.59994 -0.02714 -0.07521 -0.18265 253 ASP   A N    
624  C  CA   . ASP   A 101 ? 0.38981 0.35420 0.65958 -0.02524 -0.07673 -0.15939 253 ASP   A CA   
625  C  C    . ASP   A 101 ? 0.33009 0.29510 0.58762 -0.01754 -0.07179 -0.14688 253 ASP   A C    
626  O  O    . ASP   A 101 ? 0.32467 0.28730 0.57294 -0.01729 -0.07157 -0.12293 253 ASP   A O    
627  C  CB   . ASP   A 101 ? 0.36359 0.30761 0.67582 -0.02578 -0.08080 -0.16795 253 ASP   A CB   
628  C  CG   . ASP   A 101 ? 0.46066 0.40038 0.78756 -0.03464 -0.08600 -0.16763 253 ASP   A CG   
629  O  OD1  . ASP   A 101 ? 0.53057 0.45756 0.88585 -0.03411 -0.08712 -0.17056 253 ASP   A OD1  
630  O  OD2  . ASP   A 101 ? 0.43288 0.38473 0.74137 -0.04114 -0.08803 -0.16217 253 ASP   A OD2  
631  N  N    . ASP   A 102 ? 0.34308 0.31335 0.60067 -0.01171 -0.06754 -0.16379 254 ASP   A N    
632  C  CA   . ASP   A 102 ? 0.34137 0.31311 0.59187 -0.00494 -0.06335 -0.15307 254 ASP   A CA   
633  C  C    . ASP   A 102 ? 0.34612 0.33270 0.55818 -0.00593 -0.05934 -0.14153 254 ASP   A C    
634  O  O    . ASP   A 102 ? 0.31122 0.29611 0.51491 -0.00368 -0.05792 -0.12316 254 ASP   A O    
635  C  CB   . ASP   A 102 ? 0.31886 0.29431 0.58329 0.00150  -0.05934 -0.17527 254 ASP   A CB   
636  C  CG   . ASP   A 102 ? 0.39595 0.35232 0.70294 0.00640  -0.06271 -0.17681 254 ASP   A CG   
637  O  OD1  . ASP   A 102 ? 0.40675 0.36409 0.73305 0.01189  -0.05986 -0.19898 254 ASP   A OD1  
638  O  OD2  . ASP   A 102 ? 0.40968 0.35096 0.73178 0.00483  -0.06804 -0.15544 254 ASP   A OD2  
639  N  N    . GLN   A 103 ? 0.29153 0.29310 0.48079 -0.00953 -0.05784 -0.15194 255 GLN   A N    
640  C  CA   . GLN   A 103 ? 0.28327 0.29624 0.43937 -0.01064 -0.05482 -0.13890 255 GLN   A CA   
641  C  C    . GLN   A 103 ? 0.29513 0.29993 0.44780 -0.01288 -0.05745 -0.11576 255 GLN   A C    
642  O  O    . GLN   A 103 ? 0.25238 0.25832 0.38803 -0.01149 -0.05449 -0.10069 255 GLN   A O    
643  C  CB   . GLN   A 103 ? 0.29574 0.32647 0.43150 -0.01450 -0.05456 -0.15134 255 GLN   A CB   
644  C  CG   . GLN   A 103 ? 0.38133 0.42597 0.51461 -0.01326 -0.05060 -0.17471 255 GLN   A CG   
645  C  CD   . GLN   A 103 ? 0.46889 0.53426 0.58081 -0.01829 -0.05148 -0.18534 255 GLN   A CD   
646  O  OE1  . GLN   A 103 ? 0.46985 0.54094 0.56323 -0.02108 -0.05376 -0.17119 255 GLN   A OE1  
647  N  NE2  . GLN   A 103 ? 0.45637 0.53471 0.57153 -0.01932 -0.04976 -0.21059 255 GLN   A NE2  
648  N  N    . ILE   A 104 ? 0.32324 0.32070 0.49292 -0.01691 -0.06259 -0.11370 256 ILE   A N    
649  C  CA   . ILE   A 104 ? 0.30839 0.30158 0.47591 -0.01969 -0.06428 -0.09286 256 ILE   A CA   
650  C  C    . ILE   A 104 ? 0.25704 0.23977 0.43305 -0.01711 -0.06356 -0.07617 256 ILE   A C    
651  O  O    . ILE   A 104 ? 0.29300 0.27817 0.45292 -0.01697 -0.06115 -0.06029 256 ILE   A O    
652  C  CB   . ILE   A 104 ? 0.30442 0.29435 0.49099 -0.02577 -0.06981 -0.09516 256 ILE   A CB   
653  C  CG1  . ILE   A 104 ? 0.34696 0.35251 0.51871 -0.02920 -0.07125 -0.10587 256 ILE   A CG1  
654  C  CG2  . ILE   A 104 ? 0.35234 0.33638 0.54564 -0.02873 -0.07103 -0.07301 256 ILE   A CG2  
655  C  CD1  . ILE   A 104 ? 0.32591 0.33092 0.51782 -0.03621 -0.07727 -0.11190 256 ILE   A CD1  
656  N  N    A VAL   A 105 ? 0.29317 0.26511 0.49522 -0.01491 -0.06583 -0.07975 257 VAL   A N    
657  N  N    B VAL   A 105 ? 0.29904 0.27089 0.50149 -0.01505 -0.06594 -0.07992 257 VAL   A N    
658  C  CA   A VAL   A 105 ? 0.32657 0.29097 0.53806 -0.01285 -0.06667 -0.06157 257 VAL   A CA   
659  C  CA   B VAL   A 105 ? 0.32411 0.28806 0.53731 -0.01261 -0.06679 -0.06298 257 VAL   A CA   
660  C  C    A VAL   A 105 ? 0.31465 0.28676 0.50537 -0.00857 -0.06209 -0.05809 257 VAL   A C    
661  C  C    B VAL   A 105 ? 0.31295 0.28506 0.50379 -0.00865 -0.06212 -0.05848 257 VAL   A C    
662  O  O    A VAL   A 105 ? 0.31482 0.28770 0.49764 -0.00890 -0.06170 -0.04079 257 VAL   A O    
663  O  O    B VAL   A 105 ? 0.29675 0.26975 0.47886 -0.00925 -0.06169 -0.04091 257 VAL   A O    
664  C  CB   A VAL   A 105 ? 0.33998 0.29058 0.58806 -0.01066 -0.07106 -0.06463 257 VAL   A CB   
665  C  CB   B VAL   A 105 ? 0.35243 0.30370 0.60101 -0.00957 -0.07051 -0.06990 257 VAL   A CB   
666  C  CG1  A VAL   A 105 ? 0.36973 0.31099 0.64009 -0.01661 -0.07583 -0.06636 257 VAL   A CG1  
667  C  CG1  B VAL   A 105 ? 0.36082 0.30941 0.61732 -0.00452 -0.07096 -0.05646 257 VAL   A CG1  
668  C  CG2  A VAL   A 105 ? 0.36858 0.32067 0.62501 -0.00460 -0.06880 -0.08659 257 VAL   A CG2  
669  C  CG2  B VAL   A 105 ? 0.36814 0.30744 0.64267 -0.01511 -0.07602 -0.06490 257 VAL   A CG2  
670  N  N    . LEU   A 106 ? 0.30566 0.28538 0.48697 -0.00546 -0.05840 -0.07479 258 LEU   A N    
671  C  CA   . LEU   A 106 ? 0.30863 0.29637 0.47123 -0.00275 -0.05384 -0.07155 258 LEU   A CA   
672  C  C    . LEU   A 106 ? 0.28682 0.27999 0.42062 -0.00589 -0.05101 -0.06040 258 LEU   A C    
673  O  O    . LEU   A 106 ? 0.24010 0.23502 0.36277 -0.00562 -0.04905 -0.04960 258 LEU   A O    
674  C  CB   . LEU   A 106 ? 0.28954 0.28673 0.44846 0.00014  -0.04972 -0.09132 258 LEU   A CB   
675  C  CG   . LEU   A 106 ? 0.29661 0.29067 0.48450 0.00528  -0.05050 -0.10461 258 LEU   A CG   
676  C  CD1  . LEU   A 106 ? 0.27702 0.28532 0.45677 0.00727  -0.04470 -0.12505 258 LEU   A CD1  
677  C  CD2  . LEU   A 106 ? 0.25774 0.24738 0.46053 0.00921  -0.05238 -0.09081 258 LEU   A CD2  
678  N  N    . LEU   A 107 ? 0.27421 0.27056 0.39736 -0.00883 -0.05104 -0.06333 259 LEU   A N    
679  C  CA   . LEU   A 107 ? 0.27622 0.27693 0.37565 -0.01047 -0.04818 -0.05340 259 LEU   A CA   
680  C  C    . LEU   A 107 ? 0.25137 0.24742 0.35358 -0.01256 -0.04939 -0.03693 259 LEU   A C    
681  O  O    . LEU   A 107 ? 0.25709 0.25492 0.34355 -0.01274 -0.04612 -0.02772 259 LEU   A O    
682  C  CB   . LEU   A 107 ? 0.32185 0.33005 0.41079 -0.01210 -0.04843 -0.06068 259 LEU   A CB   
683  C  CG   . LEU   A 107 ? 0.36672 0.38476 0.44096 -0.01100 -0.04531 -0.07208 259 LEU   A CG   
684  C  CD1  . LEU   A 107 ? 0.41062 0.43867 0.47976 -0.01317 -0.04771 -0.08119 259 LEU   A CD1  
685  C  CD2  . LEU   A 107 ? 0.35489 0.37467 0.40809 -0.01030 -0.04054 -0.06266 259 LEU   A CD2  
686  N  N    . LYS   A 108 ? 0.23578 0.22667 0.35833 -0.01481 -0.05372 -0.03349 260 LYS   A N    
687  C  CA   . LYS   A 108 ? 0.28263 0.27206 0.40850 -0.01771 -0.05443 -0.01661 260 LYS   A CA   
688  C  C    . LYS   A 108 ? 0.30616 0.29494 0.42999 -0.01659 -0.05383 -0.00633 260 LYS   A C    
689  O  O    . LYS   A 108 ? 0.29643 0.28984 0.40701 -0.01840 -0.05132 0.00484  260 LYS   A O    
690  C  CB   . LYS   A 108 ? 0.32856 0.31219 0.48009 -0.02131 -0.05950 -0.01363 260 LYS   A CB   
691  C  CG   . LYS   A 108 ? 0.43967 0.42714 0.59323 -0.02453 -0.06071 -0.02005 260 LYS   A CG   
692  C  CD   . LYS   A 108 ? 0.51830 0.49957 0.69892 -0.02974 -0.06558 -0.01484 260 LYS   A CD   
693  C  CE   . LYS   A 108 ? 0.57732 0.56153 0.75855 -0.03353 -0.06446 0.00616  260 LYS   A CE   
694  N  NZ   . LYS   A 108 ? 0.63036 0.60818 0.83989 -0.03970 -0.06920 0.01459  260 LYS   A NZ   
695  N  N    A SER   A 109 ? 0.26683 0.25177 0.40441 -0.01355 -0.05613 -0.01086 261 SER   A N    
696  N  N    B SER   A 109 ? 0.27626 0.26116 0.41400 -0.01357 -0.05616 -0.01077 261 SER   A N    
697  C  CA   A SER   A 109 ? 0.35300 0.33978 0.49149 -0.01254 -0.05706 -0.00029 261 SER   A CA   
698  C  CA   B SER   A 109 ? 0.34848 0.33527 0.48695 -0.01254 -0.05706 -0.00029 261 SER   A CA   
699  C  C    A SER   A 109 ? 0.31806 0.31200 0.43250 -0.01164 -0.05223 -0.00323 261 SER   A C    
700  C  C    B SER   A 109 ? 0.31765 0.31158 0.43216 -0.01163 -0.05224 -0.00325 261 SER   A C    
701  O  O    A SER   A 109 ? 0.29332 0.29218 0.39916 -0.01333 -0.05200 0.00716  261 SER   A O    
702  O  O    B SER   A 109 ? 0.29655 0.29539 0.40258 -0.01330 -0.05204 0.00714  261 SER   A O    
703  C  CB   A SER   A 109 ? 0.35714 0.33829 0.52248 -0.00857 -0.06143 -0.00389 261 SER   A CB   
704  C  CB   B SER   A 109 ? 0.35746 0.33872 0.52264 -0.00854 -0.06142 -0.00380 261 SER   A CB   
705  O  OG   A SER   A 109 ? 0.36320 0.34872 0.53108 -0.00724 -0.06346 0.00734  261 SER   A OG   
706  O  OG   B SER   A 109 ? 0.36952 0.35057 0.53729 -0.00487 -0.05925 -0.02343 261 SER   A OG   
707  N  N    . SER   A 110 ? 0.28236 0.27796 0.38586 -0.00991 -0.04855 -0.01688 262 SER   A N    
708  C  CA   . SER   A 110 ? 0.25120 0.25224 0.33606 -0.00965 -0.04413 -0.01986 262 SER   A CA   
709  C  C    . SER   A 110 ? 0.26794 0.27010 0.32962 -0.01198 -0.03964 -0.01733 262 SER   A C    
710  O  O    . SER   A 110 ? 0.24243 0.24707 0.28996 -0.01306 -0.03627 -0.01692 262 SER   A O    
711  C  CB   . SER   A 110 ? 0.29031 0.29460 0.37716 -0.00689 -0.04210 -0.03467 262 SER   A CB   
712  O  OG   . SER   A 110 ? 0.32755 0.33276 0.40535 -0.00741 -0.04028 -0.04278 262 SER   A OG   
713  N  N    . ALA   A 111 ? 0.25321 0.25370 0.31298 -0.01276 -0.03960 -0.01578 263 ALA   A N    
714  C  CA   . ALA   A 111 ? 0.24121 0.24261 0.28278 -0.01314 -0.03529 -0.01520 263 ALA   A CA   
715  C  C    . ALA   A 111 ? 0.23011 0.23197 0.25909 -0.01494 -0.03186 -0.00850 263 ALA   A C    
716  O  O    . ALA   A 111 ? 0.24550 0.24617 0.26043 -0.01499 -0.02779 -0.01105 263 ALA   A O    
717  C  CB   . ALA   A 111 ? 0.27264 0.27474 0.31859 -0.01341 -0.03649 -0.01306 263 ALA   A CB   
718  N  N    . ILE   A 112 ? 0.22251 0.22674 0.25662 -0.01711 -0.03353 0.00009  264 ILE   A N    
719  C  CA   . ILE   A 112 ? 0.25532 0.26304 0.27640 -0.01978 -0.03033 0.00459  264 ILE   A CA   
720  C  C    . ILE   A 112 ? 0.28954 0.29786 0.30391 -0.02077 -0.02970 0.00050  264 ILE   A C    
721  O  O    . ILE   A 112 ? 0.23469 0.24282 0.23503 -0.02280 -0.02559 -0.00180 264 ILE   A O    
722  C  CB   . ILE   A 112 ? 0.33245 0.34674 0.36000 -0.02289 -0.03296 0.01580  264 ILE   A CB   
723  C  CG1  . ILE   A 112 ? 0.35803 0.37957 0.37002 -0.02654 -0.02953 0.01846  264 ILE   A CG1  
724  C  CG2  . ILE   A 112 ? 0.29600 0.31065 0.34102 -0.02271 -0.03955 0.02071  264 ILE   A CG2  
725  C  CD1  . ILE   A 112 ? 0.32826 0.34835 0.32715 -0.02587 -0.02266 0.01296  264 ILE   A CD1  
726  N  N    . GLU   A 113 ? 0.22387 0.23321 0.25016 -0.01943 -0.03351 -0.00138 265 GLU   A N    
727  C  CA   . GLU   A 113 ? 0.23936 0.25241 0.26238 -0.02068 -0.03312 -0.00472 265 GLU   A CA   
728  C  C    . GLU   A 113 ? 0.24492 0.25450 0.25700 -0.02054 -0.02821 -0.01321 265 GLU   A C    
729  O  O    . GLU   A 113 ? 0.24637 0.25699 0.24838 -0.02383 -0.02543 -0.01491 265 GLU   A O    
730  C  CB   . GLU   A 113 ? 0.26363 0.28033 0.30615 -0.01812 -0.03817 -0.00455 265 GLU   A CB   
731  C  CG   . GLU   A 113 ? 0.23406 0.25405 0.28988 -0.01849 -0.04404 0.00715  265 GLU   A CG   
732  C  CD   . GLU   A 113 ? 0.29452 0.31595 0.37424 -0.01445 -0.04922 0.00734  265 GLU   A CD   
733  O  OE1  . GLU   A 113 ? 0.27966 0.30412 0.36288 -0.01222 -0.04774 -0.00169 265 GLU   A OE1  
734  O  OE2  . GLU   A 113 ? 0.31491 0.33473 0.41161 -0.01346 -0.05449 0.01676  265 GLU   A OE2  
735  N  N    . VAL   A 114 ? 0.27416 0.28061 0.28831 -0.01762 -0.02745 -0.01803 266 VAL   A N    
736  C  CA   . VAL   A 114 ? 0.22769 0.23283 0.23091 -0.01797 -0.02324 -0.02320 266 VAL   A CA   
737  C  C    . VAL   A 114 ? 0.26173 0.26044 0.25109 -0.01942 -0.01936 -0.01998 266 VAL   A C    
738  O  O    . VAL   A 114 ? 0.26284 0.25878 0.24297 -0.02163 -0.01570 -0.02123 266 VAL   A O    
739  C  CB   . VAL   A 114 ? 0.26166 0.26860 0.26923 -0.01507 -0.02417 -0.02875 266 VAL   A CB   
740  C  CG1  . VAL   A 114 ? 0.25825 0.26737 0.25369 -0.01620 -0.02022 -0.03175 266 VAL   A CG1  
741  C  CG2  . VAL   A 114 ? 0.27481 0.28656 0.29936 -0.01303 -0.02749 -0.03443 266 VAL   A CG2  
742  N  N    . ILE   A 115 ? 0.24990 0.24628 0.23954 -0.01828 -0.01972 -0.01585 267 ILE   A N    
743  C  CA   . ILE   A 115 ? 0.25136 0.24215 0.23097 -0.01860 -0.01536 -0.01442 267 ILE   A CA   
744  C  C    . ILE   A 115 ? 0.24067 0.23063 0.21292 -0.02312 -0.01291 -0.01591 267 ILE   A C    
745  O  O    . ILE   A 115 ? 0.28748 0.27037 0.25198 -0.02455 -0.00876 -0.01831 267 ILE   A O    
746  C  CB   . ILE   A 115 ? 0.26929 0.26176 0.25269 -0.01662 -0.01556 -0.01052 267 ILE   A CB   
747  C  CG1  . ILE   A 115 ? 0.26363 0.25641 0.25260 -0.01279 -0.01730 -0.01013 267 ILE   A CG1  
748  C  CG2  . ILE   A 115 ? 0.25066 0.24006 0.22580 -0.01710 -0.01026 -0.01096 267 ILE   A CG2  
749  C  CD1  . ILE   A 115 ? 0.29110 0.28870 0.28901 -0.01192 -0.01897 -0.00606 267 ILE   A CD1  
750  N  N    . MET   A 116 ? 0.26118 0.25867 0.23699 -0.02586 -0.01601 -0.01418 268 MET   A N    
751  C  CA   . MET   A 116 ? 0.29250 0.29283 0.26130 -0.03126 -0.01492 -0.01628 268 MET   A CA   
752  C  C    . MET   A 116 ? 0.23459 0.23302 0.20196 -0.03391 -0.01372 -0.02052 268 MET   A C    
753  O  O    . MET   A 116 ? 0.29672 0.29118 0.25644 -0.03851 -0.01045 -0.02435 268 MET   A O    
754  C  CB   . MET   A 116 ? 0.30021 0.31242 0.27431 -0.03352 -0.02006 -0.01111 268 MET   A CB   
755  C  CG   . MET   A 116 ? 0.31896 0.33579 0.29208 -0.03334 -0.02031 -0.00540 268 MET   A CG   
756  S  SD   . MET   A 116 ? 0.33113 0.36255 0.31317 -0.03577 -0.02775 0.00567  268 MET   A SD   
757  C  CE   . MET   A 116 ? 0.30621 0.34414 0.28228 -0.03736 -0.02510 0.01185  268 MET   A CE   
758  N  N    . LEU   A 117 ? 0.23970 0.24152 0.21525 -0.03159 -0.01581 -0.02075 269 LEU   A N    
759  C  CA   . LEU   A 117 ? 0.25872 0.26208 0.23337 -0.03453 -0.01374 -0.02424 269 LEU   A CA   
760  C  C    . LEU   A 117 ? 0.32269 0.31563 0.28834 -0.03528 -0.00875 -0.02468 269 LEU   A C    
761  O  O    . LEU   A 117 ? 0.28067 0.26972 0.24135 -0.04062 -0.00565 -0.02608 269 LEU   A O    
762  C  CB   . LEU   A 117 ? 0.28403 0.29577 0.26989 -0.03126 -0.01598 -0.02611 269 LEU   A CB   
763  C  CG   . LEU   A 117 ? 0.38285 0.40565 0.38262 -0.03052 -0.02066 -0.02589 269 LEU   A CG   
764  C  CD1  . LEU   A 117 ? 0.37873 0.40638 0.39156 -0.02531 -0.02182 -0.03020 269 LEU   A CD1  
765  C  CD2  . LEU   A 117 ? 0.35279 0.38367 0.35224 -0.03619 -0.02009 -0.02723 269 LEU   A CD2  
766  N  N    . ARG   A 118 ? 0.28848 0.27719 0.25346 -0.03034 -0.00847 -0.02265 270 ARG   A N    
767  C  CA   . ARG   A 118 ? 0.25540 0.23596 0.21377 -0.03031 -0.00492 -0.02027 270 ARG   A CA   
768  C  C    . ARG   A 118 ? 0.27209 0.24000 0.22570 -0.03155 -0.00154 -0.01975 270 ARG   A C    
769  O  O    . ARG   A 118 ? 0.32359 0.28240 0.27394 -0.03366 0.00174  -0.01764 270 ARG   A O    
770  C  CB   . ARG   A 118 ? 0.29676 0.27922 0.25625 -0.02476 -0.00671 -0.01781 270 ARG   A CB   
771  C  CG   . ARG   A 118 ? 0.28832 0.26734 0.25058 -0.02022 -0.00813 -0.01607 270 ARG   A CG   
772  C  CD   . ARG   A 118 ? 0.38320 0.36869 0.34985 -0.01607 -0.01168 -0.01543 270 ARG   A CD   
773  N  NE   . ARG   A 118 ? 0.39409 0.37890 0.35556 -0.01444 -0.01108 -0.01131 270 ARG   A NE   
774  C  CZ   . ARG   A 118 ? 0.35141 0.34408 0.30897 -0.01594 -0.01164 -0.01175 270 ARG   A CZ   
775  N  NH1  . ARG   A 118 ? 0.32737 0.32130 0.27935 -0.01486 -0.01180 -0.00541 270 ARG   A NH1  
776  N  NH2  . ARG   A 118 ? 0.49010 0.49122 0.44994 -0.01839 -0.01196 -0.01820 270 ARG   A NH2  
777  N  N    . SER   A 119 ? 0.26778 0.23541 0.22185 -0.03058 -0.00193 -0.02179 271 SER   A N    
778  C  CA   . SER   A 119 ? 0.28705 0.24442 0.23732 -0.03182 0.00224  -0.02480 271 SER   A CA   
779  C  C    . SER   A 119 ? 0.34307 0.29668 0.29010 -0.03968 0.00433  -0.02963 271 SER   A C    
780  O  O    . SER   A 119 ? 0.34467 0.28618 0.29004 -0.04145 0.00848  -0.03354 271 SER   A O    
781  C  CB   . SER   A 119 ? 0.28161 0.24463 0.23169 -0.03024 0.00198  -0.02683 271 SER   A CB   
782  O  OG   . SER   A 119 ? 0.32175 0.29503 0.26990 -0.03569 -0.00053 -0.02916 271 SER   A OG   
783  N  N    . ASN   A 120 ? 0.30792 0.27187 0.25616 -0.04441 0.00157  -0.03015 272 ASN   A N    
784  C  CA   . ASN   A 120 ? 0.30779 0.27092 0.25456 -0.05303 0.00295  -0.03463 272 ASN   A CA   
785  C  C    . ASN   A 120 ? 0.37508 0.32445 0.32182 -0.05588 0.00718  -0.03270 272 ASN   A C    
786  O  O    . ASN   A 120 ? 0.36115 0.30389 0.30763 -0.06345 0.00948  -0.03730 272 ASN   A O    
787  C  CB   . ASN   A 120 ? 0.25976 0.23932 0.21112 -0.05633 -0.00100 -0.03420 272 ASN   A CB   
788  C  CG   . ASN   A 120 ? 0.33133 0.31504 0.28237 -0.06603 -0.00095 -0.03936 272 ASN   A CG   
789  O  OD1  . ASN   A 120 ? 0.37247 0.35909 0.32702 -0.07110 0.00025  -0.03886 272 ASN   A OD1  
790  N  ND2  . ASN   A 120 ? 0.33259 0.31905 0.27931 -0.06946 -0.00223 -0.04461 272 ASN   A ND2  
791  N  N    . GLN   A 121 ? 0.34323 0.28892 0.29072 -0.05073 0.00780  -0.02542 273 GLN   A N    
792  C  CA   . GLN   A 121 ? 0.35411 0.28765 0.30198 -0.05348 0.01122  -0.01994 273 GLN   A CA   
793  C  C    . GLN   A 121 ? 0.41087 0.32450 0.36065 -0.05291 0.01475  -0.02229 273 GLN   A C    
794  O  O    . GLN   A 121 ? 0.42085 0.32146 0.37360 -0.05864 0.01776  -0.02080 273 GLN   A O    
795  C  CB   . GLN   A 121 ? 0.43582 0.37360 0.38267 -0.04789 0.01014  -0.01071 273 GLN   A CB   
796  C  CG   . GLN   A 121 ? 0.45083 0.38160 0.39726 -0.05180 0.01280  -0.00134 273 GLN   A CG   
797  C  CD   . GLN   A 121 ? 0.47329 0.41667 0.41585 -0.04846 0.01108  0.00686  273 GLN   A CD   
798  O  OE1  . GLN   A 121 ? 0.40205 0.36164 0.34324 -0.04599 0.00860  0.00259  273 GLN   A OE1  
799  N  NE2  . GLN   A 121 ? 0.50146 0.43801 0.44294 -0.04868 0.01216  0.01859  273 GLN   A NE2  
800  N  N    . SER   A 122 ? 0.35203 0.26322 0.30195 -0.04627 0.01487  -0.02628 274 SER   A N    
801  C  CA   . SER   A 122 ? 0.35216 0.24626 0.30588 -0.04445 0.01912  -0.03152 274 SER   A CA   
802  C  C    . SER   A 122 ? 0.42542 0.32003 0.37645 -0.05096 0.02095  -0.04534 274 SER   A C    
803  O  O    . SER   A 122 ? 0.45188 0.33179 0.40670 -0.05131 0.02540  -0.05337 274 SER   A O    
804  C  CB   . SER   A 122 ? 0.35672 0.25079 0.31326 -0.03366 0.01932  -0.02934 274 SER   A CB   
805  O  OG   . SER   A 122 ? 0.44042 0.34955 0.39282 -0.03222 0.01761  -0.03457 274 SER   A OG   
806  N  N    . PHE   A 123 ? 0.38454 0.29660 0.33008 -0.05598 0.01742  -0.04861 275 PHE   A N    
807  C  CA   . PHE   A 123 ? 0.37490 0.29255 0.31601 -0.06293 0.01786  -0.06081 275 PHE   A CA   
808  C  C    . PHE   A 123 ? 0.43308 0.33972 0.37689 -0.07319 0.02006  -0.06740 275 PHE   A C    
809  O  O    . PHE   A 123 ? 0.44617 0.35151 0.39356 -0.07784 0.01909  -0.06080 275 PHE   A O    
810  C  CB   . PHE   A 123 ? 0.35351 0.29419 0.29021 -0.06532 0.01208  -0.05913 275 PHE   A CB   
811  C  CG   . PHE   A 123 ? 0.34275 0.29480 0.27283 -0.07165 0.01120  -0.06930 275 PHE   A CG   
812  C  CD1  . PHE   A 123 ? 0.39025 0.34746 0.31512 -0.06784 0.01301  -0.07348 275 PHE   A CD1  
813  C  CD2  . PHE   A 123 ? 0.32012 0.28070 0.24900 -0.08208 0.00853  -0.07451 275 PHE   A CD2  
814  C  CE1  . PHE   A 123 ? 0.40491 0.37637 0.32131 -0.07452 0.01224  -0.08255 275 PHE   A CE1  
815  C  CE2  . PHE   A 123 ? 0.41198 0.38646 0.33330 -0.08873 0.00679  -0.08376 275 PHE   A CE2  
816  C  CZ   . PHE   A 123 ? 0.40576 0.38607 0.31975 -0.08507 0.00868  -0.08773 275 PHE   A CZ   
817  N  N    . THR   A 124 ? 0.41914 0.31885 0.36182 -0.07744 0.02346  -0.08133 276 THR   A N    
818  C  CA   . THR   A 124 ? 0.48753 0.37699 0.43385 -0.08884 0.02525  -0.09058 276 THR   A CA   
819  C  C    . THR   A 124 ? 0.47739 0.38328 0.41543 -0.09740 0.02336  -0.10505 276 THR   A C    
820  O  O    . THR   A 124 ? 0.44376 0.35689 0.37498 -0.09393 0.02488  -0.11324 276 THR   A O    
821  C  CB   . THR   A 124 ? 0.54076 0.40174 0.49695 -0.08690 0.03162  -0.09589 276 THR   A CB   
822  O  OG1  . THR   A 124 ? 0.62079 0.47185 0.58137 -0.09945 0.03327  -0.10805 276 THR   A OG1  
823  C  CG2  . THR   A 124 ? 0.50317 0.36121 0.45828 -0.07803 0.03587  -0.10544 276 THR   A CG2  
824  N  N    . MET   A 125 ? 0.45904 0.37383 0.39757 -0.10902 0.01989  -0.10756 277 MET   A N    
825  C  CA   . MET   A 125 ? 0.46821 0.40061 0.39912 -0.11892 0.01698  -0.12119 277 MET   A CA   
826  C  C    . MET   A 125 ? 0.60246 0.51891 0.53488 -0.12636 0.02223  -0.14089 277 MET   A C    
827  O  O    . MET   A 125 ? 0.63744 0.56932 0.56138 -0.13461 0.02051  -0.15537 277 MET   A O    
828  C  CB   . MET   A 125 ? 0.54088 0.49143 0.47419 -0.12854 0.01066  -0.11656 277 MET   A CB   
829  C  CG   . MET   A 125 ? 0.52144 0.49320 0.45365 -0.12159 0.00480  -0.10157 277 MET   A CG   
830  S  SD   . MET   A 125 ? 0.60070 0.59725 0.53935 -0.13137 -0.00241 -0.09739 277 MET   A SD   
831  C  CE   . MET   A 125 ? 0.61111 0.58857 0.56183 -0.13577 0.00273  -0.09239 277 MET   A CE   
832  N  N    . ASP   A 126 ? 0.57183 0.45845 0.51559 -0.12359 0.02831  -0.14183 278 ASP   A N    
833  C  CA   . ASP   A 126 ? 0.64922 0.51676 0.59835 -0.12931 0.03402  -0.16203 278 ASP   A CA   
834  C  C    . ASP   A 126 ? 0.63567 0.51310 0.57457 -0.12483 0.03738  -0.17780 278 ASP   A C    
835  O  O    . ASP   A 126 ? 0.67067 0.55248 0.60521 -0.13424 0.03901  -0.19910 278 ASP   A O    
836  C  CB   . ASP   A 126 ? 0.76453 0.59737 0.73052 -0.12384 0.03967  -0.15641 278 ASP   A CB   
837  C  CG   . ASP   A 126 ? 0.94256 0.76569 0.91867 -0.13191 0.03756  -0.14320 278 ASP   A CG   
838  O  OD1  . ASP   A 126 ? 1.00353 0.80230 0.99239 -0.12723 0.04070  -0.13187 278 ASP   A OD1  
839  O  OD2  . ASP   A 126 ? 0.98135 0.82323 0.95329 -0.14310 0.03269  -0.14321 278 ASP   A OD2  
840  N  N    . ASP   A 127 ? 0.63676 0.52003 0.57161 -0.11131 0.03865  -0.16825 279 ASP   A N    
841  C  CA   . ASP   A 127 ? 0.62771 0.52581 0.55202 -0.10749 0.04217  -0.18091 279 ASP   A CA   
842  C  C    . ASP   A 127 ? 0.56884 0.49139 0.48287 -0.09979 0.03801  -0.16528 279 ASP   A C    
843  O  O    . ASP   A 127 ? 0.58900 0.52087 0.49756 -0.09327 0.04214  -0.16983 279 ASP   A O    
844  C  CB   . ASP   A 127 ? 0.73711 0.61173 0.67261 -0.09827 0.05172  -0.19208 279 ASP   A CB   
845  C  CG   . ASP   A 127 ? 0.80835 0.66544 0.75653 -0.08441 0.05286  -0.17295 279 ASP   A CG   
846  O  OD1  . ASP   A 127 ? 0.84535 0.68466 0.80545 -0.07522 0.05984  -0.17922 279 ASP   A OD1  
847  O  OD2  . ASP   A 127 ? 0.78137 0.64366 0.72847 -0.08257 0.04680  -0.15256 279 ASP   A OD2  
848  N  N    . MET   A 128 ? 0.50723 0.44040 0.42031 -0.10056 0.03042  -0.14752 280 MET   A N    
849  C  CA   . MET   A 128 ? 0.48823 0.44447 0.39378 -0.09515 0.02529  -0.13325 280 MET   A CA   
850  C  C    . MET   A 128 ? 0.48271 0.43257 0.39198 -0.08168 0.02951  -0.12584 280 MET   A C    
851  O  O    . MET   A 128 ? 0.47335 0.44054 0.37527 -0.07826 0.02996  -0.12465 280 MET   A O    
852  C  CB   . MET   A 128 ? 0.53117 0.51637 0.42204 -0.10285 0.02205  -0.14074 280 MET   A CB   
853  C  CG   . MET   A 128 ? 0.56811 0.56368 0.45571 -0.11673 0.01676  -0.14837 280 MET   A CG   
854  S  SD   . MET   A 128 ? 0.54528 0.54596 0.44191 -0.11785 0.00792  -0.12913 280 MET   A SD   
855  C  CE   . MET   A 128 ? 0.54401 0.55874 0.43819 -0.13523 0.00293  -0.14205 280 MET   A CE   
856  N  N    . SER   A 129 ? 0.41150 0.33809 0.33286 -0.07463 0.03226  -0.11958 281 SER   A N    
857  C  CA   . SER   A 129 ? 0.42427 0.34443 0.35171 -0.06200 0.03573  -0.11263 281 SER   A CA   
858  C  C    . SER   A 129 ? 0.43692 0.34800 0.37229 -0.05624 0.03199  -0.09494 281 SER   A C    
859  O  O    . SER   A 129 ? 0.44141 0.34533 0.37958 -0.06150 0.02927  -0.09022 281 SER   A O    
860  C  CB   . SER   A 129 ? 0.46973 0.37059 0.40588 -0.05747 0.04439  -0.12605 281 SER   A CB   
861  O  OG   . SER   A 129 ? 0.57107 0.44608 0.52042 -0.05551 0.04523  -0.12075 281 SER   A OG   
862  N  N    . TRP   A 130 ? 0.42363 0.33743 0.36247 -0.04601 0.03211  -0.08567 282 TRP   A N    
863  C  CA   . TRP   A 130 ? 0.39558 0.30259 0.34133 -0.03972 0.02902  -0.07054 282 TRP   A CA   
864  C  C    . TRP   A 130 ? 0.44199 0.32762 0.39934 -0.03275 0.03389  -0.07035 282 TRP   A C    
865  O  O    . TRP   A 130 ? 0.49200 0.37763 0.45494 -0.02410 0.03727  -0.07158 282 TRP   A O    
866  C  CB   . TRP   A 130 ? 0.32502 0.24823 0.26953 -0.03354 0.02536  -0.06100 282 TRP   A CB   
867  C  CG   . TRP   A 130 ? 0.34065 0.28253 0.27818 -0.03897 0.01945  -0.05748 282 TRP   A CG   
868  C  CD1  . TRP   A 130 ? 0.34290 0.28959 0.28162 -0.04030 0.01384  -0.04883 282 TRP   A CD1  
869  C  CD2  . TRP   A 130 ? 0.34532 0.30469 0.27528 -0.04317 0.01854  -0.06178 282 TRP   A CD2  
870  N  NE1  . TRP   A 130 ? 0.34258 0.30646 0.27763 -0.04417 0.00925  -0.04746 282 TRP   A NE1  
871  C  CE2  . TRP   A 130 ? 0.32592 0.29816 0.25490 -0.04635 0.01150  -0.05384 282 TRP   A CE2  
872  C  CE3  . TRP   A 130 ? 0.37946 0.34652 0.30358 -0.04463 0.02318  -0.07149 282 TRP   A CE3  
873  C  CZ2  . TRP   A 130 ? 0.36540 0.35673 0.28870 -0.05080 0.00792  -0.05266 282 TRP   A CZ2  
874  C  CZ3  . TRP   A 130 ? 0.38384 0.37229 0.29925 -0.05013 0.02004  -0.07078 282 TRP   A CZ3  
875  C  CH2  . TRP   A 130 ? 0.36493 0.36474 0.28043 -0.05309 0.01195  -0.06013 282 TRP   A CH2  
876  N  N    . ASP   A 131 ? 0.43572 0.30410 0.39851 -0.03650 0.03414  -0.06757 283 ASP   A N    
877  C  CA   . ASP   A 131 ? 0.51507 0.36035 0.49148 -0.03096 0.03828  -0.06620 283 ASP   A CA   
878  C  C    . ASP   A 131 ? 0.45632 0.30017 0.43766 -0.02392 0.03441  -0.04723 283 ASP   A C    
879  O  O    . ASP   A 131 ? 0.51500 0.35948 0.49328 -0.02900 0.03080  -0.03691 283 ASP   A O    
880  C  CB   . ASP   A 131 ? 0.53218 0.35882 0.51328 -0.04043 0.04060  -0.07272 283 ASP   A CB   
881  C  CG   . ASP   A 131 ? 0.62913 0.42885 0.62780 -0.03476 0.04537  -0.07304 283 ASP   A CG   
882  O  OD1  . ASP   A 131 ? 0.68640 0.46788 0.69206 -0.04238 0.04824  -0.08126 283 ASP   A OD1  
883  O  OD2  . ASP   A 131 ? 0.59259 0.38933 0.60007 -0.02277 0.04597  -0.06510 283 ASP   A OD2  
884  N  N    . CYS   A 132 ? 0.49502 0.33931 0.48416 -0.01266 0.03529  -0.04305 284 CYS   A N    
885  C  CA   . CYS   A 132 ? 0.49555 0.34277 0.48883 -0.00567 0.03075  -0.02573 284 CYS   A CA   
886  C  C    . CYS   A 132 ? 0.53845 0.36619 0.54863 0.00227  0.03282  -0.01856 284 CYS   A C    
887  O  O    . CYS   A 132 ? 0.48227 0.31474 0.50032 0.01215  0.03072  -0.00919 284 CYS   A O    
888  C  CB   . CYS   A 132 ? 0.47360 0.34138 0.46384 0.00057  0.02808  -0.02390 284 CYS   A CB   
889  S  SG   . CYS   A 132 ? 0.41510 0.30481 0.38982 -0.00719 0.02318  -0.02520 284 CYS   A SG   
890  N  N    . GLY   A 133 ? 0.59997 0.40565 0.61797 -0.00206 0.03655  -0.02257 285 GLY   A N    
891  C  CA   . GLY   A 133 ? 0.62052 0.40498 0.65623 0.00379  0.03715  -0.01130 285 GLY   A CA   
892  C  C    . GLY   A 133 ? 0.66305 0.42904 0.71806 0.01191  0.04377  -0.02312 285 GLY   A C    
893  O  O    . GLY   A 133 ? 0.70641 0.44942 0.77949 0.01542  0.04475  -0.01522 285 GLY   A O    
894  N  N    . SER   A 134 ? 0.61872 0.39450 0.67175 0.01510  0.04860  -0.04135 286 SER   A N    
895  C  CA   . SER   A 134 ? 0.64565 0.40733 0.71787 0.02394  0.05612  -0.05518 286 SER   A CA   
896  C  C    . SER   A 134 ? 0.61577 0.39363 0.67741 0.02149  0.06198  -0.07807 286 SER   A C    
897  O  O    . SER   A 134 ? 0.57557 0.37648 0.61755 0.01551  0.05897  -0.07854 286 SER   A O    
898  C  CB   . SER   A 134 ? 0.66703 0.42971 0.75786 0.03960  0.05480  -0.04199 286 SER   A CB   
899  O  OG   . SER   A 134 ? 0.66162 0.45255 0.74180 0.04318  0.05082  -0.03574 286 SER   A OG   
900  N  N    . GLN   A 135 ? 0.58351 0.34959 0.65948 0.02632  0.07056  -0.09698 287 GLN   A N    
901  C  CA   . GLN   A 135 ? 0.63411 0.41691 0.69936 0.02302  0.07726  -0.12032 287 GLN   A CA   
902  C  C    . GLN   A 135 ? 0.62481 0.43774 0.68227 0.02909  0.07663  -0.11571 287 GLN   A C    
903  O  O    . GLN   A 135 ? 0.60211 0.43741 0.64066 0.02184  0.07729  -0.12396 287 GLN   A O    
904  C  CB   . GLN   A 135 ? 0.65562 0.42080 0.74033 0.02853  0.08751  -0.14271 287 GLN   A CB   
905  C  CG   . GLN   A 135 ? 0.85104 0.59632 0.93440 0.01626  0.09022  -0.15990 287 GLN   A CG   
906  C  CD   . GLN   A 135 ? 0.94325 0.71117 0.99919 0.00194  0.08984  -0.17395 287 GLN   A CD   
907  O  OE1  . GLN   A 135 ? 0.98201 0.77759 1.02470 0.00302  0.09232  -0.18098 287 GLN   A OE1  
908  N  NE2  . GLN   A 135 ? 0.95863 0.71653 1.00686 -0.01199 0.08635  -0.17666 287 GLN   A NE2  
909  N  N    . ASP   A 136 ? 0.55253 0.36744 0.62544 0.04182  0.07488  -0.10154 288 ASP   A N    
910  C  CA   . ASP   A 136 ? 0.53659 0.37998 0.60495 0.04683  0.07403  -0.09649 288 ASP   A CA   
911  C  C    . ASP   A 136 ? 0.51107 0.37192 0.55740 0.03749  0.06540  -0.08397 288 ASP   A C    
912  O  O    . ASP   A 136 ? 0.49221 0.37705 0.52762 0.03504  0.06570  -0.08614 288 ASP   A O    
913  C  CB   . ASP   A 136 ? 0.60002 0.44257 0.69117 0.06163  0.07243  -0.08265 288 ASP   A CB   
914  C  CG   . ASP   A 136 ? 0.73922 0.57496 0.85443 0.07344  0.08261  -0.09771 288 ASP   A CG   
915  O  OD1  . ASP   A 136 ? 0.81664 0.64884 0.92903 0.06952  0.09147  -0.12067 288 ASP   A OD1  
916  O  OD2  . ASP   A 136 ? 0.81440 0.65019 0.95203 0.08675  0.08174  -0.08741 288 ASP   A OD2  
917  N  N    . TYR   A 137 ? 0.51191 0.36141 0.55291 0.03212  0.05804  -0.07076 289 TYR   A N    
918  C  CA   . TYR   A 137 ? 0.42124 0.28537 0.44448 0.02418  0.05012  -0.05994 289 TYR   A CA   
919  C  C    . TYR   A 137 ? 0.40884 0.26860 0.41707 0.01107  0.04931  -0.06717 289 TYR   A C    
920  O  O    . TYR   A 137 ? 0.45548 0.31511 0.45561 0.00491  0.04310  -0.05693 289 TYR   A O    
921  C  CB   . TYR   A 137 ? 0.45248 0.31396 0.48023 0.02798  0.04232  -0.03948 289 TYR   A CB   
922  C  CG   . TYR   A 137 ? 0.40445 0.26924 0.44992 0.04099  0.04207  -0.03127 289 TYR   A CG   
923  C  CD1  . TYR   A 137 ? 0.48873 0.34091 0.54694 0.04714  0.03816  -0.01629 289 TYR   A CD1  
924  C  CD2  . TYR   A 137 ? 0.42800 0.31059 0.47839 0.04677  0.04558  -0.03736 289 TYR   A CD2  
925  C  CE1  . TYR   A 137 ? 0.53634 0.39399 0.61238 0.05939  0.03689  -0.00775 289 TYR   A CE1  
926  C  CE2  . TYR   A 137 ? 0.48854 0.37672 0.55733 0.05866  0.04521  -0.03003 289 TYR   A CE2  
927  C  CZ   . TYR   A 137 ? 0.51508 0.39086 0.59703 0.06529  0.04045  -0.01534 289 TYR   A CZ   
928  O  OH   . TYR   A 137 ? 0.49852 0.38214 0.60034 0.07748  0.03900  -0.00687 289 TYR   A OH   
929  N  N    . LYS   A 138 ? 0.42357 0.28191 0.42853 0.00652  0.05576  -0.08585 290 LYS   A N    
930  C  CA   . LYS   A 138 ? 0.40657 0.26713 0.39674 -0.00656 0.05466  -0.09464 290 LYS   A CA   
931  C  C    . LYS   A 138 ? 0.45038 0.33607 0.42718 -0.01025 0.05651  -0.10419 290 LYS   A C    
932  O  O    . LYS   A 138 ? 0.49135 0.38224 0.47115 -0.00673 0.06401  -0.11798 290 LYS   A O    
933  C  CB   . LYS   A 138 ? 0.50176 0.33942 0.49940 -0.01091 0.05982  -0.10893 290 LYS   A CB   
934  C  CG   . LYS   A 138 ? 0.61077 0.45269 0.59448 -0.02533 0.05866  -0.12025 290 LYS   A CG   
935  C  CD   . LYS   A 138 ? 0.74480 0.55972 0.73943 -0.03067 0.06181  -0.12971 290 LYS   A CD   
936  C  CE   . LYS   A 138 ? 0.78174 0.60237 0.76404 -0.04606 0.05990  -0.14109 290 LYS   A CE   
937  N  NZ   . LYS   A 138 ? 0.89038 0.69521 0.88000 -0.05128 0.06664  -0.16465 290 LYS   A NZ   
938  N  N    . TYR   A 139 ? 0.41837 0.32061 0.38155 -0.01716 0.04994  -0.09644 291 TYR   A N    
939  C  CA   . TYR   A 139 ? 0.41971 0.34776 0.37176 -0.01979 0.04960  -0.09793 291 TYR   A CA   
940  C  C    . TYR   A 139 ? 0.44915 0.38763 0.38640 -0.03209 0.04756  -0.10623 291 TYR   A C    
941  O  O    . TYR   A 139 ? 0.39063 0.32360 0.32498 -0.03851 0.04206  -0.10193 291 TYR   A O    
942  C  CB   . TYR   A 139 ? 0.36848 0.30833 0.32061 -0.01662 0.04266  -0.08009 291 TYR   A CB   
943  C  CG   . TYR   A 139 ? 0.39298 0.32339 0.35913 -0.00607 0.04218  -0.07012 291 TYR   A CG   
944  C  CD1  . TYR   A 139 ? 0.38920 0.30830 0.35890 -0.00510 0.03653  -0.05869 291 TYR   A CD1  
945  C  CD2  . TYR   A 139 ? 0.38903 0.32488 0.36496 0.00258  0.04734  -0.07200 291 TYR   A CD2  
946  C  CE1  . TYR   A 139 ? 0.34451 0.25837 0.32567 0.00383  0.03505  -0.04869 291 TYR   A CE1  
947  C  CE2  . TYR   A 139 ? 0.39518 0.32518 0.38499 0.01214  0.04578  -0.06205 291 TYR   A CE2  
948  C  CZ   . TYR   A 139 ? 0.41103 0.33018 0.40269 0.01254  0.03914  -0.05008 291 TYR   A CZ   
949  O  OH   . TYR   A 139 ? 0.39990 0.31643 0.40405 0.02139  0.03661  -0.03936 291 TYR   A OH   
950  N  N    . ASP   A 140 ? 0.49640 0.45265 0.42443 -0.03567 0.05193  -0.11777 292 ASP   A N    
951  C  CA   . ASP   A 140 ? 0.50796 0.47987 0.42063 -0.04768 0.04922  -0.12505 292 ASP   A CA   
952  C  C    . ASP   A 140 ? 0.44082 0.44218 0.34282 -0.04983 0.04655  -0.11669 292 ASP   A C    
953  O  O    . ASP   A 140 ? 0.46610 0.47361 0.37365 -0.04276 0.04672  -0.10541 292 ASP   A O    
954  C  CB   . ASP   A 140 ? 0.56230 0.52931 0.47198 -0.05283 0.05669  -0.14889 292 ASP   A CB   
955  C  CG   . ASP   A 140 ? 0.58769 0.56506 0.49771 -0.04745 0.06674  -0.16200 292 ASP   A CG   
956  O  OD1  . ASP   A 140 ? 0.66057 0.63256 0.57064 -0.05022 0.07410  -0.18417 292 ASP   A OD1  
957  O  OD2  . ASP   A 140 ? 0.53077 0.52217 0.44226 -0.04087 0.06784  -0.15167 292 ASP   A OD2  
958  N  N    . VAL   A 141 ? 0.46883 0.48935 0.35623 -0.06042 0.04359  -0.12147 293 VAL   A N    
959  C  CA   . VAL   A 141 ? 0.43283 0.48215 0.31011 -0.06397 0.03969  -0.11035 293 VAL   A CA   
960  C  C    . VAL   A 141 ? 0.44378 0.50734 0.31977 -0.05951 0.04819  -0.11381 293 VAL   A C    
961  O  O    . VAL   A 141 ? 0.44599 0.52676 0.32126 -0.05853 0.04580  -0.09877 293 VAL   A O    
962  C  CB   . VAL   A 141 ? 0.42733 0.49668 0.28890 -0.07657 0.03486  -0.11556 293 VAL   A CB   
963  C  CG1  . VAL   A 141 ? 0.42540 0.48543 0.29107 -0.08047 0.02569  -0.10855 293 VAL   A CG1  
964  C  CG2  . VAL   A 141 ? 0.47174 0.54308 0.32449 -0.08224 0.04295  -0.14095 293 VAL   A CG2  
965  N  N    . THR   A 142 ? 0.48412 0.54110 0.36185 -0.05682 0.05853  -0.13366 294 THR   A N    
966  C  CA   . THR   A 142 ? 0.44497 0.51798 0.32315 -0.05213 0.06801  -0.13883 294 THR   A CA   
967  C  C    . THR   A 142 ? 0.39527 0.45908 0.29092 -0.04046 0.06860  -0.12479 294 THR   A C    
968  O  O    . THR   A 142 ? 0.42318 0.50689 0.31956 -0.03827 0.07217  -0.11827 294 THR   A O    
969  C  CB   . THR   A 142 ? 0.54378 0.61126 0.42253 -0.05121 0.07953  -0.16626 294 THR   A CB   
970  O  OG1  . THR   A 142 ? 0.69354 0.72674 0.59100 -0.04260 0.08145  -0.17116 294 THR   A OG1  
971  C  CG2  . THR   A 142 ? 0.50207 0.58018 0.36310 -0.06427 0.07835  -0.18228 294 THR   A CG2  
972  N  N    . ASP   A 143 ? 0.41193 0.44803 0.32154 -0.03381 0.06494  -0.11949 295 ASP   A N    
973  C  CA   . ASP   A 143 ? 0.42187 0.45137 0.34720 -0.02370 0.06372  -0.10556 295 ASP   A CA   
974  C  C    . ASP   A 143 ? 0.39674 0.44161 0.31949 -0.02661 0.05550  -0.08540 295 ASP   A C    
975  O  O    . ASP   A 143 ? 0.38176 0.43770 0.31229 -0.02221 0.05698  -0.07672 295 ASP   A O    
976  C  CB   . ASP   A 143 ? 0.40916 0.40890 0.34712 -0.01767 0.06040  -0.10271 295 ASP   A CB   
977  C  CG   . ASP   A 143 ? 0.46980 0.45132 0.41838 -0.01156 0.06897  -0.11901 295 ASP   A CG   
978  O  OD1  . ASP   A 143 ? 0.49029 0.48127 0.44422 -0.00640 0.07804  -0.12939 295 ASP   A OD1  
979  O  OD2  . ASP   A 143 ? 0.51916 0.47705 0.47258 -0.01181 0.06694  -0.12116 295 ASP   A OD2  
980  N  N    . VAL   A 144 ? 0.37962 0.42538 0.29384 -0.03405 0.04674  -0.07793 296 VAL   A N    
981  C  CA   . VAL   A 144 ? 0.34344 0.40184 0.25799 -0.03670 0.03866  -0.05942 296 VAL   A CA   
982  C  C    . VAL   A 144 ? 0.34981 0.43669 0.25622 -0.04175 0.04175  -0.05571 296 VAL   A C    
983  O  O    . VAL   A 144 ? 0.35991 0.45708 0.27289 -0.04113 0.03891  -0.04078 296 VAL   A O    
984  C  CB   . VAL   A 144 ? 0.41986 0.47405 0.32953 -0.04273 0.02922  -0.05373 296 VAL   A CB   
985  C  CG1  . VAL   A 144 ? 0.36201 0.42539 0.27696 -0.04383 0.02070  -0.03499 296 VAL   A CG1  
986  C  CG2  . VAL   A 144 ? 0.41925 0.44820 0.33560 -0.03911 0.02768  -0.05798 296 VAL   A CG2  
987  N  N    . SER   A 145 ? 0.36853 0.46965 0.26072 -0.04762 0.04772  -0.06928 297 SER   A N    
988  C  CA   . SER   A 145 ? 0.36550 0.49746 0.24796 -0.05302 0.05208  -0.06630 297 SER   A CA   
989  C  C    . SER   A 145 ? 0.40679 0.54468 0.30059 -0.04571 0.06101  -0.06691 297 SER   A C    
990  O  O    . SER   A 145 ? 0.36172 0.52178 0.25560 -0.04859 0.06181  -0.05430 297 SER   A O    
991  C  CB   . SER   A 145 ? 0.46200 0.60947 0.32562 -0.06103 0.05735  -0.08429 297 SER   A CB   
992  O  OG   . SER   A 145 ? 0.61254 0.79443 0.46216 -0.06941 0.05821  -0.07679 297 SER   A OG   
993  N  N    . LYS   A 146 ? 0.39485 0.51393 0.30021 -0.03637 0.06749  -0.08013 298 LYS   A N    
994  C  CA   . LYS   A 146 ? 0.40768 0.53271 0.32721 -0.02808 0.07579  -0.08146 298 LYS   A CA   
995  C  C    . LYS   A 146 ? 0.40667 0.52446 0.34291 -0.02281 0.06897  -0.06278 298 LYS   A C    
996  O  O    . LYS   A 146 ? 0.40579 0.52732 0.35689 -0.01538 0.07426  -0.06257 298 LYS   A O    
997  C  CB   . LYS   A 146 ? 0.42647 0.53404 0.35523 -0.01916 0.08465  -0.10193 298 LYS   A CB   
998  C  CG   . LYS   A 146 ? 0.51008 0.63032 0.42575 -0.02366 0.09477  -0.12465 298 LYS   A CG   
999  C  CD   . LYS   A 146 ? 0.63336 0.73146 0.56191 -0.01456 0.10299  -0.14564 298 LYS   A CD   
1000 C  CE   . LYS   A 146 ? 0.71612 0.82638 0.63164 -0.02016 0.11293  -0.17146 298 LYS   A CE   
1001 N  NZ   . LYS   A 146 ? 0.71014 0.79095 0.63676 -0.01462 0.11757  -0.19213 298 LYS   A NZ   
1002 N  N    . ALA   A 147 ? 0.36178 0.47030 0.29727 -0.02638 0.05747  -0.04853 299 ALA   A N    
1003 C  CA   . ALA   A 147 ? 0.36928 0.47601 0.31856 -0.02428 0.05044  -0.03131 299 ALA   A CA   
1004 C  C    . ALA   A 147 ? 0.39510 0.52207 0.34038 -0.03314 0.04581  -0.01520 299 ALA   A C    
1005 O  O    . ALA   A 147 ? 0.36521 0.49053 0.32296 -0.03304 0.03937  -0.00094 299 ALA   A O    
1006 C  CB   . ALA   A 147 ? 0.38088 0.46234 0.33558 -0.02112 0.04124  -0.02759 299 ALA   A CB   
1007 N  N    . GLY   A 148 ? 0.37243 0.51869 0.30126 -0.04125 0.04853  -0.01689 300 GLY   A N    
1008 C  CA   . GLY   A 148 ? 0.40291 0.57162 0.32771 -0.05014 0.04481  0.00049  300 GLY   A CA   
1009 C  C    . GLY   A 148 ? 0.42376 0.59314 0.33811 -0.05739 0.03509  0.00900  300 GLY   A C    
1010 O  O    . GLY   A 148 ? 0.41607 0.60485 0.32724 -0.06503 0.03121  0.02547  300 GLY   A O    
1011 N  N    . HIS   A 149 ? 0.35691 0.50731 0.26727 -0.05553 0.03082  -0.00021 301 HIS   A N    
1012 C  CA   . HIS   A 149 ? 0.33061 0.48189 0.23551 -0.06133 0.02061  0.00892  301 HIS   A CA   
1013 C  C    . HIS   A 149 ? 0.38782 0.55854 0.27139 -0.06950 0.02267  0.00056  301 HIS   A C    
1014 O  O    . HIS   A 149 ? 0.42200 0.59786 0.29500 -0.06968 0.03221  -0.01786 301 HIS   A O    
1015 C  CB   . HIS   A 149 ? 0.30319 0.42719 0.21655 -0.05606 0.01436  0.00494  301 HIS   A CB   
1016 C  CG   . HIS   A 149 ? 0.30237 0.41177 0.23504 -0.05031 0.00943  0.01532  301 HIS   A CG   
1017 N  ND1  . HIS   A 149 ? 0.28724 0.40201 0.23053 -0.05294 0.00171  0.03342  301 HIS   A ND1  
1018 C  CD2  . HIS   A 149 ? 0.32622 0.41687 0.26999 -0.04256 0.01082  0.00981  301 HIS   A CD2  
1019 C  CE1  . HIS   A 149 ? 0.30824 0.40765 0.26817 -0.04737 -0.00104 0.03614  301 HIS   A CE1  
1020 N  NE2  . HIS   A 149 ? 0.31137 0.39763 0.27064 -0.04123 0.00415  0.02241  301 HIS   A NE2  
1021 N  N    . THR   A 150 ? 0.37726 0.55972 0.25593 -0.07628 0.01320  0.01400  302 THR   A N    
1022 C  CA   . THR   A 150 ? 0.39876 0.60584 0.25689 -0.08584 0.01245  0.01057  302 THR   A CA   
1023 C  C    . THR   A 150 ? 0.37712 0.57420 0.23307 -0.08759 0.00417  0.00571  302 THR   A C    
1024 O  O    . THR   A 150 ? 0.37791 0.55069 0.24843 -0.08153 -0.00073 0.00702  302 THR   A O    
1025 C  CB   . THR   A 150 ? 0.43072 0.66684 0.28484 -0.09357 0.00744  0.03399  302 THR   A CB   
1026 O  OG1  . THR   A 150 ? 0.45068 0.67803 0.32000 -0.09259 -0.00536 0.05432  302 THR   A OG1  
1027 C  CG2  . THR   A 150 ? 0.42609 0.67162 0.28632 -0.09236 0.01523  0.04152  302 THR   A CG2  
1028 N  N    . LEU   A 151 ? 0.35928 0.57846 0.19654 -0.09674 0.00277  -0.00031 303 LEU   A N    
1029 C  CA   . LEU   A 151 ? 0.35952 0.57403 0.19439 -0.10005 -0.00497 -0.00590 303 LEU   A CA   
1030 C  C    . LEU   A 151 ? 0.37110 0.58316 0.22114 -0.09852 -0.01804 0.01635  303 LEU   A C    
1031 O  O    . LEU   A 151 ? 0.39996 0.59951 0.25703 -0.09729 -0.02377 0.01260  303 LEU   A O    
1032 C  CB   . LEU   A 151 ? 0.38217 0.62607 0.19367 -0.11155 -0.00480 -0.01601 303 LEU   A CB   
1033 C  CG   . LEU   A 151 ? 0.59059 0.83240 0.39785 -0.11684 -0.01108 -0.02744 303 LEU   A CG   
1034 C  CD1  . LEU   A 151 ? 0.60031 0.85327 0.38775 -0.12464 -0.00315 -0.05432 303 LEU   A CD1  
1035 C  CD2  . LEU   A 151 ? 0.63600 0.90093 0.44304 -0.12283 -0.02521 -0.00647 303 LEU   A CD2  
1036 N  N    . GLU   A 152 ? 0.38267 0.60681 0.23982 -0.09869 -0.02254 0.03943  304 GLU   A N    
1037 C  CA   . GLU   A 152 ? 0.39754 0.61663 0.27389 -0.09581 -0.03453 0.06028  304 GLU   A CA   
1038 C  C    . GLU   A 152 ? 0.37639 0.56277 0.27201 -0.08619 -0.03508 0.05367  304 GLU   A C    
1039 O  O    . GLU   A 152 ? 0.37489 0.55561 0.28389 -0.08388 -0.04383 0.06036  304 GLU   A O    
1040 C  CB   . GLU   A 152 ? 0.51361 0.74321 0.39937 -0.09636 -0.03736 0.08483  304 GLU   A CB   
1041 C  CG   . GLU   A 152 ? 0.68477 0.95029 0.55686 -0.10648 -0.04276 0.10218  304 GLU   A CG   
1042 C  CD   . GLU   A 152 ? 0.85591 1.14457 0.70610 -0.11318 -0.03203 0.09593  304 GLU   A CD   
1043 O  OE1  . GLU   A 152 ? 0.92581 1.24179 0.77006 -0.12030 -0.03455 0.11641  304 GLU   A OE1  
1044 O  OE2  . GLU   A 152 ? 0.90529 1.18562 0.74544 -0.11124 -0.02084 0.07105  304 GLU   A OE2  
1045 N  N    . LEU   A 153 ? 0.31283 0.47976 0.21069 -0.08041 -0.02585 0.04090  305 LEU   A N    
1046 C  CA   . LEU   A 153 ? 0.29329 0.43205 0.20514 -0.07233 -0.02531 0.03270  305 LEU   A CA   
1047 C  C    . LEU   A 153 ? 0.34315 0.47098 0.24524 -0.07281 -0.02001 0.01146  305 LEU   A C    
1048 O  O    . LEU   A 153 ? 0.34291 0.45722 0.25288 -0.07040 -0.02330 0.00751  305 LEU   A O    
1049 C  CB   . LEU   A 153 ? 0.28439 0.40899 0.20698 -0.06565 -0.01995 0.03402  305 LEU   A CB   
1050 C  CG   . LEU   A 153 ? 0.27783 0.37631 0.21190 -0.05775 -0.01855 0.02494  305 LEU   A CG   
1051 C  CD1  . LEU   A 153 ? 0.31762 0.40878 0.26772 -0.05505 -0.02758 0.03316  305 LEU   A CD1  
1052 C  CD2  . LEU   A 153 ? 0.27888 0.36853 0.22063 -0.05239 -0.01312 0.02482  305 LEU   A CD2  
1053 N  N    . ILE   A 154 ? 0.36647 0.50067 0.25273 -0.07634 -0.01156 -0.00251 306 ILE   A N    
1054 C  CA   . ILE   A 154 ? 0.33557 0.45311 0.21723 -0.07544 -0.00503 -0.02303 306 ILE   A CA   
1055 C  C    . ILE   A 154 ? 0.35437 0.47566 0.23072 -0.08220 -0.01026 -0.02973 306 ILE   A C    
1056 O  O    . ILE   A 154 ? 0.34775 0.45020 0.23009 -0.08040 -0.00968 -0.03811 306 ILE   A O    
1057 C  CB   . ILE   A 154 ? 0.35995 0.48270 0.22981 -0.07648 0.00597  -0.03760 306 ILE   A CB   
1058 C  CG1  . ILE   A 154 ? 0.36193 0.47772 0.24155 -0.06840 0.01163  -0.03245 306 ILE   A CG1  
1059 C  CG2  . ILE   A 154 ? 0.36418 0.47018 0.23053 -0.07697 0.01192  -0.05909 306 ILE   A CG2  
1060 C  CD1  . ILE   A 154 ? 0.37169 0.49870 0.24245 -0.06872 0.02270  -0.04432 306 ILE   A CD1  
1061 N  N    A GLU   A 155 ? 0.38243 0.52988 0.24783 -0.09073 -0.01569 -0.02532 307 GLU   A N    
1062 N  N    B GLU   A 155 ? 0.38506 0.53256 0.25037 -0.09076 -0.01564 -0.02541 307 GLU   A N    
1063 C  CA   A GLU   A 155 ? 0.35653 0.51106 0.21827 -0.09792 -0.02175 -0.03120 307 GLU   A CA   
1064 C  CA   B GLU   A 155 ? 0.35213 0.50679 0.21386 -0.09794 -0.02178 -0.03112 307 GLU   A CA   
1065 C  C    A GLU   A 155 ? 0.37268 0.51772 0.25245 -0.09376 -0.02992 -0.02048 307 GLU   A C    
1066 C  C    B GLU   A 155 ? 0.37356 0.51832 0.25342 -0.09365 -0.02983 -0.02050 307 GLU   A C    
1067 O  O    A GLU   A 155 ? 0.39417 0.52765 0.27759 -0.09522 -0.02966 -0.03089 307 GLU   A O    
1068 O  O    B GLU   A 155 ? 0.39256 0.52522 0.27617 -0.09493 -0.02939 -0.03098 307 GLU   A O    
1069 C  CB   A GLU   A 155 ? 0.42345 0.61236 0.26945 -0.10812 -0.02708 -0.02689 307 GLU   A CB   
1070 C  CB   B GLU   A 155 ? 0.42362 0.61270 0.26995 -0.10806 -0.02736 -0.02633 307 GLU   A CB   
1071 C  CG   A GLU   A 155 ? 0.48597 0.68783 0.33022 -0.11611 -0.03579 -0.02965 307 GLU   A CG   
1072 C  CG   B GLU   A 155 ? 0.48607 0.68766 0.33050 -0.11610 -0.03583 -0.02978 307 GLU   A CG   
1073 C  CD   A GLU   A 155 ? 0.50677 0.73178 0.32896 -0.12823 -0.03422 -0.04556 307 GLU   A CD   
1074 C  CD   B GLU   A 155 ? 0.58080 0.80852 0.42942 -0.11866 -0.04867 -0.00713 307 GLU   A CD   
1075 O  OE1  A GLU   A 155 ? 0.55380 0.79460 0.37304 -0.13653 -0.04209 -0.04813 307 GLU   A OE1  
1076 O  OE1  B GLU   A 155 ? 0.65750 0.89340 0.50905 -0.11531 -0.05064 0.01126  307 GLU   A OE1  
1077 O  OE2  A GLU   A 155 ? 0.58936 0.81849 0.39783 -0.12966 -0.02495 -0.05666 307 GLU   A OE2  
1078 O  OE2  B GLU   A 155 ? 0.66217 0.90280 0.51300 -0.12417 -0.05712 -0.00670 307 GLU   A OE2  
1079 N  N    . PRO   A 156 ? 0.34193 0.49114 0.23495 -0.08879 -0.03673 -0.00087 308 PRO   A N    
1080 C  CA   . PRO   A 156 ? 0.32146 0.46030 0.23374 -0.08357 -0.04272 0.00540  308 PRO   A CA   
1081 C  C    . PRO   A 156 ? 0.34381 0.45496 0.26390 -0.07676 -0.03604 -0.00425 308 PRO   A C    
1082 O  O    . PRO   A 156 ? 0.33193 0.43582 0.26217 -0.07528 -0.03818 -0.00669 308 PRO   A O    
1083 C  CB   . PRO   A 156 ? 0.34148 0.48763 0.26772 -0.07894 -0.04978 0.02673  308 PRO   A CB   
1084 C  CG   . PRO   A 156 ? 0.40722 0.57638 0.31898 -0.08542 -0.05082 0.03478  308 PRO   A CG   
1085 C  CD   . PRO   A 156 ? 0.34484 0.50951 0.23801 -0.08837 -0.03967 0.01675  308 PRO   A CD   
1086 N  N    . LEU   A 157 ? 0.32292 0.42085 0.23878 -0.07279 -0.02800 -0.00926 309 LEU   A N    
1087 C  CA   . LEU   A 157 ? 0.29371 0.36763 0.21612 -0.06658 -0.02244 -0.01666 309 LEU   A CA   
1088 C  C    . LEU   A 157 ? 0.31938 0.38389 0.23517 -0.07110 -0.01805 -0.03186 309 LEU   A C    
1089 O  O    . LEU   A 157 ? 0.31683 0.36772 0.24030 -0.06885 -0.01733 -0.03434 309 LEU   A O    
1090 C  CB   . LEU   A 157 ? 0.30367 0.36888 0.22496 -0.06116 -0.01589 -0.01693 309 LEU   A CB   
1091 C  CG   . LEU   A 157 ? 0.31669 0.35953 0.24315 -0.05483 -0.01030 -0.02363 309 LEU   A CG   
1092 C  CD1  . LEU   A 157 ? 0.29174 0.32691 0.23185 -0.05013 -0.01493 -0.01735 309 LEU   A CD1  
1093 C  CD2  . LEU   A 157 ? 0.34773 0.38688 0.27406 -0.04984 -0.00453 -0.02349 309 LEU   A CD2  
1094 N  N    . ILE   A 158 ? 0.31114 0.38331 0.21313 -0.07815 -0.01481 -0.04249 310 ILE   A N    
1095 C  CA   . ILE   A 158 ? 0.34182 0.40409 0.23970 -0.08388 -0.01106 -0.05773 310 ILE   A CA   
1096 C  C    . ILE   A 158 ? 0.35978 0.43032 0.26319 -0.08961 -0.01809 -0.05575 310 ILE   A C    
1097 O  O    . ILE   A 158 ? 0.37051 0.42754 0.27979 -0.09104 -0.01619 -0.06122 310 ILE   A O    
1098 C  CB   . ILE   A 158 ? 0.40796 0.47835 0.29078 -0.09071 -0.00610 -0.07214 310 ILE   A CB   
1099 C  CG1  . ILE   A 158 ? 0.44561 0.50210 0.32740 -0.08388 0.00339  -0.07835 310 ILE   A CG1  
1100 C  CG2  . ILE   A 158 ? 0.45822 0.52378 0.33812 -0.09987 -0.00514 -0.08755 310 ILE   A CG2  
1101 C  CD1  . ILE   A 158 ? 0.47258 0.50041 0.36389 -0.07879 0.00881  -0.08428 310 ILE   A CD1  
1102 N  N    . LYS   A 159 ? 0.35234 0.44667 0.25534 -0.09307 -0.02642 -0.04661 311 LYS   A N    
1103 C  CA   . LYS   A 159 ? 0.37414 0.47996 0.28528 -0.09775 -0.03373 -0.04389 311 LYS   A CA   
1104 C  C    . LYS   A 159 ? 0.32101 0.41528 0.24961 -0.09007 -0.03463 -0.03667 311 LYS   A C    
1105 O  O    . LYS   A 159 ? 0.33851 0.43306 0.27474 -0.09336 -0.03579 -0.03998 311 LYS   A O    
1106 C  CB   . LYS   A 159 ? 0.39769 0.53271 0.30698 -0.10152 -0.04338 -0.03272 311 LYS   A CB   
1107 C  CG   . LYS   A 159 ? 0.52418 0.67695 0.41444 -0.11245 -0.04341 -0.04289 311 LYS   A CG   
1108 C  CD   . LYS   A 159 ? 0.61640 0.80000 0.50107 -0.11582 -0.05236 -0.02890 311 LYS   A CD   
1109 C  CE   . LYS   A 159 ? 0.67706 0.88112 0.54036 -0.12808 -0.05192 -0.04205 311 LYS   A CE   
1110 N  NZ   . LYS   A 159 ? 0.75809 0.97555 0.62242 -0.13798 -0.05819 -0.05011 311 LYS   A NZ   
1111 N  N    . PHE   A 160 ? 0.32274 0.40845 0.25809 -0.08049 -0.03377 -0.02771 312 PHE   A N    
1112 C  CA   . PHE   A 160 ? 0.32363 0.39831 0.27372 -0.07332 -0.03334 -0.02412 312 PHE   A CA   
1113 C  C    . PHE   A 160 ? 0.36440 0.42021 0.31181 -0.07422 -0.02579 -0.03411 312 PHE   A C    
1114 O  O    . PHE   A 160 ? 0.30208 0.35688 0.25781 -0.07502 -0.02565 -0.03530 312 PHE   A O    
1115 C  CB   . PHE   A 160 ? 0.30134 0.37006 0.25825 -0.06420 -0.03372 -0.01498 312 PHE   A CB   
1116 C  CG   . PHE   A 160 ? 0.28451 0.34150 0.25381 -0.05717 -0.03207 -0.01472 312 PHE   A CG   
1117 C  CD1  . PHE   A 160 ? 0.32207 0.38719 0.30813 -0.05368 -0.03726 -0.00978 312 PHE   A CD1  
1118 C  CD2  . PHE   A 160 ? 0.27612 0.31581 0.24092 -0.05394 -0.02539 -0.01981 312 PHE   A CD2  
1119 C  CE1  . PHE   A 160 ? 0.32658 0.38353 0.32285 -0.04774 -0.03494 -0.01213 312 PHE   A CE1  
1120 C  CE2  . PHE   A 160 ? 0.35156 0.38417 0.32530 -0.04855 -0.02414 -0.01994 312 PHE   A CE2  
1121 C  CZ   . PHE   A 160 ? 0.35185 0.39350 0.34043 -0.04577 -0.02850 -0.01719 312 PHE   A CZ   
1122 N  N    . GLN   A 161 ? 0.32519 0.36688 0.26236 -0.07397 -0.01926 -0.04049 313 GLN   A N    
1123 C  CA   . GLN   A 161 ? 0.34604 0.36837 0.28230 -0.07452 -0.01259 -0.04751 313 GLN   A CA   
1124 C  C    . GLN   A 161 ? 0.32242 0.34669 0.25845 -0.08451 -0.01247 -0.05508 313 GLN   A C    
1125 O  O    . GLN   A 161 ? 0.28890 0.30462 0.23073 -0.08580 -0.00999 -0.05523 313 GLN   A O    
1126 C  CB   . GLN   A 161 ? 0.33298 0.34148 0.26114 -0.07219 -0.00615 -0.05337 313 GLN   A CB   
1127 C  CG   . GLN   A 161 ? 0.30275 0.30897 0.23281 -0.06289 -0.00550 -0.04615 313 GLN   A CG   
1128 C  CD   . GLN   A 161 ? 0.28078 0.27782 0.21958 -0.05616 -0.00553 -0.03977 313 GLN   A CD   
1129 O  OE1  . GLN   A 161 ? 0.32931 0.31645 0.27008 -0.05747 -0.00312 -0.04157 313 GLN   A OE1  
1130 N  NE2  . GLN   A 161 ? 0.31338 0.31475 0.25748 -0.04975 -0.00828 -0.03225 313 GLN   A NE2  
1131 N  N    . VAL   A 162 ? 0.32003 0.35754 0.24933 -0.09263 -0.01528 -0.06114 314 VAL   A N    
1132 C  CA   . VAL   A 162 ? 0.34964 0.39103 0.27969 -0.10374 -0.01597 -0.06949 314 VAL   A CA   
1133 C  C    . VAL   A 162 ? 0.33849 0.39418 0.28114 -0.10474 -0.02125 -0.06227 314 VAL   A C    
1134 O  O    . VAL   A 162 ? 0.34574 0.39697 0.29480 -0.11001 -0.01899 -0.06504 314 VAL   A O    
1135 C  CB   . VAL   A 162 ? 0.39159 0.44810 0.31053 -0.11269 -0.01870 -0.07865 314 VAL   A CB   
1136 C  CG1  . VAL   A 162 ? 0.36903 0.43500 0.29092 -0.12522 -0.02168 -0.08649 314 VAL   A CG1  
1137 C  CG2  . VAL   A 162 ? 0.35726 0.39872 0.26562 -0.11241 -0.01128 -0.09006 314 VAL   A CG2  
1138 N  N    . GLY   A 163 ? 0.35272 0.42627 0.30102 -0.09965 -0.02807 -0.05250 315 GLY   A N    
1139 C  CA   . GLY   A 163 ? 0.32482 0.41330 0.28849 -0.09887 -0.03284 -0.04646 315 GLY   A CA   
1140 C  C    . GLY   A 163 ? 0.31293 0.38928 0.28565 -0.09286 -0.02767 -0.04436 315 GLY   A C    
1141 O  O    . GLY   A 163 ? 0.29765 0.38165 0.28044 -0.09624 -0.02724 -0.04510 315 GLY   A O    
1142 N  N    . LEU   A 164 ? 0.27814 0.33820 0.24724 -0.08449 -0.02365 -0.04180 316 LEU   A N    
1143 C  CA   . LEU   A 164 ? 0.28951 0.34029 0.26439 -0.07943 -0.01893 -0.04016 316 LEU   A CA   
1144 C  C    . LEU   A 164 ? 0.32571 0.36397 0.29611 -0.08670 -0.01252 -0.04498 316 LEU   A C    
1145 O  O    . LEU   A 164 ? 0.34671 0.38807 0.32376 -0.08813 -0.00976 -0.04374 316 LEU   A O    
1146 C  CB   . LEU   A 164 ? 0.29679 0.33539 0.26866 -0.06973 -0.01732 -0.03638 316 LEU   A CB   
1147 C  CG   . LEU   A 164 ? 0.33714 0.36939 0.31326 -0.06400 -0.01356 -0.03473 316 LEU   A CG   
1148 C  CD1  . LEU   A 164 ? 0.31849 0.36702 0.30926 -0.06120 -0.01614 -0.03379 316 LEU   A CD1  
1149 C  CD2  . LEU   A 164 ? 0.31595 0.33772 0.28867 -0.05592 -0.01310 -0.03183 316 LEU   A CD2  
1150 N  N    . LYS   A 165 ? 0.30728 0.33166 0.26759 -0.09149 -0.00971 -0.05047 317 LYS   A N    
1151 C  CA   . LYS   A 165 ? 0.33148 0.34100 0.29040 -0.09896 -0.00406 -0.05436 317 LYS   A CA   
1152 C  C    . LYS   A 165 ? 0.40237 0.42519 0.36857 -0.11006 -0.00546 -0.05729 317 LYS   A C    
1153 O  O    . LYS   A 165 ? 0.42090 0.43848 0.39169 -0.11530 -0.00120 -0.05560 317 LYS   A O    
1154 C  CB   . LYS   A 165 ? 0.45600 0.44865 0.40608 -0.10147 -0.00111 -0.06213 317 LYS   A CB   
1155 C  CG   . LYS   A 165 ? 0.49684 0.46514 0.44750 -0.10326 0.00551  -0.06269 317 LYS   A CG   
1156 C  CD   . LYS   A 165 ? 0.48785 0.44422 0.43726 -0.09182 0.00812  -0.05461 317 LYS   A CD   
1157 C  CE   . LYS   A 165 ? 0.51538 0.45085 0.46798 -0.09347 0.01341  -0.05049 317 LYS   A CE   
1158 N  NZ   . LYS   A 165 ? 0.39296 0.31807 0.34428 -0.08248 0.01504  -0.04260 317 LYS   A NZ   
1159 N  N    . LYS   A 166 ? 0.34903 0.39120 0.31694 -0.11433 -0.01172 -0.06052 318 LYS   A N    
1160 C  CA   . LYS   A 166 ? 0.30827 0.36685 0.28471 -0.12533 -0.01414 -0.06360 318 LYS   A CA   
1161 C  C    . LYS   A 166 ? 0.36761 0.44112 0.35771 -0.12258 -0.01382 -0.05697 318 LYS   A C    
1162 O  O    . LYS   A 166 ? 0.36301 0.44812 0.36205 -0.13200 -0.01338 -0.05867 318 LYS   A O    
1163 C  CB   . LYS   A 166 ? 0.38556 0.46536 0.36069 -0.12963 -0.02235 -0.06704 318 LYS   A CB   
1164 C  CG   . LYS   A 166 ? 0.47193 0.54377 0.43424 -0.13772 -0.02207 -0.07817 318 LYS   A CG   
1165 C  CD   . LYS   A 166 ? 0.46821 0.56632 0.42708 -0.14179 -0.03101 -0.07966 318 LYS   A CD   
1166 C  CE   . LYS   A 166 ? 0.54110 0.63591 0.48656 -0.15204 -0.03039 -0.09407 318 LYS   A CE   
1167 N  NZ   . LYS   A 166 ? 0.49389 0.61951 0.43476 -0.15832 -0.03995 -0.09516 318 LYS   A NZ   
1168 N  N    . LEU   A 167 ? 0.33656 0.41159 0.32962 -0.11039 -0.01375 -0.05067 319 LEU   A N    
1169 C  CA   . LEU   A 167 ? 0.31675 0.40615 0.32284 -0.10722 -0.01195 -0.04715 319 LEU   A CA   
1170 C  C    . LEU   A 167 ? 0.40478 0.48410 0.40889 -0.11213 -0.00368 -0.04595 319 LEU   A C    
1171 O  O    . LEU   A 167 ? 0.39016 0.48545 0.40463 -0.11431 -0.00087 -0.04470 319 LEU   A O    
1172 C  CB   . LEU   A 167 ? 0.31381 0.40594 0.32425 -0.09335 -0.01380 -0.04314 319 LEU   A CB   
1173 C  CG   . LEU   A 167 ? 0.35898 0.46475 0.37708 -0.08770 -0.02244 -0.04060 319 LEU   A CG   
1174 C  CD1  . LEU   A 167 ? 0.35285 0.45846 0.37920 -0.07477 -0.02343 -0.03718 319 LEU   A CD1  
1175 C  CD2  . LEU   A 167 ? 0.33393 0.46494 0.36660 -0.09318 -0.02744 -0.04096 319 LEU   A CD2  
1176 N  N    A ASN   A 168 ? 0.36795 0.42282 0.36029 -0.11398 0.00030  -0.04560 320 ASN   A N    
1177 N  N    B ASN   A 168 ? 0.36940 0.42420 0.36171 -0.11381 0.00036  -0.04551 320 ASN   A N    
1178 C  CA   A ASN   A 168 ? 0.38507 0.42771 0.37492 -0.11819 0.00744  -0.04106 320 ASN   A CA   
1179 C  CA   B ASN   A 168 ? 0.38531 0.42861 0.37553 -0.11853 0.00748  -0.04108 320 ASN   A CA   
1180 C  C    A ASN   A 168 ? 0.37194 0.42773 0.36547 -0.11188 0.01065  -0.03601 320 ASN   A C    
1181 C  C    B ASN   A 168 ? 0.37291 0.42857 0.36638 -0.11191 0.01075  -0.03592 320 ASN   A C    
1182 O  O    A ASN   A 168 ? 0.38869 0.45701 0.38816 -0.11827 0.01501  -0.03354 320 ASN   A O    
1183 O  O    B ASN   A 168 ? 0.39202 0.45977 0.39110 -0.11819 0.01525  -0.03325 320 ASN   A O    
1184 C  CB   A ASN   A 168 ? 0.41743 0.46084 0.41279 -0.13330 0.00978  -0.04287 320 ASN   A CB   
1185 C  CB   B ASN   A 168 ? 0.41411 0.46065 0.41073 -0.13362 0.00950  -0.04306 320 ASN   A CB   
1186 C  CG   A ASN   A 168 ? 0.44963 0.47130 0.44109 -0.13865 0.01624  -0.03676 320 ASN   A CG   
1187 C  CG   B ASN   A 168 ? 0.45838 0.49245 0.45146 -0.14130 0.00669  -0.05113 320 ASN   A CG   
1188 O  OD1  A ASN   A 168 ? 0.48044 0.48427 0.46381 -0.13090 0.01801  -0.03219 320 ASN   A OD1  
1189 O  OD1  B ASN   A 168 ? 0.50852 0.55870 0.50637 -0.14716 0.00157  -0.05740 320 ASN   A OD1  
1190 N  ND2  A ASN   A 168 ? 0.46398 0.48768 0.46288 -0.15222 0.01937  -0.03546 320 ASN   A ND2  
1191 N  ND2  B ASN   A 168 ? 0.47630 0.48305 0.46179 -0.14116 0.00990  -0.05165 320 ASN   A ND2  
1192 N  N    . LEU   A 169 ? 0.33743 0.39164 0.32761 -0.09976 0.00869  -0.03539 321 LEU   A N    
1193 C  CA   . LEU   A 169 ? 0.32422 0.39141 0.31754 -0.09299 0.01127  -0.03390 321 LEU   A CA   
1194 C  C    . LEU   A 169 ? 0.34746 0.40836 0.33267 -0.09669 0.01783  -0.02729 321 LEU   A C    
1195 O  O    . LEU   A 169 ? 0.38765 0.42736 0.36389 -0.09865 0.01898  -0.02224 321 LEU   A O    
1196 C  CB   . LEU   A 169 ? 0.31370 0.37686 0.30537 -0.08051 0.00734  -0.03524 321 LEU   A CB   
1197 C  CG   . LEU   A 169 ? 0.31740 0.38759 0.31788 -0.07556 0.00031  -0.03850 321 LEU   A CG   
1198 C  CD1  . LEU   A 169 ? 0.29388 0.36028 0.29526 -0.06423 -0.00247 -0.03860 321 LEU   A CD1  
1199 C  CD2  . LEU   A 169 ? 0.25129 0.34535 0.26805 -0.07751 -0.00104 -0.04144 321 LEU   A CD2  
1200 N  N    . HIS   A 170 ? 0.31448 0.39570 0.30413 -0.09724 0.02203  -0.02722 322 HIS   A N    
1201 C  CA   . HIS   A 170 ? 0.29623 0.37586 0.27588 -0.09918 0.02759  -0.01952 322 HIS   A CA   
1202 C  C    . HIS   A 170 ? 0.35373 0.42315 0.32456 -0.08807 0.02475  -0.01932 322 HIS   A C    
1203 O  O    . HIS   A 170 ? 0.37880 0.45109 0.35465 -0.07955 0.02048  -0.02645 322 HIS   A O    
1204 C  CB   . HIS   A 170 ? 0.28256 0.39105 0.26772 -0.10102 0.03308  -0.02181 322 HIS   A CB   
1205 C  CG   . HIS   A 170 ? 0.29969 0.42270 0.29535 -0.11229 0.03648  -0.02152 322 HIS   A CG   
1206 N  ND1  . HIS   A 170 ? 0.30854 0.45979 0.31065 -0.11614 0.04294  -0.02298 322 HIS   A ND1  
1207 C  CD2  . HIS   A 170 ? 0.32095 0.43587 0.32235 -0.12128 0.03453  -0.02070 322 HIS   A CD2  
1208 C  CE1  . HIS   A 170 ? 0.31368 0.47356 0.32614 -0.12690 0.04456  -0.02193 322 HIS   A CE1  
1209 N  NE2  . HIS   A 170 ? 0.31945 0.45715 0.33146 -0.13055 0.03916  -0.02076 322 HIS   A NE2  
1210 N  N    . GLU   A 171 ? 0.32018 0.38117 0.27966 -0.08873 0.02712  -0.01025 323 GLU   A N    
1211 C  CA   . GLU   A 171 ? 0.32828 0.38319 0.27991 -0.07896 0.02413  -0.00965 323 GLU   A CA   
1212 C  C    . GLU   A 171 ? 0.32953 0.40613 0.28548 -0.07233 0.02389  -0.01990 323 GLU   A C    
1213 O  O    . GLU   A 171 ? 0.34003 0.41167 0.29745 -0.06358 0.01927  -0.02522 323 GLU   A O    
1214 C  CB   . GLU   A 171 ? 0.39556 0.44495 0.33568 -0.08162 0.02649  0.00333  323 GLU   A CB   
1215 C  CG   . GLU   A 171 ? 0.52291 0.56221 0.45624 -0.07256 0.02216  0.00580  323 GLU   A CG   
1216 C  CD   . GLU   A 171 ? 0.60566 0.63681 0.52996 -0.07453 0.02283  0.02131  323 GLU   A CD   
1217 O  OE1  . GLU   A 171 ? 0.70599 0.74534 0.62682 -0.08298 0.02721  0.03077  323 GLU   A OE1  
1218 O  OE2  . GLU   A 171 ? 0.69251 0.71035 0.61456 -0.06768 0.01884  0.02507  323 GLU   A OE2  
1219 N  N    . GLU   A 172 ? 0.32848 0.42829 0.28797 -0.07682 0.02917  -0.02296 324 GLU   A N    
1220 C  CA   . GLU   A 172 ? 0.33591 0.45827 0.30230 -0.07071 0.03048  -0.03537 324 GLU   A CA   
1221 C  C    . GLU   A 172 ? 0.32175 0.44019 0.30384 -0.06305 0.02491  -0.04486 324 GLU   A C    
1222 O  O    . GLU   A 172 ? 0.29321 0.41485 0.28012 -0.05455 0.02241  -0.05344 324 GLU   A O    
1223 C  CB   . GLU   A 172 ? 0.30510 0.45434 0.27561 -0.07759 0.03820  -0.03768 324 GLU   A CB   
1224 C  CG   . GLU   A 172 ? 0.33254 0.49145 0.28692 -0.08497 0.04393  -0.02759 324 GLU   A CG   
1225 C  CD   . GLU   A 172 ? 0.37913 0.52481 0.32842 -0.09602 0.04570  -0.01151 324 GLU   A CD   
1226 O  OE1  . GLU   A 172 ? 0.41138 0.57025 0.35209 -0.10443 0.05153  -0.00170 324 GLU   A OE1  
1227 O  OE2  . GLU   A 172 ? 0.33859 0.46127 0.29296 -0.09667 0.04137  -0.00897 324 GLU   A OE2  
1228 N  N    . GLU   A 173 ? 0.25239 0.36485 0.24262 -0.06659 0.02264  -0.04292 325 GLU   A N    
1229 C  CA   . GLU   A 173 ? 0.24344 0.35447 0.24813 -0.05995 0.01653  -0.04880 325 GLU   A CA   
1230 C  C    . GLU   A 173 ? 0.25820 0.34767 0.25696 -0.05434 0.01050  -0.04597 325 GLU   A C    
1231 O  O    . GLU   A 173 ? 0.24608 0.33495 0.25484 -0.04666 0.00575  -0.05035 325 GLU   A O    
1232 C  CB   . GLU   A 173 ? 0.24026 0.35601 0.25421 -0.06649 0.01524  -0.04727 325 GLU   A CB   
1233 C  CG   . GLU   A 173 ? 0.24233 0.38395 0.26787 -0.07092 0.02073  -0.05128 325 GLU   A CG   
1234 C  CD   . GLU   A 173 ? 0.30528 0.44991 0.33299 -0.08265 0.02167  -0.04663 325 GLU   A CD   
1235 O  OE1  . GLU   A 173 ? 0.32589 0.49346 0.36525 -0.08720 0.02588  -0.04929 325 GLU   A OE1  
1236 O  OE2  . GLU   A 173 ? 0.27931 0.40435 0.29817 -0.08762 0.01853  -0.04145 325 GLU   A OE2  
1237 N  N    . HIS   A 174 ? 0.28556 0.35754 0.27004 -0.05803 0.01088  -0.03823 326 HIS   A N    
1238 C  CA   . HIS   A 174 ? 0.31645 0.37030 0.29575 -0.05285 0.00633  -0.03572 326 HIS   A CA   
1239 C  C    . HIS   A 174 ? 0.27840 0.33440 0.25769 -0.04497 0.00471  -0.03923 326 HIS   A C    
1240 O  O    . HIS   A 174 ? 0.25961 0.31023 0.24507 -0.03900 -0.00008 -0.04134 326 HIS   A O    
1241 C  CB   . HIS   A 174 ? 0.31217 0.34840 0.27903 -0.05750 0.00820  -0.02779 326 HIS   A CB   
1242 C  CG   . HIS   A 174 ? 0.32741 0.34688 0.29054 -0.05266 0.00464  -0.02597 326 HIS   A CG   
1243 N  ND1  . HIS   A 174 ? 0.36271 0.37333 0.31871 -0.04838 0.00454  -0.02157 326 HIS   A ND1  
1244 C  CD2  . HIS   A 174 ? 0.27381 0.28661 0.23949 -0.05178 0.00131  -0.02767 326 HIS   A CD2  
1245 C  CE1  . HIS   A 174 ? 0.29341 0.29229 0.24920 -0.04469 0.00192  -0.02130 326 HIS   A CE1  
1246 N  NE2  . HIS   A 174 ? 0.38593 0.38613 0.34647 -0.04695 0.00025  -0.02504 326 HIS   A NE2  
1247 N  N    . VAL   A 175 ? 0.27881 0.34407 0.25118 -0.04579 0.00850  -0.03972 327 VAL   A N    
1248 C  CA   . VAL   A 175 ? 0.26437 0.33307 0.23557 -0.03961 0.00656  -0.04457 327 VAL   A CA   
1249 C  C    . VAL   A 175 ? 0.26678 0.34838 0.25401 -0.03443 0.00555  -0.05698 327 VAL   A C    
1250 O  O    . VAL   A 175 ? 0.28072 0.35934 0.27386 -0.02855 0.00170  -0.06250 327 VAL   A O    
1251 C  CB   . VAL   A 175 ? 0.28782 0.36542 0.24481 -0.04284 0.01029  -0.04087 327 VAL   A CB   
1252 C  CG1  . VAL   A 175 ? 0.31610 0.37805 0.26147 -0.04665 0.01050  -0.02696 327 VAL   A CG1  
1253 C  CG2  . VAL   A 175 ? 0.25820 0.35744 0.21590 -0.04779 0.01662  -0.04504 327 VAL   A CG2  
1254 N  N    . LEU   A 176 ? 0.24093 0.33695 0.23796 -0.03642 0.00892  -0.06176 328 LEU   A N    
1255 C  CA   . LEU   A 176 ? 0.23064 0.33779 0.24754 -0.03012 0.00790  -0.07362 328 LEU   A CA   
1256 C  C    . LEU   A 176 ? 0.30346 0.39746 0.33404 -0.02508 0.00062  -0.07121 328 LEU   A C    
1257 O  O    . LEU   A 176 ? 0.25634 0.34920 0.30132 -0.01832 -0.00275 -0.07811 328 LEU   A O    
1258 C  CB   . LEU   A 176 ? 0.23231 0.35967 0.25903 -0.03302 0.01326  -0.07821 328 LEU   A CB   
1259 C  CG   . LEU   A 176 ? 0.24133 0.39057 0.26248 -0.03534 0.02120  -0.08638 328 LEU   A CG   
1260 C  CD1  . LEU   A 176 ? 0.24376 0.41235 0.27110 -0.04111 0.02740  -0.08638 328 LEU   A CD1  
1261 C  CD2  . LEU   A 176 ? 0.27277 0.43103 0.30679 -0.02714 0.02126  -0.10273 328 LEU   A CD2  
1262 N  N    . LEU   A 177 ? 0.26154 0.34583 0.28786 -0.02894 -0.00189 -0.06134 329 LEU   A N    
1263 C  CA   . LEU   A 177 ? 0.21388 0.28908 0.25036 -0.02552 -0.00875 -0.05700 329 LEU   A CA   
1264 C  C    . LEU   A 177 ? 0.21252 0.27350 0.24515 -0.02162 -0.01237 -0.05497 329 LEU   A C    
1265 O  O    . LEU   A 177 ? 0.27152 0.32899 0.31852 -0.01667 -0.01749 -0.05484 329 LEU   A O    
1266 C  CB   . LEU   A 177 ? 0.23219 0.30310 0.26141 -0.03194 -0.00998 -0.04875 329 LEU   A CB   
1267 C  CG   . LEU   A 177 ? 0.28642 0.35406 0.32426 -0.03016 -0.01700 -0.04314 329 LEU   A CG   
1268 C  CD1  . LEU   A 177 ? 0.26045 0.34152 0.32219 -0.02494 -0.02056 -0.04586 329 LEU   A CD1  
1269 C  CD2  . LEU   A 177 ? 0.26368 0.32937 0.29094 -0.03795 -0.01751 -0.03789 329 LEU   A CD2  
1270 N  N    . MET   A 178 ? 0.23658 0.28992 0.25180 -0.02396 -0.01005 -0.05219 330 MET   A N    
1271 C  CA   . MET   A 178 ? 0.25520 0.29815 0.26801 -0.02053 -0.01328 -0.05064 330 MET   A CA   
1272 C  C    . MET   A 178 ? 0.25856 0.30733 0.28352 -0.01561 -0.01471 -0.06072 330 MET   A C    
1273 O  O    . MET   A 178 ? 0.26734 0.30922 0.30286 -0.01208 -0.01937 -0.06082 330 MET   A O    
1274 C  CB   . MET   A 178 ? 0.23756 0.27392 0.23184 -0.02328 -0.01071 -0.04542 330 MET   A CB   
1275 C  CG   . MET   A 178 ? 0.29033 0.31547 0.27553 -0.02686 -0.00999 -0.03692 330 MET   A CG   
1276 S  SD   . MET   A 178 ? 0.32840 0.34290 0.29854 -0.02722 -0.00807 -0.03009 330 MET   A SD   
1277 C  CE   . MET   A 178 ? 0.28900 0.31380 0.25068 -0.03134 -0.00340 -0.02992 330 MET   A CE   
1278 N  N    . ALA   A 179 ? 0.23804 0.30038 0.26236 -0.01597 -0.01039 -0.06994 331 ALA   A N    
1279 C  CA   . ALA   A 179 ? 0.23499 0.30439 0.27117 -0.01169 -0.01095 -0.08330 331 ALA   A CA   
1280 C  C    . ALA   A 179 ? 0.29329 0.36163 0.35576 -0.00627 -0.01429 -0.08824 331 ALA   A C    
1281 O  O    . ALA   A 179 ? 0.31664 0.37903 0.39345 -0.00227 -0.01817 -0.09407 331 ALA   A O    
1282 C  CB   . ALA   A 179 ? 0.23495 0.32306 0.26331 -0.01392 -0.00445 -0.09295 331 ALA   A CB   
1283 N  N    . ILE   A 180 ? 0.23064 0.30490 0.30161 -0.00630 -0.01333 -0.08532 332 ILE   A N    
1284 C  CA   . ILE   A 180 ? 0.24948 0.32364 0.34764 -0.00049 -0.01751 -0.08696 332 ILE   A CA   
1285 C  C    . ILE   A 180 ? 0.26144 0.31959 0.36527 0.00066  -0.02491 -0.07536 332 ILE   A C    
1286 O  O    . ILE   A 180 ? 0.23781 0.29034 0.36406 0.00582  -0.02948 -0.07723 332 ILE   A O    
1287 C  CB   . ILE   A 180 ? 0.23081 0.31746 0.33579 -0.00156 -0.01583 -0.08399 332 ILE   A CB   
1288 C  CG1  . ILE   A 180 ? 0.24120 0.34704 0.34596 -0.00220 -0.00779 -0.09669 332 ILE   A CG1  
1289 C  CG2  . ILE   A 180 ? 0.24407 0.33035 0.37737 0.00461  -0.02207 -0.08068 332 ILE   A CG2  
1290 C  CD1  . ILE   A 180 ? 0.22639 0.34593 0.33094 -0.00656 -0.00484 -0.09211 332 ILE   A CD1  
1291 N  N    . CYS   A 181 ? 0.22307 0.27408 0.30790 -0.00437 -0.02580 -0.06324 333 CYS   A N    
1292 C  CA   . CYS   A 181 ? 0.28555 0.32486 0.37300 -0.00431 -0.03160 -0.05197 333 CYS   A CA   
1293 C  C    . CYS   A 181 ? 0.35905 0.38973 0.45439 -0.00168 -0.03399 -0.05617 333 CYS   A C    
1294 O  O    . CYS   A 181 ? 0.28754 0.31131 0.40013 0.00058  -0.03938 -0.05066 333 CYS   A O    
1295 C  CB   . CYS   A 181 ? 0.25239 0.28707 0.31644 -0.01003 -0.03014 -0.04253 333 CYS   A CB   
1296 S  SG   . CYS   A 181 ? 0.28530 0.30996 0.34809 -0.01107 -0.03507 -0.02965 333 CYS   A SG   
1297 N  N    . ILE   A 182 ? 0.29544 0.32766 0.37938 -0.00259 -0.03049 -0.06534 334 ILE   A N    
1298 C  CA   . ILE   A 182 ? 0.26717 0.29293 0.35661 -0.00165 -0.03320 -0.06990 334 ILE   A CA   
1299 C  C    . ILE   A 182 ? 0.31458 0.33998 0.43116 0.00305  -0.03553 -0.08170 334 ILE   A C    
1300 O  O    . ILE   A 182 ? 0.29937 0.31478 0.43286 0.00415  -0.04051 -0.07964 334 ILE   A O    
1301 C  CB   . ILE   A 182 ? 0.32768 0.35871 0.39685 -0.00430 -0.02974 -0.07586 334 ILE   A CB   
1302 C  CG1  . ILE   A 182 ? 0.29562 0.32225 0.34376 -0.00774 -0.02854 -0.06294 334 ILE   A CG1  
1303 C  CG2  . ILE   A 182 ? 0.34902 0.37826 0.42657 -0.00369 -0.03287 -0.08499 334 ILE   A CG2  
1304 C  CD1  . ILE   A 182 ? 0.29002 0.32322 0.31811 -0.01010 -0.02487 -0.06478 334 ILE   A CD1  
1305 N  N    A VAL   A 183 ? 0.30914 0.34558 0.43183 0.00567  -0.03152 -0.09455 335 VAL   A N    
1306 N  N    B VAL   A 183 ? 0.30373 0.34007 0.42698 0.00576  -0.03160 -0.09450 335 VAL   A N    
1307 C  CA   A VAL   A 183 ? 0.27936 0.31674 0.42884 0.01097  -0.03216 -0.11013 335 VAL   A CA   
1308 C  CA   B VAL   A 183 ? 0.28761 0.32434 0.43756 0.01097  -0.03241 -0.11020 335 VAL   A CA   
1309 C  C    A VAL   A 183 ? 0.29779 0.33260 0.47320 0.01617  -0.03536 -0.10371 335 VAL   A C    
1310 C  C    B VAL   A 183 ? 0.29586 0.32961 0.47371 0.01653  -0.03569 -0.10503 335 VAL   A C    
1311 O  O    A VAL   A 183 ? 0.30650 0.35258 0.49380 0.02022  -0.03198 -0.11246 335 VAL   A O    
1312 O  O    B VAL   A 183 ? 0.30972 0.35305 0.50391 0.02145  -0.03268 -0.11661 335 VAL   A O    
1313 C  CB   A VAL   A 183 ? 0.30032 0.35484 0.44300 0.01131  -0.02507 -0.12925 335 VAL   A CB   
1314 C  CB   B VAL   A 183 ? 0.30149 0.35503 0.44480 0.01130  -0.02546 -0.12975 335 VAL   A CB   
1315 C  CG1  A VAL   A 183 ? 0.25158 0.30661 0.42081 0.01642  -0.02510 -0.14986 335 VAL   A CG1  
1316 C  CG1  B VAL   A 183 ? 0.30202 0.35938 0.42211 0.00621  -0.02429 -0.13466 335 VAL   A CG1  
1317 C  CG2  A VAL   A 183 ? 0.30169 0.36237 0.41395 0.00528  -0.02245 -0.12959 335 VAL   A CG2  
1318 C  CG2  B VAL   A 183 ? 0.27574 0.34349 0.40781 0.01022  -0.01980 -0.12644 335 VAL   A CG2  
1319 N  N    . SER   A 184 ? 0.29554 0.31801 0.48030 0.01596  -0.04193 -0.08736 336 SER   A N    
1320 C  CA   . SER   A 184 ? 0.30827 0.32927 0.51979 0.02105  -0.04660 -0.07885 336 SER   A CA   
1321 C  C    . SER   A 184 ? 0.33271 0.33961 0.57692 0.02540  -0.05207 -0.08112 336 SER   A C    
1322 O  O    . SER   A 184 ? 0.36420 0.35922 0.60673 0.02160  -0.05551 -0.07487 336 SER   A O    
1323 C  CB   . SER   A 184 ? 0.40551 0.42646 0.60486 0.01711  -0.05048 -0.05656 336 SER   A CB   
1324 O  OG   . SER   A 184 ? 0.45767 0.48712 0.62578 0.01165  -0.04538 -0.05555 336 SER   A OG   
1325 N  N    . PRO   A 185 ? 0.27456 0.28234 0.55104 0.03327  -0.05279 -0.09029 337 PRO   A N    
1326 C  CA   . PRO   A 185 ? 0.30979 0.30162 0.62096 0.03759  -0.05734 -0.09595 337 PRO   A CA   
1327 C  C    . PRO   A 185 ? 0.42827 0.40618 0.75729 0.03703  -0.06639 -0.07162 337 PRO   A C    
1328 O  O    . PRO   A 185 ? 0.44258 0.40423 0.79689 0.03786  -0.07052 -0.07311 337 PRO   A O    
1329 C  CB   . PRO   A 185 ? 0.34408 0.34281 0.68562 0.04732  -0.05455 -0.11286 337 PRO   A CB   
1330 C  CG   . PRO   A 185 ? 0.31989 0.33720 0.64902 0.04824  -0.05199 -0.10523 337 PRO   A CG   
1331 C  CD   . PRO   A 185 ? 0.26680 0.29093 0.55101 0.03859  -0.04843 -0.09896 337 PRO   A CD   
1332 N  N    . ASP   A 186 ? 0.37255 0.35726 0.68983 0.03486  -0.06967 -0.04946 338 ASP   A N    
1333 C  CA   . ASP   A 186 ? 0.41231 0.38847 0.74520 0.03380  -0.07835 -0.02423 338 ASP   A CA   
1334 C  C    . ASP   A 186 ? 0.40461 0.37548 0.71365 0.02438  -0.07945 -0.01074 338 ASP   A C    
1335 O  O    . ASP   A 186 ? 0.47693 0.44609 0.79013 0.02138  -0.08551 0.01263  338 ASP   A O    
1336 C  CB   . ASP   A 186 ? 0.30955 0.29982 0.64356 0.03600  -0.08216 -0.00726 338 ASP   A CB   
1337 C  CG   . ASP   A 186 ? 0.39118 0.39685 0.68455 0.02940  -0.07766 -0.00485 338 ASP   A CG   
1338 O  OD1  . ASP   A 186 ? 0.48635 0.50142 0.77079 0.02622  -0.08209 0.01416  338 ASP   A OD1  
1339 O  OD2  . ASP   A 186 ? 0.38182 0.39062 0.65262 0.02699  -0.06991 -0.02192 338 ASP   A OD2  
1340 N  N    . ARG   A 187 ? 0.36472 0.33516 0.64985 0.01974  -0.07379 -0.02422 339 ARG   A N    
1341 C  CA   . ARG   A 187 ? 0.32899 0.29582 0.59488 0.01174  -0.07428 -0.01306 339 ARG   A CA   
1342 C  C    . ARG   A 187 ? 0.40724 0.35845 0.70136 0.01013  -0.07998 -0.00587 339 ARG   A C    
1343 O  O    . ARG   A 187 ? 0.32427 0.26482 0.64683 0.01427  -0.08131 -0.01980 339 ARG   A O    
1344 C  CB   . ARG   A 187 ? 0.31329 0.28417 0.55135 0.00825  -0.06773 -0.02909 339 ARG   A CB   
1345 C  CG   . ARG   A 187 ? 0.36141 0.34591 0.57308 0.00887  -0.06175 -0.03599 339 ARG   A CG   
1346 C  CD   . ARG   A 187 ? 0.29434 0.28567 0.48350 0.00464  -0.06173 -0.01833 339 ARG   A CD   
1347 N  NE   . ARG   A 187 ? 0.29406 0.29492 0.45496 0.00284  -0.05552 -0.02506 339 ARG   A NE   
1348 C  CZ   . ARG   A 187 ? 0.27809 0.28472 0.41723 -0.00122 -0.05408 -0.01488 339 ARG   A CZ   
1349 N  NH1  . ARG   A 187 ? 0.33376 0.34070 0.47344 -0.00404 -0.05809 0.00189  339 ARG   A NH1  
1350 N  NH2  . ARG   A 187 ? 0.28084 0.29344 0.39785 -0.00305 -0.04847 -0.02162 339 ARG   A NH2  
1351 N  N    . PRO   A 188 ? 0.50293 0.45304 0.79092 0.00365  -0.08297 0.01492  340 PRO   A N    
1352 C  CA   . PRO   A 188 ? 0.48567 0.42140 0.80112 0.00042  -0.08819 0.02373  340 PRO   A CA   
1353 C  C    . PRO   A 188 ? 0.42550 0.35354 0.74304 -0.00232 -0.08567 0.00339  340 PRO   A C    
1354 O  O    . PRO   A 188 ? 0.45757 0.39389 0.74657 -0.00606 -0.08088 -0.00448 340 PRO   A O    
1355 C  CB   . PRO   A 188 ? 0.59329 0.53634 0.89252 -0.00726 -0.08965 0.04935  340 PRO   A CB   
1356 C  CG   . PRO   A 188 ? 0.61847 0.57686 0.87738 -0.00887 -0.08319 0.04474  340 PRO   A CG   
1357 C  CD   . PRO   A 188 ? 0.57063 0.53356 0.82701 -0.00168 -0.08111 0.03035  340 PRO   A CD   
1358 N  N    . GLY   A 189 ? 0.47016 0.38265 0.82334 -0.00039 -0.08936 -0.00547 341 GLY   A N    
1359 C  CA   . GLY   A 189 ? 0.48720 0.39255 0.84700 -0.00415 -0.08844 -0.02527 341 GLY   A CA   
1360 C  C    . GLY   A 189 ? 0.43493 0.34221 0.79621 0.00140  -0.08445 -0.05655 341 GLY   A C    
1361 O  O    . GLY   A 189 ? 0.42428 0.32764 0.79145 -0.00206 -0.08420 -0.07556 341 GLY   A O    
1362 N  N    . VAL   A 190 ? 0.36971 0.28539 0.72573 0.00914  -0.08123 -0.06277 342 VAL   A N    
1363 C  CA   . VAL   A 190 ? 0.34253 0.26435 0.69783 0.01394  -0.07611 -0.09245 342 VAL   A CA   
1364 C  C    . VAL   A 190 ? 0.36711 0.27294 0.76476 0.01751  -0.07886 -0.10980 342 VAL   A C    
1365 O  O    . VAL   A 190 ? 0.45892 0.35093 0.89129 0.02209  -0.08378 -0.09853 342 VAL   A O    
1366 C  CB   . VAL   A 190 ? 0.40342 0.33914 0.74725 0.02088  -0.07185 -0.09312 342 VAL   A CB   
1367 C  CG1  . VAL   A 190 ? 0.40602 0.34951 0.75497 0.02618  -0.06605 -0.12350 342 VAL   A CG1  
1368 C  CG2  . VAL   A 190 ? 0.36613 0.31647 0.66765 0.01639  -0.06834 -0.08118 342 VAL   A CG2  
1369 N  N    . GLN   A 191 ? 0.41399 0.32200 0.80985 0.01518  -0.07603 -0.13736 343 GLN   A N    
1370 C  CA   . GLN   A 191 ? 0.46110 0.36177 0.89005 0.01799  -0.07630 -0.15637 343 GLN   A CA   
1371 C  C    . GLN   A 191 ? 0.49605 0.40779 0.93328 0.02768  -0.07041 -0.17539 343 GLN   A C    
1372 O  O    . GLN   A 191 ? 0.48727 0.39311 0.95584 0.03458  -0.07192 -0.17082 343 GLN   A O    
1373 C  CB   . GLN   A 191 ? 0.53592 0.44244 0.95341 0.01024  -0.07514 -0.17446 343 GLN   A CB   
1374 C  CG   . GLN   A 191 ? 0.63393 0.52758 1.06440 0.00220  -0.08113 -0.16000 343 GLN   A CG   
1375 C  CD   . GLN   A 191 ? 0.66125 0.56448 1.06679 -0.00706 -0.08093 -0.16954 343 GLN   A CD   
1376 O  OE1  . GLN   A 191 ? 0.58085 0.47976 0.98109 -0.01482 -0.08499 -0.15252 343 GLN   A OE1  
1377 N  NE2  . GLN   A 191 ? 0.59759 0.51677 0.98758 -0.00660 -0.07620 -0.19586 343 GLN   A NE2  
1378 N  N    . ASP   A 192 ? 0.46081 0.39092 0.86999 0.02761  -0.06363 -0.19569 344 ASP   A N    
1379 C  CA   . ASP   A 192 ? 0.42446 0.37037 0.83802 0.03517  -0.05641 -0.21619 344 ASP   A CA   
1380 C  C    . ASP   A 192 ? 0.44406 0.39607 0.84852 0.04148  -0.05423 -0.20590 344 ASP   A C    
1381 O  O    . ASP   A 192 ? 0.40167 0.37408 0.77383 0.04015  -0.04784 -0.21218 344 ASP   A O    
1382 C  CB   . ASP   A 192 ? 0.43781 0.40431 0.82530 0.03067  -0.04989 -0.24193 344 ASP   A CB   
1383 C  CG   . ASP   A 192 ? 0.52089 0.50417 0.91959 0.03672  -0.04241 -0.26532 344 ASP   A CG   
1384 O  OD1  . ASP   A 192 ? 0.49543 0.49517 0.88056 0.03285  -0.03776 -0.28661 344 ASP   A OD1  
1385 O  OD2  . ASP   A 192 ? 0.48077 0.46259 0.90190 0.04505  -0.04129 -0.26187 344 ASP   A OD2  
1386 N  N    . ALA   A 193 ? 0.41161 0.35106 0.84209 0.04718  -0.05959 -0.18458 345 ALA   A N    
1387 C  CA   . ALA   A 193 ? 0.45624 0.40858 0.87396 0.05100  -0.05840 -0.16639 345 ALA   A CA   
1388 C  C    . ALA   A 193 ? 0.40910 0.38155 0.82765 0.05809  -0.04991 -0.18782 345 ALA   A C    
1389 O  O    . ALA   A 193 ? 0.36990 0.36094 0.76160 0.05705  -0.04574 -0.18067 345 ALA   A O    
1390 C  CB   . ALA   A 193 ? 0.42960 0.36789 0.87890 0.05598  -0.06671 -0.14045 345 ALA   A CB   
1391 N  N    . LYS   A 194 ? 0.47693 0.45004 0.92217 0.06291  -0.04667 -0.21161 346 LYS   A N    
1392 C  CA   . LYS   A 194 ? 0.48529 0.48147 0.93073 0.06838  -0.03769 -0.23124 346 LYS   A CA   
1393 C  C    . LYS   A 194 ? 0.41060 0.42798 0.81553 0.06264  -0.02915 -0.24849 346 LYS   A C    
1394 O  O    . LYS   A 194 ? 0.36358 0.40218 0.75586 0.06550  -0.02193 -0.25385 346 LYS   A O    
1395 C  CB   . LYS   A 194 ? 0.60104 0.59664 1.07822 0.07157  -0.03610 -0.24910 346 LYS   A CB   
1396 C  CG   . LYS   A 194 ? 0.68942 0.68327 1.20267 0.08131  -0.03801 -0.24097 346 LYS   A CG   
1397 C  CD   . LYS   A 194 ? 0.77792 0.79695 1.28096 0.08661  -0.03038 -0.24657 346 LYS   A CD   
1398 C  CE   . LYS   A 194 ? 0.82598 0.84443 1.36280 0.09615  -0.03377 -0.23330 346 LYS   A CE   
1399 N  NZ   . LYS   A 194 ? 0.83663 0.87154 1.36101 0.09936  -0.03308 -0.21773 346 LYS   A NZ   
1400 N  N    . LEU   A 195 ? 0.34136 0.35572 0.72585 0.05385  -0.03002 -0.25581 347 LEU   A N    
1401 C  CA   . LEU   A 195 ? 0.38401 0.41969 0.72751 0.04716  -0.02332 -0.26780 347 LEU   A CA   
1402 C  C    . LEU   A 195 ? 0.37960 0.42093 0.68852 0.04230  -0.02396 -0.24165 347 LEU   A C    
1403 O  O    . LEU   A 195 ? 0.36529 0.42878 0.64740 0.03995  -0.01692 -0.24385 347 LEU   A O    
1404 C  CB   . LEU   A 195 ? 0.40798 0.44206 0.73782 0.03835  -0.02567 -0.27641 347 LEU   A CB   
1405 C  CG   . LEU   A 195 ? 0.39083 0.44768 0.67696 0.03040  -0.02071 -0.28408 347 LEU   A CG   
1406 C  CD1  . LEU   A 195 ? 0.36662 0.45254 0.64425 0.03241  -0.01041 -0.30111 347 LEU   A CD1  
1407 C  CD2  . LEU   A 195 ? 0.36302 0.41936 0.63964 0.02253  -0.02434 -0.29065 347 LEU   A CD2  
1408 N  N    . VAL   A 196 ? 0.36664 0.38964 0.67500 0.03968  -0.03202 -0.21526 348 VAL   A N    
1409 C  CA   . VAL   A 196 ? 0.28676 0.31470 0.56476 0.03512  -0.03261 -0.18995 348 VAL   A CA   
1410 C  C    . VAL   A 196 ? 0.28066 0.32213 0.56302 0.04029  -0.02866 -0.18509 348 VAL   A C    
1411 O  O    . VAL   A 196 ? 0.28358 0.33969 0.53710 0.03608  -0.02429 -0.17801 348 VAL   A O    
1412 C  CB   . VAL   A 196 ? 0.28054 0.28839 0.56216 0.03223  -0.04139 -0.16448 348 VAL   A CB   
1413 C  CG1  . VAL   A 196 ? 0.32718 0.34080 0.57887 0.02783  -0.04130 -0.14163 348 VAL   A CG1  
1414 C  CG2  . VAL   A 196 ? 0.28618 0.28336 0.56409 0.02620  -0.04498 -0.16899 348 VAL   A CG2  
1415 N  N    . GLU   A 197 ? 0.28797 0.32505 0.60876 0.04941  -0.03037 -0.18862 349 GLU   A N    
1416 C  CA   . GLU   A 197 ? 0.32625 0.37894 0.65562 0.05480  -0.02715 -0.18478 349 GLU   A CA   
1417 C  C    . GLU   A 197 ? 0.29792 0.37648 0.61233 0.05424  -0.01601 -0.20604 349 GLU   A C    
1418 O  O    . GLU   A 197 ? 0.30692 0.40263 0.60382 0.05166  -0.01184 -0.19827 349 GLU   A O    
1419 C  CB   . GLU   A 197 ? 0.38716 0.43095 0.76530 0.06600  -0.03158 -0.18544 349 GLU   A CB   
1420 C  CG   . GLU   A 197 ? 0.51620 0.57870 0.90809 0.07243  -0.02904 -0.18171 349 GLU   A CG   
1421 C  CD   . GLU   A 197 ? 0.64734 0.69891 1.08027 0.08139  -0.03805 -0.16566 349 GLU   A CD   
1422 O  OE1  . GLU   A 197 ? 0.69380 0.72515 1.15877 0.08671  -0.04293 -0.16942 349 GLU   A OE1  
1423 O  OE2  . GLU   A 197 ? 0.66621 0.72992 1.10037 0.08267  -0.04076 -0.14860 349 GLU   A OE2  
1424 N  N    . ALA   A 198 ? 0.33240 0.41544 0.65349 0.05570  -0.01097 -0.23331 350 ALA   A N    
1425 C  CA   . ALA   A 198 ? 0.37195 0.48316 0.67868 0.05465  0.00030  -0.25446 350 ALA   A CA   
1426 C  C    . ALA   A 198 ? 0.38754 0.51160 0.64659 0.04352  0.00357  -0.24380 350 ALA   A C    
1427 O  O    . ALA   A 198 ? 0.37314 0.52046 0.61719 0.04121  0.01134  -0.24508 350 ALA   A O    
1428 C  CB   . ALA   A 198 ? 0.42445 0.53851 0.74529 0.05717  0.00447  -0.28693 350 ALA   A CB   
1429 N  N    . ILE   A 199 ? 0.34523 0.45471 0.58216 0.03655  -0.00227 -0.23232 351 ILE   A N    
1430 C  CA   . ILE   A 199 ? 0.32607 0.44485 0.52123 0.02704  -0.00015 -0.21997 351 ILE   A CA   
1431 C  C    . ILE   A 199 ? 0.30995 0.42899 0.49576 0.02528  -0.00075 -0.19649 351 ILE   A C    
1432 O  O    . ILE   A 199 ? 0.27468 0.41071 0.43753 0.02004  0.00532  -0.19264 351 ILE   A O    
1433 C  CB   . ILE   A 199 ? 0.33727 0.44030 0.51627 0.02141  -0.00685 -0.21276 351 ILE   A CB   
1434 C  CG1  . ILE   A 199 ? 0.39893 0.50463 0.58592 0.02143  -0.00653 -0.23800 351 ILE   A CG1  
1435 C  CG2  . ILE   A 199 ? 0.32915 0.43991 0.46892 0.01302  -0.00535 -0.19802 351 ILE   A CG2  
1436 C  CD1  . ILE   A 199 ? 0.36663 0.45615 0.54661 0.01654  -0.01442 -0.23171 351 ILE   A CD1  
1437 N  N    . GLN   A 200 ? 0.33550 0.43667 0.53891 0.02871  -0.00825 -0.18021 352 GLN   A N    
1438 C  CA   . GLN   A 200 ? 0.26077 0.36306 0.45509 0.02614  -0.00971 -0.15928 352 GLN   A CA   
1439 C  C    . GLN   A 200 ? 0.24852 0.37211 0.45429 0.02907  -0.00353 -0.16514 352 GLN   A C    
1440 O  O    . GLN   A 200 ? 0.27513 0.40939 0.46247 0.02328  -0.00043 -0.15511 352 GLN   A O    
1441 C  CB   . GLN   A 200 ? 0.36430 0.44718 0.57569 0.02896  -0.01930 -0.14158 352 GLN   A CB   
1442 C  CG   . GLN   A 200 ? 0.36274 0.44576 0.55767 0.02394  -0.02182 -0.12005 352 GLN   A CG   
1443 C  CD   . GLN   A 200 ? 0.35277 0.42375 0.56704 0.02707  -0.03090 -0.10332 352 GLN   A CD   
1444 O  OE1  . GLN   A 200 ? 0.33264 0.40510 0.57898 0.03467  -0.03391 -0.10511 352 GLN   A OE1  
1445 N  NE2  . GLN   A 200 ? 0.26670 0.32702 0.46244 0.02140  -0.03524 -0.08654 352 GLN   A NE2  
1446 N  N    . ASP   A 201 ? 0.25958 0.38953 0.49824 0.03801  -0.00163 -0.18156 353 ASP   A N    
1447 C  CA   . ASP   A 201 ? 0.29700 0.44995 0.55109 0.04185  0.00462  -0.18821 353 ASP   A CA   
1448 C  C    . ASP   A 201 ? 0.33197 0.50925 0.55864 0.03452  0.01541  -0.19716 353 ASP   A C    
1449 O  O    . ASP   A 201 ? 0.34091 0.53636 0.56451 0.03165  0.01994  -0.19175 353 ASP   A O    
1450 C  CB   . ASP   A 201 ? 0.28642 0.44168 0.58272 0.05388  0.00572  -0.20751 353 ASP   A CB   
1451 C  CG   . ASP   A 201 ? 0.39164 0.52849 0.72132 0.06174  -0.00489 -0.19325 353 ASP   A CG   
1452 O  OD1  . ASP   A 201 ? 0.38913 0.51526 0.70660 0.05712  -0.01253 -0.16894 353 ASP   A OD1  
1453 O  OD2  . ASP   A 201 ? 0.47326 0.60707 0.84189 0.07244  -0.00554 -0.20620 353 ASP   A OD2  
1454 N  N    A ARG   A 202 ? 0.35767 0.53719 0.56456 0.03061  0.01925  -0.20984 354 ARG   A N    
1455 N  N    B ARG   A 202 ? 0.35684 0.53641 0.56365 0.03059  0.01927  -0.20984 354 ARG   A N    
1456 C  CA   A ARG   A 202 ? 0.38595 0.58897 0.56327 0.02229  0.02860  -0.21441 354 ARG   A CA   
1457 C  CA   B ARG   A 202 ? 0.38686 0.59006 0.56425 0.02229  0.02866  -0.21436 354 ARG   A CA   
1458 C  C    A ARG   A 202 ? 0.35173 0.55080 0.50052 0.01271  0.02696  -0.19007 354 ARG   A C    
1459 C  C    B ARG   A 202 ? 0.35326 0.55236 0.50204 0.01270  0.02697  -0.19000 354 ARG   A C    
1460 O  O    A ARG   A 202 ? 0.32451 0.54346 0.46123 0.00680  0.03403  -0.18671 354 ARG   A O    
1461 O  O    B ARG   A 202 ? 0.32164 0.54053 0.45838 0.00678  0.03400  -0.18654 354 ARG   A O    
1462 C  CB   A ARG   A 202 ? 0.43290 0.63846 0.59295 0.01934  0.03056  -0.22962 354 ARG   A CB   
1463 C  CB   B ARG   A 202 ? 0.43349 0.63977 0.59360 0.01934  0.03081  -0.22986 354 ARG   A CB   
1464 C  CG   A ARG   A 202 ? 0.46116 0.69561 0.59273 0.01123  0.04042  -0.23600 354 ARG   A CG   
1465 C  CG   B ARG   A 202 ? 0.46023 0.69656 0.59344 0.01162  0.04112  -0.23748 354 ARG   A CG   
1466 C  CD   A ARG   A 202 ? 0.50580 0.75384 0.63460 0.01183  0.04444  -0.26204 354 ARG   A CD   
1467 C  CD   B ARG   A 202 ? 0.50274 0.75348 0.63562 0.01287  0.04561  -0.26487 354 ARG   A CD   
1468 N  NE   A ARG   A 202 ? 0.53590 0.79073 0.70084 0.02197  0.04844  -0.28746 354 ARG   A NE   
1469 N  NE   B ARG   A 202 ? 0.55816 0.78710 0.68647 0.01250  0.03683  -0.26599 354 ARG   A NE   
1470 C  CZ   A ARG   A 202 ? 0.52693 0.81081 0.70103 0.02373  0.05896  -0.30284 354 ARG   A CZ   
1471 C  CZ   B ARG   A 202 ? 0.61754 0.85135 0.71514 0.00460  0.03540  -0.26366 354 ARG   A CZ   
1472 N  NH1  A ARG   A 202 ? 0.51242 0.79562 0.72060 0.03192  0.05909  -0.31882 354 ARG   A NH1  
1473 N  NH1  B ARG   A 202 ? 0.66346 0.92207 0.73146 -0.00356 0.04201  -0.25858 354 ARG   A NH1  
1474 N  NH2  A ARG   A 202 ? 0.48982 0.80012 0.63860 0.01529  0.06711  -0.29568 354 ARG   A NH2  
1475 N  NH2  B ARG   A 202 ? 0.55945 0.77453 0.65714 0.00449  0.02701  -0.26502 354 ARG   A NH2  
1476 N  N    . LEU   A 203 ? 0.29405 0.46784 0.43328 0.01077  0.01813  -0.17343 355 LEU   A N    
1477 C  CA   . LEU   A 203 ? 0.26693 0.43433 0.38203 0.00246  0.01652  -0.15231 355 LEU   A CA   
1478 C  C    . LEU   A 203 ? 0.23852 0.40905 0.36742 0.00270  0.01512  -0.14181 355 LEU   A C    
1479 O  O    . LEU   A 203 ? 0.28650 0.46590 0.40076 -0.00497 0.01879  -0.13271 355 LEU   A O    
1480 C  CB   . LEU   A 203 ? 0.25017 0.39206 0.35319 0.00107  0.00834  -0.13994 355 LEU   A CB   
1481 C  CG   . LEU   A 203 ? 0.27641 0.41450 0.36697 0.00034  0.00762  -0.14827 355 LEU   A CG   
1482 C  CD1  . LEU   A 203 ? 0.24145 0.35523 0.33008 0.00077  -0.00096 -0.13670 355 LEU   A CD1  
1483 C  CD2  . LEU   A 203 ? 0.32787 0.48004 0.38859 -0.00754 0.01339  -0.14607 355 LEU   A CD2  
1484 N  N    . SER   A 204 ? 0.25781 0.42162 0.41588 0.01088  0.00923  -0.14213 356 SER   A N    
1485 C  CA   . SER   A 204 ? 0.26948 0.43930 0.44229 0.01132  0.00636  -0.13175 356 SER   A CA   
1486 C  C    . SER   A 204 ? 0.31417 0.51253 0.49351 0.00966  0.01527  -0.14008 356 SER   A C    
1487 O  O    . SER   A 204 ? 0.28943 0.49666 0.46131 0.00255  0.01628  -0.12974 356 SER   A O    
1488 C  CB   . SER   A 204 ? 0.33322 0.49381 0.53933 0.02146  -0.00180 -0.13043 356 SER   A CB   
1489 O  OG   . SER   A 204 ? 0.41702 0.55311 0.61687 0.02136  -0.00990 -0.11982 356 SER   A OG   
1490 N  N    . ASN   A 205 ? 0.26407 0.47843 0.45792 0.01552  0.02232  -0.15990 357 ASN   A N    
1491 C  CA   . ASN   A 205 ? 0.30677 0.55214 0.50751 0.01393  0.03234  -0.16928 357 ASN   A CA   
1492 C  C    . ASN   A 205 ? 0.29336 0.54928 0.45981 0.00084  0.03948  -0.16295 357 ASN   A C    
1493 O  O    . ASN   A 205 ? 0.28052 0.55661 0.44733 -0.00517 0.04489  -0.15902 357 ASN   A O    
1494 C  CB   . ASN   A 205 ? 0.34864 0.60929 0.57054 0.02303  0.03936  -0.19446 357 ASN   A CB   
1495 C  CG   . ASN   A 205 ? 0.44572 0.70044 0.71019 0.03665  0.03363  -0.20041 357 ASN   A CG   
1496 O  OD1  . ASN   A 205 ? 0.48714 0.73894 0.77077 0.04542  0.03512  -0.21906 357 ASN   A OD1  
1497 N  ND2  . ASN   A 205 ? 0.44284 0.69593 0.72342 0.03826  0.02655  -0.18440 357 ASN   A ND2  
1498 N  N    . THR   A 206 ? 0.28700 0.53014 0.42546 -0.00395 0.03922  -0.16081 358 THR   A N    
1499 C  CA   . THR   A 206 ? 0.30086 0.55007 0.40773 -0.01617 0.04430  -0.15053 358 THR   A CA   
1500 C  C    . THR   A 206 ? 0.37168 0.60901 0.47133 -0.02356 0.03977  -0.13044 358 THR   A C    
1501 O  O    . THR   A 206 ? 0.31354 0.56421 0.40310 -0.03315 0.04543  -0.12338 358 THR   A O    
1502 C  CB   . THR   A 206 ? 0.29063 0.52656 0.37219 -0.01843 0.04251  -0.14981 358 THR   A CB   
1503 O  OG1  . THR   A 206 ? 0.29545 0.54579 0.38241 -0.01320 0.04707  -0.17092 358 THR   A OG1  
1504 C  CG2  . THR   A 206 ? 0.30646 0.54697 0.35761 -0.03035 0.04667  -0.13611 358 THR   A CG2  
1505 N  N    . LEU   A 207 ? 0.23610 0.44925 0.34107 -0.02003 0.02976  -0.12147 359 LEU   A N    
1506 C  CA   . LEU   A 207 ? 0.23047 0.43297 0.32847 -0.02712 0.02520  -0.10517 359 LEU   A CA   
1507 C  C    . LEU   A 207 ? 0.25476 0.47740 0.37302 -0.02865 0.02654  -0.10503 359 LEU   A C    
1508 O  O    . LEU   A 207 ? 0.25690 0.48584 0.36627 -0.03900 0.02917  -0.09689 359 LEU   A O    
1509 C  CB   . LEU   A 207 ? 0.25381 0.43044 0.35294 -0.02284 0.01479  -0.09711 359 LEU   A CB   
1510 C  CG   . LEU   A 207 ? 0.29756 0.46514 0.39212 -0.02915 0.00932  -0.08330 359 LEU   A CG   
1511 C  CD1  . LEU   A 207 ? 0.26533 0.42902 0.33554 -0.04080 0.01394  -0.07562 359 LEU   A CD1  
1512 C  CD2  . LEU   A 207 ? 0.25883 0.40459 0.35290 -0.02495 0.00019  -0.07618 359 LEU   A CD2  
1513 N  N    . GLN   A 208 ? 0.22550 0.45844 0.37343 -0.01848 0.02435  -0.11372 360 GLN   A N    
1514 C  CA   . GLN   A 208 ? 0.22318 0.47811 0.39436 -0.01861 0.02465  -0.11336 360 GLN   A CA   
1515 C  C    . GLN   A 208 ? 0.24009 0.52236 0.40714 -0.02662 0.03623  -0.11844 360 GLN   A C    
1516 O  O    . GLN   A 208 ? 0.27273 0.56771 0.44226 -0.03520 0.03704  -0.11118 360 GLN   A O    
1517 C  CB   . GLN   A 208 ? 0.29710 0.55935 0.50405 -0.00440 0.02119  -0.12280 360 GLN   A CB   
1518 C  CG   . GLN   A 208 ? 0.31612 0.55368 0.53094 0.00270  0.00925  -0.11470 360 GLN   A CG   
1519 C  CD   . GLN   A 208 ? 0.49047 0.73305 0.74376 0.01704  0.00577  -0.12277 360 GLN   A CD   
1520 O  OE1  . GLN   A 208 ? 0.58658 0.81187 0.84701 0.02479  0.00273  -0.12776 360 GLN   A OE1  
1521 N  NE2  . GLN   A 208 ? 0.48516 0.75144 0.76585 0.02062  0.00599  -0.12392 360 GLN   A NE2  
1522 N  N    . THR   A 209 ? 0.27971 0.57311 0.44013 -0.02497 0.04533  -0.13092 361 THR   A N    
1523 C  CA   . THR   A 209 ? 0.27491 0.59766 0.43014 -0.03325 0.05730  -0.13499 361 THR   A CA   
1524 C  C    . THR   A 209 ? 0.26439 0.57894 0.38896 -0.04846 0.05930  -0.11939 361 THR   A C    
1525 O  O    . THR   A 209 ? 0.28263 0.61703 0.40668 -0.05879 0.06581  -0.11467 361 THR   A O    
1526 C  CB   . THR   A 209 ? 0.31777 0.65749 0.47262 -0.02767 0.06653  -0.15358 361 THR   A CB   
1527 O  OG1  . THR   A 209 ? 0.31869 0.66372 0.50651 -0.01298 0.06485  -0.16941 361 THR   A OG1  
1528 C  CG2  . THR   A 209 ? 0.32047 0.69548 0.46999 -0.03673 0.07988  -0.15740 361 THR   A CG2  
1529 N  N    . TYR   A 210 ? 0.24886 0.53458 0.34993 -0.05010 0.05396  -0.11096 362 TYR   A N    
1530 C  CA   . TYR   A 210 ? 0.26046 0.53488 0.33643 -0.06325 0.05505  -0.09541 362 TYR   A CA   
1531 C  C    . TYR   A 210 ? 0.25066 0.52188 0.33434 -0.07121 0.05123  -0.08523 362 TYR   A C    
1532 O  O    . TYR   A 210 ? 0.31954 0.59934 0.39634 -0.08377 0.05647  -0.07724 362 TYR   A O    
1533 C  CB   . TYR   A 210 ? 0.28427 0.52765 0.33881 -0.06165 0.04888  -0.08841 362 TYR   A CB   
1534 C  CG   . TYR   A 210 ? 0.26154 0.49080 0.29449 -0.07378 0.04960  -0.07220 362 TYR   A CG   
1535 C  CD1  . TYR   A 210 ? 0.26114 0.47026 0.29404 -0.07858 0.04352  -0.06245 362 TYR   A CD1  
1536 C  CD2  . TYR   A 210 ? 0.27440 0.51170 0.28832 -0.08072 0.05641  -0.06674 362 TYR   A CD2  
1537 C  CE1  . TYR   A 210 ? 0.28292 0.47731 0.29989 -0.08923 0.04458  -0.04936 362 TYR   A CE1  
1538 C  CE2  . TYR   A 210 ? 0.30372 0.52652 0.30179 -0.09128 0.05678  -0.05047 362 TYR   A CE2  
1539 C  CZ   . TYR   A 210 ? 0.35218 0.55211 0.35313 -0.09518 0.05107  -0.04262 362 TYR   A CZ   
1540 O  OH   . TYR   A 210 ? 0.36288 0.54608 0.35130 -0.10519 0.05173  -0.02801 362 TYR   A OH   
1541 N  N    . ILE   A 211 ? 0.24068 0.50023 0.33862 -0.06492 0.04173  -0.08492 363 ILE   A N    
1542 C  CA   . ILE   A 211 ? 0.23828 0.49655 0.34265 -0.07281 0.03679  -0.07672 363 ILE   A CA   
1543 C  C    . ILE   A 211 ? 0.24046 0.53205 0.36392 -0.07828 0.04292  -0.08013 363 ILE   A C    
1544 O  O    . ILE   A 211 ? 0.27560 0.57213 0.39600 -0.09152 0.04475  -0.07286 363 ILE   A O    
1545 C  CB   . ILE   A 211 ? 0.22889 0.47415 0.34511 -0.06450 0.02518  -0.07563 363 ILE   A CB   
1546 C  CG1  . ILE   A 211 ? 0.22769 0.44110 0.32395 -0.06152 0.01987  -0.07073 363 ILE   A CG1  
1547 C  CG2  . ILE   A 211 ? 0.28452 0.53573 0.40886 -0.07295 0.01974  -0.06930 363 ILE   A CG2  
1548 C  CD1  . ILE   A 211 ? 0.28131 0.48423 0.38889 -0.05222 0.00959  -0.06956 363 ILE   A CD1  
1549 N  N    . ARG   A 212 ? 0.27906 0.59447 0.42432 -0.06829 0.04663  -0.09208 364 ARG   A N    
1550 C  CA   . ARG   A 212 ? 0.30281 0.65371 0.47027 -0.07180 0.05294  -0.09660 364 ARG   A CA   
1551 C  C    . ARG   A 212 ? 0.27977 0.64618 0.43235 -0.08588 0.06460  -0.09298 364 ARG   A C    
1552 O  O    . ARG   A 212 ? 0.30461 0.69080 0.46704 -0.09670 0.06777  -0.08876 364 ARG   A O    
1553 C  CB   . ARG   A 212 ? 0.23700 0.60905 0.43121 -0.05667 0.05607  -0.11220 364 ARG   A CB   
1554 C  CG   . ARG   A 212 ? 0.30327 0.71624 0.52283 -0.05834 0.06458  -0.11937 364 ARG   A CG   
1555 C  CD   . ARG   A 212 ? 0.27971 0.70347 0.52020 -0.06262 0.05690  -0.11151 364 ARG   A CD   
1556 N  NE   . ARG   A 212 ? 0.37915 0.84469 0.64589 -0.06446 0.06532  -0.11812 364 ARG   A NE   
1557 C  CZ   . ARG   A 212 ? 0.39341 0.87914 0.65323 -0.08006 0.07436  -0.11391 364 ARG   A CZ   
1558 N  NH1  . ARG   A 212 ? 0.46299 0.92851 0.69136 -0.09473 0.07564  -0.10257 364 ARG   A NH1  
1559 N  NH2  . ARG   A 212 ? 0.44304 0.96960 0.72954 -0.08100 0.08228  -0.12048 364 ARG   A NH2  
1560 N  N    . CYS   A 213 ? 0.28670 0.64571 0.41590 -0.08684 0.07065  -0.09327 365 CYS   A N    
1561 C  CA   . CYS   A 213 ? 0.32954 0.70830 0.44563 -0.09916 0.08241  -0.08914 365 CYS   A CA   
1562 C  C    . CYS   A 213 ? 0.31416 0.66888 0.40422 -0.11294 0.08135  -0.07166 365 CYS   A C    
1563 O  O    . CYS   A 213 ? 0.35556 0.72558 0.43919 -0.12644 0.08959  -0.06337 365 CYS   A O    
1564 C  CB   . CYS   A 213 ? 0.38715 0.78136 0.49463 -0.09230 0.09087  -0.10089 365 CYS   A CB   
1565 S  SG   . CYS   A 213 ? 0.42242 0.84666 0.56281 -0.07586 0.09503  -0.12495 365 CYS   A SG   
1566 N  N    A ARG   A 214 ? 0.29325 0.61147 0.37006 -0.10991 0.07186  -0.06554 366 ARG   A N    
1567 N  N    B ARG   A 214 ? 0.29549 0.61368 0.37233 -0.10994 0.07184  -0.06552 366 ARG   A N    
1568 C  CA   A ARG   A 214 ? 0.32183 0.61495 0.37594 -0.12059 0.07105  -0.05023 366 ARG   A CA   
1569 C  CA   B ARG   A 214 ? 0.32166 0.61492 0.37579 -0.12063 0.07109  -0.05022 366 ARG   A CA   
1570 C  C    A ARG   A 214 ? 0.34741 0.61356 0.40281 -0.12574 0.06222  -0.04317 366 ARG   A C    
1571 C  C    B ARG   A 214 ? 0.34397 0.60954 0.39901 -0.12553 0.06212  -0.04316 366 ARG   A C    
1572 O  O    A ARG   A 214 ? 0.37365 0.62157 0.41631 -0.13668 0.06279  -0.03116 366 ARG   A O    
1573 O  O    B ARG   A 214 ? 0.36323 0.60961 0.40496 -0.13601 0.06248  -0.03119 366 ARG   A O    
1574 C  CB   A ARG   A 214 ? 0.31426 0.58866 0.34696 -0.11333 0.06949  -0.04891 366 ARG   A CB   
1575 C  CB   B ARG   A 214 ? 0.32111 0.59662 0.35364 -0.11359 0.06991  -0.04887 366 ARG   A CB   
1576 C  CG   A ARG   A 214 ? 0.36095 0.66195 0.38716 -0.11025 0.07817  -0.05616 366 ARG   A CG   
1577 C  CG   B ARG   A 214 ? 0.36126 0.66434 0.38844 -0.11005 0.07858  -0.05698 366 ARG   A CG   
1578 C  CD   A ARG   A 214 ? 0.45819 0.77352 0.46967 -0.12461 0.08707  -0.04292 366 ARG   A CD   
1579 C  CD   B ARG   A 214 ? 0.45408 0.77338 0.46686 -0.12420 0.08790  -0.04448 366 ARG   A CD   
1580 N  NE   A ARG   A 214 ? 0.50861 0.85750 0.51431 -0.12304 0.09649  -0.05151 366 ARG   A NE   
1581 N  NE   B ARG   A 214 ? 0.51755 0.85736 0.51566 -0.12138 0.09435  -0.04956 366 ARG   A NE   
1582 C  CZ   A ARG   A 214 ? 0.54931 0.89739 0.53537 -0.11886 0.09669  -0.05249 366 ARG   A CZ   
1583 C  CZ   B ARG   A 214 ? 0.55745 0.93534 0.56316 -0.12003 0.10383  -0.06288 366 ARG   A CZ   
1584 N  NH1  A ARG   A 214 ? 0.54974 0.86483 0.52197 -0.11527 0.08795  -0.04424 366 ARG   A NH1  
1585 N  NH1  B ARG   A 214 ? 0.47946 0.87887 0.50955 -0.12044 0.10790  -0.07128 366 ARG   A NH1  
1586 N  NH2  A ARG   A 214 ? 0.60176 0.98429 0.58240 -0.11847 0.10573  -0.06260 366 ARG   A NH2  
1587 N  NH2  B ARG   A 214 ? 0.59433 0.99088 0.58384 -0.11825 0.10926  -0.06863 366 ARG   A NH2  
1588 N  N    . HIS   A 215 ? 0.28858 0.55205 0.35920 -0.11861 0.05410  -0.04999 367 HIS   A N    
1589 C  CA   . HIS   A 215 ? 0.27086 0.51205 0.34048 -0.12414 0.04582  -0.04502 367 HIS   A CA   
1590 C  C    . HIS   A 215 ? 0.29637 0.55857 0.38456 -0.13463 0.04577  -0.04549 367 HIS   A C    
1591 O  O    . HIS   A 215 ? 0.32767 0.61295 0.43673 -0.12828 0.04325  -0.05282 367 HIS   A O    
1592 C  CB   . HIS   A 215 ? 0.27133 0.49651 0.34278 -0.11149 0.03585  -0.04968 367 HIS   A CB   
1593 C  CG   . HIS   A 215 ? 0.32357 0.51997 0.38355 -0.11618 0.02896  -0.04448 367 HIS   A CG   
1594 N  ND1  . HIS   A 215 ? 0.28713 0.45706 0.33226 -0.10891 0.02506  -0.04283 367 HIS   A ND1  
1595 C  CD2  . HIS   A 215 ? 0.31725 0.50867 0.37902 -0.12784 0.02587  -0.04210 367 HIS   A CD2  
1596 C  CE1  . HIS   A 215 ? 0.26467 0.41514 0.30296 -0.11510 0.02053  -0.04009 367 HIS   A CE1  
1597 N  NE2  . HIS   A 215 ? 0.28812 0.45049 0.33582 -0.12680 0.02075  -0.04029 367 HIS   A NE2  
1598 N  N    . PRO   A 216 ? 0.34908 0.60437 0.43285 -0.15053 0.04793  -0.03781 368 PRO   A N    
1599 C  CA   . PRO   A 216 ? 0.35699 0.63495 0.45951 -0.16246 0.04819  -0.03856 368 PRO   A CA   
1600 C  C    . PRO   A 216 ? 0.29258 0.56609 0.40425 -0.16147 0.03671  -0.04311 368 PRO   A C    
1601 O  O    . PRO   A 216 ? 0.31611 0.56139 0.41456 -0.15805 0.02983  -0.04283 368 PRO   A O    
1602 C  CB   . PRO   A 216 ? 0.45847 0.72318 0.55156 -0.18025 0.05356  -0.02815 368 PRO   A CB   
1603 C  CG   . PRO   A 216 ? 0.43444 0.66006 0.50580 -0.17638 0.05061  -0.02324 368 PRO   A CG   
1604 C  CD   . PRO   A 216 ? 0.35636 0.58204 0.42008 -0.15843 0.04996  -0.02777 368 PRO   A CD   
1605 N  N    . PRO   A 217 ? 0.28513 0.58866 0.41948 -0.16457 0.03430  -0.04710 369 PRO   A N    
1606 C  CA   . PRO   A 217 ? 0.27414 0.57767 0.41621 -0.16762 0.02290  -0.04963 369 PRO   A CA   
1607 C  C    . PRO   A 217 ? 0.33465 0.61789 0.46625 -0.18532 0.02170  -0.04692 369 PRO   A C    
1608 O  O    . PRO   A 217 ? 0.30377 0.58232 0.43153 -0.19749 0.03007  -0.04183 369 PRO   A O    
1609 C  CB   . PRO   A 217 ? 0.26849 0.61416 0.43976 -0.16838 0.02230  -0.05305 369 PRO   A CB   
1610 C  CG   . PRO   A 217 ? 0.28059 0.64466 0.45660 -0.17462 0.03560  -0.05136 369 PRO   A CG   
1611 C  CD   . PRO   A 217 ? 0.27520 0.61735 0.42978 -0.16606 0.04218  -0.04943 369 PRO   A CD   
1612 N  N    . PRO   A 218 ? 0.30867 0.58001 0.43614 -0.18787 0.01157  -0.05030 370 PRO   A N    
1613 C  CA   . PRO   A 218 ? 0.30256 0.58152 0.43447 -0.17626 0.00063  -0.05361 370 PRO   A CA   
1614 C  C    . PRO   A 218 ? 0.30392 0.55746 0.41892 -0.16085 -0.00144 -0.05263 370 PRO   A C    
1615 O  O    . PRO   A 218 ? 0.34637 0.60732 0.46675 -0.14986 -0.00954 -0.05305 370 PRO   A O    
1616 C  CB   . PRO   A 218 ? 0.37805 0.65487 0.50806 -0.19004 -0.00776 -0.05744 370 PRO   A CB   
1617 C  CG   . PRO   A 218 ? 0.39660 0.64403 0.51190 -0.20316 -0.00130 -0.05738 370 PRO   A CG   
1618 C  CD   . PRO   A 218 ? 0.34047 0.59263 0.46037 -0.20520 0.01044  -0.05124 370 PRO   A CD   
1619 N  N    . GLY   A 219 ? 0.30082 0.52612 0.39734 -0.16038 0.00533  -0.05007 371 GLY   A N    
1620 C  CA   . GLY   A 219 ? 0.32854 0.53035 0.40966 -0.14715 0.00345  -0.04919 371 GLY   A CA   
1621 C  C    . GLY   A 219 ? 0.29924 0.51411 0.38970 -0.13052 0.00236  -0.04961 371 GLY   A C    
1622 O  O    . GLY   A 219 ? 0.31095 0.51318 0.39507 -0.11990 -0.00294 -0.04927 371 GLY   A O    
1623 N  N    . SER   A 220 ? 0.33578 0.57625 0.44277 -0.12833 0.00766  -0.05102 372 SER   A N    
1624 C  CA   . SER   A 220 ? 0.30788 0.56049 0.42705 -0.11245 0.00783  -0.05402 372 SER   A CA   
1625 C  C    . SER   A 220 ? 0.31438 0.58303 0.45335 -0.10445 -0.00245 -0.05463 372 SER   A C    
1626 O  O    . SER   A 220 ? 0.29392 0.56680 0.44464 -0.09012 -0.00397 -0.05667 372 SER   A O    
1627 C  CB   . SER   A 220 ? 0.25294 0.53022 0.38416 -0.11298 0.01814  -0.05735 372 SER   A CB   
1628 O  OG   . SER   A 220 ? 0.27480 0.57927 0.42398 -0.12307 0.01866  -0.05768 372 SER   A OG   
1629 N  N    . HIS   A 221 ? 0.32241 0.60047 0.46628 -0.11358 -0.00990 -0.05267 373 HIS   A N    
1630 C  CA   . HIS   A 221 ? 0.31864 0.61859 0.48390 -0.10732 -0.02034 -0.05087 373 HIS   A CA   
1631 C  C    . HIS   A 221 ? 0.28821 0.57295 0.45012 -0.09371 -0.02772 -0.04711 373 HIS   A C    
1632 O  O    . HIS   A 221 ? 0.29554 0.55856 0.43653 -0.09653 -0.03175 -0.04433 373 HIS   A O    
1633 C  CB   . HIS   A 221 ? 0.31725 0.62836 0.48248 -0.12150 -0.02807 -0.04938 373 HIS   A CB   
1634 C  CG   . HIS   A 221 ? 0.31936 0.65392 0.50395 -0.11583 -0.04065 -0.04496 373 HIS   A CG   
1635 N  ND1  . HIS   A 221 ? 0.31074 0.67493 0.52671 -0.10682 -0.04219 -0.04418 373 HIS   A ND1  
1636 C  CD2  . HIS   A 221 ? 0.30388 0.63800 0.48151 -0.11738 -0.05244 -0.04016 373 HIS   A CD2  
1637 C  CE1  . HIS   A 221 ? 0.30454 0.68463 0.53338 -0.10287 -0.05528 -0.03741 373 HIS   A CE1  
1638 N  NE2  . HIS   A 221 ? 0.33502 0.69831 0.53956 -0.10974 -0.06177 -0.03446 373 HIS   A NE2  
1639 N  N    A GLN   A 222 ? 0.25276 0.54915 0.43697 -0.07912 -0.02909 -0.04735 374 GLN   A N    
1640 N  N    B GLN   A 222 ? 0.25277 0.54944 0.43716 -0.07917 -0.02902 -0.04741 374 GLN   A N    
1641 C  CA   A GLN   A 222 ? 0.22578 0.50908 0.41244 -0.06610 -0.03628 -0.04253 374 GLN   A CA   
1642 C  CA   B GLN   A 222 ? 0.23604 0.51968 0.42320 -0.06592 -0.03604 -0.04274 374 GLN   A CA   
1643 C  C    A GLN   A 222 ? 0.23963 0.48989 0.39923 -0.06488 -0.03225 -0.04312 374 GLN   A C    
1644 C  C    B GLN   A 222 ? 0.23984 0.49027 0.39935 -0.06510 -0.03228 -0.04310 374 GLN   A C    
1645 O  O    A GLN   A 222 ? 0.24599 0.48152 0.39870 -0.05983 -0.03883 -0.03737 374 GLN   A O    
1646 O  O    B GLN   A 222 ? 0.24628 0.48213 0.39844 -0.06048 -0.03900 -0.03723 374 GLN   A O    
1647 C  CB   A GLN   A 222 ? 0.28662 0.57910 0.47748 -0.06793 -0.04991 -0.03305 374 GLN   A CB   
1648 C  CB   B GLN   A 222 ? 0.28968 0.58371 0.48312 -0.06696 -0.04981 -0.03319 374 GLN   A CB   
1649 C  CG   A GLN   A 222 ? 0.31187 0.63874 0.53500 -0.06510 -0.05666 -0.02993 374 GLN   A CG   
1650 C  CG   B GLN   A 222 ? 0.34267 0.66705 0.57230 -0.05856 -0.05668 -0.02948 374 GLN   A CG   
1651 C  CD   A GLN   A 222 ? 0.34791 0.68257 0.60175 -0.04780 -0.05585 -0.03098 374 GLN   A CD   
1652 C  CD   B GLN   A 222 ? 0.34663 0.69094 0.58077 -0.06531 -0.06984 -0.02008 374 GLN   A CD   
1653 O  OE1  A GLN   A 222 ? 0.36892 0.68496 0.62344 -0.03686 -0.05792 -0.02807 374 GLN   A OE1  
1654 O  OE1  B GLN   A 222 ? 0.30575 0.63863 0.51649 -0.07262 -0.07557 -0.01526 374 GLN   A OE1  
1655 N  NE2  A GLN   A 222 ? 0.41646 0.77905 0.69778 -0.04540 -0.05240 -0.03606 374 GLN   A NE2  
1656 N  NE2  B GLN   A 222 ? 0.40272 0.77955 0.66745 -0.06294 -0.07468 -0.01794 374 GLN   A NE2  
1657 N  N    . LEU   A 223 ? 0.21703 0.45740 0.36202 -0.06975 -0.02156 -0.04886 375 LEU   A N    
1658 C  CA   . LEU   A 223 ? 0.21878 0.42969 0.33807 -0.07000 -0.01819 -0.04844 375 LEU   A CA   
1659 C  C    . LEU   A 223 ? 0.30898 0.50842 0.43250 -0.05609 -0.01934 -0.04917 375 LEU   A C    
1660 O  O    . LEU   A 223 ? 0.21335 0.39189 0.32219 -0.05409 -0.02249 -0.04533 375 LEU   A O    
1661 C  CB   . LEU   A 223 ? 0.22647 0.43238 0.33196 -0.07797 -0.00731 -0.05200 375 LEU   A CB   
1662 C  CG   . LEU   A 223 ? 0.26158 0.43865 0.34223 -0.07817 -0.00408 -0.05034 375 LEU   A CG   
1663 C  CD1  . LEU   A 223 ? 0.30972 0.46894 0.37665 -0.08179 -0.01069 -0.04609 375 LEU   A CD1  
1664 C  CD2  . LEU   A 223 ? 0.30766 0.48135 0.37606 -0.08747 0.00530  -0.05027 375 LEU   A CD2  
1665 N  N    . TYR   A 224 ? 0.27241 0.48554 0.41687 -0.04675 -0.01625 -0.05524 376 TYR   A N    
1666 C  CA   . TYR   A 224 ? 0.29093 0.49249 0.44252 -0.03419 -0.01766 -0.05771 376 TYR   A CA   
1667 C  C    . TYR   A 224 ? 0.29118 0.48635 0.45168 -0.02877 -0.02910 -0.04823 376 TYR   A C    
1668 O  O    . TYR   A 224 ? 0.29196 0.46731 0.44374 -0.02473 -0.03176 -0.04506 376 TYR   A O    
1669 C  CB   . TYR   A 224 ? 0.31078 0.53012 0.48728 -0.02504 -0.01239 -0.06840 376 TYR   A CB   
1670 C  CG   . TYR   A 224 ? 0.24815 0.45445 0.43483 -0.01274 -0.01401 -0.07314 376 TYR   A CG   
1671 C  CD1  . TYR   A 224 ? 0.29636 0.48496 0.46316 -0.01271 -0.00946 -0.07780 376 TYR   A CD1  
1672 C  CD2  . TYR   A 224 ? 0.30619 0.51768 0.52399 -0.00153 -0.02074 -0.07229 376 TYR   A CD2  
1673 C  CE1  . TYR   A 224 ? 0.33439 0.51130 0.51134 -0.00292 -0.01129 -0.08326 376 TYR   A CE1  
1674 C  CE2  . TYR   A 224 ? 0.33451 0.53177 0.56405 0.00877  -0.02231 -0.07704 376 TYR   A CE2  
1675 C  CZ   . TYR   A 224 ? 0.34012 0.52027 0.54871 0.00748  -0.01744 -0.08336 376 TYR   A CZ   
1676 O  OH   . TYR   A 224 ? 0.39858 0.56497 0.61982 0.01640  -0.01932 -0.08923 376 TYR   A OH   
1677 N  N    . ALA   A 225 ? 0.25638 0.47036 0.43464 -0.02926 -0.03626 -0.04241 377 ALA   A N    
1678 C  CA   . ALA   A 225 ? 0.24705 0.45899 0.43345 -0.02518 -0.04794 -0.03049 377 ALA   A CA   
1679 C  C    . ALA   A 225 ? 0.25957 0.45474 0.41626 -0.03366 -0.05090 -0.02365 377 ALA   A C    
1680 O  O    . ALA   A 225 ? 0.29044 0.47380 0.44485 -0.02948 -0.05668 -0.01558 377 ALA   A O    
1681 C  CB   . ALA   A 225 ? 0.25980 0.49928 0.46942 -0.02546 -0.05559 -0.02458 377 ALA   A CB   
1682 N  N    . LYS   A 226 ? 0.22948 0.42358 0.36470 -0.04578 -0.04654 -0.02706 378 LYS   A N    
1683 C  CA   . LYS   A 226 ? 0.22346 0.40122 0.33163 -0.05331 -0.04774 -0.02371 378 LYS   A CA   
1684 C  C    . LYS   A 226 ? 0.26590 0.41872 0.35993 -0.04856 -0.04272 -0.02553 378 LYS   A C    
1685 O  O    . LYS   A 226 ? 0.24746 0.38800 0.32813 -0.04902 -0.04581 -0.02029 378 LYS   A O    
1686 C  CB   . LYS   A 226 ? 0.22170 0.40124 0.31402 -0.06696 -0.04341 -0.02891 378 LYS   A CB   
1687 C  CG   . LYS   A 226 ? 0.26030 0.46501 0.36321 -0.07459 -0.04963 -0.02727 378 LYS   A CG   
1688 C  CD   . LYS   A 226 ? 0.30490 0.50847 0.39451 -0.08893 -0.04425 -0.03406 378 LYS   A CD   
1689 C  CE   . LYS   A 226 ? 0.37543 0.60675 0.47810 -0.09761 -0.05020 -0.03394 378 LYS   A CE   
1690 N  NZ   . LYS   A 226 ? 0.42146 0.65142 0.51588 -0.11224 -0.04415 -0.04114 378 LYS   A NZ   
1691 N  N    . MET   A 227 ? 0.22585 0.37370 0.32263 -0.04437 -0.03502 -0.03299 379 MET   A N    
1692 C  CA   . MET   A 227 ? 0.23845 0.36556 0.32278 -0.04017 -0.03112 -0.03483 379 MET   A CA   
1693 C  C    . MET   A 227 ? 0.25922 0.38106 0.35753 -0.03010 -0.03687 -0.03062 379 MET   A C    
1694 O  O    . MET   A 227 ? 0.23332 0.33909 0.32044 -0.02877 -0.03770 -0.02732 379 MET   A O    
1695 C  CB   . MET   A 227 ? 0.25330 0.38059 0.33569 -0.03944 -0.02202 -0.04369 379 MET   A CB   
1696 C  CG   . MET   A 227 ? 0.24192 0.36641 0.30609 -0.05006 -0.01557 -0.04496 379 MET   A CG   
1697 S  SD   . MET   A 227 ? 0.25101 0.38498 0.31530 -0.05073 -0.00532 -0.05247 379 MET   A SD   
1698 C  CE   . MET   A 227 ? 0.24802 0.36030 0.29399 -0.04663 -0.00305 -0.05225 379 MET   A CE   
1699 N  N    . ILE   A 228 ? 0.28427 0.41945 0.40945 -0.02288 -0.04074 -0.03046 380 ILE   A N    
1700 C  CA   . ILE   A 228 ? 0.33557 0.46435 0.47830 -0.01374 -0.04703 -0.02489 380 ILE   A CA   
1701 C  C    . ILE   A 228 ? 0.30653 0.43446 0.44378 -0.01690 -0.05577 -0.01028 380 ILE   A C    
1702 O  O    . ILE   A 228 ? 0.28365 0.40008 0.42348 -0.01314 -0.05968 -0.00309 380 ILE   A O    
1703 C  CB   . ILE   A 228 ? 0.40035 0.54306 0.57706 -0.00440 -0.04883 -0.02872 380 ILE   A CB   
1704 C  CG1  . ILE   A 228 ? 0.29418 0.44041 0.47389 -0.00179 -0.03883 -0.04511 380 ILE   A CG1  
1705 C  CG2  . ILE   A 228 ? 0.46869 0.60208 0.66750 0.00492  -0.05592 -0.02183 380 ILE   A CG2  
1706 C  CD1  . ILE   A 228 ? 0.40998 0.53804 0.57148 -0.00198 -0.03330 -0.05197 380 ILE   A CD1  
1707 N  N    . GLN   A 229 ? 0.24405 0.38575 0.37334 -0.02478 -0.05890 -0.00583 381 GLN   A N    
1708 C  CA   . GLN   A 229 ? 0.27461 0.41840 0.39275 -0.02972 -0.06618 0.00640  381 GLN   A CA   
1709 C  C    . GLN   A 229 ? 0.28176 0.40682 0.37361 -0.03378 -0.06175 0.00541  381 GLN   A C    
1710 O  O    . GLN   A 229 ? 0.27778 0.39925 0.36513 -0.03364 -0.06622 0.01536  381 GLN   A O    
1711 C  CB   . GLN   A 229 ? 0.31670 0.48032 0.42895 -0.03898 -0.06971 0.00771  381 GLN   A CB   
1712 C  CG   . GLN   A 229 ? 0.37587 0.54642 0.47389 -0.04545 -0.07710 0.01862  381 GLN   A CG   
1713 C  CD   . GLN   A 229 ? 0.47606 0.65181 0.59165 -0.03835 -0.08665 0.03500  381 GLN   A CD   
1714 O  OE1  . GLN   A 229 ? 0.46596 0.65363 0.60962 -0.03130 -0.09259 0.04099  381 GLN   A OE1  
1715 N  NE2  . GLN   A 229 ? 0.45914 0.62623 0.56018 -0.04005 -0.08792 0.04297  381 GLN   A NE2  
1716 N  N    . LYS   A 230 ? 0.24819 0.36245 0.32376 -0.03737 -0.05291 -0.00550 382 LYS   A N    
1717 C  CA   . LYS   A 230 ? 0.24974 0.34651 0.30389 -0.03968 -0.04846 -0.00678 382 LYS   A CA   
1718 C  C    . LYS   A 230 ? 0.29070 0.37489 0.35237 -0.03170 -0.04866 -0.00421 382 LYS   A C    
1719 O  O    . LYS   A 230 ? 0.25696 0.33185 0.30709 -0.03260 -0.04842 -0.00007 382 LYS   A O    
1720 C  CB   . LYS   A 230 ? 0.30352 0.39164 0.34260 -0.04447 -0.03979 -0.01692 382 LYS   A CB   
1721 C  CG   . LYS   A 230 ? 0.29716 0.39294 0.32595 -0.05469 -0.03910 -0.01989 382 LYS   A CG   
1722 C  CD   . LYS   A 230 ? 0.39173 0.48523 0.40404 -0.06030 -0.04128 -0.01726 382 LYS   A CD   
1723 C  CE   . LYS   A 230 ? 0.51332 0.62078 0.52077 -0.07062 -0.04382 -0.02021 382 LYS   A CE   
1724 N  NZ   . LYS   A 230 ? 0.54103 0.66984 0.55754 -0.07097 -0.05365 -0.01141 382 LYS   A NZ   
1725 N  N    . LEU   A 231 ? 0.20971 0.29449 0.29181 -0.02424 -0.04881 -0.00775 383 LEU   A N    
1726 C  CA   . LEU   A 231 ? 0.25840 0.33183 0.35142 -0.01745 -0.05021 -0.00611 383 LEU   A CA   
1727 C  C    . LEU   A 231 ? 0.26719 0.34300 0.37155 -0.01601 -0.05868 0.00857  383 LEU   A C    
1728 O  O    . LEU   A 231 ? 0.25889 0.32418 0.36293 -0.01477 -0.05980 0.01385  383 LEU   A O    
1729 C  CB   . LEU   A 231 ? 0.26298 0.33774 0.37701 -0.01011 -0.04825 -0.01596 383 LEU   A CB   
1730 C  CG   . LEU   A 231 ? 0.24066 0.31435 0.34342 -0.01130 -0.03955 -0.02952 383 LEU   A CG   
1731 C  CD1  . LEU   A 231 ? 0.27366 0.35328 0.39815 -0.00416 -0.03743 -0.04071 383 LEU   A CD1  
1732 C  CD2  . LEU   A 231 ? 0.23459 0.29370 0.31771 -0.01330 -0.03600 -0.03094 383 LEU   A CD2  
1733 N  N    . ALA   A 232 ? 0.21584 0.30721 0.33113 -0.01665 -0.06508 0.01660  384 ALA   A N    
1734 C  CA   . ALA   A 232 ? 0.25532 0.35216 0.37918 -0.01657 -0.07390 0.03386  384 ALA   A CA   
1735 C  C    . ALA   A 232 ? 0.26624 0.36381 0.36293 -0.02494 -0.07327 0.04010  384 ALA   A C    
1736 O  O    . ALA   A 232 ? 0.28164 0.37586 0.37866 -0.02519 -0.07637 0.05167  384 ALA   A O    
1737 C  CB   . ALA   A 232 ? 0.23834 0.35502 0.38019 -0.01537 -0.08167 0.04177  384 ALA   A CB   
1738 N  N    . ASP   A 233 ? 0.25116 0.35367 0.32551 -0.03220 -0.06888 0.03208  385 ASP   A N    
1739 C  CA   . ASP   A 233 ? 0.27555 0.37736 0.32424 -0.03951 -0.06618 0.03322  385 ASP   A CA   
1740 C  C    . ASP   A 233 ? 0.26458 0.34904 0.30748 -0.03680 -0.06092 0.03163  385 ASP   A C    
1741 O  O    . ASP   A 233 ? 0.29187 0.37777 0.32482 -0.03977 -0.06119 0.03912  385 ASP   A O    
1742 C  CB   . ASP   A 233 ? 0.26070 0.36440 0.29013 -0.04673 -0.06065 0.02071  385 ASP   A CB   
1743 C  CG   . ASP   A 233 ? 0.31223 0.43583 0.34622 -0.05149 -0.06619 0.02180  385 ASP   A CG   
1744 O  OD1  . ASP   A 233 ? 0.34150 0.46613 0.36657 -0.05719 -0.06205 0.01090  385 ASP   A OD1  
1745 O  OD2  . ASP   A 233 ? 0.30503 0.44376 0.35306 -0.04982 -0.07512 0.03445  385 ASP   A OD2  
1746 N  N    . LEU   A 234 ? 0.23337 0.30409 0.28250 -0.03161 -0.05611 0.02196  386 LEU   A N    
1747 C  CA   . LEU   A 234 ? 0.24416 0.30047 0.28786 -0.02950 -0.05156 0.01945  386 LEU   A CA   
1748 C  C    . LEU   A 234 ? 0.27734 0.33136 0.33680 -0.02636 -0.05664 0.03109  386 LEU   A C    
1749 O  O    . LEU   A 234 ? 0.24334 0.29264 0.29547 -0.02786 -0.05462 0.03483  386 LEU   A O    
1750 C  CB   . LEU   A 234 ? 0.23341 0.27955 0.27964 -0.02551 -0.04635 0.00689  386 LEU   A CB   
1751 C  CG   . LEU   A 234 ? 0.31137 0.35497 0.33900 -0.02957 -0.03969 -0.00259 386 LEU   A CG   
1752 C  CD1  . LEU   A 234 ? 0.27062 0.31041 0.30293 -0.02635 -0.03583 -0.01217 386 LEU   A CD1  
1753 C  CD2  . LEU   A 234 ? 0.34141 0.37659 0.35167 -0.03186 -0.03524 -0.00290 386 LEU   A CD2  
1754 N  N    . ARG   A 235 ? 0.28341 0.34066 0.36696 -0.02195 -0.06309 0.03712  387 ARG   A N    
1755 C  CA   . ARG   A 235 ? 0.33175 0.38566 0.43374 -0.01973 -0.06879 0.05043  387 ARG   A CA   
1756 C  C    . ARG   A 235 ? 0.34227 0.40701 0.43220 -0.02619 -0.07169 0.06630  387 ARG   A C    
1757 O  O    . ARG   A 235 ? 0.30669 0.36730 0.39879 -0.02763 -0.07197 0.07511  387 ARG   A O    
1758 C  CB   . ARG   A 235 ? 0.30247 0.35868 0.43482 -0.01351 -0.07573 0.05511  387 ARG   A CB   
1759 C  CG   . ARG   A 235 ? 0.30978 0.35846 0.45624 -0.00687 -0.07225 0.03815  387 ARG   A CG   
1760 C  CD   . ARG   A 235 ? 0.33544 0.36836 0.48431 -0.00484 -0.06820 0.02868  387 ARG   A CD   
1761 N  NE   . ARG   A 235 ? 0.42299 0.45227 0.58671 0.00128  -0.06544 0.01222  387 ARG   A NE   
1762 C  CZ   . ARG   A 235 ? 0.35704 0.37989 0.55121 0.00769  -0.06892 0.00960  387 ARG   A CZ   
1763 N  NH1  . ARG   A 235 ? 0.44742 0.46467 0.66181 0.00863  -0.07599 0.02479  387 ARG   A NH1  
1764 N  NH2  . ARG   A 235 ? 0.44423 0.46673 0.64944 0.01287  -0.06503 -0.00830 387 ARG   A NH2  
1765 N  N    . SER   A 236 ? 0.29057 0.37146 0.36752 -0.03100 -0.07372 0.06968  388 SER   A N    
1766 C  CA   . SER   A 236 ? 0.32194 0.41766 0.38439 -0.03813 -0.07612 0.08327  388 SER   A CA   
1767 C  C    . SER   A 236 ? 0.31442 0.40675 0.35226 -0.04260 -0.06734 0.07540  388 SER   A C    
1768 O  O    . SER   A 236 ? 0.30591 0.40431 0.33793 -0.04636 -0.06698 0.08600  388 SER   A O    
1769 C  CB   . SER   A 236 ? 0.41737 0.53352 0.47201 -0.04275 -0.08102 0.08636  388 SER   A CB   
1770 O  OG   . SER   A 236 ? 0.49817 0.62810 0.52618 -0.05143 -0.07847 0.08714  388 SER   A OG   
1771 N  N    . LEU   A 237 ? 0.26584 0.34947 0.29053 -0.04221 -0.06000 0.05767  389 LEU   A N    
1772 C  CA   . LEU   A 237 ? 0.27651 0.35460 0.28274 -0.04441 -0.05155 0.04958  389 LEU   A CA   
1773 C  C    . LEU   A 237 ? 0.29242 0.35894 0.30914 -0.04048 -0.04975 0.05270  389 LEU   A C    
1774 O  O    . LEU   A 237 ? 0.29101 0.36032 0.29869 -0.04296 -0.04555 0.05516  389 LEU   A O    
1775 C  CB   . LEU   A 237 ? 0.27005 0.33882 0.26492 -0.04400 -0.04512 0.03223  389 LEU   A CB   
1776 C  CG   . LEU   A 237 ? 0.32323 0.40281 0.30557 -0.05000 -0.04549 0.02652  389 LEU   A CG   
1777 C  CD1  . LEU   A 237 ? 0.25921 0.32735 0.23896 -0.04908 -0.04079 0.01249  389 LEU   A CD1  
1778 C  CD2  . LEU   A 237 ? 0.35741 0.44723 0.31949 -0.05664 -0.04181 0.02473  389 LEU   A CD2  
1779 N  N    . ASN   A 238 ? 0.23896 0.29411 0.27569 -0.03470 -0.05268 0.05144  390 ASN   A N    
1780 C  CA   . ASN   A 238 ? 0.29810 0.34308 0.34774 -0.03194 -0.05238 0.05373  390 ASN   A CA   
1781 C  C    . ASN   A 238 ? 0.30945 0.36243 0.36669 -0.03567 -0.05635 0.07183  390 ASN   A C    
1782 O  O    . ASN   A 238 ? 0.27894 0.33183 0.33329 -0.03780 -0.05288 0.07486  390 ASN   A O    
1783 C  CB   . ASN   A 238 ? 0.27982 0.31376 0.35107 -0.02586 -0.05564 0.04779  390 ASN   A CB   
1784 C  CG   . ASN   A 238 ? 0.36262 0.38537 0.44626 -0.02367 -0.05505 0.04519  390 ASN   A CG   
1785 O  OD1  . ASN   A 238 ? 0.32926 0.35321 0.41374 -0.02676 -0.05479 0.05380  390 ASN   A OD1  
1786 N  ND2  . ASN   A 238 ? 0.30398 0.31796 0.39742 -0.01901 -0.05472 0.03259  390 ASN   A ND2  
1787 N  N    . GLU   A 239 ? 0.28333 0.34501 0.35145 -0.03673 -0.06383 0.08539  391 GLU   A N    
1788 C  CA   . GLU   A 239 ? 0.36130 0.43186 0.43780 -0.04100 -0.06849 0.10626  391 GLU   A CA   
1789 C  C    . GLU   A 239 ? 0.34288 0.42931 0.39479 -0.04825 -0.06303 0.11031  391 GLU   A C    
1790 O  O    . GLU   A 239 ? 0.33122 0.42095 0.38571 -0.05174 -0.06137 0.12035  391 GLU   A O    
1791 C  CB   . GLU   A 239 ? 0.41818 0.49818 0.50879 -0.04072 -0.07810 0.12142  391 GLU   A CB   
1792 C  CG   . GLU   A 239 ? 0.58728 0.65276 0.70985 -0.03304 -0.08401 0.12106  391 GLU   A CG   
1793 C  CD   . GLU   A 239 ? 0.77399 0.85049 0.90841 -0.03084 -0.09234 0.13060  391 GLU   A CD   
1794 O  OE1  . GLU   A 239 ? 0.81950 0.88858 0.97056 -0.02377 -0.09384 0.12022  391 GLU   A OE1  
1795 O  OE2  . GLU   A 239 ? 0.82074 0.91586 0.94784 -0.03635 -0.09736 0.14853  391 GLU   A OE2  
1796 N  N    . GLU   A 240 ? 0.33768 0.43517 0.36663 -0.05108 -0.05979 0.10170  392 GLU   A N    
1797 C  CA   . GLU   A 240 ? 0.36425 0.47845 0.36984 -0.05783 -0.05380 0.10232  392 GLU   A CA   
1798 C  C    . GLU   A 240 ? 0.34421 0.44940 0.34324 -0.05608 -0.04413 0.09023  392 GLU   A C    
1799 O  O    . GLU   A 240 ? 0.32547 0.44229 0.31763 -0.06025 -0.03957 0.09610  392 GLU   A O    
1800 C  CB   . GLU   A 240 ? 0.34455 0.47151 0.32911 -0.06166 -0.05287 0.09300  392 GLU   A CB   
1801 C  CG   . GLU   A 240 ? 0.37416 0.52102 0.33434 -0.06909 -0.04655 0.09116  392 GLU   A CG   
1802 C  CD   . GLU   A 240 ? 0.41626 0.58486 0.37678 -0.07544 -0.05068 0.11381  392 GLU   A CD   
1803 O  OE1  . GLU   A 240 ? 0.38331 0.56490 0.33099 -0.07997 -0.04353 0.11451  392 GLU   A OE1  
1804 O  OE2  . GLU   A 240 ? 0.44744 0.62134 0.42220 -0.07588 -0.06096 0.13180  392 GLU   A OE2  
1805 N  N    . HIS   A 241 ? 0.25315 0.34008 0.25465 -0.05003 -0.04088 0.07417  393 HIS   A N    
1806 C  CA   . HIS   A 241 ? 0.24858 0.32798 0.24636 -0.04754 -0.03298 0.06443  393 HIS   A CA   
1807 C  C    . HIS   A 241 ? 0.33183 0.40991 0.34635 -0.04769 -0.03427 0.07538  393 HIS   A C    
1808 O  O    . HIS   A 241 ? 0.31486 0.40020 0.32485 -0.04949 -0.02824 0.07593  393 HIS   A O    
1809 C  CB   . HIS   A 241 ? 0.27213 0.33365 0.27100 -0.04137 -0.03085 0.04869  393 HIS   A CB   
1810 C  CG   . HIS   A 241 ? 0.26769 0.32205 0.26690 -0.03795 -0.02486 0.04160  393 HIS   A CG   
1811 N  ND1  . HIS   A 241 ? 0.27017 0.31625 0.28588 -0.03491 -0.02731 0.04350  393 HIS   A ND1  
1812 C  CD2  . HIS   A 241 ? 0.28964 0.34539 0.27659 -0.03704 -0.01691 0.03282  393 HIS   A CD2  
1813 C  CE1  . HIS   A 241 ? 0.28889 0.33320 0.30168 -0.03243 -0.02176 0.03726  393 HIS   A CE1  
1814 N  NE2  . HIS   A 241 ? 0.25845 0.30791 0.25494 -0.03300 -0.01524 0.03116  393 HIS   A NE2  
1815 N  N    . SER   A 242 ? 0.34178 0.41091 0.37779 -0.04593 -0.04184 0.08334  394 SER   A N    
1816 C  CA   . SER   A 242 ? 0.33500 0.40112 0.39003 -0.04727 -0.04381 0.09345  394 SER   A CA   
1817 C  C    . SER   A 242 ? 0.33765 0.42244 0.38992 -0.05485 -0.04331 0.11168  394 SER   A C    
1818 O  O    . SER   A 242 ? 0.34841 0.43774 0.40577 -0.05779 -0.03971 0.11650  394 SER   A O    
1819 C  CB   . SER   A 242 ? 0.39745 0.44946 0.47817 -0.04413 -0.05221 0.09722  394 SER   A CB   
1820 O  OG   . SER   A 242 ? 0.54592 0.58686 0.62580 -0.03805 -0.05270 0.08164  394 SER   A OG   
1821 N  N    A LYS   A 243 ? 0.33926 0.43782 0.38357 -0.05879 -0.04699 0.12285  395 LYS   A N    
1822 N  N    B LYS   A 243 ? 0.33962 0.43820 0.38382 -0.05878 -0.04696 0.12275  395 LYS   A N    
1823 C  CA   A LYS   A 243 ? 0.35146 0.47245 0.38907 -0.06709 -0.04621 0.14107  395 LYS   A CA   
1824 C  CA   B LYS   A 243 ? 0.35187 0.47289 0.38931 -0.06707 -0.04623 0.14098  395 LYS   A CA   
1825 C  C    A LYS   A 243 ? 0.34097 0.47589 0.35820 -0.06977 -0.03495 0.13170  395 LYS   A C    
1826 C  C    B LYS   A 243 ? 0.34108 0.47613 0.35822 -0.06981 -0.03499 0.13178  395 LYS   A C    
1827 O  O    A LYS   A 243 ? 0.34820 0.49420 0.36923 -0.07444 -0.03112 0.14142  395 LYS   A O    
1828 O  O    B LYS   A 243 ? 0.34833 0.49457 0.36924 -0.07452 -0.03118 0.14164  395 LYS   A O    
1829 C  CB   A LYS   A 243 ? 0.37970 0.51652 0.40768 -0.07081 -0.05222 0.15204  395 LYS   A CB   
1830 C  CB   B LYS   A 243 ? 0.37989 0.51641 0.40754 -0.07062 -0.05222 0.15140  395 LYS   A CB   
1831 C  CG   A LYS   A 243 ? 0.34862 0.47902 0.40168 -0.06969 -0.06397 0.17046  395 LYS   A CG   
1832 C  CG   B LYS   A 243 ? 0.39227 0.55358 0.41635 -0.07983 -0.05443 0.17572  395 LYS   A CG   
1833 C  CD   A LYS   A 243 ? 0.40363 0.55429 0.44656 -0.07359 -0.07058 0.18295  395 LYS   A CD   
1834 C  CD   B LYS   A 243 ? 0.37493 0.55127 0.39349 -0.08264 -0.06317 0.18809  395 LYS   A CD   
1835 C  CE   A LYS   A 243 ? 0.45518 0.59536 0.52505 -0.06857 -0.08222 0.19438  395 LYS   A CE   
1836 C  CE   B LYS   A 243 ? 0.45485 0.66522 0.45148 -0.09311 -0.06128 0.20236  395 LYS   A CE   
1837 N  NZ   A LYS   A 243 ? 0.49432 0.65064 0.55332 -0.06928 -0.08803 0.19615  395 LYS   A NZ   
1838 N  NZ   B LYS   A 243 ? 0.55537 0.77902 0.56507 -0.09789 -0.07274 0.23342  395 LYS   A NZ   
1839 N  N    . GLN   A 244 ? 0.36129 0.49588 0.35887 -0.06684 -0.02922 0.11249  396 GLN   A N    
1840 C  CA   . GLN   A 244 ? 0.32902 0.47507 0.31000 -0.06781 -0.01800 0.10094  396 GLN   A CA   
1841 C  C    . GLN   A 244 ? 0.36281 0.49712 0.35661 -0.06287 -0.01327 0.09407  396 GLN   A C    
1842 O  O    . GLN   A 244 ? 0.34152 0.48975 0.33312 -0.06509 -0.00571 0.09480  396 GLN   A O    
1843 C  CB   . GLN   A 244 ? 0.35046 0.49479 0.31158 -0.06567 -0.01388 0.08161  396 GLN   A CB   
1844 C  CG   . GLN   A 244 ? 0.38392 0.54096 0.33332 -0.07099 -0.01987 0.08699  396 GLN   A CG   
1845 C  CD   . GLN   A 244 ? 0.40897 0.57305 0.33560 -0.07275 -0.01373 0.06834  396 GLN   A CD   
1846 O  OE1  . GLN   A 244 ? 0.36193 0.52049 0.28237 -0.06947 -0.00436 0.05182  396 GLN   A OE1  
1847 N  NE2  . GLN   A 244 ? 0.39523 0.57164 0.31123 -0.07797 -0.01940 0.07075  396 GLN   A NE2  
1848 N  N    . TYR   A 245 ? 0.28093 0.39246 0.28838 -0.05644 -0.01760 0.08719  397 TYR   A N    
1849 C  CA   . TYR   A 245 ? 0.31764 0.42044 0.33793 -0.05245 -0.01490 0.08177  397 TYR   A CA   
1850 C  C    . TYR   A 245 ? 0.35406 0.46588 0.39118 -0.05805 -0.01643 0.09811  397 TYR   A C    
1851 O  O    . TYR   A 245 ? 0.31431 0.43438 0.35540 -0.05845 -0.01049 0.09680  397 TYR   A O    
1852 C  CB   . TYR   A 245 ? 0.31026 0.39055 0.34136 -0.04608 -0.02035 0.07269  397 TYR   A CB   
1853 C  CG   . TYR   A 245 ? 0.26282 0.33700 0.30704 -0.04293 -0.01918 0.06784  397 TYR   A CG   
1854 C  CD1  . TYR   A 245 ? 0.23954 0.31263 0.27605 -0.03770 -0.01288 0.05523  397 TYR   A CD1  
1855 C  CD2  . TYR   A 245 ? 0.31629 0.38650 0.38225 -0.04552 -0.02487 0.07626  397 TYR   A CD2  
1856 C  CE1  . TYR   A 245 ? 0.25912 0.32994 0.30805 -0.03492 -0.01292 0.05203  397 TYR   A CE1  
1857 C  CE2  . TYR   A 245 ? 0.28030 0.34771 0.35821 -0.04378 -0.02458 0.07112  397 TYR   A CE2  
1858 C  CZ   . TYR   A 245 ? 0.31907 0.38822 0.38777 -0.03841 -0.01888 0.05949  397 TYR   A CZ   
1859 O  OH   . TYR   A 245 ? 0.33658 0.40592 0.41761 -0.03670 -0.01969 0.05548  397 TYR   A OH   
1860 N  N    . ARG   A 246 ? 0.32214 0.43263 0.37179 -0.06246 -0.02456 0.11441  398 ARG   A N    
1861 C  CA   . ARG   A 246 ? 0.35722 0.47437 0.42562 -0.06901 -0.02663 0.13204  398 ARG   A CA   
1862 C  C    . ARG   A 246 ? 0.38188 0.52653 0.43811 -0.07597 -0.01841 0.14095  398 ARG   A C    
1863 O  O    . ARG   A 246 ? 0.36014 0.51325 0.42738 -0.07948 -0.01449 0.14599  398 ARG   A O    
1864 C  CB   . ARG   A 246 ? 0.47883 0.58878 0.56405 -0.07212 -0.03706 0.14948  398 ARG   A CB   
1865 C  CG   . ARG   A 246 ? 0.56393 0.64781 0.66929 -0.06591 -0.04444 0.14089  398 ARG   A CG   
1866 C  CD   . ARG   A 246 ? 0.64249 0.71777 0.77364 -0.06880 -0.05420 0.15895  398 ARG   A CD   
1867 N  NE   . ARG   A 246 ? 0.71384 0.80338 0.83791 -0.07287 -0.05776 0.17773  398 ARG   A NE   
1868 C  CZ   . ARG   A 246 ? 0.81998 0.90555 0.94258 -0.06868 -0.06358 0.17771  398 ARG   A CZ   
1869 N  NH1  . ARG   A 246 ? 0.84128 0.90895 0.96871 -0.06040 -0.06531 0.15927  398 ARG   A NH1  
1870 N  NH2  . ARG   A 246 ? 0.81736 0.91949 0.93367 -0.07312 -0.06771 0.19649  398 ARG   A NH2  
1871 N  N    . SER   A 247 ? 0.34251 0.50362 0.37599 -0.07851 -0.01535 0.14173  399 SER   A N    
1872 C  CA   . SER   A 247 ? 0.42999 0.62079 0.44905 -0.08531 -0.00630 0.14741  399 SER   A CA   
1873 C  C    . SER   A 247 ? 0.40371 0.59912 0.41674 -0.08040 0.00511  0.12844  399 SER   A C    
1874 O  O    . SER   A 247 ? 0.41985 0.63503 0.43594 -0.08462 0.01257  0.13351  399 SER   A O    
1875 C  CB   . SER   A 247 ? 0.51316 0.72166 0.50780 -0.08941 -0.00616 0.14947  399 SER   A CB   
1876 O  OG   . SER   A 247 ? 0.70000 0.90221 0.70190 -0.09160 -0.01798 0.16543  399 SER   A OG   
1877 N  N    . LEU   A 248 ? 0.39151 0.57001 0.39763 -0.07145 0.00675  0.10749  400 LEU   A N    
1878 C  CA   . LEU   A 248 ? 0.35587 0.53636 0.35981 -0.06528 0.01661  0.09049  400 LEU   A CA   
1879 C  C    . LEU   A 248 ? 0.31398 0.48886 0.34128 -0.06325 0.01564  0.09360  400 LEU   A C    
1880 O  O    . LEU   A 248 ? 0.34678 0.53864 0.37900 -0.06385 0.02368  0.09289  400 LEU   A O    
1881 C  CB   . LEU   A 248 ? 0.30443 0.46578 0.29806 -0.05674 0.01718  0.07053  400 LEU   A CB   
1882 C  CG   . LEU   A 248 ? 0.39452 0.56303 0.36478 -0.05868 0.02031  0.06183  400 LEU   A CG   
1883 C  CD1  . LEU   A 248 ? 0.36351 0.50850 0.32909 -0.05158 0.01839  0.04582  400 LEU   A CD1  
1884 C  CD2  . LEU   A 248 ? 0.45154 0.64410 0.40926 -0.06050 0.03283  0.05336  400 LEU   A CD2  
1885 N  N    . SER   A 249 ? 0.36654 0.51956 0.40931 -0.06120 0.00584  0.09618  401 SER   A N    
1886 C  CA   . SER   A 249 ? 0.36560 0.51324 0.43048 -0.06014 0.00356  0.09713  401 SER   A CA   
1887 C  C    . SER   A 249 ? 0.35328 0.51799 0.43357 -0.06974 0.00397  0.11526  401 SER   A C    
1888 O  O    . SER   A 249 ? 0.32570 0.49402 0.42332 -0.07027 0.00480  0.11528  401 SER   A O    
1889 C  CB   . SER   A 249 ? 0.38812 0.51031 0.46479 -0.05684 -0.00687 0.09390  401 SER   A CB   
1890 O  OG   . SER   A 249 ? 0.49461 0.61166 0.58077 -0.06290 -0.01467 0.10857  401 SER   A OG   
1891 N  N    . PHE   A 250 ? 0.37932 0.55614 0.45441 -0.07801 0.00304  0.13184  402 PHE   A N    
1892 C  CA   . PHE   A 250 ? 0.42239 0.61597 0.51268 -0.08848 0.00342  0.15212  402 PHE   A CA   
1893 C  C    . PHE   A 250 ? 0.40012 0.62155 0.48747 -0.09046 0.01569  0.14974  402 PHE   A C    
1894 O  O    . PHE   A 250 ? 0.36055 0.59469 0.46614 -0.09771 0.01701  0.16203  402 PHE   A O    
1895 C  CB   . PHE   A 250 ? 0.43939 0.64204 0.52296 -0.09676 -0.00057 0.17251  402 PHE   A CB   
1896 C  CG   . PHE   A 250 ? 0.52216 0.73497 0.62624 -0.10814 -0.00336 0.19745  402 PHE   A CG   
1897 C  CD1  . PHE   A 250 ? 0.60677 0.85220 0.70223 -0.11766 0.00435  0.21260  402 PHE   A CD1  
1898 C  CD2  . PHE   A 250 ? 0.58340 0.77379 0.71613 -0.10999 -0.01332 0.20540  402 PHE   A CD2  
1899 C  CE1  . PHE   A 250 ? 0.65258 0.90802 0.76779 -0.12933 0.00195  0.23793  402 PHE   A CE1  
1900 C  CE2  . PHE   A 250 ? 0.63394 0.83152 0.78834 -0.12132 -0.01607 0.22913  402 PHE   A CE2  
1901 C  CZ   . PHE   A 250 ? 0.67159 0.90165 0.81736 -0.13126 -0.00856 0.24677  402 PHE   A CZ   
1902 N  N    . GLN   A 251 ? 0.38605 0.61759 0.45276 -0.08430 0.02501  0.13360  403 GLN   A N    
1903 C  CA   . GLN   A 251 ? 0.31587 0.57347 0.38172 -0.08381 0.03774  0.12744  403 GLN   A CA   
1904 C  C    . GLN   A 251 ? 0.31518 0.56199 0.39777 -0.07481 0.03807  0.11385  403 GLN   A C    
1905 O  O    . GLN   A 251 ? 0.30885 0.53581 0.38528 -0.06464 0.03618  0.09761  403 GLN   A O    
1906 C  CB   . GLN   A 251 ? 0.40582 0.67763 0.44517 -0.08052 0.04773  0.11366  403 GLN   A CB   
1907 C  CG   . GLN   A 251 ? 0.52869 0.81039 0.54794 -0.08872 0.04535  0.12478  403 GLN   A CG   
1908 C  CD   . GLN   A 251 ? 0.79516 1.11507 0.80806 -0.09996 0.05367  0.13938  403 GLN   A CD   
1909 O  OE1  . GLN   A 251 ? 0.94026 1.28325 0.93085 -0.10164 0.06299  0.13093  403 GLN   A OE1  
1910 N  NE2  . GLN   A 251 ? 0.81232 1.14008 0.84504 -0.10853 0.05056  0.16106  403 GLN   A NE2  
1911 N  N    . PRO   A 252 ? 0.33845 0.59897 0.44272 -0.07876 0.03988  0.12097  404 PRO   A N    
1912 C  CA   . PRO   A 252 ? 0.29200 0.54459 0.41337 -0.07060 0.03837  0.10935  404 PRO   A CA   
1913 C  C    . PRO   A 252 ? 0.34246 0.59848 0.45427 -0.05815 0.04717  0.08983  404 PRO   A C    
1914 O  O    . PRO   A 252 ? 0.35530 0.59557 0.47430 -0.04893 0.04293  0.07912  404 PRO   A O    
1915 C  CB   . PRO   A 252 ? 0.31656 0.59230 0.46140 -0.07935 0.04094  0.12203  404 PRO   A CB   
1916 C  CG   . PRO   A 252 ? 0.42719 0.70846 0.57208 -0.09294 0.03794  0.14349  404 PRO   A CG   
1917 C  CD   . PRO   A 252 ? 0.39217 0.67501 0.50833 -0.09204 0.04149  0.14219  404 PRO   A CD   
1918 N  N    . GLU   A 253 ? 0.37334 0.65000 0.46984 -0.05776 0.05925  0.08482  405 GLU   A N    
1919 C  CA   . GLU   A 253 ? 0.40145 0.67866 0.49140 -0.04543 0.06802  0.06486  405 GLU   A CA   
1920 C  C    . GLU   A 253 ? 0.32831 0.57380 0.40465 -0.03752 0.06166  0.05328  405 GLU   A C    
1921 O  O    . GLU   A 253 ? 0.33564 0.57031 0.41569 -0.02618 0.06337  0.03976  405 GLU   A O    
1922 C  CB   . GLU   A 253 ? 0.48349 0.78904 0.55866 -0.04767 0.08251  0.05934  405 GLU   A CB   
1923 C  CG   . GLU   A 253 ? 0.60150 0.91443 0.65483 -0.05897 0.08165  0.06951  405 GLU   A CG   
1924 C  CD   . GLU   A 253 ? 0.62417 0.96092 0.68593 -0.07278 0.08136  0.09241  405 GLU   A CD   
1925 O  OE1  . GLU   A 253 ? 0.77027 1.14133 0.82707 -0.07829 0.09330  0.09451  405 GLU   A OE1  
1926 O  OE2  . GLU   A 253 ? 0.61071 0.93219 0.68505 -0.07843 0.06951  0.10812  405 GLU   A OE2  
1927 N  N    . ASN   A 254 ? 0.26864 0.49992 0.33090 -0.04340 0.05420  0.05957  406 ASN   A N    
1928 C  CA   . ASN   A 254 ? 0.26309 0.46554 0.31447 -0.03728 0.04758  0.05018  406 ASN   A CA   
1929 C  C    . ASN   A 254 ? 0.31817 0.49943 0.38478 -0.03384 0.03652  0.05219  406 ASN   A C    
1930 O  O    . ASN   A 254 ? 0.32808 0.49213 0.39366 -0.02496 0.03444  0.04141  406 ASN   A O    
1931 C  CB   . ASN   A 254 ? 0.28793 0.48594 0.32115 -0.04461 0.04328  0.05629  406 ASN   A CB   
1932 C  CG   . ASN   A 254 ? 0.43544 0.65319 0.44847 -0.04755 0.05341  0.05003  406 ASN   A CG   
1933 O  OD1  . ASN   A 254 ? 0.47102 0.69810 0.47090 -0.05616 0.05132  0.05937  406 ASN   A OD1  
1934 N  ND2  . ASN   A 254 ? 0.44854 0.67376 0.45990 -0.04031 0.06425  0.03380  406 ASN   A ND2  
1935 N  N    . SER   A 255 ? 0.32592 0.50867 0.40692 -0.04148 0.02927  0.06593  407 SER   A N    
1936 C  CA   . SER   A 255 ? 0.29314 0.45804 0.38848 -0.03950 0.01878  0.06575  407 SER   A CA   
1937 C  C    . SER   A 255 ? 0.24152 0.41056 0.34925 -0.03141 0.02044  0.05754  407 SER   A C    
1938 O  O    . SER   A 255 ? 0.28097 0.43446 0.39252 -0.02642 0.01311  0.05198  407 SER   A O    
1939 C  CB   . SER   A 255 ? 0.40409 0.57149 0.51633 -0.04997 0.01187  0.08070  407 SER   A CB   
1940 O  OG   . SER   A 255 ? 0.56024 0.71173 0.66664 -0.05397 0.00468  0.08649  407 SER   A OG   
1941 N  N    . MET   A 256 ? 0.26474 0.45686 0.37924 -0.02992 0.03000  0.05701  408 MET   A N    
1942 C  CA   . MET   A 256 ? 0.24234 0.44105 0.37076 -0.02087 0.03183  0.05001  408 MET   A CA   
1943 C  C    . MET   A 256 ? 0.29522 0.47589 0.41290 -0.00912 0.03213  0.03759  408 MET   A C    
1944 O  O    . MET   A 256 ? 0.29029 0.46800 0.41884 -0.00150 0.02838  0.03418  408 MET   A O    
1945 C  CB   . MET   A 256 ? 0.28022 0.50870 0.41786 -0.02038 0.04393  0.05033  408 MET   A CB   
1946 C  CG   . MET   A 256 ? 0.37340 0.62356 0.53300 -0.02918 0.04277  0.06206  408 MET   A CG   
1947 S  SD   . MET   A 256 ? 0.41359 0.70017 0.58806 -0.02448 0.05747  0.05859  408 MET   A SD   
1948 C  CE   . MET   A 256 ? 0.30005 0.59207 0.44800 -0.02333 0.07098  0.05057  408 MET   A CE   
1949 N  N    . LYS   A 257 ? 0.26218 0.43183 0.35949 -0.00813 0.03611  0.03168  409 LYS   A N    
1950 C  CA   . LYS   A 257 ? 0.25021 0.40203 0.33816 0.00168  0.03734  0.02041  409 LYS   A CA   
1951 C  C    . LYS   A 257 ? 0.23187 0.35905 0.31135 0.00137  0.02687  0.02055  409 LYS   A C    
1952 O  O    . LYS   A 257 ? 0.28647 0.39810 0.35964 0.00854  0.02667  0.01343  409 LYS   A O    
1953 C  CB   . LYS   A 257 ? 0.32590 0.47984 0.39739 0.00222  0.04769  0.01147  409 LYS   A CB   
1954 C  CG   . LYS   A 257 ? 0.37906 0.55989 0.45697 0.00292  0.06008  0.00827  409 LYS   A CG   
1955 C  CD   . LYS   A 257 ? 0.50005 0.69024 0.60077 0.01271  0.06266  0.00606  409 LYS   A CD   
1956 C  CE   . LYS   A 257 ? 0.70679 0.91371 0.81143 0.01954  0.07728  -0.00601 409 LYS   A CE   
1957 N  NZ   . LYS   A 257 ? 0.74755 0.93753 0.85902 0.03338  0.07924  -0.01734 409 LYS   A NZ   
1958 N  N    . LEU   A 258 ? 0.22626 0.34984 0.30705 -0.00673 0.01862  0.02836  410 LEU   A N    
1959 C  CA   . LEU   A 258 ? 0.27047 0.37370 0.34516 -0.00691 0.00946  0.02709  410 LEU   A CA   
1960 C  C    . LEU   A 258 ? 0.29144 0.39288 0.37826 -0.00237 0.00277  0.02616  410 LEU   A C    
1961 O  O    . LEU   A 258 ? 0.28615 0.40143 0.38655 0.00137  0.00466  0.02709  410 LEU   A O    
1962 C  CB   . LEU   A 258 ? 0.32904 0.42927 0.40343 -0.01631 0.00370  0.03454  410 LEU   A CB   
1963 C  CG   . LEU   A 258 ? 0.34709 0.45298 0.40938 -0.02177 0.00871  0.03842  410 LEU   A CG   
1964 C  CD1  . LEU   A 258 ? 0.31703 0.41924 0.38327 -0.03006 0.00150  0.04856  410 LEU   A CD1  
1965 C  CD2  . LEU   A 258 ? 0.31296 0.40855 0.35639 -0.01760 0.01261  0.02905  410 LEU   A CD2  
1966 N  N    . THR   A 259 ? 0.23049 0.31748 0.31268 -0.00275 -0.00518 0.02411  411 THR   A N    
1967 C  CA   . THR   A 259 ? 0.25239 0.34034 0.34338 -0.00025 -0.01267 0.02308  411 THR   A CA   
1968 C  C    . THR   A 259 ? 0.21324 0.30199 0.31410 -0.00837 -0.02082 0.02483  411 THR   A C    
1969 O  O    . THR   A 259 ? 0.26881 0.35144 0.36811 -0.01449 -0.02148 0.02709  411 THR   A O    
1970 C  CB   . THR   A 259 ? 0.26375 0.33730 0.34192 0.00522  -0.01516 0.01833  411 THR   A CB   
1971 O  OG1  . THR   A 259 ? 0.30506 0.36616 0.37382 0.00040  -0.01907 0.01582  411 THR   A OG1  
1972 C  CG2  . THR   A 259 ? 0.27822 0.34543 0.34715 0.01179  -0.00691 0.01589  411 THR   A CG2  
1973 N  N    . PRO   A 260 ? 0.22974 0.32655 0.34265 -0.00880 -0.02754 0.02376  412 PRO   A N    
1974 C  CA   . PRO   A 260 ? 0.22117 0.31688 0.34507 -0.01699 -0.03547 0.02237  412 PRO   A CA   
1975 C  C    . PRO   A 260 ? 0.23414 0.31266 0.34781 -0.01856 -0.03918 0.01657  412 PRO   A C    
1976 O  O    . PRO   A 260 ? 0.27181 0.34437 0.39404 -0.02505 -0.04231 0.01690  412 PRO   A O    
1977 C  CB   . PRO   A 260 ? 0.25059 0.35931 0.38492 -0.01596 -0.04209 0.01954  412 PRO   A CB   
1978 C  CG   . PRO   A 260 ? 0.26501 0.38736 0.40304 -0.00907 -0.03630 0.02445  412 PRO   A CG   
1979 C  CD   . PRO   A 260 ? 0.23338 0.34341 0.35404 -0.00252 -0.02829 0.02428  412 PRO   A CD   
1980 N  N    . LEU   A 261 ? 0.24884 0.31956 0.34638 -0.01274 -0.03873 0.01182  413 LEU   A N    
1981 C  CA   . LEU   A 261 ? 0.24911 0.30645 0.33763 -0.01398 -0.04129 0.00573  413 LEU   A CA   
1982 C  C    . LEU   A 261 ? 0.23169 0.27954 0.31582 -0.01595 -0.03708 0.00947  413 LEU   A C    
1983 O  O    . LEU   A 261 ? 0.28085 0.32083 0.36933 -0.01948 -0.04041 0.00722  413 LEU   A O    
1984 C  CB   . LEU   A 261 ? 0.23998 0.29382 0.31242 -0.00827 -0.04103 0.00175  413 LEU   A CB   
1985 C  CG   . LEU   A 261 ? 0.30387 0.34749 0.36675 -0.00937 -0.04270 -0.00522 413 LEU   A CG   
1986 C  CD1  . LEU   A 261 ? 0.31305 0.35949 0.38637 -0.01407 -0.04963 -0.01366 413 LEU   A CD1  
1987 C  CD2  . LEU   A 261 ? 0.29067 0.33247 0.33743 -0.00469 -0.04117 -0.00608 413 LEU   A CD2  
1988 N  N    . VAL   A 262 ? 0.20534 0.25505 0.28182 -0.01358 -0.03000 0.01465  414 VAL   A N    
1989 C  CA   . VAL   A 262 ? 0.21991 0.26486 0.29071 -0.01634 -0.02658 0.01879  414 VAL   A CA   
1990 C  C    . VAL   A 262 ? 0.24520 0.29414 0.33150 -0.02335 -0.02935 0.02628  414 VAL   A C    
1991 O  O    . VAL   A 262 ? 0.28841 0.33042 0.37654 -0.02658 -0.03184 0.02925  414 VAL   A O    
1992 C  CB   . VAL   A 262 ? 0.25642 0.30573 0.31611 -0.01323 -0.01810 0.02056  414 VAL   A CB   
1993 C  CG1  . VAL   A 262 ? 0.28514 0.33661 0.34019 -0.01804 -0.01513 0.02625  414 VAL   A CG1  
1994 C  CG2  . VAL   A 262 ? 0.30072 0.34067 0.34615 -0.00744 -0.01578 0.01404  414 VAL   A CG2  
1995 N  N    . LEU   A 263 ? 0.26169 0.32228 0.36155 -0.02594 -0.02934 0.03052  415 LEU   A N    
1996 C  CA   . LEU   A 263 ? 0.26478 0.32903 0.38180 -0.03386 -0.03202 0.03938  415 LEU   A CA   
1997 C  C    . LEU   A 263 ? 0.24317 0.29544 0.37346 -0.03702 -0.04045 0.03494  415 LEU   A C    
1998 O  O    . LEU   A 263 ? 0.29452 0.34108 0.43615 -0.04216 -0.04328 0.04207  415 LEU   A O    
1999 C  CB   . LEU   A 263 ? 0.25296 0.33386 0.38341 -0.03654 -0.03012 0.04393  415 LEU   A CB   
2000 C  CG   . LEU   A 263 ? 0.24342 0.33936 0.36645 -0.03502 -0.02053 0.04958  415 LEU   A CG   
2001 C  CD1  . LEU   A 263 ? 0.21631 0.33055 0.35437 -0.03577 -0.01859 0.05158  415 LEU   A CD1  
2002 C  CD2  . LEU   A 263 ? 0.26260 0.36197 0.38328 -0.04151 -0.01755 0.06098  415 LEU   A CD2  
2003 N  N    . GLU   A 264 ? 0.25963 0.30884 0.38952 -0.03398 -0.04455 0.02316  416 GLU   A N    
2004 C  CA   . GLU   A 264 ? 0.31511 0.35433 0.45740 -0.03669 -0.05169 0.01498  416 GLU   A CA   
2005 C  C    . GLU   A 264 ? 0.28841 0.31443 0.42400 -0.03419 -0.05190 0.01256  416 GLU   A C    
2006 O  O    . GLU   A 264 ? 0.35302 0.36981 0.50447 -0.03730 -0.05601 0.01303  416 GLU   A O    
2007 C  CB   . GLU   A 264 ? 0.31997 0.36380 0.46011 -0.03458 -0.05559 0.00210  416 GLU   A CB   
2008 C  CG   . GLU   A 264 ? 0.29768 0.33580 0.45441 -0.03912 -0.06279 -0.00896 416 GLU   A CG   
2009 C  CD   . GLU   A 264 ? 0.31696 0.36306 0.46706 -0.03757 -0.06668 -0.02271 416 GLU   A CD   
2010 O  OE1  . GLU   A 264 ? 0.41149 0.45329 0.54881 -0.03381 -0.06657 -0.03211 416 GLU   A OE1  
2011 O  OE2  . GLU   A 264 ? 0.34579 0.40483 0.50367 -0.04064 -0.07003 -0.02361 416 GLU   A OE2  
2012 N  N    . VAL   A 265 ? 0.25781 0.28280 0.37244 -0.02860 -0.04764 0.01024  417 VAL   A N    
2013 C  CA   . VAL   A 265 ? 0.28838 0.30362 0.39703 -0.02617 -0.04801 0.00637  417 VAL   A CA   
2014 C  C    . VAL   A 265 ? 0.40479 0.41826 0.51386 -0.02808 -0.04637 0.01856  417 VAL   A C    
2015 O  O    . VAL   A 265 ? 0.35173 0.35790 0.47224 -0.02902 -0.05003 0.02044  417 VAL   A O    
2016 C  CB   . VAL   A 265 ? 0.27806 0.29361 0.36554 -0.02085 -0.04455 -0.00083 417 VAL   A CB   
2017 C  CG1  . VAL   A 265 ? 0.37029 0.37862 0.45191 -0.01907 -0.04404 -0.00369 417 VAL   A CG1  
2018 C  CG2  . VAL   A 265 ? 0.29659 0.31625 0.38330 -0.01960 -0.04744 -0.01136 417 VAL   A CG2  
2019 N  N    . PHE   A 266 ? 0.35789 0.37953 0.45523 -0.02852 -0.04098 0.02680  418 PHE   A N    
2020 C  CA   . PHE   A 266 ? 0.35903 0.38314 0.45260 -0.03106 -0.03944 0.03798  418 PHE   A CA   
2021 C  C    . PHE   A 266 ? 0.42439 0.45218 0.53620 -0.03746 -0.04233 0.05176  418 PHE   A C    
2022 O  O    . PHE   A 266 ? 0.42514 0.45233 0.54082 -0.03995 -0.04470 0.06220  418 PHE   A O    
2023 C  CB   . PHE   A 266 ? 0.30450 0.33750 0.37791 -0.02981 -0.03196 0.03921  418 PHE   A CB   
2024 C  CG   . PHE   A 266 ? 0.31383 0.34109 0.37002 -0.02509 -0.02938 0.02945  418 PHE   A CG   
2025 C  CD1  . PHE   A 266 ? 0.34053 0.37237 0.38027 -0.02362 -0.02264 0.02748  418 PHE   A CD1  
2026 C  CD2  . PHE   A 266 ? 0.36577 0.38356 0.42359 -0.02257 -0.03319 0.02163  418 PHE   A CD2  
2027 C  CE1  . PHE   A 266 ? 0.36386 0.38888 0.39008 -0.02041 -0.02042 0.01928  418 PHE   A CE1  
2028 C  CE2  . PHE   A 266 ? 0.33688 0.35064 0.37983 -0.01951 -0.03050 0.01423  418 PHE   A CE2  
2029 C  CZ   . PHE   A 266 ? 0.38225 0.39858 0.40989 -0.01876 -0.02445 0.01374  418 PHE   A CZ   
2030 N  N    . GLY   A 267 ? 0.38958 0.42245 0.51358 -0.04067 -0.04255 0.05353  419 GLY   A N    
2031 C  CA   . GLY   A 267 ? 0.41076 0.44680 0.55463 -0.04809 -0.04529 0.06752  419 GLY   A CA   
2032 C  C    . GLY   A 267 ? 0.49790 0.54994 0.64446 -0.05253 -0.04066 0.07441  419 GLY   A C    
2033 O  O    . GLY   A 267 ? 0.41175 0.47555 0.54184 -0.04975 -0.03360 0.07225  419 GLY   A O    
2034 N  N    . ASN   A 268 ? 0.56644 0.61913 0.73644 -0.05968 -0.04443 0.08248  420 ASN   A N    
2035 C  CA   . ASN   A 268 ? 0.66190 0.73172 0.83977 -0.06543 -0.04049 0.09021  420 ASN   A CA   
2036 C  C    . ASN   A 268 ? 0.69215 0.77121 0.86184 -0.06002 -0.03660 0.07736  420 ASN   A C    
2037 O  O    . ASN   A 268 ? 0.72243 0.79873 0.90419 -0.06004 -0.04121 0.06816  420 ASN   A O    
2038 C  CB   . ASN   A 268 ? 0.67890 0.76528 0.84660 -0.06966 -0.03395 0.10646  420 ASN   A CB   
2039 C  CG   . ASN   A 268 ? 0.74648 0.83330 0.93353 -0.07959 -0.03789 0.12651  420 ASN   A CG   
2040 O  OD1  . ASN   A 268 ? 0.82767 0.93194 1.00970 -0.08548 -0.03307 0.14232  420 ASN   A OD1  
2041 N  ND2  . ASN   A 268 ? 0.78312 0.85120 0.99309 -0.08171 -0.04656 0.12603  420 ASN   A ND2  
2042 N  N    . LYS   B 1   ? 0.93944 0.89580 1.12251 -0.03869 -0.06644 0.06545  625 LYS   C N    
2043 C  CA   . LYS   B 1   ? 0.87998 0.83919 1.04465 -0.03849 -0.04072 0.03348  625 LYS   C CA   
2044 C  C    . LYS   B 1   ? 0.80186 0.78240 0.98906 -0.01323 -0.02504 -0.00223 625 LYS   C C    
2045 O  O    . LYS   B 1   ? 0.80976 0.79953 1.03538 0.00443  -0.02971 -0.00538 625 LYS   C O    
2046 C  CB   . LYS   B 1   ? 0.88475 0.84718 0.98332 -0.06351 -0.03050 0.03072  625 LYS   C CB   
2047 C  CG   . LYS   B 1   ? 0.85777 0.84233 0.92973 -0.06166 -0.02906 0.02313  625 LYS   C CG   
2048 C  CD   . LYS   B 1   ? 0.88163 0.86320 0.90024 -0.09336 -0.03696 0.04435  625 LYS   C CD   
2049 C  CE   . LYS   B 1   ? 0.83845 0.84266 0.83209 -0.09503 -0.02686 0.02627  625 LYS   C CE   
2050 N  NZ   . LYS   B 1   ? 0.81110 0.83029 0.83015 -0.07235 -0.04006 0.03129  625 LYS   C NZ   
2051 N  N    . ASN   B 2   ? 0.73860 0.72704 0.90238 -0.01503 -0.00707 -0.02816 626 ASN   C N    
2052 C  CA   . ASN   B 2   ? 0.68612 0.69582 0.85943 0.00238  0.00422  -0.05810 626 ASN   C CA   
2053 C  C    . ASN   B 2   ? 0.61043 0.63832 0.75218 0.00048  0.00361  -0.05765 626 ASN   C C    
2054 O  O    . ASN   B 2   ? 0.60344 0.62784 0.71336 -0.01706 0.00498  -0.05032 626 ASN   C O    
2055 C  CB   . ASN   B 2   ? 0.79281 0.80105 0.96864 0.00122  0.01791  -0.08282 626 ASN   C CB   
2056 C  CG   . ASN   B 2   ? 0.93699 0.92702 1.14848 0.00260  0.01916  -0.08378 626 ASN   C CG   
2057 O  OD1  . ASN   B 2   ? 0.97010 0.96580 1.21614 0.01575  0.02366  -0.10264 626 ASN   C OD1  
2058 N  ND2  . ASN   B 2   ? 1.00101 0.96957 1.20509 -0.01361 0.01578  -0.06357 626 ASN   C ND2  
2059 N  N    . HIS   B 3   ? 0.49326 0.53981 0.64564 0.01536  0.00340  -0.06640 627 HIS   C N    
2060 C  CA   . HIS   B 3   ? 0.40599 0.47026 0.53703 0.01526  0.00213  -0.06504 627 HIS   C CA   
2061 C  C    . HIS   B 3   ? 0.37053 0.45334 0.50246 0.02333  0.00924  -0.08605 627 HIS   C C    
2062 O  O    . HIS   B 3   ? 0.39713 0.49558 0.53414 0.03261  0.00838  -0.08861 627 HIS   C O    
2063 C  CB   . HIS   B 3   ? 0.38349 0.45289 0.52576 0.02204  -0.00853 -0.04865 627 HIS   C CB   
2064 C  CG   . HIS   B 3   ? 0.42352 0.47549 0.56591 0.01130  -0.02300 -0.02177 627 HIS   C CG   
2065 N  ND1  . HIS   B 3   ? 0.50081 0.53556 0.67697 0.01348  -0.03042 -0.01132 627 HIS   C ND1  
2066 C  CD2  . HIS   B 3   ? 0.45359 0.50298 0.56700 -0.00485 -0.03357 -0.00168 627 HIS   C CD2  
2067 C  CE1  . HIS   B 3   ? 0.46377 0.48503 0.63116 -0.00102 -0.04854 0.01899  627 HIS   C CE1  
2068 N  NE2  . HIS   B 3   ? 0.48323 0.51373 0.60742 -0.01373 -0.05038 0.02446  627 HIS   C NE2  
2069 N  N    . PRO   B 4   ? 0.38746 0.46922 0.51553 0.01754  0.01494  -0.09979 628 PRO   C N    
2070 C  CA   . PRO   B 4   ? 0.38256 0.48114 0.51359 0.02235  0.01517  -0.11492 628 PRO   C CA   
2071 C  C    . PRO   B 4   ? 0.30482 0.42140 0.42814 0.02301  0.01019  -0.10888 628 PRO   C C    
2072 O  O    . PRO   B 4   ? 0.31991 0.45214 0.44188 0.02702  0.00656  -0.11294 628 PRO   C O    
2073 C  CB   . PRO   B 4   ? 0.32476 0.41582 0.46219 0.01427  0.01886  -0.12724 628 PRO   C CB   
2074 C  CG   . PRO   B 4   ? 0.39603 0.47218 0.52586 0.00205  0.02441  -0.11925 628 PRO   C CG   
2075 C  CD   . PRO   B 4   ? 0.43090 0.49697 0.55327 0.00362  0.02053  -0.10137 628 PRO   C CD   
2076 N  N    . MET   B 5   ? 0.28364 0.39913 0.40129 0.01633  0.01029  -0.09971 629 MET   C N    
2077 C  CA   . MET   B 5   ? 0.28415 0.41661 0.40363 0.01700  0.00619  -0.09504 629 MET   C CA   
2078 C  C    . MET   B 5   ? 0.30225 0.44406 0.41622 0.02603  0.00246  -0.08433 629 MET   C C    
2079 O  O    . MET   B 5   ? 0.29195 0.44991 0.40773 0.03006  -0.00114 -0.08251 629 MET   C O    
2080 C  CB   . MET   B 5   ? 0.29790 0.42790 0.41835 0.00426  0.01139  -0.09527 629 MET   C CB   
2081 C  CG   . MET   B 5   ? 0.34861 0.47478 0.48813 -0.00556 0.01812  -0.11087 629 MET   C CG   
2082 S  SD   . MET   B 5   ? 0.43059 0.55433 0.57393 -0.02704 0.03323  -0.12103 629 MET   C SD   
2083 C  CE   . MET   B 5   ? 0.50918 0.61103 0.61302 -0.04056 0.03972  -0.11407 629 MET   C CE   
2084 N  N    . LEU   B 6   ? 0.31979 0.45150 0.43095 0.02778  0.00203  -0.07565 630 LEU   C N    
2085 C  CA   . LEU   B 6   ? 0.35012 0.49016 0.46818 0.03705  -0.00072 -0.06820 630 LEU   C CA   
2086 C  C    . LEU   B 6   ? 0.34281 0.49061 0.46973 0.04454  0.00495  -0.08090 630 LEU   C C    
2087 O  O    . LEU   B 6   ? 0.39315 0.55680 0.52031 0.04804  0.00718  -0.08200 630 LEU   C O    
2088 C  CB   . LEU   B 6   ? 0.35709 0.48338 0.48152 0.03615  -0.00702 -0.05403 630 LEU   C CB   
2089 C  CG   . LEU   B 6   ? 0.50788 0.64069 0.65589 0.04681  -0.01015 -0.04835 630 LEU   C CG   
2090 C  CD1  . LEU   B 6   ? 0.42540 0.57623 0.56829 0.04878  -0.01098 -0.04445 630 LEU   C CD1  
2091 C  CD2  . LEU   B 6   ? 0.58583 0.70281 0.74876 0.04403  -0.02306 -0.02964 630 LEU   C CD2  
2092 N  N    . MET   B 7   ? 0.37766 0.51518 0.51096 0.04415  0.00928  -0.09261 631 MET   C N    
2093 C  CA   . MET   B 7   ? 0.41042 0.55703 0.54926 0.04622  0.01759  -0.11090 631 MET   C CA   
2094 C  C    . MET   B 7   ? 0.35201 0.51751 0.46833 0.04020  0.01562  -0.11487 631 MET   C C    
2095 O  O    . MET   B 7   ? 0.39479 0.57577 0.50437 0.03806  0.02163  -0.12209 631 MET   C O    
2096 C  CB   . MET   B 7   ? 0.47372 0.60673 0.62360 0.04458  0.02193  -0.12469 631 MET   C CB   
2097 C  CG   . MET   B 7   ? 0.59180 0.71048 0.77723 0.05041  0.02578  -0.12563 631 MET   C CG   
2098 S  SD   . MET   B 7   ? 0.56435 0.69719 0.78248 0.05585  0.04005  -0.14539 631 MET   C SD   
2099 C  CE   . MET   B 7   ? 0.69162 0.84743 0.87217 0.04490  0.04972  -0.16935 631 MET   C CE   
2100 N  N    . ASN   B 8   ? 0.33454 0.49916 0.44266 0.03488  0.00689  -0.10973 632 ASN   C N    
2101 C  CA   . ASN   B 8   ? 0.31252 0.49344 0.40816 0.02764  -0.00176 -0.10733 632 ASN   C CA   
2102 C  C    . ASN   B 8   ? 0.33757 0.53305 0.42806 0.02834  -0.00424 -0.09346 632 ASN   C C    
2103 O  O    . ASN   B 8   ? 0.38882 0.60013 0.46317 0.02090  -0.00728 -0.09149 632 ASN   C O    
2104 C  CB   . ASN   B 8   ? 0.34235 0.51803 0.44978 0.02303  -0.01151 -0.10439 632 ASN   C CB   
2105 C  CG   . ASN   B 8   ? 0.44932 0.64041 0.55645 0.01491  -0.02712 -0.09636 632 ASN   C CG   
2106 O  OD1  . ASN   B 8   ? 0.47771 0.67558 0.59905 0.01424  -0.03487 -0.08263 632 ASN   C OD1  
2107 N  ND2  . ASN   B 8   ? 0.45847 0.65549 0.55221 0.00671  -0.03367 -0.10388 632 ASN   C ND2  
2108 N  N    . LEU   B 9   ? 0.25788 0.44870 0.35944 0.03440  -0.00329 -0.08327 633 LEU   C N    
2109 C  CA   . LEU   B 9   ? 0.28468 0.48889 0.38667 0.03583  -0.00489 -0.07112 633 LEU   C CA   
2110 C  C    . LEU   B 9   ? 0.29732 0.50923 0.39537 0.03885  0.00571  -0.07649 633 LEU   C C    
2111 O  O    . LEU   B 9   ? 0.37384 0.60081 0.46581 0.03585  0.00681  -0.07020 633 LEU   C O    
2112 C  CB   . LEU   B 9   ? 0.34392 0.54219 0.45887 0.03876  -0.00660 -0.06221 633 LEU   C CB   
2113 C  CG   . LEU   B 9   ? 0.32244 0.51764 0.44952 0.03224  -0.01163 -0.06201 633 LEU   C CG   
2114 C  CD1  . LEU   B 9   ? 0.27550 0.46605 0.40857 0.02956  -0.00867 -0.05937 633 LEU   C CD1  
2115 C  CD2  . LEU   B 9   ? 0.34136 0.55129 0.48107 0.02834  -0.02135 -0.05435 633 LEU   C CD2  
2116 N  N    . LEU   B 10  ? 0.34293 0.54489 0.45104 0.04349  0.01469  -0.08896 634 LEU   C N    
2117 C  CA   . LEU   B 10  ? 0.36301 0.57297 0.48062 0.04462  0.02888  -0.10188 634 LEU   C CA   
2118 C  C    . LEU   B 10  ? 0.49507 0.71866 0.58900 0.03159  0.03774  -0.11891 634 LEU   C C    
2119 O  O    . LEU   B 10  ? 0.50514 0.73936 0.60388 0.02713  0.05474  -0.13531 634 LEU   C O    
2120 C  CB   . LEU   B 10  ? 0.32895 0.52319 0.47992 0.05303  0.03397  -0.10986 634 LEU   C CB   
2121 C  CG   . LEU   B 10  ? 0.36275 0.54671 0.53801 0.06167  0.02452  -0.09177 634 LEU   C CG   
2122 C  CD1  . LEU   B 10  ? 0.43159 0.59672 0.64070 0.06658  0.02219  -0.09252 634 LEU   C CD1  
2123 C  CD2  . LEU   B 10  ? 0.40333 0.60109 0.59527 0.06536  0.02944  -0.08930 634 LEU   C CD2  
2124 N  N    . LYS   B 11  ? 0.47889 0.70343 0.54945 0.02274  0.02677  -0.11659 635 LYS   C N    
2125 C  CA   . LYS   B 11  ? 0.63467 0.87175 0.67600 0.00569  0.02977  -0.13079 635 LYS   C CA   
2126 C  C    . LYS   B 11  ? 0.76167 0.99499 0.81555 0.00456  0.04849  -0.16111 635 LYS   C C    
2127 O  O    . LYS   B 11  ? 0.80238 1.02240 0.86780 0.00826  0.04554  -0.16925 635 LYS   C O    
2128 C  CB   . LYS   B 11  ? 0.66720 0.92546 0.68029 -0.00923 0.03330  -0.12536 635 LYS   C CB   
2129 C  CG   . LYS   B 11  ? 0.73981 1.01268 0.70980 -0.03434 0.03028  -0.13364 635 LYS   C CG   
2130 C  CD   . LYS   B 11  ? 0.78683 1.08082 0.72386 -0.05502 0.04351  -0.13692 635 LYS   C CD   
2131 C  CE   . LYS   B 11  ? 0.79332 1.08827 0.76077 -0.04417 0.07021  -0.15240 635 LYS   C CE   
2132 N  NZ   . LYS   B 11  ? 0.82703 1.14104 0.77029 -0.06828 0.09825  -0.18092 635 LYS   C NZ   
2133 C  C10  . A1L78 C .   ? 0.30165 0.29418 0.24335 -0.03300 0.00463  -0.03077 501 A1L78 A C10  
2134 C  C13  . A1L78 C .   ? 0.51170 0.52820 0.48001 -0.02181 0.00034  -0.00610 501 A1L78 A C13  
2135 C  C15  . A1L78 C .   ? 0.48040 0.50503 0.43942 -0.02105 0.01302  -0.01604 501 A1L78 A C15  
2136 C  C20  . A1L78 C .   ? 0.38108 0.45887 0.36878 -0.02613 0.01397  0.01619  501 A1L78 A C20  
2137 C  C21  . A1L78 C .   ? 0.40325 0.49435 0.40297 -0.03055 0.01150  0.02972  501 A1L78 A C21  
2138 C  C22  . A1L78 C .   ? 0.34363 0.39509 0.34650 -0.02084 0.00125  0.01750  501 A1L78 A C22  
2139 C  C26  . A1L78 C .   ? 0.49985 0.44085 0.46079 -0.01016 0.00371  -0.00725 501 A1L78 A C26  
2140 C  C28  . A1L78 C .   ? 0.45412 0.39792 0.42000 -0.00340 0.00124  0.00015  501 A1L78 A C28  
2141 C  C01  . A1L78 C .   ? 0.33629 0.28200 0.29351 -0.01505 0.01281  -0.02865 501 A1L78 A C01  
2142 C  C02  . A1L78 C .   ? 0.37587 0.32745 0.33731 -0.01136 0.00835  -0.02113 501 A1L78 A C02  
2143 C  C03  . A1L78 C .   ? 0.36451 0.32905 0.32825 -0.01121 0.00501  -0.01880 501 A1L78 A C03  
2144 C  C04  . A1L78 C .   ? 0.34627 0.31923 0.30703 -0.01484 0.00590  -0.02157 501 A1L78 A C04  
2145 C  C05  . A1L78 C .   ? 0.32859 0.29831 0.28271 -0.01856 0.01023  -0.02885 501 A1L78 A C05  
2146 C  C06  . A1L78 C .   ? 0.34585 0.30170 0.29868 -0.01870 0.01375  -0.03356 501 A1L78 A C06  
2147 C  C09  . A1L78 C .   ? 0.41705 0.41956 0.37054 -0.02248 0.00865  -0.02230 501 A1L78 A C09  
2148 C  C11  . A1L78 C .   ? 0.39652 0.38021 0.33581 -0.02682 0.01998  -0.04620 501 A1L78 A C11  
2149 C  C12  . A1L78 C .   ? 0.52209 0.52824 0.48300 -0.02228 0.00205  -0.01366 501 A1L78 A C12  
2150 C  C14  . A1L78 C .   ? 0.40192 0.42843 0.36897 -0.02177 0.00578  -0.00625 501 A1L78 A C14  
2151 C  C16  . A1L78 C .   ? 0.58741 0.59870 0.54030 -0.02136 0.01412  -0.02431 501 A1L78 A C16  
2152 C  C18  . A1L78 C .   ? 0.40068 0.45049 0.37721 -0.02241 0.00998  0.00327  501 A1L78 A C18  
2153 C  C19  . A1L78 C .   ? 0.32987 0.39038 0.31828 -0.02520 0.00600  0.01578  501 A1L78 A C19  
2154 C  C23  . A1L78 C .   ? 0.31785 0.36779 0.32498 -0.01421 0.00591  0.01170  501 A1L78 A C23  
2155 C  C25  . A1L78 C .   ? 0.46775 0.41785 0.43046 -0.00962 0.00286  -0.01171 501 A1L78 A C25  
2156 C  C29  . A1L78 C .   ? 0.50222 0.44946 0.46435 -0.00451 -0.00180 0.00751  501 A1L78 A C29  
2157 C  C30  . A1L78 C .   ? 0.59357 0.55628 0.55386 -0.00603 -0.00630 0.00455  501 A1L78 A C30  
2158 C  C33  . A1L78 C .   ? 0.33617 0.30681 0.30609 -0.00807 -0.00011 -0.01293 501 A1L78 A C33  
2159 C  C34  . A1L78 C .   ? 0.50603 0.52343 0.48560 -0.02180 -0.00706 0.00162  501 A1L78 A C34  
2160 C  C35  . A1L78 C .   ? 0.31113 0.30622 0.26116 -0.03098 -0.00180 -0.02225 501 A1L78 A C35  
2161 C  C36  . A1L78 C .   ? 0.40310 0.37984 0.35032 -0.01874 0.02572  -0.04846 501 A1L78 A C36  
2162 O  O07  . A1L78 C .   ? 0.46046 0.40461 0.42429 -0.00837 0.00744  -0.01590 501 A1L78 A O07  
2163 O  O17  . A1L78 C .   ? 0.36451 0.40199 0.34028 -0.02250 0.00408  0.00265  501 A1L78 A O17  
2164 O  O24  . A1L78 C .   ? 0.29587 0.36024 0.28410 -0.03090 -0.00004 0.02460  501 A1L78 A O24  
2165 O  O27  . A1L78 C .   ? 0.47594 0.42452 0.43291 -0.01486 0.00109  -0.00777 501 A1L78 A O27  
2166 O  O31  . A1L78 C .   ? 0.51923 0.48617 0.48124 -0.00782 -0.00681 -0.00202 501 A1L78 A O31  
2167 O  O32  . A1L78 C .   ? 0.42675 0.39758 0.38460 -0.00547 -0.00946 0.00909  501 A1L78 A O32  
2168 SI SI08 . A1L78 C .   ? 0.33774 0.32397 0.28449 -0.02480 0.01099  -0.03200 501 A1L78 A SI08 
# 
