data_8VSN
# 
_entry.id   8VSN 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8VSN         pdb_00008vsn 10.2210/pdb8vsn/pdb 
WWPDB D_1000278406 ?            ?                   
# 
_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       2025-03-19 
_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                        8VSN 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              michelle.arkin@ucsf.edu 
_pdbx_contact_author.name_first         Michelle 
_pdbx_contact_author.name_last          Arkin 
_pdbx_contact_author.name_mi            R 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9366-6770 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vickery, H.R.'        1 ? 
'Virta, J.M.'          2 ? 
'Pennings, M.'         3 ? 
'Konstantinidou, M.'   4 ? 
'van den Oetelaar, M.' 5 ? 
'Neitz, R.J.'          6 ? 
'Ottmann, C.'          7 ? 
'Brunsveld, L.'        8 ? 
'Arkin, M.R.'          9 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Ternary structure of 14-3-3 sigma, ARAF phosphopeptide (pS214) and compound 79 (1124379)' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_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 'Vickery, H.R.'        1 ? 
primary 'Virta, J.M.'          2 ? 
primary 'Pennings, M.'         3 ? 
primary 'Konstantinidou, M.'   4 ? 
primary 'van den Oetelaar, M.' 5 ? 
primary 'Neitz, R.J.'          6 ? 
primary 'Ottmann, C.'          7 ? 
primary 'Brunsveld, L.'        8 ? 
primary 'Arkin, M.R.'          9 ? 
# 
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 '14-3-3 protein sigma'                                                                 26542.914 1   ?        ? 
'residues 1-231'                       ?                              
2 polymer     syn 'Serine/threonine-protein kinase A-Raf phosphopeptide'                                 1481.594  1   2.7.11.1 ? 
'residues 209-220 (Uniprot numbering)' 'containing phosphoserine 214' 
3 non-polymer syn 'CHLORIDE ION'                                                                         35.453    1   ?        ? 
?                                      ?                              
4 non-polymer syn 'MAGNESIUM ION'                                                                        24.305    3   ?        ? 
?                                      ?                              
5 non-polymer syn '2-chloranyl-1-[8-(4-iodophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]ethanone' 470.710   1   ?        ? 
?                                      ?                              
6 water       nat water                                                                                  18.015    155 ?        ? 
?                                      ?                              
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Epithelial cell marker protein 1,Stratifin'                     
2 'Proto-oncogene A-Raf,Proto-oncogene A-Raf-1,Proto-oncogene Pks' 
# 
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  
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
A ? 
2 'polypeptide(L)' no yes 'RIRST(SEP)TPNVHM' RIRSTSTPNVHM P ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CHLORIDE ION'                                                                         CL  
4 'MAGNESIUM ION'                                                                        MG  
5 '2-chloranyl-1-[8-(4-iodophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]ethanone' WQT 
6 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   ALA n 
1 3   MET n 
1 4   GLY n 
1 5   SER n 
1 6   MET n 
1 7   GLU n 
1 8   ARG n 
1 9   ALA n 
1 10  SER n 
1 11  LEU n 
1 12  ILE n 
1 13  GLN n 
1 14  LYS n 
1 15  ALA n 
1 16  LYS n 
1 17  LEU n 
1 18  ALA n 
1 19  GLU n 
1 20  GLN n 
1 21  ALA n 
1 22  GLU n 
1 23  ARG n 
1 24  TYR n 
1 25  GLU n 
1 26  ASP n 
1 27  MET n 
1 28  ALA n 
1 29  ALA n 
1 30  PHE n 
1 31  MET n 
1 32  LYS n 
1 33  GLY n 
1 34  ALA n 
1 35  VAL n 
1 36  GLU n 
1 37  LYS n 
1 38  GLY n 
1 39  GLU n 
1 40  GLU n 
1 41  LEU n 
1 42  SER n 
1 43  CYS n 
1 44  GLU n 
1 45  GLU n 
1 46  ARG n 
1 47  ASN n 
1 48  LEU n 
1 49  LEU n 
1 50  SER n 
1 51  VAL n 
1 52  ALA n 
1 53  TYR n 
1 54  LYS n 
1 55  ASN n 
1 56  VAL n 
1 57  VAL n 
1 58  GLY n 
1 59  GLY n 
1 60  GLN n 
1 61  ARG n 
1 62  ALA n 
1 63  ALA n 
1 64  TRP n 
1 65  ARG n 
1 66  VAL n 
1 67  LEU n 
1 68  SER n 
1 69  SER n 
1 70  ILE n 
1 71  GLU n 
1 72  GLN n 
1 73  LYS n 
1 74  SER n 
1 75  ASN n 
1 76  GLU n 
1 77  GLU n 
1 78  GLY n 
1 79  SER n 
1 80  GLU n 
1 81  GLU n 
1 82  LYS n 
1 83  GLY n 
1 84  PRO n 
1 85  GLU n 
1 86  VAL n 
1 87  ARG n 
1 88  GLU n 
1 89  TYR n 
1 90  ARG n 
1 91  GLU n 
1 92  LYS n 
1 93  VAL n 
1 94  GLU n 
1 95  THR n 
1 96  GLU n 
1 97  LEU n 
1 98  GLN n 
1 99  GLY n 
1 100 VAL n 
1 101 CYS n 
1 102 ASP n 
1 103 THR n 
1 104 VAL n 
1 105 LEU n 
1 106 GLY n 
1 107 LEU n 
1 108 LEU n 
1 109 ASP n 
1 110 SER n 
1 111 HIS n 
1 112 LEU n 
1 113 ILE n 
1 114 LYS n 
1 115 GLU n 
1 116 ALA n 
1 117 GLY n 
1 118 ASP n 
1 119 ALA n 
1 120 GLU n 
1 121 SER n 
1 122 ARG n 
1 123 VAL n 
1 124 PHE n 
1 125 TYR n 
1 126 LEU n 
1 127 LYS n 
1 128 MET n 
1 129 LYS n 
1 130 GLY n 
1 131 ASP n 
1 132 TYR n 
1 133 TYR n 
1 134 ARG n 
1 135 TYR n 
1 136 LEU n 
1 137 ALA n 
1 138 GLU n 
1 139 VAL n 
1 140 ALA n 
1 141 THR n 
1 142 GLY n 
1 143 ASP n 
1 144 ASP n 
1 145 LYS n 
1 146 LYS n 
1 147 ARG n 
1 148 ILE n 
1 149 ILE n 
1 150 ASP n 
1 151 SER n 
1 152 ALA n 
1 153 ARG n 
1 154 SER n 
1 155 ALA n 
1 156 TYR n 
1 157 GLN n 
1 158 GLU n 
1 159 ALA n 
1 160 MET n 
1 161 ASP n 
1 162 ILE n 
1 163 SER n 
1 164 LYS n 
1 165 LYS n 
1 166 GLU n 
1 167 MET n 
1 168 PRO n 
1 169 PRO n 
1 170 THR n 
1 171 ASN n 
1 172 PRO n 
1 173 ILE n 
1 174 ARG n 
1 175 LEU n 
1 176 GLY n 
1 177 LEU n 
1 178 ALA n 
1 179 LEU n 
1 180 ASN n 
1 181 PHE n 
1 182 SER n 
1 183 VAL n 
1 184 PHE n 
1 185 HIS n 
1 186 TYR n 
1 187 GLU n 
1 188 ILE n 
1 189 ALA n 
1 190 ASN n 
1 191 SER n 
1 192 PRO n 
1 193 GLU n 
1 194 GLU n 
1 195 ALA n 
1 196 ILE n 
1 197 SER n 
1 198 LEU n 
1 199 ALA n 
1 200 LYS n 
1 201 THR n 
1 202 THR n 
1 203 PHE n 
1 204 ASP n 
1 205 GLU n 
1 206 ALA n 
1 207 MET n 
1 208 ALA n 
1 209 ASP n 
1 210 LEU n 
1 211 HIS n 
1 212 THR n 
1 213 LEU n 
1 214 SER n 
1 215 GLU n 
1 216 ASP n 
1 217 SER n 
1 218 TYR n 
1 219 LYS n 
1 220 ASP n 
1 221 SER n 
1 222 THR n 
1 223 LEU n 
1 224 ILE n 
1 225 MET n 
1 226 GLN n 
1 227 LEU n 
1 228 LEU n 
1 229 ARG n 
1 230 ASP n 
1 231 ASN n 
1 232 LEU n 
1 233 THR n 
1 234 LEU n 
1 235 TRP n 
1 236 THR n 
2 1   ARG n 
2 2   ILE n 
2 3   ARG n 
2 4   SER n 
2 5   THR n 
2 6   SEP n 
2 7   THR n 
2 8   PRO n 
2 9   ASN n 
2 10  VAL n 
2 11  HIS n 
2 12  MET 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                   236 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SFN, HME1' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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       12 
_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 
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 
CL  non-polymer         . 'CHLORIDE ION'                                                                         ?               
'Cl -1'                35.453  
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 
MG  non-polymer         . 'MAGNESIUM ION'                                                                        ?               
'Mg 2'                 24.305  
PHE 'L-peptide linking' y PHENYLALANINE                                                                          ?               
'C9 H11 N O2'          165.189 
PRO 'L-peptide linking' y PROLINE                                                                                ?               
'C5 H9 N O2'           115.130 
SEP 'L-peptide linking' n PHOSPHOSERINE                                                                          PHOSPHONOSERINE 
'C3 H8 N O6 P'         185.072 
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 
WQT non-polymer         . '2-chloranyl-1-[8-(4-iodophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]ethanone' ?               
'C14 H16 Cl I N2 O4 S' 470.710 
# 
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   -4  -4  GLY GLY A . n 
A 1 2   ALA 2   -3  -3  ALA ALA A . n 
A 1 3   MET 3   -2  -2  MET MET A . n 
A 1 4   GLY 4   -1  -1  GLY GLY A . n 
A 1 5   SER 5   0   0   SER SER A . n 
A 1 6   MET 6   1   1   MET MET A . n 
A 1 7   GLU 7   2   2   GLU GLU A . n 
A 1 8   ARG 8   3   3   ARG ARG A . n 
A 1 9   ALA 9   4   4   ALA ALA A . n 
A 1 10  SER 10  5   5   SER SER A . n 
A 1 11  LEU 11  6   6   LEU LEU A . n 
A 1 12  ILE 12  7   7   ILE ILE A . n 
A 1 13  GLN 13  8   8   GLN GLN A . n 
A 1 14  LYS 14  9   9   LYS LYS A . n 
A 1 15  ALA 15  10  10  ALA ALA A . n 
A 1 16  LYS 16  11  11  LYS LYS A . n 
A 1 17  LEU 17  12  12  LEU LEU A . n 
A 1 18  ALA 18  13  13  ALA ALA A . n 
A 1 19  GLU 19  14  14  GLU GLU A . n 
A 1 20  GLN 20  15  15  GLN GLN A . n 
A 1 21  ALA 21  16  16  ALA ALA A . n 
A 1 22  GLU 22  17  17  GLU GLU A . n 
A 1 23  ARG 23  18  18  ARG ARG A . n 
A 1 24  TYR 24  19  19  TYR TYR A . n 
A 1 25  GLU 25  20  20  GLU GLU A . n 
A 1 26  ASP 26  21  21  ASP ASP A . n 
A 1 27  MET 27  22  22  MET MET A . n 
A 1 28  ALA 28  23  23  ALA ALA A . n 
A 1 29  ALA 29  24  24  ALA ALA A . n 
A 1 30  PHE 30  25  25  PHE PHE A . n 
A 1 31  MET 31  26  26  MET MET A . n 
A 1 32  LYS 32  27  27  LYS LYS A . n 
A 1 33  GLY 33  28  28  GLY GLY A . n 
A 1 34  ALA 34  29  29  ALA ALA A . n 
A 1 35  VAL 35  30  30  VAL VAL A . n 
A 1 36  GLU 36  31  31  GLU GLU A . n 
A 1 37  LYS 37  32  32  LYS LYS A . n 
A 1 38  GLY 38  33  33  GLY GLY A . n 
A 1 39  GLU 39  34  34  GLU GLU A . n 
A 1 40  GLU 40  35  35  GLU GLU A . n 
A 1 41  LEU 41  36  36  LEU LEU A . n 
A 1 42  SER 42  37  37  SER SER A . n 
A 1 43  CYS 43  38  38  CYS CSO A . n 
A 1 44  GLU 44  39  39  GLU GLU A . n 
A 1 45  GLU 45  40  40  GLU GLU A . n 
A 1 46  ARG 46  41  41  ARG ARG A . n 
A 1 47  ASN 47  42  42  ASN ASN A . n 
A 1 48  LEU 48  43  43  LEU LEU A . n 
A 1 49  LEU 49  44  44  LEU LEU A . n 
A 1 50  SER 50  45  45  SER SER A . n 
A 1 51  VAL 51  46  46  VAL VAL A . n 
A 1 52  ALA 52  47  47  ALA ALA A . n 
A 1 53  TYR 53  48  48  TYR TYR A . n 
A 1 54  LYS 54  49  49  LYS LYS A . n 
A 1 55  ASN 55  50  50  ASN ASN A . n 
A 1 56  VAL 56  51  51  VAL VAL A . n 
A 1 57  VAL 57  52  52  VAL VAL A . n 
A 1 58  GLY 58  53  53  GLY GLY A . n 
A 1 59  GLY 59  54  54  GLY GLY A . n 
A 1 60  GLN 60  55  55  GLN GLN A . n 
A 1 61  ARG 61  56  56  ARG ARG A . n 
A 1 62  ALA 62  57  57  ALA ALA A . n 
A 1 63  ALA 63  58  58  ALA ALA A . n 
A 1 64  TRP 64  59  59  TRP TRP A . n 
A 1 65  ARG 65  60  60  ARG ARG A . n 
A 1 66  VAL 66  61  61  VAL VAL A . n 
A 1 67  LEU 67  62  62  LEU LEU A . n 
A 1 68  SER 68  63  63  SER SER A . n 
A 1 69  SER 69  64  64  SER SER A . n 
A 1 70  ILE 70  65  65  ILE ILE A . n 
A 1 71  GLU 71  66  66  GLU GLU A . n 
A 1 72  GLN 72  67  67  GLN GLN A . n 
A 1 73  LYS 73  68  68  LYS LYS A . n 
A 1 74  SER 74  69  69  SER SER A . n 
A 1 75  ASN 75  70  70  ASN ASN A . n 
A 1 76  GLU 76  71  71  GLU GLU A . n 
A 1 77  GLU 77  72  ?   ?   ?   A . n 
A 1 78  GLY 78  73  ?   ?   ?   A . n 
A 1 79  SER 79  74  ?   ?   ?   A . n 
A 1 80  GLU 80  75  ?   ?   ?   A . n 
A 1 81  GLU 81  76  ?   ?   ?   A . n 
A 1 82  LYS 82  77  77  LYS LYS A . n 
A 1 83  GLY 83  78  78  GLY GLY A . n 
A 1 84  PRO 84  79  79  PRO PRO A . n 
A 1 85  GLU 85  80  80  GLU GLU A . n 
A 1 86  VAL 86  81  81  VAL VAL A . n 
A 1 87  ARG 87  82  82  ARG ARG A . n 
A 1 88  GLU 88  83  83  GLU GLU A . n 
A 1 89  TYR 89  84  84  TYR TYR A . n 
A 1 90  ARG 90  85  85  ARG ARG A . n 
A 1 91  GLU 91  86  86  GLU GLU A . n 
A 1 92  LYS 92  87  87  LYS LYS A . n 
A 1 93  VAL 93  88  88  VAL VAL A . n 
A 1 94  GLU 94  89  89  GLU GLU A . n 
A 1 95  THR 95  90  90  THR THR A . n 
A 1 96  GLU 96  91  91  GLU GLU A . n 
A 1 97  LEU 97  92  92  LEU LEU A . n 
A 1 98  GLN 98  93  93  GLN GLN A . n 
A 1 99  GLY 99  94  94  GLY GLY A . n 
A 1 100 VAL 100 95  95  VAL VAL A . n 
A 1 101 CYS 101 96  96  CYS CYS A . n 
A 1 102 ASP 102 97  97  ASP ASP A . n 
A 1 103 THR 103 98  98  THR THR A . n 
A 1 104 VAL 104 99  99  VAL VAL A . n 
A 1 105 LEU 105 100 100 LEU LEU A . n 
A 1 106 GLY 106 101 101 GLY GLY A . n 
A 1 107 LEU 107 102 102 LEU LEU A . n 
A 1 108 LEU 108 103 103 LEU LEU A . n 
A 1 109 ASP 109 104 104 ASP ASP A . n 
A 1 110 SER 110 105 105 SER SER A . n 
A 1 111 HIS 111 106 106 HIS HIS A . n 
A 1 112 LEU 112 107 107 LEU LEU A . n 
A 1 113 ILE 113 108 108 ILE ILE A . n 
A 1 114 LYS 114 109 109 LYS LYS A . n 
A 1 115 GLU 115 110 110 GLU GLU A . n 
A 1 116 ALA 116 111 111 ALA ALA A . n 
A 1 117 GLY 117 112 112 GLY GLY A . n 
A 1 118 ASP 118 113 113 ASP ASP A . n 
A 1 119 ALA 119 114 114 ALA ALA A . n 
A 1 120 GLU 120 115 115 GLU GLU A . n 
A 1 121 SER 121 116 116 SER SER A . n 
A 1 122 ARG 122 117 117 ARG ARG A . n 
A 1 123 VAL 123 118 118 VAL VAL A . n 
A 1 124 PHE 124 119 119 PHE PHE A . n 
A 1 125 TYR 125 120 120 TYR TYR A . n 
A 1 126 LEU 126 121 121 LEU LEU A . n 
A 1 127 LYS 127 122 122 LYS LYS A . n 
A 1 128 MET 128 123 123 MET MET A . n 
A 1 129 LYS 129 124 124 LYS LYS A . n 
A 1 130 GLY 130 125 125 GLY GLY A . n 
A 1 131 ASP 131 126 126 ASP ASP A . n 
A 1 132 TYR 132 127 127 TYR TYR A . n 
A 1 133 TYR 133 128 128 TYR TYR A . n 
A 1 134 ARG 134 129 129 ARG ARG A . n 
A 1 135 TYR 135 130 130 TYR TYR A . n 
A 1 136 LEU 136 131 131 LEU LEU A . n 
A 1 137 ALA 137 132 132 ALA ALA A . n 
A 1 138 GLU 138 133 133 GLU GLU A . n 
A 1 139 VAL 139 134 134 VAL VAL A . n 
A 1 140 ALA 140 135 135 ALA ALA A . n 
A 1 141 THR 141 136 136 THR THR A . n 
A 1 142 GLY 142 137 137 GLY GLY A . n 
A 1 143 ASP 143 138 138 ASP ASP A . n 
A 1 144 ASP 144 139 139 ASP ASP A . n 
A 1 145 LYS 145 140 140 LYS LYS A . n 
A 1 146 LYS 146 141 141 LYS LYS A . n 
A 1 147 ARG 147 142 142 ARG ARG A . n 
A 1 148 ILE 148 143 143 ILE ILE A . n 
A 1 149 ILE 149 144 144 ILE ILE A . n 
A 1 150 ASP 150 145 145 ASP ASP A . n 
A 1 151 SER 151 146 146 SER SER A . n 
A 1 152 ALA 152 147 147 ALA ALA A . n 
A 1 153 ARG 153 148 148 ARG ARG A . n 
A 1 154 SER 154 149 149 SER SER A . n 
A 1 155 ALA 155 150 150 ALA ALA A . n 
A 1 156 TYR 156 151 151 TYR TYR A . n 
A 1 157 GLN 157 152 152 GLN GLN A . n 
A 1 158 GLU 158 153 153 GLU GLU A . n 
A 1 159 ALA 159 154 154 ALA ALA A . n 
A 1 160 MET 160 155 155 MET MET A . n 
A 1 161 ASP 161 156 156 ASP ASP A . n 
A 1 162 ILE 162 157 157 ILE ILE A . n 
A 1 163 SER 163 158 158 SER SER A . n 
A 1 164 LYS 164 159 159 LYS LYS A . n 
A 1 165 LYS 165 160 160 LYS LYS A . n 
A 1 166 GLU 166 161 161 GLU GLU A . n 
A 1 167 MET 167 162 162 MET MET A . n 
A 1 168 PRO 168 163 163 PRO PRO A . n 
A 1 169 PRO 169 164 164 PRO PRO A . n 
A 1 170 THR 170 165 165 THR THR A . n 
A 1 171 ASN 171 166 166 ASN ASN A . n 
A 1 172 PRO 172 167 167 PRO PRO A . n 
A 1 173 ILE 173 168 168 ILE ILE A . n 
A 1 174 ARG 174 169 169 ARG ARG A . n 
A 1 175 LEU 175 170 170 LEU LEU A . n 
A 1 176 GLY 176 171 171 GLY GLY A . n 
A 1 177 LEU 177 172 172 LEU LEU A . n 
A 1 178 ALA 178 173 173 ALA ALA A . n 
A 1 179 LEU 179 174 174 LEU LEU A . n 
A 1 180 ASN 180 175 175 ASN ASN A . n 
A 1 181 PHE 181 176 176 PHE PHE A . n 
A 1 182 SER 182 177 177 SER SER A . n 
A 1 183 VAL 183 178 178 VAL VAL A . n 
A 1 184 PHE 184 179 179 PHE PHE A . n 
A 1 185 HIS 185 180 180 HIS HIS A . n 
A 1 186 TYR 186 181 181 TYR TYR A . n 
A 1 187 GLU 187 182 182 GLU GLU A . n 
A 1 188 ILE 188 183 183 ILE ILE A . n 
A 1 189 ALA 189 184 184 ALA ALA A . n 
A 1 190 ASN 190 185 185 ASN ASN A . n 
A 1 191 SER 191 186 186 SER SER A . n 
A 1 192 PRO 192 187 187 PRO PRO A . n 
A 1 193 GLU 193 188 188 GLU GLU A . n 
A 1 194 GLU 194 189 189 GLU GLU A . n 
A 1 195 ALA 195 190 190 ALA ALA A . n 
A 1 196 ILE 196 191 191 ILE ILE A . n 
A 1 197 SER 197 192 192 SER SER A . n 
A 1 198 LEU 198 193 193 LEU LEU A . n 
A 1 199 ALA 199 194 194 ALA ALA A . n 
A 1 200 LYS 200 195 195 LYS LYS A . n 
A 1 201 THR 201 196 196 THR THR A . n 
A 1 202 THR 202 197 197 THR THR A . n 
A 1 203 PHE 203 198 198 PHE PHE A . n 
A 1 204 ASP 204 199 199 ASP ASP A . n 
A 1 205 GLU 205 200 200 GLU GLU A . n 
A 1 206 ALA 206 201 201 ALA ALA A . n 
A 1 207 MET 207 202 202 MET MET A . n 
A 1 208 ALA 208 203 203 ALA ALA A . n 
A 1 209 ASP 209 204 204 ASP ASP A . n 
A 1 210 LEU 210 205 205 LEU LEU A . n 
A 1 211 HIS 211 206 206 HIS HIS A . n 
A 1 212 THR 212 207 207 THR THR A . n 
A 1 213 LEU 213 208 208 LEU LEU A . n 
A 1 214 SER 214 209 209 SER SER A . n 
A 1 215 GLU 215 210 210 GLU GLU A . n 
A 1 216 ASP 216 211 211 ASP ASP A . n 
A 1 217 SER 217 212 212 SER SER A . n 
A 1 218 TYR 218 213 213 TYR TYR A . n 
A 1 219 LYS 219 214 214 LYS LYS A . n 
A 1 220 ASP 220 215 215 ASP ASP A . n 
A 1 221 SER 221 216 216 SER SER A . n 
A 1 222 THR 222 217 217 THR THR A . n 
A 1 223 LEU 223 218 218 LEU LEU A . n 
A 1 224 ILE 224 219 219 ILE ILE A . n 
A 1 225 MET 225 220 220 MET MET A . n 
A 1 226 GLN 226 221 221 GLN GLN A . n 
A 1 227 LEU 227 222 222 LEU LEU A . n 
A 1 228 LEU 228 223 223 LEU LEU A . n 
A 1 229 ARG 229 224 224 ARG ARG A . n 
A 1 230 ASP 230 225 225 ASP ASP A . n 
A 1 231 ASN 231 226 226 ASN ASN A . n 
A 1 232 LEU 232 227 227 LEU LEU A . n 
A 1 233 THR 233 228 228 THR THR A . n 
A 1 234 LEU 234 229 229 LEU LEU A . n 
A 1 235 TRP 235 230 230 TRP TRP A . n 
A 1 236 THR 236 231 231 THR THR A . n 
B 2 1   ARG 1   254 ?   ?   ?   P . n 
B 2 2   ILE 2   255 255 ILE ILE P . n 
B 2 3   ARG 3   256 256 ARG ARG P . n 
B 2 4   SER 4   257 257 SER SER P . n 
B 2 5   THR 5   258 258 THR THR P . n 
B 2 6   SEP 6   259 259 SEP SEP P . n 
B 2 7   THR 7   260 260 THR THR P . n 
B 2 8   PRO 8   261 261 PRO PRO P . n 
B 2 9   ASN 9   262 262 ASN ASN P . n 
B 2 10  VAL 10  263 263 VAL VAL P . n 
B 2 11  HIS 11  264 264 HIS HIS P . n 
B 2 12  MET 12  265 265 MET MET P . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WQT 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WQT 
_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 CL  1   301 263 CL  CL  A . 
D 4 MG  1   302 264 MG  MG  A . 
E 4 MG  1   303 265 MG  MG  A . 
F 4 MG  1   304 266 MG  MG  A . 
G 5 WQT 1   305 267 WQT 379 A . 
H 6 HOH 1   401 97  HOH HOH A . 
H 6 HOH 2   402 122 HOH HOH A . 
H 6 HOH 3   403 154 HOH HOH A . 
H 6 HOH 4   404 103 HOH HOH A . 
H 6 HOH 5   405 68  HOH HOH A . 
H 6 HOH 6   406 106 HOH HOH A . 
H 6 HOH 7   407 50  HOH HOH A . 
H 6 HOH 8   408 21  HOH HOH A . 
H 6 HOH 9   409 167 HOH HOH A . 
H 6 HOH 10  410 133 HOH HOH A . 
H 6 HOH 11  411 126 HOH HOH A . 
H 6 HOH 12  412 110 HOH HOH A . 
H 6 HOH 13  413 46  HOH HOH A . 
H 6 HOH 14  414 104 HOH HOH A . 
H 6 HOH 15  415 74  HOH HOH A . 
H 6 HOH 16  416 55  HOH HOH A . 
H 6 HOH 17  417 59  HOH HOH A . 
H 6 HOH 18  418 10  HOH HOH A . 
H 6 HOH 19  419 100 HOH HOH A . 
H 6 HOH 20  420 152 HOH HOH A . 
H 6 HOH 21  421 120 HOH HOH A . 
H 6 HOH 22  422 136 HOH HOH A . 
H 6 HOH 23  423 113 HOH HOH A . 
H 6 HOH 24  424 35  HOH HOH A . 
H 6 HOH 25  425 72  HOH HOH A . 
H 6 HOH 26  426 124 HOH HOH A . 
H 6 HOH 27  427 101 HOH HOH A . 
H 6 HOH 28  428 28  HOH HOH A . 
H 6 HOH 29  429 66  HOH HOH A . 
H 6 HOH 30  430 32  HOH HOH A . 
H 6 HOH 31  431 85  HOH HOH A . 
H 6 HOH 32  432 40  HOH HOH A . 
H 6 HOH 33  433 38  HOH HOH A . 
H 6 HOH 34  434 73  HOH HOH A . 
H 6 HOH 35  435 30  HOH HOH A . 
H 6 HOH 36  436 33  HOH HOH A . 
H 6 HOH 37  437 37  HOH HOH A . 
H 6 HOH 38  438 156 HOH HOH A . 
H 6 HOH 39  439 147 HOH HOH A . 
H 6 HOH 40  440 39  HOH HOH A . 
H 6 HOH 41  441 26  HOH HOH A . 
H 6 HOH 42  442 132 HOH HOH A . 
H 6 HOH 43  443 111 HOH HOH A . 
H 6 HOH 44  444 108 HOH HOH A . 
H 6 HOH 45  445 12  HOH HOH A . 
H 6 HOH 46  446 19  HOH HOH A . 
H 6 HOH 47  447 49  HOH HOH A . 
H 6 HOH 48  448 84  HOH HOH A . 
H 6 HOH 49  449 53  HOH HOH A . 
H 6 HOH 50  450 64  HOH HOH A . 
H 6 HOH 51  451 48  HOH HOH A . 
H 6 HOH 52  452 91  HOH HOH A . 
H 6 HOH 53  453 127 HOH HOH A . 
H 6 HOH 54  454 71  HOH HOH A . 
H 6 HOH 55  455 151 HOH HOH A . 
H 6 HOH 56  456 18  HOH HOH A . 
H 6 HOH 57  457 27  HOH HOH A . 
H 6 HOH 58  458 168 HOH HOH A . 
H 6 HOH 59  459 131 HOH HOH A . 
H 6 HOH 60  460 13  HOH HOH A . 
H 6 HOH 61  461 107 HOH HOH A . 
H 6 HOH 62  462 143 HOH HOH A . 
H 6 HOH 63  463 22  HOH HOH A . 
H 6 HOH 64  464 17  HOH HOH A . 
H 6 HOH 65  465 14  HOH HOH A . 
H 6 HOH 66  466 29  HOH HOH A . 
H 6 HOH 67  467 1   HOH HOH A . 
H 6 HOH 68  468 44  HOH HOH A . 
H 6 HOH 69  469 25  HOH HOH A . 
H 6 HOH 70  470 45  HOH HOH A . 
H 6 HOH 71  471 65  HOH HOH A . 
H 6 HOH 72  472 11  HOH HOH A . 
H 6 HOH 73  473 109 HOH HOH A . 
H 6 HOH 74  474 7   HOH HOH A . 
H 6 HOH 75  475 123 HOH HOH A . 
H 6 HOH 76  476 24  HOH HOH A . 
H 6 HOH 77  477 112 HOH HOH A . 
H 6 HOH 78  478 96  HOH HOH A . 
H 6 HOH 79  479 52  HOH HOH A . 
H 6 HOH 80  480 160 HOH HOH A . 
H 6 HOH 81  481 15  HOH HOH A . 
H 6 HOH 82  482 114 HOH HOH A . 
H 6 HOH 83  483 54  HOH HOH A . 
H 6 HOH 84  484 57  HOH HOH A . 
H 6 HOH 85  485 164 HOH HOH A . 
H 6 HOH 86  486 36  HOH HOH A . 
H 6 HOH 87  487 16  HOH HOH A . 
H 6 HOH 88  488 47  HOH HOH A . 
H 6 HOH 89  489 121 HOH HOH A . 
H 6 HOH 90  490 34  HOH HOH A . 
H 6 HOH 91  491 155 HOH HOH A . 
H 6 HOH 92  492 61  HOH HOH A . 
H 6 HOH 93  493 99  HOH HOH A . 
H 6 HOH 94  494 78  HOH HOH A . 
H 6 HOH 95  495 41  HOH HOH A . 
H 6 HOH 96  496 162 HOH HOH A . 
H 6 HOH 97  497 20  HOH HOH A . 
H 6 HOH 98  498 4   HOH HOH A . 
H 6 HOH 99  499 81  HOH HOH A . 
H 6 HOH 100 500 6   HOH HOH A . 
H 6 HOH 101 501 171 HOH HOH A . 
H 6 HOH 102 502 79  HOH HOH A . 
H 6 HOH 103 503 9   HOH HOH A . 
H 6 HOH 104 504 77  HOH HOH A . 
H 6 HOH 105 505 117 HOH HOH A . 
H 6 HOH 106 506 43  HOH HOH A . 
H 6 HOH 107 507 129 HOH HOH A . 
H 6 HOH 108 508 3   HOH HOH A . 
H 6 HOH 109 509 75  HOH HOH A . 
H 6 HOH 110 510 67  HOH HOH A . 
H 6 HOH 111 511 172 HOH HOH A . 
H 6 HOH 112 512 63  HOH HOH A . 
H 6 HOH 113 513 118 HOH HOH A . 
H 6 HOH 114 514 95  HOH HOH A . 
H 6 HOH 115 515 98  HOH HOH A . 
H 6 HOH 116 516 62  HOH HOH A . 
H 6 HOH 117 517 137 HOH HOH A . 
H 6 HOH 118 518 138 HOH HOH A . 
H 6 HOH 119 519 60  HOH HOH A . 
H 6 HOH 120 520 58  HOH HOH A . 
H 6 HOH 121 521 86  HOH HOH A . 
H 6 HOH 122 522 116 HOH HOH A . 
H 6 HOH 123 523 157 HOH HOH A . 
H 6 HOH 124 524 56  HOH HOH A . 
H 6 HOH 125 525 130 HOH HOH A . 
H 6 HOH 126 526 161 HOH HOH A . 
H 6 HOH 127 527 93  HOH HOH A . 
H 6 HOH 128 528 141 HOH HOH A . 
H 6 HOH 129 529 76  HOH HOH A . 
H 6 HOH 130 530 83  HOH HOH A . 
H 6 HOH 131 531 69  HOH HOH A . 
H 6 HOH 132 532 169 HOH HOH A . 
H 6 HOH 133 533 173 HOH HOH A . 
H 6 HOH 134 534 23  HOH HOH A . 
H 6 HOH 135 535 153 HOH HOH A . 
H 6 HOH 136 536 150 HOH HOH A . 
H 6 HOH 137 537 148 HOH HOH A . 
H 6 HOH 138 538 115 HOH HOH A . 
H 6 HOH 139 539 125 HOH HOH A . 
H 6 HOH 140 540 90  HOH HOH A . 
H 6 HOH 141 541 163 HOH HOH A . 
H 6 HOH 142 542 128 HOH HOH A . 
I 6 HOH 1   301 31  HOH HOH P . 
I 6 HOH 2   302 82  HOH HOH P . 
I 6 HOH 3   303 42  HOH HOH P . 
I 6 HOH 4   304 80  HOH HOH P . 
I 6 HOH 5   305 51  HOH HOH P . 
I 6 HOH 6   306 89  HOH HOH P . 
I 6 HOH 7   307 88  HOH HOH P . 
I 6 HOH 8   308 8   HOH HOH P . 
I 6 HOH 9   309 144 HOH HOH P . 
I 6 HOH 10  310 94  HOH HOH P . 
I 6 HOH 11  311 135 HOH HOH P . 
I 6 HOH 12  312 105 HOH HOH P . 
I 6 HOH 13  313 119 HOH HOH P . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 68  ? CG  ? A LYS 73  CG  
2  1 Y 1 A LYS 68  ? CD  ? A LYS 73  CD  
3  1 Y 1 A LYS 68  ? CE  ? A LYS 73  CE  
4  1 Y 1 A LYS 68  ? NZ  ? A LYS 73  NZ  
5  1 Y 1 A LYS 77  ? CG  ? A LYS 82  CG  
6  1 Y 1 A LYS 77  ? CD  ? A LYS 82  CD  
7  1 Y 1 A LYS 77  ? CE  ? A LYS 82  CE  
8  1 Y 1 A LYS 77  ? NZ  ? A LYS 82  NZ  
9  1 Y 1 A GLU 110 ? CG  ? A GLU 115 CG  
10 1 Y 1 A GLU 110 ? CD  ? A GLU 115 CD  
11 1 Y 1 A GLU 110 ? OE1 ? A GLU 115 OE1 
12 1 Y 1 A GLU 110 ? OE2 ? A GLU 115 OE2 
13 1 Y 1 A ASN 185 ? CG  ? A ASN 190 CG  
14 1 Y 1 A ASN 185 ? OD1 ? A ASN 190 OD1 
15 1 Y 1 A ASN 185 ? ND2 ? A ASN 190 ND2 
16 1 Y 1 P ILE 255 ? CG1 ? B ILE 2   CG1 
17 1 Y 1 P ILE 255 ? CG2 ? B ILE 2   CG2 
18 1 Y 1 P ILE 255 ? CD1 ? B ILE 2   CD1 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PDB-REDO ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8VSN 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.576 
_cell.length_a_esd                 ? 
_cell.length_b                     150.225 
_cell.length_b_esd                 ? 
_cell.length_c                     76.816 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8VSN 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                21 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 2' 
_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                   8VSN 
_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             3.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          62.17 
_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    'PEG4000, HEPES, CaCl2, glycerol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277.15 
# 
_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 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-12 
_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   0.967697 
_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                        'ESRF BEAMLINE MASSIF-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.967697 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-3 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8VSN 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.91 
_reflns.d_resolution_low                               57.76 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     58185 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.91 
_reflns_shell.d_res_low                                     1.95 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1897 
_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                                  0.631 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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]                            1.48 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.46 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.02 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               40.795 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_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                                 8VSN 
_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                            1.91 
_refine.ls_d_res_low                             57.76 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     55234 
_refine.ls_number_reflns_R_free                  2950 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.84 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.24141 
_refine.ls_R_factor_R_free                       0.27206 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.23981 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.077 
_refine.pdbx_overall_ESU_R_Free                  0.081 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             4.426 
_refine.overall_SU_ML                            0.129 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.91 
_refine_hist.d_res_low                        57.76 
_refine_hist.number_atoms_solvent             155 
_refine_hist.number_atoms_total               2071 
_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        1890 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_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' ? 0.009  0.013  1948 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.015  1835 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.573  1.649  2628 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.458  1.585  4234 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.249  5.000  241  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 32.855 22.404 104  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.765 15.000 353  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 21.371 15.000 14   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.080  0.200  255  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  2177 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  423  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.708  4.148  967  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.697  4.145  966  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.026  6.201  1204 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.025  6.206  1205 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.023  4.521  981  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.025  4.522  982  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.003  6.631  1422 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.943  78.535 8415 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 8.892  78.468 8291 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.91 
_refine_ls_shell.d_res_low                        57.76 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             218 
_refine_ls_shell.number_reflns_R_work             3988 
_refine_ls_shell.percent_reflns_obs               99.01 
_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                  0.616 
_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.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                  0.614 
# 
_struct.entry_id                     8VSN 
_struct.title                        'Ternary structure of 14-3-3 sigma, ARAF phosphopeptide (pS214) and compound 79 (1124379)' 
_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        8VSN 
_struct_keywords.text            'stabilizer, protein-protein interactions, PEPTIDE BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'PEPTIDE BINDING PROTEIN' 
# 
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 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
# 
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 1433S_HUMAN P31947 ? 1 
;MERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPE
VREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKK
EMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
1   
2 UNP ARAF_HUMAN  P10398 ? 2 RIRSTSTPNVHM 209 
# 
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 8VSN A 6 ? 236 ? P31947 1   ? 231 ? 1   231 
2 2 8VSN P 1 ? 12  ? P10398 209 ? 220 ? 254 265 
# 
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 8VSN GLY A 1 ? UNP P31947 ? ? 'expression tag' -4 1 
1 8VSN ALA A 2 ? UNP P31947 ? ? 'expression tag' -3 2 
1 8VSN MET A 3 ? UNP P31947 ? ? 'expression tag' -2 3 
1 8VSN GLY A 4 ? UNP P31947 ? ? 'expression tag' -1 4 
1 8VSN SER A 5 ? UNP P31947 ? ? 'expression tag' 0  5 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 6220  ? 
1 MORE         -83   ? 
1 'SSA (A^2)'  22300 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 3_656 -x+1,y,-z+1 -1.0000000000 0.0000000000 0.0000000000 62.5760000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 76.8160000000 
# 
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 GLU A 7   ? ALA A 21  ? GLU A 2   ALA A 16  1 ? 15 
HELX_P HELX_P2  AA2 ARG A 23  ? LYS A 37  ? ARG A 18  LYS A 32  1 ? 15 
HELX_P HELX_P3  AA3 SER A 42  ? ASN A 75  ? SER A 37  ASN A 70  1 ? 34 
HELX_P HELX_P4  AA4 PRO A 84  ? HIS A 111 ? PRO A 79  HIS A 106 1 ? 28 
HELX_P HELX_P5  AA5 ASP A 118 ? ALA A 140 ? ASP A 113 ALA A 135 1 ? 23 
HELX_P HELX_P6  AA6 GLY A 142 ? MET A 167 ? GLY A 137 MET A 162 1 ? 26 
HELX_P HELX_P7  AA7 ASN A 171 ? ILE A 188 ? ASN A 166 ILE A 183 1 ? 18 
HELX_P HELX_P8  AA8 SER A 191 ? ASP A 209 ? SER A 186 ASP A 204 1 ? 19 
HELX_P HELX_P9  AA9 LEU A 210 ? LEU A 213 ? LEU A 205 LEU A 208 5 ? 4  
HELX_P HELX_P10 AB1 SER A 217 ? TRP A 235 ? SER A 212 TRP A 230 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one  ? A CYS 43  SG  ? ? ? 1_555 G WQT . C2 ? ? A CYS 38  A WQT 305 1_555 ? ? ? ? ? ? ? 1.693 ? ? 
covale2 covale both ? B THR 5   C   ? ? ? 1_555 B SEP 6 N  ? ? P THR 258 P SEP 259 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale3 covale both ? B SEP 6   C   ? ? ? 1_555 B THR 7 N  ? ? P SEP 259 P THR 260 1_555 ? ? ? ? ? ? ? 1.342 ? ? 
metalc1 metalc ?    ? A GLU 94  OE2 ? ? ? 1_555 D MG  . MG ? ? A GLU 89  A MG  302 1_555 ? ? ? ? ? ? ? 2.513 ? ? 
metalc2 metalc ?    ? A GLU 193 OE1 ? ? ? 1_555 F MG  . MG ? ? A GLU 188 A MG  304 1_555 ? ? ? ? ? ? ? 2.882 ? ? 
metalc3 metalc ?    ? E MG  .   MG  ? ? ? 1_555 H HOH . O  ? ? A MG  303 A HOH 466 6_655 ? ? ? ? ? ? ? 2.522 ? ? 
metalc4 metalc ?    ? E MG  .   MG  ? ? ? 1_555 H HOH . O  ? ? A MG  303 A HOH 490 1_555 ? ? ? ? ? ? ? 2.793 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   H 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   HOH 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    HOH 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     466 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        6_655 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   E 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    MG 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     303 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   H 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   HOH 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    HOH 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     490 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 100.4 
_pdbx_struct_conn_angle.value_esd             ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 SEP B 6 ? .   . .  . SEP P 259 ? 1_555 .   . .  . .     .  .  SER 1 SEP Phosphorylation 'Named protein modification'     
2 WQT G . ? CYS A 43 ? WQT A 305 ? 1_555 CYS A 38 ? 1_555 C2 SG CYS 1 WQT None            'Covalent chemical modification' 
# 
_pdbx_entry_details.entry_id                   8VSN 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 18  ? ? -103.24 78.22  
2 1 HIS A 106 ? ? -134.75 -43.07 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    B 
_pdbx_struct_mod_residue.label_comp_id    SEP 
_pdbx_struct_mod_residue.label_seq_id     6 
_pdbx_struct_mod_residue.auth_asym_id     P 
_pdbx_struct_mod_residue.auth_comp_id     SEP 
_pdbx_struct_mod_residue.auth_seq_id      259 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   SER 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     439 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   H 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 GLU 72  ? A GLU 77 
2 1 Y 1 A GLY 73  ? A GLY 78 
3 1 Y 1 A SER 74  ? A SER 79 
4 1 Y 1 A GLU 75  ? A GLU 80 
5 1 Y 1 A GLU 76  ? A GLU 81 
6 1 Y 1 P ARG 254 ? B ARG 1  
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
MG  MG   MG N N 251 
PHE N    N  N N 252 
PHE CA   C  N S 253 
PHE C    C  N N 254 
PHE O    O  N N 255 
PHE CB   C  N N 256 
PHE CG   C  Y N 257 
PHE CD1  C  Y N 258 
PHE CD2  C  Y N 259 
PHE CE1  C  Y N 260 
PHE CE2  C  Y N 261 
PHE CZ   C  Y N 262 
PHE OXT  O  N N 263 
PHE H    H  N N 264 
PHE H2   H  N N 265 
PHE HA   H  N N 266 
PHE HB2  H  N N 267 
PHE HB3  H  N N 268 
PHE HD1  H  N N 269 
PHE HD2  H  N N 270 
PHE HE1  H  N N 271 
PHE HE2  H  N N 272 
PHE HZ   H  N N 273 
PHE HXT  H  N N 274 
PRO N    N  N N 275 
PRO CA   C  N S 276 
PRO C    C  N N 277 
PRO O    O  N N 278 
PRO CB   C  N N 279 
PRO CG   C  N N 280 
PRO CD   C  N N 281 
PRO OXT  O  N N 282 
PRO H    H  N N 283 
PRO HA   H  N N 284 
PRO HB2  H  N N 285 
PRO HB3  H  N N 286 
PRO HG2  H  N N 287 
PRO HG3  H  N N 288 
PRO HD2  H  N N 289 
PRO HD3  H  N N 290 
PRO HXT  H  N N 291 
SEP N    N  N N 292 
SEP CA   C  N S 293 
SEP CB   C  N N 294 
SEP OG   O  N N 295 
SEP C    C  N N 296 
SEP O    O  N N 297 
SEP OXT  O  N N 298 
SEP P    P  N N 299 
SEP O1P  O  N N 300 
SEP O2P  O  N N 301 
SEP O3P  O  N N 302 
SEP H    H  N N 303 
SEP H2   H  N N 304 
SEP HA   H  N N 305 
SEP HB2  H  N N 306 
SEP HB3  H  N N 307 
SEP HXT  H  N N 308 
SEP HOP2 H  N N 309 
SEP HOP3 H  N N 310 
SER N    N  N N 311 
SER CA   C  N S 312 
SER C    C  N N 313 
SER O    O  N N 314 
SER CB   C  N N 315 
SER OG   O  N N 316 
SER OXT  O  N N 317 
SER H    H  N N 318 
SER H2   H  N N 319 
SER HA   H  N N 320 
SER HB2  H  N N 321 
SER HB3  H  N N 322 
SER HG   H  N N 323 
SER HXT  H  N N 324 
THR N    N  N N 325 
THR CA   C  N S 326 
THR C    C  N N 327 
THR O    O  N N 328 
THR CB   C  N R 329 
THR OG1  O  N N 330 
THR CG2  C  N N 331 
THR OXT  O  N N 332 
THR H    H  N N 333 
THR H2   H  N N 334 
THR HA   H  N N 335 
THR HB   H  N N 336 
THR HG1  H  N N 337 
THR HG21 H  N N 338 
THR HG22 H  N N 339 
THR HG23 H  N N 340 
THR HXT  H  N N 341 
TRP N    N  N N 342 
TRP CA   C  N S 343 
TRP C    C  N N 344 
TRP O    O  N N 345 
TRP CB   C  N N 346 
TRP CG   C  Y N 347 
TRP CD1  C  Y N 348 
TRP CD2  C  Y N 349 
TRP NE1  N  Y N 350 
TRP CE2  C  Y N 351 
TRP CE3  C  Y N 352 
TRP CZ2  C  Y N 353 
TRP CZ3  C  Y N 354 
TRP CH2  C  Y N 355 
TRP OXT  O  N N 356 
TRP H    H  N N 357 
TRP H2   H  N N 358 
TRP HA   H  N N 359 
TRP HB2  H  N N 360 
TRP HB3  H  N N 361 
TRP HD1  H  N N 362 
TRP HE1  H  N N 363 
TRP HE3  H  N N 364 
TRP HZ2  H  N N 365 
TRP HZ3  H  N N 366 
TRP HH2  H  N N 367 
TRP HXT  H  N N 368 
TYR N    N  N N 369 
TYR CA   C  N S 370 
TYR C    C  N N 371 
TYR O    O  N N 372 
TYR CB   C  N N 373 
TYR CG   C  Y N 374 
TYR CD1  C  Y N 375 
TYR CD2  C  Y N 376 
TYR CE1  C  Y N 377 
TYR CE2  C  Y N 378 
TYR CZ   C  Y N 379 
TYR OH   O  N N 380 
TYR OXT  O  N N 381 
TYR H    H  N N 382 
TYR H2   H  N N 383 
TYR HA   H  N N 384 
TYR HB2  H  N N 385 
TYR HB3  H  N N 386 
TYR HD1  H  N N 387 
TYR HD2  H  N N 388 
TYR HE1  H  N N 389 
TYR HE2  H  N N 390 
TYR HH   H  N N 391 
TYR HXT  H  N N 392 
VAL N    N  N N 393 
VAL CA   C  N S 394 
VAL C    C  N N 395 
VAL O    O  N N 396 
VAL CB   C  N N 397 
VAL CG1  C  N N 398 
VAL CG2  C  N N 399 
VAL OXT  O  N N 400 
VAL H    H  N N 401 
VAL H2   H  N N 402 
VAL HA   H  N N 403 
VAL HB   H  N N 404 
VAL HG11 H  N N 405 
VAL HG12 H  N N 406 
VAL HG13 H  N N 407 
VAL HG21 H  N N 408 
VAL HG22 H  N N 409 
VAL HG23 H  N N 410 
VAL HXT  H  N N 411 
WQT C4   C  N N 412 
WQT C14  C  N N 413 
WQT C5   C  N N 414 
WQT C6   C  N N 415 
WQT C11  C  Y N 416 
WQT C7   C  Y N 417 
WQT C8   C  Y N 418 
WQT C9   C  Y N 419 
WQT C10  C  Y N 420 
WQT C12  C  Y N 421 
WQT C13  C  N N 422 
WQT N1   N  N N 423 
WQT N2   N  N N 424 
WQT C3   C  N N 425 
WQT C1   C  N N 426 
WQT C2   C  N N 427 
WQT I1   I  N N 428 
WQT O1   O  N N 429 
WQT O2   O  N N 430 
WQT O3   O  N N 431 
WQT O4   O  N N 432 
WQT S1   S  N N 433 
WQT H1   H  N N 434 
WQT H2   H  N N 435 
WQT H3   H  N N 436 
WQT H4   H  N N 437 
WQT H5   H  N N 438 
WQT H6   H  N N 439 
WQT H7   H  N N 440 
WQT H8   H  N N 441 
WQT H9   H  N N 442 
WQT H10  H  N N 443 
WQT H11  H  N N 444 
WQT H12  H  N N 445 
WQT H13  H  N N 446 
WQT H14  H  N N 447 
WQT H15  H  N N 448 
WQT H16  H  N N 449 
WQT CL1  CL N N 450 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SEP N   CA   sing N N 277 
SEP N   H    sing N N 278 
SEP N   H2   sing N N 279 
SEP CA  CB   sing N N 280 
SEP CA  C    sing N N 281 
SEP CA  HA   sing N N 282 
SEP CB  OG   sing N N 283 
SEP CB  HB2  sing N N 284 
SEP CB  HB3  sing N N 285 
SEP OG  P    sing N N 286 
SEP C   O    doub N N 287 
SEP C   OXT  sing N N 288 
SEP OXT HXT  sing N N 289 
SEP P   O1P  doub N N 290 
SEP P   O2P  sing N N 291 
SEP P   O3P  sing N N 292 
SEP O2P HOP2 sing N N 293 
SEP O3P HOP3 sing N N 294 
SER N   CA   sing N N 295 
SER N   H    sing N N 296 
SER N   H2   sing N N 297 
SER CA  C    sing N N 298 
SER CA  CB   sing N N 299 
SER CA  HA   sing N N 300 
SER C   O    doub N N 301 
SER C   OXT  sing N N 302 
SER CB  OG   sing N N 303 
SER CB  HB2  sing N N 304 
SER CB  HB3  sing N N 305 
SER OG  HG   sing N N 306 
SER OXT HXT  sing N N 307 
THR N   CA   sing N N 308 
THR N   H    sing N N 309 
THR N   H2   sing N N 310 
THR CA  C    sing N N 311 
THR CA  CB   sing N N 312 
THR CA  HA   sing N N 313 
THR C   O    doub N N 314 
THR C   OXT  sing N N 315 
THR CB  OG1  sing N N 316 
THR CB  CG2  sing N N 317 
THR CB  HB   sing N N 318 
THR OG1 HG1  sing N N 319 
THR CG2 HG21 sing N N 320 
THR CG2 HG22 sing N N 321 
THR CG2 HG23 sing N N 322 
THR OXT HXT  sing N N 323 
TRP N   CA   sing N N 324 
TRP N   H    sing N N 325 
TRP N   H2   sing N N 326 
TRP CA  C    sing N N 327 
TRP CA  CB   sing N N 328 
TRP CA  HA   sing N N 329 
TRP C   O    doub N N 330 
TRP C   OXT  sing N N 331 
TRP CB  CG   sing N N 332 
TRP CB  HB2  sing N N 333 
TRP CB  HB3  sing N N 334 
TRP CG  CD1  doub Y N 335 
TRP CG  CD2  sing Y N 336 
TRP CD1 NE1  sing Y N 337 
TRP CD1 HD1  sing N N 338 
TRP CD2 CE2  doub Y N 339 
TRP CD2 CE3  sing Y N 340 
TRP NE1 CE2  sing Y N 341 
TRP NE1 HE1  sing N N 342 
TRP CE2 CZ2  sing Y N 343 
TRP CE3 CZ3  doub Y N 344 
TRP CE3 HE3  sing N N 345 
TRP CZ2 CH2  doub Y N 346 
TRP CZ2 HZ2  sing N N 347 
TRP CZ3 CH2  sing Y N 348 
TRP CZ3 HZ3  sing N N 349 
TRP CH2 HH2  sing N N 350 
TRP OXT HXT  sing N N 351 
TYR N   CA   sing N N 352 
TYR N   H    sing N N 353 
TYR N   H2   sing N N 354 
TYR CA  C    sing N N 355 
TYR CA  CB   sing N N 356 
TYR CA  HA   sing N N 357 
TYR C   O    doub N N 358 
TYR C   OXT  sing N N 359 
TYR CB  CG   sing N N 360 
TYR CB  HB2  sing N N 361 
TYR CB  HB3  sing N N 362 
TYR CG  CD1  doub Y N 363 
TYR CG  CD2  sing Y N 364 
TYR CD1 CE1  sing Y N 365 
TYR CD1 HD1  sing N N 366 
TYR CD2 CE2  doub Y N 367 
TYR CD2 HD2  sing N N 368 
TYR CE1 CZ   doub Y N 369 
TYR CE1 HE1  sing N N 370 
TYR CE2 CZ   sing Y N 371 
TYR CE2 HE2  sing N N 372 
TYR CZ  OH   sing N N 373 
TYR OH  HH   sing N N 374 
TYR OXT HXT  sing N N 375 
VAL N   CA   sing N N 376 
VAL N   H    sing N N 377 
VAL N   H2   sing N N 378 
VAL CA  C    sing N N 379 
VAL CA  CB   sing N N 380 
VAL CA  HA   sing N N 381 
VAL C   O    doub N N 382 
VAL C   OXT  sing N N 383 
VAL CB  CG1  sing N N 384 
VAL CB  CG2  sing N N 385 
VAL CB  HB   sing N N 386 
VAL CG1 HG11 sing N N 387 
VAL CG1 HG12 sing N N 388 
VAL CG1 HG13 sing N N 389 
VAL CG2 HG21 sing N N 390 
VAL CG2 HG22 sing N N 391 
VAL CG2 HG23 sing N N 392 
VAL OXT HXT  sing N N 393 
WQT O1  C1   doub N N 394 
WQT C2  C1   sing N N 395 
WQT C1  N1   sing N N 396 
WQT N1  C3   sing N N 397 
WQT N1  C5   sing N N 398 
WQT C3  C4   sing N N 399 
WQT C5  C4   sing N N 400 
WQT O3  S1   doub N N 401 
WQT C4  C6   sing N N 402 
WQT C4  O4   sing N N 403 
WQT C6  N2   sing N N 404 
WQT S1  N2   sing N N 405 
WQT S1  O2   doub N N 406 
WQT S1  C7   sing N N 407 
WQT N2  C13  sing N N 408 
WQT C12 C7   doub Y N 409 
WQT C12 C11  sing Y N 410 
WQT O4  C14  sing N N 411 
WQT C7  C8   sing Y N 412 
WQT C14 C13  sing N N 413 
WQT C11 C10  doub Y N 414 
WQT C8  C9   doub Y N 415 
WQT C10 C9   sing Y N 416 
WQT C10 I1   sing N N 417 
WQT C14 H1   sing N N 418 
WQT C14 H2   sing N N 419 
WQT C5  H3   sing N N 420 
WQT C5  H4   sing N N 421 
WQT C6  H5   sing N N 422 
WQT C6  H6   sing N N 423 
WQT C11 H7   sing N N 424 
WQT C8  H8   sing N N 425 
WQT C9  H9   sing N N 426 
WQT C12 H10  sing N N 427 
WQT C13 H11  sing N N 428 
WQT C13 H12  sing N N 429 
WQT C3  H13  sing N N 430 
WQT C3  H14  sing N N 431 
WQT C2  H15  sing N N 432 
WQT C2  H16  sing N N 433 
WQT C2  CL1  sing N N 434 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM147696 
_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   3IQJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8VSN 
_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]   0.015981 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006657 
_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]   0.013018 
_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  
CL 
I  
MG 
N  
O  
P  
S  
# 
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   . GLY A 1 1   ? 35.703 41.747 24.952 1.00 53.77  ? -4  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 1   ? 35.462 40.809 26.072 1.00 51.74  ? -4  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 1   ? 36.758 40.455 26.761 1.00 50.03  ? -4  GLY A C   1 
ATOM   4    O  O   . GLY A 1 1   ? 37.821 40.927 26.294 1.00 51.98  ? -4  GLY A O   1 
ATOM   5    N  N   . ALA A 1 2   ? 36.680 39.649 27.815 1.00 41.88  ? -3  ALA A N   1 
ATOM   6    C  CA  . ALA A 1 2   ? 37.807 39.301 28.709 1.00 44.25  ? -3  ALA A CA  1 
ATOM   7    C  C   . ALA A 1 2   ? 38.916 38.581 27.938 1.00 42.33  ? -3  ALA A C   1 
ATOM   8    O  O   . ALA A 1 2   ? 40.035 38.563 28.446 1.00 45.29  ? -3  ALA A O   1 
ATOM   9    C  CB  . ALA A 1 2   ? 37.317 38.464 29.860 1.00 47.66  ? -3  ALA A CB  1 
ATOM   10   N  N   . MET A 1 3   ? 38.618 37.960 26.788 1.00 37.76  ? -2  MET A N   1 
ATOM   11   C  CA  . MET A 1 3   ? 39.628 37.187 26.002 1.00 34.78  ? -2  MET A CA  1 
ATOM   12   C  C   . MET A 1 3   ? 40.180 38.010 24.826 1.00 34.48  ? -2  MET A C   1 
ATOM   13   O  O   . MET A 1 3   ? 40.962 37.480 24.022 1.00 34.48  ? -2  MET A O   1 
ATOM   14   C  CB  . MET A 1 3   ? 38.977 35.920 25.473 1.00 34.81  ? -2  MET A CB  1 
ATOM   15   C  CG  . MET A 1 3   ? 38.435 35.046 26.589 1.00 35.53  ? -2  MET A CG  1 
ATOM   16   S  SD  . MET A 1 3   ? 39.706 34.558 27.754 1.00 39.46  ? -2  MET A SD  1 
ATOM   17   C  CE  . MET A 1 3   ? 38.723 33.776 29.031 1.00 40.90  ? -2  MET A CE  1 
ATOM   18   N  N   . GLY A 1 4   ? 39.760 39.266 24.696 1.00 37.43  ? -1  GLY A N   1 
ATOM   19   C  CA  . GLY A 1 4   ? 40.109 40.168 23.576 1.00 34.81  ? -1  GLY A CA  1 
ATOM   20   C  C   . GLY A 1 4   ? 41.604 40.342 23.385 1.00 30.23  ? -1  GLY A C   1 
ATOM   21   O  O   . GLY A 1 4   ? 42.014 40.356 22.213 1.00 32.46  ? -1  GLY A O   1 
ATOM   22   N  N   . SER A 1 5   ? 42.407 40.339 24.456 1.00 29.00  ? 0   SER A N   1 
ATOM   23   C  CA  . SER A 1 5   ? 43.881 40.553 24.346 1.00 31.83  ? 0   SER A CA  1 
ATOM   24   C  C   . SER A 1 5   ? 44.639 39.244 24.051 1.00 34.87  ? 0   SER A C   1 
ATOM   25   O  O   . SER A 1 5   ? 45.860 39.287 23.827 1.00 34.36  ? 0   SER A O   1 
ATOM   26   C  CB  . SER A 1 5   ? 44.439 41.214 25.580 1.00 31.15  ? 0   SER A CB  1 
ATOM   27   O  OG  . SER A 1 5   ? 44.314 40.381 26.717 1.00 33.89  ? 0   SER A OG  1 
ATOM   28   N  N   . MET A 1 6   ? 43.982 38.095 24.112 1.00 33.81  ? 1   MET A N   1 
ATOM   29   C  CA  . MET A 1 6   ? 44.720 36.810 23.952 1.00 34.29  ? 1   MET A CA  1 
ATOM   30   C  C   . MET A 1 6   ? 44.682 36.343 22.491 1.00 29.37  ? 1   MET A C   1 
ATOM   31   O  O   . MET A 1 6   ? 43.701 36.496 21.787 1.00 29.31  ? 1   MET A O   1 
ATOM   32   C  CB  . MET A 1 6   ? 44.197 35.745 24.924 1.00 32.16  ? 1   MET A CB  1 
ATOM   33   C  CG  . MET A 1 6   ? 45.288 34.771 25.362 1.00 37.96  ? 1   MET A CG  1 
ATOM   34   S  SD  . MET A 1 6   ? 44.598 33.312 26.229 1.00 38.55  ? 1   MET A SD  1 
ATOM   35   C  CE  . MET A 1 6   ? 43.581 34.140 27.450 1.00 35.05  ? 1   MET A CE  1 
ATOM   36   N  N   . GLU A 1 7   ? 45.803 35.855 21.997 1.00 28.91  ? 2   GLU A N   1 
ATOM   37   C  CA  . GLU A 1 7   ? 45.895 35.286 20.642 1.00 31.61  ? 2   GLU A CA  1 
ATOM   38   C  C   . GLU A 1 7   ? 44.961 34.075 20.486 1.00 31.02  ? 2   GLU A C   1 
ATOM   39   O  O   . GLU A 1 7   ? 44.856 33.277 21.438 1.00 27.36  ? 2   GLU A O   1 
ATOM   40   C  CB  . GLU A 1 7   ? 47.321 34.874 20.359 1.00 37.45  ? 2   GLU A CB  1 
ATOM   41   C  CG  . GLU A 1 7   ? 48.053 36.007 19.647 1.00 45.52  ? 2   GLU A CG  1 
ATOM   42   C  CD  . GLU A 1 7   ? 49.528 35.748 19.526 1.00 48.08  ? 2   GLU A CD  1 
ATOM   43   O  OE1 . GLU A 1 7   ? 49.968 34.642 19.957 1.00 57.30  ? 2   GLU A OE1 1 
ATOM   44   O  OE2 . GLU A 1 7   ? 50.219 36.626 18.993 1.00 44.74  ? 2   GLU A OE2 1 
ATOM   45   N  N   . ARG A 1 8   ? 44.326 33.994 19.324 1.00 29.55  ? 3   ARG A N   1 
ATOM   46   C  CA  . ARG A 1 8   ? 43.446 32.858 18.949 1.00 33.91  ? 3   ARG A CA  1 
ATOM   47   C  C   . ARG A 1 8   ? 44.117 31.522 19.297 1.00 33.55  ? 3   ARG A C   1 
ATOM   48   O  O   . ARG A 1 8   ? 43.469 30.701 19.987 1.00 35.79  ? 3   ARG A O   1 
ATOM   49   C  CB  . ARG A 1 8   ? 43.094 32.912 17.466 1.00 34.86  ? 3   ARG A CB  1 
ATOM   50   C  CG  . ARG A 1 8   ? 41.883 32.040 17.129 1.00 34.63  ? 3   ARG A CG  1 
ATOM   51   C  CD  . ARG A 1 8   ? 41.684 31.941 15.638 1.00 37.05  ? 3   ARG A CD  1 
ATOM   52   N  NE  . ARG A 1 8   ? 40.513 31.133 15.328 1.00 34.79  ? 3   ARG A NE  1 
ATOM   53   C  CZ  . ARG A 1 8   ? 40.460 29.812 15.301 1.00 37.14  ? 3   ARG A CZ  1 
ATOM   54   N  NH1 . ARG A 1 8   ? 41.531 29.072 15.557 1.00 37.33  ? 3   ARG A NH1 1 
ATOM   55   N  NH2 . ARG A 1 8   ? 39.294 29.246 15.038 1.00 39.55  ? 3   ARG A NH2 1 
ATOM   56   N  N   . ALA A 1 9   ? 45.354 31.286 18.870 1.00 31.09  ? 4   ALA A N   1 
ATOM   57   C  CA  . ALA A 1 9   ? 46.015 29.975 19.059 1.00 34.12  ? 4   ALA A CA  1 
ATOM   58   C  C   . ALA A 1 9   ? 46.168 29.668 20.556 1.00 35.41  ? 4   ALA A C   1 
ATOM   59   O  O   . ALA A 1 9   ? 45.996 28.507 20.934 1.00 31.60  ? 4   ALA A O   1 
ATOM   60   C  CB  . ALA A 1 9   ? 47.332 29.904 18.330 1.00 34.83  ? 4   ALA A CB  1 
ATOM   61   N  N   . SER A 1 10  ? 46.431 30.669 21.401 1.00 33.58  ? 5   SER A N   1 
ATOM   62   C  CA  . SER A 1 10  ? 46.576 30.505 22.858 1.00 29.71  ? 5   SER A CA  1 
ATOM   63   C  C   . SER A 1 10  ? 45.197 30.184 23.448 1.00 29.98  ? 5   SER A C   1 
ATOM   64   O  O   . SER A 1 10  ? 45.145 29.373 24.390 1.00 31.68  ? 5   SER A O   1 
ATOM   65   C  CB  . SER A 1 10  ? 47.224 31.721 23.522 1.00 34.45  ? 5   SER A CB  1 
ATOM   66   O  OG  . SER A 1 10  ? 48.449 32.077 22.864 1.00 34.23  ? 5   SER A OG  1 
ATOM   67   N  N   . LEU A 1 11  ? 44.131 30.808 22.946 1.00 27.61  ? 6   LEU A N   1 
ATOM   68   C  CA  . LEU A 1 11  ? 42.775 30.496 23.436 1.00 27.71  ? 6   LEU A CA  1 
ATOM   69   C  C   . LEU A 1 11  ? 42.452 29.015 23.112 1.00 30.61  ? 6   LEU A C   1 
ATOM   70   O  O   . LEU A 1 11  ? 41.955 28.327 24.014 1.00 28.93  ? 6   LEU A O   1 
ATOM   71   C  CB  . LEU A 1 11  ? 41.767 31.445 22.814 1.00 30.77  ? 6   LEU A CB  1 
ATOM   72   C  CG  . LEU A 1 11  ? 41.831 32.886 23.323 1.00 29.51  ? 6   LEU A CG  1 
ATOM   73   C  CD1 . LEU A 1 11  ? 41.063 33.791 22.379 1.00 29.82  ? 6   LEU A CD1 1 
ATOM   74   C  CD2 . LEU A 1 11  ? 41.288 32.949 24.742 1.00 29.35  ? 6   LEU A CD2 1 
ATOM   75   N  N   . ILE A 1 12  ? 42.771 28.538 21.904 1.00 32.39  ? 7   ILE A N   1 
ATOM   76   C  CA  . ILE A 1 12  ? 42.536 27.110 21.526 1.00 33.04  ? 7   ILE A CA  1 
ATOM   77   C  C   . ILE A 1 12  ? 43.310 26.213 22.493 1.00 34.54  ? 7   ILE A C   1 
ATOM   78   O  O   . ILE A 1 12  ? 42.697 25.296 23.032 1.00 32.40  ? 7   ILE A O   1 
ATOM   79   C  CB  . ILE A 1 12  ? 42.920 26.801 20.074 1.00 32.81  ? 7   ILE A CB  1 
ATOM   80   C  CG1 . ILE A 1 12  ? 42.135 27.667 19.088 1.00 30.87  ? 7   ILE A CG1 1 
ATOM   81   C  CG2 . ILE A 1 12  ? 42.743 25.315 19.807 1.00 30.21  ? 7   ILE A CG2 1 
ATOM   82   C  CD1 . ILE A 1 12  ? 40.650 27.555 19.223 1.00 32.14  ? 7   ILE A CD1 1 
ATOM   83   N  N   . GLN A 1 13  ? 44.599 26.497 22.693 1.00 30.62  ? 8   GLN A N   1 
ATOM   84   C  CA  . GLN A 1 13  ? 45.527 25.769 23.579 1.00 35.09  ? 8   GLN A CA  1 
ATOM   85   C  C   . GLN A 1 13  ? 44.939 25.693 24.990 1.00 33.69  ? 8   GLN A C   1 
ATOM   86   O  O   . GLN A 1 13  ? 44.962 24.587 25.618 1.00 31.03  ? 8   GLN A O   1 
ATOM   87   C  CB  . GLN A 1 13  ? 46.896 26.440 23.537 1.00 40.48  ? 8   GLN A CB  1 
ATOM   88   C  CG  . GLN A 1 13  ? 48.051 25.582 24.008 1.00 49.95  ? 8   GLN A CG  1 
ATOM   89   C  CD  . GLN A 1 13  ? 49.351 26.357 23.979 1.00 58.49  ? 8   GLN A CD  1 
ATOM   90   O  OE1 . GLN A 1 13  ? 49.488 27.355 23.261 1.00 47.26  ? 8   GLN A OE1 1 
ATOM   91   N  NE2 . GLN A 1 13  ? 50.304 25.911 24.796 1.00 57.11  ? 8   GLN A NE2 1 
ATOM   92   N  N   . LYS A 1 14  ? 44.413 26.802 25.504 1.00 28.41  ? 9   LYS A N   1 
ATOM   93   C  CA  . LYS A 1 14  ? 43.916 26.852 26.902 1.00 27.86  ? 9   LYS A CA  1 
ATOM   94   C  C   . LYS A 1 14  ? 42.581 26.115 26.978 1.00 24.16  ? 9   LYS A C   1 
ATOM   95   O  O   . LYS A 1 14  ? 42.314 25.539 28.009 1.00 28.94  ? 9   LYS A O   1 
ATOM   96   C  CB  . LYS A 1 14  ? 43.860 28.300 27.392 1.00 27.71  ? 9   LYS A CB  1 
ATOM   97   C  CG  . LYS A 1 14  ? 45.248 28.831 27.737 1.00 29.78  ? 9   LYS A CG  1 
ATOM   98   C  CD  . LYS A 1 14  ? 45.219 30.268 28.282 1.00 32.89  ? 9   LYS A CD  1 
ATOM   99   C  CE  . LYS A 1 14  ? 46.604 30.854 28.340 1.00 33.49  ? 9   LYS A CE  1 
ATOM   100  N  NZ  . LYS A 1 14  ? 46.531 32.248 28.824 1.00 34.38  ? 9   LYS A NZ  1 
ATOM   101  N  N   . ALA A 1 15  ? 41.794 26.139 25.910 1.00 27.85  ? 10  ALA A N   1 
ATOM   102  C  CA  . ALA A 1 15  ? 40.523 25.369 25.852 1.00 30.23  ? 10  ALA A CA  1 
ATOM   103  C  C   . ALA A 1 15  ? 40.855 23.878 26.016 1.00 29.94  ? 10  ALA A C   1 
ATOM   104  O  O   . ALA A 1 15  ? 40.158 23.175 26.768 1.00 27.61  ? 10  ALA A O   1 
ATOM   105  C  CB  . ALA A 1 15  ? 39.772 25.634 24.579 1.00 30.62  ? 10  ALA A CB  1 
ATOM   106  N  N   . LYS A 1 16  ? 41.905 23.421 25.370 1.00 27.97  ? 11  LYS A N   1 
ATOM   107  C  CA  . LYS A 1 16  ? 42.312 21.993 25.470 1.00 33.02  ? 11  LYS A CA  1 
ATOM   108  C  C   . LYS A 1 16  ? 42.830 21.682 26.884 1.00 35.22  ? 11  LYS A C   1 
ATOM   109  O  O   . LYS A 1 16  ? 42.461 20.634 27.426 1.00 29.61  ? 11  LYS A O   1 
ATOM   110  C  CB  . LYS A 1 16  ? 43.343 21.690 24.401 1.00 32.82  ? 11  LYS A CB  1 
ATOM   111  C  CG  . LYS A 1 16  ? 42.802 21.713 22.992 1.00 32.56  ? 11  LYS A CG  1 
ATOM   112  C  CD  . LYS A 1 16  ? 43.908 21.480 21.981 1.00 36.65  ? 11  LYS A CD  1 
ATOM   113  C  CE  . LYS A 1 16  ? 43.399 21.431 20.559 1.00 39.01  ? 11  LYS A CE  1 
ATOM   114  N  NZ  . LYS A 1 16  ? 44.492 21.691 19.600 1.00 39.26  ? 11  LYS A NZ  1 
ATOM   115  N  N   . LEU A 1 17  ? 43.597 22.574 27.499 1.00 30.93  ? 12  LEU A N   1 
ATOM   116  C  CA  . LEU A 1 17  ? 44.065 22.410 28.901 1.00 32.08  ? 12  LEU A CA  1 
ATOM   117  C  C   . LEU A 1 17  ? 42.861 22.375 29.832 1.00 29.45  ? 12  LEU A C   1 
ATOM   118  O  O   . LEU A 1 17  ? 42.842 21.516 30.752 1.00 31.04  ? 12  LEU A O   1 
ATOM   119  C  CB  . LEU A 1 17  ? 45.038 23.531 29.298 1.00 32.53  ? 12  LEU A CB  1 
ATOM   120  C  CG  . LEU A 1 17  ? 46.375 23.541 28.573 1.00 31.76  ? 12  LEU A CG  1 
ATOM   121  C  CD1 . LEU A 1 17  ? 47.084 24.872 28.855 1.00 34.48  ? 12  LEU A CD1 1 
ATOM   122  C  CD2 . LEU A 1 17  ? 47.253 22.357 28.959 1.00 31.90  ? 12  LEU A CD2 1 
ATOM   123  N  N   . ALA A 1 18  ? 41.905 23.286 29.652 1.00 29.61  ? 13  ALA A N   1 
ATOM   124  C  CA  . ALA A 1 18  ? 40.705 23.343 30.501 1.00 30.57  ? 13  ALA A CA  1 
ATOM   125  C  C   . ALA A 1 18  ? 39.929 22.006 30.374 1.00 31.27  ? 13  ALA A C   1 
ATOM   126  O  O   . ALA A 1 18  ? 39.386 21.546 31.371 1.00 28.61  ? 13  ALA A O   1 
ATOM   127  C  CB  . ALA A 1 18  ? 39.832 24.507 30.113 1.00 30.13  ? 13  ALA A CB  1 
ATOM   128  N  N   . GLU A 1 19  ? 39.819 21.459 29.166 1.00 30.64  ? 14  GLU A N   1 
ATOM   129  C  CA  . GLU A 1 19  ? 39.134 20.154 28.965 1.00 32.44  ? 14  GLU A CA  1 
ATOM   130  C  C   . GLU A 1 19  ? 39.845 19.093 29.819 1.00 33.55  ? 14  GLU A C   1 
ATOM   131  O  O   . GLU A 1 19  ? 39.164 18.373 30.563 1.00 35.22  ? 14  GLU A O   1 
ATOM   132  C  CB  . GLU A 1 19  ? 39.082 19.772 27.496 1.00 36.17  ? 14  GLU A CB  1 
ATOM   133  C  CG  . GLU A 1 19  ? 38.262 18.515 27.258 1.00 39.09  ? 14  GLU A CG  1 
ATOM   134  C  CD  . GLU A 1 19  ? 38.211 18.074 25.807 1.00 43.66  ? 14  GLU A CD  1 
ATOM   135  O  OE1 . GLU A 1 19  ? 39.113 18.458 25.025 1.00 43.23  ? 14  GLU A OE1 1 
ATOM   136  O  OE2 . GLU A 1 19  ? 37.269 17.339 25.465 1.00 44.78  ? 14  GLU A OE2 1 
ATOM   137  N  N   . GLN A 1 20  ? 41.171 19.037 29.748 1.00 34.18  ? 15  GLN A N   1 
ATOM   138  C  CA  . GLN A 1 20  ? 41.993 18.070 30.519 1.00 34.23  ? 15  GLN A CA  1 
ATOM   139  C  C   . GLN A 1 20  ? 41.758 18.237 32.016 1.00 38.27  ? 15  GLN A C   1 
ATOM   140  O  O   . GLN A 1 20  ? 41.666 17.225 32.720 1.00 34.74  ? 15  GLN A O   1 
ATOM   141  C  CB  . GLN A 1 20  ? 43.465 18.226 30.176 1.00 39.62  ? 15  GLN A CB  1 
ATOM   142  C  CG  . GLN A 1 20  ? 43.792 17.808 28.752 1.00 45.05  ? 15  GLN A CG  1 
ATOM   143  C  CD  . GLN A 1 20  ? 45.267 17.947 28.443 1.00 51.13  ? 15  GLN A CD  1 
ATOM   144  O  OE1 . GLN A 1 20  ? 45.709 18.887 27.785 1.00 64.05  ? 15  GLN A OE1 1 
ATOM   145  N  NE2 . GLN A 1 20  ? 46.058 17.011 28.930 1.00 55.36  ? 15  GLN A NE2 1 
ATOM   146  N  N   . ALA A 1 21  ? 41.575 19.459 32.490 1.00 33.84  ? 16  ALA A N   1 
ATOM   147  C  CA  . ALA A 1 21  ? 41.398 19.777 33.919 1.00 33.55  ? 16  ALA A CA  1 
ATOM   148  C  C   . ALA A 1 21  ? 39.923 19.700 34.351 1.00 32.98  ? 16  ALA A C   1 
ATOM   149  O  O   . ALA A 1 21  ? 39.633 19.983 35.544 1.00 33.06  ? 16  ALA A O   1 
ATOM   150  C  CB  . ALA A 1 21  ? 41.990 21.156 34.167 1.00 36.82  ? 16  ALA A CB  1 
ATOM   151  N  N   . GLU A 1 22  ? 39.023 19.375 33.424 1.00 32.05  ? 17  GLU A N   1 
ATOM   152  C  CA  . GLU A 1 22  ? 37.549 19.316 33.650 1.00 32.93  ? 17  GLU A CA  1 
ATOM   153  C  C   . GLU A 1 22  ? 37.068 20.678 34.172 1.00 30.29  ? 17  GLU A C   1 
ATOM   154  O  O   . GLU A 1 22  ? 36.170 20.738 35.032 1.00 32.40  ? 17  GLU A O   1 
ATOM   155  C  CB  . GLU A 1 22  ? 37.185 18.144 34.586 1.00 35.75  ? 17  GLU A CB  1 
ATOM   156  C  CG  . GLU A 1 22  ? 37.641 16.797 34.032 1.00 38.31  ? 17  GLU A CG  1 
ATOM   157  C  CD  . GLU A 1 22  ? 37.323 15.584 34.913 1.00 46.77  ? 17  GLU A CD  1 
ATOM   158  O  OE1 . GLU A 1 22  ? 36.378 15.655 35.683 1.00 48.79  ? 17  GLU A OE1 1 
ATOM   159  O  OE2 . GLU A 1 22  ? 38.066 14.594 34.851 1.00 58.08  ? 17  GLU A OE2 1 
ATOM   160  N  N   . ARG A 1 23  ? 37.618 21.754 33.624 1.00 30.80  ? 18  ARG A N   1 
ATOM   161  C  CA  . ARG A 1 23  ? 37.178 23.140 33.928 1.00 29.43  ? 18  ARG A CA  1 
ATOM   162  C  C   . ARG A 1 23  ? 36.335 23.660 32.774 1.00 31.51  ? 18  ARG A C   1 
ATOM   163  O  O   . ARG A 1 23  ? 36.868 24.361 31.889 1.00 29.23  ? 18  ARG A O   1 
ATOM   164  C  CB  . ARG A 1 23  ? 38.436 24.001 34.107 1.00 30.49  ? 18  ARG A CB  1 
ATOM   165  C  CG  . ARG A 1 23  ? 39.223 23.608 35.350 1.00 32.84  ? 18  ARG A CG  1 
ATOM   166  C  CD  . ARG A 1 23  ? 38.639 24.239 36.585 1.00 34.94  ? 18  ARG A CD  1 
ATOM   167  N  NE  . ARG A 1 23  ? 38.883 25.677 36.461 1.00 34.17  ? 18  ARG A NE  1 
ATOM   168  C  CZ  . ARG A 1 23  ? 38.772 26.562 37.432 1.00 36.05  ? 18  ARG A CZ  1 
ATOM   169  N  NH1 . ARG A 1 23  ? 38.460 26.161 38.646 1.00 34.67  ? 18  ARG A NH1 1 
ATOM   170  N  NH2 . ARG A 1 23  ? 38.981 27.848 37.189 1.00 33.04  ? 18  ARG A NH2 1 
ATOM   171  N  N   . TYR A 1 24  ? 35.072 23.257 32.687 1.00 31.65  ? 19  TYR A N   1 
ATOM   172  C  CA  . TYR A 1 24  ? 34.314 23.400 31.421 1.00 30.80  ? 19  TYR A CA  1 
ATOM   173  C  C   . TYR A 1 24  ? 33.808 24.841 31.252 1.00 29.37  ? 19  TYR A C   1 
ATOM   174  O  O   . TYR A 1 24  ? 33.590 25.242 30.100 1.00 29.52  ? 19  TYR A O   1 
ATOM   175  C  CB  . TYR A 1 24  ? 33.164 22.393 31.360 1.00 30.13  ? 19  TYR A CB  1 
ATOM   176  C  CG  . TYR A 1 24  ? 33.678 20.976 31.340 1.00 32.24  ? 19  TYR A CG  1 
ATOM   177  C  CD1 . TYR A 1 24  ? 34.302 20.477 30.207 1.00 37.64  ? 19  TYR A CD1 1 
ATOM   178  C  CD2 . TYR A 1 24  ? 33.582 20.160 32.466 1.00 33.40  ? 19  TYR A CD2 1 
ATOM   179  C  CE1 . TYR A 1 24  ? 34.812 19.192 30.175 1.00 35.72  ? 19  TYR A CE1 1 
ATOM   180  C  CE2 . TYR A 1 24  ? 34.091 18.869 32.451 1.00 35.41  ? 19  TYR A CE2 1 
ATOM   181  C  CZ  . TYR A 1 24  ? 34.700 18.397 31.303 1.00 37.59  ? 19  TYR A CZ  1 
ATOM   182  O  OH  . TYR A 1 24  ? 35.220 17.143 31.275 1.00 42.29  ? 19  TYR A OH  1 
ATOM   183  N  N   . GLU A 1 25  ? 33.550 25.543 32.346 1.00 28.81  ? 20  GLU A N   1 
ATOM   184  C  CA  . GLU A 1 25  ? 33.209 26.995 32.290 1.00 33.42  ? 20  GLU A CA  1 
ATOM   185  C  C   . GLU A 1 25  ? 34.378 27.776 31.672 1.00 31.26  ? 20  GLU A C   1 
ATOM   186  O  O   . GLU A 1 25  ? 34.131 28.578 30.762 1.00 33.79  ? 20  GLU A O   1 
ATOM   187  C  CB  . GLU A 1 25  ? 32.933 27.541 33.688 1.00 40.21  ? 20  GLU A CB  1 
ATOM   188  C  CG  . GLU A 1 25  ? 31.574 28.155 33.863 1.00 55.50  ? 20  GLU A CG  1 
ATOM   189  C  CD  . GLU A 1 25  ? 31.454 28.970 35.148 1.00 65.52  ? 20  GLU A CD  1 
ATOM   190  O  OE1 . GLU A 1 25  ? 32.065 28.568 36.158 1.00 69.38  ? 20  GLU A OE1 1 
ATOM   191  O  OE2 . GLU A 1 25  ? 30.780 30.026 35.124 1.00 71.23  ? 20  GLU A OE2 1 
ATOM   192  N  N   . ASP A 1 26  ? 35.606 27.540 32.134 1.00 29.88  ? 21  ASP A N   1 
ATOM   193  C  CA  . ASP A 1 26  ? 36.823 28.152 31.544 1.00 29.49  ? 21  ASP A CA  1 
ATOM   194  C  C   . ASP A 1 26  ? 36.908 27.743 30.080 1.00 30.91  ? 21  ASP A C   1 
ATOM   195  O  O   . ASP A 1 26  ? 37.209 28.589 29.190 1.00 26.46  ? 21  ASP A O   1 
ATOM   196  C  CB  . ASP A 1 26  ? 38.106 27.700 32.235 1.00 30.99  ? 21  ASP A CB  1 
ATOM   197  C  CG  . ASP A 1 26  ? 38.294 28.217 33.645 1.00 34.09  ? 21  ASP A CG  1 
ATOM   198  O  OD1 . ASP A 1 26  ? 37.528 29.117 34.016 1.00 35.66  ? 21  ASP A OD1 1 
ATOM   199  O  OD2 . ASP A 1 26  ? 39.196 27.700 34.351 1.00 33.79  ? 21  ASP A OD2 1 
ATOM   200  N  N   . MET A 1 27  ? 36.657 26.459 29.789 1.00 30.33  ? 22  MET A N   1 
ATOM   201  C  CA  . MET A 1 27  ? 36.808 25.958 28.410 1.00 27.45  ? 22  MET A CA  1 
ATOM   202  C  C   . MET A 1 27  ? 35.837 26.700 27.488 1.00 26.31  ? 22  MET A C   1 
ATOM   203  O  O   . MET A 1 27  ? 36.264 27.122 26.391 1.00 30.20  ? 22  MET A O   1 
ATOM   204  C  CB  . MET A 1 27  ? 36.647 24.432 28.372 1.00 28.33  ? 22  MET A CB  1 
ATOM   205  C  CG  . MET A 1 27  ? 36.753 23.838 27.045 1.00 28.53  ? 22  MET A CG  1 
ATOM   206  S  SD  . MET A 1 27  ? 36.245 22.046 27.179 1.00 30.44  ? 22  MET A SD  1 
ATOM   207  C  CE  . MET A 1 27  ? 36.661 21.527 25.521 1.00 33.50  ? 22  MET A CE  1 
ATOM   208  N  N   . ALA A 1 28  ? 34.598 26.920 27.942 1.00 25.19  ? 23  ALA A N   1 
ATOM   209  C  CA  . ALA A 1 28  ? 33.580 27.617 27.152 1.00 27.61  ? 23  ALA A CA  1 
ATOM   210  C  C   . ALA A 1 28  ? 34.030 29.074 26.912 1.00 28.60  ? 23  ALA A C   1 
ATOM   211  O  O   . ALA A 1 28  ? 33.911 29.552 25.736 1.00 30.45  ? 23  ALA A O   1 
ATOM   212  C  CB  . ALA A 1 28  ? 32.255 27.523 27.858 1.00 25.14  ? 23  ALA A CB  1 
ATOM   213  N  N   . ALA A 1 29  ? 34.584 29.708 27.941 1.00 31.77  ? 24  ALA A N   1 
ATOM   214  C  CA  . ALA A 1 29  ? 35.005 31.132 27.905 1.00 31.15  ? 24  ALA A CA  1 
ATOM   215  C  C   . ALA A 1 29  ? 36.135 31.282 26.887 1.00 32.50  ? 24  ALA A C   1 
ATOM   216  O  O   . ALA A 1 29  ? 36.056 32.158 26.042 1.00 30.63  ? 24  ALA A O   1 
ATOM   217  C  CB  . ALA A 1 29  ? 35.394 31.605 29.288 1.00 34.80  ? 24  ALA A CB  1 
ATOM   218  N  N   . PHE A 1 30  ? 37.118 30.388 26.928 1.00 28.15  ? 25  PHE A N   1 
ATOM   219  C  CA  . PHE A 1 30  ? 38.225 30.304 25.956 1.00 28.96  ? 25  PHE A CA  1 
ATOM   220  C  C   . PHE A 1 30  ? 37.698 30.119 24.534 1.00 31.50  ? 25  PHE A C   1 
ATOM   221  O  O   . PHE A 1 30  ? 38.177 30.824 23.597 1.00 30.99  ? 25  PHE A O   1 
ATOM   222  C  CB  . PHE A 1 30  ? 39.239 29.231 26.337 1.00 27.21  ? 25  PHE A CB  1 
ATOM   223  C  CG  . PHE A 1 30  ? 40.037 29.493 27.584 1.00 30.59  ? 25  PHE A CG  1 
ATOM   224  C  CD1 . PHE A 1 30  ? 40.579 30.746 27.896 1.00 30.35  ? 25  PHE A CD1 1 
ATOM   225  C  CD2 . PHE A 1 30  ? 40.275 28.454 28.466 1.00 30.05  ? 25  PHE A CD2 1 
ATOM   226  C  CE1 . PHE A 1 30  ? 41.293 30.935 29.076 1.00 29.13  ? 25  PHE A CE1 1 
ATOM   227  C  CE2 . PHE A 1 30  ? 40.968 28.643 29.647 1.00 28.09  ? 25  PHE A CE2 1 
ATOM   228  C  CZ  . PHE A 1 30  ? 41.522 29.878 29.932 1.00 31.44  ? 25  PHE A CZ  1 
ATOM   229  N  N   . MET A 1 31  ? 36.699 29.252 24.335 1.00 31.08  ? 26  MET A N   1 
ATOM   230  C  CA  . MET A 1 31  ? 36.214 28.998 22.963 1.00 28.95  ? 26  MET A CA  1 
ATOM   231  C  C   . MET A 1 31  ? 35.346 30.181 22.494 1.00 28.70  ? 26  MET A C   1 
ATOM   232  O  O   . MET A 1 31  ? 35.394 30.456 21.310 1.00 29.80  ? 26  MET A O   1 
ATOM   233  C  CB  . MET A 1 31  ? 35.420 27.683 22.883 1.00 28.34  ? 26  MET A CB  1 
ATOM   234  C  CG  . MET A 1 31  ? 36.332 26.495 22.997 1.00 27.23  ? 26  MET A CG  1 
ATOM   235  S  SD  . MET A 1 31  ? 37.725 26.458 21.898 1.00 30.13  ? 26  MET A SD  1 
ATOM   236  C  CE  . MET A 1 31  ? 36.936 26.610 20.302 1.00 29.08  ? 26  MET A CE  1 
ATOM   237  N  N   . LYS A 1 32  ? 34.582 30.812 23.372 1.00 30.32  ? 27  LYS A N   1 
ATOM   238  C  CA  . LYS A 1 32  ? 33.808 32.035 23.020 1.00 32.47  ? 27  LYS A CA  1 
ATOM   239  C  C   . LYS A 1 32  ? 34.827 33.089 22.554 1.00 31.60  ? 27  LYS A C   1 
ATOM   240  O  O   . LYS A 1 32  ? 34.580 33.717 21.486 1.00 36.53  ? 27  LYS A O   1 
ATOM   241  C  CB  . LYS A 1 32  ? 32.972 32.537 24.196 1.00 35.56  ? 27  LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 32  ? 32.279 33.887 23.984 1.00 35.37  ? 27  LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 32  ? 31.238 34.196 25.034 1.00 36.79  ? 27  LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 32  ? 30.365 35.405 24.712 1.00 40.81  ? 27  LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 32  ? 31.132 36.651 24.842 1.00 40.63  ? 27  LYS A NZ  1 
ATOM   246  N  N   . GLY A 1 33  ? 35.972 33.173 23.229 1.00 32.49  ? 28  GLY A N   1 
ATOM   247  C  CA  . GLY A 1 33  ? 37.074 34.101 22.880 1.00 33.16  ? 28  GLY A CA  1 
ATOM   248  C  C   . GLY A 1 33  ? 37.598 33.809 21.495 1.00 36.70  ? 28  GLY A C   1 
ATOM   249  O  O   . GLY A 1 33  ? 37.804 34.736 20.697 1.00 35.46  ? 28  GLY A O   1 
ATOM   250  N  N   . ALA A 1 34  ? 37.816 32.531 21.198 1.00 32.12  ? 29  ALA A N   1 
ATOM   251  C  CA  . ALA A 1 34  ? 38.339 32.086 19.906 1.00 30.51  ? 29  ALA A CA  1 
ATOM   252  C  C   . ALA A 1 34  ? 37.311 32.411 18.828 1.00 32.89  ? 29  ALA A C   1 
ATOM   253  O  O   . ALA A 1 34  ? 37.717 32.934 17.785 1.00 32.34  ? 29  ALA A O   1 
ATOM   254  C  CB  . ALA A 1 34  ? 38.733 30.629 19.961 1.00 29.25  ? 29  ALA A CB  1 
ATOM   255  N  N   . VAL A 1 35  ? 36.028 32.152 19.078 1.00 29.27  ? 30  VAL A N   1 
ATOM   256  C  CA  . VAL A 1 35  ? 34.993 32.384 18.045 1.00 34.47  ? 30  VAL A CA  1 
ATOM   257  C  C   . VAL A 1 35  ? 34.978 33.887 17.730 1.00 37.73  ? 30  VAL A C   1 
ATOM   258  O  O   . VAL A 1 35  ? 34.760 34.258 16.557 1.00 33.84  ? 30  VAL A O   1 
ATOM   259  C  CB  . VAL A 1 35  ? 33.615 31.907 18.541 1.00 36.14  ? 30  VAL A CB  1 
ATOM   260  C  CG1 . VAL A 1 35  ? 32.487 32.478 17.689 1.00 34.89  ? 30  VAL A CG1 1 
ATOM   261  C  CG2 . VAL A 1 35  ? 33.528 30.378 18.595 1.00 36.98  ? 30  VAL A CG2 1 
ATOM   262  N  N   . GLU A 1 36  ? 35.134 34.716 18.761 1.00 34.62  ? 31  GLU A N   1 
ATOM   263  C  CA  . GLU A 1 36  ? 35.023 36.205 18.647 1.00 37.11  ? 31  GLU A CA  1 
ATOM   264  C  C   . GLU A 1 36  ? 36.183 36.771 17.819 1.00 39.01  ? 31  GLU A C   1 
ATOM   265  O  O   . GLU A 1 36  ? 36.059 37.911 17.388 1.00 36.96  ? 31  GLU A O   1 
ATOM   266  C  CB  . GLU A 1 36  ? 34.906 36.868 20.015 1.00 32.46  ? 31  GLU A CB  1 
ATOM   267  C  CG  . GLU A 1 36  ? 33.479 36.829 20.490 1.00 37.57  ? 31  GLU A CG  1 
ATOM   268  C  CD  . GLU A 1 36  ? 33.276 37.073 21.960 1.00 38.67  ? 31  GLU A CD  1 
ATOM   269  O  OE1 . GLU A 1 36  ? 34.297 37.212 22.700 1.00 43.20  ? 31  GLU A OE1 1 
ATOM   270  O  OE2 . GLU A 1 36  ? 32.078 37.107 22.361 1.00 43.77  ? 31  GLU A OE2 1 
ATOM   271  N  N   . LYS A 1 37  ? 37.230 36.001 17.550 1.00 34.68  ? 32  LYS A N   1 
ATOM   272  C  CA  . LYS A 1 37  ? 38.300 36.421 16.615 1.00 37.76  ? 32  LYS A CA  1 
ATOM   273  C  C   . LYS A 1 37  ? 37.751 36.564 15.188 1.00 44.72  ? 32  LYS A C   1 
ATOM   274  O  O   . LYS A 1 37  ? 38.381 37.258 14.385 1.00 43.45  ? 32  LYS A O   1 
ATOM   275  C  CB  . LYS A 1 37  ? 39.469 35.446 16.668 1.00 36.13  ? 32  LYS A CB  1 
ATOM   276  C  CG  . LYS A 1 37  ? 40.143 35.328 18.031 1.00 39.72  ? 32  LYS A CG  1 
ATOM   277  C  CD  . LYS A 1 37  ? 40.681 36.647 18.620 1.00 39.56  ? 32  LYS A CD  1 
ATOM   278  C  CE  . LYS A 1 37  ? 41.296 36.424 19.987 1.00 40.12  ? 32  LYS A CE  1 
ATOM   279  N  NZ  . LYS A 1 37  ? 41.477 37.695 20.725 1.00 41.46  ? 32  LYS A NZ  1 
ATOM   280  N  N   . GLY A 1 38  ? 36.636 35.902 14.880 1.00 41.96  ? 33  GLY A N   1 
ATOM   281  C  CA  . GLY A 1 38  ? 35.911 36.037 13.615 1.00 40.06  ? 33  GLY A CA  1 
ATOM   282  C  C   . GLY A 1 38  ? 36.518 35.181 12.522 1.00 40.97  ? 33  GLY A C   1 
ATOM   283  O  O   . GLY A 1 38  ? 36.138 35.398 11.363 1.00 42.08  ? 33  GLY A O   1 
ATOM   284  N  N   . GLU A 1 39  ? 37.411 34.242 12.832 1.00 37.55  ? 34  GLU A N   1 
ATOM   285  C  CA  . GLU A 1 39  ? 37.817 33.197 11.846 1.00 38.03  ? 34  GLU A CA  1 
ATOM   286  C  C   . GLU A 1 39  ? 36.899 31.972 11.976 1.00 38.93  ? 34  GLU A C   1 
ATOM   287  O  O   . GLU A 1 39  ? 36.297 31.771 13.059 1.00 37.12  ? 34  GLU A O   1 
ATOM   288  C  CB  . GLU A 1 39  ? 39.255 32.728 12.043 1.00 43.81  ? 34  GLU A CB  1 
ATOM   289  C  CG  . GLU A 1 39  ? 40.316 33.795 11.839 1.00 56.87  ? 34  GLU A CG  1 
ATOM   290  C  CD  . GLU A 1 39  ? 41.713 33.219 12.037 1.00 64.03  ? 34  GLU A CD  1 
ATOM   291  O  OE1 . GLU A 1 39  ? 42.559 33.891 12.677 1.00 74.22  ? 34  GLU A OE1 1 
ATOM   292  O  OE2 . GLU A 1 39  ? 41.946 32.070 11.581 1.00 74.94  ? 34  GLU A OE2 1 
ATOM   293  N  N   . GLU A 1 40  ? 36.859 31.142 10.940 1.00 44.52  ? 35  GLU A N   1 
ATOM   294  C  CA  . GLU A 1 40  ? 36.070 29.888 10.940 1.00 46.40  ? 35  GLU A CA  1 
ATOM   295  C  C   . GLU A 1 40  ? 36.675 28.920 11.949 1.00 43.90  ? 35  GLU A C   1 
ATOM   296  O  O   . GLU A 1 40  ? 37.850 29.047 12.272 1.00 39.43  ? 35  GLU A O   1 
ATOM   297  C  CB  . GLU A 1 40  ? 36.041 29.257 9.554  1.00 55.38  ? 35  GLU A CB  1 
ATOM   298  C  CG  . GLU A 1 40  ? 35.122 30.000 8.619  1.00 63.20  ? 35  GLU A CG  1 
ATOM   299  C  CD  . GLU A 1 40  ? 34.877 29.262 7.321  1.00 70.31  ? 35  GLU A CD  1 
ATOM   300  O  OE1 . GLU A 1 40  ? 33.770 29.407 6.770  1.00 80.53  ? 35  GLU A OE1 1 
ATOM   301  O  OE2 . GLU A 1 40  ? 35.796 28.543 6.879  1.00 70.43  ? 35  GLU A OE2 1 
ATOM   302  N  N   . LEU A 1 41  ? 35.861 28.006 12.467 1.00 45.55  ? 36  LEU A N   1 
ATOM   303  C  CA  . LEU A 1 41  ? 36.363 26.908 13.330 1.00 38.63  ? 36  LEU A CA  1 
ATOM   304  C  C   . LEU A 1 41  ? 36.563 25.675 12.456 1.00 37.35  ? 36  LEU A C   1 
ATOM   305  O  O   . LEU A 1 41  ? 35.700 25.400 11.620 1.00 38.51  ? 36  LEU A O   1 
ATOM   306  C  CB  . LEU A 1 41  ? 35.352 26.602 14.440 1.00 40.84  ? 36  LEU A CB  1 
ATOM   307  C  CG  . LEU A 1 41  ? 35.120 27.669 15.508 1.00 42.81  ? 36  LEU A CG  1 
ATOM   308  C  CD1 . LEU A 1 41  ? 34.370 27.089 16.709 1.00 42.83  ? 36  LEU A CD1 1 
ATOM   309  C  CD2 . LEU A 1 41  ? 36.418 28.286 15.945 1.00 46.93  ? 36  LEU A CD2 1 
ATOM   310  N  N   . SER A 1 42  ? 37.613 24.917 12.716 1.00 36.68  ? 37  SER A N   1 
ATOM   311  C  CA  . SER A 1 42  ? 37.799 23.545 12.179 1.00 37.03  ? 37  SER A CA  1 
ATOM   312  C  C   . SER A 1 42  ? 36.867 22.541 12.884 1.00 38.23  ? 37  SER A C   1 
ATOM   313  O  O   . SER A 1 42  ? 36.271 22.865 13.942 1.00 31.01  ? 37  SER A O   1 
ATOM   314  C  CB  . SER A 1 42  ? 39.202 23.128 12.344 1.00 36.01  ? 37  SER A CB  1 
ATOM   315  O  OG  . SER A 1 42  ? 39.519 22.996 13.730 1.00 37.36  ? 37  SER A OG  1 
ATOM   316  N  N   . CYS A 1 43  ? 36.833 21.314 12.380 1.00 38.69  ? 38  CYS A N   1 
ATOM   317  C  CA  . CYS A 1 43  ? 36.110 20.176 13.024 1.00 38.61  ? 38  CYS A CA  1 
ATOM   318  C  C   . CYS A 1 43  ? 36.560 20.030 14.489 1.00 35.18  ? 38  CYS A C   1 
ATOM   319  O  O   . CYS A 1 43  ? 35.703 19.997 15.373 1.00 31.00  ? 38  CYS A O   1 
ATOM   320  C  CB  . CYS A 1 43  ? 36.301 18.899 12.218 1.00 44.43  ? 38  CYS A CB  1 
ATOM   321  S  SG  . CYS A 1 43  ? 35.052 17.610 12.520 1.00 60.73  ? 38  CYS A SG  1 
ATOM   322  N  N   . GLU A 1 44  ? 37.863 20.000 14.743 1.00 35.70  ? 39  GLU A N   1 
ATOM   323  C  CA  . GLU A 1 44  ? 38.475 19.853 16.095 1.00 37.30  ? 39  GLU A CA  1 
ATOM   324  C  C   . GLU A 1 44  ? 38.039 21.007 17.005 1.00 34.18  ? 39  GLU A C   1 
ATOM   325  O  O   . GLU A 1 44  ? 37.791 20.772 18.183 1.00 32.06  ? 39  GLU A O   1 
ATOM   326  C  CB  . GLU A 1 44  ? 39.993 19.876 15.969 1.00 39.95  ? 39  GLU A CB  1 
ATOM   327  C  CG  . GLU A 1 44  ? 40.708 19.577 17.267 1.00 51.63  ? 39  GLU A CG  1 
ATOM   328  C  CD  . GLU A 1 44  ? 42.224 19.428 17.164 1.00 58.03  ? 39  GLU A CD  1 
ATOM   329  O  OE1 . GLU A 1 44  ? 42.855 19.140 18.204 1.00 63.81  ? 39  GLU A OE1 1 
ATOM   330  O  OE2 . GLU A 1 44  ? 42.776 19.615 16.055 1.00 60.47  ? 39  GLU A OE2 1 
ATOM   331  N  N   . GLU A 1 45  ? 37.946 22.231 16.481 1.00 35.88  ? 40  GLU A N   1 
ATOM   332  C  CA  . GLU A 1 45  ? 37.564 23.402 17.313 1.00 33.09  ? 40  GLU A CA  1 
ATOM   333  C  C   . GLU A 1 45  ? 36.057 23.357 17.590 1.00 32.30  ? 40  GLU A C   1 
ATOM   334  O  O   . GLU A 1 45  ? 35.655 23.710 18.717 1.00 30.97  ? 40  GLU A O   1 
ATOM   335  C  CB  . GLU A 1 45  ? 38.018 24.703 16.648 1.00 34.50  ? 40  GLU A CB  1 
ATOM   336  C  CG  . GLU A 1 45  ? 39.542 24.773 16.525 1.00 33.78  ? 40  GLU A CG  1 
ATOM   337  C  CD  . GLU A 1 45  ? 40.087 25.827 15.562 1.00 38.08  ? 40  GLU A CD  1 
ATOM   338  O  OE1 . GLU A 1 45  ? 39.345 26.255 14.663 1.00 34.42  ? 40  GLU A OE1 1 
ATOM   339  O  OE2 . GLU A 1 45  ? 41.266 26.220 15.733 1.00 38.41  ? 40  GLU A OE2 1 
ATOM   340  N  N   . ARG A 1 46  ? 35.245 22.947 16.616 1.00 30.28  ? 41  ARG A N   1 
ATOM   341  C  CA  . ARG A 1 46  ? 33.786 22.805 16.868 1.00 32.58  ? 41  ARG A CA  1 
ATOM   342  C  C   . ARG A 1 46  ? 33.569 21.797 18.005 1.00 30.95  ? 41  ARG A C   1 
ATOM   343  O  O   . ARG A 1 46  ? 32.668 22.008 18.814 1.00 29.40  ? 41  ARG A O   1 
ATOM   344  C  CB  . ARG A 1 46  ? 33.012 22.360 15.629 1.00 32.57  ? 41  ARG A CB  1 
ATOM   345  C  CG  . ARG A 1 46  ? 32.872 23.479 14.612 1.00 35.57  ? 41  ARG A CG  1 
ATOM   346  C  CD  . ARG A 1 46  ? 31.954 23.112 13.486 1.00 38.22  ? 41  ARG A CD  1 
ATOM   347  N  NE  . ARG A 1 46  ? 32.629 22.222 12.594 1.00 37.31  ? 41  ARG A NE  1 
ATOM   348  C  CZ  . ARG A 1 46  ? 33.388 22.571 11.563 1.00 44.35  ? 41  ARG A CZ  1 
ATOM   349  N  NH1 . ARG A 1 46  ? 33.637 23.837 11.310 1.00 41.03  ? 41  ARG A NH1 1 
ATOM   350  N  NH2 . ARG A 1 46  ? 33.920 21.631 10.802 1.00 43.39  ? 41  ARG A NH2 1 
ATOM   351  N  N   . ASN A 1 47  ? 34.399 20.761 18.074 1.00 31.45  ? 42  ASN A N   1 
ATOM   352  C  CA  . ASN A 1 47  ? 34.302 19.729 19.140 1.00 31.40  ? 42  ASN A CA  1 
ATOM   353  C  C   . ASN A 1 47  ? 34.549 20.371 20.511 1.00 30.20  ? 42  ASN A C   1 
ATOM   354  O  O   . ASN A 1 47  ? 33.770 20.149 21.433 1.00 29.02  ? 42  ASN A O   1 
ATOM   355  C  CB  . ASN A 1 47  ? 35.293 18.598 18.876 1.00 34.40  ? 42  ASN A CB  1 
ATOM   356  C  CG  . ASN A 1 47  ? 35.135 17.522 19.907 1.00 35.20  ? 42  ASN A CG  1 
ATOM   357  O  OD1 . ASN A 1 47  ? 34.047 16.960 20.037 1.00 37.51  ? 42  ASN A OD1 1 
ATOM   358  N  ND2 . ASN A 1 47  ? 36.175 17.337 20.704 1.00 37.11  ? 42  ASN A ND2 1 
ATOM   359  N  N   . LEU A 1 48  ? 35.569 21.231 20.607 1.00 29.89  ? 43  LEU A N   1 
ATOM   360  C  CA  . LEU A 1 48  ? 35.909 21.955 21.856 1.00 31.32  ? 43  LEU A CA  1 
ATOM   361  C  C   . LEU A 1 48  ? 34.747 22.862 22.250 1.00 28.94  ? 43  LEU A C   1 
ATOM   362  O  O   . LEU A 1 48  ? 34.352 22.845 23.430 1.00 31.32  ? 43  LEU A O   1 
ATOM   363  C  CB  . LEU A 1 48  ? 37.197 22.766 21.644 1.00 32.28  ? 43  LEU A CB  1 
ATOM   364  C  CG  . LEU A 1 48  ? 38.444 21.933 21.335 1.00 32.61  ? 43  LEU A CG  1 
ATOM   365  C  CD1 . LEU A 1 48  ? 39.613 22.830 20.931 1.00 36.66  ? 43  LEU A CD1 1 
ATOM   366  C  CD2 . LEU A 1 48  ? 38.819 21.072 22.529 1.00 34.02  ? 43  LEU A CD2 1 
ATOM   367  N  N   . LEU A 1 49  ? 34.227 23.642 21.304 1.00 30.66  ? 44  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 49  ? 33.075 24.539 21.590 1.00 29.47  ? 44  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 49  ? 31.896 23.708 22.114 1.00 29.72  ? 44  LEU A C   1 
ATOM   370  O  O   . LEU A 1 49  ? 31.288 24.112 23.122 1.00 30.46  ? 44  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 49  ? 32.697 25.267 20.301 1.00 29.69  ? 44  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 49  ? 31.522 26.232 20.387 1.00 29.19  ? 44  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 49  ? 31.905 27.489 21.176 1.00 34.70  ? 44  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 49  ? 31.045 26.576 18.980 1.00 31.42  ? 44  LEU A CD2 1 
ATOM   375  N  N   . SER A 1 50  ? 31.544 22.638 21.394 1.00 30.76  ? 45  SER A N   1 
ATOM   376  C  CA  . SER A 1 50  ? 30.383 21.739 21.683 1.00 30.27  ? 45  SER A CA  1 
ATOM   377  C  C   . SER A 1 50  ? 30.542 21.122 23.080 1.00 27.83  ? 45  SER A C   1 
ATOM   378  O  O   . SER A 1 50  ? 29.639 21.201 23.922 1.00 27.49  ? 45  SER A O   1 
ATOM   379  C  CB  . SER A 1 50  ? 30.321 20.651 20.635 1.00 30.05  ? 45  SER A CB  1 
ATOM   380  O  OG  . SER A 1 50  ? 29.182 19.811 20.858 1.00 32.15  ? 45  SER A OG  1 
ATOM   381  N  N   . VAL A 1 51  ? 31.680 20.501 23.334 1.00 30.85  ? 46  VAL A N   1 
ATOM   382  C  CA  . VAL A 1 51  ? 31.934 19.815 24.641 1.00 30.74  ? 46  VAL A CA  1 
ATOM   383  C  C   . VAL A 1 51  ? 31.803 20.808 25.805 1.00 29.67  ? 46  VAL A C   1 
ATOM   384  O  O   . VAL A 1 51  ? 31.154 20.522 26.841 1.00 28.36  ? 46  VAL A O   1 
ATOM   385  C  CB  . VAL A 1 51  ? 33.318 19.154 24.641 1.00 32.75  ? 46  VAL A CB  1 
ATOM   386  C  CG1 . VAL A 1 51  ? 33.703 18.720 26.041 1.00 32.27  ? 46  VAL A CG1 1 
ATOM   387  C  CG2 . VAL A 1 51  ? 33.399 17.990 23.656 1.00 33.66  ? 46  VAL A CG2 1 
ATOM   388  N  N   . ALA A 1 52  ? 32.435 21.972 25.678 1.00 29.59  ? 47  ALA A N   1 
ATOM   389  C  CA  . ALA A 1 52  ? 32.494 22.944 26.779 1.00 29.87  ? 47  ALA A CA  1 
ATOM   390  C  C   . ALA A 1 52  ? 31.086 23.390 27.118 1.00 27.42  ? 47  ALA A C   1 
ATOM   391  O  O   . ALA A 1 52  ? 30.704 23.289 28.298 1.00 28.50  ? 47  ALA A O   1 
ATOM   392  C  CB  . ALA A 1 52  ? 33.370 24.110 26.389 1.00 30.92  ? 47  ALA A CB  1 
ATOM   393  N  N   . TYR A 1 53  ? 30.352 23.892 26.123 1.00 28.67  ? 48  TYR A N   1 
ATOM   394  C  CA  . TYR A 1 53  ? 29.004 24.436 26.395 1.00 30.11  ? 48  TYR A CA  1 
ATOM   395  C  C   . TYR A 1 53  ? 28.050 23.312 26.808 1.00 32.25  ? 48  TYR A C   1 
ATOM   396  O  O   . TYR A 1 53  ? 27.214 23.560 27.707 1.00 30.24  ? 48  TYR A O   1 
ATOM   397  C  CB  . TYR A 1 53  ? 28.468 25.294 25.257 1.00 30.42  ? 48  TYR A CB  1 
ATOM   398  C  CG  . TYR A 1 53  ? 29.002 26.704 25.325 1.00 30.05  ? 48  TYR A CG  1 
ATOM   399  C  CD1 . TYR A 1 53  ? 28.607 27.540 26.349 1.00 31.84  ? 48  TYR A CD1 1 
ATOM   400  C  CD2 . TYR A 1 53  ? 29.947 27.164 24.422 1.00 34.97  ? 48  TYR A CD2 1 
ATOM   401  C  CE1 . TYR A 1 53  ? 29.076 28.839 26.443 1.00 34.11  ? 48  TYR A CE1 1 
ATOM   402  C  CE2 . TYR A 1 53  ? 30.435 28.461 24.509 1.00 31.75  ? 48  TYR A CE2 1 
ATOM   403  C  CZ  . TYR A 1 53  ? 29.988 29.302 25.511 1.00 34.28  ? 48  TYR A CZ  1 
ATOM   404  O  OH  . TYR A 1 53  ? 30.480 30.584 25.636 1.00 34.12  ? 48  TYR A OH  1 
ATOM   405  N  N   . LYS A 1 54  ? 28.160 22.138 26.204 1.00 30.77  ? 49  LYS A N   1 
ATOM   406  C  CA  . LYS A 1 54  ? 27.210 21.044 26.567 1.00 30.47  ? 49  LYS A CA  1 
ATOM   407  C  C   . LYS A 1 54  ? 27.407 20.648 28.047 1.00 31.00  ? 49  LYS A C   1 
ATOM   408  O  O   . LYS A 1 54  ? 26.429 20.355 28.725 1.00 33.67  ? 49  LYS A O   1 
ATOM   409  C  CB  . LYS A 1 54  ? 27.339 19.863 25.612 1.00 36.35  ? 49  LYS A CB  1 
ATOM   410  C  CG  . LYS A 1 54  ? 26.213 18.845 25.731 1.00 44.10  ? 49  LYS A CG  1 
ATOM   411  C  CD  . LYS A 1 54  ? 26.295 17.798 24.616 1.00 52.01  ? 49  LYS A CD  1 
ATOM   412  C  CE  . LYS A 1 54  ? 24.984 17.104 24.337 1.00 54.59  ? 49  LYS A CE  1 
ATOM   413  N  NZ  . LYS A 1 54  ? 24.263 16.705 25.572 1.00 53.35  ? 49  LYS A NZ  1 
ATOM   414  N  N   . ASN A 1 55  ? 28.637 20.620 28.529 1.00 31.27  ? 50  ASN A N   1 
ATOM   415  C  CA  . ASN A 1 55  ? 28.950 20.334 29.948 1.00 31.99  ? 50  ASN A CA  1 
ATOM   416  C  C   . ASN A 1 55  ? 28.360 21.407 30.836 1.00 32.41  ? 50  ASN A C   1 
ATOM   417  O  O   . ASN A 1 55  ? 27.768 21.068 31.851 1.00 31.32  ? 50  ASN A O   1 
ATOM   418  C  CB  . ASN A 1 55  ? 30.447 20.278 30.202 1.00 34.40  ? 50  ASN A CB  1 
ATOM   419  C  CG  . ASN A 1 55  ? 30.966 18.870 30.238 1.00 40.21  ? 50  ASN A CG  1 
ATOM   420  O  OD1 . ASN A 1 55  ? 30.691 18.164 31.202 1.00 43.38  ? 50  ASN A OD1 1 
ATOM   421  N  ND2 . ASN A 1 55  ? 31.725 18.486 29.225 1.00 39.88  ? 50  ASN A ND2 1 
ATOM   422  N  N   . VAL A 1 56  ? 28.545 22.678 30.488 1.00 30.54  ? 51  VAL A N   1 
ATOM   423  C  CA  . VAL A 1 56  ? 28.020 23.751 31.344 1.00 28.65  ? 51  VAL A CA  1 
ATOM   424  C  C   . VAL A 1 56  ? 26.498 23.631 31.400 1.00 30.76  ? 51  VAL A C   1 
ATOM   425  O  O   . VAL A 1 56  ? 25.961 23.606 32.524 1.00 32.78  ? 51  VAL A O   1 
ATOM   426  C  CB  . VAL A 1 56  ? 28.460 25.127 30.843 1.00 30.12  ? 51  VAL A CB  1 
ATOM   427  C  CG1 . VAL A 1 56  ? 27.773 26.210 31.647 1.00 29.73  ? 51  VAL A CG1 1 
ATOM   428  C  CG2 . VAL A 1 56  ? 29.984 25.225 30.869 1.00 29.88  ? 51  VAL A CG2 1 
ATOM   429  N  N   . VAL A 1 57  ? 25.836 23.586 30.252 1.00 29.04  ? 52  VAL A N   1 
ATOM   430  C  CA  . VAL A 1 57  ? 24.348 23.625 30.217 1.00 30.05  ? 52  VAL A CA  1 
ATOM   431  C  C   . VAL A 1 57  ? 23.843 22.294 30.796 1.00 29.18  ? 52  VAL A C   1 
ATOM   432  O  O   . VAL A 1 57  ? 22.779 22.305 31.408 1.00 33.45  ? 52  VAL A O   1 
ATOM   433  C  CB  . VAL A 1 57  ? 23.801 23.931 28.806 1.00 33.00  ? 52  VAL A CB  1 
ATOM   434  C  CG1 . VAL A 1 57  ? 23.937 22.758 27.871 1.00 37.83  ? 52  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A 1 57  ? 22.344 24.347 28.832 1.00 38.65  ? 52  VAL A CG2 1 
ATOM   436  N  N   . GLY A 1 58  ? 24.573 21.201 30.607 1.00 30.85  ? 53  GLY A N   1 
ATOM   437  C  CA  . GLY A 1 58  ? 24.251 19.868 31.177 1.00 35.02  ? 53  GLY A CA  1 
ATOM   438  C  C   . GLY A 1 58  ? 24.048 19.924 32.682 1.00 32.45  ? 53  GLY A C   1 
ATOM   439  O  O   . GLY A 1 58  ? 23.009 19.413 33.176 1.00 32.71  ? 53  GLY A O   1 
ATOM   440  N  N   . GLY A 1 59  ? 25.018 20.486 33.409 1.00 33.53  ? 54  GLY A N   1 
ATOM   441  C  CA  . GLY A 1 59  ? 24.954 20.609 34.881 1.00 34.13  ? 54  GLY A CA  1 
ATOM   442  C  C   . GLY A 1 59  ? 23.773 21.482 35.249 1.00 33.09  ? 54  GLY A C   1 
ATOM   443  O  O   . GLY A 1 59  ? 23.079 21.192 36.237 1.00 31.44  ? 54  GLY A O   1 
ATOM   444  N  N   . GLN A 1 60  ? 23.514 22.525 34.460 1.00 31.40  ? 55  GLN A N   1 
ATOM   445  C  CA  . GLN A 1 60  ? 22.383 23.452 34.770 1.00 32.01  ? 55  GLN A CA  1 
ATOM   446  C  C   . GLN A 1 60  ? 21.051 22.734 34.570 1.00 30.56  ? 55  GLN A C   1 
ATOM   447  O  O   . GLN A 1 60  ? 20.174 22.913 35.443 1.00 33.11  ? 55  GLN A O   1 
ATOM   448  C  CB  . GLN A 1 60  ? 22.459 24.685 33.880 1.00 32.59  ? 55  GLN A CB  1 
ATOM   449  C  CG  . GLN A 1 60  ? 23.673 25.527 34.227 1.00 33.59  ? 55  GLN A CG  1 
ATOM   450  C  CD  . GLN A 1 60  ? 23.782 26.659 33.245 1.00 38.01  ? 55  GLN A CD  1 
ATOM   451  O  OE1 . GLN A 1 60  ? 23.555 26.489 32.040 1.00 35.54  ? 55  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A 1 60  ? 24.120 27.824 33.764 1.00 36.32  ? 55  GLN A NE2 1 
ATOM   453  N  N   . ARG A 1 61  ? 20.917 21.973 33.474 1.00 32.39  ? 56  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 61  ? 19.683 21.188 33.188 1.00 31.97  ? 56  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 61  ? 19.473 20.180 34.314 1.00 30.87  ? 56  ARG A C   1 
ATOM   456  O  O   . ARG A 1 61  ? 18.330 20.073 34.808 1.00 30.15  ? 56  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 61  ? 19.727 20.480 31.827 1.00 32.45  ? 56  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 61  ? 19.847 21.415 30.640 1.00 35.15  ? 56  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 61  ? 20.285 20.651 29.404 1.00 38.04  ? 56  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 61  ? 19.208 19.839 28.831 1.00 34.89  ? 56  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 61  ? 19.373 18.734 28.098 1.00 36.61  ? 56  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 61  ? 20.560 18.208 27.861 1.00 35.28  ? 56  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 61  ? 18.316 18.132 27.604 1.00 37.95  ? 56  ARG A NH2 1 
ATOM   464  N  N   . ALA A 1 62  ? 20.513 19.448 34.729 1.00 31.47  ? 57  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 62  ? 20.359 18.438 35.804 1.00 33.63  ? 57  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 62  ? 19.904 19.121 37.106 1.00 33.28  ? 57  ALA A C   1 
ATOM   467  O  O   . ALA A 1 62  ? 19.017 18.597 37.780 1.00 33.71  ? 57  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 62  ? 21.620 17.628 35.998 1.00 32.67  ? 57  ALA A CB  1 
ATOM   469  N  N   . ALA A 1 63  ? 20.509 20.252 37.453 1.00 30.65  ? 58  ALA A N   1 
ATOM   470  C  CA  . ALA A 1 63  ? 20.179 21.046 38.651 1.00 30.80  ? 58  ALA A CA  1 
ATOM   471  C  C   . ALA A 1 63  ? 18.709 21.432 38.563 1.00 30.03  ? 58  ALA A C   1 
ATOM   472  O  O   . ALA A 1 63  ? 17.963 21.224 39.561 1.00 28.67  ? 58  ALA A O   1 
ATOM   473  C  CB  . ALA A 1 63  ? 21.084 22.256 38.752 1.00 30.20  ? 58  ALA A CB  1 
ATOM   474  N  N   . TRP A 1 64  ? 18.310 21.994 37.420 1.00 32.49  ? 59  TRP A N   1 
ATOM   475  C  CA  . TRP A 1 64  ? 16.950 22.554 37.209 1.00 27.89  ? 59  TRP A CA  1 
ATOM   476  C  C   . TRP A 1 64  ? 15.942 21.414 37.383 1.00 33.14  ? 59  TRP A C   1 
ATOM   477  O  O   . TRP A 1 64  ? 14.906 21.639 38.007 1.00 30.13  ? 59  TRP A O   1 
ATOM   478  C  CB  . TRP A 1 64  ? 16.852 23.216 35.825 1.00 32.59  ? 59  TRP A CB  1 
ATOM   479  C  CG  . TRP A 1 64  ? 15.544 23.880 35.555 1.00 34.30  ? 59  TRP A CG  1 
ATOM   480  C  CD1 . TRP A 1 64  ? 15.255 25.195 35.778 1.00 35.84  ? 59  TRP A CD1 1 
ATOM   481  C  CD2 . TRP A 1 64  ? 14.331 23.274 35.078 1.00 34.08  ? 59  TRP A CD2 1 
ATOM   482  N  NE1 . TRP A 1 64  ? 13.965 25.452 35.427 1.00 34.59  ? 59  TRP A NE1 1 
ATOM   483  C  CE2 . TRP A 1 64  ? 13.363 24.297 35.019 1.00 32.83  ? 59  TRP A CE2 1 
ATOM   484  C  CE3 . TRP A 1 64  ? 13.961 21.988 34.695 1.00 35.08  ? 59  TRP A CE3 1 
ATOM   485  C  CZ2 . TRP A 1 64  ? 12.054 24.077 34.607 1.00 35.49  ? 59  TRP A CZ2 1 
ATOM   486  C  CZ3 . TRP A 1 64  ? 12.663 21.762 34.274 1.00 39.16  ? 59  TRP A CZ3 1 
ATOM   487  C  CH2 . TRP A 1 64  ? 11.731 22.805 34.198 1.00 42.38  ? 59  TRP A CH2 1 
ATOM   488  N  N   . ARG A 1 65  ? 16.262 20.218 36.878 1.00 34.29  ? 60  ARG A N   1 
ATOM   489  C  CA  . ARG A 1 65  ? 15.322 19.063 36.925 1.00 35.85  ? 60  ARG A CA  1 
ATOM   490  C  C   . ARG A 1 65  ? 15.146 18.655 38.388 1.00 34.91  ? 60  ARG A C   1 
ATOM   491  O  O   . ARG A 1 65  ? 14.001 18.384 38.795 1.00 35.77  ? 60  ARG A O   1 
ATOM   492  C  CB  . ARG A 1 65  ? 15.801 17.947 35.985 1.00 37.43  ? 60  ARG A CB  1 
ATOM   493  C  CG  . ARG A 1 65  ? 15.846 18.405 34.528 1.00 44.50  ? 60  ARG A CG  1 
ATOM   494  C  CD  . ARG A 1 65  ? 15.675 17.366 33.460 1.00 52.02  ? 60  ARG A CD  1 
ATOM   495  N  NE  . ARG A 1 65  ? 16.925 16.797 33.009 1.00 63.72  ? 60  ARG A NE  1 
ATOM   496  C  CZ  . ARG A 1 65  ? 17.322 16.669 31.742 1.00 58.83  ? 60  ARG A CZ  1 
ATOM   497  N  NH1 . ARG A 1 65  ? 16.595 17.100 30.728 1.00 53.44  ? 60  ARG A NH1 1 
ATOM   498  N  NH2 . ARG A 1 65  ? 18.482 16.097 31.499 1.00 64.26  ? 60  ARG A NH2 1 
ATOM   499  N  N   . VAL A 1 66  ? 16.227 18.653 39.169 1.00 34.56  ? 61  VAL A N   1 
ATOM   500  C  CA  . VAL A 1 66  ? 16.167 18.264 40.607 1.00 34.56  ? 61  VAL A CA  1 
ATOM   501  C  C   . VAL A 1 66  ? 15.242 19.246 41.289 1.00 35.96  ? 61  VAL A C   1 
ATOM   502  O  O   . VAL A 1 66  ? 14.336 18.808 42.021 1.00 36.41  ? 61  VAL A O   1 
ATOM   503  C  CB  . VAL A 1 66  ? 17.560 18.248 41.263 1.00 32.20  ? 61  VAL A CB  1 
ATOM   504  C  CG1 . VAL A 1 66  ? 17.489 18.319 42.774 1.00 33.43  ? 61  VAL A CG1 1 
ATOM   505  C  CG2 . VAL A 1 66  ? 18.350 17.032 40.823 1.00 36.63  ? 61  VAL A CG2 1 
ATOM   506  N  N   . LEU A 1 67  ? 15.487 20.543 41.056 1.00 34.18  ? 62  LEU A N   1 
ATOM   507  C  CA  . LEU A 1 67  ? 14.786 21.622 41.782 1.00 30.79  ? 62  LEU A CA  1 
ATOM   508  C  C   . LEU A 1 67  ? 13.319 21.623 41.351 1.00 35.97  ? 62  LEU A C   1 
ATOM   509  O  O   . LEU A 1 67  ? 12.441 21.745 42.236 1.00 38.19  ? 62  LEU A O   1 
ATOM   510  C  CB  . LEU A 1 67  ? 15.473 22.959 41.497 1.00 32.44  ? 62  LEU A CB  1 
ATOM   511  C  CG  . LEU A 1 67  ? 16.878 23.073 42.075 1.00 34.63  ? 62  LEU A CG  1 
ATOM   512  C  CD1 . LEU A 1 67  ? 17.494 24.416 41.711 1.00 38.20  ? 62  LEU A CD1 1 
ATOM   513  C  CD2 . LEU A 1 67  ? 16.877 22.862 43.585 1.00 33.84  ? 62  LEU A CD2 1 
ATOM   514  N  N   . SER A 1 68  ? 13.064 21.470 40.049 1.00 39.24  ? 63  SER A N   1 
ATOM   515  C  CA  . SER A 1 68  ? 11.689 21.478 39.481 1.00 39.74  ? 63  SER A CA  1 
ATOM   516  C  C   . SER A 1 68  ? 10.872 20.336 40.098 1.00 40.85  ? 63  SER A C   1 
ATOM   517  O  O   . SER A 1 68  ? 9.687  20.528 40.456 1.00 41.29  ? 63  SER A O   1 
ATOM   518  C  CB  . SER A 1 68  ? 11.731 21.401 37.985 1.00 41.64  ? 63  SER A CB  1 
ATOM   519  O  OG  . SER A 1 68  ? 10.441 21.495 37.457 1.00 46.81  ? 63  SER A OG  1 
ATOM   520  N  N   . SER A 1 69  ? 11.478 19.177 40.257 1.00 38.42  ? 64  SER A N   1 
ATOM   521  C  CA  . SER A 1 69  ? 10.780 18.004 40.830 1.00 43.31  ? 64  SER A CA  1 
ATOM   522  C  C   . SER A 1 69  ? 10.450 18.263 42.312 1.00 47.07  ? 64  SER A C   1 
ATOM   523  O  O   . SER A 1 69  ? 9.312  17.942 42.746 1.00 49.23  ? 64  SER A O   1 
ATOM   524  C  CB  . SER A 1 69  ? 11.592 16.771 40.614 1.00 43.72  ? 64  SER A CB  1 
ATOM   525  O  OG  . SER A 1 69  ? 11.082 15.718 41.398 1.00 50.39  ? 64  SER A OG  1 
ATOM   526  N  N   . ILE A 1 70  ? 11.377 18.845 43.077 1.00 41.60  ? 65  ILE A N   1 
ATOM   527  C  CA  . ILE A 1 70  ? 11.118 19.185 44.506 1.00 41.15  ? 65  ILE A CA  1 
ATOM   528  C  C   . ILE A 1 70  ? 9.956  20.169 44.538 1.00 46.94  ? 65  ILE A C   1 
ATOM   529  O  O   . ILE A 1 70  ? 9.079  20.008 45.394 1.00 47.11  ? 65  ILE A O   1 
ATOM   530  C  CB  . ILE A 1 70  ? 12.362 19.743 45.208 1.00 38.22  ? 65  ILE A CB  1 
ATOM   531  C  CG1 . ILE A 1 70  ? 13.421 18.652 45.334 1.00 38.74  ? 65  ILE A CG1 1 
ATOM   532  C  CG2 . ILE A 1 70  ? 11.981 20.333 46.561 1.00 38.86  ? 65  ILE A CG2 1 
ATOM   533  C  CD1 . ILE A 1 70  ? 14.831 19.145 45.397 1.00 38.12  ? 65  ILE A CD1 1 
ATOM   534  N  N   . GLU A 1 71  ? 9.947  21.120 43.602 1.00 44.15  ? 66  GLU A N   1 
ATOM   535  C  CA  . GLU A 1 71  ? 8.941  22.206 43.552 1.00 50.92  ? 66  GLU A CA  1 
ATOM   536  C  C   . GLU A 1 71  ? 7.561  21.602 43.251 1.00 50.79  ? 66  GLU A C   1 
ATOM   537  O  O   . GLU A 1 71  ? 6.592  21.956 43.944 1.00 53.75  ? 66  GLU A O   1 
ATOM   538  C  CB  . GLU A 1 71  ? 9.375  23.256 42.535 1.00 47.20  ? 66  GLU A CB  1 
ATOM   539  C  CG  . GLU A 1 71  ? 8.395  24.385 42.370 1.00 44.89  ? 66  GLU A CG  1 
ATOM   540  C  CD  . GLU A 1 71  ? 8.801  25.388 41.315 1.00 45.45  ? 66  GLU A CD  1 
ATOM   541  O  OE1 . GLU A 1 71  ? 9.707  25.086 40.508 1.00 44.10  ? 66  GLU A OE1 1 
ATOM   542  O  OE2 . GLU A 1 71  ? 8.208  26.477 41.296 1.00 48.41  ? 66  GLU A OE2 1 
ATOM   543  N  N   . GLN A 1 72  ? 7.473  20.722 42.262 1.00 52.33  ? 67  GLN A N   1 
ATOM   544  C  CA  . GLN A 1 72  ? 6.181  20.118 41.849 1.00 57.49  ? 67  GLN A CA  1 
ATOM   545  C  C   . GLN A 1 72  ? 5.666  19.241 42.999 1.00 58.21  ? 67  GLN A C   1 
ATOM   546  O  O   . GLN A 1 72  ? 4.465  19.347 43.307 1.00 58.87  ? 67  GLN A O   1 
ATOM   547  C  CB  . GLN A 1 72  ? 6.335  19.381 40.517 1.00 65.88  ? 67  GLN A CB  1 
ATOM   548  C  CG  . GLN A 1 72  ? 6.216  20.281 39.284 1.00 75.95  ? 67  GLN A CG  1 
ATOM   549  C  CD  . GLN A 1 72  ? 6.358  21.760 39.570 1.00 91.59  ? 67  GLN A CD  1 
ATOM   550  O  OE1 . GLN A 1 72  ? 5.374  22.444 39.870 1.00 91.96  ? 67  GLN A OE1 1 
ATOM   551  N  NE2 . GLN A 1 72  ? 7.588  22.265 39.485 1.00 97.57  ? 67  GLN A NE2 1 
ATOM   552  N  N   . LYS A 1 73  ? 6.534  18.447 43.641 1.00 57.33  ? 68  LYS A N   1 
ATOM   553  C  CA  . LYS A 1 73  ? 6.154  17.590 44.796 1.00 62.57  ? 68  LYS A CA  1 
ATOM   554  C  C   . LYS A 1 73  ? 5.669  18.500 45.938 1.00 71.82  ? 68  LYS A C   1 
ATOM   555  O  O   . LYS A 1 73  ? 4.725  18.103 46.661 1.00 76.91  ? 68  LYS A O   1 
ATOM   556  C  CB  . LYS A 1 73  ? 7.318  16.694 45.238 1.00 58.27  ? 68  LYS A CB  1 
ATOM   557  N  N   . SER A 1 74  ? 6.292  19.672 46.106 1.00 75.28  ? 69  SER A N   1 
ATOM   558  C  CA  . SER A 1 74  ? 5.912  20.656 47.157 1.00 75.83  ? 69  SER A CA  1 
ATOM   559  C  C   . SER A 1 74  ? 4.580  21.313 46.786 1.00 73.17  ? 69  SER A C   1 
ATOM   560  O  O   . SER A 1 74  ? 3.844  21.703 47.702 1.00 67.19  ? 69  SER A O   1 
ATOM   561  C  CB  . SER A 1 74  ? 6.980  21.688 47.390 1.00 79.75  ? 69  SER A CB  1 
ATOM   562  O  OG  . SER A 1 74  ? 6.938  22.692 46.388 1.00 82.11  ? 69  SER A OG  1 
ATOM   563  N  N   . ASN A 1 75  ? 4.247  21.376 45.495 1.00 75.52  ? 70  ASN A N   1 
ATOM   564  C  CA  . ASN A 1 75  ? 2.925  21.890 45.029 1.00 81.67  ? 70  ASN A CA  1 
ATOM   565  C  C   . ASN A 1 75  ? 1.856  20.778 45.109 1.00 85.02  ? 70  ASN A C   1 
ATOM   566  O  O   . ASN A 1 75  ? 0.862  20.865 44.348 1.00 80.94  ? 70  ASN A O   1 
ATOM   567  C  CB  . ASN A 1 75  ? 3.030  22.517 43.632 1.00 76.89  ? 70  ASN A CB  1 
ATOM   568  C  CG  . ASN A 1 75  ? 3.881  23.771 43.613 1.00 80.67  ? 70  ASN A CG  1 
ATOM   569  O  OD1 . ASN A 1 75  ? 4.001  24.460 44.628 1.00 75.56  ? 70  ASN A OD1 1 
ATOM   570  N  ND2 . ASN A 1 75  ? 4.484  24.070 42.470 1.00 86.62  ? 70  ASN A ND2 1 
ATOM   571  N  N   . GLU A 1 76  ? 2.028  19.778 45.990 1.00 87.10  ? 71  GLU A N   1 
ATOM   572  C  CA  . GLU A 1 76  ? 1.046  18.669 46.178 1.00 91.46  ? 71  GLU A CA  1 
ATOM   573  C  C   . GLU A 1 76  ? 0.251  18.849 47.485 1.00 84.53  ? 71  GLU A C   1 
ATOM   574  O  O   . GLU A 1 76  ? 0.840  19.348 48.470 1.00 75.60  ? 71  GLU A O   1 
ATOM   575  C  CB  . GLU A 1 76  ? 1.768  17.322 46.118 1.00 90.90  ? 71  GLU A CB  1 
ATOM   576  C  CG  . GLU A 1 76  ? 2.171  16.950 44.703 1.00 91.49  ? 71  GLU A CG  1 
ATOM   577  C  CD  . GLU A 1 76  ? 2.816  15.585 44.527 1.00 93.03  ? 71  GLU A CD  1 
ATOM   578  O  OE1 . GLU A 1 76  ? 3.115  14.924 45.546 1.00 94.23  ? 71  GLU A OE1 1 
ATOM   579  O  OE2 . GLU A 1 76  ? 3.032  15.194 43.364 1.00 87.35  ? 71  GLU A OE2 1 
ATOM   580  N  N   . LYS A 1 82  ? 4.797  26.045 51.667 1.00 83.28  ? 77  LYS A N   1 
ATOM   581  C  CA  . LYS A 1 82  ? 6.017  25.625 52.415 1.00 81.83  ? 77  LYS A CA  1 
ATOM   582  C  C   . LYS A 1 82  ? 7.160  26.639 52.193 1.00 80.40  ? 77  LYS A C   1 
ATOM   583  O  O   . LYS A 1 82  ? 8.339  26.252 52.432 1.00 80.55  ? 77  LYS A O   1 
ATOM   584  C  CB  . LYS A 1 82  ? 6.421  24.206 51.990 1.00 75.30  ? 77  LYS A CB  1 
ATOM   585  N  N   . GLY A 1 83  ? 6.832  27.877 51.774 1.00 63.33  ? 78  GLY A N   1 
ATOM   586  C  CA  . GLY A 1 83  ? 7.785  28.988 51.549 1.00 53.69  ? 78  GLY A CA  1 
ATOM   587  C  C   . GLY A 1 83  ? 8.150  29.167 50.075 1.00 45.21  ? 78  GLY A C   1 
ATOM   588  O  O   . GLY A 1 83  ? 8.026  28.257 49.258 1.00 43.86  ? 78  GLY A O   1 
ATOM   589  N  N   . PRO A 1 84  ? 8.666  30.352 49.685 1.00 41.50  ? 79  PRO A N   1 
ATOM   590  C  CA  . PRO A 1 84  ? 9.046  30.595 48.301 1.00 35.48  ? 79  PRO A CA  1 
ATOM   591  C  C   . PRO A 1 84  ? 10.450 30.082 47.922 1.00 32.29  ? 79  PRO A C   1 
ATOM   592  O  O   . PRO A 1 84  ? 10.832 30.247 46.798 1.00 32.78  ? 79  PRO A O   1 
ATOM   593  C  CB  . PRO A 1 84  ? 9.023  32.123 48.265 1.00 37.19  ? 79  PRO A CB  1 
ATOM   594  C  CG  . PRO A 1 84  ? 9.596  32.507 49.621 1.00 37.64  ? 79  PRO A CG  1 
ATOM   595  C  CD  . PRO A 1 84  ? 8.987  31.486 50.571 1.00 40.85  ? 79  PRO A CD  1 
ATOM   596  N  N   . GLU A 1 85  ? 11.186 29.482 48.864 1.00 33.54  ? 80  GLU A N   1 
ATOM   597  C  CA  . GLU A 1 85  ? 12.647 29.204 48.695 1.00 30.93  ? 80  GLU A CA  1 
ATOM   598  C  C   . GLU A 1 85  ? 12.882 28.289 47.477 1.00 32.80  ? 80  GLU A C   1 
ATOM   599  O  O   . GLU A 1 85  ? 13.801 28.580 46.688 1.00 32.42  ? 80  GLU A O   1 
ATOM   600  C  CB  . GLU A 1 85  ? 13.254 28.635 49.975 1.00 33.06  ? 80  GLU A CB  1 
ATOM   601  C  CG  . GLU A 1 85  ? 13.356 29.649 51.109 1.00 37.34  ? 80  GLU A CG  1 
ATOM   602  C  CD  . GLU A 1 85  ? 12.105 29.835 51.956 1.00 36.27  ? 80  GLU A CD  1 
ATOM   603  O  OE1 . GLU A 1 85  ? 11.091 29.217 51.628 1.00 37.27  ? 80  GLU A OE1 1 
ATOM   604  O  OE2 . GLU A 1 85  ? 12.166 30.585 52.957 1.00 38.05  ? 80  GLU A OE2 1 
ATOM   605  N  N   . VAL A 1 86  ? 12.126 27.199 47.328 1.00 34.98  ? 81  VAL A N   1 
ATOM   606  C  CA  . VAL A 1 86  ? 12.344 26.226 46.215 1.00 34.87  ? 81  VAL A CA  1 
ATOM   607  C  C   . VAL A 1 86  ? 12.096 26.955 44.893 1.00 35.25  ? 81  VAL A C   1 
ATOM   608  O  O   . VAL A 1 86  ? 12.954 26.836 43.995 1.00 31.58  ? 81  VAL A O   1 
ATOM   609  C  CB  . VAL A 1 86  ? 11.477 24.948 46.302 1.00 38.63  ? 81  VAL A CB  1 
ATOM   610  C  CG1 . VAL A 1 86  ? 11.801 24.011 45.142 1.00 41.44  ? 81  VAL A CG1 1 
ATOM   611  C  CG2 . VAL A 1 86  ? 11.633 24.206 47.622 1.00 42.51  ? 81  VAL A CG2 1 
ATOM   612  N  N   . ARG A 1 87  ? 10.967 27.676 44.760 1.00 35.03  ? 82  ARG A N   1 
ATOM   613  C  CA  . ARG A 1 87  ? 10.647 28.408 43.512 1.00 37.08  ? 82  ARG A CA  1 
ATOM   614  C  C   . ARG A 1 87  ? 11.777 29.416 43.247 1.00 33.11  ? 82  ARG A C   1 
ATOM   615  O  O   . ARG A 1 87  ? 12.245 29.523 42.093 1.00 35.85  ? 82  ARG A O   1 
ATOM   616  C  CB  . ARG A 1 87  ? 9.293  29.133 43.600 1.00 39.89  ? 82  ARG A CB  1 
ATOM   617  C  CG  . ARG A 1 87  ? 8.950  29.918 42.337 1.00 48.59  ? 82  ARG A CG  1 
ATOM   618  C  CD  . ARG A 1 87  ? 7.691  30.776 42.427 1.00 49.39  ? 82  ARG A CD  1 
ATOM   619  N  NE  . ARG A 1 87  ? 7.633  31.533 43.676 1.00 49.76  ? 82  ARG A NE  1 
ATOM   620  C  CZ  . ARG A 1 87  ? 8.321  32.645 43.938 1.00 46.11  ? 82  ARG A CZ  1 
ATOM   621  N  NH1 . ARG A 1 87  ? 9.174  33.141 43.061 1.00 47.00  ? 82  ARG A NH1 1 
ATOM   622  N  NH2 . ARG A 1 87  ? 8.191  33.233 45.114 1.00 49.97  ? 82  ARG A NH2 1 
ATOM   623  N  N   . GLU A 1 88  ? 12.172 30.170 44.269 1.00 32.87  ? 83  GLU A N   1 
ATOM   624  C  CA  . GLU A 1 88  ? 13.198 31.247 44.086 1.00 33.67  ? 83  GLU A CA  1 
ATOM   625  C  C   . GLU A 1 88  ? 14.485 30.622 43.570 1.00 30.90  ? 83  GLU A C   1 
ATOM   626  O  O   . GLU A 1 88  ? 15.090 31.165 42.651 1.00 34.40  ? 83  GLU A O   1 
ATOM   627  C  CB  . GLU A 1 88  ? 13.484 31.996 45.378 1.00 34.75  ? 83  GLU A CB  1 
ATOM   628  C  CG  . GLU A 1 88  ? 12.301 32.825 45.886 1.00 36.42  ? 83  GLU A CG  1 
ATOM   629  C  CD  . GLU A 1 88  ? 12.556 33.401 47.267 1.00 40.01  ? 83  GLU A CD  1 
ATOM   630  O  OE1 . GLU A 1 88  ? 11.888 34.395 47.621 1.00 37.40  ? 83  GLU A OE1 1 
ATOM   631  O  OE2 . GLU A 1 88  ? 13.453 32.868 48.005 1.00 35.96  ? 83  GLU A OE2 1 
ATOM   632  N  N   . TYR A 1 89  ? 14.911 29.515 44.150 1.00 31.22  ? 84  TYR A N   1 
ATOM   633  C  CA  . TYR A 1 89  ? 16.232 28.929 43.791 1.00 32.94  ? 84  TYR A CA  1 
ATOM   634  C  C   . TYR A 1 89  ? 16.116 28.293 42.406 1.00 28.62  ? 84  TYR A C   1 
ATOM   635  O  O   . TYR A 1 89  ? 17.043 28.435 41.589 1.00 32.46  ? 84  TYR A O   1 
ATOM   636  C  CB  . TYR A 1 89  ? 16.738 27.976 44.883 1.00 33.54  ? 84  TYR A CB  1 
ATOM   637  C  CG  . TYR A 1 89  ? 18.108 27.424 44.579 1.00 33.54  ? 84  TYR A CG  1 
ATOM   638  C  CD1 . TYR A 1 89  ? 19.130 28.257 44.139 1.00 33.92  ? 84  TYR A CD1 1 
ATOM   639  C  CD2 . TYR A 1 89  ? 18.380 26.068 44.685 1.00 34.19  ? 84  TYR A CD2 1 
ATOM   640  C  CE1 . TYR A 1 89  ? 20.380 27.761 43.814 1.00 34.08  ? 84  TYR A CE1 1 
ATOM   641  C  CE2 . TYR A 1 89  ? 19.633 25.559 44.379 1.00 31.40  ? 84  TYR A CE2 1 
ATOM   642  C  CZ  . TYR A 1 89  ? 20.629 26.404 43.941 1.00 33.23  ? 84  TYR A CZ  1 
ATOM   643  O  OH  . TYR A 1 89  ? 21.849 25.892 43.619 1.00 35.58  ? 84  TYR A OH  1 
ATOM   644  N  N   . ARG A 1 90  ? 14.988 27.645 42.101 1.00 29.72  ? 85  ARG A N   1 
ATOM   645  C  CA  . ARG A 1 90  ? 14.742 27.073 40.741 1.00 33.75  ? 85  ARG A CA  1 
ATOM   646  C  C   . ARG A 1 90  ? 14.793 28.181 39.686 1.00 32.18  ? 85  ARG A C   1 
ATOM   647  O  O   . ARG A 1 90  ? 15.454 27.965 38.654 1.00 34.11  ? 85  ARG A O   1 
ATOM   648  C  CB  . ARG A 1 90  ? 13.436 26.271 40.644 1.00 36.19  ? 85  ARG A CB  1 
ATOM   649  C  CG  . ARG A 1 90  ? 13.222 25.564 39.301 1.00 37.46  ? 85  ARG A CG  1 
ATOM   650  C  CD  . ARG A 1 90  ? 12.378 26.329 38.282 1.00 38.35  ? 85  ARG A CD  1 
ATOM   651  N  NE  . ARG A 1 90  ? 11.113 26.726 38.889 1.00 38.17  ? 85  ARG A NE  1 
ATOM   652  C  CZ  . ARG A 1 90  ? 10.400 27.808 38.575 1.00 43.83  ? 85  ARG A CZ  1 
ATOM   653  N  NH1 . ARG A 1 90  ? 10.778 28.623 37.606 1.00 41.52  ? 85  ARG A NH1 1 
ATOM   654  N  NH2 . ARG A 1 90  ? 9.291  28.067 39.248 1.00 44.19  ? 85  ARG A NH2 1 
ATOM   655  N  N   . GLU A 1 91  ? 14.199 29.342 39.971 1.00 32.80  ? 86  GLU A N   1 
ATOM   656  C  CA  . GLU A 1 91  ? 14.217 30.541 39.088 1.00 33.87  ? 86  GLU A CA  1 
ATOM   657  C  C   . GLU A 1 91  ? 15.648 31.028 38.889 1.00 31.98  ? 86  GLU A C   1 
ATOM   658  O  O   . GLU A 1 91  ? 15.984 31.377 37.750 1.00 30.81  ? 86  GLU A O   1 
ATOM   659  C  CB  . GLU A 1 91  ? 13.334 31.661 39.644 1.00 38.41  ? 86  GLU A CB  1 
ATOM   660  C  CG  . GLU A 1 91  ? 11.842 31.366 39.528 1.00 41.87  ? 86  GLU A CG  1 
ATOM   661  C  CD  . GLU A 1 91  ? 10.945 32.448 40.118 1.00 50.59  ? 86  GLU A CD  1 
ATOM   662  O  OE1 . GLU A 1 91  ? 9.712  32.302 40.051 1.00 47.63  ? 86  GLU A OE1 1 
ATOM   663  O  OE2 . GLU A 1 91  ? 11.480 33.445 40.635 1.00 57.00  ? 86  GLU A OE2 1 
ATOM   664  N  N   . LYS A 1 92  ? 16.452 31.016 39.947 1.00 32.91  ? 87  LYS A N   1 
ATOM   665  C  CA  . LYS A 1 92  ? 17.860 31.464 39.871 1.00 34.42  ? 87  LYS A CA  1 
ATOM   666  C  C   . LYS A 1 92  ? 18.628 30.551 38.914 1.00 33.04  ? 87  LYS A C   1 
ATOM   667  O  O   . LYS A 1 92  ? 19.421 31.030 38.073 1.00 31.34  ? 87  LYS A O   1 
ATOM   668  C  CB  . LYS A 1 92  ? 18.501 31.432 41.255 1.00 38.64  ? 87  LYS A CB  1 
ATOM   669  C  CG  . LYS A 1 92  ? 19.986 31.758 41.245 1.00 44.45  ? 87  LYS A CG  1 
ATOM   670  C  CD  . LYS A 1 92  ? 20.657 31.568 42.580 1.00 52.67  ? 87  LYS A CD  1 
ATOM   671  C  CE  . LYS A 1 92  ? 22.160 31.731 42.498 1.00 56.55  ? 87  LYS A CE  1 
ATOM   672  N  NZ  . LYS A 1 92  ? 22.683 32.213 43.798 1.00 64.70  ? 87  LYS A NZ  1 
ATOM   673  N  N   . VAL A 1 93  ? 18.448 29.244 39.048 1.00 35.71  ? 88  VAL A N   1 
ATOM   674  C  CA  . VAL A 1 93  ? 19.196 28.287 38.177 1.00 33.98  ? 88  VAL A CA  1 
ATOM   675  C  C   . VAL A 1 93  ? 18.643 28.441 36.745 1.00 31.24  ? 88  VAL A C   1 
ATOM   676  O  O   . VAL A 1 93  ? 19.402 28.450 35.797 1.00 30.58  ? 88  VAL A O   1 
ATOM   677  C  CB  . VAL A 1 93  ? 19.125 26.837 38.701 1.00 35.01  ? 88  VAL A CB  1 
ATOM   678  C  CG1 . VAL A 1 93  ? 19.809 25.874 37.732 1.00 34.39  ? 88  VAL A CG1 1 
ATOM   679  C  CG2 . VAL A 1 93  ? 19.743 26.705 40.080 1.00 33.75  ? 88  VAL A CG2 1 
ATOM   680  N  N   . GLU A 1 94  ? 17.339 28.631 36.607 1.00 35.91  ? 89  GLU A N   1 
ATOM   681  C  CA  . GLU A 1 94  ? 16.662 28.812 35.289 1.00 36.56  ? 89  GLU A CA  1 
ATOM   682  C  C   . GLU A 1 94  ? 17.253 30.027 34.569 1.00 33.86  ? 89  GLU A C   1 
ATOM   683  O  O   . GLU A 1 94  ? 17.595 29.946 33.379 1.00 34.80  ? 89  GLU A O   1 
ATOM   684  C  CB  . GLU A 1 94  ? 15.163 28.968 35.514 1.00 37.06  ? 89  GLU A CB  1 
ATOM   685  C  CG  . GLU A 1 94  ? 14.338 29.069 34.248 1.00 41.22  ? 89  GLU A CG  1 
ATOM   686  C  CD  . GLU A 1 94  ? 12.859 28.856 34.506 1.00 45.88  ? 89  GLU A CD  1 
ATOM   687  O  OE1 . GLU A 1 94  ? 12.506 27.851 35.197 1.00 46.14  ? 89  GLU A OE1 1 
ATOM   688  O  OE2 . GLU A 1 94  ? 12.067 29.689 34.041 1.00 45.27  ? 89  GLU A OE2 1 
ATOM   689  N  N   . THR A 1 95  ? 17.401 31.122 35.287 1.00 35.71  ? 90  THR A N   1 
ATOM   690  C  CA  . THR A 1 95  ? 17.937 32.370 34.705 1.00 36.32  ? 90  THR A CA  1 
ATOM   691  C  C   . THR A 1 95  ? 19.360 32.138 34.188 1.00 37.53  ? 90  THR A C   1 
ATOM   692  O  O   . THR A 1 95  ? 19.670 32.604 33.071 1.00 37.60  ? 90  THR A O   1 
ATOM   693  C  CB  . THR A 1 95  ? 17.798 33.480 35.747 1.00 39.47  ? 90  THR A CB  1 
ATOM   694  O  OG1 . THR A 1 95  ? 16.378 33.560 35.894 1.00 41.58  ? 90  THR A OG1 1 
ATOM   695  C  CG2 . THR A 1 95  ? 18.404 34.783 35.295 1.00 43.61  ? 90  THR A CG2 1 
ATOM   696  N  N   . GLU A 1 96  ? 20.202 31.438 34.951 1.00 33.60  ? 91  GLU A N   1 
ATOM   697  C  CA  . GLU A 1 96  ? 21.599 31.210 34.515 1.00 37.09  ? 91  GLU A CA  1 
ATOM   698  C  C   . GLU A 1 96  ? 21.603 30.326 33.267 1.00 33.87  ? 91  GLU A C   1 
ATOM   699  O  O   . GLU A 1 96  ? 22.473 30.548 32.396 1.00 31.18  ? 91  GLU A O   1 
ATOM   700  C  CB  . GLU A 1 96  ? 22.435 30.573 35.622 1.00 39.10  ? 91  GLU A CB  1 
ATOM   701  C  CG  . GLU A 1 96  ? 22.459 31.446 36.860 1.00 48.56  ? 91  GLU A CG  1 
ATOM   702  C  CD  . GLU A 1 96  ? 23.420 31.007 37.948 1.00 53.53  ? 91  GLU A CD  1 
ATOM   703  O  OE1 . GLU A 1 96  ? 24.209 30.046 37.700 1.00 45.09  ? 91  GLU A OE1 1 
ATOM   704  O  OE2 . GLU A 1 96  ? 23.380 31.644 39.034 1.00 57.32  ? 91  GLU A OE2 1 
ATOM   705  N  N   . LEU A 1 97  ? 20.742 29.306 33.236 1.00 35.07  ? 92  LEU A N   1 
ATOM   706  C  CA  . LEU A 1 97  ? 20.641 28.333 32.115 1.00 35.12  ? 92  LEU A CA  1 
ATOM   707  C  C   . LEU A 1 97  ? 20.250 29.109 30.859 1.00 37.20  ? 92  LEU A C   1 
ATOM   708  O  O   . LEU A 1 97  ? 20.878 28.910 29.817 1.00 35.55  ? 92  LEU A O   1 
ATOM   709  C  CB  . LEU A 1 97  ? 19.598 27.265 32.464 1.00 34.55  ? 92  LEU A CB  1 
ATOM   710  C  CG  . LEU A 1 97  ? 19.397 26.144 31.443 1.00 36.43  ? 92  LEU A CG  1 
ATOM   711  C  CD1 . LEU A 1 97  ? 18.877 24.869 32.127 1.00 38.77  ? 92  LEU A CD1 1 
ATOM   712  C  CD2 . LEU A 1 97  ? 18.436 26.566 30.340 1.00 37.83  ? 92  LEU A CD2 1 
ATOM   713  N  N   . GLN A 1 98  ? 19.272 30.003 30.997 1.00 39.29  ? 93  GLN A N   1 
ATOM   714  C  CA  . GLN A 1 98  ? 18.782 30.823 29.863 1.00 39.07  ? 93  GLN A CA  1 
ATOM   715  C  C   . GLN A 1 98  ? 19.924 31.723 29.391 1.00 37.16  ? 93  GLN A C   1 
ATOM   716  O  O   . GLN A 1 98  ? 20.089 31.858 28.168 1.00 36.39  ? 93  GLN A O   1 
ATOM   717  C  CB  . GLN A 1 98  ? 17.532 31.590 30.289 1.00 41.06  ? 93  GLN A CB  1 
ATOM   718  C  CG  . GLN A 1 98  ? 16.316 30.697 30.457 1.00 38.92  ? 93  GLN A CG  1 
ATOM   719  C  CD  . GLN A 1 98  ? 15.194 31.414 31.169 1.00 38.92  ? 93  GLN A CD  1 
ATOM   720  O  OE1 . GLN A 1 98  ? 15.419 32.255 32.033 1.00 42.86  ? 93  GLN A OE1 1 
ATOM   721  N  NE2 . GLN A 1 98  ? 13.973 31.033 30.867 1.00 42.03  ? 93  GLN A NE2 1 
ATOM   722  N  N   . GLY A 1 99  ? 20.704 32.270 30.326 1.00 38.99  ? 94  GLY A N   1 
ATOM   723  C  CA  . GLY A 1 99  ? 21.896 33.103 30.046 1.00 40.27  ? 94  GLY A CA  1 
ATOM   724  C  C   . GLY A 1 99  ? 22.894 32.378 29.168 1.00 38.69  ? 94  GLY A C   1 
ATOM   725  O  O   . GLY A 1 99  ? 23.460 32.985 28.202 1.00 35.57  ? 94  GLY A O   1 
ATOM   726  N  N   . VAL A 1 100 ? 23.133 31.105 29.475 1.00 33.88  ? 95  VAL A N   1 
ATOM   727  C  CA  . VAL A 1 100 ? 24.163 30.306 28.753 1.00 33.93  ? 95  VAL A CA  1 
ATOM   728  C  C   . VAL A 1 100 ? 23.605 29.969 27.361 1.00 31.88  ? 95  VAL A C   1 
ATOM   729  O  O   . VAL A 1 100 ? 24.324 30.117 26.392 1.00 33.63  ? 95  VAL A O   1 
ATOM   730  C  CB  . VAL A 1 100 ? 24.571 29.056 29.563 1.00 33.08  ? 95  VAL A CB  1 
ATOM   731  C  CG1 . VAL A 1 100 ? 25.337 28.062 28.686 1.00 37.60  ? 95  VAL A CG1 1 
ATOM   732  C  CG2 . VAL A 1 100 ? 25.394 29.455 30.773 1.00 33.91  ? 95  VAL A CG2 1 
ATOM   733  N  N   . CYS A 1 101 ? 22.336 29.576 27.254 1.00 34.46  ? 96  CYS A N   1 
ATOM   734  C  CA  . CYS A 1 101 ? 21.692 29.302 25.948 1.00 37.54  ? 96  CYS A CA  1 
ATOM   735  C  C   . CYS A 1 101 ? 21.651 30.582 25.098 1.00 35.42  ? 96  CYS A C   1 
ATOM   736  O  O   . CYS A 1 101 ? 21.860 30.464 23.857 1.00 35.99  ? 96  CYS A O   1 
ATOM   737  C  CB  . CYS A 1 101 ? 20.272 28.776 26.069 1.00 36.26  ? 96  CYS A CB  1 
ATOM   738  S  SG  . CYS A 1 101 ? 20.171 27.156 26.868 1.00 37.52  ? 96  CYS A SG  1 
ATOM   739  N  N   . ASP A 1 102 ? 21.421 31.743 25.714 1.00 39.78  ? 97  ASP A N   1 
ATOM   740  C  CA  . ASP A 1 102 ? 21.432 33.046 24.985 1.00 40.77  ? 97  ASP A CA  1 
ATOM   741  C  C   . ASP A 1 102 ? 22.839 33.314 24.453 1.00 39.83  ? 97  ASP A C   1 
ATOM   742  O  O   . ASP A 1 102 ? 22.979 33.764 23.282 1.00 44.31  ? 97  ASP A O   1 
ATOM   743  C  CB  . ASP A 1 102 ? 20.916 34.196 25.855 1.00 45.14  ? 97  ASP A CB  1 
ATOM   744  C  CG  . ASP A 1 102 ? 19.412 34.147 26.083 1.00 47.47  ? 97  ASP A CG  1 
ATOM   745  O  OD1 . ASP A 1 102 ? 18.728 33.420 25.324 1.00 56.14  ? 97  ASP A OD1 1 
ATOM   746  O  OD2 . ASP A 1 102 ? 18.943 34.775 27.050 1.00 48.49  ? 97  ASP A OD2 1 
ATOM   747  N  N   . THR A 1 103 ? 23.859 33.057 25.266 1.00 36.56  ? 98  THR A N   1 
ATOM   748  C  CA  . THR A 1 103 ? 25.272 33.262 24.856 1.00 38.35  ? 98  THR A CA  1 
ATOM   749  C  C   . THR A 1 103 ? 25.553 32.400 23.628 1.00 37.40  ? 98  THR A C   1 
ATOM   750  O  O   . THR A 1 103 ? 26.157 32.911 22.659 1.00 33.92  ? 98  THR A O   1 
ATOM   751  C  CB  . THR A 1 103 ? 26.223 33.004 26.029 1.00 35.56  ? 98  THR A CB  1 
ATOM   752  O  OG1 . THR A 1 103 ? 25.889 33.948 27.039 1.00 42.49  ? 98  THR A OG1 1 
ATOM   753  C  CG2 . THR A 1 103 ? 27.676 33.129 25.659 1.00 36.34  ? 98  THR A CG2 1 
ATOM   754  N  N   . VAL A 1 104 ? 25.124 31.133 23.653 1.00 35.94  ? 99  VAL A N   1 
ATOM   755  C  CA  . VAL A 1 104 ? 25.446 30.177 22.561 1.00 33.83  ? 99  VAL A CA  1 
ATOM   756  C  C   . VAL A 1 104 ? 24.709 30.635 21.302 1.00 36.08  ? 99  VAL A C   1 
ATOM   757  O  O   . VAL A 1 104 ? 25.329 30.681 20.238 1.00 31.18  ? 99  VAL A O   1 
ATOM   758  C  CB  . VAL A 1 104 ? 25.113 28.714 22.934 1.00 33.04  ? 99  VAL A CB  1 
ATOM   759  C  CG1 . VAL A 1 104 ? 25.229 27.797 21.733 1.00 32.94  ? 99  VAL A CG1 1 
ATOM   760  C  CG2 . VAL A 1 104 ? 26.027 28.233 24.061 1.00 34.28  ? 99  VAL A CG2 1 
ATOM   761  N  N   . LEU A 1 105 ? 23.425 30.960 21.427 1.00 38.32  ? 100 LEU A N   1 
ATOM   762  C  CA  . LEU A 1 105 ? 22.598 31.342 20.251 1.00 41.48  ? 100 LEU A CA  1 
ATOM   763  C  C   . LEU A 1 105 ? 23.140 32.652 19.652 1.00 42.57  ? 100 LEU A C   1 
ATOM   764  O  O   . LEU A 1 105 ? 23.124 32.770 18.421 1.00 43.97  ? 100 LEU A O   1 
ATOM   765  C  CB  . LEU A 1 105 ? 21.137 31.444 20.675 1.00 41.55  ? 100 LEU A CB  1 
ATOM   766  C  CG  . LEU A 1 105 ? 20.494 30.095 20.985 1.00 38.58  ? 100 LEU A CG  1 
ATOM   767  C  CD1 . LEU A 1 105 ? 19.157 30.295 21.688 1.00 38.22  ? 100 LEU A CD1 1 
ATOM   768  C  CD2 . LEU A 1 105 ? 20.360 29.272 19.720 1.00 41.73  ? 100 LEU A CD2 1 
ATOM   769  N  N   . GLY A 1 106 ? 23.673 33.534 20.501 1.00 44.68  ? 101 GLY A N   1 
ATOM   770  C  CA  . GLY A 1 106 ? 24.320 34.787 20.094 1.00 42.98  ? 101 GLY A CA  1 
ATOM   771  C  C   . GLY A 1 106 ? 25.533 34.503 19.237 1.00 45.62  ? 101 GLY A C   1 
ATOM   772  O  O   . GLY A 1 106 ? 25.689 35.166 18.194 1.00 43.16  ? 101 GLY A O   1 
ATOM   773  N  N   . LEU A 1 107 ? 26.376 33.559 19.667 1.00 40.93  ? 102 LEU A N   1 
ATOM   774  C  CA  . LEU A 1 107 ? 27.635 33.238 18.949 1.00 39.10  ? 102 LEU A CA  1 
ATOM   775  C  C   . LEU A 1 107 ? 27.281 32.653 17.599 1.00 39.78  ? 102 LEU A C   1 
ATOM   776  O  O   . LEU A 1 107 ? 27.967 32.964 16.615 1.00 40.56  ? 102 LEU A O   1 
ATOM   777  C  CB  . LEU A 1 107 ? 28.472 32.229 19.738 1.00 40.67  ? 102 LEU A CB  1 
ATOM   778  C  CG  . LEU A 1 107 ? 29.174 32.771 20.967 1.00 42.28  ? 102 LEU A CG  1 
ATOM   779  C  CD1 . LEU A 1 107 ? 29.789 31.616 21.776 1.00 39.77  ? 102 LEU A CD1 1 
ATOM   780  C  CD2 . LEU A 1 107 ? 30.247 33.799 20.556 1.00 43.62  ? 102 LEU A CD2 1 
ATOM   781  N  N   . LEU A 1 108 ? 26.295 31.760 17.586 1.00 37.62  ? 103 LEU A N   1 
ATOM   782  C  CA  . LEU A 1 108 ? 25.873 31.071 16.353 1.00 36.36  ? 103 LEU A CA  1 
ATOM   783  C  C   . LEU A 1 108 ? 25.395 32.115 15.343 1.00 39.85  ? 103 LEU A C   1 
ATOM   784  O  O   . LEU A 1 108 ? 25.811 32.020 14.178 1.00 42.20  ? 103 LEU A O   1 
ATOM   785  C  CB  . LEU A 1 108 ? 24.760 30.082 16.680 1.00 37.15  ? 103 LEU A CB  1 
ATOM   786  C  CG  . LEU A 1 108 ? 25.220 28.832 17.430 1.00 36.93  ? 103 LEU A CG  1 
ATOM   787  C  CD1 . LEU A 1 108 ? 24.027 28.107 18.017 1.00 38.93  ? 103 LEU A CD1 1 
ATOM   788  C  CD2 . LEU A 1 108 ? 26.002 27.920 16.527 1.00 37.10  ? 103 LEU A CD2 1 
ATOM   789  N  N   . ASP A 1 109 ? 24.538 33.032 15.781 1.00 45.22  ? 104 ASP A N   1 
ATOM   790  C  CA  . ASP A 1 109 ? 23.908 34.056 14.900 1.00 49.49  ? 104 ASP A CA  1 
ATOM   791  C  C   . ASP A 1 109 ? 24.924 35.145 14.542 1.00 46.83  ? 104 ASP A C   1 
ATOM   792  O  O   . ASP A 1 109 ? 24.945 35.520 13.367 1.00 49.73  ? 104 ASP A O   1 
ATOM   793  C  CB  . ASP A 1 109 ? 22.608 34.586 15.509 1.00 55.48  ? 104 ASP A CB  1 
ATOM   794  C  CG  . ASP A 1 109 ? 21.456 33.577 15.489 1.00 63.88  ? 104 ASP A CG  1 
ATOM   795  O  OD1 . ASP A 1 109 ? 21.270 32.848 14.463 1.00 62.33  ? 104 ASP A OD1 1 
ATOM   796  O  OD2 . ASP A 1 109 ? 20.757 33.490 16.511 1.00 77.55  ? 104 ASP A OD2 1 
ATOM   797  N  N   . SER A 1 110 ? 25.755 35.607 15.477 1.00 47.73  ? 105 SER A N   1 
ATOM   798  C  CA  . SER A 1 110 ? 26.736 36.702 15.237 1.00 48.40  ? 105 SER A CA  1 
ATOM   799  C  C   . SER A 1 110 ? 27.962 36.213 14.462 1.00 49.75  ? 105 SER A C   1 
ATOM   800  O  O   . SER A 1 110 ? 28.586 37.040 13.774 1.00 43.88  ? 105 SER A O   1 
ATOM   801  C  CB  . SER A 1 110 ? 27.169 37.368 16.510 1.00 48.60  ? 105 SER A CB  1 
ATOM   802  O  OG  . SER A 1 110 ? 26.064 37.959 17.175 1.00 52.13  ? 105 SER A OG  1 
ATOM   803  N  N   . HIS A 1 111 ? 28.354 34.943 14.566 1.00 41.90  ? 106 HIS A N   1 
ATOM   804  C  CA  . HIS A 1 111 ? 29.700 34.563 14.071 1.00 40.21  ? 106 HIS A CA  1 
ATOM   805  C  C   . HIS A 1 111 ? 29.721 33.280 13.237 1.00 43.25  ? 106 HIS A C   1 
ATOM   806  O  O   . HIS A 1 111 ? 30.449 33.258 12.219 1.00 46.78  ? 106 HIS A O   1 
ATOM   807  C  CB  . HIS A 1 111 ? 30.629 34.468 15.274 1.00 43.83  ? 106 HIS A CB  1 
ATOM   808  C  CG  . HIS A 1 111 ? 31.031 35.791 15.822 1.00 50.26  ? 106 HIS A CG  1 
ATOM   809  N  ND1 . HIS A 1 111 ? 30.555 36.258 17.028 1.00 55.50  ? 106 HIS A ND1 1 
ATOM   810  C  CD2 . HIS A 1 111 ? 31.893 36.723 15.357 1.00 52.21  ? 106 HIS A CD2 1 
ATOM   811  C  CE1 . HIS A 1 111 ? 31.125 37.418 17.299 1.00 57.21  ? 106 HIS A CE1 1 
ATOM   812  N  NE2 . HIS A 1 111 ? 31.940 37.732 16.275 1.00 50.19  ? 106 HIS A NE2 1 
ATOM   813  N  N   . LEU A 1 112 ? 29.011 32.228 13.647 1.00 40.92  ? 107 LEU A N   1 
ATOM   814  C  CA  . LEU A 1 112 ? 29.298 30.853 13.145 1.00 36.24  ? 107 LEU A CA  1 
ATOM   815  C  C   . LEU A 1 112 ? 28.380 30.475 11.977 1.00 38.86  ? 107 LEU A C   1 
ATOM   816  O  O   . LEU A 1 112 ? 28.875 29.850 11.029 1.00 40.47  ? 107 LEU A O   1 
ATOM   817  C  CB  . LEU A 1 112 ? 29.151 29.871 14.316 1.00 36.47  ? 107 LEU A CB  1 
ATOM   818  C  CG  . LEU A 1 112 ? 30.193 30.073 15.416 1.00 36.10  ? 107 LEU A CG  1 
ATOM   819  C  CD1 . LEU A 1 112 ? 29.824 29.342 16.692 1.00 36.31  ? 107 LEU A CD1 1 
ATOM   820  C  CD2 . LEU A 1 112 ? 31.569 29.657 14.930 1.00 35.54  ? 107 LEU A CD2 1 
ATOM   821  N  N   . ILE A 1 113 ? 27.082 30.771 12.058 1.00 38.15  ? 108 ILE A N   1 
ATOM   822  C  CA  . ILE A 1 113 ? 26.094 30.363 11.021 1.00 42.32  ? 108 ILE A CA  1 
ATOM   823  C  C   . ILE A 1 113 ? 26.290 31.264 9.779  1.00 49.83  ? 108 ILE A C   1 
ATOM   824  O  O   . ILE A 1 113 ? 26.123 32.499 9.878  1.00 47.93  ? 108 ILE A O   1 
ATOM   825  C  CB  . ILE A 1 113 ? 24.646 30.386 11.553 1.00 43.58  ? 108 ILE A CB  1 
ATOM   826  C  CG1 . ILE A 1 113 ? 24.458 29.372 12.690 1.00 44.81  ? 108 ILE A CG1 1 
ATOM   827  C  CG2 . ILE A 1 113 ? 23.665 30.121 10.419 1.00 43.44  ? 108 ILE A CG2 1 
ATOM   828  C  CD1 . ILE A 1 113 ? 23.047 29.286 13.225 1.00 43.91  ? 108 ILE A CD1 1 
ATOM   829  N  N   . LYS A 1 114 ? 26.666 30.666 8.656  1.00 53.25  ? 109 LYS A N   1 
ATOM   830  C  CA  . LYS A 1 114 ? 26.932 31.388 7.380  1.00 62.05  ? 109 LYS A CA  1 
ATOM   831  C  C   . LYS A 1 114 ? 26.261 30.628 6.221  1.00 61.93  ? 109 LYS A C   1 
ATOM   832  O  O   . LYS A 1 114 ? 26.072 29.396 6.341  1.00 58.78  ? 109 LYS A O   1 
ATOM   833  C  CB  . LYS A 1 114 ? 28.446 31.554 7.199  1.00 57.18  ? 109 LYS A CB  1 
ATOM   834  C  CG  . LYS A 1 114 ? 29.117 32.488 8.193  1.00 62.31  ? 109 LYS A CG  1 
ATOM   835  C  CD  . LYS A 1 114 ? 30.624 32.285 8.272  1.00 68.53  ? 109 LYS A CD  1 
ATOM   836  C  CE  . LYS A 1 114 ? 31.442 33.508 8.651  1.00 66.45  ? 109 LYS A CE  1 
ATOM   837  N  NZ  . LYS A 1 114 ? 30.724 34.426 9.563  1.00 70.38  ? 109 LYS A NZ  1 
ATOM   838  N  N   . GLU A 1 115 ? 25.902 31.348 5.146  1.00 64.42  ? 110 GLU A N   1 
ATOM   839  C  CA  . GLU A 1 115 ? 25.383 30.807 3.853  1.00 59.49  ? 110 GLU A CA  1 
ATOM   840  C  C   . GLU A 1 115 ? 26.473 29.940 3.215  1.00 54.51  ? 110 GLU A C   1 
ATOM   841  O  O   . GLU A 1 115 ? 26.167 28.846 2.729  1.00 66.50  ? 110 GLU A O   1 
ATOM   842  C  CB  . GLU A 1 115 ? 24.976 31.958 2.919  1.00 54.41  ? 110 GLU A CB  1 
ATOM   843  N  N   . ALA A 1 116 ? 27.713 30.412 3.268  1.00 61.87  ? 111 ALA A N   1 
ATOM   844  C  CA  . ALA A 1 116 ? 28.922 29.709 2.793  1.00 66.58  ? 111 ALA A CA  1 
ATOM   845  C  C   . ALA A 1 116 ? 29.336 28.643 3.817  1.00 68.24  ? 111 ALA A C   1 
ATOM   846  O  O   . ALA A 1 116 ? 28.599 28.423 4.809  1.00 65.98  ? 111 ALA A O   1 
ATOM   847  C  CB  . ALA A 1 116 ? 30.024 30.720 2.569  1.00 71.04  ? 111 ALA A CB  1 
ATOM   848  N  N   . GLY A 1 117 ? 30.486 28.009 3.568  1.00 67.22  ? 112 GLY A N   1 
ATOM   849  C  CA  . GLY A 1 117 ? 31.112 26.989 4.430  1.00 64.42  ? 112 GLY A CA  1 
ATOM   850  C  C   . GLY A 1 117 ? 30.802 25.594 3.929  1.00 55.35  ? 112 GLY A C   1 
ATOM   851  O  O   . GLY A 1 117 ? 29.883 25.450 3.102  1.00 50.60  ? 112 GLY A O   1 
ATOM   852  N  N   . ASP A 1 118 ? 31.503 24.575 4.424  1.00 54.75  ? 113 ASP A N   1 
ATOM   853  C  CA  . ASP A 1 118 ? 31.197 23.169 4.040  1.00 53.90  ? 113 ASP A CA  1 
ATOM   854  C  C   . ASP A 1 118 ? 29.882 22.719 4.708  1.00 49.20  ? 113 ASP A C   1 
ATOM   855  O  O   . ASP A 1 118 ? 29.382 23.402 5.625  1.00 44.82  ? 113 ASP A O   1 
ATOM   856  C  CB  . ASP A 1 118 ? 32.362 22.234 4.344  1.00 57.25  ? 113 ASP A CB  1 
ATOM   857  C  CG  . ASP A 1 118 ? 32.802 22.238 5.797  1.00 62.39  ? 113 ASP A CG  1 
ATOM   858  O  OD1 . ASP A 1 118 ? 32.112 22.862 6.645  1.00 57.58  ? 113 ASP A OD1 1 
ATOM   859  O  OD2 . ASP A 1 118 ? 33.852 21.631 6.057  1.00 64.77  ? 113 ASP A OD2 1 
ATOM   860  N  N   . ALA A 1 119 ? 29.331 21.611 4.237  1.00 47.39  ? 114 ALA A N   1 
ATOM   861  C  CA  . ALA A 1 119 ? 28.079 21.010 4.740  1.00 53.13  ? 114 ALA A CA  1 
ATOM   862  C  C   . ALA A 1 119 ? 28.244 20.676 6.225  1.00 45.84  ? 114 ALA A C   1 
ATOM   863  O  O   . ALA A 1 119 ? 27.338 21.012 7.005  1.00 48.76  ? 114 ALA A O   1 
ATOM   864  C  CB  . ALA A 1 119 ? 27.728 19.778 3.931  1.00 56.34  ? 114 ALA A CB  1 
ATOM   865  N  N   . GLU A 1 120 ? 29.353 20.049 6.600  1.00 42.46  ? 115 GLU A N   1 
ATOM   866  C  CA  . GLU A 1 120 ? 29.586 19.656 8.009  1.00 47.82  ? 115 GLU A CA  1 
ATOM   867  C  C   . GLU A 1 120 ? 29.368 20.858 8.913  1.00 45.50  ? 115 GLU A C   1 
ATOM   868  O  O   . GLU A 1 120 ? 28.594 20.719 9.898  1.00 41.21  ? 115 GLU A O   1 
ATOM   869  C  CB  . GLU A 1 120 ? 30.967 19.049 8.241  1.00 49.06  ? 115 GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 120 ? 31.107 17.682 7.613  1.00 53.71  ? 115 GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 120 ? 32.129 16.786 8.291  1.00 59.54  ? 115 GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 120 ? 31.730 15.675 8.729  1.00 63.97  ? 115 GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 120 ? 33.309 17.195 8.372  1.00 53.39  ? 115 GLU A OE2 1 
ATOM   874  N  N   . SER A 1 121 ? 30.038 21.974 8.624  1.00 44.92  ? 116 SER A N   1 
ATOM   875  C  CA  . SER A 1 121 ? 29.969 23.185 9.477  1.00 43.89  ? 116 SER A CA  1 
ATOM   876  C  C   . SER A 1 121 ? 28.531 23.696 9.476  1.00 39.89  ? 116 SER A C   1 
ATOM   877  O  O   . SER A 1 121 ? 27.989 23.982 10.552 1.00 40.05  ? 116 SER A O   1 
ATOM   878  C  CB  . SER A 1 121 ? 30.942 24.254 9.053  1.00 50.55  ? 116 SER A CB  1 
ATOM   879  O  OG  . SER A 1 121 ? 30.609 24.755 7.770  1.00 58.72  ? 116 SER A OG  1 
ATOM   880  N  N   . ARG A 1 122 ? 27.911 23.787 8.301  1.00 38.10  ? 117 ARG A N   1 
ATOM   881  C  CA  . ARG A 1 122 ? 26.547 24.385 8.221  1.00 41.17  ? 117 ARG A CA  1 
ATOM   882  C  C   . ARG A 1 122 ? 25.541 23.537 9.013  1.00 35.21  ? 117 ARG A C   1 
ATOM   883  O  O   . ARG A 1 122 ? 24.658 24.125 9.728  1.00 33.87  ? 117 ARG A O   1 
ATOM   884  C  CB  . ARG A 1 122 ? 26.130 24.550 6.759  1.00 42.82  ? 117 ARG A CB  1 
ATOM   885  C  CG  . ARG A 1 122 ? 26.674 25.841 6.165  1.00 47.51  ? 117 ARG A CG  1 
ATOM   886  C  CD  . ARG A 1 122 ? 26.385 26.062 4.696  1.00 45.56  ? 117 ARG A CD  1 
ATOM   887  N  NE  . ARG A 1 122 ? 27.062 25.072 3.873  1.00 49.72  ? 117 ARG A NE  1 
ATOM   888  C  CZ  . ARG A 1 122 ? 26.441 24.110 3.192  1.00 50.74  ? 117 ARG A CZ  1 
ATOM   889  N  NH1 . ARG A 1 122 ? 25.119 24.036 3.210  1.00 54.44  ? 117 ARG A NH1 1 
ATOM   890  N  NH2 . ARG A 1 122 ? 27.133 23.239 2.477  1.00 51.00  ? 117 ARG A NH2 1 
ATOM   891  N  N   . VAL A 1 123 ? 25.652 22.223 8.886  1.00 36.05  ? 118 VAL A N   1 
ATOM   892  C  CA  . VAL A 1 123 ? 24.696 21.285 9.537  1.00 37.20  ? 118 VAL A CA  1 
ATOM   893  C  C   . VAL A 1 123 ? 24.983 21.355 11.049 1.00 36.55  ? 118 VAL A C   1 
ATOM   894  O  O   . VAL A 1 123 ? 24.029 21.461 11.847 1.00 34.57  ? 118 VAL A O   1 
ATOM   895  C  CB  . VAL A 1 123 ? 24.793 19.857 8.966  1.00 38.33  ? 118 VAL A CB  1 
ATOM   896  C  CG1 . VAL A 1 123 ? 23.930 18.900 9.757  1.00 36.98  ? 118 VAL A CG1 1 
ATOM   897  C  CG2 . VAL A 1 123 ? 24.403 19.794 7.479  1.00 39.12  ? 118 VAL A CG2 1 
ATOM   898  N  N   . PHE A 1 124 ? 26.257 21.359 11.422 1.00 33.92  ? 119 PHE A N   1 
ATOM   899  C  CA  . PHE A 1 124 ? 26.636 21.292 12.853 1.00 35.86  ? 119 PHE A CA  1 
ATOM   900  C  C   . PHE A 1 124 ? 26.058 22.506 13.562 1.00 36.86  ? 119 PHE A C   1 
ATOM   901  O  O   . PHE A 1 124 ? 25.385 22.342 14.638 1.00 36.37  ? 119 PHE A O   1 
ATOM   902  C  CB  . PHE A 1 124 ? 28.143 21.169 13.070 1.00 35.38  ? 119 PHE A CB  1 
ATOM   903  C  CG  . PHE A 1 124 ? 28.452 21.377 14.527 1.00 37.49  ? 119 PHE A CG  1 
ATOM   904  C  CD1 . PHE A 1 124 ? 28.222 20.357 15.444 1.00 37.89  ? 119 PHE A CD1 1 
ATOM   905  C  CD2 . PHE A 1 124 ? 28.870 22.618 14.997 1.00 38.30  ? 119 PHE A CD2 1 
ATOM   906  C  CE1 . PHE A 1 124 ? 28.422 20.578 16.804 1.00 39.82  ? 119 PHE A CE1 1 
ATOM   907  C  CE2 . PHE A 1 124 ? 29.094 22.830 16.349 1.00 41.43  ? 119 PHE A CE2 1 
ATOM   908  C  CZ  . PHE A 1 124 ? 28.871 21.807 17.250 1.00 40.59  ? 119 PHE A CZ  1 
ATOM   909  N  N   . TYR A 1 125 ? 26.270 23.706 12.994 1.00 33.44  ? 120 TYR A N   1 
ATOM   910  C  CA  . TYR A 1 125 ? 25.828 24.961 13.642 1.00 32.92  ? 120 TYR A CA  1 
ATOM   911  C  C   . TYR A 1 125 ? 24.311 24.997 13.725 1.00 33.32  ? 120 TYR A C   1 
ATOM   912  O  O   . TYR A 1 125 ? 23.786 25.437 14.772 1.00 35.99  ? 120 TYR A O   1 
ATOM   913  C  CB  . TYR A 1 125 ? 26.457 26.191 12.997 1.00 34.13  ? 120 TYR A CB  1 
ATOM   914  C  CG  . TYR A 1 125 ? 27.955 26.238 13.162 1.00 35.08  ? 120 TYR A CG  1 
ATOM   915  C  CD1 . TYR A 1 125 ? 28.558 26.103 14.413 1.00 34.64  ? 120 TYR A CD1 1 
ATOM   916  C  CD2 . TYR A 1 125 ? 28.762 26.475 12.074 1.00 36.53  ? 120 TYR A CD2 1 
ATOM   917  C  CE1 . TYR A 1 125 ? 29.937 26.158 14.556 1.00 33.61  ? 120 TYR A CE1 1 
ATOM   918  C  CE2 . TYR A 1 125 ? 30.129 26.586 12.214 1.00 38.74  ? 120 TYR A CE2 1 
ATOM   919  C  CZ  . TYR A 1 125 ? 30.718 26.413 13.445 1.00 36.19  ? 120 TYR A CZ  1 
ATOM   920  O  OH  . TYR A 1 125 ? 32.077 26.499 13.481 1.00 37.71  ? 120 TYR A OH  1 
ATOM   921  N  N   . LEU A 1 126 ? 23.615 24.534 12.690 1.00 36.66  ? 121 LEU A N   1 
ATOM   922  C  CA  . LEU A 1 126 ? 22.135 24.603 12.697 1.00 36.58  ? 121 LEU A CA  1 
ATOM   923  C  C   . LEU A 1 126 ? 21.596 23.588 13.711 1.00 34.53  ? 121 LEU A C   1 
ATOM   924  O  O   . LEU A 1 126 ? 20.614 23.924 14.377 1.00 37.69  ? 121 LEU A O   1 
ATOM   925  C  CB  . LEU A 1 126 ? 21.600 24.372 11.275 1.00 37.32  ? 121 LEU A CB  1 
ATOM   926  C  CG  . LEU A 1 126 ? 21.733 25.579 10.341 1.00 37.71  ? 121 LEU A CG  1 
ATOM   927  C  CD1 . LEU A 1 126 ? 21.401 25.210 8.899  1.00 40.33  ? 121 LEU A CD1 1 
ATOM   928  C  CD2 . LEU A 1 126 ? 20.870 26.723 10.828 1.00 39.23  ? 121 LEU A CD2 1 
ATOM   929  N  N   . LYS A 1 127 ? 22.197 22.404 13.785 1.00 35.07  ? 122 LYS A N   1 
ATOM   930  C  CA  . LYS A 1 127 ? 21.910 21.380 14.834 1.00 36.00  ? 122 LYS A CA  1 
ATOM   931  C  C   . LYS A 1 127 ? 22.094 22.041 16.203 1.00 35.63  ? 122 LYS A C   1 
ATOM   932  O  O   . LYS A 1 127 ? 21.217 21.908 17.038 1.00 34.94  ? 122 LYS A O   1 
ATOM   933  C  CB  . LYS A 1 127 ? 22.823 20.157 14.713 1.00 33.07  ? 122 LYS A CB  1 
ATOM   934  C  CG  . LYS A 1 127 ? 22.741 19.191 15.900 1.00 31.44  ? 122 LYS A CG  1 
ATOM   935  C  CD  . LYS A 1 127 ? 23.751 18.094 15.827 1.00 32.06  ? 122 LYS A CD  1 
ATOM   936  C  CE  . LYS A 1 127 ? 23.866 17.308 17.125 1.00 36.93  ? 122 LYS A CE  1 
ATOM   937  N  NZ  . LYS A 1 127 ? 24.186 18.177 18.287 1.00 32.97  ? 122 LYS A NZ  1 
ATOM   938  N  N   . MET A 1 128 ? 23.205 22.755 16.404 1.00 35.29  ? 123 MET A N   1 
ATOM   939  C  CA  . MET A 1 128 ? 23.507 23.409 17.697 1.00 32.71  ? 123 MET A CA  1 
ATOM   940  C  C   . MET A 1 128 ? 22.450 24.467 18.001 1.00 36.53  ? 123 MET A C   1 
ATOM   941  O  O   . MET A 1 128 ? 22.029 24.597 19.184 1.00 34.57  ? 123 MET A O   1 
ATOM   942  C  CB  . MET A 1 128 ? 24.895 24.052 17.694 1.00 34.27  ? 123 MET A CB  1 
ATOM   943  C  CG  . MET A 1 128 ? 25.426 24.335 19.084 1.00 33.30  ? 123 MET A CG  1 
ATOM   944  S  SD  . MET A 1 128 ? 27.085 25.069 18.987 1.00 37.89  ? 123 MET A SD  1 
ATOM   945  C  CE  . MET A 1 128 ? 27.587 24.945 20.704 1.00 41.04  ? 123 MET A CE  1 
ATOM   946  N  N   . LYS A 1 129 ? 21.984 25.192 16.978 1.00 38.00  ? 124 LYS A N   1 
ATOM   947  C  CA  . LYS A 1 129 ? 20.913 26.194 17.191 1.00 35.92  ? 124 LYS A CA  1 
ATOM   948  C  C   . LYS A 1 129 ? 19.636 25.490 17.664 1.00 32.80  ? 124 LYS A C   1 
ATOM   949  O  O   . LYS A 1 129 ? 19.003 25.971 18.641 1.00 35.45  ? 124 LYS A O   1 
ATOM   950  C  CB  . LYS A 1 129 ? 20.648 26.978 15.911 1.00 37.36  ? 124 LYS A CB  1 
ATOM   951  C  CG  . LYS A 1 129 ? 19.679 28.131 16.085 1.00 42.39  ? 124 LYS A CG  1 
ATOM   952  C  CD  . LYS A 1 129 ? 19.661 28.993 14.823 1.00 45.76  ? 124 LYS A CD  1 
ATOM   953  C  CE  . LYS A 1 129 ? 18.403 29.804 14.627 1.00 45.95  ? 124 LYS A CE  1 
ATOM   954  N  NZ  . LYS A 1 129 ? 18.798 31.180 14.249 1.00 54.60  ? 124 LYS A NZ  1 
ATOM   955  N  N   . GLY A 1 130 ? 19.258 24.404 17.005 1.00 33.35  ? 125 GLY A N   1 
ATOM   956  C  CA  . GLY A 1 130 ? 18.110 23.590 17.453 1.00 38.09  ? 125 GLY A CA  1 
ATOM   957  C  C   . GLY A 1 130 ? 18.258 23.140 18.904 1.00 34.47  ? 125 GLY A C   1 
ATOM   958  O  O   . GLY A 1 130 ? 17.307 23.271 19.673 1.00 34.86  ? 125 GLY A O   1 
ATOM   959  N  N   . ASP A 1 131 ? 19.414 22.586 19.258 1.00 34.48  ? 126 ASP A N   1 
ATOM   960  C  CA  . ASP A 1 131 ? 19.644 22.052 20.629 1.00 34.59  ? 126 ASP A CA  1 
ATOM   961  C  C   . ASP A 1 131 ? 19.444 23.164 21.679 1.00 33.90  ? 126 ASP A C   1 
ATOM   962  O  O   . ASP A 1 131 ? 18.754 22.923 22.681 1.00 38.07  ? 126 ASP A O   1 
ATOM   963  C  CB  . ASP A 1 131 ? 21.007 21.383 20.721 1.00 33.85  ? 126 ASP A CB  1 
ATOM   964  C  CG  . ASP A 1 131 ? 21.179 20.141 19.885 1.00 33.29  ? 126 ASP A CG  1 
ATOM   965  O  OD1 . ASP A 1 131 ? 20.162 19.533 19.508 1.00 34.29  ? 126 ASP A OD1 1 
ATOM   966  O  OD2 . ASP A 1 131 ? 22.341 19.790 19.594 1.00 37.03  ? 126 ASP A OD2 1 
ATOM   967  N  N   . TYR A 1 132 ? 20.019 24.349 21.491 1.00 34.42  ? 127 TYR A N   1 
ATOM   968  C  CA  . TYR A 1 132 ? 19.997 25.409 22.540 1.00 35.05  ? 127 TYR A CA  1 
ATOM   969  C  C   . TYR A 1 132 ? 18.616 26.078 22.580 1.00 36.21  ? 127 TYR A C   1 
ATOM   970  O  O   . TYR A 1 132 ? 18.206 26.488 23.669 1.00 40.13  ? 127 TYR A O   1 
ATOM   971  C  CB  . TYR A 1 132 ? 21.229 26.309 22.424 1.00 32.75  ? 127 TYR A CB  1 
ATOM   972  C  CG  . TYR A 1 132 ? 22.440 25.626 22.988 1.00 31.45  ? 127 TYR A CG  1 
ATOM   973  C  CD1 . TYR A 1 132 ? 23.183 24.761 22.215 1.00 29.43  ? 127 TYR A CD1 1 
ATOM   974  C  CD2 . TYR A 1 132 ? 22.787 25.764 24.326 1.00 32.28  ? 127 TYR A CD2 1 
ATOM   975  C  CE1 . TYR A 1 132 ? 24.274 24.083 22.728 1.00 31.48  ? 127 TYR A CE1 1 
ATOM   976  C  CE2 . TYR A 1 132 ? 23.884 25.093 24.857 1.00 32.77  ? 127 TYR A CE2 1 
ATOM   977  C  CZ  . TYR A 1 132 ? 24.609 24.225 24.062 1.00 33.10  ? 127 TYR A CZ  1 
ATOM   978  O  OH  . TYR A 1 132 ? 25.681 23.529 24.557 1.00 28.78  ? 127 TYR A OH  1 
ATOM   979  N  N   . TYR A 1 133 ? 17.850 26.032 21.492 1.00 36.03  ? 128 TYR A N   1 
ATOM   980  C  CA  . TYR A 1 133 ? 16.438 26.482 21.506 1.00 37.46  ? 128 TYR A CA  1 
ATOM   981  C  C   . TYR A 1 133 ? 15.637 25.418 22.275 1.00 36.87  ? 128 TYR A C   1 
ATOM   982  O  O   . TYR A 1 133 ? 14.815 25.784 23.112 1.00 44.21  ? 128 TYR A O   1 
ATOM   983  C  CB  . TYR A 1 133 ? 15.953 26.786 20.074 1.00 38.27  ? 128 TYR A CB  1 
ATOM   984  C  CG  . TYR A 1 133 ? 16.149 28.226 19.662 1.00 40.59  ? 128 TYR A CG  1 
ATOM   985  C  CD1 . TYR A 1 133 ? 15.592 29.254 20.402 1.00 42.08  ? 128 TYR A CD1 1 
ATOM   986  C  CD2 . TYR A 1 133 ? 16.892 28.571 18.540 1.00 44.01  ? 128 TYR A CD2 1 
ATOM   987  C  CE1 . TYR A 1 133 ? 15.748 30.579 20.036 1.00 45.94  ? 128 TYR A CE1 1 
ATOM   988  C  CE2 . TYR A 1 133 ? 17.077 29.892 18.162 1.00 39.86  ? 128 TYR A CE2 1 
ATOM   989  C  CZ  . TYR A 1 133 ? 16.479 30.895 18.904 1.00 45.05  ? 128 TYR A CZ  1 
ATOM   990  O  OH  . TYR A 1 133 ? 16.663 32.202 18.590 1.00 48.21  ? 128 TYR A OH  1 
ATOM   991  N  N   . ARG A 1 134 ? 15.958 24.146 22.068 1.00 37.09  ? 129 ARG A N   1 
ATOM   992  C  CA  . ARG A 1 134 ? 15.323 23.008 22.761 1.00 37.80  ? 129 ARG A CA  1 
ATOM   993  C  C   . ARG A 1 134 ? 15.574 23.135 24.283 1.00 38.69  ? 129 ARG A C   1 
ATOM   994  O  O   . ARG A 1 134 ? 14.650 22.866 25.078 1.00 37.70  ? 129 ARG A O   1 
ATOM   995  C  CB  . ARG A 1 134 ? 15.856 21.685 22.206 1.00 36.88  ? 129 ARG A CB  1 
ATOM   996  C  CG  . ARG A 1 134 ? 15.340 20.472 22.973 1.00 35.89  ? 129 ARG A CG  1 
ATOM   997  C  CD  . ARG A 1 134 ? 15.322 19.177 22.192 1.00 38.45  ? 129 ARG A CD  1 
ATOM   998  N  NE  . ARG A 1 134 ? 16.662 18.843 21.739 1.00 37.47  ? 129 ARG A NE  1 
ATOM   999  C  CZ  . ARG A 1 134 ? 17.559 18.178 22.441 1.00 34.97  ? 129 ARG A CZ  1 
ATOM   1000 N  NH1 . ARG A 1 134 ? 17.224 17.717 23.621 1.00 38.87  ? 129 ARG A NH1 1 
ATOM   1001 N  NH2 . ARG A 1 134 ? 18.768 17.922 21.952 1.00 35.49  ? 129 ARG A NH2 1 
ATOM   1002 N  N   . TYR A 1 135 ? 16.781 23.528 24.702 1.00 39.81  ? 130 TYR A N   1 
ATOM   1003 C  CA  . TYR A 1 135 ? 17.108 23.645 26.157 1.00 37.31  ? 130 TYR A CA  1 
ATOM   1004 C  C   . TYR A 1 135 ? 16.293 24.791 26.751 1.00 35.55  ? 130 TYR A C   1 
ATOM   1005 O  O   . TYR A 1 135 ? 15.733 24.593 27.834 1.00 38.64  ? 130 TYR A O   1 
ATOM   1006 C  CB  . TYR A 1 135 ? 18.621 23.725 26.399 1.00 36.65  ? 130 TYR A CB  1 
ATOM   1007 C  CG  . TYR A 1 135 ? 19.430 22.604 25.779 1.00 35.37  ? 130 TYR A CG  1 
ATOM   1008 C  CD1 . TYR A 1 135 ? 18.909 21.327 25.605 1.00 39.08  ? 130 TYR A CD1 1 
ATOM   1009 C  CD2 . TYR A 1 135 ? 20.726 22.821 25.328 1.00 32.97  ? 130 TYR A CD2 1 
ATOM   1010 C  CE1 . TYR A 1 135 ? 19.677 20.298 25.064 1.00 33.73  ? 130 TYR A CE1 1 
ATOM   1011 C  CE2 . TYR A 1 135 ? 21.496 21.804 24.782 1.00 33.96  ? 130 TYR A CE2 1 
ATOM   1012 C  CZ  . TYR A 1 135 ? 20.975 20.529 24.639 1.00 36.84  ? 130 TYR A CZ  1 
ATOM   1013 O  OH  . TYR A 1 135 ? 21.761 19.540 24.075 1.00 34.57  ? 130 TYR A OH  1 
ATOM   1014 N  N   . LEU A 1 136 ? 16.129 25.897 26.021 1.00 36.02  ? 131 LEU A N   1 
ATOM   1015 C  CA  . LEU A 1 136 ? 15.265 27.022 26.463 1.00 38.38  ? 131 LEU A CA  1 
ATOM   1016 C  C   . LEU A 1 136 ? 13.815 26.533 26.570 1.00 37.81  ? 131 LEU A C   1 
ATOM   1017 O  O   . LEU A 1 136 ? 13.143 26.871 27.563 1.00 42.38  ? 131 LEU A O   1 
ATOM   1018 C  CB  . LEU A 1 136 ? 15.382 28.196 25.491 1.00 37.39  ? 131 LEU A CB  1 
ATOM   1019 C  CG  . LEU A 1 136 ? 16.665 29.016 25.580 1.00 39.93  ? 131 LEU A CG  1 
ATOM   1020 C  CD1 . LEU A 1 136 ? 16.732 30.041 24.471 1.00 44.25  ? 131 LEU A CD1 1 
ATOM   1021 C  CD2 . LEU A 1 136 ? 16.789 29.712 26.924 1.00 37.05  ? 131 LEU A CD2 1 
ATOM   1022 N  N   . ALA A 1 137 ? 13.370 25.729 25.608 1.00 40.16  ? 132 ALA A N   1 
ATOM   1023 C  CA  . ALA A 1 137 ? 11.993 25.184 25.556 1.00 43.86  ? 132 ALA A CA  1 
ATOM   1024 C  C   . ALA A 1 137 ? 11.705 24.285 26.776 1.00 44.98  ? 132 ALA A C   1 
ATOM   1025 O  O   . ALA A 1 137 ? 10.583 24.398 27.303 1.00 48.83  ? 132 ALA A O   1 
ATOM   1026 C  CB  . ALA A 1 137 ? 11.781 24.437 24.257 1.00 46.44  ? 132 ALA A CB  1 
ATOM   1027 N  N   . GLU A 1 138 ? 12.657 23.446 27.228 1.00 38.16  ? 133 GLU A N   1 
ATOM   1028 C  CA  . GLU A 1 138 ? 12.498 22.625 28.466 1.00 41.07  ? 133 GLU A CA  1 
ATOM   1029 C  C   . GLU A 1 138 ? 12.094 23.489 29.685 1.00 41.03  ? 133 GLU A C   1 
ATOM   1030 O  O   . GLU A 1 138 ? 11.446 22.945 30.596 1.00 49.14  ? 133 GLU A O   1 
ATOM   1031 C  CB  . GLU A 1 138 ? 13.773 21.845 28.810 1.00 40.11  ? 133 GLU A CB  1 
ATOM   1032 C  CG  . GLU A 1 138 ? 14.168 20.805 27.788 1.00 43.44  ? 133 GLU A CG  1 
ATOM   1033 C  CD  . GLU A 1 138 ? 15.500 20.102 28.009 1.00 43.24  ? 133 GLU A CD  1 
ATOM   1034 O  OE1 . GLU A 1 138 ? 16.308 20.575 28.835 1.00 44.83  ? 133 GLU A OE1 1 
ATOM   1035 O  OE2 . GLU A 1 138 ? 15.732 19.073 27.347 1.00 42.20  ? 133 GLU A OE2 1 
ATOM   1036 N  N   . VAL A 1 139 ? 12.449 24.769 29.749 1.00 38.13  ? 134 VAL A N   1 
ATOM   1037 C  CA  . VAL A 1 139 ? 12.162 25.596 30.958 1.00 44.18  ? 134 VAL A CA  1 
ATOM   1038 C  C   . VAL A 1 139 ? 11.189 26.733 30.613 1.00 44.16  ? 134 VAL A C   1 
ATOM   1039 O  O   . VAL A 1 139 ? 10.878 27.503 31.514 1.00 45.08  ? 134 VAL A O   1 
ATOM   1040 C  CB  . VAL A 1 139 ? 13.460 26.150 31.573 1.00 41.45  ? 134 VAL A CB  1 
ATOM   1041 C  CG1 . VAL A 1 139 ? 14.484 25.053 31.804 1.00 39.34  ? 134 VAL A CG1 1 
ATOM   1042 C  CG2 . VAL A 1 139 ? 14.051 27.271 30.731 1.00 43.59  ? 134 VAL A CG2 1 
ATOM   1043 N  N   . ALA A 1 140 ? 10.721 26.844 29.369 1.00 46.66  ? 135 ALA A N   1 
ATOM   1044 C  CA  . ALA A 1 140 ? 9.894  27.993 28.912 1.00 51.25  ? 135 ALA A CA  1 
ATOM   1045 C  C   . ALA A 1 140 ? 8.404  27.805 29.275 1.00 51.43  ? 135 ALA A C   1 
ATOM   1046 O  O   . ALA A 1 140 ? 7.961  26.654 29.504 1.00 50.68  ? 135 ALA A O   1 
ATOM   1047 C  CB  . ALA A 1 140 ? 10.084 28.198 27.426 1.00 47.20  ? 135 ALA A CB  1 
ATOM   1048 N  N   . THR A 1 141 ? 7.653  28.912 29.285 1.00 63.13  ? 136 THR A N   1 
ATOM   1049 C  CA  . THR A 1 141 ? 6.164  28.952 29.382 1.00 69.48  ? 136 THR A CA  1 
ATOM   1050 C  C   . THR A 1 141 ? 5.617  30.191 28.647 1.00 64.64  ? 136 THR A C   1 
ATOM   1051 O  O   . THR A 1 141 ? 6.273  31.240 28.699 1.00 66.50  ? 136 THR A O   1 
ATOM   1052 C  CB  . THR A 1 141 ? 5.717  28.980 30.847 1.00 70.56  ? 136 THR A CB  1 
ATOM   1053 O  OG1 . THR A 1 141 ? 6.524  29.986 31.464 1.00 73.20  ? 136 THR A OG1 1 
ATOM   1054 C  CG2 . THR A 1 141 ? 5.856  27.649 31.555 1.00 64.30  ? 136 THR A CG2 1 
ATOM   1055 N  N   . GLY A 1 142 ? 4.476  30.055 27.957 1.00 73.14  ? 137 GLY A N   1 
ATOM   1056 C  CA  . GLY A 1 142 ? 3.660  31.177 27.441 1.00 68.24  ? 137 GLY A CA  1 
ATOM   1057 C  C   . GLY A 1 142 ? 4.124  31.699 26.092 1.00 62.60  ? 137 GLY A C   1 
ATOM   1058 O  O   . GLY A 1 142 ? 4.577  30.906 25.250 1.00 63.43  ? 137 GLY A O   1 
ATOM   1059 N  N   . ASP A 1 143 ? 4.011  33.012 25.885 1.00 72.66  ? 138 ASP A N   1 
ATOM   1060 C  CA  . ASP A 1 143 ? 4.270  33.691 24.584 1.00 75.74  ? 138 ASP A CA  1 
ATOM   1061 C  C   . ASP A 1 143 ? 5.740  33.502 24.186 1.00 81.87  ? 138 ASP A C   1 
ATOM   1062 O  O   . ASP A 1 143 ? 6.033  33.408 22.952 1.00 84.63  ? 138 ASP A O   1 
ATOM   1063 C  CB  . ASP A 1 143 ? 3.914  35.183 24.646 1.00 70.10  ? 138 ASP A CB  1 
ATOM   1064 C  CG  . ASP A 1 143 ? 2.429  35.497 24.515 1.00 69.80  ? 138 ASP A CG  1 
ATOM   1065 O  OD1 . ASP A 1 143 ? 1.618  34.540 24.314 1.00 60.57  ? 138 ASP A OD1 1 
ATOM   1066 O  OD2 . ASP A 1 143 ? 2.094  36.706 24.579 1.00 58.33  ? 138 ASP A OD2 1 
ATOM   1067 N  N   . ASP A 1 144 ? 6.638  33.463 25.177 1.00 73.18  ? 139 ASP A N   1 
ATOM   1068 C  CA  . ASP A 1 144 ? 8.083  33.238 24.926 1.00 70.56  ? 139 ASP A CA  1 
ATOM   1069 C  C   . ASP A 1 144 ? 8.243  31.809 24.381 1.00 64.30  ? 139 ASP A C   1 
ATOM   1070 O  O   . ASP A 1 144 ? 9.113  31.597 23.513 1.00 61.55  ? 139 ASP A O   1 
ATOM   1071 C  CB  . ASP A 1 144 ? 8.926  33.535 26.173 1.00 70.58  ? 139 ASP A CB  1 
ATOM   1072 C  CG  . ASP A 1 144 ? 10.404 33.727 25.860 1.00 74.68  ? 139 ASP A CG  1 
ATOM   1073 O  OD1 . ASP A 1 144 ? 10.698 34.213 24.746 1.00 83.47  ? 139 ASP A OD1 1 
ATOM   1074 O  OD2 . ASP A 1 144 ? 11.250 33.364 26.715 1.00 67.37  ? 139 ASP A OD2 1 
ATOM   1075 N  N   . LYS A 1 145 ? 7.383  30.880 24.804 1.00 60.72  ? 140 LYS A N   1 
ATOM   1076 C  CA  . LYS A 1 145 ? 7.608  29.430 24.585 1.00 58.05  ? 140 LYS A CA  1 
ATOM   1077 C  C   . LYS A 1 145 ? 7.333  29.035 23.136 1.00 66.80  ? 140 LYS A C   1 
ATOM   1078 O  O   . LYS A 1 145 ? 8.208  28.388 22.528 1.00 68.81  ? 140 LYS A O   1 
ATOM   1079 C  CB  . LYS A 1 145 ? 6.733  28.572 25.489 1.00 55.22  ? 140 LYS A CB  1 
ATOM   1080 C  CG  . LYS A 1 145 ? 6.876  27.085 25.241 1.00 52.26  ? 140 LYS A CG  1 
ATOM   1081 C  CD  . LYS A 1 145 ? 6.547  26.248 26.448 1.00 56.68  ? 140 LYS A CD  1 
ATOM   1082 C  CE  . LYS A 1 145 ? 7.002  24.813 26.273 1.00 53.80  ? 140 LYS A CE  1 
ATOM   1083 N  NZ  . LYS A 1 145 ? 6.055  23.864 26.903 1.00 60.85  ? 140 LYS A NZ  1 
ATOM   1084 N  N   . LYS A 1 146 ? 6.155  29.347 22.604 1.00 65.29  ? 141 LYS A N   1 
ATOM   1085 C  CA  . LYS A 1 146 ? 5.820  28.883 21.234 1.00 65.44  ? 141 LYS A CA  1 
ATOM   1086 C  C   . LYS A 1 146 ? 6.843  29.509 20.273 1.00 49.08  ? 141 LYS A C   1 
ATOM   1087 O  O   . LYS A 1 146 ? 7.290  28.781 19.374 1.00 63.66  ? 141 LYS A O   1 
ATOM   1088 C  CB  . LYS A 1 146 ? 4.350  29.143 20.876 1.00 77.83  ? 141 LYS A CB  1 
ATOM   1089 C  CG  . LYS A 1 146 ? 3.541  27.876 20.602 1.00 86.13  ? 141 LYS A CG  1 
ATOM   1090 C  CD  . LYS A 1 146 ? 2.003  28.042 20.564 1.00 94.19  ? 141 LYS A CD  1 
ATOM   1091 C  CE  . LYS A 1 146 ? 1.418  28.679 19.310 1.00 93.53  ? 141 LYS A CE  1 
ATOM   1092 N  NZ  . LYS A 1 146 ? 2.121  28.274 18.065 1.00 89.73  ? 141 LYS A NZ  1 
ATOM   1093 N  N   . ARG A 1 147 ? 7.260  30.762 20.500 1.00 51.09  ? 142 ARG A N   1 
ATOM   1094 C  CA  . ARG A 1 147 ? 8.348  31.404 19.703 1.00 54.79  ? 142 ARG A CA  1 
ATOM   1095 C  C   . ARG A 1 147 ? 9.582  30.478 19.736 1.00 56.52  ? 142 ARG A C   1 
ATOM   1096 O  O   . ARG A 1 147 ? 10.181 30.232 18.669 1.00 52.02  ? 142 ARG A O   1 
ATOM   1097 C  CB  . ARG A 1 147 ? 8.766  32.779 20.238 1.00 59.68  ? 142 ARG A CB  1 
ATOM   1098 C  CG  . ARG A 1 147 ? 7.766  33.909 20.038 1.00 64.83  ? 142 ARG A CG  1 
ATOM   1099 C  CD  . ARG A 1 147 ? 8.400  35.262 20.340 1.00 65.82  ? 142 ARG A CD  1 
ATOM   1100 N  NE  . ARG A 1 147 ? 7.541  36.101 21.168 1.00 73.50  ? 142 ARG A NE  1 
ATOM   1101 C  CZ  . ARG A 1 147 ? 7.744  36.430 22.446 1.00 75.28  ? 142 ARG A CZ  1 
ATOM   1102 N  NH1 . ARG A 1 147 ? 8.827  36.027 23.095 1.00 83.39  ? 142 ARG A NH1 1 
ATOM   1103 N  NH2 . ARG A 1 147 ? 6.857  37.192 23.067 1.00 70.02  ? 142 ARG A NH2 1 
ATOM   1104 N  N   . ILE A 1 148 ? 9.924  29.958 20.924 1.00 56.41  ? 143 ILE A N   1 
ATOM   1105 C  CA  . ILE A 1 148 ? 11.133 29.106 21.152 1.00 51.21  ? 143 ILE A CA  1 
ATOM   1106 C  C   . ILE A 1 148 ? 10.987 27.781 20.406 1.00 45.01  ? 143 ILE A C   1 
ATOM   1107 O  O   . ILE A 1 148 ? 11.938 27.422 19.689 1.00 49.09  ? 143 ILE A O   1 
ATOM   1108 C  CB  . ILE A 1 148 ? 11.432 28.905 22.651 1.00 47.34  ? 143 ILE A CB  1 
ATOM   1109 C  CG1 . ILE A 1 148 ? 11.934 30.211 23.269 1.00 49.27  ? 143 ILE A CG1 1 
ATOM   1110 C  CG2 . ILE A 1 148 ? 12.441 27.775 22.858 1.00 46.81  ? 143 ILE A CG2 1 
ATOM   1111 C  CD1 . ILE A 1 148 ? 11.782 30.263 24.771 1.00 54.89  ? 143 ILE A CD1 1 
ATOM   1112 N  N   . ILE A 1 149 ? 9.848  27.103 20.523 1.00 48.60  ? 144 ILE A N   1 
ATOM   1113 C  CA  . ILE A 1 149 ? 9.639  25.764 19.902 1.00 50.03  ? 144 ILE A CA  1 
ATOM   1114 C  C   . ILE A 1 149 ? 9.714  25.869 18.365 1.00 53.50  ? 144 ILE A C   1 
ATOM   1115 O  O   . ILE A 1 149 ? 10.277 24.964 17.747 1.00 53.87  ? 144 ILE A O   1 
ATOM   1116 C  CB  . ILE A 1 149 ? 8.319  25.139 20.384 1.00 53.86  ? 144 ILE A CB  1 
ATOM   1117 C  CG1 . ILE A 1 149 ? 8.320  25.000 21.912 1.00 57.49  ? 144 ILE A CG1 1 
ATOM   1118 C  CG2 . ILE A 1 149 ? 8.095  23.813 19.670 1.00 53.87  ? 144 ILE A CG2 1 
ATOM   1119 C  CD1 . ILE A 1 149 ? 7.310  24.028 22.465 1.00 55.78  ? 144 ILE A CD1 1 
ATOM   1120 N  N   . ASP A 1 150 ? 9.147  26.912 17.771 1.00 57.47  ? 145 ASP A N   1 
ATOM   1121 C  CA  . ASP A 1 150 ? 9.192  27.139 16.302 1.00 58.29  ? 145 ASP A CA  1 
ATOM   1122 C  C   . ASP A 1 150 ? 10.651 27.312 15.881 1.00 53.16  ? 145 ASP A C   1 
ATOM   1123 O  O   . ASP A 1 150 ? 11.066 26.631 14.935 1.00 54.54  ? 145 ASP A O   1 
ATOM   1124 C  CB  . ASP A 1 150 ? 8.396  28.380 15.893 1.00 61.44  ? 145 ASP A CB  1 
ATOM   1125 C  CG  . ASP A 1 150 ? 6.909  28.290 16.219 1.00 65.83  ? 145 ASP A CG  1 
ATOM   1126 O  OD1 . ASP A 1 150 ? 6.390  27.142 16.327 1.00 62.36  ? 145 ASP A OD1 1 
ATOM   1127 O  OD2 . ASP A 1 150 ? 6.282  29.370 16.367 1.00 64.06  ? 145 ASP A OD2 1 
ATOM   1128 N  N   . SER A 1 151 ? 11.389 28.176 16.580 1.00 50.16  ? 146 SER A N   1 
ATOM   1129 C  CA  . SER A 1 151 ? 12.806 28.491 16.269 1.00 54.04  ? 146 SER A CA  1 
ATOM   1130 C  C   . SER A 1 151 ? 13.629 27.201 16.298 1.00 48.99  ? 146 SER A C   1 
ATOM   1131 O  O   . SER A 1 151 ? 14.463 27.026 15.410 1.00 50.80  ? 146 SER A O   1 
ATOM   1132 C  CB  . SER A 1 151 ? 13.354 29.520 17.174 1.00 48.02  ? 146 SER A CB  1 
ATOM   1133 O  OG  . SER A 1 151 ? 12.511 30.631 17.208 1.00 51.12  ? 146 SER A OG  1 
ATOM   1134 N  N   . ALA A 1 152 ? 13.343 26.292 17.222 1.00 46.40  ? 147 ALA A N   1 
ATOM   1135 C  CA  . ALA A 1 152 ? 14.065 25.008 17.329 1.00 45.11  ? 147 ALA A CA  1 
ATOM   1136 C  C   . ALA A 1 152 ? 13.740 24.119 16.116 1.00 48.70  ? 147 ALA A C   1 
ATOM   1137 O  O   . ALA A 1 152 ? 14.679 23.555 15.487 1.00 39.54  ? 147 ALA A O   1 
ATOM   1138 C  CB  . ALA A 1 152 ? 13.711 24.328 18.621 1.00 45.56  ? 147 ALA A CB  1 
ATOM   1139 N  N   . ARG A 1 153 ? 12.454 23.924 15.827 1.00 48.85  ? 148 ARG A N   1 
ATOM   1140 C  CA  . ARG A 1 153 ? 12.006 23.049 14.703 1.00 51.49  ? 148 ARG A CA  1 
ATOM   1141 C  C   . ARG A 1 153 ? 12.606 23.560 13.384 1.00 43.42  ? 148 ARG A C   1 
ATOM   1142 O  O   . ARG A 1 153 ? 13.100 22.740 12.587 1.00 50.14  ? 148 ARG A O   1 
ATOM   1143 C  CB  . ARG A 1 153 ? 10.477 23.011 14.618 1.00 55.19  ? 148 ARG A CB  1 
ATOM   1144 C  CG  . ARG A 1 153 ? 9.944  22.459 13.302 1.00 60.00  ? 148 ARG A CG  1 
ATOM   1145 C  CD  . ARG A 1 153 ? 8.428  22.440 13.258 1.00 61.83  ? 148 ARG A CD  1 
ATOM   1146 N  NE  . ARG A 1 153 ? 7.854  21.549 14.264 1.00 58.77  ? 148 ARG A NE  1 
ATOM   1147 C  CZ  . ARG A 1 153 ? 7.192  21.943 15.345 1.00 54.95  ? 148 ARG A CZ  1 
ATOM   1148 N  NH1 . ARG A 1 153 ? 7.014  23.228 15.608 1.00 55.42  ? 148 ARG A NH1 1 
ATOM   1149 N  NH2 . ARG A 1 153 ? 6.698  21.034 16.162 1.00 60.52  ? 148 ARG A NH2 1 
ATOM   1150 N  N   . SER A 1 154 ? 12.521 24.859 13.166 1.00 45.04  ? 149 SER A N   1 
ATOM   1151 C  CA  . SER A 1 154 ? 12.971 25.532 11.927 1.00 54.07  ? 149 SER A CA  1 
ATOM   1152 C  C   . SER A 1 154 ? 14.472 25.263 11.747 1.00 56.22  ? 149 SER A C   1 
ATOM   1153 O  O   . SER A 1 154 ? 14.876 24.824 10.646 1.00 47.95  ? 149 SER A O   1 
ATOM   1154 C  CB  . SER A 1 154 ? 12.630 27.005 11.975 1.00 57.78  ? 149 SER A CB  1 
ATOM   1155 O  OG  . SER A 1 154 ? 13.678 27.793 11.430 1.00 68.39  ? 149 SER A OG  1 
ATOM   1156 N  N   . ALA A 1 155 ? 15.269 25.484 12.799 1.00 51.98  ? 150 ALA A N   1 
ATOM   1157 C  CA  . ALA A 1 155 ? 16.735 25.281 12.747 1.00 47.06  ? 150 ALA A CA  1 
ATOM   1158 C  C   . ALA A 1 155 ? 17.018 23.813 12.446 1.00 41.91  ? 150 ALA A C   1 
ATOM   1159 O  O   . ALA A 1 155 ? 17.886 23.532 11.595 1.00 40.33  ? 150 ALA A O   1 
ATOM   1160 C  CB  . ALA A 1 155 ? 17.388 25.737 14.025 1.00 47.56  ? 150 ALA A CB  1 
ATOM   1161 N  N   . TYR A 1 156 ? 16.325 22.900 13.126 1.00 41.63  ? 151 TYR A N   1 
ATOM   1162 C  CA  . TYR A 1 156 ? 16.505 21.442 12.913 1.00 42.22  ? 151 TYR A CA  1 
ATOM   1163 C  C   . TYR A 1 156 ? 16.161 21.071 11.459 1.00 43.20  ? 151 TYR A C   1 
ATOM   1164 O  O   . TYR A 1 156 ? 16.873 20.250 10.865 1.00 39.93  ? 151 TYR A O   1 
ATOM   1165 C  CB  . TYR A 1 156 ? 15.663 20.604 13.885 1.00 40.15  ? 151 TYR A CB  1 
ATOM   1166 C  CG  . TYR A 1 156 ? 16.232 20.432 15.287 1.00 42.68  ? 151 TYR A CG  1 
ATOM   1167 C  CD1 . TYR A 1 156 ? 17.546 20.037 15.511 1.00 43.81  ? 151 TYR A CD1 1 
ATOM   1168 C  CD2 . TYR A 1 156 ? 15.430 20.580 16.409 1.00 46.50  ? 151 TYR A CD2 1 
ATOM   1169 C  CE1 . TYR A 1 156 ? 18.054 19.826 16.790 1.00 38.24  ? 151 TYR A CE1 1 
ATOM   1170 C  CE2 . TYR A 1 156 ? 15.925 20.389 17.696 1.00 46.12  ? 151 TYR A CE2 1 
ATOM   1171 C  CZ  . TYR A 1 156 ? 17.249 20.038 17.890 1.00 39.72  ? 151 TYR A CZ  1 
ATOM   1172 O  OH  . TYR A 1 156 ? 17.751 19.816 19.143 1.00 38.74  ? 151 TYR A OH  1 
ATOM   1173 N  N   . GLN A 1 157 ? 15.061 21.587 10.923 1.00 44.90  ? 152 GLN A N   1 
ATOM   1174 C  CA  A GLN A 1 157 ? 14.557 21.185 9.579  0.40 45.61  ? 152 GLN A CA  1 
ATOM   1175 C  CA  B GLN A 1 157 ? 14.562 21.166 9.579  0.60 44.68  ? 152 GLN A CA  1 
ATOM   1176 C  C   . GLN A 1 157 ? 15.559 21.652 8.517  1.00 40.06  ? 152 GLN A C   1 
ATOM   1177 O  O   . GLN A 1 157 ? 15.933 20.858 7.601  1.00 47.92  ? 152 GLN A O   1 
ATOM   1178 C  CB  A GLN A 1 157 ? 13.156 21.764 9.369  0.40 47.11  ? 152 GLN A CB  1 
ATOM   1179 C  CB  B GLN A 1 157 ? 13.143 21.700 9.359  0.60 44.42  ? 152 GLN A CB  1 
ATOM   1180 C  CG  A GLN A 1 157 ? 12.053 20.788 9.747  0.40 49.46  ? 152 GLN A CG  1 
ATOM   1181 C  CG  B GLN A 1 157 ? 12.471 21.149 8.098  0.60 44.33  ? 152 GLN A CG  1 
ATOM   1182 C  CD  A GLN A 1 157 ? 10.765 21.493 10.089 0.40 49.40  ? 152 GLN A CD  1 
ATOM   1183 C  CD  B GLN A 1 157 ? 12.530 19.644 7.994  0.60 41.17  ? 152 GLN A CD  1 
ATOM   1184 O  OE1 A GLN A 1 157 ? 10.677 22.721 10.064 0.40 51.25  ? 152 GLN A OE1 1 
ATOM   1185 O  OE1 B GLN A 1 157 ? 13.152 19.082 7.097  0.60 45.32  ? 152 GLN A OE1 1 
ATOM   1186 N  NE2 A GLN A 1 157 ? 9.754  20.710 10.423 0.40 45.15  ? 152 GLN A NE2 1 
ATOM   1187 N  NE2 B GLN A 1 157 ? 11.904 18.970 8.935  0.60 43.09  ? 152 GLN A NE2 1 
ATOM   1188 N  N   . GLU A 1 158 ? 16.016 22.874 8.660  1.00 41.81  ? 153 GLU A N   1 
ATOM   1189 C  CA  . GLU A 1 158 ? 16.992 23.412 7.697  1.00 49.45  ? 153 GLU A CA  1 
ATOM   1190 C  C   . GLU A 1 158 ? 18.231 22.519 7.752  1.00 47.23  ? 153 GLU A C   1 
ATOM   1191 O  O   . GLU A 1 158 ? 18.752 22.146 6.684  1.00 46.66  ? 153 GLU A O   1 
ATOM   1192 C  CB  . GLU A 1 158 ? 17.307 24.869 7.979  1.00 52.14  ? 153 GLU A CB  1 
ATOM   1193 C  CG  . GLU A 1 158 ? 18.317 25.389 6.969  1.00 61.41  ? 153 GLU A CG  1 
ATOM   1194 C  CD  . GLU A 1 158 ? 18.583 26.874 7.020  1.00 62.36  ? 153 GLU A CD  1 
ATOM   1195 O  OE1 . GLU A 1 158 ? 18.065 27.536 7.946  1.00 73.72  ? 153 GLU A OE1 1 
ATOM   1196 O  OE2 . GLU A 1 158 ? 19.314 27.356 6.131  1.00 68.55  ? 153 GLU A OE2 1 
ATOM   1197 N  N   . ALA A 1 159 ? 18.659 22.142 8.960  1.00 42.68  ? 154 ALA A N   1 
ATOM   1198 C  CA  . ALA A 1 159 ? 19.833 21.260 9.133  1.00 39.56  ? 154 ALA A CA  1 
ATOM   1199 C  C   . ALA A 1 159 ? 19.570 19.927 8.431  1.00 35.89  ? 154 ALA A C   1 
ATOM   1200 O  O   . ALA A 1 159 ? 20.499 19.398 7.766  1.00 35.74  ? 154 ALA A O   1 
ATOM   1201 C  CB  . ALA A 1 159 ? 20.170 21.074 10.599 1.00 38.76  ? 154 ALA A CB  1 
ATOM   1202 N  N   . MET A 1 160 ? 18.371 19.370 8.621  1.00 37.19  ? 155 MET A N   1 
ATOM   1203 C  CA  . MET A 1 160 ? 17.977 18.049 8.067  1.00 38.15  ? 155 MET A CA  1 
ATOM   1204 C  C   . MET A 1 160 ? 17.994 18.129 6.530  1.00 37.30  ? 155 MET A C   1 
ATOM   1205 O  O   . MET A 1 160 ? 18.532 17.208 5.904  1.00 38.28  ? 155 MET A O   1 
ATOM   1206 C  CB  . MET A 1 160 ? 16.577 17.665 8.551  1.00 40.47  ? 155 MET A CB  1 
ATOM   1207 C  CG  . MET A 1 160 ? 16.549 17.232 10.040 1.00 41.73  ? 155 MET A CG  1 
ATOM   1208 S  SD  . MET A 1 160 ? 17.211 15.593 10.377 1.00 50.65  ? 155 MET A SD  1 
ATOM   1209 C  CE  . MET A 1 160 ? 16.304 14.578 9.213  1.00 54.17  ? 155 MET A CE  1 
ATOM   1210 N  N   . ASP A 1 161 ? 17.463 19.219 5.969  1.00 48.31  ? 156 ASP A N   1 
ATOM   1211 C  CA  . ASP A 1 161 ? 17.417 19.465 4.496  1.00 48.73  ? 156 ASP A CA  1 
ATOM   1212 C  C   . ASP A 1 161 ? 18.843 19.364 3.930  1.00 47.28  ? 156 ASP A C   1 
ATOM   1213 O  O   . ASP A 1 161 ? 19.072 18.503 3.049  1.00 46.74  ? 156 ASP A O   1 
ATOM   1214 C  CB  . ASP A 1 161 ? 16.731 20.802 4.222  1.00 47.75  ? 156 ASP A CB  1 
ATOM   1215 C  CG  . ASP A 1 161 ? 15.243 20.779 4.544  1.00 55.98  ? 156 ASP A CG  1 
ATOM   1216 O  OD1 . ASP A 1 161 ? 14.699 19.667 4.728  1.00 61.03  ? 156 ASP A OD1 1 
ATOM   1217 O  OD2 . ASP A 1 161 ? 14.643 21.872 4.645  1.00 59.29  ? 156 ASP A OD2 1 
ATOM   1218 N  N   . ILE A 1 162 ? 19.787 20.136 4.486  1.00 46.90  ? 157 ILE A N   1 
ATOM   1219 C  CA  . ILE A 1 162 ? 21.215 20.135 4.048  1.00 44.41  ? 157 ILE A CA  1 
ATOM   1220 C  C   . ILE A 1 162 ? 21.839 18.738 4.214  1.00 43.90  ? 157 ILE A C   1 
ATOM   1221 O  O   . ILE A 1 162 ? 22.560 18.282 3.280  1.00 41.93  ? 157 ILE A O   1 
ATOM   1222 C  CB  . ILE A 1 162 ? 22.027 21.229 4.768  1.00 46.51  ? 157 ILE A CB  1 
ATOM   1223 C  CG1 . ILE A 1 162 ? 21.392 22.608 4.579  1.00 50.24  ? 157 ILE A CG1 1 
ATOM   1224 C  CG2 . ILE A 1 162 ? 23.476 21.197 4.282  1.00 47.10  ? 157 ILE A CG2 1 
ATOM   1225 C  CD1 . ILE A 1 162 ? 21.912 23.677 5.497  1.00 46.20  ? 157 ILE A CD1 1 
ATOM   1226 N  N   . SER A 1 163 ? 21.594 18.052 5.338  1.00 42.33  ? 158 SER A N   1 
ATOM   1227 C  CA  . SER A 1 163 ? 22.284 16.779 5.668  1.00 41.98  ? 158 SER A CA  1 
ATOM   1228 C  C   . SER A 1 163 ? 21.891 15.688 4.661  1.00 39.06  ? 158 SER A C   1 
ATOM   1229 O  O   . SER A 1 163 ? 22.755 14.924 4.272  1.00 37.77  ? 158 SER A O   1 
ATOM   1230 C  CB  . SER A 1 163 ? 22.010 16.325 7.108  1.00 39.99  ? 158 SER A CB  1 
ATOM   1231 O  OG  . SER A 1 163 ? 20.695 15.773 7.245  1.00 46.83  ? 158 SER A OG  1 
ATOM   1232 N  N   . LYS A 1 164 ? 20.602 15.584 4.326  1.00 42.99  ? 159 LYS A N   1 
ATOM   1233 C  CA  . LYS A 1 164 ? 20.065 14.507 3.441  1.00 51.88  ? 159 LYS A CA  1 
ATOM   1234 C  C   . LYS A 1 164 ? 20.566 14.731 2.007  1.00 43.87  ? 159 LYS A C   1 
ATOM   1235 O  O   . LYS A 1 164 ? 20.760 13.748 1.298  1.00 48.78  ? 159 LYS A O   1 
ATOM   1236 C  CB  . LYS A 1 164 ? 18.532 14.468 3.503  1.00 55.85  ? 159 LYS A CB  1 
ATOM   1237 C  CG  . LYS A 1 164 ? 17.960 14.137 4.879  1.00 65.60  ? 159 LYS A CG  1 
ATOM   1238 C  CD  . LYS A 1 164 ? 16.629 14.809 5.210  1.00 71.73  ? 159 LYS A CD  1 
ATOM   1239 C  CE  . LYS A 1 164 ? 15.421 14.141 4.588  1.00 74.29  ? 159 LYS A CE  1 
ATOM   1240 N  NZ  . LYS A 1 164 ? 15.314 12.722 4.989  1.00 75.73  ? 159 LYS A NZ  1 
ATOM   1241 N  N   . LYS A 1 165 ? 20.802 15.983 1.637  1.00 46.84  ? 160 LYS A N   1 
ATOM   1242 C  CA  . LYS A 1 165 ? 21.288 16.373 0.294  1.00 55.64  ? 160 LYS A CA  1 
ATOM   1243 C  C   . LYS A 1 165 ? 22.813 16.210 0.218  1.00 55.64  ? 160 LYS A C   1 
ATOM   1244 O  O   . LYS A 1 165 ? 23.285 15.710 -0.818 1.00 52.14  ? 160 LYS A O   1 
ATOM   1245 C  CB  . LYS A 1 165 ? 20.789 17.787 -0.000 1.00 61.38  ? 160 LYS A CB  1 
ATOM   1246 C  CG  . LYS A 1 165 ? 21.231 18.379 -1.324 1.00 76.30  ? 160 LYS A CG  1 
ATOM   1247 C  CD  . LYS A 1 165 ? 21.803 19.767 -1.145 1.00 86.33  ? 160 LYS A CD  1 
ATOM   1248 C  CE  . LYS A 1 165 ? 22.309 20.386 -2.429 1.00 88.22  ? 160 LYS A CE  1 
ATOM   1249 N  NZ  . LYS A 1 165 ? 21.175 20.806 -3.280 1.00 95.64  ? 160 LYS A NZ  1 
ATOM   1250 N  N   . GLU A 1 166 ? 23.572 16.551 1.268  1.00 49.70  ? 161 GLU A N   1 
ATOM   1251 C  CA  . GLU A 1 166 ? 25.051 16.696 1.153  1.00 42.38  ? 161 GLU A CA  1 
ATOM   1252 C  C   . GLU A 1 166 ? 25.819 15.638 1.949  1.00 46.49  ? 161 GLU A C   1 
ATOM   1253 O  O   . GLU A 1 166 ? 27.026 15.630 1.797  1.00 43.72  ? 161 GLU A O   1 
ATOM   1254 C  CB  . GLU A 1 166 ? 25.456 18.097 1.583  1.00 48.53  ? 161 GLU A CB  1 
ATOM   1255 C  CG  . GLU A 1 166 ? 24.563 19.172 0.974  1.00 54.43  ? 161 GLU A CG  1 
ATOM   1256 C  CD  . GLU A 1 166 ? 25.188 20.553 0.864  1.00 58.20  ? 161 GLU A CD  1 
ATOM   1257 O  OE1 . GLU A 1 166 ? 26.411 20.609 0.704  1.00 64.62  ? 161 GLU A OE1 1 
ATOM   1258 O  OE2 . GLU A 1 166 ? 24.451 21.562 0.943  1.00 63.94  ? 161 GLU A OE2 1 
ATOM   1259 N  N   . MET A 1 167 ? 25.197 14.808 2.796  1.00 40.46  ? 162 MET A N   1 
ATOM   1260 C  CA  . MET A 1 167 ? 25.987 13.866 3.625  1.00 42.01  ? 162 MET A CA  1 
ATOM   1261 C  C   . MET A 1 167 ? 25.497 12.447 3.423  1.00 36.83  ? 162 MET A C   1 
ATOM   1262 O  O   . MET A 1 167 ? 24.308 12.211 3.264  1.00 39.03  ? 162 MET A O   1 
ATOM   1263 C  CB  . MET A 1 167 ? 25.891 14.209 5.115  1.00 43.69  ? 162 MET A CB  1 
ATOM   1264 C  CG  . MET A 1 167 ? 26.537 15.537 5.480  1.00 47.89  ? 162 MET A CG  1 
ATOM   1265 S  SD  . MET A 1 167 ? 25.979 16.105 7.109  1.00 46.45  ? 162 MET A SD  1 
ATOM   1266 C  CE  . MET A 1 167 ? 27.516 16.828 7.666  1.00 48.46  ? 162 MET A CE  1 
ATOM   1267 N  N   . PRO A 1 168 ? 26.396 11.459 3.530  1.00 34.05  ? 163 PRO A N   1 
ATOM   1268 C  CA  . PRO A 1 168 ? 25.987 10.067 3.578  1.00 37.23  ? 163 PRO A CA  1 
ATOM   1269 C  C   . PRO A 1 168 ? 25.141 9.812  4.822  1.00 41.67  ? 163 PRO A C   1 
ATOM   1270 O  O   . PRO A 1 168 ? 25.167 10.579 5.784  1.00 33.97  ? 163 PRO A O   1 
ATOM   1271 C  CB  . PRO A 1 168 ? 27.301 9.298  3.581  1.00 37.11  ? 163 PRO A CB  1 
ATOM   1272 C  CG  . PRO A 1 168 ? 28.305 10.273 4.100  1.00 36.95  ? 163 PRO A CG  1 
ATOM   1273 C  CD  . PRO A 1 168 ? 27.854 11.626 3.613  1.00 37.85  ? 163 PRO A CD  1 
ATOM   1274 N  N   . PRO A 1 169 ? 24.288 8.779  4.776  1.00 40.87  ? 164 PRO A N   1 
ATOM   1275 C  CA  . PRO A 1 169 ? 23.340 8.528  5.859  1.00 41.19  ? 164 PRO A CA  1 
ATOM   1276 C  C   . PRO A 1 169 ? 23.989 7.974  7.143  1.00 37.39  ? 164 PRO A C   1 
ATOM   1277 O  O   . PRO A 1 169 ? 23.317 7.957  8.144  1.00 41.58  ? 164 PRO A O   1 
ATOM   1278 C  CB  . PRO A 1 169 ? 22.387 7.509  5.218  1.00 46.13  ? 164 PRO A CB  1 
ATOM   1279 C  CG  . PRO A 1 169 ? 23.224 6.800  4.172  1.00 47.07  ? 164 PRO A CG  1 
ATOM   1280 C  CD  . PRO A 1 169 ? 24.197 7.822  3.656  1.00 45.09  ? 164 PRO A CD  1 
ATOM   1281 N  N   . THR A 1 170 ? 25.247 7.527  7.097  1.00 36.72  ? 165 THR A N   1 
ATOM   1282 C  CA  . THR A 1 170 ? 26.026 7.151  8.307  1.00 35.43  ? 165 THR A CA  1 
ATOM   1283 C  C   . THR A 1 170 ? 26.808 8.351  8.901  1.00 35.74  ? 165 THR A C   1 
ATOM   1284 O  O   . THR A 1 170 ? 27.553 8.137  9.878  1.00 32.49  ? 165 THR A O   1 
ATOM   1285 C  CB  . THR A 1 170 ? 27.040 6.048  8.010  1.00 35.23  ? 165 THR A CB  1 
ATOM   1286 O  OG1 . THR A 1 170 ? 27.945 6.549  7.039  1.00 34.43  ? 165 THR A OG1 1 
ATOM   1287 C  CG2 . THR A 1 170 ? 26.420 4.730  7.579  1.00 36.78  ? 165 THR A CG2 1 
ATOM   1288 N  N   . ASN A 1 171 ? 26.729 9.548  8.327  1.00 32.09  ? 166 ASN A N   1 
ATOM   1289 C  CA  . ASN A 1 171 ? 27.597 10.678 8.778  1.00 33.39  ? 166 ASN A CA  1 
ATOM   1290 C  C   . ASN A 1 171 ? 27.228 11.021 10.220 1.00 31.69  ? 166 ASN A C   1 
ATOM   1291 O  O   . ASN A 1 171 ? 26.061 11.242 10.514 1.00 32.79  ? 166 ASN A O   1 
ATOM   1292 C  CB  . ASN A 1 171 ? 27.465 11.917 7.902  1.00 32.64  ? 166 ASN A CB  1 
ATOM   1293 C  CG  . ASN A 1 171 ? 28.273 13.098 8.418  1.00 32.56  ? 166 ASN A CG  1 
ATOM   1294 O  OD1 . ASN A 1 171 ? 27.846 13.826 9.305  1.00 37.54  ? 166 ASN A OD1 1 
ATOM   1295 N  ND2 . ASN A 1 171 ? 29.409 13.330 7.808  1.00 34.03  ? 166 ASN A ND2 1 
ATOM   1296 N  N   . PRO A 1 172 ? 28.196 11.104 11.152 1.00 33.18  ? 167 PRO A N   1 
ATOM   1297 C  CA  . PRO A 1 172 ? 27.874 11.257 12.578 1.00 33.22  ? 167 PRO A CA  1 
ATOM   1298 C  C   . PRO A 1 172 ? 27.164 12.567 12.909 1.00 31.03  ? 167 PRO A C   1 
ATOM   1299 O  O   . PRO A 1 172 ? 26.306 12.520 13.730 1.00 31.27  ? 167 PRO A O   1 
ATOM   1300 C  CB  . PRO A 1 172 ? 29.224 11.064 13.299 1.00 35.18  ? 167 PRO A CB  1 
ATOM   1301 C  CG  . PRO A 1 172 ? 30.262 11.302 12.227 1.00 38.35  ? 167 PRO A CG  1 
ATOM   1302 C  CD  . PRO A 1 172 ? 29.631 10.871 10.917 1.00 32.13  ? 167 PRO A CD  1 
ATOM   1303 N  N   . ILE A 1 173 ? 27.440 13.674 12.192 1.00 28.98  ? 168 ILE A N   1 
ATOM   1304 C  CA  . ILE A 1 173 ? 26.677 14.932 12.379 1.00 30.86  ? 168 ILE A CA  1 
ATOM   1305 C  C   . ILE A 1 173 ? 25.236 14.665 11.918 1.00 33.53  ? 168 ILE A C   1 
ATOM   1306 O  O   . ILE A 1 173 ? 24.305 15.088 12.588 1.00 32.61  ? 168 ILE A O   1 
ATOM   1307 C  CB  . ILE A 1 173 ? 27.369 16.119 11.656 1.00 32.20  ? 168 ILE A CB  1 
ATOM   1308 C  CG1 . ILE A 1 173 ? 28.817 16.306 12.121 1.00 35.81  ? 168 ILE A CG1 1 
ATOM   1309 C  CG2 . ILE A 1 173 ? 26.559 17.375 11.810 1.00 32.56  ? 168 ILE A CG2 1 
ATOM   1310 C  CD1 . ILE A 1 173 ? 29.683 17.107 11.164 1.00 39.86  ? 168 ILE A CD1 1 
ATOM   1311 N  N   . ARG A 1 174 ? 25.056 14.027 10.764 1.00 39.50  ? 169 ARG A N   1 
ATOM   1312 C  CA  . ARG A 1 174 ? 23.686 13.753 10.243 1.00 35.18  ? 169 ARG A CA  1 
ATOM   1313 C  C   . ARG A 1 174 ? 22.917 12.899 11.267 1.00 32.13  ? 169 ARG A C   1 
ATOM   1314 O  O   . ARG A 1 174 ? 21.781 13.273 11.612 1.00 33.04  ? 169 ARG A O   1 
ATOM   1315 C  CB  . ARG A 1 174 ? 23.770 13.027 8.899  1.00 34.77  ? 169 ARG A CB  1 
ATOM   1316 C  CG  . ARG A 1 174 ? 22.424 12.805 8.246  1.00 35.52  ? 169 ARG A CG  1 
ATOM   1317 C  CD  . ARG A 1 174 ? 22.586 12.318 6.816  1.00 37.62  ? 169 ARG A CD  1 
ATOM   1318 N  NE  . ARG A 1 174 ? 21.332 11.725 6.372  1.00 37.92  ? 169 ARG A NE  1 
ATOM   1319 C  CZ  . ARG A 1 174 ? 21.080 11.293 5.131  1.00 42.40  ? 169 ARG A CZ  1 
ATOM   1320 N  NH1 . ARG A 1 174 ? 22.006 11.344 4.190  1.00 39.65  ? 169 ARG A NH1 1 
ATOM   1321 N  NH2 . ARG A 1 174 ? 19.913 10.749 4.858  1.00 40.57  ? 169 ARG A NH2 1 
ATOM   1322 N  N   . LEU A 1 175 ? 23.552 11.841 11.757 1.00 31.08  ? 170 LEU A N   1 
ATOM   1323 C  CA  . LEU A 1 175 ? 22.926 10.887 12.710 1.00 34.69  ? 170 LEU A CA  1 
ATOM   1324 C  C   . LEU A 1 175 ? 22.628 11.635 14.011 1.00 34.49  ? 170 LEU A C   1 
ATOM   1325 O  O   . LEU A 1 175 ? 21.472 11.631 14.462 1.00 32.77  ? 170 LEU A O   1 
ATOM   1326 C  CB  . LEU A 1 175 ? 23.892 9.726  12.934 1.00 34.13  ? 170 LEU A CB  1 
ATOM   1327 C  CG  . LEU A 1 175 ? 24.077 8.777  11.757 1.00 32.20  ? 170 LEU A CG  1 
ATOM   1328 C  CD1 . LEU A 1 175 ? 25.118 7.750  12.097 1.00 29.90  ? 170 LEU A CD1 1 
ATOM   1329 C  CD2 . LEU A 1 175 ? 22.759 8.127  11.376 1.00 35.44  ? 170 LEU A CD2 1 
ATOM   1330 N  N   . GLY A 1 176 ? 23.611 12.362 14.554 1.00 33.00  ? 171 GLY A N   1 
ATOM   1331 C  CA  . GLY A 1 176 ? 23.363 13.114 15.804 1.00 29.54  ? 171 GLY A CA  1 
ATOM   1332 C  C   . GLY A 1 176 ? 22.261 14.135 15.665 1.00 31.26  ? 171 GLY A C   1 
ATOM   1333 O  O   . GLY A 1 176 ? 21.477 14.280 16.593 1.00 32.24  ? 171 GLY A O   1 
ATOM   1334 N  N   . LEU A 1 177 ? 22.218 14.886 14.568 1.00 31.39  ? 172 LEU A N   1 
ATOM   1335 C  CA  . LEU A 1 177 ? 21.123 15.842 14.296 1.00 35.10  ? 172 LEU A CA  1 
ATOM   1336 C  C   . LEU A 1 177 ? 19.768 15.106 14.315 1.00 33.29  ? 172 LEU A C   1 
ATOM   1337 O  O   . LEU A 1 177 ? 18.842 15.613 14.937 1.00 33.93  ? 172 LEU A O   1 
ATOM   1338 C  CB  . LEU A 1 177 ? 21.371 16.534 12.953 1.00 35.65  ? 172 LEU A CB  1 
ATOM   1339 C  CG  . LEU A 1 177 ? 20.137 17.158 12.318 1.00 36.33  ? 172 LEU A CG  1 
ATOM   1340 C  CD1 . LEU A 1 177 ? 19.647 18.340 13.119 1.00 38.23  ? 172 LEU A CD1 1 
ATOM   1341 C  CD2 . LEU A 1 177 ? 20.402 17.581 10.879 1.00 42.53  ? 172 LEU A CD2 1 
ATOM   1342 N  N   . ALA A 1 178 ? 19.656 14.005 13.585 1.00 37.05  ? 173 ALA A N   1 
ATOM   1343 C  CA  . ALA A 1 178 ? 18.404 13.213 13.468 1.00 39.29  ? 173 ALA A CA  1 
ATOM   1344 C  C   . ALA A 1 178 ? 17.993 12.678 14.854 1.00 34.99  ? 173 ALA A C   1 
ATOM   1345 O  O   . ALA A 1 178 ? 16.839 12.861 15.231 1.00 38.49  ? 173 ALA A O   1 
ATOM   1346 C  CB  . ALA A 1 178 ? 18.622 12.094 12.489 1.00 36.05  ? 173 ALA A CB  1 
ATOM   1347 N  N   . LEU A 1 179 ? 18.932 12.094 15.603 1.00 35.90  ? 174 LEU A N   1 
ATOM   1348 C  CA  . LEU A 1 179 ? 18.699 11.701 17.026 1.00 33.21  ? 174 LEU A CA  1 
ATOM   1349 C  C   . LEU A 1 179 ? 18.103 12.895 17.780 1.00 35.45  ? 174 LEU A C   1 
ATOM   1350 O  O   . LEU A 1 179 ? 17.038 12.766 18.401 1.00 38.89  ? 174 LEU A O   1 
ATOM   1351 C  CB  . LEU A 1 179 ? 20.002 11.205 17.653 1.00 34.83  ? 174 LEU A CB  1 
ATOM   1352 C  CG  . LEU A 1 179 ? 19.902 10.787 19.136 1.00 34.35  ? 174 LEU A CG  1 
ATOM   1353 C  CD1 . LEU A 1 179 ? 18.883 9.675  19.308 1.00 37.13  ? 174 LEU A CD1 1 
ATOM   1354 C  CD2 . LEU A 1 179 ? 21.245 10.329 19.656 1.00 32.94  ? 174 LEU A CD2 1 
ATOM   1355 N  N   . ASN A 1 180 ? 18.721 14.065 17.693 1.00 34.22  ? 175 ASN A N   1 
ATOM   1356 C  CA  . ASN A 1 180 ? 18.288 15.214 18.521 1.00 35.36  ? 175 ASN A CA  1 
ATOM   1357 C  C   . ASN A 1 180 ? 16.943 15.762 18.024 1.00 40.49  ? 175 ASN A C   1 
ATOM   1358 O  O   . ASN A 1 180 ? 16.130 16.159 18.884 1.00 36.17  ? 175 ASN A O   1 
ATOM   1359 C  CB  . ASN A 1 180 ? 19.383 16.277 18.619 1.00 32.24  ? 175 ASN A CB  1 
ATOM   1360 C  CG  . ASN A 1 180 ? 20.566 15.822 19.453 1.00 33.16  ? 175 ASN A CG  1 
ATOM   1361 O  OD1 . ASN A 1 180 ? 20.713 14.656 19.790 1.00 34.84  ? 175 ASN A OD1 1 
ATOM   1362 N  ND2 . ASN A 1 180 ? 21.465 16.747 19.740 1.00 32.51  ? 175 ASN A ND2 1 
ATOM   1363 N  N   . PHE A 1 181 ? 16.671 15.767 16.714 1.00 42.50  ? 176 PHE A N   1 
ATOM   1364 C  CA  . PHE A 1 181 ? 15.352 16.218 16.193 1.00 42.16  ? 176 PHE A CA  1 
ATOM   1365 C  C   . PHE A 1 181 ? 14.263 15.258 16.695 1.00 38.24  ? 176 PHE A C   1 
ATOM   1366 O  O   . PHE A 1 181 ? 13.161 15.689 17.062 1.00 43.26  ? 176 PHE A O   1 
ATOM   1367 C  CB  . PHE A 1 181 ? 15.342 16.294 14.663 1.00 42.05  ? 176 PHE A CB  1 
ATOM   1368 C  CG  . PHE A 1 181 ? 14.283 17.194 14.070 1.00 45.13  ? 176 PHE A CG  1 
ATOM   1369 C  CD1 . PHE A 1 181 ? 13.602 18.128 14.837 1.00 47.90  ? 176 PHE A CD1 1 
ATOM   1370 C  CD2 . PHE A 1 181 ? 13.980 17.125 12.714 1.00 45.38  ? 176 PHE A CD2 1 
ATOM   1371 C  CE1 . PHE A 1 181 ? 12.665 18.984 14.272 1.00 49.72  ? 176 PHE A CE1 1 
ATOM   1372 C  CE2 . PHE A 1 181 ? 13.024 17.963 12.157 1.00 44.42  ? 176 PHE A CE2 1 
ATOM   1373 C  CZ  . PHE A 1 181 ? 12.374 18.896 12.930 1.00 50.59  ? 176 PHE A CZ  1 
ATOM   1374 N  N   . SER A 1 182 ? 14.570 13.983 16.704 1.00 39.40  ? 177 SER A N   1 
ATOM   1375 C  CA  . SER A 1 182 ? 13.629 12.932 17.165 1.00 44.76  ? 177 SER A CA  1 
ATOM   1376 C  C   . SER A 1 182 ? 13.287 13.212 18.641 1.00 46.43  ? 177 SER A C   1 
ATOM   1377 O  O   . SER A 1 182 ? 12.111 13.112 19.020 1.00 41.63  ? 177 SER A O   1 
ATOM   1378 C  CB  . SER A 1 182 ? 14.182 11.555 16.913 1.00 42.38  ? 177 SER A CB  1 
ATOM   1379 O  OG  . SER A 1 182 ? 15.043 11.097 17.948 1.00 48.75  ? 177 SER A OG  1 
ATOM   1380 N  N   . VAL A 1 183 ? 14.273 13.624 19.439 1.00 46.32  ? 178 VAL A N   1 
ATOM   1381 C  CA  . VAL A 1 183 ? 14.057 13.936 20.882 1.00 41.05  ? 178 VAL A CA  1 
ATOM   1382 C  C   . VAL A 1 183 ? 13.185 15.185 20.994 1.00 41.75  ? 178 VAL A C   1 
ATOM   1383 O  O   . VAL A 1 183 ? 12.268 15.153 21.831 1.00 45.40  ? 178 VAL A O   1 
ATOM   1384 C  CB  . VAL A 1 183 ? 15.387 14.085 21.638 1.00 44.87  ? 178 VAL A CB  1 
ATOM   1385 C  CG1 . VAL A 1 183 ? 15.159 14.588 23.068 1.00 45.88  ? 178 VAL A CG1 1 
ATOM   1386 C  CG2 . VAL A 1 183 ? 16.148 12.782 21.629 1.00 38.47  ? 178 VAL A CG2 1 
ATOM   1387 N  N   . PHE A 1 184 ? 13.448 16.233 20.192 1.00 36.97  ? 179 PHE A N   1 
ATOM   1388 C  CA  . PHE A 1 184 ? 12.583 17.439 20.091 1.00 42.76  ? 179 PHE A CA  1 
ATOM   1389 C  C   . PHE A 1 184 ? 11.130 16.984 19.912 1.00 44.12  ? 179 PHE A C   1 
ATOM   1390 O  O   . PHE A 1 184 ? 10.247 17.516 20.613 1.00 48.75  ? 179 PHE A O   1 
ATOM   1391 C  CB  . PHE A 1 184 ? 13.018 18.373 18.958 1.00 36.24  ? 179 PHE A CB  1 
ATOM   1392 C  CG  . PHE A 1 184 ? 12.064 19.486 18.640 1.00 42.63  ? 179 PHE A CG  1 
ATOM   1393 C  CD1 . PHE A 1 184 ? 12.057 20.657 19.372 1.00 40.44  ? 179 PHE A CD1 1 
ATOM   1394 C  CD2 . PHE A 1 184 ? 11.179 19.366 17.575 1.00 45.93  ? 179 PHE A CD2 1 
ATOM   1395 C  CE1 . PHE A 1 184 ? 11.161 21.675 19.074 1.00 46.20  ? 179 PHE A CE1 1 
ATOM   1396 C  CE2 . PHE A 1 184 ? 10.277 20.375 17.294 1.00 43.75  ? 179 PHE A CE2 1 
ATOM   1397 C  CZ  . PHE A 1 184 ? 10.263 21.528 18.043 1.00 47.79  ? 179 PHE A CZ  1 
ATOM   1398 N  N   . HIS A 1 185 ? 10.895 16.081 18.960 1.00 47.43  ? 180 HIS A N   1 
ATOM   1399 C  CA  . HIS A 1 185 ? 9.524  15.642 18.584 1.00 46.91  ? 180 HIS A CA  1 
ATOM   1400 C  C   . HIS A 1 185 ? 8.863  14.984 19.800 1.00 43.97  ? 180 HIS A C   1 
ATOM   1401 O  O   . HIS A 1 185 ? 7.721  15.337 20.122 1.00 48.82  ? 180 HIS A O   1 
ATOM   1402 C  CB  . HIS A 1 185 ? 9.541  14.699 17.371 1.00 49.32  ? 180 HIS A CB  1 
ATOM   1403 C  CG  . HIS A 1 185 ? 9.807  15.359 16.055 1.00 47.48  ? 180 HIS A CG  1 
ATOM   1404 N  ND1 . HIS A 1 185 ? 9.247  16.557 15.693 1.00 45.47  ? 180 HIS A ND1 1 
ATOM   1405 C  CD2 . HIS A 1 185 ? 10.540 14.957 14.996 1.00 50.66  ? 180 HIS A CD2 1 
ATOM   1406 C  CE1 . HIS A 1 185 ? 9.637  16.874 14.478 1.00 45.18  ? 180 HIS A CE1 1 
ATOM   1407 N  NE2 . HIS A 1 185 ? 10.416 15.911 14.024 1.00 43.94  ? 180 HIS A NE2 1 
ATOM   1408 N  N   . TYR A 1 186 ? 9.566  14.060 20.442 1.00 46.33  ? 181 TYR A N   1 
ATOM   1409 C  CA  . TYR A 1 186 ? 9.025  13.234 21.542 1.00 51.09  ? 181 TYR A CA  1 
ATOM   1410 C  C   . TYR A 1 186 ? 8.878  14.074 22.811 1.00 56.11  ? 181 TYR A C   1 
ATOM   1411 O  O   . TYR A 1 186 ? 7.761  14.118 23.344 1.00 54.17  ? 181 TYR A O   1 
ATOM   1412 C  CB  . TYR A 1 186 ? 9.907  12.022 21.799 1.00 51.77  ? 181 TYR A CB  1 
ATOM   1413 C  CG  . TYR A 1 186 ? 9.221  10.965 22.621 1.00 58.67  ? 181 TYR A CG  1 
ATOM   1414 C  CD1 . TYR A 1 186 ? 8.434  9.998  22.016 1.00 60.09  ? 181 TYR A CD1 1 
ATOM   1415 C  CD2 . TYR A 1 186 ? 9.341  10.937 24.000 1.00 62.25  ? 181 TYR A CD2 1 
ATOM   1416 C  CE1 . TYR A 1 186 ? 7.798  9.018  22.760 1.00 65.62  ? 181 TYR A CE1 1 
ATOM   1417 C  CE2 . TYR A 1 186 ? 8.710  9.963  24.760 1.00 59.34  ? 181 TYR A CE2 1 
ATOM   1418 C  CZ  . TYR A 1 186 ? 7.933  9.008  24.135 1.00 61.58  ? 181 TYR A CZ  1 
ATOM   1419 O  OH  . TYR A 1 186 ? 7.332  8.034  24.862 1.00 68.08  ? 181 TYR A OH  1 
ATOM   1420 N  N   . GLU A 1 187 ? 9.949  14.753 23.238 1.00 49.41  ? 182 GLU A N   1 
ATOM   1421 C  CA  . GLU A 1 187 ? 10.036 15.379 24.581 1.00 46.66  ? 182 GLU A CA  1 
ATOM   1422 C  C   . GLU A 1 187 ? 9.466  16.793 24.563 1.00 46.95  ? 182 GLU A C   1 
ATOM   1423 O  O   . GLU A 1 187 ? 8.988  17.230 25.608 1.00 52.02  ? 182 GLU A O   1 
ATOM   1424 C  CB  . GLU A 1 187 ? 11.479 15.370 25.089 1.00 43.78  ? 182 GLU A CB  1 
ATOM   1425 C  CG  . GLU A 1 187 ? 12.043 13.974 25.254 1.00 46.04  ? 182 GLU A CG  1 
ATOM   1426 C  CD  . GLU A 1 187 ? 11.442 13.085 26.339 1.00 48.07  ? 182 GLU A CD  1 
ATOM   1427 O  OE1 . GLU A 1 187 ? 10.644 13.585 27.135 1.00 55.70  ? 182 GLU A OE1 1 
ATOM   1428 O  OE2 . GLU A 1 187 ? 11.811 11.898 26.397 1.00 47.65  ? 182 GLU A OE2 1 
ATOM   1429 N  N   . ILE A 1 188 ? 9.569  17.521 23.459 1.00 48.49  ? 183 ILE A N   1 
ATOM   1430 C  CA  . ILE A 1 188 ? 9.204  18.960 23.431 1.00 50.53  ? 183 ILE A CA  1 
ATOM   1431 C  C   . ILE A 1 188 ? 7.886  19.145 22.683 1.00 51.41  ? 183 ILE A C   1 
ATOM   1432 O  O   . ILE A 1 188 ? 7.069  19.937 23.142 1.00 46.45  ? 183 ILE A O   1 
ATOM   1433 C  CB  . ILE A 1 188 ? 10.341 19.766 22.787 1.00 50.96  ? 183 ILE A CB  1 
ATOM   1434 C  CG1 . ILE A 1 188 ? 11.679 19.431 23.451 1.00 53.16  ? 183 ILE A CG1 1 
ATOM   1435 C  CG2 . ILE A 1 188 ? 10.029 21.257 22.793 1.00 47.87  ? 183 ILE A CG2 1 
ATOM   1436 C  CD1 . ILE A 1 188 ? 11.840 20.012 24.841 1.00 49.93  ? 183 ILE A CD1 1 
ATOM   1437 N  N   . ALA A 1 189 ? 7.739  18.516 21.522 1.00 55.45  ? 184 ALA A N   1 
ATOM   1438 C  CA  . ALA A 1 189 ? 6.672  18.870 20.562 1.00 58.76  ? 184 ALA A CA  1 
ATOM   1439 C  C   . ALA A 1 189 ? 5.460  17.951 20.760 1.00 62.64  ? 184 ALA A C   1 
ATOM   1440 O  O   . ALA A 1 189 ? 4.487  18.099 20.009 1.00 71.27  ? 184 ALA A O   1 
ATOM   1441 C  CB  . ALA A 1 189 ? 7.215  18.810 19.160 1.00 59.76  ? 184 ALA A CB  1 
ATOM   1442 N  N   . ASN A 1 190 ? 5.507  17.035 21.727 1.00 63.32  ? 185 ASN A N   1 
ATOM   1443 C  CA  . ASN A 1 190 ? 4.380  16.111 22.009 1.00 68.92  ? 185 ASN A CA  1 
ATOM   1444 C  C   . ASN A 1 190 ? 3.961  15.430 20.694 1.00 70.93  ? 185 ASN A C   1 
ATOM   1445 O  O   . ASN A 1 190 ? 2.768  15.424 20.419 1.00 73.41  ? 185 ASN A O   1 
ATOM   1446 C  CB  . ASN A 1 190 ? 3.217  16.876 22.653 1.00 60.17  ? 185 ASN A CB  1 
ATOM   1447 N  N   . SER A 1 191 ? 4.906  14.936 19.884 1.00 68.44  ? 186 SER A N   1 
ATOM   1448 C  CA  . SER A 1 191 ? 4.645  14.295 18.562 1.00 58.53  ? 186 SER A CA  1 
ATOM   1449 C  C   . SER A 1 191 ? 5.350  12.952 18.479 1.00 51.78  ? 186 SER A C   1 
ATOM   1450 O  O   . SER A 1 191 ? 6.233  12.743 17.649 1.00 53.72  ? 186 SER A O   1 
ATOM   1451 C  CB  . SER A 1 191 ? 5.061  15.174 17.426 1.00 59.20  ? 186 SER A CB  1 
ATOM   1452 O  OG  . SER A 1 191 ? 4.430  16.435 17.529 1.00 72.37  ? 186 SER A OG  1 
ATOM   1453 N  N   . PRO A 1 192 ? 4.976  11.982 19.328 1.00 55.71  ? 187 PRO A N   1 
ATOM   1454 C  CA  . PRO A 1 192 ? 5.691  10.710 19.386 1.00 55.35  ? 187 PRO A CA  1 
ATOM   1455 C  C   . PRO A 1 192 ? 5.768  10.010 18.022 1.00 62.63  ? 187 PRO A C   1 
ATOM   1456 O  O   . PRO A 1 192 ? 6.722  9.281  17.788 1.00 59.58  ? 187 PRO A O   1 
ATOM   1457 C  CB  . PRO A 1 192 ? 4.889  9.861  20.383 1.00 57.41  ? 187 PRO A CB  1 
ATOM   1458 C  CG  . PRO A 1 192 ? 3.576  10.577 20.534 1.00 54.69  ? 187 PRO A CG  1 
ATOM   1459 C  CD  . PRO A 1 192 ? 3.824  12.039 20.235 1.00 56.80  ? 187 PRO A CD  1 
ATOM   1460 N  N   . GLU A 1 193 ? 4.757  10.216 17.176 1.00 64.88  ? 188 GLU A N   1 
ATOM   1461 C  CA  . GLU A 1 193 ? 4.667  9.568  15.841 1.00 65.47  ? 188 GLU A CA  1 
ATOM   1462 C  C   . GLU A 1 193 ? 5.827  10.070 14.982 1.00 52.53  ? 188 GLU A C   1 
ATOM   1463 O  O   . GLU A 1 193 ? 6.567  9.226  14.435 1.00 54.10  ? 188 GLU A O   1 
ATOM   1464 C  CB  . GLU A 1 193 ? 3.297  9.831  15.204 1.00 67.49  ? 188 GLU A CB  1 
ATOM   1465 C  CG  . GLU A 1 193 ? 2.373  8.621  15.247 1.00 78.50  ? 188 GLU A CG  1 
ATOM   1466 C  CD  . GLU A 1 193 ? 2.132  8.018  16.623 1.00 80.50  ? 188 GLU A CD  1 
ATOM   1467 O  OE1 . GLU A 1 193 ? 2.712  6.944  16.906 1.00 74.44  ? 188 GLU A OE1 1 
ATOM   1468 O  OE2 . GLU A 1 193 ? 1.349  8.615  17.404 1.00 89.45  ? 188 GLU A OE2 1 
ATOM   1469 N  N   . GLU A 1 194 ? 5.958  11.394 14.879 1.00 60.48  ? 189 GLU A N   1 
ATOM   1470 C  CA  . GLU A 1 194 ? 7.046  12.067 14.120 1.00 62.22  ? 189 GLU A CA  1 
ATOM   1471 C  C   . GLU A 1 194 ? 8.394  11.544 14.632 1.00 59.04  ? 189 GLU A C   1 
ATOM   1472 O  O   . GLU A 1 194 ? 9.259  11.222 13.806 1.00 59.40  ? 189 GLU A O   1 
ATOM   1473 C  CB  . GLU A 1 194 ? 6.936  13.585 14.241 1.00 65.23  ? 189 GLU A CB  1 
ATOM   1474 C  CG  . GLU A 1 194 ? 5.608  14.148 13.772 1.00 78.38  ? 189 GLU A CG  1 
ATOM   1475 C  CD  . GLU A 1 194 ? 5.662  15.589 13.284 1.00 84.87  ? 189 GLU A CD  1 
ATOM   1476 O  OE1 . GLU A 1 194 ? 5.800  15.788 12.068 1.00 91.54  ? 189 GLU A OE1 1 
ATOM   1477 O  OE2 . GLU A 1 194 ? 5.555  16.512 14.117 1.00 92.04  ? 189 GLU A OE2 1 
ATOM   1478 N  N   . ALA A 1 195 ? 8.532  11.387 15.951 1.00 56.30  ? 190 ALA A N   1 
ATOM   1479 C  CA  . ALA A 1 195 ? 9.792  10.966 16.598 1.00 51.89  ? 190 ALA A CA  1 
ATOM   1480 C  C   . ALA A 1 195 ? 10.135 9.565  16.134 1.00 49.82  ? 190 ALA A C   1 
ATOM   1481 O  O   . ALA A 1 195 ? 11.255 9.346  15.661 1.00 45.85  ? 190 ALA A O   1 
ATOM   1482 C  CB  . ALA A 1 195 ? 9.678  11.004 18.108 1.00 56.97  ? 190 ALA A CB  1 
ATOM   1483 N  N   . ILE A 1 196 ? 9.197  8.639  16.308 1.00 47.97  ? 191 ILE A N   1 
ATOM   1484 C  CA  . ILE A 1 196 ? 9.444  7.205  16.003 1.00 51.13  ? 191 ILE A CA  1 
ATOM   1485 C  C   . ILE A 1 196 ? 9.774  7.089  14.513 1.00 46.66  ? 191 ILE A C   1 
ATOM   1486 O  O   . ILE A 1 196 ? 10.674 6.299  14.177 1.00 48.14  ? 191 ILE A O   1 
ATOM   1487 C  CB  . ILE A 1 196 ? 8.246  6.331  16.428 1.00 54.51  ? 191 ILE A CB  1 
ATOM   1488 C  CG1 . ILE A 1 196 ? 8.099  6.329  17.955 1.00 54.58  ? 191 ILE A CG1 1 
ATOM   1489 C  CG2 . ILE A 1 196 ? 8.380  4.910  15.877 1.00 54.56  ? 191 ILE A CG2 1 
ATOM   1490 C  CD1 . ILE A 1 196 ? 6.696  6.037  18.440 1.00 56.82  ? 191 ILE A CD1 1 
ATOM   1491 N  N   . SER A 1 197 ? 9.052  7.820  13.669 1.00 47.58  ? 192 SER A N   1 
ATOM   1492 C  CA  . SER A 1 197 ? 9.212  7.740  12.192 1.00 54.43  ? 192 SER A CA  1 
ATOM   1493 C  C   . SER A 1 197 ? 10.637 8.198  11.831 1.00 51.76  ? 192 SER A C   1 
ATOM   1494 O  O   . SER A 1 197 ? 11.400 7.422  11.177 1.00 47.95  ? 192 SER A O   1 
ATOM   1495 C  CB  . SER A 1 197 ? 8.154  8.552  11.484 1.00 54.83  ? 192 SER A CB  1 
ATOM   1496 O  OG  . SER A 1 197 ? 8.761  9.522  10.649 1.00 69.96  ? 192 SER A OG  1 
ATOM   1497 N  N   . LEU A 1 198 ? 11.011 9.391  12.294 1.00 49.91  ? 193 LEU A N   1 
ATOM   1498 C  CA  . LEU A 1 198 ? 12.368 9.947  12.048 1.00 44.61  ? 193 LEU A CA  1 
ATOM   1499 C  C   . LEU A 1 198 ? 13.431 8.969  12.551 1.00 41.16  ? 193 LEU A C   1 
ATOM   1500 O  O   . LEU A 1 198 ? 14.352 8.613  11.770 1.00 42.48  ? 193 LEU A O   1 
ATOM   1501 C  CB  . LEU A 1 198 ? 12.498 11.321 12.698 1.00 43.97  ? 193 LEU A CB  1 
ATOM   1502 C  CG  . LEU A 1 198 ? 13.881 11.947 12.536 1.00 44.36  ? 193 LEU A CG  1 
ATOM   1503 C  CD1 . LEU A 1 198 ? 14.295 12.006 11.072 1.00 48.15  ? 193 LEU A CD1 1 
ATOM   1504 C  CD2 . LEU A 1 198 ? 13.897 13.328 13.134 1.00 49.34  ? 193 LEU A CD2 1 
ATOM   1505 N  N   . ALA A 1 199 ? 13.306 8.474  13.786 1.00 41.73  ? 194 ALA A N   1 
ATOM   1506 C  CA  . ALA A 1 199 ? 14.357 7.614  14.366 1.00 40.79  ? 194 ALA A CA  1 
ATOM   1507 C  C   . ALA A 1 199 ? 14.507 6.341  13.537 1.00 40.76  ? 194 ALA A C   1 
ATOM   1508 O  O   . ALA A 1 199 ? 15.642 5.858  13.360 1.00 43.12  ? 194 ALA A O   1 
ATOM   1509 C  CB  . ALA A 1 199 ? 14.053 7.295  15.811 1.00 45.61  ? 194 ALA A CB  1 
ATOM   1510 N  N   . LYS A 1 200 ? 13.390 5.708  13.195 1.00 46.34  ? 195 LYS A N   1 
ATOM   1511 C  CA  . LYS A 1 200 ? 13.386 4.416  12.456 1.00 43.80  ? 195 LYS A CA  1 
ATOM   1512 C  C   . LYS A 1 200 ? 13.976 4.632  11.045 1.00 37.29  ? 195 LYS A C   1 
ATOM   1513 O  O   . LYS A 1 200 ? 14.888 3.876  10.675 1.00 41.63  ? 195 LYS A O   1 
ATOM   1514 C  CB  . LYS A 1 200 ? 11.959 3.850  12.395 1.00 48.29  ? 195 LYS A CB  1 
ATOM   1515 C  CG  . LYS A 1 200 ? 11.824 2.659  11.460 1.00 50.31  ? 195 LYS A CG  1 
ATOM   1516 C  CD  . LYS A 1 200 ? 10.606 1.793  11.645 1.00 54.42  ? 195 LYS A CD  1 
ATOM   1517 C  CE  . LYS A 1 200 ? 10.719 0.503  10.857 1.00 52.31  ? 195 LYS A CE  1 
ATOM   1518 N  NZ  . LYS A 1 200 ? 11.785 -0.374 11.395 1.00 58.10  ? 195 LYS A NZ  1 
ATOM   1519 N  N   . THR A 1 201 ? 13.501 5.636  10.312 1.00 40.40  ? 196 THR A N   1 
ATOM   1520 C  CA  . THR A 1 201 ? 14.037 6.010  8.972  1.00 49.51  ? 196 THR A CA  1 
ATOM   1521 C  C   . THR A 1 201 ? 15.557 6.212  9.090  1.00 50.28  ? 196 THR A C   1 
ATOM   1522 O  O   . THR A 1 201 ? 16.324 5.703  8.237  1.00 45.88  ? 196 THR A O   1 
ATOM   1523 C  CB  . THR A 1 201 ? 13.436 7.317  8.434  1.00 51.05  ? 196 THR A CB  1 
ATOM   1524 O  OG1 . THR A 1 201 ? 12.015 7.263  8.434  1.00 53.44  ? 196 THR A OG1 1 
ATOM   1525 C  CG2 . THR A 1 201 ? 13.903 7.640  7.030  1.00 56.07  ? 196 THR A CG2 1 
ATOM   1526 N  N   . THR A 1 202 ? 15.994 6.922  10.131 1.00 47.80  ? 197 THR A N   1 
ATOM   1527 C  CA  . THR A 1 202 ? 17.428 7.288  10.281 1.00 41.32  ? 197 THR A CA  1 
ATOM   1528 C  C   . THR A 1 202 ? 18.239 6.029  10.495 1.00 37.47  ? 197 THR A C   1 
ATOM   1529 O  O   . THR A 1 202 ? 19.239 5.844  9.771  1.00 35.81  ? 197 THR A O   1 
ATOM   1530 C  CB  . THR A 1 202 ? 17.647 8.311  11.394 1.00 38.47  ? 197 THR A CB  1 
ATOM   1531 O  OG1 . THR A 1 202 ? 16.744 9.373  11.112 1.00 36.47  ? 197 THR A OG1 1 
ATOM   1532 C  CG2 . THR A 1 202 ? 19.068 8.825  11.411 1.00 45.10  ? 197 THR A CG2 1 
ATOM   1533 N  N   . PHE A 1 203 ? 17.810 5.165  11.416 1.00 36.68  ? 198 PHE A N   1 
ATOM   1534 C  CA  . PHE A 1 203 ? 18.525 3.896  11.689 1.00 34.77  ? 198 PHE A CA  1 
ATOM   1535 C  C   . PHE A 1 203 ? 18.565 3.055  10.394 1.00 37.47  ? 198 PHE A C   1 
ATOM   1536 O  O   . PHE A 1 203 ? 19.645 2.531  10.025 1.00 34.94  ? 198 PHE A O   1 
ATOM   1537 C  CB  . PHE A 1 203 ? 17.873 3.124  12.842 1.00 34.31  ? 198 PHE A CB  1 
ATOM   1538 C  CG  . PHE A 1 203 ? 18.575 1.843  13.191 1.00 31.63  ? 198 PHE A CG  1 
ATOM   1539 C  CD1 . PHE A 1 203 ? 19.609 1.818  14.107 1.00 35.92  ? 198 PHE A CD1 1 
ATOM   1540 C  CD2 . PHE A 1 203 ? 18.190 0.639  12.621 1.00 34.35  ? 198 PHE A CD2 1 
ATOM   1541 C  CE1 . PHE A 1 203 ? 20.304 0.648  14.378 1.00 37.29  ? 198 PHE A CE1 1 
ATOM   1542 C  CE2 . PHE A 1 203 ? 18.865 -0.537 12.912 1.00 34.51  ? 198 PHE A CE2 1 
ATOM   1543 C  CZ  . PHE A 1 203 ? 19.919 -0.542 13.792 1.00 37.61  ? 198 PHE A CZ  1 
ATOM   1544 N  N   . ASP A 1 204 ? 17.403 2.846  9.782  1.00 40.29  ? 199 ASP A N   1 
ATOM   1545 C  CA  . ASP A 1 204 ? 17.256 1.891  8.641  1.00 42.37  ? 199 ASP A CA  1 
ATOM   1546 C  C   . ASP A 1 204 ? 18.136 2.373  7.473  1.00 32.88  ? 199 ASP A C   1 
ATOM   1547 O  O   . ASP A 1 204 ? 18.851 1.561  6.931  1.00 41.81  ? 199 ASP A O   1 
ATOM   1548 C  CB  . ASP A 1 204 ? 15.769 1.704  8.283  1.00 41.22  ? 199 ASP A CB  1 
ATOM   1549 C  CG  . ASP A 1 204 ? 14.980 0.868  9.301  1.00 39.79  ? 199 ASP A CG  1 
ATOM   1550 O  OD1 . ASP A 1 204 ? 15.598 0.079  10.052 1.00 40.46  ? 199 ASP A OD1 1 
ATOM   1551 O  OD2 . ASP A 1 204 ? 13.744 1.023  9.331  1.00 44.90  ? 199 ASP A OD2 1 
ATOM   1552 N  N   . GLU A 1 205 ? 18.101 3.654  7.149  1.00 43.66  ? 200 GLU A N   1 
ATOM   1553 C  CA  . GLU A 1 205 ? 18.899 4.221  6.025  1.00 45.90  ? 200 GLU A CA  1 
ATOM   1554 C  C   . GLU A 1 205 ? 20.391 4.107  6.333  1.00 48.95  ? 200 GLU A C   1 
ATOM   1555 O  O   . GLU A 1 205 ? 21.173 3.753  5.396  1.00 42.78  ? 200 GLU A O   1 
ATOM   1556 C  CB  . GLU A 1 205 ? 18.401 5.620  5.704  1.00 49.54  ? 200 GLU A CB  1 
ATOM   1557 C  CG  . GLU A 1 205 ? 17.022 5.598  5.067  1.00 49.34  ? 200 GLU A CG  1 
ATOM   1558 C  CD  . GLU A 1 205 ? 16.555 6.957  4.602  1.00 56.80  ? 200 GLU A CD  1 
ATOM   1559 O  OE1 . GLU A 1 205 ? 17.297 7.939  4.840  1.00 55.35  ? 200 GLU A OE1 1 
ATOM   1560 O  OE2 . GLU A 1 205 ? 15.455 7.042  4.002  1.00 61.00  ? 200 GLU A OE2 1 
ATOM   1561 N  N   . ALA A 1 206 ? 20.808 4.256  7.601  1.00 43.48  ? 201 ALA A N   1 
ATOM   1562 C  CA  . ALA A 1 206 ? 22.239 4.116  7.941  1.00 34.90  ? 201 ALA A CA  1 
ATOM   1563 C  C   . ALA A 1 206 ? 22.625 2.687  7.680  1.00 31.18  ? 201 ALA A C   1 
ATOM   1564 O  O   . ALA A 1 206 ? 23.774 2.436  7.194  1.00 35.61  ? 201 ALA A O   1 
ATOM   1565 C  CB  . ALA A 1 206 ? 22.533 4.475  9.390  1.00 37.51  ? 201 ALA A CB  1 
ATOM   1566 N  N   . MET A 1 207 ? 21.798 1.749  8.174  1.00 31.80  ? 202 MET A N   1 
ATOM   1567 C  CA  . MET A 1 207 ? 22.158 0.307  8.085  1.00 32.81  ? 202 MET A CA  1 
ATOM   1568 C  C   . MET A 1 207 ? 22.182 -0.111 6.584  1.00 34.97  ? 202 MET A C   1 
ATOM   1569 O  O   . MET A 1 207 ? 22.985 -0.940 6.219  1.00 34.24  ? 202 MET A O   1 
ATOM   1570 C  CB  . MET A 1 207 ? 21.121 -0.540 8.834  1.00 38.03  ? 202 MET A CB  1 
ATOM   1571 C  CG  . MET A 1 207 ? 21.319 -0.508 10.374 1.00 37.94  ? 202 MET A CG  1 
ATOM   1572 S  SD  . MET A 1 207 ? 22.761 -1.425 10.913 1.00 47.92  ? 202 MET A SD  1 
ATOM   1573 C  CE  . MET A 1 207 ? 22.493 -2.981 10.080 1.00 54.23  ? 202 MET A CE  1 
ATOM   1574 N  N   . ALA A 1 208 ? 21.261 0.422  5.790  1.00 37.88  ? 203 ALA A N   1 
ATOM   1575 C  CA  . ALA A 1 208 ? 21.124 0.153  4.328  1.00 47.60  ? 203 ALA A CA  1 
ATOM   1576 C  C   . ALA A 1 208 ? 22.413 0.582  3.593  1.00 46.55  ? 203 ALA A C   1 
ATOM   1577 O  O   . ALA A 1 208 ? 22.879 -0.180 2.733  1.00 55.76  ? 203 ALA A O   1 
ATOM   1578 C  CB  . ALA A 1 208 ? 19.898 0.864  3.807  1.00 42.71  ? 203 ALA A CB  1 
ATOM   1579 N  N   . ASP A 1 209 ? 23.030 1.680  4.047  1.00 39.56  ? 204 ASP A N   1 
ATOM   1580 C  CA  . ASP A 1 209 ? 24.235 2.281  3.429  1.00 38.31  ? 204 ASP A CA  1 
ATOM   1581 C  C   . ASP A 1 209 ? 25.375 2.262  4.462  1.00 42.11  ? 204 ASP A C   1 
ATOM   1582 O  O   . ASP A 1 209 ? 26.182 3.240  4.498  1.00 41.97  ? 204 ASP A O   1 
ATOM   1583 C  CB  . ASP A 1 209 ? 23.879 3.651  2.839  1.00 36.66  ? 204 ASP A CB  1 
ATOM   1584 C  CG  . ASP A 1 209 ? 23.139 3.604  1.505  1.00 38.32  ? 204 ASP A CG  1 
ATOM   1585 O  OD1 . ASP A 1 209 ? 23.329 2.644  0.809  1.00 39.46  ? 204 ASP A OD1 1 
ATOM   1586 O  OD2 . ASP A 1 209 ? 22.297 4.470  1.266  1.00 39.54  ? 204 ASP A OD2 1 
ATOM   1587 N  N   . LEU A 1 210 ? 25.518 1.139  5.167  1.00 40.37  ? 205 LEU A N   1 
ATOM   1588 C  CA  . LEU A 1 210 ? 26.563 0.910  6.201  1.00 40.47  ? 205 LEU A CA  1 
ATOM   1589 C  C   . LEU A 1 210 ? 27.951 1.035  5.588  1.00 41.31  ? 205 LEU A C   1 
ATOM   1590 O  O   . LEU A 1 210 ? 28.881 1.486  6.294  1.00 37.01  ? 205 LEU A O   1 
ATOM   1591 C  CB  . LEU A 1 210 ? 26.417 -0.481 6.817  1.00 39.16  ? 205 LEU A CB  1 
ATOM   1592 C  CG  . LEU A 1 210 ? 27.162 -0.646 8.134  1.00 43.23  ? 205 LEU A CG  1 
ATOM   1593 C  CD1 . LEU A 1 210 ? 26.505 0.249  9.192  1.00 38.51  ? 205 LEU A CD1 1 
ATOM   1594 C  CD2 . LEU A 1 210 ? 27.199 -2.111 8.557  1.00 47.87  ? 205 LEU A CD2 1 
ATOM   1595 N  N   . HIS A 1 211 ? 28.097 0.652  4.312  1.00 38.26  ? 206 HIS A N   1 
ATOM   1596 C  CA  . HIS A 1 211 ? 29.375 0.775  3.562  1.00 33.55  ? 206 HIS A CA  1 
ATOM   1597 C  C   . HIS A 1 211 ? 29.881 2.236  3.585  1.00 29.85  ? 206 HIS A C   1 
ATOM   1598 O  O   . HIS A 1 211 ? 31.032 2.404  3.294  1.00 34.88  ? 206 HIS A O   1 
ATOM   1599 C  CB  . HIS A 1 211 ? 29.200 0.276  2.095  1.00 35.23  ? 206 HIS A CB  1 
ATOM   1600 C  CG  . HIS A 1 211 ? 28.301 1.128  1.272  1.00 33.09  ? 206 HIS A CG  1 
ATOM   1601 N  ND1 . HIS A 1 211 ? 26.922 1.035  1.351  1.00 36.59  ? 206 HIS A ND1 1 
ATOM   1602 C  CD2 . HIS A 1 211 ? 28.569 2.104  0.365  1.00 38.24  ? 206 HIS A CD2 1 
ATOM   1603 C  CE1 . HIS A 1 211 ? 26.381 1.937  0.536  1.00 38.09  ? 206 HIS A CE1 1 
ATOM   1604 N  NE2 . HIS A 1 211 ? 27.381 2.585  -0.102 1.00 36.55  ? 206 HIS A NE2 1 
ATOM   1605 N  N   . THR A 1 212 ? 29.049 3.238  3.856  1.00 31.04  ? 207 THR A N   1 
ATOM   1606 C  CA  . THR A 1 212 ? 29.440 4.673  3.857  1.00 33.46  ? 207 THR A CA  1 
ATOM   1607 C  C   . THR A 1 212 ? 30.137 5.101  5.163  1.00 41.72  ? 207 THR A C   1 
ATOM   1608 O  O   . THR A 1 212 ? 30.487 6.305  5.262  1.00 34.64  ? 207 THR A O   1 
ATOM   1609 C  CB  . THR A 1 212 ? 28.244 5.568  3.562  1.00 35.38  ? 207 THR A CB  1 
ATOM   1610 O  OG1 . THR A 1 212 ? 27.293 5.531  4.641  1.00 33.83  ? 207 THR A OG1 1 
ATOM   1611 C  CG2 . THR A 1 212 ? 27.636 5.193  2.214  1.00 36.87  ? 207 THR A CG2 1 
ATOM   1612 N  N   . LEU A 1 213 ? 30.310 4.201  6.139  1.00 37.39  ? 208 LEU A N   1 
ATOM   1613 C  CA  . LEU A 1 213 ? 31.032 4.547  7.397  1.00 34.70  ? 208 LEU A CA  1 
ATOM   1614 C  C   . LEU A 1 213 ? 32.429 5.093  7.047  1.00 34.69  ? 208 LEU A C   1 
ATOM   1615 O  O   . LEU A 1 213 ? 33.135 4.470  6.240  1.00 36.79  ? 208 LEU A O   1 
ATOM   1616 C  CB  . LEU A 1 213 ? 31.159 3.296  8.269  1.00 35.27  ? 208 LEU A CB  1 
ATOM   1617 C  CG  . LEU A 1 213 ? 29.889 2.856  8.982  1.00 31.74  ? 208 LEU A CG  1 
ATOM   1618 C  CD1 . LEU A 1 213 ? 30.145 1.536  9.642  1.00 31.78  ? 208 LEU A CD1 1 
ATOM   1619 C  CD2 . LEU A 1 213 ? 29.409 3.891  9.995  1.00 35.06  ? 208 LEU A CD2 1 
ATOM   1620 N  N   . SER A 1 214 ? 32.867 6.162  7.714  1.00 36.35  ? 209 SER A N   1 
ATOM   1621 C  CA  . SER A 1 214 ? 34.227 6.725  7.507  1.00 35.22  ? 209 SER A CA  1 
ATOM   1622 C  C   . SER A 1 214 ? 35.199 6.109  8.513  1.00 36.19  ? 209 SER A C   1 
ATOM   1623 O  O   . SER A 1 214 ? 34.827 5.987  9.706  1.00 35.78  ? 209 SER A O   1 
ATOM   1624 C  CB  . SER A 1 214 ? 34.229 8.245  7.576  1.00 37.90  ? 209 SER A CB  1 
ATOM   1625 O  OG  . SER A 1 214 ? 35.581 8.684  7.597  1.00 47.15  ? 209 SER A OG  1 
ATOM   1626 N  N   . GLU A 1 215 ? 36.405 5.761  8.042  1.00 31.27  ? 210 GLU A N   1 
ATOM   1627 C  CA  . GLU A 1 215 ? 37.558 5.280  8.836  1.00 39.90  ? 210 GLU A CA  1 
ATOM   1628 C  C   . GLU A 1 215 ? 37.831 6.156  10.073 1.00 44.69  ? 210 GLU A C   1 
ATOM   1629 O  O   . GLU A 1 215 ? 38.313 5.581  11.055 1.00 44.32  ? 210 GLU A O   1 
ATOM   1630 C  CB  . GLU A 1 215 ? 38.838 5.323  8.020  1.00 44.94  ? 210 GLU A CB  1 
ATOM   1631 C  CG  . GLU A 1 215 ? 38.894 4.295  6.927  1.00 51.08  ? 210 GLU A CG  1 
ATOM   1632 C  CD  . GLU A 1 215 ? 40.141 4.359  6.070  1.00 58.60  ? 210 GLU A CD  1 
ATOM   1633 O  OE1 . GLU A 1 215 ? 41.249 4.041  6.588  1.00 57.38  ? 210 GLU A OE1 1 
ATOM   1634 O  OE2 . GLU A 1 215 ? 39.994 4.714  4.873  1.00 71.24  ? 210 GLU A OE2 1 
ATOM   1635 N  N   . ASP A 1 216 ? 37.583 7.470  10.035 1.00 38.25  ? 211 ASP A N   1 
ATOM   1636 C  CA  . ASP A 1 216 ? 37.928 8.377  11.169 1.00 47.49  ? 211 ASP A CA  1 
ATOM   1637 C  C   . ASP A 1 216 ? 36.742 8.598  12.115 1.00 44.88  ? 211 ASP A C   1 
ATOM   1638 O  O   . ASP A 1 216 ? 36.978 9.224  13.167 1.00 47.31  ? 211 ASP A O   1 
ATOM   1639 C  CB  . ASP A 1 216 ? 38.425 9.740  10.678 1.00 58.14  ? 211 ASP A CB  1 
ATOM   1640 C  CG  . ASP A 1 216 ? 37.564 10.281 9.549  1.00 68.22  ? 211 ASP A CG  1 
ATOM   1641 O  OD1 . ASP A 1 216 ? 36.417 10.704 9.834  1.00 73.35  ? 211 ASP A OD1 1 
ATOM   1642 O  OD2 . ASP A 1 216 ? 38.017 10.199 8.381  1.00 72.73  ? 211 ASP A OD2 1 
ATOM   1643 N  N   . SER A 1 217 ? 35.513 8.171  11.784 1.00 38.87  ? 212 SER A N   1 
ATOM   1644 C  CA  . SER A 1 217 ? 34.317 8.506  12.600 1.00 33.55  ? 212 SER A CA  1 
ATOM   1645 C  C   . SER A 1 217 ? 33.351 7.318  12.821 1.00 30.84  ? 212 SER A C   1 
ATOM   1646 O  O   . SER A 1 217 ? 32.253 7.576  13.335 1.00 32.28  ? 212 SER A O   1 
ATOM   1647 C  CB  . SER A 1 217 ? 33.592 9.654  11.940 1.00 34.76  ? 212 SER A CB  1 
ATOM   1648 O  OG  . SER A 1 217 ? 33.224 9.296  10.612 1.00 37.19  ? 212 SER A OG  1 
ATOM   1649 N  N   . TYR A 1 218 ? 33.672 6.096  12.410 1.00 31.77  ? 213 TYR A N   1 
ATOM   1650 C  CA  . TYR A 1 218 ? 32.697 4.965  12.434 1.00 32.64  ? 213 TYR A CA  1 
ATOM   1651 C  C   . TYR A 1 218 ? 32.255 4.674  13.881 1.00 35.33  ? 213 TYR A C   1 
ATOM   1652 O  O   . TYR A 1 218 ? 31.069 4.350  14.093 1.00 34.38  ? 213 TYR A O   1 
ATOM   1653 C  CB  . TYR A 1 218 ? 33.270 3.729  11.741 1.00 28.59  ? 213 TYR A CB  1 
ATOM   1654 C  CG  . TYR A 1 218 ? 34.406 3.016  12.411 1.00 31.74  ? 213 TYR A CG  1 
ATOM   1655 C  CD1 . TYR A 1 218 ? 34.163 1.999  13.322 1.00 33.97  ? 213 TYR A CD1 1 
ATOM   1656 C  CD2 . TYR A 1 218 ? 35.722 3.337  12.141 1.00 32.80  ? 213 TYR A CD2 1 
ATOM   1657 C  CE1 . TYR A 1 218 ? 35.191 1.343  13.957 1.00 30.86  ? 213 TYR A CE1 1 
ATOM   1658 C  CE2 . TYR A 1 218 ? 36.765 2.680  12.759 1.00 39.06  ? 213 TYR A CE2 1 
ATOM   1659 C  CZ  . TYR A 1 218 ? 36.496 1.691  13.691 1.00 38.32  ? 213 TYR A CZ  1 
ATOM   1660 O  OH  . TYR A 1 218 ? 37.506 1.003  14.300 1.00 39.92  ? 213 TYR A OH  1 
ATOM   1661 N  N   . LYS A 1 219 ? 33.148 4.841  14.858 1.00 39.27  ? 214 LYS A N   1 
ATOM   1662 C  CA  . LYS A 1 219 ? 32.804 4.569  16.287 1.00 42.16  ? 214 LYS A CA  1 
ATOM   1663 C  C   . LYS A 1 219 ? 31.720 5.541  16.712 1.00 36.70  ? 214 LYS A C   1 
ATOM   1664 O  O   . LYS A 1 219 ? 30.738 5.128  17.343 1.00 36.06  ? 214 LYS A O   1 
ATOM   1665 C  CB  . LYS A 1 219 ? 34.074 4.621  17.136 1.00 47.00  ? 214 LYS A CB  1 
ATOM   1666 C  CG  . LYS A 1 219 ? 35.094 3.566  16.742 1.00 49.69  ? 214 LYS A CG  1 
ATOM   1667 C  CD  . LYS A 1 219 ? 36.511 3.878  17.172 1.00 55.80  ? 214 LYS A CD  1 
ATOM   1668 C  CE  . LYS A 1 219 ? 36.656 3.898  18.676 1.00 59.47  ? 214 LYS A CE  1 
ATOM   1669 N  NZ  . LYS A 1 219 ? 38.078 3.955  19.090 1.00 68.02  ? 214 LYS A NZ  1 
ATOM   1670 N  N   . ASP A 1 220 ? 31.803 6.793  16.265 1.00 37.53  ? 215 ASP A N   1 
ATOM   1671 C  CA  . ASP A 1 220 ? 30.760 7.797  16.579 1.00 34.14  ? 215 ASP A CA  1 
ATOM   1672 C  C   . ASP A 1 220 ? 29.458 7.426  15.875 1.00 31.47  ? 215 ASP A C   1 
ATOM   1673 O  O   . ASP A 1 220 ? 28.379 7.544  16.504 1.00 31.69  ? 215 ASP A O   1 
ATOM   1674 C  CB  . ASP A 1 220 ? 31.274 9.196  16.214 1.00 42.62  ? 215 ASP A CB  1 
ATOM   1675 C  CG  . ASP A 1 220 ? 32.604 9.468  16.908 1.00 46.20  ? 215 ASP A CG  1 
ATOM   1676 O  OD1 . ASP A 1 220 ? 32.632 9.373  18.166 1.00 44.55  ? 215 ASP A OD1 1 
ATOM   1677 O  OD2 . ASP A 1 220 ? 33.602 9.632  16.202 1.00 50.37  ? 215 ASP A OD2 1 
ATOM   1678 N  N   . SER A 1 221 ? 29.507 7.115  14.580 1.00 31.05  ? 216 SER A N   1 
ATOM   1679 C  CA  . SER A 1 221 ? 28.282 6.702  13.833 1.00 31.39  ? 216 SER A CA  1 
ATOM   1680 C  C   . SER A 1 221 ? 27.610 5.495  14.545 1.00 28.70  ? 216 SER A C   1 
ATOM   1681 O  O   . SER A 1 221 ? 26.397 5.562  14.789 1.00 32.38  ? 216 SER A O   1 
ATOM   1682 C  CB  . SER A 1 221 ? 28.645 6.406  12.388 1.00 32.40  ? 216 SER A CB  1 
ATOM   1683 O  OG  . SER A 1 221 ? 29.126 7.590  11.772 1.00 33.04  ? 216 SER A OG  1 
ATOM   1684 N  N   . THR A 1 222 ? 28.368 4.444  14.856 1.00 35.75  ? 217 THR A N   1 
ATOM   1685 C  CA  . THR A 1 222 ? 27.833 3.169  15.432 1.00 36.32  ? 217 THR A CA  1 
ATOM   1686 C  C   . THR A 1 222 ? 27.217 3.473  16.800 1.00 38.52  ? 217 THR A C   1 
ATOM   1687 O  O   . THR A 1 222 ? 26.076 3.000  17.083 1.00 33.41  ? 217 THR A O   1 
ATOM   1688 C  CB  . THR A 1 222 ? 28.901 2.082  15.438 1.00 33.44  ? 217 THR A CB  1 
ATOM   1689 O  OG1 . THR A 1 222 ? 30.110 2.485  16.067 1.00 44.28  ? 217 THR A OG1 1 
ATOM   1690 C  CG2 . THR A 1 222 ? 29.218 1.644  14.023 1.00 37.84  ? 217 THR A CG2 1 
ATOM   1691 N  N   . LEU A 1 223 ? 27.829 4.390  17.556 1.00 37.72  ? 218 LEU A N   1 
ATOM   1692 C  CA  . LEU A 1 223 ? 27.256 4.814  18.864 1.00 32.46  ? 218 LEU A CA  1 
ATOM   1693 C  C   . LEU A 1 223 ? 25.902 5.472  18.634 1.00 32.41  ? 218 LEU A C   1 
ATOM   1694 O  O   . LEU A 1 223 ? 24.943 5.094  19.317 1.00 33.62  ? 218 LEU A O   1 
ATOM   1695 C  CB  . LEU A 1 223 ? 28.249 5.749  19.567 1.00 40.49  ? 218 LEU A CB  1 
ATOM   1696 C  CG  . LEU A 1 223 ? 27.716 6.412  20.834 1.00 41.03  ? 218 LEU A CG  1 
ATOM   1697 C  CD1 . LEU A 1 223 ? 27.054 5.376  21.735 1.00 39.83  ? 218 LEU A CD1 1 
ATOM   1698 C  CD2 . LEU A 1 223 ? 28.856 7.115  21.580 1.00 47.12  ? 218 LEU A CD2 1 
ATOM   1699 N  N   . ILE A 1 224 ? 25.786 6.462  17.737 1.00 30.97  ? 219 ILE A N   1 
ATOM   1700 C  CA  . ILE A 1 224 ? 24.486 7.148  17.528 1.00 28.84  ? 219 ILE A CA  1 
ATOM   1701 C  C   . ILE A 1 224 ? 23.451 6.111  17.034 1.00 33.84  ? 219 ILE A C   1 
ATOM   1702 O  O   . ILE A 1 224 ? 22.253 6.222  17.386 1.00 33.43  ? 219 ILE A O   1 
ATOM   1703 C  CB  . ILE A 1 224 ? 24.575 8.321  16.538 1.00 28.98  ? 219 ILE A CB  1 
ATOM   1704 C  CG1 . ILE A 1 224 ? 25.673 9.312  16.922 1.00 37.28  ? 219 ILE A CG1 1 
ATOM   1705 C  CG2 . ILE A 1 224 ? 23.238 9.013  16.411 1.00 31.80  ? 219 ILE A CG2 1 
ATOM   1706 C  CD1 . ILE A 1 224 ? 25.516 9.876  18.313 1.00 37.26  ? 219 ILE A CD1 1 
ATOM   1707 N  N   . MET A 1 225 ? 23.853 5.197  16.163 1.00 33.18  ? 220 MET A N   1 
ATOM   1708 C  CA  . MET A 1 225 ? 22.875 4.205  15.632 1.00 34.20  ? 220 MET A CA  1 
ATOM   1709 C  C   . MET A 1 225 ? 22.260 3.416  16.805 1.00 34.43  ? 220 MET A C   1 
ATOM   1710 O  O   . MET A 1 225 ? 21.024 3.269  16.813 1.00 38.36  ? 220 MET A O   1 
ATOM   1711 C  CB  . MET A 1 225 ? 23.570 3.280  14.635 1.00 33.05  ? 220 MET A CB  1 
ATOM   1712 C  CG  . MET A 1 225 ? 23.797 3.980  13.267 1.00 34.88  ? 220 MET A CG  1 
ATOM   1713 S  SD  . MET A 1 225 ? 24.974 3.119  12.237 1.00 37.66  ? 220 MET A SD  1 
ATOM   1714 C  CE  . MET A 1 225 ? 23.995 1.663  11.821 1.00 39.06  ? 220 MET A CE  1 
ATOM   1715 N  N   . GLN A 1 226 ? 23.072 3.008  17.779 1.00 36.37  ? 221 GLN A N   1 
ATOM   1716 C  CA  . GLN A 1 226 ? 22.606 2.288  18.998 1.00 38.13  ? 221 GLN A CA  1 
ATOM   1717 C  C   . GLN A 1 226 ? 21.673 3.173  19.825 1.00 43.10  ? 221 GLN A C   1 
ATOM   1718 O  O   . GLN A 1 226 ? 20.681 2.640  20.349 1.00 40.17  ? 221 GLN A O   1 
ATOM   1719 C  CB  . GLN A 1 226 ? 23.792 1.772  19.804 1.00 43.68  ? 221 GLN A CB  1 
ATOM   1720 C  CG  . GLN A 1 226 ? 23.353 1.006  21.048 1.00 47.09  ? 221 GLN A CG  1 
ATOM   1721 C  CD  . GLN A 1 226 ? 22.610 -0.246 20.636 1.00 47.72  ? 221 GLN A CD  1 
ATOM   1722 O  OE1 . GLN A 1 226 ? 21.446 -0.444 20.970 1.00 53.56  ? 221 GLN A OE1 1 
ATOM   1723 N  NE2 . GLN A 1 226 ? 23.270 -1.070 19.841 1.00 49.04  ? 221 GLN A NE2 1 
ATOM   1724 N  N   . LEU A 1 227 ? 21.935 4.484  19.913 1.00 37.28  ? 222 LEU A N   1 
ATOM   1725 C  CA  . LEU A 1 227 ? 21.086 5.394  20.717 1.00 38.02  ? 222 LEU A CA  1 
ATOM   1726 C  C   . LEU A 1 227 ? 19.747 5.568  20.023 1.00 39.50  ? 222 LEU A C   1 
ATOM   1727 O  O   . LEU A 1 227 ? 18.725 5.598  20.722 1.00 36.19  ? 222 LEU A O   1 
ATOM   1728 C  CB  . LEU A 1 227 ? 21.812 6.722  21.003 1.00 35.08  ? 222 LEU A CB  1 
ATOM   1729 C  CG  . LEU A 1 227 ? 23.124 6.559  21.779 1.00 35.26  ? 222 LEU A CG  1 
ATOM   1730 C  CD1 . LEU A 1 227 ? 23.818 7.909  21.992 1.00 36.17  ? 222 LEU A CD1 1 
ATOM   1731 C  CD2 . LEU A 1 227 ? 22.894 5.883  23.125 1.00 38.45  ? 222 LEU A CD2 1 
ATOM   1732 N  N   . LEU A 1 228 ? 19.707 5.592  18.689 1.00 40.43  ? 223 LEU A N   1 
ATOM   1733 C  CA  . LEU A 1 228 ? 18.396 5.625  17.981 1.00 41.01  ? 223 LEU A CA  1 
ATOM   1734 C  C   . LEU A 1 228 ? 17.633 4.316  18.296 1.00 34.89  ? 223 LEU A C   1 
ATOM   1735 O  O   . LEU A 1 228 ? 16.427 4.395  18.531 1.00 37.69  ? 223 LEU A O   1 
ATOM   1736 C  CB  . LEU A 1 228 ? 18.626 5.790  16.470 1.00 43.79  ? 223 LEU A CB  1 
ATOM   1737 C  CG  . LEU A 1 228 ? 19.169 7.148  16.042 1.00 40.88  ? 223 LEU A CG  1 
ATOM   1738 C  CD1 . LEU A 1 228 ? 19.999 7.036  14.765 1.00 43.40  ? 223 LEU A CD1 1 
ATOM   1739 C  CD2 . LEU A 1 228 ? 18.046 8.150  15.885 1.00 42.99  ? 223 LEU A CD2 1 
ATOM   1740 N  N   . ARG A 1 229 ? 18.323 3.178  18.317 1.00 39.05  ? 224 ARG A N   1 
ATOM   1741 C  CA  . ARG A 1 229 ? 17.722 1.837  18.603 1.00 46.84  ? 224 ARG A CA  1 
ATOM   1742 C  C   . ARG A 1 229 ? 17.180 1.840  20.034 1.00 49.62  ? 224 ARG A C   1 
ATOM   1743 O  O   . ARG A 1 229 ? 16.029 1.417  20.212 1.00 56.44  ? 224 ARG A O   1 
ATOM   1744 C  CB  . ARG A 1 229 ? 18.738 0.703  18.426 1.00 48.36  ? 224 ARG A CB  1 
ATOM   1745 C  CG  . ARG A 1 229 ? 18.441 -0.239 17.266 1.00 64.62  ? 224 ARG A CG  1 
ATOM   1746 C  CD  . ARG A 1 229 ? 17.154 -1.057 17.402 1.00 68.80  ? 224 ARG A CD  1 
ATOM   1747 N  NE  . ARG A 1 229 ? 16.455 -1.148 16.114 1.00 76.39  ? 224 ARG A NE  1 
ATOM   1748 C  CZ  . ARG A 1 229 ? 15.158 -0.874 15.895 1.00 83.67  ? 224 ARG A CZ  1 
ATOM   1749 N  NH1 . ARG A 1 229 ? 14.355 -0.530 16.890 1.00 85.14  ? 224 ARG A NH1 1 
ATOM   1750 N  NH2 . ARG A 1 229 ? 14.657 -0.972 14.672 1.00 79.62  ? 224 ARG A NH2 1 
ATOM   1751 N  N   . ASP A 1 230 ? 17.958 2.368  20.996 1.00 51.46  ? 225 ASP A N   1 
ATOM   1752 C  CA  . ASP A 1 230 ? 17.565 2.434  22.433 1.00 46.60  ? 225 ASP A CA  1 
ATOM   1753 C  C   . ASP A 1 230 ? 16.309 3.291  22.547 1.00 48.30  ? 225 ASP A C   1 
ATOM   1754 O  O   . ASP A 1 230 ? 15.384 2.870  23.236 1.00 48.93  ? 225 ASP A O   1 
ATOM   1755 C  CB  . ASP A 1 230 ? 18.678 2.961  23.340 1.00 46.69  ? 225 ASP A CB  1 
ATOM   1756 C  CG  . ASP A 1 230 ? 19.936 2.122  23.308 1.00 45.02  ? 225 ASP A CG  1 
ATOM   1757 O  OD1 . ASP A 1 230 ? 19.844 0.948  22.919 1.00 55.01  ? 225 ASP A OD1 1 
ATOM   1758 O  OD2 . ASP A 1 230 ? 21.014 2.654  23.636 1.00 54.60  ? 225 ASP A OD2 1 
ATOM   1759 N  N   . ASN A 1 231 ? 16.246 4.451  21.892 1.00 46.27  ? 226 ASN A N   1 
ATOM   1760 C  CA  . ASN A 1 231 ? 15.028 5.304  21.971 1.00 46.12  ? 226 ASN A CA  1 
ATOM   1761 C  C   . ASN A 1 231 ? 13.820 4.564  21.366 1.00 48.19  ? 226 ASN A C   1 
ATOM   1762 O  O   . ASN A 1 231 ? 12.689 4.751  21.861 1.00 52.10  ? 226 ASN A O   1 
ATOM   1763 C  CB  . ASN A 1 231 ? 15.216 6.689  21.337 1.00 45.69  ? 226 ASN A CB  1 
ATOM   1764 C  CG  . ASN A 1 231 ? 16.032 7.626  22.215 1.00 45.47  ? 226 ASN A CG  1 
ATOM   1765 O  OD1 . ASN A 1 231 ? 16.203 7.389  23.410 1.00 41.33  ? 226 ASN A OD1 1 
ATOM   1766 N  ND2 . ASN A 1 231 ? 16.565 8.677  21.621 1.00 42.54  ? 226 ASN A ND2 1 
ATOM   1767 N  N   . LEU A 1 232 ? 14.019 3.835  20.272 1.00 48.11  ? 227 LEU A N   1 
ATOM   1768 C  CA  . LEU A 1 232 ? 12.914 3.073  19.624 1.00 51.33  ? 227 LEU A CA  1 
ATOM   1769 C  C   . LEU A 1 232 ? 12.381 2.017  20.597 1.00 46.07  ? 227 LEU A C   1 
ATOM   1770 O  O   . LEU A 1 232 ? 11.159 1.934  20.743 1.00 54.26  ? 227 LEU A O   1 
ATOM   1771 C  CB  . LEU A 1 232 ? 13.414 2.449  18.318 1.00 49.12  ? 227 LEU A CB  1 
ATOM   1772 C  CG  . LEU A 1 232 ? 13.654 3.471  17.205 1.00 48.44  ? 227 LEU A CG  1 
ATOM   1773 C  CD1 . LEU A 1 232 ? 14.530 2.872  16.108 1.00 52.72  ? 227 LEU A CD1 1 
ATOM   1774 C  CD2 . LEU A 1 232 ? 12.337 4.034  16.679 1.00 44.64  ? 227 LEU A CD2 1 
ATOM   1775 N  N   . THR A 1 233 ? 13.278 1.281  21.252 1.00 51.79  ? 228 THR A N   1 
ATOM   1776 C  CA  . THR A 1 233 ? 12.938 0.311  22.326 1.00 57.96  ? 228 THR A CA  1 
ATOM   1777 C  C   . THR A 1 233 ? 12.139 1.017  23.433 1.00 65.38  ? 228 THR A C   1 
ATOM   1778 O  O   . THR A 1 233 ? 11.119 0.451  23.871 1.00 65.52  ? 228 THR A O   1 
ATOM   1779 C  CB  . THR A 1 233 ? 14.203 -0.348 22.874 1.00 62.79  ? 228 THR A CB  1 
ATOM   1780 O  OG1 . THR A 1 233 ? 14.719 -1.086 21.770 1.00 62.61  ? 228 THR A OG1 1 
ATOM   1781 C  CG2 . THR A 1 233 ? 13.948 -1.227 24.081 1.00 61.63  ? 228 THR A CG2 1 
ATOM   1782 N  N   . LEU A 1 234 ? 12.580 2.204  23.860 1.00 59.00  ? 229 LEU A N   1 
ATOM   1783 C  CA  . LEU A 1 234 ? 11.933 2.987  24.939 1.00 58.41  ? 229 LEU A CA  1 
ATOM   1784 C  C   . LEU A 1 234 ? 10.548 3.409  24.451 1.00 60.03  ? 229 LEU A C   1 
ATOM   1785 O  O   . LEU A 1 234 ? 9.572  3.111  25.141 1.00 72.93  ? 229 LEU A O   1 
ATOM   1786 C  CB  . LEU A 1 234 ? 12.786 4.207  25.315 1.00 61.17  ? 229 LEU A CB  1 
ATOM   1787 C  CG  . LEU A 1 234 ? 12.031 5.292  26.092 1.00 66.81  ? 229 LEU A CG  1 
ATOM   1788 C  CD1 . LEU A 1 234 ? 11.678 4.802  27.496 1.00 64.58  ? 229 LEU A CD1 1 
ATOM   1789 C  CD2 . LEU A 1 234 ? 12.813 6.599  26.164 1.00 61.74  ? 229 LEU A CD2 1 
ATOM   1790 N  N   . TRP A 1 235 ? 10.459 4.051  23.288 1.00 54.73  ? 230 TRP A N   1 
ATOM   1791 C  CA  . TRP A 1 235 ? 9.162  4.479  22.702 1.00 57.32  ? 230 TRP A CA  1 
ATOM   1792 C  C   . TRP A 1 235 ? 8.392  3.245  22.202 1.00 61.04  ? 230 TRP A C   1 
ATOM   1793 O  O   . TRP A 1 235 ? 7.272  3.442  21.720 1.00 55.08  ? 230 TRP A O   1 
ATOM   1794 C  CB  . TRP A 1 235 ? 9.379  5.515  21.585 1.00 61.58  ? 230 TRP A CB  1 
ATOM   1795 C  CG  . TRP A 1 235 ? 10.279 6.647  21.974 1.00 65.47  ? 230 TRP A CG  1 
ATOM   1796 C  CD1 . TRP A 1 235 ? 10.520 7.114  23.237 1.00 66.06  ? 230 TRP A CD1 1 
ATOM   1797 C  CD2 . TRP A 1 235 ? 11.058 7.469  21.087 1.00 60.26  ? 230 TRP A CD2 1 
ATOM   1798 N  NE1 . TRP A 1 235 ? 11.398 8.160  23.194 1.00 58.97  ? 230 TRP A NE1 1 
ATOM   1799 C  CE2 . TRP A 1 235 ? 11.745 8.403  21.891 1.00 53.10  ? 230 TRP A CE2 1 
ATOM   1800 C  CE3 . TRP A 1 235 ? 11.245 7.503  19.699 1.00 58.67  ? 230 TRP A CE3 1 
ATOM   1801 C  CZ2 . TRP A 1 235 ? 12.597 9.364  21.345 1.00 57.07  ? 230 TRP A CZ2 1 
ATOM   1802 C  CZ3 . TRP A 1 235 ? 12.100 8.443  19.162 1.00 62.30  ? 230 TRP A CZ3 1 
ATOM   1803 C  CH2 . TRP A 1 235 ? 12.767 9.364  19.977 1.00 55.88  ? 230 TRP A CH2 1 
ATOM   1804 N  N   . THR A 1 236 ? 9.009  2.054  22.301 1.00 69.46  ? 231 THR A N   1 
ATOM   1805 C  CA  . THR A 1 236 ? 8.534  0.732  21.799 1.00 69.72  ? 231 THR A CA  1 
ATOM   1806 C  C   . THR A 1 236 ? 7.979  0.900  20.380 1.00 67.88  ? 231 THR A C   1 
ATOM   1807 O  O   . THR A 1 236 ? 8.751  0.675  19.441 1.00 55.17  ? 231 THR A O   1 
ATOM   1808 C  CB  . THR A 1 236 ? 7.585  0.086  22.812 1.00 67.55  ? 231 THR A CB  1 
ATOM   1809 O  OG1 . THR A 1 236 ? 8.423  -0.497 23.817 1.00 61.78  ? 231 THR A OG1 1 
ATOM   1810 C  CG2 . THR A 1 236 ? 6.697  -0.976 22.203 1.00 72.90  ? 231 THR A CG2 1 
ATOM   1811 N  N   . ILE B 2 2   ? 13.453 6.913  31.878 1.00 76.47  ? 255 ILE P N   1 
ATOM   1812 C  CA  . ILE B 2 2   ? 12.265 7.776  31.579 1.00 77.43  ? 255 ILE P CA  1 
ATOM   1813 C  C   . ILE B 2 2   ? 12.598 8.668  30.367 1.00 73.54  ? 255 ILE P C   1 
ATOM   1814 O  O   . ILE B 2 2   ? 11.936 8.489  29.323 1.00 73.28  ? 255 ILE P O   1 
ATOM   1815 C  CB  . ILE B 2 2   ? 11.823 8.586  32.821 1.00 71.82  ? 255 ILE P CB  1 
ATOM   1816 N  N   . ARG B 2 3   ? 13.593 9.561  30.471 1.00 66.40  ? 256 ARG P N   1 
ATOM   1817 C  CA  . ARG B 2 3   ? 13.862 10.624 29.452 1.00 65.24  ? 256 ARG P CA  1 
ATOM   1818 C  C   . ARG B 2 3   ? 14.525 10.022 28.201 1.00 59.05  ? 256 ARG P C   1 
ATOM   1819 O  O   . ARG B 2 3   ? 15.456 9.207  28.352 1.00 51.42  ? 256 ARG P O   1 
ATOM   1820 C  CB  . ARG B 2 3   ? 14.725 11.755 30.029 1.00 64.76  ? 256 ARG P CB  1 
ATOM   1821 C  CG  . ARG B 2 3   ? 13.942 13.036 30.277 1.00 76.19  ? 256 ARG P CG  1 
ATOM   1822 C  CD  . ARG B 2 3   ? 14.756 14.211 30.789 1.00 74.94  ? 256 ARG P CD  1 
ATOM   1823 N  NE  . ARG B 2 3   ? 13.841 15.192 31.363 1.00 73.95  ? 256 ARG P NE  1 
ATOM   1824 C  CZ  . ARG B 2 3   ? 13.415 15.202 32.633 1.00 74.99  ? 256 ARG P CZ  1 
ATOM   1825 N  NH1 . ARG B 2 3   ? 13.864 14.317 33.507 1.00 70.76  ? 256 ARG P NH1 1 
ATOM   1826 N  NH2 . ARG B 2 3   ? 12.563 16.129 33.044 1.00 70.84  ? 256 ARG P NH2 1 
ATOM   1827 N  N   . SER B 2 4   ? 14.088 10.426 27.005 1.00 52.85  ? 257 SER P N   1 
ATOM   1828 C  CA  . SER B 2 4   ? 14.761 10.052 25.727 1.00 50.44  ? 257 SER P CA  1 
ATOM   1829 C  C   . SER B 2 4   ? 16.250 10.420 25.810 1.00 47.86  ? 257 SER P C   1 
ATOM   1830 O  O   . SER B 2 4   ? 16.560 11.440 26.438 1.00 44.93  ? 257 SER P O   1 
ATOM   1831 C  CB  . SER B 2 4   ? 14.121 10.735 24.558 1.00 51.01  ? 257 SER P CB  1 
ATOM   1832 O  OG  . SER B 2 4   ? 12.731 10.491 24.519 1.00 49.15  ? 257 SER P OG  1 
ATOM   1833 N  N   . THR B 2 5   ? 17.140 9.625  25.215 1.00 46.25  ? 258 THR P N   1 
ATOM   1834 C  CA  . THR B 2 5   ? 18.597 9.910  25.165 1.00 46.49  ? 258 THR P CA  1 
ATOM   1835 C  C   . THR B 2 5   ? 18.899 10.781 23.939 1.00 45.52  ? 258 THR P C   1 
ATOM   1836 O  O   . THR B 2 5   ? 18.455 10.429 22.812 1.00 43.15  ? 258 THR P O   1 
ATOM   1837 C  CB  . THR B 2 5   ? 19.419 8.626  25.083 1.00 44.52  ? 258 THR P CB  1 
ATOM   1838 O  OG1 . THR B 2 5   ? 19.044 7.834  26.206 1.00 48.59  ? 258 THR P OG1 1 
ATOM   1839 C  CG2 . THR B 2 5   ? 20.915 8.868  25.110 1.00 47.78  ? 258 THR P CG2 1 
HETATM 1840 N  N   . SEP B 2 6   ? 19.667 11.848 24.121 1.00 37.62  ? 259 SEP P N   1 
HETATM 1841 C  CA  . SEP B 2 6   ? 20.130 12.704 23.003 1.00 36.25  ? 259 SEP P CA  1 
HETATM 1842 C  CB  . SEP B 2 6   ? 19.847 14.171 23.278 1.00 38.64  ? 259 SEP P CB  1 
HETATM 1843 O  OG  . SEP B 2 6   ? 20.691 14.627 24.349 1.00 35.14  ? 259 SEP P OG  1 
HETATM 1844 C  C   . SEP B 2 6   ? 21.584 12.424 22.679 1.00 34.04  ? 259 SEP P C   1 
HETATM 1845 O  O   . SEP B 2 6   ? 22.198 11.548 23.317 1.00 30.91  ? 259 SEP P O   1 
HETATM 1846 P  P   . SEP B 2 6   ? 20.429 16.115 24.908 1.00 35.02  ? 259 SEP P P   1 
HETATM 1847 O  O1P . SEP B 2 6   ? 20.804 17.096 23.806 1.00 34.24  ? 259 SEP P O1P 1 
HETATM 1848 O  O2P . SEP B 2 6   ? 18.988 16.217 25.337 1.00 35.14  ? 259 SEP P O2P 1 
HETATM 1849 O  O3P . SEP B 2 6   ? 21.413 16.186 26.081 1.00 34.75  ? 259 SEP P O3P 1 
ATOM   1850 N  N   . THR B 2 7   ? 22.120 13.122 21.666 1.00 30.48  ? 260 THR P N   1 
ATOM   1851 C  CA  . THR B 2 7   ? 23.526 12.919 21.271 1.00 30.81  ? 260 THR P CA  1 
ATOM   1852 C  C   . THR B 2 7   ? 24.385 13.210 22.489 1.00 34.64  ? 260 THR P C   1 
ATOM   1853 O  O   . THR B 2 7   ? 24.225 14.259 23.136 1.00 32.25  ? 260 THR P O   1 
ATOM   1854 C  CB  . THR B 2 7   ? 23.931 13.800 20.085 1.00 31.65  ? 260 THR P CB  1 
ATOM   1855 O  OG1 . THR B 2 7   ? 23.076 13.491 18.969 1.00 33.48  ? 260 THR P OG1 1 
ATOM   1856 C  CG2 . THR B 2 7   ? 25.375 13.598 19.717 1.00 32.60  ? 260 THR P CG2 1 
ATOM   1857 N  N   . PRO B 2 8   ? 25.329 12.312 22.812 1.00 31.68  ? 261 PRO P N   1 
ATOM   1858 C  CA  . PRO B 2 8   ? 26.127 12.485 24.013 1.00 37.62  ? 261 PRO P CA  1 
ATOM   1859 C  C   . PRO B 2 8   ? 27.268 13.453 23.726 1.00 36.87  ? 261 PRO P C   1 
ATOM   1860 O  O   . PRO B 2 8   ? 27.691 13.642 22.578 1.00 32.10  ? 261 PRO P O   1 
ATOM   1861 C  CB  . PRO B 2 8   ? 26.710 11.089 24.324 1.00 35.08  ? 261 PRO P CB  1 
ATOM   1862 C  CG  . PRO B 2 8   ? 26.758 10.426 22.948 1.00 33.70  ? 261 PRO P CG  1 
ATOM   1863 C  CD  . PRO B 2 8   ? 25.573 10.998 22.193 1.00 34.43  ? 261 PRO P CD  1 
ATOM   1864 N  N   . ASN B 2 9   ? 27.836 13.899 24.829 1.00 39.02  ? 262 ASN P N   1 
ATOM   1865 C  CA  . ASN B 2 9   ? 28.973 14.832 24.847 1.00 44.09  ? 262 ASN P CA  1 
ATOM   1866 C  C   . ASN B 2 9   ? 30.269 14.074 24.641 1.00 49.55  ? 262 ASN P C   1 
ATOM   1867 O  O   . ASN B 2 9   ? 31.170 14.203 25.512 1.00 53.12  ? 262 ASN P O   1 
ATOM   1868 C  CB  . ASN B 2 9   ? 29.001 15.629 26.161 1.00 45.96  ? 262 ASN P CB  1 
ATOM   1869 C  CG  . ASN B 2 9   ? 29.596 16.988 25.899 1.00 45.70  ? 262 ASN P CG  1 
ATOM   1870 O  OD1 . ASN B 2 9   ? 29.816 17.301 24.729 1.00 33.89  ? 262 ASN P OD1 1 
ATOM   1871 N  ND2 . ASN B 2 9   ? 29.818 17.784 26.941 1.00 48.39  ? 262 ASN P ND2 1 
ATOM   1872 N  N   . VAL B 2 10  ? 30.372 13.306 23.565 1.00 47.20  ? 263 VAL P N   1 
ATOM   1873 C  CA  . VAL B 2 10  ? 31.536 12.404 23.363 1.00 53.78  ? 263 VAL P CA  1 
ATOM   1874 C  C   . VAL B 2 10  ? 32.527 13.149 22.483 1.00 58.06  ? 263 VAL P C   1 
ATOM   1875 O  O   . VAL B 2 10  ? 32.131 13.561 21.367 1.00 61.27  ? 263 VAL P O   1 
ATOM   1876 C  CB  . VAL B 2 10  ? 31.139 11.050 22.743 1.00 57.33  ? 263 VAL P CB  1 
ATOM   1877 C  CG1 . VAL B 2 10  ? 32.275 10.429 21.931 1.00 54.54  ? 263 VAL P CG1 1 
ATOM   1878 C  CG2 . VAL B 2 10  ? 30.655 10.086 23.810 1.00 59.68  ? 263 VAL P CG2 1 
ATOM   1879 N  N   . HIS B 2 11  ? 33.752 13.298 22.988 1.00 68.63  ? 264 HIS P N   1 
ATOM   1880 C  CA  . HIS B 2 11  ? 34.902 13.933 22.287 1.00 70.75  ? 264 HIS P CA  1 
ATOM   1881 C  C   . HIS B 2 11  ? 35.121 13.213 20.946 1.00 76.94  ? 264 HIS P C   1 
ATOM   1882 O  O   . HIS B 2 11  ? 35.296 11.976 20.948 1.00 65.96  ? 264 HIS P O   1 
ATOM   1883 C  CB  . HIS B 2 11  ? 36.161 13.911 23.178 1.00 70.00  ? 264 HIS P CB  1 
ATOM   1884 C  CG  . HIS B 2 11  ? 37.330 14.680 22.645 1.00 68.16  ? 264 HIS P CG  1 
ATOM   1885 N  ND1 . HIS B 2 11  ? 37.685 15.932 23.151 1.00 63.75  ? 264 HIS P ND1 1 
ATOM   1886 C  CD2 . HIS B 2 11  ? 38.248 14.374 21.691 1.00 63.34  ? 264 HIS P CD2 1 
ATOM   1887 C  CE1 . HIS B 2 11  ? 38.762 16.369 22.516 1.00 68.53  ? 264 HIS P CE1 1 
ATOM   1888 N  NE2 . HIS B 2 11  ? 39.128 15.428 21.607 1.00 67.95  ? 264 HIS P NE2 1 
ATOM   1889 N  N   . MET B 2 12  ? 35.134 13.970 19.849 1.00 76.50  ? 265 MET P N   1 
ATOM   1890 C  CA  . MET B 2 12  ? 35.411 13.457 18.481 1.00 82.14  ? 265 MET P CA  1 
ATOM   1891 C  C   . MET B 2 12  ? 36.736 14.034 17.956 1.00 75.95  ? 265 MET P C   1 
ATOM   1892 O  O   . MET B 2 12  ? 36.843 15.204 17.599 1.00 67.90  ? 265 MET P O   1 
ATOM   1893 C  CB  . MET B 2 12  ? 34.249 13.819 17.553 1.00 79.28  ? 265 MET P CB  1 
ATOM   1894 C  CG  . MET B 2 12  ? 32.942 13.140 17.965 1.00 78.77  ? 265 MET P CG  1 
ATOM   1895 S  SD  . MET B 2 12  ? 31.618 13.244 16.698 1.00 83.38  ? 265 MET P SD  1 
ATOM   1896 C  CE  . MET B 2 12  ? 32.420 12.702 15.182 1.00 59.64  ? 265 MET P CE  1 
HETATM 1897 CL CL  . CL  C 3 .   ? 17.801 32.033 45.292 1.00 39.06  ? 301 CL  A CL  1 
HETATM 1898 MG MG  . MG  D 4 .   ? 10.777 31.768 34.613 1.00 62.83  ? 302 MG  A MG  1 
HETATM 1899 MG MG  . MG  E 4 .   ? 46.579 35.810 16.689 1.00 66.99  ? 303 MG  A MG  1 
HETATM 1900 MG MG  . MG  F 4 .   ? 3.706  4.276  17.354 1.00 77.58  ? 304 MG  A MG  1 
HETATM 1901 C  C4  . WQT G 5 .   ? 31.471 17.297 15.565 1.00 38.69  ? 305 WQT A C4  1 
HETATM 1902 C  C14 . WQT G 5 .   ? 31.377 17.458 17.955 1.00 45.99  ? 305 WQT A C14 1 
HETATM 1903 C  C5  . WQT G 5 .   ? 32.430 16.706 14.476 1.00 39.24  ? 305 WQT A C5  1 
HETATM 1904 C  C6  . WQT G 5 .   ? 30.301 16.370 15.866 1.00 35.29  ? 305 WQT A C6  1 
HETATM 1905 C  C11 . WQT G 5 .   ? 28.268 12.372 17.041 1.00 44.15  ? 305 WQT A C11 1 
HETATM 1906 C  C7  . WQT G 5 .   ? 28.091 14.752 17.420 1.00 40.00  ? 305 WQT A C7  1 
HETATM 1907 C  C8  . WQT G 5 .   ? 28.480 14.607 18.738 1.00 39.48  ? 305 WQT A C8  1 
HETATM 1908 C  C9  . WQT G 5 .   ? 28.741 13.341 19.215 1.00 42.37  ? 305 WQT A C9  1 
HETATM 1909 C  C10 . WQT G 5 .   ? 28.628 12.241 18.381 1.00 54.85  ? 305 WQT A C10 1 
HETATM 1910 C  C12 . WQT G 5 .   ? 27.982 13.649 16.574 1.00 43.59  ? 305 WQT A C12 1 
HETATM 1911 C  C13 . WQT G 5 .   ? 29.886 17.676 17.892 1.00 44.26  ? 305 WQT A C13 1 
HETATM 1912 N  N1  . WQT G 5 .   ? 32.152 17.955 13.760 1.00 35.53  ? 305 WQT A N1  1 
HETATM 1913 N  N2  . WQT G 5 .   ? 29.297 17.062 16.682 1.00 39.08  ? 305 WQT A N2  1 
HETATM 1914 C  C3  . WQT G 5 .   ? 31.198 18.554 14.697 1.00 34.73  ? 305 WQT A C3  1 
HETATM 1915 C  C1  . WQT G 5 .   ? 32.597 18.431 12.536 1.00 36.70  ? 305 WQT A C1  1 
HETATM 1916 C  C2  . WQT G 5 .   ? 33.551 17.567 11.737 1.00 38.84  ? 305 WQT A C2  1 
HETATM 1917 I  I1  . WQT G 5 .   ? 29.055 10.349 19.213 1.00 134.27 ? 305 WQT A I1  1 
HETATM 1918 O  O1  . WQT G 5 .   ? 32.222 19.526 12.112 1.00 34.74  ? 305 WQT A O1  1 
HETATM 1919 O  O2  . WQT G 5 .   ? 27.350 16.284 15.443 1.00 42.26  ? 305 WQT A O2  1 
HETATM 1920 O  O3  . WQT G 5 .   ? 27.070 17.126 17.741 1.00 35.35  ? 305 WQT A O3  1 
HETATM 1921 O  O4  . WQT G 5 .   ? 32.129 17.714 16.759 1.00 45.37  ? 305 WQT A O4  1 
HETATM 1922 S  S1  . WQT G 5 .   ? 27.817 16.381 16.807 1.00 37.62  ? 305 WQT A S1  1 
HETATM 1923 O  O   . HOH H 6 .   ? 46.626 20.207 26.130 1.00 55.98  ? 401 HOH A O   1 
HETATM 1924 O  O   . HOH H 6 .   ? 15.388 28.835 14.239 1.00 59.98  ? 402 HOH A O   1 
HETATM 1925 O  O   . HOH H 6 .   ? 41.875 42.066 20.498 1.00 24.92  ? 403 HOH A O   1 
HETATM 1926 O  O   . HOH H 6 .   ? 24.074 28.212 7.055  1.00 49.00  ? 404 HOH A O   1 
HETATM 1927 O  O   . HOH H 6 .   ? 16.896 5.904  25.211 1.00 53.17  ? 405 HOH A O   1 
HETATM 1928 O  O   . HOH H 6 .   ? 11.164 20.562 31.077 1.00 54.15  ? 406 HOH A O   1 
HETATM 1929 O  O   . HOH H 6 .   ? 43.427 25.077 16.027 1.00 38.46  ? 407 HOH A O   1 
HETATM 1930 O  O   . HOH H 6 .   ? 24.112 32.361 32.712 1.00 34.36  ? 408 HOH A O   1 
HETATM 1931 O  O   . HOH H 6 .   ? 42.304 38.984 27.071 1.00 52.39  ? 409 HOH A O   1 
HETATM 1932 O  O   . HOH H 6 .   ? 6.956  -1.964 25.196 1.00 67.73  ? 410 HOH A O   1 
HETATM 1933 O  O   . HOH H 6 .   ? 23.222 25.623 3.526  1.00 57.65  ? 411 HOH A O   1 
HETATM 1934 O  O   . HOH H 6 .   ? 30.359 37.862 20.720 1.00 52.00  ? 412 HOH A O   1 
HETATM 1935 O  O   . HOH H 6 .   ? 31.613 7.863  3.651  1.00 43.80  ? 413 HOH A O   1 
HETATM 1936 O  O   . HOH H 6 .   ? 41.921 22.355 14.072 1.00 49.05  ? 414 HOH A O   1 
HETATM 1937 O  O   . HOH H 6 .   ? 34.410 33.136 14.332 1.00 46.74  ? 415 HOH A O   1 
HETATM 1938 O  O   . HOH H 6 .   ? 31.387 29.913 10.731 1.00 40.82  ? 416 HOH A O   1 
HETATM 1939 O  O   . HOH H 6 .   ? 40.596 26.742 12.511 1.00 50.26  ? 417 HOH A O   1 
HETATM 1940 O  O   . HOH H 6 .   ? 26.841 23.660 34.906 1.00 37.42  ? 418 HOH A O   1 
HETATM 1941 O  O   . HOH H 6 .   ? 15.407 33.646 42.150 1.00 41.44  ? 419 HOH A O   1 
HETATM 1942 O  O   . HOH H 6 .   ? 14.498 17.117 4.721  1.00 63.38  ? 420 HOH A O   1 
HETATM 1943 O  O   . HOH H 6 .   ? 40.175 18.137 37.251 1.00 48.23  ? 421 HOH A O   1 
HETATM 1944 O  O   . HOH H 6 .   ? 12.186 17.516 37.182 1.00 48.74  ? 422 HOH A O   1 
HETATM 1945 O  O   . HOH H 6 .   ? 49.958 28.874 21.230 1.00 54.15  ? 423 HOH A O   1 
HETATM 1946 O  O   . HOH H 6 .   ? 30.821 31.527 28.015 1.00 36.28  ? 424 HOH A O   1 
HETATM 1947 O  O   . HOH H 6 .   ? 34.093 19.629 36.128 1.00 47.41  ? 425 HOH A O   1 
HETATM 1948 O  O   . HOH H 6 .   ? 6.876  21.716 25.690 1.00 58.55  ? 426 HOH A O   1 
HETATM 1949 O  O   . HOH H 6 .   ? 15.705 19.881 31.277 1.00 51.57  ? 427 HOH A O   1 
HETATM 1950 O  O   . HOH H 6 .   ? 33.161 27.802 11.490 1.00 38.83  ? 428 HOH A O   1 
HETATM 1951 O  O   . HOH H 6 .   ? 10.194 27.129 34.198 1.00 45.15  ? 429 HOH A O   1 
HETATM 1952 O  O   . HOH H 6 .   ? 14.884 17.755 25.241 1.00 37.07  ? 430 HOH A O   1 
HETATM 1953 O  O   . HOH H 6 .   ? 19.224 34.780 31.664 1.00 51.29  ? 431 HOH A O   1 
HETATM 1954 O  O   . HOH H 6 .   ? 17.748 -0.821 6.669  1.00 42.07  ? 432 HOH A O   1 
HETATM 1955 O  O   . HOH H 6 .   ? 9.296  23.819 37.995 1.00 46.03  ? 433 HOH A O   1 
HETATM 1956 O  O   . HOH H 6 .   ? 31.441 3.130  18.931 1.00 47.41  ? 434 HOH A O   1 
HETATM 1957 O  O   . HOH H 6 .   ? 36.686 38.267 23.146 1.00 43.06  ? 435 HOH A O   1 
HETATM 1958 O  O   . HOH H 6 .   ? 16.944 22.989 29.725 1.00 35.85  ? 436 HOH A O   1 
HETATM 1959 O  O   . HOH H 6 .   ? 46.489 26.471 19.309 1.00 33.46  ? 437 HOH A O   1 
HETATM 1960 O  O   . HOH H 6 .   ? 4.379  34.054 20.980 1.00 52.25  ? 438 HOH A O   1 
HETATM 1961 O  O   . HOH H 6 .   ? 31.290 27.388 38.408 0.50 81.73  ? 439 HOH A O   1 
HETATM 1962 O  O   . HOH H 6 .   ? 18.715 15.972 37.469 1.00 37.64  ? 440 HOH A O   1 
HETATM 1963 O  O   . HOH H 6 .   ? 37.110 -0.304 16.589 1.00 38.56  ? 441 HOH A O   1 
HETATM 1964 O  O   . HOH H 6 .   ? 31.408 29.139 7.981  1.00 65.90  ? 442 HOH A O   1 
HETATM 1965 O  O   . HOH H 6 .   ? 18.543 14.830 29.152 1.00 54.57  ? 443 HOH A O   1 
HETATM 1966 O  O   . HOH H 6 .   ? 14.243 16.223 42.718 1.00 51.19  ? 444 HOH A O   1 
HETATM 1967 O  O   . HOH H 6 .   ? 38.374 37.271 21.367 1.00 31.78  ? 445 HOH A O   1 
HETATM 1968 O  O   . HOH H 6 .   ? 34.969 34.503 26.766 1.00 31.96  ? 446 HOH A O   1 
HETATM 1969 O  O   . HOH H 6 .   ? 13.369 29.436 28.338 1.00 46.32  ? 447 HOH A O   1 
HETATM 1970 O  O   . HOH H 6 .   ? 49.861 31.661 20.613 1.00 40.17  ? 448 HOH A O   1 
HETATM 1971 O  O   . HOH H 6 .   ? 37.971 32.132 8.695  1.00 51.42  ? 449 HOH A O   1 
HETATM 1972 O  O   . HOH H 6 .   ? 12.029 15.312 43.893 1.00 50.71  ? 450 HOH A O   1 
HETATM 1973 O  O   . HOH H 6 .   ? 41.074 39.737 30.651 1.00 40.38  ? 451 HOH A O   1 
HETATM 1974 O  O   . HOH H 6 .   ? 17.157 10.605 8.730  1.00 47.62  ? 452 HOH A O   1 
HETATM 1975 O  O   . HOH H 6 .   ? 22.265 16.965 32.250 1.00 52.41  ? 453 HOH A O   1 
HETATM 1976 O  O   . HOH H 6 .   ? 8.569  27.492 46.702 1.00 41.98  ? 454 HOH A O   1 
HETATM 1977 O  O   . HOH H 6 .   ? 16.263 32.169 14.485 1.00 60.26  ? 455 HOH A O   1 
HETATM 1978 O  O   . HOH H 6 .   ? 27.087 22.015 22.770 1.00 40.50  ? 456 HOH A O   1 
HETATM 1979 O  O   . HOH H 6 .   ? 27.209 35.430 22.792 1.00 43.82  ? 457 HOH A O   1 
HETATM 1980 O  O   . HOH H 6 .   ? 10.076 31.532 54.451 1.00 43.66  ? 458 HOH A O   1 
HETATM 1981 O  O   . HOH H 6 .   ? 24.919 26.850 9.605  1.00 46.28  ? 459 HOH A O   1 
HETATM 1982 O  O   . HOH H 6 .   ? 31.256 7.491  9.996  1.00 33.77  ? 460 HOH A O   1 
HETATM 1983 O  O   . HOH H 6 .   ? 32.942 11.495 8.998  1.00 48.93  ? 461 HOH A O   1 
HETATM 1984 O  O   . HOH H 6 .   ? 24.204 19.765 38.292 1.00 48.68  ? 462 HOH A O   1 
HETATM 1985 O  O   . HOH H 6 .   ? 20.574 7.892  8.170  1.00 42.96  ? 463 HOH A O   1 
HETATM 1986 O  O   . HOH H 6 .   ? 38.698 18.591 19.591 1.00 36.59  ? 464 HOH A O   1 
HETATM 1987 O  O   . HOH H 6 .   ? 18.276 9.193  7.101  1.00 40.95  ? 465 HOH A O   1 
HETATM 1988 O  O   . HOH H 6 .   ? 49.618 38.916 17.566 1.00 37.46  ? 466 HOH A O   1 
HETATM 1989 O  O   . HOH H 6 .   ? 25.154 17.297 20.727 1.00 37.93  ? 467 HOH A O   1 
HETATM 1990 O  O   . HOH H 6 .   ? 37.705 20.901 9.774  1.00 43.56  ? 468 HOH A O   1 
HETATM 1991 O  O   . HOH H 6 .   ? 31.850 30.145 30.423 1.00 37.59  ? 469 HOH A O   1 
HETATM 1992 O  O   . HOH H 6 .   ? 6.051  27.001 42.986 1.00 52.78  ? 470 HOH A O   1 
HETATM 1993 O  O   . HOH H 6 .   ? 46.931 22.684 25.045 1.00 43.91  ? 471 HOH A O   1 
HETATM 1994 O  O   . HOH H 6 .   ? 23.613 35.803 28.178 1.00 43.43  ? 472 HOH A O   1 
HETATM 1995 O  O   . HOH H 6 .   ? 42.935 22.198 17.185 1.00 52.48  ? 473 HOH A O   1 
HETATM 1996 O  O   . HOH H 6 .   ? 41.882 18.553 25.594 1.00 35.38  ? 474 HOH A O   1 
HETATM 1997 O  O   . HOH H 6 .   ? 29.474 27.365 7.688  1.00 45.72  ? 475 HOH A O   1 
HETATM 1998 O  O   . HOH H 6 .   ? 19.181 12.307 8.153  1.00 42.71  ? 476 HOH A O   1 
HETATM 1999 O  O   . HOH H 6 .   ? 27.724 28.046 9.074  1.00 47.58  ? 477 HOH A O   1 
HETATM 2000 O  O   . HOH H 6 .   ? 19.796 14.613 9.705  1.00 46.35  ? 478 HOH A O   1 
HETATM 2001 O  O   . HOH H 6 .   ? 24.577 20.046 21.372 1.00 50.13  ? 479 HOH A O   1 
HETATM 2002 O  O   . HOH H 6 .   ? 21.062 9.908  1.889  1.00 55.05  ? 480 HOH A O   1 
HETATM 2003 O  O   . HOH H 6 .   ? 46.200 23.880 20.375 1.00 32.86  ? 481 HOH A O   1 
HETATM 2004 O  O   . HOH H 6 .   ? 19.971 4.990  3.082  1.00 49.92  ? 482 HOH A O   1 
HETATM 2005 O  O   . HOH H 6 .   ? 37.352 23.640 39.515 1.00 36.61  ? 483 HOH A O   1 
HETATM 2006 O  O   . HOH H 6 .   ? 30.675 10.968 6.732  1.00 43.46  ? 484 HOH A O   1 
HETATM 2007 O  O   . HOH H 6 .   ? 13.274 26.233 8.693  1.00 63.27  ? 485 HOH A O   1 
HETATM 2008 O  O   . HOH H 6 .   ? 30.081 8.409  7.666  1.00 30.53  ? 486 HOH A O   1 
HETATM 2009 O  O   . HOH H 6 .   ? 26.771 21.162 19.965 1.00 38.41  ? 487 HOH A O   1 
HETATM 2010 O  O   . HOH H 6 .   ? 10.265 26.398 49.509 1.00 41.23  ? 488 HOH A O   1 
HETATM 2011 O  O   . HOH H 6 .   ? 37.982 5.763  13.952 1.00 49.66  ? 489 HOH A O   1 
HETATM 2012 O  O   . HOH H 6 .   ? 46.789 33.045 17.022 1.00 31.69  ? 490 HOH A O   1 
HETATM 2013 O  O   . HOH H 6 .   ? 52.757 34.944 19.116 1.00 51.10  ? 491 HOH A O   1 
HETATM 2014 O  O   . HOH H 6 .   ? 25.522 20.614 17.357 1.00 43.41  ? 492 HOH A O   1 
HETATM 2015 O  O   . HOH H 6 .   ? 14.438 11.676 7.585  1.00 49.34  ? 493 HOH A O   1 
HETATM 2016 O  O   . HOH H 6 .   ? 11.005 14.955 11.281 1.00 49.89  ? 494 HOH A O   1 
HETATM 2017 O  O   . HOH H 6 .   ? 49.536 32.804 17.671 1.00 46.97  ? 495 HOH A O   1 
HETATM 2018 O  O   . HOH H 6 .   ? 32.771 35.072 12.585 1.00 70.14  ? 496 HOH A O   1 
HETATM 2019 O  O   . HOH H 6 .   ? 39.801 19.545 12.523 1.00 46.19  ? 497 HOH A O   1 
HETATM 2020 O  O   . HOH H 6 .   ? 36.861 21.454 37.854 1.00 40.35  ? 498 HOH A O   1 
HETATM 2021 O  O   . HOH H 6 .   ? 6.784  37.920 25.969 1.00 56.32  ? 499 HOH A O   1 
HETATM 2022 O  O   . HOH H 6 .   ? 44.414 29.652 16.146 1.00 34.91  ? 500 HOH A O   1 
HETATM 2023 O  O   . HOH H 6 .   ? 16.055 5.846  1.310  1.00 66.91  ? 501 HOH A O   1 
HETATM 2024 O  O   . HOH H 6 .   ? 28.534 29.518 33.149 1.00 47.77  ? 502 HOH A O   1 
HETATM 2025 O  O   . HOH H 6 .   ? 35.884 6.195  14.778 1.00 35.39  ? 503 HOH A O   1 
HETATM 2026 O  O   . HOH H 6 .   ? 35.648 28.389 36.324 1.00 51.86  ? 504 HOH A O   1 
HETATM 2027 O  O   . HOH H 6 .   ? 35.957 15.998 27.895 1.00 49.68  ? 505 HOH A O   1 
HETATM 2028 O  O   . HOH H 6 .   ? 41.197 18.783 20.782 1.00 47.80  ? 506 HOH A O   1 
HETATM 2029 O  O   . HOH H 6 .   ? 32.673 39.649 24.008 1.00 64.35  ? 507 HOH A O   1 
HETATM 2030 O  O   . HOH H 6 .   ? 35.866 26.037 34.829 1.00 32.41  ? 508 HOH A O   1 
HETATM 2031 O  O   . HOH H 6 .   ? 6.317  29.398 45.563 1.00 56.43  ? 509 HOH A O   1 
HETATM 2032 O  O   . HOH H 6 .   ? 23.659 19.130 27.879 1.00 45.12  ? 510 HOH A O   1 
HETATM 2033 O  O   . HOH H 6 .   ? 48.827 18.351 27.792 1.00 68.26  ? 511 HOH A O   1 
HETATM 2034 O  O   . HOH H 6 .   ? 42.816 35.894 15.135 1.00 46.26  ? 512 HOH A O   1 
HETATM 2035 O  O   . HOH H 6 .   ? 22.711 -0.166 16.824 1.00 53.28  ? 513 HOH A O   1 
HETATM 2036 O  O   . HOH H 6 .   ? 20.304 33.543 45.551 1.00 46.47  ? 514 HOH A O   1 
HETATM 2037 O  O   . HOH H 6 .   ? 36.521 43.793 27.341 1.00 51.61  ? 515 HOH A O   1 
HETATM 2038 O  O   . HOH H 6 .   ? 19.046 15.003 34.701 1.00 50.65  ? 516 HOH A O   1 
HETATM 2039 O  O   . HOH H 6 .   ? 19.564 7.665  2.509  1.00 62.94  ? 517 HOH A O   1 
HETATM 2040 O  O   . HOH H 6 .   ? 20.442 1.506  -0.405 1.00 45.33  ? 518 HOH A O   1 
HETATM 2041 O  O   . HOH H 6 .   ? 27.951 36.567 20.518 1.00 43.44  ? 519 HOH A O   1 
HETATM 2042 O  O   . HOH H 6 .   ? 33.289 26.640 9.067  1.00 49.88  ? 520 HOH A O   1 
HETATM 2043 O  O   . HOH H 6 .   ? 5.576  32.049 47.173 1.00 42.75  ? 521 HOH A O   1 
HETATM 2044 O  O   . HOH H 6 .   ? 38.555 39.591 19.810 1.00 46.61  ? 522 HOH A O   1 
HETATM 2045 O  O   . HOH H 6 .   ? 12.857 15.409 9.108  1.00 66.21  ? 523 HOH A O   1 
HETATM 2046 O  O   . HOH H 6 .   ? 45.950 31.594 15.200 1.00 47.97  ? 524 HOH A O   1 
HETATM 2047 O  O   . HOH H 6 .   ? 16.303 14.952 38.322 1.00 51.89  ? 525 HOH A O   1 
HETATM 2048 O  O   . HOH H 6 .   ? 32.319 25.064 37.605 1.00 60.06  ? 526 HOH A O   1 
HETATM 2049 O  O   . HOH H 6 .   ? 16.894 34.361 43.845 1.00 48.27  ? 527 HOH A O   1 
HETATM 2050 O  O   . HOH H 6 .   ? 43.769 24.565 13.242 1.00 58.39  ? 528 HOH A O   1 
HETATM 2051 O  O   . HOH H 6 .   ? 16.180 22.291 32.366 1.00 41.61  ? 529 HOH A O   1 
HETATM 2052 O  O   . HOH H 6 .   ? 49.200 26.809 19.355 1.00 53.71  ? 530 HOH A O   1 
HETATM 2053 O  O   . HOH H 6 .   ? 47.379 22.489 22.319 1.00 49.24  ? 531 HOH A O   1 
HETATM 2054 O  O   . HOH H 6 .   ? 43.288 3.157  2.834  1.00 48.01  ? 532 HOH A O   1 
HETATM 2055 O  O   . HOH H 6 .   ? 33.217 1.272  18.633 1.00 60.93  ? 533 HOH A O   1 
HETATM 2056 O  O   . HOH H 6 .   ? 45.284 27.143 17.007 1.00 41.17  ? 534 HOH A O   1 
HETATM 2057 O  O   . HOH H 6 .   ? 42.888 18.214 23.050 1.00 58.29  ? 535 HOH A O   1 
HETATM 2058 O  O   . HOH H 6 .   ? 20.412 14.809 39.177 1.00 59.33  ? 536 HOH A O   1 
HETATM 2059 O  O   . HOH H 6 .   ? 8.937  25.194 35.496 1.00 57.34  ? 537 HOH A O   1 
HETATM 2060 O  O   . HOH H 6 .   ? 15.403 14.680 40.632 1.00 56.39  ? 538 HOH A O   1 
HETATM 2061 O  O   . HOH H 6 .   ? 29.981 7.813  1.159  1.00 49.41  ? 539 HOH A O   1 
HETATM 2062 O  O   . HOH H 6 .   ? 29.279 29.472 30.881 1.00 43.66  ? 540 HOH A O   1 
HETATM 2063 O  O   . HOH H 6 .   ? 32.553 33.917 28.568 1.00 67.58  ? 541 HOH A O   1 
HETATM 2064 O  O   . HOH H 6 .   ? 50.420 30.797 16.802 1.00 53.37  ? 542 HOH A O   1 
HETATM 2065 O  O   . HOH I 6 .   ? 22.935 16.337 22.368 1.00 34.20  ? 301 HOH P O   1 
HETATM 2066 O  O   . HOH I 6 .   ? 21.024 14.574 28.046 1.00 43.56  ? 302 HOH P O   1 
HETATM 2067 O  O   . HOH I 6 .   ? 23.207 11.272 25.677 1.00 44.03  ? 303 HOH P O   1 
HETATM 2068 O  O   . HOH I 6 .   ? 27.864 13.017 27.311 1.00 45.35  ? 304 HOH P O   1 
HETATM 2069 O  O   . HOH I 6 .   ? 17.266 14.511 26.423 1.00 41.65  ? 305 HOH P O   1 
HETATM 2070 O  O   . HOH I 6 .   ? 31.499 16.165 20.967 1.00 38.59  ? 306 HOH P O   1 
HETATM 2071 O  O   . HOH I 6 .   ? 27.381 16.310 21.582 1.00 33.52  ? 307 HOH P O   1 
HETATM 2072 O  O   . HOH I 6 .   ? 20.794 12.173 26.887 1.00 38.14  ? 308 HOH P O   1 
HETATM 2073 O  O   . HOH I 6 .   ? 36.707 10.403 18.094 1.00 60.53  ? 309 HOH P O   1 
HETATM 2074 O  O   . HOH I 6 .   ? 14.850 15.093 26.513 1.00 50.82  ? 310 HOH P O   1 
HETATM 2075 O  O   . HOH I 6 .   ? 24.340 8.576  26.316 1.00 56.87  ? 311 HOH P O   1 
HETATM 2076 O  O   . HOH I 6 .   ? 26.488 7.392  24.843 1.00 47.32  ? 312 HOH P O   1 
HETATM 2077 O  O   . HOH I 6 .   ? 28.568 8.179  25.243 1.00 50.20  ? 313 HOH P O   1 
# 
