data_8QS6
# 
_entry.id   8QS6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8QS6         pdb_00008qs6 10.2210/pdb8qs6/pdb 
WWPDB D_1292132194 ?            ?                   
# 
_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       2025-04-23 
_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                        8QS6 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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            ? 
_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 
'Konstantinidou, M.' 1  ? 
'Vickery, H.'        2  ? 
'Pennings, M.A.M.'   3  ? 
'Virta, J.'          4  ? 
'Visser, E.J.'       5  ? 
'Oetelaar, M.C.M.'   6  ? 
'Overmans, M.'       7  ? 
'Neitz, J.'          8  ? 
'Ottmann, C.'        9  ? 
'Brunsveld, L.'      10 ? 
'Arkin, M.R.'        11 ? 
# 
_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                     'Small molecule stabilization of the 14-3-3sigma/CRAF complex inhibits the MAPK pathway' 
_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 'Konstantinidou, M.' 1  ? 
primary 'Vickery, H.'        2  ? 
primary 'Pennings, M.A.M.'   3  ? 
primary 'Virta, J.'          4  ? 
primary 'Visser, E.J.'       5  ? 
primary 'Oetelaar, M.C.M.'   6  ? 
primary 'Overmans, M.'       7  ? 
primary 'Neitz, J.'          8  ? 
primary 'Ottmann, C.'        9  ? 
primary 'Brunsveld, L.'      10 ? 
primary 'Arkin, M.R.'        11 ? 
# 
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  ? ? 
? ? 
2 polymer     syn 'C-RAF peptide pS259'                                                                           1208.175  1  ? ? 
? ? 
3 non-polymer syn 'CHLORIDE ION'                                                                                  35.453    1  ? ? 
? ? 
4 non-polymer syn 'MAGNESIUM ION'                                                                                 24.305    4  ? ? 
? ? 
5 non-polymer syn '~{N}-[[1-(4-bromanyl-3-fluoranyl-phenyl)sulfonylpiperidin-4-yl]methyl]-2-chloranyl-ethanamide' 427.717   1  ? ? 
? ? 
6 water       nat water                                                                                           18.015    97 ? ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Epithelial cell marker protein 1,Stratifin' 
# 
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 'QRST(SEP)TPNVH' QRSTSTPNVH 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 '~{N}-[[1-(4-bromanyl-3-fluoranyl-phenyl)sulfonylpiperidin-4-yl]methyl]-2-chloranyl-ethanamide' WQ0 
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   GLN n 
2 2   ARG n 
2 3   SER n 
2 4   THR n 
2 5   SEP n 
2 6   THR n 
2 7   PRO n 
2 8   ASN n 
2 9   VAL n 
2 10  HIS 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       10 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   ? 
_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 
WQ0 non-polymer         . '~{N}-[[1-(4-bromanyl-3-fluoranyl-phenyl)sulfonylpiperidin-4-yl]methyl]-2-chloranyl-ethanamide' ? 
'C14 H17 Br Cl F N2 O3 S' 427.717 
# 
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 CYS 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  ?   ?   ?   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   GLN 1   255 255 GLN GLN P . n 
B 2 2   ARG 2   256 256 ARG ARG P . n 
B 2 3   SER 3   257 257 SER SER P . n 
B 2 4   THR 4   258 258 THR THR P . n 
B 2 5   SEP 5   259 259 SEP SEP P . n 
B 2 6   THR 6   260 260 THR THR P . n 
B 2 7   PRO 7   261 261 PRO PRO P . n 
B 2 8   ASN 8   262 262 ASN ASN P . n 
B 2 9   VAL 9   263 263 VAL VAL P . n 
B 2 10  HIS 10  264 264 HIS HIS P . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WQ0 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WQ0 
_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  301 232 CL  CL  A . 
D 4 MG  1  302 233 MG  MG  A . 
E 4 MG  1  303 234 MG  MG  A . 
F 4 MG  1  304 235 MG  MG  A . 
G 5 WQ0 1  305 236 WQ0 917 A . 
H 4 MG  1  306 1   MG  MG  A . 
I 6 HOH 1  401 2   HOH HOH A . 
I 6 HOH 2  402 32  HOH HOH A . 
I 6 HOH 3  403 5   HOH HOH A . 
I 6 HOH 4  404 28  HOH HOH A . 
I 6 HOH 5  405 78  HOH HOH A . 
I 6 HOH 6  406 80  HOH HOH A . 
I 6 HOH 7  407 73  HOH HOH A . 
I 6 HOH 8  408 16  HOH HOH A . 
I 6 HOH 9  409 38  HOH HOH A . 
I 6 HOH 10 410 46  HOH HOH A . 
I 6 HOH 11 411 18  HOH HOH A . 
I 6 HOH 12 412 31  HOH HOH A . 
I 6 HOH 13 413 51  HOH HOH A . 
I 6 HOH 14 414 85  HOH HOH A . 
I 6 HOH 15 415 91  HOH HOH A . 
I 6 HOH 16 416 65  HOH HOH A . 
I 6 HOH 17 417 97  HOH HOH A . 
I 6 HOH 18 418 87  HOH HOH A . 
I 6 HOH 19 419 53  HOH HOH A . 
I 6 HOH 20 420 35  HOH HOH A . 
I 6 HOH 21 421 14  HOH HOH A . 
I 6 HOH 22 422 114 HOH HOH A . 
I 6 HOH 23 423 12  HOH HOH A . 
I 6 HOH 24 424 102 HOH HOH A . 
I 6 HOH 25 425 101 HOH HOH A . 
I 6 HOH 26 426 44  HOH HOH A . 
I 6 HOH 27 427 17  HOH HOH A . 
I 6 HOH 28 428 69  HOH HOH A . 
I 6 HOH 29 429 61  HOH HOH A . 
I 6 HOH 30 430 20  HOH HOH A . 
I 6 HOH 31 431 60  HOH HOH A . 
I 6 HOH 32 432 107 HOH HOH A . 
I 6 HOH 33 433 109 HOH HOH A . 
I 6 HOH 34 434 15  HOH HOH A . 
I 6 HOH 35 435 94  HOH HOH A . 
I 6 HOH 36 436 48  HOH HOH A . 
I 6 HOH 37 437 23  HOH HOH A . 
I 6 HOH 38 438 67  HOH HOH A . 
I 6 HOH 39 439 10  HOH HOH A . 
I 6 HOH 40 440 37  HOH HOH A . 
I 6 HOH 41 441 110 HOH HOH A . 
I 6 HOH 42 442 72  HOH HOH A . 
I 6 HOH 43 443 81  HOH HOH A . 
I 6 HOH 44 444 34  HOH HOH A . 
I 6 HOH 45 445 13  HOH HOH A . 
I 6 HOH 46 446 29  HOH HOH A . 
I 6 HOH 47 447 117 HOH HOH A . 
I 6 HOH 48 448 105 HOH HOH A . 
I 6 HOH 49 449 24  HOH HOH A . 
I 6 HOH 50 450 56  HOH HOH A . 
I 6 HOH 51 451 77  HOH HOH A . 
I 6 HOH 52 452 68  HOH HOH A . 
I 6 HOH 53 453 30  HOH HOH A . 
I 6 HOH 54 454 104 HOH HOH A . 
I 6 HOH 55 455 92  HOH HOH A . 
I 6 HOH 56 456 19  HOH HOH A . 
I 6 HOH 57 457 6   HOH HOH A . 
I 6 HOH 58 458 86  HOH HOH A . 
I 6 HOH 59 459 40  HOH HOH A . 
I 6 HOH 60 460 36  HOH HOH A . 
I 6 HOH 61 461 116 HOH HOH A . 
I 6 HOH 62 462 25  HOH HOH A . 
I 6 HOH 63 463 57  HOH HOH A . 
I 6 HOH 64 464 82  HOH HOH A . 
I 6 HOH 65 465 106 HOH HOH A . 
I 6 HOH 66 466 52  HOH HOH A . 
I 6 HOH 67 467 9   HOH HOH A . 
I 6 HOH 68 468 115 HOH HOH A . 
I 6 HOH 69 469 49  HOH HOH A . 
I 6 HOH 70 470 76  HOH HOH A . 
I 6 HOH 71 471 93  HOH HOH A . 
I 6 HOH 72 472 22  HOH HOH A . 
I 6 HOH 73 473 27  HOH HOH A . 
I 6 HOH 74 474 11  HOH HOH A . 
I 6 HOH 75 475 47  HOH HOH A . 
I 6 HOH 76 476 7   HOH HOH A . 
I 6 HOH 77 477 89  HOH HOH A . 
I 6 HOH 78 478 8   HOH HOH A . 
I 6 HOH 79 479 99  HOH HOH A . 
I 6 HOH 80 480 39  HOH HOH A . 
I 6 HOH 81 481 50  HOH HOH A . 
I 6 HOH 82 482 95  HOH HOH A . 
I 6 HOH 83 483 108 HOH HOH A . 
I 6 HOH 84 484 112 HOH HOH A . 
I 6 HOH 85 485 90  HOH HOH A . 
I 6 HOH 86 486 100 HOH HOH A . 
I 6 HOH 87 487 98  HOH HOH A . 
I 6 HOH 88 488 41  HOH HOH A . 
I 6 HOH 89 489 43  HOH HOH A . 
I 6 HOH 90 490 26  HOH HOH A . 
I 6 HOH 91 491 96  HOH HOH A . 
J 6 HOH 1  301 59  HOH HOH P . 
J 6 HOH 2  302 54  HOH HOH P . 
J 6 HOH 3  303 33  HOH HOH P . 
J 6 HOH 4  304 21  HOH HOH P . 
J 6 HOH 5  305 63  HOH HOH P . 
J 6 HOH 6  306 64  HOH HOH P . 
# 
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 ? ? ? . 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                     8QS6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.390 
_cell.length_a_esd                 ? 
_cell.length_b                     149.455 
_cell.length_b_esd                 ? 
_cell.length_c                     76.526 
_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                         8QS6 
_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                   8QS6 
_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             3.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.73 
_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    
;0.095 M HEPES pH=7.1-7.7
0.19 M CaCl2 
5% glycerol
24-29% PEG400
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-30 
_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   0.885603 
_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 ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.885603 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QS6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               74.84 
_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                                     31248 
_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                           93.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.2 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1955 
_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                                  0.689 
_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]                            1.53 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -1.41 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.12 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               33.408 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8QS6 
_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                            1.80 
_refine.ls_d_res_low                             74.84 
_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                     29660 
_refine.ls_number_reflns_R_free                  1587 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.01 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20388 
_refine.ls_R_factor_R_free                       0.24571 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20171 
_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                    ? 
_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       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.116 
_refine.pdbx_overall_ESU_R_Free                  0.120 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                             6.638 
_refine.overall_SU_ML                            0.101 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        74.84 
_refine_hist.number_atoms_solvent             97 
_refine_hist.number_atoms_total               2018 
_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        1894 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         27 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_struct.entry_id                     8QS6 
_struct.title                        'Ternary structure of 14-3-3s, C-RAF phosphopeptide (pS259) and compound 21 (1075354)' 
_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        8QS6 
_struct_keywords.text            'Stabilizer, protein-protein interaction, 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 4 ? 
I N N 6 ? 
J 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 PDB 8QS6        8QS6   ? 2 ? 1 
# 
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 8QS6 A 6 ? 236 ? P31947 1   ? 231 ? 1   231 
2 2 8QS6 P 1 ? 10  ? 8QS6   255 ? 264 ? 255 264 
# 
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 8QS6 GLY A 1 ? UNP P31947 ? ? 'expression tag' -4 1 
1 8QS6 ALA A 2 ? UNP P31947 ? ? 'expression tag' -3 2 
1 8QS6 MET A 3 ? UNP P31947 ? ? 'expression tag' -2 3 
1 8QS6 GLY A 4 ? UNP P31947 ? ? 'expression tag' -1 4 
1 8QS6 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)' 5790  ? 
1 MORE         -78   ? 
1 'SSA (A^2)'  22480 ? 
# 
_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,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
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 62.3900000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 76.5260000000 
# 
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  ? GLU A 36  ? ARG A 18  GLU A 31  1 ? 14 
HELX_P HELX_P3  AA3 SER A 42  ? SER A 74  ? SER A 37  SER A 69  1 ? 33 
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 ? THR A 236 ? SER A 212 THR A 231 1 ? 20 
# 
_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 WQ0 . C2 ? ? A CYS 38  A WQ0 305 1_555 ? ? ? ? ? ? ? 1.835 ? ? 
covale2 covale both ? B THR 4   C   ? ? ? 1_555 B SEP 5 N  ? ? P THR 258 P SEP 259 1_555 ? ? ? ? ? ? ? 1.337 ? ? 
covale3 covale both ? B SEP 5   C   ? ? ? 1_555 B THR 6 N  ? ? P SEP 259 P THR 260 1_555 ? ? ? ? ? ? ? 1.343 ? ? 
metalc1 metalc ?    ? A GLU 7   OE2 ? ? ? 1_555 F MG  . MG ? ? A GLU 2   A MG  304 6_655 ? ? ? ? ? ? ? 2.881 ? ? 
metalc2 metalc ?    ? A GLU 94  OE2 ? ? ? 1_555 D MG  . MG ? ? A GLU 89  A MG  302 1_555 ? ? ? ? ? ? ? 2.366 ? ? 
metalc3 metalc ?    ? A ALA 208 O   ? ? ? 1_555 H MG  . MG ? ? A ALA 203 A MG  306 4_555 ? ? ? ? ? ? ? 2.054 ? ? 
metalc4 metalc ?    ? A ASP 209 OD1 ? ? ? 1_555 H MG  . MG ? ? A ASP 204 A MG  306 1_555 ? ? ? ? ? ? ? 2.366 ? ? 
metalc5 metalc ?    ? D MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  302 A HOH 405 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
metalc6 metalc ?    ? D MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  302 A HOH 480 1_555 ? ? ? ? ? ? ? 2.578 ? ? 
metalc7 metalc ?    ? H MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  306 A HOH 408 4_555 ? ? ? ? ? ? ? 2.350 ? ? 
metalc8 metalc ?    ? H MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  306 A HOH 443 1_555 ? ? ? ? ? ? ? 2.200 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OE2 ? A GLU 94  ? A GLU 89  ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 405 ? 1_555 67.3 ? 
2 OE2 ? A GLU 94  ? A GLU 89  ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 480 ? 1_555 83.4 ? 
3 O   ? I HOH .   ? A HOH 405 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 480 ? 1_555 60.5 ? 
4 O   ? A ALA 208 ? A ALA 203 ? 1_555 MG ? H MG . ? A MG 306 ? 4_555 OD1 ? A ASP 209 ? A ASP 204 ? 1_555 48.2 ? 
5 O   ? A ALA 208 ? A ALA 203 ? 1_555 MG ? H MG . ? A MG 306 ? 4_555 O   ? I HOH .   ? A HOH 408 ? 4_555 94.2 ? 
6 OD1 ? A ASP 209 ? A ASP 204 ? 1_555 MG ? H MG . ? A MG 306 ? 4_555 O   ? I HOH .   ? A HOH 408 ? 4_555 48.0 ? 
7 O   ? A ALA 208 ? A ALA 203 ? 1_555 MG ? H MG . ? A MG 306 ? 4_555 O   ? I HOH .   ? A HOH 443 ? 1_555 69.4 ? 
8 OD1 ? A ASP 209 ? A ASP 204 ? 1_555 MG ? H MG . ? A MG 306 ? 4_555 O   ? I HOH .   ? A HOH 443 ? 1_555 37.3 ? 
9 O   ? I HOH .   ? A HOH 408 ? 4_555 MG ? H MG . ? A MG 306 ? 4_555 O   ? I HOH .   ? A HOH 443 ? 1_555 56.3 ? 
# 
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 5 ? .   . .  . SEP P 259 ? 1_555 .   . .  . .     .  .  SER 1 SEP Phosphorylation 'Named protein modification'     
2 WQ0 G . ? CYS A 43 ? WQ0 A 305 ? 1_555 CYS A 38 ? 1_555 C2 SG CYS 1 WQ0 None            'Covalent chemical modification' 
# 
_pdbx_entry_details.entry_id                   8QS6 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   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  ? ? -103.68 78.86  
2 1 ASP A 113 ? ? -36.18  142.85 
3 1 THR A 136 ? ? -125.95 -57.60 
4 1 SER A 212 ? ? -143.36 13.43  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 41  ? ? 0.125 'SIDE CHAIN' 
2 1 ARG A 117 ? ? 0.098 'SIDE CHAIN' 
3 1 ARG P 256 ? ? 0.130 'SIDE CHAIN' 
# 
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 A LYS 77 ? A LYS 82 
# 
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 
WQ0 C13  C  N N 412 
WQ0 C12  C  Y N 413 
WQ0 C14  C  N N 414 
WQ0 O1   O  N N 415 
WQ0 C1   C  N N 416 
WQ0 C2   C  N N 417 
WQ0 N1   N  N N 418 
WQ0 C3   C  N N 419 
WQ0 C4   C  N N 420 
WQ0 C5   C  N N 421 
WQ0 C6   C  N N 422 
WQ0 N2   N  N N 423 
WQ0 S1   S  N N 424 
WQ0 O2   O  N N 425 
WQ0 O3   O  N N 426 
WQ0 C7   C  Y N 427 
WQ0 C8   C  Y N 428 
WQ0 C9   C  Y N 429 
WQ0 C10  C  Y N 430 
WQ0 BR1  BR N N 431 
WQ0 C11  C  Y N 432 
WQ0 F1   F  N N 433 
WQ0 H1   H  N N 434 
WQ0 H2   H  N N 435 
WQ0 H3   H  N N 436 
WQ0 H4   H  N N 437 
WQ0 H5   H  N N 438 
WQ0 H6   H  N N 439 
WQ0 H7   H  N N 440 
WQ0 H9   H  N N 441 
WQ0 H10  H  N N 442 
WQ0 H11  H  N N 443 
WQ0 H12  H  N N 444 
WQ0 H13  H  N N 445 
WQ0 H14  H  N N 446 
WQ0 H15  H  N N 447 
WQ0 H16  H  N N 448 
WQ0 H17  H  N N 449 
WQ0 H18  H  N N 450 
WQ0 CL1  CL N N 451 
# 
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 
WQ0 C2  C1   sing N N 394 
WQ0 O1  C1   doub N N 395 
WQ0 C1  N1   sing N N 396 
WQ0 N1  C3   sing N N 397 
WQ0 C14 C13  sing N N 398 
WQ0 C14 C4   sing N N 399 
WQ0 C3  C4   sing N N 400 
WQ0 C13 N2   sing N N 401 
WQ0 C4  C5   sing N N 402 
WQ0 O2  S1   doub N N 403 
WQ0 F1  C11  sing N N 404 
WQ0 N2  S1   sing N N 405 
WQ0 N2  C6   sing N N 406 
WQ0 C12 C11  doub Y N 407 
WQ0 C12 C7   sing Y N 408 
WQ0 C5  C6   sing N N 409 
WQ0 S1  C7   sing N N 410 
WQ0 S1  O3   doub N N 411 
WQ0 C11 C10  sing Y N 412 
WQ0 C7  C8   doub Y N 413 
WQ0 C10 BR1  sing N N 414 
WQ0 C10 C9   doub Y N 415 
WQ0 C8  C9   sing Y N 416 
WQ0 C13 H1   sing N N 417 
WQ0 C13 H2   sing N N 418 
WQ0 C12 H3   sing N N 419 
WQ0 C14 H4   sing N N 420 
WQ0 C14 H5   sing N N 421 
WQ0 C2  H6   sing N N 422 
WQ0 C2  H7   sing N N 423 
WQ0 N1  H9   sing N N 424 
WQ0 C3  H10  sing N N 425 
WQ0 C3  H11  sing N N 426 
WQ0 C4  H12  sing N N 427 
WQ0 C5  H13  sing N N 428 
WQ0 C5  H14  sing N N 429 
WQ0 C6  H15  sing N N 430 
WQ0 C6  H16  sing N N 431 
WQ0 C8  H17  sing N N 432 
WQ0 C9  H18  sing N N 433 
WQ0 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   3IQU 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8QS6 
_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]   0.016028 
_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]   0.006691 
_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]   0.013067 
_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 
BR 
C  
CL 
F  
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   ? 35.202 41.323 24.784 1.00 57.72  ? -4  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 1   ? 35.210 40.339 25.855 1.00 109.35 ? -4  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 1   ? 36.544 40.272 26.595 1.00 55.57  ? -4  GLY A C   1 
ATOM   4    O  O   . GLY A 1 1   ? 37.515 40.923 26.205 1.00 44.36  ? -4  GLY A O   1 
ATOM   5    N  N   . ALA A 1 2   ? 36.569 39.457 27.657 1.00 54.85  ? -3  ALA A N   1 
ATOM   6    C  CA  . ALA A 1 2   ? 37.756 39.252 28.469 1.00 62.83  ? -3  ALA A CA  1 
ATOM   7    C  C   . ALA A 1 2   ? 38.833 38.417 27.775 1.00 36.92  ? -3  ALA A C   1 
ATOM   8    O  O   . ALA A 1 2   ? 39.938 38.298 28.298 1.00 34.83  ? -3  ALA A O   1 
ATOM   9    C  CB  . ALA A 1 2   ? 37.367 38.594 29.786 1.00 74.44  ? -3  ALA A CB  1 
ATOM   10   N  N   . MET A 1 3   ? 38.506 37.835 26.608 1.00 38.50  ? -2  MET A N   1 
ATOM   11   C  CA  . MET A 1 3   ? 39.444 37.024 25.842 1.00 29.81  ? -2  MET A CA  1 
ATOM   12   C  C   . MET A 1 3   ? 40.055 37.785 24.668 1.00 34.04  ? -2  MET A C   1 
ATOM   13   O  O   . MET A 1 3   ? 40.861 37.232 23.916 1.00 23.88  ? -2  MET A O   1 
ATOM   14   C  CB  . MET A 1 3   ? 38.722 35.776 25.325 1.00 26.44  ? -2  MET A CB  1 
ATOM   15   C  CG  . MET A 1 3   ? 38.260 34.835 26.439 1.00 28.52  ? -2  MET A CG  1 
ATOM   16   S  SD  . MET A 1 3   ? 39.595 34.389 27.564 1.00 34.82  ? -2  MET A SD  1 
ATOM   17   C  CE  . MET A 1 3   ? 38.739 33.386 28.692 1.00 39.87  ? -2  MET A CE  1 
ATOM   18   N  N   . GLY A 1 4   ? 39.693 39.070 24.550 1.00 33.89  ? -1  GLY A N   1 
ATOM   19   C  CA  . GLY A 1 4   ? 40.036 39.893 23.400 1.00 36.50  ? -1  GLY A CA  1 
ATOM   20   C  C   . GLY A 1 4   ? 41.530 40.099 23.165 1.00 36.67  ? -1  GLY A C   1 
ATOM   21   O  O   . GLY A 1 4   ? 41.951 40.255 22.025 1.00 24.20  ? -1  GLY A O   1 
ATOM   22   N  N   . SER A 1 5   ? 42.332 40.070 24.239 1.00 21.43  ? 0   SER A N   1 
ATOM   23   C  CA  . SER A 1 5   ? 43.759 40.334 24.125 1.00 16.78  ? 0   SER A CA  1 
ATOM   24   C  C   . SER A 1 5   ? 44.563 39.069 23.818 1.00 13.48  ? 0   SER A C   1 
ATOM   25   O  O   . SER A 1 5   ? 45.753 39.166 23.543 1.00 25.61  ? 0   SER A O   1 
ATOM   26   C  CB  . SER A 1 5   ? 44.310 40.975 25.397 1.00 15.13  ? 0   SER A CB  1 
ATOM   27   O  OG  . SER A 1 5   ? 44.103 40.118 26.507 1.00 27.98  ? 0   SER A OG  1 
ATOM   28   N  N   . MET A 1 6   ? 43.908 37.907 23.872 1.00 18.74  ? 1   MET A N   1 
ATOM   29   C  CA  . MET A 1 6   ? 44.591 36.636 23.685 1.00 20.52  ? 1   MET A CA  1 
ATOM   30   C  C   . MET A 1 6   ? 44.537 36.149 22.242 1.00 19.49  ? 1   MET A C   1 
ATOM   31   O  O   . MET A 1 6   ? 43.494 36.187 21.597 1.00 23.59  ? 1   MET A O   1 
ATOM   32   C  CB  . MET A 1 6   ? 44.029 35.551 24.631 1.00 26.51  ? 1   MET A CB  1 
ATOM   33   C  CG  . MET A 1 6   ? 45.111 34.596 25.129 1.00 32.93  ? 1   MET A CG  1 
ATOM   34   S  SD  . MET A 1 6   ? 44.429 33.192 26.066 1.00 30.58  ? 1   MET A SD  1 
ATOM   35   C  CE  . MET A 1 6   ? 43.515 34.111 27.288 1.00 27.96  ? 1   MET A CE  1 
ATOM   36   N  N   . GLU A 1 7   ? 45.687 35.691 21.747 1.00 21.01  ? 2   GLU A N   1 
ATOM   37   C  CA  . GLU A 1 7   ? 45.753 35.062 20.440 1.00 21.99  ? 2   GLU A CA  1 
ATOM   38   C  C   . GLU A 1 7   ? 44.794 33.893 20.289 1.00 23.09  ? 2   GLU A C   1 
ATOM   39   O  O   . GLU A 1 7   ? 44.655 33.058 21.183 1.00 20.13  ? 2   GLU A O   1 
ATOM   40   C  CB  . GLU A 1 7   ? 47.166 34.591 20.149 1.00 24.79  ? 2   GLU A CB  1 
ATOM   41   C  CG  . GLU A 1 7   ? 48.076 35.756 19.844 1.00 26.87  ? 2   GLU A CG  1 
ATOM   42   C  CD  . GLU A 1 7   ? 49.452 35.343 19.396 1.00 34.43  ? 2   GLU A CD  1 
ATOM   43   O  OE1 . GLU A 1 7   ? 49.840 34.178 19.647 1.00 35.63  ? 2   GLU A OE1 1 
ATOM   44   O  OE2 . GLU A 1 7   ? 50.139 36.181 18.775 1.00 24.91  ? 2   GLU A OE2 1 
ATOM   45   N  N   . ARG A 1 8   ? 44.157 33.832 19.118 1.00 20.80  ? 3   ARG A N   1 
ATOM   46   C  CA  . ARG A 1 8   ? 43.291 32.717 18.772 1.00 22.66  ? 3   ARG A CA  1 
ATOM   47   C  C   . ARG A 1 8   ? 43.893 31.352 19.105 1.00 19.12  ? 3   ARG A C   1 
ATOM   48   O  O   . ARG A 1 8   ? 43.207 30.488 19.656 1.00 24.18  ? 3   ARG A O   1 
ATOM   49   C  CB  . ARG A 1 8   ? 42.963 32.772 17.262 1.00 20.39  ? 3   ARG A CB  1 
ATOM   50   C  CG  . ARG A 1 8   ? 41.880 31.780 16.855 1.00 24.17  ? 3   ARG A CG  1 
ATOM   51   C  CD  . ARG A 1 8   ? 41.666 31.729 15.374 1.00 28.19  ? 3   ARG A CD  1 
ATOM   52   N  NE  . ARG A 1 8   ? 40.458 30.986 15.045 1.00 24.27  ? 3   ARG A NE  1 
ATOM   53   C  CZ  . ARG A 1 8   ? 40.341 29.665 15.073 1.00 29.53  ? 3   ARG A CZ  1 
ATOM   54   N  NH1 . ARG A 1 8   ? 41.357 28.881 15.401 1.00 26.96  ? 3   ARG A NH1 1 
ATOM   55   N  NH2 . ARG A 1 8   ? 39.175 29.117 14.750 1.00 31.84  ? 3   ARG A NH2 1 
ATOM   56   N  N   . ALA A 1 9   ? 45.158 31.137 18.717 1.00 22.41  ? 4   ALA A N   1 
ATOM   57   C  CA  . ALA A 1 9   ? 45.791 29.834 18.895 1.00 24.39  ? 4   ALA A CA  1 
ATOM   58   C  C   . ALA A 1 9   ? 45.997 29.498 20.377 1.00 22.92  ? 4   ALA A C   1 
ATOM   59   O  O   . ALA A 1 9   ? 45.889 28.338 20.771 1.00 21.28  ? 4   ALA A O   1 
ATOM   60   C  CB  . ALA A 1 9   ? 47.121 29.791 18.150 1.00 24.33  ? 4   ALA A CB  1 
ATOM   61   N  N   . SER A 1 10  ? 46.287 30.523 21.190 1.00 21.07  ? 5   SER A N   1 
ATOM   62   C  CA  . SER A 1 10  ? 46.423 30.366 22.631 1.00 21.27  ? 5   SER A CA  1 
ATOM   63   C  C   . SER A 1 10  ? 45.083 30.029 23.279 1.00 27.79  ? 5   SER A C   1 
ATOM   64   O  O   . SER A 1 10  ? 45.013 29.245 24.227 1.00 20.90  ? 5   SER A O   1 
ATOM   65   C  CB  . SER A 1 10  ? 47.028 31.624 23.246 1.00 21.73  ? 5   SER A CB  1 
ATOM   66   O  OG  . SER A 1 10  ? 48.310 31.867 22.694 1.00 22.13  ? 5   SER A OG  1 
ATOM   67   N  N   . LEU A 1 11  ? 44.007 30.603 22.736 1.00 20.26  ? 6   LEU A N   1 
ATOM   68   C  CA  . LEU A 1 11  ? 42.670 30.318 23.222 1.00 20.13  ? 6   LEU A CA  1 
ATOM   69   C  C   . LEU A 1 11  ? 42.268 28.870 22.935 1.00 25.67  ? 6   LEU A C   1 
ATOM   70   O  O   . LEU A 1 11  ? 41.702 28.202 23.802 1.00 23.45  ? 6   LEU A O   1 
ATOM   71   C  CB  . LEU A 1 11  ? 41.680 31.288 22.588 1.00 21.87  ? 6   LEU A CB  1 
ATOM   72   C  CG  . LEU A 1 11  ? 41.718 32.707 23.117 1.00 16.95  ? 6   LEU A CG  1 
ATOM   73   C  CD1 . LEU A 1 11  ? 40.927 33.654 22.200 1.00 20.23  ? 6   LEU A CD1 1 
ATOM   74   C  CD2 . LEU A 1 11  ? 41.180 32.768 24.543 1.00 22.57  ? 6   LEU A CD2 1 
ATOM   75   N  N   . ILE A 1 12  ? 42.585 28.381 21.727 1.00 22.40  ? 7   ILE A N   1 
ATOM   76   C  CA  . ILE A 1 12  ? 42.340 26.984 21.390 1.00 19.24  ? 7   ILE A CA  1 
ATOM   77   C  C   . ILE A 1 12  ? 43.143 26.040 22.290 1.00 22.44  ? 7   ILE A C   1 
ATOM   78   O  O   . ILE A 1 12  ? 42.603 25.047 22.783 1.00 25.33  ? 7   ILE A O   1 
ATOM   79   C  CB  . ILE A 1 12  ? 42.648 26.677 19.922 1.00 19.76  ? 7   ILE A CB  1 
ATOM   80   C  CG1 . ILE A 1 12  ? 41.760 27.520 18.941 1.00 27.17  ? 7   ILE A CG1 1 
ATOM   81   C  CG2 . ILE A 1 12  ? 42.519 25.182 19.628 1.00 26.27  ? 7   ILE A CG2 1 
ATOM   82   C  CD1 . ILE A 1 12  ? 40.292 27.269 19.079 1.00 29.45  ? 7   ILE A CD1 1 
ATOM   83   N  N   . GLN A 1 13  ? 44.427 26.357 22.468 1.00 20.75  ? 8   GLN A N   1 
ATOM   84   C  CA  . GLN A 1 13  ? 45.315 25.603 23.335 1.00 26.78  ? 8   GLN A CA  1 
ATOM   85   C  C   . GLN A 1 13  ? 44.787 25.548 24.769 1.00 29.92  ? 8   GLN A C   1 
ATOM   86   O  O   . GLN A 1 13  ? 44.806 24.483 25.392 1.00 24.70  ? 8   GLN A O   1 
ATOM   87   C  CB  . GLN A 1 13  ? 46.718 26.205 23.276 1.00 29.45  ? 8   GLN A CB  1 
ATOM   88   C  CG  . GLN A 1 13  ? 47.767 25.516 24.165 1.00 40.46  ? 8   GLN A CG  1 
ATOM   89   C  CD  . GLN A 1 13  ? 49.142 26.133 24.011 1.00 91.94  ? 8   GLN A CD  1 
ATOM   90   O  OE1 . GLN A 1 13  ? 49.359 27.052 23.196 1.00 40.26  ? 8   GLN A OE1 1 
ATOM   91   N  NE2 . GLN A 1 13  ? 50.102 25.641 24.804 1.00 32.53  ? 8   GLN A NE2 1 
ATOM   92   N  N   . LYS A 1 14  ? 44.307 26.689 25.286 1.00 25.11  ? 9   LYS A N   1 
ATOM   93   C  CA  . LYS A 1 14  ? 43.760 26.732 26.636 1.00 24.32  ? 9   LYS A CA  1 
ATOM   94   C  C   . LYS A 1 14  ? 42.414 26.016 26.769 1.00 24.78  ? 9   LYS A C   1 
ATOM   95   O  O   . LYS A 1 14  ? 42.144 25.442 27.814 1.00 23.98  ? 9   LYS A O   1 
ATOM   96   C  CB  . LYS A 1 14  ? 43.697 28.175 27.160 1.00 17.78  ? 9   LYS A CB  1 
ATOM   97   C  CG  . LYS A 1 14  ? 45.078 28.722 27.461 1.00 19.69  ? 9   LYS A CG  1 
ATOM   98   C  CD  . LYS A 1 14  ? 45.064 30.111 28.114 1.00 26.04  ? 9   LYS A CD  1 
ATOM   99   C  CE  . LYS A 1 14  ? 46.435 30.686 28.170 1.00 24.03  ? 9   LYS A CE  1 
ATOM   100  N  NZ  . LYS A 1 14  ? 46.402 32.103 28.595 1.00 23.77  ? 9   LYS A NZ  1 
ATOM   101  N  N   . ALA A 1 15  ? 41.588 25.999 25.713 1.00 23.14  ? 10  ALA A N   1 
ATOM   102  C  CA  . ALA A 1 15  ? 40.355 25.220 25.726 1.00 26.64  ? 10  ALA A CA  1 
ATOM   103  C  C   . ALA A 1 15  ? 40.661 23.734 25.903 1.00 28.15  ? 10  ALA A C   1 
ATOM   104  O  O   . ALA A 1 15  ? 39.958 23.021 26.629 1.00 24.28  ? 10  ALA A O   1 
ATOM   105  C  CB  . ALA A 1 15  ? 39.536 25.457 24.462 1.00 24.85  ? 10  ALA A CB  1 
ATOM   106  N  N   . LYS A 1 16  ? 41.737 23.277 25.261 1.00 22.20  ? 11  LYS A N   1 
ATOM   107  C  CA  . LYS A 1 16  ? 42.135 21.879 25.357 1.00 28.52  ? 11  LYS A CA  1 
ATOM   108  C  C   . LYS A 1 16  ? 42.654 21.530 26.750 1.00 31.40  ? 11  LYS A C   1 
ATOM   109  O  O   . LYS A 1 16  ? 42.325 20.474 27.277 1.00 28.22  ? 11  LYS A O   1 
ATOM   110  C  CB  . LYS A 1 16  ? 43.183 21.537 24.306 1.00 27.10  ? 11  LYS A CB  1 
ATOM   111  C  CG  . LYS A 1 16  ? 42.630 21.554 22.889 1.00 27.89  ? 11  LYS A CG  1 
ATOM   112  C  CD  . LYS A 1 16  ? 43.704 21.356 21.841 1.00 38.19  ? 11  LYS A CD  1 
ATOM   113  C  CE  . LYS A 1 16  ? 43.180 21.597 20.449 1.00 36.72  ? 11  LYS A CE  1 
ATOM   114  N  NZ  . LYS A 1 16  ? 44.278 21.583 19.441 1.00 31.58  ? 11  LYS A NZ  1 
ATOM   115  N  N   . LEU A 1 17  ? 43.437 22.435 27.347 1.00 27.07  ? 12  LEU A N   1 
ATOM   116  C  CA  . LEU A 1 17  ? 43.881 22.288 28.726 1.00 26.28  ? 12  LEU A CA  1 
ATOM   117  C  C   . LEU A 1 17  ? 42.705 22.247 29.697 1.00 28.53  ? 12  LEU A C   1 
ATOM   118  O  O   . LEU A 1 17  ? 42.687 21.429 30.627 1.00 27.86  ? 12  LEU A O   1 
ATOM   119  C  CB  . LEU A 1 17  ? 44.821 23.445 29.117 1.00 24.78  ? 12  LEU A CB  1 
ATOM   120  C  CG  . LEU A 1 17  ? 46.142 23.503 28.393 1.00 29.29  ? 12  LEU A CG  1 
ATOM   121  C  CD1 . LEU A 1 17  ? 46.889 24.797 28.753 1.00 31.90  ? 12  LEU A CD1 1 
ATOM   122  C  CD2 . LEU A 1 17  ? 47.002 22.250 28.677 1.00 26.12  ? 12  LEU A CD2 1 
ATOM   123  N  N   . ALA A 1 18  ? 41.735 23.142 29.473 1.00 25.28  ? 13  ALA A N   1 
ATOM   124  C  CA  . ALA A 1 18  ? 40.539 23.207 30.301 1.00 26.67  ? 13  ALA A CA  1 
ATOM   125  C  C   . ALA A 1 18  ? 39.718 21.921 30.198 1.00 30.31  ? 13  ALA A C   1 
ATOM   126  O  O   . ALA A 1 18  ? 39.183 21.434 31.192 1.00 29.92  ? 13  ALA A O   1 
ATOM   127  C  CB  . ALA A 1 18  ? 39.686 24.394 29.889 1.00 28.74  ? 13  ALA A CB  1 
ATOM   128  N  N   . GLU A 1 19  ? 39.624 21.371 28.984 1.00 29.30  ? 14  GLU A N   1 
ATOM   129  C  CA  . GLU A 1 19  ? 38.944 20.102 28.792 1.00 27.99  ? 14  GLU A CA  1 
ATOM   130  C  C   . GLU A 1 19  ? 39.629 19.017 29.625 1.00 32.64  ? 14  GLU A C   1 
ATOM   131  O  O   . GLU A 1 19  ? 38.963 18.247 30.315 1.00 29.80  ? 14  GLU A O   1 
ATOM   132  C  CB  . GLU A 1 19  ? 38.917 19.720 27.323 1.00 32.79  ? 14  GLU A CB  1 
ATOM   133  C  CG  . GLU A 1 19  ? 38.184 18.419 27.043 1.00 35.35  ? 14  GLU A CG  1 
ATOM   134  C  CD  . GLU A 1 19  ? 38.119 18.059 25.565 1.00 32.01  ? 14  GLU A CD  1 
ATOM   135  O  OE1 . GLU A 1 19  ? 39.118 18.312 24.853 1.00 33.37  ? 14  GLU A OE1 1 
ATOM   136  O  OE2 . GLU A 1 19  ? 37.085 17.504 25.127 1.00 37.77  ? 14  GLU A OE2 1 
ATOM   137  N  N   . GLN A 1 20  ? 40.962 18.969 29.567 1.00 26.25  ? 15  GLN A N   1 
ATOM   138  C  CA  . GLN A 1 20  ? 41.727 17.970 30.296 1.00 31.64  ? 15  GLN A CA  1 
ATOM   139  C  C   . GLN A 1 20  ? 41.535 18.100 31.804 1.00 37.45  ? 15  GLN A C   1 
ATOM   140  O  O   . GLN A 1 20  ? 41.429 17.099 32.511 1.00 27.78  ? 15  GLN A O   1 
ATOM   141  C  CB  . GLN A 1 20  ? 43.211 18.055 29.945 1.00 30.63  ? 15  GLN A CB  1 
ATOM   142  C  CG  . GLN A 1 20  ? 43.505 17.716 28.498 1.00 32.31  ? 15  GLN A CG  1 
ATOM   143  C  CD  . GLN A 1 20  ? 44.978 17.769 28.188 1.00 51.77  ? 15  GLN A CD  1 
ATOM   144  O  OE1 . GLN A 1 20  ? 45.712 16.808 28.416 1.00 59.68  ? 15  GLN A OE1 1 
ATOM   145  N  NE2 . GLN A 1 20  ? 45.438 18.888 27.646 1.00 56.18  ? 15  GLN A NE2 1 
ATOM   146  N  N   . ALA A 1 21  ? 41.453 19.341 32.280 1.00 29.05  ? 16  ALA A N   1 
ATOM   147  C  CA  . ALA A 1 21  ? 41.218 19.648 33.681 1.00 30.27  ? 16  ALA A CA  1 
ATOM   148  C  C   . ALA A 1 21  ? 39.754 19.566 34.121 1.00 27.13  ? 16  ALA A C   1 
ATOM   149  O  O   . ALA A 1 21  ? 39.454 19.814 35.297 1.00 27.72  ? 16  ALA A O   1 
ATOM   150  C  CB  . ALA A 1 21  ? 41.756 21.043 33.967 1.00 29.62  ? 16  ALA A CB  1 
ATOM   151  N  N   . GLU A 1 22  ? 38.861 19.248 33.176 1.00 26.12  ? 17  GLU A N   1 
ATOM   152  C  CA  . GLU A 1 22  ? 37.413 19.231 33.371 1.00 30.75  ? 17  GLU A CA  1 
ATOM   153  C  C   . GLU A 1 22  ? 36.909 20.571 33.895 1.00 37.77  ? 17  GLU A C   1 
ATOM   154  O  O   . GLU A 1 22  ? 36.028 20.644 34.750 1.00 29.16  ? 17  GLU A O   1 
ATOM   155  C  CB  . GLU A 1 22  ? 36.977 18.063 34.301 1.00 28.10  ? 17  GLU A CB  1 
ATOM   156  C  CG  . GLU A 1 22  ? 37.470 16.750 33.774 1.00 25.82  ? 17  GLU A CG  1 
ATOM   157  C  CD  . GLU A 1 22  ? 37.115 15.588 34.675 1.00 51.86  ? 17  GLU A CD  1 
ATOM   158  O  OE1 . GLU A 1 22  ? 35.907 15.342 34.886 1.00 46.87  ? 17  GLU A OE1 1 
ATOM   159  O  OE2 . GLU A 1 22  ? 38.051 14.934 35.178 1.00 54.61  ? 17  GLU A OE2 1 
ATOM   160  N  N   . ARG A 1 23  ? 37.479 21.647 33.350 1.00 29.96  ? 18  ARG A N   1 
ATOM   161  C  CA  . ARG A 1 23  ? 37.049 22.991 33.695 1.00 29.24  ? 18  ARG A CA  1 
ATOM   162  C  C   . ARG A 1 23  ? 36.201 23.529 32.546 1.00 34.06  ? 18  ARG A C   1 
ATOM   163  O  O   . ARG A 1 23  ? 36.696 24.287 31.714 1.00 29.87  ? 18  ARG A O   1 
ATOM   164  C  CB  . ARG A 1 23  ? 38.289 23.842 33.935 1.00 27.88  ? 18  ARG A CB  1 
ATOM   165  C  CG  . ARG A 1 23  ? 39.057 23.443 35.180 1.00 37.38  ? 18  ARG A CG  1 
ATOM   166  C  CD  . ARG A 1 23  ? 38.522 24.153 36.395 1.00 29.12  ? 18  ARG A CD  1 
ATOM   167  N  NE  . ARG A 1 23  ? 38.837 25.573 36.314 1.00 34.11  ? 18  ARG A NE  1 
ATOM   168  C  CZ  . ARG A 1 23  ? 38.632 26.450 37.282 1.00 39.86  ? 18  ARG A CZ  1 
ATOM   169  N  NH1 . ARG A 1 23  ? 38.317 26.072 38.511 1.00 28.55  ? 18  ARG A NH1 1 
ATOM   170  N  NH2 . ARG A 1 23  ? 38.780 27.741 37.019 1.00 27.75  ? 18  ARG A NH2 1 
ATOM   171  N  N   . TYR A 1 24  ? 34.932 23.109 32.478 1.00 29.35  ? 19  TYR A N   1 
ATOM   172  C  CA  . TYR A 1 24  ? 34.159 23.278 31.253 1.00 28.71  ? 19  TYR A CA  1 
ATOM   173  C  C   . TYR A 1 24  ? 33.677 24.714 31.056 1.00 26.67  ? 19  TYR A C   1 
ATOM   174  O  O   . TYR A 1 24  ? 33.521 25.159 29.913 1.00 27.09  ? 19  TYR A O   1 
ATOM   175  C  CB  . TYR A 1 24  ? 32.993 22.283 31.183 1.00 29.92  ? 19  TYR A CB  1 
ATOM   176  C  CG  . TYR A 1 24  ? 33.500 20.852 31.104 1.00 28.48  ? 19  TYR A CG  1 
ATOM   177  C  CD1 . TYR A 1 24  ? 34.142 20.382 29.966 1.00 35.71  ? 19  TYR A CD1 1 
ATOM   178  C  CD2 . TYR A 1 24  ? 33.424 20.003 32.206 1.00 39.75  ? 19  TYR A CD2 1 
ATOM   179  C  CE1 . TYR A 1 24  ? 34.655 19.086 29.906 1.00 31.81  ? 19  TYR A CE1 1 
ATOM   180  C  CE2 . TYR A 1 24  ? 33.939 18.706 32.159 1.00 35.59  ? 19  TYR A CE2 1 
ATOM   181  C  CZ  . TYR A 1 24  ? 34.554 18.254 31.010 1.00 46.10  ? 19  TYR A CZ  1 
ATOM   182  O  OH  . TYR A 1 24  ? 35.053 16.983 30.980 1.00 44.44  ? 19  TYR A OH  1 
ATOM   183  N  N   . GLU A 1 25  ? 33.486 25.448 32.161 1.00 25.85  ? 20  GLU A N   1 
ATOM   184  C  CA  . GLU A 1 25  ? 33.157 26.860 32.072 1.00 29.25  ? 20  GLU A CA  1 
ATOM   185  C  C   . GLU A 1 25  ? 34.300 27.657 31.445 1.00 28.07  ? 20  GLU A C   1 
ATOM   186  O  O   . GLU A 1 25  ? 34.076 28.465 30.546 1.00 29.25  ? 20  GLU A O   1 
ATOM   187  C  CB  . GLU A 1 25  ? 32.781 27.454 33.462 1.00 37.28  ? 20  GLU A CB  1 
ATOM   188  C  CG  . GLU A 1 25  ? 31.419 26.983 33.938 1.00 41.35  ? 20  GLU A CG  1 
ATOM   189  C  CD  . GLU A 1 25  ? 30.764 27.797 35.037 1.00 145.71 ? 20  GLU A CD  1 
ATOM   190  O  OE1 . GLU A 1 25  ? 31.451 28.644 35.654 1.00 50.25  ? 20  GLU A OE1 1 
ATOM   191  O  OE2 . GLU A 1 25  ? 29.547 27.599 35.263 1.00 64.01  ? 20  GLU A OE2 1 
ATOM   192  N  N   . ASP A 1 26  ? 35.522 27.422 31.928 1.00 25.49  ? 21  ASP A N   1 
ATOM   193  C  CA  . ASP A 1 26  ? 36.710 28.025 31.346 1.00 24.67  ? 21  ASP A CA  1 
ATOM   194  C  C   . ASP A 1 26  ? 36.815 27.628 29.872 1.00 29.29  ? 21  ASP A C   1 
ATOM   195  O  O   . ASP A 1 26  ? 37.077 28.472 29.012 1.00 26.12  ? 21  ASP A O   1 
ATOM   196  C  CB  . ASP A 1 26  ? 37.972 27.569 32.086 1.00 26.08  ? 21  ASP A CB  1 
ATOM   197  C  CG  . ASP A 1 26  ? 38.129 28.120 33.486 1.00 33.71  ? 21  ASP A CG  1 
ATOM   198  O  OD1 . ASP A 1 26  ? 37.374 29.018 33.840 1.00 28.86  ? 21  ASP A OD1 1 
ATOM   199  O  OD2 . ASP A 1 26  ? 39.001 27.621 34.225 1.00 31.38  ? 21  ASP A OD2 1 
ATOM   200  N  N   . MET A 1 27  ? 36.606 26.334 29.592 1.00 26.84  ? 22  MET A N   1 
ATOM   201  C  CA  . MET A 1 27  ? 36.672 25.820 28.227 1.00 25.17  ? 22  MET A CA  1 
ATOM   202  C  C   . MET A 1 27  ? 35.698 26.556 27.304 1.00 24.60  ? 22  MET A C   1 
ATOM   203  O  O   . MET A 1 27  ? 36.054 26.945 26.191 1.00 26.98  ? 22  MET A O   1 
ATOM   204  C  CB  . MET A 1 27  ? 36.359 24.333 28.240 1.00 27.14  ? 22  MET A CB  1 
ATOM   205  C  CG  . MET A 1 27  ? 36.654 23.644 26.957 1.00 25.73  ? 22  MET A CG  1 
ATOM   206  S  SD  . MET A 1 27  ? 36.067 21.916 26.978 1.00 27.99  ? 22  MET A SD  1 
ATOM   207  C  CE  . MET A 1 27  ? 36.455 21.426 25.302 1.00 28.88  ? 22  MET A CE  1 
ATOM   208  N  N   . ALA A 1 28  ? 34.467 26.758 27.789 1.00 26.58  ? 23  ALA A N   1 
ATOM   209  C  CA  . ALA A 1 28  ? 33.453 27.451 27.019 1.00 24.73  ? 23  ALA A CA  1 
ATOM   210  C  C   . ALA A 1 28  ? 33.869 28.896 26.786 1.00 28.03  ? 23  ALA A C   1 
ATOM   211  O  O   . ALA A 1 28  ? 33.724 29.385 25.672 1.00 25.66  ? 23  ALA A O   1 
ATOM   212  C  CB  . ALA A 1 28  ? 32.098 27.376 27.682 1.00 25.71  ? 23  ALA A CB  1 
ATOM   213  N  N   . ALA A 1 29  ? 34.409 29.558 27.822 1.00 24.38  ? 24  ALA A N   1 
ATOM   214  C  CA  . ALA A 1 29  ? 34.863 30.935 27.669 1.00 26.93  ? 24  ALA A CA  1 
ATOM   215  C  C   . ALA A 1 29  ? 35.992 31.088 26.649 1.00 25.47  ? 24  ALA A C   1 
ATOM   216  O  O   . ALA A 1 29  ? 35.993 32.023 25.849 1.00 21.15  ? 24  ALA A O   1 
ATOM   217  C  CB  . ALA A 1 29  ? 35.291 31.501 29.019 1.00 27.38  ? 24  ALA A CB  1 
ATOM   218  N  N   . PHE A 1 30  ? 36.971 30.180 26.694 1.00 24.66  ? 25  PHE A N   1 
ATOM   219  C  CA  . PHE A 1 30  ? 38.069 30.175 25.743 1.00 24.99  ? 25  PHE A CA  1 
ATOM   220  C  C   . PHE A 1 30  ? 37.585 30.010 24.299 1.00 24.11  ? 25  PHE A C   1 
ATOM   221  O  O   . PHE A 1 30  ? 38.052 30.728 23.420 1.00 23.71  ? 25  PHE A O   1 
ATOM   222  C  CB  . PHE A 1 30  ? 39.097 29.080 26.091 1.00 23.77  ? 25  PHE A CB  1 
ATOM   223  C  CG  . PHE A 1 30  ? 39.886 29.324 27.358 1.00 24.03  ? 25  PHE A CG  1 
ATOM   224  C  CD1 . PHE A 1 30  ? 40.490 30.553 27.599 1.00 24.83  ? 25  PHE A CD1 1 
ATOM   225  C  CD2 . PHE A 1 30  ? 40.060 28.313 28.288 1.00 25.10  ? 25  PHE A CD2 1 
ATOM   226  C  CE1 . PHE A 1 30  ? 41.205 30.771 28.767 1.00 28.11  ? 25  PHE A CE1 1 
ATOM   227  C  CE2 . PHE A 1 30  ? 40.784 28.540 29.453 1.00 25.69  ? 25  PHE A CE2 1 
ATOM   228  C  CZ  . PHE A 1 30  ? 41.361 29.752 29.677 1.00 23.42  ? 25  PHE A CZ  1 
ATOM   229  N  N   . MET A 1 31  ? 36.631 29.098 24.074 1.00 23.01  ? 26  MET A N   1 
ATOM   230  C  CA  . MET A 1 31  ? 36.089 28.860 22.745 1.00 22.08  ? 26  MET A CA  1 
ATOM   231  C  C   . MET A 1 31  ? 35.214 30.010 22.250 1.00 26.39  ? 26  MET A C   1 
ATOM   232  O  O   . MET A 1 31  ? 35.240 30.319 21.066 1.00 25.98  ? 26  MET A O   1 
ATOM   233  C  CB  . MET A 1 31  ? 35.286 27.540 22.679 1.00 27.89  ? 26  MET A CB  1 
ATOM   234  C  CG  . MET A 1 31  ? 36.151 26.303 22.785 1.00 29.59  ? 26  MET A CG  1 
ATOM   235  S  SD  . MET A 1 31  ? 37.581 26.273 21.704 1.00 26.82  ? 26  MET A SD  1 
ATOM   236  C  CE  . MET A 1 31  ? 36.787 26.560 20.058 1.00 30.14  ? 26  MET A CE  1 
ATOM   237  N  N   . LYS A 1 32  ? 34.468 30.652 23.156 1.00 27.00  ? 27  LYS A N   1 
ATOM   238  C  CA  . LYS A 1 32  ? 33.721 31.854 22.825 1.00 24.22  ? 27  LYS A CA  1 
ATOM   239  C  C   . LYS A 1 32  ? 34.695 32.915 22.316 1.00 25.65  ? 27  LYS A C   1 
ATOM   240  O  O   . LYS A 1 32  ? 34.451 33.541 21.287 1.00 26.20  ? 27  LYS A O   1 
ATOM   241  C  CB  . LYS A 1 32  ? 32.913 32.327 24.051 1.00 25.86  ? 27  LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 32  ? 32.100 33.637 23.837 1.00 37.54  ? 27  LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 32  ? 31.244 33.979 25.067 1.00 33.57  ? 27  LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 32  ? 30.301 35.141 24.854 1.00 54.54  ? 27  LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 32  ? 31.027 36.395 24.560 1.00 37.17  ? 27  LYS A NZ  1 
ATOM   246  N  N   . GLY A 1 33  ? 35.826 33.076 23.012 1.00 23.67  ? 28  GLY A N   1 
ATOM   247  C  CA  . GLY A 1 33  ? 36.850 34.017 22.583 1.00 26.93  ? 28  GLY A CA  1 
ATOM   248  C  C   . GLY A 1 33  ? 37.444 33.669 21.217 1.00 26.30  ? 28  GLY A C   1 
ATOM   249  O  O   . GLY A 1 33  ? 37.687 34.555 20.404 1.00 23.96  ? 28  GLY A O   1 
ATOM   250  N  N   . ALA A 1 34  ? 37.699 32.377 20.984 1.00 25.60  ? 29  ALA A N   1 
ATOM   251  C  CA  . ALA A 1 34  ? 38.206 31.942 19.693 1.00 31.94  ? 29  ALA A CA  1 
ATOM   252  C  C   . ALA A 1 34  ? 37.193 32.255 18.595 1.00 25.38  ? 29  ALA A C   1 
ATOM   253  O  O   . ALA A 1 34  ? 37.570 32.760 17.549 1.00 25.21  ? 29  ALA A O   1 
ATOM   254  C  CB  . ALA A 1 34  ? 38.544 30.464 19.696 1.00 24.30  ? 29  ALA A CB  1 
ATOM   255  N  N   . VAL A 1 35  ? 35.907 31.966 18.837 1.00 24.22  ? 30  VAL A N   1 
ATOM   256  C  CA  . VAL A 1 35  ? 34.881 32.240 17.835 1.00 31.21  ? 30  VAL A CA  1 
ATOM   257  C  C   . VAL A 1 35  ? 34.850 33.728 17.495 1.00 28.87  ? 30  VAL A C   1 
ATOM   258  O  O   . VAL A 1 35  ? 34.703 34.106 16.337 1.00 26.67  ? 30  VAL A O   1 
ATOM   259  C  CB  . VAL A 1 35  ? 33.486 31.765 18.307 1.00 25.53  ? 30  VAL A CB  1 
ATOM   260  C  CG1 . VAL A 1 35  ? 32.357 32.330 17.443 1.00 32.40  ? 30  VAL A CG1 1 
ATOM   261  C  CG2 . VAL A 1 35  ? 33.413 30.245 18.401 1.00 26.63  ? 30  VAL A CG2 1 
ATOM   262  N  N   . GLU A 1 36  ? 35.005 34.575 18.519 1.00 24.10  ? 31  GLU A N   1 
ATOM   263  C  CA  . GLU A 1 36  ? 34.902 36.012 18.340 1.00 24.91  ? 31  GLU A CA  1 
ATOM   264  C  C   . GLU A 1 36  ? 36.045 36.629 17.535 1.00 20.85  ? 31  GLU A C   1 
ATOM   265  O  O   . GLU A 1 36  ? 35.975 37.795 17.160 1.00 23.65  ? 31  GLU A O   1 
ATOM   266  C  CB  . GLU A 1 36  ? 34.757 36.683 19.713 1.00 27.33  ? 31  GLU A CB  1 
ATOM   267  C  CG  . GLU A 1 36  ? 33.353 36.558 20.259 1.00 29.34  ? 31  GLU A CG  1 
ATOM   268  C  CD  . GLU A 1 36  ? 33.182 36.926 21.723 1.00 39.09  ? 31  GLU A CD  1 
ATOM   269  O  OE1 . GLU A 1 36  ? 34.196 37.130 22.432 1.00 40.60  ? 31  GLU A OE1 1 
ATOM   270  O  OE2 . GLU A 1 36  ? 32.014 36.995 22.163 1.00 41.30  ? 31  GLU A OE2 1 
ATOM   271  N  N   . LYS A 1 37  ? 37.083 35.839 17.228 1.00 21.30  ? 32  LYS A N   1 
ATOM   272  C  CA  . LYS A 1 37  ? 38.129 36.284 16.323 1.00 26.79  ? 32  LYS A CA  1 
ATOM   273  C  C   . LYS A 1 37  ? 37.593 36.352 14.892 1.00 26.14  ? 32  LYS A C   1 
ATOM   274  O  O   . LYS A 1 37  ? 38.219 36.957 14.030 1.00 25.74  ? 32  LYS A O   1 
ATOM   275  C  CB  . LYS A 1 37  ? 39.354 35.351 16.393 1.00 23.71  ? 32  LYS A CB  1 
ATOM   276  C  CG  . LYS A 1 37  ? 39.975 35.191 17.786 1.00 21.05  ? 32  LYS A CG  1 
ATOM   277  C  CD  . LYS A 1 37  ? 40.444 36.495 18.442 1.00 23.45  ? 32  LYS A CD  1 
ATOM   278  C  CE  . LYS A 1 37  ? 41.097 36.219 19.772 1.00 26.67  ? 32  LYS A CE  1 
ATOM   279  N  NZ  . LYS A 1 37  ? 41.401 37.467 20.512 1.00 29.55  ? 32  LYS A NZ  1 
ATOM   280  N  N   . GLY A 1 38  ? 36.460 35.678 14.647 1.00 26.64  ? 33  GLY A N   1 
ATOM   281  C  CA  . GLY A 1 38  ? 35.726 35.808 13.401 1.00 31.32  ? 33  GLY A CA  1 
ATOM   282  C  C   . GLY A 1 38  ? 36.266 34.945 12.264 1.00 35.34  ? 33  GLY A C   1 
ATOM   283  O  O   . GLY A 1 38  ? 35.938 35.185 11.105 1.00 29.47  ? 33  GLY A O   1 
ATOM   284  N  N   . GLU A 1 39  ? 37.089 33.940 12.592 1.00 34.89  ? 34  GLU A N   1 
ATOM   285  C  CA  . GLU A 1 39  ? 37.516 32.967 11.602 1.00 30.75  ? 34  GLU A CA  1 
ATOM   286  C  C   . GLU A 1 39  ? 36.648 31.724 11.755 1.00 28.01  ? 34  GLU A C   1 
ATOM   287  O  O   . GLU A 1 39  ? 36.124 31.447 12.832 1.00 25.10  ? 34  GLU A O   1 
ATOM   288  C  CB  . GLU A 1 39  ? 38.995 32.572 11.750 1.00 27.91  ? 34  GLU A CB  1 
ATOM   289  C  CG  . GLU A 1 39  ? 39.985 33.726 11.717 1.00 49.92  ? 34  GLU A CG  1 
ATOM   290  C  CD  . GLU A 1 39  ? 41.418 33.256 11.893 1.00 62.84  ? 34  GLU A CD  1 
ATOM   291  O  OE1 . GLU A 1 39  ? 41.673 32.043 11.703 1.00 70.19  ? 34  GLU A OE1 1 
ATOM   292  O  OE2 . GLU A 1 39  ? 42.280 34.087 12.256 1.00 69.45  ? 34  GLU A OE2 1 
ATOM   293  N  N   . GLU A 1 40  ? 36.540 30.945 10.681 1.00 24.10  ? 35  GLU A N   1 
ATOM   294  C  CA  . GLU A 1 40  ? 35.808 29.690 10.751 1.00 23.75  ? 35  GLU A CA  1 
ATOM   295  C  C   . GLU A 1 40  ? 36.493 28.711 11.697 1.00 28.41  ? 35  GLU A C   1 
ATOM   296  O  O   . GLU A 1 40  ? 37.698 28.809 11.921 1.00 29.96  ? 35  GLU A O   1 
ATOM   297  C  CB  . GLU A 1 40  ? 35.683 29.058 9.353  1.00 36.66  ? 35  GLU A CB  1 
ATOM   298  C  CG  . GLU A 1 40  ? 34.731 29.824 8.459  1.00 71.36  ? 35  GLU A CG  1 
ATOM   299  C  CD  . GLU A 1 40  ? 34.640 29.274 7.054  1.00 95.37  ? 35  GLU A CD  1 
ATOM   300  O  OE1 . GLU A 1 40  ? 35.437 28.365 6.731  1.00 45.74  ? 35  GLU A OE1 1 
ATOM   301  O  OE2 . GLU A 1 40  ? 33.772 29.744 6.283  1.00 88.53  ? 35  GLU A OE2 1 
ATOM   302  N  N   . LEU A 1 41  ? 35.695 27.803 12.270 1.00 27.16  ? 36  LEU A N   1 
ATOM   303  C  CA  . LEU A 1 41  ? 36.200 26.756 13.136 1.00 21.87  ? 36  LEU A CA  1 
ATOM   304  C  C   . LEU A 1 41  ? 36.404 25.467 12.339 1.00 31.86  ? 36  LEU A C   1 
ATOM   305  O  O   . LEU A 1 41  ? 35.573 25.109 11.503 1.00 29.46  ? 36  LEU A O   1 
ATOM   306  C  CB  . LEU A 1 41  ? 35.212 26.453 14.285 1.00 28.13  ? 36  LEU A CB  1 
ATOM   307  C  CG  . LEU A 1 41  ? 34.922 27.545 15.293 1.00 39.60  ? 36  LEU A CG  1 
ATOM   308  C  CD1 . LEU A 1 41  ? 34.198 26.968 16.531 1.00 29.77  ? 36  LEU A CD1 1 
ATOM   309  C  CD2 . LEU A 1 41  ? 36.156 28.228 15.709 1.00 43.50  ? 36  LEU A CD2 1 
ATOM   310  N  N   . SER A 1 42  ? 37.509 24.768 12.614 1.00 30.09  ? 37  SER A N   1 
ATOM   311  C  CA  . SER A 1 42  ? 37.698 23.416 12.113 1.00 33.91  ? 37  SER A CA  1 
ATOM   312  C  C   . SER A 1 42  ? 36.760 22.421 12.796 1.00 31.83  ? 37  SER A C   1 
ATOM   313  O  O   . SER A 1 42  ? 36.095 22.738 13.787 1.00 27.82  ? 37  SER A O   1 
ATOM   314  C  CB  . SER A 1 42  ? 39.142 22.967 12.306 1.00 30.80  ? 37  SER A CB  1 
ATOM   315  O  OG  . SER A 1 42  ? 39.473 22.813 13.682 1.00 28.98  ? 37  SER A OG  1 
ATOM   316  N  N   . CYS A 1 43  ? 36.740 21.189 12.278 1.00 27.83  ? 38  CYS A N   1 
ATOM   317  C  CA  . CYS A 1 43  ? 36.060 20.092 12.955 1.00 26.39  ? 38  CYS A CA  1 
ATOM   318  C  C   . CYS A 1 43  ? 36.504 19.944 14.407 1.00 23.06  ? 38  CYS A C   1 
ATOM   319  O  O   . CYS A 1 43  ? 35.667 19.825 15.304 1.00 26.64  ? 38  CYS A O   1 
ATOM   320  C  CB  . CYS A 1 43  ? 36.254 18.786 12.183 1.00 33.69  ? 38  CYS A CB  1 
ATOM   321  S  SG  . CYS A 1 43  ? 35.192 18.642 10.715 1.00 45.94  ? 38  CYS A SG  1 
ATOM   322  N  N   . GLU A 1 44  ? 37.819 19.909 14.635 1.00 33.04  ? 39  GLU A N   1 
ATOM   323  C  CA  . GLU A 1 44  ? 38.336 19.709 15.981 1.00 31.54  ? 39  GLU A CA  1 
ATOM   324  C  C   . GLU A 1 44  ? 37.873 20.852 16.890 1.00 25.50  ? 39  GLU A C   1 
ATOM   325  O  O   . GLU A 1 44  ? 37.537 20.628 18.056 1.00 27.46  ? 39  GLU A O   1 
ATOM   326  C  CB  . GLU A 1 44  ? 39.877 19.600 15.966 1.00 39.19  ? 39  GLU A CB  1 
ATOM   327  C  CG  . GLU A 1 44  ? 40.481 19.272 17.327 1.00 48.07  ? 39  GLU A CG  1 
ATOM   328  C  CD  . GLU A 1 44  ? 41.992 19.113 17.380 1.00 51.29  ? 39  GLU A CD  1 
ATOM   329  O  OE1 . GLU A 1 44  ? 42.659 19.290 16.335 1.00 52.50  ? 39  GLU A OE1 1 
ATOM   330  O  OE2 . GLU A 1 44  ? 42.513 18.814 18.478 1.00 77.73  ? 39  GLU A OE2 1 
ATOM   331  N  N   . GLU A 1 45  ? 37.832 22.078 16.347 1.00 26.51  ? 40  GLU A N   1 
ATOM   332  C  CA  . GLU A 1 45  ? 37.422 23.238 17.133 1.00 26.48  ? 40  GLU A CA  1 
ATOM   333  C  C   . GLU A 1 45  ? 35.917 23.262 17.403 1.00 28.47  ? 40  GLU A C   1 
ATOM   334  O  O   . GLU A 1 45  ? 35.477 23.669 18.482 1.00 25.50  ? 40  GLU A O   1 
ATOM   335  C  CB  . GLU A 1 45  ? 37.864 24.521 16.456 1.00 26.36  ? 40  GLU A CB  1 
ATOM   336  C  CG  . GLU A 1 45  ? 39.378 24.649 16.374 1.00 27.44  ? 40  GLU A CG  1 
ATOM   337  C  CD  . GLU A 1 45  ? 39.919 25.713 15.430 1.00 25.33  ? 40  GLU A CD  1 
ATOM   338  O  OE1 . GLU A 1 45  ? 39.183 26.149 14.513 1.00 27.99  ? 40  GLU A OE1 1 
ATOM   339  O  OE2 . GLU A 1 45  ? 41.104 26.085 15.589 1.00 30.68  ? 40  GLU A OE2 1 
ATOM   340  N  N   . ARG A 1 46  ? 35.118 22.827 16.424 1.00 28.84  ? 41  ARG A N   1 
ATOM   341  C  CA  . ARG A 1 46  ? 33.682 22.695 16.628 1.00 29.33  ? 41  ARG A CA  1 
ATOM   342  C  C   . ARG A 1 46  ? 33.373 21.709 17.745 1.00 25.53  ? 41  ARG A C   1 
ATOM   343  O  O   . ARG A 1 46  ? 32.443 21.915 18.527 1.00 28.30  ? 41  ARG A O   1 
ATOM   344  C  CB  . ARG A 1 46  ? 32.966 22.261 15.333 1.00 29.10  ? 41  ARG A CB  1 
ATOM   345  C  CG  . ARG A 1 46  ? 32.829 23.391 14.368 1.00 27.76  ? 41  ARG A CG  1 
ATOM   346  C  CD  . ARG A 1 46  ? 31.990 23.082 13.155 1.00 35.56  ? 41  ARG A CD  1 
ATOM   347  N  NE  . ARG A 1 46  ? 32.559 22.000 12.378 1.00 33.78  ? 41  ARG A NE  1 
ATOM   348  C  CZ  . ARG A 1 46  ? 33.198 22.153 11.231 1.00 60.48  ? 41  ARG A CZ  1 
ATOM   349  N  NH1 . ARG A 1 46  ? 33.846 23.267 10.946 1.00 47.87  ? 41  ARG A NH1 1 
ATOM   350  N  NH2 . ARG A 1 46  ? 33.224 21.145 10.368 1.00 41.11  ? 41  ARG A NH2 1 
ATOM   351  N  N   . ASN A 1 47  ? 34.154 20.628 17.818 1.00 29.23  ? 42  ASN A N   1 
ATOM   352  C  CA  . ASN A 1 47  ? 33.983 19.655 18.883 1.00 27.92  ? 42  ASN A CA  1 
ATOM   353  C  C   . ASN A 1 47  ? 34.272 20.245 20.260 1.00 28.69  ? 42  ASN A C   1 
ATOM   354  O  O   . ASN A 1 47  ? 33.541 19.970 21.202 1.00 29.32  ? 42  ASN A O   1 
ATOM   355  C  CB  . ASN A 1 47  ? 34.875 18.485 18.675 1.00 32.92  ? 42  ASN A CB  1 
ATOM   356  C  CG  . ASN A 1 47  ? 34.413 17.320 19.465 1.00 34.11  ? 42  ASN A CG  1 
ATOM   357  O  OD1 . ASN A 1 47  ? 33.298 16.826 19.270 1.00 34.69  ? 42  ASN A OD1 1 
ATOM   358  N  ND2 . ASN A 1 47  ? 35.244 16.886 20.387 1.00 36.87  ? 42  ASN A ND2 1 
ATOM   359  N  N   . LEU A 1 48  ? 35.350 21.034 20.354 1.00 26.85  ? 43  LEU A N   1 
ATOM   360  C  CA  . LEU A 1 48  ? 35.701 21.734 21.587 1.00 27.88  ? 43  LEU A CA  1 
ATOM   361  C  C   . LEU A 1 48  ? 34.560 22.640 22.043 1.00 25.70  ? 43  LEU A C   1 
ATOM   362  O  O   . LEU A 1 48  ? 34.178 22.625 23.211 1.00 26.91  ? 43  LEU A O   1 
ATOM   363  C  CB  . LEU A 1 48  ? 36.995 22.573 21.410 1.00 28.07  ? 43  LEU A CB  1 
ATOM   364  C  CG  . LEU A 1 48  ? 38.302 21.787 21.185 1.00 30.21  ? 43  LEU A CG  1 
ATOM   365  C  CD1 . LEU A 1 48  ? 39.444 22.737 20.798 1.00 30.32  ? 43  LEU A CD1 1 
ATOM   366  C  CD2 . LEU A 1 48  ? 38.700 20.931 22.437 1.00 27.86  ? 43  LEU A CD2 1 
ATOM   367  N  N   . LEU A 1 49  ? 34.032 23.441 21.110 1.00 26.96  ? 44  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 49  ? 32.930 24.342 21.392 1.00 26.81  ? 44  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 49  ? 31.717 23.568 21.896 1.00 26.76  ? 44  LEU A C   1 
ATOM   370  O  O   . LEU A 1 49  ? 31.108 23.949 22.894 1.00 28.77  ? 44  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 49  ? 32.558 25.107 20.123 1.00 26.20  ? 44  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 49  ? 31.440 26.117 20.263 1.00 24.64  ? 44  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 49  ? 31.926 27.341 21.049 1.00 26.45  ? 44  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 49  ? 30.892 26.509 18.882 1.00 30.96  ? 44  LEU A CD2 1 
ATOM   375  N  N   . SER A 1 50  ? 31.363 22.507 21.153 1.00 30.53  ? 45  SER A N   1 
ATOM   376  C  CA  . SER A 1 50  ? 30.227 21.658 21.471 1.00 27.06  ? 45  SER A CA  1 
ATOM   377  C  C   . SER A 1 50  ? 30.347 21.047 22.860 1.00 26.35  ? 45  SER A C   1 
ATOM   378  O  O   . SER A 1 50  ? 29.432 21.176 23.667 1.00 27.41  ? 45  SER A O   1 
ATOM   379  C  CB  . SER A 1 50  ? 30.095 20.531 20.449 1.00 26.82  ? 45  SER A CB  1 
ATOM   380  O  OG  . SER A 1 50  ? 28.913 19.788 20.691 1.00 29.28  ? 45  SER A OG  1 
ATOM   381  N  N   . VAL A 1 51  ? 31.484 20.386 23.116 1.00 24.93  ? 46  VAL A N   1 
ATOM   382  C  CA  . VAL A 1 51  ? 31.725 19.709 24.386 1.00 25.72  ? 46  VAL A CA  1 
ATOM   383  C  C   . VAL A 1 51  ? 31.670 20.685 25.566 1.00 31.51  ? 46  VAL A C   1 
ATOM   384  O  O   . VAL A 1 51  ? 31.069 20.384 26.595 1.00 28.36  ? 46  VAL A O   1 
ATOM   385  C  CB  . VAL A 1 51  ? 33.081 18.953 24.356 1.00 28.80  ? 46  VAL A CB  1 
ATOM   386  C  CG1 . VAL A 1 51  ? 33.470 18.466 25.748 1.00 35.17  ? 46  VAL A CG1 1 
ATOM   387  C  CG2 . VAL A 1 51  ? 33.071 17.799 23.362 1.00 28.05  ? 46  VAL A CG2 1 
ATOM   388  N  N   . ALA A 1 52  ? 32.313 21.851 25.413 1.00 25.29  ? 47  ALA A N   1 
ATOM   389  C  CA  . ALA A 1 52  ? 32.378 22.848 26.472 1.00 29.14  ? 47  ALA A CA  1 
ATOM   390  C  C   . ALA A 1 52  ? 30.982 23.288 26.890 1.00 25.64  ? 47  ALA A C   1 
ATOM   391  O  O   . ALA A 1 52  ? 30.602 23.152 28.050 1.00 27.96  ? 47  ALA A O   1 
ATOM   392  C  CB  . ALA A 1 52  ? 33.195 24.044 26.015 1.00 33.85  ? 47  ALA A CB  1 
ATOM   393  N  N   . TYR A 1 53  ? 30.210 23.806 25.930 1.00 27.01  ? 48  TYR A N   1 
ATOM   394  C  CA  . TYR A 1 53  ? 28.899 24.340 26.247 1.00 26.12  ? 48  TYR A CA  1 
ATOM   395  C  C   . TYR A 1 53  ? 27.864 23.281 26.622 1.00 35.91  ? 48  TYR A C   1 
ATOM   396  O  O   . TYR A 1 53  ? 26.985 23.557 27.434 1.00 27.60  ? 48  TYR A O   1 
ATOM   397  C  CB  . TYR A 1 53  ? 28.395 25.234 25.116 1.00 26.26  ? 48  TYR A CB  1 
ATOM   398  C  CG  . TYR A 1 53  ? 28.939 26.644 25.193 1.00 25.05  ? 48  TYR A CG  1 
ATOM   399  C  CD1 . TYR A 1 53  ? 28.546 27.509 26.208 1.00 24.51  ? 48  TYR A CD1 1 
ATOM   400  C  CD2 . TYR A 1 53  ? 29.850 27.113 24.256 1.00 25.77  ? 48  TYR A CD2 1 
ATOM   401  C  CE1 . TYR A 1 53  ? 29.039 28.813 26.283 1.00 30.60  ? 48  TYR A CE1 1 
ATOM   402  C  CE2 . TYR A 1 53  ? 30.337 28.415 24.311 1.00 29.11  ? 48  TYR A CE2 1 
ATOM   403  C  CZ  . TYR A 1 53  ? 29.947 29.254 25.342 1.00 32.84  ? 48  TYR A CZ  1 
ATOM   404  O  OH  . TYR A 1 53  ? 30.440 30.526 25.409 1.00 27.37  ? 48  TYR A OH  1 
ATOM   405  N  N   . LYS A 1 54  ? 27.961 22.077 26.046 1.00 29.25  ? 49  LYS A N   1 
ATOM   406  C  CA  . LYS A 1 54  ? 27.046 21.010 26.439 1.00 29.43  ? 49  LYS A CA  1 
ATOM   407  C  C   . LYS A 1 54  ? 27.243 20.559 27.886 1.00 25.95  ? 49  LYS A C   1 
ATOM   408  O  O   . LYS A 1 54  ? 26.278 20.219 28.567 1.00 30.45  ? 49  LYS A O   1 
ATOM   409  C  CB  . LYS A 1 54  ? 27.156 19.806 25.490 1.00 27.78  ? 49  LYS A CB  1 
ATOM   410  C  CG  . LYS A 1 54  ? 26.154 19.846 24.343 1.00 83.03  ? 49  LYS A CG  1 
ATOM   411  C  CD  . LYS A 1 54  ? 24.806 19.289 24.760 1.00 86.29  ? 49  LYS A CD  1 
ATOM   412  C  CE  . LYS A 1 54  ? 24.821 17.779 24.879 1.00 79.28  ? 49  LYS A CE  1 
ATOM   413  N  NZ  . LYS A 1 54  ? 23.656 17.284 25.657 1.00 51.88  ? 49  LYS A NZ  1 
ATOM   414  N  N   . ASN A 1 55  ? 28.502 20.522 28.331 1.00 30.21  ? 50  ASN A N   1 
ATOM   415  C  CA  . ASN A 1 55  ? 28.827 20.230 29.713 1.00 30.83  ? 50  ASN A CA  1 
ATOM   416  C  C   . ASN A 1 55  ? 28.256 21.295 30.647 1.00 35.95  ? 50  ASN A C   1 
ATOM   417  O  O   . ASN A 1 55  ? 27.663 20.976 31.675 1.00 29.37  ? 50  ASN A O   1 
ATOM   418  C  CB  . ASN A 1 55  ? 30.331 20.122 29.901 1.00 32.60  ? 50  ASN A CB  1 
ATOM   419  C  CG  . ASN A 1 55  ? 30.876 18.735 29.766 1.00 50.18  ? 50  ASN A CG  1 
ATOM   420  O  OD1 . ASN A 1 55  ? 30.735 17.920 30.683 1.00 38.20  ? 50  ASN A OD1 1 
ATOM   421  N  ND2 . ASN A 1 55  ? 31.550 18.457 28.662 1.00 39.97  ? 50  ASN A ND2 1 
ATOM   422  N  N   . VAL A 1 56  ? 28.440 22.566 30.287 1.00 27.29  ? 51  VAL A N   1 
ATOM   423  C  CA  . VAL A 1 56  ? 27.940 23.650 31.106 1.00 27.15  ? 51  VAL A CA  1 
ATOM   424  C  C   . VAL A 1 56  ? 26.421 23.562 31.223 1.00 34.71  ? 51  VAL A C   1 
ATOM   425  O  O   . VAL A 1 56  ? 25.904 23.499 32.337 1.00 29.00  ? 51  VAL A O   1 
ATOM   426  C  CB  . VAL A 1 56  ? 28.397 25.021 30.580 1.00 30.48  ? 51  VAL A CB  1 
ATOM   427  C  CG1 . VAL A 1 56  ? 27.703 26.161 31.326 1.00 31.21  ? 51  VAL A CG1 1 
ATOM   428  C  CG2 . VAL A 1 56  ? 29.911 25.148 30.658 1.00 29.59  ? 51  VAL A CG2 1 
ATOM   429  N  N   . VAL A 1 57  ? 25.725 23.545 30.076 1.00 30.05  ? 52  VAL A N   1 
ATOM   430  C  CA  . VAL A 1 57  ? 24.268 23.569 30.061 1.00 27.17  ? 52  VAL A CA  1 
ATOM   431  C  C   . VAL A 1 57  ? 23.718 22.256 30.625 1.00 28.69  ? 52  VAL A C   1 
ATOM   432  O  O   . VAL A 1 57  ? 22.693 22.259 31.299 1.00 25.29  ? 52  VAL A O   1 
ATOM   433  C  CB  . VAL A 1 57  ? 23.688 23.910 28.653 1.00 33.37  ? 52  VAL A CB  1 
ATOM   434  C  CG1 . VAL A 1 57  ? 23.687 22.700 27.721 1.00 41.26  ? 52  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A 1 57  ? 22.298 24.490 28.758 1.00 32.42  ? 52  VAL A CG2 1 
ATOM   436  N  N   . GLY A 1 58  ? 24.412 21.140 30.365 1.00 27.98  ? 53  GLY A N   1 
ATOM   437  C  CA  . GLY A 1 58  ? 24.013 19.838 30.893 1.00 36.06  ? 53  GLY A CA  1 
ATOM   438  C  C   . GLY A 1 58  ? 23.911 19.819 32.417 1.00 31.73  ? 53  GLY A C   1 
ATOM   439  O  O   . GLY A 1 58  ? 22.958 19.275 32.979 1.00 27.22  ? 53  GLY A O   1 
ATOM   440  N  N   . GLY A 1 59  ? 24.910 20.425 33.078 1.00 29.47  ? 54  GLY A N   1 
ATOM   441  C  CA  . GLY A 1 59  ? 24.921 20.558 34.523 1.00 37.97  ? 54  GLY A CA  1 
ATOM   442  C  C   . GLY A 1 59  ? 23.761 21.419 35.014 1.00 34.51  ? 54  GLY A C   1 
ATOM   443  O  O   . GLY A 1 59  ? 23.150 21.114 36.028 1.00 28.66  ? 54  GLY A O   1 
ATOM   444  N  N   . GLN A 1 60  ? 23.437 22.479 34.262 1.00 28.76  ? 55  GLN A N   1 
ATOM   445  C  CA  . GLN A 1 60  ? 22.341 23.359 34.625 1.00 22.97  ? 55  GLN A CA  1 
ATOM   446  C  C   . GLN A 1 60  ? 20.993 22.670 34.450 1.00 23.81  ? 55  GLN A C   1 
ATOM   447  O  O   . GLN A 1 60  ? 20.119 22.843 35.289 1.00 23.40  ? 55  GLN A O   1 
ATOM   448  C  CB  . GLN A 1 60  ? 22.386 24.648 33.818 1.00 30.20  ? 55  GLN A CB  1 
ATOM   449  C  CG  . GLN A 1 60  ? 23.631 25.458 34.103 1.00 31.02  ? 55  GLN A CG  1 
ATOM   450  C  CD  . GLN A 1 60  ? 23.791 26.574 33.128 1.00 35.79  ? 55  GLN A CD  1 
ATOM   451  O  OE1 . GLN A 1 60  ? 23.535 26.422 31.901 1.00 31.62  ? 55  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A 1 60  ? 24.200 27.724 33.632 1.00 28.13  ? 55  GLN A NE2 1 
ATOM   453  N  N   . ARG A 1 61  ? 20.826 21.928 33.341 1.00 25.88  ? 56  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 61  ? 19.611 21.169 33.092 1.00 25.90  ? 56  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 61  ? 19.366 20.128 34.182 1.00 22.06  ? 56  ARG A C   1 
ATOM   456  O  O   . ARG A 1 61  ? 18.239 19.952 34.635 1.00 24.60  ? 56  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 61  ? 19.677 20.443 31.709 1.00 27.34  ? 56  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 61  ? 19.630 21.401 30.533 1.00 25.32  ? 56  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 61  ? 20.051 20.753 29.222 1.00 27.40  ? 56  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 61  ? 19.041 19.827 28.722 1.00 30.96  ? 56  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 61  ? 19.296 18.724 28.026 1.00 37.63  ? 56  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 61  ? 20.531 18.308 27.803 1.00 31.63  ? 56  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 61  ? 18.282 18.027 27.531 1.00 30.52  ? 56  ARG A NH2 1 
ATOM   464  N  N   . ALA A 1 62  ? 20.420 19.395 34.555 1.00 26.15  ? 57  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 62  ? 20.292 18.369 35.579 1.00 28.57  ? 57  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 62  ? 19.900 18.983 36.928 1.00 25.74  ? 57  ALA A C   1 
ATOM   467  O  O   . ALA A 1 62  ? 19.006 18.477 37.601 1.00 24.60  ? 57  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 62  ? 21.584 17.553 35.691 1.00 34.82  ? 57  ALA A CB  1 
ATOM   469  N  N   . ALA A 1 63  ? 20.516 20.119 37.289 1.00 25.94  ? 58  ALA A N   1 
ATOM   470  C  CA  . ALA A 1 63  ? 20.139 20.839 38.493 1.00 25.60  ? 58  ALA A CA  1 
ATOM   471  C  C   . ALA A 1 63  ? 18.686 21.302 38.414 1.00 24.70  ? 58  ALA A C   1 
ATOM   472  O  O   . ALA A 1 63  ? 17.923 21.139 39.369 1.00 21.55  ? 58  ALA A O   1 
ATOM   473  C  CB  . ALA A 1 63  ? 21.072 22.036 38.742 1.00 25.55  ? 58  ALA A CB  1 
ATOM   474  N  N   . TRP A 1 64  ? 18.313 21.892 37.268 1.00 25.20  ? 59  TRP A N   1 
ATOM   475  C  CA  . TRP A 1 64  ? 16.963 22.395 37.075 1.00 18.41  ? 59  TRP A CA  1 
ATOM   476  C  C   . TRP A 1 64  ? 15.924 21.286 37.238 1.00 25.86  ? 59  TRP A C   1 
ATOM   477  O  O   . TRP A 1 64  ? 14.918 21.486 37.914 1.00 21.96  ? 59  TRP A O   1 
ATOM   478  C  CB  . TRP A 1 64  ? 16.840 23.093 35.704 1.00 21.10  ? 59  TRP A CB  1 
ATOM   479  C  CG  . TRP A 1 64  ? 15.521 23.746 35.475 1.00 25.57  ? 59  TRP A CG  1 
ATOM   480  C  CD1 . TRP A 1 64  ? 15.216 25.061 35.673 1.00 28.92  ? 59  TRP A CD1 1 
ATOM   481  C  CD2 . TRP A 1 64  ? 14.332 23.129 34.971 1.00 29.13  ? 59  TRP A CD2 1 
ATOM   482  N  NE1 . TRP A 1 64  ? 13.906 25.295 35.351 1.00 26.90  ? 59  TRP A NE1 1 
ATOM   483  C  CE2 . TRP A 1 64  ? 13.337 24.127 34.911 1.00 29.21  ? 59  TRP A CE2 1 
ATOM   484  C  CE3 . TRP A 1 64  ? 14.008 21.827 34.564 1.00 27.40  ? 59  TRP A CE3 1 
ATOM   485  C  CZ2 . TRP A 1 64  ? 12.041 23.863 34.475 1.00 26.73  ? 59  TRP A CZ2 1 
ATOM   486  C  CZ3 . TRP A 1 64  ? 12.724 21.564 34.133 1.00 33.30  ? 59  TRP A CZ3 1 
ATOM   487  C  CH2 . TRP A 1 64  ? 11.756 22.575 34.087 1.00 49.21  ? 59  TRP A CH2 1 
ATOM   488  N  N   . ARG A 1 65  ? 16.183 20.111 36.641 1.00 26.51  ? 60  ARG A N   1 
ATOM   489  C  CA  . ARG A 1 65  ? 15.291 18.969 36.789 1.00 25.48  ? 60  ARG A CA  1 
ATOM   490  C  C   . ARG A 1 65  ? 15.117 18.533 38.243 1.00 19.64  ? 60  ARG A C   1 
ATOM   491  O  O   . ARG A 1 65  ? 14.014 18.184 38.662 1.00 24.33  ? 60  ARG A O   1 
ATOM   492  C  CB  . ARG A 1 65  ? 15.804 17.789 35.957 1.00 21.74  ? 60  ARG A CB  1 
ATOM   493  C  CG  . ARG A 1 65  ? 15.622 18.018 34.461 1.00 27.77  ? 60  ARG A CG  1 
ATOM   494  C  CD  . ARG A 1 65  ? 16.007 16.781 33.684 1.00 41.94  ? 60  ARG A CD  1 
ATOM   495  N  NE  . ARG A 1 65  ? 16.159 17.074 32.266 1.00 64.18  ? 60  ARG A NE  1 
ATOM   496  C  CZ  . ARG A 1 65  ? 17.280 16.903 31.580 1.00 97.53  ? 60  ARG A CZ  1 
ATOM   497  N  NH1 . ARG A 1 65  ? 18.418 16.583 32.178 1.00 56.24  ? 60  ARG A NH1 1 
ATOM   498  N  NH2 . ARG A 1 65  ? 17.259 17.059 30.259 1.00 58.13  ? 60  ARG A NH2 1 
ATOM   499  N  N   . VAL A 1 66  ? 16.211 18.558 39.016 1.00 27.09  ? 61  VAL A N   1 
ATOM   500  C  CA  . VAL A 1 66  ? 16.155 18.185 40.425 1.00 31.55  ? 61  VAL A CA  1 
ATOM   501  C  C   . VAL A 1 66  ? 15.249 19.143 41.197 1.00 29.27  ? 61  VAL A C   1 
ATOM   502  O  O   . VAL A 1 66  ? 14.400 18.719 41.970 1.00 22.31  ? 61  VAL A O   1 
ATOM   503  C  CB  . VAL A 1 66  ? 17.568 18.130 41.072 1.00 19.52  ? 61  VAL A CB  1 
ATOM   504  C  CG1 . VAL A 1 66  ? 17.477 18.157 42.589 1.00 27.36  ? 61  VAL A CG1 1 
ATOM   505  C  CG2 . VAL A 1 66  ? 18.356 16.910 40.593 1.00 41.17  ? 61  VAL A CG2 1 
ATOM   506  N  N   . LEU A 1 67  ? 15.444 20.445 40.974 1.00 22.05  ? 62  LEU A N   1 
ATOM   507  C  CA  . LEU A 1 67  ? 14.718 21.474 41.698 1.00 19.32  ? 62  LEU A CA  1 
ATOM   508  C  C   . LEU A 1 67  ? 13.252 21.479 41.276 1.00 21.02  ? 62  LEU A C   1 
ATOM   509  O  O   . LEU A 1 67  ? 12.362 21.606 42.116 1.00 21.58  ? 62  LEU A O   1 
ATOM   510  C  CB  . LEU A 1 67  ? 15.396 22.833 41.438 1.00 21.50  ? 62  LEU A CB  1 
ATOM   511  C  CG  . LEU A 1 67  ? 16.816 22.945 41.976 1.00 22.65  ? 62  LEU A CG  1 
ATOM   512  C  CD1 . LEU A 1 67  ? 17.455 24.271 41.597 1.00 29.23  ? 62  LEU A CD1 1 
ATOM   513  C  CD2 . LEU A 1 67  ? 16.846 22.761 43.477 1.00 23.51  ? 62  LEU A CD2 1 
ATOM   514  N  N   . SER A 1 68  ? 13.017 21.331 39.964 1.00 27.67  ? 63  SER A N   1 
ATOM   515  C  CA  . SER A 1 68  ? 11.667 21.278 39.421 1.00 26.54  ? 63  SER A CA  1 
ATOM   516  C  C   . SER A 1 68  ? 10.860 20.112 39.995 1.00 35.67  ? 63  SER A C   1 
ATOM   517  O  O   . SER A 1 68  ? 9.670  20.244 40.279 1.00 25.53  ? 63  SER A O   1 
ATOM   518  C  CB  . SER A 1 68  ? 11.714 21.175 37.897 1.00 27.63  ? 63  SER A CB  1 
ATOM   519  O  OG  . SER A 1 68  ? 10.412 21.268 37.360 1.00 39.50  ? 63  SER A OG  1 
ATOM   520  N  N   . SER A 1 69  ? 11.518 18.962 40.160 1.00 25.00  ? 64  SER A N   1 
ATOM   521  C  CA  . SER A 1 69  ? 10.867 17.800 40.743 1.00 41.44  ? 64  SER A CA  1 
ATOM   522  C  C   . SER A 1 69  ? 10.514 18.022 42.211 1.00 31.15  ? 64  SER A C   1 
ATOM   523  O  O   . SER A 1 69  ? 9.424  17.650 42.640 1.00 29.89  ? 64  SER A O   1 
ATOM   524  C  CB  . SER A 1 69  ? 11.726 16.552 40.594 1.00 42.01  ? 64  SER A CB  1 
ATOM   525  O  OG  . SER A 1 69  ? 11.089 15.456 41.229 1.00 49.47  ? 64  SER A OG  1 
ATOM   526  N  N   . ILE A 1 70  ? 11.436 18.628 42.975 1.00 29.78  ? 65  ILE A N   1 
ATOM   527  C  CA  . ILE A 1 70  ? 11.177 18.975 44.363 1.00 33.65  ? 65  ILE A CA  1 
ATOM   528  C  C   . ILE A 1 70  ? 10.005 19.951 44.437 1.00 39.43  ? 65  ILE A C   1 
ATOM   529  O  O   . ILE A 1 70  ? 9.142  19.828 45.304 1.00 27.50  ? 65  ILE A O   1 
ATOM   530  C  CB  . ILE A 1 70  ? 12.438 19.564 45.056 1.00 25.74  ? 65  ILE A CB  1 
ATOM   531  C  CG1 . ILE A 1 70  ? 13.576 18.514 45.128 1.00 29.29  ? 65  ILE A CG1 1 
ATOM   532  C  CG2 . ILE A 1 70  ? 12.081 20.145 46.450 1.00 26.10  ? 65  ILE A CG2 1 
ATOM   533  C  CD1 . ILE A 1 70  ? 14.881 19.040 45.647 1.00 25.52  ? 65  ILE A CD1 1 
ATOM   534  N  N   . GLU A 1 71  ? 9.987  20.913 43.507 1.00 28.86  ? 66  GLU A N   1 
ATOM   535  C  CA  . GLU A 1 71  ? 8.974  21.956 43.472 1.00 32.07  ? 66  GLU A CA  1 
ATOM   536  C  C   . GLU A 1 71  ? 7.590  21.366 43.207 1.00 32.69  ? 66  GLU A C   1 
ATOM   537  O  O   . GLU A 1 71  ? 6.639  21.670 43.924 1.00 34.26  ? 66  GLU A O   1 
ATOM   538  C  CB  . GLU A 1 71  ? 9.334  22.984 42.396 1.00 26.31  ? 66  GLU A CB  1 
ATOM   539  C  CG  . GLU A 1 71  ? 8.487  24.241 42.404 1.00 31.65  ? 66  GLU A CG  1 
ATOM   540  C  CD  . GLU A 1 71  ? 8.858  25.213 41.303 1.00 26.33  ? 66  GLU A CD  1 
ATOM   541  O  OE1 . GLU A 1 71  ? 9.759  24.891 40.498 1.00 24.88  ? 66  GLU A OE1 1 
ATOM   542  O  OE2 . GLU A 1 71  ? 8.248  26.301 41.241 1.00 28.65  ? 66  GLU A OE2 1 
ATOM   543  N  N   . GLN A 1 72  ? 7.499  20.518 42.176 1.00 37.23  ? 67  GLN A N   1 
ATOM   544  C  CA  . GLN A 1 72  ? 6.258  19.850 41.813 1.00 30.50  ? 67  GLN A CA  1 
ATOM   545  C  C   . GLN A 1 72  ? 5.731  18.979 42.957 1.00 38.02  ? 67  GLN A C   1 
ATOM   546  O  O   . GLN A 1 72  ? 4.528  18.971 43.212 1.00 41.89  ? 67  GLN A O   1 
ATOM   547  C  CB  . GLN A 1 72  ? 6.480  19.053 40.504 1.00 43.66  ? 67  GLN A CB  1 
ATOM   548  C  CG  . GLN A 1 72  ? 5.382  18.048 40.127 1.00 94.88  ? 67  GLN A CG  1 
ATOM   549  C  CD  . GLN A 1 72  ? 5.689  16.643 40.609 1.00 117.73 ? 67  GLN A CD  1 
ATOM   550  O  OE1 . GLN A 1 72  ? 6.782  16.105 40.386 1.00 88.65  ? 67  GLN A OE1 1 
ATOM   551  N  NE2 . GLN A 1 72  ? 4.737  16.009 41.276 1.00 54.98  ? 67  GLN A NE2 1 
ATOM   552  N  N   . LYS A 1 73  ? 6.632  18.272 43.661 1.00 38.39  ? 68  LYS A N   1 
ATOM   553  C  CA  . LYS A 1 73  ? 6.251  17.454 44.807 1.00 50.51  ? 68  LYS A CA  1 
ATOM   554  C  C   . LYS A 1 73  ? 5.686  18.272 45.965 1.00 45.49  ? 68  LYS A C   1 
ATOM   555  O  O   . LYS A 1 73  ? 4.783  17.810 46.660 1.00 38.68  ? 68  LYS A O   1 
ATOM   556  C  CB  . LYS A 1 73  ? 7.438  16.629 45.343 1.00 47.70  ? 68  LYS A CB  1 
ATOM   557  C  CG  . LYS A 1 73  ? 7.782  15.404 44.508 1.00 96.74  ? 68  LYS A CG  1 
ATOM   558  C  CD  . LYS A 1 73  ? 8.984  14.647 45.061 1.00 83.73  ? 68  LYS A CD  1 
ATOM   559  C  CE  . LYS A 1 73  ? 9.542  13.637 44.083 1.00 92.73  ? 68  LYS A CE  1 
ATOM   560  N  NZ  . LYS A 1 73  ? 8.575  12.552 43.791 1.00 99.16  ? 68  LYS A NZ  1 
ATOM   561  N  N   . SER A 1 74  ? 6.225  19.481 46.173 1.00 49.56  ? 69  SER A N   1 
ATOM   562  C  CA  . SER A 1 74  ? 5.769  20.343 47.255 1.00 36.92  ? 69  SER A CA  1 
ATOM   563  C  C   . SER A 1 74  ? 4.523  21.153 46.893 1.00 65.30  ? 69  SER A C   1 
ATOM   564  O  O   . SER A 1 74  ? 4.112  22.017 47.664 1.00 66.60  ? 69  SER A O   1 
ATOM   565  C  CB  . SER A 1 74  ? 6.888  21.279 47.707 1.00 43.32  ? 69  SER A CB  1 
ATOM   566  O  OG  . SER A 1 74  ? 7.218  22.225 46.703 1.00 47.44  ? 69  SER A OG  1 
ATOM   567  N  N   . ASN A 1 75  ? 3.933  20.868 45.722 1.00 66.98  ? 70  ASN A N   1 
ATOM   568  C  CA  . ASN A 1 75  ? 2.664  21.453 45.312 1.00 107.49 ? 70  ASN A CA  1 
ATOM   569  C  C   . ASN A 1 75  ? 1.596  20.370 45.151 1.00 68.98  ? 70  ASN A C   1 
ATOM   570  O  O   . ASN A 1 75  ? 0.869  20.355 44.160 1.00 49.11  ? 70  ASN A O   1 
ATOM   571  C  CB  . ASN A 1 75  ? 2.846  22.255 44.003 1.00 49.45  ? 70  ASN A CB  1 
ATOM   572  C  CG  . ASN A 1 75  ? 3.754  23.464 44.140 1.00 72.81  ? 70  ASN A CG  1 
ATOM   573  O  OD1 . ASN A 1 75  ? 4.316  23.960 43.164 1.00 42.24  ? 70  ASN A OD1 1 
ATOM   574  N  ND2 . ASN A 1 75  ? 3.945  23.958 45.352 1.00 54.68  ? 70  ASN A ND2 1 
ATOM   575  N  N   . GLU A 1 76  ? 1.508  19.477 46.147 1.00 122.01 ? 71  GLU A N   1 
ATOM   576  C  CA  . GLU A 1 76  ? 0.581  18.355 46.132 1.00 106.76 ? 71  GLU A CA  1 
ATOM   577  C  C   . GLU A 1 76  ? -0.213 18.297 47.430 1.00 59.42  ? 71  GLU A C   1 
ATOM   578  O  O   . GLU A 1 76  ? 0.381  18.373 48.501 1.00 47.40  ? 71  GLU A O   1 
ATOM   579  C  CB  . GLU A 1 76  ? 1.341  17.034 45.935 1.00 79.24  ? 71  GLU A CB  1 
ATOM   580  C  CG  . GLU A 1 76  ? 1.938  16.877 44.548 1.00 57.09  ? 71  GLU A CG  1 
ATOM   581  C  CD  . GLU A 1 76  ? 2.772  15.625 44.338 1.00 96.88  ? 71  GLU A CD  1 
ATOM   582  O  OE1 . GLU A 1 76  ? 3.080  14.932 45.334 1.00 54.97  ? 71  GLU A OE1 1 
ATOM   583  O  OE2 . GLU A 1 76  ? 3.111  15.331 43.168 1.00 54.88  ? 71  GLU A OE2 1 
ATOM   584  N  N   . GLY A 1 83  ? 6.398  27.678 51.472 1.00 40.08  ? 78  GLY A N   1 
ATOM   585  C  CA  . GLY A 1 83  ? 7.505  28.625 51.432 1.00 47.43  ? 78  GLY A CA  1 
ATOM   586  C  C   . GLY A 1 83  ? 8.017  28.878 50.014 1.00 34.76  ? 78  GLY A C   1 
ATOM   587  O  O   . GLY A 1 83  ? 7.981  27.985 49.163 1.00 25.51  ? 78  GLY A O   1 
ATOM   588  N  N   . PRO A 1 84  ? 8.526  30.096 49.703 1.00 19.94  ? 79  PRO A N   1 
ATOM   589  C  CA  . PRO A 1 84  ? 8.941  30.419 48.334 1.00 20.57  ? 79  PRO A CA  1 
ATOM   590  C  C   . PRO A 1 84  ? 10.312 29.899 47.896 1.00 21.24  ? 79  PRO A C   1 
ATOM   591  O  O   . PRO A 1 84  ? 10.660 30.028 46.729 1.00 20.96  ? 79  PRO A O   1 
ATOM   592  C  CB  . PRO A 1 84  ? 8.936  31.950 48.354 1.00 21.75  ? 79  PRO A CB  1 
ATOM   593  C  CG  . PRO A 1 84  ? 9.366  32.285 49.743 1.00 24.82  ? 79  PRO A CG  1 
ATOM   594  C  CD  . PRO A 1 84  ? 8.718  31.222 50.633 1.00 24.85  ? 79  PRO A CD  1 
ATOM   595  N  N   . GLU A 1 85  ? 11.089 29.302 48.815 1.00 23.39  ? 80  GLU A N   1 
ATOM   596  C  CA  . GLU A 1 85  ? 12.502 29.031 48.561 1.00 17.83  ? 80  GLU A CA  1 
ATOM   597  C  C   . GLU A 1 85  ? 12.804 28.064 47.416 1.00 20.78  ? 80  GLU A C   1 
ATOM   598  O  O   . GLU A 1 85  ? 13.742 28.299 46.651 1.00 21.50  ? 80  GLU A O   1 
ATOM   599  C  CB  . GLU A 1 85  ? 13.221 28.539 49.850 1.00 20.40  ? 80  GLU A CB  1 
ATOM   600  C  CG  . GLU A 1 85  ? 13.275 29.561 50.976 1.00 29.26  ? 80  GLU A CG  1 
ATOM   601  C  CD  . GLU A 1 85  ? 12.063 29.599 51.890 1.00 21.77  ? 80  GLU A CD  1 
ATOM   602  O  OE1 . GLU A 1 85  ? 11.092 28.849 51.634 1.00 30.23  ? 80  GLU A OE1 1 
ATOM   603  O  OE2 . GLU A 1 85  ? 12.087 30.372 52.871 1.00 23.02  ? 80  GLU A OE2 1 
ATOM   604  N  N   . VAL A 1 86  ? 12.032 26.975 47.277 1.00 20.39  ? 81  VAL A N   1 
ATOM   605  C  CA  . VAL A 1 86  ? 12.254 26.059 46.162 1.00 22.02  ? 81  VAL A CA  1 
ATOM   606  C  C   . VAL A 1 86  ? 12.046 26.736 44.800 1.00 19.57  ? 81  VAL A C   1 
ATOM   607  O  O   . VAL A 1 86  ? 12.875 26.586 43.901 1.00 18.31  ? 81  VAL A O   1 
ATOM   608  C  CB  . VAL A 1 86  ? 11.379 24.775 46.256 1.00 25.78  ? 81  VAL A CB  1 
ATOM   609  C  CG1 . VAL A 1 86  ? 11.688 23.835 45.089 1.00 31.25  ? 81  VAL A CG1 1 
ATOM   610  C  CG2 . VAL A 1 86  ? 11.561 24.065 47.595 1.00 47.55  ? 81  VAL A CG2 1 
ATOM   611  N  N   . ARG A 1 87  ? 10.929 27.460 44.647 1.00 19.17  ? 82  ARG A N   1 
ATOM   612  C  CA  . ARG A 1 87  ? 10.645 28.198 43.421 1.00 17.00  ? 82  ARG A CA  1 
ATOM   613  C  C   . ARG A 1 87  ? 11.739 29.227 43.136 1.00 17.12  ? 82  ARG A C   1 
ATOM   614  O  O   . ARG A 1 87  ? 12.213 29.333 42.007 1.00 21.97  ? 82  ARG A O   1 
ATOM   615  C  CB  . ARG A 1 87  ? 9.269  28.896 43.504 1.00 22.86  ? 82  ARG A CB  1 
ATOM   616  C  CG  . ARG A 1 87  ? 8.964  29.785 42.286 1.00 26.90  ? 82  ARG A CG  1 
ATOM   617  C  CD  . ARG A 1 87  ? 7.638  30.517 42.376 1.00 35.50  ? 82  ARG A CD  1 
ATOM   618  N  NE  . ARG A 1 87  ? 7.496  31.286 43.610 1.00 36.60  ? 82  ARG A NE  1 
ATOM   619  C  CZ  . ARG A 1 87  ? 8.177  32.388 43.912 1.00 35.48  ? 82  ARG A CZ  1 
ATOM   620  N  NH1 . ARG A 1 87  ? 9.051  32.922 43.073 1.00 31.26  ? 82  ARG A NH1 1 
ATOM   621  N  NH2 . ARG A 1 87  ? 7.977  32.967 45.091 1.00 32.28  ? 82  ARG A NH2 1 
ATOM   622  N  N   . GLU A 1 88  ? 12.137 29.987 44.169 1.00 21.27  ? 83  GLU A N   1 
ATOM   623  C  CA  . GLU A 1 88  ? 13.149 31.022 44.004 1.00 22.06  ? 83  GLU A CA  1 
ATOM   624  C  C   . GLU A 1 88  ? 14.455 30.431 43.491 1.00 19.90  ? 83  GLU A C   1 
ATOM   625  O  O   . GLU A 1 88  ? 15.080 30.974 42.595 1.00 20.81  ? 83  GLU A O   1 
ATOM   626  C  CB  . GLU A 1 88  ? 13.414 31.778 45.325 1.00 23.77  ? 83  GLU A CB  1 
ATOM   627  C  CG  . GLU A 1 88  ? 12.267 32.665 45.830 1.00 31.11  ? 83  GLU A CG  1 
ATOM   628  C  CD  . GLU A 1 88  ? 12.458 33.248 47.225 1.00 22.77  ? 83  GLU A CD  1 
ATOM   629  O  OE1 . GLU A 1 88  ? 13.366 32.778 47.950 1.00 25.12  ? 83  GLU A OE1 1 
ATOM   630  O  OE2 . GLU A 1 88  ? 11.724 34.195 47.594 1.00 19.75  ? 83  GLU A OE2 1 
ATOM   631  N  N   . TYR A 1 89  ? 14.888 29.304 44.066 1.00 24.59  ? 84  TYR A N   1 
ATOM   632  C  CA  . TYR A 1 89  ? 16.164 28.746 43.665 1.00 24.68  ? 84  TYR A CA  1 
ATOM   633  C  C   . TYR A 1 89  ? 16.069 28.129 42.263 1.00 19.87  ? 84  TYR A C   1 
ATOM   634  O  O   . TYR A 1 89  ? 16.970 28.289 41.434 1.00 22.04  ? 84  TYR A O   1 
ATOM   635  C  CB  . TYR A 1 89  ? 16.670 27.770 44.749 1.00 22.36  ? 84  TYR A CB  1 
ATOM   636  C  CG  . TYR A 1 89  ? 18.045 27.251 44.443 1.00 22.46  ? 84  TYR A CG  1 
ATOM   637  C  CD1 . TYR A 1 89  ? 19.051 28.104 44.011 1.00 28.65  ? 84  TYR A CD1 1 
ATOM   638  C  CD2 . TYR A 1 89  ? 18.349 25.905 44.587 1.00 27.65  ? 84  TYR A CD2 1 
ATOM   639  C  CE1 . TYR A 1 89  ? 20.311 27.627 43.690 1.00 25.90  ? 84  TYR A CE1 1 
ATOM   640  C  CE2 . TYR A 1 89  ? 19.611 25.418 44.286 1.00 27.97  ? 84  TYR A CE2 1 
ATOM   641  C  CZ  . TYR A 1 89  ? 20.592 26.282 43.836 1.00 26.27  ? 84  TYR A CZ  1 
ATOM   642  O  OH  . TYR A 1 89  ? 21.833 25.804 43.521 1.00 29.59  ? 84  TYR A OH  1 
ATOM   643  N  N   . ARG A 1 90  ? 14.941 27.471 41.971 1.00 21.02  ? 85  ARG A N   1 
ATOM   644  C  CA  . ARG A 1 90  ? 14.682 26.964 40.630 1.00 21.11  ? 85  ARG A CA  1 
ATOM   645  C  C   . ARG A 1 90  ? 14.744 28.074 39.582 1.00 22.82  ? 85  ARG A C   1 
ATOM   646  O  O   . ARG A 1 90  ? 15.379 27.904 38.545 1.00 23.28  ? 85  ARG A O   1 
ATOM   647  C  CB  . ARG A 1 90  ? 13.331 26.233 40.589 1.00 22.51  ? 85  ARG A CB  1 
ATOM   648  C  CG  . ARG A 1 90  ? 13.099 25.440 39.300 1.00 23.09  ? 85  ARG A CG  1 
ATOM   649  C  CD  . ARG A 1 90  ? 12.347 26.241 38.251 1.00 31.28  ? 85  ARG A CD  1 
ATOM   650  N  NE  . ARG A 1 90  ? 11.006 26.574 38.714 1.00 25.68  ? 85  ARG A NE  1 
ATOM   651  C  CZ  . ARG A 1 90  ? 10.374 27.713 38.463 1.00 28.34  ? 85  ARG A CZ  1 
ATOM   652  N  NH1 . ARG A 1 90  ? 10.773 28.534 37.501 1.00 30.08  ? 85  ARG A NH1 1 
ATOM   653  N  NH2 . ARG A 1 90  ? 9.283  28.013 39.162 1.00 27.53  ? 85  ARG A NH2 1 
ATOM   654  N  N   . GLU A 1 91  ? 14.100 29.216 39.864 1.00 23.50  ? 86  GLU A N   1 
ATOM   655  C  CA  . GLU A 1 91  ? 14.148 30.374 38.978 1.00 20.63  ? 86  GLU A CA  1 
ATOM   656  C  C   . GLU A 1 91  ? 15.564 30.912 38.772 1.00 20.45  ? 86  GLU A C   1 
ATOM   657  O  O   . GLU A 1 91  ? 15.906 31.322 37.660 1.00 25.38  ? 86  GLU A O   1 
ATOM   658  C  CB  . GLU A 1 91  ? 13.254 31.516 39.506 1.00 23.31  ? 86  GLU A CB  1 
ATOM   659  C  CG  . GLU A 1 91  ? 11.769 31.288 39.297 1.00 31.39  ? 86  GLU A CG  1 
ATOM   660  C  CD  . GLU A 1 91  ? 10.905 32.323 39.991 1.00 47.74  ? 86  GLU A CD  1 
ATOM   661  O  OE1 . GLU A 1 91  ? 11.460 33.340 40.465 1.00 51.47  ? 86  GLU A OE1 1 
ATOM   662  O  OE2 . GLU A 1 91  ? 9.678  32.104 40.088 1.00 26.92  ? 86  GLU A OE2 1 
ATOM   663  N  N   . LYS A 1 92  ? 16.385 30.885 39.838 1.00 24.40  ? 87  LYS A N   1 
ATOM   664  C  CA  . LYS A 1 92  ? 17.777 31.309 39.750 1.00 27.77  ? 87  LYS A CA  1 
ATOM   665  C  C   . LYS A 1 92  ? 18.599 30.431 38.808 1.00 26.64  ? 87  LYS A C   1 
ATOM   666  O  O   . LYS A 1 92  ? 19.344 30.937 37.967 1.00 25.38  ? 87  LYS A O   1 
ATOM   667  C  CB  . LYS A 1 92  ? 18.444 31.323 41.140 1.00 30.73  ? 87  LYS A CB  1 
ATOM   668  C  CG  . LYS A 1 92  ? 19.951 31.627 41.114 1.00 51.13  ? 87  LYS A CG  1 
ATOM   669  C  CD  . LYS A 1 92  ? 20.614 31.501 42.488 1.00 64.69  ? 87  LYS A CD  1 
ATOM   670  C  CE  . LYS A 1 92  ? 22.091 31.804 42.448 1.00 70.47  ? 87  LYS A CE  1 
ATOM   671  N  NZ  . LYS A 1 92  ? 22.648 31.967 43.815 1.00 71.13  ? 87  LYS A NZ  1 
ATOM   672  N  N   . VAL A 1 93  ? 18.460 29.109 38.962 1.00 25.81  ? 88  VAL A N   1 
ATOM   673  C  CA  . VAL A 1 93  ? 19.139 28.164 38.090 1.00 22.18  ? 88  VAL A CA  1 
ATOM   674  C  C   . VAL A 1 93  ? 18.611 28.314 36.658 1.00 23.00  ? 88  VAL A C   1 
ATOM   675  O  O   . VAL A 1 93  ? 19.384 28.311 35.709 1.00 25.18  ? 88  VAL A O   1 
ATOM   676  C  CB  . VAL A 1 93  ? 19.000 26.712 38.612 1.00 26.13  ? 88  VAL A CB  1 
ATOM   677  C  CG1 . VAL A 1 93  ? 19.567 25.688 37.619 1.00 27.93  ? 88  VAL A CG1 1 
ATOM   678  C  CG2 . VAL A 1 93  ? 19.657 26.559 39.981 1.00 26.62  ? 88  VAL A CG2 1 
ATOM   679  N  N   . GLU A 1 94  ? 17.291 28.462 36.518 1.00 25.77  ? 89  GLU A N   1 
ATOM   680  C  CA  . GLU A 1 94  ? 16.649 28.638 35.223 1.00 22.67  ? 89  GLU A CA  1 
ATOM   681  C  C   . GLU A 1 94  ? 17.177 29.856 34.467 1.00 26.81  ? 89  GLU A C   1 
ATOM   682  O  O   . GLU A 1 94  ? 17.484 29.773 33.277 1.00 25.45  ? 89  GLU A O   1 
ATOM   683  C  CB  . GLU A 1 94  ? 15.140 28.739 35.439 1.00 25.79  ? 89  GLU A CB  1 
ATOM   684  C  CG  . GLU A 1 94  ? 14.283 28.827 34.186 1.00 24.67  ? 89  GLU A CG  1 
ATOM   685  C  CD  . GLU A 1 94  ? 12.804 28.694 34.483 1.00 31.86  ? 89  GLU A CD  1 
ATOM   686  O  OE1 . GLU A 1 94  ? 12.422 27.708 35.157 1.00 27.85  ? 89  GLU A OE1 1 
ATOM   687  O  OE2 . GLU A 1 94  ? 12.024 29.578 34.062 1.00 31.38  ? 89  GLU A OE2 1 
ATOM   688  N  N   . THR A 1 95  ? 17.296 30.983 35.173 1.00 25.49  ? 90  THR A N   1 
ATOM   689  C  CA  . THR A 1 95  ? 17.809 32.211 34.590 1.00 28.24  ? 90  THR A CA  1 
ATOM   690  C  C   . THR A 1 95  ? 19.232 32.051 34.065 1.00 27.33  ? 90  THR A C   1 
ATOM   691  O  O   . THR A 1 95  ? 19.547 32.550 32.983 1.00 25.25  ? 90  THR A O   1 
ATOM   692  C  CB  . THR A 1 95  ? 17.699 33.356 35.604 1.00 33.02  ? 90  THR A CB  1 
ATOM   693  O  OG1 . THR A 1 95  ? 16.328 33.475 35.960 1.00 32.00  ? 90  THR A OG1 1 
ATOM   694  C  CG2 . THR A 1 95  ? 18.216 34.676 35.047 1.00 39.70  ? 90  THR A CG2 1 
ATOM   695  N  N   . GLU A 1 96  ? 20.077 31.356 34.841 1.00 26.82  ? 91  GLU A N   1 
ATOM   696  C  CA  . GLU A 1 96  ? 21.447 31.075 34.444 1.00 29.14  ? 91  GLU A CA  1 
ATOM   697  C  C   . GLU A 1 96  ? 21.513 30.178 33.211 1.00 24.36  ? 91  GLU A C   1 
ATOM   698  O  O   . GLU A 1 96  ? 22.356 30.395 32.345 1.00 24.82  ? 91  GLU A O   1 
ATOM   699  C  CB  . GLU A 1 96  ? 22.246 30.416 35.595 1.00 28.81  ? 91  GLU A CB  1 
ATOM   700  C  CG  . GLU A 1 96  ? 22.681 31.451 36.623 1.00 62.89  ? 91  GLU A CG  1 
ATOM   701  C  CD  . GLU A 1 96  ? 23.329 30.918 37.885 1.00 65.45  ? 91  GLU A CD  1 
ATOM   702  O  OE1 . GLU A 1 96  ? 24.079 29.920 37.792 1.00 33.09  ? 91  GLU A OE1 1 
ATOM   703  O  OE2 . GLU A 1 96  ? 23.124 31.528 38.962 1.00 50.84  ? 91  GLU A OE2 1 
ATOM   704  N  N   . LEU A 1 97  ? 20.656 29.150 33.180 1.00 24.65  ? 92  LEU A N   1 
ATOM   705  C  CA  . LEU A 1 97  ? 20.563 28.239 32.046 1.00 28.80  ? 92  LEU A CA  1 
ATOM   706  C  C   . LEU A 1 97  ? 20.184 29.008 30.785 1.00 32.61  ? 92  LEU A C   1 
ATOM   707  O  O   . LEU A 1 97  ? 20.826 28.858 29.749 1.00 28.30  ? 92  LEU A O   1 
ATOM   708  C  CB  . LEU A 1 97  ? 19.533 27.147 32.368 1.00 27.68  ? 92  LEU A CB  1 
ATOM   709  C  CG  . LEU A 1 97  ? 19.332 26.031 31.353 1.00 27.70  ? 92  LEU A CG  1 
ATOM   710  C  CD1 . LEU A 1 97  ? 18.729 24.799 32.037 1.00 37.49  ? 92  LEU A CD1 1 
ATOM   711  C  CD2 . LEU A 1 97  ? 18.434 26.445 30.217 1.00 37.84  ? 92  LEU A CD2 1 
ATOM   712  N  N   . GLN A 1 98  ? 19.172 29.876 30.904 1.00 27.64  ? 93  GLN A N   1 
ATOM   713  C  CA  . GLN A 1 98  ? 18.720 30.687 29.786 1.00 27.97  ? 93  GLN A CA  1 
ATOM   714  C  C   . GLN A 1 98  ? 19.824 31.622 29.289 1.00 34.86  ? 93  GLN A C   1 
ATOM   715  O  O   . GLN A 1 98  ? 19.977 31.807 28.085 1.00 27.71  ? 93  GLN A O   1 
ATOM   716  C  CB  . GLN A 1 98  ? 17.458 31.466 30.181 1.00 30.36  ? 93  GLN A CB  1 
ATOM   717  C  CG  . GLN A 1 98  ? 16.222 30.578 30.403 1.00 23.91  ? 93  GLN A CG  1 
ATOM   718  C  CD  . GLN A 1 98  ? 15.070 31.331 31.035 1.00 29.65  ? 93  GLN A CD  1 
ATOM   719  O  OE1 . GLN A 1 98  ? 15.255 32.204 31.897 1.00 27.68  ? 93  GLN A OE1 1 
ATOM   720  N  NE2 . GLN A 1 98  ? 13.859 31.014 30.631 1.00 22.10  ? 93  GLN A NE2 1 
ATOM   721  N  N   . GLY A 1 99  ? 20.602 32.192 30.220 1.00 30.84  ? 94  GLY A N   1 
ATOM   722  C  CA  . GLY A 1 99  ? 21.749 33.017 29.872 1.00 29.67  ? 94  GLY A CA  1 
ATOM   723  C  C   . GLY A 1 99  ? 22.800 32.283 29.038 1.00 27.51  ? 94  GLY A C   1 
ATOM   724  O  O   . GLY A 1 99  ? 23.356 32.845 28.089 1.00 28.05  ? 94  GLY A O   1 
ATOM   725  N  N   . VAL A 1 100 ? 23.069 31.020 29.402 1.00 27.51  ? 95  VAL A N   1 
ATOM   726  C  CA  . VAL A 1 100 ? 24.020 30.210 28.664 1.00 28.55  ? 95  VAL A CA  1 
ATOM   727  C  C   . VAL A 1 100 ? 23.468 29.904 27.268 1.00 25.15  ? 95  VAL A C   1 
ATOM   728  O  O   . VAL A 1 100 ? 24.192 30.059 26.289 1.00 29.57  ? 95  VAL A O   1 
ATOM   729  C  CB  . VAL A 1 100 ? 24.442 28.943 29.456 1.00 27.56  ? 95  VAL A CB  1 
ATOM   730  C  CG1 . VAL A 1 100 ? 25.263 27.986 28.576 1.00 34.88  ? 95  VAL A CG1 1 
ATOM   731  C  CG2 . VAL A 1 100 ? 25.207 29.328 30.718 1.00 35.17  ? 95  VAL A CG2 1 
ATOM   732  N  N   . CYS A 1 101 ? 22.184 29.519 27.168 1.00 27.39  ? 96  CYS A N   1 
ATOM   733  C  CA  . CYS A 1 101 ? 21.566 29.248 25.874 1.00 30.76  ? 96  CYS A CA  1 
ATOM   734  C  C   . CYS A 1 101 ? 21.569 30.485 24.976 1.00 31.44  ? 96  CYS A C   1 
ATOM   735  O  O   . CYS A 1 101 ? 21.824 30.377 23.778 1.00 30.54  ? 96  CYS A O   1 
ATOM   736  C  CB  . CYS A 1 101 ? 20.149 28.696 26.013 1.00 27.39  ? 96  CYS A CB  1 
ATOM   737  S  SG  . CYS A 1 101 ? 20.047 27.077 26.817 1.00 27.10  ? 96  CYS A SG  1 
ATOM   738  N  N   . ASP A 1 102 ? 21.261 31.652 25.555 1.00 29.82  ? 97  ASP A N   1 
ATOM   739  C  CA  . ASP A 1 102 ? 21.282 32.905 24.814 1.00 32.84  ? 97  ASP A CA  1 
ATOM   740  C  C   . ASP A 1 102 ? 22.677 33.253 24.299 1.00 27.89  ? 97  ASP A C   1 
ATOM   741  O  O   . ASP A 1 102 ? 22.816 33.769 23.191 1.00 29.08  ? 97  ASP A O   1 
ATOM   742  C  CB  . ASP A 1 102 ? 20.724 34.045 25.685 1.00 45.89  ? 97  ASP A CB  1 
ATOM   743  C  CG  . ASP A 1 102 ? 19.225 33.960 25.909 1.00 56.67  ? 97  ASP A CG  1 
ATOM   744  O  OD1 . ASP A 1 102 ? 18.559 33.168 25.201 1.00 41.74  ? 97  ASP A OD1 1 
ATOM   745  O  OD2 . ASP A 1 102 ? 18.721 34.668 26.794 1.00 39.19  ? 97  ASP A OD2 1 
ATOM   746  N  N   . THR A 1 103 ? 23.701 32.958 25.104 1.00 29.40  ? 98  THR A N   1 
ATOM   747  C  CA  . THR A 1 103 ? 25.089 33.150 24.712 1.00 35.79  ? 98  THR A CA  1 
ATOM   748  C  C   . THR A 1 103 ? 25.456 32.300 23.499 1.00 31.87  ? 98  THR A C   1 
ATOM   749  O  O   . THR A 1 103 ? 26.081 32.797 22.568 1.00 28.18  ? 98  THR A O   1 
ATOM   750  C  CB  . THR A 1 103 ? 26.008 32.853 25.894 1.00 40.86  ? 98  THR A CB  1 
ATOM   751  O  OG1 . THR A 1 103 ? 25.707 33.801 26.920 1.00 33.61  ? 98  THR A OG1 1 
ATOM   752  C  CG2 . THR A 1 103 ? 27.489 32.905 25.526 1.00 31.24  ? 98  THR A CG2 1 
ATOM   753  N  N   . VAL A 1 104 ? 25.064 31.020 23.531 1.00 28.21  ? 99  VAL A N   1 
ATOM   754  C  CA  . VAL A 1 104 ? 25.356 30.099 22.447 1.00 25.81  ? 99  VAL A CA  1 
ATOM   755  C  C   . VAL A 1 104 ? 24.602 30.514 21.190 1.00 24.70  ? 99  VAL A C   1 
ATOM   756  O  O   . VAL A 1 104 ? 25.188 30.572 20.109 1.00 27.54  ? 99  VAL A O   1 
ATOM   757  C  CB  . VAL A 1 104 ? 25.047 28.626 22.836 1.00 26.38  ? 99  VAL A CB  1 
ATOM   758  C  CG1 . VAL A 1 104 ? 25.138 27.702 21.615 1.00 31.56  ? 99  VAL A CG1 1 
ATOM   759  C  CG2 . VAL A 1 104 ? 25.968 28.173 23.949 1.00 28.45  ? 99  VAL A CG2 1 
ATOM   760  N  N   . LEU A 1 105 ? 23.311 30.835 21.340 1.00 24.23  ? 100 LEU A N   1 
ATOM   761  C  CA  . LEU A 1 105 ? 22.501 31.220 20.193 1.00 30.05  ? 100 LEU A CA  1 
ATOM   762  C  C   . LEU A 1 105 ? 23.005 32.530 19.588 1.00 38.88  ? 100 LEU A C   1 
ATOM   763  O  O   . LEU A 1 105 ? 22.957 32.717 18.374 1.00 26.72  ? 100 LEU A O   1 
ATOM   764  C  CB  . LEU A 1 105 ? 21.026 31.312 20.615 1.00 29.01  ? 100 LEU A CB  1 
ATOM   765  C  CG  . LEU A 1 105 ? 20.380 29.954 20.920 1.00 32.02  ? 100 LEU A CG  1 
ATOM   766  C  CD1 . LEU A 1 105 ? 19.027 30.115 21.577 1.00 32.11  ? 100 LEU A CD1 1 
ATOM   767  C  CD2 . LEU A 1 105 ? 20.257 29.134 19.663 1.00 26.42  ? 100 LEU A CD2 1 
ATOM   768  N  N   . GLY A 1 106 ? 23.514 33.428 20.440 1.00 28.96  ? 101 GLY A N   1 
ATOM   769  C  CA  . GLY A 1 106 ? 24.134 34.656 19.973 1.00 31.41  ? 101 GLY A CA  1 
ATOM   770  C  C   . GLY A 1 106 ? 25.398 34.437 19.143 1.00 28.77  ? 101 GLY A C   1 
ATOM   771  O  O   . GLY A 1 106 ? 25.587 35.102 18.129 1.00 30.54  ? 101 GLY A O   1 
ATOM   772  N  N   . LEU A 1 107 ? 26.263 33.518 19.595 1.00 28.06  ? 102 LEU A N   1 
ATOM   773  C  CA  . LEU A 1 107 ? 27.472 33.164 18.867 1.00 31.99  ? 102 LEU A CA  1 
ATOM   774  C  C   . LEU A 1 107 ? 27.128 32.560 17.510 1.00 29.71  ? 102 LEU A C   1 
ATOM   775  O  O   . LEU A 1 107 ? 27.790 32.845 16.517 1.00 28.93  ? 102 LEU A O   1 
ATOM   776  C  CB  . LEU A 1 107 ? 28.329 32.136 19.644 1.00 30.70  ? 102 LEU A CB  1 
ATOM   777  C  CG  . LEU A 1 107 ? 29.107 32.641 20.854 1.00 42.00  ? 102 LEU A CG  1 
ATOM   778  C  CD1 . LEU A 1 107 ? 29.739 31.467 21.636 1.00 33.37  ? 102 LEU A CD1 1 
ATOM   779  C  CD2 . LEU A 1 107 ? 30.184 33.667 20.428 1.00 35.80  ? 102 LEU A CD2 1 
ATOM   780  N  N   . LEU A 1 108 ? 26.122 31.680 17.497 1.00 27.66  ? 103 LEU A N   1 
ATOM   781  C  CA  . LEU A 1 108 ? 25.697 31.017 16.276 1.00 24.11  ? 103 LEU A CA  1 
ATOM   782  C  C   . LEU A 1 108 ? 25.208 32.059 15.276 1.00 32.28  ? 103 LEU A C   1 
ATOM   783  O  O   . LEU A 1 108 ? 25.635 32.068 14.127 1.00 24.62  ? 103 LEU A O   1 
ATOM   784  C  CB  . LEU A 1 108 ? 24.605 29.990 16.585 1.00 28.66  ? 103 LEU A CB  1 
ATOM   785  C  CG  . LEU A 1 108 ? 25.090 28.700 17.255 1.00 23.86  ? 103 LEU A CG  1 
ATOM   786  C  CD1 . LEU A 1 108 ? 23.939 27.919 17.808 1.00 26.23  ? 103 LEU A CD1 1 
ATOM   787  C  CD2 . LEU A 1 108 ? 25.858 27.863 16.269 1.00 28.48  ? 103 LEU A CD2 1 
ATOM   788  N  N   . ASP A 1 109 ? 24.347 32.965 15.746 1.00 25.20  ? 104 ASP A N   1 
ATOM   789  C  CA  . ASP A 1 109 ? 23.783 34.005 14.900 1.00 24.10  ? 104 ASP A CA  1 
ATOM   790  C  C   . ASP A 1 109 ? 24.758 35.104 14.476 1.00 33.53  ? 104 ASP A C   1 
ATOM   791  O  O   . ASP A 1 109 ? 24.723 35.558 13.335 1.00 28.60  ? 104 ASP A O   1 
ATOM   792  C  CB  . ASP A 1 109 ? 22.538 34.609 15.571 1.00 30.49  ? 104 ASP A CB  1 
ATOM   793  C  CG  . ASP A 1 109 ? 21.280 34.187 14.848 1.00 99.38  ? 104 ASP A CG  1 
ATOM   794  O  OD1 . ASP A 1 109 ? 21.061 32.947 14.697 1.00 36.71  ? 104 ASP A OD1 1 
ATOM   795  O  OD2 . ASP A 1 109 ? 20.541 35.083 14.381 1.00 53.76  ? 104 ASP A OD2 1 
ATOM   796  N  N   . SER A 1 110 ? 25.640 35.517 15.386 1.00 28.06  ? 105 SER A N   1 
ATOM   797  C  CA  . SER A 1 110 ? 26.573 36.592 15.099 1.00 40.03  ? 105 SER A CA  1 
ATOM   798  C  C   . SER A 1 110 ? 27.776 36.125 14.283 1.00 33.60  ? 105 SER A C   1 
ATOM   799  O  O   . SER A 1 110 ? 28.264 36.873 13.445 1.00 28.31  ? 105 SER A O   1 
ATOM   800  C  CB  . SER A 1 110 ? 27.025 37.255 16.397 1.00 44.16  ? 105 SER A CB  1 
ATOM   801  O  OG  . SER A 1 110 ? 25.924 37.892 17.029 1.00 43.18  ? 105 SER A OG  1 
ATOM   802  N  N   . HIS A 1 111 ? 28.233 34.881 14.491 1.00 28.39  ? 106 HIS A N   1 
ATOM   803  C  CA  . HIS A 1 111 ? 29.552 34.484 14.015 1.00 27.66  ? 106 HIS A CA  1 
ATOM   804  C  C   . HIS A 1 111 ? 29.542 33.214 13.160 1.00 26.35  ? 106 HIS A C   1 
ATOM   805  O  O   . HIS A 1 111 ? 30.276 33.142 12.179 1.00 33.21  ? 106 HIS A O   1 
ATOM   806  C  CB  . HIS A 1 111 ? 30.509 34.342 15.207 1.00 27.18  ? 106 HIS A CB  1 
ATOM   807  C  CG  . HIS A 1 111 ? 30.857 35.661 15.827 1.00 32.76  ? 106 HIS A CG  1 
ATOM   808  N  ND1 . HIS A 1 111 ? 31.782 36.521 15.269 1.00 42.75  ? 106 HIS A ND1 1 
ATOM   809  C  CD2 . HIS A 1 111 ? 30.413 36.263 16.937 1.00 40.56  ? 106 HIS A CD2 1 
ATOM   810  C  CE1 . HIS A 1 111 ? 31.887 37.606 16.031 1.00 30.77  ? 106 HIS A CE1 1 
ATOM   811  N  NE2 . HIS A 1 111 ? 31.059 37.472 17.045 1.00 46.23  ? 106 HIS A NE2 1 
ATOM   812  N  N   . LEU A 1 112 ? 28.774 32.191 13.543 1.00 25.84  ? 107 LEU A N   1 
ATOM   813  C  CA  . LEU A 1 112 ? 29.060 30.839 13.069 1.00 29.44  ? 107 LEU A CA  1 
ATOM   814  C  C   . LEU A 1 112 ? 28.207 30.349 11.900 1.00 31.56  ? 107 LEU A C   1 
ATOM   815  O  O   . LEU A 1 112 ? 28.727 29.683 11.008 1.00 30.94  ? 107 LEU A O   1 
ATOM   816  C  CB  . LEU A 1 112 ? 28.903 29.851 14.224 1.00 25.46  ? 107 LEU A CB  1 
ATOM   817  C  CG  . LEU A 1 112 ? 29.901 30.023 15.382 1.00 28.68  ? 107 LEU A CG  1 
ATOM   818  C  CD1 . LEU A 1 112 ? 29.481 29.227 16.573 1.00 32.77  ? 107 LEU A CD1 1 
ATOM   819  C  CD2 . LEU A 1 112 ? 31.310 29.635 14.972 1.00 30.20  ? 107 LEU A CD2 1 
ATOM   820  N  N   . ILE A 1 113 ? 26.899 30.631 11.945 1.00 32.82  ? 108 ILE A N   1 
ATOM   821  C  CA  . ILE A 1 113 ? 25.976 30.229 10.896 1.00 29.31  ? 108 ILE A CA  1 
ATOM   822  C  C   . ILE A 1 113 ? 26.189 31.146 9.692  1.00 42.34  ? 108 ILE A C   1 
ATOM   823  O  O   . ILE A 1 113 ? 26.079 32.366 9.809  1.00 29.38  ? 108 ILE A O   1 
ATOM   824  C  CB  . ILE A 1 113 ? 24.496 30.244 11.372 1.00 31.03  ? 108 ILE A CB  1 
ATOM   825  C  CG1 . ILE A 1 113 ? 24.225 29.147 12.400 1.00 30.69  ? 108 ILE A CG1 1 
ATOM   826  C  CG2 . ILE A 1 113 ? 23.513 30.116 10.192 1.00 45.25  ? 108 ILE A CG2 1 
ATOM   827  C  CD1 . ILE A 1 113 ? 22.891 29.339 13.217 1.00 35.53  ? 108 ILE A CD1 1 
ATOM   828  N  N   . LYS A 1 114 ? 26.501 30.544 8.538  1.00 29.85  ? 109 LYS A N   1 
ATOM   829  C  CA  . LYS A 1 114 ? 26.671 31.293 7.300  1.00 44.90  ? 109 LYS A CA  1 
ATOM   830  C  C   . LYS A 1 114 ? 25.940 30.590 6.158  1.00 94.71  ? 109 LYS A C   1 
ATOM   831  O  O   . LYS A 1 114 ? 25.487 29.455 6.312  1.00 44.13  ? 109 LYS A O   1 
ATOM   832  C  CB  . LYS A 1 114 ? 28.166 31.432 6.937  1.00 69.12  ? 109 LYS A CB  1 
ATOM   833  C  CG  . LYS A 1 114 ? 29.058 32.064 8.003  1.00 50.24  ? 109 LYS A CG  1 
ATOM   834  C  CD  . LYS A 1 114 ? 30.533 32.035 7.585  1.00 91.54  ? 109 LYS A CD  1 
ATOM   835  C  CE  . LYS A 1 114 ? 31.473 32.510 8.668  1.00 87.19  ? 109 LYS A CE  1 
ATOM   836  N  NZ  . LYS A 1 114 ? 31.234 33.931 9.025  1.00 70.53  ? 109 LYS A NZ  1 
ATOM   837  N  N   . GLU A 1 115 ? 25.840 31.285 5.016  1.00 54.82  ? 110 GLU A N   1 
ATOM   838  C  CA  . GLU A 1 115 ? 25.381 30.692 3.768  1.00 139.05 ? 110 GLU A CA  1 
ATOM   839  C  C   . GLU A 1 115 ? 26.441 29.774 3.155  1.00 33.62  ? 110 GLU A C   1 
ATOM   840  O  O   . GLU A 1 115 ? 26.100 28.748 2.567  1.00 61.32  ? 110 GLU A O   1 
ATOM   841  C  CB  . GLU A 1 115 ? 24.990 31.795 2.760  1.00 57.88  ? 110 GLU A CB  1 
ATOM   842  C  CG  . GLU A 1 115 ? 23.642 32.440 3.046  1.00 114.71 ? 110 GLU A CG  1 
ATOM   843  C  CD  . GLU A 1 115 ? 22.423 31.641 2.617  1.00 120.16 ? 110 GLU A CD  1 
ATOM   844  O  OE1 . GLU A 1 115 ? 22.568 30.712 1.789  1.00 85.62  ? 110 GLU A OE1 1 
ATOM   845  O  OE2 . GLU A 1 115 ? 21.317 31.942 3.120  1.00 103.28 ? 110 GLU A OE2 1 
ATOM   846  N  N   . ALA A 1 116 ? 27.721 30.155 3.305  1.00 58.25  ? 111 ALA A N   1 
ATOM   847  C  CA  . ALA A 1 116 ? 28.841 29.418 2.736  1.00 68.40  ? 111 ALA A CA  1 
ATOM   848  C  C   . ALA A 1 116 ? 29.423 28.368 3.687  1.00 116.39 ? 111 ALA A C   1 
ATOM   849  O  O   . ALA A 1 116 ? 28.919 28.159 4.791  1.00 43.27  ? 111 ALA A O   1 
ATOM   850  C  CB  . ALA A 1 116 ? 29.930 30.401 2.310  1.00 62.88  ? 111 ALA A CB  1 
ATOM   851  N  N   . GLY A 1 117 ? 30.487 27.695 3.229  1.00 77.16  ? 112 GLY A N   1 
ATOM   852  C  CA  . GLY A 1 117 ? 31.204 26.713 4.025  1.00 66.14  ? 112 GLY A CA  1 
ATOM   853  C  C   . GLY A 1 117 ? 30.757 25.281 3.749  1.00 46.78  ? 112 GLY A C   1 
ATOM   854  O  O   . GLY A 1 117 ? 29.822 25.057 2.978  1.00 47.93  ? 112 GLY A O   1 
ATOM   855  N  N   . ASP A 1 118 ? 31.477 24.328 4.356  1.00 45.49  ? 113 ASP A N   1 
ATOM   856  C  CA  . ASP A 1 118 ? 31.070 22.932 4.449  1.00 63.01  ? 113 ASP A CA  1 
ATOM   857  C  C   . ASP A 1 118 ? 29.566 22.734 4.631  1.00 59.63  ? 113 ASP A C   1 
ATOM   858  O  O   . ASP A 1 118 ? 28.919 23.473 5.374  1.00 32.92  ? 113 ASP A O   1 
ATOM   859  C  CB  . ASP A 1 118 ? 31.734 22.246 5.683  1.00 47.48  ? 113 ASP A CB  1 
ATOM   860  C  CG  . ASP A 1 118 ? 33.214 21.960 5.624  1.00 65.07  ? 113 ASP A CG  1 
ATOM   861  O  OD1 . ASP A 1 118 ? 33.651 21.300 4.660  1.00 86.03  ? 113 ASP A OD1 1 
ATOM   862  O  OD2 . ASP A 1 118 ? 33.931 22.363 6.565  1.00 88.29  ? 113 ASP A OD2 1 
ATOM   863  N  N   . ALA A 1 119 ? 29.030 21.687 3.998  1.00 50.85  ? 114 ALA A N   1 
ATOM   864  C  CA  . ALA A 1 119 ? 27.736 21.147 4.380  1.00 61.88  ? 114 ALA A CA  1 
ATOM   865  C  C   . ALA A 1 119 ? 27.764 20.722 5.846  1.00 48.15  ? 114 ALA A C   1 
ATOM   866  O  O   . ALA A 1 119 ? 26.823 20.997 6.593  1.00 41.84  ? 114 ALA A O   1 
ATOM   867  C  CB  . ALA A 1 119 ? 27.370 19.964 3.499  1.00 80.28  ? 114 ALA A CB  1 
ATOM   868  N  N   . GLU A 1 120 ? 28.847 20.030 6.235  1.00 32.33  ? 115 GLU A N   1 
ATOM   869  C  CA  . GLU A 1 120 ? 29.034 19.579 7.604  1.00 47.92  ? 115 GLU A CA  1 
ATOM   870  C  C   . GLU A 1 120 ? 28.879 20.731 8.584  1.00 31.25  ? 115 GLU A C   1 
ATOM   871  O  O   . GLU A 1 120 ? 28.151 20.617 9.569  1.00 37.83  ? 115 GLU A O   1 
ATOM   872  C  CB  . GLU A 1 120 ? 30.423 18.953 7.823  1.00 42.01  ? 115 GLU A CB  1 
ATOM   873  C  CG  . GLU A 1 120 ? 30.557 17.534 7.312  1.00 83.72  ? 115 GLU A CG  1 
ATOM   874  C  CD  . GLU A 1 120 ? 31.680 16.752 7.956  1.00 56.13  ? 115 GLU A CD  1 
ATOM   875  O  OE1 . GLU A 1 120 ? 32.813 17.282 8.035  1.00 51.91  ? 115 GLU A OE1 1 
ATOM   876  O  OE2 . GLU A 1 120 ? 31.427 15.595 8.363  1.00 41.80  ? 115 GLU A OE2 1 
ATOM   877  N  N   . SER A 1 121 ? 29.617 21.815 8.323  1.00 33.10  ? 116 SER A N   1 
ATOM   878  C  CA  . SER A 1 121 ? 29.666 22.934 9.246  1.00 29.11  ? 116 SER A CA  1 
ATOM   879  C  C   . SER A 1 121 ? 28.276 23.556 9.343  1.00 23.44  ? 116 SER A C   1 
ATOM   880  O  O   . SER A 1 121 ? 27.793 23.806 10.440 1.00 33.52  ? 116 SER A O   1 
ATOM   881  C  CB  . SER A 1 121 ? 30.728 23.962 8.835  1.00 32.27  ? 116 SER A CB  1 
ATOM   882  O  OG  . SER A 1 121 ? 30.338 24.725 7.710  1.00 37.01  ? 116 SER A OG  1 
ATOM   883  N  N   . ARG A 1 122 ? 27.623 23.785 8.189  1.00 30.73  ? 117 ARG A N   1 
ATOM   884  C  CA  . ARG A 1 122 ? 26.305 24.411 8.187  1.00 26.81  ? 117 ARG A CA  1 
ATOM   885  C  C   . ARG A 1 122 ? 25.268 23.563 8.924  1.00 30.88  ? 117 ARG A C   1 
ATOM   886  O  O   . ARG A 1 122 ? 24.513 24.078 9.747  1.00 25.04  ? 117 ARG A O   1 
ATOM   887  C  CB  . ARG A 1 122 ? 25.845 24.711 6.748  1.00 35.44  ? 117 ARG A CB  1 
ATOM   888  C  CG  . ARG A 1 122 ? 26.541 25.929 6.157  1.00 54.83  ? 117 ARG A CG  1 
ATOM   889  C  CD  . ARG A 1 122 ? 25.995 26.311 4.797  1.00 49.51  ? 117 ARG A CD  1 
ATOM   890  N  NE  . ARG A 1 122 ? 26.243 25.269 3.808  1.00 56.38  ? 117 ARG A NE  1 
ATOM   891  C  CZ  . ARG A 1 122 ? 25.298 24.596 3.167  1.00 69.35  ? 117 ARG A CZ  1 
ATOM   892  N  NH1 . ARG A 1 122 ? 24.063 25.065 3.059  1.00 57.61  ? 117 ARG A NH1 1 
ATOM   893  N  NH2 . ARG A 1 122 ? 25.603 23.429 2.610  1.00 38.60  ? 117 ARG A NH2 1 
ATOM   894  N  N   . VAL A 1 123 ? 25.267 22.249 8.667  1.00 30.54  ? 118 VAL A N   1 
ATOM   895  C  CA  . VAL A 1 123 ? 24.397 21.325 9.388  1.00 27.97  ? 118 VAL A CA  1 
ATOM   896  C  C   . VAL A 1 123 ? 24.707 21.341 10.887 1.00 24.34  ? 118 VAL A C   1 
ATOM   897  O  O   . VAL A 1 123 ? 23.804 21.382 11.721 1.00 25.09  ? 118 VAL A O   1 
ATOM   898  C  CB  . VAL A 1 123 ? 24.481 19.875 8.809  1.00 26.00  ? 118 VAL A CB  1 
ATOM   899  C  CG1 . VAL A 1 123 ? 23.656 18.891 9.642  1.00 29.56  ? 118 VAL A CG1 1 
ATOM   900  C  CG2 . VAL A 1 123 ? 24.055 19.835 7.340  1.00 29.64  ? 118 VAL A CG2 1 
ATOM   901  N  N   . PHE A 1 124 ? 25.992 21.297 11.235 1.00 23.53  ? 119 PHE A N   1 
ATOM   902  C  CA  . PHE A 1 124 ? 26.364 21.219 12.635 1.00 30.00  ? 119 PHE A CA  1 
ATOM   903  C  C   . PHE A 1 124 ? 25.863 22.436 13.410 1.00 33.79  ? 119 PHE A C   1 
ATOM   904  O  O   . PHE A 1 124 ? 25.337 22.286 14.512 1.00 27.67  ? 119 PHE A O   1 
ATOM   905  C  CB  . PHE A 1 124 ? 27.873 21.074 12.826 1.00 28.13  ? 119 PHE A CB  1 
ATOM   906  C  CG  . PHE A 1 124 ? 28.224 21.271 14.269 1.00 31.24  ? 119 PHE A CG  1 
ATOM   907  C  CD1 . PHE A 1 124 ? 27.921 20.297 15.215 1.00 30.71  ? 119 PHE A CD1 1 
ATOM   908  C  CD2 . PHE A 1 124 ? 28.772 22.463 14.706 1.00 29.61  ? 119 PHE A CD2 1 
ATOM   909  C  CE1 . PHE A 1 124 ? 28.205 20.503 16.564 1.00 32.35  ? 119 PHE A CE1 1 
ATOM   910  C  CE2 . PHE A 1 124 ? 29.063 22.660 16.043 1.00 29.85  ? 119 PHE A CE2 1 
ATOM   911  C  CZ  . PHE A 1 124 ? 28.781 21.676 16.968 1.00 29.97  ? 119 PHE A CZ  1 
ATOM   912  N  N   . TYR A 1 125 ? 26.034 23.639 12.843 1.00 25.40  ? 120 TYR A N   1 
ATOM   913  C  CA  . TYR A 1 125 ? 25.614 24.843 13.548 1.00 28.08  ? 120 TYR A CA  1 
ATOM   914  C  C   . TYR A 1 125 ? 24.096 24.974 13.631 1.00 19.13  ? 120 TYR A C   1 
ATOM   915  O  O   . TYR A 1 125 ? 23.580 25.445 14.635 1.00 24.16  ? 120 TYR A O   1 
ATOM   916  C  CB  . TYR A 1 125 ? 26.226 26.100 12.942 1.00 26.21  ? 120 TYR A CB  1 
ATOM   917  C  CG  . TYR A 1 125 ? 27.735 26.145 13.049 1.00 26.54  ? 120 TYR A CG  1 
ATOM   918  C  CD1 . TYR A 1 125 ? 28.371 26.011 14.275 1.00 26.92  ? 120 TYR A CD1 1 
ATOM   919  C  CD2 . TYR A 1 125 ? 28.522 26.367 11.930 1.00 34.28  ? 120 TYR A CD2 1 
ATOM   920  C  CE1 . TYR A 1 125 ? 29.758 26.065 14.378 1.00 28.73  ? 120 TYR A CE1 1 
ATOM   921  C  CE2 . TYR A 1 125 ? 29.907 26.421 12.020 1.00 30.93  ? 120 TYR A CE2 1 
ATOM   922  C  CZ  . TYR A 1 125 ? 30.522 26.265 13.243 1.00 27.69  ? 120 TYR A CZ  1 
ATOM   923  O  OH  . TYR A 1 125 ? 31.895 26.285 13.306 1.00 27.97  ? 120 TYR A OH  1 
ATOM   924  N  N   . LEU A 1 126 ? 23.371 24.529 12.600 1.00 23.76  ? 121 LEU A N   1 
ATOM   925  C  CA  . LEU A 1 126 ? 21.919 24.551 12.669 1.00 24.89  ? 121 LEU A CA  1 
ATOM   926  C  C   . LEU A 1 126 ? 21.369 23.520 13.660 1.00 25.57  ? 121 LEU A C   1 
ATOM   927  O  O   . LEU A 1 126 ? 20.339 23.756 14.279 1.00 25.57  ? 121 LEU A O   1 
ATOM   928  C  CB  . LEU A 1 126 ? 21.335 24.326 11.281 1.00 22.35  ? 121 LEU A CB  1 
ATOM   929  C  CG  . LEU A 1 126 ? 21.591 25.435 10.241 1.00 27.60  ? 121 LEU A CG  1 
ATOM   930  C  CD1 . LEU A 1 126 ? 21.179 24.979 8.881  1.00 26.47  ? 121 LEU A CD1 1 
ATOM   931  C  CD2 . LEU A 1 126 ? 20.850 26.713 10.599 1.00 37.38  ? 121 LEU A CD2 1 
ATOM   932  N  N   . LYS A 1 127 ? 22.027 22.354 13.759 1.00 26.53  ? 122 LYS A N   1 
ATOM   933  C  CA  . LYS A 1 127 ? 21.724 21.376 14.794 1.00 27.49  ? 122 LYS A CA  1 
ATOM   934  C  C   . LYS A 1 127 ? 21.936 21.987 16.180 1.00 25.14  ? 122 LYS A C   1 
ATOM   935  O  O   . LYS A 1 127 ? 21.125 21.799 17.076 1.00 23.47  ? 122 LYS A O   1 
ATOM   936  C  CB  . LYS A 1 127 ? 22.617 20.136 14.654 1.00 22.69  ? 122 LYS A CB  1 
ATOM   937  C  CG  . LYS A 1 127 ? 22.476 19.157 15.820 1.00 27.12  ? 122 LYS A CG  1 
ATOM   938  C  CD  . LYS A 1 127 ? 23.493 18.031 15.760 1.00 30.85  ? 122 LYS A CD  1 
ATOM   939  C  CE  . LYS A 1 127 ? 23.546 17.230 17.046 1.00 31.93  ? 122 LYS A CE  1 
ATOM   940  N  NZ  . LYS A 1 127 ? 24.037 18.030 18.229 1.00 29.36  ? 122 LYS A NZ  1 
ATOM   941  N  N   . MET A 1 128 ? 23.044 22.716 16.349 1.00 25.19  ? 123 MET A N   1 
ATOM   942  C  CA  . MET A 1 128 ? 23.361 23.330 17.627 1.00 25.83  ? 123 MET A CA  1 
ATOM   943  C  C   . MET A 1 128 ? 22.289 24.367 17.967 1.00 23.69  ? 123 MET A C   1 
ATOM   944  O  O   . MET A 1 128 ? 21.815 24.434 19.096 1.00 25.14  ? 123 MET A O   1 
ATOM   945  C  CB  . MET A 1 128 ? 24.754 23.942 17.564 1.00 26.48  ? 123 MET A CB  1 
ATOM   946  C  CG  . MET A 1 128 ? 25.282 24.350 18.896 1.00 34.67  ? 123 MET A CG  1 
ATOM   947  S  SD  . MET A 1 128 ? 26.901 25.116 18.757 1.00 34.20  ? 123 MET A SD  1 
ATOM   948  C  CE  . MET A 1 128 ? 27.565 24.773 20.409 1.00 46.75  ? 123 MET A CE  1 
ATOM   949  N  N   . LYS A 1 129 ? 21.838 25.125 16.959 1.00 24.38  ? 124 LYS A N   1 
ATOM   950  C  CA  . LYS A 1 129 ? 20.778 26.095 17.180 1.00 20.20  ? 124 LYS A CA  1 
ATOM   951  C  C   . LYS A 1 129 ? 19.489 25.411 17.634 1.00 26.87  ? 124 LYS A C   1 
ATOM   952  O  O   . LYS A 1 129 ? 18.853 25.856 18.591 1.00 25.44  ? 124 LYS A O   1 
ATOM   953  C  CB  . LYS A 1 129 ? 20.545 26.891 15.917 1.00 19.96  ? 124 LYS A CB  1 
ATOM   954  C  CG  . LYS A 1 129 ? 19.571 28.023 16.063 1.00 27.66  ? 124 LYS A CG  1 
ATOM   955  C  CD  . LYS A 1 129 ? 19.538 28.880 14.798 1.00 27.94  ? 124 LYS A CD  1 
ATOM   956  C  CE  . LYS A 1 129 ? 18.488 29.947 14.880 1.00 36.54  ? 124 LYS A CE  1 
ATOM   957  N  NZ  . LYS A 1 129 ? 18.515 30.824 13.690 1.00 38.33  ? 124 LYS A NZ  1 
ATOM   958  N  N   . GLY A 1 130 ? 19.111 24.329 16.942 1.00 21.06  ? 125 GLY A N   1 
ATOM   959  C  CA  . GLY A 1 130 ? 17.967 23.519 17.337 1.00 29.16  ? 125 GLY A CA  1 
ATOM   960  C  C   . GLY A 1 130 ? 18.067 23.049 18.789 1.00 26.54  ? 125 GLY A C   1 
ATOM   961  O  O   . GLY A 1 130 ? 17.123 23.191 19.559 1.00 26.22  ? 125 GLY A O   1 
ATOM   962  N  N   . ASP A 1 131 ? 19.233 22.503 19.145 1.00 22.41  ? 126 ASP A N   1 
ATOM   963  C  CA  . ASP A 1 131 ? 19.495 22.002 20.483 1.00 22.21  ? 126 ASP A CA  1 
ATOM   964  C  C   . ASP A 1 131 ? 19.325 23.057 21.582 1.00 24.60  ? 126 ASP A C   1 
ATOM   965  O  O   . ASP A 1 131 ? 18.632 22.811 22.559 1.00 25.56  ? 126 ASP A O   1 
ATOM   966  C  CB  . ASP A 1 131 ? 20.905 21.446 20.553 1.00 24.73  ? 126 ASP A CB  1 
ATOM   967  C  CG  . ASP A 1 131 ? 21.170 20.115 19.875 1.00 25.41  ? 126 ASP A CG  1 
ATOM   968  O  OD1 . ASP A 1 131 ? 20.183 19.428 19.478 1.00 24.98  ? 126 ASP A OD1 1 
ATOM   969  O  OD2 . ASP A 1 131 ? 22.355 19.771 19.721 1.00 29.30  ? 126 ASP A OD2 1 
ATOM   970  N  N   . TYR A 1 132 ? 19.951 24.227 21.418 1.00 25.24  ? 127 TYR A N   1 
ATOM   971  C  CA  . TYR A 1 132 ? 19.902 25.246 22.458 1.00 28.29  ? 127 TYR A CA  1 
ATOM   972  C  C   . TYR A 1 132 ? 18.550 25.954 22.537 1.00 24.44  ? 127 TYR A C   1 
ATOM   973  O  O   . TYR A 1 132 ? 18.178 26.384 23.615 1.00 26.07  ? 127 TYR A O   1 
ATOM   974  C  CB  . TYR A 1 132 ? 21.110 26.210 22.388 1.00 28.44  ? 127 TYR A CB  1 
ATOM   975  C  CG  . TYR A 1 132 ? 22.352 25.529 22.909 1.00 26.84  ? 127 TYR A CG  1 
ATOM   976  C  CD1 . TYR A 1 132 ? 23.137 24.749 22.081 1.00 27.83  ? 127 TYR A CD1 1 
ATOM   977  C  CD2 . TYR A 1 132 ? 22.697 25.596 24.253 1.00 24.02  ? 127 TYR A CD2 1 
ATOM   978  C  CE1 . TYR A 1 132 ? 24.246 24.065 22.565 1.00 28.51  ? 127 TYR A CE1 1 
ATOM   979  C  CE2 . TYR A 1 132 ? 23.815 24.939 24.744 1.00 30.78  ? 127 TYR A CE2 1 
ATOM   980  C  CZ  . TYR A 1 132 ? 24.592 24.167 23.893 1.00 31.55  ? 127 TYR A CZ  1 
ATOM   981  O  OH  . TYR A 1 132 ? 25.690 23.480 24.375 1.00 28.31  ? 127 TYR A OH  1 
ATOM   982  N  N   . TYR A 1 133 ? 17.785 26.019 21.438 1.00 21.96  ? 128 TYR A N   1 
ATOM   983  C  CA  . TYR A 1 133 ? 16.372 26.364 21.517 1.00 21.45  ? 128 TYR A CA  1 
ATOM   984  C  C   . TYR A 1 133 ? 15.534 25.315 22.251 1.00 34.92  ? 128 TYR A C   1 
ATOM   985  O  O   . TYR A 1 133 ? 14.623 25.664 23.008 1.00 28.06  ? 128 TYR A O   1 
ATOM   986  C  CB  . TYR A 1 133 ? 15.773 26.623 20.117 1.00 30.15  ? 128 TYR A CB  1 
ATOM   987  C  CG  . TYR A 1 133 ? 15.940 28.063 19.681 1.00 28.41  ? 128 TYR A CG  1 
ATOM   988  C  CD1 . TYR A 1 133 ? 15.399 29.103 20.429 1.00 33.51  ? 128 TYR A CD1 1 
ATOM   989  C  CD2 . TYR A 1 133 ? 16.651 28.387 18.533 1.00 30.11  ? 128 TYR A CD2 1 
ATOM   990  C  CE1 . TYR A 1 133 ? 15.545 30.430 20.034 1.00 32.95  ? 128 TYR A CE1 1 
ATOM   991  C  CE2 . TYR A 1 133 ? 16.810 29.708 18.131 1.00 34.34  ? 128 TYR A CE2 1 
ATOM   992  C  CZ  . TYR A 1 133 ? 16.262 30.728 18.890 1.00 34.22  ? 128 TYR A CZ  1 
ATOM   993  O  OH  . TYR A 1 133 ? 16.425 32.025 18.498 1.00 32.52  ? 128 TYR A OH  1 
ATOM   994  N  N   . ARG A 1 134 ? 15.852 24.033 22.034 1.00 26.85  ? 129 ARG A N   1 
ATOM   995  C  CA  . ARG A 1 134 ? 15.177 22.949 22.730 1.00 25.39  ? 129 ARG A CA  1 
ATOM   996  C  C   . ARG A 1 134 ? 15.431 23.040 24.241 1.00 20.16  ? 129 ARG A C   1 
ATOM   997  O  O   . ARG A 1 134 ? 14.524 22.818 25.038 1.00 24.80  ? 129 ARG A O   1 
ATOM   998  C  CB  . ARG A 1 134 ? 15.614 21.573 22.144 1.00 23.76  ? 129 ARG A CB  1 
ATOM   999  C  CG  . ARG A 1 134 ? 15.222 20.358 23.014 1.00 27.64  ? 129 ARG A CG  1 
ATOM   1000 C  CD  . ARG A 1 134 ? 15.191 19.060 22.216 1.00 31.30  ? 129 ARG A CD  1 
ATOM   1001 N  NE  . ARG A 1 134 ? 16.522 18.683 21.758 1.00 25.58  ? 129 ARG A NE  1 
ATOM   1002 C  CZ  . ARG A 1 134 ? 17.437 18.075 22.498 1.00 22.04  ? 129 ARG A CZ  1 
ATOM   1003 N  NH1 . ARG A 1 134 ? 17.134 17.545 23.675 1.00 23.58  ? 129 ARG A NH1 1 
ATOM   1004 N  NH2 . ARG A 1 134 ? 18.670 17.934 22.017 1.00 28.88  ? 129 ARG A NH2 1 
ATOM   1005 N  N   . TYR A 1 135 ? 16.658 23.395 24.639 1.00 23.41  ? 130 TYR A N   1 
ATOM   1006 C  CA  . TYR A 1 135 ? 16.977 23.534 26.054 1.00 26.76  ? 130 TYR A CA  1 
ATOM   1007 C  C   . TYR A 1 135 ? 16.200 24.709 26.645 1.00 26.62  ? 130 TYR A C   1 
ATOM   1008 O  O   . TYR A 1 135 ? 15.733 24.628 27.773 1.00 25.67  ? 130 TYR A O   1 
ATOM   1009 C  CB  . TYR A 1 135 ? 18.489 23.672 26.278 1.00 27.04  ? 130 TYR A CB  1 
ATOM   1010 C  CG  . TYR A 1 135 ? 19.316 22.533 25.700 1.00 29.57  ? 130 TYR A CG  1 
ATOM   1011 C  CD1 . TYR A 1 135 ? 18.776 21.262 25.536 1.00 32.01  ? 130 TYR A CD1 1 
ATOM   1012 C  CD2 . TYR A 1 135 ? 20.628 22.739 25.291 1.00 23.70  ? 130 TYR A CD2 1 
ATOM   1013 C  CE1 . TYR A 1 135 ? 19.536 20.218 25.017 1.00 25.81  ? 130 TYR A CE1 1 
ATOM   1014 C  CE2 . TYR A 1 135 ? 21.392 21.707 24.759 1.00 27.53  ? 130 TYR A CE2 1 
ATOM   1015 C  CZ  . TYR A 1 135 ? 20.842 20.446 24.621 1.00 30.80  ? 130 TYR A CZ  1 
ATOM   1016 O  OH  . TYR A 1 135 ? 21.596 19.432 24.070 1.00 33.40  ? 130 TYR A OH  1 
ATOM   1017 N  N   . LEU A 1 136 ? 16.010 25.782 25.868 1.00 24.27  ? 131 LEU A N   1 
ATOM   1018 C  CA  . LEU A 1 136 ? 15.144 26.866 26.309 1.00 24.57  ? 131 LEU A CA  1 
ATOM   1019 C  C   . LEU A 1 136 ? 13.696 26.404 26.434 1.00 24.72  ? 131 LEU A C   1 
ATOM   1020 O  O   . LEU A 1 136 ? 13.013 26.794 27.380 1.00 26.86  ? 131 LEU A O   1 
ATOM   1021 C  CB  . LEU A 1 136 ? 15.209 28.076 25.374 1.00 22.48  ? 131 LEU A CB  1 
ATOM   1022 C  CG  . LEU A 1 136 ? 16.486 28.881 25.417 1.00 20.72  ? 131 LEU A CG  1 
ATOM   1023 C  CD1 . LEU A 1 136 ? 16.421 30.036 24.408 1.00 34.60  ? 131 LEU A CD1 1 
ATOM   1024 C  CD2 . LEU A 1 136 ? 16.740 29.427 26.801 1.00 25.48  ? 131 LEU A CD2 1 
ATOM   1025 N  N   . ALA A 1 137 ? 13.249 25.555 25.497 1.00 22.85  ? 132 ALA A N   1 
ATOM   1026 C  CA  . ALA A 1 137 ? 11.879 25.076 25.476 1.00 25.97  ? 132 ALA A CA  1 
ATOM   1027 C  C   . ALA A 1 137 ? 11.546 24.189 26.675 1.00 23.72  ? 132 ALA A C   1 
ATOM   1028 O  O   . ALA A 1 137 ? 10.406 24.194 27.137 1.00 30.79  ? 132 ALA A O   1 
ATOM   1029 C  CB  . ALA A 1 137 ? 11.597 24.333 24.168 1.00 27.49  ? 132 ALA A CB  1 
ATOM   1030 N  N   . GLU A 1 138 ? 12.539 23.440 27.180 1.00 26.98  ? 133 GLU A N   1 
ATOM   1031 C  CA  . GLU A 1 138 ? 12.356 22.615 28.367 1.00 30.06  ? 133 GLU A CA  1 
ATOM   1032 C  C   . GLU A 1 138 ? 11.917 23.409 29.600 1.00 32.72  ? 133 GLU A C   1 
ATOM   1033 O  O   . GLU A 1 138 ? 11.160 22.893 30.415 1.00 29.41  ? 133 GLU A O   1 
ATOM   1034 C  CB  . GLU A 1 138 ? 13.649 21.852 28.708 1.00 28.43  ? 133 GLU A CB  1 
ATOM   1035 C  CG  . GLU A 1 138 ? 14.030 20.806 27.666 1.00 34.31  ? 133 GLU A CG  1 
ATOM   1036 C  CD  . GLU A 1 138 ? 15.324 20.053 27.911 1.00 31.23  ? 133 GLU A CD  1 
ATOM   1037 O  OE1 . GLU A 1 138 ? 16.140 20.490 28.751 1.00 30.69  ? 133 GLU A OE1 1 
ATOM   1038 O  OE2 . GLU A 1 138 ? 15.515 19.003 27.262 1.00 30.06  ? 133 GLU A OE2 1 
ATOM   1039 N  N   . VAL A 1 139 ? 12.380 24.661 29.720 1.00 23.57  ? 134 VAL A N   1 
ATOM   1040 C  CA  . VAL A 1 139 ? 12.055 25.507 30.864 1.00 29.92  ? 134 VAL A CA  1 
ATOM   1041 C  C   . VAL A 1 139 ? 11.047 26.623 30.573 1.00 40.17  ? 134 VAL A C   1 
ATOM   1042 O  O   . VAL A 1 139 ? 10.699 27.377 31.471 1.00 29.09  ? 134 VAL A O   1 
ATOM   1043 C  CB  . VAL A 1 139 ? 13.363 26.083 31.471 1.00 29.16  ? 134 VAL A CB  1 
ATOM   1044 C  CG1 . VAL A 1 139 ? 14.381 24.963 31.749 1.00 24.65  ? 134 VAL A CG1 1 
ATOM   1045 C  CG2 . VAL A 1 139 ? 13.985 27.181 30.597 1.00 24.39  ? 134 VAL A CG2 1 
ATOM   1046 N  N   . ALA A 1 140 ? 10.551 26.718 29.332 1.00 34.05  ? 135 ALA A N   1 
ATOM   1047 C  CA  . ALA A 1 140 ? 9.650  27.796 28.937 1.00 26.97  ? 135 ALA A CA  1 
ATOM   1048 C  C   . ALA A 1 140 ? 8.191  27.497 29.287 1.00 34.33  ? 135 ALA A C   1 
ATOM   1049 O  O   . ALA A 1 140 ? 7.823  26.340 29.493 1.00 42.97  ? 135 ALA A O   1 
ATOM   1050 C  CB  . ALA A 1 140 ? 9.785  28.055 27.428 1.00 28.06  ? 135 ALA A CB  1 
ATOM   1051 N  N   . THR A 1 141 ? 7.365  28.557 29.311 1.00 50.24  ? 136 THR A N   1 
ATOM   1052 C  CA  . THR A 1 141 ? 5.979  28.470 29.753 1.00 70.76  ? 136 THR A CA  1 
ATOM   1053 C  C   . THR A 1 141 ? 4.930  28.996 28.769 1.00 101.39 ? 136 THR A C   1 
ATOM   1054 O  O   . THR A 1 141 ? 4.025  28.254 28.388 1.00 73.09  ? 136 THR A O   1 
ATOM   1055 C  CB  . THR A 1 141 ? 5.828  29.210 31.090 1.00 55.86  ? 136 THR A CB  1 
ATOM   1056 O  OG1 . THR A 1 141 ? 6.363  30.530 30.950 1.00 46.05  ? 136 THR A OG1 1 
ATOM   1057 C  CG2 . THR A 1 141 ? 6.526  28.493 32.235 1.00 49.22  ? 136 THR A CG2 1 
ATOM   1058 N  N   . GLY A 1 142 ? 5.043  30.272 28.369 1.00 48.28  ? 137 GLY A N   1 
ATOM   1059 C  CA  . GLY A 1 142 ? 3.930  30.989 27.756 1.00 54.02  ? 137 GLY A CA  1 
ATOM   1060 C  C   . GLY A 1 142 ? 4.076  31.342 26.275 1.00 54.80  ? 137 GLY A C   1 
ATOM   1061 O  O   . GLY A 1 142 ? 4.402  30.489 25.452 1.00 53.19  ? 137 GLY A O   1 
ATOM   1062 N  N   . ASP A 1 143 ? 3.789  32.609 25.943 1.00 103.45 ? 138 ASP A N   1 
ATOM   1063 C  CA  . ASP A 1 143 ? 4.000  33.135 24.602 1.00 65.60  ? 138 ASP A CA  1 
ATOM   1064 C  C   . ASP A 1 143 ? 5.439  32.927 24.143 1.00 116.99 ? 138 ASP A C   1 
ATOM   1065 O  O   . ASP A 1 143 ? 5.683  32.643 22.972 1.00 53.92  ? 138 ASP A O   1 
ATOM   1066 C  CB  . ASP A 1 143 ? 3.683  34.641 24.544 1.00 70.62  ? 138 ASP A CB  1 
ATOM   1067 C  CG  . ASP A 1 143 ? 2.218  35.005 24.460 1.00 68.76  ? 138 ASP A CG  1 
ATOM   1068 O  OD1 . ASP A 1 143 ? 1.402  34.119 24.129 1.00 38.25  ? 138 ASP A OD1 1 
ATOM   1069 O  OD2 . ASP A 1 143 ? 1.888  36.178 24.723 1.00 37.31  ? 138 ASP A OD2 1 
ATOM   1070 N  N   . ASP A 1 144 ? 6.379  33.090 25.083 1.00 38.47  ? 139 ASP A N   1 
ATOM   1071 C  CA  . ASP A 1 144 ? 7.790  32.865 24.822 1.00 71.82  ? 139 ASP A CA  1 
ATOM   1072 C  C   . ASP A 1 144 ? 8.041  31.455 24.281 1.00 71.72  ? 139 ASP A C   1 
ATOM   1073 O  O   . ASP A 1 144 ? 8.897  31.278 23.416 1.00 47.03  ? 139 ASP A O   1 
ATOM   1074 C  CB  . ASP A 1 144 ? 8.614  33.116 26.111 1.00 51.32  ? 139 ASP A CB  1 
ATOM   1075 C  CG  . ASP A 1 144 ? 10.097 33.380 25.887 1.00 80.58  ? 139 ASP A CG  1 
ATOM   1076 O  OD1 . ASP A 1 144 ? 10.463 33.814 24.771 1.00 68.82  ? 139 ASP A OD1 1 
ATOM   1077 O  OD2 . ASP A 1 144 ? 10.898 33.131 26.824 1.00 49.43  ? 139 ASP A OD2 1 
ATOM   1078 N  N   . LYS A 1 145 ? 7.266  30.471 24.765 1.00 40.95  ? 140 LYS A N   1 
ATOM   1079 C  CA  . LYS A 1 145 ? 7.497  29.060 24.482 1.00 45.20  ? 140 LYS A CA  1 
ATOM   1080 C  C   . LYS A 1 145 ? 7.228  28.633 23.040 1.00 50.88  ? 140 LYS A C   1 
ATOM   1081 O  O   . LYS A 1 145 ? 8.020  27.903 22.444 1.00 32.46  ? 140 LYS A O   1 
ATOM   1082 C  CB  . LYS A 1 145 ? 6.617  28.180 25.387 1.00 36.61  ? 140 LYS A CB  1 
ATOM   1083 C  CG  . LYS A 1 145 ? 7.047  26.717 25.363 1.00 36.41  ? 140 LYS A CG  1 
ATOM   1084 C  CD  . LYS A 1 145 ? 6.215  25.801 26.227 1.00 60.00  ? 140 LYS A CD  1 
ATOM   1085 C  CE  . LYS A 1 145 ? 6.861  24.440 26.351 1.00 36.69  ? 140 LYS A CE  1 
ATOM   1086 N  NZ  . LYS A 1 145 ? 5.940  23.453 26.956 1.00 63.14  ? 140 LYS A NZ  1 
ATOM   1087 N  N   . LYS A 1 146 ? 6.076  29.044 22.504 1.00 41.23  ? 141 LYS A N   1 
ATOM   1088 C  CA  . LYS A 1 146 ? 5.703  28.683 21.147 1.00 29.42  ? 141 LYS A CA  1 
ATOM   1089 C  C   . LYS A 1 146 ? 6.677  29.292 20.141 1.00 33.50  ? 141 LYS A C   1 
ATOM   1090 O  O   . LYS A 1 146 ? 7.008  28.644 19.151 1.00 50.42  ? 141 LYS A O   1 
ATOM   1091 C  CB  . LYS A 1 146 ? 4.255  29.100 20.859 1.00 61.69  ? 141 LYS A CB  1 
ATOM   1092 C  CG  . LYS A 1 146 ? 3.248  28.319 21.688 1.00 86.94  ? 141 LYS A CG  1 
ATOM   1093 C  CD  . LYS A 1 146 ? 1.812  28.696 21.400 1.00 95.72  ? 141 LYS A CD  1 
ATOM   1094 C  CE  . LYS A 1 146 ? 0.857  27.967 22.311 1.00 64.68  ? 141 LYS A CE  1 
ATOM   1095 N  NZ  . LYS A 1 146 ? -0.545 28.377 22.074 1.00 64.54  ? 141 LYS A NZ  1 
ATOM   1096 N  N   . ARG A 1 147 ? 7.147  30.522 20.409 1.00 36.89  ? 142 ARG A N   1 
ATOM   1097 C  CA  . ARG A 1 147 ? 8.212  31.124 19.615 1.00 43.58  ? 142 ARG A CA  1 
ATOM   1098 C  C   . ARG A 1 147 ? 9.453  30.234 19.641 1.00 39.62  ? 142 ARG A C   1 
ATOM   1099 O  O   . ARG A 1 147 ? 10.070 29.987 18.609 1.00 31.47  ? 142 ARG A O   1 
ATOM   1100 C  CB  . ARG A 1 147 ? 8.620  32.522 20.126 1.00 34.89  ? 142 ARG A CB  1 
ATOM   1101 C  CG  . ARG A 1 147 ? 7.534  33.590 20.102 1.00 71.69  ? 142 ARG A CG  1 
ATOM   1102 C  CD  . ARG A 1 147 ? 8.052  34.876 20.727 1.00 70.93  ? 142 ARG A CD  1 
ATOM   1103 N  NE  . ARG A 1 147 ? 6.978  35.707 21.262 1.00 99.62  ? 142 ARG A NE  1 
ATOM   1104 C  CZ  . ARG A 1 147 ? 7.142  36.643 22.190 1.00 39.35  ? 142 ARG A CZ  1 
ATOM   1105 N  NH1 . ARG A 1 147 ? 8.332  36.905 22.707 1.00 71.78  ? 142 ARG A NH1 1 
ATOM   1106 N  NH2 . ARG A 1 147 ? 6.082  37.315 22.628 1.00 70.71  ? 142 ARG A NH2 1 
ATOM   1107 N  N   . ILE A 1 148 ? 9.813  29.765 20.843 1.00 30.90  ? 143 ILE A N   1 
ATOM   1108 C  CA  . ILE A 1 148 ? 11.013 28.968 21.037 1.00 42.00  ? 143 ILE A CA  1 
ATOM   1109 C  C   . ILE A 1 148 ? 10.929 27.610 20.342 1.00 28.70  ? 143 ILE A C   1 
ATOM   1110 O  O   . ILE A 1 148 ? 11.884 27.202 19.686 1.00 30.76  ? 143 ILE A O   1 
ATOM   1111 C  CB  . ILE A 1 148 ? 11.314 28.827 22.549 1.00 28.38  ? 143 ILE A CB  1 
ATOM   1112 C  CG1 . ILE A 1 148 ? 11.796 30.152 23.136 1.00 37.10  ? 143 ILE A CG1 1 
ATOM   1113 C  CG2 . ILE A 1 148 ? 12.330 27.730 22.811 1.00 27.01  ? 143 ILE A CG2 1 
ATOM   1114 C  CD1 . ILE A 1 148 ? 11.733 30.204 24.662 1.00 41.58  ? 143 ILE A CD1 1 
ATOM   1115 N  N   . ILE A 1 149 ? 9.787  26.923 20.489 1.00 28.17  ? 144 ILE A N   1 
ATOM   1116 C  CA  . ILE A 1 149 ? 9.577  25.629 19.858 1.00 33.96  ? 144 ILE A CA  1 
ATOM   1117 C  C   . ILE A 1 149 ? 9.622  25.717 18.330 1.00 28.03  ? 144 ILE A C   1 
ATOM   1118 O  O   . ILE A 1 149 ? 10.209 24.854 17.681 1.00 31.88  ? 144 ILE A O   1 
ATOM   1119 C  CB  . ILE A 1 149 ? 8.258  25.006 20.371 1.00 37.16  ? 144 ILE A CB  1 
ATOM   1120 C  CG1 . ILE A 1 149 ? 8.438  24.525 21.829 1.00 28.57  ? 144 ILE A CG1 1 
ATOM   1121 C  CG2 . ILE A 1 149 ? 7.760  23.873 19.457 1.00 43.35  ? 144 ILE A CG2 1 
ATOM   1122 C  CD1 . ILE A 1 149 ? 7.235  23.821 22.401 1.00 30.56  ? 144 ILE A CD1 1 
ATOM   1123 N  N   . ASP A 1 150 ? 9.000  26.766 17.778 1.00 31.92  ? 145 ASP A N   1 
ATOM   1124 C  CA  . ASP A 1 150 ? 9.022  27.036 16.347 1.00 48.89  ? 145 ASP A CA  1 
ATOM   1125 C  C   . ASP A 1 150 ? 10.436 27.285 15.827 1.00 33.74  ? 145 ASP A C   1 
ATOM   1126 O  O   . ASP A 1 150 ? 10.781 26.841 14.733 1.00 30.43  ? 145 ASP A O   1 
ATOM   1127 C  CB  . ASP A 1 150 ? 8.144  28.263 16.021 1.00 43.76  ? 145 ASP A CB  1 
ATOM   1128 C  CG  . ASP A 1 150 ? 6.651  28.034 16.147 1.00 39.57  ? 145 ASP A CG  1 
ATOM   1129 O  OD1 . ASP A 1 150 ? 6.231  26.852 16.201 1.00 55.94  ? 145 ASP A OD1 1 
ATOM   1130 O  OD2 . ASP A 1 150 ? 5.898  29.040 16.208 1.00 38.07  ? 145 ASP A OD2 1 
ATOM   1131 N  N   . SER A 1 151 ? 11.232 28.023 16.615 1.00 29.95  ? 146 SER A N   1 
ATOM   1132 C  CA  . SER A 1 151 ? 12.624 28.286 16.292 1.00 38.05  ? 146 SER A CA  1 
ATOM   1133 C  C   . SER A 1 151 ? 13.484 27.022 16.298 1.00 31.92  ? 146 SER A C   1 
ATOM   1134 O  O   . SER A 1 151 ? 14.366 26.882 15.455 1.00 31.87  ? 146 SER A O   1 
ATOM   1135 C  CB  . SER A 1 151 ? 13.209 29.311 17.253 1.00 33.96  ? 146 SER A CB  1 
ATOM   1136 O  OG  . SER A 1 151 ? 12.554 30.557 17.099 1.00 36.12  ? 146 SER A OG  1 
ATOM   1137 N  N   . ALA A 1 152 ? 13.233 26.111 17.249 1.00 38.37  ? 147 ALA A N   1 
ATOM   1138 C  CA  . ALA A 1 152 ? 13.947 24.843 17.291 1.00 27.05  ? 147 ALA A CA  1 
ATOM   1139 C  C   . ALA A 1 152 ? 13.605 23.997 16.061 1.00 26.19  ? 147 ALA A C   1 
ATOM   1140 O  O   . ALA A 1 152 ? 14.505 23.503 15.380 1.00 28.07  ? 147 ALA A O   1 
ATOM   1141 C  CB  . ALA A 1 152 ? 13.638 24.079 18.576 1.00 25.98  ? 147 ALA A CB  1 
ATOM   1142 N  N   . ARG A 1 153 ? 12.305 23.836 15.780 1.00 27.17  ? 148 ARG A N   1 
ATOM   1143 C  CA  . ARG A 1 153 ? 11.854 23.010 14.667 1.00 25.89  ? 148 ARG A CA  1 
ATOM   1144 C  C   . ARG A 1 153 ? 12.427 23.534 13.353 1.00 38.35  ? 148 ARG A C   1 
ATOM   1145 O  O   . ARG A 1 153 ? 12.936 22.757 12.552 1.00 33.61  ? 148 ARG A O   1 
ATOM   1146 C  CB  . ARG A 1 153 ? 10.314 22.954 14.574 1.00 30.52  ? 148 ARG A CB  1 
ATOM   1147 C  CG  . ARG A 1 153 ? 9.791  22.131 13.360 1.00 35.43  ? 148 ARG A CG  1 
ATOM   1148 C  CD  . ARG A 1 153 ? 8.276  22.040 13.308 1.00 41.18  ? 148 ARG A CD  1 
ATOM   1149 N  NE  . ARG A 1 153 ? 7.716  21.519 14.553 1.00 36.53  ? 148 ARG A NE  1 
ATOM   1150 C  CZ  . ARG A 1 153 ? 6.944  22.217 15.378 1.00 55.89  ? 148 ARG A CZ  1 
ATOM   1151 N  NH1 . ARG A 1 153 ? 6.715  23.508 15.187 1.00 50.83  ? 148 ARG A NH1 1 
ATOM   1152 N  NH2 . ARG A 1 153 ? 6.397  21.608 16.426 1.00 46.02  ? 148 ARG A NH2 1 
ATOM   1153 N  N   . SER A 1 154 ? 12.328 24.854 13.151 1.00 30.04  ? 149 SER A N   1 
ATOM   1154 C  CA  . SER A 1 154 ? 12.848 25.513 11.964 1.00 36.74  ? 149 SER A CA  1 
ATOM   1155 C  C   . SER A 1 154 ? 14.342 25.262 11.740 1.00 45.53  ? 149 SER A C   1 
ATOM   1156 O  O   . SER A 1 154 ? 14.760 24.937 10.628 1.00 28.72  ? 149 SER A O   1 
ATOM   1157 C  CB  . SER A 1 154 ? 12.562 27.010 12.052 1.00 48.47  ? 149 SER A CB  1 
ATOM   1158 O  OG  . SER A 1 154 ? 13.111 27.711 10.952 1.00 50.49  ? 149 SER A OG  1 
ATOM   1159 N  N   . ALA A 1 155 ? 15.140 25.406 12.805 1.00 35.25  ? 150 ALA A N   1 
ATOM   1160 C  CA  . ALA A 1 155 ? 16.575 25.163 12.741 1.00 40.50  ? 150 ALA A CA  1 
ATOM   1161 C  C   . ALA A 1 155 ? 16.890 23.703 12.420 1.00 27.62  ? 150 ALA A C   1 
ATOM   1162 O  O   . ALA A 1 155 ? 17.718 23.424 11.555 1.00 21.79  ? 150 ALA A O   1 
ATOM   1163 C  CB  . ALA A 1 155 ? 17.245 25.569 14.049 1.00 32.92  ? 150 ALA A CB  1 
ATOM   1164 N  N   . TYR A 1 156 ? 16.218 22.782 13.121 1.00 25.31  ? 151 TYR A N   1 
ATOM   1165 C  CA  . TYR A 1 156 ? 16.390 21.356 12.894 1.00 26.72  ? 151 TYR A CA  1 
ATOM   1166 C  C   . TYR A 1 156 ? 15.967 20.943 11.484 1.00 27.36  ? 151 TYR A C   1 
ATOM   1167 O  O   . TYR A 1 156 ? 16.656 20.170 10.829 1.00 22.20  ? 151 TYR A O   1 
ATOM   1168 C  CB  . TYR A 1 156 ? 15.567 20.528 13.890 1.00 21.33  ? 151 TYR A CB  1 
ATOM   1169 C  CG  . TYR A 1 156 ? 16.141 20.379 15.291 1.00 28.73  ? 151 TYR A CG  1 
ATOM   1170 C  CD1 . TYR A 1 156 ? 17.468 20.013 15.491 1.00 23.56  ? 151 TYR A CD1 1 
ATOM   1171 C  CD2 . TYR A 1 156 ? 15.330 20.501 16.410 1.00 26.73  ? 151 TYR A CD2 1 
ATOM   1172 C  CE1 . TYR A 1 156 ? 17.977 19.798 16.773 1.00 26.69  ? 151 TYR A CE1 1 
ATOM   1173 C  CE2 . TYR A 1 156 ? 15.830 20.302 17.691 1.00 25.46  ? 151 TYR A CE2 1 
ATOM   1174 C  CZ  . TYR A 1 156 ? 17.154 19.957 17.871 1.00 25.68  ? 151 TYR A CZ  1 
ATOM   1175 O  OH  . TYR A 1 156 ? 17.623 19.770 19.161 1.00 26.52  ? 151 TYR A OH  1 
ATOM   1176 N  N   . GLN A 1 157 ? 14.810 21.443 11.039 1.00 27.30  ? 152 GLN A N   1 
ATOM   1177 C  CA  . GLN A 1 157 ? 14.250 21.031 9.761  1.00 36.88  ? 152 GLN A CA  1 
ATOM   1178 C  C   . GLN A 1 157 ? 15.148 21.495 8.613  1.00 35.89  ? 152 GLN A C   1 
ATOM   1179 O  O   . GLN A 1 157 ? 15.378 20.746 7.667  1.00 30.52  ? 152 GLN A O   1 
ATOM   1180 C  CB  . GLN A 1 157 ? 12.804 21.547 9.602  1.00 31.16  ? 152 GLN A CB  1 
ATOM   1181 C  CG  . GLN A 1 157 ? 12.079 20.966 8.364  1.00 42.84  ? 152 GLN A CG  1 
ATOM   1182 C  CD  . GLN A 1 157 ? 11.983 19.447 8.384  1.00 44.68  ? 152 GLN A CD  1 
ATOM   1183 O  OE1 . GLN A 1 157 ? 11.315 18.853 9.237  1.00 41.52  ? 152 GLN A OE1 1 
ATOM   1184 N  NE2 . GLN A 1 157 ? 12.644 18.783 7.431  1.00 36.83  ? 152 GLN A NE2 1 
ATOM   1185 N  N   . GLU A 1 158 ? 15.703 22.708 8.723  1.00 27.66  ? 153 GLU A N   1 
ATOM   1186 C  CA  . GLU A 1 158 ? 16.670 23.170 7.739  1.00 39.36  ? 153 GLU A CA  1 
ATOM   1187 C  C   . GLU A 1 158 ? 17.950 22.330 7.751  1.00 23.59  ? 153 GLU A C   1 
ATOM   1188 O  O   . GLU A 1 158 ? 18.492 22.016 6.697  1.00 24.62  ? 153 GLU A O   1 
ATOM   1189 C  CB  . GLU A 1 158 ? 17.008 24.646 7.953  1.00 31.00  ? 153 GLU A CB  1 
ATOM   1190 C  CG  . GLU A 1 158 ? 17.773 25.225 6.775  1.00 49.42  ? 153 GLU A CG  1 
ATOM   1191 C  CD  . GLU A 1 158 ? 18.298 26.629 6.963  1.00 74.02  ? 153 GLU A CD  1 
ATOM   1192 O  OE1 . GLU A 1 158 ? 17.895 27.300 7.942  1.00 47.20  ? 153 GLU A OE1 1 
ATOM   1193 O  OE2 . GLU A 1 158 ? 19.134 27.052 6.131  1.00 42.98  ? 153 GLU A OE2 1 
ATOM   1194 N  N   . ALA A 1 159 ? 18.449 21.980 8.950  1.00 23.67  ? 154 ALA A N   1 
ATOM   1195 C  CA  . ALA A 1 159 ? 19.609 21.108 9.047  1.00 29.58  ? 154 ALA A CA  1 
ATOM   1196 C  C   . ALA A 1 159 ? 19.346 19.751 8.388  1.00 25.93  ? 154 ALA A C   1 
ATOM   1197 O  O   . ALA A 1 159 ? 20.236 19.183 7.764  1.00 22.52  ? 154 ALA A O   1 
ATOM   1198 C  CB  . ALA A 1 159 ? 20.025 20.926 10.495 1.00 24.39  ? 154 ALA A CB  1 
ATOM   1199 N  N   . MET A 1 160 ? 18.120 19.239 8.542  1.00 24.48  ? 155 MET A N   1 
ATOM   1200 C  CA  . MET A 1 160 ? 17.744 17.936 8.010  1.00 24.14  ? 155 MET A CA  1 
ATOM   1201 C  C   . MET A 1 160 ? 17.756 17.933 6.485  1.00 24.56  ? 155 MET A C   1 
ATOM   1202 O  O   . MET A 1 160 ? 18.228 16.976 5.870  1.00 29.85  ? 155 MET A O   1 
ATOM   1203 C  CB  . MET A 1 160 ? 16.330 17.555 8.481  1.00 25.17  ? 155 MET A CB  1 
ATOM   1204 C  CG  . MET A 1 160 ? 16.247 17.156 9.945  1.00 38.45  ? 155 MET A CG  1 
ATOM   1205 S  SD  . MET A 1 160 ? 17.012 15.572 10.388 1.00 33.53  ? 155 MET A SD  1 
ATOM   1206 C  CE  . MET A 1 160 ? 16.309 14.481 9.152  1.00 37.01  ? 155 MET A CE  1 
ATOM   1207 N  N   . ASP A 1 161 ? 17.212 19.008 5.894  1.00 27.72  ? 156 ASP A N   1 
ATOM   1208 C  CA  . ASP A 1 161 ? 17.132 19.163 4.447  1.00 27.98  ? 156 ASP A CA  1 
ATOM   1209 C  C   . ASP A 1 161 ? 18.520 19.130 3.813  1.00 26.67  ? 156 ASP A C   1 
ATOM   1210 O  O   . ASP A 1 161 ? 18.740 18.444 2.814  1.00 26.45  ? 156 ASP A O   1 
ATOM   1211 C  CB  . ASP A 1 161 ? 16.432 20.498 4.093  1.00 41.44  ? 156 ASP A CB  1 
ATOM   1212 C  CG  . ASP A 1 161 ? 14.957 20.577 4.456  1.00 50.02  ? 156 ASP A CG  1 
ATOM   1213 O  OD1 . ASP A 1 161 ? 14.351 19.515 4.723  1.00 45.29  ? 156 ASP A OD1 1 
ATOM   1214 O  OD2 . ASP A 1 161 ? 14.416 21.702 4.492  1.00 45.94  ? 156 ASP A OD2 1 
ATOM   1215 N  N   . ILE A 1 162 ? 19.454 19.875 4.418  1.00 24.12  ? 157 ILE A N   1 
ATOM   1216 C  CA  . ILE A 1 162 ? 20.826 19.918 3.941  1.00 25.02  ? 157 ILE A CA  1 
ATOM   1217 C  C   . ILE A 1 162 ? 21.522 18.568 4.127  1.00 32.28  ? 157 ILE A C   1 
ATOM   1218 O  O   . ILE A 1 162 ? 22.181 18.091 3.206  1.00 28.79  ? 157 ILE A O   1 
ATOM   1219 C  CB  . ILE A 1 162 ? 21.616 21.050 4.634  1.00 23.90  ? 157 ILE A CB  1 
ATOM   1220 C  CG1 . ILE A 1 162 ? 21.001 22.443 4.353  1.00 42.95  ? 157 ILE A CG1 1 
ATOM   1221 C  CG2 . ILE A 1 162 ? 23.091 20.997 4.237  1.00 30.46  ? 157 ILE A CG2 1 
ATOM   1222 C  CD1 . ILE A 1 162 ? 21.497 23.523 5.321  1.00 31.94  ? 157 ILE A CD1 1 
ATOM   1223 N  N   . SER A 1 163 ? 21.378 17.956 5.316  1.00 24.75  ? 158 SER A N   1 
ATOM   1224 C  CA  . SER A 1 163 ? 22.053 16.699 5.590  1.00 21.15  ? 158 SER A CA  1 
ATOM   1225 C  C   . SER A 1 163 ? 21.624 15.601 4.614  1.00 27.13  ? 158 SER A C   1 
ATOM   1226 O  O   . SER A 1 163 ? 22.459 14.842 4.148  1.00 29.87  ? 158 SER A O   1 
ATOM   1227 C  CB  . SER A 1 163 ? 21.838 16.246 7.043  1.00 26.30  ? 158 SER A CB  1 
ATOM   1228 O  OG  . SER A 1 163 ? 20.511 15.791 7.269  1.00 31.65  ? 158 SER A OG  1 
ATOM   1229 N  N   . LYS A 1 164 ? 20.324 15.531 4.306  1.00 32.82  ? 159 LYS A N   1 
ATOM   1230 C  CA  . LYS A 1 164 ? 19.788 14.512 3.415  1.00 29.64  ? 159 LYS A CA  1 
ATOM   1231 C  C   . LYS A 1 164 ? 20.272 14.674 1.973  1.00 29.24  ? 159 LYS A C   1 
ATOM   1232 O  O   . LYS A 1 164 ? 20.404 13.695 1.249  1.00 29.51  ? 159 LYS A O   1 
ATOM   1233 C  CB  . LYS A 1 164 ? 18.251 14.527 3.471  1.00 45.16  ? 159 LYS A CB  1 
ATOM   1234 C  CG  . LYS A 1 164 ? 17.675 14.023 4.810  1.00 37.36  ? 159 LYS A CG  1 
ATOM   1235 C  CD  . LYS A 1 164 ? 16.138 13.905 4.830  1.00 54.89  ? 159 LYS A CD  1 
ATOM   1236 C  CE  . LYS A 1 164 ? 15.640 12.783 3.938  1.00 84.23  ? 159 LYS A CE  1 
ATOM   1237 N  NZ  . LYS A 1 164 ? 14.160 12.739 3.875  1.00 86.79  ? 159 LYS A NZ  1 
ATOM   1238 N  N   . LYS A 1 165 ? 20.556 15.914 1.567  1.00 26.65  ? 160 LYS A N   1 
ATOM   1239 C  CA  . LYS A 1 165 ? 21.046 16.186 0.225  1.00 35.13  ? 160 LYS A CA  1 
ATOM   1240 C  C   . LYS A 1 165 ? 22.565 16.060 0.116  1.00 40.04  ? 160 LYS A C   1 
ATOM   1241 O  O   . LYS A 1 165 ? 23.073 15.676 -0.930 1.00 30.12  ? 160 LYS A O   1 
ATOM   1242 C  CB  . LYS A 1 165 ? 20.576 17.585 -0.229 1.00 34.01  ? 160 LYS A CB  1 
ATOM   1243 C  CG  . LYS A 1 165 ? 19.083 17.628 -0.509 1.00 85.13  ? 160 LYS A CG  1 
ATOM   1244 C  CD  . LYS A 1 165 ? 18.505 19.020 -0.531 1.00 84.85  ? 160 LYS A CD  1 
ATOM   1245 C  CE  . LYS A 1 165 ? 16.999 18.969 -0.624 1.00 120.70 ? 160 LYS A CE  1 
ATOM   1246 N  NZ  . LYS A 1 165 ? 16.386 20.313 -0.485 1.00 57.49  ? 160 LYS A NZ  1 
ATOM   1247 N  N   . GLU A 1 166 ? 23.295 16.353 1.197  1.00 25.60  ? 161 GLU A N   1 
ATOM   1248 C  CA  . GLU A 1 166 ? 24.736 16.537 1.094  1.00 24.05  ? 161 GLU A CA  1 
ATOM   1249 C  C   . GLU A 1 166 ? 25.613 15.561 1.870  1.00 35.07  ? 161 GLU A C   1 
ATOM   1250 O  O   . GLU A 1 166 ? 26.821 15.548 1.665  1.00 33.69  ? 161 GLU A O   1 
ATOM   1251 C  CB  . GLU A 1 166 ? 25.084 17.964 1.513  1.00 29.06  ? 161 GLU A CB  1 
ATOM   1252 C  CG  . GLU A 1 166 ? 24.304 18.975 0.694  1.00 40.17  ? 161 GLU A CG  1 
ATOM   1253 C  CD  . GLU A 1 166 ? 24.968 20.324 0.581  1.00 72.97  ? 161 GLU A CD  1 
ATOM   1254 O  OE1 . GLU A 1 166 ? 26.113 20.381 0.078  1.00 87.76  ? 161 GLU A OE1 1 
ATOM   1255 O  OE2 . GLU A 1 166 ? 24.338 21.326 0.986  1.00 53.04  ? 161 GLU A OE2 1 
ATOM   1256 N  N   . MET A 1 167 ? 25.019 14.747 2.749  1.00 31.01  ? 162 MET A N   1 
ATOM   1257 C  CA  . MET A 1 167 ? 25.807 13.860 3.592  1.00 20.79  ? 162 MET A CA  1 
ATOM   1258 C  C   . MET A 1 167 ? 25.328 12.423 3.448  1.00 26.02  ? 162 MET A C   1 
ATOM   1259 O  O   . MET A 1 167 ? 24.132 12.191 3.248  1.00 23.94  ? 162 MET A O   1 
ATOM   1260 C  CB  . MET A 1 167 ? 25.678 14.258 5.074  1.00 22.59  ? 162 MET A CB  1 
ATOM   1261 C  CG  . MET A 1 167 ? 26.055 15.692 5.342  1.00 54.57  ? 162 MET A CG  1 
ATOM   1262 S  SD  . MET A 1 167 ? 25.646 16.147 7.033  1.00 40.71  ? 162 MET A SD  1 
ATOM   1263 C  CE  . MET A 1 167 ? 27.185 16.553 7.593  1.00 34.89  ? 162 MET A CE  1 
ATOM   1264 N  N   . PRO A 1 168 ? 26.241 11.428 3.555  1.00 27.90  ? 163 PRO A N   1 
ATOM   1265 C  CA  . PRO A 1 168 ? 25.837 10.024 3.591  1.00 32.86  ? 163 PRO A CA  1 
ATOM   1266 C  C   . PRO A 1 168 ? 24.987 9.751  4.824  1.00 27.17  ? 163 PRO A C   1 
ATOM   1267 O  O   . PRO A 1 168 ? 25.092 10.464 5.824  1.00 25.34  ? 163 PRO A O   1 
ATOM   1268 C  CB  . PRO A 1 168 ? 27.163 9.255  3.616  1.00 35.89  ? 163 PRO A CB  1 
ATOM   1269 C  CG  . PRO A 1 168 ? 28.163 10.251 4.147  1.00 31.13  ? 163 PRO A CG  1 
ATOM   1270 C  CD  . PRO A 1 168 ? 27.701 11.592 3.635  1.00 36.69  ? 163 PRO A CD  1 
ATOM   1271 N  N   . PRO A 1 169 ? 24.144 8.698  4.777  1.00 22.37  ? 164 PRO A N   1 
ATOM   1272 C  CA  . PRO A 1 169 ? 23.231 8.356  5.868  1.00 21.35  ? 164 PRO A CA  1 
ATOM   1273 C  C   . PRO A 1 169 ? 23.902 7.915  7.170  1.00 20.59  ? 164 PRO A C   1 
ATOM   1274 O  O   . PRO A 1 169 ? 23.261 7.932  8.222  1.00 28.36  ? 164 PRO A O   1 
ATOM   1275 C  CB  . PRO A 1 169 ? 22.379 7.219  5.248  1.00 24.10  ? 164 PRO A CB  1 
ATOM   1276 C  CG  . PRO A 1 169 ? 22.658 7.223  3.818  1.00 37.80  ? 164 PRO A CG  1 
ATOM   1277 C  CD  . PRO A 1 169 ? 24.024 7.756  3.647  1.00 35.46  ? 164 PRO A CD  1 
ATOM   1278 N  N   . THR A 1 170 ? 25.197 7.571  7.109  1.00 28.12  ? 165 THR A N   1 
ATOM   1279 C  CA  . THR A 1 170 ? 25.963 7.237  8.304  1.00 24.90  ? 165 THR A CA  1 
ATOM   1280 C  C   . THR A 1 170 ? 26.778 8.396  8.872  1.00 22.99  ? 165 THR A C   1 
ATOM   1281 O  O   . THR A 1 170 ? 27.435 8.244  9.896  1.00 22.93  ? 165 THR A O   1 
ATOM   1282 C  CB  . THR A 1 170 ? 26.942 6.103  8.023  1.00 24.55  ? 165 THR A CB  1 
ATOM   1283 O  OG1 . THR A 1 170 ? 27.802 6.496  6.952  1.00 23.46  ? 165 THR A OG1 1 
ATOM   1284 C  CG2 . THR A 1 170 ? 26.241 4.826  7.704  1.00 24.82  ? 165 THR A CG2 1 
ATOM   1285 N  N   . ASN A 1 171 ? 26.744 9.557  8.217  1.00 22.97  ? 166 ASN A N   1 
ATOM   1286 C  CA  . ASN A 1 171 ? 27.529 10.676 8.714  1.00 25.06  ? 166 ASN A CA  1 
ATOM   1287 C  C   . ASN A 1 171 ? 27.126 10.985 10.155 1.00 24.10  ? 166 ASN A C   1 
ATOM   1288 O  O   . ASN A 1 171 ? 25.940 11.083 10.464 1.00 25.18  ? 166 ASN A O   1 
ATOM   1289 C  CB  . ASN A 1 171 ? 27.366 11.894 7.830  1.00 23.03  ? 166 ASN A CB  1 
ATOM   1290 C  CG  . ASN A 1 171 ? 28.126 13.095 8.348  1.00 21.70  ? 166 ASN A CG  1 
ATOM   1291 O  OD1 . ASN A 1 171 ? 27.675 13.797 9.272  1.00 28.21  ? 166 ASN A OD1 1 
ATOM   1292 N  ND2 . ASN A 1 171 ? 29.281 13.366 7.748  1.00 26.10  ? 166 ASN A ND2 1 
ATOM   1293 N  N   . PRO A 1 172 ? 28.095 11.163 11.085 1.00 27.87  ? 167 PRO A N   1 
ATOM   1294 C  CA  . PRO A 1 172 ? 27.769 11.380 12.495 1.00 26.87  ? 167 PRO A CA  1 
ATOM   1295 C  C   . PRO A 1 172 ? 26.974 12.647 12.815 1.00 21.37  ? 167 PRO A C   1 
ATOM   1296 O  O   . PRO A 1 172 ? 26.126 12.619 13.702 1.00 28.41  ? 167 PRO A O   1 
ATOM   1297 C  CB  . PRO A 1 172 ? 29.138 11.376 13.182 1.00 31.50  ? 167 PRO A CB  1 
ATOM   1298 C  CG  . PRO A 1 172 ? 30.139 11.635 12.113 1.00 52.94  ? 167 PRO A CG  1 
ATOM   1299 C  CD  . PRO A 1 172 ? 29.545 11.133 10.828 1.00 26.05  ? 167 PRO A CD  1 
ATOM   1300 N  N   . ILE A 1 173 ? 27.235 13.735 12.086 1.00 21.75  ? 168 ILE A N   1 
ATOM   1301 C  CA  . ILE A 1 173 ? 26.444 14.952 12.221 1.00 25.98  ? 168 ILE A CA  1 
ATOM   1302 C  C   . ILE A 1 173 ? 25.008 14.705 11.765 1.00 20.74  ? 168 ILE A C   1 
ATOM   1303 O  O   . ILE A 1 173 ? 24.061 15.071 12.452 1.00 25.72  ? 168 ILE A O   1 
ATOM   1304 C  CB  . ILE A 1 173 ? 27.080 16.127 11.468 1.00 26.60  ? 168 ILE A CB  1 
ATOM   1305 C  CG1 . ILE A 1 173 ? 28.479 16.430 11.982 1.00 28.69  ? 168 ILE A CG1 1 
ATOM   1306 C  CG2 . ILE A 1 173 ? 26.184 17.367 11.527 1.00 33.11  ? 168 ILE A CG2 1 
ATOM   1307 C  CD1 . ILE A 1 173 ? 29.312 17.250 11.066 1.00 31.30  ? 168 ILE A CD1 1 
ATOM   1308 N  N   . ARG A 1 174 ? 24.850 14.053 10.606 1.00 28.58  ? 169 ARG A N   1 
ATOM   1309 C  CA  . ARG A 1 174 ? 23.528 13.714 10.110 1.00 27.63  ? 169 ARG A CA  1 
ATOM   1310 C  C   . ARG A 1 174 ? 22.785 12.836 11.120 1.00 25.44  ? 169 ARG A C   1 
ATOM   1311 O  O   . ARG A 1 174 ? 21.622 13.085 11.428 1.00 22.89  ? 169 ARG A O   1 
ATOM   1312 C  CB  . ARG A 1 174 ? 23.635 13.051 8.717  1.00 21.31  ? 169 ARG A CB  1 
ATOM   1313 C  CG  . ARG A 1 174 ? 22.308 12.629 8.131  1.00 22.38  ? 169 ARG A CG  1 
ATOM   1314 C  CD  . ARG A 1 174 ? 22.408 12.232 6.674  1.00 20.99  ? 169 ARG A CD  1 
ATOM   1315 N  NE  . ARG A 1 174 ? 21.182 11.574 6.234  1.00 26.18  ? 169 ARG A NE  1 
ATOM   1316 C  CZ  . ARG A 1 174 ? 20.947 11.150 5.002  1.00 28.51  ? 169 ARG A CZ  1 
ATOM   1317 N  NH1 . ARG A 1 174 ? 21.845 11.277 4.038  1.00 21.39  ? 169 ARG A NH1 1 
ATOM   1318 N  NH2 . ARG A 1 174 ? 19.779 10.580 4.730  1.00 22.72  ? 169 ARG A NH2 1 
ATOM   1319 N  N   . LEU A 1 175 ? 23.470 11.824 11.660 1.00 20.14  ? 170 LEU A N   1 
ATOM   1320 C  CA  . LEU A 1 175 ? 22.857 10.912 12.609 1.00 23.55  ? 170 LEU A CA  1 
ATOM   1321 C  C   . LEU A 1 175 ? 22.538 11.604 13.935 1.00 20.25  ? 170 LEU A C   1 
ATOM   1322 O  O   . LEU A 1 175 ? 21.447 11.434 14.476 1.00 22.03  ? 170 LEU A O   1 
ATOM   1323 C  CB  . LEU A 1 175 ? 23.806 9.745  12.864 1.00 24.99  ? 170 LEU A CB  1 
ATOM   1324 C  CG  . LEU A 1 175 ? 24.023 8.762  11.742 1.00 26.93  ? 170 LEU A CG  1 
ATOM   1325 C  CD1 . LEU A 1 175 ? 25.079 7.739  12.177 1.00 27.49  ? 170 LEU A CD1 1 
ATOM   1326 C  CD2 . LEU A 1 175 ? 22.717 8.118  11.331 1.00 28.01  ? 170 LEU A CD2 1 
ATOM   1327 N  N   . GLY A 1 176 ? 23.504 12.381 14.442 1.00 23.62  ? 171 GLY A N   1 
ATOM   1328 C  CA  . GLY A 1 176 ? 23.333 13.113 15.690 1.00 28.30  ? 171 GLY A CA  1 
ATOM   1329 C  C   . GLY A 1 176 ? 22.179 14.110 15.615 1.00 29.43  ? 171 GLY A C   1 
ATOM   1330 O  O   . GLY A 1 176 ? 21.367 14.193 16.531 1.00 22.86  ? 171 GLY A O   1 
ATOM   1331 N  N   . LEU A 1 177 ? 22.092 14.827 14.487 1.00 28.55  ? 172 LEU A N   1 
ATOM   1332 C  CA  . LEU A 1 177 ? 20.981 15.723 14.220 1.00 23.85  ? 172 LEU A CA  1 
ATOM   1333 C  C   . LEU A 1 177 ? 19.635 15.003 14.236 1.00 27.38  ? 172 LEU A C   1 
ATOM   1334 O  O   . LEU A 1 177 ? 18.698 15.458 14.886 1.00 24.54  ? 172 LEU A O   1 
ATOM   1335 C  CB  . LEU A 1 177 ? 21.207 16.421 12.870 1.00 22.69  ? 172 LEU A CB  1 
ATOM   1336 C  CG  . LEU A 1 177 ? 19.972 17.054 12.264 1.00 26.94  ? 172 LEU A CG  1 
ATOM   1337 C  CD1 . LEU A 1 177 ? 19.455 18.195 13.155 1.00 30.66  ? 172 LEU A CD1 1 
ATOM   1338 C  CD2 . LEU A 1 177 ? 20.253 17.533 10.869 1.00 30.80  ? 172 LEU A CD2 1 
ATOM   1339 N  N   . ALA A 1 178 ? 19.536 13.882 13.511 1.00 28.41  ? 173 ALA A N   1 
ATOM   1340 C  CA  . ALA A 1 178 ? 18.294 13.126 13.450 1.00 29.11  ? 173 ALA A CA  1 
ATOM   1341 C  C   . ALA A 1 178 ? 17.879 12.593 14.822 1.00 24.22  ? 173 ALA A C   1 
ATOM   1342 O  O   . ALA A 1 178 ? 16.701 12.628 15.163 1.00 26.13  ? 173 ALA A O   1 
ATOM   1343 C  CB  . ALA A 1 178 ? 18.421 11.985 12.464 1.00 24.63  ? 173 ALA A CB  1 
ATOM   1344 N  N   . LEU A 1 179 ? 18.847 12.071 15.585 1.00 21.72  ? 174 LEU A N   1 
ATOM   1345 C  CA  . LEU A 1 179 ? 18.614 11.679 16.971 1.00 28.92  ? 174 LEU A CA  1 
ATOM   1346 C  C   . LEU A 1 179 ? 18.018 12.820 17.794 1.00 23.34  ? 174 LEU A C   1 
ATOM   1347 O  O   . LEU A 1 179 ? 16.994 12.649 18.449 1.00 26.73  ? 174 LEU A O   1 
ATOM   1348 C  CB  . LEU A 1 179 ? 19.928 11.218 17.630 1.00 25.77  ? 174 LEU A CB  1 
ATOM   1349 C  CG  . LEU A 1 179 ? 19.849 10.694 19.086 1.00 22.21  ? 174 LEU A CG  1 
ATOM   1350 C  CD1 . LEU A 1 179 ? 18.928 9.495  19.196 1.00 22.95  ? 174 LEU A CD1 1 
ATOM   1351 C  CD2 . LEU A 1 179 ? 21.207 10.349 19.580 1.00 28.89  ? 174 LEU A CD2 1 
ATOM   1352 N  N   . ASN A 1 180 ? 18.672 13.985 17.767 1.00 23.32  ? 175 ASN A N   1 
ATOM   1353 C  CA  . ASN A 1 180 ? 18.221 15.117 18.562 1.00 28.05  ? 175 ASN A CA  1 
ATOM   1354 C  C   . ASN A 1 180 ? 16.873 15.674 18.107 1.00 25.75  ? 175 ASN A C   1 
ATOM   1355 O  O   . ASN A 1 180 ? 16.049 16.066 18.933 1.00 27.12  ? 175 ASN A O   1 
ATOM   1356 C  CB  . ASN A 1 180 ? 19.287 16.203 18.591 1.00 24.74  ? 175 ASN A CB  1 
ATOM   1357 C  CG  . ASN A 1 180 ? 20.459 15.823 19.454 1.00 25.42  ? 175 ASN A CG  1 
ATOM   1358 O  OD1 . ASN A 1 180 ? 20.598 14.660 19.861 1.00 28.81  ? 175 ASN A OD1 1 
ATOM   1359 N  ND2 . ASN A 1 180 ? 21.337 16.780 19.765 1.00 24.50  ? 175 ASN A ND2 1 
ATOM   1360 N  N   . PHE A 1 181 ? 16.622 15.670 16.794 1.00 23.27  ? 176 PHE A N   1 
ATOM   1361 C  CA  . PHE A 1 181 ? 15.322 16.067 16.287 1.00 23.30  ? 176 PHE A CA  1 
ATOM   1362 C  C   . PHE A 1 181 ? 14.228 15.094 16.728 1.00 25.80  ? 176 PHE A C   1 
ATOM   1363 O  O   . PHE A 1 181 ? 13.120 15.519 17.056 1.00 24.77  ? 176 PHE A O   1 
ATOM   1364 C  CB  . PHE A 1 181 ? 15.360 16.184 14.748 1.00 35.69  ? 176 PHE A CB  1 
ATOM   1365 C  CG  . PHE A 1 181 ? 14.286 17.025 14.095 1.00 29.41  ? 176 PHE A CG  1 
ATOM   1366 C  CD1 . PHE A 1 181 ? 13.523 17.913 14.833 1.00 27.83  ? 176 PHE A CD1 1 
ATOM   1367 C  CD2 . PHE A 1 181 ? 14.040 16.928 12.735 1.00 26.52  ? 176 PHE A CD2 1 
ATOM   1368 C  CE1 . PHE A 1 181 ? 12.547 18.696 14.222 1.00 26.21  ? 176 PHE A CE1 1 
ATOM   1369 C  CE2 . PHE A 1 181 ? 13.060 17.709 12.129 1.00 25.98  ? 176 PHE A CE2 1 
ATOM   1370 C  CZ  . PHE A 1 181 ? 12.319 18.584 12.870 1.00 32.44  ? 176 PHE A CZ  1 
ATOM   1371 N  N   . SER A 1 182 ? 14.528 13.787 16.746 1.00 28.87  ? 177 SER A N   1 
ATOM   1372 C  CA  . SER A 1 182 ? 13.536 12.821 17.199 1.00 24.67  ? 177 SER A CA  1 
ATOM   1373 C  C   . SER A 1 182 ? 13.218 13.053 18.681 1.00 24.71  ? 177 SER A C   1 
ATOM   1374 O  O   . SER A 1 182 ? 12.061 12.967 19.086 1.00 33.73  ? 177 SER A O   1 
ATOM   1375 C  CB  . SER A 1 182 ? 13.954 11.374 16.923 1.00 30.13  ? 177 SER A CB  1 
ATOM   1376 O  OG  . SER A 1 182 ? 15.024 10.911 17.726 1.00 35.10  ? 177 SER A OG  1 
ATOM   1377 N  N   . VAL A 1 183 ? 14.247 13.382 19.473 1.00 33.31  ? 178 VAL A N   1 
ATOM   1378 C  CA  . VAL A 1 183 ? 14.062 13.717 20.879 1.00 23.42  ? 178 VAL A CA  1 
ATOM   1379 C  C   . VAL A 1 183 ? 13.161 14.944 21.001 1.00 29.85  ? 178 VAL A C   1 
ATOM   1380 O  O   . VAL A 1 183 ? 12.221 14.934 21.792 1.00 29.45  ? 178 VAL A O   1 
ATOM   1381 C  CB  . VAL A 1 183 ? 15.398 13.938 21.608 1.00 30.72  ? 178 VAL A CB  1 
ATOM   1382 C  CG1 . VAL A 1 183 ? 15.171 14.508 23.016 1.00 33.76  ? 178 VAL A CG1 1 
ATOM   1383 C  CG2 . VAL A 1 183 ? 16.216 12.657 21.661 1.00 25.94  ? 178 VAL A CG2 1 
ATOM   1384 N  N   . PHE A 1 184 ? 13.453 15.989 20.212 1.00 27.22  ? 179 PHE A N   1 
ATOM   1385 C  CA  . PHE A 1 184 ? 12.578 17.150 20.113 1.00 29.69  ? 179 PHE A CA  1 
ATOM   1386 C  C   . PHE A 1 184 ? 11.123 16.737 19.885 1.00 29.40  ? 179 PHE A C   1 
ATOM   1387 O  O   . PHE A 1 184 ? 10.232 17.160 20.618 1.00 24.84  ? 179 PHE A O   1 
ATOM   1388 C  CB  . PHE A 1 184 ? 13.054 18.111 18.995 1.00 27.44  ? 179 PHE A CB  1 
ATOM   1389 C  CG  . PHE A 1 184 ? 12.100 19.243 18.690 1.00 24.97  ? 179 PHE A CG  1 
ATOM   1390 C  CD1 . PHE A 1 184 ? 12.082 20.384 19.467 1.00 28.74  ? 179 PHE A CD1 1 
ATOM   1391 C  CD2 . PHE A 1 184 ? 11.206 19.148 17.648 1.00 26.67  ? 179 PHE A CD2 1 
ATOM   1392 C  CE1 . PHE A 1 184 ? 11.199 21.416 19.189 1.00 31.67  ? 179 PHE A CE1 1 
ATOM   1393 C  CE2 . PHE A 1 184 ? 10.319 20.179 17.377 1.00 32.81  ? 179 PHE A CE2 1 
ATOM   1394 C  CZ  . PHE A 1 184 ? 10.321 21.306 18.150 1.00 33.73  ? 179 PHE A CZ  1 
ATOM   1395 N  N   . HIS A 1 185 ? 10.879 15.906 18.863 1.00 26.15  ? 180 HIS A N   1 
ATOM   1396 C  CA  . HIS A 1 185 ? 9.527  15.495 18.517 1.00 34.19  ? 180 HIS A CA  1 
ATOM   1397 C  C   . HIS A 1 185 ? 8.852  14.809 19.705 1.00 25.86  ? 180 HIS A C   1 
ATOM   1398 O  O   . HIS A 1 185 ? 7.695  15.093 20.019 1.00 28.45  ? 180 HIS A O   1 
ATOM   1399 C  CB  . HIS A 1 185 ? 9.521  14.553 17.308 1.00 31.62  ? 180 HIS A CB  1 
ATOM   1400 C  CG  . HIS A 1 185 ? 9.778  15.195 15.983 1.00 24.73  ? 180 HIS A CG  1 
ATOM   1401 N  ND1 . HIS A 1 185 ? 9.117  16.321 15.543 1.00 25.28  ? 180 HIS A ND1 1 
ATOM   1402 C  CD2 . HIS A 1 185 ? 10.602 14.830 14.985 1.00 31.41  ? 180 HIS A CD2 1 
ATOM   1403 C  CE1 . HIS A 1 185 ? 9.536  16.622 14.322 1.00 38.73  ? 180 HIS A CE1 1 
ATOM   1404 N  NE2 . HIS A 1 185 ? 10.436 15.729 13.961 1.00 23.64  ? 180 HIS A NE2 1 
ATOM   1405 N  N   . TYR A 1 186 ? 9.580  13.895 20.352 1.00 29.53  ? 181 TYR A N   1 
ATOM   1406 C  CA  . TYR A 1 186 ? 9.026  13.117 21.446 1.00 26.21  ? 181 TYR A CA  1 
ATOM   1407 C  C   . TYR A 1 186 ? 8.800  13.962 22.700 1.00 29.13  ? 181 TYR A C   1 
ATOM   1408 O  O   . TYR A 1 186 ? 7.705  13.961 23.253 1.00 33.91  ? 181 TYR A O   1 
ATOM   1409 C  CB  . TYR A 1 186 ? 9.935  11.920 21.766 1.00 24.04  ? 181 TYR A CB  1 
ATOM   1410 C  CG  . TYR A 1 186 ? 9.253  10.870 22.623 1.00 38.24  ? 181 TYR A CG  1 
ATOM   1411 C  CD1 . TYR A 1 186 ? 9.250  10.967 24.010 1.00 47.58  ? 181 TYR A CD1 1 
ATOM   1412 C  CD2 . TYR A 1 186 ? 8.577  9.805  22.045 1.00 52.59  ? 181 TYR A CD2 1 
ATOM   1413 C  CE1 . TYR A 1 186 ? 8.616  10.011 24.800 1.00 32.95  ? 181 TYR A CE1 1 
ATOM   1414 C  CE2 . TYR A 1 186 ? 7.934  8.848  22.823 1.00 45.16  ? 181 TYR A CE2 1 
ATOM   1415 C  CZ  . TYR A 1 186 ? 7.958  8.953  24.200 1.00 41.65  ? 181 TYR A CZ  1 
ATOM   1416 O  OH  . TYR A 1 186 ? 7.324  8.002  24.958 1.00 47.82  ? 181 TYR A OH  1 
ATOM   1417 N  N   . GLU A 1 187 ? 9.837  14.700 23.116 1.00 32.66  ? 182 GLU A N   1 
ATOM   1418 C  CA  . GLU A 1 187 ? 9.860  15.339 24.422 1.00 40.76  ? 182 GLU A CA  1 
ATOM   1419 C  C   . GLU A 1 187 ? 9.283  16.754 24.451 1.00 40.13  ? 182 GLU A C   1 
ATOM   1420 O  O   . GLU A 1 187 ? 8.665  17.139 25.442 1.00 32.48  ? 182 GLU A O   1 
ATOM   1421 C  CB  . GLU A 1 187 ? 11.306 15.352 24.954 1.00 30.36  ? 182 GLU A CB  1 
ATOM   1422 C  CG  . GLU A 1 187 ? 11.858 13.960 25.240 1.00 36.87  ? 182 GLU A CG  1 
ATOM   1423 C  CD  . GLU A 1 187 ? 11.253 13.226 26.427 1.00 54.11  ? 182 GLU A CD  1 
ATOM   1424 O  OE1 . GLU A 1 187 ? 10.472 13.848 27.182 1.00 57.50  ? 182 GLU A OE1 1 
ATOM   1425 O  OE2 . GLU A 1 187 ? 11.559 12.023 26.598 1.00 41.87  ? 182 GLU A OE2 1 
ATOM   1426 N  N   . ILE A 1 188 ? 9.500  17.524 23.376 1.00 31.36  ? 183 ILE A N   1 
ATOM   1427 C  CA  . ILE A 1 188 ? 9.115  18.926 23.330 1.00 34.09  ? 183 ILE A CA  1 
ATOM   1428 C  C   . ILE A 1 188 ? 7.813  19.145 22.561 1.00 34.51  ? 183 ILE A C   1 
ATOM   1429 O  O   . ILE A 1 188 ? 6.913  19.832 23.039 1.00 28.60  ? 183 ILE A O   1 
ATOM   1430 C  CB  . ILE A 1 188 ? 10.263 19.776 22.709 1.00 27.71  ? 183 ILE A CB  1 
ATOM   1431 C  CG1 . ILE A 1 188 ? 11.597 19.580 23.443 1.00 36.39  ? 183 ILE A CG1 1 
ATOM   1432 C  CG2 . ILE A 1 188 ? 9.875  21.249 22.622 1.00 31.53  ? 183 ILE A CG2 1 
ATOM   1433 C  CD1 . ILE A 1 188 ? 11.574 19.883 24.902 1.00 35.61  ? 183 ILE A CD1 1 
ATOM   1434 N  N   . ALA A 1 189 ? 7.737  18.574 21.354 1.00 35.76  ? 184 ALA A N   1 
ATOM   1435 C  CA  . ALA A 1 189 ? 6.616  18.803 20.455 1.00 36.41  ? 184 ALA A CA  1 
ATOM   1436 C  C   . ALA A 1 189 ? 5.442  17.873 20.739 1.00 39.18  ? 184 ALA A C   1 
ATOM   1437 O  O   . ALA A 1 189 ? 4.383  18.037 20.141 1.00 37.34  ? 184 ALA A O   1 
ATOM   1438 C  CB  . ALA A 1 189 ? 7.054  18.635 19.002 1.00 36.26  ? 184 ALA A CB  1 
ATOM   1439 N  N   . ASN A 1 190 ? 5.653  16.889 21.625 1.00 31.07  ? 185 ASN A N   1 
ATOM   1440 C  CA  . ASN A 1 190 ? 4.616  15.940 21.997 1.00 44.80  ? 185 ASN A CA  1 
ATOM   1441 C  C   . ASN A 1 190 ? 4.082  15.187 20.775 1.00 38.14  ? 185 ASN A C   1 
ATOM   1442 O  O   . ASN A 1 190 ? 2.874  15.014 20.617 1.00 36.21  ? 185 ASN A O   1 
ATOM   1443 C  CB  . ASN A 1 190 ? 3.493  16.681 22.740 1.00 55.37  ? 185 ASN A CB  1 
ATOM   1444 C  CG  . ASN A 1 190 ? 2.586  15.776 23.520 1.00 91.43  ? 185 ASN A CG  1 
ATOM   1445 O  OD1 . ASN A 1 190 ? 2.941  14.639 23.854 1.00 60.78  ? 185 ASN A OD1 1 
ATOM   1446 N  ND2 . ASN A 1 190 ? 1.397  16.270 23.838 1.00 73.56  ? 185 ASN A ND2 1 
ATOM   1447 N  N   . SER A 1 191 ? 5.001  14.731 19.914 1.00 48.34  ? 186 SER A N   1 
ATOM   1448 C  CA  . SER A 1 191 ? 4.659  14.065 18.665 1.00 28.21  ? 186 SER A CA  1 
ATOM   1449 C  C   . SER A 1 191 ? 5.383  12.724 18.590 1.00 27.74  ? 186 SER A C   1 
ATOM   1450 O  O   . SER A 1 191 ? 6.358  12.593 17.851 1.00 32.23  ? 186 SER A O   1 
ATOM   1451 C  CB  . SER A 1 191 ? 5.044  14.944 17.479 1.00 34.91  ? 186 SER A CB  1 
ATOM   1452 O  OG  . SER A 1 191 ? 4.313  16.156 17.487 1.00 47.43  ? 186 SER A OG  1 
ATOM   1453 N  N   . PRO A 1 192 ? 4.936  11.690 19.342 1.00 33.71  ? 187 PRO A N   1 
ATOM   1454 C  CA  . PRO A 1 192 ? 5.703  10.449 19.474 1.00 43.29  ? 187 PRO A CA  1 
ATOM   1455 C  C   . PRO A 1 192 ? 5.825  9.679  18.161 1.00 36.12  ? 187 PRO A C   1 
ATOM   1456 O  O   . PRO A 1 192 ? 6.856  9.060  17.910 1.00 33.86  ? 187 PRO A O   1 
ATOM   1457 C  CB  . PRO A 1 192 ? 4.922  9.646  20.530 1.00 40.12  ? 187 PRO A CB  1 
ATOM   1458 C  CG  . PRO A 1 192 ? 3.934  10.630 21.142 1.00 63.49  ? 187 PRO A CG  1 
ATOM   1459 C  CD  . PRO A 1 192 ? 3.655  11.634 20.066 1.00 35.68  ? 187 PRO A CD  1 
ATOM   1460 N  N   . GLU A 1 193 ? 4.760  9.727  17.347 1.00 48.38  ? 188 GLU A N   1 
ATOM   1461 C  CA  . GLU A 1 193 ? 4.725  9.075  16.045 1.00 57.94  ? 188 GLU A CA  1 
ATOM   1462 C  C   . GLU A 1 193 ? 5.796  9.620  15.097 1.00 39.60  ? 188 GLU A C   1 
ATOM   1463 O  O   . GLU A 1 193 ? 6.467  8.845  14.417 1.00 29.02  ? 188 GLU A O   1 
ATOM   1464 C  CB  . GLU A 1 193 ? 3.302  9.173  15.412 1.00 45.10  ? 188 GLU A CB  1 
ATOM   1465 C  CG  . GLU A 1 193 ? 2.823  10.568 15.000 1.00 89.25  ? 188 GLU A CG  1 
ATOM   1466 C  CD  . GLU A 1 193 ? 2.587  11.575 16.117 1.00 161.19 ? 188 GLU A CD  1 
ATOM   1467 O  OE1 . GLU A 1 193 ? 1.776  11.279 17.024 1.00 57.05  ? 188 GLU A OE1 1 
ATOM   1468 O  OE2 . GLU A 1 193 ? 3.203  12.666 16.081 1.00 42.27  ? 188 GLU A OE2 1 
ATOM   1469 N  N   . GLU A 1 194 ? 5.973  10.950 15.076 1.00 47.99  ? 189 GLU A N   1 
ATOM   1470 C  CA  . GLU A 1 194 ? 7.000  11.580 14.258 1.00 33.42  ? 189 GLU A CA  1 
ATOM   1471 C  C   . GLU A 1 194 ? 8.400  11.279 14.786 1.00 35.04  ? 189 GLU A C   1 
ATOM   1472 O  O   . GLU A 1 194 ? 9.335  11.107 14.007 1.00 33.05  ? 189 GLU A O   1 
ATOM   1473 C  CB  . GLU A 1 194 ? 6.804  13.103 14.186 1.00 35.77  ? 189 GLU A CB  1 
ATOM   1474 C  CG  . GLU A 1 194 ? 5.597  13.536 13.374 1.00 67.01  ? 189 GLU A CG  1 
ATOM   1475 C  CD  . GLU A 1 194 ? 5.435  15.039 13.273 1.00 60.99  ? 189 GLU A CD  1 
ATOM   1476 O  OE1 . GLU A 1 194 ? 6.347  15.702 12.727 1.00 62.04  ? 189 GLU A OE1 1 
ATOM   1477 O  OE2 . GLU A 1 194 ? 4.398  15.556 13.747 1.00 76.83  ? 189 GLU A OE2 1 
ATOM   1478 N  N   . ALA A 1 195 ? 8.537  11.235 16.116 1.00 30.13  ? 190 ALA A N   1 
ATOM   1479 C  CA  . ALA A 1 195 ? 9.793  10.854 16.741 1.00 26.58  ? 190 ALA A CA  1 
ATOM   1480 C  C   . ALA A 1 195 ? 10.194 9.449  16.290 1.00 29.17  ? 190 ALA A C   1 
ATOM   1481 O  O   . ALA A 1 195 ? 11.306 9.244  15.814 1.00 28.34  ? 190 ALA A O   1 
ATOM   1482 C  CB  . ALA A 1 195 ? 9.678  10.923 18.259 1.00 35.26  ? 190 ALA A CB  1 
ATOM   1483 N  N   . ILE A 1 196 ? 9.264  8.497  16.433 1.00 33.72  ? 191 ILE A N   1 
ATOM   1484 C  CA  . ILE A 1 196 ? 9.503  7.102  16.094 1.00 49.06  ? 191 ILE A CA  1 
ATOM   1485 C  C   . ILE A 1 196 ? 9.827  6.919  14.612 1.00 29.55  ? 191 ILE A C   1 
ATOM   1486 O  O   . ILE A 1 196 ? 10.781 6.225  14.272 1.00 31.53  ? 191 ILE A O   1 
ATOM   1487 C  CB  . ILE A 1 196 ? 8.290  6.234  16.557 1.00 40.50  ? 191 ILE A CB  1 
ATOM   1488 C  CG1 . ILE A 1 196 ? 8.275  6.111  18.098 1.00 32.65  ? 191 ILE A CG1 1 
ATOM   1489 C  CG2 . ILE A 1 196 ? 8.275  4.850  15.892 1.00 36.76  ? 191 ILE A CG2 1 
ATOM   1490 C  CD1 . ILE A 1 196 ? 6.936  5.567  18.716 1.00 33.99  ? 191 ILE A CD1 1 
ATOM   1491 N  N   . SER A 1 197 ? 9.041  7.554  13.733 1.00 30.49  ? 192 SER A N   1 
ATOM   1492 C  CA  . SER A 1 197 ? 9.255  7.427  12.299 1.00 31.18  ? 192 SER A CA  1 
ATOM   1493 C  C   . SER A 1 197 ? 10.614 7.970  11.859 1.00 28.59  ? 192 SER A C   1 
ATOM   1494 O  O   . SER A 1 197 ? 11.306 7.345  11.055 1.00 26.72  ? 192 SER A O   1 
ATOM   1495 C  CB  . SER A 1 197 ? 8.140  8.116  11.514 1.00 40.76  ? 192 SER A CB  1 
ATOM   1496 O  OG  . SER A 1 197 ? 6.889  7.504  11.779 1.00 60.00  ? 192 SER A OG  1 
ATOM   1497 N  N   . LEU A 1 198 ? 10.992 9.137  12.390 1.00 31.54  ? 193 LEU A N   1 
ATOM   1498 C  CA  . LEU A 1 198 ? 12.298 9.704  12.101 1.00 24.27  ? 193 LEU A CA  1 
ATOM   1499 C  C   . LEU A 1 198 ? 13.410 8.776  12.597 1.00 27.56  ? 193 LEU A C   1 
ATOM   1500 O  O   . LEU A 1 198 ? 14.367 8.510  11.873 1.00 29.80  ? 193 LEU A O   1 
ATOM   1501 C  CB  . LEU A 1 198 ? 12.429 11.101 12.731 1.00 30.69  ? 193 LEU A CB  1 
ATOM   1502 C  CG  . LEU A 1 198 ? 13.759 11.814 12.512 1.00 25.77  ? 193 LEU A CG  1 
ATOM   1503 C  CD1 . LEU A 1 198 ? 14.069 11.966 11.046 1.00 36.52  ? 193 LEU A CD1 1 
ATOM   1504 C  CD2 . LEU A 1 198 ? 13.742 13.174 13.183 1.00 26.27  ? 193 LEU A CD2 1 
ATOM   1505 N  N   . ALA A 1 199 ? 13.272 8.267  13.827 1.00 24.48  ? 194 ALA A N   1 
ATOM   1506 C  CA  . ALA A 1 199 ? 14.321 7.458  14.427 1.00 19.87  ? 194 ALA A CA  1 
ATOM   1507 C  C   . ALA A 1 199 ? 14.507 6.152  13.653 1.00 18.19  ? 194 ALA A C   1 
ATOM   1508 O  O   . ALA A 1 199 ? 15.633 5.744  13.381 1.00 29.79  ? 194 ALA A O   1 
ATOM   1509 C  CB  . ALA A 1 199 ? 14.006 7.178  15.895 1.00 33.57  ? 194 ALA A CB  1 
ATOM   1510 N  N   . LYS A 1 200 ? 13.379 5.511  13.326 1.00 23.87  ? 195 LYS A N   1 
ATOM   1511 C  CA  . LYS A 1 200 ? 13.342 4.276  12.552 1.00 26.44  ? 195 LYS A CA  1 
ATOM   1512 C  C   . LYS A 1 200 ? 13.969 4.471  11.174 1.00 29.09  ? 195 LYS A C   1 
ATOM   1513 O  O   . LYS A 1 200 ? 14.872 3.728  10.783 1.00 27.00  ? 195 LYS A O   1 
ATOM   1514 C  CB  . LYS A 1 200 ? 11.866 3.832  12.452 1.00 26.50  ? 195 LYS A CB  1 
ATOM   1515 C  CG  . LYS A 1 200 ? 11.554 2.653  11.520 1.00 38.51  ? 195 LYS A CG  1 
ATOM   1516 C  CD  . LYS A 1 200 ? 11.814 1.302  12.158 1.00 60.25  ? 195 LYS A CD  1 
ATOM   1517 C  CE  . LYS A 1 200 ? 11.226 0.184  11.337 1.00 47.65  ? 195 LYS A CE  1 
ATOM   1518 N  NZ  . LYS A 1 200 ? 11.634 -1.138 11.857 1.00 66.28  ? 195 LYS A NZ  1 
ATOM   1519 N  N   . THR A 1 201 ? 13.475 5.486  10.453 1.00 27.03  ? 196 THR A N   1 
ATOM   1520 C  CA  . THR A 1 201 ? 13.977 5.836  9.138  1.00 28.01  ? 196 THR A CA  1 
ATOM   1521 C  C   . THR A 1 201 ? 15.471 6.139  9.158  1.00 29.76  ? 196 THR A C   1 
ATOM   1522 O  O   . THR A 1 201 ? 16.184 5.765  8.231  1.00 31.80  ? 196 THR A O   1 
ATOM   1523 C  CB  . THR A 1 201 ? 13.185 7.028  8.578  1.00 32.01  ? 196 THR A CB  1 
ATOM   1524 O  OG1 . THR A 1 201 ? 11.834 6.624  8.423  1.00 39.42  ? 196 THR A OG1 1 
ATOM   1525 C  CG2 . THR A 1 201 ? 13.723 7.527  7.251  1.00 47.77  ? 196 THR A CG2 1 
ATOM   1526 N  N   . THR A 1 202 ? 15.937 6.840  10.202 1.00 28.37  ? 197 THR A N   1 
ATOM   1527 C  CA  . THR A 1 202 ? 17.342 7.206  10.292 1.00 28.14  ? 197 THR A CA  1 
ATOM   1528 C  C   . THR A 1 202 ? 18.195 5.957  10.490 1.00 24.48  ? 197 THR A C   1 
ATOM   1529 O  O   . THR A 1 202 ? 19.218 5.782  9.822  1.00 24.26  ? 197 THR A O   1 
ATOM   1530 C  CB  . THR A 1 202 ? 17.589 8.239  11.400 1.00 23.25  ? 197 THR A CB  1 
ATOM   1531 O  OG1 . THR A 1 202 ? 16.721 9.347  11.184 1.00 26.08  ? 197 THR A OG1 1 
ATOM   1532 C  CG2 . THR A 1 202 ? 19.019 8.710  11.440 1.00 29.53  ? 197 THR A CG2 1 
ATOM   1533 N  N   . PHE A 1 203 ? 17.757 5.093  11.412 1.00 22.53  ? 198 PHE A N   1 
ATOM   1534 C  CA  . PHE A 1 203 ? 18.457 3.848  11.675 1.00 29.08  ? 198 PHE A CA  1 
ATOM   1535 C  C   . PHE A 1 203 ? 18.498 2.945  10.435 1.00 26.11  ? 198 PHE A C   1 
ATOM   1536 O  O   . PHE A 1 203 ? 19.565 2.485  10.029 1.00 23.49  ? 198 PHE A O   1 
ATOM   1537 C  CB  . PHE A 1 203 ? 17.806 3.129  12.876 1.00 27.75  ? 198 PHE A CB  1 
ATOM   1538 C  CG  . PHE A 1 203 ? 18.513 1.849  13.222 1.00 21.94  ? 198 PHE A CG  1 
ATOM   1539 C  CD1 . PHE A 1 203 ? 19.598 1.849  14.083 1.00 31.14  ? 198 PHE A CD1 1 
ATOM   1540 C  CD2 . PHE A 1 203 ? 18.129 0.649  12.643 1.00 22.80  ? 198 PHE A CD2 1 
ATOM   1541 C  CE1 . PHE A 1 203 ? 20.273 0.670  14.374 1.00 33.54  ? 198 PHE A CE1 1 
ATOM   1542 C  CE2 . PHE A 1 203 ? 18.799 -0.532 12.945 1.00 27.19  ? 198 PHE A CE2 1 
ATOM   1543 C  CZ  . PHE A 1 203 ? 19.873 -0.512 13.802 1.00 31.48  ? 198 PHE A CZ  1 
ATOM   1544 N  N   . ASP A 1 204 ? 17.333 2.713  9.818  1.00 24.32  ? 199 ASP A N   1 
ATOM   1545 C  CA  . ASP A 1 204 ? 17.226 1.777  8.709  1.00 28.03  ? 199 ASP A CA  1 
ATOM   1546 C  C   . ASP A 1 204 ? 18.037 2.221  7.489  1.00 20.52  ? 199 ASP A C   1 
ATOM   1547 O  O   . ASP A 1 204 ? 18.650 1.390  6.824  1.00 25.95  ? 199 ASP A O   1 
ATOM   1548 C  CB  . ASP A 1 204 ? 15.744 1.560  8.328  1.00 36.24  ? 199 ASP A CB  1 
ATOM   1549 C  CG  . ASP A 1 204 ? 14.936 0.760  9.348  1.00 24.50  ? 199 ASP A CG  1 
ATOM   1550 O  OD1 . ASP A 1 204 ? 15.550 0.127  10.226 1.00 21.84  ? 199 ASP A OD1 1 
ATOM   1551 O  OD2 . ASP A 1 204 ? 13.701 0.777  9.264  1.00 27.59  ? 199 ASP A OD2 1 
ATOM   1552 N  N   . GLU A 1 205 ? 18.056 3.529  7.221  1.00 26.91  ? 200 GLU A N   1 
ATOM   1553 C  CA  . GLU A 1 205 ? 18.777 4.058  6.074  1.00 45.08  ? 200 GLU A CA  1 
ATOM   1554 C  C   . GLU A 1 205 ? 20.288 4.046  6.302  1.00 21.61  ? 200 GLU A C   1 
ATOM   1555 O  O   . GLU A 1 205 ? 21.059 3.879  5.362  1.00 25.44  ? 200 GLU A O   1 
ATOM   1556 C  CB  . GLU A 1 205 ? 18.275 5.464  5.716  1.00 25.49  ? 200 GLU A CB  1 
ATOM   1557 C  CG  . GLU A 1 205 ? 16.868 5.455  5.126  1.00 35.41  ? 200 GLU A CG  1 
ATOM   1558 C  CD  . GLU A 1 205 ? 16.344 6.815  4.709  1.00 44.65  ? 200 GLU A CD  1 
ATOM   1559 O  OE1 . GLU A 1 205 ? 17.046 7.817  4.970  1.00 32.18  ? 200 GLU A OE1 1 
ATOM   1560 O  OE2 . GLU A 1 205 ? 15.240 6.886  4.122  1.00 38.30  ? 200 GLU A OE2 1 
ATOM   1561 N  N   . ALA A 1 206 ? 20.719 4.196  7.560  1.00 22.61  ? 201 ALA A N   1 
ATOM   1562 C  CA  . ALA A 1 206 ? 22.125 4.044  7.892  1.00 23.55  ? 201 ALA A CA  1 
ATOM   1563 C  C   . ALA A 1 206 ? 22.577 2.595  7.711  1.00 18.74  ? 201 ALA A C   1 
ATOM   1564 O  O   . ALA A 1 206 ? 23.673 2.360  7.220  1.00 26.09  ? 201 ALA A O   1 
ATOM   1565 C  CB  . ALA A 1 206 ? 22.404 4.525  9.320  1.00 28.45  ? 201 ALA A CB  1 
ATOM   1566 N  N   . MET A 1 207 ? 21.751 1.635  8.171  1.00 20.05  ? 202 MET A N   1 
ATOM   1567 C  CA  . MET A 1 207 ? 22.051 0.219  8.021  1.00 20.17  ? 202 MET A CA  1 
ATOM   1568 C  C   . MET A 1 207 ? 22.079 -0.149 6.542  1.00 24.89  ? 202 MET A C   1 
ATOM   1569 O  O   . MET A 1 207 ? 22.967 -0.870 6.099  1.00 20.84  ? 202 MET A O   1 
ATOM   1570 C  CB  . MET A 1 207 ? 21.003 -0.666 8.739  1.00 20.61  ? 202 MET A CB  1 
ATOM   1571 C  CG  . MET A 1 207 ? 21.165 -0.640 10.255 1.00 39.75  ? 202 MET A CG  1 
ATOM   1572 S  SD  . MET A 1 207 ? 22.660 -1.471 10.821 1.00 35.91  ? 202 MET A SD  1 
ATOM   1573 C  CE  . MET A 1 207 ? 22.352 -3.042 10.245 1.00 44.48  ? 202 MET A CE  1 
ATOM   1574 N  N   . ALA A 1 208 ? 21.087 0.343  5.793  1.00 20.88  ? 203 ALA A N   1 
ATOM   1575 C  CA  . ALA A 1 208 ? 21.005 0.057  4.369  1.00 25.86  ? 203 ALA A CA  1 
ATOM   1576 C  C   . ALA A 1 208 ? 22.245 0.555  3.630  1.00 28.06  ? 203 ALA A C   1 
ATOM   1577 O  O   . ALA A 1 208 ? 22.707 -0.087 2.694  1.00 23.37  ? 203 ALA A O   1 
ATOM   1578 C  CB  . ALA A 1 208 ? 19.743 0.663  3.764  1.00 21.74  ? 203 ALA A CB  1 
ATOM   1579 N  N   . ASP A 1 209 ? 22.799 1.690  4.059  1.00 16.86  ? 204 ASP A N   1 
ATOM   1580 C  CA  . ASP A 1 209 ? 24.018 2.206  3.452  1.00 22.98  ? 204 ASP A CA  1 
ATOM   1581 C  C   . ASP A 1 209 ? 25.200 2.172  4.422  1.00 21.79  ? 204 ASP A C   1 
ATOM   1582 O  O   . ASP A 1 209 ? 25.995 3.113  4.490  1.00 23.57  ? 204 ASP A O   1 
ATOM   1583 C  CB  . ASP A 1 209 ? 23.742 3.593  2.860  1.00 26.13  ? 204 ASP A CB  1 
ATOM   1584 C  CG  . ASP A 1 209 ? 23.032 3.585  1.501  1.00 23.95  ? 204 ASP A CG  1 
ATOM   1585 O  OD1 . ASP A 1 209 ? 23.127 2.562  0.772  1.00 16.47  ? 204 ASP A OD1 1 
ATOM   1586 O  OD2 . ASP A 1 209 ? 22.348 4.563  1.190  1.00 26.90  ? 204 ASP A OD2 1 
ATOM   1587 N  N   . LEU A 1 210 ? 25.332 1.037  5.137  1.00 21.63  ? 205 LEU A N   1 
ATOM   1588 C  CA  . LEU A 1 210 ? 26.362 0.875  6.156  1.00 18.23  ? 205 LEU A CA  1 
ATOM   1589 C  C   . LEU A 1 210 ? 27.764 1.036  5.573  1.00 21.88  ? 205 LEU A C   1 
ATOM   1590 O  O   . LEU A 1 210 ? 28.670 1.532  6.236  1.00 21.90  ? 205 LEU A O   1 
ATOM   1591 C  CB  . LEU A 1 210 ? 26.228 -0.515 6.813  1.00 22.80  ? 205 LEU A CB  1 
ATOM   1592 C  CG  . LEU A 1 210 ? 27.090 -0.758 8.031  1.00 28.19  ? 205 LEU A CG  1 
ATOM   1593 C  CD1 . LEU A 1 210 ? 26.654 0.144  9.177  1.00 26.25  ? 205 LEU A CD1 1 
ATOM   1594 C  CD2 . LEU A 1 210 ? 27.035 -2.232 8.444  1.00 31.70  ? 205 LEU A CD2 1 
ATOM   1595 N  N   . HIS A 1 211 ? 27.912 0.662  4.296  1.00 22.48  ? 206 HIS A N   1 
ATOM   1596 C  CA  . HIS A 1 211 ? 29.175 0.769  3.581  1.00 28.74  ? 206 HIS A CA  1 
ATOM   1597 C  C   . HIS A 1 211 ? 29.730 2.201  3.532  1.00 24.59  ? 206 HIS A C   1 
ATOM   1598 O  O   . HIS A 1 211 ? 30.884 2.373  3.153  1.00 22.50  ? 206 HIS A O   1 
ATOM   1599 C  CB  . HIS A 1 211 ? 29.005 0.230  2.155  1.00 26.91  ? 206 HIS A CB  1 
ATOM   1600 C  CG  . HIS A 1 211 ? 28.167 1.105  1.281  1.00 24.94  ? 206 HIS A CG  1 
ATOM   1601 N  ND1 . HIS A 1 211 ? 26.795 1.006  1.221  1.00 28.49  ? 206 HIS A ND1 1 
ATOM   1602 C  CD2 . HIS A 1 211 ? 28.511 2.079  0.410  1.00 26.62  ? 206 HIS A CD2 1 
ATOM   1603 C  CE1 . HIS A 1 211 ? 26.332 1.902  0.353  1.00 27.66  ? 206 HIS A CE1 1 
ATOM   1604 N  NE2 . HIS A 1 211 ? 27.357 2.565  -0.150 1.00 24.17  ? 206 HIS A NE2 1 
ATOM   1605 N  N   . THR A 1 212 ? 28.915 3.223  3.836  1.00 20.61  ? 207 THR A N   1 
ATOM   1606 C  CA  . THR A 1 212 ? 29.371 4.611  3.823  1.00 23.24  ? 207 THR A CA  1 
ATOM   1607 C  C   . THR A 1 212 ? 30.061 5.079  5.112  1.00 30.04  ? 207 THR A C   1 
ATOM   1608 O  O   . THR A 1 212 ? 30.506 6.226  5.210  1.00 24.09  ? 207 THR A O   1 
ATOM   1609 C  CB  . THR A 1 212 ? 28.190 5.559  3.481  1.00 24.07  ? 207 THR A CB  1 
ATOM   1610 O  OG1 . THR A 1 212 ? 27.199 5.533  4.525  1.00 20.30  ? 207 THR A OG1 1 
ATOM   1611 C  CG2 . THR A 1 212 ? 27.522 5.182  2.137  1.00 31.22  ? 207 THR A CG2 1 
ATOM   1612 N  N   . LEU A 1 213 ? 30.174 4.189  6.103  1.00 25.16  ? 208 LEU A N   1 
ATOM   1613 C  CA  . LEU A 1 213 ? 30.915 4.506  7.314  1.00 25.56  ? 208 LEU A CA  1 
ATOM   1614 C  C   . LEU A 1 213 ? 32.306 5.035  6.975  1.00 26.16  ? 208 LEU A C   1 
ATOM   1615 O  O   . LEU A 1 213 ? 32.987 4.504  6.095  1.00 23.60  ? 208 LEU A O   1 
ATOM   1616 C  CB  . LEU A 1 213 ? 31.058 3.250  8.204  1.00 24.71  ? 208 LEU A CB  1 
ATOM   1617 C  CG  . LEU A 1 213 ? 29.830 2.790  8.952  1.00 22.88  ? 208 LEU A CG  1 
ATOM   1618 C  CD1 . LEU A 1 213 ? 30.067 1.453  9.563  1.00 27.48  ? 208 LEU A CD1 1 
ATOM   1619 C  CD2 . LEU A 1 213 ? 29.406 3.792  10.047 1.00 28.77  ? 208 LEU A CD2 1 
ATOM   1620 N  N   . SER A 1 214 ? 32.724 6.102  7.663  1.00 25.70  ? 209 SER A N   1 
ATOM   1621 C  CA  . SER A 1 214 ? 34.036 6.672  7.418  1.00 30.39  ? 209 SER A CA  1 
ATOM   1622 C  C   . SER A 1 214 ? 35.045 6.117  8.421  1.00 29.24  ? 209 SER A C   1 
ATOM   1623 O  O   . SER A 1 214 ? 34.737 6.004  9.600  1.00 26.43  ? 209 SER A O   1 
ATOM   1624 C  CB  . SER A 1 214 ? 33.997 8.196  7.492  1.00 33.19  ? 209 SER A CB  1 
ATOM   1625 O  OG  . SER A 1 214 ? 35.317 8.700  7.459  1.00 41.48  ? 209 SER A OG  1 
ATOM   1626 N  N   . GLU A 1 215 ? 36.261 5.839  7.934  1.00 27.14  ? 210 GLU A N   1 
ATOM   1627 C  CA  . GLU A 1 215 ? 37.370 5.406  8.770  1.00 41.94  ? 210 GLU A CA  1 
ATOM   1628 C  C   . GLU A 1 215 ? 37.633 6.300  9.977  1.00 40.49  ? 210 GLU A C   1 
ATOM   1629 O  O   . GLU A 1 215 ? 37.982 5.797  11.042 1.00 31.00  ? 210 GLU A O   1 
ATOM   1630 C  CB  . GLU A 1 215 ? 38.656 5.353  7.952  1.00 42.18  ? 210 GLU A CB  1 
ATOM   1631 C  CG  . GLU A 1 215 ? 38.702 4.249  6.926  1.00 60.73  ? 210 GLU A CG  1 
ATOM   1632 C  CD  . GLU A 1 215 ? 39.985 4.273  6.137  1.00 83.22  ? 210 GLU A CD  1 
ATOM   1633 O  OE1 . GLU A 1 215 ? 41.058 4.106  6.764  1.00 41.42  ? 210 GLU A OE1 1 
ATOM   1634 O  OE2 . GLU A 1 215 ? 39.923 4.485  4.903  1.00 52.36  ? 210 GLU A OE2 1 
ATOM   1635 N  N   . ASP A 1 216 ? 37.468 7.619  9.822  1.00 25.52  ? 211 ASP A N   1 
ATOM   1636 C  CA  . ASP A 1 216 ? 37.802 8.523  10.912 1.00 36.04  ? 211 ASP A CA  1 
ATOM   1637 C  C   . ASP A 1 216 ? 36.651 8.783  11.888 1.00 41.66  ? 211 ASP A C   1 
ATOM   1638 O  O   . ASP A 1 216 ? 36.867 9.417  12.913 1.00 35.98  ? 211 ASP A O   1 
ATOM   1639 C  CB  . ASP A 1 216 ? 38.364 9.857  10.366 1.00 60.78  ? 211 ASP A CB  1 
ATOM   1640 C  CG  . ASP A 1 216 ? 37.489 10.537 9.341  1.00 119.41 ? 211 ASP A CG  1 
ATOM   1641 O  OD1 . ASP A 1 216 ? 36.256 10.535 9.528  1.00 42.58  ? 211 ASP A OD1 1 
ATOM   1642 O  OD2 . ASP A 1 216 ? 38.042 11.084 8.353  1.00 66.48  ? 211 ASP A OD2 1 
ATOM   1643 N  N   . SER A 1 217 ? 35.447 8.255  11.611 1.00 28.57  ? 212 SER A N   1 
ATOM   1644 C  CA  . SER A 1 217 ? 34.287 8.518  12.455 1.00 26.33  ? 212 SER A CA  1 
ATOM   1645 C  C   . SER A 1 217 ? 33.285 7.379  12.671 1.00 24.79  ? 212 SER A C   1 
ATOM   1646 O  O   . SER A 1 217 ? 32.197 7.614  13.188 1.00 27.35  ? 212 SER A O   1 
ATOM   1647 C  CB  . SER A 1 217 ? 33.524 9.705  11.871 1.00 23.08  ? 212 SER A CB  1 
ATOM   1648 O  OG  . SER A 1 217 ? 32.944 9.376  10.625 1.00 26.59  ? 212 SER A OG  1 
ATOM   1649 N  N   . TYR A 1 218 ? 33.651 6.146  12.314 1.00 27.79  ? 213 TYR A N   1 
ATOM   1650 C  CA  . TYR A 1 218 ? 32.699 5.042  12.303 1.00 26.91  ? 213 TYR A CA  1 
ATOM   1651 C  C   . TYR A 1 218 ? 32.241 4.673  13.717 1.00 27.12  ? 213 TYR A C   1 
ATOM   1652 O  O   . TYR A 1 218 ? 31.092 4.279  13.906 1.00 25.94  ? 213 TYR A O   1 
ATOM   1653 C  CB  . TYR A 1 218 ? 33.277 3.830  11.555 1.00 24.84  ? 213 TYR A CB  1 
ATOM   1654 C  CG  . TYR A 1 218 ? 34.373 3.093  12.277 1.00 24.88  ? 213 TYR A CG  1 
ATOM   1655 C  CD1 . TYR A 1 218 ? 34.078 2.080  13.185 1.00 28.78  ? 213 TYR A CD1 1 
ATOM   1656 C  CD2 . TYR A 1 218 ? 35.707 3.423  12.082 1.00 28.28  ? 213 TYR A CD2 1 
ATOM   1657 C  CE1 . TYR A 1 218 ? 35.083 1.405  13.863 1.00 24.14  ? 213 TYR A CE1 1 
ATOM   1658 C  CE2 . TYR A 1 218 ? 36.724 2.753  12.758 1.00 42.03  ? 213 TYR A CE2 1 
ATOM   1659 C  CZ  . TYR A 1 218 ? 36.407 1.745  13.653 1.00 42.49  ? 213 TYR A CZ  1 
ATOM   1660 O  OH  . TYR A 1 218 ? 37.399 1.057  14.315 1.00 30.21  ? 213 TYR A OH  1 
ATOM   1661 N  N   . LYS A 1 219 ? 33.119 4.882  14.710 1.00 23.16  ? 214 LYS A N   1 
ATOM   1662 C  CA  . LYS A 1 219 ? 32.767 4.635  16.103 1.00 30.43  ? 214 LYS A CA  1 
ATOM   1663 C  C   . LYS A 1 219 ? 31.656 5.569  16.567 1.00 28.05  ? 214 LYS A C   1 
ATOM   1664 O  O   . LYS A 1 219 ? 30.767 5.155  17.311 1.00 25.92  ? 214 LYS A O   1 
ATOM   1665 C  CB  . LYS A 1 219 ? 33.989 4.787  17.015 1.00 30.08  ? 214 LYS A CB  1 
ATOM   1666 C  CG  . LYS A 1 219 ? 35.079 3.743  16.765 1.00 44.25  ? 214 LYS A CG  1 
ATOM   1667 C  CD  . LYS A 1 219 ? 36.318 3.999  17.627 1.00 64.77  ? 214 LYS A CD  1 
ATOM   1668 C  CE  . LYS A 1 219 ? 37.516 3.207  17.178 1.00 91.15  ? 214 LYS A CE  1 
ATOM   1669 N  NZ  . LYS A 1 219 ? 38.723 3.561  17.967 1.00 84.88  ? 214 LYS A NZ  1 
ATOM   1670 N  N   . ASP A 1 220 ? 31.737 6.839  16.142 1.00 26.48  ? 215 ASP A N   1 
ATOM   1671 C  CA  . ASP A 1 220 ? 30.697 7.810  16.429 1.00 29.87  ? 215 ASP A CA  1 
ATOM   1672 C  C   . ASP A 1 220 ? 29.382 7.425  15.754 1.00 19.92  ? 215 ASP A C   1 
ATOM   1673 O  O   . ASP A 1 220 ? 28.323 7.456  16.377 1.00 26.13  ? 215 ASP A O   1 
ATOM   1674 C  CB  . ASP A 1 220 ? 31.154 9.202  15.979 1.00 34.85  ? 215 ASP A CB  1 
ATOM   1675 C  CG  . ASP A 1 220 ? 32.355 9.763  16.729 1.00 32.78  ? 215 ASP A CG  1 
ATOM   1676 O  OD1 . ASP A 1 220 ? 32.732 9.187  17.769 1.00 40.16  ? 215 ASP A OD1 1 
ATOM   1677 O  OD2 . ASP A 1 220 ? 32.905 10.784 16.283 1.00 40.93  ? 215 ASP A OD2 1 
ATOM   1678 N  N   . SER A 1 221 ? 29.456 7.075  14.468 1.00 22.04  ? 216 SER A N   1 
ATOM   1679 C  CA  . SER A 1 221 ? 28.273 6.666  13.731 1.00 26.47  ? 216 SER A CA  1 
ATOM   1680 C  C   . SER A 1 221 ? 27.559 5.502  14.419 1.00 27.86  ? 216 SER A C   1 
ATOM   1681 O  O   . SER A 1 221 ? 26.365 5.586  14.678 1.00 23.76  ? 216 SER A O   1 
ATOM   1682 C  CB  . SER A 1 221 ? 28.641 6.321  12.297 1.00 28.22  ? 216 SER A CB  1 
ATOM   1683 O  OG  . SER A 1 221 ? 29.160 7.455  11.625 1.00 26.82  ? 216 SER A OG  1 
ATOM   1684 N  N   . THR A 1 222 ? 28.301 4.439  14.767 1.00 27.46  ? 217 THR A N   1 
ATOM   1685 C  CA  . THR A 1 222 ? 27.692 3.249  15.350 1.00 35.35  ? 217 THR A CA  1 
ATOM   1686 C  C   . THR A 1 222 ? 27.116 3.526  16.736 1.00 27.05  ? 217 THR A C   1 
ATOM   1687 O  O   . THR A 1 222 ? 26.080 2.968  17.106 1.00 25.86  ? 217 THR A O   1 
ATOM   1688 C  CB  . THR A 1 222 ? 28.676 2.047  15.323 1.00 26.44  ? 217 THR A CB  1 
ATOM   1689 O  OG1 . THR A 1 222 ? 29.854 2.320  16.061 1.00 30.80  ? 217 THR A OG1 1 
ATOM   1690 C  CG2 . THR A 1 222 ? 29.067 1.681  13.922 1.00 29.92  ? 217 THR A CG2 1 
ATOM   1691 N  N   . LEU A 1 223 ? 27.773 4.421  17.484 1.00 27.06  ? 218 LEU A N   1 
ATOM   1692 C  CA  . LEU A 1 223 ? 27.263 4.848  18.776 1.00 30.65  ? 218 LEU A CA  1 
ATOM   1693 C  C   . LEU A 1 223 ? 25.885 5.481  18.601 1.00 27.79  ? 218 LEU A C   1 
ATOM   1694 O  O   . LEU A 1 223 ? 24.947 5.075  19.274 1.00 23.95  ? 218 LEU A O   1 
ATOM   1695 C  CB  . LEU A 1 223 ? 28.246 5.819  19.475 1.00 29.66  ? 218 LEU A CB  1 
ATOM   1696 C  CG  . LEU A 1 223 ? 27.752 6.439  20.798 1.00 29.36  ? 218 LEU A CG  1 
ATOM   1697 C  CD1 . LEU A 1 223 ? 27.271 5.358  21.777 1.00 52.62  ? 218 LEU A CD1 1 
ATOM   1698 C  CD2 . LEU A 1 223 ? 28.835 7.284  21.430 1.00 42.01  ? 218 LEU A CD2 1 
ATOM   1699 N  N   . ILE A 1 224 ? 25.745 6.451  17.683 1.00 27.72  ? 219 ILE A N   1 
ATOM   1700 C  CA  . ILE A 1 224 ? 24.451 7.096  17.486 1.00 22.00  ? 219 ILE A CA  1 
ATOM   1701 C  C   . ILE A 1 224 ? 23.391 6.116  16.975 1.00 27.01  ? 219 ILE A C   1 
ATOM   1702 O  O   . ILE A 1 224 ? 22.229 6.194  17.369 1.00 25.38  ? 219 ILE A O   1 
ATOM   1703 C  CB  . ILE A 1 224 ? 24.525 8.332  16.565 1.00 22.79  ? 219 ILE A CB  1 
ATOM   1704 C  CG1 . ILE A 1 224 ? 25.588 9.341  17.043 1.00 27.95  ? 219 ILE A CG1 1 
ATOM   1705 C  CG2 . ILE A 1 224 ? 23.134 8.998  16.427 1.00 23.15  ? 219 ILE A CG2 1 
ATOM   1706 C  CD1 . ILE A 1 224 ? 25.383 9.859  18.380 1.00 28.96  ? 219 ILE A CD1 1 
ATOM   1707 N  N   . MET A 1 225 ? 23.777 5.173  16.108 1.00 22.24  ? 220 MET A N   1 
ATOM   1708 C  CA  . MET A 1 225 ? 22.841 4.149  15.664 1.00 20.23  ? 220 MET A CA  1 
ATOM   1709 C  C   . MET A 1 225 ? 22.269 3.327  16.821 1.00 22.27  ? 220 MET A C   1 
ATOM   1710 O  O   . MET A 1 225 ? 21.075 3.039  16.849 1.00 26.77  ? 220 MET A O   1 
ATOM   1711 C  CB  . MET A 1 225 ? 23.540 3.236  14.653 1.00 26.40  ? 220 MET A CB  1 
ATOM   1712 C  CG  . MET A 1 225 ? 23.738 3.924  13.319 1.00 31.52  ? 220 MET A CG  1 
ATOM   1713 S  SD  . MET A 1 225 ? 24.877 3.034  12.215 1.00 29.77  ? 220 MET A SD  1 
ATOM   1714 C  CE  . MET A 1 225 ? 23.801 1.650  11.766 1.00 25.93  ? 220 MET A CE  1 
ATOM   1715 N  N   . GLN A 1 226 ? 23.122 2.985  17.791 1.00 25.01  ? 221 GLN A N   1 
ATOM   1716 C  CA  . GLN A 1 226 ? 22.678 2.265  18.979 1.00 27.17  ? 221 GLN A CA  1 
ATOM   1717 C  C   . GLN A 1 226 ? 21.749 3.133  19.828 1.00 32.53  ? 221 GLN A C   1 
ATOM   1718 O  O   . GLN A 1 226 ? 20.777 2.626  20.381 1.00 29.91  ? 221 GLN A O   1 
ATOM   1719 C  CB  . GLN A 1 226 ? 23.880 1.792  19.799 1.00 32.37  ? 221 GLN A CB  1 
ATOM   1720 C  CG  . GLN A 1 226 ? 23.516 0.996  21.050 1.00 49.60  ? 221 GLN A CG  1 
ATOM   1721 C  CD  . GLN A 1 226 ? 22.760 -0.253 20.691 1.00 39.01  ? 221 GLN A CD  1 
ATOM   1722 O  OE1 . GLN A 1 226 ? 23.165 -1.009 19.802 1.00 33.34  ? 221 GLN A OE1 1 
ATOM   1723 N  NE2 . GLN A 1 226 ? 21.632 -0.479 21.350 1.00 48.97  ? 221 GLN A NE2 1 
ATOM   1724 N  N   . LEU A 1 227 ? 22.047 4.440  19.933 1.00 28.08  ? 222 LEU A N   1 
ATOM   1725 C  CA  . LEU A 1 227 ? 21.204 5.337  20.713 1.00 25.09  ? 222 LEU A CA  1 
ATOM   1726 C  C   . LEU A 1 227 ? 19.841 5.528  20.056 1.00 25.08  ? 222 LEU A C   1 
ATOM   1727 O  O   . LEU A 1 227 ? 18.836 5.608  20.753 1.00 27.46  ? 222 LEU A O   1 
ATOM   1728 C  CB  . LEU A 1 227 ? 21.864 6.681  20.955 1.00 27.88  ? 222 LEU A CB  1 
ATOM   1729 C  CG  . LEU A 1 227 ? 23.161 6.636  21.744 1.00 29.45  ? 222 LEU A CG  1 
ATOM   1730 C  CD1 . LEU A 1 227 ? 23.716 8.038  21.944 1.00 26.73  ? 222 LEU A CD1 1 
ATOM   1731 C  CD2 . LEU A 1 227 ? 22.980 5.920  23.078 1.00 35.91  ? 222 LEU A CD2 1 
ATOM   1732 N  N   . LEU A 1 228 ? 19.798 5.523  18.714 1.00 23.66  ? 223 LEU A N   1 
ATOM   1733 C  CA  . LEU A 1 228 ? 18.527 5.521  18.008 1.00 26.09  ? 223 LEU A CA  1 
ATOM   1734 C  C   . LEU A 1 228 ? 17.720 4.269  18.359 1.00 32.81  ? 223 LEU A C   1 
ATOM   1735 O  O   . LEU A 1 228 ? 16.524 4.358  18.637 1.00 27.99  ? 223 LEU A O   1 
ATOM   1736 C  CB  . LEU A 1 228 ? 18.748 5.602  16.492 1.00 26.61  ? 223 LEU A CB  1 
ATOM   1737 C  CG  . LEU A 1 228 ? 19.240 6.947  15.965 1.00 30.54  ? 223 LEU A CG  1 
ATOM   1738 C  CD1 . LEU A 1 228 ? 19.875 6.779  14.590 1.00 31.30  ? 223 LEU A CD1 1 
ATOM   1739 C  CD2 . LEU A 1 228 ? 18.112 7.952  15.880 1.00 31.34  ? 223 LEU A CD2 1 
ATOM   1740 N  N   . ARG A 1 229 ? 18.392 3.112  18.367 1.00 31.58  ? 224 ARG A N   1 
ATOM   1741 C  CA  . ARG A 1 229 ? 17.761 1.849  18.730 1.00 38.46  ? 224 ARG A CA  1 
ATOM   1742 C  C   . ARG A 1 229 ? 17.283 1.834  20.186 1.00 34.82  ? 224 ARG A C   1 
ATOM   1743 O  O   . ARG A 1 229 ? 16.225 1.280  20.472 1.00 43.21  ? 224 ARG A O   1 
ATOM   1744 C  CB  . ARG A 1 229 ? 18.733 0.679  18.417 1.00 43.93  ? 224 ARG A CB  1 
ATOM   1745 C  CG  . ARG A 1 229 ? 18.246 -0.729 18.798 1.00 77.14  ? 224 ARG A CG  1 
ATOM   1746 C  CD  . ARG A 1 229 ? 16.848 -1.075 18.293 1.00 105.95 ? 224 ARG A CD  1 
ATOM   1747 N  NE  . ARG A 1 229 ? 16.756 -1.126 16.838 1.00 36.35  ? 224 ARG A NE  1 
ATOM   1748 C  CZ  . ARG A 1 229 ? 15.613 -1.104 16.160 1.00 101.67 ? 224 ARG A CZ  1 
ATOM   1749 N  NH1 . ARG A 1 229 ? 14.443 -1.094 16.778 1.00 60.81  ? 224 ARG A NH1 1 
ATOM   1750 N  NH2 . ARG A 1 229 ? 15.645 -1.081 14.831 1.00 58.89  ? 224 ARG A NH2 1 
ATOM   1751 N  N   . ASP A 1 230 ? 18.036 2.473  21.096 1.00 33.69  ? 225 ASP A N   1 
ATOM   1752 C  CA  . ASP A 1 230 ? 17.649 2.542  22.501 1.00 36.88  ? 225 ASP A CA  1 
ATOM   1753 C  C   . ASP A 1 230 ? 16.374 3.367  22.666 1.00 51.89  ? 225 ASP A C   1 
ATOM   1754 O  O   . ASP A 1 230 ? 15.479 2.967  23.402 1.00 37.17  ? 225 ASP A O   1 
ATOM   1755 C  CB  . ASP A 1 230 ? 18.776 3.115  23.392 1.00 36.90  ? 225 ASP A CB  1 
ATOM   1756 C  CG  . ASP A 1 230 ? 20.055 2.284  23.461 1.00 25.52  ? 225 ASP A CG  1 
ATOM   1757 O  OD1 . ASP A 1 230 ? 20.027 1.113  23.028 1.00 39.84  ? 225 ASP A OD1 1 
ATOM   1758 O  OD2 . ASP A 1 230 ? 21.092 2.827  23.906 1.00 42.58  ? 225 ASP A OD2 1 
ATOM   1759 N  N   . ASN A 1 231 ? 16.287 4.508  21.971 1.00 39.39  ? 226 ASN A N   1 
ATOM   1760 C  CA  . ASN A 1 231 ? 15.095 5.341  22.024 1.00 48.62  ? 226 ASN A CA  1 
ATOM   1761 C  C   . ASN A 1 231 ? 13.873 4.619  21.465 1.00 43.75  ? 226 ASN A C   1 
ATOM   1762 O  O   . ASN A 1 231 ? 12.796 4.685  22.050 1.00 34.29  ? 226 ASN A O   1 
ATOM   1763 C  CB  . ASN A 1 231 ? 15.304 6.673  21.291 1.00 35.49  ? 226 ASN A CB  1 
ATOM   1764 C  CG  . ASN A 1 231 ? 16.105 7.648  22.100 1.00 36.26  ? 226 ASN A CG  1 
ATOM   1765 O  OD1 . ASN A 1 231 ? 16.336 7.425  23.291 1.00 30.40  ? 226 ASN A OD1 1 
ATOM   1766 N  ND2 . ASN A 1 231 ? 16.543 8.752  21.485 1.00 31.56  ? 226 ASN A ND2 1 
ATOM   1767 N  N   . LEU A 1 232 ? 14.050 3.939  20.328 1.00 31.15  ? 227 LEU A N   1 
ATOM   1768 C  CA  . LEU A 1 232 ? 12.978 3.173  19.714 1.00 33.12  ? 227 LEU A CA  1 
ATOM   1769 C  C   . LEU A 1 232 ? 12.423 2.087  20.634 1.00 37.12  ? 227 LEU A C   1 
ATOM   1770 O  O   . LEU A 1 232 ? 11.219 1.842  20.636 1.00 32.33  ? 227 LEU A O   1 
ATOM   1771 C  CB  . LEU A 1 232 ? 13.485 2.562  18.408 1.00 30.47  ? 227 LEU A CB  1 
ATOM   1772 C  CG  . LEU A 1 232 ? 13.616 3.552  17.249 1.00 33.76  ? 227 LEU A CG  1 
ATOM   1773 C  CD1 . LEU A 1 232 ? 14.361 2.936  16.093 1.00 42.28  ? 227 LEU A CD1 1 
ATOM   1774 C  CD2 . LEU A 1 232 ? 12.245 4.057  16.819 1.00 34.84  ? 227 LEU A CD2 1 
ATOM   1775 N  N   . THR A 1 233 ? 13.307 1.451  21.412 1.00 36.84  ? 228 THR A N   1 
ATOM   1776 C  CA  . THR A 1 233 ? 12.910 0.440  22.382 1.00 51.06  ? 228 THR A CA  1 
ATOM   1777 C  C   . THR A 1 233 ? 12.141 1.056  23.549 1.00 58.09  ? 228 THR A C   1 
ATOM   1778 O  O   . THR A 1 233 ? 11.151 0.494  24.011 1.00 56.49  ? 228 THR A O   1 
ATOM   1779 C  CB  . THR A 1 233 ? 14.145 -0.332 22.863 1.00 61.23  ? 228 THR A CB  1 
ATOM   1780 O  OG1 . THR A 1 233 ? 14.683 -1.038 21.746 1.00 39.09  ? 228 THR A OG1 1 
ATOM   1781 C  CG2 . THR A 1 233 ? 13.834 -1.316 23.996 1.00 53.49  ? 228 THR A CG2 1 
ATOM   1782 N  N   . LEU A 1 234 ? 12.615 2.211  24.024 1.00 44.23  ? 229 LEU A N   1 
ATOM   1783 C  CA  . LEU A 1 234 ? 11.940 2.960  25.070 1.00 39.32  ? 229 LEU A CA  1 
ATOM   1784 C  C   . LEU A 1 234 ? 10.564 3.462  24.625 1.00 53.72  ? 229 LEU A C   1 
ATOM   1785 O  O   . LEU A 1 234 ? 9.628  3.469  25.419 1.00 53.57  ? 229 LEU A O   1 
ATOM   1786 C  CB  . LEU A 1 234 ? 12.851 4.129  25.512 1.00 36.75  ? 229 LEU A CB  1 
ATOM   1787 C  CG  . LEU A 1 234 ? 12.231 5.159  26.441 1.00 42.64  ? 229 LEU A CG  1 
ATOM   1788 C  CD1 . LEU A 1 234 ? 11.861 4.527  27.770 1.00 55.41  ? 229 LEU A CD1 1 
ATOM   1789 C  CD2 . LEU A 1 234 ? 13.169 6.354  26.635 1.00 40.33  ? 229 LEU A CD2 1 
ATOM   1790 N  N   . TRP A 1 235 ? 10.436 3.858  23.349 1.00 40.73  ? 230 TRP A N   1 
ATOM   1791 C  CA  . TRP A 1 235 ? 9.221  4.485  22.848 1.00 34.95  ? 230 TRP A CA  1 
ATOM   1792 C  C   . TRP A 1 235 ? 8.130  3.535  22.358 1.00 37.52  ? 230 TRP A C   1 
ATOM   1793 O  O   . TRP A 1 235 ? 6.995  3.971  22.186 1.00 39.51  ? 230 TRP A O   1 
ATOM   1794 C  CB  . TRP A 1 235 ? 9.556  5.431  21.690 1.00 50.78  ? 230 TRP A CB  1 
ATOM   1795 C  CG  . TRP A 1 235 ? 10.441 6.572  22.067 1.00 41.87  ? 230 TRP A CG  1 
ATOM   1796 C  CD1 . TRP A 1 235 ? 10.766 6.985  23.324 1.00 41.75  ? 230 TRP A CD1 1 
ATOM   1797 C  CD2 . TRP A 1 235 ? 11.147 7.426  21.168 1.00 36.03  ? 230 TRP A CD2 1 
ATOM   1798 N  NE1 . TRP A 1 235 ? 11.614 8.057  23.264 1.00 38.06  ? 230 TRP A NE1 1 
ATOM   1799 C  CE2 . TRP A 1 235 ? 11.874 8.346  21.949 1.00 30.81  ? 230 TRP A CE2 1 
ATOM   1800 C  CE3 . TRP A 1 235 ? 11.234 7.507  19.769 1.00 37.07  ? 230 TRP A CE3 1 
ATOM   1801 C  CZ2 . TRP A 1 235 ? 12.672 9.341  21.382 1.00 43.74  ? 230 TRP A CZ2 1 
ATOM   1802 C  CZ3 . TRP A 1 235 ? 12.035 8.486  19.209 1.00 42.42  ? 230 TRP A CZ3 1 
ATOM   1803 C  CH2 . TRP A 1 235 ? 12.740 9.392  20.013 1.00 39.24  ? 230 TRP A CH2 1 
ATOM   1804 N  N   . THR A 1 236 ? 8.491  2.269  22.087 1.00 38.43  ? 231 THR A N   1 
ATOM   1805 C  CA  . THR A 1 236 ? 7.534  1.247  21.686 1.00 49.40  ? 231 THR A CA  1 
ATOM   1806 C  C   . THR A 1 236 ? 7.433  0.136  22.748 1.00 50.37  ? 231 THR A C   1 
ATOM   1807 O  O   . THR A 1 236 ? 6.335  -0.330 23.037 1.00 55.80  ? 231 THR A O   1 
ATOM   1808 C  CB  . THR A 1 236 ? 7.891  0.674  20.298 1.00 49.27  ? 231 THR A CB  1 
ATOM   1809 O  OG1 . THR A 1 236 ? 9.225  0.176  20.314 1.00 46.77  ? 231 THR A OG1 1 
ATOM   1810 C  CG2 . THR A 1 236 ? 7.764  1.706  19.190 1.00 51.76  ? 231 THR A CG2 1 
ATOM   1811 O  OXT . THR A 1 236 ? 8.436  -0.284 23.322 1.00 45.53  ? 231 THR A OXT 1 
ATOM   1812 N  N   . GLN B 2 1   ? 11.742 7.611  32.413 1.00 70.60  ? 255 GLN P N   1 
ATOM   1813 C  CA  . GLN B 2 1   ? 13.081 7.762  31.853 1.00 111.98 ? 255 GLN P CA  1 
ATOM   1814 C  C   . GLN B 2 1   ? 13.064 8.712  30.658 1.00 96.46  ? 255 GLN P C   1 
ATOM   1815 O  O   . GLN B 2 1   ? 12.113 8.713  29.878 1.00 77.85  ? 255 GLN P O   1 
ATOM   1816 C  CB  . GLN B 2 1   ? 13.637 6.400  31.425 1.00 59.08  ? 255 GLN P CB  1 
ATOM   1817 C  CG  . GLN B 2 1   ? 15.080 6.455  30.935 1.00 70.09  ? 255 GLN P CG  1 
ATOM   1818 C  CD  . GLN B 2 1   ? 15.576 5.104  30.500 1.00 97.29  ? 255 GLN P CD  1 
ATOM   1819 O  OE1 . GLN B 2 1   ? 14.883 4.088  30.621 1.00 79.59  ? 255 GLN P OE1 1 
ATOM   1820 N  NE2 . GLN B 2 1   ? 16.793 5.066  29.981 1.00 69.96  ? 255 GLN P NE2 1 
ATOM   1821 N  N   . ARG B 2 2   ? 14.136 9.502  30.523 1.00 82.44  ? 256 ARG P N   1 
ATOM   1822 C  CA  . ARG B 2 2   ? 14.274 10.448 29.427 1.00 135.06 ? 256 ARG P CA  1 
ATOM   1823 C  C   . ARG B 2 2   ? 14.832 9.793  28.164 1.00 54.51  ? 256 ARG P C   1 
ATOM   1824 O  O   . ARG B 2 2   ? 15.635 8.860  28.232 1.00 44.91  ? 256 ARG P O   1 
ATOM   1825 C  CB  . ARG B 2 2   ? 15.195 11.621 29.822 1.00 64.09  ? 256 ARG P CB  1 
ATOM   1826 C  CG  . ARG B 2 2   ? 14.503 12.819 30.467 1.00 105.15 ? 256 ARG P CG  1 
ATOM   1827 C  CD  . ARG B 2 2   ? 15.420 14.033 30.450 1.00 96.26  ? 256 ARG P CD  1 
ATOM   1828 N  NE  . ARG B 2 2   ? 16.725 13.718 31.025 1.00 194.17 ? 256 ARG P NE  1 
ATOM   1829 C  CZ  . ARG B 2 2   ? 17.867 13.640 30.347 1.00 171.67 ? 256 ARG P CZ  1 
ATOM   1830 N  NH1 . ARG B 2 2   ? 18.076 14.347 29.245 1.00 38.89  ? 256 ARG P NH1 1 
ATOM   1831 N  NH2 . ARG B 2 2   ? 18.838 12.857 30.808 1.00 51.16  ? 256 ARG P NH2 1 
ATOM   1832 N  N   . SER B 2 3   ? 14.402 10.319 27.010 1.00 54.03  ? 257 SER P N   1 
ATOM   1833 C  CA  . SER B 2 3   ? 15.018 9.997  25.732 1.00 55.48  ? 257 SER P CA  1 
ATOM   1834 C  C   . SER B 2 3   ? 16.499 10.360 25.775 1.00 53.88  ? 257 SER P C   1 
ATOM   1835 O  O   . SER B 2 3   ? 16.884 11.316 26.448 1.00 43.50  ? 257 SER P O   1 
ATOM   1836 C  CB  . SER B 2 3   ? 14.339 10.751 24.591 1.00 49.30  ? 257 SER P CB  1 
ATOM   1837 O  OG  . SER B 2 3   ? 12.944 10.508 24.532 1.00 45.95  ? 257 SER P OG  1 
ATOM   1838 N  N   . THR B 2 4   ? 17.322 9.591  25.053 1.00 39.55  ? 258 THR P N   1 
ATOM   1839 C  CA  . THR B 2 4   ? 18.746 9.866  24.966 1.00 42.26  ? 258 THR P CA  1 
ATOM   1840 C  C   . THR B 2 4   ? 19.022 10.732 23.742 1.00 38.34  ? 258 THR P C   1 
ATOM   1841 O  O   . THR B 2 4   ? 18.569 10.411 22.643 1.00 35.23  ? 258 THR P O   1 
ATOM   1842 C  CB  . THR B 2 4   ? 19.539 8.564  24.916 1.00 48.70  ? 258 THR P CB  1 
ATOM   1843 O  OG1 . THR B 2 4   ? 19.075 7.726  25.965 1.00 38.50  ? 258 THR P OG1 1 
ATOM   1844 C  CG2 . THR B 2 4   ? 21.028 8.788  25.065 1.00 48.17  ? 258 THR P CG2 1 
HETATM 1845 N  N   . SEP B 2 5   ? 19.741 11.839 23.954 1.00 29.94  ? 259 SEP P N   1 
HETATM 1846 C  CA  . SEP B 2 5   ? 20.171 12.702 22.859 1.00 33.82  ? 259 SEP P CA  1 
HETATM 1847 C  CB  . SEP B 2 5   ? 19.873 14.171 23.153 1.00 37.29  ? 259 SEP P CB  1 
HETATM 1848 O  OG  . SEP B 2 5   ? 20.632 14.592 24.303 1.00 35.63  ? 259 SEP P OG  1 
HETATM 1849 C  C   . SEP B 2 5   ? 21.644 12.444 22.582 1.00 34.01  ? 259 SEP P C   1 
HETATM 1850 O  O   . SEP B 2 5   ? 22.258 11.603 23.238 1.00 30.75  ? 259 SEP P O   1 
HETATM 1851 P  P   . SEP B 2 5   ? 20.358 16.071 24.921 1.00 32.29  ? 259 SEP P P   1 
HETATM 1852 O  O1P . SEP B 2 5   ? 20.716 17.089 23.817 1.00 32.14  ? 259 SEP P O1P 1 
HETATM 1853 O  O2P . SEP B 2 5   ? 18.914 16.135 25.268 1.00 27.70  ? 259 SEP P O2P 1 
HETATM 1854 O  O3P . SEP B 2 5   ? 21.286 16.110 26.085 1.00 33.27  ? 259 SEP P O3P 1 
ATOM   1855 N  N   . THR B 2 6   ? 22.195 13.142 21.576 1.00 30.05  ? 260 THR P N   1 
ATOM   1856 C  CA  . THR B 2 6   ? 23.603 12.995 21.246 1.00 26.05  ? 260 THR P CA  1 
ATOM   1857 C  C   . THR B 2 6   ? 24.494 13.263 22.462 1.00 39.34  ? 260 THR P C   1 
ATOM   1858 O  O   . THR B 2 6   ? 24.304 14.276 23.141 1.00 34.12  ? 260 THR P O   1 
ATOM   1859 C  CB  . THR B 2 6   ? 23.921 13.902 20.074 1.00 38.55  ? 260 THR P CB  1 
ATOM   1860 O  OG1 . THR B 2 6   ? 23.143 13.467 18.947 1.00 37.00  ? 260 THR P OG1 1 
ATOM   1861 C  CG2 . THR B 2 6   ? 25.367 13.897 19.728 1.00 40.96  ? 260 THR P CG2 1 
ATOM   1862 N  N   . PRO B 2 7   ? 25.492 12.388 22.762 1.00 32.23  ? 261 PRO P N   1 
ATOM   1863 C  CA  . PRO B 2 7   ? 26.404 12.602 23.894 1.00 45.83  ? 261 PRO P CA  1 
ATOM   1864 C  C   . PRO B 2 7   ? 27.651 13.401 23.528 1.00 45.46  ? 261 PRO P C   1 
ATOM   1865 O  O   . PRO B 2 7   ? 27.863 13.699 22.365 1.00 34.49  ? 261 PRO P O   1 
ATOM   1866 C  CB  . PRO B 2 7   ? 26.789 11.165 24.275 1.00 43.05  ? 261 PRO P CB  1 
ATOM   1867 C  CG  . PRO B 2 7   ? 26.873 10.459 22.908 1.00 34.09  ? 261 PRO P CG  1 
ATOM   1868 C  CD  . PRO B 2 7   ? 25.761 11.104 22.071 1.00 28.81  ? 261 PRO P CD  1 
ATOM   1869 N  N   . ASN B 2 8   ? 28.490 13.726 24.521 1.00 45.05  ? 262 ASN P N   1 
ATOM   1870 C  CA  . ASN B 2 8   ? 29.813 14.287 24.261 1.00 39.07  ? 262 ASN P CA  1 
ATOM   1871 C  C   . ASN B 2 8   ? 30.920 13.251 24.059 1.00 42.85  ? 262 ASN P C   1 
ATOM   1872 O  O   . ASN B 2 8   ? 31.081 12.360 24.888 1.00 64.67  ? 262 ASN P O   1 
ATOM   1873 C  CB  . ASN B 2 8   ? 30.213 15.174 25.423 1.00 64.44  ? 262 ASN P CB  1 
ATOM   1874 C  CG  . ASN B 2 8   ? 29.287 16.342 25.551 1.00 73.72  ? 262 ASN P CG  1 
ATOM   1875 O  OD1 . ASN B 2 8   ? 29.287 17.249 24.718 1.00 36.16  ? 262 ASN P OD1 1 
ATOM   1876 N  ND2 . ASN B 2 8   ? 28.456 16.315 26.568 1.00 44.27  ? 262 ASN P ND2 1 
ATOM   1877 N  N   . VAL B 2 9   ? 31.702 13.400 22.977 1.00 35.54  ? 263 VAL P N   1 
ATOM   1878 C  CA  . VAL B 2 9   ? 32.866 12.558 22.739 1.00 38.43  ? 263 VAL P CA  1 
ATOM   1879 C  C   . VAL B 2 9   ? 34.057 13.340 22.190 1.00 43.85  ? 263 VAL P C   1 
ATOM   1880 O  O   . VAL B 2 9   ? 33.874 14.357 21.521 1.00 77.58  ? 263 VAL P O   1 
ATOM   1881 C  CB  . VAL B 2 9   ? 32.515 11.382 21.789 1.00 67.34  ? 263 VAL P CB  1 
ATOM   1882 C  CG1 . VAL B 2 9   ? 31.336 10.578 22.335 1.00 46.24  ? 263 VAL P CG1 1 
ATOM   1883 C  CG2 . VAL B 2 9   ? 32.245 11.874 20.364 1.00 55.50  ? 263 VAL P CG2 1 
ATOM   1884 N  N   . HIS B 2 10  ? 35.268 12.847 22.504 1.00 43.77  ? 264 HIS P N   1 
ATOM   1885 C  CA  . HIS B 2 10  ? 36.529 13.366 21.986 1.00 83.52  ? 264 HIS P CA  1 
ATOM   1886 C  C   . HIS B 2 10  ? 36.784 14.805 22.466 1.00 62.74  ? 264 HIS P C   1 
ATOM   1887 O  O   . HIS B 2 10  ? 37.692 15.404 21.858 1.00 51.15  ? 264 HIS P O   1 
ATOM   1888 C  CB  . HIS B 2 10  ? 36.590 13.213 20.459 1.00 90.63  ? 264 HIS P CB  1 
ATOM   1889 C  CG  . HIS B 2 10  ? 36.572 11.790 20.010 1.00 112.75 ? 264 HIS P CG  1 
ATOM   1890 N  ND1 . HIS B 2 10  ? 35.484 11.203 19.400 1.00 104.74 ? 264 HIS P ND1 1 
ATOM   1891 C  CD2 . HIS B 2 10  ? 37.504 10.833 20.110 1.00 99.12  ? 264 HIS P CD2 1 
ATOM   1892 C  CE1 . HIS B 2 10  ? 35.765 9.936  19.133 1.00 104.59 ? 264 HIS P CE1 1 
ATOM   1893 N  NE2 . HIS B 2 10  ? 36.988 9.691  19.555 1.00 170.29 ? 264 HIS P NE2 1 
ATOM   1894 O  OXT . HIS B 2 10  ? 36.121 15.277 23.416 1.00 45.99  ? 264 HIS P OXT 1 
HETATM 1895 CL CL  . CL  C 3 .   ? 17.730 31.882 45.227 1.00 46.25  ? 301 CL  A CL  1 
HETATM 1896 MG MG  . MG  D 4 .   ? 10.079 30.924 34.109 1.00 75.62  ? 302 MG  A MG  1 
HETATM 1897 MG MG  . MG  E 4 .   ? 2.138  19.207 56.851 1.00 85.98  ? 303 MG  A MG  1 
HETATM 1898 MG MG  . MG  F 4 .   ? 44.171 36.172 17.314 1.00 55.90  ? 304 MG  A MG  1 
HETATM 1899 C  C13 . WQ0 G 5 .   ? 29.386 16.032 15.294 1.00 47.69  ? 305 WQ0 A C13 1 
HETATM 1900 C  C12 . WQ0 G 5 .   ? 27.827 13.366 16.791 1.00 36.47  ? 305 WQ0 A C12 1 
HETATM 1901 C  C14 . WQ0 G 5 .   ? 30.749 16.581 14.899 1.00 49.30  ? 305 WQ0 A C14 1 
HETATM 1902 O  O1  . WQ0 G 5 .   ? 32.153 19.206 12.405 1.00 43.42  ? 305 WQ0 A O1  1 
HETATM 1903 C  C1  . WQ0 G 5 .   ? 32.985 18.334 12.710 1.00 46.72  ? 305 WQ0 A C1  1 
HETATM 1904 C  C2  . WQ0 G 5 .   ? 33.873 17.747 11.625 1.00 50.34  ? 305 WQ0 A C2  1 
HETATM 1905 N  N1  . WQ0 G 5 .   ? 33.152 17.903 13.962 1.00 47.59  ? 305 WQ0 A N1  1 
HETATM 1906 C  C3  . WQ0 G 5 .   ? 32.443 18.466 15.113 1.00 41.63  ? 305 WQ0 A C3  1 
HETATM 1907 C  C4  . WQ0 G 5 .   ? 31.029 17.976 15.425 1.00 67.17  ? 305 WQ0 A C4  1 
HETATM 1908 C  C5  . WQ0 G 5 .   ? 30.773 18.118 16.916 1.00 46.51  ? 305 WQ0 A C5  1 
HETATM 1909 C  C6  . WQ0 G 5 .   ? 29.855 17.054 17.482 1.00 46.18  ? 305 WQ0 A C6  1 
HETATM 1910 N  N2  . WQ0 G 5 .   ? 28.826 16.695 16.490 1.00 41.26  ? 305 WQ0 A N2  1 
HETATM 1911 S  S1  . WQ0 G 5 .   ? 27.437 16.046 17.063 1.00 45.13  ? 305 WQ0 A S1  1 
HETATM 1912 O  O2  . WQ0 G 5 .   ? 26.556 15.876 15.942 1.00 50.59  ? 305 WQ0 A O2  1 
HETATM 1913 O  O3  . WQ0 G 5 .   ? 26.993 16.816 18.183 1.00 61.39  ? 305 WQ0 A O3  1 
HETATM 1914 C  C7  . WQ0 G 5 .   ? 27.890 14.451 17.649 1.00 46.03  ? 305 WQ0 A C7  1 
HETATM 1915 C  C8  . WQ0 G 5 .   ? 28.350 14.303 18.942 1.00 53.73  ? 305 WQ0 A C8  1 
HETATM 1916 C  C9  . WQ0 G 5 .   ? 28.734 13.060 19.404 1.00 44.86  ? 305 WQ0 A C9  1 
HETATM 1917 C  C10 . WQ0 G 5 .   ? 28.662 11.964 18.562 1.00 44.51  ? 305 WQ0 A C10 1 
HETATM 1918 BR BR1 . WQ0 G 5 .   ? 29.151 10.235 19.177 1.00 75.51  ? 305 WQ0 A BR1 1 
HETATM 1919 C  C11 . WQ0 G 5 .   ? 28.222 12.142 17.267 1.00 45.58  ? 305 WQ0 A C11 1 
HETATM 1920 F  F1  . WQ0 G 5 .   ? 28.158 11.080 16.447 1.00 42.77  ? 305 WQ0 A F1  1 
HETATM 1921 MG MG  . MG  H 4 .   ? 22.906 1.678  -1.411 1.00 42.54  ? 306 MG  A MG  1 
HETATM 1922 O  O   . HOH I 6 .   ? 41.759 41.804 20.316 1.00 32.68  ? 401 HOH A O   1 
HETATM 1923 O  O   . HOH I 6 .   ? 32.386 7.753  19.633 1.00 49.67  ? 402 HOH A O   1 
HETATM 1924 O  O   . HOH I 6 .   ? 9.996  -1.367 25.044 1.00 58.37  ? 403 HOH A O   1 
HETATM 1925 O  O   . HOH I 6 .   ? 17.681 -0.861 6.627  1.00 46.07  ? 404 HOH A O   1 
HETATM 1926 O  O   . HOH I 6 .   ? 11.823 32.017 34.455 1.00 58.52  ? 405 HOH A O   1 
HETATM 1927 O  O   . HOH I 6 .   ? 41.935 38.919 26.966 1.00 58.81  ? 406 HOH A O   1 
HETATM 1928 O  O   . HOH I 6 .   ? 42.814 3.024  5.294  1.00 46.67  ? 407 HOH A O   1 
HETATM 1929 O  O   . HOH I 6 .   ? 24.997 -1.104 2.318  1.00 43.53  ? 408 HOH A O   1 
HETATM 1930 O  O   . HOH I 6 .   ? 26.872 23.469 34.681 1.00 45.42  ? 409 HOH A O   1 
HETATM 1931 O  O   . HOH I 6 .   ? 31.347 7.983  3.576  1.00 44.26  ? 410 HOH A O   1 
HETATM 1932 O  O   . HOH I 6 .   ? 24.089 32.308 32.643 1.00 43.58  ? 411 HOH A O   1 
HETATM 1933 O  O   . HOH I 6 .   ? 43.323 24.784 15.967 1.00 40.43  ? 412 HOH A O   1 
HETATM 1934 O  O   . HOH I 6 .   ? 41.972 22.135 13.988 1.00 50.93  ? 413 HOH A O   1 
HETATM 1935 O  O   . HOH I 6 .   ? 31.121 3.129  18.917 1.00 47.69  ? 414 HOH A O   1 
HETATM 1936 O  O   . HOH I 6 .   ? 17.302 -1.702 9.580  1.00 56.17  ? 415 HOH A O   1 
HETATM 1937 O  O   . HOH I 6 .   ? 36.075 11.056 14.824 1.00 65.82  ? 416 HOH A O   1 
HETATM 1938 O  O   . HOH I 6 .   ? 26.813 35.338 22.520 1.00 47.10  ? 417 HOH A O   1 
HETATM 1939 O  O   . HOH I 6 .   ? 17.015 5.861  25.314 1.00 57.33  ? 418 HOH A O   1 
HETATM 1940 O  O   . HOH I 6 .   ? 36.566 38.141 23.049 1.00 52.80  ? 419 HOH A O   1 
HETATM 1941 O  O   . HOH I 6 .   ? 37.662 32.237 14.939 1.00 41.97  ? 420 HOH A O   1 
HETATM 1942 O  O   . HOH I 6 .   ? 41.788 18.459 25.607 1.00 43.30  ? 421 HOH A O   1 
HETATM 1943 O  O   . HOH I 6 .   ? 8.592  27.266 46.659 1.00 44.61  ? 422 HOH A O   1 
HETATM 1944 O  O   . HOH I 6 .   ? 18.619 15.845 37.287 1.00 46.21  ? 423 HOH A O   1 
HETATM 1945 O  O   . HOH I 6 .   ? 29.423 17.487 21.970 1.00 39.44  ? 424 HOH A O   1 
HETATM 1946 O  O   . HOH I 6 .   ? 24.327 19.906 21.538 1.00 56.27  ? 425 HOH A O   1 
HETATM 1947 O  O   . HOH I 6 .   ? 31.554 13.026 15.674 1.00 47.29  ? 426 HOH A O   1 
HETATM 1948 O  O   . HOH I 6 .   ? 25.515 0.380  16.635 1.00 40.50  ? 427 HOH A O   1 
HETATM 1949 O  O   . HOH I 6 .   ? 32.691 11.563 9.065  1.00 46.55  ? 428 HOH A O   1 
HETATM 1950 O  O   . HOH I 6 .   ? 15.692 19.674 31.286 1.00 50.76  ? 429 HOH A O   1 
HETATM 1951 O  O   . HOH I 6 .   ? 16.783 22.971 29.631 1.00 41.80  ? 430 HOH A O   1 
HETATM 1952 O  O   . HOH I 6 .   ? 14.776 17.491 25.145 1.00 46.23  ? 431 HOH A O   1 
HETATM 1953 O  O   . HOH I 6 .   ? 31.402 29.697 10.580 1.00 47.17  ? 432 HOH A O   1 
HETATM 1954 O  O   . HOH I 6 .   ? 49.770 31.577 20.404 1.00 43.39  ? 433 HOH A O   1 
HETATM 1955 O  O   . HOH I 6 .   ? 31.200 7.428  9.835  1.00 39.41  ? 434 HOH A O   1 
HETATM 1956 O  O   . HOH I 6 .   ? 12.132 15.240 43.732 1.00 62.84  ? 435 HOH A O   1 
HETATM 1957 O  O   . HOH I 6 .   ? 38.285 37.127 21.069 1.00 43.57  ? 436 HOH A O   1 
HETATM 1958 O  O   . HOH I 6 .   ? 31.850 30.016 30.269 1.00 41.08  ? 437 HOH A O   1 
HETATM 1959 O  O   . HOH I 6 .   ? 30.846 31.401 27.960 1.00 42.08  ? 438 HOH A O   1 
HETATM 1960 O  O   . HOH I 6 .   ? 45.901 23.648 20.185 1.00 43.49  ? 439 HOH A O   1 
HETATM 1961 O  O   . HOH I 6 .   ? 34.825 34.389 26.604 1.00 40.08  ? 440 HOH A O   1 
HETATM 1962 O  O   . HOH I 6 .   ? 16.919 10.551 8.722  1.00 49.31  ? 441 HOH A O   1 
HETATM 1963 O  O   . HOH I 6 .   ? 46.635 22.481 24.897 1.00 44.30  ? 442 HOH A O   1 
HETATM 1964 O  O   . HOH I 6 .   ? 20.875 1.651  -0.565 1.00 57.98  ? 443 HOH A O   1 
HETATM 1965 O  O   . HOH I 6 .   ? 37.722 20.784 9.716  1.00 44.09  ? 444 HOH A O   1 
HETATM 1966 O  O   . HOH I 6 .   ? 23.284 35.621 28.054 1.00 52.31  ? 445 HOH A O   1 
HETATM 1967 O  O   . HOH I 6 .   ? 20.267 7.818  8.228  1.00 45.00  ? 446 HOH A O   1 
HETATM 1968 O  O   . HOH I 6 .   ? 25.116 17.132 20.648 1.00 51.39  ? 447 HOH A O   1 
HETATM 1969 O  O   . HOH I 6 .   ? 37.306 23.589 39.324 1.00 44.43  ? 448 HOH A O   1 
HETATM 1970 O  O   . HOH I 6 .   ? 46.250 26.110 19.108 1.00 38.76  ? 449 HOH A O   1 
HETATM 1971 O  O   . HOH I 6 .   ? 18.389 9.002  7.131  1.00 53.70  ? 450 HOH A O   1 
HETATM 1972 O  O   . HOH I 6 .   ? 4.051  37.975 24.700 1.00 56.19  ? 451 HOH A O   1 
HETATM 1973 O  O   . HOH I 6 .   ? 32.679 15.964 27.982 1.00 53.27  ? 452 HOH A O   1 
HETATM 1974 O  O   . HOH I 6 .   ? 26.500 21.157 20.134 1.00 37.21  ? 453 HOH A O   1 
HETATM 1975 O  O   . HOH I 6 .   ? 19.728 14.248 9.676  1.00 47.55  ? 454 HOH A O   1 
HETATM 1976 O  O   . HOH I 6 .   ? 35.688 16.151 27.189 1.00 48.98  ? 455 HOH A O   1 
HETATM 1977 O  O   . HOH I 6 .   ? 34.913 15.679 14.168 1.00 54.95  ? 456 HOH A O   1 
HETATM 1978 O  O   . HOH I 6 .   ? 31.156 15.756 20.811 1.00 45.41  ? 457 HOH A O   1 
HETATM 1979 O  O   . HOH I 6 .   ? 13.312 29.503 28.265 1.00 46.35  ? 458 HOH A O   1 
HETATM 1980 O  O   . HOH I 6 .   ? 41.029 26.493 12.339 1.00 53.34  ? 459 HOH A O   1 
HETATM 1981 O  O   . HOH I 6 .   ? 38.101 18.333 19.765 1.00 42.01  ? 460 HOH A O   1 
HETATM 1982 O  O   . HOH I 6 .   ? 42.645 22.150 16.934 1.00 54.00  ? 461 HOH A O   1 
HETATM 1983 O  O   . HOH I 6 .   ? 46.682 32.881 16.933 1.00 37.21  ? 462 HOH A O   1 
HETATM 1984 O  O   . HOH I 6 .   ? 18.926 12.411 7.928  1.00 49.89  ? 463 HOH A O   1 
HETATM 1985 O  O   . HOH I 6 .   ? 36.960 6.125  5.074  1.00 64.26  ? 464 HOH A O   1 
HETATM 1986 O  O   . HOH I 6 .   ? 25.307 20.527 17.278 1.00 47.06  ? 465 HOH A O   1 
HETATM 1987 O  O   . HOH I 6 .   ? 34.743 36.678 25.316 1.00 54.62  ? 466 HOH A O   1 
HETATM 1988 O  O   . HOH I 6 .   ? 39.857 19.376 12.536 1.00 41.65  ? 467 HOH A O   1 
HETATM 1989 O  O   . HOH I 6 .   ? 2.694  34.717 27.743 1.00 57.93  ? 468 HOH A O   1 
HETATM 1990 O  O   . HOH I 6 .   ? 28.354 29.322 33.128 1.00 48.25  ? 469 HOH A O   1 
HETATM 1991 O  O   . HOH I 6 .   ? 52.814 34.777 18.840 1.00 50.50  ? 470 HOH A O   1 
HETATM 1992 O  O   . HOH I 6 .   ? 26.295 32.964 29.784 1.00 60.76  ? 471 HOH A O   1 
HETATM 1993 O  O   . HOH I 6 .   ? 35.702 6.488  14.756 1.00 46.15  ? 472 HOH A O   1 
HETATM 1994 O  O   . HOH I 6 .   ? 30.063 8.426  7.614  1.00 37.96  ? 473 HOH A O   1 
HETATM 1995 O  O   . HOH I 6 .   ? 44.302 29.422 16.029 1.00 40.78  ? 474 HOH A O   1 
HETATM 1996 O  O   . HOH I 6 .   ? 30.646 10.864 6.625  1.00 44.42  ? 475 HOH A O   1 
HETATM 1997 O  O   . HOH I 6 .   ? 35.724 25.959 34.644 1.00 39.46  ? 476 HOH A O   1 
HETATM 1998 O  O   . HOH I 6 .   ? 13.752 31.890 26.835 1.00 55.93  ? 477 HOH A O   1 
HETATM 1999 O  O   . HOH I 6 .   ? 36.440 21.539 37.709 1.00 48.94  ? 478 HOH A O   1 
HETATM 2000 O  O   . HOH I 6 .   ? 15.903 33.205 27.076 1.00 64.37  ? 479 HOH A O   1 
HETATM 2001 O  O   . HOH I 6 .   ? 11.229 32.133 32.144 1.00 69.53  ? 480 HOH A O   1 
HETATM 2002 O  O   . HOH I 6 .   ? 31.054 18.519 4.322  1.00 57.43  ? 481 HOH A O   1 
HETATM 2003 O  O   . HOH I 6 .   ? 33.885 24.017 35.559 1.00 49.34  ? 482 HOH A O   1 
HETATM 2004 O  O   . HOH I 6 .   ? 27.713 36.556 20.376 1.00 50.06  ? 483 HOH A O   1 
HETATM 2005 O  O   . HOH I 6 .   ? 20.083 33.514 45.599 1.00 51.29  ? 484 HOH A O   1 
HETATM 2006 O  O   . HOH I 6 .   ? 17.641 33.886 21.720 1.00 72.21  ? 485 HOH A O   1 
HETATM 2007 O  O   . HOH I 6 .   ? 16.333 22.299 32.188 1.00 42.92  ? 486 HOH A O   1 
HETATM 2008 O  O   . HOH I 6 .   ? 27.808 31.193 29.002 1.00 48.14  ? 487 HOH A O   1 
HETATM 2009 O  O   . HOH I 6 .   ? 47.194 22.367 22.212 1.00 48.32  ? 488 HOH A O   1 
HETATM 2010 O  O   . HOH I 6 .   ? 32.329 13.966 13.132 1.00 50.19  ? 489 HOH A O   1 
HETATM 2011 O  O   . HOH I 6 .   ? 45.770 31.529 14.584 1.00 48.15  ? 490 HOH A O   1 
HETATM 2012 O  O   . HOH I 6 .   ? 43.304 3.050  2.655  1.00 53.13  ? 491 HOH A O   1 
HETATM 2013 O  O   . HOH J 6 .   ? 22.876 16.431 22.420 1.00 41.19  ? 301 HOH P O   1 
HETATM 2014 O  O   . HOH J 6 .   ? 23.338 11.191 25.631 1.00 48.43  ? 302 HOH P O   1 
HETATM 2015 O  O   . HOH J 6 .   ? 36.147 6.839  19.811 1.00 62.18  ? 303 HOH P O   1 
HETATM 2016 O  O   . HOH J 6 .   ? 20.882 12.126 26.794 1.00 45.77  ? 304 HOH P O   1 
HETATM 2017 O  O   . HOH J 6 .   ? 35.108 9.958  23.564 1.00 62.62  ? 305 HOH P O   1 
HETATM 2018 O  O   . HOH J 6 .   ? 14.846 14.874 26.529 1.00 51.36  ? 306 HOH P O   1 
# 
