data_9EW4
# 
_entry.id   9EW4 
# 
_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   9EW4         pdb_00009ew4 10.2210/pdb9ew4/pdb 
WWPDB D_1292136898 ?            ?                   
# 
_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       2025-04-16 
_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                        9EW4 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-03 
_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 'RAF proto-oncogene serine/threonine-protein kinase'                                                       
1070.028  1   2.7.11.1 ? ? ? 
3 non-polymer nat 'CHLORIDE ION'                                                                                             
35.453    1   ?        ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                                                                            
24.305    4   ?        ? ? ? 
5 non-polymer syn '1-[(5~{R})-2-(4-bromanyl-3-fluoranyl-phenyl)sulfonyl-2,7-diazaspiro[4.4]nonan-7-yl]-2-chloranyl-ethanone' 
439.727   1   ?        ? ? ? 
6 water       nat water                                                                                                      
18.015    219 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Epithelial cell marker protein 1,Stratifin' 
2 'Proto-oncogene c-RAF,cRaf,Raf-1'            
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
A ? 
2 'polypeptide(L)' no yes 'QRST(SEP)TPNV' QRSTSTPNV 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 '1-[(5~{R})-2-(4-bromanyl-3-fluoranyl-phenyl)sulfonyl-2,7-diazaspiro[4.4]nonan-7-yl]-2-chloranyl-ethanone' WQ9 
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 
# 
_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       9 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?               'C3 H7 N O2'              89.093  
ARG 'L-peptide linking' y ARGININE ?               'C6 H15 N4 O2 1'          175.209 
ASN 'L-peptide linking' y ASPARAGINE ?               'C4 H8 N2 O3'             132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?               'C4 H7 N O4'              133.103 
CL  non-polymer         . 'CHLORIDE ION' ?               'Cl -1'                   35.453  
CYS 'L-peptide linking' y CYSTEINE ?               'C3 H7 N O2 S'            121.158 
GLN 'L-peptide linking' y GLUTAMINE ?               'C5 H10 N2 O3'            146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?               'C5 H9 N O4'              147.129 
GLY 'peptide linking'   y GLYCINE ?               'C2 H5 N O2'              75.067  
HIS 'L-peptide linking' y HISTIDINE ?               'C6 H10 N3 O2 1'          156.162 
HOH non-polymer         . WATER ?               'H2 O'                    18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?               'C6 H13 N O2'             131.173 
LEU 'L-peptide linking' y LEUCINE ?               'C6 H13 N O2'             131.173 
LYS 'L-peptide linking' y LYSINE ?               'C6 H15 N2 O2 1'          147.195 
MET 'L-peptide linking' y METHIONINE ?               'C5 H11 N O2 S'           149.211 
MG  non-polymer         . 'MAGNESIUM ION' ?               'Mg 2'                    24.305  
PHE 'L-peptide linking' y PHENYLALANINE ?               'C9 H11 N O2'             165.189 
PRO 'L-peptide linking' y PROLINE ?               'C5 H9 N O2'              115.130 
SEP 'L-peptide linking' n PHOSPHOSERINE PHOSPHONOSERINE 'C3 H8 N O6 P'            185.072 
SER 'L-peptide linking' y SERINE ?               'C3 H7 N O3'              105.093 
THR 'L-peptide linking' y THREONINE ?               'C4 H9 N O3'              119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?               'C11 H12 N2 O2'           204.225 
TYR 'L-peptide linking' y TYROSINE ?               'C9 H11 N O3'             181.189 
VAL 'L-peptide linking' y VALINE ?               'C5 H11 N O2'             117.146 
WQ9 non-polymer         . 
'1-[(5~{R})-2-(4-bromanyl-3-fluoranyl-phenyl)sulfonyl-2,7-diazaspiro[4.4]nonan-7-yl]-2-chloranyl-ethanone' ?               
'C15 H17 Br Cl F N2 O3 S' 439.727 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -4  -4  GLY GLY A . n 
A 1 2   ALA 2   -3  -3  ALA ALA A . n 
A 1 3   MET 3   -2  -2  MET MET A . n 
A 1 4   GLY 4   -1  -1  GLY GLY A . n 
A 1 5   SER 5   0   0   SER SER A . n 
A 1 6   MET 6   1   1   MET MET A . n 
A 1 7   GLU 7   2   2   GLU GLU A . n 
A 1 8   ARG 8   3   3   ARG ARG A . n 
A 1 9   ALA 9   4   4   ALA ALA A . n 
A 1 10  SER 10  5   5   SER SER A . n 
A 1 11  LEU 11  6   6   LEU LEU A . n 
A 1 12  ILE 12  7   7   ILE ILE A . n 
A 1 13  GLN 13  8   8   GLN GLN A . n 
A 1 14  LYS 14  9   9   LYS LYS A . n 
A 1 15  ALA 15  10  10  ALA ALA A . n 
A 1 16  LYS 16  11  11  LYS LYS A . n 
A 1 17  LEU 17  12  12  LEU LEU A . n 
A 1 18  ALA 18  13  13  ALA ALA A . n 
A 1 19  GLU 19  14  14  GLU GLU A . n 
A 1 20  GLN 20  15  15  GLN GLN A . n 
A 1 21  ALA 21  16  16  ALA ALA A . n 
A 1 22  GLU 22  17  17  GLU GLU A . n 
A 1 23  ARG 23  18  18  ARG ARG A . n 
A 1 24  TYR 24  19  19  TYR TYR A . n 
A 1 25  GLU 25  20  20  GLU GLU A . n 
A 1 26  ASP 26  21  21  ASP ASP A . n 
A 1 27  MET 27  22  22  MET MET A . n 
A 1 28  ALA 28  23  23  ALA ALA A . n 
A 1 29  ALA 29  24  24  ALA ALA A . n 
A 1 30  PHE 30  25  25  PHE PHE A . n 
A 1 31  MET 31  26  26  MET MET A . n 
A 1 32  LYS 32  27  27  LYS LYS A . n 
A 1 33  GLY 33  28  28  GLY GLY A . n 
A 1 34  ALA 34  29  29  ALA ALA A . n 
A 1 35  VAL 35  30  30  VAL VAL A . n 
A 1 36  GLU 36  31  31  GLU GLU A . n 
A 1 37  LYS 37  32  32  LYS LYS A . n 
A 1 38  GLY 38  33  33  GLY GLY A . n 
A 1 39  GLU 39  34  34  GLU GLU A . n 
A 1 40  GLU 40  35  35  GLU GLU A . n 
A 1 41  LEU 41  36  36  LEU LEU A . n 
A 1 42  SER 42  37  37  SER SER A . n 
A 1 43  CYS 43  38  38  CYS CSO A . n 
A 1 44  GLU 44  39  39  GLU GLU A . n 
A 1 45  GLU 45  40  40  GLU GLU A . n 
A 1 46  ARG 46  41  41  ARG ARG A . n 
A 1 47  ASN 47  42  42  ASN ASN A . n 
A 1 48  LEU 48  43  43  LEU LEU A . n 
A 1 49  LEU 49  44  44  LEU LEU A . n 
A 1 50  SER 50  45  45  SER SER A . n 
A 1 51  VAL 51  46  46  VAL VAL A . n 
A 1 52  ALA 52  47  47  ALA ALA A . n 
A 1 53  TYR 53  48  48  TYR TYR A . n 
A 1 54  LYS 54  49  49  LYS LYS A . n 
A 1 55  ASN 55  50  50  ASN ASN A . n 
A 1 56  VAL 56  51  51  VAL VAL A . n 
A 1 57  VAL 57  52  52  VAL VAL A . n 
A 1 58  GLY 58  53  53  GLY GLY A . n 
A 1 59  GLY 59  54  54  GLY GLY A . n 
A 1 60  GLN 60  55  55  GLN GLN A . n 
A 1 61  ARG 61  56  56  ARG ARG A . n 
A 1 62  ALA 62  57  57  ALA ALA A . n 
A 1 63  ALA 63  58  58  ALA ALA A . n 
A 1 64  TRP 64  59  59  TRP TRP A . n 
A 1 65  ARG 65  60  60  ARG ARG A . n 
A 1 66  VAL 66  61  61  VAL VAL A . n 
A 1 67  LEU 67  62  62  LEU LEU A . n 
A 1 68  SER 68  63  63  SER SER A . n 
A 1 69  SER 69  64  64  SER SER A . n 
A 1 70  ILE 70  65  65  ILE ILE A . n 
A 1 71  GLU 71  66  66  GLU GLU A . n 
A 1 72  GLN 72  67  67  GLN GLN A . n 
A 1 73  LYS 73  68  68  LYS LYS A . n 
A 1 74  SER 74  69  69  SER SER A . n 
A 1 75  ASN 75  70  70  ASN ASN A . n 
A 1 76  GLU 76  71  71  GLU GLU A . n 
A 1 77  GLU 77  72  72  GLU GLU A . n 
A 1 78  GLY 78  73  73  GLY GLY A . n 
A 1 79  SER 79  74  74  SER SER A . n 
A 1 80  GLU 80  75  75  GLU GLU A . n 
A 1 81  GLU 81  76  76  GLU GLU A . n 
A 1 82  LYS 82  77  77  LYS LYS A . n 
A 1 83  GLY 83  78  78  GLY GLY A . n 
A 1 84  PRO 84  79  79  PRO PRO A . n 
A 1 85  GLU 85  80  80  GLU GLU A . n 
A 1 86  VAL 86  81  81  VAL VAL A . n 
A 1 87  ARG 87  82  82  ARG ARG A . n 
A 1 88  GLU 88  83  83  GLU GLU A . n 
A 1 89  TYR 89  84  84  TYR TYR A . n 
A 1 90  ARG 90  85  85  ARG ARG A . n 
A 1 91  GLU 91  86  86  GLU GLU A . n 
A 1 92  LYS 92  87  87  LYS LYS A . n 
A 1 93  VAL 93  88  88  VAL VAL A . n 
A 1 94  GLU 94  89  89  GLU GLU A . n 
A 1 95  THR 95  90  90  THR THR A . n 
A 1 96  GLU 96  91  91  GLU GLU A . n 
A 1 97  LEU 97  92  92  LEU LEU A . n 
A 1 98  GLN 98  93  93  GLN GLN A . n 
A 1 99  GLY 99  94  94  GLY GLY A . n 
A 1 100 VAL 100 95  95  VAL VAL A . n 
A 1 101 CYS 101 96  96  CYS CYS A . n 
A 1 102 ASP 102 97  97  ASP ASP A . n 
A 1 103 THR 103 98  98  THR THR A . n 
A 1 104 VAL 104 99  99  VAL VAL A . n 
A 1 105 LEU 105 100 100 LEU LEU A . n 
A 1 106 GLY 106 101 101 GLY GLY A . n 
A 1 107 LEU 107 102 102 LEU LEU A . n 
A 1 108 LEU 108 103 103 LEU LEU A . n 
A 1 109 ASP 109 104 104 ASP ASP A . n 
A 1 110 SER 110 105 105 SER SER A . n 
A 1 111 HIS 111 106 106 HIS HIS A . n 
A 1 112 LEU 112 107 107 LEU LEU A . n 
A 1 113 ILE 113 108 108 ILE ILE A . n 
A 1 114 LYS 114 109 109 LYS LYS A . n 
A 1 115 GLU 115 110 110 GLU GLU A . n 
A 1 116 ALA 116 111 111 ALA ALA A . n 
A 1 117 GLY 117 112 112 GLY GLY A . n 
A 1 118 ASP 118 113 113 ASP ASP A . n 
A 1 119 ALA 119 114 114 ALA ALA A . n 
A 1 120 GLU 120 115 115 GLU GLU A . n 
A 1 121 SER 121 116 116 SER SER A . n 
A 1 122 ARG 122 117 117 ARG ARG A . n 
A 1 123 VAL 123 118 118 VAL VAL A . n 
A 1 124 PHE 124 119 119 PHE PHE A . n 
A 1 125 TYR 125 120 120 TYR TYR A . n 
A 1 126 LEU 126 121 121 LEU LEU A . n 
A 1 127 LYS 127 122 122 LYS LYS A . n 
A 1 128 MET 128 123 123 MET MET A . n 
A 1 129 LYS 129 124 124 LYS LYS A . n 
A 1 130 GLY 130 125 125 GLY GLY A . n 
A 1 131 ASP 131 126 126 ASP ASP A . n 
A 1 132 TYR 132 127 127 TYR TYR A . n 
A 1 133 TYR 133 128 128 TYR TYR A . n 
A 1 134 ARG 134 129 129 ARG ARG A . n 
A 1 135 TYR 135 130 130 TYR TYR A . n 
A 1 136 LEU 136 131 131 LEU LEU A . n 
A 1 137 ALA 137 132 132 ALA ALA A . n 
A 1 138 GLU 138 133 133 GLU GLU A . n 
A 1 139 VAL 139 134 134 VAL VAL A . n 
A 1 140 ALA 140 135 135 ALA ALA A . n 
A 1 141 THR 141 136 136 THR THR A . n 
A 1 142 GLY 142 137 137 GLY GLY A . n 
A 1 143 ASP 143 138 138 ASP ASP A . n 
A 1 144 ASP 144 139 139 ASP ASP A . n 
A 1 145 LYS 145 140 140 LYS LYS A . n 
A 1 146 LYS 146 141 141 LYS LYS A . n 
A 1 147 ARG 147 142 142 ARG ARG A . n 
A 1 148 ILE 148 143 143 ILE ILE A . n 
A 1 149 ILE 149 144 144 ILE ILE A . n 
A 1 150 ASP 150 145 145 ASP ASP A . n 
A 1 151 SER 151 146 146 SER SER A . n 
A 1 152 ALA 152 147 147 ALA ALA A . n 
A 1 153 ARG 153 148 148 ARG ARG A . n 
A 1 154 SER 154 149 149 SER SER A . n 
A 1 155 ALA 155 150 150 ALA ALA A . n 
A 1 156 TYR 156 151 151 TYR TYR A . n 
A 1 157 GLN 157 152 152 GLN GLN A . n 
A 1 158 GLU 158 153 153 GLU GLU A . n 
A 1 159 ALA 159 154 154 ALA ALA A . n 
A 1 160 MET 160 155 155 MET MET A . n 
A 1 161 ASP 161 156 156 ASP ASP A . n 
A 1 162 ILE 162 157 157 ILE ILE A . n 
A 1 163 SER 163 158 158 SER SER A . n 
A 1 164 LYS 164 159 159 LYS LYS A . n 
A 1 165 LYS 165 160 160 LYS LYS A . n 
A 1 166 GLU 166 161 161 GLU GLU A . n 
A 1 167 MET 167 162 162 MET MET A . n 
A 1 168 PRO 168 163 163 PRO PRO A . n 
A 1 169 PRO 169 164 164 PRO PRO A . n 
A 1 170 THR 170 165 165 THR THR A . n 
A 1 171 ASN 171 166 166 ASN ASN A . n 
A 1 172 PRO 172 167 167 PRO PRO A . n 
A 1 173 ILE 173 168 168 ILE ILE A . n 
A 1 174 ARG 174 169 169 ARG ARG A . n 
A 1 175 LEU 175 170 170 LEU LEU A . n 
A 1 176 GLY 176 171 171 GLY GLY A . n 
A 1 177 LEU 177 172 172 LEU LEU A . n 
A 1 178 ALA 178 173 173 ALA ALA A . n 
A 1 179 LEU 179 174 174 LEU LEU A . n 
A 1 180 ASN 180 175 175 ASN ASN A . n 
A 1 181 PHE 181 176 176 PHE PHE A . n 
A 1 182 SER 182 177 177 SER SER A . n 
A 1 183 VAL 183 178 178 VAL VAL A . n 
A 1 184 PHE 184 179 179 PHE PHE A . n 
A 1 185 HIS 185 180 180 HIS HIS A . n 
A 1 186 TYR 186 181 181 TYR TYR A . n 
A 1 187 GLU 187 182 182 GLU GLU A . n 
A 1 188 ILE 188 183 183 ILE ILE A . n 
A 1 189 ALA 189 184 184 ALA ALA A . n 
A 1 190 ASN 190 185 185 ASN ASN A . n 
A 1 191 SER 191 186 186 SER SER A . n 
A 1 192 PRO 192 187 187 PRO PRO A . n 
A 1 193 GLU 193 188 188 GLU GLU A . n 
A 1 194 GLU 194 189 189 GLU GLU A . n 
A 1 195 ALA 195 190 190 ALA ALA A . n 
A 1 196 ILE 196 191 191 ILE ILE A . n 
A 1 197 SER 197 192 192 SER SER A . n 
A 1 198 LEU 198 193 193 LEU LEU A . n 
A 1 199 ALA 199 194 194 ALA ALA A . n 
A 1 200 LYS 200 195 195 LYS LYS A . n 
A 1 201 THR 201 196 196 THR THR A . n 
A 1 202 THR 202 197 197 THR THR A . n 
A 1 203 PHE 203 198 198 PHE PHE A . n 
A 1 204 ASP 204 199 199 ASP ASP A . n 
A 1 205 GLU 205 200 200 GLU GLU A . n 
A 1 206 ALA 206 201 201 ALA ALA A . n 
A 1 207 MET 207 202 202 MET MET A . n 
A 1 208 ALA 208 203 203 ALA ALA A . n 
A 1 209 ASP 209 204 204 ASP ASP A . n 
A 1 210 LEU 210 205 205 LEU LEU A . n 
A 1 211 HIS 211 206 206 HIS HIS A . n 
A 1 212 THR 212 207 207 THR THR A . n 
A 1 213 LEU 213 208 208 LEU LEU A . n 
A 1 214 SER 214 209 209 SER SER A . n 
A 1 215 GLU 215 210 210 GLU GLU A . n 
A 1 216 ASP 216 211 211 ASP ASP A . n 
A 1 217 SER 217 212 212 SER SER A . n 
A 1 218 TYR 218 213 213 TYR TYR A . n 
A 1 219 LYS 219 214 214 LYS LYS A . n 
A 1 220 ASP 220 215 215 ASP ASP A . n 
A 1 221 SER 221 216 216 SER SER A . n 
A 1 222 THR 222 217 217 THR THR A . n 
A 1 223 LEU 223 218 218 LEU LEU A . n 
A 1 224 ILE 224 219 219 ILE ILE A . n 
A 1 225 MET 225 220 220 MET MET A . n 
A 1 226 GLN 226 221 221 GLN GLN A . n 
A 1 227 LEU 227 222 222 LEU LEU A . n 
A 1 228 LEU 228 223 223 LEU LEU A . n 
A 1 229 ARG 229 224 224 ARG ARG A . n 
A 1 230 ASP 230 225 225 ASP ASP A . n 
A 1 231 ASN 231 226 226 ASN ASN A . n 
A 1 232 LEU 232 227 227 LEU LEU A . n 
A 1 233 THR 233 228 228 THR THR A . n 
A 1 234 LEU 234 229 229 LEU LEU A . n 
A 1 235 TRP 235 230 230 TRP TRP A . n 
A 1 236 THR 236 231 231 THR THR A . n 
B 2 1   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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WQ9 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WQ9 
_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 WQ9 1   305 236 WQ9 385 A . 
H 4 MG  1   306 1   MG  MG  A . 
I 6 HOH 1   401 193 HOH HOH A . 
I 6 HOH 2   402 98  HOH HOH A . 
I 6 HOH 3   403 19  HOH HOH A . 
I 6 HOH 4   404 222 HOH HOH A . 
I 6 HOH 5   405 243 HOH HOH A . 
I 6 HOH 6   406 87  HOH HOH A . 
I 6 HOH 7   407 154 HOH HOH A . 
I 6 HOH 8   408 70  HOH HOH A . 
I 6 HOH 9   409 166 HOH HOH A . 
I 6 HOH 10  410 38  HOH HOH A . 
I 6 HOH 11  411 219 HOH HOH A . 
I 6 HOH 12  412 241 HOH HOH A . 
I 6 HOH 13  413 16  HOH HOH A . 
I 6 HOH 14  414 116 HOH HOH A . 
I 6 HOH 15  415 65  HOH HOH A . 
I 6 HOH 16  416 141 HOH HOH A . 
I 6 HOH 17  417 17  HOH HOH A . 
I 6 HOH 18  418 50  HOH HOH A . 
I 6 HOH 19  419 49  HOH HOH A . 
I 6 HOH 20  420 55  HOH HOH A . 
I 6 HOH 21  421 165 HOH HOH A . 
I 6 HOH 22  422 28  HOH HOH A . 
I 6 HOH 23  423 14  HOH HOH A . 
I 6 HOH 24  424 60  HOH HOH A . 
I 6 HOH 25  425 104 HOH HOH A . 
I 6 HOH 26  426 181 HOH HOH A . 
I 6 HOH 27  427 18  HOH HOH A . 
I 6 HOH 28  428 13  HOH HOH A . 
I 6 HOH 29  429 234 HOH HOH A . 
I 6 HOH 30  430 105 HOH HOH A . 
I 6 HOH 31  431 40  HOH HOH A . 
I 6 HOH 32  432 69  HOH HOH A . 
I 6 HOH 33  433 67  HOH HOH A . 
I 6 HOH 34  434 112 HOH HOH A . 
I 6 HOH 35  435 48  HOH HOH A . 
I 6 HOH 36  436 27  HOH HOH A . 
I 6 HOH 37  437 139 HOH HOH A . 
I 6 HOH 38  438 227 HOH HOH A . 
I 6 HOH 39  439 44  HOH HOH A . 
I 6 HOH 40  440 94  HOH HOH A . 
I 6 HOH 41  441 152 HOH HOH A . 
I 6 HOH 42  442 43  HOH HOH A . 
I 6 HOH 43  443 131 HOH HOH A . 
I 6 HOH 44  444 7   HOH HOH A . 
I 6 HOH 45  445 114 HOH HOH A . 
I 6 HOH 46  446 73  HOH HOH A . 
I 6 HOH 47  447 126 HOH HOH A . 
I 6 HOH 48  448 183 HOH HOH A . 
I 6 HOH 49  449 51  HOH HOH A . 
I 6 HOH 50  450 8   HOH HOH A . 
I 6 HOH 51  451 5   HOH HOH A . 
I 6 HOH 52  452 45  HOH HOH A . 
I 6 HOH 53  453 80  HOH HOH A . 
I 6 HOH 54  454 21  HOH HOH A . 
I 6 HOH 55  455 32  HOH HOH A . 
I 6 HOH 56  456 86  HOH HOH A . 
I 6 HOH 57  457 10  HOH HOH A . 
I 6 HOH 58  458 179 HOH HOH A . 
I 6 HOH 59  459 77  HOH HOH A . 
I 6 HOH 60  460 6   HOH HOH A . 
I 6 HOH 61  461 137 HOH HOH A . 
I 6 HOH 62  462 90  HOH HOH A . 
I 6 HOH 63  463 124 HOH HOH A . 
I 6 HOH 64  464 102 HOH HOH A . 
I 6 HOH 65  465 15  HOH HOH A . 
I 6 HOH 66  466 109 HOH HOH A . 
I 6 HOH 67  467 118 HOH HOH A . 
I 6 HOH 68  468 163 HOH HOH A . 
I 6 HOH 69  469 29  HOH HOH A . 
I 6 HOH 70  470 95  HOH HOH A . 
I 6 HOH 71  471 93  HOH HOH A . 
I 6 HOH 72  472 127 HOH HOH A . 
I 6 HOH 73  473 100 HOH HOH A . 
I 6 HOH 74  474 42  HOH HOH A . 
I 6 HOH 75  475 62  HOH HOH A . 
I 6 HOH 76  476 11  HOH HOH A . 
I 6 HOH 77  477 81  HOH HOH A . 
I 6 HOH 78  478 76  HOH HOH A . 
I 6 HOH 79  479 92  HOH HOH A . 
I 6 HOH 80  480 3   HOH HOH A . 
I 6 HOH 81  481 4   HOH HOH A . 
I 6 HOH 82  482 198 HOH HOH A . 
I 6 HOH 83  483 120 HOH HOH A . 
I 6 HOH 84  484 33  HOH HOH A . 
I 6 HOH 85  485 132 HOH HOH A . 
I 6 HOH 86  486 232 HOH HOH A . 
I 6 HOH 87  487 85  HOH HOH A . 
I 6 HOH 88  488 61  HOH HOH A . 
I 6 HOH 89  489 31  HOH HOH A . 
I 6 HOH 90  490 56  HOH HOH A . 
I 6 HOH 91  491 223 HOH HOH A . 
I 6 HOH 92  492 58  HOH HOH A . 
I 6 HOH 93  493 36  HOH HOH A . 
I 6 HOH 94  494 140 HOH HOH A . 
I 6 HOH 95  495 171 HOH HOH A . 
I 6 HOH 96  496 39  HOH HOH A . 
I 6 HOH 97  497 231 HOH HOH A . 
I 6 HOH 98  498 115 HOH HOH A . 
I 6 HOH 99  499 88  HOH HOH A . 
I 6 HOH 100 500 122 HOH HOH A . 
I 6 HOH 101 501 59  HOH HOH A . 
I 6 HOH 102 502 153 HOH HOH A . 
I 6 HOH 103 503 173 HOH HOH A . 
I 6 HOH 104 504 195 HOH HOH A . 
I 6 HOH 105 505 83  HOH HOH A . 
I 6 HOH 106 506 236 HOH HOH A . 
I 6 HOH 107 507 111 HOH HOH A . 
I 6 HOH 108 508 151 HOH HOH A . 
I 6 HOH 109 509 35  HOH HOH A . 
I 6 HOH 110 510 143 HOH HOH A . 
I 6 HOH 111 511 37  HOH HOH A . 
I 6 HOH 112 512 161 HOH HOH A . 
I 6 HOH 113 513 9   HOH HOH A . 
I 6 HOH 114 514 107 HOH HOH A . 
I 6 HOH 115 515 26  HOH HOH A . 
I 6 HOH 116 516 148 HOH HOH A . 
I 6 HOH 117 517 12  HOH HOH A . 
I 6 HOH 118 518 20  HOH HOH A . 
I 6 HOH 119 519 103 HOH HOH A . 
I 6 HOH 120 520 249 HOH HOH A . 
I 6 HOH 121 521 229 HOH HOH A . 
I 6 HOH 122 522 71  HOH HOH A . 
I 6 HOH 123 523 186 HOH HOH A . 
I 6 HOH 124 524 214 HOH HOH A . 
I 6 HOH 125 525 149 HOH HOH A . 
I 6 HOH 126 526 180 HOH HOH A . 
I 6 HOH 127 527 106 HOH HOH A . 
I 6 HOH 128 528 82  HOH HOH A . 
I 6 HOH 129 529 164 HOH HOH A . 
I 6 HOH 130 530 202 HOH HOH A . 
I 6 HOH 131 531 189 HOH HOH A . 
I 6 HOH 132 532 224 HOH HOH A . 
I 6 HOH 133 533 47  HOH HOH A . 
I 6 HOH 134 534 169 HOH HOH A . 
I 6 HOH 135 535 101 HOH HOH A . 
I 6 HOH 136 536 64  HOH HOH A . 
I 6 HOH 137 537 209 HOH HOH A . 
I 6 HOH 138 538 25  HOH HOH A . 
I 6 HOH 139 539 57  HOH HOH A . 
I 6 HOH 140 540 142 HOH HOH A . 
I 6 HOH 141 541 216 HOH HOH A . 
I 6 HOH 142 542 242 HOH HOH A . 
I 6 HOH 143 543 74  HOH HOH A . 
I 6 HOH 144 544 121 HOH HOH A . 
I 6 HOH 145 545 199 HOH HOH A . 
I 6 HOH 146 546 226 HOH HOH A . 
I 6 HOH 147 547 136 HOH HOH A . 
I 6 HOH 148 548 177 HOH HOH A . 
I 6 HOH 149 549 168 HOH HOH A . 
I 6 HOH 150 550 2   HOH HOH A . 
I 6 HOH 151 551 208 HOH HOH A . 
I 6 HOH 152 552 72  HOH HOH A . 
I 6 HOH 153 553 113 HOH HOH A . 
I 6 HOH 154 554 235 HOH HOH A . 
I 6 HOH 155 555 233 HOH HOH A . 
I 6 HOH 156 556 245 HOH HOH A . 
I 6 HOH 157 557 192 HOH HOH A . 
I 6 HOH 158 558 96  HOH HOH A . 
I 6 HOH 159 559 159 HOH HOH A . 
I 6 HOH 160 560 205 HOH HOH A . 
I 6 HOH 161 561 228 HOH HOH A . 
I 6 HOH 162 562 46  HOH HOH A . 
I 6 HOH 163 563 79  HOH HOH A . 
I 6 HOH 164 564 108 HOH HOH A . 
I 6 HOH 165 565 68  HOH HOH A . 
I 6 HOH 166 566 128 HOH HOH A . 
I 6 HOH 167 567 175 HOH HOH A . 
I 6 HOH 168 568 238 HOH HOH A . 
I 6 HOH 169 569 218 HOH HOH A . 
I 6 HOH 170 570 110 HOH HOH A . 
I 6 HOH 171 571 230 HOH HOH A . 
I 6 HOH 172 572 156 HOH HOH A . 
I 6 HOH 173 573 133 HOH HOH A . 
I 6 HOH 174 574 89  HOH HOH A . 
I 6 HOH 175 575 170 HOH HOH A . 
I 6 HOH 176 576 194 HOH HOH A . 
I 6 HOH 177 577 207 HOH HOH A . 
I 6 HOH 178 578 23  HOH HOH A . 
I 6 HOH 179 579 187 HOH HOH A . 
I 6 HOH 180 580 244 HOH HOH A . 
I 6 HOH 181 581 221 HOH HOH A . 
I 6 HOH 182 582 160 HOH HOH A . 
I 6 HOH 183 583 84  HOH HOH A . 
I 6 HOH 184 584 52  HOH HOH A . 
I 6 HOH 185 585 117 HOH HOH A . 
I 6 HOH 186 586 63  HOH HOH A . 
I 6 HOH 187 587 138 HOH HOH A . 
I 6 HOH 188 588 155 HOH HOH A . 
I 6 HOH 189 589 212 HOH HOH A . 
I 6 HOH 190 590 66  HOH HOH A . 
I 6 HOH 191 591 125 HOH HOH A . 
I 6 HOH 192 592 213 HOH HOH A . 
I 6 HOH 193 593 53  HOH HOH A . 
I 6 HOH 194 594 75  HOH HOH A . 
I 6 HOH 195 595 147 HOH HOH A . 
I 6 HOH 196 596 210 HOH HOH A . 
I 6 HOH 197 597 119 HOH HOH A . 
I 6 HOH 198 598 34  HOH HOH A . 
I 6 HOH 199 599 220 HOH HOH A . 
I 6 HOH 200 600 130 HOH HOH A . 
I 6 HOH 201 601 184 HOH HOH A . 
I 6 HOH 202 602 211 HOH HOH A . 
I 6 HOH 203 603 162 HOH HOH A . 
I 6 HOH 204 604 97  HOH HOH A . 
I 6 HOH 205 605 246 HOH HOH A . 
I 6 HOH 206 606 217 HOH HOH A . 
J 6 HOH 1   301 123 HOH HOH P . 
J 6 HOH 2   302 41  HOH HOH P . 
J 6 HOH 3   303 78  HOH HOH P . 
J 6 HOH 4   304 178 HOH HOH P . 
J 6 HOH 5   305 30  HOH HOH P . 
J 6 HOH 6   306 22  HOH HOH P . 
J 6 HOH 7   307 24  HOH HOH P . 
J 6 HOH 8   308 150 HOH HOH P . 
J 6 HOH 9   309 91  HOH HOH P . 
J 6 HOH 10  310 172 HOH HOH P . 
J 6 HOH 11  311 99  HOH HOH P . 
J 6 HOH 12  312 54  HOH HOH P . 
J 6 HOH 13  313 134 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                     9EW4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     81.874 
_cell.length_a_esd                 ? 
_cell.length_b                     112.610 
_cell.length_b_esd                 ? 
_cell.length_c                     62.992 
_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                         9EW4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_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                   9EW4 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.63 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.19 
_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 EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-16 
_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   0.873128 
_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 ID23-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.873128 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-2 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EW4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.60 
_reflns.d_resolution_low                               62.99 
_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                                     38411 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_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                                    1.60 
_reflns_shell.d_res_low                                     1.63 
_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                             1903 
_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                                  0.496 
_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]                            1.55 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.62 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.93 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.627 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.946 
_refine.details                                  
;HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
U VALUES : REFINED INDIVIDUALLY
;
_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                                 9EW4 
_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                            1.60 
_refine.ls_d_res_low                             56.37 
_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                     36427 
_refine.ls_number_reflns_R_free                  1962 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.90 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18119 
_refine.ls_R_factor_R_free                       0.21092 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17963 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.083 
_refine.pdbx_overall_ESU_R_Free                  0.084 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             1.00 
_refine.pdbx_solvent_shrinkage_radii             1.00 
_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                             1.976 
_refine.overall_SU_ML                            0.065 
_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                       1.60 
_refine_hist.d_res_low                        56.37 
_refine_hist.number_atoms_solvent             219 
_refine_hist.number_atoms_total               2176 
_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        1929 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.017  0.016  1994 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1884 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 3.715  1.838  2704 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 0.561  1.567  4357 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 8.741  5.288  260  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 4.079  20.000 2    ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.252 10.000 372  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 0.122  0.200  297  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  2314 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  430  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 2.030  1.998  982  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.025  1.998  982  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 3.105  3.821  1225 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 3.097  3.655  1223 ? r_mcangle_other        ? ? 
'X-RAY DIFFRACTION' ? 3.384  2.399  1012 ? r_scbond_it            ? ? 
'X-RAY DIFFRACTION' ? 3.382  2.399  1013 ? r_scbond_other         ? ? 
'X-RAY DIFFRACTION' ? 5.279  4.561  1478 ? r_scangle_other        ? ? 
'X-RAY DIFFRACTION' ? 6.838  23.870 2399 ? r_long_range_B_refined ? ? 
'X-RAY DIFFRACTION' ? 6.759  22.740 2336 ? r_long_range_B_other   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.600 
_refine_ls_shell.d_res_low                        1.641 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             154 
_refine_ls_shell.number_reflns_R_work             2705 
_refine_ls_shell.percent_reflns_obs               99.83 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.294 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.275 
# 
_struct.entry_id                     9EW4 
_struct.title                        'Ternary structure of 14-3-3s, C-RAF phosphopeptide 12mer (pS259) and compound 86 (1124384)' 
_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        9EW4 
_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 UNP RAF1_HUMAN  P04049 ? 2 QRSTSTPNV 255 
# 
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 9EW4 A 6 ? 236 ? P31947 1   ? 231 ? 1   231 
2 2 9EW4 P 1 ? 9   ? P04049 255 ? 263 ? 255 263 
# 
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 9EW4 GLY A 1 ? UNP P31947 ? ? 'expression tag' -4 1 
1 9EW4 ALA A 2 ? UNP P31947 ? ? 'expression tag' -3 2 
1 9EW4 MET A 3 ? UNP P31947 ? ? 'expression tag' -2 3 
1 9EW4 GLY A 4 ? UNP P31947 ? ? 'expression tag' -1 4 
1 9EW4 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)' 5750  ? 
1 MORE         -79   ? 
1 'SSA (A^2)'  24020 ? 
# 
_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' 4_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 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 7   ? ALA A 21  ? GLU A 2   ALA A 16  1 ? 15 
HELX_P HELX_P2  AA2 ARG A 23  ? LYS A 37  ? ARG A 18  LYS A 32  1 ? 15 
HELX_P HELX_P3  AA3 SER A 42  ? ASN A 75  ? SER A 37  ASN A 70  1 ? 34 
HELX_P HELX_P4  AA4 PRO A 84  ? SER A 110 ? PRO A 79  SER A 105 1 ? 27 
HELX_P HELX_P5  AA5 HIS A 111 ? ALA A 116 ? HIS A 106 ALA A 111 1 ? 6  
HELX_P HELX_P6  AA6 ASP A 118 ? ALA A 140 ? ASP A 113 ALA A 135 1 ? 23 
HELX_P HELX_P7  AA7 ASP A 144 ? MET A 167 ? ASP A 139 MET A 162 1 ? 24 
HELX_P HELX_P8  AA8 ASN A 171 ? ILE A 188 ? ASN A 166 ILE A 183 1 ? 18 
HELX_P HELX_P9  AA9 SER A 191 ? ALA A 208 ? SER A 186 ALA A 203 1 ? 18 
HELX_P HELX_P10 AB1 ASP A 209 ? LEU A 213 ? ASP A 204 LEU A 208 5 ? 5  
HELX_P HELX_P11 AB2 SER A 214 ? THR A 236 ? SER A 209 THR A 231 1 ? 23 
# 
_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 WQ9 . C2 ? ? A CYS 38  A WQ9 305 1_555 ? ? ? ? ? ? ? 1.987 ? ? 
covale2  covale both ? B THR 4   C   ? ? ? 1_555 B SEP 5 N  ? ? P THR 258 P SEP 259 1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale3  covale both ? B SEP 5   C   ? ? ? 1_555 B THR 6 N  ? ? P SEP 259 P THR 260 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
metalc1  metalc ?    ? A GLU 7   OE1 ? ? ? 1_555 F MG  . MG ? ? A GLU 2   A MG  304 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc2  metalc ?    ? A GLU 7   OE1 ? ? ? 1_555 F MG  . MG ? ? A GLU 2   A MG  304 3_654 ? ? ? ? ? ? ? 2.327 ? ? 
metalc3  metalc ?    ? A GLU 40  OE1 ? ? ? 1_555 H MG  . MG ? ? A GLU 35  A MG  306 1_555 ? ? ? ? ? ? ? 2.680 ? ? 
metalc4  metalc ?    ? A GLU 40  OE2 ? ? ? 1_555 H MG  . MG ? ? A GLU 35  A MG  306 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc5  metalc ?    ? A GLU 80  OE1 ? ? ? 1_555 E MG  . MG ? ? A GLU 75  A MG  303 1_555 ? ? ? ? ? ? ? 2.228 ? ? 
metalc6  metalc ?    ? A GLU 94  OE2 ? ? ? 1_555 D MG  . MG ? ? A GLU 89  A MG  302 1_555 ? ? ? ? ? ? ? 2.441 ? ? 
metalc7  metalc ?    ? A GLU 115 O   ? ? ? 1_555 H MG  . MG ? ? A GLU 110 A MG  306 1_555 ? ? ? ? ? ? ? 2.254 ? ? 
metalc8  metalc ?    ? A GLU 166 O   ? ? ? 1_555 E MG  . MG ? ? A GLU 161 A MG  303 7_555 ? ? ? ? ? ? ? 2.264 ? ? 
metalc9  metalc ?    ? A GLU 193 OE2 ? ? ? 1_555 H MG  . MG ? ? A GLU 188 A MG  306 6_555 ? ? ? ? ? ? ? 2.262 ? ? 
metalc10 metalc ?    ? D MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  302 A HOH 412 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
metalc11 metalc ?    ? D MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  302 A HOH 448 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc12 metalc ?    ? D MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  302 A HOH 542 1_555 ? ? ? ? ? ? ? 2.182 ? ? 
metalc13 metalc ?    ? D MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  302 A HOH 569 1_555 ? ? ? ? ? ? ? 2.189 ? ? 
metalc14 metalc ?    ? F MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  304 A HOH 423 1_555 ? ? ? ? ? ? ? 2.498 ? ? 
metalc15 metalc ?    ? F MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  304 A HOH 423 3_654 ? ? ? ? ? ? ? 2.498 ? ? 
metalc16 metalc ?    ? F MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  304 A HOH 442 1_555 ? ? ? ? ? ? ? 1.888 ? ? 
metalc17 metalc ?    ? F MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  304 A HOH 442 3_654 ? ? ? ? ? ? ? 1.888 ? ? 
metalc18 metalc ?    ? H MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  306 A HOH 479 1_555 ? ? ? ? ? ? ? 2.310 ? ? 
metalc19 metalc ?    ? H MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  306 A HOH 491 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc20 metalc ?    ? H MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  306 A HOH 525 6_554 ? ? ? ? ? ? ? 2.491 ? ? 
# 
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  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 OE1 ? A GLU 7   ? A GLU 2   ? 1_555 0.0   ? 
2  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 423 ? 1_555 77.0  ? 
3  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 423 ? 1_555 77.0  ? 
4  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 423 ? 3_654 82.7  ? 
5  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 423 ? 3_654 82.7  ? 
6  O   ? I HOH .   ? A HOH 423 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 423 ? 3_654 152.5 ? 
7  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 442 ? 1_555 78.1  ? 
8  OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 442 ? 1_555 78.1  ? 
9  O   ? I HOH .   ? A HOH 423 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 442 ? 1_555 131.0 ? 
10 O   ? I HOH .   ? A HOH 423 ? 3_654 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 442 ? 1_555 60.4  ? 
11 OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 442 ? 3_654 135.4 ? 
12 OE1 ? A GLU 7   ? A GLU 2   ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 442 ? 3_654 135.4 ? 
13 O   ? I HOH .   ? A HOH 423 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 442 ? 3_654 60.4  ? 
14 O   ? I HOH .   ? A HOH 423 ? 3_654 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 442 ? 3_654 131.0 ? 
15 O   ? I HOH .   ? A HOH 442 ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O   ? I HOH .   ? A HOH 442 ? 3_654 140.0 ? 
16 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 52.4  ? 
17 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? A GLU 115 ? A GLU 110 ? 1_555 86.8  ? 
18 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? A GLU 115 ? A GLU 110 ? 1_555 87.3  ? 
19 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 85.3  ? 
20 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 122.1 ? 
21 O   ? A GLU 115 ? A GLU 110 ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 48.4  ? 
22 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 479 ? 1_555 85.1  ? 
23 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 479 ? 1_555 77.3  ? 
24 O   ? A GLU 115 ? A GLU 110 ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 479 ? 1_555 164.4 ? 
25 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 479 ? 1_555 143.6 ? 
26 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 491 ? 1_555 136.5 ? 
27 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 491 ? 1_555 84.1  ? 
28 O   ? A GLU 115 ? A GLU 110 ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 491 ? 1_555 91.1  ? 
29 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 491 ? 1_555 124.1 ? 
30 O   ? I HOH .   ? A HOH 479 ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 491 ? 1_555 85.6  ? 
31 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 525 ? 6_554 135.9 ? 
32 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 525 ? 6_554 154.8 ? 
33 O   ? A GLU 115 ? A GLU 110 ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 525 ? 6_554 114.9 ? 
34 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 525 ? 6_554 82.9  ? 
35 O   ? I HOH .   ? A HOH 479 ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 525 ? 6_554 80.0  ? 
36 O   ? I HOH .   ? A HOH 491 ? 1_555 MG ? H MG . ? A MG 306 ? 1_555 O   ? I HOH .   ? A HOH 525 ? 6_554 83.6  ? 
37 OE1 ? A GLU 80  ? A GLU 75  ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? A GLU 166 ? A GLU 161 ? 1_555 69.1  ? 
38 OE2 ? A GLU 94  ? A GLU 89  ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 412 ? 1_555 69.1  ? 
39 OE2 ? A GLU 94  ? A GLU 89  ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 448 ? 1_555 88.1  ? 
40 O   ? I HOH .   ? A HOH 412 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 448 ? 1_555 131.2 ? 
41 OE2 ? A GLU 94  ? A GLU 89  ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 542 ? 1_555 92.8  ? 
42 O   ? I HOH .   ? A HOH 412 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 542 ? 1_555 71.7  ? 
43 O   ? I HOH .   ? A HOH 448 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 542 ? 1_555 154.9 ? 
44 OE2 ? A GLU 94  ? A GLU 89  ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 569 ? 1_555 112.8 ? 
45 O   ? I HOH .   ? A HOH 412 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 569 ? 1_555 154.2 ? 
46 O   ? I HOH .   ? A HOH 448 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 569 ? 1_555 74.1  ? 
47 O   ? I HOH .   ? A HOH 542 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? I HOH .   ? A HOH 569 ? 1_555 82.5  ? 
# 
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 WQ9 G . ? CYS A 43 ? WQ9 A 305 ? 1_555 CYS A 38 ? 1_555 C2 SG CYS 1 WQ9 None            'Covalent chemical modification' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           110 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            105 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   HIS 
_struct_mon_prot_cis.pdbx_label_seq_id_2    111 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    HIS 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     106 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       8.63 
# 
_pdbx_entry_details.entry_id                   9EW4 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    438 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   P 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    313 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    GLU 
_pdbx_validate_symm_contact.auth_seq_id_1     110 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OH 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    TYR 
_pdbx_validate_symm_contact.auth_seq_id_2     213 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   8_555 
_pdbx_validate_symm_contact.dist              1.82 
# 
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  ? ? -103.62 73.85 
2 1 ASN A 70  ? ? -97.90  53.71 
3 1 HIS A 106 ? ? -142.91 35.97 
4 1 THR A 136 ? ? -155.50 52.43 
# 
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  ? ? 0.077 'SIDE CHAIN' 
2 1 ARG A 148 ? ? 0.236 'SIDE CHAIN' 
3 1 ARG P 256 ? ? 0.095 'SIDE CHAIN' 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    B 
_pdbx_struct_mod_residue.label_comp_id    SEP 
_pdbx_struct_mod_residue.label_seq_id     5 
_pdbx_struct_mod_residue.auth_asym_id     P 
_pdbx_struct_mod_residue.auth_comp_id     SEP 
_pdbx_struct_mod_residue.auth_seq_id      259 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   SER 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    MG 
_pdbx_struct_special_symmetry.auth_seq_id     304 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   MG 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 
WQ9 O1   O  N N 412 
WQ9 C1   C  N N 413 
WQ9 C2   C  N N 414 
WQ9 N1   N  N N 415 
WQ9 C3   C  N N 416 
WQ9 C4   C  N N 417 
WQ9 C5   C  N R 418 
WQ9 C6   C  N N 419 
WQ9 C7   C  N N 420 
WQ9 N2   N  N N 421 
WQ9 S1   S  N N 422 
WQ9 O2   O  N N 423 
WQ9 O3   O  N N 424 
WQ9 C8   C  Y N 425 
WQ9 C9   C  Y N 426 
WQ9 C10  C  Y N 427 
WQ9 C11  C  Y N 428 
WQ9 BR1  BR N N 429 
WQ9 C12  C  Y N 430 
WQ9 F1   F  N N 431 
WQ9 C13  C  Y N 432 
WQ9 C14  C  N N 433 
WQ9 C15  C  N N 434 
WQ9 H1   H  N N 435 
WQ9 H2   H  N N 436 
WQ9 H4   H  N N 437 
WQ9 H5   H  N N 438 
WQ9 H6   H  N N 439 
WQ9 H7   H  N N 440 
WQ9 H8   H  N N 441 
WQ9 H9   H  N N 442 
WQ9 H10  H  N N 443 
WQ9 H11  H  N N 444 
WQ9 H12  H  N N 445 
WQ9 H13  H  N N 446 
WQ9 H14  H  N N 447 
WQ9 H15  H  N N 448 
WQ9 H16  H  N N 449 
WQ9 H17  H  N N 450 
WQ9 H18  H  N N 451 
WQ9 CL1  CL N N 452 
# 
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 
WQ9 C2  C1   sing N N 394 
WQ9 O1  C1   doub N N 395 
WQ9 C1  N1   sing N N 396 
WQ9 N1  C3   sing N N 397 
WQ9 N1  C15  sing N N 398 
WQ9 C3  C4   sing N N 399 
WQ9 C15 C5   sing N N 400 
WQ9 O2  S1   doub N N 401 
WQ9 C14 C5   sing N N 402 
WQ9 C14 N2   sing N N 403 
WQ9 F1  C12  sing N N 404 
WQ9 C4  C5   sing N N 405 
WQ9 C5  C6   sing N N 406 
WQ9 C13 C12  doub Y N 407 
WQ9 C13 C8   sing Y N 408 
WQ9 N2  S1   sing N N 409 
WQ9 N2  C7   sing N N 410 
WQ9 S1  C8   sing N N 411 
WQ9 S1  O3   doub N N 412 
WQ9 C12 C11  sing Y N 413 
WQ9 C8  C9   doub Y N 414 
WQ9 C6  C7   sing N N 415 
WQ9 C11 BR1  sing N N 416 
WQ9 C11 C10  doub Y N 417 
WQ9 C9  C10  sing Y N 418 
WQ9 C2  H1   sing N N 419 
WQ9 C2  H2   sing N N 420 
WQ9 C3  H4   sing N N 421 
WQ9 C3  H5   sing N N 422 
WQ9 C4  H6   sing N N 423 
WQ9 C4  H7   sing N N 424 
WQ9 C6  H8   sing N N 425 
WQ9 C6  H9   sing N N 426 
WQ9 C7  H10  sing N N 427 
WQ9 C7  H11  sing N N 428 
WQ9 C9  H12  sing N N 429 
WQ9 C10 H13  sing N N 430 
WQ9 C13 H14  sing N N 431 
WQ9 C14 H15  sing N N 432 
WQ9 C14 H16  sing N N 433 
WQ9 C15 H17  sing N N 434 
WQ9 C15 H18  sing N N 435 
WQ9 C2  CL1  sing N N 436 
# 
_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                    9EW4 
_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]   0.012214 
_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]   0.008880 
_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]   0.015875 
_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   ? 45.392 12.142  -4.235  1.00 37.11  ? -4  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 1   ? 43.977 11.795  -4.238  1.00 33.48  ? -4  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 1   ? 43.722 11.115  -5.568  1.00 32.86  ? -4  GLY A C   1 
ATOM   4    O  O   . GLY A 1 1   ? 44.268 11.562  -6.585  1.00 31.21  ? -4  GLY A O   1 
ATOM   5    N  N   . ALA A 1 2   ? 42.939 10.029  -5.521  1.00 28.81  ? -3  ALA A N   1 
ATOM   6    C  CA  . ALA A 1 2   ? 42.706 9.185   -6.675  1.00 30.43  ? -3  ALA A CA  1 
ATOM   7    C  C   . ALA A 1 2   ? 41.960 9.919   -7.785  1.00 26.83  ? -3  ALA A C   1 
ATOM   8    O  O   . ALA A 1 2   ? 42.011 9.506   -8.939  1.00 28.68  ? -3  ALA A O   1 
ATOM   9    C  CB  . ALA A 1 2   ? 41.927 7.944   -6.247  1.00 34.34  ? -3  ALA A CB  1 
ATOM   10   N  N   . MET A 1 3   ? 41.280 11.017  -7.441  1.00 23.56  ? -2  MET A N   1 
ATOM   11   C  CA  . MET A 1 3   ? 40.528 11.788  -8.425  1.00 20.27  ? -2  MET A CA  1 
ATOM   12   C  C   . MET A 1 3   ? 41.311 12.973  -8.975  1.00 18.50  ? -2  MET A C   1 
ATOM   13   O  O   . MET A 1 3   ? 40.770 13.743  -9.781  1.00 17.48  ? -2  MET A O   1 
ATOM   14   C  CB  . MET A 1 3   ? 39.211 12.279  -7.799  1.00 20.32  ? -2  MET A CB  1 
ATOM   15   C  CG  . MET A 1 3   ? 38.366 11.185  -7.328  1.00 20.45  ? -2  MET A CG  1 
ATOM   16   S  SD  . MET A 1 3   ? 37.853 9.986   -8.571  1.00 20.51  ? -2  MET A SD  1 
ATOM   17   C  CE  . MET A 1 3   ? 36.924 8.811   -7.570  1.00 26.10  ? -2  MET A CE  1 
ATOM   18   N  N   . GLY A 1 4   ? 42.588 13.089  -8.558  1.00 17.34  ? -1  GLY A N   1 
ATOM   19   C  CA  . GLY A 1 4   ? 43.430 14.209  -8.942  1.00 16.02  ? -1  GLY A CA  1 
ATOM   20   C  C   . GLY A 1 4   ? 43.628 14.343  -10.466 1.00 17.54  ? -1  GLY A C   1 
ATOM   21   O  O   . GLY A 1 4   ? 43.807 15.456  -10.994 1.00 17.67  ? -1  GLY A O   1 
ATOM   22   N  N   . SER A 1 5   ? 43.584 13.207  -11.165 1.00 15.44  ? 0   SER A N   1 
ATOM   23   C  CA  . SER A 1 5   ? 43.820 13.208  -12.600 1.00 14.69  ? 0   SER A CA  1 
ATOM   24   C  C   . SER A 1 5   ? 42.565 13.433  -13.442 1.00 13.71  ? 0   SER A C   1 
ATOM   25   O  O   . SER A 1 5   ? 42.652 13.538  -14.660 1.00 13.92  ? 0   SER A O   1 
ATOM   26   C  CB  . SER A 1 5   ? 44.489 11.903  -13.049 1.00 17.94  ? 0   SER A CB  1 
ATOM   27   O  OG  . SER A 1 5   ? 43.596 10.819  -12.807 1.00 19.60  ? 0   SER A OG  1 
ATOM   28   N  N   . MET A 1 6   ? 41.366 13.468  -12.819 1.00 12.86  ? 1   MET A N   1 
ATOM   29   C  CA  . MET A 1 6   ? 40.133 13.597  -13.577 1.00 12.96  ? 1   MET A CA  1 
ATOM   30   C  C   . MET A 1 6   ? 39.667 15.052  -13.617 1.00 13.37  ? 1   MET A C   1 
ATOM   31   O  O   . MET A 1 6   ? 39.720 15.740  -12.589 1.00 14.26  ? 1   MET A O   1 
ATOM   32   C  CB  . MET A 1 6   ? 39.014 12.735  -12.961 1.00 15.08  ? 1   MET A CB  1 
ATOM   33   C  CG  . MET A 1 6   ? 37.966 12.416  -13.974 1.00 16.19  ? 1   MET A CG  1 
ATOM   34   S  SD  . MET A 1 6   ? 36.517 11.476  -13.351 1.00 17.93  ? 1   MET A SD  1 
ATOM   35   C  CE  . MET A 1 6   ? 37.366 10.209  -12.534 1.00 18.54  ? 1   MET A CE  1 
ATOM   36   N  N   . GLU A 1 7   ? 39.193 15.500  -14.788 1.00 12.23  ? 2   GLU A N   1 
ATOM   37   C  CA  . GLU A 1 7   ? 38.627 16.840  -14.926 1.00 13.54  ? 2   GLU A CA  1 
ATOM   38   C  C   . GLU A 1 7   ? 37.497 17.094  -13.918 1.00 13.19  ? 2   GLU A C   1 
ATOM   39   O  O   . GLU A 1 7   ? 36.628 16.255  -13.674 1.00 13.43  ? 2   GLU A O   1 
ATOM   40   C  CB  . GLU A 1 7   ? 38.050 17.040  -16.312 1.00 14.29  ? 2   GLU A CB  1 
ATOM   41   C  CG  . GLU A 1 7   ? 39.072 17.108  -17.431 1.00 15.70  ? 2   GLU A CG  1 
ATOM   42   C  CD  . GLU A 1 7   ? 39.740 18.455  -17.571 1.00 19.20  ? 2   GLU A CD  1 
ATOM   43   O  OE1 . GLU A 1 7   ? 39.649 19.283  -16.631 1.00 20.26  ? 2   GLU A OE1 1 
ATOM   44   O  OE2 . GLU A 1 7   ? 40.332 18.709  -18.657 1.00 19.47  ? 2   GLU A OE2 1 
ATOM   45   N  N   . ARG A 1 8   ? 37.434 18.334  -13.413 1.00 13.76  ? 3   ARG A N   1 
ATOM   46   C  CA  . ARG A 1 8   ? 36.291 18.756  -12.595 1.00 14.55  ? 3   ARG A CA  1 
ATOM   47   C  C   . ARG A 1 8   ? 34.925 18.456  -13.209 1.00 14.18  ? 3   ARG A C   1 
ATOM   48   O  O   . ARG A 1 8   ? 34.065 17.885  -12.540 1.00 14.77  ? 3   ARG A O   1 
ATOM   49   C  CB  . ARG A 1 8   ? 36.421 20.249  -12.268 1.00 14.51  ? 3   ARG A CB  1 
ATOM   50   C  CG  . ARG A 1 8   ? 35.405 20.732  -11.221 1.00 14.62  ? 3   ARG A CG  1 
ATOM   51   C  CD  . ARG A 1 8   ? 35.552 22.247  -11.003 1.00 16.34  ? 3   ARG A CD  1 
ATOM   52   N  NE  . ARG A 1 8   ? 34.762 22.688  -9.863  1.00 16.93  ? 3   ARG A NE  1 
ATOM   53   C  CZ  . ARG A 1 8   ? 33.448 22.837  -9.827  1.00 16.93  ? 3   ARG A CZ  1 
ATOM   54   N  NH1 . ARG A 1 8   ? 32.685 22.564  -10.868 1.00 19.32  ? 3   ARG A NH1 1 
ATOM   55   N  NH2 . ARG A 1 8   ? 32.889 23.313  -8.710  1.00 17.95  ? 3   ARG A NH2 1 
ATOM   56   N  N   . ALA A 1 9   ? 34.726 18.818  -14.486 1.00 14.26  ? 4   ALA A N   1 
ATOM   57   C  CA  . ALA A 1 9   ? 33.449 18.605  -15.141 1.00 15.35  ? 4   ALA A CA  1 
ATOM   58   C  C   . ALA A 1 9   ? 33.098 17.106  -15.232 1.00 12.85  ? 4   ALA A C   1 
ATOM   59   O  O   . ALA A 1 9   ? 31.940 16.713  -15.074 1.00 14.03  ? 4   ALA A O   1 
ATOM   60   C  CB  . ALA A 1 9   ? 33.409 19.245  -16.496 1.00 16.30  ? 4   ALA A CB  1 
ATOM   61   N  N   . SER A 1 10  ? 34.113 16.277  -15.471 1.00 12.37  ? 5   SER A N   1 
ATOM   62   C  CA  . SER A 1 10  ? 33.957 14.827  -15.507 1.00 13.00  ? 5   SER A CA  1 
ATOM   63   C  C   . SER A 1 10  ? 33.559 14.244  -14.143 1.00 12.19  ? 5   SER A C   1 
ATOM   64   O  O   . SER A 1 10  ? 32.687 13.377  -14.074 1.00 13.11  ? 5   SER A O   1 
ATOM   65   C  CB  . SER A 1 10  ? 35.259 14.172  -16.002 1.00 12.68  ? 5   SER A CB  1 
ATOM   66   O  OG  . SER A 1 10  ? 35.502 14.593  -17.338 1.00 14.01  ? 5   SER A OG  1 
ATOM   67   N  N   . LEU A 1 11  ? 34.174 14.735  -13.070 1.00 13.08  ? 6   LEU A N   1 
ATOM   68   C  CA  . LEU A 1 11  ? 33.791 14.345  -11.712 1.00 12.57  ? 6   LEU A CA  1 
ATOM   69   C  C   . LEU A 1 11  ? 32.343 14.681  -11.392 1.00 12.56  ? 6   LEU A C   1 
ATOM   70   O  O   . LEU A 1 11  ? 31.623 13.838  -10.864 1.00 12.18  ? 6   LEU A O   1 
ATOM   71   C  CB  . LEU A 1 11  ? 34.707 15.020  -10.705 1.00 12.29  ? 6   LEU A CB  1 
ATOM   72   C  CG  . LEU A 1 11  ? 36.138 14.483  -10.711 1.00 14.58  ? 6   LEU A CG  1 
ATOM   73   C  CD1 . LEU A 1 11  ? 37.099 15.374  -10.018 1.00 15.88  ? 6   LEU A CD1 1 
ATOM   74   C  CD2 . LEU A 1 11  ? 36.218 13.094  -10.056 1.00 14.37  ? 6   LEU A CD2 1 
ATOM   75   N  N   . ILE A 1 12  ? 31.909 15.885  -11.782 1.00 13.13  ? 7   ILE A N   1 
ATOM   76   C  CA  . ILE A 1 12  ? 30.516 16.265  -11.600 1.00 14.02  ? 7   ILE A CA  1 
ATOM   77   C  C   . ILE A 1 12  ? 29.570 15.383  -12.417 1.00 13.42  ? 7   ILE A C   1 
ATOM   78   O  O   . ILE A 1 12  ? 28.585 14.883  -11.886 1.00 12.43  ? 7   ILE A O   1 
ATOM   79   C  CB  . ILE A 1 12  ? 30.353 17.764  -11.879 1.00 14.56  ? 7   ILE A CB  1 
ATOM   80   C  CG1 . ILE A 1 12  ? 31.209 18.635  -10.896 1.00 18.58  ? 7   ILE A CG1 1 
ATOM   81   C  CG2 . ILE A 1 12  ? 28.906 18.087  -11.861 1.00 15.76  ? 7   ILE A CG2 1 
ATOM   82   C  CD1 . ILE A 1 12  ? 30.872 18.470  -9.482  1.00 20.53  ? 7   ILE A CD1 1 
ATOM   83   N  N   . GLN A 1 13  ? 29.920 15.150  -13.687 1.00 14.02  ? 8   GLN A N   1 
ATOM   84   C  CA  . GLN A 1 13  ? 29.125 14.289  -14.557 1.00 14.85  ? 8   GLN A CA  1 
ATOM   85   C  C   . GLN A 1 13  ? 28.989 12.886  -13.959 1.00 13.31  ? 8   GLN A C   1 
ATOM   86   O  O   . GLN A 1 13  ? 27.894 12.310  -13.900 1.00 14.20  ? 8   GLN A O   1 
ATOM   87   C  CB  . GLN A 1 13  ? 29.769 14.239  -15.960 1.00 16.95  ? 8   GLN A CB  1 
ATOM   88   C  CG  . GLN A 1 13  ? 28.996 13.435  -16.984 1.00 20.91  ? 8   GLN A CG  1 
ATOM   89   C  CD  . GLN A 1 13  ? 29.649 13.460  -18.380 1.00 22.30  ? 8   GLN A CD  1 
ATOM   90   O  OE1 . GLN A 1 13  ? 30.665 14.184  -18.604 1.00 25.21  ? 8   GLN A OE1 1 
ATOM   91   N  NE2 . GLN A 1 13  ? 29.060 12.681  -19.327 1.00 24.25  ? 8   GLN A NE2 1 
ATOM   92   N  N   . LYS A 1 14  ? 30.117 12.326  -13.502 1.00 12.77  ? 9   LYS A N   1 
ATOM   93   C  CA  . LYS A 1 14  ? 30.081 11.012  -12.883 1.00 12.26  ? 9   LYS A CA  1 
ATOM   94   C  C   . LYS A 1 14  ? 29.360 10.967  -11.540 1.00 12.45  ? 9   LYS A C   1 
ATOM   95   O  O   . LYS A 1 14  ? 28.725 9.955   -11.229 1.00 13.64  ? 9   LYS A O   1 
ATOM   96   C  CB  . LYS A 1 14  ? 31.485 10.437  -12.792 1.00 13.25  ? 9   LYS A CB  1 
ATOM   97   C  CG  . LYS A 1 14  ? 32.084 10.117  -14.140 1.00 12.99  ? 9   LYS A CG  1 
ATOM   98   C  CD  . LYS A 1 14  ? 33.503 9.562   -14.069 1.00 14.56  ? 9   LYS A CD  1 
ATOM   99   C  CE  . LYS A 1 14  ? 34.161 9.385   -15.429 1.00 13.93  ? 9   LYS A CE  1 
ATOM   100  N  NZ  . LYS A 1 14  ? 35.509 8.834   -15.310 1.00 15.07  ? 9   LYS A NZ  1 
ATOM   101  N  N   . ALA A 1 15  ? 29.434 12.035  -10.734 1.00 12.38  ? 10  ALA A N   1 
ATOM   102  C  CA  . ALA A 1 15  ? 28.635 12.077  -9.512  1.00 12.80  ? 10  ALA A CA  1 
ATOM   103  C  C   . ALA A 1 15  ? 27.146 11.947  -9.823  1.00 12.40  ? 10  ALA A C   1 
ATOM   104  O  O   . ALA A 1 15  ? 26.422 11.268  -9.100  1.00 12.38  ? 10  ALA A O   1 
ATOM   105  C  CB  . ALA A 1 15  ? 28.882 13.386  -8.740  1.00 13.11  ? 10  ALA A CB  1 
ATOM   106  N  N   . LYS A 1 16  ? 26.685 12.638  -10.885 1.00 13.03  ? 11  LYS A N   1 
ATOM   107  C  CA  . LYS A 1 16  ? 25.297 12.531  -11.297 1.00 13.84  ? 11  LYS A CA  1 
ATOM   108  C  C   . LYS A 1 16  ? 24.927 11.124  -11.768 1.00 14.18  ? 11  LYS A C   1 
ATOM   109  O  O   . LYS A 1 16  ? 23.851 10.629  -11.434 1.00 14.48  ? 11  LYS A O   1 
ATOM   110  C  CB  . LYS A 1 16  ? 24.953 13.552  -12.372 1.00 14.92  ? 11  LYS A CB  1 
ATOM   111  C  CG  . LYS A 1 16  ? 24.992 15.011  -11.874 1.00 16.58  ? 11  LYS A CG  1 
ATOM   112  C  CD  . LYS A 1 16  ? 24.850 16.005  -12.980 1.00 18.61  ? 11  LYS A CD  1 
ATOM   113  C  CE  . LYS A 1 16  ? 25.150 17.407  -12.544 1.00 22.63  ? 11  LYS A CE  1 
ATOM   114  N  NZ  . LYS A 1 16  ? 25.139 18.351  -13.680 1.00 24.44  ? 11  LYS A NZ  1 
ATOM   115  N  N   . LEU A 1 17  ? 25.813 10.491  -12.539 1.00 12.81  ? 12  LEU A N   1 
ATOM   116  C  CA  . LEU A 1 17  ? 25.624 9.087   -12.938 1.00 14.29  ? 12  LEU A CA  1 
ATOM   117  C  C   . LEU A 1 17  ? 25.521 8.156   -11.721 1.00 14.98  ? 12  LEU A C   1 
ATOM   118  O  O   . LEU A 1 17  ? 24.675 7.270   -11.651 1.00 13.71  ? 12  LEU A O   1 
ATOM   119  C  CB  . LEU A 1 17  ? 26.772 8.623   -13.842 1.00 14.76  ? 12  LEU A CB  1 
ATOM   120  C  CG  . LEU A 1 17  ? 26.835 9.291   -15.256 1.00 15.86  ? 12  LEU A CG  1 
ATOM   121  C  CD1 . LEU A 1 17  ? 28.046 8.924   -16.016 1.00 16.95  ? 12  LEU A CD1 1 
ATOM   122  C  CD2 . LEU A 1 17  ? 25.597 8.922   -16.115 1.00 17.72  ? 12  LEU A CD2 1 
ATOM   123  N  N   . ALA A 1 18  ? 26.405 8.357   -10.752 1.00 14.14  ? 13  ALA A N   1 
ATOM   124  C  CA  . ALA A 1 18  ? 26.455 7.520   -9.571  1.00 14.09  ? 13  ALA A CA  1 
ATOM   125  C  C   . ALA A 1 18  ? 25.185 7.703   -8.749  1.00 14.69  ? 13  ALA A C   1 
ATOM   126  O  O   . ALA A 1 18  ? 24.654 6.712   -8.208  1.00 15.27  ? 13  ALA A O   1 
ATOM   127  C  CB  . ALA A 1 18  ? 27.685 7.865   -8.770  1.00 15.35  ? 13  ALA A CB  1 
ATOM   128  N  N   . GLU A 1 19  ? 24.656 8.930   -8.706  1.00 15.46  ? 14  GLU A N   1 
ATOM   129  C  CA  . GLU A 1 19  ? 23.380 9.179   -8.059  1.00 15.75  ? 14  GLU A CA  1 
ATOM   130  C  C   . GLU A 1 19  ? 22.286 8.338   -8.718  1.00 16.92  ? 14  GLU A C   1 
ATOM   131  O  O   . GLU A 1 19  ? 21.521 7.639   -8.026  1.00 18.58  ? 14  GLU A O   1 
ATOM   132  C  CB  . GLU A 1 19  ? 23.015 10.663  -8.030  1.00 17.49  ? 14  GLU A CB  1 
ATOM   133  C  CG  . GLU A 1 19  ? 21.772 10.926  -7.196  1.00 20.36  ? 14  GLU A CG  1 
ATOM   134  C  CD  . GLU A 1 19  ? 21.295 12.366  -7.208  1.00 24.08  ? 14  GLU A CD  1 
ATOM   135  O  OE1 . GLU A 1 19  ? 21.719 13.149  -8.092  1.00 28.41  ? 14  GLU A OE1 1 
ATOM   136  O  OE2 . GLU A 1 19  ? 20.473 12.695  -6.324  1.00 30.70  ? 14  GLU A OE2 1 
ATOM   137  N  N   . GLN A 1 20  ? 22.226 8.367   -10.042 1.00 18.78  ? 15  GLN A N   1 
ATOM   138  C  CA  . GLN A 1 20  ? 21.248 7.555   -10.763 1.00 18.76  ? 15  GLN A CA  1 
ATOM   139  C  C   . GLN A 1 20  ? 21.378 6.054   -10.518 1.00 19.72  ? 15  GLN A C   1 
ATOM   140  O  O   . GLN A 1 20  ? 20.375 5.333   -10.469 1.00 21.26  ? 15  GLN A O   1 
ATOM   141  C  CB  . GLN A 1 20  ? 21.317 7.827   -12.273 1.00 21.02  ? 15  GLN A CB  1 
ATOM   142  C  CG  . GLN A 1 20  ? 20.925 9.256   -12.635 1.00 24.48  ? 15  GLN A CG  1 
ATOM   143  C  CD  . GLN A 1 20  ? 21.080 9.517   -14.127 1.00 30.41  ? 15  GLN A CD  1 
ATOM   144  O  OE1 . GLN A 1 20  ? 20.237 9.122   -14.936 1.00 28.57  ? 15  GLN A OE1 1 
ATOM   145  N  NE2 . GLN A 1 20  ? 22.197 10.152  -14.515 1.00 31.82  ? 15  GLN A NE2 1 
ATOM   146  N  N   . ALA A 1 21  ? 22.610 5.571   -10.376 1.00 16.38  ? 16  ALA A N   1 
ATOM   147  C  CA  . ALA A 1 21  ? 22.907 4.176   -10.141 1.00 16.87  ? 16  ALA A CA  1 
ATOM   148  C  C   . ALA A 1 21  ? 22.824 3.776   -8.659  1.00 17.67  ? 16  ALA A C   1 
ATOM   149  O  O   . ALA A 1 21  ? 23.109 2.625   -8.313  1.00 17.47  ? 16  ALA A O   1 
ATOM   150  C  CB  . ALA A 1 21  ? 24.282 3.900   -10.716 1.00 17.74  ? 16  ALA A CB  1 
ATOM   151  N  N   . GLU A 1 22  ? 22.496 4.748   -7.794  1.00 17.91  ? 17  GLU A N   1 
ATOM   152  C  CA  . GLU A 1 22  ? 22.437 4.545   -6.345  1.00 19.57  ? 17  GLU A CA  1 
ATOM   153  C  C   . GLU A 1 22  ? 23.772 4.057   -5.782  1.00 18.58  ? 17  GLU A C   1 
ATOM   154  O  O   . GLU A 1 22  ? 23.830 3.254   -4.851  1.00 20.01  ? 17  GLU A O   1 
ATOM   155  C  CB  . GLU A 1 22  ? 21.274 3.583   -5.974  1.00 21.42  ? 17  GLU A CB  1 
ATOM   156  C  CG  . GLU A 1 22  ? 19.915 4.255   -6.093  1.00 27.35  ? 17  GLU A CG  1 
ATOM   157  C  CD  . GLU A 1 22  ? 18.727 3.317   -5.970  1.00 33.73  ? 17  GLU A CD  1 
ATOM   158  O  OE1 . GLU A 1 22  ? 18.756 2.421   -5.105  1.00 35.40  ? 17  GLU A OE1 1 
ATOM   159  O  OE2 . GLU A 1 22  ? 17.778 3.473   -6.767  1.00 42.28  ? 17  GLU A OE2 1 
ATOM   160  N  N   . ARG A 1 23  ? 24.867 4.585   -6.346  1.00 15.75  ? 18  ARG A N   1 
ATOM   161  C  CA  . ARG A 1 23  ? 26.219 4.271   -5.946  1.00 14.46  ? 18  ARG A CA  1 
ATOM   162  C  C   . ARG A 1 23  ? 26.794 5.410   -5.119  1.00 14.77  ? 18  ARG A C   1 
ATOM   163  O  O   . ARG A 1 23  ? 27.569 6.215   -5.645  1.00 13.40  ? 18  ARG A O   1 
ATOM   164  C  CB  . ARG A 1 23  ? 27.085 4.023   -7.198  1.00 16.33  ? 18  ARG A CB  1 
ATOM   165  C  CG  . ARG A 1 23  ? 26.682 2.766   -7.899  1.00 16.45  ? 18  ARG A CG  1 
ATOM   166  C  CD  . ARG A 1 23  ? 27.372 1.547   -7.350  1.00 17.56  ? 18  ARG A CD  1 
ATOM   167  N  NE  . ARG A 1 23  ? 28.795 1.640   -7.678  1.00 18.44  ? 18  ARG A NE  1 
ATOM   168  C  CZ  . ARG A 1 23  ? 29.682 0.666   -7.543  1.00 20.97  ? 18  ARG A CZ  1 
ATOM   169  N  NH1 . ARG A 1 23  ? 29.318 -0.556  -7.201  1.00 21.03  ? 18  ARG A NH1 1 
ATOM   170  N  NH2 . ARG A 1 23  ? 30.963 0.917   -7.792  1.00 20.45  ? 18  ARG A NH2 1 
ATOM   171  N  N   . TYR A 1 24  ? 26.331 5.528   -3.862  1.00 14.11  ? 19  TYR A N   1 
ATOM   172  C  CA  . TYR A 1 24  ? 26.605 6.768   -3.140  1.00 14.98  ? 19  TYR A CA  1 
ATOM   173  C  C   . TYR A 1 24  ? 28.033 6.895   -2.631  1.00 14.03  ? 19  TYR A C   1 
ATOM   174  O  O   . TYR A 1 24  ? 28.518 7.998   -2.465  1.00 13.37  ? 19  TYR A O   1 
ATOM   175  C  CB  . TYR A 1 24  ? 25.591 6.953   -2.000  1.00 16.44  ? 19  TYR A CB  1 
ATOM   176  C  CG  . TYR A 1 24  ? 24.176 7.042   -2.527  1.00 17.79  ? 19  TYR A CG  1 
ATOM   177  C  CD1 . TYR A 1 24  ? 23.743 8.165   -3.240  1.00 19.84  ? 19  TYR A CD1 1 
ATOM   178  C  CD2 . TYR A 1 24  ? 23.286 5.980   -2.376  1.00 20.58  ? 19  TYR A CD2 1 
ATOM   179  C  CE1 . TYR A 1 24  ? 22.448 8.247   -3.735  1.00 22.32  ? 19  TYR A CE1 1 
ATOM   180  C  CE2 . TYR A 1 24  ? 21.984 6.054   -2.895  1.00 23.26  ? 19  TYR A CE2 1 
ATOM   181  C  CZ  . TYR A 1 24  ? 21.577 7.189   -3.551  1.00 21.72  ? 19  TYR A CZ  1 
ATOM   182  O  OH  . TYR A 1 24  ? 20.313 7.301   -4.057  1.00 27.98  ? 19  TYR A OH  1 
ATOM   183  N  N   . GLU A 1 25  ? 28.719 5.784   -2.343  1.00 14.46  ? 20  GLU A N   1 
ATOM   184  C  CA  . GLU A 1 25  ? 30.129 5.860   -2.007  1.00 15.12  ? 20  GLU A CA  1 
ATOM   185  C  C   . GLU A 1 25  ? 30.924 6.440   -3.185  1.00 13.18  ? 20  GLU A C   1 
ATOM   186  O  O   . GLU A 1 25  ? 31.763 7.331   -3.010  1.00 12.54  ? 20  GLU A O   1 
ATOM   187  C  CB  . GLU A 1 25  ? 30.609 4.494   -1.608  1.00 19.29  ? 20  GLU A CB  1 
ATOM   188  C  CG  . GLU A 1 25  ? 31.983 4.442   -1.079  1.00 27.75  ? 20  GLU A CG  1 
ATOM   189  C  CD  . GLU A 1 25  ? 32.292 3.045   -0.555  1.00 37.14  ? 20  GLU A CD  1 
ATOM   190  O  OE1 . GLU A 1 25  ? 31.430 2.492   0.176   1.00 40.62  ? 20  GLU A OE1 1 
ATOM   191  O  OE2 . GLU A 1 25  ? 33.340 2.483   -0.946  1.00 42.09  ? 20  GLU A OE2 1 
ATOM   192  N  N   . ASP A 1 26  ? 30.637 5.967   -4.404  1.00 12.47  ? 21  ASP A N   1 
ATOM   193  C  CA  . ASP A 1 26  ? 31.294 6.536   -5.580  1.00 12.88  ? 21  ASP A CA  1 
ATOM   194  C  C   . ASP A 1 26  ? 30.953 8.022   -5.717  1.00 12.43  ? 21  ASP A C   1 
ATOM   195  O  O   . ASP A 1 26  ? 31.814 8.842   -6.037  1.00 12.74  ? 21  ASP A O   1 
ATOM   196  C  CB  . ASP A 1 26  ? 30.884 5.829   -6.848  1.00 13.85  ? 21  ASP A CB  1 
ATOM   197  C  CG  . ASP A 1 26  ? 31.394 4.406   -7.035  1.00 16.31  ? 21  ASP A CG  1 
ATOM   198  O  OD1 . ASP A 1 26  ? 32.277 3.986   -6.267  1.00 17.49  ? 21  ASP A OD1 1 
ATOM   199  O  OD2 . ASP A 1 26  ? 30.835 3.704   -7.916  1.00 19.39  ? 21  ASP A OD2 1 
ATOM   200  N  N   . MET A 1 27  ? 29.666 8.343   -5.526  1.00 12.85  ? 22  MET A N   1 
ATOM   201  C  CA  . MET A 1 27  ? 29.195 9.711   -5.705  1.00 12.92  ? 22  MET A CA  1 
ATOM   202  C  C   . MET A 1 27  ? 29.984 10.623  -4.756  1.00 12.64  ? 22  MET A C   1 
ATOM   203  O  O   . MET A 1 27  ? 30.399 11.713  -5.150  1.00 12.03  ? 22  MET A O   1 
ATOM   204  C  CB  . MET A 1 27  ? 27.704 9.781   -5.392  1.00 13.16  ? 22  MET A CB  1 
ATOM   205  C  CG  . MET A 1 27  ? 27.047 11.065  -5.771  1.00 12.54  ? 22  MET A CG  1 
ATOM   206  S  SD  . MET A 1 27  ? 25.358 11.146  -5.203  1.00 14.34  ? 22  MET A SD  1 
ATOM   207  C  CE  . MET A 1 27  ? 24.887 12.779  -5.756  1.00 14.15  ? 22  MET A CE  1 
ATOM   208  N  N   . ALA A 1 28  ? 30.193 10.166  -3.505  1.00 12.54  ? 23  ALA A N   1 
ATOM   209  C  CA  . ALA A 1 28  ? 30.905 10.953  -2.513  1.00 13.75  ? 23  ALA A CA  1 
ATOM   210  C  C   . ALA A 1 28  ? 32.365 11.157  -2.911  1.00 13.50  ? 23  ALA A C   1 
ATOM   211  O  O   . ALA A 1 28  ? 32.915 12.265  -2.766  1.00 12.84  ? 23  ALA A O   1 
ATOM   212  C  CB  . ALA A 1 28  ? 30.777 10.314  -1.132  1.00 14.08  ? 23  ALA A CB  1 
ATOM   213  N  N   . ALA A 1 29  ? 32.998 10.082  -3.385  1.00 14.06  ? 24  ALA A N   1 
ATOM   214  C  CA  . ALA A 1 29  ? 34.375 10.170  -3.832  1.00 14.09  ? 24  ALA A CA  1 
ATOM   215  C  C   . ALA A 1 29  ? 34.556 11.131  -5.010  1.00 12.83  ? 24  ALA A C   1 
ATOM   216  O  O   . ALA A 1 29  ? 35.521 11.915  -5.037  1.00 12.71  ? 24  ALA A O   1 
ATOM   217  C  CB  . ALA A 1 29  ? 34.947 8.803   -4.148  1.00 15.51  ? 24  ALA A CB  1 
ATOM   218  N  N   . PHE A 1 30  ? 33.622 11.097  -5.965  1.00 12.46  ? 25  PHE A N   1 
ATOM   219  C  CA  . PHE A 1 30  ? 33.652 12.020  -7.090  1.00 13.23  ? 25  PHE A CA  1 
ATOM   220  C  C   . PHE A 1 30  ? 33.510 13.475  -6.593  1.00 12.50  ? 25  PHE A C   1 
ATOM   221  O  O   . PHE A 1 30  ? 34.235 14.372  -7.040  1.00 13.16  ? 25  PHE A O   1 
ATOM   222  C  CB  . PHE A 1 30  ? 32.568 11.670  -8.133  1.00 12.82  ? 25  PHE A CB  1 
ATOM   223  C  CG  . PHE A 1 30  ? 32.743 10.354  -8.863  1.00 12.23  ? 25  PHE A CG  1 
ATOM   224  C  CD1 . PHE A 1 30  ? 33.983 9.976   -9.346  1.00 15.24  ? 25  PHE A CD1 1 
ATOM   225  C  CD2 . PHE A 1 30  ? 31.658 9.527   -9.130  1.00 12.80  ? 25  PHE A CD2 1 
ATOM   226  C  CE1 . PHE A 1 30  ? 34.159 8.786   -10.047 1.00 14.09  ? 25  PHE A CE1 1 
ATOM   227  C  CE2 . PHE A 1 30  ? 31.837 8.334   -9.866  1.00 14.20  ? 25  PHE A CE2 1 
ATOM   228  C  CZ  . PHE A 1 30  ? 33.100 7.972   -10.295 1.00 15.13  ? 25  PHE A CZ  1 
ATOM   229  N  N   . MET A 1 31  ? 32.550 13.720  -5.691  1.00 12.22  ? 26  MET A N   1 
ATOM   230  C  CA  . MET A 1 31  ? 32.339 15.075  -5.184  1.00 11.81  ? 26  MET A CA  1 
ATOM   231  C  C   . MET A 1 31  ? 33.474 15.581  -4.290  1.00 12.50  ? 26  MET A C   1 
ATOM   232  O  O   . MET A 1 31  ? 33.828 16.768  -4.371  1.00 13.51  ? 26  MET A O   1 
ATOM   233  C  CB  . MET A 1 31  ? 30.987 15.210  -4.508  1.00 12.83  ? 26  MET A CB  1 
ATOM   234  C  CG  . MET A 1 31  ? 29.788 15.085  -5.443  1.00 13.53  ? 26  MET A CG  1 
ATOM   235  S  SD  . MET A 1 31  ? 29.938 16.204  -6.850  1.00 15.59  ? 26  MET A SD  1 
ATOM   236  C  CE  . MET A 1 31  ? 30.061 17.802  -6.078  1.00 13.99  ? 26  MET A CE  1 
ATOM   237  N  N   . LYS A 1 32  ? 34.105 14.701  -3.494  1.00 12.48  ? 27  LYS A N   1 
ATOM   238  C  CA  . LYS A 1 32  ? 35.319 15.056  -2.796  1.00 13.11  ? 27  LYS A CA  1 
ATOM   239  C  C   . LYS A 1 32  ? 36.376 15.526  -3.798  1.00 12.66  ? 27  LYS A C   1 
ATOM   240  O  O   . LYS A 1 32  ? 37.068 16.533  -3.584  1.00 12.80  ? 27  LYS A O   1 
ATOM   241  C  CB  . LYS A 1 32  ? 35.808 13.885  -1.935  1.00 14.56  ? 27  LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 32  ? 37.093 14.149  -1.121  1.00 16.31  ? 27  LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 32  ? 37.440 12.993  -0.237  1.00 19.07  ? 27  LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 32  ? 38.585 13.296  0.699   1.00 21.57  ? 27  LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 32  ? 39.897 13.304  0.018   1.00 23.48  ? 27  LYS A NZ  1 
ATOM   246  N  N   . GLY A 1 33  ? 36.573 14.730  -4.856  1.00 12.81  ? 28  GLY A N   1 
ATOM   247  C  CA  . GLY A 1 33  ? 37.496 15.072  -5.917  1.00 12.25  ? 28  GLY A CA  1 
ATOM   248  C  C   . GLY A 1 33  ? 37.200 16.440  -6.518  1.00 12.41  ? 28  GLY A C   1 
ATOM   249  O  O   . GLY A 1 33  ? 38.101 17.228  -6.741  1.00 12.62  ? 28  GLY A O   1 
ATOM   250  N  N   . ALA A 1 34  ? 35.922 16.735  -6.774  1.00 12.68  ? 29  ALA A N   1 
ATOM   251  C  CA  . ALA A 1 34  ? 35.519 18.022  -7.317  1.00 13.36  ? 29  ALA A CA  1 
ATOM   252  C  C   . ALA A 1 34  ? 35.847 19.157  -6.347  1.00 13.61  ? 29  ALA A C   1 
ATOM   253  O  O   . ALA A 1 34  ? 36.372 20.190  -6.768  1.00 15.74  ? 29  ALA A O   1 
ATOM   254  C  CB  . ALA A 1 34  ? 34.056 18.009  -7.667  1.00 13.69  ? 29  ALA A CB  1 
ATOM   255  N  N   . VAL A 1 35  ? 35.539 18.958  -5.071  1.00 14.04  ? 30  VAL A N   1 
ATOM   256  C  CA  . VAL A 1 35  ? 35.832 19.974  -4.067  1.00 14.10  ? 30  VAL A CA  1 
ATOM   257  C  C   . VAL A 1 35  ? 37.321 20.267  -4.036  1.00 14.97  ? 30  VAL A C   1 
ATOM   258  O  O   . VAL A 1 35  ? 37.728 21.440  -3.996  1.00 15.69  ? 30  VAL A O   1 
ATOM   259  C  CB  . VAL A 1 35  ? 35.326 19.552  -2.667  1.00 13.85  ? 30  VAL A CB  1 
ATOM   260  C  CG1 . VAL A 1 35  ? 35.944 20.434  -1.569  1.00 14.04  ? 30  VAL A CG1 1 
ATOM   261  C  CG2 . VAL A 1 35  ? 33.858 19.575  -2.648  1.00 15.38  ? 30  VAL A CG2 1 
ATOM   262  N  N   . GLU A 1 36  ? 38.129 19.206  -4.107  1.00 13.96  ? 31  GLU A N   1 
ATOM   263  C  CA  . GLU A 1 36  ? 39.576 19.350  -4.024  1.00 14.34  ? 31  GLU A CA  1 
ATOM   264  C  C   . GLU A 1 36  ? 40.203 20.044  -5.235  1.00 14.40  ? 31  GLU A C   1 
ATOM   265  O  O   . GLU A 1 36  ? 41.379 20.425  -5.182  1.00 15.15  ? 31  GLU A O   1 
ATOM   266  C  CB  . GLU A 1 36  ? 40.223 17.999  -3.740  1.00 15.00  ? 31  GLU A CB  1 
ATOM   267  C  CG  . GLU A 1 36  ? 39.875 17.551  -2.321  1.00 16.78  ? 31  GLU A CG  1 
ATOM   268  C  CD  . GLU A 1 36  ? 40.385 16.199  -1.876  1.00 20.36  ? 31  GLU A CD  1 
ATOM   269  O  OE1 . GLU A 1 36  ? 40.827 15.421  -2.737  1.00 23.68  ? 31  GLU A OE1 1 
ATOM   270  O  OE2 . GLU A 1 36  ? 40.267 15.901  -0.663  1.00 23.62  ? 31  GLU A OE2 1 
ATOM   271  N  N   . LYS A 1 37  ? 39.433 20.296  -6.292  1.00 13.84  ? 32  LYS A N   1 
ATOM   272  C  CA  . LYS A 1 37  ? 39.917 21.129  -7.386  1.00 14.59  ? 32  LYS A CA  1 
ATOM   273  C  C   . LYS A 1 37  ? 40.127 22.581  -6.952  1.00 16.09  ? 32  LYS A C   1 
ATOM   274  O  O   . LYS A 1 37  ? 40.834 23.325  -7.624  1.00 16.20  ? 32  LYS A O   1 
ATOM   275  C  CB  . LYS A 1 37  ? 39.008 21.097  -8.565  1.00 15.46  ? 32  LYS A CB  1 
ATOM   276  C  CG  . LYS A 1 37  ? 38.824 19.706  -9.226  1.00 14.95  ? 32  LYS A CG  1 
ATOM   277  C  CD  . LYS A 1 37  ? 40.098 19.073  -9.689  1.00 15.04  ? 32  LYS A CD  1 
ATOM   278  C  CE  . LYS A 1 37  ? 39.839 17.675  -10.252 1.00 16.41  ? 32  LYS A CE  1 
ATOM   279  N  NZ  . LYS A 1 37  ? 41.155 16.990  -10.587 1.00 16.77  ? 32  LYS A NZ  1 
ATOM   280  N  N   . GLY A 1 38  ? 39.455 22.979  -5.853  1.00 16.22  ? 33  GLY A N   1 
ATOM   281  C  CA  . GLY A 1 38  ? 39.733 24.254  -5.204  1.00 17.49  ? 33  GLY A CA  1 
ATOM   282  C  C   . GLY A 1 38  ? 38.810 25.384  -5.657  1.00 18.71  ? 33  GLY A C   1 
ATOM   283  O  O   . GLY A 1 38  ? 38.920 26.525  -5.179  1.00 21.26  ? 33  GLY A O   1 
ATOM   284  N  N   . GLU A 1 39  ? 37.922 25.108  -6.614  1.00 17.29  ? 34  GLU A N   1 
ATOM   285  C  CA  . GLU A 1 39  ? 36.961 26.092  -7.064  1.00 19.43  ? 34  GLU A CA  1 
ATOM   286  C  C   . GLU A 1 39  ? 35.747 26.037  -6.136  1.00 21.11  ? 34  GLU A C   1 
ATOM   287  O  O   . GLU A 1 39  ? 35.424 25.003  -5.565  1.00 21.83  ? 34  GLU A O   1 
ATOM   288  C  CB  . GLU A 1 39  ? 36.540 25.881  -8.504  1.00 23.00  ? 34  GLU A CB  1 
ATOM   289  C  CG  . GLU A 1 39  ? 37.720 25.827  -9.469  1.00 24.64  ? 34  GLU A CG  1 
ATOM   290  C  CD  . GLU A 1 39  ? 38.265 27.160  -9.938  1.00 37.95  ? 34  GLU A CD  1 
ATOM   291  O  OE1 . GLU A 1 39  ? 38.001 28.211  -9.304  1.00 37.61  ? 34  GLU A OE1 1 
ATOM   292  O  OE2 . GLU A 1 39  ? 38.916 27.152  -11.007 1.00 49.44  ? 34  GLU A OE2 1 
ATOM   293  N  N   . GLU A 1 40  ? 35.068 27.170  -5.987  1.00 23.62  ? 35  GLU A N   1 
ATOM   294  C  CA  . GLU A 1 40  ? 33.823 27.196  -5.232  1.00 22.02  ? 35  GLU A CA  1 
ATOM   295  C  C   . GLU A 1 40  ? 32.776 26.343  -5.956  1.00 22.61  ? 35  GLU A C   1 
ATOM   296  O  O   . GLU A 1 40  ? 32.873 26.073  -7.154  1.00 22.68  ? 35  GLU A O   1 
ATOM   297  C  CB  . GLU A 1 40  ? 33.362 28.681  -5.014  1.00 24.36  ? 35  GLU A CB  1 
ATOM   298  C  CG  . GLU A 1 40  ? 34.310 29.500  -4.098  1.00 25.37  ? 35  GLU A CG  1 
ATOM   299  C  CD  . GLU A 1 40  ? 33.847 30.940  -3.784  1.00 29.00  ? 35  GLU A CD  1 
ATOM   300  O  OE1 . GLU A 1 40  ? 32.622 31.139  -3.644  1.00 37.55  ? 35  GLU A OE1 1 
ATOM   301  O  OE2 . GLU A 1 40  ? 34.683 31.850  -3.612  1.00 22.62  ? 35  GLU A OE2 1 
ATOM   302  N  N   . LEU A 1 41  ? 31.800 25.846  -5.202  1.00 18.04  ? 36  LEU A N   1 
ATOM   303  C  CA  . LEU A 1 41  ? 30.759 25.002  -5.764  1.00 17.18  ? 36  LEU A CA  1 
ATOM   304  C  C   . LEU A 1 41  ? 29.506 25.817  -6.044  1.00 18.66  ? 36  LEU A C   1 
ATOM   305  O  O   . LEU A 1 41  ? 29.096 26.656  -5.238  1.00 18.71  ? 36  LEU A O   1 
ATOM   306  C  CB  . LEU A 1 41  ? 30.313 23.864  -4.812  1.00 18.74  ? 36  LEU A CB  1 
ATOM   307  C  CG  . LEU A 1 41  ? 31.359 22.876  -4.272  1.00 24.58  ? 36  LEU A CG  1 
ATOM   308  C  CD1 . LEU A 1 41  ? 30.681 21.638  -3.716  1.00 21.39  ? 36  LEU A CD1 1 
ATOM   309  C  CD2 . LEU A 1 41  ? 32.338 22.545  -5.223  1.00 25.27  ? 36  LEU A CD2 1 
ATOM   310  N  N   . SER A 1 42  ? 28.834 25.473  -7.127  1.00 16.63  ? 37  SER A N   1 
ATOM   311  C  CA  . SER A 1 42  ? 27.516 26.010  -7.404  1.00 16.96  ? 37  SER A CA  1 
ATOM   312  C  C   . SER A 1 42  ? 26.458 25.452  -6.447  1.00 17.24  ? 37  SER A C   1 
ATOM   313  O  O   . SER A 1 42  ? 26.629 24.400  -5.807  1.00 14.86  ? 37  SER A O   1 
ATOM   314  C  CB  . SER A 1 42  ? 27.132 25.698  -8.831  1.00 17.23  ? 37  SER A CB  1 
ATOM   315  O  OG  . SER A 1 42  ? 26.744 24.351  -8.948  1.00 17.35  ? 37  SER A OG  1 
ATOM   316  N  N   . CYS A 1 43  ? 25.165 25.917  -6.534  1.00 15.49  ? 38  CYS A N   1 
ATOM   317  C  CA  . CYS A 1 43  ? 24.035 25.364  -5.762  1.00 17.92  ? 38  CYS A CA  1 
ATOM   318  C  C   . CYS A 1 43  ? 23.767 23.886  -6.108  1.00 16.63  ? 38  CYS A C   1 
ATOM   319  O  O   . CYS A 1 43  ? 23.625 23.056  -5.159  1.00 17.37  ? 38  CYS A O   1 
ATOM   320  C  CB  . CYS A 1 43  ? 22.791 26.202  -6.019  1.00 19.57  ? 38  CYS A CB  1 
ATOM   321  S  SG  . CYS A 1 43  ? 21.285 25.557  -5.260  1.00 24.49  ? 38  CYS A SG  1 
ATOM   322  N  N   . GLU A 1 44  ? 23.807 23.636  -7.421  1.00 15.70  ? 39  GLU A N   1 
ATOM   323  C  CA  . GLU A 1 44  ? 23.559 22.238  -7.755  1.00 17.48  ? 39  GLU A CA  1 
ATOM   324  C  C   . GLU A 1 44  ? 24.695 21.327  -7.269  1.00 14.74  ? 39  GLU A C   1 
ATOM   325  O  O   . GLU A 1 44  ? 24.453 20.218  -6.792  1.00 15.59  ? 39  GLU A O   1 
ATOM   326  C  CB  . GLU A 1 44  ? 23.365 22.154  -9.273  1.00 21.48  ? 39  GLU A CB  1 
ATOM   327  C  CG  . GLU A 1 44  ? 23.017 20.772  -9.797  1.00 24.18  ? 39  GLU A CG  1 
ATOM   328  C  CD  . GLU A 1 44  ? 22.861 20.705  -11.315 1.00 32.73  ? 39  GLU A CD  1 
ATOM   329  O  OE1 . GLU A 1 44  ? 23.102 21.733  -11.998 1.00 31.94  ? 39  GLU A OE1 1 
ATOM   330  O  OE2 . GLU A 1 44  ? 22.555 19.596  -11.816 1.00 33.46  ? 39  GLU A OE2 1 
ATOM   331  N  N   . GLU A 1 45  ? 25.937 21.783  -7.380  1.00 15.10  ? 40  GLU A N   1 
ATOM   332  C  CA  . GLU A 1 45  ? 27.080 20.988  -6.954  1.00 15.44  ? 40  GLU A CA  1 
ATOM   333  C  C   . GLU A 1 45  ? 27.082 20.758  -5.432  1.00 15.46  ? 40  GLU A C   1 
ATOM   334  O  O   . GLU A 1 45  ? 27.404 19.671  -4.973  1.00 15.53  ? 40  GLU A O   1 
ATOM   335  C  CB  . GLU A 1 45  ? 28.337 21.667  -7.408  1.00 16.39  ? 40  GLU A CB  1 
ATOM   336  C  CG  . GLU A 1 45  ? 28.479 21.687  -8.932  1.00 16.85  ? 40  GLU A CG  1 
ATOM   337  C  CD  . GLU A 1 45  ? 29.507 22.651  -9.478  1.00 16.46  ? 40  GLU A CD  1 
ATOM   338  O  OE1 . GLU A 1 45  ? 30.078 23.434  -8.703  1.00 16.60  ? 40  GLU A OE1 1 
ATOM   339  O  OE2 . GLU A 1 45  ? 29.802 22.599  -10.705 1.00 19.69  ? 40  GLU A OE2 1 
ATOM   340  N  N   . ARG A 1 46  ? 26.688 21.768  -4.653  1.00 13.79  ? 41  ARG A N   1 
ATOM   341  C  CA  . ARG A 1 46  ? 26.543 21.620  -3.211  1.00 14.49  ? 41  ARG A CA  1 
ATOM   342  C  C   . ARG A 1 46  ? 25.497 20.571  -2.887  1.00 14.52  ? 41  ARG A C   1 
ATOM   343  O  O   . ARG A 1 46  ? 25.687 19.746  -1.975  1.00 14.61  ? 41  ARG A O   1 
ATOM   344  C  CB  . ARG A 1 46  ? 26.142 22.960  -2.536  1.00 15.79  ? 41  ARG A CB  1 
ATOM   345  C  CG  . ARG A 1 46  ? 27.257 23.945  -2.461  1.00 16.20  ? 41  ARG A CG  1 
ATOM   346  C  CD  . ARG A 1 46  ? 26.902 25.175  -1.648  1.00 16.96  ? 41  ARG A CD  1 
ATOM   347  N  NE  . ARG A 1 46  ? 25.750 25.900  -2.172  1.00 16.67  ? 41  ARG A NE  1 
ATOM   348  C  CZ  . ARG A 1 46  ? 25.788 27.005  -2.905  1.00 18.68  ? 41  ARG A CZ  1 
ATOM   349  N  NH1 . ARG A 1 46  ? 26.881 27.393  -3.532  1.00 20.25  ? 41  ARG A NH1 1 
ATOM   350  N  NH2 . ARG A 1 46  ? 24.676 27.724  -3.046  1.00 20.27  ? 41  ARG A NH2 1 
ATOM   351  N  N   . ASN A 1 47  ? 24.433 20.534  -3.679  1.00 14.35  ? 42  ASN A N   1 
ATOM   352  C  CA  . ASN A 1 47  ? 23.426 19.512  -3.515  1.00 15.94  ? 42  ASN A CA  1 
ATOM   353  C  C   . ASN A 1 47  ? 23.991 18.111  -3.773  1.00 15.67  ? 42  ASN A C   1 
ATOM   354  O  O   . ASN A 1 47  ? 23.708 17.199  -3.013  1.00 14.67  ? 42  ASN A O   1 
ATOM   355  C  CB  . ASN A 1 47  ? 22.218 19.749  -4.401  1.00 17.16  ? 42  ASN A CB  1 
ATOM   356  C  CG  . ASN A 1 47  ? 21.103 18.764  -4.096  1.00 23.69  ? 42  ASN A CG  1 
ATOM   357  O  OD1 . ASN A 1 47  ? 20.666 17.913  -4.947  1.00 30.29  ? 42  ASN A OD1 1 
ATOM   358  N  ND2 . ASN A 1 47  ? 20.658 18.795  -2.889  1.00 24.36  ? 42  ASN A ND2 1 
ATOM   359  N  N   . LEU A 1 48  ? 24.819 17.936  -4.818  1.00 13.54  ? 43  LEU A N   1 
ATOM   360  C  CA  . LEU A 1 48  ? 25.400 16.632  -5.077  1.00 14.02  ? 43  LEU A CA  1 
ATOM   361  C  C   . LEU A 1 48  ? 26.287 16.183  -3.908  1.00 14.01  ? 43  LEU A C   1 
ATOM   362  O  O   . LEU A 1 48  ? 26.230 15.030  -3.487  1.00 14.04  ? 43  LEU A O   1 
ATOM   363  C  CB  . LEU A 1 48  ? 26.202 16.634  -6.342  1.00 13.72  ? 43  LEU A CB  1 
ATOM   364  C  CG  . LEU A 1 48  ? 25.419 16.910  -7.621  1.00 14.63  ? 43  LEU A CG  1 
ATOM   365  C  CD1 . LEU A 1 48  ? 26.350 17.153  -8.777  1.00 16.35  ? 43  LEU A CD1 1 
ATOM   366  C  CD2 . LEU A 1 48  ? 24.511 15.782  -7.952  1.00 16.02  ? 43  LEU A CD2 1 
ATOM   367  N  N   . LEU A 1 49  ? 27.074 17.102  -3.368  1.00 12.80  ? 44  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 49  ? 27.957 16.833  -2.242  1.00 13.61  ? 44  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 49  ? 27.146 16.386  -1.031  1.00 14.62  ? 44  LEU A C   1 
ATOM   370  O  O   . LEU A 1 49  ? 27.477 15.396  -0.396  1.00 13.21  ? 44  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 49  ? 28.772 18.081  -1.915  1.00 13.65  ? 44  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 49  ? 29.746 17.997  -0.734  1.00 13.58  ? 44  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 49  ? 30.948 17.132  -1.055  1.00 13.74  ? 44  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 49  ? 30.161 19.419  -0.227  1.00 14.91  ? 44  LEU A CD2 1 
ATOM   375  N  N   . SER A 1 50  ? 26.108 17.166  -0.720  1.00 12.59  ? 45  SER A N   1 
ATOM   376  C  CA  . SER A 1 50  ? 25.221 16.874  0.382   1.00 13.26  ? 45  SER A CA  1 
ATOM   377  C  C   . SER A 1 50  ? 24.509 15.527  0.271   1.00 13.70  ? 45  SER A C   1 
ATOM   378  O  O   . SER A 1 50  ? 24.577 14.687  1.182   1.00 13.94  ? 45  SER A O   1 
ATOM   379  C  CB  . SER A 1 50  ? 24.198 17.995  0.516   1.00 14.77  ? 45  SER A CB  1 
ATOM   380  O  OG  . SER A 1 50  ? 23.328 17.725  1.622   1.00 15.96  ? 45  SER A OG  1 
ATOM   381  N  N   . VAL A 1 51  ? 23.917 15.252  -0.897  1.00 13.81  ? 46  VAL A N   1 
ATOM   382  C  CA  . VAL A 1 51  ? 23.233 13.982  -1.112  1.00 14.16  ? 46  VAL A CA  1 
ATOM   383  C  C   . VAL A 1 51  ? 24.159 12.777  -0.939  1.00 14.51  ? 46  VAL A C   1 
ATOM   384  O  O   . VAL A 1 51  ? 23.794 11.780  -0.321  1.00 13.77  ? 46  VAL A O   1 
ATOM   385  C  CB  . VAL A 1 51  ? 22.580 13.971  -2.503  1.00 16.40  ? 46  VAL A CB  1 
ATOM   386  C  CG1 . VAL A 1 51  ? 22.099 12.547  -2.927  1.00 16.83  ? 46  VAL A CG1 1 
ATOM   387  C  CG2 . VAL A 1 51  ? 21.408 14.964  -2.523  1.00 18.20  ? 46  VAL A CG2 1 
ATOM   388  N  N   . ALA A 1 52  ? 25.362 12.880  -1.509  1.00 13.10  ? 47  ALA A N   1 
ATOM   389  C  CA  . ALA A 1 52  ? 26.293 11.772  -1.509  1.00 13.41  ? 47  ALA A CA  1 
ATOM   390  C  C   . ALA A 1 52  ? 26.657 11.421  -0.073  1.00 12.65  ? 47  ALA A C   1 
ATOM   391  O  O   . ALA A 1 52  ? 26.539 10.249  0.351   1.00 12.60  ? 47  ALA A O   1 
ATOM   392  C  CB  . ALA A 1 52  ? 27.508 12.140  -2.339  1.00 13.93  ? 47  ALA A CB  1 
ATOM   393  N  N   . TYR A 1 53  ? 27.155 12.412  0.674   1.00 11.21  ? 48  TYR A N   1 
ATOM   394  C  CA  . TYR A 1 53  ? 27.632 12.094  2.013   1.00 12.10  ? 48  TYR A CA  1 
ATOM   395  C  C   . TYR A 1 53  ? 26.493 11.765  2.983   1.00 12.41  ? 48  TYR A C   1 
ATOM   396  O  O   . TYR A 1 53  ? 26.669 10.938  3.878   1.00 12.78  ? 48  TYR A O   1 
ATOM   397  C  CB  . TYR A 1 53  ? 28.544 13.226  2.542   1.00 12.08  ? 48  TYR A CB  1 
ATOM   398  C  CG  . TYR A 1 53  ? 29.938 13.083  2.004   1.00 12.64  ? 48  TYR A CG  1 
ATOM   399  C  CD1 . TYR A 1 53  ? 30.788 12.091  2.483   1.00 12.63  ? 48  TYR A CD1 1 
ATOM   400  C  CD2 . TYR A 1 53  ? 30.428 13.940  1.037   1.00 13.82  ? 48  TYR A CD2 1 
ATOM   401  C  CE1 . TYR A 1 53  ? 32.069 11.965  2.019   1.00 12.52  ? 48  TYR A CE1 1 
ATOM   402  C  CE2 . TYR A 1 53  ? 31.736 13.816  0.561   1.00 14.00  ? 48  TYR A CE2 1 
ATOM   403  C  CZ  . TYR A 1 53  ? 32.549 12.827  1.051   1.00 14.59  ? 48  TYR A CZ  1 
ATOM   404  O  OH  . TYR A 1 53  ? 33.860 12.654  0.602   1.00 16.22  ? 48  TYR A OH  1 
ATOM   405  N  N   . LYS A 1 54  ? 25.318 12.382  2.793   1.00 14.10  ? 49  LYS A N   1 
ATOM   406  C  CA  . LYS A 1 54  ? 24.198 12.079  3.657   1.00 14.82  ? 49  LYS A CA  1 
ATOM   407  C  C   . LYS A 1 54  ? 23.826 10.612  3.501   1.00 14.01  ? 49  LYS A C   1 
ATOM   408  O  O   . LYS A 1 54  ? 23.484 9.959   4.468   1.00 14.17  ? 49  LYS A O   1 
ATOM   409  C  CB  . LYS A 1 54  ? 22.978 12.955  3.414   1.00 17.79  ? 49  LYS A CB  1 
ATOM   410  C  CG  . LYS A 1 54  ? 21.900 12.825  4.452   1.00 25.67  ? 49  LYS A CG  1 
ATOM   411  C  CD  . LYS A 1 54  ? 20.865 14.080  4.473   1.00 32.65  ? 49  LYS A CD  1 
ATOM   412  C  CE  . LYS A 1 54  ? 19.642 13.830  5.313   1.00 35.17  ? 49  LYS A CE  1 
ATOM   413  N  NZ  . LYS A 1 54  ? 19.924 12.955  6.499   1.00 35.83  ? 49  LYS A NZ  1 
ATOM   414  N  N   . ASN A 1 55  ? 23.824 10.099  2.261   1.00 13.24  ? 50  ASN A N   1 
ATOM   415  C  CA  . ASN A 1 55  ? 23.495 8.717   2.024   1.00 14.57  ? 50  ASN A CA  1 
ATOM   416  C  C   . ASN A 1 55  ? 24.561 7.810   2.630   1.00 14.94  ? 50  ASN A C   1 
ATOM   417  O  O   . ASN A 1 55  ? 24.219 6.785   3.225   1.00 16.12  ? 50  ASN A O   1 
ATOM   418  C  CB  . ASN A 1 55  ? 23.340 8.479   0.551   1.00 16.38  ? 50  ASN A CB  1 
ATOM   419  C  CG  . ASN A 1 55  ? 22.010 8.789   0.019   1.00 22.60  ? 50  ASN A CG  1 
ATOM   420  O  OD1 . ASN A 1 55  ? 21.782 9.762   -0.718  1.00 24.96  ? 50  ASN A OD1 1 
ATOM   421  N  ND2 . ASN A 1 55  ? 21.126 7.901   0.265   1.00 24.85  ? 50  ASN A ND2 1 
ATOM   422  N  N   . VAL A 1 56  ? 25.846 8.136   2.468   1.00 13.21  ? 51  VAL A N   1 
ATOM   423  C  CA  . VAL A 1 56  ? 26.884 7.289   3.046   1.00 13.86  ? 51  VAL A CA  1 
ATOM   424  C  C   . VAL A 1 56  ? 26.735 7.224   4.574   1.00 14.48  ? 51  VAL A C   1 
ATOM   425  O  O   . VAL A 1 56  ? 26.632 6.143   5.158   1.00 13.91  ? 51  VAL A O   1 
ATOM   426  C  CB  . VAL A 1 56  ? 28.245 7.753   2.603   1.00 13.53  ? 51  VAL A CB  1 
ATOM   427  C  CG1 . VAL A 1 56  ? 29.368 7.017   3.362   1.00 14.24  ? 51  VAL A CG1 1 
ATOM   428  C  CG2 . VAL A 1 56  ? 28.431 7.556   1.086   1.00 13.99  ? 51  VAL A CG2 1 
ATOM   429  N  N   . VAL A 1 57  ? 26.693 8.389   5.216   1.00 13.34  ? 52  VAL A N   1 
ATOM   430  C  CA  . VAL A 1 57  ? 26.674 8.443   6.669   1.00 14.01  ? 52  VAL A CA  1 
ATOM   431  C  C   . VAL A 1 57  ? 25.350 7.899   7.178   1.00 15.10  ? 52  VAL A C   1 
ATOM   432  O  O   . VAL A 1 57  ? 25.286 7.309   8.263   1.00 15.23  ? 52  VAL A O   1 
ATOM   433  C  CB  . VAL A 1 57  ? 27.030 9.849   7.211   1.00 14.96  ? 52  VAL A CB  1 
ATOM   434  C  CG1 . VAL A 1 57  ? 25.840 10.816  7.142   1.00 16.01  ? 52  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A 1 57  ? 27.552 9.779   8.649   1.00 17.90  ? 52  VAL A CG2 1 
ATOM   436  N  N   . GLY A 1 58  ? 24.292 8.040   6.377   1.00 14.91  ? 53  GLY A N   1 
ATOM   437  C  CA  . GLY A 1 58  ? 22.985 7.552   6.776   1.00 15.86  ? 53  GLY A CA  1 
ATOM   438  C  C   . GLY A 1 58  ? 22.941 6.036   6.920   1.00 18.25  ? 53  GLY A C   1 
ATOM   439  O  O   . GLY A 1 58  ? 22.383 5.496   7.896   1.00 17.60  ? 53  GLY A O   1 
ATOM   440  N  N   . GLY A 1 59  ? 23.599 5.355   5.981   1.00 17.85  ? 54  GLY A N   1 
ATOM   441  C  CA  . GLY A 1 59  ? 23.816 3.918   6.089   1.00 18.07  ? 54  GLY A CA  1 
ATOM   442  C  C   . GLY A 1 59  ? 24.615 3.511   7.329   1.00 15.80  ? 54  GLY A C   1 
ATOM   443  O  O   . GLY A 1 59  ? 24.278 2.517   7.991   1.00 17.14  ? 54  GLY A O   1 
ATOM   444  N  N   . GLN A 1 60  ? 25.670 4.271   7.621   1.00 15.36  ? 55  GLN A N   1 
ATOM   445  C  CA  . GLN A 1 60  ? 26.516 3.997   8.768   1.00 15.50  ? 55  GLN A CA  1 
ATOM   446  C  C   . GLN A 1 60  ? 25.735 4.193   10.074  1.00 14.57  ? 55  GLN A C   1 
ATOM   447  O  O   . GLN A 1 60  ? 25.914 3.423   11.035  1.00 13.90  ? 55  GLN A O   1 
ATOM   448  C  CB  . GLN A 1 60  ? 27.744 4.900   8.713   1.00 15.10  ? 55  GLN A CB  1 
ATOM   449  C  CG  . GLN A 1 60  ? 28.661 4.533   7.516   1.00 18.18  ? 55  GLN A CG  1 
ATOM   450  C  CD  . GLN A 1 60  ? 29.827 5.449   7.413   1.00 17.62  ? 55  GLN A CD  1 
ATOM   451  O  OE1 . GLN A 1 60  ? 30.941 5.017   7.096   1.00 23.87  ? 55  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A 1 60  ? 29.606 6.698   7.633   1.00 16.27  ? 55  GLN A NE2 1 
ATOM   453  N  N   . ARG A 1 61  ? 24.927 5.262   10.121  1.00 14.26  ? 56  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 61  ? 24.194 5.601   11.325  1.00 13.45  ? 56  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 61  ? 23.164 4.505   11.596  1.00 13.79  ? 56  ARG A C   1 
ATOM   456  O  O   . ARG A 1 61  ? 22.981 4.103   12.725  1.00 14.85  ? 56  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 61  ? 23.461 6.951   11.238  1.00 14.32  ? 56  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 61  ? 24.423 8.164   11.215  1.00 14.66  ? 56  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 61  ? 23.795 9.416   10.700  1.00 15.39  ? 56  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 61  ? 22.802 9.918   11.646  1.00 14.60  ? 56  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 61  ? 21.802 10.710  11.299  1.00 16.70  ? 56  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 61  ? 21.470 10.878  10.034  1.00 17.03  ? 56  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 61  ? 21.072 11.281  12.247  1.00 16.46  ? 56  ARG A NH2 1 
ATOM   464  N  N   . ALA A 1 62  ? 22.464 4.088   10.554  1.00 14.06  ? 57  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 62  ? 21.495 3.030   10.686  1.00 14.55  ? 57  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 62  ? 22.148 1.753   11.196  1.00 15.48  ? 57  ALA A C   1 
ATOM   467  O  O   . ALA A 1 62  ? 21.603 1.096   12.085  1.00 15.44  ? 57  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 62  ? 20.779 2.790   9.347   1.00 15.52  ? 57  ALA A CB  1 
ATOM   469  N  N   . ALA A 1 63  ? 23.314 1.410   10.640  1.00 14.53  ? 58  ALA A N   1 
ATOM   470  C  CA  . ALA A 1 63  ? 24.008 0.201   11.070  1.00 14.75  ? 58  ALA A CA  1 
ATOM   471  C  C   . ALA A 1 63  ? 24.480 0.306   12.517  1.00 14.43  ? 58  ALA A C   1 
ATOM   472  O  O   . ALA A 1 63  ? 24.360 -0.631  13.307  1.00 14.73  ? 58  ALA A O   1 
ATOM   473  C  CB  . ALA A 1 63  ? 25.219 -0.089  10.151  1.00 15.25  ? 58  ALA A CB  1 
ATOM   474  N  N   . TRP A 1 64  ? 25.102 1.442   12.856  1.00 14.52  ? 59  TRP A N   1 
ATOM   475  C  CA  . TRP A 1 64  ? 25.554 1.688   14.217  1.00 15.14  ? 59  TRP A CA  1 
ATOM   476  C  C   . TRP A 1 64  ? 24.434 1.535   15.243  1.00 15.67  ? 59  TRP A C   1 
ATOM   477  O  O   . TRP A 1 64  ? 24.623 0.956   16.321  1.00 15.95  ? 59  TRP A O   1 
ATOM   478  C  CB  . TRP A 1 64  ? 26.201 3.082   14.312  1.00 13.99  ? 59  TRP A CB  1 
ATOM   479  C  CG  . TRP A 1 64  ? 26.816 3.359   15.635  1.00 14.38  ? 59  TRP A CG  1 
ATOM   480  C  CD1 . TRP A 1 64  ? 28.112 3.164   15.975  1.00 15.65  ? 59  TRP A CD1 1 
ATOM   481  C  CD2 . TRP A 1 64  ? 26.170 3.879   16.807  1.00 15.00  ? 59  TRP A CD2 1 
ATOM   482  N  NE1 . TRP A 1 64  ? 28.327 3.551   17.269  1.00 16.31  ? 59  TRP A NE1 1 
ATOM   483  C  CE2 . TRP A 1 64  ? 27.158 4.008   17.803  1.00 15.65  ? 59  TRP A CE2 1 
ATOM   484  C  CE3 . TRP A 1 64  ? 24.874 4.287   17.091  1.00 15.51  ? 59  TRP A CE3 1 
ATOM   485  C  CZ2 . TRP A 1 64  ? 26.874 4.472   19.087  1.00 18.20  ? 59  TRP A CZ2 1 
ATOM   486  C  CZ3 . TRP A 1 64  ? 24.597 4.799   18.363  1.00 17.05  ? 59  TRP A CZ3 1 
ATOM   487  C  CH2 . TRP A 1 64  ? 25.585 4.879   19.335  1.00 16.53  ? 59  TRP A CH2 1 
ATOM   488  N  N   . ARG A 1 65  ? 23.244 2.041   14.891  1.00 16.48  ? 60  ARG A N   1 
ATOM   489  C  CA  . ARG A 1 65  ? 22.117 1.933   15.807  1.00 16.89  ? 60  ARG A CA  1 
ATOM   490  C  C   . ARG A 1 65  ? 21.695 0.493   16.044  1.00 17.33  ? 60  ARG A C   1 
ATOM   491  O  O   . ARG A 1 65  ? 21.402 0.131   17.192  1.00 16.41  ? 60  ARG A O   1 
ATOM   492  C  CB  . ARG A 1 65  ? 20.916 2.737   15.327  1.00 17.89  ? 60  ARG A CB  1 
ATOM   493  C  CG  . ARG A 1 65  ? 21.200 4.237   15.349  1.00 20.21  ? 60  ARG A CG  1 
ATOM   494  C  CD  . ARG A 1 65  ? 20.097 5.001   14.595  1.00 25.04  ? 60  ARG A CD  1 
ATOM   495  N  NE  . ARG A 1 65  ? 20.461 6.408   14.472  1.00 27.43  ? 60  ARG A NE  1 
ATOM   496  C  CZ  . ARG A 1 65  ? 19.799 7.308   13.745  1.00 30.41  ? 60  ARG A CZ  1 
ATOM   497  N  NH1 . ARG A 1 65  ? 18.863 6.949   12.884  1.00 31.96  ? 60  ARG A NH1 1 
ATOM   498  N  NH2 . ARG A 1 65  ? 20.085 8.597   13.897  1.00 29.69  ? 60  ARG A NH2 1 
ATOM   499  N  N   . VAL A 1 66  ? 21.640 -0.300  14.959  1.00 15.05  ? 61  VAL A N   1 
ATOM   500  C  CA  . VAL A 1 66  ? 21.327 -1.711  15.075  1.00 15.41  ? 61  VAL A CA  1 
ATOM   501  C  C   . VAL A 1 66  ? 22.305 -2.374  16.033  1.00 16.74  ? 61  VAL A C   1 
ATOM   502  O  O   . VAL A 1 66  ? 21.890 -3.084  16.973  1.00 16.76  ? 61  VAL A O   1 
ATOM   503  C  CB  . VAL A 1 66  ? 21.330 -2.415  13.712  1.00 16.62  ? 61  VAL A CB  1 
ATOM   504  C  CG1 . VAL A 1 66  ? 21.285 -3.950  13.884  1.00 17.07  ? 61  VAL A CG1 1 
ATOM   505  C  CG2 . VAL A 1 66  ? 20.153 -1.939  12.885  1.00 18.73  ? 61  VAL A CG2 1 
ATOM   506  N  N   . LEU A 1 67  ? 23.598 -2.162  15.777  1.00 15.70  ? 62  LEU A N   1 
ATOM   507  C  CA  . LEU A 1 67  ? 24.647 -2.780  16.577  1.00 16.04  ? 62  LEU A CA  1 
ATOM   508  C  C   . LEU A 1 67  ? 24.692 -2.308  18.032  1.00 18.21  ? 62  LEU A C   1 
ATOM   509  O  O   . LEU A 1 67  ? 24.831 -3.133  18.950  1.00 20.20  ? 62  LEU A O   1 
ATOM   510  C  CB  . LEU A 1 67  ? 26.039 -2.638  15.928  1.00 16.11  ? 62  LEU A CB  1 
ATOM   511  C  CG  . LEU A 1 67  ? 26.135 -3.206  14.547  1.00 16.48  ? 62  LEU A CG  1 
ATOM   512  C  CD1 . LEU A 1 67  ? 27.406 -2.792  13.902  1.00 16.60  ? 62  LEU A CD1 1 
ATOM   513  C  CD2 . LEU A 1 67  ? 26.037 -4.721  14.544  1.00 17.31  ? 62  LEU A CD2 1 
ATOM   514  N  N   . SER A 1 68  ? 24.481 -1.006  18.264  1.00 16.61  ? 63  SER A N   1 
ATOM   515  C  CA  . SER A 1 68  ? 24.447 -0.453  19.608  1.00 18.93  ? 63  SER A CA  1 
ATOM   516  C  C   . SER A 1 68  ? 23.296 -1.079  20.404  1.00 19.58  ? 63  SER A C   1 
ATOM   517  O  O   . SER A 1 68  ? 23.419 -1.400  21.596  1.00 20.46  ? 63  SER A O   1 
ATOM   518  C  CB  . SER A 1 68  ? 24.438 1.093   19.511  1.00 20.22  ? 63  SER A CB  1 
ATOM   519  O  OG  . SER A 1 68  ? 24.423 1.631   20.830  1.00 23.81  ? 63  SER A OG  1 
ATOM   520  N  N   . SER A 1 69  ? 22.187 -1.309  19.743  1.00 18.68  ? 64  SER A N   1 
ATOM   521  C  CA  . SER A 1 69  ? 21.041 -1.894  20.424  1.00 21.28  ? 64  SER A CA  1 
ATOM   522  C  C   . SER A 1 69  ? 21.297 -3.341  20.833  1.00 22.83  ? 64  SER A C   1 
ATOM   523  O  O   . SER A 1 69  ? 20.995 -3.736  21.957  1.00 24.23  ? 64  SER A O   1 
ATOM   524  C  CB  . SER A 1 69  ? 19.818 -1.770  19.552  1.00 23.31  ? 64  SER A CB  1 
ATOM   525  O  OG  . SER A 1 69  ? 18.778 -2.535  20.110  1.00 31.92  ? 64  SER A OG  1 
ATOM   526  N  N   . ILE A 1 70  ? 21.949 -4.098  19.947  1.00 20.14  ? 65  ILE A N   1 
ATOM   527  C  CA  . ILE A 1 70  ? 22.315 -5.477  20.265  1.00 22.64  ? 65  ILE A CA  1 
ATOM   528  C  C   . ILE A 1 70  ? 23.281 -5.481  21.444  1.00 23.45  ? 65  ILE A C   1 
ATOM   529  O  O   . ILE A 1 70  ? 23.148 -6.260  22.406  1.00 25.74  ? 65  ILE A O   1 
ATOM   530  C  CB  . ILE A 1 70  ? 22.888 -6.179  19.011  1.00 20.00  ? 65  ILE A CB  1 
ATOM   531  C  CG1 . ILE A 1 70  ? 21.838 -6.272  17.923  1.00 19.75  ? 65  ILE A CG1 1 
ATOM   532  C  CG2 . ILE A 1 70  ? 23.538 -7.531  19.385  1.00 20.60  ? 65  ILE A CG2 1 
ATOM   533  C  CD1 . ILE A 1 70  ? 22.348 -6.700  16.592  1.00 19.87  ? 65  ILE A CD1 1 
ATOM   534  N  N   . GLU A 1 71  ? 24.228 -4.550  21.401  1.00 19.49  ? 66  GLU A N   1 
ATOM   535  C  CA  . GLU A 1 71  ? 25.264 -4.448  22.406  1.00 22.74  ? 66  GLU A CA  1 
ATOM   536  C  C   . GLU A 1 71  ? 24.636 -4.122  23.761  1.00 27.75  ? 66  GLU A C   1 
ATOM   537  O  O   . GLU A 1 71  ? 24.963 -4.734  24.787  1.00 25.20  ? 66  GLU A O   1 
ATOM   538  C  CB  . GLU A 1 71  ? 26.251 -3.403  21.988  1.00 21.71  ? 66  GLU A CB  1 
ATOM   539  C  CG  . GLU A 1 71  ? 27.505 -3.329  22.850  1.00 23.13  ? 66  GLU A CG  1 
ATOM   540  C  CD  . GLU A 1 71  ? 28.453 -2.229  22.461  1.00 25.44  ? 66  GLU A CD  1 
ATOM   541  O  OE1 . GLU A 1 71  ? 28.055 -1.363  21.632  1.00 26.09  ? 66  GLU A OE1 1 
ATOM   542  O  OE2 . GLU A 1 71  ? 29.560 -2.166  23.056  1.00 24.00  ? 66  GLU A OE2 1 
ATOM   543  N  N   . GLN A 1 72  ? 23.699 -3.181  23.735  1.00 26.43  ? 67  GLN A N   1 
ATOM   544  C  CA  . GLN A 1 72  ? 23.063 -2.735  24.962  1.00 33.15  ? 67  GLN A CA  1 
ATOM   545  C  C   . GLN A 1 72  ? 22.309 -3.911  25.567  1.00 34.94  ? 67  GLN A C   1 
ATOM   546  O  O   . GLN A 1 72  ? 22.368 -4.113  26.783  1.00 38.11  ? 67  GLN A O   1 
ATOM   547  C  CB  . GLN A 1 72  ? 22.111 -1.552  24.741  1.00 36.20  ? 67  GLN A CB  1 
ATOM   548  C  CG  . GLN A 1 72  ? 22.801 -0.188  24.463  1.00 41.85  ? 67  GLN A CG  1 
ATOM   549  C  CD  . GLN A 1 72  ? 24.069 0.069   25.261  1.00 51.01  ? 67  GLN A CD  1 
ATOM   550  O  OE1 . GLN A 1 72  ? 24.072 0.057   26.514  1.00 59.67  ? 67  GLN A OE1 1 
ATOM   551  N  NE2 . GLN A 1 72  ? 25.192 0.324   24.563  1.00 54.53  ? 67  GLN A NE2 1 
ATOM   552  N  N   . LYS A 1 73  ? 21.614 -4.670  24.717  1.00 31.43  ? 68  LYS A N   1 
ATOM   553  C  CA  . LYS A 1 73  ? 20.870 -5.826  25.187  1.00 40.13  ? 68  LYS A CA  1 
ATOM   554  C  C   . LYS A 1 73  ? 21.770 -6.899  25.782  1.00 42.66  ? 68  LYS A C   1 
ATOM   555  O  O   . LYS A 1 73  ? 21.397 -7.510  26.779  1.00 44.05  ? 68  LYS A O   1 
ATOM   556  C  CB  . LYS A 1 73  ? 19.998 -6.407  24.096  1.00 42.68  ? 68  LYS A CB  1 
ATOM   557  C  CG  . LYS A 1 73  ? 18.807 -5.484  23.828  1.00 49.86  ? 68  LYS A CG  1 
ATOM   558  C  CD  . LYS A 1 73  ? 17.908 -5.940  22.695  1.00 57.04  ? 68  LYS A CD  1 
ATOM   559  C  CE  . LYS A 1 73  ? 17.201 -4.779  22.006  1.00 62.81  ? 68  LYS A CE  1 
ATOM   560  N  NZ  . LYS A 1 73  ? 16.316 -3.997  22.927  1.00 68.90  ? 68  LYS A NZ  1 
ATOM   561  N  N   . SER A 1 74  ? 22.956 -7.106  25.201  1.00 39.46  ? 69  SER A N   1 
ATOM   562  C  CA  . SER A 1 74  ? 23.880 -8.101  25.723  1.00 44.05  ? 69  SER A CA  1 
ATOM   563  C  C   . SER A 1 74  ? 24.458 -7.725  27.088  1.00 47.34  ? 69  SER A C   1 
ATOM   564  O  O   . SER A 1 74  ? 24.906 -8.598  27.830  1.00 49.45  ? 69  SER A O   1 
ATOM   565  C  CB  . SER A 1 74  ? 25.035 -8.337  24.761  1.00 44.39  ? 69  SER A CB  1 
ATOM   566  O  OG  . SER A 1 74  ? 25.979 -7.284  24.878  1.00 45.55  ? 69  SER A OG  1 
ATOM   567  N  N   . ASN A 1 75  ? 24.467 -6.428  27.410  1.00 49.34  ? 70  ASN A N   1 
ATOM   568  C  CA  . ASN A 1 75  ? 24.973 -5.952  28.686  1.00 53.84  ? 70  ASN A CA  1 
ATOM   569  C  C   . ASN A 1 75  ? 23.844 -5.715  29.682  1.00 57.69  ? 70  ASN A C   1 
ATOM   570  O  O   . ASN A 1 75  ? 23.718 -4.630  30.238  1.00 65.97  ? 70  ASN A O   1 
ATOM   571  C  CB  . ASN A 1 75  ? 25.788 -4.666  28.507  1.00 53.03  ? 70  ASN A CB  1 
ATOM   572  C  CG  . ASN A 1 75  ? 27.017 -4.882  27.681  1.00 53.83  ? 70  ASN A CG  1 
ATOM   573  O  OD1 . ASN A 1 75  ? 27.676 -5.923  27.787  1.00 60.50  ? 70  ASN A OD1 1 
ATOM   574  N  ND2 . ASN A 1 75  ? 27.352 -3.923  26.815  1.00 51.62  ? 70  ASN A ND2 1 
ATOM   575  N  N   . GLU A 1 76  ? 23.020 -6.743  29.884  1.00 62.05  ? 71  GLU A N   1 
ATOM   576  C  CA  . GLU A 1 76  ? 22.036 -6.750  30.950  1.00 64.03  ? 71  GLU A CA  1 
ATOM   577  C  C   . GLU A 1 76  ? 22.064 -8.058  31.737  1.00 68.55  ? 71  GLU A C   1 
ATOM   578  O  O   . GLU A 1 76  ? 22.843 -8.959  31.436  1.00 71.62  ? 71  GLU A O   1 
ATOM   579  C  CB  . GLU A 1 76  ? 20.671 -6.515  30.348  1.00 61.00  ? 71  GLU A CB  1 
ATOM   580  C  CG  . GLU A 1 76  ? 20.390 -5.052  30.160  1.00 62.71  ? 71  GLU A CG  1 
ATOM   581  C  CD  . GLU A 1 76  ? 19.280 -4.814  29.175  1.00 62.49  ? 71  GLU A CD  1 
ATOM   582  O  OE1 . GLU A 1 76  ? 18.768 -5.809  28.608  1.00 55.81  ? 71  GLU A OE1 1 
ATOM   583  O  OE2 . GLU A 1 76  ? 18.932 -3.630  28.960  1.00 64.17  ? 71  GLU A OE2 1 
ATOM   584  N  N   . GLU A 1 77  ? 21.207 -8.125  32.762  1.00 78.22  ? 72  GLU A N   1 
ATOM   585  C  CA  . GLU A 1 77  ? 21.022 -9.314  33.577  1.00 77.15  ? 72  GLU A CA  1 
ATOM   586  C  C   . GLU A 1 77  ? 20.291 -10.370 32.754  1.00 72.42  ? 72  GLU A C   1 
ATOM   587  O  O   . GLU A 1 77  ? 19.518 -10.030 31.863  1.00 71.68  ? 72  GLU A O   1 
ATOM   588  C  CB  . GLU A 1 77  ? 20.220 -8.970  34.848  1.00 82.37  ? 72  GLU A CB  1 
ATOM   589  C  CG  . GLU A 1 77  ? 20.943 -8.056  35.835  1.00 87.82  ? 72  GLU A CG  1 
ATOM   590  C  CD  . GLU A 1 77  ? 21.251 -6.637  35.379  1.00 88.96  ? 72  GLU A CD  1 
ATOM   591  O  OE1 . GLU A 1 77  ? 20.900 -6.277  34.232  1.00 90.86  ? 72  GLU A OE1 1 
ATOM   592  O  OE2 . GLU A 1 77  ? 21.845 -5.880  36.182  1.00 95.19  ? 72  GLU A OE2 1 
ATOM   593  N  N   . GLY A 1 78  ? 20.557 -11.650 33.037  1.00 72.97  ? 73  GLY A N   1 
ATOM   594  C  CA  . GLY A 1 78  ? 19.961 -12.744 32.285  1.00 72.17  ? 73  GLY A CA  1 
ATOM   595  C  C   . GLY A 1 78  ? 20.638 -13.010 30.939  1.00 73.36  ? 73  GLY A C   1 
ATOM   596  O  O   . GLY A 1 78  ? 20.497 -14.102 30.380  1.00 70.13  ? 73  GLY A O   1 
ATOM   597  N  N   . SER A 1 79  ? 21.369 -12.003 30.431  1.00 74.59  ? 74  SER A N   1 
ATOM   598  C  CA  . SER A 1 79  ? 22.019 -12.069 29.129  1.00 69.40  ? 74  SER A CA  1 
ATOM   599  C  C   . SER A 1 79  ? 23.276 -12.931 29.191  1.00 66.85  ? 74  SER A C   1 
ATOM   600  O  O   . SER A 1 79  ? 24.147 -12.705 30.026  1.00 71.91  ? 74  SER A O   1 
ATOM   601  C  CB  . SER A 1 79  ? 22.407 -10.678 28.622  1.00 67.54  ? 74  SER A CB  1 
ATOM   602  O  OG  . SER A 1 79  ? 21.335 -9.753  28.694  1.00 67.85  ? 74  SER A OG  1 
ATOM   603  N  N   . GLU A 1 80  ? 23.361 -13.908 28.287  1.00 61.83  ? 75  GLU A N   1 
ATOM   604  C  CA  . GLU A 1 80  ? 24.501 -14.806 28.229  1.00 60.88  ? 75  GLU A CA  1 
ATOM   605  C  C   . GLU A 1 80  ? 25.699 -14.045 27.653  1.00 61.24  ? 75  GLU A C   1 
ATOM   606  O  O   . GLU A 1 80  ? 25.545 -13.190 26.776  1.00 59.29  ? 75  GLU A O   1 
ATOM   607  C  CB  . GLU A 1 80  ? 24.116 -16.061 27.403  1.00 57.52  ? 75  GLU A CB  1 
ATOM   608  C  CG  . GLU A 1 80  ? 24.988 -17.278 27.653  1.00 59.34  ? 75  GLU A CG  1 
ATOM   609  C  CD  . GLU A 1 80  ? 25.063 -17.686 29.111  1.00 56.30  ? 75  GLU A CD  1 
ATOM   610  O  OE1 . GLU A 1 80  ? 23.995 -17.870 29.748  1.00 52.83  ? 75  GLU A OE1 1 
ATOM   611  O  OE2 . GLU A 1 80  ? 26.202 -17.803 29.622  1.00 59.06  ? 75  GLU A OE2 1 
ATOM   612  N  N   . GLU A 1 81  ? 26.884 -14.320 28.215  1.00 58.40  ? 76  GLU A N   1 
ATOM   613  C  CA  . GLU A 1 81  ? 28.132 -13.742 27.741  1.00 54.61  ? 76  GLU A CA  1 
ATOM   614  C  C   . GLU A 1 81  ? 28.430 -14.274 26.343  1.00 49.90  ? 76  GLU A C   1 
ATOM   615  O  O   . GLU A 1 81  ? 28.294 -15.474 26.104  1.00 47.45  ? 76  GLU A O   1 
ATOM   616  C  CB  . GLU A 1 81  ? 29.277 -14.101 28.696  1.00 55.15  ? 76  GLU A CB  1 
ATOM   617  C  CG  . GLU A 1 81  ? 30.640 -13.642 28.227  1.00 55.69  ? 76  GLU A CG  1 
ATOM   618  C  CD  . GLU A 1 81  ? 30.656 -12.172 27.870  1.00 56.99  ? 76  GLU A CD  1 
ATOM   619  O  OE1 . GLU A 1 81  ? 30.068 -11.380 28.640  1.00 55.57  ? 76  GLU A OE1 1 
ATOM   620  O  OE2 . GLU A 1 81  ? 31.250 -11.813 26.827  1.00 54.98  ? 76  GLU A OE2 1 
ATOM   621  N  N   . LYS A 1 82  ? 28.813 -13.385 25.418  1.00 41.69  ? 77  LYS A N   1 
ATOM   622  C  CA  . LYS A 1 82  ? 29.056 -13.802 24.042  1.00 44.31  ? 77  LYS A CA  1 
ATOM   623  C  C   . LYS A 1 82  ? 30.413 -13.361 23.492  1.00 41.63  ? 77  LYS A C   1 
ATOM   624  O  O   . LYS A 1 82  ? 30.700 -13.520 22.302  1.00 44.96  ? 77  LYS A O   1 
ATOM   625  C  CB  . LYS A 1 82  ? 27.900 -13.298 23.146  1.00 48.03  ? 77  LYS A CB  1 
ATOM   626  C  CG  . LYS A 1 82  ? 26.539 -13.909 23.521  1.00 50.27  ? 77  LYS A CG  1 
ATOM   627  C  CD  . LYS A 1 82  ? 26.526 -15.491 23.449  1.00 51.58  ? 77  LYS A CD  1 
ATOM   628  C  CE  . LYS A 1 82  ? 25.248 -16.136 23.942  1.00 50.49  ? 77  LYS A CE  1 
ATOM   629  N  NZ  . LYS A 1 82  ? 24.027 -15.378 23.525  1.00 50.35  ? 77  LYS A NZ  1 
ATOM   630  N  N   . GLY A 1 83  ? 31.258 -12.825 24.379  1.00 31.93  ? 78  GLY A N   1 
ATOM   631  C  CA  . GLY A 1 83  ? 32.577 -12.421 23.960  1.00 25.76  ? 78  GLY A CA  1 
ATOM   632  C  C   . GLY A 1 83  ? 32.589 -11.000 23.425  1.00 21.68  ? 78  GLY A C   1 
ATOM   633  O  O   . GLY A 1 83  ? 31.596 -10.291 23.470  1.00 22.13  ? 78  GLY A O   1 
ATOM   634  N  N   . PRO A 1 84  ? 33.736 -10.589 22.867  1.00 18.96  ? 79  PRO A N   1 
ATOM   635  C  CA  . PRO A 1 84  ? 33.961 -9.211  22.468  1.00 17.37  ? 79  PRO A CA  1 
ATOM   636  C  C   . PRO A 1 84  ? 33.401 -8.824  21.097  1.00 16.66  ? 79  PRO A C   1 
ATOM   637  O  O   . PRO A 1 84  ? 33.555 -7.670  20.707  1.00 14.71  ? 79  PRO A O   1 
ATOM   638  C  CB  . PRO A 1 84  ? 35.485 -9.156  22.458  1.00 17.98  ? 79  PRO A CB  1 
ATOM   639  C  CG  . PRO A 1 84  ? 35.878 -10.545 22.012  1.00 18.99  ? 79  PRO A CG  1 
ATOM   640  C  CD  . PRO A 1 84  ? 34.920 -11.440 22.669  1.00 19.89  ? 79  PRO A CD  1 
ATOM   641  N  N   . GLU A 1 85  ? 32.768 -9.762  20.385  1.00 16.34  ? 80  GLU A N   1 
ATOM   642  C  CA  . GLU A 1 85  ? 32.509 -9.551  18.967  1.00 15.43  ? 80  GLU A CA  1 
ATOM   643  C  C   . GLU A 1 85  ? 31.521 -8.421  18.692  1.00 14.74  ? 80  GLU A C   1 
ATOM   644  O  O   . GLU A 1 85  ? 31.696 -7.692  17.723  1.00 15.54  ? 80  GLU A O   1 
ATOM   645  C  CB  . GLU A 1 85  ? 32.000 -10.827 18.281  1.00 15.03  ? 80  GLU A CB  1 
ATOM   646  C  CG  . GLU A 1 85  ? 33.056 -11.930 18.197  1.00 17.51  ? 80  GLU A CG  1 
ATOM   647  C  CD  . GLU A 1 85  ? 33.216 -12.844 19.404  1.00 20.22  ? 80  GLU A CD  1 
ATOM   648  O  OE1 . GLU A 1 85  ? 32.533 -12.617 20.433  1.00 17.82  ? 80  GLU A OE1 1 
ATOM   649  O  OE2 . GLU A 1 85  ? 34.042 -13.788 19.313  1.00 20.56  ? 80  GLU A OE2 1 
ATOM   650  N  N   . VAL A 1 86  ? 30.445 -8.314  19.470  1.00 14.77  ? 81  VAL A N   1 
ATOM   651  C  CA  . VAL A 1 86  ? 29.472 -7.261  19.231  1.00 16.85  ? 81  VAL A CA  1 
ATOM   652  C  C   . VAL A 1 86  ? 30.096 -5.883  19.424  1.00 16.56  ? 81  VAL A C   1 
ATOM   653  O  O   . VAL A 1 86  ? 29.964 -4.989  18.576  1.00 15.86  ? 81  VAL A O   1 
ATOM   654  C  CB  . VAL A 1 86  ? 28.227 -7.415  20.114  1.00 19.82  ? 81  VAL A CB  1 
ATOM   655  C  CG1 . VAL A 1 86  ? 27.367 -6.181  19.977  1.00 20.91  ? 81  VAL A CG1 1 
ATOM   656  C  CG2 . VAL A 1 86  ? 27.414 -8.654  19.757  1.00 22.27  ? 81  VAL A CG2 1 
ATOM   657  N  N   . ARG A 1 87  ? 30.835 -5.715  20.521  1.00 15.15  ? 82  ARG A N   1 
ATOM   658  C  CA  . ARG A 1 87  ? 31.529 -4.457  20.771  1.00 15.23  ? 82  ARG A CA  1 
ATOM   659  C  C   . ARG A 1 87  ? 32.553 -4.166  19.669  1.00 14.38  ? 82  ARG A C   1 
ATOM   660  O  O   . ARG A 1 87  ? 32.671 -3.037  19.179  1.00 15.25  ? 82  ARG A O   1 
ATOM   661  C  CB  . ARG A 1 87  ? 32.236 -4.450  22.146  1.00 17.66  ? 82  ARG A CB  1 
ATOM   662  C  CG  . ARG A 1 87  ? 33.150 -3.214  22.346  1.00 20.14  ? 82  ARG A CG  1 
ATOM   663  C  CD  . ARG A 1 87  ? 34.023 -3.257  23.620  1.00 23.86  ? 82  ARG A CD  1 
ATOM   664  N  NE  . ARG A 1 87  ? 34.829 -4.466  23.706  1.00 28.47  ? 82  ARG A NE  1 
ATOM   665  C  CZ  . ARG A 1 87  ? 35.935 -4.752  23.006  1.00 28.71  ? 82  ARG A CZ  1 
ATOM   666  N  NH1 . ARG A 1 87  ? 36.456 -3.902  22.145  1.00 31.15  ? 82  ARG A NH1 1 
ATOM   667  N  NH2 . ARG A 1 87  ? 36.541 -5.920  23.205  1.00 27.03  ? 82  ARG A NH2 1 
ATOM   668  N  N   . GLU A 1 88  ? 33.333 -5.174  19.265  1.00 13.54  ? 83  GLU A N   1 
ATOM   669  C  CA  . GLU A 1 88  ? 34.348 -4.971  18.243  1.00 13.11  ? 83  GLU A CA  1 
ATOM   670  C  C   . GLU A 1 88  ? 33.731 -4.469  16.942  1.00 12.76  ? 83  GLU A C   1 
ATOM   671  O  O   . GLU A 1 88  ? 34.276 -3.579  16.288  1.00 14.57  ? 83  GLU A O   1 
ATOM   672  C  CB  . GLU A 1 88  ? 35.087 -6.277  17.959  1.00 14.64  ? 83  GLU A CB  1 
ATOM   673  C  CG  . GLU A 1 88  ? 36.100 -6.668  19.001  1.00 15.24  ? 83  GLU A CG  1 
ATOM   674  C  CD  . GLU A 1 88  ? 36.669 -8.078  18.881  1.00 18.18  ? 83  GLU A CD  1 
ATOM   675  O  OE1 . GLU A 1 88  ? 36.222 -8.857  18.011  1.00 16.68  ? 83  GLU A OE1 1 
ATOM   676  O  OE2 . GLU A 1 88  ? 37.615 -8.375  19.647  1.00 17.84  ? 83  GLU A OE2 1 
ATOM   677  N  N   . TYR A 1 89  ? 32.650 -5.132  16.521  1.00 12.38  ? 84  TYR A N   1 
ATOM   678  C  CA  . TYR A 1 89  ? 32.031 -4.798  15.249  1.00 12.89  ? 84  TYR A CA  1 
ATOM   679  C  C   . TYR A 1 89  ? 31.330 -3.431  15.321  1.00 12.84  ? 84  TYR A C   1 
ATOM   680  O  O   . TYR A 1 89  ? 31.400 -2.618  14.377  1.00 13.74  ? 84  TYR A O   1 
ATOM   681  C  CB  . TYR A 1 89  ? 31.096 -5.897  14.764  1.00 13.20  ? 84  TYR A CB  1 
ATOM   682  C  CG  . TYR A 1 89  ? 30.574 -5.659  13.351  1.00 12.69  ? 84  TYR A CG  1 
ATOM   683  C  CD1 . TYR A 1 89  ? 31.433 -5.308  12.314  1.00 13.66  ? 84  TYR A CD1 1 
ATOM   684  C  CD2 . TYR A 1 89  ? 29.237 -5.780  13.064  1.00 14.47  ? 84  TYR A CD2 1 
ATOM   685  C  CE1 . TYR A 1 89  ? 30.943 -4.987  11.043  1.00 14.47  ? 84  TYR A CE1 1 
ATOM   686  C  CE2 . TYR A 1 89  ? 28.746 -5.538  11.793  1.00 14.91  ? 84  TYR A CE2 1 
ATOM   687  C  CZ  . TYR A 1 89  ? 29.592 -5.114  10.800  1.00 14.56  ? 84  TYR A CZ  1 
ATOM   688  O  OH  . TYR A 1 89  ? 29.086 -4.829  9.573   1.00 16.34  ? 84  TYR A OH  1 
ATOM   689  N  N   . ARG A 1 90  ? 30.676 -3.146  16.453  1.00 13.36  ? 85  ARG A N   1 
ATOM   690  C  CA  . ARG A 1 90  ? 30.125 -1.801  16.637  1.00 14.20  ? 85  ARG A CA  1 
ATOM   691  C  C   . ARG A 1 90  ? 31.211 -0.732  16.575  1.00 15.53  ? 85  ARG A C   1 
ATOM   692  O  O   . ARG A 1 90  ? 31.013 0.300   15.921  1.00 15.25  ? 85  ARG A O   1 
ATOM   693  C  CB  . ARG A 1 90  ? 29.350 -1.727  17.936  1.00 15.42  ? 85  ARG A CB  1 
ATOM   694  C  CG  . ARG A 1 90  ? 28.574 -0.428  18.244  1.00 15.28  ? 85  ARG A CG  1 
ATOM   695  C  CD  . ARG A 1 90  ? 29.406 0.607   18.908  1.00 15.93  ? 85  ARG A CD  1 
ATOM   696  N  NE  . ARG A 1 90  ? 29.824 0.178   20.235  1.00 17.37  ? 85  ARG A NE  1 
ATOM   697  C  CZ  . ARG A 1 90  ? 30.893 0.601   20.892  1.00 19.30  ? 85  ARG A CZ  1 
ATOM   698  N  NH1 . ARG A 1 90  ? 31.631 1.621   20.472  1.00 21.15  ? 85  ARG A NH1 1 
ATOM   699  N  NH2 . ARG A 1 90  ? 31.191 0.033   22.062  1.00 22.05  ? 85  ARG A NH2 1 
ATOM   700  N  N   . GLU A 1 91  ? 32.358 -0.990  17.199  1.00 14.36  ? 86  GLU A N   1 
ATOM   701  C  CA  . GLU A 1 91  ? 33.496 -0.092  17.135  1.00 15.73  ? 86  GLU A CA  1 
ATOM   702  C  C   . GLU A 1 91  ? 34.012 0.090   15.706  1.00 15.82  ? 86  GLU A C   1 
ATOM   703  O  O   . GLU A 1 91  ? 34.416 1.175   15.318  1.00 16.93  ? 86  GLU A O   1 
ATOM   704  C  CB  . GLU A 1 91  ? 34.623 -0.590  18.068  1.00 17.23  ? 86  GLU A CB  1 
ATOM   705  C  CG  . GLU A 1 91  ? 34.351 -0.435  19.562  1.00 20.39  ? 86  GLU A CG  1 
ATOM   706  C  CD  . GLU A 1 91  ? 35.438 -1.016  20.492  1.00 31.50  ? 86  GLU A CD  1 
ATOM   707  O  OE1 . GLU A 1 91  ? 36.325 -1.765  20.005  1.00 34.54  ? 86  GLU A OE1 1 
ATOM   708  O  OE2 . GLU A 1 91  ? 35.396 -0.719  21.714  1.00 36.12  ? 86  GLU A OE2 1 
ATOM   709  N  N   . LYS A 1 92  ? 34.003 -0.973  14.906  1.00 15.58  ? 87  LYS A N   1 
ATOM   710  C  CA  . LYS A 1 92  ? 34.478 -0.904  13.534  1.00 16.45  ? 87  LYS A CA  1 
ATOM   711  C  C   . LYS A 1 92  ? 33.588 0.047   12.728  1.00 14.56  ? 87  LYS A C   1 
ATOM   712  O  O   . LYS A 1 92  ? 34.093 0.914   12.025  1.00 15.39  ? 87  LYS A O   1 
ATOM   713  C  CB  . LYS A 1 92  ? 34.421 -2.279  12.887  1.00 18.90  ? 87  LYS A CB  1 
ATOM   714  C  CG  . LYS A 1 92  ? 34.975 -2.300  11.453  1.00 24.04  ? 87  LYS A CG  1 
ATOM   715  C  CD  . LYS A 1 92  ? 34.686 -3.634  10.739  1.00 29.06  ? 87  LYS A CD  1 
ATOM   716  C  CE  . LYS A 1 92  ? 35.279 -3.655  9.327   1.00 36.60  ? 87  LYS A CE  1 
ATOM   717  N  NZ  . LYS A 1 92  ? 35.065 -4.987  8.716   1.00 41.87  ? 87  LYS A NZ  1 
ATOM   718  N  N   . VAL A 1 93  ? 32.283 -0.164  12.826  1.00 13.09  ? 88  VAL A N   1 
ATOM   719  C  CA  . VAL A 1 93  ? 31.321 0.680   12.131  1.00 13.76  ? 88  VAL A CA  1 
ATOM   720  C  C   . VAL A 1 93  ? 31.449 2.124   12.632  1.00 13.25  ? 88  VAL A C   1 
ATOM   721  O  O   . VAL A 1 93  ? 31.460 3.059   11.823  1.00 12.71  ? 88  VAL A O   1 
ATOM   722  C  CB  . VAL A 1 93  ? 29.919 0.137   12.241  1.00 14.31  ? 88  VAL A CB  1 
ATOM   723  C  CG1 . VAL A 1 93  ? 28.892 1.108   11.713  1.00 14.40  ? 88  VAL A CG1 1 
ATOM   724  C  CG2 . VAL A 1 93  ? 29.786 -1.208  11.548  1.00 14.49  ? 88  VAL A CG2 1 
ATOM   725  N  N   . GLU A 1 94  ? 31.528 2.309   13.968  1.00 13.53  ? 89  GLU A N   1 
ATOM   726  C  CA  . GLU A 1 94  ? 31.735 3.619   14.577  1.00 13.97  ? 89  GLU A CA  1 
ATOM   727  C  C   . GLU A 1 94  ? 32.947 4.379   14.028  1.00 14.55  ? 89  GLU A C   1 
ATOM   728  O  O   . GLU A 1 94  ? 32.889 5.566   13.693  1.00 14.58  ? 89  GLU A O   1 
ATOM   729  C  CB  . GLU A 1 94  ? 31.805 3.427   16.074  1.00 14.29  ? 89  GLU A CB  1 
ATOM   730  C  CG  . GLU A 1 94  ? 31.883 4.700   16.849  1.00 15.61  ? 89  GLU A CG  1 
ATOM   731  C  CD  . GLU A 1 94  ? 31.773 4.455   18.346  1.00 16.39  ? 89  GLU A CD  1 
ATOM   732  O  OE1 . GLU A 1 94  ? 30.774 3.837   18.794  1.00 16.24  ? 89  GLU A OE1 1 
ATOM   733  O  OE2 . GLU A 1 94  ? 32.691 4.924   19.062  1.00 20.47  ? 89  GLU A OE2 1 
ATOM   734  N  N   . THR A 1 95  ? 34.083 3.683   13.930  1.00 15.16  ? 90  THR A N   1 
ATOM   735  C  CA  . THR A 1 95  ? 35.298 4.279   13.415  1.00 15.42  ? 90  THR A CA  1 
ATOM   736  C  C   . THR A 1 95  ? 35.116 4.721   11.966  1.00 14.37  ? 90  THR A C   1 
ATOM   737  O  O   . THR A 1 95  ? 35.607 5.768   11.591  1.00 15.38  ? 90  THR A O   1 
ATOM   738  C  CB  . THR A 1 95  ? 36.476 3.254   13.611  1.00 18.11  ? 90  THR A CB  1 
ATOM   739  O  OG1 . THR A 1 95  ? 36.600 3.025   15.014  1.00 19.36  ? 90  THR A OG1 1 
ATOM   740  C  CG2 . THR A 1 95  ? 37.717 3.767   13.106  1.00 21.90  ? 90  THR A CG2 1 
ATOM   741  N  N   . GLU A 1 96  ? 34.433 3.918   11.143  1.00 13.09  ? 91  GLU A N   1 
ATOM   742  C  CA  . GLU A 1 96  ? 34.220 4.265   9.753   1.00 14.57  ? 91  GLU A CA  1 
ATOM   743  C  C   . GLU A 1 96  ? 33.328 5.498   9.641   1.00 14.03  ? 91  GLU A C   1 
ATOM   744  O  O   . GLU A 1 96  ? 33.590 6.369   8.801   1.00 13.71  ? 91  GLU A O   1 
ATOM   745  C  CB  . GLU A 1 96  ? 33.599 3.100   8.963   1.00 17.33  ? 91  GLU A CB  1 
ATOM   746  C  CG  . GLU A 1 96  ? 34.503 1.885   8.955   1.00 21.01  ? 91  GLU A CG  1 
ATOM   747  C  CD  . GLU A 1 96  ? 34.170 0.762   7.982   1.00 27.28  ? 91  GLU A CD  1 
ATOM   748  O  OE1 . GLU A 1 96  ? 33.234 0.892   7.143   1.00 25.20  ? 91  GLU A OE1 1 
ATOM   749  O  OE2 . GLU A 1 96  ? 34.944 -0.238  8.041   1.00 30.77  ? 91  GLU A OE2 1 
ATOM   750  N  N   . LEU A 1 97  ? 32.253 5.516   10.440  1.00 13.12  ? 92  LEU A N   1 
ATOM   751  C  CA  . LEU A 1 97  ? 31.384 6.685   10.536  1.00 14.76  ? 92  LEU A CA  1 
ATOM   752  C  C   . LEU A 1 97  ? 32.136 7.966   10.907  1.00 14.46  ? 92  LEU A C   1 
ATOM   753  O  O   . LEU A 1 97  ? 31.967 9.001   10.251  1.00 15.37  ? 92  LEU A O   1 
ATOM   754  C  CB  . LEU A 1 97  ? 30.274 6.343   11.545  1.00 15.04  ? 92  LEU A CB  1 
ATOM   755  C  CG  . LEU A 1 97  ? 29.097 7.335   11.716  1.00 16.88  ? 92  LEU A CG  1 
ATOM   756  C  CD1 . LEU A 1 97  ? 27.934 6.647   12.366  1.00 18.48  ? 92  LEU A CD1 1 
ATOM   757  C  CD2 . LEU A 1 97  ? 29.484 8.482   12.548  1.00 19.15  ? 92  LEU A CD2 1 
ATOM   758  N  N   . GLN A 1 98  ? 32.983 7.891   11.938  1.00 14.49  ? 93  GLN A N   1 
ATOM   759  C  CA  . GLN A 1 98  ? 33.749 9.035   12.387  1.00 15.33  ? 93  GLN A CA  1 
ATOM   760  C  C   . GLN A 1 98  ? 34.666 9.467   11.260  1.00 15.68  ? 93  GLN A C   1 
ATOM   761  O  O   . GLN A 1 98  ? 34.953 10.656  11.094  1.00 16.02  ? 93  GLN A O   1 
ATOM   762  C  CB  . GLN A 1 98  ? 34.546 8.698   13.646  1.00 16.20  ? 93  GLN A CB  1 
ATOM   763  C  CG  . GLN A 1 98  ? 33.615 8.527   14.834  1.00 16.01  ? 93  GLN A CG  1 
ATOM   764  C  CD  . GLN A 1 98  ? 34.308 7.928   16.056  1.00 19.65  ? 93  GLN A CD  1 
ATOM   765  O  OE1 . GLN A 1 98  ? 35.187 7.044   15.924  1.00 18.00  ? 93  GLN A OE1 1 
ATOM   766  N  NE2 . GLN A 1 98  ? 33.919 8.328   17.270  1.00 18.37  ? 93  GLN A NE2 1 
ATOM   767  N  N   . GLY A 1 99  ? 35.210 8.481   10.533  1.00 14.79  ? 94  GLY A N   1 
ATOM   768  C  CA  . GLY A 1 99  ? 36.036 8.800   9.384   1.00 14.76  ? 94  GLY A CA  1 
ATOM   769  C  C   . GLY A 1 99  ? 35.370 9.623   8.295   1.00 13.91  ? 94  GLY A C   1 
ATOM   770  O  O   . GLY A 1 99  ? 35.929 10.574  7.768   1.00 14.84  ? 94  GLY A O   1 
ATOM   771  N  N   . VAL A 1 100 ? 34.162 9.253   7.953   1.00 13.38  ? 95  VAL A N   1 
ATOM   772  C  CA  . VAL A 1 100 ? 33.372 9.996   6.988   1.00 14.51  ? 95  VAL A CA  1 
ATOM   773  C  C   . VAL A 1 100 ? 33.061 11.400  7.496   1.00 15.18  ? 95  VAL A C   1 
ATOM   774  O  O   . VAL A 1 100 ? 33.244 12.374  6.770   1.00 13.60  ? 95  VAL A O   1 
ATOM   775  C  CB  . VAL A 1 100 ? 32.113 9.233   6.662   1.00 15.80  ? 95  VAL A CB  1 
ATOM   776  C  CG1 . VAL A 1 100 ? 31.114 10.088  5.914   1.00 18.15  ? 95  VAL A CG1 1 
ATOM   777  C  CG2 . VAL A 1 100 ? 32.450 7.981   5.880   1.00 17.57  ? 95  VAL A CG2 1 
ATOM   778  N  N   . CYS A 1 101 ? 32.652 11.507  8.762   1.00 14.31  ? 96  CYS A N   1 
ATOM   779  C  CA  . CYS A 1 101 ? 32.400 12.805  9.364   1.00 15.09  ? 96  CYS A CA  1 
ATOM   780  C  C   . CYS A 1 101 ? 33.658 13.655  9.320   1.00 15.01  ? 96  CYS A C   1 
ATOM   781  O  O   . CYS A 1 101 ? 33.570 14.821  8.962   1.00 15.65  ? 96  CYS A O   1 
ATOM   782  C  CB  . CYS A 1 101 ? 31.850 12.737  10.791  1.00 15.79  ? 96  CYS A CB  1 
ATOM   783  S  SG  . CYS A 1 101 ? 30.249 11.961  10.914  1.00 16.25  ? 96  CYS A SG  1 
ATOM   784  N  N   . ASP A 1 102 ? 34.807 13.089  9.690   1.00 13.67  ? 97  ASP A N   1 
ATOM   785  C  CA  . ASP A 1 102 ? 36.035 13.862  9.651   1.00 15.38  ? 97  ASP A CA  1 
ATOM   786  C  C   . ASP A 1 102 ? 36.433 14.287  8.238   1.00 14.44  ? 97  ASP A C   1 
ATOM   787  O  O   . ASP A 1 102 ? 36.981 15.373  8.051   1.00 14.50  ? 97  ASP A O   1 
ATOM   788  C  CB  . ASP A 1 102 ? 37.166 13.052  10.301  1.00 18.26  ? 97  ASP A CB  1 
ATOM   789  C  CG  . ASP A 1 102 ? 37.037 12.883  11.838  1.00 22.99  ? 97  ASP A CG  1 
ATOM   790  O  OD1 . ASP A 1 102 ? 36.292 13.636  12.448  1.00 26.08  ? 97  ASP A OD1 1 
ATOM   791  O  OD2 . ASP A 1 102 ? 37.704 11.991  12.390  1.00 27.57  ? 97  ASP A OD2 1 
ATOM   792  N  N   . THR A 1 103 ? 36.132 13.445  7.244   1.00 14.70  ? 98  THR A N   1 
ATOM   793  C  CA  . THR A 1 103 ? 36.392 13.812  5.856   1.00 14.75  ? 98  THR A CA  1 
ATOM   794  C  C   . THR A 1 103 ? 35.547 15.018  5.441   1.00 13.67  ? 98  THR A C   1 
ATOM   795  O  O   . THR A 1 103 ? 36.047 15.980  4.856   1.00 14.23  ? 98  THR A O   1 
ATOM   796  C  CB  . THR A 1 103 ? 36.072 12.634  4.944   1.00 17.27  ? 98  THR A CB  1 
ATOM   797  O  OG1 . THR A 1 103 ? 37.021 11.604  5.192   1.00 17.75  ? 98  THR A OG1 1 
ATOM   798  C  CG2 . THR A 1 103 ? 36.108 13.007  3.488   1.00 17.65  ? 98  THR A CG2 1 
ATOM   799  N  N   . VAL A 1 104 ? 34.251 14.999  5.792   1.00 13.95  ? 99  VAL A N   1 
ATOM   800  C  CA  . VAL A 1 104 ? 33.374 16.101  5.401   1.00 13.73  ? 99  VAL A CA  1 
ATOM   801  C  C   . VAL A 1 104 ? 33.843 17.378  6.121   1.00 13.17  ? 99  VAL A C   1 
ATOM   802  O  O   . VAL A 1 104 ? 33.941 18.456  5.525   1.00 12.25  ? 99  VAL A O   1 
ATOM   803  C  CB  . VAL A 1 104 ? 31.906 15.776  5.708   1.00 13.77  ? 99  VAL A CB  1 
ATOM   804  C  CG1 . VAL A 1 104 ? 31.000 17.037  5.625   1.00 15.11  ? 99  VAL A CG1 1 
ATOM   805  C  CG2 . VAL A 1 104 ? 31.400 14.640  4.803   1.00 14.59  ? 99  VAL A CG2 1 
ATOM   806  N  N   . LEU A 1 105 ? 34.093 17.272  7.440   1.00 12.28  ? 100 LEU A N   1 
ATOM   807  C  CA  . LEU A 1 105 ? 34.493 18.440  8.202   1.00 13.59  ? 100 LEU A CA  1 
ATOM   808  C  C   . LEU A 1 105 ? 35.797 19.000  7.649   1.00 14.02  ? 100 LEU A C   1 
ATOM   809  O  O   . LEU A 1 105 ? 35.999 20.223  7.655   1.00 16.23  ? 100 LEU A O   1 
ATOM   810  C  CB  . LEU A 1 105 ? 34.634 18.081  9.679   1.00 13.51  ? 100 LEU A CB  1 
ATOM   811  C  CG  . LEU A 1 105 ? 33.322 17.746  10.314  1.00 13.02  ? 100 LEU A CG  1 
ATOM   812  C  CD1 . LEU A 1 105 ? 33.494 17.191  11.699  1.00 15.34  ? 100 LEU A CD1 1 
ATOM   813  C  CD2 . LEU A 1 105 ? 32.427 18.975  10.447  1.00 13.15  ? 100 LEU A CD2 1 
ATOM   814  N  N   . GLY A 1 106 ? 36.665 18.095  7.145   1.00 14.73  ? 101 GLY A N   1 
ATOM   815  C  CA  . GLY A 1 106 ? 37.939 18.489  6.543   1.00 15.50  ? 101 GLY A CA  1 
ATOM   816  C  C   . GLY A 1 106 ? 37.755 19.313  5.271   1.00 16.93  ? 101 GLY A C   1 
ATOM   817  O  O   . GLY A 1 106 ? 38.434 20.333  5.091   1.00 19.36  ? 101 GLY A O   1 
ATOM   818  N  N   . LEU A 1 107 ? 36.786 18.909  4.431   1.00 12.95  ? 102 LEU A N   1 
ATOM   819  C  CA  . LEU A 1 107 ? 36.478 19.632  3.221   1.00 13.64  ? 102 LEU A CA  1 
ATOM   820  C  C   . LEU A 1 107 ? 35.913 21.008  3.554   1.00 13.46  ? 102 LEU A C   1 
ATOM   821  O  O   . LEU A 1 107 ? 36.234 22.002  2.897   1.00 14.26  ? 102 LEU A O   1 
ATOM   822  C  CB  . LEU A 1 107 ? 35.480 18.818  2.351   1.00 15.02  ? 102 LEU A CB  1 
ATOM   823  C  CG  . LEU A 1 107 ? 35.998 17.521  1.734   1.00 16.47  ? 102 LEU A CG  1 
ATOM   824  C  CD1 . LEU A 1 107 ? 34.860 16.814  1.059   1.00 18.16  ? 102 LEU A CD1 1 
ATOM   825  C  CD2 . LEU A 1 107 ? 37.151 17.729  0.747   1.00 19.06  ? 102 LEU A CD2 1 
ATOM   826  N  N   . LEU A 1 108 ? 35.063 21.061  4.600   1.00 13.12  ? 103 LEU A N   1 
ATOM   827  C  CA  . LEU A 1 108 ? 34.454 22.330  4.963   1.00 14.09  ? 103 LEU A CA  1 
ATOM   828  C  C   . LEU A 1 108 ? 35.517 23.269  5.516   1.00 13.38  ? 103 LEU A C   1 
ATOM   829  O  O   . LEU A 1 108 ? 35.497 24.470  5.221   1.00 15.24  ? 103 LEU A O   1 
ATOM   830  C  CB  . LEU A 1 108 ? 33.332 22.134  5.997   1.00 14.93  ? 103 LEU A CB  1 
ATOM   831  C  CG  . LEU A 1 108 ? 32.170 21.357  5.484   1.00 13.66  ? 103 LEU A CG  1 
ATOM   832  C  CD1 . LEU A 1 108 ? 31.237 20.937  6.584   1.00 15.42  ? 103 LEU A CD1 1 
ATOM   833  C  CD2 . LEU A 1 108 ? 31.341 22.144  4.494   1.00 14.94  ? 103 LEU A CD2 1 
ATOM   834  N  N   . ASP A 1 109 ? 36.466 22.727  6.273   1.00 14.32  ? 104 ASP A N   1 
ATOM   835  C  CA  . ASP A 1 109 ? 37.552 23.531  6.826   1.00 16.94  ? 104 ASP A CA  1 
ATOM   836  C  C   . ASP A 1 109 ? 38.684 23.882  5.863   1.00 18.29  ? 104 ASP A C   1 
ATOM   837  O  O   . ASP A 1 109 ? 39.450 24.833  6.124   1.00 18.77  ? 104 ASP A O   1 
ATOM   838  C  CB  . ASP A 1 109 ? 38.194 22.788  8.014   1.00 20.42  ? 104 ASP A CB  1 
ATOM   839  C  CG  . ASP A 1 109 ? 38.858 23.731  8.998   1.00 29.17  ? 104 ASP A CG  1 
ATOM   840  O  OD1 . ASP A 1 109 ? 38.179 24.741  9.430   1.00 34.42  ? 104 ASP A OD1 1 
ATOM   841  O  OD2 . ASP A 1 109 ? 40.013 23.480  9.350   1.00 30.57  ? 104 ASP A OD2 1 
ATOM   842  N  N   . SER A 1 110 ? 38.775 23.113  4.774   1.00 19.15  ? 105 SER A N   1 
ATOM   843  C  CA  . SER A 1 110 ? 39.828 23.243  3.789   1.00 21.43  ? 105 SER A CA  1 
ATOM   844  C  C   . SER A 1 110 ? 39.335 23.121  2.348   1.00 22.21  ? 105 SER A C   1 
ATOM   845  O  O   . SER A 1 110 ? 39.571 22.090  1.719   1.00 24.03  ? 105 SER A O   1 
ATOM   846  C  CB  . SER A 1 110 ? 40.876 22.156  4.043   1.00 25.51  ? 105 SER A CB  1 
ATOM   847  O  OG  . SER A 1 110 ? 41.399 22.283  5.340   1.00 28.55  ? 105 SER A OG  1 
ATOM   848  N  N   . HIS A 1 111 ? 38.676 24.138  1.775   1.00 19.80  ? 106 HIS A N   1 
ATOM   849  C  CA  . HIS A 1 111 ? 38.509 25.476  2.330   1.00 20.59  ? 106 HIS A CA  1 
ATOM   850  C  C   . HIS A 1 111 ? 37.122 26.031  2.006   1.00 17.89  ? 106 HIS A C   1 
ATOM   851  O  O   . HIS A 1 111 ? 36.974 27.219  1.774   1.00 18.86  ? 106 HIS A O   1 
ATOM   852  C  CB  . HIS A 1 111 ? 39.616 26.402  1.766   1.00 20.61  ? 106 HIS A CB  1 
ATOM   853  C  CG  . HIS A 1 111 ? 40.994 25.945  2.146   1.00 23.13  ? 106 HIS A CG  1 
ATOM   854  N  ND1 . HIS A 1 111 ? 41.541 26.247  3.392   1.00 24.53  ? 106 HIS A ND1 1 
ATOM   855  C  CD2 . HIS A 1 111 ? 41.891 25.218  1.453   1.00 24.76  ? 106 HIS A CD2 1 
ATOM   856  C  CE1 . HIS A 1 111 ? 42.748 25.694  3.418   1.00 24.89  ? 106 HIS A CE1 1 
ATOM   857  N  NE2 . HIS A 1 111 ? 43.006 25.050  2.282   1.00 24.32  ? 106 HIS A NE2 1 
ATOM   858  N  N   . LEU A 1 112 ? 36.087 25.166  1.995   1.00 16.01  ? 107 LEU A N   1 
ATOM   859  C  CA  . LEU A 1 112 ? 34.782 25.592  1.536   1.00 14.98  ? 107 LEU A CA  1 
ATOM   860  C  C   . LEU A 1 112 ? 34.218 26.782  2.313   1.00 15.01  ? 107 LEU A C   1 
ATOM   861  O  O   . LEU A 1 112 ? 33.723 27.728  1.702   1.00 17.14  ? 107 LEU A O   1 
ATOM   862  C  CB  . LEU A 1 112 ? 33.809 24.435  1.592   1.00 14.83  ? 107 LEU A CB  1 
ATOM   863  C  CG  . LEU A 1 112 ? 34.051 23.339  0.568   1.00 16.48  ? 107 LEU A CG  1 
ATOM   864  C  CD1 . LEU A 1 112 ? 33.184 22.148  0.852   1.00 15.11  ? 107 LEU A CD1 1 
ATOM   865  C  CD2 . LEU A 1 112 ? 33.793 23.798  -0.863  1.00 17.51  ? 107 LEU A CD2 1 
ATOM   866  N  N   . ILE A 1 113 ? 34.234 26.695  3.644   1.00 15.84  ? 108 ILE A N   1 
ATOM   867  C  CA  . ILE A 1 113 ? 33.598 27.706  4.462   1.00 15.99  ? 108 ILE A CA  1 
ATOM   868  C  C   . ILE A 1 113 ? 34.301 29.054  4.278   1.00 16.99  ? 108 ILE A C   1 
ATOM   869  O  O   . ILE A 1 113 ? 33.660 30.081  4.075   1.00 16.46  ? 108 ILE A O   1 
ATOM   870  C  CB  . ILE A 1 113 ? 33.520 27.280  5.930   1.00 16.27  ? 108 ILE A CB  1 
ATOM   871  C  CG1 . ILE A 1 113 ? 32.410 26.249  6.115   1.00 16.27  ? 108 ILE A CG1 1 
ATOM   872  C  CG2 . ILE A 1 113 ? 33.250 28.483  6.833   1.00 16.79  ? 108 ILE A CG2 1 
ATOM   873  C  CD1 . ILE A 1 113 ? 32.423 25.551  7.454   1.00 16.92  ? 108 ILE A CD1 1 
ATOM   874  N  N   . LYS A 1 114 ? 35.633 29.065  4.351   1.00 16.65  ? 109 LYS A N   1 
ATOM   875  C  CA  . LYS A 1 114 ? 36.297 30.354  4.319   1.00 18.50  ? 109 LYS A CA  1 
ATOM   876  C  C   . LYS A 1 114 ? 36.114 31.066  2.988   1.00 19.37  ? 109 LYS A C   1 
ATOM   877  O  O   . LYS A 1 114 ? 36.167 32.303  2.963   1.00 21.47  ? 109 LYS A O   1 
ATOM   878  C  CB  . LYS A 1 114 ? 37.774 30.236  4.663   1.00 21.09  ? 109 LYS A CB  1 
ATOM   879  C  CG  . LYS A 1 114 ? 38.598 29.539  3.653   1.00 25.83  ? 109 LYS A CG  1 
ATOM   880  C  CD  . LYS A 1 114 ? 40.130 29.594  4.040   1.00 26.43  ? 109 LYS A CD  1 
ATOM   881  C  CE  . LYS A 1 114 ? 40.453 29.057  5.412   1.00 28.74  ? 109 LYS A CE  1 
ATOM   882  N  NZ  . LYS A 1 114 ? 40.072 27.604  5.541   1.00 28.82  ? 109 LYS A NZ  1 
ATOM   883  N  N   . GLU A 1 115 ? 35.921 30.314  1.886   1.00 16.00  ? 110 GLU A N   1 
ATOM   884  C  CA  . GLU A 1 115 ? 35.726 30.964  0.605   1.00 19.75  ? 110 GLU A CA  1 
ATOM   885  C  C   . GLU A 1 115 ? 34.270 31.329  0.326   1.00 20.52  ? 110 GLU A C   1 
ATOM   886  O  O   . GLU A 1 115 ? 34.017 32.020  -0.665  1.00 21.56  ? 110 GLU A O   1 
ATOM   887  C  CB  . GLU A 1 115 ? 36.337 30.124  -0.552  1.00 22.94  ? 110 GLU A CB  1 
ATOM   888  C  CG  . GLU A 1 115 ? 37.878 30.108  -0.505  1.00 24.30  ? 110 GLU A CG  1 
ATOM   889  C  CD  . GLU A 1 115 ? 38.533 31.490  -0.636  1.00 34.79  ? 110 GLU A CD  1 
ATOM   890  O  OE1 . GLU A 1 115 ? 37.873 32.503  -1.013  1.00 36.97  ? 110 GLU A OE1 1 
ATOM   891  O  OE2 . GLU A 1 115 ? 39.744 31.565  -0.318  1.00 43.36  ? 110 GLU A OE2 1 
ATOM   892  N  N   . ALA A 1 116 ? 33.337 30.869  1.183   1.00 18.65  ? 111 ALA A N   1 
ATOM   893  C  CA  . ALA A 1 116 ? 31.917 31.090  0.948   1.00 19.97  ? 111 ALA A CA  1 
ATOM   894  C  C   . ALA A 1 116 ? 31.510 32.467  1.471   1.00 23.84  ? 111 ALA A C   1 
ATOM   895  O  O   . ALA A 1 116 ? 31.461 32.684  2.674   1.00 27.39  ? 111 ALA A O   1 
ATOM   896  C  CB  . ALA A 1 116 ? 31.077 30.030  1.660   1.00 20.55  ? 111 ALA A CB  1 
ATOM   897  N  N   . GLY A 1 117 ? 31.155 33.374  0.578   1.00 24.46  ? 112 GLY A N   1 
ATOM   898  C  CA  . GLY A 1 117 ? 30.754 34.701  1.019   1.00 26.36  ? 112 GLY A CA  1 
ATOM   899  C  C   . GLY A 1 117 ? 29.275 35.020  0.857   1.00 27.06  ? 112 GLY A C   1 
ATOM   900  O  O   . GLY A 1 117 ? 28.771 35.917  1.540   1.00 29.83  ? 112 GLY A O   1 
ATOM   901  N  N   . ASP A 1 118 ? 28.586 34.324  -0.057  1.00 21.17  ? 113 ASP A N   1 
ATOM   902  C  CA  . ASP A 1 118 ? 27.175 34.572  -0.218  1.00 21.83  ? 113 ASP A CA  1 
ATOM   903  C  C   . ASP A 1 118 ? 26.445 33.848  0.900   1.00 21.69  ? 113 ASP A C   1 
ATOM   904  O  O   . ASP A 1 118 ? 26.934 32.850  1.427   1.00 20.57  ? 113 ASP A O   1 
ATOM   905  C  CB  . ASP A 1 118 ? 26.650 34.122  -1.570  1.00 20.65  ? 113 ASP A CB  1 
ATOM   906  C  CG  . ASP A 1 118 ? 27.231 34.920  -2.675  1.00 25.53  ? 113 ASP A CG  1 
ATOM   907  O  OD1 . ASP A 1 118 ? 27.969 35.899  -2.375  1.00 26.33  ? 113 ASP A OD1 1 
ATOM   908  O  OD2 . ASP A 1 118 ? 26.980 34.566  -3.862  1.00 25.08  ? 113 ASP A OD2 1 
ATOM   909  N  N   . ALA A 1 119 ? 25.270 34.363  1.248   1.00 20.60  ? 114 ALA A N   1 
ATOM   910  C  CA  . ALA A 1 119 ? 24.492 33.760  2.310   1.00 21.93  ? 114 ALA A CA  1 
ATOM   911  C  C   . ALA A 1 119 ? 24.100 32.311  2.039   1.00 21.40  ? 114 ALA A C   1 
ATOM   912  O  O   . ALA A 1 119 ? 24.249 31.476  2.941   1.00 20.38  ? 114 ALA A O   1 
ATOM   913  C  CB  . ALA A 1 119 ? 23.254 34.612  2.565   1.00 23.50  ? 114 ALA A CB  1 
ATOM   914  N  N   . GLU A 1 120 ? 23.625 31.990  0.814   1.00 19.93  ? 115 GLU A N   1 
ATOM   915  C  CA  . GLU A 1 120 ? 23.220 30.620  0.512   1.00 22.69  ? 115 GLU A CA  1 
ATOM   916  C  C   . GLU A 1 120 ? 24.364 29.612  0.674   1.00 19.88  ? 115 GLU A C   1 
ATOM   917  O  O   . GLU A 1 120 ? 24.188 28.532  1.239   1.00 20.65  ? 115 GLU A O   1 
ATOM   918  C  CB  . GLU A 1 120 ? 22.617 30.447  -0.895  1.00 28.37  ? 115 GLU A CB  1 
ATOM   919  C  CG  . GLU A 1 120 ? 21.199 31.031  -0.998  1.00 36.92  ? 115 GLU A CG  1 
ATOM   920  C  CD  . GLU A 1 120 ? 20.201 30.222  -1.816  1.00 46.01  ? 115 GLU A CD  1 
ATOM   921  O  OE1 . GLU A 1 120 ? 20.601 29.692  -2.880  1.00 45.24  ? 115 GLU A OE1 1 
ATOM   922  O  OE2 . GLU A 1 120 ? 19.012 30.134  -1.401  1.00 47.90  ? 115 GLU A OE2 1 
ATOM   923  N  N   . SER A 1 121 ? 25.548 29.973  0.202   1.00 17.77  ? 116 SER A N   1 
ATOM   924  C  CA  . SER A 1 121 ? 26.676 29.078  0.342   1.00 16.78  ? 116 SER A CA  1 
ATOM   925  C  C   . SER A 1 121 ? 27.138 28.976  1.795   1.00 17.38  ? 116 SER A C   1 
ATOM   926  O  O   . SER A 1 121 ? 27.386 27.885  2.305   1.00 17.17  ? 116 SER A O   1 
ATOM   927  C  CB  . SER A 1 121 ? 27.811 29.453  -0.589  1.00 18.46  ? 116 SER A CB  1 
ATOM   928  O  OG  . SER A 1 121 ? 28.290 30.752  -0.313  1.00 21.39  ? 116 SER A OG  1 
ATOM   929  N  N   . ARG A 1 122 ? 27.282 30.128  2.466   1.00 16.28  ? 117 ARG A N   1 
ATOM   930  C  CA  . ARG A 1 122 ? 27.846 30.133  3.799   1.00 16.37  ? 117 ARG A CA  1 
ATOM   931  C  C   . ARG A 1 122 ? 26.925 29.441  4.799   1.00 16.93  ? 117 ARG A C   1 
ATOM   932  O  O   . ARG A 1 122 ? 27.375 28.610  5.604   1.00 15.37  ? 117 ARG A O   1 
ATOM   933  C  CB  . ARG A 1 122 ? 28.171 31.515  4.251   1.00 18.57  ? 117 ARG A CB  1 
ATOM   934  C  CG  . ARG A 1 122 ? 29.069 31.506  5.437   1.00 23.28  ? 117 ARG A CG  1 
ATOM   935  C  CD  . ARG A 1 122 ? 29.634 32.902  5.711   1.00 26.66  ? 117 ARG A CD  1 
ATOM   936  N  NE  . ARG A 1 122 ? 30.531 32.814  6.853   1.00 29.22  ? 117 ARG A NE  1 
ATOM   937  C  CZ  . ARG A 1 122 ? 31.765 32.325  6.798   1.00 33.50  ? 117 ARG A CZ  1 
ATOM   938  N  NH1 . ARG A 1 122 ? 32.377 32.101  5.639   1.00 32.40  ? 117 ARG A NH1 1 
ATOM   939  N  NH2 . ARG A 1 122 ? 32.414 32.093  7.935   1.00 35.17  ? 117 ARG A NH2 1 
ATOM   940  N  N   . VAL A 1 123 ? 25.627 29.706  4.680   1.00 13.77  ? 118 VAL A N   1 
ATOM   941  C  CA  . VAL A 1 123 ? 24.670 29.052  5.563   1.00 15.08  ? 118 VAL A CA  1 
ATOM   942  C  C   . VAL A 1 123 ? 24.633 27.548  5.279   1.00 15.06  ? 118 VAL A C   1 
ATOM   943  O  O   . VAL A 1 123 ? 24.594 26.736  6.202   1.00 13.57  ? 118 VAL A O   1 
ATOM   944  C  CB  . VAL A 1 123 ? 23.280 29.673  5.451   1.00 15.50  ? 118 VAL A CB  1 
ATOM   945  C  CG1 . VAL A 1 123 ? 22.262 28.829  6.187   1.00 16.78  ? 118 VAL A CG1 1 
ATOM   946  C  CG2 . VAL A 1 123 ? 23.252 31.099  5.964   1.00 17.07  ? 118 VAL A CG2 1 
ATOM   947  N  N   . PHE A 1 124 ? 24.649 27.147  3.997   1.00 15.04  ? 119 PHE A N   1 
ATOM   948  C  CA  . PHE A 1 124 ? 24.623 25.725  3.680   1.00 13.97  ? 119 PHE A CA  1 
ATOM   949  C  C   . PHE A 1 124 ? 25.828 24.996  4.310   1.00 12.78  ? 119 PHE A C   1 
ATOM   950  O  O   . PHE A 1 124 ? 25.691 23.940  4.940   1.00 13.05  ? 119 PHE A O   1 
ATOM   951  C  CB  . PHE A 1 124 ? 24.600 25.518  2.163   1.00 16.60  ? 119 PHE A CB  1 
ATOM   952  C  CG  . PHE A 1 124 ? 24.837 24.066  1.864   1.00 19.45  ? 119 PHE A CG  1 
ATOM   953  C  CD1 . PHE A 1 124 ? 23.849 23.132  2.089   1.00 23.47  ? 119 PHE A CD1 1 
ATOM   954  C  CD2 . PHE A 1 124 ? 26.089 23.621  1.505   1.00 21.21  ? 119 PHE A CD2 1 
ATOM   955  C  CE1 . PHE A 1 124 ? 24.100 21.772  1.864   1.00 26.91  ? 119 PHE A CE1 1 
ATOM   956  C  CE2 . PHE A 1 124 ? 26.335 22.264  1.275   1.00 23.59  ? 119 PHE A CE2 1 
ATOM   957  C  CZ  . PHE A 1 124 ? 25.330 21.363  1.444   1.00 25.14  ? 119 PHE A CZ  1 
ATOM   958  N  N   . TYR A 1 125 ? 27.014 25.586  4.180   1.00 12.19  ? 120 TYR A N   1 
ATOM   959  C  CA  . TYR A 1 125 ? 28.229 24.927  4.625   1.00 12.82  ? 120 TYR A CA  1 
ATOM   960  C  C   . TYR A 1 125 ? 28.265 24.876  6.144   1.00 13.15  ? 120 TYR A C   1 
ATOM   961  O  O   . TYR A 1 125 ? 28.701 23.869  6.719   1.00 13.39  ? 120 TYR A O   1 
ATOM   962  C  CB  . TYR A 1 125 ? 29.514 25.533  4.109   1.00 13.02  ? 120 TYR A CB  1 
ATOM   963  C  CG  . TYR A 1 125 ? 29.751 25.356  2.615   1.00 12.60  ? 120 TYR A CG  1 
ATOM   964  C  CD1 . TYR A 1 125 ? 29.534 24.130  1.994   1.00 12.48  ? 120 TYR A CD1 1 
ATOM   965  C  CD2 . TYR A 1 125 ? 30.087 26.429  1.822   1.00 12.63  ? 120 TYR A CD2 1 
ATOM   966  C  CE1 . TYR A 1 125 ? 29.765 23.969  0.634   1.00 12.33  ? 120 TYR A CE1 1 
ATOM   967  C  CE2 . TYR A 1 125 ? 30.330 26.280  0.476   1.00 13.39  ? 120 TYR A CE2 1 
ATOM   968  C  CZ  . TYR A 1 125 ? 30.154 25.060  -0.119  1.00 13.65  ? 120 TYR A CZ  1 
ATOM   969  O  OH  . TYR A 1 125 ? 30.310 24.926  -1.496  1.00 16.24  ? 120 TYR A OH  1 
ATOM   970  N  N   . LEU A 1 126 ? 27.831 25.953  6.817   1.00 13.02  ? 121 LEU A N   1 
ATOM   971  C  CA  . LEU A 1 126 ? 27.808 25.932  8.263   1.00 14.69  ? 121 LEU A CA  1 
ATOM   972  C  C   . LEU A 1 126 ? 26.771 24.963  8.831   1.00 13.94  ? 121 LEU A C   1 
ATOM   973  O  O   . LEU A 1 126 ? 27.050 24.307  9.839   1.00 14.74  ? 121 LEU A O   1 
ATOM   974  C  CB  . LEU A 1 126 ? 27.584 27.336  8.790   1.00 15.99  ? 121 LEU A CB  1 
ATOM   975  C  CG  . LEU A 1 126 ? 28.784 28.273  8.675   1.00 15.73  ? 121 LEU A CG  1 
ATOM   976  C  CD1 . LEU A 1 126 ? 28.330 29.731  8.912   1.00 16.19  ? 121 LEU A CD1 1 
ATOM   977  C  CD2 . LEU A 1 126 ? 29.925 27.838  9.639   1.00 17.42  ? 121 LEU A CD2 1 
ATOM   978  N  N   . LYS A 1 127 ? 25.596 24.875  8.189   1.00 12.80  ? 122 LYS A N   1 
ATOM   979  C  CA  . LYS A 1 127 ? 24.649 23.829  8.516   1.00 14.70  ? 122 LYS A CA  1 
ATOM   980  C  C   . LYS A 1 127 ? 25.283 22.438  8.419   1.00 13.68  ? 122 LYS A C   1 
ATOM   981  O  O   . LYS A 1 127 ? 25.074 21.571  9.281   1.00 12.75  ? 122 LYS A O   1 
ATOM   982  C  CB  . LYS A 1 127 ? 23.401 23.935  7.607   1.00 15.10  ? 122 LYS A CB  1 
ATOM   983  C  CG  . LYS A 1 127 ? 22.343 22.862  7.842   1.00 15.03  ? 122 LYS A CG  1 
ATOM   984  C  CD  . LYS A 1 127 ? 21.252 22.866  6.741   1.00 15.84  ? 122 LYS A CD  1 
ATOM   985  C  CE  . LYS A 1 127 ? 20.439 21.624  6.705   1.00 17.97  ? 122 LYS A CE  1 
ATOM   986  N  NZ  . LYS A 1 127 ? 21.294 20.429  6.213   1.00 18.92  ? 122 LYS A NZ  1 
ATOM   987  N  N   . MET A 1 128 ? 26.010 22.205  7.325   1.00 13.92  ? 123 MET A N   1 
ATOM   988  C  CA  . MET A 1 128 ? 26.647 20.921  7.104   1.00 13.95  ? 123 MET A CA  1 
ATOM   989  C  C   . MET A 1 128 ? 27.634 20.623  8.238   1.00 12.18  ? 123 MET A C   1 
ATOM   990  O  O   . MET A 1 128 ? 27.717 19.498  8.726   1.00 11.66  ? 123 MET A O   1 
ATOM   991  C  CB  . MET A 1 128 ? 27.373 20.920  5.735   1.00 14.92  ? 123 MET A CB  1 
ATOM   992  C  CG  . MET A 1 128 ? 27.690 19.562  5.346   1.00 18.38  ? 123 MET A CG  1 
ATOM   993  S  SD  . MET A 1 128 ? 28.361 19.540  3.652   1.00 22.88  ? 123 MET A SD  1 
ATOM   994  C  CE  . MET A 1 128 ? 28.003 17.879  3.282   1.00 21.84  ? 123 MET A CE  1 
ATOM   995  N  N   . LYS A 1 129 ? 28.415 21.641  8.622   1.00 11.77  ? 124 LYS A N   1 
ATOM   996  C  CA  . LYS A 1 129 ? 29.362 21.514  9.713   1.00 11.54  ? 124 LYS A CA  1 
ATOM   997  C  C   . LYS A 1 129 ? 28.648 21.113  11.005  1.00 11.26  ? 124 LYS A C   1 
ATOM   998  O  O   . LYS A 1 129 ? 29.022 20.163  11.685  1.00 11.82  ? 124 LYS A O   1 
ATOM   999  C  CB  . LYS A 1 129 ? 30.165 22.799  9.913   1.00 12.94  ? 124 LYS A CB  1 
ATOM   1000 C  CG  . LYS A 1 129 ? 31.208 22.715  11.009  1.00 13.93  ? 124 LYS A CG  1 
ATOM   1001 C  CD  . LYS A 1 129 ? 32.044 23.950  11.038  1.00 17.48  ? 124 LYS A CD  1 
ATOM   1002 C  CE  . LYS A 1 129 ? 33.170 23.910  12.028  1.00 20.46  ? 124 LYS A CE  1 
ATOM   1003 N  NZ  . LYS A 1 129 ? 34.010 25.123  11.866  1.00 23.32  ? 124 LYS A NZ  1 
ATOM   1004 N  N   . GLY A 1 130 ? 27.541 21.779  11.316  1.00 11.58  ? 125 GLY A N   1 
ATOM   1005 C  CA  . GLY A 1 130 ? 26.721 21.370  12.440  1.00 11.81  ? 125 GLY A CA  1 
ATOM   1006 C  C   . GLY A 1 130 ? 26.208 19.936  12.359  1.00 12.58  ? 125 GLY A C   1 
ATOM   1007 O  O   . GLY A 1 130 ? 26.186 19.215  13.363  1.00 12.76  ? 125 GLY A O   1 
ATOM   1008 N  N   . ASP A 1 131 ? 25.737 19.538  11.180  1.00 11.28  ? 126 ASP A N   1 
ATOM   1009 C  CA  . ASP A 1 131 ? 25.181 18.217  10.988  1.00 11.41  ? 126 ASP A CA  1 
ATOM   1010 C  C   . ASP A 1 131 ? 26.227 17.133  11.230  1.00 11.66  ? 126 ASP A C   1 
ATOM   1011 O  O   . ASP A 1 131 ? 25.939 16.160  11.931  1.00 12.18  ? 126 ASP A O   1 
ATOM   1012 C  CB  . ASP A 1 131 ? 24.624 18.084  9.613   1.00 11.80  ? 126 ASP A CB  1 
ATOM   1013 C  CG  . ASP A 1 131 ? 23.312 18.828  9.296   1.00 13.27  ? 126 ASP A CG  1 
ATOM   1014 O  OD1 . ASP A 1 131 ? 22.579 19.207  10.267  1.00 14.20  ? 126 ASP A OD1 1 
ATOM   1015 O  OD2 . ASP A 1 131 ? 23.009 18.995  8.065   1.00 13.02  ? 126 ASP A OD2 1 
ATOM   1016 N  N   . TYR A 1 132 ? 27.435 17.324  10.698  1.00 12.67  ? 127 TYR A N   1 
ATOM   1017 C  CA  . TYR A 1 132 ? 28.452 16.282  10.824  1.00 11.82  ? 127 TYR A CA  1 
ATOM   1018 C  C   . TYR A 1 132 ? 29.058 16.253  12.230  1.00 12.95  ? 127 TYR A C   1 
ATOM   1019 O  O   . TYR A 1 132 ? 29.385 15.165  12.693  1.00 13.53  ? 127 TYR A O   1 
ATOM   1020 C  CB  . TYR A 1 132 ? 29.501 16.263  9.627   1.00 12.50  ? 127 TYR A CB  1 
ATOM   1021 C  CG  . TYR A 1 132 ? 28.822 15.699  8.374   1.00 12.17  ? 127 TYR A CG  1 
ATOM   1022 C  CD1 . TYR A 1 132 ? 27.972 16.478  7.607   1.00 12.48  ? 127 TYR A CD1 1 
ATOM   1023 C  CD2 . TYR A 1 132 ? 28.901 14.358  8.058   1.00 12.61  ? 127 TYR A CD2 1 
ATOM   1024 C  CE1 . TYR A 1 132 ? 27.252 15.947  6.543   1.00 13.44  ? 127 TYR A CE1 1 
ATOM   1025 C  CE2 . TYR A 1 132 ? 28.208 13.827  6.980   1.00 12.68  ? 127 TYR A CE2 1 
ATOM   1026 C  CZ  . TYR A 1 132 ? 27.383 14.615  6.219   1.00 14.01  ? 127 TYR A CZ  1 
ATOM   1027 O  OH  . TYR A 1 132 ? 26.652 14.055  5.145   1.00 15.32  ? 127 TYR A OH  1 
ATOM   1028 N  N   . TYR A 1 133 ? 29.148 17.389  12.944  1.00 12.18  ? 128 TYR A N   1 
ATOM   1029 C  CA  . TYR A 1 133 ? 29.426 17.315  14.371  1.00 11.86  ? 128 TYR A CA  1 
ATOM   1030 C  C   . TYR A 1 133 ? 28.292 16.638  15.145  1.00 12.26  ? 128 TYR A C   1 
ATOM   1031 O  O   . TYR A 1 133 ? 28.540 15.905  16.087  1.00 13.64  ? 128 TYR A O   1 
ATOM   1032 C  CB  . TYR A 1 133 ? 29.748 18.708  14.970  1.00 12.09  ? 128 TYR A CB  1 
ATOM   1033 C  CG  . TYR A 1 133 ? 31.176 19.122  14.775  1.00 13.38  ? 128 TYR A CG  1 
ATOM   1034 C  CD1 . TYR A 1 133 ? 32.208 18.457  15.431  1.00 14.34  ? 128 TYR A CD1 1 
ATOM   1035 C  CD2 . TYR A 1 133 ? 31.507 20.186  13.963  1.00 15.11  ? 128 TYR A CD2 1 
ATOM   1036 C  CE1 . TYR A 1 133 ? 33.533 18.840  15.265  1.00 15.72  ? 128 TYR A CE1 1 
ATOM   1037 C  CE2 . TYR A 1 133 ? 32.833 20.588  13.816  1.00 16.30  ? 128 TYR A CE2 1 
ATOM   1038 C  CZ  . TYR A 1 133 ? 33.837 19.883  14.452  1.00 16.23  ? 128 TYR A CZ  1 
ATOM   1039 O  OH  . TYR A 1 133 ? 35.183 20.205  14.321  1.00 20.10  ? 128 TYR A OH  1 
ATOM   1040 N  N   . ARG A 1 134 ? 27.042 16.875  14.737  1.00 11.73  ? 129 ARG A N   1 
ATOM   1041 C  CA  . ARG A 1 134 ? 25.922 16.193  15.357  1.00 11.87  ? 129 ARG A CA  1 
ATOM   1042 C  C   . ARG A 1 134 ? 26.015 14.660  15.222  1.00 12.69  ? 129 ARG A C   1 
ATOM   1043 O  O   . ARG A 1 134 ? 25.761 13.898  16.155  1.00 12.72  ? 129 ARG A O   1 
ATOM   1044 C  CB  . ARG A 1 134 ? 24.628 16.768  14.826  1.00 11.92  ? 129 ARG A CB  1 
ATOM   1045 C  CG  . ARG A 1 134 ? 23.371 15.991  15.277  1.00 12.73  ? 129 ARG A CG  1 
ATOM   1046 C  CD  . ARG A 1 134 ? 22.090 16.763  15.176  1.00 12.84  ? 129 ARG A CD  1 
ATOM   1047 N  NE  . ARG A 1 134 ? 21.750 17.154  13.817  1.00 12.45  ? 129 ARG A NE  1 
ATOM   1048 C  CZ  . ARG A 1 134 ? 21.137 16.401  12.917  1.00 13.84  ? 129 ARG A CZ  1 
ATOM   1049 N  NH1 . ARG A 1 134 ? 20.617 15.230  13.232  1.00 13.52  ? 129 ARG A NH1 1 
ATOM   1050 N  NH2 . ARG A 1 134 ? 21.031 16.838  11.663  1.00 14.17  ? 129 ARG A NH2 1 
ATOM   1051 N  N   . TYR A 1 135 ? 26.401 14.205  14.039  1.00 11.78  ? 130 TYR A N   1 
ATOM   1052 C  CA  . TYR A 1 135 ? 26.566 12.773  13.821  1.00 13.21  ? 130 TYR A CA  1 
ATOM   1053 C  C   . TYR A 1 135 ? 27.694 12.234  14.698  1.00 12.15  ? 130 TYR A C   1 
ATOM   1054 O  O   . TYR A 1 135 ? 27.579 11.120  15.225  1.00 13.46  ? 130 TYR A O   1 
ATOM   1055 C  CB  . TYR A 1 135 ? 26.734 12.429  12.313  1.00 13.25  ? 130 TYR A CB  1 
ATOM   1056 C  CG  . TYR A 1 135 ? 25.651 13.023  11.418  1.00 13.25  ? 130 TYR A CG  1 
ATOM   1057 C  CD1 . TYR A 1 135 ? 24.333 13.148  11.861  1.00 13.89  ? 130 TYR A CD1 1 
ATOM   1058 C  CD2 . TYR A 1 135 ? 25.936 13.413  10.136  1.00 13.19  ? 130 TYR A CD2 1 
ATOM   1059 C  CE1 . TYR A 1 135 ? 23.346 13.675  11.037  1.00 14.81  ? 130 TYR A CE1 1 
ATOM   1060 C  CE2 . TYR A 1 135 ? 24.953 13.903  9.293   1.00 14.20  ? 130 TYR A CE2 1 
ATOM   1061 C  CZ  . TYR A 1 135 ? 23.667 14.087  9.757   1.00 14.53  ? 130 TYR A CZ  1 
ATOM   1062 O  OH  . TYR A 1 135 ? 22.706 14.641  8.901   1.00 15.29  ? 130 TYR A OH  1 
ATOM   1063 N  N   . LEU A 1 136 ? 28.780 12.977  14.833  1.00 12.51  ? 131 LEU A N   1 
ATOM   1064 C  CA  . LEU A 1 136 ? 29.847 12.587  15.745  1.00 13.57  ? 131 LEU A CA  1 
ATOM   1065 C  C   . LEU A 1 136 ? 29.328 12.535  17.175  1.00 13.32  ? 131 LEU A C   1 
ATOM   1066 O  O   . LEU A 1 136 ? 29.701 11.637  17.940  1.00 14.36  ? 131 LEU A O   1 
ATOM   1067 C  CB  . LEU A 1 136 ? 31.107 13.513  15.695  1.00 13.15  ? 131 LEU A CB  1 
ATOM   1068 C  CG  . LEU A 1 136 ? 31.906 13.460  14.409  1.00 14.35  ? 131 LEU A CG  1 
ATOM   1069 C  CD1 . LEU A 1 136 ? 32.968 14.527  14.375  1.00 16.14  ? 131 LEU A CD1 1 
ATOM   1070 C  CD2 . LEU A 1 136 ? 32.550 12.091  14.237  1.00 14.36  ? 131 LEU A CD2 1 
ATOM   1071 N  N   . ALA A 1 137 ? 28.454 13.466  17.540  1.00 14.49  ? 132 ALA A N   1 
ATOM   1072 C  CA  . ALA A 1 137 ? 27.897 13.498  18.892  1.00 13.99  ? 132 ALA A CA  1 
ATOM   1073 C  C   . ALA A 1 137 ? 27.029 12.290  19.210  1.00 15.25  ? 132 ALA A C   1 
ATOM   1074 O  O   . ALA A 1 137 ? 26.994 11.861  20.368  1.00 15.83  ? 132 ALA A O   1 
ATOM   1075 C  CB  . ALA A 1 137 ? 27.081 14.789  19.128  1.00 14.07  ? 132 ALA A CB  1 
ATOM   1076 N  N   . GLU A 1 138 ? 26.320 11.776  18.195  1.00 15.41  ? 133 GLU A N   1 
ATOM   1077 C  CA  . GLU A 1 138 ? 25.443 10.637  18.371  1.00 16.52  ? 133 GLU A CA  1 
ATOM   1078 C  C   . GLU A 1 138 ? 26.199 9.410   18.908  1.00 15.36  ? 133 GLU A C   1 
ATOM   1079 O  O   . GLU A 1 138 ? 25.605 8.556   19.570  1.00 16.06  ? 133 GLU A O   1 
ATOM   1080 C  CB  . GLU A 1 138 ? 24.712 10.299  17.068  1.00 16.46  ? 133 GLU A CB  1 
ATOM   1081 C  CG  . GLU A 1 138 ? 23.645 11.285  16.597  1.00 17.61  ? 133 GLU A CG  1 
ATOM   1082 C  CD  . GLU A 1 138 ? 23.000 10.943  15.242  1.00 20.21  ? 133 GLU A CD  1 
ATOM   1083 O  OE1 . GLU A 1 138 ? 23.563 10.182  14.423  1.00 19.57  ? 133 GLU A OE1 1 
ATOM   1084 O  OE2 . GLU A 1 138 ? 21.859 11.386  15.054  1.00 20.86  ? 133 GLU A OE2 1 
ATOM   1085 N  N   . VAL A 1 139 ? 27.483 9.292   18.575  1.00 15.48  ? 134 VAL A N   1 
ATOM   1086 C  CA  . VAL A 1 139 ? 28.269 8.123   18.963  1.00 16.79  ? 134 VAL A CA  1 
ATOM   1087 C  C   . VAL A 1 139 ? 29.327 8.441   20.025  1.00 18.67  ? 134 VAL A C   1 
ATOM   1088 O  O   . VAL A 1 139 ? 30.068 7.561   20.479  1.00 19.92  ? 134 VAL A O   1 
ATOM   1089 C  CB  . VAL A 1 139 ? 28.925 7.451   17.754  1.00 17.38  ? 134 VAL A CB  1 
ATOM   1090 C  CG1 . VAL A 1 139 ? 27.866 7.108   16.732  1.00 16.94  ? 134 VAL A CG1 1 
ATOM   1091 C  CG2 . VAL A 1 139 ? 30.052 8.271   17.142  1.00 17.53  ? 134 VAL A CG2 1 
ATOM   1092 N  N   . ALA A 1 140 ? 29.417 9.699   20.430  1.00 17.99  ? 135 ALA A N   1 
ATOM   1093 C  CA  . ALA A 1 140 ? 30.424 10.113  21.391  1.00 20.02  ? 135 ALA A CA  1 
ATOM   1094 C  C   . ALA A 1 140 ? 29.996 9.725   22.804  1.00 24.19  ? 135 ALA A C   1 
ATOM   1095 O  O   . ALA A 1 140 ? 28.821 9.761   23.152  1.00 23.77  ? 135 ALA A O   1 
ATOM   1096 C  CB  . ALA A 1 140 ? 30.651 11.596  21.271  1.00 19.75  ? 135 ALA A CB  1 
ATOM   1097 N  N   . THR A 1 141 ? 30.975 9.301   23.590  1.00 29.27  ? 136 THR A N   1 
ATOM   1098 C  CA  . THR A 1 141 ? 30.706 8.757   24.909  1.00 40.36  ? 136 THR A CA  1 
ATOM   1099 C  C   . THR A 1 141 ? 31.962 8.951   25.724  1.00 47.04  ? 136 THR A C   1 
ATOM   1100 O  O   . THR A 1 141 ? 32.507 7.982   26.221  1.00 51.87  ? 136 THR A O   1 
ATOM   1101 C  CB  . THR A 1 141 ? 30.519 7.228   24.962  1.00 39.94  ? 136 THR A CB  1 
ATOM   1102 O  OG1 . THR A 1 141 ? 31.767 6.624   24.592  1.00 42.81  ? 136 THR A OG1 1 
ATOM   1103 C  CG2 . THR A 1 141 ? 29.438 6.739   24.091  1.00 42.23  ? 136 THR A CG2 1 
ATOM   1104 N  N   . GLY A 1 142 ? 32.475 10.172  25.768  1.00 52.89  ? 137 GLY A N   1 
ATOM   1105 C  CA  . GLY A 1 142 ? 33.770 10.361  26.391  1.00 58.12  ? 137 GLY A CA  1 
ATOM   1106 C  C   . GLY A 1 142 ? 33.930 11.782  26.909  1.00 59.41  ? 137 GLY A C   1 
ATOM   1107 O  O   . GLY A 1 142 ? 32.943 12.498  27.094  1.00 55.24  ? 137 GLY A O   1 
ATOM   1108 N  N   . ASP A 1 143 ? 35.190 12.152  27.162  1.00 57.50  ? 138 ASP A N   1 
ATOM   1109 C  CA  . ASP A 1 143 ? 35.525 13.535  27.460  1.00 65.97  ? 138 ASP A CA  1 
ATOM   1110 C  C   . ASP A 1 143 ? 34.914 14.400  26.363  1.00 56.75  ? 138 ASP A C   1 
ATOM   1111 O  O   . ASP A 1 143 ? 34.037 15.237  26.601  1.00 61.95  ? 138 ASP A O   1 
ATOM   1112 C  CB  . ASP A 1 143 ? 37.061 13.743  27.527  1.00 69.69  ? 138 ASP A CB  1 
ATOM   1113 C  CG  . ASP A 1 143 ? 37.748 13.096  28.716  1.00 71.93  ? 138 ASP A CG  1 
ATOM   1114 O  OD1 . ASP A 1 143 ? 37.040 12.500  29.560  1.00 75.36  ? 138 ASP A OD1 1 
ATOM   1115 O  OD2 . ASP A 1 143 ? 38.995 13.184  28.803  1.00 78.27  ? 138 ASP A OD2 1 
ATOM   1116 N  N   . ASP A 1 144 ? 35.327 14.112  25.132  1.00 45.72  ? 139 ASP A N   1 
ATOM   1117 C  CA  . ASP A 1 144 ? 35.006 14.995  24.032  1.00 46.41  ? 139 ASP A CA  1 
ATOM   1118 C  C   . ASP A 1 144 ? 33.530 15.044  23.643  1.00 34.49  ? 139 ASP A C   1 
ATOM   1119 O  O   . ASP A 1 144 ? 33.213 15.817  22.770  1.00 30.63  ? 139 ASP A O   1 
ATOM   1120 C  CB  . ASP A 1 144 ? 35.896 14.680  22.785  1.00 54.45  ? 139 ASP A CB  1 
ATOM   1121 C  CG  . ASP A 1 144 ? 37.252 15.392  22.787  1.00 59.43  ? 139 ASP A CG  1 
ATOM   1122 O  OD1 . ASP A 1 144 ? 37.475 16.268  23.675  1.00 60.64  ? 139 ASP A OD1 1 
ATOM   1123 O  OD2 . ASP A 1 144 ? 38.090 15.077  21.906  1.00 63.58  ? 139 ASP A OD2 1 
ATOM   1124 N  N   . LYS A 1 145 ? 32.616 14.303  24.286  1.00 31.21  ? 140 LYS A N   1 
ATOM   1125 C  CA  . LYS A 1 145 ? 31.217 14.417  23.913  1.00 31.86  ? 140 LYS A CA  1 
ATOM   1126 C  C   . LYS A 1 145 ? 30.758 15.874  24.064  1.00 29.58  ? 140 LYS A C   1 
ATOM   1127 O  O   . LYS A 1 145 ? 30.114 16.448  23.173  1.00 25.20  ? 140 LYS A O   1 
ATOM   1128 C  CB  . LYS A 1 145 ? 30.310 13.504  24.724  1.00 33.66  ? 140 LYS A CB  1 
ATOM   1129 C  CG  . LYS A 1 145 ? 28.928 13.462  24.141  1.00 38.77  ? 140 LYS A CG  1 
ATOM   1130 C  CD  . LYS A 1 145 ? 27.916 12.631  24.915  1.00 45.11  ? 140 LYS A CD  1 
ATOM   1131 C  CE  . LYS A 1 145 ? 26.633 12.570  24.133  1.00 44.30  ? 140 LYS A CE  1 
ATOM   1132 N  NZ  . LYS A 1 145 ? 25.486 12.202  24.979  1.00 45.85  ? 140 LYS A NZ  1 
ATOM   1133 N  N   . LYS A 1 146 ? 31.147 16.486  25.188  1.00 25.31  ? 141 LYS A N   1 
ATOM   1134 C  CA  . LYS A 1 146 ? 30.751 17.860  25.456  1.00 26.51  ? 141 LYS A CA  1 
ATOM   1135 C  C   . LYS A 1 146 ? 31.276 18.809  24.393  1.00 22.79  ? 141 LYS A C   1 
ATOM   1136 O  O   . LYS A 1 146 ? 30.537 19.689  23.963  1.00 22.75  ? 141 LYS A O   1 
ATOM   1137 C  CB  . LYS A 1 146 ? 31.207 18.370  26.858  1.00 28.43  ? 141 LYS A CB  1 
ATOM   1138 C  CG  . LYS A 1 146 ? 30.246 18.132  28.013  1.00 33.78  ? 141 LYS A CG  1 
ATOM   1139 C  CD  . LYS A 1 146 ? 30.948 18.706  29.435  1.00 40.51  ? 141 LYS A CD  1 
ATOM   1140 C  CE  . LYS A 1 146 ? 30.079 19.143  30.648  1.00 45.70  ? 141 LYS A CE  1 
ATOM   1141 N  NZ  . LYS A 1 146 ? 30.794 20.168  31.559  1.00 41.23  ? 141 LYS A NZ  1 
ATOM   1142 N  N   . ARG A 1 147 ? 32.570 18.699  24.064  1.00 22.80  ? 142 ARG A N   1 
ATOM   1143 C  CA  . ARG A 1 147 ? 33.208 19.567  23.095  1.00 24.47  ? 142 ARG A CA  1 
ATOM   1144 C  C   . ARG A 1 147 ? 32.643 19.353  21.689  1.00 17.90  ? 142 ARG A C   1 
ATOM   1145 O  O   . ARG A 1 147 ? 32.513 20.320  20.953  1.00 18.02  ? 142 ARG A O   1 
ATOM   1146 C  CB  . ARG A 1 147 ? 34.755 19.410  23.062  1.00 29.45  ? 142 ARG A CB  1 
ATOM   1147 C  CG  . ARG A 1 147 ? 35.453 20.439  24.007  1.00 36.53  ? 142 ARG A CG  1 
ATOM   1148 C  CD  . ARG A 1 147 ? 36.966 20.288  24.032  1.00 40.36  ? 142 ARG A CD  1 
ATOM   1149 N  NE  . ARG A 1 147 ? 37.397 19.273  24.986  1.00 42.07  ? 142 ARG A NE  1 
ATOM   1150 C  CZ  . ARG A 1 147 ? 37.718 19.523  26.250  1.00 41.91  ? 142 ARG A CZ  1 
ATOM   1151 N  NH1 . ARG A 1 147 ? 37.682 20.755  26.745  1.00 37.18  ? 142 ARG A NH1 1 
ATOM   1152 N  NH2 . ARG A 1 147 ? 38.042 18.507  27.047  1.00 45.76  ? 142 ARG A NH2 1 
ATOM   1153 N  N   . ILE A 1 148 ? 32.257 18.112  21.351  1.00 18.33  ? 143 ILE A N   1 
ATOM   1154 C  CA  . ILE A 1 148 ? 31.653 17.872  20.054  1.00 16.21  ? 143 ILE A CA  1 
ATOM   1155 C  C   . ILE A 1 148 ? 30.297 18.576  19.950  1.00 16.38  ? 143 ILE A C   1 
ATOM   1156 O  O   . ILE A 1 148 ? 29.960 19.191  18.931  1.00 16.51  ? 143 ILE A O   1 
ATOM   1157 C  CB  . ILE A 1 148 ? 31.592 16.367  19.779  1.00 18.92  ? 143 ILE A CB  1 
ATOM   1158 C  CG1 . ILE A 1 148 ? 33.014 15.789  19.624  1.00 22.27  ? 143 ILE A CG1 1 
ATOM   1159 C  CG2 . ILE A 1 148 ? 30.674 16.091  18.577  1.00 18.79  ? 143 ILE A CG2 1 
ATOM   1160 C  CD1 . ILE A 1 148 ? 33.092 14.224  19.732  1.00 26.64  ? 143 ILE A CD1 1 
ATOM   1161 N  N   . ILE A 1 149 ? 29.489 18.419  21.000  1.00 16.66  ? 144 ILE A N   1 
ATOM   1162 C  CA  . ILE A 1 149 ? 28.204 19.077  21.101  1.00 16.82  ? 144 ILE A CA  1 
ATOM   1163 C  C   . ILE A 1 149 ? 28.362 20.576  20.965  1.00 17.06  ? 144 ILE A C   1 
ATOM   1164 O  O   . ILE A 1 149 ? 27.603 21.212  20.217  1.00 17.46  ? 144 ILE A O   1 
ATOM   1165 C  CB  . ILE A 1 149 ? 27.472 18.671  22.374  1.00 17.60  ? 144 ILE A CB  1 
ATOM   1166 C  CG1 . ILE A 1 149 ? 27.020 17.202  22.255  1.00 20.22  ? 144 ILE A CG1 1 
ATOM   1167 C  CG2 . ILE A 1 149 ? 26.315 19.647  22.703  1.00 17.82  ? 144 ILE A CG2 1 
ATOM   1168 C  CD1 . ILE A 1 149 ? 26.398 16.584  23.520  1.00 22.82  ? 144 ILE A CD1 1 
ATOM   1169 N  N   . ASP A 1 150 ? 29.362 21.153  21.654  1.00 16.33  ? 145 ASP A N   1 
ATOM   1170 C  CA  . ASP A 1 150 ? 29.558 22.584  21.542  1.00 18.22  ? 145 ASP A CA  1 
ATOM   1171 C  C   . ASP A 1 150 ? 29.980 23.018  20.130  1.00 16.46  ? 145 ASP A C   1 
ATOM   1172 O  O   . ASP A 1 150 ? 29.606 24.097  19.666  1.00 16.71  ? 145 ASP A O   1 
ATOM   1173 C  CB  . ASP A 1 150 ? 30.524 23.161  22.571  1.00 22.55  ? 145 ASP A CB  1 
ATOM   1174 C  CG  . ASP A 1 150 ? 30.106 24.655  22.851  1.00 32.90  ? 145 ASP A CG  1 
ATOM   1175 O  OD1 . ASP A 1 150 ? 28.913 24.897  23.270  1.00 41.18  ? 145 ASP A OD1 1 
ATOM   1176 O  OD2 . ASP A 1 150 ? 30.917 25.568  22.581  1.00 38.90  ? 145 ASP A OD2 1 
ATOM   1177 N  N   . SER A 1 151 ? 30.801 22.206  19.466  1.00 15.55  ? 146 SER A N   1 
ATOM   1178 C  CA  . SER A 1 151 ? 31.148 22.465  18.083  1.00 15.22  ? 146 SER A CA  1 
ATOM   1179 C  C   . SER A 1 151 ? 29.922 22.476  17.164  1.00 13.64  ? 146 SER A C   1 
ATOM   1180 O  O   . SER A 1 151 ? 29.794 23.345  16.311  1.00 16.00  ? 146 SER A O   1 
ATOM   1181 C  CB  . SER A 1 151 ? 32.165 21.452  17.633  1.00 16.81  ? 146 SER A CB  1 
ATOM   1182 O  OG  . SER A 1 151 ? 33.432 21.702  18.236  1.00 20.01  ? 146 SER A OG  1 
ATOM   1183 N  N   . ALA A 1 152 ? 29.064 21.484  17.314  1.00 13.51  ? 147 ALA A N   1 
ATOM   1184 C  CA  . ALA A 1 152 ? 27.842 21.460  16.526  1.00 14.02  ? 147 ALA A CA  1 
ATOM   1185 C  C   . ALA A 1 152 ? 27.024 22.724  16.800  1.00 14.73  ? 147 ALA A C   1 
ATOM   1186 O  O   . ALA A 1 152 ? 26.575 23.411  15.889  1.00 14.10  ? 147 ALA A O   1 
ATOM   1187 C  CB  . ALA A 1 152 ? 27.056 20.221  16.851  1.00 13.42  ? 147 ALA A CB  1 
ATOM   1188 N  N   . ARG A 1 153 ? 26.818 23.040  18.083  1.00 14.54  ? 148 ARG A N   1 
ATOM   1189 C  CA  A ARG A 1 153 ? 25.985 24.185  18.436  0.50 14.74  ? 148 ARG A CA  1 
ATOM   1190 C  CA  B ARG A 1 153 ? 26.033 24.194  18.489  0.50 15.87  ? 148 ARG A CA  1 
ATOM   1191 C  C   . ARG A 1 153 ? 26.555 25.479  17.845  1.00 15.49  ? 148 ARG A C   1 
ATOM   1192 O  O   . ARG A 1 153 ? 25.821 26.311  17.331  1.00 15.18  ? 148 ARG A O   1 
ATOM   1193 C  CB  A ARG A 1 153 ? 25.839 24.344  19.986  0.50 14.72  ? 148 ARG A CB  1 
ATOM   1194 C  CB  B ARG A 1 153 ? 26.140 24.317  20.033  0.50 17.15  ? 148 ARG A CB  1 
ATOM   1195 C  CG  A ARG A 1 153 ? 24.784 25.404  20.408  0.50 14.86  ? 148 ARG A CG  1 
ATOM   1196 C  CG  B ARG A 1 153 ? 25.472 25.545  20.593  0.50 19.65  ? 148 ARG A CG  1 
ATOM   1197 C  CD  A ARG A 1 153 ? 24.994 25.789  21.870  0.50 15.28  ? 148 ARG A CD  1 
ATOM   1198 C  CD  B ARG A 1 153 ? 25.934 25.750  22.020  0.50 20.71  ? 148 ARG A CD  1 
ATOM   1199 N  NE  A ARG A 1 153 ? 25.131 24.623  22.719  0.50 15.95  ? 148 ARG A NE  1 
ATOM   1200 N  NE  B ARG A 1 153 ? 26.960 26.771  22.200  0.50 24.47  ? 148 ARG A NE  1 
ATOM   1201 C  CZ  A ARG A 1 153 ? 24.117 23.899  23.143  0.50 15.16  ? 148 ARG A CZ  1 
ATOM   1202 C  CZ  B ARG A 1 153 ? 27.523 27.516  21.252  0.50 24.41  ? 148 ARG A CZ  1 
ATOM   1203 N  NH1 A ARG A 1 153 ? 22.875 24.334  23.034  0.50 15.01  ? 148 ARG A NH1 1 
ATOM   1204 N  NH1 B ARG A 1 153 ? 28.825 27.495  21.055  0.50 24.77  ? 148 ARG A NH1 1 
ATOM   1205 N  NH2 A ARG A 1 153 ? 24.359 22.729  23.729  0.50 15.78  ? 148 ARG A NH2 1 
ATOM   1206 N  NH2 B ARG A 1 153 ? 26.796 28.452  20.643  0.50 25.22  ? 148 ARG A NH2 1 
ATOM   1207 N  N   . SER A 1 154 ? 27.862 25.654  17.934  1.00 15.60  ? 149 SER A N   1 
ATOM   1208 C  CA  . SER A 1 154 ? 28.532 26.833  17.439  1.00 17.40  ? 149 SER A CA  1 
ATOM   1209 C  C   . SER A 1 154 ? 28.339 27.021  15.935  1.00 17.45  ? 149 SER A C   1 
ATOM   1210 O  O   . SER A 1 154 ? 28.035 28.122  15.468  1.00 17.23  ? 149 SER A O   1 
ATOM   1211 C  CB  . SER A 1 154 ? 30.000 26.735  17.820  1.00 21.78  ? 149 SER A CB  1 
ATOM   1212 O  OG  . SER A 1 154 ? 30.655 27.875  17.316  1.00 28.04  ? 149 SER A OG  1 
ATOM   1213 N  N   . ALA A 1 155 ? 28.462 25.922  15.187  1.00 15.05  ? 150 ALA A N   1 
ATOM   1214 C  CA  . ALA A 1 155 ? 28.271 25.974  13.748  1.00 15.28  ? 150 ALA A CA  1 
ATOM   1215 C  C   . ALA A 1 155 ? 26.820 26.336  13.441  1.00 13.49  ? 150 ALA A C   1 
ATOM   1216 O  O   . ALA A 1 155 ? 26.554 27.227  12.614  1.00 14.19  ? 150 ALA A O   1 
ATOM   1217 C  CB  . ALA A 1 155 ? 28.684 24.638  13.072  1.00 15.00  ? 150 ALA A CB  1 
ATOM   1218 N  N   . TYR A 1 156 ? 25.871 25.633  14.060  1.00 12.86  ? 151 TYR A N   1 
ATOM   1219 C  CA  . TYR A 1 156 ? 24.468 25.939  13.822  1.00 13.21  ? 151 TYR A CA  1 
ATOM   1220 C  C   . TYR A 1 156 ? 24.111 27.394  14.168  1.00 14.22  ? 151 TYR A C   1 
ATOM   1221 O  O   . TYR A 1 156 ? 23.342 28.035  13.457  1.00 14.15  ? 151 TYR A O   1 
ATOM   1222 C  CB  . TYR A 1 156 ? 23.573 24.993  14.598  1.00 13.00  ? 151 TYR A CB  1 
ATOM   1223 C  CG  . TYR A 1 156 ? 23.478 23.576  14.090  1.00 13.30  ? 151 TYR A CG  1 
ATOM   1224 C  CD1 . TYR A 1 156 ? 23.178 23.305  12.757  1.00 13.02  ? 151 TYR A CD1 1 
ATOM   1225 C  CD2 . TYR A 1 156 ? 23.574 22.501  14.954  1.00 14.09  ? 151 TYR A CD2 1 
ATOM   1226 C  CE1 . TYR A 1 156 ? 22.941 21.982  12.315  1.00 12.88  ? 151 TYR A CE1 1 
ATOM   1227 C  CE2 . TYR A 1 156 ? 23.357 21.183  14.522  1.00 13.55  ? 151 TYR A CE2 1 
ATOM   1228 C  CZ  . TYR A 1 156 ? 23.033 20.930  13.200  1.00 13.84  ? 151 TYR A CZ  1 
ATOM   1229 O  OH  . TYR A 1 156 ? 22.834 19.612  12.790  1.00 13.43  ? 151 TYR A OH  1 
ATOM   1230 N  N   . GLN A 1 157 ? 24.659 27.895  15.275  1.00 15.45  ? 152 GLN A N   1 
ATOM   1231 C  CA  . GLN A 1 157 ? 24.307 29.232  15.735  1.00 16.23  ? 152 GLN A CA  1 
ATOM   1232 C  C   . GLN A 1 157 ? 24.805 30.271  14.732  1.00 15.62  ? 152 GLN A C   1 
ATOM   1233 O  O   . GLN A 1 157 ? 24.113 31.253  14.455  1.00 16.97  ? 152 GLN A O   1 
ATOM   1234 C  CB  . GLN A 1 157 ? 24.895 29.515  17.148  1.00 18.11  ? 152 GLN A CB  1 
ATOM   1235 C  CG  . GLN A 1 157 ? 24.384 30.853  17.727  1.00 20.63  ? 152 GLN A CG  1 
ATOM   1236 C  CD  . GLN A 1 157 ? 22.900 30.878  17.785  1.00 23.81  ? 152 GLN A CD  1 
ATOM   1237 O  OE1 . GLN A 1 157 ? 22.298 30.040  18.497  1.00 25.50  ? 152 GLN A OE1 1 
ATOM   1238 N  NE2 . GLN A 1 157 ? 22.234 31.832  17.067  1.00 26.25  ? 152 GLN A NE2 1 
ATOM   1239 N  N   . GLU A 1 158 ? 26.039 30.084  14.236  1.00 16.81  ? 153 GLU A N   1 
ATOM   1240 C  CA  . GLU A 1 158 ? 26.614 31.004  13.254  1.00 18.29  ? 153 GLU A CA  1 
ATOM   1241 C  C   . GLU A 1 158 ? 25.755 31.015  11.988  1.00 17.70  ? 153 GLU A C   1 
ATOM   1242 O  O   . GLU A 1 158 ? 25.424 32.085  11.445  1.00 17.48  ? 153 GLU A O   1 
ATOM   1243 C  CB  . GLU A 1 158 ? 28.100 30.664  12.929  1.00 20.62  ? 153 GLU A CB  1 
ATOM   1244 C  CG  . GLU A 1 158 ? 28.719 31.619  11.954  1.00 24.40  ? 153 GLU A CG  1 
ATOM   1245 C  CD  . GLU A 1 158 ? 30.208 31.448  11.656  1.00 32.40  ? 153 GLU A CD  1 
ATOM   1246 O  OE1 . GLU A 1 158 ? 30.922 30.679  12.351  1.00 37.52  ? 153 GLU A OE1 1 
ATOM   1247 O  OE2 . GLU A 1 158 ? 30.646 32.128  10.698  1.00 38.30  ? 153 GLU A OE2 1 
ATOM   1248 N  N   . ALA A 1 159 ? 25.342 29.814  11.556  1.00 14.16  ? 154 ALA A N   1 
ATOM   1249 C  CA  . ALA A 1 159 ? 24.455 29.696  10.407  1.00 13.40  ? 154 ALA A CA  1 
ATOM   1250 C  C   . ALA A 1 159 ? 23.134 30.401  10.657  1.00 14.58  ? 154 ALA A C   1 
ATOM   1251 O  O   . ALA A 1 159 ? 22.600 31.063  9.759   1.00 15.43  ? 154 ALA A O   1 
ATOM   1252 C  CB  . ALA A 1 159 ? 24.205 28.214  10.047  1.00 13.74  ? 154 ALA A CB  1 
ATOM   1253 N  N   . MET A 1 160 ? 22.571 30.201  11.853  1.00 15.71  ? 155 MET A N   1 
ATOM   1254 C  CA  . MET A 1 160 ? 21.263 30.781  12.169  1.00 16.03  ? 155 MET A CA  1 
ATOM   1255 C  C   . MET A 1 160 ? 21.371 32.307  12.097  1.00 16.17  ? 155 MET A C   1 
ATOM   1256 O  O   . MET A 1 160 ? 20.474 32.992  11.566  1.00 15.72  ? 155 MET A O   1 
ATOM   1257 C  CB  . MET A 1 160 ? 20.767 30.413  13.541  1.00 18.59  ? 155 MET A CB  1 
ATOM   1258 C  CG  . MET A 1 160 ? 20.345 28.972  13.687  1.00 21.31  ? 155 MET A CG  1 
ATOM   1259 S  SD  . MET A 1 160 ? 18.749 28.557  12.897  1.00 24.06  ? 155 MET A SD  1 
ATOM   1260 C  CE  . MET A 1 160 ? 17.720 29.750  13.593  1.00 26.75  ? 155 MET A CE  1 
ATOM   1261 N  N   . ASP A 1 161 ? 22.444 32.843  12.674  1.00 16.79  ? 156 ASP A N   1 
ATOM   1262 C  CA  . ASP A 1 161 ? 22.618 34.297  12.715  1.00 20.91  ? 156 ASP A CA  1 
ATOM   1263 C  C   . ASP A 1 161 ? 22.627 34.891  11.298  1.00 20.87  ? 156 ASP A C   1 
ATOM   1264 O  O   . ASP A 1 161 ? 21.911 35.849  11.009  1.00 19.68  ? 156 ASP A O   1 
ATOM   1265 C  CB  . ASP A 1 161 ? 23.878 34.645  13.490  1.00 21.28  ? 156 ASP A CB  1 
ATOM   1266 C  CG  . ASP A 1 161 ? 23.878 34.331  14.986  1.00 25.24  ? 156 ASP A CG  1 
ATOM   1267 O  OD1 . ASP A 1 161 ? 22.810 34.097  15.542  1.00 26.27  ? 156 ASP A OD1 1 
ATOM   1268 O  OD2 . ASP A 1 161 ? 24.965 34.298  15.585  1.00 27.54  ? 156 ASP A OD2 1 
ATOM   1269 N  N   . ILE A 1 162 ? 23.393 34.281  10.375  1.00 17.52  ? 157 ILE A N   1 
ATOM   1270 C  CA  . ILE A 1 162 ? 23.431 34.756  9.000   1.00 17.50  ? 157 ILE A CA  1 
ATOM   1271 C  C   . ILE A 1 162 ? 22.080 34.608  8.310   1.00 16.01  ? 157 ILE A C   1 
ATOM   1272 O  O   . ILE A 1 162 ? 21.614 35.522  7.608   1.00 18.65  ? 157 ILE A O   1 
ATOM   1273 C  CB  . ILE A 1 162 ? 24.571 34.023  8.207   1.00 17.03  ? 157 ILE A CB  1 
ATOM   1274 C  CG1 . ILE A 1 162 ? 25.922 34.346  8.819   1.00 18.58  ? 157 ILE A CG1 1 
ATOM   1275 C  CG2 . ILE A 1 162 ? 24.475 34.379  6.748   1.00 17.56  ? 157 ILE A CG2 1 
ATOM   1276 C  CD1 . ILE A 1 162 ? 27.060 33.410  8.329   1.00 21.11  ? 157 ILE A CD1 1 
ATOM   1277 N  N   . SER A 1 163 ? 21.418 33.471  8.541   1.00 15.49  ? 158 SER A N   1 
ATOM   1278 C  CA  . SER A 1 163 ? 20.186 33.152  7.826   1.00 16.53  ? 158 SER A CA  1 
ATOM   1279 C  C   . SER A 1 163 ? 19.090 34.160  8.179   1.00 17.59  ? 158 SER A C   1 
ATOM   1280 O  O   . SER A 1 163 ? 18.292 34.534  7.324   1.00 17.02  ? 158 SER A O   1 
ATOM   1281 C  CB  . SER A 1 163 ? 19.687 31.704  8.058   1.00 17.45  ? 158 SER A CB  1 
ATOM   1282 O  OG  . SER A 1 163 ? 19.156 31.462  9.339   1.00 20.01  ? 158 SER A OG  1 
ATOM   1283 N  N   . LYS A 1 164 ? 19.049 34.554  9.454   1.00 17.63  ? 159 LYS A N   1 
ATOM   1284 C  CA  . LYS A 1 164 ? 18.005 35.455  9.921   1.00 21.00  ? 159 LYS A CA  1 
ATOM   1285 C  C   . LYS A 1 164 ? 18.225 36.860  9.382   1.00 21.52  ? 159 LYS A C   1 
ATOM   1286 O  O   . LYS A 1 164 ? 17.276 37.604  9.185   1.00 24.15  ? 159 LYS A O   1 
ATOM   1287 C  CB  . LYS A 1 164 ? 17.969 35.422  11.460  1.00 25.16  ? 159 LYS A CB  1 
ATOM   1288 C  CG  . LYS A 1 164 ? 17.398 34.087  12.002  1.00 30.70  ? 159 LYS A CG  1 
ATOM   1289 C  CD  . LYS A 1 164 ? 17.328 34.084  13.563  1.00 33.08  ? 159 LYS A CD  1 
ATOM   1290 C  CE  . LYS A 1 164 ? 16.136 33.385  14.071  1.00 41.23  ? 159 LYS A CE  1 
ATOM   1291 N  NZ  . LYS A 1 164 ? 15.766 33.878  15.441  1.00 46.37  ? 159 LYS A NZ  1 
ATOM   1292 N  N   . LYS A 1 165 ? 19.484 37.242  9.189   1.00 20.95  ? 160 LYS A N   1 
ATOM   1293 C  CA  . LYS A 1 165 ? 19.833 38.542  8.659   1.00 24.64  ? 160 LYS A CA  1 
ATOM   1294 C  C   . LYS A 1 165 ? 19.640 38.607  7.151   1.00 23.99  ? 160 LYS A C   1 
ATOM   1295 O  O   . LYS A 1 165 ? 19.271 39.649  6.634   1.00 23.54  ? 160 LYS A O   1 
ATOM   1296 C  CB  . LYS A 1 165 ? 21.276 38.902  8.933   1.00 28.79  ? 160 LYS A CB  1 
ATOM   1297 C  CG  . LYS A 1 165 ? 21.568 39.361  10.331  1.00 37.31  ? 160 LYS A CG  1 
ATOM   1298 C  CD  . LYS A 1 165 ? 22.906 40.101  10.411  1.00 45.50  ? 160 LYS A CD  1 
ATOM   1299 C  CE  . LYS A 1 165 ? 23.183 40.596  11.811  1.00 50.03  ? 160 LYS A CE  1 
ATOM   1300 N  NZ  . LYS A 1 165 ? 24.440 41.381  11.880  1.00 52.34  ? 160 LYS A NZ  1 
ATOM   1301 N  N   . GLU A 1 166 ? 19.957 37.517  6.445   1.00 21.35  ? 161 GLU A N   1 
ATOM   1302 C  CA  . GLU A 1 166 ? 20.190 37.570  5.013   1.00 20.46  ? 161 GLU A CA  1 
ATOM   1303 C  C   . GLU A 1 166 ? 19.170 36.874  4.118   1.00 20.05  ? 161 GLU A C   1 
ATOM   1304 O  O   . GLU A 1 166 ? 19.184 37.084  2.909   1.00 22.55  ? 161 GLU A O   1 
ATOM   1305 C  CB  . GLU A 1 166 ? 21.633 37.017  4.710   1.00 21.35  ? 161 GLU A CB  1 
ATOM   1306 C  CG  . GLU A 1 166 ? 22.742 37.801  5.340   1.00 24.85  ? 161 GLU A CG  1 
ATOM   1307 C  CD  . GLU A 1 166 ? 22.910 39.234  4.855   1.00 34.19  ? 161 GLU A CD  1 
ATOM   1308 O  OE1 . GLU A 1 166 ? 22.326 39.599  3.803   1.00 42.04  ? 161 GLU A OE1 1 
ATOM   1309 O  OE2 . GLU A 1 166 ? 23.615 40.001  5.554   1.00 42.17  ? 161 GLU A OE2 1 
ATOM   1310 N  N   . MET A 1 167 ? 18.320 36.016  4.680   1.00 17.77  ? 162 MET A N   1 
ATOM   1311 C  CA  . MET A 1 167 ? 17.372 35.205  3.937   1.00 19.53  ? 162 MET A CA  1 
ATOM   1312 C  C   . MET A 1 167 ? 15.956 35.434  4.418   1.00 20.88  ? 162 MET A C   1 
ATOM   1313 O  O   . MET A 1 167 ? 15.727 35.690  5.600   1.00 20.30  ? 162 MET A O   1 
ATOM   1314 C  CB  . MET A 1 167 ? 17.654 33.671  4.165   1.00 21.55  ? 162 MET A CB  1 
ATOM   1315 C  CG  . MET A 1 167 ? 18.891 33.224  3.456   1.00 23.12  ? 162 MET A CG  1 
ATOM   1316 S  SD  . MET A 1 167 ? 19.401 31.617  4.111   1.00 23.23  ? 162 MET A SD  1 
ATOM   1317 C  CE  . MET A 1 167 ? 20.483 31.072  2.870   1.00 23.07  ? 162 MET A CE  1 
ATOM   1318 N  N   . PRO A 1 168 ? 14.955 35.277  3.526   1.00 21.33  ? 163 PRO A N   1 
ATOM   1319 C  CA  . PRO A 1 168 ? 13.567 35.305  3.960   1.00 22.93  ? 163 PRO A CA  1 
ATOM   1320 C  C   . PRO A 1 168 ? 13.235 34.072  4.788   1.00 22.08  ? 163 PRO A C   1 
ATOM   1321 O  O   . PRO A 1 168 ? 13.862 33.021  4.636   1.00 20.90  ? 163 PRO A O   1 
ATOM   1322 C  CB  . PRO A 1 168 ? 12.783 35.284  2.670   1.00 24.04  ? 163 PRO A CB  1 
ATOM   1323 C  CG  . PRO A 1 168 ? 13.666 34.699  1.698   1.00 25.06  ? 163 PRO A CG  1 
ATOM   1324 C  CD  . PRO A 1 168 ? 15.092 35.049  2.084   1.00 25.38  ? 163 PRO A CD  1 
ATOM   1325 N  N   . PRO A 1 169 ? 12.184 34.145  5.622   1.00 21.79  ? 164 PRO A N   1 
ATOM   1326 C  CA  . PRO A 1 169 ? 11.796 33.024  6.471   1.00 21.40  ? 164 PRO A CA  1 
ATOM   1327 C  C   . PRO A 1 169 ? 11.393 31.749  5.768   1.00 22.15  ? 164 PRO A C   1 
ATOM   1328 O  O   . PRO A 1 169 ? 11.461 30.676  6.380   1.00 21.91  ? 164 PRO A O   1 
ATOM   1329 C  CB  . PRO A 1 169 ? 10.601 33.556  7.278   1.00 21.58  ? 164 PRO A CB  1 
ATOM   1330 C  CG  . PRO A 1 169 ? 10.453 34.950  6.953   1.00 22.05  ? 164 PRO A CG  1 
ATOM   1331 C  CD  . PRO A 1 169 ? 11.357 35.338  5.846   1.00 20.92  ? 164 PRO A CD  1 
ATOM   1332 N  N   . THR A 1 170 ? 11.015 31.863  4.483   1.00 20.44  ? 165 THR A N   1 
ATOM   1333 C  CA  . THR A 1 170 ? 10.666 30.698  3.700   1.00 19.24  ? 165 THR A CA  1 
ATOM   1334 C  C   . THR A 1 170 ? 11.851 30.108  2.928   1.00 16.74  ? 165 THR A C   1 
ATOM   1335 O  O   . THR A 1 170 ? 11.683 29.118  2.237   1.00 18.97  ? 165 THR A O   1 
ATOM   1336 C  CB  . THR A 1 170 ? 9.566  31.069  2.663   1.00 21.36  ? 165 THR A CB  1 
ATOM   1337 O  OG1 . THR A 1 170 ? 10.054 32.251  2.066   1.00 22.59  ? 165 THR A OG1 1 
ATOM   1338 C  CG2 . THR A 1 170 ? 8.213  31.231  3.319   1.00 24.32  ? 165 THR A CG2 1 
ATOM   1339 N  N   . ASN A 1 171 ? 13.034 30.717  3.003   1.00 16.93  ? 166 ASN A N   1 
ATOM   1340 C  CA  . ASN A 1 171 ? 14.162 30.159  2.254   1.00 17.51  ? 166 ASN A CA  1 
ATOM   1341 C  C   . ASN A 1 171 ? 14.378 28.687  2.654   1.00 18.59  ? 166 ASN A C   1 
ATOM   1342 O  O   . ASN A 1 171 ? 14.503 28.397  3.844   1.00 17.31  ? 166 ASN A O   1 
ATOM   1343 C  CB  . ASN A 1 171 ? 15.378 30.991  2.490   1.00 19.13  ? 166 ASN A CB  1 
ATOM   1344 C  CG  . ASN A 1 171 ? 16.565 30.447  1.769   1.00 24.67  ? 166 ASN A CG  1 
ATOM   1345 O  OD1 . ASN A 1 171 ? 17.149 29.446  2.199   1.00 24.90  ? 166 ASN A OD1 1 
ATOM   1346 N  ND2 . ASN A 1 171 ? 16.920 31.096  0.658   1.00 25.03  ? 166 ASN A ND2 1 
ATOM   1347 N  N   . PRO A 1 172 ? 14.383 27.692  1.726   1.00 18.47  ? 167 PRO A N   1 
ATOM   1348 C  CA  . PRO A 1 172 ? 14.559 26.292  2.113   1.00 17.67  ? 167 PRO A CA  1 
ATOM   1349 C  C   . PRO A 1 172 ? 15.835 25.985  2.888   1.00 15.65  ? 167 PRO A C   1 
ATOM   1350 O  O   . PRO A 1 172 ? 15.823 25.082  3.711   1.00 15.79  ? 167 PRO A O   1 
ATOM   1351 C  CB  . PRO A 1 172 ? 14.509 25.555  0.763   1.00 19.94  ? 167 PRO A CB  1 
ATOM   1352 C  CG  . PRO A 1 172 ? 13.678 26.506  -0.120  1.00 23.62  ? 167 PRO A CG  1 
ATOM   1353 C  CD  . PRO A 1 172 ? 14.121 27.830  0.287   1.00 22.33  ? 167 PRO A CD  1 
ATOM   1354 N  N   . ILE A 1 173 ? 16.936 26.680  2.589   1.00 16.17  ? 168 ILE A N   1 
ATOM   1355 C  CA  . ILE A 1 173 ? 18.146 26.442  3.357   1.00 16.69  ? 168 ILE A CA  1 
ATOM   1356 C  C   . ILE A 1 173 ? 17.942 26.905  4.801   1.00 15.93  ? 168 ILE A C   1 
ATOM   1357 O  O   . ILE A 1 173 ? 18.306 26.210  5.742   1.00 14.56  ? 168 ILE A O   1 
ATOM   1358 C  CB  . ILE A 1 173 ? 19.364 27.057  2.671   1.00 19.08  ? 168 ILE A CB  1 
ATOM   1359 C  CG1 . ILE A 1 173 ? 19.607 26.385  1.291   1.00 22.59  ? 168 ILE A CG1 1 
ATOM   1360 C  CG2 . ILE A 1 173 ? 20.604 26.936  3.546   1.00 20.87  ? 168 ILE A CG2 1 
ATOM   1361 C  CD1 . ILE A 1 173 ? 20.469 27.037  0.469   1.00 22.00  ? 168 ILE A CD1 1 
ATOM   1362 N  N   . ARG A 1 174 ? 17.356 28.094  4.962   1.00 15.95  ? 169 ARG A N   1 
ATOM   1363 C  CA  . ARG A 1 174 ? 17.029 28.612  6.290   1.00 15.11  ? 169 ARG A CA  1 
ATOM   1364 C  C   . ARG A 1 174 ? 16.108 27.660  7.064   1.00 14.33  ? 169 ARG A C   1 
ATOM   1365 O  O   . ARG A 1 174 ? 16.382 27.338  8.238   1.00 14.28  ? 169 ARG A O   1 
ATOM   1366 C  CB  . ARG A 1 174 ? 16.416 29.998  6.185   1.00 15.54  ? 169 ARG A CB  1 
ATOM   1367 C  CG  . ARG A 1 174 ? 16.031 30.573  7.551   1.00 15.92  ? 169 ARG A CG  1 
ATOM   1368 C  CD  . ARG A 1 174 ? 15.604 32.059  7.470   1.00 16.73  ? 169 ARG A CD  1 
ATOM   1369 N  NE  . ARG A 1 174 ? 15.039 32.509  8.729   1.00 17.36  ? 169 ARG A NE  1 
ATOM   1370 C  CZ  . ARG A 1 174 ? 14.581 33.740  8.951   1.00 19.89  ? 169 ARG A CZ  1 
ATOM   1371 N  NH1 . ARG A 1 174 ? 14.645 34.696  8.026   1.00 20.29  ? 169 ARG A NH1 1 
ATOM   1372 N  NH2 . ARG A 1 174 ? 13.926 33.978  10.075  1.00 19.08  ? 169 ARG A NH2 1 
ATOM   1373 N  N   . LEU A 1 175 ? 15.083 27.140  6.395   1.00 12.89  ? 170 LEU A N   1 
ATOM   1374 C  CA  . LEU A 1 175 ? 14.154 26.201  6.987   1.00 13.27  ? 170 LEU A CA  1 
ATOM   1375 C  C   . LEU A 1 175 ? 14.814 24.882  7.380   1.00 13.79  ? 170 LEU A C   1 
ATOM   1376 O  O   . LEU A 1 175 ? 14.610 24.371  8.487   1.00 14.83  ? 170 LEU A O   1 
ATOM   1377 C  CB  . LEU A 1 175 ? 13.006 25.898  6.059   1.00 14.78  ? 170 LEU A CB  1 
ATOM   1378 C  CG  . LEU A 1 175 ? 12.043 27.054  5.826   1.00 15.91  ? 170 LEU A CG  1 
ATOM   1379 C  CD1 . LEU A 1 175 ? 10.967 26.676  4.817   1.00 16.93  ? 170 LEU A CD1 1 
ATOM   1380 C  CD2 . LEU A 1 175 ? 11.341 27.461  7.091   1.00 19.11  ? 170 LEU A CD2 1 
ATOM   1381 N  N   . GLY A 1 176 ? 15.641 24.343  6.490   1.00 13.91  ? 171 GLY A N   1 
ATOM   1382 C  CA  . GLY A 1 176 ? 16.292 23.078  6.814   1.00 14.16  ? 171 GLY A CA  1 
ATOM   1383 C  C   . GLY A 1 176 ? 17.310 23.196  7.935   1.00 13.35  ? 171 GLY A C   1 
ATOM   1384 O  O   . GLY A 1 176 ? 17.452 22.268  8.744   1.00 13.44  ? 171 GLY A O   1 
ATOM   1385 N  N   . LEU A 1 177 ? 17.991 24.343  7.968   1.00 13.31  ? 172 LEU A N   1 
ATOM   1386 C  CA  . LEU A 1 177 ? 18.898 24.647  9.063   1.00 13.29  ? 172 LEU A CA  1 
ATOM   1387 C  C   . LEU A 1 177 ? 18.127 24.643  10.373  1.00 13.46  ? 172 LEU A C   1 
ATOM   1388 O  O   . LEU A 1 177 ? 18.536 24.032  11.363  1.00 12.90  ? 172 LEU A O   1 
ATOM   1389 C  CB  . LEU A 1 177 ? 19.584 25.942  8.844   1.00 14.12  ? 172 LEU A CB  1 
ATOM   1390 C  CG  . LEU A 1 177 ? 20.230 26.602  10.016  1.00 13.33  ? 172 LEU A CG  1 
ATOM   1391 C  CD1 . LEU A 1 177 ? 21.413 25.777  10.589  1.00 13.41  ? 172 LEU A CD1 1 
ATOM   1392 C  CD2 . LEU A 1 177 ? 20.770 27.931  9.648   1.00 13.55  ? 172 LEU A CD2 1 
ATOM   1393 N  N   . ALA A 1 178 ? 17.023 25.389  10.412  1.00 13.55  ? 173 ALA A N   1 
ATOM   1394 C  CA  . ALA A 1 178 ? 16.260 25.456  11.649  1.00 14.95  ? 173 ALA A CA  1 
ATOM   1395 C  C   . ALA A 1 178 ? 15.704 24.105  12.076  1.00 13.12  ? 173 ALA A C   1 
ATOM   1396 O  O   . ALA A 1 178 ? 15.693 23.772  13.257  1.00 13.43  ? 173 ALA A O   1 
ATOM   1397 C  CB  . ALA A 1 178 ? 15.127 26.505  11.488  1.00 14.38  ? 173 ALA A CB  1 
ATOM   1398 N  N   . LEU A 1 179 ? 15.214 23.311  11.108  1.00 13.27  ? 174 LEU A N   1 
ATOM   1399 C  CA  . LEU A 1 179 ? 14.766 21.959  11.373  1.00 13.27  ? 174 LEU A CA  1 
ATOM   1400 C  C   . LEU A 1 179 ? 15.901 21.161  12.028  1.00 13.16  ? 174 LEU A C   1 
ATOM   1401 O  O   . LEU A 1 179 ? 15.687 20.581  13.092  1.00 13.84  ? 174 LEU A O   1 
ATOM   1402 C  CB  . LEU A 1 179 ? 14.300 21.256  10.055  1.00 14.52  ? 174 LEU A CB  1 
ATOM   1403 C  CG  . LEU A 1 179 ? 13.859 19.789  10.184  1.00 14.96  ? 174 LEU A CG  1 
ATOM   1404 C  CD1 . LEU A 1 179 ? 12.674 19.665  11.024  1.00 16.77  ? 174 LEU A CD1 1 
ATOM   1405 C  CD2 . LEU A 1 179 ? 13.543 19.160  8.770   1.00 16.44  ? 174 LEU A CD2 1 
ATOM   1406 N  N   . ASN A 1 180 ? 17.077 21.171  11.414  1.00 13.10  ? 175 ASN A N   1 
ATOM   1407 C  CA  . ASN A 1 180 ? 18.173 20.370  11.972  1.00 13.37  ? 175 ASN A CA  1 
ATOM   1408 C  C   . ASN A 1 180 ? 18.705 20.870  13.315  1.00 12.72  ? 175 ASN A C   1 
ATOM   1409 O  O   . ASN A 1 180 ? 19.001 20.060  14.182  1.00 12.53  ? 175 ASN A O   1 
ATOM   1410 C  CB  . ASN A 1 180 ? 19.257 20.272  10.996  1.00 13.10  ? 175 ASN A CB  1 
ATOM   1411 C  CG  . ASN A 1 180 ? 18.905 19.332  9.852   1.00 13.95  ? 175 ASN A CG  1 
ATOM   1412 O  OD1 . ASN A 1 180 ? 17.794 18.913  9.656   1.00 14.34  ? 175 ASN A OD1 1 
ATOM   1413 N  ND2 . ASN A 1 180 ? 19.950 18.971  9.038   1.00 14.28  ? 175 ASN A ND2 1 
ATOM   1414 N  N   . PHE A 1 181 ? 18.701 22.187  13.535  1.00 11.51  ? 176 PHE A N   1 
ATOM   1415 C  CA  . PHE A 1 181 ? 19.097 22.709  14.823  1.00 11.48  ? 176 PHE A CA  1 
ATOM   1416 C  C   . PHE A 1 181 ? 18.070 22.323  15.886  1.00 11.63  ? 176 PHE A C   1 
ATOM   1417 O  O   . PHE A 1 181 ? 18.444 22.017  17.028  1.00 12.36  ? 176 PHE A O   1 
ATOM   1418 C  CB  . PHE A 1 181 ? 19.334 24.225  14.701  1.00 12.44  ? 176 PHE A CB  1 
ATOM   1419 C  CG  . PHE A 1 181 ? 20.106 24.950  15.799  1.00 13.02  ? 176 PHE A CG  1 
ATOM   1420 C  CD1 . PHE A 1 181 ? 20.885 24.261  16.694  1.00 13.37  ? 176 PHE A CD1 1 
ATOM   1421 C  CD2 . PHE A 1 181 ? 20.018 26.317  15.928  1.00 14.57  ? 176 PHE A CD2 1 
ATOM   1422 C  CE1 . PHE A 1 181 ? 21.599 24.900  17.695  1.00 12.52  ? 176 PHE A CE1 1 
ATOM   1423 C  CE2 . PHE A 1 181 ? 20.730 26.993  16.957  1.00 16.13  ? 176 PHE A CE2 1 
ATOM   1424 C  CZ  . PHE A 1 181 ? 21.550 26.268  17.814  1.00 14.94  ? 176 PHE A CZ  1 
ATOM   1425 N  N   . SER A 1 182 ? 16.781 22.324  15.524  1.00 12.46  ? 177 SER A N   1 
ATOM   1426 C  CA  . SER A 1 182 ? 15.766 21.884  16.472  1.00 13.77  ? 177 SER A CA  1 
ATOM   1427 C  C   . SER A 1 182 ? 15.960 20.406  16.836  1.00 13.39  ? 177 SER A C   1 
ATOM   1428 O  O   . SER A 1 182 ? 15.781 20.034  17.982  1.00 13.98  ? 177 SER A O   1 
ATOM   1429 C  CB  . SER A 1 182 ? 14.355 22.163  15.965  1.00 15.08  ? 177 SER A CB  1 
ATOM   1430 O  OG  . SER A 1 182 ? 13.933 21.282  14.922  1.00 16.61  ? 177 SER A OG  1 
ATOM   1431 N  N   . VAL A 1 183 ? 16.368 19.566  15.884  1.00 13.34  ? 178 VAL A N   1 
ATOM   1432 C  CA  . VAL A 1 183 ? 16.683 18.155  16.146  1.00 14.43  ? 178 VAL A CA  1 
ATOM   1433 C  C   . VAL A 1 183 ? 17.900 18.039  17.065  1.00 13.20  ? 178 VAL A C   1 
ATOM   1434 O  O   . VAL A 1 183 ? 17.901 17.248  18.011  1.00 14.58  ? 178 VAL A O   1 
ATOM   1435 C  CB  . VAL A 1 183 ? 16.938 17.354  14.810  1.00 15.11  ? 178 VAL A CB  1 
ATOM   1436 C  CG1 . VAL A 1 183 ? 17.441 15.947  15.077  1.00 15.14  ? 178 VAL A CG1 1 
ATOM   1437 C  CG2 . VAL A 1 183 ? 15.694 17.301  13.929  1.00 17.77  ? 178 VAL A CG2 1 
ATOM   1438 N  N   . PHE A 1 184 ? 18.923 18.859  16.810  1.00 13.12  ? 179 PHE A N   1 
ATOM   1439 C  CA  . PHE A 1 184 ? 20.076 18.951  17.692  1.00 12.96  ? 179 PHE A CA  1 
ATOM   1440 C  C   . PHE A 1 184 ? 19.629 19.208  19.131  1.00 13.19  ? 179 PHE A C   1 
ATOM   1441 O  O   . PHE A 1 184 ? 20.015 18.499  20.045  1.00 13.80  ? 179 PHE A O   1 
ATOM   1442 C  CB  . PHE A 1 184 ? 20.996 20.006  17.224  1.00 12.96  ? 179 PHE A CB  1 
ATOM   1443 C  CG  . PHE A 1 184 ? 22.056 20.357  18.228  1.00 13.24  ? 179 PHE A CG  1 
ATOM   1444 C  CD1 . PHE A 1 184 ? 23.194 19.599  18.338  1.00 14.01  ? 179 PHE A CD1 1 
ATOM   1445 C  CD2 . PHE A 1 184 ? 21.901 21.434  19.066  1.00 14.27  ? 179 PHE A CD2 1 
ATOM   1446 C  CE1 . PHE A 1 184 ? 24.174 19.938  19.246  1.00 13.88  ? 179 PHE A CE1 1 
ATOM   1447 C  CE2 . PHE A 1 184 ? 22.902 21.762  19.993  1.00 15.61  ? 179 PHE A CE2 1 
ATOM   1448 C  CZ  . PHE A 1 184 ? 24.016 20.984  20.064  1.00 15.29  ? 179 PHE A CZ  1 
ATOM   1449 N  N   . HIS A 1 185 ? 18.749 20.201  19.327  1.00 12.73  ? 180 HIS A N   1 
ATOM   1450 C  CA  . HIS A 1 185 ? 18.319 20.554  20.663  1.00 14.44  ? 180 HIS A CA  1 
ATOM   1451 C  C   . HIS A 1 185 ? 17.591 19.393  21.336  1.00 14.67  ? 180 HIS A C   1 
ATOM   1452 O  O   . HIS A 1 185 ? 17.791 19.138  22.530  1.00 14.86  ? 180 HIS A O   1 
ATOM   1453 C  CB  . HIS A 1 185 ? 17.414 21.850  20.632  1.00 14.92  ? 180 HIS A CB  1 
ATOM   1454 C  CG  . HIS A 1 185 ? 18.105 23.148  20.357  1.00 14.25  ? 180 HIS A CG  1 
ATOM   1455 N  ND1 . HIS A 1 185 ? 19.251 23.537  21.065  1.00 14.64  ? 180 HIS A ND1 1 
ATOM   1456 C  CD2 . HIS A 1 185 ? 17.798 24.107  19.449  1.00 15.37  ? 180 HIS A CD2 1 
ATOM   1457 C  CE1 . HIS A 1 185 ? 19.595 24.711  20.576  1.00 14.61  ? 180 HIS A CE1 1 
ATOM   1458 N  NE2 . HIS A 1 185 ? 18.756 25.105  19.589  1.00 14.57  ? 180 HIS A NE2 1 
ATOM   1459 N  N   . TYR A 1 186 ? 16.706 18.703  20.607  1.00 14.84  ? 181 TYR A N   1 
ATOM   1460 C  CA  . TYR A 1 186 ? 15.861 17.674  21.187  1.00 14.41  ? 181 TYR A CA  1 
ATOM   1461 C  C   . TYR A 1 186 ? 16.629 16.366  21.422  1.00 16.02  ? 181 TYR A C   1 
ATOM   1462 O  O   . TYR A 1 186 ? 16.555 15.762  22.499  1.00 17.32  ? 181 TYR A O   1 
ATOM   1463 C  CB  . TYR A 1 186 ? 14.681 17.390  20.246  1.00 18.43  ? 181 TYR A CB  1 
ATOM   1464 C  CG  . TYR A 1 186 ? 13.632 16.534  20.881  1.00 19.07  ? 181 TYR A CG  1 
ATOM   1465 C  CD1 . TYR A 1 186 ? 12.596 17.100  21.604  1.00 23.12  ? 181 TYR A CD1 1 
ATOM   1466 C  CD2 . TYR A 1 186 ? 13.706 15.158  20.817  1.00 21.77  ? 181 TYR A CD2 1 
ATOM   1467 C  CE1 . TYR A 1 186 ? 11.623 16.307  22.212  1.00 23.64  ? 181 TYR A CE1 1 
ATOM   1468 C  CE2 . TYR A 1 186 ? 12.740 14.353  21.415  1.00 23.37  ? 181 TYR A CE2 1 
ATOM   1469 C  CZ  . TYR A 1 186 ? 11.708 14.933  22.117  1.00 23.86  ? 181 TYR A CZ  1 
ATOM   1470 O  OH  . TYR A 1 186 ? 10.746 14.131  22.733  1.00 28.41  ? 181 TYR A OH  1 
ATOM   1471 N  N   . GLU A 1 187 ? 17.403 15.977  20.418  1.00 16.99  ? 182 GLU A N   1 
ATOM   1472 C  CA  . GLU A 1 187 ? 18.006 14.649  20.396  1.00 17.36  ? 182 GLU A CA  1 
ATOM   1473 C  C   . GLU A 1 187 ? 19.403 14.609  21.020  1.00 18.89  ? 182 GLU A C   1 
ATOM   1474 O  O   . GLU A 1 187 ? 19.824 13.572  21.520  1.00 21.27  ? 182 GLU A O   1 
ATOM   1475 C  CB  . GLU A 1 187 ? 18.045 14.118  18.963  1.00 18.53  ? 182 GLU A CB  1 
ATOM   1476 C  CG  . GLU A 1 187 ? 16.707 13.779  18.327  1.00 20.37  ? 182 GLU A CG  1 
ATOM   1477 C  CD  . GLU A 1 187 ? 15.909 12.614  18.897  1.00 25.29  ? 182 GLU A CD  1 
ATOM   1478 O  OE1 . GLU A 1 187 ? 16.474 11.857  19.726  1.00 25.87  ? 182 GLU A OE1 1 
ATOM   1479 O  OE2 . GLU A 1 187 ? 14.704 12.492  18.563  1.00 25.94  ? 182 GLU A OE2 1 
ATOM   1480 N  N   . ILE A 1 188 ? 20.129 15.710  21.004  1.00 16.99  ? 183 ILE A N   1 
ATOM   1481 C  CA  . ILE A 1 188 ? 21.536 15.725  21.408  1.00 17.52  ? 183 ILE A CA  1 
ATOM   1482 C  C   . ILE A 1 188 ? 21.787 16.531  22.666  1.00 18.12  ? 183 ILE A C   1 
ATOM   1483 O  O   . ILE A 1 188 ? 22.548 16.092  23.536  1.00 17.97  ? 183 ILE A O   1 
ATOM   1484 C  CB  . ILE A 1 188 ? 22.436 16.297  20.262  1.00 17.39  ? 183 ILE A CB  1 
ATOM   1485 C  CG1 . ILE A 1 188 ? 22.170 15.565  18.971  1.00 19.97  ? 183 ILE A CG1 1 
ATOM   1486 C  CG2 . ILE A 1 188 ? 23.893 16.319  20.616  1.00 19.40  ? 183 ILE A CG2 1 
ATOM   1487 C  CD1 . ILE A 1 188 ? 22.621 14.185  18.912  1.00 20.87  ? 183 ILE A CD1 1 
ATOM   1488 N  N   . ALA A 1 189 ? 21.172 17.730  22.735  1.00 17.29  ? 184 ALA A N   1 
ATOM   1489 C  CA  . ALA A 1 189 ? 21.494 18.716  23.753  1.00 17.66  ? 184 ALA A CA  1 
ATOM   1490 C  C   . ALA A 1 189 ? 20.565 18.678  24.962  1.00 17.78  ? 184 ALA A C   1 
ATOM   1491 O  O   . ALA A 1 189 ? 20.719 19.495  25.850  1.00 20.70  ? 184 ALA A O   1 
ATOM   1492 C  CB  . ALA A 1 189 ? 21.490 20.075  23.150  1.00 19.98  ? 184 ALA A CB  1 
ATOM   1493 N  N   . ASN A 1 190 ? 19.633 17.735  24.997  1.00 17.93  ? 185 ASN A N   1 
ATOM   1494 C  CA  . ASN A 1 190 ? 18.707 17.593  26.116  1.00 21.75  ? 185 ASN A CA  1 
ATOM   1495 C  C   . ASN A 1 190 ? 17.978 18.907  26.403  1.00 22.43  ? 185 ASN A C   1 
ATOM   1496 O  O   . ASN A 1 190 ? 17.761 19.305  27.551  1.00 21.13  ? 185 ASN A O   1 
ATOM   1497 C  CB  . ASN A 1 190 ? 19.443 17.036  27.392  1.00 25.03  ? 185 ASN A CB  1 
ATOM   1498 C  CG  . ASN A 1 190 ? 18.454 16.477  28.428  1.00 29.80  ? 185 ASN A CG  1 
ATOM   1499 O  OD1 . ASN A 1 190 ? 17.385 15.929  28.108  1.00 34.21  ? 185 ASN A OD1 1 
ATOM   1500 N  ND2 . ASN A 1 190 ? 18.753 16.662  29.692  1.00 34.00  ? 185 ASN A ND2 1 
ATOM   1501 N  N   . SER A 1 191 ? 17.571 19.593  25.327  1.00 17.87  ? 186 SER A N   1 
ATOM   1502 C  CA  . SER A 1 191 ? 16.858 20.853  25.429  1.00 17.83  ? 186 SER A CA  1 
ATOM   1503 C  C   . SER A 1 191 ? 15.551 20.779  24.652  1.00 18.15  ? 186 SER A C   1 
ATOM   1504 O  O   . SER A 1 191 ? 15.388 21.463  23.635  1.00 17.35  ? 186 SER A O   1 
ATOM   1505 C  CB  . SER A 1 191 ? 17.745 21.979  24.914  1.00 19.45  ? 186 SER A CB  1 
ATOM   1506 O  OG  . SER A 1 191 ? 18.974 22.075  25.610  1.00 21.60  ? 186 SER A OG  1 
ATOM   1507 N  N   . PRO A 1 192 ? 14.577 19.933  25.044  1.00 18.66  ? 187 PRO A N   1 
ATOM   1508 C  CA  . PRO A 1 192 ? 13.367 19.782  24.249  1.00 19.05  ? 187 PRO A CA  1 
ATOM   1509 C  C   . PRO A 1 192 ? 12.560 21.078  24.159  1.00 18.37  ? 187 PRO A C   1 
ATOM   1510 O  O   . PRO A 1 192 ? 11.903 21.310  23.140  1.00 17.98  ? 187 PRO A O   1 
ATOM   1511 C  CB  . PRO A 1 192 ? 12.612 18.638  24.935  1.00 18.41  ? 187 PRO A CB  1 
ATOM   1512 C  CG  . PRO A 1 192 ? 13.173 18.622  26.349  1.00 19.45  ? 187 PRO A CG  1 
ATOM   1513 C  CD  . PRO A 1 192 ? 14.589 19.039  26.224  1.00 20.34  ? 187 PRO A CD  1 
ATOM   1514 N  N   . GLU A 1 193 ? 12.601 21.909  25.186  1.00 20.28  ? 188 GLU A N   1 
ATOM   1515 C  CA  . GLU A 1 193 ? 11.835 23.145  25.134  1.00 22.07  ? 188 GLU A CA  1 
ATOM   1516 C  C   . GLU A 1 193 ? 12.410 24.133  24.112  1.00 20.34  ? 188 GLU A C   1 
ATOM   1517 O  O   . GLU A 1 193 ? 11.656 24.772  23.359  1.00 18.22  ? 188 GLU A O   1 
ATOM   1518 C  CB  . GLU A 1 193 ? 11.713 23.757  26.539  1.00 23.22  ? 188 GLU A CB  1 
ATOM   1519 C  CG  . GLU A 1 193 ? 10.652 23.051  27.393  1.00 25.14  ? 188 GLU A CG  1 
ATOM   1520 C  CD  . GLU A 1 193 ? 10.539 23.497  28.849  1.00 26.60  ? 188 GLU A CD  1 
ATOM   1521 O  OE1 . GLU A 1 193 ? 11.540 24.074  29.343  1.00 25.12  ? 188 GLU A OE1 1 
ATOM   1522 O  OE2 . GLU A 1 193 ? 9.484  23.252  29.510  1.00 27.23  ? 188 GLU A OE2 1 
ATOM   1523 N  N   . GLU A 1 194 ? 13.747 24.177  24.014  1.00 16.97  ? 189 GLU A N   1 
ATOM   1524 C  CA  . GLU A 1 194 ? 14.409 24.962  22.983  1.00 16.33  ? 189 GLU A CA  1 
ATOM   1525 C  C   . GLU A 1 194 ? 14.047 24.419  21.597  1.00 16.49  ? 189 GLU A C   1 
ATOM   1526 O  O   . GLU A 1 194 ? 13.779 25.221  20.675  1.00 15.73  ? 189 GLU A O   1 
ATOM   1527 C  CB  . GLU A 1 194 ? 15.939 24.976  23.177  1.00 15.80  ? 189 GLU A CB  1 
ATOM   1528 C  CG  . GLU A 1 194 ? 16.690 25.980  22.347  1.00 17.02  ? 189 GLU A CG  1 
ATOM   1529 C  CD  . GLU A 1 194 ? 16.463 27.464  22.670  1.00 20.85  ? 189 GLU A CD  1 
ATOM   1530 O  OE1 . GLU A 1 194 ? 15.917 27.761  23.760  1.00 21.70  ? 189 GLU A OE1 1 
ATOM   1531 O  OE2 . GLU A 1 194 ? 16.872 28.314  21.842  1.00 21.46  ? 189 GLU A OE2 1 
ATOM   1532 N  N   . ALA A 1 195 ? 14.012 23.084  21.467  1.00 15.74  ? 190 ALA A N   1 
ATOM   1533 C  CA  . ALA A 1 195 ? 13.622 22.438  20.210  1.00 15.81  ? 190 ALA A CA  1 
ATOM   1534 C  C   . ALA A 1 195 ? 12.223 22.848  19.743  1.00 17.34  ? 190 ALA A C   1 
ATOM   1535 O  O   . ALA A 1 195 ? 12.021 23.270  18.594  1.00 15.46  ? 190 ALA A O   1 
ATOM   1536 C  CB  . ALA A 1 195 ? 13.720 20.929  20.320  1.00 16.25  ? 190 ALA A CB  1 
ATOM   1537 N  N   . ILE A 1 196 ? 11.258 22.762  20.668  1.00 16.67  ? 191 ILE A N   1 
ATOM   1538 C  CA  . ILE A 1 196 ? 9.866  23.082  20.365  1.00 18.40  ? 191 ILE A CA  1 
ATOM   1539 C  C   . ILE A 1 196 ? 9.682  24.558  20.029  1.00 15.87  ? 191 ILE A C   1 
ATOM   1540 O  O   . ILE A 1 196 ? 9.003  24.902  19.056  1.00 17.19  ? 191 ILE A O   1 
ATOM   1541 C  CB  . ILE A 1 196 ? 8.968  22.676  21.570  1.00 18.25  ? 191 ILE A CB  1 
ATOM   1542 C  CG1 . ILE A 1 196 ? 8.896  21.177  21.711  1.00 20.22  ? 191 ILE A CG1 1 
ATOM   1543 C  CG2 . ILE A 1 196 ? 7.548  23.234  21.411  1.00 19.76  ? 191 ILE A CG2 1 
ATOM   1544 C  CD1 . ILE A 1 196 ? 8.365  20.623  23.093  1.00 21.91  ? 191 ILE A CD1 1 
ATOM   1545 N  N   . SER A 1 197 ? 10.347 25.420  20.785  1.00 17.28  ? 192 SER A N   1 
ATOM   1546 C  CA  . SER A 1 197 ? 10.245 26.856  20.577  1.00 18.35  ? 192 SER A CA  1 
ATOM   1547 C  C   . SER A 1 197 ? 10.772 27.268  19.213  1.00 17.62  ? 192 SER A C   1 
ATOM   1548 O  O   . SER A 1 197 ? 10.157 28.060  18.485  1.00 16.98  ? 192 SER A O   1 
ATOM   1549 C  CB  . SER A 1 197 ? 10.965 27.621  21.670  1.00 20.60  ? 192 SER A CB  1 
ATOM   1550 O  OG  . SER A 1 197 ? 10.817 29.033  21.487  1.00 24.86  ? 192 SER A OG  1 
ATOM   1551 N  N   . LEU A 1 198 ? 11.941 26.725  18.874  1.00 16.44  ? 193 LEU A N   1 
ATOM   1552 C  CA  . LEU A 1 198 ? 12.528 27.009  17.577  1.00 16.38  ? 193 LEU A CA  1 
ATOM   1553 C  C   . LEU A 1 198 ? 11.623 26.495  16.466  1.00 15.63  ? 193 LEU A C   1 
ATOM   1554 O  O   . LEU A 1 198 ? 11.419 27.205  15.475  1.00 17.17  ? 193 LEU A O   1 
ATOM   1555 C  CB  . LEU A 1 198 ? 13.922 26.385  17.469  1.00 17.05  ? 193 LEU A CB  1 
ATOM   1556 C  CG  . LEU A 1 198 ? 14.612 26.552  16.141  1.00 16.46  ? 193 LEU A CG  1 
ATOM   1557 C  CD1 . LEU A 1 198 ? 14.798 27.983  15.726  1.00 17.41  ? 193 LEU A CD1 1 
ATOM   1558 C  CD2 . LEU A 1 198 ? 15.995 25.923  16.214  1.00 17.17  ? 193 LEU A CD2 1 
ATOM   1559 N  N   . ALA A 1 199 ? 11.102 25.265  16.602  1.00 15.39  ? 194 ALA A N   1 
ATOM   1560 C  CA  . ALA A 1 199 ? 10.300 24.694  15.523  1.00 16.46  ? 194 ALA A CA  1 
ATOM   1561 C  C   . ALA A 1 199 ? 9.019  25.502  15.318  1.00 17.48  ? 194 ALA A C   1 
ATOM   1562 O  O   . ALA A 1 199 ? 8.616  25.759  14.166  1.00 17.07  ? 194 ALA A O   1 
ATOM   1563 C  CB  . ALA A 1 199 ? 9.945  23.246  15.792  1.00 18.35  ? 194 ALA A CB  1 
ATOM   1564 N  N   . LYS A 1 200 ? 8.404  25.912  16.448  1.00 18.20  ? 195 LYS A N   1 
ATOM   1565 C  CA  . LYS A 1 200 ? 7.171  26.699  16.393  1.00 21.25  ? 195 LYS A CA  1 
ATOM   1566 C  C   . LYS A 1 200 ? 7.384  28.058  15.741  1.00 17.69  ? 195 LYS A C   1 
ATOM   1567 O  O   . LYS A 1 200 ? 6.631  28.434  14.846  1.00 17.69  ? 195 LYS A O   1 
ATOM   1568 C  CB  . LYS A 1 200 ? 6.574  26.949  17.782  1.00 24.69  ? 195 LYS A CB  1 
ATOM   1569 C  CG  . LYS A 1 200 ? 5.797  25.812  18.301  1.00 32.16  ? 195 LYS A CG  1 
ATOM   1570 C  CD  . LYS A 1 200 ? 5.205  26.102  19.730  1.00 39.01  ? 195 LYS A CD  1 
ATOM   1571 C  CE  . LYS A 1 200 ? 4.331  24.965  20.249  1.00 39.28  ? 195 LYS A CE  1 
ATOM   1572 N  NZ  . LYS A 1 200 ? 4.151  25.031  21.722  1.00 44.71  ? 195 LYS A NZ  1 
ATOM   1573 N  N   . THR A 1 201 ? 8.416  28.785  16.187  1.00 17.42  ? 196 THR A N   1 
ATOM   1574 C  CA  . THR A 1 201 ? 8.698  30.108  15.674  1.00 17.19  ? 196 THR A CA  1 
ATOM   1575 C  C   . THR A 1 201 ? 9.020  30.024  14.179  1.00 18.07  ? 196 THR A C   1 
ATOM   1576 O  O   . THR A 1 201 ? 8.543  30.841  13.386  1.00 16.70  ? 196 THR A O   1 
ATOM   1577 C  CB  . THR A 1 201 ? 9.769  30.769  16.469  1.00 18.88  ? 196 THR A CB  1 
ATOM   1578 O  OG1 . THR A 1 201 ? 9.259  31.112  17.800  1.00 21.36  ? 196 THR A OG1 1 
ATOM   1579 C  CG2 . THR A 1 201 ? 10.289 32.015  15.779  1.00 21.81  ? 196 THR A CG2 1 
ATOM   1580 N  N   . THR A 1 202 ? 9.873  29.054  13.819  1.00 16.39  ? 197 THR A N   1 
ATOM   1581 C  CA  . THR A 1 202 ? 10.238 28.890  12.419  1.00 15.05  ? 197 THR A CA  1 
ATOM   1582 C  C   . THR A 1 202 ? 9.012  28.637  11.555  1.00 15.17  ? 197 THR A C   1 
ATOM   1583 O  O   . THR A 1 202 ? 8.856  29.249  10.506  1.00 17.25  ? 197 THR A O   1 
ATOM   1584 C  CB  . THR A 1 202 ? 11.229 27.730  12.259  1.00 14.68  ? 197 THR A CB  1 
ATOM   1585 O  OG1 . THR A 1 202 ? 12.377 28.014  13.108  1.00 13.88  ? 197 THR A OG1 1 
ATOM   1586 C  CG2 . THR A 1 202 ? 11.662 27.576  10.787  1.00 15.79  ? 197 THR A CG2 1 
ATOM   1587 N  N   . PHE A 1 203 ? 8.151  27.729  12.007  1.00 14.25  ? 198 PHE A N   1 
ATOM   1588 C  CA  . PHE A 1 203 ? 6.947  27.392  11.252  1.00 16.19  ? 198 PHE A CA  1 
ATOM   1589 C  C   . PHE A 1 203 ? 6.055  28.608  11.052  1.00 18.10  ? 198 PHE A C   1 
ATOM   1590 O  O   . PHE A 1 203 ? 5.643  28.888  9.920   1.00 17.90  ? 198 PHE A O   1 
ATOM   1591 C  CB  . PHE A 1 203 ? 6.172  26.291  11.953  1.00 16.86  ? 198 PHE A CB  1 
ATOM   1592 C  CG  . PHE A 1 203 ? 4.955  25.797  11.188  1.00 17.89  ? 198 PHE A CG  1 
ATOM   1593 C  CD1 . PHE A 1 203 ? 3.729  26.453  11.298  1.00 19.25  ? 198 PHE A CD1 1 
ATOM   1594 C  CD2 . PHE A 1 203 ? 5.051  24.747  10.302  1.00 19.96  ? 198 PHE A CD2 1 
ATOM   1595 C  CE1 . PHE A 1 203 ? 2.626  25.996  10.600  1.00 20.52  ? 198 PHE A CE1 1 
ATOM   1596 C  CE2 . PHE A 1 203 ? 3.948  24.294  9.604   1.00 21.01  ? 198 PHE A CE2 1 
ATOM   1597 C  CZ  . PHE A 1 203 ? 2.729  24.909  9.774   1.00 22.66  ? 198 PHE A CZ  1 
ATOM   1598 N  N   . ASP A 1 204 ? 5.828  29.332  12.142  1.00 17.49  ? 199 ASP A N   1 
ATOM   1599 C  CA  . ASP A 1 204 ? 4.898  30.460  12.113  1.00 19.21  ? 199 ASP A CA  1 
ATOM   1600 C  C   . ASP A 1 204 ? 5.406  31.601  11.230  1.00 16.73  ? 199 ASP A C   1 
ATOM   1601 O  O   . ASP A 1 204 ? 4.654  32.205  10.469  1.00 19.57  ? 199 ASP A O   1 
ATOM   1602 C  CB  . ASP A 1 204 ? 4.567  30.901  13.561  1.00 20.71  ? 199 ASP A CB  1 
ATOM   1603 C  CG  . ASP A 1 204 ? 3.718  29.916  14.374  1.00 24.27  ? 199 ASP A CG  1 
ATOM   1604 O  OD1 . ASP A 1 204 ? 3.110  29.003  13.771  1.00 31.74  ? 199 ASP A OD1 1 
ATOM   1605 O  OD2 . ASP A 1 204 ? 3.708  30.024  15.615  1.00 29.99  ? 199 ASP A OD2 1 
ATOM   1606 N  N   . GLU A 1 205 ? 6.693  31.893  11.270  1.00 15.23  ? 200 GLU A N   1 
ATOM   1607 C  CA  . GLU A 1 205 ? 7.251  32.970  10.477  1.00 17.39  ? 200 GLU A CA  1 
ATOM   1608 C  C   . GLU A 1 205 ? 7.288  32.571  9.003   1.00 18.25  ? 200 GLU A C   1 
ATOM   1609 O  O   . GLU A 1 205 ? 7.148  33.424  8.130   1.00 18.63  ? 200 GLU A O   1 
ATOM   1610 C  CB  . GLU A 1 205 ? 8.638  33.382  10.929  1.00 20.66  ? 200 GLU A CB  1 
ATOM   1611 C  CG  . GLU A 1 205 ? 8.768  33.999  12.314  1.00 26.36  ? 200 GLU A CG  1 
ATOM   1612 C  CD  . GLU A 1 205 ? 10.069 34.803  12.397  1.00 36.70  ? 200 GLU A CD  1 
ATOM   1613 O  OE1 . GLU A 1 205 ? 10.055 36.018  12.064  1.00 45.40  ? 200 GLU A OE1 1 
ATOM   1614 O  OE2 . GLU A 1 205 ? 11.125 34.180  12.662  1.00 35.23  ? 200 GLU A OE2 1 
ATOM   1615 N  N   . ALA A 1 206 ? 7.483  31.288  8.722   1.00 17.32  ? 201 ALA A N   1 
ATOM   1616 C  CA  . ALA A 1 206 ? 7.438  30.853  7.331   1.00 17.81  ? 201 ALA A CA  1 
ATOM   1617 C  C   . ALA A 1 206 ? 6.004  30.949  6.785   1.00 17.31  ? 201 ALA A C   1 
ATOM   1618 O  O   . ALA A 1 206 ? 5.773  31.412  5.673   1.00 18.12  ? 201 ALA A O   1 
ATOM   1619 C  CB  . ALA A 1 206 ? 7.984  29.425  7.196   1.00 18.25  ? 201 ALA A CB  1 
ATOM   1620 N  N   . MET A 1 207 ? 5.046  30.499  7.585   1.00 17.97  ? 202 MET A N   1 
ATOM   1621 C  CA  . MET A 1 207 ? 3.638  30.540  7.210   1.00 20.61  ? 202 MET A CA  1 
ATOM   1622 C  C   . MET A 1 207 ? 3.227  31.934  6.733   1.00 18.17  ? 202 MET A C   1 
ATOM   1623 O  O   . MET A 1 207 ? 2.561  32.114  5.704   1.00 18.43  ? 202 MET A O   1 
ATOM   1624 C  CB  . MET A 1 207 ? 2.825  30.083  8.438   1.00 22.39  ? 202 MET A CB  1 
ATOM   1625 C  CG  . MET A 1 207 ? 1.361  30.134  8.249   1.00 31.52  ? 202 MET A CG  1 
ATOM   1626 S  SD  . MET A 1 207 ? 0.785  28.947  6.979   1.00 43.60  ? 202 MET A SD  1 
ATOM   1627 C  CE  . MET A 1 207 ? 1.533  27.608  7.467   1.00 25.13  ? 202 MET A CE  1 
ATOM   1628 N  N   . ALA A 1 208 ? 3.666  32.930  7.470   1.00 16.89  ? 203 ALA A N   1 
ATOM   1629 C  CA  . ALA A 1 208 ? 3.343  34.313  7.184   1.00 17.51  ? 203 ALA A CA  1 
ATOM   1630 C  C   . ALA A 1 208 ? 4.037  34.914  5.968   1.00 18.31  ? 203 ALA A C   1 
ATOM   1631 O  O   . ALA A 1 208 ? 3.635  35.999  5.549   1.00 19.53  ? 203 ALA A O   1 
ATOM   1632 C  CB  . ALA A 1 208 ? 3.602  35.189  8.397   1.00 19.83  ? 203 ALA A CB  1 
ATOM   1633 N  N   . ASP A 1 209 ? 5.026  34.207  5.394   1.00 17.62  ? 204 ASP A N   1 
ATOM   1634 C  CA  . ASP A 1 209 ? 5.759  34.669  4.224   1.00 21.33  ? 204 ASP A CA  1 
ATOM   1635 C  C   . ASP A 1 209 ? 5.440  33.868  2.950   1.00 19.44  ? 204 ASP A C   1 
ATOM   1636 O  O   . ASP A 1 209 ? 5.912  34.222  1.858   1.00 20.91  ? 204 ASP A O   1 
ATOM   1637 C  CB  . ASP A 1 209 ? 7.299  34.657  4.528   1.00 25.68  ? 204 ASP A CB  1 
ATOM   1638 C  CG  . ASP A 1 209 ? 8.237  35.305  3.504   1.00 28.81  ? 204 ASP A CG  1 
ATOM   1639 O  OD1 . ASP A 1 209 ? 8.062  36.504  3.223   1.00 31.02  ? 204 ASP A OD1 1 
ATOM   1640 O  OD2 . ASP A 1 209 ? 9.227  34.594  3.018   1.00 32.73  ? 204 ASP A OD2 1 
ATOM   1641 N  N   . LEU A 1 210 ? 4.593  32.842  3.074   1.00 17.97  ? 205 LEU A N   1 
ATOM   1642 C  CA  . LEU A 1 210 ? 4.254  31.994  1.955   1.00 19.59  ? 205 LEU A CA  1 
ATOM   1643 C  C   . LEU A 1 210 ? 3.632  32.795  0.814   1.00 20.05  ? 205 LEU A C   1 
ATOM   1644 O  O   . LEU A 1 210 ? 3.829  32.455  -0.344  1.00 20.04  ? 205 LEU A O   1 
ATOM   1645 C  CB  . LEU A 1 210 ? 3.310  30.881  2.331   1.00 18.17  ? 205 LEU A CB  1 
ATOM   1646 C  CG  . LEU A 1 210 ? 3.950  29.768  3.175   1.00 19.45  ? 205 LEU A CG  1 
ATOM   1647 C  CD1 . LEU A 1 210 ? 2.948  28.818  3.533   1.00 19.74  ? 205 LEU A CD1 1 
ATOM   1648 C  CD2 . LEU A 1 210 ? 5.124  29.094  2.396   1.00 19.48  ? 205 LEU A CD2 1 
ATOM   1649 N  N   . HIS A 1 211 ? 2.899  33.853  1.157   1.00 20.27  ? 206 HIS A N   1 
ATOM   1650 C  CA  . HIS A 1 211 ? 2.155  34.608  0.161   1.00 21.29  ? 206 HIS A CA  1 
ATOM   1651 C  C   . HIS A 1 211 ? 3.080  35.258  -0.876  1.00 25.32  ? 206 HIS A C   1 
ATOM   1652 O  O   . HIS A 1 211 ? 2.617  35.660  -1.939  1.00 24.22  ? 206 HIS A O   1 
ATOM   1653 C  CB  . HIS A 1 211 ? 1.265  35.680  0.837   1.00 20.92  ? 206 HIS A CB  1 
ATOM   1654 C  CG  . HIS A 1 211 ? 2.021  36.817  1.459   1.00 22.23  ? 206 HIS A CG  1 
ATOM   1655 N  ND1 . HIS A 1 211 ? 2.252  38.006  0.778   1.00 24.21  ? 206 HIS A ND1 1 
ATOM   1656 C  CD2 . HIS A 1 211 ? 2.630  36.893  2.662   1.00 22.41  ? 206 HIS A CD2 1 
ATOM   1657 C  CE1 . HIS A 1 211 ? 2.963  38.761  1.595   1.00 22.97  ? 206 HIS A CE1 1 
ATOM   1658 N  NE2 . HIS A 1 211 ? 3.227  38.130  2.728   1.00 24.83  ? 206 HIS A NE2 1 
ATOM   1659 N  N   . THR A 1 212 ? 4.378  35.404  -0.549  1.00 23.94  ? 207 THR A N   1 
ATOM   1660 C  CA  . THR A 1 212 ? 5.318  36.094  -1.420  1.00 24.11  ? 207 THR A CA  1 
ATOM   1661 C  C   . THR A 1 212 ? 5.875  35.218  -2.533  1.00 22.30  ? 207 THR A C   1 
ATOM   1662 O  O   . THR A 1 212 ? 6.570  35.740  -3.406  1.00 22.58  ? 207 THR A O   1 
ATOM   1663 C  CB  . THR A 1 212 ? 6.524  36.635  -0.630  1.00 22.94  ? 207 THR A CB  1 
ATOM   1664 O  OG1 . THR A 1 212 ? 7.208  35.506  -0.096  1.00 20.51  ? 207 THR A OG1 1 
ATOM   1665 C  CG2 . THR A 1 212 ? 6.125  37.597  0.437   1.00 23.26  ? 207 THR A CG2 1 
ATOM   1666 N  N   . LEU A 1 213 ? 5.564  33.918  -2.477  1.00 24.13  ? 208 LEU A N   1 
ATOM   1667 C  CA  . LEU A 1 213 ? 6.245  32.900  -3.256  1.00 24.65  ? 208 LEU A CA  1 
ATOM   1668 C  C   . LEU A 1 213 ? 5.475  32.501  -4.513  1.00 28.24  ? 208 LEU A C   1 
ATOM   1669 O  O   . LEU A 1 213 ? 4.242  32.510  -4.532  1.00 24.84  ? 208 LEU A O   1 
ATOM   1670 C  CB  . LEU A 1 213 ? 6.427  31.638  -2.406  1.00 25.05  ? 208 LEU A CB  1 
ATOM   1671 C  CG  . LEU A 1 213 ? 7.227  31.840  -1.139  1.00 23.79  ? 208 LEU A CG  1 
ATOM   1672 C  CD1 . LEU A 1 213 ? 7.454  30.542  -0.472  1.00 23.88  ? 208 LEU A CD1 1 
ATOM   1673 C  CD2 . LEU A 1 213 ? 8.593  32.575  -1.388  1.00 26.54  ? 208 LEU A CD2 1 
ATOM   1674 N  N   . SER A 1 214 ? 6.248  32.140  -5.544  1.00 25.32  ? 209 SER A N   1 
ATOM   1675 C  CA  . SER A 1 214 ? 5.743  31.394  -6.676  1.00 28.64  ? 209 SER A CA  1 
ATOM   1676 C  C   . SER A 1 214 ? 5.314  29.993  -6.261  1.00 31.74  ? 209 SER A C   1 
ATOM   1677 O  O   . SER A 1 214 ? 5.781  29.466  -5.249  1.00 30.19  ? 209 SER A O   1 
ATOM   1678 C  CB  . SER A 1 214 ? 6.822  31.280  -7.757  1.00 26.80  ? 209 SER A CB  1 
ATOM   1679 O  OG  . SER A 1 214 ? 7.814  30.372  -7.296  1.00 28.18  ? 209 SER A OG  1 
ATOM   1680 N  N   . GLU A 1 215 ? 4.484  29.376  -7.113  1.00 32.68  ? 210 GLU A N   1 
ATOM   1681 C  CA  . GLU A 1 215 ? 4.038  28.011  -6.901  1.00 36.30  ? 210 GLU A CA  1 
ATOM   1682 C  C   . GLU A 1 215 ? 5.199  27.038  -6.657  1.00 37.61  ? 210 GLU A C   1 
ATOM   1683 O  O   . GLU A 1 215 ? 5.114  26.187  -5.772  1.00 36.97  ? 210 GLU A O   1 
ATOM   1684 C  CB  . GLU A 1 215 ? 3.197  27.596  -8.093  1.00 41.84  ? 210 GLU A CB  1 
ATOM   1685 C  CG  . GLU A 1 215 ? 2.487  26.274  -7.919  1.00 46.92  ? 210 GLU A CG  1 
ATOM   1686 C  CD  . GLU A 1 215 ? 1.585  25.971  -9.094  1.00 52.68  ? 210 GLU A CD  1 
ATOM   1687 O  OE1 . GLU A 1 215 ? 1.245  26.916  -9.847  1.00 57.90  ? 210 GLU A OE1 1 
ATOM   1688 O  OE2 . GLU A 1 215 ? 1.242  24.785  -9.280  1.00 56.35  ? 210 GLU A OE2 1 
ATOM   1689 N  N   . ASP A 1 216 ? 6.305  27.175  -7.400  1.00 34.03  ? 211 ASP A N   1 
ATOM   1690 C  CA  . ASP A 1 216 ? 7.428  26.270  -7.201  1.00 34.93  ? 211 ASP A CA  1 
ATOM   1691 C  C   . ASP A 1 216 ? 8.180  26.495  -5.888  1.00 34.26  ? 211 ASP A C   1 
ATOM   1692 O  O   . ASP A 1 216 ? 8.556  25.523  -5.238  1.00 36.08  ? 211 ASP A O   1 
ATOM   1693 C  CB  . ASP A 1 216 ? 8.427  26.329  -8.363  1.00 39.33  ? 211 ASP A CB  1 
ATOM   1694 C  CG  . ASP A 1 216 ? 8.002  25.585  -9.648  1.00 48.23  ? 211 ASP A CG  1 
ATOM   1695 O  OD1 . ASP A 1 216 ? 6.784  25.243  -9.787  1.00 47.48  ? 211 ASP A OD1 1 
ATOM   1696 O  OD2 . ASP A 1 216 ? 8.881  25.324  -10.498 1.00 55.18  ? 211 ASP A OD2 1 
ATOM   1697 N  N   . SER A 1 217 ? 8.392  27.764  -5.491  1.00 32.65  ? 212 SER A N   1 
ATOM   1698 C  CA  . SER A 1 217 ? 9.090  28.065  -4.249  1.00 28.18  ? 212 SER A CA  1 
ATOM   1699 C  C   . SER A 1 217 ? 8.216  27.691  -3.044  1.00 29.28  ? 212 SER A C   1 
ATOM   1700 O  O   . SER A 1 217 ? 8.690  27.187  -2.010  1.00 24.63  ? 212 SER A O   1 
ATOM   1701 C  CB  . SER A 1 217 ? 9.502  29.524  -4.197  1.00 29.39  ? 212 SER A CB  1 
ATOM   1702 O  OG  . SER A 1 217 ? 10.220 29.854  -5.374  1.00 30.42  ? 212 SER A OG  1 
ATOM   1703 N  N   . TYR A 1 218 ? 6.910  27.884  -3.226  1.00 26.90  ? 213 TYR A N   1 
ATOM   1704 C  CA  . TYR A 1 218 ? 5.942  27.442  -2.239  1.00 25.26  ? 213 TYR A CA  1 
ATOM   1705 C  C   . TYR A 1 218 ? 6.018  25.944  -1.976  1.00 26.75  ? 213 TYR A C   1 
ATOM   1706 O  O   . TYR A 1 218 ? 5.958  25.508  -0.819  1.00 25.44  ? 213 TYR A O   1 
ATOM   1707 C  CB  . TYR A 1 218 ? 4.565  27.851  -2.702  1.00 23.80  ? 213 TYR A CB  1 
ATOM   1708 C  CG  . TYR A 1 218 ? 3.410  27.340  -1.884  1.00 24.76  ? 213 TYR A CG  1 
ATOM   1709 C  CD1 . TYR A 1 218 ? 2.911  26.050  -2.073  1.00 29.46  ? 213 TYR A CD1 1 
ATOM   1710 C  CD2 . TYR A 1 218 ? 2.740  28.174  -1.006  1.00 26.39  ? 213 TYR A CD2 1 
ATOM   1711 C  CE1 . TYR A 1 218 ? 1.817  25.588  -1.358  1.00 28.65  ? 213 TYR A CE1 1 
ATOM   1712 C  CE2 . TYR A 1 218 ? 1.634  27.720  -0.281  1.00 28.20  ? 213 TYR A CE2 1 
ATOM   1713 C  CZ  . TYR A 1 218 ? 1.178  26.438  -0.474  1.00 29.05  ? 213 TYR A CZ  1 
ATOM   1714 O  OH  . TYR A 1 218 ? 0.108  26.012  0.239   1.00 37.10  ? 213 TYR A OH  1 
ATOM   1715 N  N   . LYS A 1 219 ? 6.140  25.152  -3.051  1.00 27.24  ? 214 LYS A N   1 
ATOM   1716 C  CA  . LYS A 1 219 ? 6.276  23.713  -2.888  1.00 30.74  ? 214 LYS A CA  1 
ATOM   1717 C  C   . LYS A 1 219 ? 7.472  23.359  -2.016  1.00 29.29  ? 214 LYS A C   1 
ATOM   1718 O  O   . LYS A 1 219 ? 7.351  22.548  -1.096  1.00 30.32  ? 214 LYS A O   1 
ATOM   1719 C  CB  . LYS A 1 219 ? 6.396  23.048  -4.277  1.00 37.51  ? 214 LYS A CB  1 
ATOM   1720 C  CG  . LYS A 1 219 ? 6.494  21.535  -4.204  1.00 45.43  ? 214 LYS A CG  1 
ATOM   1721 C  CD  . LYS A 1 219 ? 6.482  20.877  -5.591  1.00 47.74  ? 214 LYS A CD  1 
ATOM   1722 C  CE  . LYS A 1 219 ? 6.143  19.405  -5.504  1.00 53.28  ? 214 LYS A CE  1 
ATOM   1723 N  NZ  . LYS A 1 219 ? 4.740  19.209  -5.024  1.00 55.38  ? 214 LYS A NZ  1 
ATOM   1724 N  N   . ASP A 1 220 ? 8.626  23.984  -2.304  1.00 28.67  ? 215 ASP A N   1 
ATOM   1725 C  CA  . ASP A 1 220 ? 9.846  23.706  -1.555  1.00 29.33  ? 215 ASP A CA  1 
ATOM   1726 C  C   . ASP A 1 220 ? 9.752  24.070  -0.072  1.00 27.14  ? 215 ASP A C   1 
ATOM   1727 O  O   . ASP A 1 220 ? 10.092 23.294  0.795   1.00 23.29  ? 215 ASP A O   1 
ATOM   1728 C  CB  . ASP A 1 220 ? 11.036 24.452  -2.153  1.00 34.47  ? 215 ASP A CB  1 
ATOM   1729 C  CG  . ASP A 1 220 ? 11.334 24.070  -3.605  1.00 43.50  ? 215 ASP A CG  1 
ATOM   1730 O  OD1 . ASP A 1 220 ? 11.238 22.875  -3.934  1.00 39.69  ? 215 ASP A OD1 1 
ATOM   1731 O  OD2 . ASP A 1 220 ? 11.673 24.976  -4.395  1.00 51.57  ? 215 ASP A OD2 1 
ATOM   1732 N  N   . SER A 1 221 ? 9.309  25.289  0.224   1.00 25.59  ? 216 SER A N   1 
ATOM   1733 C  CA  . SER A 1 221 ? 9.170  25.705  1.613   1.00 23.54  ? 216 SER A CA  1 
ATOM   1734 C  C   . SER A 1 221 ? 8.195  24.809  2.406   1.00 23.58  ? 216 SER A C   1 
ATOM   1735 O  O   . SER A 1 221 ? 8.460  24.399  3.544   1.00 20.73  ? 216 SER A O   1 
ATOM   1736 C  CB  . SER A 1 221 ? 8.742  27.174  1.624   1.00 23.38  ? 216 SER A CB  1 
ATOM   1737 O  OG  . SER A 1 221 ? 9.745  27.999  1.050   1.00 24.59  ? 216 SER A OG  1 
ATOM   1738 N  N   . THR A 1 222 ? 7.021  24.490  1.827   1.00 21.20  ? 217 THR A N   1 
ATOM   1739 C  CA  . THR A 1 222 ? 6.005  23.765  2.582   1.00 21.46  ? 217 THR A CA  1 
ATOM   1740 C  C   . THR A 1 222 ? 6.400  22.316  2.869   1.00 21.88  ? 217 THR A C   1 
ATOM   1741 O  O   . THR A 1 222 ? 6.018  21.713  3.870   1.00 22.56  ? 217 THR A O   1 
ATOM   1742 C  CB  . THR A 1 222 ? 4.645  23.782  1.885   1.00 23.48  ? 217 THR A CB  1 
ATOM   1743 O  OG1 . THR A 1 222 ? 4.757  23.236  0.554   1.00 25.49  ? 217 THR A OG1 1 
ATOM   1744 C  CG2 . THR A 1 222 ? 4.045  25.173  1.861   1.00 24.57  ? 217 THR A CG2 1 
ATOM   1745 N  N   . LEU A 1 223 ? 7.229  21.753  1.993   1.00 26.08  ? 218 LEU A N   1 
ATOM   1746 C  CA  . LEU A 1 223 ? 7.841  20.472  2.311   1.00 27.74  ? 218 LEU A CA  1 
ATOM   1747 C  C   . LEU A 1 223 ? 8.554  20.472  3.666   1.00 25.35  ? 218 LEU A C   1 
ATOM   1748 O  O   . LEU A 1 223 ? 8.303  19.630  4.519   1.00 23.84  ? 218 LEU A O   1 
ATOM   1749 C  CB  . LEU A 1 223 ? 8.849  20.103  1.192   1.00 31.05  ? 218 LEU A CB  1 
ATOM   1750 C  CG  . LEU A 1 223 ? 9.287  18.625  1.093   1.00 41.07  ? 218 LEU A CG  1 
ATOM   1751 C  CD1 . LEU A 1 223 ? 10.344 18.423  -0.047  1.00 44.20  ? 218 LEU A CD1 1 
ATOM   1752 C  CD2 . LEU A 1 223 ? 9.848  18.084  2.393   1.00 45.72  ? 218 LEU A CD2 1 
ATOM   1753 N  N   . ILE A 1 224 ? 9.460  21.421  3.886   1.00 23.51  ? 219 ILE A N   1 
ATOM   1754 C  CA  . ILE A 1 224 ? 10.196 21.430  5.141   1.00 22.67  ? 219 ILE A CA  1 
ATOM   1755 C  C   . ILE A 1 224 ? 9.302  21.822  6.315   1.00 20.80  ? 219 ILE A C   1 
ATOM   1756 O  O   . ILE A 1 224 ? 9.453  21.342  7.416   1.00 19.53  ? 219 ILE A O   1 
ATOM   1757 C  CB  . ILE A 1 224 ? 11.423 22.356  5.035   1.00 23.50  ? 219 ILE A CB  1 
ATOM   1758 C  CG1 . ILE A 1 224 ? 12.293 22.040  3.815   1.00 27.67  ? 219 ILE A CG1 1 
ATOM   1759 C  CG2 . ILE A 1 224 ? 12.248 22.339  6.358   1.00 25.76  ? 219 ILE A CG2 1 
ATOM   1760 C  CD1 . ILE A 1 224 ? 12.794 20.688  3.863   1.00 32.27  ? 219 ILE A CD1 1 
ATOM   1761 N  N   . MET A 1 225 ? 8.314  22.699  6.062   1.00 20.85  ? 220 MET A N   1 
ATOM   1762 C  CA  . MET A 1 225 ? 7.423  23.128  7.120   1.00 17.61  ? 220 MET A CA  1 
ATOM   1763 C  C   . MET A 1 225 ? 6.674  21.933  7.668   1.00 18.99  ? 220 MET A C   1 
ATOM   1764 O  O   . MET A 1 225 ? 6.420  21.824  8.874   1.00 18.22  ? 220 MET A O   1 
ATOM   1765 C  CB  . MET A 1 225 ? 6.478  24.214  6.579   1.00 17.54  ? 220 MET A CB  1 
ATOM   1766 C  CG  . MET A 1 225 ? 7.149  25.491  6.356   1.00 17.48  ? 220 MET A CG  1 
ATOM   1767 S  SD  . MET A 1 225 ? 6.076  26.679  5.461   1.00 20.83  ? 220 MET A SD  1 
ATOM   1768 C  CE  . MET A 1 225 ? 4.882  26.989  6.667   1.00 20.66  ? 220 MET A CE  1 
ATOM   1769 N  N   . GLN A 1 226 ? 6.321  21.007  6.769   1.00 19.66  ? 221 GLN A N   1 
ATOM   1770 C  CA  . GLN A 1 226 ? 5.619  19.816  7.188   1.00 20.24  ? 221 GLN A CA  1 
ATOM   1771 C  C   . GLN A 1 226 ? 6.460  18.981  8.151   1.00 21.26  ? 221 GLN A C   1 
ATOM   1772 O  O   . GLN A 1 226 ? 5.933  18.407  9.115   1.00 20.11  ? 221 GLN A O   1 
ATOM   1773 C  CB  . GLN A 1 226 ? 5.183  18.996  5.947   1.00 25.34  ? 221 GLN A CB  1 
ATOM   1774 C  CG  . GLN A 1 226 ? 4.436  17.724  6.286   1.00 30.05  ? 221 GLN A CG  1 
ATOM   1775 C  CD  . GLN A 1 226 ? 3.145  18.022  6.993   1.00 35.54  ? 221 GLN A CD  1 
ATOM   1776 O  OE1 . GLN A 1 226 ? 2.309  18.750  6.450   1.00 43.56  ? 221 GLN A OE1 1 
ATOM   1777 N  NE2 . GLN A 1 226 ? 2.943  17.497  8.200   1.00 34.13  ? 221 GLN A NE2 1 
ATOM   1778 N  N   . LEU A 1 227 ? 7.777  18.956  7.920   1.00 20.27  ? 222 LEU A N   1 
ATOM   1779 C  CA  . LEU A 1 227 ? 8.639  18.212  8.833   1.00 20.91  ? 222 LEU A CA  1 
ATOM   1780 C  C   . LEU A 1 227 ? 8.742  18.857  10.217  1.00 20.21  ? 222 LEU A C   1 
ATOM   1781 O  O   . LEU A 1 227 ? 8.773  18.179  11.242  1.00 18.81  ? 222 LEU A O   1 
ATOM   1782 C  CB  . LEU A 1 227 ? 9.966  18.092  8.163   1.00 20.74  ? 222 LEU A CB  1 
ATOM   1783 C  CG  . LEU A 1 227 ? 9.977  17.401  6.778   1.00 23.21  ? 222 LEU A CG  1 
ATOM   1784 C  CD1 . LEU A 1 227 ? 11.371 17.282  6.251   1.00 23.53  ? 222 LEU A CD1 1 
ATOM   1785 C  CD2 . LEU A 1 227 ? 9.313  16.077  6.831   1.00 25.97  ? 222 LEU A CD2 1 
ATOM   1786 N  N   . LEU A 1 228 ? 8.763  20.198  10.270  1.00 19.53  ? 223 LEU A N   1 
ATOM   1787 C  CA  . LEU A 1 228 ? 8.696  20.898  11.541  1.00 19.05  ? 223 LEU A CA  1 
ATOM   1788 C  C   . LEU A 1 228 ? 7.428  20.491  12.271  1.00 19.34  ? 223 LEU A C   1 
ATOM   1789 O  O   . LEU A 1 228 ? 7.424  20.213  13.469  1.00 20.13  ? 223 LEU A O   1 
ATOM   1790 C  CB  . LEU A 1 228 ? 8.752  22.429  11.327  1.00 18.82  ? 223 LEU A CB  1 
ATOM   1791 C  CG  . LEU A 1 228 ? 10.037 22.994  10.783  1.00 17.78  ? 223 LEU A CG  1 
ATOM   1792 C  CD1 . LEU A 1 228 ? 9.773  24.346  10.203  1.00 19.06  ? 223 LEU A CD1 1 
ATOM   1793 C  CD2 . LEU A 1 228 ? 11.197 23.168  11.878  1.00 17.95  ? 223 LEU A CD2 1 
ATOM   1794 N  N   . ARG A 1 229 ? 6.315  20.476  11.537  1.00 20.22  ? 224 ARG A N   1 
ATOM   1795 C  CA  . ARG A 1 229 ? 5.054  20.119  12.145  1.00 21.44  ? 224 ARG A CA  1 
ATOM   1796 C  C   . ARG A 1 229 ? 5.068  18.661  12.619  1.00 20.47  ? 224 ARG A C   1 
ATOM   1797 O  O   . ARG A 1 229 ? 4.613  18.360  13.705  1.00 24.26  ? 224 ARG A O   1 
ATOM   1798 C  CB  . ARG A 1 229 ? 3.920  20.345  11.119  1.00 24.58  ? 224 ARG A CB  1 
ATOM   1799 C  CG  . ARG A 1 229 ? 2.525  19.934  11.593  1.00 31.83  ? 224 ARG A CG  1 
ATOM   1800 C  CD  . ARG A 1 229 ? 2.153  20.540  12.932  1.00 39.77  ? 224 ARG A CD  1 
ATOM   1801 N  NE  . ARG A 1 229 ? 1.948  21.985  12.870  1.00 43.85  ? 224 ARG A NE  1 
ATOM   1802 C  CZ  . ARG A 1 229 ? 2.014  22.811  13.921  1.00 50.79  ? 224 ARG A CZ  1 
ATOM   1803 N  NH1 . ARG A 1 229 ? 2.091  22.356  15.166  1.00 50.42  ? 224 ARG A NH1 1 
ATOM   1804 N  NH2 . ARG A 1 229 ? 2.010  24.126  13.715  1.00 53.97  ? 224 ARG A NH2 1 
ATOM   1805 N  N   . ASP A 1 230 ? 5.584  17.756  11.794  1.00 22.63  ? 225 ASP A N   1 
ATOM   1806 C  CA  . ASP A 1 230 ? 5.663  16.348  12.171  1.00 21.19  ? 225 ASP A CA  1 
ATOM   1807 C  C   . ASP A 1 230 ? 6.478  16.207  13.454  1.00 20.89  ? 225 ASP A C   1 
ATOM   1808 O  O   . ASP A 1 230 ? 6.101  15.472  14.350  1.00 21.80  ? 225 ASP A O   1 
ATOM   1809 C  CB  . ASP A 1 230 ? 6.332  15.548  11.102  1.00 22.56  ? 225 ASP A CB  1 
ATOM   1810 C  CG  . ASP A 1 230 ? 5.583  15.326  9.814   1.00 26.49  ? 225 ASP A CG  1 
ATOM   1811 O  OD1 . ASP A 1 230 ? 4.334  15.504  9.809   1.00 31.87  ? 225 ASP A OD1 1 
ATOM   1812 O  OD2 . ASP A 1 230 ? 6.252  14.982  8.796   1.00 30.51  ? 225 ASP A OD2 1 
ATOM   1813 N  N   . ASN A 1 231 ? 7.593  16.943  13.577  1.00 22.61  ? 226 ASN A N   1 
ATOM   1814 C  CA  . ASN A 1 231 ? 8.342  16.874  14.824  1.00 20.30  ? 226 ASN A CA  1 
ATOM   1815 C  C   . ASN A 1 231 ? 7.595  17.462  16.008  1.00 21.16  ? 226 ASN A C   1 
ATOM   1816 O  O   . ASN A 1 231 ? 7.608  16.931  17.115  1.00 21.50  ? 226 ASN A O   1 
ATOM   1817 C  CB  . ASN A 1 231 ? 9.698  17.550  14.714  1.00 18.36  ? 226 ASN A CB  1 
ATOM   1818 C  CG  . ASN A 1 231 ? 10.721 16.736  13.950  1.00 19.53  ? 226 ASN A CG  1 
ATOM   1819 O  OD1 . ASN A 1 231 ? 10.571 15.497  13.797  1.00 21.10  ? 226 ASN A OD1 1 
ATOM   1820 N  ND2 . ASN A 1 231 ? 11.751 17.421  13.445  1.00 18.15  ? 226 ASN A ND2 1 
ATOM   1821 N  N   . LEU A 1 232 ? 6.938  18.594  15.792  1.00 22.76  ? 227 LEU A N   1 
ATOM   1822 C  CA  . LEU A 1 232 ? 6.167  19.168  16.867  1.00 21.41  ? 227 LEU A CA  1 
ATOM   1823 C  C   . LEU A 1 232 ? 5.088  18.205  17.360  1.00 22.48  ? 227 LEU A C   1 
ATOM   1824 O  O   . LEU A 1 232 ? 4.881  18.150  18.565  1.00 24.31  ? 227 LEU A O   1 
ATOM   1825 C  CB  . LEU A 1 232 ? 5.559  20.481  16.427  1.00 21.40  ? 227 LEU A CB  1 
ATOM   1826 C  CG  . LEU A 1 232 ? 6.556  21.660  16.421  1.00 21.27  ? 227 LEU A CG  1 
ATOM   1827 C  CD1 . LEU A 1 232 ? 6.009  22.822  15.653  1.00 23.14  ? 227 LEU A CD1 1 
ATOM   1828 C  CD2 . LEU A 1 232 ? 6.893  22.093  17.817  1.00 20.47  ? 227 LEU A CD2 1 
ATOM   1829 N  N   . THR A 1 233 ? 4.479  17.436  16.443  1.00 25.25  ? 228 THR A N   1 
ATOM   1830 C  CA  . THR A 1 233 ? 3.472  16.445  16.830  1.00 30.14  ? 228 THR A CA  1 
ATOM   1831 C  C   . THR A 1 233 ? 4.127  15.344  17.673  1.00 33.31  ? 228 THR A C   1 
ATOM   1832 O  O   . THR A 1 233 ? 3.597  14.905  18.699  1.00 33.77  ? 228 THR A O   1 
ATOM   1833 C  CB  . THR A 1 233 ? 2.790  15.911  15.582  1.00 31.32  ? 228 THR A CB  1 
ATOM   1834 O  OG1 . THR A 1 233 ? 2.182  16.988  14.868  1.00 29.81  ? 228 THR A OG1 1 
ATOM   1835 C  CG2 . THR A 1 233 ? 1.731  14.839  15.896  1.00 35.68  ? 228 THR A CG2 1 
ATOM   1836 N  N   . LEU A 1 234 ? 5.317  14.925  17.235  1.00 26.90  ? 229 LEU A N   1 
ATOM   1837 C  CA  . LEU A 1 234 ? 6.092  13.916  17.927  1.00 29.78  ? 229 LEU A CA  1 
ATOM   1838 C  C   . LEU A 1 234 ? 6.491  14.405  19.310  1.00 28.58  ? 229 LEU A C   1 
ATOM   1839 O  O   . LEU A 1 234 ? 6.424  13.653  20.272  1.00 30.51  ? 229 LEU A O   1 
ATOM   1840 C  CB  . LEU A 1 234 ? 7.354  13.578  17.132  1.00 31.77  ? 229 LEU A CB  1 
ATOM   1841 C  CG  . LEU A 1 234 ? 8.262  12.511  17.760  1.00 32.88  ? 229 LEU A CG  1 
ATOM   1842 C  CD1 . LEU A 1 234 ? 7.531  11.142  17.849  1.00 36.05  ? 229 LEU A CD1 1 
ATOM   1843 C  CD2 . LEU A 1 234 ? 9.526  12.348  16.964  1.00 34.59  ? 229 LEU A CD2 1 
ATOM   1844 N  N   . TRP A 1 235 ? 6.879  15.676  19.414  1.00 26.54  ? 230 TRP A N   1 
ATOM   1845 C  CA  . TRP A 1 235 ? 7.436  16.213  20.643  1.00 23.96  ? 230 TRP A CA  1 
ATOM   1846 C  C   . TRP A 1 235 ? 6.425  16.686  21.679  1.00 29.61  ? 230 TRP A C   1 
ATOM   1847 O  O   . TRP A 1 235 ? 6.796  16.915  22.821  1.00 26.68  ? 230 TRP A O   1 
ATOM   1848 C  CB  . TRP A 1 235 ? 8.360  17.387  20.330  1.00 24.27  ? 230 TRP A CB  1 
ATOM   1849 C  CG  . TRP A 1 235 ? 9.554  17.018  19.512  1.00 22.20  ? 230 TRP A CG  1 
ATOM   1850 C  CD1 . TRP A 1 235 ? 10.045 15.774  19.282  1.00 22.61  ? 230 TRP A CD1 1 
ATOM   1851 C  CD2 . TRP A 1 235 ? 10.370 17.928  18.742  1.00 20.51  ? 230 TRP A CD2 1 
ATOM   1852 N  NE1 . TRP A 1 235 ? 11.141 15.844  18.447  1.00 20.81  ? 230 TRP A NE1 1 
ATOM   1853 C  CE2 . TRP A 1 235 ? 11.360 17.158  18.101  1.00 19.45  ? 230 TRP A CE2 1 
ATOM   1854 C  CE3 . TRP A 1 235 ? 10.345 19.321  18.533  1.00 21.01  ? 230 TRP A CE3 1 
ATOM   1855 C  CZ2 . TRP A 1 235 ? 12.341 17.739  17.281  1.00 20.66  ? 230 TRP A CZ2 1 
ATOM   1856 C  CZ3 . TRP A 1 235 ? 11.320 19.895  17.730  1.00 18.95  ? 230 TRP A CZ3 1 
ATOM   1857 C  CH2 . TRP A 1 235 ? 12.306 19.107  17.126  1.00 19.93  ? 230 TRP A CH2 1 
ATOM   1858 N  N   . THR A 1 236 ? 5.169  16.868  21.266  1.00 34.39  ? 231 THR A N   1 
ATOM   1859 C  CA  . THR A 1 236 ? 4.133  17.330  22.174  1.00 40.85  ? 231 THR A CA  1 
ATOM   1860 C  C   . THR A 1 236 ? 2.920  16.379  22.191  1.00 43.74  ? 231 THR A C   1 
ATOM   1861 O  O   . THR A 1 236 ? 1.917  16.718  22.810  1.00 47.50  ? 231 THR A O   1 
ATOM   1862 C  CB  . THR A 1 236 ? 3.724  18.782  21.824  1.00 40.02  ? 231 THR A CB  1 
ATOM   1863 O  OG1 . THR A 1 236 ? 3.206  18.832  20.493  1.00 40.51  ? 231 THR A OG1 1 
ATOM   1864 C  CG2 . THR A 1 236 ? 4.869  19.725  21.928  1.00 40.69  ? 231 THR A CG2 1 
ATOM   1865 O  OXT . THR A 1 236 ? 2.929  15.293  21.597  1.00 48.51  ? 231 THR A OXT 1 
ATOM   1866 N  N   . GLN B 2 1   ? 10.433 6.903   18.795  1.00 53.88  ? 255 GLN P N   1 
ATOM   1867 C  CA  . GLN B 2 1   ? 10.640 7.299   17.405  1.00 50.69  ? 255 GLN P CA  1 
ATOM   1868 C  C   . GLN B 2 1   ? 11.557 8.517   17.318  1.00 42.58  ? 255 GLN P C   1 
ATOM   1869 O  O   . GLN B 2 1   ? 11.364 9.483   18.047  1.00 49.15  ? 255 GLN P O   1 
ATOM   1870 C  CB  . GLN B 2 1   ? 9.310  7.638   16.752  1.00 49.27  ? 255 GLN P CB  1 
ATOM   1871 C  CG  . GLN B 2 1   ? 9.435  7.853   15.277  1.00 50.18  ? 255 GLN P CG  1 
ATOM   1872 C  CD  . GLN B 2 1   ? 8.078  8.071   14.686  1.00 53.80  ? 255 GLN P CD  1 
ATOM   1873 O  OE1 . GLN B 2 1   ? 7.273  7.145   14.598  1.00 61.27  ? 255 GLN P OE1 1 
ATOM   1874 N  NE2 . GLN B 2 1   ? 7.788  9.289   14.262  1.00 52.56  ? 255 GLN P NE2 1 
ATOM   1875 N  N   . ARG B 2 2   ? 12.519 8.480   16.393  1.00 38.51  ? 256 ARG P N   1 
ATOM   1876 C  CA  . ARG B 2 2   ? 13.468 9.574   16.245  1.00 36.88  ? 256 ARG P CA  1 
ATOM   1877 C  C   . ARG B 2 2   ? 12.919 10.751  15.446  1.00 31.59  ? 256 ARG P C   1 
ATOM   1878 O  O   . ARG B 2 2   ? 12.171 10.607  14.490  1.00 28.73  ? 256 ARG P O   1 
ATOM   1879 C  CB  . ARG B 2 2   ? 14.738 9.153   15.551  1.00 37.28  ? 256 ARG P CB  1 
ATOM   1880 C  CG  . ARG B 2 2   ? 15.717 8.478   16.435  1.00 43.18  ? 256 ARG P CG  1 
ATOM   1881 C  CD  . ARG B 2 2   ? 16.876 8.022   15.601  1.00 44.71  ? 256 ARG P CD  1 
ATOM   1882 N  NE  . ARG B 2 2   ? 17.422 6.790   16.146  1.00 50.81  ? 256 ARG P NE  1 
ATOM   1883 C  CZ  . ARG B 2 2   ? 18.178 6.723   17.231  1.00 46.26  ? 256 ARG P CZ  1 
ATOM   1884 N  NH1 . ARG B 2 2   ? 18.843 7.780   17.677  1.00 44.29  ? 256 ARG P NH1 1 
ATOM   1885 N  NH2 . ARG B 2 2   ? 18.308 5.558   17.859  1.00 47.83  ? 256 ARG P NH2 1 
ATOM   1886 N  N   . SER B 2 3   ? 13.378 11.932  15.821  1.00 29.39  ? 257 SER P N   1 
ATOM   1887 C  CA  . SER B 2 3   ? 13.026 13.143  15.110  1.00 24.92  ? 257 SER P CA  1 
ATOM   1888 C  C   . SER B 2 3   ? 13.471 13.105  13.653  1.00 25.39  ? 257 SER P C   1 
ATOM   1889 O  O   . SER B 2 3   ? 14.500 12.517  13.320  1.00 25.16  ? 257 SER P O   1 
ATOM   1890 C  CB  . SER B 2 3   ? 13.678 14.307  15.839  1.00 22.62  ? 257 SER P CB  1 
ATOM   1891 O  OG  . SER B 2 3   ? 13.330 14.331  17.210  1.00 21.86  ? 257 SER P OG  1 
ATOM   1892 N  N   . THR B 2 4   ? 12.691 13.765  12.787  1.00 20.46  ? 258 THR P N   1 
ATOM   1893 C  CA  . THR B 2 4   ? 13.014 13.900  11.388  1.00 20.92  ? 258 THR P CA  1 
ATOM   1894 C  C   . THR B 2 4   ? 13.875 15.126  11.134  1.00 18.70  ? 258 THR P C   1 
ATOM   1895 O  O   . THR B 2 4   ? 13.512 16.248  11.501  1.00 20.00  ? 258 THR P O   1 
ATOM   1896 C  CB  . THR B 2 4   ? 11.765 14.028  10.510  1.00 21.87  ? 258 THR P CB  1 
ATOM   1897 O  OG1 . THR B 2 4   ? 10.849 13.046  10.878  1.00 25.21  ? 258 THR P OG1 1 
ATOM   1898 C  CG2 . THR B 2 4   ? 12.121 13.937  9.056   1.00 22.59  ? 258 THR P CG2 1 
HETATM 1899 N  N   . SEP B 2 5   ? 15.023 14.892  10.486  1.00 18.98  ? 259 SEP P N   1 
HETATM 1900 C  CA  . SEP B 2 5   ? 15.877 15.962  10.021  1.00 17.50  ? 259 SEP P CA  1 
HETATM 1901 C  CB  . SEP B 2 5   ? 17.334 15.642  10.376  1.00 18.33  ? 259 SEP P CB  1 
HETATM 1902 O  OG  . SEP B 2 5   ? 17.720 14.458  9.673   1.00 16.57  ? 259 SEP P OG  1 
HETATM 1903 C  C   . SEP B 2 5   ? 15.651 16.181  8.526   1.00 17.36  ? 259 SEP P C   1 
HETATM 1904 O  O   . SEP B 2 5   ? 14.847 15.479  7.879   1.00 19.42  ? 259 SEP P O   1 
HETATM 1905 P  P   . SEP B 2 5   ? 19.170 13.847  10.060  1.00 16.19  ? 259 SEP P P   1 
HETATM 1906 O  O1P . SEP B 2 5   ? 19.248 12.655  9.098   1.00 16.12  ? 259 SEP P O1P 1 
HETATM 1907 O  O2P . SEP B 2 5   ? 20.176 14.909  9.754   1.00 15.34  ? 259 SEP P O2P 1 
HETATM 1908 O  O3P . SEP B 2 5   ? 19.164 13.465  11.516  1.00 15.12  ? 259 SEP P O3P 1 
ATOM   1909 N  N   . THR B 2 6   ? 16.404 17.103  7.934   1.00 17.14  ? 260 THR P N   1 
ATOM   1910 C  CA  A THR B 2 6   ? 16.192 17.519  6.557   0.50 18.58  ? 260 THR P CA  1 
ATOM   1911 C  CA  B THR B 2 6   ? 16.146 17.496  6.559   0.50 20.02  ? 260 THR P CA  1 
ATOM   1912 C  C   . THR B 2 6   ? 16.468 16.345  5.619   1.00 21.29  ? 260 THR P C   1 
ATOM   1913 O  O   . THR B 2 6   ? 17.514 15.713  5.715   1.00 20.35  ? 260 THR P O   1 
ATOM   1914 C  CB  A THR B 2 6   ? 17.090 18.735  6.258   0.50 18.96  ? 260 THR P CB  1 
ATOM   1915 C  CB  B THR B 2 6   ? 16.965 18.659  6.075   0.50 21.87  ? 260 THR P CB  1 
ATOM   1916 O  OG1 A THR B 2 6   ? 16.644 19.865  7.021   0.50 14.01  ? 260 THR P OG1 1 
ATOM   1917 O  OG1 B THR B 2 6   ? 16.592 18.941  4.716   0.50 26.21  ? 260 THR P OG1 1 
ATOM   1918 C  CG2 A THR B 2 6   ? 17.097 19.135  4.807   0.50 20.12  ? 260 THR P CG2 1 
ATOM   1919 C  CG2 B THR B 2 6   ? 18.418 18.390  6.120   0.50 20.24  ? 260 THR P CG2 1 
ATOM   1920 N  N   . PRO B 2 7   ? 15.586 16.049  4.654   1.00 22.09  ? 261 PRO P N   1 
ATOM   1921 C  CA  . PRO B 2 7   ? 15.838 14.942  3.734   1.00 24.94  ? 261 PRO P CA  1 
ATOM   1922 C  C   . PRO B 2 7   ? 16.735 15.326  2.564   1.00 24.30  ? 261 PRO P C   1 
ATOM   1923 O  O   . PRO B 2 7   ? 17.035 16.494  2.364   1.00 24.67  ? 261 PRO P O   1 
ATOM   1924 C  CB  . PRO B 2 7   ? 14.398 14.581  3.285   1.00 24.23  ? 261 PRO P CB  1 
ATOM   1925 C  CG  . PRO B 2 7   ? 13.707 15.894  3.218   1.00 25.57  ? 261 PRO P CG  1 
ATOM   1926 C  CD  . PRO B 2 7   ? 14.296 16.722  4.401   1.00 23.18  ? 261 PRO P CD  1 
ATOM   1927 N  N   . ASN B 2 8   ? 17.161 14.329  1.767   1.00 27.74  ? 262 ASN P N   1 
ATOM   1928 C  CA  . ASN B 2 8   ? 17.751 14.592  0.459   1.00 29.53  ? 262 ASN P CA  1 
ATOM   1929 C  C   . ASN B 2 8   ? 16.766 15.114  -0.592  1.00 35.29  ? 262 ASN P C   1 
ATOM   1930 O  O   . ASN B 2 8   ? 15.614 14.720  -0.609  1.00 37.59  ? 262 ASN P O   1 
ATOM   1931 C  CB  . ASN B 2 8   ? 18.402 13.287  -0.064  1.00 31.37  ? 262 ASN P CB  1 
ATOM   1932 C  CG  . ASN B 2 8   ? 19.625 12.856  0.752   1.00 30.75  ? 262 ASN P CG  1 
ATOM   1933 O  OD1 . ASN B 2 8   ? 19.744 11.718  1.187   1.00 38.75  ? 262 ASN P OD1 1 
ATOM   1934 N  ND2 . ASN B 2 8   ? 20.530 13.760  1.043   1.00 24.79  ? 262 ASN P ND2 1 
ATOM   1935 N  N   . VAL B 2 9   ? 17.196 16.024  -1.472  1.00 36.76  ? 263 VAL P N   1 
ATOM   1936 C  CA  . VAL B 2 9   ? 16.370 16.408  -2.604  1.00 44.66  ? 263 VAL P CA  1 
ATOM   1937 C  C   . VAL B 2 9   ? 16.532 15.341  -3.676  1.00 46.29  ? 263 VAL P C   1 
ATOM   1938 O  O   . VAL B 2 9   ? 17.329 15.512  -4.599  1.00 50.70  ? 263 VAL P O   1 
ATOM   1939 C  CB  . VAL B 2 9   ? 16.674 17.806  -3.197  1.00 51.18  ? 263 VAL P CB  1 
ATOM   1940 C  CG1 . VAL B 2 9   ? 15.596 18.204  -4.205  1.00 51.93  ? 263 VAL P CG1 1 
ATOM   1941 C  CG2 . VAL B 2 9   ? 16.801 18.864  -2.119  1.00 53.20  ? 263 VAL P CG2 1 
HETATM 1942 CL CL  . CL  C 3 .   ? 35.179 -6.289  13.595  1.00 20.49  ? 301 CL  A CL  1 
HETATM 1943 MG MG  . MG  D 4 .   ? 35.002 4.254   19.474  1.00 31.22  2 302 MG  A MG  1 
HETATM 1944 MG MG  . MG  E 4 .   ? 22.039 -18.396 30.676  1.00 33.48  2 303 MG  A MG  1 
HETATM 1945 MG MG  . MG  F 4 .   ? 40.937 21.008  -15.748 0.50 14.32  2 304 MG  A MG  1 
HETATM 1946 O  O1  . WQ9 G 5 .   ? 23.029 25.586  -2.083  1.00 28.79  ? 305 WQ9 A O1  1 
HETATM 1947 C  C1  . WQ9 G 5 .   ? 21.916 25.281  -2.507  1.00 28.46  ? 305 WQ9 A C1  1 
HETATM 1948 C  C2  . WQ9 G 5 .   ? 21.187 26.259  -3.404  1.00 27.92  ? 305 WQ9 A C2  1 
HETATM 1949 N  N1  . WQ9 G 5 .   ? 21.332 24.095  -2.229  1.00 28.64  ? 305 WQ9 A N1  1 
HETATM 1950 C  C3  . WQ9 G 5 .   ? 19.998 23.570  -2.593  1.00 30.33  ? 305 WQ9 A C3  1 
HETATM 1951 C  C4  . WQ9 G 5 .   ? 19.996 22.136  -2.074  1.00 31.60  ? 305 WQ9 A C4  1 
HETATM 1952 C  C5  . WQ9 G 5 .   ? 20.966 22.187  -0.876  1.00 30.17  ? 305 WQ9 A C5  1 
HETATM 1953 C  C6  . WQ9 G 5 .   ? 21.554 20.796  -0.554  1.00 30.85  ? 305 WQ9 A C6  1 
HETATM 1954 C  C7  . WQ9 G 5 .   ? 21.015 20.367  0.778   1.00 29.81  ? 305 WQ9 A C7  1 
HETATM 1955 N  N2  . WQ9 G 5 .   ? 20.266 21.549  1.260   1.00 33.31  ? 305 WQ9 A N2  1 
HETATM 1956 S  S1  . WQ9 G 5 .   ? 19.545 21.512  2.716   1.00 39.44  ? 305 WQ9 A S1  1 
HETATM 1957 O  O2  . WQ9 G 5 .   ? 19.492 22.860  3.208   1.00 42.47  ? 305 WQ9 A O2  1 
HETATM 1958 O  O3  . WQ9 G 5 .   ? 20.151 20.468  3.493   1.00 40.19  ? 305 WQ9 A O3  1 
HETATM 1959 C  C8  . WQ9 G 5 .   ? 17.941 21.023  2.199   1.00 44.81  ? 305 WQ9 A C8  1 
HETATM 1960 C  C9  . WQ9 G 5 .   ? 17.719 19.679  1.946   1.00 48.86  ? 305 WQ9 A C9  1 
HETATM 1961 C  C10 . WQ9 G 5 .   ? 16.493 19.257  1.482   1.00 53.82  ? 305 WQ9 A C10 1 
HETATM 1962 C  C11 . WQ9 G 5 .   ? 15.506 20.178  1.200   1.00 65.58  ? 305 WQ9 A C11 1 
HETATM 1963 BR BR1 . WQ9 G 5 .   ? 13.834 19.554  0.552   1.00 104.51 ? 305 WQ9 A BR1 1 
HETATM 1964 C  C12 . WQ9 G 5 .   ? 15.772 21.526  1.394   1.00 60.27  ? 305 WQ9 A C12 1 
HETATM 1965 F  F1  . WQ9 G 5 .   ? 14.818 22.443  1.117   1.00 65.63  ? 305 WQ9 A F1  1 
HETATM 1966 C  C13 . WQ9 G 5 .   ? 16.990 21.976  1.868   1.00 53.27  ? 305 WQ9 A C13 1 
HETATM 1967 C  C14 . WQ9 G 5 .   ? 20.335 22.764  0.413   1.00 28.97  ? 305 WQ9 A C14 1 
HETATM 1968 C  C15 . WQ9 G 5 .   ? 22.074 23.082  -1.457  1.00 28.36  ? 305 WQ9 A C15 1 
HETATM 1969 MG MG  . MG  H 4 .   ? 33.647 33.319  -2.469  1.00 18.64  2 306 MG  A MG  1 
HETATM 1970 O  O   . HOH I 6 .   ? 38.594 10.103  11.686  1.00 45.17  ? 401 HOH A O   1 
HETATM 1971 O  O   . HOH I 6 .   ? 37.864 -2.853  18.639  1.00 32.91  ? 402 HOH A O   1 
HETATM 1972 O  O   . HOH I 6 .   ? 1.919  13.823  19.950  1.00 31.88  ? 403 HOH A O   1 
HETATM 1973 O  O   . HOH I 6 .   ? 31.467 2.342   6.466   1.00 25.70  ? 404 HOH A O   1 
HETATM 1974 O  O   . HOH I 6 .   ? 34.031 0.963   22.820  1.00 41.25  ? 405 HOH A O   1 
HETATM 1975 O  O   . HOH I 6 .   ? 5.046  31.300  17.218  1.00 34.46  ? 406 HOH A O   1 
HETATM 1976 O  O   . HOH I 6 .   ? 23.297 12.198  -15.376 1.00 33.49  ? 407 HOH A O   1 
HETATM 1977 O  O   . HOH I 6 .   ? 38.549 -7.168  21.621  1.00 24.49  ? 408 HOH A O   1 
HETATM 1978 O  O   . HOH I 6 .   ? 40.088 16.927  1.634   1.00 36.81  ? 409 HOH A O   1 
HETATM 1979 O  O   . HOH I 6 .   ? 17.424 30.768  22.038  1.00 21.69  ? 410 HOH A O   1 
HETATM 1980 O  O   . HOH I 6 .   ? 30.385 36.658  -2.358  1.00 38.23  ? 411 HOH A O   1 
HETATM 1981 O  O   . HOH I 6 .   ? 34.214 5.129   21.092  1.00 41.00  ? 412 HOH A O   1 
HETATM 1982 O  O   . HOH I 6 .   ? 25.228 15.702  3.770   1.00 22.68  ? 413 HOH A O   1 
HETATM 1983 O  O   . HOH I 6 .   ? 30.060 -3.667  25.100  1.00 34.31  ? 414 HOH A O   1 
HETATM 1984 O  O   . HOH I 6 .   ? 41.526 14.961  -5.184  1.00 27.73  ? 415 HOH A O   1 
HETATM 1985 O  O   . HOH I 6 .   ? 27.178 23.143  24.050  1.00 31.09  ? 416 HOH A O   1 
HETATM 1986 O  O   . HOH I 6 .   ? 36.813 -3.015  16.275  1.00 21.22  ? 417 HOH A O   1 
HETATM 1987 O  O   . HOH I 6 .   ? 28.597 21.735  -12.841 1.00 22.49  ? 418 HOH A O   1 
HETATM 1988 O  O   . HOH I 6 .   ? 7.247  36.016  8.399   1.00 24.27  ? 419 HOH A O   1 
HETATM 1989 O  O   . HOH I 6 .   ? 26.898 3.725   4.208   1.00 23.13  ? 420 HOH A O   1 
HETATM 1990 O  O   . HOH I 6 .   ? 24.092 -12.023 24.933  1.00 41.04  ? 421 HOH A O   1 
HETATM 1991 O  O   . HOH I 6 .   ? 35.559 24.616  9.422   1.00 26.08  ? 422 HOH A O   1 
HETATM 1992 O  O   . HOH I 6 .   ? 42.154 20.415  -17.847 1.00 19.59  ? 423 HOH A O   1 
HETATM 1993 O  O   . HOH I 6 .   ? 26.766 1.084   21.880  1.00 29.91  ? 424 HOH A O   1 
HETATM 1994 O  O   . HOH I 6 .   ? 38.654 20.187  -20.042 1.00 29.08  ? 425 HOH A O   1 
HETATM 1995 O  O   . HOH I 6 .   ? 22.754 2.158   -2.708  1.00 33.44  ? 426 HOH A O   1 
HETATM 1996 O  O   . HOH I 6 .   ? 31.441 27.070  -2.534  1.00 18.16  ? 427 HOH A O   1 
HETATM 1997 O  O   . HOH I 6 .   ? 35.564 6.098   7.071   1.00 24.02  ? 428 HOH A O   1 
HETATM 1998 O  O   . HOH I 6 .   ? 4.798  13.213  13.934  1.00 41.01  ? 429 HOH A O   1 
HETATM 1999 O  O   . HOH I 6 .   ? 23.158 16.403  26.095  1.00 30.65  ? 430 HOH A O   1 
HETATM 2000 O  O   . HOH I 6 .   ? 22.668 0.591   7.110   1.00 31.46  ? 431 HOH A O   1 
HETATM 2001 O  O   . HOH I 6 .   ? 34.787 -14.882 21.622  1.00 24.55  ? 432 HOH A O   1 
HETATM 2002 O  O   . HOH I 6 .   ? 23.548 13.636  23.811  1.00 29.78  ? 433 HOH A O   1 
HETATM 2003 O  O   . HOH I 6 .   ? 32.948 26.864  -9.699  1.00 28.46  ? 434 HOH A O   1 
HETATM 2004 O  O   . HOH I 6 .   ? 30.612 29.596  -2.814  1.00 29.04  ? 435 HOH A O   1 
HETATM 2005 O  O   . HOH I 6 .   ? 20.220 6.707   8.883   1.00 34.15  ? 436 HOH A O   1 
HETATM 2006 O  O   . HOH I 6 .   ? 18.107 23.563  27.649  1.00 29.88  ? 437 HOH A O   1 
HETATM 2007 O  O   . HOH I 6 .   ? 23.007 7.963   19.779  1.00 33.75  ? 438 HOH A O   1 
HETATM 2008 O  O   . HOH I 6 .   ? 35.968 21.354  12.036  1.00 29.39  ? 439 HOH A O   1 
HETATM 2009 O  O   . HOH I 6 .   ? 13.078 10.841  19.904  1.00 39.05  ? 440 HOH A O   1 
HETATM 2010 O  O   . HOH I 6 .   ? 28.447 -7.006  23.876  1.00 39.04  ? 441 HOH A O   1 
HETATM 2011 O  O   . HOH I 6 .   ? 39.184 21.653  -15.473 1.00 44.59  ? 442 HOH A O   1 
HETATM 2012 O  O   . HOH I 6 .   ? 8.915  13.574  12.929  1.00 30.02  ? 443 HOH A O   1 
HETATM 2013 O  O   . HOH I 6 .   ? 30.043 4.877   21.156  1.00 18.53  ? 444 HOH A O   1 
HETATM 2014 O  O   . HOH I 6 .   ? 19.441 17.441  -0.915  1.00 27.97  ? 445 HOH A O   1 
HETATM 2015 O  O   . HOH I 6 .   ? 11.158 31.084  19.699  1.00 26.29  ? 446 HOH A O   1 
HETATM 2016 O  O   . HOH I 6 .   ? 14.813 15.772  24.544  1.00 33.53  ? 447 HOH A O   1 
HETATM 2017 O  O   . HOH I 6 .   ? 35.471 4.997   17.655  1.00 29.65  ? 448 HOH A O   1 
HETATM 2018 O  O   . HOH I 6 .   ? 36.759 23.866  -3.329  1.00 22.56  ? 449 HOH A O   1 
HETATM 2019 O  O   . HOH I 6 .   ? 26.034 9.176   14.024  1.00 13.22  ? 450 HOH A O   1 
HETATM 2020 O  O   . HOH I 6 .   ? 42.364 22.558  -3.844  1.00 17.42  ? 451 HOH A O   1 
HETATM 2021 O  O   . HOH I 6 .   ? 27.065 17.589  -15.423 1.00 22.43  ? 452 HOH A O   1 
HETATM 2022 O  O   . HOH I 6 .   ? 25.944 23.901  -11.497 1.00 28.76  ? 453 HOH A O   1 
HETATM 2023 O  O   . HOH I 6 .   ? 12.235 32.032  11.437  1.00 17.31  ? 454 HOH A O   1 
HETATM 2024 O  O   . HOH I 6 .   ? 41.294 23.403  -10.296 1.00 25.95  ? 455 HOH A O   1 
HETATM 2025 O  O   . HOH I 6 .   ? 22.651 7.576   15.576  1.00 26.99  ? 456 HOH A O   1 
HETATM 2026 O  O   . HOH I 6 .   ? 36.010 22.863  -7.168  1.00 16.19  ? 457 HOH A O   1 
HETATM 2027 O  O   . HOH I 6 .   ? 21.171 0.796   -8.911  1.00 29.71  ? 458 HOH A O   1 
HETATM 2028 O  O   . HOH I 6 .   ? 35.599 16.829  -18.905 1.00 21.22  ? 459 HOH A O   1 
HETATM 2029 O  O   . HOH I 6 .   ? 18.929 1.529   12.470  1.00 22.45  ? 460 HOH A O   1 
HETATM 2030 O  O   . HOH I 6 .   ? 40.977 20.149  7.004   1.00 33.04  ? 461 HOH A O   1 
HETATM 2031 O  O   . HOH I 6 .   ? 32.741 7.420   21.060  1.00 30.59  ? 462 HOH A O   1 
HETATM 2032 O  O   . HOH I 6 .   ? 22.024 17.423  -10.235 1.00 29.96  ? 463 HOH A O   1 
HETATM 2033 O  O   . HOH I 6 .   ? 33.956 22.646  21.080  1.00 29.96  ? 464 HOH A O   1 
HETATM 2034 O  O   . HOH I 6 .   ? 33.581 27.855  -1.032  1.00 17.84  ? 465 HOH A O   1 
HETATM 2035 O  O   . HOH I 6 .   ? 41.100 10.117  -11.451 1.00 31.84  ? 466 HOH A O   1 
HETATM 2036 O  O   . HOH I 6 .   ? 20.782 37.457  12.926  1.00 30.68  ? 467 HOH A O   1 
HETATM 2037 O  O   . HOH I 6 .   ? 25.659 20.736  -12.053 1.00 40.21  ? 468 HOH A O   1 
HETATM 2038 O  O   . HOH I 6 .   ? 13.688 30.429  13.109  1.00 19.22  ? 469 HOH A O   1 
HETATM 2039 O  O   . HOH I 6 .   ? 11.437 20.365  14.229  1.00 23.62  ? 470 HOH A O   1 
HETATM 2040 O  O   . HOH I 6 .   ? 21.738 12.349  -11.011 1.00 28.48  ? 471 HOH A O   1 
HETATM 2041 O  O   . HOH I 6 .   ? 37.901 7.167   12.215  1.00 26.90  ? 472 HOH A O   1 
HETATM 2042 O  O   . HOH I 6 .   ? 20.444 1.993   18.992  1.00 30.64  ? 473 HOH A O   1 
HETATM 2043 O  O   . HOH I 6 .   ? 33.340 7.627   -0.761  1.00 19.79  ? 474 HOH A O   1 
HETATM 2044 O  O   . HOH I 6 .   ? 20.187 23.688  23.662  1.00 23.52  ? 475 HOH A O   1 
HETATM 2045 O  O   . HOH I 6 .   ? 37.811 11.095  -3.722  1.00 18.63  ? 476 HOH A O   1 
HETATM 2046 O  O   . HOH I 6 .   ? 14.187 31.604  15.536  1.00 26.39  ? 477 HOH A O   1 
HETATM 2047 O  O   . HOH I 6 .   ? 28.511 20.862  25.445  1.00 25.56  ? 478 HOH A O   1 
HETATM 2048 O  O   . HOH I 6 .   ? 33.637 34.226  -4.594  1.00 27.42  ? 479 HOH A O   1 
HETATM 2049 O  O   . HOH I 6 .   ? 40.802 16.728  -7.143  1.00 17.89  ? 480 HOH A O   1 
HETATM 2050 O  O   . HOH I 6 .   ? 20.527 13.732  15.715  1.00 16.84  ? 481 HOH A O   1 
HETATM 2051 O  O   . HOH I 6 .   ? 24.547 18.593  3.963   1.00 31.99  ? 482 HOH A O   1 
HETATM 2052 O  O   . HOH I 6 .   ? 36.609 0.738   10.858  1.00 27.52  ? 483 HOH A O   1 
HETATM 2053 O  O   . HOH I 6 .   ? 29.833 18.431  -15.657 1.00 21.92  ? 484 HOH A O   1 
HETATM 2054 O  O   . HOH I 6 .   ? 38.398 16.824  9.955   1.00 32.09  ? 485 HOH A O   1 
HETATM 2055 O  O   . HOH I 6 .   ? 21.550 6.080   3.626   1.00 39.62  ? 486 HOH A O   1 
HETATM 2056 O  O   . HOH I 6 .   ? 18.827 15.140  24.010  1.00 23.93  ? 487 HOH A O   1 
HETATM 2057 O  O   . HOH I 6 .   ? 38.707 15.805  3.983   1.00 24.53  ? 488 HOH A O   1 
HETATM 2058 O  O   . HOH I 6 .   ? 34.852 10.033  0.458   1.00 22.99  ? 489 HOH A O   1 
HETATM 2059 O  O   . HOH I 6 .   ? 26.552 11.851  -18.364 1.00 32.79  ? 490 HOH A O   1 
HETATM 2060 O  O   . HOH I 6 .   ? 35.521 34.184  -2.282  1.00 30.26  ? 491 HOH A O   1 
HETATM 2061 O  O   . HOH I 6 .   ? 32.026 24.705  15.250  1.00 23.72  ? 492 HOH A O   1 
HETATM 2062 O  O   . HOH I 6 .   ? 25.494 32.382  -4.853  1.00 25.19  ? 493 HOH A O   1 
HETATM 2063 O  O   . HOH I 6 .   ? 29.654 -10.422 21.421  1.00 26.43  ? 494 HOH A O   1 
HETATM 2064 O  O   . HOH I 6 .   ? 19.282 -4.161  16.767  1.00 29.99  ? 495 HOH A O   1 
HETATM 2065 O  O   . HOH I 6 .   ? 11.878 32.028  -0.086  1.00 24.11  ? 496 HOH A O   1 
HETATM 2066 O  O   . HOH I 6 .   ? 2.472  22.000  -0.580  1.00 40.22  ? 497 HOH A O   1 
HETATM 2067 O  O   . HOH I 6 .   ? 2.434  33.632  11.517  1.00 28.50  ? 498 HOH A O   1 
HETATM 2068 O  O   . HOH I 6 .   ? 11.091 29.155  -1.171  1.00 24.62  ? 499 HOH A O   1 
HETATM 2069 O  O   . HOH I 6 .   ? 28.534 30.538  16.887  1.00 33.84  ? 500 HOH A O   1 
HETATM 2070 O  O   . HOH I 6 .   ? 25.850 12.831  -15.814 1.00 19.99  ? 501 HOH A O   1 
HETATM 2071 O  O   . HOH I 6 .   ? 6.827  30.555  19.177  1.00 31.41  ? 502 HOH A O   1 
HETATM 2072 O  O   . HOH I 6 .   ? 12.962 36.621  10.563  1.00 43.50  ? 503 HOH A O   1 
HETATM 2073 O  O   . HOH I 6 .   ? 15.774 9.249   20.658  1.00 47.89  ? 504 HOH A O   1 
HETATM 2074 O  O   . HOH I 6 .   ? 34.921 22.021  9.597   1.00 21.01  ? 505 HOH A O   1 
HETATM 2075 O  O   . HOH I 6 .   ? 43.576 17.970  -9.398  1.00 22.13  ? 506 HOH A O   1 
HETATM 2076 O  O   . HOH I 6 .   ? 18.100 27.871  19.185  1.00 28.37  ? 507 HOH A O   1 
HETATM 2077 O  O   . HOH I 6 .   ? 26.453 7.737   22.197  1.00 33.96  ? 508 HOH A O   1 
HETATM 2078 O  O   . HOH I 6 .   ? 35.927 29.488  -7.466  1.00 29.47  ? 509 HOH A O   1 
HETATM 2079 O  O   . HOH I 6 .   ? 38.803 10.699  7.563   1.00 37.22  ? 510 HOH A O   1 
HETATM 2080 O  O   . HOH I 6 .   ? 2.003  38.040  6.771   1.00 21.42  ? 511 HOH A O   1 
HETATM 2081 O  O   . HOH I 6 .   ? 19.286 10.510  -4.859  1.00 37.44  ? 512 HOH A O   1 
HETATM 2082 O  O   . HOH I 6 .   ? 37.167 26.815  5.425   1.00 19.38  ? 513 HOH A O   1 
HETATM 2083 O  O   . HOH I 6 .   ? 34.123 27.629  10.437  1.00 44.24  ? 514 HOH A O   1 
HETATM 2084 O  O   . HOH I 6 .   ? 10.994 30.802  9.328   1.00 17.97  ? 515 HOH A O   1 
HETATM 2085 O  O   . HOH I 6 .   ? 17.469 29.113  10.252  1.00 28.34  ? 516 HOH A O   1 
HETATM 2086 O  O   . HOH I 6 .   ? 32.467 10.775  17.957  1.00 16.92  ? 517 HOH A O   1 
HETATM 2087 O  O   . HOH I 6 .   ? 33.025 21.847  -13.655 1.00 23.70  ? 518 HOH A O   1 
HETATM 2088 O  O   . HOH I 6 .   ? 15.423 30.705  10.966  1.00 27.18  ? 519 HOH A O   1 
HETATM 2089 O  O   . HOH I 6 .   ? 20.772 17.702  5.375   1.00 35.09  ? 520 HOH A O   1 
HETATM 2090 O  O   . HOH I 6 .   ? 18.101 5.555   -12.268 1.00 42.93  ? 521 HOH A O   1 
HETATM 2091 O  O   . HOH I 6 .   ? 23.761 28.678  20.611  1.00 24.48  ? 522 HOH A O   1 
HETATM 2092 O  O   . HOH I 6 .   ? 36.216 8.826   4.839   1.00 41.73  ? 523 HOH A O   1 
HETATM 2093 O  O   . HOH I 6 .   ? 22.764 33.880  -1.237  1.00 26.56  ? 524 HOH A O   1 
HETATM 2094 O  O   . HOH I 6 .   ? 8.094  20.685  29.541  1.00 34.84  ? 525 HOH A O   1 
HETATM 2095 O  O   . HOH I 6 .   ? 8.969  25.337  24.355  1.00 29.68  ? 526 HOH A O   1 
HETATM 2096 O  O   . HOH I 6 .   ? 19.234 10.260  -2.077  1.00 30.12  ? 527 HOH A O   1 
HETATM 2097 O  O   . HOH I 6 .   ? 37.935 24.740  -0.996  1.00 31.69  ? 528 HOH A O   1 
HETATM 2098 O  O   . HOH I 6 .   ? 6.469  28.554  -9.988  1.00 35.32  ? 529 HOH A O   1 
HETATM 2099 O  O   . HOH I 6 .   ? 32.177 4.533   22.568  1.00 41.90  ? 530 HOH A O   1 
HETATM 2100 O  O   . HOH I 6 .   ? 37.416 16.354  12.765  1.00 44.90  ? 531 HOH A O   1 
HETATM 2101 O  O   . HOH I 6 .   ? 40.658 19.391  2.313   1.00 31.26  ? 532 HOH A O   1 
HETATM 2102 O  O   . HOH I 6 .   ? 30.788 -7.489  22.908  1.00 23.40  ? 533 HOH A O   1 
HETATM 2103 O  O   . HOH I 6 .   ? 18.487 7.570   -1.057  1.00 60.73  ? 534 HOH A O   1 
HETATM 2104 O  O   . HOH I 6 .   ? 40.798 12.323  -4.815  1.00 34.48  ? 535 HOH A O   1 
HETATM 2105 O  O   . HOH I 6 .   ? 22.964 16.653  6.224   1.00 30.98  ? 536 HOH A O   1 
HETATM 2106 O  O   . HOH I 6 .   ? 26.816 -1.415  -5.823  1.00 20.37  ? 537 HOH A O   1 
HETATM 2107 O  O   . HOH I 6 .   ? 36.668 20.499  -16.025 1.00 19.18  ? 538 HOH A O   1 
HETATM 2108 O  O   . HOH I 6 .   ? 22.209 10.679  7.080   1.00 22.69  ? 539 HOH A O   1 
HETATM 2109 O  O   . HOH I 6 .   ? 22.072 26.897  21.708  1.00 26.70  ? 540 HOH A O   1 
HETATM 2110 O  O   . HOH I 6 .   ? 9.216  32.680  -5.562  1.00 29.52  ? 541 HOH A O   1 
HETATM 2111 O  O   . HOH I 6 .   ? 34.411 2.692   20.879  1.00 46.61  ? 542 HOH A O   1 
HETATM 2112 O  O   . HOH I 6 .   ? 17.691 9.615   12.110  1.00 25.77  ? 543 HOH A O   1 
HETATM 2113 O  O   . HOH I 6 .   ? 22.022 18.367  -7.601  1.00 28.94  ? 544 HOH A O   1 
HETATM 2114 O  O   . HOH I 6 .   ? 23.673 -16.052 20.602  1.00 45.52  ? 545 HOH A O   1 
HETATM 2115 O  O   . HOH I 6 .   ? 39.923 26.501  -2.319  1.00 30.49  ? 546 HOH A O   1 
HETATM 2116 O  O   . HOH I 6 .   ? 23.673 21.575  4.704   1.00 25.87  ? 547 HOH A O   1 
HETATM 2117 O  O   . HOH I 6 .   ? 35.276 19.329  18.883  1.00 39.57  ? 548 HOH A O   1 
HETATM 2118 O  O   . HOH I 6 .   ? 24.248 0.372   -5.861  1.00 37.02  ? 549 HOH A O   1 
HETATM 2119 O  O   . HOH I 6 .   ? 29.147 3.231   -4.539  1.00 15.09  ? 550 HOH A O   1 
HETATM 2120 O  O   . HOH I 6 .   ? -0.291 22.118  10.651  1.00 53.34  ? 551 HOH A O   1 
HETATM 2121 O  O   . HOH I 6 .   ? 17.907 4.020   12.031  1.00 30.69  ? 552 HOH A O   1 
HETATM 2122 O  O   . HOH I 6 .   ? 36.264 11.994  15.271  1.00 39.59  ? 553 HOH A O   1 
HETATM 2123 O  O   . HOH I 6 .   ? 15.825 7.774   12.153  1.00 41.10  ? 554 HOH A O   1 
HETATM 2124 O  O   . HOH I 6 .   ? 34.128 11.694  23.115  1.00 38.38  ? 555 HOH A O   1 
HETATM 2125 O  O   . HOH I 6 .   ? 35.850 -7.749  25.787  1.00 35.67  ? 556 HOH A O   1 
HETATM 2126 O  O   . HOH I 6 .   ? 4.078  24.866  24.969  1.00 38.76  ? 557 HOH A O   1 
HETATM 2127 O  O   . HOH I 6 .   ? 31.812 26.880  13.506  1.00 34.19  ? 558 HOH A O   1 
HETATM 2128 O  O   . HOH I 6 .   ? 26.988 35.930  4.279   1.00 41.81  ? 559 HOH A O   1 
HETATM 2129 O  O   . HOH I 6 .   ? 32.852 -16.844 19.469  1.00 40.58  ? 560 HOH A O   1 
HETATM 2130 O  O   . HOH I 6 .   ? 2.274  21.943  7.368   1.00 41.18  ? 561 HOH A O   1 
HETATM 2131 O  O   . HOH I 6 .   ? 27.183 2.790   -2.182  1.00 41.30  ? 562 HOH A O   1 
HETATM 2132 O  O   . HOH I 6 .   ? 0.073  32.234  1.849   1.00 26.10  ? 563 HOH A O   1 
HETATM 2133 O  O   . HOH I 6 .   ? 37.645 -0.132  15.230  1.00 38.18  ? 564 HOH A O   1 
HETATM 2134 O  O   . HOH I 6 .   ? 32.651 -6.533  25.200  1.00 34.48  ? 565 HOH A O   1 
HETATM 2135 O  O   . HOH I 6 .   ? 34.612 23.934  15.972  1.00 44.77  ? 566 HOH A O   1 
HETATM 2136 O  O   . HOH I 6 .   ? 38.136 1.285   17.526  1.00 38.44  ? 567 HOH A O   1 
HETATM 2137 O  O   . HOH I 6 .   ? 36.909 -6.691  11.040  1.00 23.41  ? 568 HOH A O   1 
HETATM 2138 O  O   . HOH I 6 .   ? 35.615 2.536   18.264  1.00 40.98  ? 569 HOH A O   1 
HETATM 2139 O  O   . HOH I 6 .   ? 33.882 10.381  20.168  1.00 29.82  ? 570 HOH A O   1 
HETATM 2140 O  O   . HOH I 6 .   ? 34.055 35.157  2.806   1.00 49.39  ? 571 HOH A O   1 
HETATM 2141 O  O   . HOH I 6 .   ? 18.066 0.396   15.034  1.00 31.81  ? 572 HOH A O   1 
HETATM 2142 O  O   . HOH I 6 .   ? 46.354 14.528  -6.940  1.00 34.22  ? 573 HOH A O   1 
HETATM 2143 O  O   . HOH I 6 .   ? 16.629 11.759  5.474   1.00 37.19  ? 574 HOH A O   1 
HETATM 2144 O  O   . HOH I 6 .   ? 7.292  26.723  22.604  1.00 34.25  ? 575 HOH A O   1 
HETATM 2145 O  O   . HOH I 6 .   ? 37.224 27.946  7.865   1.00 43.25  ? 576 HOH A O   1 
HETATM 2146 O  O   . HOH I 6 .   ? 40.045 12.733  7.023   1.00 44.59  ? 577 HOH A O   1 
HETATM 2147 O  O   . HOH I 6 .   ? 25.078 6.612   14.726  1.00 20.10  ? 578 HOH A O   1 
HETATM 2148 O  O   . HOH I 6 .   ? 36.360 19.523  -18.609 1.00 33.13  ? 579 HOH A O   1 
HETATM 2149 O  O   . HOH I 6 .   ? 19.712 21.489  -6.123  1.00 36.06  ? 580 HOH A O   1 
HETATM 2150 O  O   . HOH I 6 .   ? 35.976 26.871  -2.175  1.00 29.17  ? 581 HOH A O   1 
HETATM 2151 O  O   . HOH I 6 .   ? 37.939 2.844   9.737   1.00 30.19  ? 582 HOH A O   1 
HETATM 2152 O  O   . HOH I 6 .   ? 21.506 30.164  -6.701  1.00 29.34  ? 583 HOH A O   1 
HETATM 2153 O  O   . HOH I 6 .   ? 18.085 12.385  15.705  1.00 25.49  ? 584 HOH A O   1 
HETATM 2154 O  O   . HOH I 6 .   ? 32.546 4.981   3.069   1.00 33.01  ? 585 HOH A O   1 
HETATM 2155 O  O   . HOH I 6 .   ? 37.629 -4.706  14.337  1.00 28.36  ? 586 HOH A O   1 
HETATM 2156 O  O   . HOH I 6 .   ? 34.721 12.291  17.207  1.00 29.55  ? 587 HOH A O   1 
HETATM 2157 O  O   . HOH I 6 .   ? 34.505 9.225   3.071   1.00 29.74  ? 588 HOH A O   1 
HETATM 2158 O  O   . HOH I 6 .   ? 13.283 30.783  18.258  1.00 36.27  ? 589 HOH A O   1 
HETATM 2159 O  O   . HOH I 6 .   ? 34.881 22.790  -15.416 1.00 26.72  ? 590 HOH A O   1 
HETATM 2160 O  O   . HOH I 6 .   ? 25.864 15.608  -16.625 1.00 25.55  ? 591 HOH A O   1 
HETATM 2161 O  O   . HOH I 6 .   ? 26.997 20.249  29.596  1.00 35.18  ? 592 HOH A O   1 
HETATM 2162 O  O   . HOH I 6 .   ? 30.586 20.937  -14.573 1.00 23.27  ? 593 HOH A O   1 
HETATM 2163 O  O   . HOH I 6 .   ? 28.225 3.435   22.654  1.00 28.17  ? 594 HOH A O   1 
HETATM 2164 O  O   . HOH I 6 .   ? 38.963 8.649   -4.335  1.00 34.53  ? 595 HOH A O   1 
HETATM 2165 O  O   . HOH I 6 .   ? 18.076 29.876  17.325  1.00 36.97  ? 596 HOH A O   1 
HETATM 2166 O  O   . HOH I 6 .   ? 38.296 -0.335  12.612  1.00 39.95  ? 597 HOH A O   1 
HETATM 2167 O  O   . HOH I 6 .   ? 42.541 22.436  -19.702 1.00 22.62  ? 598 HOH A O   1 
HETATM 2168 O  O   . HOH I 6 .   ? 9.129  19.579  26.740  1.00 41.78  ? 599 HOH A O   1 
HETATM 2169 O  O   . HOH I 6 .   ? 30.033 22.255  27.579  1.00 29.37  ? 600 HOH A O   1 
HETATM 2170 O  O   . HOH I 6 .   ? 17.628 -2.283  15.597  1.00 40.97  ? 601 HOH A O   1 
HETATM 2171 O  O   . HOH I 6 .   ? 26.895 19.051  26.894  1.00 26.70  ? 602 HOH A O   1 
HETATM 2172 O  O   . HOH I 6 .   ? 26.384 5.345   23.199  1.00 35.79  ? 603 HOH A O   1 
HETATM 2173 O  O   . HOH I 6 .   ? 32.686 7.342   1.862   1.00 28.89  ? 604 HOH A O   1 
HETATM 2174 O  O   . HOH I 6 .   ? 1.755  24.464  5.123   1.00 38.64  ? 605 HOH A O   1 
HETATM 2175 O  O   . HOH I 6 .   ? 40.390 3.246   10.782  1.00 38.18  ? 606 HOH A O   1 
HETATM 2176 O  O   . HOH J 6 .   ? 12.247 5.459   18.786  1.00 44.69  ? 301 HOH P O   1 
HETATM 2177 O  O   . HOH J 6 .   ? 14.691 13.046  6.996   1.00 30.23  ? 302 HOH P O   1 
HETATM 2178 O  O   . HOH J 6 .   ? 17.645 10.641  9.455   1.00 26.33  ? 303 HOH P O   1 
HETATM 2179 O  O   . HOH J 6 .   ? 20.528 4.697   18.990  1.00 38.89  ? 304 HOH P O   1 
HETATM 2180 O  O   . HOH J 6 .   ? 21.017 16.414  1.141   1.00 20.53  ? 305 HOH P O   1 
HETATM 2181 O  O   . HOH J 6 .   ? 17.243 12.181  12.937  1.00 22.36  ? 306 HOH P O   1 
HETATM 2182 O  O   . HOH J 6 .   ? 19.641 16.357  7.516   1.00 20.55  ? 307 HOH P O   1 
HETATM 2183 O  O   . HOH J 6 .   ? 8.626  13.182  9.188   1.00 37.92  ? 308 HOH P O   1 
HETATM 2184 O  O   . HOH J 6 .   ? 19.678 17.171  3.402   1.00 29.27  ? 309 HOH P O   1 
HETATM 2185 O  O   . HOH J 6 .   ? 6.825  11.826  13.118  1.00 46.67  ? 310 HOH P O   1 
HETATM 2186 O  O   . HOH J 6 .   ? 19.644 10.562  16.900  1.00 35.02  ? 311 HOH P O   1 
HETATM 2187 O  O   . HOH J 6 .   ? 15.369 12.021  9.602   1.00 25.42  ? 312 HOH P O   1 
HETATM 2188 O  O   . HOH J 6 .   ? 21.876 7.310   18.022  1.00 41.03  ? 313 HOH P O   1 
# 
